data_9KNI
# 
_entry.id   9KNI 
# 
_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   9KNI         pdb_00009kni 10.2210/pdb9kni/pdb 
WWPDB D_1300053732 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-12 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9KNI 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              yangcg@simm.ac.cn 
_pdbx_contact_author.name_first         Cai-Guang 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5778-4422 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yang, C.G.' 1 0000-0001-5778-4422 
'Gan, J.H.'  2 0000-0002-8438-8852 
# 
_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                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            289 
_citation.language                  ? 
_citation.page_first                117444 
_citation.page_last                 117444 
_citation.title                     
'Development of 3-arylaminothiophenic-2-carboxylic acid derivatives as new FTO inhibitors showing potent antileukemia activities.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2025.117444 
_citation.pdbx_database_id_PubMed   40022879 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhang, D.'  1  ? 
primary 'Liu, L.'    2  ? 
primary 'Li, M.'     3  ? 
primary 'Hu, X.'     4  ? 
primary 'Zhang, X.'  5  ? 
primary 'Xia, W.'    6  ? 
primary 'Wang, Z.'   7  ? 
primary 'Song, X.'   8  ? 
primary 'Huang, Y.'  9  ? 
primary 'Dong, Z.'   10 ? 
primary 'Yang, C.G.' 11 ? 
# 
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 'Alpha-ketoglutarate-dependent dioxygenase FTO'                                                   54933.965 1  
1.14.11.-,1.14.11.53 ? ? ? 
2 non-polymer nat '2-OXOGLUTARIC ACID'                                                                              146.098   1  ? 
? ? ? 
3 non-polymer syn '3-[[2,6-bis(chloranyl)-4-(3,5-dimethyl-1H-pyrazol-4-yl)phenyl]amino]thiophene-2-carboxylic acid' 382.264   1  ? 
? ? ? 
4 water       nat water                                                                                             18.015    13 ? 
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Fat mass and obesity-associated protein,U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO,U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO,mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTO,m6A(m)-demethylase FTO,mRNA N(6)-methyladenosine demethylase FTO,tRNA N1-methyl adenine demethylase FTO
;
# 
_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       
;GSHMTPKDDEFYQQWQLKYPKLILREASSVSEELHKEVQEAFLTLHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYK
YLNTRLFTVPWPVKGSNIKHTEAEIAAACETFLKLNDYLQIETIQALEELAAKEKANEDAVPLCMSADFPRVGMGSSYNG
QDEVDIKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGPEEESEDDSHLEGRDP
DIWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLALQNVCD
DVDNDDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEGVTNAVLHEVKREGLP
VEQRNEILTAILASLTARQNLRREWHARCQSRIARTLPADQKPECRPYWEKDDASMPLPFDLTDIVSELRGQLLEAKP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSHMTPKDDEFYQQWQLKYPKLILREASSVSEELHKEVQEAFLTLHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYK
YLNTRLFTVPWPVKGSNIKHTEAEIAAACETFLKLNDYLQIETIQALEELAAKEKANEDAVPLCMSADFPRVGMGSSYNG
QDEVDIKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGPEEESEDDSHLEGRDP
DIWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLALQNVCD
DVDNDDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEGVTNAVLHEVKREGLP
VEQRNEILTAILASLTARQNLRREWHARCQSRIARTLPADQKPECRPYWEKDDASMPLPFDLTDIVSELRGQLLEAKP
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-OXOGLUTARIC ACID'                                                                              AKG   
3 '3-[[2,6-bis(chloranyl)-4-(3,5-dimethyl-1H-pyrazol-4-yl)phenyl]amino]thiophene-2-carboxylic acid' A1EF5 
4 water                                                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   HIS n 
1 4   MET n 
1 5   THR n 
1 6   PRO n 
1 7   LYS n 
1 8   ASP n 
1 9   ASP n 
1 10  GLU n 
1 11  PHE n 
1 12  TYR n 
1 13  GLN n 
1 14  GLN n 
1 15  TRP n 
1 16  GLN n 
1 17  LEU n 
1 18  LYS n 
1 19  TYR n 
1 20  PRO n 
1 21  LYS n 
1 22  LEU n 
1 23  ILE n 
1 24  LEU n 
1 25  ARG n 
1 26  GLU n 
1 27  ALA n 
1 28  SER n 
1 29  SER n 
1 30  VAL n 
1 31  SER n 
1 32  GLU n 
1 33  GLU n 
1 34  LEU n 
1 35  HIS n 
1 36  LYS n 
1 37  GLU n 
1 38  VAL n 
1 39  GLN n 
1 40  GLU n 
1 41  ALA n 
1 42  PHE n 
1 43  LEU n 
1 44  THR n 
1 45  LEU n 
1 46  HIS n 
1 47  LYS n 
1 48  HIS n 
1 49  GLY n 
1 50  CYS n 
1 51  LEU n 
1 52  PHE n 
1 53  ARG n 
1 54  ASP n 
1 55  LEU n 
1 56  VAL n 
1 57  ARG n 
1 58  ILE n 
1 59  GLN n 
1 60  GLY n 
1 61  LYS n 
1 62  ASP n 
1 63  LEU n 
1 64  LEU n 
1 65  THR n 
1 66  PRO n 
1 67  VAL n 
1 68  SER n 
1 69  ARG n 
1 70  ILE n 
1 71  LEU n 
1 72  ILE n 
1 73  GLY n 
1 74  ASN n 
1 75  PRO n 
1 76  GLY n 
1 77  CYS n 
1 78  THR n 
1 79  TYR n 
1 80  LYS n 
1 81  TYR n 
1 82  LEU n 
1 83  ASN n 
1 84  THR n 
1 85  ARG n 
1 86  LEU n 
1 87  PHE n 
1 88  THR n 
1 89  VAL n 
1 90  PRO n 
1 91  TRP n 
1 92  PRO n 
1 93  VAL n 
1 94  LYS n 
1 95  GLY n 
1 96  SER n 
1 97  ASN n 
1 98  ILE n 
1 99  LYS n 
1 100 HIS n 
1 101 THR n 
1 102 GLU n 
1 103 ALA n 
1 104 GLU n 
1 105 ILE n 
1 106 ALA n 
1 107 ALA n 
1 108 ALA n 
1 109 CYS n 
1 110 GLU n 
1 111 THR n 
1 112 PHE n 
1 113 LEU n 
1 114 LYS n 
1 115 LEU n 
1 116 ASN n 
1 117 ASP n 
1 118 TYR n 
1 119 LEU n 
1 120 GLN n 
1 121 ILE n 
1 122 GLU n 
1 123 THR n 
1 124 ILE n 
1 125 GLN n 
1 126 ALA n 
1 127 LEU n 
1 128 GLU n 
1 129 GLU n 
1 130 LEU n 
1 131 ALA n 
1 132 ALA n 
1 133 LYS n 
1 134 GLU n 
1 135 LYS n 
1 136 ALA n 
1 137 ASN n 
1 138 GLU n 
1 139 ASP n 
1 140 ALA n 
1 141 VAL n 
1 142 PRO n 
1 143 LEU n 
1 144 CYS n 
1 145 MET n 
1 146 SER n 
1 147 ALA n 
1 148 ASP n 
1 149 PHE n 
1 150 PRO n 
1 151 ARG n 
1 152 VAL n 
1 153 GLY n 
1 154 MET n 
1 155 GLY n 
1 156 SER n 
1 157 SER n 
1 158 TYR n 
1 159 ASN n 
1 160 GLY n 
1 161 GLN n 
1 162 ASP n 
1 163 GLU n 
1 164 VAL n 
1 165 ASP n 
1 166 ILE n 
1 167 LYS n 
1 168 SER n 
1 169 ARG n 
1 170 ALA n 
1 171 ALA n 
1 172 TYR n 
1 173 ASN n 
1 174 VAL n 
1 175 THR n 
1 176 LEU n 
1 177 LEU n 
1 178 ASN n 
1 179 PHE n 
1 180 MET n 
1 181 ASP n 
1 182 PRO n 
1 183 GLN n 
1 184 LYS n 
1 185 MET n 
1 186 PRO n 
1 187 TYR n 
1 188 LEU n 
1 189 LYS n 
1 190 GLU n 
1 191 GLU n 
1 192 PRO n 
1 193 TYR n 
1 194 PHE n 
1 195 GLY n 
1 196 MET n 
1 197 GLY n 
1 198 LYS n 
1 199 MET n 
1 200 ALA n 
1 201 VAL n 
1 202 SER n 
1 203 TRP n 
1 204 HIS n 
1 205 HIS n 
1 206 ASP n 
1 207 GLU n 
1 208 ASN n 
1 209 LEU n 
1 210 VAL n 
1 211 ASP n 
1 212 ARG n 
1 213 SER n 
1 214 ALA n 
1 215 VAL n 
1 216 ALA n 
1 217 VAL n 
1 218 TYR n 
1 219 SER n 
1 220 TYR n 
1 221 SER n 
1 222 CYS n 
1 223 GLU n 
1 224 GLY n 
1 225 PRO n 
1 226 GLU n 
1 227 GLU n 
1 228 GLU n 
1 229 SER n 
1 230 GLU n 
1 231 ASP n 
1 232 ASP n 
1 233 SER n 
1 234 HIS n 
1 235 LEU n 
1 236 GLU n 
1 237 GLY n 
1 238 ARG n 
1 239 ASP n 
1 240 PRO n 
1 241 ASP n 
1 242 ILE n 
1 243 TRP n 
1 244 HIS n 
1 245 VAL n 
1 246 GLY n 
1 247 PHE n 
1 248 LYS n 
1 249 ILE n 
1 250 SER n 
1 251 TRP n 
1 252 ASP n 
1 253 ILE n 
1 254 GLU n 
1 255 THR n 
1 256 PRO n 
1 257 GLY n 
1 258 LEU n 
1 259 ALA n 
1 260 ILE n 
1 261 PRO n 
1 262 LEU n 
1 263 HIS n 
1 264 GLN n 
1 265 GLY n 
1 266 ASP n 
1 267 CYS n 
1 268 TYR n 
1 269 PHE n 
1 270 MET n 
1 271 LEU n 
1 272 ASP n 
1 273 ASP n 
1 274 LEU n 
1 275 ASN n 
1 276 ALA n 
1 277 THR n 
1 278 HIS n 
1 279 GLN n 
1 280 HIS n 
1 281 CYS n 
1 282 VAL n 
1 283 LEU n 
1 284 ALA n 
1 285 GLY n 
1 286 SER n 
1 287 GLN n 
1 288 PRO n 
1 289 ARG n 
1 290 PHE n 
1 291 SER n 
1 292 SER n 
1 293 THR n 
1 294 HIS n 
1 295 ARG n 
1 296 VAL n 
1 297 ALA n 
1 298 GLU n 
1 299 CYS n 
1 300 SER n 
1 301 THR n 
1 302 GLY n 
1 303 THR n 
1 304 LEU n 
1 305 ASP n 
1 306 TYR n 
1 307 ILE n 
1 308 LEU n 
1 309 GLN n 
1 310 ARG n 
1 311 CYS n 
1 312 GLN n 
1 313 LEU n 
1 314 ALA n 
1 315 LEU n 
1 316 GLN n 
1 317 ASN n 
1 318 VAL n 
1 319 CYS n 
1 320 ASP n 
1 321 ASP n 
1 322 VAL n 
1 323 ASP n 
1 324 ASN n 
1 325 ASP n 
1 326 ASP n 
1 327 VAL n 
1 328 SER n 
1 329 LEU n 
1 330 LYS n 
1 331 SER n 
1 332 PHE n 
1 333 GLU n 
1 334 PRO n 
1 335 ALA n 
1 336 VAL n 
1 337 LEU n 
1 338 LYS n 
1 339 GLN n 
1 340 GLY n 
1 341 GLU n 
1 342 GLU n 
1 343 ILE n 
1 344 HIS n 
1 345 ASN n 
1 346 GLU n 
1 347 VAL n 
1 348 GLU n 
1 349 PHE n 
1 350 GLU n 
1 351 TRP n 
1 352 LEU n 
1 353 ARG n 
1 354 GLN n 
1 355 PHE n 
1 356 TRP n 
1 357 PHE n 
1 358 GLN n 
1 359 GLY n 
1 360 ASN n 
1 361 ARG n 
1 362 TYR n 
1 363 ARG n 
1 364 LYS n 
1 365 CYS n 
1 366 THR n 
1 367 ASP n 
1 368 TRP n 
1 369 TRP n 
1 370 CYS n 
1 371 GLN n 
1 372 PRO n 
1 373 MET n 
1 374 ALA n 
1 375 GLN n 
1 376 LEU n 
1 377 GLU n 
1 378 ALA n 
1 379 LEU n 
1 380 TRP n 
1 381 LYS n 
1 382 LYS n 
1 383 MET n 
1 384 GLU n 
1 385 GLY n 
1 386 VAL n 
1 387 THR n 
1 388 ASN n 
1 389 ALA n 
1 390 VAL n 
1 391 LEU n 
1 392 HIS n 
1 393 GLU n 
1 394 VAL n 
1 395 LYS n 
1 396 ARG n 
1 397 GLU n 
1 398 GLY n 
1 399 LEU n 
1 400 PRO n 
1 401 VAL n 
1 402 GLU n 
1 403 GLN n 
1 404 ARG n 
1 405 ASN n 
1 406 GLU n 
1 407 ILE n 
1 408 LEU n 
1 409 THR n 
1 410 ALA n 
1 411 ILE n 
1 412 LEU n 
1 413 ALA n 
1 414 SER n 
1 415 LEU n 
1 416 THR n 
1 417 ALA n 
1 418 ARG n 
1 419 GLN n 
1 420 ASN n 
1 421 LEU n 
1 422 ARG n 
1 423 ARG n 
1 424 GLU n 
1 425 TRP n 
1 426 HIS n 
1 427 ALA n 
1 428 ARG n 
1 429 CYS n 
1 430 GLN n 
1 431 SER n 
1 432 ARG n 
1 433 ILE n 
1 434 ALA n 
1 435 ARG n 
1 436 THR n 
1 437 LEU n 
1 438 PRO n 
1 439 ALA n 
1 440 ASP n 
1 441 GLN n 
1 442 LYS n 
1 443 PRO n 
1 444 GLU n 
1 445 CYS n 
1 446 ARG n 
1 447 PRO n 
1 448 TYR n 
1 449 TRP n 
1 450 GLU n 
1 451 LYS n 
1 452 ASP n 
1 453 ASP n 
1 454 ALA n 
1 455 SER n 
1 456 MET n 
1 457 PRO n 
1 458 LEU n 
1 459 PRO n 
1 460 PHE n 
1 461 ASP n 
1 462 LEU n 
1 463 THR n 
1 464 ASP n 
1 465 ILE n 
1 466 VAL n 
1 467 SER n 
1 468 GLU n 
1 469 LEU n 
1 470 ARG n 
1 471 GLY n 
1 472 GLN n 
1 473 LEU n 
1 474 LEU n 
1 475 GLU n 
1 476 ALA n 
1 477 LYS n 
1 478 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                   478 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'FTO, KIAA1752' 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1EF5 non-polymer         . '3-[[2,6-bis(chloranyl)-4-(3,5-dimethyl-1H-pyrazol-4-yl)phenyl]amino]thiophene-2-carboxylic acid' ? 
'C16 H13 Cl2 N3 O2 S' 382.264 
AKG   non-polymer         . '2-OXOGLUTARIC ACID'                                                                              ? 
'C5 H6 O5'            146.098 
ALA   'L-peptide linking' y ALANINE                                                                                           ? 
'C3 H7 N O2'          89.093  
ARG   'L-peptide linking' y ARGININE                                                                                          ? 
'C6 H15 N4 O2 1'      175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                        ? 
'C4 H8 N2 O3'         132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                   ? 
'C4 H7 N O4'          133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                          ? 
'C3 H7 N O2 S'        121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                         ? 
'C5 H10 N2 O3'        146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                   ? 
'C5 H9 N O4'          147.129 
GLY   'peptide linking'   y GLYCINE                                                                                           ? 
'C2 H5 N O2'          75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                         ? 
'C6 H10 N3 O2 1'      156.162 
HOH   non-polymer         . WATER                                                                                             ? 
'H2 O'                18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                        ? 
'C6 H13 N O2'         131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                           ? 
'C6 H13 N O2'         131.173 
LYS   'L-peptide linking' y LYSINE                                                                                            ? 
'C6 H15 N2 O2 1'      147.195 
MET   'L-peptide linking' y METHIONINE                                                                                        ? 
'C5 H11 N O2 S'       149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                     ? 
'C9 H11 N O2'         165.189 
PRO   'L-peptide linking' y PROLINE                                                                                           ? 
'C5 H9 N O2'          115.130 
SER   'L-peptide linking' y SERINE                                                                                            ? 
'C3 H7 N O3'          105.093 
THR   'L-peptide linking' y THREONINE                                                                                         ? 
'C4 H9 N O3'          119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                        ? 
'C11 H12 N2 O2'       204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                          ? 
'C9 H11 N O3'         181.189 
VAL   'L-peptide linking' y VALINE                                                                                            ? 
'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   28  28  GLY GLY A . n 
A 1 2   SER 2   29  29  SER SER A . n 
A 1 3   HIS 3   30  30  HIS HIS A . n 
A 1 4   MET 4   31  31  MET MET A . n 
A 1 5   THR 5   32  32  THR THR A . n 
A 1 6   PRO 6   33  33  PRO PRO A . n 
A 1 7   LYS 7   34  34  LYS LYS A . n 
A 1 8   ASP 8   35  35  ASP ASP A . n 
A 1 9   ASP 9   36  36  ASP ASP A . n 
A 1 10  GLU 10  37  37  GLU GLU A . n 
A 1 11  PHE 11  38  38  PHE PHE A . n 
A 1 12  TYR 12  39  39  TYR TYR A . n 
A 1 13  GLN 13  40  40  GLN GLN A . n 
A 1 14  GLN 14  41  41  GLN GLN A . n 
A 1 15  TRP 15  42  42  TRP TRP A . n 
A 1 16  GLN 16  43  43  GLN GLN A . n 
A 1 17  LEU 17  44  44  LEU LEU A . n 
A 1 18  LYS 18  45  45  LYS LYS A . n 
A 1 19  TYR 19  46  46  TYR TYR A . n 
A 1 20  PRO 20  47  47  PRO PRO A . n 
A 1 21  LYS 21  48  48  LYS LYS A . n 
A 1 22  LEU 22  49  49  LEU LEU A . n 
A 1 23  ILE 23  50  50  ILE ILE A . n 
A 1 24  LEU 24  51  51  LEU LEU A . n 
A 1 25  ARG 25  52  52  ARG ARG A . n 
A 1 26  GLU 26  53  53  GLU GLU A . n 
A 1 27  ALA 27  54  54  ALA ALA A . n 
A 1 28  SER 28  55  55  SER SER A . n 
A 1 29  SER 29  56  56  SER SER A . n 
A 1 30  VAL 30  57  57  VAL VAL A . n 
A 1 31  SER 31  58  58  SER SER A . n 
A 1 32  GLU 32  59  59  GLU GLU A . n 
A 1 33  GLU 33  60  60  GLU GLU A . n 
A 1 34  LEU 34  61  61  LEU LEU A . n 
A 1 35  HIS 35  62  62  HIS HIS A . n 
A 1 36  LYS 36  63  63  LYS LYS A . n 
A 1 37  GLU 37  64  64  GLU GLU A . n 
A 1 38  VAL 38  65  65  VAL VAL A . n 
A 1 39  GLN 39  66  66  GLN GLN A . n 
A 1 40  GLU 40  67  67  GLU GLU A . n 
A 1 41  ALA 41  68  68  ALA ALA A . n 
A 1 42  PHE 42  69  69  PHE PHE A . n 
A 1 43  LEU 43  70  70  LEU LEU A . n 
A 1 44  THR 44  71  71  THR THR A . n 
A 1 45  LEU 45  72  72  LEU LEU A . n 
A 1 46  HIS 46  73  73  HIS HIS A . n 
A 1 47  LYS 47  74  74  LYS LYS A . n 
A 1 48  HIS 48  75  75  HIS HIS A . n 
A 1 49  GLY 49  76  76  GLY GLY A . n 
A 1 50  CYS 50  77  77  CYS CYS A . n 
A 1 51  LEU 51  78  78  LEU LEU A . n 
A 1 52  PHE 52  79  79  PHE PHE A . n 
A 1 53  ARG 53  80  80  ARG ARG A . n 
A 1 54  ASP 54  81  81  ASP ASP A . n 
A 1 55  LEU 55  82  82  LEU LEU A . n 
A 1 56  VAL 56  83  83  VAL VAL A . n 
A 1 57  ARG 57  84  84  ARG ARG A . n 
A 1 58  ILE 58  85  85  ILE ILE A . n 
A 1 59  GLN 59  86  86  GLN GLN A . n 
A 1 60  GLY 60  87  87  GLY GLY A . n 
A 1 61  LYS 61  88  88  LYS LYS A . n 
A 1 62  ASP 62  89  89  ASP ASP A . n 
A 1 63  LEU 63  90  90  LEU LEU A . n 
A 1 64  LEU 64  91  91  LEU LEU A . n 
A 1 65  THR 65  92  92  THR THR A . n 
A 1 66  PRO 66  93  93  PRO PRO A . n 
A 1 67  VAL 67  94  94  VAL VAL A . n 
A 1 68  SER 68  95  95  SER SER A . n 
A 1 69  ARG 69  96  96  ARG ARG A . n 
A 1 70  ILE 70  97  97  ILE ILE A . n 
A 1 71  LEU 71  98  98  LEU LEU A . n 
A 1 72  ILE 72  99  99  ILE ILE A . n 
A 1 73  GLY 73  100 100 GLY GLY A . n 
A 1 74  ASN 74  101 101 ASN ASN A . n 
A 1 75  PRO 75  102 102 PRO PRO A . n 
A 1 76  GLY 76  103 103 GLY GLY A . n 
A 1 77  CYS 77  104 104 CYS CYS A . n 
A 1 78  THR 78  105 105 THR THR A . n 
A 1 79  TYR 79  106 106 TYR TYR A . n 
A 1 80  LYS 80  107 107 LYS LYS A . n 
A 1 81  TYR 81  108 108 TYR TYR A . n 
A 1 82  LEU 82  109 109 LEU LEU A . n 
A 1 83  ASN 83  110 110 ASN ASN A . n 
A 1 84  THR 84  111 111 THR THR A . n 
A 1 85  ARG 85  112 112 ARG ARG A . n 
A 1 86  LEU 86  113 113 LEU LEU A . n 
A 1 87  PHE 87  114 114 PHE PHE A . n 
A 1 88  THR 88  115 115 THR THR A . n 
A 1 89  VAL 89  116 116 VAL VAL A . n 
A 1 90  PRO 90  117 117 PRO PRO A . n 
A 1 91  TRP 91  118 118 TRP TRP A . n 
A 1 92  PRO 92  119 119 PRO PRO A . n 
A 1 93  VAL 93  120 120 VAL VAL A . n 
A 1 94  LYS 94  121 121 LYS LYS A . n 
A 1 95  GLY 95  122 122 GLY GLY A . n 
A 1 96  SER 96  123 ?   ?   ?   A . n 
A 1 97  ASN 97  124 ?   ?   ?   A . n 
A 1 98  ILE 98  125 ?   ?   ?   A . n 
A 1 99  LYS 99  126 ?   ?   ?   A . n 
A 1 100 HIS 100 127 ?   ?   ?   A . n 
A 1 101 THR 101 128 ?   ?   ?   A . n 
A 1 102 GLU 102 129 129 GLU GLU A . n 
A 1 103 ALA 103 130 130 ALA ALA A . n 
A 1 104 GLU 104 131 131 GLU GLU A . n 
A 1 105 ILE 105 132 132 ILE ILE A . n 
A 1 106 ALA 106 133 133 ALA ALA A . n 
A 1 107 ALA 107 134 134 ALA ALA A . n 
A 1 108 ALA 108 135 135 ALA ALA A . n 
A 1 109 CYS 109 136 136 CYS CYS A . n 
A 1 110 GLU 110 137 137 GLU GLU A . n 
A 1 111 THR 111 138 138 THR THR A . n 
A 1 112 PHE 112 139 139 PHE PHE A . n 
A 1 113 LEU 113 140 140 LEU LEU A . n 
A 1 114 LYS 114 141 141 LYS LYS A . n 
A 1 115 LEU 115 142 142 LEU LEU A . n 
A 1 116 ASN 116 143 143 ASN ASN A . n 
A 1 117 ASP 117 144 144 ASP ASP A . n 
A 1 118 TYR 118 145 145 TYR TYR A . n 
A 1 119 LEU 119 146 146 LEU LEU A . n 
A 1 120 GLN 120 147 147 GLN GLN A . n 
A 1 121 ILE 121 148 148 ILE ILE A . n 
A 1 122 GLU 122 149 149 GLU GLU A . n 
A 1 123 THR 123 150 150 THR THR A . n 
A 1 124 ILE 124 151 151 ILE ILE A . n 
A 1 125 GLN 125 152 152 GLN GLN A . n 
A 1 126 ALA 126 153 153 ALA ALA A . n 
A 1 127 LEU 127 154 154 LEU LEU A . n 
A 1 128 GLU 128 155 155 GLU GLU A . n 
A 1 129 GLU 129 156 156 GLU GLU A . n 
A 1 130 LEU 130 157 157 LEU LEU A . n 
A 1 131 ALA 131 158 158 ALA ALA A . n 
A 1 132 ALA 132 159 159 ALA ALA A . n 
A 1 133 LYS 133 160 160 LYS LYS A . n 
A 1 134 GLU 134 161 161 GLU GLU A . n 
A 1 135 LYS 135 162 162 LYS LYS A . n 
A 1 136 ALA 136 163 163 ALA ALA A . n 
A 1 137 ASN 137 164 ?   ?   ?   A . n 
A 1 138 GLU 138 165 ?   ?   ?   A . n 
A 1 139 ASP 139 166 ?   ?   ?   A . n 
A 1 140 ALA 140 167 ?   ?   ?   A . n 
A 1 141 VAL 141 168 ?   ?   ?   A . n 
A 1 142 PRO 142 169 ?   ?   ?   A . n 
A 1 143 LEU 143 170 ?   ?   ?   A . n 
A 1 144 CYS 144 171 ?   ?   ?   A . n 
A 1 145 MET 145 172 ?   ?   ?   A . n 
A 1 146 SER 146 173 ?   ?   ?   A . n 
A 1 147 ALA 147 174 ?   ?   ?   A . n 
A 1 148 ASP 148 175 ?   ?   ?   A . n 
A 1 149 PHE 149 176 ?   ?   ?   A . n 
A 1 150 PRO 150 177 ?   ?   ?   A . n 
A 1 151 ARG 151 178 ?   ?   ?   A . n 
A 1 152 VAL 152 179 ?   ?   ?   A . n 
A 1 153 GLY 153 180 ?   ?   ?   A . n 
A 1 154 MET 154 181 ?   ?   ?   A . n 
A 1 155 GLY 155 182 ?   ?   ?   A . n 
A 1 156 SER 156 183 ?   ?   ?   A . n 
A 1 157 SER 157 184 ?   ?   ?   A . n 
A 1 158 TYR 158 185 ?   ?   ?   A . n 
A 1 159 ASN 159 186 ?   ?   ?   A . n 
A 1 160 GLY 160 187 ?   ?   ?   A . n 
A 1 161 GLN 161 188 188 GLN GLN A . n 
A 1 162 ASP 162 189 189 ASP ASP A . n 
A 1 163 GLU 163 190 190 GLU GLU A . n 
A 1 164 VAL 164 191 191 VAL VAL A . n 
A 1 165 ASP 165 192 192 ASP ASP A . n 
A 1 166 ILE 166 193 193 ILE ILE A . n 
A 1 167 LYS 167 194 194 LYS LYS A . n 
A 1 168 SER 168 195 195 SER SER A . n 
A 1 169 ARG 169 196 196 ARG ARG A . n 
A 1 170 ALA 170 197 197 ALA ALA A . n 
A 1 171 ALA 171 198 198 ALA ALA A . n 
A 1 172 TYR 172 199 199 TYR TYR A . n 
A 1 173 ASN 173 200 200 ASN ASN A . n 
A 1 174 VAL 174 201 201 VAL VAL A . n 
A 1 175 THR 175 202 202 THR THR A . n 
A 1 176 LEU 176 203 203 LEU LEU A . n 
A 1 177 LEU 177 204 204 LEU LEU A . n 
A 1 178 ASN 178 205 205 ASN ASN A . n 
A 1 179 PHE 179 206 206 PHE PHE A . n 
A 1 180 MET 180 207 207 MET MET A . n 
A 1 181 ASP 181 208 208 ASP ASP A . n 
A 1 182 PRO 182 209 209 PRO PRO A . n 
A 1 183 GLN 183 210 210 GLN GLN A . n 
A 1 184 LYS 184 211 211 LYS LYS A . n 
A 1 185 MET 185 212 212 MET MET A . n 
A 1 186 PRO 186 213 213 PRO PRO A . n 
A 1 187 TYR 187 214 214 TYR TYR A . n 
A 1 188 LEU 188 215 215 LEU LEU A . n 
A 1 189 LYS 189 216 216 LYS LYS A . n 
A 1 190 GLU 190 217 217 GLU GLU A . n 
A 1 191 GLU 191 218 218 GLU GLU A . n 
A 1 192 PRO 192 219 219 PRO PRO A . n 
A 1 193 TYR 193 220 220 TYR TYR A . n 
A 1 194 PHE 194 221 221 PHE PHE A . n 
A 1 195 GLY 195 222 222 GLY GLY A . n 
A 1 196 MET 196 223 223 MET MET A . n 
A 1 197 GLY 197 224 224 GLY GLY A . n 
A 1 198 LYS 198 225 225 LYS LYS A . n 
A 1 199 MET 199 226 226 MET MET A . n 
A 1 200 ALA 200 227 227 ALA ALA A . n 
A 1 201 VAL 201 228 228 VAL VAL A . n 
A 1 202 SER 202 229 229 SER SER A . n 
A 1 203 TRP 203 230 230 TRP TRP A . n 
A 1 204 HIS 204 231 231 HIS HIS A . n 
A 1 205 HIS 205 232 232 HIS HIS A . n 
A 1 206 ASP 206 233 233 ASP ASP A . n 
A 1 207 GLU 207 234 234 GLU GLU A . n 
A 1 208 ASN 208 235 235 ASN ASN A . n 
A 1 209 LEU 209 236 236 LEU LEU A . n 
A 1 210 VAL 210 237 237 VAL VAL A . n 
A 1 211 ASP 211 238 238 ASP ASP A . n 
A 1 212 ARG 212 239 239 ARG ARG A . n 
A 1 213 SER 213 240 240 SER SER A . n 
A 1 214 ALA 214 241 241 ALA ALA A . n 
A 1 215 VAL 215 242 242 VAL VAL A . n 
A 1 216 ALA 216 243 243 ALA ALA A . n 
A 1 217 VAL 217 244 244 VAL VAL A . n 
A 1 218 TYR 218 245 245 TYR TYR A . n 
A 1 219 SER 219 246 246 SER SER A . n 
A 1 220 TYR 220 247 247 TYR TYR A . n 
A 1 221 SER 221 248 248 SER SER A . n 
A 1 222 CYS 222 249 249 CYS CYS A . n 
A 1 223 GLU 223 250 250 GLU GLU A . n 
A 1 224 GLY 224 251 ?   ?   ?   A . n 
A 1 225 PRO 225 252 ?   ?   ?   A . n 
A 1 226 GLU 226 253 ?   ?   ?   A . n 
A 1 227 GLU 227 254 ?   ?   ?   A . n 
A 1 228 GLU 228 255 ?   ?   ?   A . n 
A 1 229 SER 229 256 ?   ?   ?   A . n 
A 1 230 GLU 230 257 ?   ?   ?   A . n 
A 1 231 ASP 231 258 ?   ?   ?   A . n 
A 1 232 ASP 232 259 ?   ?   ?   A . n 
A 1 233 SER 233 260 ?   ?   ?   A . n 
A 1 234 HIS 234 261 ?   ?   ?   A . n 
A 1 235 LEU 235 262 262 LEU LEU A . n 
A 1 236 GLU 236 263 263 GLU GLU A . n 
A 1 237 GLY 237 264 264 GLY GLY A . n 
A 1 238 ARG 238 265 265 ARG ARG A . n 
A 1 239 ASP 239 266 266 ASP ASP A . n 
A 1 240 PRO 240 267 267 PRO PRO A . n 
A 1 241 ASP 241 268 268 ASP ASP A . n 
A 1 242 ILE 242 269 269 ILE ILE A . n 
A 1 243 TRP 243 270 270 TRP TRP A . n 
A 1 244 HIS 244 271 271 HIS HIS A . n 
A 1 245 VAL 245 272 272 VAL VAL A . n 
A 1 246 GLY 246 273 273 GLY GLY A . n 
A 1 247 PHE 247 274 274 PHE PHE A . n 
A 1 248 LYS 248 275 275 LYS LYS A . n 
A 1 249 ILE 249 276 276 ILE ILE A . n 
A 1 250 SER 250 277 277 SER SER A . n 
A 1 251 TRP 251 278 278 TRP TRP A . n 
A 1 252 ASP 252 279 279 ASP ASP A . n 
A 1 253 ILE 253 280 280 ILE ILE A . n 
A 1 254 GLU 254 281 281 GLU GLU A . n 
A 1 255 THR 255 282 282 THR THR A . n 
A 1 256 PRO 256 283 283 PRO PRO A . n 
A 1 257 GLY 257 284 284 GLY GLY A . n 
A 1 258 LEU 258 285 285 LEU LEU A . n 
A 1 259 ALA 259 286 286 ALA ALA A . n 
A 1 260 ILE 260 287 287 ILE ILE A . n 
A 1 261 PRO 261 288 288 PRO PRO A . n 
A 1 262 LEU 262 289 289 LEU LEU A . n 
A 1 263 HIS 263 290 290 HIS HIS A . n 
A 1 264 GLN 264 291 291 GLN GLN A . n 
A 1 265 GLY 265 292 292 GLY GLY A . n 
A 1 266 ASP 266 293 293 ASP ASP A . n 
A 1 267 CYS 267 294 294 CYS CYS A . n 
A 1 268 TYR 268 295 295 TYR TYR A . n 
A 1 269 PHE 269 296 296 PHE PHE A . n 
A 1 270 MET 270 297 297 MET MET A . n 
A 1 271 LEU 271 298 298 LEU LEU A . n 
A 1 272 ASP 272 299 299 ASP ASP A . n 
A 1 273 ASP 273 300 300 ASP ASP A . n 
A 1 274 LEU 274 301 301 LEU LEU A . n 
A 1 275 ASN 275 302 302 ASN ASN A . n 
A 1 276 ALA 276 303 303 ALA ALA A . n 
A 1 277 THR 277 304 304 THR THR A . n 
A 1 278 HIS 278 305 305 HIS HIS A . n 
A 1 279 GLN 279 306 306 GLN GLN A . n 
A 1 280 HIS 280 307 307 HIS HIS A . n 
A 1 281 CYS 281 308 308 CYS CYS A . n 
A 1 282 VAL 282 309 309 VAL VAL A . n 
A 1 283 LEU 283 310 310 LEU LEU A . n 
A 1 284 ALA 284 311 311 ALA ALA A . n 
A 1 285 GLY 285 312 312 GLY GLY A . n 
A 1 286 SER 286 313 313 SER SER A . n 
A 1 287 GLN 287 314 314 GLN GLN A . n 
A 1 288 PRO 288 315 315 PRO PRO A . n 
A 1 289 ARG 289 316 316 ARG ARG A . n 
A 1 290 PHE 290 317 317 PHE PHE A . n 
A 1 291 SER 291 318 318 SER SER A . n 
A 1 292 SER 292 319 319 SER SER A . n 
A 1 293 THR 293 320 320 THR THR A . n 
A 1 294 HIS 294 321 321 HIS HIS A . n 
A 1 295 ARG 295 322 322 ARG ARG A . n 
A 1 296 VAL 296 323 323 VAL VAL A . n 
A 1 297 ALA 297 324 324 ALA ALA A . n 
A 1 298 GLU 298 325 325 GLU GLU A . n 
A 1 299 CYS 299 326 326 CYS CYS A . n 
A 1 300 SER 300 327 327 SER SER A . n 
A 1 301 THR 301 328 328 THR THR A . n 
A 1 302 GLY 302 329 329 GLY GLY A . n 
A 1 303 THR 303 330 330 THR THR A . n 
A 1 304 LEU 304 331 331 LEU LEU A . n 
A 1 305 ASP 305 332 332 ASP ASP A . n 
A 1 306 TYR 306 333 333 TYR TYR A . n 
A 1 307 ILE 307 334 334 ILE ILE A . n 
A 1 308 LEU 308 335 335 LEU LEU A . n 
A 1 309 GLN 309 336 336 GLN GLN A . n 
A 1 310 ARG 310 337 337 ARG ARG A . n 
A 1 311 CYS 311 338 338 CYS CYS A . n 
A 1 312 GLN 312 339 339 GLN GLN A . n 
A 1 313 LEU 313 340 340 LEU LEU A . n 
A 1 314 ALA 314 341 341 ALA ALA A . n 
A 1 315 LEU 315 342 342 LEU LEU A . n 
A 1 316 GLN 316 343 343 GLN GLN A . n 
A 1 317 ASN 317 344 344 ASN ASN A . n 
A 1 318 VAL 318 345 345 VAL VAL A . n 
A 1 319 CYS 319 346 346 CYS CYS A . n 
A 1 320 ASP 320 347 347 ASP ASP A . n 
A 1 321 ASP 321 348 348 ASP ASP A . n 
A 1 322 VAL 322 349 349 VAL VAL A . n 
A 1 323 ASP 323 350 350 ASP ASP A . n 
A 1 324 ASN 324 351 351 ASN ASN A . n 
A 1 325 ASP 325 352 352 ASP ASP A . n 
A 1 326 ASP 326 353 353 ASP ASP A . n 
A 1 327 VAL 327 354 354 VAL VAL A . n 
A 1 328 SER 328 355 355 SER SER A . n 
A 1 329 LEU 329 356 356 LEU LEU A . n 
A 1 330 LYS 330 357 357 LYS LYS A . n 
A 1 331 SER 331 358 358 SER SER A . n 
A 1 332 PHE 332 359 359 PHE PHE A . n 
A 1 333 GLU 333 360 360 GLU GLU A . n 
A 1 334 PRO 334 361 361 PRO PRO A . n 
A 1 335 ALA 335 362 362 ALA ALA A . n 
A 1 336 VAL 336 363 363 VAL VAL A . n 
A 1 337 LEU 337 364 364 LEU LEU A . n 
A 1 338 LYS 338 365 365 LYS LYS A . n 
A 1 339 GLN 339 366 366 GLN GLN A . n 
A 1 340 GLY 340 367 367 GLY GLY A . n 
A 1 341 GLU 341 368 368 GLU GLU A . n 
A 1 342 GLU 342 369 369 GLU GLU A . n 
A 1 343 ILE 343 370 370 ILE ILE A . n 
A 1 344 HIS 344 371 371 HIS HIS A . n 
A 1 345 ASN 345 372 372 ASN ASN A . n 
A 1 346 GLU 346 373 373 GLU GLU A . n 
A 1 347 VAL 347 374 374 VAL VAL A . n 
A 1 348 GLU 348 375 375 GLU GLU A . n 
A 1 349 PHE 349 376 376 PHE PHE A . n 
A 1 350 GLU 350 377 377 GLU GLU A . n 
A 1 351 TRP 351 378 378 TRP TRP A . n 
A 1 352 LEU 352 379 379 LEU LEU A . n 
A 1 353 ARG 353 380 380 ARG ARG A . n 
A 1 354 GLN 354 381 381 GLN GLN A . n 
A 1 355 PHE 355 382 382 PHE PHE A . n 
A 1 356 TRP 356 383 383 TRP TRP A . n 
A 1 357 PHE 357 384 384 PHE PHE A . n 
A 1 358 GLN 358 385 385 GLN GLN A . n 
A 1 359 GLY 359 386 386 GLY GLY A . n 
A 1 360 ASN 360 387 387 ASN ASN A . n 
A 1 361 ARG 361 388 388 ARG ARG A . n 
A 1 362 TYR 362 389 389 TYR TYR A . n 
A 1 363 ARG 363 390 390 ARG ARG A . n 
A 1 364 LYS 364 391 391 LYS LYS A . n 
A 1 365 CYS 365 392 392 CYS CYS A . n 
A 1 366 THR 366 393 393 THR THR A . n 
A 1 367 ASP 367 394 394 ASP ASP A . n 
A 1 368 TRP 368 395 395 TRP TRP A . n 
A 1 369 TRP 369 396 396 TRP TRP A . n 
A 1 370 CYS 370 397 397 CYS CYS A . n 
A 1 371 GLN 371 398 398 GLN GLN A . n 
A 1 372 PRO 372 399 399 PRO PRO A . n 
A 1 373 MET 373 400 400 MET MET A . n 
A 1 374 ALA 374 401 401 ALA ALA A . n 
A 1 375 GLN 375 402 402 GLN GLN A . n 
A 1 376 LEU 376 403 403 LEU LEU A . n 
A 1 377 GLU 377 404 404 GLU GLU A . n 
A 1 378 ALA 378 405 405 ALA ALA A . n 
A 1 379 LEU 379 406 406 LEU LEU A . n 
A 1 380 TRP 380 407 407 TRP TRP A . n 
A 1 381 LYS 381 408 408 LYS LYS A . n 
A 1 382 LYS 382 409 409 LYS LYS A . n 
A 1 383 MET 383 410 410 MET MET A . n 
A 1 384 GLU 384 411 411 GLU GLU A . n 
A 1 385 GLY 385 412 412 GLY GLY A . n 
A 1 386 VAL 386 413 413 VAL VAL A . n 
A 1 387 THR 387 414 414 THR THR A . n 
A 1 388 ASN 388 415 415 ASN ASN A . n 
A 1 389 ALA 389 416 416 ALA ALA A . n 
A 1 390 VAL 390 417 417 VAL VAL A . n 
A 1 391 LEU 391 418 418 LEU LEU A . n 
A 1 392 HIS 392 419 419 HIS HIS A . n 
A 1 393 GLU 393 420 420 GLU GLU A . n 
A 1 394 VAL 394 421 421 VAL VAL A . n 
A 1 395 LYS 395 422 422 LYS LYS A . n 
A 1 396 ARG 396 423 423 ARG ARG A . n 
A 1 397 GLU 397 424 424 GLU GLU A . n 
A 1 398 GLY 398 425 425 GLY GLY A . n 
A 1 399 LEU 399 426 426 LEU LEU A . n 
A 1 400 PRO 400 427 427 PRO PRO A . n 
A 1 401 VAL 401 428 428 VAL VAL A . n 
A 1 402 GLU 402 429 429 GLU GLU A . n 
A 1 403 GLN 403 430 430 GLN GLN A . n 
A 1 404 ARG 404 431 431 ARG ARG A . n 
A 1 405 ASN 405 432 432 ASN ASN A . n 
A 1 406 GLU 406 433 433 GLU GLU A . n 
A 1 407 ILE 407 434 434 ILE ILE A . n 
A 1 408 LEU 408 435 435 LEU LEU A . n 
A 1 409 THR 409 436 436 THR THR A . n 
A 1 410 ALA 410 437 437 ALA ALA A . n 
A 1 411 ILE 411 438 438 ILE ILE A . n 
A 1 412 LEU 412 439 439 LEU LEU A . n 
A 1 413 ALA 413 440 440 ALA ALA A . n 
A 1 414 SER 414 441 441 SER SER A . n 
A 1 415 LEU 415 442 442 LEU LEU A . n 
A 1 416 THR 416 443 443 THR THR A . n 
A 1 417 ALA 417 444 444 ALA ALA A . n 
A 1 418 ARG 418 445 445 ARG ARG A . n 
A 1 419 GLN 419 446 446 GLN GLN A . n 
A 1 420 ASN 420 447 447 ASN ASN A . n 
A 1 421 LEU 421 448 448 LEU LEU A . n 
A 1 422 ARG 422 449 449 ARG ARG A . n 
A 1 423 ARG 423 450 450 ARG ARG A . n 
A 1 424 GLU 424 451 451 GLU GLU A . n 
A 1 425 TRP 425 452 452 TRP TRP A . n 
A 1 426 HIS 426 453 453 HIS HIS A . n 
A 1 427 ALA 427 454 454 ALA ALA A . n 
A 1 428 ARG 428 455 455 ARG ARG A . n 
A 1 429 CYS 429 456 456 CYS CYS A . n 
A 1 430 GLN 430 457 457 GLN GLN A . n 
A 1 431 SER 431 458 458 SER SER A . n 
A 1 432 ARG 432 459 459 ARG ARG A . n 
A 1 433 ILE 433 460 460 ILE ILE A . n 
A 1 434 ALA 434 461 461 ALA ALA A . n 
A 1 435 ARG 435 462 462 ARG ARG A . n 
A 1 436 THR 436 463 463 THR THR A . n 
A 1 437 LEU 437 464 464 LEU LEU A . n 
A 1 438 PRO 438 465 465 PRO PRO A . n 
A 1 439 ALA 439 466 466 ALA ALA A . n 
A 1 440 ASP 440 467 467 ASP ASP A . n 
A 1 441 GLN 441 468 468 GLN GLN A . n 
A 1 442 LYS 442 469 469 LYS LYS A . n 
A 1 443 PRO 443 470 470 PRO PRO A . n 
A 1 444 GLU 444 471 471 GLU GLU A . n 
A 1 445 CYS 445 472 472 CYS CYS A . n 
A 1 446 ARG 446 473 473 ARG ARG A . n 
A 1 447 PRO 447 474 474 PRO PRO A . n 
A 1 448 TYR 448 475 475 TYR TYR A . n 
A 1 449 TRP 449 476 476 TRP TRP A . n 
A 1 450 GLU 450 477 477 GLU GLU A . n 
A 1 451 LYS 451 478 478 LYS LYS A . n 
A 1 452 ASP 452 479 479 ASP ASP A . n 
A 1 453 ASP 453 480 480 ASP ASP A . n 
A 1 454 ALA 454 481 481 ALA ALA A . n 
A 1 455 SER 455 482 482 SER SER A . n 
A 1 456 MET 456 483 483 MET MET A . n 
A 1 457 PRO 457 484 484 PRO PRO A . n 
A 1 458 LEU 458 485 485 LEU LEU A . n 
A 1 459 PRO 459 486 486 PRO PRO A . n 
A 1 460 PHE 460 487 487 PHE PHE A . n 
A 1 461 ASP 461 488 488 ASP ASP A . n 
A 1 462 LEU 462 489 489 LEU LEU A . n 
A 1 463 THR 463 490 490 THR THR A . n 
A 1 464 ASP 464 491 491 ASP ASP A . n 
A 1 465 ILE 465 492 492 ILE ILE A . n 
A 1 466 VAL 466 493 493 VAL VAL A . n 
A 1 467 SER 467 494 494 SER SER A . n 
A 1 468 GLU 468 495 495 GLU GLU A . n 
A 1 469 LEU 469 496 496 LEU LEU A . n 
A 1 470 ARG 470 497 497 ARG ARG A . n 
A 1 471 GLY 471 498 498 GLY GLY A . n 
A 1 472 GLN 472 499 499 GLN GLN A . n 
A 1 473 LEU 473 500 500 LEU LEU A . n 
A 1 474 LEU 474 501 501 LEU LEU A . n 
A 1 475 GLU 475 502 502 GLU GLU A . n 
A 1 476 ALA 476 503 ?   ?   ?   A . n 
A 1 477 LYS 477 504 ?   ?   ?   A . n 
A 1 478 PRO 478 505 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EF5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EF5 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 AKG   1  601 601 AKG   AKG A . 
C 3 A1EF5 1  602 602 A1EF5 LIG A . 
D 4 HOH   1  701 20  HOH   HOH A . 
D 4 HOH   2  702 6   HOH   HOH A . 
D 4 HOH   3  703 17  HOH   HOH A . 
D 4 HOH   4  704 1   HOH   HOH A . 
D 4 HOH   5  705 8   HOH   HOH A . 
D 4 HOH   6  706 5   HOH   HOH A . 
D 4 HOH   7  707 4   HOH   HOH A . 
D 4 HOH   8  708 9   HOH   HOH A . 
D 4 HOH   9  709 15  HOH   HOH A . 
D 4 HOH   10 710 7   HOH   HOH A . 
D 4 HOH   11 711 3   HOH   HOH A . 
D 4 HOH   12 712 12  HOH   HOH A . 
D 4 HOH   13 713 11  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 LYS 34  ? CG  ? A LYS 7   CG  
2  1 Y 1 A LYS 34  ? CD  ? A LYS 7   CD  
3  1 Y 1 A LYS 34  ? CE  ? A LYS 7   CE  
4  1 Y 1 A LYS 34  ? NZ  ? A LYS 7   NZ  
5  1 Y 1 A GLN 43  ? CG  ? A GLN 16  CG  
6  1 Y 1 A GLN 43  ? CD  ? A GLN 16  CD  
7  1 Y 1 A GLN 43  ? OE1 ? A GLN 16  OE1 
8  1 Y 1 A GLN 43  ? NE2 ? A GLN 16  NE2 
9  1 Y 1 A LYS 63  ? CG  ? A LYS 36  CG  
10 1 Y 1 A LYS 63  ? CD  ? A LYS 36  CD  
11 1 Y 1 A LYS 63  ? CE  ? A LYS 36  CE  
12 1 Y 1 A LYS 63  ? NZ  ? A LYS 36  NZ  
13 1 Y 1 A LYS 74  ? CG  ? A LYS 47  CG  
14 1 Y 1 A LYS 74  ? CD  ? A LYS 47  CD  
15 1 Y 1 A LYS 74  ? CE  ? A LYS 47  CE  
16 1 Y 1 A LYS 74  ? NZ  ? A LYS 47  NZ  
17 1 Y 1 A LYS 121 ? CG  ? A LYS 94  CG  
18 1 Y 1 A LYS 121 ? CD  ? A LYS 94  CD  
19 1 Y 1 A LYS 121 ? CE  ? A LYS 94  CE  
20 1 Y 1 A LYS 121 ? NZ  ? A LYS 94  NZ  
21 1 Y 1 A LYS 162 ? CG  ? A LYS 135 CG  
22 1 Y 1 A LYS 162 ? CD  ? A LYS 135 CD  
23 1 Y 1 A LYS 162 ? CE  ? A LYS 135 CE  
24 1 Y 1 A LYS 162 ? NZ  ? A LYS 135 NZ  
25 1 Y 1 A GLU 190 ? CG  ? A GLU 163 CG  
26 1 Y 1 A GLU 190 ? CD  ? A GLU 163 CD  
27 1 Y 1 A GLU 190 ? OE1 ? A GLU 163 OE1 
28 1 Y 1 A GLU 190 ? OE2 ? A GLU 163 OE2 
29 1 Y 1 A LYS 194 ? CG  ? A LYS 167 CG  
30 1 Y 1 A LYS 194 ? CD  ? A LYS 167 CD  
31 1 Y 1 A LYS 194 ? CE  ? A LYS 167 CE  
32 1 Y 1 A LYS 194 ? NZ  ? A LYS 167 NZ  
33 1 Y 1 A GLU 250 ? CG  ? A GLU 223 CG  
34 1 Y 1 A GLU 250 ? CD  ? A GLU 223 CD  
35 1 Y 1 A GLU 250 ? OE1 ? A GLU 223 OE1 
36 1 Y 1 A GLU 250 ? OE2 ? A GLU 223 OE2 
37 1 Y 1 A LEU 262 ? CG  ? A LEU 235 CG  
38 1 Y 1 A LEU 262 ? CD1 ? A LEU 235 CD1 
39 1 Y 1 A LEU 262 ? CD2 ? A LEU 235 CD2 
40 1 Y 1 A GLU 263 ? CG  ? A GLU 236 CG  
41 1 Y 1 A GLU 263 ? CD  ? A GLU 236 CD  
42 1 Y 1 A GLU 263 ? OE1 ? A GLU 236 OE1 
43 1 Y 1 A GLU 263 ? OE2 ? A GLU 236 OE2 
44 1 Y 1 A GLN 314 ? CD  ? A GLN 287 CD  
45 1 Y 1 A GLN 314 ? OE1 ? A GLN 287 OE1 
46 1 Y 1 A GLN 314 ? NE2 ? A GLN 287 NE2 
47 1 Y 1 A ASP 353 ? CG  ? A ASP 326 CG  
48 1 Y 1 A ASP 353 ? OD1 ? A ASP 326 OD1 
49 1 Y 1 A ASP 353 ? OD2 ? A ASP 326 OD2 
50 1 Y 1 A ASN 387 ? CG  ? A ASN 360 CG  
51 1 Y 1 A ASN 387 ? OD1 ? A ASN 360 OD1 
52 1 Y 1 A ASN 387 ? ND2 ? A ASN 360 ND2 
53 1 Y 1 A TYR 389 ? CG  ? A TYR 362 CG  
54 1 Y 1 A TYR 389 ? CD1 ? A TYR 362 CD1 
55 1 Y 1 A TYR 389 ? CD2 ? A TYR 362 CD2 
56 1 Y 1 A TYR 389 ? CE1 ? A TYR 362 CE1 
57 1 Y 1 A TYR 389 ? CE2 ? A TYR 362 CE2 
58 1 Y 1 A TYR 389 ? CZ  ? A TYR 362 CZ  
59 1 Y 1 A TYR 389 ? OH  ? A TYR 362 OH  
60 1 Y 1 A ARG 390 ? CG  ? A ARG 363 CG  
61 1 Y 1 A ARG 390 ? CD  ? A ARG 363 CD  
62 1 Y 1 A ARG 390 ? NE  ? A ARG 363 NE  
63 1 Y 1 A ARG 390 ? CZ  ? A ARG 363 CZ  
64 1 Y 1 A ARG 390 ? NH1 ? A ARG 363 NH1 
65 1 Y 1 A ARG 390 ? NH2 ? A ARG 363 NH2 
66 1 Y 1 A GLU 502 ? CG  ? A GLU 475 CG  
67 1 Y 1 A GLU 502 ? CD  ? A GLU 475 CD  
68 1 Y 1 A GLU 502 ? OE1 ? A GLU 475 OE1 
69 1 Y 1 A GLU 502 ? OE2 ? A GLU 475 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.19.1_4122: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KNI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     141.410 
_cell.length_a_esd                 ? 
_cell.length_b                     141.410 
_cell.length_b_esd                 ? 
_cell.length_c                     83.850 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        9 
_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                         9KNI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3' 
_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                   9KNI 
_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             3.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.47 
_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    
;100 mM sodium citrate, pH 5.4, 
12.0% (w/v) polyethylene glycol (PEG) 3350, 8% isopropanol
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-21 
_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   0.9735 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9735 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KNI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.63 
_reflns.d_resolution_low                               49.45 
_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                                     18535 
_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                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.067 
_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                                    2.63 
_reflns_shell.d_res_low                                     2.70 
_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                             18522 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.07 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9KNI 
_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                            2.63 
_refine.ls_d_res_low                             31.48 
_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                     18522 
_refine.ls_number_reflns_R_free                  935 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.68 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2000 
_refine.ls_R_factor_R_free                       0.2273 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1985 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.96 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.08 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.34 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.63 
_refine_hist.d_res_low                        31.48 
_refine_hist.number_atoms_solvent             13 
_refine_hist.number_atoms_total               3507 
_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        3460 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_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' ? 0.002 ? 3582 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.574 ? 4870 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.161 ? 492  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.040 ? 527  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004 ? 641  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.63 2.77  . . 132 2522 100.00 . . . . 0.3144 . . . . . . . . . . . 0.3695 
'X-RAY DIFFRACTION' 2.77 2.94  . . 152 2516 100.00 . . . . 0.2833 . . . . . . . . . . . 0.3221 
'X-RAY DIFFRACTION' 2.94 3.17  . . 140 2490 100.00 . . . . 0.2794 . . . . . . . . . . . 0.3101 
'X-RAY DIFFRACTION' 3.17 3.49  . . 85  2577 100.00 . . . . 0.2482 . . . . . . . . . . . 0.3104 
'X-RAY DIFFRACTION' 3.49 3.99  . . 169 2470 100.00 . . . . 0.2102 . . . . . . . . . . . 0.2278 
'X-RAY DIFFRACTION' 3.99 5.02  . . 121 2505 99.00  . . . . 0.1675 . . . . . . . . . . . 0.2532 
'X-RAY DIFFRACTION' 5.03 31.48 . . 136 2507 99.00  . . . . 0.1629 . . . . . . . . . . . 0.1577 
# 
_struct.entry_id                     9KNI 
_struct.title                        'Structural complex of FTO bound with 12j' 
_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        9KNI 
_struct_keywords.text            'm6A eraser, FTO Inhibitor, Complex, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FTO_HUMAN 
_struct_ref.pdbx_db_accession          Q9C0B1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TPKDDEFYQQWQLKYPKLILREASSVSEELHKEVQEAFLTLHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYKYLNT
RLFTVPWPVKGSNIKHTEAEIAAACETFLKLNDYLQIETIQALEELAAKEKANEDAVPLCMSADFPRVGMGSSYNGQDEV
DIKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGPEEESEDDSHLEGRDPDIWH
VGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLALQNVCDDVDN
DDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEGVTNAVLHEVKREGLPVEQR
NEILTAILASLTARQNLRREWHARCQSRIARTLPADQKPECRPYWEKDDASMPLPFDLTDIVSELRGQLLEAKP
;
_struct_ref.pdbx_align_begin           32 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9KNI 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 5 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 478 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9C0B1 
_struct_ref_seq.db_align_beg                  32 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  505 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       32 
_struct_ref_seq.pdbx_auth_seq_align_end       505 
# 
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 9KNI GLY A 1 ? UNP Q9C0B1 ? ? 'expression tag' 28 1 
1 9KNI SER A 2 ? UNP Q9C0B1 ? ? 'expression tag' 29 2 
1 9KNI HIS A 3 ? UNP Q9C0B1 ? ? 'expression tag' 30 3 
1 9KNI MET A 4 ? UNP Q9C0B1 ? ? 'expression tag' 31 4 
# 
_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 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 10  ? TYR A 19  ? GLU A 37  TYR A 46  1 ? 10 
HELX_P HELX_P2  AA2 GLU A 26  ? VAL A 30  ? GLU A 53  VAL A 57  5 ? 5  
HELX_P HELX_P3  AA3 SER A 31  ? HIS A 48  ? SER A 58  HIS A 75  1 ? 18 
HELX_P HELX_P4  AA4 ALA A 103 ? ALA A 136 ? ALA A 130 ALA A 163 1 ? 34 
HELX_P HELX_P5  AA5 ASP A 162 ? ARG A 169 ? ASP A 189 ARG A 196 1 ? 8  
HELX_P HELX_P6  AA6 ASP A 181 ? MET A 185 ? ASP A 208 MET A 212 5 ? 5  
HELX_P HELX_P7  AA7 ASP A 273 ? THR A 277 ? ASP A 300 THR A 304 1 ? 5  
HELX_P HELX_P8  AA8 THR A 303 ? LEU A 315 ? THR A 330 LEU A 342 1 ? 13 
HELX_P HELX_P9  AA9 GLN A 316 ? VAL A 318 ? GLN A 343 VAL A 345 5 ? 3  
HELX_P HELX_P10 AB1 GLU A 333 ? TRP A 351 ? GLU A 360 TRP A 378 1 ? 19 
HELX_P HELX_P11 AB2 TRP A 351 ? PHE A 357 ? TRP A 378 PHE A 384 1 ? 7  
HELX_P HELX_P12 AB3 ARG A 361 ? CYS A 365 ? ARG A 388 CYS A 392 5 ? 5  
HELX_P HELX_P13 AB4 TRP A 369 ? LYS A 395 ? TRP A 396 LYS A 422 1 ? 27 
HELX_P HELX_P14 AB5 PRO A 400 ? GLN A 430 ? PRO A 427 GLN A 457 1 ? 31 
HELX_P HELX_P15 AB6 SER A 431 ? LEU A 437 ? SER A 458 LEU A 464 1 ? 7  
HELX_P HELX_P16 AB7 PRO A 438 ? LYS A 442 ? PRO A 465 LYS A 469 5 ? 5  
HELX_P HELX_P17 AB8 LEU A 462 ? GLU A 475 ? LEU A 489 GLU A 502 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ARG 
_struct_mon_prot_cis.label_seq_id           446 
_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           ARG 
_struct_mon_prot_cis.auth_seq_id            473 
_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    447 
_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     474 
_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       -2.02 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 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 HIS A 3   ? MET A 4   ? HIS A 30  MET A 31  
AA1 2 GLY A 257 ? PRO A 261 ? GLY A 284 PRO A 288 
AA1 3 HIS A 244 ? ILE A 249 ? HIS A 271 ILE A 276 
AA1 4 HIS A 278 ? LEU A 283 ? HIS A 305 LEU A 310 
AA1 5 MET A 199 ? HIS A 204 ? MET A 226 HIS A 231 
AA2 1 LEU A 22  ? ARG A 25  ? LEU A 49  ARG A 52  
AA2 2 CYS A 267 ? MET A 270 ? CYS A 294 MET A 297 
AA2 3 VAL A 215 ? SER A 221 ? VAL A 242 SER A 248 
AA2 4 ARG A 289 ? ARG A 295 ? ARG A 316 ARG A 322 
AA2 5 VAL A 174 ? MET A 180 ? VAL A 201 MET A 207 
AA2 6 SER A 68  ? GLY A 73  ? SER A 95  GLY A 100 
AA2 7 VAL A 89  ? PRO A 90  ? VAL A 116 PRO A 117 
AA3 1 LEU A 55  ? ILE A 58  ? LEU A 82  ILE A 85  
AA3 2 LYS A 61  ? LEU A 64  ? LYS A 88  LEU A 91  
AA4 1 THR A 78  ? TYR A 81  ? THR A 105 TYR A 108 
AA4 2 THR A 84  ? PHE A 87  ? THR A 111 PHE A 114 
# 
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 MET A 4   ? N MET A 31  O ALA A 259 ? O ALA A 286 
AA1 2 3 O ILE A 260 ? O ILE A 287 N VAL A 245 ? N VAL A 272 
AA1 3 4 N HIS A 244 ? N HIS A 271 O LEU A 283 ? O LEU A 310 
AA1 4 5 O VAL A 282 ? O VAL A 309 N ALA A 200 ? N ALA A 227 
AA2 1 2 N ARG A 25  ? N ARG A 52  O CYS A 267 ? O CYS A 294 
AA2 2 3 O MET A 270 ? O MET A 297 N VAL A 215 ? N VAL A 242 
AA2 3 4 N ALA A 216 ? N ALA A 243 O HIS A 294 ? O HIS A 321 
AA2 4 5 O SER A 291 ? O SER A 318 N ASN A 178 ? N ASN A 205 
AA2 5 6 O PHE A 179 ? O PHE A 206 N SER A 68  ? N SER A 95  
AA2 6 7 N LEU A 71  ? N LEU A 98  O VAL A 89  ? O VAL A 116 
AA3 1 2 N ILE A 58  ? N ILE A 85  O LYS A 61  ? O LYS A 88  
AA4 1 2 N TYR A 79  ? N TYR A 106 O LEU A 86  ? O LEU A 113 
# 
_pdbx_entry_details.entry_id                   9KNI 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 LEU A 82  ? ? -106.65 77.90   
2 1 PRO A 119 ? ? -69.31  90.64   
3 1 ASP A 299 ? ? 59.32   -127.49 
4 1 ASP A 347 ? ? -96.34  37.32   
5 1 TRP A 378 ? ? -129.75 -58.93  
6 1 GLN A 457 ? ? -116.23 61.05   
7 1 CYS A 472 ? ? -84.87  47.82   
# 
_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         21.1012 
_pdbx_refine_tls.origin_y         12.1660 
_pdbx_refine_tls.origin_z         29.6243 
_pdbx_refine_tls.T[1][1]          0.5076 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0195 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0399 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4308 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0370 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.4942 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          5.1030 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -1.8015 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -1.7474 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.0429 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.9877 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.1155 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.2476 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1446 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.2794 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.1859 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0514 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.2182 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.3567 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1375 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.2044 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 123 ? A SER 96  
2  1 Y 1 A ASN 124 ? A ASN 97  
3  1 Y 1 A ILE 125 ? A ILE 98  
4  1 Y 1 A LYS 126 ? A LYS 99  
5  1 Y 1 A HIS 127 ? A HIS 100 
6  1 Y 1 A THR 128 ? A THR 101 
7  1 Y 1 A ASN 164 ? A ASN 137 
8  1 Y 1 A GLU 165 ? A GLU 138 
9  1 Y 1 A ASP 166 ? A ASP 139 
10 1 Y 1 A ALA 167 ? A ALA 140 
11 1 Y 1 A VAL 168 ? A VAL 141 
12 1 Y 1 A PRO 169 ? A PRO 142 
13 1 Y 1 A LEU 170 ? A LEU 143 
14 1 Y 1 A CYS 171 ? A CYS 144 
15 1 Y 1 A MET 172 ? A MET 145 
16 1 Y 1 A SER 173 ? A SER 146 
17 1 Y 1 A ALA 174 ? A ALA 147 
18 1 Y 1 A ASP 175 ? A ASP 148 
19 1 Y 1 A PHE 176 ? A PHE 149 
20 1 Y 1 A PRO 177 ? A PRO 150 
21 1 Y 1 A ARG 178 ? A ARG 151 
22 1 Y 1 A VAL 179 ? A VAL 152 
23 1 Y 1 A GLY 180 ? A GLY 153 
24 1 Y 1 A MET 181 ? A MET 154 
25 1 Y 1 A GLY 182 ? A GLY 155 
26 1 Y 1 A SER 183 ? A SER 156 
27 1 Y 1 A SER 184 ? A SER 157 
28 1 Y 1 A TYR 185 ? A TYR 158 
29 1 Y 1 A ASN 186 ? A ASN 159 
30 1 Y 1 A GLY 187 ? A GLY 160 
31 1 Y 1 A GLY 251 ? A GLY 224 
32 1 Y 1 A PRO 252 ? A PRO 225 
33 1 Y 1 A GLU 253 ? A GLU 226 
34 1 Y 1 A GLU 254 ? A GLU 227 
35 1 Y 1 A GLU 255 ? A GLU 228 
36 1 Y 1 A SER 256 ? A SER 229 
37 1 Y 1 A GLU 257 ? A GLU 230 
38 1 Y 1 A ASP 258 ? A ASP 231 
39 1 Y 1 A ASP 259 ? A ASP 232 
40 1 Y 1 A SER 260 ? A SER 233 
41 1 Y 1 A HIS 261 ? A HIS 234 
42 1 Y 1 A ALA 503 ? A ALA 476 
43 1 Y 1 A LYS 504 ? A LYS 477 
44 1 Y 1 A PRO 505 ? A PRO 478 
# 
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 
A1EF5 N3   N  Y N 1   
A1EF5 C5   C  Y N 2   
A1EF5 C6   C  N N 3   
A1EF5 C7   C  Y N 4   
A1EF5 C8   C  Y N 5   
A1EF5 C10  C  Y N 6   
A1EF5 C15  C  Y N 7   
A1EF5 C22  C  Y N 8   
A1EF5 C24  C  Y N 9   
A1EF5 C1   C  N N 10  
A1EF5 C12  C  Y N 11  
A1EF5 C14  C  Y N 12  
A1EF5 C16  C  Y N 13  
A1EF5 C18  C  Y N 14  
A1EF5 C19  C  N N 15  
A1EF5 C2   C  Y N 16  
A1EF5 C9   C  Y N 17  
A1EF5 N13  N  N N 18  
A1EF5 N4   N  Y N 19  
A1EF5 O20  O  N N 20  
A1EF5 O21  O  N N 21  
A1EF5 S17  S  Y N 22  
A1EF5 CL11 CL N N 23  
A1EF5 CL23 CL N N 24  
A1EF5 H1   H  N N 25  
A1EF5 H2   H  N N 26  
A1EF5 H3   H  N N 27  
A1EF5 H4   H  N N 28  
A1EF5 H5   H  N N 29  
A1EF5 H6   H  N N 30  
A1EF5 H7   H  N N 31  
A1EF5 H8   H  N N 32  
A1EF5 H9   H  N N 33  
A1EF5 H10  H  N N 34  
A1EF5 H11  H  N N 35  
A1EF5 H12  H  N N 36  
A1EF5 H13  H  N N 37  
AKG   C1   C  N N 38  
AKG   O1   O  N N 39  
AKG   O2   O  N N 40  
AKG   C2   C  N N 41  
AKG   O5   O  N N 42  
AKG   C3   C  N N 43  
AKG   C4   C  N N 44  
AKG   C5   C  N N 45  
AKG   O3   O  N N 46  
AKG   O4   O  N N 47  
AKG   HO2  H  N N 48  
AKG   H31  H  N N 49  
AKG   H32  H  N N 50  
AKG   H41  H  N N 51  
AKG   H42  H  N N 52  
AKG   HO4  H  N N 53  
ALA   N    N  N N 54  
ALA   CA   C  N S 55  
ALA   C    C  N N 56  
ALA   O    O  N N 57  
ALA   CB   C  N N 58  
ALA   OXT  O  N N 59  
ALA   H    H  N N 60  
ALA   H2   H  N N 61  
ALA   HA   H  N N 62  
ALA   HB1  H  N N 63  
ALA   HB2  H  N N 64  
ALA   HB3  H  N N 65  
ALA   HXT  H  N N 66  
ARG   N    N  N N 67  
ARG   CA   C  N S 68  
ARG   C    C  N N 69  
ARG   O    O  N N 70  
ARG   CB   C  N N 71  
ARG   CG   C  N N 72  
ARG   CD   C  N N 73  
ARG   NE   N  N N 74  
ARG   CZ   C  N N 75  
ARG   NH1  N  N N 76  
ARG   NH2  N  N N 77  
ARG   OXT  O  N N 78  
ARG   H    H  N N 79  
ARG   H2   H  N N 80  
ARG   HA   H  N N 81  
ARG   HB2  H  N N 82  
ARG   HB3  H  N N 83  
ARG   HG2  H  N N 84  
ARG   HG3  H  N N 85  
ARG   HD2  H  N N 86  
ARG   HD3  H  N N 87  
ARG   HE   H  N N 88  
ARG   HH11 H  N N 89  
ARG   HH12 H  N N 90  
ARG   HH21 H  N N 91  
ARG   HH22 H  N N 92  
ARG   HXT  H  N N 93  
ASN   N    N  N N 94  
ASN   CA   C  N S 95  
ASN   C    C  N N 96  
ASN   O    O  N N 97  
ASN   CB   C  N N 98  
ASN   CG   C  N N 99  
ASN   OD1  O  N N 100 
ASN   ND2  N  N N 101 
ASN   OXT  O  N N 102 
ASN   H    H  N N 103 
ASN   H2   H  N N 104 
ASN   HA   H  N N 105 
ASN   HB2  H  N N 106 
ASN   HB3  H  N N 107 
ASN   HD21 H  N N 108 
ASN   HD22 H  N N 109 
ASN   HXT  H  N N 110 
ASP   N    N  N N 111 
ASP   CA   C  N S 112 
ASP   C    C  N N 113 
ASP   O    O  N N 114 
ASP   CB   C  N N 115 
ASP   CG   C  N N 116 
ASP   OD1  O  N N 117 
ASP   OD2  O  N N 118 
ASP   OXT  O  N N 119 
ASP   H    H  N N 120 
ASP   H2   H  N N 121 
ASP   HA   H  N N 122 
ASP   HB2  H  N N 123 
ASP   HB3  H  N N 124 
ASP   HD2  H  N N 125 
ASP   HXT  H  N N 126 
CYS   N    N  N N 127 
CYS   CA   C  N R 128 
CYS   C    C  N N 129 
CYS   O    O  N N 130 
CYS   CB   C  N N 131 
CYS   SG   S  N N 132 
CYS   OXT  O  N N 133 
CYS   H    H  N N 134 
CYS   H2   H  N N 135 
CYS   HA   H  N N 136 
CYS   HB2  H  N N 137 
CYS   HB3  H  N N 138 
CYS   HG   H  N N 139 
CYS   HXT  H  N N 140 
GLN   N    N  N N 141 
GLN   CA   C  N S 142 
GLN   C    C  N N 143 
GLN   O    O  N N 144 
GLN   CB   C  N N 145 
GLN   CG   C  N N 146 
GLN   CD   C  N N 147 
GLN   OE1  O  N N 148 
GLN   NE2  N  N N 149 
GLN   OXT  O  N N 150 
GLN   H    H  N N 151 
GLN   H2   H  N N 152 
GLN   HA   H  N N 153 
GLN   HB2  H  N N 154 
GLN   HB3  H  N N 155 
GLN   HG2  H  N N 156 
GLN   HG3  H  N N 157 
GLN   HE21 H  N N 158 
GLN   HE22 H  N N 159 
GLN   HXT  H  N N 160 
GLU   N    N  N N 161 
GLU   CA   C  N S 162 
GLU   C    C  N N 163 
GLU   O    O  N N 164 
GLU   CB   C  N N 165 
GLU   CG   C  N N 166 
GLU   CD   C  N N 167 
GLU   OE1  O  N N 168 
GLU   OE2  O  N N 169 
GLU   OXT  O  N N 170 
GLU   H    H  N N 171 
GLU   H2   H  N N 172 
GLU   HA   H  N N 173 
GLU   HB2  H  N N 174 
GLU   HB3  H  N N 175 
GLU   HG2  H  N N 176 
GLU   HG3  H  N N 177 
GLU   HE2  H  N N 178 
GLU   HXT  H  N N 179 
GLY   N    N  N N 180 
GLY   CA   C  N N 181 
GLY   C    C  N N 182 
GLY   O    O  N N 183 
GLY   OXT  O  N N 184 
GLY   H    H  N N 185 
GLY   H2   H  N N 186 
GLY   HA2  H  N N 187 
GLY   HA3  H  N N 188 
GLY   HXT  H  N N 189 
HIS   N    N  N N 190 
HIS   CA   C  N S 191 
HIS   C    C  N N 192 
HIS   O    O  N N 193 
HIS   CB   C  N N 194 
HIS   CG   C  Y N 195 
HIS   ND1  N  Y N 196 
HIS   CD2  C  Y N 197 
HIS   CE1  C  Y N 198 
HIS   NE2  N  Y N 199 
HIS   OXT  O  N N 200 
HIS   H    H  N N 201 
HIS   H2   H  N N 202 
HIS   HA   H  N N 203 
HIS   HB2  H  N N 204 
HIS   HB3  H  N N 205 
HIS   HD1  H  N N 206 
HIS   HD2  H  N N 207 
HIS   HE1  H  N N 208 
HIS   HE2  H  N N 209 
HIS   HXT  H  N N 210 
HOH   O    O  N N 211 
HOH   H1   H  N N 212 
HOH   H2   H  N N 213 
ILE   N    N  N N 214 
ILE   CA   C  N S 215 
ILE   C    C  N N 216 
ILE   O    O  N N 217 
ILE   CB   C  N S 218 
ILE   CG1  C  N N 219 
ILE   CG2  C  N N 220 
ILE   CD1  C  N N 221 
ILE   OXT  O  N N 222 
ILE   H    H  N N 223 
ILE   H2   H  N N 224 
ILE   HA   H  N N 225 
ILE   HB   H  N N 226 
ILE   HG12 H  N N 227 
ILE   HG13 H  N N 228 
