data_9GBO
# 
_entry.id   9GBO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9GBO         pdb_00009gbo 10.2210/pdb9gbo/pdb 
WWPDB D_1292140333 ?            ?                   
# 
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 2025-01-22 ? 
2 'Structure model' 1 1 2025-03-19 ? 
# 
_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' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GBO 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              bsskra@bath.ac.uk 
_pdbx_contact_author.name_first         K.Ravi 
_pdbx_contact_author.name_last          Acharya 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3009-4058 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gregory, K.S.' 1 ? 
'Cozier, G.E.'  2 ? 
'Acharya, K.R.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            292 
_citation.language                  ? 
_citation.page_first                1141 
_citation.page_last                 1158 
_citation.title                     
'Molecular basis of human angiotensin-1 converting enzyme inhibition by a series of diprolyl-derived compounds.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.17384 
_citation.pdbx_database_id_PubMed   39763019 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gregory, K.S.'  1 ? 
primary 'Cozier, G.E.'   2 ? 
primary 'Fienberg, S.'   3 ? 
primary 'Chibale, K.'    4 ? 
primary 'Sturrock, E.D.' 5 ? 
primary 'Acharya, K.R.'  6 ? 
# 
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 'Angiotensin-converting enzyme' 68861.875 1   3.2.1.-,3.4.15.1 ? ? ? 
2 branched    man 
;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose
;
1463.349  1   ?                ? ? ? 
3 non-polymer syn 'ZINC ION' 65.409    1   ?                ? ? ? 
4 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   1   ?                ? ? ? 
5 non-polymer syn 'CHLORIDE ION' 35.453    2   ?                ? ? ? 
6 non-polymer syn 
;(2~{S})-1-[(2~{S})-2-[[(1~{S})-1-[(2~{S})-1-[(2~{S})-2-azanyl-4-oxidanyl-4-oxidanylidene-butanoyl]pyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid
;
428.437   1   ?                ? ? ? 
7 water       nat water 18.015    245 ?                ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ACE,Dipeptidyl carboxypeptidase I,Kininase II' 
# 
_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       
;LVTDEAEASKFVEEYDRTSQVVWNEYAGANWNYNTNITTETSKILLQKNMQIAQHTLKYGTQARKFDVNQLQNTTIKRII
KKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPQGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQF
YPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLG
NMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWQKSMLEKPTDGREVVCHASA
WDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSE
GGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPS
SVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPQMSASAMLSYF
KPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;LVTDEAEASKFVEEYDRTSQVVWNEYAGANWNYNTNITTETSKILLQKNMQIAQHTLKYGTQARKFDVNQLQNTTIKRII
KKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPQGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQF
YPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLG
NMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWQKSMLEKPTDGREVVCHASA
WDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSE
GGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPS
SVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPQMSASAMLSYF
KPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLP
;
_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 
3 'ZINC ION' ZN  
4 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
5 'CHLORIDE ION' CL  
6 
;(2~{S})-1-[(2~{S})-2-[[(1~{S})-1-[(2~{S})-1-[(2~{S})-2-azanyl-4-oxidanyl-4-oxidanylidene-butanoyl]pyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid
;
BJ2 
7 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LEU n 
1 2   VAL n 
1 3   THR n 
1 4   ASP n 
1 5   GLU n 
1 6   ALA n 
1 7   GLU n 
1 8   ALA n 
1 9   SER n 
1 10  LYS n 
1 11  PHE n 
1 12  VAL n 
1 13  GLU n 
1 14  GLU n 
1 15  TYR n 
1 16  ASP n 
1 17  ARG n 
1 18  THR n 
1 19  SER n 
1 20  GLN n 
1 21  VAL n 
1 22  VAL n 
1 23  TRP n 
1 24  ASN n 
1 25  GLU n 
1 26  TYR n 
1 27  ALA n 
1 28  GLY n 
1 29  ALA n 
1 30  ASN n 
1 31  TRP n 
1 32  ASN n 
1 33  TYR n 
1 34  ASN n 
1 35  THR n 
1 36  ASN n 
1 37  ILE n 
1 38  THR n 
1 39  THR n 
1 40  GLU n 
1 41  THR n 
1 42  SER n 
1 43  LYS n 
1 44  ILE n 
1 45  LEU n 
1 46  LEU n 
1 47  GLN n 
1 48  LYS n 
1 49  ASN n 
1 50  MET n 
1 51  GLN n 
1 52  ILE n 
1 53  ALA n 
1 54  GLN n 
1 55  HIS n 
1 56  THR n 
1 57  LEU n 
1 58  LYS n 
1 59  TYR n 
1 60  GLY n 
1 61  THR n 
1 62  GLN n 
1 63  ALA n 
1 64  ARG n 
1 65  LYS n 
1 66  PHE n 
1 67  ASP n 
1 68  VAL n 
1 69  ASN n 
1 70  GLN n 
1 71  LEU n 
1 72  GLN n 
1 73  ASN n 
1 74  THR n 
1 75  THR n 
1 76  ILE n 
1 77  LYS n 
1 78  ARG n 
1 79  ILE n 
1 80  ILE n 
1 81  LYS n 
1 82  LYS n 
1 83  VAL n 
1 84  GLN n 
1 85  ASP n 
1 86  LEU n 
1 87  GLU n 
1 88  ARG n 
1 89  ALA n 
1 90  ALA n 
1 91  LEU n 
1 92  PRO n 
1 93  ALA n 
1 94  GLN n 
1 95  GLU n 
1 96  LEU n 
1 97  GLU n 
1 98  GLU n 
1 99  TYR n 
1 100 ASN n 
1 101 LYS n 
1 102 ILE n 
1 103 LEU n 
1 104 LEU n 
1 105 ASP n 
1 106 MET n 
1 107 GLU n 
1 108 THR n 
1 109 THR n 
1 110 TYR n 
1 111 SER n 
1 112 VAL n 
1 113 ALA n 
1 114 THR n 
1 115 VAL n 
1 116 CYS n 
1 117 HIS n 
1 118 PRO n 
1 119 GLN n 
1 120 GLY n 
1 121 SER n 
1 122 CYS n 
1 123 LEU n 
1 124 GLN n 
1 125 LEU n 
1 126 GLU n 
1 127 PRO n 
1 128 ASP n 
1 129 LEU n 
1 130 THR n 
1 131 ASN n 
1 132 VAL n 
1 133 MET n 
1 134 ALA n 
1 135 THR n 
1 136 SER n 
1 137 ARG n 
1 138 LYS n 
1 139 TYR n 
1 140 GLU n 
1 141 ASP n 
1 142 LEU n 
1 143 LEU n 
1 144 TRP n 
1 145 ALA n 
1 146 TRP n 
1 147 GLU n 
1 148 GLY n 
1 149 TRP n 
1 150 ARG n 
1 151 ASP n 
1 152 LYS n 
1 153 ALA n 
1 154 GLY n 
1 155 ARG n 
1 156 ALA n 
1 157 ILE n 
1 158 LEU n 
1 159 GLN n 
1 160 PHE n 
1 161 TYR n 
1 162 PRO n 
1 163 LYS n 
1 164 TYR n 
1 165 VAL n 
1 166 GLU n 
1 167 LEU n 
1 168 ILE n 
1 169 ASN n 
1 170 GLN n 
1 171 ALA n 
1 172 ALA n 
1 173 ARG n 
1 174 LEU n 
1 175 ASN n 
1 176 GLY n 
1 177 TYR n 
1 178 VAL n 
1 179 ASP n 
1 180 ALA n 
1 181 GLY n 
1 182 ASP n 
1 183 SER n 
1 184 TRP n 
1 185 ARG n 
1 186 SER n 
1 187 MET n 
1 188 TYR n 
1 189 GLU n 
1 190 THR n 
1 191 PRO n 
1 192 SER n 
1 193 LEU n 
1 194 GLU n 
1 195 GLN n 
1 196 ASP n 
1 197 LEU n 
1 198 GLU n 
1 199 ARG n 
1 200 LEU n 
1 201 PHE n 
1 202 GLN n 
1 203 GLU n 
1 204 LEU n 
1 205 GLN n 
1 206 PRO n 
1 207 LEU n 
1 208 TYR n 
1 209 LEU n 
1 210 ASN n 
1 211 LEU n 
1 212 HIS n 
1 213 ALA n 
1 214 TYR n 
1 215 VAL n 
1 216 ARG n 
1 217 ARG n 
1 218 ALA n 
1 219 LEU n 
1 220 HIS n 
1 221 ARG n 
1 222 HIS n 
1 223 TYR n 
1 224 GLY n 
1 225 ALA n 
1 226 GLN n 
1 227 HIS n 
1 228 ILE n 
1 229 ASN n 
1 230 LEU n 
1 231 GLU n 
1 232 GLY n 
1 233 PRO n 
1 234 ILE n 
1 235 PRO n 
1 236 ALA n 
1 237 HIS n 
1 238 LEU n 
1 239 LEU n 
1 240 GLY n 
1 241 ASN n 
1 242 MET n 
1 243 TRP n 
1 244 ALA n 
1 245 GLN n 
1 246 THR n 
1 247 TRP n 
1 248 SER n 
1 249 ASN n 
1 250 ILE n 
1 251 TYR n 
1 252 ASP n 
1 253 LEU n 
1 254 VAL n 
1 255 VAL n 
1 256 PRO n 
1 257 PHE n 
1 258 PRO n 
1 259 SER n 
1 260 ALA n 
1 261 PRO n 
1 262 SER n 
1 263 MET n 
1 264 ASP n 
1 265 THR n 
1 266 THR n 
1 267 GLU n 
1 268 ALA n 
1 269 MET n 
1 270 LEU n 
1 271 LYS n 
1 272 GLN n 
1 273 GLY n 
1 274 TRP n 
1 275 THR n 
1 276 PRO n 
1 277 ARG n 
1 278 ARG n 
1 279 MET n 
1 280 PHE n 
1 281 LYS n 
1 282 GLU n 
1 283 ALA n 
1 284 ASP n 
1 285 ASP n 
1 286 PHE n 
1 287 PHE n 
1 288 THR n 
1 289 SER n 
1 290 LEU n 
1 291 GLY n 
1 292 LEU n 
1 293 LEU n 
1 294 PRO n 
1 295 VAL n 
1 296 PRO n 
1 297 PRO n 
1 298 GLU n 
1 299 PHE n 
1 300 TRP n 
1 301 GLN n 
1 302 LYS n 
1 303 SER n 
1 304 MET n 
1 305 LEU n 
1 306 GLU n 
1 307 LYS n 
1 308 PRO n 
1 309 THR n 
1 310 ASP n 
1 311 GLY n 
1 312 ARG n 
1 313 GLU n 
1 314 VAL n 
1 315 VAL n 
1 316 CYS n 
1 317 HIS n 
1 318 ALA n 
1 319 SER n 
1 320 ALA n 
1 321 TRP n 
1 322 ASP n 
1 323 PHE n 
1 324 TYR n 
1 325 ASN n 
1 326 GLY n 
1 327 LYS n 
1 328 ASP n 
1 329 PHE n 
1 330 ARG n 
1 331 ILE n 
1 332 LYS n 
1 333 GLN n 
1 334 CYS n 
1 335 THR n 
1 336 THR n 
1 337 VAL n 
1 338 ASN n 
1 339 LEU n 
1 340 GLU n 
1 341 ASP n 
1 342 LEU n 
1 343 VAL n 
1 344 VAL n 
1 345 ALA n 
1 346 HIS n 
1 347 HIS n 
1 348 GLU n 
1 349 MET n 
1 350 GLY n 
1 351 HIS n 
1 352 ILE n 
1 353 GLN n 
1 354 TYR n 
1 355 PHE n 
1 356 MET n 
1 357 GLN n 
1 358 TYR n 
1 359 LYS n 
1 360 ASP n 
1 361 LEU n 
1 362 PRO n 
1 363 VAL n 
1 364 ALA n 
1 365 LEU n 
1 366 ARG n 
1 367 GLU n 
1 368 GLY n 
1 369 ALA n 
1 370 ASN n 
1 371 PRO n 
1 372 GLY n 
1 373 PHE n 
1 374 HIS n 
1 375 GLU n 
1 376 ALA n 
1 377 ILE n 
1 378 GLY n 
1 379 ASP n 
1 380 VAL n 
1 381 LEU n 
1 382 ALA n 
1 383 LEU n 
1 384 SER n 
1 385 VAL n 
1 386 SER n 
1 387 THR n 
1 388 PRO n 
1 389 LYS n 
1 390 HIS n 
1 391 LEU n 
1 392 HIS n 
1 393 SER n 
1 394 LEU n 
1 395 ASN n 
1 396 LEU n 
1 397 LEU n 
1 398 SER n 
1 399 SER n 
1 400 GLU n 
1 401 GLY n 
1 402 GLY n 
1 403 SER n 
1 404 ASP n 
1 405 GLU n 
1 406 HIS n 
1 407 ASP n 
1 408 ILE n 
1 409 ASN n 
1 410 PHE n 
1 411 LEU n 
1 412 MET n 
1 413 LYS n 
1 414 MET n 
1 415 ALA n 
1 416 LEU n 
1 417 ASP n 
1 418 LYS n 
1 419 ILE n 
1 420 ALA n 
1 421 PHE n 
1 422 ILE n 
1 423 PRO n 
1 424 PHE n 
1 425 SER n 
1 426 TYR n 
1 427 LEU n 
1 428 VAL n 
1 429 ASP n 
1 430 GLN n 
1 431 TRP n 
1 432 ARG n 
1 433 TRP n 
1 434 ARG n 
1 435 VAL n 
1 436 PHE n 
1 437 ASP n 
1 438 GLY n 
1 439 SER n 
1 440 ILE n 
1 441 THR n 
1 442 LYS n 
1 443 GLU n 
1 444 ASN n 
1 445 TYR n 
1 446 ASN n 
1 447 GLN n 
1 448 GLU n 
1 449 TRP n 
1 450 TRP n 
1 451 SER n 
1 452 LEU n 
1 453 ARG n 
1 454 LEU n 
1 455 LYS n 
1 456 TYR n 
1 457 GLN n 
1 458 GLY n 
1 459 LEU n 
1 460 CYS n 
1 461 PRO n 
1 462 PRO n 
1 463 VAL n 
1 464 PRO n 
1 465 ARG n 
1 466 THR n 
1 467 GLN n 
1 468 GLY n 
1 469 ASP n 
1 470 PHE n 
1 471 ASP n 
1 472 PRO n 
1 473 GLY n 
1 474 ALA n 
1 475 LYS n 
1 476 PHE n 
1 477 HIS n 
1 478 ILE n 
1 479 PRO n 
1 480 SER n 
1 481 SER n 
1 482 VAL n 
1 483 PRO n 
1 484 TYR n 
1 485 ILE n 
1 486 ARG n 
1 487 TYR n 
1 488 PHE n 
1 489 VAL n 
1 490 SER n 
1 491 PHE n 
1 492 ILE n 
1 493 ILE n 
1 494 GLN n 
1 495 PHE n 
1 496 GLN n 
1 497 PHE n 
1 498 HIS n 
1 499 GLU n 
1 500 ALA n 
1 501 LEU n 
1 502 CYS n 
1 503 GLN n 
1 504 ALA n 
1 505 ALA n 
1 506 GLY n 
1 507 HIS n 
1 508 THR n 
1 509 GLY n 
1 510 PRO n 
1 511 LEU n 
1 512 HIS n 
1 513 LYS n 
1 514 CYS n 
1 515 ASP n 
1 516 ILE n 
1 517 TYR n 
1 518 GLN n 
1 519 SER n 
1 520 LYS n 
1 521 GLU n 
1 522 ALA n 
1 523 GLY n 
1 524 GLN n 
1 525 ARG n 
1 526 LEU n 
1 527 ALA n 
1 528 THR n 
1 529 ALA n 
1 530 MET n 
1 531 LYS n 
1 532 LEU n 
1 533 GLY n 
1 534 PHE n 
1 535 SER n 
1 536 ARG n 
1 537 PRO n 
1 538 TRP n 
1 539 PRO n 
1 540 GLU n 
1 541 ALA n 
1 542 MET n 
1 543 GLN n 
1 544 LEU n 
1 545 ILE n 
1 546 THR n 
1 547 GLY n 
1 548 GLN n 
1 549 PRO n 
1 550 GLN n 
1 551 MET n 
1 552 SER n 
1 553 ALA n 
1 554 SER n 
1 555 ALA n 
1 556 MET n 
1 557 LEU n 
1 558 SER n 
1 559 TYR n 
1 560 PHE n 
1 561 LYS n 
1 562 PRO n 
1 563 LEU n 
1 564 LEU n 
1 565 ASP n 
1 566 TRP n 
1 567 LEU n 
1 568 ARG n 
1 569 THR n 
1 570 GLU n 
1 571 ASN n 
1 572 GLU n 
1 573 LEU n 
1 574 HIS n 
1 575 GLY n 
1 576 GLU n 
1 577 LYS n 
1 578 LEU n 
1 579 GLY n 
1 580 TRP n 
1 581 PRO n 
1 582 GLN n 
1 583 TYR n 
1 584 ASN n 
1 585 TRP n 
1 586 THR n 
1 587 PRO n 
1 588 ASN n 
1 589 SER n 
1 590 ALA n 
1 591 ARG n 
1 592 SER n 
1 593 GLU n 
1 594 GLY n 
1 595 PRO n 
1 596 LEU n 
1 597 PRO 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                   597 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ACE, DCP, DCP1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Cricetulus griseus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     10029 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 'DGlcpNAcb1-2DManpa1-3[DGlcpNAcb1-2DManpa1-6]DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML 
1.0   
2 2 
;WURCS=2.0/4,8,7/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-1-3-1-4/a4-b1_a6-h1_b4-c1_c3-d1_c6-f1_d2-e1_f2-g1
;
WURCS                       PDB2Glycan 1.1.0 
3 2 
;[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][b-D-GlcpNAc]{}}[(6+1)][a-D-Manp]{[(2+1)][b-D-GlcpNAc]{}}}}[(6+1)][a-L-Fucp]{}}
;
LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 2 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 2 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
4 2 5 NAG C1 O1 4 MAN O2 HO2 sing ? 
5 2 6 MAN C1 O1 3 BMA O6 HO6 sing ? 
6 2 7 NAG C1 O1 6 MAN O2 HO2 sing ? 
7 2 8 FUC C1 O1 1 NAG O6 HO6 sing ? 
# 
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 
BJ2 non-polymer                   . 
;(2~{S})-1-[(2~{S})-2-[[(1~{S})-1-[(2~{S})-1-[(2~{S})-2-azanyl-4-oxidanyl-4-oxidanylidene-butanoyl]pyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid
;
? 'C18 H28 N4 O8'  428.437 
BMA 'D-saccharide, beta linking'  . beta-D-mannopyranose 'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
CL  non-polymer                   . 'CHLORIDE ION' ? 'Cl -1'          35.453  
CYS 'L-peptide linking'           y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
FUC 'L-saccharide, alpha linking' . alpha-L-fucopyranose 'alpha-L-fucose; 6-deoxy-alpha-L-galactopyranose; L-fucose; fucose' 
'C6 H12 O5'      164.156 
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 
MAN 'D-saccharide, alpha linking' . alpha-D-mannopyranose 'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
MET 'L-peptide linking'           y METHIONINE ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'           y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'           y PROLINE ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'           y SERINE ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'           y THREONINE ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'           y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'           y VALINE ? 'C5 H11 N O2'    117.146 
ZN  non-polymer                   . 'ZINC ION' ? 'Zn 2'           65.409  
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
FUC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 LFucpa                         
FUC 'COMMON NAME'                         GMML     1.0 a-L-fucopyranose               
FUC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-L-Fucp                       
FUC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Fuc                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   LEU 1   37  ?   ?   ?   A . n 
A 1 2   VAL 2   38  ?   ?   ?   A . n 
A 1 3   THR 3   39  ?   ?   ?   A . n 
A 1 4   ASP 4   40  40  ASP ASP A . n 
A 1 5   GLU 5   41  41  GLU GLU A . n 
A 1 6   ALA 6   42  42  ALA ALA A . n 
A 1 7   GLU 7   43  43  GLU GLU A . n 
A 1 8   ALA 8   44  44  ALA ALA A . n 
A 1 9   SER 9   45  45  SER SER A . n 
A 1 10  LYS 10  46  46  LYS LYS A . n 
A 1 11  PHE 11  47  47  PHE PHE A . n 
A 1 12  VAL 12  48  48  VAL VAL A . n 
A 1 13  GLU 13  49  49  GLU GLU A . n 
A 1 14  GLU 14  50  50  GLU GLU A . n 
A 1 15  TYR 15  51  51  TYR TYR A . n 
A 1 16  ASP 16  52  52  ASP ASP A . n 
A 1 17  ARG 17  53  53  ARG ARG A . n 
A 1 18  THR 18  54  54  THR THR A . n 
A 1 19  SER 19  55  55  SER SER A . n 
A 1 20  GLN 20  56  56  GLN GLN A . n 
A 1 21  VAL 21  57  57  VAL VAL A . n 
A 1 22  VAL 22  58  58  VAL VAL A . n 
A 1 23  TRP 23  59  59  TRP TRP A . n 
A 1 24  ASN 24  60  60  ASN ASN A . n 
A 1 25  GLU 25  61  61  GLU GLU A . n 
A 1 26  TYR 26  62  62  TYR TYR A . n 
A 1 27  ALA 27  63  63  ALA ALA A . n 
A 1 28  GLY 28  64  64  GLY GLY A . n 
A 1 29  ALA 29  65  65  ALA ALA A . n 
A 1 30  ASN 30  66  66  ASN ASN A . n 
A 1 31  TRP 31  67  67  TRP TRP A . n 
A 1 32  ASN 32  68  68  ASN ASN A . n 
A 1 33  TYR 33  69  69  TYR TYR A . n 
A 1 34  ASN 34  70  70  ASN ASN A . n 
A 1 35  THR 35  71  71  THR THR A . n 
A 1 36  ASN 36  72  72  ASN ASN A . n 
A 1 37  ILE 37  73  73  ILE ILE A . n 
A 1 38  THR 38  74  74  THR THR A . n 
A 1 39  THR 39  75  75  THR THR A . n 
A 1 40  GLU 40  76  76  GLU GLU A . n 
A 1 41  THR 41  77  77  THR THR A . n 
A 1 42  SER 42  78  78  SER SER A . n 
A 1 43  LYS 43  79  79  LYS LYS A . n 
A 1 44  ILE 44  80  80  ILE ILE A . n 
A 1 45  LEU 45  81  81  LEU LEU A . n 
A 1 46  LEU 46  82  82  LEU LEU A . n 
A 1 47  GLN 47  83  83  GLN GLN A . n 
A 1 48  LYS 48  84  84  LYS LYS A . n 
A 1 49  ASN 49  85  85  ASN ASN A . n 
A 1 50  MET 50  86  86  MET MET A . n 
A 1 51  GLN 51  87  87  GLN GLN A . n 
A 1 52  ILE 52  88  88  ILE ILE A . n 
A 1 53  ALA 53  89  89  ALA ALA A . n 
A 1 54  GLN 54  90  90  GLN GLN A . n 
A 1 55  HIS 55  91  91  HIS HIS A . n 
A 1 56  THR 56  92  92  THR THR A . n 
A 1 57  LEU 57  93  93  LEU LEU A . n 
A 1 58  LYS 58  94  94  LYS LYS A . n 
A 1 59  TYR 59  95  95  TYR TYR A . n 
A 1 60  GLY 60  96  96  GLY GLY A . n 
A 1 61  THR 61  97  97  THR THR A . n 
A 1 62  GLN 62  98  98  GLN GLN A . n 
A 1 63  ALA 63  99  99  ALA ALA A . n 
A 1 64  ARG 64  100 100 ARG ARG A . n 
A 1 65  LYS 65  101 101 LYS LYS A . n 
A 1 66  PHE 66  102 102 PHE PHE A . n 
A 1 67  ASP 67  103 103 ASP ASP A . n 
A 1 68  VAL 68  104 104 VAL VAL A . n 
A 1 69  ASN 69  105 105 ASN ASN A . n 
A 1 70  GLN 70  106 106 GLN GLN A . n 
A 1 71  LEU 71  107 107 LEU LEU A . n 
A 1 72  GLN 72  108 108 GLN GLN A . n 
A 1 73  ASN 73  109 109 ASN ASN A . n 
A 1 74  THR 74  110 110 THR THR A . n 
A 1 75  THR 75  111 111 THR THR A . n 
A 1 76  ILE 76  112 112 ILE ILE A . n 
A 1 77  LYS 77  113 113 LYS LYS A . n 
A 1 78  ARG 78  114 114 ARG ARG A . n 
A 1 79  ILE 79  115 115 ILE ILE A . n 
A 1 80  ILE 80  116 116 ILE ILE A . n 
A 1 81  LYS 81  117 117 LYS LYS A . n 
A 1 82  LYS 82  118 118 LYS LYS A . n 
A 1 83  VAL 83  119 119 VAL VAL A . n 
A 1 84  GLN 84  120 120 GLN GLN A . n 
A 1 85  ASP 85  121 121 ASP ASP A . n 
A 1 86  LEU 86  122 122 LEU LEU A . n 
A 1 87  GLU 87  123 123 GLU GLU A . n 
A 1 88  ARG 88  124 124 ARG ARG A . n 
A 1 89  ALA 89  125 125 ALA ALA A . n 
A 1 90  ALA 90  126 126 ALA ALA A . n 
A 1 91  LEU 91  127 127 LEU LEU A . n 
A 1 92  PRO 92  128 128 PRO PRO A . n 
A 1 93  ALA 93  129 129 ALA ALA A . n 
A 1 94  GLN 94  130 130 GLN GLN A . n 
A 1 95  GLU 95  131 131 GLU GLU A . n 
A 1 96  LEU 96  132 132 LEU LEU A . n 
A 1 97  GLU 97  133 133 GLU GLU A . n 
A 1 98  GLU 98  134 134 GLU GLU A . n 
A 1 99  TYR 99  135 135 TYR TYR A . n 
A 1 100 ASN 100 136 136 ASN ASN A . n 
A 1 101 LYS 101 137 137 LYS LYS A . n 
A 1 102 ILE 102 138 138 ILE ILE A . n 
A 1 103 LEU 103 139 139 LEU LEU A . n 
A 1 104 LEU 104 140 140 LEU LEU A . n 
A 1 105 ASP 105 141 141 ASP ASP A . n 
A 1 106 MET 106 142 142 MET MET A . n 
A 1 107 GLU 107 143 143 GLU GLU A . n 
A 1 108 THR 108 144 144 THR THR A . n 
A 1 109 THR 109 145 145 THR THR A . n 
A 1 110 TYR 110 146 146 TYR TYR A . n 
A 1 111 SER 111 147 147 SER SER A . n 
A 1 112 VAL 112 148 148 VAL VAL A . n 
A 1 113 ALA 113 149 149 ALA ALA A . n 
A 1 114 THR 114 150 150 THR THR A . n 
A 1 115 VAL 115 151 151 VAL VAL A . n 
A 1 116 CYS 116 152 152 CYS CYS A . n 
A 1 117 HIS 117 153 153 HIS HIS A . n 
A 1 118 PRO 118 154 154 PRO PRO A . n 
A 1 119 GLN 119 155 155 GLN GLN A . n 
A 1 120 GLY 120 156 156 GLY GLY A . n 
A 1 121 SER 121 157 157 SER SER A . n 
A 1 122 CYS 122 158 158 CYS CYS A . n 
A 1 123 LEU 123 159 159 LEU LEU A . n 
A 1 124 GLN 124 160 160 GLN GLN A . n 
A 1 125 LEU 125 161 161 LEU LEU A . n 
A 1 126 GLU 126 162 162 GLU GLU A . n 
A 1 127 PRO 127 163 163 PRO PRO A . n 
A 1 128 ASP 128 164 164 ASP ASP A . n 
A 1 129 LEU 129 165 165 LEU LEU A . n 
A 1 130 THR 130 166 166 THR THR A . n 
A 1 131 ASN 131 167 167 ASN ASN A . n 
A 1 132 VAL 132 168 168 VAL VAL A . n 
A 1 133 MET 133 169 169 MET MET A . n 
A 1 134 ALA 134 170 170 ALA ALA A . n 
A 1 135 THR 135 171 171 THR THR A . n 
A 1 136 SER 136 172 172 SER SER A . n 
A 1 137 ARG 137 173 173 ARG ARG A . n 
A 1 138 LYS 138 174 174 LYS LYS A . n 
A 1 139 TYR 139 175 175 TYR TYR A . n 
A 1 140 GLU 140 176 176 GLU GLU A . n 
A 1 141 ASP 141 177 177 ASP ASP A . n 
A 1 142 LEU 142 178 178 LEU LEU A . n 
A 1 143 LEU 143 179 179 LEU LEU A . n 
A 1 144 TRP 144 180 180 TRP TRP A . n 
A 1 145 ALA 145 181 181 ALA ALA A . n 
A 1 146 TRP 146 182 182 TRP TRP A . n 
A 1 147 GLU 147 183 183 GLU GLU A . n 
A 1 148 GLY 148 184 184 GLY GLY A . n 
A 1 149 TRP 149 185 185 TRP TRP A . n 
A 1 150 ARG 150 186 186 ARG ARG A . n 
A 1 151 ASP 151 187 187 ASP ASP A . n 
A 1 152 LYS 152 188 188 LYS LYS A . n 
A 1 153 ALA 153 189 189 ALA ALA A . n 
A 1 154 GLY 154 190 190 GLY GLY A . n 
A 1 155 ARG 155 191 191 ARG ARG A . n 
A 1 156 ALA 156 192 192 ALA ALA A . n 
A 1 157 ILE 157 193 193 ILE ILE A . n 
A 1 158 LEU 158 194 194 LEU LEU A . n 
A 1 159 GLN 159 195 195 GLN GLN A . n 
A 1 160 PHE 160 196 196 PHE PHE A . n 
A 1 161 TYR 161 197 197 TYR TYR A . n 
A 1 162 PRO 162 198 198 PRO PRO A . n 
A 1 163 LYS 163 199 199 LYS LYS A . n 
A 1 164 TYR 164 200 200 TYR TYR A . n 
A 1 165 VAL 165 201 201 VAL VAL A . n 
A 1 166 GLU 166 202 202 GLU GLU A . n 
A 1 167 LEU 167 203 203 LEU LEU A . n 
A 1 168 ILE 168 204 204 ILE ILE A . n 
A 1 169 ASN 169 205 205 ASN ASN A . n 
A 1 170 GLN 170 206 206 GLN GLN A . n 
A 1 171 ALA 171 207 207 ALA ALA A . n 
A 1 172 ALA 172 208 208 ALA ALA A . n 
A 1 173 ARG 173 209 209 ARG ARG A . n 
A 1 174 LEU 174 210 210 LEU LEU A . n 
A 1 175 ASN 175 211 211 ASN ASN A . n 
A 1 176 GLY 176 212 212 GLY GLY A . n 
A 1 177 TYR 177 213 213 TYR TYR A . n 
A 1 178 VAL 178 214 214 VAL VAL A . n 
A 1 179 ASP 179 215 215 ASP ASP A . n 
A 1 180 ALA 180 216 216 ALA ALA A . n 
A 1 181 GLY 181 217 217 GLY GLY A . n 
A 1 182 ASP 182 218 218 ASP ASP A . n 
A 1 183 SER 183 219 219 SER SER A . n 
A 1 184 TRP 184 220 220 TRP TRP A . n 
A 1 185 ARG 185 221 221 ARG ARG A . n 
A 1 186 SER 186 222 222 SER SER A . n 
A 1 187 MET 187 223 223 MET MET A . n 
A 1 188 TYR 188 224 224 TYR TYR A . n 
A 1 189 GLU 189 225 225 GLU GLU A . n 
A 1 190 THR 190 226 226 THR THR A . n 
A 1 191 PRO 191 227 227 PRO PRO A . n 
A 1 192 SER 192 228 228 SER SER A . n 
A 1 193 LEU 193 229 229 LEU LEU A . n 
A 1 194 GLU 194 230 230 GLU GLU A . n 
A 1 195 GLN 195 231 231 GLN GLN A . n 
A 1 196 ASP 196 232 232 ASP ASP A . n 
A 1 197 LEU 197 233 233 LEU LEU A . n 
A 1 198 GLU 198 234 234 GLU GLU A . n 
A 1 199 ARG 199 235 235 ARG ARG A . n 
A 1 200 LEU 200 236 236 LEU LEU A . n 
A 1 201 PHE 201 237 237 PHE PHE A . n 
A 1 202 GLN 202 238 238 GLN GLN A . n 
A 1 203 GLU 203 239 239 GLU GLU A . n 
A 1 204 LEU 204 240 240 LEU LEU A . n 
A 1 205 GLN 205 241 241 GLN GLN A . n 
A 1 206 PRO 206 242 242 PRO PRO A . n 
A 1 207 LEU 207 243 243 LEU LEU A . n 
A 1 208 TYR 208 244 244 TYR TYR A . n 
A 1 209 LEU 209 245 245 LEU LEU A . n 
A 1 210 ASN 210 246 246 ASN ASN A . n 
A 1 211 LEU 211 247 247 LEU LEU A . n 
A 1 212 HIS 212 248 248 HIS HIS A . n 
A 1 213 ALA 213 249 249 ALA ALA A . n 
A 1 214 TYR 214 250 250 TYR TYR A . n 
A 1 215 VAL 215 251 251 VAL VAL A . n 
A 1 216 ARG 216 252 252 ARG ARG A . n 
A 1 217 ARG 217 253 253 ARG ARG A . n 
A 1 218 ALA 218 254 254 ALA ALA A . n 
A 1 219 LEU 219 255 255 LEU LEU A . n 
A 1 220 HIS 220 256 256 HIS HIS A . n 
A 1 221 ARG 221 257 257 ARG ARG A . n 
A 1 222 HIS 222 258 258 HIS HIS A . n 
A 1 223 TYR 223 259 259 TYR TYR A . n 
A 1 224 GLY 224 260 260 GLY GLY A . n 
A 1 225 ALA 225 261 261 ALA ALA A . n 
A 1 226 GLN 226 262 262 GLN GLN A . n 
A 1 227 HIS 227 263 263 HIS HIS A . n 
A 1 228 ILE 228 264 264 ILE ILE A . n 
A 1 229 ASN 229 265 265 ASN ASN A . n 
A 1 230 LEU 230 266 266 LEU LEU A . n 
A 1 231 GLU 231 267 267 GLU GLU A . n 
A 1 232 GLY 232 268 268 GLY GLY A . n 
A 1 233 PRO 233 269 269 PRO PRO A . n 
A 1 234 ILE 234 270 270 ILE ILE A . n 
A 1 235 PRO 235 271 271 PRO PRO A . n 
A 1 236 ALA 236 272 272 ALA ALA A . n 
A 1 237 HIS 237 273 273 HIS HIS A . n 
A 1 238 LEU 238 274 274 LEU LEU A . n 
A 1 239 LEU 239 275 275 LEU LEU A . n 
A 1 240 GLY 240 276 276 GLY GLY A . n 
A 1 241 ASN 241 277 277 ASN ASN A . n 
A 1 242 MET 242 278 278 MET MET A . n 
A 1 243 TRP 243 279 279 TRP TRP A . n 
A 1 244 ALA 244 280 280 ALA ALA A . n 
A 1 245 GLN 245 281 281 GLN GLN A . n 
A 1 246 THR 246 282 282 THR THR A . n 
A 1 247 TRP 247 283 283 TRP TRP A . n 
A 1 248 SER 248 284 284 SER SER A . n 
A 1 249 ASN 249 285 285 ASN ASN A . n 
A 1 250 ILE 250 286 286 ILE ILE A . n 
A 1 251 TYR 251 287 287 TYR TYR A . n 
A 1 252 ASP 252 288 288 ASP ASP A . n 
A 1 253 LEU 253 289 289 LEU LEU A . n 
A 1 254 VAL 254 290 290 VAL VAL A . n 
A 1 255 VAL 255 291 291 VAL VAL A . n 
A 1 256 PRO 256 292 292 PRO PRO A . n 
A 1 257 PHE 257 293 293 PHE PHE A . n 
A 1 258 PRO 258 294 294 PRO PRO A . n 
A 1 259 SER 259 295 295 SER SER A . n 
A 1 260 ALA 260 296 296 ALA ALA A . n 
A 1 261 PRO 261 297 297 PRO PRO A . n 
A 1 262 SER 262 298 298 SER SER A . n 
A 1 263 MET 263 299 299 MET MET A . n 
A 1 264 ASP 264 300 300 ASP ASP A . n 
A 1 265 THR 265 301 301 THR THR A . n 
A 1 266 THR 266 302 302 THR THR A . n 
A 1 267 GLU 267 303 303 GLU GLU A . n 
A 1 268 ALA 268 304 304 ALA ALA A . n 
A 1 269 MET 269 305 305 MET MET A . n 
A 1 270 LEU 270 306 306 LEU LEU A . n 
A 1 271 LYS 271 307 307 LYS LYS A . n 
A 1 272 GLN 272 308 308 GLN GLN A . n 
A 1 273 GLY 273 309 309 GLY GLY A . n 
A 1 274 TRP 274 310 310 TRP TRP A . n 
A 1 275 THR 275 311 311 THR THR A . n 
A 1 276 PRO 276 312 312 PRO PRO A . n 
A 1 277 ARG 277 313 313 ARG ARG A . n 
A 1 278 ARG 278 314 314 ARG ARG A . n 
A 1 279 MET 279 315 315 MET MET A . n 
A 1 280 PHE 280 316 316 PHE PHE A . n 
A 1 281 LYS 281 317 317 LYS LYS A . n 
A 1 282 GLU 282 318 318 GLU GLU A . n 
A 1 283 ALA 283 319 319 ALA ALA A . n 
A 1 284 ASP 284 320 320 ASP ASP A . n 
A 1 285 ASP 285 321 321 ASP ASP A . n 
A 1 286 PHE 286 322 322 PHE PHE A . n 
A 1 287 PHE 287 323 323 PHE PHE A . n 
A 1 288 THR 288 324 324 THR THR A . n 
A 1 289 SER 289 325 325 SER SER A . n 
A 1 290 LEU 290 326 326 LEU LEU A . n 
A 1 291 GLY 291 327 327 GLY GLY A . n 
A 1 292 LEU 292 328 328 LEU LEU A . n 
A 1 293 LEU 293 329 329 LEU LEU A . n 
A 1 294 PRO 294 330 330 PRO PRO A . n 
A 1 295 VAL 295 331 331 VAL VAL A . n 
A 1 296 PRO 296 332 332 PRO PRO A . n 
A 1 297 PRO 297 333 333 PRO PRO A . n 
A 1 298 GLU 298 334 334 GLU GLU A . n 
A 1 299 PHE 299 335 335 PHE PHE A . n 
A 1 300 TRP 300 336 336 TRP TRP A . n 
A 1 301 GLN 301 337 337 GLN GLN A . n 
A 1 302 LYS 302 338 338 LYS LYS A . n 
A 1 303 SER 303 339 339 SER SER A . n 
A 1 304 MET 304 340 340 MET MET A . n 
A 1 305 LEU 305 341 341 LEU LEU A . n 
A 1 306 GLU 306 342 342 GLU GLU A . n 
A 1 307 LYS 307 343 343 LYS LYS A . n 
A 1 308 PRO 308 344 344 PRO PRO A . n 
A 1 309 THR 309 345 345 THR THR A . n 
A 1 310 ASP 310 346 346 ASP ASP A . n 
A 1 311 GLY 311 347 347 GLY GLY A . n 
A 1 312 ARG 312 348 348 ARG ARG A . n 
A 1 313 GLU 313 349 349 GLU GLU A . n 
A 1 314 VAL 314 350 350 VAL VAL A . n 
A 1 315 VAL 315 351 351 VAL VAL A . n 
A 1 316 CYS 316 352 352 CYS CYS A . n 
A 1 317 HIS 317 353 353 HIS HIS A . n 
A 1 318 ALA 318 354 354 ALA ALA A . n 
A 1 319 SER 319 355 355 SER SER A . n 
A 1 320 ALA 320 356 356 ALA ALA A . n 
A 1 321 TRP 321 357 357 TRP TRP A . n 
A 1 322 ASP 322 358 358 ASP ASP A . n 
A 1 323 PHE 323 359 359 PHE PHE A . n 
A 1 324 TYR 324 360 360 TYR TYR A . n 
A 1 325 ASN 325 361 361 ASN ASN A . n 
A 1 326 GLY 326 362 362 GLY GLY A . n 
A 1 327 LYS 327 363 363 LYS LYS A . n 
A 1 328 ASP 328 364 364 ASP ASP A . n 
A 1 329 PHE 329 365 365 PHE PHE A . n 
A 1 330 ARG 330 366 366 ARG ARG A . n 
A 1 331 ILE 331 367 367 ILE ILE A . n 
A 1 332 LYS 332 368 368 LYS LYS A . n 
A 1 333 GLN 333 369 369 GLN GLN A . n 
A 1 334 CYS 334 370 370 CYS CYS A . n 
A 1 335 THR 335 371 371 THR THR A . n 
A 1 336 THR 336 372 372 THR THR A . n 
A 1 337 VAL 337 373 373 VAL VAL A . n 
A 1 338 ASN 338 374 374 ASN ASN A . n 
A 1 339 LEU 339 375 375 LEU LEU A . n 
A 1 340 GLU 340 376 376 GLU GLU A . n 
A 1 341 ASP 341 377 377 ASP ASP A . n 
A 1 342 LEU 342 378 378 LEU LEU A . n 
A 1 343 VAL 343 379 379 VAL VAL A . n 
A 1 344 VAL 344 380 380 VAL VAL A . n 
A 1 345 ALA 345 381 381 ALA ALA A . n 
A 1 346 HIS 346 382 382 HIS HIS A . n 
A 1 347 HIS 347 383 383 HIS HIS A . n 
A 1 348 GLU 348 384 384 GLU GLU A . n 
A 1 349 MET 349 385 385 MET MET A . n 
A 1 350 GLY 350 386 386 GLY GLY A . n 
A 1 351 HIS 351 387 387 HIS HIS A . n 
A 1 352 ILE 352 388 388 ILE ILE A . n 
A 1 353 GLN 353 389 389 GLN GLN A . n 
A 1 354 TYR 354 390 390 TYR TYR A . n 
A 1 355 PHE 355 391 391 PHE PHE A . n 
A 1 356 MET 356 392 392 MET MET A . n 
A 1 357 GLN 357 393 393 GLN GLN A . n 
A 1 358 TYR 358 394 394 TYR TYR A . n 
A 1 359 LYS 359 395 395 LYS LYS A . n 
A 1 360 ASP 360 396 396 ASP ASP A . n 
A 1 361 LEU 361 397 397 LEU LEU A . n 
A 1 362 PRO 362 398 398 PRO PRO A . n 
A 1 363 VAL 363 399 399 VAL VAL A . n 
A 1 364 ALA 364 400 400 ALA ALA A . n 
A 1 365 LEU 365 401 401 LEU LEU A . n 
A 1 366 ARG 366 402 402 ARG ARG A . n 
A 1 367 GLU 367 403 403 GLU GLU A . n 
A 1 368 GLY 368 404 404 GLY GLY A . n 
A 1 369 ALA 369 405 405 ALA ALA A . n 
A 1 370 ASN 370 406 406 ASN ASN A . n 
A 1 371 PRO 371 407 407 PRO PRO A . n 
A 1 372 GLY 372 408 408 GLY GLY A . n 
A 1 373 PHE 373 409 409 PHE PHE A . n 
A 1 374 HIS 374 410 410 HIS HIS A . n 
A 1 375 GLU 375 411 411 GLU GLU A . n 
A 1 376 ALA 376 412 412 ALA ALA A . n 
A 1 377 ILE 377 413 413 ILE ILE A . n 
A 1 378 GLY 378 414 414 GLY GLY A . n 
A 1 379 ASP 379 415 415 ASP ASP A . n 
A 1 380 VAL 380 416 416 VAL VAL A . n 
A 1 381 LEU 381 417 417 LEU LEU A . n 
A 1 382 ALA 382 418 418 ALA ALA A . n 
A 1 383 LEU 383 419 419 LEU LEU A . n 
A 1 384 SER 384 420 420 SER SER A . n 
A 1 385 VAL 385 421 421 VAL VAL A . n 
A 1 386 SER 386 422 422 SER SER A . n 
A 1 387 THR 387 423 423 THR THR A . n 
A 1 388 PRO 388 424 424 PRO PRO A . n 
A 1 389 LYS 389 425 425 LYS LYS A . n 
A 1 390 HIS 390 426 426 HIS HIS A . n 
A 1 391 LEU 391 427 427 LEU LEU A . n 
A 1 392 HIS 392 428 428 HIS HIS A . n 
A 1 393 SER 393 429 429 SER SER A . n 
A 1 394 LEU 394 430 430 LEU LEU A . n 
A 1 395 ASN 395 431 431 ASN ASN A . n 
A 1 396 LEU 396 432 432 LEU LEU A . n 
A 1 397 LEU 397 433 433 LEU LEU A . n 
A 1 398 SER 398 434 434 SER SER A . n 
A 1 399 SER 399 435 435 SER SER A . n 
A 1 400 GLU 400 436 ?   ?   ?   A . n 
A 1 401 GLY 401 437 ?   ?   ?   A . n 
A 1 402 GLY 402 438 438 GLY GLY A . n 
A 1 403 SER 403 439 439 SER SER A . n 
A 1 404 ASP 404 440 440 ASP ASP A . n 
A 1 405 GLU 405 441 441 GLU GLU A . n 
A 1 406 HIS 406 442 442 HIS HIS A . n 
A 1 407 ASP 407 443 443 ASP ASP A . n 
A 1 408 ILE 408 444 444 ILE ILE A . n 
A 1 409 ASN 409 445 445 ASN ASN A . n 
A 1 410 PHE 410 446 446 PHE PHE A . n 
A 1 411 LEU 411 447 447 LEU LEU A . n 
A 1 412 MET 412 448 448 MET MET A . n 
A 1 413 LYS 413 449 449 LYS LYS A . n 
A 1 414 MET 414 450 450 MET MET A . n 
A 1 415 ALA 415 451 451 ALA ALA A . n 
A 1 416 LEU 416 452 452 LEU LEU A . n 
A 1 417 ASP 417 453 453 ASP ASP A . n 
A 1 418 LYS 418 454 454 LYS LYS A . n 
A 1 419 ILE 419 455 455 ILE ILE A . n 
A 1 420 ALA 420 456 456 ALA ALA A . n 
A 1 421 PHE 421 457 457 PHE PHE A . n 
A 1 422 ILE 422 458 458 ILE ILE A . n 
A 1 423 PRO 423 459 459 PRO PRO A . n 
A 1 424 PHE 424 460 460 PHE PHE A . n 
A 1 425 SER 425 461 461 SER SER A . n 
A 1 426 TYR 426 462 462 TYR TYR A . n 
A 1 427 LEU 427 463 463 LEU LEU A . n 
A 1 428 VAL 428 464 464 VAL VAL A . n 
A 1 429 ASP 429 465 465 ASP ASP A . n 
A 1 430 GLN 430 466 466 GLN GLN A . n 
A 1 431 TRP 431 467 467 TRP TRP A . n 
A 1 432 ARG 432 468 468 ARG ARG A . n 
A 1 433 TRP 433 469 469 TRP TRP A . n 
A 1 434 ARG 434 470 470 ARG ARG A . n 
A 1 435 VAL 435 471 471 VAL VAL A . n 
A 1 436 PHE 436 472 472 PHE PHE A . n 
A 1 437 ASP 437 473 473 ASP ASP A . n 
A 1 438 GLY 438 474 474 GLY GLY A . n 
A 1 439 SER 439 475 475 SER SER A . n 
A 1 440 ILE 440 476 476 ILE ILE A . n 
A 1 441 THR 441 477 477 THR THR A . n 
A 1 442 LYS 442 478 478 LYS LYS A . n 
A 1 443 GLU 443 479 479 GLU GLU A . n 
A 1 444 ASN 444 480 480 ASN ASN A . n 
A 1 445 TYR 445 481 481 TYR TYR A . n 
A 1 446 ASN 446 482 482 ASN ASN A . n 
A 1 447 GLN 447 483 483 GLN GLN A . n 
A 1 448 GLU 448 484 484 GLU GLU A . n 
A 1 449 TRP 449 485 485 TRP TRP A . n 
A 1 450 TRP 450 486 486 TRP TRP A . n 
A 1 451 SER 451 487 487 SER SER A . n 
A 1 452 LEU 452 488 488 LEU LEU A . n 
A 1 453 ARG 453 489 489 ARG ARG A . n 
A 1 454 LEU 454 490 490 LEU LEU A . n 
A 1 455 LYS 455 491 491 LYS LYS A . n 
A 1 456 TYR 456 492 492 TYR TYR A . n 
A 1 457 GLN 457 493 493 GLN GLN A . n 
A 1 458 GLY 458 494 494 GLY GLY A . n 
A 1 459 LEU 459 495 495 LEU LEU A . n 
A 1 460 CYS 460 496 496 CYS CYS A . n 
A 1 461 PRO 461 497 497 PRO PRO A . n 
A 1 462 PRO 462 498 498 PRO PRO A . n 
A 1 463 VAL 463 499 499 VAL VAL A . n 
A 1 464 PRO 464 500 500 PRO PRO A . n 
A 1 465 ARG 465 501 501 ARG ARG A . n 
A 1 466 THR 466 502 502 THR THR A . n 
A 1 467 GLN 467 503 503 GLN GLN A . n 
A 1 468 GLY 468 504 504 GLY GLY A . n 
A 1 469 ASP 469 505 505 ASP ASP A . n 
A 1 470 PHE 470 506 506 PHE PHE A . n 
A 1 471 ASP 471 507 507 ASP ASP A . n 
A 1 472 PRO 472 508 508 PRO PRO A . n 
A 1 473 GLY 473 509 509 GLY GLY A . n 
A 1 474 ALA 474 510 510 ALA ALA A . n 
A 1 475 LYS 475 511 511 LYS LYS A . n 
A 1 476 PHE 476 512 512 PHE PHE A . n 
A 1 477 HIS 477 513 513 HIS HIS A . n 
A 1 478 ILE 478 514 514 ILE ILE A . n 
A 1 479 PRO 479 515 515 PRO PRO A . n 
A 1 480 SER 480 516 516 SER SER A . n 
A 1 481 SER 481 517 517 SER SER A . n 
A 1 482 VAL 482 518 518 VAL VAL A . n 
A 1 483 PRO 483 519 519 PRO PRO A . n 
A 1 484 TYR 484 520 520 TYR TYR A . n 
A 1 485 ILE 485 521 521 ILE ILE A . n 
A 1 486 ARG 486 522 522 ARG ARG A . n 
A 1 487 TYR 487 523 523 TYR TYR A . n 
A 1 488 PHE 488 524 524 PHE PHE A . n 
A 1 489 VAL 489 525 525 VAL VAL A . n 
A 1 490 SER 490 526 526 SER SER A . n 
A 1 491 PHE 491 527 527 PHE PHE A . n 
A 1 492 ILE 492 528 528 ILE ILE A . n 
A 1 493 ILE 493 529 529 ILE ILE A . n 
A 1 494 GLN 494 530 530 GLN GLN A . n 
A 1 495 PHE 495 531 531 PHE PHE A . n 
A 1 496 GLN 496 532 532 GLN GLN A . n 
A 1 497 PHE 497 533 533 PHE PHE A . n 
A 1 498 HIS 498 534 534 HIS HIS A . n 
A 1 499 GLU 499 535 535 GLU GLU A . n 
A 1 500 ALA 500 536 536 ALA ALA A . n 
A 1 501 LEU 501 537 537 LEU LEU A . n 
A 1 502 CYS 502 538 538 CYS CYS A . n 
A 1 503 GLN 503 539 539 GLN GLN A . n 
A 1 504 ALA 504 540 540 ALA ALA A . n 
A 1 505 ALA 505 541 541 ALA ALA A . n 
A 1 506 GLY 506 542 542 GLY GLY A . n 
A 1 507 HIS 507 543 543 HIS HIS A . n 
A 1 508 THR 508 544 544 THR THR A . n 
A 1 509 GLY 509 545 545 GLY GLY A . n 
A 1 510 PRO 510 546 546 PRO PRO A . n 
A 1 511 LEU 511 547 547 LEU LEU A . n 
A 1 512 HIS 512 548 548 HIS HIS A . n 
A 1 513 LYS 513 549 549 LYS LYS A . n 
A 1 514 CYS 514 550 550 CYS CYS A . n 
A 1 515 ASP 515 551 551 ASP ASP A . n 
A 1 516 ILE 516 552 552 ILE ILE A . n 
A 1 517 TYR 517 553 553 TYR TYR A . n 
A 1 518 GLN 518 554 554 GLN GLN A . n 
A 1 519 SER 519 555 555 SER SER A . n 
A 1 520 LYS 520 556 556 LYS LYS A . n 
A 1 521 GLU 521 557 557 GLU GLU A . n 
A 1 522 ALA 522 558 558 ALA ALA A . n 
A 1 523 GLY 523 559 559 GLY GLY A . n 
A 1 524 GLN 524 560 560 GLN GLN A . n 
A 1 525 ARG 525 561 561 ARG ARG A . n 
A 1 526 LEU 526 562 562 LEU LEU A . n 
A 1 527 ALA 527 563 563 ALA ALA A . n 
A 1 528 THR 528 564 564 THR THR A . n 
A 1 529 ALA 529 565 565 ALA ALA A . n 
A 1 530 MET 530 566 566 MET MET A . n 
A 1 531 LYS 531 567 567 LYS LYS A . n 
A 1 532 LEU 532 568 568 LEU LEU A . n 
A 1 533 GLY 533 569 569 GLY GLY A . n 
A 1 534 PHE 534 570 570 PHE PHE A . n 
A 1 535 SER 535 571 571 SER SER A . n 
A 1 536 ARG 536 572 572 ARG ARG A . n 
A 1 537 PRO 537 573 573 PRO PRO A . n 
A 1 538 TRP 538 574 574 TRP TRP A . n 
A 1 539 PRO 539 575 575 PRO PRO A . n 
A 1 540 GLU 540 576 576 GLU GLU A . n 
A 1 541 ALA 541 577 577 ALA ALA A . n 
A 1 542 MET 542 578 578 MET MET A . n 
A 1 543 GLN 543 579 579 GLN GLN A . n 
A 1 544 LEU 544 580 580 LEU LEU A . n 
A 1 545 ILE 545 581 581 ILE ILE A . n 
A 1 546 THR 546 582 582 THR THR A . n 
A 1 547 GLY 547 583 583 GLY GLY A . n 
A 1 548 GLN 548 584 584 GLN GLN A . n 
A 1 549 PRO 549 585 585 PRO PRO A . n 
A 1 550 GLN 550 586 586 GLN GLN A . n 
A 1 551 MET 551 587 587 MET MET A . n 
A 1 552 SER 552 588 588 SER SER A . n 
A 1 553 ALA 553 589 589 ALA ALA A . n 
A 1 554 SER 554 590 590 SER SER A . n 
A 1 555 ALA 555 591 591 ALA ALA A . n 
A 1 556 MET 556 592 592 MET MET A . n 
A 1 557 LEU 557 593 593 LEU LEU A . n 
A 1 558 SER 558 594 594 SER SER A . n 
A 1 559 TYR 559 595 595 TYR TYR A . n 
A 1 560 PHE 560 596 596 PHE PHE A . n 
A 1 561 LYS 561 597 597 LYS LYS A . n 
A 1 562 PRO 562 598 598 PRO PRO A . n 
A 1 563 LEU 563 599 599 LEU LEU A . n 
A 1 564 LEU 564 600 600 LEU LEU A . n 
A 1 565 ASP 565 601 601 ASP ASP A . n 
A 1 566 TRP 566 602 602 TRP TRP A . n 
A 1 567 LEU 567 603 603 LEU LEU A . n 
A 1 568 ARG 568 604 604 ARG ARG A . n 
A 1 569 THR 569 605 605 THR THR A . n 
A 1 570 GLU 570 606 606 GLU GLU A . n 
A 1 571 ASN 571 607 607 ASN ASN A . n 
A 1 572 GLU 572 608 608 GLU GLU A . n 
A 1 573 LEU 573 609 609 LEU LEU A . n 
A 1 574 HIS 574 610 610 HIS HIS A . n 
A 1 575 GLY 575 611 611 GLY GLY A . n 
A 1 576 GLU 576 612 612 GLU GLU A . n 
A 1 577 LYS 577 613 613 LYS LYS A . n 
A 1 578 LEU 578 614 614 LEU LEU A . n 
A 1 579 GLY 579 615 615 GLY GLY A . n 
A 1 580 TRP 580 616 616 TRP TRP A . n 
A 1 581 PRO 581 617 617 PRO PRO A . n 
A 1 582 GLN 582 618 618 GLN GLN A . n 
A 1 583 TYR 583 619 ?   ?   ?   A . n 
A 1 584 ASN 584 620 ?   ?   ?   A . n 
A 1 585 TRP 585 621 ?   ?   ?   A . n 
A 1 586 THR 586 622 ?   ?   ?   A . n 
A 1 587 PRO 587 623 ?   ?   ?   A . n 
A 1 588 ASN 588 624 ?   ?   ?   A . n 
A 1 589 SER 589 625 ?   ?   ?   A . n 
A 1 590 ALA 590 626 ?   ?   ?   A . n 
A 1 591 ARG 591 627 ?   ?   ?   A . n 
A 1 592 SER 592 628 ?   ?   ?   A . n 
A 1 593 GLU 593 629 ?   ?   ?   A . n 
A 1 594 GLY 594 630 ?   ?   ?   A . n 
A 1 595 PRO 595 631 ?   ?   ?   A . n 
A 1 596 LEU 596 632 ?   ?   ?   A . n 
A 1 597 PRO 597 633 ?   ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 NAG 1 B NAG 1 B NAG 1 n 
B 2 NAG 2 B NAG 2 B NAG 2 n 
B 2 BMA 3 B BMA 3 B BMA 3 n 
B 2 MAN 4 B MAN 4 B MAN 4 n 
B 2 NAG 5 B NAG 5 B NAG 5 n 
B 2 MAN 6 B MAN 6 B MAN 6 n 
B 2 NAG 7 B NAG 7 B NAG 7 n 
B 2 FUC 8 B FUC 8 B FUC 8 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 BJ2 ? ? BJ2 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ZN  ? ? ZN  ? ? '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 
C 3 ZN  1   701  701  ZN  ZN  A . 
D 4 NAG 1   702  703  NAG NAG A . 
E 5 CL  1   703  710  CL  CL  A . 
F 5 CL  1   704  711  CL  CL  A . 
G 6 BJ2 1   705  712  BJ2 SG6 A . 
H 7 HOH 1   801  803  HOH HOH A . 
H 7 HOH 2   802  802  HOH HOH A . 
H 7 HOH 3   803  801  HOH HOH A . 
H 7 HOH 4   804  805  HOH HOH A . 
H 7 HOH 5   805  818  HOH HOH A . 
H 7 HOH 6   806  809  HOH HOH A . 
H 7 HOH 7   807  810  HOH HOH A . 
H 7 HOH 8   808  806  HOH HOH A . 
H 7 HOH 9   809  843  HOH HOH A . 
H 7 HOH 10  810  808  HOH HOH A . 
H 7 HOH 11  811  823  HOH HOH A . 
H 7 HOH 12  812  807  HOH HOH A . 
H 7 HOH 13  813  813  HOH HOH A . 
H 7 HOH 14  814  844  HOH HOH A . 
H 7 HOH 15  815  817  HOH HOH A . 
H 7 HOH 16  816  819  HOH HOH A . 
H 7 HOH 17  817  811  HOH HOH A . 
H 7 HOH 18  818  816  HOH HOH A . 
H 7 HOH 19  819  822  HOH HOH A . 
H 7 HOH 20  820  827  HOH HOH A . 
H 7 HOH 21  821  837  HOH HOH A . 
H 7 HOH 22  822  814  HOH HOH A . 
H 7 HOH 23  823  825  HOH HOH A . 
H 7 HOH 24  824  821  HOH HOH A . 
H 7 HOH 25  825  826  HOH HOH A . 
H 7 HOH 26  826  815  HOH HOH A . 
H 7 HOH 27  827  835  HOH HOH A . 
H 7 HOH 28  828  836  HOH HOH A . 
H 7 HOH 29  829  832  HOH HOH A . 
H 7 HOH 30  830  820  HOH HOH A . 
H 7 HOH 31  831  833  HOH HOH A . 
H 7 HOH 32  832  831  HOH HOH A . 
H 7 HOH 33  833  853  HOH HOH A . 
H 7 HOH 34  834  851  HOH HOH A . 
H 7 HOH 35  835  842  HOH HOH A . 
H 7 HOH 36  836  828  HOH HOH A . 
H 7 HOH 37  837  840  HOH HOH A . 
H 7 HOH 38  838  852  HOH HOH A . 
H 7 HOH 39  839  829  HOH HOH A . 
H 7 HOH 40  840  902  HOH HOH A . 
H 7 HOH 41  841  846  HOH HOH A . 
H 7 HOH 42  842  862  HOH HOH A . 
H 7 HOH 43  843  870  HOH HOH A . 
H 7 HOH 44  844  838  HOH HOH A . 
H 7 HOH 45  845  834  HOH HOH A . 
H 7 HOH 46  846  841  HOH HOH A . 
H 7 HOH 47  847  856  HOH HOH A . 
H 7 HOH 48  848  830  HOH HOH A . 
H 7 HOH 49  849  857  HOH HOH A . 
H 7 HOH 50  850  849  HOH HOH A . 
H 7 HOH 51  851  824  HOH HOH A . 
H 7 HOH 52  852  845  HOH HOH A . 
H 7 HOH 53  853  854  HOH HOH A . 
H 7 HOH 54  854  848  HOH HOH A . 
H 7 HOH 55  855  872  HOH HOH A . 
H 7 HOH 56  856  866  HOH HOH A . 
H 7 HOH 57  857  906  HOH HOH A . 
H 7 HOH 58  858  904  HOH HOH A . 
H 7 HOH 59  859  847  HOH HOH A . 
H 7 HOH 60  860  867  HOH HOH A . 
H 7 HOH 61  861  865  HOH HOH A . 
H 7 HOH 62  862  899  HOH HOH A . 
H 7 HOH 63  863  839  HOH HOH A . 
H 7 HOH 64  864  869  HOH HOH A . 
H 7 HOH 65  865  901  HOH HOH A . 
H 7 HOH 66  866  850  HOH HOH A . 
H 7 HOH 67  867  886  HOH HOH A . 
H 7 HOH 68  868  897  HOH HOH A . 
H 7 HOH 69  869  855  HOH HOH A . 
H 7 HOH 70  870  881  HOH HOH A . 
H 7 HOH 71  871  880  HOH HOH A . 
H 7 HOH 72  872  882  HOH HOH A . 
H 7 HOH 73  873  858  HOH HOH A . 
H 7 HOH 74  874  876  HOH HOH A . 
H 7 HOH 75  875  868  HOH HOH A . 
H 7 HOH 76  876  890  HOH HOH A . 
H 7 HOH 77  877  859  HOH HOH A . 
H 7 HOH 78  878  887  HOH HOH A . 
H 7 HOH 79  879  873  HOH HOH A . 
H 7 HOH 80  880  913  HOH HOH A . 
H 7 HOH 81  881  888  HOH HOH A . 
H 7 HOH 82  882  879  HOH HOH A . 
H 7 HOH 83  883  878  HOH HOH A . 
H 7 HOH 84  884  905  HOH HOH A . 
H 7 HOH 85  885  893  HOH HOH A . 
H 7 HOH 86  886  900  HOH HOH A . 
H 7 HOH 87  887  885  HOH HOH A . 
H 7 HOH 88  888  937  HOH HOH A . 
H 7 HOH 89  889  875  HOH HOH A . 
H 7 HOH 90  890  903  HOH HOH A . 
H 7 HOH 91  891  871  HOH HOH A . 
H 7 HOH 92  892  898  HOH HOH A . 
H 7 HOH 93  893  861  HOH HOH A . 
H 7 HOH 94  894  874  HOH HOH A . 
H 7 HOH 95  895  896  HOH HOH A . 
H 7 HOH 96  896  883  HOH HOH A . 
H 7 HOH 97  897  931  HOH HOH A . 
H 7 HOH 98  898  891  HOH HOH A . 
H 7 HOH 99  899  892  HOH HOH A . 
H 7 HOH 100 900  907  HOH HOH A . 
H 7 HOH 101 901  895  HOH HOH A . 
H 7 HOH 102 902  930  HOH HOH A . 
H 7 HOH 103 903  920  HOH HOH A . 
H 7 HOH 104 904  884  HOH HOH A . 
H 7 HOH 105 905  912  HOH HOH A . 
H 7 HOH 106 906  936  HOH HOH A . 
H 7 HOH 107 907  940  HOH HOH A . 
H 7 HOH 108 908  914  HOH HOH A . 
H 7 HOH 109 909  928  HOH HOH A . 
H 7 HOH 110 910  911  HOH HOH A . 
H 7 HOH 111 911  918  HOH HOH A . 
H 7 HOH 112 912  951  HOH HOH A . 
H 7 HOH 113 913  933  HOH HOH A . 
H 7 HOH 114 914  863  HOH HOH A . 
H 7 HOH 115 915  938  HOH HOH A . 
H 7 HOH 116 916  932  HOH HOH A . 
H 7 HOH 117 917  910  HOH HOH A . 
H 7 HOH 118 918  889  HOH HOH A . 
H 7 HOH 119 919  860  HOH HOH A . 
H 7 HOH 120 920  923  HOH HOH A . 
H 7 HOH 121 921  909  HOH HOH A . 
H 7 HOH 122 922  985  HOH HOH A . 
H 7 HOH 123 923  939  HOH HOH A . 
H 7 HOH 124 924  864  HOH HOH A . 
H 7 HOH 125 925  963  HOH HOH A . 
H 7 HOH 126 926  921  HOH HOH A . 
H 7 HOH 127 927  804  HOH HOH A . 
H 7 HOH 128 928  919  HOH HOH A . 
H 7 HOH 129 929  917  HOH HOH A . 
H 7 HOH 130 930  922  HOH HOH A . 
H 7 HOH 131 931  944  HOH HOH A . 
H 7 HOH 132 932  945  HOH HOH A . 
H 7 HOH 133 933  946  HOH HOH A . 
H 7 HOH 134 934  925  HOH HOH A . 
H 7 HOH 135 935  924  HOH HOH A . 
H 7 HOH 136 936  915  HOH HOH A . 
H 7 HOH 137 937  894  HOH HOH A . 
H 7 HOH 138 938  908  HOH HOH A . 
H 7 HOH 139 939  935  HOH HOH A . 
H 7 HOH 140 940  980  HOH HOH A . 
H 7 HOH 141 941  948  HOH HOH A . 
H 7 HOH 142 942  929  HOH HOH A . 
H 7 HOH 143 943  877  HOH HOH A . 
H 7 HOH 144 944  953  HOH HOH A . 
H 7 HOH 145 945  942  HOH HOH A . 
H 7 HOH 146 946  927  HOH HOH A . 
H 7 HOH 147 947  926  HOH HOH A . 
H 7 HOH 148 948  956  HOH HOH A . 
H 7 HOH 149 949  941  HOH HOH A . 
H 7 HOH 150 950  934  HOH HOH A . 
H 7 HOH 151 951  952  HOH HOH A . 
H 7 HOH 152 952  957  HOH HOH A . 
H 7 HOH 153 953  961  HOH HOH A . 
H 7 HOH 154 954  916  HOH HOH A . 
H 7 HOH 155 955  955  HOH HOH A . 
H 7 HOH 156 956  947  HOH HOH A . 
H 7 HOH 157 957  988  HOH HOH A . 
H 7 HOH 158 958  975  HOH HOH A . 
H 7 HOH 159 959  954  HOH HOH A . 
H 7 HOH 160 960  949  HOH HOH A . 
H 7 HOH 161 961  943  HOH HOH A . 
H 7 HOH 162 962  965  HOH HOH A . 
H 7 HOH 163 963  958  HOH HOH A . 
H 7 HOH 164 964  972  HOH HOH A . 
H 7 HOH 165 965  960  HOH HOH A . 
H 7 HOH 166 966  970  HOH HOH A . 
H 7 HOH 167 967  974  HOH HOH A . 
H 7 HOH 168 968  993  HOH HOH A . 
H 7 HOH 169 969  966  HOH HOH A . 
H 7 HOH 170 970  950  HOH HOH A . 
H 7 HOH 171 971  992  HOH HOH A . 
H 7 HOH 172 972  962  HOH HOH A . 
H 7 HOH 173 973  959  HOH HOH A . 
H 7 HOH 174 974  969  HOH HOH A . 
H 7 HOH 175 975  968  HOH HOH A . 
H 7 HOH 176 976  976  HOH HOH A . 
H 7 HOH 177 977  964  HOH HOH A . 
H 7 HOH 178 978  967  HOH HOH A . 
H 7 HOH 179 979  989  HOH HOH A . 
H 7 HOH 180 980  997  HOH HOH A . 
H 7 HOH 181 981  984  HOH HOH A . 
H 7 HOH 182 982  981  HOH HOH A . 
H 7 HOH 183 983  1014 HOH HOH A . 
H 7 HOH 184 984  990  HOH HOH A . 
H 7 HOH 185 985  973  HOH HOH A . 
H 7 HOH 186 986  979  HOH HOH A . 
H 7 HOH 187 987  996  HOH HOH A . 
H 7 HOH 188 988  994  HOH HOH A . 
H 7 HOH 189 989  987  HOH HOH A . 
H 7 HOH 190 990  1006 HOH HOH A . 
H 7 HOH 191 991  983  HOH HOH A . 
H 7 HOH 192 992  982  HOH HOH A . 
H 7 HOH 193 993  971  HOH HOH A . 
H 7 HOH 194 994  977  HOH HOH A . 
H 7 HOH 195 995  1003 HOH HOH A . 
H 7 HOH 196 996  995  HOH HOH A . 
H 7 HOH 197 997  978  HOH HOH A . 
H 7 HOH 198 998  1004 HOH HOH A . 
H 7 HOH 199 999  991  HOH HOH A . 
H 7 HOH 200 1000 999  HOH HOH A . 
H 7 HOH 201 1001 998  HOH HOH A . 
H 7 HOH 202 1002 1009 HOH HOH A . 
H 7 HOH 203 1003 1000 HOH HOH A . 
H 7 HOH 204 1004 1002 HOH HOH A . 
H 7 HOH 205 1005 986  HOH HOH A . 
H 7 HOH 206 1006 1010 HOH HOH A . 
H 7 HOH 207 1007 1008 HOH HOH A . 
H 7 HOH 208 1008 1007 HOH HOH A . 
H 7 HOH 209 1009 1011 HOH HOH A . 
H 7 HOH 210 1010 1013 HOH HOH A . 
H 7 HOH 211 1011 1022 HOH HOH A . 
H 7 HOH 212 1012 1015 HOH HOH A . 
H 7 HOH 213 1013 1012 HOH HOH A . 
H 7 HOH 214 1014 1018 HOH HOH A . 
H 7 HOH 215 1015 1005 HOH HOH A . 
H 7 HOH 216 1016 1019 HOH HOH A . 
H 7 HOH 217 1017 1001 HOH HOH A . 
H 7 HOH 218 1018 1021 HOH HOH A . 
H 7 HOH 219 1019 1017 HOH HOH A . 
H 7 HOH 220 1020 1016 HOH HOH A . 
H 7 HOH 221 1021 1020 HOH HOH A . 
H 7 HOH 222 1022 1023 HOH HOH A . 
H 7 HOH 223 1023 1025 HOH HOH A . 
H 7 HOH 224 1024 1026 HOH HOH A . 
H 7 HOH 225 1025 1024 HOH HOH A . 
H 7 HOH 226 1026 1027 HOH HOH A . 
H 7 HOH 227 1027 1028 HOH HOH A . 
H 7 HOH 228 1028 1029 HOH HOH A . 
H 7 HOH 229 1029 1031 HOH HOH A . 
H 7 HOH 230 1030 1030 HOH HOH A . 
H 7 HOH 231 1031 1032 HOH HOH A . 
H 7 HOH 232 1032 1034 HOH HOH A . 
H 7 HOH 233 1033 1035 HOH HOH A . 
H 7 HOH 234 1034 1033 HOH HOH A . 
H 7 HOH 235 1035 1036 HOH HOH A . 
H 7 HOH 236 1036 1039 HOH HOH A . 
H 7 HOH 237 1037 1040 HOH HOH A . 
H 7 HOH 238 1038 1038 HOH HOH A . 
H 7 HOH 239 1039 1041 HOH HOH A . 
H 7 HOH 240 1040 1037 HOH HOH A . 
H 7 HOH 241 1041 1042 HOH HOH A . 
H 7 HOH 242 1042 1044 HOH HOH A . 
H 7 HOH 243 1043 1043 HOH HOH A . 
H 7 HOH 244 1044 1045 HOH HOH A . 
H 7 HOH 245 1045 812  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A GLN 231 ? CG  ? A GLN 195 CG  
2 1 Y 1 A GLN 231 ? CD  ? A GLN 195 CD  
3 1 Y 1 A GLN 231 ? OE1 ? A GLN 195 OE1 
4 1 Y 1 A GLN 231 ? NE2 ? A GLN 195 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GBO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     56.781 
_cell.length_a_esd                 ? 
_cell.length_b                     84.915 
_cell.length_b_esd                 ? 
_cell.length_c                     135.065 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GBO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_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                   9GBO 
_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             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.97 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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 MIB pH 4.0, 5% glycerol, and 15% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-10-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9763 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GBO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               135.06 
_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                                     44900 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.1 
_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                                0.066 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.988 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.0 
_reflns_shell.d_res_low                                     2.05 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3243 
_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                               0.613 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.753 
_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                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.839 
_refine.aniso_B[1][2]                            -0.000 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            -2.157 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            1.317 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               35.895 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.952 
_refine.correlation_coeff_Fo_to_Fc_free          0.920 
_refine.details                                  'Hydrogens have not been used' 
_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                                 9GBO 
_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                            2.000 
_refine.ls_d_res_low                             67.624 
_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                     44826 
_refine.ls_number_reflns_R_free                  2099 
_refine.ls_number_reflns_R_work                  42727 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.753 
_refine.ls_percent_reflns_R_free                 4.683 
_refine.ls_R_factor_all                          0.199 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2554 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1958 
_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                      0.229 
_refine.ls_wR_factor_R_work                      0.176 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'MASK BULK SOLVENT' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.192 
_refine.pdbx_overall_ESU_R_Free                  0.180 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             13.921 
_refine.overall_SU_ML                            0.164 
_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                    0.9630 
_refine.pdbx_average_fsc_free                    0.9412 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.000 
_refine_hist.d_res_low                        67.624 
_refine_hist.number_atoms_solvent             245 
_refine_hist.number_atoms_total               5089 
_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        4698 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         146 
_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' ? 0.014  0.012  5065 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 2.601  1.837  6915 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.876  5.000  593  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 10.447 5.000  26   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 16.400 10.000 815  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 15.598 10.000 243  ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.168  0.200  749  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  3961 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.228  0.200  2405 ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.323  0.200  3493 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.165  0.200  280  ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.203  0.200  57   ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.214  0.200  15   ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 2.780  2.191  2351 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.790  3.921  2951 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 4.355  2.654  2714 ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 6.192  4.728  3964 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 7.368  26.795 7913 ? r_lrange_it                    ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.000 2.052  3257 . 129 3107 99.3552  . 0.330 . . 0.328 . . . . . 0.317 . 20 . 0.894 0.841 0.376 
'X-RAY DIFFRACTION' 2.052 2.108  3206 . 156 3035 99.5321  . 0.273 . . 0.272 . . . . . 0.264 . 20 . 0.940 0.930 0.301 
'X-RAY DIFFRACTION' 2.108 2.169  3094 . 167 2911 99.4829  . 0.251 . . 0.247 . . . . . 0.238 . 20 . 0.954 0.935 0.311 
'X-RAY DIFFRACTION' 2.169 2.236  3008 . 136 2852 99.3351  . 0.233 . . 0.231 . . . . . 0.219 . 20 . 0.960 0.952 0.258 
'X-RAY DIFFRACTION' 2.236 2.309  2942 . 138 2794 99.6601  . 0.260 . . 0.258 . . . . . 0.241 . 20 . 0.947 0.922 0.314 
'X-RAY DIFFRACTION' 2.309 2.390  2825 . 135 2685 99.8230  . 0.227 . . 0.222 . . . . . 0.205 . 20 . 0.966 0.934 0.324 
'X-RAY DIFFRACTION' 2.390 2.480  2753 . 128 2623 99.9274  . 0.221 . . 0.216 . . . . . 0.198 . 20 . 0.968 0.935 0.307 
'X-RAY DIFFRACTION' 2.480 2.581  2650 . 127 2516 99.7358  . 0.220 . . 0.215 . . . . . 0.193 . 20 . 0.969 0.934 0.323 
'X-RAY DIFFRACTION' 2.581 2.696  2534 . 140 2392 99.9211  . 0.217 . . 0.213 . . . . . 0.191 . 20 . 0.972 0.950 0.286 
'X-RAY DIFFRACTION' 2.696 2.827  2436 . 107 2326 99.8768  . 0.212 . . 0.209 . . . . . 0.188 . 20 . 0.974 0.954 0.257 
'X-RAY DIFFRACTION' 2.827 2.980  2307 . 119 2185 99.8700  . 0.206 . . 0.200 . . . . . 0.181 . 20 . 0.975 0.941 0.318 
'X-RAY DIFFRACTION' 2.980 3.160  2210 . 104 2104 99.9095  . 0.190 . . 0.189 . . . . . 0.173 . 20 . 0.978 0.964 0.224 
'X-RAY DIFFRACTION' 3.160 3.378  2077 . 108 1969 100.0000 . 0.191 . . 0.189 . . . . . 0.178 . 20 . 0.979 0.962 0.231 
'X-RAY DIFFRACTION' 3.378 3.648  1923 . 87  1835 99.9480  . 0.198 . . 0.196 . . . . . 0.185 . 20 . 0.978 0.964 0.252 
'X-RAY DIFFRACTION' 3.648 3.995  1793 . 81  1711 99.9442  . 0.170 . . 0.167 . . . . . 0.160 . 20 . 0.985 0.967 0.237 
'X-RAY DIFFRACTION' 3.995 4.464  1638 . 71  1566 99.9389  . 0.154 . . 0.152 . . . . . 0.147 . 20 . 0.986 0.972 0.195 
'X-RAY DIFFRACTION' 4.464 5.151  1460 . 57  1403 100.0000 . 0.138 . . 0.136 . . . . . 0.132 . 20 . 0.989 0.982 0.174 
'X-RAY DIFFRACTION' 5.151 6.300  1240 . 48  1191 99.9194  . 0.158 . . 0.155 . . . . . 0.149 . 20 . 0.987 0.976 0.225 
'X-RAY DIFFRACTION' 6.300 8.871  980  . 29  951  100.0000 . 0.150 . . 0.148 . . . . . 0.144 . 20 . 0.988 0.975 0.201 
'X-RAY DIFFRACTION' 8.871 67.624 603  . 32  571  100.0000 . 0.189 . . 0.189 . . . . . 0.179 . 20 . 0.965 0.974 0.183 
# 
_struct.entry_id                     9GBO 
_struct.title                        'Human Angiotensin-1 converting enzyme C-domain in complex with a diprolyl inhibitor- SG16' 
_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        9GBO 
_struct_keywords.text            'Inhibitor, complex, protease, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 6 ? 
H N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ACE_HUMAN 
_struct_ref.pdbx_db_accession          P12821 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARKFDVNQLQNTTIKRII
KKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQF
YPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLG
NMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASA
WDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSE
GGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPS
SVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSYF
KPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLP
;
_struct_ref.pdbx_align_begin           642 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9GBO 
_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                 597 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P12821 
_struct_ref_seq.db_align_beg                  642 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1238 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       37 
_struct_ref_seq.pdbx_auth_seq_align_end       633 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GBO GLY A 28  ? UNP P12821 GLU 669  'engineered mutation' 64  1 
1 9GBO GLN A 54  ? UNP P12821 ASN 695  'engineered mutation' 90  2 
1 9GBO GLN A 119 ? UNP P12821 ASN 760  'engineered mutation' 155 3 
1 9GBO GLN A 301 ? UNP P12821 ASN 942  'engineered mutation' 337 4 
1 9GBO GLN A 550 ? UNP P12821 ASN 1191 'engineered mutation' 586 5 
# 
_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)' 2650  ? 
1 MORE         11    ? 
1 'SSA (A^2)'  24290 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 ASP A 4   ? THR A 35  ? ASP A 40  THR A 71  1 ? 32 
HELX_P HELX_P2  AA2 THR A 38  ? LYS A 65  ? THR A 74  LYS A 101 1 ? 28 
HELX_P HELX_P3  AA3 ASN A 73  ? GLN A 84  ? ASN A 109 GLN A 120 1 ? 12 
HELX_P HELX_P4  AA4 LEU A 86  ? LEU A 91  ? LEU A 122 LEU A 127 5 ? 6  
HELX_P HELX_P5  AA5 PRO A 92  ? ALA A 113 ? PRO A 128 ALA A 149 1 ? 22 
HELX_P HELX_P6  AA6 PRO A 127 ? SER A 136 ? PRO A 163 SER A 172 1 ? 10 
HELX_P HELX_P7  AA7 LYS A 138 ? ALA A 153 ? LYS A 174 ALA A 189 1 ? 16 
HELX_P HELX_P8  AA8 ALA A 153 ? GLN A 159 ? ALA A 189 GLN A 195 1 ? 7  
HELX_P HELX_P9  AA9 PHE A 160 ? ASN A 175 ? PHE A 196 ASN A 211 1 ? 16 
HELX_P HELX_P10 AB1 ASP A 179 ? MET A 187 ? ASP A 215 MET A 223 1 ? 9  
HELX_P HELX_P11 AB2 SER A 192 ? LEU A 204 ? SER A 228 LEU A 240 1 ? 13 
HELX_P HELX_P12 AB3 LEU A 204 ? GLY A 224 ? LEU A 240 GLY A 260 1 ? 21 
HELX_P HELX_P13 AB4 ALA A 225 ? ILE A 228 ? ALA A 261 ILE A 264 5 ? 4  
HELX_P HELX_P14 AB5 TRP A 247 ? ASN A 249 ? TRP A 283 ASN A 285 5 ? 3  
HELX_P HELX_P15 AB6 ILE A 250 ? VAL A 255 ? ILE A 286 VAL A 291 1 ? 6  
HELX_P HELX_P16 AB7 ASP A 264 ? GLN A 272 ? ASP A 300 GLN A 308 1 ? 9  
HELX_P HELX_P17 AB8 THR A 275 ? LEU A 290 ? THR A 311 LEU A 326 1 ? 16 
HELX_P HELX_P18 AB9 PRO A 296 ? SER A 303 ? PRO A 332 SER A 339 1 ? 8  
HELX_P HELX_P19 AC1 ASN A 338 ? TYR A 358 ? ASN A 374 TYR A 394 1 ? 21 
HELX_P HELX_P20 AC2 PRO A 362 ? ARG A 366 ? PRO A 398 ARG A 402 5 ? 5  
HELX_P HELX_P21 AC3 ASN A 370 ? SER A 386 ? ASN A 406 SER A 422 1 ? 17 
HELX_P HELX_P22 AC4 THR A 387 ? LEU A 394 ? THR A 423 LEU A 430 1 ? 8  
HELX_P HELX_P23 AC5 SER A 403 ? ILE A 419 ? SER A 439 ILE A 455 1 ? 17 
HELX_P HELX_P24 AC6 ALA A 420 ? ASP A 437 ? ALA A 456 ASP A 473 1 ? 18 
HELX_P HELX_P25 AC7 ASN A 444 ? GLY A 458 ? ASN A 480 GLY A 494 1 ? 15 
HELX_P HELX_P26 AC8 PHE A 470 ? LYS A 475 ? PHE A 506 LYS A 511 5 ? 6  
HELX_P HELX_P27 AC9 TYR A 484 ? ALA A 505 ? TYR A 520 ALA A 541 1 ? 22 
HELX_P HELX_P28 AD1 PRO A 510 ? CYS A 514 ? PRO A 546 CYS A 550 5 ? 5  
HELX_P HELX_P29 AD2 SER A 519 ? LEU A 532 ? SER A 555 LEU A 568 1 ? 14 
HELX_P HELX_P30 AD3 PRO A 537 ? GLY A 547 ? PRO A 573 GLY A 583 1 ? 11 
HELX_P HELX_P31 AD4 ALA A 553 ? HIS A 574 ? ALA A 589 HIS A 610 1 ? 22 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 116 SG  ? ? ? 1_555 A CYS 122 SG  ? ? A CYS 152 A CYS 158 1_555 ? ? ? ? ? ? ? 2.086 ? ?               
disulf2 disulf ?    ? A CYS 316 SG  ? ? ? 1_555 A CYS 334 SG  ? ? A CYS 352 A CYS 370 1_555 ? ? ? ? ? ? ? 2.101 ? ?               
disulf3 disulf ?    ? A CYS 502 SG  ? ? ? 1_555 A CYS 514 SG  ? ? A CYS 538 A CYS 550 1_555 ? ? ? ? ? ? ? 2.061 ? ?               
covale1 covale one  ? A ASN 36  ND2 ? ? ? 1_555 D NAG .   C1  ? ? A ASN 72  A NAG 702 1_555 ? ? ? ? ? ? ? 1.433 ? N-Glycosylation 
covale2 covale one  ? A ASN 73  ND2 ? ? ? 1_555 B NAG .   C1  ? ? A ASN 109 B NAG 1   1_555 ? ? ? ? ? ? ? 1.460 ? N-Glycosylation 
covale3 covale both ? B NAG .   O4  ? ? ? 1_555 B NAG .   C1  ? ? B NAG 1   B NAG 2   1_555 ? ? ? ? ? ? ? 1.389 ? ?               
covale4 covale both ? B NAG .   O6  ? ? ? 1_555 B FUC .   C1  ? ? B NAG 1   B FUC 8   1_555 ? ? ? ? ? ? ? 1.409 ? ?               
covale5 covale both ? B NAG .   O4  ? ? ? 1_555 B BMA .   C1  ? ? B NAG 2   B BMA 3   1_555 ? ? ? ? ? ? ? 1.388 ? ?               
covale6 covale both ? B BMA .   O3  ? ? ? 1_555 B MAN .   C1  ? ? B BMA 3   B MAN 4   1_555 ? ? ? ? ? ? ? 1.406 ? ?               
covale7 covale both ? B BMA .   O6  ? ? ? 1_555 B MAN .   C1  ? ? B BMA 3   B MAN 6   1_555 ? ? ? ? ? ? ? 1.410 ? ?               
covale8 covale both ? B MAN .   O2  ? ? ? 1_555 B NAG .   C1  ? ? B MAN 4   B NAG 5   1_555 ? ? ? ? ? ? ? 1.391 ? ?               
covale9 covale both ? B MAN .   O2  ? ? ? 1_555 B NAG .   C1  ? ? B MAN 6   B NAG 7   1_555 ? ? ? ? ? ? ? 1.400 ? ?               
metalc1 metalc ?    ? A HIS 347 NE2 ? ? ? 1_555 C ZN  .   ZN  ? ? A HIS 383 A ZN  701 1_555 ? ? ? ? ? ? ? 1.991 ? ?               
metalc2 metalc ?    ? A HIS 351 NE2 ? ? ? 1_555 C ZN  .   ZN  ? ? A HIS 387 A ZN  701 1_555 ? ? ? ? ? ? ? 1.924 ? ?               
metalc3 metalc ?    ? A GLU 375 OE1 ? ? ? 1_555 C ZN  .   ZN  ? ? A GLU 411 A ZN  701 1_555 ? ? ? ? ? ? ? 1.957 ? ?               
metalc4 metalc ?    ? C ZN  .   ZN  ? ? ? 1_555 G BJ2 .   O07 ? ? A ZN  701 A BJ2 705 1_555 ? ? ? ? ? ? ? 2.014 ? ?               
metalc5 metalc ?    ? C ZN  .   ZN  ? ? ? 1_555 G BJ2 .   O06 ? ? A ZN  701 A BJ2 705 1_555 ? ? ? ? ? ? ? 2.659 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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  NE2 ? A HIS 347 ? A HIS 383 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 NE2 ? A HIS 351 ? A HIS 387 ? 1_555 109.8 ? 
2  NE2 ? A HIS 347 ? A HIS 383 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 OE1 ? A GLU 375 ? A GLU 411 ? 1_555 92.5  ? 
3  NE2 ? A HIS 351 ? A HIS 387 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 OE1 ? A GLU 375 ? A GLU 411 ? 1_555 111.7 ? 
4  NE2 ? A HIS 347 ? A HIS 383 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O07 ? G BJ2 .   ? A BJ2 705 ? 1_555 118.6 ? 
5  NE2 ? A HIS 351 ? A HIS 387 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O07 ? G BJ2 .   ? A BJ2 705 ? 1_555 121.5 ? 
6  OE1 ? A GLU 375 ? A GLU 411 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O07 ? G BJ2 .   ? A BJ2 705 ? 1_555 97.5  ? 
7  NE2 ? A HIS 347 ? A HIS 383 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O06 ? G BJ2 .   ? A BJ2 705 ? 1_555 91.3  ? 
8  NE2 ? A HIS 351 ? A HIS 387 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O06 ? G BJ2 .   ? A BJ2 705 ? 1_555 96.1  ? 
9  OE1 ? A GLU 375 ? A GLU 411 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O06 ? G BJ2 .   ? A BJ2 705 ? 1_555 148.7 ? 
10 O07 ? G BJ2 .   ? A BJ2 705 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O06 ? G BJ2 .   ? A BJ2 705 ? 1_555 54.1  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG B .   ? ASN A 73  ? NAG B 1   ? 1_555 ASN A 109 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG D .   ? ASN A 36  ? NAG A 702 ? 1_555 ASN A 72  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 CYS A 116 ? CYS A 122 ? CYS A 152 ? 1_555 CYS A 158 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4 CYS A 316 ? CYS A 334 ? CYS A 352 ? 1_555 CYS A 370 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5 CYS A 502 ? CYS A 514 ? CYS A 538 ? 1_555 CYS A 550 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           126 
_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           GLU 
_struct_mon_prot_cis.auth_seq_id            162 
_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    127 
_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     163 
_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       3.16 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 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 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 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 115 ? CYS A 116 ? VAL A 151 CYS A 152 
AA1 2 CYS A 122 ? LEU A 123 ? CYS A 158 LEU A 159 
AA2 1 ILE A 234 ? PRO A 235 ? ILE A 270 PRO A 271 
AA2 2 LEU A 459 ? CYS A 460 ? LEU A 495 CYS A 496 
AA3 1 SER A 319 ? ASP A 322 ? SER A 355 ASP A 358 
AA3 2 PHE A 329 ? LYS A 332 ? PHE A 365 LYS A 368 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 115 ? N VAL A 151 O LEU A 123 ? O LEU A 159 
AA2 1 2 N ILE A 234 ? N ILE A 270 O CYS A 460 ? O CYS A 496 
AA3 1 2 N TRP A 321 ? N TRP A 357 O ARG A 330 ? O ARG A 366 
# 
_pdbx_entry_details.entry_id                   9GBO 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 O A HOH 993 ? ? O   A HOH 1027 ? ? 2.08 
2 1 O A ASN 66  ? ? ND2 A ASN 70   ? ? 2.13 
3 1 O A HOH 896 ? ? O   A HOH 1011 ? ? 2.17 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CB  A ARG 53  ? ? CA A ARG 53  ? ? C   A ARG 53  ? ? 97.08  110.40 -13.32 2.00 N 
2  1 CG  A ARG 53  ? ? CD A ARG 53  ? ? NE  A ARG 53  ? ? 96.72  111.80 -15.08 2.10 N 
3  1 CB  A LEU 81  ? ? CG A LEU 81  ? ? CD2 A LEU 81  ? ? 122.80 111.00 11.80  1.70 N 
4  1 N   A LEU 82  ? ? CA A LEU 82  ? ? CB  A LEU 82  ? ? 123.52 110.40 13.12  2.00 N 
5  1 CG  A MET 86  ? ? SD A MET 86  ? ? CE  A MET 86  ? ? 113.57 100.20 13.37  1.60 N 
6  1 CB  A GLN 90  ? ? CA A GLN 90  ? ? C   A GLN 90  ? ? 97.81  110.40 -12.59 2.00 N 
7  1 CD  A LYS 94  ? ? CE A LYS 94  ? ? NZ  A LYS 94  ? ? 89.85  111.70 -21.85 2.30 N 
8  1 N   A GLN 98  ? ? CA A GLN 98  ? ? CB  A GLN 98  ? ? 122.33 110.60 11.73  1.80 N 
9  1 OG1 A THR 166 ? ? CB A THR 166 ? ? CG2 A THR 166 ? ? 91.39  110.00 -18.61 2.30 N 
10 1 CA  A THR 166 ? ? CB A THR 166 ? ? OG1 A THR 166 ? ? 94.05  109.00 -14.95 2.10 N 
11 1 NE  A ARG 173 ? ? CZ A ARG 173 ? ? NH1 A ARG 173 ? ? 117.24 120.30 -3.06  0.50 N 
12 1 NE  A ARG 173 ? ? CZ A ARG 173 ? ? NH2 A ARG 173 ? ? 123.56 120.30 3.26   0.50 N 
13 1 NE  A ARG 186 ? ? CZ A ARG 186 ? ? NH2 A ARG 186 ? ? 123.69 120.30 3.39   0.50 N 
14 1 NE  A ARG 191 ? ? CZ A ARG 191 ? ? NH1 A ARG 191 ? ? 115.02 120.30 -5.28  0.50 N 
15 1 NE  A ARG 191 ? ? CZ A ARG 191 ? ? NH2 A ARG 191 ? ? 124.01 120.30 3.71   0.50 N 
16 1 NE  A ARG 257 ? ? CZ A ARG 257 ? ? NH2 A ARG 257 ? ? 116.29 120.30 -4.01  0.50 N 
17 1 CG  A MET 305 ? ? SD A MET 305 ? ? CE  A MET 305 ? ? 87.79  100.20 -12.41 1.60 N 
18 1 CG  A MET 315 ? ? SD A MET 315 ? ? CE  A MET 315 ? ? 115.49 100.20 15.29  1.60 N 
19 1 CG  A MET 340 ? ? SD A MET 340 ? ? CE  A MET 340 ? ? 115.96 100.20 15.76  1.60 N 
20 1 CB  A GLU 342 ? ? CA A GLU 342 ? ? C   A GLU 342 ? ? 89.10  110.40 -21.30 2.00 N 
21 1 CA  A THR 372 ? ? CB A THR 372 ? ? OG1 A THR 372 ? ? 96.31  109.00 -12.69 2.10 N 
22 1 NE  A ARG 501 ? ? CZ A ARG 501 ? ? NH2 A ARG 501 ? ? 117.25 120.30 -3.05  0.50 N 
23 1 N   A PRO 585 ? ? CA A PRO 585 ? ? CB  A PRO 585 ? ? 94.90  103.30 -8.40  1.20 N 
24 1 N   A GLN 586 ? ? CA A GLN 586 ? ? CB  A GLN 586 ? ? 97.98  110.60 -12.62 1.80 N 
25 1 NE  A ARG 604 ? ? CZ A ARG 604 ? ? NH2 A ARG 604 ? ? 116.53 120.30 -3.77  0.50 N 
26 1 N   A LEU 609 ? ? CA A LEU 609 ? ? CB  A LEU 609 ? ? 95.04  110.40 -15.36 2.00 N 
27 1 CB  A LEU 609 ? ? CG A LEU 609 ? ? CD1 A LEU 609 ? ? 100.73 111.00 -10.27 1.70 N 
28 1 CB  A LEU 609 ? ? CG A LEU 609 ? ? CD2 A LEU 609 ? ? 99.77  111.00 -11.23 1.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 72  ? ? 156.49  59.76   
2  1 GLN A 108 ? ? -79.94  -86.47  
3  1 ASN A 109 ? ? -27.45  128.97  
4  1 GLU A 123 ? ? 42.37   -128.60 
5  1 GLN A 155 ? ? 36.12   60.97   
6  1 LYS A 343 ? ? -37.18  132.38  
7  1 HIS A 353 ? ? -21.81  120.80  
8  1 LYS A 363 ? ? -147.03 -23.72  
9  1 PHE A 506 ? ? -152.62 70.93   
10 1 GLN A 554 ? ? 81.91   4.36    
11 1 TRP A 616 ? ? -151.61 66.23   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 191 ? ? 0.091 'SIDE CHAIN' 
2 1 ARG A 235 ? ? 0.173 'SIDE CHAIN' 
3 1 ARG A 252 ? ? 0.095 'SIDE CHAIN' 
4 1 ARG A 314 ? ? 0.117 'SIDE CHAIN' 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         12.5941 
_pdbx_refine_tls.origin_y         5.3092 
_pdbx_refine_tls.origin_z         23.8336 
_pdbx_refine_tls.T[1][1]          0.0451 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0234 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0004 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0426 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0105 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0162 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.0241 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0480 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0103 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.9461 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.5528 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.1213 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0516 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1797 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0639 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.1371 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0604 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0818 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0749 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1023 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0088 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    Ap 
_pdbx_refine_tls_group.beg_auth_seq_id     40 
_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    Ap 
_pdbx_refine_tls_group.end_auth_seq_id     1045 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ALL 
_pdbx_refine_tls_group.selection_details   ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A LEU 37  ? A LEU 1   
2  1 Y 1 A VAL 38  ? A VAL 2   
3  1 Y 1 A THR 39  ? A THR 3   
4  1 Y 1 A GLU 436 ? A GLU 400 
5  1 Y 1 A GLY 437 ? A GLY 401 
6  1 Y 1 A TYR 619 ? A TYR 583 
7  1 Y 1 A ASN 620 ? A ASN 584 
8  1 Y 1 A TRP 621 ? A TRP 585 
9  1 Y 1 A THR 622 ? A THR 586 
10 1 Y 1 A PRO 623 ? A PRO 587 
11 1 Y 1 A ASN 624 ? A ASN 588 
12 1 Y 1 A SER 625 ? A SER 589 
13 1 Y 1 A ALA 626 ? A ALA 590 
14 1 Y 1 A ARG 627 ? A ARG 591 
15 1 Y 1 A SER 628 ? A SER 592 
16 1 Y 1 A GLU 629 ? A GLU 593 
17 1 Y 1 A GLY 630 ? A GLY 594 
18 1 Y 1 A PRO 631 ? A PRO 595 
19 1 Y 1 A LEU 632 ? A LEU 596 
20 1 Y 1 A PRO 633 ? A PRO 597 
# 
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  
BJ2 C01  C  N N 74  
BJ2 C02  C  N S 75  
BJ2 C04  C  N S 76  
BJ2 C05  C  N N 77  
BJ2 C08  C  N S 78  
BJ2 C09  C  N N 79  
BJ2 C10  C  N N 80  
BJ2 C11  C  N N 81  
BJ2 C13  C  N N 82  
BJ2 C15  C  N S 83  
BJ2 C17  C  N N 84  
BJ2 C18  C  N N 85  
BJ2 C21  C  N N 86  
BJ2 C24  C  N N 87  
BJ2 C25  C  N N 88  
BJ2 C26  C  N N 89  
BJ2 C27  C  N S 90  
BJ2 C28  C  N N 91  
BJ2 N03  N  N N 92  
BJ2 N12  N  N N 93  
BJ2 N16  N  N N 94  
BJ2 N23  N  N N 95  
BJ2 O06  O  N N 96  
BJ2 O07  O  N N 97  
BJ2 O14  O  N N 98  
BJ2 O19  O  N N 99  
BJ2 O20  O  N N 100 
BJ2 O22  O  N N 101 
BJ2 O29  O  N N 102 
BJ2 O30  O  N N 103 
BJ2 H011 H  N N 104 
BJ2 H013 H  N N 105 
BJ2 H012 H  N N 106 
BJ2 H021 H  N N 107 
BJ2 H041 H  N N 108 
BJ2 H081 H  N N 109 
BJ2 H091 H  N N 110 
BJ2 H092 H  N N 111 
BJ2 H101 H  N N 112 
BJ2 H102 H  N N 113 
BJ2 H112 H  N N 114 
BJ2 H111 H  N N 115 
BJ2 H151 H  N N 116 
BJ2 H172 H  N N 117 
BJ2 H171 H  N N 118 
BJ2 H242 H  N N 119 
BJ2 H241 H  N N 120 
BJ2 H251 H  N N 121 
BJ2 H252 H  N N 122 
BJ2 H262 H  N N 123 
BJ2 H261 H  N N 124 
BJ2 H271 H  N N 125 
BJ2 H031 H  N N 126 
BJ2 H162 H  N N 127 
BJ2 H161 H  N N 128 
BJ2 H3   H  N N 129 
BJ2 H4   H  N N 130 
BJ2 H5   H  N N 131 
BMA C1   C  N R 132 
BMA C2   C  N S 133 
BMA C3   C  N S 134 
BMA C4   C  N S 135 
BMA C5   C  N R 136 
BMA C6   C  N N 137 
BMA O1   O  N N 138 
BMA O2   O  N N 139 
BMA O3   O  N N 140 
BMA O4   O  N N 141 
BMA O5   O  N N 142 
BMA O6   O  N N 143 
BMA H1   H  N N 144 
BMA H2   H  N N 145 
BMA H3   H  N N 146 
BMA H4   H  N N 147 
BMA H5   H  N N 148 
BMA H61  H  N N 149 
BMA H62  H  N N 150 
BMA HO1  H  N N 151 
BMA HO2  H  N N 152 
BMA HO3  H  N N 153 
BMA HO4  H  N N 154 
BMA HO6  H  N N 155 
CL  CL   CL N N 156 
CYS N    N  N N 157 
CYS CA   C  N R 158 
CYS C    C  N N 159 
CYS O    O  N N 160 
CYS CB   C  N N 161 
CYS SG   S  N N 162 
CYS OXT  O  N N 163 
CYS H    H  N N 164 
CYS H2   H  N N 165 
CYS HA   H  N N 166 
CYS HB2  H  N N 167 
CYS HB3  H  N N 168 
CYS HG   H  N N 169 
CYS HXT  H  N N 170 
FUC C1   C  N R 171 
FUC C2   C  N S 172 
FUC C3   C  N R 173 
FUC C4   C  N S 174 
FUC C5   C  N S 175 
FUC C6   C  N N 176 
FUC O1   O  N N 177 
FUC O2   O  N N 178 
FUC O3   O  N N 179 
FUC O4   O  N N 180 
FUC O5   O  N N 181 
FUC H1   H  N N 182 
FUC H2   H  N N 183 
FUC H3   H  N N 184 
FUC H4   H  N N 185 
FUC H5   H  N N 186 
FUC H61  H  N N 187 
FUC H62  H  N N 188 
FUC H63  H  N N 189 
FUC HO1  H  N N 190 
FUC HO2  H  N N 191 
FUC HO3  H  N N 192 
FUC HO4  H  N N 193 
GLN N    N  N N 194 
GLN CA   C  N S 195 
GLN C    C  N N 196 
GLN O    O  N N 197 
GLN CB   C  N N 198 
GLN CG   C  N N 199 
GLN CD   C  N N 200 
GLN OE1  O  N N 201 
GLN NE2  N  N N 202 
GLN OXT  O  N N 203 
GLN H    H  N N 204 
GLN H2   H  N N 205 
GLN HA   H  N N 206 
GLN HB2  H  N N 207 
GLN HB3  H  N N 208 
GLN HG2  H  N N 209 
GLN HG3  H  N N 210 
GLN HE21 H  N N 211 
GLN HE22 H  N N 212 
GLN HXT  H  N N 213 
GLU N    N  N N 214 
GLU CA   C  N S 215 
GLU C    C  N N 216 
GLU O    O  N N 217 
GLU CB   C  N N 218 
GLU CG   C  N N 219 
GLU CD   C  N N 220 
GLU OE1  O  N N 221 
GLU OE2  O  N N 222 
GLU OXT  O  N N 223 
GLU H    H  N N 224 
GLU H2   H  N N 225 
GLU HA   H  N N 226 
GLU HB2  H  N N 227 
GLU HB3  H  N N 228 
GLU HG2  H  N N 229 
GLU HG3  H  N N 230 
GLU HE2  H  N N 231 
GLU HXT  H  N N 232 
GLY N    N  N N 233 
GLY CA   C  N N 234 
GLY C    C  N N 235 
GLY O    O  N N 236 
GLY OXT  O  N N 237 
GLY H    H  N N 238 
GLY H2   H  N N 239 
GLY HA2  H  N N 240 
GLY HA3  H  N N 241 
GLY HXT  H  N N 242 
HIS N    N  N N 243 
HIS CA   C  N S 244 
HIS C    C  N N 245 
HIS O    O  N N 246 
HIS CB   C  N N 247 
HIS CG   C  Y N 248 
HIS ND1  N  Y N 249 
HIS CD2  C  Y N 250 
HIS CE1  C  Y N 251 
HIS NE2  N  Y N 252 
HIS OXT  O  N N 253 
HIS H    H  N N 254 
HIS H2   H  N N 255 
HIS HA   H  N N 256 
HIS HB2  H  N N 257 
HIS HB3  H  N N 258 
HIS HD1  H  N N 259 
HIS HD2  H  N N 260 
HIS HE1  H  N N 261 
HIS HE2  H  N N 262 
HIS HXT  H  N N 263 
HOH O    O  N N 264 
HOH H1   H  N N 265 
HOH H2   H  N N 266 
ILE N    N  N N 267 
ILE CA   C  N S 268 
ILE C    C  N N 269 
ILE O    O  N N 270 
ILE CB   C  N S 271 
ILE CG1  C  N N 272 
ILE CG2  C  N N 273 
ILE CD1  C  N N 274 
ILE OXT  O  N N 275 
ILE H    H  N N 276 
ILE H2   H  N N 277 
ILE HA   H  N N 278 
ILE HB   H  N N 279 
ILE HG12 H  N N 280 
ILE HG13 H  N N 281 
ILE HG21 H  N N 282 
ILE HG22 H  N N 283 
ILE HG23 H  N N 284 
ILE HD11 H  N N 285 
ILE HD12 H  N N 286 
ILE HD13 H  N N 287 
ILE HXT  H  N N 288 
LEU N    N  N N 289 
LEU CA   C  N S 290 
LEU C    C  N N 291 
LEU O    O  N N 292 
LEU CB   C  N N 293 
LEU CG   C  N N 294 
LEU CD1  C  N N 295 
LEU CD2  C  N N 296 
LEU OXT  O  N N 297 
LEU H    H  N N 298 
LEU H2   H  N N 299 
LEU HA   H  N N 300 
LEU HB2  H  N N 301 
LEU HB3  H  N N 302 
LEU HG   H  N N 303 
LEU HD11 H  N N 304 
LEU HD12 H  N N 305 
LEU HD13 H  N N 306 
LEU HD21 H  N N 307 
LEU HD22 H  N N 308 
LEU HD23 H  N N 309 
LEU HXT  H  N N 310 
LYS N    N  N N 311 
LYS CA   C  N S 312 
LYS C    C  N N 313 
LYS O    O  N N 314 
LYS CB   C  N N 315 
LYS CG   C  N N 316 
LYS CD   C  N N 317 
LYS CE   C  N N 318 
LYS NZ   N  N N 319 
LYS OXT  O  N N 320 
LYS H    H  N N 321 
LYS H2   H  N N 322 
LYS HA   H  N N 323 
LYS HB2  H  N N 324 
LYS HB3  H  N N 325 
LYS HG2  H  N N 326 
LYS HG3  H  N N 327 
LYS HD2  H  N N 328 
LYS HD3  H  N N 329 
LYS HE2  H  N N 330 
LYS HE3  H  N N 331 
LYS HZ1  H  N N 332 
LYS HZ2  H  N N 333 
LYS HZ3  H  N N 334 
LYS HXT  H  N N 335 
MAN C1   C  N S 336 
MAN C2   C  N S 337 
MAN C3   C  N S 338 
MAN C4   C  N S 339 
MAN C5   C  N R 340 
MAN C6   C  N N 341 
MAN O1   O  N N 342 
MAN O2   O  N N 343 
MAN O3   O  N N 344 
MAN O4   O  N N 345 
MAN O5   O  N N 346 
MAN O6   O  N N 347 
MAN H1   H  N N 348 
MAN H2   H  N N 349 
MAN H3   H  N N 350 
MAN H4   H  N N 351 
MAN H5   H  N N 352 
MAN H61  H  N N 353 
MAN H62  H  N N 354 
MAN HO1  H  N N 355 
MAN HO2  H  N N 356 
MAN HO3  H  N N 357 
MAN HO4  H  N N 358 
MAN HO6  H  N N 359 
MET N    N  N N 360 
MET CA   C  N S 361 
MET C    C  N N 362 
MET O    O  N N 363 
MET CB   C  N N 364 
MET CG   C  N N 365 
MET SD   S  N N 366 
MET CE   C  N N 367 
MET OXT  O  N N 368 
MET H    H  N N 369 
MET H2   H  N N 370 
MET HA   H  N N 371 
MET HB2  H  N N 372 
MET HB3  H  N N 373 
MET HG2  H  N N 374 
MET HG3  H  N N 375 
MET HE1  H  N N 376 
MET HE2  H  N N 377 
MET HE3  H  N N 378 
MET HXT  H  N N 379 
NAG C1   C  N R 380 
NAG C2   C  N R 381 
NAG C3   C  N R 382 
NAG C4   C  N S 383 
NAG C5   C  N R 384 
NAG C6   C  N N 385 
NAG C7   C  N N 386 
NAG C8   C  N N 387 
NAG N2   N  N N 388 
NAG O1   O  N N 389 
NAG O3   O  N N 390 
NAG O4   O  N N 391 
NAG O5   O  N N 392 
NAG O6   O  N N 393 
NAG O7   O  N N 394 
NAG H1   H  N N 395 
NAG H2   H  N N 396 
NAG H3   H  N N 397 
NAG H4   H  N N 398 
NAG H5   H  N N 399 
NAG H61  H  N N 400 
NAG H62  H  N N 401 
NAG H81  H  N N 402 
NAG H82  H  N N 403 
NAG H83  H  N N 404 
NAG HN2  H  N N 405 
NAG HO1  H  N N 406 
NAG HO3  H  N N 407 
NAG HO4  H  N N 408 
NAG HO6  H  N N 409 
PHE N    N  N N 410 
PHE CA   C  N S 411 
PHE C    C  N N 412 
PHE O    O  N N 413 
PHE CB   C  N N 414 
PHE CG   C  Y N 415 
PHE CD1  C  Y N 416 
PHE CD2  C  Y N 417 
PHE CE1  C  Y N 418 
PHE CE2  C  Y N 419 
PHE CZ   C  Y N 420 
PHE OXT  O  N N 421 
PHE H    H  N N 422 
PHE H2   H  N N 423 
PHE HA   H  N N 424 
PHE HB2  H  N N 425 
PHE HB3  H  N N 426 
PHE HD1  H  N N 427 
PHE HD2  H  N N 428 
PHE HE1  H  N N 429 
PHE HE2  H  N N 430 
PHE HZ   H  N N 431 
PHE HXT  H  N N 432 
PRO N    N  N N 433 
PRO CA   C  N S 434 
PRO C    C  N N 435 
PRO O    O  N N 436 
PRO CB   C  N N 437 
PRO CG   C  N N 438 
PRO CD   C  N N 439 
PRO OXT  O  N N 440 
PRO H    H  N N 441 
PRO HA   H  N N 442 
PRO HB2  H  N N 443 
PRO HB3  H  N N 444 
PRO HG2  H  N N 445 
PRO HG3  H  N N 446 
PRO HD2  H  N N 447 
PRO HD3  H  N N 448 
PRO HXT  H  N N 449 
SER N    N  N N 450 
SER CA   C  N S 451 
SER C    C  N N 452 
SER O    O  N N 453 
SER CB   C  N N 454 
SER OG   O  N N 455 
SER OXT  O  N N 456 
SER H    H  N N 457 
SER H2   H  N N 458 
SER HA   H  N N 459 
SER HB2  H  N N 460 
SER HB3  H  N N 461 
SER HG   H  N N 462 
SER HXT  H  N N 463 
THR N    N  N N 464 
THR CA   C  N S 465 
THR C    C  N N 466 
THR O    O  N N 467 
THR CB   C  N R 468 
THR OG1  O  N N 469 
THR CG2  C  N N 470 
THR OXT  O  N N 471 
THR H    H  N N 472 
THR H2   H  N N 473 
THR HA   H  N N 474 
THR HB   H  N N 475 
THR HG1  H  N N 476 
THR HG21 H  N N 477 
THR HG22 H  N N 478 
THR HG23 H  N N 479 
THR HXT  H  N N 480 
TRP N    N  N N 481 
TRP CA   C  N S 482 
TRP C    C  N N 483 
TRP O    O  N N 484 
TRP CB   C  N N 485 
TRP CG   C  Y N 486 
TRP CD1  C  Y N 487 
TRP CD2  C  Y N 488 
TRP NE1  N  Y N 489 
TRP CE2  C  Y N 490 
TRP CE3  C  Y N 491 
TRP CZ2  C  Y N 492 
TRP CZ3  C  Y N 493 
TRP CH2  C  Y N 494 
TRP OXT  O  N N 495 
TRP H    H  N N 496 
TRP H2   H  N N 497 
TRP HA   H  N N 498 
TRP HB2  H  N N 499 
TRP HB3  H  N N 500 
TRP HD1  H  N N 501 
TRP HE1  H  N N 502 
TRP HE3  H  N N 503 
TRP HZ2  H  N N 504 
TRP HZ3  H  N N 505 
TRP HH2  H  N N 506 
TRP HXT  H  N N 507 
TYR N    N  N N 508 
TYR CA   C  N S 509 
TYR C    C  N N 510 
TYR O    O  N N 511 
TYR CB   C  N N 512 
TYR CG   C  Y N 513 
TYR CD1  C  Y N 514 
TYR CD2  C  Y N 515 
TYR CE1  C  Y N 516 
TYR CE2  C  Y N 517 
TYR CZ   C  Y N 518 
TYR OH   O  N N 519 
TYR OXT  O  N N 520 
TYR H    H  N N 521 
TYR H2   H  N N 522 
TYR HA   H  N N 523 
TYR HB2  H  N N 524 
TYR HB3  H  N N 525 
TYR HD1  H  N N 526 
TYR HD2  H  N N 527 
TYR HE1  H  N N 528 
TYR HE2  H  N N 529 
TYR HH   H  N N 530 
TYR HXT  H  N N 531 
VAL N    N  N N 532 
VAL CA   C  N S 533 
VAL C    C  N N 534 
VAL O    O  N N 535 
VAL CB   C  N N 536 
VAL CG1  C  N N 537 
VAL CG2  C  N N 538 
VAL OXT  O  N N 539 
VAL H    H  N N 540 
VAL H2   H  N N 541 
VAL HA   H  N N 542 
VAL HB   H  N N 543 
VAL HG11 H  N N 544 
VAL HG12 H  N N 545 
VAL HG13 H  N N 546 
VAL HG21 H  N N 547 
VAL HG22 H  N N 548 
VAL HG23 H  N N 549 
VAL HXT  H  N N 550 
ZN  ZN   ZN N N 551 
# 
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  
BJ2 O20 C18  doub N N 70  
BJ2 O19 C18  sing N N 71  
BJ2 C18 C17  sing N N 72  
BJ2 N16 C15  sing N N 73  
BJ2 C15 C17  sing N N 74  
BJ2 C15 C13  sing N N 75  
BJ2 C13 O14  doub N N 76  
BJ2 C13 N12  sing N N 77  
BJ2 C11 N12  sing N N 78  
BJ2 C11 C10  sing N N 79  
BJ2 N12 C08  sing N N 80  
BJ2 C10 C09  sing N N 81  
BJ2 C09 C08  sing N N 82  
BJ2 C08 C04  sing N N 83  
BJ2 O07 C05  doub N N 84  
BJ2 C05 O06  sing N N 85  
BJ2 C05 C04  sing N N 86  
BJ2 C04 N03  sing N N 87  
BJ2 N03 C02  sing N N 88  
BJ2 C02 C21  sing N N 89  
BJ2 C02 C01  sing N N 90  
BJ2 O22 C21  doub N N 91  
BJ2 C21 N23  sing N N 92  
BJ2 N23 C24  sing N N 93  
BJ2 N23 C27  sing N N 94  
BJ2 C24 C25  sing N N 95  
BJ2 C27 C26  sing N N 96  
BJ2 C27 C28  sing N N 97  
BJ2 C25 C26  sing N N 98  
BJ2 C28 O30  doub N N 99  
BJ2 C28 O29  sing N N 100 
BJ2 C01 H011 sing N N 101 
BJ2 C01 H013 sing N N 102 
BJ2 C01 H012 sing N N 103 
BJ2 C02 H021 sing N N 104 
BJ2 C04 H041 sing N N 105 
BJ2 C08 H081 sing N N 106 
BJ2 C09 H091 sing N N 107 
BJ2 C09 H092 sing N N 108 
BJ2 C10 H101 sing N N 109 
BJ2 C10 H102 sing N N 110 
BJ2 C11 H112 sing N N 111 
BJ2 C11 H111 sing N N 112 
BJ2 C15 H151 sing N N 113 
BJ2 C17 H172 sing N N 114 
BJ2 C17 H171 sing N N 115 
BJ2 C24 H242 sing N N 116 
BJ2 C24 H241 sing N N 117 
BJ2 C25 H251 sing N N 118 
BJ2 C25 H252 sing N N 119 
BJ2 C26 H262 sing N N 120 
BJ2 C26 H261 sing N N 121 
BJ2 C27 H271 sing N N 122 
BJ2 N03 H031 sing N N 123 
BJ2 N16 H162 sing N N 124 
BJ2 N16 H161 sing N N 125 
BJ2 O06 H3   sing N N 126 
BJ2 O19 H4   sing N N 127 
BJ2 O29 H5   sing N N 128 
BMA C1  C2   sing N N 129 
BMA C1  O1   sing N N 130 
BMA C1  O5   sing N N 131 
BMA C1  H1   sing N N 132 
BMA C2  C3   sing N N 133 
BMA C2  O2   sing N N 134 
BMA C2  H2   sing N N 135 
BMA C3  C4   sing N N 136 
BMA C3  O3   sing N N 137 
BMA C3  H3   sing N N 138 
BMA C4  C5   sing N N 139 
BMA C4  O4   sing N N 140 
BMA C4  H4   sing N N 141 
BMA C5  C6   sing N N 142 
BMA C5  O5   sing N N 143 
BMA C5  H5   sing N N 144 
BMA C6  O6   sing N N 145 
BMA C6  H61  sing N N 146 
BMA C6  H62  sing N N 147 
BMA O1  HO1  sing N N 148 
BMA O2  HO2  sing N N 149 
BMA O3  HO3  sing N N 150 
BMA O4  HO4  sing N N 151 
BMA O6  HO6  sing N N 152 
CYS N   CA   sing N N 153 
CYS N   H    sing N N 154 
CYS N   H2   sing N N 155 
CYS CA  C    sing N N 156 
CYS CA  CB   sing N N 157 
CYS CA  HA   sing N N 158 
CYS C   O    doub N N 159 
CYS C   OXT  sing N N 160 
CYS CB  SG   sing N N 161 
CYS CB  HB2  sing N N 162 
CYS CB  HB3  sing N N 163 
CYS SG  HG   sing N N 164 
CYS OXT HXT  sing N N 165 
FUC C1  C2   sing N N 166 
FUC C1  O1   sing N N 167 
FUC C1  O5   sing N N 168 
FUC C1  H1   sing N N 169 
FUC C2  C3   sing N N 170 
FUC C2  O2   sing N N 171 
FUC C2  H2   sing N N 172 
FUC C3  C4   sing N N 173 
FUC C3  O3   sing N N 174 
FUC C3  H3   sing N N 175 
FUC C4  C5   sing N N 176 
FUC C4  O4   sing N N 177 
FUC C4  H4   sing N N 178 
FUC C5  C6   sing N N 179 
FUC C5  O5   sing N N 180 
FUC C5  H5   sing N N 181 
FUC C6  H61  sing N N 182 
FUC C6  H62  sing N N 183 
FUC C6  H63  sing N N 184 
FUC O1  HO1  sing N N 185 
FUC O2  HO2  sing N N 186 
FUC O3  HO3  sing N N 187 
FUC O4  HO4  sing N N 188 
GLN N   CA   sing N N 189 
GLN N   H    sing N N 190 
GLN N   H2   sing N N 191 
GLN CA  C    sing N N 192 
GLN CA  CB   sing N N 193 
GLN CA  HA   sing N N 194 
GLN C   O    doub N N 195 
GLN C   OXT  sing N N 196 
GLN CB  CG   sing N N 197 
GLN CB  HB2  sing N N 198 
GLN CB  HB3  sing N N 199 
GLN CG  CD   sing N N 200 
GLN CG  HG2  sing N N 201 
GLN CG  HG3  sing N N 202 
GLN CD  OE1  doub N N 203 
GLN CD  NE2  sing N N 204 
GLN NE2 HE21 sing N N 205 
GLN NE2 HE22 sing N N 206 
GLN OXT HXT  sing N N 207 
GLU N   CA   sing N N 208 
GLU N   H    sing N N 209 
GLU N   H2   sing N N 210 
GLU CA  C    sing N N 211 
GLU CA  CB   sing N N 212 
GLU CA  HA   sing N N 213 
GLU C   O    doub N N 214 
GLU C   OXT  sing N N 215 
GLU CB  CG   sing N N 216 
GLU CB  HB2  sing N N 217 
GLU CB  HB3  sing N N 218 
GLU CG  CD   sing N N 219 
GLU CG  HG2  sing N N 220 
GLU CG  HG3  sing N N 221 
GLU CD  OE1  doub N N 222 
GLU CD  OE2  sing N N 223 
GLU OE2 HE2  sing N N 224 
GLU OXT HXT  sing N N 225 
GLY N   CA   sing N N 226 
GLY N   H    sing N N 227 
GLY N   H2   sing N N 228 
GLY CA  C    sing N N 229 
GLY CA  HA2  sing N N 230 
GLY CA  HA3  sing N N 231 
GLY C   O    doub N N 232 
GLY C   OXT  sing N N 233 
GLY OXT HXT  sing N N 234 
HIS N   CA   sing N N 235 
HIS N   H    sing N N 236 
HIS N   H2   sing N N 237 
HIS CA  C    sing N N 238 
HIS CA  CB   sing N N 239 
HIS CA  HA   sing N N 240 
HIS C   O    doub N N 241 
HIS C   OXT  sing N N 242 
HIS CB  CG   sing N N 243 
HIS CB  HB2  sing N N 244 
HIS CB  HB3  sing N N 245 
HIS CG  ND1  sing Y N 246 
HIS CG  CD2  doub Y N 247 
HIS ND1 CE1  doub Y N 248 
HIS ND1 HD1  sing N N 249 
HIS CD2 NE2  sing Y N 250 
HIS CD2 HD2  sing N N 251 
HIS CE1 NE2  sing Y N 252 
HIS CE1 HE1  sing N N 253 
HIS NE2 HE2  sing N N 254 
HIS OXT HXT  sing N N 255 
HOH O   H1   sing N N 256 
HOH O   H2   sing N N 257 
ILE N   CA   sing N N 258 
ILE N   H    sing N N 259 
ILE N   H2   sing N N 260 
ILE CA  C    sing N N 261 
ILE CA  CB   sing N N 262 
ILE CA  HA   sing N N 263 
ILE C   O    doub N N 264 
ILE C   OXT  sing N N 265 
ILE CB  CG1  sing N N 266 
ILE CB  CG2  sing N N 267 
ILE CB  HB   sing N N 268 
ILE CG1 CD1  sing N N 269 
ILE CG1 HG12 sing N N 270 
ILE CG1 HG13 sing N N 271 
ILE CG2 HG21 sing N N 272 
ILE CG2 HG22 sing N N 273 
ILE CG2 HG23 sing N N 274 
ILE CD1 HD11 sing N N 275 
ILE CD1 HD12 sing N N 276 
ILE CD1 HD13 sing N N 277 
ILE OXT HXT  sing N N 278 
LEU N   CA   sing N N 279 
LEU N   H    sing N N 280 
LEU N   H2   sing N N 281 
LEU CA  C    sing N N 282 
LEU CA  CB   sing N N 283 
LEU CA  HA   sing N N 284 
LEU C   O    doub N N 285 
LEU C   OXT  sing N N 286 
LEU CB  CG   sing N N 287 
LEU CB  HB2  sing N N 288 
LEU CB  HB3  sing N N 289 
LEU CG  CD1  sing N N 290 
LEU CG  CD2  sing N N 291 
LEU CG  HG   sing N N 292 
LEU CD1 HD11 sing N N 293 
LEU CD1 HD12 sing N N 294 
LEU CD1 HD13 sing N N 295 
LEU CD2 HD21 sing N N 296 
LEU CD2 HD22 sing N N 297 
LEU CD2 HD23 sing N N 298 
LEU OXT HXT  sing N N 299 
LYS N   CA   sing N N 300 
LYS N   H    sing N N 301 
LYS N   H2   sing N N 302 
LYS CA  C    sing N N 303 
LYS CA  CB   sing N N 304 
LYS CA  HA   sing N N 305 
LYS C   O    doub N N 306 
LYS C   OXT  sing N N 307 
LYS CB  CG   sing N N 308 
LYS CB  HB2  sing N N 309 
LYS CB  HB3  sing N N 310 
LYS CG  CD   sing N N 311 
LYS CG  HG2  sing N N 312 
LYS CG  HG3  sing N N 313 
LYS CD  CE   sing N N 314 
LYS CD  HD2  sing N N 315 
LYS CD  HD3  sing N N 316 
LYS CE  NZ   sing N N 317 
LYS CE  HE2  sing N N 318 
LYS CE  HE3  sing N N 319 
LYS NZ  HZ1  sing N N 320 
LYS NZ  HZ2  sing N N 321 
LYS NZ  HZ3  sing N N 322 
LYS OXT HXT  sing N N 323 
MAN C1  C2   sing N N 324 
MAN C1  O1   sing N N 325 
MAN C1  O5   sing N N 326 
MAN C1  H1   sing N N 327 
MAN C2  C3   sing N N 328 
MAN C2  O2   sing N N 329 
MAN C2  H2   sing N N 330 
MAN C3  C4   sing N N 331 
MAN C3  O3   sing N N 332 
MAN C3  H3   sing N N 333 
MAN C4  C5   sing N N 334 
MAN C4  O4   sing N N 335 
MAN C4  H4   sing N N 336 
MAN C5  C6   sing N N 337 
MAN C5  O5   sing N N 338 
MAN C5  H5   sing N N 339 
MAN C6  O6   sing N N 340 
MAN C6  H61  sing N N 341 
MAN C6  H62  sing N N 342 
MAN O1  HO1  sing N N 343 
MAN O2  HO2  sing N N 344 
MAN O3  HO3  sing N N 345 
MAN O4  HO4  sing N N 346 
MAN O6  HO6  sing N N 347 
MET N   CA   sing N N 348 
MET N   H    sing N N 349 
MET N   H2   sing N N 350 
MET CA  C    sing N N 351 
MET CA  CB   sing N N 352 
MET CA  HA   sing N N 353 
MET C   O    doub N N 354 
MET C   OXT  sing N N 355 
MET CB  CG   sing N N 356 
MET CB  HB2  sing N N 357 
MET CB  HB3  sing N N 358 
MET CG  SD   sing N N 359 
MET CG  HG2  sing N N 360 
MET CG  HG3  sing N N 361 
MET SD  CE   sing N N 362 
MET CE  HE1  sing N N 363 
MET CE  HE2  sing N N 364 
MET CE  HE3  sing N N 365 
MET OXT HXT  sing N N 366 
NAG C1  C2   sing N N 367 
NAG C1  O1   sing N N 368 
NAG C1  O5   sing N N 369 
NAG C1  H1   sing N N 370 
NAG C2  C3   sing N N 371 
NAG C2  N2   sing N N 372 
NAG C2  H2   sing N N 373 
NAG C3  C4   sing N N 374 
NAG C3  O3   sing N N 375 
NAG C3  H3   sing N N 376 
NAG C4  C5   sing N N 377 
NAG C4  O4   sing N N 378 
NAG C4  H4   sing N N 379 
NAG C5  C6   sing N N 380 
NAG C5  O5   sing N N 381 
NAG C5  H5   sing N N 382 
NAG C6  O6   sing N N 383 
NAG C6  H61  sing N N 384 
NAG C6  H62  sing N N 385 
NAG C7  C8   sing N N 386 
NAG C7  N2   sing N N 387 
NAG C7  O7   doub N N 388 
NAG C8  H81  sing N N 389 
NAG C8  H82  sing N N 390 
NAG C8  H83  sing N N 391 
NAG N2  HN2  sing N N 392 
NAG O1  HO1  sing N N 393 
NAG O3  HO3  sing N N 394 
NAG O4  HO4  sing N N 395 
NAG O6  HO6  sing N N 396 
PHE N   CA   sing N N 397 
PHE N   H    sing N N 398 
PHE N   H2   sing N N 399 
PHE CA  C    sing N N 400 
PHE CA  CB   sing N N 401 
PHE CA  HA   sing N N 402 
PHE C   O    doub N N 403 
PHE C   OXT  sing N N 404 
PHE CB  CG   sing N N 405 
PHE CB  HB2  sing N N 406 
PHE CB  HB3  sing N N 407 
PHE CG  CD1  doub Y N 408 
PHE CG  CD2  sing Y N 409 
PHE CD1 CE1  sing Y N 410 
PHE CD1 HD1  sing N N 411 
PHE CD2 CE2  doub Y N 412 
PHE CD2 HD2  sing N N 413 
PHE CE1 CZ   doub Y N 414 
PHE CE1 HE1  sing N N 415 
PHE CE2 CZ   sing Y N 416 
PHE CE2 HE2  sing N N 417 
PHE CZ  HZ   sing N N 418 
PHE OXT HXT  sing N N 419 
PRO N   CA   sing N N 420 
PRO N   CD   sing N N 421 
PRO N   H    sing N N 422 
PRO CA  C    sing N N 423 
PRO CA  CB   sing N N 424 
PRO CA  HA   sing N N 425 
PRO C   O    doub N N 426 
PRO C   OXT  sing N N 427 
PRO CB  CG   sing N N 428 
PRO CB  HB2  sing N N 429 
PRO CB  HB3  sing N N 430 
PRO CG  CD   sing N N 431 
PRO CG  HG2  sing N N 432 
PRO CG  HG3  sing N N 433 
PRO CD  HD2  sing N N 434 
PRO CD  HD3  sing N N 435 
PRO OXT HXT  sing N N 436 
SER N   CA   sing N N 437 
SER N   H    sing N N 438 
SER N   H2   sing N N 439 
SER CA  C    sing N N 440 
SER CA  CB   sing N N 441 
SER CA  HA   sing N N 442 
SER C   O    doub N N 443 
SER C   OXT  sing N N 444 
SER CB  OG   sing N N 445 
SER CB  HB2  sing N N 446 
SER CB  HB3  sing N N 447 
SER OG  HG   sing N N 448 
SER OXT HXT  sing N N 449 
THR N   CA   sing N N 450 
THR N   H    sing N N 451 
THR N   H2   sing N N 452 
THR CA  C    sing N N 453 
THR CA  CB   sing N N 454 
THR CA  HA   sing N N 455 
THR C   O    doub N N 456 
THR C   OXT  sing N N 457 
THR CB  OG1  sing N N 458 
THR CB  CG2  sing N N 459 
THR CB  HB   sing N N 460 
THR OG1 HG1  sing N N 461 
THR CG2 HG21 sing N N 462 
THR CG2 HG22 sing N N 463 
THR CG2 HG23 sing N N 464 
THR OXT HXT  sing N N 465 
TRP N   CA   sing N N 466 
TRP N   H    sing N N 467 
TRP N   H2   sing N N 468 
TRP CA  C    sing N N 469 
TRP CA  CB   sing N N 470 
TRP CA  HA   sing N N 471 
TRP C   O    doub N N 472 
TRP C   OXT  sing N N 473 
TRP CB  CG   sing N N 474 
TRP CB  HB2  sing N N 475 
TRP CB  HB3  sing N N 476 
TRP CG  CD1  doub Y N 477 
TRP CG  CD2  sing Y N 478 
TRP CD1 NE1  sing Y N 479 
TRP CD1 HD1  sing N N 480 
TRP CD2 CE2  doub Y N 481 
TRP CD2 CE3  sing Y N 482 
TRP NE1 CE2  sing Y N 483 
TRP NE1 HE1  sing N N 484 
TRP CE2 CZ2  sing Y N 485 
TRP CE3 CZ3  doub Y N 486 
TRP CE3 HE3  sing N N 487 
TRP CZ2 CH2  doub Y N 488 
TRP CZ2 HZ2  sing N N 489 
TRP CZ3 CH2  sing Y N 490 
TRP CZ3 HZ3  sing N N 491 
TRP CH2 HH2  sing N N 492 
TRP OXT HXT  sing N N 493 
TYR N   CA   sing N N 494 
TYR N   H    sing N N 495 
TYR N   H2   sing N N 496 
TYR CA  C    sing N N 497 
TYR CA  CB   sing N N 498 
TYR CA  HA   sing N N 499 
TYR C   O    doub N N 500 
TYR C   OXT  sing N N 501 
TYR CB  CG   sing N N 502 
TYR CB  HB2  sing N N 503 
TYR CB  HB3  sing N N 504 
TYR CG  CD1  doub Y N 505 
TYR CG  CD2  sing Y N 506 
TYR CD1 CE1  sing Y N 507 
TYR CD1 HD1  sing N N 508 
TYR CD2 CE2  doub Y N 509 
TYR CD2 HD2  sing N N 510 
TYR CE1 CZ   doub Y N 511 
TYR CE1 HE1  sing N N 512 
TYR CE2 CZ   sing Y N 513 
TYR CE2 HE2  sing N N 514 
TYR CZ  OH   sing N N 515 
TYR OH  HH   sing N N 516 
TYR OXT HXT  sing N N 517 
VAL N   CA   sing N N 518 
VAL N   H    sing N N 519 
VAL N   H2   sing N N 520 
VAL CA  C    sing N N 521 
VAL CA  CB   sing N N 522 
VAL CA  HA   sing N N 523 
VAL C   O    doub N N 524 
VAL C   OXT  sing N N 525 
VAL CB  CG1  sing N N 526 
VAL CB  CG2  sing N N 527 
VAL CB  HB   sing N N 528 
VAL CG1 HG11 sing N N 529 
VAL CG1 HG12 sing N N 530 
VAL CG1 HG13 sing N N 531 
VAL CG2 HG21 sing N N 532 
VAL CG2 HG22 sing N N 533 
VAL CG2 HG23 sing N N 534 
VAL OXT HXT  sing N N 535 
# 
_pdbx_audit_support.funding_organization   'Biotechnology and Biological Sciences Research Council (BBSRC)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           BB/X001032/1 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
2 BMA 3 n 
2 MAN 4 n 
2 NAG 5 n 
2 MAN 6 n 
2 NAG 7 n 
2 FUC 8 n 
# 
_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   6f9t 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GBO 
_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]   0.017612 
_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]   0.011776 
_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]   0.007404 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C  6  6  2.3103  20.8439 1.0201 10.2075 1.5888 0.5687  0.8651 51.6512 0.2156   
CL 17 17 11.4601 0.0104  7.1962 1.1662  6.2554 18.5194 1.6455 47.7784 -9.3453  
N  7  7  12.2220 0.0057  3.1346 9.8933  2.0141 28.9975 1.1672 0.5826  -11.5379 
O  8  8  3.0487  13.2771 2.2870 5.7011  1.5464 0.3239  0.8671 32.9089 0.2508   
S  16 16 6.9054  1.4679  5.2035 22.2151 1.4379 0.2536  1.5863 56.1720 1.0486   
ZN 30 30 14.0812 3.2655  7.0352 0.2333  5.1677 10.3163 2.4112 58.7097 1.0042   
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
_atom_site.pdbx_tls_group_id 
ATOM   1    N  N   . ASP A 1 4   ? 6.125   -28.901 0.965  1    74.524  ? 40   ASP A N   1 1 
ATOM   2    C  CA  . ASP A 1 4   ? 7.529   -29.115 0.519  1    74.609  ? 40   ASP A CA  1 1 
ATOM   3    C  C   . ASP A 1 4   ? 8.463   -28.072 1.146  1    69.508  ? 40   ASP A C   1 1 
ATOM   4    O  O   . ASP A 1 4   ? 8.168   -26.873 1.153  1    67.437  ? 40   ASP A O   1 1 
ATOM   5    C  CB  . ASP A 1 4   ? 7.591   -29.197 -1.002 1    77.946  ? 40   ASP A CB  1 1 
ATOM   6    C  CG  . ASP A 1 4   ? 8.847   -29.829 -1.589 1    80.728  ? 40   ASP A CG  1 1 
ATOM   7    O  OD1 . ASP A 1 4   ? 9.96    -29.402 -1.197 1    82.929  ? 40   ASP A OD1 1 1 
ATOM   8    O  OD2 . ASP A 1 4   ? 8.708   -30.744 -2.444 1    75.65   ? 40   ASP A OD2 1 1 
ATOM   9    N  N   . GLU A 1 5   ? 9.615   -28.564 1.639  1    71.849  ? 41   GLU A N   1 1 
ATOM   10   C  CA  . GLU A 1 5   ? 10.726  -27.778 2.166  1    65.761  ? 41   GLU A CA  1 1 
ATOM   11   C  C   . GLU A 1 5   ? 11.304  -26.911 1.05   1    61.755  ? 41   GLU A C   1 1 
ATOM   12   O  O   . GLU A 1 5   ? 11.596  -25.749 1.274  1    56.497  ? 41   GLU A O   1 1 
ATOM   13   C  CB  . GLU A 1 5   ? 11.86   -28.639 2.744  1    69.759  ? 41   GLU A CB  1 1 
ATOM   14   C  CG  . GLU A 1 5   ? 11.575  -29.21  4.133  1    75.5    ? 41   GLU A CG  1 1 
ATOM   15   C  CD  . GLU A 1 5   ? 11.611  -28.233 5.314  1    82.024  ? 41   GLU A CD  1 1 
ATOM   16   O  OE1 . GLU A 1 5   ? 12.718  -27.784 5.688  1    81.255  ? 41   GLU A OE1 1 1 
ATOM   17   O  OE2 . GLU A 1 5   ? 10.54   -27.909 5.88   1    75.739  ? 41   GLU A OE2 1 1 
ATOM   18   N  N   . ALA A 1 6   ? 11.47   -27.477 -0.152 1    59.477  ? 42   ALA A N   1 1 
ATOM   19   C  CA  . ALA A 1 6   ? 11.982  -26.691 -1.26  1    56.139  ? 42   ALA A CA  1 1 
ATOM   20   C  C   . ALA A 1 6   ? 11.042  -25.537 -1.65  1    53.824  ? 42   ALA A C   1 1 
ATOM   21   O  O   . ALA A 1 6   ? 11.528  -24.489 -2.061 1    50.413  ? 42   ALA A O   1 1 
ATOM   22   C  CB  . ALA A 1 6   ? 12.297  -27.583 -2.424 1    58.131  ? 42   ALA A CB  1 1 
ATOM   23   N  N   . GLU A 1 7   ? 9.714   -25.699 -1.554 1    52.121  ? 43   GLU A N   1 1 
ATOM   24   C  CA  . GLU A 1 7   ? 8.837   -24.626 -2.004 1    50.629  ? 43   GLU A CA  1 1 
ATOM   25   C  C   . GLU A 1 7   ? 8.863   -23.463 -1.022 1    50.753  ? 43   GLU A C   1 1 
ATOM   26   O  O   . GLU A 1 7   ? 8.741   -22.3   -1.417 1    47.719  ? 43   GLU A O   1 1 
ATOM   27   C  CB  . GLU A 1 7   ? 7.388   -25.005 -2.285 1    57.499  ? 43   GLU A CB  1 1 
ATOM   28   C  CG  . GLU A 1 7   ? 7.115   -25.063 -3.787 1    68.233  ? 43   GLU A CG  1 1 
ATOM   29   C  CD  . GLU A 1 7   ? 5.674   -24.774 -4.215 1    77.128  ? 43   GLU A CD  1 1 
ATOM   30   O  OE1 . GLU A 1 7   ? 5.152   -25.523 -5.085 1    69.229  ? 43   GLU A OE1 1 1 
ATOM   31   O  OE2 . GLU A 1 7   ? 5.066   -23.794 -3.691 1    77.553  ? 43   GLU A OE2 1 1 
ATOM   32   N  N   . ALA A 1 8   ? 9.042   -23.786 0.259  1    46.373  ? 44   ALA A N   1 1 
ATOM   33   C  CA  . ALA A 1 8   ? 9.051   -22.762 1.29   1    44.877  ? 44   ALA A CA  1 1 
ATOM   34   C  C   . ALA A 1 8   ? 10.382  -22.01  1.254  1    42.086  ? 44   ALA A C   1 1 
ATOM   35   O  O   . ALA A 1 8   ? 10.431  -20.805 1.406  1    38.841  ? 44   ALA A O   1 1 
ATOM   36   C  CB  . ALA A 1 8   ? 8.791   -23.411 2.62   1    41.914  ? 44   ALA A CB  1 1 
ATOM   37   N  N   . SER A 1 9   ? 11.465  -22.717 0.966  1    43.447  ? 45   SER A N   1 1 
ATOM   38   C  CA  . SER A 1 9   ? 12.799  -22.155 0.82   1    43.999  ? 45   SER A CA  1 1 
ATOM   39   C  C   . SER A 1 9   ? 12.842  -21.126 -0.337 1    49.219  ? 45   SER A C   1 1 
ATOM   40   O  O   . SER A 1 9   ? 13.27   -19.968 -0.148 1    45.07   ? 45   SER A O   1 1 
ATOM   41   C  CB  . SER A 1 9   ? 13.697  -23.325 0.52   1    46.192  ? 45   SER A CB  1 1 
ATOM   42   O  OG  . SER A 1 9   ? 15.033  -22.984 0.783  1    50.285  ? 45   SER A OG  1 1 
ATOM   43   N  N   . LYS A 1 10  ? 12.38   -21.554 -1.537 1    42.36   ? 46   LYS A N   1 1 
ATOM   44   C  CA  . LYS A 1 10  ? 12.206  -20.684 -2.7   1    44.344  ? 46   LYS A CA  1 1 
ATOM   45   C  C   . LYS A 1 10  ? 11.375  -19.434 -2.375 1    40.482  ? 46   LYS A C   1 1 
ATOM   46   O  O   . LYS A 1 10  ? 11.78   -18.31  -2.687 1    38.808  ? 46   LYS A O   1 1 
ATOM   47   C  CB  . LYS A 1 10  ? 11.544  -21.369 -3.896 1    48.272  ? 46   LYS A CB  1 1 
ATOM   48   C  CG  . LYS A 1 10  ? 11.712  -20.723 -5.276 1    53.608  ? 46   LYS A CG  1 1 
ATOM   49   C  CD  . LYS A 1 10  ? 10.456  -20.711 -6.151 1    56.455  ? 46   LYS A CD  1 1 
ATOM   50   C  CE  . LYS A 1 10  ? 10.004  -21.988 -6.714 1    59.013  ? 46   LYS A CE  1 1 
ATOM   51   N  NZ  . LYS A 1 10  ? 8.556   -21.931 -6.909 1    64.808  ? 46   LYS A NZ  1 1 
ATOM   52   N  N   . PHE A 1 11  ? 10.223  -19.621 -1.722 1    37.007  ? 47   PHE A N   1 1 
ATOM   53   C  CA  . PHE A 1 11  ? 9.384   -18.502 -1.366 1    34.508  ? 47   PHE A CA  1 1 
ATOM   54   C  C   . PHE A 1 11  ? 10.163  -17.546 -0.462 1    33.745  ? 47   PHE A C   1 1 
ATOM   55   O  O   . PHE A 1 11  ? 10.1    -16.329 -0.605 1    33.015  ? 47   PHE A O   1 1 
ATOM   56   C  CB  . PHE A 1 11  ? 8.088   -19.063 -0.799 1    34.316  ? 47   PHE A CB  1 1 
ATOM   57   C  CG  . PHE A 1 11  ? 7.374   -18.017 0.036  1    35.494  ? 47   PHE A CG  1 1 
ATOM   58   C  CD1 . PHE A 1 11  ? 7.692   -17.831 1.381  1    34.319  ? 47   PHE A CD1 1 1 
ATOM   59   C  CD2 . PHE A 1 11  ? 6.42    -17.188 -0.554 1    34.853  ? 47   PHE A CD2 1 1 
ATOM   60   C  CE1 . PHE A 1 11  ? 7.043   -16.849 2.126  1    35.499  ? 47   PHE A CE1 1 1 
ATOM   61   C  CE2 . PHE A 1 11  ? 5.771   -16.225 0.206  1    34.449  ? 47   PHE A CE2 1 1 
ATOM   62   C  CZ  . PHE A 1 11  ? 6.053   -16.067 1.55   1    33.639  ? 47   PHE A CZ  1 1 
ATOM   63   N  N   . VAL A 1 12  ? 10.956  -18.057 0.467  1    33.502  ? 48   VAL A N   1 1 
ATOM   64   C  CA  . VAL A 1 12  ? 11.516  -17.102 1.402  1    33.53   ? 48   VAL A CA  1 1 
ATOM   65   C  C   . VAL A 1 12  ? 12.646  -16.319 0.71   1    32.642  ? 48   VAL A C   1 1 
ATOM   66   O  O   . VAL A 1 12  ? 12.843  -15.141 0.975  1    31.83   ? 48   VAL A O   1 1 
ATOM   67   C  CB  . VAL A 1 12  ? 11.953  -17.878 2.662  1    35.567  ? 48   VAL A CB  1 1 
ATOM   68   C  CG1 . VAL A 1 12  ? 13.161  -17.281 3.326  1    35.753  ? 48   VAL A CG1 1 1 
ATOM   69   C  CG2 . VAL A 1 12  ? 10.838  -17.994 3.681  1    34.566  ? 48   VAL A CG2 1 1 
ATOM   70   N  N   . GLU A 1 13  ? 13.324  -16.947 -0.234 1    35.324  ? 49   GLU A N   1 1 
ATOM   71   C  CA  . GLU A 1 13  ? 14.293  -16.295 -1.128 1    38.051  ? 49   GLU A CA  1 1 
ATOM   72   C  C   . GLU A 1 13  ? 13.67   -15.169 -1.971 1    38.225  ? 49   GLU A C   1 1 
ATOM   73   O  O   . GLU A 1 13  ? 14.248  -14.086 -2.052 1    38.11   ? 49   GLU A O   1 1 
ATOM   74   C  CB  . GLU A 1 13  ? 14.908  -17.285 -2.096 1    41.085  ? 49   GLU A CB  1 1 
ATOM   75   C  CG  . GLU A 1 13  ? 15.858  -18.225 -1.373 1    47.912  ? 49   GLU A CG  1 1 
ATOM   76   C  CD  . GLU A 1 13  ? 16.208  -19.533 -2.075 1    56.093  ? 49   GLU A CD  1 1 
ATOM   77   O  OE1 . GLU A 1 13  ? 15.661  -19.939 -3.124 1    53.798  ? 49   GLU A OE1 1 1 
ATOM   78   O  OE2 . GLU A 1 13  ? 17.11   -20.18  -1.507 1    59.727  ? 49   GLU A OE2 1 1 
ATOM   79   N  N   . GLU A 1 14  ? 12.495  -15.404 -2.59  1    36.15   ? 50   GLU A N   1 1 
ATOM   80   C  CA  . GLU A 1 14  ? 11.779  -14.374 -3.331 1    36.381  ? 50   GLU A CA  1 1 
ATOM   81   C  C   . GLU A 1 14  ? 11.293  -13.221 -2.442 1    36.514  ? 50   GLU A C   1 1 
ATOM   82   O  O   . GLU A 1 14  ? 11.456  -12.027 -2.783 1    33.318  ? 50   GLU A O   1 1 
ATOM   83   C  CB  . GLU A 1 14  ? 10.528  -14.995 -3.911 1    37.169  ? 50   GLU A CB  1 1 
ATOM   84   C  CG  . GLU A 1 14  ? 10.91   -15.782 -5.132 1    40.505  ? 50   GLU A CG  1 1 
ATOM   85   C  CD  . GLU A 1 14  ? 9.699   -16.46  -5.692 1    42.905  ? 50   GLU A CD  1 1 
ATOM   86   O  OE1 . GLU A 1 14  ? 8.537   -16.156 -5.377 1    43.377  ? 50   GLU A OE1 1 1 
ATOM   87   O  OE2 . GLU A 1 14  ? 10.018  -17.322 -6.514 1    46.895  ? 50   GLU A OE2 1 1 
ATOM   88   N  N   . TYR A 1 15  ? 10.765  -13.587 -1.247 1    34.224  ? 51   TYR A N   1 1 
ATOM   89   C  CA  . TYR A 1 15  ? 10.327  -12.572 -0.334 1    32.51   ? 51   TYR A CA  1 1 
ATOM   90   C  C   . TYR A 1 15  ? 11.536  -11.696 -0.053 1    33.362  ? 51   TYR A C   1 1 
ATOM   91   O  O   . TYR A 1 15  ? 11.435  -10.478 -0.037 1    32.675  ? 51   TYR A O   1 1 
ATOM   92   C  CB  . TYR A 1 15  ? 9.692   -13.23  0.892  1    33.773  ? 51   TYR A CB  1 1 
ATOM   93   C  CG  . TYR A 1 15  ? 9.385   -12.201 1.949  1    30.27   ? 51   TYR A CG  1 1 
ATOM   94   C  CD1 . TYR A 1 15  ? 8.186   -11.51  1.913  1    31.798  ? 51   TYR A CD1 1 1 
ATOM   95   C  CD2 . TYR A 1 15  ? 10.325  -11.865 2.918  1    30.87   ? 51   TYR A CD2 1 1 
ATOM   96   C  CE1 . TYR A 1 15  ? 7.914   -10.525 2.857  1    29.372  ? 51   TYR A CE1 1 1 
ATOM   97   C  CE2 . TYR A 1 15  ? 10.07   -10.895 3.887  1    29.761  ? 51   TYR A CE2 1 1 
ATOM   98   C  CZ  . TYR A 1 15  ? 8.836   -10.257 3.859  1    30.682  ? 51   TYR A CZ  1 1 
ATOM   99   O  OH  . TYR A 1 15  ? 8.577   -9.276  4.766  1    30.106  ? 51   TYR A OH  1 1 
ATOM   100  N  N   . ASP A 1 16  ? 12.697  -12.31  0.126  1    33.772  ? 52   ASP A N   1 1 
ATOM   101  C  CA  . ASP A 1 16  ? 13.842  -11.547 0.626  1    36.78   ? 52   ASP A CA  1 1 
ATOM   102  C  C   . ASP A 1 16  ? 14.332  -10.533 -0.434 1    36.56   ? 52   ASP A C   1 1 
ATOM   103  O  O   . ASP A 1 16  ? 14.612  -9.378  -0.095 1    32.764  ? 52   ASP A O   1 1 
ATOM   104  C  CB  . ASP A 1 16  ? 14.952  -12.48  1.072  1    36.858  ? 52   ASP A CB  1 1 
ATOM   105  C  CG  . ASP A 1 16  ? 16.019  -11.777 1.885  1    45.652  ? 52   ASP A CG  1 1 
ATOM   106  O  OD1 . ASP A 1 16  ? 15.604  -11.176 2.907  1    47.114  ? 52   ASP A OD1 1 1 
ATOM   107  O  OD2 . ASP A 1 16  ? 17.229  -11.796 1.46   1    43.717  ? 52   ASP A OD2 1 1 
ATOM   108  N  N   . ARG A 1 17  ? 14.4    -10.979 -1.711 1    35.593  ? 53   ARG A N   1 1 
ATOM   109  C  CA  . ARG A 1 17  ? 14.841  -10.173 -2.853 1    36.122  ? 53   ARG A CA  1 1 
ATOM   110  C  C   . ARG A 1 17  ? 13.901  -8.996  -3.044 1    35.202  ? 53   ARG A C   1 1 
ATOM   111  O  O   . ARG A 1 17  ? 14.343  -7.871  -3.211 1    33.583  ? 53   ARG A O   1 1 
ATOM   112  C  CB  . ARG A 1 17  ? 14.609  -10.824 -4.221 1    36.116  ? 53   ARG A CB  1 1 
ATOM   113  C  CG  . ARG A 1 17  ? 15.615  -11.921 -4.396 1    37.968  ? 53   ARG A CG  1 1 
ATOM   114  C  CD  . ARG A 1 17  ? 15.264  -12.614 -5.588 1    40.723  ? 53   ARG A CD  1 1 
ATOM   115  N  NE  . ARG A 1 17  ? 16.077  -13.808 -5.338 1    41.783  ? 53   ARG A NE  1 1 
ATOM   116  C  CZ  . ARG A 1 17  ? 15.516  -14.979 -5.379 1    43.493  ? 53   ARG A CZ  1 1 
ATOM   117  N  NH1 . ARG A 1 17  ? 14.227  -15.118 -5.585 1    44.875  ? 53   ARG A NH1 1 1 
ATOM   118  N  NH2 . ARG A 1 17  ? 16.258  -16.035 -5.259 1    49.087  ? 53   ARG A NH2 1 1 
ATOM   119  N  N   . THR A 1 18  ? 12.608  -9.316  -3.157 1    36.115  ? 54   THR A N   1 1 
ATOM   120  C  CA  . THR A 1 18  ? 11.584  -8.328  -3.48  1    37.203  ? 54   THR A CA  1 1 
ATOM   121  C  C   . THR A 1 18  ? 11.42   -7.31   -2.329 1    35.128  ? 54   THR A C   1 1 
ATOM   122  O  O   . THR A 1 18  ? 11.326  -6.113  -2.565 1    35.265  ? 54   THR A O   1 1 
ATOM   123  C  CB  . THR A 1 18  ? 10.272  -9.022  -3.904 1    35.623  ? 54   THR A CB  1 1 
ATOM   124  O  OG1 . THR A 1 18  ? 9.831   -9.767  -2.759 1    35.326  ? 54   THR A OG1 1 1 
ATOM   125  C  CG2 . THR A 1 18  ? 10.383  -9.895  -5.149 1    36.601  ? 54   THR A CG2 1 1 
ATOM   126  N  N   . SER A 1 19  ? 11.342  -7.765  -1.075 1    32.269  ? 55   SER A N   1 1 
ATOM   127  C  CA  . SER A 1 19  ? 11.317  -6.873  0.07   1    32.213  ? 55   SER A CA  1 1 
ATOM   128  C  C   . SER A 1 19  ? 12.443  -5.862  0.053  1    33.948  ? 55   SER A C   1 1 
ATOM   129  O  O   . SER A 1 19  ? 12.257  -4.721  0.472  1    38.435  ? 55   SER A O   1 1 
ATOM   130  C  CB  . SER A 1 19  ? 11.376  -7.631  1.395  1    30.26   ? 55   SER A CB  1 1 
ATOM   131  O  OG  . SER A 1 19  ? 10.175  -8.389  1.465  1    37.067  ? 55   SER A OG  1 1 
ATOM   132  N  N   . GLN A 1 20  ? 13.657  -6.318  -0.188 1    36.508  ? 56   GLN A N   1 1 
ATOM   133  C  CA  . GLN A 1 20  ? 14.751  -5.351  -0.165 1    42.676  ? 56   GLN A CA  1 1 
ATOM   134  C  C   . GLN A 1 20  ? 14.421  -4.111  -1.026 1    40.151  ? 56   GLN A C   1 1 
ATOM   135  O  O   . GLN A 1 20  ? 14.455  -3.007  -0.526 1    36.904  ? 56   GLN A O   1 1 
ATOM   136  C  CB  . GLN A 1 20  ? 16.056  -6.022  -0.584 1    44.116  ? 56   GLN A CB  1 1 
ATOM   137  C  CG  . GLN A 1 20  ? 16.679  -6.811  0.551  1    52.148  ? 56   GLN A CG  1 1 
ATOM   138  C  CD  . GLN A 1 20  ? 18.03   -7.317  0.126  1    58.951  ? 56   GLN A CD  1 1 
ATOM   139  O  OE1 . GLN A 1 20  ? 18.865  -6.539  -0.349 1    65.21   ? 56   GLN A OE1 1 1 
ATOM   140  N  NE2 . GLN A 1 20  ? 18.234  -8.622  0.235  1    66.142  ? 56   GLN A NE2 1 1 
ATOM   141  N  N   . VAL A 1 21  ? 14.038  -4.308  -2.294 1    39.815  ? 57   VAL A N   1 1 
ATOM   142  C  CA  . VAL A 1 21  ? 13.77   -3.267  -3.278 1    41.343  ? 57   VAL A CA  1 1 
ATOM   143  C  C   . VAL A 1 21  ? 12.636  -2.358  -2.788 1    42.681  ? 57   VAL A C   1 1 
ATOM   144  O  O   . VAL A 1 21  ? 12.803  -1.141  -2.747 1    45.447  ? 57   VAL A O   1 1 
ATOM   145  C  CB  . VAL A 1 21  ? 13.431  -3.964  -4.626 1    46.834  ? 57   VAL A CB  1 1 
ATOM   146  C  CG1 . VAL A 1 21  ? 13.009  -2.998  -5.742 1    46.049  ? 57   VAL A CG1 1 1 
ATOM   147  C  CG2 . VAL A 1 21  ? 14.55   -4.877  -5.13  1    45.912  ? 57   VAL A CG2 1 1 
ATOM   148  N  N   . VAL A 1 22  ? 11.492  -2.939  -2.384 1    39.533  ? 58   VAL A N   1 1 
ATOM   149  C  CA  . VAL A 1 22  ? 10.286  -2.19   -2.062 1    38.557  ? 58   VAL A CA  1 1 
ATOM   150  C  C   . VAL A 1 22  ? 10.484  -1.399  -0.767 1    40.119  ? 58   VAL A C   1 1 
ATOM   151  O  O   . VAL A 1 22  ? 10.018  -0.261  -0.648 1    42.077  ? 58   VAL A O   1 1 
ATOM   152  C  CB  . VAL A 1 22  ? 9.068   -3.159  -1.984 1    39.526  ? 58   VAL A CB  1 1 
ATOM   153  C  CG1 . VAL A 1 22  ? 7.821   -2.595  -1.34  1    36.941  ? 58   VAL A CG1 1 1 
ATOM   154  C  CG2 . VAL A 1 22  ? 8.665   -3.642  -3.35  1    41.747  ? 58   VAL A CG2 1 1 
ATOM   155  N  N   . TRP A 1 23  ? 11.14   -2.014  0.234  1    39.078  ? 59   TRP A N   1 1 
ATOM   156  C  CA  . TRP A 1 23  ? 11.435  -1.34   1.5    1    35.239  ? 59   TRP A CA  1 1 
ATOM   157  C  C   . TRP A 1 23  ? 12.502  -0.261  1.317  1    31.28   ? 59   TRP A C   1 1 
ATOM   158  O  O   . TRP A 1 23  ? 12.427  0.804   1.908  1    29.521  ? 59   TRP A O   1 1 
ATOM   159  C  CB  . TRP A 1 23  ? 11.841  -2.334  2.603  1    37.612  ? 59   TRP A CB  1 1 
ATOM   160  C  CG  . TRP A 1 23  ? 10.764  -3.267  3.081  1    44.779  ? 59   TRP A CG  1 1 
ATOM   161  C  CD1 . TRP A 1 23  ? 9.571   -3.489  2.478  1    46.929  ? 59   TRP A CD1 1 1 
ATOM   162  C  CD2 . TRP A 1 23  ? 10.792  -4.153  4.234  1    53.188  ? 59   TRP A CD2 1 1 
ATOM   163  N  NE1 . TRP A 1 23  ? 8.833   -4.401  3.185  1    49.964  ? 59   TRP A NE1 1 1 
ATOM   164  C  CE2 . TRP A 1 23  ? 9.551   -4.841  4.261  1    56.753  ? 59   TRP A CE2 1 1 
ATOM   165  C  CE3 . TRP A 1 23  ? 11.724  -4.446  5.249  1    61.454  ? 59   TRP A CE3 1 1 
ATOM   166  C  CZ2 . TRP A 1 23  ? 9.232   -5.8    5.237  1    59.472  ? 59   TRP A CZ2 1 1 
ATOM   167  C  CZ3 . TRP A 1 23  ? 11.415  -5.399  6.208  1    63.592  ? 59   TRP A CZ3 1 1 
ATOM   168  C  CH2 . TRP A 1 23  ? 10.187  -6.073  6.199  1    61.116  ? 59   TRP A CH2 1 1 
ATOM   169  N  N   . ASN A 1 24  ? 13.473  -0.499  0.448  1    34.58   ? 60   ASN A N   1 1 
ATOM   170  C  CA  . ASN A 1 24  ? 14.449  0.55    0.166  1    38.343  ? 60   ASN A CA  1 1 
ATOM   171  C  C   . ASN A 1 24  ? 13.733  1.782   -0.405 1    41.189  ? 60   ASN A C   1 1 
ATOM   172  O  O   . ASN A 1 24  ? 13.967  2.934   0.019  1    38.036  ? 60   ASN A O   1 1 
ATOM   173  C  CB  . ASN A 1 24  ? 15.566  0.049   -0.742 1    37.696  ? 60   ASN A CB  1 1 
ATOM   174  C  CG  . ASN A 1 24  ? 16.572  1.127   -1.092 1    39.705  ? 60   ASN A CG  1 1 
ATOM   175  O  OD1 . ASN A 1 24  ? 16.69   1.516   -2.258 1    41.6    ? 60   ASN A OD1 1 1 
ATOM   176  N  ND2 . ASN A 1 24  ? 17.35   1.583   -0.126 1    36.062  ? 60   ASN A ND2 1 1 
ATOM   177  N  N   . GLU A 1 25  ? 12.832  1.503   -1.359 1    41.268  ? 61   GLU A N   1 1 
ATOM   178  C  CA  . GLU A 1 25  ? 12.093  2.55    -2.048 1    42.6    ? 61   GLU A CA  1 1 
ATOM   179  C  C   . GLU A 1 25  ? 11.289  3.361   -1.047 1    39.317  ? 61   GLU A C   1 1 
ATOM   180  O  O   . GLU A 1 25  ? 11.237  4.586   -1.14  1    39.316  ? 61   GLU A O   1 1 
ATOM   181  C  CB  . GLU A 1 25  ? 11.134  2.02    -3.116 1    45      ? 61   GLU A CB  1 1 
ATOM   182  C  CG  . GLU A 1 25  ? 11.882  1.214   -4.176 1    52.802  ? 61   GLU A CG  1 1 
ATOM   183  C  CD  . GLU A 1 25  ? 11.231  1.177   -5.551 1    56.611  ? 61   GLU A CD  1 1 
ATOM   184  O  OE1 . GLU A 1 25  ? 10.072  1.631   -5.731 1    58.896  ? 61   GLU A OE1 1 1 
ATOM   185  O  OE2 . GLU A 1 25  ? 11.95   0.733   -6.464 1    62.404  ? 61   GLU A OE2 1 1 
ATOM   186  N  N   . TYR A 1 26  ? 10.667  2.65    -0.11  1    36.396  ? 62   TYR A N   1 1 
ATOM   187  C  CA  . TYR A 1 26  ? 9.713   3.285   0.776  1    37.55   ? 62   TYR A CA  1 1 
ATOM   188  C  C   . TYR A 1 26  ? 10.486  4.018   1.876  1    38.764  ? 62   TYR A C   1 1 
ATOM   189  O  O   . TYR A 1 26  ? 10.064  5.085   2.326  1    37.098  ? 62   TYR A O   1 1 
ATOM   190  C  CB  . TYR A 1 26  ? 8.729   2.273   1.376  1    39.359  ? 62   TYR A CB  1 1 
ATOM   191  C  CG  . TYR A 1 26  ? 8.024   2.822   2.609  1    38.9    ? 62   TYR A CG  1 1 
ATOM   192  C  CD1 . TYR A 1 26  ? 8.638   2.815   3.861  1    39.934  ? 62   TYR A CD1 1 1 
ATOM   193  C  CD2 . TYR A 1 26  ? 6.765   3.399   2.502  1    40.268  ? 62   TYR A CD2 1 1 
ATOM   194  C  CE1 . TYR A 1 26  ? 8.01    3.33    4.994  1    42.394  ? 62   TYR A CE1 1 1 
ATOM   195  C  CE2 . TYR A 1 26  ? 6.13    3.932   3.615  1    44.514  ? 62   TYR A CE2 1 1 
ATOM   196  C  CZ  . TYR A 1 26  ? 6.759   3.919   4.854  1    47.089  ? 62   TYR A CZ  1 1 
ATOM   197  O  OH  . TYR A 1 26  ? 6.08    4.453   5.915  1    55.142  ? 62   TYR A OH  1 1 
ATOM   198  N  N   . ALA A 1 27  ? 11.609  3.441   2.318  1    41.718  ? 63   ALA A N   1 1 
ATOM   199  C  CA  . ALA A 1 27  ? 12.456  4.175   3.26   1    45.526  ? 63   ALA A CA  1 1 
ATOM   200  C  C   . ALA A 1 27  ? 12.918  5.5     2.622  1    44.385  ? 63   ALA A C   1 1 
ATOM   201  O  O   . ALA A 1 27  ? 12.862  6.556   3.26   1    44.306  ? 63   ALA A O   1 1 
ATOM   202  C  CB  . ALA A 1 27  ? 13.622  3.312   3.713  1    39.645  ? 63   ALA A CB  1 1 
ATOM   203  N  N   . GLY A 1 28  ? 13.383  5.425   1.364  1    46.332  ? 64   GLY A N   1 1 
ATOM   204  C  CA  . GLY A 1 28  ? 13.778  6.595   0.613  1    47.312  ? 64   GLY A CA  1 1 
ATOM   205  C  C   . GLY A 1 28  ? 12.692  7.665   0.681  1    52.745  ? 64   GLY A C   1 1 
ATOM   206  O  O   . GLY A 1 28  ? 12.969  8.805   1.043  1    56.047  ? 64   GLY A O   1 1 
ATOM   207  N  N   . ALA A 1 29  ? 11.453  7.281   0.359  1    53.35   ? 65   ALA A N   1 1 
ATOM   208  C  CA  . ALA A 1 29  ? 10.372  8.231   0.168  1    48.195  ? 65   ALA A CA  1 1 
ATOM   209  C  C   . ALA A 1 29  ? 10.103  8.905   1.497  1    47.322  ? 65   ALA A C   1 1 
ATOM   210  O  O   . ALA A 1 29  ? 9.992   10.112  1.584  1    52.335  ? 65   ALA A O   1 1 
ATOM   211  C  CB  . ALA A 1 29  ? 9.143   7.511   -0.331 1    47.407  ? 65   ALA A CB  1 1 
ATOM   212  N  N   . ASN A 1 30  ? 10.014  8.072   2.534  1    51.462  ? 66   ASN A N   1 1 
ATOM   213  C  CA  . ASN A 1 30  ? 9.806   8.471   3.906  1    45.102  ? 66   ASN A CA  1 1 
ATOM   214  C  C   . ASN A 1 30  ? 10.938  9.368   4.407  1    42.795  ? 66   ASN A C   1 1 
ATOM   215  O  O   . ASN A 1 30  ? 10.663  10.255  5.191  1    46.336  ? 66   ASN A O   1 1 
ATOM   216  C  CB  . ASN A 1 30  ? 9.561   7.24    4.76   1    46.837  ? 66   ASN A CB  1 1 
ATOM   217  C  CG  . ASN A 1 30  ? 9.029   7.564   6.134  1    48.988  ? 66   ASN A CG  1 1 
ATOM   218  O  OD1 . ASN A 1 30  ? 8.329   8.565   6.314  1    50.543  ? 66   ASN A OD1 1 1 
ATOM   219  N  ND2 . ASN A 1 30  ? 9.301   6.696   7.102  1    45.058  ? 66   ASN A ND2 1 1 
ATOM   220  N  N   . TRP A 1 31  ? 12.182  9.145   3.968  1    46.186  ? 67   TRP A N   1 1 
ATOM   221  C  CA  . TRP A 1 31  ? 13.329  9.961   4.354  1    48.953  ? 67   TRP A CA  1 1 
ATOM   222  C  C   . TRP A 1 31  ? 13.202  11.369  3.769  1    50.377  ? 67   TRP A C   1 1 
ATOM   223  O  O   . TRP A 1 31  ? 13.341  12.357  4.475  1    54.832  ? 67   TRP A O   1 1 
ATOM   224  C  CB  . TRP A 1 31  ? 14.636  9.34    3.845  1    52.29   ? 67   TRP A CB  1 1 
ATOM   225  C  CG  . TRP A 1 31  ? 15.821  10.229  4.127  1    61.688  ? 67   TRP A CG  1 1 
ATOM   226  C  CD1 . TRP A 1 31  ? 16.438  11.111  3.274  1    64.854  ? 67   TRP A CD1 1 1 
ATOM   227  C  CD2 . TRP A 1 31  ? 16.502  10.356  5.399  1    54.457  ? 67   TRP A CD2 1 1 
ATOM   228  N  NE1 . TRP A 1 31  ? 17.481  11.744  3.904  1    60.688  ? 67   TRP A NE1 1 1 
ATOM   229  C  CE2 . TRP A 1 31  ? 17.529  11.318  5.214  1    53.389  ? 67   TRP A CE2 1 1 
ATOM   230  C  CE3 . TRP A 1 31  ? 16.345  9.754   6.661  1    49.563  ? 67   TRP A CE3 1 1 
ATOM   231  C  CZ2 . TRP A 1 31  ? 18.395  11.663  6.247  1    47.846  ? 67   TRP A CZ2 1 1 
ATOM   232  C  CZ3 . TRP A 1 31  ? 17.193  10.115  7.696  1    44.189  ? 67   TRP A CZ3 1 1 
ATOM   233  C  CH2 . TRP A 1 31  ? 18.213  11.055  7.476  1    45.595  ? 67   TRP A CH2 1 1 
ATOM   234  N  N   . ASN A 1 32  ? 12.98   11.433  2.453  1    50.481  ? 68   ASN A N   1 1 
ATOM   235  C  CA  . ASN A 1 32  ? 12.801  12.667  1.693  1    49.561  ? 68   ASN A CA  1 1 
ATOM   236  C  C   . ASN A 1 32  ? 11.62   13.462  2.215  1    55.038  ? 68   ASN A C   1 1 
ATOM   237  O  O   . ASN A 1 32  ? 11.636  14.689  2.119  1    65.441  ? 68   ASN A O   1 1 
ATOM   238  C  CB  . ASN A 1 32  ? 12.334  12.381  0.287  1    46.606  ? 68   ASN A CB  1 1 
ATOM   239  C  CG  . ASN A 1 32  ? 13.474  11.727  -0.42  1    53.103  ? 68   ASN A CG  1 1 
ATOM   240  O  OD1 . ASN A 1 32  ? 14.58   11.715  0.124  1    56.237  ? 68   ASN A OD1 1 1 
ATOM   241  N  ND2 . ASN A 1 32  ? 13.236  11.169  -1.589 1    56.862  ? 68   ASN A ND2 1 1 
ATOM   242  N  N   . TYR A 1 33  ? 10.615  12.773  2.776  1    50.392  ? 69   TYR A N   1 1 
ATOM   243  C  CA  . TYR A 1 33  ? 9.508   13.531  3.324  1    50.862  ? 69   TYR A CA  1 1 
ATOM   244  C  C   . TYR A 1 33  ? 9.942   14.192  4.63   1    59.3    ? 69   TYR A C   1 1 
ATOM   245  O  O   . TYR A 1 33  ? 9.574   15.345  4.912  1    55.585  ? 69   TYR A O   1 1 
ATOM   246  C  CB  . TYR A 1 33  ? 8.269   12.665  3.492  1    45.426  ? 69   TYR A CB  1 1 
ATOM   247  C  CG  . TYR A 1 33  ? 7.219   13.334  4.366  1    48.842  ? 69   TYR A CG  1 1 
ATOM   248  C  CD1 . TYR A 1 33  ? 6.45    14.385  3.862  1    53.134  ? 69   TYR A CD1 1 1 
ATOM   249  C  CD2 . TYR A 1 33  ? 6.982   12.901  5.676  1    52.701  ? 69   TYR A CD2 1 1 
ATOM   250  C  CE1 . TYR A 1 33  ? 5.474   14.987  4.64   1    56.192  ? 69   TYR A CE1 1 1 
ATOM   251  C  CE2 . TYR A 1 33  ? 5.996   13.484  6.459  1    53.375  ? 69   TYR A CE2 1 1 
ATOM   252  C  CZ  . TYR A 1 33  ? 5.261   14.545  5.94   1    60.786  ? 69   TYR A CZ  1 1 
ATOM   253  O  OH  . TYR A 1 33  ? 4.293   15.171  6.674  1    62.012  ? 69   TYR A OH  1 1 
ATOM   254  N  N   . ASN A 1 34  ? 10.752  13.429  5.392  1    60.106  ? 70   ASN A N   1 1 
ATOM   255  C  CA  . ASN A 1 34  ? 11.091  13.723  6.775  1    53.58   ? 70   ASN A CA  1 1 
ATOM   256  C  C   . ASN A 1 34  ? 12.13   14.841  6.878  1    50.095  ? 70   ASN A C   1 1 
ATOM   257  O  O   . ASN A 1 34  ? 12.277  15.439  7.935  1    55.265  ? 70   ASN A O   1 1 
ATOM   258  C  CB  . ASN A 1 34  ? 11.491  12.45   7.52   1    60.065  ? 70   ASN A CB  1 1 
ATOM   259  C  CG  . ASN A 1 34  ? 10.3    11.611  7.94   1    49.229  ? 70   ASN A CG  1 1 
ATOM   260  O  OD1 . ASN A 1 34  ? 9.905   11.624  9.112  1    37.984  ? 70   ASN A OD1 1 1 
ATOM   261  N  ND2 . ASN A 1 34  ? 9.704   10.91   6.981  1    48.912  ? 70   ASN A ND2 1 1 
ATOM   262  N  N   . THR A 1 35  ? 12.845  15.098  5.785  1    46.753  ? 71   THR A N   1 1 
ATOM   263  C  CA  . THR A 1 35  ? 13.972  16.004  5.751  1    48.127  ? 71   THR A CA  1 1 
ATOM   264  C  C   . THR A 1 35  ? 13.723  16.999  4.62   1    60.579  ? 71   THR A C   1 1 
ATOM   265  O  O   . THR A 1 35  ? 14.639  17.324  3.846  1    58.813  ? 71   THR A O   1 1 
ATOM   266  C  CB  . THR A 1 35  ? 15.205  15.153  5.448  1    48.272  ? 71   THR A CB  1 1 
ATOM   267  O  OG1 . THR A 1 35  ? 15.165  14.632  4.103  1    41.926  ? 71   THR A OG1 1 1 
ATOM   268  C  CG2 . THR A 1 35  ? 15.399  14.087  6.514  1    45.505  ? 71   THR A CG2 1 1 
ATOM   269  N  N   . ASN A 1 36  ? 12.444  17.389  4.483  1    60.546  ? 72   ASN A N   1 1 
ATOM   270  C  CA  . ASN A 1 36  ? 11.953  18.213  3.384  1    54.798  ? 72   ASN A CA  1 1 
ATOM   271  C  C   . ASN A 1 36  ? 10.46   17.953  3.245  1    51.54   ? 72   ASN A C   1 1 
ATOM   272  O  O   . ASN A 1 36  ? 10.066  17.421  2.217  1    59.224  ? 72   ASN A O   1 1 
ATOM   273  C  CB  . ASN A 1 36  ? 12.727  18.005  2.074  1    62.766  ? 72   ASN A CB  1 1 
ATOM   274  C  CG  . ASN A 1 36  ? 12.479  19.077  1.025  1    71.622  ? 72   ASN A CG  1 1 
ATOM   275  O  OD1 . ASN A 1 36  ? 11.676  20.002  1.223  1    67.848  ? 72   ASN A OD1 1 1 
ATOM   276  N  ND2 . ASN A 1 36  ? 13.161  18.974  -0.107 1    75.454  ? 72   ASN A ND2 1 1 
ATOM   277  N  N   . ILE A 1 37  ? 9.671   18.222  4.305  1    49.384  ? 73   ILE A N   1 1 
ATOM   278  C  CA  . ILE A 1 37  ? 8.222   18.214  4.223  1    50.06   ? 73   ILE A CA  1 1 
ATOM   279  C  C   . ILE A 1 37  ? 7.824   19.23   3.144  1    63.901  ? 73   ILE A C   1 1 
ATOM   280  O  O   . ILE A 1 37  ? 8.167   20.411  3.261  1    68.699  ? 73   ILE A O   1 1 
ATOM   281  C  CB  . ILE A 1 37  ? 7.621   18.611  5.576  1    50.073  ? 73   ILE A CB  1 1 
ATOM   282  C  CG1 . ILE A 1 37  ? 8.167   17.763  6.714  1    55.401  ? 73   ILE A CG1 1 1 
ATOM   283  C  CG2 . ILE A 1 37  ? 6.096   18.629  5.526  1    49.506  ? 73   ILE A CG2 1 1 
ATOM   284  C  CD1 . ILE A 1 37  ? 7.419   17.894  8.036  1    51.082  ? 73   ILE A CD1 1 1 
ATOM   285  N  N   . THR A 1 38  ? 7.183   18.738  2.057  1    66.469  ? 74   THR A N   1 1 
ATOM   286  C  CA  . THR A 1 38  ? 6.588   19.512  0.967  1    57.885  ? 74   THR A CA  1 1 
ATOM   287  C  C   . THR A 1 38  ? 5.278   18.831  0.527  1    59.842  ? 74   THR A C   1 1 
ATOM   288  O  O   . THR A 1 38  ? 4.835   17.856  1.141  1    59.309  ? 74   THR A O   1 1 
ATOM   289  C  CB  . THR A 1 38  ? 7.578   19.741  -0.193 1    56.81   ? 74   THR A CB  1 1 
ATOM   290  O  OG1 . THR A 1 38  ? 7.609   18.724  -1.192 1    56.705  ? 74   THR A OG1 1 1 
ATOM   291  C  CG2 . THR A 1 38  ? 9.02    20.031  0.199  1    52.096  ? 74   THR A CG2 1 1 
ATOM   292  N  N   . THR A 1 39  ? 4.627   19.363  -0.525 1    64.263  ? 75   THR A N   1 1 
ATOM   293  C  CA  . THR A 1 39  ? 3.533   18.695  -1.236 1    66.534  ? 75   THR A CA  1 1 
ATOM   294  C  C   . THR A 1 39  ? 4.042   17.455  -1.976 1    59.806  ? 75   THR A C   1 1 
ATOM   295  O  O   . THR A 1 39  ? 3.569   16.35   -1.717 1    63.593  ? 75   THR A O   1 1 
ATOM   296  C  CB  . THR A 1 39  ? 2.857   19.671  -2.203 1    70.715  ? 75   THR A CB  1 1 
ATOM   297  O  OG1 . THR A 1 39  ? 2.369   20.592  -1.241 1    73.281  ? 75   THR A OG1 1 1 
ATOM   298  C  CG2 . THR A 1 39  ? 1.656   19.08   -2.926 1    68.605  ? 75   THR A CG2 1 1 
ATOM   299  N  N   . GLU A 1 40  ? 5.029   17.682  -2.854 1    57.18   ? 76   GLU A N   1 1 
ATOM   300  C  CA  . GLU A 1 40  ? 5.695   16.717  -3.711 1    62.478  ? 76   GLU A CA  1 1 
ATOM   301  C  C   . GLU A 1 40  ? 6.246   15.517  -2.933 1    62.98   ? 76   GLU A C   1 1 
ATOM   302  O  O   . GLU A 1 40  ? 5.979   14.368  -3.3   1    65.342  ? 76   GLU A O   1 1 
ATOM   303  C  CB  . GLU A 1 40  ? 6.779   17.452  -4.501 1    74.179  ? 76   GLU A CB  1 1 
ATOM   304  C  CG  . GLU A 1 40  ? 7.674   16.529  -5.326 1    92.18   ? 76   GLU A CG  1 1 
ATOM   305  C  CD  . GLU A 1 40  ? 7.062   15.882  -6.566 1    113.185 ? 76   GLU A CD  1 1 
ATOM   306  O  OE1 . GLU A 1 40  ? 5.838   16.063  -6.791 1    126.526 ? 76   GLU A OE1 1 1 
ATOM   307  O  OE2 . GLU A 1 40  ? 7.806   15.199  -7.319 1    108.995 ? 76   GLU A OE2 1 1 
ATOM   308  N  N   . THR A 1 41  ? 7.054   15.768  -1.891 1    60.932  ? 77   THR A N   1 1 
ATOM   309  C  CA  . THR A 1 41  ? 7.573   14.691  -1.048 1    60.967  ? 77   THR A CA  1 1 
ATOM   310  C  C   . THR A 1 41  ? 6.42    13.93   -0.372 1    58.904  ? 77   THR A C   1 1 
ATOM   311  O  O   . THR A 1 41  ? 6.425   12.696  -0.34  1    52.479  ? 77   THR A O   1 1 
ATOM   312  C  CB  . THR A 1 41  ? 8.684   15.122  -0.071 1    52.792  ? 77   THR A CB  1 1 
ATOM   313  O  OG1 . THR A 1 41  ? 8.076   16.053  0.824  1    46.281  ? 77   THR A OG1 1 1 
ATOM   314  C  CG2 . THR A 1 41  ? 9.974   15.542  -0.781 1    54.04   ? 77   THR A CG2 1 1 
ATOM   315  N  N   . SER A 1 42  ? 5.408   14.668  0.102  1    58.947  ? 78   SER A N   1 1 
ATOM   316  C  CA  . SER A 1 42  ? 4.256   14.036  0.726  1    58.199  ? 78   SER A CA  1 1 
ATOM   317  C  C   . SER A 1 42  ? 3.474   13.151  -0.268 1    58.609  ? 78   SER A C   1 1 
ATOM   318  O  O   . SER A 1 42  ? 3.084   12.039  0.094  1    52.426  ? 78   SER A O   1 1 
ATOM   319  C  CB  . SER A 1 42  ? 3.404   15.065  1.416  1    51.844  ? 78   SER A CB  1 1 
ATOM   320  O  OG  . SER A 1 42  ? 2.331   14.415  2.075  1    59.326  ? 78   SER A OG  1 1 
ATOM   321  N  N   . LYS A 1 43  ? 3.266   13.61   -1.525 1    59.372  ? 79   LYS A N   1 1 
ATOM   322  C  CA  . LYS A 1 43  ? 2.531   12.825  -2.52  1    65.666  ? 79   LYS A CA  1 1 
ATOM   323  C  C   . LYS A 1 43  ? 3.246   11.487  -2.718 1    68.851  ? 79   LYS A C   1 1 
ATOM   324  O  O   . LYS A 1 43  ? 2.618   10.443  -2.565 1    78.507  ? 79   LYS A O   1 1 
ATOM   325  C  CB  . LYS A 1 43  ? 2.36    13.351  -3.97  1    66.202  ? 79   LYS A CB  1 1 
ATOM   326  C  CG  . LYS A 1 43  ? 1.915   14.807  -4.21  1    72.49   ? 79   LYS A CG  1 1 
ATOM   327  C  CD  . LYS A 1 43  ? 2.169   15.374  -5.612 1    83.06   ? 79   LYS A CD  1 1 
ATOM   328  C  CE  . LYS A 1 43  ? 2.642   16.812  -5.821 1    84.56   ? 79   LYS A CE  1 1 
ATOM   329  N  NZ  . LYS A 1 43  ? 1.688   17.885  -5.513 1    83.196  ? 79   LYS A NZ  1 1 
ATOM   330  N  N   . ILE A 1 44  ? 4.537   11.543  -3.1   1    63.257  ? 80   ILE A N   1 1 
ATOM   331  C  CA  . ILE A 1 44  ? 5.359   10.37   -3.387 1    61.636  ? 80   ILE A CA  1 1 
ATOM   332  C  C   . ILE A 1 44  ? 5.346   9.388   -2.21  1    56.248  ? 80   ILE A C   1 1 
ATOM   333  O  O   . ILE A 1 44  ? 5.442   8.188   -2.443 1    49.6    ? 80   ILE A O   1 1 
ATOM   334  C  CB  . ILE A 1 44  ? 6.798   10.737  -3.841 1    63.358  ? 80   ILE A CB  1 1 
ATOM   335  C  CG1 . ILE A 1 44  ? 6.794   11.669  -5.063 1    62.406  ? 80   ILE A CG1 1 1 
ATOM   336  C  CG2 . ILE A 1 44  ? 7.681   9.504   -4.106 1    55.621  ? 80   ILE A CG2 1 1 
ATOM   337  C  CD1 . ILE A 1 44  ? 8.169   12.226  -5.379 1    64.974  ? 80   ILE A CD1 1 1 
ATOM   338  N  N   . LEU A 1 45  ? 5.244   9.902   -0.968 1    54.607  ? 81   LEU A N   1 1 
ATOM   339  C  CA  . LEU A 1 45  ? 5.202   9.075   0.233  1    55.562  ? 81   LEU A CA  1 1 
ATOM   340  C  C   . LEU A 1 45  ? 3.957   8.185   0.189  1    60.656  ? 81   LEU A C   1 1 
ATOM   341  O  O   . LEU A 1 45  ? 4.104   6.972   0.36   1    64.307  ? 81   LEU A O   1 1 
ATOM   342  C  CB  . LEU A 1 45  ? 5.384   9.733   1.617  1    49.279  ? 81   LEU A CB  1 1 
ATOM   343  C  CG  . LEU A 1 45  ? 5.363   8.808   2.845  1    43.091  ? 81   LEU A CG  1 1 
ATOM   344  C  CD1 . LEU A 1 45  ? 6.436   7.784   2.646  1    43.157  ? 81   LEU A CD1 1 1 
ATOM   345  C  CD2 . LEU A 1 45  ? 5.455   9.34    4.3    1    42.754  ? 81   LEU A CD2 1 1 
ATOM   346  N  N   . LEU A 1 46  ? 2.75    8.75    -0.031 1    57.956  ? 82   LEU A N   1 1 
ATOM   347  C  CA  . LEU A 1 46  ? 1.572   7.914   0.191  1    58.711  ? 82   LEU A CA  1 1 
ATOM   348  C  C   . LEU A 1 46  ? 1.41    6.957   -0.996 1    53.172  ? 82   LEU A C   1 1 
ATOM   349  O  O   . LEU A 1 46  ? 1.041   5.81    -0.849 1    54.681  ? 82   LEU A O   1 1 
ATOM   350  C  CB  . LEU A 1 46  ? 0.286   8.418   0.886  1    61.899  ? 82   LEU A CB  1 1 
ATOM   351  C  CG  . LEU A 1 46  ? 0.386   8.859   2.377  1    72.893  ? 82   LEU A CG  1 1 
ATOM   352  C  CD1 . LEU A 1 46  ? -0.892  8.828   3.313  1    67.782  ? 82   LEU A CD1 1 1 
ATOM   353  C  CD2 . LEU A 1 46  ? 1.63    8.446   3.234  1    64.506  ? 82   LEU A CD2 1 1 
ATOM   354  N  N   . GLN A 1 47  ? 1.873   7.371   -2.163 1    57.927  ? 83   GLN A N   1 1 
ATOM   355  C  CA  . GLN A 1 47  ? 2.016   6.461   -3.282 1    64.46   ? 83   GLN A CA  1 1 
ATOM   356  C  C   . GLN A 1 47  ? 2.917   5.275   -2.902 1    66.947  ? 83   GLN A C   1 1 
ATOM   357  O  O   . GLN A 1 47  ? 2.578   4.122   -3.19  1    58.85   ? 83   GLN A O   1 1 
ATOM   358  C  CB  . GLN A 1 47  ? 2.413   7.36    -4.448 1    68.689  ? 83   GLN A CB  1 1 
ATOM   359  C  CG  . GLN A 1 47  ? 2.401   6.679   -5.805 1    72.365  ? 83   GLN A CG  1 1 
ATOM   360  C  CD  . GLN A 1 47  ? 3.793   6.274   -6.214 1    76.635  ? 83   GLN A CD  1 1 
ATOM   361  O  OE1 . GLN A 1 47  ? 4.549   5.704   -5.418 1    71.577  ? 83   GLN A OE1 1 1 
ATOM   362  N  NE2 . GLN A 1 47  ? 4.159   6.646   -7.435 1    80.819  ? 83   GLN A NE2 1 1 
ATOM   363  N  N   . LYS A 1 48  ? 4.047   5.542   -2.218 1    58.59   ? 84   LYS A N   1 1 
ATOM   364  C  CA  . LYS A 1 48  ? 4.933   4.462   -1.787 1    56.141  ? 84   LYS A CA  1 1 
ATOM   365  C  C   . LYS A 1 48  ? 4.272   3.638   -0.673 1    50.16   ? 84   LYS A C   1 1 
ATOM   366  O  O   . LYS A 1 48  ? 4.626   2.482   -0.452 1    45.066  ? 84   LYS A O   1 1 
ATOM   367  C  CB  . LYS A 1 48  ? 6.345   4.867   -1.333 1    47.972  ? 84   LYS A CB  1 1 
ATOM   368  C  CG  . LYS A 1 48  ? 7.269   5.478   -2.345 1    48.305  ? 84   LYS A CG  1 1 
ATOM   369  C  CD  . LYS A 1 48  ? 7.517   4.76    -3.663 1    47.994  ? 84   LYS A CD  1 1 
ATOM   370  C  CE  . LYS A 1 48  ? 8.652   5.459   -4.336 1    50.116  ? 84   LYS A CE  1 1 
ATOM   371  N  NZ  . LYS A 1 48  ? 8.619   4.995   -5.719 1    51.982  ? 84   LYS A NZ  1 1 
ATOM   372  N  N   . ASN A 1 49  ? 3.288   4.223   0.008  1    49.583  ? 85   ASN A N   1 1 
ATOM   373  C  CA  . ASN A 1 49  ? 2.657   3.555   1.137  1    48.948  ? 85   ASN A CA  1 1 
ATOM   374  C  C   . ASN A 1 49  ? 1.863   2.377   0.588  1    50.904  ? 85   ASN A C   1 1 
ATOM   375  O  O   . ASN A 1 49  ? 1.946   1.288   1.137  1    47.164  ? 85   ASN A O   1 1 
ATOM   376  C  CB  . ASN A 1 49  ? 1.636   4.469   1.791  1    55.004  ? 85   ASN A CB  1 1 
ATOM   377  C  CG  . ASN A 1 49  ? 1.788   4.489   3.282  1    62.579  ? 85   ASN A CG  1 1 
ATOM   378  O  OD1 . ASN A 1 49  ? 2.745   3.92    3.801  1    69.747  ? 85   ASN A OD1 1 1 
ATOM   379  N  ND2 . ASN A 1 49  ? 0.884   5.158   3.977  1    69.519  ? 85   ASN A ND2 1 1 
ATOM   380  N  N   . MET A 1 50  ? 1.168   2.613   -0.547 1    53.386  ? 86   MET A N   1 1 
ATOM   381  C  CA  . MET A 1 50  ? 0.297   1.658   -1.213 1    55.473  ? 86   MET A CA  1 1 
ATOM   382  C  C   . MET A 1 50  ? 1.128   0.546   -1.858 1    48.946  ? 86   MET A C   1 1 
ATOM   383  O  O   . MET A 1 50  ? 0.725   -0.618  -1.84  1    45.372  ? 86   MET A O   1 1 
ATOM   384  C  CB  . MET A 1 50  ? -0.708  2.321   -2.193 1    63.161  ? 86   MET A CB  1 1 
ATOM   385  C  CG  . MET A 1 50  ? -2.003  2.925   -1.543 1    79.947  ? 86   MET A CG  1 1 
ATOM   386  S  SD  . MET A 1 50  ? -2.62   2.409   0.097  1    105.226 ? 86   MET A SD  1 1 
ATOM   387  C  CE  . MET A 1 50  ? -4.37   2.767   0.355  1    92.168  ? 86   MET A CE  1 1 
ATOM   388  N  N   . GLN A 1 51  ? 2.277   0.92    -2.442 1    48.316  ? 87   GLN A N   1 1 
ATOM   389  C  CA  . GLN A 1 51  ? 3.205   -0.039  -3.03  1    46.132  ? 87   GLN A CA  1 1 
ATOM   390  C  C   . GLN A 1 51  ? 3.685   -1.07   -1.996 1    44.279  ? 87   GLN A C   1 1 
ATOM   391  O  O   . GLN A 1 51  ? 3.738   -2.265  -2.292 1    48.2    ? 87   GLN A O   1 1 
ATOM   392  C  CB  . GLN A 1 51  ? 4.458   0.644   -3.559 1    46.132  ? 87   GLN A CB  1 1 
ATOM   393  C  CG  . GLN A 1 51  ? 5.225   -0.224  -4.549 1    50.055  ? 87   GLN A CG  1 1 
ATOM   394  C  CD  . GLN A 1 51  ? 6.623   0.276   -4.884 1    56.309  ? 87   GLN A CD  1 1 
ATOM   395  O  OE1 . GLN A 1 51  ? 7.356   0.875   -4.079 1    55.791  ? 87   GLN A OE1 1 1 
ATOM   396  N  NE2 . GLN A 1 51  ? 7.053   -0.065  -6.083 1    56.004  ? 87   GLN A NE2 1 1 
ATOM   397  N  N   . ILE A 1 52  ? 4.038   -0.633  -0.781 1    38.443  ? 88   ILE A N   1 1 
ATOM   398  C  CA  . ILE A 1 52  ? 4.578   -1.584  0.168  1    35.531  ? 88   ILE A CA  1 1 
ATOM   399  C  C   . ILE A 1 52  ? 3.432   -2.399  0.774  1    33.289  ? 88   ILE A C   1 1 
ATOM   400  O  O   . ILE A 1 52  ? 3.537   -3.603  1.017  1    30.874  ? 88   ILE A O   1 1 
ATOM   401  C  CB  . ILE A 1 52  ? 5.488   -0.886  1.2    1    40.285  ? 88   ILE A CB  1 1 
ATOM   402  C  CG1 . ILE A 1 52  ? 6.273   -1.902  2.007  1    40.587  ? 88   ILE A CG1 1 1 
ATOM   403  C  CG2 . ILE A 1 52  ? 4.732   0.092   2.093  1    36.547  ? 88   ILE A CG2 1 1 
ATOM   404  C  CD1 . ILE A 1 52  ? 7.279   -1.303  2.964  1    42.042  ? 88   ILE A CD1 1 1 
ATOM   405  N  N   . ALA A 1 53  ? 2.272   -1.762  0.934  1    35.758  ? 89   ALA A N   1 1 
ATOM   406  C  CA  . ALA A 1 53  ? 1.083   -2.478  1.383  1    36.952  ? 89   ALA A CA  1 1 
ATOM   407  C  C   . ALA A 1 53  ? 0.728   -3.587  0.385  1    38.487  ? 89   ALA A C   1 1 
ATOM   408  O  O   . ALA A 1 53  ? 0.502   -4.728  0.779  1    40.738  ? 89   ALA A O   1 1 
ATOM   409  C  CB  . ALA A 1 53  ? -0.076  -1.525  1.61   1    36.439  ? 89   ALA A CB  1 1 
ATOM   410  N  N   . GLN A 1 54  ? 0.763   -3.276  -0.907 1    36.328  ? 90   GLN A N   1 1 
ATOM   411  C  CA  . GLN A 1 54  ? 0.493   -4.323  -1.892 1    40.422  ? 90   GLN A CA  1 1 
ATOM   412  C  C   . GLN A 1 54  ? 1.512   -5.459  -1.851 1    36.94   ? 90   GLN A C   1 1 
ATOM   413  O  O   . GLN A 1 54  ? 1.152   -6.595  -2.117 1    39.701  ? 90   GLN A O   1 1 
ATOM   414  C  CB  . GLN A 1 54  ? 0.674   -3.936  -3.349 1    44.756  ? 90   GLN A CB  1 1 
ATOM   415  C  CG  . GLN A 1 54  ? -0.446  -3.074  -3.871 1    54.034  ? 90   GLN A CG  1 1 
ATOM   416  C  CD  . GLN A 1 54  ? -0.044  -2.583  -5.239 1    63.243  ? 90   GLN A CD  1 1 
ATOM   417  O  OE1 . GLN A 1 54  ? 0.483   -3.351  -6.068 1    61.212  ? 90   GLN A OE1 1 1 
ATOM   418  N  NE2 . GLN A 1 54  ? -0.184  -1.276  -5.415 1    62.564  ? 90   GLN A NE2 1 1 
ATOM   419  N  N   . HIS A 1 55  ? 2.785   -5.163  -1.579 1    33.363  ? 91   HIS A N   1 1 
ATOM   420  C  CA  . HIS A 1 55  ? 3.757   -6.228  -1.504 1    32.278  ? 91   HIS A CA  1 1 
ATOM   421  C  C   . HIS A 1 55  ? 3.546   -7.072  -0.241 1    30.69   ? 91   HIS A C   1 1 
ATOM   422  O  O   . HIS A 1 55  ? 3.664   -8.306  -0.276 1    30.917  ? 91   HIS A O   1 1 
ATOM   423  C  CB  . HIS A 1 55  ? 5.136   -5.573  -1.505 1    32.553  ? 91   HIS A CB  1 1 
ATOM   424  C  CG  . HIS A 1 55  ? 6.235   -6.484  -1.073 1    32.381  ? 91   HIS A CG  1 1 
ATOM   425  N  ND1 . HIS A 1 55  ? 7       -7.165  -1.991 1    32.892  ? 91   HIS A ND1 1 1 
ATOM   426  C  CD2 . HIS A 1 55  ? 6.734   -6.767  0.126  1    30.733  ? 91   HIS A CD2 1 1 
ATOM   427  C  CE1 . HIS A 1 55  ? 7.916   -7.872  -1.367 1    31.241  ? 91   HIS A CE1 1 1 
ATOM   428  N  NE2 . HIS A 1 55  ? 7.778   -7.627  -0.075 1    31.278  ? 91   HIS A NE2 1 1 
ATOM   429  N  N   . THR A 1 56  ? 3.282   -6.402  0.874  1    30.884  ? 92   THR A N   1 1 
ATOM   430  C  CA  . THR A 1 56  ? 2.973   -7.059  2.139  1    30.057  ? 92   THR A CA  1 1 
ATOM   431  C  C   . THR A 1 56  ? 1.796   -8.01   1.924  1    32.339  ? 92   THR A C   1 1 
ATOM   432  O  O   . THR A 1 56  ? 1.918   -9.176  2.227  1    32.683  ? 92   THR A O   1 1 