ILE   HG21 H  N N 229 
ILE   HG22 H  N N 230 
ILE   HG23 H  N N 231 
ILE   HD11 H  N N 232 
ILE   HD12 H  N N 233 
ILE   HD13 H  N N 234 
ILE   HXT  H  N N 235 
LEU   N    N  N N 236 
LEU   CA   C  N S 237 
LEU   C    C  N N 238 
LEU   O    O  N N 239 
LEU   CB   C  N N 240 
LEU   CG   C  N N 241 
LEU   CD1  C  N N 242 
LEU   CD2  C  N N 243 
LEU   OXT  O  N N 244 
LEU   H    H  N N 245 
LEU   H2   H  N N 246 
LEU   HA   H  N N 247 
LEU   HB2  H  N N 248 
LEU   HB3  H  N N 249 
LEU   HG   H  N N 250 
LEU   HD11 H  N N 251 
LEU   HD12 H  N N 252 
LEU   HD13 H  N N 253 
LEU   HD21 H  N N 254 
LEU   HD22 H  N N 255 
LEU   HD23 H  N N 256 
LEU   HXT  H  N N 257 
LYS   N    N  N N 258 
LYS   CA   C  N S 259 
LYS   C    C  N N 260 
LYS   O    O  N N 261 
LYS   CB   C  N N 262 
LYS   CG   C  N N 263 
LYS   CD   C  N N 264 
LYS   CE   C  N N 265 
LYS   NZ   N  N N 266 
LYS   OXT  O  N N 267 
LYS   H    H  N N 268 
LYS   H2   H  N N 269 
LYS   HA   H  N N 270 
LYS   HB2  H  N N 271 
LYS   HB3  H  N N 272 
LYS   HG2  H  N N 273 
LYS   HG3  H  N N 274 
LYS   HD2  H  N N 275 
LYS   HD3  H  N N 276 
LYS   HE2  H  N N 277 
LYS   HE3  H  N N 278 
LYS   HZ1  H  N N 279 
LYS   HZ2  H  N N 280 
LYS   HZ3  H  N N 281 
LYS   HXT  H  N N 282 
MET   N    N  N N 283 
MET   CA   C  N S 284 
MET   C    C  N N 285 
MET   O    O  N N 286 
MET   CB   C  N N 287 
MET   CG   C  N N 288 
MET   SD   S  N N 289 
MET   CE   C  N N 290 
MET   OXT  O  N N 291 
MET   H    H  N N 292 
MET   H2   H  N N 293 
MET   HA   H  N N 294 
MET   HB2  H  N N 295 
MET   HB3  H  N N 296 
MET   HG2  H  N N 297 
MET   HG3  H  N N 298 
MET   HE1  H  N N 299 
MET   HE2  H  N N 300 
MET   HE3  H  N N 301 
MET   HXT  H  N N 302 
PHE   N    N  N N 303 
PHE   CA   C  N S 304 
PHE   C    C  N N 305 
PHE   O    O  N N 306 
PHE   CB   C  N N 307 
PHE   CG   C  Y N 308 
PHE   CD1  C  Y N 309 
PHE   CD2  C  Y N 310 
PHE   CE1  C  Y N 311 
PHE   CE2  C  Y N 312 
PHE   CZ   C  Y N 313 
PHE   OXT  O  N N 314 
PHE   H    H  N N 315 
PHE   H2   H  N N 316 
PHE   HA   H  N N 317 
PHE   HB2  H  N N 318 
PHE   HB3  H  N N 319 
PHE   HD1  H  N N 320 
PHE   HD2  H  N N 321 
PHE   HE1  H  N N 322 
PHE   HE2  H  N N 323 
PHE   HZ   H  N N 324 
PHE   HXT  H  N N 325 
PRO   N    N  N N 326 
PRO   CA   C  N S 327 
PRO   C    C  N N 328 
PRO   O    O  N N 329 
PRO   CB   C  N N 330 
PRO   CG   C  N N 331 
PRO   CD   C  N N 332 
PRO   OXT  O  N N 333 
PRO   H    H  N N 334 
PRO   HA   H  N N 335 
PRO   HB2  H  N N 336 
PRO   HB3  H  N N 337 
PRO   HG2  H  N N 338 
PRO   HG3  H  N N 339 
PRO   HD2  H  N N 340 
PRO   HD3  H  N N 341 
PRO   HXT  H  N N 342 
SER   N    N  N N 343 
SER   CA   C  N S 344 
SER   C    C  N N 345 
SER   O    O  N N 346 
SER   CB   C  N N 347 
SER   OG   O  N N 348 
SER   OXT  O  N N 349 
SER   H    H  N N 350 
SER   H2   H  N N 351 
SER   HA   H  N N 352 
SER   HB2  H  N N 353 
SER   HB3  H  N N 354 
SER   HG   H  N N 355 
SER   HXT  H  N N 356 
THR   N    N  N N 357 
THR   CA   C  N S 358 
THR   C    C  N N 359 
THR   O    O  N N 360 
THR   CB   C  N R 361 
THR   OG1  O  N N 362 
THR   CG2  C  N N 363 
THR   OXT  O  N N 364 
THR   H    H  N N 365 
THR   H2   H  N N 366 
THR   HA   H  N N 367 
THR   HB   H  N N 368 
THR   HG1  H  N N 369 
THR   HG21 H  N N 370 
THR   HG22 H  N N 371 
THR   HG23 H  N N 372 
THR   HXT  H  N N 373 
TRP   N    N  N N 374 
TRP   CA   C  N S 375 
TRP   C    C  N N 376 
TRP   O    O  N N 377 
TRP   CB   C  N N 378 
TRP   CG   C  Y N 379 
TRP   CD1  C  Y N 380 
TRP   CD2  C  Y N 381 
TRP   NE1  N  Y N 382 
TRP   CE2  C  Y N 383 
TRP   CE3  C  Y N 384 
TRP   CZ2  C  Y N 385 
TRP   CZ3  C  Y N 386 
TRP   CH2  C  Y N 387 
TRP   OXT  O  N N 388 
TRP   H    H  N N 389 
TRP   H2   H  N N 390 
TRP   HA   H  N N 391 
TRP   HB2  H  N N 392 
TRP   HB3  H  N N 393 
TRP   HD1  H  N N 394 
TRP   HE1  H  N N 395 
TRP   HE3  H  N N 396 
TRP   HZ2  H  N N 397 
TRP   HZ3  H  N N 398 
TRP   HH2  H  N N 399 
TRP   HXT  H  N N 400 
TYR   N    N  N N 401 
TYR   CA   C  N S 402 
TYR   C    C  N N 403 
TYR   O    O  N N 404 
TYR   CB   C  N N 405 
TYR   CG   C  Y N 406 
TYR   CD1  C  Y N 407 
TYR   CD2  C  Y N 408 
TYR   CE1  C  Y N 409 
TYR   CE2  C  Y N 410 
TYR   CZ   C  Y N 411 
TYR   OH   O  N N 412 
TYR   OXT  O  N N 413 
TYR   H    H  N N 414 
TYR   H2   H  N N 415 
TYR   HA   H  N N 416 
TYR   HB2  H  N N 417 
TYR   HB3  H  N N 418 
TYR   HD1  H  N N 419 
TYR   HD2  H  N N 420 
TYR   HE1  H  N N 421 
TYR   HE2  H  N N 422 
TYR   HH   H  N N 423 
TYR   HXT  H  N N 424 
VAL   N    N  N N 425 
VAL   CA   C  N S 426 
VAL   C    C  N N 427 
VAL   O    O  N N 428 
VAL   CB   C  N N 429 
VAL   CG1  C  N N 430 
VAL   CG2  C  N N 431 
VAL   OXT  O  N N 432 
VAL   H    H  N N 433 
VAL   H2   H  N N 434 
VAL   HA   H  N N 435 
VAL   HB   H  N N 436 
VAL   HG11 H  N N 437 
VAL   HG12 H  N N 438 
VAL   HG13 H  N N 439 
VAL   HG21 H  N N 440 
VAL   HG22 H  N N 441 
VAL   HG23 H  N N 442 
VAL   HXT  H  N N 443 
# 
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 
A1EF5 C6  C5   sing N N 1   
A1EF5 N4  C5   doub Y N 2   
A1EF5 N4  N3   sing Y N 3   
A1EF5 C5  C7   sing Y N 4   
A1EF5 N3  C2   sing Y N 5   
A1EF5 C7  C2   doub Y N 6   
A1EF5 C7  C8   sing N N 7   
A1EF5 C2  C1   sing N N 8   
A1EF5 C8  C24  doub Y N 9   
A1EF5 C8  C9   sing Y N 10  
A1EF5 C24 C22  sing Y N 11  
A1EF5 C9  C10  doub Y N 12  
A1EF5 C22 CL23 sing N N 13  
A1EF5 C22 C12  doub Y N 14  
A1EF5 C10 C12  sing Y N 15  
A1EF5 C10 CL11 sing N N 16  
A1EF5 C12 N13  sing N N 17  
A1EF5 N13 C14  sing N N 18  
A1EF5 O20 C19  doub N N 19  
A1EF5 C14 C15  sing Y N 20  
A1EF5 C14 C18  doub Y N 21  
A1EF5 C19 C18  sing N N 22  
A1EF5 C19 O21  sing N N 23  
A1EF5 C15 C16  doub Y N 24  
A1EF5 C18 S17  sing Y N 25  
A1EF5 C16 S17  sing Y N 26  
A1EF5 N3  H1   sing N N 27  
A1EF5 C6  H2   sing N N 28  
A1EF5 C6  H3   sing N N 29  
A1EF5 C6  H4   sing N N 30  
A1EF5 C15 H5   sing N N 31  
A1EF5 C24 H6   sing N N 32  
A1EF5 C1  H7   sing N N 33  
A1EF5 C1  H8   sing N N 34  
A1EF5 C1  H9   sing N N 35  
A1EF5 C16 H10  sing N N 36  
A1EF5 C9  H11  sing N N 37  
A1EF5 N13 H12  sing N N 38  
A1EF5 O21 H13  sing N N 39  
AKG   C1  O1   doub N N 40  
AKG   C1  O2   sing N N 41  
AKG   C1  C2   sing N N 42  
AKG   O2  HO2  sing N N 43  
AKG   C2  O5   doub N N 44  
AKG   C2  C3   sing N N 45  
AKG   C3  C4   sing N N 46  
AKG   C3  H31  sing N N 47  
AKG   C3  H32  sing N N 48  
AKG   C4  C5   sing N N 49  
AKG   C4  H41  sing N N 50  
AKG   C4  H42  sing N N 51  
AKG   C5  O3   doub N N 52  
AKG   C5  O4   sing N N 53  
AKG   O4  HO4  sing N N 54  
ALA   N   CA   sing N N 55  
ALA   N   H    sing N N 56  
ALA   N   H2   sing N N 57  
ALA   CA  C    sing N N 58  
ALA   CA  CB   sing N N 59  
ALA   CA  HA   sing N N 60  
ALA   C   O    doub N N 61  
ALA   C   OXT  sing N N 62  
ALA   CB  HB1  sing N N 63  
ALA   CB  HB2  sing N N 64  
ALA   CB  HB3  sing N N 65  
ALA   OXT HXT  sing N N 66  
ARG   N   CA   sing N N 67  
ARG   N   H    sing N N 68  
ARG   N   H2   sing N N 69  
ARG   CA  C    sing N N 70  
ARG   CA  CB   sing N N 71  
ARG   CA  HA   sing N N 72  
ARG   C   O    doub N N 73  
ARG   C   OXT  sing N N 74  
ARG   CB  CG   sing N N 75  
ARG   CB  HB2  sing N N 76  
ARG   CB  HB3  sing N N 77  
ARG   CG  CD   sing N N 78  
ARG   CG  HG2  sing N N 79  
ARG   CG  HG3  sing N N 80  
ARG   CD  NE   sing N N 81  
ARG   CD  HD2  sing N N 82  
ARG   CD  HD3  sing N N 83  
ARG   NE  CZ   sing N N 84  
ARG   NE  HE   sing N N 85  
ARG   CZ  NH1  sing N N 86  
ARG   CZ  NH2  doub N N 87  
ARG   NH1 HH11 sing N N 88  
ARG   NH1 HH12 sing N N 89  
ARG   NH2 HH21 sing N N 90  
ARG   NH2 HH22 sing N N 91  
ARG   OXT HXT  sing N N 92  
ASN   N   CA   sing N N 93  
ASN   N   H    sing N N 94  
ASN   N   H2   sing N N 95  
ASN   CA  C    sing N N 96  
ASN   CA  CB   sing N N 97  
ASN   CA  HA   sing N N 98  
ASN   C   O    doub N N 99  
ASN   C   OXT  sing N N 100 
ASN   CB  CG   sing N N 101 
ASN   CB  HB2  sing N N 102 
ASN   CB  HB3  sing N N 103 
ASN   CG  OD1  doub N N 104 
ASN   CG  ND2  sing N N 105 
ASN   ND2 HD21 sing N N 106 
ASN   ND2 HD22 sing N N 107 
ASN   OXT HXT  sing N N 108 
ASP   N   CA   sing N N 109 
ASP   N   H    sing N N 110 
ASP   N   H2   sing N N 111 
ASP   CA  C    sing N N 112 
ASP   CA  CB   sing N N 113 
ASP   CA  HA   sing N N 114 
ASP   C   O    doub N N 115 
ASP   C   OXT  sing N N 116 
ASP   CB  CG   sing N N 117 
ASP   CB  HB2  sing N N 118 
ASP   CB  HB3  sing N N 119 
ASP   CG  OD1  doub N N 120 
ASP   CG  OD2  sing N N 121 
ASP   OD2 HD2  sing N N 122 
ASP   OXT HXT  sing N N 123 
CYS   N   CA   sing N N 124 
CYS   N   H    sing N N 125 
CYS   N   H2   sing N N 126 
CYS   CA  C    sing N N 127 
CYS   CA  CB   sing N N 128 
CYS   CA  HA   sing N N 129 
CYS   C   O    doub N N 130 
CYS   C   OXT  sing N N 131 
CYS   CB  SG   sing N N 132 
CYS   CB  HB2  sing N N 133 
CYS   CB  HB3  sing N N 134 
CYS   SG  HG   sing N N 135 
CYS   OXT HXT  sing N N 136 
GLN   N   CA   sing N N 137 
GLN   N   H    sing N N 138 
GLN   N   H2   sing N N 139 
GLN   CA  C    sing N N 140 
GLN   CA  CB   sing N N 141 
GLN   CA  HA   sing N N 142 
GLN   C   O    doub N N 143 
GLN   C   OXT  sing N N 144 
GLN   CB  CG   sing N N 145 
GLN   CB  HB2  sing N N 146 
GLN   CB  HB3  sing N N 147 
GLN   CG  CD   sing N N 148 
GLN   CG  HG2  sing N N 149 
GLN   CG  HG3  sing N N 150 
GLN   CD  OE1  doub N N 151 
GLN   CD  NE2  sing N N 152 
GLN   NE2 HE21 sing N N 153 
GLN   NE2 HE22 sing N N 154 
GLN   OXT HXT  sing N N 155 
GLU   N   CA   sing N N 156 
GLU   N   H    sing N N 157 
GLU   N   H2   sing N N 158 
GLU   CA  C    sing N N 159 
GLU   CA  CB   sing N N 160 
GLU   CA  HA   sing N N 161 
GLU   C   O    doub N N 162 
GLU   C   OXT  sing N N 163 
GLU   CB  CG   sing N N 164 
GLU   CB  HB2  sing N N 165 
GLU   CB  HB3  sing N N 166 
GLU   CG  CD   sing N N 167 
GLU   CG  HG2  sing N N 168 
GLU   CG  HG3  sing N N 169 
GLU   CD  OE1  doub N N 170 
GLU   CD  OE2  sing N N 171 
GLU   OE2 HE2  sing N N 172 
GLU   OXT HXT  sing N N 173 
GLY   N   CA   sing N N 174 
GLY   N   H    sing N N 175 
GLY   N   H2   sing N N 176 
GLY   CA  C    sing N N 177 
GLY   CA  HA2  sing N N 178 
GLY   CA  HA3  sing N N 179 
GLY   C   O    doub N N 180 
GLY   C   OXT  sing N N 181 
GLY   OXT HXT  sing N N 182 
HIS   N   CA   sing N N 183 
HIS   N   H    sing N N 184 
HIS   N   H2   sing N N 185 
HIS   CA  C    sing N N 186 
HIS   CA  CB   sing N N 187 
HIS   CA  HA   sing N N 188 
HIS   C   O    doub N N 189 
HIS   C   OXT  sing N N 190 
HIS   CB  CG   sing N N 191 
HIS   CB  HB2  sing N N 192 
HIS   CB  HB3  sing N N 193 
HIS   CG  ND1  sing Y N 194 
HIS   CG  CD2  doub Y N 195 
HIS   ND1 CE1  doub Y N 196 
HIS   ND1 HD1  sing N N 197 
HIS   CD2 NE2  sing Y N 198 
HIS   CD2 HD2  sing N N 199 
HIS   CE1 NE2  sing Y N 200 
HIS   CE1 HE1  sing N N 201 
HIS   NE2 HE2  sing N N 202 
HIS   OXT HXT  sing N N 203 
HOH   O   H1   sing N N 204 
HOH   O   H2   sing N N 205 
ILE   N   CA   sing N N 206 
ILE   N   H    sing N N 207 
ILE   N   H2   sing N N 208 
ILE   CA  C    sing N N 209 
ILE   CA  CB   sing N N 210 
ILE   CA  HA   sing N N 211 
ILE   C   O    doub N N 212 
ILE   C   OXT  sing N N 213 
ILE   CB  CG1  sing N N 214 
ILE   CB  CG2  sing N N 215 
ILE   CB  HB   sing N N 216 
ILE   CG1 CD1  sing N N 217 
ILE   CG1 HG12 sing N N 218 
ILE   CG1 HG13 sing N N 219 
ILE   CG2 HG21 sing N N 220 
ILE   CG2 HG22 sing N N 221 
ILE   CG2 HG23 sing N N 222 
ILE   CD1 HD11 sing N N 223 
ILE   CD1 HD12 sing N N 224 
ILE   CD1 HD13 sing N N 225 
ILE   OXT HXT  sing N N 226 
LEU   N   CA   sing N N 227 
LEU   N   H    sing N N 228 
LEU   N   H2   sing N N 229 
LEU   CA  C    sing N N 230 
LEU   CA  CB   sing N N 231 
LEU   CA  HA   sing N N 232 
LEU   C   O    doub N N 233 
LEU   C   OXT  sing N N 234 
LEU   CB  CG   sing N N 235 
LEU   CB  HB2  sing N N 236 
LEU   CB  HB3  sing N N 237 
LEU   CG  CD1  sing N N 238 
LEU   CG  CD2  sing N N 239 
LEU   CG  HG   sing N N 240 
LEU   CD1 HD11 sing N N 241 
LEU   CD1 HD12 sing N N 242 
LEU   CD1 HD13 sing N N 243 
LEU   CD2 HD21 sing N N 244 
LEU   CD2 HD22 sing N N 245 
LEU   CD2 HD23 sing N N 246 
LEU   OXT HXT  sing N N 247 
LYS   N   CA   sing N N 248 
LYS   N   H    sing N N 249 
LYS   N   H2   sing N N 250 
LYS   CA  C    sing N N 251 
LYS   CA  CB   sing N N 252 
LYS   CA  HA   sing N N 253 
LYS   C   O    doub N N 254 
LYS   C   OXT  sing N N 255 
LYS   CB  CG   sing N N 256 
LYS   CB  HB2  sing N N 257 
LYS   CB  HB3  sing N N 258 
LYS   CG  CD   sing N N 259 
LYS   CG  HG2  sing N N 260 
LYS   CG  HG3  sing N N 261 
LYS   CD  CE   sing N N 262 
LYS   CD  HD2  sing N N 263 
LYS   CD  HD3  sing N N 264 
LYS   CE  NZ   sing N N 265 
LYS   CE  HE2  sing N N 266 
LYS   CE  HE3  sing N N 267 
LYS   NZ  HZ1  sing N N 268 
LYS   NZ  HZ2  sing N N 269 
LYS   NZ  HZ3  sing N N 270 
LYS   OXT HXT  sing N N 271 
MET   N   CA   sing N N 272 
MET   N   H    sing N N 273 
MET   N   H2   sing N N 274 
MET   CA  C    sing N N 275 
MET   CA  CB   sing N N 276 
MET   CA  HA   sing N N 277 
MET   C   O    doub N N 278 
MET   C   OXT  sing N N 279 
MET   CB  CG   sing N N 280 
MET   CB  HB2  sing N N 281 
MET   CB  HB3  sing N N 282 
MET   CG  SD   sing N N 283 
MET   CG  HG2  sing N N 284 
MET   CG  HG3  sing N N 285 
MET   SD  CE   sing N N 286 
MET   CE  HE1  sing N N 287 
MET   CE  HE2  sing N N 288 
MET   CE  HE3  sing N N 289 
MET   OXT HXT  sing N N 290 
PHE   N   CA   sing N N 291 
PHE   N   H    sing N N 292 
PHE   N   H2   sing N N 293 
PHE   CA  C    sing N N 294 
PHE   CA  CB   sing N N 295 
PHE   CA  HA   sing N N 296 
PHE   C   O    doub N N 297 
PHE   C   OXT  sing N N 298 
PHE   CB  CG   sing N N 299 
PHE   CB  HB2  sing N N 300 
PHE   CB  HB3  sing N N 301 
PHE   CG  CD1  doub Y N 302 
PHE   CG  CD2  sing Y N 303 
PHE   CD1 CE1  sing Y N 304 
PHE   CD1 HD1  sing N N 305 
PHE   CD2 CE2  doub Y N 306 
PHE   CD2 HD2  sing N N 307 
PHE   CE1 CZ   doub Y N 308 
PHE   CE1 HE1  sing N N 309 
PHE   CE2 CZ   sing Y N 310 
PHE   CE2 HE2  sing N N 311 
PHE   CZ  HZ   sing N N 312 
PHE   OXT HXT  sing N N 313 
PRO   N   CA   sing N N 314 
PRO   N   CD   sing N N 315 
PRO   N   H    sing N N 316 
PRO   CA  C    sing N N 317 
PRO   CA  CB   sing N N 318 
PRO   CA  HA   sing N N 319 
PRO   C   O    doub N N 320 
PRO   C   OXT  sing N N 321 
PRO   CB  CG   sing N N 322 
PRO   CB  HB2  sing N N 323 
PRO   CB  HB3  sing N N 324 
PRO   CG  CD   sing N N 325 
PRO   CG  HG2  sing N N 326 
PRO   CG  HG3  sing N N 327 
PRO   CD  HD2  sing N N 328 
PRO   CD  HD3  sing N N 329 
PRO   OXT HXT  sing N N 330 
SER   N   CA   sing N N 331 
SER   N   H    sing N N 332 
SER   N   H2   sing N N 333 
SER   CA  C    sing N N 334 
SER   CA  CB   sing N N 335 
SER   CA  HA   sing N N 336 
SER   C   O    doub N N 337 
SER   C   OXT  sing N N 338 
SER   CB  OG   sing N N 339 
SER   CB  HB2  sing N N 340 
SER   CB  HB3  sing N N 341 
SER   OG  HG   sing N N 342 
SER   OXT HXT  sing N N 343 
THR   N   CA   sing N N 344 
THR   N   H    sing N N 345 
THR   N   H2   sing N N 346 
THR   CA  C    sing N N 347 
THR   CA  CB   sing N N 348 
THR   CA  HA   sing N N 349 
THR   C   O    doub N N 350 
THR   C   OXT  sing N N 351 
THR   CB  OG1  sing N N 352 
THR   CB  CG2  sing N N 353 
THR   CB  HB   sing N N 354 
THR   OG1 HG1  sing N N 355 
THR   CG2 HG21 sing N N 356 
THR   CG2 HG22 sing N N 357 
THR   CG2 HG23 sing N N 358 
THR   OXT HXT  sing N N 359 
TRP   N   CA   sing N N 360 
TRP   N   H    sing N N 361 
TRP   N   H2   sing N N 362 
TRP   CA  C    sing N N 363 
TRP   CA  CB   sing N N 364 
TRP   CA  HA   sing N N 365 
TRP   C   O    doub N N 366 
TRP   C   OXT  sing N N 367 
TRP   CB  CG   sing N N 368 
TRP   CB  HB2  sing N N 369 
TRP   CB  HB3  sing N N 370 
TRP   CG  CD1  doub Y N 371 
TRP   CG  CD2  sing Y N 372 
TRP   CD1 NE1  sing Y N 373 
TRP   CD1 HD1  sing N N 374 
TRP   CD2 CE2  doub Y N 375 
TRP   CD2 CE3  sing Y N 376 
TRP   NE1 CE2  sing Y N 377 
TRP   NE1 HE1  sing N N 378 
TRP   CE2 CZ2  sing Y N 379 
TRP   CE3 CZ3  doub Y N 380 
TRP   CE3 HE3  sing N N 381 
TRP   CZ2 CH2  doub Y N 382 
TRP   CZ2 HZ2  sing N N 383 
TRP   CZ3 CH2  sing Y N 384 
TRP   CZ3 HZ3  sing N N 385 
TRP   CH2 HH2  sing N N 386 
TRP   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           22077133 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4QKN 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9KNI 
_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]   0.007072 
_atom_sites.fract_transf_matrix[1][2]   0.004083 
_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]   0.008166 
_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]   0.011926 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . GLY   A 1 1   ? 43.123  -12.329 31.686 1.00 120.44 ?  28  GLY   A N    1 
ATOM   2    C  CA   . GLY   A 1 1   ? 43.196  -12.396 30.238 1.00 117.24 ?  28  GLY   A CA   1 
ATOM   3    C  C    . GLY   A 1 1   ? 44.087  -11.331 29.628 1.00 123.60 ?  28  GLY   A C    1 
ATOM   4    O  O    . GLY   A 1 1   ? 44.891  -10.708 30.321 1.00 123.44 ?  28  GLY   A O    1 
ATOM   5    N  N    . SER   A 1 2   ? 43.942  -11.126 28.321 1.00 109.46 ?  29  SER   A N    1 
ATOM   6    C  CA   . SER   A 1 2   ? 44.707  -10.123 27.591 1.00 101.87 ?  29  SER   A CA   1 
ATOM   7    C  C    . SER   A 1 2   ? 43.777  -9.471  26.572 1.00 101.48 ?  29  SER   A C    1 
ATOM   8    O  O    . SER   A 1 2   ? 42.556  -9.651  26.612 1.00 104.47 ?  29  SER   A O    1 
ATOM   9    C  CB   . SER   A 1 2   ? 45.947  -10.752 26.942 1.00 111.57 ?  29  SER   A CB   1 
ATOM   10   O  OG   . SER   A 1 2   ? 45.614  -11.947 26.257 1.00 119.63 ?  29  SER   A OG   1 
ATOM   11   N  N    . HIS   A 1 3   ? 44.354  -8.705  25.647 1.00 94.58  ?  30  HIS   A N    1 
ATOM   12   C  CA   . HIS   A 1 3   ? 43.583  -8.002  24.633 1.00 92.52  ?  30  HIS   A CA   1 
ATOM   13   C  C    . HIS   A 1 3   ? 44.209  -8.221  23.261 1.00 86.15  ?  30  HIS   A C    1 
ATOM   14   O  O    . HIS   A 1 3   ? 45.321  -8.741  23.132 1.00 85.07  ?  30  HIS   A O    1 
ATOM   15   C  CB   . HIS   A 1 3   ? 43.477  -6.503  24.948 1.00 82.02  ?  30  HIS   A CB   1 
ATOM   16   C  CG   . HIS   A 1 3   ? 44.792  -5.789  24.960 1.00 77.99  ?  30  HIS   A CG   1 
ATOM   17   N  ND1  . HIS   A 1 3   ? 45.692  -5.906  25.997 1.00 73.63  ?  30  HIS   A ND1  1 
ATOM   18   C  CD2  . HIS   A 1 3   ? 45.355  -4.941  24.067 1.00 75.53  ?  30  HIS   A CD2  1 
ATOM   19   C  CE1  . HIS   A 1 3   ? 46.755  -5.165  25.739 1.00 89.20  ?  30  HIS   A CE1  1 
ATOM   20   N  NE2  . HIS   A 1 3   ? 46.576  -4.569  24.574 1.00 86.20  ?  30  HIS   A NE2  1 
ATOM   21   N  N    . MET   A 1 4   ? 43.474  -7.813  22.226 1.00 84.29  ?  31  MET   A N    1 
ATOM   22   C  CA   . MET   A 1 4   ? 43.858  -8.049  20.842 1.00 76.21  ?  31  MET   A CA   1 
ATOM   23   C  C    . MET   A 1 4   ? 43.782  -6.759  20.041 1.00 71.55  ?  31  MET   A C    1 
ATOM   24   O  O    . MET   A 1 4   ? 42.821  -5.994  20.162 1.00 83.08  ?  31  MET   A O    1 
ATOM   25   C  CB   . MET   A 1 4   ? 42.962  -9.107  20.194 1.00 79.33  ?  31  MET   A CB   1 
ATOM   26   C  CG   . MET   A 1 4   ? 43.039  -10.466 20.856 1.00 78.35  ?  31  MET   A CG   1 
ATOM   27   S  SD   . MET   A 1 4   ? 42.807  -11.803 19.675 1.00 99.85  ?  31  MET   A SD   1 
ATOM   28   C  CE   . MET   A 1 4   ? 41.320  -12.555 20.326 1.00 95.73  ?  31  MET   A CE   1 
ATOM   29   N  N    . THR   A 1 5   ? 44.797  -6.533  19.220 1.00 70.34  ?  32  THR   A N    1 
ATOM   30   C  CA   . THR   A 1 5   ? 44.898  -5.394  18.320 1.00 73.05  ?  32  THR   A CA   1 
ATOM   31   C  C    . THR   A 1 5   ? 45.229  -5.906  16.930 1.00 81.61  ?  32  THR   A C    1 
ATOM   32   O  O    . THR   A 1 5   ? 45.608  -7.069  16.761 1.00 81.08  ?  32  THR   A O    1 
ATOM   33   C  CB   . THR   A 1 5   ? 45.982  -4.413  18.803 1.00 71.65  ?  32  THR   A CB   1 
ATOM   34   O  OG1  . THR   A 1 5   ? 47.270  -5.034  18.708 1.00 86.17  ?  32  THR   A OG1  1 
ATOM   35   C  CG2  . THR   A 1 5   ? 45.724  -3.991  20.244 1.00 75.00  ?  32  THR   A CG2  1 
ATOM   36   N  N    . PRO   A 1 6   ? 45.091  -5.055  15.890 1.00 81.95  ?  33  PRO   A N    1 
ATOM   37   C  CA   . PRO   A 1 6   ? 45.469  -5.480  14.531 1.00 75.03  ?  33  PRO   A CA   1 
ATOM   38   C  C    . PRO   A 1 6   ? 46.879  -6.049  14.407 1.00 84.36  ?  33  PRO   A C    1 
ATOM   39   O  O    . PRO   A 1 6   ? 47.225  -6.626  13.371 1.00 83.49  ?  33  PRO   A O    1 
ATOM   40   C  CB   . PRO   A 1 6   ? 45.325  -4.190  13.716 1.00 79.73  ?  33  PRO   A CB   1 
ATOM   41   C  CG   . PRO   A 1 6   ? 44.248  -3.440  14.409 1.00 77.10  ?  33  PRO   A CG   1 
ATOM   42   C  CD   . PRO   A 1 6   ? 44.339  -3.786  15.875 1.00 65.81  ?  33  PRO   A CD   1 
ATOM   43   N  N    . LYS   A 1 7   ? 47.702  -5.893  15.447 1.00 80.90  ?  34  LYS   A N    1 
ATOM   44   C  CA   . LYS   A 1 7   ? 49.031  -6.492  15.441 1.00 83.24  ?  34  LYS   A CA   1 
ATOM   45   C  C    . LYS   A 1 7   ? 48.988  -8.007  15.606 1.00 80.66  ?  34  LYS   A C    1 
ATOM   46   O  O    . LYS   A 1 7   ? 49.975  -8.678  15.288 1.00 95.65  ?  34  LYS   A O    1 
ATOM   47   C  CB   . LYS   A 1 7   ? 49.890  -5.875  16.546 1.00 67.68  ?  34  LYS   A CB   1 
ATOM   48   N  N    . ASP   A 1 8   ? 47.878  -8.557  16.090 1.00 85.88  ?  35  ASP   A N    1 
ATOM   49   C  CA   . ASP   A 1 8   ? 47.756  -9.986  16.343 1.00 82.71  ?  35  ASP   A CA   1 
ATOM   50   C  C    . ASP   A 1 8   ? 47.054  -10.677 15.180 1.00 88.06  ?  35  ASP   A C    1 
ATOM   51   O  O    . ASP   A 1 8   ? 46.136  -10.118 14.571 1.00 81.67  ?  35  ASP   A O    1 
ATOM   52   C  CB   . ASP   A 1 8   ? 46.990  -10.249 17.642 1.00 90.93  ?  35  ASP   A CB   1 
ATOM   53   C  CG   . ASP   A 1 8   ? 47.673  -9.645  18.854 1.00 92.00  ?  35  ASP   A CG   1 
ATOM   54   O  OD1  . ASP   A 1 8   ? 47.403  -8.466  19.169 1.00 91.40  ?  35  ASP   A OD1  1 
ATOM   55   O  OD2  . ASP   A 1 8   ? 48.477  -10.352 19.497 1.00 120.92 ?  35  ASP   A OD2  1 
ATOM   56   N  N    . ASP   A 1 9   ? 47.489  -11.904 14.884 1.00 83.61  ?  36  ASP   A N    1 
ATOM   57   C  CA   . ASP   A 1 9   ? 46.904  -12.655 13.778 1.00 88.16  ?  36  ASP   A CA   1 
ATOM   58   C  C    . ASP   A 1 9   ? 45.453  -13.025 14.064 1.00 89.07  ?  36  ASP   A C    1 
ATOM   59   O  O    . ASP   A 1 9   ? 44.596  -12.930 13.177 1.00 94.02  ?  36  ASP   A O    1 
ATOM   60   C  CB   . ASP   A 1 9   ? 47.731  -13.911 13.505 1.00 94.63  ?  36  ASP   A CB   1 
ATOM   61   C  CG   . ASP   A 1 9   ? 49.103  -13.597 12.939 1.00 101.23 ?  36  ASP   A CG   1 
ATOM   62   O  OD1  . ASP   A 1 9   ? 49.180  -12.867 11.928 1.00 111.54 ?  36  ASP   A OD1  1 
ATOM   63   O  OD2  . ASP   A 1 9   ? 50.105  -14.082 13.505 1.00 107.01 ?  36  ASP   A OD2  1 
ATOM   64   N  N    . GLU   A 1 10  ? 45.159  -13.448 15.295 1.00 88.57  ?  37  GLU   A N    1 
ATOM   65   C  CA   . GLU   A 1 10  ? 43.811  -13.868 15.661 1.00 81.08  ?  37  GLU   A CA   1 
ATOM   66   C  C    . GLU   A 1 10  ? 42.834  -12.705 15.768 1.00 92.67  ?  37  GLU   A C    1 
ATOM   67   O  O    . GLU   A 1 10  ? 41.626  -12.945 15.878 1.00 84.91  ?  37  GLU   A O    1 
ATOM   68   C  CB   . GLU   A 1 10  ? 43.841  -14.623 16.990 1.00 88.44  ?  37  GLU   A CB   1 
ATOM   69   C  CG   . GLU   A 1 10  ? 45.019  -15.567 17.153 1.00 104.77 ?  37  GLU   A CG   1 
ATOM   70   C  CD   . GLU   A 1 10  ? 45.475  -15.679 18.596 1.00 114.23 ?  37  GLU   A CD   1 
ATOM   71   O  OE1  . GLU   A 1 10  ? 46.443  -14.983 18.970 1.00 112.91 ?  37  GLU   A OE1  1 
ATOM   72   O  OE2  . GLU   A 1 10  ? 44.863  -16.459 19.356 1.00 105.41 ?  37  GLU   A OE2  1 
ATOM   73   N  N    . PHE   A 1 11  ? 43.325  -11.463 15.741 1.00 91.35  ?  38  PHE   A N    1 
ATOM   74   C  CA   . PHE   A 1 11  ? 42.459  -10.307 15.952 1.00 83.71  ?  38  PHE   A CA   1 
ATOM   75   C  C    . PHE   A 1 11  ? 41.375  -10.217 14.886 1.00 77.03  ?  38  PHE   A C    1 
ATOM   76   O  O    . PHE   A 1 11  ? 40.234  -9.839  15.178 1.00 78.63  ?  38  PHE   A O    1 
ATOM   77   C  CB   . PHE   A 1 11  ? 43.303  -9.032  15.969 1.00 81.36  ?  38  PHE   A CB   1 
ATOM   78   C  CG   . PHE   A 1 11  ? 42.509  -7.767  15.806 1.00 71.76  ?  38  PHE   A CG   1 
ATOM   79   C  CD1  . PHE   A 1 11  ? 41.956  -7.136  16.907 1.00 78.58  ?  38  PHE   A CD1  1 
ATOM   80   C  CD2  . PHE   A 1 11  ? 42.333  -7.195  14.554 1.00 84.33  ?  38  PHE   A CD2  1 
ATOM   81   C  CE1  . PHE   A 1 11  ? 41.231  -5.970  16.764 1.00 72.33  ?  38  PHE   A CE1  1 
ATOM   82   C  CE2  . PHE   A 1 11  ? 41.607  -6.030  14.404 1.00 81.37  ?  38  PHE   A CE2  1 
ATOM   83   C  CZ   . PHE   A 1 11  ? 41.057  -5.416  15.510 1.00 74.62  ?  38  PHE   A CZ   1 
ATOM   84   N  N    . TYR   A 1 12  ? 41.711  -10.561 13.644 1.00 87.24  ?  39  TYR   A N    1 
ATOM   85   C  CA   . TYR   A 1 12  ? 40.778  -10.376 12.540 1.00 87.33  ?  39  TYR   A CA   1 
ATOM   86   C  C    . TYR   A 1 12  ? 39.680  -11.431 12.549 1.00 84.61  ?  39  TYR   A C    1 
ATOM   87   O  O    . TYR   A 1 12  ? 38.524  -11.129 12.231 1.00 85.62  ?  39  TYR   A O    1 
ATOM   88   C  CB   . TYR   A 1 12  ? 41.543  -10.391 11.218 1.00 93.68  ?  39  TYR   A CB   1 
ATOM   89   C  CG   . TYR   A 1 12  ? 42.684  -9.398  11.195 1.00 94.35  ?  39  TYR   A CG   1 
ATOM   90   C  CD1  . TYR   A 1 12  ? 43.948  -9.751  11.650 1.00 89.77  ?  39  TYR   A CD1  1 
ATOM   91   C  CD2  . TYR   A 1 12  ? 42.491  -8.102  10.743 1.00 106.29 ?  39  TYR   A CD2  1 
ATOM   92   C  CE1  . TYR   A 1 12  ? 44.991  -8.842  11.642 1.00 102.40 ?  39  TYR   A CE1  1 
ATOM   93   C  CE2  . TYR   A 1 12  ? 43.527  -7.189  10.729 1.00 102.78 ?  39  TYR   A CE2  1 
ATOM   94   C  CZ   . TYR   A 1 12  ? 44.773  -7.561  11.180 1.00 99.29  ?  39  TYR   A CZ   1 
ATOM   95   O  OH   . TYR   A 1 12  ? 45.802  -6.648  11.166 1.00 100.64 ?  39  TYR   A OH   1 
ATOM   96   N  N    . GLN   A 1 13  ? 40.018  -12.668 12.916 1.00 86.83  ?  40  GLN   A N    1 
ATOM   97   C  CA   . GLN   A 1 13  ? 39.010  -13.719 12.991 1.00 84.27  ?  40  GLN   A CA   1 
ATOM   98   C  C    . GLN   A 1 13  ? 38.158  -13.606 14.250 1.00 92.25  ?  40  GLN   A C    1 
ATOM   99   O  O    . GLN   A 1 13  ? 37.017  -14.081 14.262 1.00 96.25  ?  40  GLN   A O    1 
ATOM   100  C  CB   . GLN   A 1 13  ? 39.679  -15.092 12.916 1.00 87.34  ?  40  GLN   A CB   1 
ATOM   101  C  CG   . GLN   A 1 13  ? 40.202  -15.608 14.241 1.00 92.83  ?  40  GLN   A CG   1 
ATOM   102  C  CD   . GLN   A 1 13  ? 40.993  -16.888 14.093 1.00 90.03  ?  40  GLN   A CD   1 
ATOM   103  O  OE1  . GLN   A 1 13  ? 41.142  -17.417 12.991 1.00 88.01  ?  40  GLN   A OE1  1 
ATOM   104  N  NE2  . GLN   A 1 13  ? 41.509  -17.395 15.206 1.00 97.97  ?  40  GLN   A NE2  1 
ATOM   105  N  N    . GLN   A 1 14  ? 38.684  -12.989 15.311 1.00 88.29  ?  41  GLN   A N    1 
ATOM   106  C  CA   . GLN   A 1 14  ? 37.858  -12.720 16.483 1.00 90.01  ?  41  GLN   A CA   1 
ATOM   107  C  C    . GLN   A 1 14  ? 36.808  -11.661 16.175 1.00 91.94  ?  41  GLN   A C    1 
ATOM   108  O  O    . GLN   A 1 14  ? 35.665  -11.757 16.637 1.00 93.60  ?  41  GLN   A O    1 
ATOM   109  C  CB   . GLN   A 1 14  ? 38.731  -12.280 17.659 1.00 94.63  ?  41  GLN   A CB   1 
ATOM   110  C  CG   . GLN   A 1 14  ? 37.997  -12.243 18.990 1.00 99.09  ?  41  GLN   A CG   1 
ATOM   111  C  CD   . GLN   A 1 14  ? 38.059  -13.564 19.734 1.00 113.68 ?  41  GLN   A CD   1 
ATOM   112  O  OE1  . GLN   A 1 14  ? 38.155  -14.631 19.127 1.00 107.33 ?  41  GLN   A OE1  1 
ATOM   113  N  NE2  . GLN   A 1 14  ? 38.006  -13.497 21.060 1.00 110.55 ?  41  GLN   A NE2  1 
ATOM   114  N  N    . TRP   A 1 15  ? 37.183  -10.642 15.398 1.00 85.46  ?  42  TRP   A N    1 
ATOM   115  C  CA   . TRP   A 1 15  ? 36.212  -9.653  14.945 1.00 82.95  ?  42  TRP   A CA   1 
ATOM   116  C  C    . TRP   A 1 15  ? 35.124  -10.306 14.101 1.00 83.70  ?  42  TRP   A C    1 
ATOM   117  O  O    . TRP   A 1 15  ? 33.942  -9.967  14.226 1.00 87.59  ?  42  TRP   A O    1 
ATOM   118  C  CB   . TRP   A 1 15  ? 36.930  -8.552  14.161 1.00 77.13  ?  42  TRP   A CB   1 
ATOM   119  C  CG   . TRP   A 1 15  ? 36.133  -7.293  13.943 1.00 82.11  ?  42  TRP   A CG   1 
ATOM   120  C  CD1  . TRP   A 1 15  ? 34.774  -7.169  13.924 1.00 77.79  ?  42  TRP   A CD1  1 
ATOM   121  C  CD2  . TRP   A 1 15  ? 36.657  -5.978  13.718 1.00 83.52  ?  42  TRP   A CD2  1 
ATOM   122  N  NE1  . TRP   A 1 15  ? 34.420  -5.862  13.696 1.00 85.97  ?  42  TRP   A NE1  1 
ATOM   123  C  CE2  . TRP   A 1 15  ? 35.557  -5.110  13.568 1.00 83.00  ?  42  TRP   A CE2  1 
ATOM   124  C  CE3  . TRP   A 1 15  ? 37.949  -5.451  13.628 1.00 90.37  ?  42  TRP   A CE3  1 
ATOM   125  C  CZ2  . TRP   A 1 15  ? 35.710  -3.745  13.333 1.00 77.19  ?  42  TRP   A CZ2  1 
ATOM   126  C  CZ3  . TRP   A 1 15  ? 38.098  -4.095  13.397 1.00 91.46  ?  42  TRP   A CZ3  1 
ATOM   127  C  CH2  . TRP   A 1 15  ? 36.985  -3.259  13.250 1.00 79.71  ?  42  TRP   A CH2  1 
ATOM   128  N  N    . GLN   A 1 16  ? 35.503  -11.260 13.251 1.00 80.83  ?  43  GLN   A N    1 
ATOM   129  C  CA   . GLN   A 1 16  ? 34.525  -11.909 12.385 1.00 86.19  ?  43  GLN   A CA   1 
ATOM   130  C  C    . GLN   A 1 16  ? 33.548  -12.760 13.188 1.00 91.36  ?  43  GLN   A C    1 
ATOM   131  O  O    . GLN   A 1 16  ? 32.332  -12.695 12.975 1.00 93.29  ?  43  GLN   A O    1 
ATOM   132  C  CB   . GLN   A 1 16  ? 35.242  -12.759 11.334 1.00 92.98  ?  43  GLN   A CB   1 
ATOM   133  N  N    . LEU   A 1 17  ? 34.060  -13.556 14.129 1.00 97.16  ?  44  LEU   A N    1 
ATOM   134  C  CA   . LEU   A 1 17  ? 33.229  -14.562 14.783 1.00 88.36  ?  44  LEU   A CA   1 
ATOM   135  C  C    . LEU   A 1 17  ? 32.374  -13.967 15.897 1.00 86.52  ?  44  LEU   A C    1 
ATOM   136  O  O    . LEU   A 1 17  ? 31.167  -14.223 15.962 1.00 99.75  ?  44  LEU   A O    1 
ATOM   137  C  CB   . LEU   A 1 17  ? 34.104  -15.690 15.334 1.00 87.71  ?  44  LEU   A CB   1 
ATOM   138  C  CG   . LEU   A 1 17  ? 34.218  -16.954 14.478 1.00 102.96 ?  44  LEU   A CG   1 
ATOM   139  C  CD1  . LEU   A 1 17  ? 34.806  -16.635 13.111 1.00 103.77 ?  44  LEU   A CD1  1 
ATOM   140  C  CD2  . LEU   A 1 17  ? 35.043  -18.016 15.191 1.00 108.83 ?  44  LEU   A CD2  1 
ATOM   141  N  N    . LYS   A 1 18  ? 32.978  -13.177 16.785 1.00 92.96  ?  45  LYS   A N    1 
ATOM   142  C  CA   . LYS   A 1 18  ? 32.314  -12.771 18.015 1.00 89.08  ?  45  LYS   A CA   1 
ATOM   143  C  C    . LYS   A 1 18  ? 32.036  -11.276 18.112 1.00 82.84  ?  45  LYS   A C    1 
ATOM   144  O  O    . LYS   A 1 18  ? 31.519  -10.827 19.142 1.00 81.65  ?  45  LYS   A O    1 
ATOM   145  C  CB   . LYS   A 1 18  ? 33.139  -13.227 19.226 1.00 85.82  ?  45  LYS   A CB   1 
ATOM   146  C  CG   . LYS   A 1 18  ? 33.585  -14.680 19.122 1.00 88.67  ?  45  LYS   A CG   1 
ATOM   147  C  CD   . LYS   A 1 18  ? 33.264  -15.478 20.375 1.00 89.83  ?  45  LYS   A CD   1 
ATOM   148  C  CE   . LYS   A 1 18  ? 33.495  -14.666 21.636 1.00 97.21  ?  45  LYS   A CE   1 
ATOM   149  N  NZ   . LYS   A 1 18  ? 33.770  -15.547 22.804 1.00 103.19 ?  45  LYS   A NZ   1 
ATOM   150  N  N    . TYR   A 1 19  ? 32.364  -10.493 17.086 1.00 86.12  ?  46  TYR   A N    1 
ATOM   151  C  CA   . TYR   A 1 19  ? 31.919  -9.105  17.025 1.00 73.94  ?  46  TYR   A CA   1 
ATOM   152  C  C    . TYR   A 1 19  ? 31.431  -8.737  15.627 1.00 81.69  ?  46  TYR   A C    1 
ATOM   153  O  O    . TYR   A 1 19  ? 31.879  -7.723  15.077 1.00 89.79  ?  46  TYR   A O    1 
ATOM   154  C  CB   . TYR   A 1 19  ? 33.041  -8.142  17.423 1.00 74.37  ?  46  TYR   A CB   1 
ATOM   155  C  CG   . TYR   A 1 19  ? 33.541  -8.262  18.844 1.00 69.90  ?  46  TYR   A CG   1 
ATOM   156  C  CD1  . TYR   A 1 19  ? 34.487  -9.218  19.190 1.00 75.40  ?  46  TYR   A CD1  1 
ATOM   157  C  CD2  . TYR   A 1 19  ? 33.093  -7.397  19.833 1.00 69.37  ?  46  TYR   A CD2  1 
ATOM   158  C  CE1  . TYR   A 1 19  ? 34.959  -9.320  20.486 1.00 71.19  ?  46  TYR   A CE1  1 
ATOM   159  C  CE2  . TYR   A 1 19  ? 33.560  -7.491  21.131 1.00 69.30  ?  46  TYR   A CE2  1 
ATOM   160  C  CZ   . TYR   A 1 19  ? 34.491  -8.455  21.452 1.00 78.58  ?  46  TYR   A CZ   1 
ATOM   161  O  OH   . TYR   A 1 19  ? 34.958  -8.555  22.743 1.00 89.33  ?  46  TYR   A OH   1 
ATOM   162  N  N    . PRO   A 1 20  ? 30.520  -9.502  15.014 1.00 81.08  ?  47  PRO   A N    1 
ATOM   163  C  CA   . PRO   A 1 20  ? 30.096  -9.151  13.650 1.00 85.88  ?  47  PRO   A CA   1 
ATOM   164  C  C    . PRO   A 1 20  ? 29.213  -7.919  13.592 1.00 89.59  ?  47  PRO   A C    1 
ATOM   165  O  O    . PRO   A 1 20  ? 29.058  -7.341  12.508 1.00 92.19  ?  47  PRO   A O    1 
ATOM   166  C  CB   . PRO   A 1 20  ? 29.344  -10.402 13.180 1.00 92.86  ?  47  PRO   A CB   1 
ATOM   167  C  CG   . PRO   A 1 20  ? 28.812  -11.004 14.425 1.00 97.25  ?  47  PRO   A CG   1 
ATOM   168  C  CD   . PRO   A 1 20  ? 29.757  -10.648 15.546 1.00 86.92  ?  47  PRO   A CD   1 
ATOM   169  N  N    . LYS   A 1 21  ? 28.637  -7.494  14.714 1.00 73.45  ?  48  LYS   A N    1 
ATOM   170  C  CA   . LYS   A 1 21  ? 27.787  -6.313  14.759 1.00 73.35  ?  48  LYS   A CA   1 
ATOM   171  C  C    . LYS   A 1 21  ? 28.571  -5.025  14.982 1.00 71.17  ?  48  LYS   A C    1 
ATOM   172  O  O    . LYS   A 1 21  ? 27.961  -3.962  15.138 1.00 76.01  ?  48  LYS   A O    1 
ATOM   173  C  CB   . LYS   A 1 21  ? 26.718  -6.474  15.844 1.00 64.63  ?  48  LYS   A CB   1 
ATOM   174  C  CG   . LYS   A 1 21  ? 25.558  -7.366  15.426 1.00 72.63  ?  48  LYS   A CG   1 
ATOM   175  C  CD   . LYS   A 1 21  ? 24.841  -7.970  16.621 1.00 84.03  ?  48  LYS   A CD   1 
ATOM   176  C  CE   . LYS   A 1 21  ? 23.883  -9.071  16.185 1.00 71.86  ?  48  LYS   A CE   1 
ATOM   177  N  NZ   . LYS   A 1 21  ? 23.115  -9.630  17.332 1.00 67.73  ?  48  LYS   A NZ   1 
ATOM   178  N  N    . LEU   A 1 22  ? 29.899  -5.094  15.003 1.00 67.37  ?  49  LEU   A N    1 
ATOM   179  C  CA   . LEU   A 1 22  ? 30.748  -3.913  15.083 1.00 59.96  ?  49  LEU   A CA   1 
ATOM   180  C  C    . LEU   A 1 22  ? 31.330  -3.639  13.702 1.00 68.61  ?  49  LEU   A C    1 
ATOM   181  O  O    . LEU   A 1 22  ? 32.015  -4.496  13.132 1.00 64.36  ?  49  LEU   A O    1 
ATOM   182  C  CB   . LEU   A 1 22  ? 31.866  -4.102  16.108 1.00 66.97  ?  49  LEU   A CB   1 
ATOM   183  C  CG   . LEU   A 1 22  ? 32.883  -2.962  16.193 1.00 64.42  ?  49  LEU   A CG   1 
ATOM   184  C  CD1  . LEU   A 1 22  ? 32.219  -1.681  16.674 1.00 65.37  ?  49  LEU   A CD1  1 
ATOM   185  C  CD2  . LEU   A 1 22  ? 34.047  -3.339  17.094 1.00 66.21  ?  49  LEU   A CD2  1 
ATOM   186  N  N    . ILE   A 1 23  ? 31.053  -2.453  13.168 1.00 69.05  ?  50  ILE   A N    1 
ATOM   187  C  CA   . ILE   A 1 23  ? 31.493  -2.054  11.836 1.00 70.43  ?  50  ILE   A CA   1 
ATOM   188  C  C    . ILE   A 1 23  ? 32.480  -0.903  11.976 1.00 75.78  ?  50  ILE   A C    1 
ATOM   189  O  O    . ILE   A 1 23  ? 32.270  0.010   12.783 1.00 73.08  ?  50  ILE   A O    1 
ATOM   190  C  CB   . ILE   A 1 23  ? 30.298  -1.647  10.947 1.00 74.62  ?  50  ILE   A CB   1 
ATOM   191  C  CG1  . ILE   A 1 23  ? 29.354  -2.829  10.693 1.00 70.47  ?  50  ILE   A CG1  1 
ATOM   192  C  CG2  . ILE   A 1 23  ? 30.779  -1.084  9.619  1.00 71.59  ?  50  ILE   A CG2  1 
ATOM   193  C  CD1  . ILE   A 1 23  ? 30.028  -4.184  10.611 1.00 85.44  ?  50  ILE   A CD1  1 
ATOM   194  N  N    . LEU   A 1 24  ? 33.559  -0.950  11.197 1.00 72.46  ?  51  LEU   A N    1 
ATOM   195  C  CA   . LEU   A 1 24  ? 34.534  0.131   11.129 1.00 71.29  ?  51  LEU   A CA   1 
ATOM   196  C  C    . LEU   A 1 24  ? 34.578  0.681   9.711  1.00 74.60  ?  51  LEU   A C    1 
ATOM   197  O  O    . LEU   A 1 24  ? 34.701  -0.084  8.748  1.00 79.83  ?  51  LEU   A O    1 
ATOM   198  C  CB   . LEU   A 1 24  ? 35.928  -0.341  11.552 1.00 66.94  ?  51  LEU   A CB   1 
ATOM   199  C  CG   . LEU   A 1 24  ? 37.016  0.737   11.614 1.00 78.48  ?  51  LEU   A CG   1 
ATOM   200  C  CD1  . LEU   A 1 24  ? 36.534  1.966   12.369 1.00 72.75  ?  51  LEU   A CD1  1 
ATOM   201  C  CD2  . LEU   A 1 24  ? 38.296  0.195   12.232 1.00 87.43  ?  51  LEU   A CD2  1 
ATOM   202  N  N    . ARG   A 1 25  ? 34.474  2.002   9.588  1.00 70.34  ?  52  ARG   A N    1 
ATOM   203  C  CA   . ARG   A 1 25  ? 34.595  2.700   8.312  1.00 74.16  ?  52  ARG   A CA   1 
ATOM   204  C  C    . ARG   A 1 25  ? 35.728  3.707   8.447  1.00 80.54  ?  52  ARG   A C    1 
ATOM   205  O  O    . ARG   A 1 25  ? 35.594  4.706   9.162  1.00 87.42  ?  52  ARG   A O    1 
ATOM   206  C  CB   . ARG   A 1 25  ? 33.286  3.391   7.932  1.00 82.34  ?  52  ARG   A CB   1 
ATOM   207  C  CG   . ARG   A 1 25  ? 32.153  2.436   7.611  1.00 85.30  ?  52  ARG   A CG   1 
ATOM   208  C  CD   . ARG   A 1 25  ? 31.854  2.402   6.121  1.00 88.93  ?  52  ARG   A CD   1 
ATOM   209  N  NE   . ARG   A 1 25  ? 30.688  1.579   5.819  1.00 102.57 ?  52  ARG   A NE   1 
ATOM   210  C  CZ   . ARG   A 1 25  ? 30.660  0.255   5.896  1.00 94.30  ?  52  ARG   A CZ   1 
ATOM   211  N  NH1  . ARG   A 1 25  ? 31.732  -0.441  6.239  1.00 82.66  ?  52  ARG   A NH1  1 
ATOM   212  N  NH2  . ARG   A 1 25  ? 29.529  -0.387  5.618  1.00 97.81  ?  52  ARG   A NH2  1 
ATOM   213  N  N    . GLU   A 1 26  ? 36.841  3.445   7.769  1.00 81.73  ?  53  GLU   A N    1 
ATOM   214  C  CA   . GLU   A 1 26  ? 38.013  4.291   7.918  1.00 93.13  ?  53  GLU   A CA   1 
ATOM   215  C  C    . GLU   A 1 26  ? 37.785  5.648   7.256  1.00 85.54  ?  53  GLU   A C    1 
ATOM   216  O  O    . GLU   A 1 26  ? 36.877  5.830   6.439  1.00 85.77  ?  53  GLU   A O    1 
ATOM   217  C  CB   . GLU   A 1 26  ? 39.245  3.600   7.336  1.00 87.25  ?  53  GLU   A CB   1 
ATOM   218  C  CG   . GLU   A 1 26  ? 39.490  2.222   7.937  1.00 94.84  ?  53  GLU   A CG   1 
ATOM   219  C  CD   . GLU   A 1 26  ? 40.960  1.860   8.016  1.00 111.90 ?  53  GLU   A CD   1 
ATOM   220  O  OE1  . GLU   A 1 26  ? 41.470  1.703   9.146  1.00 115.13 ?  53  GLU   A OE1  1 
ATOM   221  O  OE2  . GLU   A 1 26  ? 41.603  1.724   6.955  1.00 116.08 ?  53  GLU   A OE2  1 
ATOM   222  N  N    . ALA   A 1 27  ? 38.631  6.613   7.629  1.00 83.17  ?  54  ALA   A N    1 
ATOM   223  C  CA   . ALA   A 1 27  ? 38.454  7.992   7.185  1.00 90.26  ?  54  ALA   A CA   1 
ATOM   224  C  C    . ALA   A 1 27  ? 38.496  8.132   5.669  1.00 96.43  ?  54  ALA   A C    1 
ATOM   225  O  O    . ALA   A 1 27  ? 37.944  9.099   5.133  1.00 99.42  ?  54  ALA   A O    1 
ATOM   226  C  CB   . ALA   A 1 27  ? 39.520  8.888   7.818  1.00 82.16  ?  54  ALA   A CB   1 
ATOM   227  N  N    . SER   A 1 28  ? 39.129  7.190   4.968  1.00 96.44  ?  55  SER   A N    1 
ATOM   228  C  CA   . SER   A 1 28  ? 39.217  7.254   3.514  1.00 99.71  ?  55  SER   A CA   1 
ATOM   229  C  C    . SER   A 1 28  ? 37.876  7.031   2.827  1.00 104.59 ?  55  SER   A C    1 
ATOM   230  O  O    . SER   A 1 28  ? 37.785  7.230   1.611  1.00 107.99 ?  55  SER   A O    1 
ATOM   231  C  CB   . SER   A 1 28  ? 40.233  6.228   3.010  1.00 99.83  ?  55  SER   A CB   1 
ATOM   232  O  OG   . SER   A 1 28  ? 41.321  6.108   3.910  1.00 106.40 ?  55  SER   A OG   1 
ATOM   233  N  N    . SER   A 1 29  ? 36.841  6.626   3.564  1.00 95.53  ?  56  SER   A N    1 
ATOM   234  C  CA   . SER   A 1 29  ? 35.516  6.400   3.003  1.00 88.62  ?  56  SER   A CA   1 
ATOM   235  C  C    . SER   A 1 29  ? 34.564  7.561   3.270  1.00 98.29  ?  56  SER   A C    1 
ATOM   236  O  O    . SER   A 1 29  ? 33.345  7.395   3.152  1.00 105.95 ?  56  SER   A O    1 
ATOM   237  C  CB   . SER   A 1 29  ? 34.926  5.099   3.548  1.00 88.51  ?  56  SER   A CB   1 
ATOM   238  O  OG   . SER   A 1 29  ? 34.676  5.195   4.939  1.00 97.94  ?  56  SER   A OG   1 
ATOM   239  N  N    . VAL   A 1 30  ? 35.093  8.729   3.628  1.00 102.29 ?  57  VAL   A N    1 
ATOM   240  C  CA   . VAL   A 1 30  ? 34.292  9.919   3.883  1.00 100.82 ?  57  VAL   A CA   1 
ATOM   241  C  C    . VAL   A 1 30  ? 34.926  11.086  3.141  1.00 98.35  ?  57  VAL   A C    1 
ATOM   242  O  O    . VAL   A 1 30  ? 36.151  11.252  3.160  1.00 95.19  ?  57  VAL   A O    1 
ATOM   243  C  CB   . VAL   A 1 30  ? 34.179  10.218  5.395  1.00 102.87 ?  57  VAL   A CB   1 
ATOM   244  C  CG1  . VAL   A 1 30  ? 33.962  11.704  5.646  1.00 97.29  ?  57  VAL   A CG1  1 
ATOM   245  C  CG2  . VAL   A 1 30  ? 33.061  9.398   6.018  1.00 98.42  ?  57  VAL   A CG2  1 
ATOM   246  N  N    . SER   A 1 31  ? 34.090  11.884  2.475  1.00 103.52 ?  58  SER   A N    1 
ATOM   247  C  CA   . SER   A 1 31  ? 34.572  13.023  1.704  1.00 106.79 ?  58  SER   A CA   1 
ATOM   248  C  C    . SER   A 1 31  ? 35.405  13.955  2.574  1.00 109.71 ?  58  SER   A C    1 
ATOM   249  O  O    . SER   A 1 31  ? 35.065  14.225  3.728  1.00 108.06 ?  58  SER   A O    1 
ATOM   250  C  CB   . SER   A 1 31  ? 33.389  13.787  1.104  1.00 108.45 ?  58  SER   A CB   1 
ATOM   251  O  OG   . SER   A 1 31  ? 32.951  14.815  1.978  1.00 101.48 ?  58  SER   A OG   1 
ATOM   252  N  N    . GLU   A 1 32  ? 36.516  14.439  2.014  1.00 104.78 ?  59  GLU   A N    1 
ATOM   253  C  CA   . GLU   A 1 32  ? 37.305  15.449  2.713  1.00 109.35 ?  59  GLU   A CA   1 
ATOM   254  C  C    . GLU   A 1 32  ? 36.472  16.696  2.974  1.00 113.88 ?  59  GLU   A C    1 
ATOM   255  O  O    . GLU   A 1 32  ? 36.636  17.359  4.006  1.00 115.91 ?  59  GLU   A O    1 
ATOM   256  C  CB   . GLU   A 1 32  ? 38.554  15.797  1.899  1.00 121.14 ?  59  GLU   A CB   1 
ATOM   257  C  CG   . GLU   A 1 32  ? 39.348  17.078  2.287  1.00 128.93 ?  59  GLU   A CG   1 
ATOM   258  C  CD   . GLU   A 1 32  ? 39.605  17.334  3.780  1.00 140.87 ?  59  GLU   A CD   1 
ATOM   259  O  OE1  . GLU   A 1 32  ? 40.321  18.310  4.072  1.00 143.82 ?  59  GLU   A OE1  1 
ATOM   260  O  OE2  . GLU   A 1 32  ? 39.187  16.551  4.659  1.00 129.07 ?  59  GLU   A OE2  1 
ATOM   261  N  N    . GLU   A 1 33  ? 35.572  17.033  2.043  1.00 113.27 ?  60  GLU   A N    1 
ATOM   262  C  CA   . GLU   A 1 33  ? 34.673  18.165  2.240  1.00 114.51 ?  60  GLU   A CA   1 
ATOM   263  C  C    . GLU   A 1 33  ? 33.938  18.059  3.568  1.00 107.25 ?  60  GLU   A C    1 
ATOM   264  O  O    . GLU   A 1 33  ? 33.677  19.076  4.220  1.00 117.78 ?  60  GLU   A O    1 
ATOM   265  C  CB   . GLU   A 1 33  ? 33.667  18.259  1.085  1.00 113.89 ?  60  GLU   A CB   1 
ATOM   266  C  CG   . GLU   A 1 33  ? 34.229  18.716  -0.269 1.00 128.82 ?  60  GLU   A CG   1 
ATOM   267  C  CD   . GLU   A 1 33  ? 35.468  17.951  -0.704 1.00 133.79 ?  60  GLU   A CD   1 
ATOM   268  O  OE1  . GLU   A 1 33  ? 35.460  16.706  -0.615 1.00 131.21 ?  60  GLU   A OE1  1 
ATOM   269  O  OE2  . GLU   A 1 33  ? 36.449  18.594  -1.134 1.00 130.92 ?  60  GLU   A OE2  1 
ATOM   270  N  N    . LEU   A 1 34  ? 33.619  16.835  3.995  1.00 98.66  ?  61  LEU   A N    1 
ATOM   271  C  CA   . LEU   A 1 34  ? 32.946  16.637  5.274  1.00 90.70  ?  61  LEU   A CA   1 
ATOM   272  C  C    . LEU   A 1 34  ? 33.928  16.642  6.440  1.00 104.48 ?  61  LEU   A C    1 
ATOM   273  O  O    . LEU   A 1 34  ? 33.593  17.124  7.528  1.00 92.97  ?  61  LEU   A O    1 
ATOM   274  C  CB   . LEU   A 1 34  ? 32.157  15.328  5.254  1.00 94.32  ?  61  LEU   A CB   1 
ATOM   275  C  CG   . LEU   A 1 34  ? 31.048  15.208  6.300  1.00 90.35  ?  61  LEU   A CG   1 
ATOM   276  C  CD1  . LEU   A 1 34  ? 30.006  16.293  6.091  1.00 79.14  ?  61  LEU   A CD1  1 
ATOM   277  C  CD2  . LEU   A 1 34  ? 30.409  13.829  6.255  1.00 80.39  ?  61  LEU   A CD2  1 
ATOM   278  N  N    . HIS   A 1 35  ? 35.132  16.099  6.241  1.00 107.61 ?  62  HIS   A N    1 
ATOM   279  C  CA   . HIS   A 1 35  ? 36.128  16.089  7.310  1.00 101.37 ?  62  HIS   A CA   1 
ATOM   280  C  C    . HIS   A 1 35  ? 36.462  17.506  7.762  1.00 104.66 ?  62  HIS   A C    1 
ATOM   281  O  O    . HIS   A 1 35  ? 36.485  17.799  8.962  1.00 100.34 ?  62  HIS   A O    1 
ATOM   282  C  CB   . HIS   A 1 35  ? 37.398  15.371  6.852  1.00 111.31 ?  62  HIS   A CB   1 
ATOM   283  C  CG   . HIS   A 1 35  ? 37.272  13.881  6.775  1.00 105.43 ?  62  HIS   A CG   1 
ATOM   284  N  ND1  . HIS   A 1 35  ? 36.922  13.104  7.859  1.00 94.44  ?  62  HIS   A ND1  1 
ATOM   285  C  CD2  . HIS   A 1 35  ? 37.477  13.023  5.748  1.00 99.82  ?  62  HIS   A CD2  1 
ATOM   286  C  CE1  . HIS   A 1 35  ? 36.904  11.833  7.499  1.00 101.80 ?  62  HIS   A CE1  1 
ATOM   287  N  NE2  . HIS   A 1 35  ? 37.238  11.756  6.223  1.00 96.89  ?  62  HIS   A NE2  1 
ATOM   288  N  N    . LYS   A 1 36  ? 36.723  18.401  6.806  1.00 112.63 ?  63  LYS   A N    1 
ATOM   289  C  CA   . LYS   A 1 36  ? 37.110  19.765  7.154  1.00 115.89 ?  63  LYS   A CA   1 
ATOM   290  C  C    . LYS   A 1 36  ? 35.985  20.495  7.878  1.00 110.04 ?  63  LYS   A C    1 
ATOM   291  O  O    . LYS   A 1 36  ? 36.234  21.252  8.824  1.00 118.24 ?  63  LYS   A O    1 
ATOM   292  C  CB   . LYS   A 1 36  ? 37.524  20.530  5.897  1.00 115.52 ?  63  LYS   A CB   1 
ATOM   293  N  N    . GLU   A 1 37  ? 34.739  20.276  7.454  1.00 103.15 ?  64  GLU   A N    1 
ATOM   294  C  CA   . GLU   A 1 37  ? 33.617  20.978  8.070  1.00 105.20 ?  64  GLU   A CA   1 
ATOM   295  C  C    . GLU   A 1 37  ? 33.365  20.487  9.491  1.00 101.90 ?  64  GLU   A C    1 
ATOM   296  O  O    . GLU   A 1 37  ? 33.132  21.293  10.400 1.00 95.89  ?  64  GLU   A O    1 
ATOM   297  C  CB   . GLU   A 1 37  ? 32.362  20.813  7.214  1.00 103.74 ?  64  GLU   A CB   1 
ATOM   298  C  CG   . GLU   A 1 37  ? 31.244  21.780  7.565  1.00 120.34 ?  64  GLU   A CG   1 
ATOM   299  C  CD   . GLU   A 1 37  ? 30.039  21.631  6.659  1.00 126.82 ?  64  GLU   A CD   1 
ATOM   300  O  OE1  . GLU   A 1 37  ? 30.170  20.993  5.593  1.00 133.04 ?  64  GLU   A OE1  1 
ATOM   301  O  OE2  . GLU   A 1 37  ? 28.959  22.150  7.013  1.00 111.66 ?  64  GLU   A OE2  1 
ATOM   302  N  N    . VAL   A 1 38  ? 33.406  19.170  9.702  1.00 91.66  ?  65  VAL   A N    1 
ATOM   303  C  CA   . VAL   A 1 38  ? 33.176  18.624  11.036 1.00 89.67  ?  65  VAL   A CA   1 
ATOM   304  C  C    . VAL   A 1 38  ? 34.313  19.005  11.975 1.00 96.11  ?  65  VAL   A C    1 
ATOM   305  O  O    . VAL   A 1 38  ? 34.082  19.393  13.127 1.00 94.20  ?  65  VAL   A O    1 
ATOM   306  C  CB   . VAL   A 1 38  ? 32.991  17.097  10.961 1.00 87.02  ?  65  VAL   A CB   1 
ATOM   307  C  CG1  . VAL   A 1 38  ? 33.041  16.481  12.352 1.00 74.77  ?  65  VAL   A CG1  1 
ATOM   308  C  CG2  . VAL   A 1 38  ? 31.681  16.753  10.268 1.00 80.62  ?  65  VAL   A CG2  1 
ATOM   309  N  N    . GLN   A 1 39  ? 35.556  18.911  11.498 1.00 96.96  ?  66  GLN   A N    1 
ATOM   310  C  CA   . GLN   A 1 39  ? 36.700  19.193  12.357 1.00 102.96 ?  66  GLN   A CA   1 
ATOM   311  C  C    . GLN   A 1 39  ? 36.792  20.673  12.709 1.00 104.27 ?  66  GLN   A C    1 
ATOM   312  O  O    . GLN   A 1 39  ? 37.281  21.020  13.790 1.00 102.34 ?  66  GLN   A O    1 
ATOM   313  C  CB   . GLN   A 1 39  ? 37.985  18.712  11.683 1.00 99.11  ?  66  GLN   A CB   1 
ATOM   314  C  CG   . GLN   A 1 39  ? 38.087  17.196  11.600 1.00 93.32  ?  66  GLN   A CG   1 
ATOM   315  C  CD   . GLN   A 1 39  ? 39.263  16.727  10.765 1.00 104.03 ?  66  GLN   A CD   1 
ATOM   316  O  OE1  . GLN   A 1 39  ? 40.212  17.474  10.530 1.00 109.07 ?  66  GLN   A OE1  1 
ATOM   317  N  NE2  . GLN   A 1 39  ? 39.204  15.479  10.311 1.00 94.20  ?  66  GLN   A NE2  1 
ATOM   318  N  N    . GLU   A 1 40  ? 36.326  21.556  11.823 1.00 105.36 ?  67  GLU   A N    1 
ATOM   319  C  CA   . GLU   A 1 40  ? 36.279  22.976  12.152 1.00 104.06 ?  67  GLU   A CA   1 
ATOM   320  C  C    . GLU   A 1 40  ? 35.137  23.300  13.106 1.00 101.94 ?  67  GLU   A C    1 
ATOM   321  O  O    . GLU   A 1 40  ? 35.269  24.205  13.937 1.00 107.70 ?  67  GLU   A O    1 
ATOM   322  C  CB   . GLU   A 1 40  ? 36.148  23.814  10.880 1.00 110.23 ?  67  GLU   A CB   1 
ATOM   323  C  CG   . GLU   A 1 40  ? 37.462  24.382  10.372 1.00 123.22 ?  67  GLU   A CG   1 
ATOM   324  C  CD   . GLU   A 1 40  ? 37.547  24.387  8.859  1.00 140.88 ?  67  GLU   A CD   1 
ATOM   325  O  OE1  . GLU   A 1 40  ? 38.675  24.392  8.324  1.00 140.10 ?  67  GLU   A OE1  1 
ATOM   326  O  OE2  . GLU   A 1 40  ? 36.483  24.384  8.205  1.00 135.89 ?  67  GLU   A OE2  1 
ATOM   327  N  N    . ALA   A 1 41  ? 34.015  22.583  13.000 1.00 92.85  ?  68  ALA   A N    1 
ATOM   328  C  CA   . ALA   A 1 41  ? 32.920  22.781  13.943 1.00 83.95  ?  68  ALA   A CA   1 
ATOM   329  C  C    . ALA   A 1 41  ? 33.293  22.292  15.336 1.00 94.53  ?  68  ALA   A C    1 
ATOM   330  O  O    . ALA   A 1 41  ? 32.838  22.863  16.335 1.00 96.99  ?  68  ALA   A O    1 
ATOM   331  C  CB   . ALA   A 1 41  ? 31.663  22.069  13.448 1.00 84.23  ?  68  ALA   A CB   1 
ATOM   332  N  N    . PHE   A 1 42  ? 34.106  21.235  15.422 1.00 97.73  ?  69  PHE   A N    1 
ATOM   333  C  CA   . PHE   A 1 42  ? 34.640  20.801  16.709 1.00 94.75  ?  69  PHE   A CA   1 
ATOM   334  C  C    . PHE   A 1 42  ? 35.416  21.923  17.387 1.00 100.40 ?  69  PHE   A C    1 
ATOM   335  O  O    . PHE   A 1 42  ? 35.194  22.228  18.564 1.00 100.05 ?  69  PHE   A O    1 
ATOM   336  C  CB   . PHE   A 1 42  ? 35.533  19.576  16.509 1.00 93.54  ?  69  PHE   A CB   1 
ATOM   337  C  CG   . PHE   A 1 42  ? 34.787  18.272  16.477 1.00 91.05  ?  69  PHE   A CG   1 
ATOM   338  C  CD1  . PHE   A 1 42  ? 33.574  18.129  17.129 1.00 95.58  ?  69  PHE   A CD1  1 
ATOM   339  C  CD2  . PHE   A 1 42  ? 35.291  17.195  15.769 1.00 95.24  ?  69  PHE   A CD2  1 
ATOM   340  C  CE1  . PHE   A 1 42  ? 32.895  16.922  17.100 1.00 94.29  ?  69  PHE   A CE1  1 
ATOM   341  C  CE2  . PHE   A 1 42  ? 34.613  15.993  15.727 1.00 97.31  ?  69  PHE   A CE2  1 
ATOM   342  C  CZ   . PHE   A 1 42  ? 33.411  15.857  16.389 1.00 89.97  ?  69  PHE   A CZ   1 
ATOM   343  N  N    . LEU   A 1 43  ? 36.334  22.552  16.651 1.00 99.14  ?  70  LEU   A N    1 
ATOM   344  C  CA   . LEU   A 1 43  ? 37.147  23.625  17.207 1.00 101.71 ?  70  LEU   A CA   1 
ATOM   345  C  C    . LEU   A 1 43  ? 36.370  24.923  17.374 1.00 105.77 ?  70  LEU   A C    1 
ATOM   346  O  O    . LEU   A 1 43  ? 36.743  25.748  18.216 1.00 105.82 ?  70  LEU   A O    1 
ATOM   347  C  CB   . LEU   A 1 43  ? 38.373  23.861  16.323 1.00 103.86 ?  70  LEU   A CB   1 
ATOM   348  C  CG   . LEU   A 1 43  ? 39.314  22.659  16.196 1.00 103.25 ?  70  LEU   A CG   1 
ATOM   349  C  CD1  . LEU   A 1 43  ? 39.962  22.617  14.818 1.00 101.61 ?  70  LEU   A CD1  1 
ATOM   350  C  CD2  . LEU   A 1 43  ? 40.366  22.666  17.297 1.00 104.11 ?  70  LEU   A CD2  1 
ATOM   351  N  N    . THR   A 1 44  ? 35.305  25.126  16.593 1.00 100.05 ?  71  THR   A N    1 
ATOM   352  C  CA   . THR   A 1 44  ? 34.469  26.307  16.781 1.00 94.61  ?  71  THR   A CA   1 
ATOM   353  C  C    . THR   A 1 44  ? 33.730  26.246  18.112 1.00 105.64 ?  71  THR   A C    1 
ATOM   354  O  O    . THR   A 1 44  ? 33.682  27.238  18.850 1.00 108.64 ?  71  THR   A O    1 
ATOM   355  C  CB   . THR   A 1 44  ? 33.482  26.446  15.618 1.00 100.81 ?  71  THR   A CB   1 
ATOM   356  O  OG1  . THR   A 1 44  ? 34.134  27.073  14.507 1.00 102.20 ?  71  THR   A OG1  1 
ATOM   357  C  CG2  . THR   A 1 44  ? 32.275  27.286  16.023 1.00 105.77 ?  71  THR   A CG2  1 
ATOM   358  N  N    . LEU   A 1 45  ? 33.160  25.084  18.444 1.00 102.12 ?  72  LEU   A N    1 
ATOM   359  C  CA   . LEU   A 1 45  ? 32.472  24.937  19.722 1.00 99.20  ?  72  LEU   A CA   1 
ATOM   360  C  C    . LEU   A 1 45  ? 33.446  24.958  20.892 1.00 97.83  ?  72  LEU   A C    1 
ATOM   361  O  O    . LEU   A 1 45  ? 33.097  25.441  21.976 1.00 99.68  ?  72  LEU   A O    1 
ATOM   362  C  CB   . LEU   A 1 45  ? 31.657  23.644  19.737 1.00 83.19  ?  72  LEU   A CB   1 
ATOM   363  C  CG   . LEU   A 1 45  ? 30.621  23.485  18.625 1.00 81.33  ?  72  LEU   A CG   1 
ATOM   364  C  CD1  . LEU   A 1 45  ? 30.372  22.017  18.333 1.00 79.20  ?  72  LEU   A CD1  1 
ATOM   365  C  CD2  . LEU   A 1 45  ? 29.326  24.184  19.000 1.00 89.43  ?  72  LEU   A CD2  1 
ATOM   366  N  N    . HIS   A 1 46  ? 34.662  24.443  20.700 1.00 100.73 ?  73  HIS   A N    1 
ATOM   367  C  CA   . HIS   A 1 46  ? 35.644  24.459  21.779 1.00 109.90 ?  73  HIS   A CA   1 
ATOM   368  C  C    . HIS   A 1 46  ? 36.116  25.878  22.074 1.00 113.80 ?  73  HIS   A C    1 
ATOM   369  O  O    . HIS   A 1 46  ? 36.313  26.242  23.239 1.00 110.93 ?  73  HIS   A O    1 
ATOM   370  C  CB   . HIS   A 1 46  ? 36.830  23.561  21.425 1.00 109.16 ?  73  HIS   A CB   1 
ATOM   371  C  CG   . HIS   A 1 46  ? 37.873  23.487  22.497 1.00 116.06 ?  73  HIS   A CG   1 
ATOM   372  N  ND1  . HIS   A 1 46  ? 39.197  23.794  22.271 1.00 119.49 ?  73  HIS   A ND1  1 
ATOM   373  C  CD2  . HIS   A 1 46  ? 37.786  23.138  23.803 1.00 111.35 ?  73  HIS   A CD2  1 
ATOM   374  C  CE1  . HIS   A 1 46  ? 39.881  23.639  23.391 1.00 116.12 ?  73  HIS   A CE1  1 
ATOM   375  N  NE2  . HIS   A 1 46  ? 39.048  23.241  24.336 1.00 113.69 ?  73  HIS   A NE2  1 
ATOM   376  N  N    . LYS   A 1 47  ? 36.299  26.693  21.031 1.00 108.50 ?  74  LYS   A N    1 
ATOM   377  C  CA   . LYS   A 1 47  ? 36.743  28.068  21.234 1.00 116.93 ?  74  LYS   A CA   1 
ATOM   378  C  C    . LYS   A 1 47  ? 35.668  28.901  21.922 1.00 120.10 ?  74  LYS   A C    1 
ATOM   379  O  O    . LYS   A 1 47  ? 35.979  29.764  22.751 1.00 113.53 ?  74  LYS   A O    1 