ATOM   433  C  CB  . THR A 1 56  ? 2.737   -6.028  3.253  1    32.119  ? 92   THR A CB  1 1 
ATOM   434  O  OG1 . THR A 1 56  ? 3.881   -5.169  3.292  1    30.111  ? 92   THR A OG1 1 1 
ATOM   435  C  CG2 . THR A 1 56  ? 2.657   -6.599  4.669  1    30.089  ? 92   THR A CG2 1 1 
ATOM   436  N  N   . LEU A 1 57  ? 0.719   -7.559  1.272  1    35.568  ? 93   LEU A N   1 1 
ATOM   437  C  CA  . LEU A 1 57  ? -0.449  -8.376  0.974  1    36.235  ? 93   LEU A CA  1 1 
ATOM   438  C  C   . LEU A 1 57  ? -0.082  -9.568  0.089  1    39.617  ? 93   LEU A C   1 1 
ATOM   439  O  O   . LEU A 1 57  ? -0.471  -10.7   0.338  1    40.815  ? 93   LEU A O   1 1 
ATOM   440  C  CB  . LEU A 1 57  ? -1.486  -7.483  0.288  1    38.196  ? 93   LEU A CB  1 1 
ATOM   441  C  CG  . LEU A 1 57  ? -2.883  -8.088  0.099  1    36.852  ? 93   LEU A CG  1 1 
ATOM   442  C  CD1 . LEU A 1 57  ? -3.409  -8.373  1.519  1    33.113  ? 93   LEU A CD1 1 1 
ATOM   443  C  CD2 . LEU A 1 57  ? -3.83   -7.23   -0.774 1    36.96   ? 93   LEU A CD2 1 1 
ATOM   444  N  N   . LYS A 1 58  ? 0.649   -9.32   -0.998 1    40.94   ? 94   LYS A N   1 1 
ATOM   445  C  CA  . LYS A 1 58  ? 0.954   -10.408 -1.906 1    40.232  ? 94   LYS A CA  1 1 
ATOM   446  C  C   . LYS A 1 58  ? 1.717   -11.502 -1.155 1    38.604  ? 94   LYS A C   1 1 
ATOM   447  O  O   . LYS A 1 58  ? 1.312   -12.669 -1.242 1    40.718  ? 94   LYS A O   1 1 
ATOM   448  C  CB  . LYS A 1 58  ? 1.715   -9.883  -3.124 1    38.695  ? 94   LYS A CB  1 1 
ATOM   449  C  CG  . LYS A 1 58  ? 2.038   -10.987 -4.059 1    37.235  ? 94   LYS A CG  1 1 
ATOM   450  C  CD  . LYS A 1 58  ? 2.956   -10.477 -5.153 1    43.205  ? 94   LYS A CD  1 1 
ATOM   451  C  CE  . LYS A 1 58  ? 2.451   -11.085 -6.399 1    45.578  ? 94   LYS A CE  1 1 
ATOM   452  N  NZ  . LYS A 1 58  ? 3.801   -11.447 -6.765 1    50.776  ? 94   LYS A NZ  1 1 
ATOM   453  N  N   . TYR A 1 59  ? 2.812   -11.11  -0.469 1    35.534  ? 95   TYR A N   1 1 
ATOM   454  C  CA  . TYR A 1 59  ? 3.735   -12.033 0.183  1    33.339  ? 95   TYR A CA  1 1 
ATOM   455  C  C   . TYR A 1 59  ? 3.039   -12.662 1.392  1    33.712  ? 95   TYR A C   1 1 
ATOM   456  O  O   . TYR A 1 59  ? 3.101   -13.882 1.584  1    31.221  ? 95   TYR A O   1 1 
ATOM   457  C  CB  . TYR A 1 59  ? 5.177   -11.602 0.45   1    30.368  ? 95   TYR A CB  1 1 
ATOM   458  C  CG  . TYR A 1 59  ? 5.891   -11.641 -0.883 1    31.492  ? 95   TYR A CG  1 1 
ATOM   459  C  CD1 . TYR A 1 59  ? 5.736   -10.606 -1.807 1    31.387  ? 95   TYR A CD1 1 1 
ATOM   460  C  CD2 . TYR A 1 59  ? 6.557   -12.798 -1.302 1    32.001  ? 95   TYR A CD2 1 1 
ATOM   461  C  CE1 . TYR A 1 59  ? 6.284   -10.684 -3.078 1    32.334  ? 95   TYR A CE1 1 1 
ATOM   462  C  CE2 . TYR A 1 59  ? 7.097   -12.89  -2.571 1    31.589  ? 95   TYR A CE2 1 1 
ATOM   463  C  CZ  . TYR A 1 59  ? 6.977   -11.826 -3.45  1    32.964  ? 95   TYR A CZ  1 1 
ATOM   464  O  OH  . TYR A 1 59  ? 7.503   -11.946 -4.711 1    34.48   ? 95   TYR A OH  1 1 
ATOM   465  N  N   . GLY A 1 60  ? 2.277   -11.835 2.112  1    32.408  ? 96   GLY A N   1 1 
ATOM   466  C  CA  . GLY A 1 60  ? 1.595   -12.26  3.322  1    33.568  ? 96   GLY A CA  1 1 
ATOM   467  C  C   . GLY A 1 60  ? 0.571   -13.37  3.075  1    38.269  ? 96   GLY A C   1 1 
ATOM   468  O  O   . GLY A 1 60  ? 0.513   -14.314 3.867  1    40.124  ? 96   GLY A O   1 1 
ATOM   469  N  N   . THR A 1 61  ? -0.241  -13.22  2.012  1    36.435  ? 97   THR A N   1 1 
ATOM   470  C  CA  . THR A 1 61  ? -1.224  -14.178 1.515  1    40.078  ? 97   THR A CA  1 1 
ATOM   471  C  C   . THR A 1 61  ? -0.539  -15.511 1.151  1    45.598  ? 97   THR A C   1 1 
ATOM   472  O  O   . THR A 1 61  ? -1.014  -16.572 1.604  1    44.023  ? 97   THR A O   1 1 
ATOM   473  C  CB  . THR A 1 61  ? -2.041  -13.602 0.34   1    38.603  ? 97   THR A CB  1 1 
ATOM   474  O  OG1 . THR A 1 61  ? -2.577  -12.378 0.839  1    37.411  ? 97   THR A OG1 1 1 
ATOM   475  C  CG2 . THR A 1 61  ? -3.129  -14.524 -0.194 1    37.486  ? 97   THR A CG2 1 1 
ATOM   476  N  N   . GLN A 1 62  ? 0.549   -15.483 0.348  1    40.784  ? 98   GLN A N   1 1 
ATOM   477  C  CA  . GLN A 1 62  ? 1.221   -16.736 0.016  1    41.06   ? 98   GLN A CA  1 1 
ATOM   478  C  C   . GLN A 1 62  ? 1.726   -17.402 1.283  1    38.663  ? 98   GLN A C   1 1 
ATOM   479  O  O   . GLN A 1 62  ? 1.644   -18.602 1.38   1    40.575  ? 98   GLN A O   1 1 
ATOM   480  C  CB  . GLN A 1 62  ? 2.435   -16.792 -0.913 1    43.204  ? 98   GLN A CB  1 1 
ATOM   481  C  CG  . GLN A 1 62  ? 2.112   -17.099 -2.365 1    52.183  ? 98   GLN A CG  1 1 
ATOM   482  C  CD  . GLN A 1 62  ? 3.335   -17.085 -3.268 1    61.27   ? 98   GLN A CD  1 1 
ATOM   483  O  OE1 . GLN A 1 62  ? 3.517   -18.008 -4.076 1    75.622  ? 98   GLN A OE1 1 1 
ATOM   484  N  NE2 . GLN A 1 62  ? 4.168   -16.046 -3.201 1    49.658  ? 98   GLN A NE2 1 1 
ATOM   485  N  N   . ALA A 1 63  ? 2.294   -16.647 2.212  1    35.667  ? 99   ALA A N   1 1 
ATOM   486  C  CA  . ALA A 1 63  ? 2.874   -17.237 3.416  1    38.526  ? 99   ALA A CA  1 1 
ATOM   487  C  C   . ALA A 1 63  ? 1.842   -17.98  4.283  1    39.295  ? 99   ALA A C   1 1 
ATOM   488  O  O   . ALA A 1 63  ? 2.172   -19.011 4.856  1    40.942  ? 99   ALA A O   1 1 
ATOM   489  C  CB  . ALA A 1 63  ? 3.604   -16.184 4.222  1    33.935  ? 99   ALA A CB  1 1 
ATOM   490  N  N   . ARG A 1 64  ? 0.623   -17.432 4.417  1    39.148  ? 100  ARG A N   1 1 
ATOM   491  C  CA  . ARG A 1 64  ? -0.558  -18.046 5.031  1    39.194  ? 100  ARG A CA  1 1 
ATOM   492  C  C   . ARG A 1 64  ? -0.987  -19.39  4.408  1    43.711  ? 100  ARG A C   1 1 
ATOM   493  O  O   . ARG A 1 64  ? -1.668  -20.176 5.067  1    43.771  ? 100  ARG A O   1 1 
ATOM   494  C  CB  . ARG A 1 64  ? -1.764  -17.108 4.89   1    35.407  ? 100  ARG A CB  1 1 
ATOM   495  C  CG  . ARG A 1 64  ? -1.556  -16.01  5.902  1    36.647  ? 100  ARG A CG  1 1 
ATOM   496  C  CD  . ARG A 1 64  ? -2.696  -15.025 5.904  1    37.77   ? 100  ARG A CD  1 1 
ATOM   497  N  NE  . ARG A 1 64  ? -2.334  -14.029 6.916  1    33.616  ? 100  ARG A NE  1 1 
ATOM   498  C  CZ  . ARG A 1 64  ? -3.211  -13.167 7.385  1    39.525  ? 100  ARG A CZ  1 1 
ATOM   499  N  NH1 . ARG A 1 64  ? -4.473  -13.314 7.006  1    44.25   ? 100  ARG A NH1 1 1 
ATOM   500  N  NH2 . ARG A 1 64  ? -2.872  -12.244 8.29   1    39.846  ? 100  ARG A NH2 1 1 
ATOM   501  N  N   . LYS A 1 65  ? -0.604  -19.685 3.154  1    48.001  ? 101  LYS A N   1 1 
ATOM   502  C  CA  . LYS A 1 65  ? -0.852  -20.989 2.542  1    46.082  ? 101  LYS A CA  1 1 
ATOM   503  C  C   . LYS A 1 65  ? 0.152   -22.049 2.988  1    45.619  ? 101  LYS A C   1 1 
ATOM   504  O  O   . LYS A 1 65  ? -0.014  -23.218 2.691  1    52.624  ? 101  LYS A O   1 1 
ATOM   505  C  CB  . LYS A 1 65  ? -0.707  -20.916 1.027  1    49.295  ? 101  LYS A CB  1 1 
ATOM   506  C  CG  . LYS A 1 65  ? -1.604  -19.921 0.341  1    59.084  ? 101  LYS A CG  1 1 
ATOM   507  C  CD  . LYS A 1 65  ? -1.262  -19.783 -1.137 1    66.864  ? 101  LYS A CD  1 1 
ATOM   508  C  CE  . LYS A 1 65  ? -2.197  -18.792 -1.757 1    77.084  ? 101  LYS A CE  1 1 
ATOM   509  N  NZ  . LYS A 1 65  ? -3.594  -19.084 -1.415 1    81.362  ? 101  LYS A NZ  1 1 
ATOM   510  N  N   . PHE A 1 66  ? 1.223   -21.677 3.669  1    45.4    ? 102  PHE A N   1 1 
ATOM   511  C  CA  . PHE A 1 66  ? 2.064   -22.701 4.262  1    47.602  ? 102  PHE A CA  1 1 
ATOM   512  C  C   . PHE A 1 66  ? 1.465   -23.122 5.594  1    54.863  ? 102  PHE A C   1 1 
ATOM   513  O  O   . PHE A 1 66  ? 1.172   -22.271 6.44   1    58.084  ? 102  PHE A O   1 1 
ATOM   514  C  CB  . PHE A 1 66  ? 3.486   -22.209 4.537  1    42.569  ? 102  PHE A CB  1 1 
ATOM   515  C  CG  . PHE A 1 66  ? 4.187   -22.128 3.191  1    44.665  ? 102  PHE A CG  1 1 
ATOM   516  C  CD1 . PHE A 1 66  ? 4.816   -23.255 2.65   1    43.126  ? 102  PHE A CD1 1 1 
ATOM   517  C  CD2 . PHE A 1 66  ? 4.171   -20.941 2.454  1    43.039  ? 102  PHE A CD2 1 1 
ATOM   518  C  CE1 . PHE A 1 66  ? 5.421   -23.205 1.395  1    46.314  ? 102  PHE A CE1 1 1 
ATOM   519  C  CE2 . PHE A 1 66  ? 4.8     -20.869 1.232  1    43.72   ? 102  PHE A CE2 1 1 
ATOM   520  C  CZ  . PHE A 1 66  ? 5.412   -22.018 0.686  1    49.565  ? 102  PHE A CZ  1 1 
ATOM   521  N  N   . ASP A 1 67  ? 1.274   -24.442 5.732  1    61.126  ? 103  ASP A N   1 1 
ATOM   522  C  CA  . ASP A 1 67  ? 1.237   -25.13  7.018  1    60.719  ? 103  ASP A CA  1 1 
ATOM   523  C  C   . ASP A 1 67  ? 2.628   -25.036 7.658  1    55.322  ? 103  ASP A C   1 1 
ATOM   524  O  O   . ASP A 1 67  ? 3.574   -25.713 7.278  1    60.818  ? 103  ASP A O   1 1 
ATOM   525  C  CB  . ASP A 1 67  ? 0.61    -26.521 6.88   1    64.154  ? 103  ASP A CB  1 1 
ATOM   526  C  CG  . ASP A 1 67  ? 0.187   -27.244 8.159  1    66.269  ? 103  ASP A CG  1 1 
ATOM   527  O  OD1 . ASP A 1 67  ? 0.379   -26.719 9.28   1    68.032  ? 103  ASP A OD1 1 1 
ATOM   528  O  OD2 . ASP A 1 67  ? -0.348  -28.347 8.031  1    74.431  ? 103  ASP A OD2 1 1 
ATOM   529  N  N   . VAL A 1 68  ? 2.764   -24.158 8.639  1    57.178  ? 104  VAL A N   1 1 
ATOM   530  C  CA  . VAL A 1 68  ? 4.032   -24.016 9.331  1    63.779  ? 104  VAL A CA  1 1 
ATOM   531  C  C   . VAL A 1 68  ? 4.247   -25.174 10.313 1    67.391  ? 104  VAL A C   1 1 
ATOM   532  O  O   . VAL A 1 68  ? 5.387   -25.454 10.703 1    64.317  ? 104  VAL A O   1 1 
ATOM   533  C  CB  . VAL A 1 68  ? 3.884   -22.639 10.005 1    57.695  ? 104  VAL A CB  1 1 
ATOM   534  C  CG1 . VAL A 1 68  ? 4.364   -22.609 11.443 1    56.264  ? 104  VAL A CG1 1 1 
ATOM   535  C  CG2 . VAL A 1 68  ? 4.528   -21.553 9.162  1    63.693  ? 104  VAL A CG2 1 1 
ATOM   536  N  N   . ASN A 1 69  ? 3.141   -25.83  10.718 1    70.548  ? 105  ASN A N   1 1 
ATOM   537  C  CA  . ASN A 1 69  ? 3.216   -27.072 11.477 1    69.166  ? 105  ASN A CA  1 1 
ATOM   538  C  C   . ASN A 1 69  ? 4.169   -28.001 10.742 1    66.481  ? 105  ASN A C   1 1 
ATOM   539  O  O   . ASN A 1 69  ? 5.17    -28.397 11.324 1    72.33   ? 105  ASN A O   1 1 
ATOM   540  C  CB  . ASN A 1 69  ? 1.852   -27.663 11.842 1    63.835  ? 105  ASN A CB  1 1 
ATOM   541  C  CG  . ASN A 1 69  ? 1.092   -26.767 12.795 1    64.668  ? 105  ASN A CG  1 1 
ATOM   542  O  OD1 . ASN A 1 69  ? 1.664   -25.859 13.413 1    63.738  ? 105  ASN A OD1 1 1 
ATOM   543  N  ND2 . ASN A 1 69  ? -0.199  -26.986 12.935 1    63.572  ? 105  ASN A ND2 1 1 
ATOM   544  N  N   . GLN A 1 70  ? 3.895   -28.21  9.447  1    67.863  ? 106  GLN A N   1 1 
ATOM   545  C  CA  . GLN A 1 70  ? 4.633   -29.108 8.56   1    72.907  ? 106  GLN A CA  1 1 
ATOM   546  C  C   . GLN A 1 70  ? 6.076   -28.686 8.214  1    69.342  ? 106  GLN A C   1 1 
ATOM   547  O  O   . GLN A 1 70  ? 6.799   -29.482 7.619  1    66.986  ? 106  GLN A O   1 1 
ATOM   548  C  CB  . GLN A 1 70  ? 3.819   -29.353 7.283  1    78.356  ? 106  GLN A CB  1 1 
ATOM   549  C  CG  . GLN A 1 70  ? 2.444   -29.97  7.539  1    88.788  ? 106  GLN A CG  1 1 
ATOM   550  C  CD  . GLN A 1 70  ? 2.483   -31.347 8.181  1    87.962  ? 106  GLN A CD  1 1 
ATOM   551  O  OE1 . GLN A 1 70  ? 2.939   -32.324 7.573  1    89.569  ? 106  GLN A OE1 1 1 
ATOM   552  N  NE2 . GLN A 1 70  ? 1.99    -31.449 9.411  1    75.97   ? 106  GLN A NE2 1 1 
ATOM   553  N  N   . LEU A 1 71  ? 6.521   -27.461 8.55   1    69.059  ? 107  LEU A N   1 1 
ATOM   554  C  CA  . LEU A 1 71  ? 7.833   -26.984 8.111  1    62.522  ? 107  LEU A CA  1 1 
ATOM   555  C  C   . LEU A 1 71  ? 8.889   -27.455 9.09   1    59.616  ? 107  LEU A C   1 1 
ATOM   556  O  O   . LEU A 1 71  ? 8.764   -27.201 10.278 1    63.185  ? 107  LEU A O   1 1 
ATOM   557  C  CB  . LEU A 1 71  ? 7.995   -25.475 7.893  1    63.06   ? 107  LEU A CB  1 1 
ATOM   558  C  CG  . LEU A 1 71  ? 7.084   -24.852 6.827  1    65.954  ? 107  LEU A CG  1 1 
ATOM   559  C  CD1 . LEU A 1 71  ? 7.307   -23.363 6.616  1    58.264  ? 107  LEU A CD1 1 1 
ATOM   560  C  CD2 . LEU A 1 71  ? 7.175   -25.62  5.517  1    62.805  ? 107  LEU A CD2 1 1 
ATOM   561  N  N   . GLN A 1 72  ? 9.954   -28.033 8.535  1    56.482  ? 108  GLN A N   1 1 
ATOM   562  C  CA  . GLN A 1 72  ? 11.057  -28.649 9.257  1    61.93   ? 108  GLN A CA  1 1 
ATOM   563  C  C   . GLN A 1 72  ? 12.017  -27.578 9.747  1    54.528  ? 108  GLN A C   1 1 
ATOM   564  O  O   . GLN A 1 72  ? 11.875  -27.132 10.875 1    64.241  ? 108  GLN A O   1 1 
ATOM   565  C  CB  . GLN A 1 72  ? 11.852  -29.618 8.376  1    68.614  ? 108  GLN A CB  1 1 
ATOM   566  C  CG  . GLN A 1 72  ? 11.073  -30.856 7.943  1    87.749  ? 108  GLN A CG  1 1 
ATOM   567  C  CD  . GLN A 1 72  ? 10.665  -31.688 9.137  1    99.077  ? 108  GLN A CD  1 1 
ATOM   568  O  OE1 . GLN A 1 72  ? 11.516  -32.25  9.838  1    100.317 ? 108  GLN A OE1 1 1 
ATOM   569  N  NE2 . GLN A 1 72  ? 9.365   -31.726 9.407  1    99.876  ? 108  GLN A NE2 1 1 
ATOM   570  N  N   . ASN A 1 73  ? 12.967  -27.203 8.875  1    53.577  ? 109  ASN A N   1 1 
ATOM   571  C  CA  . ASN A 1 73  ? 13.888  -26.082 8.999  1    56.907  ? 109  ASN A CA  1 1 
ATOM   572  C  C   . ASN A 1 73  ? 13.295  -24.962 9.858  1    50.614  ? 109  ASN A C   1 1 
ATOM   573  O  O   . ASN A 1 73  ? 12.179  -24.494 9.615  1    55.526  ? 109  ASN A O   1 1 
ATOM   574  C  CB  . ASN A 1 73  ? 14.362  -25.571 7.639  1    54.468  ? 109  ASN A CB  1 1 
ATOM   575  C  CG  . ASN A 1 73  ? 15.472  -24.57  7.837  1    59.722  ? 109  ASN A CG  1 1 
ATOM   576  O  OD1 . ASN A 1 73  ? 15.197  -23.424 8.215  1    63.485  ? 109  ASN A OD1 1 1 
ATOM   577  N  ND2 . ASN A 1 73  ? 16.72   -24.977 7.629  1    62.799  ? 109  ASN A ND2 1 1 
ATOM   578  N  N   . THR A 1 74  ? 14.056  -24.51  10.851 1    47.289  ? 110  THR A N   1 1 
ATOM   579  C  CA  . THR A 1 74  ? 13.466  -23.59  11.812 1    49.906  ? 110  THR A CA  1 1 
ATOM   580  C  C   . THR A 1 74  ? 13.639  -22.134 11.374 1    48.762  ? 110  THR A C   1 1 
ATOM   581  O  O   . THR A 1 74  ? 12.711  -21.354 11.574 1    44.551  ? 110  THR A O   1 1 
ATOM   582  C  CB  . THR A 1 74  ? 13.82   -23.844 13.29  1    48.58   ? 110  THR A CB  1 1 
ATOM   583  O  OG1 . THR A 1 74  ? 15.215  -23.597 13.353 1    50.346  ? 110  THR A OG1 1 1 
ATOM   584  C  CG2 . THR A 1 74  ? 13.415  -25.223 13.799 1    46.998  ? 110  THR A CG2 1 1 
ATOM   585  N  N   . THR A 1 75  ? 14.795  -21.76  10.801 1    49.765  ? 111  THR A N   1 1 
ATOM   586  C  CA  . THR A 1 75  ? 14.946  -20.425 10.222 1    47.23   ? 111  THR A CA  1 1 
ATOM   587  C  C   . THR A 1 75  ? 13.765  -20.106 9.28   1    47.586  ? 111  THR A C   1 1 
ATOM   588  O  O   . THR A 1 75  ? 13.219  -18.988 9.316  1    42.335  ? 111  THR A O   1 1 
ATOM   589  C  CB  . THR A 1 75  ? 16.27   -20.324 9.47   1    44.785  ? 111  THR A CB  1 1 
ATOM   590  O  OG1 . THR A 1 75  ? 17.272  -20.542 10.444 1    47.958  ? 111  THR A OG1 1 1 
ATOM   591  C  CG2 . THR A 1 75  ? 16.59   -18.908 9.026  1    43.562  ? 111  THR A CG2 1 1 
ATOM   592  N  N   . ILE A 1 76  ? 13.39   -21.076 8.419  1    44.218  ? 112  ILE A N   1 1 
ATOM   593  C  CA  . ILE A 1 76  ? 12.382  -20.858 7.395  1    41.722  ? 112  ILE A CA  1 1 
ATOM   594  C  C   . ILE A 1 76  ? 10.988  -20.795 8.016  1    47.551  ? 112  ILE A C   1 1 
ATOM   595  O  O   . ILE A 1 76  ? 10.165  -19.946 7.623  1    42.992  ? 112  ILE A O   1 1 
ATOM   596  C  CB  . ILE A 1 76  ? 12.507  -21.893 6.272  1    41.442  ? 112  ILE A CB  1 1 
ATOM   597  C  CG1 . ILE A 1 76  ? 13.694  -21.523 5.393  1    41.343  ? 112  ILE A CG1 1 1 
ATOM   598  C  CG2 . ILE A 1 76  ? 11.214  -21.983 5.469  1    41.672  ? 112  ILE A CG2 1 1 
ATOM   599  C  CD1 . ILE A 1 76  ? 14.385  -22.703 4.751  1    42.118  ? 112  ILE A CD1 1 1 
ATOM   600  N  N   . LYS A 1 77  ? 10.728  -21.694 8.978  1    47.574  ? 113  LYS A N   1 1 
ATOM   601  C  CA  . LYS A 1 77  ? 9.474   -21.673 9.728  1    46.687  ? 113  LYS A CA  1 1 
ATOM   602  C  C   . LYS A 1 77  ? 9.27    -20.284 10.336 1    41.103  ? 113  LYS A C   1 1 
ATOM   603  O  O   . LYS A 1 77  ? 8.164   -19.738 10.357 1    38.172  ? 113  LYS A O   1 1 
ATOM   604  C  CB  . LYS A 1 77  ? 9.551   -22.65  10.918 1    51.742  ? 113  LYS A CB  1 1 
ATOM   605  C  CG  . LYS A 1 77  ? 8.272   -23.308 11.455 1    62.279  ? 113  LYS A CG  1 1 
ATOM   606  C  CD  . LYS A 1 77  ? 8.566   -24.15  12.7   1    68.631  ? 113  LYS A CD  1 1 
ATOM   607  C  CE  . LYS A 1 77  ? 7.817   -25.431 12.877 1    67.196  ? 113  LYS A CE  1 1 
ATOM   608  N  NZ  . LYS A 1 77  ? 6.401   -25.236 13.214 1    66.505  ? 113  LYS A NZ  1 1 
ATOM   609  N  N   . ARG A 1 78  ? 10.344  -19.744 10.901 1    36.864  ? 114  ARG A N   1 1 
ATOM   610  C  CA  . ARG A 1 78  ? 10.295  -18.477 11.636 1    38.387  ? 114  ARG A CA  1 1 
ATOM   611  C  C   . ARG A 1 78  ? 10.046  -17.292 10.692 1    39.124  ? 114  ARG A C   1 1 
ATOM   612  O  O   . ARG A 1 78  ? 9.326   -16.331 11.008 1    32.48   ? 114  ARG A O   1 1 
ATOM   613  C  CB  . ARG A 1 78  ? 11.722  -18.247 12.149 1    33.913  ? 114  ARG A CB  1 1 
ATOM   614  C  CG  . ARG A 1 78  ? 11.804  -17.227 13.267 1    35.299  ? 114  ARG A CG  1 1 
ATOM   615  C  CD  . ARG A 1 78  ? 12.96   -17.53  14.193 1    34.06   ? 114  ARG A CD  1 1 
ATOM   616  N  NE  . ARG A 1 78  ? 13.175  -16.41  15.121 1    35.816  ? 114  ARG A NE  1 1 
ATOM   617  C  CZ  . ARG A 1 78  ? 12.446  -16.104 16.189 1    31.73   ? 114  ARG A CZ  1 1 
ATOM   618  N  NH1 . ARG A 1 78  ? 11.4    -16.828 16.497 1    28.312  ? 114  ARG A NH1 1 1 
ATOM   619  N  NH2 . ARG A 1 78  ? 12.788  -15.066 16.937 1    33.235  ? 114  ARG A NH2 1 1 
ATOM   620  N  N   . ILE A 1 79  ? 10.777  -17.31  9.57   1    37.303  ? 115  ILE A N   1 1 
ATOM   621  C  CA  . ILE A 1 79  ? 10.641  -16.286 8.542  1    36.507  ? 115  ILE A CA  1 1 
ATOM   622  C  C   . ILE A 1 79  ? 9.218   -16.282 8.01   1    32.386  ? 115  ILE A C   1 1 
ATOM   623  O  O   . ILE A 1 79  ? 8.608   -15.226 7.905  1    33.304  ? 115  ILE A O   1 1 
ATOM   624  C  CB  . ILE A 1 79  ? 11.682  -16.495 7.427  1    38.434  ? 115  ILE A CB  1 1 
ATOM   625  C  CG1 . ILE A 1 79  ? 13.14   -16.182 7.936  1    33.835  ? 115  ILE A CG1 1 1 
ATOM   626  C  CG2 . ILE A 1 79  ? 11.306  -15.67  6.197  1    37.655  ? 115  ILE A CG2 1 1 
ATOM   627  C  CD1 . ILE A 1 79  ? 14.25   -16.62  6.969  1    34.139  ? 115  ILE A CD1 1 1 
ATOM   628  N  N   . ILE A 1 80  ? 8.672   -17.46  7.72   1    34.47   ? 116  ILE A N   1 1 
ATOM   629  C  CA  . ILE A 1 80  ? 7.354   -17.542 7.104  1    34.026  ? 116  ILE A CA  1 1 
ATOM   630  C  C   . ILE A 1 80  ? 6.281   -17.143 8.11   1    38.755  ? 116  ILE A C   1 1 
ATOM   631  O  O   . ILE A 1 80  ? 5.246   -16.633 7.691  1    35.521  ? 116  ILE A O   1 1 
ATOM   632  C  CB  . ILE A 1 80  ? 7.061   -18.929 6.518  1    36.697  ? 116  ILE A CB  1 1 
ATOM   633  C  CG1 . ILE A 1 80  ? 7.904   -19.145 5.26   1    37.799  ? 116  ILE A CG1 1 1 
ATOM   634  C  CG2 . ILE A 1 80  ? 5.548   -19.197 6.303  1    35.532  ? 116  ILE A CG2 1 1 
ATOM   635  C  CD1 . ILE A 1 80  ? 7.81    -20.543 4.68   1    41.094  ? 116  ILE A CD1 1 1 
ATOM   636  N  N   . LYS A 1 81  ? 6.52    -17.395 9.411  1    39.622  ? 117  LYS A N   1 1 
ATOM   637  C  CA  . LYS A 1 81  ? 5.522   -16.982 10.396 1    45.854  ? 117  LYS A CA  1 1 
ATOM   638  C  C   . LYS A 1 81  ? 5.484   -15.461 10.536 1    38.373  ? 117  LYS A C   1 1 
ATOM   639  O  O   . LYS A 1 81  ? 4.42    -14.888 10.649 1    40.47   ? 117  LYS A O   1 1 
ATOM   640  C  CB  . LYS A 1 81  ? 5.651   -17.513 11.822 1    53.797  ? 117  LYS A CB  1 1 
ATOM   641  C  CG  . LYS A 1 81  ? 4.935   -18.8   12.091 1    65.367  ? 117  LYS A CG  1 1 
ATOM   642  C  CD  . LYS A 1 81  ? 5.125   -18.987 13.59  1    82.487  ? 117  LYS A CD  1 1 
ATOM   643  C  CE  . LYS A 1 81  ? 5.846   -20.282 13.831 1    87.386  ? 117  LYS A CE  1 1 
ATOM   644  N  NZ  . LYS A 1 81  ? 5.675   -20.722 15.216 1    84.52   ? 117  LYS A NZ  1 1 
ATOM   645  N  N   . LYS A 1 82  ? 6.627   -14.797 10.5   1    38.737  ? 118  LYS A N   1 1 
ATOM   646  C  CA  . LYS A 1 82  ? 6.623   -13.348 10.404 1    40.127  ? 118  LYS A CA  1 1 
ATOM   647  C  C   . LYS A 1 82  ? 5.898   -12.822 9.146  1    41.406  ? 118  LYS A C   1 1 
ATOM   648  O  O   . LYS A 1 82  ? 5.055   -11.933 9.263  1    42.054  ? 118  LYS A O   1 1 
ATOM   649  C  CB  . LYS A 1 82  ? 8.045   -12.808 10.463 1    43.255  ? 118  LYS A CB  1 1 
ATOM   650  C  CG  . LYS A 1 82  ? 7.974   -11.28  10.416 1    54.837  ? 118  LYS A CG  1 1 
ATOM   651  C  CD  . LYS A 1 82  ? 9.231   -10.624 10.969 1    60.078  ? 118  LYS A CD  1 1 
ATOM   652  C  CE  . LYS A 1 82  ? 9.709   -11.39  12.166 1    54.838  ? 118  LYS A CE  1 1 
ATOM   653  N  NZ  . LYS A 1 82  ? 9.411   -10.74  13.443 1    51.214  ? 118  LYS A NZ  1 1 
ATOM   654  N  N   . VAL A 1 83  ? 6.176   -13.369 7.945  1    35.424  ? 119  VAL A N   1 1 
ATOM   655  C  CA  . VAL A 1 83  ? 5.525   -12.862 6.748  1    33.664  ? 119  VAL A CA  1 1 
ATOM   656  C  C   . VAL A 1 83  ? 3.997   -12.957 6.804  1    36.988  ? 119  VAL A C   1 1 
ATOM   657  O  O   . VAL A 1 83  ? 3.288   -12.202 6.122  1    38.567  ? 119  VAL A O   1 1 
ATOM   658  C  CB  . VAL A 1 83  ? 6.068   -13.488 5.464  1    29.984  ? 119  VAL A CB  1 1 
ATOM   659  C  CG1 . VAL A 1 83  ? 5.254   -13.028 4.263  1    31.035  ? 119  VAL A CG1 1 1 
ATOM   660  C  CG2 . VAL A 1 83  ? 7.536   -13.168 5.312  1    28.572  ? 119  VAL A CG2 1 1 
ATOM   661  N  N   . GLN A 1 84  ? 3.463   -13.89  7.595  1    37.478  ? 120  GLN A N   1 1 
ATOM   662  C  CA  . GLN A 1 84  ? 2.02    -14.081 7.618  1    38.105  ? 120  GLN A CA  1 1 
ATOM   663  C  C   . GLN A 1 84  ? 1.299   -12.972 8.392  1    35.891  ? 120  GLN A C   1 1 
ATOM   664  O  O   . GLN A 1 84  ? 0.062   -12.922 8.406  1    37.865  ? 120  GLN A O   1 1 
ATOM   665  C  CB  . GLN A 1 84  ? 1.747   -15.396 8.352  1    41.413  ? 120  GLN A CB  1 1 
ATOM   666  C  CG  . GLN A 1 84  ? 1.811   -16.63  7.453  1    42.249  ? 120  GLN A CG  1 1 
ATOM   667  C  CD  . GLN A 1 84  ? 1.726   -17.915 8.234  1    43.209  ? 120  GLN A CD  1 1 
ATOM   668  O  OE1 . GLN A 1 84  ? 1.745   -17.898 9.469  1    41.756  ? 120  GLN A OE1 1 1 
ATOM   669  N  NE2 . GLN A 1 84  ? 1.68    -19.028 7.515  1    43.423  ? 120  GLN A NE2 1 1 
ATOM   670  N  N   . ASP A 1 85  ? 2.061   -12.132 9.084  1    32.431  ? 121  ASP A N   1 1 
ATOM   671  C  CA  . ASP A 1 85  ? 1.494   -10.948 9.696  1    31.7    ? 121  ASP A CA  1 1 
ATOM   672  C  C   . ASP A 1 85  ? 1.491   -9.793  8.688  1    31.503  ? 121  ASP A C   1 1 
ATOM   673  O  O   . ASP A 1 85  ? 2.545   -9.276  8.363  1    31.578  ? 121  ASP A O   1 1 
ATOM   674  C  CB  . ASP A 1 85  ? 2.376   -10.415 10.811 1    32.102  ? 121  ASP A CB  1 1 
ATOM   675  C  CG  . ASP A 1 85  ? 1.611   -9.502  11.754 1    36.191  ? 121  ASP A CG  1 1 
ATOM   676  O  OD1 . ASP A 1 85  ? 0.562   -8.934  11.36  1    38.443  ? 121  ASP A OD1 1 1 
ATOM   677  O  OD2 . ASP A 1 85  ? 1.998   -9.443  12.912 1    44.061  ? 121  ASP A OD2 1 1 
ATOM   678  N  N   . LEU A 1 86  ? 0.312   -9.287  8.307  1    31.152  ? 122  LEU A N   1 1 
ATOM   679  C  CA  . LEU A 1 86  ? 0.199   -8.281  7.251  1    32.494  ? 122  LEU A CA  1 1 
ATOM   680  C  C   . LEU A 1 86  ? 0.329   -6.885  7.867  1    32.356  ? 122  LEU A C   1 1 
ATOM   681  O  O   . LEU A 1 86  ? 0.405   -5.914  7.122  1    31.612  ? 122  LEU A O   1 1 
ATOM   682  C  CB  . LEU A 1 86  ? -1.139  -8.424  6.509  1    31.347  ? 122  LEU A CB  1 1 
ATOM   683  C  CG  . LEU A 1 86  ? -1.292  -9.545  5.469  1    37.685  ? 122  LEU A CG  1 1 
ATOM   684  C  CD1 . LEU A 1 86  ? -0.678  -10.882 5.811  1    40.806  ? 122  LEU A CD1 1 1 
ATOM   685  C  CD2 . LEU A 1 86  ? -2.775  -9.785  5.154  1    39.282  ? 122  LEU A CD2 1 1 
ATOM   686  N  N   . GLU A 1 87  ? 0.336   -6.798  9.215  1    29.472  ? 123  GLU A N   1 1 
ATOM   687  C  CA  . GLU A 1 87  ? 0.084   -5.562  9.918  1    28.38   ? 123  GLU A CA  1 1 
ATOM   688  C  C   . GLU A 1 87  ? -1.089  -4.82   9.25   1    30.481  ? 123  GLU A C   1 1 
ATOM   689  O  O   . GLU A 1 87  ? -2.132  -5.415  8.988  1    33.811  ? 123  GLU A O   1 1 
ATOM   690  C  CB  . GLU A 1 87  ? 1.462   -4.887  9.865  1    35.732  ? 123  GLU A CB  1 1 
ATOM   691  C  CG  . GLU A 1 87  ? 2.507   -5.554  10.77  1    45.634  ? 123  GLU A CG  1 1 
ATOM   692  C  CD  . GLU A 1 87  ? 2.206   -5.291  12.259 1    56.909  ? 123  GLU A CD  1 1 
ATOM   693  O  OE1 . GLU A 1 87  ? 2.886   -5.752  13.211 1    52.318  ? 123  GLU A OE1 1 1 
ATOM   694  O  OE2 . GLU A 1 87  ? 1.228   -4.54   12.472 1    61.158  ? 123  GLU A OE2 1 1 
ATOM   695  N  N   . ARG A 1 88  ? -0.927  -3.522  8.905  1    29.042  ? 124  ARG A N   1 1 
ATOM   696  C  CA  . ARG A 1 88  ? -2.057  -2.68   8.516  1    29.483  ? 124  ARG A CA  1 1 
ATOM   697  C  C   . ARG A 1 88  ? -2.513  -3.122  7.128  1    29.785  ? 124  ARG A C   1 1 
ATOM   698  O  O   . ARG A 1 88  ? -3.637  -2.849  6.698  1    31.16   ? 124  ARG A O   1 1 
ATOM   699  C  CB  . ARG A 1 88  ? -1.622  -1.215  8.608  1    31.757  ? 124  ARG A CB  1 1 
ATOM   700  C  CG  . ARG A 1 88  ? -0.616  -0.95   7.479  1    37.944  ? 124  ARG A CG  1 1 
ATOM   701  C  CD  . ARG A 1 88  ? 0.032   0.459   7.244  1    39.826  ? 124  ARG A CD  1 1 
ATOM   702  N  NE  . ARG A 1 88  ? 0.942   0.653   8.372  1    46.409  ? 124  ARG A NE  1 1 
ATOM   703  C  CZ  . ARG A 1 88  ? 1.385   1.805   8.873  1    54.015  ? 124  ARG A CZ  1 1 
ATOM   704  N  NH1 . ARG A 1 88  ? 1.157   2.942   8.232  1    55.784  ? 124  ARG A NH1 1 1 
ATOM   705  N  NH2 . ARG A 1 88  ? 2.068   1.809   10.004 1    48.124  ? 124  ARG A NH2 1 1 
ATOM   706  N  N   . ALA A 1 89  ? -1.667  -3.898  6.444  1    29.972  ? 125  ALA A N   1 1 
ATOM   707  C  CA  . ALA A 1 89  ? -2.033  -4.342  5.085  1    32.901  ? 125  ALA A CA  1 1 
ATOM   708  C  C   . ALA A 1 89  ? -3.17   -5.377  5.113  1    33.907  ? 125  ALA A C   1 1 
ATOM   709  O  O   . ALA A 1 89  ? -3.654  -5.797  4.07   1    32.938  ? 125  ALA A O   1 1 
ATOM   710  C  CB  . ALA A 1 89  ? -0.802  -4.846  4.327  1    29.114  ? 125  ALA A CB  1 1 
ATOM   711  N  N   . ALA A 1 90  ? -3.606  -5.785  6.314  1    32.028  ? 126  ALA A N   1 1 
ATOM   712  C  CA  . ALA A 1 90  ? -4.716  -6.729  6.439  1    31.519  ? 126  ALA A CA  1 1 
ATOM   713  C  C   . ALA A 1 90  ? -6.009  -5.951  6.207  1    30.777  ? 126  ALA A C   1 1 
ATOM   714  O  O   . ALA A 1 90  ? -7.032  -6.51   5.836  1    31.527  ? 126  ALA A O   1 1 
ATOM   715  C  CB  . ALA A 1 90  ? -4.656  -7.405  7.838  1    30.495  ? 126  ALA A CB  1 1 
ATOM   716  N  N   . LEU A 1 91  ? -5.976  -4.621  6.396  1    29.661  ? 127  LEU A N   1 1 
ATOM   717  C  CA  . LEU A 1 91  ? -7.244  -3.89   6.439  1    28.189  ? 127  LEU A CA  1 1 
ATOM   718  C  C   . LEU A 1 91  ? -7.851  -3.849  5.053  1    29.518  ? 127  LEU A C   1 1 
ATOM   719  O  O   . LEU A 1 91  ? -7.103  -3.707  4.119  1    29.665  ? 127  LEU A O   1 1 
ATOM   720  C  CB  . LEU A 1 91  ? -7.11   -2.456  6.94   1    25.974  ? 127  LEU A CB  1 1 
ATOM   721  C  CG  . LEU A 1 91  ? -6.669  -2.299  8.399  1    25.091  ? 127  LEU A CG  1 1 
ATOM   722  C  CD1 . LEU A 1 91  ? -6.023  -0.894  8.634  1    24.023  ? 127  LEU A CD1 1 1 
ATOM   723  C  CD2 . LEU A 1 91  ? -7.923  -2.512  9.249  1    22.805  ? 127  LEU A CD2 1 1 
ATOM   724  N  N   . PRO A 1 92  ? -9.191  -3.77   4.895  1    31.769  ? 128  PRO A N   1 1 
ATOM   725  C  CA  . PRO A 1 92  ? -9.778  -3.438  3.579  1    34.083  ? 128  PRO A CA  1 1 
ATOM   726  C  C   . PRO A 1 92  ? -9.306  -2.087  3.005  1    37.927  ? 128  PRO A C   1 1 
ATOM   727  O  O   . PRO A 1 92  ? -8.923  -1.181  3.751  1    39.783  ? 128  PRO A O   1 1 
ATOM   728  C  CB  . PRO A 1 92  ? -11.298 -3.509  3.753  1    32.923  ? 128  PRO A CB  1 1 
ATOM   729  C  CG  . PRO A 1 92  ? -11.518 -3.916  5.205  1    32.029  ? 128  PRO A CG  1 1 
ATOM   730  C  CD  . PRO A 1 92  ? -10.177 -3.858  5.996  1    30.854  ? 128  PRO A CD  1 1 
ATOM   731  N  N   . ALA A 1 93  ? -9.317  -1.945  1.667  1    40.007  ? 129  ALA A N   1 1 
ATOM   732  C  CA  . ALA A 1 93  ? -8.83   -0.769  0.929  1    42.411  ? 129  ALA A CA  1 1 
ATOM   733  C  C   . ALA A 1 93  ? -9.127  0.551   1.668  1    43.294  ? 129  ALA A C   1 1 
ATOM   734  O  O   . ALA A 1 93  ? -8.215  1.36    1.944  1    42.025  ? 129  ALA A O   1 1 
ATOM   735  C  CB  . ALA A 1 93  ? -9.429  -0.747  -0.484 1    39.384  ? 129  ALA A CB  1 1 
ATOM   736  N  N   . GLN A 1 94  ? -10.417 0.749   1.98   1    43.5    ? 130  GLN A N   1 1 
ATOM   737  C  CA  . GLN A 1 94  ? -10.9   1.984   2.578  1    44.229  ? 130  GLN A CA  1 1 
ATOM   738  C  C   . GLN A 1 94  ? -10.289 2.265   3.961  1    42.41   ? 130  GLN A C   1 1 
ATOM   739  O  O   . GLN A 1 94  ? -9.704  3.344   4.157  1    39.515  ? 130  GLN A O   1 1 
ATOM   740  C  CB  . GLN A 1 94  ? -12.393 1.834   2.778  1    44.471  ? 130  GLN A CB  1 1 
ATOM   741  C  CG  . GLN A 1 94  ? -13.142 3.037   2.234  1    52.465  ? 130  GLN A CG  1 1 
ATOM   742  C  CD  . GLN A 1 94  ? -14.506 3.122   2.855  1    57.175  ? 130  GLN A CD  1 1 
ATOM   743  O  OE1 . GLN A 1 94  ? -14.597 3.188   4.083  1    61.501  ? 130  GLN A OE1 1 1 
ATOM   744  N  NE2 . GLN A 1 94  ? -15.554 3.07    2.039  1    60.53   ? 130  GLN A NE2 1 1 
ATOM   745  N  N   . GLU A 1 95  ? -10.44  1.297   4.903  1    37.576  ? 131  GLU A N   1 1 
ATOM   746  C  CA  . GLU A 1 95  ? -9.848  1.354   6.236  1    35.465  ? 131  GLU A CA  1 1 
ATOM   747  C  C   . GLU A 1 95  ? -8.341  1.58    6.142  1    34.047  ? 131  GLU A C   1 1 
ATOM   748  O  O   . GLU A 1 95  ? -7.756  2.22    7.008  1    33.864  ? 131  GLU A O   1 1 
ATOM   749  C  CB  . GLU A 1 95  ? -10.035 0.031   6.979  1    35.56   ? 131  GLU A CB  1 1 
ATOM   750  C  CG  . GLU A 1 95  ? -11.448 -0.094  7.548  1    37.492  ? 131  GLU A CG  1 1 
ATOM   751  C  CD  . GLU A 1 95  ? -12.514 -0.339  6.466  1    44.643  ? 131  GLU A CD  1 1 
ATOM   752  O  OE1 . GLU A 1 95  ? -12.275 -0.669  5.284  1    51.162  ? 131  GLU A OE1 1 1 
ATOM   753  O  OE2 . GLU A 1 95  ? -13.664 -0.135  6.817  1    46.247  ? 131  GLU A OE2 1 1 
ATOM   754  N  N   . LEU A 1 96  ? -7.689  1.042   5.099  1    34.286  ? 132  LEU A N   1 1 
ATOM   755  C  CA  . LEU A 1 96  ? -6.241  1.167   5.076  1    32.472  ? 132  LEU A CA  1 1 
ATOM   756  C  C   . LEU A 1 96  ? -5.858  2.61    4.754  1    35.885  ? 132  LEU A C   1 1 
ATOM   757  O  O   . LEU A 1 96  ? -4.989  3.191   5.437  1    32.526  ? 132  LEU A O   1 1 
ATOM   758  C  CB  . LEU A 1 96  ? -5.624  0.196   4.088  1    32.145  ? 132  LEU A CB  1 1 
ATOM   759  C  CG  . LEU A 1 96  ? -4.16   0.446   3.728  1    31.236  ? 132  LEU A CG  1 1 
ATOM   760  C  CD1 . LEU A 1 96  ? -3.271  0.46    4.94   1    29.109  ? 132  LEU A CD1 1 1 
ATOM   761  C  CD2 . LEU A 1 96  ? -3.742  -0.553  2.641  1    33.275  ? 132  LEU A CD2 1 1 
ATOM   762  N  N   . GLU A 1 97  ? -6.485  3.142   3.677  1    38.599  ? 133  GLU A N   1 1 
ATOM   763  C  CA  . GLU A 1 97  ? -6.295  4.533   3.298  1    42.517  ? 133  GLU A CA  1 1 
ATOM   764  C  C   . GLU A 1 97  ? -6.583  5.449   4.51   1    39.486  ? 133  GLU A C   1 1 
ATOM   765  O  O   . GLU A 1 97  ? -5.81   6.326   4.839  1    39.694  ? 133  GLU A O   1 1 
ATOM   766  C  CB  . GLU A 1 97  ? -7.155  4.852   2.076  1    42.518  ? 133  GLU A CB  1 1 
ATOM   767  C  CG  . GLU A 1 97  ? -7.527  6.324   2.046  1    49.217  ? 133  GLU A CG  1 1 
ATOM   768  C  CD  . GLU A 1 97  ? -9.01   6.435   1.712  1    60.972  ? 133  GLU A CD  1 1 
ATOM   769  O  OE1 . GLU A 1 97  ? -9.892  6.399   2.658  1    57.473  ? 133  GLU A OE1 1 1 
ATOM   770  O  OE2 . GLU A 1 97  ? -9.235  6.45    0.459  1    52.281  ? 133  GLU A OE2 1 1 
ATOM   771  N  N   . GLU A 1 98  ? -7.695  5.212   5.189  1    39.161  ? 134  GLU A N   1 1 
ATOM   772  C  CA  . GLU A 1 98  ? -8.114  5.974   6.345  1    41.483  ? 134  GLU A CA  1 1 
ATOM   773  C  C   . GLU A 1 98  ? -7.115  5.884   7.524  1    39.088  ? 134  GLU A C   1 1 
ATOM   774  O  O   . GLU A 1 98  ? -6.812  6.889   8.189  1    34.997  ? 134  GLU A O   1 1 
ATOM   775  C  CB  . GLU A 1 98  ? -9.556  5.561   6.624  1    39.818  ? 134  GLU A CB  1 1 
ATOM   776  C  CG  . GLU A 1 98  ? -9.957  6.195   7.945  1    45.099  ? 134  GLU A CG  1 1 
ATOM   777  C  CD  . GLU A 1 98  ? -11.371 5.872   8.314  1    52.793  ? 134  GLU A CD  1 1 
ATOM   778  O  OE1 . GLU A 1 98  ? -11.887 4.987   7.599  1    56.368  ? 134  GLU A OE1 1 1 
ATOM   779  O  OE2 . GLU A 1 98  ? -11.925 6.473   9.265  1    55.368  ? 134  GLU A OE2 1 1 
ATOM   780  N  N   . TYR A 1 99  ? -6.586  4.683   7.793  1    37.467  ? 135  TYR A N   1 1 
ATOM   781  C  CA  . TYR A 1 99  ? -5.655  4.567   8.898  1    34.755  ? 135  TYR A CA  1 1 
ATOM   782  C  C   . TYR A 1 99  ? -4.341  5.285   8.569  1    34.202  ? 135  TYR A C   1 1 
ATOM   783  O  O   . TYR A 1 99  ? -3.74   5.947   9.416  1    34.519  ? 135  TYR A O   1 1 
ATOM   784  C  CB  . TYR A 1 99  ? -5.467  3.069   9.096  1    33.157  ? 135  TYR A CB  1 1 
ATOM   785  C  CG  . TYR A 1 99  ? -4.401  2.71    10.118 1    34.913  ? 135  TYR A CG  1 1 
ATOM   786  C  CD1 . TYR A 1 99  ? -4.588  2.983   11.473 1    35.94   ? 135  TYR A CD1 1 1 
ATOM   787  C  CD2 . TYR A 1 99  ? -3.221  2.067   9.741  1    38.775  ? 135  TYR A CD2 1 1 
ATOM   788  C  CE1 . TYR A 1 99  ? -3.62   2.639   12.414 1    36.656  ? 135  TYR A CE1 1 1 
ATOM   789  C  CE2 . TYR A 1 99  ? -2.242  1.723   10.669 1    36.242  ? 135  TYR A CE2 1 1 
ATOM   790  C  CZ  . TYR A 1 99  ? -2.457  1.999   12.005 1    36.917  ? 135  TYR A CZ  1 1 
ATOM   791  O  OH  . TYR A 1 99  ? -1.536  1.652   12.926 1    37.805  ? 135  TYR A OH  1 1 
ATOM   792  N  N   . ASN A 1 100 ? -3.884  5.16    7.326  1    34.435  ? 136  ASN A N   1 1 
ATOM   793  C  CA  . ASN A 1 100 ? -2.66   5.814   6.878  1    36.136  ? 136  ASN A CA  1 1 
ATOM   794  C  C   . ASN A 1 100 ? -2.75   7.331   7.057  1    33.737  ? 136  ASN A C   1 1 
ATOM   795  O  O   . ASN A 1 100 ? -1.773  7.959   7.474  1    34.42   ? 136  ASN A O   1 1 
ATOM   796  C  CB  . ASN A 1 100 ? -2.339  5.533   5.412  1    34.952  ? 136  ASN A CB  1 1 
ATOM   797  C  CG  . ASN A 1 100 ? -1.715  4.173   5.194  1    39.06   ? 136  ASN A CG  1 1 
ATOM   798  O  OD1 . ASN A 1 100 ? -0.913  3.736   6.029  1    38.905  ? 136  ASN A OD1 1 1 
ATOM   799  N  ND2 . ASN A 1 100 ? -2.07   3.5     4.099  1    35.788  ? 136  ASN A ND2 1 1 
ATOM   800  N  N   . LYS A 1 101 ? -3.934  7.874   6.776  1    35.631  ? 137  LYS A N   1 1 
ATOM   801  C  CA  . LYS A 1 101 ? -4.24   9.299   6.825  1    37.478  ? 137  LYS A CA  1 1 
ATOM   802  C  C   . LYS A 1 101 ? -4.318  9.749   8.288  1    37.691  ? 137  LYS A C   1 1 
ATOM   803  O  O   . LYS A 1 101 ? -3.785  10.799  8.64   1    35.581  ? 137  LYS A O   1 1 
ATOM   804  C  CB  . LYS A 1 101 ? -5.526  9.564   6.045  1    38.888  ? 137  LYS A CB  1 1 
ATOM   805  C  CG  . LYS A 1 101 ? -6.124  10.939  6.2    1    42.291  ? 137  LYS A CG  1 1 
ATOM   806  C  CD  . LYS A 1 101 ? -5.208  12.129  5.907  1    48.686  ? 137  LYS A CD  1 1 
ATOM   807  C  CE  . LYS A 1 101 ? -5.907  13.326  5.253  1    53.159  ? 137  LYS A CE  1 1 
ATOM   808  N  NZ  . LYS A 1 101 ? -7.161  13.662  5.95   1    47.547  ? 137  LYS A NZ  1 1 
ATOM   809  N  N   . ILE A 1 102 ? -4.936  8.915   9.128  1    37.91   ? 138  ILE A N   1 1 
ATOM   810  C  CA  . ILE A 1 102 ? -5.015  9.148   10.562 1    37.773  ? 138  ILE A CA  1 1 
ATOM   811  C  C   . ILE A 1 102 ? -3.622  9.217   11.167 1    33.832  ? 138  ILE A C   1 1 
ATOM   812  O  O   . ILE A 1 102 ? -3.296  10.13   11.9   1    33.097  ? 138  ILE A O   1 1 
ATOM   813  C  CB  . ILE A 1 102 ? -5.935  8.093   11.195 1    42.576  ? 138  ILE A CB  1 1 
ATOM   814  C  CG1 . ILE A 1 102 ? -7.338  8.67    11.37  1    46.817  ? 138  ILE A CG1 1 1 
ATOM   815  C  CG2 . ILE A 1 102 ? -5.39   7.524   12.5   1    39.314  ? 138  ILE A CG2 1 1 
ATOM   816  C  CD1 . ILE A 1 102 ? -8.364  7.595   11.632 1    47.189  ? 138  ILE A CD1 1 1 
ATOM   817  N  N   . LEU A 1 103 ? -2.77   8.248   10.872 1    35.799  ? 139  LEU A N   1 1 
ATOM   818  C  CA  . LEU A 1 103 ? -1.452  8.305   11.479 1    32.319  ? 139  LEU A CA  1 1 
ATOM   819  C  C   . LEU A 1 103 ? -0.699  9.551   11.001 1    36.66   ? 139  LEU A C   1 1 
ATOM   820  O  O   . LEU A 1 103 ? 0.051   10.164  11.743 1    30.742  ? 139  LEU A O   1 1 
ATOM   821  C  CB  . LEU A 1 103 ? -0.729  7.054   11.005 1    32.093  ? 139  LEU A CB  1 1 
ATOM   822  C  CG  . LEU A 1 103 ? -1.127  5.75    11.692 1    35.628  ? 139  LEU A CG  1 1 
ATOM   823  C  CD1 . LEU A 1 103 ? -0.137  4.76    11.102 1    36.809  ? 139  LEU A CD1 1 1 
ATOM   824  C  CD2 . LEU A 1 103 ? -0.982  5.829   13.204 1    30.904  ? 139  LEU A CD2 1 1 
ATOM   825  N  N   . LEU A 1 104 ? -0.887  9.93    9.73   1    36.802  ? 140  LEU A N   1 1 
ATOM   826  C  CA  . LEU A 1 104 ? -0.141  11.064  9.215  1    36.455  ? 140  LEU A CA  1 1 
ATOM   827  C  C   . LEU A 1 104 ? -0.697  12.321  9.876  1    32.343  ? 140  LEU A C   1 1 
ATOM   828  O  O   . LEU A 1 104 ? 0.05    13.235  10.183 1    33.558  ? 140  LEU A O   1 1 
ATOM   829  C  CB  . LEU A 1 104 ? -0.327  11.106  7.692  1    41.17   ? 140  LEU A CB  1 1 
ATOM   830  C  CG  . LEU A 1 104 ? 0.392   12.238  6.949  1    45.743  ? 140  LEU A CG  1 1 
ATOM   831  C  CD1 . LEU A 1 104 ? 1.925   12.094  6.96   1    47.671  ? 140  LEU A CD1 1 1 
ATOM   832  C  CD2 . LEU A 1 104 ? -0.088  12.257  5.514  1    46.988  ? 140  LEU A CD2 1 1 
ATOM   833  N  N   . ASP A 1 105 ? -2.017  12.362  10.079 1    29.938  ? 141  ASP A N   1 1 
ATOM   834  C  CA  . ASP A 1 105 ? -2.587  13.564  10.635 1    31.215  ? 141  ASP A CA  1 1 
ATOM   835  C  C   . ASP A 1 105 ? -2.174  13.707  12.105 1    30.859  ? 141  ASP A C   1 1 
ATOM   836  O  O   . ASP A 1 105 ? -2.089  14.847  12.581 1    32.205  ? 141  ASP A O   1 1 
ATOM   837  C  CB  . ASP A 1 105 ? -4.082  13.684  10.422 1    33.812  ? 141  ASP A CB  1 1 
ATOM   838  C  CG  . ASP A 1 105 ? -4.53   13.908  8.969  1    40.328  ? 141  ASP A CG  1 1 
ATOM   839  O  OD1 . ASP A 1 105 ? -3.692  14.276  8.09   1    42.222  ? 141  ASP A OD1 1 1 
ATOM   840  O  OD2 . ASP A 1 105 ? -5.708  13.638  8.699  1    38.763  ? 141  ASP A OD2 1 1 
ATOM   841  N  N   . MET A 1 106 ? -1.966  12.587  12.815 1    26.501  ? 142  MET A N   1 1 
ATOM   842  C  CA  . MET A 1 106 ? -1.625  12.709  14.223 1    28.477  ? 142  MET A CA  1 1 
ATOM   843  C  C   . MET A 1 106 ? -0.204  13.243  14.334 1    28.826  ? 142  MET A C   1 1 
ATOM   844  O  O   . MET A 1 106 ? 0.089   14.094  15.166 1    30.235  ? 142  MET A O   1 1 
ATOM   845  C  CB  . MET A 1 106 ? -1.746  11.384  14.989 1    24.744  ? 142  MET A CB  1 1 
ATOM   846  C  CG  . MET A 1 106 ? -3.22   11.018  15.259 1    28.85   ? 142  MET A CG  1 1 
ATOM   847  S  SD  . MET A 1 106 ? -3.55   9.74    16.497 1    28.822  ? 142  MET A SD  1 1 
ATOM   848  C  CE  . MET A 1 106 ? -2.809  8.386   15.567 1    30.535  ? 142  MET A CE  1 1 
ATOM   849  N  N   . GLU A 1 107 ? 0.696   12.727  13.507 1    30.417  ? 143  GLU A N   1 1 
ATOM   850  C  CA  . GLU A 1 107 ? 2.103   13.108  13.617 1    33.773  ? 143  GLU A CA  1 1 
ATOM   851  C  C   . GLU A 1 107 ? 2.293   14.592  13.3   1    36.673  ? 143  GLU A C   1 1 
ATOM   852  O  O   . GLU A 1 107 ? 3.127   15.227  13.952 1    32.703  ? 143  GLU A O   1 1 
ATOM   853  C  CB  . GLU A 1 107 ? 2.951   12.435  12.544 1    37.736  ? 143  GLU A CB  1 1 
ATOM   854  C  CG  . GLU A 1 107 ? 3.074   10.971  12.902 1    52.776  ? 143  GLU A CG  1 1 
ATOM   855  C  CD  . GLU A 1 107 ? 3.772   10.073  11.912 1    61.676  ? 143  GLU A CD  1 1 
ATOM   856  O  OE1 . GLU A 1 107 ? 3.791   10.343  10.689 1    71.851  ? 143  GLU A OE1 1 1 
ATOM   857  O  OE2 . GLU A 1 107 ? 4.338   9.099   12.442 1    58.148  ? 143  GLU A OE2 1 1 
ATOM   858  N  N   . THR A 1 108 ? 1.589   15.058  12.246 1    32.289  ? 144  THR A N   1 1 
ATOM   859  C  CA  . THR A 1 108 ? 1.667   16.422  11.76  1    35.899  ? 144  THR A CA  1 1 
ATOM   860  C  C   . THR A 1 108 ? 1.114   17.367  12.829 1    39.281  ? 144  THR A C   1 1 
ATOM   861  O  O   . THR A 1 108 ? 1.76    18.349  13.182 1    39.582  ? 144  THR A O   1 1 
ATOM   862  C  CB  . THR A 1 108 ? 0.972   16.546  10.402 1    35.055  ? 144  THR A CB  1 1 
ATOM   863  O  OG1 . THR A 1 108 ? 1.628   15.574  9.587  1    34.496  ? 144  THR A OG1 1 1 
ATOM   864  C  CG2 . THR A 1 108 ? 1.035   17.944  9.827  1    36.715  ? 144  THR A CG2 1 1 
ATOM   865  N  N   . THR A 1 109 ? -0.065  17.05   13.378 1    36.785  ? 145  THR A N   1 1 
ATOM   866  C  CA  . THR A 1 109 ? -0.616  17.852  14.462 1    34.191  ? 145  THR A CA  1 1 
ATOM   867  C  C   . THR A 1 109 ? 0.425   18.027  15.573 1    30.845  ? 145  THR A C   1 1 
ATOM   868  O  O   . THR A 1 109 ? 0.647   19.147  16.063 1    28.595  ? 145  THR A O   1 1 
ATOM   869  C  CB  . THR A 1 109 ? -1.922  17.243  14.976 1    33.163  ? 145  THR A CB  1 1 
ATOM   870  O  OG1 . THR A 1 109 ? -2.727  17.235  13.797 1    32.558  ? 145  THR A OG1 1 1 
ATOM   871  C  CG2 . THR A 1 109 ? -2.62   18.14   15.979 1    29.431  ? 145  THR A CG2 1 1 
ATOM   872  N  N   . TYR A 1 110 ? 1.076   16.932  15.95  1    26.69   ? 146  TYR A N   1 1 
ATOM   873  C  CA  . TYR A 1 110 ? 1.985   16.984  17.072 1    31.037  ? 146  TYR A CA  1 1 
ATOM   874  C  C   . TYR A 1 110 ? 3.16    17.884  16.673 1    35.075  ? 146  TYR A C   1 1 
ATOM   875  O  O   . TYR A 1 110 ? 3.661   18.717  17.451 1    35.988  ? 146  TYR A O   1 1 
ATOM   876  C  CB  . TYR A 1 110 ? 2.369   15.541  17.443 1    24.416  ? 146  TYR A CB  1 1 
ATOM   877  C  CG  . TYR A 1 110 ? 3.33    15.47   18.622 1    25.829  ? 146  TYR A CG  1 1 
ATOM   878  C  CD1 . TYR A 1 110 ? 4.721   15.59   18.446 1    24.049  ? 146  TYR A CD1 1 1 
ATOM   879  C  CD2 . TYR A 1 110 ? 2.847   15.358  19.936 1    23.321  ? 146  TYR A CD2 1 1 
ATOM   880  C  CE1 . TYR A 1 110 ? 5.597   15.607  19.527 1    21.791  ? 146  TYR A CE1 1 1 
ATOM   881  C  CE2 . TYR A 1 110 ? 3.732   15.263  21.013 1    21.599  ? 146  TYR A CE2 1 1 
ATOM   882  C  CZ  . TYR A 1 110 ? 5.089   15.399  20.803 1    22.813  ? 146  TYR A CZ  1 1 
ATOM   883  O  OH  . TYR A 1 110 ? 5.889   15.341  21.894 1    21.312  ? 146  TYR A OH  1 1 
ATOM   884  N  N   A SER A 1 111 ? 3.62    17.726  15.441 0.71 36.501  ? 147  SER A N   1 1 
ATOM   885  N  N   B SER A 1 111 ? 3.576   17.718  15.414 0.29 35.077  ? 147  SER A N   1 1 
ATOM   886  C  CA  A SER A 1 111 ? 4.932   18.279  15.183 0.71 41.053  ? 147  SER A CA  1 1 
ATOM   887  C  CA  B SER A 1 111 ? 4.883   18.166  14.969 0.29 37.032  ? 147  SER A CA  1 1 
ATOM   888  C  C   A SER A 1 111 ? 4.818   19.773  14.892 0.71 37.74   ? 147  SER A C   1 1 
ATOM   889  C  C   B SER A 1 111 ? 4.853   19.661  14.645 0.29 37.134  ? 147  SER A C   1 1 
ATOM   890  O  O   A SER A 1 111 ? 5.76    20.519  15.125 0.71 42.033  ? 147  SER A O   1 1 
ATOM   891  O  O   B SER A 1 111 ? 5.907   20.286  14.609 0.29 40.676  ? 147  SER A O   1 1 
ATOM   892  C  CB  A SER A 1 111 ? 5.637   17.52   14.097 0.71 44.703  ? 147  SER A CB  1 1 
ATOM   893  C  CB  B SER A 1 111 ? 5.38    17.316  13.806 0.29 36.603  ? 147  SER A CB  1 1 
ATOM   894  O  OG  A SER A 1 111 ? 4.964   17.779  12.878 0.71 46.569  ? 147  SER A OG  1 1 
ATOM   895  O  OG  B SER A 1 111 ? 6.775   17.034  13.872 0.29 35.154  ? 147  SER A OG  1 1 
ATOM   896  N  N   . VAL A 1 112 ? 3.649   20.22   14.436 1    37.19   ? 148  VAL A N   1 1 
ATOM   897  C  CA  . VAL A 1 112 ? 3.433   21.639  14.172 1    37.084  ? 148  VAL A CA  1 1 
ATOM   898  C  C   . VAL A 1 112 ? 2.779   22.405  15.347 1    39.787  ? 148  VAL A C   1 1 
ATOM   899  O  O   . VAL A 1 112 ? 2.578   23.609  15.236 1    41.344  ? 148  VAL A O   1 1 
ATOM   900  C  CB  . VAL A 1 112 ? 2.713   21.946  12.838 1    38.616  ? 148  VAL A CB  1 1 
ATOM   901  C  CG1 . VAL A 1 112 ? 3.281   21.119  11.675 1    40.032  ? 148  VAL A CG1 1 1 
ATOM   902  C  CG2 . VAL A 1 112 ? 1.183   21.864  12.943 1    34      ? 148  VAL A CG2 1 1 
ATOM   903  N  N   . ALA A 1 113 ? 2.406   21.76   16.473 1    35.786  ? 149  ALA A N   1 1 
ATOM   904  C  CA  . ALA A 1 113 ? 1.729   22.422  17.583 1    33.936  ? 149  ALA A CA  1 1 
ATOM   905  C  C   . ALA A 1 113 ? 2.626   23.513  18.165 1    32.862  ? 149  ALA A C   1 1 
ATOM   906  O  O   . ALA A 1 113 ? 3.825   23.295  18.407 1    32.434  ? 149  ALA A O   1 1 
ATOM   907  C  CB  . ALA A 1 113 ? 1.386   21.402  18.659 1    29.434  ? 149  ALA A CB  1 1 
ATOM   908  N  N   . THR A 1 114 ? 2.032   24.682  18.425 1    38.95   ? 150  THR A N   1 1 
ATOM   909  C  CA  . THR A 1 114 ? 2.765   25.764  19.081 1    37.567  ? 150  THR A CA  1 1 
ATOM   910  C  C   . THR A 1 114 ? 1.912   26.322  20.224 1    39.258  ? 150  THR A C   1 1 
ATOM   911  O  O   . THR A 1 114 ? 0.679   26.193  20.175 1    32.365  ? 150  THR A O   1 1 
ATOM   912  C  CB  . THR A 1 114 ? 3.309   26.837  18.126 1    40.389  ? 150  THR A CB  1 1 
ATOM   913  O  OG1 . THR A 1 114 ? 2.282   27.741  17.767 1    41.558  ? 150  THR A OG1 1 1 
ATOM   914  C  CG2 . THR A 1 114 ? 3.993   26.294  16.887 1    41.872  ? 150  THR A CG2 1 1 
ATOM   915  N  N   . VAL A 1 115 ? 2.596   26.915  21.232 1    38.705  ? 151  VAL A N   1 1 
ATOM   916  C  CA  . VAL A 1 115 ? 1.994   27.658  22.342 1    40.369  ? 151  VAL A CA  1 1 
ATOM   917  C  C   . VAL A 1 115 ? 2.346   29.146  22.278 1    40.692  ? 151  VAL A C   1 1 
ATOM   918  O  O   . VAL A 1 115 ? 3.514   29.498  22.236 1    41.13   ? 151  VAL A O   1 1 
ATOM   919  C  CB  . VAL A 1 115 ? 2.401   27.071  23.717 1    39.577  ? 151  VAL A CB  1 1 
ATOM   920  C  CG1 . VAL A 1 115 ? 1.632   27.729  24.879 1    37.382  ? 151  VAL A CG1 1 1 
ATOM   921  C  CG2 . VAL A 1 115 ? 2.219   25.582  23.736 1    35.826  ? 151  VAL A CG2 1 1 
ATOM   922  N  N   . CYS A 1 116 ? 1.347   30.027  22.37  1    44.99   ? 152  CYS A N   1 1 
ATOM   923  C  CA  . CYS A 1 116 ? 1.548   31.447  22.087 1    52.092  ? 152  CYS A CA  1 1 
ATOM   924  C  C   . CYS A 1 116 ? 1.179   32.333  23.269 1    54.995  ? 152  CYS A C   1 1 
ATOM   925  O  O   . CYS A 1 116 ? 0.145   32.159  23.899 1    56.678  ? 152  CYS A O   1 1 
ATOM   926  C  CB  . CYS A 1 116 ? 0.722   31.899  20.889 1    50.83   ? 152  CYS A CB  1 1 
ATOM   927  S  SG  . CYS A 1 116 ? 1.05    30.882  19.417 1    70.923  ? 152  CYS A SG  1 1 
ATOM   928  N  N   . HIS A 1 117 ? 2.008   33.349  23.508 1    66.158  ? 153  HIS A N   1 1 
ATOM   929  C  CA  . HIS A 1 117 ? 1.58    34.518  24.267 1    63.795  ? 153  HIS A CA  1 1 
ATOM   930  C  C   . HIS A 1 117 ? 0.645   35.398  23.432 1    71.706  ? 153  HIS A C   1 1 
ATOM   931  O  O   . HIS A 1 117 ? 0.82    35.588  22.219 1    69.326  ? 153  HIS A O   1 1 
ATOM   932  C  CB  . HIS A 1 117 ? 2.79    35.323  24.733 1    63.614  ? 153  HIS A CB  1 1 
ATOM   933  C  CG  . HIS A 1 117 ? 3.8     34.514  25.467 1    62.97   ? 153  HIS A CG  1 1 
ATOM   934  N  ND1 . HIS A 1 117 ? 3.583   34.053  26.748 1    67.43   ? 153  HIS A ND1 1 1 
ATOM   935  C  CD2 . HIS A 1 117 ? 5.023   34.088  25.115 1    64.099  ? 153  HIS A CD2 1 1 
ATOM   936  C  CE1 . HIS A 1 117 ? 4.669   33.394  27.163 1    68.905  ? 153  HIS A CE1 1 1 
ATOM   937  N  NE2 . HIS A 1 117 ? 5.557   33.4    26.187 1    65.68   ? 153  HIS A NE2 1 1 
ATOM   938  N  N   . PRO A 1 118 ? -0.367  36.018  24.075 1    79.186  ? 154  PRO A N   1 1 
ATOM   939  C  CA  . PRO A 1 118 ? -1.335  36.842  23.35  1    76.977  ? 154  PRO A CA  1 1 
ATOM   940  C  C   . PRO A 1 118 ? -0.521  38.076  22.994 1    79.255  ? 154  PRO A C   1 1 
ATOM   941  O  O   . PRO A 1 118 ? 0.247   38.571  23.819 1    83.064  ? 154  PRO A O   1 1 
ATOM   942  C  CB  . PRO A 1 118 ? -2.404  37.106  24.4   1    79.148  ? 154  PRO A CB  1 1 
ATOM   943  C  CG  . PRO A 1 118 ? -1.616  37.096  25.697 1    82.568  ? 154  PRO A CG  1 1 
ATOM   944  C  CD  . PRO A 1 118 ? -0.571  36.009  25.533 1    81.324  ? 154  PRO A CD  1 1 
ATOM   945  N  N   . GLN A 1 119 ? -0.661  38.516  21.741 1    82.03   ? 155  GLN A N   1 1 
ATOM   946  C  CA  . GLN A 1 119 ? 0.252   39.481  21.143 1    90.119  ? 155  GLN A CA  1 1 
ATOM   947  C  C   . GLN A 1 119 ? 1.682   39.223  21.646 1    85.519  ? 155  GLN A C   1 1 
ATOM   948  O  O   . GLN A 1 119 ? 2.288   40.092  22.273 1    95.206  ? 155  GLN A O   1 1 
ATOM   949  C  CB  . GLN A 1 119 ? -0.36   40.892  21.192 1    87.168  ? 155  GLN A CB  1 1 
ATOM   950  C  CG  . GLN A 1 119 ? -1.12   41.281  19.92  1    93.157  ? 155  GLN A CG  1 1 
ATOM   951  C  CD  . GLN A 1 119 ? -0.308  42.073  18.899 1    101.038 ? 155  GLN A CD  1 1 
ATOM   952  O  OE1 . GLN A 1 119 ? -0.836  42.913  18.151 1    93.526  ? 155  GLN A OE1 1 1 
ATOM   953  N  NE2 . GLN A 1 119 ? 0.994   41.81   18.828 1    94.438  ? 155  GLN A NE2 1 1 
ATOM   954  N  N   . GLY A 1 120 ? 2.209   38.017  21.357 1    80.132  ? 156  GLY A N   1 1 
ATOM   955  C  CA  . GLY A 1 120 ? 3.552   37.584  21.726 1    69.484  ? 156  GLY A CA  1 1 
ATOM   956  C  C   . GLY A 1 120 ? 4.102   36.532  20.761 1    61.315  ? 156  GLY A C   1 1 
ATOM   957  O  O   . GLY A 1 120 ? 3.582   36.338  19.659 1    58.465  ? 156  GLY A O   1 1 
ATOM   958  N  N   . SER A 1 121 ? 5.188   35.88   21.185 1    55.235  ? 157  SER A N   1 1 
ATOM   959  C  CA  . SER A 1 121 ? 5.868   34.821  20.44  1    59.793  ? 157  SER A CA  1 1 
ATOM   960  C  C   . SER A 1 121 ? 5.046   33.545  20.451 1    55.113  ? 157  SER A C   1 1 
ATOM   961  O  O   . SER A 1 121 ? 4.291   33.304  21.396 1    60.906  ? 157  SER A O   1 1 
ATOM   962  C  CB  . SER A 1 121 ? 7.197   34.468  21.07  1    60.138  ? 157  SER A CB  1 1 
ATOM   963  O  OG  . SER A 1 121 ? 7.86    35.631  21.533 1    65.412  ? 157  SER A OG  1 1 
ATOM   964  N  N   . CYS A 1 122 ? 5.263   32.71   19.427 1    51.673  ? 158  CYS A N   1 1 
ATOM   965  C  CA  . CYS A 1 122 ? 4.767   31.348  19.441 1    48.95   ? 158  CYS A CA  1 1 
ATOM   966  C  C   . CYS A 1 122 ? 5.953   30.419  19.633 1    50.391  ? 158  CYS A C   1 1 
ATOM   967  O  O   . CYS A 1 122 ? 6.998   30.6    19.017 1    58.973  ? 158  CYS A O   1 1 
ATOM   968  C  CB  . CYS A 1 122 ? 3.932   31.007  18.22  1    53.602  ? 158  CYS A CB  1 1 
ATOM   969  S  SG  . CYS A 1 122 ? 2.391   31.959  18.237 1    68.79   ? 158  CYS A SG  1 1 
ATOM   970  N  N   . LEU A 1 123 ? 5.781   29.455  20.536 1    41.052  ? 159  LEU A N   1 1 
ATOM   971  C  CA  . LEU A 1 123 ? 6.881   28.632  20.949 1    38.674  ? 159  LEU A CA  1 1 
ATOM   972  C  C   . LEU A 1 123 ? 6.597   27.238  20.411 1    38.928  ? 159  LEU A C   1 1 
ATOM   973  O  O   . LEU A 1 123 ? 5.513   26.671  20.572 1    36.861  ? 159  LEU A O   1 1 
ATOM   974  C  CB  . LEU A 1 123 ? 6.916   28.668  22.485 1    37.026  ? 159  LEU A CB  1 1 
ATOM   975  C  CG  . LEU A 1 123 ? 7.776   29.74   23.163 1    36.116  ? 159  LEU A CG  1 1 
ATOM   976  C  CD1 . LEU A 1 123 ? 7.317   31.202  23.037 1    37.037  ? 159  LEU A CD1 1 1 
ATOM   977  C  CD2 . LEU A 1 123 ? 8.022   29.338  24.641 1    35.129  ? 159  LEU A CD2 1 1 
ATOM   978  N  N   . GLN A 1 124 ? 7.622   26.658  19.822 1    39.209  ? 160  GLN A N   1 1 
ATOM   979  C  CA  . GLN A 1 124 ? 7.523   25.266  19.466 1    37.646  ? 160  GLN A CA  1 1 
ATOM   980  C  C   . GLN A 1 124 ? 8.048   24.445  20.632 1    37.042  ? 160  GLN A C   1 1 
ATOM   981  O  O   . GLN A 1 124 ? 8.631   24.999  21.575 1    39.468  ? 160  GLN A O   1 1 
ATOM   982  C  CB  . GLN A 1 124 ? 8.496   25.048  18.324 1    41.639  ? 160  GLN A CB  1 1 
ATOM   983  C  CG  . GLN A 1 124 ? 8.01    25.654  17.017 1    51.536  ? 160  GLN A CG  1 1 
ATOM   984  C  CD  . GLN A 1 124 ? 8.703   24.978  15.867 1    55.213  ? 160  GLN A CD  1 1 
ATOM   985  O  OE1 . GLN A 1 124 ? 9.655   25.527  15.322 1    51.284  ? 160  GLN A OE1 1 1 
ATOM   986  N  NE2 . GLN A 1 124 ? 8.321   23.731  15.598 1    61.411  ? 160  GLN A NE2 1 1 
ATOM   987  N  N   . LEU A 1 125 ? 7.848   23.126  20.528 1    34.519  ? 161  LEU A N   1 1 
ATOM   988  C  CA  . LEU A 1 125 ? 8.253   22.175  21.55  1    32.134  ? 161  LEU A CA  1 1 
ATOM   989  C  C   . LEU A 1 125 ? 9.778   22.132  21.634 1    35.696  ? 161  LEU A C   1 1 
ATOM   990  O  O   . LEU A 1 125 ? 10.333  22.261  22.708 1    35.157  ? 161  LEU A O   1 1 
ATOM   991  C  CB  . LEU A 1 125 ? 7.595   20.802  21.418 1    27.256  ? 161  LEU A CB  1 1 
ATOM   992  C  CG  . LEU A 1 125 ? 8.123   19.764  22.418 1    27.68   ? 161  LEU A CG  1 1 
ATOM   993  C  CD1 . LEU A 1 125 ? 7.616   20.117  23.835 1    28.33   ? 161  LEU A CD1 1 1 
ATOM   994  C  CD2 . LEU A 1 125 ? 7.755   18.347  22.06  1    26.919  ? 161  LEU A CD2 1 1 
ATOM   995  N  N   . GLU A 1 126 ? 10.467  22.039  20.498 1    37.224  ? 162  GLU A N   1 1 
ATOM   996  C  CA  . GLU A 1 126 ? 11.926  21.987  20.487 1    41.484  ? 162  GLU A CA  1 1 
ATOM   997  C  C   . GLU A 1 126 ? 12.461  23.166  19.673 1    41.024  ? 162  GLU A C   1 1 
ATOM   998  O  O   . GLU A 1 126 ? 12.082  23.362  18.527 1    40.114  ? 162  GLU A O   1 1 
ATOM   999  C  CB  . GLU A 1 126 ? 12.369  20.644  19.909 1    49.055  ? 162  GLU A CB  1 1 
ATOM   1000 C  CG  . GLU A 1 126 ? 11.738  19.452  20.628 1    61.953  ? 162  GLU A CG  1 1 
ATOM   1001 C  CD  . GLU A 1 126 ? 11.635  18.163  19.81  1    81.591  ? 162  GLU A CD  1 1 
ATOM   1002 O  OE1 . GLU A 1 126 ? 12.387  17.225  20.157 1    81.702  ? 162  GLU A OE1 1 1 
ATOM   1003 O  OE2 . GLU A 1 126 ? 10.825  18.06   18.846 1    83.126  ? 162  GLU A OE2 1 1 
ATOM   1004 N  N   . PRO A 1 127 ? 13.335  24.035  20.226 1    40.816  ? 163  PRO A N   1 1 
ATOM   1005 C  CA  . PRO A 1 127 ? 13.854  23.857  21.576 1    37.01   ? 163  PRO A CA  1 1 
ATOM   1006 C  C   . PRO A 1 127 ? 13.048  24.662  22.605 1    36.476  ? 163  PRO A C   1 1 
ATOM   1007 O  O   . PRO A 1 127 ? 13.267  24.483  23.794 1    35.531  ? 163  PRO A O   1 1 
ATOM   1008 C  CB  . PRO A 1 127 ? 15.29   24.407  21.403 1    36.037  ? 163  PRO A CB  1 1 
ATOM   1009 C  CG  . PRO A 1 127 ? 15.154  25.51   20.336 1    38.166  ? 163  PRO A CG  1 1 
ATOM   1010 C  CD  . PRO A 1 127 ? 13.836  25.262  19.569 1    37.11   ? 163  PRO A CD  1 1 
ATOM   1011 N  N   . ASP A 1 128 ? 12.082  25.484  22.168 1    34.321  ? 164  ASP A N   1 1 
ATOM   1012 C  CA  . ASP A 1 128 ? 11.638  26.606  22.977 1    34.93   ? 164  ASP A CA  1 1 
ATOM   1013 C  C   . ASP A 1 128 ? 10.955  26.177  24.279 1    38.421  ? 164  ASP A C   1 1 
ATOM   1014 O  O   . ASP A 1 128 ? 11.398  26.617  25.34  1    35.637  ? 164  ASP A O   1 1 
ATOM   1015 C  CB  . ASP A 1 128 ? 10.826  27.592  22.181 1    38.384  ? 164  ASP A CB  1 1 
ATOM   1016 C  CG  . ASP A 1 128 ? 11.45   27.972  20.856 1    46.166  ? 164  ASP A CG  1 1 
ATOM   1017 O  OD1 . ASP A 1 128 ? 12.655  28.381  20.837 1    48.254  ? 164  ASP A OD1 1 1 
ATOM   1018 O  OD2 . ASP A 1 128 ? 10.701  27.864  19.875 1    47.805  ? 164  ASP A OD2 1 1 
ATOM   1019 N  N   . LEU A 1 129 ? 9.926   25.3    24.206 1    38.566  ? 165  LEU A N   1 1 
ATOM   1020 C  CA  . LEU A 1 129 ? 9.178   24.859  25.389 1    34.458  ? 165  LEU A CA  1 1 
ATOM   1021 C  C   . LEU A 1 129 ? 10.022  23.97   26.284 1    34.721  ? 165  LEU A C   1 1 
ATOM   1022 O  O   . LEU A 1 129 ? 9.899   24.104  27.495 1    30.071  ? 165  LEU A O   1 1 
ATOM   1023 C  CB  . LEU A 1 129 ? 7.781   24.251  25.179 1    31.921  ? 165  LEU A CB  1 1 
ATOM   1024 C  CG  . LEU A 1 129 ? 6.762   25.17   24.502 1    33.14   ? 165  LEU A CG  1 1 
ATOM   1025 C  CD1 . LEU A 1 129 ? 5.637   24.423  23.849 1    38.405  ? 165  LEU A CD1 1 1 
ATOM   1026 C  CD2 . LEU A 1 129 ? 6.171   26.131  25.523 1    35.885  ? 165  LEU A CD2 1 1 
ATOM   1027 N  N   . THR A 1 130 ? 10.809  23.046  25.693 1    32.951  ? 166  THR A N   1 1 
ATOM   1028 C  CA  . THR A 1 130 ? 11.686  22.166  26.458 1    32.844  ? 166  THR A CA  1 1 
ATOM   1029 C  C   . THR A 1 130 ? 12.738  22.982  27.218 1    32.284  ? 166  THR A C   1 1 
ATOM   1030 O  O   . THR A 1 130 ? 13.082  22.619  28.347 1    33.142  ? 166  THR A O   1 1 
ATOM   1031 C  CB  . THR A 1 130 ? 12.312  20.989  25.682 1    35.664  ? 166  THR A CB  1 1 
ATOM   1032 O  OG1 . THR A 1 130 ? 12.775  21.796  24.635 1    46.394  ? 166  THR A OG1 1 1 
ATOM   1033 C  CG2 . THR A 1 130 ? 11.412  20.21   24.733 1    35.495  ? 166  THR A CG2 1 1 
ATOM   1034 N  N   . ASN A 1 131 ? 13.31   24.012  26.585 1    32.185  ? 167  ASN A N   1 1 
ATOM   1035 C  CA  . ASN A 1 131 ? 14.141  24.966  27.316 1    35.776  ? 167  ASN A CA  1 1 
ATOM   1036 C  C   . ASN A 1 131 ? 13.377  25.653  28.452 1    32.376  ? 167  ASN A C   1 1 
ATOM   1037 O  O   . ASN A 1 131 ? 13.965  25.899  29.5   1    30.202  ? 167  ASN A O   1 1 
ATOM   1038 C  CB  . ASN A 1 131 ? 14.699  26.099  26.454 1    38.446  ? 167  ASN A CB  1 1 
ATOM   1039 C  CG  . ASN A 1 131 ? 15.737  25.633  25.45  1    43.916  ? 167  ASN A CG  1 1 
ATOM   1040 O  OD1 . ASN A 1 131 ? 16.156  24.464  25.464 1    48.305  ? 167  ASN A OD1 1 1 
ATOM   1041 N  ND2 . ASN A 1 131 ? 16.108  26.488  24.507 1    44.053  ? 167  ASN A ND2 1 1 
ATOM   1042 N  N   . VAL A 1 132 ? 12.118  26.048  28.248 1    26.397  ? 168  VAL A N   1 1 
ATOM   1043 C  CA  . VAL A 1 132 ? 11.394  26.611  29.382 1    28.044  ? 168  VAL A CA  1 1 
ATOM   1044 C  C   . VAL A 1 132 ? 11.351  25.623  30.563 1    26.974  ? 168  VAL A C   1 1 
ATOM   1045 O  O   . VAL A 1 132 ? 11.752  25.926  31.69  1    27.361  ? 168  VAL A O   1 1 
ATOM   1046 C  CB  . VAL A 1 132 ? 10.023  27.284  29.09  1    31.278  ? 168  VAL A CB  1 1 
ATOM   1047 C  CG1 . VAL A 1 132 ? 9.344   27.816  30.354 1    30.291  ? 168  VAL A CG1 1 1 
ATOM   1048 C  CG2 . VAL A 1 132 ? 10.157  28.486  28.134 1    30.161  ? 168  VAL A CG2 1 1 
ATOM   1049 N  N   . MET A 1 133 ? 10.902  24.416  30.292 1    25.609  ? 169  MET A N   1 1 
ATOM   1050 C  CA  . MET A 1 133 ? 10.711  23.338  31.254 1    26.912  ? 169  MET A CA  1 1 
ATOM   1051 C  C   . MET A 1 133 ? 12.024  22.975  31.96  1    28.812  ? 169  MET A C   1 1 
ATOM   1052 O  O   . MET A 1 133 ? 12      22.715  33.16  1    26.192  ? 169  MET A O   1 1 
ATOM   1053 C  CB  . MET A 1 133 ? 10.177  22.077  30.571 1    24.83   ? 169  MET A CB  1 1 
ATOM   1054 C  CG  . MET A 1 133 ? 8.702   22.103  30.134 1    22.821  ? 169  MET A CG  1 1 
ATOM   1055 S  SD  . MET A 1 133 ? 7.575   22.944  31.273 1    25.921  ? 169  MET A SD  1 1 
ATOM   1056 C  CE  . MET A 1 133 ? 7.618   21.67   32.546 1    23.034  ? 169  MET A CE  1 1 
ATOM   1057 N  N   . ALA A 1 134 ? 13.156  23.035  31.223 1    26.827  ? 170  ALA A N   1 1 
ATOM   1058 C  CA  . ALA A 1 134 ? 14.506  22.778  31.74  1    27.038  ? 170  ALA A CA  1 1 
ATOM   1059 C  C   . ALA A 1 134 ? 15.066  23.882  32.652 1    28.441  ? 170  ALA A C   1 1 
ATOM   1060 O  O   . ALA A 1 134 ? 15.845  23.59   33.568 1    27.405  ? 170  ALA A O   1 1 
ATOM   1061 C  CB  . ALA A 1 134 ? 15.471  22.449  30.623 1    23.512  ? 170  ALA A CB  1 1 
ATOM   1062 N  N   . THR A 1 135 ? 14.751  25.154  32.364 1    26.466  ? 171  THR A N   1 1 
ATOM   1063 C  CA  . THR A 1 135 ? 15.567  26.153  33.007 1    30.289  ? 171  THR A CA  1 1 
ATOM   1064 C  C   . THR A 1 135 ? 14.691  27.082  33.867 1    30.409  ? 171  THR A C   1 1 
ATOM   1065 O  O   . THR A 1 135 ? 15.186  27.668  34.812 1    27.531  ? 171  THR A O   1 1 
ATOM   1066 C  CB  . THR A 1 135 ? 16.433  26.911  31.991 1    34.744  ? 171  THR A CB  1 1 
ATOM   1067 O  OG1 . THR A 1 135 ? 15.48   27.85   31.522 1    42.268  ? 171  THR A OG1 1 1 
ATOM   1068 C  CG2 . THR A 1 135 ? 16.96   26.135  30.787 1    30.734  ? 171  THR A CG2 1 1 
ATOM   1069 N  N   . SER A 1 136 ? 13.375  27.209  33.613 1    29.135  ? 172  SER A N   1 1 
ATOM   1070 C  CA  . SER A 1 136 ? 12.568  28.069  34.48  1    28.743  ? 172  SER A CA  1 1 
ATOM   1071 C  C   . SER A 1 136 ? 12.497  27.452  35.89  1    30.226  ? 172  SER A C   1 1 
ATOM   1072 O  O   . SER A 1 136 ? 12.379  26.209  36.042 1    30.24   ? 172  SER A O   1 1 
ATOM   1073 C  CB  . SER A 1 136 ? 11.169  28.257  33.933 1    28.795  ? 172  SER A CB  1 1 
ATOM   1074 O  OG  . SER A 1 136 ? 10.428  29.145  34.758 1    29.17   ? 172  SER A OG  1 1 
ATOM   1075 N  N   . ARG A 1 137 ? 12.571  28.341  36.911 1    34.182  ? 173  ARG A N   1 1 
ATOM   1076 C  CA  . ARG A 1 137 ? 12.302  28.04   38.322 1    31.493  ? 173  ARG A CA  1 1 
ATOM   1077 C  C   . ARG A 1 137 ? 11.117  28.895  38.802 1    31.001  ? 173  ARG A C   1 1 
ATOM   1078 O  O   . ARG A 1 137 ? 10.97   29.146  39.992 1    28.368  ? 173  ARG A O   1 1 
ATOM   1079 C  CB  . ARG A 1 137 ? 13.606  28.192  39.128 1    31.941  ? 173  ARG A CB  1 1 
ATOM   1080 C  CG  . ARG A 1 137 ? 14.747  27.268  38.706 1    28.317  ? 173  ARG A CG  1 1 
ATOM   1081 C  CD  . ARG A 1 137 ? 14.373  25.77   38.697 1    31.05   ? 173  ARG A CD  1 1 
ATOM   1082 N  NE  . ARG A 1 137 ? 15.64   25.088  38.424 1    32.928  ? 173  ARG A NE  1 1 
ATOM   1083 C  CZ  . ARG A 1 137 ? 15.927  24.351  37.36  1    40.255  ? 173  ARG A CZ  1 1 
ATOM   1084 N  NH1 . ARG A 1 137 ? 17.109  23.783  37.324 1    42.741  ? 173  ARG A NH1 1 1 
ATOM   1085 N  NH2 . ARG A 1 137 ? 15.058  24.106  36.375 1    41.216  ? 173  ARG A NH2 1 1 
ATOM   1086 N  N   . LYS A 1 138 ? 10.281  29.383  37.876 1    32.008  ? 174  LYS A N   1 1 
ATOM   1087 C  CA  . LYS A 1 138 ? 9.038   30.08   38.243 1    31.314  ? 174  LYS A CA  1 1 
ATOM   1088 C  C   . LYS A 1 138 ? 7.829   29.165  38.024 1    32.453  ? 174  LYS A C   1 1 
ATOM   1089 O  O   . LYS A 1 138 ? 7.597   28.679  36.911 1    33.827  ? 174  LYS A O   1 1 
ATOM   1090 C  CB  . LYS A 1 138 ? 8.89    31.42   37.551 1    32.632  ? 174  LYS A CB  1 1 
ATOM   1091 C  CG  . LYS A 1 138 ? 10.095  32.312  37.928 1    35.356  ? 174  LYS A CG  1 1 
ATOM   1092 C  CD  . LYS A 1 138 ? 10.038  33.668  37.268 1    38.253  ? 174  LYS A CD  1 1 
ATOM   1093 C  CE  . LYS A 1 138 ? 8.847   34.334  37.867 1    40.506  ? 174  LYS A CE  1 1 
ATOM   1094 N  NZ  . LYS A 1 138 ? 9.153   35.741  38.114 1    48.377  ? 174  LYS A NZ  1 1 
ATOM   1095 N  N   . TYR A 1 139 ? 7.101   28.89   39.122 1    29.216  ? 175  TYR A N   1 1 
ATOM   1096 C  CA  . TYR A 1 139 ? 5.929   28.014  39.164 1    26.724  ? 175  TYR A CA  1 1 
ATOM   1097 C  C   . TYR A 1 139 ? 4.957   28.365  38.036 1    23.761  ? 175  TYR A C   1 1 
ATOM   1098 O  O   . TYR A 1 139 ? 4.426   27.498  37.332 1    24.155  ? 175  TYR A O   1 1 
ATOM   1099 C  CB  . TYR A 1 139 ? 5.242   28.214  40.526 1    26.801  ? 175  TYR A CB  1 1 
ATOM   1100 C  CG  . TYR A 1 139 ? 4.318   27.037  40.819 1    27.67   ? 175  TYR A CG  1 1 
ATOM   1101 C  CD1 . TYR A 1 139 ? 2.978   27.049  40.404 1    26.896  ? 175  TYR A CD1 1 1 
ATOM   1102 C  CD2 . TYR A 1 139 ? 4.772   25.922  41.522 1    25.076  ? 175  TYR A CD2 1 1 
ATOM   1103 C  CE1 . TYR A 1 139 ? 2.147   25.969  40.67  1    25.306  ? 175  TYR A CE1 1 1 
ATOM   1104 C  CE2 . TYR A 1 139 ? 3.935   24.844  41.764 1    25.301  ? 175  TYR A CE2 1 1 
ATOM   1105 C  CZ  . TYR A 1 139 ? 2.612   24.864  41.359 1    26.303  ? 175  TYR A CZ  1 1 
ATOM   1106 O  OH  . TYR A 1 139 ? 1.794   23.75   41.531 1    26.803  ? 175  TYR A OH  1 1 
ATOM   1107 N  N   . GLU A 1 140 ? 4.648   29.663  37.921 1    25.123  ? 176  GLU A N   1 1 
ATOM   1108 C  CA  . GLU A 1 140 ? 3.643   30.1    36.968 1    26.041  ? 176  GLU A CA  1 1 
ATOM   1109 C  C   . GLU A 1 140 ? 4.171   29.961  35.545 1    24.24   ? 176  GLU A C   1 1 
ATOM   1110 O  O   . GLU A 1 140 ? 3.365   29.692  34.681 1    25.173  ? 176  GLU A O   1 1 
ATOM   1111 C  CB  . GLU A 1 140 ? 3.227   31.559  37.236 1    30.818  ? 176  GLU A CB  1 1 
ATOM   1112 C  CG  . GLU A 1 140 ? 2.479   31.739  38.556 1    36.031  ? 176  GLU A CG  1 1 
ATOM   1113 C  CD  . GLU A 1 140 ? 1.15    30.943  38.59  1    47.238  ? 176  GLU A CD  1 1 
ATOM   1114 O  OE1 . GLU A 1 140 ? 0.464   30.754  37.518 1    45.701  ? 176  GLU A OE1 1 1 
ATOM   1115 O  OE2 . GLU A 1 140 ? 0.795   30.477  39.707 1    45.469  ? 176  GLU A OE2 1 1 
ATOM   1116 N  N   . ASP A 1 141 ? 5.487   30.146  35.297 1    24.817  ? 177  ASP A N   1 1 
ATOM   1117 C  CA  . ASP A 1 141 ? 6.051   30.089  33.934 1    26.766  ? 177  ASP A CA  1 1 
ATOM   1118 C  C   . ASP A 1 141 ? 6.133   28.633  33.461 1    25.965  ? 177  ASP A C   1 1 
ATOM   1119 O  O   . ASP A 1 141 ? 5.817   28.295  32.303 1    25.307  ? 177  ASP A O   1 1 
ATOM   1120 C  CB  . ASP A 1 141 ? 7.399   30.795  33.801 1    27.22   ? 177  ASP A CB  1 1 
ATOM   1121 C  CG  . ASP A 1 141 ? 7.369   32.309  34.012 1    32.412  ? 177  ASP A CG  1 1 
ATOM   1122 O  OD1 . ASP A 1 141 ? 6.231   32.891  33.971 1    37.783  ? 177  ASP A OD1 1 1 
ATOM   1123 O  OD2 . ASP A 1 141 ? 8.488   32.898  34.289 1    32.468  ? 177  ASP A OD2 1 1 
ATOM   1124 N  N   . LEU A 1 142 ? 6.456   27.733  34.403 1    23.24   ? 178  LEU A N   1 1 
ATOM   1125 C  CA  . LEU A 1 142 ? 6.439   26.32   34.116 1    22.352  ? 178  LEU A CA  1 1 
ATOM   1126 C  C   . LEU A 1 142 ? 4.999   25.857  33.859 1    22.569  ? 178  LEU A C   1 1 
ATOM   1127 O  O   . LEU A 1 142 ? 4.72    25.02   32.997 1    21.756  ? 178  LEU A O   1 1 
ATOM   1128 C  CB  . LEU A 1 142 ? 7.06    25.66   35.335 1    20.73   ? 178  LEU A CB  1 1 
ATOM   1129 C  CG  . LEU A 1 142 ? 8.594   25.777  35.449 1    22.536  ? 178  LEU A CG  1 1 
ATOM   1130 C  CD1 . LEU A 1 142 ? 9.098   25.213  36.802 1    21.931  ? 178  LEU A CD1 1 1 
ATOM   1131 C  CD2 . LEU A 1 142 ? 9.204   24.963  34.325 1    20.446  ? 178  LEU A CD2 1 1 
ATOM   1132 N  N   . LEU A 1 143 ? 4.068   26.411  34.614 1    22.978  ? 179  LEU A N   1 1 
ATOM   1133 C  CA  . LEU A 1 143 ? 2.708   25.944  34.394 1    22.309  ? 179  LEU A CA  1 1 
ATOM   1134 C  C   . LEU A 1 143 ? 2.163   26.388  33.028 1    22.595  ? 179  LEU A C   1 1 
ATOM   1135 O  O   . LEU A 1 143 ? 1.434   25.667  32.366 1    23.174  ? 179  LEU A O   1 1 
ATOM   1136 C  CB  . LEU A 1 143 ? 1.857   26.417  35.571 1    24.205  ? 179  LEU A CB  1 1 
ATOM   1137 C  CG  . LEU A 1 143 ? 0.349   26.19   35.456 1    27.815  ? 179  LEU A CG  1 1 
ATOM   1138 C  CD1 . LEU A 1 143 ? 0.119   24.658  35.375 1    27.602  ? 179  LEU A CD1 1 1 
ATOM   1139 C  CD2 . LEU A 1 143 ? -0.403  26.854  36.59  1    31.197  ? 179  LEU A CD2 1 1 
ATOM   1140 N  N   . TRP A 1 144 ? 2.445   27.627  32.636 1    25.483  ? 180  TRP A N   1 1 
ATOM   1141 C  CA  . TRP A 1 144 ? 2.014   28.143  31.351 1    27.299  ? 180  TRP A CA  1 1 
ATOM   1142 C  C   . TRP A 1 144 ? 2.485   27.171  30.242 1    26.53   ? 180  TRP A C   1 1 
ATOM   1143 O  O   . TRP A 1 144 ? 1.744   26.807  29.336 1    24.484  ? 180  TRP A O   1 1 
ATOM   1144 C  CB  . TRP A 1 144 ? 2.55    29.592  31.229 1    29.877  ? 180  TRP A CB  1 1 
ATOM   1145 C  CG  . TRP A 1 144 ? 2.297   30.186  29.879 1    36.572  ? 180  TRP A CG  1 1 
ATOM   1146 C  CD1 . TRP A 1 144 ? 1.226   30.939  29.503 1    45.853  ? 180  TRP A CD1 1 1 
ATOM   1147 C  CD2 . TRP A 1 144 ? 3.097   29.992  28.695 1    37.429  ? 180  TRP A CD2 1 1 
ATOM   1148 N  NE1 . TRP A 1 144 ? 1.309   31.247  28.168 1    51.436  ? 180  TRP A NE1 1 1 
ATOM   1149 C  CE2 . TRP A 1 144 ? 2.444   30.669  27.641 1    45.821  ? 180  TRP A CE2 1 1 
ATOM   1150 C  CE3 . TRP A 1 144 ? 4.308   29.346  28.432 1    38.635  ? 180  TRP A CE3 1 1 
ATOM   1151 C  CZ2 . TRP A 1 144 ? 2.951   30.692  26.333 1    47.134  ? 180  TRP A CZ2 1 1 
ATOM   1152 C  CZ3 . TRP A 1 144 ? 4.822   29.376  27.146 1    43.834  ? 180  TRP A CZ3 1 1 
ATOM   1153 C  CH2 . TRP A 1 144 ? 4.143   30.028  26.105 1    46.047  ? 180  TRP A CH2 1 1 
ATOM   1154 N  N   . ALA A 1 145 ? 3.71    26.667  30.359 1    25.869  ? 181  ALA A N   1 1 
ATOM   1155 C  CA  . ALA A 1 145 ? 4.313   25.867  29.304 1    26.278  ? 181  ALA A CA  1 1 
ATOM   1156 C  C   . ALA A 1 145 ? 3.719   24.467  29.332 1    25.968  ? 181  ALA A C   1 1 
ATOM   1157 O  O   . ALA A 1 145 ? 3.42    23.864  28.283 1    22.726  ? 181  ALA A O   1 1 
ATOM   1158 C  CB  . ALA A 1 145 ? 5.828   25.765  29.502 1    25.045  ? 181  ALA A CB  1 1 
ATOM   1159 N  N   . TRP A 1 146 ? 3.604   23.952  30.569 1    24.729  ? 182  TRP A N   1 1 
ATOM   1160 C  CA  . TRP A 1 146 ? 3.071   22.609  30.81  1    25.164  ? 182  TRP A CA  1 1 
ATOM   1161 C  C   . TRP A 1 146 ? 1.609   22.517  30.327 1    23.74   ? 182  TRP A C   1 1 
ATOM   1162 O  O   . TRP A 1 146 ? 1.297   21.571  29.611 1    21.616  ? 182  TRP A O   1 1 
ATOM   1163 C  CB  . TRP A 1 146 ? 3.18    22.232  32.309 1    21.81   ? 182  TRP A CB  1 1 
ATOM   1164 C  CG  . TRP A 1 146 ? 2.775   20.827  32.629 1    22.615  ? 182  TRP A CG  1 1 
ATOM   1165 C  CD1 . TRP A 1 146 ? 3.642   19.763  32.735 1    23.417  ? 182  TRP A CD1 1 1 
ATOM   1166 C  CD2 . TRP A 1 146 ? 1.451   20.309  32.872 1    21.473  ? 182  TRP A CD2 1 1 
ATOM   1167 N  NE1 . TRP A 1 146 ? 2.955   18.624  32.999 1    21.397  ? 182  TRP A NE1 1 1 
ATOM   1168 C  CE2 . TRP A 1 146 ? 1.61    18.927  33.101 1    21.874  ? 182  TRP A CE2 1 1 
ATOM   1169 C  CE3 . TRP A 1 146 ? 0.175   20.882  32.971 1    22.329  ? 182  TRP A CE3 1 1 
ATOM   1170 C  CZ2 . TRP A 1 146 ? 0.524   18.083  33.382 1    20.479  ? 182  TRP A CZ2 1 1 
ATOM   1171 C  CZ3 . TRP A 1 146 ? -0.889  20.053  33.267 1    21.021  ? 182  TRP A CZ3 1 1 
ATOM   1172 C  CH2 . TRP A 1 146 ? -0.716  18.683  33.429 1    21.477  ? 182  TRP A CH2 1 1 
ATOM   1173 N  N   . GLU A 1 147 ? 0.769   23.489  30.758 1    23.569  ? 183  GLU A N   1 1 
ATOM   1174 C  CA  . GLU A 1 147 ? -0.651  23.598  30.467 1    25.571  ? 183  GLU A CA  1 1 
ATOM   1175 C  C   . GLU A 1 147 ? -0.856  23.886  28.969 1    30.459  ? 183  GLU A C   1 1 
ATOM   1176 O  O   . GLU A 1 147 ? -1.663  23.229  28.263 1    27.646  ? 183  GLU A O   1 1 
ATOM   1177 C  CB  . GLU A 1 147 ? -1.415  24.554  31.398 1    27.114  ? 183  GLU A CB  1 1 
ATOM   1178 C  CG  . GLU A 1 147 ? -2.942  24.566  31.204 1    35.057  ? 183  GLU A CG  1 1 
ATOM   1179 C  CD  . GLU A 1 147 ? -3.722  23.235  31.321 1    47.495  ? 183  GLU A CD  1 1 
ATOM   1180 O  OE1 . GLU A 1 147 ? -3.263  22.419  32.173 1    45.038  ? 183  GLU A OE1 1 1 
ATOM   1181 O  OE2 . GLU A 1 147 ? -4.781  22.958  30.661 1    44.856  ? 183  GLU A OE2 1 1 
ATOM   1182 N  N   . GLY A 1 148 ? -0.074  24.84   28.468 1    31.557  ? 184  GLY A N   1 1 
ATOM   1183 C  CA  . GLY A 1 148 ? -0.207  25.274  27.078 1    29.9    ? 184  GLY A CA  1 1 
ATOM   1184 C  C   . GLY A 1 148 ? 0.081   24.127  26.111 1    26.723  ? 184  GLY A C   1 1 
ATOM   1185 O  O   . GLY A 1 148 ? -0.64   23.959  25.13  1    30.615  ? 184  GLY A O   1 1 
ATOM   1186 N  N   . TRP A 1 149 ? 1.107   23.331  26.397 1    25.441  ? 185  TRP A N   1 1 
ATOM   1187 C  CA  . TRP A 1 149 ? 1.463   22.219  25.519 1    27.737  ? 185  TRP A CA  1 1 
ATOM   1188 C  C   . TRP A 1 149 ? 0.35    21.154  25.426 1    27.103  ? 185  TRP A C   1 1 
ATOM   1189 O  O   . TRP A 1 149 ? 0.022   20.63   24.35  1    26.871  ? 185  TRP A O   1 1 
ATOM   1190 C  CB  . TRP A 1 149 ? 2.798   21.597  25.95  1    24.679  ? 185  TRP A CB  1 1 
ATOM   1191 C  CG  . TRP A 1 149 ? 3.214   20.467  25.054 1    25.356  ? 185  TRP A CG  1 1 
ATOM   1192 C  CD1 . TRP A 1 149 ? 3.28    19.137  25.367 1    25.986  ? 185  TRP A CD1 1 1 
ATOM   1193 C  CD2 . TRP A 1 149 ? 3.502   20.538  23.65  1    23.753  ? 185  TRP A CD2 1 1 
ATOM   1194 N  NE1 . TRP A 1 149 ? 3.657   18.388  24.287 1    22.764  ? 185  TRP A NE1 1 1 
ATOM   1195 C  CE2 . TRP A 1 149 ? 3.763   19.22   23.216 1    25.1    ? 185  TRP A CE2 1 1 
ATOM   1196 C  CE3 . TRP A 1 149 ? 3.526   21.558  22.712 1    25.334  ? 185  TRP A CE3 1 1 
ATOM   1197 C  CZ2 . TRP A 1 149 ? 4.095   18.917  21.895 1    26.141  ? 185  TRP A CZ2 1 1 
ATOM   1198 C  CZ3 . TRP A 1 149 ? 3.821   21.255  21.391 1    28.24   ? 185  TRP A CZ3 1 1 
ATOM   1199 C  CH2 . TRP A 1 149 ? 4.051   19.935  20.985 1    26.255  ? 185  TRP A CH2 1 1 
ATOM   1200 N  N   . ARG A 1 150 ? -0.214  20.844  26.586 1    26.106  ? 186  ARG A N   1 1 
ATOM   1201 C  CA  . ARG A 1 150 ? -1.4    20.013  26.696 1    25.696  ? 186  ARG A CA  1 1 
ATOM   1202 C  C   . ARG A 1 150 ? -2.585  20.634  25.965 1    27.403  ? 186  ARG A C   1 1 
ATOM   1203 O  O   . ARG A 1 150 ? -3.232  19.904  25.247 1    27.277  ? 186  ARG A O   1 1 
ATOM   1204 C  CB  . ARG A 1 150 ? -1.669  19.492  28.112 1    24.682  ? 186  ARG A CB  1 1 
ATOM   1205 C  CG  . ARG A 1 150 ? -0.611  18.439  28.403 1    25.001  ? 186  ARG A CG  1 1 
ATOM   1206 C  CD  . ARG A 1 150 ? -0.34   18.309  29.868 1    24.232  ? 186  ARG A CD  1 1 
ATOM   1207 N  NE  . ARG A 1 150 ? 0.778   17.402  30.106 1    24.066  ? 186  ARG A NE  1 1 
ATOM   1208 C  CZ  . ARG A 1 150 ? 2.109   17.685  30.006 1    26.048  ? 186  ARG A CZ  1 1 
ATOM   1209 N  NH1 . ARG A 1 150 ? 2.994   16.766  30.268 1    23.423  ? 186  ARG A NH1 1 1 
ATOM   1210 N  NH2 . ARG A 1 150 ? 2.578   18.853  29.646 1    24.227  ? 186  ARG A NH2 1 1 
ATOM   1211 N  N   . ASP A 1 151 ? -2.843  21.952  26.105 1    28.57   ? 187  ASP A N   1 1 
ATOM   1212 C  CA  . ASP A 1 151 ? -4.006  22.566  25.49  1    28.926  ? 187  ASP A CA  1 1 
ATOM   1213 C  C   . ASP A 1 151 ? -3.885  22.448  23.96  1    28.545  ? 187  ASP A C   1 1 
ATOM   1214 O  O   . ASP A 1 151 ? -4.871  22.265  23.26  1    25.954  ? 187  ASP A O   1 1 
ATOM   1215 C  CB  . ASP A 1 151 ? -4.165  24.019  25.946 1    34.393  ? 187  ASP A CB  1 1 
ATOM   1216 C  CG  . ASP A 1 151 ? -4.569  24.205  27.408 1    38.441  ? 187  ASP A CG  1 1 
ATOM   1217 O  OD1 . ASP A 1 151 ? -4.739  23.175  28.063 1    35.166  ? 187  ASP A OD1 1 1 
ATOM   1218 O  OD2 . ASP A 1 151 ? -4.71   25.369  27.905 1    41.604  ? 187  ASP A OD2 1 1 
ATOM   1219 N  N   . LYS A 1 152 ? -2.664  22.529  23.433 1    27.546  ? 188  LYS A N   1 1 
ATOM   1220 C  CA  . LYS A 1 152 ? -2.526  22.721  22.008 1    31.271  ? 188  LYS A CA  1 1 
ATOM   1221 C  C   . LYS A 1 152 ? -2.259  21.377  21.345 1    36.631  ? 188  LYS A C   1 1 
ATOM   1222 O  O   . LYS A 1 152 ? -2.8    21.125  20.264 1    40.583  ? 188  LYS A O   1 1 
ATOM   1223 C  CB  . LYS A 1 152 ? -1.452  23.756  21.623 1    32.826  ? 188  LYS A CB  1 1 
ATOM   1224 C  CG  . LYS A 1 152 ? -1.743  25.23   21.992 1    36.646  ? 188  LYS A CG  1 1 
ATOM   1225 C  CD  . LYS A 1 152 ? -3.102  25.906  21.712 1    40.787  ? 188  LYS A CD  1 1 
ATOM   1226 C  CE  . LYS A 1 152 ? -3.559  26.338  20.324 1    44.064  ? 188  LYS A CE  1 1 
ATOM   1227 N  NZ  . LYS A 1 152 ? -2.338  26.45   19.527 1    46.565  ? 188  LYS A NZ  1 1 
ATOM   1228 N  N   . ALA A 1 153 ? -1.321  20.594  21.912 1    29.245  ? 189  ALA A N   1 1 
ATOM   1229 C  CA  . ALA A 1 153 ? -0.998  19.335  21.273 1    29.741  ? 189  ALA A CA  1 1 
ATOM   1230 C  C   . ALA A 1 153 ? -1.959  18.241  21.732 1    29.074  ? 189  ALA A C   1 1 
ATOM   1231 O  O   . ALA A 1 153 ? -2.55   17.536  20.901 1    28.829  ? 189  ALA A O   1 1 
ATOM   1232 C  CB  . ALA A 1 153 ? 0.431   18.928  21.542 1    30.312  ? 189  ALA A CB  1 1 
ATOM   1233 N  N   . GLY A 1 154 ? -2.056  18.054  23.049 1    22.589  ? 190  GLY A N   1 1 
ATOM   1234 C  CA  . GLY A 1 154 ? -2.839  16.924  23.526 1    23.01   ? 190  GLY A CA  1 1 
ATOM   1235 C  C   . GLY A 1 154 ? -4.295  17.056  23.086 1    26.993  ? 190  GLY A C   1 1 
ATOM   1236 O  O   . GLY A 1 154 ? -4.845  16.155  22.476 1    27.464  ? 190  GLY A O   1 1 
ATOM   1237 N  N   . ARG A 1 155 ? -4.95   18.199  23.279 1    25.275  ? 191  ARG A N   1 1 
ATOM   1238 C  CA  . ARG A 1 155 ? -6.363  18.175  22.894 1    26.77   ? 191  ARG A CA  1 1 
ATOM   1239 C  C   . ARG A 1 155 ? -6.561  17.94   21.391 1    29.156  ? 191  ARG A C   1 1 
ATOM   1240 O  O   . ARG A 1 155 ? -7.621  17.504  20.906 1    28.698  ? 191  ARG A O   1 1 
ATOM   1241 C  CB  . ARG A 1 155 ? -7.025  19.513  23.214 1    26.767  ? 191  ARG A CB  1 1 
ATOM   1242 C  CG  . ARG A 1 155 ? -7.002  19.565  24.733 1    26.683  ? 191  ARG A CG  1 1 
ATOM   1243 C  CD  . ARG A 1 155 ? -7.021  21.047  24.985 1    31.947  ? 191  ARG A CD  1 1 
ATOM   1244 N  NE  . ARG A 1 155 ? -8.37   21.404  25.371 1    41.477  ? 191  ARG A NE  1 1 
ATOM   1245 C  CZ  . ARG A 1 155 ? -8.764  21.899  26.54  1    57.92   ? 191  ARG A CZ  1 1 
ATOM   1246 N  NH1 . ARG A 1 155 ? -10.06  21.757  26.803 1    71.389  ? 191  ARG A NH1 1 1 
ATOM   1247 N  NH2 . ARG A 1 155 ? -7.938  22.459  27.433 1    47.574  ? 191  ARG A NH2 1 1 
ATOM   1248 N  N   . ALA A 1 156 ? -5.606  18.411  20.608 1    29.325  ? 192  ALA A N   1 1 
ATOM   1249 C  CA  . ALA A 1 156 ? -5.857  18.382  19.163 1    31.324  ? 192  ALA A CA  1 1 
ATOM   1250 C  C   . ALA A 1 156 ? -5.659  16.961  18.593 1    29.574  ? 192  ALA A C   1 1 
ATOM   1251 O  O   . ALA A 1 156 ? -6.107  16.691  17.481 1    29.548  ? 192  ALA A O   1 1 
ATOM   1252 C  CB  . ALA A 1 156 ? -5.053  19.489  18.454 1    29.643  ? 192  ALA A CB  1 1 
ATOM   1253 N  N   . ILE A 1 157 ? -5.058  16.036  19.382 1    25.12   ? 193  ILE A N   1 1 
ATOM   1254 C  CA  . ILE A 1 157 ? -4.947  14.629  19.046 1    24.355  ? 193  ILE A CA  1 1 
ATOM   1255 C  C   . ILE A 1 157 ? -6.276  13.892  19.282 1    25.888  ? 193  ILE A C   1 1 
ATOM   1256 O  O   . ILE A 1 157 ? -6.577  12.917  18.559 1    25.74   ? 193  ILE A O   1 1 
ATOM   1257 C  CB  . ILE A 1 157 ? -3.757  13.989  19.808 1    24.989  ? 193  ILE A CB  1 1 
ATOM   1258 C  CG1 . ILE A 1 157 ? -2.454  14.681  19.478 1    25.825  ? 193  ILE A CG1 1 1 
ATOM   1259 C  CG2 . ILE A 1 157 ? -3.62   12.489  19.516 1    24.879  ? 193  ILE A CG2 1 1 
ATOM   1260 C  CD1 . ILE A 1 157 ? -2.226  14.759  17.962 1    27.329  ? 193  ILE A CD1 1 1 
ATOM   1261 N  N   . LEU A 1 158 ? -7.017  14.287  20.344 1    25.351  ? 194  LEU A N   1 1 
ATOM   1262 C  CA  . LEU A 1 158 ? -8.263  13.643  20.763 1    25.552  ? 194  LEU A CA  1 1 
ATOM   1263 C  C   . LEU A 1 158 ? -9.192  13.301  19.591 1    28.637  ? 194  LEU A C   1 1 
ATOM   1264 O  O   . LEU A 1 158 ? -9.806  12.221  19.613 1    29.472  ? 194  LEU A O   1 1 
ATOM   1265 C  CB  . LEU A 1 158 ? -9.045  14.457  21.795 1    25.01   ? 194  LEU A CB  1 1 
ATOM   1266 C  CG  . LEU A 1 158 ? -10.256 13.718  22.395 1    26.882  ? 194  LEU A CG  1 1 
ATOM   1267 C  CD1 . LEU A 1 158 ? -9.887  12.348  23.071 1    21.872  ? 194  LEU A CD1 1 1 
ATOM   1268 C  CD2 . LEU A 1 158 ? -10.919 14.614  23.44  1    26.462  ? 194  LEU A CD2 1 1 
ATOM   1269 N  N   . GLN A 1 159 ? -9.392  14.235  18.623 1    26.991  ? 195  GLN A N   1 1 
ATOM   1270 C  CA  . GLN A 1 159 ? -10.326 13.991  17.521 1    29.68   ? 195  GLN A CA  1 1 
ATOM   1271 C  C   . GLN A 1 159 ? -10     12.672  16.783 1    29.744  ? 195  GLN A C   1 1 
ATOM   1272 O  O   . GLN A 1 159 ? -10.907 12.033  16.285 1    29.641  ? 195  GLN A O   1 1 
ATOM   1273 C  CB  . GLN A 1 159 ? -10.374 15.127  16.494 1    31.036  ? 195  GLN A CB  1 1 
ATOM   1274 C  CG  . GLN A 1 159 ? -9.039  15.415  15.825 1    33.37   ? 195  GLN A CG  1 1 
ATOM   1275 C  CD  . GLN A 1 159 ? -8.966  16.795  15.205 1    42.742  ? 195  GLN A CD  1 1 
ATOM   1276 O  OE1 . GLN A 1 159 ? -8.075  17.626  15.498 1    50.599  ? 195  GLN A OE1 1 1 
ATOM   1277 N  NE2 . GLN A 1 159 ? -9.877  17.017  14.28  1    34.311  ? 195  GLN A NE2 1 1 
ATOM   1278 N  N   . PHE A 1 160 ? -8.707  12.288  16.692 1    27.351  ? 196  PHE A N   1 1 
ATOM   1279 C  CA  . PHE A 1 160 ? -8.213  11.153  15.919 1    27.613  ? 196  PHE A CA  1 1 
ATOM   1280 C  C   . PHE A 1 160 ? -8.178  9.846   16.725 1    25.637  ? 196  PHE A C   1 1 
ATOM   1281 O  O   . PHE A 1 160 ? -8.212  8.776   16.139 1    22.759  ? 196  PHE A O   1 1 
ATOM   1282 C  CB  . PHE A 1 160 ? -6.789  11.471  15.421 1    28.013  ? 196  PHE A CB  1 1 
ATOM   1283 C  CG  . PHE A 1 160 ? -6.686  12.708  14.526 1    30.294  ? 196  PHE A CG  1 1 
ATOM   1284 C  CD1 . PHE A 1 160 ? -7.412  12.779  13.325 1    34.471  ? 196  PHE A CD1 1 1 
ATOM   1285 C  CD2 . PHE A 1 160 ? -5.915  13.815  14.937 1    29.111  ? 196  PHE A CD2 1 1 
ATOM   1286 C  CE1 . PHE A 1 160 ? -7.353  13.928  12.51  1    35.164  ? 196  PHE A CE1 1 1 
ATOM   1287 C  CE2 . PHE A 1 160 ? -5.856  14.964  14.146 1    32.996  ? 196  PHE A CE2 1 1 
ATOM   1288 C  CZ  . PHE A 1 160 ? -6.559  15.002  12.918 1    37.127  ? 196  PHE A CZ  1 1 
ATOM   1289 N  N   . TYR A 1 161 ? -7.965  9.904   18.066 1    25.384  ? 197  TYR A N   1 1 
ATOM   1290 C  CA  . TYR A 1 161 ? -7.5    8.739   18.786 1    23.561  ? 197  TYR A CA  1 1 
ATOM   1291 C  C   . TYR A 1 161 ? -8.537  7.618   18.694 1    23.725  ? 197  TYR A C   1 1 
ATOM   1292 O  O   . TYR A 1 161 ? -8.203  6.489   18.422 1    24.223  ? 197  TYR A O   1 1 
ATOM   1293 C  CB  . TYR A 1 161 ? -7.101  9.064   20.229 1    23.841  ? 197  TYR A CB  1 1 
ATOM   1294 C  CG  . TYR A 1 161 ? -5.94   8.154   20.636 1    24.012  ? 197  TYR A CG  1 1 
ATOM   1295 C  CD1 . TYR A 1 161 ? -4.661  8.267   20.051 1    22.735  ? 197  TYR A CD1 1 1 
ATOM   1296 C  CD2 . TYR A 1 161 ? -6.1    7.175   21.617 1    22.612  ? 197  TYR A CD2 1 1 
ATOM   1297 C  CE1 . TYR A 1 161 ? -3.592  7.464   20.444 1    18.748  ? 197  TYR A CE1 1 1 
ATOM   1298 C  CE2 . TYR A 1 161 ? -5.065  6.31    21.94  1    19.343  ? 197  TYR A CE2 1 1 
ATOM   1299 C  CZ  . TYR A 1 161 ? -3.802  6.468   21.381 1    20.312  ? 197  TYR A CZ  1 1 
ATOM   1300 O  OH  . TYR A 1 161 ? -2.794  5.599   21.734 1    17.077  ? 197  TYR A OH  1 1 
ATOM   1301 N  N   . PRO A 1 162 ? -9.827  7.833   19.002 1    26.58   ? 198  PRO A N   1 1 
ATOM   1302 C  CA  . PRO A 1 162 ? -10.773 6.719   18.995 1    26.665  ? 198  PRO A CA  1 1 
ATOM   1303 C  C   . PRO A 1 162 ? -10.744 5.963   17.66  1    26.697  ? 198  PRO A C   1 1 
ATOM   1304 O  O   . PRO A 1 162 ? -10.721 4.738   17.624 1    25.273  ? 198  PRO A O   1 1 
ATOM   1305 C  CB  . PRO A 1 162 ? -12.136 7.466   19.264 1    27.188  ? 198  PRO A CB  1 1 
ATOM   1306 C  CG  . PRO A 1 162 ? -11.715 8.627   20.153 1    27.31   ? 198  PRO A CG  1 1 
ATOM   1307 C  CD  . PRO A 1 162 ? -10.437 9.104   19.458 1    26.036  ? 198  PRO A CD  1 1 
ATOM   1308 N  N   . LYS A 1 163 ? -10.69  6.687   16.541 1    26.228  ? 199  LYS A N   1 1 
ATOM   1309 C  CA  . LYS A 1 163 ? -10.688 6.016   15.244 1    27.788  ? 199  LYS A CA  1 1 
ATOM   1310 C  C   . LYS A 1 163 ? -9.374  5.276   14.984 1    25.568  ? 199  LYS A C   1 1 
ATOM   1311 O  O   . LYS A 1 163 ? -9.416  4.215   14.401 1    25.054  ? 199  LYS A O   1 1 
ATOM   1312 C  CB  . LYS A 1 163 ? -11.146 6.924   14.095 1    31.991  ? 199  LYS A CB  1 1 
ATOM   1313 C  CG  . LYS A 1 163 ? -11.309 6.233   12.727 1    37.725  ? 199  LYS A CG  1 1 
ATOM   1314 C  CD  . LYS A 1 163 ? -12.215 5.025   12.401 1    39.573  ? 199  LYS A CD  1 1 
ATOM   1315 C  CE  . LYS A 1 163 ? -13.658 5.224   12.803 1    44.302  ? 199  LYS A CE  1 1 
ATOM   1316 N  NZ  . LYS A 1 163 ? -14.564 4.538   11.866 1    42.409  ? 199  LYS A NZ  1 1 
ATOM   1317 N  N   . TYR A 1 164 ? -8.23   5.812   15.429 1    23.959  ? 200  TYR A N   1 1 
ATOM   1318 C  CA  . TYR A 1 164 ? -6.973  5.09    15.346 1    23.797  ? 200  TYR A CA  1 1 
ATOM   1319 C  C   . TYR A 1 164 ? -7.059  3.798   16.148 1    23.104  ? 200  TYR A C   1 1 
ATOM   1320 O  O   . TYR A 1 164 ? -6.746  2.761   15.604 1    22.535  ? 200  TYR A O   1 1 
ATOM   1321 C  CB  . TYR A 1 164 ? -5.945  5.973   16.035 1    22.464  ? 200  TYR A CB  1 1 
ATOM   1322 C  CG  . TYR A 1 164 ? -4.704  5.249   16.57  1    22.553  ? 200  TYR A CG  1 1 
ATOM   1323 C  CD1 . TYR A 1 164 ? -3.735  4.74    15.71  1    23.181  ? 200  TYR A CD1 1 1 
ATOM   1324 C  CD2 . TYR A 1 164 ? -4.518  5.106   17.95  1    22.21   ? 200  TYR A CD2 1 1 
ATOM   1325 C  CE1 . TYR A 1 164 ? -2.586  4.144   16.203 1    25.246  ? 200  TYR A CE1 1 1 
ATOM   1326 C  CE2 . TYR A 1 164 ? -3.39   4.499   18.456 1    22.202  ? 200  TYR A CE2 1 1 
ATOM   1327 C  CZ  . TYR A 1 164 ? -2.42   4.067   17.582 1    23.737  ? 200  TYR A CZ  1 1 
ATOM   1328 O  OH  . TYR A 1 164 ? -1.356  3.515   18.14  1    24.243  ? 200  TYR A OH  1 1 
ATOM   1329 N  N   . VAL A 1 165 ? -7.496  3.854   17.424 1    23.234  ? 201  VAL A N   1 1 
ATOM   1330 C  CA  . VAL A 1 165 ? -7.665  2.619   18.188 1    22.537  ? 201  VAL A CA  1 1 
ATOM   1331 C  C   . VAL A 1 165 ? -8.472  1.591   17.406 1    25.328  ? 201  VAL A C   1 1 
ATOM   1332 O  O   . VAL A 1 165 ? -8.089  0.418   17.308 1    24.304  ? 201  VAL A O   1 1 
ATOM   1333 C  CB  . VAL A 1 165 ? -8.324  2.978   19.536 1    25.836  ? 201  VAL A CB  1 1 
ATOM   1334 C  CG1 . VAL A 1 165 ? -8.796  1.767   20.34  1    20.888  ? 201  VAL A CG1 1 1 
ATOM   1335 C  CG2 . VAL A 1 165 ? -7.352  3.871   20.338 1    19.73   ? 201  VAL A CG2 1 1 
ATOM   1336 N  N   . GLU A 1 166 ? -9.584  2.037   16.807 1    24.308  ? 202  GLU A N   1 1 
ATOM   1337 C  CA  . GLU A 1 166 ? -10.447 1.116   16.151 1    26.224  ? 202  GLU A CA  1 1 
ATOM   1338 C  C   . GLU A 1 166 ? -9.737  0.43    14.964 1    27.854  ? 202  GLU A C   1 1 
ATOM   1339 O  O   . GLU A 1 166 ? -9.833  -0.809  14.797 1    25.029  ? 202  GLU A O   1 1 
ATOM   1340 C  CB  . GLU A 1 166 ? -11.719 1.899   15.872 1    33.1    ? 202  GLU A CB  1 1 
ATOM   1341 C  CG  . GLU A 1 166 ? -12.53  1.212   14.796 1    40.515  ? 202  GLU A CG  1 1 
ATOM   1342 C  CD  . GLU A 1 166 ? -13.915 1.757   14.58  1    50.83   ? 202  GLU A CD  1 1 
ATOM   1343 O  OE1 . GLU A 1 166 ? -14.617 2.163   15.55  1    55.01   ? 202  GLU A OE1 1 1 
ATOM   1344 O  OE2 . GLU A 1 166 ? -14.26  1.684   13.387 1    52.81   ? 202  GLU A OE2 1 1 
ATOM   1345 N  N   . LEU A 1 167 ? -9.024  1.215   14.141 1    25.202  ? 203  LEU A N   1 1 
ATOM   1346 C  CA  . LEU A 1 167 ? -8.353  0.694   12.96  1    27.345  ? 203  LEU A CA  1 1 
ATOM   1347 C  C   . LEU A 1 167 ? -7.149  -0.194  13.329 1    24.29   ? 203  LEU A C   1 1 
ATOM   1348 O  O   . LEU A 1 167 ? -6.917  -1.219  12.674 1    22.088  ? 203  LEU A O   1 1 
ATOM   1349 C  CB  . LEU A 1 167 ? -7.958  1.878   12.081 1    27.285  ? 203  LEU A CB  1 1 
ATOM   1350 C  CG  . LEU A 1 167 ? -9.154  2.565   11.399 1    30.147  ? 203  LEU A CG  1 1 
ATOM   1351 C  CD1 . LEU A 1 167 ? -8.786  3.951   10.835 1    31.054  ? 203  LEU A CD1 1 1 
ATOM   1352 C  CD2 . LEU A 1 167 ? -9.885  1.729   10.338 1    31.37   ? 203  LEU A CD2 1 1 
ATOM   1353 N  N   . ILE A 1 168 ? -6.382  0.197   14.352 1    22.348  ? 204  ILE A N   1 1 
ATOM   1354 C  CA  . ILE A 1 168 ? -5.201  -0.59   14.681 1    22.242  ? 204  ILE A CA  1 1 
ATOM   1355 C  C   . ILE A 1 168 ? -5.577  -1.934  15.327 1    24.465  ? 204  ILE A C   1 1 
ATOM   1356 O  O   . ILE A 1 168 ? -4.93   -2.976  15.054 1    23.018  ? 204  ILE A O   1 1 
ATOM   1357 C  CB  . ILE A 1 168 ? -4.188  0.178   15.554 1    22.586  ? 204  ILE A CB  1 1 
ATOM   1358 C  CG1 . ILE A 1 168 ? -2.855  -0.499  15.615 1    19.841  ? 204  ILE A CG1 1 1 
ATOM   1359 C  CG2 . ILE A 1 168 ? -4.718  0.476   16.961 1    22.789  ? 204  ILE A CG2 1 1 
ATOM   1360 C  CD1 . ILE A 1 168 ? -1.784  0.433   16.154 1    19.451  ? 204  ILE A CD1 1 1 
ATOM   1361 N  N   . ASN A 1 169 ? -6.584  -1.913  16.222 1    22.391  ? 205  ASN A N   1 1 
ATOM   1362 C  CA  . ASN A 1 169 ? -7.198  -3.149  16.74  1    21.145  ? 205  ASN A CA  1 1 
ATOM   1363 C  C   . ASN A 1 169 ? -7.748  -4.003  15.602 1    22.279  ? 205  ASN A C   1 1 
ATOM   1364 O  O   . ASN A 1 169 ? -7.609  -5.25   15.606 1    20.885  ? 205  ASN A O   1 1 
ATOM   1365 C  CB  . ASN A 1 169 ? -8.307  -2.892  17.773 1    19.967  ? 205  ASN A CB  1 1 
ATOM   1366 C  CG  . ASN A 1 169 ? -7.762  -2.59   19.147 1    21.139  ? 205  ASN A CG  1 1 
ATOM   1367 O  OD1 . ASN A 1 169 ? -6.592  -2.849  19.437 1    18.19   ? 205  ASN A OD1 1 1 
ATOM   1368 N  ND2 . ASN A 1 169 ? -8.561  -1.96   19.988 1    22.261  ? 205  ASN A ND2 1 1 
ATOM   1369 N  N   . GLN A 1 170 ? -8.406  -3.346  14.626 1    23.367  ? 206  GLN A N   1 1 
ATOM   1370 C  CA  . GLN A 1 170 ? -8.969  -4.103  13.517 1    25.179  ? 206  GLN A CA  1 1 
ATOM   1371 C  C   . GLN A 1 170 ? -7.86   -4.809  12.74  1    26.351  ? 206  GLN A C   1 1 
ATOM   1372 O  O   . GLN A 1 170 ? -7.98   -5.997  12.489 1    24.9    ? 206  GLN A O   1 1 
ATOM   1373 C  CB  . GLN A 1 170 ? -9.973  -3.356  12.649 1    29.399  ? 206  GLN A CB  1 1 
ATOM   1374 C  CG  . GLN A 1 170 ? -10.563 -4.146  11.473 1    34.39   ? 206  GLN A CG  1 1 
ATOM   1375 C  CD  . GLN A 1 170 ? -11.274 -3.212  10.495 1    39.409  ? 206  GLN A CD  1 1 
ATOM   1376 O  OE1 . GLN A 1 170 ? -11.427 -2.021  10.771 1    44.635  ? 206  GLN A OE1 1 1 
ATOM   1377 N  NE2 . GLN A 1 170 ? -11.691 -3.669  9.326  1    36.525  ? 206  GLN A NE2 1 1 
ATOM   1378 N  N   . ALA A 1 171 ? -6.737  -4.124  12.456 1    27.305  ? 207  ALA A N   1 1 
ATOM   1379 C  CA  . ALA A 1 171 ? -5.654  -4.809  11.741 1    27.878  ? 207  ALA A CA  1 1 
ATOM   1380 C  C   . ALA A 1 171 ? -5.096  -5.956  12.595 1    26.029  ? 207  ALA A C   1 1 
ATOM   1381 O  O   . ALA A 1 171 ? -4.783  -7.029  12.054 1    24.425  ? 207  ALA A O   1 1 
ATOM   1382 C  CB  . ALA A 1 171 ? -4.543  -3.876  11.296 1    25.77   ? 207  ALA A CB  1 1 
ATOM   1383 N  N   . ALA A 1 172 ? -4.987  -5.716  13.925 1    24.233  ? 208  ALA A N   1 1 
ATOM   1384 C  CA  . ALA A 1 172 ? -4.454  -6.76   14.776 1    22.92   ? 208  ALA A CA  1 1 
ATOM   1385 C  C   . ALA A 1 172 ? -5.353  -8.008  14.8   1    23.856  ? 208  ALA A C   1 1 
ATOM   1386 O  O   . ALA A 1 172 ? -4.85   -9.129  14.677 1    23.485  ? 208  ALA A O   1 1 
ATOM   1387 C  CB  . ALA A 1 172 ? -4.126  -6.184  16.131 1    20.866  ? 208  ALA A CB  1 1 
ATOM   1388 N  N   . ARG A 1 173 ? -6.688  -7.853  14.914 1    22.672  ? 209  ARG A N   1 1 
ATOM   1389 C  CA  . ARG A 1 173 ? -7.569  -9.022  14.893 1    24.598  ? 209  ARG A CA  1 1 
ATOM   1390 C  C   . ARG A 1 173 ? -7.493  -9.741  13.534 1    28.299  ? 209  ARG A C   1 1 
ATOM   1391 O  O   . ARG A 1 173 ? -7.474  -10.967 13.45  1    27.265  ? 209  ARG A O   1 1 
ATOM   1392 C  CB  . ARG A 1 173 ? -9.061  -8.687  15.106 1    24.598  ? 209  ARG A CB  1 1 
ATOM   1393 C  CG  . ARG A 1 173 ? -9.298  -8.123  16.503 1    24.844  ? 209  ARG A CG  1 1 
ATOM   1394 C  CD  . ARG A 1 173 ? -10.814 -8.053  16.776 1    24.044  ? 209  ARG A CD  1 1 
ATOM   1395 N  NE  . ARG A 1 173 ? -11.563 -7.301  15.764 1    27      ? 209  ARG A NE  1 1 
ATOM   1396 C  CZ  . ARG A 1 173 ? -11.642 -5.907  15.732 1    28.166  ? 209  ARG A CZ  1 1 
ATOM   1397 N  NH1 . ARG A 1 173 ? -11.057 -5.171  16.693 1    24.678  ? 209  ARG A NH1 1 1 
ATOM   1398 N  NH2 . ARG A 1 173 ? -12.297 -5.283  14.762 1    25.936  ? 209  ARG A NH2 1 1 
ATOM   1399 N  N   . LEU A 1 174 ? -7.463  -8.967  12.437 1    29.485  ? 210  LEU A N   1 1 
ATOM   1400 C  CA  . LEU A 1 174 ? -7.226  -9.561  11.131 1    28.471  ? 210  LEU A CA  1 1 
ATOM   1401 C  C   . LEU A 1 174 ? -5.905  -10.313 11.063 1    25.997  ? 210  LEU A C   1 1 
ATOM   1402 O  O   . LEU A 1 174 ? -5.794  -11.146 10.218 1    28.222  ? 210  LEU A O   1 1 
ATOM   1403 C  CB  . LEU A 1 174 ? -7.387  -8.618  9.944  1    29.239  ? 210  LEU A CB  1 1 
ATOM   1404 C  CG  . LEU A 1 174 ? -8.822  -8.104  9.798  1    31.499  ? 210  LEU A CG  1 1 
ATOM   1405 C  CD1 . LEU A 1 174 ? -8.778  -6.774  9.062  1    34.018  ? 210  LEU A CD1 1 1 
ATOM   1406 C  CD2 . LEU A 1 174 ? -9.644  -9.167  9.027  1    31.096  ? 210  LEU A CD2 1 1 
ATOM   1407 N  N   . ASN A 1 175 ? -4.914  -10.052 11.909 1    24.858  ? 211  ASN A N   1 1 
ATOM   1408 C  CA  . ASN A 1 175 ? -3.693  -10.846 11.831 1    25.929  ? 211  ASN A CA  1 1 
ATOM   1409 C  C   . ASN A 1 175 ? -3.656  -11.951 12.922 1    27.907  ? 211  ASN A C   1 1 
ATOM   1410 O  O   . ASN A 1 175 ? -2.563  -12.482 13.209 1    24.416  ? 211  ASN A O   1 1 
ATOM   1411 C  CB  . ASN A 1 175 ? -2.459  -9.931  11.933 1    25.866  ? 211  ASN A CB  1 1 
ATOM   1412 C  CG  . ASN A 1 175 ? -2.201  -9.207  10.615 1    27.796  ? 211  ASN A CG  1 1 
ATOM   1413 O  OD1 . ASN A 1 175 ? -1.917  -9.841  9.601  1    30.215  ? 211  ASN A OD1 1 1 
ATOM   1414 N  ND2 . ASN A 1 175 ? -2.35   -7.894  10.568 1    25.888  ? 211  ASN A ND2 1 1 
ATOM   1415 N  N   . GLY A 1 176 ? -4.815  -12.222 13.58  1    25.054  ? 212  GLY A N   1 1 
ATOM   1416 C  CA  . GLY A 1 176 ? -4.974  -13.341 14.497 1    25.388  ? 212  GLY A CA  1 1 
ATOM   1417 C  C   . GLY A 1 176 ? -4.762  -12.952 15.973 1    23.814  ? 212  GLY A C   1 1 
ATOM   1418 O  O   . GLY A 1 176 ? -4.811  -13.833 16.826 1    22.669  ? 212  GLY A O   1 1 
ATOM   1419 N  N   . TYR A 1 177 ? -4.512  -11.668 16.301 1    22.503  ? 213  TYR A N   1 1 
ATOM   1420 C  CA  . TYR A 1 177 ? -4.34   -11.214 17.683 1    22.394  ? 213  TYR A CA  1 1 
ATOM   1421 C  C   . TYR A 1 177 ? -5.684  -10.814 18.288 1    23.196  ? 213  TYR A C   1 1 
ATOM   1422 O  O   . TYR A 1 177 ? -6.655  -10.728 17.552 1    22.703  ? 213  TYR A O   1 1 
ATOM   1423 C  CB  . TYR A 1 177 ? -3.279  -10.134 17.897 1    22.993  ? 213  TYR A CB  1 1 
ATOM   1424 C  CG  . TYR A 1 177 ? -1.906  -10.547 17.392 1    25.175  ? 213  TYR A CG  1 1 
ATOM   1425 C  CD1 . TYR A 1 177 ? -1.002  -11.198 18.227 1    24.348  ? 213  TYR A CD1 1 1 
ATOM   1426 C  CD2 . TYR A 1 177 ? -1.535  -10.335 16.065 1    27.894  ? 213  TYR A CD2 1 1 
ATOM   1427 C  CE1 . TYR A 1 177 ? 0.266   -11.544 17.778 1    24.615  ? 213  TYR A CE1 1 1 
ATOM   1428 C  CE2 . TYR A 1 177 ? -0.261  -10.678 15.616 1    26.64   ? 213  TYR A CE2 1 1 
ATOM   1429 C  CZ  . TYR A 1 177 ? 0.631   -11.302 16.465 1    24.635  ? 213  TYR A CZ  1 1 
ATOM   1430 O  OH  . TYR A 1 177 ? 1.867   -11.646 16.016 1    27.533  ? 213  TYR A OH  1 1 
ATOM   1431 N  N   . VAL A 1 178 ? -5.767  -10.551 19.615 1    24.555  ? 214  VAL A N   1 1 
ATOM   1432 C  CA  . VAL A 1 178 ? -7.067  -10.126 20.158 1    26.649  ? 214  VAL A CA  1 1 
ATOM   1433 C  C   . VAL A 1 178 ? -7.262  -8.606  20.019 1    26.595  ? 214  VAL A C   1 1 
ATOM   1434 O  O   . VAL A 1 178 ? -8.399  -8.115  19.899 1    27.987  ? 214  VAL A O   1 1 
ATOM   1435 C  CB  . VAL A 1 178 ? -7.445  -10.608 21.584 1    29.814  ? 214  VAL A CB  1 1 
ATOM   1436 C  CG1 . VAL A 1 178 ? -7.775  -12.074 21.56  1    36.403  ? 214  VAL A CG1 1 1 
ATOM   1437 C  CG2 . VAL A 1 178 ? -6.291  -10.422 22.548 1    30.126  ? 214  VAL A CG2 1 1 
ATOM   1438 N  N   . ASP A 1 179 ? -6.155  -7.852  20.065 1    23.123  ? 215  ASP A N   1 1 
ATOM   1439 C  CA  . ASP A 1 179 ? -6.16   -6.408  19.925 1    22.881  ? 215  ASP A CA  1 1 
ATOM   1440 C  C   . ASP A 1 179 ? -4.702  -5.97   19.686 1    20.085  ? 215  ASP A C   1 1 
ATOM   1441 O  O   . ASP A 1 179 ? -3.797  -6.792  19.695 1    21.238  ? 215  ASP A O   1 1 
ATOM   1442 C  CB  . ASP A 1 179 ? -6.782  -5.724  21.135 1    20.965  ? 215  ASP A CB  1 1 
ATOM   1443 C  CG  . ASP A 1 179 ? -5.982  -6.032  22.392 1    22.629  ? 215  ASP A CG  1 1 
ATOM   1444 O  OD1 . ASP A 1 179 ? -4.798  -5.581  22.499 1    21.398  ? 215  ASP A OD1 1 1 
ATOM   1445 O  OD2 . ASP A 1 179 ? -6.549  -6.723  23.266 1    23.425  ? 215  ASP A OD2 1 1 
ATOM   1446 N  N   . ALA A 1 180 ? -4.496  -4.686  19.424 1    19.314  ? 216  ALA A N   1 1 
ATOM   1447 C  CA  . ALA A 1 180 ? -3.222  -4.171  18.993 1    22.183  ? 216  ALA A CA  1 1 
ATOM   1448 C  C   . ALA A 1 180 ? -2.188  -4.315  20.096 1    22.468  ? 216  ALA A C   1 1 
ATOM   1449 O  O   . ALA A 1 180 ? -1.011  -4.511  19.811 1    23.026  ? 216  ALA A O   1 1 
ATOM   1450 C  CB  . ALA A 1 180 ? -3.355  -2.704  18.612 1    21.662  ? 216  ALA A CB  1 1 
ATOM   1451 N  N   . GLY A 1 181 ? -2.654  -4.245  21.353 1    22.426  ? 217  GLY A N   1 1 
ATOM   1452 C  CA  . GLY A 1 181 ? -1.731  -4.419  22.471 1    22.358  ? 217  GLY A CA  1 1 
ATOM   1453 C  C   . GLY A 1 181 ? -1.126  -5.821  22.522 1    22.457  ? 217  GLY A C   1 1 
ATOM   1454 O  O   . GLY A 1 181 ? 0.059   -5.979  22.792 1    24.572  ? 217  GLY A O   1 1 
ATOM   1455 N  N   . ASP A 1 182 ? -1.964  -6.824  22.294 1    18.661  ? 218  ASP A N   1 1 
ATOM   1456 C  CA  . ASP A 1 182 ? -1.551  -8.207  22.216 1    21.051  ? 218  ASP A CA  1 1 
ATOM   1457 C  C   . ASP A 1 182 ? -0.547  -8.368  21.065 1    24.533  ? 218  ASP A C   1 1 
ATOM   1458 O  O   . ASP A 1 182 ? 0.495   -9.006  21.266 1    20.505  ? 218  ASP A O   1 1 
ATOM   1459 C  CB  . ASP A 1 182 ? -2.821  -9.046  22.051 1    25.719  ? 218  ASP A CB  1 1 
ATOM   1460 C  CG  . ASP A 1 182 ? -2.593  -10.533 21.89  1    27.665  ? 218  ASP A CG  1 1 
ATOM   1461 O  OD1 . ASP A 1 182 ? -1.698  -11.005 22.607 1    26.923  ? 218  ASP A OD1 1 1 
ATOM   1462 O  OD2 . ASP A 1 182 ? -3.31   -11.18  21.033 1    30.22   ? 218  ASP A OD2 1 1 
ATOM   1463 N  N   A SER A 1 183 ? -0.857  -7.766  19.888 0.57 21.581  ? 219  SER A N   1 1 
ATOM   1464 N  N   B SER A 1 183 ? -0.83   -7.75   19.898 0.43 21.824  ? 219  SER A N   1 1 
ATOM   1465 C  CA  A SER A 1 183 ? 0.115   -7.755  18.812 0.57 22.862  ? 219  SER A CA  1 1 
ATOM   1466 C  CA  B SER A 1 183 ? 0.157   -7.798  18.835 0.43 22.58   ? 219  SER A CA  1 1 
ATOM   1467 C  C   A SER A 1 183 ? 1.452   -7.117  19.24  0.57 24.409  ? 219  SER A C   1 1 
ATOM   1468 C  C   B SER A 1 183 ? 1.477   -7.12   19.244 0.43 24.084  ? 219  SER A C   1 1 
ATOM   1469 O  O   A SER A 1 183 ? 2.513   -7.66   18.957 0.57 23.372  ? 219  SER A O   1 1 
ATOM   1470 O  O   B SER A 1 183 ? 2.548   -7.637  18.949 0.43 23.143  ? 219  SER A O   1 1 
ATOM   1471 C  CB  A SER A 1 183 ? -0.497  -7.159  17.551 0.57 21.796  ? 219  SER A CB  1 1 
ATOM   1472 C  CB  B SER A 1 183 ? -0.423  -7.296  17.53  0.43 21.447  ? 219  SER A CB  1 1 
ATOM   1473 O  OG  A SER A 1 183 ? 0.479   -6.997  16.529 0.57 23.123  ? 219  SER A OG  1 1 
ATOM   1474 O  OG  B SER A 1 183 ? -0.614  -5.892  17.568 0.43 20.657  ? 219  SER A OG  1 1 
ATOM   1475 N  N   . TRP A 1 184 ? 1.431   -5.997  19.978 1    26.052  ? 220  TRP A N   1 1 
ATOM   1476 C  CA  . TRP A 1 184 ? 2.687   -5.356  20.431 1    27.737  ? 220  TRP A CA  1 1 
ATOM   1477 C  C   . TRP A 1 184 ? 3.503   -6.26   21.397 1    23.738  ? 220  TRP A C   1 1 
ATOM   1478 O  O   . TRP A 1 184 ? 4.707   -6.464  21.203 1    22      ? 220  TRP A O   1 1 
ATOM   1479 C  CB  . TRP A 1 184 ? 2.476   -3.94   21.024 1    23.501  ? 220  TRP A CB  1 1 
ATOM   1480 C  CG  . TRP A 1 184 ? 2.006   -2.893  20.039 1    20.062  ? 220  TRP A CG  1 1 
ATOM   1481 C  CD1 . TRP A 1 184 ? 1.818   -3.032  18.695 1    21.906  ? 220  TRP A CD1 1 1 
ATOM   1482 C  CD2 . TRP A 1 184 ? 1.771   -1.494  20.305 1    20.135  ? 220  TRP A CD2 1 1 
ATOM   1483 N  NE1 . TRP A 1 184 ? 1.457   -1.842  18.12  1    22.593  ? 220  TRP A NE1 1 1 
ATOM   1484 C  CE2 . TRP A 1 184 ? 1.434   -0.868  19.068 1    20.558  ? 220  TRP A CE2 1 1 
ATOM   1485 C  CE3 . TRP A 1 184 ? 1.825   -0.711  21.455 1    16.178  ? 220  TRP A CE3 1 1 
ATOM   1486 C  CZ2 . TRP A 1 184 ? 1.123   0.501   18.963 1    21.864  ? 220  TRP A CZ2 1 1 
ATOM   1487 C  CZ3 . TRP A 1 184 ? 1.612   0.646   21.31  1    17.298  ? 220  TRP A CZ3 1 1 
ATOM   1488 C  CH2 . TRP A 1 184 ? 1.191   1.243   20.127 1    17.217  ? 220  TRP A CH2 1 1 
ATOM   1489 N  N   . ARG A 1 185 ? 2.85    -6.798  22.441 1    19.596  ? 221  ARG A N   1 1 
ATOM   1490 C  CA  . ARG A 1 185 ? 3.446   -7.693  23.441 1    19.847  ? 221  ARG A CA  1 1 
ATOM   1491 C  C   . ARG A 1 185 ? 4.07    -8.91   22.723 1    20.705  ? 221  ARG A C   1 1 
ATOM   1492 O  O   . ARG A 1 185 ? 5.181   -9.353  23.075 1    21.148  ? 221  ARG A O   1 1 
ATOM   1493 C  CB  . ARG A 1 185 ? 2.398   -8.071  24.5   1    17.656  ? 221  ARG A CB  1 1 
ATOM   1494 C  CG  . ARG A 1 185 ? 1.99    -6.903  25.377 1    17.935  ? 221  ARG A CG  1 1 
ATOM   1495 C  CD  . ARG A 1 185 ? 1.118   -7.393  26.544 1    18.448  ? 221  ARG A CD  1 1 
ATOM   1496 N  NE  . ARG A 1 185 ? -0.155  -8.064  26.233 1    19.708  ? 221  ARG A NE  1 1 
ATOM   1497 C  CZ  . ARG A 1 185 ? -1.326  -7.473  26.029 1    20.056  ? 221  ARG A CZ  1 1 
ATOM   1498 N  NH1 . ARG A 1 185 ? -2.364  -8.21   25.691 1    18.963  ? 221  ARG A NH1 1 1 
ATOM   1499 N  NH2 . ARG A 1 185 ? -1.446  -6.153  26.056 1    19.706  ? 221  ARG A NH2 1 1 
ATOM   1500 N  N   . SER A 1 186 ? 3.529   -9.278  21.538 1    19.422  ? 222  SER A N   1 1 
ATOM   1501 C  CA  . SER A 1 186 ? 3.928   -10.571 20.943 1    22.479  ? 222  SER A CA  1 1 
ATOM   1502 C  C   . SER A 1 186 ? 5.358   -10.437 20.413 1    20.009  ? 222  SER A C   1 1 
ATOM   1503 O  O   . SER A 1 186 ? 6.059   -11.404 20.241 1    17.725  ? 222  SER A O   1 1 
ATOM   1504 C  CB  . SER A 1 186 ? 3.018   -11.048 19.828 1    24.796  ? 222  SER A CB  1 1 
ATOM   1505 O  OG  . SER A 1 186 ? 3.334   -10.34  18.608 1    25.457  ? 222  SER A OG  1 1 
ATOM   1506 N  N   . MET A 1 187 ? 5.83    -9.209  20.275 1    18.811  ? 223  MET A N   1 1 
ATOM   1507 C  CA  . MET A 1 187 ? 7.162   -8.956  19.751 1    23.079  ? 223  MET A CA  1 1 
ATOM   1508 C  C   . MET A 1 187 ? 8.25    -9.502  20.676 1    21.842  ? 223  MET A C   1 1 
ATOM   1509 O  O   . MET A 1 187 ? 9.371   -9.631  20.223 1    25.67   ? 223  MET A O   1 1 
ATOM   1510 C  CB  . MET A 1 187 ? 7.396   -7.433  19.577 1    23.294  ? 223  MET A CB  1 1 
ATOM   1511 C  CG  . MET A 1 187 ? 6.618   -6.822  18.408 1    27.275  ? 223  MET A CG  1 1 
ATOM   1512 S  SD  . MET A 1 187 ? 6.966   -5.066  18.096 1    33.93   ? 223  MET A SD  1 1 
ATOM   1513 C  CE  . MET A 1 187 ? 6.315   -4.183  19.5   1    27.466  ? 223  MET A CE  1 1 
ATOM   1514 N  N   . TYR A 1 188 ? 7.97    -9.614  21.976 1    20.502  ? 224  TYR A N   1 1 
ATOM   1515 C  CA  . TYR A 1 188 ? 8.854   -10.202 22.981 1    24.293  ? 224  TYR A CA  1 1 
ATOM   1516 C  C   . TYR A 1 188 ? 8.855   -11.736 23.001 1    23.74   ? 224  TYR A C   1 1 
ATOM   1517 O  O   . TYR A 1 188 ? 9.774   -12.318 23.631 1    23.863  ? 224  TYR A O   1 1 
ATOM   1518 C  CB  . TYR A 1 188 ? 8.5     -9.699  24.399 1    20.234  ? 224  TYR A CB  1 1 
ATOM   1519 C  CG  . TYR A 1 188 ? 8.831   -8.235  24.416 1    20.409  ? 224  TYR A CG  1 1 
ATOM   1520 C  CD1 . TYR A 1 188 ? 7.899   -7.27   23.988 1    22.292  ? 224  TYR A CD1 1 1 
ATOM   1521 C  CD2 . TYR A 1 188 ? 10.101  -7.813  24.8   1    25.322  ? 224  TYR A CD2 1 1 
ATOM   1522 C  CE1 . TYR A 1 188 ? 8.271   -5.928  23.916 1    22.63   ? 224  TYR A CE1 1 1 
ATOM   1523 C  CE2 . TYR A 1 188 ? 10.474  -6.457  24.731 1    27.538  ? 224  TYR A CE2 1 1 
ATOM   1524 C  CZ  . TYR A 1 188 ? 9.558   -5.508  24.292 1    24.954  ? 224  TYR A CZ  1 1 
ATOM   1525 O  OH  . TYR A 1 188 ? 9.936   -4.161  24.19  1    23.365  ? 224  TYR A OH  1 1 
ATOM   1526 N  N   . GLU A 1 189 ? 7.846   -12.385 22.385 1    22.693  ? 225  GLU A N   1 1 
ATOM   1527 C  CA  . GLU A 1 189 ? 7.707   -13.861 22.397 1    25.824  ? 225  GLU A CA  1 1 
ATOM   1528 C  C   . GLU A 1 189 ? 7.856   -14.441 23.823 1    24.956  ? 225  GLU A C   1 1 
ATOM   1529 O  O   . GLU A 1 189 ? 8.623   -15.381 24.047 1    27.701  ? 225  GLU A O   1 1 
ATOM   1530 C  CB  . GLU A 1 189 ? 8.781   -14.604 21.598 1    25.856  ? 225  GLU A CB  1 1 
ATOM   1531 C  CG  . GLU A 1 189 ? 8.936   -14.073 20.186 1    32.734  ? 225  GLU A CG  1 1 
ATOM   1532 C  CD  . GLU A 1 189 ? 9.856   -14.861 19.239 1    38.681  ? 225  GLU A CD  1 1 
ATOM   1533 O  OE1 . GLU A 1 189 ? 11.023  -15.316 19.449 1    36.425  ? 225  GLU A OE1 1 1 
ATOM   1534 O  OE2 . GLU A 1 189 ? 9.285   -15.012 18.163 1    44.937  ? 225  GLU A OE2 1 1 
ATOM   1535 N  N   . THR A 1 190 ? 7.279   -13.788 24.821 1    23.108  ? 226  THR A N   1 1 
ATOM   1536 C  CA  . THR A 1 190 ? 7.51    -14.138 26.23  1    22.859  ? 226  THR A CA  1 1 
ATOM   1537 C  C   . THR A 1 190 ? 6.126   -14.141 26.872 1    21.545  ? 226  THR A C   1 1 
ATOM   1538 O  O   . THR A 1 190 ? 5.562   -13.106 27.226 1    22.714  ? 226  THR A O   1 1 
ATOM   1539 C  CB  . THR A 1 190 ? 8.366   -13.057 26.913 1    25.007  ? 226  THR A CB  1 1 
ATOM   1540 O  OG1 . THR A 1 190 ? 9.656   -13.155 26.32  1    28.696  ? 226  THR A OG1 1 1 
ATOM   1541 C  CG2 . THR A 1 190 ? 8.57    -13.29  28.397 1    22.454  ? 226  THR A CG2 1 1 
ATOM   1542 N  N   . PRO A 1 191 ? 5.484   -15.317 26.921 1    23.458  ? 227  PRO A N   1 1 
ATOM   1543 C  CA  . PRO A 1 191 ? 4.12    -15.381 27.455 1    25.148  ? 227  PRO A CA  1 1 
ATOM   1544 C  C   . PRO A 1 191 ? 3.938   -14.804 28.87  1    23.91   ? 227  PRO A C   1 1 
ATOM   1545 O  O   . PRO A 1 191 ? 2.841   -14.346 29.213 1    25.725  ? 227  PRO A O   1 1 
ATOM   1546 C  CB  . PRO A 1 191 ? 3.792   -16.872 27.366 1    25.646  ? 227  PRO A CB  1 1 
ATOM   1547 C  CG  . PRO A 1 191 ? 4.868   -17.512 26.466 1    26.607  ? 227  PRO A CG  1 1 
ATOM   1548 C  CD  . PRO A 1 191 ? 6.057   -16.584 26.438 1    22.117  ? 227  PRO A CD  1 1 
ATOM   1549 N  N   . SER A 1 192 ? 5.001   -14.848 29.71  1    23.903  ? 228  SER A N   1 1 
ATOM   1550 C  CA  . SER A 1 192 ? 4.993   -14.315 31.091 1    24.999  ? 228  SER A CA  1 1 
ATOM   1551 C  C   . SER A 1 192 ? 5.41    -12.819 31.131 1    22.134  ? 228  SER A C   1 1 
ATOM   1552 O  O   . SER A 1 192 ? 5.728   -12.296 32.195 1    23.337  ? 228  SER A O   1 1 
ATOM   1553 C  CB  . SER A 1 192 ? 5.995   -15.131 31.923 1    26.016  ? 228  SER A CB  1 1 
ATOM   1554 O  OG  . SER A 1 192 ? 7.333   -14.898 31.436 1    25.263  ? 228  SER A OG  1 1 
ATOM   1555 N  N   . LEU A 1 193 ? 5.498   -12.135 29.983 1    21.41   ? 229  LEU A N   1 1 
ATOM   1556 C  CA  . LEU A 1 193 ? 5.897   -10.734 29.947 1    23.049  ? 229  LEU A CA  1 1 
ATOM   1557 C  C   . LEU A 1 193 ? 5.266   -9.842  31.039 1    26.179  ? 229  LEU A C   1 1 
ATOM   1558 O  O   . LEU A 1 193 ? 5.99    -9.059  31.697 1    26.1    ? 229  LEU A O   1 1 
ATOM   1559 C  CB  . LEU A 1 193 ? 5.687   -10.11  28.572 1    21.879  ? 229  LEU A CB  1 1 
ATOM   1560 C  CG  . LEU A 1 193 ? 6.194   -8.667  28.377 1    21.445  ? 229  LEU A CG  1 1 
ATOM   1561 C  CD1 . LEU A 1 193 ? 7.711   -8.618  28.259 1    22.324  ? 229  LEU A CD1 1 1 
ATOM   1562 C  CD2 . LEU A 1 193 ? 5.663   -8.226  27.007 1    20.889  ? 229  LEU A CD2 1 1 
ATOM   1563 N  N   . GLU A 1 194 ? 3.912   -9.778  31.131 1    22.408  ? 230  GLU A N   1 1 
ATOM   1564 C  CA  . GLU A 1 194 ? 3.345   -8.743  31.979 1    23.868  ? 230  GLU A CA  1 1 
ATOM   1565 C  C   . GLU A 1 194 ? 3.785   -8.987  33.421 1    24.504  ? 230  GLU A C   1 1 
ATOM   1566 O  O   . GLU A 1 194 ? 4.064   -8.04   34.134 1    24.121  ? 230  GLU A O   1 1 
ATOM   1567 C  CB  . GLU A 1 194 ? 1.816   -8.565  31.936 1    23.705  ? 230  GLU A CB  1 1 
ATOM   1568 C  CG  . GLU A 1 194 ? 1.346   -8.209  30.523 1    27.65   ? 230  GLU A CG  1 1 
ATOM   1569 C  CD  . GLU A 1 194 ? -0.151  -7.88   30.422 1    31.013  ? 230  GLU A CD  1 1 
ATOM   1570 O  OE1 . GLU A 1 194 ? -0.833  -7.926  31.445 1    30.363  ? 230  GLU A OE1 1 1 
ATOM   1571 O  OE2 . GLU A 1 194 ? -0.668  -7.66   29.325 1    31.976  ? 230  GLU A OE2 1 1 
ATOM   1572 N  N   . GLN A 1 195 ? 3.816   -10.24  33.861 1    19.877  ? 231  GLN A N   1 1 
ATOM   1573 C  CA  . GLN A 1 195 ? 4.233   -10.574 35.237 1    21.561  ? 231  GLN A CA  1 1 
ATOM   1574 C  C   . GLN A 1 195 ? 5.738   -10.286 35.425 1    22.201  ? 231  GLN A C   1 1 
ATOM   1575 O  O   . GLN A 1 195 ? 6.168   -9.843  36.496 1    26.756  ? 231  GLN A O   1 1 
ATOM   1576 C  CB  . GLN A 1 195 ? 3.916   -12.052 35.608 1    21.906  ? 231  GLN A CB  1 1 
ATOM   1577 N  N   . ASP A 1 196 ? 6.571   -10.579 34.41  1    20.982  ? 232  ASP A N   1 1 
ATOM   1578 C  CA  . ASP A 1 196 ? 8.01    -10.35  34.49  1    22.379  ? 232  ASP A CA  1 1 
ATOM   1579 C  C   . ASP A 1 196 ? 8.297   -8.851  34.624 1    26.717  ? 232  ASP A C   1 1 
ATOM   1580 O  O   . ASP A 1 196 ? 9.099   -8.488  35.485 1    24.161  ? 232  ASP A O   1 1 
ATOM   1581 C  CB  . ASP A 1 196 ? 8.793   -10.765 33.252 1    24.809  ? 232  ASP A CB  1 1 
ATOM   1582 C  CG  . ASP A 1 196 ? 8.774   -12.257 32.94  1    29.875  ? 232  ASP A CG  1 1 
ATOM   1583 O  OD1 . ASP A 1 196 ? 8.585   -12.995 33.89  1    31.603  ? 232  ASP A OD1 1 1 
ATOM   1584 O  OD2 . ASP A 1 196 ? 8.88    -12.636 31.739 1    36.742  ? 232  ASP A OD2 1 1 
ATOM   1585 N  N   . LEU A 1 197 ? 7.579   -8.023  33.841 1    24.146  ? 233  LEU A N   1 1 
ATOM   1586 C  CA  . LEU A 1 197 ? 7.867   -6.602  33.926 1    21.983  ? 233  LEU A CA  1 1 
ATOM   1587 C  C   . LEU A 1 197 ? 7.416   -6.056  35.274 1    23.072  ? 233  LEU A C   1 1 
ATOM   1588 O  O   . LEU A 1 197 ? 8.086   -5.201  35.789 1    21.285  ? 233  LEU A O   1 1 
ATOM   1589 C  CB  . LEU A 1 197 ? 7.173   -5.887  32.793 1    21.57   ? 233  LEU A CB  1 1 
ATOM   1590 C  CG  . LEU A 1 197 ? 7.743   -6.258  31.423 1    22.311  ? 233  LEU A CG  1 1 
ATOM   1591 C  CD1 . LEU A 1 197 ? 6.961   -5.606  30.306 1    18.593  ? 233  LEU A CD1 1 1 
ATOM   1592 C  CD2 . LEU A 1 197 ? 9.284   -6.21   31.226 1    22.417  ? 233  LEU A CD2 1 1 
ATOM   1593 N  N   . GLU A 1 198 ? 6.296   -6.55   35.804 1    23.468  ? 234  GLU A N   1 1 
ATOM   1594 C  CA  . GLU A 1 198 ? 5.745   -6.22   37.118 1    31.055  ? 234  GLU A CA  1 1 
ATOM   1595 C  C   . GLU A 1 198 ? 6.779   -6.486  38.241 1    27.203  ? 234  GLU A C   1 1 
ATOM   1596 O  O   . GLU A 1 198 ? 7.068   -5.63   39.091 1    28.777  ? 234  GLU A O   1 1 
ATOM   1597 C  CB  . GLU A 1 198 ? 4.352   -6.883  37.263 1    33.255  ? 234  GLU A CB  1 1 
ATOM   1598 C  CG  . GLU A 1 198 ? 3.564   -6.616  38.553 1    36.254  ? 234  GLU A CG  1 1 
ATOM   1599 C  CD  . GLU A 1 198 ? 3.432   -5.129  38.845 1    51.429  ? 234  GLU A CD  1 1 
ATOM   1600 O  OE1 . GLU A 1 198 ? 3.102   -4.394  37.883 1    61.597  ? 234  GLU A OE1 1 1 
ATOM   1601 O  OE2 . GLU A 1 198 ? 3.635   -4.651  40     1    61.921  ? 234  GLU A OE2 1 1 
ATOM   1602 N  N   . ARG A 1 199 ? 7.371   -7.671  38.226 1    29.938  ? 235  ARG A N   1 1 
ATOM   1603 C  CA  . ARG A 1 199 ? 8.369   -8.03   39.215 1    29.707  ? 235  ARG A CA  1 1 
ATOM   1604 C  C   . ARG A 1 199 ? 9.558   -7.072  39.131 1    29.182  ? 235  ARG A C   1 1 
ATOM   1605 O  O   . ARG A 1 199 ? 10.048  -6.66   40.161 1    25.547  ? 235  ARG A O   1 1 
ATOM   1606 C  CB  . ARG A 1 199 ? 8.881   -9.45   38.953 1    31.068  ? 235  ARG A CB  1 1 
ATOM   1607 C  CG  . ARG A 1 199 ? 7.879   -10.294 39.726 1    38.599  ? 235  ARG A CG  1 1 
ATOM   1608 C  CD  . ARG A 1 199 ? 8.523   -11.588 40.199 1    52.475  ? 235  ARG A CD  1 1 
ATOM   1609 N  NE  . ARG A 1 199 ? 7.832   -12.565 39.367 1    54.488  ? 235  ARG A NE  1 1 
ATOM   1610 C  CZ  . ARG A 1 199 ? 8.143   -12.71  38.088 1    58.675  ? 235  ARG A CZ  1 1 
ATOM   1611 N  NH1 . ARG A 1 199 ? 9.416   -12.635 37.714 1    54.782  ? 235  ARG A NH1 1 1 
ATOM   1612 N  NH2 . ARG A 1 199 ? 7.181   -13.024 37.225 1    51.323  ? 235  ARG A NH2 1 1 
ATOM   1613 N  N   . LEU A 1 200 ? 10.028  -6.758  37.909 1    26.283  ? 236  LEU A N   1 1 
ATOM   1614 C  CA  . LEU A 1 200 ? 11.157  -5.843  37.746 1    29.825  ? 236  LEU A CA  1 1 
ATOM   1615 C  C   . LEU A 1 200 ? 10.804  -4.466  38.295 1    29.742  ? 236  LEU A C   1 1 
ATOM   1616 O  O   . LEU A 1 200 ? 11.621  -3.817  38.984 1    32.406  ? 236  LEU A O   1 1 
ATOM   1617 C  CB  . LEU A 1 200 ? 11.614  -5.764  36.3   1    24.073  ? 236  LEU A CB  1 1 
ATOM   1618 C  CG  . LEU A 1 200 ? 12.039  -7.104  35.691 1    23.224  ? 236  LEU A CG  1 1 
ATOM   1619 C  CD1 . LEU A 1 200 ? 12.016  -6.781  34.186 1    23.925  ? 236  LEU A CD1 1 1 
ATOM   1620 C  CD2 . LEU A 1 200 ? 13.468  -7.501  36.165 1    20.062  ? 236  LEU A CD2 1 1 
ATOM   1621 N  N   . PHE A 1 201 ? 9.574   -4.018  37.979 1    25.43   ? 237  PHE A N   1 1 
ATOM   1622 C  CA  . PHE A 1 201 ? 9.157   -2.713  38.455 1    23.584  ? 237  PHE A CA  1 1 
ATOM   1623 C  C   . PHE A 1 201 ? 9.141   -2.724  39.995 1    22.366  ? 237  PHE A C   1 1 
ATOM   1624 O  O   . PHE A 1 201 ? 9.662   -1.81   40.612 1    21.313  ? 237  PHE A O   1 1 
ATOM   1625 C  CB  . PHE A 1 201 ? 7.802   -2.366  37.849 1    20.706  ? 237  PHE A CB  1 1 
ATOM   1626 C  CG  . PHE A 1 201 ? 7.296   -1.072  38.442 1    27.429  ? 237  PHE A CG  1 1 
ATOM   1627 C  CD1 . PHE A 1 201 ? 7.839   0.139   38.054 1    23.212  ? 237  PHE A CD1 1 1 
ATOM   1628 C  CD2 . PHE A 1 201 ? 6.362   -1.08   39.49  1    37.71   ? 237  PHE A CD2 1 1 
ATOM   1629 C  CE1 . PHE A 1 201 ? 7.361   1.305   38.585 1    30.517  ? 237  PHE A CE1 1 1 
ATOM   1630 C  CE2 . PHE A 1 201 ? 5.895   0.106   40.038 1    28.336  ? 237  PHE A CE2 1 1 
ATOM   1631 C  CZ  . PHE A 1 201 ? 6.407   1.295   39.589 1    32.269  ? 237  PHE A CZ  1 1 
ATOM   1632 N  N   . GLN A 1 202 ? 8.615   -3.779  40.628 1    25.35   ? 238  GLN A N   1 1 
ATOM   1633 C  CA  . GLN A 1 202 ? 8.577   -3.826  42.098 1    27.746  ? 238  GLN A CA  1 1 
ATOM   1634 C  C   . GLN A 1 202 ? 9.959   -3.784  42.752 1    29.054  ? 238  GLN A C   1 1 
ATOM   1635 O  O   . GLN A 1 202 ? 10.104  -3.185  43.811 1    26.247  ? 238  GLN A O   1 1 
ATOM   1636 C  CB  . GLN A 1 202 ? 7.719   -4.987  42.574 1    26.58   ? 238  GLN A CB  1 1 
ATOM   1637 C  CG  . GLN A 1 202 ? 6.275   -4.786  42.122 1    33.614  ? 238  GLN A CG  1 1 
ATOM   1638 C  CD  . GLN A 1 202 ? 5.625   -3.584  42.79  1    41.83   ? 238  GLN A CD  1 1 
ATOM   1639 O  OE1 . GLN A 1 202 ? 5.95    -3.248  43.929 1    40.415  ? 238  GLN A OE1 1 1 
ATOM   1640 N  NE2 . GLN A 1 202 ? 4.66    -2.951  42.136 1    42.784  ? 238  GLN A NE2 1 1 
ATOM   1641 N  N   . GLU A 1 203 ? 10.966  -4.388  42.113 1    26.237  ? 239  GLU A N   1 1 
ATOM   1642 C  CA  . GLU A 1 203 ? 12.325  -4.309  42.623 1    28.469  ? 239  GLU A CA  1 1 
ATOM   1643 C  C   . GLU A 1 203 ? 12.94   -2.906  42.611 1    26.695  ? 239  GLU A C   1 1 
ATOM   1644 O  O   . GLU A 1 203 ? 13.799  -2.652  43.455 1    24.714  ? 239  GLU A O   1 1 
ATOM   1645 C  CB  . GLU A 1 203 ? 13.169  -5.293  41.855 1    29.629  ? 239  GLU A CB  1 1 
ATOM   1646 C  CG  . GLU A 1 203 ? 12.606  -6.673  42.183 1    42.117  ? 239  GLU A CG  1 1 
ATOM   1647 C  CD  . GLU A 1 203 ? 13.76   -7.484  41.729 1    54.53   ? 239  GLU A CD  1 1 
ATOM   1648 O  OE1 . GLU A 1 203 ? 14.541  -7.759  42.665 1    70.591  ? 239  GLU A OE1 1 1 
ATOM   1649 O  OE2 . GLU A 1 203 ? 13.925  -7.713  40.487 1    67.916  ? 239  GLU A OE2 1 1 
ATOM   1650 N  N   . LEU A 1 204 ? 12.599  -2.042  41.645 1    26.549  ? 240  LEU A N   1 1 
ATOM   1651 C  CA  . LEU A 1 204 ? 13.04   -0.643  41.677 1    26.038  ? 240  LEU A CA  1 1 
ATOM   1652 C  C   . LEU A 1 204 ? 12.263  0.283   42.624 1    27.467  ? 240  LEU A C   1 1 
ATOM   1653 O  O   . LEU A 1 204 ? 12.551  1.478   42.668 1    28.294  ? 240  LEU A O   1 1 
ATOM   1654 C  CB  . LEU A 1 204 ? 12.998  -0.026  40.288 1    25.836  ? 240  LEU A CB  1 1 
ATOM   1655 C  CG  . LEU A 1 204 ? 14.193  -0.318  39.361 1    30.455  ? 240  LEU A CG  1 1 
ATOM   1656 C  CD1 . LEU A 1 204 ? 15.5    0.375   39.72  1    29.223  ? 240  LEU A CD1 1 1 
ATOM   1657 C  CD2 . LEU A 1 204 ? 14.447  -1.761  39.209 1    24.322  ? 240  LEU A CD2 1 1 
ATOM   1658 N  N   . GLN A 1 205 ? 11.308  -0.198  43.423 1    27.748  ? 241  GLN A N   1 1 
ATOM   1659 C  CA  . GLN A 1 205 ? 10.505  0.708   44.245 1    30.928  ? 241  GLN A CA  1 1 
ATOM   1660 C  C   . GLN A 1 205 ? 11.297  1.391   45.373 1    33.994  ? 241  GLN A C   1 1 
ATOM   1661 O  O   . GLN A 1 205 ? 11.22   2.605   45.569 1    31.937  ? 241  GLN A O   1 1 
ATOM   1662 C  CB  . GLN A 1 205 ? 9.322   -0.086  44.789 1    35.529  ? 241  GLN A CB  1 1 
ATOM   1663 C  CG  . GLN A 1 205 ? 8.239   -0.2    43.713 1    35.031  ? 241  GLN A CG  1 1 
ATOM   1664 C  CD  . GLN A 1 205 ? 7.505   1.105   43.49  1    33.865  ? 241  GLN A CD  1 1 
ATOM   1665 O  OE1 . GLN A 1 205 ? 7.77    1.828   42.545 1    35.512  ? 241  GLN A OE1 1 1 
ATOM   1666 N  NE2 . GLN A 1 205 ? 6.602   1.438   44.395 1    36.055  ? 241  GLN A NE2 1 1 
ATOM   1667 N  N   . PRO A 1 206 ? 12.058  0.66    46.213 1    33.748  ? 242  PRO A N   1 1 
ATOM   1668 C  CA  . PRO A 1 206 ? 12.945  1.325   47.162 1    32.945  ? 242  PRO A CA  1 1 
ATOM   1669 C  C   . PRO A 1 206 ? 13.71   2.515   46.576 1    31.166  ? 242  PRO A C   1 1 
ATOM   1670 O  O   . PRO A 1 206 ? 13.758  3.593   47.166 1    34.873  ? 242  PRO A O   1 1 
ATOM   1671 C  CB  . PRO A 1 206 ? 13.872  0.166   47.716 1    31.734  ? 242  PRO A CB  1 1 
ATOM   1672 C  CG  . PRO A 1 206 ? 12.927  -1.047  47.623 1    31.907  ? 242  PRO A CG  1 1 
ATOM   1673 C  CD  . PRO A 1 206 ? 12.027  -0.802  46.386 1    31.792  ? 242  PRO A CD  1 1 
ATOM   1674 N  N   . LEU A 1 207 ? 14.411  2.302   45.475 1    26.65   ? 243  LEU A N   1 1 
ATOM   1675 C  CA  . LEU A 1 207 ? 15.208  3.391   44.96  1    25.172  ? 243  LEU A CA  1 1 
ATOM   1676 C  C   . LEU A 1 207 ? 14.261  4.521   44.51  1    28.436  ? 243  LEU A C   1 1 
ATOM   1677 O  O   . LEU A 1 207 ? 14.5    5.7     44.847 1    24.17   ? 243  LEU A O   1 1 
ATOM   1678 C  CB  . LEU A 1 207 ? 15.914  2.781   43.764 1    23.864  ? 243  LEU A CB  1 1 
ATOM   1679 C  CG  . LEU A 1 207 ? 17.341  3.183   43.43  1    33.015  ? 243  LEU A CG  1 1 
ATOM   1680 C  CD1 . LEU A 1 207 ? 18.17   3.687   44.587 1    30.957  ? 243  LEU A CD1 1 1 
ATOM   1681 C  CD2 . LEU A 1 207 ? 17.985  1.909   42.818 1    30.347  ? 243  LEU A CD2 1 1 
ATOM   1682 N  N   . TYR A 1 208 ? 13.261  4.174   43.657 1    22.872  ? 244  TYR A N   1 1 
ATOM   1683 C  CA  . TYR A 1 208 ? 12.345  5.22    43.199 1    21.578  ? 244  TYR A CA  1 1 
ATOM   1684 C  C   . TYR A 1 208 ? 11.694  5.966   44.383 1    19.53   ? 244  TYR A C   1 1 
ATOM   1685 O  O   . TYR A 1 208 ? 11.69   7.199   44.419 1    19.238  ? 244  TYR A O   1 1 
ATOM   1686 C  CB  . TYR A 1 208 ? 11.247  4.724   42.265 1    18.862  ? 244  TYR A CB  1 1 
ATOM   1687 C  CG  . TYR A 1 208 ? 10.488  5.916   41.711 1    21.995  ? 244  TYR A CG  1 1 
ATOM   1688 C  CD1 . TYR A 1 208 ? 11.143  6.836   40.859 1    21.456  ? 244  TYR A CD1 1 1 
ATOM   1689 C  CD2 . TYR A 1 208 ? 9.14    6.117   42.07  1    21.263  ? 244  TYR A CD2 1 1 
ATOM   1690 C  CE1 . TYR A 1 208 ? 10.499  7.99    40.432 1    23.23   ? 244  TYR A CE1 1 1 
ATOM   1691 C  CE2 . TYR A 1 208 ? 8.487   7.27    41.633 1    22.061  ? 244  TYR A CE2 1 1 
ATOM   1692 C  CZ  . TYR A 1 208 ? 9.147   8.164   40.775 1    23.602  ? 244  TYR A CZ  1 1 
ATOM   1693 O  OH  . TYR A 1 208 ? 8.422   9.213   40.256 1    21.52   ? 244  TYR A OH  1 1 
ATOM   1694 N  N   . LEU A 1 209 ? 11.029  5.259   45.295 1    18.462  ? 245  LEU A N   1 1 
ATOM   1695 C  CA  . LEU A 1 209 ? 10.412  5.935   46.434 1    21.097  ? 245  LEU A CA  1 1 
ATOM   1696 C  C   . LEU A 1 209 ? 11.392  6.857   47.169 1    20.198  ? 245  LEU A C   1 1 
ATOM   1697 O  O   . LEU A 1 209 ? 11.013  7.963   47.511 1    19.757  ? 245  LEU A O   1 1 
ATOM   1698 C  CB  . LEU A 1 209 ? 9.731   5.012   47.439 1    23.563  ? 245  LEU A CB  1 1 
ATOM   1699 C  CG  . LEU A 1 209 ? 8.594   4.188   46.837 1    27.046  ? 245  LEU A CG  1 1 
ATOM   1700 C  CD1 . LEU A 1 209 ? 8.142   3.081   47.723 1    24.84   ? 245  LEU A CD1 1 1 
ATOM   1701 C  CD2 . LEU A 1 209 ? 7.459   5.105   46.424 1    25.369  ? 245  LEU A CD2 1 1 
ATOM   1702 N  N   . ASN A 1 210 ? 12.612  6.38    47.451 1    19.551  ? 246  ASN A N   1 1 
ATOM   1703 C  CA  . ASN A 1 210 ? 13.597  7.213   48.14  1    22.505  ? 246  ASN A CA  1 1 
ATOM   1704 C  C   . ASN A 1 210 ? 13.978  8.458   47.334 1    22.446  ? 246  ASN A C   1 1 
ATOM   1705 O  O   . ASN A 1 210 ? 14.171  9.517   47.925 1    25.601  ? 246  ASN A O   1 1 
ATOM   1706 C  CB  . ASN A 1 210 ? 14.774  6.366   48.617 1    20.414  ? 246  ASN A CB  1 1 
ATOM   1707 C  CG  . ASN A 1 210 ? 14.428  5.652   49.904 1    23.691  ? 246  ASN A CG  1 1 
ATOM   1708 O  OD1 . ASN A 1 210 ? 14.528  6.234   51.007 1    24.933  ? 246  ASN A OD1 1 1 
ATOM   1709 N  ND2 . ASN A 1 210 ? 14.052  4.382   49.8   1    23.524  ? 246  ASN A ND2 1 1 
ATOM   1710 N  N   . LEU A 1 211 ? 14.216  8.305   46.017 1    22.111  ? 247  LEU A N   1 1 
ATOM   1711 C  CA  . LEU A 1 211 ? 14.566  9.418   45.153 1    22.259  ? 247  LEU A CA  1 1 
ATOM   1712 C  C   . LEU A 1 211 ? 13.417  10.433  45.114 1    19.692  ? 247  LEU A C   1 1 
ATOM   1713 O  O   . LEU A 1 211 ? 13.645  11.657  45.22  1    18.014  ? 247  LEU A O   1 1 
ATOM   1714 C  CB  . LEU A 1 211 ? 14.902  8.937   43.733 1    20.788  ? 247  LEU A CB  1 1 
ATOM   1715 C  CG  . LEU A 1 211 ? 15.257  10.063  42.731 1    22.476  ? 247  LEU A CG  1 1 
ATOM   1716 C  CD1 . LEU A 1 211 ? 16.641  10.69   42.973 1    22.022  ? 247  LEU A CD1 1 1 
ATOM   1717 C  CD2 . LEU A 1 211 ? 15.209  9.49    41.276 1    20.474  ? 247  LEU A CD2 1 1 
ATOM   1718 N  N   . HIS A 1 212 ? 12.191  9.901   45.009 1    16.161  ? 248  HIS A N   1 1 
ATOM   1719 C  CA  . HIS A 1 212 ? 11.013  10.75   44.951 1    16.998  ? 248  HIS A CA  1 1 
ATOM   1720 C  C   . HIS A 1 212 ? 10.849  11.561  46.228 1    18.643  ? 248  HIS A C   1 1 
ATOM   1721 O  O   . HIS A 1 212 ? 10.516  12.749  46.189 1    21.215  ? 248  HIS A O   1 1 
ATOM   1722 C  CB  . HIS A 1 212 ? 9.8     9.85    44.729 1    16.945  ? 248  HIS A CB  1 1 
ATOM   1723 C  CG  . HIS A 1 212 ? 8.466   10.502  44.656 1    20.216  ? 248  HIS A CG  1 1 
ATOM   1724 N  ND1 . HIS A 1 212 ? 7.843   10.977  45.785 1    22.155  ? 248  HIS A ND1 1 1 
ATOM   1725 C  CD2 . HIS A 1 212 ? 7.645   10.765  43.619 1    21.187  ? 248  HIS A CD2 1 1 
ATOM   1726 C  CE1 . HIS A 1 212 ? 6.665   11.505  45.453 1    22.58   ? 248  HIS A CE1 1 1 
ATOM   1727 N  NE2 . HIS A 1 212 ? 6.547   11.429  44.116 1    21.899  ? 248  HIS A NE2 1 1 
ATOM   1728 N  N   . ALA A 1 213 ? 11.115  10.945  47.378 1    17.322  ? 249  ALA A N   1 1 
ATOM   1729 C  CA  . ALA A 1 213 ? 10.888  11.7    48.605 1    18.238  ? 249  ALA A CA  1 1 
ATOM   1730 C  C   . ALA A 1 213 ? 11.955  12.807  48.793 1    18.769  ? 249  ALA A C   1 1 
ATOM   1731 O  O   . ALA A 1 213 ? 11.669  13.905  49.357 1    18.565  ? 249  ALA A O   1 1 
ATOM   1732 C  CB  . ALA A 1 213 ? 10.824  10.717  49.813 1    15.804  ? 249  ALA A CB  1 1 
ATOM   1733 N  N   . TYR A 1 214 ? 13.214  12.505  48.414 1    19.435  ? 250  TYR A N   1 1 
ATOM   1734 C  CA  . TYR A 1 214 ? 14.273  13.49   48.599 1    19.51   ? 250  TYR A CA  1 1 
ATOM   1735 C  C   . TYR A 1 214 ? 14.066  14.684  47.642 1    18.724  ? 250  TYR A C   1 1 
ATOM   1736 O  O   . TYR A 1 214 ? 14.296  15.861  48     1    18.173  ? 250  TYR A O   1 1 
ATOM   1737 C  CB  . TYR A 1 214 ? 15.549  12.682  48.333 1    19.174  ? 250  TYR A CB  1 1 
ATOM   1738 C  CG  . TYR A 1 214 ? 16.756  13.617  48.22  1    23.583  ? 250  TYR A CG  1 1 
ATOM   1739 C  CD1 . TYR A 1 214 ? 17.3    14.234  49.327 1    27.006  ? 250  TYR A CD1 1 1 
ATOM   1740 C  CD2 . TYR A 1 214 ? 17.324  13.926  47     1    21.842  ? 250  TYR A CD2 1 1 
ATOM   1741 C  CE1 . TYR A 1 214 ? 18.39   15.092  49.23  1    27.566  ? 250  TYR A CE1 1 1 
ATOM   1742 C  CE2 . TYR A 1 214 ? 18.433  14.766  46.891 1    22.78   ? 250  TYR A CE2 1 1 
ATOM   1743 C  CZ  . TYR A 1 214 ? 18.934  15.412  47.995 1    26.424  ? 250  TYR A CZ  1 1 
ATOM   1744 O  OH  . TYR A 1 214 ? 20.011  16.287  47.883 1    26.832  ? 250  TYR A OH  1 1 
ATOM   1745 N  N   . VAL A 1 215 ? 13.699  14.365  46.371 1    19.222  ? 251  VAL A N   1 1 
ATOM   1746 C  CA  . VAL A 1 215 ? 13.333  15.369  45.394 1    18.53   ? 251  VAL A CA  1 1 
ATOM   1747 C  C   . VAL A 1 215 ? 12.182  16.249  45.932 1    21.171  ? 251  VAL A C   1 1 
ATOM   1748 O  O   . VAL A 1 215 ? 12.256  17.479  45.868 1    22.193  ? 251  VAL A O   1 1 
ATOM   1749 C  CB  . VAL A 1 215 ? 13.121  14.809  43.963 1    17.303  ? 251  VAL A CB  1 1 
ATOM   1750 C  CG1 . VAL A 1 215 ? 12.628  15.938  43.015 1    15.657  ? 251  VAL A CG1 1 1 
ATOM   1751 C  CG2 . VAL A 1 215 ? 14.494  14.402  43.502 1    16.699  ? 251  VAL A CG2 1 1 
ATOM   1752 N  N   . ARG A 1 216 ? 11.065  15.639  46.401 1    23.249  ? 252  ARG A N   1 1 
ATOM   1753 C  CA  . ARG A 1 216 ? 9.921   16.393  46.919 1    19.325  ? 252  ARG A CA  1 1 
ATOM   1754 C  C   . ARG A 1 216 ? 10.345  17.378  48.023 1    23.874  ? 252  ARG A C   1 1 
ATOM   1755 O  O   . ARG A 1 216 ? 9.948   18.568  48.042 1    20.344  ? 252  ARG A O   1 1 
ATOM   1756 C  CB  . ARG A 1 216 ? 8.923   15.378  47.468 1    20.756  ? 252  ARG A CB  1 1 
ATOM   1757 C  CG  . ARG A 1 216 ? 7.568   15.962  47.881 1    21.464  ? 252  ARG A CG  1 1 
ATOM   1758 C  CD  . ARG A 1 216 ? 6.596   14.799  48.133 1    21.257  ? 252  ARG A CD  1 1 
ATOM   1759 N  NE  . ARG A 1 216 ? 7.08    13.994  49.263 1    20.82   ? 252  ARG A NE  1 1 
ATOM   1760 C  CZ  . ARG A 1 216 ? 6.654   12.712  49.466 1    22.55   ? 252  ARG A CZ  1 1 
ATOM   1761 N  NH1 . ARG A 1 216 ? 5.475   12.31   48.937 1    20.194  ? 252  ARG A NH1 1 1 
ATOM   1762 N  NH2 . ARG A 1 216 ? 7.369   11.92   50.285 1    20.056  ? 252  ARG A NH2 1 1 
ATOM   1763 N  N   . ARG A 1 217 ? 11.264  16.91   48.894 1    23.82   ? 253  ARG A N   1 1 
ATOM   1764 C  CA  . ARG A 1 217 ? 11.762  17.75   49.965 1    25.667  ? 253  ARG A CA  1 1 
ATOM   1765 C  C   . ARG A 1 217 ? 12.48   18.974  49.38  1    25.769  ? 253  ARG A C   1 1 
ATOM   1766 O  O   . ARG A 1 217 ? 12.227  20.115  49.81  1    26.634  ? 253  ARG A O   1 1 
ATOM   1767 C  CB  . ARG A 1 217 ? 12.658  16.939  50.918 1    22.93   ? 253  ARG A CB  1 1 
ATOM   1768 C  CG  . ARG A 1 217 ? 13.333  17.841  51.953 1    24.519  ? 253  ARG A CG  1 1 
ATOM   1769 C  CD  . ARG A 1 217 ? 12.505  18.463  53.039 1    24.859  ? 253  ARG A CD  1 1 
ATOM   1770 N  NE  . ARG A 1 217 ? 11.888  17.353  53.771 1    28.692  ? 253  ARG A NE  1 1 
ATOM   1771 C  CZ  . ARG A 1 217 ? 11.09   17.552  54.832 1    32.512  ? 253  ARG A CZ  1 1 
ATOM   1772 N  NH1 . ARG A 1 217 ? 10.484  16.52   55.405 1    29.995  ? 253  ARG A NH1 1 1 
ATOM   1773 N  NH2 . ARG A 1 217 ? 10.827  18.774  55.277 1    30.244  ? 253  ARG A NH2 1 1 
ATOM   1774 N  N   . ALA A 1 218 ? 13.357  18.724  48.386 1    22.7    ? 254  ALA A N   1 1 
ATOM   1775 C  CA  . ALA A 1 218 ? 14.104  19.807  47.777 1    26.15   ? 254  ALA A CA  1 1 
ATOM   1776 C  C   . ALA A 1 218 ? 13.139  20.764  47.061 1    24.106  ? 254  ALA A C   1 1 
ATOM   1777 O  O   . ALA A 1 218 ? 13.354  21.977  47.143 1    26.72   ? 254  ALA A O   1 1 
ATOM   1778 C  CB  . ALA A 1 218 ? 15.207  19.297  46.886 1    23.64   ? 254  ALA A CB  1 1 
ATOM   1779 N  N   . LEU A 1 219 ? 12.052  20.244  46.442 1    21.406  ? 255  LEU A N   1 1 
ATOM   1780 C  CA  . LEU A 1 219 ? 11.114  21.135  45.754 1    21.599  ? 255  LEU A CA  1 1 
ATOM   1781 C  C   . LEU A 1 219 ? 10.439  22.004  46.824 1    24.357  ? 255  LEU A C   1 1 
ATOM   1782 O  O   . LEU A 1 219 ? 10.093  23.183  46.621 1    24.62   ? 255  LEU A O   1 1 
ATOM   1783 C  CB  . LEU A 1 219 ? 10.111  20.342  44.915 1    19.794  ? 255  LEU A CB  1 1 
ATOM   1784 C  CG  . LEU A 1 219 ? 10.682  19.621  43.677 1    22.204  ? 255  LEU A CG  1 1 
ATOM   1785 C  CD1 . LEU A 1 219 ? 9.673   18.787  42.908 1    18.81   ? 255  LEU A CD1 1 1 
ATOM   1786 C  CD2 . LEU A 1 219 ? 11.279  20.698  42.802 1    21.476  ? 255  LEU A CD2 1 1 
ATOM   1787 N  N   . HIS A 1 220 ? 10.147  21.362  47.969 1    23.298  ? 256  HIS A N   1 1 
ATOM   1788 C  CA  . HIS A 1 220 ? 9.445   22.073  49.033 1    23.325  ? 256  HIS A CA  1 1 
ATOM   1789 C  C   . HIS A 1 220 ? 10.275  23.304  49.419 1    24.554  ? 256  HIS A C   1 1 
ATOM   1790 O  O   . HIS A 1 220 ? 9.74    24.413  49.644 1    24.003  ? 256  HIS A O   1 1 
ATOM   1791 C  CB  . HIS A 1 220 ? 9.202   21.059  50.162 1    23.697  ? 256  HIS A CB  1 1 
ATOM   1792 C  CG  . HIS A 1 220 ? 8.607   21.588  51.439 1    24.452  ? 256  HIS A CG  1 1 
ATOM   1793 N  ND1 . HIS A 1 220 ? 9.36    22.119  52.463 1    23.444  ? 256  HIS A ND1 1 1 
ATOM   1794 C  CD2 . HIS A 1 220 ? 7.289   21.629  51.849 1    21.825  ? 256  HIS A CD2 1 1 
ATOM   1795 C  CE1 . HIS A 1 220 ? 8.551   22.477  53.471 1    23.604  ? 256  HIS A CE1 1 1 
ATOM   1796 N  NE2 . HIS A 1 220 ? 7.296   22.185  53.098 1    23.82   ? 256  HIS A NE2 1 1 
ATOM   1797 N  N   . ARG A 1 221 ? 11.601  23.1    49.49  1    22.516  ? 257  ARG A N   1 1 
ATOM   1798 C  CA  . ARG A 1 221 ? 12.503  24.156  49.902 1    27.404  ? 257  ARG A CA  1 1 
ATOM   1799 C  C   . ARG A 1 221 ? 12.521  25.304  48.882 1    26.702  ? 257  ARG A C   1 1 
ATOM   1800 O  O   . ARG A 1 221 ? 12.537  26.463  49.253 1    27.109  ? 257  ARG A O   1 1 
ATOM   1801 C  CB  . ARG A 1 221 ? 13.803  23.38   50.127 1    30.765  ? 257  ARG A CB  1 1 
ATOM   1802 C  CG  . ARG A 1 221 ? 14.835  24.304  50.752 1    41.613  ? 257  ARG A CG  1 1 
ATOM   1803 C  CD  . ARG A 1 221 ? 15.943  23.419  51.343 1    50.368  ? 257  ARG A CD  1 1 
ATOM   1804 N  NE  . ARG A 1 221 ? 16.711  22.765  50.279 1    45.454  ? 257  ARG A NE  1 1 
ATOM   1805 C  CZ  . ARG A 1 221 ? 16.789  21.497  49.92  1    45.646  ? 257  ARG A CZ  1 1 
ATOM   1806 N  NH1 . ARG A 1 221 ? 16.239  20.514  50.627 1    43.094  ? 257  ARG A NH1 1 1 
ATOM   1807 N  NH2 . ARG A 1 221 ? 17.421  21.247  48.783 1    46.815  ? 257  ARG A NH2 1 1 
ATOM   1808 N  N   . HIS A 1 222 ? 12.5    24.987  47.582 1    25.683  ? 258  HIS A N   1 1 
ATOM   1809 C  CA  . HIS A 1 222 ? 12.584  25.968  46.506 1    25.199  ? 258  HIS A CA  1 1 
ATOM   1810 C  C   . HIS A 1 222 ? 11.211  26.6    46.237 1    26.371  ? 258  HIS A C   1 1 
ATOM   1811 O  O   . HIS A 1 222 ? 11.095  27.827  46.18  1    27.012  ? 258  HIS A O   1 1 
ATOM   1812 C  CB  . HIS A 1 222 ? 13.196  25.365  45.223 1    25.401  ? 258  HIS A CB  1 1 
ATOM   1813 C  CG  . HIS A 1 222 ? 13.203  26.457  44.227 1    32.29   ? 258  HIS A CG  1 1 
ATOM   1814 N  ND1 . HIS A 1 222 ? 14.225  27.389  44.19  1    34.341  ? 258  HIS A ND1 1 1 
ATOM   1815 C  CD2 . HIS A 1 222 ? 12.27   26.871  43.31  1    36.194  ? 258  HIS A CD2 1 1 
ATOM   1816 C  CE1 . HIS A 1 222 ? 13.932  28.339  43.28  1    37.349  ? 258  HIS A CE1 1 1 
ATOM   1817 N  NE2 . HIS A 1 222 ? 12.748  28.032  42.713 1    40.325  ? 258  HIS A NE2 1 1 
ATOM   1818 N  N   . TYR A 1 223 ? 10.156  25.79   46.108 1    24.03   ? 259  TYR A N   1 1 
ATOM   1819 C  CA  . TYR A 1 223 ? 8.884   26.313  45.639 1    24.007  ? 259  TYR A CA  1 1 
ATOM   1820 C  C   . TYR A 1 223 ? 7.942   26.663  46.781 1    27.661  ? 259  TYR A C   1 1 
ATOM   1821 O  O   . TYR A 1 223 ? 6.874   27.238  46.521 1    28.233  ? 259  TYR A O   1 1 
ATOM   1822 C  CB  . TYR A 1 223 ? 8.186   25.402  44.632 1    24.575  ? 259  TYR A CB  1 1 
ATOM   1823 C  CG  . TYR A 1 223 ? 8.934   25.336  43.3   1    25.011  ? 259  TYR A CG  1 1 
ATOM   1824 C  CD1 . TYR A 1 223 ? 8.774   26.383  42.366 1    26.745  ? 259  TYR A CD1 1 1 
ATOM   1825 C  CD2 . TYR A 1 223 ? 9.711   24.235  42.938 1    23.484  ? 259  TYR A CD2 1 1 
ATOM   1826 C  CE1 . TYR A 1 223 ? 9.343   26.299  41.1   1    25.956  ? 259  TYR A CE1 1 1 
ATOM   1827 C  CE2 . TYR A 1 223 ? 10.351  24.174  41.696 1    25.088  ? 259  TYR A CE2 1 1 
ATOM   1828 C  CZ  . TYR A 1 223 ? 10.215  25.265  40.813 1    26.957  ? 259  TYR A CZ  1 1 
ATOM   1829 O  OH  . TYR A 1 223 ? 10.828  25.342  39.618 1    23.821  ? 259  TYR A OH  1 1 
ATOM   1830 N  N   . GLY A 1 224 ? 8.332   26.321  48.031 1    27.486  ? 260  GLY A N   1 1 
ATOM   1831 C  CA  . GLY A 1 224 ? 7.516   26.734  49.167 1    26.282  ? 260  GLY A CA  1 1 
ATOM   1832 C  C   . GLY A 1 224 ? 6.515   25.692  49.685 1    23.476  ? 260  GLY A C   1 1 
ATOM   1833 O  O   . GLY A 1 224 ? 5.93    24.927  48.942 1    19.378  ? 260  GLY A O   1 1 
ATOM   1834 N  N   . ALA A 1 225 ? 6.324   25.734  51.018 1    25.339  ? 261  ALA A N   1 1 
ATOM   1835 C  CA  . ALA A 1 225 ? 5.462   24.867  51.829 1    23.81   ? 261  ALA A CA  1 1 
ATOM   1836 C  C   . ALA A 1 225 ? 4.035   24.879  51.271 1    24.193  ? 261  ALA A C   1 1 
ATOM   1837 O  O   . ALA A 1 225 ? 3.365   23.864  51.21  1    24.168  ? 261  ALA A O   1 1 
ATOM   1838 C  CB  . ALA A 1 225 ? 5.549   25.292  53.331 1    23.848  ? 261  ALA A CB  1 1 
ATOM   1839 N  N   . GLN A 1 226 ? 3.544   26.015  50.809 1    25.12   ? 262  GLN A N   1 1 
ATOM   1840 C  CA  . GLN A 1 226 ? 2.177   25.959  50.331 1    27.893  ? 262  GLN A CA  1 1 
ATOM   1841 C  C   . GLN A 1 226 ? 2.027   25.257  48.993 1    27.93   ? 262  GLN A C   1 1 
ATOM   1842 O  O   . GLN A 1 226 ? 0.897   24.992  48.614 1    29.501  ? 262  GLN A O   1 1 
ATOM   1843 C  CB  . GLN A 1 226 ? 1.617   27.363  50.163 1    30.248  ? 262  GLN A CB  1 1 
ATOM   1844 C  CG  . GLN A 1 226 ? 1.633   28.191  51.448 1    31.727  ? 262  GLN A CG  1 1 
ATOM   1845 C  CD  . GLN A 1 226 ? 0.481   27.863  52.373 1    35.467  ? 262  GLN A CD  1 1 
ATOM   1846 O  OE1 . GLN A 1 226 ? -0.298  26.931  52.139 1    32.322  ? 262  GLN A OE1 1 1 
ATOM   1847 N  NE2 . GLN A 1 226 ? 0.396   28.634  53.454 1    38.198  ? 262  GLN A NE2 1 1 
ATOM   1848 N  N   . HIS A 1 227 ? 3.114   25.025  48.245 1    27.535  ? 263  HIS A N   1 1 
ATOM   1849 C  CA  . HIS A 1 227 ? 2.909   24.405  46.926 1    25.839  ? 263  HIS A CA  1 1 
ATOM   1850 C  C   . HIS A 1 227 ? 3.43    22.974  46.849 1    24.577  ? 263  HIS A C   1 1 
ATOM   1851 O  O   . HIS A 1 227 ? 3.331   22.427  45.771 1    24.755  ? 263  HIS A O   1 1 
ATOM   1852 C  CB  . HIS A 1 227 ? 3.59    25.169  45.785 1    27.047  ? 263  HIS A CB  1 1 
ATOM   1853 C  CG  . HIS A 1 227 ? 3.086   26.577  45.779 1    34.475  ? 263  HIS A CG  1 1 
ATOM   1854 N  ND1 . HIS A 1 227 ? 1.893   26.97   45.199 1    39.332  ? 263  HIS A ND1 1 1 
ATOM   1855 C  CD2 . HIS A 1 227 ? 3.568   27.65   46.421 1    33.465  ? 263  HIS A CD2 1 1 
ATOM   1856 C  CE1 . HIS A 1 227 ? 1.692   28.257  45.461 1    37.434  ? 263  HIS A CE1 1 1 
ATOM   1857 N  NE2 . HIS A 1 227 ? 2.7     28.68   46.218 1    38.71   ? 263  HIS A NE2 1 1 
ATOM   1858 N  N   . ILE A 1 228 ? 3.971   22.397  47.962 1    22.512  ? 264  ILE A N   1 1 
ATOM   1859 C  CA  . ILE A 1 228 ? 4.491   21.023  47.979 1    21.585  ? 264  ILE A CA  1 1 
ATOM   1860 C  C   . ILE A 1 228 ? 3.938   20.305  49.197 1    23.916  ? 264  ILE A C   1 1 
ATOM   1861 O  O   . ILE A 1 228 ? 4.236   20.676  50.335 1    27.417  ? 264  ILE A O   1 1 
ATOM   1862 C  CB  . ILE A 1 228 ? 6.036   20.984  47.974 1    22.193  ? 264  ILE A CB  1 1 
ATOM   1863 C  CG1 . ILE A 1 228 ? 6.552   21.606  46.662 1    26.891  ? 264  ILE A CG1 1 1 
ATOM   1864 C  CG2 . ILE A 1 228 ? 6.541   19.549  48.12  1    21.236  ? 264  ILE A CG2 1 1 
ATOM   1865 C  CD1 . ILE A 1 228 ? 6.003   20.87   45.443 1    25.522  ? 264  ILE A CD1 1 1 
ATOM   1866 N  N   . ASN A 1 229 ? 3.122   19.289  48.98  1    25.615  ? 265  ASN A N   1 1 
ATOM   1867 C  CA  . ASN A 1 229 ? 2.686   18.501  50.132 1    27.116  ? 265  ASN A CA  1 1 
ATOM   1868 C  C   . ASN A 1 229 ? 3.732   17.421  50.469 1    22.883  ? 265  ASN A C   1 1 
ATOM   1869 O  O   . ASN A 1 229 ? 4.04    16.62   49.588 1    22.535  ? 265  ASN A O   1 1 
ATOM   1870 C  CB  . ASN A 1 229 ? 1.378   17.811  49.786 1    27.748  ? 265  ASN A CB  1 1 
ATOM   1871 C  CG  . ASN A 1 229 ? 0.856   17.029  50.971 1    33.391  ? 265  ASN A CG  1 1 
ATOM   1872 O  OD1 . ASN A 1 229 ? 1.559   16.796  51.957 1    28.256  ? 265  ASN A OD1 1 1 
ATOM   1873 N  ND2 . ASN A 1 229 ? -0.342  16.503  50.83  1    40.232  ? 265  ASN A ND2 1 1 
ATOM   1874 N  N   . LEU A 1 230 ? 4.315   17.381  51.688 1    20.677  ? 266  LEU A N   1 1 
ATOM   1875 C  CA  . LEU A 1 230 ? 5.502   16.548  51.93  1    20.573  ? 266  LEU A CA  1 1 
ATOM   1876 C  C   . LEU A 1 230 ? 5.099   15.082  52.051 1    22.451  ? 266  LEU A C   1 1 
ATOM   1877 O  O   . LEU A 1 230 ? 5.996   14.257  52.093 1    22.928  ? 266  LEU A O   1 1 
ATOM   1878 C  CB  . LEU A 1 230 ? 6.304   16.951  53.163 1    22.143  ? 266  LEU A CB  1 1 
ATOM   1879 C  CG  . LEU A 1 230 ? 7.186   18.195  52.988 1    23.451  ? 266  LEU A CG  1 1 
ATOM   1880 C  CD1 . LEU A 1 230 ? 7.546   18.798  54.392 1    25      ? 266  LEU A CD1 1 1 
ATOM   1881 C  CD2 . LEU A 1 230 ? 8.402   17.772  52.104 1    23.171  ? 266  LEU A CD2 1 1 
ATOM   1882 N  N   . GLU A 1 231 ? 3.774   14.811  52.035 1    21.676  ? 267  GLU A N   1 1 
ATOM   1883 C  CA  . GLU A 1 231 ? 3.206   13.475  52.037 1    26.146  ? 267  GLU A CA  1 1 
ATOM   1884 C  C   . GLU A 1 231 ? 2.402   13.165  50.785 1    25.639  ? 267  GLU A C   1 1 
ATOM   1885 O  O   . GLU A 1 231 ? 1.633   12.192  50.765 1    28.5    ? 267  GLU A O   1 1 
ATOM   1886 C  CB  . GLU A 1 231 ? 2.313   13.276  53.267 1    24.522  ? 267  GLU A CB  1 1 
ATOM   1887 C  CG  . GLU A 1 231 ? 3.193   13.233  54.502 1    32.949  ? 267  GLU A CG  1 1 
ATOM   1888 C  CD  . GLU A 1 231 ? 2.42    12.984  55.805 1    46.217  ? 267  GLU A CD  1 1 
ATOM   1889 O  OE1 . GLU A 1 231 ? 2.99    12.292  56.671 1    55.438  ? 267  GLU A OE1 1 1 
ATOM   1890 O  OE2 . GLU A 1 231 ? 1.277   13.458  55.988 1    52.384  ? 267  GLU A OE2 1 1 
ATOM   1891 N  N   . GLY A 1 232 ? 2.459   14.042  49.788 1    22.368  ? 268  GLY A N   1 1 
ATOM   1892 C  CA  . GLY A 1 232 ? 1.574   13.81   48.658 1    20.513  ? 268  GLY A CA  1 1 
ATOM   1893 C  C   . GLY A 1 232 ? 2.316   13.678  47.327 1    20.669  ? 268  GLY A C   1 1 
ATOM   1894 O  O   . GLY A 1 232 ? 3.541   13.731  47.248 1    20.834  ? 268  GLY A O   1 1 
ATOM   1895 N  N   . PRO A 1 233 ? 1.584   13.608  46.203 1    18.587  ? 269  PRO A N   1 1 
ATOM   1896 C  CA  . PRO A 1 233 ? 2.247   13.545  44.887 1    19.926  ? 269  PRO A CA  1 1 
ATOM   1897 C  C   . PRO A 1 233 ? 2.968   14.852  44.55  1    21.293  ? 269  PRO A C   1 1 
ATOM   1898 O  O   . PRO A 1 233 ? 2.564   15.89   45.042 1    21.631  ? 269  PRO A O   1 1 
ATOM   1899 C  CB  . PRO A 1 233 ? 1.083   13.245  43.934 1    20.706  ? 269  PRO A CB  1 1 
ATOM   1900 C  CG  . PRO A 1 233 ? -0.166  13.636  44.654 1    19.632  ? 269  PRO A CG  1 1 
ATOM   1901 C  CD  . PRO A 1 233 ? 0.127   13.696  46.175 1    19.433  ? 269  PRO A CD  1 1 
ATOM   1902 N  N   . ILE A 1 234 ? 4.031   14.827  43.732 1    19.55   ? 270  ILE A N   1 1 
ATOM   1903 C  CA  . ILE A 1 234 ? 4.697   16.041  43.272 1    19.259  ? 270  ILE A CA  1 1 
ATOM   1904 C  C   . ILE A 1 234 ? 3.959   16.666  42.078 1    20.319  ? 270  ILE A C   1 1 
ATOM   1905 O  O   . ILE A 1 234 ? 3.553   15.945  41.182 1    19.04   ? 270  ILE A O   1 1 
ATOM   1906 C  CB  . ILE A 1 234 ? 6.119   15.649  42.85  1    22.248  ? 270  ILE A CB  1 1 
ATOM   1907 C  CG1 . ILE A 1 234 ? 6.841   14.882  44.025 1    24.192  ? 270  ILE A CG1 1 1 
ATOM   1908 C  CG2 . ILE A 1 234 ? 6.883   16.871  42.326 1    23.567  ? 270  ILE A CG2 1 1 
ATOM   1909 C  CD1 . ILE A 1 234 ? 8.277   14.475  43.732 1    19.908  ? 270  ILE A CD1 1 1 
ATOM   1910 N  N   . PRO A 1 235 ? 3.781   18.008  41.975 1    18.433  ? 271  PRO A N   1 1 
ATOM   1911 C  CA  . PRO A 1 235 ? 3.21    18.554  40.759 1    18.704  ? 271  PRO A CA  1 1 
ATOM   1912 C  C   . PRO A 1 235 ? 4.07    18.265  39.519 1    18.001  ? 271  PRO A C   1 1 
ATOM   1913 O  O   . PRO A 1 235 ? 5.291   18.445  39.569 1    16.831  ? 271  PRO A O   1 1 
ATOM   1914 C  CB  . PRO A 1 235 ? 3.028   20.046  41.078 1    17.751  ? 271  PRO A CB  1 1 
ATOM   1915 C  CG  . PRO A 1 235 ? 3.059   20.108  42.632 1    18.49   ? 271  PRO A CG  1 1 
ATOM   1916 C  CD  . PRO A 1 235 ? 4.014   19.017  43.034 1    18.306  ? 271  PRO A CD  1 1 
ATOM   1917 N  N   . ALA A 1 236 ? 3.397   17.825  38.436 1    18.079  ? 272  ALA A N   1 1 
ATOM   1918 C  CA  . ALA A 1 236 ? 4.008   17.251  37.227 1    19.665  ? 272  ALA A CA  1 1 
ATOM   1919 C  C   . ALA A 1 236 ? 4.906   18.211  36.449 1    20.11   ? 272  ALA A C   1 1 
ATOM   1920 O  O   . ALA A 1 236 ? 5.605   17.766  35.549 1    20.898  ? 272  ALA A O   1 1 
ATOM   1921 C  CB  . ALA A 1 236 ? 2.956   16.67   36.298 1    17.003  ? 272  ALA A CB  1 1 
ATOM   1922 N  N   . HIS A 1 237 ? 4.837   19.526  36.731 1    23.66   ? 273  HIS A N   1 1 
ATOM   1923 C  CA  . HIS A 1 237 ? 5.509   20.523  35.898 1    21.988  ? 273  HIS A CA  1 1 
ATOM   1924 C  C   . HIS A 1 237 ? 6.849   20.952  36.497 1    23.606  ? 273  HIS A C   1 1 
ATOM   1925 O  O   . HIS A 1 237 ? 7.524   21.845  35.953 1    22.717  ? 273  HIS A O   1 1 
ATOM   1926 C  CB  . HIS A 1 237 ? 4.566   21.694  35.68  1    21.211  ? 273  HIS A CB  1 1 
ATOM   1927 C  CG  . HIS A 1 237 ? 4.246   22.477  36.944 1    24.903  ? 273  HIS A CG  1 1 
ATOM   1928 N  ND1 . HIS A 1 237 ? 3.921   21.938  38.176 1    22.225  ? 273  HIS A ND1 1 1 
ATOM   1929 C  CD2 . HIS A 1 237 ? 4.171   23.798  37.095 1    21.723  ? 273  HIS A CD2 1 1 
ATOM   1930 C  CE1 . HIS A 1 237 ? 3.657   22.925  39.027 1    23.744  ? 273  HIS A CE1 1 1 
ATOM   1931 N  NE2 . HIS A 1 237 ? 3.786   24.056  38.393 1    23.353  ? 273  HIS A NE2 1 1 
ATOM   1932 N  N   . LEU A 1 238 ? 7.27    20.327  37.598 1    20.135  ? 274  LEU A N   1 1 
ATOM   1933 C  CA  . LEU A 1 238 ? 8.381   20.907  38.373 1    20.411  ? 274  LEU A CA  1 1 
ATOM   1934 C  C   . LEU A 1 238 ? 9.7     20.124  38.245 1    20.614  ? 274  LEU A C   1 1 
ATOM   1935 O  O   . LEU A 1 238 ? 10.664  20.424  38.954 1    22.182  ? 274  LEU A O   1 1 
ATOM   1936 C  CB  . LEU A 1 238 ? 7.996   20.976  39.847 1    18.293  ? 274  LEU A CB  1 1 
ATOM   1937 C  CG  . LEU A 1 238 ? 6.834   21.901  40.185 1    19.766  ? 274  LEU A CG  1 1 
ATOM   1938 C  CD1 . LEU A 1 238 ? 6.675   21.858  41.721 1    20.318  ? 274  LEU A CD1 1 1 
ATOM   1939 C  CD2 . LEU A 1 238 ? 7.167   23.335  39.675 1    18.384  ? 274  LEU A CD2 1 1 
ATOM   1940 N  N   . LEU A 1 239 ? 9.759   19.168  37.322 1    20.567  ? 275  LEU A N   1 1 
ATOM   1941 C  CA  . LEU A 1 239 ? 10.845  18.21   37.28  1    25.364  ? 275  LEU A CA  1 1 
ATOM   1942 C  C   . LEU A 1 239 ? 11.859  18.468  36.16  1    24.279  ? 275  LEU A C   1 1 
ATOM   1943 O  O   . LEU A 1 239 ? 12.687  17.585  35.945 1    21.369  ? 275  LEU A O   1 1 
ATOM   1944 C  CB  . LEU A 1 239 ? 10.263  16.802  37.134 1    22.975  ? 275  LEU A CB  1 1 
ATOM   1945 C  CG  . LEU A 1 239 ? 9.681   16.138  38.4   1    28.924  ? 275  LEU A CG  1 1 
ATOM   1946 C  CD1 . LEU A 1 239 ? 10.488  16.511  39.664 1    23.828  ? 275  LEU A CD1 1 1 
ATOM   1947 C  CD2 . LEU A 1 239 ? 8.222   16.533  38.562 1    25.835  ? 275  LEU A CD2 1 1 
ATOM   1948 N  N   . GLY A 1 240 ? 11.774  19.621  35.458 1    21.766  ? 276  GLY A N   1 1 
ATOM   1949 C  CA  . GLY A 1 240 ? 12.711  20.056  34.414 1    22.86   ? 276  GLY A CA  1 1 
ATOM   1950 C  C   . GLY A 1 240 ? 12.446  19.438  33.009 1    23.683  ? 276  GLY A C   1 1 
ATOM   1951 O  O   . GLY A 1 240 ? 13.251  19.642  32.084 1    20.828  ? 276  GLY A O   1 1 
ATOM   1952 N  N   . ASN A 1 241 ? 11.379  18.63   32.847 1    21.116  ? 277  ASN A N   1 1 
ATOM   1953 C  CA  . ASN A 1 241 ? 11.113  17.876  31.615 1    18.404  ? 277  ASN A CA  1 1 
ATOM   1954 C  C   . ASN A 1 241 ? 9.596   17.975  31.369 1    18.504  ? 277  ASN A C   1 1 
ATOM   1955 O  O   . ASN A 1 241 ? 8.822   17.92   32.316 1    15.847  ? 277  ASN A O   1 1 
ATOM   1956 C  CB  . ASN A 1 241 ? 11.628  16.436  31.726 1    17.154  ? 277  ASN A CB  1 1 
ATOM   1957 C  CG  . ASN A 1 241 ? 11.192  15.535  30.588 1    18.795  ? 277  ASN A CG  1 1 
ATOM   1958 O  OD1 . ASN A 1 241 ? 10.038  15.063  30.559 1    20.535  ? 277  ASN A OD1 1 1 
ATOM   1959 N  ND2 . ASN A 1 241 ? 12.047  15.391  29.569 1    17.251  ? 277  ASN A ND2 1 1 
ATOM   1960 N  N   . MET A 1 242 ? 9.159   18.087  30.091 1    17.263  ? 278  MET A N   1 1 
ATOM   1961 C  CA  . MET A 1 242 ? 7.764   18.25   29.734 1    18.968  ? 278  MET A CA  1 1 
ATOM   1962 C  C   . MET A 1 242 ? 6.904   17.123  30.302 1    18.457  ? 278  MET A C   1 1 
ATOM   1963 O  O   . MET A 1 242 ? 5.741   17.361  30.642 1    20.862  ? 278  MET A O   1 1 
ATOM   1964 C  CB  . MET A 1 242 ? 7.599   18.385  28.212 1    19.933  ? 278  MET A CB  1 1 
ATOM   1965 C  CG  . MET A 1 242 ? 6.132   18.74   27.776 1    21.958  ? 278  MET A CG  1 1 
ATOM   1966 S  SD  . MET A 1 242 ? 5.447   20.255  28.51  1    23.774  ? 278  MET A SD  1 1 
ATOM   1967 C  CE  . MET A 1 242 ? 6.026   21.431  27.287 1    25.939  ? 278  MET A CE  1 1 
ATOM   1968 N  N   . TRP A 1 243 ? 7.428   15.891  30.345 1    16.388  ? 279  TRP A N   1 1 
ATOM   1969 C  CA  . TRP A 1 243 ? 6.608   14.759  30.752 1    18.038  ? 279  TRP A CA  1 1 
ATOM   1970 C  C   . TRP A 1 243 ? 7.012   14.287  32.148 1    19.942  ? 279  TRP A C   1 1 
ATOM   1971 O  O   . TRP A 1 243 ? 6.503   13.253  32.619 1    19.28   ? 279  TRP A O   1 1 
ATOM   1972 C  CB  . TRP A 1 243 ? 6.703   13.58   29.758 1    19.113  ? 279  TRP A CB  1 1 
ATOM   1973 C  CG  . TRP A 1 243 ? 6.348   14.123  28.41  1    18.231  ? 279  TRP A CG  1 1 
ATOM   1974 C  CD1 . TRP A 1 243 ? 5.075   14.348  28.016 1    19.16   ? 279  TRP A CD1 1 1 
ATOM   1975 C  CD2 . TRP A 1 243 ? 7.215   14.754  27.446 1    20.65   ? 279  TRP A CD2 1 1 
ATOM   1976 N  NE1 . TRP A 1 243 ? 5.083   14.993  26.796 1    21.656  ? 279  TRP A NE1 1 1 
ATOM   1977 C  CE2 . TRP A 1 243 ? 6.381   15.269  26.436 1    21.682  ? 279  TRP A CE2 1 1 
ATOM   1978 C  CE3 . TRP A 1 243 ? 8.61    14.936  27.326 1    27.675  ? 279  TRP A CE3 1 1 
ATOM   1979 C  CZ2 . TRP A 1 243 ? 6.889   15.904  25.308 1    21.314  ? 279  TRP A CZ2 1 1 
ATOM   1980 C  CZ3 . TRP A 1 243 ? 9.128   15.543  26.189 1    24.917  ? 279  TRP A CZ3 1 1 
ATOM   1981 C  CH2 . TRP A 1 243 ? 8.261   16.014  25.195 1    24.092  ? 279  TRP A CH2 1 1 
ATOM   1982 N  N   . ALA A 1 244 ? 7.86    15.092  32.814 1    18.149  ? 280  ALA A N   1 1 
ATOM   1983 C  CA  . ALA A 1 244 ? 8.518   14.64   34.044 1    21.175  ? 280  ALA A CA  1 1 
ATOM   1984 C  C   . ALA A 1 244 ? 9.07    13.226  33.905 1    21.796  ? 280  ALA A C   1 1 
ATOM   1985 O  O   . ALA A 1 244 ? 9.08    12.495  34.884 1    20.988  ? 280  ALA A O   1 1 
ATOM   1986 C  CB  . ALA A 1 244 ? 7.595   14.723  35.293 1    18.031  ? 280  ALA A CB  1 1 
ATOM   1987 N  N   . GLN A 1 245 ? 9.61    12.868  32.735 1    22.336  ? 281  GLN A N   1 1 
ATOM   1988 C  CA  . GLN A 1 245 ? 9.983   11.48   32.531 1    22.684  ? 281  GLN A CA  1 1 
ATOM   1989 C  C   . GLN A 1 245 ? 11.448  11.344  32.935 1    23.17   ? 281  GLN A C   1 1 
ATOM   1990 O  O   . GLN A 1 245 ? 11.847  10.255  33.25  1    22.966  ? 281  GLN A O   1 1 
ATOM   1991 C  CB  . GLN A 1 245 ? 9.785   10.925  31.11  1    20.531  ? 281  GLN A CB  1 1 
ATOM   1992 C  CG  . GLN A 1 245 ? 10.796  11.515  30.125 1    22.799  ? 281  GLN A CG  1 1 
ATOM   1993 C  CD  . GLN A 1 245 ? 10.471  11.283  28.659 1    28.135  ? 281  GLN A CD  1 1 
ATOM   1994 O  OE1 . GLN A 1 245 ? 9.345   11.526  28.221 1    28.713  ? 281  GLN A OE1 1 1 
ATOM   1995 N  NE2 . GLN A 1 245 ? 11.423  10.858  27.849 1    25.054  ? 281  GLN A NE2 1 1 
ATOM   1996 N  N   . THR A 1 246 ? 12.226  12.43   32.935 1    21.676  ? 282  THR A N   1 1 
ATOM   1997 C  CA  . THR A 1 246 ? 13.598  12.416  33.439 1    22.46   ? 282  THR A CA  1 1 
ATOM   1998 C  C   . THR A 1 246 ? 13.798  13.73   34.175 1    22.442  ? 282  THR A C   1 1 
ATOM   1999 O  O   . THR A 1 246 ? 13.144  14.717  33.87  1    20.916  ? 282  THR A O   1 1 
ATOM   2000 C  CB  . THR A 1 246 ? 14.7    12.132  32.395 1    29.862  ? 282  THR A CB  1 1 
ATOM   2001 O  OG1 . THR A 1 246 ? 14.511  13.14   31.423 1    32.249  ? 282  THR A OG1 1 1 
ATOM   2002 C  CG2 . THR A 1 246 ? 14.643  10.737  31.777 1    27.92   ? 282  THR A CG2 1 1 
ATOM   2003 N  N   . TRP A 1 247 ? 14.498  13.646  35.306 1    21.778  ? 283  TRP A N   1 1 
ATOM   2004 C  CA  . TRP A 1 247 ? 14.546  14.762  36.234 1    22.212  ? 283  TRP A CA  1 1 
ATOM   2005 C  C   . TRP A 1 247 ? 15.924  15.431  36.261 1    23.881  ? 283  TRP A C   1 1 
ATOM   2006 O  O   . TRP A 1 247 ? 16.145  16.32   37.084 1    23.921  ? 283  TRP A O   1 1 
ATOM   2007 C  CB  . TRP A 1 247 ? 14.167  14.298  37.644 1    19.601  ? 283  TRP A CB  1 1 
ATOM   2008 C  CG  . TRP A 1 247 ? 12.813  13.665  37.739 1    19.056  ? 283  TRP A CG  1 1 
ATOM   2009 C  CD1 . TRP A 1 247 ? 11.8    13.557  36.829 1    19.727  ? 283  TRP A CD1 1 1 
ATOM   2010 C  CD2 . TRP A 1 247 ? 12.329  13.08   38.946 1    16.995  ? 283  TRP A CD2 1 1 
ATOM   2011 N  NE1 . TRP A 1 247 ? 10.73   12.907  37.372 1    17.134  ? 283  TRP A NE1 1 1 
ATOM   2012 C  CE2 . TRP A 1 247 ? 11.019  12.641  38.689 1    16.205  ? 283  TRP A CE2 1 1 
ATOM   2013 C  CE3 . TRP A 1 247 ? 12.914  12.928  40.219 1    18.988  ? 283  TRP A CE3 1 1 
ATOM   2014 C  CZ2 . TRP A 1 247 ? 10.24   12.032  39.664 1    16.159  ? 283  TRP A CZ2 1 1 
ATOM   2015 C  CZ3 . TRP A 1 247 ? 12.136  12.299  41.161 1    18.515  ? 283  TRP A CZ3 1 1 
ATOM   2016 C  CH2 . TRP A 1 247 ? 10.817  11.921  40.912 1    17.822  ? 283  TRP A CH2 1 1 
ATOM   2017 N  N   . SER A 1 248 ? 16.839  15.107  35.333 1    24.419  ? 284  SER A N   1 1 
ATOM   2018 C  CA  . SER A 1 248 ? 18.194  15.632  35.517 1    27.555  ? 284  SER A CA  1 1 
ATOM   2019 C  C   . SER A 1 248 ? 18.273  17.16   35.359 1    24.576  ? 284  SER A C   1 1 
ATOM   2020 O  O   . SER A 1 248 ? 19.212  17.738  35.901 1    25.04   ? 284  SER A O   1 1 
ATOM   2021 C  CB  . SER A 1 248 ? 19.197  14.93   34.639 1    31.457  ? 284  SER A CB  1 1 
ATOM   2022 O  OG  . SER A 1 248 ? 18.693  15.112  33.327 1    33.433  ? 284  SER A OG  1 1 
ATOM   2023 N  N   . ASN A 1 249 ? 17.244  17.835  34.771 1    22.431  ? 285  ASN A N   1 1 
ATOM   2024 C  CA  . ASN A 1 249 ? 17.342  19.288  34.671 1    22.112  ? 285  ASN A CA  1 1 
ATOM   2025 C  C   . ASN A 1 249 ? 17.174  20.024  35.982 1    21.582  ? 285  ASN A C   1 1 
ATOM   2026 O  O   . ASN A 1 249 ? 17.503  21.182  35.995 1    21.906  ? 285  ASN A O   1 1 
ATOM   2027 C  CB  . ASN A 1 249 ? 16.475  19.922  33.591 1    25.932  ? 285  ASN A CB  1 1 
ATOM   2028 C  CG  . ASN A 1 249 ? 16.996  19.481  32.238 1    31.829  ? 285  ASN A CG  1 1 
ATOM   2029 O  OD1 . ASN A 1 249 ? 18.198  19.595  32.002 1    28.566  ? 285  ASN A OD1 1 1 
ATOM   2030 N  ND2 . ASN A 1 249 ? 16.164  18.935  31.366 1    28.239  ? 285  ASN A ND2 1 1 
ATOM   2031 N  N   . ILE A 1 250 ? 16.702  19.394  37.065 1    22.02   ? 286  ILE A N   1 1 
ATOM   2032 C  CA  . ILE A 1 250 ? 16.654  20.018  38.394 1    22.516  ? 286  ILE A CA  1 1 
ATOM   2033 C  C   . ILE A 1 250 ? 17.793  19.562  39.315 1    23.56   ? 286  ILE A C   1 1 
ATOM   2034 O  O   . ILE A 1 250 ? 17.758  19.79   40.515 1    22.897  ? 286  ILE A O   1 1 
ATOM   2035 C  CB  . ILE A 1 250 ? 15.272  19.805  39.041 1    22.28   ? 286  ILE A CB  1 1 
ATOM   2036 C  CG1 . ILE A 1 250 ? 14.992  18.344  39.226 1    25.42   ? 286  ILE A CG1 1 1 
ATOM   2037 C  CG2 . ILE A 1 250 ? 14.196  20.41   38.115 1    21.581  ? 286  ILE A CG2 1 1 
ATOM   2038 C  CD1 . ILE A 1 250 ? 13.957  18.07   40.29  1    33.963  ? 286  ILE A CD1 1 1 
ATOM   2039 N  N   . TYR A 1 251 ? 18.861  19.002  38.743 1    26.174  ? 287  TYR A N   1 1 
ATOM   2040 C  CA  . TYR A 1 251 ? 20.018  18.632  39.523 1    28.291  ? 287  TYR A CA  1 1 
ATOM   2041 C  C   . TYR A 1 251 ? 20.515  19.788  40.424 1    31.617  ? 287  TYR A C   1 1 
ATOM   2042 O  O   . TYR A 1 251 ? 20.907  19.579  41.583 1    30.005  ? 287  TYR A O   1 1 
ATOM   2043 C  CB  . TYR A 1 251 ? 21.099  18.099  38.569 1    30.868  ? 287  TYR A CB  1 1 
ATOM   2044 C  CG  . TYR A 1 251 ? 22.369  17.782  39.352 1    32.997  ? 287  TYR A CG  1 1 
ATOM   2045 C  CD1 . TYR A 1 251 ? 22.449  16.667  40.194 1    34.634  ? 287  TYR A CD1 1 1 
ATOM   2046 C  CD2 . TYR A 1 251 ? 23.453  18.656  39.335 1    34.122  ? 287  TYR A CD2 1 1 
ATOM   2047 C  CE1 . TYR A 1 251 ? 23.575  16.401  40.967 1    34.113  ? 287  TYR A CE1 1 1 
ATOM   2048 C  CE2 . TYR A 1 251 ? 24.583  18.406  40.092 1    36.345  ? 287  TYR A CE2 1 1 
ATOM   2049 C  CZ  . TYR A 1 251 ? 24.652  17.271  40.892 1    40.38   ? 287  TYR A CZ  1 1 
ATOM   2050 O  OH  . TYR A 1 251 ? 25.779  17.025  41.649 1    42.73   ? 287  TYR A OH  1 1 
ATOM   2051 N  N   . ASP A 1 252 ? 20.568  21.016  39.915 1    33.141  ? 288  ASP A N   1 1 
ATOM   2052 C  CA  . ASP A 1 252 ? 20.992  22.155  40.739 1    36.801  ? 288  ASP A CA  1 1 
ATOM   2053 C  C   . ASP A 1 252 ? 20.09   22.403  41.974 1    32.611  ? 288  ASP A C   1 1 
ATOM   2054 O  O   . ASP A 1 252 ? 20.582  22.909  42.968 1    33.748  ? 288  ASP A O   1 1 
ATOM   2055 C  CB  . ASP A 1 252 ? 21.053  23.416  39.894 1    43.081  ? 288  ASP A CB  1 1 
ATOM   2056 C  CG  . ASP A 1 252 ? 19.693  23.742  39.296 1    51.406  ? 288  ASP A CG  1 1 
ATOM   2057 O  OD1 . ASP A 1 252 ? 19.188  22.902  38.536 1    63.116  ? 288  ASP A OD1 1 1 
ATOM   2058 O  OD2 . ASP A 1 252 ? 19.102  24.781  39.655 1    60.324  ? 288  ASP A OD2 1 1 
ATOM   2059 N  N   . LEU A 1 253 ? 18.781  22.08   41.946 1    29.585  ? 289  LEU A N   1 1 
ATOM   2060 C  CA  . LEU A 1 253 ? 17.965  22.194  43.16  1    29.555  ? 289  LEU A CA  1 1 
ATOM   2061 C  C   . LEU A 1 253 ? 18.161  21.012  44.115 1    31.691  ? 289  LEU A C   1 1 
ATOM   2062 O  O   . LEU A 1 253 ? 17.627  21.102  45.212 1    33.444  ? 289  LEU A O   1 1 
ATOM   2063 C  CB  . LEU A 1 253 ? 16.467  22.169  42.863 1    26.132  ? 289  LEU A CB  1 1 
ATOM   2064 C  CG  . LEU A 1 253 ? 15.941  23.172  41.848 1    24.988  ? 289  LEU A CG  1 1 
ATOM   2065 C  CD1 . LEU A 1 253 ? 14.5    22.837  41.508 1    25.134  ? 289  LEU A CD1 1 1 
ATOM   2066 C  CD2 . LEU A 1 253 ? 16.124  24.639  42.38  1    27.856  ? 289  LEU A CD2 1 1 
ATOM   2067 N  N   . VAL A 1 254 ? 18.816  19.897  43.722 1    24.921  ? 290  VAL A N   1 1 
ATOM   2068 C  CA  . VAL A 1 254 ? 18.77   18.697  44.551 1    25.274  ? 290  VAL A CA  1 1 
ATOM   2069 C  C   . VAL A 1 254 ? 20.182  18.195  44.865 1    27.971  ? 290  VAL A C   1 1 
ATOM   2070 O  O   . VAL A 1 254 ? 20.3    17.076  45.35  1    31.106  ? 290  VAL A O   1 1 
ATOM   2071 C  CB  . VAL A 1 254 ? 17.957  17.51   43.961 1    21.664  ? 290  VAL A CB  1 1 
ATOM   2072 C  CG1 . VAL A 1 254 ? 16.509  17.91   43.661 1    22.338  ? 290  VAL A CG1 1 1 
ATOM   2073 C  CG2 . VAL A 1 254 ? 18.567  16.96   42.667 1    18.191  ? 290  VAL A CG2 1 1 
ATOM   2074 N  N   . VAL A 1 255 ? 21.245  18.936  44.532 1    29.287  ? 291  VAL A N   1 1 
ATOM   2075 C  CA  . VAL A 1 255 ? 22.621  18.428  44.645 1    32.117  ? 291  VAL A CA  1 1 
ATOM   2076 C  C   . VAL A 1 255 ? 22.854  17.852  46.046 1    30.932  ? 291  VAL A C   1 1 
ATOM   2077 O  O   . VAL A 1 255 ? 22.756  18.626  46.996 1    27.148  ? 291  VAL A O   1 1 
ATOM   2078 C  CB  . VAL A 1 255 ? 23.686  19.542  44.516 1    36.108  ? 291  VAL A CB  1 1 
ATOM   2079 C  CG1 . VAL A 1 255 ? 25.084  18.944  44.526 1    37.526  ? 291  VAL A CG1 1 1 
ATOM   2080 C  CG2 . VAL A 1 255 ? 23.52   20.411  43.293 1    35.842  ? 291  VAL A CG2 1 1 
ATOM   2081 N  N   . PRO A 1 256 ? 23.295  16.569  46.228 1    30.206  ? 292  PRO A N   1 1 
ATOM   2082 C  CA  . PRO A 1 256 ? 23.56   16.022  47.564 1    27.622  ? 292  PRO A CA  1 1 
ATOM   2083 C  C   . PRO A 1 256 ? 24.654  16.773  48.284 1    31.801  ? 292  PRO A C   1 1 
ATOM   2084 O  O   . PRO A 1 256 ? 24.536  17.063  49.475 1    34.01   ? 292  PRO A O   1 1 
ATOM   2085 C  CB  . PRO A 1 256 ? 23.827  14.49   47.407 1    25.555  ? 292  PRO A CB  1 1 
ATOM   2086 C  CG  . PRO A 1 256 ? 23.338  14.2    46.03  1    25.962  ? 292  PRO A CG  1 1 
ATOM   2087 C  CD  . PRO A 1 256 ? 23.336  15.513  45.21  1    25.971  ? 292  PRO A CD  1 1 
ATOM   2088 N  N   . PHE A 1 257 ? 25.728  17.078  47.569 1    33.312  ? 293  PHE A N   1 1 
ATOM   2089 C  CA  . PHE A 1 257 ? 26.842  17.766  48.221 1    36.759  ? 293  PHE A CA  1 1 
ATOM   2090 C  C   . PHE A 1 257 ? 27.178  19.062  47.479 1    38.362  ? 293  PHE A C   1 1 
ATOM   2091 O  O   . PHE A 1 257 ? 28.074  19.029  46.635 1    33.252  ? 293  PHE A O   1 1 
ATOM   2092 C  CB  . PHE A 1 257 ? 28.061  16.84   48.243 1    33.881  ? 293  PHE A CB  1 1 
ATOM   2093 C  CG  . PHE A 1 257 ? 27.878  15.718  49.249 1    35.91   ? 293  PHE A CG  1 1 
ATOM   2094 C  CD1 . PHE A 1 257 ? 28.015  15.971  50.615 1    35.502  ? 293  PHE A CD1 1 1 
ATOM   2095 C  CD2 . PHE A 1 257 ? 27.559  14.424  48.828 1    35.924  ? 293  PHE A CD2 1 1 
ATOM   2096 C  CE1 . PHE A 1 257 ? 27.858  14.949  51.531 1    35.258  ? 293  PHE A CE1 1 1 
ATOM   2097 C  CE2 . PHE A 1 257 ? 27.414  13.408  49.764 1    36.567  ? 293  PHE A CE2 1 1 
ATOM   2098 C  CZ  . PHE A 1 257 ? 27.579  13.664  51.109 1    31.884  ? 293  PHE A CZ  1 1 
ATOM   2099 N  N   . PRO A 1 258 ? 26.51   20.219  47.78  1    39.274  ? 294  PRO A N   1 1 
ATOM   2100 C  CA  . PRO A 1 258 ? 26.745  21.468  47.049 1    46.191  ? 294  PRO A CA  1 1 
ATOM   2101 C  C   . PRO A 1 258 ? 28.182  21.951  47.247 1    43.91   ? 294  PRO A C   1 1 
ATOM   2102 O  O   . PRO A 1 258 ? 28.666  22.741  46.448 1    42.747  ? 294  PRO A O   1 1 
ATOM   2103 C  CB  . PRO A 1 258 ? 25.702  22.508  47.56  1    45.697  ? 294  PRO A CB  1 1 
ATOM   2104 C  CG  . PRO A 1 258 ? 25.284  21.957  48.897 1    47.454  ? 294  PRO A CG  1 1 
ATOM   2105 C  CD  . PRO A 1 258 ? 25.517  20.412  48.845 1    43.81   ? 294  PRO A CD  1 1 
ATOM   2106 N  N   . SER A 1 259 ? 28.829  21.472  48.311 1    40.37   ? 295  SER A N   1 1 
ATOM   2107 C  CA  . SER A 1 259 ? 30.189  21.863  48.619 1    54.195  ? 295  SER A CA  1 1 
ATOM   2108 C  C   . SER A 1 259 ? 31.173  21.253  47.612 1    53.981  ? 295  SER A C   1 1 
ATOM   2109 O  O   . SER A 1 259 ? 32.302  21.707  47.52  1    52.149  ? 295  SER A O   1 1 
ATOM   2110 C  CB  . SER A 1 259 ? 30.553  21.46   50.054 1    59.461  ? 295  SER A CB  1 1 
ATOM   2111 O  OG  . SER A 1 259 ? 30.357  20.055  50.223 1    59.356  ? 295  SER A OG  1 1 
ATOM   2112 N  N   . ALA A 1 260 ? 30.783  20.174  46.92  1    48.481  ? 296  ALA A N   1 1 
ATOM   2113 C  CA  . ALA A 1 260 ? 31.628  19.522  45.935 1    47.592  ? 296  ALA A CA  1 1 
ATOM   2114 C  C   . ALA A 1 260 ? 31.073  19.828  44.549 1    54.695  ? 296  ALA A C   1 1 
ATOM   2115 O  O   . ALA A 1 260 ? 30.4    18.98   43.937 1    54.654  ? 296  ALA A O   1 1 
ATOM   2116 C  CB  . ALA A 1 260 ? 31.683  18.029  46.189 1    43.455  ? 296  ALA A CB  1 1 
ATOM   2117 N  N   . PRO A 1 261 ? 31.406  21.012  43.976 1    62.447  ? 297  PRO A N   1 1 
ATOM   2118 C  CA  . PRO A 1 261 ? 30.659  21.549  42.833 1    57.788  ? 297  PRO A CA  1 1 
ATOM   2119 C  C   . PRO A 1 261 ? 31.235  20.897  41.568 1    52.447  ? 297  PRO A C   1 1 
ATOM   2120 O  O   . PRO A 1 261 ? 32.354  20.377  41.58  1    46.016  ? 297  PRO A O   1 1 
ATOM   2121 C  CB  . PRO A 1 261 ? 30.956  23.076  42.964 1    61.34   ? 297  PRO A CB  1 1 
ATOM   2122 C  CG  . PRO A 1 261 ? 32.362  23.158  43.589 1    68.927  ? 297  PRO A CG  1 1 
ATOM   2123 C  CD  . PRO A 1 261 ? 32.619  21.805  44.271 1    66.761  ? 297  PRO A CD  1 1 
ATOM   2124 N  N   . SER A 1 262 ? 30.477  20.878  40.47  1    50.128  ? 298  SER A N   1 1 
ATOM   2125 C  CA  . SER A 1 262 ? 31.154  20.458  39.247 1    58.381  ? 298  SER A CA  1 1 
ATOM   2126 C  C   . SER A 1 262 ? 30.672  21.251  38.037 1    51.496  ? 298  SER A C   1 1 
ATOM   2127 O  O   . SER A 1 262 ? 29.652  21.921  38.087 1    48.139  ? 298  SER A O   1 1 
ATOM   2128 C  CB  . SER A 1 262 ? 31.143  18.934  39.013 1    63.504  ? 298  SER A CB  1 1 
ATOM   2129 O  OG  . SER A 1 262 ? 29.838  18.365  39.017 1    57.951  ? 298  SER A OG  1 1 
ATOM   2130 N  N   . MET A 1 263 ? 31.445  21.173  36.958 1    52.128  ? 299  MET A N   1 1 
ATOM   2131 C  CA  . MET A 1 263 ? 31.098  21.876  35.744 1    50.559  ? 299  MET A CA  1 1 
ATOM   2132 C  C   . MET A 1 263 ? 29.796  21.338  35.182 1    53.758  ? 299  MET A C   1 1 
ATOM   2133 O  O   . MET A 1 263 ? 29.423  20.18   35.398 1    64.75   ? 299  MET A O   1 1 
ATOM   2134 C  CB  . MET A 1 263 ? 32.247  21.757  34.76  1    45.749  ? 299  MET A CB  1 1 
ATOM   2135 C  CG  . MET A 1 263 ? 33.485  22.329  35.392 1    46.929  ? 299  MET A CG  1 1 
ATOM   2136 S  SD  . MET A 1 263 ? 34.802  22.125  34.195 1    52.321  ? 299  MET A SD  1 1 
ATOM   2137 C  CE  . MET A 1 263 ? 33.835  22.324  32.694 1    44.833  ? 299  MET A CE  1 1 
ATOM   2138 N  N   . ASP A 1 264 ? 29.059  22.213  34.507 1    54.054  ? 300  ASP A N   1 1 
ATOM   2139 C  CA  . ASP A 1 264 ? 27.929  21.694  33.764 1    48.784  ? 300  ASP A CA  1 1 
ATOM   2140 C  C   . ASP A 1 264 ? 28.461  21.258  32.386 1    48.533  ? 300  ASP A C   1 1 
ATOM   2141 O  O   . ASP A 1 264 ? 29.186  22.012  31.723 1    40.068  ? 300  ASP A O   1 1 
ATOM   2142 C  CB  . ASP A 1 264 ? 26.759  22.654  33.897 1    57.407  ? 300  ASP A CB  1 1 
ATOM   2143 C  CG  . ASP A 1 264 ? 25.679  22.501  32.84  1    66.338  ? 300  ASP A CG  1 1 
ATOM   2144 O  OD1 . ASP A 1 264 ? 24.845  21.567  32.982 1    64.701  ? 300  ASP A OD1 1 1 
ATOM   2145 O  OD2 . ASP A 1 264 ? 25.71   23.31   31.876 1    67.649  ? 300  ASP A OD2 1 1 
ATOM   2146 N  N   . THR A 1 265 ? 28.148  20.013  31.97  1    48.669  ? 301  THR A N   1 1 
ATOM   2147 C  CA  . THR A 1 265 ? 28.703  19.511  30.726 1    46.534  ? 301  THR A CA  1 1 
ATOM   2148 C  C   . THR A 1 265 ? 28.309  20.466  29.595 1    45.303  ? 301  THR A C   1 1 
ATOM   2149 O  O   . THR A 1 265 ? 29.172  20.937  28.842 1    40.88   ? 301  THR A O   1 1 
ATOM   2150 C  CB  . THR A 1 265 ? 28.156  18.103  30.521 1    54.893  ? 301  THR A CB  1 1 
ATOM   2151 O  OG1 . THR A 1 265 ? 28.257  17.42   31.768 1    56.719  ? 301  THR A OG1 1 1 
ATOM   2152 C  CG2 . THR A 1 265 ? 28.837  17.348  29.394 1    52.342  ? 301  THR A CG2 1 1 
ATOM   2153 N  N   . THR A 1 266 ? 26.991  20.782  29.548 1    48.969  ? 302  THR A N   1 1 
ATOM   2154 C  CA  . THR A 1 266 ? 26.335  21.6    28.524 1    46.35   ? 302  THR A CA  1 1 
ATOM   2155 C  C   . THR A 1 266 ? 27.035  22.943  28.355 1    46.367  ? 302  THR A C   1 1 
ATOM   2156 O  O   . THR A 1 266 ? 27.364  23.337  27.243 1    49.22   ? 302  THR A O   1 1 
ATOM   2157 C  CB  . THR A 1 266 ? 24.851  21.802  28.82  1    40.479  ? 302  THR A CB  1 1 
ATOM   2158 O  OG1 . THR A 1 266 ? 24.372  20.47   28.685 1    46.038  ? 302  THR A OG1 1 1 
ATOM   2159 C  CG2 . THR A 1 266 ? 24.194  22.756  27.834 1    43.509  ? 302  THR A CG2 1 1 
ATOM   2160 N  N   . GLU A 1 267 ? 27.267  23.625  29.481 1    49.55   ? 303  GLU A N   1 1 
ATOM   2161 C  CA  . GLU A 1 267 ? 27.979  24.888  29.5   1    53.251  ? 303  GLU A CA  1 1 
ATOM   2162 C  C   . GLU A 1 267 ? 29.402  24.727  28.966 1    50.694  ? 303  GLU A C   1 1 
ATOM   2163 O  O   . GLU A 1 267 ? 29.922  25.62   28.302 1    52.505  ? 303  GLU A O   1 1 
ATOM   2164 C  CB  . GLU A 1 267 ? 27.967  25.302  30.962 1    62.221  ? 303  GLU A CB  1 1 
ATOM   2165 C  CG  . GLU A 1 267 ? 27.826  26.807  31.133 1    77.494  ? 303  GLU A CG  1 1 
ATOM   2166 C  CD  . GLU A 1 267 ? 27.884  27.062  32.624 1    83.699  ? 303  GLU A CD  1 1 
ATOM   2167 O  OE1 . GLU A 1 267 ? 26.936  26.671  33.328 1    88.191  ? 303  GLU A OE1 1 1 
ATOM   2168 O  OE2 . GLU A 1 267 ? 28.908  27.598  33.082 1    83.209  ? 303  GLU A OE2 1 1 
ATOM   2169 N  N   . ALA A 1 268 ? 30.07   23.613  29.303 1    52.548  ? 304  ALA A N   1 1 
ATOM   2170 C  CA  . ALA A 1 268 ? 31.458  23.381  28.887 1    52.255  ? 304  ALA A CA  1 1 
ATOM   2171 C  C   . ALA A 1 268 ? 31.541  22.973  27.404 1    46.232  ? 304  ALA A C   1 1 
ATOM   2172 O  O   . ALA A 1 268 ? 32.541  23.267  26.744 1    40.684  ? 304  ALA A O   1 1 
ATOM   2173 C  CB  . ALA A 1 268 ? 32.097  22.34   29.803 1    46.881  ? 304  ALA A CB  1 1 
ATOM   2174 N  N   . MET A 1 269 ? 30.5    22.243  26.916 1    46.977  ? 305  MET A N   1 1 
ATOM   2175 C  CA  . MET A 1 269 ? 30.443  21.836  25.506 1    49.152  ? 305  MET A CA  1 1 
ATOM   2176 C  C   . MET A 1 269 ? 30.356  23.086  24.606 1    51.717  ? 305  MET A C   1 1 
ATOM   2177 O  O   . MET A 1 269 ? 31.171  23.232  23.671 1    50.458  ? 305  MET A O   1 1 
ATOM   2178 C  CB  . MET A 1 269 ? 29.298  20.847  25.2   1    41.962  ? 305  MET A CB  1 1 
ATOM   2179 C  CG  . MET A 1 269 ? 29.524  19.387  25.614 1    39.502  ? 305  MET A CG  1 1 
ATOM   2180 S  SD  . MET A 1 269 ? 27.92   18.593  25.715 1    42.057  ? 305  MET A SD  1 1 
ATOM   2181 C  CE  . MET A 1 269 ? 28.037  18.288  23.944 1    37.608  ? 305  MET A CE  1 1 
ATOM   2182 N  N   . LEU A 1 270 ? 29.344  23.963  24.89  1    52.031  ? 306  LEU A N   1 1 
ATOM   2183 C  CA  . LEU A 1 270 ? 29.191  25.305  24.296 1    47.809  ? 306  LEU A CA  1 1 
ATOM   2184 C  C   . LEU A 1 270 ? 30.54   26.015  24.41  1    48.984  ? 306  LEU A C   1 1 
ATOM   2185 O  O   . LEU A 1 270 ? 31.173  26.232  23.381 1    49.636  ? 306  LEU A O   1 1 
ATOM   2186 C  CB  . LEU A 1 270 ? 28.056  26.162  24.881 1    47.953  ? 306  LEU A CB  1 1 
ATOM   2187 C  CG  . LEU A 1 270 ? 26.591  25.795  24.558 1    47.289  ? 306  LEU A CG  1 1 
ATOM   2188 C  CD1 . LEU A 1 270 ? 25.62   26.436  25.578 1    41.705  ? 306  LEU A CD1 1 1 
ATOM   2189 C  CD2 . LEU A 1 270 ? 26.202  26.194  23.129 1    44.203  ? 306  LEU A CD2 1 1 
ATOM   2190 N  N   . LYS A 1 271 ? 31.021  26.225  25.661 1    46.415  ? 307  LYS A N   1 1 
ATOM   2191 C  CA  . LYS A 1 271 ? 32.285  26.902  25.913 1    51.565  ? 307  LYS A CA  1 1 
ATOM   2192 C  C   . LYS A 1 271 ? 33.406  26.393  25.007 1    51.675  ? 307  LYS A C   1 1 
ATOM   2193 O  O   . LYS A 1 271 ? 34.238  27.175  24.593 1    51.196  ? 307  LYS A O   1 1 
ATOM   2194 C  CB  . LYS A 1 271 ? 32.743  27.055  27.367 1    55.834  ? 307  LYS A CB  1 1 
ATOM   2195 C  CG  . LYS A 1 271 ? 33.427  28.432  27.503 1    65.295  ? 307  LYS A CG  1 1 
ATOM   2196 C  CD  . LYS A 1 271 ? 34.209  28.792  28.761 1    69.791  ? 307  LYS A CD  1 1 
ATOM   2197 C  CE  . LYS A 1 271 ? 34.708  30.231  28.815 1    76.184  ? 307  LYS A CE  1 1 
ATOM   2198 N  NZ  . LYS A 1 271 ? 35.5    30.432  30.04  1    73.059  ? 307  LYS A NZ  1 1 
ATOM   2199 N  N   . GLN A 1 272 ? 33.423  25.097  24.665 1    56.02   ? 308  GLN A N   1 1 
ATOM   2200 C  CA  . GLN A 1 272 ? 34.524  24.634  23.841 1    54.118  ? 308  GLN A CA  1 1 
ATOM   2201 C  C   . GLN A 1 272 ? 34.153  24.428  22.383 1    51.706  ? 308  GLN A C   1 1 
ATOM   2202 O  O   . GLN A 1 272 ? 34.92   23.821  21.653 1    50.457  ? 308  GLN A O   1 1 
ATOM   2203 C  CB  . GLN A 1 272 ? 35.107  23.334  24.36  1    56.478  ? 308  GLN A CB  1 1 
ATOM   2204 C  CG  . GLN A 1 272 ? 36.343  23.589  25.207 1    65.593  ? 308  GLN A CG  1 1 
ATOM   2205 C  CD  . GLN A 1 272 ? 36.762  22.341  25.933 1    65.71   ? 308  GLN A CD  1 1 
ATOM   2206 O  OE1 . GLN A 1 272 ? 37.778  21.73   25.599 1    64.138  ? 308  GLN A OE1 1 1 
ATOM   2207 N  NE2 . GLN A 1 272 ? 35.925  21.916  26.867 1    60.009  ? 308  GLN A NE2 1 1 
ATOM   2208 N  N   . GLY A 1 273 ? 33.026  24.977  21.934 1    52.563  ? 309  GLY A N   1 1 
ATOM   2209 C  CA  . GLY A 1 273 ? 32.725  24.948  20.503 1    56.611  ? 309  GLY A CA  1 1 
ATOM   2210 C  C   . GLY A 1 273 ? 32.412  23.548  19.948 1    53.74   ? 309  GLY A C   1 1 
ATOM   2211 O  O   . GLY A 1 273 ? 32.758  23.229  18.81  1    53.722  ? 309  GLY A O   1 1 
ATOM   2212 N  N   . TRP A 1 274 ? 31.776  22.696  20.755 1    49.317  ? 310  TRP A N   1 1 
ATOM   2213 C  CA  . TRP A 1 274 ? 31.346  21.404  20.242 1    49.667  ? 310  TRP A CA  1 1 
ATOM   2214 C  C   . TRP A 1 274 ? 30.271  21.636  19.174 1    48.818  ? 310  TRP A C   1 1 
ATOM   2215 O  O   . TRP A 1 274 ? 29.446  22.512  19.359 1    51.222  ? 310  TRP A O   1 1 
ATOM   2216 C  CB  . TRP A 1 274 ? 30.808  20.569  21.42  1    44.412  ? 310  TRP A CB  1 1 
ATOM   2217 C  CG  . TRP A 1 274 ? 31.903  19.859  22.167 1    44.525  ? 310  TRP A CG  1 1 
ATOM   2218 C  CD1 . TRP A 1 274 ? 33.052  20.409  22.663 1    49.002  ? 310  TRP A CD1 1 1 
ATOM   2219 C  CD2 . TRP A 1 274 ? 32.004  18.44   22.398 1    44.82   ? 310  TRP A CD2 1 1 
ATOM   2220 N  NE1 . TRP A 1 274 ? 33.839  19.442  23.225 1    48.559  ? 310  TRP A NE1 1 1 
ATOM   2221 C  CE2 . TRP A 1 274 ? 33.228  18.219  23.074 1    47.133  ? 310  TRP A CE2 1 1 
ATOM   2222 C  CE3 . TRP A 1 274 ? 31.18   17.341  22.119 1    43.725  ? 310  TRP A CE3 1 1 
ATOM   2223 C  CZ2 . TRP A 1 274 ? 33.649  16.941  23.461 1    44.39   ? 310  TRP A CZ2 1 1 
ATOM   2224 C  CZ3 . TRP A 1 274 ? 31.608  16.078  22.479 1    47.859  ? 310  TRP A CZ3 1 1 
ATOM   2225 C  CH2 . TRP A 1 274 ? 32.833  15.88   23.131 1    50.408  ? 310  TRP A CH2 1 1 
ATOM   2226 N  N   . THR A 1 275 ? 30.295  20.893  18.062 1    47.101  ? 311  THR A N   1 1 
ATOM   2227 C  CA  . THR A 1 275 ? 29.22   20.927  17.075 1    47.1    ? 311  THR A CA  1 1 
ATOM   2228 C  C   . THR A 1 275 ? 28.471  19.586  17.055 1    52.496  ? 311  THR A C   1 1 
ATOM   2229 O  O   . THR A 1 275 ? 29.028  18.575  17.491 1    48.049  ? 311  THR A O   1 1 
ATOM   2230 C  CB  . THR A 1 275 ? 29.857  21.171  15.71  1    49.1    ? 311  THR A CB  1 1 
ATOM   2231 O  OG1 . THR A 1 275 ? 30.53   19.954  15.411 1    53.351  ? 311  THR A OG1 1 1 
ATOM   2232 C  CG2 . THR A 1 275 ? 30.882  22.298  15.668 1    48.414  ? 311  THR A CG2 1 1 
ATOM   2233 N  N   . PRO A 1 276 ? 27.22   19.494  16.509 1    51.578  ? 312  PRO A N   1 1 
ATOM   2234 C  CA  . PRO A 1 276 ? 26.534  18.201  16.345 1    50.413  ? 312  PRO A CA  1 1 
ATOM   2235 C  C   . PRO A 1 276 ? 27.427  17.121  15.748 1    50.077  ? 312  PRO A C   1 1 
ATOM   2236 O  O   . PRO A 1 276 ? 27.417  15.974  16.197 1    52.146  ? 312  PRO A O   1 1 
ATOM   2237 C  CB  . PRO A 1 276 ? 25.374  18.575  15.415 1    46.927  ? 312  PRO A CB  1 1 
ATOM   2238 C  CG  . PRO A 1 276 ? 24.976  19.92   15.935 1    43.914  ? 312  PRO A CG  1 1 
ATOM   2239 C  CD  . PRO A 1 276 ? 26.353  20.616  16.088 1    47.4    ? 312  PRO A CD  1 1 
ATOM   2240 N  N   . ARG A 1 277 ? 28.276  17.539  14.815 1    49.967  ? 313  ARG A N   1 1 
ATOM   2241 C  CA  . ARG A 1 277 ? 29.058  16.606  14.038 1    52.285  ? 313  ARG A CA  1 1 
ATOM   2242 C  C   . ARG A 1 277 ? 30.141  15.979  14.918 1    53.698  ? 313  ARG A C   1 1 
ATOM   2243 O  O   . ARG A 1 277 ? 30.536  14.825  14.726 1    53.491  ? 313  ARG A O   1 1 
ATOM   2244 C  CB  . ARG A 1 277 ? 29.396  17.281  12.711 1    55.658  ? 313  ARG A CB  1 1 
ATOM   2245 C  CG  . ARG A 1 277 ? 30.217  16.392  11.795 1    68.097  ? 313  ARG A CG  1 1 
ATOM   2246 C  CD  . ARG A 1 277 ? 29.964  16.738  10.33  1    77.474  ? 313  ARG A CD  1 1 
ATOM   2247 N  NE  . ARG A 1 277 ? 30.926  16.003  9.492  1    80.406  ? 313  ARG A NE  1 1 
ATOM   2248 C  CZ  . ARG A 1 277 ? 30.617  15.132  8.53   1    75.723  ? 313  ARG A CZ  1 1 
ATOM   2249 N  NH1 . ARG A 1 277 ? 31.59   14.585  7.799  1    63.53   ? 313  ARG A NH1 1 1 
ATOM   2250 N  NH2 . ARG A 1 277 ? 29.332  14.847  8.311  1    73.119  ? 313  ARG A NH2 1 1 
ATOM   2251 N  N   . ARG A 1 278 ? 30.585  16.734  15.923 1    51.927  ? 314  ARG A N   1 1 
ATOM   2252 C  CA  . ARG A 1 278 ? 31.646  16.252  16.791 1    48.334  ? 314  ARG A CA  1 1 
ATOM   2253 C  C   . ARG A 1 278 ? 31.088  15.208  17.761 1    41.807  ? 314  ARG A C   1 1 
ATOM   2254 O  O   . ARG A 1 278 ? 31.792  14.242  18.101 1    38.871  ? 314  ARG A O   1 1 
ATOM   2255 C  CB  . ARG A 1 278 ? 32.29   17.409  17.559 1    48.507  ? 314  ARG A CB  1 1 
ATOM   2256 C  CG  . ARG A 1 278 ? 33.664  16.892  17.942 1    51.123  ? 314  ARG A CG  1 1 
ATOM   2257 C  CD  . ARG A 1 278 ? 33.895  17.373  19.346 1    56.453  ? 314  ARG A CD  1 1 
ATOM   2258 N  NE  . ARG A 1 278 ? 35.203  17.091  19.948 1    52.929  ? 314  ARG A NE  1 1 
ATOM   2259 C  CZ  . ARG A 1 278 ? 35.892  18.045  20.542 1    55.925  ? 314  ARG A CZ  1 1 
ATOM   2260 N  NH1 . ARG A 1 278 ? 35.705  19.316  20.206 1    57.809  ? 314  ARG A NH1 1 1 
ATOM   2261 N  NH2 . ARG A 1 278 ? 36.807  17.713  21.432 1    55.896  ? 314  ARG A NH2 1 1 
ATOM   2262 N  N   . MET A 1 279 ? 29.838  15.451  18.2   1    36.534  ? 315  MET A N   1 1 
ATOM   2263 C  CA  . MET A 1 279 ? 29.098  14.598  19.099 1    38.361  ? 315  MET A CA  1 1 
ATOM   2264 C  C   . MET A 1 279 ? 28.967  13.208  18.475 1    39.475  ? 315  MET A C   1 1 
ATOM   2265 O  O   . MET A 1 279 ? 29.219  12.216  19.149 1    37.819  ? 315  MET A O   1 1 
ATOM   2266 C  CB  . MET A 1 279 ? 27.742  15.222  19.436 1    38.467  ? 315  MET A CB  1 1 
ATOM   2267 C  CG  . MET A 1 279 ? 27.864  16.667  19.894 1    39.292  ? 315  MET A CG  1 1 
ATOM   2268 S  SD  . MET A 1 279 ? 26.302  17.538  20.177 1    42.457  ? 315  MET A SD  1 1 
ATOM   2269 C  CE  . MET A 1 279 ? 25.205  16.786  21.387 1    34.797  ? 315  MET A CE  1 1 
ATOM   2270 N  N   . PHE A 1 280 ? 28.721  13.179  17.16  1    38.833  ? 316  PHE A N   1 1 
ATOM   2271 C  CA  . PHE A 1 280 ? 28.514  11.96   16.389 1    36.867  ? 316  PHE A CA  1 1 
ATOM   2272 C  C   . PHE A 1 280 ? 29.844  11.257  16.141 1    35.54   ? 316  PHE A C   1 1 
ATOM   2273 O  O   . PHE A 1 280 ? 29.939  10.035  16.292 1    36.055  ? 316  PHE A O   1 1 
ATOM   2274 C  CB  . PHE A 1 280 ? 27.639  12.148  15.134 1    33.57   ? 316  PHE A CB  1 1 
ATOM   2275 C  CG  . PHE A 1 280 ? 26.16   12.338  15.468 1    31.441  ? 316  PHE A CG  1 1 
ATOM   2276 C  CD1 . PHE A 1 280 ? 25.305  11.259  15.635 1    30.17   ? 316  PHE A CD1 1 1 
ATOM   2277 C  CD2 . PHE A 1 280 ? 25.599  13.592  15.622 1    30.175  ? 316  PHE A CD2 1 1 
ATOM   2278 C  CE1 . PHE A 1 280 ? 23.955  11.412  15.99  1    29.351  ? 316  PHE A CE1 1 1 
ATOM   2279 C  CE2 . PHE A 1 280 ? 24.236  13.732  15.89  1    30.04   ? 316  PHE A CE2 1 1 
ATOM   2280 C  CZ  . PHE A 1 280 ? 23.402  12.654  16.093 1    28.585  ? 316  PHE A CZ  1 1 
ATOM   2281 N  N   . LYS A 1 281 ? 30.865  12.022  15.776 1    38.002  ? 317  LYS A N   1 1 
ATOM   2282 C  CA  . LYS A 1 281 ? 32.221  11.509  15.637 1    36.794  ? 317  LYS A CA  1 1 
ATOM   2283 C  C   . LYS A 1 281 ? 32.691  10.893  16.961 1    37.598  ? 317  LYS A C   1 1 
ATOM   2284 O  O   . LYS A 1 281 ? 33.314  9.835   16.939 1    38.103  ? 317  LYS A O   1 1 
ATOM   2285 C  CB  . LYS A 1 281 ? 33.217  12.596  15.227 1    38.36   ? 317  LYS A CB  1 1 
ATOM   2286 C  CG  . LYS A 1 281 ? 33.014  13.226  13.855 1    42.87   ? 317  LYS A CG  1 1 
ATOM   2287 C  CD  . LYS A 1 281 ? 33.309  12.183  12.785 1    43.759  ? 317  LYS A CD  1 1 
ATOM   2288 C  CE  . LYS A 1 281 ? 33.616  12.793  11.44  1    47.465  ? 317  LYS A CE  1 1 
ATOM   2289 N  NZ  . LYS A 1 281 ? 33.691  11.693  10.464 1    47.46   ? 317  LYS A NZ  1 1 
ATOM   2290 N  N   . GLU A 1 282 ? 32.394  11.525  18.114 1    37.164  ? 318  GLU A N   1 1 
ATOM   2291 C  CA  . GLU A 1 282 ? 32.745  10.94   19.416 1    39.224  ? 318  GLU A CA  1 1 
ATOM   2292 C  C   . GLU A 1 282 ? 32.03   9.608   19.68  1    38.74   ? 318  GLU A C   1 1 
ATOM   2293 O  O   . GLU A 1 282 ? 32.642  8.698   20.249 1    39.312  ? 318  GLU A O   1 1 
ATOM   2294 C  CB  . GLU A 1 282 ? 32.492  11.824  20.637 1    39.235  ? 318  GLU A CB  1 1 
ATOM   2295 C  CG  . GLU A 1 282 ? 33.435  13.017  20.716 1    47.179  ? 318  GLU A CG  1 1 
ATOM   2296 C  CD  . GLU A 1 282 ? 34.876  12.594  20.931 1    53.83   ? 318  GLU A CD  1 1 
ATOM   2297 O  OE1 . GLU A 1 282 ? 35.103  11.6    21.642 1    59.691  ? 318  GLU A OE1 1 1 
ATOM   2298 O  OE2 . GLU A 1 282 ? 35.77   13.262  20.412 1    61.249  ? 318  GLU A OE2 1 1 
ATOM   2299 N  N   . ALA A 1 283 ? 30.738  9.477   19.293 1    34.849  ? 319  ALA A N   1 1 
ATOM   2300 C  CA  . ALA A 1 283 ? 30.005  8.215   19.423 1    30.567  ? 319  ALA A CA  1 1 
ATOM   2301 C  C   . ALA A 1 283 ? 30.625  7.155   18.517 1    32.143  ? 319  ALA A C   1 1 
ATOM   2302 O  O   . ALA A 1 283 ? 30.919  6.034   18.961 1    31.698  ? 319  ALA A O   1 1 
ATOM   2303 C  CB  . ALA A 1 283 ? 28.52   8.393   19.146 1    30.643  ? 319  ALA A CB  1 1 
ATOM   2304 N  N   . ASP A 1 284 ? 30.885  7.543   17.257 1    30.53   ? 320  ASP A N   1 1 
ATOM   2305 C  CA  . ASP A 1 284 ? 31.5    6.623   16.33  1    32.739  ? 320  ASP A CA  1 1 
ATOM   2306 C  C   . ASP A 1 284 ? 32.848  6.141   16.878 1    34.94   ? 320  ASP A C   1 1 
ATOM   2307 O  O   . ASP A 1 284 ? 33.181  4.961   16.699 1    33.654  ? 320  ASP A O   1 1 
ATOM   2308 C  CB  . ASP A 1 284 ? 31.588  7.182   14.912 1    33.679  ? 320  ASP A CB  1 1 
ATOM   2309 C  CG  . ASP A 1 284 ? 32.037  6.185   13.844 1    39.997  ? 320  ASP A CG  1 1 
ATOM   2310 O  OD1 . ASP A 1 284 ? 31.327  5.171   13.644 1    38.633  ? 320  ASP A OD1 1 1 
ATOM   2311 O  OD2 . ASP A 1 284 ? 33.075  6.439   13.154 1    44.69   ? 320  ASP A OD2 1 1 
ATOM   2312 N  N   . ASP A 1 285 ? 33.604  7.039   17.548 1    34.036  ? 321  ASP A N   1 1 
ATOM   2313 C  CA  . ASP A 1 285 ? 34.931  6.655   18.059 1    34.08   ? 321  ASP A CA  1 1 
ATOM   2314 C  C   . ASP A 1 285 ? 34.807  5.633   19.204 1    32.935  ? 321  ASP A C   1 1 
ATOM   2315 O  O   . ASP A 1 285 ? 35.566  4.657   19.226 1    32.658  ? 321  ASP A O   1 1 
ATOM   2316 C  CB  . ASP A 1 285 ? 35.801  7.819   18.498 1    33.263  ? 321  ASP A CB  1 1 
ATOM   2317 C  CG  . ASP A 1 285 ? 37.109  7.409   19.19  1    37.103  ? 321  ASP A CG  1 1 
ATOM   2318 O  OD1 . ASP A 1 285 ? 37.99   6.88    18.499 1    38.854  ? 321  ASP A OD1 1 1 
ATOM   2319 O  OD2 . ASP A 1 285 ? 37.241  7.57    20.428 1    37.45   ? 321  ASP A OD2 1 1 
ATOM   2320 N  N   . PHE A 1 286 ? 33.804  5.821   20.081 1    28.84   ? 322  PHE A N   1 1 
ATOM   2321 C  CA  . PHE A 1 286 ? 33.494  4.882   21.155 1    31.186  ? 322  PHE A CA  1 1 
ATOM   2322 C  C   . PHE A 1 286 ? 33.129  3.51    20.566 1    32.249  ? 322  PHE A C   1 1 
ATOM   2323 O  O   . PHE A 1 286 ? 33.686  2.482   20.984 1    34.496  ? 322  PHE A O   1 1 
ATOM   2324 C  CB  . PHE A 1 286 ? 32.428  5.337   22.177 1    27.423  ? 322  PHE A CB  1 1 
ATOM   2325 C  CG  . PHE A 1 286 ? 32.575  4.723   23.573 1    29.003  ? 322  PHE A CG  1 1 
ATOM   2326 C  CD1 . PHE A 1 286 ? 32.487  3.356   23.777 1    29.629  ? 322  PHE A CD1 1 1 
ATOM   2327 C  CD2 . PHE A 1 286 ? 32.781  5.519   24.716 1    30.652  ? 322  PHE A CD2 1 1 
ATOM   2328 C  CE1 . PHE A 1 286 ? 32.63   2.807   25.053 1    31.103  ? 322  PHE A CE1 1 1 
ATOM   2329 C  CE2 . PHE A 1 286 ? 32.864  4.98    25.998 1    28.834  ? 322  PHE A CE2 1 1 
ATOM   2330 C  CZ  . PHE A 1 286 ? 32.776  3.621   26.173 1    30.825  ? 322  PHE A CZ  1 1 
ATOM   2331 N  N   . PHE A 1 287 ? 32.215  3.466   19.583 1    29.954  ? 323  PHE A N   1 1 
ATOM   2332 C  CA  . PHE A 1 287 ? 31.974  2.152   18.988 1    31.969  ? 323  PHE A CA  1 1 
ATOM   2333 C  C   . PHE A 1 287 ? 33.231  1.472   18.413 1    31.816  ? 323  PHE A C   1 1 
ATOM   2334 O  O   . PHE A 1 287 ? 33.461  0.277   18.67  1    32.242  ? 323  PHE A O   1 1 
ATOM   2335 C  CB  . PHE A 1 287 ? 30.852  2.095   17.956 1    31.521  ? 323  PHE A CB  1 1 
ATOM   2336 C  CG  . PHE A 1 287 ? 29.481  2.2     18.594 1    28.809  ? 323  PHE A CG  1 1 
ATOM   2337 C  CD1 . PHE A 1 287 ? 28.892  3.454   18.843 1    27.778  ? 323  PHE A CD1 1 1 
ATOM   2338 C  CD2 . PHE A 1 287 ? 28.746  1.05    18.885 1    26.937  ? 323  PHE A CD2 1 1 
ATOM   2339 C  CE1 . PHE A 1 287 ? 27.596  3.56    19.375 1    23.77   ? 323  PHE A CE1 1 1 
ATOM   2340 C  CE2 . PHE A 1 287 ? 27.446  1.176   19.445 1    25.962  ? 323  PHE A CE2 1 1 
ATOM   2341 C  CZ  . PHE A 1 287 ? 26.891  2.412   19.691 1    23.671  ? 323  PHE A CZ  1 1 
ATOM   2342 N  N   . THR A 1 288 ? 34.022  2.174   17.582 1    33.85   ? 324  THR A N   1 1 
ATOM   2343 C  CA  . THR A 1 288 ? 35.193  1.524   16.995 1    35.694  ? 324  THR A CA  1 1 
ATOM   2344 C  C   . THR A 1 288 ? 36.245  1.248   18.075 1    34.019  ? 324  THR A C   1 1 
ATOM   2345 O  O   . THR A 1 288 ? 37.076  0.378   17.844 1    36.054  ? 324  THR A O   1 1 
ATOM   2346 C  CB  . THR A 1 288 ? 35.873  2.247   15.81  1    38.146  ? 324  THR A CB  1 1 
ATOM   2347 O  OG1 . THR A 1 288 ? 36.134  3.473   16.465 1    37.803  ? 324  THR A OG1 1 1 
ATOM   2348 C  CG2 . THR A 1 288 ? 34.972  2.516   14.615 1    37.23   ? 324  THR A CG2 1 1 
ATOM   2349 N  N   . SER A 1 289 ? 36.231  1.947   19.225 1    31.752  ? 325  SER A N   1 1 
ATOM   2350 C  CA  . SER A 1 289 ? 37.224  1.64    20.261 1    31.935  ? 325  SER A CA  1 1 
ATOM   2351 C  C   . SER A 1 289 ? 37.005  0.23    20.819 1    33.595  ? 325  SER A C   1 1 
ATOM   2352 O  O   . SER A 1 289 ? 37.964  -0.432  21.251 1    31.595  ? 325  SER A O   1 1 
ATOM   2353 C  CB  . SER A 1 289 ? 37.287  2.631   21.394 1    30.197  ? 325  SER A CB  1 1 
ATOM   2354 O  OG  . SER A 1 289 ? 36.221  2.345   22.308 1    28.752  ? 325  SER A OG  1 1 
ATOM   2355 N  N   . LEU A 1 290 ? 35.735  -0.211  20.746 1    31.517  ? 326  LEU A N   1 1 
ATOM   2356 C  CA  . LEU A 1 290 ? 35.299  -1.527  21.201 1    34.526  ? 326  LEU A CA  1 1 
ATOM   2357 C  C   . LEU A 1 290 ? 35.528  -2.655  20.175 1    34.517  ? 326  LEU A C   1 1 
ATOM   2358 O  O   . LEU A 1 290 ? 35.192  -3.828  20.446 1    35.43   ? 326  LEU A O   1 1 
ATOM   2359 C  CB  . LEU A 1 290 ? 33.809  -1.412  21.536 1    35.892  ? 326  LEU A CB  1 1 
ATOM   2360 C  CG  . LEU A 1 290 ? 33.417  -0.509  22.703 1    31.192  ? 326  LEU A CG  1 1 
ATOM   2361 C  CD1 . LEU A 1 290 ? 31.999  -0.747  23.097 1    29.839  ? 326  LEU A CD1 1 1 
ATOM   2362 C  CD2 . LEU A 1 290 ? 34.303  -0.686  23.935 1    33.024  ? 326  LEU A CD2 1 1 
ATOM   2363 N  N   . GLY A 1 291 ? 36.073  -2.325  18.99  1    33.681  ? 327  GLY A N   1 1 
ATOM   2364 C  CA  . GLY A 1 291 ? 36.161  -3.326  17.949 1    36.095  ? 327  GLY A CA  1 1 
ATOM   2365 C  C   . GLY A 1 291 ? 34.861  -3.428  17.146 1    36.629  ? 327  GLY A C   1 1 
ATOM   2366 O  O   . GLY A 1 291 ? 34.799  -4.22   16.223 1    35.299  ? 327  GLY A O   1 1 
ATOM   2367 N  N   . LEU A 1 292 ? 33.849  -2.603  17.484 1    35.956  ? 328  LEU A N   1 1 
ATOM   2368 C  CA  . LEU A 1 292 ? 32.576  -2.526  16.765 1    37.523  ? 328  LEU A CA  1 1 
ATOM   2369 C  C   . LEU A 1 292 ? 32.765  -1.759  15.445 1    39.278  ? 328  LEU A C   1 1 
ATOM   2370 O  O   . LEU A 1 292 ? 33.833  -1.177  15.188 1    35.969  ? 328  LEU A O   1 1 
ATOM   2371 C  CB  . LEU A 1 292 ? 31.451  -1.984  17.656 1    34.978  ? 328  LEU A CB  1 1 
ATOM   2372 C  CG  . LEU A 1 292 ? 31.167  -2.835  18.91  1    38.019  ? 328  LEU A CG  1 1 
ATOM   2373 C  CD1 . LEU A 1 292 ? 30.168  -2.208  19.889 1    32.854  ? 328  LEU A CD1 1 1 
ATOM   2374 C  CD2 . LEU A 1 292 ? 30.727  -4.275  18.551 1    40.125  ? 328  LEU A CD2 1 1 
ATOM   2375 N  N   . LEU A 1 293 ? 31.731  -1.796  14.598 1    35.463  ? 329  LEU A N   1 1 
ATOM   2376 C  CA  . LEU A 1 293 ? 31.867  -1.348  13.214 1    36.699  ? 329  LEU A CA  1 1 
ATOM   2377 C  C   . LEU A 1 293 ? 31.749  0.164   13.067 1    34.496  ? 329  LEU A C   1 1 
ATOM   2378 O  O   . LEU A 1 293 ? 30.851  0.78    13.625 1    34.328  ? 329  LEU A O   1 1 
ATOM   2379 C  CB  . LEU A 1 293 ? 30.768  -2.027  12.388 1    38.568  ? 329  LEU A CB  1 1 
ATOM   2380 C  CG  . LEU A 1 293 ? 31.018  -3.482  11.982 1    36.655  ? 329  LEU A CG  1 1 
ATOM   2381 C  CD1 . LEU A 1 293 ? 29.651  -3.966  11.541 1    39.168  ? 329  LEU A CD1 1 1 
ATOM   2382 C  CD2 . LEU A 1 293 ? 32.114  -3.601  10.903 1    37.987  ? 329  LEU A CD2 1 1 
ATOM   2383 N  N   . PRO A 1 294 ? 32.572  0.814   12.203 1    37.421  ? 330  PRO A N   1 1 
ATOM   2384 C  CA  . PRO A 1 294 ? 32.408  2.259   11.998 1    36.651  ? 330  PRO A CA  1 1 
ATOM   2385 C  C   . PRO A 1 294 ? 31.203  2.487   11.082 1    37.653  ? 330  PRO A C   1 1 
ATOM   2386 O  O   . PRO A 1 294 ? 30.916  1.644   10.232 1    37.666  ? 330  PRO A O   1 1 
ATOM   2387 C  CB  . PRO A 1 294 ? 33.729  2.682   11.36  1    37.569  ? 330  PRO A CB  1 1 
ATOM   2388 C  CG  . PRO A 1 294 ? 34.229  1.388   10.666 1    38.003  ? 330  PRO A CG  1 1 
ATOM   2389 C  CD  . PRO A 1 294 ? 33.61   0.189   11.353 1    36.131  ? 330  PRO A CD  1 1 
ATOM   2390 N  N   . VAL A 1 295 ? 30.55   3.652   11.192 1    36.317  ? 331  VAL A N   1 1 
ATOM   2391 C  CA  . VAL A 1 295 ? 29.478  3.97    10.256 1    37.278  ? 331  VAL A CA  1 1 
ATOM   2392 C  C   . VAL A 1 295 ? 30.085  4.254   8.883  1    41.157  ? 331  VAL A C   1 1 
ATOM   2393 O  O   . VAL A 1 295 ? 31.191  4.789   8.845  1    45.164  ? 331  VAL A O   1 1 
ATOM   2394 C  CB  . VAL A 1 295 ? 28.647  5.15    10.787 1    35.432  ? 331  VAL A CB  1 1 
ATOM   2395 C  CG1 . VAL A 1 295 ? 27.974  4.788   12.106 1    31.381  ? 331  VAL A CG1 1 1 
ATOM   2396 C  CG2 . VAL A 1 295 ? 29.477  6.442   10.904 1    34.705  ? 331  VAL A CG2 1 1 
ATOM   2397 N  N   . PRO A 1 296 ? 29.475  3.795   7.74   1    40.815  ? 332  PRO A N   1 1 
ATOM   2398 C  CA  . PRO A 1 296 ? 30.051  4.028   6.409  1    40.678  ? 332  PRO A CA  1 1 
ATOM   2399 C  C   . PRO A 1 296 ? 30.264  5.493   6.032  1    41.811  ? 332  PRO A C   1 1 
ATOM   2400 O  O   . PRO A 1 296 ? 29.59   6.356   6.575  1    41.465  ? 332  PRO A O   1 1 
ATOM   2401 C  CB  . PRO A 1 296 ? 29.083  3.335   5.406  1    39.836  ? 332  PRO A CB  1 1 
ATOM   2402 C  CG  . PRO A 1 296 ? 28.003  2.671   6.228  1    39.127  ? 332  PRO A CG  1 1 
ATOM   2403 C  CD  . PRO A 1 296 ? 28.235  2.982   7.685  1    37.53   ? 332  PRO A CD  1 1 
ATOM   2404 N  N   A PRO A 1 297 ? 31.192  5.821   5.095  0.5  47.255  ? 333  PRO A N   1 1 
ATOM   2405 N  N   B PRO A 1 297 ? 31.192  5.821   5.095  0.5  47.255  ? 333  PRO A N   1 1 
ATOM   2406 C  CA  A PRO A 1 297 ? 31.329  7.202   4.595  0.5  47.681  ? 333  PRO A CA  1 1 
ATOM   2407 C  CA  B PRO A 1 297 ? 31.329  7.202   4.595  0.5  47.681  ? 333  PRO A CA  1 1 
ATOM   2408 C  C   A PRO A 1 297 ? 30.012  7.866   4.148  0.5  48.251  ? 333  PRO A C   1 1 
ATOM   2409 C  C   B PRO A 1 297 ? 30.012  7.866   4.148  0.5  48.251  ? 333  PRO A C   1 1 
ATOM   2410 O  O   A PRO A 1 297 ? 29.804  9.123   4.343  0.5  47.12   ? 333  PRO A O   1 1 
ATOM   2411 O  O   B PRO A 1 297 ? 29.804  9.123   4.343  0.5  47.12   ? 333  PRO A O   1 1 
ATOM   2412 C  CB  A PRO A 1 297 ? 32.314  7.028   3.425  0.5  48.357  ? 333  PRO A CB  1 1 
ATOM   2413 C  CB  B PRO A 1 297 ? 32.314  7.028   3.425  0.5  48.357  ? 333  PRO A CB  1 1 
ATOM   2414 C  CG  A PRO A 1 297 ? 33.169  5.847   3.824  0.5  46.763  ? 333  PRO A CG  1 1 
ATOM   2415 C  CG  B PRO A 1 297 ? 33.169  5.847   3.824  0.5  46.763  ? 333  PRO A CG  1 1 
ATOM   2416 C  CD  A PRO A 1 297 ? 32.18   4.898   4.5    0.5  46.116  ? 333  PRO A CD  1 1 
ATOM   2417 C  CD  B PRO A 1 297 ? 32.18   4.898   4.5    0.5  46.116  ? 333  PRO A CD  1 1 
ATOM   2418 N  N   . GLU A 1 298 ? 29.129  7.007   3.573  1    51.034  ? 334  GLU A N   1 1 
ATOM   2419 C  CA  . GLU A 1 298 ? 27.792  7.374   3.102  1    49.481  ? 334  GLU A CA  1 1 
ATOM   2420 C  C   . GLU A 1 298 ? 26.919  7.916   4.228  1    48.119  ? 334  GLU A C   1 1 
ATOM   2421 O  O   . GLU A 1 298 ? 26.075  8.789   3.988  1    50.279  ? 334  GLU A O   1 1 
ATOM   2422 C  CB  . GLU A 1 298 ? 27.063  6.183   2.466  1    50.872  ? 334  GLU A CB  1 1 
ATOM   2423 C  CG  . GLU A 1 298 ? 25.755  6.571   1.774  1    50.993  ? 334  GLU A CG  1 1 
ATOM   2424 C  CD  . GLU A 1 298 ? 24.993  5.479   1.025  1    53.242  ? 334  GLU A CD  1 1 
ATOM   2425 O  OE1 . GLU A 1 298 ? 25.516  4.359   0.905  1    47.921  ? 334  GLU A OE1 1 1 
ATOM   2426 O  OE2 . GLU A 1 298 ? 23.831  5.732   0.611  1    56.415  ? 334  GLU A OE2 1 1 
ATOM   2427 N  N   . PHE A 1 299 ? 27.121  7.37    5.445  1    42.155  ? 335  PHE A N   1 1 
ATOM   2428 C  CA  . PHE A 1 299 ? 26.373  7.799   6.62   1    38.088  ? 335  PHE A CA  1 1 
ATOM   2429 C  C   . PHE A 1 299 ? 26.614  9.294   6.863  1    38.829  ? 335  PHE A C   1 1 
ATOM   2430 O  O   . PHE A 1 299 ? 25.71   10.041  7.238  1    35.452  ? 335  PHE A O   1 1 
ATOM   2431 C  CB  . PHE A 1 299 ? 26.63   6.884   7.836  1    36.154  ? 335  PHE A CB  1 1 
ATOM   2432 C  CG  . PHE A 1 299 ? 26.198  7.555   9.136  1    36.879  ? 335  PHE A CG  1 1 
ATOM   2433 C  CD1 . PHE A 1 299 ? 26.834  8.709   9.604  1    36.478  ? 335  PHE A CD1 1 1 
ATOM   2434 C  CD2 . PHE A 1 299 ? 25.153  7.05    9.907  1    37.192  ? 335  PHE A CD2 1 1 
ATOM   2435 C  CE1 . PHE A 1 299 ? 26.416  9.317   10.781 1    32.827  ? 335  PHE A CE1 1 1 
ATOM   2436 C  CE2 . PHE A 1 299 ? 24.756  7.668   11.097 1    33.614  ? 335  PHE A CE2 1 1 
ATOM   2437 C  CZ  . PHE A 1 299 ? 25.376  8.814   11.525 1    33.299  ? 335  PHE A CZ  1 1 
ATOM   2438 N  N   . TRP A 1 300 ? 27.867  9.72    6.685  1    39.88   ? 336  TRP A N   1 1 
ATOM   2439 C  CA  . TRP A 1 300 ? 28.263  11.074  7.06   1    44.972  ? 336  TRP A CA  1 1 
ATOM   2440 C  C   . TRP A 1 300 ? 27.741  12.096  6.034  1    47.832  ? 336  TRP A C   1 1 
ATOM   2441 O  O   . TRP A 1 300 ? 27.354  13.213  6.419  1    47.435  ? 336  TRP A O   1 1 
ATOM   2442 C  CB  . TRP A 1 300 ? 29.792  11.148  7.212  1    41.614  ? 336  TRP A CB  1 1 
ATOM   2443 C  CG  . TRP A 1 300 ? 30.324  10.403  8.406  1    38.559  ? 336  TRP A CG  1 1 
ATOM   2444 C  CD1 . TRP A 1 300 ? 31.114  9.281   8.413  1    39.43   ? 336  TRP A CD1 1 1 
ATOM   2445 C  CD2 . TRP A 1 300 ? 30.073  10.74   9.785  1    38.262  ? 336  TRP A CD2 1 1 
ATOM   2446 N  NE1 . TRP A 1 300 ? 31.359  8.891   9.711  1    40.458  ? 336  TRP A NE1 1 1 
ATOM   2447 C  CE2 . TRP A 1 300 ? 30.739  9.773   10.571 1    38.936  ? 336  TRP A CE2 1 1 
ATOM   2448 C  CE3 . TRP A 1 300 ? 29.344  11.745  10.436 1    38.339  ? 336  TRP A CE3 1 1 
ATOM   2449 C  CZ2 . TRP A 1 300 ? 30.689  9.803   11.967 1    38.167  ? 336  TRP A CZ2 1 1 
ATOM   2450 C  CZ3 . TRP A 1 300 ? 29.294  11.768  11.82  1    38.002  ? 336  TRP A CZ3 1 1 
ATOM   2451 C  CH2 . TRP A 1 300 ? 29.967  10.804  12.582 1    36.723  ? 336  TRP A CH2 1 1 
ATOM   2452 N  N   . GLN A 1 301 ? 27.692  11.673  4.753  1    45.822  ? 337  GLN A N   1 1 
ATOM   2453 C  CA  . GLN A 1 301 ? 27.17   12.473  3.656  1    50.599  ? 337  GLN A CA  1 1 
ATOM   2454 C  C   . GLN A 1 301 ? 25.648  12.61   3.711  1    52.385  ? 337  GLN A C   1 1 
ATOM   2455 O  O   . GLN A 1 301 ? 25.138  13.674  3.385  1    53.034  ? 337  GLN A O   1 1 
ATOM   2456 C  CB  . GLN A 1 301 ? 27.452  11.785  2.33   1    53.599  ? 337  GLN A CB  1 1 
ATOM   2457 C  CG  . GLN A 1 301 ? 28.931  11.763  1.979  1    66.035  ? 337  GLN A CG  1 1 
ATOM   2458 C  CD  . GLN A 1 301 ? 29.319  10.631  1.045  1    77.969  ? 337  GLN A CD  1 1 
ATOM   2459 O  OE1 . GLN A 1 301 ? 28.489  9.826   0.584  1    75.295  ? 337  GLN A OE1 1 1 
ATOM   2460 N  NE2 . GLN A 1 301 ? 30.616  10.56   0.768  1    77.033  ? 337  GLN A NE2 1 1 
ATOM   2461 N  N   . LYS A 1 302 ? 24.918  11.556  4.118  1    49.328  ? 338  LYS A N   1 1 
ATOM   2462 C  CA  . LYS A 1 302 ? 23.478  11.511  3.895  1    45.133  ? 338  LYS A CA  1 1 
ATOM   2463 C  C   . LYS A 1 302 ? 22.671  11.809  5.153  1    41.755  ? 338  LYS A C   1 1 
ATOM   2464 O  O   . LYS A 1 302 ? 21.525  12.227  5.067  1    41.614  ? 338  LYS A O   1 1 
ATOM   2465 C  CB  . LYS A 1 302 ? 23.084  10.162  3.287  1    47.76   ? 338  LYS A CB  1 1 
ATOM   2466 C  CG  . LYS A 1 302 ? 23.288  10.039  1.77   1    50.898  ? 338  LYS A CG  1 1 
ATOM   2467 C  CD  . LYS A 1 302 ? 22.586  8.778   1.272  1    51.824  ? 338  LYS A CD  1 1 
ATOM   2468 C  CE  . LYS A 1 302 ? 22.399  8.527   -0.187 1    57.168  ? 338  LYS A CE  1 1 
ATOM   2469 N  NZ  . LYS A 1 302 ? 23.641  8.852   -0.89  1    60.267  ? 338  LYS A NZ  1 1 
ATOM   2470 N  N   . SER A 1 303 ? 23.225  11.585  6.347  1    44.638  ? 339  SER A N   1 1 
ATOM   2471 C  CA  . SER A 1 303 ? 22.431  11.788  7.544  1    42.759  ? 339  SER A CA  1 1 
ATOM   2472 C  C   . SER A 1 303 ? 22.1    13.262  7.678  1    44.528  ? 339  SER A C   1 1 
ATOM   2473 O  O   . SER A 1 303 ? 22.812  14.084  7.115  1    39.553  ? 339  SER A O   1 1 
ATOM   2474 C  CB  . SER A 1 303 ? 23.19   11.401  8.752  1    45.944  ? 339  SER A CB  1 1 
ATOM   2475 O  OG  . SER A 1 303 ? 23.437  10.011  8.713  1    48.343  ? 339  SER A OG  1 1 
ATOM   2476 N  N   . MET A 1 304 ? 21.139  13.576  8.552  1    43.02   ? 340  MET A N   1 1 
ATOM   2477 C  CA  . MET A 1 304 ? 20.849  14.961  8.882  1    43.359  ? 340  MET A CA  1 1 
ATOM   2478 C  C   . MET A 1 304 ? 21.163  15.138  10.362 1    45.266  ? 340  MET A C   1 1 
ATOM   2479 O  O   . MET A 1 304 ? 20.376  14.666  11.188 1    39.715  ? 340  MET A O   1 1 
ATOM   2480 C  CB  . MET A 1 304 ? 19.353  15.254  8.7    1    43.712  ? 340  MET A CB  1 1 
ATOM   2481 C  CG  . MET A 1 304 ? 18.947  16.729  8.629  1    42.717  ? 340  MET A CG  1 1 
ATOM   2482 S  SD  . MET A 1 304 ? 17.22   16.891  9.147  1    43.375  ? 340  MET A SD  1 1 
ATOM   2483 C  CE  . MET A 1 304 ? 16.92   16.825  10.919 1    39.477  ? 340  MET A CE  1 1 
ATOM   2484 N  N   . LEU A 1 305 ? 22.255  15.871  10.696 1    45.52   ? 341  LEU A N   1 1 
ATOM   2485 C  CA  . LEU A 1 305 ? 22.69   15.862  12.092 1    44.742  ? 341  LEU A CA  1 1 
ATOM   2486 C  C   . LEU A 1 305 ? 22.29   17.119  12.879 1    46.722  ? 341  LEU A C   1 1 
ATOM   2487 O  O   . LEU A 1 305 ? 22.382  17.131  14.114 1    52.484  ? 341  LEU A O   1 1 
ATOM   2488 C  CB  . LEU A 1 305 ? 24.147  15.415  12.245 1    39.092  ? 341  LEU A CB  1 1 
ATOM   2489 C  CG  . LEU A 1 305 ? 24.511  14.045  11.66  1    37.41   ? 341  LEU A CG  1 1 
ATOM   2490 C  CD1 . LEU A 1 305 ? 26      13.725  11.821 1    41.104  ? 341  LEU A CD1 1 1 
ATOM   2491 C  CD2 . LEU A 1 305 ? 23.694  12.893  12.248 1    36.382  ? 341  LEU A CD2 1 1 
ATOM   2492 N  N   . GLU A 1 306 ? 21.769  18.152  12.193 1    47.348  ? 342  GLU A N   1 1 
ATOM   2493 C  CA  . GLU A 1 306 ? 21.099  19.274  12.851 1    48.427  ? 342  GLU A CA  1 1 
ATOM   2494 C  C   . GLU A 1 306 ? 19.932  19.733  11.982 1    51.254  ? 342  GLU A C   1 1 
ATOM   2495 O  O   . GLU A 1 306 ? 19.941  19.46   10.783 1    53.583  ? 342  GLU A O   1 1 
ATOM   2496 C  CB  . GLU A 1 306 ? 21.797  20.61   12.577 1    55.386  ? 342  GLU A CB  1 1 
ATOM   2497 C  CG  . GLU A 1 306 ? 23.224  20.764  13.085 1    63.075  ? 342  GLU A CG  1 1 
ATOM   2498 C  CD  . GLU A 1 306 ? 24.228  20.671  11.959 1    69.16   ? 342  GLU A CD  1 1 
ATOM   2499 O  OE1 . GLU A 1 306 ? 25.379  21.163  12.079 1    62.74   ? 342  GLU A OE1 1 1 
ATOM   2500 O  OE2 . GLU A 1 306 ? 23.818  20.077  10.944 1    72.838  ? 342  GLU A OE2 1 1 
ATOM   2501 N  N   . LYS A 1 307 ? 18.983  20.49   12.546 1    51.165  ? 343  LYS A N   1 1 
ATOM   2502 C  CA  . LYS A 1 307 ? 18.032  21.218  11.718 1    57.415  ? 343  LYS A CA  1 1 
ATOM   2503 C  C   . LYS A 1 307 ? 18.697  21.766  10.447 1    72.725  ? 343  LYS A C   1 1 
ATOM   2504 O  O   . LYS A 1 307 ? 19.775  22.356  10.528 1    79.308  ? 343  LYS A O   1 1 
ATOM   2505 C  CB  . LYS A 1 307 ? 17.594  22.387  12.59  1    58.968  ? 343  LYS A CB  1 1 
ATOM   2506 C  CG  . LYS A 1 307 ? 16.586  23.251  11.916 1    63.415  ? 343  LYS A CG  1 1 
ATOM   2507 C  CD  . LYS A 1 307 ? 15.457  23.139  12.926 1    63.853  ? 343  LYS A CD  1 1 
ATOM   2508 C  CE  . LYS A 1 307 ? 14.21   23.745  12.401 1    70.364  ? 343  LYS A CE  1 1 
ATOM   2509 N  NZ  . LYS A 1 307 ? 13.142  23.31   13.304 1    77.702  ? 343  LYS A NZ  1 1 
ATOM   2510 N  N   . PRO A 1 308 ? 18.134  21.609  9.217  1    78.566  ? 344  PRO A N   1 1 
ATOM   2511 C  CA  . PRO A 1 308 ? 18.756  22.195  8.024  1    72.311  ? 344  PRO A CA  1 1 
ATOM   2512 C  C   . PRO A 1 308 ? 18.503  23.698  8.026  1    68.625  ? 344  PRO A C   1 1 
ATOM   2513 O  O   . PRO A 1 308 ? 17.661  24.206  8.769  1    68.09   ? 344  PRO A O   1 1 
ATOM   2514 C  CB  . PRO A 1 308 ? 18.144  21.493  6.811  1    76.224  ? 344  PRO A CB  1 1 
ATOM   2515 C  CG  . PRO A 1 308 ? 17.114  20.553  7.404  1    78.214  ? 344  PRO A CG  1 1 
ATOM   2516 C  CD  . PRO A 1 308 ? 16.896  20.884  8.895  1    76.534  ? 344  PRO A CD  1 1 
ATOM   2517 N  N   . THR A 1 309 ? 19.259  24.398  7.196  1    70.368  ? 345  THR A N   1 1 
ATOM   2518 C  CA  . THR A 1 309 ? 19.408  25.826  7.376  1    83.759  ? 345  THR A CA  1 1 
ATOM   2519 C  C   . THR A 1 309 ? 19.108  26.537  6.057  1    97.034  ? 345  THR A C   1 1 
ATOM   2520 O  O   . THR A 1 309 ? 19.388  27.725  5.903  1    101.082 ? 345  THR A O   1 1 
ATOM   2521 C  CB  . THR A 1 309 ? 20.824  26.07   7.902  1    81.845  ? 345  THR A CB  1 1 
ATOM   2522 O  OG1 . THR A 1 309 ? 20.536  27.153  8.773  1    80.202  ? 345  THR A OG1 1 1 
ATOM   2523 C  CG2 . THR A 1 309 ? 21.879  26.34   6.835  1    73.754  ? 345  THR A CG2 1 1 
ATOM   2524 N  N   . ASP A 1 310 ? 18.522  25.787  5.116  1    97.645  ? 346  ASP A N   1 1 
ATOM   2525 C  CA  . ASP A 1 310 ? 18.19   26.257  3.777  1    87.258  ? 346  ASP A CA  1 1 
ATOM   2526 C  C   . ASP A 1 310 ? 16.668  26.45   3.655  1    83.484  ? 346  ASP A C   1 1 
ATOM   2527 O  O   . ASP A 1 310 ? 16.132  26.319  2.554  1    90.831  ? 346  ASP A O   1 1 
ATOM   2528 C  CB  . ASP A 1 310 ? 18.851  25.371  2.718  1    84.477  ? 346  ASP A CB  1 1 
ATOM   2529 C  CG  . ASP A 1 310 ? 18.549  23.872  2.811  1    84.056  ? 346  ASP A CG  1 1 
ATOM   2530 O  OD1 . ASP A 1 310 ? 17.51   23.504  3.394  1    77.686  ? 346  ASP A OD1 1 1 
ATOM   2531 O  OD2 . ASP A 1 310 ? 19.359  23.057  2.328  1    85.309  ? 346  ASP A OD2 1 1 
ATOM   2532 N  N   . GLY A 1 311 ? 15.977  26.757  4.775  1    75.351  ? 347  GLY A N   1 1 
ATOM   2533 C  CA  . GLY A 1 311 ? 14.519  26.758  4.84   1    71.46   ? 347  GLY A CA  1 1 
ATOM   2534 C  C   . GLY A 1 311 ? 13.914  25.512  4.173  1    76.412  ? 347  GLY A C   1 1 
ATOM   2535 O  O   . GLY A 1 311 ? 12.994  25.63   3.36   1    83.25   ? 347  GLY A O   1 1 
ATOM   2536 N  N   . ARG A 1 312 ? 14.496  24.33   4.445  1    64.731  ? 348  ARG A N   1 1 
ATOM   2537 C  CA  . ARG A 1 312 ? 13.84   23.048  4.217  1    66.134  ? 348  ARG A CA  1 1 
ATOM   2538 C  C   . ARG A 1 312 ? 13.201  22.6    5.52   1    61.04   ? 348  ARG A C   1 1 
ATOM   2539 O  O   . ARG A 1 312 ? 13.9    22.49   6.513  1    71.284  ? 348  ARG A O   1 1 
ATOM   2540 C  CB  . ARG A 1 312 ? 14.754  21.85   3.914  1    61.367  ? 348  ARG A CB  1 1 
ATOM   2541 C  CG  . ARG A 1 312 ? 14.91   21.541  2.434  1    64.342  ? 348  ARG A CG  1 1 
ATOM   2542 C  CD  . ARG A 1 312 ? 15.557  20.182  2.232  1    63.487  ? 348  ARG A CD  1 1 
ATOM   2543 N  NE  . ARG A 1 312 ? 16.987  20.137  2.569  1    64.279  ? 348  ARG A NE  1 1 
ATOM   2544 C  CZ  . ARG A 1 312 ? 17.585  19.582  3.638  1    60.474  ? 348  ARG A CZ  1 1 
ATOM   2545 N  NH1 . ARG A 1 312 ? 16.908  19.146  4.691  1    58.575  ? 348  ARG A NH1 1 1 
ATOM   2546 N  NH2 . ARG A 1 312 ? 18.902  19.518  3.655  1    57.962  ? 348  ARG A NH2 1 1 
ATOM   2547 N  N   . GLU A 1 313 ? 11.91   22.266  5.478  1    63.206  ? 349  GLU A N   1 1 
ATOM   2548 C  CA  . GLU A 1 313 ? 11.155  21.778  6.63   1    68.838  ? 349  GLU A CA  1 1 
ATOM   2549 C  C   . GLU A 1 313 ? 11.403  20.279  6.906  1    67.334  ? 349  GLU A C   1 1 
ATOM   2550 O  O   . GLU A 1 313 ? 11.462  19.463  5.979  1    68.182  ? 349  GLU A O   1 1 
ATOM   2551 C  CB  . GLU A 1 313 ? 9.675   22.165  6.484  1    72.553  ? 349  GLU A CB  1 1 
ATOM   2552 C  CG  . GLU A 1 313 ? 9.048   22.674  7.783  1    65.7    ? 349  GLU A CG  1 1 
ATOM   2553 C  CD  . GLU A 1 313 ? 10.032  23.701  8.307  1    72.478  ? 349  GLU A CD  1 1 
ATOM   2554 O  OE1 . GLU A 1 313 ? 10.62   24.438  7.475  1    75.796  ? 349  GLU A OE1 1 1 
ATOM   2555 O  OE2 . GLU A 1 313 ? 10.24   23.747  9.535  1    73.564  ? 349  GLU A OE2 1 1 
ATOM   2556 N  N   . VAL A 1 314 ? 11.528  19.913  8.207  1    57.551  ? 350  VAL A N   1 1 
ATOM   2557 C  CA  . VAL A 1 314 ? 12.005  18.599  8.637  1    50.151  ? 350  VAL A CA  1 1 
ATOM   2558 C  C   . VAL A 1 314 ? 11.311  18.216  9.943  1    46.074  ? 350  VAL A C   1 1 
ATOM   2559 O  O   . VAL A 1 314 ? 10.97   19.114  10.688 1    45.182  ? 350  VAL A O   1 1 
ATOM   2560 C  CB  . VAL A 1 314 ? 13.539  18.532  8.823  1    48.392  ? 350  VAL A CB  1 1 
ATOM   2561 C  CG1 . VAL A 1 314 ? 14.333  19.132  7.656  1    47.969  ? 350  VAL A CG1 1 1 
ATOM   2562 C  CG2 . VAL A 1 314 ? 13.946  19.083  10.188 1    45.686  ? 350  VAL A CG2 1 1 
ATOM   2563 N  N   . VAL A 1 315 ? 11.117  16.897  10.211 1    50.538  ? 351  VAL A N   1 1 
ATOM   2564 C  CA  . VAL A 1 315 ? 10.603  16.361  11.482 1    49.372  ? 351  VAL A CA  1 1 
ATOM   2565 C  C   . VAL A 1 315 ? 11.785  16.281  12.465 1    50.062  ? 351  VAL A C   1 1 
ATOM   2566 O  O   . VAL A 1 315 ? 12.884  15.885  12.039 1    43.902  ? 351  VAL A O   1 1 
ATOM   2567 C  CB  . VAL A 1 315 ? 9.953   14.968  11.225 1    56.596  ? 351  VAL A CB  1 1 
ATOM   2568 C  CG1 . VAL A 1 315 ? 9.225   14.367  12.436 1    42.15   ? 351  VAL A CG1 1 1 
ATOM   2569 C  CG2 . VAL A 1 315 ? 9.047   14.982  9.984  1    57.976  ? 351  VAL A CG2 1 1 
ATOM   2570 N  N   . CYS A 1 316 ? 11.59   16.66   13.763 1    54.55   ? 352  CYS A N   1 1 
ATOM   2571 C  CA  . CYS A 1 316 ? 12.744  16.934  14.629 1    50.18   ? 352  CYS A CA  1 1 
ATOM   2572 C  C   . CYS A 1 316 ? 13.23   15.774  15.487 1    52.756  ? 352  CYS A C   1 1 
ATOM   2573 O  O   . CYS A 1 316 ? 14.442  15.531  15.491 1    53.503  ? 352  CYS A O   1 1 
ATOM   2574 C  CB  . CYS A 1 316 ? 12.773  18.261  15.375 1    46.44   ? 352  CYS A CB  1 1 
ATOM   2575 S  SG  . CYS A 1 316 ? 13.662  19.544  14.437 1    59.348  ? 352  CYS A SG  1 1 
ATOM   2576 N  N   . HIS A 1 317 ? 12.308  15.118  16.212 1    43.388  ? 353  HIS A N   1 1 
ATOM   2577 C  CA  . HIS A 1 317 ? 12.54   13.835  16.877 1    42.301  ? 353  HIS A CA  1 1 
ATOM   2578 C  C   . HIS A 1 317 ? 13.707  13.036  16.276 1    42.713  ? 353  HIS A C   1 1 
ATOM   2579 O  O   . HIS A 1 317 ? 13.764  12.745  15.061 1    46.348  ? 353  HIS A O   1 1 
ATOM   2580 C  CB  . HIS A 1 317 ? 11.268  12.99   16.924 1    34.51   ? 353  HIS A CB  1 1 
ATOM   2581 C  CG  . HIS A 1 317 ? 11.247  12.27   18.211 1    29.423  ? 353  HIS A CG  1 1 
ATOM   2582 N  ND1 . HIS A 1 317 ? 10.518  12.707  19.291 1    32.839  ? 353  HIS A ND1 1 1 
ATOM   2583 C  CD2 . HIS A 1 317 ? 11.852  11.17   18.611 1    34.449  ? 353  HIS A CD2 1 1 
ATOM   2584 C  CE1 . HIS A 1 317 ? 10.702  11.923  20.339 1    28.717  ? 353  HIS A CE1 1 1 
ATOM   2585 N  NE2 . HIS A 1 317 ? 11.481  10.935  19.932 1    34.029  ? 353  HIS A NE2 1 1 
ATOM   2586 N  N   . ALA A 1 318 ? 14.681  12.765  17.15  1    39.494  ? 354  ALA A N   1 1 
ATOM   2587 C  CA  . ALA A 1 318 ? 15.831  11.926  16.841 1    38.864  ? 354  ALA A CA  1 1 
ATOM   2588 C  C   . ALA A 1 318 ? 15.331  10.544  16.404 1    35.621  ? 354  ALA A C   1 1 
ATOM   2589 O  O   . ALA A 1 318 ? 14.453  9.982   17.063 1    33.108  ? 354  ALA A O   1 1 
ATOM   2590 C  CB  . ALA A 1 318 ? 16.675  11.809  18.1   1    33.31   ? 354  ALA A CB  1 1 
ATOM   2591 N  N   . SER A 1 319 ? 15.862  10.038  15.271 1    33.99   ? 355  SER A N   1 1 
ATOM   2592 C  CA  . SER A 1 319 ? 15.53   8.706   14.81  1    29.85   ? 355  SER A CA  1 1 
ATOM   2593 C  C   . SER A 1 319 ? 16.655  8.182   13.917 1    34.104  ? 355  SER A C   1 1 
ATOM   2594 O  O   . SER A 1 319 ? 17.427  8.972   13.306 1    31.528  ? 355  SER A O   1 1 
ATOM   2595 C  CB  . SER A 1 319 ? 14.154  8.715   14.169 1    29.206  ? 355  SER A CB  1 1 
ATOM   2596 O  OG  . SER A 1 319 ? 14.247  9.401   12.918 1    37.366  ? 355  SER A OG  1 1 
ATOM   2597 N  N   . ALA A 1 320 ? 16.788  6.84    13.926 1    31.687  ? 356  ALA A N   1 1 
ATOM   2598 C  CA  . ALA A 1 320 ? 17.806  6.091   13.2   1    29.852  ? 356  ALA A CA  1 1 
ATOM   2599 C  C   . ALA A 1 320 ? 17.106  5.293   12.108 1    30.438  ? 356  ALA A C   1 1 
ATOM   2600 O  O   . ALA A 1 320 ? 16      4.837   12.325 1    35.118  ? 356  ALA A O   1 1 
ATOM   2601 C  CB  . ALA A 1 320 ? 18.5    5.196   14.182 1    28.697  ? 356  ALA A CB  1 1 
ATOM   2602 N  N   . TRP A 1 321 ? 17.739  5.137   10.954 1    29.75   ? 357  TRP A N   1 1 
ATOM   2603 C  CA  . TRP A 1 321 ? 17.073  4.711   9.74   1    32.476  ? 357  TRP A CA  1 1 
ATOM   2604 C  C   . TRP A 1 321 ? 17.895  3.631   9.033  1    32.327  ? 357  TRP A C   1 1 
ATOM   2605 O  O   . TRP A 1 321 ? 19.051  3.817   8.688  1    30.975  ? 357  TRP A O   1 1 
ATOM   2606 C  CB  . TRP A 1 321 ? 16.935  5.952   8.833  1    35.422  ? 357  TRP A CB  1 1 
ATOM   2607 C  CG  . TRP A 1 321 ? 15.863  6.921   9.263  1    35.424  ? 357  TRP A CG  1 1 
ATOM   2608 C  CD1 . TRP A 1 321 ? 15.812  7.717   10.369 1    36.239  ? 357  TRP A CD1 1 1 
ATOM   2609 C  CD2 . TRP A 1 321 ? 14.661  7.208   8.509  1    38.397  ? 357  TRP A CD2 1 1 
ATOM   2610 N  NE1 . TRP A 1 321 ? 14.624  8.414   10.414 1    40.728  ? 357  TRP A NE1 1 1 
ATOM   2611 C  CE2 . TRP A 1 321 ? 13.905  8.136   9.274  1    42.109  ? 357  TRP A CE2 1 1 
ATOM   2612 C  CE3 . TRP A 1 321 ? 14.161  6.757   7.278  1    40.236  ? 357  TRP A CE3 1 1 
ATOM   2613 C  CZ2 . TRP A 1 321 ? 12.661  8.615   8.836  1    43.81   ? 357  TRP A CZ2 1 1 
ATOM   2614 C  CZ3 . TRP A 1 321 ? 12.94   7.234   6.838  1    46.085  ? 357  TRP A CZ3 1 1 
ATOM   2615 C  CH2 . TRP A 1 321 ? 12.191  8.125   7.63   1    51.238  ? 357  TRP A CH2 1 1 
ATOM   2616 N  N   . ASP A 1 322 ? 17.276  2.476   8.802  1    33.038  ? 358  ASP A N   1 1 
ATOM   2617 C  CA  . ASP A 1 322 ? 17.814  1.419   7.959  1    34.853  ? 358  ASP A CA  1 1 
ATOM   2618 C  C   . ASP A 1 322 ? 17.059  1.447   6.621  1    33.821  ? 358  ASP A C   1 1 
ATOM   2619 O  O   . ASP A 1 322 ? 15.818  1.472   6.598  1    34.765  ? 358  ASP A O   1 1 
ATOM   2620 C  CB  . ASP A 1 322 ? 17.643  0.081   8.678  1    32.33   ? 358  ASP A CB  1 1 
ATOM   2621 C  CG  . ASP A 1 322 ? 18.318  -1.116  8.045  1    33.127  ? 358  ASP A CG  1 1 
ATOM   2622 O  OD1 . ASP A 1 322 ? 18.845  -0.935  6.929  1    35.95   ? 358  ASP A OD1 1 1 
ATOM   2623 O  OD2 . ASP A 1 322 ? 18.341  -2.203  8.686  1    32.606  ? 358  ASP A OD2 1 1 
ATOM   2624 N  N   . PHE A 1 323 ? 17.807  1.371   5.53   1    33.399  ? 359  PHE A N   1 1 
ATOM   2625 C  CA  . PHE A 1 323 ? 17.264  1.485   4.177  1    37.003  ? 359  PHE A CA  1 1 
ATOM   2626 C  C   . PHE A 1 323 ? 17.261  0.133   3.495  1    36.959  ? 359  PHE A C   1 1 
ATOM   2627 O  O   . PHE A 1 323 ? 17.016  0.106   2.295  1    37.911  ? 359  PHE A O   1 1 
ATOM   2628 C  CB  . PHE A 1 323 ? 17.995  2.44    3.206  1    36.382  ? 359  PHE A CB  1 1 
ATOM   2629 C  CG  . PHE A 1 323 ? 17.754  3.85    3.709  1    36.111  ? 359  PHE A CG  1 1 
ATOM   2630 C  CD1 . PHE A 1 323 ? 18.45   4.334   4.805  1    35.249  ? 359  PHE A CD1 1 1 
ATOM   2631 C  CD2 . PHE A 1 323 ? 16.772  4.654   3.148  1    41.874  ? 359  PHE A CD2 1 1 
ATOM   2632 C  CE1 . PHE A 1 323 ? 18.191  5.589   5.324  1    36.473  ? 359  PHE A CE1 1 1 
ATOM   2633 C  CE2 . PHE A 1 323 ? 16.495  5.909   3.686  1    42.403  ? 359  PHE A CE2 1 1 
ATOM   2634 C  CZ  . PHE A 1 323 ? 17.212  6.382   4.771  1    41.59   ? 359  PHE A CZ  1 1 
ATOM   2635 N  N   . TYR A 1 324 ? 17.614  -0.941  4.23   1    33.907  ? 360  TYR A N   1 1 
ATOM   2636 C  CA  . TYR A 1 324 ? 17.374  -2.292  3.751  1    36.09   ? 360  TYR A CA  1 1 
ATOM   2637 C  C   . TYR A 1 324 ? 18.209  -2.602  2.521  1    38.675  ? 360  TYR A C   1 1 
ATOM   2638 O  O   . TYR A 1 324 ? 17.86   -3.464  1.738  1    41.69   ? 360  TYR A O   1 1 
ATOM   2639 C  CB  . TYR A 1 324 ? 15.876  -2.453  3.427  1    40.194  ? 360  TYR A CB  1 1 
ATOM   2640 C  CG  . TYR A 1 324 ? 15.118  -2.395  4.737  1    37.359  ? 360  TYR A CG  1 1 
ATOM   2641 C  CD1 . TYR A 1 324 ? 15.323  -3.406  5.68   1    41.918  ? 360  TYR A CD1 1 1 
ATOM   2642 C  CD2 . TYR A 1 324 ? 14.33   -1.298  5.072  1    37.362  ? 360  TYR A CD2 1 1 
ATOM   2643 C  CE1 . TYR A 1 324 ? 14.733  -3.338  6.933  1    45.849  ? 360  TYR A CE1 1 1 
ATOM   2644 C  CE2 . TYR A 1 324 ? 13.716  -1.23   6.309  1    42.231  ? 360  TYR A CE2 1 1 
ATOM   2645 C  CZ  . TYR A 1 324 ? 13.948  -2.234  7.239  1    45.818  ? 360  TYR A CZ  1 1 
ATOM   2646 O  OH  . TYR A 1 324 ? 13.371  -2.215  8.467  1    62.787  ? 360  TYR A OH  1 1 
ATOM   2647 N  N   . ASN A 1 325 ? 19.332  -1.926  2.35   1    39.025  ? 361  ASN A N   1 1 
ATOM   2648 C  CA  . ASN A 1 325 ? 20.198  -2.343  1.26   1    44.281  ? 361  ASN A CA  1 1 
ATOM   2649 C  C   . ASN A 1 325 ? 21.558  -2.746  1.815  1    41.269  ? 361  ASN A C   1 1 
ATOM   2650 O  O   . ASN A 1 325 ? 22.444  -2.949  1.015  1    41.742  ? 361  ASN A O   1 1 
ATOM   2651 C  CB  . ASN A 1 325 ? 20.412  -1.255  0.206  1    42.725  ? 361  ASN A CB  1 1 
ATOM   2652 C  CG  . ASN A 1 325 ? 21.212  -0.102  0.773  1    47.096  ? 361  ASN A CG  1 1 
ATOM   2653 O  OD1 . ASN A 1 325 ? 21.633  -0.145  1.954  1    44.2    ? 361  ASN A OD1 1 1 
ATOM   2654 N  ND2 . ASN A 1 325 ? 21.389  0.936   -0.036 1    44.796  ? 361  ASN A ND2 1 1 
ATOM   2655 N  N   . GLY A 1 326 ? 21.732  -2.758  3.143  1    38.983  ? 362  GLY A N   1 1 
ATOM   2656 C  CA  . GLY A 1 326 ? 22.951  -3.251  3.767  1    37.049  ? 362  GLY A CA  1 1 
ATOM   2657 C  C   . GLY A 1 326 ? 24.124  -2.278  3.683  1    39.026  ? 362  GLY A C   1 1 
ATOM   2658 O  O   . GLY A 1 326 ? 25.243  -2.66   3.994  1    39.675  ? 362  GLY A O   1 1 
ATOM   2659 N  N   . LYS A 1 327 ? 23.888  -1.021  3.271  1    40.433  ? 363  LYS A N   1 1 
ATOM   2660 C  CA  . LYS A 1 327 ? 25.008  -0.108  3.072  1    42.234  ? 363  LYS A CA  1 1 
ATOM   2661 C  C   . LYS A 1 327 ? 24.64   1.351   3.401  1    41.876  ? 363  LYS A C   1 1 
ATOM   2662 O  O   . LYS A 1 327 ? 25.498  2.141   3.81   1    41.504  ? 363  LYS A O   1 1 
ATOM   2663 C  CB  . LYS A 1 327 ? 25.74   -0.387  1.755  1    45.017  ? 363  LYS A CB  1 1 
ATOM   2664 C  CG  . LYS A 1 327 ? 24.985  -0.35   0.486  1    45.636  ? 363  LYS A CG  1 1 
ATOM   2665 C  CD  . LYS A 1 327 ? 26.035  -0.768  -0.521 1    55.046  ? 363  LYS A CD  1 1 
ATOM   2666 C  CE  . LYS A 1 327 ? 25.484  -1.503  -1.719 1    60.702  ? 363  LYS A CE  1 1 
ATOM   2667 N  NZ  . LYS A 1 327 ? 24.574  -0.706  -2.55  1    67.326  ? 363  LYS A NZ  1 1 
ATOM   2668 N  N   . ASP A 1 328 ? 23.347  1.684   3.334  1    38.385  ? 364  ASP A N   1 1 
ATOM   2669 C  CA  . ASP A 1 328 ? 22.839  3.024   3.601  1    37.766  ? 364  ASP A CA  1 1 
ATOM   2670 C  C   . ASP A 1 328 ? 22.096  3.076   4.943  1    38.134  ? 364  ASP A C   1 1 
ATOM   2671 O  O   . ASP A 1 328 ? 20.976  2.561   5.099  1    38.38   ? 364  ASP A O   1 1 
ATOM   2672 C  CB  . ASP A 1 328 ? 22.04   3.517   2.406  1    40.126  ? 364  ASP A CB  1 1 
ATOM   2673 C  CG  . ASP A 1 328 ? 21.46   4.928   2.474  1    46.01   ? 364  ASP A CG  1 1 
ATOM   2674 O  OD1 . ASP A 1 328 ? 21.64   5.641   3.519  1    42.309  ? 364  ASP A OD1 1 1 
ATOM   2675 O  OD2 . ASP A 1 328 ? 20.778  5.298   1.483  1    45.223  ? 364  ASP A OD2 1 1 
ATOM   2676 N  N   . PHE A 1 329 ? 22.72   3.742   5.916  1    36.498  ? 365  PHE A N   1 1 
ATOM   2677 C  CA  . PHE A 1 329 ? 22.134  3.873   7.248  1    35.362  ? 365  PHE A CA  1 1 
ATOM   2678 C  C   . PHE A 1 329 ? 22.264  5.32    7.701  1    35.212  ? 365  PHE A C   1 1 
ATOM   2679 O  O   . PHE A 1 329 ? 23.266  5.972   7.408  1    40.396  ? 365  PHE A O   1 1 
ATOM   2680 C  CB  . PHE A 1 329 ? 23      3.079   8.227  1    34.951  ? 365  PHE A CB  1 1 
ATOM   2681 C  CG  . PHE A 1 329 ? 23.22   1.638   7.797  1    36.724  ? 365  PHE A CG  1 1 
ATOM   2682 C  CD1 . PHE A 1 329 ? 22.239  0.679   8.013  1    34.687  ? 365  PHE A CD1 1 1 
ATOM   2683 C  CD2 . PHE A 1 329 ? 24.419  1.253   7.201  1    34.831  ? 365  PHE A CD2 1 1 
ATOM   2684 C  CE1 . PHE A 1 329 ? 22.452  -0.634  7.641  1    36.942  ? 365  PHE A CE1 1 1 
ATOM   2685 C  CE2 . PHE A 1 329 ? 24.627  -0.064  6.849  1    36.089  ? 365  PHE A CE2 1 1 
ATOM   2686 C  CZ  . PHE A 1 329 ? 23.644  -0.997  7.034  1    36.191  ? 365  PHE A CZ  1 1 
ATOM   2687 N  N   . ARG A 1 330 ? 21.255  5.828   8.397  1    33.996  ? 366  ARG A N   1 1 
ATOM   2688 C  CA  . ARG A 1 330 ? 21.199  7.271   8.6    1    36.171  ? 366  ARG A CA  1 1 
ATOM   2689 C  C   . ARG A 1 330 ? 20.579  7.618   9.948  1    32.52   ? 366  ARG A C   1 1 
ATOM   2690 O  O   . ARG A 1 330 ? 19.692  6.931   10.454 1    34.203  ? 366  ARG A O   1 1 
ATOM   2691 C  CB  . ARG A 1 330 ? 20.44   8.065   7.525  1    34.543  ? 366  ARG A CB  1 1 
ATOM   2692 C  CG  . ARG A 1 330 ? 21.025  7.846   6.144  1    37.394  ? 366  ARG A CG  1 1 
ATOM   2693 C  CD  . ARG A 1 330 ? 20.097  8.587   5.204  1    40.071  ? 366  ARG A CD  1 1 
ATOM   2694 N  NE  . ARG A 1 330 ? 20.104  8.02    3.86   1    41.655  ? 366  ARG A NE  1 1 
ATOM   2695 C  CZ  . ARG A 1 330 ? 19.358  8.457   2.832  1    46.683  ? 366  ARG A CZ  1 1 
ATOM   2696 N  NH1 . ARG A 1 330 ? 18.489  9.447   2.952  1    44.56   ? 366  ARG A NH1 1 1 
ATOM   2697 N  NH2 . ARG A 1 330 ? 19.509  7.893   1.655  1    42.097  ? 366  ARG A NH2 1 1 
ATOM   2698 N  N   . ILE A 1 331 ? 20.981  8.779   10.439 1    32.116  ? 367  ILE A N   1 1 
ATOM   2699 C  CA  . ILE A 1 331 ? 20.321  9.436   11.552 1    32.387  ? 367  ILE A CA  1 1 
ATOM   2700 C  C   . ILE A 1 331 ? 19.781  10.802  11.107 1    36.731  ? 367  ILE A C   1 1 
ATOM   2701 O  O   . ILE A 1 331 ? 20.339  11.519  10.245 1    38.863  ? 367  ILE A O   1 1 
ATOM   2702 C  CB  . ILE A 1 331 ? 21.339  9.537   12.701 1    33.462  ? 367  ILE A CB  1 1 
ATOM   2703 C  CG1 . ILE A 1 331 ? 21.579  8.15    13.34  1    29.732  ? 367  ILE A CG1 1 1 
ATOM   2704 C  CG2 . ILE A 1 331 ? 20.923  10.584  13.727 1    31.16   ? 367  ILE A CG2 1 1 
ATOM   2705 C  CD1 . ILE A 1 331 ? 22.685  8.129   14.425 1    27.893  ? 367  ILE A CD1 1 1 
ATOM   2706 N  N   . LYS A 1 332 ? 18.624  11.106  11.679 1    36.463  ? 368  LYS A N   1 1 
ATOM   2707 C  CA  . LYS A 1 332 ? 17.973  12.38   11.551 1    37.093  ? 368  LYS A CA  1 1 
ATOM   2708 C  C   . LYS A 1 332 ? 17.753  12.89   12.962 1    39.41   ? 368  LYS A C   1 1 
ATOM   2709 O  O   . LYS A 1 332 ? 16.949  12.352  13.725 1    38.647  ? 368  LYS A O   1 1 
ATOM   2710 C  CB  . LYS A 1 332 ? 16.608  12.137  10.892 1    39.628  ? 368  LYS A CB  1 1 
ATOM   2711 C  CG  . LYS A 1 332 ? 15.701  13.351  10.837 1    41.517  ? 368  LYS A CG  1 1 
ATOM   2712 C  CD  . LYS A 1 332 ? 14.376  13.075  10.144 1    43.735  ? 368  LYS A CD  1 1 
ATOM   2713 C  CE  . LYS A 1 332 ? 13.381  12.281  10.932 1    38.754  ? 368  LYS A CE  1 1 
ATOM   2714 N  NZ  . LYS A 1 332 ? 13.353  12.553  12.363 1    41.106  ? 368  LYS A NZ  1 1 
ATOM   2715 N  N   . GLN A 1 333 ? 18.469  13.958  13.297 1    38.141  ? 369  GLN A N   1 1 
ATOM   2716 C  CA  . GLN A 1 333 ? 18.292  14.553  14.603 1    36.609  ? 369  GLN A CA  1 1 
ATOM   2717 C  C   . GLN A 1 333 ? 18.512  16.063  14.494 1    37.517  ? 369  GLN A C   1 1 
ATOM   2718 O  O   . GLN A 1 333 ? 19.488  16.527  13.917 1    38.566  ? 369  GLN A O   1 1 
ATOM   2719 C  CB  . GLN A 1 333 ? 19.293  13.89   15.55  1    36.679  ? 369  GLN A CB  1 1 
ATOM   2720 C  CG  . GLN A 1 333 ? 19.265  14.423  16.972 1    37.029  ? 369  GLN A CG  1 1 
ATOM   2721 C  CD  . GLN A 1 333 ? 20.058  13.556  17.931 1    36.549  ? 369  GLN A CD  1 1 
ATOM   2722 O  OE1 . GLN A 1 333 ? 20.39   12.398  17.65  1    35.714  ? 369  GLN A OE1 1 1 
ATOM   2723 N  NE2 . GLN A 1 333 ? 20.313  14.103  19.102 1    37.654  ? 369  GLN A NE2 1 1 
ATOM   2724 N  N   . CYS A 1 334 ? 17.592  16.809  15.085 1    35.196  ? 370  CYS A N   1 1 
ATOM   2725 C  CA  . CYS A 1 334 ? 17.789  18.236  15.249 1    40.5    ? 370  CYS A CA  1 1 
ATOM   2726 C  C   . CYS A 1 334 ? 18.68   18.431  16.489 1    36.926  ? 370  CYS A C   1 1 
ATOM   2727 O  O   . CYS A 1 334 ? 18.186  18.765  17.547 1    38.527  ? 370  CYS A O   1 1 
ATOM   2728 C  CB  . CYS A 1 334 ? 16.386  18.833  15.328 1    40.301  ? 370  CYS A CB  1 1 
ATOM   2729 S  SG  . CYS A 1 334 ? 15.56   19.014  13.709 1    54.007  ? 370  CYS A SG  1 1 
ATOM   2730 N  N   . THR A 1 335 ? 19.971  18.081  16.391 1    39.555  ? 371  THR A N   1 1 
ATOM   2731 C  CA  . THR A 1 335 ? 20.836  17.916  17.558 1    41.414  ? 371  THR A CA  1 1 
ATOM   2732 C  C   . THR A 1 335 ? 21.122  19.309  18.067 1    44.172  ? 371  THR A C   1 1 
ATOM   2733 O  O   . THR A 1 335 ? 21.701  20.062  17.301 1    43.969  ? 371  THR A O   1 1 
ATOM   2734 C  CB  . THR A 1 335 ? 22.209  17.405  17.095 1    42.916  ? 371  THR A CB  1 1 
ATOM   2735 O  OG1 . THR A 1 335 ? 22.108  16.329  16.168 1    40.703  ? 371  THR A OG1 1 1 
ATOM   2736 C  CG2 . THR A 1 335 ? 23.127  17.063  18.257 1    41.57   ? 371  THR A CG2 1 1 
ATOM   2737 N  N   . THR A 1 336 ? 20.738  19.644  19.299 1    48.782  ? 372  THR A N   1 1 
ATOM   2738 C  CA  . THR A 1 336 ? 21.347  20.808  19.912 1    51.548  ? 372  THR A CA  1 1 
ATOM   2739 C  C   . THR A 1 336 ? 22.442  20.383  20.905 1    54.34   ? 372  THR A C   1 1 
ATOM   2740 O  O   . THR A 1 336 ? 22.361  19.31   21.497 1    49.404  ? 372  THR A O   1 1 
ATOM   2741 C  CB  . THR A 1 336 ? 20.302  21.788  20.444 1    58.295  ? 372  THR A CB  1 1 
ATOM   2742 O  OG1 . THR A 1 336 ? 19.648  20.871  21.294 1    42.558  ? 372  THR A OG1 1 1 
ATOM   2743 C  CG2 . THR A 1 336 ? 19.37   22.34   19.366 1    61.04   ? 372  THR A CG2 1 1 
ATOM   2744 N  N   . VAL A 1 337 ? 23.49   21.232  21.016 1    53.242  ? 373  VAL A N   1 1 
ATOM   2745 C  CA  . VAL A 1 337 ? 24.766  20.97   21.673 1    45.756  ? 373  VAL A CA  1 1 
ATOM   2746 C  C   . VAL A 1 337 ? 24.611  21.013  23.204 1    44.699  ? 373  VAL A C   1 1 
ATOM   2747 O  O   . VAL A 1 337 ? 24.784  22.057  23.822 1    45.939  ? 373  VAL A O   1 1 
ATOM   2748 C  CB  . VAL A 1 337 ? 25.882  21.916  21.185 1    40.084  ? 373  VAL A CB  1 1 
ATOM   2749 C  CG1 . VAL A 1 337 ? 27.193  21.657  21.893 1    39.736  ? 373  VAL A CG1 1 1 
ATOM   2750 C  CG2 . VAL A 1 337 ? 26.14   21.838  19.695 1    41.352  ? 373  VAL A CG2 1 1 
ATOM   2751 N  N   . ASN A 1 338 ? 24.361  19.858  23.827 1    40.049  ? 374  ASN A N   1 1 
ATOM   2752 C  CA  . ASN A 1 338 ? 24.339  19.659  25.276 1    43.267  ? 374  ASN A CA  1 1 
ATOM   2753 C  C   . ASN A 1 338 ? 24.484  18.152  25.578 1    48.48   ? 374  ASN A C   1 1 
ATOM   2754 O  O   . ASN A 1 338 ? 24.469  17.356  24.651 1    42.807  ? 374  ASN A O   1 1 
ATOM   2755 C  CB  . ASN A 1 338 ? 23.042  20.155  25.913 1    39.94   ? 374  ASN A CB  1 1 
ATOM   2756 C  CG  . ASN A 1 338 ? 21.802  19.517  25.336 1    48.653  ? 374  ASN A CG  1 1 
ATOM   2757 O  OD1 . ASN A 1 338 ? 21.788  18.319  25.003 1    47.162  ? 374  ASN A OD1 1 1 
ATOM   2758 N  ND2 . ASN A 1 338 ? 20.747  20.304  25.191 1    49.413  ? 374  ASN A ND2 1 1 
ATOM   2759 N  N   . LEU A 1 339 ? 24.526  17.767  26.87  1    43.434  ? 375  LEU A N   1 1 
ATOM   2760 C  CA  . LEU A 1 339 ? 24.789  16.412  27.298 1    41.066  ? 375  LEU A CA  1 1 
ATOM   2761 C  C   . LEU A 1 339 ? 23.581  15.513  27.025 1    43.927  ? 375  LEU A C   1 1 
ATOM   2762 O  O   . LEU A 1 339 ? 23.738  14.362  26.618 1    46.803  ? 375  LEU A O   1 1 
ATOM   2763 C  CB  . LEU A 1 339 ? 25.043  16.537  28.796 1    45.338  ? 375  LEU A CB  1 1 
ATOM   2764 C  CG  . LEU A 1 339 ? 25.264  15.205  29.525 1    47.82   ? 375  LEU A CG  1 1 
ATOM   2765 C  CD1 . LEU A 1 339 ? 26.577  14.536  29.055 1    46.052  ? 375  LEU A CD1 1 1 
ATOM   2766 C  CD2 . LEU A 1 339 ? 25.199  15.352  31.03  1    45.985  ? 375  LEU A CD2 1 1 
ATOM   2767 N  N   . GLU A 1 340 ? 22.368  16.012  27.29  1    41.995  ? 376  GLU A N   1 1 
ATOM   2768 C  CA  . GLU A 1 340 ? 21.175  15.252  26.961 1    46.629  ? 376  GLU A CA  1 1 
ATOM   2769 C  C   . GLU A 1 340 ? 21.192  14.709  25.518 1    47.133  ? 376  GLU A C   1 1 
ATOM   2770 O  O   . GLU A 1 340 ? 20.861  13.538  25.263 1    40.133  ? 376  GLU A O   1 1 
ATOM   2771 C  CB  . GLU A 1 340 ? 19.986  16.152  27.258 1    55.408  ? 376  GLU A CB  1 1 
ATOM   2772 C  CG  . GLU A 1 340 ? 18.685  15.513  26.791 1    62.91   ? 376  GLU A CG  1 1 
ATOM   2773 C  CD  . GLU A 1 340 ? 17.557  15.805  27.756 1    76.765  ? 376  GLU A CD  1 1 
ATOM   2774 O  OE1 . GLU A 1 340 ? 17.675  16.694  28.656 1    69.396  ? 376  GLU A OE1 1 1 
ATOM   2775 O  OE2 . GLU A 1 340 ? 16.56   15.063  27.591 1    67.846  ? 376  GLU A OE2 1 1 
ATOM   2776 N  N   . ASP A 1 341 ? 21.551  15.561  24.556 1    42.588  ? 377  ASP A N   1 1 
ATOM   2777 C  CA  . ASP A 1 341 ? 21.635  15.178  23.155 1    43.13   ? 377  ASP A CA  1 1 
ATOM   2778 C  C   . ASP A 1 341 ? 22.895  14.36   22.842 1    42.705  ? 377  ASP A C   1 1 
ATOM   2779 O  O   . ASP A 1 341 ? 22.949  13.641  21.824 1    35.921  ? 377  ASP A O   1 1 
ATOM   2780 C  CB  . ASP A 1 341 ? 21.436  16.363  22.216 1    48.674  ? 377  ASP A CB  1 1 
ATOM   2781 C  CG  . ASP A 1 341 ? 19.987  16.697  21.878 1    53.833  ? 377  ASP A CG  1 1 
ATOM   2782 O  OD1 . ASP A 1 341 ? 19.074  16.208  22.603 1    55.666  ? 377  ASP A OD1 1 1 
ATOM   2783 O  OD2 . ASP A 1 341 ? 19.774  17.393  20.85  1    63.902  ? 377  ASP A OD2 1 1 
ATOM   2784 N  N   . LEU A 1 342 ? 23.956  14.536  23.639 1    38.975  ? 378  LEU A N   1 1 
ATOM   2785 C  CA  . LEU A 1 342 ? 25.131  13.702  23.427 1    34.487  ? 378  LEU A CA  1 1 
ATOM   2786 C  C   . LEU A 1 342 ? 24.797  12.234  23.744 1    36.882  ? 378  LEU A C   1 1 
ATOM   2787 O  O   . LEU A 1 342 ? 25.261  11.331  23.044 1    32.417  ? 378  LEU A O   1 1 
ATOM   2788 C  CB  . LEU A 1 342 ? 26.264  14.191  24.316 1    36.702  ? 378  LEU A CB  1 1 
ATOM   2789 C  CG  . LEU A 1 342 ? 27.561  13.401  24.155 1    38.207  ? 378  LEU A CG  1 1 
ATOM   2790 C  CD1 . LEU A 1 342 ? 28.025  13.33   22.702 1    39.715  ? 378  LEU A CD1 1 1 
ATOM   2791 C  CD2 . LEU A 1 342 ? 28.616  13.981  25.05  1    38.877  ? 378  LEU A CD2 1 1 
ATOM   2792 N  N   . VAL A 1 343 ? 23.97   12.018  24.787 1    31.551  ? 379  VAL A N   1 1 
ATOM   2793 C  CA  . VAL A 1 343 ? 23.467  10.717  25.158 1    31.002  ? 379  VAL A CA  1 1 
ATOM   2794 C  C   . VAL A 1 343 ? 22.59   10.21   23.999 1    33.121  ? 379  VAL A C   1 1 
ATOM   2795 O  O   . VAL A 1 343 ? 22.813  9.111   23.484 1    29.382  ? 379  VAL A O   1 1 
ATOM   2796 C  CB  . VAL A 1 343 ? 22.765  10.738  26.539 1    32.156  ? 379  VAL A CB  1 1 
ATOM   2797 C  CG1 . VAL A 1 343 ? 22      9.44    26.867 1    29.487  ? 379  VAL A CG1 1 1 
ATOM   2798 C  CG2 . VAL A 1 343 ? 23.758  11.062  27.661 1    31.393  ? 379  VAL A CG2 1 1 
ATOM   2799 N  N   . VAL A 1 344 ? 21.616  11.029  23.557 1    31.671  ? 380  VAL A N   1 1 
ATOM   2800 C  CA  . VAL A 1 344 ? 20.727  10.675  22.452 1    29.612  ? 380  VAL A CA  1 1 
ATOM   2801 C  C   . VAL A 1 344 ? 21.543  10.355  21.187 1    34.92   ? 380  VAL A C   1 1 
ATOM   2802 O  O   . VAL A 1 344 ? 21.241  9.396   20.453 1    32.923  ? 380  VAL A O   1 1 
ATOM   2803 C  CB  . VAL A 1 344 ? 19.682  11.789  22.218 1    28.677  ? 380  VAL A CB  1 1 
ATOM   2804 C  CG1 . VAL A 1 344 ? 18.953  11.639  20.86  1    29.251  ? 380  VAL A CG1 1 1 
ATOM   2805 C  CG2 . VAL A 1 344 ? 18.716  11.925  23.377 1    26.32   ? 380  VAL A CG2 1 1 
ATOM   2806 N  N   . ALA A 1 345 ? 22.618  11.121  20.929 1    30.046  ? 381  ALA A N   1 1 
ATOM   2807 C  CA  . ALA A 1 345 ? 23.464  10.747  19.807 1    32.732  ? 381  ALA A CA  1 1 
ATOM   2808 C  C   . ALA A 1 345 ? 23.956  9.29    19.951 1    34.106  ? 381  ALA A C   1 1 
ATOM   2809 O  O   . ALA A 1 345 ? 24.108  8.56    18.952 1    29.573  ? 381  ALA A O   1 1 
ATOM   2810 C  CB  . ALA A 1 345 ? 24.617  11.747  19.617 1    32.159  ? 381  ALA A CB  1 1 
ATOM   2811 N  N   . HIS A 1 346 ? 24.282  8.872   21.198 1    31.202  ? 382  HIS A N   1 1 
ATOM   2812 C  CA  . HIS A 1 346 ? 24.879  7.545   21.424 1    31.378  ? 382  HIS A CA  1 1 
ATOM   2813 C  C   . HIS A 1 346 ? 23.752  6.523   21.252 1    27.252  ? 382  HIS A C   1 1 
ATOM   2814 O  O   . HIS A 1 346 ? 23.92   5.532   20.557 1    31.247  ? 382  HIS A O   1 1 
ATOM   2815 C  CB  . HIS A 1 346 ? 25.613  7.437   22.782 1    27.511  ? 382  HIS A CB  1 1 
ATOM   2816 C  CG  . HIS A 1 346 ? 26.975  8.058   22.805 1    27.488  ? 382  HIS A CG  1 1 
ATOM   2817 N  ND1 . HIS A 1 346 ? 27.227  9.413   22.931 1    26.826  ? 382  HIS A ND1 1 1 
ATOM   2818 C  CD2 . HIS A 1 346 ? 28.18   7.478   22.667 1    28.729  ? 382  HIS A CD2 1 1 
ATOM   2819 C  CE1 . HIS A 1 346 ? 28.545  9.61    22.911 1    26.891  ? 382  HIS A CE1 1 1 
ATOM   2820 N  NE2 . HIS A 1 346 ? 29.139  8.46    22.737 1    27.905  ? 382  HIS A NE2 1 1 
ATOM   2821 N  N   . HIS A 1 347 ? 22.605  6.817   21.861 1    24.956  ? 383  HIS A N   1 1 
ATOM   2822 C  CA  . HIS A 1 347 ? 21.411  6.039   21.643 1    23.901  ? 383  HIS A CA  1 1 
ATOM   2823 C  C   . HIS A 1 347 ? 21.222  5.719   20.158 1    26.795  ? 383  HIS A C   1 1 
ATOM   2824 O  O   . HIS A 1 347 ? 20.99   4.544   19.776 1    28.958  ? 383  HIS A O   1 1 
ATOM   2825 C  CB  . HIS A 1 347 ? 20.193  6.813   22.149 1    26.288  ? 383  HIS A CB  1 1 
ATOM   2826 C  CG  . HIS A 1 347 ? 18.904  6.039   22.048 1    25.398  ? 383  HIS A CG  1 1 
ATOM   2827 N  ND1 . HIS A 1 347 ? 18.493  5.16    23.027 1    25.635  ? 383  HIS A ND1 1 1 
ATOM   2828 C  CD2 . HIS A 1 347 ? 17.997  5.96    21.09  1    23.399  ? 383  HIS A CD2 1 1 
ATOM   2829 C  CE1 . HIS A 1 347 ? 17.328  4.615   22.679 1    27.685  ? 383  HIS A CE1 1 1 
ATOM   2830 N  NE2 . HIS A 1 347 ? 16.997  5.128   21.496 1    25.543  ? 383  HIS A NE2 1 1 
ATOM   2831 N  N   . GLU A 1 348 ? 21.214  6.773   19.338 1    22.716  ? 384  GLU A N   1 1 
ATOM   2832 C  CA  . GLU A 1 348 ? 20.868  6.657   17.925 1    24.111  ? 384  GLU A CA  1 1 
ATOM   2833 C  C   . GLU A 1 348 ? 21.971  5.877   17.226 1    24.121  ? 384  GLU A C   1 1 
ATOM   2834 O  O   . GLU A 1 348 ? 21.692  5.021   16.434 1    28.54   ? 384  GLU A O   1 1 
ATOM   2835 C  CB  . GLU A 1 348 ? 20.585  7.964   17.174 1    25.066  ? 384  GLU A CB  1 1 
ATOM   2836 C  CG  . GLU A 1 348 ? 19.43   8.729   17.793 1    27.248  ? 384  GLU A CG  1 1 
ATOM   2837 C  CD  . GLU A 1 348 ? 18.075  8.033   17.804 1    32.882  ? 384  GLU A CD  1 1 
ATOM   2838 O  OE1 . GLU A 1 348 ? 17.945  7.091   16.931 1    34.702  ? 384  GLU A OE1 1 1 
ATOM   2839 O  OE2 . GLU A 1 348 ? 17.19   8.391   18.675 1    26.402  ? 384  GLU A OE2 1 1 
ATOM   2840 N  N   . MET A 1 349 ? 23.224  6.085   17.6   1    27.229  ? 385  MET A N   1 1 
ATOM   2841 C  CA  . MET A 1 349 ? 24.331  5.398   16.956 1    27.147  ? 385  MET A CA  1 1 
ATOM   2842 C  C   . MET A 1 349 ? 24.283  3.915   17.341 1    24.376  ? 385  MET A C   1 1 
ATOM   2843 O  O   . MET A 1 349 ? 24.661  3.062   16.557 1    24.861  ? 385  MET A O   1 1 
ATOM   2844 C  CB  . MET A 1 349 ? 25.65   6.085   17.358 1    29.07   ? 385  MET A CB  1 1 
ATOM   2845 C  CG  . MET A 1 349 ? 25.829  7.413   16.624 1    31.669  ? 385  MET A CG  1 1 
ATOM   2846 S  SD  . MET A 1 349 ? 26.344  7.169   14.913 1    32.858  ? 385  MET A SD  1 1 
ATOM   2847 C  CE  . MET A 1 349 ? 28.142  7.005   14.934 1    30.113  ? 385  MET A CE  1 1 
ATOM   2848 N  N   . GLY A 1 350 ? 23.747  3.632   18.517 1    23.374  ? 386  GLY A N   1 1 
ATOM   2849 C  CA  . GLY A 1 350 ? 23.445  2.267   18.944 1    24.637  ? 386  GLY A CA  1 1 
ATOM   2850 C  C   . GLY A 1 350 ? 22.503  1.541   17.966 1    24.612  ? 386  GLY A C   1 1 
ATOM   2851 O  O   . GLY A 1 350 ? 22.73   0.369   17.612 1    22.381  ? 386  GLY A O   1 1 
ATOM   2852 N  N   . HIS A 1 351 ? 21.422  2.226   17.561 1    26.053  ? 387  HIS A N   1 1 
ATOM   2853 C  CA  . HIS A 1 351 ? 20.498  1.677   16.557 1    27.547  ? 387  HIS A CA  1 1 
ATOM   2854 C  C   . HIS A 1 351 ? 21.241  1.447   15.242 1    27.356  ? 387  HIS A C   1 1 
ATOM   2855 O  O   . HIS A 1 351 ? 21.064  0.415   14.593 1    24.77   ? 387  HIS A O   1 1 
ATOM   2856 C  CB  . HIS A 1 351 ? 19.351  2.65    16.252 1    26.252  ? 387  HIS A CB  1 1 
ATOM   2857 C  CG  . HIS A 1 351 ? 18.332  2.741   17.334 1    25.055  ? 387  HIS A CG  1 1 
ATOM   2858 N  ND1 . HIS A 1 351 ? 17.801  1.622   17.951 1    25.702  ? 387  HIS A ND1 1 1 
ATOM   2859 C  CD2 . HIS A 1 351 ? 17.731  3.801   17.91  1    27.233  ? 387  HIS A CD2 1 1 
ATOM   2860 C  CE1 . HIS A 1 351 ? 16.874  1.984   18.862 1    22.96   ? 387  HIS A CE1 1 1 
ATOM   2861 N  NE2 . HIS A 1 351 ? 16.805  3.329   18.852 1    25.347  ? 387  HIS A NE2 1 1 
ATOM   2862 N  N   . ILE A 1 352 ? 22.059  2.423   14.829 1    26.191  ? 388  ILE A N   1 1 
ATOM   2863 C  CA  . ILE A 1 352 ? 22.784  2.224   13.584 1    26.635  ? 388  ILE A CA  1 1 
ATOM   2864 C  C   . ILE A 1 352 ? 23.694  1.003   13.702 1    27.958  ? 388  ILE A C   1 1 
ATOM   2865 O  O   . ILE A 1 352 ? 23.933  0.293   12.718 1    27.946  ? 388  ILE A O   1 1 
ATOM   2866 C  CB  . ILE A 1 352 ? 23.579  3.492   13.228 1    29.759  ? 388  ILE A CB  1 1 
ATOM   2867 C  CG1 . ILE A 1 352 ? 22.625  4.703   13.027 1    30.179  ? 388  ILE A CG1 1 1 
ATOM   2868 C  CG2 . ILE A 1 352 ? 24.484  3.218   12.016 1    29.128  ? 388  ILE A CG2 1 1 
ATOM   2869 C  CD1 . ILE A 1 352 ? 21.68   4.563   11.844 1    33.345  ? 388  ILE A CD1 1 1 
ATOM   2870 N  N   . GLN A 1 353 ? 24.275  0.811   14.901 1    26.55   ? 389  GLN A N   1 1 
ATOM   2871 C  CA  . GLN A 1 353 ? 25.299  -0.216  15.006 1    27.464  ? 389  GLN A CA  1 1 
ATOM   2872 C  C   . GLN A 1 353 ? 24.603  -1.566  14.854 1    26.811  ? 389  GLN A C   1 1 
ATOM   2873 O  O   . GLN A 1 353 ? 25.166  -2.489  14.275 1    27.593  ? 389  GLN A O   1 1 
ATOM   2874 C  CB  . GLN A 1 353 ? 26.004  -0.214  16.38  1    27.717  ? 389  GLN A CB  1 1 
ATOM   2875 C  CG  . GLN A 1 353 ? 27.021  -1.336  16.606 1    25.006  ? 389  GLN A CG  1 1 
ATOM   2876 C  CD  . GLN A 1 353 ? 28.23   -1.205  15.709 1    28.353  ? 389  GLN A CD  1 1 
ATOM   2877 O  OE1 . GLN A 1 353 ? 28.854  -2.202  15.314 1    31.968  ? 389  GLN A OE1 1 1 
ATOM   2878 N  NE2 . GLN A 1 353 ? 28.645  0.03    15.431 1    27.972  ? 389  GLN A NE2 1 1 
ATOM   2879 N  N   . TYR A 1 354 ? 23.403  -1.668  15.438 1    25.992  ? 390  TYR A N   1 1 
ATOM   2880 C  CA  . TYR A 1 354 ? 22.66   -2.915  15.372 1    25.791  ? 390  TYR A CA  1 1 
ATOM   2881 C  C   . TYR A 1 354 ? 22.314  -3.222  13.903 1    26.932  ? 390  TYR A C   1 1 
ATOM   2882 O  O   . TYR A 1 354 ? 22.444  -4.363  13.437 1    25.623  ? 390  TYR A O   1 1 
ATOM   2883 C  CB  . TYR A 1 354 ? 21.475  -2.751  16.333 1    24.47   ? 390  TYR A CB  1 1 
ATOM   2884 C  CG  . TYR A 1 354 ? 21.012  -4.02   17.06  1    23.726  ? 390  TYR A CG  1 1 
ATOM   2885 C  CD1 . TYR A 1 354 ? 21.123  -5.301  16.514 1    24.267  ? 390  TYR A CD1 1 1 
ATOM   2886 C  CD2 . TYR A 1 354 ? 20.574  -3.917  18.379 1    24.3    ? 390  TYR A CD2 1 1 
ATOM   2887 C  CE1 . TYR A 1 354 ? 20.712  -6.423  17.231 1    23.989  ? 390  TYR A CE1 1 1 
ATOM   2888 C  CE2 . TYR A 1 354 ? 20.163  -5.002  19.119 1    22.372  ? 390  TYR A CE2 1 1 
ATOM   2889 C  CZ  . TYR A 1 354 ? 20.258  -6.256  18.543 1    24.354  ? 390  TYR A CZ  1 1 
ATOM   2890 O  OH  . TYR A 1 354 ? 19.783  -7.258  19.332 1    21.638  ? 390  TYR A OH  1 1 
ATOM   2891 N  N   . PHE A 1 355 ? 21.866  -2.221  13.156 1    27.072  ? 391  PHE A N   1 1 
ATOM   2892 C  CA  . PHE A 1 355 ? 21.47   -2.463  11.758 1    29.142  ? 391  PHE A CA  1 1 
ATOM   2893 C  C   . PHE A 1 355 ? 22.64   -2.993  10.945 1    32.014  ? 391  PHE A C   1 1 
ATOM   2894 O  O   . PHE A 1 355 ? 22.463  -3.899  10.117 1    31.883  ? 391  PHE A O   1 1 
ATOM   2895 C  CB  . PHE A 1 355 ? 21.129  -1.159  11.016 1    28.876  ? 391  PHE A CB  1 1 
ATOM   2896 C  CG  . PHE A 1 355 ? 19.957  -0.35   11.584 1    26.451  ? 391  PHE A CG  1 1 
ATOM   2897 C  CD1 . PHE A 1 355 ? 18.906  -0.971  12.239 1    24.923  ? 391  PHE A CD1 1 1 
ATOM   2898 C  CD2 . PHE A 1 355 ? 19.87   1.034   11.366 1    28.246  ? 391  PHE A CD2 1 1 
ATOM   2899 C  CE1 . PHE A 1 355 ? 17.829  -0.226  12.703 1    26.342  ? 391  PHE A CE1 1 1 
ATOM   2900 C  CE2 . PHE A 1 355 ? 18.792  1.769   11.825 1    27.89   ? 391  PHE A CE2 1 1 
ATOM   2901 C  CZ  . PHE A 1 355 ? 17.777  1.149   12.517 1    27.316  ? 391  PHE A CZ  1 1 
ATOM   2902 N  N   . MET A 1 356 ? 23.82   -2.389  11.181 1    29.671  ? 392  MET A N   1 1 
ATOM   2903 C  CA  . MET A 1 356 ? 25.036  -2.84   10.522 1    33.022  ? 392  MET A CA  1 1 
ATOM   2904 C  C   . MET A 1 356 ? 25.444  -4.276  10.922 1    31.573  ? 392  MET A C   1 1 
ATOM   2905 O  O   . MET A 1 356 ? 25.887  -5.057  10.068 1    30.875  ? 392  MET A O   1 1 
ATOM   2906 C  CB  . MET A 1 356 ? 26.221  -1.85   10.68  1    31.838  ? 392  MET A CB  1 1 
ATOM   2907 C  CG  . MET A 1 356 ? 25.982  -0.418  10.201 1    31.653  ? 392  MET A CG  1 1 
ATOM   2908 S  SD  . MET A 1 356 ? 27.533  0.52    10.219 1    31.894  ? 392  MET A SD  1 1 
ATOM   2909 C  CE  . MET A 1 356 ? 27.958  0.515   11.987 1    28.651  ? 392  MET A CE  1 1 
ATOM   2910 N  N   . GLN A 1 357 ? 25.319  -4.647  12.208 1    29.745  ? 393  GLN A N   1 1 
ATOM   2911 C  CA  . GLN A 1 357 ? 25.686  -5.98   12.685 1    29.146  ? 393  GLN A CA  1 1 
ATOM   2912 C  C   . GLN A 1 357 ? 24.794  -7.084  12.075 1    30.367  ? 393  GLN A C   1 1 
ATOM   2913 O  O   . GLN A 1 357 ? 25.276  -8.172  11.752 1    29.285  ? 393  GLN A O   1 1 
ATOM   2914 C  CB  . GLN A 1 357 ? 25.656  -5.932  14.225 1    30.607  ? 393  GLN A CB  1 1 
ATOM   2915 C  CG  . GLN A 1 357 ? 26.83   -5.165  14.868 1    27.146  ? 393  GLN A CG  1 1 
ATOM   2916 C  CD  . GLN A 1 357 ? 28.128  -5.955  14.851 1    31.081  ? 393  GLN A CD  1 1 
ATOM   2917 O  OE1 . GLN A 1 357 ? 28.174  -7.163  14.525 1    29.864  ? 393  GLN A OE1 1 1 
ATOM   2918 N  NE2 . GLN A 1 357 ? 29.231  -5.273  15.178 1    30.684  ? 393  GLN A NE2 1 1 
ATOM   2919 N  N   . TYR A 1 358 ? 23.487  -6.819  11.889 1    27.726  ? 394  TYR A N   1 1 
ATOM   2920 C  CA  . TYR A 1 358 ? 22.58   -7.866  11.403 1    30.848  ? 394  TYR A CA  1 1 
ATOM   2921 C  C   . TYR A 1 358 ? 22.226  -7.768  9.91   1    32.2    ? 394  TYR A C   1 1 
ATOM   2922 O  O   . TYR A 1 358 ? 21.305  -8.455  9.419  1    33.232  ? 394  TYR A O   1 1 
ATOM   2923 C  CB  . TYR A 1 358 ? 21.329  -7.929  12.281 1    27.837  ? 394  TYR A CB  1 1 
ATOM   2924 C  CG  . TYR A 1 358 ? 20.36   -6.76   12.455 1    28.292  ? 394  TYR A CG  1 1 
ATOM   2925 C  CD1 . TYR A 1 358 ? 19.841  -6.076  11.355 1    26.846  ? 394  TYR A CD1 1 1 
ATOM   2926 C  CD2 . TYR A 1 358 ? 19.854  -6.434  13.728 1    25.895  ? 394  TYR A CD2 1 1 
ATOM   2927 C  CE1 . TYR A 1 358 ? 18.898  -5.074  11.528 1    26.261  ? 394  TYR A CE1 1 1 
ATOM   2928 C  CE2 . TYR A 1 358 ? 18.918  -5.416  13.903 1    25.292  ? 394  TYR A CE2 1 1 
ATOM   2929 C  CZ  . TYR A 1 358 ? 18.417  -4.745  12.791 1    24.561  ? 394  TYR A CZ  1 1 
ATOM   2930 O  OH  . TYR A 1 358 ? 17.463  -3.747  12.894 1    24.317  ? 394  TYR A OH  1 1 
ATOM   2931 N  N   . LYS A 1 359 ? 23.019  -6.987  9.169  1    32.786  ? 395  LYS A N   1 1 
ATOM   2932 C  CA  . LYS A 1 359 ? 22.72   -6.649  7.768  1    34.762  ? 395  LYS A CA  1 1 
ATOM   2933 C  C   . LYS A 1 359 ? 22.818  -7.848  6.822  1    34.417  ? 395  LYS A C   1 1 
ATOM   2934 O  O   . LYS A 1 359 ? 22.393  -7.778  5.66   1    34.718  ? 395  LYS A O   1 1 
ATOM   2935 C  CB  . LYS A 1 359 ? 23.598  -5.506  7.238  1    35.924  ? 395  LYS A CB  1 1 
ATOM   2936 C  CG  . LYS A 1 359 ? 25.063  -5.87   7.008  1    39.389  ? 395  LYS A CG  1 1 
ATOM   2937 C  CD  . LYS A 1 359 ? 25.775  -4.664  6.411  1    43.552  ? 395  LYS A CD  1 1 
ATOM   2938 C  CE  . LYS A 1 359 ? 26.703  -5.232  5.388  1    52.959  ? 395  LYS A CE  1 1 
ATOM   2939 N  NZ  . LYS A 1 359 ? 27.907  -5.369  6.197  1    53.755  ? 395  LYS A NZ  1 1 
ATOM   2940 N  N   . ASP A 1 360 ? 23.376  -8.964  7.292  1    37.174  ? 396  ASP A N   1 1 
ATOM   2941 C  CA  . ASP A 1 360 ? 23.465  -10.081 6.371  1    42.695  ? 396  ASP A CA  1 1 
ATOM   2942 C  C   . ASP A 1 360 ? 22.329  -11.082 6.531  1    43.453  ? 396  ASP A C   1 1 
ATOM   2943 O  O   . ASP A 1 360 ? 22.157  -11.949 5.676  1    54.627  ? 396  ASP A O   1 1 
ATOM   2944 C  CB  . ASP A 1 360 ? 24.883  -10.579 6.189  1    50.8    ? 396  ASP A CB  1 1 
ATOM   2945 C  CG  . ASP A 1 360 ? 25.745  -9.576  5.425  1    65.46   ? 396  ASP A CG  1 1 
ATOM   2946 O  OD1 . ASP A 1 360 ? 25.267  -9.043  4.369  1    72.127  ? 396  ASP A OD1 1 1 
ATOM   2947 O  OD2 . ASP A 1 360 ? 26.874  -9.302  5.902  1    66.107  ? 396  ASP A OD2 1 1 
ATOM   2948 N  N   . LEU A 1 361 ? 21.527  -10.933 7.576  1    37.035  ? 397  LEU A N   1 1 
ATOM   2949 C  CA  . LEU A 1 361 ? 20.442  -11.874 7.776  1    36.362  ? 397  LEU A CA  1 1 
ATOM   2950 C  C   . LEU A 1 361 ? 19.404  -11.597 6.717  1    36.583  ? 397  LEU A C   1 1 
ATOM   2951 O  O   . LEU A 1 361 ? 19.296  -10.455 6.291  1    36.787  ? 397  LEU A O   1 1 
ATOM   2952 C  CB  . LEU A 1 361 ? 19.808  -11.551 9.13   1    34.399  ? 397  LEU A CB  1 1 
ATOM   2953 C  CG  . LEU A 1 361 ? 20.692  -11.8   10.355 1    32.457  ? 397  LEU A CG  1 1 
ATOM   2954 C  CD1 . LEU A 1 361 ? 19.903  -11.786 11.679 1    27.473  ? 397  LEU A CD1 1 1 
ATOM   2955 C  CD2 . LEU A 1 361 ? 21.461  -13.083 10.182 1    33.065  ? 397  LEU A CD2 1 1 
ATOM   2956 N  N   . PRO A 1 362 ? 18.537  -12.574 6.392  1    36.367  ? 398  PRO A N   1 1 
ATOM   2957 C  CA  . PRO A 1 362 ? 17.254  -12.252 5.737  1    38.399  ? 398  PRO A CA  1 1 
ATOM   2958 C  C   . PRO A 1 362 ? 16.497  -11.077 6.398  1    36.8    ? 398  PRO A C   1 1 
ATOM   2959 O  O   . PRO A 1 362 ? 16.424  -10.957 7.618  1    32.526  ? 398  PRO A O   1 1 
ATOM   2960 C  CB  . PRO A 1 362 ? 16.46   -13.591 5.756  1    34.479  ? 398  PRO A CB  1 1 
ATOM   2961 C  CG  . PRO A 1 362 ? 17.261  -14.443 6.686  1    33.692  ? 398  PRO A CG  1 1 
ATOM   2962 C  CD  . PRO A 1 362 ? 18.711  -13.996 6.714  1    33.701  ? 398  PRO A CD  1 1 
ATOM   2963 N  N   . VAL A 1 363 ? 15.873  -10.225 5.571  1    35.644  ? 399  VAL A N   1 1 
ATOM   2964 C  CA  . VAL A 1 363 ? 15.254  -9.008  6.063  1    35.834  ? 399  VAL A CA  1 1 
ATOM   2965 C  C   . VAL A 1 363 ? 14.216  -9.33   7.144  1    32.647  ? 399  VAL A C   1 1 
ATOM   2966 O  O   . VAL A 1 363 ? 14.071  -8.542  8.055  1    32.443  ? 399  VAL A O   1 1 
ATOM   2967 C  CB  . VAL A 1 363 ? 14.737  -7.953  5.042  1    41.967  ? 399  VAL A CB  1 1 
ATOM   2968 C  CG1 . VAL A 1 363 ? 15.537  -7.89   3.749  1    41.413  ? 399  VAL A CG1 1 1 
ATOM   2969 C  CG2 . VAL A 1 363 ? 13.29   -8.169  4.656  1    43.637  ? 399  VAL A CG2 1 1 
ATOM   2970 N  N   . ALA A 1 364 ? 13.504  -10.461 7.113  1    32.377  ? 400  ALA A N   1 1 
ATOM   2971 C  CA  . ALA A 1 364 ? 12.472  -10.724 8.125  1    30.001  ? 400  ALA A CA  1 1 
ATOM   2972 C  C   . ALA A 1 364 ? 13.082  -10.885 9.507  1    29.82   ? 400  ALA A C   1 1 
ATOM   2973 O  O   . ALA A 1 364 ? 12.396  -10.775 10.518 1    36.251  ? 400  ALA A O   1 1 
ATOM   2974 C  CB  . ALA A 1 364 ? 11.689  -11.99  7.79   1    32.264  ? 400  ALA A CB  1 1 
ATOM   2975 N  N   . LEU A 1 365 ? 14.401  -11.091 9.555  1    32.832  ? 401  LEU A N   1 1 
ATOM   2976 C  CA  . LEU A 1 365 ? 15.145  -11.313 10.788 1    29.891  ? 401  LEU A CA  1 1 
ATOM   2977 C  C   . LEU A 1 365 ? 15.977  -10.073 11.125 1    30.119  ? 401  LEU A C   1 1 
ATOM   2978 O  O   . LEU A 1 365 ? 16.594  -10.037 12.197 1    27.945  ? 401  LEU A O   1 1 
ATOM   2979 C  CB  . LEU A 1 365 ? 15.99   -12.589 10.615 1    31.942  ? 401  LEU A CB  1 1 
ATOM   2980 C  CG  . LEU A 1 365 ? 15.148  -13.827 10.222 1    32.485  ? 401  LEU A CG  1 1 
ATOM   2981 C  CD1 . LEU A 1 365 ? 15.976  -15.081 10.148 1    34.735  ? 401  LEU A CD1 1 1 
ATOM   2982 C  CD2 . LEU A 1 365 ? 13.909  -14.047 11.133 1    30.082  ? 401  LEU A CD2 1 1 
ATOM   2983 N  N   . ARG A 1 366 ? 15.957  -9.05   10.254 1    26.939  ? 402  ARG A N   1 1 
ATOM   2984 C  CA  . ARG A 1 366 ? 16.683  -7.812  10.532 1    30.599  ? 402  ARG A CA  1 1 
ATOM   2985 C  C   . ARG A 1 366 ? 15.97   -6.974  11.6   1    27.485  ? 402  ARG A C   1 1 
ATOM   2986 O  O   . ARG A 1 366 ? 15.49   -5.884  11.334 1    32.996  ? 402  ARG A O   1 1 
ATOM   2987 C  CB  . ARG A 1 366 ? 16.94   -6.988  9.265  1    29.414  ? 402  ARG A CB  1 1 
ATOM   2988 C  CG  . ARG A 1 366 ? 18.111  -7.589  8.519  1    35.163  ? 402  ARG A CG  1 1 
ATOM   2989 C  CD  . ARG A 1 366 ? 18.27   -6.709  7.314  1    40.12   ? 402  ARG A CD  1 1 
ATOM   2990 N  NE  . ARG A 1 366 ? 18.764  -7.546  6.231  1    41.733  ? 402  ARG A NE  1 1 
ATOM   2991 C  CZ  . ARG A 1 366 ? 19.065  -7.18   4.997  1    44.014  ? 402  ARG A CZ  1 1 
ATOM   2992 N  NH1 . ARG A 1 366 ? 19.185  -5.899  4.716  1    45.252  ? 402  ARG A NH1 1 1 
ATOM   2993 N  NH2 . ARG A 1 366 ? 19.322  -8.107  4.085  1    40.255  ? 402  ARG A NH2 1 1 
ATOM   2994 N  N   . GLU A 1 367 ? 15.926  -7.461  12.836 1    27.154  ? 403  GLU A N   1 1 
ATOM   2995 C  CA  . GLU A 1 367 ? 15.36   -6.769  13.985 1    25.677  ? 403  GLU A CA  1 1 
ATOM   2996 C  C   . GLU A 1 367 ? 16.203  -7.076  15.21  1    23.275  ? 403  GLU A C   1 1 
ATOM   2997 O  O   . GLU A 1 367 ? 17.003  -7.964  15.18  1    24.66   ? 403  GLU A O   1 1 
ATOM   2998 C  CB  . GLU A 1 367 ? 13.89   -7.142  14.267 1    28.359  ? 403  GLU A CB  1 1 
ATOM   2999 C  CG  . GLU A 1 367 ? 13.042  -7.114  12.995 1    38.109  ? 403  GLU A CG  1 1 
ATOM   3000 C  CD  . GLU A 1 367 ? 11.585  -7.32   13.404 1    49.373  ? 403  GLU A CD  1 1 
ATOM   3001 O  OE1 . GLU A 1 367 ? 11.335  -7.704  14.574 1    55.465  ? 403  GLU A OE1 1 1 
ATOM   3002 O  OE2 . GLU A 1 367 ? 10.685  -7.105  12.576 1    53.347  ? 403  GLU A OE2 1 1 
ATOM   3003 N  N   . GLY A 1 368 ? 15.973  -6.419  16.341 1    27.863  ? 404  GLY A N   1 1 
ATOM   3004 C  CA  . GLY A 1 368 ? 16.771  -6.733  17.524 1    26.993  ? 404  GLY A CA  1 1 
ATOM   3005 C  C   . GLY A 1 368 ? 16.252  -7.985  18.208 1    27.937  ? 404  GLY A C   1 1 
ATOM   3006 O  O   . GLY A 1 368 ? 15.185  -8.475  17.879 1    28.041  ? 404  GLY A O   1 1 
ATOM   3007 N  N   . ALA A 1 369 ? 17.016  -8.549  19.127 1    26.196  ? 405  ALA A N   1 1 
ATOM   3008 C  CA  . ALA A 1 369 ? 16.543  -9.757  19.787 1    25.317  ? 405  ALA A CA  1 1 
ATOM   3009 C  C   . ALA A 1 369 ? 15.119  -9.576  20.326 1    23.512  ? 405  ALA A C   1 1 
ATOM   3010 O  O   . ALA A 1 369 ? 14.285  -10.48  20.234 1    21.018  ? 405  ALA A O   1 1 
ATOM   3011 C  CB  . ALA A 1 369 ? 17.501  -10.159 20.883 1    25.655  ? 405  ALA A CB  1 1 
ATOM   3012 N  N   . ASN A 1 370 ? 14.868  -8.398  20.9   1    22.1    ? 406  ASN A N   1 1 
ATOM   3013 C  CA  . ASN A 1 370 ? 13.533  -7.86   21.18  1    22.927  ? 406  ASN A CA  1 1 
ATOM   3014 C  C   . ASN A 1 370 ? 13.639  -6.338  21.09  1    20.799  ? 406  ASN A C   1 1 
ATOM   3015 O  O   . ASN A 1 370 ? 14.748  -5.848  20.979 1    22.028  ? 406  ASN A O   1 1 
ATOM   3016 C  CB  . ASN A 1 370 ? 12.95   -8.378  22.502 1    22.242  ? 406  ASN A CB  1 1 
ATOM   3017 C  CG  . ASN A 1 370 ? 13.566  -7.795  23.759 1    20.977  ? 406  ASN A CG  1 1 
ATOM   3018 O  OD1 . ASN A 1 370 ? 13.773  -6.571  23.897 1    21.357  ? 406  ASN A OD1 1 1 
ATOM   3019 N  ND2 . ASN A 1 370 ? 13.781  -8.654  24.745 1    20.465  ? 406  ASN A ND2 1 1 
ATOM   3020 N  N   . PRO A 1 371 ? 12.532  -5.545  21.03  1    22.481  ? 407  PRO A N   1 1 
ATOM   3021 C  CA  . PRO A 1 371 ? 12.646  -4.093  20.862 1    20.89   ? 407  PRO A CA  1 1 
ATOM   3022 C  C   . PRO A 1 371 ? 13.493  -3.495  21.976 1    18.541  ? 407  PRO A C   1 1 
ATOM   3023 O  O   . PRO A 1 371 ? 14.199  -2.56   21.714 1    25.284  ? 407  PRO A O   1 1 
ATOM   3024 C  CB  . PRO A 1 371 ? 11.181  -3.555  20.86  1    19.926  ? 407  PRO A CB  1 1 
ATOM   3025 C  CG  . PRO A 1 371 ? 10.398  -4.765  20.365 1    21.599  ? 407  PRO A CG  1 1 
ATOM   3026 C  CD  . PRO A 1 371 ? 11.122  -5.993  20.934 1    21.491  ? 407  PRO A CD  1 1 
ATOM   3027 N  N   . GLY A 1 372 ? 13.49   -4.06   23.185 1    20.298  ? 408  GLY A N   1 1 
ATOM   3028 C  CA  . GLY A 1 372 ? 14.302  -3.488  24.268 1    20.434  ? 408  GLY A CA  1 1 
ATOM   3029 C  C   . GLY A 1 372 ? 15.808  -3.563  23.997 1    21.26   ? 408  GLY A C   1 1 
ATOM   3030 O  O   . GLY A 1 372 ? 16.542  -2.608  24.339 1    19.827  ? 408  GLY A O   1 1 
ATOM   3031 N  N   . PHE A 1 373 ? 16.258  -4.676  23.368 1    19.58   ? 409  PHE A N   1 1 
ATOM   3032 C  CA  . PHE A 1 373 ? 17.671  -4.783  23.025 1    21.812  ? 409  PHE A CA  1 1 
ATOM   3033 C  C   . PHE A 1 373 ? 18.073  -3.673  22.058 1    22.206  ? 409  PHE A C   1 1 
ATOM   3034 O  O   . PHE A 1 373 ? 19.174  -3.088  22.122 1    22.759  ? 409  PHE A O   1 1 
ATOM   3035 C  CB  . PHE A 1 373 ? 17.891  -6.133  22.341 1    21.55   ? 409  PHE A CB  1 1 
ATOM   3036 C  CG  . PHE A 1 373 ? 18.161  -7.253  23.339 1    23.64   ? 409  PHE A CG  1 1 
ATOM   3037 C  CD1 . PHE A 1 373 ? 17.176  -7.619  24.267 1    23.884  ? 409  PHE A CD1 1 1 
ATOM   3038 C  CD2 . PHE A 1 373 ? 19.361  -7.978  23.295 1    27.221  ? 409  PHE A CD2 1 1 
ATOM   3039 C  CE1 . PHE A 1 373 ? 17.403  -8.661  25.148 1    23.74   ? 409  PHE A CE1 1 1 
ATOM   3040 C  CE2 . PHE A 1 373 ? 19.598  -9.01   24.193 1    25.29   ? 409  PHE A CE2 1 1 
ATOM   3041 C  CZ  . PHE A 1 373 ? 18.612  -9.339  25.109 1    26      ? 409  PHE A CZ  1 1 
ATOM   3042 N  N   . HIS A 1 374 ? 17.155  -3.367  21.15  1    22.375  ? 410  HIS A N   1 1 
ATOM   3043 C  CA  . HIS A 1 374 ? 17.521  -2.406  20.121 1    24.075  ? 410  HIS A CA  1 1 
ATOM   3044 C  C   . HIS A 1 374 ? 17.708  -1.039  20.807 1    24.951  ? 410  HIS A C   1 1 
ATOM   3045 O  O   . HIS A 1 374 ? 18.596  -0.264  20.446 1    24.091  ? 410  HIS A O   1 1 
ATOM   3046 C  CB  . HIS A 1 374 ? 16.478  -2.447  18.994 1    21.864  ? 410  HIS A CB  1 1 
ATOM   3047 C  CG  . HIS A 1 374 ? 17.041  -2.242  17.597 1    22.629  ? 410  HIS A CG  1 1 
ATOM   3048 N  ND1 . HIS A 1 374 ? 17.904  -1.22   17.219 1    25.032  ? 410  HIS A ND1 1 1 
ATOM   3049 C  CD2 . HIS A 1 374 ? 16.797  -2.962  16.501 1    22.343  ? 410  HIS A CD2 1 1 
ATOM   3050 C  CE1 . HIS A 1 374 ? 18.2    -1.348  15.895 1    23.752  ? 410  HIS A CE1 1 1 
ATOM   3051 N  NE2 . HIS A 1 374 ? 17.556  -2.466  15.434 1    25.274  ? 410  HIS A NE2 1 1 
ATOM   3052 N  N   . GLU A 1 375 ? 16.89   -0.785  21.842 1    25.992  ? 411  GLU A N   1 1 
ATOM   3053 C  CA  . GLU A 1 375 ? 16.903  0.51    22.511 1    25.869  ? 411  GLU A CA  1 1 
ATOM   3054 C  C   . GLU A 1 375 ? 18.145  0.609   23.397 1    29.769  ? 411  GLU A C   1 1 
ATOM   3055 O  O   . GLU A 1 375 ? 18.635  1.696   23.704 1    29.205  ? 411  GLU A O   1 1 
ATOM   3056 C  CB  . GLU A 1 375 ? 15.605  0.731   23.294 1    21.441  ? 411  GLU A CB  1 1 
ATOM   3057 C  CG  . GLU A 1 375 ? 14.331  0.828   22.453 1    20.662  ? 411  GLU A CG  1 1 
ATOM   3058 C  CD  . GLU A 1 375 ? 14.501  1.89    21.34  1    22.55   ? 411  GLU A CD  1 1 
ATOM   3059 O  OE1 . GLU A 1 375 ? 15.119  2.983   21.563 1    21.673  ? 411  GLU A OE1 1 1 
ATOM   3060 O  OE2 . GLU A 1 375 ? 14.093  1.56    20.182 1    23.081  ? 411  GLU A OE2 1 1 
ATOM   3061 N  N   . ALA A 1 376 ? 18.66   -0.532  23.837 1    26.625  ? 412  ALA A N   1 1 
ATOM   3062 C  CA  . ALA A 1 376 ? 19.622  -0.532  24.937 1    23.17   ? 412  ALA A CA  1 1 
ATOM   3063 C  C   . ALA A 1 376 ? 21.065  -0.269  24.46  1    22.408  ? 412  ALA A C   1 1 
ATOM   3064 O  O   . ALA A 1 376 ? 21.903  0.111   25.247 1    24.161  ? 412  ALA A O   1 1 
ATOM   3065 C  CB  . ALA A 1 376 ? 19.517  -1.902  25.621 1    20.059  ? 412  ALA A CB  1 1 
ATOM   3066 N  N   . ILE A 1 377 ? 21.426  -0.564  23.209 1    24.571  ? 413  ILE A N   1 1 
ATOM   3067 C  CA  . ILE A 1 377 ? 22.821  -0.676  22.78  1    24.725  ? 413  ILE A CA  1 1 
ATOM   3068 C  C   . ILE A 1 377 ? 23.646  0.607   23.034 1    25.675  ? 413  ILE A C   1 1 
ATOM   3069 O  O   . ILE A 1 377 ? 24.734  0.553   23.643 1    24.593  ? 413  ILE A O   1 1 
ATOM   3070 C  CB  . ILE A 1 377 ? 22.95   -1.094  21.298 1    24.267  ? 413  ILE A CB  1 1 
ATOM   3071 C  CG1 . ILE A 1 377 ? 22.263  -2.434  21.016 1    25.788  ? 413  ILE A CG1 1 1 
ATOM   3072 C  CG2 . ILE A 1 377 ? 24.439  -1.136  20.915 1    27.622  ? 413  ILE A CG2 1 1 
ATOM   3073 C  CD1 . ILE A 1 377 ? 22.75   -3.615  21.852 1    25.337  ? 413  ILE A CD1 1 1 
ATOM   3074 N  N   . GLY A 1 378 ? 23.154  1.731   22.47  1    20.528  ? 414  GLY A N   1 1 
ATOM   3075 C  CA  . GLY A 1 378 ? 23.725  3.062   22.601 1    22.803  ? 414  GLY A CA  1 1 
ATOM   3076 C  C   . GLY A 1 378 ? 23.776  3.513   24.06  1    23.784  ? 414  GLY A C   1 1 
ATOM   3077 O  O   . GLY A 1 378 ? 24.782  4.05    24.495 1    27.387  ? 414  GLY A O   1 1 
ATOM   3078 N  N   . ASP A 1 379 ? 22.731  3.23    24.824 1    22.461  ? 415  ASP A N   1 1 
ATOM   3079 C  CA  . ASP A 1 379 ? 22.667  3.666   26.221 1    22.038  ? 415  ASP A CA  1 1 
ATOM   3080 C  C   . ASP A 1 379 ? 23.783  3.012   27.023 1    22.889  ? 415  ASP A C   1 1 
ATOM   3081 O  O   . ASP A 1 379 ? 24.278  3.588   27.994 1    26.184  ? 415  ASP A O   1 1 
ATOM   3082 C  CB  . ASP A 1 379 ? 21.348  3.399   26.893 1    21.471  ? 415  ASP A CB  1 1 
ATOM   3083 C  CG  . ASP A 1 379 ? 20.132  4.148   26.344 1    27.823  ? 415  ASP A CG  1 1 
ATOM   3084 O  OD1 . ASP A 1 379 ? 20.074  4.44    25.136 1    29.821  ? 415  ASP A OD1 1 1 
ATOM   3085 O  OD2 . ASP A 1 379 ? 19.184  4.361   27.111 1    29.148  ? 415  ASP A OD2 1 1 
ATOM   3086 N  N   . VAL A 1 380 ? 24.087  1.754   26.7   1    22.873  ? 416  VAL A N   1 1 
ATOM   3087 C  CA  . VAL A 1 380 ? 25.151  1.025   27.362 1    21.285  ? 416  VAL A CA  1 1 
ATOM   3088 C  C   . VAL A 1 380 ? 26.445  1.855   27.229 1    24.889  ? 416  VAL A C   1 1 
ATOM   3089 O  O   . VAL A 1 380 ? 27.123  2.129   28.227 1    22.403  ? 416  VAL A O   1 1 
ATOM   3090 C  CB  . VAL A 1 380 ? 25.362  -0.409  26.878 1    20.537  ? 416  VAL A CB  1 1 
ATOM   3091 C  CG1 . VAL A 1 380 ? 26.622  -0.987  27.53  1    21.951  ? 416  VAL A CG1 1 1 
ATOM   3092 C  CG2 . VAL A 1 380 ? 24.154  -1.303  27.186 1    19.559  ? 416  VAL A CG2 1 1 
ATOM   3093 N  N   . LEU A 1 381 ? 26.799  2.239   25.988 1    23.638  ? 417  LEU A N   1 1 
ATOM   3094 C  CA  . LEU A 1 381 ? 28.045  2.926   25.735 1    25.541  ? 417  LEU A CA  1 1 
ATOM   3095 C  C   . LEU A 1 381 ? 27.99   4.264   26.45  1    25.311  ? 417  LEU A C   1 1 
ATOM   3096 O  O   . LEU A 1 381 ? 28.961  4.669   27.042 1    25.483  ? 417  LEU A O   1 1 
ATOM   3097 C  CB  . LEU A 1 381 ? 28.356  3.099   24.247 1    26.741  ? 417  LEU A CB  1 1 
ATOM   3098 C  CG  . LEU A 1 381 ? 29.162  1.941   23.652 1    26.432  ? 417  LEU A CG  1 1 
ATOM   3099 C  CD1 . LEU A 1 381 ? 28.441  0.594   23.703 1    23.964  ? 417  LEU A CD1 1 1 
ATOM   3100 C  CD2 . LEU A 1 381 ? 29.503  2.347   22.231 1    27.309  ? 417  LEU A CD2 1 1 
ATOM   3101 N  N   . ALA A 1 382 ? 26.829  4.911   26.422 1    24.684  ? 418  ALA A N   1 1 
ATOM   3102 C  CA  . ALA A 1 382 ? 26.672  6.215   27.054 1    25.455  ? 418  ALA A CA  1 1 
ATOM   3103 C  C   . ALA A 1 382 ? 26.787  6.194   28.607 1    25.791  ? 418  ALA A C   1 1 
ATOM   3104 O  O   . ALA A 1 382 ? 27.174  7.203   29.224 1    25.212  ? 418  ALA A O   1 1 
ATOM   3105 C  CB  . ALA A 1 382 ? 25.359  6.795   26.557 1    23.484  ? 418  ALA A CB  1 1 
ATOM   3106 N  N   . LEU A 1 383 ? 26.484  5.055   29.252 1    22.934  ? 419  LEU A N   1 1 
ATOM   3107 C  CA  . LEU A 1 383 ? 26.794  4.868   30.674 1    24.924  ? 419  LEU A CA  1 1 
ATOM   3108 C  C   . LEU A 1 383 ? 28.288  5.161   30.905 1    26.404  ? 419  LEU A C   1 1 
ATOM   3109 O  O   . LEU A 1 383 ? 28.626  5.927   31.824 1    23.509  ? 419  LEU A O   1 1 
ATOM   3110 C  CB  . LEU A 1 383 ? 26.418  3.464   31.165 1    22.877  ? 419  LEU A CB  1 1 
ATOM   3111 C  CG  . LEU A 1 383 ? 24.909  3.199   31.302 1    23.298  ? 419  LEU A CG  1 1 
ATOM   3112 C  CD1 . LEU A 1 383 ? 24.679  1.722   31.659 1    22.1    ? 419  LEU A CD1 1 1 
ATOM   3113 C  CD2 . LEU A 1 383 ? 24.401  4.159   32.404 1    24.539  ? 419  LEU A CD2 1 1 
ATOM   3114 N  N   . SER A 1 384 ? 29.148  4.597   30.021 1    23.471  ? 420  SER A N   1 1 
ATOM   3115 C  CA  . SER A 1 384 ? 30.589  4.781   30.137 1    26.432  ? 420  SER A CA  1 1 
ATOM   3116 C  C   . SER A 1 384 ? 30.986  6.241   29.862 1    27.117  ? 420  SER A C   1 1 
ATOM   3117 O  O   . SER A 1 384 ? 31.886  6.768   30.537 1    27.631  ? 420  SER A O   1 1 
ATOM   3118 C  CB  . SER A 1 384 ? 31.419  3.804   29.304 1    27.933  ? 420  SER A CB  1 1 
ATOM   3119 O  OG  . SER A 1 384 ? 31.394  2.497   29.873 1    26.527  ? 420  SER A OG  1 1 
ATOM   3120 N  N   . VAL A 1 385 ? 30.265  6.879   28.917 1    26.096  ? 421  VAL A N   1 1 
ATOM   3121 C  CA  . VAL A 1 385 ? 30.592  8.205   28.424 1    29.542  ? 421  VAL A CA  1 1 
ATOM   3122 C  C   . VAL A 1 385 ? 30.341  9.222   29.549 1    28.924  ? 421  VAL A C   1 1 
ATOM   3123 O  O   . VAL A 1 385 ? 31.075  10.179  29.693 1    30.018  ? 421  VAL A O   1 1 
ATOM   3124 C  CB  . VAL A 1 385 ? 29.763  8.57    27.177 1    26.674  ? 421  VAL A CB  1 1 
ATOM   3125 C  CG1 . VAL A 1 385 ? 30.016  10.018  26.788 1    26.61   ? 421  VAL A CG1 1 1 
ATOM   3126 C  CG2 . VAL A 1 385 ? 30.135  7.744   25.971 1    27.806  ? 421  VAL A CG2 1 1 
ATOM   3127 N  N   . SER A 1 386 ? 29.296  8.975   30.352 1    27.757  ? 422  SER A N   1 1 
ATOM   3128 C  CA  . SER A 1 386 ? 28.821  9.865   31.379 1    24.885  ? 422  SER A CA  1 1 
ATOM   3129 C  C   . SER A 1 386 ? 29.695  9.819   32.624 1    28.107  ? 422  SER A C   1 1 
ATOM   3130 O  O   . SER A 1 386 ? 29.581  10.712  33.486 1    29.056  ? 422  SER A O   1 1 
ATOM   3131 C  CB  . SER A 1 386 ? 27.367  9.564   31.689 1    24.513  ? 422  SER A CB  1 1 
ATOM   3132 O  OG  . SER A 1 386 ? 26.615  9.637   30.477 1    25.949  ? 422  SER A OG  1 1 
ATOM   3133 N  N   . THR A 1 387 ? 30.583  8.823   32.749 1    27.753  ? 423  THR A N   1 1 
ATOM   3134 C  CA  . THR A 1 387 ? 31.386  8.82    33.979 1    28.515  ? 423  THR A CA  1 1 
ATOM   3135 C  C   . THR A 1 387 ? 32.248  10.091  34.065 1    32.267  ? 423  THR A C   1 1 
ATOM   3136 O  O   . THR A 1 387 ? 32.7    10.636  33.053 1    28.928  ? 423  THR A O   1 1 
ATOM   3137 C  CB  . THR A 1 387 ? 32.253  7.565   34.162 1    30.123  ? 423  THR A CB  1 1 
ATOM   3138 O  OG1 . THR A 1 387 ? 33.17   7.524   33.059 1    31.874  ? 423  THR A OG1 1 1 
ATOM   3139 C  CG2 . THR A 1 387 ? 31.428  6.279   34.209 1    30.865  ? 423  THR A CG2 1 1 
ATOM   3140 N  N   . PRO A 1 388 ? 32.531  10.549  35.31  1    31.687  ? 424  PRO A N   1 1 
ATOM   3141 C  CA  . PRO A 1 388 ? 33.437  11.659  35.548 1    33.511  ? 424  PRO A CA  1 1 
ATOM   3142 C  C   . PRO A 1 388 ? 34.761  11.459  34.857 1    36.759  ? 424  PRO A C   1 1 
ATOM   3143 O  O   . PRO A 1 388 ? 35.226  12.384  34.186 1    38.935  ? 424  PRO A O   1 1 
ATOM   3144 C  CB  . PRO A 1 388 ? 33.567  11.593  37.086 1    36.027  ? 424  PRO A CB  1 1 
ATOM   3145 C  CG  . PRO A 1 388 ? 32.131  11.213  37.517 1    34.794  ? 424  PRO A CG  1 1 
ATOM   3146 C  CD  . PRO A 1 388 ? 31.893  10.05   36.547 1    31.659  ? 424  PRO A CD  1 1 
ATOM   3147 N  N   . LYS A 1 389 ? 35.329  10.258  35.027 1    35      ? 425  LYS A N   1 1 
ATOM   3148 C  CA  . LYS A 1 389 ? 36.552  9.883   34.335 1    40.2    ? 425  LYS A CA  1 1 
ATOM   3149 C  C   . LYS A 1 389 ? 36.494  10.188  32.82  1    39.887  ? 425  LYS A C   1 1 
ATOM   3150 O  O   . LYS A 1 389 ? 37.425  10.815  32.266 1    35.311  ? 425  LYS A O   1 1 
ATOM   3151 C  CB  . LYS A 1 389 ? 36.907  8.427   34.668 1    37.38   ? 425  LYS A CB  1 1 
ATOM   3152 C  CG  . LYS A 1 389 ? 37.476  7.668   33.49  1    43.418  ? 425  LYS A CG  1 1 
ATOM   3153 C  CD  . LYS A 1 389 ? 38.386  6.459   33.732 1    49.218  ? 425  LYS A CD  1 1 
ATOM   3154 C  CE  . LYS A 1 389 ? 38.7    5.911   32.359 1    48.786  ? 425  LYS A CE  1 1 
ATOM   3155 N  NZ  . LYS A 1 389 ? 39.939  5.137   32.416 1    47.33   ? 425  LYS A NZ  1 1 
ATOM   3156 N  N   . HIS A 1 390 ? 35.431  9.677   32.148 1    35.684  ? 426  HIS A N   1 1 
ATOM   3157 C  CA  . HIS A 1 390 ? 35.319  9.807   30.696 1    34.755  ? 426  HIS A CA  1 1 
ATOM   3158 C  C   . HIS A 1 390 ? 35.074  11.283  30.323 1    32.496  ? 426  HIS A C   1 1 
ATOM   3159 O  O   . HIS A 1 390 ? 35.645  11.766  29.355 1    33.064  ? 426  HIS A O   1 1 
ATOM   3160 C  CB  . HIS A 1 390 ? 34.247  8.898   30.072 1    32.159  ? 426  HIS A CB  1 1 
ATOM   3161 C  CG  . HIS A 1 390 ? 34.383  8.869   28.582 1    37.239  ? 426  HIS A CG  1 1 
ATOM   3162 N  ND1 . HIS A 1 390 ? 35.204  7.954   27.96  1    40.173  ? 426  HIS A ND1 1 1 
ATOM   3163 C  CD2 . HIS A 1 390 ? 33.944  9.693   27.597 1    35.739  ? 426  HIS A CD2 1 1 
ATOM   3164 C  CE1 . HIS A 1 390 ? 35.271  8.211   26.657 1    40.685  ? 426  HIS A CE1 1 1 
ATOM   3165 N  NE2 . HIS A 1 390 ? 34.477  9.237   26.413 1    43.261  ? 426  HIS A NE2 1 1 
ATOM   3166 N  N   . LEU A 1 391 ? 34.132  11.961  31.009 1    32.011  ? 427  LEU A N   1 1 
ATOM   3167 C  CA  . LEU A 1 391 ? 33.866  13.389  30.794 1    31.574  ? 427  LEU A CA  1 1 
ATOM   3168 C  C   . LEU A 1 391 ? 35.155  14.217  30.943 1    32.847  ? 427  LEU A C   1 1 
ATOM   3169 O  O   . LEU A 1 391 ? 35.444  15.066  30.101 1    32.754  ? 427  LEU A O   1 1 
ATOM   3170 C  CB  . LEU A 1 391 ? 32.727  13.948  31.647 1    27.262  ? 427  LEU A CB  1 1 
ATOM   3171 C  CG  . LEU A 1 391 ? 31.364  13.309  31.378 1    25.145  ? 427  LEU A CG  1 1 
ATOM   3172 C  CD1 . LEU A 1 391 ? 30.243  13.847  32.25  1    22.891  ? 427  LEU A CD1 1 1 
ATOM   3173 C  CD2 . LEU A 1 391 ? 30.98   13.48   29.895 1    24.559  ? 427  LEU A CD2 1 1 
ATOM   3174 N  N   . HIS A 1 392 ? 35.959  13.928  31.98  1    32.055  ? 428  HIS A N   1 1 
ATOM   3175 C  CA  . HIS A 1 392 ? 37.195  14.678  32.134 1    32.711  ? 428  HIS A CA  1 1 
ATOM   3176 C  C   . HIS A 1 392 ? 38.106  14.459  30.936 1    33.325  ? 428  HIS A C   1 1 
ATOM   3177 O  O   . HIS A 1 392 ? 38.803  15.381  30.487 1    34.003  ? 428  HIS A O   1 1 
ATOM   3178 C  CB  . HIS A 1 392 ? 37.844  14.432  33.494 1    34.801  ? 428  HIS A CB  1 1 
ATOM   3179 C  CG  . HIS A 1 392 ? 39.252  14.942  33.554 1    38.808  ? 428  HIS A CG  1 1 
ATOM   3180 N  ND1 . HIS A 1 392 ? 39.61   16.271  33.734 1    43.198  ? 428  HIS A ND1 1 1 
ATOM   3181 C  CD2 . HIS A 1 392 ? 40.399  14.272  33.406 1    40.694  ? 428  HIS A CD2 1 1 
ATOM   3182 C  CE1 . HIS A 1 392 ? 40.947  16.385  33.741 1    45.792  ? 428  HIS A CE1 1 1 
ATOM   3183 N  NE2 . HIS A 1 392 ? 41.446  15.174  33.539 1    44.206  ? 428  HIS A NE2 1 1 
ATOM   3184 N  N   . SER A 1 393 ? 38.066  13.25   30.372 1    34.027  ? 429  SER A N   1 1 
ATOM   3185 C  CA  . SER A 1 393 ? 38.934  12.959  29.236 1    35.039  ? 429  SER A CA  1 1 
ATOM   3186 C  C   . SER A 1 393 ? 38.46   13.65   27.945 1    33.431  ? 429  SER A C   1 1 
ATOM   3187 O  O   . SER A 1 393 ? 39.246  13.799  27.04  1    33.093  ? 429  SER A O   1 1 
ATOM   3188 C  CB  . SER A 1 393 ? 39.128  11.453  29.054 1    35.445  ? 429  SER A CB  1 1 
ATOM   3189 O  OG  . SER A 1 393 ? 38.048  10.838  28.347 1    36.83   ? 429  SER A OG  1 1 
ATOM   3190 N  N   . LEU A 1 394 ? 37.174  14.01   27.84  1    32.09   ? 430  LEU A N   1 1 
ATOM   3191 C  CA  . LEU A 1 394 ? 36.666  14.839  26.755 1    35.915  ? 430  LEU A CA  1 1 
ATOM   3192 C  C   . LEU A 1 394 ? 36.855  16.331  27.047 1    41.443  ? 430  LEU A C   1 1 
ATOM   3193 O  O   . LEU A 1 394 ? 36.396  17.185  26.268 1    41.292  ? 430  LEU A O   1 1 
ATOM   3194 C  CB  . LEU A 1 394 ? 35.175  14.568  26.592 1    33.323  ? 430  LEU A CB  1 1 
ATOM   3195 C  CG  . LEU A 1 394 ? 34.825  13.16   26.115 1    32.94   ? 430  LEU A CG  1 1 
ATOM   3196 C  CD1 . LEU A 1 394 ? 33.35   13.025  26.145 1    30.913  ? 430  LEU A CD1 1 1 
ATOM   3197 C  CD2 . LEU A 1 394 ? 35.408  12.902  24.733 1    35.061  ? 430  LEU A CD2 1 1 
ATOM   3198 N  N   . ASN A 1 395 ? 37.479  16.636  28.194 1    39.553  ? 431  ASN A N   1 1 
ATOM   3199 C  CA  . ASN A 1 395 ? 37.686  18.006  28.619 1    40.914  ? 431  ASN A CA  1 1 
ATOM   3200 C  C   . ASN A 1 395 ? 36.356  18.708  28.928 1    38.666  ? 431  ASN A C   1 1 
ATOM   3201 O  O   . ASN A 1 395 ? 36.233  19.892  28.606 1    37.787  ? 431  ASN A O   1 1 
ATOM   3202 C  CB  . ASN A 1 395 ? 38.517  18.818  27.617 1    45.912  ? 431  ASN A CB  1 1 
ATOM   3203 C  CG  . ASN A 1 395 ? 39.347  19.908  28.277 1    47.556  ? 431  ASN A CG  1 1 
ATOM   3204 O  OD1 . ASN A 1 395 ? 39.622  19.86   29.475 1    50.673  ? 431  ASN A OD1 1 1 
ATOM   3205 N  ND2 . ASN A 1 395 ? 39.761  20.919  27.536 1    46.902  ? 431  ASN A ND2 1 1 
ATOM   3206 N  N   . LEU A 1 396 ? 35.452  18.047  29.66  1    32.076  ? 432  LEU A N   1 1 
ATOM   3207 C  CA  . LEU A 1 396 ? 34.15   18.615  29.967 1    32.3    ? 432  LEU A CA  1 1 
ATOM   3208 C  C   . LEU A 1 396 ? 33.948  18.63   31.482 1    33.054  ? 432  LEU A C   1 1 
ATOM   3209 O  O   . LEU A 1 396 ? 32.858  18.922  31.92  1    34.304  ? 432  LEU A O   1 1 
ATOM   3210 C  CB  . LEU A 1 396 ? 32.968  17.902  29.284 1    31.358  ? 432  LEU A CB  1 1 
ATOM   3211 C  CG  . LEU A 1 396 ? 33.074  17.667  27.763 1    30.335  ? 432  LEU A CG  1 1 
ATOM   3212 C  CD1 . LEU A 1 396 ? 31.804  16.957  27.292 1    28.925  ? 432  LEU A CD1 1 1 
ATOM   3213 C  CD2 . LEU A 1 396 ? 33.23   18.944  26.986 1    31.181  ? 432  LEU A CD2 1 1 
ATOM   3214 N  N   . LEU A 1 397 ? 34.967  18.286  32.282 1    33.76   ? 433  LEU A N   1 1 
ATOM   3215 C  CA  . LEU A 1 397 ? 34.827  18.211  33.735 1    37.963  ? 433  LEU A CA  1 1 
ATOM   3216 C  C   . LEU A 1 397 ? 36.23   18.459  34.244 1    42.272  ? 433  LEU A C   1 1 
ATOM   3217 O  O   . LEU A 1 397 ? 37.125  18.078  33.492 1    42.526  ? 433  LEU A O   1 1 
ATOM   3218 C  CB  . LEU A 1 397 ? 34.349  16.829  34.198 1    40.931  ? 433  LEU A CB  1 1 
ATOM   3219 C  CG  . LEU A 1 397 ? 33.77   16.742  35.622 1    52.426  ? 433  LEU A CG  1 1 
ATOM   3220 C  CD1 . LEU A 1 397 ? 33.042  15.415  35.796 1    51.466  ? 433  LEU A CD1 1 1 
ATOM   3221 C  CD2 . LEU A 1 397 ? 34.696  17.012  36.841 1    60.098  ? 433  LEU A CD2 1 1 
ATOM   3222 N  N   . SER A 1 398 ? 36.398  19.077  35.432 1    43.948  ? 434  SER A N   1 1 
ATOM   3223 C  CA  . SER A 1 398 ? 37.715  19.396  36.007 1    51.711  ? 434  SER A CA  1 1 
ATOM   3224 C  C   . SER A 1 398 ? 38.552  18.157  36.362 1    52.793  ? 434  SER A C   1 1 
ATOM   3225 O  O   . SER A 1 398 ? 39.789  18.175  36.297 1    53.59   ? 434  SER A O   1 1 
ATOM   3226 C  CB  . SER A 1 398 ? 37.594  20.249  37.23  1    51.162  ? 434  SER A CB  1 1 
ATOM   3227 O  OG  . SER A 1 398 ? 36.999  21.476  36.89  1    62.324  ? 434  SER A OG  1 1 
ATOM   3228 N  N   . SER A 1 399 ? 37.858  17.106  36.802 1    57.71   ? 435  SER A N   1 1 
ATOM   3229 C  CA  . SER A 1 399 ? 38.418  15.8    37.09  1    58.435  ? 435  SER A CA  1 1 
ATOM   3230 C  C   . SER A 1 399 ? 37.275  14.911  37.601 1    69.323  ? 435  SER A C   1 1 
ATOM   3231 O  O   . SER A 1 399 ? 37.484  13.675  37.627 1    84.631  ? 435  SER A O   1 1 
ATOM   3232 C  CB  . SER A 1 399 ? 39.487  15.903  38.102 1    55.111  ? 435  SER A CB  1 1 
ATOM   3233 O  OG  . SER A 1 399 ? 38.876  16.286  39.319 1    49.881  ? 435  SER A OG  1 1 
ATOM   3234 N  N   . GLY A 1 402 ? 37.982  11.91   42.61  1    65.035  ? 438  GLY A N   1 1 
ATOM   3235 C  CA  . GLY A 1 402 ? 38.381  11.826  44.033 1    69.008  ? 438  GLY A CA  1 1 
ATOM   3236 C  C   . GLY A 1 402 ? 37.234  11.396  44.963 1    71.835  ? 438  GLY A C   1 1 
ATOM   3237 O  O   . GLY A 1 402 ? 36.973  10.212  45.16  1    66.016  ? 438  GLY A O   1 1 
ATOM   3238 N  N   . SER A 1 403 ? 36.534  12.378  45.541 1    67.626  ? 439  SER A N   1 1 
ATOM   3239 C  CA  . SER A 1 403 ? 35.797  12.224  46.789 1    55.152  ? 439  SER A CA  1 1 
ATOM   3240 C  C   . SER A 1 403 ? 34.539  11.354  46.662 1    53.046  ? 439  SER A C   1 1 
ATOM   3241 O  O   . SER A 1 403 ? 33.92   11.213  45.594 1    49.9    ? 439  SER A O   1 1 
ATOM   3242 C  CB  . SER A 1 403 ? 35.463  13.587  47.331 1    58.492  ? 439  SER A CB  1 1 
ATOM   3243 O  OG  . SER A 1 403 ? 34.779  14.341  46.336 1    55.42   ? 439  SER A OG  1 1 
ATOM   3244 N  N   . ASP A 1 404 ? 34.136  10.805  47.809 1    45.708  ? 440  ASP A N   1 1 
ATOM   3245 C  CA  . ASP A 1 404 ? 32.784  10.315  48.07  1    53.201  ? 440  ASP A CA  1 1 
ATOM   3246 C  C   . ASP A 1 404 ? 31.691  11.317  47.661 1    44.564  ? 440  ASP A C   1 1 
ATOM   3247 O  O   . ASP A 1 404 ? 30.632  10.947  47.167 1    38.347  ? 440  ASP A O   1 1 
ATOM   3248 C  CB  . ASP A 1 404 ? 32.541  10.19   49.57  1    56.314  ? 440  ASP A CB  1 1 
ATOM   3249 C  CG  . ASP A 1 404 ? 32.498  8.775   50.117 1    70.073  ? 440  ASP A CG  1 1 
ATOM   3250 O  OD1 . ASP A 1 404 ? 33.599  8.211   50.364 1    69.375  ? 440  ASP A OD1 1 1 
ATOM   3251 O  OD2 . ASP A 1 404 ? 31.356  8.256   50.266 1    71.301  ? 440  ASP A OD2 1 1 
ATOM   3252 N  N   . GLU A 1 405 ? 31.924  12.591  47.997 1    43.254  ? 441  GLU A N   1 1 
ATOM   3253 C  CA  . GLU A 1 405 ? 30.97   13.651  47.725 1    42.069  ? 441  GLU A CA  1 1 
ATOM   3254 C  C   . GLU A 1 405 ? 30.717  13.754  46.229 1    38.544  ? 441  GLU A C   1 1 
ATOM   3255 O  O   . GLU A 1 405 ? 29.561  13.825  45.862 1    32.26   ? 441  GLU A O   1 1 
ATOM   3256 C  CB  . GLU A 1 405 ? 31.424  14.93   48.415 1    44.697  ? 441  GLU A CB  1 1 
ATOM   3257 C  CG  . GLU A 1 405 ? 31.521  14.701  49.925 1    51.221  ? 441  GLU A CG  1 1 
ATOM   3258 C  CD  . GLU A 1 405 ? 31.471  15.994  50.717 1    56.539  ? 441  GLU A CD  1 1 
ATOM   3259 O  OE1 . GLU A 1 405 ? 31.631  17.011  49.999 1    58.312  ? 441  GLU A OE1 1 1 
ATOM   3260 O  OE2 . GLU A 1 405 ? 31.259  16.032  51.975 1    61.082  ? 441  GLU A OE2 1 1 
ATOM   3261 N  N   . HIS A 1 406 ? 31.786  13.723  45.399 1    40.034  ? 442  HIS A N   1 1 
ATOM   3262 C  CA  . HIS A 1 406 ? 31.615  13.841  43.957 1    38.943  ? 442  HIS A CA  1 1 
ATOM   3263 C  C   . HIS A 1 406 ? 30.95   12.562  43.459 1    39.9    ? 442  HIS A C   1 1 
ATOM   3264 O  O   . HIS A 1 406 ? 30.239  12.564  42.457 1    36.523  ? 442  HIS A O   1 1 
ATOM   3265 C  CB  . HIS A 1 406 ? 32.947  14.029  43.233 1    39.696  ? 442  HIS A CB  1 1 
ATOM   3266 C  CG  . HIS A 1 406 ? 33.46   15.431  43.238 1    50.788  ? 442  HIS A CG  1 1 
ATOM   3267 N  ND1 . HIS A 1 406 ? 32.741  16.523  42.758 1    47.381  ? 442  HIS A ND1 1 1 
ATOM   3268 C  CD2 . HIS A 1 406 ? 34.661  15.909  43.671 1    49.173  ? 442  HIS A CD2 1 1 
ATOM   3269 C  CE1 . HIS A 1 406 ? 33.467  17.628  42.917 1    53.985  ? 442  HIS A CE1 1 1 
ATOM   3270 N  NE2 . HIS A 1 406 ? 34.632  17.29   43.493 1    58.039  ? 442  HIS A NE2 1 1 
ATOM   3271 N  N   . ASP A 1 407 ? 31.207  11.478  44.192 1    35.72   ? 443  ASP A N   1 1 
ATOM   3272 C  CA  . ASP A 1 407 ? 30.672  10.195  43.829 1    33.086  ? 443  ASP A CA  1 1 
ATOM   3273 C  C   . ASP A 1 407 ? 29.144  10.181  43.934 1    31.277  ? 443  ASP A C   1 1 
ATOM   3274 O  O   . ASP A 1 407 ? 28.475  9.742   42.993 1    28.34   ? 443  ASP A O   1 1 
ATOM   3275 C  CB  . ASP A 1 407 ? 31.234  9.154   44.762 1    39.853  ? 443  ASP A CB  1 1 
ATOM   3276 C  CG  . ASP A 1 407 ? 31.291  7.771   44.149 1    44.387  ? 443  ASP A CG  1 1 
ATOM   3277 O  OD1 . ASP A 1 407 ? 31.593  7.687   42.933 1    47.731  ? 443  ASP A OD1 1 1 
ATOM   3278 O  OD2 . ASP A 1 407 ? 31.118  6.802   44.901 1    51.976  ? 443  ASP A OD2 1 1 
ATOM   3279 N  N   . ILE A 1 408 ? 28.605  10.621  45.091 1    28.62   ? 444  ILE A N   1 1 
ATOM   3280 C  CA  . ILE A 1 408 ? 27.18   10.556  45.422 1    26.946  ? 444  ILE A CA  1 1 
ATOM   3281 C  C   . ILE A 1 408 ? 26.503  11.548  44.507 1    25.745  ? 444  ILE A C   1 1 
ATOM   3282 O  O   . ILE A 1 408 ? 25.346  11.355  44.137 1    28.425  ? 444  ILE A O   1 1 
ATOM   3283 C  CB  . ILE A 1 408 ? 26.932  10.915  46.929 1    25.922  ? 444  ILE A CB  1 1 
ATOM   3284 C  CG1 . ILE A 1 408 ? 27.409  9.808   47.912 1    25.601  ? 444  ILE A CG1 1 1 
ATOM   3285 C  CG2 . ILE A 1 408 ? 25.472  11.247  47.206 1    24.595  ? 444  ILE A CG2 1 1 
ATOM   3286 C  CD1 . ILE A 1 408 ? 27.135  8.348   47.517 1    25.654  ? 444  ILE A CD1 1 1 
ATOM   3287 N  N   . ASN A 1 409 ? 27.229  12.638  44.208 1    25.257  ? 445  ASN A N   1 1 
ATOM   3288 C  CA  . ASN A 1 409 ? 26.747  13.685  43.319 1    26.233  ? 445  ASN A CA  1 1 
ATOM   3289 C  C   . ASN A 1 409 ? 26.563  13.123  41.902 1    26.11   ? 445  ASN A C   1 1 
ATOM   3290 O  O   . ASN A 1 409 ? 25.552  13.445  41.273 1    25.905  ? 445  ASN A O   1 1 
ATOM   3291 C  CB  . ASN A 1 409 ? 27.637  14.919  43.266 1    29.567  ? 445  ASN A CB  1 1 
ATOM   3292 C  CG  . ASN A 1 409 ? 27.488  15.938  44.391 1    32.324  ? 445  ASN A CG  1 1 
ATOM   3293 O  OD1 . ASN A 1 409 ? 26.538  15.947  45.202 1    32.183  ? 445  ASN A OD1 1 1 
ATOM   3294 N  ND2 . ASN A 1 409 ? 28.392  16.905  44.381 1    32.339  ? 445  ASN A ND2 1 1 
ATOM   3295 N  N   . PHE A 1 410 ? 27.519  12.32   41.398 1    24.364  ? 446  PHE A N   1 1 
ATOM   3296 C  CA  . PHE A 1 410 ? 27.411  11.719  40.069 1    23.652  ? 446  PHE A CA  1 1 
ATOM   3297 C  C   . PHE A 1 410 ? 26.248  10.73   40.017 1    24.289  ? 446  PHE A C   1 1 
ATOM   3298 O  O   . PHE A 1 410 ? 25.449  10.734  39.078 1    24.427  ? 446  PHE A O   1 1 
ATOM   3299 C  CB  . PHE A 1 410 ? 28.723  10.969  39.763 1    26.105  ? 446  PHE A CB  1 1 
ATOM   3300 C  CG  . PHE A 1 410 ? 28.607  10.01   38.582 1    27.383  ? 446  PHE A CG  1 1 
ATOM   3301 C  CD1 . PHE A 1 410 ? 28.348  10.51   37.3   1    27.214  ? 446  PHE A CD1 1 1 
ATOM   3302 C  CD2 . PHE A 1 410 ? 28.697  8.627   38.767 1    26.62   ? 446  PHE A CD2 1 1 
ATOM   3303 C  CE1 . PHE A 1 410 ? 28.208  9.659   36.202 1    27.055  ? 446  PHE A CE1 1 1 
ATOM   3304 C  CE2 . PHE A 1 410 ? 28.575  7.77    37.695 1    27.508  ? 446  PHE A CE2 1 1 
ATOM   3305 C  CZ  . PHE A 1 410 ? 28.343  8.28    36.394 1    28.366  ? 446  PHE A CZ  1 1 
ATOM   3306 N  N   . LEU A 1 411 ? 26.122  9.892   41.055 1    23.282  ? 447  LEU A N   1 1 
ATOM   3307 C  CA  . LEU A 1 411 ? 25.059  8.887   41.189 1    23.628  ? 447  LEU A CA  1 1 
ATOM   3308 C  C   . LEU A 1 411 ? 23.679  9.547   41.181 1    22.32   ? 447  LEU A C   1 1 
ATOM   3309 O  O   . LEU A 1 411 ? 22.75   9.049   40.512 1    22.215  ? 447  LEU A O   1 1 
ATOM   3310 C  CB  . LEU A 1 411 ? 25.204  7.92    42.378 1    24.328  ? 447  LEU A CB  1 1 
ATOM   3311 C  CG  . LEU A 1 411 ? 26.296  6.851   42.236 1    25.953  ? 447  LEU A CG  1 1 
ATOM   3312 C  CD1 . LEU A 1 411 ? 26.565  6.084   43.513 1    23.47   ? 447  LEU A CD1 1 1 
ATOM   3313 C  CD2 . LEU A 1 411 ? 26.004  5.882   41.069 1    22.393  ? 447  LEU A CD2 1 1 
ATOM   3314 N  N   . MET A 1 412 ? 23.564  10.691  41.869 1    22.145  ? 448  MET A N   1 1 
ATOM   3315 C  CA  . MET A 1 412 ? 22.31   11.437  41.894 1    20.824  ? 448  MET A CA  1 1 
ATOM   3316 C  C   . MET A 1 412 ? 22.011  11.92   40.468 1    22.328  ? 448  MET A C   1 1 
ATOM   3317 O  O   . MET A 1 412 ? 20.886  11.881  40.016 1    20.874  ? 448  MET A O   1 1 