ATOM   380  C  CB   . LYS   A 1 47  ? 37.137  28.696  19.897 1.00 115.77 ?  74  LYS   A CB   1 
ATOM   381  N  N    . HIS   A 1 48  ? 34.401  28.658  21.594 1.00 107.49 ?  75  HIS   A N    1 
ATOM   382  C  CA   . HIS   A 1 48  ? 33.299  29.362  22.235 1.00 101.19 ?  75  HIS   A CA   1 
ATOM   383  C  C    . HIS   A 1 48  ? 32.947  28.790  23.603 1.00 105.21 ?  75  HIS   A C    1 
ATOM   384  O  O    . HIS   A 1 48  ? 31.982  29.255  24.220 1.00 106.71 ?  75  HIS   A O    1 
ATOM   385  C  CB   . HIS   A 1 48  ? 32.063  29.341  21.332 1.00 99.20  ?  75  HIS   A CB   1 
ATOM   386  C  CG   . HIS   A 1 48  ? 32.189  30.199  20.110 1.00 106.36 ?  75  HIS   A CG   1 
ATOM   387  N  ND1  . HIS   A 1 48  ? 31.162  30.997  19.651 1.00 110.51 ?  75  HIS   A ND1  1 
ATOM   388  C  CD2  . HIS   A 1 48  ? 33.219  30.382  19.250 1.00 117.08 ?  75  HIS   A CD2  1 
ATOM   389  C  CE1  . HIS   A 1 48  ? 31.554  31.635  18.563 1.00 102.75 ?  75  HIS   A CE1  1 
ATOM   390  N  NE2  . HIS   A 1 48  ? 32.799  31.279  18.298 1.00 113.80 ?  75  HIS   A NE2  1 
ATOM   391  N  N    . GLY   A 1 49  ? 33.697  27.800  24.085 1.00 103.74 ?  76  GLY   A N    1 
ATOM   392  C  CA   . GLY   A 1 49  ? 33.485  27.237  25.406 1.00 87.52  ?  76  GLY   A CA   1 
ATOM   393  C  C    . GLY   A 1 49  ? 32.153  26.536  25.579 1.00 91.26  ?  76  GLY   A C    1 
ATOM   394  O  O    . GLY   A 1 49  ? 31.476  26.726  26.592 1.00 82.53  ?  76  GLY   A O    1 
ATOM   395  N  N    . CYS   A 1 50  ? 31.774  25.709  24.608 1.00 98.26  ?  77  CYS   A N    1 
ATOM   396  C  CA   . CYS   A 1 50  ? 30.471  25.059  24.608 1.00 102.11 ?  77  CYS   A CA   1 
ATOM   397  C  C    . CYS   A 1 50  ? 30.501  23.639  25.155 1.00 94.40  ?  77  CYS   A C    1 
ATOM   398  O  O    . CYS   A 1 50  ? 29.443  23.012  25.264 1.00 98.58  ?  77  CYS   A O    1 
ATOM   399  C  CB   . CYS   A 1 50  ? 29.890  25.051  23.193 1.00 101.70 ?  77  CYS   A CB   1 
ATOM   400  S  SG   . CYS   A 1 50  ? 29.345  26.674  22.640 1.00 107.63 ?  77  CYS   A SG   1 
ATOM   401  N  N    . LEU   A 1 51  ? 31.673  23.117  25.500 1.00 91.23  ?  78  LEU   A N    1 
ATOM   402  C  CA   . LEU   A 1 51  ? 31.794  21.782  26.070 1.00 82.63  ?  78  LEU   A CA   1 
ATOM   403  C  C    . LEU   A 1 51  ? 32.046  21.893  27.566 1.00 78.58  ?  78  LEU   A C    1 
ATOM   404  O  O    . LEU   A 1 51  ? 32.942  22.625  27.999 1.00 89.98  ?  78  LEU   A O    1 
ATOM   405  C  CB   . LEU   A 1 51  ? 32.916  20.998  25.392 1.00 74.81  ?  78  LEU   A CB   1 
ATOM   406  C  CG   . LEU   A 1 51  ? 32.656  20.655  23.925 1.00 76.42  ?  78  LEU   A CG   1 
ATOM   407  C  CD1  . LEU   A 1 51  ? 33.576  21.447  23.011 1.00 81.24  ?  78  LEU   A CD1  1 
ATOM   408  C  CD2  . LEU   A 1 51  ? 32.804  19.159  23.686 1.00 96.71  ?  78  LEU   A CD2  1 
ATOM   409  N  N    . PHE   A 1 52  ? 31.255  21.165  28.351 1.00 72.83  ?  79  PHE   A N    1 
ATOM   410  C  CA   . PHE   A 1 52  ? 31.288  21.273  29.800 1.00 82.75  ?  79  PHE   A CA   1 
ATOM   411  C  C    . PHE   A 1 52  ? 31.433  19.898  30.433 1.00 72.95  ?  79  PHE   A C    1 
ATOM   412  O  O    . PHE   A 1 52  ? 30.953  18.893  29.901 1.00 71.49  ?  79  PHE   A O    1 
ATOM   413  C  CB   . PHE   A 1 52  ? 30.022  21.948  30.344 1.00 87.69  ?  79  PHE   A CB   1 
ATOM   414  C  CG   . PHE   A 1 52  ? 29.738  23.288  29.733 1.00 100.18 ?  79  PHE   A CG   1 
ATOM   415  C  CD1  . PHE   A 1 52  ? 28.988  23.404  28.576 1.00 98.22  ?  79  PHE   A CD1  1 
ATOM   416  C  CD2  . PHE   A 1 52  ? 30.197  24.437  30.343 1.00 94.57  ?  79  PHE   A CD2  1 
ATOM   417  C  CE1  . PHE   A 1 52  ? 28.724  24.649  28.029 1.00 101.91 ?  79  PHE   A CE1  1 
ATOM   418  C  CE2  . PHE   A 1 52  ? 29.939  25.681  29.807 1.00 100.10 ?  79  PHE   A CE2  1 
ATOM   419  C  CZ   . PHE   A 1 52  ? 29.202  25.788  28.649 1.00 108.01 ?  79  PHE   A CZ   1 
ATOM   420  N  N    . ARG   A 1 53  ? 32.103  19.868  31.582 1.00 74.54  ?  80  ARG   A N    1 
ATOM   421  C  CA   . ARG   A 1 53  ? 32.147  18.670  32.403 1.00 76.25  ?  80  ARG   A CA   1 
ATOM   422  C  C    . ARG   A 1 53  ? 30.898  18.604  33.271 1.00 83.10  ?  80  ARG   A C    1 
ATOM   423  O  O    . ARG   A 1 53  ? 30.486  19.604  33.867 1.00 86.20  ?  80  ARG   A O    1 
ATOM   424  C  CB   . ARG   A 1 53  ? 33.400  18.663  33.278 1.00 79.78  ?  80  ARG   A CB   1 
ATOM   425  C  CG   . ARG   A 1 53  ? 34.682  18.319  32.534 1.00 80.44  ?  80  ARG   A CG   1 
ATOM   426  C  CD   . ARG   A 1 53  ? 35.912  18.770  33.309 1.00 93.87  ?  80  ARG   A CD   1 
ATOM   427  N  NE   . ARG   A 1 53  ? 36.176  17.926  34.468 1.00 101.07 ?  80  ARG   A NE   1 
ATOM   428  C  CZ   . ARG   A 1 53  ? 37.356  17.395  34.757 1.00 105.69 ?  80  ARG   A CZ   1 
ATOM   429  N  NH1  . ARG   A 1 53  ? 38.412  17.594  33.984 1.00 105.02 ?  80  ARG   A NH1  1 
ATOM   430  N  NH2  . ARG   A 1 53  ? 37.482  16.646  35.849 1.00 102.70 ?  80  ARG   A NH2  1 
ATOM   431  N  N    . ASP   A 1 54  ? 30.289  17.426  33.334 1.00 85.83  ?  81  ASP   A N    1 
ATOM   432  C  CA   . ASP   A 1 54  ? 29.057  17.245  34.086 1.00 74.90  ?  81  ASP   A CA   1 
ATOM   433  C  C    . ASP   A 1 54  ? 29.354  16.777  35.505 1.00 76.59  ?  81  ASP   A C    1 
ATOM   434  O  O    . ASP   A 1 54  ? 30.363  16.117  35.768 1.00 84.03  ?  81  ASP   A O    1 
ATOM   435  C  CB   . ASP   A 1 54  ? 28.139  16.243  33.384 1.00 76.11  ?  81  ASP   A CB   1 
ATOM   436  C  CG   . ASP   A 1 54  ? 27.587  16.777  32.075 1.00 86.86  ?  81  ASP   A CG   1 
ATOM   437  O  OD1  . ASP   A 1 54  ? 26.703  17.658  32.116 1.00 78.58  ?  81  ASP   A OD1  1 
ATOM   438  O  OD2  . ASP   A 1 54  ? 28.040  16.316  31.006 1.00 99.90  ?  81  ASP   A OD2  1 
ATOM   439  N  N    . LEU   A 1 55  ? 28.462  17.134  36.425 1.00 84.65  ?  82  LEU   A N    1 
ATOM   440  C  CA   . LEU   A 1 55  ? 28.573  16.756  37.832 1.00 77.60  ?  82  LEU   A CA   1 
ATOM   441  C  C    . LEU   A 1 55  ? 27.526  15.679  38.103 1.00 82.90  ?  82  LEU   A C    1 
ATOM   442  O  O    . LEU   A 1 55  ? 26.465  15.936  38.675 1.00 88.27  ?  82  LEU   A O    1 
ATOM   443  C  CB   . LEU   A 1 55  ? 28.392  17.976  38.739 1.00 81.66  ?  82  LEU   A CB   1 
ATOM   444  C  CG   . LEU   A 1 55  ? 28.745  17.789  40.215 1.00 90.68  ?  82  LEU   A CG   1 
ATOM   445  C  CD1  . LEU   A 1 55  ? 30.140  17.204  40.360 1.00 96.97  ?  82  LEU   A CD1  1 
ATOM   446  C  CD2  . LEU   A 1 55  ? 28.633  19.107  40.963 1.00 94.17  ?  82  LEU   A CD2  1 
ATOM   447  N  N    . VAL   A 1 56  ? 27.836  14.455  37.681 1.00 71.63  ?  83  VAL   A N    1 
ATOM   448  C  CA   . VAL   A 1 56  ? 26.903  13.338  37.775 1.00 77.08  ?  83  VAL   A CA   1 
ATOM   449  C  C    . VAL   A 1 56  ? 26.969  12.721  39.165 1.00 79.42  ?  83  VAL   A C    1 
ATOM   450  O  O    . VAL   A 1 56  ? 27.786  13.124  40.000 1.00 87.45  ?  83  VAL   A O    1 
ATOM   451  C  CB   . VAL   A 1 56  ? 27.194  12.282  36.692 1.00 71.67  ?  83  VAL   A CB   1 
ATOM   452  C  CG1  . VAL   A 1 56  ? 27.124  12.908  35.308 1.00 72.71  ?  83  VAL   A CG1  1 
ATOM   453  C  CG2  . VAL   A 1 56  ? 28.554  11.644  36.926 1.00 87.34  ?  83  VAL   A CG2  1 
ATOM   454  N  N    . ARG   A 1 57  ? 26.102  11.742  39.422 1.00 75.14  ?  84  ARG   A N    1 
ATOM   455  C  CA   . ARG   A 1 57  ? 26.098  10.998  40.676 1.00 77.33  ?  84  ARG   A CA   1 
ATOM   456  C  C    . ARG   A 1 57  ? 26.066  9.511   40.362 1.00 96.72  ?  84  ARG   A C    1 
ATOM   457  O  O    . ARG   A 1 57  ? 25.177  9.046   39.642 1.00 88.95  ?  84  ARG   A O    1 
ATOM   458  C  CB   . ARG   A 1 57  ? 24.907  11.386  41.558 1.00 77.68  ?  84  ARG   A CB   1 
ATOM   459  C  CG   . ARG   A 1 57  ? 25.000  10.833  42.972 1.00 89.93  ?  84  ARG   A CG   1 
ATOM   460  C  CD   . ARG   A 1 57  ? 23.964  11.443  43.902 1.00 87.88  ?  84  ARG   A CD   1 
ATOM   461  N  NE   . ARG   A 1 57  ? 24.307  11.208  45.299 1.00 99.83  ?  84  ARG   A NE   1 
ATOM   462  C  CZ   . ARG   A 1 57  ? 24.296  12.138  46.245 1.00 110.43 ?  84  ARG   A CZ   1 
ATOM   463  N  NH1  . ARG   A 1 57  ? 23.941  13.384  45.985 1.00 102.82 ?  84  ARG   A NH1  1 
ATOM   464  N  NH2  . ARG   A 1 57  ? 24.648  11.808  47.484 1.00 111.10 ?  84  ARG   A NH2  1 
ATOM   465  N  N    . ILE   A 1 58  ? 27.037  8.774   40.895 1.00 96.43  ?  85  ILE   A N    1 
ATOM   466  C  CA   . ILE   A 1 58  ? 27.136  7.330   40.716 1.00 93.85  ?  85  ILE   A CA   1 
ATOM   467  C  C    . ILE   A 1 58  ? 27.314  6.702   42.089 1.00 101.59 ?  85  ILE   A C    1 
ATOM   468  O  O    . ILE   A 1 58  ? 28.292  6.998   42.784 1.00 100.56 ?  85  ILE   A O    1 
ATOM   469  C  CB   . ILE   A 1 58  ? 28.304  6.933   39.796 1.00 94.52  ?  85  ILE   A CB   1 
ATOM   470  C  CG1  . ILE   A 1 58  ? 28.432  7.906   38.622 1.00 102.63 ?  85  ILE   A CG1  1 
ATOM   471  C  CG2  . ILE   A 1 58  ? 28.128  5.503   39.298 1.00 98.91  ?  85  ILE   A CG2  1 
ATOM   472  C  CD1  . ILE   A 1 58  ? 29.361  7.424   37.526 1.00 111.55 ?  85  ILE   A CD1  1 
ATOM   473  N  N    . GLN   A 1 59  ? 26.375  5.839   42.477 1.00 104.75 ?  86  GLN   A N    1 
ATOM   474  C  CA   . GLN   A 1 59  ? 26.489  5.048   43.704 1.00 98.19  ?  86  GLN   A CA   1 
ATOM   475  C  C    . GLN   A 1 59  ? 26.608  5.937   44.941 1.00 103.67 ?  86  GLN   A C    1 
ATOM   476  O  O    . GLN   A 1 59  ? 27.295  5.598   45.907 1.00 114.28 ?  86  GLN   A O    1 
ATOM   477  C  CB   . GLN   A 1 59  ? 27.666  4.072   43.623 1.00 101.73 ?  86  GLN   A CB   1 
ATOM   478  C  CG   . GLN   A 1 59  ? 27.808  3.382   42.277 1.00 104.96 ?  86  GLN   A CG   1 
ATOM   479  C  CD   . GLN   A 1 59  ? 27.345  1.945   42.315 1.00 111.02 ?  86  GLN   A CD   1 
ATOM   480  O  OE1  . GLN   A 1 59  ? 26.189  1.672   42.620 1.00 109.89 ?  86  GLN   A OE1  1 
ATOM   481  N  NE2  . GLN   A 1 59  ? 28.243  1.019   42.001 1.00 106.18 ?  86  GLN   A NE2  1 
ATOM   482  N  N    . GLY   A 1 60  ? 25.938  7.087   44.912 1.00 105.31 ?  87  GLY   A N    1 
ATOM   483  C  CA   . GLY   A 1 60  ? 25.875  7.967   46.059 1.00 113.70 ?  87  GLY   A CA   1 
ATOM   484  C  C    . GLY   A 1 60  ? 26.977  9.000   46.167 1.00 120.54 ?  87  GLY   A C    1 
ATOM   485  O  O    . GLY   A 1 60  ? 26.940  9.821   47.093 1.00 119.38 ?  87  GLY   A O    1 
ATOM   486  N  N    . LYS   A 1 61  ? 27.953  8.992   45.263 1.00 105.80 ?  88  LYS   A N    1 
ATOM   487  C  CA   . LYS   A 1 61  ? 29.045  9.955   45.286 1.00 106.23 ?  88  LYS   A CA   1 
ATOM   488  C  C    . LYS   A 1 61  ? 28.988  10.826  44.039 1.00 95.66  ?  88  LYS   A C    1 
ATOM   489  O  O    . LYS   A 1 61  ? 28.628  10.355  42.955 1.00 91.99  ?  88  LYS   A O    1 
ATOM   490  C  CB   . LYS   A 1 61  ? 30.408  9.251   45.386 1.00 110.77 ?  88  LYS   A CB   1 
ATOM   491  C  CG   . LYS   A 1 61  ? 30.613  8.131   44.382 1.00 97.15  ?  88  LYS   A CG   1 
ATOM   492  C  CD   . LYS   A 1 61  ? 31.065  6.846   45.061 1.00 104.93 ?  88  LYS   A CD   1 
ATOM   493  C  CE   . LYS   A 1 61  ? 31.384  5.764   44.040 1.00 98.27  ?  88  LYS   A CE   1 
ATOM   494  N  NZ   . LYS   A 1 61  ? 31.917  4.529   44.681 1.00 92.95  ?  88  LYS   A NZ   1 
ATOM   495  N  N    . ASP   A 1 62  ? 29.336  12.101  44.202 1.00 105.46 ?  89  ASP   A N    1 
ATOM   496  C  CA   . ASP   A 1 62  ? 29.303  13.064  43.110 1.00 99.54  ?  89  ASP   A CA   1 
ATOM   497  C  C    . ASP   A 1 62  ? 30.656  13.101  42.410 1.00 91.97  ?  89  ASP   A C    1 
ATOM   498  O  O    . ASP   A 1 62  ? 31.688  13.327  43.049 1.00 92.00  ?  89  ASP   A O    1 
ATOM   499  C  CB   . ASP   A 1 62  ? 28.933  14.454  43.630 1.00 112.87 ?  89  ASP   A CB   1 
ATOM   500  C  CG   . ASP   A 1 62  ? 27.833  14.411  44.674 1.00 107.23 ?  89  ASP   A CG   1 
ATOM   501  O  OD1  . ASP   A 1 62  ? 26.663  14.195  44.294 1.00 102.12 ?  89  ASP   A OD1  1 
ATOM   502  O  OD2  . ASP   A 1 62  ? 28.138  14.592  45.871 1.00 105.26 ?  89  ASP   A OD2  1 
ATOM   503  N  N    . LEU   A 1 63  ? 30.643  12.882  41.097 1.00 81.96  ?  90  LEU   A N    1 
ATOM   504  C  CA   . LEU   A 1 63  ? 31.853  12.776  40.293 1.00 87.68  ?  90  LEU   A CA   1 
ATOM   505  C  C    . LEU   A 1 63  ? 31.853  13.825  39.191 1.00 81.58  ?  90  LEU   A C    1 
ATOM   506  O  O    . LEU   A 1 63  ? 30.816  14.097  38.579 1.00 90.10  ?  90  LEU   A O    1 
ATOM   507  C  CB   . LEU   A 1 63  ? 31.979  11.382  39.663 1.00 89.83  ?  90  LEU   A CB   1 
ATOM   508  C  CG   . LEU   A 1 63  ? 32.102  10.127  40.531 1.00 88.62  ?  90  LEU   A CG   1 
ATOM   509  C  CD1  . LEU   A 1 63  ? 32.953  9.099   39.811 1.00 91.94  ?  90  LEU   A CD1  1 
ATOM   510  C  CD2  . LEU   A 1 63  ? 32.702  10.439  41.893 1.00 83.81  ?  90  LEU   A CD2  1 
ATOM   511  N  N    . LEU   A 1 64  ? 33.022  14.407  38.938 1.00 83.10  ?  91  LEU   A N    1 
ATOM   512  C  CA   . LEU   A 1 64  ? 33.230  15.264  37.778 1.00 80.68  ?  91  LEU   A CA   1 
ATOM   513  C  C    . LEU   A 1 64  ? 33.733  14.404  36.626 1.00 85.49  ?  91  LEU   A C    1 
ATOM   514  O  O    . LEU   A 1 64  ? 34.739  13.699  36.765 1.00 99.11  ?  91  LEU   A O    1 
ATOM   515  C  CB   . LEU   A 1 64  ? 34.226  16.381  38.087 1.00 100.83 ?  91  LEU   A CB   1 
ATOM   516  C  CG   . LEU   A 1 64  ? 33.697  17.816  38.123 1.00 96.53  ?  91  LEU   A CG   1 
ATOM   517  C  CD1  . LEU   A 1 64  ? 34.849  18.808  38.075 1.00 76.14  ?  91  LEU   A CD1  1 
ATOM   518  C  CD2  . LEU   A 1 64  ? 32.725  18.068  36.979 1.00 89.40  ?  91  LEU   A CD2  1 
ATOM   519  N  N    . THR   A 1 65  ? 33.036  14.456  35.499 1.00 87.05  ?  92  THR   A N    1 
ATOM   520  C  CA   . THR   A 1 65  ? 33.434  13.657  34.347 1.00 88.60  ?  92  THR   A CA   1 
ATOM   521  C  C    . THR   A 1 65  ? 34.757  14.170  33.792 1.00 82.01  ?  92  THR   A C    1 
ATOM   522  O  O    . THR   A 1 65  ? 34.929  15.384  33.635 1.00 87.81  ?  92  THR   A O    1 
ATOM   523  C  CB   . THR   A 1 65  ? 32.359  13.698  33.260 1.00 86.09  ?  92  THR   A CB   1 
ATOM   524  O  OG1  . THR   A 1 65  ? 32.476  14.916  32.513 1.00 83.36  ?  92  THR   A OG1  1 
ATOM   525  C  CG2  . THR   A 1 65  ? 30.972  13.611  33.873 1.00 90.31  ?  92  THR   A CG2  1 
ATOM   526  N  N    . PRO   A 1 66  ? 35.716  13.291  33.496 1.00 86.42  ?  93  PRO   A N    1 
ATOM   527  C  CA   . PRO   A 1 66  ? 36.950  13.752  32.839 1.00 96.63  ?  93  PRO   A CA   1 
ATOM   528  C  C    . PRO   A 1 66  ? 36.708  14.314  31.451 1.00 87.06  ?  93  PRO   A C    1 
ATOM   529  O  O    . PRO   A 1 66  ? 37.566  15.038  30.931 1.00 94.90  ?  93  PRO   A O    1 
ATOM   530  C  CB   . PRO   A 1 66  ? 37.832  12.496  32.779 1.00 95.18  ?  93  PRO   A CB   1 
ATOM   531  C  CG   . PRO   A 1 66  ? 37.024  11.367  33.297 1.00 94.70  ?  93  PRO   A CG   1 
ATOM   532  C  CD   . PRO   A 1 66  ? 35.742  11.866  33.864 1.00 97.17  ?  93  PRO   A CD   1 
ATOM   533  N  N    . VAL   A 1 67  ? 35.566  14.013  30.843 1.00 72.37  ?  94  VAL   A N    1 
ATOM   534  C  CA   . VAL   A 1 67  ? 35.277  14.368  29.459 1.00 78.79  ?  94  VAL   A CA   1 
ATOM   535  C  C    . VAL   A 1 67  ? 34.325  15.555  29.430 1.00 71.46  ?  94  VAL   A C    1 
ATOM   536  O  O    . VAL   A 1 67  ? 33.345  15.601  30.185 1.00 80.26  ?  94  VAL   A O    1 
ATOM   537  C  CB   . VAL   A 1 67  ? 34.683  13.162  28.706 1.00 79.32  ?  94  VAL   A CB   1 
ATOM   538  C  CG1  . VAL   A 1 67  ? 34.272  13.557  27.303 1.00 81.69  ?  94  VAL   A CG1  1 
ATOM   539  C  CG2  . VAL   A 1 67  ? 35.680  12.012  28.674 1.00 76.94  ?  94  VAL   A CG2  1 
ATOM   540  N  N    . SER   A 1 68  ? 34.615  16.521  28.560 1.00 69.27  ?  95  SER   A N    1 
ATOM   541  C  CA   . SER   A 1 68  ? 33.727  17.651  28.327 1.00 68.58  ?  95  SER   A CA   1 
ATOM   542  C  C    . SER   A 1 68  ? 32.714  17.288  27.250 1.00 73.76  ?  95  SER   A C    1 
ATOM   543  O  O    . SER   A 1 68  ? 33.058  16.648  26.252 1.00 84.08  ?  95  SER   A O    1 
ATOM   544  C  CB   . SER   A 1 68  ? 34.525  18.885  27.906 1.00 70.86  ?  95  SER   A CB   1 
ATOM   545  O  OG   . SER   A 1 68  ? 35.531  19.189  28.856 1.00 79.49  ?  95  SER   A OG   1 
ATOM   546  N  N    . ARG   A 1 69  ? 31.463  17.700  27.451 1.00 74.48  ?  96  ARG   A N    1 
ATOM   547  C  CA   . ARG   A 1 69  ? 30.374  17.241  26.601 1.00 71.54  ?  96  ARG   A CA   1 
ATOM   548  C  C    . ARG   A 1 69  ? 29.443  18.387  26.232 1.00 76.53  ?  96  ARG   A C    1 
ATOM   549  O  O    . ARG   A 1 69  ? 29.385  19.418  26.906 1.00 67.10  ?  96  ARG   A O    1 
ATOM   550  C  CB   . ARG   A 1 69  ? 29.571  16.124  27.281 1.00 75.73  ?  96  ARG   A CB   1 
ATOM   551  C  CG   . ARG   A 1 69  ? 30.324  14.815  27.390 1.00 92.37  ?  96  ARG   A CG   1 
ATOM   552  C  CD   . ARG   A 1 69  ? 29.620  13.832  28.304 1.00 91.20  ?  96  ARG   A CD   1 
ATOM   553  N  NE   . ARG   A 1 69  ? 30.575  13.058  29.086 1.00 87.19  ?  96  ARG   A NE   1 
ATOM   554  C  CZ   . ARG   A 1 69  ? 31.119  11.917  28.687 1.00 97.05  ?  96  ARG   A CZ   1 
ATOM   555  N  NH1  . ARG   A 1 69  ? 30.809  11.375  27.520 1.00 91.73  ?  96  ARG   A NH1  1 
ATOM   556  N  NH2  . ARG   A 1 69  ? 31.995  11.304  29.477 1.00 100.53 ?  96  ARG   A NH2  1 
ATOM   557  N  N    . ILE   A 1 70  ? 28.712  18.181  25.136 1.00 74.01  ?  97  ILE   A N    1 
ATOM   558  C  CA   . ILE   A 1 70  ? 27.605  19.044  24.737 1.00 67.44  ?  97  ILE   A CA   1 
ATOM   559  C  C    . ILE   A 1 70  ? 26.649  18.226  23.881 1.00 69.26  ?  97  ILE   A C    1 
ATOM   560  O  O    . ILE   A 1 70  ? 27.074  17.530  22.952 1.00 71.24  ?  97  ILE   A O    1 
ATOM   561  C  CB   . ILE   A 1 70  ? 28.091  20.297  23.985 1.00 76.33  ?  97  ILE   A CB   1 
ATOM   562  C  CG1  . ILE   A 1 70  ? 26.916  20.968  23.266 1.00 82.89  ?  97  ILE   A CG1  1 
ATOM   563  C  CG2  . ILE   A 1 70  ? 29.188  19.939  22.994 1.00 81.39  ?  97  ILE   A CG2  1 
ATOM   564  C  CD1  . ILE   A 1 70  ? 27.141  22.428  22.953 1.00 84.20  ?  97  ILE   A CD1  1 
ATOM   565  N  N    . LEU   A 1 71  ? 25.356  18.294  24.189 1.00 72.04  ?  98  LEU   A N    1 
ATOM   566  C  CA   . LEU   A 1 71  ? 24.348  17.540  23.457 1.00 63.20  ?  98  LEU   A CA   1 
ATOM   567  C  C    . LEU   A 1 71  ? 23.751  18.403  22.352 1.00 70.61  ?  98  LEU   A C    1 
ATOM   568  O  O    . LEU   A 1 71  ? 23.406  19.566  22.580 1.00 76.37  ?  98  LEU   A O    1 
ATOM   569  C  CB   . LEU   A 1 71  ? 23.250  17.051  24.400 1.00 59.79  ?  98  LEU   A CB   1 
ATOM   570  C  CG   . LEU   A 1 71  ? 22.298  15.996  23.834 1.00 59.03  ?  98  LEU   A CG   1 
ATOM   571  C  CD1  . LEU   A 1 71  ? 22.982  14.637  23.754 1.00 69.41  ?  98  LEU   A CD1  1 
ATOM   572  C  CD2  . LEU   A 1 71  ? 21.038  15.915  24.677 1.00 56.87  ?  98  LEU   A CD2  1 
ATOM   573  N  N    . ILE   A 1 72  ? 23.638  17.828  21.156 1.00 69.71  ?  99  ILE   A N    1 
ATOM   574  C  CA   . ILE   A 1 72  ? 23.069  18.499  19.994 1.00 66.06  ?  99  ILE   A CA   1 
ATOM   575  C  C    . ILE   A 1 72  ? 22.082  17.546  19.337 1.00 73.08  ?  99  ILE   A C    1 
ATOM   576  O  O    . ILE   A 1 72  ? 22.421  16.388  19.067 1.00 78.90  ?  99  ILE   A O    1 
ATOM   577  C  CB   . ILE   A 1 72  ? 24.156  18.926  18.987 1.00 65.30  ?  99  ILE   A CB   1 
ATOM   578  C  CG1  . ILE   A 1 72  ? 25.128  19.917  19.629 1.00 72.43  ?  99  ILE   A CG1  1 
ATOM   579  C  CG2  . ILE   A 1 72  ? 23.525  19.530  17.741 1.00 73.13  ?  99  ILE   A CG2  1 
ATOM   580  C  CD1  . ILE   A 1 72  ? 26.366  20.180  18.800 1.00 70.24  ?  99  ILE   A CD1  1 
ATOM   581  N  N    . GLY   A 1 73  ? 20.866  18.024  19.080 1.00 68.55  ?  100 GLY   A N    1 
ATOM   582  C  CA   . GLY   A 1 73  ? 19.869  17.168  18.468 1.00 66.34  ?  100 GLY   A CA   1 
ATOM   583  C  C    . GLY   A 1 73  ? 18.545  17.829  18.144 1.00 74.84  ?  100 GLY   A C    1 
ATOM   584  O  O    . GLY   A 1 73  ? 18.484  19.038  17.896 1.00 86.16  ?  100 GLY   A O    1 
ATOM   585  N  N    . ASN   A 1 74  ? 17.481  17.031  18.138 1.00 80.70  ?  101 ASN   A N    1 
ATOM   586  C  CA   . ASN   A 1 74  ? 16.160  17.539  17.805 1.00 75.12  ?  101 ASN   A CA   1 
ATOM   587  C  C    . ASN   A 1 74  ? 15.736  18.608  18.809 1.00 76.13  ?  101 ASN   A C    1 
ATOM   588  O  O    . ASN   A 1 74  ? 16.058  18.507  19.999 1.00 74.46  ?  101 ASN   A O    1 
ATOM   589  C  CB   . ASN   A 1 74  ? 15.134  16.405  17.798 1.00 69.60  ?  101 ASN   A CB   1 
ATOM   590  C  CG   . ASN   A 1 74  ? 15.224  15.542  16.557 1.00 76.18  ?  101 ASN   A CG   1 
ATOM   591  O  OD1  . ASN   A 1 74  ? 15.970  15.847  15.626 1.00 79.45  ?  101 ASN   A OD1  1 
ATOM   592  N  ND2  . ASN   A 1 74  ? 14.460  14.456  16.536 1.00 73.50  ?  101 ASN   A ND2  1 
ATOM   593  N  N    . PRO   A 1 75  ? 15.022  19.642  18.369 1.00 74.89  ?  102 PRO   A N    1 
ATOM   594  C  CA   . PRO   A 1 75  ? 14.513  20.642  19.315 1.00 66.22  ?  102 PRO   A CA   1 
ATOM   595  C  C    . PRO   A 1 75  ? 13.553  20.009  20.311 1.00 61.93  ?  102 PRO   A C    1 
ATOM   596  O  O    . PRO   A 1 75  ? 12.641  19.267  19.938 1.00 70.48  ?  102 PRO   A O    1 
ATOM   597  C  CB   . PRO   A 1 75  ? 13.805  21.656  18.408 1.00 73.40  ?  102 PRO   A CB   1 
ATOM   598  C  CG   . PRO   A 1 75  ? 14.456  21.473  17.069 1.00 70.99  ?  102 PRO   A CG   1 
ATOM   599  C  CD   . PRO   A 1 75  ? 14.703  19.997  16.977 1.00 81.96  ?  102 PRO   A CD   1 
ATOM   600  N  N    . GLY   A 1 76  ? 13.775  20.296  21.592 1.00 68.17  ?  103 GLY   A N    1 
ATOM   601  C  CA   . GLY   A 1 76  ? 12.929  19.789  22.649 1.00 69.07  ?  103 GLY   A CA   1 
ATOM   602  C  C    . GLY   A 1 76  ? 13.281  18.412  23.165 1.00 75.32  ?  103 GLY   A C    1 
ATOM   603  O  O    . GLY   A 1 76  ? 12.643  17.946  24.116 1.00 71.80  ?  103 GLY   A O    1 
ATOM   604  N  N    . CYS   A 1 77  ? 14.270  17.747  22.578 1.00 66.62  ?  104 CYS   A N    1 
ATOM   605  C  CA   . CYS   A 1 77  ? 14.640  16.412  23.018 1.00 62.62  ?  104 CYS   A CA   1 
ATOM   606  C  C    . CYS   A 1 77  ? 15.549  16.484  24.243 1.00 62.01  ?  104 CYS   A C    1 
ATOM   607  O  O    . CYS   A 1 77  ? 16.119  17.529  24.566 1.00 76.02  ?  104 CYS   A O    1 
ATOM   608  C  CB   . CYS   A 1 77  ? 15.334  15.653  21.887 1.00 63.32  ?  104 CYS   A CB   1 
ATOM   609  S  SG   . CYS   A 1 77  ? 15.161  13.862  21.970 1.00 79.01  ?  104 CYS   A SG   1 
ATOM   610  N  N    . THR   A 1 78  ? 15.660  15.356  24.943 1.00 67.14  ?  105 THR   A N    1 
ATOM   611  C  CA   . THR   A 1 78  ? 16.589  15.223  26.057 1.00 59.86  ?  105 THR   A CA   1 
ATOM   612  C  C    . THR   A 1 78  ? 17.214  13.836  26.026 1.00 61.66  ?  105 THR   A C    1 
ATOM   613  O  O    . THR   A 1 78  ? 16.664  12.895  25.448 1.00 63.14  ?  105 THR   A O    1 
ATOM   614  C  CB   . THR   A 1 78  ? 15.918  15.449  27.427 1.00 55.24  ?  105 THR   A CB   1 
ATOM   615  O  OG1  . THR   A 1 78  ? 14.909  14.455  27.644 1.00 48.71  ?  105 THR   A OG1  1 
ATOM   616  C  CG2  . THR   A 1 78  ? 15.303  16.838  27.529 1.00 60.15  ?  105 THR   A CG2  1 
ATOM   617  N  N    . TYR   A 1 79  ? 18.379  13.725  26.660 1.00 65.50  ?  106 TYR   A N    1 
ATOM   618  C  CA   . TYR   A 1 79  ? 19.095  12.463  26.798 1.00 59.44  ?  106 TYR   A CA   1 
ATOM   619  C  C    . TYR   A 1 79  ? 19.593  12.356  28.230 1.00 66.01  ?  106 TYR   A C    1 
ATOM   620  O  O    . TYR   A 1 79  ? 20.289  13.254  28.714 1.00 68.38  ?  106 TYR   A O    1 
ATOM   621  C  CB   . TYR   A 1 79  ? 20.267  12.375  25.814 1.00 58.84  ?  106 TYR   A CB   1 
ATOM   622  C  CG   . TYR   A 1 79  ? 21.102  11.120  25.946 1.00 68.89  ?  106 TYR   A CG   1 
ATOM   623  C  CD1  . TYR   A 1 79  ? 20.584  9.877   25.606 1.00 66.01  ?  106 TYR   A CD1  1 
ATOM   624  C  CD2  . TYR   A 1 79  ? 22.411  11.180  26.408 1.00 62.30  ?  106 TYR   A CD2  1 
ATOM   625  C  CE1  . TYR   A 1 79  ? 21.346  8.729   25.723 1.00 64.99  ?  106 TYR   A CE1  1 
ATOM   626  C  CE2  . TYR   A 1 79  ? 23.179  10.037  26.530 1.00 60.80  ?  106 TYR   A CE2  1 
ATOM   627  C  CZ   . TYR   A 1 79  ? 22.642  8.814   26.186 1.00 66.27  ?  106 TYR   A CZ   1 
ATOM   628  O  OH   . TYR   A 1 79  ? 23.404  7.674   26.305 1.00 66.69  ?  106 TYR   A OH   1 
ATOM   629  N  N    . LYS   A 1 80  ? 19.236  11.268  28.906 1.00 72.65  ?  107 LYS   A N    1 
ATOM   630  C  CA   . LYS   A 1 80  ? 19.531  11.092  30.322 1.00 65.24  ?  107 LYS   A CA   1 
ATOM   631  C  C    . LYS   A 1 80  ? 20.554  9.978   30.498 1.00 59.91  ?  107 LYS   A C    1 
ATOM   632  O  O    . LYS   A 1 80  ? 20.340  8.853   30.034 1.00 71.66  ?  107 LYS   A O    1 
ATOM   633  C  CB   . LYS   A 1 80  ? 18.260  10.777  31.109 1.00 56.61  ?  107 LYS   A CB   1 
ATOM   634  C  CG   . LYS   A 1 80  ? 18.472  10.702  32.611 1.00 53.84  ?  107 LYS   A CG   1 
ATOM   635  C  CD   . LYS   A 1 80  ? 17.159  10.829  33.361 1.00 47.87  ?  107 LYS   A CD   1 
ATOM   636  C  CE   . LYS   A 1 80  ? 17.395  11.118  34.833 1.00 58.85  ?  107 LYS   A CE   1 
ATOM   637  N  NZ   . LYS   A 1 80  ? 16.237  10.700  35.668 1.00 75.71  ?  107 LYS   A NZ   1 
ATOM   638  N  N    . TYR   A 1 81  ? 21.658  10.293  31.172 1.00 70.80  ?  108 TYR   A N    1 
ATOM   639  C  CA   . TYR   A 1 81  ? 22.664  9.305   31.529 1.00 79.11  ?  108 TYR   A CA   1 
ATOM   640  C  C    . TYR   A 1 81  ? 23.248  9.670   32.885 1.00 73.60  ?  108 TYR   A C    1 
ATOM   641  O  O    . TYR   A 1 81  ? 23.531  10.842  33.150 1.00 78.78  ?  108 TYR   A O    1 
ATOM   642  C  CB   . TYR   A 1 81  ? 23.772  9.213   30.467 1.00 75.85  ?  108 TYR   A CB   1 
ATOM   643  C  CG   . TYR   A 1 81  ? 24.804  10.315  30.546 1.00 79.81  ?  108 TYR   A CG   1 
ATOM   644  C  CD1  . TYR   A 1 81  ? 24.574  11.551  29.961 1.00 78.70  ?  108 TYR   A CD1  1 
ATOM   645  C  CD2  . TYR   A 1 81  ? 26.013  10.116  31.203 1.00 91.99  ?  108 TYR   A CD2  1 
ATOM   646  C  CE1  . TYR   A 1 81  ? 25.514  12.560  30.031 1.00 92.08  ?  108 TYR   A CE1  1 
ATOM   647  C  CE2  . TYR   A 1 81  ? 26.958  11.119  31.279 1.00 90.57  ?  108 TYR   A CE2  1 
ATOM   648  C  CZ   . TYR   A 1 81  ? 26.704  12.339  30.690 1.00 98.66  ?  108 TYR   A CZ   1 
ATOM   649  O  OH   . TYR   A 1 81  ? 27.643  13.341  30.763 1.00 106.42 ?  108 TYR   A OH   1 
ATOM   650  N  N    . LEU   A 1 82  ? 23.411  8.660   33.740 1.00 65.85  ?  109 LEU   A N    1 
ATOM   651  C  CA   . LEU   A 1 82  ? 23.966  8.831   35.084 1.00 62.57  ?  109 LEU   A CA   1 
ATOM   652  C  C    . LEU   A 1 82  ? 23.208  9.902   35.867 1.00 65.10  ?  109 LEU   A C    1 
ATOM   653  O  O    . LEU   A 1 82  ? 23.795  10.810  36.461 1.00 78.95  ?  109 LEU   A O    1 
ATOM   654  C  CB   . LEU   A 1 82  ? 25.461  9.149   35.024 1.00 67.24  ?  109 LEU   A CB   1 
ATOM   655  C  CG   . LEU   A 1 82  ? 26.342  8.091   34.355 1.00 86.04  ?  109 LEU   A CG   1 
ATOM   656  C  CD1  . LEU   A 1 82  ? 27.797  8.531   34.343 1.00 79.07  ?  109 LEU   A CD1  1 
ATOM   657  C  CD2  . LEU   A 1 82  ? 26.188  6.742   35.044 1.00 73.49  ?  109 LEU   A CD2  1 
ATOM   658  N  N    . ASN   A 1 83  ? 21.877  9.789   35.852 1.00 65.94  ?  110 ASN   A N    1 
ATOM   659  C  CA   . ASN   A 1 83  ? 20.983  10.662  36.615 1.00 65.19  ?  110 ASN   A CA   1 
ATOM   660  C  C    . ASN   A 1 83  ? 21.147  12.133  36.242 1.00 61.99  ?  110 ASN   A C    1 
ATOM   661  O  O    . ASN   A 1 83  ? 20.865  13.022  37.049 1.00 84.21  ?  110 ASN   A O    1 
ATOM   662  C  CB   . ASN   A 1 83  ? 21.176  10.478  38.124 1.00 71.36  ?  110 ASN   A CB   1 
ATOM   663  C  CG   . ASN   A 1 83  ? 21.029  9.034   38.558 1.00 96.37  ?  110 ASN   A CG   1 
ATOM   664  O  OD1  . ASN   A 1 83  ? 22.017  8.317   38.714 1.00 101.43 ?  110 ASN   A OD1  1 
ATOM   665  N  ND2  . ASN   A 1 83  ? 19.789  8.601   38.757 1.00 105.73 ?  110 ASN   A ND2  1 
ATOM   666  N  N    . THR   A 1 84  ? 21.599  12.410  35.021 1.00 60.70  ?  111 THR   A N    1 
ATOM   667  C  CA   . THR   A 1 84  ? 21.775  13.778  34.549 1.00 58.81  ?  111 THR   A CA   1 
ATOM   668  C  C    . THR   A 1 84  ? 21.098  13.917  33.196 1.00 67.60  ?  111 THR   A C    1 
ATOM   669  O  O    . THR   A 1 84  ? 21.518  13.284  32.221 1.00 67.78  ?  111 THR   A O    1 
ATOM   670  C  CB   . THR   A 1 84  ? 23.258  14.148  34.448 1.00 67.67  ?  111 THR   A CB   1 
ATOM   671  O  OG1  . THR   A 1 84  ? 23.896  13.921  35.711 1.00 69.90  ?  111 THR   A OG1  1 
ATOM   672  C  CG2  . THR   A 1 84  ? 23.413  15.612  34.066 1.00 57.87  ?  111 THR   A CG2  1 
ATOM   673  N  N    . ARG   A 1 85  ? 20.052  14.735  33.138 1.00 54.46  ?  112 ARG   A N    1 
ATOM   674  C  CA   . ARG   A 1 85  ? 19.326  14.977  31.899 1.00 63.96  ?  112 ARG   A CA   1 
ATOM   675  C  C    . ARG   A 1 85  ? 20.021  16.087  31.122 1.00 55.82  ?  112 ARG   A C    1 
ATOM   676  O  O    . ARG   A 1 85  ? 20.228  17.185  31.650 1.00 69.40  ?  112 ARG   A O    1 
ATOM   677  C  CB   . ARG   A 1 85  ? 17.871  15.349  32.182 1.00 55.72  ?  112 ARG   A CB   1 
ATOM   678  C  CG   . ARG   A 1 85  ? 16.993  15.383  30.943 1.00 55.56  ?  112 ARG   A CG   1 
ATOM   679  C  CD   . ARG   A 1 85  ? 15.553  15.712  31.296 1.00 53.19  ?  112 ARG   A CD   1 
ATOM   680  N  NE   . ARG   A 1 85  ? 14.921  14.631  32.042 1.00 64.16  ?  112 ARG   A NE   1 
ATOM   681  C  CZ   . ARG   A 1 85  ? 14.444  13.521  31.496 1.00 61.55  ?  112 ARG   A CZ   1 
ATOM   682  N  NH1  . ARG   A 1 85  ? 14.487  13.319  30.189 1.00 51.87  ?  112 ARG   A NH1  1 
ATOM   683  N  NH2  . ARG   A 1 85  ? 13.909  12.589  32.281 1.00 52.26  ?  112 ARG   A NH2  1 
ATOM   684  N  N    . LEU   A 1 86  ? 20.385  15.799  29.878 1.00 64.63  ?  113 LEU   A N    1 
ATOM   685  C  CA   . LEU   A 1 86  ? 21.003  16.779  28.998 1.00 61.29  ?  113 LEU   A CA   1 
ATOM   686  C  C    . LEU   A 1 86  ? 19.971  17.303  28.010 1.00 61.41  ?  113 LEU   A C    1 
ATOM   687  O  O    . LEU   A 1 86  ? 19.164  16.538  27.474 1.00 63.58  ?  113 LEU   A O    1 
ATOM   688  C  CB   . LEU   A 1 86  ? 22.196  16.179  28.250 1.00 63.21  ?  113 LEU   A CB   1 
ATOM   689  C  CG   . LEU   A 1 86  ? 23.574  16.304  28.910 1.00 77.92  ?  113 LEU   A CG   1 
ATOM   690  C  CD1  . LEU   A 1 86  ? 23.541  15.926  30.386 1.00 80.93  ?  113 LEU   A CD1  1 
ATOM   691  C  CD2  . LEU   A 1 86  ? 24.597  15.463  28.170 1.00 69.98  ?  113 LEU   A CD2  1 
ATOM   692  N  N    . PHE   A 1 87  ? 20.001  18.610  27.776 1.00 59.93  ?  114 PHE   A N    1 
ATOM   693  C  CA   . PHE   A 1 87  ? 19.046  19.283  26.909 1.00 61.54  ?  114 PHE   A CA   1 
ATOM   694  C  C    . PHE   A 1 87  ? 19.738  19.671  25.611 1.00 68.25  ?  114 PHE   A C    1 
ATOM   695  O  O    . PHE   A 1 87  ? 20.827  20.253  25.634 1.00 73.90  ?  114 PHE   A O    1 
ATOM   696  C  CB   . PHE   A 1 87  ? 18.460  20.511  27.609 1.00 66.35  ?  114 PHE   A CB   1 
ATOM   697  C  CG   . PHE   A 1 87  ? 17.767  20.190  28.905 1.00 67.11  ?  114 PHE   A CG   1 
ATOM   698  C  CD1  . PHE   A 1 87  ? 18.474  20.167  30.097 1.00 67.04  ?  114 PHE   A CD1  1 
ATOM   699  C  CD2  . PHE   A 1 87  ? 16.415  19.892  28.929 1.00 61.63  ?  114 PHE   A CD2  1 
ATOM   700  C  CE1  . PHE   A 1 87  ? 17.842  19.862  31.289 1.00 63.90  ?  114 PHE   A CE1  1 
ATOM   701  C  CE2  . PHE   A 1 87  ? 15.776  19.588  30.118 1.00 59.98  ?  114 PHE   A CE2  1 
ATOM   702  C  CZ   . PHE   A 1 87  ? 16.491  19.574  31.300 1.00 65.52  ?  114 PHE   A CZ   1 
ATOM   703  N  N    . THR   A 1 88  ? 19.107  19.347  24.485 1.00 70.77  ?  115 THR   A N    1 
ATOM   704  C  CA   . THR   A 1 88  ? 19.752  19.522  23.190 1.00 68.81  ?  115 THR   A CA   1 
ATOM   705  C  C    . THR   A 1 88  ? 19.865  20.989  22.804 1.00 74.73  ?  115 THR   A C    1 
ATOM   706  O  O    . THR   A 1 88  ? 18.909  21.759  22.934 1.00 83.40  ?  115 THR   A O    1 
ATOM   707  C  CB   . THR   A 1 88  ? 18.988  18.769  22.097 1.00 76.78  ?  115 THR   A CB   1 
ATOM   708  O  OG1  . THR   A 1 88  ? 17.911  19.587  21.611 1.00 68.38  ?  115 THR   A OG1  1 
ATOM   709  C  CG2  . THR   A 1 88  ? 18.462  17.441  22.603 1.00 76.90  ?  115 THR   A CG2  1 
ATOM   710  N  N    . VAL   A 1 89  ? 21.046  21.367  22.329 1.00 73.80  ?  116 VAL   A N    1 
ATOM   711  C  CA   . VAL   A 1 89  ? 21.205  22.563  21.511 1.00 82.85  ?  116 VAL   A CA   1 
ATOM   712  C  C    . VAL   A 1 89  ? 20.609  22.203  20.156 1.00 84.11  ?  116 VAL   A C    1 
ATOM   713  O  O    . VAL   A 1 89  ? 21.069  21.246  19.516 1.00 88.06  ?  116 VAL   A O    1 
ATOM   714  C  CB   . VAL   A 1 89  ? 22.677  22.989  21.403 1.00 76.71  ?  116 VAL   A CB   1 
ATOM   715  C  CG1  . VAL   A 1 89  ? 22.801  24.273  20.598 1.00 85.70  ?  116 VAL   A CG1  1 
ATOM   716  C  CG2  . VAL   A 1 89  ? 23.285  23.152  22.788 1.00 76.95  ?  116 VAL   A CG2  1 
ATOM   717  N  N    . PRO   A 1 90  ? 19.590  22.917  19.684 1.00 83.74  ?  117 PRO   A N    1 
ATOM   718  C  CA   . PRO   A 1 90  ? 18.827  22.427  18.530 1.00 82.18  ?  117 PRO   A CA   1 
ATOM   719  C  C    . PRO   A 1 90  ? 19.602  22.554  17.229 1.00 83.80  ?  117 PRO   A C    1 
ATOM   720  O  O    . PRO   A 1 90  ? 20.353  23.510  17.019 1.00 89.01  ?  117 PRO   A O    1 
ATOM   721  C  CB   . PRO   A 1 90  ? 17.583  23.321  18.526 1.00 81.77  ?  117 PRO   A CB   1 
ATOM   722  C  CG   . PRO   A 1 90  ? 18.036  24.592  19.164 1.00 80.15  ?  117 PRO   A CG   1 
ATOM   723  C  CD   . PRO   A 1 90  ? 19.129  24.240  20.142 1.00 79.69  ?  117 PRO   A CD   1 
ATOM   724  N  N    . TRP   A 1 91  ? 19.414  21.563  16.348 1.00 84.23  ?  118 TRP   A N    1 
ATOM   725  C  CA   . TRP   A 1 91  ? 19.923  21.659  14.991 1.00 95.01  ?  118 TRP   A CA   1 
ATOM   726  C  C    . TRP   A 1 91  ? 18.769  21.867  14.011 1.00 97.95  ?  118 TRP   A C    1 
ATOM   727  O  O    . TRP   A 1 91  ? 17.642  21.433  14.270 1.00 97.26  ?  118 TRP   A O    1 
ATOM   728  C  CB   . TRP   A 1 91  ? 20.743  20.421  14.590 1.00 89.88  ?  118 TRP   A CB   1 
ATOM   729  C  CG   . TRP   A 1 91  ? 20.087  19.077  14.790 1.00 79.86  ?  118 TRP   A CG   1 
ATOM   730  C  CD1  . TRP   A 1 91  ? 18.751  18.807  14.862 1.00 79.95  ?  118 TRP   A CD1  1 
ATOM   731  C  CD2  . TRP   A 1 91  ? 20.757  17.819  14.936 1.00 75.98  ?  118 TRP   A CD2  1 
ATOM   732  N  NE1  . TRP   A 1 91  ? 18.549  17.460  15.043 1.00 85.22  ?  118 TRP   A NE1  1 
ATOM   733  C  CE2  . TRP   A 1 91  ? 19.765  16.831  15.092 1.00 77.73  ?  118 TRP   A CE2  1 
ATOM   734  C  CE3  . TRP   A 1 91  ? 22.101  17.433  14.951 1.00 80.97  ?  118 TRP   A CE3  1 
ATOM   735  C  CZ2  . TRP   A 1 91  ? 20.074  15.483  15.264 1.00 79.27  ?  118 TRP   A CZ2  1 
ATOM   736  C  CZ3  . TRP   A 1 91  ? 22.406  16.094  15.119 1.00 77.69  ?  118 TRP   A CZ3  1 
ATOM   737  C  CH2  . TRP   A 1 91  ? 21.397  15.136  15.274 1.00 81.63  ?  118 TRP   A CH2  1 
ATOM   738  N  N    . PRO   A 1 92  ? 19.008  22.551  12.890 1.00 108.37 ?  119 PRO   A N    1 
ATOM   739  C  CA   . PRO   A 1 92  ? 17.891  22.963  12.028 1.00 114.07 ?  119 PRO   A CA   1 
ATOM   740  C  C    . PRO   A 1 92  ? 17.191  21.821  11.308 1.00 116.93 ?  119 PRO   A C    1 
ATOM   741  O  O    . PRO   A 1 92  ? 17.576  21.449  10.194 1.00 128.09 ?  119 PRO   A O    1 
ATOM   742  C  CB   . PRO   A 1 92  ? 18.561  23.915  11.025 1.00 113.12 ?  119 PRO   A CB   1 
ATOM   743  C  CG   . PRO   A 1 92  ? 19.825  24.351  11.704 1.00 111.47 ?  119 PRO   A CG   1 
ATOM   744  C  CD   . PRO   A 1 92  ? 20.281  23.129  12.431 1.00 112.24 ?  119 PRO   A CD   1 
ATOM   745  N  N    . VAL   A 1 93  ? 16.162  21.264  11.930 1.00 120.36 ?  120 VAL   A N    1 
ATOM   746  C  CA   . VAL   A 1 93  ? 15.212  20.404  11.235 1.00 130.52 ?  120 VAL   A CA   1 
ATOM   747  C  C    . VAL   A 1 93  ? 14.076  21.286  10.737 1.00 132.35 ?  120 VAL   A C    1 
ATOM   748  O  O    . VAL   A 1 93  ? 13.717  22.278  11.384 1.00 128.54 ?  120 VAL   A O    1 
ATOM   749  C  CB   . VAL   A 1 93  ? 14.706  19.273  12.154 1.00 133.01 ?  120 VAL   A CB   1 
ATOM   750  C  CG1  . VAL   A 1 93  ? 13.934  19.836  13.340 1.00 124.93 ?  120 VAL   A CG1  1 
ATOM   751  C  CG2  . VAL   A 1 93  ? 13.858  18.277  11.370 1.00 139.76 ?  120 VAL   A CG2  1 
ATOM   752  N  N    . LYS   A 1 94  ? 13.528  20.945  9.571  1.00 131.78 ?  121 LYS   A N    1 
ATOM   753  C  CA   . LYS   A 1 94  ? 12.545  21.803  8.920  1.00 136.48 ?  121 LYS   A CA   1 
ATOM   754  C  C    . LYS   A 1 94  ? 11.357  22.074  9.835  1.00 146.17 ?  121 LYS   A C    1 
ATOM   755  O  O    . LYS   A 1 94  ? 10.844  21.172  10.503 1.00 139.86 ?  121 LYS   A O    1 
ATOM   756  C  CB   . LYS   A 1 94  ? 12.068  21.163  7.616  1.00 125.53 ?  121 LYS   A CB   1 
ATOM   757  N  N    . GLY   A 1 95  ? 10.928  23.332  9.869  1.00 130.38 ?  122 GLY   A N    1 
ATOM   758  C  CA   . GLY   A 1 95  ? 9.816   23.740  10.706 1.00 130.32 ?  122 GLY   A CA   1 
ATOM   759  C  C    . GLY   A 1 95  ? 10.157  23.771  12.183 1.00 125.08 ?  122 GLY   A C    1 
ATOM   760  O  O    . GLY   A 1 95  ? 11.288  24.074  12.564 1.00 124.21 ?  122 GLY   A O    1 
ATOM   761  N  N    . GLU   A 1 102 ? 26.370  33.556  18.302 1.00 126.08 ?  129 GLU   A N    1 
ATOM   762  C  CA   . GLU   A 1 102 ? 25.379  32.490  18.235 1.00 127.45 ?  129 GLU   A CA   1 
ATOM   763  C  C    . GLU   A 1 102 ? 25.160  32.060  16.787 1.00 134.29 ?  129 GLU   A C    1 
ATOM   764  O  O    . GLU   A 1 102 ? 24.454  31.088  16.516 1.00 142.28 ?  129 GLU   A O    1 
ATOM   765  C  CB   . GLU   A 1 102 ? 24.061  32.942  18.869 1.00 123.47 ?  129 GLU   A CB   1 
ATOM   766  C  CG   . GLU   A 1 102 ? 23.298  31.839  19.590 1.00 125.18 ?  129 GLU   A CG   1 
ATOM   767  C  CD   . GLU   A 1 102 ? 22.071  31.376  18.828 1.00 129.19 ?  129 GLU   A CD   1 
ATOM   768  O  OE1  . GLU   A 1 102 ? 21.845  31.870  17.703 1.00 124.26 ?  129 GLU   A OE1  1 
ATOM   769  O  OE2  . GLU   A 1 102 ? 21.331  30.520  19.356 1.00 122.78 ?  129 GLU   A OE2  1 
ATOM   770  N  N    . ALA   A 1 103 ? 25.774  32.795  15.858 1.00 129.19 ?  130 ALA   A N    1 
ATOM   771  C  CA   . ALA   A 1 103 ? 25.707  32.464  14.439 1.00 120.60 ?  130 ALA   A CA   1 
ATOM   772  C  C    . ALA   A 1 103 ? 26.771  31.450  14.038 1.00 125.50 ?  130 ALA   A C    1 
ATOM   773  O  O    . ALA   A 1 103 ? 26.497  30.552  13.235 1.00 125.99 ?  130 ALA   A O    1 
ATOM   774  C  CB   . ALA   A 1 103 ? 25.846  33.731  13.593 1.00 113.39 ?  130 ALA   A CB   1 
ATOM   775  N  N    . GLU   A 1 104 ? 27.986  31.586  14.576 1.00 124.49 ?  131 GLU   A N    1 
ATOM   776  C  CA   . GLU   A 1 104 ? 28.995  30.550  14.389 1.00 112.46 ?  131 GLU   A CA   1 
ATOM   777  C  C    . GLU   A 1 104 ? 28.575  29.249  15.057 1.00 117.74 ?  131 GLU   A C    1 
ATOM   778  O  O    . GLU   A 1 104 ? 28.916  28.162  14.576 1.00 112.78 ?  131 GLU   A O    1 
ATOM   779  C  CB   . GLU   A 1 104 ? 30.339  31.018  14.950 1.00 112.32 ?  131 GLU   A CB   1 
ATOM   780  C  CG   . GLU   A 1 104 ? 31.203  31.790  13.971 1.00 122.51 ?  131 GLU   A CG   1 
ATOM   781  C  CD   . GLU   A 1 104 ? 32.474  32.313  14.613 1.00 126.29 ?  131 GLU   A CD   1 
ATOM   782  O  OE1  . GLU   A 1 104 ? 33.128  31.546  15.351 1.00 112.50 ?  131 GLU   A OE1  1 
ATOM   783  O  OE2  . GLU   A 1 104 ? 32.816  33.493  14.384 1.00 131.96 ?  131 GLU   A OE2  1 
ATOM   784  N  N    . ILE   A 1 105 ? 27.833  29.342  16.162 1.00 117.93 ?  132 ILE   A N    1 
ATOM   785  C  CA   . ILE   A 1 105 ? 27.386  28.150  16.873 1.00 101.45 ?  132 ILE   A CA   1 
ATOM   786  C  C    . ILE   A 1 105 ? 26.280  27.450  16.103 1.00 109.24 ?  132 ILE   A C    1 
ATOM   787  O  O    . ILE   A 1 105 ? 26.277  26.219  15.977 1.00 106.28 ?  132 ILE   A O    1 
ATOM   788  C  CB   . ILE   A 1 105 ? 26.929  28.520  18.293 1.00 105.90 ?  132 ILE   A CB   1 
ATOM   789  C  CG1  . ILE   A 1 105 ? 28.014  29.340  18.988 1.00 113.22 ?  132 ILE   A CG1  1 
ATOM   790  C  CG2  . ILE   A 1 105 ? 26.558  27.267  19.081 1.00 96.28  ?  132 ILE   A CG2  1 
ATOM   791  C  CD1  . ILE   A 1 105 ? 28.991  28.507  19.752 1.00 98.90  ?  132 ILE   A CD1  1 
ATOM   792  N  N    . ALA   A 1 106 ? 25.310  28.216  15.599 1.00 113.26 ?  133 ALA   A N    1 
ATOM   793  C  CA   . ALA   A 1 106 ? 24.277  27.628  14.757 1.00 104.79 ?  133 ALA   A CA   1 
ATOM   794  C  C    . ALA   A 1 106 ? 24.899  26.856  13.603 1.00 95.59  ?  133 ALA   A C    1 
ATOM   795  O  O    . ALA   A 1 106 ? 24.531  25.704  13.352 1.00 104.78 ?  133 ALA   A O    1 
ATOM   796  C  CB   . ALA   A 1 106 ? 23.334  28.714  14.238 1.00 111.02 ?  133 ALA   A CB   1 
ATOM   797  N  N    . ALA   A 1 107 ? 25.884  27.460  12.929 1.00 106.68 ?  134 ALA   A N    1 
ATOM   798  C  CA   . ALA   A 1 107 ? 26.542  26.812  11.798 1.00 114.74 ?  134 ALA   A CA   1 
ATOM   799  C  C    . ALA   A 1 107 ? 27.174  25.482  12.186 1.00 108.70 ?  134 ALA   A C    1 
ATOM   800  O  O    . ALA   A 1 107 ? 27.193  24.546  11.376 1.00 108.68 ?  134 ALA   A O    1 
ATOM   801  C  CB   . ALA   A 1 107 ? 27.597  27.746  11.204 1.00 107.15 ?  134 ALA   A CB   1 
ATOM   802  N  N    . ALA   A 1 108 ? 27.702  25.377  13.407 1.00 104.31 ?  135 ALA   A N    1 
ATOM   803  C  CA   . ALA   A 1 108 ? 28.248  24.102  13.859 1.00 102.22 ?  135 ALA   A CA   1 
ATOM   804  C  C    . ALA   A 1 108 ? 27.150  23.056  14.001 1.00 105.94 ?  135 ALA   A C    1 
ATOM   805  O  O    . ALA   A 1 108 ? 27.348  21.889  13.644 1.00 98.12  ?  135 ALA   A O    1 
ATOM   806  C  CB   . ALA   A 1 108 ? 28.994  24.287  15.181 1.00 98.38  ?  135 ALA   A CB   1 
ATOM   807  N  N    . CYS   A 1 109 ? 25.981  23.457  14.507 1.00 105.32 ?  136 CYS   A N    1 
ATOM   808  C  CA   . CYS   A 1 109 ? 24.875  22.515  14.643 1.00 100.36 ?  136 CYS   A CA   1 
ATOM   809  C  C    . CYS   A 1 109 ? 24.374  22.044  13.281 1.00 104.40 ?  136 CYS   A C    1 
ATOM   810  O  O    . CYS   A 1 109 ? 24.020  20.870  13.118 1.00 96.80  ?  136 CYS   A O    1 
ATOM   811  C  CB   . CYS   A 1 109 ? 23.742  23.147  15.451 1.00 95.36  ?  136 CYS   A CB   1 
ATOM   812  S  SG   . CYS   A 1 109 ? 24.197  23.602  17.143 1.00 85.61  ?  136 CYS   A SG   1 
ATOM   813  N  N    . GLU   A 1 110 ? 24.330  22.943  12.292 1.00 96.58  ?  137 GLU   A N    1 
ATOM   814  C  CA   . GLU   A 1 110 ? 23.995  22.515  10.935 1.00 98.78  ?  137 GLU   A CA   1 
ATOM   815  C  C    . GLU   A 1 110 ? 24.996  21.486  10.430 1.00 96.36  ?  137 GLU   A C    1 
ATOM   816  O  O    . GLU   A 1 110 ? 24.618  20.513  9.768  1.00 95.44  ?  137 GLU   A O    1 
ATOM   817  C  CB   . GLU   A 1 110 ? 23.942  23.714  9.982  1.00 106.48 ?  137 GLU   A CB   1 
ATOM   818  C  CG   . GLU   A 1 110 ? 23.659  25.046  10.651 1.00 128.33 ?  137 GLU   A CG   1 
ATOM   819  C  CD   . GLU   A 1 110 ? 23.430  26.185  9.672  1.00 144.16 ?  137 GLU   A CD   1 
ATOM   820  O  OE1  . GLU   A 1 110 ? 22.378  26.200  9.002  1.00 144.07 ?  137 GLU   A OE1  1 
ATOM   821  O  OE2  . GLU   A 1 110 ? 24.301  27.078  9.578  1.00 141.32 ?  137 GLU   A OE2  1 
ATOM   822  N  N    . THR   A 1 111 ? 26.280  21.685  10.738 1.00 95.35  ?  138 THR   A N    1 
ATOM   823  C  CA   . THR   A 1 111 ? 27.306  20.738  10.315 1.00 96.53  ?  138 THR   A CA   1 
ATOM   824  C  C    . THR   A 1 111 ? 27.033  19.347  10.873 1.00 95.40  ?  138 THR   A C    1 
ATOM   825  O  O    . THR   A 1 111 ? 27.094  18.350  10.144 1.00 94.88  ?  138 THR   A O    1 
ATOM   826  C  CB   . THR   A 1 111 ? 28.688  21.230  10.751 1.00 97.02  ?  138 THR   A CB   1 
ATOM   827  O  OG1  . THR   A 1 111 ? 29.002  22.453  10.073 1.00 107.23 ?  138 THR   A OG1  1 
ATOM   828  C  CG2  . THR   A 1 111 ? 29.750  20.187  10.438 1.00 95.88  ?  138 THR   A CG2  1 
ATOM   829  N  N    . PHE   A 1 112 ? 26.715  19.261  12.165 1.00 84.70  ?  139 PHE   A N    1 
ATOM   830  C  CA   . PHE   A 1 112 ? 26.471  17.962  12.778 1.00 85.88  ?  139 PHE   A CA   1 
ATOM   831  C  C    . PHE   A 1 112 ? 25.117  17.383  12.406 1.00 89.80  ?  139 PHE   A C    1 
ATOM   832  O  O    . PHE   A 1 112 ? 24.915  16.173  12.553 1.00 90.40  ?  139 PHE   A O    1 
ATOM   833  C  CB   . PHE   A 1 112 ? 26.607  18.064  14.295 1.00 75.09  ?  139 PHE   A CB   1 
ATOM   834  C  CG   . PHE   A 1 112 ? 28.015  18.274  14.741 1.00 73.48  ?  139 PHE   A CG   1 
ATOM   835  C  CD1  . PHE   A 1 112 ? 28.924  17.233  14.706 1.00 77.52  ?  139 PHE   A CD1  1 
ATOM   836  C  CD2  . PHE   A 1 112 ? 28.442  19.517  15.168 1.00 86.05  ?  139 PHE   A CD2  1 
ATOM   837  C  CE1  . PHE   A 1 112 ? 30.227  17.425  15.099 1.00 77.51  ?  139 PHE   A CE1  1 
ATOM   838  C  CE2  . PHE   A 1 112 ? 29.745  19.717  15.564 1.00 88.38  ?  139 PHE   A CE2  1 
ATOM   839  C  CZ   . PHE   A 1 112 ? 30.638  18.671  15.528 1.00 85.03  ?  139 PHE   A CZ   1 
ATOM   840  N  N    . LEU   A 1 113 ? 24.186  18.213  11.936 1.00 87.87  ?  140 LEU   A N    1 
ATOM   841  C  CA   . LEU   A 1 113 ? 22.998  17.672  11.289 1.00 85.41  ?  140 LEU   A CA   1 
ATOM   842  C  C    . LEU   A 1 113 ? 23.368  17.020  9.964  1.00 84.44  ?  140 LEU   A C    1 
ATOM   843  O  O    . LEU   A 1 113 ? 22.840  15.958  9.615  1.00 83.73  ?  140 LEU   A O    1 
ATOM   844  C  CB   . LEU   A 1 113 ? 21.960  18.780  11.088 1.00 89.87  ?  140 LEU   A CB   1 
ATOM   845  C  CG   . LEU   A 1 113 ? 20.529  18.413  10.669 1.00 87.89  ?  140 LEU   A CG   1 
ATOM   846  C  CD1  . LEU   A 1 113 ? 20.390  18.227  9.160  1.00 95.87  ?  140 LEU   A CD1  1 
ATOM   847  C  CD2  . LEU   A 1 113 ? 20.058  17.170  11.411 1.00 77.30  ?  140 LEU   A CD2  1 
ATOM   848  N  N    . LYS   A 1 114 ? 24.289  17.640  9.220  1.00 88.37  ?  141 LYS   A N    1 
ATOM   849  C  CA   . LYS   A 1 114 ? 24.755  17.061  7.965  1.00 98.11  ?  141 LYS   A CA   1 
ATOM   850  C  C    . LYS   A 1 114 ? 25.496  15.751  8.204  1.00 91.82  ?  141 LYS   A C    1 
ATOM   851  O  O    . LYS   A 1 114 ? 25.319  14.785  7.453  1.00 90.96  ?  141 LYS   A O    1 
ATOM   852  C  CB   . LYS   A 1 114 ? 25.650  18.061  7.232  1.00 94.01  ?  141 LYS   A CB   1 
ATOM   853  C  CG   . LYS   A 1 114 ? 25.911  17.727  5.773  1.00 102.81 ?  141 LYS   A CG   1 
ATOM   854  C  CD   . LYS   A 1 114 ? 26.851  18.743  5.144  1.00 101.51 ?  141 LYS   A CD   1 
ATOM   855  C  CE   . LYS   A 1 114 ? 26.279  19.299  3.851  1.00 106.30 ?  141 LYS   A CE   1 
ATOM   856  N  NZ   . LYS   A 1 114 ? 27.336  19.879  2.977  1.00 110.95 ?  141 LYS   A NZ   1 
ATOM   857  N  N    . LEU   A 1 115 ? 26.334  15.702  9.243  1.00 90.28  ?  142 LEU   A N    1 
ATOM   858  C  CA   . LEU   A 1 115 ? 26.984  14.447  9.604  1.00 80.18  ?  142 LEU   A CA   1 
ATOM   859  C  C    . LEU   A 1 115 ? 25.960  13.412  10.049 1.00 80.98  ?  142 LEU   A C    1 
ATOM   860  O  O    . LEU   A 1 115 ? 26.119  12.215  9.783  1.00 81.78  ?  142 LEU   A O    1 
ATOM   861  C  CB   . LEU   A 1 115 ? 28.021  14.690  10.702 1.00 78.40  ?  142 LEU   A CB   1 
ATOM   862  C  CG   . LEU   A 1 115 ? 28.774  13.468  11.236 1.00 81.89  ?  142 LEU   A CG   1 
ATOM   863  C  CD1  . LEU   A 1 115 ? 29.833  13.013  10.246 1.00 70.80  ?  142 LEU   A CD1  1 
ATOM   864  C  CD2  . LEU   A 1 115 ? 29.402  13.774  12.587 1.00 67.47  ?  142 LEU   A CD2  1 
ATOM   865  N  N    . ASN   A 1 116 ? 24.895  13.858  10.720 1.00 84.49  ?  143 ASN   A N    1 
ATOM   866  C  CA   . ASN   A 1 116 ? 23.852  12.937  11.161 1.00 84.85  ?  143 ASN   A CA   1 
ATOM   867  C  C    . ASN   A 1 116 ? 23.174  12.258  9.979  1.00 91.08  ?  143 ASN   A C    1 
ATOM   868  O  O    . ASN   A 1 116 ? 22.870  11.061  10.033 1.00 89.56  ?  143 ASN   A O    1 
ATOM   869  C  CB   . ASN   A 1 116 ? 22.823  13.677  12.013 1.00 81.59  ?  143 ASN   A CB   1 
ATOM   870  C  CG   . ASN   A 1 116 ? 21.965  12.738  12.835 1.00 82.92  ?  143 ASN   A CG   1 
ATOM   871  O  OD1  . ASN   A 1 116 ? 22.418  12.179  13.833 1.00 89.56  ?  143 ASN   A OD1  1 
ATOM   872  N  ND2  . ASN   A 1 116 ? 20.717  12.559  12.418 1.00 86.98  ?  143 ASN   A ND2  1 
ATOM   873  N  N    . ASP   A 1 117 ? 22.924  13.007  8.903  1.00 94.58  ?  144 ASP   A N    1 
ATOM   874  C  CA   . ASP   A 1 117 ? 22.316  12.405  7.720  1.00 95.39  ?  144 ASP   A CA   1 
ATOM   875  C  C    . ASP   A 1 117 ? 23.241  11.370  7.093  1.00 100.64 ?  144 ASP   A C    1 
ATOM   876  O  O    . ASP   A 1 117 ? 22.794  10.283  6.712  1.00 96.89  ?  144 ASP   A O    1 
ATOM   877  C  CB   . ASP   A 1 117 ? 21.947  13.486  6.703  1.00 105.14 ?  144 ASP   A CB   1 
ATOM   878  C  CG   . ASP   A 1 117 ? 20.995  14.523  7.271  1.00 115.18 ?  144 ASP   A CG   1 
ATOM   879  O  OD1  . ASP   A 1 117 ? 19.914  14.133  7.760  1.00 113.30 ?  144 ASP   A OD1  1 
ATOM   880  O  OD2  . ASP   A 1 117 ? 21.323  15.726  7.218  1.00 116.82 ?  144 ASP   A OD2  1 
ATOM   881  N  N    . TYR   A 1 118 ? 24.536  11.681  6.993  1.00 92.58  ?  145 TYR   A N    1 
ATOM   882  C  CA   . TYR   A 1 118 ? 25.479  10.746  6.385  1.00 83.39  ?  145 TYR   A CA   1 
ATOM   883  C  C    . TYR   A 1 118 ? 25.559  9.449   7.183  1.00 85.45  ?  145 TYR   A C    1 
ATOM   884  O  O    . TYR   A 1 118 ? 25.418  8.355   6.624  1.00 90.77  ?  145 TYR   A O    1 
ATOM   885  C  CB   . TYR   A 1 118 ? 26.859  11.401  6.255  1.00 84.68  ?  145 TYR   A CB   1 
ATOM   886  C  CG   . TYR   A 1 118 ? 27.927  10.528  5.615  1.00 81.82  ?  145 TYR   A CG   1 
ATOM   887  C  CD1  . TYR   A 1 118 ? 28.544  9.503   6.323  1.00 84.89  ?  145 TYR   A CD1  1 
ATOM   888  C  CD2  . TYR   A 1 118 ? 28.352  10.767  4.314  1.00 90.68  ?  145 TYR   A CD2  1 
ATOM   889  C  CE1  . TYR   A 1 118 ? 29.523  8.719   5.743  1.00 92.23  ?  145 TYR   A CE1  1 
ATOM   890  C  CE2  . TYR   A 1 118 ? 29.329  9.985   3.725  1.00 93.10  ?  145 TYR   A CE2  1 
ATOM   891  C  CZ   . TYR   A 1 118 ? 29.911  8.964   4.445  1.00 97.44  ?  145 TYR   A CZ   1 
ATOM   892  O  OH   . TYR   A 1 118 ? 30.887  8.185   3.866  1.00 106.89 ?  145 TYR   A OH   1 
ATOM   893  N  N    . LEU   A 1 119 ? 25.792  9.552   8.494  1.00 82.61  ?  146 LEU   A N    1 
ATOM   894  C  CA   . LEU   A 1 119 ? 25.891  8.352   9.320  1.00 81.79  ?  146 LEU   A CA   1 
ATOM   895  C  C    . LEU   A 1 119 ? 24.590  7.562   9.321  1.00 86.56  ?  146 LEU   A C    1 
ATOM   896  O  O    . LEU   A 1 119 ? 24.608  6.338   9.497  1.00 77.88  ?  146 LEU   A O    1 
ATOM   897  C  CB   . LEU   A 1 119 ? 26.291  8.722   10.749 1.00 72.19  ?  146 LEU   A CB   1 
ATOM   898  C  CG   . LEU   A 1 119 ? 27.536  9.594   10.923 1.00 74.44  ?  146 LEU   A CG   1 
ATOM   899  C  CD1  . LEU   A 1 119 ? 27.950  9.654   12.384 1.00 60.93  ?  146 LEU   A CD1  1 
ATOM   900  C  CD2  . LEU   A 1 119 ? 28.678  9.074   10.065 1.00 79.89  ?  146 LEU   A CD2  1 
ATOM   901  N  N    . GLN   A 1 120 ? 23.458  8.238   9.124  1.00 83.26  ?  147 GLN   A N    1 
ATOM   902  C  CA   . GLN   A 1 120 ? 22.183  7.536   9.037  1.00 85.36  ?  147 GLN   A CA   1 
ATOM   903  C  C    . GLN   A 1 120 ? 22.134  6.634   7.810  1.00 89.44  ?  147 GLN   A C    1 
ATOM   904  O  O    . GLN   A 1 120 ? 21.761  5.459   7.907  1.00 86.84  ?  147 GLN   A O    1 
ATOM   905  C  CB   . GLN   A 1 120 ? 21.029  8.541   9.022  1.00 89.21  ?  147 GLN   A CB   1 
ATOM   906  C  CG   . GLN   A 1 120 ? 19.809  8.059   9.782  1.00 95.80  ?  147 GLN   A CG   1 
ATOM   907  C  CD   . GLN   A 1 120 ? 18.670  9.058   9.791  1.00 106.22 ?  147 GLN   A CD   1 
ATOM   908  O  OE1  . GLN   A 1 120 ? 18.889  10.269  9.816  1.00 110.82 ?  147 GLN   A OE1  1 
ATOM   909  N  NE2  . GLN   A 1 120 ? 17.442  8.552   9.786  1.00 103.71 ?  147 GLN   A NE2  1 
ATOM   910  N  N    . ILE   A 1 121 ? 22.518  7.164   6.645  1.00 91.66  ?  148 ILE   A N    1 
ATOM   911  C  CA   . ILE   A 1 121 ? 22.514  6.356   5.427  1.00 88.60  ?  148 ILE   A CA   1 
ATOM   912  C  C    . ILE   A 1 121 ? 23.520  5.216   5.536  1.00 90.00  ?  148 ILE   A C    1 
ATOM   913  O  O    . ILE   A 1 121 ? 23.276  4.106   5.048  1.00 91.31  ?  148 ILE   A O    1 
ATOM   914  C  CB   . ILE   A 1 121 ? 22.790  7.231   4.188  1.00 98.32  ?  148 ILE   A CB   1 
ATOM   915  C  CG1  . ILE   A 1 121 ? 22.111  8.597   4.309  1.00 93.69  ?  148 ILE   A CG1  1 
ATOM   916  C  CG2  . ILE   A 1 121 ? 22.330  6.524   2.926  1.00 93.62  ?  148 ILE   A CG2  1 
ATOM   917  C  CD1  . ILE   A 1 121 ? 20.603  8.538   4.458  1.00 100.67 ?  148 ILE   A CD1  1 
ATOM   918  N  N    . GLU   A 1 122 ? 24.665  5.471   6.174  1.00 90.57  ?  149 GLU   A N    1 
ATOM   919  C  CA   . GLU   A 1 122 ? 25.654  4.415   6.361  1.00 87.84  ?  149 GLU   A CA   1 
ATOM   920  C  C    . GLU   A 1 122 ? 25.123  3.320   7.279  1.00 86.17  ?  149 GLU   A C    1 
ATOM   921  O  O    . GLU   A 1 122 ? 25.356  2.130   7.036  1.00 91.14  ?  149 GLU   A O    1 
ATOM   922  C  CB   . GLU   A 1 122 ? 26.948  5.000   6.924  1.00 86.86  ?  149 GLU   A CB   1 
ATOM   923  C  CG   . GLU   A 1 122 ? 27.774  5.784   5.917  1.00 92.02  ?  149 GLU   A CG   1 
ATOM   924  C  CD   . GLU   A 1 122 ? 28.735  4.911   5.133  1.00 114.72 ?  149 GLU   A CD   1 
ATOM   925  O  OE1  . GLU   A 1 122 ? 28.269  3.999   4.421  1.00 118.91 ?  149 GLU   A OE1  1 
ATOM   926  O  OE2  . GLU   A 1 122 ? 29.961  5.135   5.232  1.00 117.60 ?  149 GLU   A OE2  1 
ATOM   927  N  N    . THR   A 1 123 ? 24.406  3.705   8.338  1.00 86.28  ?  150 THR   A N    1 
ATOM   928  C  CA   . THR   A 1 123 ? 23.874  2.718   9.273  1.00 84.53  ?  150 THR   A CA   1 
ATOM   929  C  C    . THR   A 1 123 ? 22.827  1.833   8.608  1.00 85.75  ?  150 THR   A C    1 
ATOM   930  O  O    . THR   A 1 123 ? 22.818  0.613   8.814  1.00 92.49  ?  150 THR   A O    1 
ATOM   931  C  CB   . THR   A 1 123 ? 23.282  3.420   10.496 1.00 83.97  ?  150 THR   A CB   1 
ATOM   932  O  OG1  . THR   A 1 123 ? 24.285  4.231   11.118 1.00 75.62  ?  150 THR   A OG1  1 
ATOM   933  C  CG2  . THR   A 1 123 ? 22.772  2.400   11.499 1.00 70.96  ?  150 THR   A CG2  1 
ATOM   934  N  N    . ILE   A 1 124 ? 21.941  2.428   7.805  1.00 87.67  ?  151 ILE   A N    1 
ATOM   935  C  CA   . ILE   A 1 124 ? 20.901  1.651   7.137  1.00 88.20  ?  151 ILE   A CA   1 
ATOM   936  C  C    . ILE   A 1 124 ? 21.519  0.635   6.184  1.00 94.32  ?  151 ILE   A C    1 
ATOM   937  O  O    . ILE   A 1 124 ? 21.065  -0.513  6.098  1.00 93.23  ?  151 ILE   A O    1 
ATOM   938  C  CB   . ILE   A 1 124 ? 19.915  2.587   6.412  1.00 90.68  ?  151 ILE   A CB   1 
ATOM   939  C  CG1  . ILE   A 1 124 ? 19.159  3.457   7.419  1.00 89.79  ?  151 ILE   A CG1  1 
ATOM   940  C  CG2  . ILE   A 1 124 ? 18.943  1.791   5.555  1.00 88.80  ?  151 ILE   A CG2  1 
ATOM   941  C  CD1  . ILE   A 1 124 ? 18.804  4.834   6.896  1.00 84.08  ?  151 ILE   A CD1  1 
ATOM   942  N  N    . GLN   A 1 125 ? 22.568  1.035   5.462  1.00 94.03  ?  152 GLN   A N    1 
ATOM   943  C  CA   . GLN   A 1 125 ? 23.211  0.113   4.532  1.00 98.95  ?  152 GLN   A CA   1 
ATOM   944  C  C    . GLN   A 1 125 ? 23.903  -1.025  5.274  1.00 102.80 ?  152 GLN   A C    1 
ATOM   945  O  O    . GLN   A 1 125 ? 23.818  -2.187  4.858  1.00 110.87 ?  152 GLN   A O    1 
ATOM   946  C  CB   . GLN   A 1 125 ? 24.206  0.866   3.647  1.00 105.94 ?  152 GLN   A CB   1 
ATOM   947  C  CG   . GLN   A 1 125 ? 25.449  0.068   3.284  1.00 116.42 ?  152 GLN   A CG   1 
ATOM   948  C  CD   . GLN   A 1 125 ? 26.520  0.915   2.626  1.00 131.61 ?  152 GLN   A CD   1 
ATOM   949  O  OE1  . GLN   A 1 125 ? 27.197  1.702   3.287  1.00 130.44 ?  152 GLN   A OE1  1 
ATOM   950  N  NE2  . GLN   A 1 125 ? 26.681  0.756   1.318  1.00 133.18 ?  152 GLN   A NE2  1 
ATOM   951  N  N    . ALA   A 1 126 ? 24.584  -0.713  6.380  1.00 108.36 ?  153 ALA   A N    1 
ATOM   952  C  CA   . ALA   A 1 126 ? 25.257  -1.755  7.148  1.00 91.22  ?  153 ALA   A CA   1 
ATOM   953  C  C    . ALA   A 1 126 ? 24.262  -2.692  7.819  1.00 91.65  ?  153 ALA   A C    1 
ATOM   954  O  O    . ALA   A 1 126 ? 24.564  -3.874  8.018  1.00 95.49  ?  153 ALA   A O    1 
ATOM   955  C  CB   . ALA   A 1 126 ? 26.182  -1.128  8.190  1.00 81.41  ?  153 ALA   A CB   1 
ATOM   956  N  N    . LEU   A 1 127 ? 23.078  -2.190  8.175  1.00 91.44  ?  154 LEU   A N    1 
ATOM   957  C  CA   . LEU   A 1 127 ? 22.045  -3.054  8.734  1.00 93.57  ?  154 LEU   A CA   1 
ATOM   958  C  C    . LEU   A 1 127 ? 21.376  -3.901  7.661  1.00 105.37 ?  154 LEU   A C    1 
ATOM   959  O  O    . LEU   A 1 127 ? 20.874  -4.990  7.961  1.00 99.48  ?  154 LEU   A O    1 
ATOM   960  C  CB   . LEU   A 1 127 ? 20.998  -2.221  9.474  1.00 91.47  ?  154 LEU   A CB   1 
ATOM   961  C  CG   . LEU   A 1 127 ? 21.370  -1.738  10.877 1.00 84.95  ?  154 LEU   A CG   1 
ATOM   962  C  CD1  . LEU   A 1 127 ? 20.521  -0.540  11.275 1.00 82.24  ?  154 LEU   A CD1  1 
ATOM   963  C  CD2  . LEU   A 1 127 ? 21.225  -2.864  11.889 1.00 82.15  ?  154 LEU   A CD2  1 
ATOM   964  N  N    . GLU   A 1 128 ? 21.353  -3.421  6.415  1.00 103.81 ?  155 GLU   A N    1 
ATOM   965  C  CA   . GLU   A 1 128 ? 20.806  -4.223  5.326  1.00 106.94 ?  155 GLU   A CA   1 
ATOM   966  C  C    . GLU   A 1 128 ? 21.758  -5.350  4.946  1.00 112.34 ?  155 GLU   A C    1 
ATOM   967  O  O    . GLU   A 1 128 ? 21.319  -6.464  4.636  1.00 118.57 ?  155 GLU   A O    1 
ATOM   968  C  CB   . GLU   A 1 128 ? 20.509  -3.338  4.117  1.00 105.11 ?  155 GLU   A CB   1 
ATOM   969  C  CG   . GLU   A 1 128 ? 19.060  -2.886  4.018  1.00 110.10 ?  155 GLU   A CG   1 
ATOM   970  C  CD   . GLU   A 1 128 ? 18.908  -1.573  3.274  1.00 108.81 ?  155 GLU   A CD   1 
ATOM   971  O  OE1  . GLU   A 1 128 ? 19.921  -1.065  2.748  1.00 113.85 ?  155 GLU   A OE1  1 
ATOM   972  O  OE2  . GLU   A 1 128 ? 17.775  -1.050  3.215  1.00 103.29 ?  155 GLU   A OE2  1 
ATOM   973  N  N    . GLU   A 1 129 ? 23.066  -5.079  4.963  1.00 112.04 ?  156 GLU   A N    1 
ATOM   974  C  CA   . GLU   A 1 129 ? 24.043  -6.125  4.684  1.00 115.41 ?  156 GLU   A CA   1 
ATOM   975  C  C    . GLU   A 1 129 ? 24.060  -7.183  5.780  1.00 120.78 ?  156 GLU   A C    1 
ATOM   976  O  O    . GLU   A 1 129 ? 24.370  -8.348  5.509  1.00 131.74 ?  156 GLU   A O    1 
ATOM   977  C  CB   . GLU   A 1 129 ? 25.435  -5.514  4.520  1.00 112.15 ?  156 GLU   A CB   1 
ATOM   978  C  CG   . GLU   A 1 129 ? 25.602  -4.654  3.277  1.00 120.95 ?  156 GLU   A CG   1 
ATOM   979  C  CD   . GLU   A 1 129 ? 26.757  -3.677  3.394  1.00 119.43 ?  156 GLU   A CD   1 
ATOM   980  O  OE1  . GLU   A 1 129 ? 27.513  -3.766  4.384  1.00 113.99 ?  156 GLU   A OE1  1 
ATOM   981  O  OE2  . GLU   A 1 129 ? 26.910  -2.822  2.496  1.00 124.19 ?  156 GLU   A OE2  1 
ATOM   982  N  N    . LEU   A 1 130 ? 23.728  -6.799  7.015  1.00 118.53 ?  157 LEU   A N    1 
ATOM   983  C  CA   . LEU   A 1 130 ? 23.749  -7.755  8.118  1.00 114.11 ?  157 LEU   A CA   1 
ATOM   984  C  C    . LEU   A 1 130 ? 22.582  -8.731  8.028  1.00 124.87 ?  157 LEU   A C    1 
ATOM   985  O  O    . LEU   A 1 130 ? 22.752  -9.933  8.267  1.00 131.87 ?  157 LEU   A O    1 
ATOM   986  C  CB   . LEU   A 1 130 ? 23.730  -7.011  9.453  1.00 109.09 ?  157 LEU   A CB   1 
ATOM   987  C  CG   . LEU   A 1 130 ? 23.503  -7.853  10.710 1.00 112.32 ?  157 LEU   A CG   1 
ATOM   988  C  CD1  . LEU   A 1 130 ? 24.770  -8.603  11.091 1.00 109.17 ?  157 LEU   A CD1  1 
ATOM   989  C  CD2  . LEU   A 1 130 ? 23.027  -6.979  11.860 1.00 99.26  ?  157 LEU   A CD2  1 
ATOM   990  N  N    . ALA   A 1 131 ? 21.389  -8.235  7.687  1.00 118.18 ?  158 ALA   A N    1 
ATOM   991  C  CA   . ALA   A 1 131 ? 20.231  -9.114  7.574  1.00 122.74 ?  158 ALA   A CA   1 
ATOM   992  C  C    . ALA   A 1 131 ? 20.359  -10.069 6.394  1.00 136.85 ?  158 ALA   A C    1 
ATOM   993  O  O    . ALA   A 1 131 ? 19.869  -11.202 6.460  1.00 139.57 ?  158 ALA   A O    1 
ATOM   994  C  CB   . ALA   A 1 131 ? 18.951  -8.288  7.452  1.00 112.65 ?  158 ALA   A CB   1 
ATOM   995  N  N    . ALA   A 1 132 ? 21.010  -9.634  5.312  1.00 137.60 ?  159 ALA   A N    1 
ATOM   996  C  CA   . ALA   A 1 132 ? 21.212  -10.519 4.169  1.00 133.70 ?  159 ALA   A CA   1 
ATOM   997  C  C    . ALA   A 1 132 ? 22.229  -11.607 4.489  1.00 139.96 ?  159 ALA   A C    1 
ATOM   998  O  O    . ALA   A 1 132 ? 22.082  -12.751 4.044  1.00 146.92 ?  159 ALA   A O    1 
ATOM   999  C  CB   . ALA   A 1 132 ? 21.652  -9.710  2.949  1.00 128.88 ?  159 ALA   A CB   1 
ATOM   1000 N  N    . LYS   A 1 133 ? 23.267  -11.268 5.257  1.00 134.52 ?  160 LYS   A N    1 
ATOM   1001 C  CA   . LYS   A 1 133 ? 24.248  -12.270 5.660  1.00 133.03 ?  160 LYS   A CA   1 
ATOM   1002 C  C    . LYS   A 1 133 ? 23.645  -13.289 6.618  1.00 143.29 ?  160 LYS   A C    1 
ATOM   1003 O  O    . LYS   A 1 133 ? 24.048  -14.458 6.612  1.00 147.58 ?  160 LYS   A O    1 
ATOM   1004 C  CB   . LYS   A 1 133 ? 25.458  -11.591 6.301  1.00 119.89 ?  160 LYS   A CB   1 
ATOM   1005 C  CG   . LYS   A 1 133 ? 26.649  -12.511 6.514  1.00 118.99 ?  160 LYS   A CG   1 
ATOM   1006 C  CD   . LYS   A 1 133 ? 27.567  -11.979 7.603  1.00 110.27 ?  160 LYS   A CD   1 
ATOM   1007 C  CE   . LYS   A 1 133 ? 27.001  -12.260 8.985  1.00 113.09 ?  160 LYS   A CE   1 
ATOM   1008 N  NZ   . LYS   A 1 133 ? 27.905  -11.776 10.065 1.00 106.03 ?  160 LYS   A NZ   1 
ATOM   1009 N  N    . GLU   A 1 134 ? 22.683  -12.870 7.441  1.00 146.76 ?  161 GLU   A N    1 
ATOM   1010 C  CA   . GLU   A 1 134 ? 22.050  -13.776 8.389  1.00 145.12 ?  161 GLU   A CA   1 
ATOM   1011 C  C    . GLU   A 1 134 ? 20.928  -14.592 7.762  1.00 143.90 ?  161 GLU   A C    1 
ATOM   1012 O  O    . GLU   A 1 134 ? 20.596  -15.663 8.281  1.00 146.86 ?  161 GLU   A O    1 
ATOM   1013 C  CB   . GLU   A 1 134 ? 21.512  -12.987 9.585  1.00 144.07 ?  161 GLU   A CB   1 
ATOM   1014 C  CG   . GLU   A 1 134 ? 22.581  -12.603 10.597 1.00 146.98 ?  161 GLU   A CG   1 
ATOM   1015 C  CD   . GLU   A 1 134 ? 22.011  -11.905 11.817 1.00 146.23 ?  161 GLU   A CD   1 
ATOM   1016 O  OE1  . GLU   A 1 134 ? 20.896  -11.353 11.720 1.00 150.85 ?  161 GLU   A OE1  1 
ATOM   1017 O  OE2  . GLU   A 1 134 ? 22.681  -11.906 12.871 1.00 139.51 ?  161 GLU   A OE2  1 
ATOM   1018 N  N    . LYS   A 1 135 ? 20.341  -14.115 6.663  1.00 145.66 ?  162 LYS   A N    1 
ATOM   1019 C  CA   . LYS   A 1 135 ? 19.302  -14.885 5.986  1.00 148.39 ?  162 LYS   A CA   1 
ATOM   1020 C  C    . LYS   A 1 135 ? 19.897  -16.092 5.270  1.00 149.51 ?  162 LYS   A C    1 
ATOM   1021 O  O    . LYS   A 1 135 ? 19.393  -17.214 5.397  1.00 150.39 ?  162 LYS   A O    1 
ATOM   1022 C  CB   . LYS   A 1 135 ? 18.542  -13.993 5.005  1.00 139.37 ?  162 LYS   A CB   1 
ATOM   1023 N  N    . ALA   A 1 136 ? 20.970  -15.881 4.515  1.00 141.56 ?  163 ALA   A N    1 
ATOM   1024 C  CA   . ALA   A 1 136 ? 21.641  -16.969 3.815  1.00 143.71 ?  163 ALA   A CA   1 
ATOM   1025 C  C    . ALA   A 1 136 ? 22.934  -17.353 4.528  1.00 137.02 ?  163 ALA   A C    1 
ATOM   1026 O  O    . ALA   A 1 136 ? 22.908  -17.977 5.589  1.00 130.82 ?  163 ALA   A O    1 
ATOM   1027 C  CB   . ALA   A 1 136 ? 21.924  -16.579 2.372  1.00 151.30 ?  163 ALA   A CB   1 
ATOM   1028 N  N    . GLN   A 1 161 ? 7.720   -3.975  7.178  1.00 145.77 ?  188 GLN   A N    1 
ATOM   1029 C  CA   . GLN   A 1 161 ? 7.811   -5.052  8.156  1.00 150.48 ?  188 GLN   A CA   1 
ATOM   1030 C  C    . GLN   A 1 161 ? 9.098   -4.939  8.967  1.00 156.82 ?  188 GLN   A C    1 
ATOM   1031 O  O    . GLN   A 1 161 ? 9.065   -4.627  10.158 1.00 151.34 ?  188 GLN   A O    1 
ATOM   1032 C  CB   . GLN   A 1 161 ? 7.736   -6.412  7.461  1.00 143.71 ?  188 GLN   A CB   1 
ATOM   1033 C  CG   . GLN   A 1 161 ? 6.493   -6.594  6.606  1.00 147.54 ?  188 GLN   A CG   1 
ATOM   1034 C  CD   . GLN   A 1 161 ? 6.687   -7.616  5.504  1.00 164.91 ?  188 GLN   A CD   1 
ATOM   1035 O  OE1  . GLN   A 1 161 ? 7.584   -8.456  5.571  1.00 172.08 ?  188 GLN   A OE1  1 
ATOM   1036 N  NE2  . GLN   A 1 161 ? 5.845   -7.547  4.479  1.00 159.64 ?  188 GLN   A NE2  1 
ATOM   1037 N  N    . ASP   A 1 162 ? 10.234  -5.196  8.316  1.00 154.75 ?  189 ASP   A N    1 
ATOM   1038 C  CA   . ASP   A 1 162 ? 11.535  -5.047  8.950  1.00 161.11 ?  189 ASP   A CA   1 
ATOM   1039 C  C    . ASP   A 1 162 ? 12.343  -3.874  8.417  1.00 158.67 ?  189 ASP   A C    1 
ATOM   1040 O  O    . ASP   A 1 162 ? 13.259  -3.416  9.108  1.00 144.90 ?  189 ASP   A O    1 
ATOM   1041 C  CB   . ASP   A 1 162 ? 12.358  -6.335  8.800  1.00 172.77 ?  189 ASP   A CB   1 
ATOM   1042 C  CG   . ASP   A 1 162 ? 12.010  -7.370  9.852  1.00 183.04 ?  189 ASP   A CG   1 
ATOM   1043 O  OD1  . ASP   A 1 162 ? 11.621  -6.973  10.971 1.00 187.84 ?  189 ASP   A OD1  1 
ATOM   1044 O  OD2  . ASP   A 1 162 ? 12.124  -8.580  9.562  1.00 173.75 ?  189 ASP   A OD2  1 
ATOM   1045 N  N    . GLU   A 1 163 ? 12.035  -3.380  7.215  1.00 154.53 ?  190 GLU   A N    1 
ATOM   1046 C  CA   . GLU   A 1 163 ? 12.598  -2.108  6.780  1.00 137.61 ?  190 GLU   A CA   1 
ATOM   1047 C  C    . GLU   A 1 163 ? 12.108  -0.958  7.648  1.00 128.35 ?  190 GLU   A C    1 
ATOM   1048 O  O    . GLU   A 1 163 ? 12.746  0.100   7.681  1.00 117.57 ?  190 GLU   A O    1 
ATOM   1049 C  CB   . GLU   A 1 163 ? 12.251  -1.848  5.313  1.00 128.99 ?  190 GLU   A CB   1 
ATOM   1050 N  N    . VAL   A 1 164 ? 10.986  -1.146  8.345  1.00 132.25 ?  191 VAL   A N    1 
ATOM   1051 C  CA   . VAL   A 1 164 ? 10.532  -0.163  9.322  1.00 124.41 ?  191 VAL   A CA   1 
ATOM   1052 C  C    . VAL   A 1 164 ? 11.421  -0.201  10.560 1.00 122.60 ?  191 VAL   A C    1 
ATOM   1053 O  O    . VAL   A 1 164 ? 11.841  0.841   11.076 1.00 119.30 ?  191 VAL   A O    1 
ATOM   1054 C  CB   . VAL   A 1 164 ? 9.055   -0.410  9.679  1.00 121.42 ?  191 VAL   A CB   1 
ATOM   1055 C  CG1  . VAL   A 1 164 ? 8.674   0.348   10.943 1.00 102.42 ?  191 VAL   A CG1  1 
ATOM   1056 C  CG2  . VAL   A 1 164 ? 8.154   -0.019  8.517  1.00 105.39 ?  191 VAL   A CG2  1 
ATOM   1057 N  N    . ASP   A 1 165 ? 11.722  -1.407  11.051 1.00 127.81 ?  192 ASP   A N    1 
ATOM   1058 C  CA   . ASP   A 1 165 ? 12.584  -1.537  12.222 1.00 117.76 ?  192 ASP   A CA   1 
ATOM   1059 C  C    . ASP   A 1 165 ? 13.991  -1.031  11.932 1.00 107.03 ?  192 ASP   A C    1 
ATOM   1060 O  O    . ASP   A 1 165 ? 14.627  -0.413  12.794 1.00 104.98 ?  192 ASP   A O    1 
ATOM   1061 C  CB   . ASP   A 1 165 ? 12.626  -2.994  12.686 1.00 122.75 ?  192 ASP   A CB   1 
ATOM   1062 C  CG   . ASP   A 1 165 ? 11.316  -3.450  13.296 1.00 135.78 ?  192 ASP   A CG   1 
ATOM   1063 O  OD1  . ASP   A 1 165 ? 10.280  -2.801  13.042 1.00 151.67 ?  192 ASP   A OD1  1 
ATOM   1064 O  OD2  . ASP   A 1 165 ? 11.324  -4.460  14.032 1.00 135.14 ?  192 ASP   A OD2  1 
ATOM   1065 N  N    . ILE   A 1 166 ? 14.495  -1.283  10.723 1.00 114.28 ?  193 ILE   A N    1 
ATOM   1066 C  CA   . ILE   A 1 166 ? 15.830  -0.815  10.365 1.00 104.09 ?  193 ILE   A CA   1 
ATOM   1067 C  C    . ILE   A 1 166 ? 15.864  0.707   10.297 1.00 101.37 ?  193 ILE   A C    1 
ATOM   1068 O  O    . ILE   A 1 166 ? 16.828  1.342   10.744 1.00 103.69 ?  193 ILE   A O    1 
ATOM   1069 C  CB   . ILE   A 1 166 ? 16.280  -1.458  9.039  1.00 106.32 ?  193 ILE   A CB   1 
ATOM   1070 C  CG1  . ILE   A 1 166 ? 16.641  -2.930  9.258  1.00 103.14 ?  193 ILE   A CG1  1 
ATOM   1071 C  CG2  . ILE   A 1 166 ? 17.457  -0.702  8.440  1.00 99.00  ?  193 ILE   A CG2  1 
ATOM   1072 C  CD1  . ILE   A 1 166 ? 17.306  -3.584  8.065  1.00 109.50 ?  193 ILE   A CD1  1 
ATOM   1073 N  N    . LYS   A 1 167 ? 14.808  1.318   9.755  1.00 102.13 ?  194 LYS   A N    1 
ATOM   1074 C  CA   . LYS   A 1 167 ? 14.765  2.774   9.659  1.00 90.30  ?  194 LYS   A CA   1 
ATOM   1075 C  C    . LYS   A 1 167 ? 14.673  3.420   11.036 1.00 87.08  ?  194 LYS   A C    1 
ATOM   1076 O  O    . LYS   A 1 167 ? 15.258  4.485   11.268 1.00 87.86  ?  194 LYS   A O    1 
ATOM   1077 C  CB   . LYS   A 1 167 ? 13.590  3.208   8.783  1.00 98.45  ?  194 LYS   A CB   1 
ATOM   1078 N  N    . SER   A 1 168 ? 13.947  2.792   11.963 1.00 86.04  ?  195 SER   A N    1 
ATOM   1079 C  CA   . SER   A 1 168 ? 13.790  3.375   13.292 1.00 75.77  ?  195 SER   A CA   1 
ATOM   1080 C  C    . SER   A 1 168 ? 15.053  3.206   14.127 1.00 78.48  ?  195 SER   A C    1 
ATOM   1081 O  O    . SER   A 1 168 ? 15.440  4.119   14.866 1.00 78.98  ?  195 SER   A O    1 
ATOM   1082 C  CB   . SER   A 1 168 ? 12.590  2.752   14.004 1.00 80.65  ?  195 SER   A CB   1 
ATOM   1083 O  OG   . SER   A 1 168 ? 12.547  1.351   13.803 1.00 95.08  ?  195 SER   A OG   1 
ATOM   1084 N  N    . ARG   A 1 169 ? 15.709  2.048   14.025 1.00 84.64  ?  196 ARG   A N    1 
ATOM   1085 C  CA   . ARG   A 1 169 ? 16.942  1.814   14.768 1.00 80.82  ?  196 ARG   A CA   1 
ATOM   1086 C  C    . ARG   A 1 169 ? 18.118  2.618   14.235 1.00 82.38  ?  196 ARG   A C    1 
ATOM   1087 O  O    . ARG   A 1 169 ? 19.195  2.582   14.841 1.00 73.06  ?  196 ARG   A O    1 
ATOM   1088 C  CB   . ARG   A 1 169 ? 17.291  0.324   14.762 1.00 80.67  ?  196 ARG   A CB   1 
ATOM   1089 C  CG   . ARG   A 1 169 ? 16.339  -0.536  15.577 1.00 75.00  ?  196 ARG   A CG   1 
ATOM   1090 C  CD   . ARG   A 1 169 ? 16.349  -1.978  15.101 1.00 73.70  ?  196 ARG   A CD   1 
ATOM   1091 N  NE   . ARG   A 1 169 ? 15.377  -2.795  15.817 1.00 82.32  ?  196 ARG   A NE   1 
ATOM   1092 C  CZ   . ARG   A 1 169 ? 15.327  -4.119  15.764 1.00 92.51  ?  196 ARG   A CZ   1 
ATOM   1093 N  NH1  . ARG   A 1 169 ? 16.189  -4.816  15.041 1.00 94.26  ?  196 ARG   A NH1  1 
ATOM   1094 N  NH2  . ARG   A 1 169 ? 14.390  -4.761  16.456 1.00 85.33  ?  196 ARG   A NH2  1 
ATOM   1095 N  N    . ALA   A 1 170 ? 17.946  3.334   13.124 1.00 73.96  ?  197 ALA   A N    1 
ATOM   1096 C  CA   . ALA   A 1 170 ? 18.977  4.213   12.602 1.00 73.25  ?  197 ALA   A CA   1 
ATOM   1097 C  C    . ALA   A 1 170 ? 18.597  5.686   12.644 1.00 84.37  ?  197 ALA   A C    1 
ATOM   1098 O  O    . ALA   A 1 170 ? 19.463  6.533   12.402 1.00 86.46  ?  197 ALA   A O    1 
ATOM   1099 C  CB   . ALA   A 1 170 ? 19.332  3.829   11.157 1.00 73.56  ?  197 ALA   A CB   1 
ATOM   1100 N  N    . ALA   A 1 171 ? 17.344  6.017   12.959 1.00 84.70  ?  198 ALA   A N    1 
ATOM   1101 C  CA   . ALA   A 1 171 ? 16.875  7.404   12.964 1.00 82.90  ?  198 ALA   A CA   1 
ATOM   1102 C  C    . ALA   A 1 171 ? 17.433  8.118   14.192 1.00 85.94  ?  198 ALA   A C    1 
ATOM   1103 O  O    . ALA   A 1 171 ? 16.751  8.334   15.198 1.00 80.39  ?  198 ALA   A O    1 
ATOM   1104 C  CB   . ALA   A 1 171 ? 15.353  7.456   12.928 1.00 81.49  ?  198 ALA   A CB   1 
ATOM   1105 N  N    . TYR   A 1 172 ? 18.707  8.495   14.098 1.00 80.35  ?  199 TYR   A N    1 
ATOM   1106 C  CA   . TYR   A 1 172 ? 19.356  9.229   15.177 1.00 69.71  ?  199 TYR   A CA   1 
ATOM   1107 C  C    . TYR   A 1 172 ? 18.674  10.575  15.386 1.00 72.54  ?  199 TYR   A C    1 
ATOM   1108 O  O    . TYR   A 1 172 ? 18.439  11.321  14.431 1.00 67.92  ?  199 TYR   A O    1 
ATOM   1109 C  CB   . TYR   A 1 172 ? 20.838  9.438   14.860 1.00 63.97  ?  199 TYR   A CB   1 
ATOM   1110 C  CG   . TYR   A 1 172 ? 21.606  8.172   14.551 1.00 66.10  ?  199 TYR   A CG   1 
ATOM   1111 C  CD1  . TYR   A 1 172 ? 21.576  7.087   15.415 1.00 72.37  ?  199 TYR   A CD1  1 
ATOM   1112 C  CD2  . TYR   A 1 172 ? 22.367  8.066   13.394 1.00 80.37  ?  199 TYR   A CD2  1 
ATOM   1113 C  CE1  . TYR   A 1 172 ? 22.280  5.929   15.135 1.00 75.25  ?  199 TYR   A CE1  1 
ATOM   1114 C  CE2  . TYR   A 1 172 ? 23.074  6.914   13.104 1.00 73.72  ?  199 TYR   A CE2  1 
ATOM   1115 C  CZ   . TYR   A 1 172 ? 23.027  5.849   13.978 1.00 69.33  ?  199 TYR   A CZ   1 
ATOM   1116 O  OH   . TYR   A 1 172 ? 23.729  4.701   13.693 1.00 68.67  ?  199 TYR   A OH   1 
ATOM   1117 N  N    . ASN   A 1 173 ? 18.354  10.887  16.645 1.00 71.77  ?  200 ASN   A N    1 
ATOM   1118 C  CA   . ASN   A 1 173 ? 17.738  12.162  16.981 1.00 67.70  ?  200 ASN   A CA   1 
ATOM   1119 C  C    . ASN   A 1 173 ? 18.663  13.113  17.724 1.00 68.22  ?  200 ASN   A C    1 
ATOM   1120 O  O    . ASN   A 1 173 ? 18.388  14.317  17.749 1.00 71.92  ?  200 ASN   A O    1 
ATOM   1121 C  CB   . ASN   A 1 173 ? 16.469  11.945  17.821 1.00 66.17  ?  200 ASN   A CB   1 
ATOM   1122 C  CG   . ASN   A 1 173 ? 16.690  11.003  18.989 1.00 64.74  ?  200 ASN   A CG   1 
ATOM   1123 O  OD1  . ASN   A 1 173 ? 17.798  10.883  19.510 1.00 75.37  ?  200 ASN   A OD1  1 
ATOM   1124 N  ND2  . ASN   A 1 173 ? 15.625  10.332  19.412 1.00 70.78  ?  200 ASN   A ND2  1 
ATOM   1125 N  N    . VAL   A 1 174 ? 19.740  12.612  18.335 1.00 67.60  ?  201 VAL   A N    1 
ATOM   1126 C  CA   . VAL   A 1 174 ? 20.691  13.444  19.061 1.00 64.85  ?  201 VAL   A CA   1 
ATOM   1127 C  C    . VAL   A 1 174 ? 22.103  12.945  18.785 1.00 68.20  ?  201 VAL   A C    1 
ATOM   1128 O  O    . VAL   A 1 174 ? 22.314  11.822  18.324 1.00 62.97  ?  201 VAL   A O    1 
ATOM   1129 C  CB   . VAL   A 1 174 ? 20.438  13.450  20.589 1.00 71.91  ?  201 VAL   A CB   1 
ATOM   1130 C  CG1  . VAL   A 1 174 ? 19.045  13.974  20.916 1.00 55.38  ?  201 VAL   A CG1  1 
ATOM   1131 C  CG2  . VAL   A 1 174 ? 20.649  12.057  21.170 1.00 60.93  ?  201 VAL   A CG2  1 
ATOM   1132 N  N    . THR   A 1 175 ? 23.075  13.807  19.073 1.00 65.37  ?  202 THR   A N    1 
ATOM   1133 C  CA   . THR   A 1 175 ? 24.477  13.421  19.113 1.00 63.74  ?  202 THR   A CA   1 
ATOM   1134 C  C    . THR   A 1 175 ? 25.120  14.071  20.328 1.00 70.36  ?  202 THR   A C    1 
ATOM   1135 O  O    . THR   A 1 175 ? 24.842  15.231  20.644 1.00 66.15  ?  202 THR   A O    1 
ATOM   1136 C  CB   . THR   A 1 175 ? 25.228  13.810  17.827 1.00 71.51  ?  202 THR   A CB   1 
ATOM   1137 O  OG1  . THR   A 1 175 ? 26.595  13.388  17.923 1.00 77.01  ?  202 THR   A OG1  1 
ATOM   1138 C  CG2  . THR   A 1 175 ? 25.173  15.313  17.582 1.00 68.78  ?  202 THR   A CG2  1 
ATOM   1139 N  N    . LEU   A 1 176 ? 25.957  13.308  21.024 1.00 67.65  ?  203 LEU   A N    1 
ATOM   1140 C  CA   . LEU   A 1 176 ? 26.618  13.767  22.239 1.00 60.78  ?  203 LEU   A CA   1 
ATOM   1141 C  C    . LEU   A 1 176 ? 28.101  13.935  21.937 1.00 64.09  ?  203 LEU   A C    1 
ATOM   1142 O  O    . LEU   A 1 176 ? 28.825  12.947  21.777 1.00 80.61  ?  203 LEU   A O    1 
ATOM   1143 C  CB   . LEU   A 1 176 ? 26.385  12.789  23.389 1.00 61.72  ?  203 LEU   A CB   1 
ATOM   1144 C  CG   . LEU   A 1 176 ? 27.063  13.128  24.715 1.00 69.39  ?  203 LEU   A CG   1 
ATOM   1145 C  CD1  . LEU   A 1 176 ? 26.429  14.363  25.318 1.00 70.78  ?  203 LEU   A CD1  1 
ATOM   1146 C  CD2  . LEU   A 1 176 ? 26.963  11.958  25.679 1.00 69.18  ?  203 LEU   A CD2  1 
ATOM   1147 N  N    . LEU   A 1 177 ? 28.546  15.185  21.854 1.00 78.11  ?  204 LEU   A N    1 
ATOM   1148 C  CA   . LEU   A 1 177 ? 29.933  15.480  21.529 1.00 71.51  ?  204 LEU   A CA   1 
ATOM   1149 C  C    . LEU   A 1 177 ? 30.799  15.374  22.775 1.00 75.12  ?  204 LEU   A C    1 
ATOM   1150 O  O    . LEU   A 1 177 ? 30.381  15.753  23.872 1.00 84.48  ?  204 LEU   A O    1 
ATOM   1151 C  CB   . LEU   A 1 177 ? 30.052  16.878  20.920 1.00 72.14  ?  204 LEU   A CB   1 
ATOM   1152 C  CG   . LEU   A 1 177 ? 29.832  17.044  19.412 1.00 74.01  ?  204 LEU   A CG   1 
ATOM   1153 C  CD1  . LEU   A 1 177 ? 28.540  16.394  18.936 1.00 80.39  ?  204 LEU   A CD1  1 
ATOM   1154 C  CD2  . LEU   A 1 177 ? 29.845  18.517  19.049 1.00 80.95  ?  204 LEU   A CD2  1 
ATOM   1155 N  N    . ASN   A 1 178 ? 32.012  14.854  22.603 1.00 71.86  ?  205 ASN   A N    1 
ATOM   1156 C  CA   . ASN   A 1 178 ? 32.928  14.631  23.711 1.00 73.69  ?  205 ASN   A CA   1 
ATOM   1157 C  C    . ASN   A 1 178 ? 34.287  15.236  23.392 1.00 78.88  ?  205 ASN   A C    1 
ATOM   1158 O  O    . ASN   A 1 178 ? 34.668  15.368  22.225 1.00 80.35  ?  205 ASN   A O    1 
ATOM   1159 C  CB   . ASN   A 1 178 ? 33.091  13.135  24.016 1.00 74.26  ?  205 ASN   A CB   1 
ATOM   1160 C  CG   . ASN   A 1 178 ? 31.765  12.439  24.256 1.00 87.08  ?  205 ASN   A CG   1 
ATOM   1161 O  OD1  . ASN   A 1 178 ? 31.212  12.491  25.355 1.00 94.70  ?  205 ASN   A OD1  1 
ATOM   1162 N  ND2  . ASN   A 1 178 ? 31.255  11.770  23.229 1.00 81.52  ?  205 ASN   A ND2  1 
ATOM   1163 N  N    . PHE   A 1 179 ? 35.018  15.603  24.444 1.00 85.24  ?  206 PHE   A N    1 
ATOM   1164 C  CA   . PHE   A 1 179 ? 36.372  16.117  24.298 1.00 72.74  ?  206 PHE   A CA   1 
ATOM   1165 C  C    . PHE   A 1 179 ? 37.156  15.840  25.571 1.00 79.94  ?  206 PHE   A C    1 
ATOM   1166 O  O    . PHE   A 1 179 ? 36.624  15.969  26.677 1.00 81.12  ?  206 PHE   A O    1 
ATOM   1167 C  CB   . PHE   A 1 179 ? 36.385  17.621  23.998 1.00 81.56  ?  206 PHE   A CB   1 
ATOM   1168 C  CG   . PHE   A 1 179 ? 37.753  18.243  24.089 1.00 79.16  ?  206 PHE   A CG   1 
ATOM   1169 C  CD1  . PHE   A 1 179 ? 38.689  18.035  23.090 1.00 84.46  ?  206 PHE   A CD1  1 
ATOM   1170 C  CD2  . PHE   A 1 179 ? 38.102  19.034  25.173 1.00 83.81  ?  206 PHE   A CD2  1 
ATOM   1171 C  CE1  . PHE   A 1 179 ? 39.948  18.603  23.169 1.00 87.65  ?  206 PHE   A CE1  1 
ATOM   1172 C  CE2  . PHE   A 1 179 ? 39.360  19.604  25.257 1.00 79.95  ?  206 PHE   A CE2  1 
ATOM   1173 C  CZ   . PHE   A 1 179 ? 40.284  19.388  24.253 1.00 88.03  ?  206 PHE   A CZ   1 
ATOM   1174 N  N    . MET   A 1 180 ? 38.420  15.458  25.404 1.00 80.42  ?  207 MET   A N    1 
ATOM   1175 C  CA   . MET   A 1 180 ? 39.332  15.292  26.527 1.00 82.73  ?  207 MET   A CA   1 
ATOM   1176 C  C    . MET   A 1 180 ? 40.752  15.582  26.068 1.00 94.75  ?  207 MET   A C    1 
ATOM   1177 O  O    . MET   A 1 180 ? 41.179  15.094  25.018 1.00 82.57  ?  207 MET   A O    1 
ATOM   1178 C  CB   . MET   A 1 180 ? 39.264  13.879  27.118 1.00 90.99  ?  207 MET   A CB   1 
ATOM   1179 C  CG   . MET   A 1 180 ? 40.335  13.633  28.178 1.00 88.51  ?  207 MET   A CG   1 
ATOM   1180 S  SD   . MET   A 1 180 ? 39.877  12.480  29.483 1.00 111.96 ?  207 MET   A SD   1 
ATOM   1181 C  CE   . MET   A 1 180 ? 41.315  11.412  29.490 1.00 90.01  ?  207 MET   A CE   1 
ATOM   1182 N  N    . ASP   A 1 181 ? 41.472  16.377  26.857 1.00 99.03  ?  208 ASP   A N    1 
ATOM   1183 C  CA   . ASP   A 1 181 ? 42.904  16.544  26.676 1.00 100.08 ?  208 ASP   A CA   1 
ATOM   1184 C  C    . ASP   A 1 181 ? 43.605  15.641  27.679 1.00 102.34 ?  208 ASP   A C    1 
ATOM   1185 O  O    . ASP   A 1 181 ? 43.604  15.951  28.880 1.00 107.10 ?  208 ASP   A O    1 
ATOM   1186 C  CB   . ASP   A 1 181 ? 43.314  18.002  26.877 1.00 103.68 ?  208 ASP   A CB   1 
ATOM   1187 C  CG   . ASP   A 1 181 ? 44.820  18.189  26.929 1.00 117.28 ?  208 ASP   A CG   1 
ATOM   1188 O  OD1  . ASP   A 1 181 ? 45.423  17.939  27.994 1.00 130.76 ?  208 ASP   A OD1  1 
ATOM   1189 O  OD2  . ASP   A 1 181 ? 45.404  18.589  25.901 1.00 117.61 ?  208 ASP   A OD2  1 
ATOM   1190 N  N    . PRO   A 1 182 ? 44.194  14.521  27.253 1.00 100.94 ?  209 PRO   A N    1 
ATOM   1191 C  CA   . PRO   A 1 182 ? 44.774  13.579  28.225 1.00 98.67  ?  209 PRO   A CA   1 
ATOM   1192 C  C    . PRO   A 1 182 ? 45.888  14.175  29.066 1.00 119.90 ?  209 PRO   A C    1 
ATOM   1193 O  O    . PRO   A 1 182 ? 46.131  13.688  30.178 1.00 121.56 ?  209 PRO   A O    1 
ATOM   1194 C  CB   . PRO   A 1 182 ? 45.294  12.433  27.344 1.00 85.66  ?  209 PRO   A CB   1 
ATOM   1195 C  CG   . PRO   A 1 182 ? 45.361  12.999  25.956 1.00 92.56  ?  209 PRO   A CG   1 
ATOM   1196 C  CD   . PRO   A 1 182 ? 44.264  14.009  25.876 1.00 98.72  ?  209 PRO   A CD   1 
ATOM   1197 N  N    . GLN   A 1 183 ? 46.569  15.214  28.580 1.00 114.57 ?  210 GLN   A N    1 
ATOM   1198 C  CA   . GLN   A 1 183 ? 47.657  15.820  29.335 1.00 126.31 ?  210 GLN   A CA   1 
ATOM   1199 C  C    . GLN   A 1 183 ? 47.174  16.567  30.572 1.00 134.68 ?  210 GLN   A C    1 
ATOM   1200 O  O    . GLN   A 1 183 ? 47.994  16.886  31.439 1.00 141.32 ?  210 GLN   A O    1 
ATOM   1201 C  CB   . GLN   A 1 183 ? 48.452  16.771  28.436 1.00 124.71 ?  210 GLN   A CB   1 
ATOM   1202 C  CG   . GLN   A 1 183 ? 49.435  16.092  27.480 1.00 133.89 ?  210 GLN   A CG   1 
ATOM   1203 C  CD   . GLN   A 1 183 ? 49.930  14.742  27.972 1.00 140.97 ?  210 GLN   A CD   1 
ATOM   1204 O  OE1  . GLN   A 1 183 ? 49.702  13.717  27.330 1.00 126.07 ?  210 GLN   A OE1  1 
ATOM   1205 N  NE2  . GLN   A 1 183 ? 50.644  14.741  29.094 1.00 140.07 ?  210 GLN   A NE2  1 
ATOM   1206 N  N    . LYS   A 1 184 ? 45.875  16.849  30.676 1.00 133.24 ?  211 LYS   A N    1 
ATOM   1207 C  CA   . LYS   A 1 184 ? 45.324  17.575  31.814 1.00 132.37 ?  211 LYS   A CA   1 
ATOM   1208 C  C    . LYS   A 1 184 ? 45.051  16.690  33.023 1.00 133.70 ?  211 LYS   A C    1 
ATOM   1209 O  O    . LYS   A 1 184 ? 44.590  17.203  34.050 1.00 131.67 ?  211 LYS   A O    1 
ATOM   1210 C  CB   . LYS   A 1 184 ? 44.026  18.282  31.414 1.00 133.11 ?  211 LYS   A CB   1 
ATOM   1211 C  CG   . LYS   A 1 184 ? 44.218  19.654  30.796 1.00 131.42 ?  211 LYS   A CG   1 
ATOM   1212 C  CD   . LYS   A 1 184 ? 42.938  20.147  30.133 1.00 131.80 ?  211 LYS   A CD   1 
ATOM   1213 C  CE   . LYS   A 1 184 ? 41.819  20.350  31.147 1.00 122.52 ?  211 LYS   A CE   1 
ATOM   1214 N  NZ   . LYS   A 1 184 ? 40.887  19.189  31.219 1.00 117.36 ?  211 LYS   A NZ   1 
ATOM   1215 N  N    . MET   A 1 185 ? 45.314  15.388  32.938 1.00 134.71 ?  212 MET   A N    1 
ATOM   1216 C  CA   . MET   A 1 185 ? 44.979  14.486  34.029 1.00 136.11 ?  212 MET   A CA   1 
ATOM   1217 C  C    . MET   A 1 185 ? 46.238  13.995  34.724 1.00 146.82 ?  212 MET   A C    1 
ATOM   1218 O  O    . MET   A 1 185 ? 47.180  13.550  34.054 1.00 147.18 ?  212 MET   A O    1 
ATOM   1219 C  CB   . MET   A 1 185 ? 44.169  13.294  33.510 1.00 124.20 ?  212 MET   A CB   1 
ATOM   1220 C  CG   . MET   A 1 185 ? 42.845  13.686  32.872 1.00 126.08 ?  212 MET   A CG   1 
ATOM   1221 S  SD   . MET   A 1 185 ? 41.561  14.159  34.055 1.00 136.88 ?  212 MET   A SD   1 
ATOM   1222 C  CE   . MET   A 1 185 ? 42.026  13.222  35.512 1.00 121.37 ?  212 MET   A CE   1 
ATOM   1223 N  N    . PRO   A 1 186 ? 46.289  14.059  36.059 1.00 141.78 ?  213 PRO   A N    1 
ATOM   1224 C  CA   . PRO   A 1 186 ? 47.503  13.606  36.758 1.00 126.95 ?  213 PRO   A CA   1 
ATOM   1225 C  C    . PRO   A 1 186 ? 47.719  12.107  36.663 1.00 126.19 ?  213 PRO   A C    1 
ATOM   1226 O  O    . PRO   A 1 186 ? 48.858  11.659  36.472 1.00 120.35 ?  213 PRO   A O    1 
ATOM   1227 C  CB   . PRO   A 1 186 ? 47.257  14.055  38.208 1.00 109.67 ?  213 PRO   A CB   1 
ATOM   1228 C  CG   . PRO   A 1 186 ? 46.180  15.105  38.117 1.00 102.10 ?  213 PRO   A CG   1 
ATOM   1229 C  CD   . PRO   A 1 186 ? 45.315  14.662  36.981 1.00 123.12 ?  213 PRO   A CD   1 
ATOM   1230 N  N    . TYR   A 1 187 ? 46.655  11.319  36.797 1.00 132.40 ?  214 TYR   A N    1 
ATOM   1231 C  CA   . TYR   A 1 187 ? 46.751  9.865   36.730 1.00 123.05 ?  214 TYR   A CA   1 
ATOM   1232 C  C    . TYR   A 1 187 ? 45.461  9.335   36.126 1.00 123.90 ?  214 TYR   A C    1 
ATOM   1233 O  O    . TYR   A 1 187 ? 44.389  9.495   36.716 1.00 116.79 ?  214 TYR   A O    1 
ATOM   1234 C  CB   . TYR   A 1 187 ? 46.991  9.266   38.119 1.00 119.58 ?  214 TYR   A CB   1 
ATOM   1235 C  CG   . TYR   A 1 187 ? 47.073  7.753   38.159 1.00 125.17 ?  214 TYR   A CG   1 
ATOM   1236 C  CD1  . TYR   A 1 187 ? 48.230  7.085   37.779 1.00 118.33 ?  214 TYR   A CD1  1 
ATOM   1237 C  CD2  . TYR   A 1 187 ? 45.994  6.996   38.591 1.00 122.24 ?  214 TYR   A CD2  1 
ATOM   1238 C  CE1  . TYR   A 1 187 ? 48.304  5.700   37.822 1.00 124.78 ?  214 TYR   A CE1  1 
ATOM   1239 C  CE2  . TYR   A 1 187 ? 46.057  5.615   38.636 1.00 127.54 ?  214 TYR   A CE2  1 
ATOM   1240 C  CZ   . TYR   A 1 187 ? 47.213  4.972   38.251 1.00 134.92 ?  214 TYR   A CZ   1 
ATOM   1241 O  OH   . TYR   A 1 187 ? 47.275  3.598   38.297 1.00 145.52 ?  214 TYR   A OH   1 
ATOM   1242 N  N    . LEU   A 1 188 ? 45.562  8.725   34.950 1.00 124.41 ?  215 LEU   A N    1 
ATOM   1243 C  CA   . LEU   A 1 188 ? 44.411  8.127   34.292 1.00 106.77 ?  215 LEU   A CA   1 
ATOM   1244 C  C    . LEU   A 1 188 ? 44.255  6.680   34.736 1.00 104.88 ?  215 LEU   A C    1 
ATOM   1245 O  O    . LEU   A 1 188 ? 45.242  5.957   34.899 1.00 108.24 ?  215 LEU   A O    1 
ATOM   1246 C  CB   . LEU   A 1 188 ? 44.555  8.201   32.771 1.00 99.04  ?  215 LEU   A CB   1 
ATOM   1247 C  CG   . LEU   A 1 188 ? 44.227  9.555   32.141 1.00 98.47  ?  215 LEU   A CG   1 
ATOM   1248 C  CD1  . LEU   A 1 188 ? 44.288  9.474   30.624 1.00 92.78  ?  215 LEU   A CD1  1 
ATOM   1249 C  CD2  . LEU   A 1 188 ? 42.856  10.023  32.598 1.00 95.21  ?  215 LEU   A CD2  1 
ATOM   1250 N  N    . LYS   A 1 189 ? 43.007  6.266   34.938 1.00 101.61 ?  216 LYS   A N    1 
ATOM   1251 C  CA   . LYS   A 1 189 ? 42.736  4.919   35.417 1.00 91.94  ?  216 LYS   A CA   1 
ATOM   1252 C  C    . LYS   A 1 189 ? 43.216  3.882   34.409 1.00 89.26  ?  216 LYS   A C    1 
ATOM   1253 O  O    . LYS   A 1 189 ? 43.018  4.024   33.200 1.00 92.10  ?  216 LYS   A O    1 
ATOM   1254 C  CB   . LYS   A 1 189 ? 41.239  4.741   35.682 1.00 95.67  ?  216 LYS   A CB   1 
ATOM   1255 C  CG   . LYS   A 1 189 ? 40.858  3.338   36.127 1.00 100.56 ?  216 LYS   A CG   1 
ATOM   1256 C  CD   . LYS   A 1 189 ? 39.646  3.350   37.042 1.00 104.09 ?  216 LYS   A CD   1 
ATOM   1257 C  CE   . LYS   A 1 189 ? 39.168  1.936   37.337 1.00 111.31 ?  216 LYS   A CE   1 
ATOM   1258 N  NZ   . LYS   A 1 189 ? 39.781  1.391   38.581 1.00 102.36 ?  216 LYS   A NZ   1 
ATOM   1259 N  N    . GLU   A 1 190 ? 43.863  2.838   34.918 1.00 89.94  ?  217 GLU   A N    1 
ATOM   1260 C  CA   . GLU   A 1 190 ? 44.312  1.738   34.078 1.00 87.41  ?  217 GLU   A CA   1 
ATOM   1261 C  C    . GLU   A 1 190 ? 43.160  0.782   33.798 1.00 86.60  ?  217 GLU   A C    1 
ATOM   1262 O  O    . GLU   A 1 190 ? 42.292  0.564   34.649 1.00 80.85  ?  217 GLU   A O    1 
ATOM   1263 C  CB   . GLU   A 1 190 ? 45.460  0.984   34.752 1.00 93.47  ?  217 GLU   A CB   1 
ATOM   1264 C  CG   . GLU   A 1 190 ? 46.420  0.311   33.785 1.00 100.08 ?  217 GLU   A CG   1 
ATOM   1265 C  CD   . GLU   A 1 190 ? 47.667  1.135   33.529 1.00 91.30  ?  217 GLU   A CD   1 
ATOM   1266 O  OE1  . GLU   A 1 190 ? 47.798  2.220   34.133 1.00 117.81 ?  217 GLU   A OE1  1 
ATOM   1267 O  OE2  . GLU   A 1 190 ? 48.516  0.697   32.725 1.00 91.89  ?  217 GLU   A OE2  1 
ATOM   1268 N  N    . GLU   A 1 191 ? 43.150  0.219   32.598 1.00 83.93  ?  218 GLU   A N    1 
ATOM   1269 C  CA   . GLU   A 1 191 ? 42.167  -0.804  32.259 1.00 71.09  ?  218 GLU   A CA   1 
ATOM   1270 C  C    . GLU   A 1 191 ? 42.441  -2.044  33.100 1.00 70.48  ?  218 GLU   A C    1 
ATOM   1271 O  O    . GLU   A 1 191 ? 43.552  -2.588  33.043 1.00 78.55  ?  218 GLU   A O    1 
ATOM   1272 C  CB   . GLU   A 1 191 ? 42.224  -1.124  30.770 1.00 73.58  ?  218 GLU   A CB   1 
ATOM   1273 C  CG   . GLU   A 1 191 ? 40.996  -1.843  30.235 1.00 69.20  ?  218 GLU   A CG   1 
ATOM   1274 C  CD   . GLU   A 1 191 ? 41.025  -3.331  30.521 1.00 79.50  ?  218 GLU   A CD   1 
ATOM   1275 O  OE1  . GLU   A 1 191 ? 41.991  -3.996  30.092 1.00 72.81  ?  218 GLU   A OE1  1 
ATOM   1276 O  OE2  . GLU   A 1 191 ? 40.087  -3.834  31.173 1.00 70.88  ?  218 GLU   A OE2  1 
ATOM   1277 N  N    . PRO   A 1 192 ? 41.476  -2.526  33.887 1.00 68.30  ?  219 PRO   A N    1 
ATOM   1278 C  CA   . PRO   A 1 192 ? 41.788  -3.497  34.942 1.00 70.10  ?  219 PRO   A CA   1 
ATOM   1279 C  C    . PRO   A 1 192 ? 41.686  -4.970  34.574 1.00 75.59  ?  219 PRO   A C    1 
ATOM   1280 O  O    . PRO   A 1 192 ? 42.039  -5.808  35.416 1.00 89.20  ?  219 PRO   A O    1 
ATOM   1281 C  CB   . PRO   A 1 192 ? 40.747  -3.152  36.020 1.00 70.27  ?  219 PRO   A CB   1 
ATOM   1282 C  CG   . PRO   A 1 192 ? 39.573  -2.622  35.252 1.00 63.65  ?  219 PRO   A CG   1 
ATOM   1283 C  CD   . PRO   A 1 192 ? 40.075  -2.070  33.941 1.00 70.88  ?  219 PRO   A CD   1 
ATOM   1284 N  N    . TYR   A 1 193 ? 41.235  -5.325  33.374 1.00 75.15  ?  220 TYR   A N    1 
ATOM   1285 C  CA   . TYR   A 1 193 ? 40.987  -6.726  33.044 1.00 77.55  ?  220 TYR   A CA   1 
ATOM   1286 C  C    . TYR   A 1 193 ? 41.913  -7.289  31.978 1.00 71.10  ?  220 TYR   A C    1 
ATOM   1287 O  O    . TYR   A 1 193 ? 42.362  -8.430  32.105 1.00 78.25  ?  220 TYR   A O    1 
ATOM   1288 C  CB   . TYR   A 1 193 ? 39.534  -6.912  32.593 1.00 69.10  ?  220 TYR   A CB   1 
ATOM   1289 C  CG   . TYR   A 1 193 ? 38.530  -6.341  33.567 1.00 82.43  ?  220 TYR   A CG   1 
ATOM   1290 C  CD1  . TYR   A 1 193 ? 38.490  -6.778  34.884 1.00 73.46  ?  220 TYR   A CD1  1 
ATOM   1291 C  CD2  . TYR   A 1 193 ? 37.628  -5.361  33.173 1.00 65.71  ?  220 TYR   A CD2  1 
ATOM   1292 C  CE1  . TYR   A 1 193 ? 37.580  -6.256  35.782 1.00 77.64  ?  220 TYR   A CE1  1 
ATOM   1293 C  CE2  . TYR   A 1 193 ? 36.713  -4.833  34.065 1.00 69.68  ?  220 TYR   A CE2  1 
ATOM   1294 C  CZ   . TYR   A 1 193 ? 36.695  -5.286  35.368 1.00 77.35  ?  220 TYR   A CZ   1 
ATOM   1295 O  OH   . TYR   A 1 193 ? 35.790  -4.767  36.265 1.00 78.08  ?  220 TYR   A OH   1 
ATOM   1296 N  N    . PHE   A 1 194 ? 42.218  -6.527  30.928 1.00 67.66  ?  221 PHE   A N    1 
ATOM   1297 C  CA   . PHE   A 1 194 ? 42.954  -7.053  29.785 1.00 68.32  ?  221 PHE   A CA   1 
ATOM   1298 C  C    . PHE   A 1 194 ? 44.293  -6.361  29.564 1.00 83.36  ?  221 PHE   A C    1 
ATOM   1299 O  O    . PHE   A 1 194 ? 44.940  -6.604  28.538 1.00 84.62  ?  221 PHE   A O    1 
ATOM   1300 C  CB   . PHE   A 1 194 ? 42.098  -6.947  28.518 1.00 78.34  ?  221 PHE   A CB   1 
ATOM   1301 C  CG   . PHE   A 1 194 ? 40.704  -7.485  28.682 1.00 75.83  ?  221 PHE   A CG   1 
ATOM   1302 C  CD1  . PHE   A 1 194 ? 40.486  -8.838  28.888 1.00 74.25  ?  221 PHE   A CD1  1 
ATOM   1303 C  CD2  . PHE   A 1 194 ? 39.610  -6.636  28.634 1.00 57.76  ?  221 PHE   A CD2  1 
ATOM   1304 C  CE1  . PHE   A 1 194 ? 39.203  -9.334  29.039 1.00 73.66  ?  221 PHE   A CE1  1 
ATOM   1305 C  CE2  . PHE   A 1 194 ? 38.325  -7.125  28.785 1.00 60.65  ?  221 PHE   A CE2  1 
ATOM   1306 C  CZ   . PHE   A 1 194 ? 38.122  -8.476  28.988 1.00 76.85  ?  221 PHE   A CZ   1 
ATOM   1307 N  N    . GLY   A 1 195 ? 44.732  -5.515  30.493 1.00 88.32  ?  222 GLY   A N    1 
ATOM   1308 C  CA   . GLY   A 1 195 ? 45.982  -4.796  30.308 1.00 67.75  ?  222 GLY   A CA   1 
ATOM   1309 C  C    . GLY   A 1 195 ? 45.964  -3.828  29.148 1.00 72.85  ?  222 GLY   A C    1 
ATOM   1310 O  O    . GLY   A 1 195 ? 46.993  -3.636  28.491 1.00 68.37  ?  222 GLY   A O    1 
ATOM   1311 N  N    . MET   A 1 196 ? 44.816  -3.210  28.876 1.00 85.01  ?  223 MET   A N    1 
ATOM   1312 C  CA   . MET   A 1 196 ? 44.665  -2.304  27.745 1.00 72.91  ?  223 MET   A CA   1 
ATOM   1313 C  C    . MET   A 1 196 ? 45.290  -0.937  27.987 1.00 73.29  ?  223 MET   A C    1 
ATOM   1314 O  O    . MET   A 1 196 ? 45.304  -0.110  27.069 1.00 71.23  ?  223 MET   A O    1 
ATOM   1315 C  CB   . MET   A 1 196 ? 43.182  -2.135  27.411 1.00 70.85  ?  223 MET   A CB   1 
ATOM   1316 C  CG   . MET   A 1 196 ? 42.519  -3.389  26.873 1.00 80.12  ?  223 MET   A CG   1 
ATOM   1317 S  SD   . MET   A 1 196 ? 40.867  -3.062  26.233 1.00 75.28  ?  223 MET   A SD   1 
ATOM   1318 C  CE   . MET   A 1 196 ? 40.904  -3.996  24.708 1.00 74.83  ?  223 MET   A CE   1 
ATOM   1319 N  N    . GLY   A 1 197 ? 45.793  -0.672  29.189 1.00 77.33  ?  224 GLY   A N    1 
ATOM   1320 C  CA   . GLY   A 1 197 ? 46.435  0.595   29.463 1.00 74.72  ?  224 GLY   A CA   1 
ATOM   1321 C  C    . GLY   A 1 197 ? 45.490  1.673   29.952 1.00 78.46  ?  224 GLY   A C    1 
ATOM   1322 O  O    . GLY   A 1 197 ? 44.451  1.380   30.551 1.00 75.25  ?  224 GLY   A O    1 
ATOM   1323 N  N    . LYS   A 1 198 ? 45.840  2.928   29.684 1.00 81.40  ?  225 LYS   A N    1 
ATOM   1324 C  CA   . LYS   A 1 198 ? 45.127  4.054   30.269 1.00 80.19  ?  225 LYS   A CA   1 
ATOM   1325 C  C    . LYS   A 1 198 ? 43.756  4.233   29.627 1.00 73.13  ?  225 LYS   A C    1 
ATOM   1326 O  O    . LYS   A 1 198 ? 43.588  4.060   28.417 1.00 84.86  ?  225 LYS   A O    1 
ATOM   1327 C  CB   . LYS   A 1 198 ? 45.954  5.330   30.117 1.00 88.62  ?  225 LYS   A CB   1 
ATOM   1328 C  CG   . LYS   A 1 198 ? 46.766  5.685   31.352 1.00 83.24  ?  225 LYS   A CG   1 
ATOM   1329 C  CD   . LYS   A 1 198 ? 47.916  4.710   31.555 1.00 86.21  ?  225 LYS   A CD   1 
ATOM   1330 C  CE   . LYS   A 1 198 ? 48.709  5.044   32.808 1.00 90.05  ?  225 LYS   A CE   1 
ATOM   1331 N  NZ   . LYS   A 1 198 ? 47.925  4.784   34.048 1.00 93.74  ?  225 LYS   A NZ   1 
ATOM   1332 N  N    . MET   A 1 199 ? 42.775  4.594   30.452 1.00 79.81  ?  226 MET   A N    1 
ATOM   1333 C  CA   . MET   A 1 199 ? 41.389  4.742   30.034 1.00 80.92  ?  226 MET   A CA   1 
ATOM   1334 C  C    . MET   A 1 199 ? 40.942  6.188   30.186 1.00 81.12  ?  226 MET   A C    1 
ATOM   1335 O  O    . MET   A 1 199 ? 41.299  6.860   31.159 1.00 93.73  ?  226 MET   A O    1 
ATOM   1336 C  CB   . MET   A 1 199 ? 40.462  3.846   30.861 1.00 78.87  ?  226 MET   A CB   1 
ATOM   1337 C  CG   . MET   A 1 199 ? 40.225  2.461   30.294 1.00 73.79  ?  226 MET   A CG   1 
ATOM   1338 S  SD   . MET   A 1 199 ? 39.042  1.539   31.297 1.00 78.92  ?  226 MET   A SD   1 
ATOM   1339 C  CE   . MET   A 1 199 ? 39.346  2.236   32.920 1.00 81.12  ?  226 MET   A CE   1 
ATOM   1340 N  N    . ALA   A 1 200 ? 40.153  6.658   29.222 1.00 67.77  ?  227 ALA   A N    1 
ATOM   1341 C  CA   . ALA   A 1 200 ? 39.446  7.928   29.333 1.00 70.83  ?  227 ALA   A CA   1 
ATOM   1342 C  C    . ALA   A 1 200 ? 38.013  7.750   29.814 1.00 69.84  ?  227 ALA   A C    1 
ATOM   1343 O  O    . ALA   A 1 200 ? 37.537  8.535   30.639 1.00 79.05  ?  227 ALA   A O    1 
ATOM   1344 C  CB   . ALA   A 1 200 ? 39.445  8.658   27.986 1.00 69.63  ?  227 ALA   A CB   1 
ATOM   1345 N  N    . VAL   A 1 201 ? 37.319  6.732   29.309 1.00 58.83  ?  228 VAL   A N    1 
ATOM   1346 C  CA   . VAL   A 1 201 ? 35.993  6.344   29.774 1.00 71.49  ?  228 VAL   A CA   1 
ATOM   1347 C  C    . VAL   A 1 201 ? 36.030  4.852   30.073 1.00 67.34  ?  228 VAL   A C    1 
ATOM   1348 O  O    . VAL   A 1 201 ? 36.487  4.064   29.238 1.00 71.41  ?  228 VAL   A O    1 
ATOM   1349 C  CB   . VAL   A 1 201 ? 34.900  6.662   28.735 1.00 61.47  ?  228 VAL   A CB   1 
ATOM   1350 C  CG1  . VAL   A 1 201 ? 33.522  6.376   29.309 1.00 65.26  ?  228 VAL   A CG1  1 
ATOM   1351 C  CG2  . VAL   A 1 201 ? 35.002  8.109   28.273 1.00 75.04  ?  228 VAL   A CG2  1 
ATOM   1352 N  N    . SER   A 1 202 ? 35.556  4.465   31.255 1.00 65.24  ?  229 SER   A N    1 
ATOM   1353 C  CA   . SER   A 1 202 ? 35.641  3.075   31.681 1.00 75.45  ?  229 SER   A CA   1 
ATOM   1354 C  C    . SER   A 1 202 ? 34.538  2.240   31.029 1.00 68.18  ?  229 SER   A C    1 
ATOM   1355 O  O    . SER   A 1 202 ? 33.701  2.740   30.272 1.00 56.15  ?  229 SER   A O    1 
ATOM   1356 C  CB   . SER   A 1 202 ? 35.579  2.980   33.204 1.00 65.48  ?  229 SER   A CB   1 
ATOM   1357 O  OG   . SER   A 1 202 ? 35.015  4.149   33.769 1.00 95.48  ?  229 SER   A OG   1 
ATOM   1358 N  N    . TRP   A 1 203 ? 34.546  0.942   31.333 1.00 75.42  ?  230 TRP   A N    1 
ATOM   1359 C  CA   . TRP   A 1 203 ? 33.617  0.003   30.714 1.00 63.01  ?  230 TRP   A CA   1 
ATOM   1360 C  C    . TRP   A 1 203 ? 32.177  0.347   31.070 1.00 66.10  ?  230 TRP   A C    1 
ATOM   1361 O  O    . TRP   A 1 203 ? 31.849  0.561   32.241 1.00 64.33  ?  230 TRP   A O    1 
ATOM   1362 C  CB   . TRP   A 1 203 ? 33.940  -1.423  31.162 1.00 62.10  ?  230 TRP   A CB   1 
ATOM   1363 C  CG   . TRP   A 1 203 ? 35.265  -1.926  30.683 1.00 60.86  ?  230 TRP   A CG   1 
ATOM   1364 C  CD1  . TRP   A 1 203 ? 36.383  -2.138  31.437 1.00 69.50  ?  230 TRP   A CD1  1 
ATOM   1365 C  CD2  . TRP   A 1 203 ? 35.611  -2.295  29.342 1.00 65.37  ?  230 TRP   A CD2  1 
ATOM   1366 N  NE1  . TRP   A 1 203 ? 37.405  -2.610  30.649 1.00 61.98  ?  230 TRP   A NE1  1 
ATOM   1367 C  CE2  . TRP   A 1 203 ? 36.956  -2.716  29.358 1.00 69.50  ?  230 TRP   A CE2  1 
ATOM   1368 C  CE3  . TRP   A 1 203 ? 34.915  -2.309  28.129 1.00 65.69  ?  230 TRP   A CE3  1 
ATOM   1369 C  CZ2  . TRP   A 1 203 ? 37.618  -3.144  28.209 1.00 61.21  ?  230 TRP   A CZ2  1 
ATOM   1370 C  CZ3  . TRP   A 1 203 ? 35.574  -2.735  26.989 1.00 68.33  ?  230 TRP   A CZ3  1 
ATOM   1371 C  CH2  . TRP   A 1 203 ? 36.912  -3.146  27.038 1.00 61.75  ?  230 TRP   A CH2  1 
ATOM   1372 N  N    . HIS   A 1 204 ? 31.314  0.384   30.057 1.00 52.70  ?  231 HIS   A N    1 
ATOM   1373 C  CA   . HIS   A 1 204 ? 29.921  0.758   30.259 1.00 58.58  ?  231 HIS   A CA   1 
ATOM   1374 C  C    . HIS   A 1 204 ? 29.104  0.332   29.048 1.00 59.72  ?  231 HIS   A C    1 
ATOM   1375 O  O    . HIS   A 1 204 ? 29.644  0.009   27.987 1.00 59.26  ?  231 HIS   A O    1 
ATOM   1376 C  CB   . HIS   A 1 204 ? 29.776  2.267   30.479 1.00 55.26  ?  231 HIS   A CB   1 
ATOM   1377 C  CG   . HIS   A 1 204 ? 30.013  3.080   29.243 1.00 60.53  ?  231 HIS   A CG   1 
ATOM   1378 N  ND1  . HIS   A 1 204 ? 31.265  3.252   28.692 1.00 67.11  ?  231 HIS   A ND1  1 
ATOM   1379 C  CD2  . HIS   A 1 204 ? 29.155  3.756   28.443 1.00 58.21  ?  231 HIS   A CD2  1 
ATOM   1380 C  CE1  . HIS   A 1 204 ? 31.168  4.005   27.610 1.00 54.98  ?  231 HIS   A CE1  1 
ATOM   1381 N  NE2  . HIS   A 1 204 ? 29.899  4.324   27.437 1.00 62.41  ?  231 HIS   A NE2  1 
ATOM   1382 N  N    . HIS   A 1 205 ? 27.786  0.333   29.228 1.00 69.43  ?  232 HIS   A N    1 
ATOM   1383 C  CA   . HIS   A 1 205 ? 26.841  0.366   28.123 1.00 55.54  ?  232 HIS   A CA   1 
ATOM   1384 C  C    . HIS   A 1 205 ? 26.306  1.783   27.978 1.00 58.07  ?  232 HIS   A C    1 
ATOM   1385 O  O    . HIS   A 1 205 ? 26.287  2.557   28.938 1.00 62.61  ?  232 HIS   A O    1 
ATOM   1386 C  CB   . HIS   A 1 205 ? 25.668  -0.595  28.339 1.00 50.98  ?  232 HIS   A CB   1 
ATOM   1387 C  CG   . HIS   A 1 205 ? 26.066  -1.956  28.814 1.00 50.76  ?  232 HIS   A CG   1 
ATOM   1388 N  ND1  . HIS   A 1 205 ? 26.397  -2.978  27.950 1.00 61.34  ?  232 HIS   A ND1  1 
ATOM   1389 C  CD2  . HIS   A 1 205 ? 26.160  -2.473  30.062 1.00 59.07  ?  232 HIS   A CD2  1 
ATOM   1390 C  CE1  . HIS   A 1 205 ? 26.691  -4.062  28.646 1.00 59.79  ?  232 HIS   A CE1  1 
ATOM   1391 N  NE2  . HIS   A 1 205 ? 26.555  -3.782  29.930 1.00 61.48  ?  232 HIS   A NE2  1 
ATOM   1392 N  N    . ASP   A 1 206 ? 25.872  2.121   26.769 1.00 73.63  ?  233 ASP   A N    1 
ATOM   1393 C  CA   . ASP   A 1 206 ? 25.206  3.397   26.544 1.00 69.47  ?  233 ASP   A CA   1 
ATOM   1394 C  C    . ASP   A 1 206 ? 23.771  3.305   27.050 1.00 64.00  ?  233 ASP   A C    1 
ATOM   1395 O  O    . ASP   A 1 206 ? 22.988  2.480   26.567 1.00 64.75  ?  233 ASP   A O    1 
ATOM   1396 C  CB   . ASP   A 1 206 ? 25.244  3.775   25.065 1.00 70.19  ?  233 ASP   A CB   1 
ATOM   1397 C  CG   . ASP   A 1 206 ? 26.616  4.242   24.616 1.00 77.84  ?  233 ASP   A CG   1 
ATOM   1398 O  OD1  . ASP   A 1 206 ? 27.527  4.322   25.466 1.00 85.40  ?  233 ASP   A OD1  1 
ATOM   1399 O  OD2  . ASP   A 1 206 ? 26.783  4.531   23.411 1.00 78.66  ?  233 ASP   A OD2  1 
ATOM   1400 N  N    . GLU   A 1 207 ? 23.435  4.139   28.030 1.00 70.21  ?  234 GLU   A N    1 
ATOM   1401 C  CA   . GLU   A 1 207 ? 22.117  4.114   28.642 1.00 59.82  ?  234 GLU   A CA   1 
ATOM   1402 C  C    . GLU   A 1 207 ? 21.099  4.858   27.783 1.00 70.58  ?  234 GLU   A C    1 
ATOM   1403 O  O    . GLU   A 1 207 ? 21.444  5.643   26.895 1.00 53.96  ?  234 GLU   A O    1 
ATOM   1404 C  CB   . GLU   A 1 207 ? 22.155  4.745   30.034 1.00 68.95  ?  234 GLU   A CB   1 
ATOM   1405 C  CG   . GLU   A 1 207 ? 22.657  3.839   31.143 1.00 72.51  ?  234 GLU   A CG   1 
ATOM   1406 C  CD   . GLU   A 1 207 ? 22.695  4.546   32.486 1.00 86.22  ?  234 GLU   A CD   1 
ATOM   1407 O  OE1  . GLU   A 1 207 ? 23.222  3.964   33.457 1.00 101.89 ?  234 GLU   A OE1  1 
ATOM   1408 O  OE2  . GLU   A 1 207 ? 22.198  5.690   32.569 1.00 83.19  ?  234 GLU   A OE2  1 
ATOM   1409 N  N    . ASN   A 1 208 ? 19.823  4.591   28.068 1.00 71.00  ?  235 ASN   A N    1 
ATOM   1410 C  CA   . ASN   A 1 208 ? 18.697  5.363   27.540 1.00 69.35  ?  235 ASN   A CA   1 
ATOM   1411 C  C    . ASN   A 1 208 ? 18.727  5.391   26.009 1.00 64.81  ?  235 ASN   A C    1 
ATOM   1412 O  O    . ASN   A 1 208 ? 18.715  6.444   25.369 1.00 71.18  ?  235 ASN   A O    1 
ATOM   1413 C  CB   . ASN   A 1 208 ? 18.689  6.772   28.151 1.00 72.29  ?  235 ASN   A CB   1 
ATOM   1414 C  CG   . ASN   A 1 208 ? 17.628  7.683   27.553 1.00 83.11  ?  235 ASN   A CG   1 
ATOM   1415 O  OD1  . ASN   A 1 208 ? 17.940  8.663   26.879 1.00 83.68  ?  235 ASN   A OD1  1 
ATOM   1416 N  ND2  . ASN   A 1 208 ? 16.363  7.354   27.794 1.00 86.51  ?  235 ASN   A ND2  1 
ATOM   1417 N  N    . LEU   A 1 209 ? 18.795  4.203   25.416 1.00 59.67  ?  236 LEU   A N    1 
ATOM   1418 C  CA   . LEU   A 1 209 ? 18.706  4.044   23.974 1.00 57.98  ?  236 LEU   A CA   1 
ATOM   1419 C  C    . LEU   A 1 209 ? 17.502  3.177   23.639 1.00 61.13  ?  236 LEU   A C    1 
ATOM   1420 O  O    . LEU   A 1 209 ? 17.099  2.317   24.428 1.00 50.77  ?  236 LEU   A O    1 
ATOM   1421 C  CB   . LEU   A 1 209 ? 19.972  3.408   23.387 1.00 70.15  ?  236 LEU   A CB   1 
ATOM   1422 C  CG   . LEU   A 1 209 ? 21.317  4.076   23.667 1.00 78.70  ?  236 LEU   A CG   1 
ATOM   1423 C  CD1  . LEU   A 1 209 ? 22.413  3.342   22.919 1.00 63.69  ?  236 LEU   A CD1  1 
ATOM   1424 C  CD2  . LEU   A 1 209 ? 21.289  5.547   23.283 1.00 62.71  ?  236 LEU   A CD2  1 
ATOM   1425 N  N    . VAL   A 1 210 ? 16.922  3.422   22.462 1.00 55.75  ?  237 VAL   A N    1 
ATOM   1426 C  CA   . VAL   A 1 210 ? 15.870  2.547   21.969 1.00 57.99  ?  237 VAL   A CA   1 
ATOM   1427 C  C    . VAL   A 1 210 ? 16.425  1.136   21.847 1.00 67.37  ?  237 VAL   A C    1 
ATOM   1428 O  O    . VAL   A 1 210 ? 17.597  0.935   21.500 1.00 60.89  ?  237 VAL   A O    1 
ATOM   1429 C  CB   . VAL   A 1 210 ? 15.324  3.061   20.627 1.00 62.48  ?  237 VAL   A CB   1 
ATOM   1430 C  CG1  . VAL   A 1 210 ? 14.157  2.205   20.157 1.00 57.36  ?  237 VAL   A CG1  1 
ATOM   1431 C  CG2  . VAL   A 1 210 ? 14.890  4.510   20.760 1.00 66.36  ?  237 VAL   A CG2  1 
ATOM   1432 N  N    . ASP   A 1 211 ? 15.590  0.150   22.169 1.00 66.77  ?  238 ASP   A N    1 
ATOM   1433 C  CA   . ASP   A 1 211 ? 16.022  -1.240  22.134 1.00 54.47  ?  238 ASP   A CA   1 
ATOM   1434 C  C    . ASP   A 1 211 ? 16.557  -1.597  20.754 1.00 71.50  ?  238 ASP   A C    1 
ATOM   1435 O  O    . ASP   A 1 211 ? 15.912  -1.330  19.736 1.00 68.00  ?  238 ASP   A O    1 
ATOM   1436 C  CB   . ASP   A 1 211 ? 14.863  -2.161  22.511 1.00 64.70  ?  238 ASP   A CB   1 
ATOM   1437 C  CG   . ASP   A 1 211 ? 15.334  -3.488  23.069 1.00 78.96  ?  238 ASP   A CG   1 
ATOM   1438 O  OD1  . ASP   A 1 211 ? 15.805  -3.516  24.225 1.00 84.95  ?  238 ASP   A OD1  1 
ATOM   1439 O  OD2  . ASP   A 1 211 ? 15.233  -4.505  22.350 1.00 72.31  ?  238 ASP   A OD2  1 
ATOM   1440 N  N    . ARG   A 1 212 ? 17.758  -2.177  20.728 1.00 70.43  ?  239 ARG   A N    1 
ATOM   1441 C  CA   . ARG   A 1 212 ? 18.423  -2.623  19.506 1.00 65.60  ?  239 ARG   A CA   1 
ATOM   1442 C  C    . ARG   A 1 212 ? 18.692  -1.478  18.533 1.00 63.33  ?  239 ARG   A C    1 
ATOM   1443 O  O    . ARG   A 1 212 ? 18.838  -1.705  17.328 1.00 64.40  ?  239 ARG   A O    1 
ATOM   1444 C  CB   . ARG   A 1 212 ? 17.621  -3.732  18.817 1.00 68.94  ?  239 ARG   A CB   1 
ATOM   1445 C  CG   . ARG   A 1 212 ? 17.427  -4.962  19.687 1.00 74.63  ?  239 ARG   A CG   1 
ATOM   1446 C  CD   . ARG   A 1 212 ? 16.597  -6.024  18.989 1.00 83.46  ?  239 ARG   A CD   1 
ATOM   1447 N  NE   . ARG   A 1 212 ? 17.343  -7.265  18.826 1.00 96.94  ?  239 ARG   A NE   1 
ATOM   1448 C  CZ   . ARG   A 1 212 ? 17.522  -8.163  19.786 1.00 102.87 ?  239 ARG   A CZ   1 
ATOM   1449 N  NH1  . ARG   A 1 212 ? 17.021  -7.988  20.998 1.00 101.71 ?  239 ARG   A NH1  1 
ATOM   1450 N  NH2  . ARG   A 1 212 ? 18.225  -9.261  19.524 1.00 94.79  ?  239 ARG   A NH2  1 
ATOM   1451 N  N    . SER   A 1 213 ? 18.766  -0.247  19.031 1.00 67.70  ?  240 SER   A N    1 
ATOM   1452 C  CA   . SER   A 1 213 ? 19.097  0.889   18.186 1.00 68.94  ?  240 SER   A CA   1 
ATOM   1453 C  C    . SER   A 1 213 ? 20.607  1.000   18.014 1.00 76.41  ?  240 SER   A C    1 
ATOM   1454 O  O    . SER   A 1 213 ? 21.385  0.676   18.917 1.00 66.46  ?  240 SER   A O    1 
ATOM   1455 C  CB   . SER   A 1 213 ? 18.542  2.184   18.777 1.00 64.78  ?  240 SER   A CB   1 
ATOM   1456 O  OG   . SER   A 1 213 ? 19.340  2.633   19.857 1.00 62.72  ?  240 SER   A OG   1 
ATOM   1457 N  N    . ALA   A 1 214 ? 21.017  1.464   16.839 1.00 63.99  ?  241 ALA   A N    1 
ATOM   1458 C  CA   . ALA   A 1 214 ? 22.431  1.558   16.519 1.00 69.71  ?  241 ALA   A CA   1 
ATOM   1459 C  C    . ALA   A 1 214 ? 23.042  2.821   17.123 1.00 66.61  ?  241 ALA   A C    1 
ATOM   1460 O  O    . ALA   A 1 214 ? 22.345  3.724   17.594 1.00 64.29  ?  241 ALA   A O    1 
ATOM   1461 C  CB   . ALA   A 1 214 ? 22.640  1.536   15.006 1.00 69.37  ?  241 ALA   A CB   1 
ATOM   1462 N  N    . VAL   A 1 215 ? 24.372  2.868   17.110 1.00 54.07  ?  242 VAL   A N    1 
ATOM   1463 C  CA   . VAL   A 1 215 ? 25.134  4.020   17.581 1.00 60.05  ?  242 VAL   A CA   1 
ATOM   1464 C  C    . VAL   A 1 215 ? 26.303  4.234   16.631 1.00 50.82  ?  242 VAL   A C    1 
ATOM   1465 O  O    . VAL   A 1 215 ? 27.084  3.310   16.384 1.00 56.66  ?  242 VAL   A O    1 
ATOM   1466 C  CB   . VAL   A 1 215 ? 25.642  3.831   19.025 1.00 63.61  ?  242 VAL   A CB   1 
ATOM   1467 C  CG1  . VAL   A 1 215 ? 26.720  4.855   19.349 1.00 58.00  ?  242 VAL   A CG1  1 
ATOM   1468 C  CG2  . VAL   A 1 215 ? 24.493  3.940   20.012 1.00 64.71  ?  242 VAL   A CG2  1 
ATOM   1469 N  N    . ALA   A 1 216 ? 26.418  5.444   16.092 1.00 61.29  ?  243 ALA   A N    1 
ATOM   1470 C  CA   . ALA   A 1 216 ? 27.496  5.808   15.185 1.00 74.36  ?  243 ALA   A CA   1 
ATOM   1471 C  C    . ALA   A 1 216 ? 28.383  6.858   15.838 1.00 65.71  ?  243 ALA   A C    1 
ATOM   1472 O  O    . ALA   A 1 216 ? 27.886  7.817   16.438 1.00 72.32  ?  243 ALA   A O    1 
ATOM   1473 C  CB   . ALA   A 1 216 ? 26.948  6.336   13.857 1.00 64.62  ?  243 ALA   A CB   1 
ATOM   1474 N  N    . VAL   A 1 217 ? 29.697  6.675   15.720 1.00 58.98  ?  244 VAL   A N    1 
ATOM   1475 C  CA   . VAL   A 1 217 ? 30.673  7.539   16.373 1.00 67.02  ?  244 VAL   A CA   1 
ATOM   1476 C  C    . VAL   A 1 217 ? 31.669  8.036   15.334 1.00 68.97  ?  244 VAL   A C    1 
ATOM   1477 O  O    . VAL   A 1 217 ? 32.250  7.237   14.593 1.00 63.48  ?  244 VAL   A O    1 
ATOM   1478 C  CB   . VAL   A 1 217 ? 31.410  6.809   17.512 1.00 69.55  ?  244 VAL   A CB   1 
ATOM   1479 C  CG1  . VAL   A 1 217 ? 32.533  7.679   18.062 1.00 70.55  ?  244 VAL   A CG1  1 
ATOM   1480 C  CG2  . VAL   A 1 217 ? 30.437  6.420   18.616 1.00 59.80  ?  244 VAL   A CG2  1 
ATOM   1481 N  N    . TYR   A 1 218 ? 31.864  9.351   15.284 1.00 71.19  ?  245 TYR   A N    1 
ATOM   1482 C  CA   . TYR   A 1 218 ? 32.920  9.967   14.491 1.00 65.56  ?  245 TYR   A CA   1 
ATOM   1483 C  C    . TYR   A 1 218 ? 34.066  10.323  15.430 1.00 67.43  ?  245 TYR   A C    1 
ATOM   1484 O  O    . TYR   A 1 218 ? 33.907  11.175  16.311 1.00 74.67  ?  245 TYR   A O    1 
ATOM   1485 C  CB   . TYR   A 1 218 ? 32.403  11.208  13.758 1.00 63.61  ?  245 TYR   A CB   1 
ATOM   1486 C  CG   . TYR   A 1 218 ? 33.405  11.870  12.827 1.00 70.10  ?  245 TYR   A CG   1 