ATOM   3318 C  CB  . MET A 1 412 ? 22.413  12.633  42.865 1    23.572  ? 448  MET A CB  1 1 
ATOM   3319 C  CG  . MET A 1 412 ? 21.19   13.52   42.862 1    23.703  ? 448  MET A CG  1 1 
ATOM   3320 S  SD  . MET A 1 412 ? 19.654  12.629  43.231 1    31.711  ? 448  MET A SD  1 1 
ATOM   3321 C  CE  . MET A 1 412 ? 19.706  12.017  44.909 1    28.21   ? 448  MET A CE  1 1 
ATOM   3322 N  N   . LYS A 1 413 ? 23.016  12.438  39.762 1    25.912  ? 449  LYS A N   1 1 
ATOM   3323 C  CA  . LYS A 1 413 ? 22.797  12.921  38.404 1    28.642  ? 449  LYS A CA  1 1 
ATOM   3324 C  C   . LYS A 1 413 ? 22.257  11.785  37.527 1    26.836  ? 449  LYS A C   1 1 
ATOM   3325 O  O   . LYS A 1 413 ? 21.214  11.947  36.843 1    25.338  ? 449  LYS A O   1 1 
ATOM   3326 C  CB  . LYS A 1 413 ? 24.012  13.724  37.937 1    31.174  ? 449  LYS A CB  1 1 
ATOM   3327 C  CG  . LYS A 1 413 ? 23.887  14.164  36.508 1    40.548  ? 449  LYS A CG  1 1 
ATOM   3328 C  CD  . LYS A 1 413 ? 24.659  15.431  36.123 1    60.171  ? 449  LYS A CD  1 1 
ATOM   3329 C  CE  . LYS A 1 413 ? 23.821  16.391  35.26  1    69.461  ? 449  LYS A CE  1 1 
ATOM   3330 N  NZ  . LYS A 1 413 ? 23.28   15.862  33.989 1    68.442  ? 449  LYS A NZ  1 1 
ATOM   3331 N  N   . MET A 1 414 ? 22.864  10.604  37.655 1    23.912  ? 450  MET A N   1 1 
ATOM   3332 C  CA  . MET A 1 414 ? 22.468  9.419   36.893 1    21.901  ? 450  MET A CA  1 1 
ATOM   3333 C  C   . MET A 1 414 ? 21.065  8.946   37.269 1    20.927  ? 450  MET A C   1 1 
ATOM   3334 O  O   . MET A 1 414 ? 20.302  8.54    36.384 1    22.216  ? 450  MET A O   1 1 
ATOM   3335 C  CB  . MET A 1 414 ? 23.499  8.276   36.955 1    23.648  ? 450  MET A CB  1 1 
ATOM   3336 C  CG  . MET A 1 414 ? 24.94   8.596   36.412 1    25.745  ? 450  MET A CG  1 1 
ATOM   3337 S  SD  . MET A 1 414 ? 24.911  8.845   34.601 1    34.991  ? 450  MET A SD  1 1 
ATOM   3338 C  CE  . MET A 1 414 ? 23.682  7.626   34.117 1    30.097  ? 450  MET A CE  1 1 
ATOM   3339 N  N   . ALA A 1 415 ? 20.76   8.932   38.564 1    19.164  ? 451  ALA A N   1 1 
ATOM   3340 C  CA  . ALA A 1 415 ? 19.454  8.59    39.128 1    20.63   ? 451  ALA A CA  1 1 
ATOM   3341 C  C   . ALA A 1 415 ? 18.33   9.448   38.539 1    21.321  ? 451  ALA A C   1 1 
ATOM   3342 O  O   . ALA A 1 415 ? 17.255  8.937   38.248 1    20.269  ? 451  ALA A O   1 1 
ATOM   3343 C  CB  . ALA A 1 415 ? 19.502  8.726   40.655 1    17.915  ? 451  ALA A CB  1 1 
ATOM   3344 N  N   . LEU A 1 416 ? 18.575  10.763  38.367 1    20.077  ? 452  LEU A N   1 1 
ATOM   3345 C  CA  . LEU A 1 416 ? 17.488  11.634  37.923 1    21.27   ? 452  LEU A CA  1 1 
ATOM   3346 C  C   . LEU A 1 416 ? 17.085  11.286  36.473 1    24.484  ? 452  LEU A C   1 1 
ATOM   3347 O  O   . LEU A 1 416 ? 15.94   11.515  36.084 1    26.014  ? 452  LEU A O   1 1 
ATOM   3348 C  CB  . LEU A 1 416 ? 17.914  13.097  38.118 1    17.814  ? 452  LEU A CB  1 1 
ATOM   3349 C  CG  . LEU A 1 416 ? 18.157  13.511  39.579 1    19.889  ? 452  LEU A CG  1 1 
ATOM   3350 C  CD1 . LEU A 1 416 ? 18.802  14.922  39.619 1    19.723  ? 452  LEU A CD1 1 1 
ATOM   3351 C  CD2 . LEU A 1 416 ? 16.86   13.599  40.333 1    19.517  ? 452  LEU A CD2 1 1 
ATOM   3352 N  N   . ASP A 1 417 ? 18.03   10.723  35.702 1    25.67   ? 453  ASP A N   1 1 
ATOM   3353 C  CA  . ASP A 1 417 ? 17.798  10.283  34.331 1    28.203  ? 453  ASP A CA  1 1 
ATOM   3354 C  C   . ASP A 1 417 ? 17.326  8.835   34.311 1    31.242  ? 453  ASP A C   1 1 
ATOM   3355 O  O   . ASP A 1 417 ? 16.432  8.532   33.552 1    51.823  ? 453  ASP A O   1 1 
ATOM   3356 C  CB  . ASP A 1 417 ? 19.037  10.443  33.463 1    32.393  ? 453  ASP A CB  1 1 
ATOM   3357 C  CG  . ASP A 1 417 ? 19.534  11.885  33.396 1    51.568  ? 453  ASP A CG  1 1 
ATOM   3358 O  OD1 . ASP A 1 417 ? 18.69   12.758  33.058 1    55.162  ? 453  ASP A OD1 1 1 
ATOM   3359 O  OD2 . ASP A 1 417 ? 20.733  12.155  33.768 1    54.472  ? 453  ASP A OD2 1 1 
ATOM   3360 N  N   . LYS A 1 418 ? 17.927  7.925   35.092 1    24.09   ? 454  LYS A N   1 1 
ATOM   3361 C  CA  . LYS A 1 418 ? 17.702  6.5     34.909 1    22.101  ? 454  LYS A CA  1 1 
ATOM   3362 C  C   . LYS A 1 418 ? 16.586  5.952   35.79  1    22.225  ? 454  LYS A C   1 1 
ATOM   3363 O  O   . LYS A 1 418 ? 15.721  5.26    35.277 1    19.474  ? 454  LYS A O   1 1 
ATOM   3364 C  CB  . LYS A 1 418 ? 18.979  5.675   35.116 1    22.659  ? 454  LYS A CB  1 1 
ATOM   3365 C  CG  . LYS A 1 418 ? 20.04   6.113   34.063 1    22.574  ? 454  LYS A CG  1 1 
ATOM   3366 C  CD  . LYS A 1 418 ? 19.62   5.772   32.625 1    17.535  ? 454  LYS A CD  1 1 
ATOM   3367 C  CE  . LYS A 1 418 ? 20.906  6.044   31.825 1    21.182  ? 454  LYS A CE  1 1 
ATOM   3368 N  NZ  . LYS A 1 418 ? 20.582  5.765   30.426 1    22.691  ? 454  LYS A NZ  1 1 
ATOM   3369 N  N   . ILE A 1 419 ? 16.582  6.268   37.094 1    22.04   ? 455  ILE A N   1 1 
ATOM   3370 C  CA  . ILE A 1 419 ? 15.596  5.743   38.043 1    19.1    ? 455  ILE A CA  1 1 
ATOM   3371 C  C   . ILE A 1 419 ? 14.266  6.458   37.814 1    18.474  ? 455  ILE A C   1 1 
ATOM   3372 O  O   . ILE A 1 419 ? 13.217  5.848   37.84  1    20.629  ? 455  ILE A O   1 1 
ATOM   3373 C  CB  . ILE A 1 419 ? 16.088  6.031   39.478 1    19.767  ? 455  ILE A CB  1 1 
ATOM   3374 C  CG1 . ILE A 1 419 ? 17.415  5.315   39.859 1    24.739  ? 455  ILE A CG1 1 1 
ATOM   3375 C  CG2 . ILE A 1 419 ? 15.021  5.758   40.516 1    14.422  ? 455  ILE A CG2 1 1 
ATOM   3376 C  CD1 . ILE A 1 419 ? 17.345  3.792   39.728 1    31.981  ? 455  ILE A CD1 1 1 
ATOM   3377 N  N   . ALA A 1 420 ? 14.279  7.808   37.694 1    19.809  ? 456  ALA A N   1 1 
ATOM   3378 C  CA  . ALA A 1 420 ? 13.038  8.544   37.533 1    20.14   ? 456  ALA A CA  1 1 
ATOM   3379 C  C   . ALA A 1 420 ? 12.273  8.011   36.32  1    20.149  ? 456  ALA A C   1 1 
ATOM   3380 O  O   . ALA A 1 420 ? 11.045  7.993   36.32  1    19.45   ? 456  ALA A O   1 1 
ATOM   3381 C  CB  . ALA A 1 420 ? 13.341  10.06   37.398 1    18.714  ? 456  ALA A CB  1 1 
ATOM   3382 N  N   . PHE A 1 421 ? 13.004  7.582   35.274 1    17.431  ? 457  PHE A N   1 1 
ATOM   3383 C  CA  . PHE A 1 421 ? 12.329  7.186   34.032 1    19.54   ? 457  PHE A CA  1 1 
ATOM   3384 C  C   . PHE A 1 421 ? 11.643  5.826   34.166 1    21.06   ? 457  PHE A C   1 1 
ATOM   3385 O  O   . PHE A 1 421 ? 10.753  5.512   33.376 1    22.217  ? 457  PHE A O   1 1 
ATOM   3386 C  CB  . PHE A 1 421 ? 13.393  7.117   32.937 1    17.51   ? 457  PHE A CB  1 1 
ATOM   3387 C  CG  . PHE A 1 421 ? 12.864  6.804   31.528 1    22.191  ? 457  PHE A CG  1 1 
ATOM   3388 C  CD1 . PHE A 1 421 ? 12.112  7.751   30.807 1    21.56   ? 457  PHE A CD1 1 1 
ATOM   3389 C  CD2 . PHE A 1 421 ? 13.112  5.567   30.937 1    18.845  ? 457  PHE A CD2 1 1 
ATOM   3390 C  CE1 . PHE A 1 421 ? 11.724  7.518   29.494 1    21.063  ? 457  PHE A CE1 1 1 
ATOM   3391 C  CE2 . PHE A 1 421 ? 12.642  5.314   29.649 1    19.048  ? 457  PHE A CE2 1 1 
ATOM   3392 C  CZ  . PHE A 1 421 ? 11.913  6.255   28.972 1    23.302  ? 457  PHE A CZ  1 1 
ATOM   3393 N  N   . ILE A 1 422 ? 11.98   5.052   35.23  1    21.176  ? 458  ILE A N   1 1 
ATOM   3394 C  CA  . ILE A 1 422 ? 11.477  3.686   35.342 1    22.415  ? 458  ILE A CA  1 1 
ATOM   3395 C  C   . ILE A 1 422 ? 9.949   3.703   35.394 1    26.158  ? 458  ILE A C   1 1 
ATOM   3396 O  O   . ILE A 1 422 ? 9.335   2.99    34.572 1    25.565  ? 458  ILE A O   1 1 
ATOM   3397 C  CB  . ILE A 1 422 ? 12.169  2.907   36.471 1    22.287  ? 458  ILE A CB  1 1 
ATOM   3398 C  CG1 . ILE A 1 422 ? 13.626  2.54    36.026 1    26.022  ? 458  ILE A CG1 1 1 
ATOM   3399 C  CG2 . ILE A 1 422 ? 11.361  1.69    36.984 1    20.271  ? 458  ILE A CG2 1 1 
ATOM   3400 C  CD1 . ILE A 1 422 ? 13.753  1.297   35.094 1    25.975  ? 458  ILE A CD1 1 1 
ATOM   3401 N  N   . PRO A 1 423 ? 9.279   4.457   36.32  1    22.231  ? 459  PRO A N   1 1 
ATOM   3402 C  CA  . PRO A 1 423 ? 7.825   4.363   36.379 1    18.419  ? 459  PRO A CA  1 1 
ATOM   3403 C  C   . PRO A 1 423 ? 7.198   4.979   35.146 1    17.739  ? 459  PRO A C   1 1 
ATOM   3404 O  O   . PRO A 1 423 ? 6.177   4.474   34.711 1    18.967  ? 459  PRO A O   1 1 
ATOM   3405 C  CB  . PRO A 1 423 ? 7.401   5.086   37.684 1    20.766  ? 459  PRO A CB  1 1 
ATOM   3406 C  CG  . PRO A 1 423 ? 8.583   5.964   37.978 1    24.647  ? 459  PRO A CG  1 1 
ATOM   3407 C  CD  . PRO A 1 423 ? 9.824   5.186   37.493 1    20.043  ? 459  PRO A CD  1 1 
ATOM   3408 N  N   . PHE A 1 424 ? 7.789   6.066   34.631 1    17.358  ? 460  PHE A N   1 1 
ATOM   3409 C  CA  . PHE A 1 424 ? 7.224   6.652   33.427 1    18.429  ? 460  PHE A CA  1 1 
ATOM   3410 C  C   . PHE A 1 424 ? 7.265   5.642   32.259 1    22.325  ? 460  PHE A C   1 1 
ATOM   3411 O  O   . PHE A 1 424 ? 6.257   5.475   31.545 1    21.181  ? 460  PHE A O   1 1 
ATOM   3412 C  CB  . PHE A 1 424 ? 7.88    7.978   33.024 1    18.076  ? 460  PHE A CB  1 1 
ATOM   3413 C  CG  . PHE A 1 424 ? 7.245   8.545   31.769 1    18.77   ? 460  PHE A CG  1 1 
ATOM   3414 C  CD1 . PHE A 1 424 ? 6.063   9.267   31.857 1    20.52   ? 460  PHE A CD1 1 1 
ATOM   3415 C  CD2 . PHE A 1 424 ? 7.815   8.351   30.505 1    16.374  ? 460  PHE A CD2 1 1 
ATOM   3416 C  CE1 . PHE A 1 424 ? 5.456   9.861   30.734 1    23.553  ? 460  PHE A CE1 1 1 
ATOM   3417 C  CE2 . PHE A 1 424 ? 7.168   8.872   29.379 1    16.424  ? 460  PHE A CE2 1 1 
ATOM   3418 C  CZ  . PHE A 1 424 ? 6.048   9.692   29.494 1    21.638  ? 460  PHE A CZ  1 1 
ATOM   3419 N  N   . SER A 1 425 ? 8.411   4.991   32.042 1    18.365  ? 461  SER A N   1 1 
ATOM   3420 C  CA  . SER A 1 425 ? 8.505   4.099   30.889 1    23.289  ? 461  SER A CA  1 1 
ATOM   3421 C  C   . SER A 1 425 ? 7.58    2.894   31.067 1    23.041  ? 461  SER A C   1 1 
ATOM   3422 O  O   . SER A 1 425 ? 7.166   2.223   30.107 1    22.352  ? 461  SER A O   1 1 
ATOM   3423 C  CB  . SER A 1 425 ? 9.956   3.628   30.629 1    17.939  ? 461  SER A CB  1 1 
ATOM   3424 O  OG  . SER A 1 425 ? 10.444  2.979   31.818 1    21.175  ? 461  SER A OG  1 1 
ATOM   3425 N  N   . TYR A 1 426 ? 7.271   2.607   32.336 1    26.126  ? 462  TYR A N   1 1 
ATOM   3426 C  CA  . TYR A 1 426 ? 6.426   1.479   32.652 1    22.715  ? 462  TYR A CA  1 1 
ATOM   3427 C  C   . TYR A 1 426 ? 4.95    1.76    32.364 1    28.48   ? 462  TYR A C   1 1 
ATOM   3428 O  O   . TYR A 1 426 ? 4.277   0.88    31.802 1    24.854  ? 462  TYR A O   1 1 
ATOM   3429 C  CB  . TYR A 1 426 ? 6.607   1.069   34.109 1    30.141  ? 462  TYR A CB  1 1 
ATOM   3430 C  CG  . TYR A 1 426 ? 5.878   -0.201  34.509 1    26.436  ? 462  TYR A CG  1 1 
ATOM   3431 C  CD1 . TYR A 1 426 ? 6.286   -1.429  34.006 1    31.877  ? 462  TYR A CD1 1 1 
ATOM   3432 C  CD2 . TYR A 1 426 ? 4.785   -0.174  35.369 1    26.017  ? 462  TYR A CD2 1 1 
ATOM   3433 C  CE1 . TYR A 1 426 ? 5.66    -2.608  34.383 1    29.038  ? 462  TYR A CE1 1 1 
ATOM   3434 C  CE2 . TYR A 1 426 ? 4.116   -1.336  35.72  1    23.634  ? 462  TYR A CE2 1 1 
ATOM   3435 C  CZ  . TYR A 1 426 ? 4.623   -2.545  35.295 1    27.983  ? 462  TYR A CZ  1 1 
ATOM   3436 O  OH  . TYR A 1 426 ? 3.969   -3.663  35.611 1    26.656  ? 462  TYR A OH  1 1 
ATOM   3437 N  N   . LEU A 1 427 ? 4.459   2.961   32.74  1    23.923  ? 463  LEU A N   1 1 
ATOM   3438 C  CA  . LEU A 1 427 ? 3.03    3.271   32.705 1    23.382  ? 463  LEU A CA  1 1 
ATOM   3439 C  C   . LEU A 1 427 ? 2.497   3.515   31.293 1    19.777  ? 463  LEU A C   1 1 
ATOM   3440 O  O   . LEU A 1 427 ? 1.308   3.283   31.093 1    18.722  ? 463  LEU A O   1 1 
ATOM   3441 C  CB  . LEU A 1 427 ? 2.638   4.428   33.635 1    24.168  ? 463  LEU A CB  1 1 
ATOM   3442 C  CG  . LEU A 1 427 ? 3.158   5.819   33.301 1    26.207  ? 463  LEU A CG  1 1 
ATOM   3443 C  CD1 . LEU A 1 427 ? 2.044   6.437   32.416 1    22.45   ? 463  LEU A CD1 1 1 
ATOM   3444 C  CD2 . LEU A 1 427 ? 3.335   6.665   34.579 1    26.212  ? 463  LEU A CD2 1 1 
ATOM   3445 N  N   . VAL A 1 428 ? 3.34    3.992   30.354 1    18.474  ? 464  VAL A N   1 1 
ATOM   3446 C  CA  . VAL A 1 428 ? 2.828   4.47    29.068 1    22.08   ? 464  VAL A CA  1 1 
ATOM   3447 C  C   . VAL A 1 428 ? 1.984   3.351   28.428 1    22.474  ? 464  VAL A C   1 1 
ATOM   3448 O  O   . VAL A 1 428 ? 0.849   3.535   28     1    20.084  ? 464  VAL A O   1 1 
ATOM   3449 C  CB  . VAL A 1 428 ? 3.876   5.12    28.113 1    21.322  ? 464  VAL A CB  1 1 
ATOM   3450 C  CG1 . VAL A 1 428 ? 3.366   5.366   26.685 1    18.188  ? 464  VAL A CG1 1 1 
ATOM   3451 C  CG2 . VAL A 1 428 ? 4.46    6.406   28.698 1    18.742  ? 464  VAL A CG2 1 1 
ATOM   3452 N  N   . ASP A 1 429 ? 2.549   2.164   28.357 1    20.624  ? 465  ASP A N   1 1 
ATOM   3453 C  CA  . ASP A 1 429 ? 1.87    1.093   27.651 1    21.338  ? 465  ASP A CA  1 1 
ATOM   3454 C  C   . ASP A 1 429 ? 0.946   0.334   28.596 1    21.45   ? 465  ASP A C   1 1 
ATOM   3455 O  O   . ASP A 1 429 ? -0.01   -0.245  28.102 1    20.035  ? 465  ASP A O   1 1 
ATOM   3456 C  CB  . ASP A 1 429 ? 2.839   0.173   26.913 1    23.638  ? 465  ASP A CB  1 1 
ATOM   3457 C  CG  . ASP A 1 429 ? 3.285   0.64    25.526 1    25.244  ? 465  ASP A CG  1 1 
ATOM   3458 O  OD1 . ASP A 1 429 ? 2.846   1.762   25.085 1    19.404  ? 465  ASP A OD1 1 1 
ATOM   3459 O  OD2 . ASP A 1 429 ? 4.153   -0.077  24.943 1    20.967  ? 465  ASP A OD2 1 1 
ATOM   3460 N  N   . GLN A 1 430 ? 1.112   0.437   29.941 1    18.596  ? 466  GLN A N   1 1 
ATOM   3461 C  CA  . GLN A 1 430 ? -0.009  -0.032  30.736 1    18.968  ? 466  GLN A CA  1 1 
ATOM   3462 C  C   . GLN A 1 430 ? -1.293  0.669   30.31  1    21.429  ? 466  GLN A C   1 1 
ATOM   3463 O  O   . GLN A 1 430 ? -2.342  0.031   30.158 1    21.958  ? 466  GLN A O   1 1 
ATOM   3464 C  CB  . GLN A 1 430 ? 0.158   0.258   32.245 1    18.772  ? 466  GLN A CB  1 1 
ATOM   3465 C  CG  . GLN A 1 430 ? 1.398   -0.38   32.845 1    18.53   ? 466  GLN A CG  1 1 
ATOM   3466 C  CD  . GLN A 1 430 ? 1.493   -1.867  32.614 1    25.499  ? 466  GLN A CD  1 1 
ATOM   3467 O  OE1 . GLN A 1 430 ? 0.496   -2.585  32.576 1    25.025  ? 466  GLN A OE1 1 1 
ATOM   3468 N  NE2 . GLN A 1 430 ? 2.702   -2.346  32.34  1    29.223  ? 466  GLN A NE2 1 1 
ATOM   3469 N  N   . TRP A 1 431 ? -1.22   2.002   30.152 1    19.76   ? 467  TRP A N   1 1 
ATOM   3470 C  CA  . TRP A 1 431 ? -2.375  2.749   29.674 1    20.929  ? 467  TRP A CA  1 1 
ATOM   3471 C  C   . TRP A 1 431 ? -2.834  2.249   28.296 1    18.746  ? 467  TRP A C   1 1 
ATOM   3472 O  O   . TRP A 1 431 ? -4.013  2.067   28.099 1    17.601  ? 467  TRP A O   1 1 
ATOM   3473 C  CB  . TRP A 1 431 ? -2.039  4.263   29.635 1    20.929  ? 467  TRP A CB  1 1 
ATOM   3474 C  CG  . TRP A 1 431 ? -3.212  5.147   29.241 1    20.047  ? 467  TRP A CG  1 1 
ATOM   3475 C  CD1 . TRP A 1 431 ? -4.243  5.614   30.026 1    19.331  ? 467  TRP A CD1 1 1 
ATOM   3476 C  CD2 . TRP A 1 431 ? -3.454  5.662   27.927 1    19.212  ? 467  TRP A CD2 1 1 
ATOM   3477 N  NE1 . TRP A 1 431 ? -5.123  6.364   29.293 1    24.288  ? 467  TRP A NE1 1 1 
ATOM   3478 C  CE2 . TRP A 1 431 ? -4.664  6.414   27.997 1    20.301  ? 467  TRP A CE2 1 1 
ATOM   3479 C  CE3 . TRP A 1 431 ? -2.765  5.543   26.711 1    18.1    ? 467  TRP A CE3 1 1 
ATOM   3480 C  CZ2 . TRP A 1 431 ? -5.214  7.038   26.881 1    22.996  ? 467  TRP A CZ2 1 1 
ATOM   3481 C  CZ3 . TRP A 1 431 ? -3.329  6.146   25.605 1    19.987  ? 467  TRP A CZ3 1 1 
ATOM   3482 C  CH2 . TRP A 1 431 ? -4.53   6.872   25.69  1    21.211  ? 467  TRP A CH2 1 1 
ATOM   3483 N  N   . ARG A 1 432 ? -1.933  2.171   27.298 1    18.77   ? 468  ARG A N   1 1 
ATOM   3484 C  CA  . ARG A 1 432 ? -2.362  1.83    25.931 1    18.935  ? 468  ARG A CA  1 1 
ATOM   3485 C  C   . ARG A 1 432 ? -2.831  0.372   25.834 1    20.692  ? 468  ARG A C   1 1 
ATOM   3486 O  O   . ARG A 1 432 ? -3.774  0.093   25.085 1    20.685  ? 468  ARG A O   1 1 
ATOM   3487 C  CB  . ARG A 1 432 ? -1.292  2.056   24.859 1    20.183  ? 468  ARG A CB  1 1 
ATOM   3488 C  CG  . ARG A 1 432 ? -1.073  3.47    24.314 1    22.837  ? 468  ARG A CG  1 1 
ATOM   3489 C  CD  . ARG A 1 432 ? -0.194  3.533   23.02  1    20.633  ? 468  ARG A CD  1 1 
ATOM   3490 N  NE  . ARG A 1 432 ? 1.24    3.275   23.31  1    18.681  ? 468  ARG A NE  1 1 
ATOM   3491 C  CZ  . ARG A 1 432 ? 2.279   3.884   22.697 1    19.622  ? 468  ARG A CZ  1 1 
ATOM   3492 N  NH1 . ARG A 1 432 ? 2.018   4.627   21.611 1    22.153  ? 468  ARG A NH1 1 1 
ATOM   3493 N  NH2 . ARG A 1 432 ? 3.545   3.732   23.107 1    17.895  ? 468  ARG A NH2 1 1 
ATOM   3494 N  N   . TRP A 1 433 ? -2.212  -0.547  26.617 1    17.743  ? 469  TRP A N   1 1 
ATOM   3495 C  CA  . TRP A 1 433 ? -2.71   -1.93   26.607 1    19.821  ? 469  TRP A CA  1 1 
ATOM   3496 C  C   . TRP A 1 433 ? -4.176  -1.991  27.014 1    22.881  ? 469  TRP A C   1 1 
ATOM   3497 O  O   . TRP A 1 433 ? -4.952  -2.73   26.384 1    22.99   ? 469  TRP A O   1 1 
ATOM   3498 C  CB  . TRP A 1 433 ? -1.929  -2.883  27.496 1    18.772  ? 469  TRP A CB  1 1 
ATOM   3499 C  CG  . TRP A 1 433 ? -0.524  -3.094  27.009 1    22.061  ? 469  TRP A CG  1 1 
ATOM   3500 C  CD1 . TRP A 1 433 ? 0.02    -2.791  25.789 1    19.594  ? 469  TRP A CD1 1 1 
ATOM   3501 C  CD2 . TRP A 1 433 ? 0.538   -3.639  27.819 1    23.682  ? 469  TRP A CD2 1 1 
ATOM   3502 N  NE1 . TRP A 1 433 ? 1.362   -3.07   25.784 1    21.264  ? 469  TRP A NE1 1 1 
ATOM   3503 C  CE2 . TRP A 1 433 ? 1.706   -3.622  27.01  1    24.471  ? 469  TRP A CE2 1 1 
ATOM   3504 C  CE3 . TRP A 1 433 ? 0.595   -4.141  29.129 1    21.105  ? 469  TRP A CE3 1 1 
ATOM   3505 C  CZ2 . TRP A 1 433 ? 2.939   -4.098  27.491 1    23.326  ? 469  TRP A CZ2 1 1 
ATOM   3506 C  CZ3 . TRP A 1 433 ? 1.819   -4.585  29.606 1    24.421  ? 469  TRP A CZ3 1 1 
ATOM   3507 C  CH2 . TRP A 1 433 ? 2.986   -4.518  28.81  1    24.851  ? 469  TRP A CH2 1 1 
ATOM   3508 N  N   . ARG A 1 434 ? -4.562  -1.065  27.92  1    24.125  ? 470  ARG A N   1 1 
ATOM   3509 C  CA  . ARG A 1 434 ? -5.94   -1.089  28.432 1    22.365  ? 470  ARG A CA  1 1 
ATOM   3510 C  C   . ARG A 1 434 ? -6.869  -0.316  27.487 1    20.712  ? 470  ARG A C   1 1 
ATOM   3511 O  O   . ARG A 1 434 ? -8.068  -0.595  27.415 1    20.536  ? 470  ARG A O   1 1 
ATOM   3512 C  CB  . ARG A 1 434 ? -5.968  -0.57   29.877 1    22.459  ? 470  ARG A CB  1 1 
ATOM   3513 C  CG  . ARG A 1 434 ? -5.363  -1.575  30.872 1    26.514  ? 470  ARG A CG  1 1 
ATOM   3514 C  CD  . ARG A 1 434 ? -5.293  -1.119  32.366 1    29.454  ? 470  ARG A CD  1 1 
ATOM   3515 N  NE  . ARG A 1 434 ? -6.523  -0.421  32.812 1    34.171  ? 470  ARG A NE  1 1 
ATOM   3516 C  CZ  . ARG A 1 434 ? -6.539  0.704   33.526 1    33.559  ? 470  ARG A CZ  1 1 
ATOM   3517 N  NH1 . ARG A 1 434 ? -5.419  1.305   33.895 1    31.332  ? 470  ARG A NH1 1 1 
ATOM   3518 N  NH2 . ARG A 1 434 ? -7.688  1.23    33.875 1    37.258  ? 470  ARG A NH2 1 1 
ATOM   3519 N  N   . VAL A 1 435 ? -6.313  0.653   26.745 1    20.757  ? 471  VAL A N   1 1 
ATOM   3520 C  CA  . VAL A 1 435 ? -7.146  1.294   25.73  1    21.776  ? 471  VAL A CA  1 1 
ATOM   3521 C  C   . VAL A 1 435 ? -7.395  0.262   24.638 1    21.683  ? 471  VAL A C   1 1 
ATOM   3522 O  O   . VAL A 1 435 ? -8.523  0.063   24.167 1    20.547  ? 471  VAL A O   1 1 
ATOM   3523 C  CB  . VAL A 1 435 ? -6.46   2.508   25.114 1    22.138  ? 471  VAL A CB  1 1 
ATOM   3524 C  CG1 . VAL A 1 435 ? -7.163  2.963   23.847 1    25.002  ? 471  VAL A CG1 1 1 
ATOM   3525 C  CG2 . VAL A 1 435 ? -6.267  3.644   26.103 1    20.278  ? 471  VAL A CG2 1 1 
ATOM   3526 N  N   . PHE A 1 436 ? -6.319  -0.404  24.219 1    19.06   ? 472  PHE A N   1 1 
ATOM   3527 C  CA  . PHE A 1 436 ? -6.522  -1.311  23.08  1    21.247  ? 472  PHE A CA  1 1 
ATOM   3528 C  C   . PHE A 1 436 ? -7.456  -2.482  23.435 1    20.398  ? 472  PHE A C   1 1 
ATOM   3529 O  O   . PHE A 1 436 ? -8.241  -2.967  22.594 1    18.743  ? 472  PHE A O   1 1 
ATOM   3530 C  CB  . PHE A 1 436 ? -5.187  -1.879  22.58  1    18.754  ? 472  PHE A CB  1 1 
ATOM   3531 C  CG  . PHE A 1 436 ? -4.223  -0.901  21.907 1    20.06   ? 472  PHE A CG  1 1 
ATOM   3532 C  CD1 . PHE A 1 436 ? -4.697  0.075   21.027 1    20.877  ? 472  PHE A CD1 1 1 
ATOM   3533 C  CD2 . PHE A 1 436 ? -2.84   -0.993  22.116 1    18.67   ? 472  PHE A CD2 1 1 
ATOM   3534 C  CE1 . PHE A 1 436 ? -3.818  0.97    20.403 1    22.308  ? 472  PHE A CE1 1 1 
ATOM   3535 C  CE2 . PHE A 1 436 ? -1.956  -0.203  21.413 1    19.636  ? 472  PHE A CE2 1 1 
ATOM   3536 C  CZ  . PHE A 1 436 ? -2.44   0.842   20.609 1    20.182  ? 472  PHE A CZ  1 1 
ATOM   3537 N  N   . ASP A 1 437 ? -7.332  -3.023  24.665 1    22.362  ? 473  ASP A N   1 1 
ATOM   3538 C  CA  . ASP A 1 437 ? -8.247  -4.113  25.017 1    24.243  ? 473  ASP A CA  1 1 
ATOM   3539 C  C   . ASP A 1 437 ? -9.612  -3.592  25.433 1    24.147  ? 473  ASP A C   1 1 
ATOM   3540 O  O   . ASP A 1 437 ? -10.453 -4.387  25.761 1    24.922  ? 473  ASP A O   1 1 
ATOM   3541 C  CB  . ASP A 1 437 ? -7.745  -5.104  26.055 1    27.19   ? 473  ASP A CB  1 1 
ATOM   3542 C  CG  . ASP A 1 437 ? -7.724  -4.581  27.49  1    28.364  ? 473  ASP A CG  1 1 
ATOM   3543 O  OD1 . ASP A 1 437 ? -8.351  -3.553  27.789 1    33.722  ? 473  ASP A OD1 1 1 
ATOM   3544 O  OD2 . ASP A 1 437 ? -7.017  -5.156  28.307 1    37.418  ? 473  ASP A OD2 1 1 
ATOM   3545 N  N   . GLY A 1 438 ? -9.845  -2.27   25.425 1    26.361  ? 474  GLY A N   1 1 
ATOM   3546 C  CA  . GLY A 1 438 ? -11.213 -1.815  25.543 1    25.41   ? 474  GLY A CA  1 1 
ATOM   3547 C  C   . GLY A 1 438 ? -11.625 -1.464  26.981 1    30.405  ? 474  GLY A C   1 1 
ATOM   3548 O  O   . GLY A 1 438 ? -12.697 -0.882  27.163 1    34.295  ? 474  GLY A O   1 1 
ATOM   3549 N  N   A SER A 1 439 ? -10.767 -1.81   27.954 0.43 27.213  ? 475  SER A N   1 1 
ATOM   3550 N  N   B SER A 1 439 ? -10.785 -1.744  27.988 0.57 28.03   ? 475  SER A N   1 1 
ATOM   3551 C  CA  A SER A 1 439 ? -10.909 -1.463  29.364 0.43 28.401  ? 475  SER A CA  1 1 
ATOM   3552 C  CA  B SER A 1 439 ? -11.114 -1.42   29.378 0.57 30.406  ? 475  SER A CA  1 1 
ATOM   3553 C  C   A SER A 1 439 ? -11.093 0.039   29.593 0.43 28.16   ? 475  SER A C   1 1 
ATOM   3554 C  C   B SER A 1 439 ? -10.942 0.067   29.75  0.57 28.815  ? 475  SER A C   1 1 
ATOM   3555 O  O   A SER A 1 439 ? -11.947 0.417   30.385 0.43 28.027  ? 475  SER A O   1 1 
ATOM   3556 O  O   B SER A 1 439 ? -11.388 0.504   30.795 0.57 28.639  ? 475  SER A O   1 1 
ATOM   3557 C  CB  A SER A 1 439 ? -9.749  -2.001  30.181 0.43 26.229  ? 475  SER A CB  1 1 
ATOM   3558 C  CB  B SER A 1 439 ? -10.392 -2.356  30.338 0.57 31.749  ? 475  SER A CB  1 1 
ATOM   3559 O  OG  A SER A 1 439 ? -9.762  -3.421  30.142 0.43 24.049  ? 475  SER A OG  1 1 
ATOM   3560 O  OG  B SER A 1 439 ? -8.984  -2.192  30.271 0.57 27.825  ? 475  SER A OG  1 1 
ATOM   3561 N  N   . ILE A 1 440 ? -10.289 0.875   28.907 1    28.682  ? 476  ILE A N   1 1 
ATOM   3562 C  CA  . ILE A 1 440 ? -10.386 2.333   28.965 1    25.088  ? 476  ILE A CA  1 1 
ATOM   3563 C  C   . ILE A 1 440 ? -11.099 2.787   27.698 1    26.584  ? 476  ILE A C   1 1 
ATOM   3564 O  O   . ILE A 1 440 ? -10.658 2.444   26.615 1    27.92   ? 476  ILE A O   1 1 
ATOM   3565 C  CB  . ILE A 1 440 ? -8.963  2.954   29.029 1    23.108  ? 476  ILE A CB  1 1 
ATOM   3566 C  CG1 . ILE A 1 440 ? -8.157  2.383   30.249 1    20.16   ? 476  ILE A CG1 1 1 
ATOM   3567 C  CG2 . ILE A 1 440 ? -8.977  4.515   29.015 1    19.314  ? 476  ILE A CG2 1 1 
ATOM   3568 C  CD1 . ILE A 1 440 ? -6.689  2.833   30.302 1    16.991  ? 476  ILE A CD1 1 1 
ATOM   3569 N  N   . THR A 1 441 ? -12.152 3.603   27.798 1    31.637  ? 477  THR A N   1 1 
ATOM   3570 C  CA  . THR A 1 441 ? -12.854 4.143   26.631 1    28.373  ? 477  THR A CA  1 1 
ATOM   3571 C  C   . THR A 1 441 ? -12.523 5.63    26.508 1    28.231  ? 477  THR A C   1 1 
ATOM   3572 O  O   . THR A 1 441 ? -11.892 6.184   27.415 1    24.945  ? 477  THR A O   1 1 
ATOM   3573 C  CB  . THR A 1 441 ? -14.366 3.905   26.745 1    27.795  ? 477  THR A CB  1 1 
ATOM   3574 O  OG1 . THR A 1 441 ? -14.861 4.911   27.622 1    27.836  ? 477  THR A OG1 1 1 
ATOM   3575 C  CG2 . THR A 1 441 ? -14.737 2.545   27.314 1    25.299  ? 477  THR A CG2 1 1 
ATOM   3576 N  N   . LYS A 1 442 ? -12.996 6.279   25.424 1    26.488  ? 478  LYS A N   1 1 
ATOM   3577 C  CA  . LYS A 1 442 ? -12.708 7.698   25.208 1    29.412  ? 478  LYS A CA  1 1 
ATOM   3578 C  C   . LYS A 1 442 ? -13.355 8.561   26.287 1    31.323  ? 478  LYS A C   1 1 
ATOM   3579 O  O   . LYS A 1 442 ? -12.979 9.709   26.458 1    36.2    ? 478  LYS A O   1 1 
ATOM   3580 C  CB  . LYS A 1 442 ? -13.157 8.269   23.856 1    29.935  ? 478  LYS A CB  1 1 
ATOM   3581 C  CG  . LYS A 1 442 ? -14.673 8.44    23.59  1    32.045  ? 478  LYS A CG  1 1 
ATOM   3582 C  CD  . LYS A 1 442 ? -15.049 8.891   22.168 1    31.223  ? 478  LYS A CD  1 1 
ATOM   3583 C  CE  . LYS A 1 442 ? -16.462 9.44    22.119 1    34.061  ? 478  LYS A CE  1 1 
ATOM   3584 N  NZ  . LYS A 1 442 ? -16.968 9.357   20.74  1    35.675  ? 478  LYS A NZ  1 1 
ATOM   3585 N  N   . GLU A 1 443 ? -14.339 8.007   26.998 1    31.927  ? 479  GLU A N   1 1 
ATOM   3586 C  CA  . GLU A 1 443 ? -14.918 8.681   28.137 1    30.063  ? 479  GLU A CA  1 1 
ATOM   3587 C  C   . GLU A 1 443 ? -13.887 8.774   29.254 1    30.39   ? 479  GLU A C   1 1 
ATOM   3588 O  O   . GLU A 1 443 ? -13.954 9.72    29.999 1    31.693  ? 479  GLU A O   1 1 
ATOM   3589 C  CB  . GLU A 1 443 ? -16.102 7.989   28.805 1    31.662  ? 479  GLU A CB  1 1 
ATOM   3590 C  CG  . GLU A 1 443 ? -17.304 7.788   27.893 1    38.179  ? 479  GLU A CG  1 1 
ATOM   3591 C  CD  . GLU A 1 443 ? -18.128 6.657   28.524 1    47.749  ? 479  GLU A CD  1 1 
ATOM   3592 O  OE1 . GLU A 1 443 ? -17.631 5.494   28.827 1    42.994  ? 479  GLU A OE1 1 1 
ATOM   3593 O  OE2 . GLU A 1 443 ? -19.315 6.978   28.719 1    44.134  ? 479  GLU A OE2 1 1 
ATOM   3594 N  N   . ASN A 1 444 ? -12.929 7.852   29.375 1    27.581  ? 480  ASN A N   1 1 
ATOM   3595 C  CA  . ASN A 1 444 ? -12.019 8.038   30.482 1    25.549  ? 480  ASN A CA  1 1 
ATOM   3596 C  C   . ASN A 1 444 ? -10.544 7.87    30.11  1    24.9    ? 480  ASN A C   1 1 
ATOM   3597 O  O   . ASN A 1 444 ? -9.694  7.635   30.988 1    22.753  ? 480  ASN A O   1 1 
ATOM   3598 C  CB  . ASN A 1 444 ? -12.558 7.373   31.726 1    29.799  ? 480  ASN A CB  1 1 
ATOM   3599 C  CG  . ASN A 1 444 ? -12.6   5.917   31.453 1    35.832  ? 480  ASN A CG  1 1 
ATOM   3600 O  OD1 . ASN A 1 444 ? -12.239 5.505   30.345 1    38.473  ? 480  ASN A OD1 1 1 
ATOM   3601 N  ND2 . ASN A 1 444 ? -13.072 5.141   32.409 1    45.285  ? 480  ASN A ND2 1 1 
ATOM   3602 N  N   . TYR A 1 445 ? -10.195 8.129   28.838 1    22.067  ? 481  TYR A N   1 1 
ATOM   3603 C  CA  . TYR A 1 445 ? -8.773  8.155   28.545 1    22.397  ? 481  TYR A CA  1 1 
ATOM   3604 C  C   . TYR A 1 445 ? -7.943  8.894   29.618 1    22.238  ? 481  TYR A C   1 1 
ATOM   3605 O  O   . TYR A 1 445 ? -6.937  8.381   30.148 1    20.996  ? 481  TYR A O   1 1 
ATOM   3606 C  CB  . TYR A 1 445 ? -8.71   8.955   27.251 1    20.916  ? 481  TYR A CB  1 1 
ATOM   3607 C  CG  . TYR A 1 445 ? -9.055  8.241   25.956 1    21.88   ? 481  TYR A CG  1 1 
ATOM   3608 C  CD1 . TYR A 1 445 ? -9.109  6.846   25.824 1    21.969  ? 481  TYR A CD1 1 1 
ATOM   3609 C  CD2 . TYR A 1 445 ? -9.312  9.027   24.831 1    23.664  ? 481  TYR A CD2 1 1 
ATOM   3610 C  CE1 . TYR A 1 445 ? -9.385  6.246   24.599 1    22.628  ? 481  TYR A CE1 1 1 
ATOM   3611 C  CE2 . TYR A 1 445 ? -9.576  8.442   23.601 1    24.738  ? 481  TYR A CE2 1 1 
ATOM   3612 C  CZ  . TYR A 1 445 ? -9.617  7.056   23.484 1    23.717  ? 481  TYR A CZ  1 1 
ATOM   3613 O  OH  . TYR A 1 445 ? -9.86   6.617   22.205 1    25.34   ? 481  TYR A OH  1 1 
ATOM   3614 N  N   . ASN A 1 446 ? -8.34   10.158  29.898 1    20.855  ? 482  ASN A N   1 1 
ATOM   3615 C  CA  . ASN A 1 446 ? -7.489  11.113  30.581 1    20.475  ? 482  ASN A CA  1 1 
ATOM   3616 C  C   . ASN A 1 446 ? -7.399  10.729  32.056 1    22.209  ? 482  ASN A C   1 1 
ATOM   3617 O  O   . ASN A 1 446 ? -6.313  10.82   32.673 1    22.334  ? 482  ASN A O   1 1 
ATOM   3618 C  CB  . ASN A 1 446 ? -7.958  12.564  30.32  1    20.724  ? 482  ASN A CB  1 1 
ATOM   3619 C  CG  . ASN A 1 446 ? -6.76   13.491  30.348 1    24.85   ? 482  ASN A CG  1 1 
ATOM   3620 O  OD1 . ASN A 1 446 ? -5.81   13.306  29.559 1    24.548  ? 482  ASN A OD1 1 1 
ATOM   3621 N  ND2 . ASN A 1 446 ? -6.713  14.407  31.31  1    20.931  ? 482  ASN A ND2 1 1 
ATOM   3622 N  N   . GLN A 1 447 ? -8.585  10.426  32.647 1    21.216  ? 483  GLN A N   1 1 
ATOM   3623 C  CA  . GLN A 1 447 ? -8.678  10.108  34.071 1    22.444  ? 483  GLN A CA  1 1 
ATOM   3624 C  C   . GLN A 1 447 ? -7.805  8.885   34.346 1    21.767  ? 483  GLN A C   1 1 
ATOM   3625 O  O   . GLN A 1 447 ? -7.103  8.767   35.381 1    20.507  ? 483  GLN A O   1 1 
ATOM   3626 C  CB  . GLN A 1 447 ? -10.133 9.833   34.514 1    23.204  ? 483  GLN A CB  1 1 
ATOM   3627 C  CG  . GLN A 1 447 ? -11.11  11.024  34.467 1    27.336  ? 483  GLN A CG  1 1 
ATOM   3628 C  CD  . GLN A 1 447 ? -11.689 11.383  33.087 1    34.616  ? 483  GLN A CD  1 1 
ATOM   3629 O  OE1 . GLN A 1 447 ? -11.313 10.91   31.975 1    28.871  ? 483  GLN A OE1 1 1 
ATOM   3630 N  NE2 . GLN A 1 447 ? -12.668 12.274  33.152 1    33.333  ? 483  GLN A NE2 1 1 
ATOM   3631 N  N   A GLU A 1 448 ? -7.88   7.938   33.405 0.61 23.92   ? 484  GLU A N   1 1 
ATOM   3632 N  N   B GLU A 1 448 ? -7.834  7.93    33.407 0.39 23.108  ? 484  GLU A N   1 1 
ATOM   3633 C  CA  A GLU A 1 448 ? -7.089  6.704   33.518 0.61 23.477  ? 484  GLU A CA  1 1 
ATOM   3634 C  CA  B GLU A 1 448 ? -7.057  6.698   33.582 0.39 22.34   ? 484  GLU A CA  1 1 
ATOM   3635 C  C   A GLU A 1 448 ? -5.578  6.963   33.389 0.61 22.41   ? 484  GLU A C   1 1 
ATOM   3636 C  C   B GLU A 1 448 ? -5.554  6.942   33.385 0.39 21.785  ? 484  GLU A C   1 1 
ATOM   3637 O  O   A GLU A 1 448 ? -4.767  6.338   34.071 0.61 25.353  ? 484  GLU A O   1 1 
ATOM   3638 O  O   B GLU A 1 448 ? -4.731  6.293   34.03  0.39 23.444  ? 484  GLU A O   1 1 
ATOM   3639 C  CB  A GLU A 1 448 ? -7.662  5.658   32.552 0.61 24.416  ? 484  GLU A CB  1 1 
ATOM   3640 C  CB  B GLU A 1 448 ? -7.657  5.569   32.736 0.39 22.703  ? 484  GLU A CB  1 1 
ATOM   3641 C  CG  A GLU A 1 448 ? -9.135  5.311   32.802 0.61 25.816  ? 484  GLU A CG  1 1 
ATOM   3642 C  CG  B GLU A 1 448 ? -7.366  4.157   33.252 0.39 23.071  ? 484  GLU A CG  1 1 
ATOM   3643 C  CD  A GLU A 1 448 ? -9.445  4.942   34.236 0.61 30.445  ? 484  GLU A CD  1 1 
ATOM   3644 C  CD  B GLU A 1 448 ? -7.3    3.981   34.769 0.39 22.245  ? 484  GLU A CD  1 1 
ATOM   3645 O  OE1 A GLU A 1 448 ? -9.125  3.8     34.555 0.61 29.855  ? 484  GLU A OE1 1 1 
ATOM   3646 O  OE1 B GLU A 1 448 ? -8.295  4.358   35.443 0.39 20.337  ? 484  GLU A OE1 1 1 
ATOM   3647 O  OE2 A GLU A 1 448 ? -9.926  5.779   35.046 0.61 32.343  ? 484  GLU A OE2 1 1 
ATOM   3648 O  OE2 B GLU A 1 448 ? -6.212  3.554   35.249 0.39 20.143  ? 484  GLU A OE2 1 1 
ATOM   3649 N  N   . TRP A 1 449 ? -5.184  7.866   32.495 1    21.723  ? 485  TRP A N   1 1 
ATOM   3650 C  CA  . TRP A 1 449 ? -3.792  8.301   32.426 1    20.483  ? 485  TRP A CA  1 1 
ATOM   3651 C  C   . TRP A 1 449 ? -3.342  8.88    33.774 1    19.538  ? 485  TRP A C   1 1 
ATOM   3652 O  O   . TRP A 1 449 ? -2.305  8.493   34.259 1    17.449  ? 485  TRP A O   1 1 
ATOM   3653 C  CB  . TRP A 1 449 ? -3.656  9.335   31.308 1    18.028  ? 485  TRP A CB  1 1 
ATOM   3654 C  CG  . TRP A 1 449 ? -2.302  9.974   31.175 1    18.656  ? 485  TRP A CG  1 1 
ATOM   3655 C  CD1 . TRP A 1 449 ? -1.949  11.24   31.558 1    17.549  ? 485  TRP A CD1 1 1 
ATOM   3656 C  CD2 . TRP A 1 449 ? -1.153  9.408   30.5   1    18.873  ? 485  TRP A CD2 1 1 
ATOM   3657 N  NE1 . TRP A 1 449 ? -0.663  11.507  31.129 1    21.066  ? 485  TRP A NE1 1 1 
ATOM   3658 C  CE2 . TRP A 1 449 ? -0.15   10.406  30.493 1    19.049  ? 485  TRP A CE2 1 1 
ATOM   3659 C  CE3 . TRP A 1 449 ? -0.898  8.17    29.87  1    19.95   ? 485  TRP A CE3 1 1 
ATOM   3660 C  CZ2 . TRP A 1 449 ? 1.099   10.197  29.882 1    20.725  ? 485  TRP A CZ2 1 1 
ATOM   3661 C  CZ3 . TRP A 1 449 ? 0.326   7.976   29.234 1    20.177  ? 485  TRP A CZ3 1 1 
ATOM   3662 C  CH2 . TRP A 1 449 ? 1.293   8.988   29.23  1    20.094  ? 485  TRP A CH2 1 1 
ATOM   3663 N  N   . TRP A 1 450 ? -4.094  9.841   34.332 1    20.171  ? 486  TRP A N   1 1 
ATOM   3664 C  CA  . TRP A 1 450 ? -3.752  10.451  35.615 1    22.6    ? 486  TRP A CA  1 1 
ATOM   3665 C  C   . TRP A 1 450 ? -3.702  9.441   36.761 1    22.304  ? 486  TRP A C   1 1 
ATOM   3666 O  O   . TRP A 1 450 ? -2.843  9.527   37.627 1    23.613  ? 486  TRP A O   1 1 
ATOM   3667 C  CB  . TRP A 1 450 ? -4.522  11.749  35.913 1    20.518  ? 486  TRP A CB  1 1 
ATOM   3668 C  CG  . TRP A 1 450 ? -3.857  12.82   35.088 1    20.961  ? 486  TRP A CG  1 1 
ATOM   3669 C  CD1 . TRP A 1 450 ? -4.238  13.215  33.831 1    21.912  ? 486  TRP A CD1 1 1 
ATOM   3670 C  CD2 . TRP A 1 450 ? -2.558  13.396  35.306 1    19.594  ? 486  TRP A CD2 1 1 
ATOM   3671 N  NE1 . TRP A 1 450 ? -3.324  14.094  33.296 1    22.278  ? 486  TRP A NE1 1 1 
ATOM   3672 C  CE2 . TRP A 1 450 ? -2.254  14.177  34.149 1    20.774  ? 486  TRP A CE2 1 1 
ATOM   3673 C  CE3 . TRP A 1 450 ? -1.614  13.346  36.348 1    20.864  ? 486  TRP A CE3 1 1 
ATOM   3674 C  CZ2 . TRP A 1 450 ? -1.073  14.918  34.042 1    20.779  ? 486  TRP A CZ2 1 1 
ATOM   3675 C  CZ3 . TRP A 1 450 ? -0.413  14.011  36.196 1    21.108  ? 486  TRP A CZ3 1 1 
ATOM   3676 C  CH2 . TRP A 1 450 ? -0.161  14.841  35.086 1    20.52   ? 486  TRP A CH2 1 1 
ATOM   3677 N  N   A SER A 1 451 ? -4.591  8.448   36.726 0.44 21.439  ? 487  SER A N   1 1 
ATOM   3678 N  N   B SER A 1 451 ? -4.623  8.484   36.731 0.38 22.497  ? 487  SER A N   1 1 
ATOM   3679 N  N   C SER A 1 451 ? -4.592  8.441   36.72  0.18 22.202  ? 487  SER A N   1 1 
ATOM   3680 C  CA  A SER A 1 451 ? -4.558  7.399   37.734 0.44 21.092  ? 487  SER A CA  1 1 
ATOM   3681 C  CA  B SER A 1 451 ? -4.56   7.4     37.689 0.38 22.941  ? 487  SER A CA  1 1 
ATOM   3682 C  CA  C SER A 1 451 ? -4.585  7.377   37.714 0.18 21.992  ? 487  SER A CA  1 1 
ATOM   3683 C  C   A SER A 1 451 ? -3.232  6.633   37.736 0.44 20.79   ? 487  SER A C   1 1 
ATOM   3684 C  C   B SER A 1 451 ? -3.151  6.804   37.743 0.38 21.514  ? 487  SER A C   1 1 
ATOM   3685 C  C   C SER A 1 451 ? -3.234  6.656   37.738 0.18 20.954  ? 487  SER A C   1 1 
ATOM   3686 O  O   A SER A 1 451 ? -2.774  6.196   38.797 0.44 20.085  ? 487  SER A O   1 1 
ATOM   3687 O  O   B SER A 1 451 ? -2.577  6.617   38.818 0.38 20.598  ? 487  SER A O   1 1 
ATOM   3688 O  O   C SER A 1 451 ? -2.767  6.25    38.804 0.18 20.518  ? 487  SER A O   1 1 
ATOM   3689 C  CB  A SER A 1 451 ? -5.761  6.517   37.647 0.44 19.975  ? 487  SER A CB  1 1 
ATOM   3690 C  CB  B SER A 1 451 ? -5.573  6.365   37.367 0.38 23.496  ? 487  SER A CB  1 1 
ATOM   3691 C  CB  C SER A 1 451 ? -5.741  6.415   37.538 0.18 22.341  ? 487  SER A CB  1 1 
ATOM   3692 O  OG  A SER A 1 451 ? -6.876  7.334   37.954 0.44 17.899  ? 487  SER A OG  1 1 
ATOM   3693 O  OG  B SER A 1 451 ? -5.855  5.698   38.577 0.38 25.033  ? 487  SER A OG  1 1 
ATOM   3694 O  OG  C SER A 1 451 ? -5.498  5.476   36.499 0.18 22.088  ? 487  SER A OG  1 1 
ATOM   3695 N  N   . LEU A 1 452 ? -2.604  6.53    36.563 1    19.123  ? 488  LEU A N   1 1 
ATOM   3696 C  CA  . LEU A 1 452 ? -1.375  5.782   36.423 1    20.517  ? 488  LEU A CA  1 1 
ATOM   3697 C  C   . LEU A 1 452 ? -0.208  6.705   36.74  1    18.748  ? 488  LEU A C   1 1 
ATOM   3698 O  O   . LEU A 1 452 ? 0.747   6.26    37.367 1    18.107  ? 488  LEU A O   1 1 
ATOM   3699 C  CB  . LEU A 1 452 ? -1.262  5.207   35.014 1    19.652  ? 488  LEU A CB  1 1 
ATOM   3700 C  CG  . LEU A 1 452 ? -2.264  4.082   34.745 1    23.367  ? 488  LEU A CG  1 1 
ATOM   3701 C  CD1 . LEU A 1 452 ? -2.151  3.656   33.308 1    25.207  ? 488  LEU A CD1 1 1 
ATOM   3702 C  CD2 . LEU A 1 452 ? -2.115  2.849   35.627 1    23.25   ? 488  LEU A CD2 1 1 
ATOM   3703 N  N   . ARG A 1 453 ? -0.328  7.979   36.321 1    18.359  ? 489  ARG A N   1 1 
ATOM   3704 C  CA  . ARG A 1 453 ? 0.658   8.984   36.679 1    19.306  ? 489  ARG A CA  1 1 
ATOM   3705 C  C   . ARG A 1 453 ? 0.82    9.016   38.211 1    17.791  ? 489  ARG A C   1 1 
ATOM   3706 O  O   . ARG A 1 453 ? 1.961   9.128   38.712 1    17.874  ? 489  ARG A O   1 1 
ATOM   3707 C  CB  . ARG A 1 453 ? 0.36    10.336  35.976 1    20.173  ? 489  ARG A CB  1 1 
ATOM   3708 C  CG  . ARG A 1 453 ? 0.45    10.309  34.434 1    19.833  ? 489  ARG A CG  1 1 
ATOM   3709 C  CD  . ARG A 1 453 ? 1.833   10.699  33.912 1    17.231  ? 489  ARG A CD  1 1 
ATOM   3710 N  NE  . ARG A 1 453 ? 1.928   12.18   33.879 1    16.793  ? 489  ARG A NE  1 1 
ATOM   3711 C  CZ  . ARG A 1 453 ? 3.083   12.824  33.718 1    19.017  ? 489  ARG A CZ  1 1 
ATOM   3712 N  NH1 . ARG A 1 453 ? 3.074   14.108  33.387 1    20.113  ? 489  ARG A NH1 1 1 
ATOM   3713 N  NH2 . ARG A 1 453 ? 4.236   12.181  33.774 1    17.715  ? 489  ARG A NH2 1 1 
ATOM   3714 N  N   . LEU A 1 454 ? -0.314  8.965   38.924 1    16.171  ? 490  LEU A N   1 1 
ATOM   3715 C  CA  . LEU A 1 454 ? -0.298  9.013   40.381 1    19.278  ? 490  LEU A CA  1 1 
ATOM   3716 C  C   . LEU A 1 454 ? 0.252   7.68    40.92  1    21.701  ? 490  LEU A C   1 1 
ATOM   3717 O  O   . LEU A 1 454 ? 1.204   7.624   41.688 1    24.397  ? 490  LEU A O   1 1 
ATOM   3718 C  CB  . LEU A 1 454 ? -1.718  9.248   40.908 1    19.674  ? 490  LEU A CB  1 1 
ATOM   3719 C  CG  . LEU A 1 454 ? -1.824  9.178   42.444 1    23.485  ? 490  LEU A CG  1 1 
ATOM   3720 C  CD1 . LEU A 1 454 ? -0.876  10.16   43.071 1    21.276  ? 490  LEU A CD1 1 1 
ATOM   3721 C  CD2 . LEU A 1 454 ? -3.271  9.449   42.956 1    22.7    ? 490  LEU A CD2 1 1 
ATOM   3722 N  N   . LYS A 1 455 ? -0.316  6.58    40.464 1    20.85   ? 491  LYS A N   1 1 
ATOM   3723 C  CA  . LYS A 1 455 ? 0.024   5.29    41.044 1    24.308  ? 491  LYS A CA  1 1 
ATOM   3724 C  C   . LYS A 1 455 ? 1.509   4.935   40.846 1    23.199  ? 491  LYS A C   1 1 
ATOM   3725 O  O   . LYS A 1 455 ? 2.179   4.533   41.801 1    19.567  ? 491  LYS A O   1 1 
ATOM   3726 C  CB  . LYS A 1 455 ? -0.914  4.195   40.544 1    26.437  ? 491  LYS A CB  1 1 
ATOM   3727 C  CG  . LYS A 1 455 ? -0.475  2.775   40.88  1    26.885  ? 491  LYS A CG  1 1 
ATOM   3728 C  CD  . LYS A 1 455 ? -1.358  1.769   40.119 1    36.171  ? 491  LYS A CD  1 1 
ATOM   3729 C  CE  . LYS A 1 455 ? -1.135  0.413   40.798 1    45.906  ? 491  LYS A CE  1 1 
ATOM   3730 N  NZ  . LYS A 1 455 ? -1.951  -0.715  40.321 1    42.263  ? 491  LYS A NZ  1 1 
ATOM   3731 N  N   . TYR A 1 456 ? 2.02    5.11    39.625 1    17.752  ? 492  TYR A N   1 1 
ATOM   3732 C  CA  . TYR A 1 456 ? 3.38    4.725   39.332 1    21.344  ? 492  TYR A CA  1 1 
ATOM   3733 C  C   . TYR A 1 456 ? 4.385   5.844   39.624 1    21.975  ? 492  TYR A C   1 1 
ATOM   3734 O  O   . TYR A 1 456 ? 5.443   5.541   40.189 1    21.641  ? 492  TYR A O   1 1 
ATOM   3735 C  CB  . TYR A 1 456 ? 3.453   4.295   37.849 1    22.199  ? 492  TYR A CB  1 1 
ATOM   3736 C  CG  . TYR A 1 456 ? 2.755   2.961   37.691 1    27.734  ? 492  TYR A CG  1 1 
ATOM   3737 C  CD1 . TYR A 1 456 ? 3.043   1.909   38.57  1    28.602  ? 492  TYR A CD1 1 1 
ATOM   3738 C  CD2 . TYR A 1 456 ? 1.739   2.785   36.739 1    28.311  ? 492  TYR A CD2 1 1 
ATOM   3739 C  CE1 . TYR A 1 456 ? 2.401   0.692   38.428 1    33.886  ? 492  TYR A CE1 1 1 
ATOM   3740 C  CE2 . TYR A 1 456 ? 1.07    1.568   36.622 1    28.739  ? 492  TYR A CE2 1 1 
ATOM   3741 C  CZ  . TYR A 1 456 ? 1.39    0.552   37.487 1    33.792  ? 492  TYR A CZ  1 1 
ATOM   3742 O  OH  . TYR A 1 456 ? 0.693   -0.588  37.331 1    49.899  ? 492  TYR A OH  1 1 
ATOM   3743 N  N   . GLN A 1 457 ? 4.14    7.084   39.123 1    18.23   ? 493  GLN A N   1 1 
ATOM   3744 C  CA  . GLN A 1 457 ? 5.165   8.127   39.299 1    17.82   ? 493  GLN A CA  1 1 
ATOM   3745 C  C   . GLN A 1 457 ? 4.946   8.927   40.589 1    18.19   ? 493  GLN A C   1 1 
ATOM   3746 O  O   . GLN A 1 457 ? 5.836   9.626   41.009 1    20.33   ? 493  GLN A O   1 1 
ATOM   3747 C  CB  . GLN A 1 457 ? 5.278   9.09    38.121 1    16.782  ? 493  GLN A CB  1 1 
ATOM   3748 C  CG  . GLN A 1 457 ? 5.82    8.474   36.843 1    16.9    ? 493  GLN A CG  1 1 
ATOM   3749 C  CD  . GLN A 1 457 ? 5.795   9.495   35.74  1    19.433  ? 493  GLN A CD  1 1 
ATOM   3750 O  OE1 . GLN A 1 457 ? 4.75    9.739   35.109 1    21.176  ? 493  GLN A OE1 1 1 
ATOM   3751 N  NE2 . GLN A 1 457 ? 6.925   10.18   35.585 1    17.182  ? 493  GLN A NE2 1 1 
ATOM   3752 N  N   . GLY A 1 458 ? 3.759   8.898   41.198 1    17.251  ? 494  GLY A N   1 1 
ATOM   3753 C  CA  . GLY A 1 458 ? 3.599   9.783   42.352 1    17.689  ? 494  GLY A CA  1 1 
ATOM   3754 C  C   . GLY A 1 458 ? 3.474   11.248  41.909 1    20.722  ? 494  GLY A C   1 1 
ATOM   3755 O  O   . GLY A 1 458 ? 3.942   12.182  42.616 1    20.206  ? 494  GLY A O   1 1 
ATOM   3756 N  N   . LEU A 1 459 ? 2.84    11.488  40.741 1    17.087  ? 495  LEU A N   1 1 
ATOM   3757 C  CA  . LEU A 1 459 ? 2.734   12.882  40.311 1    19.873  ? 495  LEU A CA  1 1 
ATOM   3758 C  C   . LEU A 1 459 ? 1.278   13.32   40.315 1    18.876  ? 495  LEU A C   1 1 
ATOM   3759 O  O   . LEU A 1 459 ? 0.389   12.493  40.189 1    24.909  ? 495  LEU A O   1 1 
ATOM   3760 C  CB  . LEU A 1 459 ? 3.307   13.08   38.913 1    20.01   ? 495  LEU A CB  1 1 
ATOM   3761 C  CG  . LEU A 1 459 ? 4.759   12.668  38.693 1    23.233  ? 495  LEU A CG  1 1 
ATOM   3762 C  CD1 . LEU A 1 459 ? 5.085   12.765  37.171 1    21.334  ? 495  LEU A CD1 1 1 
ATOM   3763 C  CD2 . LEU A 1 459 ? 5.625   13.562  39.537 1    24.064  ? 495  LEU A CD2 1 1 
ATOM   3764 N  N   . CYS A 1 460 ? 1.046   14.633  40.346 1    21.335  ? 496  CYS A N   1 1 
ATOM   3765 C  CA  . CYS A 1 460 ? -0.296  15.162  40.148 1    22.917  ? 496  CYS A CA  1 1 
ATOM   3766 C  C   . CYS A 1 460 ? -0.214  16.264  39.086 1    24.019  ? 496  CYS A C   1 1 
ATOM   3767 O  O   . CYS A 1 460 ? 0.802   16.987  38.938 1    22.919  ? 496  CYS A O   1 1 
ATOM   3768 C  CB  . CYS A 1 460 ? -0.947  15.644  41.471 1    21.232  ? 496  CYS A CB  1 1 
ATOM   3769 S  SG  . CYS A 1 460 ? 0.072   16.817  42.406 1    31.874  ? 496  CYS A SG  1 1 
ATOM   3770 N  N   . PRO A 1 461 ? -1.37   16.533  38.457 1    22.581  ? 497  PRO A N   1 1 
ATOM   3771 C  CA  . PRO A 1 461 ? -1.484  17.621  37.474 1    22.506  ? 497  PRO A CA  1 1 
ATOM   3772 C  C   . PRO A 1 461 ? -1.499  18.954  38.233 1    26.853  ? 497  PRO A C   1 1 
ATOM   3773 O  O   . PRO A 1 461 ? -2.276  19.066  39.189 1    26.758  ? 497  PRO A O   1 1 
ATOM   3774 C  CB  . PRO A 1 461 ? -2.872  17.307  36.811 1    20.323  ? 497  PRO A CB  1 1 
ATOM   3775 C  CG  . PRO A 1 461 ? -3.669  16.344  37.759 1    19.133  ? 497  PRO A CG  1 1 
ATOM   3776 C  CD  . PRO A 1 461 ? -2.64   15.796  38.689 1    21.4    ? 497  PRO A CD  1 1 
ATOM   3777 N  N   . PRO A 1 462 ? -0.672  19.97   37.866 1    22.726  ? 498  PRO A N   1 1 
ATOM   3778 C  CA  . PRO A 1 462 ? -0.706  21.261  38.556 1    23.741  ? 498  PRO A CA  1 1 
ATOM   3779 C  C   . PRO A 1 462 ? -2.055  21.94   38.355 1    26.284  ? 498  PRO A C   1 1 
ATOM   3780 O  O   . PRO A 1 462 ? -2.438  22.732  39.186 1    27.009  ? 498  PRO A O   1 1 
ATOM   3781 C  CB  . PRO A 1 462 ? 0.431   22.032  37.906 1    24.57   ? 498  PRO A CB  1 1 
ATOM   3782 C  CG  . PRO A 1 462 ? 0.58    21.416  36.547 1    21.539  ? 498  PRO A CG  1 1 
ATOM   3783 C  CD  . PRO A 1 462 ? 0.36    19.935  36.796 1    24.032  ? 498  PRO A CD  1 1 
ATOM   3784 N  N   . VAL A 1 463 ? -2.773  21.587  37.273 1    23.027  ? 499  VAL A N   1 1 
ATOM   3785 C  CA  . VAL A 1 463 ? -4.062  22.147  36.96  1    24.516  ? 499  VAL A CA  1 1 
ATOM   3786 C  C   . VAL A 1 463 ? -5.096  21.033  36.784 1    23.703  ? 499  VAL A C   1 1 
ATOM   3787 O  O   . VAL A 1 463 ? -4.776  19.974  36.236 1    25.384  ? 499  VAL A O   1 1 
ATOM   3788 C  CB  . VAL A 1 463 ? -3.852  23.048  35.717 1    29.715  ? 499  VAL A CB  1 1 
ATOM   3789 C  CG1 . VAL A 1 463 ? -5.125  23.197  34.903 1    37.681  ? 499  VAL A CG1 1 1 
ATOM   3790 C  CG2 . VAL A 1 463 ? -3.453  24.45   36.197 1    28.771  ? 499  VAL A CG2 1 1 
ATOM   3791 N  N   . PRO A 1 464 ? -6.326  21.185  37.329 1    24.918  ? 500  PRO A N   1 1 
ATOM   3792 C  CA  . PRO A 1 464 ? -7.376  20.184  37.16  1    24.967  ? 500  PRO A CA  1 1 
ATOM   3793 C  C   . PRO A 1 464 ? -7.561  19.968  35.658 1    25.948  ? 500  PRO A C   1 1 
ATOM   3794 O  O   . PRO A 1 464 ? -7.449  20.879  34.852 1    26.548  ? 500  PRO A O   1 1 
ATOM   3795 C  CB  . PRO A 1 464 ? -8.641  20.897  37.782 1    27.19   ? 500  PRO A CB  1 1 
ATOM   3796 C  CG  . PRO A 1 464 ? -8.084  21.884  38.788 1    30.81   ? 500  PRO A CG  1 1 
ATOM   3797 C  CD  . PRO A 1 464 ? -6.705  22.271  38.258 1    27.913  ? 500  PRO A CD  1 1 
ATOM   3798 N  N   . ARG A 1 465 ? -7.69   18.717  35.248 1    23.837  ? 501  ARG A N   1 1 
ATOM   3799 C  CA  . ARG A 1 465 ? -7.914  18.412  33.859 1    24.147  ? 501  ARG A CA  1 1 
ATOM   3800 C  C   . ARG A 1 465 ? -9.417  18.435  33.647 1    28.451  ? 501  ARG A C   1 1 
ATOM   3801 O  O   . ARG A 1 465 ? -10.219 18.272  34.573 1    30.726  ? 501  ARG A O   1 1 
ATOM   3802 C  CB  . ARG A 1 465 ? -7.41   16.983  33.713 1    21.178  ? 501  ARG A CB  1 1 
ATOM   3803 C  CG  . ARG A 1 465 ? -6.002  16.698  34.203 1    24.011  ? 501  ARG A CG  1 1 
ATOM   3804 C  CD  . ARG A 1 465 ? -4.881  17.793  34.037 1    25.675  ? 501  ARG A CD  1 1 
ATOM   3805 N  NE  . ARG A 1 465 ? -4.519  17.972  32.614 1    25.227  ? 501  ARG A NE  1 1 
ATOM   3806 C  CZ  . ARG A 1 465 ? -4.575  19.131  32.001 1    29.101  ? 501  ARG A CZ  1 1 
ATOM   3807 N  NH1 . ARG A 1 465 ? -4.872  20.264  32.682 1    30.609  ? 501  ARG A NH1 1 1 
ATOM   3808 N  NH2 . ARG A 1 465 ? -4.305  19.145  30.705 1    26.169  ? 501  ARG A NH2 1 1 
ATOM   3809 N  N   . THR A 1 466 ? -9.835  18.651  32.417 1    31.502  ? 502  THR A N   1 1 
ATOM   3810 C  CA  . THR A 1 466 ? -11.26  18.757  32.206 1    32.797  ? 502  THR A CA  1 1 
ATOM   3811 C  C   . THR A 1 466 ? -11.596 17.865  31.009 1    34.694  ? 502  THR A C   1 1 
ATOM   3812 O  O   . THR A 1 466 ? -10.721 17.412  30.27  1    32.691  ? 502  THR A O   1 1 
ATOM   3813 C  CB  . THR A 1 466 ? -11.692 20.234  32.128 1    34.999  ? 502  THR A CB  1 1 
ATOM   3814 O  OG1 . THR A 1 466 ? -10.87  21.015  31.263 1    34.64   ? 502  THR A OG1 1 1 
ATOM   3815 C  CG2 . THR A 1 466 ? -11.499 21.008  33.429 1    35.504  ? 502  THR A CG2 1 1 
ATOM   3816 N  N   . GLN A 1 467 ? -12.875 17.582  30.803 1    34.496  ? 503  GLN A N   1 1 
ATOM   3817 C  CA  . GLN A 1 467 ? -13.236 16.802  29.628 1    39.631  ? 503  GLN A CA  1 1 
ATOM   3818 C  C   . GLN A 1 467 ? -12.721 17.515  28.37  1    34.459  ? 503  GLN A C   1 1 
ATOM   3819 O  O   . GLN A 1 467 ? -12.834 18.739  28.245 1    32.8    ? 503  GLN A O   1 1 
ATOM   3820 C  CB  . GLN A 1 467 ? -14.773 16.724  29.594 1    47.702  ? 503  GLN A CB  1 1 
ATOM   3821 C  CG  . GLN A 1 467 ? -15.375 15.874  28.474 1    56.788  ? 503  GLN A CG  1 1 
ATOM   3822 C  CD  . GLN A 1 467 ? -15.44  16.566  27.123 1    65.465  ? 503  GLN A CD  1 1 
ATOM   3823 O  OE1 . GLN A 1 467 ? -15.868 17.725  26.991 1    68.363  ? 503  GLN A OE1 1 1 
ATOM   3824 N  NE2 . GLN A 1 467 ? -14.96  15.869  26.1   1    72.515  ? 503  GLN A NE2 1 1 
ATOM   3825 N  N   . GLY A 1 468 ? -12.228 16.749  27.401 1    29.918  ? 504  GLY A N   1 1 
ATOM   3826 C  CA  . GLY A 1 468 ? -11.639 17.352  26.222 1    32.021  ? 504  GLY A CA  1 1 
ATOM   3827 C  C   . GLY A 1 468 ? -10.109 17.361  26.377 1    31.464  ? 504  GLY A C   1 1 
ATOM   3828 O  O   . GLY A 1 468 ? -9.387  17.411  25.392 1    34.619  ? 504  GLY A O   1 1 
ATOM   3829 N  N   . ASP A 1 469 ? -9.592  17.275  27.609 1    28.599  ? 505  ASP A N   1 1 
ATOM   3830 C  CA  . ASP A 1 469 ? -8.155  17.095  27.718 1    26.972  ? 505  ASP A CA  1 1 
ATOM   3831 C  C   . ASP A 1 469 ? -7.769  15.704  27.225 1    25.534  ? 505  ASP A C   1 1 
ATOM   3832 O  O   . ASP A 1 469 ? -8.529  14.771  27.36  1    26.069  ? 505  ASP A O   1 1 
ATOM   3833 C  CB  . ASP A 1 469 ? -7.688  17.375  29.13  1    28.7    ? 505  ASP A CB  1 1 
ATOM   3834 C  CG  . ASP A 1 469 ? -7.682  18.858  29.509 1    29.781  ? 505  ASP A CG  1 1 
ATOM   3835 O  OD1 . ASP A 1 469 ? -7.762  19.727  28.579 1    29.245  ? 505  ASP A OD1 1 1 
ATOM   3836 O  OD2 . ASP A 1 469 ? -7.646  19.132  30.753 1    28.846  ? 505  ASP A OD2 1 1 
ATOM   3837 N  N   . PHE A 1 470 ? -6.556  15.551  26.689 1    24.274  ? 506  PHE A N   1 1 
ATOM   3838 C  CA  . PHE A 1 470 ? -6.078  14.257  26.242 1    22.009  ? 506  PHE A CA  1 1 
ATOM   3839 C  C   . PHE A 1 470 ? -4.576  14.341  26.37  1    22.738  ? 506  PHE A C   1 1 
ATOM   3840 O  O   . PHE A 1 470 ? -3.851  14.462  25.359 1    18.87   ? 506  PHE A O   1 1 
ATOM   3841 C  CB  . PHE A 1 470 ? -6.472  13.97   24.779 1    22.576  ? 506  PHE A CB  1 1 
ATOM   3842 C  CG  . PHE A 1 470 ? -6.052  12.584  24.279 1    23.708  ? 506  PHE A CG  1 1 
ATOM   3843 C  CD1 . PHE A 1 470 ? -6.358  11.436  24.998 1    21.185  ? 506  PHE A CD1 1 1 
ATOM   3844 C  CD2 . PHE A 1 470 ? -5.32   12.432  23.089 1    24.18   ? 506  PHE A CD2 1 1 
ATOM   3845 C  CE1 . PHE A 1 470 ? -5.906  10.175  24.566 1    24.356  ? 506  PHE A CE1 1 1 
ATOM   3846 C  CE2 . PHE A 1 470 ? -4.826  11.197  22.705 1    25.835  ? 506  PHE A CE2 1 1 
ATOM   3847 C  CZ  . PHE A 1 470 ? -5.135  10.042  23.415 1    24.682  ? 506  PHE A CZ  1 1 
ATOM   3848 N  N   . ASP A 1 471 ? -4.152  14.345  27.63  1    20.01   ? 507  ASP A N   1 1 
ATOM   3849 C  CA  . ASP A 1 471 ? -2.755  14.52   27.968 1    21.443  ? 507  ASP A CA  1 1 
ATOM   3850 C  C   . ASP A 1 471 ? -1.845  13.501  27.28  1    22.023  ? 507  ASP A C   1 1 
ATOM   3851 O  O   . ASP A 1 471 ? -0.694  13.832  26.947 1    24.143  ? 507  ASP A O   1 1 
ATOM   3852 C  CB  . ASP A 1 471 ? -2.581  14.669  29.471 1    19.634  ? 507  ASP A CB  1 1 
ATOM   3853 C  CG  . ASP A 1 471 ? -3.331  15.871  30.015 1    21.305  ? 507  ASP A CG  1 1 
ATOM   3854 O  OD1 . ASP A 1 471 ? -3.482  16.921  29.309 1    24.723  ? 507  ASP A OD1 1 1 
ATOM   3855 O  OD2 . ASP A 1 471 ? -3.786  15.761  31.148 1    22.936  ? 507  ASP A OD2 1 1 
ATOM   3856 N  N   . PRO A 1 472 ? -2.243  12.21   27.11  1    20.428  ? 508  PRO A N   1 1 
ATOM   3857 C  CA  . PRO A 1 472 ? -1.373  11.266  26.435 1    22.697  ? 508  PRO A CA  1 1 
ATOM   3858 C  C   . PRO A 1 472 ? -0.967  11.777  25.056 1    21.872  ? 508  PRO A C   1 1 
ATOM   3859 O  O   . PRO A 1 472 ? 0.166   11.58   24.68  1    23.188  ? 508  PRO A O   1 1 
ATOM   3860 C  CB  . PRO A 1 472 ? -2.182  9.929   26.389 1    21.18   ? 508  PRO A CB  1 1 
ATOM   3861 C  CG  . PRO A 1 472 ? -3.125  10.039  27.599 1    20.684  ? 508  PRO A CG  1 1 
ATOM   3862 C  CD  . PRO A 1 472 ? -3.454  11.553  27.641 1    20.237  ? 508  PRO A CD  1 1 
ATOM   3863 N  N   . GLY A 1 473 ? -1.874  12.433  24.35  1    20.279  ? 509  GLY A N   1 1 
ATOM   3864 C  CA  . GLY A 1 473 ? -1.568  12.891  22.998 1    26.123  ? 509  GLY A CA  1 1 
ATOM   3865 C  C   . GLY A 1 473 ? -0.46   13.954  23.01  1    24.516  ? 509  GLY A C   1 1 
ATOM   3866 O  O   . GLY A 1 473 ? 0.064   14.329  21.952 1    23.509  ? 509  GLY A O   1 1 
ATOM   3867 N  N   . ALA A 1 474 ? -0.127  14.438  24.208 1    20.924  ? 510  ALA A N   1 1 
ATOM   3868 C  CA  . ALA A 1 474 ? 0.949   15.4    24.326 1    22.701  ? 510  ALA A CA  1 1 
ATOM   3869 C  C   . ALA A 1 474 ? 2.323   14.727  24.471 1    20.924  ? 510  ALA A C   1 1 
ATOM   3870 O  O   . ALA A 1 474 ? 3.328   15.388  24.648 1    23.808  ? 510  ALA A O   1 1 
ATOM   3871 C  CB  . ALA A 1 474 ? 0.662   16.385  25.444 1    24.543  ? 510  ALA A CB  1 1 
ATOM   3872 N  N   . LYS A 1 475 ? 2.407   13.403  24.383 1    19.436  ? 511  LYS A N   1 1 
ATOM   3873 C  CA  . LYS A 1 475 ? 3.713   12.762  24.356 1    20.634  ? 511  LYS A CA  1 1 
ATOM   3874 C  C   . LYS A 1 475 ? 3.932   12.163  22.946 1    22.75   ? 511  LYS A C   1 1 
ATOM   3875 O  O   . LYS A 1 475 ? 3.066   11.402  22.457 1    22.681  ? 511  LYS A O   1 1 
ATOM   3876 C  CB  . LYS A 1 475 ? 3.609   11.727  25.498 1    19.102  ? 511  LYS A CB  1 1 
ATOM   3877 C  CG  . LYS A 1 475 ? 4.713   10.656  25.634 1    17.65   ? 511  LYS A CG  1 1 
ATOM   3878 C  CD  . LYS A 1 475 ? 6.077   11.345  25.736 1    21.034  ? 511  LYS A CD  1 1 
ATOM   3879 C  CE  . LYS A 1 475 ? 7.293   10.483  25.567 1    20.439  ? 511  LYS A CE  1 1 
ATOM   3880 N  NZ  . LYS A 1 475 ? 8.582   11.193  25.575 1    23.125  ? 511  LYS A NZ  1 1 
ATOM   3881 N  N   . PHE A 1 476 ? 5.103   12.366  22.328 1    21.867  ? 512  PHE A N   1 1 
ATOM   3882 C  CA  . PHE A 1 476 ? 5.317   12.025  20.88  1    23.803  ? 512  PHE A CA  1 1 
ATOM   3883 C  C   . PHE A 1 476 ? 4.837   10.608  20.477 1    21.429  ? 512  PHE A C   1 1 
ATOM   3884 O  O   . PHE A 1 476 ? 4.127   10.41   19.468 1    20.404  ? 512  PHE A O   1 1 
ATOM   3885 C  CB  . PHE A 1 476 ? 6.827   12.176  20.542 1    22.924  ? 512  PHE A CB  1 1 
ATOM   3886 C  CG  . PHE A 1 476 ? 7.232   11.617  19.181 1    23.837  ? 512  PHE A CG  1 1 
ATOM   3887 C  CD1 . PHE A 1 476 ? 7.216   12.438  18.054 1    22.352  ? 512  PHE A CD1 1 1 
ATOM   3888 C  CD2 . PHE A 1 476 ? 7.64    10.276  19.04  1    24.125  ? 512  PHE A CD2 1 1 
ATOM   3889 C  CE1 . PHE A 1 476 ? 7.653   11.939  16.823 1    23.694  ? 512  PHE A CE1 1 1 
ATOM   3890 C  CE2 . PHE A 1 476 ? 8.033   9.76    17.778 1    21.424  ? 512  PHE A CE2 1 1 
ATOM   3891 C  CZ  . PHE A 1 476 ? 8.007   10.587  16.689 1    22.236  ? 512  PHE A CZ  1 1 
ATOM   3892 N  N   . HIS A 1 477 ? 5.239   9.598   21.273 1    19.54   ? 513  HIS A N   1 1 
ATOM   3893 C  CA  . HIS A 1 477 ? 5.029   8.181   20.96  1    22.795  ? 513  HIS A CA  1 1 
ATOM   3894 C  C   . HIS A 1 477 ? 3.544   7.784   20.832 1    23.633  ? 513  HIS A C   1 1 
ATOM   3895 O  O   . HIS A 1 477 ? 3.248   6.762   20.203 1    21.632  ? 513  HIS A O   1 1 
ATOM   3896 C  CB  . HIS A 1 477 ? 5.732   7.255   21.964 1    20.019  ? 513  HIS A CB  1 1 
ATOM   3897 C  CG  . HIS A 1 477 ? 7.193   7.55    22.007 1    21.558  ? 513  HIS A CG  1 1 
ATOM   3898 N  ND1 . HIS A 1 477 ? 7.655   8.763   22.485 1    25.397  ? 513  HIS A ND1 1 1 
ATOM   3899 C  CD2 . HIS A 1 477 ? 8.273   6.839   21.611 1    24.498  ? 513  HIS A CD2 1 1 
ATOM   3900 C  CE1 . HIS A 1 477 ? 8.994   8.778   22.407 1    29.029  ? 513  HIS A CE1 1 1 
ATOM   3901 N  NE2 . HIS A 1 477 ? 9.386   7.588   21.923 1    26.372  ? 513  HIS A NE2 1 1 
ATOM   3902 N  N   . ILE A 1 478 ? 2.643   8.518   21.493 1    20.669  ? 514  ILE A N   1 1 
ATOM   3903 C  CA  . ILE A 1 478 ? 1.201   8.24    21.407 1    18.893  ? 514  ILE A CA  1 1 
ATOM   3904 C  C   . ILE A 1 478 ? 0.67    8.59    20.015 1    21.439  ? 514  ILE A C   1 1 
ATOM   3905 O  O   . ILE A 1 478 ? 0.214   7.684   19.325 1    22.759  ? 514  ILE A O   1 1 
ATOM   3906 C  CB  . ILE A 1 478 ? 0.478   8.953   22.57  1    21.063  ? 514  ILE A CB  1 1 
ATOM   3907 C  CG1 . ILE A 1 478 ? 1.022   8.357   23.903 1    18.915  ? 514  ILE A CG1 1 1 
ATOM   3908 C  CG2 . ILE A 1 478 ? -1.073  8.914   22.465 1    18.089  ? 514  ILE A CG2 1 1 
ATOM   3909 C  CD1 . ILE A 1 478 ? 0.642   6.907   24.119 1    25.415  ? 514  ILE A CD1 1 1 
ATOM   3910 N  N   . PRO A 1 479 ? 0.728   9.842   19.495 1    23.491  ? 515  PRO A N   1 1 
ATOM   3911 C  CA  . PRO A 1 479 ? 0.229   10.086  18.142 1    25.063  ? 515  PRO A CA  1 1 
ATOM   3912 C  C   . PRO A 1 479 ? 1.069   9.361   17.08  1    25.481  ? 515  PRO A C   1 1 
ATOM   3913 O  O   . PRO A 1 479 ? 0.629   9.113   15.959 1    23.811  ? 515  PRO A O   1 1 
ATOM   3914 C  CB  . PRO A 1 479 ? 0.195   11.656  18.01  1    26.135  ? 515  PRO A CB  1 1 
ATOM   3915 C  CG  . PRO A 1 479 ? 1.113   12.211  19.079 1    23.875  ? 515  PRO A CG  1 1 
ATOM   3916 C  CD  . PRO A 1 479 ? 1.115   11.108  20.163 1    20.852  ? 515  PRO A CD  1 1 
ATOM   3917 N  N   . SER A 1 480 ? 2.32    9.056   17.414 1    22.706  ? 516  SER A N   1 1 
ATOM   3918 C  CA  . SER A 1 480 ? 3.19    8.391   16.45  1    25.534  ? 516  SER A CA  1 1 
ATOM   3919 C  C   . SER A 1 480 ? 3.007   6.871   16.498 1    22.337  ? 516  SER A C   1 1 
ATOM   3920 O  O   . SER A 1 480 ? 3.558   6.214   15.655 1    22.231  ? 516  SER A O   1 1 
ATOM   3921 C  CB  . SER A 1 480 ? 4.671   8.78    16.644 1    26.943  ? 516  SER A CB  1 1 
ATOM   3922 O  OG  . SER A 1 480 ? 4.886   10.033  16.009 1    31.057  ? 516  SER A OG  1 1 
ATOM   3923 N  N   . SER A 1 481 ? 2.312   6.322   17.508 1    20.872  ? 517  SER A N   1 1 
ATOM   3924 C  CA  . SER A 1 481 ? 2.011   4.905   17.506 1    24.345  ? 517  SER A CA  1 1 
ATOM   3925 C  C   . SER A 1 481 ? 3.339   4.138   17.559 1    22.868  ? 517  SER A C   1 1 
ATOM   3926 O  O   . SER A 1 481 ? 3.559   3.181   16.837 1    19.564  ? 517  SER A O   1 1 
ATOM   3927 C  CB  . SER A 1 481 ? 1.194   4.577   16.256 1    20.861  ? 517  SER A CB  1 1 
ATOM   3928 O  OG  . SER A 1 481 ? 0.654   3.285   16.423 1    21.105  ? 517  SER A OG  1 1 
ATOM   3929 N  N   . VAL A 1 482 ? 4.231   4.612   18.428 1    22.443  ? 518  VAL A N   1 1 
ATOM   3930 C  CA  . VAL A 1 482 ? 5.488   3.917   18.652 1    21.638  ? 518  VAL A CA  1 1 
ATOM   3931 C  C   . VAL A 1 482 ? 5.36    3.247   19.998 1    21.157  ? 518  VAL A C   1 1 
ATOM   3932 O  O   . VAL A 1 482 ? 5.119   3.952   20.969 1    22.207  ? 518  VAL A O   1 1 
ATOM   3933 C  CB  . VAL A 1 482 ? 6.766   4.77    18.555 1    25.075  ? 518  VAL A CB  1 1 
ATOM   3934 C  CG1 . VAL A 1 482 ? 8.005   3.955   18.95  1    24.654  ? 518  VAL A CG1 1 1 
ATOM   3935 C  CG2 . VAL A 1 482 ? 6.947   5.338   17.134 1    28.236  ? 518  VAL A CG2 1 1 
ATOM   3936 N  N   . PRO A 1 483 ? 5.479   1.89    20.076 1    18.135  ? 519  PRO A N   1 1 
ATOM   3937 C  CA  . PRO A 1 483 ? 5.37    1.173   21.357 1    19.831  ? 519  PRO A CA  1 1 
ATOM   3938 C  C   . PRO A 1 483 ? 6.392   1.7     22.369 1    20.765  ? 519  PRO A C   1 1 
ATOM   3939 O  O   . PRO A 1 483 ? 7.501   2.117   21.991 1    19.813  ? 519  PRO A O   1 1 
ATOM   3940 C  CB  . PRO A 1 483 ? 5.613   -0.334  20.951 1    16.561  ? 519  PRO A CB  1 1 
ATOM   3941 C  CG  . PRO A 1 483 ? 5.218   -0.339  19.416 1    19.283  ? 519  PRO A CG  1 1 
ATOM   3942 C  CD  . PRO A 1 483 ? 5.696   1.014   18.903 1    18.969  ? 519  PRO A CD  1 1 
ATOM   3943 N  N   . TYR A 1 484 ? 6.042   1.641   23.646 1    18.756  ? 520  TYR A N   1 1 
ATOM   3944 C  CA  . TYR A 1 484 ? 6.891   2.299   24.627 1    19.307  ? 520  TYR A CA  1 1 
ATOM   3945 C  C   . TYR A 1 484 ? 7.508   1.325   25.63  1    20.392  ? 520  TYR A C   1 1 
ATOM   3946 O  O   . TYR A 1 484 ? 8.475   1.725   26.304 1    20.189  ? 520  TYR A O   1 1 
ATOM   3947 C  CB  . TYR A 1 484 ? 6.129   3.282   25.554 1    19.983  ? 520  TYR A CB  1 1 
ATOM   3948 C  CG  . TYR A 1 484 ? 6.983   4.485   25.963 1    19.401  ? 520  TYR A CG  1 1 
ATOM   3949 C  CD1 . TYR A 1 484 ? 7.253   5.496   25.04  1    17.249  ? 520  TYR A CD1 1 1 
ATOM   3950 C  CD2 . TYR A 1 484 ? 7.594   4.549   27.239 1    17.331  ? 520  TYR A CD2 1 1 
ATOM   3951 C  CE1 . TYR A 1 484 ? 8.145   6.514   25.354 1    18.59   ? 520  TYR A CE1 1 1 
ATOM   3952 C  CE2 . TYR A 1 484 ? 8.424   5.616   27.582 1    15.88   ? 520  TYR A CE2 1 1 
ATOM   3953 C  CZ  . TYR A 1 484 ? 8.652   6.599   26.645 1    18.729  ? 520  TYR A CZ  1 1 
ATOM   3954 O  OH  . TYR A 1 484 ? 9.447   7.644   26.997 1    20.345  ? 520  TYR A OH  1 1 
ATOM   3955 N  N   . ILE A 1 485 ? 6.958   0.104   25.807 1    20.322  ? 521  ILE A N   1 1 
ATOM   3956 C  CA  . ILE A 1 485 ? 7.53    -0.755  26.869 1    21.955  ? 521  ILE A CA  1 1 
ATOM   3957 C  C   . ILE A 1 485 ? 9.013   -1.104  26.561 1    17.861  ? 521  ILE A C   1 1 
ATOM   3958 O  O   . ILE A 1 485 ? 9.8     -1.448  27.438 1    16.777  ? 521  ILE A O   1 1 
ATOM   3959 C  CB  . ILE A 1 485 ? 6.619   -1.977  27.128 1    20.415  ? 521  ILE A CB  1 1 
ATOM   3960 C  CG1 . ILE A 1 485 ? 6.802   -2.643  28.489 1    24.993  ? 521  ILE A CG1 1 1 
ATOM   3961 C  CG2 . ILE A 1 485 ? 6.822   -3.016  25.998 1    26.48   ? 521  ILE A CG2 1 1 
ATOM   3962 C  CD1 . ILE A 1 485 ? 6.391   -1.85   29.721 1    20.096  ? 521  ILE A CD1 1 1 
ATOM   3963 N  N   . ARG A 1 486 ? 9.44    -1.011  25.29  1    19.817  ? 522  ARG A N   1 1 
ATOM   3964 C  CA  . ARG A 1 486 ? 10.845  -1.246  24.926 1    19.374  ? 522  ARG A CA  1 1 
ATOM   3965 C  C   . ARG A 1 486 ? 11.812  -0.404  25.79  1    23.32   ? 522  ARG A C   1 1 
ATOM   3966 O  O   . ARG A 1 486 ? 12.963  -0.821  26.083 1    22.1    ? 522  ARG A O   1 1 
ATOM   3967 C  CB  . ARG A 1 486 ? 10.957  -0.946  23.416 1    19.732  ? 522  ARG A CB  1 1 
ATOM   3968 C  CG  . ARG A 1 486 ? 10.547  0.474   23.025 1    19.412  ? 522  ARG A CG  1 1 
ATOM   3969 C  CD  . ARG A 1 486 ? 10.434  0.807   21.542 1    20.09   ? 522  ARG A CD  1 1 
ATOM   3970 N  NE  . ARG A 1 486 ? 9.682   -0.293  20.933 1    18.352  ? 522  ARG A NE  1 1 
ATOM   3971 C  CZ  . ARG A 1 486 ? 9.404   -0.404  19.618 1    18.739  ? 522  ARG A CZ  1 1 
ATOM   3972 N  NH1 . ARG A 1 486 ? 9.896   0.447   18.766 1    17.37   ? 522  ARG A NH1 1 1 
ATOM   3973 N  NH2 . ARG A 1 486 ? 8.73    -1.442  19.19  1    19.103  ? 522  ARG A NH2 1 1 
ATOM   3974 N  N   . TYR A 1 487 ? 11.324  0.783   26.216 1    19.334  ? 523  TYR A N   1 1 
ATOM   3975 C  CA  . TYR A 1 487 ? 12.154  1.761   26.909 1    20.095  ? 523  TYR A CA  1 1 
ATOM   3976 C  C   . TYR A 1 487 ? 12.303  1.338   28.365 1    21.057  ? 523  TYR A C   1 1 
ATOM   3977 O  O   . TYR A 1 487 ? 13.375  1.496   28.934 1    23.006  ? 523  TYR A O   1 1 
ATOM   3978 C  CB  . TYR A 1 487 ? 11.671  3.219   26.812 1    19.251  ? 523  TYR A CB  1 1 
ATOM   3979 C  CG  . TYR A 1 487 ? 11.651  3.749   25.379 1    21.656  ? 523  TYR A CG  1 1 
ATOM   3980 C  CD1 . TYR A 1 487 ? 12.839  3.988   24.697 1    20.537  ? 523  TYR A CD1 1 1 
ATOM   3981 C  CD2 . TYR A 1 487 ? 10.442  3.938   24.696 1    19.848  ? 523  TYR A CD2 1 1 
ATOM   3982 C  CE1 . TYR A 1 487 ? 12.831  4.336   23.352 1    24.158  ? 523  TYR A CE1 1 1 
ATOM   3983 C  CE2 . TYR A 1 487 ? 10.427  4.362   23.38  1    19.822  ? 523  TYR A CE2 1 1 
ATOM   3984 C  CZ  . TYR A 1 487 ? 11.623  4.578   22.723 1    23.03   ? 523  TYR A CZ  1 1 
ATOM   3985 O  OH  . TYR A 1 487 ? 11.595  4.963   21.424 1    29.323  ? 523  TYR A OH  1 1 
ATOM   3986 N  N   . PHE A 1 488 ? 11.275  0.708   28.934 1    19.807  ? 524  PHE A N   1 1 
ATOM   3987 C  CA  . PHE A 1 488 ? 11.368  0.215   30.315 1    18.965  ? 524  PHE A CA  1 1 
ATOM   3988 C  C   . PHE A 1 488 ? 12.327  -0.991  30.357 1    22.638  ? 524  PHE A C   1 1 
ATOM   3989 O  O   . PHE A 1 488 ? 13.215  -1.093  31.213 1    19.229  ? 524  PHE A O   1 1 
ATOM   3990 C  CB  . PHE A 1 488 ? 9.951   -0.261  30.691 1    18.251  ? 524  PHE A CB  1 1 
ATOM   3991 C  CG  . PHE A 1 488 ? 9.954   -0.97   32.04  1    19.471  ? 524  PHE A CG  1 1 
ATOM   3992 C  CD1 . PHE A 1 488 ? 9.896   -0.227  33.22  1    19.161  ? 524  PHE A CD1 1 1 
ATOM   3993 C  CD2 . PHE A 1 488 ? 10.001  -2.367  32.124 1    18.263  ? 524  PHE A CD2 1 1 
ATOM   3994 C  CE1 . PHE A 1 488 ? 9.885   -0.848  34.447 1    17.672  ? 524  PHE A CE1 1 1 
ATOM   3995 C  CE2 . PHE A 1 488 ? 10.035  -2.978  33.374 1    21.076  ? 524  PHE A CE2 1 1 
ATOM   3996 C  CZ  . PHE A 1 488 ? 9.974   -2.238  34.523 1    17.202  ? 524  PHE A CZ  1 1 
ATOM   3997 N  N   . VAL A 1 489 ? 12.181  -1.878  29.365 1    19.721  ? 525  VAL A N   1 1 
ATOM   3998 C  CA  . VAL A 1 489 ? 13.022  -3.048  29.18  1    20.712  ? 525  VAL A CA  1 1 
ATOM   3999 C  C   . VAL A 1 489 ? 14.451  -2.569  28.981 1    22.199  ? 525  VAL A C   1 1 
ATOM   4000 O  O   . VAL A 1 489 ? 15.343  -3.045  29.702 1    22.76   ? 525  VAL A O   1 1 
ATOM   4001 C  CB  . VAL A 1 489 ? 12.597  -3.956  28.007 1    20.314  ? 525  VAL A CB  1 1 
ATOM   4002 C  CG1 . VAL A 1 489 ? 13.58   -5.144  27.836 1    19.421  ? 525  VAL A CG1 1 1 
ATOM   4003 C  CG2 . VAL A 1 489 ? 11.123  -4.438  28.165 1    20.765  ? 525  VAL A CG2 1 1 
ATOM   4004 N  N   . SER A 1 490 ? 14.653  -1.68   27.998 1    18.874  ? 526  SER A N   1 1 
ATOM   4005 C  CA  . SER A 1 490 ? 15.984  -1.114  27.749 1    19.99   ? 526  SER A CA  1 1 
ATOM   4006 C  C   . SER A 1 490 ? 16.685  -0.67   29.064 1    20.741  ? 526  SER A C   1 1 
ATOM   4007 O  O   . SER A 1 490 ? 17.87   -0.885  29.323 1    22.141  ? 526  SER A O   1 1 
ATOM   4008 C  CB  . SER A 1 490 ? 15.809  0.1     26.88  1    19.86   ? 526  SER A CB  1 1 
ATOM   4009 O  OG  . SER A 1 490 ? 17.107  0.62    26.671 1    27.562  ? 526  SER A OG  1 1 
ATOM   4010 N  N   . PHE A 1 491 ? 15.971  0.087   29.894 1    19.878  ? 527  PHE A N   1 1 
ATOM   4011 C  CA  . PHE A 1 491 ? 16.596  0.691   31.069 1    23.006  ? 527  PHE A CA  1 1 
ATOM   4012 C  C   . PHE A 1 491 ? 17.015  -0.372  32.095 1    22.79   ? 527  PHE A C   1 1 
ATOM   4013 O  O   . PHE A 1 491 ? 18.002  -0.183  32.804 1    27.377  ? 527  PHE A O   1 1 
ATOM   4014 C  CB  . PHE A 1 491 ? 15.76   1.842   31.67  1    24.376  ? 527  PHE A CB  1 1 
ATOM   4015 C  CG  . PHE A 1 491 ? 16.019  3.199   31.06  1    24.577  ? 527  PHE A CG  1 1 
ATOM   4016 C  CD1 . PHE A 1 491 ? 16.048  3.362   29.661 1    31.246  ? 527  PHE A CD1 1 1 
ATOM   4017 C  CD2 . PHE A 1 491 ? 16.228  4.314   31.884 1    28.015  ? 527  PHE A CD2 1 1 
ATOM   4018 C  CE1 . PHE A 1 491 ? 16.279  4.625   29.076 1    27.209  ? 527  PHE A CE1 1 1 
ATOM   4019 C  CE2 . PHE A 1 491 ? 16.439  5.555   31.302 1    26      ? 527  PHE A CE2 1 1 
ATOM   4020 C  CZ  . PHE A 1 491 ? 16.527  5.688   29.919 1    28.117  ? 527  PHE A CZ  1 1 
ATOM   4021 N  N   . ILE A 1 492 ? 16.227  -1.448  32.254 1    23.57   ? 528  ILE A N   1 1 
ATOM   4022 C  CA  . ILE A 1 492 ? 16.629  -2.601  33.088 1    22.096  ? 528  ILE A CA  1 1 
ATOM   4023 C  C   . ILE A 1 492 ? 17.871  -3.297  32.503 1    24.907  ? 528  ILE A C   1 1 
ATOM   4024 O  O   . ILE A 1 492 ? 18.937  -3.412  33.137 1    25.022  ? 528  ILE A O   1 1 
ATOM   4025 C  CB  . ILE A 1 492 ? 15.448  -3.565  33.3   1    23.274  ? 528  ILE A CB  1 1 
ATOM   4026 C  CG1 . ILE A 1 492 ? 14.19   -2.893  34.023 1    27.328  ? 528  ILE A CG1 1 1 
ATOM   4027 C  CG2 . ILE A 1 492 ? 15.886  -4.863  34.016 1    24.551  ? 528  ILE A CG2 1 1 
ATOM   4028 C  CD1 . ILE A 1 492 ? 14.329  -2.733  35.545 1    26.574  ? 528  ILE A CD1 1 1 
ATOM   4029 N  N   . ILE A 1 493 ? 17.737  -3.751  31.256 1    23.241  ? 529  ILE A N   1 1 
ATOM   4030 C  CA  . ILE A 1 493 ? 18.757  -4.629  30.708 1    23.66   ? 529  ILE A CA  1 1 
ATOM   4031 C  C   . ILE A 1 493 ? 20.021  -3.841  30.356 1    23.703  ? 529  ILE A C   1 1 
ATOM   4032 O  O   . ILE A 1 493 ? 21.08   -4.456  30.31  1    24.448  ? 529  ILE A O   1 1 
ATOM   4033 C  CB  . ILE A 1 493 ? 18.204  -5.383  29.499 1    23.465  ? 529  ILE A CB  1 1 
ATOM   4034 C  CG1 . ILE A 1 493 ? 18.036  -4.486  28.247 1    18.437  ? 529  ILE A CG1 1 1 
ATOM   4035 C  CG2 . ILE A 1 493 ? 16.944  -6.143  29.902 1    18.613  ? 529  ILE A CG2 1 1 
ATOM   4036 C  CD1 . ILE A 1 493 ? 17.701  -5.261  26.959 1    20.828  ? 529  ILE A CD1 1 1 
ATOM   4037 N  N   . GLN A 1 494 ? 19.942  -2.488  30.163 1    21.574  ? 530  GLN A N   1 1 
ATOM   4038 C  CA  . GLN A 1 494 ? 21.183  -1.747  29.922 1    23.113  ? 530  GLN A CA  1 1 
ATOM   4039 C  C   . GLN A 1 494 ? 22.194  -1.905  31.07  1    20.38   ? 530  GLN A C   1 1 
ATOM   4040 O  O   . GLN A 1 494 ? 23.383  -1.898  30.79  1    20.759  ? 530  GLN A O   1 1 
ATOM   4041 C  CB  . GLN A 1 494 ? 21.044  -0.266  29.485 1    23.708  ? 530  GLN A CB  1 1 
ATOM   4042 C  CG  . GLN A 1 494 ? 20.567  0.73    30.548 1    21.747  ? 530  GLN A CG  1 1 
ATOM   4043 C  CD  . GLN A 1 494 ? 20.152  2.052   29.91  1    24.444  ? 530  GLN A CD  1 1 
ATOM   4044 O  OE1 . GLN A 1 494 ? 20.701  3.104   30.258 1    28.418  ? 530  GLN A OE1 1 1 
ATOM   4045 N  NE2 . GLN A 1 494 ? 19.244  2.035   28.919 1    22.538  ? 530  GLN A NE2 1 1 
ATOM   4046 N  N   . PHE A 1 495 ? 21.731  -1.914  32.347 1    19.19   ? 531  PHE A N   1 1 
ATOM   4047 C  CA  . PHE A 1 495 ? 22.627  -2.033  33.483 1    19.874  ? 531  PHE A CA  1 1 
ATOM   4048 C  C   . PHE A 1 495 ? 23.156  -3.492  33.524 1    22.378  ? 531  PHE A C   1 1 
ATOM   4049 O  O   . PHE A 1 495 ? 24.347  -3.757  33.798 1    21.049  ? 531  PHE A O   1 1 
ATOM   4050 C  CB  . PHE A 1 495 ? 21.799  -1.636  34.721 1    19.011  ? 531  PHE A CB  1 1 
ATOM   4051 C  CG  . PHE A 1 495 ? 21.722  -0.119  34.814 1    22.923  ? 531  PHE A CG  1 1 
ATOM   4052 C  CD1 . PHE A 1 495 ? 22.798  0.624   35.304 1    24.472  ? 531  PHE A CD1 1 1 
ATOM   4053 C  CD2 . PHE A 1 495 ? 20.609  0.576   34.307 1    21.08   ? 531  PHE A CD2 1 1 
ATOM   4054 C  CE1 . PHE A 1 495 ? 22.746  2.022   35.319 1    23.739  ? 531  PHE A CE1 1 1 
ATOM   4055 C  CE2 . PHE A 1 495 ? 20.557  1.973   34.318 1    24.266  ? 531  PHE A CE2 1 1 
ATOM   4056 C  CZ  . PHE A 1 495 ? 21.638  2.706   34.84  1    24.427  ? 531  PHE A CZ  1 1 
ATOM   4057 N  N   . GLN A 1 496 ? 22.292  -4.457  33.166 1    20.429  ? 532  GLN A N   1 1 
ATOM   4058 C  CA  . GLN A 1 496 ? 22.806  -5.826  33.068 1    22.715  ? 532  GLN A CA  1 1 
ATOM   4059 C  C   . GLN A 1 496 ? 23.961  -5.954  32.054 1    23.578  ? 532  GLN A C   1 1 
ATOM   4060 O  O   . GLN A 1 496 ? 24.98   -6.64   32.324 1    27.287  ? 532  GLN A O   1 1 
ATOM   4061 C  CB  . GLN A 1 496 ? 21.745  -6.853  32.665 1    22.681  ? 532  GLN A CB  1 1 
ATOM   4062 C  CG  . GLN A 1 496 ? 20.603  -7.083  33.663 1    25.681  ? 532  GLN A CG  1 1 
ATOM   4063 C  CD  . GLN A 1 496 ? 19.554  -8.073  33.143 1    26.139  ? 532  GLN A CD  1 1 
ATOM   4064 O  OE1 . GLN A 1 496 ? 18.455  -7.715  32.697 1    24.35   ? 532  GLN A OE1 1 1 
ATOM   4065 N  NE2 . GLN A 1 496 ? 19.887  -9.347  33.19  1    25.02   ? 532  GLN A NE2 1 1 
ATOM   4066 N  N   . PHE A 1 497 ? 23.809  -5.319  30.882 1    22.251  ? 533  PHE A N   1 1 
ATOM   4067 C  CA  . PHE A 1 497 ? 24.828  -5.375  29.854 1    24.852  ? 533  PHE A CA  1 1 
ATOM   4068 C  C   . PHE A 1 497 ? 26.082  -4.617  30.298 1    25.163  ? 533  PHE A C   1 1 
ATOM   4069 O  O   . PHE A 1 497 ? 27.185  -5.083  30.107 1    28.597  ? 533  PHE A O   1 1 
ATOM   4070 C  CB  . PHE A 1 497 ? 24.332  -4.757  28.545 1    27.589  ? 533  PHE A CB  1 1 
ATOM   4071 C  CG  . PHE A 1 497 ? 23.17   -5.443  27.838 1    26.027  ? 533  PHE A CG  1 1 
ATOM   4072 C  CD1 . PHE A 1 497 ? 22.671  -6.667  28.278 1    25.111  ? 533  PHE A CD1 1 1 
ATOM   4073 C  CD2 . PHE A 1 497 ? 22.565  -4.827  26.728 1    25.87   ? 533  PHE A CD2 1 1 
ATOM   4074 C  CE1 . PHE A 1 497 ? 21.598  -7.288  27.636 1    25.942  ? 533  PHE A CE1 1 1 
ATOM   4075 C  CE2 . PHE A 1 497 ? 21.51   -5.444  26.051 1    24.287  ? 533  PHE A CE2 1 1 
ATOM   4076 C  CZ  . PHE A 1 497 ? 21.01   -6.664  26.518 1    26.586  ? 533  PHE A CZ  1 1 
ATOM   4077 N  N   . HIS A 1 498 ? 25.916  -3.434  30.873 1    25.853  ? 534  HIS A N   1 1 
ATOM   4078 C  CA  . HIS A 1 498 ? 27.018  -2.689  31.459 1    27.807  ? 534  HIS A CA  1 1 
ATOM   4079 C  C   . HIS A 1 498 ? 27.759  -3.527  32.505 1    26.677  ? 534  HIS A C   1 1 
ATOM   4080 O  O   . HIS A 1 498 ? 28.991  -3.6    32.459 1    28.53   ? 534  HIS A O   1 1 
ATOM   4081 C  CB  . HIS A 1 498 ? 26.46   -1.492  32.235 1    25.776  ? 534  HIS A CB  1 1 
ATOM   4082 C  CG  . HIS A 1 498 ? 27.474  -0.511  32.728 1    24.833  ? 534  HIS A CG  1 1 
ATOM   4083 N  ND1 . HIS A 1 498 ? 28.417  0.115   31.944 1    23.356  ? 534  HIS A ND1 1 1 
ATOM   4084 C  CD2 . HIS A 1 498 ? 27.71   -0.102  34.008 1    25.605  ? 534  HIS A CD2 1 1 
ATOM   4085 C  CE1 . HIS A 1 498 ? 29.126  0.927   32.702 1    24.668  ? 534  HIS A CE1 1 1 
ATOM   4086 N  NE2 . HIS A 1 498 ? 28.763  0.764   33.965 1    26.344  ? 534  HIS A NE2 1 1 
ATOM   4087 N  N   . GLU A 1 499 ? 27.04   -4.204  33.409 1    25.891  ? 535  GLU A N   1 1 
ATOM   4088 C  CA  . GLU A 1 499 ? 27.743  -5.082  34.377 1    26.972  ? 535  GLU A CA  1 1 
ATOM   4089 C  C   . GLU A 1 499 ? 28.503  -6.194  33.669 1    28.768  ? 535  GLU A C   1 1 
ATOM   4090 O  O   . GLU A 1 499 ? 29.64   -6.525  34.046 1    28.956  ? 535  GLU A O   1 1 
ATOM   4091 C  CB  . GLU A 1 499 ? 26.853  -5.471  35.56  1    26.42   ? 535  GLU A CB  1 1 
ATOM   4092 C  CG  . GLU A 1 499 ? 27.288  -6.655  36.428 1    32.036  ? 535  GLU A CG  1 1 
ATOM   4093 C  CD  . GLU A 1 499 ? 26.053  -7.28   37.097 1    34.399  ? 535  GLU A CD  1 1 
ATOM   4094 O  OE1 . GLU A 1 499 ? 25.195  -7.983  36.478 1    35.467  ? 535  GLU A OE1 1 1 
ATOM   4095 O  OE2 . GLU A 1 499 ? 25.837  -6.935  38.276 1    40.665  ? 535  GLU A OE2 1 1 
ATOM   4096 N  N   . ALA A 1 500 ? 27.893  -6.804  32.633 1    26.705  ? 536  ALA A N   1 1 
ATOM   4097 C  CA  . ALA A 1 500 ? 28.585  -7.924  31.995 1    26.693  ? 536  ALA A CA  1 1 
ATOM   4098 C  C   . ALA A 1 500 ? 29.804  -7.438  31.221 1    27.515  ? 536  ALA A C   1 1 
ATOM   4099 O  O   . ALA A 1 500 ? 30.831  -8.073  31.288 1    25.309  ? 536  ALA A O   1 1 
ATOM   4100 C  CB  . ALA A 1 500 ? 27.699  -8.694  31.073 1    30.174  ? 536  ALA A CB  1 1 
ATOM   4101 N  N   . LEU A 1 501 ? 29.691  -6.315  30.491 1    26.551  ? 537  LEU A N   1 1 
ATOM   4102 C  CA  . LEU A 1 501 ? 30.8    -5.823  29.692 1    27.43   ? 537  LEU A CA  1 1 
ATOM   4103 C  C   . LEU A 1 501 ? 31.954  -5.332  30.559 1    29.794  ? 537  LEU A C   1 1 
ATOM   4104 O  O   . LEU A 1 501 ? 33.108  -5.518  30.165 1    30.587  ? 537  LEU A O   1 1 
ATOM   4105 C  CB  . LEU A 1 501 ? 30.327  -4.724  28.754 1    31.613  ? 537  LEU A CB  1 1 
ATOM   4106 C  CG  . LEU A 1 501 ? 29.305  -5.149  27.697 1    33.653  ? 537  LEU A CG  1 1 
ATOM   4107 C  CD1 . LEU A 1 501 ? 29.275  -4.078  26.626 1    36.631  ? 537  LEU A CD1 1 1 
ATOM   4108 C  CD2 . LEU A 1 501 ? 29.669  -6.472  27.143 1    32.058  ? 537  LEU A CD2 1 1 
ATOM   4109 N  N   . CYS A 1 502 ? 31.622  -4.779  31.734 1    29.8    ? 538  CYS A N   1 1 
ATOM   4110 C  CA  . CYS A 1 502 ? 32.583  -4.28   32.729 1    31.611  ? 538  CYS A CA  1 1 
ATOM   4111 C  C   . CYS A 1 502 ? 33.392  -5.425  33.321 1    36.508  ? 538  CYS A C   1 1 
ATOM   4112 O  O   . CYS A 1 502 ? 34.634  -5.34   33.45  1    37.939  ? 538  CYS A O   1 1 
ATOM   4113 C  CB  . CYS A 1 502 ? 31.871  -3.505  33.836 1    29.719  ? 538  CYS A CB  1 1 
ATOM   4114 S  SG  . CYS A 1 502 ? 31.265  -1.897  33.2   1    32.773  ? 538  CYS A SG  1 1 
ATOM   4115 N  N   . GLN A 1 503 ? 32.687  -6.524  33.628 1    34.049  ? 539  GLN A N   1 1 
ATOM   4116 C  CA  . GLN A 1 503 ? 33.366  -7.768  33.966 1    36.461  ? 539  GLN A CA  1 1 
ATOM   4117 C  C   . GLN A 1 503 ? 34.182  -8.269  32.758 1    35.151  ? 539  GLN A C   1 1 
ATOM   4118 O  O   . GLN A 1 503 ? 35.361  -8.6    32.878 1    31.79   ? 539  GLN A O   1 1 
ATOM   4119 C  CB  . GLN A 1 503 ? 32.392  -8.783  34.564 1    38.741  ? 539  GLN A CB  1 1 
ATOM   4120 C  CG  . GLN A 1 503 ? 33.141  -10.006 35.07  1    45.822  ? 539  GLN A CG  1 1 
ATOM   4121 C  CD  . GLN A 1 503 ? 32.479  -11.248 34.543 1    58.522  ? 539  GLN A CD  1 1 
ATOM   4122 O  OE1 . GLN A 1 503 ? 32.776  -11.699 33.426 1    59.473  ? 539  GLN A OE1 1 1 
ATOM   4123 N  NE2 . GLN A 1 503 ? 31.48   -11.718 35.285 1    64.015  ? 539  GLN A NE2 1 1 
ATOM   4124 N  N   . ALA A 1 504 ? 33.581  -8.269  31.57  1    33.433  ? 540  ALA A N   1 1 
ATOM   4125 C  CA  . ALA A 1 504 ? 34.334  -8.692  30.407 1    35.43   ? 540  ALA A CA  1 1 
ATOM   4126 C  C   . ALA A 1 504 ? 35.67   -7.95   30.3   1    36.318  ? 540  ALA A C   1 1 
ATOM   4127 O  O   . ALA A 1 504 ? 36.636  -8.483  29.733 1    36.78   ? 540  ALA A O   1 1 
ATOM   4128 C  CB  . ALA A 1 504 ? 33.506  -8.514  29.151 1    38.109  ? 540  ALA A CB  1 1 
ATOM   4129 N  N   . ALA A 1 505 ? 35.699  -6.702  30.774 1    35.244  ? 541  ALA A N   1 1 
ATOM   4130 C  CA  . ALA A 1 505 ? 36.842  -5.837  30.539 1    35.768  ? 541  ALA A CA  1 1 
ATOM   4131 C  C   . ALA A 1 505 ? 37.836  -5.849  31.713 1    38.687  ? 541  ALA A C   1 1 
ATOM   4132 O  O   . ALA A 1 505 ? 38.796  -5.079  31.689 1    42.069  ? 541  ALA A O   1 1 
ATOM   4133 C  CB  . ALA A 1 505 ? 36.34   -4.449  30.238 1    31.412  ? 541  ALA A CB  1 1 
ATOM   4134 N  N   . GLY A 1 506 ? 37.629  -6.706  32.738 1    37.909  ? 542  GLY A N   1 1 
ATOM   4135 C  CA  . GLY A 1 506 ? 38.455  -6.723  33.947 1    37.85   ? 542  GLY A CA  1 1 
ATOM   4136 C  C   . GLY A 1 506 ? 38.179  -5.627  35.007 1    39.93   ? 542  GLY A C   1 1 
ATOM   4137 O  O   . GLY A 1 506 ? 38.953  -5.461  35.948 1    40.309  ? 542  GLY A O   1 1 
ATOM   4138 N  N   . HIS A 1 507 ? 37.068  -4.883  34.933 1    38.122  ? 543  HIS A N   1 1 
ATOM   4139 C  CA  . HIS A 1 507 ? 36.91   -3.76   35.839 1    37.648  ? 543  HIS A CA  1 1 
ATOM   4140 C  C   . HIS A 1 507 ? 36.693  -4.336  37.227 1    38.898  ? 543  HIS A C   1 1 
ATOM   4141 O  O   . HIS A 1 507 ? 35.989  -5.31   37.389 1    39.216  ? 543  HIS A O   1 1 
ATOM   4142 C  CB  . HIS A 1 507 ? 35.661  -2.951  35.458 1    37.749  ? 543  HIS A CB  1 1 
ATOM   4143 C  CG  . HIS A 1 507 ? 35.18   -1.996  36.539 1    44.398  ? 543  HIS A CG  1 1 
ATOM   4144 N  ND1 . HIS A 1 507 ? 35.887  -0.856  36.895 1    42.877  ? 543  HIS A ND1 1 1 
ATOM   4145 C  CD2 . HIS A 1 507 ? 34.074  -2.009  37.346 1    46.428  ? 543  HIS A CD2 1 1 
ATOM   4146 C  CE1 . HIS A 1 507 ? 35.277  -0.228  37.895 1    40.649  ? 543  HIS A CE1 1 1 
ATOM   4147 N  NE2 . HIS A 1 507 ? 34.161  -0.893  38.174 1    46.19   ? 543  HIS A NE2 1 1 
ATOM   4148 N  N   . THR A 1 508 ? 37.229  -3.721  38.271 1    42.723  ? 544  THR A N   1 1 
ATOM   4149 C  CA  . THR A 1 508 ? 36.845  -4.228  39.576 1    43.462  ? 544  THR A CA  1 1 
ATOM   4150 C  C   . THR A 1 508 ? 36.437  -3.048  40.446 1    43.823  ? 544  THR A C   1 1 
ATOM   4151 O  O   . THR A 1 508 ? 36.623  -1.886  40.057 1    41.13   ? 544  THR A O   1 1 
ATOM   4152 C  CB  . THR A 1 508 ? 38.003  -5.055  40.129 1    47.467  ? 544  THR A CB  1 1 
ATOM   4153 O  OG1 . THR A 1 508 ? 38.984  -4.128  40.57  1    49.853  ? 544  THR A OG1 1 1 
ATOM   4154 C  CG2 . THR A 1 508 ? 38.724  -5.835  39.048 1    45.66   ? 544  THR A CG2 1 1 
ATOM   4155 N  N   . GLY A 1 509 ? 35.815  -3.356  41.584 1    44.27   ? 545  GLY A N   1 1 
ATOM   4156 C  CA  . GLY A 1 509 ? 35.244  -2.306  42.416 1    39.818  ? 545  GLY A CA  1 1 
ATOM   4157 C  C   . GLY A 1 509 ? 33.845  -1.886  41.932 1    38.793  ? 545  GLY A C   1 1 
ATOM   4158 O  O   . GLY A 1 509 ? 33.257  -2.465  41.025 1    37.028  ? 545  GLY A O   1 1 
ATOM   4159 N  N   . PRO A 1 510 ? 33.312  -0.76   42.447 1    37.901  ? 546  PRO A N   1 1 
ATOM   4160 C  CA  . PRO A 1 510 ? 31.901  -0.438  42.227 1    33.714  ? 546  PRO A CA  1 1 
ATOM   4161 C  C   . PRO A 1 510 ? 31.616  -0.285  40.727 1    33.81   ? 546  PRO A C   1 1 
ATOM   4162 O  O   . PRO A 1 510 ? 32.365  0.368   39.977 1    30.94   ? 546  PRO A O   1 1 
ATOM   4163 C  CB  . PRO A 1 510 ? 31.77   0.887   42.976 1    31.295  ? 546  PRO A CB  1 1 
ATOM   4164 C  CG  . PRO A 1 510 ? 32.938  0.895   43.935 1    36.799  ? 546  PRO A CG  1 1 
ATOM   4165 C  CD  . PRO A 1 510 ? 34.089  0.269   43.189 1    35.809  ? 546  PRO A CD  1 1 
ATOM   4166 N  N   . LEU A 1 511 ? 30.485  -0.852  40.304 1    30.623  ? 547  LEU A N   1 1 
ATOM   4167 C  CA  . LEU A 1 511 ? 30.079  -0.845  38.907 1    31.134  ? 547  LEU A CA  1 1 
ATOM   4168 C  C   . LEU A 1 511 ? 29.981  0.564   38.297 1    32.626  ? 547  LEU A C   1 1 
ATOM   4169 O  O   . LEU A 1 511 ? 30.215  0.764   37.084 1    29.26   ? 547  LEU A O   1 1 
ATOM   4170 C  CB  . LEU A 1 511 ? 28.711  -1.526  38.876 1    31.914  ? 547  LEU A CB  1 1 
ATOM   4171 C  CG  . LEU A 1 511 ? 28.112  -1.674  37.477 1    30.333  ? 547  LEU A CG  1 1 
ATOM   4172 C  CD1 . LEU A 1 511 ? 29.149  -2.466  36.596 1    32.067  ? 547  LEU A CD1 1 1 
ATOM   4173 C  CD2 . LEU A 1 511 ? 26.887  -2.508  37.74  1    30.55   ? 547  LEU A CD2 1 1 
ATOM   4174 N  N   . HIS A 1 512 ? 29.592  1.562   39.117 1    32.699  ? 548  HIS A N   1 1 
ATOM   4175 C  CA  . HIS A 1 512 ? 29.323  2.891   38.562 1    28.266  ? 548  HIS A CA  1 1 
ATOM   4176 C  C   . HIS A 1 512 ? 30.608  3.62    38.202 1    27.167  ? 548  HIS A C   1 1 
ATOM   4177 O  O   . HIS A 1 512 ? 30.537  4.656   37.579 1    29.971  ? 548  HIS A O   1 1 
ATOM   4178 C  CB  . HIS A 1 512 ? 28.475  3.734   39.506 1    27.565  ? 548  HIS A CB  1 1 
ATOM   4179 C  CG  . HIS A 1 512 ? 29.25   4.222   40.709 1    33.656  ? 548  HIS A CG  1 1 
ATOM   4180 N  ND1 . HIS A 1 512 ? 29.352  3.554   41.922 1    31.511  ? 548  HIS A ND1 1 1 
ATOM   4181 C  CD2 . HIS A 1 512 ? 29.976  5.356   40.846 1    33.163  ? 548  HIS A CD2 1 1 
ATOM   4182 C  CE1 . HIS A 1 512 ? 30.13   4.249   42.751 1    33.883  ? 548  HIS A CE1 1 1 
ATOM   4183 N  NE2 . HIS A 1 512 ? 30.531  5.353   42.11  1    34.341  ? 548  HIS A NE2 1 1 
ATOM   4184 N  N   . LYS A 1 513 ? 31.77   3.111   38.599 1    26.759  ? 549  LYS A N   1 1 
ATOM   4185 C  CA  . LYS A 1 513 ? 33.063  3.684   38.238 1    28.788  ? 549  LYS A CA  1 1 
ATOM   4186 C  C   . LYS A 1 513 ? 33.59   3.068   36.944 1    29.887  ? 549  LYS A C   1 1 
ATOM   4187 O  O   . LYS A 1 513 ? 34.685  3.394   36.482 1    29.736  ? 549  LYS A O   1 1 
ATOM   4188 C  CB  . LYS A 1 513 ? 34.113  3.422   39.325 1    29.697  ? 549  LYS A CB  1 1 
ATOM   4189 C  CG  . LYS A 1 513 ? 33.771  4.191   40.555 1    34.676  ? 549  LYS A CG  1 1 
ATOM   4190 C  CD  . LYS A 1 513 ? 34.97   4.38    41.472 1    45.826  ? 549  LYS A CD  1 1 
ATOM   4191 C  CE  . LYS A 1 513 ? 34.846  5.556   42.384 1    49.302  ? 549  LYS A CE  1 1 
ATOM   4192 N  NZ  . LYS A 1 513 ? 34.794  6.776   41.584 1    53.691  ? 549  LYS A NZ  1 1 
ATOM   4193 N  N   . CYS A 1 514 ? 32.827  2.159   36.352 1    32.301  ? 550  CYS A N   1 1 
ATOM   4194 C  CA  . CYS A 1 514 ? 33.345  1.41    35.217 1    31.626  ? 550  CYS A CA  1 1 
ATOM   4195 C  C   . CYS A 1 514 ? 33.249  2.256   33.961 1    29.697  ? 550  CYS A C   1 1 
ATOM   4196 O  O   . CYS A 1 514 ? 32.242  2.908   33.723 1    27.551  ? 550  CYS A O   1 1 
ATOM   4197 C  CB  . CYS A 1 514 ? 32.559  0.129   34.988 1    30.746  ? 550  CYS A CB  1 1 
ATOM   4198 S  SG  . CYS A 1 514 ? 32.906  -0.664  33.386 1    35.107  ? 550  CYS A SG  1 1 
ATOM   4199 N  N   . ASP A 1 515 ? 34.298  2.155   33.144 1    31.459  ? 551  ASP A N   1 1 
ATOM   4200 C  CA  . ASP A 1 515 ? 34.272  2.749   31.823 1    30.656  ? 551  ASP A CA  1 1 
ATOM   4201 C  C   . ASP A 1 515 ? 34.858  1.745   30.855 1    30.15   ? 551  ASP A C   1 1 
ATOM   4202 O  O   . ASP A 1 515 ? 36.033  1.425   30.953 1    29.382  ? 551  ASP A O   1 1 
ATOM   4203 C  CB  . ASP A 1 515 ? 35.043  4.059   31.835 1    29.44   ? 551  ASP A CB  1 1 
ATOM   4204 C  CG  . ASP A 1 515 ? 35.286  4.688   30.476 1    32.119  ? 551  ASP A CG  1 1 
ATOM   4205 O  OD1 . ASP A 1 515 ? 34.786  4.169   29.453 1    34.898  ? 551  ASP A OD1 1 1 
ATOM   4206 O  OD2 . ASP A 1 515 ? 36.01   5.685   30.437 1    34.418  ? 551  ASP A OD2 1 1 
ATOM   4207 N  N   . ILE A 1 516 ? 34.054  1.293   29.896 1    28.816  ? 552  ILE A N   1 1 
ATOM   4208 C  CA  . ILE A 1 516 ? 34.506  0.207   29.044 1    29.445  ? 552  ILE A CA  1 1 
ATOM   4209 C  C   . ILE A 1 516 ? 35.243  0.732   27.806 1    32.014  ? 552  ILE A C   1 1 
ATOM   4210 O  O   . ILE A 1 516 ? 35.497  -0.034  26.87  1    31.634  ? 552  ILE A O   1 1 
ATOM   4211 C  CB  . ILE A 1 516 ? 33.316  -0.688  28.647 1    27.939  ? 552  ILE A CB  1 1 
ATOM   4212 C  CG1 . ILE A 1 516 ? 32.343  0.037   27.755 1    26.96   ? 552  ILE A CG1 1 1 
ATOM   4213 C  CG2 . ILE A 1 516 ? 32.668  -1.312  29.883 1    28.895  ? 552  ILE A CG2 1 1 
ATOM   4214 C  CD1 . ILE A 1 516 ? 31.313  -0.848  27.06  1    26.262  ? 552  ILE A CD1 1 1 
ATOM   4215 N  N   . TYR A 1 517 ? 35.597  2.034   27.775 1    31.041  ? 553  TYR A N   1 1 
ATOM   4216 C  CA  . TYR A 1 517 ? 36.168  2.582   26.547 1    32.03   ? 553  TYR A CA  1 1 
ATOM   4217 C  C   . TYR A 1 517 ? 37.377  1.756   26.114 1    31.306  ? 553  TYR A C   1 1 
ATOM   4218 O  O   . TYR A 1 517 ? 38.22   1.503   26.945 1    30.902  ? 553  TYR A O   1 1 
ATOM   4219 C  CB  . TYR A 1 517 ? 36.718  4.001   26.806 1    32.936  ? 553  TYR A CB  1 1 
ATOM   4220 C  CG  . TYR A 1 517 ? 37.302  4.61    25.537 1    33.748  ? 553  TYR A CG  1 1 
ATOM   4221 C  CD1 . TYR A 1 517 ? 36.463  5.097   24.532 1    32.312  ? 553  TYR A CD1 1 1 
ATOM   4222 C  CD2 . TYR A 1 517 ? 38.677  4.688   25.324 1    34.936  ? 553  TYR A CD2 1 1 
ATOM   4223 C  CE1 . TYR A 1 517 ? 36.972  5.671   23.371 1    32.067  ? 553  TYR A CE1 1 1 
ATOM   4224 C  CE2 . TYR A 1 517 ? 39.194  5.193   24.13  1    39.046  ? 553  TYR A CE2 1 1 
ATOM   4225 C  CZ  . TYR A 1 517 ? 38.334  5.708   23.161 1    36.655  ? 553  TYR A CZ  1 1 
ATOM   4226 O  OH  . TYR A 1 517 ? 38.806  6.283   22.017 1    37.4    ? 553  TYR A OH  1 1 
ATOM   4227 N  N   . GLN A 1 518 ? 37.432  1.319   24.846 1    29.908  ? 554  GLN A N   1 1 
ATOM   4228 C  CA  . GLN A 1 518 ? 38.549  0.607   24.239 1    33.285  ? 554  GLN A CA  1 1 
ATOM   4229 C  C   . GLN A 1 518 ? 38.558  -0.9    24.55  1    34.116  ? 554  GLN A C   1 1 
ATOM   4230 O  O   . GLN A 1 518 ? 39.486  -1.575  24.155 1    33.522  ? 554  GLN A O   1 1 
ATOM   4231 C  CB  . GLN A 1 518 ? 39.931  1.251   24.43  1    34.797  ? 554  GLN A CB  1 1 
ATOM   4232 C  CG  . GLN A 1 518 ? 40.96   0.796   23.395 1    37.819  ? 554  GLN A CG  1 1 
ATOM   4233 C  CD  . GLN A 1 518 ? 42.263  1.57    23.48  1    40.815  ? 554  GLN A CD  1 1 
ATOM   4234 O  OE1 . GLN A 1 518 ? 42.275  2.79    23.733 1    39.006  ? 554  GLN A OE1 1 1 
ATOM   4235 N  NE2 . GLN A 1 518 ? 43.384  0.861   23.31  1    37.619  ? 554  GLN A NE2 1 1 
ATOM   4236 N  N   . SER A 1 519 ? 37.552  -1.443  25.238 1    31.907  ? 555  SER A N   1 1 
ATOM   4237 C  CA  . SER A 1 519 ? 37.581  -2.846  25.616 1    32.575  ? 555  SER A CA  1 1 
ATOM   4238 C  C   . SER A 1 519 ? 37.09   -3.751  24.482 1    34.483  ? 555  SER A C   1 1 
ATOM   4239 O  O   . SER A 1 519 ? 35.904  -3.755  24.104 1    32.978  ? 555  SER A O   1 1 
ATOM   4240 C  CB  . SER A 1 519 ? 36.773  -3.078  26.849 1    32.184  ? 555  SER A CB  1 1 
ATOM   4241 O  OG  . SER A 1 519 ? 36.589  -4.486  27.011 1    33.444  ? 555  SER A OG  1 1 
ATOM   4242 N  N   . LYS A 1 520 ? 38.009  -4.573  23.964 1    35.122  ? 556  LYS A N   1 1 
ATOM   4243 C  CA  . LYS A 1 520 ? 37.693  -5.391  22.806 1    36.254  ? 556  LYS A CA  1 1 
ATOM   4244 C  C   . LYS A 1 520 ? 36.856  -6.59   23.261 1    35.775  ? 556  LYS A C   1 1 
ATOM   4245 O  O   . LYS A 1 520 ? 35.984  -7.071  22.53  1    34.352  ? 556  LYS A O   1 1 
ATOM   4246 C  CB  . LYS A 1 520 ? 38.972  -5.804  22.07  1    36.936  ? 556  LYS A CB  1 1 
ATOM   4247 C  CG  . LYS A 1 520 ? 39.747  -4.648  21.441 1    41.005  ? 556  LYS A CG  1 1 
ATOM   4248 C  CD  . LYS A 1 520 ? 39.077  -3.732  20.409 1    44.391  ? 556  LYS A CD  1 1 
ATOM   4249 C  CE  . LYS A 1 520 ? 40.034  -2.656  19.825 1    43.171  ? 556  LYS A CE  1 1 
ATOM   4250 N  NZ  . LYS A 1 520 ? 40.249  -1.589  20.817 1    41.1    ? 556  LYS A NZ  1 1 
ATOM   4251 N  N   . GLU A 1 521 ? 37.141  -7.076  24.473 1    34.537  ? 557  GLU A N   1 1 
ATOM   4252 C  CA  . GLU A 1 521 ? 36.332  -8.113  25.107 1    35.007  ? 557  GLU A CA  1 1 
ATOM   4253 C  C   . GLU A 1 521 ? 34.876  -7.627  25.229 1    33.771  ? 557  GLU A C   1 1 
ATOM   4254 O  O   . GLU A 1 521 ? 33.94   -8.326  24.859 1    32.371  ? 557  GLU A O   1 1 
ATOM   4255 C  CB  . GLU A 1 521 ? 36.979  -8.615  26.404 1    37.035  ? 557  GLU A CB  1 1 
ATOM   4256 C  CG  . GLU A 1 521 ? 38.433  -9.077  26.227 1    43.032  ? 557  GLU A CG  1 1 
ATOM   4257 C  CD  . GLU A 1 521 ? 39.524  -8.014  26.06  1    49.813  ? 557  GLU A CD  1 1 
ATOM   4258 O  OE1 . GLU A 1 521 ? 39.297  -6.773  26.234 1    50.19   ? 557  GLU A OE1 1 1 
ATOM   4259 O  OE2 . GLU A 1 521 ? 40.646  -8.455  25.711 1    53.614  ? 557  GLU A OE2 1 1 
ATOM   4260 N  N   . ALA A 1 522 ? 34.676  -6.412  25.741 1    33.322  ? 558  ALA A N   1 1 
ATOM   4261 C  CA  . ALA A 1 522 ? 33.344  -5.847  25.794 1    33.287  ? 558  ALA A CA  1 1 
ATOM   4262 C  C   . ALA A 1 522 ? 32.753  -5.718  24.38  1    35.465  ? 558  ALA A C   1 1 
ATOM   4263 O  O   . ALA A 1 522 ? 31.607  -6.113  24.161 1    35.356  ? 558  ALA A O   1 1 
ATOM   4264 C  CB  . ALA A 1 522 ? 33.381  -4.57   26.598 1    33.397  ? 558  ALA A CB  1 1 
ATOM   4265 N  N   . GLY A 1 523 ? 33.545  -5.324  23.364 1    34.004  ? 559  GLY A N   1 1 
ATOM   4266 C  CA  . GLY A 1 523 ? 32.924  -5.26   22.043 1    31.665  ? 559  GLY A CA  1 1 
ATOM   4267 C  C   . GLY A 1 523 ? 32.407  -6.647  21.59  1    33.61   ? 559  GLY A C   1 1 
ATOM   4268 O  O   . GLY A 1 523 ? 31.306  -6.811  21.063 1    29.82   ? 559  GLY A O   1 1 
ATOM   4269 N  N   . GLN A 1 524 ? 33.274  -7.648  21.716 1    34.83   ? 560  GLN A N   1 1 
ATOM   4270 C  CA  . GLN A 1 524 ? 32.965  -9.006  21.314 1    37.031  ? 560  GLN A CA  1 1 
ATOM   4271 C  C   . GLN A 1 524 ? 31.647  -9.522  21.921 1    35.813  ? 560  GLN A C   1 1 
ATOM   4272 O  O   . GLN A 1 524 ? 30.839  -10.121 21.229 1    35.985  ? 560  GLN A O   1 1 
ATOM   4273 C  CB  . GLN A 1 524 ? 34.212  -9.877  21.451 1    41.728  ? 560  GLN A CB  1 1 
ATOM   4274 C  CG  . GLN A 1 524 ? 34.134  -11.072 20.518 1    53.822  ? 560  GLN A CG  1 1 
ATOM   4275 C  CD  . GLN A 1 524 ? 33.914  -10.603 19.099 1    60.295  ? 560  GLN A CD  1 1 
ATOM   4276 O  OE1 . GLN A 1 524 ? 34.722  -9.831  18.571 1    64.429  ? 560  GLN A OE1 1 1 
ATOM   4277 N  NE2 . GLN A 1 524 ? 32.802  -11.008 18.495 1    62.013  ? 560  GLN A NE2 1 1 
ATOM   4278 N  N   . ARG A 1 525 ? 31.366  -9.253  23.197 1    36.576  ? 561  ARG A N   1 1 
ATOM   4279 C  CA  . ARG A 1 525 ? 30.084  -9.647  23.741 1    34.484  ? 561  ARG A CA  1 1 
ATOM   4280 C  C   . ARG A 1 525 ? 28.917  -9.052  22.969 1    37.667  ? 561  ARG A C   1 1 
ATOM   4281 O  O   . ARG A 1 525 ? 27.978  -9.781  22.618 1    36.177  ? 561  ARG A O   1 1 
ATOM   4282 C  CB  . ARG A 1 525 ? 30.034  -9.262  25.209 1    38.851  ? 561  ARG A CB  1 1 
ATOM   4283 C  CG  . ARG A 1 525 ? 31.029  -10.1   25.998 1    36.775  ? 561  ARG A CG  1 1 
ATOM   4284 C  CD  . ARG A 1 525 ? 30.406  -11.326 26.537 1    37.731  ? 561  ARG A CD  1 1 
ATOM   4285 N  NE  . ARG A 1 525 ? 31.435  -11.714 27.512 1    38.189  ? 561  ARG A NE  1 1 
ATOM   4286 C  CZ  . ARG A 1 525 ? 31.311  -11.705 28.817 1    39.033  ? 561  ARG A CZ  1 1 
ATOM   4287 N  NH1 . ARG A 1 525 ? 30.152  -11.395 29.386 1    39.857  ? 561  ARG A NH1 1 1 
ATOM   4288 N  NH2 . ARG A 1 525 ? 32.33   -12.077 29.557 1    38.06   ? 561  ARG A NH2 1 1 
ATOM   4289 N  N   . LEU A 1 526 ? 28.971  -7.744  22.675 1    35.325  ? 562  LEU A N   1 1 
ATOM   4290 C  CA  . LEU A 1 526 ? 27.81   -7.118  22.053 1    37.753  ? 562  LEU A CA  1 1 
ATOM   4291 C  C   . LEU A 1 526 ? 27.643  -7.599  20.596 1    33.505  ? 562  LEU A C   1 1 
ATOM   4292 O  O   . LEU A 1 526 ? 26.527  -7.797  20.118 1    30.938  ? 562  LEU A O   1 1 
ATOM   4293 C  CB  . LEU A 1 526 ? 27.864  -5.586  22.122 1    39.302  ? 562  LEU A CB  1 1 
ATOM   4294 C  CG  . LEU A 1 526 ? 27.675  -4.916  23.48  1    42.282  ? 562  LEU A CG  1 1 
ATOM   4295 C  CD1 . LEU A 1 526 ? 27.706  -3.4    23.214 1    44.146  ? 562  LEU A CD1 1 1 
ATOM   4296 C  CD2 . LEU A 1 526 ? 26.329  -5.364  24.049 1    40.983  ? 562  LEU A CD2 1 1 
ATOM   4297 N  N   . ALA A 1 527 ? 28.762  -7.763  19.899 1    30.804  ? 563  ALA A N   1 1 
ATOM   4298 C  CA  . ALA A 1 527 ? 28.763  -8.071  18.471 1    34.172  ? 563  ALA A CA  1 1 
ATOM   4299 C  C   . ALA A 1 527 ? 28.073  -9.401  18.209 1    34.352  ? 563  ALA A C   1 1 
ATOM   4300 O  O   . ALA A 1 527 ? 27.23   -9.5    17.319 1    33.916  ? 563  ALA A O   1 1 
ATOM   4301 C  CB  . ALA A 1 527 ? 30.172  -8.156  17.96  1    33.1    ? 563  ALA A CB  1 1 
ATOM   4302 N  N   . THR A 1 528 ? 28.472  -10.435 18.955 1    33.464  ? 564  THR A N   1 1 
ATOM   4303 C  CA  . THR A 1 528 ? 27.971  -11.76  18.63  1    35.799  ? 564  THR A CA  1 1 
ATOM   4304 C  C   . THR A 1 528 ? 26.457  -11.747 18.896 1    32.591  ? 564  THR A C   1 1 
ATOM   4305 O  O   . THR A 1 528 ? 25.7    -12.303 18.101 1    35.618  ? 564  THR A O   1 1 
ATOM   4306 C  CB  . THR A 1 528 ? 28.779  -12.86  19.355 1    38.345  ? 564  THR A CB  1 1 
ATOM   4307 O  OG1 . THR A 1 528 ? 28.686  -12.455 20.72  1    48.266  ? 564  THR A OG1 1 1 
ATOM   4308 C  CG2 . THR A 1 528 ? 30.285  -12.771 19.146 1    34.091  ? 564  THR A CG2 1 1 
ATOM   4309 N  N   . ALA A 1 529 ? 26      -11.03  19.952 1    28.089  ? 565  ALA A N   1 1 
ATOM   4310 C  CA  . ALA A 1 529 ? 24.572  -10.986 20.229 1    27.328  ? 565  ALA A CA  1 1 
ATOM   4311 C  C   . ALA A 1 529 ? 23.875  -10.213 19.102 1    27.284  ? 565  ALA A C   1 1 
ATOM   4312 O  O   . ALA A 1 529 ? 22.824  -10.632 18.592 1    25.276  ? 565  ALA A O   1 1 
ATOM   4313 C  CB  . ALA A 1 529 ? 24.264  -10.366 21.581 1    27.223  ? 565  ALA A CB  1 1 
ATOM   4314 N  N   . MET A 1 530 ? 24.454  -9.064  18.725 1    25.616  ? 566  MET A N   1 1 
ATOM   4315 C  CA  . MET A 1 530 ? 23.785  -8.189  17.777 1    26.248  ? 566  MET A CA  1 1 
ATOM   4316 C  C   . MET A 1 530 ? 23.708  -8.908  16.43  1    28.364  ? 566  MET A C   1 1 
ATOM   4317 O  O   . MET A 1 530 ? 22.698  -8.816  15.737 1    27.671  ? 566  MET A O   1 1 
ATOM   4318 C  CB  . MET A 1 530 ? 24.479  -6.837  17.641 1    24.81   ? 566  MET A CB  1 1 
ATOM   4319 C  CG  . MET A 1 530 ? 24.164  -5.917  18.802 1    25.492  ? 566  MET A CG  1 1 
ATOM   4320 S  SD  . MET A 1 530 ? 24.853  -4.3    18.473 1    30.156  ? 566  MET A SD  1 1 
ATOM   4321 C  CE  . MET A 1 530 ? 26.559  -4.689  18.857 1    28.734  ? 566  MET A CE  1 1 
ATOM   4322 N  N   . LYS A 1 531 ? 24.721  -9.715  16.14  1    29.62   ? 567  LYS A N   1 1 
ATOM   4323 C  CA  . LYS A 1 531 ? 24.737  -10.483 14.9   1    33.731  ? 567  LYS A CA  1 1 
ATOM   4324 C  C   . LYS A 1 531 ? 23.529  -11.394 14.765 1    31.994  ? 567  LYS A C   1 1 
ATOM   4325 O  O   . LYS A 1 531 ? 23.175  -11.719 13.64  1    29.156  ? 567  LYS A O   1 1 
ATOM   4326 C  CB  . LYS A 1 531 ? 25.973  -11.35  14.621 1    32.466  ? 567  LYS A CB  1 1 
ATOM   4327 C  CG  . LYS A 1 531 ? 27.127  -10.481 14.285 1    37.621  ? 567  LYS A CG  1 1 
ATOM   4328 C  CD  . LYS A 1 531 ? 28.283  -11.146 13.534 1    41.197  ? 567  LYS A CD  1 1 
ATOM   4329 C  CE  . LYS A 1 531 ? 29.204  -10.037 13.089 1    42.319  ? 567  LYS A CE  1 1 
ATOM   4330 N  NZ  . LYS A 1 531 ? 29.77   -9.22   14.183 1    41.176  ? 567  LYS A NZ  1 1 
ATOM   4331 N  N   . LEU A 1 532 ? 22.939  -11.83  15.881 1    29.949  ? 568  LEU A N   1 1 
ATOM   4332 C  CA  . LEU A 1 532 ? 21.832  -12.785 15.811 1    29.927  ? 568  LEU A CA  1 1 
ATOM   4333 C  C   . LEU A 1 532 ? 20.573  -12.15  15.232 1    30.821  ? 568  LEU A C   1 1 
ATOM   4334 O  O   . LEU A 1 532 ? 19.648  -12.871 14.879 1    26.602  ? 568  LEU A O   1 1 
ATOM   4335 C  CB  . LEU A 1 532 ? 21.504  -13.418 17.172 1    31.143  ? 568  LEU A CB  1 1 
ATOM   4336 C  CG  . LEU A 1 532 ? 22.551  -14.401 17.725 1    34.587  ? 568  LEU A CG  1 1 
ATOM   4337 C  CD1 . LEU A 1 532 ? 22.342  -14.591 19.268 1    35.599  ? 568  LEU A CD1 1 1 
ATOM   4338 C  CD2 . LEU A 1 532 ? 22.687  -15.738 17.004 1    34.213  ? 568  LEU A CD2 1 1 
ATOM   4339 N  N   . GLY A 1 533 ? 20.508  -10.81  15.192 1    27.227  ? 569  GLY A N   1 1 
ATOM   4340 C  CA  . GLY A 1 533 ? 19.267  -10.175 14.825 1    28.176  ? 569  GLY A CA  1 1 
ATOM   4341 C  C   . GLY A 1 533 ? 18.105  -10.79  15.618 1    28.35   ? 569  GLY A C   1 1 
ATOM   4342 O  O   . GLY A 1 533 ? 18.202  -10.981 16.822 1    26.138  ? 569  GLY A O   1 1 
ATOM   4343 N  N   . PHE A 1 534 ? 17.045  -11.153 14.902 1    27.408  ? 570  PHE A N   1 1 
ATOM   4344 C  CA  . PHE A 1 534 ? 15.851  -11.768 15.445 1    27.828  ? 570  PHE A CA  1 1 
ATOM   4345 C  C   . PHE A 1 534 ? 15.818  -13.262 15.096 1    30.637  ? 570  PHE A C   1 1 
ATOM   4346 O  O   . PHE A 1 534 ? 14.759  -13.887 15.172 1    30.859  ? 570  PHE A O   1 1 
ATOM   4347 C  CB  . PHE A 1 534 ? 14.672  -10.946 14.926 1    30.045  ? 570  PHE A CB  1 1 
ATOM   4348 C  CG  . PHE A 1 534 ? 13.352  -11.278 15.597 1    31.719  ? 570  PHE A CG  1 1 
ATOM   4349 C  CD1 . PHE A 1 534 ? 13.121  -10.962 16.927 1    35.089  ? 570  PHE A CD1 1 1 
ATOM   4350 C  CD2 . PHE A 1 534 ? 12.328  -11.901 14.904 1    43.023  ? 570  PHE A CD2 1 1 
ATOM   4351 C  CE1 . PHE A 1 534 ? 11.907  -11.254 17.559 1    34.139  ? 570  PHE A CE1 1 1 
ATOM   4352 C  CE2 . PHE A 1 534 ? 11.122  -12.215 15.552 1    44.517  ? 570  PHE A CE2 1 1 
ATOM   4353 C  CZ  . PHE A 1 534 ? 10.919  -11.874 16.87  1    35.226  ? 570  PHE A CZ  1 1 
ATOM   4354 N  N   . SER A 1 535 ? 16.989  -13.85  14.816 1    28.478  ? 571  SER A N   1 1 
ATOM   4355 C  CA  . SER A 1 535 ? 17.076  -15.256 14.4   1    34.538  ? 571  SER A CA  1 1 
ATOM   4356 C  C   . SER A 1 535 ? 16.856  -16.277 15.535 1    33.324  ? 571  SER A C   1 1 
ATOM   4357 O  O   . SER A 1 535 ? 16.542  -17.424 15.239 1    35.92   ? 571  SER A O   1 1 
ATOM   4358 C  CB  . SER A 1 535 ? 18.346  -15.541 13.599 1    31.395  ? 571  SER A CB  1 1 
ATOM   4359 O  OG  . SER A 1 535 ? 19.456  -15.329 14.448 1    30.666  ? 571  SER A OG  1 1 
ATOM   4360 N  N   . ARG A 1 536 ? 16.934  -15.881 16.817 1    29.523  ? 572  ARG A N   1 1 
ATOM   4361 C  CA  . ARG A 1 536 ? 16.782  -16.818 17.921 1    31.113  ? 572  ARG A CA  1 1 
ATOM   4362 C  C   . ARG A 1 536 ? 15.962  -16.188 19.045 1    29.256  ? 572  ARG A C   1 1 
ATOM   4363 O  O   . ARG A 1 536 ? 15.94   -14.991 19.157 1    30.285  ? 572  ARG A O   1 1 
ATOM   4364 C  CB  . ARG A 1 536 ? 18.154  -16.875 18.59  1    32.262  ? 572  ARG A CB  1 1 
ATOM   4365 C  CG  . ARG A 1 536 ? 19.292  -17.372 17.696 1    38.913  ? 572  ARG A CG  1 1 
ATOM   4366 C  CD  . ARG A 1 536 ? 19.007  -18.719 17.03  1    45.742  ? 572  ARG A CD  1 1 
ATOM   4367 N  NE  . ARG A 1 536 ? 18.143  -19.587 17.842 1    57.342  ? 572  ARG A NE  1 1 
ATOM   4368 C  CZ  . ARG A 1 536 ? 17.798  -20.873 17.661 1    65.411  ? 572  ARG A CZ  1 1 
ATOM   4369 N  NH1 . ARG A 1 536 ? 17.118  -21.526 18.602 1    53.511  ? 572  ARG A NH1 1 1 
ATOM   4370 N  NH2 . ARG A 1 536 ? 18.191  -21.513 16.568 1    66.153  ? 572  ARG A NH2 1 1 
ATOM   4371 N  N   . PRO A 1 537 ? 15.306  -16.91  19.974 1    29.797  ? 573  PRO A N   1 1 
ATOM   4372 C  CA  . PRO A 1 537 ? 14.607  -16.222 21.076 1    27.559  ? 573  PRO A CA  1 1 
ATOM   4373 C  C   . PRO A 1 537 ? 15.581  -15.331 21.868 1    26.227  ? 573  PRO A C   1 1 
ATOM   4374 O  O   . PRO A 1 537 ? 16.75   -15.665 21.997 1    23.463  ? 573  PRO A O   1 1 
ATOM   4375 C  CB  . PRO A 1 537 ? 14.085  -17.464 21.87  1    30.147  ? 573  PRO A CB  1 1 
ATOM   4376 C  CG  . PRO A 1 537 ? 13.902  -18.535 20.763 1    31.572  ? 573  PRO A CG  1 1 
ATOM   4377 C  CD  . PRO A 1 537 ? 15.248  -18.393 20.058 1    29.664  ? 573  PRO A CD  1 1 
ATOM   4378 N  N   . TRP A 1 538 ? 15.109  -14.182 22.376 1    23.704  ? 574  TRP A N   1 1 
ATOM   4379 C  CA  . TRP A 1 538 ? 16.019  -13.191 22.956 1    25.961  ? 574  TRP A CA  1 1 
ATOM   4380 C  C   . TRP A 1 538 ? 16.833  -13.741 24.125 1    26.723  ? 574  TRP A C   1 1 
ATOM   4381 O  O   . TRP A 1 538 ? 17.96   -13.273 24.347 1    29.183  ? 574  TRP A O   1 1 
ATOM   4382 C  CB  . TRP A 1 538 ? 15.301  -11.886 23.35  1    20.26   ? 574  TRP A CB  1 1 
ATOM   4383 C  CG  . TRP A 1 538 ? 14.281  -12.011 24.462 1    18.846  ? 574  TRP A CG  1 1 
ATOM   4384 C  CD1 . TRP A 1 538 ? 12.903  -12.053 24.351 1    19.176  ? 574  TRP A CD1 1 1 
ATOM   4385 C  CD2 . TRP A 1 538 ? 14.565  -12.031 25.883 1    16.791  ? 574  TRP A CD2 1 1 
ATOM   4386 N  NE1 . TRP A 1 538 ? 12.325  -12.065 25.609 1    19.234  ? 574  TRP A NE1 1 1 
ATOM   4387 C  CE2 . TRP A 1 538 ? 13.325  -12.085 26.557 1    17.576  ? 574  TRP A CE2 1 1 
ATOM   4388 C  CE3 . TRP A 1 538 ? 15.756  -12.002 26.637 1    18.528  ? 574  TRP A CE3 1 1 
ATOM   4389 C  CZ2 . TRP A 1 538 ? 13.237  -12.152 27.947 1    20.11   ? 574  TRP A CZ2 1 1 
ATOM   4390 C  CZ3 . TRP A 1 538 ? 15.673  -12.086 28.007 1    18.824  ? 574  TRP A CZ3 1 1 
ATOM   4391 C  CH2 . TRP A 1 538 ? 14.429  -12.184 28.647 1    20.767  ? 574  TRP A CH2 1 1 
ATOM   4392 N  N   . PRO A 1 539 ? 16.327  -14.691 24.952 1    27.681  ? 575  PRO A N   1 1 
ATOM   4393 C  CA  . PRO A 1 539 ? 17.122  -15.158 26.096 1    26.648  ? 575  PRO A CA  1 1 
ATOM   4394 C  C   . PRO A 1 539 ? 18.465  -15.631 25.561 1    29.214  ? 575  PRO A C   1 1 
ATOM   4395 O  O   . PRO A 1 539 ? 19.43   -15.653 26.304 1    29.022  ? 575  PRO A O   1 1 
ATOM   4396 C  CB  . PRO A 1 539 ? 16.227  -16.318 26.657 1    25.875  ? 575  PRO A CB  1 1 
ATOM   4397 C  CG  . PRO A 1 539 ? 14.832  -15.731 26.386 1    27.666  ? 575  PRO A CG  1 1 
ATOM   4398 C  CD  . PRO A 1 539 ? 14.996  -15.343 24.916 1    27.346  ? 575  PRO A CD  1 1 
ATOM   4399 N  N   . GLU A 1 540 ? 18.548  -16.025 24.272 1    28.7    ? 576  GLU A N   1 1 
ATOM   4400 C  CA  . GLU A 1 540 ? 19.845  -16.483 23.772 1    30.597  ? 576  GLU A CA  1 1 
ATOM   4401 C  C   . GLU A 1 540 ? 20.814  -15.3   23.605 1    28.809  ? 576  GLU A C   1 1 
ATOM   4402 O  O   . GLU A 1 540 ? 21.994  -15.392 23.948 1    29.485  ? 576  GLU A O   1 1 
ATOM   4403 C  CB  . GLU A 1 540 ? 19.77   -17.334 22.503 1    32.14   ? 576  GLU A CB  1 1 
ATOM   4404 C  CG  . GLU A 1 540 ? 19.03   -18.653 22.706 1    36.724  ? 576  GLU A CG  1 1 
ATOM   4405 C  CD  . GLU A 1 540 ? 18.913  -19.393 21.372 1    49.846  ? 576  GLU A CD  1 1 
ATOM   4406 O  OE1 . GLU A 1 540 ? 19.796  -19.167 20.491 1    51.061  ? 576  GLU A OE1 1 1 
ATOM   4407 O  OE2 . GLU A 1 540 ? 17.941  -20.177 21.179 1    54.769  ? 576  GLU A OE2 1 1 
ATOM   4408 N  N   . ALA A 1 541 ? 20.317  -14.193 23.055 1    26.293  ? 577  ALA A N   1 1 
ATOM   4409 C  CA  . ALA A 1 541 ? 21.151  -13.006 23.008 1    27.205  ? 577  ALA A CA  1 1 
ATOM   4410 C  C   . ALA A 1 541 ? 21.507  -12.581 24.446 1    25.725  ? 577  ALA A C   1 1 
ATOM   4411 O  O   . ALA A 1 541 ? 22.671  -12.308 24.761 1    25.543  ? 577  ALA A O   1 1 
ATOM   4412 C  CB  . ALA A 1 541 ? 20.463  -11.907 22.231 1    25.809  ? 577  ALA A CB  1 1 
ATOM   4413 N  N   . MET A 1 542 ? 20.519  -12.556 25.339 1    22.8    ? 578  MET A N   1 1 
ATOM   4414 C  CA  . MET A 1 542 ? 20.832  -12.263 26.727 1    23.889  ? 578  MET A CA  1 1 
ATOM   4415 C  C   . MET A 1 542 ? 21.954  -13.133 27.329 1    25.95   ? 578  MET A C   1 1 
ATOM   4416 O  O   . MET A 1 542 ? 22.817  -12.605 28.037 1    24.052  ? 578  MET A O   1 1 
ATOM   4417 C  CB  . MET A 1 542 ? 19.556  -12.293 27.552 1    22.793  ? 578  MET A CB  1 1 
ATOM   4418 C  CG  . MET A 1 542 ? 19.837  -12.11  29.01  1    23.28   ? 578  MET A CG  1 1 
ATOM   4419 S  SD  . MET A 1 542 ? 20.157  -10.418 29.519 1    26.29   ? 578  MET A SD  1 1 
ATOM   4420 C  CE  . MET A 1 542 ? 18.556  -9.579  29.439 1    25.405  ? 578  MET A CE  1 1 
ATOM   4421 N  N   A GLN A 1 543 ? 21.924  -14.447 27.046 0.47 26.544  ? 579  GLN A N   1 1 
ATOM   4422 N  N   B GLN A 1 543 ? 21.94   -14.459 27.04  0.53 26.87   ? 579  GLN A N   1 1 
ATOM   4423 C  CA  A GLN A 1 543 ? 22.923  -15.395 27.514 0.47 26.207  ? 579  GLN A CA  1 1 
ATOM   4424 C  CA  B GLN A 1 543 ? 22.913  -15.426 27.547 0.53 26.472  ? 579  GLN A CA  1 1 
ATOM   4425 C  C   A GLN A 1 543 ? 24.309  -15.085 26.968 0.47 27.09   ? 579  GLN A C   1 1 
ATOM   4426 C  C   B GLN A 1 543 ? 24.302  -15.155 26.959 0.53 27.174  ? 579  GLN A C   1 1 
ATOM   4427 O  O   A GLN A 1 543 ? 25.293  -15.157 27.698 0.47 26.849  ? 579  GLN A O   1 1 
ATOM   4428 O  O   B GLN A 1 543 ? 25.293  -15.256 27.674 0.53 26.622  ? 579  GLN A O   1 1 
ATOM   4429 C  CB  A GLN A 1 543 ? 22.572  -16.775 26.959 0.47 25.975  ? 579  GLN A CB  1 1 
ATOM   4430 C  CB  B GLN A 1 543 ? 22.424  -16.886 27.403 0.53 26.57   ? 579  GLN A CB  1 1 
ATOM   4431 C  CG  A GLN A 1 543 ? 23.706  -17.784 27.07  0.47 27.103  ? 579  GLN A CG  1 1 
ATOM   4432 C  CG  B GLN A 1 543 ? 22.645  -17.77  28.635 0.53 26.403  ? 579  GLN A CG  1 1 
ATOM   4433 C  CD  A GLN A 1 543 ? 24.187  -18.035 28.48  0.47 26.427  ? 579  GLN A CD  1 1 
ATOM   4434 C  CD  B GLN A 1 543 ? 22.105  -19.192 28.577 0.53 28.139  ? 579  GLN A CD  1 1 
ATOM   4435 O  OE1 A GLN A 1 543 ? 23.38   -18.159 29.397 0.47 24.858  ? 579  GLN A OE1 1 1 
ATOM   4436 O  OE1 B GLN A 1 543 ? 22.51   -20.016 27.759 0.53 31.238  ? 579  GLN A OE1 1 1 
ATOM   4437 N  NE2 A GLN A 1 543 ? 25.5    -18.126 28.653 0.47 27.891  ? 579  GLN A NE2 1 1 
ATOM   4438 N  NE2 B GLN A 1 543 ? 21.22   -19.555 29.487 0.53 27.106  ? 579  GLN A NE2 1 1 
ATOM   4439 N  N   . LEU A 1 544 ? 24.391  -14.806 25.665 1    27.721  ? 580  LEU A N   1 1 
ATOM   4440 C  CA  . LEU A 1 544 ? 25.668  -14.386 25.075 1    30.102  ? 580  LEU A CA  1 1 
ATOM   4441 C  C   . LEU A 1 544 ? 26.302  -13.177 25.788 1    29.47   ? 580  LEU A C   1 1 
ATOM   4442 O  O   . LEU A 1 544 ? 27.524  -13.123 26.009 1    28.992  ? 580  LEU A O   1 1 
ATOM   4443 C  CB  . LEU A 1 544 ? 25.485  -14.064 23.588 1    28.565  ? 580  LEU A CB  1 1 
ATOM   4444 C  CG  . LEU A 1 544 ? 25.344  -15.302 22.71  1    30.832  ? 580  LEU A CG  1 1 
ATOM   4445 C  CD1 . LEU A 1 544 ? 24.783  -14.946 21.354 1    29.249  ? 580  LEU A CD1 1 1 
ATOM   4446 C  CD2 . LEU A 1 544 ? 26.702  -16.022 22.57  1    33.667  ? 580  LEU A CD2 1 1 
ATOM   4447 N  N   . ILE A 1 545 ? 25.489  -12.159 26.065 1    25.816  ? 581  ILE A N   1 1 
ATOM   4448 C  CA  . ILE A 1 545 ? 26.055  -10.966 26.696 1    26.21   ? 581  ILE A CA  1 1 
ATOM   4449 C  C   . ILE A 1 545 ? 26.373  -11.226 28.183 1    29.601  ? 581  ILE A C   1 1 
ATOM   4450 O  O   . ILE A 1 545 ? 27.462  -10.85  28.621 1    31.068  ? 581  ILE A O   1 1 
ATOM   4451 C  CB  . ILE A 1 545 ? 25.152  -9.722  26.45  1    26.194  ? 581  ILE A CB  1 1 
ATOM   4452 C  CG1 . ILE A 1 545 ? 24.938  -9.422  24.925 1    23.762  ? 581  ILE A CG1 1 1 
ATOM   4453 C  CG2 . ILE A 1 545 ? 25.668  -8.475  27.18  1    21.299  ? 581  ILE A CG2 1 1 
ATOM   4454 C  CD1 . ILE A 1 545 ? 23.763  -8.489  24.7   1    22.057  ? 581  ILE A CD1 1 1 
ATOM   4455 N  N   . THR A 1 546 ? 25.423  -11.792 28.977 1    29.434  ? 582  THR A N   1 1 
ATOM   4456 C  CA  . THR A 1 546 ? 25.489  -11.688 30.432 1    30.441  ? 582  THR A CA  1 1 
ATOM   4457 C  C   . THR A 1 546 ? 25.867  -13.028 31.077 1    34.04   ? 582  THR A C   1 1 
ATOM   4458 O  O   . THR A 1 546 ? 25.988  -13.108 32.307 1    31.371  ? 582  THR A O   1 1 
ATOM   4459 C  CB  . THR A 1 546 ? 24.22   -11.118 31.081 1    27.05   ? 582  THR A CB  1 1 
ATOM   4460 O  OG1 . THR A 1 546 ? 23.307  -12.205 30.997 1    25.877  ? 582  THR A OG1 1 1 
ATOM   4461 C  CG2 . THR A 1 546 ? 23.684  -9.875  30.386 1    22.75   ? 582  THR A CG2 1 1 
ATOM   4462 N  N   . GLY A 1 547 ? 25.928  -14.101 30.278 1    31.801  ? 583  GLY A N   1 1 
ATOM   4463 C  CA  . GLY A 1 547 ? 26.193  -15.394 30.876 1    32.046  ? 583  GLY A CA  1 1 
ATOM   4464 C  C   . GLY A 1 547 ? 24.972  -16.055 31.51  1    32.681  ? 583  GLY A C   1 1 
ATOM   4465 O  O   . GLY A 1 547 ? 25.084  -17.2   31.947 1    35.077  ? 583  GLY A O   1 1 
ATOM   4466 N  N   . GLN A 1 548 ? 23.807  -15.381 31.518 1    30.928  ? 584  GLN A N   1 1 
ATOM   4467 C  CA  . GLN A 1 548 ? 22.572  -15.991 31.993 1    29.062  ? 584  GLN A CA  1 1 
ATOM   4468 C  C   . GLN A 1 548 ? 21.408  -15.472 31.141 1    28.533  ? 584  GLN A C   1 1 
ATOM   4469 O  O   . GLN A 1 548 ? 21.611  -14.607 30.3   1    27.437  ? 584  GLN A O   1 1 
ATOM   4470 C  CB  . GLN A 1 548 ? 22.453  -15.82  33.496 1    26.372  ? 584  GLN A CB  1 1 
ATOM   4471 C  CG  . GLN A 1 548 ? 22.222  -14.378 33.9   1    29.837  ? 584  GLN A CG  1 1 
ATOM   4472 C  CD  . GLN A 1 548 ? 20.848  -13.805 33.539 1    30.851  ? 584  GLN A CD  1 1 
ATOM   4473 O  OE1 . GLN A 1 548 ? 19.804  -14.326 33.989 1    30.859  ? 584  GLN A OE1 1 1 
ATOM   4474 N  NE2 . GLN A 1 548 ? 20.832  -12.675 32.813 1    25.303  ? 584  GLN A NE2 1 1 
ATOM   4475 N  N   . PRO A 1 549 ? 20.185  -16.059 31.178 1    28.638  ? 585  PRO A N   1 1 
ATOM   4476 C  CA  . PRO A 1 549 ? 19.157  -15.687 30.189 1    27.413  ? 585  PRO A CA  1 1 
ATOM   4477 C  C   . PRO A 1 549 ? 17.928  -14.883 30.618 1    25.155  ? 585  PRO A C   1 1 
ATOM   4478 O  O   . PRO A 1 549 ? 17.015  -14.702 29.837 1    23.431  ? 585  PRO A O   1 1 
ATOM   4479 C  CB  . PRO A 1 549 ? 18.791  -17.18  29.806 1    30.234  ? 585  PRO A CB  1 1 
ATOM   4480 C  CG  . PRO A 1 549 ? 18.615  -17.835 31.203 1    30.366  ? 585  PRO A CG  1 1 
ATOM   4481 C  CD  . PRO A 1 549 ? 19.796  -17.23  31.984 1    28.506  ? 585  PRO A CD  1 1 
ATOM   4482 N  N   . GLN A 1 550 ? 17.858  -14.47  31.888 1    26.123  ? 586  GLN A N   1 1 
ATOM   4483 C  CA  . GLN A 1 550 ? 16.757  -13.628 32.335 1    30.501  ? 586  GLN A CA  1 1 
ATOM   4484 C  C   . GLN A 1 550 ? 17.025  -12.113 32.323 1    27.115  ? 586  GLN A C   1 1 
ATOM   4485 O  O   . GLN A 1 550 ? 18.175  -11.635 32.389 1    27.148  ? 586  GLN A O   1 1 
ATOM   4486 C  CB  . GLN A 1 550 ? 16.837  -13.946 33.818 1    33.206  ? 586  GLN A CB  1 1 
ATOM   4487 C  CG  . GLN A 1 550 ? 16.701  -15.419 34.116 1    38.861  ? 586  GLN A CG  1 1 
ATOM   4488 C  CD  . GLN A 1 550 ? 15.316  -15.659 34.644 1    54.376  ? 586  GLN A CD  1 1 
ATOM   4489 O  OE1 . GLN A 1 550 ? 14.349  -15.611 33.87  1    66.536  ? 586  GLN A OE1 1 1 
ATOM   4490 N  NE2 . GLN A 1 550 ? 15.198  -15.828 35.96  1    47.536  ? 586  GLN A NE2 1 1 
ATOM   4491 N  N   . MET A 1 551 ? 15.924  -11.355 32.306 1    24.901  ? 587  MET A N   1 1 
ATOM   4492 C  CA  . MET A 1 551 ? 15.936  -9.959  32.682 1    26.794  ? 587  MET A CA  1 1 
ATOM   4493 C  C   . MET A 1 551 ? 16.047  -9.892  34.21  1    27.679  ? 587  MET A C   1 1 
ATOM   4494 O  O   . MET A 1 551 ? 15.434  -10.691 34.89  1    23.849  ? 587  MET A O   1 1 
ATOM   4495 C  CB  . MET A 1 551 ? 14.664  -9.237  32.214 1    27.467  ? 587  MET A CB  1 1 
ATOM   4496 C  CG  . MET A 1 551 ? 14.551  -8.984  30.69  1    27.667  ? 587  MET A CG  1 1 
ATOM   4497 S  SD  . MET A 1 551 ? 13.08   -8.047  30.2   1    28.281  ? 587  MET A SD  1 1 
ATOM   4498 C  CE  . MET A 1 551 ? 11.946  -9.395  30.548 1    27.312  ? 587  MET A CE  1 1 
ATOM   4499 N  N   . SER A 1 552 ? 16.807  -8.924  34.747 1    26.631  ? 588  SER A N   1 1 
ATOM   4500 C  CA  . SER A 1 552 ? 17.079  -8.826  36.18  1    27.035  ? 588  SER A CA  1 1 
ATOM   4501 C  C   . SER A 1 552 ? 17.406  -7.365  36.516 1    26.378  ? 588  SER A C   1 1 
ATOM   4502 O  O   . SER A 1 552 ? 18.147  -6.728  35.789 1    26.698  ? 588  SER A O   1 1 
ATOM   4503 C  CB  . SER A 1 552 ? 18.248  -9.772  36.566 1    27.04   ? 588  SER A CB  1 1 
ATOM   4504 O  OG  . SER A 1 552 ? 18.665  -9.58   37.913 1    29.342  ? 588  SER A OG  1 1 
ATOM   4505 N  N   . ALA A 1 553 ? 16.784  -6.808  37.56  1    24.124  ? 589  ALA A N   1 1 
ATOM   4506 C  CA  . ALA A 1 553 ? 17.126  -5.485  38.072 1    22.548  ? 589  ALA A CA  1 1 
ATOM   4507 C  C   . ALA A 1 553 ? 18.398  -5.51   38.947 1    23.253  ? 589  ALA A C   1 1 
ATOM   4508 O  O   . ALA A 1 553 ? 18.754  -4.472  39.436 1    25.429  ? 589  ALA A O   1 1 
ATOM   4509 C  CB  . ALA A 1 553 ? 15.988  -4.998  38.938 1    19.114  ? 589  ALA A CB  1 1 
ATOM   4510 N  N   . SER A 1 554 ? 19.013  -6.671  39.25  1    23.664  ? 590  SER A N   1 1 
ATOM   4511 C  CA  . SER A 1 554 ? 20.242  -6.778  40.047 1    26.547  ? 590  SER A CA  1 1 
ATOM   4512 C  C   . SER A 1 554 ? 21.28   -5.723  39.691 1    26.146  ? 590  SER A C   1 1 
ATOM   4513 O  O   . SER A 1 554 ? 21.811  -5.048  40.579 1    23.976  ? 590  SER A O   1 1 
ATOM   4514 C  CB  . SER A 1 554 ? 20.926  -8.108  39.851 1    28.995  ? 590  SER A CB  1 1 
ATOM   4515 O  OG  . SER A 1 554 ? 20.24   -8.899  40.765 1    36.539  ? 590  SER A OG  1 1 
ATOM   4516 N  N   . ALA A 1 555 ? 21.634  -5.684  38.4   1    23.077  ? 591  ALA A N   1 1 
ATOM   4517 C  CA  . ALA A 1 555 ? 22.695  -4.811  37.927 1    22.041  ? 591  ALA A CA  1 1 
ATOM   4518 C  C   . ALA A 1 555 ? 22.324  -3.344  38.183 1    22.443  ? 591  ALA A C   1 1 
ATOM   4519 O  O   . ALA A 1 555 ? 23.114  -2.595  38.805 1    21.536  ? 591  ALA A O   1 1 
ATOM   4520 C  CB  . ALA A 1 555 ? 22.979  -5.078  36.471 1    21.832  ? 591  ALA A CB  1 1 
ATOM   4521 N  N   . MET A 1 556 ? 21.077  -2.954  37.837 1    20.989  ? 592  MET A N   1 1 
ATOM   4522 C  CA  . MET A 1 556 ? 20.695  -1.569  38.126 1    22.353  ? 592  MET A CA  1 1 
ATOM   4523 C  C   . MET A 1 556 ? 20.793  -1.27   39.646 1    25.595  ? 592  MET A C   1 1 
ATOM   4524 O  O   . MET A 1 556 ? 21.255  -0.189  40.067 1    25.68   ? 592  MET A O   1 1 
ATOM   4525 C  CB  . MET A 1 556 ? 19.265  -1.237  37.629 1    20.894  ? 592  MET A CB  1 1 
ATOM   4526 C  CG  . MET A 1 556 ? 18.852  0.271   37.774 1    21.522  ? 592  MET A CG  1 1 
ATOM   4527 S  SD  . MET A 1 556 ? 17.369  0.513   36.773 1    27.129  ? 592  MET A SD  1 1 
ATOM   4528 C  CE  . MET A 1 556 ? 17.387  2.266   36.373 1    33.065  ? 592  MET A CE  1 1 
ATOM   4529 N  N   . LEU A 1 557 ? 20.319  -2.199  40.492 1    26.852  ? 593  LEU A N   1 1 
ATOM   4530 C  CA  . LEU A 1 557 ? 20.362  -1.981  41.937 1    28.564  ? 593  LEU A CA  1 1 
ATOM   4531 C  C   . LEU A 1 557 ? 21.802  -1.845  42.452 1    28.628  ? 593  LEU A C   1 1 
ATOM   4532 O  O   . LEU A 1 557 ? 22.1    -0.99   43.285 1    28.022  ? 593  LEU A O   1 1 
ATOM   4533 C  CB  . LEU A 1 557 ? 19.626  -3.116  42.653 1    31.729  ? 593  LEU A CB  1 1 
ATOM   4534 C  CG  . LEU A 1 557 ? 18.091  -3.159  42.577 1    33.51   ? 593  LEU A CG  1 1 
ATOM   4535 C  CD1 . LEU A 1 557 ? 17.503  -4.155  43.635 1    32.191  ? 593  LEU A CD1 1 1 
ATOM   4536 C  CD2 . LEU A 1 557 ? 17.495  -1.786  42.74  1    32.897  ? 593  LEU A CD2 1 1 
ATOM   4537 N  N   A SER A 1 558 ? 22.689  -2.68   41.915 0.64 25.784  ? 594  SER A N   1 1 
ATOM   4538 N  N   B SER A 1 558 ? 22.695  -2.726  41.983 0.36 26.064  ? 594  SER A N   1 1 
ATOM   4539 C  CA  A SER A 1 558 ? 24.084  -2.75   42.307 0.64 25.69   ? 594  SER A CA  1 1 
ATOM   4540 C  CA  B SER A 1 558 ? 24.095  -2.654  42.373 0.36 25.399  ? 594  SER A CA  1 1 
ATOM   4541 C  C   A SER A 1 558 ? 24.775  -1.44   41.915 0.64 25.207  ? 594  SER A C   1 1 
ATOM   4542 C  C   B SER A 1 558 ? 24.613  -1.275  41.999 0.36 24.716  ? 594  SER A C   1 1 
ATOM   4543 O  O   A SER A 1 558 ? 25.56   -0.887  42.69  0.64 25.231  ? 594  SER A O   1 1 
ATOM   4544 O  O   B SER A 1 558 ? 25.138  -0.547  42.848 0.36 24.83   ? 594  SER A O   1 1 
ATOM   4545 C  CB  A SER A 1 558 ? 24.693  -3.951  41.608 0.64 24.685  ? 594  SER A CB  1 1 
ATOM   4546 C  CB  B SER A 1 558 ? 24.939  -3.676  41.66  0.36 24.891  ? 594  SER A CB  1 1 
ATOM   4547 O  OG  A SER A 1 558 ? 26.101  -4.022  41.675 0.64 26.528  ? 594  SER A OG  1 1 
ATOM   4548 O  OG  B SER A 1 558 ? 24.428  -4.978  41.839 0.36 24.656  ? 594  SER A OG  1 1 
ATOM   4549 N  N   . TYR A 1 559 ? 24.469  -0.952  40.706 1    22.733  ? 595  TYR A N   1 1 
ATOM   4550 C  CA  . TYR A 1 559 ? 24.956  0.337   40.225 1    23.93   ? 595  TYR A CA  1 1 
ATOM   4551 C  C   . TYR A 1 559 ? 24.621  1.438   41.247 1    24.083  ? 595  TYR A C   1 1 
ATOM   4552 O  O   . TYR A 1 559 ? 25.509  2.224   41.629 1    25.273  ? 595  TYR A O   1 1 
ATOM   4553 C  CB  . TYR A 1 559 ? 24.417  0.583   38.82  1    20.422  ? 595  TYR A CB  1 1 
ATOM   4554 C  CG  . TYR A 1 559 ? 24.947  1.846   38.162 1    22.657  ? 595  TYR A CG  1 1 
ATOM   4555 C  CD1 . TYR A 1 559 ? 24.41   3.095   38.483 1    21.09   ? 595  TYR A CD1 1 1 
ATOM   4556 C  CD2 . TYR A 1 559 ? 25.943  1.806   37.206 1    24.031  ? 595  TYR A CD2 1 1 
ATOM   4557 C  CE1 . TYR A 1 559 ? 24.819  4.258   37.882 1    20.564  ? 595  TYR A CE1 1 1 
ATOM   4558 C  CE2 . TYR A 1 559 ? 26.378  2.979   36.584 1    23.904  ? 595  TYR A CE2 1 1 
ATOM   4559 C  CZ  . TYR A 1 559 ? 25.804  4.193   36.93  1    23.403  ? 595  TYR A CZ  1 1 
ATOM   4560 O  OH  . TYR A 1 559 ? 26.195  5.339   36.34  1    23.878  ? 595  TYR A OH  1 1 
ATOM   4561 N  N   . PHE A 1 560 ? 23.354  1.46    41.701 1    22.752  ? 596  PHE A N   1 1 
ATOM   4562 C  CA  . PHE A 1 560 ? 22.815  2.593   42.455 1    26.187  ? 596  PHE A CA  1 1 
ATOM   4563 C  C   . PHE A 1 560 ? 22.945  2.387   43.982 1    26.583  ? 596  PHE A C   1 1 
ATOM   4564 O  O   . PHE A 1 560 ? 22.63   3.268   44.79  1    25.608  ? 596  PHE A O   1 1 
ATOM   4565 C  CB  . PHE A 1 560 ? 21.383  2.966   42.016 1    22.039  ? 596  PHE A CB  1 1 
ATOM   4566 C  CG  . PHE A 1 560 ? 21.359  3.789   40.743 1    21.099  ? 596  PHE A CG  1 1 
ATOM   4567 C  CD1 . PHE A 1 560 ? 21.798  5.122   40.738 1    20.174  ? 596  PHE A CD1 1 1 
ATOM   4568 C  CD2 . PHE A 1 560 ? 20.835  3.242   39.564 1    22.735  ? 596  PHE A CD2 1 1 
ATOM   4569 C  CE1 . PHE A 1 560 ? 21.761  5.889   39.544 1    21.178  ? 596  PHE A CE1 1 1 
ATOM   4570 C  CE2 . PHE A 1 560 ? 20.831  3.965   38.363 1    22.938  ? 596  PHE A CE2 1 1 
ATOM   4571 C  CZ  . PHE A 1 560 ? 21.267  5.311   38.36  1    22.843  ? 596  PHE A CZ  1 1 
ATOM   4572 N  N   . LYS A 1 561 ? 23.467  1.235   44.393 1    27.123  ? 597  LYS A N   1 1 
ATOM   4573 C  CA  . LYS A 1 561 ? 23.485  0.876   45.808 1    27.449  ? 597  LYS A CA  1 1 
ATOM   4574 C  C   . LYS A 1 561 ? 24.098  1.962   46.712 1    27.941  ? 597  LYS A C   1 1 
ATOM   4575 O  O   . LYS A 1 561 ? 23.563  2.207   47.791 1    30.813  ? 597  LYS A O   1 1 
ATOM   4576 C  CB  . LYS A 1 561 ? 24.101  -0.519  45.969 1    27.752  ? 597  LYS A CB  1 1 
ATOM   4577 C  CG  . LYS A 1 561 ? 24.759  -0.696  47.321 1    31.357  ? 597  LYS A CG  1 1 
ATOM   4578 C  CD  . LYS A 1 561 ? 23.961  -1.413  48.385 1    35.174  ? 597  LYS A CD  1 1 
ATOM   4579 C  CE  . LYS A 1 561 ? 24.955  -1.955  49.451 1    38.873  ? 597  LYS A CE  1 1 
ATOM   4580 N  NZ  . LYS A 1 561 ? 24.124  -1.878  50.638 1    32.76   ? 597  LYS A NZ  1 1 
ATOM   4581 N  N   . PRO A 1 562 ? 25.246  2.621   46.408 1    27.444  ? 598  PRO A N   1 1 
ATOM   4582 C  CA  . PRO A 1 562 ? 25.723  3.671   47.301 1    28.462  ? 598  PRO A CA  1 1 
ATOM   4583 C  C   . PRO A 1 562 ? 24.723  4.813   47.385 1    26.812  ? 598  PRO A C   1 1 
ATOM   4584 O  O   . PRO A 1 562 ? 24.683  5.528   48.383 1    28.41   ? 598  PRO A O   1 1 
ATOM   4585 C  CB  . PRO A 1 562 ? 27.079  4.091   46.739 1    28.832  ? 598  PRO A CB  1 1 
ATOM   4586 C  CG  . PRO A 1 562 ? 27.504  2.878   45.883 1    31.469  ? 598  PRO A CG  1 1 
ATOM   4587 C  CD  . PRO A 1 562 ? 26.17   2.39    45.28  1    29.292  ? 598  PRO A CD  1 1 
ATOM   4588 N  N   . LEU A 1 563 ? 23.925  5.029   46.348 1    25.924  ? 599  LEU A N   1 1 
ATOM   4589 C  CA  . LEU A 1 563 ? 23.008  6.18    46.386 1    23.214  ? 599  LEU A CA  1 1 
ATOM   4590 C  C   . LEU A 1 563 ? 21.814  5.792   47.243 1    25.965  ? 599  LEU A C   1 1 
ATOM   4591 O  O   . LEU A 1 563 ? 21.322  6.607   48.036 1    25.903  ? 599  LEU A O   1 1 
ATOM   4592 C  CB  . LEU A 1 563 ? 22.541  6.615   44.992 1    24.016  ? 599  LEU A CB  1 1 
ATOM   4593 C  CG  . LEU A 1 563 ? 21.455  7.699   44.904 1    25.493  ? 599  LEU A CG  1 1 
ATOM   4594 C  CD1 . LEU A 1 563 ? 22.016  9.05    45.35  1    28.727  ? 599  LEU A CD1 1 1 
ATOM   4595 C  CD2 . LEU A 1 563 ? 21.111  7.79    43.437 1    26.623  ? 599  LEU A CD2 1 1 
ATOM   4596 N  N   . LEU A 1 564 ? 21.376  4.531   47.11  1    23.882  ? 600  LEU A N   1 1 
ATOM   4597 C  CA  . LEU A 1 564 ? 20.246  4.064   47.905 1    25.374  ? 600  LEU A CA  1 1 
ATOM   4598 C  C   . LEU A 1 564 ? 20.563  4.25    49.406 1    27.783  ? 600  LEU A C   1 1 
ATOM   4599 O  O   . LEU A 1 564 ? 19.684  4.675   50.176 1    25.511  ? 600  LEU A O   1 1 
ATOM   4600 C  CB  . LEU A 1 564 ? 19.938  2.582   47.588 1    27.919  ? 600  LEU A CB  1 1 
ATOM   4601 C  CG  . LEU A 1 564 ? 18.915  1.886   48.518 1    31.801  ? 600  LEU A CG  1 1 
ATOM   4602 C  CD1 . LEU A 1 564 ? 17.516  2.491   48.26  1    29.44   ? 600  LEU A CD1 1 1 
ATOM   4603 C  CD2 . LEU A 1 564 ? 18.806  0.356   48.497 1    29.3    ? 600  LEU A CD2 1 1 
ATOM   4604 N  N   . ASP A 1 565 ? 21.792  3.887   49.831 1    25.948  ? 601  ASP A N   1 1 
ATOM   4605 C  CA  . ASP A 1 565 ? 22.195  3.97    51.223 1    29.686  ? 601  ASP A CA  1 1 
ATOM   4606 C  C   . ASP A 1 565 ? 22.173  5.424   51.683 1    31.129  ? 601  ASP A C   1 1 
ATOM   4607 O  O   . ASP A 1 565 ? 21.69   5.74    52.783 1    27.173  ? 601  ASP A O   1 1 
ATOM   4608 C  CB  . ASP A 1 565 ? 23.61   3.416   51.407 1    30.643  ? 601  ASP A CB  1 1 
ATOM   4609 C  CG  . ASP A 1 565 ? 23.653  1.904   51.297 1    36.15   ? 601  ASP A CG  1 1 
ATOM   4610 O  OD1 . ASP A 1 565 ? 22.572  1.289   51.385 1    44.327  ? 601  ASP A OD1 1 1 
ATOM   4611 O  OD2 . ASP A 1 565 ? 24.724  1.35    51.026 1    39.847  ? 601  ASP A OD2 1 1 
ATOM   4612 N  N   . TRP A 1 566 ? 22.714  6.298   50.808 1    28.153  ? 602  TRP A N   1 1 
ATOM   4613 C  CA  . TRP A 1 566 ? 22.796  7.712   51.119 1    26.597  ? 602  TRP A CA  1 1 
ATOM   4614 C  C   . TRP A 1 566 ? 21.384  8.308   51.279 1    26.689  ? 602  TRP A C   1 1 
ATOM   4615 O  O   . TRP A 1 566 ? 21.106  9.017   52.278 1    26.602  ? 602  TRP A O   1 1 
ATOM   4616 C  CB  . TRP A 1 566 ? 23.638  8.47    50.083 1    25.227  ? 602  TRP A CB  1 1 
ATOM   4617 C  CG  . TRP A 1 566 ? 23.77   9.93    50.454 1    27.698  ? 602  TRP A CG  1 1 
ATOM   4618 C  CD1 . TRP A 1 566 ? 24.79   10.479  51.186 1    28.782  ? 602  TRP A CD1 1 1 
ATOM   4619 C  CD2 . TRP A 1 566 ? 22.855  11.002  50.152 1    27.731  ? 602  TRP A CD2 1 1 
ATOM   4620 N  NE1 . TRP A 1 566 ? 24.576  11.819  51.35  1    31.224  ? 602  TRP A NE1 1 1 
ATOM   4621 C  CE2 . TRP A 1 566 ? 23.378  12.174  50.765 1    30.792  ? 602  TRP A CE2 1 1 
ATOM   4622 C  CE3 . TRP A 1 566 ? 21.647  11.101  49.452 1    29.389  ? 602  TRP A CE3 1 1 
ATOM   4623 C  CZ2 . TRP A 1 566 ? 22.739  13.423  50.704 1    28.829  ? 602  TRP A CZ2 1 1 
ATOM   4624 C  CZ3 . TRP A 1 566 ? 21.02   12.346  49.357 1    31.011  ? 602  TRP A CZ3 1 1 
ATOM   4625 C  CH2 . TRP A 1 566 ? 21.561  13.486  49.97  1    34.133  ? 602  TRP A CH2 1 1 
ATOM   4626 N  N   . LEU A 1 567 ? 20.467  7.959   50.349 1    26.253  ? 603  LEU A N   1 1 
ATOM   4627 C  CA  . LEU A 1 567 ? 19.084  8.438   50.341 1    24.887  ? 603  LEU A CA  1 1 
ATOM   4628 C  C   . LEU A 1 567 ? 18.352  7.992   51.595 1    27.68   ? 603  LEU A C   1 1 
ATOM   4629 O  O   . LEU A 1 567 ? 17.558  8.741   52.172 1    28.904  ? 603  LEU A O   1 1 
ATOM   4630 C  CB  . LEU A 1 567 ? 18.322  7.934   49.131 1    22.574  ? 603  LEU A CB  1 1 
ATOM   4631 C  CG  . LEU A 1 567 ? 18.691  8.596   47.8   1    24.529  ? 603  LEU A CG  1 1 
ATOM   4632 C  CD1 . LEU A 1 567 ? 18.011  7.868   46.607 1    22.936  ? 603  LEU A CD1 1 1 
ATOM   4633 C  CD2 . LEU A 1 567 ? 18.235  10.085  47.937 1    25.16   ? 603  LEU A CD2 1 1 
ATOM   4634 N  N   . ARG A 1 568 ? 18.547  6.723   51.956 1    28.752  ? 604  ARG A N   1 1 
ATOM   4635 C  CA  . ARG A 1 568 ? 17.906  6.177   53.152 1    28.755  ? 604  ARG A CA  1 1 
ATOM   4636 C  C   . ARG A 1 568 ? 18.305  6.936   54.397 1    24.023  ? 604  ARG A C   1 1 
ATOM   4637 O  O   . ARG A 1 568 ? 17.435  7.384   55.118 1    27.645  ? 604  ARG A O   1 1 
ATOM   4638 C  CB  . ARG A 1 568 ? 18.127  4.67    53.358 1    29.292  ? 604  ARG A CB  1 1 
ATOM   4639 C  CG  . ARG A 1 568 ? 17.152  3.927   52.459 1    31.563  ? 604  ARG A CG  1 1 
ATOM   4640 C  CD  . ARG A 1 568 ? 17.51   2.433   52.667 1    42.876  ? 604  ARG A CD  1 1 
ATOM   4641 N  NE  . ARG A 1 568 ? 16.442  1.569   52.166 1    45.318  ? 604  ARG A NE  1 1 
ATOM   4642 C  CZ  . ARG A 1 568 ? 16.631  0.427   51.532 1    51.45   ? 604  ARG A CZ  1 1 
ATOM   4643 N  NH1 . ARG A 1 568 ? 17.859  -0.084  51.375 1    44.004  ? 604  ARG A NH1 1 1 
ATOM   4644 N  NH2 . ARG A 1 568 ? 15.544  -0.198  51.101 1    51.852  ? 604  ARG A NH2 1 1 
ATOM   4645 N  N   . THR A 1 569 ? 19.61   7.103   54.63  1    27.942  ? 605  THR A N   1 1 
ATOM   4646 C  CA  . THR A 1 569 ? 20.075  7.883   55.778 1    28.73   ? 605  THR A CA  1 1 
ATOM   4647 C  C   . THR A 1 569 ? 19.513  9.318   55.748 1    27.481  ? 605  THR A C   1 1 
ATOM   4648 O  O   . THR A 1 569 ? 19.042  9.826   56.762 1    25.975  ? 605  THR A O   1 1 
ATOM   4649 C  CB  . THR A 1 569 ? 21.59   7.942   55.752 1    29.501  ? 605  THR A CB  1 1 
ATOM   4650 O  OG1 . THR A 1 569 ? 21.952  6.566   55.733 1    30.296  ? 605  THR A OG1 1 1 
ATOM   4651 C  CG2 . THR A 1 569 ? 22.151  8.669   56.972 1    29.165  ? 605  THR A CG2 1 1 
ATOM   4652 N  N   . GLU A 1 570 ? 19.606  9.968   54.579 1    26.546  ? 606  GLU A N   1 1 
ATOM   4653 C  CA  . GLU A 1 570 ? 19.122  11.327  54.382 1    27.734  ? 606  GLU A CA  1 1 
ATOM   4654 C  C   . GLU A 1 570 ? 17.608  11.397  54.635 1    25.642  ? 606  GLU A C   1 1 
ATOM   4655 O  O   . GLU A 1 570 ? 17.18   12.215  55.413 1    25.584  ? 606  GLU A O   1 1 
ATOM   4656 C  CB  . GLU A 1 570 ? 19.469  11.798  52.965 1    30.245  ? 606  GLU A CB  1 1 
ATOM   4657 C  CG  . GLU A 1 570 ? 19.007  13.22   52.631 1    29.361  ? 606  GLU A CG  1 1 
ATOM   4658 C  CD  . GLU A 1 570 ? 19.645  14.396  53.335 1    34.418  ? 606  GLU A CD  1 1 
ATOM   4659 O  OE1 . GLU A 1 570 ? 20.611  14.218  54.103 1    30.759  ? 606  GLU A OE1 1 1 
ATOM   4660 O  OE2 . GLU A 1 570 ? 19.101  15.516  53.195 1    36.904  ? 606  GLU A OE2 1 1 
ATOM   4661 N  N   . ASN A 1 571 ? 16.788  10.54   54.022 1    25.228  ? 607  ASN A N   1 1 
ATOM   4662 C  CA  . ASN A 1 571 ? 15.34   10.677  54.155 1    23.851  ? 607  ASN A CA  1 1 
ATOM   4663 C  C   . ASN A 1 571 ? 14.912  10.358  55.595 1    26.674  ? 607  ASN A C   1 1 
ATOM   4664 O  O   . ASN A 1 571 ? 13.966  10.962  56.141 1    28.368  ? 607  ASN A O   1 1 
ATOM   4665 C  CB  . ASN A 1 571 ? 14.644  9.753   53.16  1    22.505  ? 607  ASN A CB  1 1 
ATOM   4666 C  CG  . ASN A 1 571 ? 14.667  10.252  51.722 1    21.919  ? 607  ASN A CG  1 1 
ATOM   4667 O  OD1 . ASN A 1 571 ? 14.834  11.463  51.489 1    23.911  ? 607  ASN A OD1 1 1 
ATOM   4668 N  ND2 . ASN A 1 571 ? 14.526  9.35    50.743 1    21.129  ? 607  ASN A ND2 1 1 
ATOM   4669 N  N   . GLU A 1 572 ? 15.635  9.416   56.215 1    28.401  ? 608  GLU A N   1 1 
ATOM   4670 C  CA  . GLU A 1 572 ? 15.362  9.024   57.597 1    33.164  ? 608  GLU A CA  1 1 
ATOM   4671 C  C   . GLU A 1 572 ? 15.666  10.173  58.584 1    30.893  ? 608  GLU A C   1 1 
ATOM   4672 O  O   . GLU A 1 572 ? 14.906  10.419  59.529 1    29.831  ? 608  GLU A O   1 1 
ATOM   4673 C  CB  . GLU A 1 572 ? 15.973  7.63    57.862 1    37.651  ? 608  GLU A CB  1 1 
ATOM   4674 C  CG  . GLU A 1 572 ? 15.881  7.239   59.338 1    50.345  ? 608  GLU A CG  1 1 
ATOM   4675 C  CD  . GLU A 1 572 ? 16.881  6.233   59.876 1    57.748  ? 608  GLU A CD  1 1 
ATOM   4676 O  OE1 . GLU A 1 572 ? 16.734  5.079   59.413 1    66.231  ? 608  GLU A OE1 1 1 
ATOM   4677 O  OE2 . GLU A 1 572 ? 17.782  6.569   60.707 1    47.477  ? 608  GLU A OE2 1 1 
ATOM   4678 N  N   . LEU A 1 573 ? 16.737  10.939  58.33  1    30.179  ? 609  LEU A N   1 1 
ATOM   4679 C  CA  . LEU A 1 573 ? 17.152  12.025  59.21  1    33.394  ? 609  LEU A CA  1 1 
ATOM   4680 C  C   . LEU A 1 573 ? 16.085  13.121  59.27  1    32.953  ? 609  LEU A C   1 1 
ATOM   4681 O  O   . LEU A 1 573 ? 15.855  13.732  60.315 1    30.931  ? 609  LEU A O   1 1 
ATOM   4682 C  CB  . LEU A 1 573 ? 18.334  12.449  58.351 1    36.234  ? 609  LEU A CB  1 1 
ATOM   4683 C  CG  . LEU A 1 573 ? 19.087  13.724  58.679 1    35.33   ? 609  LEU A CG  1 1 
ATOM   4684 C  CD1 . LEU A 1 573 ? 19.374  13.512  60.13  1    45.317  ? 609  LEU A CD1 1 1 
ATOM   4685 C  CD2 . LEU A 1 573 ? 20.374  13.455  57.95  1    35.075  ? 609  LEU A CD2 1 1 
ATOM   4686 N  N   . HIS A 1 574 ? 15.38   13.314  58.136 1    30.9    ? 610  HIS A N   1 1 
ATOM   4687 C  CA  . HIS A 1 574 ? 14.355  14.322  57.981 1    28.872  ? 610  HIS A CA  1 1 
ATOM   4688 C  C   . HIS A 1 574 ? 12.981  13.779  58.304 1    27.738  ? 610  HIS A C   1 1 
ATOM   4689 O  O   . HIS A 1 574 ? 12.034  14.525  58.26  1    31.836  ? 610  HIS A O   1 1 
ATOM   4690 C  CB  . HIS A 1 574 ? 14.31   14.834  56.528 1    30.086  ? 610  HIS A CB  1 1 
ATOM   4691 C  CG  . HIS A 1 574 ? 15.587  15.527  56.196 1    34.353  ? 610  HIS A CG  1 1 
ATOM   4692 N  ND1 . HIS A 1 574 ? 15.903  16.732  56.792 1    37.938  ? 610  HIS A ND1 1 1 
ATOM   4693 C  CD2 . HIS A 1 574 ? 16.659  15.207  55.429 1    33.962  ? 610  HIS A CD2 1 1 
ATOM   4694 C  CE1 . HIS A 1 574 ? 17.138  17.089  56.419 1    37.798  ? 610  HIS A CE1 1 1 
ATOM   4695 N  NE2 . HIS A 1 574 ? 17.601  16.2    55.571 1    34.449  ? 610  HIS A NE2 1 1 
ATOM   4696 N  N   . GLY A 1 575 ? 12.847  12.475  58.502 1    30.14   ? 611  GLY A N   1 1 
ATOM   4697 C  CA  . GLY A 1 575 ? 11.548  11.855  58.714 1    27.88   ? 611  GLY A CA  1 1 
ATOM   4698 C  C   . GLY A 1 575 ? 10.671  11.738  57.472 1    30.268  ? 611  GLY A C   1 1 
ATOM   4699 O  O   . GLY A 1 575 ? 9.439   11.726  57.58  1    28.417  ? 611  GLY A O   1 1 
ATOM   4700 N  N   . GLU A 1 576 ? 11.261  11.58   56.277 1    29.498  ? 612  GLU A N   1 1 
ATOM   4701 C  CA  . GLU A 1 576 ? 10.382  11.605  55.12  1    28.654  ? 612  GLU A CA  1 1 
ATOM   4702 C  C   . GLU A 1 576 ? 9.417   10.436  55.208 1    34.216  ? 612  GLU A C   1 1 
ATOM   4703 O  O   . GLU A 1 576 ? 9.827   9.376   55.654 1    37.084  ? 612  GLU A O   1 1 
ATOM   4704 C  CB  . GLU A 1 576 ? 11.134  11.396  53.807 1    27.76   ? 612  GLU A CB  1 1 
ATOM   4705 C  CG  . GLU A 1 576 ? 12.174  12.508  53.598 1    26.937  ? 612  GLU A CG  1 1 
ATOM   4706 C  CD  . GLU A 1 576 ? 11.646  13.935  53.593 1    27.845  ? 612  GLU A CD  1 1 
ATOM   4707 O  OE1 . GLU A 1 576 ? 10.39   14.142  53.563 1    26.245  ? 612  GLU A OE1 1 1 
ATOM   4708 O  OE2 . GLU A 1 576 ? 12.508  14.866  53.61  1    31.024  ? 612  GLU A OE2 1 1 
ATOM   4709 N  N   . LYS A 1 577 ? 8.157   10.607  54.787 1    29.514  ? 613  LYS A N   1 1 
ATOM   4710 C  CA  . LYS A 1 577 ? 7.294   9.452   54.63  1    30.768  ? 613  LYS A CA  1 1 
ATOM   4711 C  C   . LYS A 1 577 ? 7.313   9.062   53.168 1    30.981  ? 613  LYS A C   1 1 
ATOM   4712 O  O   . LYS A 1 577 ? 6.871   9.871   52.366 1    37.44   ? 613  LYS A O   1 1 
ATOM   4713 C  CB  . LYS A 1 577 ? 5.832   9.727   54.985 1    34.327  ? 613  LYS A CB  1 1 
ATOM   4714 C  CG  . LYS A 1 577 ? 5.539   9.641   56.514 1    52.538  ? 613  LYS A CG  1 1 
ATOM   4715 C  CD  . LYS A 1 577 ? 4.028   9.451   56.645 1    66.146  ? 613  LYS A CD  1 1 
ATOM   4716 C  CE  . LYS A 1 577 ? 3.562   8.547   55.504 1    76.131  ? 613  LYS A CE  1 1 
ATOM   4717 N  NZ  . LYS A 1 577 ? 2.502   9.106   54.647 1    74.326  ? 613  LYS A NZ  1 1 
ATOM   4718 N  N   . LEU A 1 578 ? 7.767   7.833   52.845 1    26.9    ? 614  LEU A N   1 1 
ATOM   4719 C  CA  . LEU A 1 578 ? 7.948   7.401   51.458 1    27.791  ? 614  LEU A CA  1 1 
ATOM   4720 C  C   . LEU A 1 578 ? 6.58    7.112   50.831 1    31.939  ? 614  LEU A C   1 1 
ATOM   4721 O  O   . LEU A 1 578 ? 5.719   6.519   51.471 1    35.659  ? 614  LEU A O   1 1 
ATOM   4722 C  CB  . LEU A 1 578 ? 8.797   6.138   51.391 1    25.455  ? 614  LEU A CB  1 1 
ATOM   4723 C  CG  . LEU A 1 578 ? 10.207  6.189   51.993 1    30.812  ? 614  LEU A CG  1 1 
ATOM   4724 C  CD1 . LEU A 1 578 ? 10.853  4.845   51.705 1    31.202  ? 614  LEU A CD1 1 1 
ATOM   4725 C  CD2 . LEU A 1 578 ? 11.086  7.337   51.502 1    28.888  ? 614  LEU A CD2 1 1 
ATOM   4726 N  N   . GLY A 1 579 ? 6.384   7.493   49.565 1    28.576  ? 615  GLY A N   1 1 
ATOM   4727 C  CA  . GLY A 1 579 ? 5.091   7.318   48.923 1    22.364  ? 615  GLY A CA  1 1 
ATOM   4728 C  C   . GLY A 1 579 ? 4.263   8.589   49.051 1    24.341  ? 615  GLY A C   1 1 
ATOM   4729 O  O   . GLY A 1 579 ? 4.735   9.613   49.528 1    22.396  ? 615  GLY A O   1 1 
ATOM   4730 N  N   . TRP A 1 580 ? 3       8.5     48.707 1    22.872  ? 616  TRP A N   1 1 
ATOM   4731 C  CA  . TRP A 1 580 ? 2.202   9.705   48.599 1    29.614  ? 616  TRP A CA  1 1 
ATOM   4732 C  C   . TRP A 1 580 ? 0.78    9.297   48.901 1    29.811  ? 616  TRP A C   1 1 
ATOM   4733 O  O   . TRP A 1 580 ? -0.017  9.341   48.016 1    39.812  ? 616  TRP A O   1 1 
ATOM   4734 C  CB  . TRP A 1 580 ? 2.254   10.228  47.158 1    25.801  ? 616  TRP A CB  1 1 
ATOM   4735 C  CG  . TRP A 1 580 ? 2.226   9.088   46.157 1    23.813  ? 616  TRP A CG  1 1 
ATOM   4736 C  CD1 . TRP A 1 580 ? 1.151   8.473   45.55  1    24.602  ? 616  TRP A CD1 1 1 
ATOM   4737 C  CD2 . TRP A 1 580 ? 3.408   8.477   45.603 1    21.393  ? 616  TRP A CD2 1 1 
ATOM   4738 N  NE1 . TRP A 1 580 ? 1.585   7.515   44.647 1    22.929  ? 616  TRP A NE1 1 1 
ATOM   4739 C  CE2 . TRP A 1 580 ? 2.969   7.512   44.653 1    19.808  ? 616  TRP A CE2 1 1 
ATOM   4740 C  CE3 . TRP A 1 580 ? 4.785   8.69    45.788 1    20.663  ? 616  TRP A CE3 1 1 
ATOM   4741 C  CZ2 . TRP A 1 580 ? 3.863   6.734   43.946 1    18.746  ? 616  TRP A CZ2 1 1 
ATOM   4742 C  CZ3 . TRP A 1 580 ? 5.667   7.92    45.04  1    22.265  ? 616  TRP A CZ3 1 1 
ATOM   4743 C  CH2 . TRP A 1 580 ? 5.212   6.981   44.119 1    19.993  ? 616  TRP A CH2 1 1 
ATOM   4744 N  N   . PRO A 1 581 ? 0.455   8.872   50.138 1    41.268  ? 617  PRO A N   1 1 
ATOM   4745 C  CA  . PRO A 1 581 ? -0.92   8.493   50.462 1    46.771  ? 617  PRO A CA  1 1 
ATOM   4746 C  C   . PRO A 1 581 ? -1.863  9.688   50.305 1    54.571  ? 617  PRO A C   1 1 
ATOM   4747 O  O   . PRO A 1 581 ? -3.05   9.503   50.118 1    52.533  ? 617  PRO A O   1 1 
ATOM   4748 C  CB  . PRO A 1 581 ? -0.755  8.053   51.932 1    46.049  ? 617  PRO A CB  1 1 
ATOM   4749 C  CG  . PRO A 1 581 ? 0.39    8.948   52.436 1    43.076  ? 617  PRO A CG  1 1 
ATOM   4750 C  CD  . PRO A 1 581 ? 1.392   8.792   51.297 1    38.207  ? 617  PRO A CD  1 1 
ATOM   4751 N  N   . GLN A 1 582 ? -1.339  10.919  50.347 1    54.888  ? 618  GLN A N   1 1 
ATOM   4752 C  CA  . GLN A 1 582 ? -2.189  12.091  50.174 1    63.169  ? 618  GLN A CA  1 1 
ATOM   4753 C  C   . GLN A 1 582 ? -2.571  12.246  48.686 1    50.579  ? 618  GLN A C   1 1 
ATOM   4754 O  O   . GLN A 1 582 ? -2.699  13.404  48.272 1    56.935  ? 618  GLN A O   1 1 
ATOM   4755 C  CB  . GLN A 1 582 ? -1.604  13.398  50.73  1    63.338  ? 618  GLN A CB  1 1 
ATOM   4756 C  CG  . GLN A 1 582 ? -1.498  13.49   52.249 1    57.493  ? 618  GLN A CG  1 1 
ATOM   4757 C  CD  . GLN A 1 582 ? -2.696  12.946  52.999 1    67.198  ? 618  GLN A CD  1 1 
ATOM   4758 O  OE1 . GLN A 1 582 ? -3.812  13.501  52.988 1    69.064  ? 618  GLN A OE1 1 1 
ATOM   4759 N  NE2 . GLN A 1 582 ? -2.443  11.841  53.687 1    63.534  ? 618  GLN A NE2 1 1 
HETATM 4760 C  C1  . NAG B 2 .   ? 17.853  -24.079 7.832  1    47.073  ? 1    NAG B C1  1 ? 