ATOM   1487 C  CD1  . TYR   A 1 218 ? 34.459  12.629  13.324 1.00 67.47  ?  245 TYR   A CD1  1 
ATOM   1488 C  CD2  . TYR   A 1 218 ? 33.288  11.743  11.448 1.00 81.86  ?  245 TYR   A CD2  1 
ATOM   1489 C  CE1  . TYR   A 1 218 ? 35.370  13.234  12.478 1.00 84.93  ?  245 TYR   A CE1  1 
ATOM   1490 C  CE2  . TYR   A 1 218 ? 34.195  12.346  10.593 1.00 84.37  ?  245 TYR   A CE2  1 
ATOM   1491 C  CZ   . TYR   A 1 218 ? 35.233  13.091  11.113 1.00 93.20  ?  245 TYR   A CZ   1 
ATOM   1492 O  OH   . TYR   A 1 218 ? 36.139  13.693  10.269 1.00 84.76  ?  245 TYR   A OH   1 
ATOM   1493 N  N    . SER   A 1 219 ? 35.210  9.672   15.246 1.00 76.55  ?  246 SER   A N    1 
ATOM   1494 C  CA   . SER   A 1 219 ? 36.379  9.893   16.086 1.00 77.70  ?  246 SER   A CA   1 
ATOM   1495 C  C    . SER   A 1 219 ? 37.326  10.867  15.397 1.00 88.05  ?  246 SER   A C    1 
ATOM   1496 O  O    . SER   A 1 219 ? 37.648  10.699  14.217 1.00 87.21  ?  246 SER   A O    1 
ATOM   1497 C  CB   . SER   A 1 219 ? 37.097  8.575   16.382 1.00 79.63  ?  246 SER   A CB   1 
ATOM   1498 O  OG   . SER   A 1 219 ? 38.261  8.792   17.161 1.00 89.19  ?  246 SER   A OG   1 
ATOM   1499 N  N    . TYR   A 1 220 ? 37.769  11.882  16.138 1.00 84.99  ?  247 TYR   A N    1 
ATOM   1500 C  CA   . TYR   A 1 220 ? 38.665  12.917  15.621 1.00 90.21  ?  247 TYR   A CA   1 
ATOM   1501 C  C    . TYR   A 1 220 ? 39.808  13.105  16.615 1.00 93.37  ?  247 TYR   A C    1 
ATOM   1502 O  O    . TYR   A 1 220 ? 39.715  13.916  17.539 1.00 96.20  ?  247 TYR   A O    1 
ATOM   1503 C  CB   . TYR   A 1 220 ? 37.908  14.220  15.365 1.00 91.53  ?  247 TYR   A CB   1 
ATOM   1504 C  CG   . TYR   A 1 220 ? 38.794  15.414  15.071 1.00 101.53 ?  247 TYR   A CG   1 
ATOM   1505 C  CD1  . TYR   A 1 220 ? 39.789  15.345  14.106 1.00 103.42 ?  247 TYR   A CD1  1 
ATOM   1506 C  CD2  . TYR   A 1 220 ? 38.616  16.617  15.742 1.00 104.95 ?  247 TYR   A CD2  1 
ATOM   1507 C  CE1  . TYR   A 1 220 ? 40.598  16.435  13.832 1.00 112.21 ?  247 TYR   A CE1  1 
ATOM   1508 C  CE2  . TYR   A 1 220 ? 39.415  17.715  15.471 1.00 98.85  ?  247 TYR   A CE2  1 
ATOM   1509 C  CZ   . TYR   A 1 220 ? 40.403  17.618  14.514 1.00 109.70 ?  247 TYR   A CZ   1 
ATOM   1510 O  OH   . TYR   A 1 220 ? 41.200  18.707  14.242 1.00 118.07 ?  247 TYR   A OH   1 
ATOM   1511 N  N    . SER   A 1 221 ? 40.882  12.345  16.425 1.00 94.41  ?  248 SER   A N    1 
ATOM   1512 C  CA   . SER   A 1 221 ? 42.103  12.553  17.188 1.00 96.67  ?  248 SER   A CA   1 
ATOM   1513 C  C    . SER   A 1 221 ? 42.834  13.770  16.634 1.00 99.45  ?  248 SER   A C    1 
ATOM   1514 O  O    . SER   A 1 221 ? 43.029  13.886  15.420 1.00 100.15 ?  248 SER   A O    1 
ATOM   1515 C  CB   . SER   A 1 221 ? 42.995  11.314  17.126 1.00 95.53  ?  248 SER   A CB   1 
ATOM   1516 O  OG   . SER   A 1 221 ? 42.413  10.232  17.834 1.00 88.34  ?  248 SER   A OG   1 
ATOM   1517 N  N    . CYS   A 1 222 ? 43.231  14.680  17.526 1.00 106.61 ?  249 CYS   A N    1 
ATOM   1518 C  CA   . CYS   A 1 222 ? 43.796  15.950  17.081 1.00 115.70 ?  249 CYS   A CA   1 
ATOM   1519 C  C    . CYS   A 1 222 ? 45.135  15.753  16.380 1.00 122.69 ?  249 CYS   A C    1 
ATOM   1520 O  O    . CYS   A 1 222 ? 45.417  16.413  15.374 1.00 133.65 ?  249 CYS   A O    1 
ATOM   1521 C  CB   . CYS   A 1 222 ? 43.942  16.902  18.267 1.00 117.14 ?  249 CYS   A CB   1 
ATOM   1522 S  SG   . CYS   A 1 222 ? 42.503  17.963  18.550 1.00 112.26 ?  249 CYS   A SG   1 
ATOM   1523 N  N    . GLU   A 1 223 ? 45.969  14.852  16.891 1.00 117.03 ?  250 GLU   A N    1 
ATOM   1524 C  CA   . GLU   A 1 223 ? 47.268  14.585  16.284 1.00 122.26 ?  250 GLU   A CA   1 
ATOM   1525 C  C    . GLU   A 1 223 ? 47.797  13.217  16.700 1.00 119.18 ?  250 GLU   A C    1 
ATOM   1526 O  O    . GLU   A 1 223 ? 47.591  12.223  16.004 1.00 121.18 ?  250 GLU   A O    1 
ATOM   1527 C  CB   . GLU   A 1 223 ? 48.273  15.676  16.662 1.00 113.07 ?  250 GLU   A CB   1 
ATOM   1528 N  N    . LEU   A 1 235 ? 55.658  -2.614  21.122 1.00 118.92 ?  262 LEU   A N    1 
ATOM   1529 C  CA   . LEU   A 1 235 ? 55.101  -3.669  20.237 1.00 119.67 ?  262 LEU   A CA   1 
ATOM   1530 C  C    . LEU   A 1 235 ? 54.458  -4.753  21.105 1.00 127.92 ?  262 LEU   A C    1 
ATOM   1531 O  O    . LEU   A 1 235 ? 53.763  -5.621  20.547 1.00 132.67 ?  262 LEU   A O    1 
ATOM   1532 C  CB   . LEU   A 1 235 ? 56.233  -4.254  19.390 1.00 106.88 ?  262 LEU   A CB   1 
ATOM   1533 N  N    . GLU   A 1 236 ? 54.680  -4.694  22.417 1.00 131.24 ?  263 GLU   A N    1 
ATOM   1534 C  CA   . GLU   A 1 236 ? 54.151  -5.751  23.315 1.00 120.54 ?  263 GLU   A CA   1 
ATOM   1535 C  C    . GLU   A 1 236 ? 52.633  -5.827  23.148 1.00 124.19 ?  263 GLU   A C    1 
ATOM   1536 O  O    . GLU   A 1 236 ? 52.116  -6.946  22.982 1.00 120.55 ?  263 GLU   A O    1 
ATOM   1537 C  CB   . GLU   A 1 236 ? 54.518  -5.443  24.765 1.00 115.91 ?  263 GLU   A CB   1 
ATOM   1538 N  N    . GLY   A 1 237 ? 51.953  -4.680  23.184 1.00 108.96 ?  264 GLY   A N    1 
ATOM   1539 C  CA   . GLY   A 1 237 ? 50.484  -4.690  23.106 1.00 104.69 ?  264 GLY   A CA   1 
ATOM   1540 C  C    . GLY   A 1 237 ? 49.937  -3.495  22.356 1.00 101.28 ?  264 GLY   A C    1 
ATOM   1541 O  O    . GLY   A 1 237 ? 50.283  -3.340  21.176 1.00 103.36 ?  264 GLY   A O    1 
ATOM   1542 N  N    . ARG   A 1 238 ? 49.133  -2.667  23.024 1.00 92.18  ?  265 ARG   A N    1 
ATOM   1543 C  CA   . ARG   A 1 238 ? 48.469  -1.534  22.332 1.00 94.83  ?  265 ARG   A CA   1 
ATOM   1544 C  C    . ARG   A 1 238 ? 49.365  -0.299  22.312 1.00 91.97  ?  265 ARG   A C    1 
ATOM   1545 O  O    . ARG   A 1 238 ? 50.085  -0.072  23.294 1.00 94.10  ?  265 ARG   A O    1 
ATOM   1546 C  CB   . ARG   A 1 238 ? 47.144  -1.194  23.022 1.00 89.44  ?  265 ARG   A CB   1 
ATOM   1547 C  CG   . ARG   A 1 238 ? 47.262  -0.190  24.160 1.00 82.12  ?  265 ARG   A CG   1 
ATOM   1548 C  CD   . ARG   A 1 238 ? 46.377  1.025   23.964 1.00 83.56  ?  265 ARG   A CD   1 
ATOM   1549 N  NE   . ARG   A 1 238 ? 46.184  1.774   25.197 1.00 77.91  ?  265 ARG   A NE   1 
ATOM   1550 C  CZ   . ARG   A 1 238 ? 46.016  3.089   25.257 1.00 78.01  ?  265 ARG   A CZ   1 
ATOM   1551 N  NH1  . ARG   A 1 238 ? 46.154  3.822   24.168 1.00 80.50  ?  265 ARG   A NH1  1 
ATOM   1552 N  NH2  . ARG   A 1 238 ? 45.708  3.666   26.405 1.00 82.02  ?  265 ARG   A NH2  1 
ATOM   1553 N  N    . ASP   A 1 239 ? 49.321  0.455   21.218 1.00 91.08  ?  266 ASP   A N    1 
ATOM   1554 C  CA   . ASP   A 1 239 ? 50.055  1.712   21.162 1.00 96.19  ?  266 ASP   A CA   1 
ATOM   1555 C  C    . ASP   A 1 239 ? 49.428  2.713   22.124 1.00 92.77  ?  266 ASP   A C    1 
ATOM   1556 O  O    . ASP   A 1 239 ? 48.297  3.154   21.884 1.00 88.82  ?  266 ASP   A O    1 
ATOM   1557 C  CB   . ASP   A 1 239 ? 50.049  2.259   19.733 1.00 95.61  ?  266 ASP   A CB   1 
ATOM   1558 C  CG   . ASP   A 1 239 ? 50.970  3.457   19.551 1.00 104.62 ?  266 ASP   A CG   1 
ATOM   1559 O  OD1  . ASP   A 1 239 ? 51.542  3.944   20.549 1.00 104.83 ?  266 ASP   A OD1  1 
ATOM   1560 O  OD2  . ASP   A 1 239 ? 51.125  3.911   18.398 1.00 110.72 ?  266 ASP   A OD2  1 
ATOM   1561 N  N    . PRO   A 1 240 ? 50.108  3.102   23.207 1.00 97.35  ?  267 PRO   A N    1 
ATOM   1562 C  CA   . PRO   A 1 240 ? 49.486  4.034   24.162 1.00 94.16  ?  267 PRO   A CA   1 
ATOM   1563 C  C    . PRO   A 1 240 ? 49.334  5.443   23.619 1.00 93.22  ?  267 PRO   A C    1 
ATOM   1564 O  O    . PRO   A 1 240 ? 48.583  6.233   24.204 1.00 88.73  ?  267 PRO   A O    1 
ATOM   1565 C  CB   . PRO   A 1 240 ? 50.439  4.002   25.368 1.00 96.09  ?  267 PRO   A CB   1 
ATOM   1566 C  CG   . PRO   A 1 240 ? 51.446  2.910   25.081 1.00 85.42  ?  267 PRO   A CG   1 
ATOM   1567 C  CD   . PRO   A 1 240 ? 51.479  2.742   23.600 1.00 88.27  ?  267 PRO   A CD   1 
ATOM   1568 N  N    . ASP   A 1 241 ? 50.014  5.782   22.523 1.00 89.44  ?  268 ASP   A N    1 
ATOM   1569 C  CA   . ASP   A 1 241 ? 49.920  7.121   21.958 1.00 89.68  ?  268 ASP   A CA   1 
ATOM   1570 C  C    . ASP   A 1 241 ? 48.677  7.314   21.100 1.00 89.01  ?  268 ASP   A C    1 
ATOM   1571 O  O    . ASP   A 1 241 ? 48.269  8.459   20.875 1.00 95.86  ?  268 ASP   A O    1 
ATOM   1572 C  CB   . ASP   A 1 241 ? 51.166  7.428   21.123 1.00 94.84  ?  268 ASP   A CB   1 
ATOM   1573 C  CG   . ASP   A 1 241 ? 52.321  7.931   21.964 1.00 107.81 ?  268 ASP   A CG   1 
ATOM   1574 O  OD1  . ASP   A 1 241 ? 52.194  7.939   23.207 1.00 113.05 ?  268 ASP   A OD1  1 
ATOM   1575 O  OD2  . ASP   A 1 241 ? 53.354  8.320   21.382 1.00 115.43 ?  268 ASP   A OD2  1 
ATOM   1576 N  N    . ILE   A 1 242 ? 48.072  6.232   20.622 1.00 93.93  ?  269 ILE   A N    1 
ATOM   1577 C  CA   . ILE   A 1 242 ? 46.935  6.293   19.709 1.00 86.30  ?  269 ILE   A CA   1 
ATOM   1578 C  C    . ILE   A 1 242 ? 45.663  5.988   20.487 1.00 75.67  ?  269 ILE   A C    1 
ATOM   1579 O  O    . ILE   A 1 242 ? 45.647  5.104   21.354 1.00 72.54  ?  269 ILE   A O    1 
ATOM   1580 C  CB   . ILE   A 1 242 ? 47.120  5.312   18.532 1.00 82.32  ?  269 ILE   A CB   1 
ATOM   1581 C  CG1  . ILE   A 1 242 ? 48.345  5.674   17.679 1.00 74.25  ?  269 ILE   A CG1  1 
ATOM   1582 C  CG2  . ILE   A 1 242 ? 45.881  5.279   17.654 1.00 78.32  ?  269 ILE   A CG2  1 
ATOM   1583 C  CD1  . ILE   A 1 242 ? 48.727  7.146   17.677 1.00 91.67  ?  269 ILE   A CD1  1 
ATOM   1584 N  N    . TRP   A 1 243 ? 44.596  6.724   20.188 1.00 71.33  ?  270 TRP   A N    1 
ATOM   1585 C  CA   . TRP   A 1 243 ? 43.321  6.479   20.845 1.00 80.30  ?  270 TRP   A CA   1 
ATOM   1586 C  C    . TRP   A 1 243 ? 42.678  5.205   20.314 1.00 75.17  ?  270 TRP   A C    1 
ATOM   1587 O  O    . TRP   A 1 243 ? 42.739  4.907   19.118 1.00 68.56  ?  270 TRP   A O    1 
ATOM   1588 C  CB   . TRP   A 1 243 ? 42.379  7.664   20.645 1.00 77.38  ?  270 TRP   A CB   1 
ATOM   1589 C  CG   . TRP   A 1 243 ? 42.761  8.859   21.450 1.00 79.67  ?  270 TRP   A CG   1 
ATOM   1590 C  CD1  . TRP   A 1 243 ? 43.787  9.721   21.202 1.00 71.52  ?  270 TRP   A CD1  1 
ATOM   1591 C  CD2  . TRP   A 1 243 ? 42.128  9.320   22.649 1.00 78.88  ?  270 TRP   A CD2  1 
ATOM   1592 N  NE1  . TRP   A 1 243 ? 43.829  10.696  22.168 1.00 77.66  ?  270 TRP   A NE1  1 
ATOM   1593 C  CE2  . TRP   A 1 243 ? 42.821  10.473  23.068 1.00 83.91  ?  270 TRP   A CE2  1 
ATOM   1594 C  CE3  . TRP   A 1 243 ? 41.042  8.872   23.407 1.00 75.63  ?  270 TRP   A CE3  1 
ATOM   1595 C  CZ2  . TRP   A 1 243 ? 42.463  11.184  24.211 1.00 86.31  ?  270 TRP   A CZ2  1 
ATOM   1596 C  CZ3  . TRP   A 1 243 ? 40.687  9.580   24.539 1.00 81.31  ?  270 TRP   A CZ3  1 
ATOM   1597 C  CH2  . TRP   A 1 243 ? 41.395  10.723  24.932 1.00 85.77  ?  270 TRP   A CH2  1 
ATOM   1598 N  N    . HIS   A 1 244 ? 42.058  4.451   21.217 1.00 78.62  ?  271 HIS   A N    1 
ATOM   1599 C  CA   . HIS   A 1 244 ? 41.385  3.210   20.877 1.00 63.29  ?  271 HIS   A CA   1 
ATOM   1600 C  C    . HIS   A 1 244 ? 39.977  3.218   21.453 1.00 67.38  ?  271 HIS   A C    1 
ATOM   1601 O  O    . HIS   A 1 244 ? 39.636  4.033   22.313 1.00 72.01  ?  271 HIS   A O    1 
ATOM   1602 C  CB   . HIS   A 1 244 ? 42.137  1.983   21.414 1.00 65.54  ?  271 HIS   A CB   1 
ATOM   1603 C  CG   . HIS   A 1 244 ? 43.485  1.773   20.800 1.00 76.52  ?  271 HIS   A CG   1 
ATOM   1604 N  ND1  . HIS   A 1 244 ? 44.503  2.696   20.900 1.00 75.03  ?  271 HIS   A ND1  1 
ATOM   1605 C  CD2  . HIS   A 1 244 ? 43.987  0.735   20.089 1.00 66.17  ?  271 HIS   A CD2  1 
ATOM   1606 C  CE1  . HIS   A 1 244 ? 45.572  2.240   20.271 1.00 72.72  ?  271 HIS   A CE1  1 
ATOM   1607 N  NE2  . HIS   A 1 244 ? 45.284  1.052   19.771 1.00 72.27  ?  271 HIS   A NE2  1 
ATOM   1608 N  N    . VAL   A 1 245 ? 39.160  2.292   20.961 1.00 66.49  ?  272 VAL   A N    1 
ATOM   1609 C  CA   . VAL   A 1 245 ? 37.892  1.942   21.587 1.00 67.62  ?  272 VAL   A CA   1 
ATOM   1610 C  C    . VAL   A 1 245 ? 37.955  0.464   21.948 1.00 64.82  ?  272 VAL   A C    1 
ATOM   1611 O  O    . VAL   A 1 245 ? 38.346  -0.368  21.120 1.00 67.88  ?  272 VAL   A O    1 
ATOM   1612 C  CB   . VAL   A 1 245 ? 36.686  2.259   20.679 1.00 75.19  ?  272 VAL   A CB   1 
ATOM   1613 C  CG1  . VAL   A 1 245 ? 36.807  1.563   19.329 1.00 62.60  ?  272 VAL   A CG1  1 
ATOM   1614 C  CG2  . VAL   A 1 245 ? 35.386  1.876   21.373 1.00 62.30  ?  272 VAL   A CG2  1 
ATOM   1615 N  N    . GLY   A 1 246 ? 37.617  0.148   23.193 1.00 61.35  ?  273 GLY   A N    1 
ATOM   1616 C  CA   . GLY   A 1 246 ? 37.698  -1.208  23.695 1.00 61.18  ?  273 GLY   A CA   1 
ATOM   1617 C  C    . GLY   A 1 246 ? 36.348  -1.899  23.662 1.00 63.22  ?  273 GLY   A C    1 
ATOM   1618 O  O    . GLY   A 1 246 ? 35.304  -1.254  23.692 1.00 64.00  ?  273 GLY   A O    1 
ATOM   1619 N  N    . PHE   A 1 247 ? 36.379  -3.227  23.596 1.00 61.45  ?  274 PHE   A N    1 
ATOM   1620 C  CA   . PHE   A 1 247 ? 35.156  -4.013  23.559 1.00 61.69  ?  274 PHE   A CA   1 
ATOM   1621 C  C    . PHE   A 1 247 ? 35.366  -5.320  24.304 1.00 69.70  ?  274 PHE   A C    1 
ATOM   1622 O  O    . PHE   A 1 247 ? 36.433  -5.932  24.216 1.00 64.70  ?  274 PHE   A O    1 
ATOM   1623 C  CB   . PHE   A 1 247 ? 34.711  -4.292  22.119 1.00 58.79  ?  274 PHE   A CB   1 
ATOM   1624 C  CG   . PHE   A 1 247 ? 33.915  -3.177  21.508 1.00 56.45  ?  274 PHE   A CG   1 
ATOM   1625 C  CD1  . PHE   A 1 247 ? 32.579  -3.005  21.831 1.00 65.77  ?  274 PHE   A CD1  1 
ATOM   1626 C  CD2  . PHE   A 1 247 ? 34.503  -2.297  20.615 1.00 62.77  ?  274 PHE   A CD2  1 
ATOM   1627 C  CE1  . PHE   A 1 247 ? 31.842  -1.974  21.273 1.00 62.29  ?  274 PHE   A CE1  1 
ATOM   1628 C  CE2  . PHE   A 1 247 ? 33.773  -1.266  20.053 1.00 72.38  ?  274 PHE   A CE2  1 
ATOM   1629 C  CZ   . PHE   A 1 247 ? 32.440  -1.104  20.383 1.00 71.32  ?  274 PHE   A CZ   1 
ATOM   1630 N  N    . LYS   A 1 248 ? 34.337  -5.737  25.036 1.00 69.57  ?  275 LYS   A N    1 
ATOM   1631 C  CA   . LYS   A 1 248 ? 34.370  -6.977  25.794 1.00 66.56  ?  275 LYS   A CA   1 
ATOM   1632 C  C    . LYS   A 1 248 ? 32.954  -7.519  25.891 1.00 65.48  ?  275 LYS   A C    1 
ATOM   1633 O  O    . LYS   A 1 248 ? 31.976  -6.787  25.721 1.00 70.39  ?  275 LYS   A O    1 
ATOM   1634 C  CB   . LYS   A 1 248 ? 34.949  -6.769  27.198 1.00 66.47  ?  275 LYS   A CB   1 
ATOM   1635 C  CG   . LYS   A 1 248 ? 34.023  -5.993  28.128 1.00 66.34  ?  275 LYS   A CG   1 
ATOM   1636 C  CD   . LYS   A 1 248 ? 34.688  -5.683  29.458 1.00 69.21  ?  275 LYS   A CD   1 
ATOM   1637 C  CE   . LYS   A 1 248 ? 34.833  -6.937  30.304 1.00 81.30  ?  275 LYS   A CE   1 
ATOM   1638 N  NZ   . LYS   A 1 248 ? 33.522  -7.413  30.826 1.00 70.50  ?  275 LYS   A NZ   1 
ATOM   1639 N  N    . ILE   A 1 249 ? 32.850  -8.810  26.168 1.00 65.68  ?  276 ILE   A N    1 
ATOM   1640 C  CA   . ILE   A 1 249 ? 31.555  -9.418  26.442 1.00 71.86  ?  276 ILE   A CA   1 
ATOM   1641 C  C    . ILE   A 1 249 ? 31.182  -9.138  27.890 1.00 72.36  ?  276 ILE   A C    1 
ATOM   1642 O  O    . ILE   A 1 249 ? 32.038  -9.168  28.784 1.00 72.78  ?  276 ILE   A O    1 
ATOM   1643 C  CB   . ILE   A 1 249 ? 31.591  -10.929 26.153 1.00 63.17  ?  276 ILE   A CB   1 
ATOM   1644 C  CG1  . ILE   A 1 249 ? 32.063  -11.187 24.723 1.00 68.94  ?  276 ILE   A CG1  1 
ATOM   1645 C  CG2  . ILE   A 1 249 ? 30.219  -11.551 26.371 1.00 65.96  ?  276 ILE   A CG2  1 
ATOM   1646 C  CD1  . ILE   A 1 249 ? 32.270  -12.652 24.413 1.00 75.29  ?  276 ILE   A CD1  1 
ATOM   1647 N  N    . SER   A 1 250 ? 29.905  -8.846  28.126 1.00 61.80  ?  277 SER   A N    1 
ATOM   1648 C  CA   . SER   A 1 250 ? 29.436  -8.628  29.487 1.00 67.29  ?  277 SER   A CA   1 
ATOM   1649 C  C    . SER   A 1 250 ? 29.673  -9.872  30.332 1.00 66.43  ?  277 SER   A C    1 
ATOM   1650 O  O    . SER   A 1 250 ? 29.518  -11.002 29.860 1.00 81.83  ?  277 SER   A O    1 
ATOM   1651 C  CB   . SER   A 1 250 ? 27.952  -8.263  29.487 1.00 61.40  ?  277 SER   A CB   1 
ATOM   1652 O  OG   . SER   A 1 250 ? 27.611  -7.508  28.337 1.00 60.20  ?  277 SER   A OG   1 
ATOM   1653 N  N    . TRP   A 1 251 ? 30.072  -9.654  31.586 1.00 68.74  ?  278 TRP   A N    1 
ATOM   1654 C  CA   . TRP   A 1 251 ? 30.361  -10.691 32.574 1.00 69.28  ?  278 TRP   A CA   1 
ATOM   1655 C  C    . TRP   A 1 251 ? 31.578  -11.534 32.221 1.00 69.90  ?  278 TRP   A C    1 
ATOM   1656 O  O    . TRP   A 1 251 ? 31.852  -12.525 32.909 1.00 91.92  ?  278 TRP   A O    1 
ATOM   1657 C  CB   . TRP   A 1 251 ? 29.166  -11.628 32.790 1.00 64.31  ?  278 TRP   A CB   1 
ATOM   1658 C  CG   . TRP   A 1 251 ? 27.851  -10.930 32.919 1.00 75.08  ?  278 TRP   A CG   1 
ATOM   1659 C  CD1  . TRP   A 1 251 ? 26.923  -10.744 31.937 1.00 59.05  ?  278 TRP   A CD1  1 
ATOM   1660 C  CD2  . TRP   A 1 251 ? 27.305  -10.343 34.105 1.00 67.15  ?  278 TRP   A CD2  1 
ATOM   1661 N  NE1  . TRP   A 1 251 ? 25.837  -10.067 32.434 1.00 62.77  ?  278 TRP   A NE1  1 
ATOM   1662 C  CE2  . TRP   A 1 251 ? 26.046  -9.810  33.764 1.00 61.12  ?  278 TRP   A CE2  1 
ATOM   1663 C  CE3  . TRP   A 1 251 ? 27.760  -10.211 35.420 1.00 68.18  ?  278 TRP   A CE3  1 
ATOM   1664 C  CZ2  . TRP   A 1 251 ? 25.236  -9.158  34.691 1.00 72.47  ?  278 TRP   A CZ2  1 
ATOM   1665 C  CZ3  . TRP   A 1 251 ? 26.955  -9.562  36.338 1.00 76.63  ?  278 TRP   A CZ3  1 
ATOM   1666 C  CH2  . TRP   A 1 251 ? 25.708  -9.043  35.969 1.00 72.93  ?  278 TRP   A CH2  1 
ATOM   1667 N  N    . ASP   A 1 252 ? 32.324  -11.176 31.177 1.00 73.84  ?  279 ASP   A N    1 
ATOM   1668 C  CA   . ASP   A 1 252 ? 33.384  -12.030 30.650 1.00 80.21  ?  279 ASP   A CA   1 
ATOM   1669 C  C    . ASP   A 1 252 ? 34.695  -11.259 30.606 1.00 73.63  ?  279 ASP   A C    1 
ATOM   1670 O  O    . ASP   A 1 252 ? 34.865  -10.360 29.776 1.00 77.37  ?  279 ASP   A O    1 
ATOM   1671 C  CB   . ASP   A 1 252 ? 33.019  -12.555 29.261 1.00 91.92  ?  279 ASP   A CB   1 
ATOM   1672 C  CG   . ASP   A 1 252 ? 33.868  -13.738 28.841 1.00 80.30  ?  279 ASP   A CG   1 
ATOM   1673 O  OD1  . ASP   A 1 252 ? 34.879  -14.024 29.517 1.00 83.92  ?  279 ASP   A OD1  1 
ATOM   1674 O  OD2  . ASP   A 1 252 ? 33.520  -14.387 27.833 1.00 87.55  ?  279 ASP   A OD2  1 
ATOM   1675 N  N    . ILE   A 1 253 ? 35.621  -11.618 31.494 1.00 67.70  ?  280 ILE   A N    1 
ATOM   1676 C  CA   . ILE   A 1 253 ? 37.002  -11.157 31.422 1.00 76.55  ?  280 ILE   A CA   1 
ATOM   1677 C  C    . ILE   A 1 253 ? 37.947  -12.258 30.981 1.00 80.30  ?  280 ILE   A C    1 
ATOM   1678 O  O    . ILE   A 1 253 ? 39.161  -12.020 30.888 1.00 84.77  ?  280 ILE   A O    1 
ATOM   1679 C  CB   . ILE   A 1 253 ? 37.468  -10.556 32.761 1.00 68.32  ?  280 ILE   A CB   1 
ATOM   1680 C  CG1  . ILE   A 1 253 ? 37.363  -11.591 33.882 1.00 74.42  ?  280 ILE   A CG1  1 
ATOM   1681 C  CG2  . ILE   A 1 253 ? 36.656  -9.315  33.097 1.00 72.69  ?  280 ILE   A CG2  1 
ATOM   1682 C  CD1  . ILE   A 1 253 ? 38.043  -11.166 35.166 1.00 65.49  ?  280 ILE   A CD1  1 
ATOM   1683 N  N    . GLU   A 1 254 ? 37.434  -13.461 30.712 1.00 77.89  ?  281 GLU   A N    1 
ATOM   1684 C  CA   . GLU   A 1 254 ? 38.269  -14.535 30.186 1.00 89.75  ?  281 GLU   A CA   1 
ATOM   1685 C  C    . GLU   A 1 254 ? 38.426  -14.427 28.675 1.00 91.28  ?  281 GLU   A C    1 
ATOM   1686 O  O    . GLU   A 1 254 ? 39.525  -14.633 28.147 1.00 95.30  ?  281 GLU   A O    1 
ATOM   1687 C  CB   . GLU   A 1 254 ? 37.681  -15.894 30.564 1.00 92.74  ?  281 GLU   A CB   1 
ATOM   1688 C  CG   . GLU   A 1 254 ? 37.479  -16.091 32.054 1.00 104.05 ?  281 GLU   A CG   1 
ATOM   1689 C  CD   . GLU   A 1 254 ? 37.857  -17.485 32.507 1.00 123.46 ?  281 GLU   A CD   1 
ATOM   1690 O  OE1  . GLU   A 1 254 ? 37.140  -18.442 32.147 1.00 135.15 ?  281 GLU   A OE1  1 
ATOM   1691 O  OE2  . GLU   A 1 254 ? 38.874  -17.625 33.219 1.00 132.85 ?  281 GLU   A OE2  1 
ATOM   1692 N  N    . THR   A 1 255 ? 37.347  -14.118 27.969 1.00 84.06  ?  282 THR   A N    1 
ATOM   1693 C  CA   . THR   A 1 255 ? 37.431  -13.892 26.532 1.00 81.42  ?  282 THR   A CA   1 
ATOM   1694 C  C    . THR   A 1 255 ? 38.216  -12.615 26.272 1.00 81.80  ?  282 THR   A C    1 
ATOM   1695 O  O    . THR   A 1 255 ? 37.818  -11.546 26.755 1.00 92.12  ?  282 THR   A O    1 
ATOM   1696 C  CB   . THR   A 1 255 ? 36.038  -13.792 25.915 1.00 85.52  ?  282 THR   A CB   1 
ATOM   1697 O  OG1  . THR   A 1 255 ? 35.238  -14.897 26.351 1.00 90.82  ?  282 THR   A OG1  1 
ATOM   1698 C  CG2  . THR   A 1 255 ? 36.128  -13.807 24.397 1.00 83.38  ?  282 THR   A CG2  1 
ATOM   1699 N  N    . PRO   A 1 256 ? 39.328  -12.673 25.542 1.00 96.33  ?  283 PRO   A N    1 
ATOM   1700 C  CA   . PRO   A 1 256 ? 40.125  -11.460 25.315 1.00 84.72  ?  283 PRO   A CA   1 
ATOM   1701 C  C    . PRO   A 1 256 ? 39.328  -10.401 24.567 1.00 82.41  ?  283 PRO   A C    1 
ATOM   1702 O  O    . PRO   A 1 256 ? 38.591  -10.699 23.624 1.00 88.03  ?  283 PRO   A O    1 
ATOM   1703 C  CB   . PRO   A 1 256 ? 41.314  -11.958 24.485 1.00 88.87  ?  283 PRO   A CB   1 
ATOM   1704 C  CG   . PRO   A 1 256 ? 40.934  -13.317 23.996 1.00 90.44  ?  283 PRO   A CG   1 
ATOM   1705 C  CD   . PRO   A 1 256 ? 39.947  -13.875 24.962 1.00 87.66  ?  283 PRO   A CD   1 
ATOM   1706 N  N    . GLY   A 1 257 ? 39.482  -9.149  25.005 1.00 67.89  ?  284 GLY   A N    1 
ATOM   1707 C  CA   . GLY   A 1 257 ? 38.769  -8.046  24.398 1.00 69.43  ?  284 GLY   A CA   1 
ATOM   1708 C  C    . GLY   A 1 257 ? 39.506  -7.447  23.213 1.00 66.57  ?  284 GLY   A C    1 
ATOM   1709 O  O    . GLY   A 1 257 ? 40.679  -7.725  22.971 1.00 82.05  ?  284 GLY   A O    1 
ATOM   1710 N  N    . LEU   A 1 258 ? 38.790  -6.607  22.471 1.00 58.36  ?  285 LEU   A N    1 
ATOM   1711 C  CA   . LEU   A 1 258 ? 39.325  -5.960  21.282 1.00 58.86  ?  285 LEU   A CA   1 
ATOM   1712 C  C    . LEU   A 1 258 ? 39.648  -4.500  21.564 1.00 68.01  ?  285 LEU   A C    1 
ATOM   1713 O  O    . LEU   A 1 258 ? 38.855  -3.784  22.181 1.00 70.36  ?  285 LEU   A O    1 
ATOM   1714 C  CB   . LEU   A 1 258 ? 38.339  -6.043  20.115 1.00 63.95  ?  285 LEU   A CB   1 
ATOM   1715 C  CG   . LEU   A 1 258 ? 38.030  -7.410  19.508 1.00 74.91  ?  285 LEU   A CG   1 
ATOM   1716 C  CD1  . LEU   A 1 258 ? 37.208  -7.232  18.241 1.00 66.75  ?  285 LEU   A CD1  1 
ATOM   1717 C  CD2  . LEU   A 1 258 ? 39.308  -8.181  19.221 1.00 58.42  ?  285 LEU   A CD2  1 
ATOM   1718 N  N    . ALA   A 1 259 ? 40.818  -4.067  21.104 1.00 71.76  ?  286 ALA   A N    1 
ATOM   1719 C  CA   . ALA   A 1 259 ? 41.223  -2.666  21.133 1.00 69.11  ?  286 ALA   A CA   1 
ATOM   1720 C  C    . ALA   A 1 259 ? 41.318  -2.188  19.690 1.00 73.00  ?  286 ALA   A C    1 
ATOM   1721 O  O    . ALA   A 1 259 ? 42.238  -2.577  18.962 1.00 76.44  ?  286 ALA   A O    1 
ATOM   1722 C  CB   . ALA   A 1 259 ? 42.552  -2.488  21.864 1.00 81.65  ?  286 ALA   A CB   1 
ATOM   1723 N  N    . ILE   A 1 260 ? 40.368  -1.355  19.276 1.00 70.01  ?  287 ILE   A N    1 
ATOM   1724 C  CA   . ILE   A 1 260 ? 40.270  -0.896  17.893 1.00 70.30  ?  287 ILE   A CA   1 
ATOM   1725 C  C    . ILE   A 1 260 ? 40.943  0.473   17.809 1.00 79.97  ?  287 ILE   A C    1 
ATOM   1726 O  O    . ILE   A 1 260 ? 40.420  1.443   18.382 1.00 73.51  ?  287 ILE   A O    1 
ATOM   1727 C  CB   . ILE   A 1 260 ? 38.813  -0.825  17.418 1.00 75.92  ?  287 ILE   A CB   1 
ATOM   1728 C  CG1  . ILE   A 1 260 ? 38.068  -2.135  17.701 1.00 75.93  ?  287 ILE   A CG1  1 
ATOM   1729 C  CG2  . ILE   A 1 260 ? 38.759  -0.501  15.935 1.00 80.18  ?  287 ILE   A CG2  1 
ATOM   1730 C  CD1  . ILE   A 1 260 ? 38.859  -3.394  17.406 1.00 71.13  ?  287 ILE   A CD1  1 
ATOM   1731 N  N    . PRO   A 1 261 ? 42.079  0.601   17.123 1.00 77.38  ?  288 PRO   A N    1 
ATOM   1732 C  CA   . PRO   A 1 261 ? 42.717  1.917   16.997 1.00 80.58  ?  288 PRO   A CA   1 
ATOM   1733 C  C    . PRO   A 1 261 ? 41.876  2.858   16.150 1.00 71.60  ?  288 PRO   A C    1 
ATOM   1734 O  O    . PRO   A 1 261 ? 41.303  2.465   15.130 1.00 74.87  ?  288 PRO   A O    1 
ATOM   1735 C  CB   . PRO   A 1 261 ? 44.058  1.603   16.320 1.00 70.80  ?  288 PRO   A CB   1 
ATOM   1736 C  CG   . PRO   A 1 261 ? 44.262  0.127   16.521 1.00 71.33  ?  288 PRO   A CG   1 
ATOM   1737 C  CD   . PRO   A 1 261 ? 42.887  -0.462  16.507 1.00 69.99  ?  288 PRO   A CD   1 
ATOM   1738 N  N    . LEU   A 1 262 ? 41.807  4.115   16.583 1.00 65.86  ?  289 LEU   A N    1 
ATOM   1739 C  CA   . LEU   A 1 262 ? 41.011  5.137   15.917 1.00 81.06  ?  289 LEU   A CA   1 
ATOM   1740 C  C    . LEU   A 1 262 ? 41.923  6.282   15.505 1.00 87.76  ?  289 LEU   A C    1 
ATOM   1741 O  O    . LEU   A 1 262 ? 42.625  6.854   16.345 1.00 77.86  ?  289 LEU   A O    1 
ATOM   1742 C  CB   . LEU   A 1 262 ? 39.892  5.638   16.831 1.00 68.16  ?  289 LEU   A CB   1 
ATOM   1743 C  CG   . LEU   A 1 262 ? 38.824  4.596   17.171 1.00 72.55  ?  289 LEU   A CG   1 
ATOM   1744 C  CD1  . LEU   A 1 262 ? 37.955  5.068   18.325 1.00 67.84  ?  289 LEU   A CD1  1 
ATOM   1745 C  CD2  . LEU   A 1 262 ? 37.977  4.279   15.947 1.00 67.21  ?  289 LEU   A CD2  1 
ATOM   1746 N  N    . HIS   A 1 263 ? 41.913  6.609   14.218 1.00 82.26  ?  290 HIS   A N    1 
ATOM   1747 C  CA   . HIS   A 1 263 ? 42.716  7.690   13.676 1.00 85.33  ?  290 HIS   A CA   1 
ATOM   1748 C  C    . HIS   A 1 263 ? 41.837  8.917   13.443 1.00 87.86  ?  290 HIS   A C    1 
ATOM   1749 O  O    . HIS   A 1 263 ? 40.674  8.966   13.854 1.00 98.74  ?  290 HIS   A O    1 
ATOM   1750 C  CB   . HIS   A 1 263 ? 43.414  7.230   12.394 1.00 93.36  ?  290 HIS   A CB   1 
ATOM   1751 C  CG   . HIS   A 1 263 ? 44.313  6.048   12.587 1.00 103.55 ?  290 HIS   A CG   1 
ATOM   1752 N  ND1  . HIS   A 1 263 ? 44.119  4.850   11.934 1.00 103.14 ?  290 HIS   A ND1  1 
ATOM   1753 C  CD2  . HIS   A 1 263 ? 45.412  5.881   13.360 1.00 97.09  ?  290 HIS   A CD2  1 
ATOM   1754 C  CE1  . HIS   A 1 263 ? 45.059  3.996   12.297 1.00 95.18  ?  290 HIS   A CE1  1 
ATOM   1755 N  NE2  . HIS   A 1 263 ? 45.857  4.597   13.161 1.00 94.54  ?  290 HIS   A NE2  1 
ATOM   1756 N  N    . GLN   A 1 264 ? 42.395  9.923   12.774 1.00 97.69  ?  291 GLN   A N    1 
ATOM   1757 C  CA   . GLN   A 1 264 ? 41.679  11.169  12.509 1.00 96.43  ?  291 GLN   A CA   1 
ATOM   1758 C  C    . GLN   A 1 264 ? 40.653  10.933  11.409 1.00 96.87  ?  291 GLN   A C    1 
ATOM   1759 O  O    . GLN   A 1 264 ? 40.994  10.863  10.227 1.00 100.23 ?  291 GLN   A O    1 
ATOM   1760 C  CB   . GLN   A 1 264 ? 42.660  12.270  12.122 1.00 104.18 ?  291 GLN   A CB   1 
ATOM   1761 C  CG   . GLN   A 1 264 ? 42.028  13.644  11.977 1.00 104.36 ?  291 GLN   A CG   1 
ATOM   1762 C  CD   . GLN   A 1 264 ? 43.043  14.723  11.654 1.00 113.44 ?  291 GLN   A CD   1 
ATOM   1763 O  OE1  . GLN   A 1 264 ? 43.835  15.122  12.507 1.00 119.31 ?  291 GLN   A OE1  1 
ATOM   1764 N  NE2  . GLN   A 1 264 ? 43.023  15.200  10.415 1.00 111.69 ?  291 GLN   A NE2  1 
ATOM   1765 N  N    . GLY   A 1 265 ? 39.384  10.808  11.795 1.00 91.85  ?  292 GLY   A N    1 
ATOM   1766 C  CA   . GLY   A 1 265 ? 38.298  10.661  10.846 1.00 85.80  ?  292 GLY   A CA   1 
ATOM   1767 C  C    . GLY   A 1 265 ? 37.670  9.285   10.782 1.00 85.60  ?  292 GLY   A C    1 
ATOM   1768 O  O    . GLY   A 1 265 ? 36.750  9.087   9.980  1.00 88.20  ?  292 GLY   A O    1 
ATOM   1769 N  N    . ASP   A 1 266 ? 38.127  8.330   11.587 1.00 85.50  ?  293 ASP   A N    1 
ATOM   1770 C  CA   . ASP   A 1 266 ? 37.537  7.000   11.573 1.00 84.75  ?  293 ASP   A CA   1 
ATOM   1771 C  C    . ASP   A 1 266 ? 36.154  7.013   12.217 1.00 75.38  ?  293 ASP   A C    1 
ATOM   1772 O  O    . ASP   A 1 266 ? 35.884  7.774   13.150 1.00 72.06  ?  293 ASP   A O    1 
ATOM   1773 C  CB   . ASP   A 1 266 ? 38.439  6.002   12.301 1.00 81.72  ?  293 ASP   A CB   1 
ATOM   1774 C  CG   . ASP   A 1 266 ? 39.638  5.581   11.471 1.00 92.62  ?  293 ASP   A CG   1 
ATOM   1775 O  OD1  . ASP   A 1 266 ? 39.770  6.056   10.324 1.00 88.57  ?  293 ASP   A OD1  1 
ATOM   1776 O  OD2  . ASP   A 1 266 ? 40.448  4.769   11.968 1.00 92.09  ?  293 ASP   A OD2  1 
ATOM   1777 N  N    . CYS   A 1 267 ? 35.273  6.157   11.702 1.00 75.97  ?  294 CYS   A N    1 
ATOM   1778 C  CA   . CYS   A 1 267 ? 33.928  5.988   12.238 1.00 73.57  ?  294 CYS   A CA   1 
ATOM   1779 C  C    . CYS   A 1 267 ? 33.686  4.516   12.526 1.00 74.27  ?  294 CYS   A C    1 
ATOM   1780 O  O    . CYS   A 1 267 ? 33.954  3.665   11.674 1.00 74.27  ?  294 CYS   A O    1 
ATOM   1781 C  CB   . CYS   A 1 267 ? 32.863  6.506   11.264 1.00 74.73  ?  294 CYS   A CB   1 
ATOM   1782 S  SG   . CYS   A 1 267 ? 33.026  8.239   10.797 1.00 84.33  ?  294 CYS   A SG   1 
ATOM   1783 N  N    . TYR   A 1 268 ? 33.178  4.217   13.720 1.00 67.81  ?  295 TYR   A N    1 
ATOM   1784 C  CA   . TYR   A 1 268 ? 32.763  2.866   14.061 1.00 67.94  ?  295 TYR   A CA   1 
ATOM   1785 C  C    . TYR   A 1 268 ? 31.286  2.860   14.433 1.00 68.96  ?  295 TYR   A C    1 
ATOM   1786 O  O    . TYR   A 1 268 ? 30.731  3.875   14.864 1.00 65.29  ?  295 TYR   A O    1 
ATOM   1787 C  CB   . TYR   A 1 268 ? 33.617  2.271   15.198 1.00 62.56  ?  295 TYR   A CB   1 
ATOM   1788 C  CG   . TYR   A 1 268 ? 33.404  2.864   16.575 1.00 66.13  ?  295 TYR   A CG   1 
ATOM   1789 C  CD1  . TYR   A 1 268 ? 34.160  3.944   17.012 1.00 66.00  ?  295 TYR   A CD1  1 
ATOM   1790 C  CD2  . TYR   A 1 268 ? 32.473  2.320   17.452 1.00 71.32  ?  295 TYR   A CD2  1 
ATOM   1791 C  CE1  . TYR   A 1 268 ? 33.980  4.477   18.276 1.00 71.68  ?  295 TYR   A CE1  1 
ATOM   1792 C  CE2  . TYR   A 1 268 ? 32.284  2.849   18.715 1.00 65.24  ?  295 TYR   A CE2  1 
ATOM   1793 C  CZ   . TYR   A 1 268 ? 33.040  3.927   19.122 1.00 62.49  ?  295 TYR   A CZ   1 
ATOM   1794 O  OH   . TYR   A 1 268 ? 32.856  4.454   20.379 1.00 74.72  ?  295 TYR   A OH   1 
ATOM   1795 N  N    . PHE   A 1 269 ? 30.652  1.703   14.245 1.00 65.13  ?  296 PHE   A N    1 
ATOM   1796 C  CA   . PHE   A 1 269 ? 29.211  1.555   14.394 1.00 64.02  ?  296 PHE   A CA   1 
ATOM   1797 C  C    . PHE   A 1 269 ? 28.913  0.370   15.299 1.00 69.32  ?  296 PHE   A C    1 
ATOM   1798 O  O    . PHE   A 1 269 ? 29.475  -0.714  15.111 1.00 68.70  ?  296 PHE   A O    1 
ATOM   1799 C  CB   . PHE   A 1 269 ? 28.521  1.348   13.036 1.00 66.79  ?  296 PHE   A CB   1 
ATOM   1800 C  CG   . PHE   A 1 269 ? 28.745  2.466   12.048 1.00 70.46  ?  296 PHE   A CG   1 
ATOM   1801 C  CD1  . PHE   A 1 269 ? 29.975  2.644   11.434 1.00 74.92  ?  296 PHE   A CD1  1 
ATOM   1802 C  CD2  . PHE   A 1 269 ? 27.712  3.330   11.721 1.00 82.95  ?  296 PHE   A CD2  1 
ATOM   1803 C  CE1  . PHE   A 1 269 ? 30.175  3.667   10.526 1.00 71.81  ?  296 PHE   A CE1  1 
ATOM   1804 C  CE2  . PHE   A 1 269 ? 27.906  4.355   10.812 1.00 80.25  ?  296 PHE   A CE2  1 
ATOM   1805 C  CZ   . PHE   A 1 269 ? 29.139  4.523   10.214 1.00 70.23  ?  296 PHE   A CZ   1 
ATOM   1806 N  N    . MET   A 1 270 ? 28.028  0.573   16.272 1.00 63.09  ?  297 MET   A N    1 
ATOM   1807 C  CA   . MET   A 1 270 ? 27.511  -0.504  17.110 1.00 62.91  ?  297 MET   A CA   1 
ATOM   1808 C  C    . MET   A 1 270 ? 26.089  -0.810  16.656 1.00 61.83  ?  297 MET   A C    1 
ATOM   1809 O  O    . MET   A 1 270 ? 25.172  -0.019  16.896 1.00 67.46  ?  297 MET   A O    1 
ATOM   1810 C  CB   . MET   A 1 270 ? 27.546  -0.124  18.589 1.00 62.92  ?  297 MET   A CB   1 
ATOM   1811 C  CG   . MET   A 1 270 ? 28.864  0.465   19.055 1.00 70.72  ?  297 MET   A CG   1 
ATOM   1812 S  SD   . MET   A 1 270 ? 29.014  0.439   20.851 1.00 86.34  ?  297 MET   A SD   1 
ATOM   1813 C  CE   . MET   A 1 270 ? 27.454  1.174   21.332 1.00 67.01  ?  297 MET   A CE   1 
ATOM   1814 N  N    . LEU   A 1 271 ? 25.908  -1.953  16.005 1.00 57.30  ?  298 LEU   A N    1 
ATOM   1815 C  CA   . LEU   A 1 271 ? 24.634  -2.315  15.404 1.00 62.90  ?  298 LEU   A CA   1 
ATOM   1816 C  C    . LEU   A 1 271 ? 23.844  -3.253  16.308 1.00 71.52  ?  298 LEU   A C    1 
ATOM   1817 O  O    . LEU   A 1 271 ? 24.412  -4.060  17.048 1.00 66.76  ?  298 LEU   A O    1 
ATOM   1818 C  CB   . LEU   A 1 271 ? 24.843  -2.983  14.044 1.00 68.34  ?  298 LEU   A CB   1 
ATOM   1819 C  CG   . LEU   A 1 271 ? 25.725  -2.266  13.024 1.00 71.58  ?  298 LEU   A CG   1 
ATOM   1820 C  CD1  . LEU   A 1 271 ? 25.665  -2.982  11.684 1.00 60.86  ?  298 LEU   A CD1  1 
ATOM   1821 C  CD2  . LEU   A 1 271 ? 25.302  -0.813  12.876 1.00 67.49  ?  298 LEU   A CD2  1 
ATOM   1822 N  N    . ASP   A 1 272 ? 22.520  -3.130  16.234 1.00 77.10  ?  299 ASP   A N    1 
ATOM   1823 C  CA   . ASP   A 1 272 ? 21.571  -4.088  16.819 1.00 68.93  ?  299 ASP   A CA   1 
ATOM   1824 C  C    . ASP   A 1 272 ? 21.820  -4.166  18.325 1.00 75.32  ?  299 ASP   A C    1 
ATOM   1825 O  O    . ASP   A 1 272 ? 21.843  -3.118  18.991 1.00 65.76  ?  299 ASP   A O    1 
ATOM   1826 C  CB   . ASP   A 1 272 ? 21.690  -5.404  16.059 1.00 73.29  ?  299 ASP   A CB   1 
ATOM   1827 C  CG   . ASP   A 1 272 ? 20.494  -6.311  16.267 1.00 79.54  ?  299 ASP   A CG   1 
ATOM   1828 O  OD1  . ASP   A 1 272 ? 19.360  -5.882  15.965 1.00 89.38  ?  299 ASP   A OD1  1 
ATOM   1829 O  OD2  . ASP   A 1 272 ? 20.690  -7.456  16.726 1.00 76.16  ?  299 ASP   A OD2  1 
ATOM   1830 N  N    . ASP   A 1 273 ? 22.011  -5.354  18.898 1.00 75.93  ?  300 ASP   A N    1 
ATOM   1831 C  CA   . ASP   A 1 273 ? 22.141  -5.534  20.336 1.00 75.31  ?  300 ASP   A CA   1 
ATOM   1832 C  C    . ASP   A 1 273 ? 23.592  -5.523  20.810 1.00 73.02  ?  300 ASP   A C    1 
ATOM   1833 O  O    . ASP   A 1 273 ? 23.876  -6.009  21.912 1.00 70.95  ?  300 ASP   A O    1 
ATOM   1834 C  CB   . ASP   A 1 273 ? 21.457  -6.836  20.761 1.00 75.54  ?  300 ASP   A CB   1 
ATOM   1835 C  CG   . ASP   A 1 273 ? 22.035  -8.053  20.061 1.00 80.19  ?  300 ASP   A CG   1 
ATOM   1836 O  OD1  . ASP   A 1 273 ? 22.776  -7.875  19.072 1.00 82.34  ?  300 ASP   A OD1  1 
ATOM   1837 O  OD2  . ASP   A 1 273 ? 21.746  -9.187  20.496 1.00 79.73  ?  300 ASP   A OD2  1 
ATOM   1838 N  N    . LEU   A 1 274 ? 24.511  -4.980  20.008 1.00 58.79  ?  301 LEU   A N    1 
ATOM   1839 C  CA   . LEU   A 1 274 ? 25.914  -4.944  20.413 1.00 62.02  ?  301 LEU   A CA   1 
ATOM   1840 C  C    . LEU   A 1 274 ? 26.106  -4.111  21.673 1.00 62.71  ?  301 LEU   A C    1 
ATOM   1841 O  O    . LEU   A 1 274 ? 26.916  -4.460  22.541 1.00 63.72  ?  301 LEU   A O    1 
ATOM   1842 C  CB   . LEU   A 1 274 ? 26.777  -4.398  19.276 1.00 65.25  ?  301 LEU   A CB   1 
ATOM   1843 C  CG   . LEU   A 1 274 ? 28.288  -4.444  19.511 1.00 65.22  ?  301 LEU   A CG   1 
ATOM   1844 C  CD1  . LEU   A 1 274 ? 28.777  -5.880  19.611 1.00 69.97  ?  301 LEU   A CD1  1 
ATOM   1845 C  CD2  . LEU   A 1 274 ? 29.029  -3.696  18.415 1.00 76.59  ?  301 LEU   A CD2  1 
ATOM   1846 N  N    . ASN   A 1 275 ? 25.368  -3.005  21.794 1.00 70.85  ?  302 ASN   A N    1 
ATOM   1847 C  CA   . ASN   A 1 275 ? 25.472  -2.163  22.978 1.00 61.94  ?  302 ASN   A CA   1 
ATOM   1848 C  C    . ASN   A 1 275 ? 24.963  -2.863  24.232 1.00 59.67  ?  302 ASN   A C    1 
ATOM   1849 O  O    . ASN   A 1 275 ? 25.377  -2.500  25.338 1.00 61.48  ?  302 ASN   A O    1 
ATOM   1850 C  CB   . ASN   A 1 275 ? 24.706  -0.857  22.760 1.00 62.83  ?  302 ASN   A CB   1 
ATOM   1851 C  CG   . ASN   A 1 275 ? 24.869  0.115   23.913 1.00 60.67  ?  302 ASN   A CG   1 
ATOM   1852 O  OD1  . ASN   A 1 275 ? 25.982  0.521   24.246 1.00 70.38  ?  302 ASN   A OD1  1 
ATOM   1853 N  ND2  . ASN   A 1 275 ? 23.756  0.489   24.532 1.00 73.49  ?  302 ASN   A ND2  1 
ATOM   1854 N  N    . ALA   A 1 276 ? 24.088  -3.858  24.087 1.00 57.19  ?  303 ALA   A N    1 
ATOM   1855 C  CA   . ALA   A 1 276 ? 23.517  -4.547  25.238 1.00 54.89  ?  303 ALA   A CA   1 
ATOM   1856 C  C    . ALA   A 1 276 ? 24.332  -5.764  25.656 1.00 57.39  ?  303 ALA   A C    1 
ATOM   1857 O  O    . ALA   A 1 276 ? 24.537  -5.988  26.854 1.00 81.34  ?  303 ALA   A O    1 
ATOM   1858 C  CB   . ALA   A 1 276 ? 22.076  -4.966  24.937 1.00 52.66  ?  303 ALA   A CB   1 
ATOM   1859 N  N    . THR   A 1 277 ? 24.800  -6.560  24.696 1.00 61.56  ?  304 THR   A N    1 
ATOM   1860 C  CA   . THR   A 1 277 ? 25.556  -7.764  25.014 1.00 64.64  ?  304 THR   A CA   1 
ATOM   1861 C  C    . THR   A 1 277 ? 27.026  -7.489  25.295 1.00 69.93  ?  304 THR   A C    1 
ATOM   1862 O  O    . THR   A 1 277 ? 27.715  -8.372  25.818 1.00 64.06  ?  304 THR   A O    1 
ATOM   1863 C  CB   . THR   A 1 277 ? 25.447  -8.777  23.871 1.00 74.25  ?  304 THR   A CB   1 
ATOM   1864 O  OG1  . THR   A 1 277 ? 25.900  -8.175  22.652 1.00 70.34  ?  304 THR   A OG1  1 
ATOM   1865 C  CG2  . THR   A 1 277 ? 24.006  -9.234  23.698 1.00 54.52  ?  304 THR   A CG2  1 
ATOM   1866 N  N    . HIS   A 1 278 ? 27.524  -6.302  24.960 1.00 68.57  ?  305 HIS   A N    1 
ATOM   1867 C  CA   . HIS   A 1 278 ? 28.932  -5.980  25.119 1.00 65.43  ?  305 HIS   A CA   1 
ATOM   1868 C  C    . HIS   A 1 278 ? 29.088  -4.641  25.822 1.00 69.26  ?  305 HIS   A C    1 
ATOM   1869 O  O    . HIS   A 1 278 ? 28.235  -3.757  25.710 1.00 67.30  ?  305 HIS   A O    1 
ATOM   1870 C  CB   . HIS   A 1 278 ? 29.661  -5.933  23.765 1.00 70.15  ?  305 HIS   A CB   1 
ATOM   1871 C  CG   . HIS   A 1 278 ? 29.699  -7.247  23.048 1.00 71.46  ?  305 HIS   A CG   1 
ATOM   1872 N  ND1  . HIS   A 1 278 ? 28.560  -7.928  22.675 1.00 79.36  ?  305 HIS   A ND1  1 
ATOM   1873 C  CD2  . HIS   A 1 278 ? 30.742  -8.010  22.644 1.00 84.91  ?  305 HIS   A CD2  1 
ATOM   1874 C  CE1  . HIS   A 1 278 ? 28.900  -9.051  22.067 1.00 82.28  ?  305 HIS   A CE1  1 
ATOM   1875 N  NE2  . HIS   A 1 278 ? 30.218  -9.125  22.035 1.00 74.93  ?  305 HIS   A NE2  1 
ATOM   1876 N  N    . GLN   A 1 279 ? 30.189  -4.506  26.553 1.00 68.80  ?  306 GLN   A N    1 
ATOM   1877 C  CA   . GLN   A 1 279 ? 30.608  -3.237  27.123 1.00 60.60  ?  306 GLN   A CA   1 
ATOM   1878 C  C    . GLN   A 1 279 ? 31.696  -2.630  26.249 1.00 59.46  ?  306 GLN   A C    1 
ATOM   1879 O  O    . GLN   A 1 279 ? 32.427  -3.342  25.556 1.00 68.63  ?  306 GLN   A O    1 
ATOM   1880 C  CB   . GLN   A 1 279 ? 31.130  -3.416  28.551 1.00 60.43  ?  306 GLN   A CB   1 
ATOM   1881 C  CG   . GLN   A 1 279 ? 30.196  -4.174  29.475 1.00 64.03  ?  306 GLN   A CG   1 
ATOM   1882 C  CD   . GLN   A 1 279 ? 30.823  -4.448  30.827 1.00 66.35  ?  306 GLN   A CD   1 
ATOM   1883 O  OE1  . GLN   A 1 279 ? 31.588  -5.399  30.986 1.00 76.59  ?  306 GLN   A OE1  1 
ATOM   1884 N  NE2  . GLN   A 1 279 ? 30.504  -3.614  31.810 1.00 76.72  ?  306 GLN   A NE2  1 
ATOM   1885 N  N    . HIS   A 1 280 ? 31.799  -1.304  26.281 1.00 60.37  ?  307 HIS   A N    1 
ATOM   1886 C  CA   . HIS   A 1 280 ? 32.849  -0.620  25.543 1.00 63.15  ?  307 HIS   A CA   1 
ATOM   1887 C  C    . HIS   A 1 280 ? 33.449  0.478   26.407 1.00 64.08  ?  307 HIS   A C    1 
ATOM   1888 O  O    . HIS   A 1 280 ? 32.800  1.010   27.311 1.00 63.17  ?  307 HIS   A O    1 
ATOM   1889 C  CB   . HIS   A 1 280 ? 32.341  -0.037  24.214 1.00 61.68  ?  307 HIS   A CB   1 
ATOM   1890 C  CG   . HIS   A 1 280 ? 31.320  1.047   24.370 1.00 65.02  ?  307 HIS   A CG   1 
ATOM   1891 N  ND1  . HIS   A 1 280 ? 30.084  0.832   24.938 1.00 69.85  ?  307 HIS   A ND1  1 
ATOM   1892 C  CD2  . HIS   A 1 280 ? 31.352  2.355   24.021 1.00 64.16  ?  307 HIS   A CD2  1 
ATOM   1893 C  CE1  . HIS   A 1 280 ? 29.398  1.962   24.936 1.00 81.16  ?  307 HIS   A CE1  1 
ATOM   1894 N  NE2  . HIS   A 1 280 ? 30.146  2.902   24.386 1.00 75.24  ?  307 HIS   A NE2  1 
ATOM   1895 N  N    . CYS   A 1 281 ? 34.708  0.801   26.121 1.00 56.94  ?  308 CYS   A N    1 
ATOM   1896 C  CA   . CYS   A 1 281 ? 35.439  1.837   26.831 1.00 59.01  ?  308 CYS   A CA   1 
ATOM   1897 C  C    . CYS   A 1 281 ? 36.210  2.664   25.812 1.00 66.62  ?  308 CYS   A C    1 
ATOM   1898 O  O    . CYS   A 1 281 ? 36.188  2.384   24.609 1.00 73.19  ?  308 CYS   A O    1 
ATOM   1899 C  CB   . CYS   A 1 281 ? 36.375  1.231   27.882 1.00 54.98  ?  308 CYS   A CB   1 
ATOM   1900 S  SG   . CYS   A 1 281 ? 37.769  0.308   27.194 1.00 63.72  ?  308 CYS   A SG   1 
ATOM   1901 N  N    . VAL   A 1 282 ? 36.896  3.694   26.297 1.00 61.54  ?  309 VAL   A N    1 
ATOM   1902 C  CA   . VAL   A 1 282 ? 37.715  4.564   25.461 1.00 64.96  ?  309 VAL   A CA   1 
ATOM   1903 C  C    . VAL   A 1 282 ? 39.128  4.561   26.025 1.00 63.29  ?  309 VAL   A C    1 
ATOM   1904 O  O    . VAL   A 1 282 ? 39.346  4.978   27.170 1.00 77.69  ?  309 VAL   A O    1 
ATOM   1905 C  CB   . VAL   A 1 282 ? 37.153  5.992   25.393 1.00 75.75  ?  309 VAL   A CB   1 
ATOM   1906 C  CG1  . VAL   A 1 282 ? 38.072  6.882   24.570 1.00 73.21  ?  309 VAL   A CG1  1 
ATOM   1907 C  CG2  . VAL   A 1 282 ? 35.749  5.982   24.808 1.00 67.10  ?  309 VAL   A CG2  1 
ATOM   1908 N  N    . LEU   A 1 283 ? 40.082  4.091   25.227 1.00 62.63  ?  310 LEU   A N    1 
ATOM   1909 C  CA   . LEU   A 1 283 ? 41.480  4.049   25.629 1.00 70.61  ?  310 LEU   A CA   1 
ATOM   1910 C  C    . LEU   A 1 283 ? 42.176  5.333   25.200 1.00 75.84  ?  310 LEU   A C    1 
ATOM   1911 O  O    . LEU   A 1 283 ? 42.134  5.710   24.025 1.00 75.29  ?  310 LEU   A O    1 
ATOM   1912 C  CB   . LEU   A 1 283 ? 42.175  2.830   25.023 1.00 64.72  ?  310 LEU   A CB   1 
ATOM   1913 C  CG   . LEU   A 1 283 ? 41.493  1.492   25.310 1.00 69.11  ?  310 LEU   A CG   1 
ATOM   1914 C  CD1  . LEU   A 1 283 ? 42.370  0.340   24.862 1.00 74.51  ?  310 LEU   A CD1  1 
ATOM   1915 C  CD2  . LEU   A 1 283 ? 41.170  1.369   26.791 1.00 66.58  ?  310 LEU   A CD2  1 
ATOM   1916 N  N    . ALA   A 1 284 ? 42.820  5.997   26.156 1.00 79.79  ?  311 ALA   A N    1 
ATOM   1917 C  CA   . ALA   A 1 284 ? 43.378  7.319   25.917 1.00 72.42  ?  311 ALA   A CA   1 
ATOM   1918 C  C    . ALA   A 1 284 ? 44.703  7.237   25.172 1.00 85.29  ?  311 ALA   A C    1 
ATOM   1919 O  O    . ALA   A 1 284 ? 45.510  6.331   25.398 1.00 79.78  ?  311 ALA   A O    1 
ATOM   1920 C  CB   . ALA   A 1 284 ? 43.573  8.059   27.240 1.00 79.58  ?  311 ALA   A CB   1 
ATOM   1921 N  N    . GLY   A 1 285 ? 44.918  8.194   24.280 1.00 89.51  ?  312 GLY   A N    1 
ATOM   1922 C  CA   . GLY   A 1 285 ? 46.183  8.407   23.612 1.00 74.27  ?  312 GLY   A CA   1 
ATOM   1923 C  C    . GLY   A 1 285 ? 46.981  9.512   24.270 1.00 83.08  ?  312 GLY   A C    1 
ATOM   1924 O  O    . GLY   A 1 285 ? 46.850  9.773   25.471 1.00 86.76  ?  312 GLY   A O    1 
ATOM   1925 N  N    . SER   A 1 286 ? 47.814  10.181  23.475 1.00 90.79  ?  313 SER   A N    1 
ATOM   1926 C  CA   . SER   A 1 286 ? 48.628  11.281  23.980 1.00 92.95  ?  313 SER   A CA   1 
ATOM   1927 C  C    . SER   A 1 286 ? 48.119  12.651  23.562 1.00 99.38  ?  313 SER   A C    1 
ATOM   1928 O  O    . SER   A 1 286 ? 48.271  13.612  24.322 1.00 104.79 ?  313 SER   A O    1 
ATOM   1929 C  CB   . SER   A 1 286 ? 50.080  11.127  23.518 1.00 96.11  ?  313 SER   A CB   1 
ATOM   1930 O  OG   . SER   A 1 286 ? 50.480  9.772   23.552 1.00 102.81 ?  313 SER   A OG   1 
ATOM   1931 N  N    . GLN   A 1 287 ? 47.530  12.765  22.384 1.00 90.98  ?  314 GLN   A N    1 
ATOM   1932 C  CA   . GLN   A 1 287 ? 46.986  14.024  21.906 1.00 93.13  ?  314 GLN   A CA   1 
ATOM   1933 C  C    . GLN   A 1 287 ? 45.500  14.116  22.220 1.00 101.40 ?  314 GLN   A C    1 
ATOM   1934 O  O    . GLN   A 1 287 ? 44.827  13.096  22.401 1.00 92.75  ?  314 GLN   A O    1 
ATOM   1935 C  CB   . GLN   A 1 287 ? 47.214  14.158  20.398 1.00 96.05  ?  314 GLN   A CB   1 
ATOM   1936 C  CG   . GLN   A 1 287 ? 48.678  14.268  20.002 1.00 107.30 ?  314 GLN   A CG   1 
ATOM   1937 N  N    . PRO   A 1 288 ? 44.953  15.330  22.310 1.00 100.05 ?  315 PRO   A N    1 
ATOM   1938 C  CA   . PRO   A 1 288 ? 43.510  15.471  22.539 1.00 84.26  ?  315 PRO   A CA   1 
ATOM   1939 C  C    . PRO   A 1 288 ? 42.705  14.850  21.408 1.00 90.94  ?  315 PRO   A C    1 
ATOM   1940 O  O    . PRO   A 1 288 ? 43.219  14.561  20.325 1.00 88.06  ?  315 PRO   A O    1 
ATOM   1941 C  CB   . PRO   A 1 288 ? 43.304  16.990  22.604 1.00 90.84  ?  315 PRO   A CB   1 
ATOM   1942 C  CG   . PRO   A 1 288 ? 44.645  17.542  22.949 1.00 82.39  ?  315 PRO   A CG   1 
ATOM   1943 C  CD   . PRO   A 1 288 ? 45.639  16.633  22.295 1.00 101.10 ?  315 PRO   A CD   1 
ATOM   1944 N  N    . ARG   A 1 289 ? 41.416  14.643  21.673 1.00 85.85  ?  316 ARG   A N    1 
ATOM   1945 C  CA   . ARG   A 1 289 ? 40.558  13.962  20.711 1.00 88.98  ?  316 ARG   A CA   1 
ATOM   1946 C  C    . ARG   A 1 289 ? 39.112  14.382  20.919 1.00 76.17  ?  316 ARG   A C    1 
ATOM   1947 O  O    . ARG   A 1 289 ? 38.632  14.421  22.055 1.00 73.49  ?  316 ARG   A O    1 
ATOM   1948 C  CB   . ARG   A 1 289 ? 40.693  12.441  20.841 1.00 75.93  ?  316 ARG   A CB   1 
ATOM   1949 C  CG   . ARG   A 1 289 ? 39.616  11.661  20.108 1.00 80.12  ?  316 ARG   A CG   1 
ATOM   1950 C  CD   . ARG   A 1 289 ? 39.309  10.354  20.813 1.00 69.97  ?  316 ARG   A CD   1 
ATOM   1951 N  NE   . ARG   A 1 289 ? 38.327  9.557   20.089 1.00 83.01  ?  316 ARG   A NE   1 
ATOM   1952 C  CZ   . ARG   A 1 289 ? 37.184  9.126   20.607 1.00 80.22  ?  316 ARG   A CZ   1 
ATOM   1953 N  NH1  . ARG   A 1 289 ? 36.849  9.392   21.858 1.00 83.91  ?  316 ARG   A NH1  1 
ATOM   1954 N  NH2  . ARG   A 1 289 ? 36.358  8.410   19.850 1.00 73.19  ?  316 ARG   A NH2  1 
ATOM   1955 N  N    . PHE   A 1 290 ? 38.429  14.693  19.822 1.00 81.16  ?  317 PHE   A N    1 
ATOM   1956 C  CA   . PHE   A 1 290 ? 36.993  14.924  19.811 1.00 84.74  ?  317 PHE   A CA   1 
ATOM   1957 C  C    . PHE   A 1 290 ? 36.271  13.668  19.337 1.00 79.15  ?  317 PHE   A C    1 
ATOM   1958 O  O    . PHE   A 1 290 ? 36.845  12.811  18.661 1.00 80.36  ?  317 PHE   A O    1 
ATOM   1959 C  CB   . PHE   A 1 290 ? 36.630  16.101  18.900 1.00 83.17  ?  317 PHE   A CB   1 
ATOM   1960 C  CG   . PHE   A 1 290 ? 37.164  17.426  19.365 1.00 89.88  ?  317 PHE   A CG   1 
ATOM   1961 C  CD1  . PHE   A 1 290 ? 38.462  17.811  19.065 1.00 96.29  ?  317 PHE   A CD1  1 
ATOM   1962 C  CD2  . PHE   A 1 290 ? 36.364  18.294  20.089 1.00 82.94  ?  317 PHE   A CD2  1 
ATOM   1963 C  CE1  . PHE   A 1 290 ? 38.953  19.032  19.487 1.00 77.44  ?  317 PHE   A CE1  1 
ATOM   1964 C  CE2  . PHE   A 1 290 ? 36.849  19.517  20.513 1.00 84.76  ?  317 PHE   A CE2  1 
ATOM   1965 C  CZ   . PHE   A 1 290 ? 38.146  19.886  20.211 1.00 91.11  ?  317 PHE   A CZ   1 
ATOM   1966 N  N    . SER   A 1 291 ? 34.993  13.570  19.697 1.00 65.97  ?  318 SER   A N    1 
ATOM   1967 C  CA   . SER   A 1 291 ? 34.159  12.473  19.231 1.00 71.94  ?  318 SER   A CA   1 
ATOM   1968 C  C    . SER   A 1 291 ? 32.711  12.935  19.186 1.00 71.74  ?  318 SER   A C    1 
ATOM   1969 O  O    . SER   A 1 291 ? 32.274  13.720  20.033 1.00 71.04  ?  318 SER   A O    1 
ATOM   1970 C  CB   . SER   A 1 291 ? 34.293  11.233  20.124 1.00 71.68  ?  318 SER   A CB   1 
ATOM   1971 O  OG   . SER   A 1 291 ? 33.770  11.470  21.417 1.00 78.85  ?  318 SER   A OG   1 
ATOM   1972 N  N    . SER   A 1 292 ? 31.975  12.446  18.190 1.00 71.80  ?  319 SER   A N    1 
ATOM   1973 C  CA   . SER   A 1 292 ? 30.560  12.766  18.007 1.00 71.91  ?  319 SER   A CA   1 
ATOM   1974 C  C    . SER   A 1 292 ? 29.796  11.448  17.942 1.00 72.66  ?  319 SER   A C    1 
ATOM   1975 O  O    . SER   A 1 292 ? 29.826  10.755  16.921 1.00 77.23  ?  319 SER   A O    1 
ATOM   1976 C  CB   . SER   A 1 292 ? 30.341  13.602  16.749 1.00 75.36  ?  319 SER   A CB   1 
ATOM   1977 O  OG   . SER   A 1 292 ? 28.962  13.837  16.524 1.00 78.33  ?  319 SER   A OG   1 
ATOM   1978 N  N    . THR   A 1 293 ? 29.113  11.103  19.032 1.00 66.77  ?  320 THR   A N    1 
ATOM   1979 C  CA   . THR   A 1 293 ? 28.403  9.834   19.151 1.00 74.16  ?  320 THR   A CA   1 
ATOM   1980 C  C    . THR   A 1 293 ? 26.914  10.077  18.928 1.00 73.72  ?  320 THR   A C    1 
ATOM   1981 O  O    . THR   A 1 293 ? 26.245  10.694  19.764 1.00 65.46  ?  320 THR   A O    1 
ATOM   1982 C  CB   . THR   A 1 293 ? 28.662  9.197   20.515 1.00 70.17  ?  320 THR   A CB   1 
ATOM   1983 O  OG1  . THR   A 1 293 ? 27.770  9.759   21.485 1.00 78.13  ?  320 THR   A OG1  1 
ATOM   1984 C  CG2  . THR   A 1 293 ? 30.097  9.450   20.951 1.00 75.23  ?  320 THR   A CG2  1 
ATOM   1985 N  N    . HIS   A 1 294 ? 26.399  9.584   17.805 1.00 70.04  ?  321 HIS   A N    1 
ATOM   1986 C  CA   . HIS   A 1 294 ? 25.004  9.779   17.433 1.00 63.45  ?  321 HIS   A CA   1 
ATOM   1987 C  C    . HIS   A 1 294 ? 24.176  8.593   17.905 1.00 61.65  ?  321 HIS   A C    1 
ATOM   1988 O  O    . HIS   A 1 294 ? 24.549  7.437   17.681 1.00 65.14  ?  321 HIS   A O    1 
ATOM   1989 C  CB   . HIS   A 1 294 ? 24.870  9.957   15.921 1.00 63.71  ?  321 HIS   A CB   1 
ATOM   1990 C  CG   . HIS   A 1 294 ? 25.710  11.066  15.368 1.00 72.97  ?  321 HIS   A CG   1 
ATOM   1991 N  ND1  . HIS   A 1 294 ? 25.176  12.120  14.659 1.00 67.61  ?  321 HIS   A ND1  1 
ATOM   1992 C  CD2  . HIS   A 1 294 ? 27.045  11.287  15.420 1.00 82.62  ?  321 HIS   A CD2  1 
ATOM   1993 C  CE1  . HIS   A 1 294 ? 26.145  12.943  14.299 1.00 78.52  ?  321 HIS   A CE1  1 
ATOM   1994 N  NE2  . HIS   A 1 294 ? 27.289  12.460  14.750 1.00 79.94  ?  321 HIS   A NE2  1 
ATOM   1995 N  N    . ARG   A 1 295 ? 23.052  8.883   18.557 1.00 65.76  ?  322 ARG   A N    1 
ATOM   1996 C  CA   . ARG   A 1 295 ? 22.231  7.860   19.184 1.00 62.64  ?  322 ARG   A CA   1 
ATOM   1997 C  C    . ARG   A 1 295 ? 20.764  8.078   18.845 1.00 74.01  ?  322 ARG   A C    1 
ATOM   1998 O  O    . ARG   A 1 295 ? 20.354  9.160   18.416 1.00 67.60  ?  322 ARG   A O    1 
ATOM   1999 C  CB   . ARG   A 1 295 ? 22.409  7.860   20.709 1.00 60.34  ?  322 ARG   A CB   1 
ATOM   2000 C  CG   . ARG   A 1 295 ? 23.851  7.976   21.173 1.00 70.11  ?  322 ARG   A CG   1 
ATOM   2001 C  CD   . ARG   A 1 295 ? 23.968  8.892   22.378 1.00 64.85  ?  322 ARG   A CD   1 
ATOM   2002 N  NE   . ARG   A 1 295 ? 25.342  8.978   22.855 1.00 68.40  ?  322 ARG   A NE   1 
ATOM   2003 C  CZ   . ARG   A 1 295 ? 25.860  8.190   23.786 1.00 76.35  ?  322 ARG   A CZ   1 
ATOM   2004 N  NH1  . ARG   A 1 295 ? 25.142  7.242   24.365 1.00 76.56  ?  322 ARG   A NH1  1 
ATOM   2005 N  NH2  . ARG   A 1 295 ? 27.131  8.355   24.143 1.00 82.21  ?  322 ARG   A NH2  1 
ATOM   2006 N  N    . VAL   A 1 296 ? 19.977  7.025   19.041 1.00 70.08  ?  323 VAL   A N    1 
ATOM   2007 C  CA   . VAL   A 1 296 ? 18.520  7.111   18.988 1.00 65.07  ?  323 VAL   A CA   1 
ATOM   2008 C  C    . VAL   A 1 296 ? 18.056  7.077   20.440 1.00 64.94  ?  323 VAL   A C    1 
ATOM   2009 O  O    . VAL   A 1 296 ? 17.800  6.016   21.012 1.00 63.18  ?  323 VAL   A O    1 
ATOM   2010 C  CB   . VAL   A 1 296 ? 17.904  5.988   18.157 1.00 72.79  ?  323 VAL   A CB   1 
ATOM   2011 C  CG1  . VAL   A 1 296 ? 16.417  6.239   17.960 1.00 62.52  ?  323 VAL   A CG1  1 
ATOM   2012 C  CG2  . VAL   A 1 296 ? 18.607  5.867   16.816 1.00 65.09  ?  323 VAL   A CG2  1 
ATOM   2013 N  N    . ALA   A 1 297 ? 17.956  8.257   21.046 1.00 60.37  ?  324 ALA   A N    1 
ATOM   2014 C  CA   . ALA   A 1 297 ? 17.605  8.347   22.455 1.00 59.49  ?  324 ALA   A CA   1 
ATOM   2015 C  C    . ALA   A 1 297 ? 16.161  7.921   22.682 1.00 69.49  ?  324 ALA   A C    1 
ATOM   2016 O  O    . ALA   A 1 297 ? 15.269  8.236   21.890 1.00 59.63  ?  324 ALA   A O    1 
ATOM   2017 C  CB   . ALA   A 1 297 ? 17.817  9.772   22.964 1.00 56.35  ?  324 ALA   A CB   1 
ATOM   2018 N  N    . GLU   A 1 298 ? 15.936  7.189   23.769 1.00 67.14  ?  325 GLU   A N    1 
ATOM   2019 C  CA   . GLU   A 1 298 ? 14.585  6.824   24.185 1.00 67.67  ?  325 GLU   A CA   1 
ATOM   2020 C  C    . GLU   A 1 298 ? 13.994  8.031   24.905 1.00 62.26  ?  325 GLU   A C    1 
ATOM   2021 O  O    . GLU   A 1 298 ? 14.330  8.315   26.057 1.00 72.42  ?  325 GLU   A O    1 
ATOM   2022 C  CB   . GLU   A 1 298 ? 14.616  5.572   25.058 1.00 66.68  ?  325 GLU   A CB   1 
ATOM   2023 C  CG   . GLU   A 1 298 ? 13.434  5.342   26.016 1.00 75.20  ?  325 GLU   A CG   1 
ATOM   2024 C  CD   . GLU   A 1 298 ? 12.047  5.573   25.425 1.00 83.35  ?  325 GLU   A CD   1 
ATOM   2025 O  OE1  . GLU   A 1 298 ? 11.106  5.739   26.227 1.00 80.63  ?  325 GLU   A OE1  1 
ATOM   2026 O  OE2  . GLU   A 1 298 ? 11.872  5.541   24.186 1.00 82.40  ?  325 GLU   A OE2  1 
ATOM   2027 N  N    . CYS   A 1 299 ? 13.117  8.756   24.213 1.00 66.58  ?  326 CYS   A N    1 
ATOM   2028 C  CA   . CYS   A 1 299 ? 12.618  10.043  24.680 1.00 66.21  ?  326 CYS   A CA   1 
ATOM   2029 C  C    . CYS   A 1 299 ? 11.097  10.061  24.787 1.00 58.75  ?  326 CYS   A C    1 
ATOM   2030 O  O    . CYS   A 1 299 ? 10.475  11.114  24.640 1.00 69.38  ?  326 CYS   A O    1 
ATOM   2031 C  CB   . CYS   A 1 299 ? 13.100  11.165  23.760 1.00 65.89  ?  326 CYS   A CB   1 
ATOM   2032 S  SG   . CYS   A 1 299 ? 12.615  10.967  22.025 1.00 85.22  ?  326 CYS   A SG   1 
ATOM   2033 N  N    . SER   A 1 300 ? 10.483  8.903   25.043 1.00 60.28  ?  327 SER   A N    1 
ATOM   2034 C  CA   . SER   A 1 300 ? 9.033   8.856   25.203 1.00 65.38  ?  327 SER   A CA   1 
ATOM   2035 C  C    . SER   A 1 300 ? 8.567   9.642   26.420 1.00 64.34  ?  327 SER   A C    1 
ATOM   2036 O  O    . SER   A 1 300 ? 7.414   10.088  26.454 1.00 62.03  ?  327 SER   A O    1 
ATOM   2037 C  CB   . SER   A 1 300 ? 8.558   7.408   25.305 1.00 62.04  ?  327 SER   A CB   1 
ATOM   2038 O  OG   . SER   A 1 300 ? 8.995   6.817   26.516 1.00 59.46  ?  327 SER   A OG   1 
ATOM   2039 N  N    . THR   A 1 301 ? 9.430   9.811   27.421 1.00 60.57  ?  328 THR   A N    1 