HETATM 4761 C  C2  . NAG B 2 .   ? 19.231  -24.692 8.024  1    49.223  ? 1    NAG B C2  1 ? 
HETATM 4762 C  C3  . NAG B 2 .   ? 20.258  -23.594 8.263  1    49.482  ? 1    NAG B C3  1 ? 
HETATM 4763 C  C4  . NAG B 2 .   ? 20.16   -22.469 7.243  1    48.559  ? 1    NAG B C4  1 ? 
HETATM 4764 C  C5  . NAG B 2 .   ? 18.735  -21.955 7.166  1    48.032  ? 1    NAG B C5  1 ? 
HETATM 4765 C  C6  . NAG B 2 .   ? 18.515  -20.861 6.127  1    44.544  ? 1    NAG B C6  1 ? 
HETATM 4766 C  C7  . NAG B 2 .   ? 19.491  -26.966 8.933  1    71.695  ? 1    NAG B C7  1 ? 
HETATM 4767 C  C8  . NAG B 2 .   ? 19.338  -27.847 10.139 1    53.889  ? 1    NAG B C8  1 ? 
HETATM 4768 N  N2  . NAG B 2 .   ? 19.332  -25.643 9.116  1    64.418  ? 1    NAG B N2  1 ? 
HETATM 4769 O  O3  . NAG B 2 .   ? 21.51   -24.237 8.096  1    55.901  ? 1    NAG B O3  1 ? 
HETATM 4770 O  O4  . NAG B 2 .   ? 20.983  -21.387 7.667  1    55.117  ? 1    NAG B O4  1 ? 
HETATM 4771 O  O5  . NAG B 2 .   ? 17.934  -23.092 6.809  1    53.812  ? 1    NAG B O5  1 ? 
HETATM 4772 O  O6  . NAG B 2 .   ? 19.227  -21.137 4.883  1    44.38   ? 1    NAG B O6  1 ? 
HETATM 4773 O  O7  . NAG B 2 .   ? 19.727  -27.439 7.824  1    63.588  ? 1    NAG B O7  1 ? 
HETATM 4774 C  C1  . NAG B 2 .   ? 22.075  -20.993 6.905  1    50.378  ? 2    NAG B C1  1 ? 
HETATM 4775 C  C2  . NAG B 2 .   ? 22.464  -19.639 7.458  1    56.611  ? 2    NAG B C2  1 ? 
HETATM 4776 C  C3  . NAG B 2 .   ? 23.76   -19.175 6.819  1    56.511  ? 2    NAG B C3  1 ? 
HETATM 4777 C  C4  . NAG B 2 .   ? 24.866  -20.2   7.005  1    57.649  ? 2    NAG B C4  1 ? 
HETATM 4778 C  C5  . NAG B 2 .   ? 24.366  -21.546 6.501  1    61.089  ? 2    NAG B C5  1 ? 
HETATM 4779 C  C6  . NAG B 2 .   ? 25.321  -22.667 6.793  1    60.98   ? 2    NAG B C6  1 ? 
HETATM 4780 C  C7  . NAG B 2 .   ? 21.072  -17.862 8.187  1    63.431  ? 2    NAG B C7  1 ? 
HETATM 4781 C  C8  . NAG B 2 .   ? 21.308  -16.388 8.003  1    60.262  ? 2    NAG B C8  1 ? 
HETATM 4782 N  N2  . NAG B 2 .   ? 21.444  -18.649 7.186  1    61.957  ? 2    NAG B N2  1 ? 
HETATM 4783 O  O3  . NAG B 2 .   ? 24.067  -17.978 7.505  1    62.298  ? 2    NAG B O3  1 ? 
HETATM 4784 O  O4  . NAG B 2 .   ? 26.031  -19.806 6.264  1    53.695  ? 2    NAG B O4  1 ? 
HETATM 4785 O  O5  . NAG B 2 .   ? 23.13   -21.907 7.153  1    56.117  ? 2    NAG B O5  1 ? 
HETATM 4786 O  O6  . NAG B 2 .   ? 24.659  -23.839 6.348  1    70.028  ? 2    NAG B O6  1 ? 
HETATM 4787 O  O7  . NAG B 2 .   ? 20.646  -18.35  9.226  1    52.886  ? 2    NAG B O7  1 ? 
HETATM 4788 C  C1  . BMA B 2 .   ? 26.832  -18.778 6.743  1    67.265  ? 3    BMA B C1  1 ? 
HETATM 4789 C  C2  . BMA B 2 .   ? 28.209  -19.009 6.133  1    74.93   ? 3    BMA B C2  1 ? 
HETATM 4790 C  C3  . BMA B 2 .   ? 29.132  -17.807 6.419  1    74.375  ? 3    BMA B C3  1 ? 
HETATM 4791 C  C4  . BMA B 2 .   ? 28.498  -16.554 5.77   1    88.674  ? 3    BMA B C4  1 ? 
HETATM 4792 C  C5  . BMA B 2 .   ? 27.17   -16.332 6.541  1    93.399  ? 3    BMA B C5  1 ? 
HETATM 4793 C  C6  . BMA B 2 .   ? 26.408  -15.032 6.242  1    81.051  ? 3    BMA B C6  1 ? 
HETATM 4794 O  O2  . BMA B 2 .   ? 28.076  -19.3   4.741  1    84.769  ? 3    BMA B O2  1 ? 
HETATM 4795 O  O3  . BMA B 2 .   ? 30.542  -18.089 6.165  1    71.731  ? 3    BMA B O3  1 ? 
HETATM 4796 O  O4  . BMA B 2 .   ? 29.293  -15.358 5.785  1    84.81   ? 3    BMA B O4  1 ? 
HETATM 4797 O  O5  . BMA B 2 .   ? 26.291  -17.513 6.336  1    90.155  ? 3    BMA B O5  1 ? 
HETATM 4798 O  O6  . BMA B 2 .   ? 25.527  -15.077 5.076  1    68.843  ? 3    BMA B O6  1 ? 
HETATM 4799 C  C1  . MAN B 2 .   ? 31.068  -19.162 6.906  1    76.465  ? 4    MAN B C1  1 ? 
HETATM 4800 C  C2  . MAN B 2 .   ? 32.594  -19.324 7.057  1    92.209  ? 4    MAN B C2  1 ? 
HETATM 4801 C  C3  . MAN B 2 .   ? 33.219  -20.555 6.385  1    76.025  ? 4    MAN B C3  1 ? 
HETATM 4802 C  C4  . MAN B 2 .   ? 32.389  -21.737 6.758  1    80.387  ? 4    MAN B C4  1 ? 
HETATM 4803 C  C5  . MAN B 2 .   ? 31.055  -21.52  6.039  1    93.507  ? 4    MAN B C5  1 ? 
HETATM 4804 C  C6  . MAN B 2 .   ? 30.117  -22.72  6.073  1    93.974  ? 4    MAN B C6  1 ? 
HETATM 4805 O  O2  . MAN B 2 .   ? 32.927  -19.406 8.469  1    94.563  ? 4    MAN B O2  1 ? 
HETATM 4806 O  O3  . MAN B 2 .   ? 34.552  -20.818 6.832  1    67.021  ? 4    MAN B O3  1 ? 
HETATM 4807 O  O4  . MAN B 2 .   ? 33.089  -22.908 6.376  1    51.302  ? 4    MAN B O4  1 ? 
HETATM 4808 O  O5  . MAN B 2 .   ? 30.363  -20.392 6.679  1    72.57   ? 4    MAN B O5  1 ? 
HETATM 4809 O  O6  . MAN B 2 .   ? 29.195  -22.667 7.176  1    102.764 ? 4    MAN B O6  1 ? 
HETATM 4810 C  C1  . NAG B 2 .   ? 33.448  -18.245 9.031  0.92 90.727  ? 5    NAG B C1  1 ? 
HETATM 4811 C  C2  . NAG B 2 .   ? 34.476  -18.591 10.101 0.92 88.83   ? 5    NAG B C2  1 ? 
HETATM 4812 C  C3  . NAG B 2 .   ? 35.061  -17.307 10.692 0.92 91.07   ? 5    NAG B C3  1 ? 
HETATM 4813 C  C4  . NAG B 2 .   ? 35.532  -16.349 9.599  0.92 93.749  ? 5    NAG B C4  1 ? 
HETATM 4814 C  C5  . NAG B 2 .   ? 34.353  -16.085 8.663  0.92 92.659  ? 5    NAG B C5  1 ? 
HETATM 4815 C  C6  . NAG B 2 .   ? 34.594  -15.082 7.554  0.92 77.69   ? 5    NAG B C6  1 ? 
HETATM 4816 C  C7  . NAG B 2 .   ? 33.836  -20.726 11.124 0.92 80.183  ? 5    NAG B C7  1 ? 
HETATM 4817 C  C8  . NAG B 2 .   ? 34.844  -21.43  11.986 0.92 64.282  ? 5    NAG B C8  1 ? 
HETATM 4818 N  N2  . NAG B 2 .   ? 33.872  -19.394 11.145 0.92 82.084  ? 5    NAG B N2  1 ? 
HETATM 4819 O  O3  . NAG B 2 .   ? 36.102  -17.615 11.605 0.92 86.777  ? 5    NAG B O3  1 ? 
HETATM 4820 O  O4  . NAG B 2 .   ? 35.952  -15.127 10.198 0.92 101.223 ? 5    NAG B O4  1 ? 
HETATM 4821 O  O5  . NAG B 2 .   ? 34.01   -17.351 8.065  0.92 94.734  ? 5    NAG B O5  1 ? 
HETATM 4822 O  O6  . NAG B 2 .   ? 35.338  -15.66  6.492  0.92 88.493  ? 5    NAG B O6  1 ? 
HETATM 4823 O  O7  . NAG B 2 .   ? 33.03   -21.335 10.423 0.92 94.82   ? 5    NAG B O7  1 ? 
HETATM 4824 C  C1  . MAN B 2 .   ? 25.365  -13.902 4.313  0.94 68.13   ? 6    MAN B C1  1 ? 
HETATM 4825 C  C2  . MAN B 2 .   ? 24.97   -14.316 2.891  0.94 68.849  ? 6    MAN B C2  1 ? 
HETATM 4826 C  C3  . MAN B 2 .   ? 26.186  -15     2.191  0.94 73.121  ? 6    MAN B C3  1 ? 
HETATM 4827 C  C4  . MAN B 2 .   ? 27.459  -14.122 2.182  0.94 79.897  ? 6    MAN B C4  1 ? 
HETATM 4828 C  C5  . MAN B 2 .   ? 27.722  -13.45  3.564  0.94 78.469  ? 6    MAN B C5  1 ? 
HETATM 4829 C  C6  . MAN B 2 .   ? 28.719  -12.291 3.525  0.94 74.18   ? 6    MAN B C6  1 ? 
HETATM 4830 O  O2  . MAN B 2 .   ? 24.372  -13.211 2.148  0.94 57.215  ? 6    MAN B O2  1 ? 
HETATM 4831 O  O3  . MAN B 2 .   ? 25.854  -15.425 0.87   0.94 67.807  ? 6    MAN B O3  1 ? 
HETATM 4832 O  O4  . MAN B 2 .   ? 28.607  -14.933 1.862  0.94 67.236  ? 6    MAN B O4  1 ? 
HETATM 4833 O  O5  . MAN B 2 .   ? 26.486  -13.003 4.278  0.94 61.67   ? 6    MAN B O5  1 ? 
HETATM 4834 O  O6  . MAN B 2 .   ? 28.184  -11.033 3.037  0.94 67.926  ? 6    MAN B O6  1 ? 
HETATM 4835 C  C1  . NAG B 2 .   ? 23.228  -12.528 2.577  0.79 56.93   ? 7    NAG B C1  1 ? 
HETATM 4836 C  C2  . NAG B 2 .   ? 23.031  -11.183 1.866  0.79 67.258  ? 7    NAG B C2  1 ? 
HETATM 4837 C  C3  . NAG B 2 .   ? 21.729  -10.544 2.366  0.79 55.741  ? 7    NAG B C3  1 ? 
HETATM 4838 C  C4  . NAG B 2 .   ? 20.546  -11.473 2.119  0.79 52.277  ? 7    NAG B C4  1 ? 
HETATM 4839 C  C5  . NAG B 2 .   ? 20.803  -12.824 2.768  0.79 49.328  ? 7    NAG B C5  1 ? 
HETATM 4840 C  C6  . NAG B 2 .   ? 19.752  -13.842 2.343  0.79 58.3    ? 7    NAG B C6  1 ? 
HETATM 4841 C  C7  . NAG B 2 .   ? 25.084  -10.204 0.936  0.79 56.883  ? 7    NAG B C7  1 ? 
HETATM 4842 C  C8  . NAG B 2 .   ? 26.471  -9.748  1.277  0.79 44.936  ? 7    NAG B C8  1 ? 
HETATM 4843 N  N2  . NAG B 2 .   ? 24.195  -10.301 1.936  0.79 65.781  ? 7    NAG B N2  1 ? 
HETATM 4844 O  O3  . NAG B 2 .   ? 21.476  -9.232  1.866  0.79 65.738  ? 7    NAG B O3  1 ? 
HETATM 4845 O  O4  . NAG B 2 .   ? 19.342  -10.966 2.701  0.79 33.08   ? 7    NAG B O4  1 ? 
HETATM 4846 O  O5  . NAG B 2 .   ? 22.089  -13.364 2.391  0.79 51.455  ? 7    NAG B O5  1 ? 
HETATM 4847 O  O6  . NAG B 2 .   ? 19.942  -15.117 3      0.79 64.604  ? 7    NAG B O6  1 ? 
HETATM 4848 O  O7  . NAG B 2 .   ? 24.766  -10.477 -0.215 0.79 57.106  ? 7    NAG B O7  1 ? 
HETATM 4849 C  C1  . FUC B 2 .   ? 19.414  -20.059 3.995  1    51.975  ? 8    FUC B C1  1 ? 
HETATM 4850 C  C2  . FUC B 2 .   ? 20.271  -20.528 2.82   1    50.942  ? 8    FUC B C2  1 ? 
HETATM 4851 C  C3  . FUC B 2 .   ? 19.547  -21.637 2.09   1    55.917  ? 8    FUC B C3  1 ? 
HETATM 4852 C  C4  . FUC B 2 .   ? 18.205  -21.127 1.597  1    54.877  ? 8    FUC B C4  1 ? 
HETATM 4853 C  C5  . FUC B 2 .   ? 17.4    -20.654 2.804  1    49.282  ? 8    FUC B C5  1 ? 
HETATM 4854 C  C6  . FUC B 2 .   ? 16.057  -20.059 2.449  1    42.832  ? 8    FUC B C6  1 ? 
HETATM 4855 O  O2  . FUC B 2 .   ? 21.555  -20.931 3.269  1    61.841  ? 8    FUC B O2  1 ? 
HETATM 4856 O  O3  . FUC B 2 .   ? 20.358  -22.093 1.022  1    68.707  ? 8    FUC B O3  1 ? 
HETATM 4857 O  O4  . FUC B 2 .   ? 18.428  -20.015 0.724  1    55.178  ? 8    FUC B O4  1 ? 
HETATM 4858 O  O5  . FUC B 2 .   ? 18.153  -19.623 3.484  1    51.968  ? 8    FUC B O5  1 ? 
HETATM 4859 ZN ZN  . ZN  C 3 .   ? 15.776  4.23    20.205 1    25.206  ? 701  ZN  A ZN  1 1 
HETATM 4860 C  C1  . NAG D 4 .   ? 12.961  19.864  -1.212 0.99 86.511  ? 702  NAG A C1  1 1 
HETATM 4861 C  C2  . NAG D 4 .   ? 14.122  19.676  -2.196 0.99 90.617  ? 702  NAG A C2  1 1 
HETATM 4862 C  C3  . NAG D 4 .   ? 13.767  20.14   -3.617 0.99 90.57   ? 702  NAG A C3  1 1 
HETATM 4863 C  C4  . NAG D 4 .   ? 12.44   19.548  -4.081 0.99 93.457  ? 702  NAG A C4  1 1 
HETATM 4864 C  C5  . NAG D 4 .   ? 11.36   19.964  -3.078 0.99 95.576  ? 702  NAG A C5  1 1 
HETATM 4865 C  C6  . NAG D 4 .   ? 9.994   19.404  -3.417 0.99 97.014  ? 702  NAG A C6  1 1 
HETATM 4866 C  C7  . NAG D 4 .   ? 16.467  19.533  -1.505 0.99 74.565  ? 702  NAG A C7  1 1 
HETATM 4867 C  C8  . NAG D 4 .   ? 17.764  20.278  -1.469 0.99 71.082  ? 702  NAG A C8  1 1 
HETATM 4868 N  N2  . NAG D 4 .   ? 15.368  20.26   -1.721 0.99 82.997  ? 702  NAG A N2  1 1 
HETATM 4869 O  O3  . NAG D 4 .   ? 14.813  19.793  -4.517 0.99 83.767  ? 702  NAG A O3  1 1 
HETATM 4870 O  O4  . NAG D 4 .   ? 12.13   19.921  -5.433 0.99 96.627  ? 702  NAG A O4  1 1 
HETATM 4871 O  O5  . NAG D 4 .   ? 11.691  19.474  -1.755 0.99 85.836  ? 702  NAG A O5  1 1 
HETATM 4872 O  O6  . NAG D 4 .   ? 10.106  18.055  -3.894 0.99 97.445  ? 702  NAG A O6  1 1 
HETATM 4873 O  O7  . NAG D 4 .   ? 16.409  18.321  -1.337 0.99 75.482  ? 702  NAG A O7  1 1 
HETATM 4874 CL CL  . CL  E 5 .   ? 0.833   14.399  31.154 1    23.674  ? 703  CL  A CL  1 1 
HETATM 4875 CL CL  . CL  F 5 .   ? 8.035   -2.561  22.404 1    24.305  ? 704  CL  A CL  1 1 
HETATM 4876 C  C01 . BJ2 G 6 .   ? 14.985  9.969   21.07  1    46.255  ? 705  BJ2 A C01 1 ? 
HETATM 4877 C  C02 . BJ2 G 6 .   ? 14.222  8.631   20.854 1    42.55   ? 705  BJ2 A C02 1 ? 
HETATM 4878 C  C04 . BJ2 G 6 .   ? 13.199  7.209   18.994 1    43.303  ? 705  BJ2 A C04 1 ? 
HETATM 4879 C  C05 . BJ2 G 6 .   ? 14.292  6.187   19.213 1    41.144  ? 705  BJ2 A C05 1 ? 
HETATM 4880 C  C08 . BJ2 G 6 .   ? 12.796  7.158   17.536 1    38.464  ? 705  BJ2 A C08 1 ? 
HETATM 4881 C  C09 . BJ2 G 6 .   ? 11.213  7.52    17.566 1    41.045  ? 705  BJ2 A C09 1 ? 
HETATM 4882 C  C10 . BJ2 G 6 .   ? 10.723  6.333   17.994 1    37.214  ? 705  BJ2 A C10 1 ? 
HETATM 4883 C  C11 . BJ2 G 6 .   ? 11.357  5.387   16.931 1    33.059  ? 705  BJ2 A C11 1 ? 
HETATM 4884 C  C13 . BJ2 G 6 .   ? 13.827  5.359   16.052 1    34.533  ? 705  BJ2 A C13 1 ? 
HETATM 4885 C  C15 . BJ2 G 6 .   ? 13.514  3.976   15.344 1    35.038  ? 705  BJ2 A C15 1 ? 
HETATM 4886 C  C17 . BJ2 G 6 .   ? 14.692  3.093   15.715 1    38.523  ? 705  BJ2 A C17 1 ? 
HETATM 4887 C  C18 . BJ2 G 6 .   ? 14.406  1.594   15.775 1    44.795  ? 705  BJ2 A C18 1 ? 
HETATM 4888 C  C21 . BJ2 G 6 .   ? 13.103  8.489   21.947 1    44.476  ? 705  BJ2 A C21 1 ? 
HETATM 4889 C  C24 . BJ2 G 6 .   ? 14.814  7.569   23.625 1    38.963  ? 705  BJ2 A C24 1 ? 
HETATM 4890 C  C25 . BJ2 G 6 .   ? 14.777  7.122   25.179 1    49.803  ? 705  BJ2 A C25 1 ? 
HETATM 4891 C  C26 . BJ2 G 6 .   ? 13.244  7.367   25.636 1    40.836  ? 705  BJ2 A C26 1 ? 
HETATM 4892 C  C27 . BJ2 G 6 .   ? 12.425  7.783   24.58  1    34.904  ? 705  BJ2 A C27 1 ? 
HETATM 4893 C  C28 . BJ2 G 6 .   ? 11.672  9.11    24.796 1    27.603  ? 705  BJ2 A C28 1 ? 
HETATM 4894 N  N03 . BJ2 G 6 .   ? 13.686  8.578   19.448 1    58.86   ? 705  BJ2 A N03 1 ? 
HETATM 4895 N  N12 . BJ2 G 6 .   ? 12.798  5.982   16.855 1    32.36   ? 705  BJ2 A N12 1 ? 
HETATM 4896 N  N16 . BJ2 G 6 .   ? 13.319  3.986   13.877 1    39.764  ? 705  BJ2 A N16 1 ? 
HETATM 4897 N  N23 . BJ2 G 6 .   ? 13.509  7.954   23.292 1    50.74   ? 705  BJ2 A N23 1 ? 
HETATM 4898 O  O06 . BJ2 G 6 .   ? 15.447  6.494   18.849 1    39.555  ? 705  BJ2 A O06 1 ? 
HETATM 4899 O  O07 . BJ2 G 6 .   ? 14.013  5.105   19.778 1    44.321  ? 705  BJ2 A O07 1 ? 
HETATM 4900 O  O14 . BJ2 G 6 .   ? 14.945  5.833   16.069 1    28.044  ? 705  BJ2 A O14 1 ? 
HETATM 4901 O  O19 . BJ2 G 6 .   ? 15.197  0.634   15.55  1    52.105  ? 705  BJ2 A O19 1 ? 
HETATM 4902 O  O20 . BJ2 G 6 .   ? 13.278  1.299   16.126 1    39.075  ? 705  BJ2 A O20 1 ? 
HETATM 4903 O  O22 . BJ2 G 6 .   ? 11.938  8.793   21.734 1    28.785  ? 705  BJ2 A O22 1 ? 
HETATM 4904 O  O29 . BJ2 G 6 .   ? 10.513  9.428   25.243 1    27.87   ? 705  BJ2 A O29 1 ? 
HETATM 4905 O  O30 . BJ2 G 6 .   ? 12.217  10.123  24.392 1    32.738  ? 705  BJ2 A O30 1 ? 
HETATM 4906 O  O   . HOH H 7 .   ? 11.734  11.028  13.085 1    44.28   ? 801  HOH A O   1 1 
HETATM 4907 O  O   . HOH H 7 .   ? 1.074   2.014   14.443 1    42.721  ? 802  HOH A O   1 1 
HETATM 4908 O  O   . HOH H 7 .   ? -9.29   -7.162  5.327  1    46.181  ? 803  HOH A O   1 1 
HETATM 4909 O  O   . HOH H 7 .   ? 5.985   22.13   18.34  1    38.45   ? 804  HOH A O   1 1 
HETATM 4910 O  O   . HOH H 7 .   ? 3.793   -3.346  -4.51  1    43.448  ? 805  HOH A O   1 1 
HETATM 4911 O  O   . HOH H 7 .   ? 24.6    19.268  32.108 1    45.435  ? 806  HOH A O   1 1 
HETATM 4912 O  O   . HOH H 7 .   ? 26.479  5.51    50.087 1    31.264  ? 807  HOH A O   1 1 
HETATM 4913 O  O   . HOH H 7 .   ? -2.015  30.662  37.594 1    32.019  ? 808  HOH A O   1 1 
HETATM 4914 O  O   . HOH H 7 .   ? 11.908  27.596  51.371 1    47.232  ? 809  HOH A O   1 1 
HETATM 4915 O  O   . HOH H 7 .   ? -7.481  21.211  32.113 1    41.473  ? 810  HOH A O   1 1 
HETATM 4916 O  O   . HOH H 7 .   ? 21.247  20.522  47.598 1    41.516  ? 811  HOH A O   1 1 
HETATM 4917 O  O   . HOH H 7 .   ? 24.338  6.533   54.978 1    42.696  ? 812  HOH A O   1 1 
HETATM 4918 O  O   . HOH H 7 .   ? 33.318  4.285   7.624  1    50.423  ? 813  HOH A O   1 1 
HETATM 4919 O  O   . HOH H 7 .   ? 15.248  15.534  31.394 1    37.255  ? 814  HOH A O   1 1 
HETATM 4920 O  O   . HOH H 7 .   ? -11.014 11.338  29.521 1    31.81   ? 815  HOH A O   1 1 
HETATM 4921 O  O   . HOH H 7 .   ? 7.6     13.326  53.783 1    31.339  ? 816  HOH A O   1 1 
HETATM 4922 O  O   . HOH H 7 .   ? 43.112  5.109   23.26  1    44.285  ? 817  HOH A O   1 1 
HETATM 4923 O  O   . HOH H 7 .   ? 30.842  -0.085  8.412  1    46.51   ? 818  HOH A O   1 1 
HETATM 4924 O  O   . HOH H 7 .   ? 16.666  -2.862  10.677 1    29.453  ? 819  HOH A O   1 1 
HETATM 4925 O  O   . HOH H 7 .   ? -0.644  28.413  39.833 1    40.121  ? 820  HOH A O   1 1 
HETATM 4926 O  O   . HOH H 7 .   ? 22.607  12.726  54.502 1    40.608  ? 821  HOH A O   1 1 
HETATM 4927 O  O   . HOH H 7 .   ? 11.55   23.054  38.828 1    26.583  ? 822  HOH A O   1 1 
HETATM 4928 O  O   . HOH H 7 .   ? 1.4     22.281  50.949 1    38.085  ? 823  HOH A O   1 1 
HETATM 4929 O  O   . HOH H 7 .   ? 24.233  -7.748  40.069 1    38.543  ? 824  HOH A O   1 1 
HETATM 4930 O  O   . HOH H 7 .   ? 29.596  4.784   2.437  1    45.972  ? 825  HOH A O   1 1 
HETATM 4931 O  O   . HOH H 7 .   ? 28.067  5.129   34.174 1    28.428  ? 826  HOH A O   1 1 
HETATM 4932 O  O   . HOH H 7 .   ? 18.38   -13.984 20.992 1    49.521  ? 827  HOH A O   1 1 
HETATM 4933 O  O   . HOH H 7 .   ? -9.108  16.955  18.906 1    32.882  ? 828  HOH A O   1 1 
HETATM 4934 O  O   . HOH H 7 .   ? 32.9    6.359   10.605 1    44.612  ? 829  HOH A O   1 1 
HETATM 4935 O  O   . HOH H 7 .   ? 10.619  31.542  33.864 1    43.122  ? 830  HOH A O   1 1 
HETATM 4936 O  O   . HOH H 7 .   ? 1.041   8.452   13.518 1    47.32   ? 831  HOH A O   1 1 
HETATM 4937 O  O   . HOH H 7 .   ? 24.947  -8.643  34     1    21.662  ? 832  HOH A O   1 1 
HETATM 4938 O  O   . HOH H 7 .   ? 36.744  -11.052 29.496 1    32.531  ? 833  HOH A O   1 1 
HETATM 4939 O  O   . HOH H 7 .   ? 12.66   28.864  25.508 1    32.712  ? 834  HOH A O   1 1 
HETATM 4940 O  O   . HOH H 7 .   ? 19.47   9.154   59.226 1    33.421  ? 835  HOH A O   1 1 
HETATM 4941 O  O   . HOH H 7 .   ? -0.62   5.324   20.353 1    19.779  ? 836  HOH A O   1 1 
HETATM 4942 O  O   . HOH H 7 .   ? 14.22   -4.082  45.578 1    28.899  ? 837  HOH A O   1 1 
HETATM 4943 O  O   . HOH H 7 .   ? 34.438  10.724  43.096 1    41.499  ? 838  HOH A O   1 1 
HETATM 4944 O  O   . HOH H 7 .   ? -5.215  -7.96   25.127 1    24.969  ? 839  HOH A O   1 1 
HETATM 4945 O  O   . HOH H 7 .   ? -0.786  21.319  15.998 1    39.028  ? 840  HOH A O   1 1 
HETATM 4946 O  O   . HOH H 7 .   ? 16.85   -14.069 -1.893 1    36.724  ? 841  HOH A O   1 1 
HETATM 4947 O  O   . HOH H 7 .   ? 30.259  16.827  42.02  1    38.734  ? 842  HOH A O   1 1 
HETATM 4948 O  O   . HOH H 7 .   ? -12.37  12.077  20.068 1    30.783  ? 843  HOH A O   1 1 
HETATM 4949 O  O   . HOH H 7 .   ? 13.282  -0.837  19.548 1    19.854  ? 844  HOH A O   1 1 
HETATM 4950 O  O   . HOH H 7 .   ? 3.654   -2.486  24.073 1    20.008  ? 845  HOH A O   1 1 
HETATM 4951 O  O   . HOH H 7 .   ? 14.843  17.284  33.907 1    25.547  ? 846  HOH A O   1 1 
HETATM 4952 O  O   . HOH H 7 .   ? 15.473  -9.172  38.973 1    36.369  ? 847  HOH A O   1 1 
HETATM 4953 O  O   . HOH H 7 .   ? 14.682  -15.87  29.975 1    32.469  ? 848  HOH A O   1 1 
HETATM 4954 O  O   . HOH H 7 .   ? 20.239  -5.928  1.791  1    57.272  ? 849  HOH A O   1 1 
HETATM 4955 O  O   . HOH H 7 .   ? 9.618   14.089  50.971 1    18.771  ? 850  HOH A O   1 1 
HETATM 4956 O  O   . HOH H 7 .   ? 23.807  6.399   4.785  1    45.734  ? 851  HOH A O   1 1 
HETATM 4957 O  O   . HOH H 7 .   ? 29.376  0.867   29.457 1    22.076  ? 852  HOH A O   1 1 
HETATM 4958 O  O   . HOH H 7 .   ? 11.26   -15.226 26.567 1    28.824  ? 853  HOH A O   1 1 
HETATM 4959 O  O   . HOH H 7 .   ? 39.953  11.009  32.979 1    38.857  ? 854  HOH A O   1 1 
HETATM 4960 O  O   . HOH H 7 .   ? 21.716  3.75    54.528 1    42.076  ? 855  HOH A O   1 1 
HETATM 4961 O  O   . HOH H 7 .   ? -10.68  2.027   23.995 1    20.435  ? 856  HOH A O   1 1 
HETATM 4962 O  O   . HOH H 7 .   ? 5.564   -31.383 0.212  1    67.847  ? 857  HOH A O   1 1 
HETATM 4963 O  O   . HOH H 7 .   ? 4.23    9.912   52.625 1    46.853  ? 858  HOH A O   1 1 
HETATM 4964 O  O   . HOH H 7 .   ? 5.043   1.072   29.003 1    19.797  ? 859  HOH A O   1 1 
HETATM 4965 O  O   . HOH H 7 .   ? 34.203  8.815   12.768 1    51.311  ? 860  HOH A O   1 1 
HETATM 4966 O  O   . HOH H 7 .   ? -2.442  -3.708  14.463 1    27.669  ? 861  HOH A O   1 1 
HETATM 4967 O  O   . HOH H 7 .   ? 27.824  -5.275  40.077 1    48.652  ? 862  HOH A O   1 1 
HETATM 4968 O  O   . HOH H 7 .   ? 12.781  9.081   60.427 1    41.146  ? 863  HOH A O   1 1 
HETATM 4969 O  O   . HOH H 7 .   ? 20.254  -4.049  8.458  1    33.261  ? 864  HOH A O   1 1 
HETATM 4970 O  O   . HOH H 7 .   ? 14.045  6.332   53.63  1    33.479  ? 865  HOH A O   1 1 
HETATM 4971 O  O   . HOH H 7 .   ? -4.223  5.883   41.017 1    28.707  ? 866  HOH A O   1 1 
HETATM 4972 O  O   . HOH H 7 .   ? 22.93   10.284  53.764 1    30.012  ? 867  HOH A O   1 1 
HETATM 4973 O  O   . HOH H 7 .   ? 5.174   14.475  15.499 1    35.714  ? 868  HOH A O   1 1 
HETATM 4974 O  O   . HOH H 7 .   ? 24.789  16.595  52.096 1    40.302  ? 869  HOH A O   1 1 
HETATM 4975 O  O   . HOH H 7 .   ? 30.107  3.112   14.839 1    29.726  ? 870  HOH A O   1 1 
HETATM 4976 O  O   . HOH H 7 .   ? 12.136  6.254   -3.03  1    51.703  ? 871  HOH A O   1 1 
HETATM 4977 O  O   . HOH H 7 .   ? 14.886  14.167  52.599 1    25.361  ? 872  HOH A O   1 1 
HETATM 4978 O  O   . HOH H 7 .   ? 31.829  8.618   22.799 1    38.148  ? 873  HOH A O   1 1 
HETATM 4979 O  O   . HOH H 7 .   ? 24.888  -9.493  9.453  1    32.119  ? 874  HOH A O   1 1 
HETATM 4980 O  O   . HOH H 7 .   ? 12.225  23.533  36.052 1    34.359  ? 875  HOH A O   1 1 
HETATM 4981 O  O   . HOH H 7 .   ? 22.852  5.856   28.998 1    23.289  ? 876  HOH A O   1 1 
HETATM 4982 O  O   . HOH H 7 .   ? -9.165  -7.286  23.509 1    29.957  ? 877  HOH A O   1 1 
HETATM 4983 O  O   . HOH H 7 .   ? 12.221  -13.872 21.375 1    26.03   ? 878  HOH A O   1 1 
HETATM 4984 O  O   . HOH H 7 .   ? -0.86   23.954  41.096 1    32.744  ? 879  HOH A O   1 1 
HETATM 4985 O  O   . HOH H 7 .   ? 14.551  -12.566 18.543 1    45.811  ? 880  HOH A O   1 1 
HETATM 4986 O  O   . HOH H 7 .   ? 10.947  18.405  28.093 1    23.907  ? 881  HOH A O   1 1 
HETATM 4987 O  O   . HOH H 7 .   ? 17.045  3.204   25.882 1    33.582  ? 882  HOH A O   1 1 
HETATM 4988 O  O   . HOH H 7 .   ? -7.607  10.162  37.641 1    27.866  ? 883  HOH A O   1 1 
HETATM 4989 O  O   . HOH H 7 .   ? 19.126  3.622   -0.174 1    41.963  ? 884  HOH A O   1 1 
HETATM 4990 O  O   . HOH H 7 .   ? 20.263  -9.746  18.386 1    23.079  ? 885  HOH A O   1 1 
HETATM 4991 O  O   . HOH H 7 .   ? 16.714  16.271  52.169 1    26.144  ? 886  HOH A O   1 1 
HETATM 4992 O  O   . HOH H 7 .   ? 7.536   1.738   -1.521 1    43.599  ? 887  HOH A O   1 1 
HETATM 4993 O  O   . HOH H 7 .   ? -12.113 8.854   10.539 1    47.756  ? 888  HOH A O   1 1 
HETATM 4994 O  O   . HOH H 7 .   ? 31.744  -6.277  15.067 1    42.865  ? 889  HOH A O   1 1 
HETATM 4995 O  O   . HOH H 7 .   ? 20.3    -0.388  45.219 1    42.667  ? 890  HOH A O   1 1 
HETATM 4996 O  O   . HOH H 7 .   ? 6.092   -8.185  4.683  1    37.691  ? 891  HOH A O   1 1 
HETATM 4997 O  O   . HOH H 7 .   ? 9.787   -8.078  42.464 1    36.8    ? 892  HOH A O   1 1 
HETATM 4998 O  O   . HOH H 7 .   ? 16.871  -7.535  -4.16  1    53.421  ? 893  HOH A O   1 1 
HETATM 4999 O  O   . HOH H 7 .   ? 5.346   -11.721 24.409 1    24.825  ? 894  HOH A O   1 1 
HETATM 5000 O  O   . HOH H 7 .   ? 12.833  -7.098  17.939 1    21.112  ? 895  HOH A O   1 1 
HETATM 5001 O  O   . HOH H 7 .   ? 27.976  1.125   42.029 1    27.418  ? 896  HOH A O   1 1 
HETATM 5002 O  O   . HOH H 7 .   ? -8.206  -12.355 16.002 1    31.038  ? 897  HOH A O   1 1 
HETATM 5003 O  O   . HOH H 7 .   ? 13.036  20.015  29.384 1    21.291  ? 898  HOH A O   1 1 
HETATM 5004 O  O   . HOH H 7 .   ? 29.942  3.348   35.139 1    23.815  ? 899  HOH A O   1 1 
HETATM 5005 O  O   . HOH H 7 .   ? 8.154   18.533  34.912 1    17.024  ? 900  HOH A O   1 1 
HETATM 5006 O  O   . HOH H 7 .   ? 36.675  1.125   34.04  1    42.455  ? 901  HOH A O   1 1 
HETATM 5007 O  O   . HOH H 7 .   ? -9.614  12.539  6.465  1    56.424  ? 902  HOH A O   1 1 
HETATM 5008 O  O   . HOH H 7 .   ? 3.611   19.26   53.569 1    21.687  ? 903  HOH A O   1 1 
HETATM 5009 O  O   . HOH H 7 .   ? 27.747  18.927  41.969 1    41.823  ? 904  HOH A O   1 1 
HETATM 5010 O  O   . HOH H 7 .   ? 16.135  17.151  49.596 1    27.723  ? 905  HOH A O   1 1 
HETATM 5011 O  O   . HOH H 7 .   ? -11.684 -2.223  16.281 1    26.814  ? 906  HOH A O   1 1 
HETATM 5012 O  O   . HOH H 7 .   ? -5.181  18.485  14.029 1    44.841  ? 907  HOH A O   1 1 
HETATM 5013 O  O   . HOH H 7 .   ? 19.466  -4.302  35.934 1    20.588  ? 908  HOH A O   1 1 
HETATM 5014 O  O   . HOH H 7 .   ? 20.716  -0.328  4.56   1    38.525  ? 909  HOH A O   1 1 
HETATM 5015 O  O   . HOH H 7 .   ? -10.386 -4.514  21.769 1    31.51   ? 910  HOH A O   1 1 
HETATM 5016 O  O   . HOH H 7 .   ? 3.272   -5.472  33.446 1    28.901  ? 911  HOH A O   1 1 
HETATM 5017 O  O   . HOH H 7 .   ? 36.242  19.483  24.618 1    50.636  ? 912  HOH A O   1 1 
HETATM 5018 O  O   . HOH H 7 .   ? 14.802  -0.34   44.627 1    24.671  ? 913  HOH A O   1 1 
HETATM 5019 O  O   . HOH H 7 .   ? 10.823  -10.47  36.397 1    48.108  ? 914  HOH A O   1 1 
HETATM 5020 O  O   . HOH H 7 .   ? 12.055  22.263  53.134 1    42.169  ? 915  HOH A O   1 1 
HETATM 5021 O  O   . HOH H 7 .   ? 9.01    9.579   37.361 1    24.228  ? 916  HOH A O   1 1 
HETATM 5022 O  O   . HOH H 7 .   ? 10.256  22.037  35.459 1    27.64   ? 917  HOH A O   1 1 
HETATM 5023 O  O   . HOH H 7 .   ? -11.914 3.305   19.691 1    21.984  ? 918  HOH A O   1 1 
HETATM 5024 O  O   . HOH H 7 .   ? -0.487  -13.569 -3.167 1    44.654  ? 919  HOH A O   1 1 
HETATM 5025 O  O   . HOH H 7 .   ? -0.021  -7.482  13.831 1    45.594  ? 920  HOH A O   1 1 
HETATM 5026 O  O   . HOH H 7 .   ? 8.645   14.996  21.67  1    27.076  ? 921  HOH A O   1 1 
HETATM 5027 O  O   . HOH H 7 .   ? 18.824  -13.356 -5.21  1    51.763  ? 922  HOH A O   1 1 
HETATM 5028 O  O   . HOH H 7 .   ? 17.343  -2.746  -0.907 1    51.458  ? 923  HOH A O   1 1 
HETATM 5029 O  O   . HOH H 7 .   ? 22.997  -7.205  2.998  1    57.334  ? 924  HOH A O   1 1 
HETATM 5030 O  O   . HOH H 7 .   ? 23.529  17.108  8.545  1    45.007  ? 925  HOH A O   1 1 
HETATM 5031 O  O   . HOH H 7 .   ? -2.129  -2.403  31.648 1    30.505  ? 926  HOH A O   1 1 
HETATM 5032 O  O   . HOH H 7 .   ? 5.926   24.773  14.614 1    46.424  ? 927  HOH A O   1 1 
HETATM 5033 O  O   . HOH H 7 .   ? 27.401  -1.533  5.367  1    49.84   ? 928  HOH A O   1 1 
HETATM 5034 O  O   . HOH H 7 .   ? -11.772 9.375   16.32  1    37.795  ? 929  HOH A O   1 1 
HETATM 5035 O  O   . HOH H 7 .   ? 31.963  8.572   40.307 1    41.962  ? 930  HOH A O   1 1 
HETATM 5036 O  O   . HOH H 7 .   ? 26.496  -14.604 16.726 1    32.96   ? 931  HOH A O   1 1 
HETATM 5037 O  O   . HOH H 7 .   ? -3.843  -5.03   25.069 1    20.236  ? 932  HOH A O   1 1 
HETATM 5038 O  O   . HOH H 7 .   ? 3.988   17.43   46.892 1    32.534  ? 933  HOH A O   1 1 
HETATM 5039 O  O   . HOH H 7 .   ? -2.312  22.402  17.824 1    40.158  ? 934  HOH A O   1 1 
HETATM 5040 O  O   . HOH H 7 .   ? 18.033  -13.51  18.025 1    27.324  ? 935  HOH A O   1 1 
HETATM 5041 O  O   . HOH H 7 .   ? 27.408  2.533   15.181 1    26.483  ? 936  HOH A O   1 1 
HETATM 5042 O  O   . HOH H 7 .   ? 17.854  27.04   35.401 1    36.865  ? 937  HOH A O   1 1 
HETATM 5043 O  O   . HOH H 7 .   ? 12.309  8.105   55.349 1    40.617  ? 938  HOH A O   1 1 
HETATM 5044 O  O   . HOH H 7 .   ? 4.712   16.444  33.216 1    19.148  ? 939  HOH A O   1 1 
HETATM 5045 O  O   . HOH H 7 .   ? -1.216  -7.198  -3.503 1    44.825  ? 940  HOH A O   1 1 
HETATM 5046 O  O   . HOH H 7 .   ? 27.042  -10.862 33.627 1    33.797  ? 941  HOH A O   1 1 
HETATM 5047 O  O   . HOH H 7 .   ? 12.415  -17.911 -7.87  1    55.3    ? 942  HOH A O   1 1 
HETATM 5048 O  O   . HOH H 7 .   ? 7.1     -9.729  -6.406 1    37.945  ? 943  HOH A O   1 1 
HETATM 5049 O  O   . HOH H 7 .   ? 20.129  -3.458  5.772  1    36.924  ? 944  HOH A O   1 1 
HETATM 5050 O  O   . HOH H 7 .   ? 13.364  -11.774 4.617  1    40.737  ? 945  HOH A O   1 1 
HETATM 5051 O  O   . HOH H 7 .   ? 13.413  -12.646 32.194 1    34.673  ? 946  HOH A O   1 1 
HETATM 5052 O  O   . HOH H 7 .   ? 11.368  12.801  24.711 1    30.734  ? 947  HOH A O   1 1 
HETATM 5053 O  O   . HOH H 7 .   ? -10.919 3.993   22.231 1    25.951  ? 948  HOH A O   1 1 
HETATM 5054 O  O   . HOH H 7 .   ? 20.669  2       20.976 1    26.91   ? 949  HOH A O   1 1 
HETATM 5055 O  O   . HOH H 7 .   ? 11.67   -11.306 20.941 1    29.219  ? 950  HOH A O   1 1 
HETATM 5056 O  O   . HOH H 7 .   ? 1.068   -11.439 23.038 1    32.92   ? 951  HOH A O   1 1 
HETATM 5057 O  O   . HOH H 7 .   ? 6.403   19.247  17.945 1    34.663  ? 952  HOH A O   1 1 
HETATM 5058 O  O   . HOH H 7 .   ? -7.426  11.554  9.574  1    42.255  ? 953  HOH A O   1 1 
HETATM 5059 O  O   . HOH H 7 .   ? 8.659   12.968  23.354 1    43.25   ? 954  HOH A O   1 1 
HETATM 5060 O  O   . HOH H 7 .   ? 21.561  -6.068  43.223 1    27.597  ? 955  HOH A O   1 1 
HETATM 5061 O  O   . HOH H 7 .   ? 6.548   -6.15   3.016  1    36.818  ? 956  HOH A O   1 1 
HETATM 5062 O  O   . HOH H 7 .   ? 25.465  4.61    5.248  1    41.614  ? 957  HOH A O   1 1 
HETATM 5063 O  O   . HOH H 7 .   ? 14.395  17.961  22.054 1    52.081  ? 958  HOH A O   1 1 
HETATM 5064 O  O   . HOH H 7 .   ? -4.554  17.601  26.702 1    26.225  ? 959  HOH A O   1 1 
HETATM 5065 O  O   . HOH H 7 .   ? 18.089  -11.99  -1.267 1    41.755  ? 960  HOH A O   1 1 
HETATM 5066 O  O   . HOH H 7 .   ? 9       11.138  -0.902 1    50.978  ? 961  HOH A O   1 1 
HETATM 5067 O  O   . HOH H 7 .   ? -9.65   -5.619  19.24  1    28.239  ? 962  HOH A O   1 1 
HETATM 5068 O  O   . HOH H 7 .   ? 13.848  -4.77   17.345 1    29.624  ? 963  HOH A O   1 1 
HETATM 5069 O  O   . HOH H 7 .   ? -1.869  5.537   2.081  1    51.822  ? 964  HOH A O   1 1 
HETATM 5070 O  O   . HOH H 7 .   ? 8.226   8.985   47.934 1    21.081  ? 965  HOH A O   1 1 
HETATM 5071 O  O   . HOH H 7 .   ? 19.148  8.128   29.622 1    38.119  ? 966  HOH A O   1 1 
HETATM 5072 O  O   . HOH H 7 .   ? 21.052  -8.104  36.951 1    37.314  ? 967  HOH A O   1 1 
HETATM 5073 O  O   . HOH H 7 .   ? 0.18    25.216  15.177 1    56.267  ? 968  HOH A O   1 1 
HETATM 5074 O  O   . HOH H 7 .   ? 1.968   13.828  28.077 1    26.151  ? 969  HOH A O   1 1 
HETATM 5075 O  O   . HOH H 7 .   ? 1.872   -3.495  6.522  1    43.055  ? 970  HOH A O   1 1 
HETATM 5076 O  O   . HOH H 7 .   ? 1.775   -2.435  39.854 1    38.63   ? 971  HOH A O   1 1 
HETATM 5077 O  O   . HOH H 7 .   ? 12.557  -10.939 34.633 1    41.344  ? 972  HOH A O   1 1 
HETATM 5078 O  O   . HOH H 7 .   ? 23.332  2.882   -0.962 1    51.148  ? 973  HOH A O   1 1 
HETATM 5079 O  O   . HOH H 7 .   ? 11.523  -15.479 23.959 1    38.081  ? 974  HOH A O   1 1 
HETATM 5080 O  O   . HOH H 7 .   ? 14.807  -8.656  27.468 1    19.624  ? 975  HOH A O   1 1 
HETATM 5081 O  O   . HOH H 7 .   ? 11.658  3.125   19.168 1    30.338  ? 976  HOH A O   1 1 
HETATM 5082 O  O   . HOH H 7 .   ? 14.762  1.633   10.05  1    42.236  ? 977  HOH A O   1 1 
HETATM 5083 O  O   . HOH H 7 .   ? 18.767  23.345  33.639 1    35.046  ? 978  HOH A O   1 1 
HETATM 5084 O  O   . HOH H 7 .   ? -18.811 11.083  19.23  1    51.588  ? 979  HOH A O   1 1 
HETATM 5085 O  O   . HOH H 7 .   ? 22.516  -10.047 34.314 1    31.897  ? 980  HOH A O   1 1 
HETATM 5086 O  O   . HOH H 7 .   ? 24.116  8.065   30.431 1    29.101  ? 981  HOH A O   1 1 
HETATM 5087 O  O   . HOH H 7 .   ? 20.478  16.87   55.604 1    49.561  ? 982  HOH A O   1 1 
HETATM 5088 O  O   . HOH H 7 .   ? 1.427   0.413   3.917  1    51.806  ? 983  HOH A O   1 1 
HETATM 5089 O  O   . HOH H 7 .   ? 5.004   -12.749 40.225 1    45.415  ? 984  HOH A O   1 1 
HETATM 5090 O  O   . HOH H 7 .   ? 9.173   15.096  58.771 1    47.837  ? 985  HOH A O   1 1 
HETATM 5091 O  O   . HOH H 7 .   ? 4.206   21.643  53.139 1    27.654  ? 986  HOH A O   1 1 
HETATM 5092 O  O   . HOH H 7 .   ? -8.508  13.594  33.545 1    35.232  ? 987  HOH A O   1 1 
HETATM 5093 O  O   . HOH H 7 .   ? 22.756  23.887  25.017 1    39.54   ? 988  HOH A O   1 1 
HETATM 5094 O  O   . HOH H 7 .   ? 5.46    -4.007  22.726 1    22.949  ? 989  HOH A O   1 1 
HETATM 5095 O  O   . HOH H 7 .   ? 8.098   27.627  52.517 1    34.421  ? 990  HOH A O   1 1 
HETATM 5096 O  O   . HOH H 7 .   ? 6.323   -7.288  -4.915 1    53.467  ? 991  HOH A O   1 1 
HETATM 5097 O  O   . HOH H 7 .   ? 5.963   31.977  39.316 1    29.889  ? 992  HOH A O   1 1 
HETATM 5098 O  O   . HOH H 7 .   ? 16.492  9.402   0.349  1    48.734  ? 993  HOH A O   1 1 
HETATM 5099 O  O   . HOH H 7 .   ? 7.578   29.977  41.893 1    30.14   ? 994  HOH A O   1 1 
HETATM 5100 O  O   . HOH H 7 .   ? 8.887   19.312  57.527 1    38.428  ? 995  HOH A O   1 1 
HETATM 5101 O  O   . HOH H 7 .   ? 25.01   13.973  53.427 1    34.444  ? 996  HOH A O   1 1 
HETATM 5102 O  O   . HOH H 7 .   ? 16.493  -26.313 10.992 1    47.581  ? 997  HOH A O   1 1 
HETATM 5103 O  O   . HOH H 7 .   ? 2.301   -12.495 32.473 1    33.75   ? 998  HOH A O   1 1 
HETATM 5104 O  O   . HOH H 7 .   ? 3.977   -9.781  4.397  1    40.688  ? 999  HOH A O   1 1 
HETATM 5105 O  O   . HOH H 7 .   ? -1.07   6.007   44.538 1    34.968  ? 1000 HOH A O   1 1 
HETATM 5106 O  O   . HOH H 7 .   ? 42.622  -2.4    22.563 1    46.214  ? 1001 HOH A O   1 1 
HETATM 5107 O  O   . HOH H 7 .   ? -7.69   16.771  37.605 1    30.072  ? 1002 HOH A O   1 1 
HETATM 5108 O  O   . HOH H 7 .   ? 23.008  24.189  20.359 1    46.063  ? 1003 HOH A O   1 1 
HETATM 5109 O  O   . HOH H 7 .   ? 11.972  -6.88   9.612  1    45.695  ? 1004 HOH A O   1 1 
HETATM 5110 O  O   . HOH H 7 .   ? 13.605  -14.232 3.847  1    42.101  ? 1005 HOH A O   1 1 
HETATM 5111 O  O   . HOH H 7 .   ? 15.281  10.457  24.808 1    35.238  ? 1006 HOH A O   1 1 
HETATM 5112 O  O   . HOH H 7 .   ? 14.191  13.846  20.025 1    41.231  ? 1007 HOH A O   1 1 
HETATM 5113 O  O   . HOH H 7 .   ? -11.351 -1.409  18.697 1    27.893  ? 1008 HOH A O   1 1 
HETATM 5114 O  O   . HOH H 7 .   ? 13.168  1.791   51.697 1    29.253  ? 1009 HOH A O   1 1 
HETATM 5115 O  O   . HOH H 7 .   ? 1.67    -1.159  15.046 1    39.249  ? 1010 HOH A O   1 1 
HETATM 5116 O  O   . HOH H 7 .   ? 28.476  -0.157  43.701 1    49.868  ? 1011 HOH A O   1 1 
HETATM 5117 O  O   . HOH H 7 .   ? 10.899  -21.727 14.191 1    40.965  ? 1012 HOH A O   1 1 
HETATM 5118 O  O   . HOH H 7 .   ? 2.943   -2.302  4.385  1    55.515  ? 1013 HOH A O   1 1 
HETATM 5119 O  O   . HOH H 7 .   ? -6.278  7.698   41.096 1    44.103  ? 1014 HOH A O   1 1 
HETATM 5120 O  O   . HOH H 7 .   ? 27.249  3.378   50.668 1    46.428  ? 1015 HOH A O   1 1 
HETATM 5121 O  O   . HOH H 7 .   ? 12.965  17.66   58.309 1    35.373  ? 1016 HOH A O   1 1 
HETATM 5122 O  O   . HOH H 7 .   ? 0.54    9.132   -4.728 1    61.084  ? 1017 HOH A O   1 1 
HETATM 5123 O  O   . HOH H 7 .   ? -2.905  -0.589  34.82  1    31.142  ? 1018 HOH A O   1 1 
HETATM 5124 O  O   . HOH H 7 .   ? 13.46   31.473  36.501 1    31.386  ? 1019 HOH A O   1 1 
HETATM 5125 O  O   . HOH H 7 .   ? 18.619  -10.018 -2.74  1    46.7    ? 1020 HOH A O   1 1 
HETATM 5126 O  O   . HOH H 7 .   ? 27.193  13.034  33.629 1    35.064  ? 1021 HOH A O   1 1 
HETATM 5127 O  O   . HOH H 7 .   ? 16.468  18.607  53.445 1    31.35   ? 1022 HOH A O   1 1 
HETATM 5128 O  O   . HOH H 7 .   ? 20.743  -2.311  46.182 1    44.164  ? 1023 HOH A O   1 1 
HETATM 5129 O  O   . HOH H 7 .   ? 19.358  -7.308  43.751 1    38.559  ? 1024 HOH A O   1 1 
HETATM 5130 O  O   . HOH H 7 .   ? -5.903  10.213  39.706 1    38.528  ? 1025 HOH A O   1 1 
HETATM 5131 O  O   . HOH H 7 .   ? 28.478  -2.094  7.823  1    40.249  ? 1026 HOH A O   1 1 
HETATM 5132 O  O   . HOH H 7 .   ? 16.577  7.567   -0.624 1    54.09   ? 1027 HOH A O   1 1 
HETATM 5133 O  O   . HOH H 7 .   ? -14.318 13.442  29.91  1    44.248  ? 1028 HOH A O   1 1 
HETATM 5134 O  O   . HOH H 7 .   ? 6.919   14.282  56.465 1    32.687  ? 1029 HOH A O   1 1 
HETATM 5135 O  O   . HOH H 7 .   ? 10.564  -6.916  44.897 1    40.024  ? 1030 HOH A O   1 1 
HETATM 5136 O  O   . HOH H 7 .   ? 12.678  -2.278  17.469 1    29.363  ? 1031 HOH A O   1 1 
HETATM 5137 O  O   . HOH H 7 .   ? 22.449  -4.323  45.686 1    42.52   ? 1032 HOH A O   1 1 
HETATM 5138 O  O   . HOH H 7 .   ? 24.873  -4.631  45.843 1    46.108  ? 1033 HOH A O   1 1 
HETATM 5139 O  O   . HOH H 7 .   ? 44.256  0.739   19.361 1    39.514  ? 1034 HOH A O   1 1 
HETATM 5140 O  O   . HOH H 7 .   ? -2.865  5.342   43.39  1    38.209  ? 1035 HOH A O   1 1 
HETATM 5141 O  O   . HOH H 7 .   ? -4.702  12.53   39.855 1    42.163  ? 1036 HOH A O   1 1 
HETATM 5142 O  O   . HOH H 7 .   ? 25.786  -14.978 14.134 1    43.61   ? 1037 HOH A O   1 1 
HETATM 5143 O  O   . HOH H 7 .   ? 12.468  -4.852  46.875 1    30.912  ? 1038 HOH A O   1 1 
HETATM 5144 O  O   . HOH H 7 .   ? 30.148  25.46   49.395 1    43.101  ? 1039 HOH A O   1 1 
HETATM 5145 O  O   . HOH H 7 .   ? 11.214  1.184   50.392 1    43.792  ? 1040 HOH A O   1 1 
HETATM 5146 O  O   . HOH H 7 .   ? -8.077  12.871  36.365 1    40.791  ? 1041 HOH A O   1 1 
HETATM 5147 O  O   . HOH H 7 .   ? 29.779  -5.066  38.932 1    42.32   ? 1042 HOH A O   1 1 
HETATM 5148 O  O   . HOH H 7 .   ? 7.159   -8.398  43.083 1    39.452  ? 1043 HOH A O   1 1 
HETATM 5149 O  O   . HOH H 7 .   ? 12.099  -15.342 29.358 1    26.863  ? 1044 HOH A O   1 1 
HETATM 5150 O  O   . HOH H 7 .   ? 18.062  -17.49  4.659  1    40.899  ? 1045 HOH A O   1 1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ASP A 4   ? 0.963118 0.952384 0.916054 -0.0440176  0.0291646   -0.317456   40   ASP A N   
2    C  CA  . ASP A 4   ? 0.964476 0.956537 0.913781 -0.0350921  0.0337718   -0.322338   40   ASP A CA  
3    C  C   . ASP A 4   ? 0.899302 0.896187 0.845499 -0.0288779  0.0356536   -0.304863   40   ASP A C   
4    O  O   . ASP A 4   ? 0.87071  0.881915 0.809676 -0.0309686  0.0330377   -0.292726   40   ASP A O   
5    C  CB  . ASP A 4   ? 1.00327  1.01599  0.942325 -0.0354772  0.0333063   -0.337917   40   ASP A CB  
6    C  CG  . ASP A 4   ? 1.0385   1.05219  0.976624 -0.0277073  0.0386877   -0.349694   40   ASP A CG  
7    O  OD1 . ASP A 4   ? 1.06598  1.08083  1.00411  -0.0205691  0.0424117   -0.340747   40   ASP A OD1 
8    O  OD2 . ASP A 4   ? 0.97399  0.988275 0.91208  -0.0288191  0.0391165   -0.36861    40   ASP A OD2 
9    N  N   . GLU A 5   ? 0.930977 0.915867 0.883103 -0.0208664  0.039984    -0.30472    41   GLU A N   
10   C  CA  . GLU A 5   ? 0.852544 0.842247 0.803836 -0.0138825  0.0424531   -0.2919     41   GLU A CA  
11   C  C   . GLU A 5   ? 0.796775 0.813542 0.736088 -0.0126485  0.0441373   -0.293453   41   GLU A C   
12   O  O   . GLU A 5   ? 0.728246 0.756029 0.662362 -0.0122568  0.0441082   -0.279733   41   GLU A O   
13   C  CB  . GLU A 5   ? 0.905463 0.878822 0.866248 -0.00466296 0.0461737   -0.295327   41   GLU A CB  
14   C  CG  . GLU A 5   ? 0.984375 0.929543 0.954738 -0.00400371 0.0449853   -0.287306   41   GLU A CG  
15   C  CD  . GLU A 5   ? 1.06765  1.01042  1.03846  -0.00352406 0.0434743   -0.267193   41   GLU A CD  
16   O  OE1 . GLU A 5   ? 1.05592  1.00339  1.02802  0.00404507  0.0451153   -0.260511   41   GLU A OE1 
17   O  OE2 . GLU A 5   ? 0.990047 0.927084 0.96059  -0.0107134  0.0407132   -0.258712   41   GLU A OE2 
18   N  N   . ALA A 6   ? 0.766225 0.793085 0.700546 -0.0123483  0.0459306   -0.310277   42   ALA A N   
19   C  CA  . ALA A 6   ? 0.72     0.772177 0.640849 -0.0118971  0.0481848   -0.312003   42   ALA A CA  
20   C  C   . ALA A 6   ? 0.690094 0.756869 0.59812  -0.0187381  0.0434409   -0.302328   42   ALA A C   
21   O  O   . ALA A 6   ? 0.645041 0.728247 0.542177 -0.0182037  0.0451482   -0.294208   42   ALA A O   
22   C  CB  . ALA A 6   ? 0.743919 0.803222 0.66156  -0.0102297  0.0510879   -0.332624   42   ALA A CB  
23   N  N   . GLU A 7   ? 0.669935 0.731316 0.579097 -0.0251027  0.037561    -0.303309   43   GLU A N   
24   C  CA  . GLU A 7   ? 0.650026 0.726515 0.547136 -0.0302458  0.0322975   -0.29549    43   GLU A CA  
25   C  C   . GLU A 7   ? 0.651981 0.726477 0.549941 -0.0299639  0.0311121   -0.27466    43   GLU A C   
26   O  O   . GLU A 7   ? 0.612881 0.701641 0.498565 -0.0312083  0.0290964   -0.265036   43   GLU A O   
27   C  CB  . GLU A 7   ? 0.736814 0.812939 0.634935 -0.037006   0.0257451   -0.303227   43   GLU A CB  
28   C  CG  . GLU A 7   ? 0.871187 0.966413 0.754956 -0.0388024  0.0236169   -0.316847   43   GLU A CG  
29   C  CD  . GLU A 7   ? 0.982275 1.08678  0.861442 -0.0450012  0.0151482   -0.319013   43   GLU A CD  
30   O  OE1 . GLU A 7   ? 0.88101  0.991296 0.758075 -0.0478218  0.0126412   -0.336318   43   GLU A OE1 
31   O  OE2 . GLU A 7   ? 0.987246 1.09405  0.865376 -0.0467436  0.0107141   -0.304165   43   GLU A OE2 
32   N  N   . ALA A 8   ? 0.598127 0.653993 0.509838 -0.0280779  0.0323611   -0.26783    44   ALA A N   
33   C  CA  . ALA A 8   ? 0.579601 0.632226 0.493309 -0.0277562  0.0311937   -0.249151   44   ALA A CA  
34   C  C   . ALA A 8   ? 0.54281  0.604364 0.451891 -0.0225449  0.0360229   -0.241524   44   ALA A C   
35   O  O   . ALA A 8   ? 0.501168 0.570768 0.403855 -0.0233592  0.0350246   -0.228174   44   ALA A O   
36   C  CB  . ALA A 8   ? 0.54474  0.574914 0.472895 -0.0276337  0.0310331   -0.245371   44   ALA A CB  
37   N  N   . SER A 9   ? 0.559028 0.620378 0.471374 -0.017375   0.0414329   -0.251178   45   SER A N   
38   C  CA  . SER A 9   ? 0.563286 0.635372 0.473094 -0.0126917  0.0469707   -0.247336   45   SER A CA  
39   C  C   . SER A 9   ? 0.628019 0.721853 0.520228 -0.0159725  0.0478888   -0.244998   45   SER A C   
40   O  O   . SER A 9   ? 0.574695 0.67602  0.461757 -0.0163809  0.0492419   -0.231763   45   SER A O   
41   C  CB  . SER A 9   ? 0.589718 0.658659 0.506695 -0.00694389 0.0517896   -0.262633   45   SER A CB  
42   O  OG  . SER A 9   ? 0.638166 0.713168 0.559262 -0.0012711  0.0570071   -0.258905   45   SER A OG  
43   N  N   . LYS A 10  ? 0.541393 0.644506 0.423594 -0.0184921  0.0470471   -0.257926   46   LYS A N   
44   C  CA  . LYS A 10  ? 0.566758 0.68866  0.429434 -0.0218954  0.0467065   -0.256349   46   LYS A CA  
45   C  C   . LYS A 10  ? 0.519901 0.643057 0.375184 -0.0257387  0.0408626   -0.239534   46   LYS A C   
46   O  O   . LYS A 10  ? 0.499282 0.632572 0.342675 -0.0265856  0.0427279   -0.228932   46   LYS A O   
47   C  CB  . LYS A 10  ? 0.617092 0.746728 0.470307 -0.0243098  0.0443141   -0.272475   46   LYS A CB  
48   C  CG  . LYS A 10  ? 0.685259 0.835286 0.516329 -0.026143   0.045977    -0.274618   46   LYS A CG  
49   C  CD  . LYS A 10  ? 0.723235 0.880569 0.541246 -0.0302348  0.0383071   -0.280369   46   LYS A CD  
50   C  CE  . LYS A 10  ? 0.754687 0.911029 0.576499 -0.0307546  0.036623    -0.300574   46   LYS A CE  
51   N  NZ  . LYS A 10  ? 0.828829 0.98625  0.647317 -0.0350233  0.0269723   -0.301943   46   LYS A NZ  
52   N  N   . PHE A 11  ? 0.476962 0.589304 0.33983  -0.0281447  0.0341271   -0.237117   47   PHE A N   
53   C  CA  . PHE A 11  ? 0.446624 0.559954 0.304564 -0.0309965  0.0282129   -0.222568   47   PHE A CA  
54   C  C   . PHE A 11  ? 0.437015 0.546743 0.29841  -0.0290153  0.0313585   -0.206431   47   PHE A C   
55   O  O   . PHE A 11  ? 0.429078 0.54548  0.279857 -0.0303375  0.0299075   -0.194189   47   PHE A O   
56   C  CB  . PHE A 11  ? 0.444074 0.547209 0.312549 -0.0339422  0.0217445   -0.225713   47   PHE A CB  
57   C  CG  . PHE A 11  ? 0.459471 0.559372 0.329754 -0.0355426  0.016768    -0.209792   47   PHE A CG  
58   C  CD1 . PHE A 11  ? 0.444839 0.531707 0.327431 -0.0339981  0.0186414   -0.19923    47   PHE A CD1 
59   C  CD2 . PHE A 11  ? 0.451627 0.562194 0.310426 -0.037909   0.00997519  -0.205638   47   PHE A CD2 
60   C  CE1 . PHE A 11  ? 0.460045 0.544725 0.344027 -0.0353168  0.0143179   -0.185495   47   PHE A CE1 
61   C  CE2 . PHE A 11  ? 0.44664  0.554377 0.30788  -0.0386542  0.00534893  -0.191846   47   PHE A CE2 
62   C  CZ  . PHE A 11  ? 0.436357 0.531227 0.310526 -0.0376531  0.00769815  -0.18219    47   PHE A CZ  
63   N  N   . VAL A 12  ? 0.432694 0.531731 0.30849  -0.0255364  0.0356052   -0.206226   48   VAL A N   
64   C  CA  . VAL A 12  ? 0.432797 0.528683 0.312509 -0.024189   0.0370753   -0.190944   48   VAL A CA  
65   C  C   . VAL A 12  ? 0.420315 0.530312 0.289628 -0.0235872  0.0431667   -0.187627   48   VAL A C   
66   O  O   . VAL A 12  ? 0.41065  0.523515 0.275216 -0.0249077  0.0433262   -0.174204   48   VAL A O   
67   C  CB  . VAL A 12  ? 0.457958 0.537869 0.355566 -0.0202892  0.0386792   -0.191315   48   VAL A CB  
68   C  CG1 . VAL A 12  ? 0.458318 0.539174 0.360966 -0.0167453  0.0430971   -0.18255    48   VAL A CG1 
69   C  CG2 . VAL A 12  ? 0.447303 0.513055 0.35299  -0.0224071  0.0330717   -0.185681   48   VAL A CG2 
70   N  N   . GLU A 13  ? 0.452667 0.57182  0.317665 -0.0222475  0.0483467   -0.200244   49   GLU A N   
71   C  CA  . GLU A 13  ? 0.486038 0.620947 0.338788 -0.0229929  0.0550205   -0.199467   49   GLU A CA  
72   C  C   . GLU A 13  ? 0.492159 0.636211 0.324008 -0.0277217  0.0521547   -0.190838   49   GLU A C   
73   O  O   . GLU A 13  ? 0.491388 0.641206 0.315429 -0.0295293  0.0557388   -0.179833   49   GLU A O   
74   C  CB  . GLU A 13  ? 0.522184 0.665974 0.372878 -0.0209907  0.0605214   -0.216877   49   GLU A CB  
75   C  CG  . GLU A 13  ? 0.604505 0.741525 0.474403 -0.0150728  0.0647832   -0.22457    49   GLU A CG  
76   C  CD  . GLU A 13  ? 0.70615  0.845848 0.579266 -0.0116863  0.0681525   -0.244231   49   GLU A CD  
77   O  OE1 . GLU A 13  ? 0.678729 0.824748 0.540607 -0.0139733  0.0670896   -0.254803   49   GLU A OE1 
78   O  OE2 . GLU A 13  ? 0.748678 0.88378  0.636895 -0.0058867  0.0717837   -0.24955    49   GLU A OE2 
79   N  N   . GLU A 14  ? 0.468588 0.613596 0.291345 -0.0296731  0.0454575   -0.195673   50   GLU A N   
80   C  CA  . GLU A 14  ? 0.475768 0.627879 0.278665 -0.0328965  0.0408136   -0.187257   50   GLU A CA  
81   C  C   . GLU A 14  ? 0.479442 0.623729 0.284206 -0.0338517  0.035968    -0.169515   50   GLU A C   
82   O  O   . GLU A 14  ? 0.442327 0.590906 0.232702 -0.0356816  0.0365722   -0.157498   50   GLU A O   
83   C  CB  . GLU A 14  ? 0.486805 0.640306 0.28513  -0.0338342  0.0329973   -0.197183   50   GLU A CB  
84   C  CG  . GLU A 14  ? 0.528634 0.693373 0.317015 -0.0336946  0.0370271   -0.213214   50   GLU A CG  
85   C  CD  . GLU A 14  ? 0.55938  0.726097 0.344701 -0.0348326  0.0291121   -0.224737   50   GLU A CD  
86   O  OE1 . GLU A 14  ? 0.566083 0.729102 0.352934 -0.0361179  0.0203767   -0.21974    50   GLU A OE1 
87   O  OE2 . GLU A 14  ? 0.60889  0.782519 0.390392 -0.0343521  0.0324836   -0.240236   50   GLU A OE2 
88   N  N   . TYR A 15  ? 0.448618 0.580337 0.27142  -0.0326321  0.0318931   -0.16779    51   TYR A N   
89   C  CA  . TYR A 15  ? 0.428192 0.552612 0.254414 -0.0331517  0.0277164   -0.15251    51   TYR A CA  
90   C  C   . TYR A 15  ? 0.43894  0.564792 0.263856 -0.0331332  0.0345476   -0.142264   51   TYR A C   
91   O  O   . TYR A 15  ? 0.433188 0.559304 0.249016 -0.034765   0.0330341   -0.129261   51   TYR A O   
92   C  CB  . TYR A 15  ? 0.442108 0.553496 0.287606 -0.0321187  0.0239475   -0.15381    51   TYR A CB  
93   C  CG  . TYR A 15  ? 0.398529 0.502582 0.248996 -0.0322497  0.0207846   -0.138633   51   TYR A CG  
94   C  CD1 . TYR A 15  ? 0.419497 0.524057 0.264611 -0.0336032  0.0130028   -0.132431   51   TYR A CD1 
95   C  CD2 . TYR A 15  ? 0.404973 0.503081 0.264855 -0.030668   0.0253751   -0.131057   51   TYR A CD2 
96   C  CE1 . TYR A 15  ? 0.389434 0.487616 0.238946 -0.0333658  0.0102534   -0.119114   51   TYR A CE1 
97   C  CE2 . TYR A 15  ? 0.391687 0.483335 0.255775 -0.0308098  0.0225767   -0.117819   51   TYR A CE2 
98   C  CZ  . TYR A 15  ? 0.405158 0.49639  0.264224 -0.0321845  0.0151423   -0.112178   51   TYR A CZ  
99   O  OH  . TYR A 15  ? 0.39857  0.483868 0.261469 -0.0320128  0.012453    -0.0999232  51   TYR A OH  
100  N  N   . ASP A 16  ? 0.440623 0.567823 0.274749 -0.0312675  0.0420774   -0.148732   52   ASP A N   
101  C  CA  . ASP A 16  ? 0.477021 0.605427 0.315008 -0.0313093  0.0482422   -0.139821   52   ASP A CA  
102  C  C   . ASP A 16  ? 0.476994 0.616738 0.295363 -0.0350815  0.0528791   -0.133973   52   ASP A C   
103  O  O   . ASP A 16  ? 0.43052  0.568601 0.245747 -0.0372914  0.0539811   -0.120856   52   ASP A O   
104  C  CB  . ASP A 16  ? 0.472732 0.601181 0.326505 -0.0275823  0.0544649   -0.149111   52   ASP A CB  
105  C  CG  . ASP A 16  ? 0.581022 0.709652 0.443882 -0.0270425  0.0590967   -0.140445   52   ASP A CG  
106  O  OD1 . ASP A 16  ? 0.60074  0.719689 0.469682 -0.0271074  0.0545551   -0.129587   52   ASP A OD1 
107  O  OD2 . ASP A 16  ? 0.552601 0.692198 0.416229 -0.0268836  0.0672255   -0.145046   52   ASP A OD2 
108  N  N   . ARG A 17  ? 0.465821 0.616203 0.270345 -0.0360645  0.0556083   -0.14387    53   ARG A N   
109  C  CA  . ARG A 17  ? 0.476086 0.637336 0.25905  -0.0399246  0.0607341   -0.139777   53   ARG A CA  
110  C  C   . ARG A 17  ? 0.471323 0.627997 0.238177 -0.0422439  0.0537336   -0.125646   53   ARG A C   
111  O  O   . ARG A 17  ? 0.454236 0.611513 0.210262 -0.0454984  0.0572743   -0.113757   53   ARG A O   
112  C  CB  . ARG A 17  ? 0.477827 0.649703 0.244701 -0.0403617  0.0614943   -0.152215   53   ARG A CB  
113  C  CG  . ARG A 17  ? 0.495217 0.67448  0.272896 -0.0381892  0.0695948   -0.167586   53   ARG A CG  
114  C  CD  . ARG A 17  ? 0.531742 0.71979  0.295773 -0.0382499  0.0692148   -0.180544   53   ARG A CD  
115  N  NE  . ARG A 17  ? 0.538503 0.728536 0.320543 -0.0344837  0.0748811   -0.195473   53   ARG A NE  
116  C  CZ  . ARG A 17  ? 0.55894  0.745051 0.348538 -0.0315734  0.0706585   -0.208996   53   ARG A CZ  
117  N  NH1 . ARG A 17  ? 0.580099 0.761636 0.363296 -0.0324625  0.0614763   -0.209856   53   ARG A NH1 
118  N  NH2 . ARG A 17  ? 0.624685 0.811905 0.428481 -0.0277281  0.0757117   -0.2226     53   ARG A NH2 
119  N  N   . THR A 18  ? 0.484952 0.638084 0.249163 -0.0406118  0.0440184   -0.128435   54   THR A N   
120  C  CA  . THR A 18  ? 0.504955 0.655312 0.253289 -0.0414082  0.0358248   -0.11742    54   THR A CA  
121  C  C   . THR A 18  ? 0.479458 0.618409 0.236849 -0.0413566  0.0328356   -0.10222    54   THR A C   
122  O  O   . THR A 18  ? 0.486759 0.623171 0.229997 -0.0429825  0.0315287   -0.0892362  54   THR A O   
123  C  CB  . THR A 18  ? 0.48518  0.637374 0.230975 -0.0394806  0.026177    -0.126686   54   THR A CB  
124  O  OG1 . THR A 18  ? 0.476241 0.620114 0.24586  -0.0375903  0.0228638   -0.131367   54   THR A OG1 
125  C  CG2 . THR A 18  ? 0.497654 0.661605 0.231425 -0.0397744  0.028471    -0.141542   54   THR A CG2 
126  N  N   . SER A 19  ? 0.438325 0.569365 0.218372 -0.0393641  0.0314288   -0.103599   55   SER A N   
127  C  CA  . SER A 19  ? 0.437724 0.558843 0.227379 -0.0392507  0.0296286   -0.0907561  55   SER A CA  
128  C  C   . SER A 19  ? 0.461344 0.583208 0.245317 -0.042243   0.0372455   -0.0807886  55   SER A C   
129  O  O   . SER A 19  ? 0.521507 0.636399 0.302448 -0.043265   0.0347816   -0.0677646  55   SER A O   
130  C  CB  . SER A 19  ? 0.407446 0.521056 0.221235 -0.0368604  0.0294002   -0.0948864  55   SER A CB  
131  O  OG  . SER A 19  ? 0.492868 0.604155 0.311343 -0.0353201  0.0220269   -0.102079   55   SER A OG  
132  N  N   . GLN A 20  ? 0.490185 0.619446 0.277518 -0.0434679  0.0466928   -0.0873869  56   GLN A N   
133  C  CA  . GLN A 20  ? 0.568818 0.699887 0.352773 -0.0473063  0.0545975   -0.0785509  56   GLN A CA  
134  C  C   . GLN A 20  ? 0.545436 0.675169 0.304967 -0.0509956  0.0534936   -0.0664409  56   GLN A C   
135  O  O   . GLN A 20  ? 0.507251 0.628983 0.265955 -0.052872   0.052704    -0.0537518  56   GLN A O   
136  C  CB  . GLN A 20  ? 0.581674 0.724548 0.369981 -0.0483748  0.0652733   -0.0889798  56   GLN A CB  
137  C  CG  . GLN A 20  ? 0.675445 0.816708 0.489242 -0.0446389  0.0670309   -0.0957956  56   GLN A CG  
138  C  CD  . GLN A 20  ? 0.755695 0.909889 0.574294 -0.0452489  0.0775455   -0.105498   56   GLN A CD  
139  O  OE1 . GLN A 20  ? 0.835052 0.996822 0.64581  -0.050186   0.085377    -0.100831   56   GLN A OE1 
140  N  NE2 . GLN A 20  ? 0.841767 0.998641 0.672701 -0.0404575  0.0780816   -0.11943    56   GLN A NE2 
141  N  N   . VAL A 21  ? 0.545729 0.68213  0.284923 -0.0515703  0.052641    -0.0704312  57   VAL A N   
142  C  CA  . VAL A 21  ? 0.57436  0.709738 0.286732 -0.0544919  0.0517958   -0.0598708  57   VAL A CA  
143  C  C   . VAL A 21  ? 0.596464 0.719262 0.305941 -0.052126   0.0408537   -0.0475851  57   VAL A C   
144  O  O   . VAL A 21  ? 0.637338 0.752294 0.337137 -0.0547632  0.041815    -0.0337675  57   VAL A O   
145  C  CB  . VAL A 21  ? 0.646624 0.792542 0.340331 -0.0538777  0.0510747   -0.069952   57   VAL A CB  
146  C  CG1 . VAL A 21  ? 0.647514 0.792154 0.309989 -0.0557594  0.0485536   -0.0595781  57   VAL A CG1 
147  C  CG2 . VAL A 21  ? 0.629481 0.788489 0.326485 -0.055748   0.0621768   -0.0833129  57   VAL A CG2 
148  N  N   . VAL A 22  ? 0.554146 0.674799 0.273113 -0.047311   0.0307543   -0.0529381  58   VAL A N   
149  C  CA  . VAL A 22  ? 0.545777 0.657491 0.261722 -0.04423    0.019627    -0.0437771  58   VAL A CA  
150  C  C   . VAL A 22  ? 0.56413  0.664665 0.295556 -0.0444801  0.0197865   -0.0336059  58   VAL A C   
151  O  O   . VAL A 22  ? 0.594645 0.686162 0.317939 -0.0438507  0.0148359   -0.0211976  58   VAL A O   
152  C  CB  . VAL A 22  ? 0.554004 0.669255 0.278563 -0.0399102  0.0101126   -0.0547445  58   VAL A CB  
153  C  CG1 . VAL A 22  ? 0.521843 0.629681 0.252056 -0.0362312  -0.00101536 -0.0482549  58   VAL A CG1 
154  C  CG2 . VAL A 22  ? 0.58517  0.710565 0.29046  -0.0393683  0.00747437  -0.0627109  58   VAL A CG2 
155  N  N   . TRP A 23  ? 0.543443 0.644065 0.297261 -0.0447761  0.0247752   -0.0392152  59   TRP A N   
156  C  CA  . TRP A 23  ? 0.492851 0.584212 0.261856 -0.0450785  0.0254326   -0.0310261  59   TRP A CA  
157  C  C   . TRP A 23  ? 0.44638  0.535324 0.206796 -0.0501189  0.0333893   -0.0209307  59   TRP A C   
158  O  O   . TRP A 23  ? 0.427011 0.506107 0.188553 -0.0508819  0.031507    -0.00987239 59   TRP A O   
159  C  CB  . TRP A 23  ? 0.514465 0.606554 0.308069 -0.0434262  0.0279444   -0.039878   59   TRP A CB  
160  C  CG  . TRP A 23  ? 0.601929 0.692625 0.406827 -0.0394511  0.0205311   -0.0477497  59   TRP A CG  
161  C  CD1 . TRP A 23  ? 0.631269 0.723955 0.427849 -0.0375821  0.0127477   -0.0508261  59   TRP A CD1 
162  C  CD2 . TRP A 23  ? 0.702433 0.789739 0.528727 -0.0372666  0.0205497   -0.0541339  59   TRP A CD2 
163  N  NE1 . TRP A 23  ? 0.665067 0.75602  0.47732  -0.0352623  0.00841486  -0.0585892  59   TRP A NE1 
164  C  CE2 . TRP A 23  ? 0.746681 0.833338 0.576321 -0.0350642  0.013253    -0.0603578  59   TRP A CE2 
165  C  CE3 . TRP A 23  ? 0.802583 0.887261 0.645141 -0.0368313  0.0257072   -0.055289   59   TRP A CE3 
166  C  CZ2 . TRP A 23  ? 0.776735 0.858844 0.624089 -0.0333042  0.0119949   -0.0669501  59   TRP A CZ2 
167  C  CZ3 . TRP A 23  ? 0.82581  0.905716 0.684689 -0.0340185  0.0236341   -0.0614849  59   TRP A CZ3 
168  C  CH2 . TRP A 23  ? 0.794486 0.872377 0.655281 -0.0326572  0.0173263   -0.0669458  59   TRP A CH2 
169  N  N   . ASN A 24  ? 0.488266 0.586234 0.239374 -0.0540013  0.0425584   -0.024905   60   ASN A N   
170  C  CA  . ASN A 24  ? 0.539728 0.635916 0.281217 -0.0600943  0.0509174   -0.0153427  60   ASN A CA  
171  C  C   . ASN A 24  ? 0.58677  0.672392 0.305819 -0.0608911  0.0455817   -0.00139792 60   ASN A C   
172  O  O   . ASN A 24  ? 0.550762 0.62584  0.268588 -0.0637436  0.0466649   0.0104546   60   ASN A O   
173  C  CB  . ASN A 24  ? 0.529386 0.638809 0.264089 -0.064433   0.0622899   -0.0228933  60   ASN A CB  
174  C  CG  . ASN A 24  ? 0.558612 0.667012 0.282971 -0.0720753  0.0720758   -0.0133265  60   ASN A CG  
175  O  OD1 . ASN A 24  ? 0.58989  0.700396 0.290329 -0.0759949  0.0762086   -0.0093459  60   ASN A OD1 
176  N  ND2 . ASN A 24  ? 0.507574 0.613426 0.249204 -0.0747868  0.0765142   -0.0101689  60   ASN A ND2 
177  N  N   . GLU A 25  ? 0.592743 0.680928 0.29433  -0.0578469  0.0391446   -0.00347706 61   GLU A N   
178  C  CA  . GLU A 25  ? 0.620647 0.699608 0.298368 -0.0570907  0.0328282   0.00878184  61   GLU A CA  
179  C  C   . GLU A 25  ? 0.58034  0.64581  0.267733 -0.0533158  0.0237717   0.017803    61   GLU A C   
180  O  O   . GLU A 25  ? 0.58858  0.641835 0.263413 -0.0546795  0.0226218   0.0312653   61   GLU A O   
181  C  CB  . GLU A 25  ? 0.654758 0.740123 0.314929 -0.0529382  0.025194    0.00338452  61   GLU A CB  
182  C  CG  . GLU A 25  ? 0.752739 0.85191  0.401571 -0.0563995  0.0340057   -0.00643232 61   GLU A CG  
183  C  CD  . GLU A 25  ? 0.808986 0.912594 0.429364 -0.0545823  0.0290077   -0.00685001 61   GLU A CD  
184  O  OE1 . GLU A 25  ? 0.843354 0.940858 0.453585 -0.0494625  0.0169856   -0.001157   61   GLU A OE1 
185  O  OE2 . GLU A 25  ? 0.883165 0.997009 0.490892 -0.0583098  0.0375834   -0.0129141  61   GLU A OE2 
186  N  N   . TYR A 26  ? 0.535409 0.602811 0.244658 -0.0486973  0.0177613   0.00998669  62   TYR A N   
187  C  CA  . TYR A 26  ? 0.550494 0.607503 0.268717 -0.0442333  0.00825056  0.0163788   62   TYR A CA  
188  C  C   . TYR A 26  ? 0.564073 0.612334 0.29646  -0.0473955  0.0135199   0.0231809   62   TYR A C   
189  O  O   . TYR A 26  ? 0.547399 0.583578 0.278583 -0.0459802  0.00870975  0.0334343   62   TYR A O   
190  C  CB  . TYR A 26  ? 0.56575  0.628248 0.301469 -0.0390203  0.00062242  0.00557429  62   TYR A CB  
191  C  CG  . TYR A 26  ? 0.557707 0.61108  0.309228 -0.0355632  -0.00602383 0.0104306   62   TYR A CG  
192  C  CD1 . TYR A 26  ? 0.565372 0.614957 0.336967 -0.0371686  -0.00135712 0.0103408   62   TYR A CD1 
193  C  CD2 . TYR A 26  ? 0.578411 0.6275   0.324077 -0.0303699  -0.0170632  0.0150337   62   TYR A CD2 
194  C  CE1 . TYR A 26  ? 0.594663 0.636376 0.379725 -0.0341446  -0.00694344 0.0143516   62   TYR A CE1 
195  C  CE2 . TYR A 26  ? 0.629831 0.671465 0.390035 -0.027119   -0.0225926  0.0188519   62   TYR A CE2 
196  C  CZ  . TYR A 26  ? 0.657441 0.695089 0.43663  -0.0292895  -0.0172111  0.01872     62   TYR A CZ  
197  O  OH  . TYR A 26  ? 0.757397 0.788308 0.549453 -0.025947   -0.022741   0.0219869   62   TYR A OH  
198  N  N   . ALA A 27  ? 0.594674 0.649355 0.341046 -0.0512128  0.0229227   0.0167897   63   ALA A N   
199  C  CA  . ALA A 27  ? 0.641068 0.689153 0.399571 -0.0548321  0.0283046   0.0227059   63   ALA A CA  
200  C  C   . ALA A 27  ? 0.636001 0.675025 0.375417 -0.0601772  0.0325105   0.0356866   63   ALA A C   
201  O  O   . ALA A 27  ? 0.638157 0.664838 0.380413 -0.0609284  0.0306503   0.0450817   63   ALA A O   
202  C  CB  . ALA A 27  ? 0.557505 0.615858 0.332978 -0.0574601  0.0372648   0.0130057   63   ALA A CB  
203  N  N   . GLY A 28  ? 0.665402 0.710055 0.384952 -0.0641493  0.0385844   0.03592     64   GLY A N   
204  C  CA  . GLY A 28  ? 0.68815  0.723558 0.385941 -0.0697679  0.0431868   0.0484529   64   GLY A CA  
205  C  C   . GLY A 28  ? 0.766284 0.784875 0.452916 -0.0654106  0.0325834   0.0606212   64   GLY A C   
206  O  O   . GLY A 28  ? 0.813224 0.818152 0.498151 -0.068688   0.0342527   0.071362    64   GLY A O   
207  N  N   . ALA A 29  ? 0.775522 0.795504 0.456037 -0.0577979  0.0214453   0.0580556   65   ALA A N   
208  C  CA  . ALA A 29  ? 0.719426 0.725674 0.386073 -0.0524547  0.0106157   0.0687107   65   ALA A CA  
209  C  C   . ALA A 29  ? 0.705584 0.700871 0.391569 -0.0502125  0.00645519  0.0729031   65   ALA A C   
210  O  O   . ALA A 29  ? 0.777194 0.756521 0.454776 -0.0504386  0.00434132  0.08488     65   ALA A O   
211  C  CB  . ALA A 29  ? 0.708462 0.72272  0.370054 -0.0446777  -0.00037755 0.0619      65   ALA A CB  
212  N  N   . ASN A 30  ? 0.746647 0.750373 0.458286 -0.0480519  0.00556278  0.0624654   66   ASN A N   
213  C  CA  . ASN A 30  ? 0.661458 0.658193 0.394011 -0.0459442  0.00241551  0.0635428   66   ASN A CA  
214  C  C   . ASN A 30  ? 0.633872 0.621667 0.370482 -0.0529408  0.0110854   0.0705619   66   ASN A C   
215  O  O   . ASN A 30  ? 0.680495 0.656257 0.423797 -0.0514137  0.00728403  0.0767492   66   ASN A O   
216  C  CB  . ASN A 30  ? 0.671873 0.680343 0.427386 -0.0429497  0.00096335  0.0505807   66   ASN A CB  
217  C  CG  . ASN A 30  ? 0.694742 0.696955 0.469625 -0.0392463  -0.00434342 0.051004    66   ASN A CG  
218  O  OD1 . ASN A 30  ? 0.719584 0.71055  0.490252 -0.0358512  -0.0110897  0.0590589   66   ASN A OD1 
219  N  ND2 . ASN A 30  ? 0.635753 0.644995 0.431261 -0.0392343  -0.00178716 0.0420833   66   ASN A ND2 
220  N  N   . TRP A 31  ? 0.675653 0.670005 0.409181 -0.0605764  0.0225876   0.0687876   67   TRP A N   
221  C  CA  . TRP A 31  ? 0.711311 0.699453 0.449218 -0.0684529  0.0317313   0.0742811   67   TRP A CA  
222  C  C   . TRP A 31  ? 0.742561 0.712358 0.459171 -0.0712453  0.0311469   0.0891646   67   TRP A C   
223  O  O   . TRP A 31  ? 0.801329 0.757954 0.52408  -0.0730913  0.0309085   0.0959339   67   TRP A O   
224  C  CB  . TRP A 31  ? 0.748819 0.750783 0.487197 -0.0758906  0.044331    0.067952    67   TRP A CB  
225  C  CG  . TRP A 31  ? 0.868218 0.865155 0.610483 -0.0850364  0.0542164   0.0733651   67   TRP A CG  
226  C  CD1 . TRP A 31  ? 0.917076 0.90665  0.640421 -0.0933073  0.0621414   0.0827683   67   TRP A CD1 
227  C  CD2 . TRP A 31  ? 0.767863 0.766355 0.534887 -0.0871281  0.0569696   0.0695911   67   TRP A CD2 
228  N  NE1 . TRP A 31  ? 0.860788 0.848218 0.596877 -0.101132   0.0702543   0.0842951   67   TRP A NE1 
229  C  CE2 . TRP A 31  ? 0.757494 0.750579 0.52046  -0.097121   0.0666703   0.0761798   67   TRP A CE2 
230  C  CE3 . TRP A 31  ? 0.696073 0.69985  0.487234 -0.0817617  0.0522658   0.0613721   67   TRP A CE3 
231  C  CZ2 . TRP A 31  ? 0.679855 0.674398 0.463686 -0.101566   0.0711545   0.0735875   67   TRP A CZ2 
232  C  CZ3 . TRP A 31  ? 0.621553 0.625857 0.43156  -0.0855006  0.0563186   0.0596464   67   TRP A CZ3 
233  C  CH2 . TRP A 31  ? 0.641653 0.642168 0.448581 -0.0952455  0.065458    0.0652042   67   TRP A CH2 
234  N  N   . ASN A 32  ? 0.752914 0.721541 0.44359  -0.0716995  0.0312259   0.0939968   68   ASN A N   
235  C  CA  . ASN A 32  ? 0.755888 0.706104 0.421082 -0.0736668  0.030283    0.108873    68   ASN A CA  
236  C  C   . ASN A 32  ? 0.830367 0.764737 0.496101 -0.06526    0.017365    0.11587     68   ASN A C   
237  O  O   . ASN A 32  ? 0.972615 0.887474 0.626356 -0.067197   0.0169868   0.128375    68   ASN A O   
238  C  CB  . ASN A 32  ? 0.726688 0.679873 0.364244 -0.0713866  0.0277674   0.11108     68   ASN A CB  
239  C  CG  . ASN A 32  ? 0.805955 0.773514 0.438217 -0.079816   0.0409853   0.105316    68   ASN A CG  
240  O  OD1 . ASN A 32  ? 0.838825 0.811175 0.486767 -0.0873231  0.0514195   0.101983    68   ASN A OD1 
241  N  ND2 . ASN A 32  ? 0.857648 0.833436 0.469422 -0.0784769  0.0406191   0.103062    68   ASN A ND2 
242  N  N   . TYR A 33  ? 0.764052 0.706467 0.444162 -0.0562262  0.00727071  0.10757     69   TYR A N   
243  C  CA  . TYR A 33  ? 0.773447 0.702705 0.456389 -0.048092   -0.00454301 0.113018    69   TYR A CA  
244  C  C   . TYR A 33  ? 0.876398 0.796855 0.579863 -0.0507458  -0.00192322 0.114315    69   TYR A C   
245  O  O   . TYR A 33  ? 0.836688 0.738943 0.536361 -0.0485179  -0.00664259 0.123662    69   TYR A O   
246  C  CB  . TYR A 33  ? 0.697733 0.638718 0.389512 -0.0383995  -0.0156202  0.103795    69   TYR A CB  
247  C  CG  . TYR A 33  ? 0.740585 0.67179  0.44339  -0.030331   -0.0264566  0.106323    69   TYR A CG  
248  C  CD1 . TYR A 33  ? 0.806018 0.721526 0.491314 -0.024463   -0.0352721  0.117198    69   TYR A CD1 
249  C  CD2 . TYR A 33  ? 0.778244 0.715984 0.508171 -0.0281091  -0.027979   0.0976584   69   TYR A CD2 
250  C  CE1 . TYR A 33  ? 0.843686 0.751381 0.539964 -0.0163322  -0.045303   0.118463    69   TYR A CE1 
251  C  CE2 . TYR A 33  ? 0.785799 0.716312 0.525913 -0.0207056  -0.0373839  0.0989297   69   TYR A CE2 
252  C  CZ  . TYR A 33  ? 0.889933 0.805719 0.613949 -0.0148109  -0.0458979  0.10905     69   TYR A CZ  
253  O  OH  . TYR A 33  ? 0.904384 0.813197 0.638588 -0.00687609 -0.0552461  0.109931    69   TYR A OH  
254  N  N   . ASN A 34  ? 0.875178 0.808804 0.599759 -0.0552279  0.00548319  0.10443     70   ASN A N   
255  C  CA  . ASN A 34  ? 0.785692 0.716527 0.533583 -0.0564218  0.00681447  0.101768    70   ASN A CA  
256  C  C   . ASN A 34  ? 0.746951 0.664586 0.491849 -0.0653735  0.0151556   0.110124    70   ASN A C   
257  O  O   . ASN A 34  ? 0.809829 0.720143 0.569837 -0.0659641  0.0145959   0.110522    70   ASN A O   
258  C  CB  . ASN A 34  ? 0.854345 0.803717 0.624145 -0.0565814  0.010212    0.0882903   70   ASN A CB  
259  C  CG  . ASN A 34  ? 0.711281 0.668493 0.490721 -0.0475962  0.00068339  0.0806053   70   ASN A CG  
260  O  OD1 . ASN A 34  ? 0.56327  0.519504 0.360439 -0.0439728  -0.00337185 0.077201    70   ASN A OD1 
261  N  ND2 . ASN A 34  ? 0.708687 0.673695 0.47607  -0.0443476  -0.00278018 0.0777085   70   ASN A ND2 
262  N  N   . THR A 35  ? 0.711906 0.627056 0.43744  -0.0727348  0.0232011   0.116168    71   THR A N   
263  C  CA  . THR A 35  ? 0.733543 0.638956 0.456126 -0.0834486  0.0335138   0.122856    71   THR A CA  
264  C  C   . THR A 35  ? 0.907637 0.793937 0.600163 -0.0853254  0.0331261   0.137334    71   THR A C   
265  O  O   . THR A 35  ? 0.890917 0.774513 0.569188 -0.0952381  0.0438736   0.142718    71   THR A O   
266  C  CB  . THR A 35  ? 0.727145 0.651595 0.455387 -0.09164    0.0457941   0.114632    71   THR A CB  
267  O  OG1 . THR A 35  ? 0.651827 0.583037 0.358124 -0.0924016  0.0485198   0.115555    71   THR A OG1 
268  C  CG2 . THR A 35  ? 0.676931 0.619258 0.432813 -0.0882886  0.0450393   0.10067     71   THR A CG2 
269  N  N   . ASN A 36  ? 0.914524 0.789042 0.596914 -0.0752491  0.0205231   0.14301     72   ASN A N   
270  C  CA  . ASN A 36  ? 0.857932 0.714245 0.509909 -0.0735621  0.0167724   0.15661     72   ASN A CA  
271  C  C   . ASN A 36  ? 0.817893 0.674966 0.465442 -0.0597655  0.00148623  0.155556    72   ASN A C   
272  O  O   . ASN A 36  ? 0.918811 0.78311  0.548321 -0.0566233  -0.00131326 0.155526    72   ASN A O   
273  C  CB  . ASN A 36  ? 0.965434 0.825719 0.593657 -0.0820131  0.0271016   0.160622    72   ASN A CB  
274  C  CG  . ASN A 36  ? 1.09649  0.933386 0.691447 -0.0828026  0.0257027   0.177163    72   ASN A CG  
275  O  OD1 . ASN A 36  ? 1.05756  0.873949 0.646419 -0.075969   0.0159226   0.186113    72   ASN A OD1 
276  N  ND2 . ASN A 36  ? 1.15183  0.990929 0.724153 -0.0908244  0.0354511   0.181522    72   ASN A ND2 
277  N  N   . ILE A 37  ? 0.785889 0.638694 0.451789 -0.051901   -0.00781283 0.152798    73   ILE A N   
278  C  CA  . ILE A 37  ? 0.795995 0.647401 0.458661 -0.0388955  -0.0225509  0.152752    73   ILE A CA  
279  C  C   . ILE A 37  ? 0.988701 0.818924 0.620321 -0.035959   -0.0275427  0.16775     73   ILE A C   
280  O  O   . ILE A 37  ? 1.05938  0.866965 0.683904 -0.0394158  -0.0252134  0.17863     73   ILE A O   
281  C  CB  . ILE A 37  ? 0.78974  0.636579 0.47624  -0.0327798  -0.0294286  0.149035    73   ILE A CB  
282  C  CG1 . ILE A 37  ? 0.842041 0.705999 0.556956 -0.0367262  -0.0234353  0.136243    73   ILE A CG1 
283  C  CG2 . ILE A 37  ? 0.782804 0.629921 0.468281 -0.0191777  -0.0445529  0.148004    73   ILE A CG2 
284  C  CD1 . ILE A 37  ? 0.779539 0.6437   0.517658 -0.02966    -0.0308136  0.130329    73   ILE A CD1 
285  N  N   . THR A 38  ? 1.02536  0.862741 0.637433 -0.0303153  -0.0337082  0.168216    74   THR A N   
286  C  CA  . THR A 38  ? 0.932733 0.752988 0.513638 -0.0246403  -0.0413591  0.18128     74   THR A CA  
287  C  C   . THR A 38  ? 0.953813 0.788176 0.531724 -0.0120614  -0.0554155  0.174826    74   THR A C   
288  O  O   . THR A 38  ? 0.932487 0.787464 0.533536 -0.00865695 -0.0584791  0.160926    74   THR A O   
289  C  CB  . THR A 38  ? 0.931243 0.743982 0.483299 -0.0349831  -0.0301493  0.190992    74   THR A CB  
290  O  OG1 . THR A 38  ? 0.928266 0.759734 0.466518 -0.0356578  -0.0284225  0.185413    74   THR A OG1 
291  C  CG2 . THR A 38  ? 0.870457 0.678813 0.430128 -0.0497165  -0.0137091  0.192648    74   THR A CG2 
292  N  N   . THR A 39  ? 1.02322  0.845996 0.572465 -0.00498186 -0.0644054  0.184964    75   THR A N   
293  C  CA  . THR A 39  ? 1.04987  0.887487 0.590633 0.00549983  -0.0767712  0.17928     75   THR A CA  
294  C  C   . THR A 39  ? 0.959303 0.819129 0.493906 -0.00094539 -0.0692115  0.170259    75   THR A C   
295  O  O   . THR A 39  ? 0.993702 0.876244 0.546298 0.00207747  -0.0725593  0.155731    75   THR A O   
296  C  CB  . THR A 39  ? 1.12009  0.937678 0.629067 0.0143704   -0.0878147  0.193742    75   THR A CB  
297  O  OG1 . THR A 39  ? 1.15273  0.954473 0.677152 0.0206483   -0.0944145  0.197403    75   THR A OG1 
298  C  CG2 . THR A 39  ? 1.09104  0.924121 0.591533 0.0264111   -0.102462   0.187724    75   THR A CG2 
299  N  N   . GLU A 40  ? 0.936909 0.78898  0.446675 -0.0103097  -0.0583486  0.178899    76   GLU A N   
300  C  CA  . GLU A 40  ? 1.00213  0.871342 0.5004   -0.0175966  -0.0491801  0.172784    76   GLU A CA  
301  C  C   . GLU A 40  ? 0.990554 0.882763 0.519634 -0.0235321  -0.0406227  0.156176    76   GLU A C   
302  O  O   . GLU A 40  ? 1.01235  0.925652 0.544682 -0.0216983  -0.0422891  0.144016    76   GLU A O   
303  C  CB  . GLU A 40  ? 1.16521  1.01776  0.635486 -0.0281449  -0.0368805  0.186644    76   GLU A CB  
304  C  CG  . GLU A 40  ? 1.3909   1.26106  0.850473 -0.0374918  -0.0244496  0.180192    76   GLU A CG  
305  C  CD  . GLU A 40  ? 1.66106  1.54342  1.09603  -0.0316108  -0.0314693  0.177059    76   GLU A CD  
306  O  OE1 . GLU A 40  ? 1.83345  1.71301  1.26095  -0.0191902  -0.0476289  0.178782    76   GLU A OE1 
307  O  OE2 . GLU A 40  ? 1.60745  1.50299  1.03086  -0.0392089  -0.0209837  0.172239    76   GLU A OE2 
308  N  N   . THR A 41  ? 0.958879 0.846642 0.5096   -0.0307665  -0.0313605  0.155522    77   THR A N   
309  C  CA  . THR A 41  ? 0.942886 0.850368 0.523209 -0.0352754  -0.0242073  0.140607    77   THR A CA  
310  C  C   . THR A 41  ? 0.904855 0.825987 0.507244 -0.0254277  -0.0358698  0.12863     77   THR A C   
311  O  O   . THR A 41  ? 0.812802 0.753962 0.427216 -0.0259604  -0.0340939  0.115314    77   THR A O   
312  C  CB  . THR A 41  ? 0.835479 0.736405 0.433964 -0.0445616  -0.0126879  0.141998    77   THR A CB  
313  O  OG1 . THR A 41  ? 0.754766 0.639782 0.363902 -0.0390162  -0.0206024  0.147611    77   THR A OG1 
314  C  CG2 . THR A 41  ? 0.859405 0.753953 0.439925 -0.0566585  0.00167905  0.149752    77   THR A CG2 
315  N  N   . SER A 42  ? 0.907681 0.817726 0.514303 -0.0164439  -0.0477198  0.13328     78   SER A N   
316  C  CA  . SER A 42  ? 0.887026 0.810031 0.514221 -0.00747548 -0.0585311  0.122295    78   SER A CA  
317  C  C   . SER A 42  ? 0.890665 0.829876 0.50634  -0.00202607 -0.0661641  0.114934    78   SER A C   
318  O  O   . SER A 42  ? 0.799966 0.757647 0.434333 -0.00073089 -0.0677138  0.101054    78   SER A O   
319  C  CB  . SER A 42  ? 0.809052 0.717496 0.443279 0.00076152  -0.0687058  0.128444    78   SER A CB  
320  O  OG  . SER A 42  ? 0.891657 0.814654 0.547809 0.00833726  -0.0776973  0.116791    78   SER A OG  
321  N  N   . LYS A 43  ? 0.913046 0.845304 0.497512 0.00078609  -0.0706953  0.123859    79   LYS A N   
322  C  CA  . LYS A 43  ? 0.991789 0.93966  0.563569 0.00612999  -0.0786266  0.11669     79   LYS A CA  
323  C  C   . LYS A 43  ? 1.02326  0.990591 0.602165 -0.00172449 -0.0682816  0.103766    79   LYS A C   
324  O  O   . LYS A 43  ? 1.13447  1.11975  0.728686 0.00136392  -0.0729326  0.0898984   79   LYS A O   
325  C  CB  . LYS A 43  ? 1.01402  0.953847 0.547516 0.00933731  -0.0836507  0.127277    79   LYS A CB  
326  C  CG  . LYS A 43  ? 1.10848  1.02372  0.622098 0.0162375   -0.0922919  0.144268    79   LYS A CG  
327  C  CD  . LYS A 43  ? 1.26027  1.16326  0.732363 0.0158762   -0.0923755  0.157474    79   LYS A CD  
328  C  CE  . LYS A 43  ? 1.29703  1.16952  0.74633  0.0138714   -0.0894638  0.177431    79   LYS A CE  
329  N  NZ  . LYS A 43  ? 1.28639  1.1405   0.73416  0.0255665   -0.103497   0.186674    79   LYS A NZ  
330  N  N   . ILE A 44  ? 0.957586 0.921032 0.524847 -0.0117771  -0.0543654  0.10823     80   ILE A N   
331  C  CA  . ILE A 44  ? 0.929949 0.910451 0.501476 -0.0192158  -0.0435167  0.0968417   80   ILE A CA  
332  C  C   . ILE A 44  ? 0.845651 0.83913  0.45237  -0.0199403  -0.0414467  0.0826944   80   ILE A C   
333  O  O   . ILE A 44  ? 0.753686 0.763961 0.366911 -0.0215067  -0.0387027  0.06975     80   ILE A O   
334  C  CB  . ILE A 44  ? 0.958973 0.932776 0.515549 -0.030144   -0.0281164  0.104324    80   ILE A CB  
335  C  CG1 . ILE A 44  ? 0.964219 0.924035 0.48288  -0.0300165  -0.029532   0.11899     80   ILE A CG1 
336  C  CG2 . ILE A 44  ? 0.852514 0.845229 0.415618 -0.0371061  -0.0167285  0.0912896   80   ILE A CG2 
337  C  CD1 . ILE A 44  ? 1.00431  0.954765 0.509643 -0.0417009  -0.013811   0.128035    80   ILE A CD1 
338  N  N   . LEU A 45  ? 0.820685 0.805474 0.448653 -0.0188566  -0.0425568  0.085292    81   LEU A N   
339  C  CA  . LEU A 45  ? 0.818956 0.813543 0.478608 -0.019244   -0.0408911  0.0735929   81   LEU A CA  
340  C  C   . LEU A 45  ? 0.875784 0.884424 0.544453 -0.0121638  -0.0515341  0.0620346   81   LEU A C   
341  O  O   . LEU A 45  ? 0.91285  0.93548  0.595049 -0.0145554  -0.0477366  0.0492925   81   LEU A O   
342  C  CB  . LEU A 45  ? 0.735947 0.719888 0.416541 -0.0198685  -0.0393348  0.0775005   81   LEU A CB  
343  C  CG  . LEU A 45  ? 0.644075 0.638194 0.355006 -0.020312   -0.0372974  0.0655546   81   LEU A CG  
344  C  CD1 . LEU A 45  ? 0.640039 0.645285 0.354451 -0.0272425  -0.0261735  0.0574183   81   LEU A CD1 
345  C  CD2 . LEU A 45  ? 0.635363 0.621173 0.367906 -0.0202681  -0.0365006  0.067558    81   LEU A CD2 
346  N  N   . LEU A 46  ? 0.844852 0.850108 0.507101 -0.00357333 -0.0646801  0.065743    82   LEU A N   
347  C  CA  . LEU A 46  ? 0.844424 0.864285 0.52204  0.00223688  -0.0740394  0.0533532   82   LEU A CA  
348  C  C   . LEU A 46  ? 0.774007 0.808609 0.437669 0.00198138  -0.0755304  0.0445399   82   LEU A C   
349  O  O   . LEU A 46  ? 0.78335  0.832615 0.461674 0.00153833  -0.0762084  0.0307529   82   LEU A O   
350  C  CB  . LEU A 46  ? 0.880748 0.899007 0.572137 0.010876    -0.0862384  0.0534195   82   LEU A CB  
351  C  CG  . LEU A 46  ? 1.01479  1.02487  0.729954 0.0102031   -0.083327   0.055248    82   LEU A CG  
352  C  CD1 . LEU A 46  ? 0.940466 0.956452 0.678476 0.017066    -0.0927075  0.0486855   82   LEU A CD1 
353  C  CD2 . LEU A 46  ? 0.904477 0.912705 0.633767 0.00128906  -0.0695279  0.0532483   82   LEU A CD2 
354  N  N   . GLN A 47  ? 0.845362 0.87542  0.480166 0.00068611  -0.0737827  0.052245    83   GLN A N   
355  C  CA  . GLN A 47  ? 0.9285   0.972066 0.548602 -0.00127958 -0.0721797  0.0438555   83   GLN A CA  
356  C  C   . GLN A 47  ? 0.951054 1.00477  0.587872 -0.00900823 -0.0599415  0.0320312   83   GLN A C   
357  O  O   . GLN A 47  ? 0.841391 0.910065 0.48456  -0.00887777 -0.0614264  0.0180969   83   GLN A O   
358  C  CB  . GLN A 47  ? 0.997273 1.03037  0.582241 -0.00150081 -0.0716162  0.0572463   83   GLN A CB  
359  C  CG  . GLN A 47  ? 1.04725  1.0928   0.609488 -0.00180215 -0.0723834  0.0509409   83   GLN A CG  
360  C  CD  . GLN A 47  ? 1.10339  1.15112  0.657253 -0.0115889  -0.0565638  0.0498094   83   GLN A CD  
361  O  OE1 . GLN A 47  ? 1.03077  1.08199  0.606818 -0.0174723  -0.0464266  0.0433275   83   GLN A OE1 
362  N  NE2 . GLN A 47  ? 1.16825  1.21314  0.689348 -0.0131491  -0.0543032  0.0569738   83   GLN A NE2 
363  N  N   . LYS A 48  ? 0.845124 0.890658 0.490384 -0.0154116  -0.0483077  0.0369312   84   LYS A N   
364  C  CA  . LYS A 48  ? 0.805509 0.859926 0.467653 -0.021551   -0.037368   0.0260966   84   LYS A CA  
365  C  C   . LYS A 48  ? 0.717835 0.778493 0.409509 -0.0191577  -0.0411584  0.0151504   84   LYS A C   
366  O  O   . LYS A 48  ? 0.645796 0.71567  0.350849 -0.0220685  -0.0356964  0.00331078  84   LYS A O   
367  C  CB  . LYS A 48  ? 0.703456 0.750291 0.368975 -0.0288327  -0.0241719  0.0323493   84   LYS A CB  
368  C  CG  . LYS A 48  ? 0.71779  0.760116 0.35747  -0.0340592  -0.0162146  0.0412081   84   LYS A CG  
369  C  CD  . LYS A 48  ? 0.716434 0.770768 0.336335 -0.0359289  -0.0129279  0.0344537   84   LYS A CD  
370  C  CE  . LYS A 48  ? 0.75217  0.800539 0.351473 -0.0430252  -0.0018269  0.0442015   84   LYS A CE  
371  N  NZ  . LYS A 48  ? 0.78086  0.838929 0.355288 -0.0432775  -0.00132702 0.0399734   84   LYS A NZ  
372  N  N   . ASN A 49  ? 0.70911  0.764438 0.410363 -0.013725   -0.0504731  0.0189481   85   ASN A N   
373  C  CA  . ASN A 49  ? 0.690368 0.750474 0.418958 -0.0121742  -0.0531527  0.00988956  85   ASN A CA  
374  C  C   . ASN A 49  ? 0.709177 0.784368 0.440574 -0.0105933  -0.0583146  -0.00424045 85   ASN A C   
375  O  O   . ASN A 49  ? 0.653737 0.735195 0.403072 -0.0133092  -0.0542528  -0.015198   85   ASN A O   
376  C  CB  . ASN A 49  ? 0.766925 0.820362 0.502618 -0.00604732 -0.0629108  0.0160942   85   ASN A CB  
377  C  CG  . ASN A 49  ? 0.856427 0.904826 0.616456 -0.00744883 -0.0591171  0.0156753   85   ASN A CG  
378  O  OD1 . ASN A 49  ? 0.944013 0.992395 0.713652 -0.0128334  -0.0493404  0.0124141   85   ASN A OD1 
379  N  ND2 . ASN A 49  ? 0.942495 0.986789 0.712122 -0.00228862 -0.0667757  0.0188528   85   ASN A ND2 
380  N  N   . MET A 50  ? 0.745438 0.825583 0.457393 -0.00639533 -0.0670117  -0.00365525 86   MET A N   
381  C  CA  . MET A 50  ? 0.76686  0.861993 0.478867 -0.00431179 -0.073894   -0.0168287  86   MET A CA  
382  C  C   . MET A 50  ? 0.68319  0.786324 0.390209 -0.00987144 -0.0650712  -0.0267548  86   MET A C   
383  O  O   . MET A 50  ? 0.630217 0.743967 0.349729 -0.0110067  -0.0658575  -0.0410187  86   MET A O   
384  C  CB  . MET A 50  ? 0.869629 0.968012 0.562188 0.00287212  -0.0870917  -0.0130513  86   MET A CB  
385  C  CG  . MET A 50  ? 1.07784  1.17604  0.783761 0.0100914   -0.0991387  -0.0113486  86   MET A CG  
386  S  SD  . MET A 50  ? 1.38444  1.48553  1.12815  0.00907059  -0.0984312  -0.0196417  86   MET A SD  
387  C  CE  . MET A 50  ? 1.21172  1.32201  0.968227 0.0176691   -0.114      -0.023869   86   MET A CE  
388  N  N   . GLN A 51  ? 0.68299  0.780942 0.371852 -0.0134861  -0.0564772  -0.0195379  87   GLN A N   
389  C  CA  . GLN A 51  ? 0.654411 0.759784 0.338614 -0.0186307  -0.0468147  -0.0285025  87   GLN A CA  
390  C  C   . GLN A 51  ? 0.621534 0.728328 0.332556 -0.0222398  -0.039162   -0.0382738  87   GLN A C   
391  O  O   . GLN A 51  ? 0.666292 0.782345 0.382752 -0.0239224  -0.0367845  -0.0519717  87   GLN A O   
392  C  CB  . GLN A 51  ? 0.663032 0.761873 0.327913 -0.0228076  -0.0369705  -0.0181726  87   GLN A CB  
393  C  CG  . GLN A 51  ? 0.713192 0.822501 0.366184 -0.0267513  -0.0290489  -0.0276408  87   GLN A CG  
394  C  CD  . GLN A 51  ? 0.79821  0.903144 0.438136 -0.0324943  -0.016372   -0.0197612  87   GLN A CD  
395  O  OE1 . GLN A 51  ? 0.79157  0.887254 0.440969 -0.0354689  -0.0098038  -0.0114185  87   GLN A OE1 
396  N  NE2 . GLN A 51  ? 0.79844  0.911782 0.417665 -0.0346777  -0.0120137  -0.0241605  87   GLN A NE2 
397  N  N   . ILE A 52  ? 0.54544  0.642467 0.272751 -0.0231831  -0.0355118  -0.0315689  88   ILE A N   
398  C  CA  . ILE A 52  ? 0.500972 0.598235 0.250805 -0.0260879  -0.0282994  -0.0397226  88   ILE A CA  
399  C  C   . ILE A 52  ? 0.464914 0.566361 0.233545 -0.0240248  -0.0351061  -0.0498107  88   ILE A C   
400  O  O   . ILE A 52  ? 0.428686 0.534132 0.21024  -0.0260084  -0.0315779  -0.0616154  88   ILE A O   
401  C  CB  . ILE A 52  ? 0.561652 0.648191 0.320793 -0.0281562  -0.021386   -0.0298626  88   ILE A CB  
402  C  CG1 . ILE A 52  ? 0.55881  0.646148 0.337172 -0.0307533  -0.0132543  -0.0381541  88   ILE A CG1 
403  C  CG2 . ILE A 52  ? 0.514699 0.592433 0.281485 -0.0249389  -0.0282555  -0.0205701  88   ILE A CG2 
404  C  CD1 . ILE A 52  ? 0.576973 0.65607  0.36436  -0.0327933  -0.00636494 -0.0301041  88   ILE A CD1 
405  N  N   . ALA A 53  ? 0.496049 0.597043 0.265544 -0.0199743  -0.0452153  -0.0458403  89   ALA A N   
406  C  CA  . ALA A 53  ? 0.503474 0.610657 0.289862 -0.0185717  -0.0518796  -0.055917   89   ALA A CA  
407  C  C   . ALA A 53  ? 0.520476 0.639877 0.301977 -0.0196187  -0.0539357  -0.0701249  89   ALA A C   
408  O  O   . ALA A 53  ? 0.542534 0.665244 0.340071 -0.022166   -0.0519422  -0.0819589  89   ALA A O   
409  C  CB  . ALA A 53  ? 0.496788 0.603512 0.284199 -0.0134536  -0.0625784  -0.0496788  89   ALA A CB  
410  N  N   . GLN A 54  ? 0.498925 0.623989 0.257372 -0.0180479  -0.0571582  -0.0690042  90   GLN A N   
411  C  CA  . GLN A 54  ? 0.548643 0.68585  0.301343 -0.0191233  -0.0589075  -0.0833071  90   GLN A CA  
412  C  C   . GLN A 54  ? 0.502386 0.639633 0.261514 -0.0239065  -0.0478746  -0.0927663  90   GLN A C   
413  O  O   . GLN A 54  ? 0.532525 0.677118 0.298796 -0.0255238  -0.0485959  -0.107285   90   GLN A O   
414  C  CB  . GLN A 54  ? 0.611183 0.754296 0.335031 -0.0174726  -0.0614912  -0.0812192  90   GLN A CB  
415  C  CG  . GLN A 54  ? 0.731527 0.878396 0.443136 -0.0115128  -0.0747233  -0.0758776  90   GLN A CG  
416  C  CD  . GLN A 54  ? 0.858017 1.00722  0.537706 -0.0101402  -0.0755451  -0.0707524  90   GLN A CD  
417  O  OE1 . GLN A 54  ? 0.833274 0.989863 0.502658 -0.0130998  -0.0705348  -0.0798145  90   GLN A OE1 
418  N  NE2 . GLN A 54  ? 0.85744  0.998545 0.521144 -0.00597556 -0.0805797  -0.0554399  90   GLN A NE2 
419  N  N   . HIS A 55  ? 0.460525 0.590132 0.216991 -0.0260201  -0.0379078  -0.0853717  91   HIS A N   
420  C  CA  . HIS A 55  ? 0.444094 0.574219 0.208086 -0.0293895  -0.0280205  -0.0947115  91   HIS A CA  
421  C  C   . HIS A 55  ? 0.417034 0.54154  0.207504 -0.0305314  -0.0262714  -0.100882   91   HIS A C   
422  O  O   . HIS A 55  ? 0.416159 0.542883 0.215662 -0.0323123  -0.0230203  -0.113919   91   HIS A O   
423  C  CB  . HIS A 55  ? 0.452185 0.577059 0.207613 -0.0310902  -0.0184501  -0.0847902  91   HIS A CB  
424  C  CG  . HIS A 55  ? 0.446187 0.569834 0.214315 -0.0334755  -0.00817497 -0.0920436  91   HIS A CG  
425  N  ND1 . HIS A 55  ? 0.45312  0.584463 0.212169 -0.0350263  -0.00175506 -0.10118    91   HIS A ND1 
426  C  CD2 . HIS A 55  ? 0.421375 0.537363 0.208992 -0.0339404  -0.00345344 -0.0912332  91   HIS A CD2 
427  C  CE1 . HIS A 55  ? 0.428148 0.556736 0.202133 -0.0359414  0.00628117  -0.10634    91   HIS A CE1 
428  N  NE2 . HIS A 55  ? 0.426213 0.545141 0.217057 -0.0352084  0.00513367  -0.0998786  91   HIS A NE2 
429  N  N   . THR A 56  ? 0.418461 0.534689 0.220317 -0.0295411  -0.027961   -0.0913526  92   THR A N   
430  C  CA  . THR A 56  ? 0.402381 0.512371 0.227271 -0.0305662  -0.0268166  -0.0952211  92   THR A CA  
431  C  C   . THR A 56  ? 0.426319 0.543088 0.259326 -0.0314758  -0.0327285  -0.108406   92   THR A C   
432  O  O   . THR A 56  ? 0.427475 0.542089 0.272251 -0.0339117  -0.028683   -0.118656   92   THR A O   
433  C  CB  . THR A 56  ? 0.42861  0.530381 0.26138  -0.0290122  -0.0288359  -0.0826924  92   THR A CB  
434  O  OG1 . THR A 56  ? 0.407854 0.504274 0.231951 -0.0289671  -0.0231553  -0.071793   92   THR A OG1 
435  C  CG2 . THR A 56  ? 0.398406 0.492152 0.252705 -0.0302668  -0.0258198  -0.0844813  92   THR A CG2 
436  N  N   . LEU A 57  ? 0.466843 0.592314 0.292265 -0.0295115  -0.0422439  -0.109093   93   LEU A N   
437  C  CA  . LEU A 57  ? 0.469703 0.604207 0.302857 -0.0306635  -0.0486527  -0.122364   93   LEU A CA  
438  C  C   . LEU A 57  ? 0.512181 0.65219  0.340892 -0.033237   -0.0452262  -0.136649   93   LEU A C   
439  O  O   . LEU A 57  ? 0.522621 0.662773 0.365407 -0.0364854  -0.0441494  -0.148985   93   LEU A O   
440  C  CB  . LEU A 57  ? 0.494916 0.639132 0.317241 -0.0266736  -0.060074   -0.119139   93   LEU A CB  
441  C  CG  . LEU A 57  ? 0.470458 0.62633  0.30343  -0.0273284  -0.0686297  -0.131934   93   LEU A CG  
442  C  CD1 . LEU A 57  ? 0.416851 0.566608 0.274686 -0.0299621  -0.0665809  -0.132499   93   LEU A CD1 
443  C  CD2 . LEU A 57  ? 0.472345 0.639874 0.292096 -0.0220036  -0.0810699  -0.129813   93   LEU A CD2 
444  N  N   . LYS A 58  ? 0.534233 0.678764 0.34252  -0.0320317  -0.0433424  -0.135527   94   LYS A N   
445  C  CA  . LYS A 58  ? 0.52482  0.675918 0.327909 -0.0340175  -0.0404893  -0.15003    94   LYS A CA  
446  C  C   . LYS A 58  ? 0.501873 0.643569 0.321352 -0.0368494  -0.031036   -0.156763   94   LYS A C   
447  O  O   . LYS A 58  ? 0.524846 0.668    0.354259 -0.0393923  -0.0311688  -0.17116    94   LYS A O   
448  C  CB  . LYS A 58  ? 0.51189  0.668995 0.289336 -0.0324398  -0.0385939  -0.146466   94   LYS A CB  
449  C  CG  . LYS A 58  ? 0.492736 0.657417 0.264592 -0.0342191  -0.0354082  -0.162188   94   LYS A CG  
450  C  CD  . LYS A 58  ? 0.574991 0.744909 0.321684 -0.0333157  -0.0311332  -0.158019   94   LYS A CD  
451  C  CE  . LYS A 58  ? 0.604985 0.788015 0.338773 -0.0332834  -0.0360854  -0.171929   94   LYS A CE  
452  N  NZ  . LYS A 58  ? 0.673204 0.855759 0.400288 -0.0347037  -0.024632   -0.174697   94   LYS A NZ  
453  N  N   . TYR A 59  ? 0.465454 0.597626 0.287061 -0.0362084  -0.0233433  -0.146672   95   TYR A N   
454  C  CA  . TYR A 59  ? 0.436374 0.559596 0.270764 -0.037352   -0.0144876  -0.151556   95   TYR A CA  
455  C  C   . TYR A 59  ? 0.437133 0.550902 0.292884 -0.0390968  -0.0156061  -0.154179   95   TYR A C   
456  O  O   . TYR A 59  ? 0.403697 0.512465 0.270087 -0.0409423  -0.0123392  -0.165483   95   TYR A O   
457  C  CB  . TYR A 59  ? 0.401437 0.519824 0.232576 -0.0360646  -0.00592042 -0.143078   95   TYR A CB  
458  C  CG  . TYR A 59  ? 0.418356 0.546873 0.231319 -0.0359431  -0.00237007 -0.148065   95   TYR A CG  
459  C  CD1 . TYR A 59  ? 0.421323 0.557799 0.213433 -0.035441   -0.00583287 -0.140697   95   TYR A CD1 
460  C  CD2 . TYR A 59  ? 0.423275 0.553663 0.238968 -0.0362513  0.00357043  -0.161664   95   TYR A CD2 
461  C  CE1 . TYR A 59  ? 0.436259 0.582542 0.209748 -0.0358015  -0.00261057 -0.145818   95   TYR A CE1 
462  C  CE2 . TYR A 59  ? 0.420081 0.561331 0.218815 -0.0363419  0.00672184  -0.167952   95   TYR A CE2 
463  C  CZ  . TYR A 59  ? 0.441967 0.591387 0.219147 -0.0364115  0.00399522  -0.159748   95   TYR A CZ  
464  O  OH  . TYR A 59  ? 0.463673 0.623881 0.222516 -0.0368654  0.00766079  -0.166072   95   TYR A OH  
465  N  N   . GLY A 60  ? 0.419577 0.531387 0.28041  -0.0386725  -0.0206391  -0.144541   96   GLY A N   
466  C  CA  . GLY A 60  ? 0.43077  0.534128 0.310519 -0.0407024  -0.0211362  -0.145167   96   GLY A CA  
467  C  C   . GLY A 60  ? 0.486096 0.592992 0.374963 -0.044467   -0.0243095  -0.160096   96   GLY A C   
468  O  O   . GLY A 60  ? 0.508223 0.604867 0.41145  -0.0473182  -0.0203012  -0.165292   96   GLY A O   
469  N  N   . THR A 61  ? 0.461073 0.581903 0.341397 -0.044531   -0.0316627  -0.166525   97   THR A N   
470  C  CA  . THR A 61  ? 0.502609 0.630687 0.389475 -0.048253   -0.0357882  -0.182246   97   THR A CA  
471  C  C   . THR A 61  ? 0.57369  0.69648  0.462354 -0.0505515  -0.0292841  -0.195254   97   THR A C   
472  O  O   . THR A 61  ? 0.550922 0.667293 0.454459 -0.0550226  -0.0275694  -0.205204   97   THR A O   
473  C  CB  . THR A 61  ? 0.48242  0.627968 0.356337 -0.046348   -0.0456537  -0.185524   97   THR A CB  
474  O  OG1 . THR A 61  ? 0.466718 0.613993 0.340735 -0.0433531  -0.0510227  -0.172613   97   THR A OG1 
475  C  CG2 . THR A 61  ? 0.462339 0.617966 0.343975 -0.0503151  -0.0510426  -0.202743   97   THR A CG2 
476  N  N   . GLN A 62  ? 0.516827 0.641862 0.390929 -0.0477755  -0.0253396  -0.195689   98   GLN A N   
477  C  CA  . GLN A 62  ? 0.521096 0.641258 0.397746 -0.0490691  -0.0191788  -0.2087     98   GLN A CA  
478  C  C   . GLN A 62  ? 0.491451 0.593348 0.384211 -0.049894   -0.0122183  -0.206496   98   GLN A C   
479  O  O   . GLN A 62  ? 0.514999 0.609334 0.417339 -0.0525887  -0.00954437 -0.218347   98   GLN A O   
480  C  CB  . GLN A 62  ? 0.551773 0.676338 0.413451 -0.0461131  -0.0140147  -0.211351   98   GLN A CB  
481  C  CG  . GLN A 62  ? 0.665119 0.804528 0.513057 -0.0466549  -0.0179775  -0.224322   98   GLN A CG  
482  C  CD  . GLN A 62  ? 0.783696 0.928422 0.615876 -0.0439857  -0.0118743  -0.226441   98   GLN A CD  
483  O  OE1 . GLN A 62  ? 0.964985 1.11426  0.794053 -0.0447097  -0.0100751  -0.24182    98   GLN A OE1 
484  N  NE2 . GLN A 62  ? 0.639907 0.785089 0.461771 -0.0412949  -0.00841459 -0.21213    98   GLN A NE2 
485  N  N   . ALA A 63  ? 0.455408 0.549669 0.350098 -0.0473562  -0.00934123 -0.191756   99   ALA A N   
486  C  CA  . ALA A 63  ? 0.49304  0.570001 0.400784 -0.0470955  -0.00313448 -0.188835   99   ALA A CA  
487  C  C   . ALA A 63  ? 0.500812 0.567879 0.424334 -0.0519119  -0.00422427 -0.193152   99   ALA A C   
488  O  O   . ALA A 63  ? 0.523491 0.575926 0.456174 -0.0528625  0.00067384  -0.198009   99   ALA A O   
489  C  CB  . ALA A 63  ? 0.436793 0.509594 0.342982 -0.0435784  -0.00088207 -0.172496   99   ALA A CB  
490  N  N   . ARG A 64  ? 0.495402 0.569949 0.422108 -0.0547788  -0.0103534  -0.190868   100  ARG A N   
491  C  CA  . ARG A 64  ? 0.492595 0.562804 0.433791 -0.0607062  -0.0118725  -0.196626   100  ARG A CA  
492  C  C   . ARG A 64  ? 0.548305 0.617635 0.494864 -0.0656167  -0.0113963  -0.214567   100  ARG A C   
493  O  O   . ARG A 64  ? 0.547763 0.607658 0.507684 -0.0713255  -0.00961766 -0.219809   100  ARG A O   
494  C  CB  . ARG A 64  ? 0.439554 0.524613 0.381133 -0.0618197  -0.0198244  -0.193551   100  ARG A CB  
495  C  CG  . ARG A 64  ? 0.456568 0.537098 0.398762 -0.0586599  -0.0192609  -0.176942   100  ARG A CG  
496  C  CD  . ARG A 64  ? 0.465923 0.559441 0.409712 -0.0585886  -0.0269234  -0.172926   100  ARG A CD  
497  N  NE  . ARG A 64  ? 0.415388 0.502272 0.359602 -0.0553065  -0.0253426  -0.15747    100  ARG A NE  
498  C  CZ  . ARG A 64  ? 0.486557 0.579545 0.435686 -0.0548257  -0.0300965  -0.151637   100  ARG A CZ  
499  N  NH1 . ARG A 64  ? 0.540012 0.645407 0.495885 -0.0577349  -0.036084   -0.160569   100  ARG A NH1 
500  N  NH2 . ARG A 64  ? 0.492594 0.579498 0.441884 -0.0517559  -0.028736   -0.138334   100  ARG A NH2 
501  N  N   . LYS A 65  ? 0.603017 0.681587 0.539216 -0.0639884  -0.0125314  -0.224513   101  LYS A N   
502  C  CA  . LYS A 65  ? 0.577842 0.654451 0.518624 -0.0681496  -0.011547   -0.242439   101  LYS A CA  
503  C  C   . LYS A 65  ? 0.576966 0.633833 0.522508 -0.0670264  -0.00342473 -0.245893   101  LYS A C   
504  O  O   . LYS A 65  ? 0.665928 0.716208 0.617317 -0.0705962  -0.00162848 -0.260139   101  LYS A O   
505  C  CB  . LYS A 65  ? 0.617632 0.71135  0.544008 -0.0660663  -0.0153819  -0.25219    101  LYS A CB  
506  C  CG  . LYS A 65  ? 0.737615 0.851597 0.655692 -0.0656524  -0.0244983  -0.250156   101  LYS A CG  
507  C  CD  . LYS A 65  ? 0.83713  0.96644  0.736946 -0.0625993  -0.0275491  -0.257582   101  LYS A CD  
508  C  CE  . LYS A 65  ? 0.963399 1.11115  0.854278 -0.0613994  -0.0375441  -0.254606   101  LYS A CE  
509  N  NZ  . LYS A 65  ? 1.01079  1.16325  0.91733  -0.0666623  -0.0433445  -0.261798   101  LYS A NZ  
510  N  N   . PHE A 66  ? 0.578167 0.625422 0.521388 -0.061692   0.00122532  -0.233784   102  PHE A N   
511  C  CA  . PHE A 66  ? 0.610594 0.637772 0.56028  -0.0600019  0.00795567  -0.236454   102  PHE A CA  
512  C  C   . PHE A 66  ? 0.704184 0.71347  0.666891 -0.0643578  0.00995104  -0.231505   102  PHE A C   
513  O  O   . PHE A 66  ? 0.744326 0.753793 0.708796 -0.0644121  0.00883381  -0.218349   102  PHE A O   
514  C  CB  . PHE A 66  ? 0.549891 0.574006 0.493518 -0.0522753  0.0120465   -0.226285   102  PHE A CB  
515  C  CG  . PHE A 66  ? 0.57552  0.614426 0.507106 -0.0488466  0.0123275   -0.234254   102  PHE A CG  
516  C  CD1 . PHE A 66  ? 0.557507 0.590902 0.490196 -0.047082   0.016178    -0.248145   102  PHE A CD1 
517  C  CD2 . PHE A 66  ? 0.55299  0.610734 0.471566 -0.0475487  0.00883508  -0.228186   102  PHE A CD2 
518  C  CE1 . PHE A 66  ? 0.59677  0.644926 0.518036 -0.044343   0.0169898   -0.25652    102  PHE A CE1 
519  C  CE2 . PHE A 66  ? 0.561431 0.632356 0.467371 -0.0450287  0.00983044  -0.23503    102  PHE A CE2 
520  C  CZ  . PHE A 66  ? 0.63625  0.703349 0.54365  -0.0436239  0.0140763   -0.249806   102  PHE A CZ  
521  N  N   . ASP A 67  ? 0.785923 0.779615 0.756983 -0.0682523  0.0131128   -0.242617   103  ASP A N   
522  C  CA  . ASP A 67  ? 0.785664 0.755106 0.766267 -0.0704248  0.0177409   -0.237794   103  ASP A CA  
523  C  C   . ASP A 67  ? 0.722574 0.679853 0.699542 -0.0616342  0.0216647   -0.227778   103  ASP A C   
524  O  O   . ASP A 67  ? 0.795046 0.745582 0.770167 -0.0565758  0.0243937   -0.234446   103  ASP A O   
525  C  CB  . ASP A 67  ? 0.830717 0.786731 0.820116 -0.0775725  0.0198466   -0.252673   103  ASP A CB  
526  C  CG  . ASP A 67  ? 0.862594 0.793764 0.861567 -0.0828702  0.0244109   -0.248379   103  ASP A CG  
527  O  OD1 . ASP A 67  ? 0.887672 0.810686 0.88653  -0.0807111  0.0260965   -0.233359   103  ASP A OD1 
528  O  OD2 . ASP A 67  ? 0.967515 0.886973 0.973558 -0.0895959  0.0264936   -0.260309   103  ASP A OD2 
529  N  N   . VAL A 68  ? 0.746771 0.702478 0.723243 -0.0594152  0.0216628   -0.212174   104  VAL A N   
530  C  CA  . VAL A 68  ? 0.834562 0.780074 0.808671 -0.0512673  0.0246688   -0.202606   104  VAL A CA  
531  C  C   . VAL A 68  ? 0.887462 0.805259 0.867835 -0.0509743  0.0288846   -0.202722   104  VAL A C   
532  O  O   . VAL A 68  ? 0.852505 0.759486 0.831761 -0.0432161  0.0311795   -0.199497   104  VAL A O   
533  C  CB  . VAL A 68  ? 0.755277 0.709921 0.726942 -0.0503853  0.0224272   -0.187112   104  VAL A CB  
534  C  CG1 . VAL A 68  ? 0.742031 0.679298 0.716451 -0.0471264  0.0251105   -0.174861   104  VAL A CG1 
535  C  CG2 . VAL A 68  ? 0.827455 0.80257  0.790022 -0.0457046  0.0201625   -0.183985   104  VAL A CG2 
536  N  N   . ASN A 69  ? 0.92906  0.835494 0.915957 -0.0594707  0.0298468   -0.206337   105  ASN A N   
537  C  CA  . ASN A 69  ? 0.919461 0.797543 0.910994 -0.0606694  0.0341449   -0.208259   105  ASN A CA  
538  C  C   . ASN A 69  ? 0.888214 0.759113 0.878657 -0.0546093  0.0355644   -0.219704   105  ASN A C   
539  O  O   . ASN A 69  ? 0.967988 0.822823 0.957414 -0.0467961  0.0376224   -0.215285   105  ASN A O   
540  C  CB  . ASN A 69  ? 0.852638 0.721324 0.851461 -0.0723129  0.035769    -0.212362   105  ASN A CB  
541  C  CG  . ASN A 69  ? 0.861109 0.734558 0.861417 -0.0765933  0.0353568   -0.199679   105  ASN A CG  
542  O  OD1 . ASN A 69  ? 0.84963  0.726791 0.845318 -0.0704018  0.0344196   -0.186637   105  ASN A OD1 
543  N  ND2 . ASN A 69  ? 0.844523 0.718916 0.851993 -0.0872846  0.0361616   -0.203905   105  ASN A ND2 
544  N  N   . GLN A 70  ? 0.900905 0.7866   0.890994 -0.0572737  0.0338467   -0.23403    106  GLN A N   
545  C  CA  . GLN A 70  ? 0.966153 0.848352 0.955634 -0.0527116  0.0351699   -0.248125   106  GLN A CA  
546  C  C   . GLN A 70  ? 0.919829 0.811229 0.903623 -0.0413163  0.035509    -0.245834   106  GLN A C   
547  O  O   . GLN A 70  ? 0.891383 0.778155 0.875629 -0.0363336  0.03727     -0.257207   106  GLN A O   
548  C  CB  . GLN A 70  ? 1.02976  0.92774  1.01966  -0.059586   0.0328467   -0.264186   106  GLN A CB  
549  C  CG  . GLN A 70  ? 1.16223  1.05101  1.16029  -0.0713368  0.0330411   -0.269966   106  GLN A CG  
550  C  CD  . GLN A 70  ? 1.16036  1.01693  1.16488  -0.073458   0.0377414   -0.274511   106  GLN A CD  
551  O  OE1 . GLN A 70  ? 1.18352  1.0306   1.1891   -0.0710521  0.039241    -0.287786   106  GLN A OE1 
552  N  NE2 . GLN A 70  ? 1.01321  0.851787 1.0215   -0.0780663  0.0403026   -0.263699   106  GLN A NE2 
553  N  N   . LEU A 71  ? 0.913301 0.81815  0.892492 -0.0372921  0.0341533   -0.232358   107  LEU A N   
554  C  CA  . LEU A 71  ? 0.82792  0.745148 0.802464 -0.0281034  0.0349177   -0.231304   107  LEU A CA  
555  C  C   . LEU A 71  ? 0.796251 0.694357 0.774536 -0.0194374  0.0372397   -0.225551   107  LEU A C   
556  O  O   . LEU A 71  ? 0.844942 0.731076 0.824731 -0.0192884  0.0369268   -0.212833   107  LEU A O   
557  C  CB  . LEU A 71  ? 0.829226 0.769836 0.796913 -0.0273797  0.0328339   -0.220901   107  LEU A CB  
558  C  CG  . LEU A 71  ? 0.860824 0.822693 0.822429 -0.0339168  0.0295307   -0.225515   107  LEU A CG  
559  C  CD1 . LEU A 71  ? 0.759459 0.7413   0.713022 -0.0325777  0.0275722   -0.214375   107  LEU A CD1 
560  C  CD2 . LEU A 71  ? 0.819465 0.788428 0.778429 -0.0342668  0.0301956   -0.243203   107  LEU A CD2 
561  N  N   . GLN A 72  ? 0.756217 0.654507 0.735351 -0.0117298  0.0392208   -0.235007   108  GLN A N   
562  C  CA  . GLN A 72  ? 0.82941  0.710735 0.812914 -0.00171815 0.040791    -0.233215   108  GLN A CA  
563  C  C   . GLN A 72  ? 0.731939 0.625825 0.714043 0.00491066  0.040348    -0.221013   108  GLN A C   
564  O  O   . GLN A 72  ? 0.85772  0.743114 0.840041 0.00490483  0.0389883   -0.207381   108  GLN A O   
565  C  CB  . GLN A 72  ? 0.913527 0.79379  0.899685 0.00463165  0.0429558   -0.24969    108  GLN A CB  
566  C  CG  . GLN A 72  ? 1.16037  1.0244   1.14927  -0.00068983 0.0436431   -0.263579   108  GLN A CG  
567  C  CD  . GLN A 72  ? 1.31337  1.14477  1.30632  -0.00166288 0.0437783   -0.257724   108  GLN A CD  
568  O  OE1 . GLN A 72  ? 1.33426  1.1473   1.33004  0.00767983  0.0442519   -0.254928   108  GLN A OE1 
569  N  NE2 . GLN A 72  ? 1.3258   1.15035  1.31869  -0.0128544  0.0433209   -0.25517    108  GLN A NE2 
570  N  N   . ASN A 73  ? 0.713589 0.627775 0.694319 0.00990924  0.0418851   -0.226881   109  ASN A N   
571  C  CA  . ASN A 73  ? 0.750214 0.682424 0.729576 0.0143966   0.0422757   -0.218133   109  ASN A CA  
572  C  C   . ASN A 73  ? 0.670831 0.605033 0.647228 0.009577    0.0397577   -0.201573   109  ASN A C   
573  O  O   . ASN A 73  ? 0.732844 0.672182 0.7047   0.00099868  0.0381176   -0.198985   109  ASN A O   
574  C  CB  . ASN A 73  ? 0.712214 0.670705 0.686601 0.0138949   0.0447318   -0.226389   109  ASN A CB  
575  C  CG  . ASN A 73  ? 0.773306 0.747677 0.748182 0.0188175   0.0462203   -0.218424   109  ASN A CG  
576  O  OD1 . ASN A 73  ? 0.819668 0.801838 0.790621 0.0148653   0.044714    -0.205667   109  ASN A OD1 
577  N  ND2 . ASN A 73  ? 0.808753 0.787923 0.789391 0.0273672   0.0491363   -0.22601    109  ASN A ND2 
578  N  N   . THR A 74  ? 0.628696 0.560002 0.608085 0.0155352   0.0391409   -0.191036   110  THR A N   
579  C  CA  . THR A 74  ? 0.663176 0.592621 0.640417 0.011462    0.0367285   -0.176073   110  THR A CA  
580  C  C   . THR A 74  ? 0.642241 0.595683 0.614806 0.00871751  0.0366479   -0.169527   110  THR A C   
581  O  O   . THR A 74  ? 0.589131 0.545843 0.557748 0.0021253   0.0346103   -0.161558   110  THR A O   
582  C  CB  . THR A 74  ? 0.651563 0.561675 0.632582 0.0171659   0.0352174   -0.166517   110  THR A CB  
583  O  OG1 . THR A 74  ? 0.669515 0.588998 0.654416 0.0262432   0.0357536   -0.166682   110  THR A OG1 
584  C  CG2 . THR A 74  ? 0.640007 0.522556 0.623155 0.0181489   0.0352724   -0.170569   110  THR A CG2 
585  N  N   . THR A 75  ? 0.64935  0.618939 0.622556 0.0135154   0.039041    -0.172803   111  THR A N   
586  C  CA  . THR A 75  ? 0.611958 0.60327  0.57928  0.00979527  0.0398447   -0.167438   111  THR A CA  
587  C  C   . THR A 75  ? 0.616824 0.615966 0.575279 0.00126507  0.0386514   -0.169684   111  THR A C   
588  O  O   . THR A 75  ? 0.549492 0.556611 0.502447 -0.0035427  0.0366929   -0.160211   111  THR A O   
589  C  CB  . THR A 75  ? 0.574983 0.582772 0.543881 0.0146763   0.0440486   -0.1744     111  THR A CB  
590  O  OG1 . THR A 75  ? 0.614203 0.615602 0.592369 0.0227972   0.0439163   -0.171681   111  THR A OG1 
591  C  CG2 . THR A 75  ? 0.554789 0.582675 0.517692 0.0108767   0.045716    -0.16717    111  THR A CG2 
592  N  N   . ILE A 76  ? 0.57522  0.572473 0.532382 -0.00012053 0.0394285   -0.182783   112  ILE A N   
593  C  CA  . ILE A 76  ? 0.543136 0.550223 0.491872 -0.00720543 0.037867    -0.187265   112  ILE A CA  
594  C  C   . ILE A 76  ? 0.620101 0.616963 0.569663 -0.0132528  0.0336487   -0.181565   112  ILE A C   
595  O  O   . ILE A 76  ? 0.560984 0.568497 0.504003 -0.0185464  0.0307624   -0.177195   112  ILE A O   
596  C  CB  . ILE A 76  ? 0.539095 0.549028 0.486488 -0.00655193 0.0400477   -0.204196   112  ILE A CB  
597  C  CG1 . ILE A 76  ? 0.533216 0.561342 0.476289 -0.0028539  0.044474    -0.208606   112  ILE A CG1 
598  C  CG2 . ILE A 76  ? 0.542651 0.557116 0.483579 -0.0139657  0.0369212   -0.210138   112  ILE A CG2 
599  C  CD1 . ILE A 76  ? 0.542095 0.569174 0.48902  0.00203646  0.0480741   -0.224898   112  ILE A CD1 
600  N  N   . LYS A 77  ? 0.624665 0.600867 0.582075 -0.0123241  0.0334033   -0.181679   113  LYS A N   
601  C  CA  . LYS A 77  ? 0.616196 0.581943 0.575771 -0.0183065  0.0306109   -0.175924   113  LYS A CA  
602  C  C   . LYS A 77  ? 0.543711 0.517362 0.500641 -0.0196266  0.0284024   -0.16127    113  LYS A C   
603  O  O   . LYS A 77  ? 0.505705 0.483734 0.460923 -0.0254448  0.0254292   -0.15753    113  LYS A O   
604  C  CB  . LYS A 77  ? 0.68604  0.626994 0.652907 -0.0158471  0.0317877   -0.174187   113  LYS A CB  
605  C  CG  . LYS A 77  ? 0.823562 0.748825 0.793944 -0.0229231  0.0310781   -0.175074   113  LYS A CG  
606  C  CD  . LYS A 77  ? 0.91111  0.810654 0.885904 -0.0194537  0.0328201   -0.170714   113  LYS A CD  
607  C  CE  . LYS A 77  ? 0.898605 0.777385 0.87714  -0.0242917  0.0344335   -0.178086   113  LYS A CE  
608  N  NZ  . LYS A 77  ? 0.889688 0.767516 0.869696 -0.0343905  0.0338189   -0.175213   113  LYS A NZ  
609  N  N   . ARG A 78  ? 0.489326 0.464179 0.447147 -0.0138949  0.029701    -0.15349    114  ARG A N   
610  C  CA  . ARG A 78  ? 0.507479 0.487101 0.463958 -0.0144224  0.0279074   -0.139722   114  ARG A CA  
611  C  C   . ARG A 78  ? 0.513031 0.512183 0.461309 -0.0178044  0.0264208   -0.137096   114  ARG A C   
612  O  O   . ARG A 78  ? 0.428412 0.431258 0.374439 -0.0210844  0.0234623   -0.128362   114  ARG A O   
613  C  CB  . ARG A 78  ? 0.449659 0.429778 0.409112 -0.00717308 0.0299978   -0.135523   114  ARG A CB  
614  C  CG  . ARG A 78  ? 0.467205 0.446202 0.427792 -0.00654025 0.0282998   -0.122034   114  ARG A CG  
615  C  CD  . ARG A 78  ? 0.452182 0.423297 0.418654 0.0010199   0.0292944   -0.119475   114  ARG A CD  
616  N  NE  . ARG A 78  ? 0.473329 0.44718  0.440321 0.00159704  0.0276672   -0.1076     114  ARG A NE  
617  C  CZ  . ARG A 78  ? 0.424732 0.389017 0.391835 -0.00043048 0.0253755   -0.0990744  114  ARG A CZ  
618  N  NH1 . ARG A 78  ? 0.385873 0.337065 0.352792 -0.00389072 0.0248109   -0.100449   114  ARG A NH1 
619  N  NH2 . ARG A 78  ? 0.442225 0.41064  0.409896 0.00066059  0.0240637   -0.089775   114  ARG A NH2 
620  N  N   . ILE A 79  ? 0.487523 0.49895  0.430861 -0.0161934  0.0288185   -0.144071   115  ILE A N   
621  C  CA  . ILE A 79  ? 0.475142 0.503874 0.408098 -0.0191367  0.0279848   -0.142066   115  ILE A CA  
622  C  C   . ILE A 79  ? 0.423519 0.454981 0.352035 -0.0246412  0.0235523   -0.145026   115  ILE A C   
623  O  O   . ILE A 79  ? 0.434628 0.473278 0.357506 -0.0272049  0.0201322   -0.137248   115  ILE A O   
624  C  CB  . ILE A 79  ? 0.497272 0.537811 0.425247 -0.0167697  0.0323907   -0.150529   115  ILE A CB  
625  C  CG1 . ILE A 79  ? 0.436599 0.479263 0.369702 -0.0116091  0.0366017   -0.146323   115  ILE A CG1 
626  C  CG2 . ILE A 79  ? 0.486691 0.54308  0.400941 -0.0207139  0.0313074   -0.150216   115  ILE A CG2 
627  C  CD1 . ILE A 79  ? 0.437294 0.49096  0.368882 -0.00864195 0.0420192   -0.156799   115  ILE A CD1 
628  N  N   . ILE A 80  ? 0.45081  0.476133 0.382742 -0.0262951  0.0232795   -0.156479   116  ILE A N   
629  C  CA  . ILE A 80  ? 0.444512 0.47492  0.373384 -0.0316579  0.0189289   -0.161747   116  ILE A CA  
630  C  C   . ILE A 80  ? 0.504615 0.528509 0.439386 -0.0349473  0.0153596   -0.153524   116  ILE A C   
631  O  O   . ILE A 80  ? 0.461765 0.49464  0.393249 -0.0385313  0.0107161   -0.153296   116  ILE A O   
632  C  CB  . ILE A 80  ? 0.478849 0.504602 0.410856 -0.0333049  0.0198334   -0.177452   116  ILE A CB  
633  C  CG1 . ILE A 80  ? 0.491722 0.529026 0.415441 -0.0307628  0.0225705   -0.186867   116  ILE A CG1 
634  C  CG2 . ILE A 80  ? 0.462931 0.490035 0.397093 -0.0396961  0.0151205   -0.18305    116  ILE A CG2 
635  C  CD1 . ILE A 80  ? 0.53405  0.566156 0.461191 -0.0313942  0.0240525   -0.203514   116  ILE A CD1 
636  N  N   . LYS A 81  ? 0.517777 0.52673  0.460943 -0.0334128  0.017387    -0.14739    117  LYS A N   
637  C  CA  . LYS A 81  ? 0.59676  0.600433 0.545048 -0.0367268  0.0148146   -0.139663   117  LYS A CA  
638  C  C   . LYS A 81  ? 0.500251 0.514196 0.44354  -0.0357781  0.011984    -0.127772   117  LYS A C   
639  O  O   . LYS A 81  ? 0.524985 0.543715 0.468971 -0.0389204  0.00804193  -0.124712   117  LYS A O   
640  C  CB  . LYS A 81  ? 0.700845 0.685952 0.657226 -0.0358458  0.0174219   -0.134675   117  LYS A CB  
641  C  CG  . LYS A 81  ? 0.849763 0.821129 0.812737 -0.0400543  0.0188721   -0.142882   117  LYS A CG  
642  C  CD  . LYS A 81  ? 1.07092  1.02475  1.03846  -0.0385887  0.0211895   -0.134005   117  LYS A CD  
643  C  CE  . LYS A 81  ? 1.13808  1.07417  1.108    -0.0353564  0.0247575   -0.139537   117  LYS A CE  
644  N  NZ  . LYS A 81  ? 1.10729  1.02358  1.08051  -0.03578    0.0267524   -0.132678   117  LYS A NZ  
645  N  N   . LYS A 82  ? 0.505112 0.522822 0.443914 -0.0315486  0.0139618   -0.121678   118  LYS A N   
646  C  CA  . LYS A 82  ? 0.521555 0.548966 0.454113 -0.0311915  0.0114624   -0.111541   118  LYS A CA  
647  C  C   . LYS A 82  ? 0.536349 0.577667 0.459238 -0.033535   0.00728778  -0.114369   118  LYS A C   
648  O  O   . LYS A 82  ? 0.543687 0.589257 0.464931 -0.0347891  0.00269048  -0.108209   118  LYS A O   
649  C  CB  . LYS A 82  ? 0.561335 0.591033 0.491112 -0.027256   0.0151375   -0.106143   118  LYS A CB  
650  C  CG  . LYS A 82  ? 0.707633 0.744913 0.630998 -0.0277367  0.0127027   -0.0951922  118  LYS A CG  
651  C  CD  . LYS A 82  ? 0.773772 0.810465 0.698445 -0.0249052  0.0161337   -0.0877348  118  LYS A CD  
652  C  CE  . LYS A 82  ? 0.707787 0.732684 0.643136 -0.0219915  0.0182252   -0.088227   118  LYS A CE  
653  N  NZ  . LYS A 82  ? 0.662553 0.680546 0.602814 -0.02168    0.0162087   -0.0788031  118  LYS A NZ  
654  N  N   . VAL A 83  ? 0.460423 0.508983 0.376552 -0.0336953  0.0083918   -0.124018   119  VAL A N   
655  C  CA  . VAL A 83  ? 0.437476 0.499219 0.342387 -0.0353161  0.00393018  -0.126356   119  VAL A CA  
656  C  C   . VAL A 83  ? 0.477454 0.541215 0.386696 -0.0385174  -0.00230645 -0.129557   119  VAL A C   
657  O  O   . VAL A 83  ? 0.496674 0.570871 0.397836 -0.0388436  -0.0079735  -0.127712   119  VAL A O   
658  C  CB  . VAL A 83  ? 0.391159 0.460766 0.287346 -0.0350388  0.00638017  -0.137137   119  VAL A CB  
659  C  CG1 . VAL A 83  ? 0.404306 0.487075 0.287797 -0.0365907  0.00070946  -0.13989    119  VAL A CG1 
660  C  CG2 . VAL A 83  ? 0.374224 0.445659 0.265705 -0.0321684  0.012509    -0.133437   119  VAL A CG2 
661  N  N   . GLN A 84  ? 0.482685 0.536719 0.404597 -0.0409207  -0.00137713 -0.134622   120  GLN A N   
662  C  CA  . GLN A 84  ? 0.487447 0.545014 0.415373 -0.044914   -0.00641481 -0.139551   120  GLN A CA  
663  C  C   . GLN A 84  ? 0.457754 0.516964 0.38897  -0.0446981  -0.0103412  -0.12875    120  GLN A C   
664  O  O   . GLN A 84  ? 0.478969 0.544059 0.415669 -0.0474665  -0.015099   -0.132096   120  GLN A O   
665  C  CB  . GLN A 84  ? 0.529489 0.573897 0.470122 -0.0484095  -0.0027413  -0.147073   120  GLN A CB  
666  C  CG  . GLN A 84  ? 0.540163 0.584732 0.480365 -0.0503782  -0.00127831 -0.162057   120  GLN A CG  
667  C  CD  . GLN A 84  ? 0.554162 0.581766 0.505808 -0.0534217  0.00321838  -0.168023   120  GLN A CD  
668  O  OE1 . GLN A 84  ? 0.537641 0.552865 0.496049 -0.0536043  0.00574731  -0.160075   120  GLN A OE1 
669  N  NE2 . GLN A 84  ? 0.557044 0.583069 0.50978  -0.0556275  0.00437862  -0.18187    120  GLN A NE2 
670  N  N   . ASP A 85  ? 0.416205 0.470425 0.3456   -0.0414941  -0.00820308 -0.116836   121  ASP A N   
671  C  CA  . ASP A 85  ? 0.405786 0.46215  0.336526 -0.0404698  -0.0120443  -0.106654   121  ASP A CA  
672  C  C   . ASP A 85  ? 0.40402  0.471645 0.321317 -0.0378055  -0.0169619  -0.101686   121  ASP A C   
673  O  O   . ASP A 85  ? 0.408169 0.475434 0.316228 -0.0355148  -0.014262   -0.0960079  121  ASP A O   
674  C  CB  . ASP A 85  ? 0.413339 0.459893 0.346515 -0.0380175  -0.00806614 -0.0958888  121  ASP A CB  
675  C  CG  . ASP A 85  ? 0.46348  0.509301 0.402314 -0.0378209  -0.0111845  -0.0878228  121  ASP A CG  
676  O  OD1 . ASP A 85  ? 0.48915  0.544129 0.427367 -0.0381269  -0.0171428  -0.0882928  121  ASP A OD1 
677  O  OD2 . ASP A 85  ? 0.564395 0.60073  0.508991 -0.037183   -0.00788532 -0.0821701  121  ASP A OD2 
678  N  N   . LEU A 86  ? 0.396714 0.47364  0.313284 -0.0379009  -0.0241811  -0.102612   122  LEU A N   
679  C  CA  . LEU A 86  ? 0.415377 0.501944 0.317314 -0.0349187  -0.0298648  -0.0983982  122  LEU A CA  
680  C  C   . LEU A 86  ? 0.415606 0.498409 0.315361 -0.0317571  -0.0315225  -0.0845592  122  LEU A C   
681  O  O   . LEU A 86  ? 0.409247 0.496246 0.295623 -0.028983   -0.03539    -0.0783052  122  LEU A O   
682  C  CB  . LEU A 86  ? 0.39667  0.495579 0.298813 -0.0354651  -0.0380117  -0.106748   122  LEU A CB  
683  C  CG  . LEU A 86  ? 0.475602 0.581664 0.374596 -0.0380198  -0.038411   -0.120809   122  LEU A CG  
684  C  CD1 . LEU A 86  ? 0.515318 0.612697 0.422429 -0.0416189  -0.0305684  -0.129049   122  LEU A CD1 
685  C  CD2 . LEU A 86  ? 0.489545 0.607339 0.395654 -0.0395087  -0.0463588  -0.130134   122  LEU A CD2 
686  N  N   . GLU A 87  ? 0.377838 0.452046 0.289934 -0.0322408  -0.0286426  -0.0799922  123  GLU A N   
687  C  CA  . GLU A 87  ? 0.364319 0.436021 0.277982 -0.0295774  -0.0315075  -0.0695158  123  GLU A CA  
688  C  C   . GLU A 87  ? 0.388936 0.470727 0.298474 -0.0269868  -0.0408071  -0.0694735  123  GLU A C   
689  O  O   . GLU A 87  ? 0.426222 0.516289 0.342146 -0.0283843  -0.0448586  -0.078696   123  GLU A O   
690  C  CB  . GLU A 87  ? 0.462665 0.528267 0.366717 -0.0280857  -0.0269845  -0.060415   123  GLU A CB  
691  C  CG  . GLU A 87  ? 0.588616 0.645071 0.500193 -0.0295018  -0.0190479  -0.0605217  123  GLU A CG  
692  C  CD  . GLU A 87  ? 0.7298   0.778898 0.653603 -0.0292701  -0.0184124  -0.0558733  123  GLU A CD  
693  O  OE1 . GLU A 87  ? 0.672156 0.713035 0.602657 -0.029716   -0.013219   -0.0550209  123  GLU A OE1 
694  O  OE2 . GLU A 87  ? 0.78181  0.833955 0.707963 -0.0280792  -0.0237664  -0.0529244  123  GLU A OE2 
695  N  N   . ARG A 88  ? 0.374567 0.455861 0.273034 -0.023048   -0.0446385  -0.0594853  124  ARG A N   
696  C  CA  . ARG A 88  ? 0.378548 0.467133 0.274544 -0.0190259  -0.054227   -0.057778   124  ARG A CA  
697  C  C   . ARG A 88  ? 0.38209  0.481874 0.267728 -0.0185799  -0.0595724  -0.0655541  124  ARG A C   
698  O  O   . ARG A 88  ? 0.39612  0.505547 0.282266 -0.0156105  -0.0684212  -0.0688599  124  ARG A O   
699  C  CB  . ARG A 88  ? 0.412962 0.494229 0.299444 -0.0150438  -0.0559342  -0.0443218  124  ARG A CB  
700  C  CG  . ARG A 88  ? 0.498609 0.578052 0.365054 -0.0151564  -0.0537487  -0.0397046  124  ARG A CG  
701  C  CD  . ARG A 88  ? 0.530122 0.600943 0.382154 -0.0126522  -0.054106   -0.0259765  124  ARG A CD  
702  N  NE  . ARG A 88  ? 0.613726 0.674832 0.474761 -0.0149627  -0.04655    -0.0209468  124  ARG A NE  
703  C  CZ  . ARG A 88  ? 0.713902 0.765551 0.572884 -0.0137663  -0.0457349  -0.0103869  124  ARG A CZ  
704  N  NH1 . ARG A 88  ? 0.742026 0.790202 0.587312 -0.010435   -0.0511684  -0.00198469 124  ARG A NH1 
705  N  NH2 . ARG A 88  ? 0.637799 0.682872 0.507824 -0.0158103  -0.0396987  -0.00837786 124  ARG A NH2 
706  N  N   . ALA A 89  ? 0.387233 0.486936 0.264634 -0.0214408  -0.0543028  -0.0700253  125  ALA A N   
707  C  CA  . ALA A 89  ? 0.42448  0.535156 0.290448 -0.0211244  -0.0590846  -0.0781541  125  ALA A CA  
708  C  C   . ALA A 89  ? 0.429245 0.549685 0.309372 -0.0236145  -0.0627113  -0.0922292  125  ALA A C   
709  O  O   . ALA A 89  ? 0.41562  0.546807 0.289058 -0.0234617  -0.0677958  -0.100884   125  ALA A O   
710  C  CB  . ALA A 89  ? 0.381466 0.490181 0.234542 -0.0233683  -0.0520445  -0.0797121  125  ALA A CB  
711  N  N   . ALA A 90  ? 0.400192 0.517053 0.299684 -0.0263361  -0.0598977  -0.094757   126  ALA A N   
712  C  CA  . ALA A 90  ? 0.385848 0.511353 0.300364 -0.0299441  -0.0623376  -0.107823   126  ALA A CA  
713  C  C   . ALA A 90  ? 0.371369 0.509295 0.288721 -0.0258018  -0.0731178  -0.108365   126  ALA A C   
714  O  O   . ALA A 90  ? 0.373995 0.524497 0.299391 -0.0274625  -0.0782916  -0.119935   126  ALA A O   
715  C  CB  . ALA A 90  ? 0.370225 0.485911 0.302525 -0.0347196  -0.0544485  -0.109011   126  ALA A CB  
716  N  N   . LEU A 91  ? 0.360413 0.495197 0.271381 -0.0199933  -0.0770648  -0.0962016  127  LEU A N   
717  C  CA  . LEU A 91  ? 0.336003 0.48137  0.253672 -0.0153043  -0.0870094  -0.096834   127  LEU A CA  
718  C  C   . LEU A 91  ? 0.352079 0.511304 0.258163 -0.011673   -0.0970948  -0.102864   127  LEU A C   
719  O  O   . LEU A 91  ? 0.361457 0.517819 0.247863 -0.0101927  -0.0970522  -0.0990514  127  LEU A O   
720  C  CB  . LEU A 91  ? 0.311925 0.449576 0.225389 -0.00920365 -0.0895779  -0.082896   127  LEU A CB  
721  C  CG  . LEU A 91  ? 0.300727 0.426353 0.226269 -0.0116424  -0.081366   -0.076845   127  LEU A CG  
722  C  CD1 . LEU A 91  ? 0.294591 0.408718 0.209465 -0.00636983 -0.0820293  -0.0618335  127  LEU A CD1 
723  C  CD2 . LEU A 91  ? 0.261612 0.396237 0.208637 -0.0127531  -0.0835673  -0.0843673  127  LEU A CD2 
724  N  N   . PRO A 92  ? 0.372021 0.546621 0.288416 -0.00906816 -0.106612   -0.11079    128  PRO A N   
725  C  CA  . PRO A 92  ? 0.401508 0.589207 0.304282 -0.0031845  -0.118517   -0.114149   128  PRO A CA  
726  C  C   . PRO A 92  ? 0.460444 0.640262 0.340351 0.00511117  -0.123864   -0.0990468  128  PRO A C   
727  O  O   . PRO A 92  ? 0.488051 0.655511 0.368016 0.00765268  -0.121209   -0.0868861  128  PRO A O   
728  C  CB  . PRO A 92  ? 0.374413 0.580171 0.296359 -0.00146478 -0.127498   -0.124973   128  PRO A CB  
729  C  CG  . PRO A 92  ? 0.356406 0.558108 0.302445 -0.00758298 -0.118903   -0.127351   128  PRO A CG  
730  C  CD  . PRO A 92  ? 0.350459 0.530747 0.291104 -0.0108556  -0.106659   -0.115815   128  PRO A CD  
731  N  N   . ALA A 93  ? 0.491587 0.677684 0.350815 0.00908504  -0.131216   -0.0997054  129  ALA A N   
732  C  CA  . ALA A 93  ? 0.533516 0.711068 0.366835 0.0161154   -0.135888   -0.0854744  129  ALA A CA  
733  C  C   . ALA A 93  ? 0.546311 0.7153   0.383367 0.0228317   -0.140054   -0.0732094  129  ALA A C   
734  O  O   . ALA A 93  ? 0.539517 0.691538 0.365716 0.0234735   -0.134694   -0.059175   129  ALA A O   
735  C  CB  . ALA A 93  ? 0.496486 0.687504 0.312417 0.0215152   -0.147826   -0.0906716  129  ALA A CB  
736  N  N   . GLN A 94  ? 0.539227 0.720819 0.392764 0.0276571   -0.149559   -0.0796029  130  GLN A N   
737  C  CA  . GLN A 94  ? 0.548655 0.725007 0.406851 0.0355328   -0.155601   -0.0704225  130  GLN A CA  
738  C  C   . GLN A 94  ? 0.52624  0.68786  0.397299 0.0315127   -0.144746   -0.0631983  130  GLN A C   
739  O  O   . GLN A 94  ? 0.498561 0.644338 0.358474 0.0352954   -0.143876   -0.0491606  130  GLN A O   
740  C  CB  . GLN A 94  ? 0.538028 0.734332 0.417334 0.0395459   -0.16563    -0.0826982  130  GLN A CB  
741  C  CG  . GLN A 94  ? 0.641526 0.840776 0.511143 0.0524248   -0.180565   -0.0766394  130  GLN A CG  
742  C  CD  . GLN A 94  ? 0.686678 0.903023 0.582699 0.0567481   -0.188235   -0.0867404  130  GLN A CD  
743  O  OE1 . GLN A 94  ? 0.735869 0.948953 0.651936 0.0536727   -0.181394   -0.0869222  130  GLN A OE1 
744  N  NE2 . GLN A 94  ? 0.722424 0.958171 0.619283 0.0634001   -0.201901   -0.0960611  130  GLN A NE2 
745  N  N   . GLU A 95  ? 0.455859 0.622315 0.349549 0.0237771   -0.136712   -0.0728817  131  GLU A N   
746  C  CA  . GLU A 95  ? 0.429284 0.583134 0.335072 0.0191401   -0.125916   -0.0677809  131  GLU A CA  
747  C  C   . GLU A 95  ? 0.423196 0.558949 0.311475 0.0161554   -0.117018   -0.0562612  131  GLU A C   
748  O  O   . GLU A 95  ? 0.424562 0.547086 0.315034 0.0160333   -0.111644   -0.0470357  131  GLU A O   
749  C  CB  . GLU A 95  ? 0.421623 0.581695 0.347808 0.0100048   -0.117612   -0.0798941  131  GLU A CB  
750  C  CG  . GLU A 95  ? 0.43312  0.608991 0.382418 0.0110516   -0.122859   -0.0902002  131  GLU A CG  
751  C  CD  . GLU A 95  ? 0.516982 0.712808 0.466432 0.0146962   -0.134644   -0.101134   131  GLU A CD  
752  O  OE1 . GLU A 95  ? 0.603742 0.803129 0.537055 0.0151476   -0.138431   -0.103514   131  GLU A OE1 
753  O  OE2 . GLU A 95  ? 0.527021 0.736583 0.493557 0.017784    -0.140886   -0.107907   131  GLU A OE2 
754  N  N   . LEU A 96  ? 0.431731 0.567783 0.303212 0.0134618   -0.115103   -0.0575647  132  LEU A N   
755  C  CA  . LEU A 96  ? 0.418274 0.539321 0.276181 0.00974213  -0.105419   -0.0482436  132  LEU A CA  
756  C  C   . LEU A 96  ? 0.471495 0.580563 0.311415 0.0157176   -0.109154   -0.0331367  132  LEU A C   
757  O  O   . LEU A 96  ? 0.433882 0.52877  0.273192 0.0140205   -0.102184   -0.0234881  132  LEU A O   
758  C  CB  . LEU A 96  ? 0.416812 0.541962 0.262589 0.00512861  -0.101412   -0.0544785  132  LEU A CB  
759  C  CG  . LEU A 96  ? 0.415386 0.528137 0.243294 0.00241975  -0.0929179  -0.0450765  132  LEU A CG  
760  C  CD1 . LEU A 96  ? 0.388638 0.489438 0.227948 -0.00176293 -0.0825179  -0.0400971  132  LEU A CD1 
761  C  CD2 . LEU A 96  ? 0.442597 0.56272  0.258967 -0.00119945 -0.090262   -0.053606   132  LEU A CD2 
762  N  N   . GLU A 97  ? 0.509156 0.623693 0.333742 0.0224917   -0.120207   -0.0314824  133  GLU A N   
763  C  CA  . GLU A 97  ? 0.569032 0.671149 0.375286 0.0290092   -0.125313   -0.0170182  133  GLU A CA  
764  C  C   . GLU A 97  ? 0.528599 0.621902 0.349787 0.0324732   -0.126068   -0.0108759  133  GLU A C   
765  O  O   . GLU A 97  ? 0.539136 0.616124 0.352941 0.0323493   -0.121748   0.00100338  133  GLU A O   
766  C  CB  . GLU A 97  ? 0.571387 0.682375 0.361729 0.0369103   -0.138771   -0.0179374  133  GLU A CB  
767  C  CG  . GLU A 97  ? 0.663109 0.763037 0.443886 0.0463523   -0.147713   -0.00536835 133  GLU A CG  
768  C  CD  . GLU A 97  ? 0.80455  0.920103 0.591996 0.0556508   -0.162874   -0.012974   133  GLU A CD  
769  O  OE1 . GLU A 97  ? 0.748858 0.872892 0.56195  0.0578837   -0.165864   -0.020169   133  GLU A OE1 
770  O  OE2 . GLU A 97  ? 0.699665 0.820529 0.466244 0.059947    -0.17102    -0.012825   133  GLU A OE2 
771  N  N   . GLU A 98  ? 0.513323 0.618212 0.356415 0.0349984   -0.131028   -0.019958   134  GLU A N   
772  C  CA  . GLU A 98  ? 0.539091 0.638868 0.398217 0.0385363   -0.132053   -0.0167648  134  GLU A CA  
773  C  C   . GLU A 98  ? 0.509732 0.597366 0.37806  0.0314194   -0.119172   -0.0128865  134  GLU A C   
774  O  O   . GLU A 98  ? 0.462102 0.536635 0.331008 0.0338636   -0.11803    -0.00374231 134  GLU A O   
775  C  CB  . GLU A 98  ? 0.504734 0.623614 0.384539 0.0419454   -0.139806   -0.0296193  134  GLU A CB  
776  C  CG  . GLU A 98  ? 0.566508 0.681756 0.465294 0.0443806   -0.138817   -0.0282244  134  GLU A CG  
777  C  CD  . GLU A 98  ? 0.650074 0.784798 0.57102  0.0474174   -0.145394   -0.0409015  134  GLU A CD  
778  O  OE1 . GLU A 98  ? 0.6897   0.839962 0.612077 0.0455561   -0.148901   -0.0512557  134  GLU A OE1 
779  O  OE2 . GLU A 98  ? 0.677422 0.812454 0.613839 0.0511968   -0.146696   -0.0410989  134  GLU A OE2 
780  N  N   . TYR A 99  ? 0.485569 0.577033 0.360965 0.0229132   -0.109769   -0.0200604  135  TYR A N   
781  C  CA  . TYR A 99  ? 0.452046 0.532852 0.33563  0.0171265   -0.0986746  -0.0167252  135  TYR A CA  
782  C  C   . TYR A 99  ? 0.456378 0.521426 0.321713 0.015784    -0.093606   -0.00432004 135  TYR A C   
783  O  O   . TYR A 99  ? 0.463173 0.516447 0.331947 0.0149537   -0.0889184  0.00280476  135  TYR A O   
784  C  CB  . TYR A 99  ? 0.425978 0.514435 0.319394 0.00951723  -0.0913217  -0.0275614  135  TYR A CB  
785  C  CG  . TYR A 99  ? 0.449395 0.527705 0.349436 0.00349087  -0.0798354  -0.0251684  135  TYR A CG  
786  C  CD1 . TYR A 99  ? 0.458587 0.532849 0.374104 0.00334783  -0.0770588  -0.0242083  135  TYR A CD1 
787  C  CD2 . TYR A 99  ? 0.502759 0.576585 0.393912 -0.00166371 -0.0719892  -0.0246729  135  TYR A CD2 
788  C  CE1 . TYR A 99  ? 0.468874 0.534349 0.389552 -0.00151793 -0.067442   -0.0222177  135  TYR A CE1 
789  C  CE2 . TYR A 99  ? 0.471285 0.536813 0.368945 -0.00619297 -0.0624572  -0.0229951  135  TYR A CE2 
790  C  CZ  . TYR A 99  ? 0.47645  0.537735 0.388507 -0.00600837 -0.0605664  -0.0216671  135  TYR A CZ  
791  O  OH  . TYR A 99  ? 0.488326 0.542029 0.406074 -0.00976194 -0.0522153  -0.020254   135  TYR A OH  
792  N  N   . ASN A 100 ? 0.465769 0.531131 0.311481 0.0151261   -0.0942255  -0.00216314 136  ASN A N   
793  C  CA  . ASN A 100 ? 0.497944 0.549844 0.325223 0.0129537   -0.0888397  0.00911841  136  ASN A CA  
794  C  C   . ASN A 100 ? 0.474358 0.51264  0.294855 0.018461    -0.0936313  0.0213249   136  ASN A C   
795  O  O   . ASN A 100 ? 0.488557 0.513512 0.305749 0.0153417   -0.0869468  0.0298221   136  ASN A O   
796  C  CB  . ASN A 100 ? 0.4891   0.544652 0.294282 0.0121907   -0.0898344  0.00947516  136  ASN A CB  
797  C  CG  . ASN A 100 ? 0.537511 0.601174 0.345423 0.00531148  -0.0816658  -5.729e-05  136  ASN A CG  
798  O  OD1 . ASN A 100 ? 0.533099 0.592921 0.352212 8.677e-05   -0.0723089  -0.0013387  136  ASN A OD1 
799  N  ND2 . ASN A 100 ? 0.495747 0.570398 0.293651 0.00571458  -0.0854596  -0.0071445  136  ASN A ND2 
800  N  N   . LYS A 101 ? 0.497222 0.539386 0.317207 0.0266705   -0.105296   0.0211569   137  LYS A N   
801  C  CA  . LYS A 101 ? 0.527154 0.556595 0.340258 0.0338781   -0.112225   0.0317547   137  LYS A CA  
802  C  C   . LYS A 101 ? 0.524957 0.5487   0.358418 0.0341006   -0.109385   0.0319134   137  LYS A C   
803  O  O   . LYS A 101 ? 0.505219 0.512783 0.3339   0.0348094   -0.107608   0.0418994   137  LYS A O   
804  C  CB  . LYS A 101 ? 0.54389  0.582044 0.351627 0.043436    -0.126311   0.0293877   137  LYS A CB  
805  C  CG  . LYS A 101 ? 0.591602 0.618648 0.396608 0.0530258   -0.135598   0.0378755   137  LYS A CG  
806  C  CD  . LYS A 101 ? 0.687259 0.690852 0.471737 0.0529844   -0.133037   0.0538392   137  LYS A CD  
807  C  CE  . LYS A 101 ? 0.752496 0.745774 0.521516 0.0642563   -0.145857   0.0629448   137  LYS A CE  
808  N  NZ  . LYS A 101 ? 0.672288 0.672993 0.461289 0.0735954   -0.155639   0.0567026   137  LYS A NZ  
809  N  N   . ILE A 102 ? 0.516063 0.552837 0.371493 0.0327009   -0.108219   0.0205736   138  ILE A N   
810  C  CA  . ILE A 102 ? 0.508877 0.542586 0.383737 0.0320442   -0.104457   0.019046    138  ILE A CA  
811  C  C   . ILE A 102 ? 0.463648 0.484911 0.336887 0.0248329   -0.0931835  0.0247896   138  ILE A C   
812  O  O   . ILE A 102 ? 0.457314 0.466731 0.333492 0.0258387   -0.0916761  0.0309845   138  ILE A O   
813  C  CB  . ILE A 102 ? 0.556947 0.607852 0.452911 0.0306885   -0.104465   0.00556854  138  ILE A CB  
814  C  CG1 . ILE A 102 ? 0.604393 0.663463 0.510969 0.0394501   -0.115091   0.00172342  138  ILE A CG1 
815  C  CG2 . ILE A 102 ? 0.511214 0.560249 0.422292 0.0239267   -0.0940269  0.00228434  138  ILE A CG2 
816  C  CD1 . ILE A 102 ? 0.596468 0.675305 0.521182 0.0377932   -0.116228   -0.0122993  138  ILE A CD1 
817  N  N   . LEU A 103 ? 0.488863 0.513197 0.358138 0.0176717   -0.0853154  0.0220573   139  LEU A N   
818  C  CA  . LEU A 103 ? 0.447964 0.462435 0.31758  0.0114438   -0.0751886  0.0265248   139  LEU A CA  
819  C  C   . LEU A 103 ? 0.513653 0.512557 0.366707 0.0119221   -0.074913   0.0390423   139  LEU A C   
820  O  O   . LEU A 103 ? 0.441059 0.429414 0.297576 0.0093961   -0.0698641  0.0441197   139  LEU A O   
821  C  CB  . LEU A 103 ? 0.443837 0.465326 0.31024  0.00506133  -0.0681543  0.0210056   139  LEU A CB  
822  C  CG  . LEU A 103 ? 0.47929  0.511697 0.362711 0.00234791  -0.0652309  0.00951432  139  LEU A CG  
823  C  CD1 . LEU A 103 ? 0.495703 0.530612 0.372272 -0.00336918 -0.0579658  0.00645241  139  LEU A CD1 
824  C  CD2 . LEU A 103 ? 0.415468 0.443547 0.315201 0.00106187  -0.0608463  0.00894807  139  LEU A CD2 
825  N  N   . LEU A 104 ? 0.522434 0.51945  0.356412 0.0148493   -0.0802911  0.0441161   140  LEU A N   
826  C  CA  . LEU A 104 ? 0.529384 0.510107 0.345628 0.0142101   -0.0790195  0.0566489   140  LEU A CA  
827  C  C   . LEU A 104 ? 0.479587 0.448443 0.300871 0.0204405   -0.0851435  0.0624393   140  LEU A C   
828  O  O   . LEU A 104 ? 0.501357 0.455002 0.318706 0.0180598   -0.0812127  0.0707651   140  LEU A O   
829  C  CB  . LEU A 104 ? 0.596494 0.578253 0.389541 0.0164397   -0.0839112  0.0605183   140  LEU A CB  
830  C  CG  . LEU A 104 ? 0.667911 0.631967 0.43814  0.0153198   -0.082474   0.0744487   140  LEU A CG  
831  C  CD1 . LEU A 104 ? 0.695346 0.654605 0.461332 0.00505326  -0.0692199  0.0775966   140  LEU A CD1 
832  C  CD2 . LEU A 104 ? 0.690567 0.656881 0.437865 0.0195315   -0.0896237  0.0775135   140  LEU A CD2 
833  N  N   . ASP A 105 ? 0.443483 0.41985  0.27417  0.0283748   -0.0947487  0.0572726   141  ASP A N   
834  C  CA  . ASP A 105 ? 0.461769 0.427258 0.297013 0.0353803   -0.101145   0.0620598   141  ASP A CA  
835  C  C   . ASP A 105 ? 0.452251 0.41411  0.306157 0.0318726   -0.0944598  0.0595734   141  ASP A C   
836  O  O   . ASP A 105 ? 0.47398  0.421323 0.328336 0.0346521   -0.0959917  0.0658655   141  ASP A O   
837  C  CB  . ASP A 105 ? 0.489807 0.4647   0.330211 0.0456167   -0.113576   0.0572077   141  ASP A CB  
838  C  CG  . ASP A 105 ? 0.579523 0.554207 0.398567 0.0514051   -0.122684   0.0619354   141  ASP A CG  
839  O  OD1 . ASP A 105 ? 0.615068 0.577479 0.411692 0.0482707   -0.119817   0.0719024   141  ASP A OD1 
840  O  OD2 . ASP A 105 ? 0.553243 0.541578 0.378013 0.0585629   -0.132297   0.0549179   141  ASP A OD2 
841  N  N   . MET A 106 ? 0.388136 0.36222  0.256569 0.0263771   -0.0877395  0.050467    142  MET A N   
842  C  CA  . MET A 106 ? 0.408737 0.379878 0.2934   0.0237555   -0.0821758  0.0480352   142  MET A CA  
843  C  C   . MET A 106 ? 0.420358 0.377525 0.297381 0.0173429   -0.0742752  0.0558717   142  MET A C   
844  O  O   . MET A 106 ? 0.439784 0.386435 0.322588 0.0174713   -0.0729454  0.0589711   142  MET A O   
845  C  CB  . MET A 106 ? 0.351305 0.337078 0.251772 0.0196735   -0.0769959  0.0372535   142  MET A CB  
846  C  CG  . MET A 106 ? 0.394464 0.39374  0.307969 0.0252583   -0.083781   0.0284882   142  MET A CG  
847  S  SD  . MET A 106 ? 0.38278  0.395369 0.316951 0.0207573   -0.0775589  0.0167821   142  MET A SD  
848  C  CE  . MET A 106 ? 0.405655 0.424077 0.330469 0.0138301   -0.0720792  0.0142079   142  MET A CE  
849  N  N   . GLU A 107 ? 0.444242 0.402299 0.309151 0.0113967   -0.068699   0.0581558   143  GLU A N   
850  C  CA  . GLU A 107 ? 0.491785 0.439776 0.351644 0.00423142  -0.0601107  0.0640035   143  GLU A CA  
851  C  C   . GLU A 107 ? 0.538685 0.468005 0.386716 0.00580368  -0.0626729  0.0751186   143  GLU A C   
852  O  O   . GLU A 107 ? 0.490398 0.409789 0.342386 0.00155094  -0.0574395  0.0784326   143  GLU A O   
853  C  CB  . GLU A 107 ? 0.545095 0.497372 0.391347 -0.00162856 -0.0543423  0.0651144   143  GLU A CB  
854  C  CG  . GLU A 107 ? 0.726636 0.694264 0.584356 -0.00451802 -0.0499183  0.0546106   143  GLU A CG  
855  C  CD  . GLU A 107 ? 0.840306 0.815335 0.687758 -0.00931613 -0.0445882  0.0525665   143  GLU A CD  
856  O  OE1 . GLU A 107 ? 0.975949 0.948781 0.805273 -0.00917863 -0.0462776  0.057585    143  GLU A OE1 
857  O  OE2 . GLU A 107 ? 0.78963  0.772204 0.64754  -0.0130457  -0.0384724  0.0457459   143  GLU A OE2 
858  N  N   . THR A 108 ? 0.489784 0.414594 0.322472 0.0114012   -0.0703895  0.0805737   144  THR A N   
859  C  CA  . THR A 108 ? 0.547014 0.452114 0.364864 0.013725    -0.0737851  0.0921845   144  THR A CA  
860  C  C   . THR A 108 ? 0.588589 0.484277 0.41964  0.0193518   -0.0785478  0.0922146   144  THR A C   
861  O  O   . THR A 108 ? 0.598458 0.477677 0.427819 0.016479    -0.0753947  0.0986507   144  THR A O   
862  C  CB  . THR A 108 ? 0.543345 0.447398 0.341203 0.0195189   -0.0818605  0.0971914   144  THR A CB  
863  O  OG1 . THR A 108 ? 0.536062 0.450393 0.324219 0.0129831   -0.0755371  0.0952386   144  THR A OG1 
864  C  CG2 . THR A 108 ? 0.578074 0.459289 0.357647 0.0223849   -0.0857231  0.110477    144  THR A CG2 
865  N  N   . THR A 109 ? 0.548492 0.455387 0.393796 0.0268259   -0.0855361  0.0840829   145  THR A N   
866  C  CA  . THR A 109 ? 0.512963 0.413588 0.372566 0.0322886   -0.0894206  0.0822039   145  THR A CA  
867  C  C   . THR A 109 ? 0.468813 0.364112 0.339059 0.0248064   -0.0802647  0.0811146   145  THR A C   
868  O  O   . THR A 109 ? 0.445207 0.324582 0.316698 0.0256803   -0.0807044  0.0856327   145  THR A O   
869  C  CB  . THR A 109 ? 0.488693 0.406736 0.364603 0.0392917   -0.0956885  0.071461    145  THR A CB  
870  O  OG1 . THR A 109 ? 0.48412  0.405312 0.347618 0.0459048   -0.104579   0.073701    145  THR A OG1 
871  C  CG2 . THR A 109 ? 0.438757 0.35118  0.328297 0.0462791   -0.100547   0.0691684   145  THR A CG2 
872  N  N   . TYR A 110 ? 0.409486 0.317568 0.287052 0.0177455   -0.0723891  0.0749561   146  TYR A N   
873  C  CA  . TYR A 110 ? 0.461433 0.367427 0.350403 0.0117457   -0.064855   0.0724514   146  TYR A CA  
874  C  C   . TYR A 110 ? 0.521978 0.411275 0.399428 0.0054481   -0.0598292  0.0817748   146  TYR A C   
875  O  O   . TYR A 110 ? 0.535153 0.413563 0.418659 0.0032768   -0.0575181  0.0832233   146  TYR A O   
876  C  CB  . TYR A 110 ? 0.369026 0.292087 0.266585 0.00678414  -0.0586036  0.0642007   146  TYR A CB  
877  C  CG  . TYR A 110 ? 0.383178 0.305965 0.292243 0.00126379  -0.051435   0.0609875   146  TYR A CG  
878  C  CD1 . TYR A 110 ? 0.363872 0.28178  0.268099 -0.00657224 -0.0439897  0.0647011   146  TYR A CD1 
879  C  CD2 . TYR A 110 ? 0.344589 0.272191 0.269298 0.0040155   -0.0522683  0.0540705   146  TYR A CD2 
880  C  CE1 . TYR A 110 ? 0.331539 0.249748 0.246667 -0.0109294  -0.0385703  0.0613917   146  TYR A CE1 
881  C  CE2 . TYR A 110 ? 0.319634 0.247549 0.253469 -0.0005217  -0.0464009  0.050978    146  TYR A CE2 
882  C  CZ  . TYR A 110 ? 0.338024 0.261401 0.267369 -0.00756601 -0.0401593  0.054511    146  TYR A CZ  
883  O  OH  . TYR A 110 ? 0.315247 0.24008  0.254433 -0.0110225  -0.0356913  0.0507073   146  TYR A OH  
884  N  N   A SER A 111 ? 0.546326 0.433711 0.406851 0.00189532  -0.0576838  0.087802    147  SER A N   
885  N  N   B SER A 111 ? 0.528316 0.415863 0.388588 0.00218676  -0.0579977  0.0878051   147  SER A N   
886  C  CA  A SER A 111 ? 0.610402 0.486514 0.462915 -0.0068654  -0.0497905  0.0945029   147  SER A CA  
887  C  CA  B SER A 111 ? 0.559908 0.437208 0.409929 -0.00668289 -0.0500658  0.0948459   147  SER A CA  
888  C  C   A SER A 111 ? 0.579616 0.432814 0.421508 -0.00479921 -0.0535313  0.104693    147  SER A C   
889  C  C   B SER A 111 ? 0.572697 0.426859 0.41137  -0.00525496 -0.0532136  0.105435    147  SER A C   
890  O  O   A SER A 111 ? 0.638376 0.479165 0.479534 -0.0115602  -0.047727   0.109052    147  SER A O   
891  O  O   B SER A 111 ? 0.622805 0.465528 0.45716  -0.0131233  -0.0463894  0.110791    147  SER A O   
892  C  CB  A SER A 111 ? 0.658478 0.541942 0.498104 -0.0129233  -0.0439394  0.0962414   147  SER A CB  
893  C  CB  B SER A 111 ? 0.556027 0.442122 0.392586 -0.0113596  -0.0455864  0.0960342   147  SER A CB  
894  O  OG  A SER A 111 ? 0.690141 0.568237 0.511019 -0.00831064 -0.0500117  0.102901    147  SER A OG  
895  O  OG  B SER A 111 ? 0.536246 0.425136 0.374297 -0.0212818  -0.0349682  0.0954813   147  SER A OG  
896  N  N   . VAL A 112 ? 0.576965 0.424342 0.411747 0.0047829   -0.0635205  0.107947    148  VAL A N   
897  C  CA  . VAL A 112 ? 0.58701  0.410701 0.411319 0.00843491  -0.0683374  0.117782    148  VAL A CA  
898  C  C   . VAL A 112 ? 0.618138 0.43497  0.458614 0.0152048   -0.073818   0.113749    148  VAL A C   
899  O  O   . VAL A 112 ? 0.647111 0.442985 0.480776 0.018934    -0.0781486  0.121051    148  VAL A O   
900  C  CB  . VAL A 112 ? 0.616281 0.432108 0.418839 0.015143    -0.0762777  0.126396    148  VAL A CB  
901  C  CG1 . VAL A 112 ? 0.636701 0.461437 0.422885 0.00894027  -0.0710229  0.129029    148  VAL A CG1 
902  C  CG2 . VAL A 112 ? 0.55313  0.376552 0.362159 0.0284597   -0.0887066  0.121405    148  VAL A CG2 
903  N  N   . ALA A 113 ? 0.555193 0.388254 0.416259 0.0172373   -0.0738222  0.102299    149  ALA A N   
904  C  CA  . ALA A 113 ? 0.528095 0.356991 0.404315 0.0239134   -0.0787041  0.0973075   149  ALA A CA  
905  C  C   . ALA A 113 ? 0.520245 0.330107 0.39827  0.0183734   -0.0741017  0.101119    149  ALA A C   
906  O  O   . ALA A 113 ? 0.513798 0.324947 0.393596 0.00799599  -0.0649492  0.100811    149  ALA A O   
907  C  CB  . ALA A 113 ? 0.4574   0.307917 0.353048 0.0244683   -0.0769625  0.0847849   149  ALA A CB  
908  N  N   . THR A 114 ? 0.602706 0.395575 0.481655 0.0255439   -0.0806812  0.10372     150  THR A N   
909  C  CA  . THR A 114 ? 0.590149 0.364324 0.472907 0.0208477   -0.0770495  0.105794    150  THR A CA  
910  C  C   . THR A 114 ? 0.606486 0.379445 0.505689 0.0296134   -0.0829677  0.0978799   150  THR A C   
911  O  O   . THR A 114 ? 0.515613 0.295802 0.418298 0.0405428   -0.0913182  0.0945027   150  THR A O   
912  C  CB  . THR A 114 ? 0.641221 0.388654 0.504728 0.0172413   -0.0762848  0.119229    150  THR A CB  
913  O  OG1 . THR A 114 ? 0.663835 0.39477  0.520392 0.028712    -0.0866311  0.124394    150  THR A OG1 
914  C  CG2 . THR A 114 ? 0.665383 0.41493  0.510618 0.00970162  -0.070886   0.127126    150  THR A CG2 
915  N  N   . VAL A 115 ? 0.598579 0.36385  0.508175 0.0244811   -0.0783831  0.0941997   151  VAL A N   
916  C  CA  . VAL A 115 ? 0.616589 0.376739 0.540502 0.0313834   -0.0827677  0.0870085   151  VAL A CA  
917  C  C   . VAL A 115 ? 0.63246  0.362835 0.550817 0.0307018   -0.0839577  0.0937473   151  VAL A C   
918  O  O   . VAL A 115 ? 0.642855 0.362521 0.55736  0.0198164   -0.0767301  0.0977204   151  VAL A O   
919  C  CB  . VAL A 115 ? 0.594935 0.372207 0.536587 0.0268466   -0.077098   0.0751299   151  VAL A CB  
920  C  CG1 . VAL A 115 ? 0.562877 0.338271 0.519207 0.0349311   -0.0817635  0.066244    151  VAL A CG1 
921  C  CG2 . VAL A 115 ? 0.537551 0.34088  0.482807 0.0258307   -0.0746721  0.0698186   151  VAL A CG2 
922  N  N   . CYS A 116 ? 0.690706 0.408082 0.610629 0.0422125   -0.0928448  0.093819    152  CYS A N   
923  C  CA  . CYS A 116 ? 0.794125 0.479589 0.705533 0.0430391   -0.0952734  0.102044    152  CYS A CA  
924  C  C   . CYS A 116 ? 0.828513 0.505424 0.755628 0.0487068   -0.0984305  0.0933184   152  CYS A C   
925  O  O   . CYS A 116 ? 0.84126  0.531297 0.780952 0.0591194   -0.104198   0.0840499   152  CYS A O   
926  C  CB  . CYS A 116 ? 0.788718 0.45939  0.683205 0.0530052   -0.104384   0.11265     152  CYS A CB  
927  S  SG  . CYS A 116 ? 1.04664  0.727518 0.920571 0.0474887   -0.101569   0.122514    152  CYS A SG  
928  N  N   . HIS A 117 ? 0.978111 0.631672 0.903901 0.0417677   -0.0946334  0.0964031   153  HIS A N   
929  C  CA  . HIS A 117 ? 0.951163 0.586594 0.88618  0.0487653   -0.0995401  0.0915871   153  HIS A CA  
930  C  C   . HIS A 117 ? 1.063    0.675263 0.986226 0.0614      -0.10985    0.100489    153  HIS A C   
931  O  O   . HIS A 117 ? 1.04472  0.64133  0.948028 0.0599681   -0.110851   0.114189    153  HIS A O   
932  C  CB  . HIS A 117 ? 0.954332 0.571203 0.8915   0.0365683   -0.0921869  0.0918769   153  HIS A CB  
933  C  CG  . HIS A 117 ? 0.935568 0.574007 0.882986 0.0243718   -0.0827658  0.0839631   153  HIS A CG  
934  N  ND1 . HIS A 117 ? 0.979001 0.638614 0.944408 0.0266871   -0.0823139  0.0696351   153  HIS A ND1 
935  C  CD2 . HIS A 117 ? 0.950306 0.592719 0.892444 0.0103442   -0.0737213  0.0881004   153  HIS A CD2 
936  C  CE1 . HIS A 117 ? 0.991157 0.665606 0.961308 0.0147993   -0.0739059  0.0657408   153  HIS A CE1 
937  N  NE2 . HIS A 117 ? 0.957709 0.622827 0.914987 0.00487414  -0.0686284  0.0763343   153  HIS A NE2 
938  N  N   . PRO A 118 ? 1.1552   0.763516 1.09     0.0746146   -0.118011   0.092848    154  PRO A N   
939  C  CA  . PRO A 118 ? 1.13728  0.724879 1.06262  0.0888095   -0.129203   0.100085    154  PRO A CA  
940  C  C   . PRO A 118 ? 1.18313  0.732232 1.09595  0.0823664   -0.126871   0.110803    154  PRO A C   
941  O  O   . PRO A 118 ? 1.23118  0.771669 1.15319  0.0736654   -0.120544   0.105472    154  PRO A O   
942  C  CB  . PRO A 118 ? 1.15469  0.752182 1.1004   0.101977    -0.135838   0.085791    154  PRO A CB  
943  C  CG  . PRO A 118 ? 1.19045  0.795044 1.15172  0.091779    -0.126972   0.0745553   154  PRO A CG  
944  C  CD  . PRO A 118 ? 1.17021  0.792682 1.12704  0.0765058   -0.116718   0.0768782   154  PRO A CD  
945  N  N   . GLN A 119 ? 1.23304  0.75975  1.12399  0.0858703   -0.131613   0.126015    155  GLN A N   
946  C  CA  . GLN A 119 ? 1.3532   0.843885 1.22702  0.076542    -0.127247   0.139403    155  GLN A CA  
947  C  C   . GLN A 119 ? 1.29119  0.78741  1.17072  0.0567908   -0.113266   0.136349    155  GLN A C   
948  O  O   . GLN A 119 ? 1.41807  0.895063 1.30425  0.0503124   -0.109272   0.133669    155  GLN A O   
949  C  CB  . GLN A 119 ? 1.32824  0.783962 1.19979  0.0884776   -0.136386   0.142656    155  GLN A CB  
950  C  CG  . GLN A 119 ? 1.41821  0.854074 1.26727  0.100893    -0.146966   0.157209    155  GLN A CG  
951  C  CD  . GLN A 119 ? 1.53958  0.937307 1.36209  0.0918723   -0.143062   0.175971    155  GLN A CD  
952  O  OE1 . GLN A 119 ? 1.46027  0.827826 1.26547  0.102442    -0.152039   0.187716    155  GLN A OE1 
953  N  NE2 . GLN A 119 ? 1.4572   0.855605 1.27542  0.0721848   -0.129505   0.179346    155  GLN A NE2 
954  N  N   . GLY A 120 ? 1.21472  0.737743 1.09217  0.0476631   -0.106262   0.136151    156  GLY A N   
955  C  CA  . GLY A 120 ? 1.07462  0.608023 0.957415 0.0298677   -0.0935495  0.13305     156  GLY A CA  
956  C  C   . GLY A 120 ? 0.970192 0.520033 0.839482 0.0213714   -0.0874059  0.140307    156  GLY A C   
957  O  O   . GLY A 120 ? 0.941184 0.487499 0.792735 0.0273578   -0.0922425  0.150379    156  GLY A O   
958  N  N   . SER A 121 ? 0.884434 0.452037 0.762198 0.00754548  -0.0768847  0.134686    157  SER A N   
959  C  CA  . SER A 121 ? 0.939046 0.525064 0.807766 -0.00177253 -0.0695506  0.138842    157  SER A CA  
960  C  C   . SER A 121 ? 0.867755 0.484917 0.741382 0.00704101  -0.0741243  0.132407    157  SER A C   
961  O  O   . SER A 121 ? 0.930858 0.562295 0.821005 0.0158456   -0.0792674  0.121121    157  SER A O   
962  C  CB  . SER A 121 ? 0.935225 0.533989 0.815756 -0.0171477  -0.0581513  0.13203     157  SER A CB  
963  O  OG  . SER A 121 ? 1.00845  0.583498 0.893397 -0.024659   -0.0545443  0.132121    157  SER A OG  
964  N  N   . CYS A 122 ? 0.825174 0.453323 0.68485  0.0033998   -0.0711863  0.138944    158  CYS A N   
965  C  CA  . CYS A 122 ? 0.778373 0.437866 0.643639 0.00782844  -0.0727839  0.131985    158  CYS A CA  
966  C  C   . CYS A 122 ? 0.788172 0.467331 0.65912  -0.00548732 -0.0616978  0.127514    158  CYS A C   
967  O  O   . CYS A 122 ? 0.903214 0.573691 0.763797 -0.0170185  -0.0536699  0.134696    158  CYS A O   
968  C  CB  . CYS A 122 ? 0.842949 0.503222 0.690479 0.0162365   -0.0796756  0.140136    158  CYS A CB  
969  S  SG  . CYS A 122 ? 1.04114  0.684712 0.887864 0.034871    -0.0946187  0.141621    158  CYS A SG  
970  N  N   . LEU A 123 ? 0.655537 0.360784 0.543481 -0.00364014 -0.0612606  0.115309    159  LEU A N   
971  C  CA  . LEU A 123 ? 0.616549 0.339959 0.512916 -0.0145593  -0.0519203  0.109398    159  LEU A CA  
972  C  C   . LEU A 123 ? 0.613093 0.360109 0.50589  -0.0125908  -0.0517463  0.10777     159  LEU A C   
973  O  O   . LEU A 123 ? 0.581362 0.340783 0.478417 -0.00269465 -0.0583719  0.103076    159  LEU A O   
974  C  CB  . LEU A 123 ? 0.585655 0.317945 0.503237 -0.01357    -0.0519268  0.096787    159  LEU A CB  
975  C  CG  . LEU A 123 ? 0.577184 0.29318  0.501861 -0.0211925  -0.0479099  0.0951738   159  LEU A CG  
976  C  CD1 . LEU A 123 ? 0.600713 0.286478 0.520037 -0.0168036  -0.0530945  0.101042    159  LEU A CD1 
977  C  CD2 . LEU A 123 ? 0.552133 0.285752 0.496872 -0.0218709  -0.046392   0.08127     159  LEU A CD2 
978  N  N   . GLN A 124 ? 0.616303 0.370629 0.502843 -0.0227061  -0.0435094  0.110499    160  GLN A N   
979  C  CA  . GLN A 124 ? 0.588944 0.366653 0.474795 -0.0220578  -0.0421567  0.106906    160  GLN A CA  
980  C  C   . GLN A 124 ? 0.568437 0.366137 0.472855 -0.0253449  -0.0378471  0.0952357   160  GLN A C   
981  O  O   . GLN A 124 ? 0.596832 0.390214 0.512552 -0.0293827  -0.0352687  0.0908668   160  GLN A O   
982  C  CB  . GLN A 124 ? 0.644918 0.42127  0.515917 -0.0318032  -0.0344534  0.114492    160  GLN A CB  
983  C  CG  . GLN A 124 ? 0.783701 0.542179 0.632243 -0.028788   -0.0382725  0.126973    160  GLN A CG  
984  C  CD  . GLN A 124 ? 0.832647 0.598654 0.666559 -0.0361899  -0.0313968  0.131855    160  GLN A CD  
985  O  OE1 . GLN A 124 ? 0.790161 0.544231 0.614178 -0.0461509  -0.0238535  0.138967    160  GLN A OE1 
986  N  NE2 . GLN A 124 ? 0.903757 0.691148 0.738419 -0.0324877  -0.0327956  0.12658     160  GLN A NE2 
987  N  N   . LEU A 125 ? 0.52879  0.347478 0.435296 -0.0235646  -0.0373009  0.0903816   161  LEU A N   
988  C  CA  . LEU A 125 ? 0.487153 0.324963 0.408839 -0.0253957  -0.0339041  0.080075    161  LEU A CA  
989  C  C   . LEU A 125 ? 0.530367 0.370842 0.455087 -0.0366164  -0.0249438  0.0793511   161  LEU A C   
990  O  O   . LEU A 125 ? 0.518007 0.362008 0.455793 -0.0392801  -0.0229229  0.0727938   161  LEU A O   
991  C  CB  . LEU A 125 ? 0.418618 0.275533 0.341467 -0.0205289  -0.0357538  0.0753199   161  LEU A CB  
992  C  CG  . LEU A 125 ? 0.413657 0.288178 0.349871 -0.022865   -0.0316751  0.065905    161  LEU A CG  
993  C  CD1 . LEU A 125 ? 0.417372 0.291976 0.367071 -0.0181209  -0.0351442  0.0589665   161  LEU A CD1 
994  C  CD2 . LEU A 125 ? 0.398924 0.289986 0.333876 -0.0206736  -0.0314609  0.0625228   161  LEU A CD2 
995  N  N   . GLU A 126 ? 0.554374 0.39298  0.466981 -0.0432923  -0.0196149  0.0858764   162  GLU A N   
996  C  CA  . GLU A 126 ? 0.605595 0.448726 0.521889 -0.0542906  -0.0105617  0.0846535   162  GLU A CA  