ATOM   2040 C  CA   . THR   A 1 301 ? 9.168   10.683  28.559 1.00 54.30  ?  328 THR   A CA   1 
ATOM   2041 C  C    . THR   A 1 301 ? 10.263  11.736  28.699 1.00 53.30  ?  328 THR   A C    1 
ATOM   2042 O  O    . THR   A 1 301 ? 10.613  12.137  29.811 1.00 66.75  ?  328 THR   A O    1 
ATOM   2043 C  CB   . THR   A 1 301 ? 9.035   9.877   29.852 1.00 55.75  ?  328 THR   A CB   1 
ATOM   2044 O  OG1  . THR   A 1 301 ? 10.303  9.300   30.192 1.00 75.46  ?  328 THR   A OG1  1 
ATOM   2045 C  CG2  . THR   A 1 301 ? 8.001   8.771   29.694 1.00 54.29  ?  328 THR   A CG2  1 
ATOM   2046 N  N    . GLY   A 1 302 ? 10.813  12.191  27.575 1.00 51.23  ?  329 GLY   A N    1 
ATOM   2047 C  CA   . GLY   A 1 302 ? 11.932  13.111  27.612 1.00 53.34  ?  329 GLY   A CA   1 
ATOM   2048 C  C    . GLY   A 1 302 ? 11.938  14.168  26.526 1.00 60.94  ?  329 GLY   A C    1 
ATOM   2049 O  O    . GLY   A 1 302 ? 13.008  14.623  26.108 1.00 56.03  ?  329 GLY   A O    1 
ATOM   2050 N  N    . THR   A 1 303 ? 10.760  14.569  26.056 1.00 57.10  ?  330 THR   A N    1 
ATOM   2051 C  CA   . THR   A 1 303 ? 10.631  15.684  25.131 1.00 64.03  ?  330 THR   A CA   1 
ATOM   2052 C  C    . THR   A 1 303 ? 9.804   16.786  25.776 1.00 61.25  ?  330 THR   A C    1 
ATOM   2053 O  O    . THR   A 1 303 ? 8.986   16.531  26.665 1.00 66.21  ?  330 THR   A O    1 
ATOM   2054 C  CB   . THR   A 1 303 ? 9.979   15.265  23.803 1.00 53.78  ?  330 THR   A CB   1 
ATOM   2055 O  OG1  . THR   A 1 303 ? 8.581   15.024  24.003 1.00 55.62  ?  330 THR   A OG1  1 
ATOM   2056 C  CG2  . THR   A 1 303 ? 10.642  14.013  23.249 1.00 57.38  ?  330 THR   A CG2  1 
ATOM   2057 N  N    . LEU   A 1 304 ? 10.033  18.020  25.320 1.00 69.82  ?  331 LEU   A N    1 
ATOM   2058 C  CA   . LEU   A 1 304 ? 9.270   19.152  25.833 1.00 63.42  ?  331 LEU   A CA   1 
ATOM   2059 C  C    . LEU   A 1 304 ? 7.780   18.973  25.578 1.00 64.22  ?  331 LEU   A C    1 
ATOM   2060 O  O    . LEU   A 1 304 ? 6.952   19.314  26.431 1.00 70.08  ?  331 LEU   A O    1 
ATOM   2061 C  CB   . LEU   A 1 304 ? 9.764   20.451  25.199 1.00 64.79  ?  331 LEU   A CB   1 
ATOM   2062 C  CG   . LEU   A 1 304 ? 9.085   21.725  25.707 1.00 74.66  ?  331 LEU   A CG   1 
ATOM   2063 C  CD1  . LEU   A 1 304 ? 9.288   21.889  27.209 1.00 62.18  ?  331 LEU   A CD1  1 
ATOM   2064 C  CD2  . LEU   A 1 304 ? 9.587   22.943  24.947 1.00 68.73  ?  331 LEU   A CD2  1 
ATOM   2065 N  N    . ASP   A 1 305 ? 7.419   18.442  24.407 1.00 69.55  ?  332 ASP   A N    1 
ATOM   2066 C  CA   . ASP   A 1 305 ? 6.011   18.210  24.102 1.00 64.83  ?  332 ASP   A CA   1 
ATOM   2067 C  C    . ASP   A 1 305 ? 5.391   17.221  25.079 1.00 63.12  ?  332 ASP   A C    1 
ATOM   2068 O  O    . ASP   A 1 305 ? 4.238   17.388  25.494 1.00 63.96  ?  332 ASP   A O    1 
ATOM   2069 C  CB   . ASP   A 1 305 ? 5.857   17.712  22.666 1.00 68.27  ?  332 ASP   A CB   1 
ATOM   2070 C  CG   . ASP   A 1 305 ? 6.220   18.766  21.642 1.00 89.66  ?  332 ASP   A CG   1 
ATOM   2071 O  OD1  . ASP   A 1 305 ? 6.480   19.920  22.044 1.00 91.34  ?  332 ASP   A OD1  1 
ATOM   2072 O  OD2  . ASP   A 1 305 ? 6.242   18.442  20.436 1.00 103.03 ?  332 ASP   A OD2  1 
ATOM   2073 N  N    . TYR   A 1 306 ? 6.141   16.185  25.461 1.00 62.98  ?  333 TYR   A N    1 
ATOM   2074 C  CA   . TYR   A 1 306 ? 5.622   15.212  26.416 1.00 61.22  ?  333 TYR   A CA   1 
ATOM   2075 C  C    . TYR   A 1 306 ? 5.334   15.865  27.761 1.00 64.82  ?  333 TYR   A C    1 
ATOM   2076 O  O    . TYR   A 1 306 ? 4.256   15.679  28.337 1.00 69.97  ?  333 TYR   A O    1 
ATOM   2077 C  CB   . TYR   A 1 306 ? 6.609   14.056  26.587 1.00 57.42  ?  333 TYR   A CB   1 
ATOM   2078 C  CG   . TYR   A 1 306 ? 6.406   13.289  27.876 1.00 57.45  ?  333 TYR   A CG   1 
ATOM   2079 C  CD1  . TYR   A 1 306 ? 5.462   12.273  27.959 1.00 50.03  ?  333 TYR   A CD1  1 
ATOM   2080 C  CD2  . TYR   A 1 306 ? 7.151   13.583  29.012 1.00 52.62  ?  333 TYR   A CD2  1 
ATOM   2081 C  CE1  . TYR   A 1 306 ? 5.266   11.573  29.134 1.00 48.65  ?  333 TYR   A CE1  1 
ATOM   2082 C  CE2  . TYR   A 1 306 ? 6.960   12.891  30.191 1.00 53.09  ?  333 TYR   A CE2  1 
ATOM   2083 C  CZ   . TYR   A 1 306 ? 6.018   11.886  30.247 1.00 54.85  ?  333 TYR   A CZ   1 
ATOM   2084 O  OH   . TYR   A 1 306 ? 5.826   11.191  31.420 1.00 63.18  ?  333 TYR   A OH   1 
ATOM   2085 N  N    . ILE   A 1 307 ? 6.293   16.634  28.282 1.00 56.03  ?  334 ILE   A N    1 
ATOM   2086 C  CA   . ILE   A 1 307 ? 6.156   17.165  29.634 1.00 53.02  ?  334 ILE   A CA   1 
ATOM   2087 C  C    . ILE   A 1 307 ? 5.145   18.306  29.674 1.00 71.28  ?  334 ILE   A C    1 
ATOM   2088 O  O    . ILE   A 1 307 ? 4.509   18.543  30.709 1.00 59.38  ?  334 ILE   A O    1 
ATOM   2089 C  CB   . ILE   A 1 307 ? 7.534   17.589  30.178 1.00 52.08  ?  334 ILE   A CB   1 
ATOM   2090 C  CG1  . ILE   A 1 307 ? 7.444   17.923  31.670 1.00 56.65  ?  334 ILE   A CG1  1 
ATOM   2091 C  CG2  . ILE   A 1 307 ? 8.098   18.760  29.388 1.00 70.59  ?  334 ILE   A CG2  1 
ATOM   2092 C  CD1  . ILE   A 1 307 ? 7.166   16.722  32.547 1.00 54.96  ?  334 ILE   A CD1  1 
ATOM   2093 N  N    . LEU   A 1 308 ? 4.963   19.024  28.562 1.00 66.44  ?  335 LEU   A N    1 
ATOM   2094 C  CA   . LEU   A 1 308 ? 3.923   20.047  28.520 1.00 58.47  ?  335 LEU   A CA   1 
ATOM   2095 C  C    . LEU   A 1 308 ? 2.535   19.417  28.526 1.00 68.47  ?  335 LEU   A C    1 
ATOM   2096 O  O    . LEU   A 1 308 ? 1.615   19.934  29.171 1.00 75.87  ?  335 LEU   A O    1 
ATOM   2097 C  CB   . LEU   A 1 308 ? 4.099   20.940  27.292 1.00 54.84  ?  335 LEU   A CB   1 
ATOM   2098 C  CG   . LEU   A 1 308 ? 5.243   21.955  27.318 1.00 67.87  ?  335 LEU   A CG   1 
ATOM   2099 C  CD1  . LEU   A 1 308 ? 5.272   22.750  26.022 1.00 51.80  ?  335 LEU   A CD1  1 
ATOM   2100 C  CD2  . LEU   A 1 308 ? 5.120   22.880  28.518 1.00 57.14  ?  335 LEU   A CD2  1 
ATOM   2101 N  N    . GLN   A 1 309 ? 2.365   18.304  27.808 1.00 68.00  ?  336 GLN   A N    1 
ATOM   2102 C  CA   . GLN   A 1 309 ? 1.093   17.590  27.834 1.00 69.40  ?  336 GLN   A CA   1 
ATOM   2103 C  C    . GLN   A 1 309 ? 0.820   17.054  29.233 1.00 67.01  ?  336 GLN   A C    1 
ATOM   2104 O  O    . GLN   A 1 309 ? -0.291  17.195  29.757 1.00 72.48  ?  336 GLN   A O    1 
ATOM   2105 C  CB   . GLN   A 1 309 ? 1.114   16.469  26.780 1.00 72.50  ?  336 GLN   A CB   1 
ATOM   2106 C  CG   . GLN   A 1 309 ? -0.228  15.791  26.395 1.00 89.90  ?  336 GLN   A CG   1 
ATOM   2107 C  CD   . GLN   A 1 309 ? -0.247  15.024  25.078 1.00 115.08 ?  336 GLN   A CD   1 
ATOM   2108 O  OE1  . GLN   A 1 309 ? 0.803   14.709  24.523 1.00 111.75 ?  336 GLN   A OE1  1 
ATOM   2109 N  NE2  . GLN   A 1 309 ? -1.441  14.624  24.637 1.00 93.06  ?  336 GLN   A NE2  1 
ATOM   2110 N  N    . ARG   A 1 310 ? 1.834   16.449  29.857 1.00 66.38  ?  337 ARG   A N    1 
ATOM   2111 C  CA   . ARG   A 1 310 ? 1.691   15.952  31.221 1.00 61.88  ?  337 ARG   A CA   1 
ATOM   2112 C  C    . ARG   A 1 310 ? 1.252   17.057  32.174 1.00 61.65  ?  337 ARG   A C    1 
ATOM   2113 O  O    . ARG   A 1 310 ? 0.438   16.826  33.075 1.00 65.50  ?  337 ARG   A O    1 
ATOM   2114 C  CB   . ARG   A 1 310 ? 3.009   15.338  31.690 1.00 56.07  ?  337 ARG   A CB   1 
ATOM   2115 C  CG   . ARG   A 1 310 ? 3.400   14.075  30.948 1.00 65.00  ?  337 ARG   A CG   1 
ATOM   2116 C  CD   . ARG   A 1 310 ? 2.683   12.875  31.530 1.00 55.02  ?  337 ARG   A CD   1 
ATOM   2117 N  NE   . ARG   A 1 310 ? 3.174   12.582  32.870 1.00 63.28  ?  337 ARG   A NE   1 
ATOM   2118 C  CZ   . ARG   A 1 310 ? 2.598   11.739  33.714 1.00 65.98  ?  337 ARG   A CZ   1 
ATOM   2119 N  NH1  . ARG   A 1 310 ? 1.491   11.090  33.395 1.00 56.21  ?  337 ARG   A NH1  1 
ATOM   2120 N  NH2  . ARG   A 1 310 ? 3.144   11.547  34.912 1.00 56.85  ?  337 ARG   A NH2  1 
ATOM   2121 N  N    . CYS   A 1 311 ? 1.781   18.268  31.986 1.00 62.50  ?  338 CYS   A N    1 
ATOM   2122 C  CA   . CYS   A 1 311 ? 1.363   19.393  32.816 1.00 66.70  ?  338 CYS   A CA   1 
ATOM   2123 C  C    . CYS   A 1 311 ? -0.090  19.763  32.548 1.00 73.31  ?  338 CYS   A C    1 
ATOM   2124 O  O    . CYS   A 1 311 ? -0.854  20.022  33.485 1.00 71.41  ?  338 CYS   A O    1 
ATOM   2125 C  CB   . CYS   A 1 311 ? 2.277   20.592  32.566 1.00 63.34  ?  338 CYS   A CB   1 
ATOM   2126 S  SG   . CYS   A 1 311 ? 3.917   20.446  33.304 1.00 69.54  ?  338 CYS   A SG   1 
ATOM   2127 N  N    . GLN   A 1 312 ? -0.487  19.795  31.273 1.00 68.79  ?  339 GLN   A N    1 
ATOM   2128 C  CA   . GLN   A 1 312 ? -1.870  20.111  30.930 1.00 66.21  ?  339 GLN   A CA   1 
ATOM   2129 C  C    . GLN   A 1 312 ? -2.834  19.095  31.530 1.00 61.40  ?  339 GLN   A C    1 
ATOM   2130 O  O    . GLN   A 1 312 ? -3.930  19.455  31.976 1.00 74.48  ?  339 GLN   A O    1 
ATOM   2131 C  CB   . GLN   A 1 312 ? -2.026  20.180  29.410 1.00 68.54  ?  339 GLN   A CB   1 
ATOM   2132 C  CG   . GLN   A 1 312 ? -3.413  19.825  28.897 1.00 75.96  ?  339 GLN   A CG   1 
ATOM   2133 C  CD   . GLN   A 1 312 ? -3.699  20.417  27.530 1.00 94.83  ?  339 GLN   A CD   1 
ATOM   2134 O  OE1  . GLN   A 1 312 ? -3.977  21.610  27.403 1.00 104.24 ?  339 GLN   A OE1  1 
ATOM   2135 N  NE2  . GLN   A 1 312 ? -3.632  19.583  26.498 1.00 97.28  ?  339 GLN   A NE2  1 
ATOM   2136 N  N    . LEU   A 1 313 ? -2.438  17.820  31.563 1.00 74.64  ?  340 LEU   A N    1 
ATOM   2137 C  CA   . LEU   A 1 313 ? -3.304  16.793  32.135 1.00 77.34  ?  340 LEU   A CA   1 
ATOM   2138 C  C    . LEU   A 1 313 ? -3.489  16.987  33.635 1.00 64.35  ?  340 LEU   A C    1 
ATOM   2139 O  O    . LEU   A 1 313 ? -4.573  16.718  34.166 1.00 65.66  ?  340 LEU   A O    1 
ATOM   2140 C  CB   . LEU   A 1 313 ? -2.735  15.405  31.841 1.00 67.43  ?  340 LEU   A CB   1 
ATOM   2141 C  CG   . LEU   A 1 313 ? -3.376  14.226  32.576 1.00 72.90  ?  340 LEU   A CG   1 
ATOM   2142 C  CD1  . LEU   A 1 313 ? -4.838  14.083  32.183 1.00 68.77  ?  340 LEU   A CD1  1 
ATOM   2143 C  CD2  . LEU   A 1 313 ? -2.615  12.939  32.301 1.00 67.56  ?  340 LEU   A CD2  1 
ATOM   2144 N  N    . ALA   A 1 314 ? -2.453  17.458  34.332 1.00 59.32  ?  341 ALA   A N    1 
ATOM   2145 C  CA   . ALA   A 1 314 ? -2.581  17.693  35.766 1.00 68.82  ?  341 ALA   A CA   1 
ATOM   2146 C  C    . ALA   A 1 314 ? -3.452  18.906  36.062 1.00 70.21  ?  341 ALA   A C    1 
ATOM   2147 O  O    . ALA   A 1 314 ? -4.116  18.950  37.104 1.00 63.33  ?  341 ALA   A O    1 
ATOM   2148 C  CB   . ALA   A 1 314 ? -1.200  17.866  36.398 1.00 77.73  ?  341 ALA   A CB   1 
ATOM   2149 N  N    . LEU   A 1 315 ? -3.467  19.893  35.169 1.00 70.70  ?  342 LEU   A N    1 
ATOM   2150 C  CA   . LEU   A 1 315 ? -4.243  21.107  35.376 1.00 64.99  ?  342 LEU   A CA   1 
ATOM   2151 C  C    . LEU   A 1 315 ? -5.674  20.998  34.869 1.00 73.35  ?  342 LEU   A C    1 
ATOM   2152 O  O    . LEU   A 1 315 ? -6.433  21.965  34.996 1.00 76.26  ?  342 LEU   A O    1 
ATOM   2153 C  CB   . LEU   A 1 315 ? -3.558  22.300  34.709 1.00 64.56  ?  342 LEU   A CB   1 
ATOM   2154 C  CG   . LEU   A 1 315 ? -2.196  22.691  35.280 1.00 63.72  ?  342 LEU   A CG   1 
ATOM   2155 C  CD1  . LEU   A 1 315 ? -1.653  23.885  34.526 1.00 71.20  ?  342 LEU   A CD1  1 
ATOM   2156 C  CD2  . LEU   A 1 315 ? -2.292  22.982  36.770 1.00 65.87  ?  342 LEU   A CD2  1 
ATOM   2157 N  N    . GLN   A 1 316 ? -6.060  19.858  34.293 1.00 66.81  ?  343 GLN   A N    1 
ATOM   2158 C  CA   . GLN   A 1 316 ? -7.462  19.647  33.955 1.00 65.00  ?  343 GLN   A CA   1 
ATOM   2159 C  C    . GLN   A 1 316 ? -8.335  19.559  35.199 1.00 73.88  ?  343 GLN   A C    1 
ATOM   2160 O  O    . GLN   A 1 316 ? -9.559  19.695  35.097 1.00 78.14  ?  343 GLN   A O    1 
ATOM   2161 C  CB   . GLN   A 1 316 ? -7.620  18.382  33.110 1.00 69.22  ?  343 GLN   A CB   1 
ATOM   2162 C  CG   . GLN   A 1 316 ? -7.543  18.632  31.612 1.00 64.33  ?  343 GLN   A CG   1 
ATOM   2163 C  CD   . GLN   A 1 316 ? -7.114  17.404  30.835 1.00 74.16  ?  343 GLN   A CD   1 
ATOM   2164 O  OE1  . GLN   A 1 316 ? -6.344  17.499  29.879 1.00 84.31  ?  343 GLN   A OE1  1 
ATOM   2165 N  NE2  . GLN   A 1 316 ? -7.616  16.243  31.238 1.00 80.55  ?  343 GLN   A NE2  1 
ATOM   2166 N  N    . ASN   A 1 317 ? -7.730  19.338  36.364 1.00 68.84  ?  344 ASN   A N    1 
ATOM   2167 C  CA   . ASN   A 1 317 ? -8.427  19.311  37.640 1.00 72.55  ?  344 ASN   A CA   1 
ATOM   2168 C  C    . ASN   A 1 317 ? -8.527  20.690  38.282 1.00 80.19  ?  344 ASN   A C    1 
ATOM   2169 O  O    . ASN   A 1 317 ? -8.891  20.787  39.457 1.00 72.93  ?  344 ASN   A O    1 
ATOM   2170 C  CB   . ASN   A 1 317 ? -7.718  18.342  38.594 1.00 63.41  ?  344 ASN   A CB   1 
ATOM   2171 C  CG   . ASN   A 1 317 ? -8.642  17.784  39.658 1.00 77.66  ?  344 ASN   A CG   1 
ATOM   2172 O  OD1  . ASN   A 1 317 ? -9.754  17.346  39.364 1.00 93.87  ?  344 ASN   A OD1  1 
ATOM   2173 N  ND2  . ASN   A 1 317 ? -8.183  17.794  40.904 1.00 73.64  ?  344 ASN   A ND2  1 
ATOM   2174 N  N    . VAL   A 1 318 ? -8.218  21.753  37.543 1.00 77.34  ?  345 VAL   A N    1 
ATOM   2175 C  CA   . VAL   A 1 318 ? -8.148  23.104  38.086 1.00 76.26  ?  345 VAL   A CA   1 
ATOM   2176 C  C    . VAL   A 1 318 ? -9.084  24.008  37.298 1.00 75.26  ?  345 VAL   A C    1 
ATOM   2177 O  O    . VAL   A 1 318 ? -9.144  23.931  36.065 1.00 74.13  ?  345 VAL   A O    1 
ATOM   2178 C  CB   . VAL   A 1 318 ? -6.707  23.656  38.041 1.00 68.93  ?  345 VAL   A CB   1 
ATOM   2179 C  CG1  . VAL   A 1 318 ? -6.639  25.039  38.676 1.00 69.00  ?  345 VAL   A CG1  1 
ATOM   2180 C  CG2  . VAL   A 1 318 ? -5.745  22.699  38.721 1.00 72.16  ?  345 VAL   A CG2  1 
ATOM   2181 N  N    . CYS   A 1 319 ? -9.816  24.862  38.010 1.00 71.85  ?  346 CYS   A N    1 
ATOM   2182 C  CA   A CYS   A 1 319 ? -10.639 25.887  37.373 0.54 78.75  ?  346 CYS   A CA   1 
ATOM   2183 C  CA   B CYS   A 1 319 ? -10.639 25.889  37.374 0.46 85.54  ?  346 CYS   A CA   1 
ATOM   2184 C  C    . CYS   A 1 319 ? -9.710  26.919  36.747 1.00 78.86  ?  346 CYS   A C    1 
ATOM   2185 O  O    . CYS   A 1 319 ? -9.138  27.762  37.440 1.00 83.57  ?  346 CYS   A O    1 
ATOM   2186 C  CB   A CYS   A 1 319 ? -11.585 26.523  38.385 0.54 84.85  ?  346 CYS   A CB   1 
ATOM   2187 C  CB   B CYS   A 1 319 ? -11.577 26.530  38.390 0.46 92.47  ?  346 CYS   A CB   1 
ATOM   2188 S  SG   A CYS   A 1 319 ? -12.709 25.356  39.190 0.54 76.90  ?  346 CYS   A SG   1 
ATOM   2189 S  SG   B CYS   A 1 319 ? -12.298 28.100  37.854 0.46 77.97  ?  346 CYS   A SG   1 
ATOM   2190 N  N    . ASP   A 1 320 ? -9.554  26.849  35.427 1.00 85.33  ?  347 ASP   A N    1 
ATOM   2191 C  CA   . ASP   A 1 320 ? -8.580  27.651  34.689 1.00 76.72  ?  347 ASP   A CA   1 
ATOM   2192 C  C    . ASP   A 1 320 ? -9.181  28.916  34.090 1.00 75.63  ?  347 ASP   A C    1 
ATOM   2193 O  O    . ASP   A 1 320 ? -8.809  29.322  32.985 1.00 80.72  ?  347 ASP   A O    1 
ATOM   2194 C  CB   . ASP   A 1 320 ? -7.939  26.799  33.599 1.00 73.50  ?  347 ASP   A CB   1 
ATOM   2195 C  CG   . ASP   A 1 320 ? -8.939  26.340  32.560 1.00 72.88  ?  347 ASP   A CG   1 
ATOM   2196 O  OD1  . ASP   A 1 320 ? -10.038 25.891  32.951 1.00 73.46  ?  347 ASP   A OD1  1 
ATOM   2197 O  OD2  . ASP   A 1 320 ? -8.630  26.428  31.355 1.00 83.60  ?  347 ASP   A OD2  1 
ATOM   2198 N  N    . ASP   A 1 321 ? -10.105 29.570  34.793 1.00 74.08  ?  348 ASP   A N    1 
ATOM   2199 C  CA   . ASP   A 1 321 ? -10.636 30.832  34.290 1.00 83.87  ?  348 ASP   A CA   1 
ATOM   2200 C  C    . ASP   A 1 321 ? -9.586  31.935  34.345 1.00 79.98  ?  348 ASP   A C    1 
ATOM   2201 O  O    . ASP   A 1 321 ? -9.426  32.698  33.385 1.00 76.20  ?  348 ASP   A O    1 
ATOM   2202 C  CB   . ASP   A 1 321 ? -11.873 31.244  35.086 1.00 73.13  ?  348 ASP   A CB   1 
ATOM   2203 C  CG   . ASP   A 1 321 ? -13.051 30.322  34.857 1.00 80.30  ?  348 ASP   A CG   1 
ATOM   2204 O  OD1  . ASP   A 1 321 ? -12.859 29.238  34.268 1.00 75.33  ?  348 ASP   A OD1  1 
ATOM   2205 O  OD2  . ASP   A 1 321 ? -14.175 30.689  35.262 1.00 83.27  ?  348 ASP   A OD2  1 
ATOM   2206 N  N    . VAL   A 1 322 ? -8.856  32.027  35.455 1.00 83.14  ?  349 VAL   A N    1 
ATOM   2207 C  CA   . VAL   A 1 322 ? -7.940  33.134  35.700 1.00 87.45  ?  349 VAL   A CA   1 
ATOM   2208 C  C    . VAL   A 1 322 ? -6.753  32.608  36.495 1.00 84.50  ?  349 VAL   A C    1 
ATOM   2209 O  O    . VAL   A 1 322 ? -6.866  31.633  37.243 1.00 90.36  ?  349 VAL   A O    1 
ATOM   2210 C  CB   . VAL   A 1 322 ? -8.665  34.290  36.434 1.00 90.26  ?  349 VAL   A CB   1 
ATOM   2211 C  CG1  . VAL   A 1 322 ? -9.187  33.820  37.783 1.00 82.70  ?  349 VAL   A CG1  1 
ATOM   2212 C  CG2  . VAL   A 1 322 ? -7.761  35.509  36.584 1.00 92.12  ?  349 VAL   A CG2  1 
ATOM   2213 N  N    . ASP   A 1 323 ? -5.601  33.253  36.317 1.00 89.18  ?  350 ASP   A N    1 
ATOM   2214 C  CA   . ASP   A 1 323 ? -4.358  32.864  36.981 1.00 92.19  ?  350 ASP   A CA   1 
ATOM   2215 C  C    . ASP   A 1 323 ? -4.187  33.709  38.240 1.00 100.90 ?  350 ASP   A C    1 
ATOM   2216 O  O    . ASP   A 1 323 ? -3.705  34.844  38.179 1.00 111.08 ?  350 ASP   A O    1 
ATOM   2217 C  CB   . ASP   A 1 323 ? -3.170  33.029  36.037 1.00 92.82  ?  350 ASP   A CB   1 
ATOM   2218 C  CG   . ASP   A 1 323 ? -1.880  32.476  36.617 1.00 106.73 ?  350 ASP   A CG   1 
ATOM   2219 O  OD1  . ASP   A 1 323 ? -1.940  31.770  37.645 1.00 112.71 ?  350 ASP   A OD1  1 
ATOM   2220 O  OD2  . ASP   A 1 323 ? -0.806  32.750  36.043 1.00 114.67 ?  350 ASP   A OD2  1 
ATOM   2221 N  N    . ASN   A 1 324 ? -4.580  33.153  39.383 1.00 99.37  ?  351 ASN   A N    1 
ATOM   2222 C  CA   . ASN   A 1 324 ? -4.334  33.781  40.675 1.00 104.86 ?  351 ASN   A CA   1 
ATOM   2223 C  C    . ASN   A 1 324 ? -4.099  32.682  41.706 1.00 117.63 ?  351 ASN   A C    1 
ATOM   2224 O  O    . ASN   A 1 324 ? -4.009  31.498  41.368 1.00 118.99 ?  351 ASN   A O    1 
ATOM   2225 C  CB   . ASN   A 1 324 ? -5.486  34.719  41.067 1.00 111.89 ?  351 ASN   A CB   1 
ATOM   2226 C  CG   . ASN   A 1 324 ? -6.844  34.038  41.035 1.00 108.57 ?  351 ASN   A CG   1 
ATOM   2227 O  OD1  . ASN   A 1 324 ? -6.989  32.880  41.426 1.00 109.15 ?  351 ASN   A OD1  1 
ATOM   2228 N  ND2  . ASN   A 1 324 ? -7.855  34.772  40.586 1.00 97.97  ?  351 ASN   A ND2  1 
ATOM   2229 N  N    . ASP   A 1 325 ? -4.004  33.079  42.974 1.00 116.61 ?  352 ASP   A N    1 
ATOM   2230 C  CA   . ASP   A 1 325 ? -3.724  32.145  44.057 1.00 114.20 ?  352 ASP   A CA   1 
ATOM   2231 C  C    . ASP   A 1 325 ? -4.966  31.421  44.562 1.00 112.02 ?  352 ASP   A C    1 
ATOM   2232 O  O    . ASP   A 1 325 ? -4.842  30.543  45.422 1.00 111.45 ?  352 ASP   A O    1 
ATOM   2233 C  CB   . ASP   A 1 325 ? -3.046  32.879  45.218 1.00 126.75 ?  352 ASP   A CB   1 
ATOM   2234 C  CG   . ASP   A 1 325 ? -1.533  32.880  45.103 1.00 137.21 ?  352 ASP   A CG   1 
ATOM   2235 O  OD1  . ASP   A 1 325 ? -0.988  33.772  44.418 1.00 141.64 ?  352 ASP   A OD1  1 
ATOM   2236 O  OD2  . ASP   A 1 325 ? -0.889  31.991  45.697 1.00 138.03 ?  352 ASP   A OD2  1 
ATOM   2237 N  N    . ASP   A 1 326 ? -6.153  31.762  44.056 1.00 114.15 ?  353 ASP   A N    1 
ATOM   2238 C  CA   . ASP   A 1 326 ? -7.390  31.088  44.452 1.00 114.77 ?  353 ASP   A CA   1 
ATOM   2239 C  C    . ASP   A 1 326 ? -7.543  29.828  43.603 1.00 108.31 ?  353 ASP   A C    1 
ATOM   2240 O  O    . ASP   A 1 326 ? -8.335  29.757  42.660 1.00 113.18 ?  353 ASP   A O    1 
ATOM   2241 C  CB   . ASP   A 1 326 ? -8.585  32.020  44.303 1.00 108.31 ?  353 ASP   A CB   1 
ATOM   2242 N  N    . VAL   A 1 327 ? -6.761  28.813  43.955 1.00 93.74  ?  354 VAL   A N    1 
ATOM   2243 C  CA   . VAL   A 1 327 ? -6.750  27.554  43.219 1.00 90.03  ?  354 VAL   A CA   1 
ATOM   2244 C  C    . VAL   A 1 327 ? -7.885  26.677  43.733 1.00 86.55  ?  354 VAL   A C    1 
ATOM   2245 O  O    . VAL   A 1 327 ? -7.931  26.337  44.920 1.00 95.30  ?  354 VAL   A O    1 
ATOM   2246 C  CB   . VAL   A 1 327 ? -5.394  26.848  43.357 1.00 95.32  ?  354 VAL   A CB   1 
ATOM   2247 C  CG1  . VAL   A 1 327 ? -5.494  25.402  42.902 1.00 82.88  ?  354 VAL   A CG1  1 
ATOM   2248 C  CG2  . VAL   A 1 327 ? -4.326  27.591  42.566 1.00 97.50  ?  354 VAL   A CG2  1 
ATOM   2249 N  N    . SER   A 1 328 ? -8.804  26.315  42.842 1.00 89.54  ?  355 SER   A N    1 
ATOM   2250 C  CA   . SER   A 1 328 ? -9.958  25.488  43.179 1.00 94.01  ?  355 SER   A CA   1 
ATOM   2251 C  C    . SER   A 1 328 ? -9.937  24.241  42.306 1.00 82.88  ?  355 SER   A C    1 
ATOM   2252 O  O    . SER   A 1 328 ? -9.916  24.342  41.075 1.00 92.89  ?  355 SER   A O    1 
ATOM   2253 C  CB   . SER   A 1 328 ? -11.263 26.264  42.990 1.00 89.36  ?  355 SER   A CB   1 
ATOM   2254 O  OG   . SER   A 1 328 ? -11.885 25.935  41.761 1.00 107.90 ?  355 SER   A OG   1 
ATOM   2255 N  N    . LEU   A 1 329 ? -9.950  23.073  42.944 1.00 83.70  ?  356 LEU   A N    1 
ATOM   2256 C  CA   . LEU   A 1 329 ? -9.817  21.794  42.259 1.00 85.98  ?  356 LEU   A CA   1 
ATOM   2257 C  C    . LEU   A 1 329 ? -11.184 21.194  41.961 1.00 85.62  ?  356 LEU   A C    1 
ATOM   2258 O  O    . LEU   A 1 329 ? -12.052 21.144  42.834 1.00 86.77  ?  356 LEU   A O    1 
ATOM   2259 C  CB   . LEU   A 1 329 ? -8.999  20.808  43.096 1.00 80.91  ?  356 LEU   A CB   1 
ATOM   2260 C  CG   . LEU   A 1 329 ? -7.626  21.254  43.594 1.00 83.35  ?  356 LEU   A CG   1 
ATOM   2261 C  CD1  . LEU   A 1 329 ? -6.789  20.038  43.935 1.00 87.29  ?  356 LEU   A CD1  1 
ATOM   2262 C  CD2  . LEU   A 1 329 ? -6.921  22.098  42.548 1.00 81.76  ?  356 LEU   A CD2  1 
ATOM   2263 N  N    . LYS   A 1 330 ? -11.353 20.704  40.728 1.00 89.23  ?  357 LYS   A N    1 
ATOM   2264 C  CA   . LYS   A 1 330 ? -12.650 20.185  40.300 1.00 88.18  ?  357 LYS   A CA   1 
ATOM   2265 C  C    . LYS   A 1 330 ? -13.003 18.882  41.009 1.00 85.69  ?  357 LYS   A C    1 
ATOM   2266 O  O    . LYS   A 1 330 ? -14.161 18.671  41.386 1.00 93.24  ?  357 LYS   A O    1 
ATOM   2267 C  CB   . LYS   A 1 330 ? -12.662 19.980  38.785 1.00 81.47  ?  357 LYS   A CB   1 
ATOM   2268 C  CG   . LYS   A 1 330 ? -12.229 21.191  37.975 1.00 78.44  ?  357 LYS   A CG   1 
ATOM   2269 C  CD   . LYS   A 1 330 ? -13.129 21.378  36.761 1.00 96.92  ?  357 LYS   A CD   1 
ATOM   2270 C  CE   . LYS   A 1 330 ? -12.327 21.427  35.470 1.00 81.02  ?  357 LYS   A CE   1 
ATOM   2271 N  NZ   . LYS   A 1 330 ? -11.679 22.752  35.266 1.00 95.78  ?  357 LYS   A NZ   1 
ATOM   2272 N  N    . SER   A 1 331 ? -12.029 17.993  41.191 1.00 82.65  ?  358 SER   A N    1 
ATOM   2273 C  CA   . SER   A 1 331 ? -12.283 16.677  41.758 1.00 77.41  ?  358 SER   A CA   1 
ATOM   2274 C  C    . SER   A 1 331 ? -11.289 16.376  42.869 1.00 85.59  ?  358 SER   A C    1 
ATOM   2275 O  O    . SER   A 1 331 ? -10.139 16.821  42.836 1.00 93.02  ?  358 SER   A O    1 
ATOM   2276 C  CB   . SER   A 1 331 ? -12.200 15.578  40.687 1.00 75.89  ?  358 SER   A CB   1 
ATOM   2277 O  OG   . SER   A 1 331 ? -12.433 14.298  41.249 1.00 75.35  ?  358 SER   A OG   1 
ATOM   2278 N  N    . PHE   A 1 332 ? -11.752 15.609  43.859 1.00 85.44  ?  359 PHE   A N    1 
ATOM   2279 C  CA   . PHE   A 1 332 ? -10.894 15.087  44.917 1.00 88.80  ?  359 PHE   A CA   1 
ATOM   2280 C  C    . PHE   A 1 332 ? -10.856 13.565  44.913 1.00 84.43  ?  359 PHE   A C    1 
ATOM   2281 O  O    . PHE   A 1 332 ? -10.563 12.949  45.943 1.00 81.54  ?  359 PHE   A O    1 
ATOM   2282 C  CB   . PHE   A 1 332 ? -11.339 15.597  46.286 1.00 79.79  ?  359 PHE   A CB   1 
ATOM   2283 C  CG   . PHE   A 1 332 ? -11.120 17.062  46.479 1.00 87.30  ?  359 PHE   A CG   1 
ATOM   2284 C  CD1  . PHE   A 1 332 ? -9.868  17.544  46.821 1.00 93.89  ?  359 PHE   A CD1  1 
ATOM   2285 C  CD2  . PHE   A 1 332 ? -12.161 17.958  46.324 1.00 90.10  ?  359 PHE   A CD2  1 
ATOM   2286 C  CE1  . PHE   A 1 332 ? -9.658  18.897  47.000 1.00 87.15  ?  359 PHE   A CE1  1 
ATOM   2287 C  CE2  . PHE   A 1 332 ? -11.959 19.313  46.504 1.00 87.08  ?  359 PHE   A CE2  1 
ATOM   2288 C  CZ   . PHE   A 1 332 ? -10.705 19.783  46.843 1.00 84.34  ?  359 PHE   A CZ   1 
ATOM   2289 N  N    . GLU   A 1 333 ? -11.161 12.951  43.781 1.00 85.55  ?  360 GLU   A N    1 
ATOM   2290 C  CA   . GLU   A 1 333 ? -11.058 11.506  43.659 1.00 90.43  ?  360 GLU   A CA   1 
ATOM   2291 C  C    . GLU   A 1 333 ? -9.596  11.095  43.811 1.00 92.73  ?  360 GLU   A C    1 
ATOM   2292 O  O    . GLU   A 1 333 ? -8.718  11.704  43.183 1.00 86.81  ?  360 GLU   A O    1 
ATOM   2293 C  CB   . GLU   A 1 333 ? -11.652 11.076  42.311 1.00 93.48  ?  360 GLU   A CB   1 
ATOM   2294 C  CG   . GLU   A 1 333 ? -12.946 10.247  42.253 1.00 102.81 ?  360 GLU   A CG   1 
ATOM   2295 C  CD   . GLU   A 1 333 ? -13.596 10.190  40.885 1.00 116.82 ?  360 GLU   A CD   1 
ATOM   2296 O  OE1  . GLU   A 1 333 ? -14.313 11.146  40.536 1.00 116.49 ?  360 GLU   A OE1  1 
ATOM   2297 O  OE2  . GLU   A 1 333 ? -13.478 9.163   40.207 1.00 111.56 ?  360 GLU   A OE2  1 
ATOM   2298 N  N    . PRO   A 1 334 ? -9.293  10.119  44.674 1.00 104.04 ?  361 PRO   A N    1 
ATOM   2299 C  CA   . PRO   A 1 334 ? -7.898  9.684   44.881 1.00 85.93  ?  361 PRO   A CA   1 
ATOM   2300 C  C    . PRO   A 1 334 ? -7.034  9.537   43.633 1.00 85.27  ?  361 PRO   A C    1 
ATOM   2301 O  O    . PRO   A 1 334 ? -5.917  10.067  43.624 1.00 87.67  ?  361 PRO   A O    1 
ATOM   2302 C  CB   . PRO   A 1 334 ? -8.085  8.353   45.621 1.00 93.02  ?  361 PRO   A CB   1 
ATOM   2303 C  CG   . PRO   A 1 334 ? -9.312  8.611   46.452 1.00 101.90 ?  361 PRO   A CG   1 
ATOM   2304 C  CD   . PRO   A 1 334 ? -10.220 9.466   45.613 1.00 95.86  ?  361 PRO   A CD   1 
ATOM   2305 N  N    . ALA   A 1 335 ? -7.489  8.850   42.585 1.00 80.37  ?  362 ALA   A N    1 
ATOM   2306 C  CA   . ALA   A 1 335 ? -6.587  8.603   41.462 1.00 80.80  ?  362 ALA   A CA   1 
ATOM   2307 C  C    . ALA   A 1 335 ? -6.271  9.889   40.702 1.00 81.55  ?  362 ALA   A C    1 
ATOM   2308 O  O    . ALA   A 1 335 ? -5.167  10.041  40.165 1.00 76.87  ?  362 ALA   A O    1 
ATOM   2309 C  CB   . ALA   A 1 335 ? -7.168  7.545   40.524 1.00 61.97  ?  362 ALA   A CB   1 
ATOM   2310 N  N    . VAL   A 1 336 ? -7.216  10.831  40.652 1.00 83.84  ?  363 VAL   A N    1 
ATOM   2311 C  CA   . VAL   A 1 336 ? -6.935  12.105  39.995 1.00 88.14  ?  363 VAL   A CA   1 
ATOM   2312 C  C    . VAL   A 1 336 ? -5.914  12.904  40.798 1.00 82.19  ?  363 VAL   A C    1 
ATOM   2313 O  O    . VAL   A 1 336 ? -5.053  13.585  40.228 1.00 68.98  ?  363 VAL   A O    1 
ATOM   2314 C  CB   . VAL   A 1 336 ? -8.233  12.904  39.773 1.00 70.89  ?  363 VAL   A CB   1 
ATOM   2315 C  CG1  . VAL   A 1 336 ? -7.945  14.158  38.958 1.00 71.39  ?  363 VAL   A CG1  1 
ATOM   2316 C  CG2  . VAL   A 1 336 ? -9.275  12.047  39.076 1.00 82.75  ?  363 VAL   A CG2  1 
ATOM   2317 N  N    . LEU   A 1 337 ? -5.987  12.830  42.129 1.00 83.41  ?  364 LEU   A N    1 
ATOM   2318 C  CA   . LEU   A 1 337 ? -5.025  13.538  42.967 1.00 69.98  ?  364 LEU   A CA   1 
ATOM   2319 C  C    . LEU   A 1 337 ? -3.679  12.824  42.995 1.00 71.80  ?  364 LEU   A C    1 
ATOM   2320 O  O    . LEU   A 1 337 ? -2.630  13.476  43.058 1.00 72.07  ?  364 LEU   A O    1 
ATOM   2321 C  CB   . LEU   A 1 337 ? -5.579  13.695  44.382 1.00 65.96  ?  364 LEU   A CB   1 
ATOM   2322 C  CG   . LEU   A 1 337 ? -6.876  14.498  44.488 1.00 66.43  ?  364 LEU   A CG   1 
ATOM   2323 C  CD1  . LEU   A 1 337 ? -7.363  14.531  45.923 1.00 72.50  ?  364 LEU   A CD1  1 
ATOM   2324 C  CD2  . LEU   A 1 337 ? -6.678  15.907  43.953 1.00 78.32  ?  364 LEU   A CD2  1 
ATOM   2325 N  N    . LYS   A 1 338 ? -3.692  11.489  42.966 1.00 84.64  ?  365 LYS   A N    1 
ATOM   2326 C  CA   . LYS   A 1 338 ? -2.456  10.731  42.801 1.00 72.53  ?  365 LYS   A CA   1 
ATOM   2327 C  C    . LYS   A 1 338 ? -1.738  11.139  41.522 1.00 69.53  ?  365 LYS   A C    1 
ATOM   2328 O  O    . LYS   A 1 338 ? -0.526  11.383  41.521 1.00 73.74  ?  365 LYS   A O    1 
ATOM   2329 C  CB   . LYS   A 1 338 ? -2.766  9.233   42.785 1.00 75.57  ?  365 LYS   A CB   1 
ATOM   2330 C  CG   . LYS   A 1 338 ? -1.606  8.330   43.170 1.00 79.02  ?  365 LYS   A CG   1 
ATOM   2331 C  CD   . LYS   A 1 338 ? -2.005  6.863   43.073 1.00 85.62  ?  365 LYS   A CD   1 
ATOM   2332 C  CE   . LYS   A 1 338 ? -0.792  5.946   43.086 1.00 83.64  ?  365 LYS   A CE   1 
ATOM   2333 N  NZ   . LYS   A 1 338 ? -0.336  5.657   44.473 1.00 90.53  ?  365 LYS   A NZ   1 
ATOM   2334 N  N    . GLN   A 1 339 ? -2.484  11.224  40.420 1.00 67.58  ?  366 GLN   A N    1 
ATOM   2335 C  CA   . GLN   A 1 339 ? -1.900  11.615  39.143 1.00 66.93  ?  366 GLN   A CA   1 
ATOM   2336 C  C    . GLN   A 1 339 ? -1.383  13.047  39.185 1.00 73.65  ?  366 GLN   A C    1 
ATOM   2337 O  O    . GLN   A 1 339 ? -0.359  13.364  38.569 1.00 75.54  ?  366 GLN   A O    1 
ATOM   2338 C  CB   . GLN   A 1 339 ? -2.941  11.447  38.037 1.00 68.16  ?  366 GLN   A CB   1 
ATOM   2339 C  CG   . GLN   A 1 339 ? -2.465  11.790  36.640 1.00 69.56  ?  366 GLN   A CG   1 
ATOM   2340 C  CD   . GLN   A 1 339 ? -3.507  11.464  35.588 1.00 67.81  ?  366 GLN   A CD   1 
ATOM   2341 O  OE1  . GLN   A 1 339 ? -3.332  10.545  34.790 1.00 76.61  ?  366 GLN   A OE1  1 
ATOM   2342 N  NE2  . GLN   A 1 339 ? -4.603  12.214  35.588 1.00 64.33  ?  366 GLN   A NE2  1 
ATOM   2343 N  N    . GLY   A 1 340 ? -2.073  13.926  39.914 1.00 58.55  ?  367 GLY   A N    1 
ATOM   2344 C  CA   . GLY   A 1 340 ? -1.655  15.317  39.968 1.00 66.25  ?  367 GLY   A CA   1 
ATOM   2345 C  C    . GLY   A 1 340 ? -0.336  15.511  40.690 1.00 67.44  ?  367 GLY   A C    1 
ATOM   2346 O  O    . GLY   A 1 340 ? 0.539   16.242  40.217 1.00 69.78  ?  367 GLY   A O    1 
ATOM   2347 N  N    . GLU   A 1 341 ? -0.171  14.862  41.844 1.00 68.38  ?  368 GLU   A N    1 
ATOM   2348 C  CA   . GLU   A 1 341 ? 1.058   15.012  42.612 1.00 70.34  ?  368 GLU   A CA   1 
ATOM   2349 C  C    . GLU   A 1 341 ? 2.224   14.234  42.017 1.00 71.39  ?  368 GLU   A C    1 
ATOM   2350 O  O    . GLU   A 1 341 ? 3.381   14.572  42.294 1.00 72.39  ?  368 GLU   A O    1 
ATOM   2351 C  CB   . GLU   A 1 341 ? 0.827   14.584  44.062 1.00 72.05  ?  368 GLU   A CB   1 
ATOM   2352 C  CG   . GLU   A 1 341 ? -0.225  15.413  44.782 1.00 72.44  ?  368 GLU   A CG   1 
ATOM   2353 C  CD   . GLU   A 1 341 ? 0.026   16.905  44.662 1.00 77.75  ?  368 GLU   A CD   1 
ATOM   2354 O  OE1  . GLU   A 1 341 ? 1.094   17.370  45.111 1.00 80.77  ?  368 GLU   A OE1  1 
ATOM   2355 O  OE2  . GLU   A 1 341 ? -0.845  17.614  44.114 1.00 81.14  ?  368 GLU   A OE2  1 
ATOM   2356 N  N    . GLU   A 1 342 ? 1.954   13.204  41.211 1.00 67.94  ?  369 GLU   A N    1 
ATOM   2357 C  CA   . GLU   A 1 342 ? 3.038   12.513  40.520 1.00 66.65  ?  369 GLU   A CA   1 
ATOM   2358 C  C    . GLU   A 1 342 ? 3.581   13.355  39.373 1.00 68.85  ?  369 GLU   A C    1 
ATOM   2359 O  O    . GLU   A 1 342 ? 4.800   13.438  39.178 1.00 63.21  ?  369 GLU   A O    1 
ATOM   2360 C  CB   . GLU   A 1 342 ? 2.561   11.152  40.012 1.00 64.73  ?  369 GLU   A CB   1 
ATOM   2361 C  CG   . GLU   A 1 342 ? 2.425   10.096  41.097 1.00 63.51  ?  369 GLU   A CG   1 
ATOM   2362 C  CD   . GLU   A 1 342 ? 1.685   8.861   40.621 1.00 76.30  ?  369 GLU   A CD   1 
ATOM   2363 O  OE1  . GLU   A 1 342 ? 1.256   8.837   39.448 1.00 62.39  ?  369 GLU   A OE1  1 
ATOM   2364 O  OE2  . GLU   A 1 342 ? 1.535   7.912   41.420 1.00 84.59  ?  369 GLU   A OE2  1 
ATOM   2365 N  N    . ILE   A 1 343 ? 2.692   13.982  38.598 1.00 69.65  ?  370 ILE   A N    1 
ATOM   2366 C  CA   . ILE   A 1 343 ? 3.131   14.930  37.580 1.00 59.04  ?  370 ILE   A CA   1 
ATOM   2367 C  C    . ILE   A 1 343 ? 3.846   16.105  38.229 1.00 63.21  ?  370 ILE   A C    1 
ATOM   2368 O  O    . ILE   A 1 343 ? 4.813   16.642  37.673 1.00 65.39  ?  370 ILE   A O    1 
ATOM   2369 C  CB   . ILE   A 1 343 ? 1.930   15.391  36.729 1.00 56.83  ?  370 ILE   A CB   1 
ATOM   2370 C  CG1  . ILE   A 1 343 ? 1.326   14.205  35.976 1.00 65.01  ?  370 ILE   A CG1  1 
ATOM   2371 C  CG2  . ILE   A 1 343 ? 2.342   16.480  35.751 1.00 55.71  ?  370 ILE   A CG2  1 
ATOM   2372 C  CD1  . ILE   A 1 343 ? -0.006  14.508  35.324 1.00 61.34  ?  370 ILE   A CD1  1 
ATOM   2373 N  N    . HIS   A 1 344 ? 3.394   16.515  39.419 1.00 71.47  ?  371 HIS   A N    1 
ATOM   2374 C  CA   . HIS   A 1 344 ? 4.076   17.569  40.164 1.00 69.40  ?  371 HIS   A CA   1 
ATOM   2375 C  C    . HIS   A 1 344 ? 5.530   17.198  40.432 1.00 64.63  ?  371 HIS   A C    1 
ATOM   2376 O  O    . HIS   A 1 344 ? 6.434   18.022  40.249 1.00 72.64  ?  371 HIS   A O    1 
ATOM   2377 C  CB   . HIS   A 1 344 ? 3.323   17.835  41.472 1.00 66.91  ?  371 HIS   A CB   1 
ATOM   2378 C  CG   . HIS   A 1 344 ? 3.837   19.006  42.256 1.00 70.48  ?  371 HIS   A CG   1 
ATOM   2379 N  ND1  . HIS   A 1 344 ? 3.236   19.435  43.420 1.00 71.82  ?  371 HIS   A ND1  1 
ATOM   2380 C  CD2  . HIS   A 1 344 ? 4.890   19.832  42.052 1.00 74.40  ?  371 HIS   A CD2  1 
ATOM   2381 C  CE1  . HIS   A 1 344 ? 3.896   20.475  43.898 1.00 69.57  ?  371 HIS   A CE1  1 
ATOM   2382 N  NE2  . HIS   A 1 344 ? 4.905   20.736  43.087 1.00 75.95  ?  371 HIS   A NE2  1 
ATOM   2383 N  N    . ASN   A 1 345 ? 5.777   15.954  40.849 1.00 59.56  ?  372 ASN   A N    1 
ATOM   2384 C  CA   . ASN   A 1 345 ? 7.147   15.521  41.099 1.00 58.30  ?  372 ASN   A CA   1 
ATOM   2385 C  C    . ASN   A 1 345 ? 7.940   15.388  39.806 1.00 57.73  ?  372 ASN   A C    1 
ATOM   2386 O  O    . ASN   A 1 345 ? 9.152   15.635  39.797 1.00 74.84  ?  372 ASN   A O    1 
ATOM   2387 C  CB   . ASN   A 1 345 ? 7.150   14.193  41.856 1.00 55.89  ?  372 ASN   A CB   1 
ATOM   2388 C  CG   . ASN   A 1 345 ? 6.699   14.341  43.296 1.00 70.46  ?  372 ASN   A CG   1 
ATOM   2389 O  OD1  . ASN   A 1 345 ? 6.541   15.453  43.799 1.00 68.85  ?  372 ASN   A OD1  1 
ATOM   2390 N  ND2  . ASN   A 1 345 ? 6.492   13.215  43.969 1.00 67.11  ?  372 ASN   A ND2  1 
ATOM   2391 N  N    . GLU   A 1 346 ? 7.281   15.009  38.709 1.00 56.57  ?  373 GLU   A N    1 
ATOM   2392 C  CA   . GLU   A 1 346 ? 8.000   14.765  37.463 1.00 67.69  ?  373 GLU   A CA   1 
ATOM   2393 C  C    . GLU   A 1 346 ? 8.587   16.054  36.898 1.00 66.96  ?  373 GLU   A C    1 
ATOM   2394 O  O    . GLU   A 1 346 ? 9.759   16.093  36.509 1.00 61.67  ?  373 GLU   A O    1 
ATOM   2395 C  CB   . GLU   A 1 346 ? 7.077   14.096  36.443 1.00 58.93  ?  373 GLU   A CB   1 
ATOM   2396 C  CG   . GLU   A 1 346 ? 7.822   13.364  35.335 1.00 57.88  ?  373 GLU   A CG   1 
ATOM   2397 C  CD   . GLU   A 1 346 ? 6.900   12.809  34.267 1.00 73.20  ?  373 GLU   A CD   1 
ATOM   2398 O  OE1  . GLU   A 1 346 ? 5.676   12.731  34.509 1.00 60.21  ?  373 GLU   A OE1  1 
ATOM   2399 O  OE2  . GLU   A 1 346 ? 7.402   12.441  33.185 1.00 64.62  ?  373 GLU   A OE2  1 
ATOM   2400 N  N    . VAL   A 1 347 ? 7.789   17.123  36.848 1.00 53.27  ?  374 VAL   A N    1 
ATOM   2401 C  CA   . VAL   A 1 347 ? 8.276   18.371  36.267 1.00 59.01  ?  374 VAL   A CA   1 
ATOM   2402 C  C    . VAL   A 1 347 ? 9.340   18.999  37.160 1.00 59.82  ?  374 VAL   A C    1 
ATOM   2403 O  O    . VAL   A 1 347 ? 10.333  19.551  36.671 1.00 55.39  ?  374 VAL   A O    1 
ATOM   2404 C  CB   . VAL   A 1 347 ? 7.106   19.340  36.010 1.00 66.25  ?  374 VAL   A CB   1 
ATOM   2405 C  CG1  . VAL   A 1 347 ? 6.194   19.417  37.222 1.00 79.29  ?  374 VAL   A CG1  1 
ATOM   2406 C  CG2  . VAL   A 1 347 ? 7.621   20.722  35.632 1.00 61.40  ?  374 VAL   A CG2  1 
ATOM   2407 N  N    . GLU   A 1 348 ? 9.161   18.912  38.481 1.00 58.94  ?  375 GLU   A N    1 
ATOM   2408 C  CA   . GLU   A 1 348 ? 10.110  19.536  39.397 1.00 65.32  ?  375 GLU   A CA   1 
ATOM   2409 C  C    . GLU   A 1 348 ? 11.484  18.885  39.301 1.00 64.61  ?  375 GLU   A C    1 
ATOM   2410 O  O    . GLU   A 1 348 ? 12.499  19.572  39.146 1.00 63.81  ?  375 GLU   A O    1 
ATOM   2411 C  CB   . GLU   A 1 348 ? 9.594   19.460  40.834 1.00 71.03  ?  375 GLU   A CB   1 
ATOM   2412 C  CG   . GLU   A 1 348 ? 10.603  19.975  41.855 1.00 70.57  ?  375 GLU   A CG   1 
ATOM   2413 C  CD   . GLU   A 1 348 ? 10.030  20.105  43.252 1.00 72.69  ?  375 GLU   A CD   1 
ATOM   2414 O  OE1  . GLU   A 1 348 ? 8.814   19.884  43.425 1.00 74.88  ?  375 GLU   A OE1  1 
ATOM   2415 O  OE2  . GLU   A 1 348 ? 10.802  20.424  44.181 1.00 75.11  ?  375 GLU   A OE2  1 
ATOM   2416 N  N    . PHE   A 1 349 ? 11.536  17.558  39.388 1.00 61.46  ?  376 PHE   A N    1 
ATOM   2417 C  CA   . PHE   A 1 349 ? 12.795  16.844  39.559 1.00 61.89  ?  376 PHE   A CA   1 
ATOM   2418 C  C    . PHE   A 1 349 ? 13.405  16.363  38.251 1.00 67.14  ?  376 PHE   A C    1 
ATOM   2419 O  O    . PHE   A 1 349 ? 14.627  16.432  38.086 1.00 76.87  ?  376 PHE   A O    1 
ATOM   2420 C  CB   . PHE   A 1 349 ? 12.591  15.654  40.500 1.00 63.26  ?  376 PHE   A CB   1 
ATOM   2421 C  CG   . PHE   A 1 349 ? 12.110  16.048  41.864 1.00 73.60  ?  376 PHE   A CG   1 
ATOM   2422 C  CD1  . PHE   A 1 349 ? 12.777  17.018  42.593 1.00 67.98  ?  376 PHE   A CD1  1 
ATOM   2423 C  CD2  . PHE   A 1 349 ? 10.980  15.464  42.411 1.00 75.65  ?  376 PHE   A CD2  1 
ATOM   2424 C  CE1  . PHE   A 1 349 ? 12.335  17.390  43.846 1.00 67.08  ?  376 PHE   A CE1  1 
ATOM   2425 C  CE2  . PHE   A 1 349 ? 10.531  15.832  43.666 1.00 78.44  ?  376 PHE   A CE2  1 
ATOM   2426 C  CZ   . PHE   A 1 349 ? 11.211  16.797  44.384 1.00 70.02  ?  376 PHE   A CZ   1 
ATOM   2427 N  N    . GLU   A 1 350 ? 12.595  15.871  37.315 1.00 62.96  ?  377 GLU   A N    1 
ATOM   2428 C  CA   . GLU   A 1 350 ? 13.137  15.399  36.048 1.00 59.81  ?  377 GLU   A CA   1 
ATOM   2429 C  C    . GLU   A 1 350 ? 13.437  16.528  35.072 1.00 59.87  ?  377 GLU   A C    1 
ATOM   2430 O  O    . GLU   A 1 350 ? 14.131  16.293  34.078 1.00 70.35  ?  377 GLU   A O    1 
ATOM   2431 C  CB   . GLU   A 1 350 ? 12.175  14.405  35.392 1.00 62.71  ?  377 GLU   A CB   1 
ATOM   2432 C  CG   . GLU   A 1 350 ? 12.077  13.064  36.099 1.00 68.94  ?  377 GLU   A CG   1 
ATOM   2433 C  CD   . GLU   A 1 350 ? 13.429  12.416  36.327 1.00 85.11  ?  377 GLU   A CD   1 
ATOM   2434 O  OE1  . GLU   A 1 350 ? 14.261  12.416  35.394 1.00 61.10  ?  377 GLU   A OE1  1 
ATOM   2435 O  OE2  . GLU   A 1 350 ? 13.658  11.903  37.443 1.00 78.67  ?  377 GLU   A OE2  1 
ATOM   2436 N  N    . TRP   A 1 351 ? 12.946  17.741  35.326 1.00 59.93  ?  378 TRP   A N    1 
ATOM   2437 C  CA   . TRP   A 1 351 ? 13.132  18.826  34.371 1.00 65.08  ?  378 TRP   A CA   1 
ATOM   2438 C  C    . TRP   A 1 351 ? 13.681  20.086  35.029 1.00 67.73  ?  378 TRP   A C    1 
ATOM   2439 O  O    . TRP   A 1 351 ? 14.754  20.565  34.651 1.00 74.42  ?  378 TRP   A O    1 
ATOM   2440 C  CB   . TRP   A 1 351 ? 11.813  19.128  33.655 1.00 58.46  ?  378 TRP   A CB   1 
ATOM   2441 C  CG   . TRP   A 1 351 ? 11.387  18.014  32.754 1.00 55.20  ?  378 TRP   A CG   1 
ATOM   2442 C  CD1  . TRP   A 1 351 ? 10.738  16.869  33.116 1.00 56.23  ?  378 TRP   A CD1  1 
ATOM   2443 C  CD2  . TRP   A 1 351 ? 11.606  17.921  31.341 1.00 55.42  ?  378 TRP   A CD2  1 
ATOM   2444 N  NE1  . TRP   A 1 351 ? 10.529  16.075  32.015 1.00 57.88  ?  378 TRP   A NE1  1 
ATOM   2445 C  CE2  . TRP   A 1 351 ? 11.053  16.697  30.913 1.00 59.17  ?  378 TRP   A CE2  1 
ATOM   2446 C  CE3  . TRP   A 1 351 ? 12.210  18.755  30.396 1.00 63.33  ?  378 TRP   A CE3  1 
ATOM   2447 C  CZ2  . TRP   A 1 351 ? 11.086  16.289  29.582 1.00 56.59  ?  378 TRP   A CZ2  1 
ATOM   2448 C  CZ3  . TRP   A 1 351 ? 12.242  18.348  29.075 1.00 65.21  ?  378 TRP   A CZ3  1 
ATOM   2449 C  CH2  . TRP   A 1 351 ? 11.684  17.125  28.680 1.00 66.14  ?  378 TRP   A CH2  1 
ATOM   2450 N  N    . LEU   A 1 352 ? 12.962  20.628  36.013 1.00 61.31  ?  379 LEU   A N    1 
ATOM   2451 C  CA   . LEU   A 1 352 ? 13.352  21.908  36.599 1.00 67.11  ?  379 LEU   A CA   1 
ATOM   2452 C  C    . LEU   A 1 352 ? 14.705  21.812  37.297 1.00 70.13  ?  379 LEU   A C    1 
ATOM   2453 O  O    . LEU   A 1 352 ? 15.663  22.496  36.919 1.00 64.72  ?  379 LEU   A O    1 
ATOM   2454 C  CB   . LEU   A 1 352 ? 12.273  22.392  37.568 1.00 67.01  ?  379 LEU   A CB   1 
ATOM   2455 C  CG   . LEU   A 1 352 ? 11.071  23.073  36.913 1.00 69.28  ?  379 LEU   A CG   1 
ATOM   2456 C  CD1  . LEU   A 1 352 ? 10.079  23.544  37.965 1.00 68.57  ?  379 LEU   A CD1  1 
ATOM   2457 C  CD2  . LEU   A 1 352 ? 11.526  24.231  36.037 1.00 61.48  ?  379 LEU   A CD2  1 
ATOM   2458 N  N    . ARG   A 1 353 ? 14.802  20.965  38.324 1.00 67.94  ?  380 ARG   A N    1 
ATOM   2459 C  CA   . ARG   A 1 353 ? 16.051  20.865  39.073 1.00 71.06  ?  380 ARG   A CA   1 
ATOM   2460 C  C    . ARG   A 1 353 ? 17.175  20.281  38.228 1.00 77.76  ?  380 ARG   A C    1 
ATOM   2461 O  O    . ARG   A 1 353 ? 18.345  20.614  38.445 1.00 72.36  ?  380 ARG   A O    1 
ATOM   2462 C  CB   . ARG   A 1 353 ? 15.845  20.035  40.341 1.00 65.50  ?  380 ARG   A CB   1 
ATOM   2463 C  CG   . ARG   A 1 353 ? 14.703  20.531  41.209 1.00 69.12  ?  380 ARG   A CG   1 
ATOM   2464 C  CD   . ARG   A 1 353 ? 14.834  20.065  42.650 1.00 68.95  ?  380 ARG   A CD   1 
ATOM   2465 N  NE   . ARG   A 1 353 ? 13.848  20.710  43.510 1.00 76.72  ?  380 ARG   A NE   1 
ATOM   2466 C  CZ   . ARG   A 1 353 ? 13.906  21.975  43.905 1.00 89.91  ?  380 ARG   A CZ   1 
ATOM   2467 N  NH1  . ARG   A 1 353 ? 14.914  22.762  43.564 1.00 94.38  ?  380 ARG   A NH1  1 
ATOM   2468 N  NH2  . ARG   A 1 353 ? 12.927  22.465  44.661 1.00 84.24  ?  380 ARG   A NH2  1 
ATOM   2469 N  N    . GLN   A 1 354 ? 16.849  19.417  37.263 1.00 68.08  ?  381 GLN   A N    1 
ATOM   2470 C  CA   . GLN   A 1 354 ? 17.873  18.909  36.356 1.00 61.62  ?  381 GLN   A CA   1 
ATOM   2471 C  C    . GLN   A 1 354 ? 18.440  20.024  35.488 1.00 73.17  ?  381 GLN   A C    1 
ATOM   2472 O  O    . GLN   A 1 354 ? 19.651  20.078  35.243 1.00 80.82  ?  381 GLN   A O    1 
ATOM   2473 C  CB   . GLN   A 1 354 ? 17.299  17.795  35.481 1.00 60.98  ?  381 GLN   A CB   1 
ATOM   2474 C  CG   . GLN   A 1 354 ? 17.231  16.437  36.157 1.00 57.05  ?  381 GLN   A CG   1 
ATOM   2475 C  CD   . GLN   A 1 354 ? 18.545  15.684  36.085 1.00 64.71  ?  381 GLN   A CD   1 
ATOM   2476 O  OE1  . GLN   A 1 354 ? 19.526  16.176  35.527 1.00 66.43  ?  381 GLN   A OE1  1 
ATOM   2477 N  NE2  . GLN   A 1 354 ? 18.570  14.483  36.650 1.00 65.94  ?  381 GLN   A NE2  1 
ATOM   2478 N  N    . PHE   A 1 355 ? 17.578  20.927  35.017 1.00 77.08  ?  382 PHE   A N    1 
ATOM   2479 C  CA   . PHE   A 1 355 ? 18.025  22.006  34.143 1.00 66.11  ?  382 PHE   A CA   1 
ATOM   2480 C  C    . PHE   A 1 355 ? 18.905  22.997  34.894 1.00 68.51  ?  382 PHE   A C    1 
ATOM   2481 O  O    . PHE   A 1 355 ? 20.029  23.290  34.472 1.00 79.53  ?  382 PHE   A O    1 
ATOM   2482 C  CB   . PHE   A 1 355 ? 16.814  22.715  33.536 1.00 70.78  ?  382 PHE   A CB   1 
ATOM   2483 C  CG   . PHE   A 1 355 ? 17.167  23.812  32.572 1.00 68.38  ?  382 PHE   A CG   1 
ATOM   2484 C  CD1  . PHE   A 1 355 ? 17.349  23.535  31.228 1.00 62.86  ?  382 PHE   A CD1  1 
ATOM   2485 C  CD2  . PHE   A 1 355 ? 17.304  25.122  33.007 1.00 70.71  ?  382 PHE   A CD2  1 
ATOM   2486 C  CE1  . PHE   A 1 355 ? 17.669  24.541  30.336 1.00 78.14  ?  382 PHE   A CE1  1 
ATOM   2487 C  CE2  . PHE   A 1 355 ? 17.625  26.132  32.120 1.00 72.75  ?  382 PHE   A CE2  1 
ATOM   2488 C  CZ   . PHE   A 1 355 ? 17.807  25.841  30.782 1.00 62.97  ?  382 PHE   A CZ   1 
ATOM   2489 N  N    . TRP   A 1 356 ? 18.406  23.528  36.012 1.00 70.06  ?  383 TRP   A N    1 
ATOM   2490 C  CA   . TRP   A 1 356 ? 19.135  24.556  36.742 1.00 77.91  ?  383 TRP   A CA   1 
ATOM   2491 C  C    . TRP   A 1 356 ? 20.315  24.004  37.530 1.00 76.74  ?  383 TRP   A C    1 
ATOM   2492 O  O    . TRP   A 1 356 ? 21.148  24.792  37.992 1.00 86.00  ?  383 TRP   A O    1 
ATOM   2493 C  CB   . TRP   A 1 356 ? 18.181  25.305  37.671 1.00 85.78  ?  383 TRP   A CB   1 
ATOM   2494 C  CG   . TRP   A 1 356 ? 17.159  26.114  36.929 1.00 88.74  ?  383 TRP   A CG   1 
ATOM   2495 C  CD1  . TRP   A 1 356 ? 15.807  25.932  36.938 1.00 81.85  ?  383 TRP   A CD1  1 
ATOM   2496 C  CD2  . TRP   A 1 356 ? 17.409  27.230  36.065 1.00 89.20  ?  383 TRP   A CD2  1 
ATOM   2497 N  NE1  . TRP   A 1 356 ? 15.199  26.867  36.134 1.00 82.74  ?  383 TRP   A NE1  1 
ATOM   2498 C  CE2  . TRP   A 1 356 ? 16.160  27.675  35.588 1.00 85.15  ?  383 TRP   A CE2  1 
ATOM   2499 C  CE3  . TRP   A 1 356 ? 18.566  27.896  35.651 1.00 89.26  ?  383 TRP   A CE3  1 
ATOM   2500 C  CZ2  . TRP   A 1 356 ? 16.036  28.756  34.717 1.00 99.79  ?  383 TRP   A CZ2  1 
ATOM   2501 C  CZ3  . TRP   A 1 356 ? 18.441  28.969  34.785 1.00 95.65  ?  383 TRP   A CZ3  1 
ATOM   2502 C  CH2  . TRP   A 1 356 ? 17.186  29.388  34.328 1.00 102.55 ?  383 TRP   A CH2  1 
ATOM   2503 N  N    . PHE   A 1 357 ? 20.410  22.682  37.697 1.00 80.07  ?  384 PHE   A N    1 
ATOM   2504 C  CA   . PHE   A 1 357 ? 21.612  22.096  38.277 1.00 88.87  ?  384 PHE   A CA   1 
ATOM   2505 C  C    . PHE   A 1 357 ? 22.837  22.351  37.412 1.00 90.97  ?  384 PHE   A C    1 
ATOM   2506 O  O    . PHE   A 1 357 ? 23.961  22.351  37.926 1.00 90.80  ?  384 PHE   A O    1 
ATOM   2507 C  CB   . PHE   A 1 357 ? 21.423  20.591  38.483 1.00 78.48  ?  384 PHE   A CB   1 
ATOM   2508 C  CG   . PHE   A 1 357 ? 22.567  19.922  39.191 1.00 75.67  ?  384 PHE   A CG   1 
ATOM   2509 C  CD1  . PHE   A 1 357 ? 22.709  20.034  40.565 1.00 86.39  ?  384 PHE   A CD1  1 
ATOM   2510 C  CD2  . PHE   A 1 357 ? 23.493  19.172  38.486 1.00 74.88  ?  384 PHE   A CD2  1 
ATOM   2511 C  CE1  . PHE   A 1 357 ? 23.759  19.418  41.221 1.00 87.22  ?  384 PHE   A CE1  1 
ATOM   2512 C  CE2  . PHE   A 1 357 ? 24.545  18.553  39.136 1.00 76.70  ?  384 PHE   A CE2  1 
ATOM   2513 C  CZ   . PHE   A 1 357 ? 24.678  18.675  40.505 1.00 88.52  ?  384 PHE   A CZ   1 
ATOM   2514 N  N    . GLN   A 1 358 ? 22.644  22.570  36.111 1.00 83.72  ?  385 GLN   A N    1 
ATOM   2515 C  CA   . GLN   A 1 358 ? 23.763  22.883  35.234 1.00 94.37  ?  385 GLN   A CA   1 
ATOM   2516 C  C    . GLN   A 1 358 ? 24.188  24.341  35.361 1.00 103.55 ?  385 GLN   A C    1 
ATOM   2517 O  O    . GLN   A 1 358 ? 25.371  24.653  35.189 1.00 112.40 ?  385 GLN   A O    1 
ATOM   2518 C  CB   . GLN   A 1 358 ? 23.398  22.533  33.789 1.00 93.37  ?  385 GLN   A CB   1 
ATOM   2519 C  CG   . GLN   A 1 358 ? 23.693  21.078  33.438 1.00 95.34  ?  385 GLN   A CG   1 
ATOM   2520 C  CD   . GLN   A 1 358 ? 22.663  20.467  32.506 1.00 89.92  ?  385 GLN   A CD   1 
ATOM   2521 O  OE1  . GLN   A 1 358 ? 22.170  19.364  32.748 1.00 76.79  ?  385 GLN   A OE1  1 
ATOM   2522 N  NE2  . GLN   A 1 358 ? 22.342  21.174  31.430 1.00 99.16  ?  385 GLN   A NE2  1 
ATOM   2523 N  N    . GLY   A 1 359 ? 23.253  25.239  35.669 1.00 105.20 ?  386 GLY   A N    1 
ATOM   2524 C  CA   . GLY   A 1 359 ? 23.600  26.597  36.044 1.00 103.62 ?  386 GLY   A CA   1 
ATOM   2525 C  C    . GLY   A 1 359 ? 23.657  27.604  34.914 1.00 120.73 ?  386 GLY   A C    1 
ATOM   2526 O  O    . GLY   A 1 359 ? 24.624  28.366  34.809 1.00 119.67 ?  386 GLY   A O    1 
ATOM   2527 N  N    . ASN   A 1 360 ? 22.626  27.620  34.067 1.00 137.58 ?  387 ASN   A N    1 
ATOM   2528 C  CA   . ASN   A 1 360 ? 22.510  28.579  32.966 1.00 144.59 ?  387 ASN   A CA   1 
ATOM   2529 C  C    . ASN   A 1 360 ? 23.716  28.532  32.031 1.00 149.35 ?  387 ASN   A C    1 
ATOM   2530 O  O    . ASN   A 1 360 ? 24.037  29.519  31.365 1.00 151.46 ?  387 ASN   A O    1 
ATOM   2531 C  CB   . ASN   A 1 360 ? 22.298  30.004  33.490 1.00 126.23 ?  387 ASN   A CB   1 
ATOM   2532 N  N    . ARG   A 1 361 ? 24.402  27.389  31.978 1.00 134.20 ?  388 ARG   A N    1 
ATOM   2533 C  CA   . ARG   A 1 361 ? 25.490  27.231  31.022 1.00 119.52 ?  388 ARG   A CA   1 
ATOM   2534 C  C    . ARG   A 1 361 ? 24.965  26.986  29.616 1.00 124.39 ?  388 ARG   A C    1 
ATOM   2535 O  O    . ARG   A 1 361 ? 25.662  27.284  28.638 1.00 122.16 ?  388 ARG   A O    1 
ATOM   2536 C  CB   . ARG   A 1 361 ? 26.413  26.089  31.447 1.00 119.59 ?  388 ARG   A CB   1 
ATOM   2537 C  CG   . ARG   A 1 361 ? 25.698  24.916  32.088 1.00 111.44 ?  388 ARG   A CG   1 
ATOM   2538 C  CD   . ARG   A 1 361 ? 26.582  23.681  32.105 1.00 99.65  ?  388 ARG   A CD   1 
ATOM   2539 N  NE   . ARG   A 1 361 ? 26.170  22.696  31.113 1.00 111.87 ?  388 ARG   A NE   1 
ATOM   2540 C  CZ   . ARG   A 1 361 ? 26.323  21.386  31.250 1.00 111.53 ?  388 ARG   A CZ   1 
ATOM   2541 N  NH1  . ARG   A 1 361 ? 26.895  20.866  32.324 1.00 104.68 ?  388 ARG   A NH1  1 
ATOM   2542 N  NH2  . ARG   A 1 361 ? 25.891  20.577  30.287 1.00 92.85  ?  388 ARG   A NH2  1 
ATOM   2543 N  N    . TYR   A 1 362 ? 23.749  26.447  29.496 1.00 126.59 ?  389 TYR   A N    1 
ATOM   2544 C  CA   . TYR   A 1 362 ? 23.120  26.338  28.185 1.00 127.97 ?  389 TYR   A CA   1 
ATOM   2545 C  C    . TYR   A 1 362 ? 22.851  27.714  27.592 1.00 132.31 ?  389 TYR   A C    1 
ATOM   2546 O  O    . TYR   A 1 362 ? 22.786  27.860  26.366 1.00 131.18 ?  389 TYR   A O    1 
ATOM   2547 C  CB   . TYR   A 1 362 ? 21.821  25.538  28.288 1.00 113.03 ?  389 TYR   A CB   1 
ATOM   2548 N  N    . ARG   A 1 363 ? 22.708  28.735  28.442 1.00 134.30 ?  390 ARG   A N    1 
ATOM   2549 C  CA   . ARG   A 1 363 ? 22.536  30.109  27.986 1.00 132.02 ?  390 ARG   A CA   1 
ATOM   2550 C  C    . ARG   A 1 363 ? 23.774  30.663  27.294 1.00 128.54 ?  390 ARG   A C    1 
ATOM   2551 O  O    . ARG   A 1 363 ? 23.721  31.786  26.780 1.00 124.72 ?  390 ARG   A O    1 
ATOM   2552 C  CB   . ARG   A 1 363 ? 22.155  31.006  29.166 1.00 127.08 ?  390 ARG   A CB   1 
ATOM   2553 N  N    . LYS   A 1 364 ? 24.882  29.920  27.274 1.00 129.23 ?  391 LYS   A N    1 
ATOM   2554 C  CA   . LYS   A 1 364 ? 26.048  30.343  26.510 1.00 136.55 ?  391 LYS   A CA   1 
ATOM   2555 C  C    . LYS   A 1 364 ? 25.927  29.966  25.039 1.00 139.72 ?  391 LYS   A C    1 
ATOM   2556 O  O    . LYS   A 1 364 ? 26.452  30.677  24.175 1.00 147.15 ?  391 LYS   A O    1 
ATOM   2557 C  CB   . LYS   A 1 364 ? 27.320  29.732  27.103 1.00 134.23 ?  391 LYS   A CB   1 
ATOM   2558 C  CG   . LYS   A 1 364 ? 28.605  30.206  26.441 1.00 140.51 ?  391 LYS   A CG   1 
ATOM   2559 C  CD   . LYS   A 1 364 ? 29.788  29.333  26.821 1.00 120.35 ?  391 LYS   A CD   1 
ATOM   2560 C  CE   . LYS   A 1 364 ? 30.623  29.955  27.929 1.00 117.61 ?  391 LYS   A CE   1 
ATOM   2561 N  NZ   . LYS   A 1 364 ? 29.871  30.072  29.208 1.00 123.65 ?  391 LYS   A NZ   1 
ATOM   2562 N  N    . CYS   A 1 365 ? 25.235  28.868  24.736 1.00 131.71 ?  392 CYS   A N    1 
ATOM   2563 C  CA   . CYS   A 1 365 ? 25.096  28.376  23.371 1.00 131.41 ?  392 CYS   A CA   1 
ATOM   2564 C  C    . CYS   A 1 365 ? 23.769  28.756  22.727 1.00 131.79 ?  392 CYS   A C    1 
ATOM   2565 O  O    . CYS   A 1 365 ? 23.741  29.094  21.540 1.00 136.78 ?  392 CYS   A O    1 
ATOM   2566 C  CB   . CYS   A 1 365 ? 25.254  26.852  23.342 1.00 122.23 ?  392 CYS   A CB   1 
ATOM   2567 S  SG   . CYS   A 1 365 ? 26.373  26.198  24.602 1.00 134.00 ?  392 CYS   A SG   1 
ATOM   2568 N  N    . THR   A 1 366 ? 22.670  28.706  23.475 1.00 116.84 ?  393 THR   A N    1 
ATOM   2569 C  CA   . THR   A 1 366 ? 21.363  29.026  22.918 1.00 117.04 ?  393 THR   A CA   1 
ATOM   2570 C  C    . THR   A 1 366 ? 20.430  29.453  24.041 1.00 111.93 ?  393 THR   A C    1 
ATOM   2571 O  O    . THR   A 1 366 ? 20.667  29.166  25.217 1.00 116.88 ?  393 THR   A O    1 
ATOM   2572 C  CB   . THR   A 1 366 ? 20.769  27.837  22.150 1.00 103.80 ?  393 THR   A CB   1 
ATOM   2573 O  OG1  . THR   A 1 366 ? 19.698  28.290  21.313 1.00 109.44 ?  393 THR   A OG1  1 
ATOM   2574 C  CG2  . THR   A 1 366 ? 20.240  26.784  23.114 1.00 97.55  ?  393 THR   A CG2  1 
ATOM   2575 N  N    . ASP   A 1 367 ? 19.364  30.157  23.658 1.00 111.72 ?  394 ASP   A N    1 
ATOM   2576 C  CA   . ASP   A 1 367 ? 18.292  30.527  24.572 1.00 105.25 ?  394 ASP   A CA   1 
ATOM   2577 C  C    . ASP   A 1 367 ? 17.015  29.742  24.292 1.00 100.32 ?  394 ASP   A C    1 
ATOM   2578 O  O    . ASP   A 1 367 ? 15.924  30.177  24.676 1.00 96.54  ?  394 ASP   A O    1 
ATOM   2579 C  CB   . ASP   A 1 367 ? 18.022  32.031  24.499 1.00 108.85 ?  394 ASP   A CB   1 
ATOM   2580 C  CG   . ASP   A 1 367 ? 17.936  32.541  23.072 1.00 118.78 ?  394 ASP   A CG   1 
ATOM   2581 O  OD1  . ASP   A 1 367 ? 17.766  31.718  22.148 1.00 122.88 ?  394 ASP   A OD1  1 
ATOM   2582 O  OD2  . ASP   A 1 367 ? 18.036  33.771  22.875 1.00 119.20 ?  394 ASP   A OD2  1 
ATOM   2583 N  N    . TRP   A 1 368 ? 17.139  28.590  23.628 1.00 89.09  ?  395 TRP   A N    1 
ATOM   2584 C  CA   . TRP   A 1 368 ? 15.967  27.830  23.207 1.00 84.58  ?  395 TRP   A CA   1 
ATOM   2585 C  C    . TRP   A 1 368 ? 15.137  27.372  24.399 1.00 81.02  ?  395 TRP   A C    1 
ATOM   2586 O  O    . TRP   A 1 368 ? 13.903  27.333  24.327 1.00 81.77  ?  395 TRP   A O    1 
ATOM   2587 C  CB   . TRP   A 1 368 ? 16.404  26.627  22.369 1.00 73.35  ?  395 TRP   A CB   1 
ATOM   2588 C  CG   . TRP   A 1 368 ? 15.296  25.998  21.583 1.00 68.90  ?  395 TRP   A CG   1 
ATOM   2589 C  CD1  . TRP   A 1 368 ? 14.981  26.236  20.277 1.00 78.49  ?  395 TRP   A CD1  1 
ATOM   2590 C  CD2  . TRP   A 1 368 ? 14.357  25.022  22.051 1.00 70.03  ?  395 TRP   A CD2  1 
ATOM   2591 N  NE1  . TRP   A 1 368 ? 13.904  25.471  19.903 1.00 70.23  ?  395 TRP   A NE1  1 
ATOM   2592 C  CE2  . TRP   A 1 368 ? 13.502  24.717  20.974 1.00 64.41  ?  395 TRP   A CE2  1 