997  C  C   . GLU A 126 ? 0.610426 0.433452 0.514847 -0.0618207  -0.00663831 0.0944457   162  GLU A C   
998  O  O   . GLU A 126 ? 0.607836 0.421407 0.4949   -0.0609736  -0.00750344 0.103456    162  GLU A O   
999  C  CB  . GLU A 126 ? 0.695871 0.558116 0.609877 -0.0563853  -0.00605727 0.0819809   162  GLU A CB  
1000 C  CG  . GLU A 126 ? 0.850402 0.729572 0.773974 -0.0488772  -0.0100245  0.0734511   162  GLU A CG  
1001 C  CD  . GLU A 126 ? 1.09656  0.989892 1.01364  -0.0476697  -0.0085153  0.0723899   162  GLU A CD  
1002 O  OE1 . GLU A 126 ? 1.09023  0.99842  1.01564  -0.0502547  -0.00414277 0.065844    162  GLU A OE1 
1003 O  OE2 . GLU A 126 ? 1.12142  1.01147  1.02553  -0.0438153  -0.0119886  0.07741     162  GLU A OE2 
1004 N  N   . PRO A 127 ? 0.607956 0.422476 0.520372 -0.0696128  -0.0023173  0.0933064   163  PRO A N   
1005 C  CA  . PRO A 127 ? 0.549396 0.375305 0.481528 -0.0708081  -0.00161428 0.0824029   163  PRO A CA  
1006 C  C   . PRO A 127 ? 0.543851 0.358381 0.483705 -0.0639203  -0.00889885 0.0793481   163  PRO A C   
1007 O  O   . PRO A 127 ? 0.523675 0.347854 0.478496 -0.0629704  -0.00975799 0.0699511   163  PRO A O   
1008 C  CB  . PRO A 127 ? 0.536921 0.360119 0.472199 -0.084201   0.00758823  0.0830095   163  PRO A CB  
1009 C  CG  . PRO A 127 ? 0.577969 0.376312 0.495866 -0.0883959  0.00918581  0.0955364   163  PRO A CG  
1010 C  CD  . PRO A 127 ? 0.571849 0.364262 0.473893 -0.0777788  0.00190031  0.102585    163  PRO A CD  
1011 N  N   . ASP A 128 ? 0.526429 0.321659 0.455944 -0.0581643  -0.0145797  0.0866733   164  ASP A N   
1012 C  CA  . ASP A 128 ? 0.53741  0.316382 0.47337  -0.0546609  -0.019393   0.0849584   164  ASP A CA  
1013 C  C   . ASP A 128 ? 0.57253  0.364281 0.523011 -0.046087   -0.0249078  0.07416     164  ASP A C   
1014 O  O   . ASP A 128 ? 0.533141 0.324691 0.496217 -0.0485719  -0.0241937  0.0669104   164  ASP A O   
1015 C  CB  . ASP A 128 ? 0.594148 0.348698 0.515581 -0.0499693  -0.0243443  0.0953706   164  ASP A CB  
1016 C  CG  . ASP A 128 ? 0.702991 0.444109 0.606983 -0.0583933  -0.018609   0.107112    164  ASP A CG  
1017 O  OD1 . ASP A 128 ? 0.730007 0.46697  0.636468 -0.0706617  -0.0102904  0.107665    164  ASP A OD1 
1018 O  OD2 . ASP A 128 ? 0.730893 0.466382 0.619111 -0.0525421  -0.0226269  0.115175    164  ASP A OD2 
1019 N  N   . LEU A 129 ? 0.571011 0.374604 0.519709 -0.0368193  -0.0298453  0.0726325   165  LEU A N   
1020 C  CA  . LEU A 129 ? 0.510908 0.326508 0.471819 -0.0289108  -0.0344058  0.0630029   165  LEU A CA  
1021 C  C   . LEU A 129 ? 0.504124 0.338841 0.476288 -0.0332604  -0.0298795  0.0542293   165  LEU A C   
1022 O  O   . LEU A 129 ? 0.440279 0.278846 0.423443 -0.0306291  -0.0317439  0.0461927   165  LEU A O   
1023 C  CB  . LEU A 129 ? 0.477387 0.300132 0.435352 -0.0182754  -0.0407642  0.0627112   165  LEU A CB  
1024 C  CG  . LEU A 129 ? 0.50166  0.306767 0.450755 -0.0110287  -0.0475294  0.0695999   165  LEU A CG  
1025 C  CD1 . LEU A 129 ? 0.567135 0.381648 0.510439 -0.00297197 -0.0526122  0.0709724   165  LEU A CD1 
1026 C  CD2 . LEU A 129 ? 0.536329 0.331809 0.495343 -0.00506412 -0.0523272  0.0642936   165  LEU A CD2 
1027 N  N   . THR A 130 ? 0.478772 0.325575 0.447637 -0.0388689  -0.0244914  0.0554988   166  THR A N   
1028 C  CA  . THR A 130 ? 0.468159 0.33273  0.447031 -0.0423622  -0.0206038  0.0476447   166  THR A CA  
1029 C  C   . THR A 130 ? 0.459176 0.319721 0.447755 -0.0493094  -0.017737   0.0432672   166  THR A C   
1030 O  O   . THR A 130 ? 0.462699 0.334544 0.462011 -0.0485574  -0.018063   0.034662    166  THR A O   
1031 C  CB  . THR A 130 ? 0.50064  0.379299 0.475133 -0.046002   -0.0157198  0.0488889   166  THR A CB  
1032 O  OG1 . THR A 130 ? 0.643951 0.509456 0.60937  -0.0525021  -0.0123539  0.0569213   166  THR A OG1 
1033 C  CG2 . THR A 130 ? 0.500869 0.383037 0.46475  -0.0408649  -0.017848   0.053281    166  THR A CG2 
1034 N  N   . ASN A 131 ? 0.464371 0.309681 0.44882  -0.0566195  -0.014596   0.0489763   167  ASN A N   
1035 C  CA  . ASN A 131 ? 0.508769 0.347457 0.503081 -0.0632028  -0.0126171  0.0444323   167  ASN A CA  
1036 C  C   . ASN A 131 ? 0.465792 0.297071 0.46728  -0.0565064  -0.0187946  0.0386586   167  ASN A C   
1037 O  O   . ASN A 131 ? 0.432795 0.268891 0.44586  -0.0590819  -0.018495   0.0301474   167  ASN A O   
1038 C  CB  . ASN A 131 ? 0.551259 0.370465 0.539036 -0.0722102  -0.00834097 0.0522445   167  ASN A CB  
1039 C  CG  . ASN A 131 ? 0.619734 0.446377 0.60251  -0.0816351  -0.00030685 0.0564259   167  ASN A CG  
1040 O  OD1 . ASN A 131 ? 0.667251 0.514619 0.653487 -0.0814321  0.00195546  0.052244    167  ASN A OD1 
1041 N  ND2 . ASN A 131 ? 0.630318 0.439856 0.603649 -0.0895247  0.00423134  0.0650975   167  ASN A ND2 
1042 N  N   . VAL A 132 ? 0.396115 0.215595 0.39126  -0.0481408  -0.024419   0.0426249   168  VAL A N   
1043 C  CA  . VAL A 132 ? 0.415687 0.230981 0.418889 -0.0413044  -0.0298366  0.0355932   168  VAL A CA  
1044 C  C   . VAL A 132 ? 0.391956 0.228561 0.404375 -0.0374147  -0.0307439  0.0254649   168  VAL A C   
1045 O  O   . VAL A 132 ? 0.392467 0.232427 0.414706 -0.0385232  -0.031122   0.01688     168  VAL A O   
1046 C  CB  . VAL A 132 ? 0.463731 0.263583 0.46109  -0.0319084  -0.036308   0.0398523   168  VAL A CB  
1047 C  CG1 . VAL A 132 ? 0.448407 0.246661 0.455863 -0.0249924  -0.0411047  0.0306781   168  VAL A CG1 
1048 C  CG2 . VAL A 132 ? 0.461157 0.235477 0.449362 -0.0356822  -0.0359864  0.049535    168  VAL A CG2 
1049 N  N   . MET A 133 ? 0.371299 0.221987 0.379738 -0.0332293  -0.0309364  0.0265086   169  MET A N   
1050 C  CA  . MET A 133 ? 0.37985  0.248941 0.393746 -0.0289704  -0.0316352  0.0189805   169  MET A CA  
1051 C  C   . MET A 133 ? 0.39756  0.27818  0.419    -0.0351118  -0.0280838  0.0127538   169  MET A C   
1052 O  O   . MET A 133 ? 0.35934  0.248708 0.387114 -0.0320885  -0.0297451  0.00478036  169  MET A O   
1053 C  CB  . MET A 133 ? 0.35209  0.232105 0.359219 -0.0255756  -0.0312699  0.0225972   169  MET A CB  
1054 C  CG  . MET A 133 ? 0.329829 0.205441 0.33181  -0.0175098  -0.0358974  0.0258083   169  MET A CG  
1055 S  SD  . MET A 133 ? 0.368508 0.238588 0.377797 -0.00941431 -0.0413317  0.0191882   169  MET A SD  
1056 C  CE  . MET A 133 ? 0.323108 0.213701 0.338365 -0.00788208 -0.0394662  0.0103172   169  MET A CE  
1057 N  N   . ALA A 134 ? 0.372725 0.253154 0.393428 -0.0436338  -0.0233335  0.0161288   170  ALA A N   
1058 C  CA  . ALA A 134 ? 0.368706 0.260747 0.397876 -0.0499942  -0.0199964  0.0100937   170  ALA A CA  
1059 C  C   . ALA A 134 ? 0.385228 0.271314 0.424076 -0.0539242  -0.02085    0.00331028  170  ALA A C   
1060 O  O   . ALA A 134 ? 0.365033 0.263744 0.412479 -0.0553857  -0.020879   -0.00493095 170  ALA A O   
1061 C  CB  . ALA A 134 ? 0.32377  0.219553 0.350012 -0.0577142  -0.0141587  0.0150375   170  ALA A CB  
1062 N  N   . THR A 135 ? 0.367193 0.233789 0.404612 -0.0559462  -0.0216138  0.00658696  171  THR A N   
1063 C  CA  . THR A 135 ? 0.414178 0.275375 0.461283 -0.0624965  -0.0208461  0.00028604  171  THR A CA  
1064 C  C   . THR A 135 ? 0.418902 0.267749 0.46876  -0.0566521  -0.0260898  -0.00431893 171  THR A C   
1065 O  O   . THR A 135 ? 0.379204 0.228461 0.438406 -0.0592453  -0.0270703  -0.0130929  171  THR A O   
1066 C  CB  . THR A 135 ? 0.47497  0.324355 0.520778 -0.0736566  -0.0152073  0.0063112   171  THR A CB  
1067 O  OG1 . THR A 135 ? 0.580429 0.407096 0.618482 -0.0705376  -0.0177254  0.0131031   171  THR A OG1 
1068 C  CG2 . THR A 135 ? 0.423998 0.280804 0.462967 -0.0783687  -0.00967124 0.0136401   171  THR A CG2 
1069 N  N   . SER A 136 ? 0.4083   0.247654 0.451051 -0.0482173  -0.029837   0.00021546  172  SER A N   
1070 C  CA  . SER A 136 ? 0.405278 0.234726 0.452086 -0.0421207  -0.034638   -0.00558289 172  SER A CA  
1071 C  C   . SER A 136 ? 0.415922 0.263172 0.469371 -0.0373968  -0.0368119  -0.0166852  172  SER A C   
1072 O  O   . SER A 136 ? 0.411313 0.275544 0.462111 -0.0340794  -0.0363535  -0.0168983  172  SER A O   
1073 C  CB  . SER A 136 ? 0.412065 0.230693 0.451303 -0.0332351  -0.0385047  0.00055736  172  SER A CB  
1074 O  OG  . SER A 136 ? 0.418275 0.22742  0.462632 -0.0271751  -0.0429208  -0.0058665  172  SER A OG  
1075 N  N   . ARG A 137 ? 0.465161 0.30725  0.526356 -0.0372266  -0.0391079  -0.0258215  173  ARG A N   
1076 C  CA  . ARG A 137 ? 0.425286 0.28022  0.491098 -0.031675   -0.0418895  -0.0367257  173  ARG A CA  
1077 C  C   . ARG A 137 ? 0.422603 0.265757 0.489523 -0.0239645  -0.0458663  -0.0405521  173  ARG A C   
1078 O  O   . ARG A 137 ? 0.385994 0.233958 0.457902 -0.0208221  -0.047999   -0.0509418  173  ARG A O   
1079 C  CB  . ARG A 137 ? 0.425236 0.288826 0.499543 -0.0386515  -0.0409751  -0.0457031  173  ARG A CB  
1080 C  CG  . ARG A 137 ? 0.374418 0.252438 0.449072 -0.0448811  -0.0374457  -0.0431294  173  ARG A CG  
1081 C  CD  . ARG A 137 ? 0.405927 0.300139 0.473705 -0.0388924  -0.0373065  -0.0400038  173  ARG A CD  
1082 N  NE  . ARG A 137 ? 0.42444  0.331518 0.495146 -0.0450505  -0.0344056  -0.0398874  173  ARG A NE  
1083 C  CZ  . ARG A 137 ? 0.517423 0.428285 0.583782 -0.0475207  -0.0309273  -0.0320062  173  ARG A CZ  
1084 N  NH1 . ARG A 137 ? 0.542832 0.467163 0.613967 -0.0522555  -0.0287728  -0.0344295  173  ARG A NH1 
1085 N  NH2 . ARG A 137 ? 0.535049 0.4383   0.592678 -0.0447073  -0.0299308  -0.0227094  173  ARG A NH2 
1086 N  N   . LYS A 138 ? 0.442093 0.269744 0.504313 -0.0205186  -0.0471403  -0.0326158  174  LYS A N   
1087 C  CA  . LYS A 138 ? 0.435985 0.254174 0.499649 -0.0114235  -0.0513778  -0.0360877  174  LYS A CA  
1088 C  C   . LYS A 138 ? 0.448571 0.277346 0.50716  -0.00268445 -0.0527354  -0.0328852  174  LYS A C   
1089 O  O   . LYS A 138 ? 0.468622 0.296326 0.520313 -0.00258861 -0.0521053  -0.0230252  174  LYS A O   
1090 C  CB  . LYS A 138 ? 0.461386 0.253613 0.524866 -0.0122453  -0.0531249  -0.0314801  174  LYS A CB  
1091 C  CG  . LYS A 138 ? 0.496798 0.279587 0.566999 -0.0219503  -0.0511954  -0.0366057  174  LYS A CG  
1092 C  CD  . LYS A 138 ? 0.543262 0.297457 0.612707 -0.0240001  -0.0522677  -0.0317198  174  LYS A CD  
1093 C  CE  . LYS A 138 ? 0.57344  0.319406 0.646196 -0.0129806  -0.0575868  -0.0379621  174  LYS A CE  
1094 N  NZ  . LYS A 138 ? 0.678874 0.401918 0.757323 -0.0161957  -0.0587064  -0.0423957  174  LYS A NZ  
1095 N  N   . TYR A 139 ? 0.402573 0.242924 0.464595 0.00396575  -0.0541539  -0.0419208  175  TYR A N   
1096 C  CA  . TYR A 139 ? 0.36775  0.220578 0.427072 0.0115836   -0.0547365  -0.0414786  175  TYR A CA  
1097 C  C   . TYR A 139 ? 0.334912 0.176506 0.391392 0.0169975   -0.0577201  -0.0336873  175  TYR A C   
1098 O  O   . TYR A 139 ? 0.338936 0.188335 0.390506 0.0191322   -0.0574072  -0.0276375  175  TYR A O   
1099 C  CB  . TYR A 139 ? 0.36436  0.224805 0.429143 0.0176881   -0.0558999  -0.0535031  175  TYR A CB  
1100 C  CG  . TYR A 139 ? 0.37032  0.24864  0.432386 0.0226532   -0.0543998  -0.0543994  175  TYR A CG  
1101 C  CD1 . TYR A 139 ? 0.359958 0.238671 0.42329  0.0302208   -0.0564052  -0.0531992  175  TYR A CD1 
1102 C  CD2 . TYR A 139 ? 0.33326  0.227796 0.391725 0.0198193   -0.0510752  -0.0566983  175  TYR A CD2 
1103 C  CE1 . TYR A 139 ? 0.334734 0.230169 0.396607 0.033453    -0.0543028  -0.0545547  175  TYR A CE1 
1104 C  CE2 . TYR A 139 ? 0.332394 0.24116  0.387756 0.0233414   -0.0490083  -0.0569178  175  TYR A CE2 
1105 C  CZ  . TYR A 139 ? 0.34403  0.253767 0.401582 0.0296381   -0.0502116  -0.0562275  175  TYR A CZ  
1106 O  OH  . TYR A 139 ? 0.346289 0.270561 0.401543 0.031803    -0.0474781  -0.0564414  175  TYR A OH  
1107 N  N   . GLU A 140 ? 0.357231 0.180291 0.417042 0.0201364   -0.0612359  -0.0347016  176  GLU A N   
1108 C  CA  . GLU A 140 ? 0.373506 0.185184 0.43074  0.0272314   -0.0654419  -0.0282913  176  GLU A CA  
1109 C  C   . GLU A 140 ? 0.357064 0.159169 0.404782 0.0219226   -0.0645777  -0.0150374  176  GLU A C   
1110 O  O   . GLU A 140 ? 0.370557 0.172514 0.413389 0.0272505   -0.067264   -0.0087131  176  GLU A O   
1111 C  CB  . GLU A 140 ? 0.438679 0.230765 0.50151  0.0325648   -0.069799   -0.0327742  176  GLU A CB  
1112 C  CG  . GLU A 140 ? 0.498294 0.300307 0.570396 0.0396161   -0.0709981  -0.0464628  176  GLU A CG  
1113 C  CD  . GLU A 140 ? 0.633935 0.453422 0.70749  0.0484162   -0.0722339  -0.0484553  176  GLU A CD  
1114 O  OE1 . GLU A 140 ? 0.616537 0.433649 0.686235 0.05291     -0.0751995  -0.0403602  176  GLU A OE1 
1115 O  OE2 . GLU A 140 ? 0.604254 0.440789 0.682585 0.0504527   -0.0700106  -0.058467   176  GLU A OE2 
1116 N  N   . ASP A 141 ? 0.367486 0.162696 0.412763 0.0115723   -0.0608321  -0.011432   177  ASP A N   
1117 C  CA  . ASP A 141 ? 0.398627 0.184165 0.434176 0.00563649  -0.0590153  0.00099264  177  ASP A CA  
1118 C  C   . ASP A 141 ? 0.383769 0.188808 0.413966 0.00389278  -0.0560915  0.00497469  177  ASP A C   
1119 O  O   . ASP A 141 ? 0.379136 0.181893 0.400521 0.00497606  -0.056795   0.0141463   177  ASP A O   
1120 C  CB  . ASP A 141 ? 0.40866  0.181125 0.444435 -0.00544908 -0.0551842  0.00292389  177  ASP A CB  
1121 C  CG  . ASP A 141 ? 0.481334 0.229476 0.520709 -0.00497319 -0.0578006  0.00098675  177  ASP A CG  
1122 O  OD1 . ASP A 141 ? 0.552788 0.290573 0.592205 0.0052198   -0.0634049  0.00078771  177  ASP A OD1 
1123 O  OD2 . ASP A 141 ? 0.48325  0.223669 0.526713 -0.0146795  -0.0543287  -0.0015555  177  ASP A OD2 
1124 N  N   . LEU A 142 ? 0.341153 0.165601 0.376267 0.00225032  -0.0533349  -0.00249302 178  LEU A N   
1125 C  CA  . LEU A 142 ? 0.325304 0.167653 0.356321 0.00163845  -0.0508535  -0.00012599 178  LEU A CA  
1126 C  C   . LEU A 142 ? 0.326497 0.175039 0.355968 0.0107655   -0.0542971  0.00051881  178  LEU A C   
1127 O  O   . LEU A 142 ? 0.316061 0.171142 0.339417 0.011161    -0.0538518  0.00632229  178  LEU A O   
1128 C  CB  . LEU A 142 ? 0.297707 0.155722 0.334203 -0.00104626 -0.0480481  -0.00874905 178  LEU A CB  
1129 C  CG  . LEU A 142 ? 0.320019 0.177828 0.358419 -0.0106239  -0.044439   -0.00939674 178  LEU A CG  
1130 C  CD1 . LEU A 142 ? 0.305435 0.178656 0.349184 -0.0112174  -0.0433663  -0.0190557  178  LEU A CD1 
1131 C  CD2 . LEU A 142 ? 0.294285 0.156548 0.326009 -0.0157984  -0.040982   -0.00104118 178  LEU A CD2 
1132 N  N   . LEU A 143 ? 0.329925 0.177328 0.365791 0.0181235   -0.0577297  -0.0063844  179  LEU A N   
1133 C  CA  . LEU A 143 ? 0.318469 0.174365 0.354799 0.0263931   -0.0607002  -0.00693439 179  LEU A CA  
1134 C  C   . LEU A 143 ? 0.328351 0.171914 0.358255 0.0301784   -0.0650982  0.00222097  179  LEU A C   
1135 O  O   . LEU A 143 ? 0.333795 0.186167 0.360549 0.0336348   -0.0665892  0.0052078   179  LEU A O   
1136 C  CB  . LEU A 143 ? 0.338129 0.197781 0.383784 0.0333425   -0.0627241  -0.0176196  179  LEU A CB  
1137 C  CG  . LEU A 143 ? 0.379738 0.247996 0.429116 0.042652    -0.0661512  -0.0203099  179  LEU A CG  
1138 C  CD1 . LEU A 143 ? 0.371325 0.259296 0.418139 0.0403924   -0.0624631  -0.0196754  179  LEU A CD1 
1139 C  CD2 . LEU A 143 ? 0.418608 0.288956 0.477792 0.0493206   -0.0677753  -0.0313862  179  LEU A CD2 
1140 N  N   . TRP A 144 ? 0.372694 0.195034 0.400522 0.0300916   -0.0676677  0.00627358  180  TRP A N   
1141 C  CA  . TRP A 144 ? 0.403403 0.211055 0.422786 0.0337915   -0.0721786  0.0159857   180  TRP A CA  
1142 C  C   . TRP A 144 ? 0.395066 0.209209 0.403758 0.0280713   -0.0692032  0.0248139   180  TRP A C   
1143 O  O   . TRP A 144 ? 0.370208 0.187117 0.372942 0.0328715   -0.0726709  0.0297282   180  TRP A O   
1144 C  CB  . TRP A 144 ? 0.445323 0.226851 0.463016 0.031894    -0.0736124  0.0193379   180  TRP A CB  
1145 C  CG  . TRP A 144 ? 0.540323 0.302998 0.546257 0.0345584   -0.0777439  0.0311194   180  TRP A CG  
1146 C  CD1 . TRP A 144 ? 0.662265 0.412804 0.667149 0.0454939   -0.085438   0.0330106   180  TRP A CD1 
1147 C  CD2 . TRP A 144 ? 0.558145 0.313377 0.550615 0.0267342   -0.0745543  0.0427092   180  TRP A CD2 
1148 N  NE1 . TRP A 144 ? 0.74311  0.477767 0.733441 0.0452018   -0.0877326  0.0457219   180  TRP A NE1 
1149 C  CE2 . TRP A 144 ? 0.673832 0.411263 0.655894 0.0333821   -0.080712   0.0519132   180  TRP A CE2 
1150 C  CE3 . TRP A 144 ? 0.572636 0.334466 0.560842 0.015104    -0.0671496  0.0458623   180  TRP A CE3 
1151 C  CZ2 . TRP A 144 ? 0.69963  0.425688 0.665543 0.0282374   -0.0792232  0.0645955   180  TRP A CZ2 
1152 C  CZ3 . TRP A 144 ? 0.646612 0.398262 0.620606 0.00975962  -0.0651754  0.0575534   180  TRP A CZ3 
1153 C  CH2 . TRP A 144 ? 0.684493 0.418427 0.646644 0.0160061   -0.070925   0.0670533   180  TRP A CH2 
1154 N  N   . ALA A 145 ? 0.385602 0.204588 0.39272  0.0180965   -0.0628214  0.0255675   181  ALA A N   
1155 C  CA  . ALA A 145 ? 0.392585 0.216016 0.389844 0.0120423   -0.0593528  0.0334011   181  ALA A CA  
1156 C  C   . ALA A 145 ? 0.381115 0.226101 0.379456 0.0147425   -0.0587973  0.0302499   181  ALA A C   
1157 O  O   . ALA A 145 ? 0.341471 0.190274 0.331729 0.0154905   -0.059636   0.0359702   181  ALA A O   
1158 C  CB  . ALA A 145 ? 0.376751 0.200482 0.374351 0.00095322  -0.0526425  0.0335757   181  ALA A CB  
1159 N  N   . TRP A 146 ? 0.357743 0.216283 0.365561 0.0155795   -0.057014   0.0209034   182  TRP A N   
1160 C  CA  . TRP A 146 ? 0.356108 0.234154 0.365839 0.0172424   -0.0555332  0.0170004   182  TRP A CA  
1161 C  C   . TRP A 146 ? 0.336649 0.218559 0.346809 0.0257757   -0.0608307  0.0169118   182  TRP A C   
1162 O  O   . TRP A 146 ? 0.308035 0.199389 0.313883 0.0256064   -0.0605409  0.0193916   182  TRP A O   
1163 C  CB  . TRP A 146 ? 0.307128 0.196142 0.325413 0.0168665   -0.052742   0.00745015  182  TRP A CB  
1164 C  CG  . TRP A 146 ? 0.311149 0.217901 0.330216 0.0171548   -0.0500959  0.00410392  182  TRP A CG  
1165 C  CD1 . TRP A 146 ? 0.319423 0.23468  0.335629 0.0114527   -0.0454164  0.00461394  182  TRP A CD1 
1166 C  CD2 . TRP A 146 ? 0.291708 0.209314 0.314839 0.0229788   -0.0516089  -0.00033045 182  TRP A CD2 
1167 N  NE1 . TRP A 146 ? 0.289201 0.217587 0.306189 0.0131748   -0.0439162  0.0016158   182  TRP A NE1 
1168 C  CE2 . TRP A 146 ? 0.292968 0.223659 0.314488 0.0195998   -0.047244   -0.00163677 182  TRP A CE2 
1169 C  CE3 . TRP A 146 ? 0.300535 0.218446 0.329403 0.0306442   -0.05602    -0.00399469 182  TRP A CE3 
1170 C  CZ2 . TRP A 146 ? 0.269955 0.21333  0.294832 0.0224711   -0.0465187  -0.00596716 182  TRP A CZ2 
1171 C  CZ3 . TRP A 146 ? 0.277487 0.210284 0.310913 0.0337163   -0.0553581  -0.00905805 182  TRP A CZ3 
1172 C  CH2 . TRP A 146 ? 0.280046 0.224827 0.311171 0.0291465   -0.0504651  -0.00966872 182  TRP A CH2 
1173 N  N   . GLU A 147 ? 0.334618 0.209979 0.35092  0.0331087   -0.0656092  0.0130837   183  GLU A N   
1174 C  CA  . GLU A 147 ? 0.357426 0.236988 0.377185 0.0424673   -0.0714651  0.0110683   183  GLU A CA  
1175 C  C   . GLU A 147 ? 0.426167 0.295686 0.435451 0.044882    -0.076317   0.0208046   183  GLU A C   
1176 O  O   . GLU A 147 ? 0.387772 0.267478 0.395158 0.0485979   -0.079244   0.0216764   183  GLU A O   
1177 C  CB  . GLU A 147 ? 0.374615 0.250799 0.404783 0.0499922   -0.0749652  0.00322504  183  GLU A CB  
1178 C  CG  . GLU A 147 ? 0.470172 0.355056 0.506777 0.0602215   -0.0808175  -0.00091751 183  GLU A CG  
1179 C  CD  . GLU A 147 ? 0.618411 0.526608 0.659581 0.0603177   -0.078564   -0.00596595 183  GLU A CD  
1180 O  OE1 . GLU A 147 ? 0.583222 0.501752 0.626264 0.0540804   -0.0718163  -0.0101016  183  GLU A OE1 
1181 O  OE2 . GLU A 147 ? 0.581372 0.498217 0.624731 0.0662498   -0.0831862  -0.00655608 183  GLU A OE2 
1182 N  N   . GLY A 148 ? 0.449303 0.298771 0.45093  0.042029    -0.0768313  0.0282157   184  GLY A N   
1183 C  CA  . GLY A 148 ? 0.436844 0.273255 0.425983 0.0443101   -0.081384   0.0385258   184  GLY A CA  
1184 C  C   . GLY A 148 ? 0.396153 0.243309 0.375893 0.0394099   -0.0786467  0.0434677   184  GLY A C   
1185 O  O   . GLY A 148 ? 0.447196 0.295853 0.420166 0.0445289   -0.0837743  0.0474817   184  GLY A O   
1186 N  N   . TRP A 149 ? 0.377239 0.232474 0.356912 0.0301827   -0.071083   0.0424415   185  TRP A N   
1187 C  CA  . TRP A 149 ? 0.405741 0.27099  0.377146 0.0253708   -0.0679285  0.0461682   185  TRP A CA  
1188 C  C   . TRP A 149 ? 0.390122 0.274003 0.365661 0.0304016   -0.0704863  0.0409451   185  TRP A C   
1189 O  O   . TRP A 149 ? 0.388459 0.276706 0.355813 0.0314015   -0.0726557  0.0447287   185  TRP A O   
1190 C  CB  . TRP A 149 ? 0.364887 0.235441 0.337345 0.01546     -0.0596404  0.0449021   185  TRP A CB  
1191 C  CG  . TRP A 149 ? 0.372846 0.253192 0.337377 0.0108145   -0.0561479  0.0479938   185  TRP A CG  
1192 C  CD1 . TRP A 149 ? 0.373839 0.271092 0.342404 0.00866952  -0.0525334  0.0427587   185  TRP A CD1 
1193 C  CD2 . TRP A 149 ? 0.359519 0.233113 0.309883 0.00855559  -0.0563479  0.0567723   185  TRP A CD2 
1194 N  NE1 . TRP A 149 ? 0.334725 0.236288 0.293922 0.00507997  -0.0503176  0.0468967   185  TRP A NE1 
1195 C  CE2 . TRP A 149 ? 0.372578 0.260803 0.320309 0.00504132  -0.0526114  0.055298    185  TRP A CE2 
1196 C  CE3 . TRP A 149 ? 0.389251 0.245423 0.327915 0.00939807  -0.0593308  0.0657818   185  TRP A CE3 
1197 C  CZ2 . TRP A 149 ? 0.390574 0.277772 0.324876 0.00207542  -0.0514419  0.0617598   185  TRP A CZ2 
1198 C  CZ3 . TRP A 149 ? 0.431433 0.286161 0.355388 0.0064566   -0.0582302  0.0731098   185  TRP A CZ3 
1199 C  CH2 . TRP A 149 ? 0.401425 0.272607 0.323552 0.00314325  -0.0545214  0.0705728   185  TRP A CH2 
1200 N  N   . ARG A 150 ? 0.369541 0.264574 0.357811 0.0330235   -0.0698428  0.0317543   186  ARG A N   
1201 C  CA  . ARG A 150 ? 0.356429 0.268432 0.351459 0.0377966   -0.072047   0.0254073   186  ARG A CA  
1202 C  C   . ARG A 150 ? 0.379111 0.28857  0.373525 0.0472531   -0.0808485  0.0266918   186  ARG A C   
1203 O  O   . ARG A 150 ? 0.374484 0.29487  0.367052 0.0491233   -0.0833218  0.0262091   186  ARG A O   
1204 C  CB  . ARG A 150 ? 0.335359 0.259765 0.342683 0.0372187   -0.0680151  0.0157344   186  ARG A CB  
1205 C  CG  . ARG A 150 ? 0.338395 0.268639 0.342884 0.0285584   -0.0605154  0.0158351   186  ARG A CG  
1206 C  CD  . ARG A 150 ? 0.324612 0.2592   0.336888 0.0267003   -0.0561572  0.00914266  186  ARG A CD  
1207 N  NE  . ARG A 150 ? 0.322533 0.260667 0.331203 0.0194083   -0.0500583  0.0100198   186  ARG A NE  
1208 C  CZ  . ARG A 150 ? 0.351881 0.281884 0.355927 0.0140464   -0.0474263  0.0140642   186  ARG A CZ  
1209 N  NH1 . ARG A 150 ? 0.317248 0.253036 0.319679 0.00883902  -0.0425432  0.0135418   186  ARG A NH1 
1210 N  NH2 . ARG A 150 ? 0.334278 0.250541 0.335681 0.0136809   -0.0494666  0.0183762   186  ARG A NH2 
1211 N  N   . ASP A 151 ? 0.398301 0.293217 0.394019 0.0533464   -0.0859021  0.0281607   187  ASP A N   
1212 C  CA  . ASP A 151 ? 0.403473 0.296046 0.399538 0.0639273   -0.0952213  0.0287625   187  ASP A CA  
1213 C  C   . ASP A 151 ? 0.405892 0.292701 0.386    0.0639374   -0.0989338  0.0384838   187  ASP A C   
1214 O  O   . ASP A 151 ? 0.370773 0.265221 0.350123 0.0709479   -0.1058     0.0378207   187  ASP A O   
1215 C  CB  . ASP A 151 ? 0.477327 0.352499 0.476939 0.0703471   -0.0996198  0.0288987   187  ASP A CB  
1216 C  CG  . ASP A 151 ? 0.52063  0.403454 0.536482 0.0727357   -0.0975315  0.0177042   187  ASP A CG  
1217 O  OD1 . ASP A 151 ? 0.470388 0.37202  0.493755 0.069114    -0.0924289  0.0105851   187  ASP A OD1 
1218 O  OD2 . ASP A 151 ? 0.563599 0.433109 0.584035 0.078079    -0.100727   0.0159484   187  ASP A OD2 
1219 N  N   . LYS A 152 ? 0.401597 0.276154 0.368873 0.055854    -0.0942267  0.0470208   188  LYS A N   
1220 C  CA  . LYS A 152 ? 0.457774 0.322557 0.407821 0.0564655   -0.0979027  0.0572115   188  LYS A CA  
1221 C  C   . LYS A 152 ? 0.522412 0.402654 0.466727 0.0504597   -0.0938891  0.0571023   188  LYS A C   
1222 O  O   . LYS A 152 ? 0.574415 0.458057 0.509494 0.0543194   -0.0992259  0.0603019   188  LYS A O   
1223 C  CB  . LYS A 152 ? 0.489901 0.330048 0.427298 0.051667    -0.0955972  0.0676031   188  LYS A CB  
1224 C  CG  . LYS A 152 ? 0.544445 0.363964 0.483953 0.058378    -0.100932   0.0696495   188  LYS A CG  
1225 C  CD  . LYS A 152 ? 0.597638 0.413246 0.538833 0.0724708   -0.112434   0.069056    188  LYS A CD  
1226 C  CE  . LYS A 152 ? 0.648813 0.452743 0.572693 0.0793259   -0.120869   0.0791594   188  LYS A CE  
1227 N  NZ  . LYS A 152 ? 0.69157  0.480572 0.5971   0.0691972   -0.114777   0.0905072   188  LYS A NZ  
1228 N  N   . ALA A 153 ? 0.425249 0.31267  0.373261 0.0410777   -0.0847814  0.0541811   189  ALA A N   
1229 C  CA  . ALA A 153 ? 0.429072 0.329374 0.371578 0.0355405   -0.0807844  0.0539061   189  ALA A CA  
1230 C  C   . ALA A 153 ? 0.409597 0.330826 0.364273 0.0380444   -0.0815157  0.043897    189  ALA A C   
1231 O  O   . ALA A 153 ? 0.404352 0.335855 0.355174 0.0398328   -0.0846205  0.0428707   189  ALA A O   
1232 C  CB  . ALA A 153 ? 0.437472 0.336328 0.37792  0.0251878   -0.0713435  0.0553552   189  ALA A CB  
1233 N  N   . GLY A 154 ? 0.320678 0.248277 0.289342 0.0372466   -0.0779996  0.0363928   190  GLY A N   
1234 C  CA  . GLY A 154 ? 0.316136 0.262738 0.295418 0.0375103   -0.0766914  0.0273668   190  GLY A CA  
1235 C  C   . GLY A 154 ? 0.362187 0.317229 0.346177 0.0462083   -0.0850576  0.0236755   190  GLY A C   
1236 O  O   . GLY A 154 ? 0.363957 0.331791 0.347743 0.0460847   -0.0864362  0.0206813   190  GLY A O   
1237 N  N   . ARG A 155 ? 0.341399 0.289434 0.329486 0.0543794   -0.0915234  0.0236561   191  ARG A N   
1238 C  CA  . ARG A 155 ? 0.354173 0.31403  0.348925 0.0629696   -0.0995894  0.01851     191  ARG A CA  
1239 C  C   . ARG A 155 ? 0.388492 0.349092 0.370203 0.0650571   -0.105509   0.0238428   191  ARG A C   
1240 O  O   . ARG A 155 ? 0.376301 0.351435 0.362662 0.0699738   -0.11133    0.0186151   191  ARG A O   
1241 C  CB  . ARG A 155 ? 0.355224 0.306153 0.355628 0.0729764   -0.106788   0.0180143   191  ARG A CB  
1242 C  CG  . ARG A 155 ? 0.348117 0.303025 0.362674 0.0709788   -0.100781   0.0102975   191  ARG A CG  
1243 C  CD  . ARG A 155 ? 0.42054  0.357955 0.435346 0.0780288   -0.105746   0.0130809   191  ARG A CD  
1244 N  NE  . ARG A 155 ? 0.532866 0.480978 0.562074 0.0880889   -0.111907   0.00433835  191  ARG A NE  
1245 C  CZ  . ARG A 155 ? 0.73582  0.6864   0.778494 0.0914882   -0.110615   -0.00360235 191  ARG A CZ  
1246 N  NH1 . ARG A 155 ? 0.895644 0.863962 0.952865 0.0986043   -0.114404   -0.0134115  191  ARG A NH1 
1247 N  NH2 . ARG A 155 ? 0.608922 0.547088 0.651593 0.0877129   -0.1055     -0.00303675 191  ARG A NH2 
1248 N  N   . ALA A 156 ? 0.401806 0.345757 0.366645 0.0623473   -0.105097   0.0344272   192  ALA A N   
1249 C  CA  . ALA A 156 ? 0.432388 0.375192 0.382587 0.0656983   -0.111724   0.0401681   192  ALA A CA  
1250 C  C   . ALA A 156 ? 0.406392 0.364165 0.353125 0.0587992   -0.107413   0.0371083   192  ALA A C   
1251 O  O   . ALA A 156 ? 0.407338 0.370322 0.345018 0.0618751   -0.113254   0.0384242   192  ALA A O   
1252 C  CB  . ALA A 156 ? 0.4252   0.34391  0.357171 0.0659965   -0.113344   0.0529994   192  ALA A CB  
1253 N  N   . ILE A 157 ? 0.345015 0.310086 0.299356 0.0502085   -0.097821   0.0322556   193  ILE A N   
1254 C  CA  . ILE A 157 ? 0.330691 0.309795 0.284905 0.0440243   -0.0933552  0.0276063   193  ILE A CA  
1255 C  C   . ILE A 157 ? 0.33871  0.337503 0.307424 0.047293    -0.0967401  0.0167264   193  ILE A C   
1256 O  O   . ILE A 157 ? 0.333618 0.344171 0.300223 0.045184    -0.0974096  0.0129672   193  ILE A O   
1257 C  CB  . ILE A 157 ? 0.338792 0.31583  0.294842 0.0345543   -0.0824337  0.027282    193  ILE A CB  
1258 C  CG1 . ILE A 157 ? 0.359342 0.319555 0.302344 0.0306727   -0.0790039  0.0369754   193  ILE A CG1 
1259 C  CG2 . ILE A 157 ? 0.332997 0.322895 0.289405 0.0284963   -0.07761    0.0221181   193  ILE A CG2 
1260 C  CD1 . ILE A 157 ? 0.385854 0.341667 0.310843 0.0308277   -0.0821579  0.0440396   193  ILE A CD1 
1261 N  N   . LEU A 158 ? 0.325273 0.328471 0.309469 0.0513616   -0.0977603  0.0107589   194  LEU A N   
1262 C  CA  . LEU A 158 ? 0.315881 0.338558 0.316428 0.0533958   -0.0993333  -0.00044802 194  LEU A CA  
1263 C  C   . LEU A 158 ? 0.351438 0.386464 0.350164 0.057965    -0.107758   -0.00358635 194  LEU A C   
1264 O  O   . LEU A 158 ? 0.353273 0.405268 0.361277 0.0544902   -0.105932   -0.0123954  194  LEU A O   
1265 C  CB  . LEU A 158 ? 0.303405 0.328218 0.318659 0.059771    -0.101666   -0.00550224 194  LEU A CB  
1266 C  CG  . LEU A 158 ? 0.313695 0.360146 0.347542 0.0599173   -0.100784   -0.0179998  194  LEU A CG  
1267 C  CD1 . LEU A 158 ? 0.2463   0.300291 0.284448 0.0489307   -0.0897659  -0.0226535  194  LEU A CD1 
1268 C  CD2 . LEU A 158 ? 0.303304 0.351212 0.350914 0.0662947   -0.102284   -0.0229317  194  LEU A CD2 
1269 N  N   . GLN A 159 ? 0.336943 0.363948 0.324625 0.0661241   -0.117422   0.00287283  195  GLN A N   
1270 C  CA  . GLN A 159 ? 0.36758  0.407025 0.3531   0.0718454   -0.126935   -0.00044605 195  GLN A CA  
1271 C  C   . GLN A 159 ? 0.367547 0.416167 0.346411 0.0637867   -0.122947   -0.00287501 195  GLN A C   
1272 O  O   . GLN A 159 ? 0.358472 0.424295 0.343462 0.0654408   -0.127784   -0.0109198  195  GLN A O   
1273 C  CB  . GLN A 159 ? 0.394573 0.420657 0.363996 0.0812138   -0.137469   0.00906233  195  GLN A CB  
1274 C  CG  . GLN A 159 ? 0.438329 0.444398 0.385173 0.0762562   -0.133567   0.0218092   195  GLN A CG  
1275 C  CD  . GLN A 159 ? 0.568534 0.555116 0.500344 0.0847631   -0.141758   0.0328532   195  GLN A CD  
1276 O  OE1 . GLN A 159 ? 0.677446 0.6436   0.60149  0.0826769   -0.137754   0.0417213   195  GLN A OE1 
1277 N  NE2 . GLN A 159 ? 0.461588 0.453961 0.388117 0.0941375   -0.153439   0.0325218   195  GLN A NE2 
1278 N  N   . PHE A 160 ? 0.34492  0.38247  0.311832 0.0553663   -0.114439   0.0034252   196  PHE A N   
1279 C  CA  . PHE A 160 ? 0.349388 0.392249 0.307528 0.0482649   -0.110464   0.00224658  196  PHE A CA  
1280 C  C   . PHE A 160 ? 0.316281 0.369947 0.287866 0.0396928   -0.101285   -0.00675573 196  PHE A C   
1281 O  O   . PHE A 160 ? 0.277389 0.340175 0.247172 0.0351575   -0.0997026  -0.0116463  196  PHE A O   
1282 C  CB  . PHE A 160 ? 0.366702 0.392007 0.305641 0.0439873   -0.105657   0.0134746   196  PHE A CB  
1283 C  CG  . PHE A 160 ? 0.405919 0.417343 0.327753 0.0508641   -0.113385   0.0240474   196  PHE A CG  
1284 C  CD1 . PHE A 160 ? 0.460186 0.477508 0.372057 0.0572223   -0.123334   0.0242623   196  PHE A CD1 
1285 C  CD2 . PHE A 160 ? 0.399282 0.391426 0.315382 0.0511575   -0.111029   0.0334195   196  PHE A CD2 
1286 C  CE1 . PHE A 160 ? 0.479696 0.482409 0.373959 0.0641291   -0.130839   0.0348974   196  PHE A CE1 
1287 C  CE2 . PHE A 160 ? 0.458899 0.435973 0.358837 0.0571901   -0.117828   0.0436335   196  PHE A CE2 
1288 C  CZ  . PHE A 160 ? 0.513637 0.495372 0.401637 0.0637274   -0.127615   0.0449235   196  PHE A CZ  
1289 N  N   . TYR A 161 ? 0.310362 0.360795 0.293303 0.0368384   -0.094468   -0.0082109  197  TYR A N   
1290 C  CA  . TYR A 161 ? 0.284178 0.337782 0.273252 0.0279658   -0.0844349  -0.0127394  197  TYR A CA  
1291 C  C   . TYR A 161 ? 0.276332 0.348005 0.277098 0.025474    -0.0847289  -0.0239673  197  TYR A C   
1292 O  O   . TYR A 161 ? 0.282325 0.357052 0.280987 0.0189266   -0.0798425  -0.0270954  197  TYR A O   
1293 C  CB  . TYR A 161 ? 0.287385 0.333987 0.284464 0.0260802   -0.0779028  -0.0118597  197  TYR A CB  
1294 C  CG  . TYR A 161 ? 0.292865 0.333633 0.285848 0.0177072   -0.0681612  -0.0103726  197  TYR A CG  
1295 C  CD1 . TYR A 161 ? 0.2852   0.314686 0.263949 0.0151889   -0.0657625  -0.00264464 197  TYR A CD1 
1296 C  CD2 . TYR A 161 ? 0.269875 0.316224 0.273055 0.0123889   -0.0611551  -0.0166955  197  TYR A CD2 
1297 C  CE1 . TYR A 161 ? 0.236917 0.262102 0.213322 0.00866763  -0.0575132  -0.00198199 197  TYR A CE1 
1298 C  CE2 . TYR A 161 ? 0.231859 0.272348 0.230739 0.0059613   -0.0533295  -0.0153152  197  TYR A CE2 
1299 C  CZ  . TYR A 161 ? 0.25169  0.282083 0.237973 0.00456883  -0.0517912  -0.0082776  197  TYR A CZ  
1300 O  OH  . TYR A 161 ? 0.213104 0.238998 0.196737 -0.00083467 -0.0445441  -0.0078464  197  TYR A OH  
1301 N  N   . PRO A 162 ? 0.30335  0.388048 0.318539 0.0299523   -0.0896405  -0.0314114  198  PRO A N   
1302 C  CA  . PRO A 162 ? 0.294267 0.39665  0.322248 0.0258687   -0.0885369  -0.0428734  198  PRO A CA  
1303 C  C   . PRO A 162 ? 0.295845 0.403835 0.314675 0.0239559   -0.0919982  -0.044935   198  PRO A C   
1304 O  O   . PRO A 162 ? 0.274852 0.388422 0.297002 0.0163835   -0.0864784  -0.0510509  198  PRO A O   
1305 C  CB  . PRO A 162 ? 0.291488 0.407044 0.334499 0.0337747   -0.0961078  -0.0492086  198  PRO A CB  
1306 C  CG  . PRO A 162 ? 0.297632 0.399999 0.340042 0.0381504   -0.0949945  -0.0424301  198  PRO A CG  
1307 C  CD  . PRO A 162 ? 0.294642 0.378256 0.316358 0.0385782   -0.095626   -0.0302834  198  PRO A CD  
1308 N  N   . LYS A 163 ? 0.295233 0.400328 0.300965 0.0307243   -0.100969   -0.0395092  199  LYS A N   
1309 C  CA  . LYS A 163 ? 0.316305 0.427545 0.311957 0.0294232   -0.104745   -0.0418767  199  LYS A CA  
1310 C  C   . LYS A 163 ? 0.29616  0.396495 0.278826 0.0217528   -0.096267   -0.0374421  199  LYS A C   
1311 O  O   . LYS A 163 ? 0.287501 0.395266 0.269154 0.0169333   -0.0947582  -0.0437771  199  LYS A O   
1312 C  CB  . LYS A 163 ? 0.3726   0.485629 0.357283 0.0392197   -0.117412   -0.0382026  199  LYS A CB  
1313 C  CG  . LYS A 163 ? 0.445606 0.567868 0.419921 0.0386144   -0.12256    -0.042204   199  LYS A CG  
1314 C  CD  . LYS A 163 ? 0.45803  0.600879 0.444698 0.0344849   -0.123879   -0.0565428  199  LYS A CD  
1315 C  CE  . LYS A 163 ? 0.505041 0.665864 0.512362 0.0393279   -0.130552   -0.0663862  199  LYS A CE  
1316 N  NZ  . LYS A 163 ? 0.473053 0.653685 0.484618 0.0397746   -0.138057   -0.0777103  199  LYS A NZ  
1317 N  N   . TYR A 164 ? 0.284174 0.367894 0.258272 0.0206326   -0.0907967  -0.0276642  200  TYR A N   
1318 C  CA  . TYR A 164 ? 0.288058 0.363042 0.253084 0.0135704   -0.0821594  -0.0246243  200  TYR A CA  
1319 C  C   . TYR A 164 ? 0.273307 0.353436 0.251089 0.00612268  -0.0740641  -0.0329369  200  TYR A C   
1320 O  O   . TYR A 164 ? 0.266534 0.349104 0.240589 0.00127873  -0.0709308  -0.0370031  200  TYR A O   
1321 C  CB  . TYR A 164 ? 0.278167 0.337194 0.238158 0.0139003   -0.077833   -0.0147017  200  TYR A CB  
1322 C  CG  . TYR A 164 ? 0.282543 0.333641 0.240712 0.00673462  -0.0674676  -0.0130948  200  TYR A CG  
1323 C  CD1 . TYR A 164 ? 0.295876 0.343579 0.241331 0.00323491  -0.0642298  -0.0108536  200  TYR A CD1 
1324 C  CD2 . TYR A 164 ? 0.275755 0.323309 0.244824 0.00414157  -0.0612927  -0.014109   200  TYR A CD2 
1325 C  CE1 . TYR A 164 ? 0.324464 0.365524 0.269241 -0.00206202 -0.0555422  -0.00967346 200  TYR A CE1 
1326 C  CE2 . TYR A 164 ? 0.278704 0.319    0.245853 -0.00107148 -0.0530662  -0.0124569  200  TYR A CE2 
1327 C  CZ  . TYR A 164 ? 0.303076 0.340132 0.258671 -0.00375113 -0.0505442  -0.0101391  200  TYR A CZ  
1328 O  OH  . TYR A 164 ? 0.311551 0.342496 0.267072 -0.00778353 -0.0431731  -0.00916236 200  TYR A OH  
1329 N  N   . VAL A 165 ? 0.269859 0.351035 0.261882 0.00524481  -0.0706043  -0.0355377  201  VAL A N   
1330 C  CA  . VAL A 165 ? 0.256176 0.341088 0.259028 -0.00204446 -0.0628411  -0.0429064  201  VAL A CA  
1331 C  C   . VAL A 165 ? 0.285498 0.383814 0.293033 -0.00517108 -0.0650406  -0.0530036  201  VAL A C   
1332 O  O   . VAL A 165 ? 0.273336 0.370051 0.280036 -0.0116482  -0.0592244  -0.0569099  201  VAL A O   
1333 C  CB  . VAL A 165 ? 0.29242  0.379711 0.309538 -0.00153137 -0.0604528  -0.0450724  201  VAL A CB  
1334 C  CG1 . VAL A 165 ? 0.224048 0.316558 0.253059 -0.00905471 -0.0529178  -0.0531526  201  VAL A CG1 
1335 C  CG2 . VAL A 165 ? 0.22174  0.294603 0.233315 0.00055686  -0.0574448  -0.0357371  201  VAL A CG2 
1336 N  N   . GLU A 166 ? 0.266521 0.378087 0.278992 -0.00015319 -0.0740353  -0.0576826  202  GLU A N   
1337 C  CA  . GLU A 166 ? 0.283589 0.409914 0.302885 -0.00319938 -0.0766445  -0.0686374  202  GLU A CA  
1338 C  C   . GLU A 166 ? 0.309948 0.43356  0.314806 -0.00563773 -0.0768716  -0.0686902  202  GLU A C   
1339 O  O   . GLU A 166 ? 0.271391 0.399105 0.280497 -0.0124975  -0.0726348  -0.0768989  202  GLU A O   
1340 C  CB  . GLU A 166 ? 0.362733 0.503992 0.39093  0.00407123  -0.0869016  -0.0730948  202  GLU A CB  
1341 C  CG  . GLU A 166 ? 0.450223 0.607885 0.481269 0.00328621  -0.0931947  -0.0834571  202  GLU A CG  
1342 C  CD  . GLU A 166 ? 0.57042  0.746691 0.614205 0.00984654  -0.1033     -0.0908165  202  GLU A CD  
1343 O  OE1 . GLU A 166 ? 0.616105 0.798352 0.675679 0.011277    -0.102281   -0.093687   202  GLU A OE1 
1344 O  OE2 . GLU A 166 ? 0.594518 0.78009  0.631923 0.0132691   -0.112057   -0.0944793  202  GLU A OE2 
1345 N  N   . LEU A 167 ? 0.284558 0.400815 0.272183 -0.00043347 -0.0812914  -0.059879   203  LEU A N   
1346 C  CA  . LEU A 167 ? 0.31727  0.431956 0.289763 -0.00208592 -0.0816274  -0.0597598  203  LEU A CA  
1347 C  C   . LEU A 167 ? 0.283611 0.38683  0.252461 -0.00901324 -0.0708078  -0.0582846  203  LEU A C   
1348 O  O   . LEU A 167 ? 0.25604  0.361883 0.221334 -0.01326    -0.0685594  -0.0644145  203  LEU A O   
1349 C  CB  . LEU A 167 ? 0.32426  0.433468 0.278966 0.00513911  -0.0885725  -0.0498306  203  LEU A CB  
1350 C  CG  . LEU A 167 ? 0.356263 0.477627 0.311565 0.0129745   -0.101051   -0.0524377  203  LEU A CG  
1351 C  CD1 . LEU A 167 ? 0.376836 0.488091 0.314982 0.0209029   -0.107493   -0.04011    203  LEU A CD1 
1352 C  CD2 . LEU A 167 ? 0.366477 0.503873 0.32156  0.0121476   -0.106841   -0.0634145  203  LEU A CD2 
1353 N  N   . ILE A 168 ? 0.262834 0.353719 0.232584 -0.00963179 -0.0646469  -0.0507706  204  ILE A N   
1354 C  CA  . ILE A 168 ? 0.266169 0.346653 0.232256 -0.0148289  -0.0554976  -0.0492175  204  ILE A CA  
1355 C  C   . ILE A 168 ? 0.289463 0.371988 0.268093 -0.0213615  -0.0494942  -0.0583166  204  ILE A C   
1356 O  O   . ILE A 168 ? 0.273648 0.352057 0.248871 -0.0256038  -0.044397   -0.0616756  204  ILE A O   
1357 C  CB  . ILE A 168 ? 0.275948 0.34328  0.238921 -0.0135891  -0.051033   -0.0391048  204  ILE A CB  
1358 C  CG1 . ILE A 168 ? 0.246239 0.30448  0.203138 -0.0172905  -0.0434151  -0.0371499  204  ILE A CG1 
1359 C  CG2 . ILE A 168 ? 0.274518 0.340521 0.25085  -0.0134925  -0.0490594  -0.0389557  204  ILE A CG2 
1360 C  CD1 . ILE A 168 ? 0.246597 0.294143 0.198291 -0.0154781  -0.0407354  -0.0272272  204  ILE A CD1 
1361 N  N   . ASN A 169 ? 0.256637 0.344493 0.249634 -0.0223228  -0.0494623  -0.0621863  205  ASN A N   
1362 C  CA  . ASN A 169 ? 0.235662 0.326825 0.240918 -0.0292412  -0.0442864  -0.071515   205  ASN A CA  
1363 C  C   . ASN A 169 ? 0.246371 0.348041 0.252074 -0.0319832  -0.0476235  -0.0816309  205  ASN A C   
1364 O  O   . ASN A 169 ? 0.228885 0.327354 0.23729  -0.038334   -0.0420588  -0.0880139  205  ASN A O   
1365 C  CB  . ASN A 169 ? 0.213344 0.311336 0.233982 -0.0300788  -0.0438365  -0.0747214  205  ASN A CB  
1366 C  CG  . ASN A 169 ? 0.231644 0.317912 0.253626 -0.030455   -0.0373297  -0.0677261  205  ASN A CG  
1367 O  OD1 . ASN A 169 ? 0.201534 0.274479 0.215137 -0.0313956  -0.0322504  -0.0619515  205  ASN A OD1 
1368 N  ND2 . ASN A 169 ? 0.240618 0.332421 0.272759 -0.0289383  -0.0379442  -0.0682581  205  ASN A ND2 
1369 N  N   . GLN A 170 ? 0.256958 0.370921 0.259942 -0.0269816  -0.057135   -0.0835686  206  GLN A N   
1370 C  CA  . GLN A 170 ? 0.27597  0.401629 0.279074 -0.0291381  -0.0613648  -0.0939847  206  GLN A CA  
1371 C  C   . GLN A 170 ? 0.2981   0.415619 0.287513 -0.0312701  -0.0578598  -0.0936286  206  GLN A C   
1372 O  O   . GLN A 170 ? 0.277826 0.396949 0.27133  -0.0371198  -0.0546046  -0.102928   206  GLN A O   
1373 C  CB  . GLN A 170 ? 0.324003 0.46573  0.327306 -0.0230081  -0.0730066  -0.0972791  206  GLN A CB  
1374 C  CG  . GLN A 170 ? 0.382748 0.53809  0.385821 -0.0250833  -0.0781986  -0.109066   206  GLN A CG  
1375 C  CD  . GLN A 170 ? 0.44377  0.61246  0.441127 -0.0166285  -0.09109    -0.10924    206  GLN A CD  
1376 O  OE1 . GLN A 170 ? 0.510952 0.678291 0.506683 -0.00951033 -0.0958151  -0.101122   206  GLN A OE1 
1377 N  NE2 . GLN A 170 ? 0.40467  0.585503 0.397595 -0.0164122  -0.0976148  -0.117959   206  GLN A NE2 
1378 N  N   . ALA A 171 ? 0.318413 0.426343 0.292712 -0.027177   -0.057387   -0.0832846  207  ALA A N   
1379 C  CA  . ALA A 171 ? 0.331737 0.43337  0.294136 -0.0292272  -0.0532611  -0.0837891  207  ALA A CA  
1380 C  C   . ALA A 171 ? 0.309477 0.40043  0.279087 -0.0352255  -0.0435105  -0.0866899  207  ALA A C   
1381 O  O   . ALA A 171 ? 0.290173 0.380094 0.257756 -0.0388293  -0.040528   -0.0939603  207  ALA A O   
1382 C  CB  . ALA A 171 ? 0.312963 0.407307 0.25887  -0.0247118  -0.0535248  -0.0726743  207  ALA A CB  
1383 N  N   . ALA A 172 ? 0.286942 0.369521 0.264287 -0.0358373  -0.0389138  -0.081112   208  ALA A N   
1384 C  CA  . ALA A 172 ? 0.272535 0.34346  0.254866 -0.0406465  -0.0302878  -0.0826408  208  ALA A CA  
1385 C  C   . ALA A 172 ? 0.27951  0.354117 0.272799 -0.0472957  -0.0282255  -0.0944402  208  ALA A C   
1386 O  O   . ALA A 172 ? 0.277735 0.344589 0.269981 -0.0509898  -0.0232284  -0.0991443  208  ALA A O   
1387 C  CB  . ALA A 172 ? 0.248398 0.31013  0.234288 -0.039397   -0.0265108  -0.073979   208  ALA A CB  
1388 N  N   . ARG A 173 ? 0.256771 0.343445 0.26122  -0.0490143  -0.0320197  -0.100121   209  ARG A N   
1389 C  CA  . ARG A 173 ? 0.275855 0.367034 0.291737 -0.056466   -0.0297413  -0.112136   209  ARG A CA  
1390 C  C   . ARG A 173 ? 0.322676 0.419618 0.332943 -0.0577133  -0.0328386  -0.121266   209  ARG A C   
1391 O  O   . ARG A 173 ? 0.310084 0.401802 0.324048 -0.0637924  -0.0281692  -0.129378   209  ARG A O   
1392 C  CB  . ARG A 173 ? 0.26573  0.372891 0.29599  -0.0580892  -0.0339437  -0.118334   209  ARG A CB  
1393 C  CG  . ARG A 173 ? 0.267787 0.370671 0.305497 -0.0580273  -0.0299319  -0.111743   209  ARG A CG  
1394 C  CD  . ARG A 173 ? 0.246418 0.365945 0.301206 -0.0612754  -0.0321631  -0.120392   209  ARG A CD  
1395 N  NE  . ARG A 173 ? 0.277119 0.415404 0.333342 -0.0556244  -0.0431827  -0.124731   209  ARG A NE  
1396 C  CZ  . ARG A 173 ? 0.291376 0.434786 0.343999 -0.0465962  -0.0502407  -0.117396   209  ARG A CZ  
1397 N  NH1 . ARG A 173 ? 0.252142 0.384245 0.301265 -0.0433981  -0.0466966  -0.106665   209  ARG A NH1 
1398 N  NH2 . ARG A 173 ? 0.258117 0.416973 0.310373 -0.0407666  -0.0608768  -0.121017   209  ARG A NH2 
1399 N  N   . LEU A 174 ? 0.337536 0.444825 0.33794  -0.0518516  -0.0409024  -0.120122   210  LEU A N   
1400 C  CA  . LEU A 174 ? 0.325921 0.438117 0.317728 -0.0522357  -0.0436222  -0.127754   210  LEU A CA  
1401 C  C   . LEU A 174 ? 0.302402 0.399783 0.285588 -0.0534167  -0.0363788  -0.126174   210  LEU A C   
1402 O  O   . LEU A 174 ? 0.330902 0.430468 0.310947 -0.0557397  -0.0363388  -0.135192   210  LEU A O   
1403 C  CB  . LEU A 174 ? 0.335403 0.460236 0.315318 -0.0456233  -0.0533672  -0.126097   210  LEU A CB  
1404 C  CG  . LEU A 174 ? 0.354951 0.497118 0.344748 -0.0440604  -0.0620774  -0.131348   210  LEU A CG  
1405 C  CD1 . LEU A 174 ? 0.389416 0.537603 0.365524 -0.0351349  -0.0711208  -0.12317    210  LEU A CD1 
1406 C  CD2 . LEU A 174 ? 0.343235 0.49801  0.340255 -0.0493583  -0.0648658  -0.147526   210  LEU A CD2 
1407 N  N   . ASN A 175 ? 0.293751 0.37714  0.273609 -0.0515557  -0.0306585  -0.115929   211  ASN A N   
1408 C  CA  . ASN A 175 ? 0.313585 0.384458 0.287128 -0.0521403  -0.0242609  -0.115989   211  ASN A CA  
1409 C  C   . ASN A 175 ? 0.339993 0.396658 0.323684 -0.0574206  -0.0165449  -0.118566   211  ASN A C   
1410 O  O   . ASN A 175 ? 0.301547 0.344973 0.281187 -0.0564772  -0.0110228  -0.116027   211  ASN A O   
1411 C  CB  . ASN A 175 ? 0.318473 0.383428 0.280878 -0.0464227  -0.0230103  -0.103952   211  ASN A CB  
1412 C  CG  . ASN A 175 ? 0.344153 0.419253 0.2927   -0.0424126  -0.0284729  -0.102708   211  ASN A CG  
1413 O  OD1 . ASN A 175 ? 0.375793 0.45453  0.317705 -0.0431896  -0.0284628  -0.110088   211  ASN A OD1 
1414 N  ND2 . ASN A 175 ? 0.32028  0.399835 0.263521 -0.0381675  -0.0333227  -0.093858   211  ASN A ND2 
1415 N  N   . GLY A 176 ? 0.298779 0.357924 0.295229 -0.0625578  -0.0160783  -0.122742   212  GLY A N   
1416 C  CA  . GLY A 176 ? 0.304564 0.350362 0.309718 -0.0689063  -0.00876937 -0.126114   212  GLY A CA  
1417 C  C   . GLY A 176 ? 0.287501 0.322142 0.295168 -0.0682579  -0.00410713 -0.115571   212  GLY A C   
1418 O  O   . GLY A 176 ? 0.275867 0.297142 0.288292 -0.0730873  0.00235589  -0.116422   212  GLY A O   
1419 N  N   . TYR A 177 ? 0.270842 0.309606 0.274557 -0.0624729  -0.00713731 -0.105683   213  TYR A N   
1420 C  CA  . TYR A 177 ? 0.271755 0.301633 0.277471 -0.0615436  -0.00336466 -0.0964423  213  TYR A CA  
1421 C  C   . TYR A 177 ? 0.274957 0.314415 0.29196  -0.0649395  -0.00429379 -0.0984049  213  TYR A C   
1422 O  O   . TYR A 177 ? 0.261746 0.316143 0.284723 -0.0666609  -0.00908284 -0.106142   213  TYR A O   
1423 C  CB  . TYR A 177 ? 0.283319 0.310275 0.280039 -0.054272   -0.00488319 -0.0853564  213  TYR A CB  
1424 C  CG  . TYR A 177 ? 0.316858 0.33555  0.304116 -0.0512013  -0.00300149 -0.0839241  213  TYR A CG  
1425 C  CD1 . TYR A 177 ? 0.312179 0.315114 0.297831 -0.0507253  0.00268876  -0.0804498  213  TYR A CD1 
1426 C  CD2 . TYR A 177 ? 0.350931 0.378109 0.33079  -0.0486563  -0.00689571 -0.0866989  213  TYR A CD2 
1427 C  CE1 . TYR A 177 ? 0.319813 0.317002 0.298457 -0.0471683  0.00416464  -0.0799215  213  TYR A CE1 
1428 C  CE2 . TYR A 177 ? 0.339613 0.360917 0.311657 -0.0459074  -0.00448397 -0.0859854  213  TYR A CE2 
1429 C  CZ  . TYR A 177 ? 0.318872 0.325774 0.291376 -0.0450888  0.0009956   -0.0831603  213  TYR A CZ  
1430 O  OH  . TYR A 177 ? 0.358892 0.361807 0.325441 -0.0418696  0.00313954  -0.0835562  213  TYR A OH  
1431 N  N   . VAL A 178 ? 0.293463 0.325846 0.313658 -0.0656558  1.701e-05   -0.0920898  214  VAL A N   
1432 C  CA  . VAL A 178 ? 0.312381 0.356063 0.344107 -0.0687479  -0.00051568 -0.0949034  214  VAL A CA  
1433 C  C   . VAL A 178 ? 0.307811 0.363721 0.338948 -0.0615849  -0.00758807 -0.0898733  214  VAL A C   
1434 O  O   . VAL A 178 ? 0.31716  0.388329 0.357878 -0.0619245  -0.0115897  -0.0946837  214  VAL A O   
1435 C  CB  . VAL A 178 ? 0.353808 0.387827 0.39118  -0.0745315  0.00769985  -0.0931996  214  VAL A CB  
1436 C  CG1 . VAL A 178 ? 0.438586 0.464437 0.480108 -0.0833276  0.0136975   -0.100909   214  VAL A CG1 
1437 C  CG2 . VAL A 178 ? 0.366563 0.384004 0.394102 -0.0705197  0.0114634   -0.0822917  214  VAL A CG2 
1438 N  N   . ASP A 179 ? 0.269661 0.31865  0.290243 -0.0550495  -0.0090908  -0.0804471  215  ASP A N   
1439 C  CA  . ASP A 179 ? 0.26493  0.321428 0.283013 -0.0481952  -0.01535    -0.0745556  215  ASP A CA  
1440 C  C   . ASP A 179 ? 0.237076 0.283838 0.242215 -0.0431687  -0.0155902  -0.0660302  215  ASP A C   
1441 O  O   . ASP A 179 ? 0.256912 0.293157 0.256865 -0.044648   -0.0111412  -0.0655593  215  ASP A O   
1442 C  CB  . ASP A 179 ? 0.237443 0.295827 0.26331  -0.0478091  -0.0138367  -0.0716811  215  ASP A CB  
1443 C  CG  . ASP A 179 ? 0.264986 0.307634 0.287197 -0.0491113  -0.00644369 -0.0653259  215  ASP A CG  
1444 O  OD1 . ASP A 179 ? 0.255476 0.28925  0.268287 -0.0445928  -0.00665531 -0.0576055  215  ASP A OD1 
1445 O  OD2 . ASP A 179 ? 0.273957 0.313527 0.302565 -0.0548229  -0.00043999 -0.0682471  215  ASP A OD2 
1446 N  N   . ALA A 180 ? 0.22759  0.278198 0.228072 -0.0373026  -0.0208613  -0.0599007  216  ALA A N   
1447 C  CA  . ALA A 180 ? 0.269889 0.314163 0.258807 -0.0333403  -0.021506   -0.0527975  216  ALA A CA  
1448 C  C   . ALA A 180 ? 0.278424 0.309677 0.265591 -0.0333565  -0.0154908  -0.0469719  216  ALA A C   
1449 O  O   . ALA A 180 ? 0.290059 0.31498  0.269859 -0.0322103  -0.0134707  -0.0441296  216  ALA A O   
1450 C  CB  . ALA A 180 ? 0.262843 0.312345 0.247861 -0.0277726  -0.0280572  -0.0470898  216  ALA A CB  
1451 N  N   . GLY A 181 ? 0.276534 0.304882 0.270654 -0.0345929  -0.0126803  -0.0458773  217  GLY A N   
1452 C  CA  . GLY A 181 ? 0.280503 0.296739 0.272248 -0.0342558  -0.00756467 -0.040643   217  GLY A CA  
1453 C  C   . GLY A 181 ? 0.28574  0.292385 0.275121 -0.0372678  -0.00238243 -0.0434112  217  GLY A C   
1454 O  O   . GLY A 181 ? 0.317208 0.315252 0.301149 -0.0350093  -0.00022413 -0.0394025  217  GLY A O   
1455 N  N   . ASP A 182 ? 0.235521 0.243677 0.229828 -0.0422578  -0.00054379 -0.0506926  218  ASP A N   
1456 C  CA  . ASP A 182 ? 0.269657 0.267934 0.262257 -0.0453758  0.00397006  -0.0544863  218  ASP A CA  
1457 C  C   . ASP A 182 ? 0.315935 0.314665 0.301532 -0.0424443  0.00209955  -0.0554616  218  ASP A C   
1458 O  O   . ASP A 182 ? 0.269791 0.258107 0.251205 -0.04095    0.00528318  -0.0540712  218  ASP A O   
1459 C  CB  . ASP A 182 ? 0.324756 0.327067 0.325364 -0.0520509  0.00555727  -0.063047   218  ASP A CB  
1460 C  CG  . ASP A 182 ? 0.353325 0.344635 0.35319  -0.0562709  0.0101749   -0.0683467  218  ASP A CG  
1461 O  OD1 . ASP A 182 ? 0.35048  0.327203 0.345269 -0.0546774  0.0140535   -0.063705   218  ASP A OD1 
1462 O  OD2 . ASP A 182 ? 0.382085 0.379649 0.386498 -0.0607051  0.0093199   -0.0773968  218  ASP A OD2 
1463 N  N   A SER A 183 ? 0.274999 0.286032 0.258931 -0.0412131  -0.00312498 -0.0577868  219  SER A N   
1464 N  N   B SER A 183 ? 0.278169 0.289069 0.261961 -0.0411039  -0.00311185 -0.0575932  219  SER A N   
1465 C  CA  A SER A 183 ? 0.293399 0.305976 0.26926  -0.0385084  -0.00440585 -0.0579571  219  SER A CA  
1466 C  CA  B SER A 183 ? 0.290034 0.302056 0.265846 -0.038524   -0.00415881 -0.0579567  219  SER A CA  
1467 C  C   A SER A 183 ? 0.316728 0.323498 0.287188 -0.0341318  -0.00304805 -0.0498234  219  SER A C   
1468 C  C   B SER A 183 ? 0.312688 0.319319 0.283068 -0.0340834  -0.00299158 -0.0497583  219  SER A C   
1469 O  O   A SER A 183 ? 0.306462 0.308591 0.272984 -0.0327887  -0.00046394 -0.0505667  219  SER A O   
1470 O  O   B SER A 183 ? 0.303604 0.305773 0.269944 -0.0326702  -0.00047747 -0.0504034  219  SER A O   
1471 C  CB  A SER A 183 ? 0.276381 0.302375 0.249378 -0.0378367  -0.0103587  -0.0608325  219  SER A CB  
1472 C  CB  B SER A 183 ? 0.272284 0.297483 0.245111 -0.0380542  -0.00985582 -0.0613509  219  SER A CB  
1473 O  OG  A SER A 183 ? 0.29581  0.323613 0.259145 -0.0353536  -0.0110472  -0.0598727  219  SER A OG  
1474 O  OG  B SER A 183 ? 0.261063 0.291851 0.231965 -0.0345854  -0.0143067  -0.0546697  219  SER A OG  
1475 N  N   . TRP A 184 ? 0.337118 0.344289 0.308435 -0.0318989  -0.00459222 -0.0428216  220  TRP A N   
1476 C  CA  . TRP A 184 ? 0.361294 0.363771 0.328797 -0.0283769  -0.00341912 -0.0358961  220  TRP A CA  
1477 C  C   . TRP A 184 ? 0.314022 0.30525  0.282647 -0.0277808  0.00125992  -0.0354868  220  TRP A C   
1478 O  O   . TRP A 184 ? 0.293911 0.282603 0.259382 -0.0253916  0.00287552  -0.0347305  220  TRP A O   
1479 C  CB  . TRP A 184 ? 0.306608 0.311236 0.275094 -0.0262568  -0.00628027 -0.0292454  220  TRP A CB  
1480 C  CG  . TRP A 184 ? 0.26134  0.274537 0.226373 -0.0250774  -0.0114345  -0.0276865  220  TRP A CG  
1481 C  CD1 . TRP A 184 ? 0.284245 0.304049 0.244033 -0.0255517  -0.0138918  -0.0309673  220  TRP A CD1 
1482 C  CD2 . TRP A 184 ? 0.261786 0.276523 0.226737 -0.0225763  -0.0150362  -0.0218699  220  TRP A CD2 
1483 N  NE1 . TRP A 184 ? 0.292677 0.317464 0.248279 -0.023342   -0.0189602  -0.0269553  220  TRP A NE1 
1484 C  CE2 . TRP A 184 ? 0.266994 0.288202 0.225927 -0.0214088  -0.019763   -0.021263   220  TRP A CE2 
1485 C  CE3 . TRP A 184 ? 0.211766 0.222469 0.180473 -0.0209774  -0.0148826  -0.0173316  220  TRP A CE3 
1486 C  CZ2 . TRP A 184 ? 0.283908 0.306132 0.240681 -0.0184586  -0.024432   -0.0157797  220  TRP A CZ2 
1487 C  CZ3 . TRP A 184 ? 0.225911 0.238222 0.193096 -0.0183816  -0.0191043  -0.0126286  220  TRP A CZ3 
1488 C  CH2 . TRP A 184 ? 0.224994 0.242376 0.186804 -0.0170075  -0.0239426  -0.0117445  220  TRP A CH2 
1489 N  N   . ARG A 185 ? 0.262356 0.24699  0.235199 -0.0297648  0.00344444  -0.0360023  221  ARG A N   
1490 C  CA  . ARG A 185 ? 0.269899 0.241935 0.242246 -0.0289923  0.00739239  -0.0349372  221  ARG A CA  
1491 C  C   . ARG A 185 ? 0.28308  0.250172 0.253432 -0.0288373  0.0094559   -0.0402766  221  ARG A C   
1492 O  O   . ARG A 185 ? 0.291911 0.251573 0.260061 -0.0251802  0.011053    -0.0388636  221  ARG A O   
1493 C  CB  . ARG A 185 ? 0.242859 0.209299 0.218678 -0.0325474  0.00982981  -0.0349821  221  ARG A CB  
1494 C  CG  . ARG A 185 ? 0.244482 0.214856 0.222112 -0.031573   0.00837295  -0.0299741  221  ARG A CG  
1495 C  CD  . ARG A 185 ? 0.252344 0.216345 0.232246 -0.0351956  0.0122378   -0.0299795  221  ARG A CD  
1496 N  NE  . ARG A 185 ? 0.265482 0.232459 0.250854 -0.041327   0.0141731   -0.0362053  221  ARG A NE  
1497 C  CZ  . ARG A 185 ? 0.263693 0.242526 0.255823 -0.0438134  0.0123578   -0.0392513  221  ARG A CZ  
1498 N  NH1 . ARG A 185 ? 0.246781 0.228937 0.244775 -0.0496566  0.0142117   -0.0460174  221  ARG A NH1 
1499 N  NH2 . ARG A 185 ? 0.255743 0.243597 0.249405 -0.0402685  0.00823105  -0.0363056  221  ARG A NH2 
1500 N  N   . SER A 186 ? 0.264499 0.238137 0.235323 -0.0316423  0.00849086  -0.0467788  222  SER A N   
1501 C  CA  . SER A 186 ? 0.305509 0.273242 0.275367 -0.0321391  0.0108898   -0.0534127  222  SER A CA  
1502 C  C   . SER A 186 ? 0.27486  0.244581 0.240807 -0.0272204  0.0109358   -0.0526975  222  SER A C   
1503 O  O   . SER A 186 ? 0.248332 0.211423 0.213714 -0.025351   0.0131635   -0.056658   222  SER A O   
1504 C  CB  . SER A 186 ? 0.332017 0.3067   0.303401 -0.0364817  0.00978761  -0.0617334  222  SER A CB  
1505 O  OG  . SER A 186 ? 0.337656 0.324938 0.304672 -0.0347347  0.00658317  -0.0627139  222  SER A OG  
1506 N  N   . MET A 187 ? 0.257582 0.235697 0.221464 -0.0250191  0.00880666  -0.0474087  223  MET A N   
1507 C  CA  . MET A 187 ? 0.311197 0.293422 0.272264 -0.0214438  0.00949208  -0.0468634  223  MET A CA  
1508 C  C   . MET A 187 ? 0.297973 0.27101  0.260929 -0.0170781  0.0116246   -0.0453837  223  MET A C   
1509 O  O   . MET A 187 ? 0.345501 0.321811 0.308042 -0.0139987  0.0128307   -0.0473627  223  MET A O   
1510 C  CB  . MET A 187 ? 0.31171  0.302933 0.270434 -0.0209406  0.00720924  -0.0404692  223  MET A CB  
1511 C  CG  . MET A 187 ? 0.360298 0.361275 0.314749 -0.0235736  0.00443082  -0.0415586  223  MET A CG  
1512 S  SD  . MET A 187 ? 0.443756 0.45193  0.393506 -0.0229075  0.00202721  -0.0334329  223  MET A SD  
1513 C  CE  . MET A 187 ? 0.361708 0.365242 0.316646 -0.0223076  -0.00031445 -0.0269417  223  MET A CE  
1514 N  N   . TYR A 188 ? 0.283609 0.247122 0.248258 -0.0164646  0.011734    -0.0412644  224  TYR A N   
1515 C  CA  . TYR A 188 ? 0.334933 0.288029 0.300062 -0.0117539  0.0128291   -0.039419   224  TYR A CA  
1516 C  C   . TYR A 188 ? 0.332274 0.272615 0.297112 -0.0109478  0.0150772   -0.0445677  224  TYR A C   
1517 O  O   . TYR A 188 ? 0.336826 0.268476 0.301393 -0.00549258 0.0154023   -0.0437969  224  TYR A O   
1518 C  CB  . TYR A 188 ? 0.285566 0.232805 0.250437 -0.0114546  0.0120155   -0.0326204  224  TYR A CB  
1519 C  CG  . TYR A 188 ? 0.283859 0.242023 0.249572 -0.0108727  0.00974848  -0.0281647  224  TYR A CG  
1520 C  CD1 . TYR A 188 ? 0.304922 0.271174 0.270903 -0.0147524  0.00818244  -0.0267669  224  TYR A CD1 
1521 C  CD2 . TYR A 188 ? 0.344937 0.305491 0.311675 -0.00631315 0.00894842  -0.0259099  224  TYR A CD2 
1522 C  CE1 . TYR A 188 ? 0.306442 0.280737 0.272645 -0.014138   0.00618558  -0.0226515  224  TYR A CE1 
1523 C  CE2 . TYR A 188 ? 0.369414 0.339511 0.337394 -0.00662828 0.00733467  -0.0223861  224  TYR A CE2 
1524 C  CZ  . TYR A 188 ? 0.335053 0.310858 0.302237 -0.0106201  0.00609247  -0.0203879  224  TYR A CZ  
1525 O  OH  . TYR A 188 ? 0.31236  0.295276 0.28014  -0.0110288  0.00460751  -0.0166193  224  TYR A OH  
1526 N  N   . GLU A 189 ? 0.319551 0.258039 0.284651 -0.0159823  0.0162602   -0.0498277  225  GLU A N   
1527 C  CA  . GLU A 189 ? 0.363934 0.288284 0.328972 -0.0164266  0.0187451   -0.0551594  225  GLU A CA  
1528 C  C   . GLU A 189 ? 0.359543 0.266326 0.32236  -0.0138782  0.0199604   -0.0498783  225  GLU A C   
1529 O  O   . GLU A 189 ? 0.398731 0.29355  0.360215 -0.00900209 0.0207023   -0.0513825  225  GLU A O   
1530 C  CB  . GLU A 189 ? 0.364345 0.288339 0.329711 -0.0117599  0.0194317   -0.0615816  225  GLU A CB  
1531 C  CG  . GLU A 189 ? 0.445769 0.386814 0.411175 -0.0131036  0.0187361   -0.0665555  225  GLU A CG  
1532 C  CD  . GLU A 189 ? 0.520365 0.463076 0.486242 -0.00947604 0.0202367   -0.0748843  225  GLU A CD  
1533 O  OE1 . GLU A 189 ? 0.492538 0.431409 0.460049 -0.00296473 0.0209571   -0.0762507  225  GLU A OE1 
1534 O  OE2 . GLU A 189 ? 0.597668 0.54733  0.562403 -0.013539   0.0204496   -0.0812186  225  GLU A OE2 
1535 N  N   . THR A 190 ? 0.336875 0.242617 0.298522 -0.0158651  0.019728    -0.0432228  226  THR A N   
1536 C  CA  . THR A 190 ? 0.340186 0.230876 0.297484 -0.0129004  0.0205338   -0.0369988  226  THR A CA  
1537 C  C   . THR A 190 ? 0.325322 0.211369 0.281922 -0.0202015  0.0231804   -0.0348279  226  THR A C   
1538 O  O   . THR A 190 ? 0.336464 0.23215  0.294423 -0.0225453  0.0223094   -0.031476   226  THR A O   
1539 C  CB  . THR A 190 ? 0.36527  0.263142 0.321728 -0.00742351 0.0174855   -0.0308789  226  THR A CB  
1540 O  OG1 . THR A 190 ? 0.409706 0.312469 0.368126 -0.00122221 0.0157614   -0.0338574  226  THR A OG1 
1541 C  CG2 . THR A 190 ? 0.339452 0.223644 0.290057 -0.00405837 0.0175366   -0.0243065  226  THR A CG2 
1542 N  N   . PRO A 191 ? 0.354559 0.226643 0.310108 -0.0246525  0.0268407   -0.0378656  227  PRO A N   
1543 C  CA  . PRO A 191 ? 0.376676 0.245858 0.332976 -0.0328907  0.0303827   -0.0370474  227  PRO A CA  
1544 C  C   . PRO A 191 ? 0.363869 0.229236 0.315351 -0.0324088  0.0313185   -0.0287027  227  PRO A C   
1545 O  O   . PRO A 191 ? 0.383957 0.255358 0.338126 -0.0385623  0.0333886   -0.0282703  227  PRO A O   
1546 C  CB  . PRO A 191 ? 0.389533 0.240508 0.344397 -0.0368404  0.0345589   -0.0411739  227  PRO A CB  
1547 C  CG  . PRO A 191 ? 0.40261  0.250614 0.357707 -0.0307304  0.0324364   -0.0462774  227  PRO A CG  
1548 C  CD  . PRO A 191 ? 0.342197 0.201497 0.296641 -0.0221085  0.0279056   -0.0428148  227  PRO A CD  
1549 N  N   . SER A 192 ? 0.369252 0.225211 0.313741 -0.024872   0.0297028   -0.0227207  228  SER A N   
1550 C  CA  . SER A 192 ? 0.386558 0.23861  0.324677 -0.0232241  0.0299843   -0.0149567  228  SER A CA  
1551 C  C   . SER A 192 ? 0.343087 0.21329  0.284601 -0.0194579  0.0255033   -0.0129152  228  SER A C   
1552 O  O   . SER A 192 ? 0.360536 0.22913  0.29702  -0.0160834  0.024375    -0.0073403  228  SER A O   
1553 C  CB  . SER A 192 ? 0.408993 0.242096 0.337385 -0.0160129  0.0293223   -0.0100878  228  SER A CB  
1554 O  OG  . SER A 192 ? 0.396467 0.236119 0.327276 -0.00726889 0.0241782   -0.0115183  228  SER A OG  
1555 N  N   . LEU A 193 ? 0.325993 0.212425 0.275047 -0.019659   0.0227794   -0.0172995  229  LEU A N   
1556 C  CA  . LEU A 193 ? 0.34075  0.242237 0.292777 -0.0167549  0.0189304   -0.0152736  229  LEU A CA  
1557 C  C   . LEU A 193 ? 0.379892 0.284236 0.330555 -0.0183602  0.0192896   -0.0108007  229  LEU A C   
1558 O  O   . LEU A 193 ? 0.378537 0.285852 0.327283 -0.0136064  0.0165131   -0.00703029 229  LEU A O   
1559 C  CB  . LEU A 193 ? 0.318537 0.235498 0.27725  -0.0188743  0.0169696   -0.0199331  229  LEU A CB  
1560 C  CG  . LEU A 193 ? 0.307643 0.23831  0.268869 -0.0161097  0.0131858   -0.017647   229  LEU A CG  
1561 C  CD1 . LEU A 193 ? 0.3188   0.250208 0.279189 -0.00985404 0.0111533   -0.0169352  229  LEU A CD1 
1562 C  CD2 . LEU A 193 ? 0.295099 0.238027 0.260576 -0.0193969  0.0118959   -0.0218144  229  LEU A CD2 
1563 N  N   . GLU A 194 ? 0.330352 0.237277 0.283759 -0.0250966  0.0222797   -0.0123404  230  GLU A N   
1564 C  CA  . GLU A 194 ? 0.346474 0.259946 0.300473 -0.0260135  0.0221915   -0.00952792 230  GLU A CA  
1565 C  C   . GLU A 194 ? 0.361656 0.263059 0.306311 -0.0230444  0.0236669   -0.00389642 230  GLU A C   
1566 O  O   . GLU A 194 ? 0.355626 0.261951 0.298924 -0.0199533  0.0214842   -0.00102137 230  GLU A O   
1567 C  CB  . GLU A 194 ? 0.340177 0.260547 0.299974 -0.0331352  0.0251649   -0.0127575  230  GLU A CB  
1568 C  CG  . GLU A 194 ? 0.382844 0.316548 0.351171 -0.0351163  0.0223801   -0.0182843  230  GLU A CG  
1569 C  CD  . GLU A 194 ? 0.419414 0.363431 0.395511 -0.0409206  0.0238324   -0.0224028  230  GLU A CD  
1570 O  OE1 . GLU A 194 ? 0.4122   0.353638 0.387808 -0.0440437  0.0278504   -0.0213177  230  GLU A OE1 
1571 O  OE2 . GLU A 194 ? 0.425866 0.380684 0.408411 -0.0424816  0.0211954   -0.0271958  230  GLU A OE2 
1572 N  N   . GLN A 195 ? 0.310899 0.195907 0.248439 -0.0240079  0.0272476   -0.00236368 231  GLN A N   
1573 C  CA  . GLN A 195 ? 0.340596 0.212058 0.266572 -0.0207336  0.0284251   0.00373695  231  GLN A CA  
1574 C  C   . GLN A 195 ? 0.349753 0.221162 0.272603 -0.011272   0.0225741   0.00620881  231  GLN A C   
1575 O  O   . GLN A 195 ? 0.41018  0.279948 0.326473 -0.00717561 0.0208014   0.0103629   231  GLN A O   
1576 C  CB  . GLN A 195 ? 0.354522 0.205556 0.272244 -0.0240079  0.033712    0.00546953  231  GLN A CB  
1577 N  N   . ASP A 196 ? 0.331989 0.205679 0.259548 -0.00770247 0.0196454   0.00305804  232  ASP A N   
1578 C  CA  . ASP A 196 ? 0.34914  0.225037 0.276123 0.00085431  0.0144555   0.00401399  232  ASP A CA  
1579 C  C   . ASP A 196 ? 0.397014 0.289032 0.329063 0.00221572  0.0109284   0.00425394  232  ASP A C   
1580 O  O   . ASP A 196 ? 0.366009 0.257807 0.294209 0.00776944  0.00768059  0.00695715  232  ASP A O   
1581 C  CB  . ASP A 196 ? 0.376607 0.256178 0.309836 0.00358894  0.0126624   -0.0007314  232  ASP A CB  
1582 C  CG  . ASP A 196 ? 0.447188 0.310954 0.376958 0.00372656  0.0151802   -0.00242534 232  ASP A CG  
1583 O  OD1 . ASP A 196 ? 0.47763  0.324979 0.398148 0.00441742  0.0170088   0.00176427  232  ASP A OD1 
1584 O  OD2 . ASP A 196 ? 0.530844 0.398536 0.466654 0.00263597  0.015567    -0.00799143 232  ASP A OD2 
1585 N  N   . LEU A 197 ? 0.357629 0.262249 0.297553 -0.00284908 0.0114676   0.00145983  233  LEU A N   
1586 C  CA  . LEU A 197 ? 0.324374 0.24199  0.268888 -0.00159079 0.00817353  0.00182086  233  LEU A CA  
1587 C  C   . LEU A 197 ? 0.340445 0.256197 0.279982 -0.0016974  0.00861769  0.00504245  233  LEU A C   
1588 O  O   . LEU A 197 ? 0.315898 0.237007 0.255833 0.00188325  0.00525399  0.00602765  233  LEU A O   
1589 C  CB  . LEU A 197 ? 0.312662 0.241843 0.265066 -0.00619656 0.00824064  -0.00122995 233  LEU A CB  
1590 C  CG  . LEU A 197 ? 0.319445 0.252535 0.275742 -0.00578629 0.0075239   -0.00463293 233  LEU A CG  
1591 C  CD1 . LEU A 197 ? 0.267094 0.210554 0.228815 -0.0101683  0.00726388  -0.0071475  233  LEU A CD1 
1592 C  CD2 . LEU A 197 ? 0.319557 0.255294 0.276911 -0.00010159 0.0048281   -0.00494867 233  LEU A CD2 
1593 N  N   . GLU A 198 ? 0.349164 0.258061 0.284459 -0.00622838 0.0130849   0.00599993  234  GLU A N   
1594 C  CA  . GLU A 198 ? 0.448267 0.354409 0.377256 -0.00709385 0.0149973   0.00872321  234  GLU A CA  
1595 C  C   . GLU A 198 ? 0.405879 0.303283 0.324425 -0.00051346 0.0125095   0.0127542   234  GLU A C   
1596 O  O   . GLU A 198 ? 0.425021 0.327101 0.341278 0.00229328  0.0100237   0.013781    234  GLU A O   
1597 C  CB  . GLU A 198 ? 0.478369 0.379273 0.405879 -0.0143841  0.0214565   0.00814113  234  GLU A CB  
1598 C  CG  . GLU A 198 ? 0.519062 0.418138 0.440279 -0.0169418  0.0252998   0.0101821   234  GLU A CG  
1599 C  CD  . GLU A 198 ? 0.704746 0.617727 0.631582 -0.0154508  0.0223794   0.00850168  234  GLU A CD  
1600 O  OE1 . GLU A 198 ? 0.825891 0.750578 0.763919 -0.016775   0.0202726   0.00483897  234  GLU A OE1 
1601 O  OE2 . GLU A 198 ? 0.840193 0.752358 0.760154 -0.0128129  0.0219169   0.0105653   234  GLU A OE2 
1602 N  N   . ARG A 199 ? 0.446825 0.331568 0.359108 0.00256932  0.0125556   0.0145834   235  ARG A N   
1603 C  CA  . ARG A 199 ? 0.450277 0.326188 0.352284 0.00994402  0.00923956  0.0183499   235  ARG A CA  
1604 C  C   . ARG A 199 ? 0.437269 0.325878 0.345647 0.0159631   0.0026753   0.0163339   235  ARG A C   
1605 O  O   . ARG A 199 ? 0.393064 0.28209  0.295498 0.0203443   -0.00047662 0.0181767   235  ARG A O   
1606 C  CB  . ARG A 199 ? 0.474396 0.33503  0.371007 0.01326     0.0094767   0.0197387   235  ARG A CB  
1607 C  CG  . ARG A 199 ? 0.579171 0.423509 0.463897 0.00844123  0.0156264   0.0239776   235  ARG A CG  
1608 C  CD  . ARG A 199 ? 0.765891 0.589716 0.638185 0.0141821   0.0148067   0.0283703   235  ARG A CD  
1609 N  NE  . ARG A 199 ? 0.793503 0.608076 0.668723 0.00800478  0.0200617   0.0264444   235  ARG A NE  
1610 C  CZ  . ARG A 199 ? 0.84037  0.661738 0.72727  0.00818243  0.0185946   0.0208985   235  ARG A CZ  
1611 N  NH1 . ARG A 199 ? 0.788042 0.614416 0.679016 0.016648    0.0125205   0.0190123   235  ARG A NH1 
1612 N  NH2 . ARG A 199 ? 0.744562 0.567139 0.638355 -9.003e-05  0.0234371   0.0169732   235  ARG A NH2 
1613 N  N   . LEU A 200 ? 0.393297 0.292097 0.313247 0.0158165   0.00090765  0.0123305   236  LEU A N   
1614 C  CA  . LEU A 200 ? 0.431564 0.342905 0.35876  0.0200895   -0.00428487 0.0100072   236  LEU A CA  
1615 C  C   . LEU A 200 ? 0.426511 0.347382 0.356178 0.0178542   -0.00528747 0.00972596  236  LEU A C   
1616 O  O   . LEU A 200 ? 0.458506 0.384597 0.388184 0.0220825   -0.00954889 0.00928275  236  LEU A O   
1617 C  CB  . LEU A 200 ? 0.352241 0.272283 0.29013  0.0189897   -0.00455346 0.00606613  236  LEU A CB  
1618 C  CG  . LEU A 200 ? 0.344721 0.256324 0.281378 0.0217536   -0.0037265  0.00492303  236  LEU A CG  
1619 C  CD1 . LEU A 200 ? 0.346751 0.268997 0.293307 0.0177747   -0.00237629 0.0007597   236  LEU A CD1 
1620 C  CD2 . LEU A 200 ? 0.3054   0.215927 0.240928 0.0308231   -0.00854582 0.0045139   236  LEU A CD2 
1621 N  N   . PHE A 201 ? 0.370047 0.293617 0.302565 0.0114038   -0.00163045 0.00924439  237  PHE A N   
1622 C  CA  . PHE A 201 ? 0.342914 0.274743 0.27844  0.00963655  -0.00249768 0.00839845  237  PHE A CA  
1623 C  C   . PHE A 201 ? 0.332822 0.25918  0.257821 0.01243     -0.00291536 0.0106377   237  PHE A C   
1624 O  O   . PHE A 201 ? 0.317094 0.249622 0.243072 0.0150445   -0.00648901 0.00943356  237  PHE A O   
1625 C  CB  . PHE A 201 ? 0.303604 0.239004 0.244141 0.00333127  0.0011289   0.00710651  237  PHE A CB  
1626 C  CG  . PHE A 201 ? 0.385469 0.327931 0.32877  0.00233676  0.0002845   0.00593477  237  PHE A CG  
1627 C  CD1 . PHE A 201 ? 0.326607 0.277762 0.277569 0.00327363  -0.00346774 0.00416999  237  PHE A CD1 
1628 C  CD2 . PHE A 201 ? 0.518577 0.458141 0.456073 0.00065416  0.00348677  0.00645579  237  PHE A CD2 
1629 C  CE1 . PHE A 201 ? 0.416578 0.372645 0.37029  0.00266337  -0.00433945 0.00264967  237  PHE A CE1 
1630 C  CE2 . PHE A 201 ? 0.39655  0.342933 0.337149 0.00026647  0.00275858  0.00438213  237  PHE A CE2 
1631 C  CZ  . PHE A 201 ? 0.441065 0.395144 0.389875 0.00160879  -0.00148392 0.00240286  237  PHE A CZ  
1632 N  N   . GLN A 202 ? 0.378306 0.292512 0.292383 0.0118807   0.00069745  0.0138485   238  GLN A N   
1633 C  CA  . GLN A 202 ? 0.414846 0.323066 0.31631  0.0143989   0.00073022  0.0165841   238  GLN A CA  
1634 C  C   . GLN A 202 ? 0.432983 0.341163 0.329755 0.0224813   -0.00578081 0.017178    238  GLN A C   
1635 O  O   . GLN A 202 ? 0.398548 0.309218 0.289503 0.0248641   -0.00796438 0.0171033   238  GLN A O   
1636 C  CB  . GLN A 202 ? 0.408738 0.302635 0.298535 0.0112252   0.00677449  0.0205277   238  GLN A CB  
1637 C  CG  . GLN A 202 ? 0.494292 0.392352 0.390527 0.00288117  0.0129445   0.0183967   238  GLN A CG  
1638 C  CD  . GLN A 202 ? 0.594222 0.502462 0.492682 0.0010363   0.0136938   0.0159934   238  GLN A CD  
1639 O  OE1 . GLN A 202 ? 0.579619 0.486855 0.469126 0.0044129   0.0121653   0.0172184   238  GLN A OE1 
1640 N  NE2 . GLN A 202 ? 0.599289 0.517226 0.509084 -0.00394366 0.0159302   0.0122001   238  GLN A NE2 
1641 N  N   . GLU A 203 ? 0.396676 0.303437 0.296771 0.0268355   -0.0090592  0.0168687   239  GLU A N   
1642 C  CA  . GLU A 203 ? 0.424424 0.334155 0.323113 0.0348706   -0.0158912  0.0161012   239  GLU A CA  
1643 C  C   . GLU A 203 ? 0.393004 0.318811 0.302488 0.0352463   -0.0201571  0.0113596   239  GLU A C   
1644 O  O   . GLU A 203 ? 0.367926 0.296966 0.274116 0.040993    -0.0255605  0.0103315   239  GLU A O   
1645 C  CB  . GLU A 203 ? 0.439464 0.345151 0.341157 0.0392048   -0.0177298  0.0158412   239  GLU A CB  
1646 C  CG  . GLU A 203 ? 0.608491 0.495054 0.496696 0.0395728   -0.0140725  0.020996    239  GLU A CG  
1647 C  CD  . GLU A 203 ? 0.765815 0.649577 0.656503 0.0469312   -0.018295   0.0199136   239  GLU A CD  
1648 O  OE1 . GLU A 203 ? 0.973575 0.852994 0.855572 0.0550421   -0.0236089  0.0218098   239  GLU A OE1 
1649 O  OE2 . GLU A 203 ? 0.930302 0.818278 0.831908 0.0450766   -0.0168974  0.0165343   239  GLU A OE2 
1650 N  N   . LEU A 204 ? 0.383795 0.31909  0.305838 0.0296363   -0.0183063  0.00838598  240  LEU A N   
1651 C  CA  . LEU A 204 ? 0.369954 0.317951 0.301403 0.0287811   -0.0214713  0.00434986  240  LEU A CA  
1652 C  C   . LEU A 204 ? 0.38877  0.3383   0.31654  0.0266031   -0.0207654  0.00367456  240  LEU A C   
1653 O  O   . LEU A 204 ? 0.393636 0.352157 0.329242 0.0255554   -0.0232009  1.819e-05   240  LEU A O   
1654 C  CB  . LEU A 204 ? 0.36045  0.316173 0.305037 0.0238731   -0.0198778  0.00216338  240  LEU A CB  
1655 C  CG  . LEU A 204 ? 0.414338 0.375741 0.367088 0.0259843   -0.021864   6.464e-05   240  LEU A CG  
1656 C  CD1 . LEU A 204 ? 0.393075 0.364742 0.35254  0.0292937   -0.0269709  -0.00383104 240  LEU A CD1 
1657 C  CD2 . LEU A 204 ? 0.341329 0.294409 0.288389 0.0299535   -0.0213416  0.00186783  240  LEU A CD2 
1658 N  N   . GLN A 205 ? 0.399021 0.340092 0.315166 0.0257152   -0.0172379  0.00661965  241  GLN A N   
1659 C  CA  . GLN A 205 ? 0.439094 0.383135 0.352885 0.0233898   -0.0157897  0.0049465   241  GLN A CA  
1660 C  C   . GLN A 205 ? 0.477566 0.42647  0.387592 0.0280223   -0.0211714  0.00215443  241  GLN A C   
1661 O  O   . GLN A 205 ? 0.446653 0.403449 0.363371 0.0265226   -0.0226156  -0.00215864 241  GLN A O   
1662 C  CB  . GLN A 205 ? 0.50442  0.438881 0.406635 0.0206941   -0.00967171 0.00853614  241  GLN A CB  
1663 C  CG  . GLN A 205 ? 0.495223 0.430151 0.405633 0.0143597   -0.00443479 0.00843192  241  GLN A CG  
1664 C  CD  . GLN A 205 ? 0.473803 0.418482 0.394441 0.0109613   -0.00384034 0.00431195  241  GLN A CD  
1665 O  OE1 . GLN A 205 ? 0.488616 0.439845 0.420819 0.0101086   -0.00625895 0.0021689   241  GLN A OE1 
1666 N  NE2 . GLN A 205 ? 0.502937 0.448255 0.418751 0.00932053  -0.00061248 0.00313545  241  GLN A NE2 
1667 N  N   . PRO A 206 ? 0.479888 0.423918 0.378477 0.0341419   -0.0247246  0.00414684  242  PRO A N   
1668 C  CA  . PRO A 206 ? 0.468084 0.418932 0.364733 0.0389783   -0.0311074  0.0003854   242  PRO A CA  
1669 C  C   . PRO A 206 ? 0.435514 0.399358 0.349278 0.0377024   -0.0350275  -0.00575759 242  PRO A C   
1670 O  O   . PRO A 206 ? 0.479279 0.449869 0.39588  0.0371103   -0.037245   -0.0104723  242  PRO A O   
1671 C  CB  . PRO A 206 ? 0.459006 0.402973 0.343769 0.046921    -0.0356498  0.00377313  242  PRO A CB  
1672 C  CG  . PRO A 206 ? 0.470138 0.398954 0.343225 0.0448372   -0.0291502  0.0106378   242  PRO A CG  
1673 C  CD  . PRO A 206 ? 0.46372  0.394649 0.349571 0.0368847   -0.0230177  0.00994611  242  PRO A CD  
1674 N  N   . LEU A 207 ? 0.373572 0.340805 0.298211 0.0374522   -0.0360058  -0.00610841 243  LEU A N   
1675 C  CA  . LEU A 207 ? 0.345912 0.324786 0.285736 0.035588    -0.0390604  -0.0115664  243  LEU A CA  
1676 C  C   . LEU A 207 ? 0.38428  0.364733 0.331435 0.0288168   -0.0352886  -0.0129643  243  LEU A C   
1677 O  O   . LEU A 207 ? 0.326019 0.312814 0.279535 0.0274238   -0.0377008  -0.0178093  243  LEU A O   
1678 C  CB  . LEU A 207 ? 0.325882 0.306741 0.274101 0.0357258   -0.0387796  -0.0107777  243  LEU A CB  
1679 C  CG  . LEU A 207 ? 0.43369  0.426451 0.394289 0.0373698   -0.0433462  -0.0159124  243  LEU A CG  
1680 C  CD1 . LEU A 207 ? 0.405309 0.405508 0.365411 0.0417683   -0.0498778  -0.0208948  243  LEU A CD1 
1681 C  CD2 . LEU A 207 ? 0.40054  0.391457 0.361065 0.0417186   -0.0436971  -0.0140721  243  LEU A CD2 
1682 N  N   . TYR A 208 ? 0.315502 0.290487 0.263041 0.0248253   -0.0298957  -0.00925514 244  TYR A N   
1683 C  CA  . TYR A 208 ? 0.296333 0.272755 0.250783 0.0196282   -0.0271922  -0.0105136  244  TYR A CA  
1684 C  C   . TYR A 208 ? 0.271908 0.24857  0.221574 0.0200098   -0.0273813  -0.0133847  244  TYR A C   
1685 O  O   . TYR A 208 ? 0.264238 0.245127 0.221596 0.0181872   -0.0288789  -0.0174733  244  TYR A O   
1686 C  CB  . TYR A 208 ? 0.263455 0.235106 0.218127 0.0160069   -0.0220873  -0.00688114 244  TYR A CB  
1687 C  CG  . TYR A 208 ? 0.29942  0.273682 0.262599 0.0119716   -0.0209728  -0.00860558 244  TYR A CG  
1688 C  CD1 . TYR A 208 ? 0.287749 0.266219 0.261281 0.00982492  -0.0229812  -0.0100806  244  TYR A CD1 
1689 C  CD2 . TYR A 208 ? 0.29165  0.263957 0.252297 0.0105055   -0.0178703  -0.00884798 244  TYR A CD2 
1690 C  CE1 . TYR A 208 ? 0.30797  0.286704 0.287959 0.00697036  -0.0227004  -0.0112068  244  TYR A CE1 
1691 C  CE2 . TYR A 208 ? 0.2983   0.272861 0.267059 0.00824643  -0.0179276  -0.0109165  244  TYR A CE2 
1692 C  CZ  . TYR A 208 ? 0.314153 0.290752 0.291856 0.00671752  -0.0205124  -0.0115214  244  TYR A CZ  
1693 O  OH  . TYR A 208 ? 0.285696 0.262026 0.269924 0.00497576  -0.0206681  -0.012452   244  TYR A OH  
1694 N  N   . LEU A 209 ? 0.264369 0.235765 0.201331 0.0217595   -0.0250725  -0.0113271  245  LEU A N   
1695 C  CA  . LEU A 209 ? 0.299108 0.271718 0.230773 0.022116    -0.0246121  -0.0146385  245  LEU A CA  
1696 C  C   . LEU A 209 ? 0.284682 0.263807 0.218954 0.0247971   -0.0305307  -0.0203541  245  LEU A C   
1697 O  O   . LEU A 209 ? 0.276447 0.258909 0.215305 0.0233547   -0.0308148  -0.0251753  245  LEU A O   
1698 C  CB  . LEU A 209 ? 0.337878 0.304112 0.253314 0.0235315   -0.0210395  -0.0115463  245  LEU A CB  
1699 C  CG  . LEU A 209 ? 0.384518 0.344865 0.298235 0.0196045   -0.0143533  -0.00719928 245  LEU A CG  
1700 C  CD1 . LEU A 209 ? 0.364931 0.316936 0.261954 0.0203283   -0.0104132  -0.00300339 245  LEU A CD1 
1701 C  CD2 . LEU A 209 ? 0.358431 0.323431 0.282061 0.0154381   -0.0111457  -0.0104853  245  LEU A CD2 
1702 N  N   . ASN A 210 ? 0.276761 0.257849 0.208252 0.0289848   -0.0353896  -0.0204369  246  ASN A N   
1703 C  CA  . ASN A 210 ? 0.310355 0.29926  0.245466 0.0313582   -0.0415219  -0.0268543  246  ASN A CA  
1704 C  C   . ASN A 210 ? 0.301854 0.296696 0.254301 0.0269493   -0.0427128  -0.0314401  246  ASN A C   
1705 O  O   . ASN A 210 ? 0.338952 0.33829  0.295487 0.0264267   -0.045451   -0.0377323  246  ASN A O   
1706 C  CB  . ASN A 210 ? 0.285393 0.276124 0.214119 0.0375317   -0.0469488  -0.0262621  246  ASN A CB  
1707 C  CG  . ASN A 210 ? 0.335343 0.320366 0.244424 0.0423076   -0.0473197  -0.0238078  246  ASN A CG  
1708 O  OD1 . ASN A 210 ? 0.351771 0.340743 0.254838 0.0445024   -0.0504934  -0.0285205  246  ASN A OD1 
1709 N  ND2 . ASN A 210 ? 0.340209 0.315384 0.238218 0.0438903   -0.0441056  -0.0165642  246  ASN A ND2 
1710 N  N   . LEU A 211 ? 0.294507 0.28917  0.25643  0.0238949   -0.0409532  -0.0285553  247  LEU A N   
1711 C  CA  . LEU A 211 ? 0.290303 0.288583 0.266845 0.0190554   -0.0411976  -0.0314288  247  LEU A CA  
1712 C  C   . LEU A 211 ? 0.25828  0.252589 0.237346 0.0157757   -0.0385206  -0.032595   247  LEU A C   
1713 O  O   . LEU A 211 ? 0.233654 0.229906 0.220886 0.0134774   -0.0404039  -0.0376373  247  LEU A O   
1714 C  CB  . LEU A 211 ? 0.269563 0.267619 0.252665 0.0164551   -0.0388697  -0.0272545  247  LEU A CB  
1715 C  CG  . LEU A 211 ? 0.285769 0.286063 0.282155 0.0106763   -0.038205   -0.0289111  247  LEU A CG  
1716 C  CD1 . LEU A 211 ? 0.273968 0.283028 0.279751 0.00976972  -0.0421654  -0.0349791  247  LEU A CD1 
1717 C  CD2 . LEU A 211 ? 0.260129 0.258594 0.259208 0.00799427  -0.0345172  -0.0236356  247  LEU A CD2 
1718 N  N   . HIS A 212 ? 0.217604 0.206428 0.190006 0.015784    -0.0342677  -0.0284969  248  HIS A N   
1719 C  CA  . HIS A 212 ? 0.228147 0.214252 0.203463 0.0137238   -0.0318424  -0.0298674  248  HIS A CA  
1720 C  C   . HIS A 212 ? 0.24909  0.237278 0.221994 0.0155466   -0.0337476  -0.0363839  248  HIS A C   
1721 O  O   . HIS A 212 ? 0.279347 0.266951 0.259776 0.0139883   -0.0343515  -0.0405143  248  HIS A O   
1722 C  CB  . HIS A 212 ? 0.230949 0.213168 0.199714 0.0135956   -0.0269775  -0.0252513  248  HIS A CB  
1723 C  CG  . HIS A 212 ? 0.271712 0.25277  0.243624 0.0122917   -0.0242509  -0.0267699  248  HIS A CG  
1724 N  ND1 . HIS A 212 ? 0.297002 0.279561 0.265211 0.0139068   -0.0235734  -0.0315162  248  HIS A ND1 
1725 C  CD2 . HIS A 212 ? 0.282363 0.261793 0.260845 0.0101405   -0.022411   -0.0248016  248  HIS A CD2 
1726 C  CE1 . HIS A 212 ? 0.300665 0.283004 0.274249 0.0129412   -0.021196   -0.0327797  248  HIS A CE1 
1727 N  NE2 . HIS A 212 ? 0.29054  0.270839 0.270682 0.0108562   -0.0210153  -0.0286401  248  HIS A NE2 
1728 N  N   . ALA A 213 ? 0.235436 0.225505 0.197198 0.0191785   -0.0350024  -0.0375664  249  ALA A N   
1729 C  CA  . ALA A 213 ? 0.247424 0.24002  0.205526 0.0209352   -0.0364948  -0.0442894  249  ALA A CA  
1730 C  C   . ALA A 213 ? 0.249428 0.246653 0.217064 0.0203207   -0.0419645  -0.0512909  249  ALA A C   
1731 O  O   . ALA A 213 ? 0.24534  0.243442 0.216612 0.019939    -0.0430143  -0.0581467  249  ALA A O   
1732 C  CB  . ALA A 213 ? 0.222334 0.214949 0.163197 0.0250041   -0.0361177  -0.0430726  249  ALA A CB  
1733 N  N   . TYR A 214 ? 0.255232 0.256104 0.22712  0.0203197   -0.0454772  -0.0506137  250  TYR A N   
1734 C  CA  . TYR A 214 ? 0.250937 0.257447 0.23291  0.0188587   -0.0503029  -0.0578607  250  TYR A CA  
1735 C  C   . TYR A 214 ? 0.237687 0.240166 0.233557 0.0132614   -0.0486666  -0.0590221  250  TYR A C   
1736 O  O   . TYR A 214 ? 0.228072 0.231154 0.231258 0.0113123   -0.0509482  -0.066148   250  TYR A O   
1737 C  CB  . TYR A 214 ? 0.244275 0.256648 0.227616 0.0204302   -0.0535105  -0.0562564  250  TYR A CB  
1738 C  CG  . TYR A 214 ? 0.292992 0.312772 0.290281 0.0173433   -0.0576661  -0.0634191  250  TYR A CG  
1739 C  CD1 . TYR A 214 ? 0.334041 0.360346 0.331725 0.0189952   -0.0628088  -0.0722544  250  TYR A CD1 
1740 C  CD2 . TYR A 214 ? 0.26644  0.286865 0.276596 0.0120749   -0.0560259  -0.0618352  250  TYR A CD2 
1741 C  CE1 . TYR A 214 ? 0.334015 0.367642 0.345733 0.0152759   -0.0663296  -0.0796689  250  TYR A CE1 
1742 C  CE2 . TYR A 214 ? 0.271542 0.298949 0.295027 0.00805853  -0.0588476  -0.0685474  250  TYR A CE2 
1743 C  CZ  . TYR A 214 ? 0.314958 0.348727 0.340298 0.00919656  -0.0639087  -0.0778103  250  TYR A CZ  
1744 O  OH  . TYR A 214 ? 0.312825 0.353814 0.352861 0.00417352  -0.0663943  -0.085375   250  TYR A OH  
1745 N  N   . VAL A 215 ? 0.244498 0.242177 0.243689 0.0106155   -0.0449469  -0.0518778  251  VAL A N   
1746 C  CA  . VAL A 215 ? 0.234474 0.226115 0.243451 0.00608927  -0.0431534  -0.0509393  251  VAL A CA  
1747 C  C   . VAL A 215 ? 0.269701 0.256461 0.278227 0.00720266  -0.0424324  -0.0546787  251  VAL A C   
1748 O  O   . VAL A 215 ? 0.281132 0.26414  0.297951 0.00480353  -0.0437896  -0.0590877  251  VAL A O   
1749 C  CB  . VAL A 215 ? 0.219651 0.207678 0.230114 0.0037115   -0.0397329  -0.0427032  251  VAL A CB  
1750 C  CG1 . VAL A 215 ? 0.198843 0.17902  0.217041 -0.00018654 -0.0384304  -0.0412518  251  VAL A CG1 
1751 C  CG2 . VAL A 215 ? 0.208511 0.202473 0.223498 0.00182896  -0.040973   -0.042247   251  VAL A CG2 
1752 N  N   . ARG A 216 ? 0.299173 0.285446 0.298722 0.0105804   -0.0398151  -0.053032   252  ARG A N   
1753 C  CA  . ARG A 216 ? 0.250265 0.233891 0.250095 0.0121584   -0.0386272  -0.0573302  252  ARG A CA  
1754 C  C   . ARG A 216 ? 0.306467 0.292318 0.308313 0.0130339   -0.042064   -0.0669969  252  ARG A C   
1755 O  O   . ARG A 216 ? 0.260763 0.242165 0.270061 0.0124731   -0.0428162  -0.0720282  252  ARG A O   
1756 C  CB  . ARG A 216 ? 0.271333 0.257153 0.260157 0.0150673   -0.0348624  -0.0550161  252  ARG A CB  
1757 C  CG  . ARG A 216 ? 0.280239 0.265354 0.269954 0.0167541   -0.0323215  -0.0591181  252  ARG A CG  
1758 C  CD  . ARG A 216 ? 0.280012 0.267503 0.260162 0.017817    -0.0272343  -0.0553252  252  ARG A CD  
1759 N  NE  . ARG A 216 ? 0.277798 0.268627 0.244658 0.0195283   -0.0270636  -0.055825   252  ARG A NE  
1760 C  CZ  . ARG A 216 ? 0.30342  0.294188 0.259204 0.0196562   -0.0228996  -0.0505171  252  ARG A CZ  
1761 N  NH1 . ARG A 216 ? 0.27322  0.263328 0.230719 0.0180823   -0.0178422  -0.0475808  252  ARG A NH1 
1762 N  NH2 . ARG A 216 ? 0.275887 0.267216 0.218928 0.0215504   -0.0240401  -0.0490236  252  ARG A NH2 
1763 N  N   . ARG A 217 ? 0.305611 0.29808  0.301376 0.0145477   -0.044876   -0.0699549  253  ARG A N   
1764 C  CA  . ARG A 217 ? 0.327359 0.323507 0.324366 0.0153998   -0.0487654  -0.0798498  253  ARG A CA  
1765 C  C   . ARG A 217 ? 0.324893 0.317607 0.336588 0.0107813   -0.0513227  -0.0838969  253  ARG A C   
1766 O  O   . ARG A 217 ? 0.335083 0.32466  0.352215 0.0103346   -0.0525563  -0.091486   253  ARG A O   
1767 C  CB  . ARG A 217 ? 0.293232 0.297667 0.280353 0.0184748   -0.0521863  -0.0816474  253  ARG A CB  
1768 C  CG  . ARG A 217 ? 0.310773 0.320534 0.300316 0.0190194   -0.057252   -0.0928481  253  ARG A CG  
1769 C  CD  . ARG A 217 ? 0.316864 0.326825 0.300828 0.0215497   -0.0566839  -0.100557   253  ARG A CD  
1770 N  NE  . ARG A 217 ? 0.37048  0.382731 0.33695  0.0258571   -0.0540082  -0.0965371  253  ARG A NE  
1771 C  CZ  . ARG A 217 ? 0.42142  0.435435 0.378439 0.028597    -0.052168   -0.101936   253  ARG A CZ  
1772 N  NH1 . ARG A 217 ? 0.394726 0.409559 0.335401 0.0313818   -0.0484905  -0.0971716  253  ARG A NH1 
1773 N  NH2 . ARG A 217 ? 0.390373 0.404535 0.354229 0.0282289   -0.0532182  -0.11197    253  ARG A NH2 
1774 N  N   . ALA A 218 ? 0.283915 0.27671  0.301865 0.00709161  -0.0516033  -0.0789263  254  ALA A N   
1775 C  CA  . ALA A 218 ? 0.324405 0.313581 0.355587 0.00145514  -0.0529767  -0.0818691  254  ALA A CA  
1776 C  C   . ALA A 218 ? 0.300833 0.277698 0.337375 -0.00027759 -0.0505598  -0.0798816  254  ALA A C   
1777 O  O   . ALA A 218 ? 0.333015 0.304211 0.378003 -0.00320259 -0.0521206  -0.0857798  254  ALA A O   
1778 C  CB  . ALA A 218 ? 0.289629 0.282762 0.325818 -0.00230502 -0.0528409  -0.0772701  254  ALA A CB  
1779 N  N   . LEU A 219 ? 0.269677 0.242324 0.301334 0.00196239  -0.0472298  -0.0724445  255  LEU A N   
1780 C  CA  . LEU A 219 ? 0.274179 0.235709 0.310763 0.0016098   -0.0459698  -0.0706112  255  LEU A CA  
1781 C  C   . LEU A 219 ? 0.309335 0.269248 0.346863 0.00502734  -0.0473976  -0.0799057  255  LEU A C   
1782 O  O   . LEU A 219 ? 0.313529 0.263693 0.358232 0.004493    -0.0483538  -0.0830185  255  LEU A O   
1783 C  CB  . LEU A 219 ? 0.253466 0.21337  0.285233 0.00366284  -0.0428245  -0.0619283  255  LEU A CB  
1784 C  CG  . LEU A 219 ? 0.284119 0.243955 0.315579 0.00017176  -0.0412123  -0.0530503  255  LEU A CG  
1785 C  CD1 . LEU A 219 ? 0.24297  0.202223 0.269489 0.00223137  -0.0384838  -0.045714   255  LEU A CD1 
1786 C  CD2 . LEU A 219 ? 0.275158 0.225966 0.314873 -0.00501002 -0.0418988  -0.0517675  255  LEU A CD2 
1787 N  N   . HIS A 220 ? 0.295763 0.26469  0.324769 0.00909619  -0.0471842  -0.0840513  256  HIS A N   
1788 C  CA  . HIS A 220 ? 0.296158 0.265418 0.324682 0.0126769   -0.0477777  -0.0933994  256  HIS A CA  
1789 C  C   . HIS A 220 ? 0.310045 0.275695 0.347194 0.00991019  -0.0515888  -0.102379   256  HIS A C   
1790 O  O   . HIS A 220 ? 0.30343  0.262011 0.346582 0.0110908   -0.0523907  -0.108914   256  HIS A O   
1791 C  CB  . HIS A 220 ? 0.301616 0.28149  0.317271 0.0164273   -0.046441   -0.0952416  256  HIS A CB  
1792 C  CG  . HIS A 220 ? 0.311183 0.294564 0.32332  0.0200799   -0.0464881  -0.105523   256  HIS A CG  
1793 N  ND1 . HIS A 220 ? 0.297301 0.284816 0.308639 0.0202329   -0.0502142  -0.115222   256  HIS A ND1 
1794 C  CD2 . HIS A 220 ? 0.278465 0.263083 0.287706 0.0237497   -0.0429056  -0.108132   256  HIS A CD2 
1795 C  CE1 . HIS A 220 ? 0.299779 0.290327 0.30675  0.0239432   -0.0489048  -0.123384   256  HIS A CE1 
1796 N  NE2 . HIS A 220 ? 0.303319 0.292327 0.309417 0.0260032   -0.0441898  -0.119104   256  HIS A NE2 
1797 N  N   . ARG A 221 ? 0.282042 0.252814 0.320666 0.00622762  -0.0540346  -0.103296   257  ARG A N   
1798 C  CA  . ARG A 221 ? 0.341458 0.310917 0.388865 0.00260847  -0.057614   -0.112631   257  ARG A CA  
1799 C  C   . ARG A 221 ? 0.333576 0.288357 0.392631 -0.00224474 -0.0570847  -0.110893   257  ARG A C   
1800 O  O   . ARG A 221 ? 0.338715 0.286544 0.404772 -0.003479   -0.0588983  -0.119205   257  ARG A O   
1801 C  CB  . ARG A 221 ? 0.380731 0.361861 0.42634  0.00066246  -0.0599756  -0.112663   257  ARG A CB  
1802 C  CG  . ARG A 221 ? 0.514191 0.49833  0.568593 -0.00301613 -0.0642432  -0.124069   257  ARG A CG  
1803 C  CD  . ARG A 221 ? 0.621341 0.620748 0.671671 -0.00203975 -0.0678044  -0.126308   257  ARG A CD  
1804 N  NE  . ARG A 221 ? 0.556901 0.558679 0.611481 -0.00568962 -0.0664375  -0.117939   257  ARG A NE  
1805 C  CZ  . ARG A 221 ? 0.560083 0.567083 0.607177 -0.00293651 -0.0651781  -0.109445   257  ARG A CZ  
1806 N  NH1 . ARG A 221 ? 0.531046 0.542467 0.563846 0.00379573  -0.0653571  -0.107065   257  ARG A NH1 
1807 N  NH2 . ARG A 221 ? 0.572653 0.579335 0.626771 -0.00753867 -0.0631697  -0.103178   257  ARG A NH2 
1808 N  N   . HIS A 222 ? 0.32221  0.271178 0.38246  -0.00494805 -0.0545434  -0.0999519  258  HIS A N   
1809 C  CA  . HIS A 222 ? 0.318292 0.252254 0.386883 -0.00986715 -0.0537309  -0.0961388  258  HIS A CA  
1810 C  C   . HIS A 222 ? 0.337237 0.259051 0.405688 -0.00512799 -0.0532072  -0.0946639  258  HIS A C   
1811 O  O   . HIS A 222 ? 0.347409 0.256196 0.42272  -0.00634719 -0.0545347  -0.0987934  258  HIS A O   
1812 C  CB  . HIS A 222 ? 0.320963 0.254575 0.389602 -0.0147865  -0.0511948  -0.0853353  258  HIS A CB  
1813 C  CG  . HIS A 222 ? 0.411758 0.328436 0.486695 -0.0196645  -0.0501973  -0.0815227  258  HIS A CG  
1814 N  ND1 . HIS A 222 ? 0.436534 0.347708 0.520557 -0.027217   -0.050628   -0.0862272  258  HIS A ND1 
1815 C  CD2 . HIS A 222 ? 0.466414 0.369104 0.539682 -0.0178426  -0.0491573  -0.0741621  258  HIS A CD2 
1816 C  CE1 . HIS A 222 ? 0.479931 0.372553 0.566619 -0.0302677  -0.0493874  -0.0811084  258  HIS A CE1 
1817 N  NE2 . HIS A 222 ? 0.521742 0.408955 0.601477 -0.0240963  -0.0488914  -0.0734104  258  HIS A NE2 
1818 N  N   . TYR A 223 ? 0.30855  0.234559 0.369905 0.00050048  -0.0514739  -0.089575   259  TYR A N   
1819 C  CA  . TYR A 223 ? 0.311179 0.227182 0.373814 0.0050917   -0.0512471  -0.0872799  259  TYR A CA  
1820 C  C   . TYR A 223 ? 0.356328 0.275819 0.418864 0.0115332   -0.051969   -0.0971887  259  TYR A C   
1821 O  O   . TYR A 223 ? 0.365042 0.276972 0.430705 0.016235    -0.0523752  -0.0975911  259  TYR A O   
1822 C  CB  . TYR A 223 ? 0.319583 0.237104 0.377047 0.00697909  -0.049017   -0.0764227  259  TYR A CB  
1823 C  CG  . TYR A 223 ? 0.32722  0.237815 0.385263 0.00104744  -0.0481917  -0.066625   259  TYR A CG  
1824 C  CD1 . TYR A 223 ? 0.353454 0.247231 0.415493 -0.00042348 -0.049243   -0.0625129  259  TYR A CD1 
1825 C  CD2 . TYR A 223 ? 0.30618  0.226125 0.359982 -0.00250291 -0.0462201  -0.0612298  259  TYR A CD2 
1826 C  CE1 . TYR A 223 ? 0.346131 0.233409 0.406659 -0.00578458 -0.0477722  -0.0528481  259  TYR A CE1 
1827 C  CE2 . TYR A 223 ? 0.328161 0.242775 0.3823   -0.00790626 -0.0447826  -0.0528382  259  TYR A CE2 
1828 C  CZ  . TYR A 223 ? 0.356217 0.254455 0.41359  -0.0101481  -0.045331   -0.0489344  259  TYR A CZ  
1829 O  OH  . TYR A 223 ? 0.318973 0.210578 0.375544 -0.0159499  -0.0434477  -0.0408388  259  TYR A OH  
1830 N  N   . GLY A 224 ? 0.351452 0.282752 0.410151 0.0121471   -0.0522754  -0.105369   260  GLY A N   
1831 C  CA  . GLY A 224 ? 0.335168 0.270151 0.393275 0.0176878   -0.0524916  -0.11592    260  GLY A CA  
1832 C  C   . GLY A 224 ? 0.298535 0.245708 0.347755 0.0226699   -0.049081   -0.115027   260  GLY A C   
1833 O  O   . GLY A 224 ? 0.247041 0.195689 0.293531 0.0235213   -0.0466634  -0.106263   260  GLY A O   
1834 N  N   . ALA A 225 ? 0.320774 0.276521 0.365485 0.0255734   -0.0487502  -0.125179   261  ALA A N   
1835 C  CA  . ALA A 225 ? 0.300619 0.268419 0.335615 0.0294925   -0.0448234  -0.126839   261  ALA A CA  
1836 C  C   . ALA A 225 ? 0.304507 0.27098  0.343719 0.0334734   -0.0418728  -0.12432    261  ALA A C   
1837 O  O   . ALA A 225 ? 0.303685 0.277848 0.336756 0.0343637   -0.0378241  -0.119322   261  ALA A O   
1838 C  CB  . ALA A 225 ? 0.300257 0.27498  0.330866 0.0317563   -0.0455041  -0.14003    261  ALA A CB  
1839 N  N   . GLN A 226 ? 0.315947 0.272326 0.366189 0.035979    -0.0440818  -0.127653   262  GLN A N   
1840 C  CA  . GLN A 226 ? 0.349221 0.306815 0.403754 0.0406918   -0.0419454  -0.12602    262  GLN A CA  
1841 C  C   . GLN A 226 ? 0.350617 0.305469 0.405136 0.0388964   -0.0415016  -0.113107   262  GLN A C   
1842 O  O   . GLN A 226 ? 0.368248 0.327152 0.425515 0.0424742   -0.0396486  -0.11157    262  GLN A O   
1843 C  CB  . GLN A 226 ? 0.378736 0.325507 0.44506  0.0453814   -0.0451932  -0.132945   262  GLN A CB  
1844 C  CG  . GLN A 226 ? 0.396246 0.344972 0.46426  0.0479242   -0.0457705  -0.147489   262  GLN A CG  
1845 C  CD  . GLN A 226 ? 0.439545 0.402756 0.505274 0.052947    -0.0411928  -0.155617   262  GLN A CD  
1846 O  OE1 . GLN A 226 ? 0.397564 0.370392 0.46015  0.0537391   -0.0370922  -0.150444   262  GLN A OE1 
1847 N  NE2 . GLN A 226 ? 0.472922 0.438133 0.540283 0.0558012   -0.0414994  -0.169117   262  GLN A NE2 
1848 N  N   . HIS A 227 ? 0.348353 0.296912 0.400926 0.0335937   -0.0432896  -0.1048     263  HIS A N   
1849 C  CA  . HIS A 227 ? 0.327838 0.273788 0.380127 0.0322386   -0.0428299  -0.0932278  263  HIS A CA  
1850 C  C   . HIS A 227 ? 0.312116 0.266802 0.354914 0.0282854   -0.0398558  -0.0861318  263  HIS A C   
1851 O  O   . HIS A 227 ? 0.315129 0.268067 0.357388 0.0268412   -0.039411   -0.0772697  263  HIS A O   
1852 C  CB  . HIS A 227 ? 0.346535 0.27735  0.403769 0.0293067   -0.0464382  -0.0870723  263  HIS A CB  
1853 C  CG  . HIS A 227 ? 0.441631 0.360676 0.507588 0.0334777   -0.0497219  -0.0929802  263  HIS A CG  
1854 N  ND1 . HIS A 227 ? 0.502758 0.417797 0.573882 0.0395873   -0.0511571  -0.0921132  263  HIS A ND1 
1855 C  CD2 . HIS A 227 ? 0.429831 0.341273 0.500403 0.0330938   -0.0519762  -0.101306   263  HIS A CD2 
1856 C  CE1 . HIS A 227 ? 0.480009 0.383956 0.558371 0.0431978   -0.0543173  -0.0991456  263  HIS A CE1 
1857 N  NE2 . HIS A 227 ? 0.497122 0.398503 0.575192 0.0389416   -0.0545664  -0.104988   263  HIS A NE2 
1858 N  N   . ILE A 228 ? 0.28572  0.248958 0.320663 0.027048    -0.0382393  -0.09009    264  ILE A N   
1859 C  CA  . ILE A 228 ? 0.274962 0.245069 0.300105 0.0242236   -0.0358595  -0.0835676  264  ILE A CA  
1860 C  C   . ILE A 228 ? 0.304118 0.284615 0.31997  0.0263103   -0.0319968  -0.0880097  264  ILE A C   
1861 O  O   . ILE A 228 ? 0.348546 0.332316 0.360844 0.0274621   -0.0327502  -0.0959871  264  ILE A O   
1862 C  CB  . ILE A 228 ? 0.283819 0.252126 0.307306 0.0201702   -0.0387426  -0.0820411  264  ILE A CB  
1863 C  CG1 . ILE A 228 ? 0.344011 0.301989 0.375733 0.0168936   -0.0410901  -0.0764799  264  ILE A CG1 
1864 C  CG2 . ILE A 228 ? 0.272794 0.2482   0.285891 0.0187963   -0.036794   -0.0763015  264  ILE A CG2 
1865 C  CD1 . ILE A 228 ? 0.327404 0.284172 0.358145 0.0165053   -0.0390588  -0.0666943  264  ILE A CD1 
1866 N  N   . ASN A 229 ? 0.32542  0.31101  0.336813 0.0264506   -0.0276218  -0.0831917  265  ASN A N   
1867 C  CA  . ASN A 229 ? 0.345176 0.339475 0.34562  0.0272069   -0.0229802  -0.0860833  265  ASN A CA  
1868 C  C   . ASN A 229 ? 0.295376 0.290747 0.283338 0.02491     -0.0230145  -0.0806465  265  ASN A C   
1869 O  O   . ASN A 229 ? 0.292107 0.285016 0.279119 0.0226744   -0.0227794  -0.072138   265  ASN A O   
1870 C  CB  . ASN A 229 ? 0.351294 0.35054  0.352469 0.0273901   -0.0176364  -0.0834435  265  ASN A CB  
1871 C  CG  . ASN A 229 ? 0.423946 0.43134  0.413405 0.0271948   -0.0115989  -0.0862162  265  ASN A CG  
1872 O  OD1 . ASN A 229 ? 0.362341 0.3708   0.34046  0.0270864   -0.0117824  -0.0879134  265  ASN A OD1 
1873 N  ND2 . ASN A 229 ? 0.50811  0.521308 0.499204 0.026668    -0.00605546 -0.0858228  265  ASN A ND2 
1874 N  N   . LEU A 230 ? 0.269491 0.268366 0.247784 0.0259189   -0.0238524  -0.0855123  266  LEU A N   
1875 C  CA  . LEU A 230 ? 0.271486 0.270439 0.239751 0.0249549   -0.0261235  -0.0808834  266  LEU A CA  
1876 C  C   . LEU A 230 ? 0.299037 0.299346 0.254654 0.0242964   -0.0210651  -0.0734818  266  LEU A C   
1877 O  O   . LEU A 230 ? 0.308193 0.307257 0.255721 0.0241469   -0.0228993  -0.0683325  266  LEU A O   
1878 C  CB  . LEU A 230 ? 0.292473 0.295013 0.253845 0.0268257   -0.0297793  -0.0884075  266  LEU A CB  
1879 C  CG  . LEU A 230 ? 0.305854 0.306058 0.279131 0.0261574   -0.0358837  -0.0947165  266  LEU A CG  
1880 C  CD1 . LEU A 230 ? 0.325687 0.331111 0.2931   0.0284935   -0.0386728  -0.10564    266  LEU A CD1 
1881 C  CD2 . LEU A 230 ? 0.301891 0.299712 0.278791 0.0235643   -0.0394362  -0.0879027  266  LEU A CD2 
1882 N  N   . GLU A 231 ? 0.288469 0.291064 0.244039 0.0238286   -0.0149597  -0.0733473  267  GLU A N   
1883 C  CA  . GLU A 231 ? 0.348306 0.351179 0.29395  0.0219397   -0.00901895 -0.0666353  267  GLU A CA  
1884 C  C   . GLU A 231 ? 0.338894 0.340678 0.294602 0.0196417   -0.00638823 -0.0619395  267  GLU A C   
1885 O  O   . GLU A 231 ? 0.376458 0.379493 0.326926 0.0173798   -0.00044127 -0.0582704  267  GLU A O   
1886 C  CB  . GLU A 231 ? 0.329458 0.337787 0.264495 0.0223097   -0.0028132  -0.0712453  267  GLU A CB  
1887 C  CG  . GLU A 231 ? 0.440971 0.449762 0.361172 0.0245807   -0.00543396 -0.0737947  267  GLU A CG  
1888 C  CD  . GLU A 231 ? 0.612111 0.625855 0.518087 0.0247717   0.0010383   -0.0778327  267  GLU A CD  
1889 O  OE1 . GLU A 231 ? 0.735567 0.747464 0.623373 0.0257283   0.00088511  -0.0749199  267  GLU A OE1 
1890 O  OE2 . GLU A 231 ? 0.686225 0.705845 0.598298 0.0242213   0.0062189   -0.0838876  267  GLU A OE2 
1891 N  N   . GLY A 232 ? 0.29342  0.293078 0.263402 0.0200781   -0.0104315  -0.0627515  268  GLY A N   
1892 C  CA  . GLY A 232 ? 0.26693  0.26678  0.245698 0.0186478   -0.00838732 -0.0592572  268  GLY A CA  
1893 C  C   . GLY A 232 ? 0.269115 0.263119 0.253092 0.0172045   -0.012369   -0.0524144  268  GLY A C   
1894 O  O   . GLY A 232 ? 0.273183 0.26344  0.25496  0.0169263   -0.0162257  -0.0502926  268  GLY A O   
1895 N  N   . PRO A 233 ? 0.240042 0.234054 0.232115 0.01639     -0.011822   -0.0496125  269  PRO A N   
1896 C  CA  . PRO A 233 ? 0.257412 0.246129 0.253572 0.0149548   -0.015295   -0.0433705  269  PRO A CA  
1897 C  C   . PRO A 233 ? 0.274086 0.257569 0.277397 0.016108    -0.0207761  -0.0451687  269  PRO A C   
1898 O  O   . PRO A 233 ? 0.276623 0.260196 0.285042 0.0185939   -0.0221139  -0.0514039  269  PRO A O   
1899 C  CB  . PRO A 233 ? 0.264333 0.255748 0.266652 0.0144363   -0.0134416  -0.0415794  269  PRO A CB  
1900 C  CG  . PRO A 233 ? 0.247128 0.245325 0.253464 0.0164804   -0.0105573  -0.0485293  269  PRO A CG  
1901 C  CD  . PRO A 233 ? 0.246704 0.246855 0.244821 0.0171336   -0.00828416 -0.0533307  269  PRO A CD  
1902 N  N   . ILE A 234 ? 0.253375 0.232091 0.257339 0.0140555   -0.0235472  -0.0402303  270  ILE A N   
1903 C  CA  . ILE A 234 ? 0.24942  0.222032 0.260319 0.013745    -0.0278194  -0.0410991  270  ILE A CA  
1904 C  C   . ILE A 234 ? 0.261998 0.229995 0.280048 0.0144773   -0.0293644  -0.0384308  270  ILE A C   
1905 O  O   . ILE A 234 ? 0.24573  0.214967 0.262755 0.0136149   -0.0281163  -0.0333501  270  ILE A O   
1906 C  CB  . ILE A 234 ? 0.288592 0.259544 0.297201 0.0105974   -0.0291298  -0.0368954  270  ILE A CB  
1907 C  CG1 . ILE A 234 ? 0.314239 0.290246 0.314682 0.0111198   -0.0285134  -0.0390956  270  ILE A CG1 
1908 C  CG2 . ILE A 234 ? 0.30509  0.269458 0.320906 0.00868602  -0.0325289  -0.0374515  270  ILE A CG2 
1909 C  CD1 . ILE A 234 ? 0.260123 0.236662 0.259643 0.00905749  -0.0303304  -0.0364312  270  ILE A CD1 
1910 N  N   . PRO A 235 ? 0.237888 0.19963  0.262843 0.0163223   -0.0325405  -0.0415693  271  PRO A N   
1911 C  CA  . PRO A 235 ? 0.24175  0.197443 0.271462 0.0175177   -0.0348329  -0.0375988  271  PRO A CA  
1912 C  C   . PRO A 235 ? 0.235334 0.186163 0.262462 0.0134586   -0.0354144  -0.0294431  271  PRO A C   
1913 O  O   . PRO A 235 ? 0.221835 0.169598 0.248054 0.00985854  -0.0357072  -0.0285561  271  PRO A O   
1914 C  CB  . PRO A 235 ? 0.230061 0.177958 0.26642  0.0204435   -0.038185   -0.0428402  271  PRO A CB  
1915 C  CG  . PRO A 235 ? 0.237631 0.191684 0.273228 0.021713    -0.0366281  -0.0516149  271  PRO A CG  
1916 C  CD  . PRO A 235 ? 0.235957 0.195794 0.263793 0.0178867   -0.0342039  -0.049333   271  PRO A CD  
1917 N  N   . ALA A 236 ? 0.236368 0.187785 0.262756 0.0140895   -0.0355013  -0.0244027  272  ALA A N   
1918 C  CA  . ALA A 236 ? 0.258425 0.208035 0.280715 0.0104867   -0.0350422  -0.0169684  272  ALA A CA  
1919 C  C   . ALA A 236 ? 0.267485 0.206393 0.290204 0.00766252  -0.0370924  -0.0128632  272  ALA A C   
1920 O  O   . ALA A 236 ? 0.278972 0.217138 0.297926 0.00391856  -0.0359039  -0.00738157 272  ALA A O   
1921 C  CB  . ALA A 236 ? 0.223779 0.176927 0.245311 0.0123031   -0.0352661  -0.0138928  272  ALA A CB  
1922 N  N   . HIS A 237 ? 0.313916 0.243993 0.341073 0.00926756  -0.0398169  -0.0154953  273  HIS A N   
1923 C  CA  . HIS A 237 ? 0.29701  0.21434  0.324101 0.00628034  -0.0414568  -0.0108489  273  HIS A CA  
1924 C  C   . HIS A 237 ? 0.317479 0.232526 0.346902 0.00112152  -0.0402434  -0.0136726  273  HIS A C   
1925 O  O   . HIS A 237 ? 0.309572 0.213716 0.339863 -0.00277533 -0.0407075  -0.0107577  273  HIS A O   
1926 C  CB  . HIS A 237 ? 0.2896   0.196429 0.31988  0.0113749   -0.0455375  -0.0112725  273  HIS A CB  
1927 C  CG  . HIS A 237 ? 0.334562 0.240227 0.371411 0.0148415   -0.0469145  -0.0201432  273  HIS A CG  
1928 N  ND1 . HIS A 237 ? 0.296036 0.213464 0.334936 0.016877    -0.0451441  -0.0277103  273  HIS A ND1 
1929 C  CD2 . HIS A 237 ? 0.29713  0.190041 0.338209 0.0167275   -0.0498815  -0.0224915  273  HIS A CD2 
1930 C  CE1 . HIS A 237 ? 0.314924 0.227948 0.359293 0.019994    -0.0469895  -0.0349169  273  HIS A CE1 
1931 N  NE2 . HIS A 237 ? 0.314304 0.212323 0.36069  0.0201689   -0.0500381  -0.0321681  273  HIS A NE2 
1932 N  N   . LEU A 238 ? 0.269926 0.195018 0.300096 0.00076481  -0.0387063  -0.0193025  274  LEU A N   
1933 C  CA  . LEU A 238 ? 0.272459 0.196525 0.306558 -0.00279159 -0.0388912  -0.0243829  274  LEU A CA  
1934 C  C   . LEU A 238 ? 0.272972 0.204482 0.305789 -0.00789099 -0.0366349  -0.0229227  274  LEU A C   
1935 O  O   . LEU A 238 ? 0.290679 0.224779 0.327351 -0.0106122  -0.0370581  -0.0280721  274  LEU A O   
1936 C  CB  . LEU A 238 ? 0.243098 0.17295  0.278993 0.00112582  -0.0398112  -0.0332364  274  LEU A CB  
1937 C  CG  . LEU A 238 ? 0.262615 0.186322 0.302078 0.00632614  -0.0420089  -0.0373339  274  LEU A CG  
1938 C  CD1 . LEU A 238 ? 0.266786 0.198377 0.306837 0.00914888  -0.0419467  -0.0468335  274  LEU A CD1 
1939 C  CD2 . LEU A 238 ? 0.248675 0.156808 0.293022 0.0042056   -0.044356   -0.0366026  274  LEU A CD2 
1940 N  N   . LEU A 239 ? 0.272638 0.207941 0.300867 -0.00899678 -0.0345564  -0.0166819  275  LEU A N   
1941 C  CA  . LEU A 239 ? 0.330765 0.275102 0.357866 -0.0119981  -0.0324916  -0.0161792  275  LEU A CA  
1942 C  C   . LEU A 239 ? 0.317522 0.258918 0.346034 -0.0183304  -0.0304692  -0.0116544  275  LEU A C   
1943 O  O   . LEU A 239 ? 0.278032 0.227891 0.306004 -0.0202667  -0.0285096  -0.0110595  275  LEU A O   
1944 C  CB  . LEU A 239 ? 0.300091 0.251709 0.321134 -0.00881737 -0.0309853  -0.013576   275  LEU A CB  
1945 C  CG  . LEU A 239 ? 0.374237 0.332142 0.39259  -0.00419618 -0.0313145  -0.0182225  275  LEU A CG  
1946 C  CD1 . LEU A 239 ? 0.307714 0.269028 0.328624 -0.00413284 -0.0330075  -0.0250258  275  LEU A CD1 
1947 C  CD2 . LEU A 239 ? 0.336247 0.290849 0.354533 -0.00034228 -0.0320373  -0.0191777  275  LEU A CD2 
1948 N  N   . GLY A 240 ? 0.289308 0.218655 0.319064 -0.0212831  -0.0307053  -0.00846273 276  GLY A N   
1949 C  CA  . GLY A 240 ? 0.304565 0.22917  0.334858 -0.0284128  -0.0279445  -0.0039285  276  GLY A CA  
1950 C  C   . GLY A 240 ? 0.317787 0.24168  0.340367 -0.0291656  -0.0256767  0.00430288  276  GLY A C   
1951 O  O   . GLY A 240 ? 0.282767 0.204358 0.304235 -0.0353802  -0.0224138  0.00834881  276  GLY A O   
1952 N  N   . ASN A 241 ? 0.285939 0.213089 0.303298 -0.0234577  -0.0269349  0.00616346  277  ASN A N   
1953 C  CA  . ASN A 241 ? 0.2534   0.182318 0.263566 -0.0236732  -0.0252277  0.0123411   277  ASN A CA  
1954 C  C   . ASN A 241 ? 0.257572 0.181696 0.263805 -0.0176431  -0.0286108  0.0145674   277  ASN A C   
1955 O  O   . ASN A 241 ? 0.22207  0.148619 0.231432 -0.0128046  -0.0308504  0.00995915  277  ASN A O   
1956 C  CB  . ASN A 241 ? 0.233251 0.175544 0.242988 -0.0235262  -0.0228408  0.0103188   277  ASN A CB  
1957 C  CG  . ASN A 241 ? 0.2555   0.200482 0.258146 -0.022845   -0.0214447  0.0150022   277  ASN A CG  
1958 O  OD1 . ASN A 241 ? 0.278302 0.223996 0.277927 -0.0182242  -0.023351   0.0154057   277  ASN A OD1 
1959 N  ND2 . ASN A 241 ? 0.23638  0.182684 0.236387 -0.0277932  -0.018022   0.0183257   277  ASN A ND2 
1960 N  N   . MET A 242 ? 0.246044 0.16458  0.245289 -0.0177727  -0.0289923  0.0212305   278  MET A N   
1961 C  CA  . MET A 242 ? 0.269907 0.184709 0.266095 -0.0118075  -0.0329954  0.023164    278  MET A CA  
1962 C  C   . MET A 242 ? 0.258842 0.185432 0.257014 -0.0072495  -0.0335086  0.0186307   278  MET A C   
1963 O  O   . MET A 242 ? 0.288597 0.214887 0.289172 -0.00185    -0.036769   0.0163783   278  MET A O   
1964 C  CB  . MET A 242 ? 0.28731  0.196018 0.274042 -0.0129053  -0.0334094  0.0310877   278  MET A CB  
1965 C  CG  . MET A 242 ? 0.315426 0.21959  0.299285 -0.0057824  -0.039048   0.0330869   278  MET A CG  
1966 S  SD  . MET A 242 ? 0.340931 0.231894 0.330481 -0.00061463 -0.0440631  0.0311689   278  MET A SD  
1967 C  CE  . MET A 242 ? 0.378104 0.249727 0.357731 -0.00447195 -0.0444268  0.041139    278  MET A CE  
1968 N  N   . TRP A 243 ? 0.229624 0.166228 0.226827 -0.00937106 -0.0301723  0.017299    279  TRP A N   
1969 C  CA  . TRP A 243 ? 0.247281 0.193073 0.245013 -0.00605408 -0.0299675  0.0139667   279  TRP A CA  
1970 C  C   . TRP A 243 ? 0.268173 0.219534 0.270013 -0.00577566 -0.0282772  0.008391    279  TRP A C   
1971 O  O   . TRP A 243 ? 0.257701 0.215769 0.259063 -0.0039949  -0.0270412  0.00584884  279  TRP A O   
1972 C  CB  . TRP A 243 ? 0.260717 0.212381 0.253101 -0.00773171 -0.027824   0.0164433   279  TRP A CB  
1973 C  CG  . TRP A 243 ? 0.253319 0.199386 0.239977 -0.00782433 -0.0298866  0.021981    279  TRP A CG  
1974 C  CD1 . TRP A 243 ? 0.26569  0.210869 0.251436 -0.00344878 -0.0338358  0.0225853   279  TRP A CD1 
1975 C  CD2 . TRP A 243 ? 0.287974 0.227315 0.269308 -0.0119751  -0.0287033  0.027481    279  TRP A CD2 
1976 N  NE1 . TRP A 243 ? 0.302096 0.24004  0.280688 -0.00391413 -0.0358422  0.0287059   279  TRP A NE1 
1977 C  CE2 . TRP A 243 ? 0.30505  0.23857  0.280187 -0.00951244 -0.0322946  0.032145    279  TRP A CE2 
1978 C  CE3 . TRP A 243 ? 0.377349 0.315579 0.358597 -0.0176942  -0.0248033  0.0287345   279  TRP A CE3 
1979 C  CZ2 . TRP A 243 ? 0.305946 0.231237 0.272656 -0.0127313  -0.031749   0.0388979   279  TRP A CZ2 
1980 C  CZ3 . TRP A 243 ? 0.346974 0.278389 0.321352 -0.0217612  -0.0233901  0.0348082   279  TRP A CZ3 
1981 C  CH2 . TRP A 243 ? 0.341665 0.265889 0.30782  -0.0193278  -0.0267166  0.0402781   279  TRP A CH2 
1982 N  N   . ALA A 244 ? 0.24542  0.193318 0.25083  -0.00753503 -0.028428   0.00643214  280  ALA A N   
1983 C  CA  . ALA A 244 ? 0.281012 0.234647 0.288885 -0.00754035 -0.0272712  0.00147045  280  ALA A CA  
1984 C  C   . ALA A 244 ? 0.287434 0.248582 0.292148 -0.00842913 -0.0246042  0.00195632  280  ALA A C   
1985 O  O   . ALA A 244 ? 0.275889 0.241641 0.279913 -0.00638797 -0.024052   -0.00128694 280  ALA A O   
1986 C  CB  . ALA A 244 ? 0.239991 0.195381 0.249724 -0.00323894 -0.0285078  -0.00363637 280  ALA A CB  
1987 N  N   . GLN A 245 ? 0.294859 0.256639 0.297166 -0.0113911  -0.0228836  0.00581575  281  GLN A N   
1988 C  CA  . GLN A 245 ? 0.298058 0.266254 0.297583 -0.0113593  -0.0205486  0.00576362  281  GLN A CA  
1989 C  C   . GLN A 245 ? 0.301674 0.274217 0.30445  -0.0132137  -0.0195318  0.00344309  281  GLN A C   
1990 O  O   . GLN A 245 ? 0.297835 0.275354 0.299413 -0.011595   -0.0185646  0.00186921  281  GLN A O   
1991 C  CB  . GLN A 245 ? 0.272052 0.240866 0.267168 -0.0129097  -0.0190116  0.00962575  281  GLN A CB  
1992 C  CG  . GLN A 245 ? 0.301293 0.268792 0.29618  -0.0174415  -0.0174316  0.0125589   281  GLN A CG  
1993 C  CD  . GLN A 245 ? 0.371207 0.337911 0.359899 -0.0189722  -0.0163668  0.0168215   281  GLN A CD  
1994 O  OE1 . GLN A 245 ? 0.380834 0.343941 0.3662   -0.0169527  -0.018696   0.0189794   281  GLN A OE1 
1995 N  NE2 . GLN A 245 ? 0.331432 0.302108 0.318409 -0.022304   -0.0130924  0.0177138   281  GLN A NE2 
1996 N  N   . THR A 246 ? 0.281921 0.252491 0.289193 -0.0164792  -0.0198977  0.00290925  282  THR A N   
1997 C  CA  . THR A 246 ? 0.28806  0.264654 0.300653 -0.0182789  -0.0194764  -0.00079879 282  THR A CA  
1998 C  C   . THR A 246 ? 0.287369 0.260037 0.305272 -0.0198474  -0.021544   -0.00373782 282  THR A C   
1999 O  O   . THR A 246 ? 0.271054 0.235137 0.288517 -0.0209353  -0.0223019  -0.00149311 282  THR A O   
2000 C  CB  . THR A 246 ? 0.37956  0.361188 0.393877 -0.0225588  -0.0162049  0.000496    282  THR A CB  
2001 O  OG1 . THR A 246 ? 0.412644 0.38705  0.425612 -0.0270512  -0.0148787  0.00482976  282  THR A OG1 
2002 C  CG2 . THR A 246 ? 0.354874 0.34122  0.364735 -0.0204871  -0.0142873  0.0017276   282  THR A CG2 
2003 N  N   . TRP A 247 ? 0.275685 0.254139 0.297641 -0.0184469  -0.0232916  -0.00929931 283  TRP A N   
2004 C  CA  . TRP A 247 ? 0.280669 0.256091 0.307198 -0.0189155  -0.0258345  -0.0136991  283  TRP A CA  
2005 C  C   . TRP A 247 ? 0.297541 0.277112 0.33272  -0.0241951  -0.0255393  -0.017487   283  TRP A C   
2006 O  O   . TRP A 247 ? 0.296846 0.275077 0.336979 -0.0251062  -0.0278101  -0.0225169  283  TRP A O   
2007 C  CB  . TRP A 247 ? 0.247372 0.226218 0.271165 -0.0132608  -0.0285459  -0.0181527  283  TRP A CB  
2008 C  CG  . TRP A 247 ? 0.243959 0.219671 0.260414 -0.00905127 -0.0280565  -0.0154088  283  TRP A CG  
2009 C  CD1 . TRP A 247 ? 0.255145 0.225987 0.268395 -0.0090319  -0.0265347  -0.0105759  283  TRP A CD1 
2010 C  CD2 . TRP A 247 ? 0.218667 0.196824 0.23024  -0.00436704 -0.02917    -0.0182805  283  TRP A CD2 
2011 N  NE1 . TRP A 247 ? 0.223822 0.195018 0.232159 -0.00509851 -0.0263359  -0.0108157  283  TRP A NE1 
2012 C  CE2 . TRP A 247 ? 0.21135  0.186273 0.218087 -0.00248291 -0.0275156  -0.0152251  283  TRP A CE2 
2013 C  CE3 . TRP A 247 ? 0.242614 0.225682 0.253158 -0.00178991 -0.0314985  -0.0233511  283  TRP A CE3 
2014 C  CZ2 . TRP A 247 ? 0.21232  0.188357 0.213286 0.00109847  -0.0270311  -0.0168049  283  TRP A CZ2 
2015 C  CZ3 . TRP A 247 ? 0.239184 0.222312 0.241984 0.00237604  -0.0313594  -0.0240803  283  TRP A CZ3 
2016 C  CH2 . TRP A 247 ? 0.23309  0.212523 0.231543 0.00333457  -0.0287547  -0.0209816  283  TRP A CH2 
2017 N  N   . SER A 248 ? 0.301735 0.286476 0.339607 -0.0283474  -0.0224278  -0.0157827  284  SER A N   
2018 C  CA  . SER A 248 ? 0.335771 0.327531 0.383643 -0.0334066  -0.0219779  -0.0209926  284  SER A CA  
2019 C  C   . SER A 248 ? 0.299589 0.281891 0.35231  -0.0398877  -0.0212418  -0.0212841  284  SER A C   
2020 O  O   . SER A 248 ? 0.300685 0.288087 0.362636 -0.0436244  -0.0219866  -0.0275931  284  SER A O   
2021 C  CB  . SER A 248 ? 0.380945 0.382349 0.431936 -0.0363713  -0.0183446  -0.0203951  284  SER A CB  
2022 O  OG  . SER A 248 ? 0.410616 0.403912 0.455765 -0.0399411  -0.0143993  -0.0130678  284  SER A OG  
2023 N  N   . ASN A 249 ? 0.279066 0.247293 0.325909 -0.0404542  -0.0206425  -0.0153689  285  ASN A N   
2024 C  CA  . ASN A 249 ? 0.277429 0.234348 0.32839  -0.0461276  -0.020245   -0.0155312  285  ASN A CA  
2025 C  C   . ASN A 249 ? 0.269827 0.224443 0.325746 -0.0439486  -0.024433   -0.0227844  285  ASN A C   
2026 O  O   . ASN A 249 ? 0.274806 0.221361 0.336157 -0.0493712  -0.0240257  -0.0246379  285  ASN A O   
2027 C  CB  . ASN A 249 ? 0.333461 0.274872 0.376966 -0.047521   -0.0187749  -0.00702165 285  ASN A CB  
2028 C  CG  . ASN A 249 ? 0.408653 0.352398 0.448301 -0.0524297  -0.0137582  -0.00093184 285  ASN A CG  
2029 O  OD1 . ASN A 249 ? 0.363009 0.313253 0.409115 -0.0592708  -0.0101401  -0.00321912 285  ASN A OD1 
2030 N  ND2 . ASN A 249 ? 0.367527 0.307997 0.397429 -0.0492276  -0.0133074  0.00577935  285  ASN A ND2 
2031 N  N   . ILE A 250 ? 0.273984 0.234959 0.327702 -0.036674   -0.0280416  -0.0270362  286  ILE A N   
2032 C  CA  . ILE A 250 ? 0.278821 0.240019 0.336652 -0.0345076  -0.031929   -0.0351882  286  ILE A CA  
2033 C  C   . ILE A 250 ? 0.285089 0.261269 0.348813 -0.0343137  -0.0340487  -0.0431731  286  ILE A C   
2034 O  O   . ILE A 250 ? 0.275251 0.254563 0.340168 -0.0311078  -0.0378172  -0.0503019  286  ILE A O   
2035 C  CB  . ILE A 250 ? 0.279586 0.236839 0.330101 -0.0267536  -0.0343291  -0.0349606  286  ILE A CB  
2036 C  CG1 . ILE A 250 ? 0.318635 0.285136 0.362056 -0.0213298  -0.0341838  -0.0329167  286  ILE A CG1 
2037 C  CG2 . ILE A 250 ? 0.27669  0.21984  0.323444 -0.0266292  -0.0332283  -0.0281585  286  ILE A CG2 
2038 C  CD1 . ILE A 250 ? 0.428603 0.395494 0.466338 -0.014645   -0.0362956  -0.0357254  286  ILE A CD1 
2039 N  N   . TYR A 251 ? 0.313498 0.299453 0.381536 -0.0378485  -0.031827   -0.0427231  287  TYR A N   
2040 C  CA  . TYR A 251 ? 0.332877 0.333943 0.408094 -0.0374343  -0.0344321  -0.0507116  287  TYR A CA  
2041 C  C   . TYR A 251 ? 0.371853 0.373246 0.456185 -0.0409364  -0.0373941  -0.0599723  287  TYR A C   
2042 O  O   . TYR A 251 ? 0.347538 0.358827 0.433678 -0.0369014  -0.0421505  -0.067792   287  TYR A O   
2043 C  CB  . TYR A 251 ? 0.360334 0.371145 0.441378 -0.0420022  -0.0307169  -0.0492695  287  TYR A CB  
2044 C  CG  . TYR A 251 ? 0.378293 0.406415 0.469033 -0.0412871  -0.0340434  -0.0585956  287  TYR A CG  
2045 C  CD1 . TYR A 251 ? 0.397373 0.435163 0.483409 -0.032318   -0.038624   -0.0610902  287  TYR A CD1 
2046 C  CD2 . TYR A 251 ? 0.3859   0.420155 0.490412 -0.0494068  -0.0331204  -0.0653857  287  TYR A CD2 
2047 C  CE1 . TYR A 251 ? 0.382771 0.436378 0.477005 -0.0302815  -0.0430046  -0.0698321  287  TYR A CE1 
2048 C  CE2 . TYR A 251 ? 0.404902 0.456575 0.519457 -0.0482771  -0.0370483  -0.0750391  287  TYR A CE2 
2049 C  CZ  . TYR A 251 ? 0.454433 0.516118 0.563716 -0.0381766  -0.0423937  -0.0771974  287  TYR A CZ  
2050 O  OH  . TYR A 251 ? 0.475124 0.554444 0.593981 -0.0359428  -0.0473719  -0.086882   287  TYR A OH  
2051 N  N   . ASP A 252 ? 0.392903 0.383412 0.482893 -0.048615   -0.0348298  -0.0596092  288  ASP A N   
2052 C  CA  . ASP A 252 ? 0.436683 0.425785 0.535785 -0.0525326  -0.0374212  -0.0689353  288  ASP A CA  
2053 C  C   . ASP A 252 ? 0.386771 0.371916 0.480389 -0.0452798  -0.0423909  -0.0737965  288  ASP A C   
2054 O  O   . ASP A 252 ? 0.397217 0.387892 0.497146 -0.0458403  -0.0461084  -0.0838023  288  ASP A O   
2055 C  CB  . ASP A 252 ? 0.519615 0.493512 0.623747 -0.0619637  -0.0332294  -0.0661085  288  ASP A CB  
2056 C  CG  . ASP A 252 ? 0.63478  0.59     0.72842  -0.058963   -0.0319905  -0.0569546  288  ASP A CG  
2057 O  OD1 . ASP A 252 ? 0.785937 0.741154 0.871023 -0.0556284  -0.0300028  -0.0485127  288  ASP A OD1 
2058 O  OD2 . ASP A 252 ? 0.752058 0.693706 0.846262 -0.0589932  -0.0336405  -0.0591121  288  ASP A OD2 
2059 N  N   . LEU A 253 ? 0.354981 0.331646 0.437466 -0.0387454  -0.0423954  -0.0677841  289  LEU A N   
2060 C  CA  . LEU A 253 ? 0.356671 0.332412 0.433876 -0.031841   -0.0463032  -0.0730806  289  LEU A CA  
2061 C  C   . LEU A 253 ? 0.380958 0.371274 0.451866 -0.0248929  -0.049494   -0.0761225  289  LEU A C   
2062 O  O   . LEU A 253 ? 0.404547 0.395689 0.470478 -0.0197864  -0.0524835  -0.0813436  289  LEU A O   
2063 C  CB  . LEU A 253 ? 0.320165 0.284312 0.388408 -0.026961   -0.0449695  -0.0664568  289  LEU A CB  
2064 C  CG  . LEU A 253 ? 0.310585 0.257884 0.380956 -0.030976   -0.0424977  -0.060989   289  LEU A CG  
2065 C  CD1 . LEU A 253 ? 0.317613 0.258121 0.379227 -0.0247667  -0.0418465  -0.0544321  289  LEU A CD1 
2066 C  CD2 . LEU A 253 ? 0.347264 0.285245 0.425895 -0.0346453  -0.0443471  -0.0689677  289  LEU A CD2 
2067 N  N   . VAL A 254 ? 0.292249 0.292722 0.361896 -0.0239837  -0.0487849  -0.0725968  290  VAL A N   
2068 C  CA  . VAL A 254 ? 0.296585 0.306598 0.357124 -0.0161617  -0.0516736  -0.0731888  290  VAL A CA  
2069 C  C   . VAL A 254 ? 0.32352  0.348937 0.390303 -0.0161165  -0.0548927  -0.0786211  290  VAL A C   
2070 O  O   . VAL A 254 ? 0.363401 0.396015 0.422452 -0.00949395 -0.0572822  -0.0776271  290  VAL A O   
2071 C  CB  . VAL A 254 ? 0.255496 0.262357 0.305284 -0.0118636  -0.0486603  -0.0634295  290  VAL A CB  
2072 C  CG1 . VAL A 254 ? 0.270113 0.264186 0.314429 -0.0110622  -0.0460006  -0.0586667  290  VAL A CG1 
2073 C  CG2 . VAL A 254 ? 0.209377 0.218644 0.263152 -0.015518   -0.0452129  -0.0575358  290  VAL A CG2 
2074 N  N   . VAL A 255 ? 0.333891 0.364357 0.414535 -0.023308   -0.0547517  -0.0839061  291  VAL A N   
2075 C  CA  . VAL A 255 ? 0.361326 0.408546 0.450446 -0.0235589  -0.0573869  -0.0892717  291  VAL A CA  
2076 C  C   . VAL A 255 ? 0.344925 0.402499 0.427866 -0.0150245  -0.064547   -0.0957349  291  VAL A C   
2077 O  O   . VAL A 255 ? 0.296843 0.354239 0.380406 -0.0148911  -0.0681285  -0.103355   291  VAL A O   
2078 C  CB  . VAL A 255 ? 0.404319 0.457092 0.510518 -0.0328399  -0.0572468  -0.0977577  291  VAL A CB  
2079 C  CG1 . VAL A 255 ? 0.412305 0.484642 0.528884 -0.0328889  -0.0596168  -0.103525   291  VAL A CG1 
2080 C  CG2 . VAL A 255 ? 0.403198 0.443525 0.51512  -0.0425477  -0.0504165  -0.0924715  291  VAL A CG2 
2081 N  N   . PRO A 256 ? 0.334288 0.40147  0.411926 -0.00797092 -0.0672671  -0.0939412  292  PRO A N   
2082 C  CA  . PRO A 256 ? 0.301235 0.377164 0.371093 0.00065827  -0.0746392  -0.0993709  292  PRO A CA  
2083 C  C   . PRO A 256 ? 0.345482 0.435026 0.427781 -0.00154563 -0.0804247  -0.11209    292  PRO A C   
2084 O  O   . PRO A 256 ? 0.374592 0.466517 0.451103 0.00241189  -0.0858229  -0.118641   292  PRO A O   
2085 C  CB  . PRO A 256 ? 0.276077 0.356763 0.338143 0.0084189   -0.075909   -0.0935513  292  PRO A CB  
2086 C  CG  . PRO A 256 ? 0.28397  0.355747 0.346736 0.00418999  -0.0683327  -0.084169   292  PRO A CG  
2087 C  CD  . PRO A 256 ? 0.28148  0.348537 0.356758 -0.00664654 -0.0634446  -0.0855164  292  PRO A CD  
2088 N  N   . PHE A 257 ? 0.355581 0.455017 0.455089 -0.00812998 -0.0791374  -0.116188   293  PHE A N   
2089 C  CA  . PHE A 257 ? 0.389474 0.504048 0.503165 -0.0109629  -0.0846612  -0.129457   293  PHE A CA  
2090 C  C   . PHE A 257 ? 0.405169 0.516704 0.535709 -0.0240834  -0.0793291  -0.133315   293  PHE A C   
2091 O  O   . PHE A 257 ? 0.332853 0.453396 0.477194 -0.0300461  -0.0761296  -0.134394   293  PHE A O   
2092 C  CB  . PHE A 257 ? 0.344137 0.478112 0.465068 -0.00600912 -0.0893468  -0.133435   293  PHE A CB  
2093 C  CG  . PHE A 257 ? 0.374524 0.511327 0.478573 0.00740175  -0.0965981  -0.131725   293  PHE A CG  
2094 C  CD1 . PHE A 257 ? 0.369051 0.512192 0.467671 0.0127277   -0.104876   -0.140257   293  PHE A CD1 
2095 C  CD2 . PHE A 257 ? 0.380072 0.512122 0.472747 0.0144371   -0.0950079  -0.121569   293  PHE A CD2 
2096 C  CE1 . PHE A 257 ? 0.371426 0.515759 0.45246  0.0248848   -0.111317   -0.137786   293  PHE A CE1 
2097 C  CE2 . PHE A 257 ? 0.393571 0.526067 0.46976  0.0263432   -0.101438   -0.119437   293  PHE A CE2 
2098 C  CZ  . PHE A 257 ? 0.334366 0.472892 0.404204 0.031631    -0.109569   -0.127111   293  PHE A CZ  
2099 N  N   . PRO A 258 ? 0.421135 0.519979 0.551105 -0.0288996  -0.0780715  -0.135799   294  PRO A N   
2100 C  CA  . PRO A 258 ? 0.506413 0.598154 0.650462 -0.0414467  -0.0726159  -0.138095   294  PRO A CA  
2101 C  C   . PRO A 258 ? 0.464892 0.574731 0.628773 -0.0480745  -0.0753121  -0.150891   294  PRO A C   
2102 O  O   . PRO A 258 ? 0.446438 0.553819 0.623945 -0.0595809  -0.069655   -0.15216    294  PRO A O   
2103 C  CB  . PRO A 258 ? 0.507915 0.582451 0.64591  -0.0425488  -0.0724888  -0.139379   294  PRO A CB  
2104 C  CG  . PRO A 258 ? 0.532813 0.612684 0.657545 -0.031448   -0.0795971  -0.143198   294  PRO A CG  
2105 C  CD  . PRO A 258 ? 0.486138 0.57641  0.602021 -0.0226437  -0.0815849  -0.136969   294  PRO A CD  
2106 N  N   . SER A 259 ? 0.4138   0.541451 0.578631 -0.0408306  -0.0838984  -0.160181   295  SER A N   
2107 C  CA  . SER A 259 ? 0.575638 0.723557 0.759968 -0.045871   -0.0878451  -0.173921   295  SER A CA  
2108 C  C   . SER A 259 ? 0.564019 0.725849 0.761158 -0.0493898  -0.0840047  -0.172263   295  SER A C   
2109 O  O   . SER A 259 ? 0.52892  0.706658 0.745853 -0.0569329  -0.0842817  -0.182726   295  SER A O   
2110 C  CB  . SER A 259 ? 0.638661 0.802124 0.818477 -0.0355167  -0.0991884  -0.184021   295  SER A CB  
2111 O  OG  . SER A 259 ? 0.64103  0.808279 0.80595  -0.0229384  -0.102599   -0.176358   295  SER A OG  
2112 N  N   . ALA A 260 ? 0.499285 0.657018 0.685753 -0.043519   -0.0807767  -0.160377   296  ALA A N   
2113 C  CA  . ALA A 260 ? 0.480305 0.650598 0.677387 -0.0458668  -0.0766886  -0.158583   296  ALA A CA  
2114 C  C   . ALA A 260 ? 0.576613 0.729917 0.771636 -0.0548367  -0.0655051  -0.147174   296  ALA A C   
2115 O  O   . ALA A 260 ? 0.583432 0.727808 0.765348 -0.0496108  -0.0623357  -0.1357     296  ALA A O   
2116 C  CB  . ALA A 260 ? 0.428528 0.607287 0.615265 -0.0320251  -0.081916   -0.15469    296  ALA A CB  
2117 N  N   . PRO A 261 ? 0.671902 0.820826 0.879968 -0.0688065  -0.0592087  -0.15019    297  PRO A N   
2118 C  CA  . PRO A 261 ? 0.622085 0.749477 0.824121 -0.0769658  -0.0496557  -0.138747   297  PRO A CA  
2119 C  C   . PRO A 261 ? 0.550114 0.685444 0.757193 -0.0807844  -0.0424053  -0.133422   297  PRO A C   
2120 O  O   . PRO A 261 ? 0.456696 0.614584 0.677118 -0.0803193  -0.0438573  -0.141146   297  PRO A O   
2121 C  CB  . PRO A 261 ? 0.665032 0.785981 0.879617 -0.0897223  -0.0473535  -0.146285   297  PRO A CB  
2122 C  CG  . PRO A 261 ? 0.745575 0.892808 0.980546 -0.0926483  -0.051951   -0.162073   297  PRO A CG  
2123 C  CD  . PRO A 261 ? 0.713651 0.879263 0.943703 -0.0779482  -0.0604031  -0.164484   297  PRO A CD  
2124 N  N   . SER A 262 ? 0.530065 0.648144 0.726422 -0.0838158  -0.0349021  -0.120722   298  SER A N   
2125 C  CA  . SER A 262 ? 0.62956  0.756212 0.832437 -0.0897003  -0.0271306  -0.117529   298  SER A CA  
2126 C  C   . SER A 262 ? 0.550704 0.65749  0.748437 -0.100683   -0.017341   -0.107523   298  SER A C   
2127 O  O   . SER A 262 ? 0.519084 0.60414  0.705845 -0.101104   -0.0173219  -0.101225   298  SER A O   
2128 C  CB  . SER A 262 ? 0.693509 0.830117 0.889245 -0.0784815  -0.0289246  -0.113488   298  SER A CB  
2129 O  OG  . SER A 262 ? 0.635574 0.755222 0.81108  -0.0696238  -0.0305065  -0.102783   298  SER A OG  
2130 N  N   . MET A 263 ? 0.553268 0.668323 0.759052 -0.109317   -0.00911435 -0.10652    299  MET A N   
2131 C  CA  . MET A 263 ? 0.541451 0.638471 0.741074 -0.120016   0.00054664  -0.0965953  299  MET A CA  
2132 C  C   . MET A 263 ? 0.595099 0.674152 0.773317 -0.11231    0.00087284  -0.0829793  299  MET A C   
2133 O  O   . MET A 263 ? 0.734879 0.819956 0.905388 -0.100622   -0.00355106 -0.0810742  299  MET A O   
2134 C  CB  . MET A 263 ? 0.471175 0.583883 0.683202 -0.130161   0.00947377  -0.0991209  299  MET A CB  
2135 C  CG  . MET A 263 ? 0.472248 0.603771 0.707076 -0.137942   0.00865546  -0.113769   299  MET A CG  
2136 S  SD  . MET A 263 ? 0.528642 0.680658 0.778652 -0.149976   0.0202628   -0.117094   299  MET A SD  
2137 C  CE  . MET A 263 ? 0.450308 0.575088 0.678056 -0.155293   0.0303561   -0.098585   299  MET A CE  
2138 N  N   . ASP A 264 ? 0.60986  0.6657   0.778259 -0.118601   0.0055781   -0.0736741  300  ASP A N   
2139 C  CA  . ASP A 264 ? 0.554178 0.59559  0.703805 -0.112524   0.00673001  -0.0611034  300  ASP A CA  
2140 C  C   . ASP A 264 ? 0.549385 0.596806 0.697846 -0.118831   0.0157146   -0.0559342  300  ASP A C   
2141 O  O   . ASP A 264 ? 0.440062 0.486864 0.595462 -0.13159    0.0234119   -0.0562262  300  ASP A O   
2142 C  CB  . ASP A 264 ? 0.675611 0.691277 0.814321 -0.112183   0.00481846  -0.0545522  300  ASP A CB  
2143 C  CG  . ASP A 264 ? 0.800471 0.798725 0.921337 -0.109872   0.0077537   -0.0410178  300  ASP A CG  
2144 O  OD1 . ASP A 264 ? 0.782864 0.781805 0.893673 -0.0989468  0.00356883  -0.0374715  300  ASP A OD1 
2145 O  OD2 . ASP A 264 ? 0.822961 0.80735  0.940058 -0.119337   0.0142755   -0.0342972  300  ASP A OD2 
2146 N  N   . THR A 265 ? 0.551739 0.605722 0.691723 -0.110276   0.01515     -0.0518941  301  THR A N   
2147 C  CA  . THR A 265 ? 0.522159 0.584378 0.661532 -0.115389   0.0233909   -0.0486997  301  THR A CA  
2148 C  C   . THR A 265 ? 0.516784 0.558894 0.645647 -0.125623   0.0310763   -0.0382915  301  THR A C   
2149 O  O   . THR A 265 ? 0.457283 0.503635 0.592328 -0.137555   0.0397225   -0.0388417  301  THR A O   
2150 C  CB  . THR A 265 ? 0.629786 0.696832 0.759063 -0.103591   0.0204912   -0.0452641  301  THR A CB  
2151 O  OG1 . THR A 265 ? 0.647161 0.725499 0.782388 -0.0932164  0.0118486   -0.0530027  301  THR A OG1 
2152 C  CG2 . THR A 265 ? 0.592659 0.672924 0.723191 -0.106579   0.0278697   -0.0448336  301  THR A CG2 
2153 N  N   . THR A 266 ? 0.575806 0.595895 0.688912 -0.120691   0.0275535   -0.0291473  302  THR A N   
2154 C  CA  . THR A 266 ? 0.554857 0.55239  0.653846 -0.126788   0.0324092   -0.0175367  302  THR A CA  
2155 C  C   . THR A 266 ? 0.555406 0.544443 0.661873 -0.140842   0.0383596   -0.0184495  302  THR A C   
2156 O  O   . THR A 266 ? 0.59541  0.578283 0.696424 -0.150703   0.0470147   -0.0121077  302  THR A O   
2157 C  CB  . THR A 266 ? 0.491638 0.469481 0.576918 -0.117753   0.0255274   -0.0106469  302  THR A CB  
2158 O  OG1 . THR A 266 ? 0.561156 0.548458 0.639628 -0.107616   0.0227391   -0.00931186 302  THR A OG1 
2159 C  CG2 . THR A 266 ? 0.542786 0.496342 0.613998 -0.123175   0.0292153   0.0009756   302  THR A CG2 
2160 N  N   . GLU A 267 ? 0.591798 0.580501 0.710367 -0.141932   0.0338442   -0.0266763  303  GLU A N   
2161 C  CA  . GLU A 267 ? 0.637826 0.619269 0.766193 -0.155458   0.0388403   -0.0297048  303  GLU A CA  
2162 C  C   . GLU A 267 ? 0.59421  0.5958   0.736144 -0.166877   0.0477721   -0.0355996  303  GLU A C   
2163 O  O   . GLU A 267 ? 0.61952  0.612364 0.763065 -0.180731   0.0563895   -0.0328481  303  GLU A O   
2164 C  CB  . GLU A 267 ? 0.74682  0.730455 0.886825 -0.151472   0.0305777   -0.0401607  303  GLU A CB  
2165 C  CG  . GLU A 267 ? 0.947294 0.908352 1.08878  -0.160249   0.0317814   -0.0393173  303  GLU A CG  
2166 C  CD  . GLU A 267 ? 1.01968  0.987169 1.17333  -0.155475   0.0233155   -0.0515972  303  GLU A CD  
2167 O  OE1 . GLU A 267 ? 1.08003  1.0445   1.22633  -0.14275    0.0151822   -0.0513032  303  GLU A OE1 
2168 O  OE2 . GLU A 267 ? 1.00448  0.98187  1.17522  -0.164617   0.0250413   -0.062107   303  GLU A OE2 
2169 N  N   . ALA A 268 ? 0.605027 0.633882 0.757679 -0.161257   0.0457999   -0.0443856  304  ALA A N   
2170 C  CA  . ALA A 268 ? 0.58832  0.640399 0.756727 -0.170735   0.0536083   -0.0521342  304  ALA A CA  
2171 C  C   . ALA A 268 ? 0.515943 0.567668 0.672984 -0.175642   0.0635214   -0.0431586  304  ALA A C   
2172 O  O   . ALA A 268 ? 0.439538 0.500933 0.60533  -0.188448   0.0735561   -0.0458116  304  ALA A O   
2173 C  CB  . ALA A 268 ? 0.505789 0.586227 0.689264 -0.161259   0.0467878   -0.0648252  304  ALA A CB  
2174 N  N   . MET A 269 ? 0.534841 0.577182 0.672901 -0.165299   0.0606452   -0.0335128  305  MET A N   
2175 C  CA  . MET A 269 ? 0.567445 0.608112 0.691988 -0.168727   0.0690565   -0.0247483  305  MET A CA  
2176 C  C   . MET A 269 ? 0.611079 0.628952 0.724976 -0.182407   0.0776865   -0.014684   305  MET A C   
2177 O  O   . MET A 269 ? 0.592544 0.616949 0.707679 -0.194209   0.0888416   -0.0137713  305  MET A O   
2178 C  CB  . MET A 269 ? 0.484287 0.518987 0.591077 -0.15513    0.0635427   -0.0172441  305  MET A CB  
2179 C  CG  . MET A 269 ? 0.443234 0.500682 0.55698  -0.143532   0.0587155   -0.0250742  305  MET A CG  
2180 S  SD  . MET A 269 ? 0.486688 0.530059 0.581233 -0.128162   0.0497816   -0.0168796  305  MET A SD  
2181 C  CE  . MET A 269 ? 0.435054 0.478046 0.515841 -0.134701   0.0604234   -0.00885192 305  MET A CE  
2182 N  N   . LEU A 270 ? 0.627796 0.618549 0.730578 -0.180299   0.0725102   -0.00705895 306  LEU A N   
2183 C  CA  . LEU A 270 ? 0.586239 0.550759 0.679532 -0.191961   0.0784651   0.00220061  306  LEU A CA  
2184 C  C   . LEU A 270 ? 0.591627 0.565898 0.703645 -0.207891   0.086967    -0.00617494 306  LEU A C   
2185 O  O   . LEU A 270 ? 0.600799 0.575779 0.709346 -0.220069   0.0984236   -0.00210875 306  LEU A O   
2186 C  CB  . LEU A 270 ? 0.600006 0.537276 0.684706 -0.186227   0.0701515   0.00771574  306  LEU A CB  
2187 C  CG  . LEU A 270 ? 0.603785 0.525293 0.667679 -0.173112   0.0631759   0.0183446   306  LEU A CG  
2188 C  CD1 . LEU A 270 ? 0.538845 0.443173 0.602602 -0.164962   0.0531087   0.0177922   306  LEU A CD1 
2189 C  CD2 . LEU A 270 ? 0.578508 0.480314 0.620689 -0.178469   0.0697276   0.0329891   306  LEU A CD2 
2190 N  N   . LYS A 271 ? 0.548475 0.534125 0.680945 -0.207291   0.0814322   -0.0190224  307  LYS A N   
2191 C  CA  . LYS A 271 ? 0.603032 0.59998  0.756207 -0.222026   0.0881848   -0.0291277  307  LYS A CA  
2192 C  C   . LYS A 271 ? 0.594467 0.614072 0.754889 -0.231762   0.0998213   -0.0322264  307  LYS A C   
2193 O  O   . LYS A 271 ? 0.586031 0.60496  0.754237 -0.248165   0.11015     -0.0337212  307  LYS A O   
2194 C  CB  . LYS A 271 ? 0.645021 0.656152 0.820251 -0.219371   0.0801091   -0.0443426  307  LYS A CB  
2195 C  CG  . LYS A 271 ? 0.764231 0.765222 0.951471 -0.236468   0.0864248   -0.0484326  307  LYS A CG  
2196 C  CD  . LYS A 271 ? 0.807286 0.824711 1.01974  -0.239384   0.0815244   -0.0653907  307  LYS A CD  
2197 C  CE  . LYS A 271 ? 0.890326 0.892229 1.1121   -0.256774   0.0879392   -0.0680378  307  LYS A CE  
2198 N  NZ  . LYS A 271 ? 0.83542  0.857789 1.08269  -0.258601   0.08238     -0.0861955  307  LYS A NZ  
2199 N  N   . GLN A 272 ? 0.643907 0.682946 0.801641 -0.222222   0.0988326   -0.0332762  308  GLN A N   
2200 C  CA  . GLN A 272 ? 0.609297 0.671362 0.775566 -0.231269   0.110075    -0.0377681  308  GLN A CA  
2201 C  C   . GLN A 272 ? 0.589982 0.641086 0.733542 -0.234472   0.118908    -0.0244301  308  GLN A C   
2202 O  O   . GLN A 272 ? 0.565917 0.63743  0.713794 -0.239047   0.127554    -0.0279205  308  GLN A O   
2203 C  CB  . GLN A 272 ? 0.622718 0.718139 0.805067 -0.220603   0.105011    -0.0505124  308  GLN A CB  
2204 C  CG  . GLN A 272 ? 0.720286 0.839995 0.931948 -0.227229   0.10516     -0.0670424  308  GLN A CG  
2205 C  CD  . GLN A 272 ? 0.707168 0.85624  0.933282 -0.21339    0.0967545   -0.0791738  308  GLN A CD  
2206 O  OE1 . GLN A 272 ? 0.673173 0.849732 0.91403  -0.215982   0.10228     -0.0881937  308  GLN A OE1 
2207 N  NE2 . GLN A 272 ? 0.639205 0.781482 0.859363 -0.198045   0.0836246   -0.0786232  308  GLN A NE2 
2208 N  N   . GLY A 273 ? 0.619273 0.638875 0.738998 -0.232548   0.117085    -0.00972398 309  GLY A N   
2209 C  CA  . GLY A 273 ? 0.682217 0.689742 0.778982 -0.237232   0.125876    0.00337378  309  GLY A CA  
2210 C  C   . GLY A 273 ? 0.643747 0.666668 0.73147  -0.225427   0.124038    0.00404673  309  GLY A C   
2211 O  O   . GLY A 273 ? 0.644614 0.673596 0.722963 -0.231373   0.133947    0.00789586  309  GLY A O   
2212 N  N   . TRP A 274 ? 0.584647 0.614032 0.675145 -0.20907    0.111771    -0.00016636 310  TRP A N   
2213 C  CA  . TRP A 274 ? 0.588933 0.62871  0.669461 -0.197709   0.109422    0.00118113  310  TRP A CA  
2214 C  C   . TRP A 274 ? 0.596081 0.611022 0.647759 -0.196635   0.110593    0.0169485   310  TRP A C   
2215 O  O   . TRP A 274 ? 0.638611 0.627976 0.679624 -0.196057   0.106022    0.0254583   310  TRP A O   
2216 C  CB  . TRP A 274 ? 0.517177 0.564675 0.605584 -0.18129    0.095931    -0.00556928 310  TRP A CB  
2217 C  CG  . TRP A 274 ? 0.500346 0.577999 0.613397 -0.17911    0.0948663   -0.0209769  310  TRP A CG  
2218 C  CD1 . TRP A 274 ? 0.54514  0.636979 0.679747 -0.188842   0.0987957   -0.0311388  310  TRP A CD1 
2219 C  CD2 . TRP A 274 ? 0.495481 0.59345  0.614028 -0.166658   0.0900083   -0.0281327  310  TRP A CD2 
2220 N  NE1 . TRP A 274 ? 0.523802 0.644119 0.677114 -0.182274   0.0957405   -0.0442459  310  TRP A NE1 
2221 C  CE2 . TRP A 274 ? 0.507888 0.631589 0.65136  -0.168476   0.09041     -0.0423466  310  TRP A CE2 
2222 C  CE3 . TRP A 274 ? 0.486529 0.582982 0.591833 -0.154142   0.0850828   -0.0242853  310  TRP A CE3 
2223 C  CZ2 . TRP A 274 ? 0.461909 0.608476 0.616249 -0.157354   0.0857706   -0.0520034  310  TRP A CZ2 
2224 C  CZ3 . TRP A 274 ? 0.528095 0.646223 0.644123 -0.14431    0.0814228   -0.0337882  310  TRP A CZ3 
2225 C  CH2 . TRP A 274 ? 0.544373 0.686752 0.684152 -0.145527   0.0816796   -0.0471474  310  TRP A CH2 
2226 N  N   . THR A 275 ? 0.575944 0.598442 0.615222 -0.196281   0.116482    0.0203393   311  THR A N   
2227 C  CA  . THR A 275 ? 0.592004 0.594047 0.603517 -0.192816   0.115732    0.0341271   311  THR A CA  
2228 C  C   . THR A 275 ? 0.65916  0.670432 0.665027 -0.177439   0.107797    0.0322481   311  THR A C   
2229 O  O   . THR A 275 ? 0.589656 0.624714 0.611261 -0.172109   0.106557    0.020921    311  THR A O   
2230 C  CB  . THR A 275 ? 0.621085 0.623995 0.62049  -0.205908   0.129799    0.0396461   311  THR A CB  
2231 O  OG1 . THR A 275 ? 0.662364 0.693982 0.670748 -0.203166   0.1338      0.0298397   311  THR A OG1 
2232 C  CG2 . THR A 275 ? 0.610238 0.610368 0.618895 -0.223425   0.140561    0.0389482   311  THR A CG2 
2233 N  N   . PRO A 276 ? 0.660863 0.654374 0.644498 -0.169925   0.102366    0.0427723   312  PRO A N   
2234 C  CA  . PRO A 276 ? 0.645078 0.647578 0.622823 -0.15709    0.0962472   0.0407822   312  PRO A CA  
2235 C  C   . PRO A 276 ? 0.630457 0.658224 0.614032 -0.158444   0.10367     0.0325763   312  PRO A C   
2236 O  O   . PRO A 276 ? 0.648282 0.69166  0.641366 -0.148668   0.098749    0.0241083   312  PRO A O   
2237 C  CB  . PRO A 276 ? 0.617323 0.597392 0.568279 -0.154858   0.0939801   0.054413    312  PRO A CB  
2238 C  CG  . PRO A 276 ? 0.587497 0.544223 0.536807 -0.158077   0.0905516   0.0612066   312  PRO A CG  
2239 C  CD  . PRO A 276 ? 0.624475 0.588071 0.588432 -0.172459   0.10074     0.0565156   312  PRO A CD  
2240 N  N   . ARG A 277 ? 0.629104 0.660868 0.608547 -0.171128   0.115954    0.0344194   313  ARG A N   
2241 C  CA  . ARG A 277 ? 0.650183 0.704523 0.63189  -0.173151   0.124312    0.0276031   313  ARG A CA  
2242 C  C   . ARG A 277 ? 0.64976  0.730459 0.660047 -0.171625   0.124662    0.0122247   313  ARG A C   
2243 O  O   . ARG A 277 ? 0.638117 0.739149 0.655147 -0.165971   0.125774    0.00350273  313  ARG A O   
2244 C  CB  . ARG A 277 ? 0.7013   0.748449 0.665001 -0.186407   0.136822    0.0362458   313  ARG A CB  
2245 C  CG  . ARG A 277 ? 0.850775 0.921441 0.815152 -0.189627   0.146989    0.0292031   313  ARG A CG  
2246 C  CD  . ARG A 277 ? 0.982867 1.04192  0.918861 -0.197033   0.155542    0.0405605   313  ARG A CD  
2247 N  NE  . ARG A 277 ? 1.01082  1.09449  0.949754 -0.202206   0.167283    0.032356    313  ARG A NE  
2248 C  CZ  . ARG A 277 ? 0.954551 1.0447   0.877867 -0.197408   0.168989    0.0322669   313  ARG A CZ  
2249 N  NH1 . ARG A 277 ? 0.791176 0.904086 0.718575 -0.203364   0.180867    0.0240561   313  ARG A NH1 
2250 N  NH2 . ARG A 277 ? 0.933192 1.00748  0.837501 -0.18692    0.15885     0.0398024   313  ARG A NH2 
2251 N  N   . ARG A 278 ? 0.622024 0.701802 0.649158 -0.175724   0.122714    0.00853704  314  ARG A N   
2252 C  CA  . ARG A 278 ? 0.559036 0.663925 0.613493 -0.174421   0.122303    -0.00612775 314  ARG A CA  
2253 C  C   . ARG A 278 ? 0.472441 0.58244  0.533591 -0.157806   0.10946     -0.0118099  314  ARG A C   
2254 O  O   . ARG A 278 ? 0.422346 0.55507  0.499503 -0.152095   0.108598    -0.023308   314  ARG A O   
2255 C  CB  . ARG A 278 ? 0.556756 0.659405 0.6269   -0.184388   0.123917    -0.00894397 314  ARG A CB  
2256 C  CG  . ARG A 278 ? 0.570537 0.70466  0.667234 -0.186653   0.128017    -0.024488   314  ARG A CG  
2257 C  CD  . ARG A 278 ? 0.631208 0.766852 0.746909 -0.184942   0.119991    -0.0313286  314  ARG A CD  
2258 N  NE  . ARG A 278 ? 0.567519 0.732326 0.711228 -0.186969   0.121673    -0.0468812  314  ARG A NE  
2259 C  CZ  . ARG A 278 ? 0.598976 0.766942 0.758964 -0.196981   0.123675    -0.0521694  314  ARG A CZ  
2260 N  NH1 . ARG A 278 ? 0.632859 0.779777 0.78383  -0.21002    0.1296      -0.0433282  314  ARG A NH1 
2261 N  NH2 . ARG A 278 ? 0.581943 0.774509 0.767357 -0.194062   0.119901    -0.0666969  314  ARG A NH2 
2262 N  N   . MET A 279 ? 0.417003 0.505306 0.465817 -0.150491   0.0998922   -0.00362993 315  MET A N   
2263 C  CA  . MET A 279 ? 0.439466 0.527481 0.490581 -0.135839   0.0881117   -0.00652582 315  MET A CA  
2264 C  C   . MET A 279 ? 0.451546 0.550977 0.497337 -0.127748   0.0883549   -0.00959993 315  MET A C   
2265 O  O   . MET A 279 ? 0.422025 0.535066 0.479859 -0.118507   0.0832642   -0.0183766  315  MET A O   
2266 C  CB  . MET A 279 ? 0.454117 0.516537 0.490936 -0.131557   0.0801049   0.00363942  315  MET A CB  
2267 C  CG  . MET A 279 ? 0.467942 0.516663 0.508298 -0.140317   0.0808338   0.00708216  315  MET A CG  
2268 S  SD  . MET A 279 ? 0.523823 0.5418   0.547534 -0.135638   0.0722375   0.0188744   315  MET A SD  
2269 C  CE  . MET A 279 ? 0.426725 0.442745 0.452666 -0.119591   0.0587412   0.0159449   315  MET A CE  
2270 N  N   . PHE A 280 ? 0.450724 0.545566 0.479184 -0.132208   0.0951435   -0.00310904 316  PHE A N   
2271 C  CA  . PHE A 280 ? 0.425612 0.529022 0.446129 -0.125765   0.0961522   -0.00541423 316  PHE A CA  
2272 C  C   . PHE A 280 ? 0.394726 0.524454 0.431189 -0.127961   0.103668    -0.0173311  316  PHE A C   
2273 O  O   . PHE A 280 ? 0.39507  0.537048 0.437793 -0.118307   0.100385    -0.0251167  316  PHE A O   
2274 C  CB  . PHE A 280 ? 0.397389 0.485969 0.392154 -0.128141   0.0989238   0.00549887  316  PHE A CB  
2275 C  CG  . PHE A 280 ? 0.382004 0.449157 0.363449 -0.120479   0.0884832   0.0141899   316  PHE A CG  
2276 C  CD1 . PHE A 280 ? 0.367133 0.434295 0.344896 -0.108881   0.0808222   0.0122291   316  PHE A CD1 
2277 C  CD2 . PHE A 280 ? 0.375466 0.422344 0.348705 -0.124784   0.0863284   0.0238698   316  PHE A CD2 
2278 C  CE1 . PHE A 280 ? 0.365789 0.415739 0.333685 -0.102087   0.0715499   0.0189284   316  PHE A CE1 
2279 C  CE2 . PHE A 280 ? 0.383286 0.412627 0.345454 -0.117089   0.0768245   0.0307851   316  PHE A CE2 
2280 C  CZ  . PHE A 280 ? 0.364809 0.396453 0.324842 -0.105887   0.0694517   0.0281352   316  PHE A CZ  
2281 N  N   . LYS A 281 ? 0.420676 0.558918 0.464296 -0.140557   0.113777    -0.0191171  317  LYS A N   
2282 C  CA  . LYS A 281 ? 0.390019 0.555534 0.45247  -0.143631   0.121305    -0.0316786  317  LYS A CA  
2283 C  C   . LYS A 281 ? 0.387789 0.567344 0.47342  -0.133825   0.112644    -0.0429845  317  LYS A C   
2284 O  O   . LYS A 281 ? 0.383768 0.583078 0.480902 -0.127309   0.113081    -0.0534195  317  LYS A O   
2285 C  CB  . LYS A 281 ? 0.405684 0.577258 0.474563 -0.160099   0.133281    -0.0319009  317  LYS A CB  
2286 C  CG  . LYS A 281 ? 0.474157 0.634238 0.520454 -0.171533   0.144046    -0.021316   317  LYS A CG  
2287 C  CD  . LYS A 281 ? 0.482006 0.658271 0.522357 -0.169471   0.150952    -0.0263157  317  LYS A CD  
2288 C  CE  . LYS A 281 ? 0.535238 0.709284 0.558931 -0.183511   0.165063    -0.0197763  317  LYS A CE  
2289 N  NZ  . LYS A 281 ? 0.533253 0.721138 0.548861 -0.1791     0.169691    -0.0246826  317  LYS A NZ  
2290 N  N   . GLU A 282 ? 0.383635 0.552919 0.4755   -0.13205    0.104454    -0.0412078  318  GLU A N   
2291 C  CA  . GLU A 282 ? 0.399633 0.580364 0.51032  -0.121791   0.0951032   -0.0509352  318  GLU A CA  
2292 C  C   . GLU A 282 ? 0.396225 0.574711 0.501025 -0.106399   0.0864388   -0.0519977  318  GLU A C   
2293 O  O   . GLU A 282 ? 0.393142 0.587866 0.512672 -0.0977222  0.0824835   -0.0621557  318  GLU A O   
2294 C  CB  . GLU A 282 ? 0.401365 0.571248 0.518122 -0.122038   0.0874628   -0.0492043  318  GLU A CB  
2295 C  CG  . GLU A 282 ? 0.495493 0.671719 0.625392 -0.136066   0.0944287   -0.0522301  318  GLU A CG  
2296 C  CD  . GLU A 282 ? 0.561372 0.767868 0.716066 -0.137327   0.0980225   -0.0669099  318  GLU A CD  
2297 O  OE1 . GLU A 282 ? 0.627732 0.847144 0.7931   -0.124877   0.0902326   -0.0752567  318  GLU A OE1 
2298 O  OE2 . GLU A 282 ? 0.648846 0.865916 0.81242  -0.150616   0.108447    -0.0701246  318  GLU A OE2 
2299 N  N   . ALA A 283 ? 0.360685 0.518963 0.444467 -0.102752   0.0831481   -0.0418519  319  ALA A N   
2300 C  CA  . ALA A 283 ? 0.309728 0.464725 0.386954 -0.0898282  0.0762089   -0.0425991  319  ALA A CA  
2301 C  C   . ALA A 283 ? 0.323384 0.495025 0.402886 -0.0877012  0.0822998   -0.049956   319  ALA A C   
2302 O  O   . ALA A 283 ? 0.311272 0.492923 0.400173 -0.0773543  0.077839    -0.0581185  319  ALA A O   
2303 C  CB  . ALA A 283 ? 0.325475 0.457358 0.381446 -0.0878398  0.0720794   -0.0311161  319  ALA A CB  
2304 N  N   . ASP A 284 ? 0.304767 0.479447 0.37577  -0.0976585  0.0928214   -0.0473875  320  ASP A N   
2305 C  CA  . ASP A 284 ? 0.326595 0.517985 0.39936  -0.0966173  0.099741    -0.0549748  320  ASP A CA  
2306 C  C   . ASP A 284 ? 0.33776  0.553978 0.435836 -0.0936822  0.100854    -0.0688703  320  ASP A C   
2307 O  O   . ASP A 284 ? 0.315452 0.543862 0.419374 -0.0851577  0.100351    -0.0774815  320  ASP A O   
2308 C  CB  . ASP A 284 ? 0.343494 0.534445 0.401714 -0.108448   0.111419    -0.0498022  320  ASP A CB  
2309 C  CG  . ASP A 284 ? 0.418985 0.625582 0.475132 -0.106913   0.118661    -0.0572526  320  ASP A CG  
2310 O  OD1 . ASP A 284 ? 0.406292 0.607833 0.453737 -0.0972771  0.113588    -0.0579405  320  ASP A OD1 
2311 O  OD2 . ASP A 284 ? 0.470581 0.694281 0.533168 -0.11607    0.130076    -0.0625357  320  ASP A OD2 
2312 N  N   . ASP A 285 ? 0.318738 0.542313 0.432177 -0.100248   0.101854    -0.0715723  321  ASP A N   
2313 C  CA  . ASP A 285 ? 0.302095 0.55163  0.441162 -0.0977425  0.102603    -0.0856274  321  ASP A CA  
2314 C  C   . ASP A 285 ? 0.284231 0.534979 0.432151 -0.0814991  0.0899512   -0.0912943  321  ASP A C   
2315 O  O   . ASP A 285 ? 0.270144 0.539217 0.431512 -0.0736503  0.0895292   -0.102362   321  ASP A O   
2316 C  CB  . ASP A 285 ? 0.283353 0.542319 0.438185 -0.10891    0.106537    -0.0885993  321  ASP A CB  
2317 C  CG  . ASP A 285 ? 0.313292 0.600066 0.496386 -0.104656   0.104913    -0.104007   321  ASP A CG  
2318 O  OD1 . ASP A 285 ? 0.3248   0.633306 0.518174 -0.105807   0.112664    -0.113439   321  ASP A OD1 
2319 O  OD2 . ASP A 285 ? 0.31348  0.601087 0.508353 -0.0992585  0.0954089   -0.107228   321  ASP A OD2 
2320 N  N   . PHE A 286 ? 0.242272 0.472539 0.380977 -0.0762545  0.0800849   -0.0833559  322  PHE A N   
2321 C  CA  . PHE A 286 ? 0.272092 0.498711 0.414112 -0.0614452  0.0683293   -0.086174   322  PHE A CA  
2322 C  C   . PHE A 286 ? 0.288718 0.513892 0.422721 -0.0519368  0.0677476   -0.0880566  322  PHE A C   
2323 O  O   . PHE A 286 ? 0.309711 0.545947 0.45504  -0.0411239  0.0633973   -0.0970325  322  PHE A O   
2324 C  CB  . PHE A 286 ? 0.234883 0.439844 0.367212 -0.0582693  0.0589251   -0.0772796  322  PHE A CB  
2325 C  CG  . PHE A 286 ? 0.251025 0.45811  0.392857 -0.04583    0.0477065   -0.0823576  322  PHE A CG  
2326 C  CD1 . PHE A 286 ? 0.258974 0.466633 0.400147 -0.0329224  0.0424919   -0.0861304  322  PHE A CD1 
2327 C  CD2 . PHE A 286 ? 0.269081 0.476215 0.419325 -0.0468537  0.0420257   -0.0831701  322  PHE A CD2 
2328 C  CE1 . PHE A 286 ? 0.275388 0.483341 0.423033 -0.021441   0.0322111   -0.0897618  322  PHE A CE1 
2329 C  CE2 . PHE A 286 ? 0.243828 0.451847 0.399874 -0.0353158  0.0314613   -0.0870253  322  PHE A CE2 
2330 C  CZ  . PHE A 286 ? 0.269835 0.477624 0.423759 -0.0224934  0.0264973   -0.0897255  322  PHE A CZ  
2331 N  N   . PHE A 287 ? 0.270612 0.482238 0.385283 -0.0554958  0.0718004   -0.0801878  323  PHE A N   
2332 C  CA  . PHE A 287 ? 0.297834 0.510038 0.40679  -0.047166   0.0717814   -0.0838647  323  PHE A CA  
2333 C  C   . PHE A 287 ? 0.282689 0.519457 0.406728 -0.0455221  0.0781964   -0.0967443  323  PHE A C   
2334 O  O   . PHE A 287 ? 0.284256 0.525929 0.414847 -0.033734   0.0736968   -0.104255   323  PHE A O   
2335 C  CB  . PHE A 287 ? 0.304727 0.501454 0.391486 -0.0505689  0.0748419   -0.0753661  323  PHE A CB  
2336 C  CG  . PHE A 287 ? 0.282615 0.456049 0.355944 -0.046755   0.0662188   -0.0654539  323  PHE A CG  
2337 C  CD1 . PHE A 287 ? 0.276255 0.437004 0.342181 -0.0541533  0.0652908   -0.0557796  323  PHE A CD1 
2338 C  CD2 . PHE A 287 ? 0.26396  0.427758 0.331768 -0.0362233  0.0596558   -0.0659811  323  PHE A CD2 
2339 C  CE1 . PHE A 287 ? 0.236065 0.376873 0.290195 -0.0506072  0.057878    -0.0474151  323  PHE A CE1 
2340 C  CE2 . PHE A 287 ? 0.262328 0.405901 0.318218 -0.0337675  0.0526862   -0.0571794  323  PHE A CE2 
2341 C  CZ  . PHE A 287 ? 0.238778 0.372131 0.288498 -0.040599   0.0517934   -0.0484168  323  PHE A CZ  
2342 N  N   . THR A 288 ? 0.301833 0.553542 0.430763 -0.0571116  0.0891407   -0.0995098  324  THR A N   
2343 C  CA  . THR A 288 ? 0.311908 0.588605 0.455711 -0.0557272  0.0960226   -0.112588   324  THR A CA  
2344 C  C   . THR A 288 ? 0.276439 0.570854 0.445255 -0.0480085  0.0901956   -0.123584   324  THR A C   
2345 O  O   . THR A 288 ? 0.291516 0.604576 0.473795 -0.0413019  0.0919529   -0.135481   324  THR A O   
2346 C  CB  . THR A 288 ? 0.338134 0.629268 0.481974 -0.0702564  0.1105      -0.114247   324  THR A CB  
2347 O  OG1 . THR A 288 ? 0.331722 0.621944 0.482663 -0.0789641  0.110301    -0.110335   324  THR A OG1 
2348 C  CG2 . THR A 288 ? 0.34     0.616227 0.458347 -0.077881   0.116923    -0.10416    324  THR A CG2 
2349 N  N   . SER A 289 ? 0.247197 0.536808 0.422439 -0.048216   0.0830346   -0.120537   325  SER A N   
2350 C  CA  . SER A 289 ? 0.235998 0.543173 0.434219 -0.0398062  0.0763281   -0.131449   325  SER A CA  
2351 C  C   . SER A 289 ? 0.258722 0.560837 0.456888 -0.0220671  0.0662588   -0.135212   325  SER A C   
2352 O  O   . SER A 289 ? 0.221167 0.541478 0.437829 -0.0125669  0.062489    -0.146863   325  SER A O   
2353 C  CB  . SER A 289 ? 0.212748 0.516874 0.41772  -0.0431318  0.0702841   -0.128631   325  SER A CB  
2354 O  OG  . SER A 289 ? 0.206566 0.487532 0.398352 -0.0340776  0.0590479   -0.120309   325  SER A OG  
2355 N  N   . LEU A 290 ? 0.247713 0.524933 0.424869 -0.0181161  0.0623962   -0.125371   326  LEU A N   
2356 C  CA  . LEU A 290 ? 0.290951 0.557324 0.463568 -0.00299692 0.0537308   -0.126492   326  LEU A CA  
2357 C  C   . LEU A 290 ? 0.288598 0.561882 0.461001 0.00207578  0.0588083   -0.133954   326  LEU A C   
2358 O  O   . LEU A 290 ? 0.304737 0.568033 0.473401 0.0144892   0.0523987   -0.13556    326  LEU A O   
2359 C  CB  . LEU A 290 ? 0.325003 0.562613 0.476107 -0.00307252 0.0485796   -0.113093   326  LEU A CB  
2360 C  CG  . LEU A 290 ? 0.269368 0.496808 0.418977 -0.00500257 0.041745    -0.105989   326  LEU A CG  
2361 C  CD1 . LEU A 290 ? 0.267284 0.468557 0.397892 -0.0016342  0.0359476   -0.0953383  326  LEU A CD1 
2362 C  CD2 . LEU A 290 ? 0.283033 0.522121 0.449602 0.00397838  0.0334133   -0.113433   326  LEU A CD2 
2363 N  N   . GLY A 291 ? 0.271675 0.56091  0.447123 -0.00760089 0.0705975   -0.138545   327  GLY A N   
2364 C  CA  . GLY A 291 ? 0.301525 0.595857 0.474073 -0.0037606  0.0759953   -0.145199   327  GLY A CA  
2365 C  C   . GLY A 291 ? 0.323701 0.596629 0.471416 -0.00810941 0.0784621   -0.135273   327  GLY A C   
2366 O  O   . GLY A 291 ? 0.307786 0.582977 0.450435 -0.00582184 0.0829718   -0.140236   327  GLY A O   
2367 N  N   . LEU A 292 ? 0.326508 0.580028 0.45963  -0.0142923  0.075434    -0.122156   328  LEU A N   
2368 C  CA  . LEU A 292 ? 0.360403 0.594661 0.470627 -0.0190703  0.077047    -0.112291   328  LEU A CA  
2369 C  C   . LEU A 292 ? 0.382292 0.62529  0.484812 -0.0324623  0.0891232   -0.110771   328  LEU A C   
2370 O  O   . LEU A 292 ? 0.329795 0.592195 0.444676 -0.0394081  0.096603    -0.116189   328  LEU A O   
2371 C  CB  . LEU A 292 ? 0.339343 0.551105 0.438539 -0.0193     0.0688702   -0.100063   328  LEU A CB  
2372 C  CG  . LEU A 292 ? 0.380071 0.581224 0.483271 -0.00624297 0.0576252   -0.100775   328  LEU A CG  
2373 C  CD1 . LEU A 292 ? 0.324057 0.505973 0.418275 -0.00704663 0.0503347   -0.0897389  328  LEU A CD1 
2374 C  CD2 . LEU A 292 ? 0.411372 0.604616 0.508568 0.00318697  0.0555433   -0.104787   328  LEU A CD2 
2375 N  N   . LEU A 293 ? 0.345522 0.574569 0.427347 -0.036031   0.0910828   -0.103736   329  LEU A N   
2376 C  CA  . LEU A 293 ? 0.362258 0.598751 0.433378 -0.0466465  0.102293    -0.103032   329  LEU A CA  
2377 C  C   . LEU A 293 ? 0.338463 0.570257 0.401986 -0.059816   0.106722    -0.092514   329  LEU A C   
2378 O  O   . LEU A 293 ? 0.345403 0.558871 0.400051 -0.0608621  0.100376    -0.0819496  329  LEU A O   
2379 C  CB  . LEU A 293 ? 0.397016 0.620169 0.448231 -0.044237   0.101306    -0.100058   329  LEU A CB  
2380 C  CG  . LEU A 293 ? 0.368829 0.599357 0.424556 -0.0346465  0.101507    -0.112072   329  LEU A CG  
2381 C  CD1 . LEU A 293 ? 0.413522 0.625151 0.449534 -0.032555   0.0972426   -0.106486   329  LEU A CD1 
2382 C  CD2 . LEU A 293 ? 0.376007 0.629985 0.437334 -0.0392611  0.113399    -0.122478   329  LEU A CD2 
2383 N  N   . PRO A 294 ? 0.370188 0.616886 0.43477  -0.0708308  0.118461    -0.0946022  330  PRO A N   
2384 C  CA  . PRO A 294 ? 0.366246 0.605046 0.421297 -0.0838725  0.123056    -0.083565   330  PRO A CA  
2385 C  C   . PRO A 294 ? 0.394245 0.614618 0.42178  -0.0873422  0.12344     -0.0725182  330  PRO A C   
2386 O  O   . PRO A 294 ? 0.39705  0.6195   0.41459  -0.0838374  0.125374    -0.0761905  330  PRO A O   
2387 C  CB  . PRO A 294 ? 0.366647 0.62835  0.432463 -0.0939441  0.136063    -0.0907725  330  PRO A CB  
2388 C  CG  . PRO A 294 ? 0.364765 0.643726 0.435454 -0.0870151  0.140165    -0.103743   330  PRO A CG  
2389 C  CD  . PRO A 294 ? 0.343175 0.61317  0.416468 -0.0714281  0.128101    -0.107165   330  PRO A CD  
2390 N  N   . VAL A 295 ? 0.387012 0.59041  0.402444 -0.0943861  0.121919    -0.0597135  331  VAL A N   
2391 C  CA  . VAL A 295 ? 0.413279 0.600607 0.402524 -0.0978336  0.122337    -0.0492122  331  VAL A CA  
2392 C  C   . VAL A 295 ? 0.462453 0.660525 0.440797 -0.10809    0.135569    -0.0498268  331  VAL A C   
2393 O  O   . VAL A 295 ? 0.504777 0.716605 0.49466  -0.116424   0.144428    -0.0534492  331  VAL A O   
2394 C  CB  . VAL A 295 ? 0.399939 0.566034 0.38029  -0.101486   0.116604    -0.0358157  331  VAL A CB  
2395 C  CG1 . VAL A 295 ? 0.348931 0.505067 0.338322 -0.0911132  0.10403     -0.0357154  331  VAL A CG1 
2396 C  CG2 . VAL A 295 ? 0.387819 0.556476 0.374326 -0.113535   0.123907    -0.0322243  331  VAL A CG2 
2397 N  N   . PRO A 296 ? 0.466059 0.660959 0.423757 -0.107496   0.137693    -0.0482363  332  PRO A N   
2398 C  CA  . PRO A 296 ? 0.46499  0.670469 0.410134 -0.117176   0.150736    -0.048947   332  PRO A CA  
2399 C  C   . PRO A 296 ? 0.485684 0.683382 0.419573 -0.131027   0.158357    -0.03739    332  PRO A C   
2400 O  O   . PRO A 296 ? 0.4895   0.668081 0.417906 -0.132253   0.151875    -0.0262814  332  PRO A O   
2401 C  CB  . PRO A 296 ? 0.4641   0.663014 0.38648  -0.112616   0.148357    -0.0476537  332  PRO A CB  
2402 C  CG  . PRO A 296 ? 0.458612 0.644255 0.383771 -0.100626   0.134205    -0.0471356  332  PRO A CG  
2403 C  CD  . PRO A 296 ? 0.432463 0.614915 0.378578 -0.0976311  0.127902    -0.0468038  332  PRO A CD  
2404 N  N   A PRO A 297 ? 0.551412 0.762835 0.481216 -0.141995   0.172596    -0.0396488  333  PRO A N   
2405 N  N   B PRO A 297 ? 0.551412 0.762835 0.481216 -0.141995   0.172596    -0.0396488  333  PRO A N   
2406 C  CA  A PRO A 297 ? 0.565254 0.766265 0.480153 -0.156125   0.18082     -0.0273327  333  PRO A CA  
2407 C  CA  B PRO A 297 ? 0.565254 0.766265 0.480153 -0.156125   0.18082     -0.0273327  333  PRO A CA  
2408 C  C   A PRO A 297 ? 0.591339 0.765147 0.476843 -0.156314   0.174499    -0.0110894  333  PRO A C   
2409 C  C   B PRO A 297 ? 0.591339 0.765147 0.476843 -0.156314   0.174499    -0.0110894  333  PRO A C   
2410 O  O   A PRO A 297 ? 0.5855   0.741553 0.463282 -0.163889   0.174553    0.00142006  333  PRO A O   
2411 O  O   B PRO A 297 ? 0.5855   0.741553 0.463282 -0.163889   0.174553    0.00142006  333  PRO A O   
2412 C  CB  A PRO A 297 ? 0.568675 0.789836 0.47882  -0.165261   0.196805    -0.0339345  333  PRO A CB  
2413 C  CB  B PRO A 297 ? 0.568675 0.789836 0.47882  -0.165261   0.196805    -0.0339345  333  PRO A CB  
2414 C  CG  A PRO A 297 ? 0.530833 0.777973 0.467968 -0.157553   0.197614    -0.0523019  333  PRO A CG  
2415 C  CG  B PRO A 297 ? 0.530833 0.777973 0.467968 -0.157553   0.197614    -0.0523019  333  PRO A CG  
2416 C  CD  A PRO A 297 ? 0.524956 0.762399 0.464839 -0.141606   0.181986    -0.0544105  333  PRO A CD  
2417 C  CD  B PRO A 297 ? 0.524956 0.762399 0.464839 -0.141606   0.181986    -0.0544105  333  PRO A CD  
2418 N  N   . GLU A 298 ? 0.632684 0.8034   0.502986 -0.147511   0.168556    -0.0120592  334  GLU A N   
2419 C  CA  . GLU A 298 ? 0.629359 0.777831 0.472876 -0.1448     0.160692    0.00069471  334  GLU A CA  
2420 C  C   . GLU A 298 ? 0.616726 0.745664 0.4659   -0.139337   0.147862    0.00860169  334  GLU A C   
2421 O  O   . GLU A 298 ? 0.657364 0.76579  0.487229 -0.1411     0.143591    0.0219577   334  GLU A O   
2422 C  CB  . GLU A 298 ? 0.649267 0.801798 0.481849 -0.135256   0.155523    -0.0053592  334  GLU A CB  
2423 C  CG  . GLU A 298 ? 0.667062 0.800065 0.470384 -0.1333     0.148465    0.00685676  334  GLU A CG  
2424 C  CD  . GLU A 298 ? 0.698505 0.835553 0.488883 -0.125186   0.143566    0.00092868  334  GLU A CD  
2425 O  OE1 . GLU A 298 ? 0.621227 0.776157 0.423382 -0.121459   0.146911    -0.0130721  334  GLU A OE1 
2426 O  OE2 . GLU A 298 ? 0.750621 0.872629 0.520265 -0.121857   0.135425    0.00974026  334  GLU A OE2 
2427 N  N   . PHE A 299 ? 0.530342 0.665913 0.405444 -0.132122   0.14161     9.18e-06    335  PHE A N   
2428 C  CA  . PHE A 299 ? 0.481586 0.601243 0.36436  -0.12666    0.130009    0.00560912  335  PHE A CA  
2429 C  C   . PHE A 299 ? 0.496084 0.602776 0.376465 -0.136705   0.133362    0.0162738   335  PHE A C   
2430 O  O   . PHE A 299 ? 0.462771 0.549272 0.334955 -0.134978   0.125487    0.0265084   335  PHE A O   
2431 C  CB  . PHE A 299 ? 0.444891 0.574826 0.353968 -0.11734    0.123606    -0.00578258 335  PHE A CB  
2432 C  CG  . PHE A 299 ? 0.45516  0.571496 0.374575 -0.114737   0.114676    -0.00054972 335  PHE A CG  
2433 C  CD1 . PHE A 299 ? 0.448539 0.561736 0.37572  -0.123411   0.118688    0.00357618  335  PHE A CD1 
2434 C  CD2 . PHE A 299 ? 0.461616 0.568327 0.383173 -0.104119   0.102631    -0.00020414 335  PHE A CD2 
2435 C  CE1 . PHE A 299 ? 0.403463 0.504341 0.339478 -0.120753   0.110401    0.00752737  335  PHE A CE1 
2436 C  CE2 . PHE A 299 ? 0.417238 0.512345 0.347605 -0.101791   0.0950016   0.00403706  335  PHE A CE2 
2437 C  CZ  . PHE A 299 ? 0.412031 0.504027 0.349172 -0.109843   0.0986479   0.00787344  335  PHE A CZ  
2438 N  N   . TRP A 300 ? 0.502345 0.621277 0.391647 -0.147308   0.145277    0.0129286   336  TRP A N   
2439 C  CA  . TRP A 300 ? 0.569452 0.677766 0.46152  -0.157629   0.149156    0.0207332   336  TRP A CA  
2440 C  C   . TRP A 300 ? 0.622337 0.710447 0.484616 -0.165579   0.153052    0.0359994   336  TRP A C   
2441 O  O   . TRP A 300 ? 0.625717 0.693476 0.483128 -0.169082   0.149752    0.0465172   336  TRP A O   
2442 C  CB  . TRP A 300 ? 0.512684 0.642533 0.425915 -0.16686    0.160888    0.0108995   336  TRP A CB  
2443 C  CG  . TRP A 300 ? 0.458441 0.60487  0.401739 -0.158977   0.155458    -0.0024465  336  TRP A CG  
2444 C  CD1 . TRP A 300 ? 0.455656 0.626847 0.41564  -0.154363   0.15855     -0.0169277  336  TRP A CD1 
2445 C  CD2 . TRP A 300 ? 0.452139 0.590495 0.411161 -0.154017   0.145327    -0.00227662 336  TRP A CD2 
2446 N  NE1 . TRP A 300 ? 0.458309 0.636399 0.442524 -0.146412   0.150412    -0.0250381  336  TRP A NE1 
2447 C  CE2 . TRP A 300 ? 0.445647 0.604396 0.42936  -0.14642    0.142492    -0.0163446  336  TRP A CE2 
2448 C  CE3 . TRP A 300 ? 0.462152 0.578084 0.416461 -0.154656   0.138164    0.00797656  336  TRP A CE3 
2449 C  CZ2 . TRP A 300 ? 0.430449 0.58746  0.432251 -0.139952   0.132854    -0.019653   336  TRP A CZ2 
2450 C  CZ3 . TRP A 300 ? 0.451793 0.566971 0.425124 -0.148483   0.12908     0.00380867  336  TRP A CZ3 
2451 C  CH2 . TRP A 300 ? 0.421131 0.556785 0.417406 -0.141361   0.126484    -0.00969024 336  TRP A CH2 
2452 N  N   . GLN A 301 ? 0.601995 0.695137 0.443888 -0.16739    0.159266    0.0368939   337  GLN A N   
2453 C  CA  . GLN A 301 ? 0.679141 0.75416  0.489244 -0.173446   0.162501    0.0511456   337  GLN A CA  
2454 C  C   . GLN A 301 ? 0.714515 0.767973 0.507891 -0.16321    0.148125    0.060734    337  GLN A C   
2455 O  O   . GLN A 301 ? 0.73653  0.767939 0.510569 -0.167051   0.146813    0.0746567   337  GLN A O   
2456 C  CB  . GLN A 301 ? 0.718203 0.806983 0.511326 -0.175853   0.171405    0.0474671   337  GLN A CB  
2457 C  CG  . GLN A 301 ? 0.864923 0.974941 0.669183 -0.187677   0.187858    0.0393158   337  GLN A CG  
2458 C  CD  . GLN A 301 ? 1.01024  1.14242  0.809812 -0.185893   0.194818    0.0284196   337  GLN A CD  
2459 O  OE1 . GLN A 301 ? 0.980919 1.11244  0.767518 -0.176179   0.187589    0.026782    337  GLN A OE1 
2460 N  NE2 . GLN A 301 ? 0.98739  1.14058  0.79893  -0.195549   0.209262    0.0197895   337  GLN A NE2 
2461 N  N   . LYS A 302 ? 0.671373 0.730657 0.472224 -0.15031    0.137425    0.0533388   338  LYS A N   
2462 C  CA  . LYS A 302 ? 0.629392 0.67297  0.412481 -0.141046   0.125263    0.0606162   338  LYS A CA  
2463 C  C   . LYS A 302 ? 0.586442 0.617192 0.382855 -0.133247   0.112657    0.0628577   338  LYS A C   
2464 O  O   . LYS A 302 ? 0.595055 0.608775 0.377317 -0.127842   0.103291    0.0716423   338  LYS A O   
2465 C  CB  . LYS A 302 ? 0.659702 0.717186 0.437779 -0.133107   0.122579    0.0515142   338  LYS A CB  
2466 C  CG  . LYS A 302 ? 0.706285 0.768792 0.458813 -0.138481   0.13121     0.0535953   338  LYS A CG  
2467 C  CD  . LYS A 302 ? 0.716804 0.788795 0.463474 -0.128834   0.125058    0.0452444   338  LYS A CD  
2468 C  CE  . LYS A 302 ? 0.792644 0.867978 0.511518 -0.130645   0.129251    0.0467927   338  LYS A CE  
2469 N  NZ  . LYS A 302 ? 0.830501 0.91567  0.543705 -0.142612   0.145254    0.046474    338  LYS A NZ  
2470 N  N   . SER A 303 ? 0.611027 0.650392 0.434622 -0.131932   0.111804    0.0545396   339  SER A N   
2471 C  CA  . SER A 303 ? 0.587021 0.615407 0.422217 -0.124175   0.100084    0.0558639   339  SER A CA  
2472 C  C   . SER A 303 ? 0.620077 0.625992 0.445796 -0.129035   0.0984807   0.0688364   339  SER A C   
2473 O  O   . SER A 303 ? 0.561358 0.562795 0.378685 -0.139916   0.108024    0.0747105   339  SER A O   
2474 C  CB  . SER A 303 ? 0.613735 0.654723 0.477193 -0.122914   0.100262    0.0454966   339  SER A CB  
2475 O  OG  . SER A 303 ? 0.634857 0.694354 0.507593 -0.116949   0.100513    0.0336136   339  SER A OG  
2476 N  N   . MET A 304 ? 0.603753 0.596678 0.434147 -0.121478   0.0872289   0.0719301   340  MET A N   
2477 C  CA  . MET A 304 ? 0.61683  0.588215 0.442387 -0.124889   0.0848201   0.0825526   340  MET A CA  
2478 C  C   . MET A 304 ? 0.631738 0.605271 0.482901 -0.123587   0.0816314   0.076341    340  MET A C   
2479 O  O   . MET A 304 ? 0.558336 0.532095 0.418574 -0.113694   0.0718552   0.0724509   340  MET A O   
2480 C  CB  . MET A 304 ? 0.632378 0.586465 0.442023 -0.115906   0.0732054   0.0909255   340  MET A CB  
2481 C  CG  . MET A 304 ? 0.632536 0.561136 0.429379 -0.118901   0.0709238   0.104135    340  MET A CG  
2482 S  SD  . MET A 304 ? 0.646559 0.561051 0.440427 -0.104854   0.0544397   0.107878    340  MET A SD  
2483 C  CE  . MET A 304 ? 0.587101 0.503783 0.409075 -0.0983445  0.0468129   0.0996725   340  MET A CE  
2484 N  N   . LEU A 305 ? 0.63115  0.605432 0.492972 -0.133802   0.0896695   0.0756964   341  LEU A N   
2485 C  CA  . LEU A 305 ? 0.610527 0.591543 0.497904 -0.132306   0.08685     0.0673676   341  LEU A CA  
2486 C  C   . LEU A 305 ? 0.64154  0.60218  0.531487 -0.133378   0.0817872   0.0737458   341  LEU A C   
2487 O  O   . LEU A 305 ? 0.707094 0.671047 0.615994 -0.130075   0.0770377   0.0673113   341  LEU A O   
2488 C  CB  . LEU A 305 ? 0.525566 0.528762 0.430985 -0.139262   0.0964668   0.0567976   341  LEU A CB  
2489 C  CG  . LEU A 305 ? 0.496727 0.521289 0.40338  -0.135827   0.10005     0.0481239   341  LEU A CG  
2490 C  CD1 . LEU A 305 ? 0.529661 0.576475 0.455646 -0.142624   0.109595    0.0373562   341  LEU A CD1 
2491 C  CD2 . LEU A 305 ? 0.480066 0.509846 0.392453 -0.122235   0.0896846   0.0420622   341  LEU A CD2 
2492 N  N   . GLU A 306 ? 0.663443 0.602075 0.533488 -0.136826   0.0818511   0.0863105   342  GLU A N   
2493 C  CA  . GLU A 306 ? 0.684681 0.6011   0.554238 -0.134938   0.0749161   0.0929121   342  GLU A CA  
2494 C  C   . GLU A 306 ? 0.735682 0.631869 0.579858 -0.130089   0.0692914   0.105265    342  GLU A C   
2495 O  O   . GLU A 306 ? 0.770979 0.668419 0.596522 -0.132339   0.0736576   0.11014     342  GLU A O   
2496 C  CB  . GLU A 306 ? 0.779771 0.680211 0.644447 -0.147872   0.083032    0.10044     342  GLU A CB  
2497 C  CG  . GLU A 306 ? 0.865778 0.779923 0.750879 -0.159014   0.0925553   0.0920461   342  GLU A CG  
2498 C  CD  . GLU A 306 ? 0.942613 0.865836 0.819332 -0.170889   0.106178    0.0934273   342  GLU A CD  
2499 O  OE1 . GLU A 306 ? 0.855612 0.784358 0.743846 -0.183301   0.116032    0.0900446   342  GLU A OE1 
2500 O  OE2 . GLU A 306 ? 0.994485 0.920097 0.852936 -0.167552   0.106844    0.0973827   342  GLU A OE2 
2501 N  N   . LYS A 307 ? 0.741234 0.618744 0.584047 -0.12376    0.059953    0.110292    343  LYS A N   
2502 C  CA  . LYS A 307 ? 0.835831 0.690996 0.654679 -0.120454   0.0551373   0.123156    343  LYS A CA  
2503 C  C   . LYS A 307 ? 1.03978  0.885731 0.837706 -0.13165    0.0654981   0.132983    343  LYS A C   
2504 O  O   . LYS A 307 ? 1.12188  0.965815 0.925647 -0.143799   0.0753654   0.133198    343  LYS A O   
2505 C  CB  . LYS A 307 ? 0.860408 0.69474  0.685356 -0.11856    0.0491118   0.126784    343  LYS A CB  
2506 C  CG  . LYS A 307 ? 0.932533 0.741667 0.7353   -0.113642   0.0426169   0.139703    343  LYS A CG  
2507 C  CD  . LYS A 307 ? 0.934192 0.742873 0.749056 -0.100614   0.0300896   0.134686    343  LYS A CD  
2508 C  CE  . LYS A 307 ? 1.02928  0.818168 0.826083 -0.0914589  0.0204544   0.14458     343  LYS A CE  
2509 N  NZ  . LYS A 307 ? 1.11525  0.911498 0.925586 -0.0789303  0.00955558  0.137143    343  LYS A NZ  
2510 N  N   . PRO A 308 ? 1.12406  0.964541 0.896558 -0.128886   0.0643475   0.14126     344  PRO A N   
2511 C  CA  . PRO A 308 ? 1.05583  0.885711 0.805951 -0.13993    0.0746449   0.151608    344  PRO A CA  
2512 C  C   . PRO A 308 ? 1.02366  0.821573 0.7622   -0.143096   0.0730375   0.164471    344  PRO A C   
2513 O  O   . PRO A 308 ? 1.01938  0.803809 0.763919 -0.134522   0.0624605   0.165724    344  PRO A O   
2514 C  CB  . PRO A 308 ? 1.11152  0.946424 0.838219 -0.134282   0.0722423   0.155371    344  PRO A CB  
2515 C  CG  . PRO A 308 ? 1.12865  0.976079 0.867038 -0.119917   0.059824    0.146709    344  PRO A CG  
2516 C  CD  . PRO A 308 ? 1.10009  0.944453 0.863404 -0.115718   0.0535015   0.140987    344  PRO A CD  
2517 N  N   . THR A 309 ? 1.05525  0.841014 0.777388 -0.155775   0.0841579   0.173672    345  THR A N   
2518 C  CA  . THR A 309 ? 1.23619  0.992957 0.953304 -0.162687   0.0861315   0.183666    345  THR A CA  
2519 C  C   . THR A 309 ? 1.42455  1.15652  1.10577  -0.16546    0.0882405   0.200845    345  THR A C   
2520 O  O   . THR A 309 ? 1.48808  1.19356  1.159    -0.173884   0.0928544   0.211485    345  THR A O   
2521 C  CB  . THR A 309 ? 1.20204  0.968088 0.939617 -0.178025   0.0992193   0.176569    345  THR A CB  
2522 O  OG1 . THR A 309 ? 1.18585  0.929399 0.932078 -0.177238   0.0937222   0.179407    345  THR A OG1 
2523 C  CG2 . THR A 309 ? 1.1052   0.869998 0.827127 -0.19421    0.1153      0.182888    345  THR A CG2 
2524 N  N   . ASP A 310 ? 1.43601  1.17629  1.09777  -0.158086   0.0844883   0.203312    346  ASP A N   
2525 C  CA  . ASP A 310 ? 1.32321  1.04392  0.948272 -0.159027   0.0855207   0.218853    346  ASP A CA  
2526 C  C   . ASP A 310 ? 1.28522  0.990508 0.896289 -0.141854   0.0681433   0.22558     346  ASP A C   
2527 O  O   . ASP A 310 ? 1.3894   1.08946  0.972304 -0.137146   0.0648311   0.234064    346  ASP A O   
2528 C  CB  . ASP A 310 ? 1.28531  1.0271   0.897353 -0.16591    0.0963362   0.216491    346  ASP A CB  
2529 C  CG  . ASP A 310 ? 1.26492  1.03911  0.889699 -0.156537   0.0914142   0.202208    346  ASP A CG  
2530 O  OD1 . ASP A 310 ? 1.18006  0.957163 0.814488 -0.142432   0.0773918   0.197537    346  ASP A OD1 
2531 O  OD2 . ASP A 310 ? 1.27279  1.0696   0.898982 -0.163477   0.101879    0.195067    346  ASP A OD2 
2532 N  N   . GLY A 311 ? 1.17769  0.876884 0.808436 -0.132381   0.0570408   0.221217    347  GLY A N   
2533 C  CA  . GLY A 311 ? 1.13281  0.824619 0.757726 -0.115011   0.0401313   0.223476    347  GLY A CA  
2534 C  C   . GLY A 311 ? 1.1904   0.905466 0.807433 -0.106175   0.0347348   0.218084    347  GLY A C   
2535 O  O   . GLY A 311 ? 1.28817  0.993211 0.881734 -0.0969134  0.0256565   0.226419    347  GLY A O   
2536 N  N   . ARG A 312 ? 1.02622  0.771781 0.66148  -0.109621   0.0408077   0.20432     348  ARG A N   
2537 C  CA  . ARG A 312 ? 1.03519  0.804789 0.672823 -0.0999542  0.0341154   0.19506     348  ARG A CA  
2538 C  C   . ARG A 312 ? 0.957171 0.73812  0.623944 -0.0903857  0.0247596   0.183255    348  ARG A C   
2539 O  O   . ARG A 312 ? 1.07595  0.865492 0.767003 -0.095752   0.0301308   0.174902    348  ARG A O   
2540 C  CB  . ARG A 312 ? 0.963068 0.760996 0.60761  -0.107274   0.0448853   0.184476    348  ARG A CB  
2541 C  CG  . ARG A 312 ? 1.00973  0.810313 0.624651 -0.110603   0.0500252   0.19052     348  ARG A CG  
2542 C  CD  . ARG A 312 ? 0.985318 0.816562 0.610348 -0.114018   0.0576171   0.177186    348  ARG A CD  
2543 N  NE  . ARG A 312 ? 0.98674  0.828243 0.627341 -0.127525   0.0725209   0.17167     348  ARG A NE  
2544 C  CZ  . ARG A 312 ? 0.922321 0.781284 0.594123 -0.129287   0.075554    0.158711    348  ARG A CZ  
2545 N  NH1 . ARG A 312 ? 0.88911  0.754254 0.582205 -0.119233   0.0651799   0.15053     348  ARG A NH1 
2546 N  NH2 . ARG A 312 ? 0.883729 0.753569 0.564991 -0.14162    0.0894313   0.154249    348  ARG A NH2 
2547 N  N   . GLU A 313 ? 0.984734 0.767961 0.64885  -0.0766429  0.0113206   0.181831    349  GLU A N   
2548 C  CA  . GLU A 313 ? 1.04377  0.838503 0.733257 -0.0670323  0.00222222  0.170797    349  GLU A CA  
2549 C  C   . GLU A 313 ? 1.0091   0.833935 0.715363 -0.0671499  0.00526889  0.15631     349  GLU A C   
2550 O  O   . GLU A 313 ? 1.01968  0.857288 0.713635 -0.0677222  0.0075468   0.154521    349  GLU A O   
2551 C  CB  . GLU A 313 ? 1.09746  0.881128 0.778086 -0.0529071  -0.0129747  0.175419    349  GLU A CB  
2552 C  CG  . GLU A 313 ? 1.00561  0.782832 0.70787  -0.045849   -0.0207498  0.171312    349  GLU A CG  
2553 C  CD  . GLU A 313 ? 1.09557  0.855435 0.802825 -0.0559904  -0.0123208  0.17611     349  GLU A CD  
2554 O  OE1 . GLU A 313 ? 1.15037  0.892667 0.836854 -0.0636864  -0.00605411 0.187703    349  GLU A OE1 
2555 O  OE2 . GLU A 313 ? 1.09983  0.864033 0.831233 -0.0568426  -0.0115416  0.168045    349  GLU A OE2 
2556 N  N   . VAL A 314 ? 0.87245  0.707805 0.606417 -0.0661797  0.00497499  0.145796    350  VAL A N   
2557 C  CA  . VAL A 314 ? 0.764436 0.625013 0.516073 -0.0678363  0.00951159  0.132653    350  VAL A CA  
2558 C  C   . VAL A 314 ? 0.702583 0.570397 0.47764  -0.0598388  0.0018787   0.123439    350  VAL A C   
2559 O  O   . VAL A 314 ? 0.693609 0.547714 0.475395 -0.0572381  -0.00256003 0.126312    350  VAL A O   
2560 C  CB  . VAL A 314 ? 0.736843 0.604483 0.497361 -0.0802892  0.0230004   0.129483    350  VAL A CB  
2561 C  CG1 . VAL A 314 ? 0.741989 0.600124 0.480484 -0.0903556  0.0324944   0.139356    350  VAL A CG1 
2562 C  CG2 . VAL A 314 ? 0.696524 0.559973 0.479354 -0.0825522  0.0237668   0.125798    350  VAL A CG2 
2563 N  N   . VAL A 315 ? 0.748339 0.636789 0.535068 -0.0563053  0.00084832  0.112429    351  VAL A N   
2564 C  CA  . VAL A 315 ? 0.723209 0.620519 0.532192 -0.0503251  -0.00425119 0.102943    351  VAL A CA  
2565 C  C   . VAL A 315 ? 0.723931 0.627    0.551187 -0.0572554  0.00369892  0.0972356   351  VAL A C   
2566 O  O   . VAL A 315 ? 0.643485 0.555023 0.469582 -0.0648773  0.0128533   0.0953858   351  VAL A O   
2567 C  CB  . VAL A 315 ? 0.808062 0.723121 0.619213 -0.0447742  -0.00781018 0.0944324   351  VAL A CB  
2568 C  CG1 . VAL A 315 ? 0.615724 0.538882 0.446899 -0.0382978  -0.013449   0.0854924   351  VAL A CG1 
2569 C  CG2 . VAL A 315 ? 0.833382 0.745621 0.623803 -0.0398494  -0.0140821  0.0996007   351  VAL A CG2 
2570 N  N   . CYS A 316 ? 0.776344 0.675881 0.620417 -0.0545703  0.00028818  0.0938955   352  CYS A N   
2571 C  CA  . CYS A 316 ? 0.715623 0.616786 0.574221 -0.0615647  0.00704526  0.090406    352  CYS A CA  
2572 C  C   . CYS A 316 ? 0.736074 0.655849 0.61258  -0.0610703  0.00943902  0.0790708   352  CYS A C   
2573 O  O   . CYS A 316 ? 0.740862 0.668976 0.623028 -0.0681044  0.0174458   0.0757975   352  CYS A O   
2574 C  CB  . CYS A 316 ? 0.672127 0.556507 0.535866 -0.0629147  0.00533107  0.0944924   352  CYS A CB  
2575 S  SG  . CYS A 316 ? 0.846909 0.713166 0.694885 -0.0737195  0.0129312   0.105937    352  CYS A SG  
2576 N  N   . HIS A 317 ? 0.612592 0.538158 0.497787 -0.052995   0.00271392  0.073365    353  HIS A N   
2577 C  CA  . HIS A 317 ? 0.589078 0.530809 0.487354 -0.0510002  0.0038915   0.063531    353  HIS A CA  
2578 C  C   . HIS A 317 ? 0.590291 0.544486 0.488124 -0.0567239  0.0121421   0.0598959   353  HIS A C   
2579 O  O   . HIS A 317 ? 0.639964 0.596645 0.524413 -0.0586878  0.0148678   0.0624034   353  HIS A O   
2580 C  CB  . HIS A 317 ? 0.488791 0.435532 0.386893 -0.0429668  -0.00289089 0.0600292   353  HIS A CB  
2581 C  CG  . HIS A 317 ? 0.416405 0.370962 0.330575 -0.0399599  -0.00388415 0.0520244   353  HIS A CG  
2582 N  ND1 . HIS A 317 ? 0.458581 0.408109 0.381057 -0.0354983  -0.0091001  0.0509155   353  HIS A ND1 
2583 C  CD2 . HIS A 317 ? 0.473408 0.439543 0.395968 -0.0404368  -0.00043927 0.0449863   353  HIS A CD2 
2584 C  CE1 . HIS A 317 ? 0.399709 0.357213 0.33419  -0.0338963  -0.00846144 0.0439443   353  HIS A CE1 
2585 N  NE2 . HIS A 317 ? 0.463726 0.43098  0.398255 -0.0364204  -0.00362902 0.040403    353  HIS A NE2 
2586 N  N   . ALA A 318 ? 0.541956 0.50407  0.454556 -0.059324   0.0160592   0.0537539   354  ALA A N   
2587 C  CA  . ALA A 318 ? 0.527809 0.504049 0.444797 -0.063346   0.0232785   0.0480478   354  ALA A CA  
2588 C  C   . ALA A 318 ? 0.484474 0.47041  0.398554 -0.0582031  0.0217233   0.0429995   354  ALA A C   
2589 O  O   . ALA A 318 ? 0.450987 0.437071 0.369911 -0.0516908  0.0157945   0.0398814   354  ALA A O   
2590 C  CB  . ALA A 318 ? 0.449192 0.432157 0.384283 -0.0639166  0.0245322   0.0414069   354  ALA A CB  
2591 N  N   . SER A 319 ? 0.464084 0.457584 0.369797 -0.0616121  0.0273929   0.0421028   355  SER A N   
2592 C  CA  . SER A 319 ? 0.409192 0.412184 0.312805 -0.0574907  0.0267221   0.0361145   355  SER A CA  
2593 C  C   . SER A 319 ? 0.46007  0.474629 0.361089 -0.0624259  0.0352901   0.0323055   355  SER A C   
2594 O  O   . SER A 319 ? 0.429774 0.44336  0.324779 -0.0696777  0.0416626   0.0366517   355  SER A O   
2595 C  CB  . SER A 319 ? 0.407583 0.404045 0.29806  -0.0532607  0.0202912   0.0401161   355  SER A CB  
2596 O  OG  . SER A 319 ? 0.518256 0.510108 0.391358 -0.0576353  0.0230785   0.0471967   355  SER A OG  
2597 N  N   . ALA A 320 ? 0.4239   0.449305 0.330739 -0.0586552  0.0358747   0.023616    356  ALA A N   
2598 C  CA  . ALA A 320 ? 0.396143 0.434654 0.303449 -0.0614093  0.0434046   0.0173131   356  ALA A CA  
2599 C  C   . ALA A 320 ? 0.407095 0.448165 0.301251 -0.0590292  0.042334    0.0153373   356  ALA A C   
2600 O  O   . ALA A 320 ? 0.468267 0.504921 0.36112  -0.0536021  0.0354323   0.0146449   356  ALA A O   
2601 C  CB  . ALA A 320 ? 0.372544 0.419935 0.29788  -0.0577633  0.0438463   0.00837883  356  ALA A CB  
2602 N  N   . TRP A 321 ? 0.398949 0.447743 0.283677 -0.0633971  0.0492913   0.0139153   357  TRP A N   
2603 C  CA  . TRP A 321 ? 0.438686 0.488615 0.306621 -0.0625366  0.048453    0.0138329   357  TRP A CA  
2604 C  C   . TRP A 321 ? 0.431575 0.49613  0.300579 -0.0632773  0.0553748   0.00401879  357  TRP A C   
2605 O  O   . TRP A 321 ? 0.411074 0.484002 0.281834 -0.0686423  0.0639762   0.00228496  357  TRP A O   
2606 C  CB  . TRP A 321 ? 0.485142 0.526774 0.333972 -0.0681064  0.0502495   0.0247589   357  TRP A CB  
2607 C  CG  . TRP A 321 ? 0.491866 0.518107 0.335979 -0.0656429  0.0419364   0.0340454   357  TRP A CG  
2608 C  CD1 . TRP A 321 ? 0.501577 0.518986 0.356341 -0.0653814  0.0389572   0.0381407   357  TRP A CD1 
2609 C  CD2 . TRP A 321 ? 0.537908 0.556434 0.364576 -0.0625608  0.0351774   0.0398393   357  TRP A CD2 
2610 N  NE1 . TRP A 321 ? 0.565359 0.570151 0.411973 -0.0617694  0.0307953   0.0454127   357  TRP A NE1 
2611 C  CE2 . TRP A 321 ? 0.588376 0.593752 0.41784  -0.0598366  0.0281116   0.0468127   357  TRP A CE2 
2612 C  CE3 . TRP A 321 ? 0.565683 0.588028 0.375089 -0.061419   0.0340648   0.039027    357  TRP A CE3 
2613 C  CZ2 . TRP A 321 ? 0.617291 0.613613 0.43368  -0.0554694  0.0197336   0.0529696   357  TRP A CZ2 
2614 C  CZ3 . TRP A 321 ? 0.647259 0.660833 0.442925 -0.0573666  0.025497    0.0453224   357  TRP A CZ3 
2615 C  CH2 . TRP A 321 ? 0.715233 0.716306 0.515282 -0.0540668  0.0182296   0.0519765   357  TRP A CH2 
2616 N  N   . ASP A 322 ? 0.439588 0.507606 0.308097 -0.0579602  0.0517839   -0.0032045  358  ASP A N   
2617 C  CA  . ASP A 322 ? 0.459143 0.539481 0.325626 -0.0577978  0.0572134   -0.012898   358  ASP A CA  
2618 C  C   . ASP A 322 ? 0.453503 0.533315 0.298236 -0.0588797  0.0560102   -0.0107413  358  ASP A C   
2619 O  O   . ASP A 322 ? 0.470192 0.542389 0.308317 -0.0554138  0.0477465   -0.00775599 358  ASP A O   
2620 C  CB  . ASP A 322 ? 0.421454 0.504248 0.30268  -0.0510134  0.0537119   -0.0229248  358  ASP A CB  
2621 C  CG  . ASP A 322 ? 0.426679 0.521528 0.310474 -0.0495666  0.0590875   -0.034702   358  ASP A CG  
2622 O  OD1 . ASP A 322 ? 0.463444 0.566456 0.336023 -0.0540481  0.0657699   -0.035637   358  ASP A OD1 
2623 O  OD2 . ASP A 322 ? 0.415591 0.511034 0.312245 -0.043987   0.0568713   -0.0427794  358  ASP A OD2 
2624 N  N   . PHE A 323 ? 0.448459 0.537729 0.282824 -0.0633106  0.0641333   -0.0133535  359  PHE A N   
2625 C  CA  . PHE A 323 ? 0.501681 0.591477 0.312782 -0.0650107  0.06404     -0.0109528  359  PHE A CA  
2626 C  C   . PHE A 323 ? 0.497752 0.598692 0.307822 -0.0619934  0.0654524   -0.0237558  359  PHE A C   
2627 O  O   . PHE A 323 ? 0.515021 0.61956  0.305847 -0.0637031  0.0667838   -0.0239467  359  PHE A O   
2628 C  CB  . PHE A 323 ? 0.498988 0.590464 0.292879 -0.0730558  0.0727237   -0.00373384 359  PHE A CB  
2629 C  CG  . PHE A 323 ? 0.501508 0.578421 0.292128 -0.0759267  0.0699509   0.0100124   359  PHE A CG  
2630 C  CD1 . PHE A 323 ? 0.485265 0.56008  0.293939 -0.0780516  0.0723373   0.0116567   359  PHE A CD1 
2631 C  CD2 . PHE A 323 ? 0.58523  0.650144 0.355662 -0.075496   0.0638145   0.0205556   359  PHE A CD2 
2632 C  CE1 . PHE A 323 ? 0.506043 0.566764 0.312996 -0.0803175  0.0693553   0.0230883   359  PHE A CE1 
2633 C  CE2 . PHE A 323 ? 0.597404 0.647394 0.366338 -0.0769801  0.0604183   0.0324738   359  PHE A CE2 
2634 C  CZ  . PHE A 323 ? 0.581772 0.629407 0.369037 -0.0797141  0.063513    0.0335843   359  PHE A CZ  
2635 N  N   . TYR A 324 ? 0.450882 0.556867 0.280568 -0.0577076  0.0656307   -0.0342537  360  TYR A N   
2636 C  CA  . TYR A 324 ? 0.475985 0.58877  0.306506 -0.0536355  0.0648361   -0.0466807  360  TYR A CA  
2637 C  C   . TYR A 324 ? 0.507787 0.633954 0.327745 -0.0571071  0.0740658   -0.0533628  360  TYR A C   
2638 O  O   . TYR A 324 ? 0.546629 0.678085 0.359298 -0.0550587  0.0734103   -0.0620473  360  TYR A O   
2639 C  CB  . TYR A 324 ? 0.533914 0.639713 0.353581 -0.0506696  0.0552204   -0.0452376  360  TYR A CB  
2640 C  CG  . TYR A 324 ? 0.49693  0.591818 0.330735 -0.0468429  0.0472642   -0.0416326  360  TYR A CG  
2641 C  CD1 . TYR A 324 ? 0.548465 0.642914 0.401306 -0.0427516  0.0467051   -0.0497152  360  TYR A CD1 
2642 C  CD2 . TYR A 324 ? 0.502118 0.587038 0.330436 -0.0473202  0.0412058   -0.0300801  360  TYR A CD2 
2643 C  CE1 . TYR A 324 ? 0.597422 0.682126 0.462501 -0.0398091  0.0406608   -0.0461513  360  TYR A CE1 
2644 C  CE2 . TYR A 324 ? 0.562137 0.638413 0.404028 -0.0440851  0.0350311   -0.0274915  360  TYR A CE2 
2645 C  CZ  . TYR A 324 ? 0.601536 0.678045 0.461293 -0.0407657  0.0352248   -0.0353054  360  TYR A CZ  
2646 O  OH  . TYR A 324 ? 0.815204 0.883371 0.687061 -0.0379065  0.029917    -0.0329018  360  TYR A OH  
2647 N  N   . ASN A 325 ? 0.510193 0.642665 0.329907 -0.062714   0.0831476   -0.0502462  361  ASN A N   
2648 C  CA  . ASN A 325 ? 0.574351 0.721552 0.386588 -0.0658898  0.0930187   -0.0584549  361  ASN A CA  
2649 C  C   . ASN A 325 ? 0.525304 0.683934 0.358813 -0.0657839  0.100788    -0.0667965  361  ASN A C   
2650 O  O   . ASN A 325 ? 0.527795 0.700284 0.357917 -0.0691469  0.110407    -0.0734431  361  ASN A O   
2651 C  CB  . ASN A 325 ? 0.562038 0.710268 0.351045 -0.0739544  0.0993546   -0.0490046  361  ASN A CB  
2652 C  CG  . ASN A 325 ? 0.616194 0.761705 0.411518 -0.0801984  0.104822    -0.0395601  361  ASN A CG  
2653 O  OD1 . ASN A 325 ? 0.572347 0.717003 0.39005  -0.0780513  0.10353     -0.0410724  361  ASN A OD1 
2654 N  ND2 . ASN A 325 ? 0.594586 0.7377   0.36977  -0.0879255  0.110496    -0.0296292  361  ASN A ND2 
2655 N  N   . GLY A 326 ? 0.491209 0.644711 0.34526  -0.0622782  0.0968243   -0.0659082  362  GLY A N   
2656 C  CA  . GLY A 326 ? 0.455804 0.620252 0.331651 -0.0602112  0.102062    -0.0748229  362  GLY A CA  
2657 C  C   . GLY A 326 ? 0.476633 0.650553 0.355617 -0.0680677  0.111751    -0.0711701  362  GLY A C   
2658 O  O   . GLY A 326 ? 0.474695 0.661707 0.371079 -0.0670258  0.117336    -0.0799343  362  GLY A O   
2659 N  N   . LYS A 327 ? 0.502053 0.669345 0.364857 -0.0759359  0.113777    -0.0585448  363  LYS A N   
2660 C  CA  . LYS A 327 ? 0.521412 0.697409 0.385862 -0.0849869  0.124342    -0.0553963  363  LYS A CA  
2661 C  C   . LYS A 327 ? 0.524648 0.685732 0.380722 -0.0912971  0.12227     -0.0395994  363  LYS A C   
2662 O  O   . LYS A 327 ? 0.515655 0.680027 0.381261 -0.0976     0.128063    -0.0366274  363  LYS A O   
2663 C  CB  . LYS A 327 ? 0.554852 0.747103 0.408496 -0.0901054  0.136085    -0.0624878  363  LYS A CB  
2664 C  CG  . LYS A 327 ? 0.573339 0.761759 0.398863 -0.0923126  0.136499    -0.0588079  363  LYS A CG  
2665 C  CD  . LYS A 327 ? 0.686736 0.895333 0.509439 -0.0967127  0.149562    -0.0691911  363  LYS A CD  
2666 C  CE  . LYS A 327 ? 0.763837 0.976161 0.56642  -0.0944742  0.1497      -0.0751358  363  LYS A CE  
2667 N  NZ  . LYS A 327 ? 0.861936 1.06186  0.634274 -0.0987912  0.147125    -0.0622532  363  LYS A NZ  
2668 N  N   . ASP A 328 ? 0.49106  0.635566 0.331813 -0.0889173  0.113171    -0.0303109  364  ASP A N   
2669 C  CA  . ASP A 328 ? 0.491782 0.62001  0.323151 -0.0932954  0.109791    -0.0154859  364  ASP A CA  
2670 C  C   . ASP A 328 ? 0.495857 0.611931 0.341119 -0.0866207  0.0984806   -0.0125993  364  ASP A C   
2671 O  O   . ASP A 328 ? 0.502573 0.611177 0.344502 -0.0796402  0.0890511   -0.0128894  364  ASP A O   
2672 C  CB  . ASP A 328 ? 0.534313 0.65406  0.33622  -0.0961109  0.109013    -0.00663673 364  ASP A CB  
2673 C  CG  . ASP A 328 ? 0.619651 0.720776 0.407761 -0.100117   0.105428    0.00940702  364  ASP A CG  
2674 O  OD1 . ASP A 328 ? 0.570698 0.664152 0.372701 -0.101408   0.103512    0.0142565   364  ASP A OD1 
2675 O  OD2 . ASP A 328 ? 0.620563 0.714242 0.383452 -0.101201   0.10374     0.0168146   364  ASP A OD2 
2676 N  N   . PHE A 329 ? 0.470477 0.585022 0.331254 -0.0893536  0.0997405   -0.0100001  365  PHE A N   
2677 C  CA  . PHE A 329 ? 0.45522  0.559169 0.329205 -0.0837104  0.090079    -0.00744329 365  PHE A CA  
2678 C  C   . PHE A 329 ? 0.457141 0.55024  0.330497 -0.0900599  0.0906913   0.00341612  365  PHE A C   
2679 O  O   . PHE A 329 ? 0.520624 0.619336 0.394886 -0.0985634  0.0999098   0.00475246  365  PHE A O   
2680 C  CB  . PHE A 329 ? 0.437876 0.553371 0.336726 -0.0794623  0.0907995   -0.0183179  365  PHE A CB  
2681 C  CG  . PHE A 329 ? 0.454947 0.582684 0.357729 -0.0738443  0.0923344   -0.0307396  365  PHE A CG  
2682 C  CD1 . PHE A 329 ? 0.431386 0.55309  0.333468 -0.0656437  0.084127    -0.0341863  365  PHE A CD1 
2683 C  CD2 . PHE A 329 ? 0.423312 0.568599 0.331499 -0.0769998  0.102295    -0.0395329  365  PHE A CD2 
2684 C  CE1 . PHE A 329 ? 0.455474 0.58659  0.361571 -0.06063    0.0855434   -0.0458749  365  PHE A CE1 
2685 C  CE2 . PHE A 329 ? 0.434247 0.589941 0.347023 -0.0711052  0.103377    -0.0516131  365  PHE A CE2 
2686 C  CZ  . PHE A 329 ? 0.438784 0.586569 0.34974  -0.0630551  0.0950266   -0.0545742  365  PHE A CZ  
2687 N  N   . ARG A 330 ? 0.447295 0.524997 0.319388 -0.0863264  0.0813287   0.0106704   366  ARG A N   
2688 C  CA  . ARG A 330 ? 0.481072 0.545444 0.34783  -0.0922455  0.0814884   0.0219483   366  ARG A CA  
2689 C  C   . ARG A 330 ? 0.434333 0.488023 0.313248 -0.0871161  0.072298    0.0243919   366  ARG A C   
2690 O  O   . ARG A 330 ? 0.455275 0.506457 0.337835 -0.0789326  0.0640578   0.0215534   366  ARG A O   
2691 C  CB  . ARG A 330 ? 0.473445 0.524838 0.314175 -0.0953208  0.0807408   0.0332923   366  ARG A CB  
2692 C  CG  . ARG A 330 ? 0.511637 0.572397 0.336764 -0.101195   0.0903365   0.0321279   366  ARG A CG  
2693 C  CD  . ARG A 330 ? 0.559526 0.605333 0.357646 -0.102111   0.0869973   0.0440091   366  ARG A CD  
2694 N  NE  . ARG A 330 ? 0.58313  0.637126 0.362429 -0.103274   0.0914745   0.0417163   366  ARG A NE  
2695 C  CZ  . ARG A 330 ? 0.658908 0.70314  0.411704 -0.103419   0.0888856   0.0505393   366  ARG A CZ  
2696 N  NH1 . ARG A 330 ? 0.64198  0.667289 0.383809 -0.101695   0.0812762   0.0624549   366  ARG A NH1 
2697 N  NH2 . ARG A 330 ? 0.602959 0.656866 0.339685 -0.104924   0.0938852   0.0469802   366  ARG A NH2 
2698 N  N   . ILE A 331 ? 0.430376 0.476509 0.313366 -0.0927985  0.0741434   0.0303778   367  ILE A N   
2699 C  CA  . ILE A 331 ? 0.43587  0.468953 0.325744 -0.0893511  0.0660041   0.0348296   367  ILE A CA  
2700 C  C   . ILE A 331 ? 0.502432 0.517239 0.37593  -0.0937444  0.0649336   0.0475467   367  ILE A C   
2701 O  O   . ILE A 331 ? 0.534383 0.546161 0.396073 -0.102327   0.0726284   0.0533627   367  ILE A O   
2702 C  CB  . ILE A 331 ? 0.439495 0.480241 0.351651 -0.0911696  0.0682365   0.0287062   367  ILE A CB  
2703 C  CG1 . ILE A 331 ? 0.38257  0.437149 0.309979 -0.0835891  0.065839    0.0172492   367  ILE A CG1 
2704 C  CG2 . ILE A 331 ? 0.413258 0.439895 0.330779 -0.0909507  0.0624938   0.0342763   367  ILE A CG2 
2705 C  CD1 . ILE A 331 ? 0.348576 0.413391 0.297846 -0.0843157  0.067591    0.0100575   367  ILE A CD1 
2706 N  N   . LYS A 332 ? 0.503694 0.505927 0.375791 -0.0872579  0.0551437   0.0517499   368  LYS A N   
2707 C  CA  . LYS A 332 ? 0.521983 0.505212 0.382157 -0.0886663  0.0515409   0.0629227   368  LYS A CA  
2708 C  C   . LYS A 332 ? 0.548259 0.52471  0.424423 -0.085712   0.0458853   0.0620693   368  LYS A C   
2709 O  O   . LYS A 332 ? 0.535702 0.513106 0.419595 -0.0775682  0.0381929   0.0581403   368  LYS A O   
2710 C  CB  . LYS A 332 ? 0.56165  0.538372 0.405672 -0.0814852  0.0435547   0.0669995   368  LYS A CB  
2711 C  CG  . LYS A 332 ? 0.596129 0.552815 0.428512 -0.0797267  0.0371064   0.077927    368  LYS A CG  
2712 C  CD  . LYS A 332 ? 0.630474 0.58338  0.447859 -0.0720804  0.0286564   0.0808939   368  LYS A CD  
2713 C  CE  . LYS A 332 ? 0.561486 0.519973 0.391026 -0.0629305  0.0199606   0.0738677   368  LYS A CE  
2714 N  NZ  . LYS A 332 ? 0.585898 0.541607 0.434338 -0.0608717  0.0171434   0.0710017   368  LYS A NZ  
2715 N  N   . GLN A 333 ? 0.533058 0.502418 0.413698 -0.092956   0.0501541   0.0656143   369  GLN A N   
2716 C  CA  . GLN A 333 ? 0.51133  0.473614 0.406024 -0.0906973  0.0449989   0.0646342   369  GLN A CA  
2717 C  C   . GLN A 333 ? 0.530665 0.475449 0.419375 -0.0980124  0.0474845   0.0735139   369  GLN A C   
2718 O  O   . GLN A 333 ? 0.544891 0.490133 0.430302 -0.107939   0.0565732   0.0758522   369  GLN A O   
2719 C  CB  . GLN A 333 ? 0.499599 0.47845  0.415587 -0.091389   0.0479376   0.0537808   369  GLN A CB  
2720 C  CG  . GLN A 333 ? 0.50044  0.474755 0.43174  -0.0893654  0.0431062   0.0511475   369  GLN A CG  
2721 C  CD  . GLN A 333 ? 0.482325 0.473677 0.432701 -0.0871676  0.0436648   0.0401617   369  GLN A CD  
2722 O  OE1 . GLN A 333 ? 0.466217 0.471676 0.419088 -0.0846022  0.045737    0.0341644   369  GLN A OE1 
2723 N  NE2 . GLN A 333 ? 0.492606 0.481966 0.456101 -0.0872883  0.0410158   0.0372767   369  GLN A NE2 
2724 N  N   . CYS A 334 ? 0.506632 0.435963 0.394711 -0.0930972  0.0395763   0.0779015   370  CYS A N   
2725 C  CA  . CYS A 334 ? 0.580497 0.491777 0.466543 -0.0990378  0.0408842   0.084828    370  CYS A CA  
2726 C  C   . CYS A 334 ? 0.525534 0.443785 0.433701 -0.102826   0.0430785   0.0767001   370  CYS A C   
2727 O  O   . CYS A 334 ? 0.544458 0.457182 0.462217 -0.0977726  0.0364644   0.0743336   370  CYS A O   
2728 C  CB  . CYS A 334 ? 0.587012 0.480577 0.463655 -0.0906216  0.0308462   0.0915666   370  CYS A CB  
2729 S  SG  . CYS A 334 ? 0.774205 0.655896 0.621923 -0.0885144  0.028981    0.103284    370  CYS A SG  
2730 N  N   . THR A 335 ? 0.550771 0.484128 0.468011 -0.110684   0.0518759   0.0709224   371  THR A N   
2731 C  CA  . THR A 335 ? 0.56256  0.508764 0.502203 -0.112292   0.0528691   0.0607305   371  THR A CA  
2732 C  C   . THR A 335 ? 0.600963 0.532091 0.545279 -0.119104   0.0538015   0.0637988   371  THR A C   
2733 O  O   . THR A 335 ? 0.603494 0.526847 0.540269 -0.129365   0.0615076   0.0695775   371  THR A O   
2734 C  CB  . THR A 335 ? 0.572915 0.537986 0.519713 -0.120425   0.0630517   0.0547597   371  THR A CB  
2735 O  OG1 . THR A 335 ? 0.544351 0.520355 0.481833 -0.117436   0.0653183   0.053948    371  THR A OG1 
2736 C  CG2 . THR A 335 ? 0.542459 0.524154 0.512861 -0.120546   0.0631054   0.0430765   371  THR A CG2 
2737 N  N   . THR A 336 ? 0.657013 0.583717 0.612758 -0.114062   0.0467008   0.0599351   372  THR A N   
2738 C  CA  . THR A 336 ? 0.691769 0.609658 0.657144 -0.121853   0.0488966   0.0590207   372  THR A CA  
2739 C  C   . THR A 336 ? 0.712928 0.65123  0.700531 -0.12418    0.0507058   0.0465206   372  THR A C   
2740 O  O   . THR A 336 ? 0.642577 0.596455 0.638079 -0.116074   0.0464998   0.0392361   372  THR A O   
2741 C  CB  . THR A 336 ? 0.785968 0.681805 0.747176 -0.116942   0.0411152   0.064029    372  THR A CB  
2742 O  OG1 . THR A 336 ? 0.580632 0.487438 0.548931 -0.105635   0.0334171   0.0574577   372  THR A OG1 
2743 C  CG2 . THR A 336 ? 0.835002 0.710101 0.774143 -0.115357   0.0396031   0.0767706   372  THR A CG2 
2744 N  N   . VAL A 337 ? 0.696056 0.633889 0.693016 -0.135726   0.0572696   0.0443051   373  VAL A N   
2745 C  CA  . VAL A 337 ? 0.587386 0.546023 0.605127 -0.140839   0.0610089   0.0326928   373  VAL A CA  
2746 C  C   . VAL A 337 ? 0.567863 0.52991  0.600592 -0.13405    0.0523565   0.0241982   373  VAL A C   
2747 O  O   . VAL A 337 ? 0.584502 0.53667  0.624309 -0.138986   0.0515285   0.0226909   373  VAL A O   
2748 C  CB  . VAL A 337 ? 0.514667 0.471398 0.53696  -0.156632   0.0715341   0.0332756   373  VAL A CB  
2749 C  CG1 . VAL A 337 ? 0.494449 0.474995 0.540353 -0.161578   0.0747034   0.0199515   373  VAL A CG1 
2750 C  CG2 . VAL A 337 ? 0.536338 0.491549 0.543293 -0.164129   0.0812405   0.0411272   373  VAL A CG2 
2751 N  N   . ASN A 338 ? 0.502519 0.479    0.540178 -0.123237   0.0463714   0.0180771   374  ASN A N   
2752 C  CA  . ASN A 338 ? 0.536437 0.520145 0.58738  -0.11628    0.0387245   0.00922904  374  ASN A CA  
2753 C  C   . ASN A 338 ? 0.594355 0.597873 0.649787 -0.107131   0.0358495   0.00286788  374  ASN A C   
2754 O  O   . ASN A 338 ? 0.523115 0.532336 0.571028 -0.10606    0.0394108   0.00559269  374  ASN A O   
2755 C  CB  . ASN A 338 ? 0.502734 0.468298 0.546504 -0.108832   0.0305961   0.0132818   374  ASN A CB  
2756 C  CG  . ASN A 338 ? 0.620767 0.579132 0.648679 -0.100231   0.0271961   0.0206902   374  ASN A CG  
2757 O  OD1 . ASN A 338 ? 0.598521 0.569409 0.62402  -0.0954038  0.0275161   0.0193545   374  ASN A OD1 
2758 N  ND2 . ASN A 338 ? 0.640557 0.578852 0.658045 -0.0980833  0.0237322   0.0280501   374  ASN A ND2 
2759 N  N   . LEU A 339 ? 0.524226 0.536082 0.589971 -0.0999372  0.0289918   -0.00501966 375  LEU A N   
2760 C  CA  . LEU A 339 ? 0.486785 0.515881 0.557651 -0.091445   0.0259456   -0.0113799  375  LEU A CA  
2761 C  C   . LEU A 339 ? 0.529926 0.552364 0.586738 -0.0820587  0.022291    -0.00570237 375  LEU A C   
2762 O  O   . LEU A 339 ? 0.563391 0.596199 0.618697 -0.0778657  0.0234205   -0.00724138 375  LEU A O   
2763 C  CB  . LEU A 339 ? 0.535007 0.569874 0.61774  -0.0871519  0.0191905   -0.0196987  375  LEU A CB  
2764 C  CG  . LEU A 339 ? 0.559862 0.609876 0.647202 -0.0768682  0.0141741   -0.0261847  375  LEU A CG  
2765 C  CD1 . LEU A 339 ? 0.526907 0.597533 0.625318 -0.0794519  0.01892     -0.0327251  375  LEU A CD1 
2766 C  CD2 . LEU A 339 ? 0.534028 0.585584 0.627596 -0.0711587  0.00638347  -0.0323029  375  LEU A CD2 
2767 N  N   . GLU A 340 ? 0.514067 0.519839 0.561694 -0.0784878  0.0177121   -6.938e-05  376  GLU A N   
2768 C  CA  . GLU A 340 ? 0.578921 0.578701 0.614085 -0.0708098  0.0146859   0.00504645  376  GLU A CA  
2769 C  C   . GLU A 340 ? 0.587827 0.58954  0.613465 -0.0732755  0.0201833   0.00983876  376  GLU A C   
2770 O  O   . GLU A 340 ? 0.498583 0.506301 0.519997 -0.0673311  0.0192421   0.00913687  376  GLU A O   
2771 C  CB  . GLU A 340 ? 0.698387 0.680324 0.726528 -0.0687604  0.0102831   0.0103245   376  GLU A CB  
2772 C  CG  . GLU A 340 ? 0.799573 0.775375 0.815347 -0.061936   0.00744768  0.0156971   376  GLU A CG  
2773 C  CD  . GLU A 340 ? 0.978277 0.945394 0.993059 -0.0553539  0.0008983   0.0155798   376  GLU A CD  
2774 O  OE1 . GLU A 340 ? 0.884288 0.846767 0.90566  -0.0563845  -0.00138803 0.0126489   376  GLU A OE1 
2775 O  OE2 . GLU A 340 ? 0.867937 0.834193 0.875696 -0.049242   -0.00161891 0.0176599   376  GLU A OE2 
2776 N  N   . ASP A 341 ? 0.53375  0.529435 0.554953 -0.0822662  0.0261193   0.0148022   377  ASP A N   
2777 C  CA  . ASP A 341 ? 0.543541 0.540932 0.554284 -0.0856188  0.0319816   0.0193973   377  ASP A CA  
2778 C  C   . ASP A 341 ? 0.528476 0.545806 0.548315 -0.0884598  0.0378918   0.0123132   377  ASP A C   
2779 O  O   . ASP A 341 ? 0.443168 0.466124 0.455558 -0.0885732  0.0419658   0.0135399   377  ASP A O   
2780 C  CB  . ASP A 341 ? 0.622849 0.604371 0.622178 -0.0935288  0.035989    0.028583    377  ASP A CB  
2781 C  CG  . ASP A 341 ? 0.699091 0.663022 0.683312 -0.0882544  0.0306035   0.0371317   377  ASP A CG  
2782 O  OD1 . ASP A 341 ? 0.722202 0.685442 0.707399 -0.0791041  0.023432    0.0352082   377  ASP A OD1 
2783 O  OD2 . ASP A 341 ? 0.835094 0.786773 0.806116 -0.0931612  0.0337345   0.045632    377  ASP A OD2 
2784 N  N   . LEU A 342 ? 0.472015 0.50068  0.508184 -0.0912529  0.0387106   0.0044342   378  LEU A N   
2785 C  CA  . LEU A 342 ? 0.404722 0.454137 0.451508 -0.0923306  0.0433286   -0.00354699 378  LEU A CA  
2786 C  C   . LEU A 342 ? 0.432463 0.489865 0.479034 -0.0809067  0.0384146   -0.00757095 378  LEU A C   
2787 O  O   . LEU A 342 ? 0.371989 0.440957 0.418753 -0.0799445  0.0424084   -0.010683   378  LEU A O   
2788 C  CB  . LEU A 342 ? 0.42276  0.483539 0.488194 -0.0965307  0.0436751   -0.0119921  378  LEU A CB  
2789 C  CG  . LEU A 342 ? 0.429352 0.513754 0.508589 -0.0973262  0.0480438   -0.021559   378  LEU A CG  
2790 C  CD1 . LEU A 342 ? 0.448627 0.538199 0.522171 -0.105252   0.0583149   -0.0191385  378  LEU A CD1 
2791 C  CD2 . LEU A 342 ? 0.427638 0.523612 0.525881 -0.101613   0.0475443   -0.0302678  378  LEU A CD2 
2792 N  N   . VAL A 343 ? 0.367628 0.417901 0.413252 -0.0726057  0.0301781   -0.00747078 379  VAL A N   
2793 C  CA  . VAL A 343 ? 0.360518 0.413708 0.403727 -0.0623066  0.0253812   -0.00970985 379  VAL A CA  
2794 C  C   . VAL A 343 ? 0.394596 0.440973 0.422898 -0.0613198  0.0274134   -0.00366624 379  VAL A C   
2795 O  O   . VAL A 343 ? 0.344697 0.399563 0.37213  -0.0580649  0.0293029   -0.00678939 379  VAL A O   
2796 C  CB  . VAL A 343 ? 0.377075 0.423272 0.421439 -0.0552386  0.0172231   -0.0103746  379  VAL A CB  
2797 C  CG1 . VAL A 343 ? 0.345661 0.390485 0.384218 -0.0454847  0.0128387   -0.0106591  379  VAL A CG1 
2798 C  CG2 . VAL A 343 ? 0.359254 0.415225 0.418324 -0.0553574  0.0147932   -0.0179172  379  VAL A CG2 
2799 N  N   . VAL A 344 ? 0.3851   0.41639  0.401857 -0.0639597  0.0268026   0.00448665  380  VAL A N   
2800 C  CA  . VAL A 344 ? 0.366075 0.390907 0.368131 -0.0630315  0.0277671   0.0102264   380  VAL A CA  
2801 C  C   . VAL A 344 ? 0.431079 0.465484 0.43023  -0.0685157  0.0356793   0.00933016  380  VAL A C   
2802 O  O   . VAL A 344 ? 0.406909 0.444931 0.399066 -0.0653606  0.0366492   0.00865496  380  VAL A O   
2803 C  CB  . VAL A 344 ? 0.363543 0.371123 0.354931 -0.0649068  0.0252989   0.0188693   380  VAL A CB  
2804 C  CG1 . VAL A 344 ? 0.378035 0.380018 0.353361 -0.0655427  0.0269156   0.0251771   380  VAL A CG1 
2805 C  CG2 . VAL A 344 ? 0.335676 0.335266 0.329115 -0.0583707  0.0177206   0.0188846   380  VAL A CG2 
2806 N  N   . ALA A 345 ? 0.36565  0.405218 0.370757 -0.0771539  0.0418998   0.00842418  381  ALA A N   
2807 C  CA  . ALA A 345 ? 0.396319 0.447423 0.399923 -0.0824149  0.0502301   0.00628575  381  ALA A CA  
2808 C  C   . ALA A 345 ? 0.405641 0.472673 0.417556 -0.0755278  0.0499175   -0.00284579 381  ALA A C   
2809 O  O   . ALA A 345 ? 0.347866 0.421812 0.353973 -0.0756207  0.0544146   -0.00445491 381  ALA A O   
2810 C  CB  . ALA A 345 ? 0.38488  0.440965 0.396059 -0.0934533  0.0577051   0.00547332  381  ALA A CB  
2811 N  N   . HIS A 346 ? 0.362338 0.435349 0.387847 -0.0694434  0.0446929   -0.00927965 382  HIS A N   
2812 C  CA  . HIS A 346 ? 0.356896 0.444015 0.391311 -0.0623944  0.043972    -0.0180444  382  HIS A CA  
2813 C  C   . HIS A 346 ? 0.311036 0.390027 0.334403 -0.0545375  0.0396677   -0.0159222  382  HIS A C   
2814 O  O   . HIS A 346 ? 0.360026 0.445861 0.381361 -0.0519325  0.0423003   -0.0196794  382  HIS A O   
2815 C  CB  . HIS A 346 ? 0.299629 0.39519  0.350471 -0.0579923  0.0392811   -0.0251273  382  HIS A CB  
2816 C  CG  . HIS A 346 ? 0.289585 0.399847 0.355003 -0.065062   0.0443698   -0.0309652  382  HIS A CG  
2817 N  ND1 . HIS A 346 ? 0.281454 0.387923 0.349884 -0.074303   0.046818    -0.0282087  382  HIS A ND1 
2818 C  CD2 . HIS A 346 ? 0.294375 0.42407  0.373143 -0.0644797  0.0478825   -0.0401973  382  HIS A CD2 
2819 C  CE1 . HIS A 346 ? 0.271396 0.395196 0.355139 -0.0795874  0.0517352   -0.035872   382  HIS A CE1 
2820 N  NE2 . HIS A 346 ? 0.276975 0.415847 0.36743  -0.0736051  0.0524506   -0.0433103  382  HIS A NE2 
2821 N  N   . HIS A 347 ? 0.288909 0.353605 0.305682 -0.0514229  0.0334857   -0.0103901  383  HIS A N   
2822 C  CA  . HIS A 347 ? 0.281939 0.338128 0.288074 -0.0458563  0.0299109   -0.00776654 383  HIS A CA  
2823 C  C   . HIS A 347 ? 0.32176  0.379478 0.316866 -0.0489125  0.0349017   -0.00616831 383  HIS A C   
2824 O  O   . HIS A 347 ? 0.349095 0.409739 0.34142  -0.0442213  0.0347033   -0.00985439 383  HIS A O   
2825 C  CB  . HIS A 347 ? 0.319378 0.360706 0.318745 -0.045291   0.0246802   -0.00088842 383  HIS A CB  
2826 C  CG  . HIS A 347 ? 0.313575 0.347369 0.304071 -0.0398303  0.0207027   0.0009885   383  HIS A CG  
2827 N  ND1 . HIS A 347 ? 0.31599  0.348081 0.309958 -0.0328807  0.0161562   -0.00204218 383  HIS A ND1 
2828 C  CD2 . HIS A 347 ? 0.2939   0.322414 0.272753 -0.0405391  0.0208076   0.00489857  383  HIS A CD2 
2829 C  CE1 . HIS A 347 ? 0.346874 0.372601 0.332439 -0.0303551  0.0140635   -6.572e-05  383  HIS A CE1 
2830 N  NE2 . HIS A 347 ? 0.323275 0.347294 0.299932 -0.0347522  0.0163898   0.00395396  383  HIS A NE2 
2831 N  N   . GLU A 348 ? 0.273998 0.327835 0.261278 -0.0565582  0.0389029   -0.00025923 384  GLU A N   
2832 C  CA  . GLU A 348 ? 0.296664 0.349604 0.269823 -0.0596506  0.0428732   0.00294032  384  GLU A CA  
2833 C  C   . GLU A 348 ? 0.290057 0.35872  0.267699 -0.0611565  0.04981     -0.00444334 384  GLU A C   
2834 O  O   . GLU A 348 ? 0.347434 0.419055 0.317894 -0.0588578  0.051036    -0.00677412 384  GLU A O   
2835 C  CB  . GLU A 348 ? 0.316036 0.359229 0.277113 -0.0670723  0.0453866   0.0120524   384  GLU A CB  
2836 C  CG  . GLU A 348 ? 0.350338 0.377928 0.307031 -0.0645594  0.0381553   0.0187927   384  GLU A CG  
2837 C  CD  . GLU A 348 ? 0.42596  0.447753 0.375647 -0.0572645  0.0315435   0.0196264   384  GLU A CD  
2838 O  OE1 . GLU A 348 ? 0.449215 0.476907 0.392409 -0.0557751  0.033319    0.0168252   384  GLU A OE1 
2839 O  OE2 . GLU A 348 ? 0.34632  0.358973 0.297846 -0.0533501  0.0250916   0.0220453   384  GLU A OE2 
2840 N  N   . MET A 349 ? 0.321113 0.401107 0.312362 -0.0642254  0.0538662   -0.00954708 385  MET A N   
2841 C  CA  . MET A 349 ? 0.31235  0.409253 0.309872 -0.0655706  0.0608436   -0.0175766  385  MET A CA  
2842 C  C   . MET A 349 ? 0.273457 0.375604 0.277102 -0.0554799  0.0568392   -0.025435   385  MET A C   
2843 O  O   . MET A 349 ? 0.276748 0.388288 0.279578 -0.0541517  0.061011    -0.0312769  385  MET A O   
2844 C  CB  . MET A 349 ? 0.327771 0.436316 0.340454 -0.0715489  0.0656089   -0.0215634  385  MET A CB  
2845 C  CG  . MET A 349 ? 0.364932 0.468793 0.369559 -0.0832895  0.0723681   -0.0143242  385  MET A CG  
2846 S  SD  . MET A 349 ? 0.380315 0.494278 0.373852 -0.0902734  0.0837089   -0.0152929  385  MET A SD  
2847 C  CE  . MET A 349 ? 0.330034 0.469405 0.344699 -0.0952164  0.092742    -0.0271121  385  MET A CE  
2848 N  N   . GLY A 350 ? 0.261816 0.356295 0.270003 -0.0485562  0.048905    -0.0251224  386  GLY A N   
2849 C  CA  . GLY A 350 ? 0.277223 0.37103  0.287855 -0.0390371  0.0443197   -0.0302993  386  GLY A CA  
2850 C  C   . GLY A 350 ? 0.283339 0.371421 0.280375 -0.0376677  0.0446511   -0.0292246  386  GLY A C   
2851 O  O   . GLY A 350 ? 0.252699 0.346221 0.251449 -0.0330045  0.0457511   -0.0361222  386  GLY A O   
2852 N  N   . HIS A 351 ? 0.309662 0.386573 0.293656 -0.0411784  0.0430595   -0.0211139  387  HIS A N   
2853 C  CA  . HIS A 351 ? 0.334445 0.407146 0.305066 -0.0406276  0.0429675   -0.0201748  387  HIS A CA  
2854 C  C   . HIS A 351 ? 0.32968  0.413865 0.295841 -0.0446969  0.0507443   -0.0242432  387  HIS A C   
2855 O  O   . HIS A 351 ? 0.297156 0.38456  0.259443 -0.0416772  0.0516623   -0.0297083  387  HIS A O   
2856 C  CB  . HIS A 351 ? 0.326272 0.387167 0.284021 -0.0439854  0.039999    -0.0107358  387  HIS A CB  
2857 C  CG  . HIS A 351 ? 0.314185 0.363971 0.273835 -0.0396671  0.0325268   -0.00742106 387  HIS A CG  
2858 N  ND1 . HIS A 351 ? 0.322037 0.369096 0.285418 -0.033253   0.0284874   -0.0116348  387  HIS A ND1 
2859 C  CD2 . HIS A 351 ? 0.345344 0.38585  0.303522 -0.0409605  0.0287692   -0.00060968 387  HIS A CD2 
2860 C  CE1 . HIS A 351 ? 0.290407 0.327808 0.254162 -0.0311561  0.0229078   -0.00746149 387  HIS A CE1 
2861 N  NE2 . HIS A 351 ? 0.322828 0.35648  0.283772 -0.0354247  0.0227326   -0.00099724 387  HIS A NE2 
2862 N  N   . ILE A 352 ? 0.312907 0.403063 0.279172 -0.0521069  0.0568214   -0.0218163  388  ILE A N   
2863 C  CA  . ILE A 352 ? 0.316233 0.418155 0.277624 -0.0566269  0.0652457   -0.02579    388  ILE A CA  
2864 C  C   . ILE A 352 ? 0.324011 0.439672 0.298606 -0.051241   0.067577    -0.0376887  388  ILE A C   
2865 O  O   . ILE A 352 ? 0.322639 0.446552 0.292628 -0.0511264  0.0723171   -0.0435737  388  ILE A O   
2866 C  CB  . ILE A 352 ? 0.354788 0.460586 0.31534  -0.0664278  0.0722794   -0.0212246  388  ILE A CB  
2867 C  CG1 . ILE A 352 ? 0.37052  0.460059 0.316097 -0.0710145  0.0695591   -0.00886146 388  ILE A CG1 
2868 C  CG2 . ILE A 352 ? 0.342975 0.463552 0.3002   -0.0714828  0.0823984   -0.0266363  388  ILE A CG2 
2869 C  CD1 . ILE A 352 ? 0.419462 0.502961 0.344536 -0.0713065  0.0690941   -0.00453569 388  ILE A CD1 
2870 N  N   . GLN A 353 ? 0.299634 0.418389 0.290754 -0.0466535  0.0643219   -0.0415891  389  GLN A N   
2871 C  CA  . GLN A 353 ? 0.302002 0.434747 0.306749 -0.0412885  0.0665686   -0.0528756  389  GLN A CA  
2872 C  C   . GLN A 353 ? 0.297159 0.424048 0.297487 -0.0333171  0.0626695   -0.0572742  389  GLN A C   
2873 O  O   . GLN A 353 ? 0.302599 0.43936  0.306467 -0.0302114  0.0663368   -0.0662969  389  GLN A O   
2874 C  CB  . GLN A 353 ? 0.298073 0.434572 0.320483 -0.0364541  0.0622392   -0.0561506  389  GLN A CB  
2875 C  CG  . GLN A 353 ? 0.254326 0.404267 0.291537 -0.0286905  0.0627056   -0.0679235  389  GLN A CG  
2876 C  CD  . GLN A 353 ? 0.287618 0.457708 0.331975 -0.0338611  0.0722558   -0.0752685  389  GLN A CD  
2877 O  OE1 . GLN A 353 ? 0.327364 0.508712 0.378551 -0.0286226  0.0748426   -0.0852784  389  GLN A OE1 
2878 N  NE2 . GLN A 353 ? 0.281056 0.456454 0.325303 -0.0442226  0.0779433   -0.0710707  389  GLN A NE2 
2879 N  N   . TYR A 354 ? 0.294252 0.405222 0.28812  -0.0301259  0.0553715   -0.0514759  390  TYR A N   
2880 C  CA  . TYR A 354 ? 0.295404 0.399072 0.285453 -0.0236219  0.0516697   -0.0552929  390  TYR A CA  
2881 C  C   . TYR A 354 ? 0.312986 0.419974 0.290316 -0.0270061  0.0562092   -0.0576025  390  TYR A C   
2882 O  O   . TYR A 354 ? 0.294951 0.405376 0.273227 -0.0227312  0.0574865   -0.0660636  390  TYR A O   
2883 C  CB  . TYR A 354 ? 0.285258 0.372756 0.271746 -0.0213799  0.0440005   -0.0480995  390  TYR A CB  
2884 C  CG  . TYR A 354 ? 0.277685 0.356231 0.267567 -0.0132586  0.0388985   -0.0519547  390  TYR A CG  
2885 C  CD1 . TYR A 354 ? 0.283941 0.363986 0.274106 -0.00894189 0.0403157   -0.0602138  390  TYR A CD1 
2886 C  CD2 . TYR A 354 ? 0.287207 0.355528 0.280553 -0.00989504 0.0330117   -0.047561   390  TYR A CD2 
2887 C  CE1 . TYR A 354 ? 0.283119 0.35242  0.275938 -0.00203618 0.0358848   -0.0629339  390  TYR A CE1 
2888 C  CE2 . TYR A 354 ? 0.265482 0.323943 0.260613 -0.00324218 0.0288692   -0.0497888  390  TYR A CE2 
2889 C  CZ  . TYR A 354 ? 0.290649 0.349052 0.285647 0.00059011  0.0303769   -0.0572552  390  TYR A CZ  
2890 O  OH  . TYR A 354 ? 0.26022  0.306022 0.255893 0.00640179  0.0263608   -0.0581876  390  TYR A OH  
2891 N  N   . PHE A 355 ? 0.319551 0.424915 0.284165 -0.0343221  0.0583877   -0.0503144  391  PHE A N   
2892 C  CA  . PHE A 355 ? 0.34966  0.457839 0.29975  -0.0373462  0.0619321   -0.0519051  391  PHE A CA  
2893 C  C   . PHE A 355 ? 0.379329 0.503701 0.333362 -0.0380906  0.0701188   -0.0615325  391  PHE A C   
2894 O  O   . PHE A 355 ? 0.378448 0.506151 0.326808 -0.0360373  0.0717603   -0.0685546  391  PHE A O   
2895 C  CB  . PHE A 355 ? 0.352049 0.45775  0.287343 -0.0454502  0.0642563   -0.0421744  391  PHE A CB  
2896 C  CG  . PHE A 355 ? 0.328356 0.419112 0.257555 -0.0458105  0.0569529   -0.0318049  391  PHE A CG  
2897 C  CD1 . PHE A 355 ? 0.311631 0.392753 0.242586 -0.0401142  0.0493783   -0.0321383  391  PHE A CD1 
2898 C  CD2 . PHE A 355 ? 0.355434 0.44157  0.27621  -0.0521594  0.0581385   -0.0219276  391  PHE A CD2 
2899 C  CE1 . PHE A 355 ? 0.335109 0.404578 0.261172 -0.0403792  0.0432165   -0.0236842  391  PHE A CE1 
2900 C  CE2 . PHE A 355 ? 0.357116 0.429998 0.272585 -0.0516843  0.0513433   -0.0132862  391  PHE A CE2 
2901 C  CZ  . PHE A 355 ? 0.351158 0.416693 0.270014 -0.0456235  0.0438612   -0.0144909  391  PHE A CZ  
2902 N  N   . MET A 356 ? 0.342693 0.47777  0.306918 -0.0413976  0.0753792   -0.0623628  392  MET A N   
2903 C  CA  . MET A 356 ? 0.376862 0.529819 0.348021 -0.0421086  0.0837023   -0.0724246  392  MET A CA  
2904 C  C   . MET A 356 ? 0.352596 0.509885 0.337133 -0.0321109  0.0814526   -0.0842918  392  MET A C   
2905 O  O   . MET A 356 ? 0.3404   0.508032 0.324683 -0.0305679  0.0865449   -0.0938882  392  MET A O   
2906 C  CB  . MET A 356 ? 0.354622 0.519704 0.335388 -0.0487344  0.0903008   -0.0714739  392  MET A CB  
2907 C  CG  . MET A 356 ? 0.358368 0.518529 0.325788 -0.0593666  0.0939819   -0.060067   392  MET A CG  
2908 S  SD  . MET A 356 ? 0.35141  0.528532 0.331894 -0.0682684  0.104006    -0.0621138  392  MET A SD  
2909 C  CE  . MET A 356 ? 0.30267  0.479313 0.306628 -0.061665   0.0961068   -0.0644697  392  MET A CE  
2910 N  N   . GLN A 357 ? 0.328515 0.477515 0.32415  -0.0249777  0.0739619   -0.0839527  393  GLN A N   
2911 C  CA  . GLN A 357 ? 0.316769 0.466574 0.324064 -0.0147867  0.0709684   -0.0938237  393  GLN A CA  
2912 C  C   . GLN A 357 ? 0.338471 0.479297 0.336021 -0.0111193  0.0690318   -0.097955   393  GLN A C   
2913 O  O   . GLN A 357 ? 0.321025 0.467275 0.324413 -0.00527417 0.0707838   -0.108751   393  GLN A O   
2914 C  CB  . GLN A 357 ? 0.334861 0.475609 0.352451 -0.00912736 0.0631944   -0.0899553  393  GLN A CB  
2915 C  CG  . GLN A 357 ? 0.281925 0.435495 0.314006 -0.0104862  0.0648964   -0.0906417  393  GLN A CG  
2916 C  CD  . GLN A 357 ? 0.32089  0.490902 0.369135 -0.00398838 0.0676384   -0.103192   393  GLN A CD  
2917 O  OE1 . GLN A 357 ? 0.305158 0.474805 0.354747 0.00319327  0.0673136   -0.111425   393  GLN A OE1 
2918 N  NE2 . GLN A 357 ? 0.306203 0.491697 0.367967 -0.00645205 0.0704995   -0.105658   393  GLN A NE2 
2919 N  N   . TYR A 358 ? 0.314202 0.441749 0.297518 -0.0144505  0.0653307   -0.090244   394  TYR A N   
2920 C  CA  . TYR A 358 ? 0.3592   0.478148 0.334727 -0.0114152  0.0628168   -0.0946896  394  TYR A CA  
2921 C  C   . TYR A 358 ? 0.379284 0.504467 0.33969  -0.0171196  0.0675682   -0.096702   394  TYR A C   
2922 O  O   . TYR A 358 ? 0.3975   0.515735 0.34944  -0.0161265  0.0649564   -0.0995916  394  TYR A O   
2923 C  CB  . TYR A 358 ? 0.328211 0.428973 0.300481 -0.00975415 0.0547693   -0.0874209  394  TYR A CB  
2924 C  CG  . TYR A 358 ? 0.339645 0.433    0.302337 -0.015614   0.0515346   -0.0754668  394  TYR A CG  
2925 C  CD1 . TYR A 358 ? 0.32513  0.421505 0.273401 -0.0221199  0.0537179   -0.0716406  394  TYR A CD1 
2926 C  CD2 . TYR A 358 ? 0.311591 0.393608 0.27869  -0.013755   0.045615    -0.0684     394  TYR A CD2 
2927 C  CE1 . TYR A 358 ? 0.323172 0.411546 0.263073 -0.0260146  0.0497694   -0.0611812  394  TYR A CE1 
2928 C  CE2 . TYR A 358 ? 0.30886  0.383969 0.268163 -0.0181946  0.0423613   -0.0585503  394  TYR A CE2 
2929 C  CZ  . TYR A 358 ? 0.303074 0.381038 0.249101 -0.0240065  0.0441309   -0.0549883  394  TYR A CZ  
2930 O  OH  . TYR A 358 ? 0.305011 0.375829 0.243102 -0.0274137  0.040324    -0.045581   394  TYR A OH  
2931 N  N   . LYS A 359 ? 0.383144 0.522212 0.340369 -0.0230835  0.0749368   -0.0962329  395  LYS A N   
2932 C  CA  . LYS A 359 ? 0.412066 0.556897 0.351843 -0.0295174  0.0797888   -0.0957737  395  LYS A CA  
2933 C  C   . LYS A 359 ? 0.406423 0.557896 0.343364 -0.0263046  0.0828822   -0.108616   395  LYS A C   
2934 O  O   . LYS A 359 ? 0.414458 0.569333 0.335325 -0.0304324  0.0855098   -0.109484   395  LYS A O   
2935 C  CB  . LYS A 359 ? 0.423893 0.580914 0.360139 -0.037517   0.0879883   -0.0915519  395  LYS A CB  
2936 C  CG  . LYS A 359 ? 0.457304 0.632778 0.406523 -0.036767   0.0963987   -0.102218   395  LYS A CG  
2937 C  CD  . LYS A 359 ? 0.508353 0.694587 0.451829 -0.0467201  0.105235    -0.0969733  395  LYS A CD  
2938 C  CE  . LYS A 359 ? 0.62101  0.825882 0.5653   -0.0477016  0.114988    -0.10895    395  LYS A CE  
2939 N  NZ  . LYS A 359 ? 0.619377 0.835994 0.587056 -0.0444641  0.117257    -0.115599   395  LYS A NZ  
2940 N  N   . ASP A 360 ? 0.435887 0.58885  0.387693 -0.0185161  0.0823092   -0.118992   396  ASP A N   
2941 C  CA  . ASP A 360 ? 0.504799 0.66338  0.454035 -0.0154349  0.0853503   -0.131877   396  ASP A CA  
2942 C  C   . ASP A 360 ? 0.520555 0.663604 0.466838 -0.01102    0.0781728   -0.134853   396  ASP A C   
2943 O  O   . ASP A 360 ? 0.662887 0.808473 0.604216 -0.00957821 0.0798649   -0.145041   396  ASP A O   
2944 C  CB  . ASP A 360 ? 0.597445 0.772436 0.560285 -0.011702   0.0923275   -0.143606   396  ASP A CB  
2945 C  CG  . ASP A 360 ? 0.77859  0.971576 0.736996 -0.0197725  0.101923    -0.142001   396  ASP A CG  
2946 O  OD1 . ASP A 360 ? 0.868612 1.0639   0.80799  -0.0271032  0.105417    -0.138139   396  ASP A OD1 
2947 O  OD2 . ASP A 360 ? 0.77794  0.982319 0.751487 -0.0189718  0.105742    -0.144249   396  ASP A OD2 
2948 N  N   . LEU A 361 ? 0.443645 0.571159 0.392347 -0.00968711 0.0706681   -0.126341   397  LEU A N   
2949 C  CA  . LEU A 361 ? 0.440626 0.553435 0.387536 -0.00658806 0.0646061   -0.129158   397  LEU A CA  
2950 C  C   . LEU A 361 ? 0.448983 0.562381 0.378632 -0.0124692  0.0637922   -0.127685   397  LEU A C   
2951 O  O   . LEU A 361 ? 0.453193 0.572126 0.372437 -0.0183509  0.065247    -0.119272   397  LEU A O   
2952 C  CB  . LEU A 361 ? 0.419046 0.51693  0.371026 -0.00536973 0.0577682   -0.118875   397  LEU A CB  
2953 C  CG  . LEU A 361 ? 0.390187 0.485114 0.357935 0.00112912  0.0566333   -0.118875   397  LEU A CG  
2954 C  CD1 . LEU A 361 ? 0.331751 0.409507 0.302579 0.00307132  0.0496155   -0.110526   397  LEU A CD1 
2955 C  CD2 . LEU A 361 ? 0.394124 0.491247 0.370963 0.00845394  0.0588248   -0.13197    397  LEU A CD2 
2956 N  N   . PRO A 362 ? 0.449824 0.555717 0.376234 -0.0109823  0.0604605   -0.13473    398  PRO A N   
2957 C  CA  . PRO A 362 ? 0.48125  0.584603 0.393146 -0.0159341  0.0565095   -0.131342   398  PRO A CA  
2958 C  C   . PRO A 362 ? 0.46441  0.561156 0.372652 -0.0193585  0.0515423   -0.116674   398  PRO A C   
2959 O  O   . PRO A 362 ? 0.41013  0.497303 0.328407 -0.0171862  0.0484092   -0.110726   398  PRO A O   
2960 C  CB  . PRO A 362 ? 0.433859 0.526976 0.349192 -0.0131154  0.0527024   -0.14115    398  PRO A CB  
2961 C  CG  . PRO A 362 ? 0.420927 0.507    0.352201 -0.0064708  0.0537815   -0.145849   398  PRO A CG  
2962 C  CD  . PRO A 362 ? 0.414982 0.513379 0.352139 -0.00440681 0.0596941   -0.145858   398  PRO A CD  
2963 N  N   . VAL A 363 ? 0.453352 0.554698 0.346247 -0.0243104  0.050373    -0.111109   399  VAL A N   
2964 C  CA  . VAL A 363 ? 0.458904 0.555084 0.347555 -0.0271482  0.0461232   -0.0975679  399  VAL A CA  
2965 C  C   . VAL A 363 ? 0.420138 0.502983 0.317313 -0.0251137  0.0391054   -0.0949675  399  VAL A C   
2966 O  O   . VAL A 363 ? 0.418102 0.495168 0.319403 -0.025389   0.0366432   -0.0852879  399  VAL A O   
2967 C  CB  . VAL A 363 ? 0.541137 0.642494 0.410927 -0.0319134  0.0451449   -0.0905812  399  VAL A CB  
2968 C  CG1 . VAL A 363 ? 0.533836 0.64819  0.391496 -0.0345226  0.0522976   -0.0952434  399  VAL A CG1 
2969 C  CG2 . VAL A 363 ? 0.566142 0.663732 0.42814  -0.0321737  0.0377264   -0.091735   399  VAL A CG2 
2970 N  N   . ALA A 364 ? 0.417413 0.494975 0.317808 -0.0234804  0.0362826   -0.103562   400  ALA A N   
2971 C  CA  . ALA A 364 ? 0.388918 0.454186 0.296781 -0.0228105  0.0305724   -0.100745   400  ALA A CA  
2972 C  C   . ALA A 364 ? 0.385151 0.441539 0.306329 -0.0192971  0.0313918   -0.0972127  400  ALA A C   
2973 O  O   . ALA A 364 ? 0.468082 0.514765 0.39452  -0.0191377  0.0275684   -0.0917464  400  ALA A O   
2974 C  CB  . ALA A 364 ? 0.418434 0.479557 0.327913 -0.0226623  0.0285566   -0.111775   400  ALA A CB  
2975 N  N   . LEU A 365 ? 0.420051 0.480936 0.346464 -0.016332   0.0363847   -0.100343   401  LEU A N   
2976 C  CA  . LEU A 365 ? 0.380917 0.435127 0.319662 -0.0118333  0.036853    -0.0983061  401  LEU A CA  
2977 C  C   . LEU A 365 ? 0.381087 0.442308 0.320971 -0.0128793  0.0388029   -0.0897979  401  LEU A C   
2978 O  O   . LEU A 365 ? 0.351604 0.408933 0.301261 -0.00939129 0.038413    -0.0870307  401  LEU A O   
2979 C  CB  . LEU A 365 ? 0.404567 0.45875  0.35033  -0.00667271 0.0401789   -0.109913   401  LEU A CB  
2980 C  CG  . LEU A 365 ? 0.414596 0.460578 0.359105 -0.006411   0.0385321   -0.119135   401  LEU A CG  
2981 C  CD1 . LEU A 365 ? 0.441478 0.484783 0.393518 -0.00050582 0.041378    -0.130372   401  LEU A CD1 
2982 C  CD2 . LEU A 365 ? 0.388554 0.419412 0.335003 -0.00787869 0.03341     -0.114312   401  LEU A CD2 
2983 N  N   . ARG A 366 ? 0.341201 0.411676 0.270668 -0.0177786  0.0405457   -0.0853859  402  ARG A N   
2984 C  CA  . ARG A 366 ? 0.385594 0.461353 0.31566  -0.0200782  0.0427609   -0.0770688  402  ARG A CA  
2985 C  C   . ARG A 366 ? 0.348723 0.414878 0.280689 -0.0208332  0.0374748   -0.066539   402  ARG A C   
2986 O  O   . ARG A 366 ? 0.421202 0.487602 0.344875 -0.0247764  0.0360167   -0.0586117  402  ARG A O   
2987 C  CB  . ARG A 366 ? 0.371299 0.457942 0.288348 -0.0254351  0.0470453   -0.0750594  402  ARG A CB  
2988 C  CG  . ARG A 366 ? 0.439323 0.538187 0.358505 -0.0245964  0.0542602   -0.0848412  402  ARG A CG  
2989 C  CD  . ARG A 366 ? 0.504027 0.612237 0.408096 -0.0307388  0.0587877   -0.0814173  402  ARG A CD  
2990 N  NE  . ARG A 366 ? 0.522273 0.641065 0.422325 -0.0302634  0.0642099   -0.0928198  402  ARG A NE  
2991 C  CZ  . ARG A 366 ? 0.552284 0.681505 0.43854  -0.034816   0.0698345   -0.0939047  402  ARG A CZ  
2992 N  NH1 . ARG A 366 ? 0.570799 0.701579 0.446975 -0.0406544  0.0721302   -0.0833915  402  ARG A NH1 
2993 N  NH2 . ARG A 366 ? 0.503019 0.640655 0.385844 -0.0334815  0.0736543   -0.105744   402  ARG A NH2 
2994 N  N   . GLU A 367 ? 0.344037 0.401237 0.286467 -0.0167249  0.0346247   -0.0663419  403  GLU A N   
2995 C  CA  . GLU A 367 ? 0.327164 0.375778 0.272656 -0.0167987  0.0302046   -0.0576506  403  GLU A CA  
2996 C  C   . GLU A 367 ? 0.293939 0.339163 0.251248 -0.0120461  0.0301229   -0.0580252  403  GLU A C   
2997 O  O   . GLU A 367 ? 0.308768 0.3563   0.271887 -0.00804747 0.0323938   -0.0651849  403  GLU A O   
2998 C  CB  . GLU A 367 ? 0.365274 0.404047 0.308207 -0.0171401  0.0252193   -0.056677   403  GLU A CB  
2999 C  CG  . GLU A 367 ? 0.490905 0.534093 0.422977 -0.0205758  0.0243613   -0.0588908  403  GLU A CG  
3000 C  CD  . GLU A 367 ? 0.636175 0.671508 0.568263 -0.021285   0.0191548   -0.0577395  403  GLU A CD  
3001 O  OE1 . GLU A 367 ? 0.713749 0.739967 0.653708 -0.0193398  0.0176556   -0.0565724  403  GLU A OE1 
3002 O  OE2 . GLU A 367 ? 0.687996 0.726723 0.612236 -0.0237693  0.0165709   -0.0581959  403  GLU A OE2 
3003 N  N   . GLY A 368 ? 0.352906 0.391998 0.313746 -0.0116714  0.0268729   -0.0508703  404  GLY A N   
3004 C  CA  . GLY A 368 ? 0.339567 0.375687 0.310375 -0.00657363 0.02603     -0.0513938  404  GLY A CA  
3005 C  C   . GLY A 368 ? 0.35493  0.378666 0.327899 -0.00203457 0.0234802   -0.0544911  404  GLY A C   
3006 O  O   . GLY A 368 ? 0.359998 0.377462 0.327958 -0.00391775 0.0223878   -0.0556401  404  GLY A O   
3007 N  N   . ALA A 369 ? 0.331692 0.351701 0.311931 0.00394266  0.0225439   -0.0562188  405  ALA A N   
3008 C  CA  . ALA A 369 ? 0.325211 0.330874 0.305829 0.00814266  0.0204525   -0.0582564  405  ALA A CA  
3009 C  C   . ALA A 369 ? 0.307635 0.302645 0.283067 0.00441591  0.0178875   -0.0524574  405  ALA A C   
3010 O  O   . ALA A 369 ? 0.280106 0.265552 0.252916 0.00368369  0.0177526   -0.0551078  405  ALA A O   
3011 C  CB  . ALA A 369 ? 0.328502 0.330377 0.315906 0.0155433   0.0185474   -0.0585112  405  ALA A CB  
3012 N  N   . ASN A 370 ? 0.289226 0.286383 0.2641   0.00192428  0.0161065   -0.0452059  406  ASN A N   
3013 C  CA  . ASN A 370 ? 0.302754 0.295009 0.27337  -0.00246738 0.0141047   -0.039979   406  ASN A CA  
3014 C  C   . ASN A 370 ? 0.273193 0.273955 0.243135 -0.00561315 0.0134137   -0.0343269  406  ASN A C   
3015 O  O   . ASN A 370 ? 0.28506  0.293648 0.258238 -0.00464632 0.0147748   -0.0344872  406  ASN A O   
3016 C  CB  . ASN A 370 ? 0.298441 0.277248 0.269397 -0.0004396  0.0121773   -0.0370825  406  ASN A CB  
3017 C  CG  . ASN A 370 ? 0.281993 0.25937  0.255666 0.00295084  0.0101847   -0.0321384  406  ASN A CG  
3018 O  OD1 . ASN A 370 ? 0.283954 0.268683 0.258823 0.00122745  0.00924131  -0.0282368  406  ASN A OD1 
3019 N  ND2 . ASN A 370 ? 0.279059 0.245625 0.252877 0.00768865  0.00922893  -0.0319991  406  ASN A ND2 
3020 N  N   . PRO A 371 ? 0.29598  0.296038 0.262149 -0.00956481 0.0115106   -0.0298658  407  PRO A N   
3021 C  CA  . PRO A 371 ? 0.274244 0.280389 0.239096 -0.0122717  0.0107796   -0.0244735  407  PRO A CA  
3022 C  C   . PRO A 371 ? 0.242739 0.248645 0.213098 -0.0100289  0.0100923   -0.0213427  407  PRO A C   
3023 O  O   . PRO A 371 ? 0.325616 0.338037 0.297018 -0.0118014  0.0111069   -0.0193278  407  PRO A O   
3024 C  CB  . PRO A 371 ? 0.264303 0.267346 0.225465 -0.0150281  0.00780245  -0.0209628  407  PRO A CB  
3025 C  CG  . PRO A 371 ? 0.286992 0.287266 0.246402 -0.0154947  0.00811849  -0.0264956  407  PRO A CG  
3026 C  CD  . PRO A 371 ? 0.286251 0.280764 0.249534 -0.0118721  0.0101132   -0.0306659  407  PRO A CD  
3027 N  N   . GLY A 372 ? 0.266414 0.264953 0.239857 -0.00631896 0.00856972  -0.0212669  408  GLY A N   
3028 C  CA  . GLY A 372 ? 0.266316 0.265594 0.244496 -0.00377294 0.0071542   -0.0189263  408  GLY A CA  
3029 C  C   . GLY A 372 ? 0.271959 0.280086 0.255721 -0.0015749  0.00895998  -0.0226176  408  GLY A C   
3030 O  O   . GLY A 372 ? 0.250355 0.264529 0.238465 -0.00237777 0.00861831  -0.0209943  408  GLY A O   
3031 N  N   . PHE A 373 ? 0.249982 0.259491 0.234476 0.00095848  0.0110274   -0.028315   409  PHE A N   
3032 C  CA  . PHE A 373 ? 0.272565 0.292572 0.263616 0.00322796  0.0131573   -0.0330663  409  PHE A CA  
3033 C  C   . PHE A 373 ? 0.27382  0.305129 0.264775 -0.00279754 0.0164531   -0.0320623  409  PHE A C   
3034 O  O   . PHE A 373 ? 0.275332 0.31641  0.272999 -0.00334664 0.0179746   -0.0333329  409  PHE A O   
3035 C  CB  . PHE A 373 ? 0.269525 0.288736 0.260524 0.00657178  0.01515     -0.0398896  409  PHE A CB  
3036 C  CG  . PHE A 373 ? 0.298268 0.308032 0.291932 0.014225    0.012396    -0.0419878  409  PHE A CG  
3037 C  CD1 . PHE A 373 ? 0.307859 0.303124 0.296485 0.0151633   0.00962432  -0.0377153  409  PHE A CD1 
3038 C  CD2 . PHE A 373 ? 0.339565 0.354543 0.340155 0.0205399   0.0128101   -0.0483744  409  PHE A CD2 
3039 C  CE1 . PHE A 373 ? 0.309626 0.294047 0.29833  0.0219545   0.00737785  -0.0386588  409  PHE A CE1 
3040 C  CE2 . PHE A 373 ? 0.318264 0.322735 0.319924 0.0284441   0.00961399  -0.0496672  409  PHE A CE2 
3041 C  CZ  . PHE A 373 ? 0.334944 0.323259 0.329682 0.0288997   0.00697834  -0.0442615  409  PHE A CZ  
3042 N  N   . HIS A 374 ? 0.279126 0.308948 0.262088 -0.00759471 0.0175439   -0.0297111  410  HIS A N   
3043 C  CA  . HIS A 374 ? 0.298651 0.337292 0.278783 -0.0132752  0.0210517   -0.0281659  410  HIS A CA  
3044 C  C   . HIS A 374 ? 0.30884  0.347494 0.291693 -0.0160801  0.019699    -0.0223015  410  HIS A C   
3045 O  O   . HIS A 374 ? 0.294305 0.341081 0.279977 -0.0197774  0.0229698   -0.0220239  410  HIS A O   
3046 C  CB  . HIS A 374 ? 0.274875 0.311436 0.244431 -0.0167059  0.0215394   -0.0270233  410  HIS A CB  
3047 C  CG  . HIS A 374 ? 0.282989 0.329304 0.247495 -0.0206657  0.0265709   -0.0291308  410  HIS A CG  
3048 N  ND1 . HIS A 374 ? 0.3108   0.364632 0.275674 -0.0251465  0.0303697   -0.0266341  410  HIS A ND1 
3049 C  CD2 . HIS A 374 ? 0.280516 0.329761 0.23865  -0.0211466  0.028618    -0.0336944  410  HIS A CD2 
3050 C  CE1 . HIS A 374 ? 0.294391 0.355765 0.25233  -0.0283151  0.0351857   -0.0293302  410  HIS A CE1 
3051 N  NE2 . HIS A 374 ? 0.315725 0.374964 0.269596 -0.0254018  0.0339804   -0.0343211  410  HIS A NE2 
3052 N  N   . GLU A 375 ? 0.325172 0.354688 0.307724 -0.014472   0.0152294   -0.0182911  411  GLU A N   
3053 C  CA  . GLU A 375 ? 0.323416 0.351474 0.308009 -0.0169076  0.0134833   -0.0132649  411  GLU A CA  
3054 C  C   . GLU A 375 ? 0.367465 0.401423 0.362209 -0.0145847  0.0133201   -0.0161949  411  GLU A C   
3055 O  O   . GLU A 375 ? 0.358009 0.394916 0.356746 -0.0177442  0.0134825   -0.0142197  411  GLU A O   
3056 C  CB  . GLU A 375 ? 0.271884 0.289713 0.253073 -0.0157529  0.00913169  -0.00915072 411  GLU A CB  
3057 C  CG  . GLU A 375 ? 0.266184 0.279974 0.238917 -0.0180712  0.00838534  -0.00651795 411  GLU A CG  
3058 C  CD  . GLU A 375 ? 0.290699 0.307926 0.258191 -0.0231385  0.0104185   -0.00295391 411  GLU A CD  
3059 O  OE1 . GLU A 375 ? 0.278393 0.296594 0.248506 -0.0258529  0.0111806   4.175e-05   411  GLU A OE1 
3060 O  OE2 . GLU A 375 ? 0.299284 0.318261 0.259441 -0.02462    0.0116332   -0.00357444 411  GLU A OE2 
3061 N  N   . ALA A 376 ? 0.325688 0.361059 0.324894 -0.00875461 0.0125668   -0.0212509  412  ALA A N   
3062 C  CA  . ALA A 376 ? 0.277598 0.316987 0.285766 -0.00460296 0.0102183   -0.0238518  412  ALA A CA  
3063 C  C   . ALA A 376 ? 0.259904 0.314092 0.277392 -0.00620737 0.0137643   -0.0288676  412  ALA A C   
3064 O  O   . ALA A 376 ? 0.277194 0.337492 0.303315 -0.00470292 0.011955    -0.0309821  412  ALA A O   
3065 C  CB  . ALA A 376 ? 0.240518 0.273399 0.248236 0.00317327  0.00734113  -0.0265674  412  ALA A CB  
3066 N  N   . ILE A 377 ? 0.285181 0.346617 0.301803 -0.00886717 0.0188845   -0.0319478  413  ILE A N   
3067 C  CA  . ILE A 377 ? 0.278651 0.355496 0.305272 -0.00902487 0.0228271   -0.0386949  413  ILE A CA  
3068 C  C   . ILE A 377 ? 0.284985 0.370866 0.319698 -0.0147261  0.0244712   -0.0381701  413  ILE A C   
3069 O  O   . ILE A 377 ? 0.263621 0.360134 0.310676 -0.0117908  0.0234372   -0.0437687  413  ILE A O   
3070 C  CB  . ILE A 377 ? 0.272203 0.355312 0.294533 -0.0121614  0.0290361   -0.0418093  413  ILE A CB  
3071 C  CG1 . ILE A 377 ? 0.296098 0.371421 0.312305 -0.00666159 0.0276196   -0.0442534  413  ILE A CG1 
3072 C  CG2 . ILE A 377 ? 0.304729 0.405807 0.338973 -0.0127316  0.0338488   -0.0495294  413  ILE A CG2 
3073 C  CD1 . ILE A 377 ? 0.288367 0.362398 0.311922 0.00298957  0.0238859   -0.0498692  413  ILE A CD1 
3074 N  N   . GLY A 378 ? 0.2234   0.305342 0.251234 -0.0229584  0.0272025   -0.0319448  414  GLY A N   
3075 C  CA  . GLY A 378 ? 0.248932 0.335399 0.282063 -0.0300725  0.0293505   -0.0300825  414  GLY A CA  
3076 C  C   . GLY A 378 ? 0.260134 0.343446 0.300103 -0.0270502  0.0232385   -0.0298114  414  GLY A C   
3077 O  O   . GLY A 378 ? 0.298605 0.391951 0.350028 -0.0291585  0.0238321   -0.0337478  414  GLY A O   
3078 N  N   . ASP A 379 ? 0.249757 0.320473 0.283203 -0.0220629  0.0175575   -0.0261319  415  ASP A N   
3079 C  CA  . ASP A 379 ? 0.244263 0.311222 0.28187  -0.0191407  0.0118306   -0.0256661  415  ASP A CA  
3080 C  C   . ASP A 379 ? 0.247668 0.325389 0.29661  -0.0127013  0.0090068   -0.0330344  415  ASP A C   
3081 O  O   . ASP A 379 ? 0.285705 0.367205 0.341974 -0.0121152  0.00558633  -0.0350692  415  ASP A O   
3082 C  CB  . ASP A 379 ? 0.244975 0.297571 0.273242 -0.0150473  0.00712782  -0.020918   415  ASP A CB  
3083 C  CG  . ASP A 379 ? 0.332271 0.374269 0.350611 -0.0199676  0.00800151  -0.013979   415  ASP A CG  
3084 O  OD1 . ASP A 379 ? 0.358626 0.401785 0.372666 -0.0251642  0.0123662   -0.0119263  415  ASP A OD1 
3085 O  OD2 . ASP A 379 ? 0.353609 0.386158 0.367716 -0.0179459  0.00412847  -0.0107545  415  ASP A OD2 
3086 N  N   . VAL A 380 ? 0.246003 0.327386 0.295667 -0.00679358 0.0094425   -0.0371609  416  VAL A N   
3087 C  CA  . VAL A 380 ? 0.219068 0.310479 0.279171 0.00082735  0.0062211   -0.0443712  416  VAL A CA  
3088 C  C   . VAL A 380 ? 0.25405  0.363113 0.328511 -0.00420697 0.00903565  -0.0500519  416  VAL A C   
3089 O  O   . VAL A 380 ? 0.217162 0.333166 0.300874 -0.00124177 0.00448891  -0.0539109  416  VAL A O   
3090 C  CB  . VAL A 380 ? 0.209329 0.30201  0.268969 0.00776916  0.00690034  -0.0486269  416  VAL A CB  
3091 C  CG1 . VAL A 380 ? 0.218841 0.323934 0.291254 0.0159302   0.00320398  -0.0566855  416  VAL A CG1 
3092 C  CG2 . VAL A 380 ? 0.20711  0.281995 0.254052 0.0127447   0.0037976   -0.0438707  416  VAL A CG2 
3093 N  N   . LEU A 381 ? 0.235034 0.351904 0.311184 -0.0121121  0.0167332   -0.0509303  417  LEU A N   
3094 C  CA  . LEU A 381 ? 0.248591 0.383063 0.338782 -0.0180084  0.021015    -0.0568745  417  LEU A CA  
3095 C  C   . LEU A 381 ? 0.245799 0.377252 0.338669 -0.0241273  0.0191696   -0.0539108  417  LEU A C   
3096 O  O   . LEU A 381 ? 0.239161 0.3833   0.345787 -0.024779   0.0177585   -0.0600737  417  LEU A O   
3097 C  CB  . LEU A 381 ? 0.261717 0.403632 0.350689 -0.026221   0.0306232   -0.0574803  417  LEU A CB  
3098 C  CG  . LEU A 381 ? 0.250764 0.406615 0.346898 -0.0208166  0.0334754   -0.0660801  417  LEU A CG  
3099 C  CD1 . LEU A 381 ? 0.226094 0.371117 0.31332  -0.0107553  0.0292643   -0.0655062  417  LEU A CD1 
3100 C  CD2 . LEU A 381 ? 0.259685 0.423885 0.354032 -0.0307494  0.0438534   -0.0665131  417  LEU A CD2 
3101 N  N   . ALA A 382 ? 0.247642 0.36241  0.327845 -0.0279721  0.0186677   -0.0451665  418  ALA A N   
3102 C  CA  . ALA A 382 ? 0.258596 0.368181 0.340386 -0.033681   0.0170138   -0.0422588  418  ALA A CA  
3103 C  C   . ALA A 382 ? 0.260948 0.370684 0.348295 -0.0267382  0.00857668  -0.045475   418  ALA A C   
3104 O  O   . ALA A 382 ? 0.250162 0.362805 0.344955 -0.0310877  0.00720246  -0.0474142  418  ALA A O   
3105 C  CB  . ALA A 382 ? 0.244595 0.336437 0.311244 -0.0379162  0.0182269   -0.0325808  418  ALA A CB  
3106 N  N   . LEU A 383 ? 0.22724  0.333569 0.310563 -0.0161715  0.00298657  -0.04628    419  LEU A N   
3107 C  CA  . LEU A 383 ? 0.25011  0.358856 0.338049 -0.00858981 -0.00489898 -0.0500936  419  LEU A CA  
3108 C  C   . LEU A 383 ? 0.256058 0.385181 0.36199  -0.00958941 -0.00522588 -0.0595888  419  LEU A C   
3109 O  O   . LEU A 383 ? 0.215936 0.348888 0.3284   -0.0107152  -0.0092629  -0.0625809  419  LEU A O   
3110 C  CB  . LEU A 383 ? 0.228796 0.331098 0.30931  0.0027855   -0.00973898 -0.0495378  419  LEU A CB  
3111 C  CG  . LEU A 383 ? 0.246053 0.32887  0.310276 0.00412017  -0.0106898  -0.0412273  419  LEU A CG  
3112 C  CD1 . LEU A 383 ? 0.235139 0.311666 0.292881 0.0142411   -0.0141125  -0.0411731  419  LEU A CD1 
3113 C  CD2 . LEU A 383 ? 0.264897 0.341095 0.32639  0.00277783  -0.0148609  -0.0387819  419  LEU A CD2 
3114 N  N   . SER A 384 ? 0.211555 0.354371 0.325866 -0.00980208 -0.00056224 -0.0648723  420  SER A N   
3115 C  CA  . SER A 384 ? 0.235392 0.400245 0.368665 -0.0107     -0.00022266 -0.0750492  420  SER A CA  
3116 C  C   . SER A 384 ? 0.239444 0.409966 0.380898 -0.0239762  0.00512677  -0.0759175  420  SER A C   
3117 O  O   . SER A 384 ? 0.236532 0.420768 0.392568 -0.0253124  0.00240345  -0.0834195  420  SER A O   
3118 C  CB  . SER A 384 ? 0.246826 0.42626  0.38824  -0.00712296 0.00360267  -0.0815958  420  SER A CB  
3119 O  OG  . SER A 384 ? 0.2308   0.407737 0.369374 0.00663718  -0.00332455 -0.0834853  420  SER A OG  
3120 N  N   . VAL A 385 ? 0.233883 0.392542 0.365091 -0.0333435  0.0120935   -0.0680714  421  VAL A N   
3121 C  CA  . VAL A 385 ? 0.275145 0.435831 0.411484 -0.0467254  0.0187075   -0.0673536  421  VAL A CA  
3122 C  C   . VAL A 385 ? 0.269147 0.422626 0.407193 -0.0486187  0.0131245   -0.0667659  421  VAL A C   
3123 O  O   . VAL A 385 ? 0.276232 0.43799  0.426308 -0.0568689  0.0153824   -0.0713796  421  VAL A O   
3124 C  CB  . VAL A 385 ? 0.248412 0.395111 0.369966 -0.054436   0.0261935   -0.0578047  421  VAL A CB  
3125 C  CG1 . VAL A 385 ? 0.247385 0.391751 0.371908 -0.0680546  0.0323614   -0.0555461  421  VAL A CG1 
3126 C  CG2 . VAL A 385 ? 0.260034 0.41583  0.380655 -0.054699   0.0329906   -0.0595637  421  VAL A CG2 
3127 N  N   . SER A 386 ? 0.263388 0.401733 0.389517 -0.0410497  0.00611254  -0.0616744  422  SER A N   
3128 C  CA  . SER A 386 ? 0.230755 0.359663 0.355113 -0.0418841  0.00094213  -0.0603285  422  SER A CA  
3129 C  C   . SER A 386 ? 0.262617 0.405447 0.399864 -0.0366304  -0.0062833  -0.0698841  422  SER A C   
3130 O  O   . SER A 386 ? 0.275163 0.414296 0.414547 -0.0389062  -0.0100746  -0.0714027  422  SER A O   
3131 C  CB  . SER A 386 ? 0.238403 0.347704 0.34528  -0.0360661  -0.00277138 -0.0518477  422  SER A CB  
3132 O  OG  . SER A 386 ? 0.263788 0.362275 0.359862 -0.0409345  0.0034073   -0.0439163  422  SER A OG  
3133 N  N   . THR A 387 ? 0.249752 0.408849 0.395878 -0.0292637  -0.00873868 -0.0769701  423  THR A N   
3134 C  CA  . THR A 387 ? 0.251139 0.42358  0.408732 -0.0234211  -0.0168911  -0.0860873  423  THR A CA  
3135 C  C   . THR A 387 ? 0.289201 0.473575 0.463209 -0.0344723  -0.0143573  -0.0932101  423  THR A C   
3136 O  O   . THR A 387 ? 0.242649 0.432461 0.424025 -0.045436   -0.00547965 -0.0938089  423  THR A O   
3137 C  CB  . THR A 387 ? 0.263582 0.452003 0.428964 -0.0123844  -0.0212002  -0.093156   423  THR A CB  
3138 O  OG1 . THR A 387 ? 0.275949 0.480495 0.454612 -0.0186237  -0.0133381  -0.0982896  423  THR A OG1 
3139 C  CG2 . THR A 387 ? 0.282887 0.457743 0.432107 -0.00124411 -0.0242882  -0.086575   423  THR A CG2 
3140 N  N   . PRO A 388 ? 0.278256 0.467448 0.458244 -0.0317843  -0.0221695  -0.0993271  424  PRO A N   
3141 C  CA  . PRO A 388 ? 0.291097 0.493512 0.488666 -0.0413861  -0.0210693  -0.10818    424  PRO A CA  
3142 C  C   . PRO A 388 ? 0.317751 0.544154 0.534776 -0.045646   -0.0160611  -0.11718    424  PRO A C   
3143 O  O   . PRO A 388 ? 0.340413 0.571428 0.567513 -0.0592713  -0.00781591 -0.119232   424  PRO A O   
3144 C  CB  . PRO A 388 ? 0.321    0.528039 0.519839 -0.0320203  -0.0328673  -0.114447   424  PRO A CB  
3145 C  CG  . PRO A 388 ? 0.321008 0.504355 0.496666 -0.0246164  -0.0363227  -0.103606   424  PRO A CG  
3146 C  CD  . PRO A 388 ? 0.284743 0.465138 0.453003 -0.0199915  -0.0320581  -0.0975316  424  PRO A CD  
3147 N  N   . LYS A 389 ? 0.289186 0.529763 0.510905 -0.0339796  -0.0208376  -0.12233    425  LYS A N   
3148 C  CA  . LYS A 389 ? 0.340742 0.605556 0.581102 -0.0359463  -0.0162067  -0.131473   425  LYS A CA  
3149 C  C   . LYS A 389 ? 0.338165 0.59996  0.577415 -0.0483879  -0.00254821 -0.126471   425  LYS A C   
3150 O  O   . LYS A 389 ? 0.269119 0.5473   0.525256 -0.0597352  0.00492204  -0.133441   425  LYS A O   
3151 C  CB  . LYS A 389 ? 0.301592 0.576111 0.542556 -0.0194871  -0.0236623  -0.135344   425  LYS A CB  
3152 C  CG  . LYS A 389 ? 0.371551 0.658401 0.619737 -0.0195402  -0.0161212  -0.137991   425  LYS A CG  
3153 C  CD  . LYS A 389 ? 0.434611 0.741084 0.694384 -0.00554783 -0.0224491  -0.147488   425  LYS A CD  
3154 C  CE  . LYS A 389 ? 0.425266 0.739302 0.689066 -0.00876298 -0.0121567  -0.14832    425  LYS A CE  
3155 N  NZ  . LYS A 389 ? 0.391136 0.732155 0.675044 0.00016189  -0.015532   -0.161515   425  LYS A NZ  
3156 N  N   . HIS A 390 ? 0.298158 0.540163 0.517498 -0.0459856  0.00068405  -0.114908   426  HIS A N   
3157 C  CA  . HIS A 390 ? 0.288906 0.52762  0.50401  -0.0557632  0.0126632   -0.109698   426  HIS A CA  
3158 C  C   . HIS A 390 ? 0.264443 0.492393 0.477881 -0.0715632  0.0197456   -0.104911   426  HIS A C   
3159 O  O   . HIS A 390 ? 0.266811 0.502356 0.487096 -0.0833252  0.0300089   -0.106182   426  HIS A O   
3160 C  CB  . HIS A 390 ? 0.26864  0.48991  0.463339 -0.0491943  0.0136549   -0.0995219  426  HIS A CB  
3161 C  CG  . HIS A 390 ? 0.332889 0.556583 0.525427 -0.0577334  0.0252998   -0.0969327  426  HIS A CG  
3162 N  ND1 . HIS A 390 ? 0.360762 0.602884 0.562743 -0.0540882  0.0288414   -0.104165   426  HIS A ND1 
3163 C  CD2 . HIS A 390 ? 0.320766 0.533028 0.504127 -0.0700379  0.0344219   -0.0891246  426  HIS A CD2 
3164 C  CE1 . HIS A 390 ? 0.368145 0.611001 0.566683 -0.0642867  0.0401605   -0.101238   426  HIS A CE1 
3165 N  NE2 . HIS A 390 ? 0.411334 0.635138 0.597266 -0.0737448  0.0434178   -0.0913929  426  HIS A NE2 
3166 N  N   . LEU A 391 ? 0.268714 0.476714 0.47086  -0.0716969  0.014914    -0.098382   427  LEU A N   
3167 C  CA  . LEU A 391 ? 0.26796  0.463271 0.468439 -0.0852483  0.0201422   -0.0940741  427  LEU A CA  
3168 C  C   . LEU A 391 ? 0.270146 0.48468  0.493195 -0.0959722  0.0236815   -0.105194   427  LEU A C   
3169 O  O   . LEU A 391 ? 0.26865  0.481201 0.494636 -0.110079   0.0336795   -0.103288   427  LEU A O   
3170 C  CB  . LEU A 391 ? 0.225009 0.398376 0.412464 -0.0820951  0.0133336   -0.0876127  427  LEU A CB  
3171 C  CG  . LEU A 391 ? 0.212093 0.365583 0.377736 -0.0742545  0.0115255   -0.076209   427  LEU A CG  
3172 C  CD1 . LEU A 391 ? 0.193821 0.327855 0.348074 -0.0708962  0.00514852  -0.0709531  427  LEU A CD1 
3173 C  CD2 . LEU A 391 ? 0.211337 0.355078 0.366702 -0.0823201  0.0214625   -0.0673369  427  LEU A CD2 
3174 N  N   . HIS A 392 ? 0.248373 0.482225 0.487359 -0.0893697  0.0156634   -0.117035   428  HIS A N   
3175 C  CA  . HIS A 392 ? 0.242061 0.496457 0.504366 -0.099627   0.0186872   -0.128973   428  HIS A CA  
3176 C  C   . HIS A 392 ? 0.240149 0.512255 0.513789 -0.107875   0.0300387   -0.132802   428  HIS A C   
3177 O  O   . HIS A 392 ? 0.241999 0.521607 0.528347 -0.122983   0.0387889   -0.136952   428  HIS A O   
3178 C  CB  . HIS A 392 ? 0.257777 0.530054 0.534453 -0.0903106  0.00683782  -0.141315   428  HIS A CB  
3179 C  CG  . HIS A 392 ? 0.290372 0.589931 0.594231 -0.0994218  0.0097682   -0.15581    428  HIS A CG  
3180 N  ND1 . HIS A 392 ? 0.34226  0.641705 0.657354 -0.113944   0.0134668   -0.160395   428  HIS A ND1 
3181 C  CD2 . HIS A 392 ? 0.298216 0.626755 0.62122  -0.0962621  0.00999786  -0.167276   428  HIS A CD2 
3182 C  CE1 . HIS A 392 ? 0.356656 0.685506 0.697723 -0.119735   0.0156994   -0.174764   428  HIS A CE1 
3183 N  NE2 . HIS A 392 ? 0.328461 0.676164 0.674996 -0.108734   0.0135165   -0.179274   428  HIS A NE2 
3184 N  N   . SER A 393 ? 0.248998 0.526653 0.517228 -0.098666   0.0307535   -0.131189   429  SER A N   
3185 C  CA  . SER A 393 ? 0.252159 0.548221 0.530948 -0.105481   0.0416619   -0.13579    429  SER A CA  
3186 C  C   . SER A 393 ? 0.241907 0.52128  0.507025 -0.119693   0.0547566   -0.124769   429  SER A C   
3187 O  O   . SER A 393 ? 0.22969  0.523385 0.50431  -0.12994    0.0657184   -0.128708   429  SER A O   
3188 C  CB  . SER A 393 ? 0.253136 0.561521 0.532078 -0.0908991  0.0381989   -0.139209   429  SER A CB  
3189 O  OG  . SER A 393 ? 0.28533  0.573066 0.540995 -0.0862028  0.0402119   -0.12695    429  SER A OG  
3190 N  N   . LEU A 394 ? 0.242372 0.492231 0.484683 -0.119553   0.0535163   -0.111102   430  LEU A N   
3191 C  CA  . LEU A 394 ? 0.301801 0.532966 0.529838 -0.132625   0.0641085   -0.0999661  430  LEU A CA  
3192 C  C   . LEU A 394 ? 0.372527 0.595318 0.606796 -0.146657   0.0672131   -0.0999727  430  LEU A C   
3193 O  O   . LEU A 394 ? 0.381326 0.584765 0.60282  -0.157741   0.0750884   -0.0898833  430  LEU A O   
3194 C  CB  . LEU A 394 ? 0.286704 0.490622 0.488805 -0.124926   0.0598882   -0.0862183  430  LEU A CB  
3195 C  CG  . LEU A 394 ? 0.283882 0.491126 0.476563 -0.113049   0.0583363   -0.0843887  430  LEU A CG  
3196 C  CD1 . LEU A 394 ? 0.274437 0.455725 0.444394 -0.106372   0.05323     -0.0722705  430  LEU A CD1 
3197 C  CD2 . LEU A 394 ? 0.306944 0.525281 0.499942 -0.120725   0.0705303   -0.084869   430  LEU A CD2 
3198 N  N   . ASN A 395 ? 0.338136 0.573899 0.590818 -0.1455     0.0602981   -0.11106    431  ASN A N   
3199 C  CA  . ASN A 395 ? 0.355123 0.583713 0.615707 -0.157956   0.0619454   -0.113071   431  ASN A CA  
3200 C  C   . ASN A 395 ? 0.344364 0.54005  0.584718 -0.156606   0.0574288   -0.101013   431  ASN A C   
3201 O  O   . ASN A 395 ? 0.339538 0.51918  0.577024 -0.169631   0.0636061   -0.0961912  431  ASN A O   
3202 C  CB  . ASN A 395 ? 0.413435 0.647979 0.683019 -0.177042   0.0766245   -0.114317   431  ASN A CB  
3203 C  CG  . ASN A 395 ? 0.424415 0.667453 0.715048 -0.189038   0.0775573   -0.12472    431  ASN A CG  
3204 O  OD1 . ASN A 395 ? 0.455764 0.709955 0.759632 -0.182123   0.0670642   -0.134898   431  ASN A OD1 
3205 N  ND2 . ASN A 395 ? 0.416936 0.654459 0.710674 -0.207421   0.0899642   -0.122609   431  ASN A ND2 
3206 N  N   . LEU A 396 ? 0.267681 0.454563 0.496496 -0.141389   0.0465028   -0.0976679  432  LEU A N   
3207 C  CA  . LEU A 396 ? 0.286217 0.444282 0.496772 -0.138739   0.0420014   -0.0872044  432  LEU A CA  
3208 C  C   . LEU A 396 ? 0.293664 0.453135 0.509115 -0.12926    0.0296927   -0.0939109  432  LEU A C   
3209 O  O   . LEU A 396 ? 0.320981 0.459884 0.522519 -0.124392   0.0245366   -0.0870671  432  LEU A O   
3210 C  CB  . LEU A 396 ? 0.287531 0.428936 0.475004 -0.130564   0.0418198   -0.074451   432  LEU A CB  
3211 C  CG  . LEU A 396 ? 0.277505 0.418346 0.456753 -0.137361   0.0529232   -0.0676222  432  LEU A CG  
3212 C  CD1 . LEU A 396 ? 0.272519 0.397023 0.429495 -0.12772    0.0502575   -0.0564228  432  LEU A CD1 
3213 C  CD2 . LEU A 396 ? 0.293297 0.421257 0.470181 -0.153675   0.0628361   -0.0621447  432  LEU A CD2 
3214 N  N   . LEU A 397 ? 0.288012 0.472211 0.522506 -0.125926   0.0246841   -0.107425   433  LEU A N   
3215 C  CA  . LEU A 397 ? 0.339193 0.526387 0.576842 -0.116008   0.0125055   -0.114155   433  LEU A CA  
3216 C  C   . LEU A 397 ? 0.37631  0.590382 0.639468 -0.120992   0.0114045   -0.129786   433  LEU A C   
3217 O  O   . LEU A 397 ? 0.369492 0.601986 0.644315 -0.12549    0.0181086   -0.134122   433  LEU A O   
3218 C  CB  . LEU A 397 ? 0.379188 0.569405 0.606589 -0.0985706  0.00411226  -0.112249   433  LEU A CB  
3219 C  CG  . LEU A 397 ? 0.528702 0.713232 0.750033 -0.0874874  -0.00786849 -0.11435    433  LEU A CG  
3220 C  CD1 . LEU A 397 ? 0.523243 0.70318  0.72904  -0.072455   -0.0132746  -0.108201   433  LEU A CD1 
3221 C  CD2 . LEU A 397 ? 0.613669 0.817382 0.852393 -0.0856934  -0.0159512  -0.12878    433  LEU A CD2 
3222 N  N   . SER A 398 ? 0.393825 0.610641 0.665345 -0.1204     0.00356137  -0.138318   434  SER A N   
3223 C  CA  . SER A 398 ? 0.474825 0.718106 0.771833 -0.125334   0.00134872  -0.154593   434  SER A CA  
3224 C  C   . SER A 398 ? 0.4753   0.747088 0.783524 -0.113131   -0.0052066  -0.164028   434  SER A C   
3225 O  O   . SER A 398 ? 0.468897 0.767277 0.800001 -0.118218   -0.00335247 -0.176518   434  SER A O   
3226 C  CB  . SER A 398 ? 0.468047 0.706915 0.768977 -0.125744   -0.00674346 -0.161545   434  SER A CB  
3227 O  OG  . SER A 398 ? 0.619762 0.834082 0.914175 -0.13791    -0.00041343 -0.15489    434  SER A OG  
3228 N  N   . SER A 399 ? 0.544902 0.810596 0.837214 -0.0967749  -0.013345   -0.158422   435  SER A N   
3229 C  CA  . SER A 399 ? 0.545679 0.831672 0.842932 -0.0827267  -0.0201273  -0.164126   435  SER A CA  
3230 C  C   . SER A 399 ? 0.697575 0.965426 0.970957 -0.0672659  -0.0278592  -0.15409    435  SER A C   
3231 O  O   . SER A 399 ? 0.888936 1.16623  1.16044  -0.0547919  -0.0321613  -0.154708   435  SER A O   
3232 C  CB  . SER A 399 ? 0.488237 0.799756 0.805957 -0.0797692  -0.0288287  -0.180119   435  SER A CB  
3233 O  OG  . SER A 399 ? 0.429074 0.729032 0.737133 -0.0741152  -0.0386653  -0.180294   435  SER A OG  
3234 N  N   . GLY A 402 ? 0.636396 0.937839 0.896779 -0.00387351 -0.0822493  -0.175113   438  GLY A N   
3235 C  CA  . GLY A 402 ? 0.682857 0.995372 0.943761 0.00660527  -0.0960377  -0.183934   438  GLY A CA  
3236 C  C   . GLY A 402 ? 0.735383 1.02552  0.968489 0.0173874   -0.102725   -0.174184   438  GLY A C   
3237 O  O   . GLY A 402 ? 0.668352 0.95253  0.887407 0.0307135   -0.107359   -0.168037   438  GLY A O   
3238 N  N   . SER A 403 ? 0.689086 0.966213 0.914189 0.0112283   -0.102767   -0.172973   439  SER A N   
3239 C  CA  . SER A 403 ? 0.541957 0.80706  0.746507 0.0208836   -0.111492   -0.16992    439  SER A CA  
3240 C  C   . SER A 403 ? 0.532261 0.772469 0.710789 0.0279807   -0.108963   -0.154408   439  SER A C   
3241 O  O   . SER A 403 ? 0.498271 0.725079 0.672625 0.0223821   -0.0991796  -0.144866   439  SER A O   
3242 C  CB  . SER A 403 ? 0.585431 0.845322 0.791686 0.0111417   -0.111046   -0.174579   439  SER A CB  
3243 O  OG  . SER A 403 ? 0.551906 0.795481 0.758336 -0.002152   -0.099055   -0.167285   439  SER A OG  
3244 N  N   . ASP A 404 ? 0.447505 0.681464 0.607742 0.0400134   -0.117954   -0.152213   440  ASP A N   
3245 C  CA  . ASP A 404 ? 0.559411 0.768522 0.693451 0.0447388   -0.116156   -0.139193   440  ASP A CA  
3246 C  C   . ASP A 404 ? 0.457504 0.648937 0.586806 0.0327781   -0.107033   -0.133397   440  ASP A C   
3247 O  O   . ASP A 404 ? 0.389674 0.562383 0.504944 0.0322573   -0.100785   -0.121945   440  ASP A O   
3248 C  CB  . ASP A 404 ? 0.605109 0.811922 0.722649 0.0546013   -0.1264     -0.141003   440  ASP A CB  
3249 C  CG  . ASP A 404 ? 0.786857 0.988963 0.886636 0.0701149   -0.133354   -0.134993   440  ASP A CG  
3250 O  OD1 . ASP A 404 ? 0.769246 0.988786 0.877913 0.0788948   -0.141646   -0.142025   440  ASP A OD1 
3251 O  OD2 . ASP A 404 ? 0.816866 0.997659 0.894572 0.0730726   -0.130189   -0.123418   440  ASP A OD2 
3252 N  N   . GLU A 405 ? 0.435305 0.632511 0.575631 0.0241167   -0.107417   -0.142056   441  GLU A N   
3253 C  CA  . GLU A 405 ? 0.426849 0.607709 0.56387  0.0136812   -0.100202   -0.138127   441  GLU A CA  
3254 C  C   . GLU A 405 ? 0.382897 0.555792 0.525825 0.00441586  -0.0890793  -0.130625   441  GLU A C   
3255 O  O   . GLU A 405 ? 0.313971 0.467724 0.444021 0.0023655   -0.0835344  -0.120792   441  GLU A O   
3256 C  CB  . GLU A 405 ? 0.453248 0.642759 0.602276 0.00701299  -0.103703   -0.150322   441  GLU A CB  
3257 C  CG  . GLU A 405 ? 0.53726  0.733111 0.675793 0.0177181   -0.115094   -0.15657    441  GLU A CG  
3258 C  CD  . GLU A 405 ? 0.602713 0.799601 0.745906 0.0116161   -0.117741   -0.166458   441  GLU A CD  
3259 O  OE1 . GLU A 405 ? 0.62038  0.815955 0.779245 -0.00120154 -0.111052   -0.169519   441  GLU A OE1 
3260 O  OE2 . GLU A 405 ? 0.663956 0.861775 0.795122 0.0187812   -0.125675   -0.170933   441  GLU A OE2 
3261 N  N   . HIS A 406 ? 0.390334 0.578751 0.552025 -0.00058334 -0.0860917  -0.135544   442  HIS A N   
3262 C  CA  . HIS A 406 ? 0.377152 0.558975 0.543538 -0.0097543  -0.0752817  -0.12877    442  HIS A CA  
3263 C  C   . HIS A 406 ? 0.397863 0.569303 0.548857 -0.00160298 -0.0732571  -0.117655   442  HIS A C   
3264 O  O   . HIS A 406 ? 0.361457 0.519549 0.50671  -0.00674688 -0.0651728  -0.108632   442  HIS A O   
3265 C  CB  . HIS A 406 ? 0.372084 0.574593 0.561581 -0.0168067  -0.0720737  -0.13724    442  HIS A CB  
3266 C  CG  . HIS A 406 ? 0.505245 0.713361 0.711117 -0.0298843  -0.0694362  -0.145787   442  HIS A CG  
3267 N  ND1 . HIS A 406 ? 0.469057 0.65917  0.672023 -0.041152   -0.0621607  -0.140625   442  HIS A ND1 
3268 C  CD2 . HIS A 406 ? 0.470716 0.700738 0.696912 -0.0334836  -0.0733523  -0.159781   442  HIS A CD2 
3269 C  CE1 . HIS A 406 ? 0.544096 0.742927 0.764165 -0.0515379  -0.061389   -0.150715   442  HIS A CE1 
3270 N  NE2 . HIS A 406 ? 0.582192 0.805987 0.817047 -0.047492   -0.0681004  -0.162912   442  HIS A NE2 
3271 N  N   . ASP A 407 ? 0.34516  0.522658 0.489362 0.0113128   -0.0811512  -0.118777   443  ASP A N   
3272 C  CA  . ASP A 407 ? 0.3197   0.48747  0.449946 0.0195792   -0.0800259  -0.109406   443  ASP A CA  
3273 C  C   . ASP A 407 ? 0.311486 0.455644 0.42127  0.0196442   -0.076815   -0.0984367  443  ASP A C   
3274 O  O   . ASP A 407 ? 0.280177 0.413045 0.383557 0.0176797   -0.0701091  -0.0898022  443  ASP A O   
3275 C  CB  . ASP A 407 ? 0.404026 0.580563 0.529657 0.0336435   -0.0900595  -0.112848   443  ASP A CB  
3276 C  CG  . ASP A 407 ? 0.463961 0.638023 0.584508 0.0416015   -0.0889604  -0.107201   443  ASP A CG  
3277 O  OD1 . ASP A 407 ? 0.501338 0.679739 0.632494 0.035726    -0.081627   -0.106706   443  ASP A OD1 
3278 O  OD2 . ASP A 407 ? 0.566602 0.735123 0.673127 0.053567    -0.0955574  -0.104088   443  ASP A OD2 
3279 N  N   . ILE A 408 ? 0.283183 0.421256 0.382992 0.0222647   -0.0817641  -0.0995447  444  ILE A N   
3280 C  CA  . ILE A 408 ? 0.274974 0.393275 0.355569 0.0237138   -0.0796986  -0.090769   444  ILE A CA  
3281 C  C   . ILE A 408 ? 0.261694 0.370062 0.346431 0.0123242   -0.0713453  -0.0871059  444  ILE A C   
3282 O  O   . ILE A 408 ? 0.304732 0.397654 0.377634 0.0117437   -0.0667349  -0.0783128  444  ILE A O   
3283 C  CB  . ILE A 408 ? 0.26545  0.383059 0.336391 0.0286938   -0.0869673  -0.0951165  444  ILE A CB  
3284 C  CG1 . ILE A 408 ? 0.262797 0.386254 0.323669 0.0417154   -0.0958159  -0.0963355  444  ILE A CG1 
3285 C  CG2 . ILE A 408 ? 0.259759 0.359246 0.315474 0.0269741   -0.0831993  -0.0883814  444  ILE A CG2 
3286 C  CD1 . ILE A 408 ? 0.270101 0.385228 0.319411 0.0493375   -0.0945439  -0.0871969  444  ILE A CD1 
3287 N  N   . ASN A 409 ? 0.246986 0.364189 0.348468 0.00339161  -0.0698579  -0.0942829  445  ASN A N   
3288 C  CA  . ASN A 409 ? 0.261056 0.36845  0.367232 -0.00777386 -0.0623177  -0.0911255  445  ASN A CA  
3289 C  C   . ASN A 409 ? 0.26123  0.364064 0.366748 -0.0107386  -0.0548673  -0.0829779  445  ASN A C   
3290 O  O   . ASN A 409 ? 0.266139 0.353933 0.364192 -0.0147192  -0.0496382  -0.0752771  445  ASN A O   
3291 C  CB  . ASN A 409 ? 0.294199 0.41091  0.418306 -0.0174479  -0.0616985  -0.100317   445  ASN A CB  
3292 C  CG  . ASN A 409 ? 0.329381 0.444504 0.454284 -0.0186731  -0.0665036  -0.107598   445  ASN A CG  
3293 O  OD1 . ASN A 409 ? 0.335651 0.440458 0.446705 -0.0133757  -0.0693786  -0.105316   445  ASN A OD1 
3294 N  ND2 . ASN A 409 ? 0.320694 0.44543  0.462623 -0.0270705  -0.066387   -0.11683    445  ASN A ND2 
3295 N  N   . PHE A 410 ? 0.232049 0.348196 0.345457 -0.0085538  -0.0546082  -0.0852346  446  PHE A N   
3296 C  CA  . PHE A 410 ? 0.224267 0.337612 0.336802 -0.0108754  -0.0476679  -0.0786709  446  PHE A CA  
3297 C  C   . PHE A 410 ? 0.243165 0.342042 0.337678 -0.00379363 -0.047325   -0.0692867  446  PHE A C   
3298 O  O   . PHE A 410 ? 0.25073  0.33833  0.339045 -0.00775761 -0.0413379  -0.0617436  446  PHE A O   
3299 C  CB  . PHE A 410 ? 0.24472  0.377314 0.369834 -0.00792927 -0.0486962  -0.0849909  446  PHE A CB  
3300 C  CG  . PHE A 410 ? 0.26273  0.393284 0.384404 -0.00686259 -0.0430115  -0.07906    446  PHE A CG  
3301 C  CD1 . PHE A 410 ? 0.262039 0.386984 0.38498  -0.0167714  -0.0341289  -0.0742526  446  PHE A CD1 
3302 C  CD2 . PHE A 410 ? 0.254442 0.386925 0.370064 0.00418185  -0.0466938  -0.0780202  446  PHE A CD2 
3303 C  CE1 . PHE A 410 ? 0.261915 0.385234 0.380805 -0.0159976  -0.0289248  -0.0694024  446  PHE A CE1 
3304 C  CE2 . PHE A 410 ? 0.267404 0.397593 0.380185 0.00499762  -0.0415181  -0.0735717  446  PHE A CE2 
3305 C  CZ  . PHE A 410 ? 0.278823 0.405433 0.393518 -0.00520481 -0.0325489  -0.0696778  446  PHE A CZ  
3306 N  N   . LEU A 411 ? 0.233503 0.332204 0.3189   0.0065516   -0.0538575  -0.0697317  447  LEU A N   
3307 C  CA  . LEU A 411 ? 0.248188 0.333226 0.31635  0.01326     -0.0537572  -0.061551   447  LEU A CA  
3308 C  C   . LEU A 411 ? 0.240137 0.309362 0.298548 0.00897074  -0.0503667  -0.0555568  447  LEU A C   
3309 O  O   . LEU A 411 ? 0.245327 0.303708 0.295047 0.00868711  -0.0460253  -0.0480882  447  LEU A O   
3310 C  CB  . LEU A 411 ? 0.259872 0.345995 0.318489 0.0247201   -0.0612148  -0.0626504  447  LEU A CB  
3311 C  CG  . LEU A 411 ? 0.274738 0.372334 0.339025 0.032024    -0.064584   -0.0659764  447  LEU A CG  
3312 C  CD1 . LEU A 411 ? 0.246047 0.344749 0.300974 0.0436493   -0.0733105  -0.0675949  447  LEU A CD1 
3313 C  CD2 . LEU A 411 ? 0.232662 0.324131 0.294044 0.0323638   -0.0588366  -0.0599073  447  LEU A CD2 
3314 N  N   . MET A 412 ? 0.237189 0.305904 0.298332 0.00551933  -0.0523549  -0.0596326  448  MET A N   
3315 C  CA  . MET A 412 ? 0.227433 0.28235  0.281438 0.00190735  -0.0495894  -0.05536    448  MET A CA  
3316 C  C   . MET A 412 ? 0.246949 0.296069 0.305359 -0.00616814 -0.0427178  -0.0504439  448  MET A C   
3317 O  O   . MET A 412 ? 0.235146 0.272677 0.285302 -0.00685149 -0.039517   -0.043868   448  MET A O   
3318 C  CB  . MET A 412 ? 0.2603   0.316801 0.318543 -0.00034022 -0.0531901  -0.0623179  448  MET A CB  
3319 C  CG  . MET A 412 ? 0.26816  0.311109 0.321325 -0.00384946 -0.0504883  -0.0591762  448  MET A CG  
3320 S  SD  . MET A 412 ? 0.379606 0.410732 0.414542 0.00269225  -0.0493701  -0.0515862  448  MET A SD  
3321 C  CE  . MET A 412 ? 0.337614 0.372705 0.361529 0.0115305   -0.0556018  -0.0555496  448  MET A CE  
3322 N  N   . LYS A 413 ? 0.285205 0.342707 0.356628 -0.0126748  -0.0403902  -0.0538951  449  LYS A N   
3323 C  CA  . LYS A 413 ? 0.320998 0.372512 0.394738 -0.020568   -0.0337132  -0.0487726  449  LYS A CA  
3324 C  C   . LYS A 413 ? 0.302376 0.34986  0.367412 -0.0174381  -0.0304617  -0.0416782  449  LYS A C   
3325 O  O   . LYS A 413 ? 0.289825 0.325591 0.34731  -0.0195247  -0.0271493  -0.0348989  449  LYS A O   
3326 C  CB  . LYS A 413 ? 0.344733 0.406129 0.433601 -0.0289353  -0.0312735  -0.0542841  449  LYS A CB  
3327 C  CG  . LYS A 413 ? 0.465348 0.520519 0.55478  -0.0372378  -0.0239266  -0.0484223  449  LYS A CG  
3328 C  CD  . LYS A 413 ? 0.7093   0.766333 0.810606 -0.0481315  -0.0203374  -0.0519297  449  LYS A CD  
3329 C  CE  . LYS A 413 ? 0.834987 0.874318 0.929894 -0.0548963  -0.0156481  -0.0440699  449  LYS A CE  
3330 N  NZ  . LYS A 413 ? 0.82729  0.860486 0.9127   -0.0554111  -0.0107542  -0.0352642  449  LYS A NZ  
3331 N  N   . MET A 414 ? 0.262319 0.318671 0.327576 -0.0113516  -0.0322808  -0.0435736  450  MET A N   
3332 C  CA  . MET A 414 ? 0.240366 0.293486 0.298267 -0.00791961 -0.0295845  -0.0383028  450  MET A CA  
3333 C  C   . MET A 414 ? 0.237197 0.276959 0.280982 -0.00355484 -0.0303481  -0.0324214  450  MET A C   
3334 O  O   . MET A 414 ? 0.257904 0.290604 0.295618 -0.00473216 -0.0265695  -0.026849   450  MET A O   
3335 C  CB  . MET A 414 ? 0.257081 0.322022 0.319399 -0.00184335 -0.0316221  -0.0423885  450  MET A CB  
3336 C  CG  . MET A 414 ? 0.272817 0.354189 0.351195 -0.00632787 -0.0297971  -0.0491155  450  MET A CG  
3337 S  SD  . MET A 414 ? 0.389613 0.469842 0.470056 -0.0157145  -0.0203813  -0.0448146  450  MET A SD  
3338 C  CE  . MET A 414 ? 0.337239 0.404443 0.401863 -0.0100089  -0.0191827  -0.0369987  450  MET A CE  
3339 N  N   . ALA A 415 ? 0.217329 0.254841 0.255958 0.00142607  -0.0350539  -0.0341835  451  ALA A N   
3340 C  CA  . ALA A 415 ? 0.243866 0.270109 0.269857 0.00493097  -0.035452   -0.0297652  451  ALA A CA  
3341 C  C   . ALA A 415 ? 0.256377 0.273273 0.280465 -0.00045664 -0.0319442  -0.025713   451  ALA A C   
3342 O  O   . ALA A 415 ? 0.248295 0.257465 0.264373 0.00063833  -0.0298095  -0.0208652  451  ALA A O   
3343 C  CB  . ALA A 415 ? 0.210457 0.237854 0.232359 0.00982854  -0.0407892  -0.0336562  451  ALA A CB  
3344 N  N   . LEU A 416 ? 0.237884 0.25524  0.269706 -0.00619278 -0.0315714  -0.0279836  452  LEU A N   
3345 C  CA  . LEU A 416 ? 0.25716  0.264372 0.286638 -0.00986803 -0.0294024  -0.024258   452  LEU A CA  
3346 C  C   . LEU A 416 ? 0.299933 0.303377 0.326975 -0.0127267  -0.0250322  -0.018186   452  LEU A C   
3347 O  O   . LEU A 416 ? 0.323784 0.31893  0.345712 -0.0131202  -0.0238641  -0.0140403  452  LEU A O   
3348 C  CB  . LEU A 416 ? 0.210769 0.217452 0.248642 -0.0150374  -0.030278   -0.0281752  452  LEU A CB  
3349 C  CG  . LEU A 416 ? 0.235371 0.245456 0.274846 -0.0121369  -0.0349656  -0.0350094  452  LEU A CG  
3350 C  CD1 . LEU A 416 ? 0.229662 0.240009 0.279727 -0.0185203  -0.0354182  -0.039933   452  LEU A CD1 
3351 C  CD2 . LEU A 416 ? 0.236125 0.238418 0.267021 -0.00818571 -0.0360878  -0.0339608  452  LEU A CD2 
3352 N  N   . ASP A 417 ? 0.311276 0.321903 0.342152 -0.0142826  -0.0229025  -0.0184087  453  ASP A N   
3353 C  CA  . ASP A 417 ? 0.344939 0.3538   0.372863 -0.0167366  -0.0187579  -0.0136523  453  ASP A CA  
3354 C  C   . ASP A 417 ? 0.385957 0.394367 0.406715 -0.0112369  -0.0186868  -0.0119456  453  ASP A C   
3355 O  O   . ASP A 417 ? 0.650399 0.653282 0.665343 -0.0118129  -0.0166287  -0.00773322 453  ASP A O   
3356 C  CB  . ASP A 417 ? 0.392633 0.409863 0.428301 -0.0217948  -0.0155544  -0.0153739  453  ASP A CB  
3357 C  CG  . ASP A 417 ? 0.633372 0.649727 0.67626  -0.0287735  -0.0146197  -0.0167897  453  ASP A CG  
3358 O  OD1 . ASP A 417 ? 0.683918 0.68929  0.7227   -0.0316262  -0.0139767  -0.0124761  453  ASP A OD1 
3359 O  OD2 . ASP A 417 ? 0.663458 0.689765 0.716477 -0.0310085  -0.0150255  -0.0226921  453  ASP A OD2 
3360 N  N   . LYS A 418 ? 0.293548 0.307244 0.314524 -0.00590785 -0.0210656  -0.0152208  454  LYS A N   
3361 C  CA  . LYS A 418 ? 0.270809 0.283156 0.285768 -0.00132726 -0.0203853  -0.0136716  454  LYS A CA  
3362 C  C   . LYS A 418 ? 0.278342 0.28227  0.283839 0.00285532  -0.0218683  -0.011456   454  LYS A C   
3363 O  O   . LYS A 418 ? 0.247312 0.245625 0.246994 0.00298698  -0.0195845  -0.00821768 454  LYS A O   
3364 C  CB  . LYS A 418 ? 0.273297 0.294661 0.292982 0.00285709  -0.0219652  -0.0178879  454  LYS A CB  
3365 C  CG  . LYS A 418 ? 0.265574 0.296849 0.295305 -0.00226321 -0.0188854  -0.0204404  454  LYS A CG  
3366 C  CD  . LYS A 418 ? 0.203692 0.232428 0.230139 -0.00579181 -0.0138364  -0.0168617  454  LYS A CD  
3367 C  CE  . LYS A 418 ? 0.242556 0.283304 0.278974 -0.00992111 -0.010703   -0.0206269  454  LYS A CE  
3368 N  NZ  . LYS A 418 ? 0.263581 0.302754 0.295816 -0.0134942  -0.00568228 -0.0175589  454  LYS A NZ  
3369 N  N   . ILE A 419 ? 0.276708 0.280182 0.280545 0.00574616  -0.0253201  -0.0135582  455  ILE A N   
3370 C  CA  . ILE A 419 ? 0.245184 0.241345 0.239191 0.0093713   -0.0260262  -0.0117121  455  ILE A CA  
3371 C  C   . ILE A 419 ? 0.239756 0.230188 0.231985 0.00580168  -0.0238975  -0.00937116 455  ILE A C   
3372 O  O   . ILE A 419 ? 0.27106  0.255888 0.256869 0.00642312  -0.0219119  -0.00676569 455  ILE A O   
3373 C  CB  . ILE A 419 ? 0.253245 0.252079 0.245746 0.0132295   -0.0304398  -0.0153215  455  ILE A CB  
3374 C  CG1 . ILE A 419 ? 0.313408 0.31889  0.307664 0.0183886   -0.0340435  -0.0182792  455  ILE A CG1 
3375 C  CG2 . ILE A 419 ? 0.191559 0.18313  0.173282 0.0157448   -0.0303716  -0.0135847  455  ILE A CG2 
3376 C  CD1 . ILE A 419 ? 0.409468 0.409598 0.396062 0.0231356   -0.0332405  -0.0151117  455  ILE A CD1 
3377 N  N   . ALA A 420 ? 0.254229 0.245864 0.252558 0.00224371  -0.0245671  -0.010827   456  ALA A N   
3378 C  CA  . ALA A 420 ? 0.260566 0.246783 0.257866 0.0001832   -0.0234738  -0.00915355 456  ALA A CA  
3379 C  C   . ALA A 420 ? 0.262364 0.245715 0.257474 -0.00157948 -0.0205117  -0.00507943 456  ALA A C   
3380 O  O   . ALA A 420 ? 0.255757 0.235412 0.247858 -0.00139805 -0.0195683  -0.003735   456  ALA A O   
3381 C  CB  . ALA A 420 ? 0.240078 0.226316 0.244662 -0.00334037 -0.0247582  -0.0110223  456  ALA A CB  
3382 N  N   . PHE A 421 ? 0.226326 0.212569 0.22342  -0.0033019  -0.0190466  -0.00387146 457  PHE A N   
3383 C  CA  . PHE A 421 ? 0.25447  0.238715 0.249257 -0.00526747 -0.016608   -0.00064311 457  PHE A CA  
3384 C  C   . PHE A 421 ? 0.276461 0.258383 0.265352 -0.00279852 -0.0151802  3.884e-05   457  PHE A C   
3385 O  O   . PHE A 421 ? 0.292416 0.272512 0.27921  -0.0041815  -0.0136471  0.00176696  457  PHE A O   
3386 C  CB  . PHE A 421 ? 0.226161 0.214951 0.224189 -0.00796167 -0.0149572  -0.00033208 457  PHE A CB  
3387 C  CG  . PHE A 421 ? 0.286862 0.274569 0.281743 -0.0103111  -0.012588   0.0026163   457  PHE A CG  
3388 C  CD1 . PHE A 421 ? 0.280489 0.264463 0.274211 -0.0129771  -0.012834   0.00563155  457  PHE A CD1 
3389 C  CD2 . PHE A 421 ? 0.244454 0.234513 0.237065 -0.00931834 -0.010598   0.00205915  457  PHE A CD2 
3390 C  CE1 . PHE A 421 ? 0.275559 0.259328 0.265394 -0.0148552  -0.011327   0.00818241  457  PHE A CE1 
3391 C  CE2 . PHE A 421 ? 0.248186 0.23805  0.237499 -0.0115319  -0.00871319 0.00392636  457  PHE A CE2 
3392 C  CZ  . PHE A 421 ? 0.303602 0.290687 0.291084 -0.0141217  -0.00928202 0.0069845   457  PHE A CZ  
3393 N  N   . ILE A 422 ? 0.279235 0.260473 0.264901 0.00083948  -0.0158981  -0.00135546 458  ILE A N   
3394 C  CA  . ILE A 422 ? 0.298407 0.275396 0.277879 0.00269216  -0.0140373  -0.00031155 458  ILE A CA  
3395 C  C   . ILE A 422 ? 0.347918 0.321267 0.324694 0.00096223  -0.0122656  0.00077631  458  ILE A C   
3396 O  O   . ILE A 422 ? 0.341282 0.313207 0.31685  -0.000691   -0.0100955  0.00161924  458  ILE A O   
3397 C  CB  . ILE A 422 ? 0.298908 0.274057 0.273847 0.00734986  -0.0155201  -0.0011338  458  ILE A CB  
3398 C  CG1 . ILE A 422 ? 0.343057 0.323383 0.322283 0.00942886  -0.0168948  -0.00288223 458  ILE A CG1 
3399 C  CG2 . ILE A 422 ? 0.278978 0.246056 0.245184 0.00882938  -0.0132964  0.00075222  458  ILE A CG2 
3400 C  CD1 . ILE A 422 ? 0.343602 0.321873 0.321442 0.010067    -0.0145742  -0.00238062 458  ILE A CD1 
3401 N  N   . PRO A 423 ? 0.298511 0.271245 0.274929 0.00126855  -0.0129975  -6.63e-05   459  PRO A N   
3402 C  CA  . PRO A 423 ? 0.251161 0.222322 0.226341 -0.00020469 -0.0108743  -2.98e-06   459  PRO A CA  
3403 C  C   . PRO A 423 ? 0.240042 0.213664 0.220294 -0.00262049 -0.0113088  0.00047615  459  PRO A C   
3404 O  O   . PRO A 423 ? 0.255628 0.229403 0.23562  -0.00405464 -0.00954654 0.00036422  459  PRO A O   
3405 C  CB  . PRO A 423 ? 0.281211 0.252461 0.255327 0.00119305  -0.0115025  -0.00194331 459  PRO A CB  
3406 C  CG  . PRO A 423 ? 0.328684 0.302026 0.305771 0.00258719  -0.0149433  -0.00317573 459  PRO A CG  
3407 C  CD  . PRO A 423 ? 0.270384 0.244293 0.246865 0.00341122  -0.0154869  -0.00202571 459  PRO A CD  
3408 N  N   . PHE A 424 ? 0.233289 0.208523 0.217727 -0.00315135 -0.0136961  0.0009295   460  PHE A N   
3409 C  CA  . PHE A 424 ? 0.245725 0.221747 0.232741 -0.0049034  -0.0145398  0.00236139  460  PHE A CA  
3410 C  C   . PHE A 424 ? 0.29548  0.2726   0.280164 -0.00645457 -0.0128699  0.00355144  460  PHE A C   
3411 O  O   . PHE A 424 ? 0.280615 0.258866 0.265286 -0.0073128  -0.0128498  0.00359206  460  PHE A O   
3412 C  CB  . PHE A 424 ? 0.240419 0.215631 0.230751 -0.00584911 -0.016804   0.00355482  460  PHE A CB  
3413 C  CG  . PHE A 424 ? 0.249479 0.223727 0.239959 -0.0070397  -0.0180112  0.00606766  460  PHE A CG  
3414 C  CD1 . PHE A 424 ? 0.271358 0.244406 0.263894 -0.00536916 -0.0201469  0.00557212  460  PHE A CD1 
3415 C  CD2 . PHE A 424 ? 0.219707 0.194635 0.207801 -0.00932949 -0.017201   0.00866974  460  PHE A CD2 
3416 C  CE1 . PHE A 424 ? 0.31045  0.282058 0.302412 -0.00527606 -0.0224443  0.00810545  460  PHE A CE1 
3417 C  CE2 . PHE A 424 ? 0.221471 0.194981 0.207573 -0.00987364 -0.0188385  0.011386    460  PHE A CE2 
3418 C  CZ  . PHE A 424 ? 0.287681 0.258921 0.275549 -0.00762221 -0.0219162  0.0114775   460  PHE A CZ  
3419 N  N   . SER A 425 ? 0.245594 0.223269 0.228924 -0.00653239 -0.0117722  0.00372986  461  SER A N   
3420 C  CA  . SER A 425 ? 0.30819  0.287136 0.28953  -0.00786609 -0.0101163  0.00399354  461  SER A CA  
3421 C  C   . SER A 425 ? 0.306588 0.283506 0.285369 -0.00778665 -0.00819557 0.00258642  461  SER A C   
3422 O  O   . SER A 425 ? 0.297909 0.275817 0.275544 -0.00931913 -0.0071335  0.00186866  461  SER A O   
3423 C  CB  . SER A 425 ? 0.23968  0.220638 0.221295 -0.00745928 -0.00910897 0.00344127  461  SER A CB  
3424 O  OG  . SER A 425 ? 0.281619 0.260567 0.262352 -0.00440318 -0.00916283 0.00211103  461  SER A OG  
3425 N  N   . TYR A 426 ? 0.347142 0.320977 0.32456  -0.00637183 -0.00747367 0.00194789  462  TYR A N   
3426 C  CA  . TYR A 426 ? 0.305977 0.27651  0.280565 -0.007215   -0.00473516 0.00091659  462  TYR A CA  
3427 C  C   . TYR A 426 ? 0.376988 0.350603 0.354531 -0.00945181 -0.00441491 -0.00047746 462  TYR A C   
3428 O  O   . TYR A 426 ? 0.331075 0.304778 0.308501 -0.0117139  -0.00252883 -0.00205657 462  TYR A O   
3429 C  CB  . TYR A 426 ? 0.403152 0.368673 0.37339  -0.00523692 -0.00356969 0.00131079  462  TYR A CB  
3430 C  CG  . TYR A 426 ? 0.359738 0.319315 0.325387 -0.00674642 0.00021527  0.00107296  462  TYR A CG  
3431 C  CD1 . TYR A 426 ? 0.431267 0.38583  0.394076 -0.00680196 0.00177255  0.00109072  462  TYR A CD1 
3432 C  CD2 . TYR A 426 ? 0.35515  0.313842 0.31954  -0.00847187 0.00269352  0.00047623  462  TYR A CD2 
3433 C  CE1 . TYR A 426 ? 0.399403 0.346273 0.35763  -0.0087259  0.00556485  0.00109654  462  TYR A CE1 
3434 C  CE2 . TYR A 426 ? 0.328459 0.281022 0.28852  -0.0110866  0.00709146  0.00043452  462  TYR A CE2 
3435 C  CZ  . TYR A 426 ? 0.387148 0.332585 0.34349  -0.0110873  0.00837437  0.00119438  462  TYR A CZ  
3436 O  OH  . TYR A 426 ? 0.37436  0.31204  0.326395 -0.0142295  0.012914    0.00128195  462  TYR A OH  
3437 N  N   . LEU A 427 ? 0.317173 0.293667 0.298128 -0.00863202 -0.00644814 -0.00063204 463  LEU A N   
3438 C  CA  . LEU A 427 ? 0.307589 0.288183 0.292651 -0.00962252 -0.00645747 -0.00285835 463  LEU A CA  
3439 C  C   . LEU A 427 ? 0.25946  0.244606 0.247386 -0.0103979  -0.00895107 -0.00324031 463  LEU A C   
3440 O  O   . LEU A 427 ? 0.243404 0.23303  0.234909 -0.0115956  -0.00860758 -0.00609665 463  LEU A O   
3441 C  CB  . LEU A 427 ? 0.316032 0.298099 0.30415  -0.00761892 -0.00786962 -0.00381039 463  LEU A CB  
3442 C  CG  . LEU A 427 ? 0.34108  0.323029 0.331651 -0.0055425  -0.0120512  -0.00228352 463  LEU A CG  
3443 C  CD1 . LEU A 427 ? 0.2905   0.276676 0.285837 -0.00495013 -0.0148291  -0.00323658 463  LEU A CD1 
3444 C  CD2 . LEU A 427 ? 0.341276 0.321906 0.332754 -0.00350638 -0.0125992  -0.00357656 463  LEU A CD2 
3445 N  N   . VAL A 428 ? 0.243688 0.228322 0.229907 -0.00984846 -0.0113366  -0.00066339 464  VAL A N   
3446 C  CA  . VAL A 428 ? 0.287928 0.276185 0.274839 -0.00986221 -0.0144797  -0.00018237 464  VAL A CA  
3447 C  C   . VAL A 428 ? 0.291434 0.283673 0.278793 -0.0119874  -0.0132368  -0.00349269 464  VAL A C   
3448 O  O   . VAL A 428 ? 0.258145 0.255838 0.249102 -0.0117792  -0.0154432  -0.00583849 464  VAL A O   
3449 C  CB  . VAL A 428 ? 0.28019  0.266599 0.263343 -0.00984226 -0.0162313  0.00361909  464  VAL A CB  
3450 C  CG1 . VAL A 428 ? 0.240367 0.229723 0.220973 -0.00996218 -0.0191476  0.00460129  464  VAL A CG1 
3451 C  CG2 . VAL A 428 ? 0.248316 0.231    0.232789 -0.00847    -0.0178451  0.00610146  464  VAL A CG2 
3452 N  N   . ASP A 429 ? 0.269887 0.259541 0.254174 -0.0138751  -0.00993301 -0.00430327 465  ASP A N   
3453 C  CA  . ASP A 429 ? 0.277874 0.270337 0.262554 -0.0164303  -0.00869965 -0.00795692 465  ASP A CA  
3454 C  C   . ASP A 429 ? 0.278324 0.270288 0.266406 -0.0186754  -0.00522666 -0.0112138  465  ASP A C   
3455 O  O   . ASP A 429 ? 0.257789 0.254329 0.249137 -0.0212559  -0.00481324 -0.0152865  465  ASP A O   
3456 C  CB  . ASP A 429 ? 0.309457 0.29921  0.289453 -0.0174069  -0.00693622 -0.00810864 465  ASP A CB  
3457 C  CG  . ASP A 429 ? 0.329727 0.32317  0.306242 -0.0169828  -0.00960327 -0.0068591  465  ASP A CG  
3458 O  OD1 . ASP A 429 ? 0.254612 0.25137  0.231297 -0.0156693  -0.0134629  -0.00483089 465  ASP A OD1 
3459 O  OD2 . ASP A 429 ? 0.277152 0.269364 0.250154 -0.0176135  -0.00767051 -0.00761061 465  ASP A OD2 
3460 N  N   . GLN A 430 ? 0.243823 0.231361 0.231386 -0.0179947  -0.00285803 -0.00983154 466  GLN A N   
3461 C  CA  . GLN A 430 ? 0.246945 0.235858 0.237893 -0.0206917  0.00057165  -0.0129572  466  GLN A CA  
3462 C  C   . GLN A 430 ? 0.272025 0.271301 0.270863 -0.0207142  -0.00217471 -0.0165346  466  GLN A C   
3463 O  O   . GLN A 430 ? 0.275388 0.27978  0.279132 -0.0241957  -0.00019662 -0.0211294  466  GLN A O   
3464 C  CB  . GLN A 430 ? 0.246622 0.231275 0.235356 -0.0195525  0.00299329  -0.0112026  466  GLN A CB  
3465 C  CG  . GLN A 430 ? 0.249481 0.224305 0.230279 -0.0183549  0.00480702  -0.00775165 466  GLN A CG  
3466 C  CD  . GLN A 430 ? 0.341228 0.309336 0.318283 -0.021177   0.00840942  -0.00835331 466  GLN A CD  
3467 O  OE1 . GLN A 430 ? 0.334324 0.302919 0.313605 -0.0254631  0.0117935   -0.011309   466  GLN A OE1 
3468 N  NE2 . GLN A 430 ? 0.391896 0.354143 0.364286 -0.01891    0.00760232  -0.00625764 466  GLN A NE2 
3469 N  N   . TRP A 431 ? 0.249304 0.251568 0.249931 -0.0167037  -0.00686045 -0.0147607  467  TRP A N   
3470 C  CA  . TRP A 431 ? 0.258552 0.270165 0.26648  -0.0150738  -0.0108015  -0.0179183  467  TRP A CA  
3471 C  C   . TRP A 431 ? 0.228662 0.24601  0.2376   -0.0163919  -0.0134282  -0.0204458  467  TRP A C   
3472 O  O   . TRP A 431 ? 0.208762 0.235068 0.224947 -0.0175375  -0.0141331  -0.025675   467  TRP A O   
3473 C  CB  . TRP A 431 ? 0.258987 0.269361 0.266851 -0.0100409  -0.0158229  -0.0145931  467  TRP A CB  
3474 C  CG  . TRP A 431 ? 0.242595 0.261254 0.257854 -0.00667936 -0.0207902  -0.0175477  467  TRP A CG  
3475 C  CD1 . TRP A 431 ? 0.228573 0.25366  0.252243 -0.00504456 -0.0206446  -0.021944   467  TRP A CD1 
3476 C  CD2 . TRP A 431 ? 0.231309 0.252919 0.245751 -0.00389849 -0.0269984  -0.0164607  467  TRP A CD2 
3477 N  NE1 . TRP A 431 ? 0.287041 0.319301 0.316509 -0.00090189 -0.0267729  -0.0241092  467  TRP A NE1 
3478 C  CE2 . TRP A 431 ? 0.239533 0.269176 0.262651 1.668e-05   -0.0310789  -0.0203563  467  TRP A CE2 
3479 C  CE3 . TRP A 431 ? 0.220858 0.239348 0.227499 -0.00417408 -0.0293573  -0.0127424  467  TRP A CE3 
3480 C  CZ2 . TRP A 431 ? 0.272073 0.305913 0.295749 0.00428291  -0.0383137  -0.0201698  467  TRP A CZ2 
3481 C  CZ3 . TRP A 431 ? 0.243587 0.26619  0.249631 -0.00073626 -0.0358351  -0.0123657  467  TRP A CZ3 
3482 C  CH2 . TRP A 431 ? 0.25403  0.283741 0.268153 0.00369066  -0.0406203  -0.0157632  467  TRP A CH2 
3483 N  N   . ARG A 432 ? 0.232434 0.246167 0.234572 -0.0158323  -0.0154388  -0.0172521  468  ARG A N   
3484 C  CA  . ARG A 432 ? 0.232651 0.252468 0.234318 -0.0164661  -0.0186814  -0.0198225  468  ARG A CA  
3485 C  C   . ARG A 432 ? 0.253402 0.2753   0.257515 -0.0215912  -0.0145843  -0.0253989  468  ARG A C   
3486 O  O   . ARG A 432 ? 0.248855 0.279638 0.257456 -0.0227711  -0.0170421  -0.0305729  468  ARG A O   
3487 C  CB  . ARG A 432 ? 0.252705 0.268685 0.245455 -0.0151975  -0.0209149  -0.0154759  468  ARG A CB  
3488 C  CG  . ARG A 432 ? 0.287798 0.302931 0.276975 -0.0109581  -0.0263146  -0.0104993  468  ARG A CG  
3489 C  CD  . ARG A 432 ? 0.263842 0.276903 0.243206 -0.0110645  -0.0277426  -0.0069671  468  ARG A CD  
3490 N  NE  . ARG A 432 ? 0.242918 0.249019 0.217847 -0.0127992  -0.0231738  -0.00381856 468  ARG A NE  
3491 C  CZ  . ARG A 432 ? 0.2584   0.260808 0.226353 -0.012589   -0.0233617  0.00107979  468  ARG A CZ  
3492 N  NH1 . ARG A 432 ? 0.292003 0.295675 0.254041 -0.0111025  -0.0276515  0.00390001  468  ARG A NH1 
3493 N  NH2 . ARG A 432 ? 0.238464 0.236442 0.20502  -0.0139019  -0.0193841  0.00296967  468  ARG A NH2 
3494 N  N   . TRP A 433 ? 0.219789 0.233218 0.22115  -0.0245006  -0.00864781 -0.0246274  469  TRP A N   
3495 C  CA  . TRP A 433 ? 0.245507 0.258445 0.249163 -0.0298224  -0.00426942 -0.0297584  469  TRP A CA  
3496 C  C   . TRP A 433 ? 0.277958 0.299906 0.291511 -0.0327624  -0.00316704 -0.0354488  469  TRP A C   
3497 O  O   . TRP A 433 ? 0.275632 0.303788 0.29408  -0.0366399  -0.00291378 -0.0416447  469  TRP A O   
3498 C  CB  . TRP A 433 ? 0.238004 0.238651 0.236611 -0.0318965  0.00170944  -0.0275335  469  TRP A CB  
3499 C  CG  . TRP A 433 ? 0.284574 0.278167 0.27547  -0.0294385  0.00108998  -0.0239837  469  TRP A CG  
3500 C  CD1 . TRP A 433 ? 0.253191 0.250292 0.241015 -0.0274639  -0.00259781 -0.0235815  469  TRP A CD1 
3501 C  CD2 . TRP A 433 ? 0.310745 0.293059 0.296006 -0.0284307  0.00449164  -0.0204736  469  TRP A CD2 
3502 N  NE1 . TRP A 433 ? 0.278645 0.268639 0.260648 -0.0256359  -0.00122371 -0.02055    469  TRP A NE1 
3503 C  CE2 . TRP A 433 ? 0.322656 0.303654 0.303474 -0.0257749  0.00264832  -0.0188513  469  TRP A CE2 
3504 C  CE3 . TRP A 433 ? 0.281752 0.255362 0.264784 -0.0293166  0.00876473  -0.0186514  469  TRP A CE3 
3505 C  CZ2 . TRP A 433 ? 0.312608 0.28495  0.288706 -0.023463   0.004513    -0.0161916  469  TRP A CZ2 
3506 C  CZ3 . TRP A 433 ? 0.329183 0.292918 0.305776 -0.0265507  0.00994583  -0.0151528  469  TRP A CZ3 
3507 C  CH2 . TRP A 433 ? 0.3354   0.299285 0.309544 -0.023317   0.00750327  -0.0141914  469  TRP A CH2 
3508 N  N   . ARG A 434 ? 0.291538 0.316231 0.308885 -0.0303992  -0.00343767 -0.0341267  470  ARG A N   
3509 C  CA  . ARG A 434 ? 0.262406 0.297054 0.290299 -0.0331739  -0.00149082 -0.0401483  470  ARG A CA  
3510 C  C   . ARG A 434 ? 0.234102 0.282936 0.269939 -0.0298405  -0.00870426 -0.0444356  470  ARG A C   
3511 O  O   . ARG A 434 ? 0.224503 0.284998 0.270767 -0.0326805  -0.00830408 -0.0516973  470  ARG A O   
3512 C  CB  . ARG A 434 ? 0.264464 0.296172 0.292713 -0.0323045  0.00223791  -0.0379419  470  ARG A CB  
3513 C  CG  . ARG A 434 ? 0.322588 0.341549 0.343288 -0.0364712  0.00978304  -0.0350231  470  ARG A CG  
3514 C  CD  . ARG A 434 ? 0.361885 0.377139 0.380108 -0.0355595  0.0136509   -0.0325161  470  ARG A CD  
3515 N  NE  . ARG A 434 ? 0.413881 0.441906 0.442562 -0.0355732  0.014045    -0.0377711  470  ARG A NE  
3516 C  CZ  . ARG A 434 ? 0.404815 0.435486 0.434783 -0.030995   0.01238     -0.036979   470  ARG A CZ  
3517 N  NH1 . ARG A 434 ? 0.382306 0.404081 0.404069 -0.0265486  0.0100983   -0.0312207  470  ARG A NH1 
3518 N  NH2 . ARG A 434 ? 0.444072 0.487061 0.484511 -0.0308892  0.0130135   -0.0428208  470  ARG A NH2 
3519 N  N   . VAL A 435 ? 0.236679 0.284527 0.267464 -0.023813   -0.01541    -0.0400002  471  VAL A N   
3520 C  CA  . VAL A 435 ? 0.243966 0.303558 0.279855 -0.0199777  -0.0230938  -0.0433531  471  VAL A CA  
3521 C  C   . VAL A 435 ? 0.241268 0.305733 0.276869 -0.0237914  -0.0238902  -0.0482248  471  VAL A C   
3522 O  O   . VAL A 435 ? 0.219453 0.297074 0.264184 -0.0247554  -0.0267351  -0.0556562  471  VAL A O   
3523 C  CB  . VAL A 435 ? 0.252687 0.307597 0.280862 -0.0132505  -0.0296799  -0.0365711  471  VAL A CB  
3524 C  CG1 . VAL A 435 ? 0.285372 0.349891 0.314694 -0.00919584 -0.0380888  -0.0389154  471  VAL A CG1 
3525 C  CG2 . VAL A 435 ? 0.230284 0.280576 0.259627 -0.00914321 -0.0298859  -0.0327132  471  VAL A CG2 
3526 N  N   . PHE A 436 ? 0.214651 0.269257 0.240281 -0.0258064  -0.0215566  -0.0448301  472  PHE A N   
3527 C  CA  . PHE A 436 ? 0.241097 0.300422 0.265781 -0.0288317  -0.0229411  -0.0500769  472  PHE A CA  
3528 C  C   . PHE A 436 ? 0.225301 0.289878 0.259861 -0.036034   -0.017889   -0.0585902  472  PHE A C   
3529 O  O   . PHE A 436 ? 0.199015 0.274152 0.238992 -0.0383248  -0.0206916  -0.0661692  472  PHE A O   
3530 C  CB  . PHE A 436 ? 0.217114 0.265356 0.230104 -0.0296401  -0.0207029  -0.0459887  472  PHE A CB  
3531 C  CG  . PHE A 436 ? 0.238411 0.282739 0.241029 -0.0242546  -0.0251027  -0.0387184  472  PHE A CG  
3532 C  CD1 . PHE A 436 ? 0.246804 0.298645 0.247779 -0.0195678  -0.0327803  -0.0378632  472  PHE A CD1 
3533 C  CD2 . PHE A 436 ? 0.227301 0.260429 0.221639 -0.0240383  -0.0215131  -0.0329301  472  PHE A CD2 
3534 C  CE1 . PHE A 436 ? 0.270255 0.316837 0.260505 -0.0155808  -0.0359735  -0.0305463  472  PHE A CE1 
3535 C  CE2 . PHE A 436 ? 0.243461 0.27383  0.2288   -0.0206499  -0.0244336  -0.0271325  472  PHE A CE2 
3536 C  CZ  . PHE A 436 ? 0.2493   0.285406 0.232115 -0.016704   -0.0312913  -0.0252709  472  PHE A CZ  
3537 N  N   . ASP A 437 ? 0.252392 0.308804 0.28847  -0.0402754  -0.0100371  -0.0575162  473  ASP A N   
3538 C  CA  . ASP A 437 ? 0.271991 0.332133 0.316993 -0.0481479  -0.00434873 -0.065162   473  ASP A CA  
3539 C  C   . ASP A 437 ? 0.261049 0.336592 0.319832 -0.048722   -0.00523843 -0.0711233  473  ASP A C   
3540 O  O   . ASP A 437 ? 0.266228 0.346775 0.333935 -0.0558504  -9.727e-05  -0.0779397  473  ASP A O   
3541 C  CB  . ASP A 437 ? 0.315771 0.360904 0.356416 -0.0536438  0.00485943  -0.0625684  473  ASP A CB  
3542 C  CG  . ASP A 437 ? 0.332246 0.372919 0.372548 -0.0528293  0.0091869   -0.0578833  473  ASP A CG  
3543 O  OD1 . ASP A 437 ? 0.394447 0.445535 0.441287 -0.0494356  0.0063014   -0.0587623  473  ASP A OD1 
3544 O  OD2 . ASP A 437 ? 0.454264 0.480591 0.486854 -0.0547287  0.0149318   -0.0531919  473  ASP A OD2 
3545 N  N   . GLY A 438 ? 0.285822 0.368809 0.346967 -0.0414088  -0.0114637  -0.0690266  474  GLY A N   
3546 C  CA  . GLY A 438 ? 0.263    0.363573 0.338898 -0.0408782  -0.0139075  -0.0766258  474  GLY A CA  
3547 C  C   . GLY A 438 ? 0.323957 0.425289 0.40602  -0.0421107  -0.00778174 -0.0765754  474  GLY A C   
3548 O  O   . GLY A 438 ? 0.363857 0.480483 0.458699 -0.0401713  -0.0100362  -0.0826731  474  GLY A O   
3549 N  N   A SER A 439 ? 0.291879 0.377488 0.364597 -0.044728   -0.00057649 -0.0701176  475  SER A N   
3550 N  N   B SER A 439 ? 0.30203  0.387973 0.374995 -0.0444157  -0.00070755 -0.0700625  475  SER A N   
3551 C  CA  A SER A 439 ? 0.307191 0.390591 0.38132  -0.0454221  0.00543366  -0.0685063  475  SER A CA  
3552 C  CA  B SER A 439 ? 0.330926 0.417011 0.407343 -0.0455746  0.00536826  -0.069796   475  SER A CA  
3553 C  C   A SER A 439 ? 0.300709 0.390739 0.378512 -0.036757   -0.0005436  -0.0673034  475  SER A C   
3554 C  C   B SER A 439 ? 0.310326 0.39805  0.386453 -0.0366462  0.00014882  -0.0661162  475  SER A C   
3555 O  O   A SER A 439 ? 0.292572 0.392275 0.380046 -0.0370905  0.00222779  -0.0720071  475  SER A O   
3556 O  O   B SER A 439 ? 0.305226 0.396725 0.386217 -0.0364835  0.00390065  -0.0677533  475  SER A O   
3557 C  CB  A SER A 439 ? 0.290724 0.354841 0.351034 -0.047626   0.0117117   -0.060594   475  SER A CB  
3558 C  CB  B SER A 439 ? 0.356866 0.426363 0.423106 -0.0514949  0.0146637   -0.0648689  475  SER A CB  
3559 O  OG  A SER A 439 ? 0.266047 0.323388 0.324331 -0.0558768  0.0181325   -0.0624982  475  SER A OG  
3560 O  OG  B SER A 439 ? 0.31694  0.371127 0.369164 -0.0470957  0.0125063   -0.0560113  475  SER A OG  
3561 N  N   . ILE A 440 ? 0.311807 0.396122 0.381856 -0.0293729  -0.00819763 -0.061258   476  ILE A N   
3562 C  CA  . ILE A 440 ? 0.26438  0.352094 0.336768 -0.0207602  -0.0147833  -0.0595049  476  ILE A CA  
3563 C  C   . ILE A 440 ? 0.277186 0.377025 0.355856 -0.0159098  -0.0241637  -0.0634921  476  ILE A C   
3564 O  O   . ILE A 440 ? 0.297431 0.394243 0.369158 -0.0159186  -0.0279187  -0.0613735  476  ILE A O   
3565 C  CB  . ILE A 440 ? 0.249239 0.320868 0.3079   -0.0165852  -0.0166664  -0.0496476  476  ILE A CB  
3566 C  CG1 . ILE A 440 ? 0.218457 0.277975 0.269573 -0.0209657  -0.00818111 -0.0457169  476  ILE A CG1 
3567 C  CG2 . ILE A 440 ? 0.200541 0.272685 0.260617 -0.00788506 -0.0237075  -0.0472582  476  ILE A CG2 
3568 C  CD1 . ILE A 440 ? 0.187149 0.23241  0.226025 -0.0177401  -0.00973192 -0.0371839  476  ILE A CD1 
3569 N  N   . THR A 441 ? 0.332594 0.445966 0.42349  -0.0109073  -0.0285519  -0.0691405  477  THR A N   
3570 C  CA  . THR A 441 ? 0.285583 0.410496 0.381967 -0.00454157 -0.0388991  -0.0726759  477  THR A CA  
3571 C  C   . THR A 441 ? 0.287421 0.405926 0.379291 0.00567311  -0.0466178  -0.0666859  477  THR A C   
3572 O  O   . THR A 441 ? 0.25083  0.358644 0.338327 0.006814    -0.0431812  -0.061818   477  THR A O   
3573 C  CB  . THR A 441 ? 0.26476  0.411274 0.380057 -0.00593089 -0.0390031  -0.0847297  477  THR A CB  
3574 O  OG1 . THR A 441 ? 0.260763 0.412237 0.38466  -0.00038325 -0.0394174  -0.0868348  477  THR A OG1 
3575 C  CG2 . THR A 441 ? 0.229663 0.380625 0.350975 -0.0175037  -0.0284512  -0.0907217  477  THR A CG2 
3576 N  N   . LYS A 442 ? 0.262821 0.387744 0.355864 0.013125    -0.0571444  -0.067457   478  LYS A N   
3577 C  CA  . LYS A 442 ? 0.304442 0.420976 0.392091 0.0229454   -0.0649264  -0.0611614  478  LYS A CA  
3578 C  C   . LYS A 442 ? 0.322952 0.444477 0.422689 0.0277193   -0.0644225  -0.0654281  478  LYS A C   
3579 O  O   . LYS A 442 ? 0.389588 0.500777 0.485061 0.0345401   -0.0683877  -0.0601828  478  LYS A O   
3580 C  CB  . LYS A 442 ? 0.310302 0.431613 0.395488 0.031002    -0.0769543  -0.0606218  478  LYS A CB  
3581 C  CG  . LYS A 442 ? 0.324251 0.466971 0.426349 0.0365046   -0.0839373  -0.0713161  478  LYS A CG  
3582 C  CD  . LYS A 442 ? 0.314152 0.461046 0.411125 0.0447588   -0.0967099  -0.07025    478  LYS A CD  
3583 C  CE  . LYS A 442 ? 0.337908 0.503951 0.452316 0.0533492   -0.105029   -0.0798924  478  LYS A CE  
3584 N  NZ  . LYS A 442 ? 0.356254 0.531717 0.467499 0.0584707   -0.116073   -0.081916   478  LYS A NZ  
3585 N  N   . GLU A 443 ? 0.320198 0.457651 0.435219 0.0238045   -0.0592051  -0.0754318  479  GLU A N   
3586 C  CA  . GLU A 443 ? 0.290816 0.434116 0.41731  0.0269729   -0.0566226  -0.0805109  479  GLU A CA  
3587 C  C   . GLU A 443 ? 0.303429 0.430808 0.420445 0.0232043   -0.0484611  -0.0742999  479  GLU A C   
3588 O  O   . GLU A 443 ? 0.319531 0.444673 0.439972 0.0284241   -0.0489517  -0.0749355  479  GLU A O   
3589 C  CB  . GLU A 443 ? 0.298409 0.462048 0.44256  0.0216489   -0.0502228  -0.0925248  479  GLU A CB  
3590 C  CG  . GLU A 443 ? 0.369334 0.553826 0.527464 0.0243184   -0.0572673  -0.101857   479  GLU A CG  
3591 C  CD  . GLU A 443 ? 0.480515 0.68135  0.652375 0.0137478   -0.0471994  -0.112127   479  GLU A CD  
3592 O  OE1 . GLU A 443 ? 0.425008 0.618671 0.589881 0.00244367  -0.0375026  -0.109935   479  GLU A OE1 
3593 O  OE2 . GLU A 443 ? 0.421784 0.642901 0.612194 0.0171832   -0.0491737  -0.122787   479  GLU A OE2 
3594 N  N   . ASN A 444 ? 0.275423 0.391798 0.38074  0.0150509   -0.0416839  -0.0687488  480  ASN A N   
3595 C  CA  . ASN A 444 ? 0.256751 0.359875 0.354127 0.0129136   -0.0352664  -0.06375    480  ASN A CA  
3596 C  C   . ASN A 444 ? 0.260221 0.345149 0.340734 0.0108935   -0.0350293  -0.0534261  480  ASN A C   
3597 O  O   . ASN A 444 ? 0.238833 0.313694 0.311983 0.00715575  -0.028729   -0.0496615  480  ASN A O   
3598 C  CB  . ASN A 444 ? 0.305616 0.416535 0.410091 0.00642499  -0.0251994  -0.0700462  480  ASN A CB  
3599 C  CG  . ASN A 444 ? 0.381901 0.494958 0.484605 -0.00287736 -0.0193854  -0.0711924  480  ASN A CG  
3600 O  OD1 . ASN A 444 ? 0.41834  0.528043 0.51542  -0.00347272 -0.0235477  -0.0680707  480  ASN A OD1 
3601 N  ND2 . ASN A 444 ? 0.498314 0.616755 0.605537 -0.0102024  -0.00980245 -0.0759197  480  ASN A ND2 
3602 N  N   . TYR A 445 ? 0.227933 0.30857  0.301927 0.0142414   -0.0423619  -0.0487494  481  TYR A N   
3603 C  CA  . TYR A 445 ? 0.242472 0.306833 0.301695 0.0127969   -0.0418225  -0.0394689  481  TYR A CA  
3604 C  C   . TYR A 445 ? 0.24563  0.298556 0.300765 0.0139556   -0.0389468  -0.0354794  481  TYR A C   
3605 O  O   . TYR A 445 ? 0.235427 0.279566 0.282746 0.00927365  -0.0333046  -0.0316623  481  TYR A O   
3606 C  CB  . TYR A 445 ? 0.226396 0.287729 0.280589 0.0190574   -0.0512628  -0.0351985  481  TYR A CB  
3607 C  CG  . TYR A 445 ? 0.23694  0.305394 0.289013 0.0178419   -0.0549825  -0.0365613  481  TYR A CG  
3608 C  CD1 . TYR A 445 ? 0.236036 0.31001  0.288693 0.0103229   -0.0495721  -0.0402674  481  TYR A CD1 
3609 C  CD2 . TYR A 445 ? 0.260776 0.329197 0.30915  0.0247299   -0.0644966  -0.0339327  481  TYR A CD2 
3610 C  CE1 . TYR A 445 ? 0.243047 0.323349 0.293357 0.00940306  -0.0534622  -0.0421737  481  TYR A CE1 
3611 C  CE2 . TYR A 445 ? 0.273518 0.348344 0.318069 0.0241655   -0.0686444  -0.0350805  481  TYR A CE2 
3612 C  CZ  . TYR A 445 ? 0.257875 0.339341 0.30392  0.0164349   -0.0631533  -0.0397238  481  TYR A CZ  
3613 O  OH  . TYR A 445 ? 0.277885 0.365433 0.319494 0.0167075   -0.0682758  -0.0411888  481  TYR A OH  
3614 N  N   . ASN A 446 ? 0.226422 0.279126 0.286847 0.0209399   -0.0436839  -0.0366109  482  ASN A N   
3615 C  CA  . ASN A 446 ? 0.227314 0.267589 0.283036 0.023254    -0.0435141  -0.0324004  482  ASN A CA  
3616 C  C   . ASN A 446 ? 0.24802  0.289837 0.305995 0.019347    -0.0355046  -0.0360444  482  ASN A C   
3617 O  O   . ASN A 446 ? 0.255647 0.287044 0.305913 0.0172224   -0.0324184  -0.0319081  482  ASN A O   
3618 C  CB  . ASN A 446 ? 0.229795 0.267626 0.290015 0.0321754   -0.0515139  -0.0326012  482  ASN A CB  
3619 C  CG  . ASN A 446 ? 0.290887 0.311463 0.341823 0.0333722   -0.0530711  -0.0251394  482  ASN A CG  
3620 O  OD1 . ASN A 446 ? 0.29356  0.30533  0.333836 0.0304677   -0.0535145  -0.0179428  482  ASN A OD1 
3621 N  ND2 . ASN A 446 ? 0.241442 0.257498 0.296351 0.0365391   -0.0528274  -0.0273651  482  ASN A ND2 
3622 N  N   . GLN A 447 ? 0.227203 0.282745 0.29618  0.0189915   -0.0325601  -0.0442852  483  GLN A N   
3623 C  CA  . GLN A 447 ? 0.241335 0.299492 0.311938 0.015462    -0.0246243  -0.048245   483  GLN A CA  
3624 C  C   . GLN A 447 ? 0.238543 0.289956 0.298566 0.00776453  -0.0179227  -0.0438596  483  GLN A C   
3625 O  O   . GLN A 447 ? 0.227093 0.2717   0.280379 0.00556587  -0.0131084  -0.0420451  483  GLN A O   
3626 C  CB  . GLN A 447 ? 0.240622 0.31617  0.324853 0.0149036   -0.021454   -0.0580038  483  GLN A CB  
3627 C  CG  . GLN A 447 ? 0.285721 0.370186 0.382731 0.0234947   -0.0275736  -0.0643261  483  GLN A CG  
3628 C  CD  . GLN A 447 ? 0.3744   0.463935 0.476917 0.0292408   -0.0370839  -0.0645791  483  GLN A CD  
3629 O  OE1 . GLN A 447 ? 0.305192 0.390803 0.400972 0.027591    -0.0404849  -0.0593902  483  GLN A OE1 
3630 N  NE2 . GLN A 447 ? 0.350781 0.449877 0.46585  0.0369618   -0.0419831  -0.0713062  483  GLN A NE2 
3631 N  N   A GLU A 448 ? 0.265583 0.319137 0.324127 0.00405892  -0.0179978  -0.0426555  484  GLU A N   
3632 N  N   B GLU A 448 ? 0.255595 0.308677 0.313713 0.00399059  -0.017951   -0.0424054  484  GLU A N   
3633 C  CA  A GLU A 448 ? 0.265517 0.311961 0.314545 -0.00258799 -0.0122883  -0.0387842  484  GLU A CA  
3634 C  CA  B GLU A 448 ? 0.251341 0.297428 0.300062 -0.00269124 -0.0120011  -0.0386955  484  GLU A CA  
3635 C  C   A GLU A 448 ? 0.260526 0.292894 0.298055 -0.00157257 -0.0140478  -0.0309748  484  GLU A C   
3636 C  C   B GLU A 448 ? 0.252748 0.284917 0.290049 -0.00166916 -0.0139791  -0.0308594  484  GLU A C   
3637 O  O   A GLU A 448 ? 0.302793 0.327931 0.332578 -0.00482734 -0.00930501 -0.0281581  484  GLU A O   
3638 O  O   B GLU A 448 ? 0.278817 0.303683 0.308265 -0.00497996 -0.00929524 -0.0279478  484  GLU A O   
3639 C  CB  A GLU A 448 ? 0.274176 0.327325 0.326191 -0.00668847 -0.0119591  -0.0411527  484  GLU A CB  
3640 C  CB  B GLU A 448 ? 0.252654 0.305537 0.304411 -0.00736433 -0.010769   -0.0413318  484  GLU A CB  
3641 C  CG  A GLU A 448 ? 0.28249  0.351045 0.347362 -0.00905764 -0.00908865 -0.0499635  484  GLU A CG  
3642 C  CG  B GLU A 448 ? 0.260849 0.309016 0.306711 -0.0149822  -0.00257996 -0.0405876  484  GLU A CG  
3643 C  CD  A GLU A 448 ? 0.340302 0.410328 0.406145 -0.0133397  -0.00026761 -0.0529594  484  GLU A CD  
3644 C  CD  B GLU A 448 ? 0.252587 0.297457 0.295158 -0.0174755  0.0046954   -0.0409008  484  GLU A CD  
3645 O  OE1 A GLU A 448 ? 0.336993 0.40114  0.396237 -0.0199981  0.00627843  -0.0510969  484  GLU A OE1 
3646 O  OE1 B GLU A 448 ? 0.222239 0.277093 0.273367 -0.0172851  0.00711008  -0.0468014  484  GLU A OE1 
3647 O  OE2 A GLU A 448 ? 0.36057  0.436102 0.432234 -0.00993243 0.00022408  -0.056701   484  GLU A OE2 
3648 O  OE2 B GLU A 448 ? 0.233795 0.26654  0.265004 -0.0187903  0.00730051  -0.035343   484  GLU A OE2 
3649 N  N   . TRP A 449 ? 0.253563 0.282042 0.289777 0.00286588  -0.0208432  -0.0274538  485  TRP A N   
3650 C  CA  . TRP A 449 ? 0.244764 0.261366 0.272115 0.00354315  -0.0221822  -0.0209782  485  TRP A CA  
3651 C  C   . TRP A 449 ? 0.234578 0.246783 0.261005 0.00461443  -0.0198427  -0.0215311  485  TRP A C   
3652 O  O   . TRP A 449 ? 0.212662 0.218305 0.232031 0.00233361  -0.0170332  -0.0185064  485  TRP A O   
3653 C  CB  . TRP A 449 ? 0.215029 0.228247 0.241697 0.00791163  -0.029405   -0.0175024  485  TRP A CB  
3654 C  CG  . TRP A 449 ? 0.229315 0.231021 0.248496 0.00812576  -0.0306685  -0.0113426  485  TRP A CG  
3655 C  CD1 . TRP A 449 ? 0.217311 0.212281 0.237199 0.011427    -0.0334102  -0.00998855 485  TRP A CD1 
3656 C  CD2 . TRP A 449 ? 0.236631 0.232934 0.247519 0.00469462  -0.0293417  -0.00635078 485  TRP A CD2 
3657 N  NE1 . TRP A 449 ? 0.267228 0.253159 0.280007 0.00957222  -0.0337158  -0.00425933 485  TRP A NE1 
3658 C  CE2 . TRP A 449 ? 0.243002 0.230345 0.250411 0.00564601  -0.0311473  -0.00208532 485  TRP A CE2 
3659 C  CE3 . TRP A 449 ? 0.25093  0.249377 0.257701 0.0009123   -0.0267395  -0.00573778 485  TRP A CE3 
3660 C  CZ2 . TRP A 449 ? 0.268294 0.250364 0.268785 0.00268271  -0.0300188  0.00264342  485  TRP A CZ2 
3661 C  CZ3 . TRP A 449 ? 0.258091 0.250912 0.257629 -0.00113423 -0.0261069  -0.0011471  485  TRP A CZ3 
3662 C  CH2 . TRP A 449 ? 0.260406 0.245935 0.257131 -0.00031914 -0.0276106  0.00294801  485  TRP A CH2 
3663 N  N   . TRP A 450 ? 0.238877 0.255002 0.272532 0.00867119  -0.0216267  -0.0258255  486  TRP A N   
3664 C  CA  . TRP A 450 ? 0.270926 0.283849 0.303931 0.00996843  -0.0196752  -0.0276317  486  TRP A CA  
3665 C  C   . TRP A 450 ? 0.267958 0.282785 0.296699 0.00562697  -0.0123318  -0.0294177  486  TRP A C   
3666 O  O   . TRP A 450 ? 0.288602 0.29757  0.311027 0.00522327  -0.0106149  -0.0280205  486  TRP A O   
3667 C  CB  . TRP A 450 ? 0.240673 0.256548 0.282364 0.01584     -0.0234368  -0.0323805  486  TRP A CB  
3668 C  CG  . TRP A 450 ? 0.250246 0.256143 0.290033 0.0193398   -0.0299931  -0.0275252  486  TRP A CG  
3669 C  CD1 . TRP A 450 ? 0.261918 0.267159 0.30349  0.0223902   -0.0357707  -0.0250579  486  TRP A CD1 
3670 C  CD2 . TRP A 450 ? 0.238775 0.233352 0.272373 0.0186392   -0.0308081  -0.0233555  486  TRP A CD2 
3671 N  NE1 . TRP A 450 ? 0.272349 0.265359 0.308751 0.0236975   -0.0397156  -0.0192803  486  TRP A NE1 
3672 C  CE2 . TRP A 450 ? 0.25679  0.243585 0.288956 0.0208215   -0.0364454  -0.0183136  486  TRP A CE2 
3673 C  CE3 . TRP A 450 ? 0.257735 0.248275 0.286737 0.0163497   -0.0275632  -0.0235479  486  TRP A CE3 
3674 C  CZ2 . TRP A 450 ? 0.262229 0.237548 0.289733 0.0198732   -0.0379489  -0.013891   486  TRP A CZ2 
3675 C  CZ3 . TRP A 450 ? 0.265372 0.246091 0.290546 0.0157394   -0.0297694  -0.0196745  486  TRP A CZ3 
3676 C  CH2 . TRP A 450 ? 0.260481 0.233575 0.285627 0.0171525   -0.03454    -0.015173   486  TRP A CH2 
3677 N  N   A SER A 451 ? 0.253534 0.276022 0.285035 0.00211071  -0.00810547 -0.0322758  487  SER A N   
3678 N  N   B SER A 451 ? 0.266745 0.289472 0.298576 0.0022625   -0.00820136 -0.0324539  487  SER A N   
3679 N  N   C SER A 451 ? 0.263196 0.285692 0.294691 0.00208887  -0.00810166 -0.0322631  487  SER A N   