ATOM   2593 C  CE3  . TRP   A 1 368 ? 14.156  24.378  23.276 1.00 64.67  ?  395 TRP   A CE3  1 
ATOM   2594 C  CZ2  . TRP   A 1 368 ? 12.462  23.797  21.084 1.00 57.24  ?  395 TRP   A CZ2  1 
ATOM   2595 C  CZ3  . TRP   A 1 368 ? 13.123  23.465  23.383 1.00 65.83  ?  395 TRP   A CZ3  1 
ATOM   2596 C  CH2  . TRP   A 1 368 ? 12.289  23.184  22.294 1.00 59.28  ?  395 TRP   A CH2  1 
ATOM   2597 N  N    . TRP   A 1 369 ? 15.792  27.026  25.503 1.00 79.07  ?  396 TRP   A N    1 
ATOM   2598 C  CA   . TRP   A 1 369 ? 15.117  26.473  26.669 1.00 74.50  ?  396 TRP   A CA   1 
ATOM   2599 C  C    . TRP   A 1 369 ? 14.687  27.531  27.677 1.00 75.73  ?  396 TRP   A C    1 
ATOM   2600 O  O    . TRP   A 1 369 ? 14.035  27.185  28.667 1.00 77.34  ?  396 TRP   A O    1 
ATOM   2601 C  CB   . TRP   A 1 369 ? 16.023  25.451  27.362 1.00 69.67  ?  396 TRP   A CB   1 
ATOM   2602 C  CG   . TRP   A 1 369 ? 16.186  24.174  26.601 1.00 69.00  ?  396 TRP   A CG   1 
ATOM   2603 C  CD1  . TRP   A 1 369 ? 17.230  23.830  25.792 1.00 76.36  ?  396 TRP   A CD1  1 
ATOM   2604 C  CD2  . TRP   A 1 369 ? 15.282  23.063  26.584 1.00 70.19  ?  396 TRP   A CD2  1 
ATOM   2605 N  NE1  . TRP   A 1 369 ? 17.030  22.576  25.268 1.00 66.30  ?  396 TRP   A NE1  1 
ATOM   2606 C  CE2  . TRP   A 1 369 ? 15.841  22.083  25.739 1.00 70.02  ?  396 TRP   A CE2  1 
ATOM   2607 C  CE3  . TRP   A 1 369 ? 14.054  22.802  27.199 1.00 67.29  ?  396 TRP   A CE3  1 
ATOM   2608 C  CZ2  . TRP   A 1 369 ? 15.214  20.863  25.493 1.00 66.87  ?  396 TRP   A CZ2  1 
ATOM   2609 C  CZ3  . TRP   A 1 369 ? 13.433  21.591  26.954 1.00 67.68  ?  396 TRP   A CZ3  1 
ATOM   2610 C  CH2  . TRP   A 1 369 ? 14.014  20.637  26.109 1.00 77.77  ?  396 TRP   A CH2  1 
ATOM   2611 N  N    . CYS   A 1 370 ? 15.026  28.803  27.451 1.00 77.03  ?  397 CYS   A N    1 
ATOM   2612 C  CA   . CYS   A 1 370 ? 14.729  29.837  28.439 1.00 84.25  ?  397 CYS   A CA   1 
ATOM   2613 C  C    . CYS   A 1 370 ? 13.226  29.994  28.647 1.00 77.07  ?  397 CYS   A C    1 
ATOM   2614 O  O    . CYS   A 1 370 ? 12.736  29.938  29.781 1.00 81.19  ?  397 CYS   A O    1 
ATOM   2615 C  CB   . CYS   A 1 370 ? 15.357  31.165  28.013 1.00 93.80  ?  397 CYS   A CB   1 
ATOM   2616 S  SG   . CYS   A 1 370 ? 17.158  31.222  28.160 1.00 118.97 ?  397 CYS   A SG   1 
ATOM   2617 N  N    . GLN   A 1 371 ? 12.479  30.197  27.564 1.00 78.35  ?  398 GLN   A N    1 
ATOM   2618 C  CA   . GLN   A 1 371 ? 11.030  30.343  27.656 1.00 79.49  ?  398 GLN   A CA   1 
ATOM   2619 C  C    . GLN   A 1 371 ? 10.361  29.047  28.116 1.00 77.22  ?  398 GLN   A C    1 
ATOM   2620 O  O    . GLN   A 1 371 ? 9.477   29.099  28.980 1.00 83.74  ?  398 GLN   A O    1 
ATOM   2621 C  CB   . GLN   A 1 371 ? 10.451  30.817  26.318 1.00 86.28  ?  398 GLN   A CB   1 
ATOM   2622 C  CG   . GLN   A 1 371 ? 8.972   31.190  26.361 1.00 90.84  ?  398 GLN   A CG   1 
ATOM   2623 C  CD   . GLN   A 1 371 ? 8.054   29.987  26.223 1.00 102.16 ?  398 GLN   A CD   1 
ATOM   2624 O  OE1  . GLN   A 1 371 ? 8.427   28.975  25.628 1.00 100.75 ?  398 GLN   A OE1  1 
ATOM   2625 N  NE2  . GLN   A 1 371 ? 6.856   30.085  26.787 1.00 105.22 ?  398 GLN   A NE2  1 
ATOM   2626 N  N    . PRO   A 1 372 ? 10.722  27.875  27.573 1.00 70.07  ?  399 PRO   A N    1 
ATOM   2627 C  CA   . PRO   A 1 372 ? 10.124  26.634  28.102 1.00 61.78  ?  399 PRO   A CA   1 
ATOM   2628 C  C    . PRO   A 1 372 ? 10.390  26.418  29.582 1.00 71.81  ?  399 PRO   A C    1 
ATOM   2629 O  O    . PRO   A 1 372 ? 9.465   26.077  30.332 1.00 77.76  ?  399 PRO   A O    1 
ATOM   2630 C  CB   . PRO   A 1 372 ? 10.769  25.545  27.235 1.00 77.44  ?  399 PRO   A CB   1 
ATOM   2631 C  CG   . PRO   A 1 372 ? 11.093  26.231  25.967 1.00 63.28  ?  399 PRO   A CG   1 
ATOM   2632 C  CD   . PRO   A 1 372 ? 11.521  27.605  26.363 1.00 67.31  ?  399 PRO   A CD   1 
ATOM   2633 N  N    . MET   A 1 373 ? 11.635  26.604  30.030 1.00 80.28  ?  400 MET   A N    1 
ATOM   2634 C  CA   . MET   A 1 373 ? 11.936  26.423  31.447 1.00 80.74  ?  400 MET   A CA   1 
ATOM   2635 C  C    . MET   A 1 373 ? 11.188  27.431  32.307 1.00 70.71  ?  400 MET   A C    1 
ATOM   2636 O  O    . MET   A 1 373 ? 10.831  27.128  33.451 1.00 69.73  ?  400 MET   A O    1 
ATOM   2637 C  CB   . MET   A 1 373 ? 13.439  26.538  31.692 1.00 73.28  ?  400 MET   A CB   1 
ATOM   2638 C  CG   . MET   A 1 373 ? 14.223  25.275  31.388 1.00 74.51  ?  400 MET   A CG   1 
ATOM   2639 S  SD   . MET   A 1 373 ? 13.694  23.848  32.356 1.00 79.72  ?  400 MET   A SD   1 
ATOM   2640 C  CE   . MET   A 1 373 ? 13.051  22.788  31.067 1.00 65.81  ?  400 MET   A CE   1 
ATOM   2641 N  N    . ALA   A 1 374 ? 10.946  28.632  31.778 1.00 79.96  ?  401 ALA   A N    1 
ATOM   2642 C  CA   . ALA   A 1 374 ? 10.146  29.606  32.509 1.00 81.98  ?  401 ALA   A CA   1 
ATOM   2643 C  C    . ALA   A 1 374 ? 8.667   29.244  32.482 1.00 78.61  ?  401 ALA   A C    1 
ATOM   2644 O  O    . ALA   A 1 374 ? 7.935   29.563  33.426 1.00 73.88  ?  401 ALA   A O    1 
ATOM   2645 C  CB   . ALA   A 1 374 ? 10.364  31.005  31.936 1.00 72.15  ?  401 ALA   A CB   1 
ATOM   2646 N  N    . GLN   A 1 375 ? 8.208   28.582  31.418 1.00 68.89  ?  402 GLN   A N    1 
ATOM   2647 C  CA   . GLN   A 1 375 ? 6.817   28.147  31.368 1.00 72.70  ?  402 GLN   A CA   1 
ATOM   2648 C  C    . GLN   A 1 375 ? 6.580   26.945  32.271 1.00 76.74  ?  402 GLN   A C    1 
ATOM   2649 O  O    . GLN   A 1 375 ? 5.551   26.871  32.952 1.00 68.10  ?  402 GLN   A O    1 
ATOM   2650 C  CB   . GLN   A 1 375 ? 6.410   27.819  29.930 1.00 70.35  ?  402 GLN   A CB   1 
ATOM   2651 C  CG   . GLN   A 1 375 ? 4.903   27.769  29.724 1.00 90.70  ?  402 GLN   A CG   1 
ATOM   2652 C  CD   . GLN   A 1 375 ? 4.512   27.210  28.370 1.00 103.34 ?  402 GLN   A CD   1 
ATOM   2653 O  OE1  . GLN   A 1 375 ? 5.273   27.292  27.406 1.00 102.40 ?  402 GLN   A OE1  1 
ATOM   2654 N  NE2  . GLN   A 1 375 ? 3.314   26.641  28.289 1.00 106.16 ?  402 GLN   A NE2  1 
ATOM   2655 N  N    . LEU   A 1 376 ? 7.519   25.995  32.290 1.00 67.80  ?  403 LEU   A N    1 
ATOM   2656 C  CA   . LEU   A 1 376 ? 7.381   24.843  33.175 1.00 62.08  ?  403 LEU   A CA   1 
ATOM   2657 C  C    . LEU   A 1 376 ? 7.458   25.259  34.639 1.00 69.39  ?  403 LEU   A C    1 
ATOM   2658 O  O    . LEU   A 1 376 ? 6.761   24.691  35.488 1.00 66.93  ?  403 LEU   A O    1 
ATOM   2659 C  CB   . LEU   A 1 376 ? 8.449   23.798  32.853 1.00 66.91  ?  403 LEU   A CB   1 
ATOM   2660 C  CG   . LEU   A 1 376 ? 8.259   23.017  31.551 1.00 63.73  ?  403 LEU   A CG   1 
ATOM   2661 C  CD1  . LEU   A 1 376 ? 9.507   22.225  31.209 1.00 59.44  ?  403 LEU   A CD1  1 
ATOM   2662 C  CD2  . LEU   A 1 376 ? 7.053   22.096  31.650 1.00 64.52  ?  403 LEU   A CD2  1 
ATOM   2663 N  N    . GLU   A 1 377 ? 8.301   26.245  34.955 1.00 69.77  ?  404 GLU   A N    1 
ATOM   2664 C  CA   . GLU   A 1 377 ? 8.343   26.761  36.319 1.00 72.05  ?  404 GLU   A CA   1 
ATOM   2665 C  C    . GLU   A 1 377 ? 7.029   27.436  36.689 1.00 79.96  ?  404 GLU   A C    1 
ATOM   2666 O  O    . GLU   A 1 377 ? 6.534   27.277  37.812 1.00 73.45  ?  404 GLU   A O    1 
ATOM   2667 C  CB   . GLU   A 1 377 ? 9.511   27.734  36.483 1.00 76.80  ?  404 GLU   A CB   1 
ATOM   2668 C  CG   . GLU   A 1 377 ? 9.568   28.393  37.853 1.00 77.60  ?  404 GLU   A CG   1 
ATOM   2669 C  CD   . GLU   A 1 377 ? 10.979  28.741  38.281 1.00 93.69  ?  404 GLU   A CD   1 
ATOM   2670 O  OE1  . GLU   A 1 377 ? 11.910  28.568  37.466 1.00 98.12  ?  404 GLU   A OE1  1 
ATOM   2671 O  OE2  . GLU   A 1 377 ? 11.156  29.186  39.435 1.00 100.48 ?  404 GLU   A OE2  1 
ATOM   2672 N  N    . ALA   A 1 378 ? 6.450   28.196  35.757 1.00 71.75  ?  405 ALA   A N    1 
ATOM   2673 C  CA   . ALA   A 1 378 ? 5.149   28.808  36.004 1.00 64.67  ?  405 ALA   A CA   1 
ATOM   2674 C  C    . ALA   A 1 378 ? 4.072   27.747  36.188 1.00 76.11  ?  405 ALA   A C    1 
ATOM   2675 O  O    . ALA   A 1 378 ? 3.218   27.865  37.074 1.00 72.67  ?  405 ALA   A O    1 
ATOM   2676 C  CB   . ALA   A 1 378 ? 4.785   29.751  34.858 1.00 58.65  ?  405 ALA   A CB   1 
ATOM   2677 N  N    . LEU   A 1 379 ? 4.100   26.700  35.359 1.00 76.88  ?  406 LEU   A N    1 
ATOM   2678 C  CA   . LEU   A 1 379 ? 3.146   25.609  35.516 1.00 68.43  ?  406 LEU   A CA   1 
ATOM   2679 C  C    . LEU   A 1 379 ? 3.361   24.888  36.841 1.00 71.51  ?  406 LEU   A C    1 
ATOM   2680 O  O    . LEU   A 1 379 ? 2.400   24.447  37.482 1.00 76.96  ?  406 LEU   A O    1 
ATOM   2681 C  CB   . LEU   A 1 379 ? 3.275   24.629  34.350 1.00 69.17  ?  406 LEU   A CB   1 
ATOM   2682 C  CG   . LEU   A 1 379 ? 2.751   25.098  32.991 1.00 73.85  ?  406 LEU   A CG   1 
ATOM   2683 C  CD1  . LEU   A 1 379 ? 3.233   24.172  31.881 1.00 71.47  ?  406 LEU   A CD1  1 
ATOM   2684 C  CD2  . LEU   A 1 379 ? 1.238   25.210  32.986 1.00 69.55  ?  406 LEU   A CD2  1 
ATOM   2685 N  N    . TRP   A 1 380 ? 4.620   24.769  37.269 1.00 76.10  ?  407 TRP   A N    1 
ATOM   2686 C  CA   . TRP   A 1 380 ? 4.927   24.092  38.526 1.00 67.73  ?  407 TRP   A CA   1 
ATOM   2687 C  C    . TRP   A 1 380 ? 4.405   24.877  39.725 1.00 74.33  ?  407 TRP   A C    1 
ATOM   2688 O  O    . TRP   A 1 380 ? 3.924   24.284  40.697 1.00 67.33  ?  407 TRP   A O    1 
ATOM   2689 C  CB   . TRP   A 1 380 ? 6.436   23.871  38.635 1.00 69.40  ?  407 TRP   A CB   1 
ATOM   2690 C  CG   . TRP   A 1 380 ? 6.906   23.478  40.001 1.00 75.68  ?  407 TRP   A CG   1 
ATOM   2691 C  CD1  . TRP   A 1 380 ? 6.978   22.215  40.512 1.00 67.95  ?  407 TRP   A CD1  1 
ATOM   2692 C  CD2  . TRP   A 1 380 ? 7.381   24.355  41.028 1.00 69.67  ?  407 TRP   A CD2  1 
ATOM   2693 N  NE1  . TRP   A 1 380 ? 7.464   22.252  41.797 1.00 71.09  ?  407 TRP   A NE1  1 
ATOM   2694 C  CE2  . TRP   A 1 380 ? 7.719   23.555  42.137 1.00 74.54  ?  407 TRP   A CE2  1 
ATOM   2695 C  CE3  . TRP   A 1 380 ? 7.550   25.740  41.118 1.00 70.60  ?  407 TRP   A CE3  1 
ATOM   2696 C  CZ2  . TRP   A 1 380 ? 8.217   24.094  43.321 1.00 74.18  ?  407 TRP   A CZ2  1 
ATOM   2697 C  CZ3  . TRP   A 1 380 ? 8.044   26.273  42.294 1.00 79.64  ?  407 TRP   A CZ3  1 
ATOM   2698 C  CH2  . TRP   A 1 380 ? 8.369   25.451  43.380 1.00 85.61  ?  407 TRP   A CH2  1 
ATOM   2699 N  N    . LYS   A 1 381 ? 4.494   26.211  39.676 1.00 72.32  ?  408 LYS   A N    1 
ATOM   2700 C  CA   . LYS   A 1 381 ? 3.979   27.030  40.771 1.00 73.26  ?  408 LYS   A CA   1 
ATOM   2701 C  C    . LYS   A 1 381 ? 2.489   26.798  40.983 1.00 75.32  ?  408 LYS   A C    1 
ATOM   2702 O  O    . LYS   A 1 381 ? 2.020   26.730  42.125 1.00 77.09  ?  408 LYS   A O    1 
ATOM   2703 C  CB   . LYS   A 1 381 ? 4.252   28.510  40.499 1.00 70.76  ?  408 LYS   A CB   1 
ATOM   2704 C  CG   . LYS   A 1 381 ? 3.705   29.445  41.570 1.00 77.06  ?  408 LYS   A CG   1 
ATOM   2705 C  CD   . LYS   A 1 381 ? 4.445   30.772  41.599 1.00 94.08  ?  408 LYS   A CD   1 
ATOM   2706 C  CE   . LYS   A 1 381 ? 3.852   31.712  42.641 1.00 90.59  ?  408 LYS   A CE   1 
ATOM   2707 N  NZ   . LYS   A 1 381 ? 2.578   32.336  42.185 1.00 95.66  ?  408 LYS   A NZ   1 
ATOM   2708 N  N    . LYS   A 1 382 ? 1.728   26.679  39.892 1.00 82.53  ?  409 LYS   A N    1 
ATOM   2709 C  CA   . LYS   A 1 382 ? 0.303   26.391  40.009 1.00 67.51  ?  409 LYS   A CA   1 
ATOM   2710 C  C    . LYS   A 1 382 ? 0.067   25.063  40.717 1.00 69.60  ?  409 LYS   A C    1 
ATOM   2711 O  O    . LYS   A 1 382 ? -0.877  24.929  41.504 1.00 74.32  ?  409 LYS   A O    1 
ATOM   2712 C  CB   . LYS   A 1 382 ? -0.345  26.386  38.624 1.00 73.16  ?  409 LYS   A CB   1 
ATOM   2713 C  CG   . LYS   A 1 382 ? -1.853  26.190  38.642 1.00 79.61  ?  409 LYS   A CG   1 
ATOM   2714 C  CD   . LYS   A 1 382 ? -2.562  27.386  39.256 1.00 83.40  ?  409 LYS   A CD   1 
ATOM   2715 C  CE   . LYS   A 1 382 ? -2.249  28.662  38.494 1.00 77.99  ?  409 LYS   A CE   1 
ATOM   2716 N  NZ   . LYS   A 1 382 ? -2.834  29.860  39.154 1.00 90.31  ?  409 LYS   A NZ   1 
ATOM   2717 N  N    . MET   A 1 383 ? 0.923   24.072  40.456 1.00 76.03  ?  410 MET   A N    1 
ATOM   2718 C  CA   . MET   A 1 383 ? 0.774   22.777  41.110 1.00 74.19  ?  410 MET   A CA   1 
ATOM   2719 C  C    . MET   A 1 383 ? 1.125   22.849  42.589 1.00 73.18  ?  410 MET   A C    1 
ATOM   2720 O  O    . MET   A 1 383 ? 0.611   22.053  43.384 1.00 78.04  ?  410 MET   A O    1 
ATOM   2721 C  CB   . MET   A 1 383 ? 1.631   21.733  40.399 1.00 66.45  ?  410 MET   A CB   1 
ATOM   2722 C  CG   . MET   A 1 383 ? 1.485   21.773  38.890 1.00 65.65  ?  410 MET   A CG   1 
ATOM   2723 S  SD   . MET   A 1 383 ? 2.042   20.277  38.061 1.00 66.66  ?  410 MET   A SD   1 
ATOM   2724 C  CE   . MET   A 1 383 ? 2.885   20.990  36.654 1.00 71.29  ?  410 MET   A CE   1 
ATOM   2725 N  N    . GLU   A 1 384 ? 1.997   23.783  42.977 1.00 69.14  ?  411 GLU   A N    1 
ATOM   2726 C  CA   . GLU   A 1 384 ? 2.213   24.034  44.398 1.00 67.82  ?  411 GLU   A CA   1 
ATOM   2727 C  C    . GLU   A 1 384 ? 0.925   24.497  45.063 1.00 75.26  ?  411 GLU   A C    1 
ATOM   2728 O  O    . GLU   A 1 384 ? 0.600   24.068  46.177 1.00 83.16  ?  411 GLU   A O    1 
ATOM   2729 C  CB   . GLU   A 1 384 ? 3.321   25.070  44.592 1.00 78.71  ?  411 GLU   A CB   1 
ATOM   2730 C  CG   . GLU   A 1 384 ? 4.736   24.510  44.525 1.00 74.85  ?  411 GLU   A CG   1 
ATOM   2731 C  CD   . GLU   A 1 384 ? 5.099   23.682  45.743 1.00 71.69  ?  411 GLU   A CD   1 
ATOM   2732 O  OE1  . GLU   A 1 384 ? 4.939   24.187  46.875 1.00 89.07  ?  411 GLU   A OE1  1 
ATOM   2733 O  OE2  . GLU   A 1 384 ? 5.552   22.531  45.570 1.00 71.69  ?  411 GLU   A OE2  1 
ATOM   2734 N  N    . GLY   A 1 385 ? 0.172   25.371  44.390 1.00 83.76  ?  412 GLY   A N    1 
ATOM   2735 C  CA   . GLY   A 1 385 ? -1.121  25.778  44.907 1.00 81.34  ?  412 GLY   A CA   1 
ATOM   2736 C  C    . GLY   A 1 385 ? -2.146  24.663  44.882 1.00 77.95  ?  412 GLY   A C    1 
ATOM   2737 O  O    . GLY   A 1 385 ? -3.068  24.644  45.702 1.00 80.60  ?  412 GLY   A O    1 
ATOM   2738 N  N    . VAL   A 1 386 ? -2.006  23.724  43.943 1.00 67.65  ?  413 VAL   A N    1 
ATOM   2739 C  CA   . VAL   A 1 386 ? -2.889  22.561  43.915 1.00 70.73  ?  413 VAL   A CA   1 
ATOM   2740 C  C    . VAL   A 1 386 ? -2.639  21.682  45.134 1.00 78.73  ?  413 VAL   A C    1 
ATOM   2741 O  O    . VAL   A 1 386 ? -3.580  21.226  45.796 1.00 77.56  ?  413 VAL   A O    1 
ATOM   2742 C  CB   . VAL   A 1 386 ? -2.700  21.777  42.604 1.00 74.60  ?  413 VAL   A CB   1 
ATOM   2743 C  CG1  . VAL   A 1 386 ? -3.216  20.350  42.751 1.00 58.25  ?  413 VAL   A CG1  1 
ATOM   2744 C  CG2  . VAL   A 1 386 ? -3.396  22.488  41.456 1.00 68.47  ?  413 VAL   A CG2  1 
ATOM   2745 N  N    . THR   A 1 387 ? -1.365  21.435  45.448 1.00 73.30  ?  414 THR   A N    1 
ATOM   2746 C  CA   . THR   A 1 387 ? -1.030  20.674  46.647 1.00 76.76  ?  414 THR   A CA   1 
ATOM   2747 C  C    . THR   A 1 387 ? -1.547  21.371  47.899 1.00 73.71  ?  414 THR   A C    1 
ATOM   2748 O  O    . THR   A 1 387 ? -2.048  20.717  48.822 1.00 77.84  ?  414 THR   A O    1 
ATOM   2749 C  CB   . THR   A 1 387 ? 0.484   20.468  46.732 1.00 73.25  ?  414 THR   A CB   1 
ATOM   2750 O  OG1  . THR   A 1 387 ? 0.951   19.841  45.532 1.00 65.84  ?  414 THR   A OG1  1 
ATOM   2751 C  CG2  . THR   A 1 387 ? 0.839   19.593  47.926 1.00 71.03  ?  414 THR   A CG2  1 
ATOM   2752 N  N    . ASN   A 1 388 ? -1.443  22.702  47.946 1.00 73.64  ?  415 ASN   A N    1 
ATOM   2753 C  CA   . ASN   A 1 388 ? -2.002  23.445  49.069 1.00 73.19  ?  415 ASN   A CA   1 
ATOM   2754 C  C    . ASN   A 1 388 ? -3.521  23.334  49.110 1.00 82.91  ?  415 ASN   A C    1 
ATOM   2755 O  O    . ASN   A 1 388 ? -4.109  23.298  50.198 1.00 75.54  ?  415 ASN   A O    1 
ATOM   2756 C  CB   . ASN   A 1 388 ? -1.578  24.911  48.993 1.00 73.14  ?  415 ASN   A CB   1 
ATOM   2757 C  CG   . ASN   A 1 388 ? -2.137  25.737  50.132 1.00 73.67  ?  415 ASN   A CG   1 
ATOM   2758 O  OD1  . ASN   A 1 388 ? -2.024  25.363  51.299 1.00 81.72  ?  415 ASN   A OD1  1 
ATOM   2759 N  ND2  . ASN   A 1 388 ? -2.751  26.867  49.798 1.00 95.15  ?  415 ASN   A ND2  1 
ATOM   2760 N  N    . ALA   A 1 389 ? -4.169  23.276  47.944 1.00 77.10  ?  416 ALA   A N    1 
ATOM   2761 C  CA   . ALA   A 1 389 ? -5.616  23.089  47.913 1.00 70.83  ?  416 ALA   A CA   1 
ATOM   2762 C  C    . ALA   A 1 389 ? -6.003  21.707  48.423 1.00 80.91  ?  416 ALA   A C    1 
ATOM   2763 O  O    . ALA   A 1 389 ? -7.027  21.553  49.100 1.00 85.28  ?  416 ALA   A O    1 
ATOM   2764 C  CB   . ALA   A 1 389 ? -6.145  23.307  46.496 1.00 68.36  ?  416 ALA   A CB   1 
ATOM   2765 N  N    . VAL   A 1 390 ? -5.199  20.689  48.106 1.00 82.06  ?  417 VAL   A N    1 
ATOM   2766 C  CA   . VAL   A 1 390 ? -5.454  19.352  48.632 1.00 73.16  ?  417 VAL   A CA   1 
ATOM   2767 C  C    . VAL   A 1 390 ? -5.227  19.322  50.137 1.00 79.30  ?  417 VAL   A C    1 
ATOM   2768 O  O    . VAL   A 1 390 ? -6.026  18.751  50.889 1.00 90.23  ?  417 VAL   A O    1 
ATOM   2769 C  CB   . VAL   A 1 390 ? -4.578  18.315  47.906 1.00 81.58  ?  417 VAL   A CB   1 
ATOM   2770 C  CG1  . VAL   A 1 390 ? -4.700  16.953  48.575 1.00 75.82  ?  417 VAL   A CG1  1 
ATOM   2771 C  CG2  . VAL   A 1 390 ? -4.963  18.226  46.441 1.00 66.93  ?  417 VAL   A CG2  1 
ATOM   2772 N  N    . LEU   A 1 391 ? -4.136  19.939  50.602 1.00 83.74  ?  418 LEU   A N    1 
ATOM   2773 C  CA   . LEU   A 1 391 ? -3.887  20.019  52.037 1.00 76.92  ?  418 LEU   A CA   1 
ATOM   2774 C  C    . LEU   A 1 391 ? -4.966  20.830  52.742 1.00 90.25  ?  418 LEU   A C    1 
ATOM   2775 O  O    . LEU   A 1 391 ? -5.231  20.612  53.929 1.00 96.12  ?  418 LEU   A O    1 
ATOM   2776 C  CB   . LEU   A 1 391 ? -2.508  20.625  52.295 1.00 76.19  ?  418 LEU   A CB   1 
ATOM   2777 C  CG   . LEU   A 1 391 ? -1.313  19.765  51.879 1.00 78.75  ?  418 LEU   A CG   1 
ATOM   2778 C  CD1  . LEU   A 1 391 ? -0.007  20.517  52.084 1.00 76.62  ?  418 LEU   A CD1  1 
ATOM   2779 C  CD2  . LEU   A 1 391 ? -1.304  18.449  52.641 1.00 83.86  ?  418 LEU   A CD2  1 
ATOM   2780 N  N    . HIS   A 1 392 ? -5.596  21.766  52.029 1.00 93.97  ?  419 HIS   A N    1 
ATOM   2781 C  CA   . HIS   A 1 392 ? -6.708  22.516  52.602 1.00 94.88  ?  419 HIS   A CA   1 
ATOM   2782 C  C    . HIS   A 1 392 ? -7.949  21.646  52.761 1.00 95.39  ?  419 HIS   A C    1 
ATOM   2783 O  O    . HIS   A 1 392 ? -8.717  21.832  53.711 1.00 99.59  ?  419 HIS   A O    1 
ATOM   2784 C  CB   . HIS   A 1 392 ? -7.019  23.732  51.729 1.00 95.67  ?  419 HIS   A CB   1 
ATOM   2785 C  CG   . HIS   A 1 392 ? -7.995  24.685  52.343 1.00 115.20 ?  419 HIS   A CG   1 
ATOM   2786 N  ND1  . HIS   A 1 392 ? -9.087  25.175  51.659 1.00 123.54 ?  419 HIS   A ND1  1 
ATOM   2787 C  CD2  . HIS   A 1 392 ? -8.044  25.244  53.576 1.00 118.29 ?  419 HIS   A CD2  1 
ATOM   2788 C  CE1  . HIS   A 1 392 ? -9.767  25.991  52.444 1.00 115.09 ?  419 HIS   A CE1  1 
ATOM   2789 N  NE2  . HIS   A 1 392 ? -9.155  26.050  53.613 1.00 122.38 ?  419 HIS   A NE2  1 
ATOM   2790 N  N    . GLU   A 1 393 ? -8.156  20.690  51.852 1.00 97.58  ?  420 GLU   A N    1 
ATOM   2791 C  CA   . GLU   A 1 393 ? -9.358  19.865  51.890 1.00 101.63 ?  420 GLU   A CA   1 
ATOM   2792 C  C    . GLU   A 1 393 ? -9.297  18.822  53.001 1.00 101.51 ?  420 GLU   A C    1 
ATOM   2793 O  O    . GLU   A 1 393 ? -10.308 18.559  53.662 1.00 103.29 ?  420 GLU   A O    1 
ATOM   2794 C  CB   . GLU   A 1 393 ? -9.571  19.189  50.533 1.00 96.00  ?  420 GLU   A CB   1 
ATOM   2795 C  CG   . GLU   A 1 393 ? -10.694 18.160  50.503 1.00 101.71 ?  420 GLU   A CG   1 
ATOM   2796 C  CD   . GLU   A 1 393 ? -12.075 18.790  50.500 1.00 109.94 ?  420 GLU   A CD   1 
ATOM   2797 O  OE1  . GLU   A 1 393 ? -12.171 20.024  50.331 1.00 114.58 ?  420 GLU   A OE1  1 
ATOM   2798 O  OE2  . GLU   A 1 393 ? -13.067 18.048  50.663 1.00 106.32 ?  420 GLU   A OE2  1 
ATOM   2799 N  N    . VAL   A 1 394 ? -8.126  18.218  53.223 1.00 94.39  ?  421 VAL   A N    1 
ATOM   2800 C  CA   . VAL   A 1 394 ? -8.009  17.192  54.253 1.00 95.11  ?  421 VAL   A CA   1 
ATOM   2801 C  C    . VAL   A 1 394 ? -8.155  17.775  55.652 1.00 100.98 ?  421 VAL   A C    1 
ATOM   2802 O  O    . VAL   A 1 394 ? -8.486  17.043  56.592 1.00 106.69 ?  421 VAL   A O    1 
ATOM   2803 C  CB   . VAL   A 1 394 ? -6.675  16.433  54.121 1.00 92.80  ?  421 VAL   A CB   1 
ATOM   2804 C  CG1  . VAL   A 1 394 ? -6.528  15.856  52.721 1.00 87.11  ?  421 VAL   A CG1  1 
ATOM   2805 C  CG2  . VAL   A 1 394 ? -5.502  17.343  54.455 1.00 99.86  ?  421 VAL   A CG2  1 
ATOM   2806 N  N    . LYS   A 1 395 ? -7.919  19.075  55.819 1.00 104.29 ?  422 LYS   A N    1 
ATOM   2807 C  CA   . LYS   A 1 395 ? -8.089  19.740  57.103 1.00 106.99 ?  422 LYS   A CA   1 
ATOM   2808 C  C    . LYS   A 1 395 ? -9.471  20.360  57.262 1.00 106.14 ?  422 LYS   A C    1 
ATOM   2809 O  O    . LYS   A 1 395 ? -9.678  21.155  58.185 1.00 111.34 ?  422 LYS   A O    1 
ATOM   2810 C  CB   . LYS   A 1 395 ? -7.012  20.814  57.289 1.00 106.51 ?  422 LYS   A CB   1 
ATOM   2811 C  CG   . LYS   A 1 395 ? -5.619  20.258  57.541 1.00 106.48 ?  422 LYS   A CG   1 
ATOM   2812 C  CD   . LYS   A 1 395 ? -4.542  21.197  57.021 1.00 106.64 ?  422 LYS   A CD   1 
ATOM   2813 C  CE   . LYS   A 1 395 ? -3.183  20.866  57.617 1.00 111.10 ?  422 LYS   A CE   1 
ATOM   2814 N  NZ   . LYS   A 1 395 ? -2.411  19.934  56.749 1.00 105.99 ?  422 LYS   A NZ   1 
ATOM   2815 N  N    . ARG   A 1 396 ? -10.415 20.017  56.389 1.00 101.96 ?  423 ARG   A N    1 
ATOM   2816 C  CA   . ARG   A 1 396 ? -11.764 20.556  56.477 1.00 109.84 ?  423 ARG   A CA   1 
ATOM   2817 C  C    . ARG   A 1 396 ? -12.592 19.744  57.465 1.00 118.42 ?  423 ARG   A C    1 
ATOM   2818 O  O    . ARG   A 1 396 ? -12.432 18.526  57.581 1.00 117.88 ?  423 ARG   A O    1 
ATOM   2819 C  CB   . ARG   A 1 396 ? -12.429 20.559  55.099 1.00 108.51 ?  423 ARG   A CB   1 
ATOM   2820 C  CG   . ARG   A 1 396 ? -13.713 21.369  55.027 1.00 101.90 ?  423 ARG   A CG   1 
ATOM   2821 C  CD   . ARG   A 1 396 ? -14.385 21.222  53.671 1.00 97.41  ?  423 ARG   A CD   1 
ATOM   2822 N  NE   . ARG   A 1 396 ? -14.677 19.831  53.351 1.00 107.96 ?  423 ARG   A NE   1 
ATOM   2823 C  CZ   . ARG   A 1 396 ? -15.780 19.420  52.740 1.00 115.79 ?  423 ARG   A CZ   1 
ATOM   2824 N  NH1  . ARG   A 1 396 ? -16.725 20.270  52.374 1.00 119.53 ?  423 ARG   A NH1  1 
ATOM   2825 N  NH2  . ARG   A 1 396 ? -15.940 18.123  52.493 1.00 115.38 ?  423 ARG   A NH2  1 
ATOM   2826 N  N    . GLU   A 1 397 ? -13.482 20.433  58.181 1.00 123.02 ?  424 GLU   A N    1 
ATOM   2827 C  CA   . GLU   A 1 397 ? -14.223 19.799  59.265 1.00 126.77 ?  424 GLU   A CA   1 
ATOM   2828 C  C    . GLU   A 1 397 ? -15.349 18.912  58.746 1.00 133.36 ?  424 GLU   A C    1 
ATOM   2829 O  O    . GLU   A 1 397 ? -15.642 17.868  59.339 1.00 132.79 ?  424 GLU   A O    1 
ATOM   2830 C  CB   . GLU   A 1 397 ? -14.778 20.869  60.206 1.00 129.81 ?  424 GLU   A CB   1 
ATOM   2831 C  CG   . GLU   A 1 397 ? -13.701 21.699  60.890 1.00 130.74 ?  424 GLU   A CG   1 
ATOM   2832 C  CD   . GLU   A 1 397 ? -14.263 22.644  61.933 1.00 134.70 ?  424 GLU   A CD   1 
ATOM   2833 O  OE1  . GLU   A 1 397 ? -15.502 22.779  62.010 1.00 131.86 ?  424 GLU   A OE1  1 
ATOM   2834 O  OE2  . GLU   A 1 397 ? -13.465 23.254  62.675 1.00 139.33 ?  424 GLU   A OE2  1 
ATOM   2835 N  N    . GLY   A 1 398 ? -15.988 19.305  57.645 1.00 127.57 ?  425 GLY   A N    1 
ATOM   2836 C  CA   . GLY   A 1 398 ? -17.104 18.565  57.096 1.00 128.84 ?  425 GLY   A CA   1 
ATOM   2837 C  C    . GLY   A 1 398 ? -16.749 17.357  56.261 1.00 136.30 ?  425 GLY   A C    1 
ATOM   2838 O  O    . GLY   A 1 398 ? -17.637 16.769  55.637 1.00 138.40 ?  425 GLY   A O    1 
ATOM   2839 N  N    . LEU   A 1 399 ? -15.479 16.962  56.226 1.00 127.21 ?  426 LEU   A N    1 
ATOM   2840 C  CA   . LEU   A 1 399 ? -15.059 15.817  55.430 1.00 113.70 ?  426 LEU   A CA   1 
ATOM   2841 C  C    . LEU   A 1 399 ? -15.062 14.564  56.294 1.00 113.11 ?  426 LEU   A C    1 
ATOM   2842 O  O    . LEU   A 1 399 ? -14.408 14.551  57.345 1.00 119.14 ?  426 LEU   A O    1 
ATOM   2843 C  CB   . LEU   A 1 399 ? -13.674 16.046  54.849 1.00 112.97 ?  426 LEU   A CB   1 
ATOM   2844 C  CG   . LEU   A 1 399 ? -13.149 14.975  53.892 1.00 110.40 ?  426 LEU   A CG   1 
ATOM   2845 C  CD1  . LEU   A 1 399 ? -13.787 15.121  52.520 1.00 107.30 ?  426 LEU   A CD1  1 
ATOM   2846 C  CD2  . LEU   A 1 399 ? -11.635 15.054  53.789 1.00 100.69 ?  426 LEU   A CD2  1 
ATOM   2847 N  N    . PRO   A 1 400 ? -15.773 13.506  55.903 1.00 114.79 ?  427 PRO   A N    1 
ATOM   2848 C  CA   . PRO   A 1 400 ? -15.764 12.279  56.707 1.00 110.81 ?  427 PRO   A CA   1 
ATOM   2849 C  C    . PRO   A 1 400 ? -14.376 11.662  56.753 1.00 104.93 ?  427 PRO   A C    1 
ATOM   2850 O  O    . PRO   A 1 400 ? -13.549 11.868  55.862 1.00 107.77 ?  427 PRO   A O    1 
ATOM   2851 C  CB   . PRO   A 1 400 ? -16.760 11.368  55.980 1.00 108.08 ?  427 PRO   A CB   1 
ATOM   2852 C  CG   . PRO   A 1 400 ? -16.816 11.898  54.585 1.00 111.16 ?  427 PRO   A CG   1 
ATOM   2853 C  CD   . PRO   A 1 400 ? -16.606 13.378  54.696 1.00 115.86 ?  427 PRO   A CD   1 
ATOM   2854 N  N    . VAL   A 1 401 ? -14.127 10.898  57.818 1.00 106.30 ?  428 VAL   A N    1 
ATOM   2855 C  CA   . VAL   A 1 401 ? -12.806 10.310  58.022 1.00 114.23 ?  428 VAL   A CA   1 
ATOM   2856 C  C    . VAL   A 1 401 ? -12.478 9.329   56.903 1.00 111.88 ?  428 VAL   A C    1 
ATOM   2857 O  O    . VAL   A 1 401 ? -11.337 9.267   56.426 1.00 107.03 ?  428 VAL   A O    1 
ATOM   2858 C  CB   . VAL   A 1 401 ? -12.732 9.646   59.411 1.00 113.70 ?  428 VAL   A CB   1 
ATOM   2859 C  CG1  . VAL   A 1 401 ? -11.724 8.505   59.421 1.00 114.12 ?  428 VAL   A CG1  1 
ATOM   2860 C  CG2  . VAL   A 1 401 ? -12.386 10.681  60.474 1.00 109.59 ?  428 VAL   A CG2  1 
ATOM   2861 N  N    . GLU   A 1 402 ? -13.475 8.564   56.451 1.00 115.52 ?  429 GLU   A N    1 
ATOM   2862 C  CA   . GLU   A 1 402 ? -13.237 7.580   55.399 1.00 112.75 ?  429 GLU   A CA   1 
ATOM   2863 C  C    . GLU   A 1 402 ? -12.805 8.246   54.098 1.00 112.41 ?  429 GLU   A C    1 
ATOM   2864 O  O    . GLU   A 1 402 ? -11.981 7.699   53.356 1.00 112.61 ?  429 GLU   A O    1 
ATOM   2865 C  CB   . GLU   A 1 402 ? -14.490 6.733   55.182 1.00 118.51 ?  429 GLU   A CB   1 
ATOM   2866 C  CG   . GLU   A 1 402 ? -14.696 5.651   56.229 1.00 121.91 ?  429 GLU   A CG   1 
ATOM   2867 C  CD   . GLU   A 1 402 ? -13.729 4.494   56.070 1.00 131.15 ?  429 GLU   A CD   1 
ATOM   2868 O  OE1  . GLU   A 1 402 ? -13.850 3.752   55.072 1.00 131.03 ?  429 GLU   A OE1  1 
ATOM   2869 O  OE2  . GLU   A 1 402 ? -12.849 4.328   56.939 1.00 137.05 ?  429 GLU   A OE2  1 
ATOM   2870 N  N    . GLN   A 1 403 ? -13.351 9.428   53.804 1.00 110.06 ?  430 GLN   A N    1 
ATOM   2871 C  CA   . GLN   A 1 403 ? -12.939 10.146  52.603 1.00 111.10 ?  430 GLN   A CA   1 
ATOM   2872 C  C    . GLN   A 1 403 ? -11.558 10.764  52.776 1.00 105.70 ?  430 GLN   A C    1 
ATOM   2873 O  O    . GLN   A 1 403 ? -10.768 10.809  51.826 1.00 106.20 ?  430 GLN   A O    1 
ATOM   2874 C  CB   . GLN   A 1 403 ? -13.965 11.222  52.251 1.00 117.78 ?  430 GLN   A CB   1 
ATOM   2875 C  CG   . GLN   A 1 403 ? -15.012 10.777  51.246 1.00 125.06 ?  430 GLN   A CG   1 
ATOM   2876 C  CD   . GLN   A 1 403 ? -15.579 11.934  50.450 1.00 136.49 ?  430 GLN   A CD   1 
ATOM   2877 O  OE1  . GLN   A 1 403 ? -16.788 12.160  50.437 1.00 134.38 ?  430 GLN   A OE1  1 
ATOM   2878 N  NE2  . GLN   A 1 403 ? -14.704 12.674  49.779 1.00 137.31 ?  430 GLN   A NE2  1 
ATOM   2879 N  N    . ARG   A 1 404 ? -11.253 11.248  53.982 1.00 98.92  ?  431 ARG   A N    1 
ATOM   2880 C  CA   . ARG   A 1 404 ? -9.941  11.829  54.243 1.00 104.82 ?  431 ARG   A CA   1 
ATOM   2881 C  C    . ARG   A 1 404 ? -8.834  10.803  54.042 1.00 100.66 ?  431 ARG   A C    1 
ATOM   2882 O  O    . ARG   A 1 404 ? -7.807  11.099  53.419 1.00 100.92 ?  431 ARG   A O    1 
ATOM   2883 C  CB   . ARG   A 1 404 ? -9.899  12.397  55.662 1.00 100.04 ?  431 ARG   A CB   1 
ATOM   2884 C  CG   . ARG   A 1 404 ? -8.626  13.151  56.006 1.00 102.27 ?  431 ARG   A CG   1 
ATOM   2885 C  CD   . ARG   A 1 404 ? -8.572  13.557  57.482 1.00 98.87  ?  431 ARG   A CD   1 
ATOM   2886 N  NE   . ARG   A 1 404 ? -7.912  12.578  58.343 1.00 107.07 ?  431 ARG   A NE   1 
ATOM   2887 C  CZ   . ARG   A 1 404 ? -8.445  11.435  58.759 1.00 108.52 ?  431 ARG   A CZ   1 
ATOM   2888 N  NH1  . ARG   A 1 404 ? -9.681  11.090  58.446 1.00 115.96 ?  431 ARG   A NH1  1 
ATOM   2889 N  NH2  . ARG   A 1 404 ? -7.720  10.624  59.525 1.00 107.48 ?  431 ARG   A NH2  1 
ATOM   2890 N  N    . ASN   A 1 405 ? -9.029  9.587   54.555 1.00 98.63  ?  432 ASN   A N    1 
ATOM   2891 C  CA   . ASN   A 1 405 ? -8.018  8.546   54.415 1.00 104.46 ?  432 ASN   A CA   1 
ATOM   2892 C  C    . ASN   A 1 405 ? -7.887  8.055   52.980 1.00 101.13 ?  432 ASN   A C    1 
ATOM   2893 O  O    . ASN   A 1 405 ? -6.829  7.533   52.611 1.00 94.47  ?  432 ASN   A O    1 
ATOM   2894 C  CB   . ASN   A 1 405 ? -8.344  7.381   55.348 1.00 105.98 ?  432 ASN   A CB   1 
ATOM   2895 C  CG   . ASN   A 1 405 ? -8.228  7.761   56.811 1.00 101.65 ?  432 ASN   A CG   1 
ATOM   2896 O  OD1  . ASN   A 1 405 ? -7.711  8.827   57.148 1.00 102.13 ?  432 ASN   A OD1  1 
ATOM   2897 N  ND2  . ASN   A 1 405 ? -8.714  6.892   57.689 1.00 94.24  ?  432 ASN   A ND2  1 
ATOM   2898 N  N    . GLU   A 1 406 ? -8.935  8.206   52.166 1.00 106.10 ?  433 GLU   A N    1 
ATOM   2899 C  CA   . GLU   A 1 406 ? -8.820  7.891   50.746 1.00 109.03 ?  433 GLU   A CA   1 
ATOM   2900 C  C    . GLU   A 1 406 ? -7.837  8.829   50.058 1.00 104.64 ?  433 GLU   A C    1 
ATOM   2901 O  O    . GLU   A 1 406 ? -7.107  8.421   49.147 1.00 103.96 ?  433 GLU   A O    1 
ATOM   2902 C  CB   . GLU   A 1 406 ? -10.193 7.974   50.078 1.00 117.46 ?  433 GLU   A CB   1 
ATOM   2903 C  CG   . GLU   A 1 406 ? -10.934 6.650   49.978 1.00 121.92 ?  433 GLU   A CG   1 
ATOM   2904 C  CD   . GLU   A 1 406 ? -11.664 6.491   48.657 1.00 127.60 ?  433 GLU   A CD   1 
ATOM   2905 O  OE1  . GLU   A 1 406 ? -11.239 5.653   47.835 1.00 114.25 ?  433 GLU   A OE1  1 
ATOM   2906 O  OE2  . GLU   A 1 406 ? -12.664 7.209   48.441 1.00 127.34 ?  433 GLU   A OE2  1 
ATOM   2907 N  N    . ILE   A 1 407 ? -7.800  10.090  50.489 1.00 104.03 ?  434 ILE   A N    1 
ATOM   2908 C  CA   . ILE   A 1 407 ? -6.923  11.077  49.869 1.00 99.27  ?  434 ILE   A CA   1 
ATOM   2909 C  C    . ILE   A 1 407 ? -5.496  10.936  50.381 1.00 100.21 ?  434 ILE   A C    1 
ATOM   2910 O  O    . ILE   A 1 407 ? -4.536  11.062  49.612 1.00 93.72  ?  434 ILE   A O    1 
ATOM   2911 C  CB   . ILE   A 1 407 ? -7.477  12.492  50.112 1.00 100.31 ?  434 ILE   A CB   1 
ATOM   2912 C  CG1  . ILE   A 1 407 ? -8.966  12.547  49.759 1.00 94.74  ?  434 ILE   A CG1  1 
ATOM   2913 C  CG2  . ILE   A 1 407 ? -6.682  13.519  49.324 1.00 98.20  ?  434 ILE   A CG2  1 
ATOM   2914 C  CD1  . ILE   A 1 407 ? -9.548  13.944  49.760 1.00 94.65  ?  434 ILE   A CD1  1 
ATOM   2915 N  N    . LEU   A 1 408 ? -5.331  10.680  51.681 1.00 94.41  ?  435 LEU   A N    1 
ATOM   2916 C  CA   . LEU   A 1 408 ? -3.992  10.531  52.242 1.00 92.27  ?  435 LEU   A CA   1 
ATOM   2917 C  C    . LEU   A 1 408 ? -3.264  9.347   51.620 1.00 94.93  ?  435 LEU   A C    1 
ATOM   2918 O  O    . LEU   A 1 408 ? -2.080  9.447   51.277 1.00 93.30  ?  435 LEU   A O    1 
ATOM   2919 C  CB   . LEU   A 1 408 ? -4.070  10.369  53.760 1.00 89.00  ?  435 LEU   A CB   1 
ATOM   2920 C  CG   . LEU   A 1 408 ? -4.849  11.427  54.544 1.00 91.92  ?  435 LEU   A CG   1 
ATOM   2921 C  CD1  . LEU   A 1 408 ? -4.573  11.307  56.037 1.00 99.92  ?  435 LEU   A CD1  1 
ATOM   2922 C  CD2  . LEU   A 1 408 ? -4.527  12.816  54.036 1.00 90.29  ?  435 LEU   A CD2  1 
ATOM   2923 N  N    . THR   A 1 409 ? -3.959  8.218   51.462 1.00 94.78  ?  436 THR   A N    1 
ATOM   2924 C  CA   . THR   A 1 409 ? -3.342  7.037   50.868 1.00 90.44  ?  436 THR   A CA   1 
ATOM   2925 C  C    . THR   A 1 409 ? -2.928  7.289   49.423 1.00 94.62  ?  436 THR   A C    1 
ATOM   2926 O  O    . THR   A 1 409 ? -1.962  6.689   48.937 1.00 96.25  ?  436 THR   A O    1 
ATOM   2927 C  CB   . THR   A 1 409 ? -4.307  5.851   50.950 1.00 94.25  ?  436 THR   A CB   1 
ATOM   2928 O  OG1  . THR   A 1 409 ? -4.739  5.680   52.306 1.00 89.84  ?  436 THR   A OG1  1 
ATOM   2929 C  CG2  . THR   A 1 409 ? -3.634  4.568   50.483 1.00 91.21  ?  436 THR   A CG2  1 
ATOM   2930 N  N    . ALA   A 1 410 ? -3.629  8.186   48.728 1.00 90.78  ?  437 ALA   A N    1 
ATOM   2931 C  CA   . ALA   A 1 410 ? -3.330  8.439   47.325 1.00 84.95  ?  437 ALA   A CA   1 
ATOM   2932 C  C    . ALA   A 1 410 ? -2.121  9.347   47.137 1.00 87.04  ?  437 ALA   A C    1 
ATOM   2933 O  O    . ALA   A 1 410 ? -1.393  9.198   46.150 1.00 93.05  ?  437 ALA   A O    1 
ATOM   2934 C  CB   . ALA   A 1 410 ? -4.549  9.052   46.631 1.00 92.52  ?  437 ALA   A CB   1 
ATOM   2935 N  N    . ILE   A 1 411 ? -1.880  10.276  48.061 1.00 81.95  ?  438 ILE   A N    1 
ATOM   2936 C  CA   . ILE   A 1 411 ? -0.888  11.328  47.851 1.00 85.33  ?  438 ILE   A CA   1 
ATOM   2937 C  C    . ILE   A 1 411 ? 0.337   11.197  48.743 1.00 80.78  ?  438 ILE   A C    1 
ATOM   2938 O  O    . ILE   A 1 411 ? 1.318   11.928  48.523 1.00 85.64  ?  438 ILE   A O    1 
ATOM   2939 C  CB   . ILE   A 1 411 ? -1.513  12.728  48.029 1.00 79.82  ?  438 ILE   A CB   1 
ATOM   2940 C  CG1  . ILE   A 1 411 ? -1.717  13.032  49.514 1.00 77.97  ?  438 ILE   A CG1  1 
ATOM   2941 C  CG2  . ILE   A 1 411 ? -2.828  12.825  47.272 1.00 74.42  ?  438 ILE   A CG2  1 
ATOM   2942 C  CD1  . ILE   A 1 411 ? -1.943  14.496  49.812 1.00 81.90  ?  438 ILE   A CD1  1 
ATOM   2943 N  N    . LEU   A 1 412 ? 0.328   10.299  49.730 1.00 81.52  ?  439 LEU   A N    1 
ATOM   2944 C  CA   . LEU   A 1 412 ? 1.437   10.246  50.680 1.00 87.06  ?  439 LEU   A CA   1 
ATOM   2945 C  C    . LEU   A 1 412 ? 2.723   9.771   50.009 1.00 83.65  ?  439 LEU   A C    1 
ATOM   2946 O  O    . LEU   A 1 412 ? 3.802   10.316  50.272 1.00 83.54  ?  439 LEU   A O    1 
ATOM   2947 C  CB   . LEU   A 1 412 ? 1.069   9.346   51.863 1.00 92.20  ?  439 LEU   A CB   1 
ATOM   2948 C  CG   . LEU   A 1 412 ? 1.789   9.504   53.210 1.00 94.24  ?  439 LEU   A CG   1 
ATOM   2949 C  CD1  . LEU   A 1 412 ? 3.263   9.118   53.162 1.00 102.24 ?  439 LEU   A CD1  1 
ATOM   2950 C  CD2  . LEU   A 1 412 ? 1.635   10.932  53.712 1.00 90.60  ?  439 LEU   A CD2  1 
ATOM   2951 N  N    . ALA   A 1 413 ? 2.630   8.762   49.139 1.00 90.06  ?  440 ALA   A N    1 
ATOM   2952 C  CA   . ALA   A 1 413 ? 3.824   8.261   48.465 1.00 73.98  ?  440 ALA   A CA   1 
ATOM   2953 C  C    . ALA   A 1 413 ? 4.462   9.325   47.582 1.00 83.71  ?  440 ALA   A C    1 
ATOM   2954 O  O    . ALA   A 1 413 ? 5.687   9.336   47.411 1.00 77.49  ?  440 ALA   A O    1 
ATOM   2955 C  CB   . ALA   A 1 413 ? 3.482   7.020   47.640 1.00 68.27  ?  440 ALA   A CB   1 
ATOM   2956 N  N    . SER   A 1 414 ? 3.655   10.228  47.019 1.00 85.74  ?  441 SER   A N    1 
ATOM   2957 C  CA   . SER   A 1 414 ? 4.198   11.298  46.189 1.00 74.36  ?  441 SER   A CA   1 
ATOM   2958 C  C    . SER   A 1 414 ? 4.815   12.404  47.036 1.00 72.70  ?  441 SER   A C    1 
ATOM   2959 O  O    . SER   A 1 414 ? 5.836   12.986  46.653 1.00 71.76  ?  441 SER   A O    1 
ATOM   2960 C  CB   . SER   A 1 414 ? 3.104   11.866  45.284 1.00 75.21  ?  441 SER   A CB   1 
ATOM   2961 O  OG   . SER   A 1 414 ? 2.247   10.839  44.816 1.00 92.22  ?  441 SER   A OG   1 
ATOM   2962 N  N    . LEU   A 1 415 ? 4.211   12.709  48.187 1.00 70.74  ?  442 LEU   A N    1 
ATOM   2963 C  CA   . LEU   A 1 415 ? 4.769   13.734  49.062 1.00 74.31  ?  442 LEU   A CA   1 
ATOM   2964 C  C    . LEU   A 1 415 ? 6.034   13.248  49.757 1.00 86.64  ?  442 LEU   A C    1 
ATOM   2965 O  O    . LEU   A 1 415 ? 6.945   14.045  50.011 1.00 79.33  ?  442 LEU   A O    1 
ATOM   2966 C  CB   . LEU   A 1 415 ? 3.728   14.172  50.092 1.00 65.37  ?  442 LEU   A CB   1 
ATOM   2967 C  CG   . LEU   A 1 415 ? 2.498   14.890  49.530 1.00 71.36  ?  442 LEU   A CG   1 
ATOM   2968 C  CD1  . LEU   A 1 415 ? 1.629   15.439  50.652 1.00 64.70  ?  442 LEU   A CD1  1 
ATOM   2969 C  CD2  . LEU   A 1 415 ? 2.905   15.997  48.569 1.00 75.23  ?  442 LEU   A CD2  1 
ATOM   2970 N  N    . THR   A 1 416 ? 6.107   11.953  50.073 1.00 86.20  ?  443 THR   A N    1 
ATOM   2971 C  CA   . THR   A 1 416 ? 7.331   11.393  50.637 1.00 87.37  ?  443 THR   A CA   1 
ATOM   2972 C  C    . THR   A 1 416 ? 8.486   11.510  49.651 1.00 82.99  ?  443 THR   A C    1 
ATOM   2973 O  O    . THR   A 1 416 ? 9.581   11.962  50.008 1.00 94.38  ?  443 THR   A O    1 
ATOM   2974 C  CB   . THR   A 1 416 ? 7.109   9.932   51.033 1.00 87.60  ?  443 THR   A CB   1 
ATOM   2975 O  OG1  . THR   A 1 416 ? 6.229   9.866   52.162 1.00 95.04  ?  443 THR   A OG1  1 
ATOM   2976 C  CG2  . THR   A 1 416 ? 8.431   9.262   51.382 1.00 94.30  ?  443 THR   A CG2  1 
ATOM   2977 N  N    . ALA   A 1 417 ? 8.255   11.109  48.398 1.00 75.64  ?  444 ALA   A N    1 
ATOM   2978 C  CA   . ALA   A 1 417 ? 9.300   11.198  47.386 1.00 75.71  ?  444 ALA   A CA   1 
ATOM   2979 C  C    . ALA   A 1 417 ? 9.707   12.641  47.122 1.00 80.49  ?  444 ALA   A C    1 
ATOM   2980 O  O    . ALA   A 1 417 ? 10.879  12.911  46.836 1.00 77.68  ?  444 ALA   A O    1 
ATOM   2981 C  CB   . ALA   A 1 417 ? 8.835   10.532  46.091 1.00 62.96  ?  444 ALA   A CB   1 
ATOM   2982 N  N    . ARG   A 1 418 ? 8.762   13.580  47.217 1.00 79.28  ?  445 ARG   A N    1 
ATOM   2983 C  CA   . ARG   A 1 418 ? 9.092   14.983  46.989 1.00 72.15  ?  445 ARG   A CA   1 
ATOM   2984 C  C    . ARG   A 1 418 ? 10.048  15.501  48.056 1.00 72.27  ?  445 ARG   A C    1 
ATOM   2985 O  O    . ARG   A 1 418 ? 11.043  16.163  47.742 1.00 76.37  ?  445 ARG   A O    1 
ATOM   2986 C  CB   . ARG   A 1 418 ? 7.816   15.826  46.949 1.00 70.24  ?  445 ARG   A CB   1 
ATOM   2987 C  CG   . ARG   A 1 418 ? 8.056   17.282  46.577 1.00 78.73  ?  445 ARG   A CG   1 
ATOM   2988 C  CD   . ARG   A 1 418 ? 6.750   18.044  46.416 1.00 77.74  ?  445 ARG   A CD   1 
ATOM   2989 N  NE   . ARG   A 1 418 ? 5.786   17.312  45.602 1.00 81.07  ?  445 ARG   A NE   1 
ATOM   2990 C  CZ   . ARG   A 1 418 ? 4.478   17.531  45.613 1.00 67.54  ?  445 ARG   A CZ   1 
ATOM   2991 N  NH1  . ARG   A 1 418 ? 3.940   18.469  46.374 1.00 68.88  ?  445 ARG   A NH1  1 
ATOM   2992 N  NH2  . ARG   A 1 418 ? 3.690   16.790  44.839 1.00 71.89  ?  445 ARG   A NH2  1 
ATOM   2993 N  N    . GLN   A 1 419 ? 9.767   15.202  49.327 1.00 80.26  ?  446 GLN   A N    1 
ATOM   2994 C  CA   . GLN   A 1 419 ? 10.652  15.643  50.401 1.00 83.70  ?  446 GLN   A CA   1 
ATOM   2995 C  C    . GLN   A 1 419 ? 11.999  14.934  50.337 1.00 78.65  ?  446 GLN   A C    1 
ATOM   2996 O  O    . GLN   A 1 419 ? 13.046  15.560  50.540 1.00 80.13  ?  446 GLN   A O    1 
ATOM   2997 C  CB   . GLN   A 1 419 ? 9.987   15.413  51.759 1.00 88.45  ?  446 GLN   A CB   1 
ATOM   2998 C  CG   . GLN   A 1 419 ? 10.886  15.698  52.960 1.00 103.79 ?  446 GLN   A CG   1 
ATOM   2999 C  CD   . GLN   A 1 419 ? 11.264  17.164  53.100 1.00 111.25 ?  446 GLN   A CD   1 
ATOM   3000 O  OE1  . GLN   A 1 419 ? 10.732  18.031  52.405 1.00 105.64 ?  446 GLN   A OE1  1 
ATOM   3001 N  NE2  . GLN   A 1 419 ? 12.195  17.447  54.006 1.00 111.35 ?  446 GLN   A NE2  1 
ATOM   3002 N  N    . ASN   A 1 420 ? 11.993  13.629  50.054 1.00 81.52  ?  447 ASN   A N    1 
ATOM   3003 C  CA   . ASN   A 1 420 ? 13.245  12.883  49.979 1.00 77.10  ?  447 ASN   A CA   1 
ATOM   3004 C  C    . ASN   A 1 420 ? 14.111  13.365  48.822 1.00 76.68  ?  447 ASN   A C    1 
ATOM   3005 O  O    . ASN   A 1 420 ? 15.327  13.527  48.975 1.00 88.30  ?  447 ASN   A O    1 
ATOM   3006 C  CB   . ASN   A 1 420 ? 12.960  11.387  49.847 1.00 78.13  ?  447 ASN   A CB   1 
ATOM   3007 C  CG   . ASN   A 1 420 ? 12.416  10.782  51.125 1.00 90.72  ?  447 ASN   A CG   1 
ATOM   3008 O  OD1  . ASN   A 1 420 ? 12.295  11.461  52.145 1.00 97.60  ?  447 ASN   A OD1  1 
ATOM   3009 N  ND2  . ASN   A 1 420 ? 12.087  9.496   51.078 1.00 101.52 ?  447 ASN   A ND2  1 
ATOM   3010 N  N    . LEU   A 1 421 ? 13.504  13.601  47.657 1.00 75.19  ?  448 LEU   A N    1 
ATOM   3011 C  CA   . LEU   A 1 421 ? 14.283  14.040  46.505 1.00 77.02  ?  448 LEU   A CA   1 
ATOM   3012 C  C    . LEU   A 1 421 ? 14.746  15.484  46.654 1.00 74.97  ?  448 LEU   A C    1 
ATOM   3013 O  O    . LEU   A 1 421 ? 15.804  15.848  46.130 1.00 79.31  ?  448 LEU   A O    1 
ATOM   3014 C  CB   . LEU   A 1 421 ? 13.470  13.869  45.221 1.00 72.15  ?  448 LEU   A CB   1 
ATOM   3015 C  CG   . LEU   A 1 421 ? 13.462  12.458  44.628 1.00 78.78  ?  448 LEU   A CG   1 
ATOM   3016 C  CD1  . LEU   A 1 421 ? 12.167  12.192  43.876 1.00 78.66  ?  448 LEU   A CD1  1 
ATOM   3017 C  CD2  . LEU   A 1 421 ? 14.667  12.246  43.723 1.00 71.26  ?  448 LEU   A CD2  1 
ATOM   3018 N  N    . ARG   A 1 422 ? 13.977  16.316  47.360 1.00 74.85  ?  449 ARG   A N    1 
ATOM   3019 C  CA   . ARG   A 1 422 ? 14.395  17.698  47.566 1.00 80.27  ?  449 ARG   A CA   1 
ATOM   3020 C  C    . ARG   A 1 422 ? 15.642  17.773  48.437 1.00 87.35  ?  449 ARG   A C    1 
ATOM   3021 O  O    . ARG   A 1 422 ? 16.509  18.627  48.218 1.00 96.43  ?  449 ARG   A O    1 
ATOM   3022 C  CB   . ARG   A 1 422 ? 13.257  18.509  48.185 1.00 77.56  ?  449 ARG   A CB   1 
ATOM   3023 C  CG   . ARG   A 1 422 ? 12.244  19.012  47.172 1.00 80.33  ?  449 ARG   A CG   1 
ATOM   3024 C  CD   . ARG   A 1 422 ? 11.103  19.757  47.841 1.00 83.30  ?  449 ARG   A CD   1 
ATOM   3025 N  NE   . ARG   A 1 422 ? 10.261  20.432  46.861 1.00 78.87  ?  449 ARG   A NE   1 
ATOM   3026 C  CZ   . ARG   A 1 422 ? 9.159   21.107  47.156 1.00 74.57  ?  449 ARG   A CZ   1 
ATOM   3027 N  NH1  . ARG   A 1 422 ? 8.745   21.243  48.404 1.00 77.20  ?  449 ARG   A NH1  1 
ATOM   3028 N  NH2  . ARG   A 1 422 ? 8.457   21.664  46.173 1.00 86.45  ?  449 ARG   A NH2  1 
ATOM   3029 N  N    . ARG   A 1 423 ? 15.751  16.886  49.429 1.00 82.15  ?  450 ARG   A N    1 
ATOM   3030 C  CA   . ARG   A 1 423 ? 16.939  16.871  50.275 1.00 85.45  ?  450 ARG   A CA   1 
ATOM   3031 C  C    . ARG   A 1 423 ? 18.171  16.443  49.488 1.00 85.27  ?  450 ARG   A C    1 
ATOM   3032 O  O    . ARG   A 1 423 ? 19.250  17.025  49.649 1.00 94.93  ?  450 ARG   A O    1 
ATOM   3033 C  CB   . ARG   A 1 423 ? 16.720  15.950  51.475 1.00 90.17  ?  450 ARG   A CB   1 
ATOM   3034 C  CG   . ARG   A 1 423 ? 15.977  16.602  52.630 1.00 94.95  ?  450 ARG   A CG   1 
ATOM   3035 C  CD   . ARG   A 1 423 ? 16.069  15.760  53.893 1.00 108.57 ?  450 ARG   A CD   1 
ATOM   3036 N  NE   . ARG   A 1 423 ? 15.710  16.518  55.086 1.00 125.88 ?  450 ARG   A NE   1 
ATOM   3037 C  CZ   . ARG   A 1 423 ? 16.585  17.058  55.922 1.00 124.98 ?  450 ARG   A CZ   1 
ATOM   3038 N  NH1  . ARG   A 1 423 ? 17.889  16.947  55.725 1.00 114.47 ?  450 ARG   A NH1  1 
ATOM   3039 N  NH2  . ARG   A 1 423 ? 16.142  17.725  56.984 1.00 123.40 ?  450 ARG   A NH2  1 
ATOM   3040 N  N    . GLU   A 1 424 ? 18.031  15.429  48.630 1.00 77.83  ?  451 GLU   A N    1 
ATOM   3041 C  CA   . GLU   A 1 424 ? 19.157  14.991  47.810 1.00 83.14  ?  451 GLU   A CA   1 
ATOM   3042 C  C    . GLU   A 1 424 ? 19.595  16.092  46.852 1.00 90.95  ?  451 GLU   A C    1 
ATOM   3043 O  O    . GLU   A 1 424 ? 20.792  16.362  46.703 1.00 102.98 ?  451 GLU   A O    1 
ATOM   3044 C  CB   . GLU   A 1 424 ? 18.787  13.724  47.036 1.00 88.94  ?  451 GLU   A CB   1 
ATOM   3045 C  CG   . GLU   A 1 424 ? 19.499  13.593  45.693 1.00 108.84 ?  451 GLU   A CG   1 
ATOM   3046 C  CD   . GLU   A 1 424 ? 19.136  12.322  44.949 1.00 121.63 ?  451 GLU   A CD   1 
ATOM   3047 O  OE1  . GLU   A 1 424 ? 19.015  11.263  45.600 1.00 123.98 ?  451 GLU   A OE1  1 
ATOM   3048 O  OE2  . GLU   A 1 424 ? 18.976  12.382  43.712 1.00 108.89 ?  451 GLU   A OE2  1 
ATOM   3049 N  N    . TRP   A 1 425 ? 18.632  16.744  46.196 1.00 79.14  ?  452 TRP   A N    1 
ATOM   3050 C  CA   . TRP   A 1 425 ? 18.972  17.790  45.236 1.00 87.45  ?  452 TRP   A CA   1 
ATOM   3051 C  C    . TRP   A 1 425 ? 19.595  18.996  45.928 1.00 87.24  ?  452 TRP   A C    1 
ATOM   3052 O  O    . TRP   A 1 425 ? 20.560  19.578  45.421 1.00 86.32  ?  452 TRP   A O    1 
ATOM   3053 C  CB   . TRP   A 1 425 ? 17.731  18.202  44.444 1.00 75.85  ?  452 TRP   A CB   1 
ATOM   3054 C  CG   . TRP   A 1 425 ? 17.434  17.293  43.290 1.00 60.96  ?  452 TRP   A CG   1 
ATOM   3055 C  CD1  . TRP   A 1 425 ? 16.470  16.328  43.231 1.00 64.00  ?  452 TRP   A CD1  1 
ATOM   3056 C  CD2  . TRP   A 1 425 ? 18.116  17.256  42.031 1.00 64.94  ?  452 TRP   A CD2  1 
ATOM   3057 N  NE1  . TRP   A 1 425 ? 16.505  15.698  42.010 1.00 60.83  ?  452 TRP   A NE1  1 
ATOM   3058 C  CE2  . TRP   A 1 425 ? 17.507  16.248  41.256 1.00 63.62  ?  452 TRP   A CE2  1 
ATOM   3059 C  CE3  . TRP   A 1 425 ? 19.179  17.980  41.483 1.00 63.32  ?  452 TRP   A CE3  1 
ATOM   3060 C  CZ2  . TRP   A 1 425 ? 17.928  15.946  39.962 1.00 57.67  ?  452 TRP   A CZ2  1 
ATOM   3061 C  CZ3  . TRP   A 1 425 ? 19.594  17.678  40.199 1.00 68.63  ?  452 TRP   A CZ3  1 
ATOM   3062 C  CH2  . TRP   A 1 425 ? 18.970  16.671  39.453 1.00 61.56  ?  452 TRP   A CH2  1 
ATOM   3063 N  N    . HIS   A 1 426 ? 19.060  19.385  47.088 1.00 90.67  ?  453 HIS   A N    1 
ATOM   3064 C  CA   . HIS   A 1 426 ? 19.656  20.487  47.836 1.00 97.15  ?  453 HIS   A CA   1 
ATOM   3065 C  C    . HIS   A 1 426 ? 21.050  20.130  48.335 1.00 105.86 ?  453 HIS   A C    1 
ATOM   3066 O  O    . HIS   A 1 426 ? 21.914  21.008  48.437 1.00 107.81 ?  453 HIS   A O    1 
ATOM   3067 C  CB   . HIS   A 1 426 ? 18.753  20.880  49.006 1.00 92.57  ?  453 HIS   A CB   1 
ATOM   3068 C  CG   . HIS   A 1 426 ? 19.289  22.009  49.829 1.00 97.67  ?  453 HIS   A CG   1 
ATOM   3069 N  ND1  . HIS   A 1 426 ? 20.058  21.810  50.955 1.00 109.79 ?  453 HIS   A ND1  1 
ATOM   3070 C  CD2  . HIS   A 1 426 ? 19.166  23.351  49.690 1.00 105.86 ?  453 HIS   A CD2  1 
ATOM   3071 C  CE1  . HIS   A 1 426 ? 20.385  22.980  51.475 1.00 121.93 ?  453 HIS   A CE1  1 
ATOM   3072 N  NE2  . HIS   A 1 426 ? 19.856  23.931  50.726 1.00 113.88 ?  453 HIS   A NE2  1 
ATOM   3073 N  N    . ALA   A 1 427 ? 21.288  18.853  48.646 1.00 102.78 ?  454 ALA   A N    1 
ATOM   3074 C  CA   . ALA   A 1 427 ? 22.623  18.427  49.049 1.00 92.74  ?  454 ALA   A CA   1 
ATOM   3075 C  C    . ALA   A 1 427 ? 23.578  18.381  47.864 1.00 101.74 ?  454 ALA   A C    1 
ATOM   3076 O  O    . ALA   A 1 427 ? 24.777  18.637  48.026 1.00 110.39 ?  454 ALA   A O    1 
ATOM   3077 C  CB   . ALA   A 1 427 ? 22.558  17.062  49.732 1.00 89.03  ?  454 ALA   A CB   1 
ATOM   3078 N  N    . ARG   A 1 428 ? 23.071  18.055  46.672 1.00 96.90  ?  455 ARG   A N    1 
ATOM   3079 C  CA   . ARG   A 1 428 ? 23.917  18.050  45.482 1.00 99.84  ?  455 ARG   A CA   1 
ATOM   3080 C  C    . ARG   A 1 428 ? 24.378  19.457  45.127 1.00 99.88  ?  455 ARG   A C    1 
ATOM   3081 O  O    . ARG   A 1 428 ? 25.533  19.657  44.734 1.00 110.67 ?  455 ARG   A O    1 
ATOM   3082 C  CB   . ARG   A 1 428 ? 23.167  17.427  44.305 1.00 102.14 ?  455 ARG   A CB   1 
ATOM   3083 C  CG   . ARG   A 1 428 ? 23.219  15.915  44.264 1.00 89.21  ?  455 ARG   A CG   1 
ATOM   3084 C  CD   . ARG   A 1 428 ? 22.591  15.364  42.994 1.00 97.56  ?  455 ARG   A CD   1 
ATOM   3085 N  NE   . ARG   A 1 428 ? 23.462  15.506  41.833 1.00 84.89  ?  455 ARG   A NE   1 
ATOM   3086 C  CZ   . ARG   A 1 428 ? 23.169  15.058  40.620 1.00 86.45  ?  455 ARG   A CZ   1 
ATOM   3087 N  NH1  . ARG   A 1 428 ? 22.027  14.439  40.369 1.00 81.76  ?  455 ARG   A NH1  1 
ATOM   3088 N  NH2  . ARG   A 1 428 ? 24.045  15.234  39.634 1.00 84.32  ?  455 ARG   A NH2  1 
ATOM   3089 N  N    . CYS   A 1 429 ? 23.489  20.443  45.259 1.00 97.71  ?  456 CYS   A N    1 
ATOM   3090 C  CA   . CYS   A 1 429 ? 23.847  21.813  44.912 1.00 107.09 ?  456 CYS   A CA   1 
ATOM   3091 C  C    . CYS   A 1 429 ? 24.820  22.414  45.918 1.00 118.39 ?  456 CYS   A C    1 
ATOM   3092 O  O    . CYS   A 1 429 ? 25.588  23.318  45.570 1.00 119.71 ?  456 CYS   A O    1 
ATOM   3093 C  CB   . CYS   A 1 429 ? 22.588  22.674  44.811 1.00 107.31 ?  456 CYS   A CB   1 
ATOM   3094 S  SG   . CYS   A 1 429 ? 21.406  22.117  43.561 1.00 97.16  ?  456 CYS   A SG   1 
ATOM   3095 N  N    . GLN   A 1 430 ? 24.808  21.928  47.158 1.00 120.92 ?  457 GLN   A N    1 
ATOM   3096 C  CA   . GLN   A 1 430 ? 25.702  22.451  48.183 1.00 124.59 ?  457 GLN   A CA   1 
ATOM   3097 C  C    . GLN   A 1 430 ? 26.680  21.383  48.657 1.00 124.55 ?  457 GLN   A C    1 
ATOM   3098 O  O    . GLN   A 1 430 ? 26.687  21.017  49.837 1.00 123.98 ?  457 GLN   A O    1 
ATOM   3099 C  CB   . GLN   A 1 430 ? 24.900  23.005  49.363 1.00 121.80 ?  457 GLN   A CB   1 
ATOM   3100 C  CG   . GLN   A 1 430 ? 24.486  24.459  49.195 1.00 126.32 ?  457 GLN   A CG   1 
ATOM   3101 C  CD   . GLN   A 1 430 ? 23.570  24.941  50.302 1.00 143.46 ?  457 GLN   A CD   1 
ATOM   3102 O  OE1  . GLN   A 1 430 ? 23.691  24.519  51.452 1.00 142.55 ?  457 GLN   A OE1  1 
ATOM   3103 N  NE2  . GLN   A 1 430 ? 22.646  25.832  49.960 1.00 148.20 ?  457 GLN   A NE2  1 
ATOM   3104 N  N    . SER   A 1 431 ? 27.502  20.877  47.744 1.00 118.34 ?  458 SER   A N    1 
ATOM   3105 C  CA   . SER   A 1 431 ? 28.574  19.949  48.067 1.00 121.38 ?  458 SER   A CA   1 
ATOM   3106 C  C    . SER   A 1 431 ? 29.920  20.618  47.820 1.00 132.95 ?  458 SER   A C    1 
ATOM   3107 O  O    . SER   A 1 431 ? 30.019  21.617  47.103 1.00 135.91 ?  458 SER   A O    1 
ATOM   3108 C  CB   . SER   A 1 431 ? 28.459  18.661  47.243 1.00 117.13 ?  458 SER   A CB   1 
ATOM   3109 O  OG   . SER   A 1 431 ? 28.752  18.895  45.877 1.00 113.61 ?  458 SER   A OG   1 
ATOM   3110 N  N    . ARG   A 1 432 ? 30.965  20.053  48.433 1.00 134.21 ?  459 ARG   A N    1 
ATOM   3111 C  CA   . ARG   A 1 432 ? 32.288  20.667  48.351 1.00 131.50 ?  459 ARG   A CA   1 
ATOM   3112 C  C    . ARG   A 1 432 ? 32.789  20.729  46.914 1.00 120.92 ?  459 ARG   A C    1 
ATOM   3113 O  O    . ARG   A 1 432 ? 33.384  21.731  46.501 1.00 123.76 ?  459 ARG   A O    1 
ATOM   3114 C  CB   . ARG   A 1 432 ? 33.279  19.911  49.236 1.00 138.90 ?  459 ARG   A CB   1 
ATOM   3115 C  CG   . ARG   A 1 432 ? 32.999  20.040  50.723 1.00 138.89 ?  459 ARG   A CG   1 
ATOM   3116 C  CD   . ARG   A 1 432 ? 33.802  19.037  51.532 1.00 137.92 ?  459 ARG   A CD   1 
ATOM   3117 N  NE   . ARG   A 1 432 ? 33.913  19.442  52.928 1.00 142.93 ?  459 ARG   A NE   1 
ATOM   3118 C  CZ   . ARG   A 1 432 ? 34.780  20.336  53.383 1.00 152.30 ?  459 ARG   A CZ   1 
ATOM   3119 N  NH1  . ARG   A 1 432 ? 35.643  20.934  52.578 1.00 142.15 ?  459 ARG   A NH1  1 
ATOM   3120 N  NH2  . ARG   A 1 432 ? 34.783  20.636  54.679 1.00 161.47 ?  459 ARG   A NH2  1 
ATOM   3121 N  N    . ILE   A 1 433 ? 32.558  19.670  46.134 1.00 105.99 ?  460 ILE   A N    1 
ATOM   3122 C  CA   . ILE   A 1 433 ? 32.963  19.691  44.735 1.00 101.98 ?  460 ILE   A CA   1 
ATOM   3123 C  C    . ILE   A 1 433 ? 32.105  20.649  43.917 1.00 114.82 ?  460 ILE   A C    1 
ATOM   3124 O  O    . ILE   A 1 433 ? 32.546  21.126  42.865 1.00 114.22 ?  460 ILE   A O    1 
ATOM   3125 C  CB   . ILE   A 1 433 ? 32.922  18.271  44.136 1.00 94.90  ?  460 ILE   A CB   1 
ATOM   3126 C  CG1  . ILE   A 1 433 ? 33.763  18.206  42.860 1.00 88.18  ?  460 ILE   A CG1  1 
ATOM   3127 C  CG2  . ILE   A 1 433 ? 31.490  17.837  43.860 1.00 101.71 ?  460 ILE   A CG2  1 
ATOM   3128 C  CD1  . ILE   A 1 433 ? 34.163  16.810  42.462 1.00 92.65  ?  460 ILE   A CD1  1 
ATOM   3129 N  N    . ALA   A 1 434 ? 30.891  20.958  44.381 1.00 119.10 ?  461 ALA   A N    1 
ATOM   3130 C  CA   . ALA   A 1 434 ? 30.010  21.861  43.653 1.00 119.31 ?  461 ALA   A CA   1 
ATOM   3131 C  C    . ALA   A 1 434 ? 30.445  23.317  43.749 1.00 126.82 ?  461 ALA   A C    1 
ATOM   3132 O  O    . ALA   A 1 434 ? 30.030  24.130  42.916 1.00 126.97 ?  461 ALA   A O    1 
ATOM   3133 C  CB   . ALA   A 1 434 ? 28.572  21.720  44.156 1.00 124.78 ?  461 ALA   A CB   1 
ATOM   3134 N  N    . ARG   A 1 435 ? 31.265  23.665  44.743 1.00 129.38 ?  462 ARG   A N    1 
ATOM   3135 C  CA   . ARG   A 1 435 ? 31.753  25.034  44.859 1.00 128.18 ?  462 ARG   A CA   1 
ATOM   3136 C  C    . ARG   A 1 435 ? 32.965  25.287  43.972 1.00 120.65 ?  462 ARG   A C    1 
ATOM   3137 O  O    . ARG   A 1 435 ? 33.156  26.413  43.499 1.00 123.90 ?  462 ARG   A O    1 
ATOM   3138 C  CB   . ARG   A 1 435 ? 32.111  25.350  46.313 1.00 129.70 ?  462 ARG   A CB   1 
ATOM   3139 C  CG   . ARG   A 1 435 ? 31.166  24.760  47.347 1.00 134.24 ?  462 ARG   A CG   1 
ATOM   3140 C  CD   . ARG   A 1 435 ? 30.964  25.725  48.508 1.00 140.06 ?  462 ARG   A CD   1 
ATOM   3141 N  NE   . ARG   A 1 435 ? 29.729  25.468  49.238 1.00 147.01 ?  462 ARG   A NE   1 
ATOM   3142 C  CZ   . ARG   A 1 435 ? 29.566  24.488  50.117 1.00 141.21 ?  462 ARG   A CZ   1 
ATOM   3143 N  NH1  . ARG   A 1 435 ? 30.543  23.640  50.396 1.00 139.09 ?  462 ARG   A NH1  1 
ATOM   3144 N  NH2  . ARG   A 1 435 ? 28.395  24.355  50.732 1.00 139.04 ?  462 ARG   A NH2  1 
ATOM   3145 N  N    . THR   A 1 436 ? 33.785  24.261  43.732 1.00 118.94 ?  463 THR   A N    1 
ATOM   3146 C  CA   . THR   A 1 436 ? 35.027  24.449  42.991 1.00 118.72 ?  463 THR   A CA   1 