3680 C  CA  A SER A 451 ? 0.251267 0.273291 0.276823 -0.00267825 -0.00062656 -0.0327856  487  SER A CA  
3681 C  CA  B SER A 451 ? 0.27464  0.296692 0.300327 -0.00265122 -0.00078383 -0.0327279  487  SER A CA  
3682 C  CA  C SER A 451 ? 0.262548 0.284777 0.288259 -0.00276548 -0.00057749 -0.0328467  487  SER A CA  
3683 C  C   A SER A 451 ? 0.254912 0.26616  0.268864 -0.00499493 0.00047054  -0.0264223  487  SER A C   
3684 C  C   B SER A 451 ? 0.264162 0.275019 0.278235 -0.00434328 -0.00023492 -0.0263128  487  SER A C   
3685 C  C   C SER A 451 ? 0.256944 0.268232 0.270991 -0.00491484 0.00039471  -0.0264585  487  SER A C   
3686 O  O   A SER A 451 ? 0.250069 0.256906 0.256146 -0.00644923 0.00454579  -0.0254003  487  SER A O   
3687 O  O   B SER A 451 ? 0.256616 0.262816 0.263201 -0.00486375 0.00278011  -0.0253214  487  SER A O   
3688 O  O   C SER A 451 ? 0.255494 0.26238  0.261732 -0.00626193 0.00436471  -0.025464   487  SER A O   
3689 C  CB  A SER A 451 ? 0.23205  0.263483 0.263423 -0.00691644 0.00411312  -0.0371614  487  SER A CB  
3690 C  CB  B SER A 451 ? 0.277619 0.30737  0.307766 -0.00726787 0.00339816  -0.0357713  487  SER A CB  
3691 C  CB  C SER A 451 ? 0.262166 0.293358 0.293316 -0.00727361 0.00407469  -0.036823   487  SER A CB  
3692 O  OG  A SER A 451 ? 0.1984   0.240835 0.240852 -0.00393429 0.00348467  -0.0440431  487  SER A OG  
3693 O  OG  B SER A 451 ? 0.29827  0.328583 0.324273 -0.0113187  0.0111728   -0.0375991  487  SER A OG  
3694 O  OG  C SER A 451 ? 0.260664 0.289199 0.289381 -0.0104754  0.00356144  -0.033719   487  SER A OG  
3695 N  N   . LEU A 452 ? 0.235509 0.242906 0.248179 -0.00471981 -0.00348393 -0.0224153  488  LEU A N   
3696 C  CA  . LEU A 452 ? 0.258991 0.25793  0.262639 -0.00640183 -0.00271159 -0.0173567  488  LEU A CA  
3697 C  C   . LEU A 452 ? 0.239523 0.232808 0.240014 -0.00324036 -0.00619023 -0.0148472  488  LEU A C   
3698 O  O   . LEU A 452 ? 0.235579 0.223514 0.228897 -0.00364185 -0.00469484 -0.0126179  488  LEU A O   
3699 C  CB  . LEU A 452 ? 0.247922 0.246807 0.251966 -0.00795707 -0.0045824  -0.0153127  488  LEU A CB  
3700 C  CG  . LEU A 452 ? 0.292506 0.29616  0.299161 -0.012169   -0.00066291 -0.0183032  488  LEU A CG  
3701 C  CD1 . LEU A 452 ? 0.315403 0.319827 0.322521 -0.0131095  -0.00341316 -0.0172467  488  LEU A CD1 
3702 C  CD2 . LEU A 452 ? 0.295114 0.293298 0.294975 -0.0161416  0.00589457  -0.017609   488  LEU A CD2 
3703 N  N   . ARG A 453 ? 0.232355 0.226718 0.238485 -4.91e-05   -0.0109539  -0.0155437  489  ARG A N   
3704 C  CA  . ARG A 453 ? 0.246543 0.235654 0.251344 0.00220718  -0.0139314  -0.0142683  489  ARG A CA  
3705 C  C   . ARG A 453 ? 0.228534 0.217411 0.230043 0.00276087  -0.0112084  -0.0170918  489  ARG A C   
3706 O  O   . ARG A 453 ? 0.232613 0.217113 0.229392 0.00307804  -0.0120052  -0.0156424  489  ARG A O   
3707 C  CB  . ARG A 453 ? 0.255739 0.244003 0.26674  0.00533665  -0.019165   -0.0144241  489  ARG A CB  
3708 C  CG  . ARG A 453 ? 0.251996 0.238871 0.262681 0.00483713  -0.0221918  -0.0103123  489  ARG A CG  
3709 C  CD  . ARG A 453 ? 0.222882 0.202568 0.229254 0.00363628  -0.0238201  -0.00556021 489  ARG A CD  
3710 N  NE  . ARG A 453 ? 0.218111 0.192357 0.227598 0.00618818  -0.027761   -0.00520758 489  ARG A NE  
3711 C  CZ  . ARG A 453 ? 0.249155 0.216732 0.25668  0.00474312  -0.0287766  -0.00231687 489  ARG A CZ  
3712 N  NH1 . ARG A 453 ? 0.264609 0.225354 0.274247 0.00640434  -0.032314   -0.00099489 489  ARG A NH1 
3713 N  NH2 . ARG A 453 ? 0.233953 0.201454 0.237701 0.00157472  -0.0263448  -0.0006612  489  ARG A NH2 
3714 N  N   . LEU A 454 ? 0.205206 0.199767 0.209463 0.00294665  -0.008177   -0.0215947  490  LEU A N   
3715 C  CA  . LEU A 454 ? 0.245827 0.240931 0.24571  0.00340896  -0.00509093 -0.0246541  490  LEU A CA  
3716 C  C   . LEU A 454 ? 0.281403 0.272631 0.270505 0.00055029  -0.00086069 -0.0213747  490  LEU A C   
3717 O  O   . LEU A 454 ? 0.319455 0.306425 0.301102 0.0015741   -0.00133128 -0.0201279  490  LEU A O   
3718 C  CB  . LEU A 454 ? 0.246023 0.249474 0.252017 0.0038342   -0.00200547 -0.0306754  490  LEU A CB  
3719 C  CG  . LEU A 454 ? 0.29587  0.30082  0.295651 0.00364921  0.00253418  -0.034126   490  LEU A CG  
3720 C  CD1 . LEU A 454 ? 0.270135 0.270821 0.26744  0.00697672  -0.00137195 -0.0351957  490  LEU A CD1 
3721 C  CD2 . LEU A 454 ? 0.280065 0.295254 0.287183 0.00379561  0.00647423  -0.0411695  490  LEU A CD2 
3722 N  N   . LYS A 455 ? 0.27061  0.262717 0.258868 -0.00282918 0.00278427  -0.0199854  491  LYS A N   
3723 C  CA  . LYS A 455 ? 0.319769 0.306422 0.297418 -0.00544597 0.00732127  -0.0169626  491  LYS A CA  
3724 C  C   . LYS A 455 ? 0.310449 0.289562 0.281433 -0.00388203 0.00417035  -0.0122661  491  LYS A C   
3725 O  O   . LYS A 455 ? 0.269253 0.243564 0.230644 -0.00276123 0.00506699  -0.0106444  491  LYS A O   
3726 C  CB  . LYS A 455 ? 0.345706 0.333922 0.324876 -0.0100703  0.0120783   -0.0170281  491  LYS A CB  
3727 C  CG  . LYS A 455 ? 0.35807  0.337325 0.326115 -0.0128833  0.0162773   -0.012853   491  LYS A CG  
3728 C  CD  . LYS A 455 ? 0.474012 0.454442 0.445898 -0.0180523  0.0202526   -0.0135899  491  LYS A CD  
3729 C  CE  . LYS A 455 ? 0.604959 0.574652 0.564591 -0.0212304  0.0258778   -0.00987639 491  LYS A CE  
3730 N  NZ  . LYS A 455 ? 0.558716 0.526927 0.520173 -0.027398   0.0311532   -0.0106727  491  LYS A NZ  
3731 N  N   . TYR A 456 ? 0.239921 0.218736 0.215833 -0.00350811 0.00038607  -0.0104211  492  TYR A N   
3732 C  CA  . TYR A 456 ? 0.288565 0.262331 0.260091 -0.00233447 -0.00198292 -0.00693284 492  TYR A CA  
3733 C  C   . TYR A 456 ? 0.295817 0.270043 0.269107 0.00055921  -0.00652873 -0.00763447 492  TYR A C   
3734 O  O   . TYR A 456 ? 0.294367 0.265799 0.262105 0.00230038  -0.00770194 -0.00649802 492  TYR A O   
3735 C  CB  . TYR A 456 ? 0.298036 0.272014 0.27342  -0.00403857 -0.00286965 -0.00510723 492  TYR A CB  
3736 C  CG  . TYR A 456 ? 0.369848 0.341723 0.342185 -0.00717093 0.00166519  -0.00470947 492  TYR A CG  
3737 C  CD1 . TYR A 456 ? 0.386213 0.351242 0.349307 -0.00747051 0.00500907  -0.00288171 492  TYR A CD1 
3738 C  CD2 . TYR A 456 ? 0.373625 0.349992 0.35206  -0.00985891 0.00253139  -0.00646099 492  TYR A CD2 
3739 C  CE1 . TYR A 456 ? 0.45538  0.416538 0.415601 -0.0110741  0.0096341   -0.00243783 492  TYR A CE1 
3740 C  CE2 . TYR A 456 ? 0.380224 0.354809 0.356931 -0.0136296  0.00699909  -0.0070409  492  TYR A CE2 
3741 C  CZ  . TYR A 456 ? 0.449934 0.416347 0.417677 -0.0145768  0.0108951   -0.00496626 492  TYR A CZ  
3742 O  OH  . TYR A 456 ? 0.655345 0.618753 0.621852 -0.0190044  0.0156019   -0.00560977 492  TYR A OH  
3743 N  N   . GLN A 457 ? 0.244725 0.221921 0.226006 0.00108738  -0.0094836  -0.00938295 493  GLN A N   
3744 C  CA  . GLN A 457 ? 0.239013 0.215441 0.222634 0.00269967  -0.013425   -0.010125   493  GLN A CA  
3745 C  C   . GLN A 457 ? 0.243425 0.221073 0.226648 0.00470015  -0.0139346  -0.0144456  493  GLN A C   
3746 O  O   . GLN A 457 ? 0.27044  0.247511 0.254489 0.005822    -0.0168387  -0.0160294  493  GLN A O   
3747 C  CB  . GLN A 457 ? 0.223626 0.199696 0.214315 0.00202773  -0.0164468  -0.00903154 493  GLN A CB  
3748 C  CG  . GLN A 457 ? 0.225545 0.200863 0.215734 8.888e-05   -0.016369   -0.00515804 493  GLN A CG  
3749 C  CD  . GLN A 457 ? 0.256444 0.230504 0.2514   -0.00067888 -0.0189706  -0.0035403  493  GLN A CD  
3750 O  OE1 . GLN A 457 ? 0.277511 0.252289 0.274784 -0.00031062 -0.0196468  -0.00328921 493  GLN A OE1 
3751 N  NE2 . GLN A 457 ? 0.228072 0.200171 0.224578 -0.00163511 -0.0206336  -0.00273157 493  GLN A NE2 
3752 N  N   . GLY A 458 ? 0.230787 0.211029 0.213657 0.00491748  -0.0110459  -0.0172274  494  GLY A N   
3753 C  CA  . GLY A 458 ? 0.235727 0.217721 0.218668 0.00704014  -0.0116592  -0.0222102  494  GLY A CA  
3754 C  C   . GLY A 458 ? 0.270967 0.252781 0.263585 0.00845436  -0.0155729  -0.024979   494  GLY A C   
3755 O  O   . GLY A 458 ? 0.264273 0.245294 0.258161 0.0100743   -0.0180073  -0.0288047  494  GLY A O   
3756 N  N   . LEU A 459 ? 0.222763 0.204573 0.221883 0.00805875  -0.0165609  -0.0232541  495  LEU A N   
3757 C  CA  . LEU A 459 ? 0.256385 0.235486 0.263196 0.00992484  -0.0206094  -0.0249525  495  LEU A CA  
3758 C  C   . LEU A 459 ? 0.240283 0.223528 0.253408 0.0124446   -0.0202738  -0.0288769  495  LEU A C   
3759 O  O   . LEU A 459 ? 0.314852 0.303628 0.327935 0.0116      -0.0171518  -0.0290622  495  LEU A O   
3760 C  CB  . LEU A 459 ? 0.259062 0.233518 0.267716 0.00839068  -0.0233107  -0.0195783  495  LEU A CB  
3761 C  CG  . LEU A 459 ? 0.302034 0.274071 0.306642 0.00574768  -0.0234832  -0.0161415  495  LEU A CG  
3762 C  CD1 . LEU A 459 ? 0.278671 0.247427 0.284485 0.00374736  -0.0248625  -0.0108414  495  LEU A CD1 
3763 C  CD2 . LEU A 459 ? 0.3128   0.282669 0.318857 0.00610864  -0.0255241  -0.0195844  495  LEU A CD2 
3764 N  N   . CYS A 460 ? 0.270244 0.250599 0.289798 0.0155194   -0.0237647  -0.0321338  496  CYS A N   
3765 C  CA  . CYS A 460 ? 0.2864   0.270616 0.313716 0.0191275   -0.0247609  -0.0359257  496  CYS A CA  
3766 C  C   . CYS A 460 ? 0.301454 0.277545 0.333623 0.021529    -0.0304383  -0.0331858  496  CYS A C   
3767 O  O   . CYS A 460 ? 0.290958 0.258013 0.321855 0.0205374   -0.0329501  -0.0309321  496  CYS A O   
3768 C  CB  . CYS A 460 ? 0.262378 0.25174  0.292587 0.0219093   -0.0228064  -0.0442663  496  CYS A CB  
3769 S  SG  . CYS A 460 ? 0.399824 0.381981 0.429262 0.0231772   -0.0254617  -0.0482743  496  CYS A SG  
3770 N  N   . PRO A 461 ? 0.280109 0.259332 0.318548 0.0251849   -0.0326628  -0.0343529  497  PRO A N   
3771 C  CA  . PRO A 461 ? 0.280896 0.251373 0.322851 0.0287681   -0.0386216  -0.0315559  497  PRO A CA  
3772 C  C   . PRO A 461 ? 0.336355 0.300539 0.383409 0.0327557   -0.0410979  -0.0369588  497  PRO A C   
3773 O  O   . PRO A 461 ? 0.330897 0.302721 0.383082 0.0357254   -0.039357   -0.044727   497  PRO A O   
3774 C  CB  . PRO A 461 ? 0.248412 0.227759 0.296009 0.0323487   -0.0401669  -0.0330522  497  PRO A CB  
3775 C  CG  . PRO A 461 ? 0.227686 0.22127  0.278002 0.030921    -0.0342973  -0.0394321  497  PRO A CG  
3776 C  CD  . PRO A 461 ? 0.259664 0.251283 0.302161 0.0260519   -0.029549   -0.0386974  497  PRO A CD  
3777 N  N   . PRO A 462 ? 0.289025 0.239473 0.334981 0.0325378   -0.0446045  -0.0336752  498  PRO A N   
3778 C  CA  . PRO A 462 ? 0.302582 0.24554  0.353911 0.0362304   -0.0471261  -0.039399   498  PRO A CA  
3779 C  C   . PRO A 462 ? 0.33173  0.275712 0.391214 0.0441832   -0.0510261  -0.0434967  498  PRO A C   
3780 O  O   . PRO A 462 ? 0.339137 0.282328 0.404739 0.0483768   -0.0518924  -0.0511739  498  PRO A O   
3781 C  CB  . PRO A 462 ? 0.31944  0.246779 0.367331 0.032981    -0.0496114  -0.0332909  498  PRO A CB  
3782 C  CG  . PRO A 462 ? 0.283376 0.209518 0.325474 0.0305185   -0.0501156  -0.0240463  498  PRO A CG  
3783 C  CD  . PRO A 462 ? 0.310762 0.251992 0.350345 0.0281155   -0.0456729  -0.0248247  498  PRO A CD  
3784 N  N   . VAL A 463 ? 0.289391 0.236326 0.349207 0.0465374   -0.053527   -0.0391319  499  VAL A N   
3785 C  CA  . VAL A 463 ? 0.304622 0.254199 0.372663 0.0547977   -0.0581739  -0.0428518  499  VAL A CA  
3786 C  C   . VAL A 463 ? 0.287172 0.25473  0.358691 0.0552356   -0.0560194  -0.0453164  499  VAL A C   
3787 O  O   . VAL A 463 ? 0.309103 0.280971 0.374403 0.0498044   -0.0534593  -0.0400109  499  VAL A O   
3788 C  CB  . VAL A 463 ? 0.377218 0.309989 0.441823 0.0578215   -0.0649067  -0.0348377  499  VAL A CB  
3789 C  CG1 . VAL A 463 ? 0.474877 0.41221  0.544615 0.0658946   -0.070744   -0.0351712  499  VAL A CG1 
3790 C  CG2 . VAL A 463 ? 0.369781 0.286465 0.436917 0.0605907   -0.0676434  -0.0372448  499  VAL A CG2 
3791 N  N   . PRO A 464 ? 0.295051 0.274491 0.377216 0.0609864   -0.0561785  -0.0543992  500  PRO A N   
3792 C  CA  . PRO A 464 ? 0.287918 0.285373 0.375354 0.0608517   -0.0538936  -0.0578195  500  PRO A CA  
3793 C  C   . PRO A 464 ? 0.302017 0.297211 0.386689 0.0622011   -0.0594302  -0.0504868  500  PRO A C   
3794 O  O   . PRO A 464 ? 0.314428 0.296965 0.397324 0.0672115   -0.0664174  -0.0457577  500  PRO A O   
3795 C  CB  . PRO A 464 ? 0.308127 0.315338 0.409615 0.0691698   -0.0556065  -0.0689677  500  PRO A CB  
3796 C  CG  . PRO A 464 ? 0.35737  0.354538 0.458739 0.0707789   -0.0550077  -0.0729997  500  PRO A CG  
3797 C  CD  . PRO A 464 ? 0.330999 0.308352 0.421214 0.0669763   -0.0574538  -0.0630844  500  PRO A CD  
3798 N  N   . ARG A 465 ? 0.272777 0.27816  0.354745 0.0568498   -0.0560358  -0.0485211  501  ARG A N   
3799 C  CA  . ARG A 465 ? 0.277657 0.283129 0.356703 0.0578632   -0.060995   -0.0428232  501  ARG A CA  
3800 C  C   . ARG A 465 ? 0.322719 0.34368  0.414612 0.064468    -0.0646731  -0.0504479  501  ARG A C   
3801 O  O   . ARG A 465 ? 0.34346  0.37811  0.445861 0.0653027   -0.0607451  -0.0598769  501  ARG A O   
3802 C  CB  . ARG A 465 ? 0.240587 0.251519 0.31255  0.0487984   -0.0547599  -0.0395374  501  ARG A CB  
3803 C  CG  . ARG A 465 ? 0.283261 0.284114 0.344939 0.0419477   -0.0496634  -0.0345283  501  ARG A CG  
3804 C  CD  . ARG A 465 ? 0.312578 0.295212 0.367731 0.0427385   -0.0528714  -0.0285361  501  ARG A CD  
3805 N  NE  . ARG A 465 ? 0.312244 0.286089 0.36019  0.04305     -0.0576962  -0.0200823  501  ARG A NE  
3806 C  CZ  . ARG A 465 ? 0.365538 0.327627 0.412556 0.0484275   -0.0641115  -0.0166336  501  ARG A CZ  
3807 N  NH1 . ARG A 465 ? 0.384446 0.340609 0.437949 0.0539797   -0.0667162  -0.0209944  501  ARG A NH1 
3808 N  NH2 . ARG A 465 ? 0.333438 0.288795 0.372076 0.0481535   -0.0677229  -0.00872687 501  ARG A NH2 
3809 N  N   . THR A 466 ? 0.361897 0.381812 0.453214 0.0694214   -0.0723601  -0.0468713  502  THR A N   
3810 C  CA  . THR A 466 ? 0.36854  0.404176 0.473412 0.0767823   -0.0770634  -0.0549142  502  THR A CA  
3811 C  C   . THR A 466 ? 0.390636 0.43478  0.492793 0.0748482   -0.079897   -0.0521108  502  THR A C   
3812 O  O   . THR A 466 ? 0.372698 0.407661 0.461764 0.0695607   -0.0794128  -0.0433711  502  THR A O   
3813 C  CB  . THR A 466 ? 0.397516 0.424395 0.507904 0.0884482   -0.0856401  -0.0565196  502  THR A CB  
3814 O  OG1 . THR A 466 ? 0.40453  0.409467 0.502157 0.0907478   -0.091677   -0.0456506  502  THR A OG1 
3815 C  CG2 . THR A 466 ? 0.403971 0.425691 0.519315 0.0899903   -0.0820158  -0.0620913  502  THR A CG2 
3816 N  N   . GLN A 467 ? 0.377484 0.440555 0.492665 0.078958    -0.082765   -0.0604084  503  GLN A N   
3817 C  CA  . GLN A 467 ? 0.440331 0.512001 0.553448 0.0776835   -0.0865241  -0.058775   503  GLN A CA  
3818 C  C   . GLN A 467 ? 0.384855 0.439738 0.484673 0.0831383   -0.0958982  -0.0482943  503  GLN A C   
3819 O  O   . GLN A 467 ? 0.367475 0.411471 0.467297 0.0923749   -0.103102   -0.0462868  503  GLN A O   
3820 C  CB  . GLN A 467 ? 0.528745 0.623384 0.660338 0.0837229   -0.0904046  -0.0704698  503  GLN A CB  
3821 C  CG  . GLN A 467 ? 0.638699 0.747095 0.771908 0.0826404   -0.0946087  -0.0720085  503  GLN A CG  
3822 C  CD  . GLN A 467 ? 0.753881 0.854264 0.879233 0.0919216   -0.107344   -0.0656065  503  GLN A CD  
3823 O  OE1 . GLN A 467 ? 0.790925 0.886562 0.920002 0.103438    -0.116032   -0.0659708  503  GLN A OE1 
3824 N  NE2 . GLN A 467 ? 0.848426 0.945595 0.961233 0.0871091   -0.108509   -0.0591678  503  GLN A NE2 
3825 N  N   . GLY A 468 ? 0.331814 0.384723 0.420197 0.0777716   -0.0959659  -0.0419684  504  GLY A N   
3826 C  CA  . GLY A 468 ? 0.369008 0.405456 0.442193 0.0814161   -0.103272   -0.0312741  504  GLY A CA  
3827 C  C   . GLY A 468 ? 0.373083 0.390791 0.431613 0.0734967   -0.0968284  -0.0218191  504  GLY A C   
3828 O  O   . GLY A 468 ? 0.421721 0.427986 0.465661 0.0718821   -0.0990516  -0.0126896  504  GLY A O   
3829 N  N   . ASP A 469 ? 0.336261 0.3519   0.398452 0.0682933   -0.0886411  -0.0243535  505  ASP A N   
3830 C  CA  . ASP A 469 ? 0.324427 0.326136 0.374236 0.0603455   -0.0826334  -0.0166884  505  ASP A CA  
3831 C  C   . ASP A 469 ? 0.305756 0.314773 0.34963  0.0520565   -0.0777001  -0.0152815  505  ASP A C   
3832 O  O   . ASP A 469 ? 0.304581 0.329574 0.356366 0.05005     -0.0754886  -0.0221205  505  ASP A O   
3833 C  CB  . ASP A 469 ? 0.346025 0.343991 0.400459 0.0576641   -0.0762779  -0.019985   505  ASP A CB  
3834 C  CG  . ASP A 469 ? 0.363279 0.34819  0.420084 0.064731    -0.0808318  -0.0195712  505  ASP A CG  
3835 O  OD1 . ASP A 469 ? 0.362063 0.335639 0.413459 0.0708776   -0.0886357  -0.0138225  505  ASP A OD1 
3836 O  OD2 . ASP A 469 ? 0.348768 0.334719 0.412534 0.0643148   -0.0766282  -0.0253668  505  ASP A OD2 
3837 N  N   . PHE A 470 ? 0.29818  0.29542  0.328684 0.0467806   -0.0753692  -0.00694025 506  PHE A N   
3838 C  CA  . PHE A 470 ? 0.269611 0.272329 0.294297 0.0392914   -0.070491   -0.00586527 506  PHE A CA  
3839 C  C   . PHE A 470 ? 0.286683 0.27594  0.301305 0.0335713   -0.0655437  0.00102232  506  PHE A C   
3840 O  O   . PHE A 470 ? 0.244327 0.225283 0.247347 0.031949    -0.0668687  0.00826673  506  PHE A O   
3841 C  CB  . PHE A 470 ? 0.277699 0.284297 0.295778 0.0412989   -0.0763847  -0.00339592 506  PHE A CB  
3842 C  CG  . PHE A 470 ? 0.291646 0.304616 0.304545 0.0338216   -0.0714657  -0.0037122  506  PHE A CG  
3843 C  CD1 . PHE A 470 ? 0.253152 0.277406 0.274382 0.0286957   -0.0652196  -0.0107604  506  PHE A CD1 
3844 C  CD2 . PHE A 470 ? 0.30438  0.31101  0.303343 0.0317377   -0.072666   0.00308177  506  PHE A CD2 
3845 C  CE1 . PHE A 470 ? 0.293852 0.321438 0.310111 0.0220292   -0.060629   -0.011017   506  PHE A CE1 
3846 C  CE2 . PHE A 470 ? 0.325258 0.336583 0.319784 0.0250762   -0.0676513  0.00222852  506  PHE A CE2 
3847 C  CZ  . PHE A 470 ? 0.304286 0.325839 0.307691 0.0204662   -0.061981   -0.00497414 506  PHE A CZ  
3848 N  N   . ASP A 471 ? 0.251027 0.238877 0.270392 0.0308944   -0.0600887  -0.00173606 507  ASP A N   
3849 C  CA  . ASP A 471 ? 0.275081 0.251885 0.287752 0.0260687   -0.055766   0.00309198  507  ASP A CA  
3850 C  C   . ASP A 471 ? 0.285212 0.262395 0.289153 0.0197259   -0.0518146  0.00693071  507  ASP A C   
3851 O  O   . ASP A 471 ? 0.317808 0.285369 0.314159 0.0166481   -0.0503617  0.0127149   507  ASP A O   
3852 C  CB  . ASP A 471 ? 0.249802 0.227001 0.26919  0.0251883   -0.0515584  -0.00169076 507  ASP A CB  
3853 C  CG  . ASP A 471 ? 0.269282 0.243931 0.296284 0.031903    -0.0558225  -0.00518749 507  ASP A CG  
3854 O  OD1 . ASP A 471 ? 0.316401 0.281809 0.341152 0.0367951   -0.0619749  -0.00130128 507  ASP A OD1 
3855 O  OD2 . ASP A 471 ? 0.285101 0.266528 0.319839 0.0325246   -0.052964   -0.0118827  507  ASP A OD2 
3856 N  N   . PRO A 472 ? 0.260903 0.249023 0.26623  0.0169868   -0.0491946  0.00327265  508  PRO A N   
3857 C  CA  . PRO A 472 ? 0.292378 0.280247 0.28976  0.0116914   -0.0456848  0.00621805  508  PRO A CA  
3858 C  C   . PRO A 472 ? 0.287453 0.268946 0.274623 0.0123688   -0.0494507  0.0128424   508  PRO A C   
3859 O  O   . PRO A 472 ? 0.308187 0.284742 0.288092 0.00818283  -0.0461249  0.0169253   508  PRO A O   
3860 C  CB  . PRO A 472 ? 0.267648 0.26771  0.269403 0.00971605  -0.043622   0.00025909  508  PRO A CB  
3861 C  CG  . PRO A 472 ? 0.255681 0.261827 0.268383 0.0116771   -0.0426197  -0.00598764 508  PRO A CG  
3862 C  CD  . PRO A 472 ? 0.251005 0.251851 0.266073 0.0179815   -0.0484347  -0.00440118 508  PRO A CD  
3863 N  N   . GLY A 473 ? 0.2674   0.249225 0.253894 0.0177794   -0.0562252  0.0137367   509  GLY A N   
3864 C  CA  . GLY A 473 ? 0.347656 0.322853 0.322032 0.0186765   -0.0600237  0.0206405   509  GLY A CA  
3865 C  C   . GLY A 473 ? 0.334677 0.294574 0.302244 0.0170444   -0.05873    0.0279791   509  GLY A C   
3866 O  O   . GLY A 473 ? 0.328413 0.280753 0.284061 0.0159114   -0.0598051  0.0348499   509  GLY A O   
3867 N  N   . ALA A 474 ? 0.288151 0.243755 0.263099 0.016552    -0.0562113  0.0261535   510  ALA A N   
3868 C  CA  . ALA A 474 ? 0.31666  0.258658 0.28722  0.0139611   -0.0544405  0.0316927   510  ALA A CA  
3869 C  C   . ALA A 474 ? 0.294649 0.23765  0.262701 0.00641507  -0.0471801  0.0324555   510  ALA A C   
3870 O  O   . ALA A 474 ? 0.334702 0.268935 0.300942 0.00295515  -0.0446636  0.03574     510  ALA A O   
3871 C  CB  . ALA A 474 ? 0.338999 0.27524  0.318277 0.0174926   -0.0561646  0.0289661   510  ALA A CB  
3872 N  N   . LYS A 475 ? 0.272097 0.2258   0.240595 0.00378679  -0.043786   0.0290147   511  LYS A N   
3873 C  CA  . LYS A 475 ? 0.287812 0.242611 0.253566 -0.00222449 -0.0377017  0.0297613   511  LYS A CA  
3874 C  C   . LYS A 475 ? 0.317033 0.274628 0.272734 -0.00440958 -0.0370045  0.0327458   511  LYS A C   
3875 O  O   . LYS A 475 ? 0.313852 0.279099 0.26881  -0.00238493 -0.0391514  0.0299335   511  LYS A O   
3876 C  CB  . LYS A 475 ? 0.262814 0.226072 0.236911 -0.00264155 -0.0345435  0.0230596   511  LYS A CB  
3877 C  CG  . LYS A 475 ? 0.243307 0.210712 0.216587 -0.00706914 -0.028928   0.0216211   511  LYS A CG  
3878 C  CD  . LYS A 475 ? 0.288498 0.250083 0.260598 -0.0105432  -0.026367   0.0247145   511  LYS A CD  
3879 C  CE  . LYS A 475 ? 0.279903 0.245886 0.250819 -0.0144521  -0.0214855  0.023852    511  LYS A CE  
3880 N  NZ  . LYS A 475 ? 0.315015 0.277395 0.28622  -0.0183273  -0.0189284  0.0260922   511  LYS A NZ  
3881 N  N   . PHE A 476 ? 0.30962  0.262883 0.258326 -0.00909446 -0.0333345  0.0371901   512  PHE A N   
3882 C  CA  . PHE A 476 ? 0.337594 0.292308 0.274496 -0.0111135  -0.0326542  0.0407197   512  PHE A CA  
3883 C  C   . PHE A 476 ? 0.30364  0.270002 0.240549 -0.0106     -0.0322558  0.0353623   512  PHE A C   
3884 O  O   . PHE A 476 ? 0.292113 0.261342 0.221808 -0.00861338 -0.035803   0.0360278   512  PHE A O   
3885 C  CB  . PHE A 476 ? 0.32887  0.280758 0.261394 -0.0175674  -0.0263407  0.0439367   512  PHE A CB  
3886 C  CG  . PHE A 476 ? 0.342927 0.298745 0.264015 -0.0205506  -0.0236791  0.0459692   512  PHE A CG  
3887 C  CD1 . PHE A 476 ? 0.331275 0.279175 0.238818 -0.0214133  -0.0250442  0.0534167   512  PHE A CD1 
3888 C  CD2 . PHE A 476 ? 0.342319 0.308926 0.265389 -0.0223132  -0.0197312  0.0404004   512  PHE A CD2 
3889 C  CE1 . PHE A 476 ? 0.350796 0.302817 0.246632 -0.0245619  -0.0218968  0.0550352   512  PHE A CE1 
3890 C  CE2 . PHE A 476 ? 0.310191 0.281099 0.222731 -0.0249803  -0.0169647  0.0412557   512  PHE A CE2 
3891 C  CZ  . PHE A 476 ? 0.327205 0.291565 0.226093 -0.0261023  -0.0180534  0.0483453   512  PHE A CZ  
3892 N  N   . HIS A 477 ? 0.275028 0.247651 0.219751 -0.0123376  -0.0281147  0.0297956   513  HIS A N   
3893 C  CA  . HIS A 477 ? 0.313156 0.294714 0.258242 -0.0129906  -0.0263707  0.0245021   513  HIS A CA  
3894 C  C   . HIS A 477 ? 0.32112  0.308088 0.26872  -0.00944053 -0.0311381  0.0207023   513  HIS A C   
3895 O  O   . HIS A 477 ? 0.294236 0.287851 0.239848 -0.0102761  -0.0306933  0.0168397   513  HIS A O   
3896 C  CB  . HIS A 477 ? 0.274513 0.258954 0.227146 -0.0147398  -0.0215318  0.0200033   513  HIS A CB  
3897 C  CG  . HIS A 477 ? 0.295119 0.277229 0.246746 -0.0180199  -0.0172408  0.0223121   513  HIS A CG  
3898 N  ND1 . HIS A 477 ? 0.345351 0.320987 0.298637 -0.0187237  -0.0176059  0.0260718   513  HIS A ND1 
3899 C  CD2 . HIS A 477 ? 0.331581 0.317593 0.281655 -0.0208339  -0.0125802  0.0207598   513  HIS A CD2 
3900 C  CE1 . HIS A 477 ? 0.391034 0.367486 0.344438 -0.0224658  -0.0130896  0.0266124   513  HIS A CE1 
3901 N  NE2 . HIS A 477 ? 0.355562 0.338917 0.307546 -0.0233806  -0.0100131  0.0231791   513  HIS A NE2 
3902 N  N   . ILE A 478 ? 0.282248 0.267381 0.235685 -0.00572725 -0.0352615  0.020583    514  ILE A N   
3903 C  CA  . ILE A 478 ? 0.255947 0.248053 0.213858 -0.00227716 -0.039893   0.0161808   514  ILE A CA  
3904 C  C   . ILE A 478 ? 0.290879 0.284222 0.23948  0.00018675  -0.0454758  0.0188365   514  ILE A C   
3905 O  O   . ILE A 478 ? 0.305447 0.306908 0.252378 -0.00045741 -0.0462759  0.0147004   514  ILE A O   
3906 C  CB  . ILE A 478 ? 0.280614 0.271415 0.248277 0.00119355  -0.0420934  0.0145624   514  ILE A CB  
3907 C  CG1 . ILE A 478 ? 0.251114 0.241876 0.225686 -0.00162949 -0.0361964  0.0114253   514  ILE A CG1 
3908 C  CG2 . ILE A 478 ? 0.238062 0.237253 0.212002 0.00541335  -0.0474656  0.00976664  514  ILE A CG2 
3909 C  CD1 . ILE A 478 ? 0.329653 0.32795  0.308033 -0.00408619 -0.0328791  0.00550392  514  ILE A CD1 
3910 N  N   . PRO A 479 ? 0.322175 0.307146 0.263231 0.00295537  -0.0495801  0.0256908   515  PRO A N   
3911 C  CA  . PRO A 479 ? 0.345525 0.33135  0.275409 0.0057343   -0.0552418  0.0286174   515  PRO A CA  
3912 C  C   . PRO A 479 ? 0.353944 0.341878 0.272322 0.00107859  -0.0512567  0.0298002   515  PRO A C   
3913 O  O   . PRO A 479 ? 0.334304 0.326793 0.24362  0.00250933  -0.0550176  0.0296331   515  PRO A O   
3914 C  CB  . PRO A 479 ? 0.365383 0.338257 0.289354 0.00977931  -0.0599393  0.0366723   515  PRO A CB  
3915 C  CG  . PRO A 479 ? 0.337805 0.301936 0.267411 0.00672024  -0.0547356  0.0387665   515  PRO A CG  
3916 C  CD  . PRO A 479 ? 0.292001 0.265767 0.23451  0.00421107  -0.0499447  0.0306501   515  PRO A CD  
3917 N  N   . SER A 480 ? 0.319695 0.304825 0.238191 -0.00423676 -0.0437623  0.0306715   516  SER A N   
3918 C  CA  . SER A 480 ? 0.357862 0.345751 0.266556 -0.00854532 -0.0392413  0.0310098   516  SER A CA  
3919 C  C   . SER A 480 ? 0.311846 0.310379 0.226461 -0.0101775  -0.0366986  0.0222427   516  SER A C   
3920 O  O   . SER A 480 ? 0.311722 0.313942 0.219022 -0.0129138  -0.0336347  0.0208433   516  SER A O   
3921 C  CB  . SER A 480 ? 0.378669 0.360025 0.285022 -0.0134371  -0.0323816  0.0354062   516  SER A CB  
3922 O  OG  . SER A 480 ? 0.437858 0.409198 0.332983 -0.01341    -0.0341568  0.0440738   516  SER A OG  
3923 N  N   . SER A 481 ? 0.28767  0.290196 0.215183 -0.00897966 -0.0371791  0.0163922   517  SER A N   
3924 C  CA  . SER A 481 ? 0.327299 0.337926 0.259764 -0.010782   -0.0350503  0.00838817  517  SER A CA  
3925 C  C   . SER A 481 ? 0.309431 0.318864 0.240602 -0.0148082  -0.0277761  0.00736803  517  SER A C   
3926 O  O   . SER A 481 ? 0.267237 0.281378 0.194718 -0.0166809  -0.0256741  0.00313122  517  SER A O   
3927 C  CB  . SER A 481 ? 0.283034 0.301012 0.208593 -0.00944555 -0.0399322  0.0054841   517  SER A CB  
3928 O  OG  . SER A 481 ? 0.281097 0.306505 0.214301 -0.0112234  -0.0385653  -0.00325472 517  SER A OG  
3929 N  N   . VAL A 482 ? 0.304825 0.308319 0.239591 -0.0157151  -0.024322   0.0107749   518  VAL A N   
3930 C  CA  . VAL A 482 ? 0.294255 0.297636 0.230264 -0.0185264  -0.0180562  0.00913815  518  VAL A CA  
3931 C  C   . VAL A 482 ? 0.284926 0.287325 0.231606 -0.017955   -0.0163271  0.00528216  518  VAL A C   
3932 O  O   . VAL A 482 ? 0.297729 0.296466 0.249575 -0.0165193  -0.0177438  0.00746563  518  VAL A O   
3933 C  CB  . VAL A 482 ? 0.340419 0.339708 0.272606 -0.0205947  -0.0148324  0.0146363   518  VAL A CB  
3934 C  CG1 . VAL A 482 ? 0.33287  0.334314 0.269549 -0.0225147  -0.00894473 0.0112529   518  VAL A CG1 
3935 C  CG2 . VAL A 482 ? 0.384799 0.384177 0.303868 -0.0220462  -0.0153438  0.0189884   518  VAL A CG2 
3936 N  N   . PRO A 483 ? 0.244988 0.249763 0.194303 -0.0189427  -0.0133138  -0.00047144 519  PRO A N   
3937 C  CA  . PRO A 483 ? 0.264764 0.266681 0.222049 -0.0185113  -0.0113254  -0.00335619 519  PRO A CA  
3938 C  C   . PRO A 483 ? 0.277048 0.274622 0.237316 -0.0177768  -0.00938306 -5.673e-05  519  PRO A C   
3939 O  O   . PRO A 483 ? 0.26576  0.263687 0.223364 -0.01855    -0.00763816 0.00227276  519  PRO A O   
3940 C  CB  . PRO A 483 ? 0.223053 0.226268 0.179914 -0.0197934  -0.00812304 -0.00928496 519  PRO A CB  
3941 C  CG  . PRO A 483 ? 0.257866 0.267148 0.207652 -0.0208068  -0.0102077  -0.0109648  519  PRO A CG  
3942 C  CD  . PRO A 483 ? 0.255938 0.265268 0.199541 -0.0204181  -0.0117673  -0.00438279 519  PRO A CD  
3943 N  N   . TYR A 484 ? 0.250853 0.245165 0.216639 -0.0166208  -0.00938961 -0.00045418 520  TYR A N   
3944 C  CA  . TYR A 484 ? 0.258053 0.249106 0.22643  -0.0155933  -0.00871622 0.00231028  520  TYR A CA  
3945 C  C   . TYR A 484 ? 0.271911 0.260051 0.242838 -0.0144827  -0.00600146 5.595e-05   520  TYR A C   
3946 O  O   . TYR A 484 ? 0.269118 0.256149 0.241841 -0.013393   -0.00555921 0.00145323  520  TYR A O   
3947 C  CB  . TYR A 484 ? 0.266154 0.255041 0.238074 -0.0142269  -0.01138    0.00416788  520  TYR A CB  
3948 C  CG  . TYR A 484 ? 0.259282 0.245728 0.232147 -0.0139165  -0.0120452  0.0076885   520  TYR A CG  
3949 C  CD1 . TYR A 484 ? 0.233344 0.219321 0.20273  -0.0150826  -0.0134011  0.0113796   520  TYR A CD1 
3950 C  CD2 . TYR A 484 ? 0.232597 0.216838 0.20908  -0.0128056  -0.0111137  0.00715728  520  TYR A CD2 
3951 C  CE1 . TYR A 484 ? 0.250849 0.233975 0.221499 -0.0160102  -0.0131375  0.0141351   520  TYR A CE1 
3952 C  CE2 . TYR A 484 ? 0.214092 0.196888 0.192402 -0.0131312  -0.0117298  0.00923087  520  TYR A CE2 
3953 C  CZ  . TYR A 484 ? 0.251213 0.233194 0.227227 -0.0150464  -0.0125639  0.0125659   520  TYR A CZ  
3954 O  OH  . TYR A 484 ? 0.271645 0.251314 0.250069 -0.016282   -0.0126938  0.0142577   520  TYR A OH  
3955 N  N   . ILE A 485 ? 0.271612 0.257855 0.242676 -0.0146506  -0.00447752 -0.0033253  521  ILE A N   
3956 C  CA  . ILE A 485 ? 0.293819 0.274737 0.265646 -0.0128708  -0.00237751 -0.00426879 521  ILE A CA  
3957 C  C   . ILE A 485 ? 0.241705 0.223724 0.213196 -0.0112278  -0.00104545 -0.00499519 521  ILE A C   
3958 O  O   . ILE A 485 ? 0.228667 0.207648 0.201121 -0.0084815  -0.00064249 -0.00499908 521  ILE A O   
3959 C  CB  . ILE A 485 ? 0.275944 0.252408 0.247313 -0.0140572  -0.00047731 -0.00721697 521  ILE A CB  
3960 C  CG1 . ILE A 485 ? 0.336949 0.30541  0.307261 -0.012335   0.0012608   -0.00652112 521  ILE A CG1 
3961 C  CG2 . ILE A 485 ? 0.353099 0.330242 0.322797 -0.015116   0.00104949  -0.0110428  521  ILE A CG2 
3962 C  CD1 . ILE A 485 ? 0.275063 0.242454 0.246052 -0.0116462  0.00043905  -0.00399894 521  ILE A CD1 
3963 N  N   . ARG A 486 ? 0.265208 0.252514 0.23524  -0.0126334  -0.00040672 -0.00596612 522  ARG A N   
3964 C  CA  . ARG A 486 ? 0.258109 0.248885 0.229133 -0.0114374  0.00143146  -0.00748322 522  ARG A CA  
3965 C  C   . ARG A 486 ? 0.306344 0.298492 0.281224 -0.0100122  0.00062091  -0.00529181 522  ARG A C   
3966 O  O   . ARG A 486 ? 0.289151 0.283383 0.267163 -0.00747836 0.00151061  -0.00743552 522  ARG A O   
3967 C  CB  . ARG A 486 ? 0.261685 0.258788 0.22924  -0.0142609  0.00252216  -0.00801305 522  ARG A CB  
3968 C  CG  . ARG A 486 ? 0.257847 0.256704 0.223004 -0.0167423  0.00063126  -0.00330001 522  ARG A CG  
3969 C  CD  . ARG A 486 ? 0.267119 0.270417 0.225782 -0.0194266  0.00114553  -0.00259196 522  ARG A CD  
3970 N  NE  . ARG A 486 ? 0.245735 0.249727 0.201813 -0.0193021  0.00108702  -0.0070198  522  ARG A NE  
3971 C  CZ  . ARG A 486 ? 0.251408 0.259696 0.200888 -0.0210098  0.00115049  -0.00837161 522  ARG A CZ  
3972 N  NH1 . ARG A 486 ? 0.234915 0.246464 0.178585 -0.0229419  0.00194948  -0.00502213 522  ARG A NH1 
3973 N  NH2 . ARG A 486 ? 0.256111 0.265113 0.204591 -0.0210067  0.00089001  -0.0134945  522  ARG A NH2 
3974 N  N   . TYR A 487 ? 0.255975 0.247305 0.23133  -0.0113254  -0.00143912 -0.00172903 523  TYR A N   
3975 C  CA  . TYR A 487 ? 0.263763 0.25674  0.242996 -0.0110363  -0.00238224 -0.00016904 523  TYR A CA  
3976 C  C   . TYR A 487 ? 0.276596 0.265802 0.257673 -0.0072993  -0.00375229 -0.00107267 523  TYR A C   
3977 O  O   . TYR A 487 ? 0.299094 0.291144 0.283892 -0.0054838  -0.00432395 -0.00220391 523  TYR A O   
3978 C  CB  . TYR A 487 ? 0.253422 0.245594 0.232445 -0.013581   -0.00411915 0.0035401   523  TYR A CB  
3979 C  CG  . TYR A 487 ? 0.284358 0.279011 0.25947  -0.0170327  -0.00303039 0.0056109   523  TYR A CG  
3980 C  CD1 . TYR A 487 ? 0.268302 0.267939 0.244079 -0.0194804  -0.00019635 0.0054125   523  TYR A CD1 
3981 C  CD2 . TYR A 487 ? 0.263699 0.256396 0.234045 -0.0177251  -0.00474488 0.00741239  523  TYR A CD2 
3982 C  CE1 . TYR A 487 ? 0.315499 0.316994 0.285395 -0.0228188  0.00152734  0.00751683  523  TYR A CE1 
3983 C  CE2 . TYR A 487 ? 0.264726 0.259123 0.229289 -0.0202621  -0.00421549 0.00967513  523  TYR A CE2 
3984 C  CZ  . TYR A 487 ? 0.304497 0.302571 0.267965 -0.0230076  -0.00083853 0.0101589   523  TYR A CZ  
3985 O  OH  . TYR A 487 ? 0.386413 0.385597 0.342143 -0.0257824  0.00021553  0.0128142   523  TYR A OH  
3986 N  N   . PHE A 488 ? 0.26371  0.24702  0.241855 -0.00621117 -0.00406978 -0.00095019 524  PHE A N   
3987 C  CA  . PHE A 488 ? 0.255021 0.233344 0.232201 -0.00275519 -0.00491459 -0.00111276 524  PHE A CA  
3988 C  C   . PHE A 488 ? 0.302131 0.279115 0.278879 0.00086402  -0.00417324 -0.00341315 524  PHE A C   
3989 O  O   . PHE A 488 ? 0.258572 0.235643 0.23638  0.00474714  -0.00587593 -0.00396905 524  PHE A O   
3990 C  CB  . PHE A 488 ? 0.249151 0.22155  0.222757 -0.00383785 -0.00403455 -0.00049987 524  PHE A CB  
3991 C  CG  . PHE A 488 ? 0.268218 0.23357  0.238014 -0.00082998 -0.00386785 -2.421e-05  524  PHE A CG  
3992 C  CD1 . PHE A 488 ? 0.264658 0.229539 0.233826 0.00047406  -0.00549018 0.00120183  524  PHE A CD1 
3993 C  CD2 . PHE A 488 ? 0.256599 0.214862 0.22244  0.00071779  -0.00208191 -0.00074931 524  PHE A CD2 
3994 C  CE1 . PHE A 488 ? 0.249908 0.20814  0.213426 0.0032251   -0.00530342 0.00210852  524  PHE A CE1 
3995 C  CE2 . PHE A 488 ? 0.296839 0.246892 0.257078 0.00364574  -0.00201212 0.00077779  524  PHE A CE2 
3996 C  CZ  . PHE A 488 ? 0.248293 0.198582 0.206727 0.00487866  -0.00357014 0.00239707  524  PHE A CZ  
3997 N  N   . VAL A 489 ? 0.265795 0.242168 0.241332 -1.156e-05  -0.00205267 -0.00534405 525  VAL A N   
3998 C  CA  . VAL A 489 ? 0.278809 0.253636 0.254506 0.00361031  -0.00119383 -0.00833296 525  VAL A CA  
3999 C  C   . VAL A 489 ? 0.292612 0.276745 0.274092 0.00545038  -0.00188791 -0.0102428  525  VAL A C   
4000 O  O   . VAL A 489 ? 0.299304 0.282935 0.282532 0.0106409   -0.00357676 -0.0117348  525  VAL A O   
4001 C  CB  . VAL A 489 ? 0.274721 0.24836  0.248758 0.0017189   0.00135837  -0.0111829  525  VAL A CB  
4002 C  CG1 . VAL A 489 ? 0.263679 0.235444 0.238781 0.00638359  0.00209753  -0.0151029  525  VAL A CG1 
4003 C  CG2 . VAL A 489 ? 0.284409 0.250214 0.254369 -0.00113514 0.0023055   -0.0103002  525  VAL A CG2 
4004 N  N   . SER A 490 ? 0.24687  0.239266 0.230996 0.00126447  -0.00055226 -0.0102922  526  SER A N   
4005 C  CA  . SER A 490 ? 0.255527 0.257959 0.246058 0.00129634  -0.0001139  -0.0123467  526  SER A CA  
4006 C  C   . SER A 490 ? 0.263194 0.266958 0.257913 0.00463494  -0.00336471 -0.0123495  526  SER A C   
4007 O  O   . SER A 490 ? 0.276806 0.287067 0.277391 0.00811151  -0.00425618 -0.0158462  526  SER A O   
4008 C  CB  . SER A 490 ? 0.252258 0.259566 0.242762 -0.00476099 0.00147016  -0.0100249  526  SER A CB  
4009 O  OG  . SER A 490 ? 0.344391 0.361322 0.341532 -0.00580652 0.0028206   -0.0122458  526  SER A OG  
4010 N  N   . PHE A 491 ? 0.25456  0.253723 0.247009 0.00349203  -0.00542803 -0.00903332 527  PHE A N   
4011 C  CA  . PHE A 491 ? 0.292201 0.29371  0.288211 0.00584404  -0.00864218 -0.00955195 527  PHE A CA  
4012 C  C   . PHE A 491 ? 0.291474 0.289071 0.285361 0.0130145   -0.0113769  -0.0110007  527  PHE A C   
4013 O  O   . PHE A 491 ? 0.346184 0.349381 0.344633 0.0165411   -0.014366   -0.0134593  527  PHE A O   
4014 C  CB  . PHE A 491 ? 0.311274 0.309319 0.305593 0.00290758  -0.0100234  -0.00650593 527  PHE A CB  
4015 C  CG  . PHE A 491 ? 0.310475 0.313768 0.309582 -0.00250773 -0.00909583 -0.00590082 527  PHE A CG  
4016 C  CD1 . PHE A 491 ? 0.393966 0.400161 0.393068 -0.00680222 -0.0057944  -0.00504785 527  PHE A CD1 
4017 C  CD2 . PHE A 491 ? 0.352474 0.356823 0.355135 -0.00347489 -0.0114127  -0.00615853 527  PHE A CD2 
4018 C  CE1 . PHE A 491 ? 0.341138 0.349877 0.34279  -0.0121929  -0.00453289 -0.00341382 527  PHE A CE1 
4019 C  CE2 . PHE A 491 ? 0.324892 0.331569 0.331428 -0.00891786 -0.0102274  -0.00521541 527  PHE A CE2 
4020 C  CZ  . PHE A 491 ? 0.351285 0.35987  0.357172 -0.013238   -0.00668028 -0.0035558  527  PHE A CZ  
4021 N  N   . ILE A 492 ? 0.307257 0.294552 0.293743 0.0151562   -0.0106923  -0.00934171 528  ILE A N   
4022 C  CA  . ILE A 492 ? 0.292114 0.2728   0.274615 0.022236    -0.0129523  -0.00987997 528  ILE A CA  
4023 C  C   . ILE A 492 ? 0.323516 0.310678 0.312173 0.0265889   -0.0132646  -0.0144966  528  ILE A C   
4024 O  O   . ILE A 492 ? 0.322054 0.314092 0.314575 0.0324444   -0.0169211  -0.0170657  528  ILE A O   
4025 C  CB  . ILE A 492 ? 0.314817 0.281573 0.287917 0.0220187   -0.0110658  -0.00684394 528  ILE A CB  
4026 C  CG1 . ILE A 492 ? 0.36955  0.331404 0.337395 0.0180967   -0.0104954  -0.00309819 528  ILE A CG1 
4027 C  CG2 . ILE A 492 ? 0.336158 0.293072 0.303594 0.0293145   -0.0129567  -0.0066589  528  ILE A CG2 
4028 C  CD1 . ILE A 492 ? 0.363092 0.321054 0.325562 0.0220993   -0.0136215  -0.00128644 528  ILE A CD1 
4029 N  N   . ILE A 493 ? 0.301506 0.289972 0.291578 0.0239498   -0.00956436 -0.0163161  529  ILE A N   
4030 C  CA  . ILE A 493 ? 0.303684 0.296616 0.298676 0.0287149   -0.0092934  -0.021311   529  ILE A CA  
4031 C  C   . ILE A 493 ? 0.294928 0.304684 0.301013 0.0281853   -0.0094101  -0.0256287  529  ILE A C   
4032 O  O   . ILE A 493 ? 0.300299 0.316125 0.312472 0.0340008   -0.0106477  -0.0305611  529  ILE A O   
4033 C  CB  . ILE A 493 ? 0.303199 0.292576 0.295797 0.025959    -0.00512755 -0.0228294  529  ILE A CB  
4034 C  CG1 . ILE A 493 ? 0.235214 0.234634 0.230674 0.0183051   -0.00136321 -0.0234223  529  ILE A CG1 
4035 C  CG2 . ILE A 493 ? 0.250291 0.22359  0.233326 0.0254715   -0.00470394 -0.0191978  529  ILE A CG2 
4036 C  CD1 . ILE A 493 ? 0.266422 0.265141 0.259787 0.0163128   0.00236064  -0.0264783  529  ILE A CD1 
4037 N  N   . GLN A 494 ? 0.264461 0.281518 0.273721 0.0214609   -0.00820499 -0.0241061  530  GLN A N   
4038 C  CA  . GLN A 494 ? 0.275113 0.307657 0.295421 0.0200814   -0.00779672 -0.0284081  530  GLN A CA  
4039 C  C   . GLN A 494 ? 0.236802 0.274532 0.263008 0.0273831   -0.01316    -0.0318405  530  GLN A C   
4040 O  O   . GLN A 494 ? 0.233524 0.284859 0.270371 0.0290513   -0.0129927  -0.0377276  530  GLN A O   
4041 C  CB  . GLN A 494 ? 0.279946 0.318054 0.302797 0.0112845   -0.00525959 -0.0262599  530  GLN A CB  
4042 C  CG  . GLN A 494 ? 0.257224 0.290836 0.278244 0.00974723  -0.00858455 -0.0227851  530  GLN A CG  
4043 C  CD  . GLN A 494 ? 0.291088 0.325486 0.312195 0.00118284  -0.00565298 -0.0196812  530  GLN A CD  
4044 O  OE1 . GLN A 494 ? 0.337435 0.377465 0.364858 -0.00195464 -0.00635982 -0.0207474  530  GLN A OE1 
4045 N  NE2 . GLN A 494 ? 0.271005 0.299956 0.285394 -0.00271524 -0.00247595 -0.0161754  530  GLN A NE2 
4046 N  N   . PHE A 495 ? 0.226951 0.255558 0.246625 0.0311119   -0.0177969  -0.0285114  531  PHE A N   
4047 C  CA  . PHE A 495 ? 0.232896 0.266056 0.256185 0.0385246   -0.0238153  -0.0314596  531  PHE A CA  
4048 C  C   . PHE A 495 ? 0.266087 0.295759 0.288431 0.0481002   -0.0260786  -0.0340702  531  PHE A C   
4049 O  O   . PHE A 495 ? 0.242846 0.283036 0.27387  0.0547818   -0.0298806  -0.0397171  531  PHE A O   
4050 C  CB  . PHE A 495 ? 0.22862  0.251457 0.242244 0.0389553   -0.0271534  -0.0265055  531  PHE A CB  
4051 C  CG  . PHE A 495 ? 0.274163 0.303991 0.292807 0.0315957   -0.0264778  -0.0265619  531  PHE A CG  
4052 C  CD1 . PHE A 495 ? 0.28599  0.329011 0.314843 0.0322018   -0.0298206  -0.0316639  531  PHE A CD1 
4053 C  CD2 . PHE A 495 ? 0.254301 0.278001 0.268636 0.0239252   -0.0224594  -0.0221896  531  PHE A CD2 
4054 C  CE1 . PHE A 495 ? 0.27334  0.321324 0.307306 0.0247482   -0.0287191  -0.0320781  531  PHE A CE1 
4055 C  CE2 . PHE A 495 ? 0.291563 0.3199   0.310548 0.0175145   -0.021846   -0.0222029  531  PHE A CE2 
4056 C  CZ  . PHE A 495 ? 0.286556 0.326322 0.315253 0.0176279   -0.0247763  -0.0271036  531  PHE A CZ  
4057 N  N   . GLN A 496 ? 0.249326 0.264652 0.262218 0.0487801   -0.0236563  -0.0306987  532  GLN A N   
4058 C  CA  . GLN A 496 ? 0.279946 0.290608 0.292504 0.0575017   -0.025296   -0.03358    532  GLN A CA  
4059 C  C   . GLN A 496 ? 0.280795 0.307974 0.307071 0.0586897   -0.0232897  -0.041576   532  GLN A C   
4060 O  O   . GLN A 496 ? 0.324062 0.356299 0.356436 0.0679955   -0.0272852  -0.0466748  532  GLN A O   
4061 C  CB  . GLN A 496 ? 0.288876 0.282038 0.290865 0.0567434   -0.0220542  -0.0299906  532  GLN A CB  
4062 C  CG  . GLN A 496 ? 0.337563 0.312723 0.325476 0.0564465   -0.0231808  -0.0226605  532  GLN A CG  
4063 C  CD  . GLN A 496 ? 0.351358 0.310802 0.331007 0.0540056   -0.0190465  -0.0202297  532  GLN A CD  
4064 O  OE1 . GLN A 496 ? 0.330788 0.28726  0.307156 0.0458797   -0.0149381  -0.0176288  532  GLN A OE1 
4065 N  NE2 . GLN A 496 ? 0.341592 0.290718 0.318331 0.0612627   -0.0203749  -0.0215683  532  GLN A NE2 
4066 N  N   . PHE A 497 ? 0.259647 0.295378 0.290428 0.0497091   -0.0171245  -0.042848   533  PHE A N   
4067 C  CA  . PHE A 497 ? 0.283167 0.335179 0.325911 0.049265    -0.0137138  -0.0503195  533  PHE A CA  
4068 C  C   . PHE A 497 ? 0.276449 0.346916 0.332722 0.050579    -0.0163996  -0.0556149  533  PHE A C   
4069 O  O   . PHE A 497 ? 0.312167 0.395057 0.379344 0.0563569   -0.0173353  -0.063101   533  PHE A O   
4070 C  CB  . PHE A 497 ? 0.316745 0.372878 0.358632 0.0386145   -0.00637919 -0.0493636  533  PHE A CB  
4071 C  CG  . PHE A 497 ? 0.305212 0.347547 0.336141 0.0361687   -0.00317376 -0.0461423  533  PHE A CG  
4072 C  CD1 . PHE A 497 ? 0.301257 0.32801  0.324841 0.042743    -0.00572066 -0.0449732  533  PHE A CD1 
4073 C  CD2 . PHE A 497 ? 0.303532 0.348246 0.331181 0.0269468   0.00227668  -0.0442712  533  PHE A CD2 
4074 C  CE1 . PHE A 497 ? 0.318641 0.333539 0.333511 0.0396517   -0.00267477 -0.0429948  533  PHE A CE1 
4075 C  CE2 . PHE A 497 ? 0.290072 0.324136 0.30858  0.0247347   0.0046333   -0.0424198  533  PHE A CE2 
4076 C  CZ  . PHE A 497 ? 0.32589  0.345513 0.338757 0.0306817   0.00225675  -0.0421423  533  PHE A CZ  
4077 N  N   . HIS A 498 ? 0.284205 0.357273 0.340834 0.0450793   -0.0175758  -0.0525712  534  HIS A N   
4078 C  CA  . HIS A 498 ? 0.299314 0.388688 0.368525 0.045921    -0.0208614  -0.0577759  534  HIS A CA  
4079 C  C   . HIS A 498 ? 0.283715 0.374327 0.355555 0.0587863   -0.0290232  -0.0615416  534  HIS A C   
4080 O  O   . HIS A 498 ? 0.296596 0.404677 0.382731 0.063001    -0.0308417  -0.0697912  534  HIS A O   
4081 C  CB  . HIS A 498 ? 0.27627  0.361661 0.341446 0.0401      -0.0226388  -0.052919   534  HIS A CB  
4082 C  CG  . HIS A 498 ? 0.254384 0.356391 0.332778 0.038138    -0.0250418  -0.0584556  534  HIS A CG  
4083 N  ND1 . HIS A 498 ? 0.224834 0.344888 0.317695 0.0318453   -0.0203953  -0.0645953  534  HIS A ND1 
4084 C  CD2 . HIS A 498 ? 0.263396 0.366878 0.342615 0.04193     -0.0319436  -0.0593825  534  HIS A CD2 
4085 C  CE1 . HIS A 498 ? 0.234401 0.365748 0.337116 0.0308778   -0.0240856  -0.0689283  534  HIS A CE1 
4086 N  NE2 . HIS A 498 ? 0.261226 0.383542 0.356189 0.037736    -0.0316604  -0.0664207  534  HIS A NE2 
4087 N  N   . GLU A 499 ? 0.284364 0.35688  0.342506 0.0653047   -0.0338193  -0.0557932  535  GLU A N   
4088 C  CA  . GLU A 499 ? 0.298411 0.369809 0.35659  0.0786181   -0.042071   -0.0584655  535  GLU A CA  
4089 C  C   . GLU A 499 ? 0.317043 0.393284 0.382711 0.086219    -0.0416517  -0.0648075  535  GLU A C   
4090 O  O   . GLU A 499 ? 0.31188  0.400347 0.387975 0.0955524   -0.0473134  -0.0717397  535  GLU A O   
4091 C  CB  . GLU A 499 ? 0.304208 0.354931 0.344712 0.0832227   -0.0468596  -0.0503871  535  GLU A CB  
4092 C  CG  . GLU A 499 ? 0.38044  0.422064 0.414722 0.0974005   -0.0545973  -0.050334   535  GLU A CG  
4093 C  CD  . GLU A 499 ? 0.425982 0.441601 0.43942  0.0984655   -0.054794   -0.0405363  535  GLU A CD  
4094 O  OE1 . GLU A 499 ? 0.447123 0.447724 0.452753 0.0955043   -0.0495093  -0.0366358  535  GLU A OE1 
4095 O  OE2 . GLU A 499 ? 0.50999  0.520683 0.514396 0.100606    -0.059585   -0.0366737  535  GLU A OE2 
4096 N  N   . ALA A 500 ? 0.295431 0.36282  0.356427 0.0828882   -0.0353195  -0.0633413  536  ALA A N   
4097 C  CA  . ALA A 500 ? 0.29196  0.362645 0.359588 0.0908741   -0.0350487  -0.070044   536  ALA A CA  
4098 C  C   . ALA A 500 ? 0.286956 0.38436  0.374109 0.08877     -0.0319726  -0.0801836  536  ALA A C   
4099 O  O   . ALA A 500 ? 0.252091 0.359693 0.349851 0.0986265   -0.0356927  -0.0879252  536  ALA A O   
4100 C  CB  . ALA A 500 ? 0.343876 0.399973 0.402627 0.0877806   -0.0291957  -0.0674799  536  ALA A CB  
4101 N  N   . LEU A 501 ? 0.26951  0.378006 0.361314 0.07598     -0.0250528  -0.0801604  537  LEU A N   
4102 C  CA  . LEU A 501 ? 0.266469 0.399834 0.375902 0.0720433   -0.020438   -0.0893349  537  LEU A CA  
4103 C  C   . LEU A 501 ? 0.285414 0.437068 0.409541 0.0766396   -0.0265689  -0.0958141  537  LEU A C   
4104 O  O   . LEU A 501 ? 0.283105 0.455193 0.42388  0.0800544   -0.0257603  -0.105982   537  LEU A O   
4105 C  CB  . LEU A 501 ? 0.318623 0.455942 0.426568 0.0569525   -0.0116011  -0.086153   537  LEU A CB  
4106 C  CG  . LEU A 501 ? 0.353047 0.477056 0.448564 0.0519197   -0.005253   -0.08162    537  LEU A CG  
4107 C  CD1 . LEU A 501 ? 0.38671  0.520807 0.4843   0.0385606   0.0033751   -0.0810775  537  LEU A CD1 
4108 C  CD2 . LEU A 501 ? 0.332024 0.456093 0.429956 0.0603216   -0.00465307 -0.0879016  537  LEU A CD2 
4109 N  N   . CYS A 502 ? 0.289896 0.434517 0.407862 0.0772502   -0.0328074  -0.0906392  538  CYS A N   
4110 C  CA  . CYS A 502 ? 0.30375  0.46388  0.433443 0.0818346   -0.0401185  -0.0963178  538  CYS A CA  
4111 C  C   . CYS A 502 ? 0.363128 0.526397 0.497596 0.0982604   -0.048798   -0.102128   538  CYS A C   
4112 O  O   . CYS A 502 ? 0.367578 0.553603 0.520311 0.103154    -0.0522176  -0.112457   538  CYS A O   
4113 C  CB  . CYS A 502 ? 0.287223 0.436077 0.405884 0.078959    -0.044649   -0.0889472  538  CYS A CB  
4114 S  SG  . CYS A 502 ? 0.325108 0.476043 0.444063 0.0602923   -0.0356527  -0.0848909  538  CYS A SG  
4115 N  N   . GLN A 503 ? 0.345015 0.485256 0.463445 0.106748    -0.0521133  -0.0957683  539  GLN A N   
4116 C  CA  . GLN A 503 ? 0.375119 0.51408  0.496137 0.122767    -0.0593455  -0.100451   539  GLN A CA  
4117 C  C   . GLN A 503 ? 0.347683 0.503061 0.484826 0.124198    -0.0539005  -0.110684   539  GLN A C   
4118 O  O   . GLN A 503 ? 0.293697 0.467322 0.446855 0.133804    -0.0586901  -0.120769   539  GLN A O   
4119 C  CB  . GLN A 503 ? 0.421479 0.529831 0.520662 0.130101    -0.0632131  -0.0906438  539  GLN A CB  
4120 C  CG  . GLN A 503 ? 0.511863 0.61673  0.612446 0.14782     -0.0721375  -0.0946828  539  GLN A CG  
4121 C  CD  . GLN A 503 ? 0.684326 0.766033 0.773226 0.151669    -0.0691205  -0.09074    539  GLN A CD  
4122 O  OE1 . GLN A 503 ? 0.690882 0.779493 0.789336 0.151059    -0.0634203  -0.0973644  539  GLN A OE1 
4123 N  NE2 . GLN A 503 ? 0.770154 0.824268 0.837846 0.153512    -0.0715838  -0.0798793  539  GLN A NE2 
4124 N  N   . ALA A 504 ? 0.328509 0.479542 0.462254 0.114429    -0.0437707  -0.10894    540  ALA A N   
4125 C  CA  . ALA A 504 ? 0.34358  0.511006 0.491608 0.114999    -0.0378078  -0.11901    540  ALA A CA  
4126 C  C   . ALA A 504 ? 0.336215 0.536123 0.507594 0.113286    -0.03726    -0.130311   540  ALA A C   
4127 O  O   . ALA A 504 ? 0.33098  0.548458 0.518045 0.11926     -0.0359435  -0.141359   540  ALA A O   
4128 C  CB  . ALA A 504 ? 0.382075 0.543263 0.522624 0.102467    -0.0267053  -0.115471   540  ALA A CB  
4129 N  N   . ALA A 505 ? 0.318808 0.52711  0.493185 0.104192    -0.0373542  -0.128185   541  ALA A N   
4130 C  CA  . ALA A 505 ? 0.307988 0.546628 0.5044   0.0985176   -0.0345387  -0.138448   541  ALA A CA  
4131 C  C   . ALA A 505 ? 0.335737 0.589122 0.545074 0.109828    -0.0460135  -0.145662   541  ALA A C   
4132 O  O   . ALA A 505 ? 0.363348 0.642862 0.592236 0.105065    -0.0448086  -0.15479    541  ALA A O   
4133 C  CB  . ALA A 505 ? 0.25364  0.492931 0.446935 0.0810754   -0.0270993  -0.132877   541  ALA A CB  
4134 N  N   . GLY A 506 ? 0.334922 0.572082 0.533373 0.124531    -0.0571392  -0.141832   542  GLY A N   
4135 C  CA  . GLY A 506 ? 0.327634 0.576047 0.534455 0.136267    -0.069535   -0.147253   542  GLY A CA  
4136 C  C   . GLY A 506 ? 0.3561   0.603357 0.557686 0.130465    -0.0743342  -0.142573   542  GLY A C   
4137 O  O   . GLY A 506 ? 0.353256 0.614354 0.563962 0.138365    -0.0841647  -0.148698   542  GLY A O   
4138 N  N   . HIS A 507 ? 0.343696 0.574434 0.530314 0.117625    -0.0684116  -0.132162   543  HIS A N   
4139 C  CA  . HIS A 507 ? 0.337668 0.570386 0.522414 0.111427    -0.0720273  -0.129882   543  HIS A CA  
4140 C  C   . HIS A 507 ? 0.363121 0.581422 0.533412 0.125291    -0.0846583  -0.12528    543  HIS A C   
4141 O  O   . HIS A 507 ? 0.380829 0.575856 0.533343 0.132882    -0.0866298  -0.117295   543  HIS A O   
4142 C  CB  . HIS A 507 ? 0.349618 0.564862 0.519823 0.0964383   -0.0633958  -0.119201   543  HIS A CB  
4143 C  CG  . HIS A 507 ? 0.438704 0.647528 0.600702 0.0923046   -0.0680257  -0.114492   543  HIS A CG  
4144 N  ND1 . HIS A 507 ? 0.407769 0.636401 0.584975 0.0857403   -0.0693039  -0.121785   543  HIS A ND1 
4145 C  CD2 . HIS A 507 ? 0.479287 0.664756 0.620023 0.093564    -0.071359   -0.104066   543  HIS A CD2 
4146 C  CE1 . HIS A 507 ? 0.386954 0.604832 0.552696 0.0840848   -0.0739285  -0.116569   543  HIS A CE1 
4147 N  NE2 . HIS A 507 ? 0.473169 0.665251 0.616603 0.0885787   -0.0748961  -0.10568    543  HIS A NE2 
4148 N  N   . THR A 508 ? 0.405637 0.636033 0.581601 0.128092    -0.0931462  -0.129701   544  THR A N   
4149 C  CA  . THR A 508 ? 0.426911 0.640155 0.58428  0.140092    -0.104236   -0.123316   544  THR A CA  
4150 C  C   . THR A 508 ? 0.433696 0.646167 0.585201 0.132064    -0.1063     -0.12062    544  THR A C   
4151 O  O   . THR A 508 ? 0.390345 0.617344 0.555077 0.11868     -0.10031    -0.125159   544  THR A O   
4152 C  CB  . THR A 508 ? 0.469715 0.696754 0.63707  0.157838    -0.116011   -0.132123   544  THR A CB  
4153 O  OG1 . THR A 508 ? 0.483963 0.739255 0.670968 0.155711    -0.120753   -0.143311   544  THR A OG1 
4154 C  CG2 . THR A 508 ? 0.437427 0.676507 0.620954 0.162418    -0.112034   -0.139953   544  THR A CG2 
4155 N  N   . GLY A 509 ? 0.452726 0.64628  0.583055 0.139652    -0.113911   -0.11273    545  GLY A N   
4156 C  CA  . GLY A 509 ? 0.400684 0.590032 0.522192 0.13221     -0.115163   -0.109324   545  GLY A CA  
4157 C  C   . GLY A 509 ? 0.399555 0.567829 0.506572 0.119247    -0.104561   -0.0984907  545  GLY A C   
4158 O  O   . GLY A 509 ? 0.383223 0.53877  0.484916 0.116516    -0.0970011  -0.092908   545  GLY A O   
4159 N  N   . PRO A 510 ? 0.390332 0.556716 0.493007 0.110053    -0.103433   -0.0966053  546  PRO A N   
4160 C  CA  . PRO A 510 ? 0.349847 0.494745 0.436379 0.100565    -0.0955705  -0.0860021  546  PRO A CA  
4161 C  C   . PRO A 510 ? 0.348397 0.493284 0.442953 0.0896839   -0.0838983  -0.0846884  546  PRO A C   
4162 O  O   . PRO A 510 ? 0.299402 0.463    0.413185 0.0823218   -0.0796668  -0.0921915  546  PRO A O   
4163 C  CB  . PRO A 510 ? 0.316843 0.46742  0.404785 0.0932544   -0.097334   -0.0885061  546  PRO A CB  
4164 C  CG  . PRO A 510 ? 0.377508 0.546373 0.474296 0.102916    -0.108765   -0.098051   546  PRO A CG  
4165 C  CD  . PRO A 510 ? 0.352879 0.539405 0.4683   0.10819     -0.109497   -0.105975   546  PRO A CD  
4166 N  N   . LEU A 511 ? 0.320355 0.443916 0.399247 0.0879772   -0.0784076  -0.0750181  547  LEU A N   
4167 C  CA  . LEU A 511 ? 0.326446 0.447429 0.409063 0.0789602   -0.068112   -0.0728015  547  LEU A CA  
4168 C  C   . LEU A 511 ? 0.339228 0.468786 0.43163  0.0644311   -0.0612217  -0.0744405  547  LEU A C   
4169 O  O   . LEU A 511 ? 0.290852 0.42787  0.393039 0.0570264   -0.0536178  -0.0764865  547  LEU A O   
4170 C  CB  . LEU A 511 ? 0.351603 0.447261 0.413724 0.0792425   -0.0650036  -0.0620571  547  LEU A CB  
4171 C  CG  . LEU A 511 ? 0.333303 0.423511 0.395714 0.0711553   -0.0552766  -0.0589571  547  LEU A CG  
4172 C  CD1 . LEU A 511 ? 0.346715 0.449495 0.422197 0.0760447   -0.0541539  -0.0660093  547  LEU A CD1 
4173 C  CD2 . LEU A 511 ? 0.35045  0.416951 0.393344 0.0738838   -0.0545624  -0.0498489  547  LEU A CD2 
4174 N  N   . HIS A 512 ? 0.342236 0.469365 0.430814 0.0600569   -0.06349    -0.0732307  548  HIS A N   
4175 C  CA  . HIS A 512 ? 0.282975 0.412998 0.378013 0.0464458   -0.0569024  -0.0732214  548  HIS A CA  
4176 C  C   . HIS A 512 ? 0.254088 0.407252 0.370881 0.0412389   -0.0559278  -0.0833547  548  HIS A C   
4177 O  O   . HIS A 512 ? 0.286577 0.442324 0.409871 0.0295215   -0.0495542  -0.0835507  548  HIS A O   
4178 C  CB  . HIS A 512 ? 0.281021 0.400494 0.365828 0.0434256   -0.059201   -0.0694471  548  HIS A CB  
4179 C  CG  . HIS A 512 ? 0.352103 0.483605 0.44305  0.0475066   -0.0676354  -0.0769093  548  HIS A CG  
4180 N  ND1 . HIS A 512 ? 0.329052 0.458004 0.410206 0.0591686   -0.0766772  -0.0771563  548  HIS A ND1 
4181 C  CD2 . HIS A 512 ? 0.335856 0.482265 0.441904 0.0408091   -0.0682563  -0.0847845  548  HIS A CD2 
4182 C  CE1 . HIS A 512 ? 0.351278 0.494593 0.441518 0.0600675   -0.083119   -0.0854347  548  HIS A CE1 
4183 N  NE2 . HIS A 512 ? 0.347952 0.502434 0.454431 0.0486286   -0.0779897  -0.0906456  548  HIS A NE2 
4184 N  N   . LYS A 513 ? 0.239582 0.409396 0.367752 0.0496995   -0.062188   -0.091839   549  LYS A N   
4185 C  CA  . LYS A 513 ? 0.249383 0.443969 0.400463 0.0450325   -0.061026   -0.102849   549  LYS A CA  
4186 C  C   . LYS A 513 ? 0.257065 0.460748 0.417775 0.0438325   -0.0540455  -0.105465   549  LYS A C   
4187 O  O   . LYS A 513 ? 0.241299 0.46678  0.421738 0.0397967   -0.0514823  -0.114876   549  LYS A O   
4188 C  CB  . LYS A 513 ? 0.2522   0.46342  0.412731 0.055743    -0.0721173  -0.112303   549  LYS A CB  
4189 C  CG  . LYS A 513 ? 0.319118 0.525685 0.472739 0.0554694   -0.0785504  -0.112029   549  LYS A CG  
4190 C  CD  . LYS A 513 ? 0.44807  0.676821 0.616277 0.0616588   -0.0883742  -0.124025   549  LYS A CD  
4191 C  CE  . LYS A 513 ? 0.491506 0.721731 0.660021 0.0559927   -0.0919551  -0.127164   549  LYS A CE  
4192 N  NZ  . LYS A 513 ? 0.542449 0.7754   0.722177 0.0394277   -0.0821988  -0.128497   549  LYS A NZ  
4193 N  N   . CYS A 514 ? 0.297357 0.485257 0.444686 0.0470969   -0.0506553  -0.0979223  550  CYS A N   
4194 C  CA  . CYS A 514 ? 0.283306 0.479736 0.438584 0.0481554   -0.0451223  -0.10136    550  CYS A CA  
4195 C  C   . CYS A 514 ? 0.2559   0.456018 0.416442 0.0332296   -0.0336088  -0.100385   550  CYS A C   
4196 O  O   . CYS A 514 ? 0.237725 0.422445 0.386657 0.0248929   -0.0293229  -0.0920904  550  CYS A O   
4197 C  CB  . CYS A 514 ? 0.283777 0.461465 0.422957 0.0563998   -0.0453782  -0.0943355  550  CYS A CB  
4198 S  SG  . CYS A 514 ? 0.334539 0.518953 0.480398 0.0550352   -0.036405   -0.0975613  550  CYS A SG  
4199 N  N   . ASP A 515 ? 0.265835 0.486246 0.443234 0.0308466   -0.0287393  -0.108904   551  ASP A N   
4200 C  CA  . ASP A 515 ? 0.253502 0.477275 0.434011 0.0175902   -0.0169928  -0.107743   551  ASP A CA  
4201 C  C   . ASP A 515 ? 0.241273 0.475908 0.428399 0.0218299   -0.0125257  -0.113107   551  ASP A C   
4202 O  O   . ASP A 515 ? 0.218423 0.474687 0.423274 0.0268578   -0.0145827  -0.123978   551  ASP A O   
4203 C  CB  . ASP A 515 ? 0.227373 0.467351 0.423861 0.00594591  -0.0135461  -0.11375    551  ASP A CB  
4204 C  CG  . ASP A 515 ? 0.257317 0.503997 0.459061 -0.00809866 -0.00090621 -0.113851   551  ASP A CG  
4205 O  OD1 . ASP A 515 ? 0.298573 0.537148 0.490226 -0.00924147 0.00539227  -0.108833   551  ASP A OD1 
4206 O  OD2 . ASP A 515 ? 0.277128 0.537573 0.493044 -0.0180896  0.00277033  -0.119369   551  ASP A OD2 
4207 N  N   . ILE A 516 ? 0.233368 0.454318 0.407189 0.019548    -0.00633689 -0.106368   552  ILE A N   
4208 C  CA  . ILE A 516 ? 0.237263 0.466171 0.41534  0.0251623   -0.00288534 -0.111661   552  ILE A CA  
4209 C  C   . ILE A 516 ? 0.259674 0.507037 0.449683 0.013798    0.00845844  -0.117345   552  ILE A C   
4210 O  O   . ILE A 516 ? 0.252294 0.505694 0.44396  0.0158514   0.0137041   -0.121212   552  ILE A O   
4211 C  CB  . ILE A 516 ? 0.232473 0.438381 0.390693 0.0293234   -0.00237888 -0.103082   552  ILE A CB  
4212 C  CG1 . ILE A 516 ? 0.22845  0.422088 0.373833 0.016783    0.00569819  -0.0943033  552  ILE A CG1 
4213 C  CG2 . ILE A 516 ? 0.254249 0.442601 0.40103  0.0405415   -0.0127478  -0.0979826  552  ILE A CG2 
4214 C  CD1 . ILE A 516 ? 0.23078  0.407152 0.359904 0.0192122   0.00794431  -0.0883605  552  ILE A CD1 
4215 N  N   . TYR A 517 ? 0.241779 0.497845 0.439796 0.00137112  0.0128327   -0.118125   553  TYR A N   
4216 C  CA  . TYR A 517 ? 0.246989 0.517171 0.452828 -0.0111563  0.0250071   -0.121561   553  TYR A CA  
4217 C  C   . TYR A 517 ? 0.223469 0.51864  0.447395 -0.00527597 0.0273084   -0.134572   553  TYR A C   
4218 O  O   . TYR A 517 ? 0.20796  0.518449 0.447737 0.00291539  0.020107    -0.14361    553  TYR A O   
4219 C  CB  . TYR A 517 ? 0.251212 0.531446 0.468759 -0.0237707  0.0281074   -0.123793   553  TYR A CB  
4220 C  CG  . TYR A 517 ? 0.25491  0.548257 0.479104 -0.0380665  0.0417586   -0.126425   553  TYR A CG  
4221 C  CD1 . TYR A 517 ? 0.2481   0.525038 0.454578 -0.0482951  0.0501849   -0.115895   553  TYR A CD1 
4222 C  CD2 . TYR A 517 ? 0.252516 0.574836 0.500038 -0.0413331  0.0463948   -0.139406   553  TYR A CD2 
4223 C  CE1 . TYR A 517 ? 0.240516 0.527672 0.450227 -0.0616987  0.0630203   -0.117183   553  TYR A CE1 
4224 C  CE2 . TYR A 517 ? 0.299066 0.633176 0.551323 -0.0549815  0.0600821   -0.14157    553  TYR A CE2 
4225 C  CZ  . TYR A 517 ? 0.281685 0.597159 0.513875 -0.0654641  0.0685365   -0.129855   553  TYR A CZ  
4226 O  OH  . TYR A 517 ? 0.287391 0.61223  0.521402 -0.0796193  0.082199    -0.130613   553  TYR A OH  
4227 N  N   . GLN A 518 ? 0.205325 0.504597 0.426447 -0.0086253  0.0367034   -0.135828   554  GLN A N   
4228 C  CA  . GLN A 518 ? 0.234217 0.558117 0.472359 -0.00464923 0.0411198   -0.148667   554  GLN A CA  
4229 C  C   . GLN A 518 ? 0.245773 0.566938 0.48356  0.0133847   0.0329917   -0.153033   554  GLN A C   
4230 O  O   . GLN A 518 ? 0.226522 0.567771 0.479376 0.0190822   0.0351168   -0.164565   554  GLN A O   
4231 C  CB  . GLN A 518 ? 0.234693 0.588502 0.498927 -0.0100496  0.0438669   -0.160884   554  GLN A CB  
4232 C  CG  . GLN A 518 ? 0.259113 0.638876 0.538947 -0.0116246  0.0534984   -0.172954   554  GLN A CG  
4233 C  CD  . GLN A 518 ? 0.278253 0.688328 0.584203 -0.020057   0.058224    -0.184807   554  GLN A CD  
4234 O  OE1 . GLN A 518 ? 0.255033 0.664098 0.562903 -0.0328407  0.0608934   -0.181278   554  GLN A OE1 
4235 N  NE2 . GLN A 518 ? 0.221401 0.659059 0.548903 -0.0126429  0.0589212   -0.199757   554  GLN A NE2 
4236 N  N   . SER A 519 ? 0.231573 0.528073 0.452682 0.0223196   0.024129    -0.144306   555  SER A N   
4237 C  CA  . SER A 519 ? 0.241997 0.533457 0.462264 0.0391987   0.0161801   -0.147863   555  SER A CA  
4238 C  C   . SER A 519 ? 0.272634 0.555439 0.482136 0.0405512   0.0224171   -0.146975   555  SER A C   
4239 O  O   . SER A 519 ? 0.267549 0.528379 0.457076 0.036104    0.0246287   -0.136548   555  SER A O   
4240 C  CB  . SER A 519 ? 0.248875 0.518027 0.455956 0.0476444   0.00481469  -0.139358   555  SER A CB  
4241 O  OG  . SER A 519 ? 0.270369 0.528611 0.471731 0.0623227   -0.00103162 -0.140365   555  SER A OG  
4242 N  N   . LYS A 520 ? 0.270048 0.570853 0.493568 0.0476513   0.0246568   -0.158963   556  LYS A N   
4243 C  CA  . LYS A 520 ? 0.288516 0.584837 0.504142 0.0482765   0.0314975   -0.16052    556  LYS A CA  
4244 C  C   . LYS A 520 ? 0.295623 0.566685 0.496996 0.061288    0.0230629   -0.155622   556  LYS A C   
4245 O  O   . LYS A 520 ? 0.288024 0.543201 0.473989 0.0593485   0.0269197   -0.150928   556  LYS A O   
4246 C  CB  . LYS A 520 ? 0.280635 0.605923 0.516842 0.050815    0.037654    -0.175929   556  LYS A CB  
4247 C  CG  . LYS A 520 ? 0.319742 0.669555 0.568711 0.035653    0.0485488   -0.180639   556  LYS A CG  
4248 C  CD  . LYS A 520 ? 0.370173 0.712796 0.603682 0.0180418   0.0602007   -0.171708   556  LYS A CD  
4249 C  CE  . LYS A 520 ? 0.341307 0.709568 0.589424 0.00341212  0.0715222   -0.177605   556  LYS A CE  
4250 N  NZ  . LYS A 520 ? 0.311695 0.682188 0.567729 -0.0019231  0.0669601   -0.17463    556  LYS A NZ  
4251 N  N   . GLU A 521 ? 0.279447 0.546951 0.485855 0.0744217   0.0115225   -0.156978   557  GLU A N   
4252 C  CA  . GLU A 521 ? 0.299197 0.540122 0.490806 0.0860439   0.00303012  -0.150682   557  GLU A CA  
4253 C  C   . GLU A 521 ? 0.299429 0.514885 0.468822 0.077099    0.00384983  -0.136068   557  GLU A C   
4254 O  O   . GLU A 521 ? 0.293339 0.488826 0.447786 0.0782363   0.00483721  -0.130968   557  GLU A O   
4255 C  CB  . GLU A 521 ? 0.321498 0.564087 0.521574 0.101376    -0.00945896 -0.154302   557  GLU A CB  
4256 C  CG  . GLU A 521 ? 0.380283 0.650454 0.604274 0.110785    -0.0105361  -0.169918   557  GLU A CG  
4257 C  CD  . GLU A 521 ? 0.448087 0.750918 0.69365  0.102372    -0.00592261 -0.178908   557  GLU A CD  
4258 O  OE1 . GLU A 521 ? 0.452627 0.758008 0.696362 0.089153    -0.00285636 -0.173264   557  GLU A OE1 
4259 O  OE2 . GLU A 521 ? 0.481598 0.808304 0.747188 0.109082    -0.00492606 -0.192643   557  GLU A OE2 
4260 N  N   . ALA A 522 ? 0.293787 0.510455 0.461849 0.0680399   0.00347385  -0.130004   558  ALA A N   
4261 C  CA  . ALA A 522 ? 0.306724 0.50216  0.455863 0.0593039   0.00475559  -0.117293   558  ALA A CA  
4262 C  C   . ALA A 522 ? 0.338083 0.530962 0.478461 0.0488395   0.0151256   -0.115066   558  ALA A C   
4263 O  O   . ALA A 522 ? 0.348951 0.521468 0.472938 0.0480491   0.0152265   -0.107777   558  ALA A O   
4264 C  CB  . ALA A 522 ? 0.306052 0.505149 0.457725 0.0525109   0.00230284  -0.113115   558  ALA A CB  
4265 N  N   . GLY A 523 ? 0.30908  0.522873 0.460058 0.041736    0.0239121   -0.122265   559  GLY A N   
4266 C  CA  . GLY A 523 ? 0.284635 0.494305 0.424202 0.0326742   0.0330452   -0.119504   559  GLY A CA  
4267 C  C   . GLY A 523 ? 0.316315 0.513342 0.447361 0.0411041   0.0320897   -0.12151    559  GLY A C   
4268 O  O   . GLY A 523 ? 0.279122 0.459873 0.39403  0.0371376   0.034069    -0.114995   559  GLY A O   
4269 N  N   . GLN A 524 ? 0.324601 0.530823 0.467945 0.0527195   0.0293793   -0.131851   560  GLN A N   
4270 C  CA  . GLN A 524 ? 0.357947 0.553131 0.495928 0.0615742   0.0284081   -0.13566    560  GLN A CA  
4271 C  C   . GLN A 524 ? 0.358299 0.523782 0.478655 0.0648111   0.0221616   -0.125457   560  GLN A C   
4272 O  O   . GLN A 524 ? 0.368571 0.521263 0.477424 0.0633642   0.024922    -0.124044   560  GLN A O   
4273 C  CB  . GLN A 524 ? 0.406207 0.617049 0.56223  0.0742555   0.0257999   -0.148782   560  GLN A CB  
4274 C  CG  . GLN A 524 ? 0.561429 0.76857  0.714993 0.0797306   0.0292907   -0.156117   560  GLN A CG  
4275 C  CD  . GLN A 524 ? 0.642237 0.858601 0.790115 0.0668807   0.0408906   -0.15738    560  GLN A CD  
4276 O  OE1 . GLN A 524 ? 0.683363 0.923043 0.841615 0.0594283   0.0480402   -0.162399   560  GLN A OE1 
4277 N  NE2 . GLN A 524 ? 0.675761 0.873937 0.806523 0.0635126   0.0428594   -0.152452   560  GLN A NE2 
4278 N  N   . ARG A 525 ? 0.372542 0.527127 0.490038 0.0681811   0.0142175   -0.118338   561  ARG A N   
4279 C  CA  . ARG A 525 ? 0.360593 0.488382 0.461257 0.0693632   0.00982246  -0.108536   561  ARG A CA  
4280 C  C   . ARG A 525 ? 0.408326 0.527673 0.495174 0.0569071   0.0156484   -0.1011     561  ARG A C   
4281 O  O   . ARG A 525 ? 0.398756 0.501664 0.47416  0.0571918   0.0161344   -0.0986368  561  ARG A O   
4282 C  CB  . ARG A 525 ? 0.418601 0.539289 0.518281 0.0734604   0.00147649  -0.102319   561  ARG A CB  
4283 C  CG  . ARG A 525 ? 0.387579 0.512139 0.497582 0.0881897   -0.0059974  -0.109026   561  ARG A CG  
4284 C  CD  . ARG A 525 ? 0.411737 0.511547 0.510318 0.097898    -0.0114896  -0.105378   561  ARG A CD  
4285 N  NE  . ARG A 525 ? 0.412274 0.518081 0.520638 0.111205    -0.0200406  -0.110001   561  ARG A NE  
4286 C  CZ  . ARG A 525 ? 0.428655 0.523522 0.530915 0.117388    -0.0284017  -0.103936   561  ARG A CZ  
4287 N  NH1 . ARG A 525 ? 0.450839 0.526614 0.53692  0.111696    -0.0291189  -0.0927795  561  ARG A NH1 
4288 N  NH2 . ARG A 525 ? 0.410512 0.513272 0.522324 0.130073    -0.0363185  -0.109374   561  ARG A NH2 
4289 N  N   . LEU A 526 ? 0.374624 0.50492  0.462626 0.0460557   0.0199452   -0.0978695  562  LEU A N   
4290 C  CA  . LEU A 526 ? 0.413266 0.533978 0.487194 0.0354472   0.0239296   -0.089779   562  LEU A CA  
4291 C  C   . LEU A 526 ? 0.359838 0.484151 0.429049 0.0318448   0.0310846   -0.094414   562  LEU A C   
4292 O  O   . LEU A 526 ? 0.336119 0.447237 0.392159 0.0282614   0.0319948   -0.0898505  562  LEU A O   
4293 C  CB  . LEU A 526 ? 0.429998 0.558385 0.504913 0.0251826   0.026304    -0.0843926  562  LEU A CB  
4294 C  CG  . LEU A 526 ? 0.469738 0.591548 0.545219 0.0262436   0.0196381   -0.0782619  562  LEU A CG  
4295 C  CD1 . LEU A 526 ? 0.490757 0.619815 0.566776 0.0145802   0.0238092   -0.0739759  562  LEU A CD1 
4296 C  CD2 . LEU A 526 ? 0.465629 0.564579 0.52697  0.0287343   0.0149469   -0.0704514  562  LEU A CD2 
4297 N  N   . ALA A 527 ? 0.315509 0.45903  0.39589  0.0326875   0.0361637   -0.104119   563  ALA A N   
4298 C  CA  . ALA A 527 ? 0.357128 0.507818 0.433431 0.0283892   0.0439773   -0.10948    563  ALA A CA  
4299 C  C   . ALA A 527 ? 0.366948 0.502583 0.435674 0.0349818   0.0418413   -0.112236   563  ALA A C   
4300 O  O   . ALA A 527 ? 0.367579 0.496948 0.42411  0.0295028   0.0452083   -0.110463   563  ALA A O   
4301 C  CB  . ALA A 527 ? 0.330404 0.505075 0.422174 0.0299275   0.0493831   -0.12087    563  ALA A CB  
4302 N  N   . THR A 528 ? 0.355107 0.485153 0.431222 0.0468976   0.0361682   -0.117116   564  THR A N   
4303 C  CA  . THR A 528 ? 0.391162 0.507285 0.461746 0.0531335   0.0350185   -0.121344   564  THR A CA  
4304 C  C   . THR A 528 ? 0.363255 0.457028 0.418023 0.0486404   0.0321212   -0.11113    564  THR A C   
4305 O  O   . THR A 528 ? 0.40716  0.493101 0.453077 0.0460947   0.0345499   -0.112783   564  THR A O   
4306 C  CB  . THR A 528 ? 0.420564 0.534213 0.502139 0.06744     0.0294803   -0.128561   564  THR A CB  
4307 O  OG1 . THR A 528 ? 0.548968 0.654265 0.63067  0.0703985   0.0222729   -0.120413   564  THR A OG1 
4308 C  CG2 . THR A 528 ? 0.352364 0.49111  0.451826 0.0719658   0.0319252   -0.139274   564  THR A CG2 
4309 N  N   . ALA A 529 ? 0.310068 0.395561 0.361615 0.0467704   0.0274153   -0.10122    565  ALA A N   
4310 C  CA  . ALA A 529 ? 0.311287 0.377691 0.349379 0.0424252   0.0250972   -0.0923039  565  ALA A CA  
4311 C  C   . ALA A 529 ? 0.31193  0.383486 0.341235 0.0312684   0.0304908   -0.0895569  565  ALA A C   
4312 O  O   . ALA A 529 ? 0.293338 0.354287 0.312743 0.0282846   0.0310047   -0.0884107  565  ALA A O   
4313 C  CB  . ALA A 529 ? 0.313223 0.371206 0.349908 0.0429816   0.0194432   -0.0832482  565  ALA A CB  
4314 N  N   . MET A 530 ? 0.284369 0.371891 0.317022 0.0249799   0.0343048   -0.0883897  566  MET A N   
4315 C  CA  . MET A 530 ? 0.294841 0.385162 0.317308 0.0147296   0.0385446   -0.0837389  566  MET A CA  
4316 C  C   . MET A 530 ? 0.321813 0.416599 0.339289 0.0136039   0.0435474   -0.0912048  566  MET A C   
4317 O  O   . MET A 530 ? 0.318981 0.407851 0.324538 0.0083889   0.0443502   -0.088214   566  MET A O   
4318 C  CB  . MET A 530 ? 0.270552 0.37513  0.296981 0.00791444  0.0421812   -0.0807746  566  MET A CB  
4319 C  CG  . MET A 530 ? 0.281288 0.378908 0.308401 0.00647289  0.0372908   -0.07199    566  MET A CG  
4320 S  SD  . MET A 530 ? 0.334549 0.44637  0.364856 -0.00328732 0.0423661   -0.0685246  566  MET A SD  
4321 C  CE  . MET A 530 ? 0.303896 0.434226 0.353641 0.00268974  0.0436582   -0.0790941  566  MET A CE  
4322 N  N   . LYS A 531 ? 0.331366 0.435805 0.35825  0.019592    0.0460144   -0.101587   567  LYS A N   
4323 C  CA  . LYS A 531 ? 0.38306  0.492438 0.406129 0.0194521   0.0508614   -0.110395   567  LYS A CA  
4324 C  C   . LYS A 531 ? 0.37017  0.461796 0.38365  0.0208544   0.0476355   -0.110359   567  LYS A C   
4325 O  O   . LYS A 531 ? 0.335802 0.430246 0.341763 0.017636    0.0512712   -0.11519    567  LYS A O   
4326 C  CB  . LYS A 531 ? 0.358693 0.480535 0.394348 0.0270137   0.0537938   -0.123163   567  LYS A CB  
4327 C  CG  . LYS A 531 ? 0.413753 0.557727 0.457963 0.0230372   0.059698    -0.125791   567  LYS A CG  
4328 C  CD  . LYS A 531 ? 0.449487 0.611552 0.504255 0.0273625   0.0655687   -0.139725   567  LYS A CD  
4329 C  CE  . LYS A 531 ? 0.454577 0.638477 0.514893 0.0195042   0.0729498   -0.140206   567  LYS A CE  
4330 N  NZ  . LYS A 531 ? 0.434957 0.623228 0.506317 0.0195042   0.0696562   -0.135271   567  LYS A NZ  
4331 N  N   . LEU A 532 ? 0.349979 0.424201 0.363745 0.0253711   0.0412585   -0.105675   568  LEU A N   
4332 C  CA  . LEU A 532 ? 0.357906 0.414939 0.364261 0.0262833   0.038757    -0.106521   568  LEU A CA  
4333 C  C   . LEU A 532 ? 0.374391 0.428386 0.368289 0.0172015   0.0390606   -0.100446   568  LEU A C   
4334 O  O   . LEU A 532 ? 0.326295 0.370309 0.314159 0.0161999   0.0380766   -0.102912   568  LEU A O   
4335 C  CB  . LEU A 532 ? 0.378796 0.417045 0.387462 0.0326572   0.0326704   -0.102471   568  LEU A CB  
4336 C  CG  . LEU A 532 ? 0.419752 0.455692 0.438715 0.0438264   0.0307793   -0.109292   568  LEU A CG  
4337 C  CD1 . LEU A 532 ? 0.438051 0.457228 0.457327 0.0492802   0.0243542   -0.101695   568  LEU A CD1 
4338 C  CD2 . LEU A 532 ? 0.416107 0.447444 0.436393 0.0488501   0.0325738   -0.120412   568  LEU A CD2 
4339 N  N   . GLY A 533 ? 0.327437 0.389126 0.317956 0.0108888   0.0398854   -0.0925916  569  GLY A N   
4340 C  CA  . GLY A 533 ? 0.344737 0.40182  0.324    0.00386934  0.0385948   -0.0859031  569  GLY A CA  
4341 C  C   . GLY A 533 ? 0.353565 0.392798 0.330818 0.00536891  0.0334923   -0.0829346  569  GLY A C   
4342 O  O   . GLY A 533 ? 0.32681  0.356881 0.309429 0.00962545  0.0302738   -0.0796289  569  GLY A O   
4343 N  N   . PHE A 534 ? 0.345611 0.380727 0.315041 0.0017882   0.033081    -0.0849567  570  PHE A N   
4344 C  CA  . PHE A 534 ? 0.356578 0.376622 0.32413  0.00145094  0.029418    -0.0835596  570  PHE A CA  
4345 C  C   . PHE A 534 ? 0.394053 0.40669  0.363326 0.00481219  0.0303729   -0.0936842  570  PHE A C   
4346 O  O   . PHE A 534 ? 0.401325 0.403062 0.3681   0.00275972  0.0285819   -0.0949328  570  PHE A O   
4347 C  CB  . PHE A 534 ? 0.386728 0.409187 0.345677 -0.00534475 0.0277531   -0.0785981  570  PHE A CB  
4348 C  CG  . PHE A 534 ? 0.412407 0.422065 0.370712 -0.00703226 0.0240734   -0.0758627  570  PHE A CG  
4349 C  CD1 . PHE A 534 ? 0.456832 0.457688 0.4187   -0.00584015 0.0216317   -0.068512   570  PHE A CD1 
4350 C  CD2 . PHE A 534 ? 0.557646 0.565029 0.512    -0.0102214  0.0232991   -0.081219   570  PHE A CD2 
4351 C  CE1 . PHE A 534 ? 0.448514 0.438655 0.409963 -0.00806807 0.0192647   -0.0662421  570  PHE A CE1 
4352 C  CE2 . PHE A 534 ? 0.579743 0.576577 0.535113 -0.0125473  0.0206267   -0.0793712  570  PHE A CE2 
4353 C  CZ  . PHE A 534 ? 0.463715 0.45218  0.422516 -0.0116377  0.0189938   -0.071686   570  PHE A CZ  
4354 N  N   . SER A 535 ? 0.363138 0.38095  0.33795  0.0102068   0.0331349   -0.101165   571  SER A N   
4355 C  CA  . SER A 535 ? 0.4415   0.452418 0.418385 0.0141125   0.0342745   -0.111904   571  SER A CA  
4356 C  C   . SER A 535 ? 0.431592 0.421915 0.412642 0.0192981   0.0312825   -0.111249   571  SER A C   
4357 O  O   . SER A 535 ? 0.467926 0.447921 0.448952 0.020674    0.0316972   -0.118796   571  SER A O   
4358 C  CB  . SER A 535 ? 0.395633 0.42024  0.376995 0.0182518   0.038531    -0.121342   571  SER A CB  
4359 O  OG  . SER A 535 ? 0.38245  0.409932 0.372792 0.0243757   0.0380213   -0.119033   571  SER A OG  
4360 N  N   . ARG A 536 ? 0.385133 0.368122 0.368486 0.0216166   0.0283243   -0.102214   572  ARG A N   
4361 C  CA  . ARG A 536 ? 0.411483 0.37411  0.396555 0.0266973   0.0257147   -0.100494   572  ARG A CA  
4362 C  C   . ARG A 536 ? 0.392004 0.346029 0.373566 0.0232832   0.0229225   -0.0892276  572  ARG A C   
4363 O  O   . ARG A 536 ? 0.401659 0.366636 0.382412 0.0199526   0.0223911   -0.0830707  572  ARG A O   
4364 C  CB  . ARG A 536 ? 0.422716 0.388012 0.415077 0.0359887   0.0244056   -0.100641   572  ARG A CB  
4365 C  CG  . ARG A 536 ? 0.500892 0.477907 0.49971  0.0414596   0.0271464   -0.111796   572  ARG A CG  
4366 C  CD  . ARG A 536 ? 0.591287 0.557398 0.589307 0.0433011   0.0286279   -0.121836   572  ARG A CD  
4367 N  NE  . ARG A 536 ? 0.747835 0.688888 0.742017 0.0437687   0.0260839   -0.118418   572  ARG A NE  
4368 C  CZ  . ARG A 536 ? 0.855972 0.779963 0.849393 0.0456952   0.0264983   -0.125115   572  ARG A CZ  
4369 N  NH1 . ARG A 536 ? 0.714356 0.614794 0.704041 0.0458551   0.0244982   -0.119827   572  ARG A NH1 
4370 N  NH2 . ARG A 536 ? 0.862366 0.792431 0.85871  0.0475992   0.0292241   -0.1373     572  ARG A NH2 
4371 N  N   . PRO A 537 ? 0.406271 0.340385 0.385483 0.0239868   0.0213309   -0.0858246  573  PRO A N   
4372 C  CA  . PRO A 537 ? 0.38097  0.309282 0.356848 0.0208504   0.019294    -0.075392   573  PRO A CA  
4373 C  C   . PRO A 537 ? 0.360439 0.29679  0.33927  0.025739    0.0169933   -0.0695455  573  PRO A C   
4374 O  O   . PRO A 537 ? 0.323094 0.26169  0.30671  0.0334825   0.0161404   -0.0728111  573  PRO A O   
4375 C  CB  . PRO A 537 ? 0.422816 0.326899 0.395743 0.0225326   0.0190514   -0.07473    573  PRO A CB  
4376 C  CG  . PRO A 537 ? 0.441752 0.342114 0.415717 0.0213863   0.0215142   -0.0854308  573  PRO A CG  
4377 C  CD  . PRO A 537 ? 0.410767 0.326304 0.390044 0.0278332   0.0217653   -0.0916063  573  PRO A CD  
4378 N  N   . TRP A 538 ? 0.327375 0.269024 0.304243 0.0213698   0.0158037   -0.0617815  574  TRP A N   
4379 C  CA  . TRP A 538 ? 0.351328 0.303352 0.331733 0.0245719   0.0138681   -0.0574993  574  TRP A CA  
4380 C  C   . TRP A 538 ? 0.363629 0.306009 0.345701 0.0334852   0.0107924   -0.0557731  574  TRP A C   
4381 O  O   . TRP A 538 ? 0.389241 0.342477 0.377106 0.0383575   0.00919405  -0.0564517  574  TRP A O   
4382 C  CB  . TRP A 538 ? 0.278251 0.235447 0.256076 0.0185049   0.0129243   -0.049843   574  TRP A CB  
4383 C  CG  . TRP A 538 ? 0.266815 0.20959  0.239674 0.0167793   0.0115181   -0.0435877  574  TRP A CG  
4384 C  CD1 . TRP A 538 ? 0.274108 0.211431 0.243058 0.010132    0.0126643   -0.0421282  574  TRP A CD1 
4385 C  CD2 . TRP A 538 ? 0.244366 0.178024 0.215582 0.021551    0.00885438  -0.038095   574  TRP A CD2 
4386 N  NE1 . TRP A 538 ? 0.279809 0.205779 0.245215 0.00994643  0.0116883   -0.0360676  574  TRP A NE1 
4387 C  CE2 . TRP A 538 ? 0.259841 0.182497 0.225454 0.0169937   0.00934806  -0.0332975  574  TRP A CE2 
4388 C  CE3 . TRP A 538 ? 0.265037 0.199923 0.239009 0.0293433   0.00594119  -0.0372634  574  TRP A CE3 
4389 C  CZ2 . TRP A 538 ? 0.297164 0.208769 0.258171 0.0197619   0.00763167  -0.0273198  574  TRP A CZ2 
4390 C  CZ3 . TRP A 538 ? 0.274071 0.19782  0.243336 0.0327664   0.00325909  -0.0314205  574  TRP A CZ3 
4391 C  CH2 . TRP A 538 ? 0.305157 0.216719 0.267171 0.0279324   0.00439391  -0.0263012  574  TRP A CH2 
4392 N  N   . PRO A 539 ? 0.384236 0.306396 0.361103 0.0359444   0.0096508   -0.0531965  575  PRO A N   
4393 C  CA  . PRO A 539 ? 0.374573 0.286952 0.350996 0.0452818   0.00589679  -0.0505694  575  PRO A CA  
4394 C  C   . PRO A 539 ? 0.401634 0.322278 0.3861   0.0535845   0.00507457  -0.0584947  575  PRO A C   
4395 O  O   . PRO A 539 ? 0.39779  0.319573 0.385328 0.0619892   0.0012016   -0.057784   575  PRO A O   
4396 C  CB  . PRO A 539 ? 0.375914 0.26322  0.343981 0.0448919   0.00656202  -0.0479635  575  PRO A CB  
4397 C  CG  . PRO A 539 ? 0.399015 0.288378 0.36378  0.0335771   0.00959693  -0.0450897  575  PRO A CG  
4398 C  CD  . PRO A 539 ? 0.386981 0.294291 0.357749 0.0299563   0.011761    -0.0522832  575  PRO A CD  
4399 N  N   . GLU A 540 ? 0.391612 0.319057 0.379801 0.0516596   0.00855103  -0.0667996  576  GLU A N   
4400 C  CA  . GLU A 540 ? 0.409694 0.346401 0.406468 0.0598332   0.00828005  -0.0753191  576  GLU A CA  
4401 C  C   . GLU A 540 ? 0.376341 0.337046 0.381226 0.0597751   0.00823853  -0.0761142  576  GLU A C   
4402 O  O   . GLU A 540 ? 0.379831 0.347918 0.392533 0.0681889   0.00566621  -0.0794701  576  GLU A O   
4403 C  CB  . GLU A 540 ? 0.4286   0.365538 0.427038 0.0589057   0.0121154   -0.085136   576  GLU A CB  
4404 C  CG  . GLU A 540 ? 0.496982 0.408955 0.489404 0.0601878   0.0120114   -0.0859972  576  GLU A CG  
4405 C  CD  . GLU A 540 ? 0.661794 0.575896 0.656233 0.0582661   0.0158845   -0.0968574  576  GLU A CD  
4406 O  OE1 . GLU A 540 ? 0.668554 0.601533 0.669985 0.0604511   0.0177993   -0.104601   576  GLU A OE1 
4407 O  OE2 . GLU A 540 ? 0.731256 0.62924  0.720461 0.0540093   0.0173884   -0.098233   576  GLU A OE2 
4408 N  N   . ALA A 541 ? 0.340942 0.313774 0.344296 0.0502268   0.0110722   -0.0733598  577  ALA A N   
4409 C  CA  . ALA A 541 ? 0.343626 0.33634  0.353699 0.0488364   0.0113806   -0.0728208  577  ALA A CA  
4410 C  C   . ALA A 541 ? 0.325587 0.314991 0.336872 0.0535479   0.0061245   -0.0666113  577  ALA A C   
4411 O  O   . ALA A 541 ? 0.31629  0.317762 0.336478 0.0590009   0.00414345  -0.0695549  577  ALA A O   
4412 C  CB  . ALA A 541 ? 0.324089 0.326314 0.330233 0.0380514   0.0148942   -0.0696526  577  ALA A CB  
4413 N  N   . MET A 542 ? 0.296639 0.270462 0.299209 0.0516013   0.00384365  -0.0587163  578  MET A N   
4414 C  CA  . MET A 542 ? 0.312099 0.281641 0.31394  0.0566352   -0.00125664 -0.0532663  578  MET A CA  
4415 C  C   . MET A 542 ? 0.337634 0.30418  0.344151 0.0690043   -0.0057314  -0.0571403  578  MET A C   
4416 O  O   . MET A 542 ? 0.308584 0.284643 0.320656 0.0737529   -0.00970306 -0.0568931  578  MET A O   
4417 C  CB  . MET A 542 ? 0.307758 0.259834 0.298453 0.0528524   -0.00210016 -0.0450145  578  MET A CB  
4418 C  CG  . MET A 542 ? 0.316973 0.263014 0.30455  0.05847     -0.00725934 -0.039528   578  MET A CG  
4419 S  SD  . MET A 542 ? 0.347842 0.311042 0.340015 0.0545557   -0.00903973 -0.0363102  578  MET A SD  
4420 C  CE  . MET A 542 ? 0.34066  0.299376 0.325233 0.0430431   -0.00570897 -0.0298299  578  MET A CE  
4421 N  N   A GLN A 543 ? 0.350289 0.303511 0.354762 0.0743479   -0.00545529 -0.0610506  579  GLN A N   
4422 N  N   B GLN A 543 ? 0.354348 0.307635 0.358937 0.074474    -0.00546765 -0.0611716  579  GLN A N   
4423 C  CA  A GLN A 543 ? 0.346455 0.29447  0.354822 0.087175    -0.0100088  -0.0651049  579  GLN A CA  
4424 C  CA  B GLN A 543 ? 0.350164 0.297402 0.358232 0.0874031   -0.0101465  -0.064948   579  GLN A CA  
4425 C  C   A GLN A 543 ? 0.344755 0.316554 0.368005 0.0919877   -0.0102095  -0.0740729  579  GLN A C   
4426 C  C   B GLN A 543 ? 0.346169 0.317083 0.369232 0.0923147   -0.0102275  -0.0742335  579  GLN A C   
4427 O  O   A GLN A 543 ? 0.338069 0.31477  0.367293 0.101636    -0.0157092  -0.0757316  579  GLN A O   
4428 O  O   B GLN A 543 ? 0.335592 0.311235 0.364672 0.102134    -0.0157094  -0.0760425  579  GLN A O   
4429 C  CB  A GLN A 543 ? 0.350426 0.281309 0.355181 0.0900045   -0.00807039 -0.0693085  579  GLN A CB  
4430 C  CB  B GLN A 543 ? 0.361437 0.285402 0.362719 0.0912532   -0.00956815 -0.0663623  579  GLN A CB  
4431 C  CG  A GLN A 543 ? 0.363458 0.29159  0.374725 0.103755    -0.0120138  -0.0761673  579  GLN A CG  
4432 C  CG  B GLN A 543 ? 0.368752 0.271494 0.362962 0.10213     -0.0156683  -0.0618071  579  GLN A CG  
4433 C  CD  A GLN A 543 ? 0.359874 0.277041 0.367182 0.1144      -0.0196791  -0.0706369  579  GLN A CD  
4434 C  CD  B GLN A 543 ? 0.402297 0.278351 0.3885   0.105105    -0.0147954  -0.0620384  579  GLN A CD  
4435 O  OE1 A GLN A 543 ? 0.350711 0.248624 0.34515  0.112737    -0.0213091  -0.0612886  579  GLN A OE1 
4436 O  OE1 B GLN A 543 ? 0.439969 0.314961 0.431962 0.109432    -0.0134214  -0.0706252  579  GLN A OE1 
4437 N  NE2 A GLN A 543 ? 0.370531 0.300493 0.38869  0.125495    -0.0243961  -0.0767449  579  GLN A NE2 
4438 N  NE2 B GLN A 543 ? 0.401451 0.254381 0.374079 0.103178    -0.015455   -0.052936   579  GLN A NE2 
4439 N  N   . LEU A 544 ? 0.345836 0.332526 0.374904 0.085563    -0.00416498 -0.0804071  580  LEU A N   
4440 C  CA  . LEU A 544 ? 0.362857 0.374538 0.406332 0.0879137   -0.00266666 -0.0890385  580  LEU A CA  
4441 C  C   . LEU A 544 ? 0.347404 0.374881 0.397427 0.0867741   -0.00539957 -0.086194   580  LEU A C   
4442 O  O   . LEU A 544 ? 0.332128 0.374858 0.394589 0.0939394   -0.00808916 -0.092416   580  LEU A O   
4443 C  CB  . LEU A 544 ? 0.338466 0.363207 0.38367  0.0786469   0.00520496  -0.0942023  580  LEU A CB  
4444 C  CG  . LEU A 544 ? 0.370214 0.387016 0.414252 0.0818597   0.00795436  -0.101864   580  LEU A CG  
4445 C  CD1 . LEU A 544 ? 0.348588 0.373787 0.388968 0.0711884   0.015097    -0.104462   580  LEU A CD1 
4446 C  CD2 . LEU A 544 ? 0.398282 0.425421 0.455485 0.0935342   0.0065641   -0.112758   580  LEU A CD2 
4447 N  N   . ILE A 545 ? 0.304069 0.329753 0.347081 0.0773042   -0.00440834 -0.0779107  581  ILE A N   
4448 C  CA  . ILE A 545 ? 0.302138 0.342218 0.351519 0.075276    -0.00663392 -0.0758627  581  ILE A CA  
4449 C  C   . ILE A 545 ? 0.34841  0.38     0.39628  0.085061    -0.0150472  -0.0725593  581  ILE A C   
4450 O  O   . ILE A 545 ? 0.358158 0.40519  0.417093 0.0900304   -0.0186354  -0.0768659  581  ILE A O   
4451 C  CB  . ILE A 545 ? 0.303463 0.345087 0.346711 0.0623968   -0.00285972 -0.0689171  581  ILE A CB  
4452 C  CG1 . ILE A 545 ? 0.269365 0.320506 0.312977 0.0533786   0.00496437  -0.072112   581  ILE A CG1 
4453 C  CG2 . ILE A 545 ? 0.235391 0.289175 0.2847   0.0599211   -0.00531276 -0.0667324  581  ILE A CG2 
4454 C  CD1 . ILE A 545 ? 0.252747 0.298593 0.286721 0.0426793   0.00739432  -0.0641811  581  ILE A CD1 
4455 N  N   . THR A 546 ? 0.358725 0.3669   0.392725 0.0871622   -0.0180584  -0.06493    582  THR A N   
4456 C  CA  . THR A 546 ? 0.375941 0.376096 0.404586 0.093196    -0.0251771  -0.0593255  582  THR A CA  
4457 C  C   . THR A 546 ? 0.428088 0.412654 0.452615 0.106687    -0.0310063  -0.0600036  582  THR A C   
4458 O  O   . THR A 546 ? 0.399189 0.375424 0.417336 0.11347     -0.0376155  -0.0553134  582  THR A O   
4459 C  CB  . THR A 546 ? 0.341813 0.328737 0.357227 0.0854952   -0.0245429  -0.0494137  582  THR A CB  
4460 O  OG1 . THR A 546 ? 0.338082 0.302905 0.34222  0.0860562   -0.0228542  -0.0460925  582  THR A OG1 
4461 C  CG2 . THR A 546 ? 0.282771 0.28111  0.300513 0.0727409   -0.0190242  -0.0480442  582  THR A CG2 
4462 N  N   . GLY A 547 ? 0.401555 0.379321 0.427411 0.110326    -0.0285589  -0.0650352  583  GLY A N   
4463 C  CA  . GLY A 547 ? 0.412609 0.371836 0.43315  0.123061    -0.0340087  -0.0648959  583  GLY A CA  
4464 C  C   . GLY A 547 ? 0.436759 0.366155 0.438812 0.1213      -0.0338901  -0.0552224  583  GLY A C   
4465 O  O   . GLY A 547 ? 0.475801 0.385674 0.471277 0.130981    -0.037594   -0.0541363  583  GLY A O   
4466 N  N   . GLN A 548 ? 0.418569 0.343962 0.412594 0.109045    -0.0293407  -0.0486168  584  GLN A N   
4467 C  CA  . GLN A 548 ? 0.408916 0.308269 0.387043 0.105391    -0.0275764  -0.04054    584  GLN A CA  
4468 C  C   . GLN A 548 ? 0.401713 0.303773 0.378628 0.0911637   -0.0200757  -0.0395624  584  GLN A C   
4469 O  O   . GLN A 548 ? 0.377849 0.300336 0.364284 0.0852223   -0.0171252  -0.0438857  584  GLN A O   
4470 C  CB  . GLN A 548 ? 0.382324 0.27073  0.348948 0.109553    -0.0329901  -0.0318829  584  GLN A CB  
4471 C  CG  . GLN A 548 ? 0.420534 0.324534 0.388594 0.102041    -0.0327906  -0.0287254  584  GLN A CG  
4472 C  CD  . GLN A 548 ? 0.435953 0.337266 0.398965 0.0882775   -0.0260503  -0.0245322  584  GLN A CD  
4473 O  OE1 . GLN A 548 ? 0.446928 0.3283   0.397292 0.0849283   -0.0238192  -0.0183099  584  GLN A OE1 
4474 N  NE2 . GLN A 548 ? 0.355854 0.277199 0.328361 0.0802683   -0.0229925  -0.02755    584  GLN A NE2 
4475 N  N   . PRO A 549 ? 0.413309 0.295423 0.379366 0.0852885   -0.016439   -0.0349449  585  PRO A N   
4476 C  CA  . PRO A 549 ? 0.395888 0.282735 0.362934 0.0730655   -0.0100042  -0.0361831  585  PRO A CA  
4477 C  C   . PRO A 549 ? 0.370246 0.255186 0.330355 0.0629564   -0.00754929 -0.029103   585  PRO A C   
4478 O  O   . PRO A 549 ? 0.347541 0.23474  0.308007 0.0539127   -0.00300872 -0.0302405  585  PRO A O   
4479 C  CB  . PRO A 549 ? 0.440155 0.305962 0.40265  0.0751402   -0.00791021 -0.0388638  585  PRO A CB  
4480 C  CG  . PRO A 549 ? 0.45392  0.296088 0.403774 0.0808909   -0.0113312  -0.0307047  585  PRO A CG  
4481 C  CD  . PRO A 549 ? 0.4251   0.279453 0.378552 0.0902683   -0.0179617  -0.0297687  585  PRO A CD  
4482 N  N   . GLN A 550 ? 0.386398 0.26648  0.339662 0.064957    -0.0107486  -0.0221563  586  GLN A N   
4483 C  CA  . GLN A 550 ? 0.443499 0.323938 0.39145  0.0560712   -0.00845549 -0.0163902  586  GLN A CA  
4484 C  C   . GLN A 550 ? 0.391291 0.292766 0.346176 0.0527597   -0.00965957 -0.0164548  586  GLN A C   
4485 O  O   . GLN A 550 ? 0.384801 0.299653 0.347062 0.0581806   -0.0132987  -0.0193675  586  GLN A O   
4486 C  CB  . GLN A 550 ? 0.486445 0.352054 0.423169 0.0620806   -0.0121393  -0.00959176 586  GLN A CB  
4487 C  CG  . GLN A 550 ? 0.569348 0.410479 0.496727 0.0667737   -0.0118369  -0.007659   586  GLN A CG  
4488 C  CD  . GLN A 550 ? 0.774985 0.59999  0.691062 0.0585138   -0.00708237 -0.00141706 586  GLN A CD  
4489 O  OE1 . GLN A 550 ? 0.927283 0.754237 0.846561 0.0489467   -0.001745   -0.00361137 586  GLN A OE1 
4490 N  NE2 . GLN A 550 ? 0.6973   0.508473 0.60039  0.0617421   -0.00893773 0.00604239  586  GLN A NE2 
4491 N  N   . MET A 551 ? 0.363259 0.266941 0.31591  0.0437934   -0.00665148 -0.0133188  587  MET A N   
4492 C  CA  . MET A 551 ? 0.381819 0.298806 0.337415 0.0407947   -0.00806993 -0.0113213  587  MET A CA  
4493 C  C   . MET A 551 ? 0.398436 0.307444 0.345785 0.0455722   -0.011761   -0.00610417 587  MET A C   
4494 O  O   . MET A 551 ? 0.359125 0.251051 0.295985 0.046248    -0.0107785  -0.00195585 587  MET A O   
4495 C  CB  . MET A 551 ? 0.389234 0.309661 0.344715 0.0308923   -0.00420049 -0.00984611 587  MET A CB  
4496 C  CG  . MET A 551 ? 0.385714 0.31715  0.348371 0.0258045   -0.00136509 -0.014546   587  MET A CG  
4497 S  SD  . MET A 551 ? 0.391993 0.328221 0.354339 0.0158878   0.00143427  -0.0126419  587  MET A SD  
4498 C  CE  . MET A 551 ? 0.388395 0.306171 0.343162 0.0138402   0.00439417  -0.0115869  587  MET A CE  
4499 N  N   . SER A 552 ? 0.37969  0.300954 0.331226 0.0483212   -0.0157413  -0.00644002 588  SER A N   
4500 C  CA  . SER A 552 ? 0.389162 0.305155 0.332889 0.0538907   -0.0202216  -0.00259761 588  SER A CA  
4501 C  C   . SER A 552 ? 0.373366 0.305496 0.323394 0.0517235   -0.0225606  -0.00368552 588  SER A C   
4502 O  O   . SER A 552 ? 0.368385 0.315855 0.330145 0.0507808   -0.0230503  -0.00837536 588  SER A O   
4503 C  CB  . SER A 552 ? 0.391248 0.302364 0.333798 0.0652757   -0.0253986  -0.00411692 588  SER A CB  
4504 O  OG  . SER A 552 ? 0.423635 0.332382 0.358837 0.0716248   -0.0309771  -0.00103067 588  SER A OG  
4505 N  N   . ALA A 553 ? 0.348611 0.277077 0.290922 0.0499179   -0.0231825  0.00034873  589  ALA A N   
4506 C  CA  . ALA A 553 ? 0.322688 0.264165 0.269855 0.0488246   -0.0260721  -0.00103664 589  ALA A CA  
4507 C  C   . ALA A 553 ? 0.329776 0.276312 0.277429 0.0579702   -0.0331334  -0.00307177 589  ALA A C   
4508 O  O   . ALA A 553 ? 0.352356 0.309568 0.304248 0.057335    -0.0359721  -0.00504215 589  ALA A O   
4509 C  CB  . ALA A 553 ? 0.28437  0.2195   0.222365 0.0445222   -0.0242307  0.00318761  589  ALA A CB  
4510 N  N   . SER A 554 ? 0.339541 0.27755  0.28202  0.0667412   -0.0364477  -0.0025727  590  SER A N   
4511 C  CA  . SER A 554 ? 0.373985 0.317455 0.317212 0.0768101   -0.0442225  -0.00498663 590  SER A CA  
4512 C  C   . SER A 554 ? 0.355834 0.32181  0.315802 0.0761132   -0.0469361  -0.0121432  590  SER A C   
4513 O  O   . SER A 554 ? 0.325304 0.299556 0.286107 0.079039    -0.0522274  -0.0139673  590  SER A O   
4514 C  CB  . SER A 554 ? 0.408178 0.343545 0.349954 0.0860835   -0.0469181  -0.00577728 590  SER A CB  
4515 O  OG  . SER A 554 ? 0.516788 0.43126  0.440252 0.0889442   -0.0471431  0.00144865  590  SER A OG  
4516 N  N   . ALA A 555 ? 0.3095   0.285004 0.282317 0.0726272   -0.0433448  -0.016583   591  ALA A N   
4517 C  CA  . ALA A 555 ? 0.283832 0.280415 0.273195 0.0712754   -0.0446532  -0.0236251  591  ALA A CA  
4518 C  C   . ALA A 555 ? 0.285377 0.289687 0.277681 0.0630729   -0.0435379  -0.0233995  591  ALA A C   
4519 O  O   . ALA A 555 ? 0.267623 0.284073 0.266584 0.0648207   -0.0481934  -0.0274733  591  ALA A O   
4520 C  CB  . ALA A 555 ? 0.275463 0.278876 0.275165 0.0679885   -0.0395938  -0.0275258  591  ALA A CB  
4521 N  N   . MET A 556 ? 0.271493 0.267815 0.258164 0.0548405   -0.0380869  -0.0188368  592  MET A N   
4522 C  CA  . MET A 556 ? 0.286063 0.288014 0.275223 0.0480777   -0.0374805  -0.0187224  592  MET A CA  
4523 C  C   . MET A 556 ? 0.329986 0.330412 0.312102 0.0527935   -0.0432605  -0.0182881  592  MET A C   
4524 O  O   . MET A 556 ? 0.325218 0.33633  0.314158 0.0509186   -0.0459134  -0.0220281  592  MET A O   
4525 C  CB  . MET A 556 ? 0.272325 0.265558 0.256011 0.0400335   -0.031695   -0.0140291  592  MET A CB  
4526 C  CG  . MET A 556 ? 0.277208 0.275776 0.264765 0.0332077   -0.0309421  -0.014295   592  MET A CG  
4527 S  SD  . MET A 556 ? 0.351639 0.342936 0.336189 0.0251058   -0.0245799  -0.0100772  592  MET A SD  
4528 C  CE  . MET A 556 ? 0.420901 0.420823 0.414599 0.0178247   -0.0237854  -0.0116429  592  MET A CE  
4529 N  N   . LEU A 557 ? 0.355448 0.341865 0.322928 0.0584221   -0.0449695  -0.0137109  593  LEU A N   
4530 C  CA  . LEU A 557 ? 0.381075 0.365195 0.339032 0.0630983   -0.0502093  -0.0128264  593  LEU A CA  
4531 C  C   . LEU A 557 ? 0.374955 0.372355 0.340414 0.0706032   -0.0580231  -0.0188702  593  LEU A C   
4532 O  O   . LEU A 557 ? 0.364301 0.369556 0.33084  0.0709645   -0.062203   -0.0219609  593  LEU A O   
4533 C  CB  . LEU A 557 ? 0.433647 0.398858 0.373053 0.0674531   -0.0497517  -0.00604166 593  LEU A CB  
4534 C  CG  . LEU A 557 ? 0.463377 0.41621  0.393631 0.0600804   -0.0426995  -0.00056275 593  LEU A CG  
4535 C  CD1 . LEU A 557 ? 0.459318 0.394164 0.369638 0.0643647   -0.0426987  0.00590731  593  LEU A CD1 
4536 C  CD2 . LEU A 557 ? 0.451664 0.41208  0.386177 0.0529658   -0.0408366  -0.00223039 593  LEU A CD2 
4537 N  N   A SER A 558 ? 0.335686 0.336568 0.307436 0.0765486   -0.0599914  -0.0214448  594  SER A N   
4538 N  N   B SER A 558 ? 0.339688 0.340008 0.310629 0.0771092   -0.0603361  -0.0212763  594  SER A N   
4539 C  CA  A SER A 558 ? 0.327122 0.341541 0.307444 0.0849249   -0.0676732  -0.0278774  594  SER A CA  
4540 C  CA  B SER A 558 ? 0.323121 0.338321 0.303613 0.0847172   -0.067943   -0.0281107  594  SER A CA  
4541 C  C   A SER A 558 ? 0.308025 0.343019 0.306693 0.0784204   -0.0674436  -0.0354397  594  SER A C   
4542 C  C   B SER A 558 ? 0.302481 0.336631 0.299993 0.0771633   -0.0670443  -0.0349     594  SER A C   
4543 O  O   A SER A 558 ? 0.302606 0.349581 0.306469 0.0817625   -0.0738541  -0.040824   594  SER A O   
4544 O  O   B SER A 558 ? 0.299595 0.343611 0.300221 0.0787357   -0.0725576  -0.0392571  594  SER A O   
4545 C  CB  A SER A 558 ? 0.313692 0.326384 0.297828 0.0916942   -0.0681017  -0.0290921  594  SER A CB  
4546 C  CB  B SER A 558 ? 0.313255 0.331372 0.301118 0.09146     -0.0691307  -0.0310581  594  SER A CB  
4547 O  OG  A SER A 558 ? 0.327189 0.356448 0.324313 0.0993054   -0.0745776  -0.0369086  594  SER A OG  
4548 O  OG  B SER A 558 ? 0.321891 0.320187 0.294729 0.0974943   -0.0689984  -0.0246854  594  SER A OG  
4549 N  N   . TYR A 559 ? 0.272493 0.310962 0.280313 0.0688803   -0.0600173  -0.0358006  595  TYR A N   
4550 C  CA  . TYR A 559 ? 0.2772   0.331492 0.300556 0.0606752   -0.0580152  -0.0414014  595  TYR A CA  
4551 C  C   . TYR A 559 ? 0.280047 0.334899 0.300081 0.0576626   -0.0607877  -0.0418551  595  TYR A C   
4552 O  O   . TYR A 559 ? 0.286527 0.356018 0.317698 0.0571403   -0.0647415  -0.0488382  595  TYR A O   
4553 C  CB  . TYR A 559 ? 0.231872 0.284435 0.259651 0.0513271   -0.0493741  -0.0391941  595  TYR A CB  
4554 C  CG  . TYR A 559 ? 0.250469 0.317195 0.293212 0.0422364   -0.0461937  -0.043952   595  TYR A CG  
4555 C  CD1 . TYR A 559 ? 0.231315 0.296357 0.27365  0.0350825   -0.0452188  -0.0429177  595  TYR A CD1 
4556 C  CD2 . TYR A 559 ? 0.258489 0.339261 0.315334 0.0403623   -0.0435632  -0.0494002  595  TYR A CD2 
4557 C  CE1 . TYR A 559 ? 0.217456 0.291991 0.271881 0.0262215   -0.0418938  -0.0462812  595  TYR A CE1 
4558 C  CE2 . TYR A 559 ? 0.249065 0.340976 0.318204 0.0307235   -0.0395212  -0.0528882  595  TYR A CE2 
4559 C  CZ  . TYR A 559 ? 0.244748 0.332332 0.312109 0.0236658   -0.038808   -0.0508857  595  TYR A CZ  
4560 O  OH  . TYR A 559 ? 0.244529 0.340074 0.322652 0.01402     -0.0347217  -0.053556   595  TYR A OH  
4561 N  N   . PHE A 560 ? 0.273172 0.312771 0.278512 0.0557523   -0.0586434  -0.0352386  596  PHE A N   
4562 C  CA  . PHE A 560 ? 0.317799 0.356838 0.320334 0.0512624   -0.0592915  -0.0356634  596  PHE A CA  
4563 C  C   . PHE A 560 ? 0.327302 0.364325 0.318408 0.0592556   -0.0665542  -0.0362927  596  PHE A C   
4564 O  O   . PHE A 560 ? 0.31564  0.35355  0.303785 0.0570727   -0.0682316  -0.0380455  596  PHE A O   
4565 C  CB  . PHE A 560 ? 0.271455 0.298513 0.267422 0.0437607   -0.0524889  -0.0297564  596  PHE A CB  
4566 C  CG  . PHE A 560 ? 0.253741 0.285946 0.261975 0.0346974   -0.047037   -0.0307789  596  PHE A CG  
4567 C  CD1 . PHE A 560 ? 0.235282 0.27669  0.254561 0.0289383   -0.0474864  -0.0356318  596  PHE A CD1 
4568 C  CD2 . PHE A 560 ? 0.276654 0.303133 0.284024 0.0316546   -0.0413651  -0.0266388  596  PHE A CD2 
4569 C  CE1 . PHE A 560 ? 0.244102 0.287938 0.272616 0.0203238   -0.0420998  -0.0354126  596  PHE A CE1 
4570 C  CE2 . PHE A 560 ? 0.274833 0.305458 0.29124  0.0237362   -0.0365257  -0.0269402  596  PHE A CE2 
4571 C  CZ  . PHE A 560 ? 0.26776  0.306186 0.293994 0.0179683   -0.0367271  -0.0307121  596  PHE A CZ  
4572 N  N   . LYS A 561 ? 0.337266 0.371691 0.321603 0.0690838   -0.0713289  -0.0352684  597  LYS A N   
4573 C  CA  . LYS A 561 ? 0.348102 0.37745  0.317367 0.0773999   -0.0780419  -0.0340185  597  LYS A CA  
4574 C  C   . LYS A 561 ? 0.347944 0.391004 0.322693 0.0776356   -0.084241   -0.0415522  597  LYS A C   
4575 O  O   . LYS A 561 ? 0.390752 0.428052 0.351956 0.0791409   -0.0864123  -0.0400305  597  LYS A O   
4576 C  CB  . LYS A 561 ? 0.355799 0.380201 0.318439 0.0886143   -0.0828481  -0.0319478  597  LYS A CB  
4577 C  CG  . LYS A 561 ? 0.403506 0.430932 0.356995 0.0989201   -0.092835   -0.0341102  597  LYS A CG  
4578 C  CD  . LYS A 561 ? 0.466679 0.475113 0.394665 0.10417     -0.0939974  -0.0258289  597  LYS A CD  
4579 C  CE  . LYS A 561 ? 0.515159 0.526861 0.434973 0.117672    -0.10549    -0.027829   597  LYS A CE  
4580 N  NZ  . LYS A 561 ? 0.449223 0.448807 0.346684 0.118225    -0.105778   -0.0224271  597  LYS A NZ  
4581 N  N   . PRO A 562 ? 0.328996 0.390877 0.322884 0.0763498   -0.0875006  -0.0505006  598  PRO A N   
4582 C  CA  . PRO A 562 ? 0.336242 0.410126 0.335055 0.075648    -0.0931393  -0.058162   598  PRO A CA  
4583 C  C   . PRO A 562 ? 0.317773 0.386146 0.314822 0.0659783   -0.0878239  -0.0572841  598  PRO A C   
4584 O  O   . PRO A 562 ? 0.338194 0.409756 0.331505 0.0662733   -0.0918776  -0.0614503  598  PRO A O   
4585 C  CB  . PRO A 562 ? 0.326301 0.421036 0.348129 0.0742796   -0.0957346  -0.0678019  598  PRO A CB  
4586 C  CG  . PRO A 562 ? 0.35901  0.452873 0.383778 0.0795784   -0.0944612  -0.065148   598  PRO A CG  
4587 C  CD  . PRO A 562 ? 0.3426   0.416107 0.354261 0.0754896   -0.0860228  -0.0546275  598  PRO A CD  
4588 N  N   . LEU A 563 ? 0.308124 0.368766 0.308118 0.0577816   -0.0792118  -0.052572   599  LEU A N   
4589 C  CA  . LEU A 563 ? 0.275396 0.331299 0.275341 0.0493519   -0.0747998  -0.0523754  599  LEU A CA  
4590 C  C   . LEU A 563 ? 0.321742 0.363309 0.301502 0.052255    -0.0737656  -0.0462694  599  LEU A C   
4591 O  O   . LEU A 563 ? 0.322742 0.363364 0.298072 0.0503609   -0.074491   -0.0487425  599  LEU A O   
4592 C  CB  . LEU A 563 ? 0.283482 0.336165 0.292854 0.0400941   -0.066672   -0.0494383  599  LEU A CB  
4593 C  CG  . LEU A 563 ? 0.305023 0.350196 0.313415 0.0324879   -0.0620518  -0.0479591  599  LEU A CG  
4594 C  CD1 . LEU A 563 ? 0.339244 0.393603 0.35865  0.0282896   -0.065019   -0.0563038  599  LEU A CD1 
4595 C  CD2 . LEU A 563 ? 0.318244 0.35982  0.33348  0.0257346   -0.0551434  -0.0437926  599  LEU A CD2 
4596 N  N   . LEU A 564 ? 0.303085 0.333631 0.270702 0.0567534   -0.0718594  -0.0388387  600  LEU A N   
4597 C  CA  . LEU A 564 ? 0.333119 0.349783 0.2812   0.0587233   -0.0698021  -0.0326977  600  LEU A CA  
4598 C  C   . LEU A 564 ? 0.36626  0.386045 0.303328 0.0649171   -0.0768318  -0.0361966  600  LEU A C   
4599 O  O   . LEU A 564 ? 0.342827 0.357275 0.269209 0.063145    -0.0749305  -0.0354318  600  LEU A O   
4600 C  CB  . LEU A 564 ? 0.373179 0.377351 0.310261 0.0629854   -0.0674101  -0.024805   600  LEU A CB  
4601 C  CG  . LEU A 564 ? 0.434729 0.423763 0.349786 0.0655495   -0.065324   -0.0180112  600  LEU A CG  
4602 C  CD1 . LEU A 564 ? 0.406914 0.390414 0.321241 0.0568808   -0.0573707  -0.0158735  600  LEU A CD1 
4603 C  CD2 . LEU A 564 ? 0.412114 0.387224 0.313928 0.0711343   -0.064548   -0.010605   600  LEU A CD2 
4604 N  N   . ASP A 565 ? 0.339356 0.36816  0.278381 0.0726739   -0.0850417  -0.040261   601  ASP A N   
4605 C  CA  . ASP A 565 ? 0.389202 0.421838 0.316881 0.0797424   -0.0929638  -0.0437551  601  ASP A CA  
4606 C  C   . ASP A 565 ? 0.401491 0.444082 0.337196 0.0741921   -0.0940923  -0.052149   601  ASP A C   
4607 O  O   . ASP A 565 ? 0.356838 0.396692 0.27891  0.0757469   -0.0957203  -0.0531367  601  ASP A O   
4608 C  CB  . ASP A 565 ? 0.396007 0.439499 0.328802 0.0890352   -0.102294   -0.0480487  601  ASP A CB  
4609 C  CG  . ASP A 565 ? 0.47397  0.505258 0.394314 0.0972389   -0.103094   -0.0399341  601  ASP A CG  
4610 O  OD1 . ASP A 565 ? 0.588854 0.602557 0.492805 0.0960387   -0.0971931  -0.0310181  601  ASP A OD1 
4611 O  OD2 . ASP A 565 ? 0.515457 0.554558 0.444007 0.104066    -0.108785   -0.0427801  601  ASP A OD2 
4612 N  N   . TRP A 566 ? 0.352755 0.406407 0.310514 0.0674413   -0.0928311  -0.0583215  602  TRP A N   
4613 C  CA  . TRP A 566 ? 0.326797 0.389046 0.29473  0.0614932   -0.0937993  -0.0668724  602  TRP A CA  
4614 C  C   . TRP A 566 ? 0.334508 0.385267 0.29429  0.0557823   -0.087076   -0.0636453  602  TRP A C   
4615 O  O   . TRP A 566 ? 0.334877 0.387175 0.288716 0.0559446   -0.0893968  -0.0686477  602  TRP A O   
4616 C  CB  . TRP A 566 ? 0.29737  0.371475 0.289649 0.0545391   -0.0926862  -0.0730007  602  TRP A CB  
4617 C  CG  . TRP A 566 ? 0.322789 0.404112 0.32548  0.0482129   -0.093917   -0.0821432  602  TRP A CG  
4618 C  CD1 . TRP A 566 ? 0.328903 0.425013 0.339654 0.0500289   -0.101658   -0.0927814  602  TRP A CD1 
4619 C  CD2 . TRP A 566 ? 0.324617 0.398322 0.330698 0.0396504   -0.0877822  -0.0820263  602  TRP A CD2 
4620 N  NE1 . TRP A 566 ? 0.35667  0.454044 0.37567  0.0424859   -0.100268   -0.0993901  602  TRP A NE1 
4621 C  CE2 . TRP A 566 ? 0.357093 0.440129 0.372741 0.0365356   -0.0919869  -0.0927963  602  TRP A CE2 
4622 C  CE3 . TRP A 566 ? 0.351382 0.411595 0.353675 0.0347824   -0.0797384  -0.0745133  602  TRP A CE3 
4623 C  CZ2 . TRP A 566 ? 0.332263 0.40985  0.353255 0.0290353   -0.0882538  -0.0958947  602  TRP A CZ2 
4624 C  CZ3 . TRP A 566 ? 0.371422 0.42738  0.379478 0.0278437   -0.0764258  -0.0774169  602  TRP A CZ3 
4625 C  CH2 . TRP A 566 ? 0.405391 0.469038 0.422457 0.0251108   -0.0805018  -0.0877308  602  TRP A CH2 
4626 N  N   . LEU A 567 ? 0.332989 0.372773 0.291743 0.0514981   -0.0790766  -0.0557765  603  LEU A N   
4627 C  CA  . LEU A 567 ? 0.320852 0.350749 0.273996 0.0463995   -0.0724194  -0.0526626  603  LEU A CA  
4628 C  C   . LEU A 567 ? 0.365498 0.3886   0.297615 0.051233    -0.0728204  -0.0502369  603  LEU A C   
4629 O  O   . LEU A 567 ? 0.38293  0.404229 0.311067 0.0486856   -0.0706249  -0.0529705  603  LEU A O   
4630 C  CB  . LEU A 567 ? 0.293902 0.314782 0.249025 0.0422993   -0.0649799  -0.0448408  603  LEU A CB  
4631 C  CG  . LEU A 567 ? 0.310962 0.336169 0.284865 0.0355289   -0.0623643  -0.0463495  603  LEU A CG  
4632 C  CD1 . LEU A 567 ? 0.293735 0.310598 0.267119 0.0329181   -0.0559421  -0.0384141  603  LEU A CD1 
4633 C  CD2 . LEU A 567 ? 0.316248 0.342131 0.297577 0.0296506   -0.0611689  -0.0515895  603  LEU A CD2 
4634 N  N   . ARG A 568 ? 0.385485 0.40346  0.303481 0.0580278   -0.0747944  -0.0444986  604  ARG A N   
4635 C  CA  . ARG A 568 ? 0.395742 0.405769 0.291065 0.0625592   -0.0746938  -0.0409019  604  ARG A CA  
4636 C  C   . ARG A 568 ? 0.334682 0.353233 0.224857 0.0656975   -0.0810701  -0.0490045  604  ARG A C   
4637 O  O   . ARG A 568 ? 0.384767 0.400293 0.265325 0.0639021   -0.0779482  -0.0502082  604  ARG A O   
4638 C  CB  . ARG A 568 ? 0.410866 0.411673 0.290435 0.0697494   -0.0762598  -0.0327932  604  ARG A CB  
4639 C  CG  . ARG A 568 ? 0.44434  0.43265  0.322242 0.0652988   -0.0674329  -0.0243425  604  ARG A CG  
4640 C  CD  . ARG A 568 ? 0.596051 0.573974 0.459055 0.0727942   -0.069673   -0.0168737  604  ARG A CD  
4641 N  NE  . ARG A 568 ? 0.634353 0.597672 0.489861 0.0689851   -0.0611271  -0.00849552 604  ARG A NE  
4642 C  CZ  . ARG A 568 ? 0.715554 0.669945 0.569376 0.0713985   -0.0601603  -0.002746   604  ARG A CZ  
4643 N  NH1 . ARG A 568 ? 0.618762 0.576736 0.476438 0.0788666   -0.0674286  -0.00388349 604  ARG A NH1 
4644 N  NH2 . ARG A 568 ? 0.726516 0.668686 0.574922 0.0663269   -0.0518103  0.00347853  604  ARG A NH2 
4645 N  N   . THR A 569 ? 0.37792  0.408283 0.275476 0.0702057   -0.0898916  -0.055447   605  THR A N   
4646 C  CA  . THR A 569 ? 0.385606 0.425963 0.280044 0.0729938   -0.0968611  -0.0647504  605  THR A CA  
4647 C  C   . THR A 569 ? 0.36484  0.408731 0.270565 0.0649816   -0.0932139  -0.0722018  605  THR A C   
4648 O  O   . THR A 569 ? 0.349171 0.39342  0.244356 0.0656634   -0.0937732  -0.0764719  605  THR A O   
4649 C  CB  . THR A 569 ? 0.386317 0.441267 0.293332 0.0774272   -0.106405   -0.071852   605  THR A CB  
4650 O  OG1 . THR A 569 ? 0.402044 0.451252 0.297803 0.0854816   -0.109143   -0.0641205  605  THR A OG1 
4651 C  CG2 . THR A 569 ? 0.37931  0.445883 0.282932 0.0809499   -0.11483    -0.0823382  605  THR A CG2 
4652 N  N   . GLU A 570 ? 0.345238 0.391398 0.272001 0.0577314   -0.089679   -0.0739043  606  GLU A N   
4653 C  CA  . GLU A 570 ? 0.355854 0.403106 0.294788 0.0502663   -0.0863422  -0.0801807  606  GLU A CA  
4654 C  C   . GLU A 570 ? 0.336893 0.373248 0.264151 0.0482467   -0.0789424  -0.0759357  606  GLU A C   
4655 O  O   . GLU A 570 ? 0.336635 0.374518 0.260912 0.0474711   -0.0791371  -0.0824278  606  GLU A O   
4656 C  CB  . GLU A 570 ? 0.38003  0.428718 0.340436 0.0432776   -0.0832518  -0.0799733  606  GLU A CB  
4657 C  CG  . GLU A 570 ? 0.364992 0.412216 0.338374 0.0355655   -0.0799166  -0.0854407  606  GLU A CG  
4658 C  CD  . GLU A 570 ? 0.423136 0.479307 0.405265 0.0338528   -0.0852787  -0.097699   606  GLU A CD  
4659 O  OE1 . GLU A 570 ? 0.373805 0.44066  0.354245 0.0383983   -0.0927123  -0.103758   606  GLU A OE1 
4660 O  OE2 . GLU A 570 ? 0.45347  0.505426 0.443273 0.0284154   -0.0823321  -0.101755   606  GLU A OE2 
4661 N  N   . ASN A 571 ? 0.337097 0.363371 0.258062 0.0474474   -0.0724117  -0.0660063  607  ASN A N   
4662 C  CA  . ASN A 571 ? 0.324826 0.343    0.238413 0.0446168   -0.0649572  -0.0631476  607  ASN A CA  
4663 C  C   . ASN A 571 ? 0.368097 0.385087 0.26029  0.0492881   -0.0655068  -0.0639708  607  ASN A C   
4664 O  O   . ASN A 571 ? 0.391304 0.40727  0.27928  0.0473699   -0.0615268  -0.0674622  607  ASN A O   
4665 C  CB  . ASN A 571 ? 0.31117  0.320227 0.22368  0.0424938   -0.0583439  -0.053056   607  ASN A CB  
4666 C  CG  . ASN A 571 ? 0.297393 0.306362 0.229073 0.0367581   -0.0558498  -0.052249   607  ASN A CG  
4667 O  OD1 . ASN A 571 ? 0.316796 0.329808 0.2619   0.0331221   -0.0570511  -0.0586736  607  ASN A OD1 
4668 N  ND2 . ASN A 571 ? 0.288824 0.292563 0.221419 0.0358024   -0.0524495  -0.0445458  607  ASN A ND2 
4669 N  N   . GLU A 572 ? 0.394508 0.411776 0.27281  0.0558205   -0.0706148  -0.0609668  608  GLU A N   
4670 C  CA  . GLU A 572 ? 0.463244 0.47861  0.318209 0.0608479   -0.0717744  -0.0607026  608  GLU A CA  
4671 C  C   . GLU A 572 ? 0.43084  0.456433 0.286513 0.0618208   -0.0769631  -0.0726792  608  GLU A C   
4672 O  O   . GLU A 572 ? 0.422338 0.446866 0.264234 0.0621449   -0.0740473  -0.0751605  608  GLU A O   
4673 C  CB  . GLU A 572 ? 0.527241 0.537118 0.366196 0.0679196   -0.0756079  -0.0525594  608  GLU A CB  
4674 C  CG  . GLU A 572 ? 0.697532 0.705194 0.510155 0.0739611   -0.0782451  -0.0519724  608  GLU A CG  
4675 C  CD  . GLU A 572 ? 0.796851 0.80278  0.594549 0.0833517   -0.0866596  -0.0477706  608  GLU A CD  
4676 O  OE1 . GLU A 572 ? 0.910563 0.90472  0.701174 0.0848099   -0.083634   -0.0374264  608  GLU A OE1 
4677 O  OE2 . GLU A 572 ? 0.664842 0.680638 0.458439 0.0893543   -0.0962941  -0.0548152  608  GLU A OE2 
4678 N  N   . LEU A 573 ? 0.41256  0.448538 0.285564 0.0614474   -0.0839645  -0.0809985  609  LEU A N   
4679 C  CA  . LEU A 573 ? 0.448984 0.495131 0.324711 0.0620423   -0.0896814  -0.0935031  609  LEU A CA  
4680 C  C   . LEU A 573 ? 0.442161 0.486252 0.323655 0.0563572   -0.083409   -0.0990842  609  LEU A C   
4681 O  O   . LEU A 573 ? 0.417857 0.466074 0.291315 0.0577504   -0.0849275  -0.107227   609  LEU A O   
4682 C  CB  . LEU A 573 ? 0.474494 0.528979 0.373238 0.0598303   -0.0949459  -0.0980312  609  LEU A CB  
4683 C  CG  . LEU A 573 ? 0.45418  0.520369 0.367818 0.0574617   -0.100985   -0.111904   609  LEU A CG  
4684 C  CD1 . LEU A 573 ? 0.58505  0.657266 0.479528 0.0648051   -0.107843   -0.116873   609  LEU A CD1 
4685 C  CD2 . LEU A 573 ? 0.443159 0.517419 0.372096 0.0577616   -0.106272   -0.112398   609  LEU A CD2 
4686 N  N   . HIS A 574 ? 0.414058 0.451449 0.308557 0.0505315   -0.0763089  -0.0944947  610  HIS A N   
4687 C  CA  . HIS A 574 ? 0.386603 0.421171 0.289244 0.0457385   -0.0705946  -0.0989446  610  HIS A CA  
4688 C  C   . HIS A 574 ? 0.379449 0.407193 0.267265 0.045933    -0.0623703  -0.0931984  610  HIS A C   
4689 O  O   . HIS A 574 ? 0.429974 0.45625  0.3234   0.0430193   -0.0574831  -0.0970919  610  HIS A O   
4690 C  CB  . HIS A 574 ? 0.396019 0.426849 0.32028  0.0397752   -0.0677967  -0.0967229  610  HIS A CB  
4691 C  CG  . HIS A 574 ? 0.442356 0.480038 0.382863 0.0378427   -0.0743707  -0.103382   610  HIS A CG  
4692 N  ND1 . HIS A 574 ? 0.483491 0.526465 0.431516 0.0364539   -0.0782516  -0.115475   610  HIS A ND1 
4693 C  CD2 . HIS A 574 ? 0.432788 0.474046 0.383559 0.0368711   -0.0777039  -0.100991   610  HIS A CD2 
4694 C  CE1 . HIS A 574 ? 0.47478  0.524415 0.436939 0.0342897   -0.083706   -0.119983   610  HIS A CE1 
4695 N  NE2 . HIS A 574 ? 0.43174  0.480914 0.396264 0.034419    -0.0831842  -0.11137    610  HIS A NE2 
4696 N  N   . GLY A 575 ? 0.417138 0.440092 0.287957 0.0488909   -0.0603586  -0.0836833  611  GLY A N   
4697 C  CA  . GLY A 575 ? 0.395176 0.411346 0.252807 0.0477276   -0.0514537  -0.0775074  611  GLY A CA  
4698 C  C   . GLY A 575 ? 0.423126 0.433462 0.293465 0.0425847   -0.0443251  -0.071679   611  GLY A C   
4699 O  O   . GLY A 575 ? 0.401601 0.409604 0.268511 0.0401926   -0.0367109  -0.0708571  611  GLY A O   
4700 N  N   . GLU A 576 ? 0.40925  0.417856 0.293686 0.0408888   -0.0464148  -0.0675608  612  GLU A N   
4701 C  CA  . GLU A 576 ? 0.396185 0.400165 0.292356 0.036206    -0.0402443  -0.0632389  612  GLU A CA  
4702 C  C   . GLU A 576 ? 0.473379 0.470951 0.355726 0.0356001   -0.0329382  -0.0549928  612  GLU A C   
4703 O  O   . GLU A 576 ? 0.516049 0.509844 0.383131 0.0385775   -0.033877   -0.0492738  612  GLU A O   
4704 C  CB  . GLU A 576 ? 0.380827 0.383286 0.290657 0.0344634   -0.0426948  -0.0587265  612  GLU A CB  
4705 C  CG  . GLU A 576 ? 0.363382 0.371861 0.288227 0.0336906   -0.0491784  -0.0663354  612  GLU A CG  
4706 C  CD  . GLU A 576 ? 0.370627 0.380213 0.307159 0.0308      -0.0483903  -0.0743313  612  GLU A CD  
4707 O  OE1 . GLU A 576 ? 0.351611 0.358041 0.287544 0.0295422   -0.0427327  -0.0740569  612  GLU A OE1 
4708 O  OE2 . GLU A 576 ? 0.405932 0.419621 0.353209 0.0297756   -0.0535575  -0.0814117  612  GLU A OE2 
4709 N  N   . LYS A 577 ? 0.412497 0.40861  0.300286 0.0318504   -0.0258835  -0.0544851  613  LYS A N   
4710 C  CA  . LYS A 577 ? 0.433487 0.423711 0.311835 0.0298174   -0.0186404  -0.0465729  613  LYS A CA  
4711 C  C   . LYS A 577 ? 0.433162 0.419703 0.324261 0.0270718   -0.0180082  -0.0408289  613  LYS A C   
4712 O  O   . LYS A 577 ? 0.508904 0.49791  0.41574  0.0246352   -0.0174432  -0.0438027  613  LYS A O   
4713 C  CB  . LYS A 577 ? 0.478037 0.47062  0.355631 0.0269423   -0.0106616  -0.0497306  613  LYS A CB  
4714 C  CG  . LYS A 577 ? 0.71436  0.709009 0.572836 0.0287598   -0.00791255 -0.0529654  613  LYS A CG  
4715 C  CD  . LYS A 577 ? 0.886634 0.882782 0.743817 0.0246524   0.00222741  -0.0533418  613  LYS A CD  
4716 C  CE  . LYS A 577 ? 1.01285  1.00346  0.876315 0.020706    0.00636957  -0.0452652  613  LYS A CE  
4717 N  NZ  . LYS A 577 ? 0.982173 0.977823 0.864046 0.0174946   0.0100926   -0.0488007  613  LYS A NZ  
4718 N  N   . LEU A 578 ? 0.386155 0.366307 0.269612 0.02778     -0.0180288  -0.0328364  614  LEU A N   
4719 C  CA  . LEU A 578 ? 0.394752 0.371843 0.289324 0.025633    -0.0180279  -0.0279364  614  LEU A CA  
4720 C  C   . LEU A 578 ? 0.446529 0.421693 0.34532  0.0208961   -0.0104491  -0.0256061  614  LEU A C   
4721 O  O   . LEU A 578 ? 0.498179 0.47079  0.385914 0.019373    -0.00436937 -0.0238564  614  LEU A O   
4722 C  CB  . LEU A 578 ? 0.370618 0.341247 0.255313 0.0284498   -0.020183   -0.0211031  614  LEU A CB  
4723 C  CG  . LEU A 578 ? 0.43911  0.412424 0.319195 0.0341194   -0.0283431  -0.023002   614  LEU A CG  
4724 C  CD1 . LEU A 578 ? 0.449108 0.414986 0.321456 0.0371487   -0.0297289  -0.0157443  614  LEU A CD1 
4725 C  CD2 . LEU A 578 ? 0.406176 0.388109 0.303321 0.0340791   -0.0343501  -0.0294837  614  LEU A CD2 
4726 N  N   . GLY A 579 ? 0.398258 0.374867 0.312618 0.01836     -0.0106972  -0.0255404  615  GLY A N   
4727 C  CA  . GLY A 579 ? 0.31758  0.294383 0.237781 0.0143742   -0.00471475 -0.0245687  615  GLY A CA  
4728 C  C   . GLY A 579 ? 0.337071 0.320482 0.267276 0.0139375   -0.00404822 -0.031656   615  GLY A C   
4729 O  O   . GLY A 579 ? 0.310424 0.296888 0.243644 0.016283    -0.00819288 -0.0370541  615  GLY A O   
4730 N  N   . TRP A 580 ? 0.31596  0.301818 0.251244 0.0111508   0.00120319  -0.0323684  616  TRP A N   
4731 C  CA  . TRP A 580 ? 0.395264 0.387294 0.342654 0.0116546   0.00100284  -0.0390729  616  TRP A CA  
4732 C  C   . TRP A 580 ? 0.396433 0.393072 0.343182 0.00903856  0.00853171  -0.0409423  616  TRP A C   
4733 O  O   . TRP A 580 ? 0.518545 0.518147 0.475997 0.00743284  0.00980505  -0.0412238  616  TRP A O   
4734 C  CB  . TRP A 580 ? 0.342384 0.333772 0.304161 0.0113004   -0.00281237 -0.0377569  616  TRP A CB  
4735 C  CG  . TRP A 580 ? 0.318533 0.30662  0.279616 0.00849186  -0.00102135 -0.0309819  616  TRP A CG  
4736 C  CD1 . TRP A 580 ? 0.326607 0.316818 0.291356 0.00557946  0.00336366  -0.0297608  616  TRP A CD1 
4737 C  CD2 . TRP A 580 ? 0.290826 0.273546 0.248482 0.00850357  -0.00410665 -0.0255051  616  TRP A CD2 
4738 N  NE1 . TRP A 580 ? 0.307498 0.293068 0.270617 0.00366049  0.00314703  -0.0238522  616  TRP A NE1 
4739 C  CE2 . TRP A 580 ? 0.270939 0.251872 0.229813 0.00565854  -0.00131157 -0.0211436  616  TRP A CE2 
4740 C  CE3 . TRP A 580 ? 0.283164 0.263643 0.238294 0.0106681   -0.00907765 -0.0248309  616  TRP A CE3 
4741 C  CZ2 . TRP A 580 ? 0.259838 0.23608  0.21633  0.00530906  -0.00300587 -0.016131   616  TRP A CZ2 
4742 C  CZ3 . TRP A 580 ? 0.305036 0.281962 0.258985 0.0103086   -0.0107368  -0.0197885  616  TRP A CZ3 
4743 C  CH2 . TRP A 580 ? 0.276846 0.251417 0.231394 0.00784759  -0.00771729 -0.0155368  616  TRP A CH2 
4744 N  N   . PRO A 581 ? 0.545426 0.543195 0.479369 0.00836758  0.0137129   -0.0422975  617  PRO A N   
4745 C  CA  . PRO A 581 ? 0.613208 0.616643 0.547217 0.0048494   0.0220925   -0.0447508  617  PRO A CA  
4746 C  C   . PRO A 581 ? 0.70349  0.716729 0.653225 0.00650486  0.021904    -0.053447   617  PRO A C   
4747 O  O   . PRO A 581 ? 0.673033 0.693212 0.629766 0.0038842   0.0273696   -0.0562051  617  PRO A O   
4748 C  CB  . PRO A 581 ? 0.611047 0.612644 0.525957 0.00474375  0.0262823   -0.0446245  617  PRO A CB  
4749 C  CG  . PRO A 581 ? 0.574619 0.5752   0.486879 0.010005    0.018451    -0.0476078  617  PRO A CG  
4750 C  CD  . PRO A 581 ? 0.512806 0.50734  0.431538 0.010973    0.0116816   -0.0420806  617  PRO A CD  
4751 N  N   . GLN A 582 ? 0.705151 0.718888 0.661445 0.0109438   0.0154055   -0.0581456  618  GLN A N   
4752 C  CA  . GLN A 582 ? 0.802628 0.823628 0.773884 0.0135776   0.0143921   -0.0663282  618  GLN A CA  
4753 C  C   . GLN A 582 ? 0.638352 0.659136 0.624266 0.0135916   0.0111474   -0.0638642  618  GLN A C   
4754 O  O   . GLN A 582 ? 0.71475  0.73615  0.712382 0.0173877   0.00621089  -0.0681967  618  GLN A O   
4755 C  CB  . GLN A 582 ? 0.804167 0.824441 0.777936 0.0181242   0.00889189  -0.0729078  618  GLN A CB  
4756 C  CG  . GLN A 582 ? 0.733253 0.756771 0.694449 0.0189958   0.0119692   -0.0783128  618  GLN A CG  
4757 C  CD  . GLN A 582 ? 0.855019 0.886995 0.81122  0.0165044   0.021422    -0.0816353  618  GLN A CD  
4758 O  OE1 . GLN A 582 ? 0.87183  0.912665 0.839611 0.0174628   0.0244999   -0.0889824  618  GLN A OE1 
4759 N  NE2 . GLN A 582 ? 0.815508 0.844586 0.753899 0.0133356   0.0262052   -0.0762408  618  GLN A NE2 
4859 ZN ZN  . ZN  C .   ? 0.32416  0.345893 0.287678 -0.0332842  0.0158535   0.00454508  701  ZN  A ZN  
4860 C  C1  . NAG D .   ? 1.31074  1.12851  0.847788 -0.0918433  0.0348408   0.197432    702  NAG A C1  
4861 C  C2  . NAG D .   ? 1.36646  1.19077  0.885815 -0.105002   0.0508886   0.199501    702  NAG A C2  
4862 C  C3  . NAG D .   ? 1.38469  1.19438  0.862187 -0.104104   0.0493053   0.213372    702  NAG A C3  
4863 C  C4  . NAG D .   ? 1.42238  1.23906  0.889475 -0.0890322  0.033217    0.210387    702  NAG A C4  
4864 C  C5  . NAG D .   ? 1.44657  1.25314  0.931719 -0.0769231  0.0178799   0.210287    702  NAG A C5  
4865 C  C6  . NAG D .   ? 1.46386  1.27894  0.943314 -0.0618865  0.00133984  0.205976    702  NAG A C6  
4866 C  C7  . NAG D .   ? 1.1477   0.988795 0.696631 -0.128177   0.0778155   0.189848    702  NAG A C7  
4867 C  C8  . NAG D .   ? 1.10555  0.939443 0.655811 -0.144225   0.0938264   0.194727    702  NAG A C8  
4868 N  N2  . NAG D .   ? 1.26788  1.08688  0.798763 -0.118992   0.0651898   0.20132     702  NAG A N2  
4869 O  O3  . NAG D .   ? 1.30008  1.12023  0.762462 -0.116072   0.064702    0.212938    702  NAG A O3  
4870 O  O4  . NAG D .   ? 1.47997  1.28471  0.906717 -0.0875904  0.0311648   0.222698    702  NAG A O4  
4871 O  O5  . NAG D .   ? 1.30566  1.12633  0.829401 -0.0785218  0.0204427   0.197173    702  NAG A O5  
4872 O  O6  . NAG D .   ? 1.45925  1.30209  0.941106 -0.0622719  0.00410632  0.192674    702  NAG A O6  
4873 O  O7  . NAG D .   ? 1.14595  1.01179  0.710216 -0.123623   0.0762381   0.17572     702  NAG A O7  
4874 CL CL  . CL  E .   ? 0.308719 0.271766 0.319037 0.0126787   -0.0397321  0.0025493   703  CL  A CL  
4875 CL CL  . CL  F .   ? 0.322345 0.316121 0.284999 -0.0173096  0.00076217  -0.0143305  704  CL  A CL  
4906 O  O   . HOH H .   ? 0.61857  0.58523  0.478655 -0.0483426  0.00607214  0.060369    801  HOH A O   
4907 O  O   . HOH H .   ? 0.556954 0.590737 0.47552  -0.0143308  -0.0373499  -0.00918554 802  HOH A O   
4908 O  O   . HOH H .   ? 0.543694 0.722062 0.48893  -0.0293938  -0.0907261  -0.140997   803  HOH A O   
4909 O  O   . HOH H .   ? 0.584697 0.410903 0.465307 -0.0106809  -0.0479316  0.0986194   804  HOH A O   
4910 O  O   . HOH H .   ? 0.60959  0.7446   0.296648 -0.0248461  -0.0369952  -0.0678863  805  HOH A O   
4911 O  O   . HOH H .   ? 0.537154 0.552597 0.636583 -0.0877017  0.00456492  -0.0317589  806  HOH A O   
4912 O  O   . HOH H .   ? 0.366304 0.460188 0.361385 0.0799041   -0.109493   -0.0743925  807  HOH A O   
4913 O  O   . HOH H .   ? 0.434597 0.267289 0.514684 0.071684    -0.0814944  -0.0484123  808  HOH A O   
4914 O  O   . HOH H .   ? 0.59271  0.543684 0.658209 0.00273607  -0.0625728  -0.140748   809  HOH A O   
4915 O  O   . HOH H .   ? 0.512143 0.480293 0.583356 0.0723032   -0.0791647  -0.030167   810  HOH A O   
4916 O  O   . HOH H .   ? 0.486618 0.522951 0.567862 -0.018628   -0.0666687  -0.107585   811  HOH A O   
4917 O  O   . HOH H .   ? 0.540288 0.615076 0.4669   0.0906848   -0.12124    -0.0751132  812  HOH A O   
4918 O  O   . HOH H .   ? 0.551809 0.80618  0.557839 -0.125842   0.166046    -0.0721959  813  HOH A O   
4919 O  O   . HOH H .   ? 0.47736  0.440609 0.497567 -0.035623   -0.0145359  0.00521743  814  HOH A O   
4920 O  O   . HOH H .   ? 0.348    0.42642  0.434209 0.0342246   -0.055223   -0.050607   815  HOH A O   
4921 O  O   . HOH H .   ? 0.421717 0.423752 0.345284 0.0282135   -0.0280689  -0.0685619  816  HOH A O   
4922 O  O   . HOH H .   ? 0.311001 0.736946 0.634694 -0.0648896  0.0775694   -0.182943   817  HOH A O   
4923 O  O   . HOH H .   ? 0.509541 0.744962 0.512662 -0.0782927  0.132671    -0.0888631  818  HOH A O   
4924 O  O   . HOH H .   ? 0.377413 0.45325  0.288435 -0.0352787  0.0426615   -0.0408358  819  HOH A O   
4925 O  O   . HOH H .   ? 0.524701 0.397525 0.602184 0.0553316   -0.0664049  -0.0597149  820  HOH A O   
4926 O  O   . HOH H .   ? 0.493227 0.577898 0.471802 0.0495961   -0.104931   -0.105126   821  HOH A O   
4927 O  O   . HOH H .   ? 0.349643 0.262438 0.39796  -0.0182474  -0.0391056  -0.0322523  822  HOH A O   
4928 O  O   . HOH H .   ? 0.47723  0.465074 0.504743 0.0370261   -0.0289446  -0.112677   823  HOH A O   
4929 O  O   . HOH H .   ? 0.507351 0.480563 0.476559 0.104704    -0.0624171  -0.0215938  824  HOH A O   
4930 O  O   . HOH H .   ? 0.557338 0.759775 0.429618 -0.138032   0.174345    -0.0346623  825  HOH A O   
4931 O  O   . HOH H .   ? 0.285088 0.407669 0.387364 0.00638869  -0.02459    -0.0623663  826  HOH A O   
4932 O  O   . HOH H .   ? 0.637649 0.613374 0.630554 0.0332659   0.0181899   -0.0759944  827  HOH A O   
4933 O  O   . HOH H .   ? 0.425633 0.418996 0.404723 0.0794504   -0.126156   0.0165117   828  HOH A O   
4934 O  O   . HOH H .   ? 0.480065 0.705285 0.509695 -0.12756    0.147456    -0.0572305  829  HOH A O   
4935 O  O   . HOH H .   ? 0.610698 0.374815 0.652932 -0.0330259  -0.043781   0.00164558  830  HOH A O   
4936 O  O   . HOH H .   ? 0.638976 0.636932 0.522028 9.256e-05   -0.0556699  0.0317931   831  HOH A O   
4937 O  O   . HOH H .   ? 0.26765  0.271791 0.283628 0.0872326   -0.0374924  -0.0422719  832  HOH A O   
4938 O  O   . HOH H .   ? 0.286038 0.482394 0.467605 0.144088    -0.0422545  -0.146365   833  HOH A O   
4939 O  O   . HOH H .   ? 0.506352 0.263864 0.472683 -0.0628401  -0.0188766  0.0700848   834  HOH A O   
4940 O  O   . HOH H .   ? 0.454914 0.502597 0.312327 0.0797656   -0.104999   -0.079306   835  HOH A O   
4941 O  O   . HOH H .   ? 0.257446 0.273119 0.220951 -0.00493015 -0.040394   0.00029165  836  HOH A O   
4942 O  O   . HOH H .   ? 0.437637 0.346696 0.313711 0.0524872   -0.0300639  0.0175892   837  HOH A O   
4943 O  O   . HOH H .   ? 0.384206 0.616528 0.576042 0.0115887   -0.0824822  -0.139807   838  HOH A O   
4944 O  O   . HOH H .   ? 0.307113 0.316126 0.325479 -0.0583745  0.0122446   -0.0595495  839  HOH A O   
4945 O  O   . HOH H .   ? 0.587617 0.440605 0.454657 0.0423408   -0.0968904  0.0937052   840  HOH A O   
4946 O  O   . HOH H .   ? 0.465482 0.627987 0.301865 -0.0267755  0.0725065   -0.183449   841  HOH A O   
4947 O  O   . HOH H .   ? 0.385073 0.530258 0.556374 -0.0427203  -0.0536973  -0.118246   842  HOH A O   
4948 O  O   . HOH H .   ? 0.34797  0.433811 0.387819 0.06366     -0.114894   -0.0318055  843  HOH A O   
4949 O  O   . HOH H .   ? 0.259335 0.278311 0.216702 -0.0205328  0.0117832   -0.013095   844  HOH A O   
4950 O  O   . HOH H .   ? 0.265456 0.256991 0.237783 -0.0214472  -0.00378245 -0.0165171  845  HOH A O   
4951 O  O   . HOH H .   ? 0.328319 0.283527 0.358814 -0.0322863  -0.0216915  -0.00482736 846  HOH A O   
4952 O  O   . HOH H .   ? 0.527733 0.414016 0.440127 0.0539329   -0.0200572  0.0111848   847  HOH A O   
4953 O  O   . HOH H .   ? 0.476802 0.333498 0.423379 0.0419499   0.00378652  -0.0255248  848  HOH A O   
4954 O  O   . HOH H .   ? 0.724221 0.881931 0.56993  -0.0490884  0.0885796   -0.0937841  849  HOH A O   
4955 O  O   . HOH H .   ? 0.253019 0.250572 0.209632 0.0232141   -0.0372195  -0.0632409  850  HOH A O   
4956 O  O   . HOH H .   ? 0.598442 0.704295 0.434934 -0.111975   0.116675    0.00999824  851  HOH A O   
4957 O  O   . HOH H .   ? 0.195724 0.338843 0.304202 0.0155081   -0.00431184 -0.0707651  852  HOH A O   
4958 O  O   . HOH H .   ? 0.419643 0.299876 0.375658 0.0107001   0.0156224   -0.0381929  853  HOH A O   
4959 O  O   . HOH H .   ? 0.280156 0.612585 0.583663 -0.0615161  0.00120421  -0.161324   854  HOH A O   
4960 O  O   . HOH H .   ? 0.564666 0.588877 0.445148 0.0933908   -0.10363    -0.0427989  855  HOH A O   
4961 O  O   . HOH H .   ? 0.202673 0.306564 0.267188 -0.0134792  -0.03993    -0.0631423  856  HOH A O   
4962 O  O   . HOH H .   ? 0.882037 0.848757 0.847094 -0.0495399  0.0310205   -0.351707   857  HOH A O   
4963 O  O   . HOH H .   ? 0.626835 0.619155 0.534216 0.0199101   -0.00394174 -0.0466036  858  HOH A O   
4964 O  O   . HOH H .   ? 0.264743 0.245063 0.242397 -0.0128664  -0.00571228 -0.00176817 859  HOH A O   
4965 O  O   . HOH H .   ? 0.552491 0.778103 0.618998 -0.143738   0.146714    -0.0555394  860  HOH A O   
4966 O  O   . HOH H .   ? 0.344142 0.406365 0.30078  -0.0274864  -0.0350682  -0.0561235  861  HOH A O   
4967 O  O   . HOH H .   ? 0.593656 0.64001  0.614889 0.108474    -0.0748432  -0.0477525  862  HOH A O   
4968 O  O   . HOH H .   ? 0.583463 0.590935 0.38895  0.0612077   -0.0588661  -0.0619149  863  HOH A O   
4969 O  O   . HOH H .   ? 0.410861 0.526533 0.326358 -0.0390684  0.0668677   -0.063788   864  HOH A O   
4970 O  O   . HOH H .   ? 0.470603 0.458373 0.343062 0.0507877   -0.0529129  -0.031815   865  HOH A O   
4971 O  O   . HOH H .   ? 0.356916 0.372361 0.361455 -0.0099029  0.0158735   -0.0330499  866  HOH A O   
4972 O  O   . HOH H .   ? 0.365492 0.443877 0.330945 0.0598749   -0.104734   -0.088913   867  HOH A O   
4973 O  O   . HOH H .   ? 0.519661 0.445529 0.391793 -0.0114238  -0.0410471  0.0713434   868  HOH A O   
4974 O  O   . HOH H .   ? 0.456234 0.561682 0.513394 0.0174571   -0.10044    -0.130402   869  HOH A O   
4975 O  O   . HOH H .   ? 0.296745 0.486633 0.34607  -0.0721835  0.0945882   -0.0629117  870  HOH A O   
4976 O  O   . HOH H .   ? 0.766114 0.807907 0.390459 -0.0641135  0.0328481   0.0516641   871  HOH A O   
4977 O  O   . HOH H .   ? 0.327959 0.348656 0.286986 0.0294868   -0.0616857  -0.0780054  872  HOH A O   
4978 O  O   . HOH H .   ? 0.380826 0.561321 0.507286 -0.0815104  0.0611268   -0.0623581  873  HOH A O   
4979 O  O   . HOH H .   ? 0.359901 0.513703 0.346774 -0.00637791 0.078453    -0.123447   874  HOH A O   
4980 O  O   . HOH H .   ? 0.455492 0.351007 0.498979 -0.0285317  -0.0344236  -0.0149644  875  HOH A O   
4981 O  O   . HOH H .   ? 0.257824 0.320639 0.306432 -0.0202829  0.00196425  -0.0253449  876  HOH A O   
4982 O  O   . HOH H .   ? 0.340896 0.403092 0.394254 -0.0654892  0.00191492  -0.0843673  877  HOH A O   
4983 O  O   . HOH H .   ? 0.359832 0.300264 0.328943 0.0042135   0.0179176   -0.0612616  878  HOH A O   
4984 O  O   . HOH H .   ? 0.415578 0.34775  0.480776 0.0445775   -0.0501245  -0.0607795  879  HOH A O   
4985 O  O   . HOH H .   ? 0.59475  0.578503 0.567364 0.0059699   0.0218667   -0.0719313  880  HOH A O   
4986 O  O   . HOH H .   ? 0.335128 0.247717 0.3255   -0.03       -0.0221362  0.0310865   881  HOH A O   
4987 O  O   . HOH H .   ? 0.419686 0.439535 0.41673  -0.0166133  0.0047286   -0.00588457 882  HOH A O   
4988 O  O   . HOH H .   ? 0.316876 0.365738 0.376184 0.0104559   -0.00914574 -0.0505685  883  HOH A O   
4989 O  O   . HOH H .   ? 0.586193 0.687103 0.321096 -0.0901633  0.0934681   0.00658055  884  HOH A O   
4990 O  O   . HOH H .   ? 0.278391 0.321509 0.276999 0.0154165   0.0290483   -0.0744355  885  HOH A O   
4991 O  O   . HOH H .   ? 0.324194 0.354848 0.314317 0.0220283   -0.0694117  -0.0933382  886  HOH A O   
4992 O  O   . HOH H .   ? 0.629896 0.707346 0.319303 -0.0353964  -0.00889238 -0.00081963 887  HOH A O   
4993 O  O   . HOH H .   ? 0.586128 0.700518 0.527871 0.0645811   -0.151924   -0.02637    888  HOH A O   
4994 O  O   . HOH H .   ? 0.436511 0.660151 0.532026 0.00346173  0.0765169   -0.129482   889  HOH A O   
4995 O  O   . HOH H .   ? 0.564414 0.552657 0.504063 0.0683319   -0.0612662  -0.0148118  890  HOH A O   
4996 O  O   . HOH H .   ? 0.496166 0.583    0.352911 -0.0326528  -0.00290174 -0.0924725  891  HOH A O   
4997 O  O   . HOH H .   ? 0.555525 0.415758 0.426942 0.0248317   0.00186282  0.0282169   892  HOH A O   
4998 O  O   . HOH H .   ? 0.70154  0.878399 0.44981  -0.0518151  0.0798646   -0.117062   893  HOH A O   
4999 O  O   . HOH H .   ? 0.348628 0.279518 0.315078 -0.025181   0.0171601   -0.0409457  894  HOH A O   
5000 O  O   . HOH H .   ? 0.277131 0.289609 0.235437 -0.0119905  0.0171364   -0.0449478  895  HOH A O   
5001 O  O   . HOH H .   ? 0.299382 0.394574 0.347786 0.0737409   -0.0768045  -0.0614885  896  HOH A O   
5002 O  O   . HOH H .   ? 0.357277 0.428632 0.393384 -0.0775406  -0.0119578  -0.130633   897  HOH A O   
5003 O  O   . HOH H .   ? 0.2988   0.205635 0.304512 -0.040971   -0.0184219  0.0243131   898  HOH A O   
5004 O  O   . HOH H .   ? 0.213994 0.3601   0.330775 0.0261307   -0.0355134  -0.0757492  899  HOH A O   
5005 O  O   . HOH H .   ? 0.232715 0.162296 0.251825 -0.00642013 -0.0340624  -0.0031799  900  HOH A O   
5006 O  O   . HOH H .   ? 0.380851 0.641887 0.590369 0.0500206   -0.0413736  -0.130696   901  HOH A O   
5007 O  O   . HOH H .   ? 0.757445 0.800483 0.58591  0.0834185   -0.170406   0.0303206   902  HOH A O   
5008 O  O   . HOH H .   ? 0.279324 0.284235 0.26045  0.0310168   -0.0243726  -0.106818   903  HOH A O   
5009 O  O   . HOH H .   ? 0.447073 0.543963 0.598066 -0.0522341  -0.0477147  -0.105714   904  HOH A O   
5010 O  O   . HOH H .   ? 0.341616 0.358024 0.353716 0.0109772   -0.0608309  -0.0841551  905  HOH A O   
5011 O  O   . HOH H .   ? 0.27623  0.421592 0.321004 -0.0238601  -0.0648385  -0.0956718  906  HOH A O   
5012 O  O   . HOH H .   ? 0.634967 0.557616 0.511179 0.0683389   -0.126062   0.0694798   907  HOH A O   
5013 O  O   . HOH H .   ? 0.274575 0.253215 0.254454 0.0475242   -0.0271805  -0.0141407  908  HOH A O   
5014 O  O   . HOH H .   ? 0.495767 0.621804 0.346212 -0.0672241  0.0866292   -0.0380814  909  HOH A O   
5015 O  O   . HOH H .   ? 0.345828 0.444691 0.406731 -0.0489299  -0.0208037  -0.0869503  910  HOH A O   
5016 O  O   . HOH H .   ? 0.40187  0.336735 0.3595   -0.0208818  0.0162139   -0.00412249 911  HOH A O   
5017 O  O   . HOH H .   ? 0.516152 0.686179 0.721617 -0.189453   0.0959999   -0.0734584  912  HOH A O   
5018 O  O   . HOH H .   ? 0.357108 0.308174 0.272117 0.0431476   -0.0341287  0.00208448  913  HOH A O   
5019 O  O   . HOH H .   ? 0.682301 0.548977 0.596612 0.0213177   0.00397797  0.0106616   914  HOH A O   
5020 O  O   . HOH H .   ? 0.530173 0.527428 0.544628 0.0157646   -0.0595575  -0.123158   915  HOH A O   
5021 O  O   . HOH H .   ? 0.317349 0.29247  0.310735 -0.00031532 -0.0209074  -0.00632881 916  HOH A O   
5022 O  O   . HOH H .   ? 0.371633 0.274618 0.403949 -0.01732    -0.0358419  -0.00828248 917  HOH A O   
5023 O  O   . HOH H .   ? 0.217305 0.346339 0.271645 0.0047042   -0.0727777  -0.0669829  918  HOH A O   
5024 O  O   . HOH H .   ? 0.569694 0.737944 0.388994 -0.0411476  -0.0456396  -0.196586   919  HOH A O   
5025 O  O   . HOH H .   ? 0.578246 0.623775 0.530347 -0.0363893  -0.0173462  -0.0723243  920  HOH A O   
5026 O  O   . HOH H .   ? 0.387711 0.315408 0.325635 -0.0250927  -0.0223448  0.0519369   921  HOH A O   
5027 O  O   . HOH H .   ? 0.655095 0.862591 0.449054 -0.0350794  0.0956059   -0.19582    922  HOH A O   
5028 O  O   . HOH H .   ? 0.684295 0.823082 0.447796 -0.0619432  0.0769554   -0.0570565  923  HOH A O   
5029 O  O   . HOH H .   ? 0.702831 0.881448 0.59414  -0.0418556  0.10077     -0.114072   924  HOH A O   
5030 O  O   . HOH H .   ? 0.638002 0.603487 0.46859  -0.156853   0.111704    0.089509    925  HOH A O   
5031 O  O   . HOH H .   ? 0.391951 0.379609 0.387499 -0.0321474  0.0122795   -0.0210383  926  HOH A O   
5032 O  O   . HOH H .   ? 0.728771 0.493045 0.542093 -0.0109373  -0.0535417  0.137852    927  HOH A O   
5033 O  O   . HOH H .   ? 0.586471 0.790052 0.51717  -0.0734575  0.126503    -0.0802752  928  HOH A O   
5034 O  O   . HOH H .   ? 0.443491 0.543889 0.448663 0.0521376   -0.120014   -0.0317948  929  HOH A O   
5035 O  O   . HOH H .   ? 0.418704 0.603459 0.572198 0.01361     -0.0621023  -0.105849   930  HOH A O   
5036 O  O   . HOH H .   ? 0.370109 0.458741 0.42348  0.0583399   0.0388896   -0.135213   931  HOH A O   
5037 O  O   . HOH H .   ? 0.248167 0.263572 0.257134 -0.0424019  0.00117824  -0.0452396  932  HOH A O   
5038 O  O   . HOH H .   ? 0.415867 0.397335 0.422933 0.0204065   -0.0269993  -0.0632894  933  HOH A O   
5039 O  O   . HOH H .   ? 0.592733 0.444193 0.488883 0.0568181   -0.106609   0.0828919   934  HOH A O   
5040 O  O   . HOH H .   ? 0.349548 0.35091  0.337718 0.0215613   0.0263146   -0.0869308  935  HOH A O   
5041 O  O   . HOH H .   ? 0.277641 0.429587 0.298991 -0.0612059  0.0791171   -0.0489103  936  HOH A O   
5042 O  O   . HOH H .   ? 0.481832 0.360497 0.55837  -0.0740746  -0.0210783  -0.0249582  937  HOH A O   
5043 O  O   . HOH H .   ? 0.562357 0.555315 0.425589 0.046597    -0.0470023  -0.0429426  938  HOH A O   
5044 O  O   . HOH H .   ? 0.258274 0.200278 0.268973 0.00387473  -0.0356191  0.00273759  939  HOH A O   
5045 O  O   . HOH H .   ? 0.591272 0.759818 0.352053 -0.0219846  -0.0693492  -0.126422   940  HOH A O   
5046 O  O   . HOH H .   ? 0.415137 0.423824 0.445154 0.111283    -0.0447417  -0.0556815  941  HOH A O   
5047 O  O   . HOH H .   ? 0.712854 0.905286 0.483023 -0.0317267  0.0517356   -0.256517   942  HOH A O   
5048 O  O   . HOH H .   ? 0.520029 0.691208 0.230506 -0.0367444  0.00090163  -0.145965   943  HOH A O   
5049 O  O   . HOH H .   ? 0.464791 0.592371 0.345767 -0.0489501  0.0759462   -0.0627324  944  HOH A O   
5050 O  O   . HOH H .   ? 0.523802 0.617079 0.40695  -0.0250615  0.0397632   -0.124846   945  HOH A O   
5051 O  O   . HOH H .   ? 0.500442 0.376693 0.440292 0.0316307   0.00176321  -0.00949227 946  HOH A O   
5052 O  O   . HOH H .   ? 0.414175 0.37     0.383572 -0.0304808  -0.0113842  0.0322075   947  HOH A O   
5053 O  O   . HOH H .   ? 0.273469 0.382112 0.330427 0.00240601  -0.0591195  -0.0578925  948  HOH A O   
5054 O  O   . HOH H .   ? 0.320392 0.381429 0.320637 -0.0282691  0.0274773   -0.0199752  949  HOH A O   
5055 O  O   . HOH H .   ? 0.392843 0.357225 0.360119 -0.00296532 0.0158717   -0.0525144  950  HOH A O   
5056 O  O   . HOH H .   ? 0.438198 0.393673 0.418931 -0.0443698  0.0161779   -0.0545214  951  HOH A O   
5057 O  O   . HOH H .   ? 0.521378 0.389252 0.406388 -0.0152927  -0.0404956  0.0871126   952  HOH A O   
5058 O  O   . HOH H .   ? 0.569661 0.600773 0.435062 0.0578135   -0.134565   0.02664     953  HOH A O   
5059 O  O   . HOH H .   ? 0.57999  0.528184 0.535145 -0.0222078  -0.0202812  0.0383801   954  HOH A O   
5060 O  O   . HOH H .   ? 0.390494 0.339985 0.318064 0.0934222   -0.0618056  -0.00460259 955  HOH A O   
5061 O  O   . HOH H .   ? 0.493436 0.589344 0.316141 -0.0325729  -0.00432019 -0.0775738  956  HOH A O   
5062 O  O   . HOH H .   ? 0.523089 0.663533 0.394518 -0.107468   0.124636    -0.0149506  957  HOH A O   
5063 O  O   . HOH H .   ? 0.705065 0.617488 0.65628  -0.0600011  0.00254602  0.0564128   958  HOH A O   
5064 O  O   . HOH H .   ? 0.340398 0.300874 0.35516  0.0464331   -0.0761147  0.00738124  959  HOH A O   
5065 O  O   . HOH H .   ? 0.527788 0.695926 0.362791 -0.0316342  0.0797983   -0.160645   960  HOH A O   
5066 O  O   . HOH H .   ? 0.784647 0.750215 0.402061 -0.045899   -0.00503331 0.102255    961  HOH A O   
5067 O  O   . HOH H .   ? 0.308799 0.408565 0.355587 -0.0494158  -0.0278277  -0.0930647  962  HOH A O   
5068 O  O   . HOH H .   ? 0.381432 0.408255 0.335873 -0.0163337  0.0189312   -0.0359231  963  HOH A O   
5069 O  O   . HOH H .   ? 0.720218 0.780813 0.467976 0.0136569   -0.0953287  0.0146495   964  HOH A O   
5070 O  O   . HOH H .   ? 0.293318 0.274707 0.232948 0.0188424   -0.0216561  -0.0288788  965  HOH A O   
5071 O  O   . HOH H .   ? 0.466657 0.490107 0.491585 -0.0251438  -0.00316146 -0.00799087 966  HOH A O   
5072 O  O   . HOH H .   ? 0.49988  0.451723 0.466167 0.0756629   -0.0368425  -0.014857   967  HOH A O   
5073 O  O   . HOH H .   ? 0.843264 0.618967 0.675662 0.0445465   -0.101494   0.12456     968  HOH A O   
5074 O  O   . HOH H .   ? 0.347999 0.30509  0.340521 0.00708312  -0.040842   0.0159315   969  HOH A O   
5075 O  O   . HOH H .   ? 0.565309 0.645712 0.424868 -0.0245481  -0.0343939  -0.0548005  970  HOH A O   
5076 O  O   . HOH H .   ? 0.530397 0.468461 0.468904 -0.0177474  0.0226505   0.00263166  971  HOH A O   
5077 O  O   . HOH H .   ? 0.588376 0.465719 0.516774 0.0287839   -0.00019022 0.00225624  972  HOH A O   
5078 O  O   . HOH H .   ? 0.678117 0.827779 0.437487 -0.108671   0.133939    -0.0166642  973  HOH A O   
5079 O  O   . HOH H .   ? 0.527741 0.427529 0.491652 0.00777867  0.0175374   -0.0530189  974  HOH A O   
5080 O  O   . HOH H .   ? 0.272249 0.227136 0.246238 0.0180389   0.00393676  -0.0250618  975  HOH A O   
5081 O  O   . HOH H .   ? 0.399659 0.409139 0.343905 -0.0270385  0.00455841  0.00655978  976  HOH A O   
5082 O  O   . HOH H .   ? 0.558434 0.612187 0.434172 -0.0462709  0.0337368   -0.00443164 977  HOH A O   
5083 O  O   . HOH H .   ? 0.448159 0.370124 0.513316 -0.0714696  -0.0134     -0.0141773  978  HOH A O   
5084 O  O   . HOH H .   ? 0.548318 0.743397 0.668407 0.0850662   -0.14505    -0.0877128  979  HOH A O   
5085 O  O   . HOH H .   ? 0.421901 0.381596 0.408443 0.0832267   -0.03271    -0.0287653  980  HOH A O   
5086 O  O   . HOH H .   ? 0.32221  0.394268 0.389237 -0.0279277  -0.00114817 -0.0313909  981  HOH A O   
5087 O  O   . HOH H .   ? 0.606461 0.679552 0.597088 0.0324027   -0.0973379  -0.127224   982  HOH A O   
5088 O  O   . HOH H .   ? 0.696392 0.774518 0.4975   -0.0146819  -0.0513211  -0.0240235  983  HOH A O   
5089 O  O   . HOH H .   ? 0.68314  0.490641 0.551781 -0.0120746  0.0357826   0.0287387   984  HOH A O   
5090 O  O   . HOH H .   ? 0.635796 0.658299 0.52351  0.0399716   -0.0416886  -0.100472   985  HOH A O   
5091 O  O   . HOH H .   ? 0.351081 0.345371 0.354288 0.0321486   -0.032927   -0.118025   986  HOH A O   
5092 O  O   . HOH H .   ? 0.406875 0.449646 0.482131 0.0347438   -0.0423334  -0.0454511  987  HOH A O   
5093 O  O   . HOH H .   ? 0.521091 0.429476 0.551771 -0.130024   0.0373915   0.0301263   988  HOH A O   
5094 O  O   . HOH H .   ? 0.305476 0.294834 0.271631 -0.0209541  6.378e-05   -0.0210153  989  HOH A O   
5095 O  O   . HOH H .   ? 0.434216 0.38581  0.487811 0.0212767   -0.0563306  -0.147021   990  HOH A O   
5096 O  O   . HOH H .   ? 0.721857 0.874634 0.435014 -0.0345476  -0.00845255 -0.111878   991  HOH A O   
5097 O  O   . HOH H .   ? 0.421973 0.219285 0.494407 0.0132531   -0.0623182  -0.0493162  992  HOH A O   
5098 O  O   . HOH H .   ? 0.718368 0.733646 0.399644 -0.0941746  0.0698686   0.0735169   993  HOH A O   
5099 O  O   . HOH H .   ? 0.407852 0.254081 0.483239 0.0048082   -0.0559769  -0.0677606  994  HOH A O   
5100 O  O   . HOH H .   ? 0.49831  0.518729 0.443062 0.0341184   -0.0468854  -0.126243   995  HOH A O   
5101 O  O   . HOH H .   ? 0.390946 0.50268  0.415082 0.0398744   -0.110723   -0.122006   996  HOH A O   
5102 O  O   . HOH H .   ? 0.632446 0.54969  0.625743 0.0377133   0.0417313   -0.207202   997  HOH A O   
5103 O  O   . HOH H .   ? 0.489154 0.360976 0.432233 -0.0372272  0.0356321   -0.0117125  998  HOH A O   
5104 O  O   . HOH H .   ? 0.528953 0.620457 0.396562 -0.0347551  -0.0119887  -0.111629   999  HOH A O   
5105 O  O   . HOH H .   ? 0.456613 0.449638 0.422359 -0.00444831 0.0165045   -0.0257331  1000 HOH A O   
5106 O  O   . HOH H .   ? 0.343497 0.761097 0.651325 0.0212841   0.0510541   -0.20213    1001 HOH A O   
5107 O  O   . HOH H .   ? 0.345103 0.371317 0.42619  0.044251    -0.0377448  -0.0581749  1002 HOH A O   
5108 O  O   . HOH H .   ? 0.629539 0.513316 0.607339 -0.150358   0.0609469   0.063099    1003 HOH A O   
5109 O  O   . HOH H .   ? 0.591098 0.652049 0.493041 -0.0272727  0.0241378   -0.0654397  1004 HOH A O   
5110 O  O   . HOH H .   ? 0.538755 0.631523 0.429386 -0.0209046  0.0430959   -0.151386   1005 HOH A O   
5111 O  O   . HOH H .   ? 0.455651 0.443012 0.440203 -0.038454   0.00233344  0.0194221   1006 HOH A O   
5112 O  O   . HOH H .   ? 0.558907 0.510809 0.496885 -0.053507   0.00718418  0.0493239   1007 HOH A O   
5113 O  O   . HOH H .   ? 0.291933 0.422601 0.345286 -0.0240567  -0.0541144  -0.0855829  1008 HOH A O   
5114 O  O   . HOH H .   ? 0.437445 0.386257 0.287791 0.05165     -0.039685   -0.00204466 1009 HOH A O   
5115 O  O   . HOH H .   ? 0.507434 0.54398  0.439869 -0.0217279  -0.0256762  -0.026279   1010 HOH A O   
5116 O  O   . HOH H .   ? 0.590817 0.680581 0.623352 0.0933467   -0.0905775  -0.0609321  1011 HOH A O   
5117 O  O   . HOH H .   ? 0.555512 0.47345  0.527514 -0.00408348 0.030966    -0.143711   1012 HOH A O   
5118 O  O   . HOH H .   ? 0.734633 0.818554 0.556131 -0.02359    -0.0337959  -0.04489    1013 HOH A O   
5119 O  O   . HOH H .   ? 0.536932 0.573787 0.565012 -0.00445735 0.0136841   -0.0464529  1014 HOH A O   
5120 O  O   . HOH H .   ? 0.565566 0.654847 0.543643 0.0999274   -0.119557   -0.0688686  1015 HOH A O   
5121 O  O   . HOH H .   ? 0.460032 0.49504  0.388959 0.038079    -0.0666427  -0.122763   1016 HOH A O   
5122 O  O   . HOH H .   ? 0.912596 0.928958 0.479344 0.0157272   -0.096726   0.0735783   1017 HOH A O   
5123 O  O   . HOH H .   ? 0.398618 0.390044 0.394574 -0.0290292  0.0167167   -0.0196139  1018 HOH A O   
5124 O  O   . HOH H .   ? 0.442366 0.237685 0.512488 -0.0510558  -0.0380346  -0.0264086  1019 HOH A O   
5125 O  O   . HOH H .   ? 0.596402 0.780131 0.397854 -0.0421933  0.0887368   -0.145765   1020 HOH A O   
5126 O  O   . HOH H .   ? 0.372951 0.468941 0.490395 -0.0503795  -0.008403   -0.0557902  1021 HOH A O   
5127 O  O   . HOH H .   ? 0.38679  0.418288 0.386061 0.0189798   -0.0729535  -0.112749   1022 HOH A O   
5128 O  O   . HOH H .   ? 0.595876 0.567744 0.514416 0.0829668   -0.0674111  -0.00871327 1023 HOH A O   
5129 O  O   . HOH H .   ? 0.551834 0.463824 0.449419 0.087666    -0.0522766  0.00951031  1024 HOH A O   
5130 O  O   . HOH H .   ? 0.46287  0.496931 0.504082 0.00805998  -0.00274892 -0.0468501  1025 HOH A O   
5131 O  O   . HOH H .   ? 0.447886 0.657171 0.424212 -0.061493   0.117883    -0.0894351  1026 HOH A O   
5132 O  O   . HOH H .   ? 0.778685 0.819568 0.456904 -0.0909699  0.0727194   0.0559827   1027 HOH A O   
5133 O  O   . HOH H .   ? 0.48073  0.593141 0.607336 0.0567801   -0.0698342  -0.0726218  1028 HOH A O   
5134 O  O   . HOH H .   ? 0.441872 0.453436 0.346631 0.0326459   -0.0265305  -0.0848423  1029 HOH A O   
5135 O  O   . HOH H .   ? 0.600719 0.465592 0.454423 0.0338969   -0.00549301 0.0312662   1030 HOH A O   
5136 O  O   . HOH H .   ? 0.381448 0.406142 0.328086 -0.0218001  0.0140331   -0.0213816  1031 HOH A O   
5137 O  O   . HOH H .   ? 0.575118 0.543867 0.496578 0.099976    -0.0755266  -0.00954578 1032 HOH A O   
5138 O  O   . HOH H .   ? 0.606989 0.598953 0.545954 0.116302    -0.08997    -0.020778   1033 HOH A O   
5139 O  O   . HOH H .   ? 0.234465 0.705422 0.56145  -0.0395336  0.101331    -0.209748   1034 HOH A O   
5140 O  O   . HOH H .   ? 0.490059 0.492266 0.469456 -0.0101401  0.0216569   -0.0286098  1035 HOH A O   
5141 O  O   . HOH H .   ? 0.513207 0.533966 0.554832 0.0170464   -0.0127902  -0.0459049  1036 HOH A O   
5142 O  O   . HOH H .   ? 0.506296 0.604979 0.545704 0.0472739   0.0503621   -0.146231   1037 HOH A O   
5143 O  O   . HOH H .   ? 0.478847 0.366765 0.328894 0.0475363   -0.0212373  0.0261232   1038 HOH A O   
5144 O  O   . HOH H .   ? 0.433881 0.561807 0.641963 -0.0696974  -0.0859667  -0.196283   1039 HOH A O   
5145 O  O   . HOH H .   ? 0.623203 0.561605 0.479077 0.0402394   -0.0253897  0.00394747  1040 HOH A O   
5146 O  O   . HOH H .   ? 0.477145 0.522891 0.549841 0.026419    -0.0263193  -0.0520866  1041 HOH A O   
5147 O  O   . HOH H .   ? 0.490442 0.572447 0.545079 0.110616    -0.0752883  -0.0637415  1042 HOH A O   
5148 O  O   . HOH H .   ? 0.59533  0.445901 0.457771 0.00901894  0.0164607   0.031202    1043 HOH A O   
5149 O  O   . HOH H .   ? 0.405945 0.264207 0.350511 0.0218075   0.0114396   -0.0243027  1044 HOH A O   
5150 O  O   . HOH H .   ? 0.50877  0.601923 0.443296 0.00164362  0.0615203   -0.185726   1045 HOH A O   
# 