ATOM   3147 C  C    . THR   A 1 436 ? 34.799  24.766  41.518 1.00 123.79 ?  463 THR   A C    1 
ATOM   3148 O  O    . THR   A 1 436 ? 35.723  25.249  40.857 1.00 129.79 ?  463 THR   A O    1 
ATOM   3149 C  CB   . THR   A 1 436 ? 35.913  23.208  43.120 1.00 123.56 ?  463 THR   A CB   1 
ATOM   3150 O  OG1  . THR   A 1 436 ? 35.589  22.274  42.082 1.00 122.38 ?  463 THR   A OG1  1 
ATOM   3151 C  CG2  . THR   A 1 436 ? 35.719  22.550  44.478 1.00 119.74 ?  463 THR   A CG2  1 
ATOM   3152 N  N    . LEU   A 1 437 ? 33.606  24.504  40.987 1.00 124.15 ?  464 LEU   A N    1 
ATOM   3153 C  CA   . LEU   A 1 437 ? 33.321  24.876  39.611 1.00 118.78 ?  464 LEU   A CA   1 
ATOM   3154 C  C    . LEU   A 1 437 ? 33.303  26.397  39.468 1.00 131.99 ?  464 LEU   A C    1 
ATOM   3155 O  O    . LEU   A 1 437 ? 33.008  27.115  40.428 1.00 128.03 ?  464 LEU   A O    1 
ATOM   3156 C  CB   . LEU   A 1 437 ? 31.982  24.300  39.155 1.00 123.94 ?  464 LEU   A CB   1 
ATOM   3157 C  CG   . LEU   A 1 437 ? 31.827  22.781  39.097 1.00 115.43 ?  464 LEU   A CG   1 
ATOM   3158 C  CD1  . LEU   A 1 437 ? 30.993  22.285  40.259 1.00 114.19 ?  464 LEU   A CD1  1 
ATOM   3159 C  CD2  . LEU   A 1 437 ? 31.211  22.358  37.773 1.00 103.95 ?  464 LEU   A CD2  1 
ATOM   3160 N  N    . PRO   A 1 438 ? 33.625  26.914  38.283 1.00 151.61 ?  465 PRO   A N    1 
ATOM   3161 C  CA   . PRO   A 1 438 ? 33.549  28.364  38.067 1.00 138.46 ?  465 PRO   A CA   1 
ATOM   3162 C  C    . PRO   A 1 438 ? 32.116  28.864  38.174 1.00 134.72 ?  465 PRO   A C    1 
ATOM   3163 O  O    . PRO   A 1 438 ? 31.150  28.098  38.200 1.00 130.44 ?  465 PRO   A O    1 
ATOM   3164 C  CB   . PRO   A 1 438 ? 34.121  28.568  36.659 1.00 137.60 ?  465 PRO   A CB   1 
ATOM   3165 C  CG   . PRO   A 1 438 ? 34.228  27.225  36.053 1.00 135.97 ?  465 PRO   A CG   1 
ATOM   3166 C  CD   . PRO   A 1 438 ? 34.180  26.190  37.126 1.00 134.97 ?  465 PRO   A CD   1 
ATOM   3167 N  N    . ALA   A 1 439 ? 31.989  30.192  38.228 1.00 138.77 ?  466 ALA   A N    1 
ATOM   3168 C  CA   . ALA   A 1 439 ? 30.723  30.810  38.608 1.00 127.30 ?  466 ALA   A CA   1 
ATOM   3169 C  C    . ALA   A 1 439 ? 29.630  30.594  37.569 1.00 124.36 ?  466 ALA   A C    1 
ATOM   3170 O  O    . ALA   A 1 439 ? 28.447  30.545  37.924 1.00 128.77 ?  466 ALA   A O    1 
ATOM   3171 C  CB   . ALA   A 1 439 ? 30.924  32.305  38.854 1.00 99.22  ?  466 ALA   A CB   1 
ATOM   3172 N  N    . ASP   A 1 440 ? 29.989  30.466  36.294 1.00 128.76 ?  467 ASP   A N    1 
ATOM   3173 C  CA   . ASP   A 1 440 ? 28.981  30.393  35.244 1.00 133.76 ?  467 ASP   A CA   1 
ATOM   3174 C  C    . ASP   A 1 440 ? 28.396  28.999  35.062 1.00 138.24 ?  467 ASP   A C    1 
ATOM   3175 O  O    . ASP   A 1 440 ? 27.519  28.823  34.209 1.00 137.60 ?  467 ASP   A O    1 
ATOM   3176 C  CB   . ASP   A 1 440 ? 29.560  30.893  33.919 1.00 142.01 ?  467 ASP   A CB   1 
ATOM   3177 C  CG   . ASP   A 1 440 ? 29.234  32.351  33.661 1.00 159.44 ?  467 ASP   A CG   1 
ATOM   3178 O  OD1  . ASP   A 1 440 ? 29.294  33.151  34.619 1.00 170.96 ?  467 ASP   A OD1  1 
ATOM   3179 O  OD2  . ASP   A 1 440 ? 28.912  32.698  32.505 1.00 155.68 ?  467 ASP   A OD2  1 
ATOM   3180 N  N    . GLN   A 1 441 ? 28.850  28.007  35.832 1.00 135.51 ?  468 GLN   A N    1 
ATOM   3181 C  CA   . GLN   A 1 441 ? 28.195  26.705  35.834 1.00 130.68 ?  468 GLN   A CA   1 
ATOM   3182 C  C    . GLN   A 1 441 ? 28.033  26.169  37.249 1.00 129.58 ?  468 GLN   A C    1 
ATOM   3183 O  O    . GLN   A 1 441 ? 27.970  24.951  37.452 1.00 127.01 ?  468 GLN   A O    1 
ATOM   3184 C  CB   . GLN   A 1 441 ? 28.947  25.689  34.978 1.00 132.65 ?  468 GLN   A CB   1 
ATOM   3185 C  CG   . GLN   A 1 441 ? 30.426  25.556  35.274 1.00 140.54 ?  468 GLN   A CG   1 
ATOM   3186 C  CD   . GLN   A 1 441 ? 30.979  24.278  34.701 1.00 138.19 ?  468 GLN   A CD   1 
ATOM   3187 O  OE1  . GLN   A 1 441 ? 30.233  23.473  34.159 1.00 128.90 ?  468 GLN   A OE1  1 
ATOM   3188 N  NE2  . GLN   A 1 441 ? 32.275  24.065  34.844 1.00 126.55 ?  468 GLN   A NE2  1 
ATOM   3189 N  N    . LYS   A 1 442 ? 27.972  27.054  38.234 1.00 127.67 ?  469 LYS   A N    1 
ATOM   3190 C  CA   . LYS   A 1 442 ? 27.684  26.625  39.593 1.00 125.95 ?  469 LYS   A CA   1 
ATOM   3191 C  C    . LYS   A 1 442 ? 26.230  26.177  39.682 1.00 124.53 ?  469 LYS   A C    1 
ATOM   3192 O  O    . LYS   A 1 442 ? 25.339  26.882  39.195 1.00 122.05 ?  469 LYS   A O    1 
ATOM   3193 C  CB   . LYS   A 1 442 ? 27.952  27.754  40.586 1.00 134.94 ?  469 LYS   A CB   1 
ATOM   3194 C  CG   . LYS   A 1 442 ? 29.421  27.960  40.910 1.00 149.62 ?  469 LYS   A CG   1 
ATOM   3195 C  CD   . LYS   A 1 442 ? 29.768  27.391  42.276 1.00 140.62 ?  469 LYS   A CD   1 
ATOM   3196 C  CE   . LYS   A 1 442 ? 29.166  28.227  43.394 1.00 139.92 ?  469 LYS   A CE   1 
ATOM   3197 N  NZ   . LYS   A 1 442 ? 29.602  27.748  44.735 1.00 136.03 ?  469 LYS   A NZ   1 
ATOM   3198 N  N    . PRO   A 1 443 ? 25.951  25.019  40.278 1.00 114.62 ?  470 PRO   A N    1 
ATOM   3199 C  CA   . PRO   A 1 443 ? 24.566  24.533  40.333 1.00 106.16 ?  470 PRO   A CA   1 
ATOM   3200 C  C    . PRO   A 1 443 ? 23.676  25.475  41.131 1.00 103.07 ?  470 PRO   A C    1 
ATOM   3201 O  O    . PRO   A 1 443 ? 24.004  25.867  42.253 1.00 103.37 ?  470 PRO   A O    1 
ATOM   3202 C  CB   . PRO   A 1 443 ? 24.696  23.167  41.017 1.00 98.11  ?  470 PRO   A CB   1 
ATOM   3203 C  CG   . PRO   A 1 443 ? 26.124  22.771  40.825 1.00 94.65  ?  470 PRO   A CG   1 
ATOM   3204 C  CD   . PRO   A 1 443 ? 26.902  24.049  40.844 1.00 116.09 ?  470 PRO   A CD   1 
ATOM   3205 N  N    . GLU   A 1 444 ? 22.546  25.846  40.537 1.00 98.95  ?  471 GLU   A N    1 
ATOM   3206 C  CA   . GLU   A 1 444 ? 21.519  26.611  41.228 1.00 102.02 ?  471 GLU   A CA   1 
ATOM   3207 C  C    . GLU   A 1 444 ? 20.422  25.659  41.684 1.00 101.53 ?  471 GLU   A C    1 
ATOM   3208 O  O    . GLU   A 1 444 ? 19.955  24.822  40.905 1.00 95.89  ?  471 GLU   A O    1 
ATOM   3209 C  CB   . GLU   A 1 444 ? 20.934  27.704  40.334 1.00 102.81 ?  471 GLU   A CB   1 
ATOM   3210 C  CG   . GLU   A 1 444 ? 20.221  28.804  41.114 1.00 116.85 ?  471 GLU   A CG   1 
ATOM   3211 C  CD   . GLU   A 1 444 ? 19.341  29.676  40.241 1.00 118.74 ?  471 GLU   A CD   1 
ATOM   3212 O  OE1  . GLU   A 1 444 ? 19.189  29.360  39.042 1.00 126.40 ?  471 GLU   A OE1  1 
ATOM   3213 O  OE2  . GLU   A 1 444 ? 18.798  30.678  40.755 1.00 115.05 ?  471 GLU   A OE2  1 
ATOM   3214 N  N    . CYS   A 1 445 ? 20.018  25.787  42.946 1.00 99.50  ?  472 CYS   A N    1 
ATOM   3215 C  CA   . CYS   A 1 445 ? 19.007  24.906  43.518 1.00 94.91  ?  472 CYS   A CA   1 
ATOM   3216 C  C    . CYS   A 1 445 ? 17.609  25.420  43.199 1.00 105.24 ?  472 CYS   A C    1 
ATOM   3217 O  O    . CYS   A 1 445 ? 16.752  25.503  44.083 1.00 116.54 ?  472 CYS   A O    1 
ATOM   3218 C  CB   . CYS   A 1 445 ? 19.214  24.772  45.027 1.00 95.65  ?  472 CYS   A CB   1 
ATOM   3219 S  SG   . CYS   A 1 445 ? 18.343  23.390  45.798 1.00 96.86  ?  472 CYS   A SG   1 
ATOM   3220 N  N    . ARG   A 1 446 ? 17.371  25.763  41.933 1.00 97.21  ?  473 ARG   A N    1 
ATOM   3221 C  CA   . ARG   A 1 446 ? 16.094  26.320  41.508 1.00 86.95  ?  473 ARG   A CA   1 
ATOM   3222 C  C    . ARG   A 1 446 ? 15.069  25.203  41.317 1.00 88.39  ?  473 ARG   A C    1 
ATOM   3223 O  O    . ARG   A 1 446 ? 15.385  24.164  40.731 1.00 85.63  ?  473 ARG   A O    1 
ATOM   3224 C  CB   . ARG   A 1 446 ? 16.261  27.100  40.205 1.00 88.39  ?  473 ARG   A CB   1 
ATOM   3225 C  CG   . ARG   A 1 446 ? 15.310  28.273  40.034 1.00 88.10  ?  473 ARG   A CG   1 
ATOM   3226 C  CD   . ARG   A 1 446 ? 15.867  29.276  39.039 1.00 94.22  ?  473 ARG   A CD   1 
ATOM   3227 N  NE   . ARG   A 1 446 ? 14.820  30.067  38.403 1.00 97.31  ?  473 ARG   A NE   1 
ATOM   3228 C  CZ   . ARG   A 1 446 ? 15.047  31.055  37.548 1.00 106.61 ?  473 ARG   A CZ   1 
ATOM   3229 N  NH1  . ARG   A 1 446 ? 16.276  31.402  37.203 1.00 101.08 ?  473 ARG   A NH1  1 
ATOM   3230 N  NH2  . ARG   A 1 446 ? 14.014  31.712  37.027 1.00 113.48 ?  473 ARG   A NH2  1 
ATOM   3231 N  N    . PRO   A 1 447 ? 13.834  25.385  41.807 1.00 86.67  ?  474 PRO   A N    1 
ATOM   3232 C  CA   . PRO   A 1 447 ? 13.405  26.570  42.555 1.00 93.51  ?  474 PRO   A CA   1 
ATOM   3233 C  C    . PRO   A 1 447 ? 13.623  26.427  44.059 1.00 97.18  ?  474 PRO   A C    1 
ATOM   3234 O  O    . PRO   A 1 447 ? 13.453  25.338  44.607 1.00 91.41  ?  474 PRO   A O    1 
ATOM   3235 C  CB   . PRO   A 1 447 ? 11.916  26.668  42.223 1.00 83.00  ?  474 PRO   A CB   1 
ATOM   3236 C  CG   . PRO   A 1 447 ? 11.497  25.258  41.929 1.00 78.36  ?  474 PRO   A CG   1 
ATOM   3237 C  CD   . PRO   A 1 447 ? 12.720  24.449  41.574 1.00 83.43  ?  474 PRO   A CD   1 
ATOM   3238 N  N    . TYR   A 1 448 ? 13.999  27.524  44.713 1.00 95.48  ?  475 TYR   A N    1 
ATOM   3239 C  CA   . TYR   A 1 448 ? 14.275  27.526  46.141 1.00 96.66  ?  475 TYR   A CA   1 
ATOM   3240 C  C    . TYR   A 1 448 ? 13.717  28.797  46.759 1.00 101.22 ?  475 TYR   A C    1 
ATOM   3241 O  O    . TYR   A 1 448 ? 13.814  29.878  46.171 1.00 96.33  ?  475 TYR   A O    1 
ATOM   3242 C  CB   . TYR   A 1 448 ? 15.780  27.421  46.419 1.00 104.95 ?  475 TYR   A CB   1 
ATOM   3243 C  CG   . TYR   A 1 448 ? 16.126  27.123  47.860 1.00 112.40 ?  475 TYR   A CG   1 
ATOM   3244 C  CD1  . TYR   A 1 448 ? 15.845  25.884  48.421 1.00 107.39 ?  475 TYR   A CD1  1 
ATOM   3245 C  CD2  . TYR   A 1 448 ? 16.743  28.078  48.657 1.00 108.39 ?  475 TYR   A CD2  1 
ATOM   3246 C  CE1  . TYR   A 1 448 ? 16.164  25.606  49.738 1.00 109.89 ?  475 TYR   A CE1  1 
ATOM   3247 C  CE2  . TYR   A 1 448 ? 17.065  27.810  49.974 1.00 110.53 ?  475 TYR   A CE2  1 
ATOM   3248 C  CZ   . TYR   A 1 448 ? 16.774  26.574  50.510 1.00 111.27 ?  475 TYR   A CZ   1 
ATOM   3249 O  OH   . TYR   A 1 448 ? 17.094  26.304  51.821 1.00 106.61 ?  475 TYR   A OH   1 
ATOM   3250 N  N    . TRP   A 1 449 ? 13.135  28.660  47.948 1.00 104.17 ?  476 TRP   A N    1 
ATOM   3251 C  CA   . TRP   A 1 449 ? 12.528  29.788  48.636 1.00 106.60 ?  476 TRP   A CA   1 
ATOM   3252 C  C    . TRP   A 1 449 ? 12.615  29.565  50.137 1.00 110.40 ?  476 TRP   A C    1 
ATOM   3253 O  O    . TRP   A 1 449 ? 12.662  28.427  50.610 1.00 109.04 ?  476 TRP   A O    1 
ATOM   3254 C  CB   . TRP   A 1 449 ? 11.069  29.986  48.210 1.00 107.48 ?  476 TRP   A CB   1 
ATOM   3255 C  CG   . TRP   A 1 449 ? 10.156  28.884  48.655 1.00 108.73 ?  476 TRP   A CG   1 
ATOM   3256 C  CD1  . TRP   A 1 449 ? 9.341   28.883  49.750 1.00 109.14 ?  476 TRP   A CD1  1 
ATOM   3257 C  CD2  . TRP   A 1 449 ? 9.967   27.617  48.013 1.00 103.15 ?  476 TRP   A CD2  1 
ATOM   3258 N  NE1  . TRP   A 1 449 ? 8.654   27.695  49.828 1.00 97.76  ?  476 TRP   A NE1  1 
ATOM   3259 C  CE2  . TRP   A 1 449 ? 9.021   26.901  48.773 1.00 96.24  ?  476 TRP   A CE2  1 
ATOM   3260 C  CE3  . TRP   A 1 449 ? 10.504  27.020  46.869 1.00 96.34  ?  476 TRP   A CE3  1 
ATOM   3261 C  CZ2  . TRP   A 1 449 ? 8.600   25.619  48.424 1.00 96.07  ?  476 TRP   A CZ2  1 
ATOM   3262 C  CZ3  . TRP   A 1 449 ? 10.087  25.747  46.526 1.00 94.70  ?  476 TRP   A CZ3  1 
ATOM   3263 C  CH2  . TRP   A 1 449 ? 9.145   25.060  47.302 1.00 88.94  ?  476 TRP   A CH2  1 
ATOM   3264 N  N    . GLU   A 1 450 ? 12.635  30.666  50.877 1.00 111.80 ?  477 GLU   A N    1 
ATOM   3265 C  CA   . GLU   A 1 450 ? 12.719  30.620  52.326 1.00 116.92 ?  477 GLU   A CA   1 
ATOM   3266 C  C    . GLU   A 1 450 ? 11.323  30.580  52.938 1.00 112.04 ?  477 GLU   A C    1 
ATOM   3267 O  O    . GLU   A 1 450 ? 10.320  30.869  52.282 1.00 118.20 ?  477 GLU   A O    1 
ATOM   3268 C  CB   . GLU   A 1 450 ? 13.485  31.835  52.858 1.00 115.50 ?  477 GLU   A CB   1 
ATOM   3269 C  CG   . GLU   A 1 450 ? 14.943  31.903  52.425 1.00 108.20 ?  477 GLU   A CG   1 
ATOM   3270 C  CD   . GLU   A 1 450 ? 15.783  30.763  52.972 1.00 121.83 ?  477 GLU   A CD   1 
ATOM   3271 O  OE1  . GLU   A 1 450 ? 15.358  30.116  53.952 1.00 117.28 ?  477 GLU   A OE1  1 
ATOM   3272 O  OE2  . GLU   A 1 450 ? 16.873  30.511  52.415 1.00 123.09 ?  477 GLU   A OE2  1 
ATOM   3273 N  N    . LYS   A 1 451 ? 11.272  30.212  54.221 1.00 112.80 ?  478 LYS   A N    1 
ATOM   3274 C  CA   . LYS   A 1 451 ? 10.035  30.347  54.981 1.00 128.55 ?  478 LYS   A CA   1 
ATOM   3275 C  C    . LYS   A 1 451 ? 9.554   31.791  55.004 1.00 135.64 ?  478 LYS   A C    1 
ATOM   3276 O  O    . LYS   A 1 451 ? 8.354   32.037  55.181 1.00 125.96 ?  478 LYS   A O    1 
ATOM   3277 C  CB   . LYS   A 1 451 ? 10.239  29.834  56.408 1.00 134.43 ?  478 LYS   A CB   1 
ATOM   3278 C  CG   . LYS   A 1 451 ? 11.042  28.543  56.491 1.00 141.93 ?  478 LYS   A CG   1 
ATOM   3279 C  CD   . LYS   A 1 451 ? 10.564  27.650  57.625 1.00 143.17 ?  478 LYS   A CD   1 
ATOM   3280 C  CE   . LYS   A 1 451 ? 11.252  26.295  57.579 1.00 145.21 ?  478 LYS   A CE   1 
ATOM   3281 N  NZ   . LYS   A 1 451 ? 10.279  25.167  57.576 1.00 136.64 ?  478 LYS   A NZ   1 
ATOM   3282 N  N    . ASP   A 1 452 ? 10.475  32.744  54.833 1.00 145.73 ?  479 ASP   A N    1 
ATOM   3283 C  CA   . ASP   A 1 452 ? 10.113  34.148  54.675 1.00 153.98 ?  479 ASP   A CA   1 
ATOM   3284 C  C    . ASP   A 1 452 ? 9.180   34.333  53.481 1.00 149.37 ?  479 ASP   A C    1 
ATOM   3285 O  O    . ASP   A 1 452 ? 8.150   35.009  53.584 1.00 135.80 ?  479 ASP   A O    1 
ATOM   3286 C  CB   . ASP   A 1 452 ? 11.405  34.966  54.521 1.00 152.85 ?  479 ASP   A CB   1 
ATOM   3287 C  CG   . ASP   A 1 452 ? 11.200  36.370  53.936 1.00 163.83 ?  479 ASP   A CG   1 
ATOM   3288 O  OD1  . ASP   A 1 452 ? 10.062  36.876  53.830 1.00 161.72 ?  479 ASP   A OD1  1 
ATOM   3289 O  OD2  . ASP   A 1 452 ? 12.227  37.014  53.639 1.00 170.11 ?  479 ASP   A OD2  1 
ATOM   3290 N  N    . ASP   A 1 453 ? 9.518   33.717  52.348 1.00 138.85 ?  480 ASP   A N    1 
ATOM   3291 C  CA   . ASP   A 1 453 ? 8.836   33.989  51.086 1.00 131.44 ?  480 ASP   A CA   1 
ATOM   3292 C  C    . ASP   A 1 453 ? 7.336   33.750  51.207 1.00 126.60 ?  480 ASP   A C    1 
ATOM   3293 O  O    . ASP   A 1 453 ? 6.890   32.621  51.431 1.00 120.49 ?  480 ASP   A O    1 
ATOM   3294 C  CB   . ASP   A 1 453 ? 9.427   33.120  49.977 1.00 122.81 ?  480 ASP   A CB   1 
ATOM   3295 C  CG   . ASP   A 1 453 ? 9.185   33.698  48.594 1.00 121.64 ?  480 ASP   A CG   1 
ATOM   3296 O  OD1  . ASP   A 1 453 ? 8.037   34.087  48.298 1.00 118.17 ?  480 ASP   A OD1  1 
ATOM   3297 O  OD2  . ASP   A 1 453 ? 10.150  33.765  47.803 1.00 122.69 ?  480 ASP   A OD2  1 
ATOM   3298 N  N    . ALA   A 1 454 ? 6.561   34.823  51.052 1.00 127.03 ?  481 ALA   A N    1 
ATOM   3299 C  CA   . ALA   A 1 454 ? 5.109   34.755  51.111 1.00 115.22 ?  481 ALA   A CA   1 
ATOM   3300 C  C    . ALA   A 1 454 ? 4.466   34.523  49.751 1.00 116.00 ?  481 ALA   A C    1 
ATOM   3301 O  O    . ALA   A 1 454 ? 3.268   34.227  49.694 1.00 121.34 ?  481 ALA   A O    1 
ATOM   3302 C  CB   . ALA   A 1 454 ? 4.544   36.038  51.728 1.00 109.11 ?  481 ALA   A CB   1 
ATOM   3303 N  N    . SER   A 1 455 ? 5.223   34.659  48.658 1.00 110.77 ?  482 SER   A N    1 
ATOM   3304 C  CA   . SER   A 1 455 ? 4.670   34.365  47.341 1.00 109.26 ?  482 SER   A CA   1 
ATOM   3305 C  C    . SER   A 1 455 ? 4.450   32.870  47.152 1.00 101.75 ?  482 SER   A C    1 
ATOM   3306 O  O    . SER   A 1 455 ? 3.570   32.466  46.382 1.00 95.18  ?  482 SER   A O    1 
ATOM   3307 C  CB   . SER   A 1 455 ? 5.589   34.911  46.247 1.00 105.00 ?  482 SER   A CB   1 
ATOM   3308 O  OG   . SER   A 1 455 ? 6.839   34.245  46.250 1.00 111.25 ?  482 SER   A OG   1 
ATOM   3309 N  N    . MET   A 1 456 ? 5.236   32.041  47.838 1.00 109.57 ?  483 MET   A N    1 
ATOM   3310 C  CA   . MET   A 1 456 ? 5.030   30.600  47.819 1.00 98.65  ?  483 MET   A CA   1 
ATOM   3311 C  C    . MET   A 1 456 ? 3.950   30.216  48.831 1.00 100.43 ?  483 MET   A C    1 
ATOM   3312 O  O    . MET   A 1 456 ? 3.965   30.697  49.967 1.00 98.24  ?  483 MET   A O    1 
ATOM   3313 C  CB   . MET   A 1 456 ? 6.324   29.861  48.151 1.00 96.40  ?  483 MET   A CB   1 
ATOM   3314 C  CG   . MET   A 1 456 ? 7.292   29.609  46.990 1.00 101.38 ?  483 MET   A CG   1 
ATOM   3315 S  SD   . MET   A 1 456 ? 6.593   29.417  45.337 1.00 104.44 ?  483 MET   A SD   1 
ATOM   3316 C  CE   . MET   A 1 456 ? 6.672   31.100  44.727 1.00 102.94 ?  483 MET   A CE   1 
ATOM   3317 N  N    . PRO   A 1 457 ? 3.004   29.353  48.449 1.00 88.01  ?  484 PRO   A N    1 
ATOM   3318 C  CA   . PRO   A 1 457 ? 1.971   28.922  49.401 1.00 91.88  ?  484 PRO   A CA   1 
ATOM   3319 C  C    . PRO   A 1 457 ? 2.404   27.787  50.314 1.00 93.42  ?  484 PRO   A C    1 
ATOM   3320 O  O    . PRO   A 1 457 ? 1.708   27.513  51.301 1.00 80.32  ?  484 PRO   A O    1 
ATOM   3321 C  CB   . PRO   A 1 457 ? 0.825   28.476  48.486 1.00 80.37  ?  484 PRO   A CB   1 
ATOM   3322 C  CG   . PRO   A 1 457 ? 1.512   27.990  47.254 1.00 85.68  ?  484 PRO   A CG   1 
ATOM   3323 C  CD   . PRO   A 1 457 ? 2.778   28.805  47.100 1.00 84.65  ?  484 PRO   A CD   1 
ATOM   3324 N  N    . LEU   A 1 458 ? 3.520   27.126  50.025 1.00 85.70  ?  485 LEU   A N    1 
ATOM   3325 C  CA   . LEU   A 1 458 ? 3.979   25.976  50.785 1.00 82.11  ?  485 LEU   A CA   1 
ATOM   3326 C  C    . LEU   A 1 458 ? 5.478   26.096  51.011 1.00 89.19  ?  485 LEU   A C    1 
ATOM   3327 O  O    . LEU   A 1 458 ? 6.197   26.622  50.153 1.00 94.82  ?  485 LEU   A O    1 
ATOM   3328 C  CB   . LEU   A 1 458 ? 3.664   24.662  50.051 1.00 91.52  ?  485 LEU   A CB   1 
ATOM   3329 C  CG   . LEU   A 1 458 ? 2.219   24.164  50.158 1.00 83.13  ?  485 LEU   A CG   1 
ATOM   3330 C  CD1  . LEU   A 1 458 ? 2.010   22.922  49.304 1.00 76.17  ?  485 LEU   A CD1  1 
ATOM   3331 C  CD2  . LEU   A 1 458 ? 1.846   23.892  51.607 1.00 72.65  ?  485 LEU   A CD2  1 
ATOM   3332 N  N    . PRO   A 1 459 ? 5.976   25.623  52.151 1.00 92.11  ?  486 PRO   A N    1 
ATOM   3333 C  CA   . PRO   A 1 459 ? 7.413   25.722  52.426 1.00 87.28  ?  486 PRO   A CA   1 
ATOM   3334 C  C    . PRO   A 1 459 ? 8.206   24.741  51.576 1.00 86.43  ?  486 PRO   A C    1 
ATOM   3335 O  O    . PRO   A 1 459 ? 7.658   23.874  50.893 1.00 85.92  ?  486 PRO   A O    1 
ATOM   3336 C  CB   . PRO   A 1 459 ? 7.512   25.382  53.915 1.00 82.33  ?  486 PRO   A CB   1 
ATOM   3337 C  CG   . PRO   A 1 459 ? 6.351   24.478  54.160 1.00 88.12  ?  486 PRO   A CG   1 
ATOM   3338 C  CD   . PRO   A 1 459 ? 5.250   24.933  53.232 1.00 86.99  ?  486 PRO   A CD   1 
ATOM   3339 N  N    . PHE   A 1 460 ? 9.530   24.898  51.619 1.00 92.92  ?  487 PHE   A N    1 
ATOM   3340 C  CA   . PHE   A 1 460 ? 10.400  23.970  50.905 1.00 86.20  ?  487 PHE   A CA   1 
ATOM   3341 C  C    . PHE   A 1 460 ? 10.590  22.679  51.691 1.00 94.87  ?  487 PHE   A C    1 
ATOM   3342 O  O    . PHE   A 1 460 ? 10.644  21.593  51.103 1.00 85.15  ?  487 PHE   A O    1 
ATOM   3343 C  CB   . PHE   A 1 460 ? 11.749  24.629  50.610 1.00 89.15  ?  487 PHE   A CB   1 
ATOM   3344 C  CG   . PHE   A 1 460 ? 12.708  23.744  49.860 1.00 94.09  ?  487 PHE   A CG   1 
ATOM   3345 C  CD1  . PHE   A 1 460 ? 12.712  23.725  48.475 1.00 91.93  ?  487 PHE   A CD1  1 
ATOM   3346 C  CD2  . PHE   A 1 460 ? 13.598  22.925  50.538 1.00 90.74  ?  487 PHE   A CD2  1 
ATOM   3347 C  CE1  . PHE   A 1 460 ? 13.588  22.910  47.781 1.00 81.29  ?  487 PHE   A CE1  1 
ATOM   3348 C  CE2  . PHE   A 1 460 ? 14.476  22.109  49.850 1.00 92.09  ?  487 PHE   A CE2  1 
ATOM   3349 C  CZ   . PHE   A 1 460 ? 14.471  22.102  48.469 1.00 88.51  ?  487 PHE   A CZ   1 
ATOM   3350 N  N    . ASP   A 1 461 ? 10.694  22.778  53.013 1.00 89.48  ?  488 ASP   A N    1 
ATOM   3351 C  CA   . ASP   A 1 461 ? 10.818  21.611  53.874 1.00 91.25  ?  488 ASP   A CA   1 
ATOM   3352 C  C    . ASP   A 1 461 ? 9.422   21.091  54.198 1.00 97.26  ?  488 ASP   A C    1 
ATOM   3353 O  O    . ASP   A 1 461 ? 8.623   21.791  54.830 1.00 101.26 ?  488 ASP   A O    1 
ATOM   3354 C  CB   . ASP   A 1 461 ? 11.579  21.962  55.152 1.00 98.16  ?  488 ASP   A CB   1 
ATOM   3355 C  CG   . ASP   A 1 461 ? 12.119  20.737  55.867 1.00 102.46 ?  488 ASP   A CG   1 
ATOM   3356 O  OD1  . ASP   A 1 461 ? 11.607  19.624  55.623 1.00 99.05  ?  488 ASP   A OD1  1 
ATOM   3357 O  OD2  . ASP   A 1 461 ? 13.060  20.888  56.675 1.00 119.33 ?  488 ASP   A OD2  1 
ATOM   3358 N  N    . LEU   A 1 462 ? 9.132   19.866  53.765 1.00 99.22  ?  489 LEU   A N    1 
ATOM   3359 C  CA   . LEU   A 1 462 ? 7.817   19.259  53.930 1.00 99.94  ?  489 LEU   A CA   1 
ATOM   3360 C  C    . LEU   A 1 462 ? 7.770   18.244  55.065 1.00 108.77 ?  489 LEU   A C    1 
ATOM   3361 O  O    . LEU   A 1 462 ? 6.812   17.470  55.148 1.00 100.02 ?  489 LEU   A O    1 
ATOM   3362 C  CB   . LEU   A 1 462 ? 7.373   18.590  52.623 1.00 89.18  ?  489 LEU   A CB   1 
ATOM   3363 C  CG   . LEU   A 1 462 ? 6.789   19.407  51.463 1.00 86.23  ?  489 LEU   A CG   1 
ATOM   3364 C  CD1  . LEU   A 1 462 ? 7.426   20.777  51.327 1.00 99.84  ?  489 LEU   A CD1  1 
ATOM   3365 C  CD2  . LEU   A 1 462 ? 6.925   18.629  50.161 1.00 73.33  ?  489 LEU   A CD2  1 
ATOM   3366 N  N    . THR   A 1 463 ? 8.777   18.233  55.942 1.00 110.15 ?  490 THR   A N    1 
ATOM   3367 C  CA   . THR   A 1 463 ? 8.846   17.209  56.980 1.00 112.98 ?  490 THR   A CA   1 
ATOM   3368 C  C    . THR   A 1 463 ? 7.690   17.333  57.966 1.00 114.88 ?  490 THR   A C    1 
ATOM   3369 O  O    . THR   A 1 463 ? 7.101   16.323  58.371 1.00 113.00 ?  490 THR   A O    1 
ATOM   3370 C  CB   . THR   A 1 463 ? 10.185  17.296  57.711 1.00 130.50 ?  490 THR   A CB   1 
ATOM   3371 O  OG1  . THR   A 1 463 ? 11.255  17.143  56.768 1.00 125.37 ?  490 THR   A OG1  1 
ATOM   3372 C  CG2  . THR   A 1 463 ? 10.289  16.207  58.767 1.00 124.77 ?  490 THR   A CG2  1 
ATOM   3373 N  N    . ASP   A 1 464 ? 7.349   18.563  58.364 1.00 113.10 ?  491 ASP   A N    1 
ATOM   3374 C  CA   . ASP   A 1 464 ? 6.242   18.756  59.294 1.00 118.21 ?  491 ASP   A CA   1 
ATOM   3375 C  C    . ASP   A 1 464 ? 4.912   18.359  58.678 1.00 112.11 ?  491 ASP   A C    1 
ATOM   3376 O  O    . ASP   A 1 464 ? 4.035   17.841  59.377 1.00 107.52 ?  491 ASP   A O    1 
ATOM   3377 C  CB   . ASP   A 1 464 ? 6.181   20.209  59.755 1.00 112.88 ?  491 ASP   A CB   1 
ATOM   3378 C  CG   . ASP   A 1 464 ? 7.393   20.611  60.548 1.00 117.73 ?  491 ASP   A CG   1 
ATOM   3379 O  OD1  . ASP   A 1 464 ? 7.995   19.731  61.201 1.00 118.95 ?  491 ASP   A OD1  1 
ATOM   3380 O  OD2  . ASP   A 1 464 ? 7.744   21.808  60.519 1.00 128.56 ?  491 ASP   A OD2  1 
ATOM   3381 N  N    . ILE   A 1 465 ? 4.735   18.600  57.384 1.00 104.14 ?  492 ILE   A N    1 
ATOM   3382 C  CA   . ILE   A 1 465 ? 3.499   18.185  56.743 1.00 106.70 ?  492 ILE   A CA   1 
ATOM   3383 C  C    . ILE   A 1 465 ? 3.447   16.664  56.624 1.00 105.95 ?  492 ILE   A C    1 
ATOM   3384 O  O    . ILE   A 1 465 ? 2.538   16.028  57.164 1.00 104.19 ?  492 ILE   A O    1 
ATOM   3385 C  CB   . ILE   A 1 465 ? 3.356   18.908  55.390 1.00 105.03 ?  492 ILE   A CB   1 
ATOM   3386 C  CG1  . ILE   A 1 465 ? 3.272   20.416  55.654 1.00 102.17 ?  492 ILE   A CG1  1 
ATOM   3387 C  CG2  . ILE   A 1 465 ? 2.119   18.471  54.661 1.00 104.13 ?  492 ILE   A CG2  1 
ATOM   3388 C  CD1  . ILE   A 1 465 ? 2.782   21.250  54.480 1.00 92.97  ?  492 ILE   A CD1  1 
ATOM   3389 N  N    . VAL   A 1 466 ? 4.456   16.052  55.988 1.00 100.41 ?  493 VAL   A N    1 
ATOM   3390 C  CA   . VAL   A 1 466 ? 4.447   14.604  55.759 1.00 100.04 ?  493 VAL   A CA   1 
ATOM   3391 C  C    . VAL   A 1 466 ? 4.232   13.845  57.064 1.00 104.88 ?  493 VAL   A C    1 
ATOM   3392 O  O    . VAL   A 1 466 ? 3.446   12.892  57.118 1.00 103.38 ?  493 VAL   A O    1 
ATOM   3393 C  CB   . VAL   A 1 466 ? 5.744   14.155  55.051 1.00 101.65 ?  493 VAL   A CB   1 
ATOM   3394 C  CG1  . VAL   A 1 466 ? 5.800   12.632  54.941 1.00 92.69  ?  493 VAL   A CG1  1 
ATOM   3395 C  CG2  . VAL   A 1 466 ? 5.860   14.778  53.667 1.00 85.72  ?  493 VAL   A CG2  1 
ATOM   3396 N  N    . SER   A 1 467 ? 4.917   14.255  58.137 1.00 103.42 ?  494 SER   A N    1 
ATOM   3397 C  CA   . SER   A 1 467 ? 4.759   13.564  59.413 1.00 109.12 ?  494 SER   A CA   1 
ATOM   3398 C  C    . SER   A 1 467 ? 3.355   13.733  59.980 1.00 110.00 ?  494 SER   A C    1 
ATOM   3399 O  O    . SER   A 1 467 ? 2.843   12.821  60.639 1.00 108.26 ?  494 SER   A O    1 
ATOM   3400 C  CB   . SER   A 1 467 ? 5.791   14.067  60.421 1.00 115.47 ?  494 SER   A CB   1 
ATOM   3401 O  OG   . SER   A 1 467 ? 5.670   15.465  60.620 1.00 120.87 ?  494 SER   A OG   1 
ATOM   3402 N  N    . GLU   A 1 468 ? 2.722   14.885  59.742 1.00 107.57 ?  495 GLU   A N    1 
ATOM   3403 C  CA   . GLU   A 1 468 ? 1.357   15.089  60.218 1.00 103.74 ?  495 GLU   A CA   1 
ATOM   3404 C  C    . GLU   A 1 468 ? 0.376   14.156  59.512 1.00 110.03 ?  495 GLU   A C    1 
ATOM   3405 O  O    . GLU   A 1 468 ? -0.469  13.527  60.158 1.00 111.50 ?  495 GLU   A O    1 
ATOM   3406 C  CB   . GLU   A 1 468 ? 0.940   16.548  60.026 1.00 101.31 ?  495 GLU   A CB   1 
ATOM   3407 C  CG   . GLU   A 1 468 ? -0.566  16.760  60.060 1.00 107.20 ?  495 GLU   A CG   1 
ATOM   3408 C  CD   . GLU   A 1 468 ? -0.961  18.054  60.742 1.00 122.15 ?  495 GLU   A CD   1 
ATOM   3409 O  OE1  . GLU   A 1 468 ? -0.092  18.938  60.880 1.00 133.97 ?  495 GLU   A OE1  1 
ATOM   3410 O  OE2  . GLU   A 1 468 ? -2.140  18.186  61.136 1.00 116.63 ?  495 GLU   A OE2  1 
ATOM   3411 N  N    . LEU   A 1 469 ? 0.463   14.056  58.183 1.00 106.96 ?  496 LEU   A N    1 
ATOM   3412 C  CA   . LEU   A 1 469 ? -0.465  13.191  57.455 1.00 108.88 ?  496 LEU   A CA   1 
ATOM   3413 C  C    . LEU   A 1 469 ? -0.332  11.729  57.880 1.00 112.55 ?  496 LEU   A C    1 
ATOM   3414 O  O    . LEU   A 1 469 ? -1.326  10.992  57.908 1.00 116.14 ?  496 LEU   A O    1 
ATOM   3415 C  CB   . LEU   A 1 469 ? -0.271  13.348  55.943 1.00 104.76 ?  496 LEU   A CB   1 
ATOM   3416 C  CG   . LEU   A 1 469 ? -0.814  14.591  55.227 1.00 106.12 ?  496 LEU   A CG   1 
ATOM   3417 C  CD1  . LEU   A 1 469 ? -2.282  14.779  55.646 1.00 103.01 ?  496 LEU   A CD1  1 
ATOM   3418 C  CD2  . LEU   A 1 469 ? 0.025   15.855  55.428 1.00 109.22 ?  496 LEU   A CD2  1 
ATOM   3419 N  N    . ARG   A 1 470 ? 0.878   11.293  58.234 1.00 108.15 ?  497 ARG   A N    1 
ATOM   3420 C  CA   . ARG   A 1 470 ? 1.022   9.962   58.813 1.00 112.78 ?  497 ARG   A CA   1 
ATOM   3421 C  C    . ARG   A 1 470 ? 0.357   9.891   60.181 1.00 119.78 ?  497 ARG   A C    1 
ATOM   3422 O  O    . ARG   A 1 470 ? -0.294  8.893   60.509 1.00 126.95 ?  497 ARG   A O    1 
ATOM   3423 C  CB   . ARG   A 1 470 ? 2.497   9.579   58.910 1.00 113.83 ?  497 ARG   A CB   1 
ATOM   3424 C  CG   . ARG   A 1 470 ? 2.841   8.261   58.230 1.00 114.03 ?  497 ARG   A CG   1 
ATOM   3425 C  CD   . ARG   A 1 470 ? 4.332   7.979   58.299 1.00 119.50 ?  497 ARG   A CD   1 
ATOM   3426 N  NE   . ARG   A 1 470 ? 4.982   8.181   57.010 1.00 113.33 ?  497 ARG   A NE   1 
ATOM   3427 C  CZ   . ARG   A 1 470 ? 5.968   9.041   56.791 1.00 119.85 ?  497 ARG   A CZ   1 
ATOM   3428 N  NH1  . ARG   A 1 470 ? 6.452   9.799   57.762 1.00 115.63 ?  497 ARG   A NH1  1 
ATOM   3429 N  NH2  . ARG   A 1 470 ? 6.483   9.141   55.569 1.00 112.53 ?  497 ARG   A NH2  1 
ATOM   3430 N  N    . GLY   A 1 471 ? 0.507   10.944  60.989 1.00 120.14 ?  498 GLY   A N    1 
ATOM   3431 C  CA   . GLY   A 1 471 ? -0.152  10.977  62.282 1.00 125.76 ?  498 GLY   A CA   1 
ATOM   3432 C  C    . GLY   A 1 471 ? -1.664  10.987  62.178 1.00 130.73 ?  498 GLY   A C    1 
ATOM   3433 O  O    . GLY   A 1 471 ? -2.354  10.459  63.054 1.00 139.92 ?  498 GLY   A O    1 
ATOM   3434 N  N    . GLN   A 1 472 ? -2.200  11.587  61.113 1.00 125.88 ?  499 GLN   A N    1 
ATOM   3435 C  CA   . GLN   A 1 472 ? -3.639  11.545  60.880 1.00 127.51 ?  499 GLN   A CA   1 
ATOM   3436 C  C    . GLN   A 1 472 ? -4.110  10.156  60.473 1.00 128.32 ?  499 GLN   A C    1 
ATOM   3437 O  O    . GLN   A 1 472 ? -5.306  9.865   60.571 1.00 133.37 ?  499 GLN   A O    1 
ATOM   3438 C  CB   . GLN   A 1 472 ? -4.030  12.567  59.811 1.00 123.42 ?  499 GLN   A CB   1 
ATOM   3439 C  CG   . GLN   A 1 472 ? -3.573  13.985  60.116 1.00 122.99 ?  499 GLN   A CG   1 
ATOM   3440 C  CD   . GLN   A 1 472 ? -4.576  15.034  59.682 1.00 129.23 ?  499 GLN   A CD   1 
ATOM   3441 O  OE1  . GLN   A 1 472 ? -5.596  14.719  59.069 1.00 137.92 ?  499 GLN   A OE1  1 
ATOM   3442 N  NE2  . GLN   A 1 472 ? -4.289  16.293  59.997 1.00 130.77 ?  499 GLN   A NE2  1 
ATOM   3443 N  N    . LEU   A 1 473 ? -3.198  9.297   60.017 1.00 125.43 ?  500 LEU   A N    1 
ATOM   3444 C  CA   . LEU   A 1 473 ? -3.541  7.916   59.705 1.00 125.37 ?  500 LEU   A CA   1 
ATOM   3445 C  C    . LEU   A 1 473 ? -3.577  7.048   60.958 1.00 135.03 ?  500 LEU   A C    1 
ATOM   3446 O  O    . LEU   A 1 473 ? -4.238  6.004   60.959 1.00 138.95 ?  500 LEU   A O    1 
ATOM   3447 C  CB   . LEU   A 1 473 ? -2.544  7.367   58.675 1.00 129.60 ?  500 LEU   A CB   1 
ATOM   3448 C  CG   . LEU   A 1 473 ? -2.841  6.175   57.749 1.00 136.72 ?  500 LEU   A CG   1 
ATOM   3449 C  CD1  . LEU   A 1 473 ? -2.989  4.843   58.474 1.00 145.23 ?  500 LEU   A CD1  1 
ATOM   3450 C  CD2  . LEU   A 1 473 ? -4.079  6.464   56.910 1.00 118.27 ?  500 LEU   A CD2  1 
ATOM   3451 N  N    . LEU   A 1 474 ? -2.904  7.472   62.031 1.00 139.89 ?  501 LEU   A N    1 
ATOM   3452 C  CA   . LEU   A 1 474 ? -2.967  6.743   63.294 1.00 141.24 ?  501 LEU   A CA   1 
ATOM   3453 C  C    . LEU   A 1 474 ? -4.378  6.771   63.872 1.00 139.08 ?  501 LEU   A C    1 
ATOM   3454 O  O    . LEU   A 1 474 ? -5.016  5.725   64.042 1.00 136.47 ?  501 LEU   A O    1 
ATOM   3455 C  CB   . LEU   A 1 474 ? -1.957  7.330   64.287 1.00 136.46 ?  501 LEU   A CB   1 
ATOM   3456 C  CG   . LEU   A 1 474 ? -2.209  7.134   65.786 1.00 144.51 ?  501 LEU   A CG   1 
ATOM   3457 C  CD1  . LEU   A 1 474 ? -2.040  5.675   66.189 1.00 141.66 ?  501 LEU   A CD1  1 
ATOM   3458 C  CD2  . LEU   A 1 474 ? -1.295  8.032   66.609 1.00 139.65 ?  501 LEU   A CD2  1 
ATOM   3459 N  N    . GLU   A 1 475 ? -4.886  7.963   64.173 1.00 130.68 ?  502 GLU   A N    1 
ATOM   3460 C  CA   . GLU   A 1 475 ? -6.217  8.103   64.752 1.00 134.72 ?  502 GLU   A CA   1 
ATOM   3461 C  C    . GLU   A 1 475 ? -7.018  9.177   64.025 1.00 137.13 ?  502 GLU   A C    1 
ATOM   3462 O  O    . GLU   A 1 475 ? -6.932  9.308   62.804 1.00 123.33 ?  502 GLU   A O    1 
ATOM   3463 C  CB   . GLU   A 1 475 ? -6.122  8.433   66.243 1.00 125.99 ?  502 GLU   A CB   1 
HETATM 3464 C  C1   . AKG   B 2 .   ? 30.736  8.072   24.893 1.00 104.71 ?  601 AKG   A C1   1 
HETATM 3465 O  O1   . AKG   B 2 .   ? 29.748  8.616   24.418 1.00 99.50  ?  601 AKG   A O1   1 
HETATM 3466 O  O2   . AKG   B 2 .   ? 31.622  8.674   25.643 1.00 101.76 ?  601 AKG   A O2   1 
HETATM 3467 C  C2   . AKG   B 2 .   ? 31.019  6.582   24.634 1.00 90.64  ?  601 AKG   A C2   1 
HETATM 3468 O  O5   . AKG   B 2 .   ? 30.272  5.728   25.096 1.00 82.52  ?  601 AKG   A O5   1 
HETATM 3469 C  C3   . AKG   B 2 .   ? 32.222  6.237   23.798 1.00 87.82  ?  601 AKG   A C3   1 
HETATM 3470 C  C4   . AKG   B 2 .   ? 32.230  6.946   22.456 1.00 86.54  ?  601 AKG   A C4   1 
HETATM 3471 C  C5   . AKG   B 2 .   ? 33.518  7.661   22.166 1.00 94.06  ?  601 AKG   A C5   1 
HETATM 3472 O  O3   . AKG   B 2 .   ? 33.766  8.777   22.575 1.00 87.37  ?  601 AKG   A O3   1 
HETATM 3473 O  O4   . AKG   B 2 .   ? 34.341  6.966   21.425 1.00 95.58  ?  601 AKG   A O4   1 
HETATM 3474 N  N3   . A1EF5 C 3 .   ? 25.617  6.481   28.664 1.00 75.01  ?  602 A1EF5 A N3   1 
HETATM 3475 C  C5   . A1EF5 C 3 .   ? 27.413  7.738   28.149 1.00 89.49  ?  602 A1EF5 A C5   1 
HETATM 3476 C  C6   . A1EF5 C 3 .   ? 28.231  8.674   27.318 1.00 95.62  ?  602 A1EF5 A C6   1 
HETATM 3477 C  C7   . A1EF5 C 3 .   ? 27.669  7.119   29.366 1.00 83.37  ?  602 A1EF5 A C7   1 
HETATM 3478 C  C8   . A1EF5 C 3 .   ? 28.851  7.347   30.237 1.00 86.68  ?  602 A1EF5 A C8   1 
HETATM 3479 C  C10  . A1EF5 C 3 .   ? 30.698  6.492   31.511 1.00 90.67  ?  602 A1EF5 A C10  1 
HETATM 3480 C  C15  . A1EF5 C 3 .   ? 31.546  9.379   34.464 1.00 109.88 ?  602 A1EF5 A C15  1 
HETATM 3481 C  C22  . A1EF5 C 3 .   ? 30.394  8.847   31.303 1.00 112.04 ?  602 A1EF5 A C22  1 
HETATM 3482 C  C24  . A1EF5 C 3 .   ? 29.268  8.642   30.530 1.00 96.05  ?  602 A1EF5 A C24  1 
HETATM 3483 C  C1   . A1EF5 C 3 .   ? 26.229  5.462   30.817 1.00 76.28  ?  602 A1EF5 A C1   1 
HETATM 3484 C  C12  . A1EF5 C 3 .   ? 31.143  7.783   31.816 1.00 108.61 ?  602 A1EF5 A C12  1 
HETATM 3485 C  C14  . A1EF5 C 3 .   ? 32.491  8.538   33.801 1.00 112.76 ?  602 A1EF5 A C14  1 
HETATM 3486 C  C16  . A1EF5 C 3 .   ? 32.004  9.774   35.688 1.00 106.93 ?  602 A1EF5 A C16  1 
HETATM 3487 C  C18  . A1EF5 C 3 .   ? 33.638  8.319   34.543 1.00 126.07 ?  602 A1EF5 A C18  1 
HETATM 3488 C  C19  . A1EF5 C 3 .   ? 34.818  7.480   34.146 1.00 116.58 ?  602 A1EF5 A C19  1 
HETATM 3489 C  C2   . A1EF5 C 3 .   ? 26.511  6.342   29.643 1.00 79.27  ?  602 A1EF5 A C2   1 
HETATM 3490 C  C9   . A1EF5 C 3 .   ? 29.576  6.271   30.737 1.00 87.42  ?  602 A1EF5 A C9   1 
HETATM 3491 N  N13  . A1EF5 C 3 .   ? 32.349  8.000   32.548 1.00 110.12 ?  602 A1EF5 A N13  1 
HETATM 3492 N  N4   . A1EF5 C 3 .   ? 26.189  7.335   27.769 1.00 87.23  ?  602 A1EF5 A N4   1 
HETATM 3493 O  O20  . A1EF5 C 3 .   ? 34.666  6.701   33.181 1.00 94.52  ?  602 A1EF5 A O20  1 
HETATM 3494 O  O21  . A1EF5 C 3 .   ? 35.878  7.613   34.810 1.00 113.22 -1 602 A1EF5 A O21  1 
HETATM 3495 S  S17  . A1EF5 C 3 .   ? 33.560  9.145   36.055 1.00 116.03 ?  602 A1EF5 A S17  1 
HETATM 3496 CL CL11 . A1EF5 C 3 .   ? 31.574  5.125   32.118 1.00 101.58 ?  602 A1EF5 A CL11 1 
HETATM 3497 CL CL23 . A1EF5 C 3 .   ? 30.899  10.476  31.619 1.00 151.96 ?  602 A1EF5 A CL23 1 
HETATM 3498 O  O    . HOH   D 4 .   ? 20.872  4.375   19.867 1.00 68.44  ?  701 HOH   A O    1 
HETATM 3499 O  O    . HOH   D 4 .   ? 44.142  8.133   17.981 1.00 71.94  ?  702 HOH   A O    1 
HETATM 3500 O  O    . HOH   D 4 .   ? 6.156   22.748  48.632 1.00 77.06  ?  703 HOH   A O    1 
HETATM 3501 O  O    . HOH   D 4 .   ? 9.879   13.165  32.218 1.00 53.99  ?  704 HOH   A O    1 
HETATM 3502 O  O    . HOH   D 4 .   ? 0.388   19.415  42.491 1.00 77.64  ?  705 HOH   A O    1 
HETATM 3503 O  O    . HOH   D 4 .   ? 23.951  -1.442  19.481 1.00 69.01  ?  706 HOH   A O    1 
HETATM 3504 O  O    . HOH   D 4 .   ? -12.725 25.310  32.951 1.00 84.40  ?  707 HOH   A O    1 
HETATM 3505 O  O    . HOH   D 4 .   ? 21.435  -0.340  21.527 1.00 65.13  ?  708 HOH   A O    1 
HETATM 3506 O  O    . HOH   D 4 .   ? 18.682  21.851  40.960 1.00 73.20  ?  709 HOH   A O    1 
HETATM 3507 O  O    . HOH   D 4 .   ? -9.631  30.517  37.862 1.00 84.26  ?  710 HOH   A O    1 
HETATM 3508 O  O    . HOH   D 4 .   ? 12.248  9.312   27.914 1.00 53.27  ?  711 HOH   A O    1 
HETATM 3509 O  O    . HOH   D 4 .   ? 47.109  -14.526 25.844 1.00 87.85  ?  712 HOH   A O    1 
HETATM 3510 O  O    . HOH   D 4 .   ? 47.988  5.680   27.225 1.00 78.50  ?  713 HOH   A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N    . GLY   A 1   ? 1.2714 1.5769 1.7281 0.2819  -0.0095 0.1539  28  GLY   A N    
2    C  CA   . GLY   A 1   ? 1.2359 1.5096 1.7090 0.2608  -0.0031 0.1241  28  GLY   A CA   
3    C  C    . GLY   A 1   ? 1.3073 1.6182 1.7709 0.2419  -0.0160 0.0928  28  GLY   A C    
4    O  O    . GLY   A 1   ? 1.2895 1.6558 1.7448 0.2481  -0.0293 0.0922  28  GLY   A O    
5    N  N    . SER   A 2   ? 1.1366 1.4191 1.6033 0.2197  -0.0107 0.0657  29  SER   A N    
6    C  CA   . SER   A 2   ? 1.0338 1.3434 1.4934 0.2004  -0.0171 0.0378  29  SER   A CA   
7    C  C    . SER   A 2   ? 1.0485 1.3192 1.4880 0.1725  -0.0139 0.0169  29  SER   A C    
8    O  O    . SER   A 2   ? 1.1026 1.3348 1.5318 0.1672  -0.0111 0.0225  29  SER   A O    
9    C  CB   . SER   A 2   ? 1.1400 1.4690 1.6301 0.2130  -0.0106 0.0294  29  SER   A CB   
10   O  OG   . SER   A 2   ? 1.2488 1.5351 1.7615 0.2224  0.0041  0.0312  29  SER   A OG   
11   N  N    . HIS   A 3   ? 0.9588 1.2415 1.3934 0.1560  -0.0131 -0.0064 30  HIS   A N    
12   C  CA   . HIS   A 3   ? 0.9503 1.2028 1.3624 0.1335  -0.0095 -0.0242 30  HIS   A CA   
13   C  C    . HIS   A 3   ? 0.8668 1.1168 1.2895 0.1313  0.0012  -0.0438 30  HIS   A C    
14   O  O    . HIS   A 3   ? 0.8365 1.1113 1.2845 0.1437  0.0051  -0.0455 30  HIS   A O    
15   C  CB   . HIS   A 3   ? 0.8205 1.0891 1.2068 0.1137  -0.0170 -0.0302 30  HIS   A CB   
16   C  CG   . HIS   A 3   ? 0.7505 1.0641 1.1485 0.1087  -0.0179 -0.0408 30  HIS   A CG   
17   N  ND1  . HIS   A 3   ? 0.6737 1.0340 1.0899 0.1216  -0.0266 -0.0342 30  HIS   A ND1  
18   C  CD2  . HIS   A 3   ? 0.7173 1.0387 1.1138 0.0928  -0.0099 -0.0580 30  HIS   A CD2  
19   C  CE1  . HIS   A 3   ? 0.8544 1.2507 1.2840 0.1117  -0.0249 -0.0505 30  HIS   A CE1  
20   N  NE2  . HIS   A 3   ? 0.8285 1.1995 1.2474 0.0935  -0.0131 -0.0637 30  HIS   A NE2  
21   N  N    . MET   A 4   ? 0.8592 1.0822 1.2612 0.1174  0.0060  -0.0587 31  MET   A N    
22   C  CA   . MET   A 4   ? 0.7570 0.9761 1.1626 0.1174  0.0169  -0.0779 31  MET   A CA   
23   C  C    . MET   A 4   ? 0.7074 0.9285 1.0826 0.0998  0.0208  -0.0888 31  MET   A C    
24   O  O    . MET   A 4   ? 0.8683 1.0722 1.2164 0.0883  0.0164  -0.0863 31  MET   A O    
25   C  CB   . MET   A 4   ? 0.8053 0.9899 1.2188 0.1244  0.0213  -0.0876 31  MET   A CB   
26   C  CG   . MET   A 4   ? 0.7838 0.9593 1.2340 0.1427  0.0234  -0.0760 31  MET   A CG   
27   S  SD   . MET   A 4   ? 1.0549 1.2051 1.5339 0.1525  0.0356  -0.0999 31  MET   A SD   
28   C  CE   . MET   A 4   ? 1.0115 1.1207 1.5050 0.1531  0.0354  -0.0915 31  MET   A CE   
29   N  N    . THR   A 5   ? 0.6833 0.9250 1.0644 0.0994  0.0312  -0.0992 32  THR   A N    
30   C  CA   . THR   A 5   ? 0.7251 0.9691 1.0814 0.0863  0.0412  -0.1066 32  THR   A CA   
31   C  C    . THR   A 5   ? 0.8336 1.0780 1.1891 0.0951  0.0541  -0.1221 32  THR   A C    
32   O  O    . THR   A 5   ? 0.8173 1.0653 1.1980 0.1093  0.0551  -0.1291 32  THR   A O    
33   C  CB   . THR   A 5   ? 0.6925 0.9690 1.0609 0.0755  0.0449  -0.1031 32  THR   A CB   
34   O  OG1  . THR   A 5   ? 0.8549 1.1625 1.2566 0.0854  0.0501  -0.1081 32  THR   A OG1  
35   C  CG2  . THR   A 5   ? 0.7313 1.0154 1.1029 0.0695  0.0304  -0.0922 32  THR   A CG2  
36   N  N    . PRO   A 6   ? 0.8486 1.0901 1.1749 0.0889  0.0657  -0.1273 33  PRO   A N    
37   C  CA   . PRO   A 6   ? 0.7602 1.0090 1.0816 0.0996  0.0791  -0.1424 33  PRO   A CA   
38   C  C    . PRO   A 6   ? 0.8571 1.1347 1.2133 0.1073  0.0879  -0.1476 33  PRO   A C    
39   O  O    . PRO   A 6   ? 0.8431 1.1284 1.2006 0.1188  0.0981  -0.1622 33  PRO   A O    
40   C  CB   . PRO   A 6   ? 0.8323 1.0798 1.1172 0.0918  0.0928  -0.1381 33  PRO   A CB   
41   C  CG   . PRO   A 6   ? 0.8135 1.0386 1.0773 0.0807  0.0821  -0.1267 33  PRO   A CG   
42   C  CD   . PRO   A 6   ? 0.6604 0.8872 0.9530 0.0756  0.0667  -0.1192 33  PRO   A CD   
43   N  N    . LYS   A 7   ? 0.7970 1.0949 1.1819 0.1024  0.0838  -0.1378 34  LYS   A N    
44   C  CA   . LYS   A 7   ? 0.8038 1.1331 1.2258 0.1116  0.0900  -0.1427 34  LYS   A CA   
45   C  C    . LYS   A 7   ? 0.7649 1.0875 1.2122 0.1307  0.0832  -0.1478 34  LYS   A C    
46   O  O    . LYS   A 7   ? 0.9383 1.2822 1.4137 0.1426  0.0907  -0.1553 34  LYS   A O    
47   C  CB   . LYS   A 7   ? 0.5882 0.9482 1.0354 0.1025  0.0854  -0.1336 34  LYS   A CB   
48   N  N    . ASP   A 8   ? 0.8430 1.1356 1.2845 0.1340  0.0713  -0.1439 35  ASP   A N    
49   C  CA   . ASP   A 8   ? 0.7972 1.0771 1.2684 0.1512  0.0680  -0.1463 35  ASP   A CA   
50   C  C    . ASP   A 8   ? 0.8748 1.1321 1.3391 0.1573  0.0740  -0.1688 35  ASP   A C    
51   O  O    . ASP   A 8   ? 0.8099 1.0528 1.2402 0.1486  0.0730  -0.1769 35  ASP   A O    
52   C  CB   . ASP   A 8   ? 0.9056 1.1673 1.3819 0.1521  0.0546  -0.1275 35  ASP   A CB   
53   C  CG   . ASP   A 8   ? 0.9069 1.1982 1.3903 0.1496  0.0464  -0.1087 35  ASP   A CG   
54   O  OD1  . ASP   A 8   ? 0.9059 1.2020 1.3648 0.1330  0.0415  -0.1042 35  ASP   A OD1  
55   O  OD2  . ASP   A 8   ? 1.2559 1.5679 1.7708 0.1657  0.0449  -0.0997 35  ASP   A OD2  
56   N  N    . ASP   A 9   ? 0.8072 1.0640 1.3059 0.1736  0.0801  -0.1806 36  ASP   A N    
57   C  CA   . ASP   A 9   ? 0.8697 1.1104 1.3695 0.1803  0.0858  -0.2088 36  ASP   A CA   
58   C  C    . ASP   A 9   ? 0.8937 1.0993 1.3913 0.1761  0.0772  -0.2124 36  ASP   A C    
59   O  O    . ASP   A 9   ? 0.9661 1.1638 1.4423 0.1728  0.0764  -0.2347 36  ASP   A O    
60   C  CB   . ASP   A 9   ? 0.9347 1.1814 1.4792 0.1986  0.0954  -0.2215 36  ASP   A CB   
61   C  CG   . ASP   A 9   ? 1.0051 1.2893 1.5519 0.2034  0.1060  -0.2252 36  ASP   A CG   
62   O  OD1  . ASP   A 9   ? 1.1415 1.4407 1.6559 0.1977  0.1129  -0.2375 36  ASP   A OD1  
63   O  OD2  . ASP   A 9   ? 1.0612 1.3617 1.6429 0.2144  0.1087  -0.2145 36  ASP   A OD2  
64   N  N    . GLU   A 10  ? 0.8859 1.0736 1.4059 0.1777  0.0713  -0.1908 37  GLU   A N    
65   C  CA   . GLU   A 10  ? 0.8005 0.9542 1.3260 0.1736  0.0660  -0.1922 37  GLU   A CA   
66   C  C    . GLU   A 10  ? 0.9638 1.1127 1.4447 0.1569  0.0556  -0.1865 37  GLU   A C    
67   O  O    . GLU   A 10  ? 0.8732 0.9976 1.3552 0.1520  0.0513  -0.1927 37  GLU   A O    
68   C  CB   . GLU   A 10  ? 0.8873 1.0248 1.4481 0.1828  0.0663  -0.1651 37  GLU   A CB   
69   C  CG   . GLU   A 10  ? 1.0769 1.2249 1.6789 0.2022  0.0760  -0.1597 37  GLU   A CG   
70   C  CD   . GLU   A 10  ? 1.1900 1.3448 1.8054 0.2129  0.0728  -0.1219 37  GLU   A CD   
71   O  OE1  . GLU   A 10  ? 1.1655 1.3567 1.7680 0.2140  0.0672  -0.1091 37  GLU   A OE1  
72   O  OE2  . GLU   A 10  ? 1.0796 1.2060 1.7196 0.2212  0.0766  -0.1056 37  GLU   A OE2  
73   N  N    . PHE   A 11  ? 0.9513 1.1223 1.3975 0.1481  0.0532  -0.1756 38  PHE   A N    
74   C  CA   . PHE   A 11  ? 0.8699 1.0344 1.2763 0.1333  0.0449  -0.1668 38  PHE   A CA   
75   C  C    . PHE   A 11  ? 0.7966 0.9507 1.1795 0.1311  0.0437  -0.1909 38  PHE   A C    
76   O  O    . PHE   A 11  ? 0.8280 0.9657 1.1938 0.1231  0.0354  -0.1879 38  PHE   A O    
77   C  CB   . PHE   A 11  ? 0.8400 1.0295 1.2217 0.1248  0.0473  -0.1544 38  PHE   A CB   
78   C  CG   . PHE   A 11  ? 0.7349 0.9177 1.0741 0.1114  0.0438  -0.1500 38  PHE   A CG   
79   C  CD1  . PHE   A 11  ? 0.8275 1.0007 1.1575 0.1011  0.0342  -0.1316 38  PHE   A CD1  
80   C  CD2  . PHE   A 11  ? 0.9028 1.0907 1.2104 0.1114  0.0513  -0.1631 38  PHE   A CD2  
81   C  CE1  . PHE   A 11  ? 0.7631 0.9284 1.0568 0.0898  0.0323  -0.1275 38  PHE   A CE1  
82   C  CE2  . PHE   A 11  ? 0.8807 1.0612 1.1498 0.1022  0.0499  -0.1558 38  PHE   A CE2  
83   C  CZ   . PHE   A 11  ? 0.8012 0.9688 1.0651 0.0907  0.0405  -0.1385 38  PHE   A CZ   
84   N  N    . TYR   A 12  ? 0.9220 1.0896 1.3032 0.1397  0.0515  -0.2161 39  TYR   A N    
85   C  CA   . TYR   A 12  ? 0.9319 1.1011 1.2851 0.1412  0.0493  -0.2411 39  TYR   A CA   
86   C  C    . TYR   A 12  ? 0.8943 1.0436 1.2767 0.1432  0.0434  -0.2639 39  TYR   A C    
87   O  O    . TYR   A 12  ? 0.9152 1.0605 1.2774 0.1395  0.0354  -0.2763 39  TYR   A O    
88   C  CB   . TYR   A 12  ? 1.0078 1.2041 1.3476 0.1523  0.0602  -0.2612 39  TYR   A CB   
89   C  CG   . TYR   A 12  ? 1.0166 1.2320 1.3363 0.1492  0.0702  -0.2392 39  TYR   A CG   
90   C  CD1  . TYR   A 12  ? 0.9444 1.1706 1.2960 0.1514  0.0773  -0.2293 39  TYR   A CD1  
91   C  CD2  . TYR   A 12  ? 1.1809 1.4040 1.4538 0.1443  0.0740  -0.2280 39  TYR   A CD2  
92   C  CE1  . TYR   A 12  ? 1.1011 1.3478 1.4418 0.1466  0.0873  -0.2128 39  TYR   A CE1  
93   C  CE2  . TYR   A 12  ? 1.1349 1.3731 1.3973 0.1395  0.0867  -0.2090 39  TYR   A CE2  
94   C  CZ   . TYR   A 12  ? 1.0745 1.3257 1.3725 0.1393  0.0930  -0.2032 39  TYR   A CZ   
95   O  OH   . TYR   A 12  ? 1.0867 1.3560 1.3812 0.1327  0.1066  -0.1878 39  TYR   A OH   
96   N  N    . GLN   A 13  ? 0.9095 1.0465 1.3431 0.1495  0.0487  -0.2699 40  GLN   A N    
97   C  CA   . GLN   A 13  ? 0.8717 0.9860 1.3441 0.1497  0.0473  -0.2914 40  GLN   A CA   
98   C  C    . GLN   A 13  ? 0.9789 1.0665 1.4596 0.1396  0.0414  -0.2657 40  GLN   A C    
99   O  O    . GLN   A 13  ? 1.0285 1.0993 1.5294 0.1351  0.0388  -0.2826 40  GLN   A O    
100  C  CB   . GLN   A 13  ? 0.8945 1.0009 1.4233 0.1612  0.0592  -0.3056 40  GLN   A CB   
101  C  CG   . GLN   A 13  ? 0.9590 1.0451 1.5229 0.1645  0.0649  -0.2705 40  GLN   A CG   
102  C  CD   . GLN   A 13  ? 0.9079 0.9877 1.5253 0.1791  0.0788  -0.2816 40  GLN   A CD   
103  O  OE1  . GLN   A 13  ? 0.8745 0.9643 1.5053 0.1852  0.0842  -0.3191 40  GLN   A OE1  
104  N  NE2  . GLN   A 13  ? 1.0032 1.0683 1.6509 0.1871  0.0851  -0.2489 40  GLN   A NE2  
105  N  N    . GLN   A 14  ? 0.9334 1.0202 1.4009 0.1362  0.0396  -0.2273 41  GLN   A N    
106  C  CA   . GLN   A 14  ? 0.9623 1.0293 1.4284 0.1277  0.0335  -0.2025 41  GLN   A CA   
107  C  C    . GLN   A 14  ? 1.0002 1.0699 1.4232 0.1164  0.0229  -0.2082 41  GLN   A C    
108  O  O    . GLN   A 14  ? 1.0248 1.0766 1.4550 0.1098  0.0185  -0.2076 41  GLN   A O    
109  C  CB   . GLN   A 14  ? 1.0203 1.0945 1.4807 0.1290  0.0327  -0.1646 41  GLN   A CB   
110  C  CG   . GLN   A 14  ? 1.0813 1.1372 1.5466 0.1250  0.0288  -0.1375 41  GLN   A CG   
111  C  CD   . GLN   A 14  ? 1.2561 1.2914 1.7720 0.1373  0.0393  -0.1245 41  GLN   A CD   
112  O  OE1  . GLN   A 14  ? 1.1667 1.1904 1.7211 0.1448  0.0496  -0.1446 41  GLN   A OE1  
113  N  NE2  . GLN   A 14  ? 1.2174 1.2487 1.7342 0.1408  0.0383  -0.0905 41  GLN   A NE2  
114  N  N    . TRP   A 15  ? 0.9252 1.0172 1.3047 0.1153  0.0206  -0.2121 42  TRP   A N    
115  C  CA   . TRP   A 15  ? 0.9061 1.0020 1.2436 0.1089  0.0125  -0.2179 42  TRP   A CA   
116  C  C    . TRP   A 15  ? 0.9119 1.0072 1.2613 0.1123  0.0087  -0.2543 42  TRP   A C    
117  O  O    . TRP   A 15  ? 0.9669 1.0558 1.3052 0.1064  0.0002  -0.2581 42  TRP   A O    
118  C  CB   . TRP   A 15  ? 0.8395 0.9581 1.1328 0.1108  0.0162  -0.2138 42  TRP   A CB   
119  C  CG   . TRP   A 15  ? 0.9177 1.0379 1.1644 0.1056  0.0106  -0.2067 42  TRP   A CG   
120  C  CD1  . TRP   A 15  ? 0.8690 0.9809 1.1057 0.1032  0.0009  -0.2158 42  TRP   A CD1  
121  C  CD2  . TRP   A 15  ? 0.9452 1.0753 1.1527 0.1029  0.0165  -0.1884 42  TRP   A CD2  
122  N  NE1  . TRP   A 15  ? 0.9865 1.1027 1.1775 0.1013  -0.0005 -0.2030 42  TRP   A NE1  
123  C  CE2  . TRP   A 15  ? 0.9519 1.0767 1.1251 0.1007  0.0103  -0.1854 42  TRP   A CE2  
124  C  CE3  . TRP   A 15  ? 1.0294 1.1724 1.2318 0.1020  0.0282  -0.1747 42  TRP   A CE3  
125  C  CZ2  . TRP   A 15  ? 0.8904 1.0182 1.0244 0.0986  0.0170  -0.1672 42  TRP   A CZ2  
126  C  CZ3  . TRP   A 15  ? 1.0539 1.2003 1.2206 0.0976  0.0355  -0.1584 42  TRP   A CZ3  
127  C  CH2  . TRP   A 15  ? 0.9196 1.0565 1.0524 0.0964  0.0307  -0.1538 42  TRP   A CH2  
128  N  N    . GLN   A 16  ? 0.8636 0.9684 1.2391 0.1220  0.0146  -0.2841 43  GLN   A N    
129  C  CA   . GLN   A 16  ? 0.9239 1.0354 1.3156 0.1255  0.0104  -0.3265 43  GLN   A CA   
130  C  C    . GLN   A 16  ? 0.9820 1.0657 1.4238 0.1172  0.0099  -0.3315 43  GLN   A C    
131  O  O    . GLN   A 16  ? 1.0055 1.0914 1.4478 0.1126  0.0016  -0.3516 43  GLN   A O    
132  C  CB   . GLN   A 16  ? 0.9970 1.1267 1.4090 0.1380  0.0180  -0.3599 43  GLN   A CB   
133  N  N    . LEU   A 17  ? 1.0493 1.1079 1.5346 0.1164  0.0200  -0.3118 44  LEU   A N    
134  C  CA   . LEU   A 17  ? 0.9284 0.9582 1.4707 0.1111  0.0260  -0.3174 44  LEU   A CA   
135  C  C    . LEU   A 17  ? 0.9149 0.9278 1.4447 0.1005  0.0208  -0.2868 44  LEU   A C    
136  O  O    . LEU   A 17  ? 1.0782 1.0817 1.6301 0.0928  0.0189  -0.3033 44  LEU   A O    
137  C  CB   . LEU   A 17  ? 0.9098 0.9184 1.5042 0.1187  0.0422  -0.3048 44  LEU   A CB   
138  C  CG   . LEU   A 17  ? 1.0857 1.0918 1.7347 0.1253  0.0528  -0.3478 44  LEU   A CG   
139  C  CD1  . LEU   A 17  ? 1.0944 1.1374 1.7110 0.1333  0.0470  -0.3799 44  LEU   A CD1  
140  C  CD2  . LEU   A 17  ? 1.1513 1.1310 1.8526 0.1346  0.0710  -0.3269 44  LEU   A CD2  
141  N  N    . LYS   A 18  ? 1.0076 1.0193 1.5049 0.0998  0.0189  -0.2448 45  LYS   A N    
142  C  CA   . LYS   A 18  ? 0.9660 0.9611 1.4576 0.0920  0.0165  -0.2134 45  LYS   A CA   
143  C  C    . LYS   A 18  ? 0.9021 0.9117 1.3337 0.0852  0.0035  -0.1993 45  LYS   A C    
144  O  O    . LYS   A 18  ? 0.8936 0.8926 1.3160 0.0791  0.0008  -0.1741 45  LYS   A O    
145  C  CB   . LYS   A 18  ? 0.9222 0.9037 1.4347 0.0989  0.0263  -0.1753 45  LYS   A CB   
146  C  CG   . LYS   A 18  ? 0.9440 0.9091 1.5161 0.1090  0.0423  -0.1844 45  LYS   A CG   
147  C  CD   . LYS   A 18  ? 0.9548 0.8905 1.5677 0.1131  0.0560  -0.1541 45  LYS   A CD   
148  C  CE   . LYS   A 18  ? 1.0580 1.0007 1.6347 0.1149  0.0500  -0.1097 45  LYS   A CE   
149  N  NZ   . LYS   A 18  ? 1.1283 1.0523 1.7402 0.1289  0.0657  -0.0736 45  LYS   A NZ   
150  N  N    . TYR   A 19  ? 0.9493 0.9820 1.3407 0.0872  -0.0026 -0.2136 46  TYR   A N    
151  C  CA   . TYR   A 19  ? 0.8092 0.8518 1.1484 0.0817  -0.0122 -0.2038 46  TYR   A CA   
152  C  C    . TYR   A 19  ? 0.9094 0.9729 1.2215 0.0869  -0.0180 -0.2348 46  TYR   A C    
153  O  O    . TYR   A 19  ? 1.0217 1.1008 1.2892 0.0902  -0.0187 -0.2277 46  TYR   A O    
154  C  CB   . TYR   A 19  ? 0.8223 0.8737 1.1299 0.0808  -0.0107 -0.1755 46  TYR   A CB   
155  C  CG   . TYR   A 19  ? 0.7635 0.8052 1.0874 0.0783  -0.0084 -0.1444 46  TYR   A CG   
156  C  CD1  . TYR   A 19  ? 0.8217 0.8628 1.1803 0.0864  -0.0006 -0.1377 46  TYR   A CD1  
157  C  CD2  . TYR   A 19  ? 0.7652 0.8023 1.0684 0.0704  -0.0142 -0.1219 46  TYR   A CD2  
158  C  CE1  . TYR   A 19  ? 0.7652 0.8044 1.1351 0.0886  0.0006  -0.1083 46  TYR   A CE1  
159  C  CE2  . TYR   A 19  ? 0.7609 0.7967 1.0754 0.0712  -0.0132 -0.0953 46  TYR   A CE2  
160  C  CZ   . TYR   A 19  ? 0.8668 0.9054 1.2134 0.0813  -0.0062 -0.0879 46  TYR   A CZ   
161  O  OH   . TYR   A 19  ? 0.9986 1.0423 1.3534 0.0863  -0.0060 -0.0605 46  TYR   A OH   
162  N  N    . PRO   A 20  ? 0.8917 0.9590 1.2299 0.0889  -0.0211 -0.2696 47  PRO   A N    
163  C  CA   . PRO   A 20  ? 0.9526 1.0492 1.2612 0.0982  -0.0283 -0.3008 47  PRO   A CA   
164  C  C    . PRO   A 20  ? 1.0126 1.1172 1.2742 0.0974  -0.0382 -0.2909 47  PRO   A C    
165  O  O    . PRO   A 20  ? 1.0496 1.1809 1.2723 0.1092  -0.0426 -0.3051 47  PRO   A O    
166  C  CB   . PRO   A 20  ? 1.0225 1.1232 1.3828 0.0991  -0.0295 -0.3446 47  PRO   A CB   
167  C  CG   . PRO   A 20  ? 1.0734 1.1415 1.4802 0.0866  -0.0248 -0.3298 47  PRO   A CG   
168  C  CD   . PRO   A 20  ? 0.9530 1.0005 1.3492 0.0833  -0.0177 -0.2825 47  PRO   A CD   
169  N  N    . LYS   A 21  ? 0.8148 0.8984 1.0776 0.0862  -0.0407 -0.2660 48  LYS   A N    
170  C  CA   . LYS   A 21  ? 0.8258 0.9138 1.0475 0.0856  -0.0490 -0.2549 48  LYS   A CA   
171  C  C    . LYS   A 21  ? 0.8146 0.8991 0.9903 0.0852  -0.0445 -0.2208 48  LYS   A C    
172  O  O    . LYS   A 21  ? 0.8874 0.9703 1.0304 0.0843  -0.0486 -0.2069 48  LYS   A O    
173  C  CB   . LYS   A 21  ? 0.7131 0.7819 0.9607 0.0739  -0.0529 -0.2475 48  LYS   A CB   
174  C  CG   . LYS   A 21  ? 0.7982 0.8765 1.0848 0.0738  -0.0586 -0.2857 48  LYS   A CG   
175  C  CD   . LYS   A 21  ? 0.9358 0.9887 1.2682 0.0608  -0.0545 -0.2767 48  LYS   A CD   
176  C  CE   . LYS   A 21  ? 0.7607 0.8212 1.1484 0.0583  -0.0553 -0.3189 48  LYS   A CE   
177  N  NZ   . LYS   A 21  ? 0.7013 0.7358 1.1362 0.0456  -0.0473 -0.3079 48  LYS   A NZ   
178  N  N    . LEU   A 22  ? 0.7664 0.8501 0.9432 0.0856  -0.0349 -0.2085 49  LEU   A N    
179  C  CA   . LEU   A 22  ? 0.6844 0.7682 0.8256 0.0843  -0.0278 -0.1818 49  LEU   A CA   
180  C  C    . LEU   A 22  ? 0.7960 0.9022 0.9086 0.0982  -0.0209 -0.1926 49  LEU   A C    
181  O  O    . LEU   A 22  ? 0.7322 0.8500 0.8632 0.1047  -0.0165 -0.2095 49  LEU   A O    
182  C  CB   . LEU   A 22  ? 0.7690 0.8423 0.9332 0.0754  -0.0214 -0.1609 49  LEU   A CB   
183  C  CG   . LEU   A 22  ? 0.7439 0.8209 0.8830 0.0717  -0.0125 -0.1390 49  LEU   A CG   
184  C  CD1  . LEU   A 22  ? 0.7688 0.8354 0.8795 0.0646  -0.0148 -0.1220 49  LEU   A CD1  
185  C  CD2  . LEU   A 22  ? 0.7569 0.8343 0.9246 0.0658  -0.0084 -0.1261 49  LEU   A CD2  
186  N  N    . ILE   A 23  ? 0.8146 0.9266 0.8824 0.1046  -0.0183 -0.1815 50  ILE   A N    
187  C  CA   . ILE   A 23  ? 0.8362 0.9707 0.8692 0.1214  -0.0092 -0.1863 50  ILE   A CA   
188  C  C    . ILE   A 23  ? 0.9140 1.0396 0.9258 0.1167  0.0076  -0.1549 50  ILE   A C    
189  O  O    . ILE   A 23  ? 0.8885 0.9948 0.8935 0.1056  0.0088  -0.1327 50  ILE   A O    
190  C  CB   . ILE   A 23  ? 0.8949 1.0478 0.8926 0.1382  -0.0173 -0.1989 50  ILE   A CB   
191  C  CG1  . ILE   A 23  ? 0.8276 0.9963 0.8537 0.1422  -0.0333 -0.2379 50  ILE   A CG1  
192  C  CG2  . ILE   A 23  ? 0.8628 1.0403 0.8169 0.1594  -0.0050 -0.1962 50  ILE   A CG2  
193  C  CD1  . ILE   A 23  ? 1.0012 1.1738 1.0713 0.1393  -0.0318 -0.2620 50  ILE   A CD1  
194  N  N    . LEU   A 24  ? 0.8692 1.0096 0.8745 0.1245  0.0218  -0.1550 51  LEU   A N    
195  C  CA   . LEU   A 24  ? 0.8614 0.9967 0.8505 0.1210  0.0418  -0.1283 51  LEU   A CA   
196  C  C    . LEU   A 24  ? 0.9115 1.0662 0.8566 0.1430  0.0559  -0.1255 51  LEU   A C    
197  O  O    . LEU   A 24  ? 0.9711 1.1516 0.9104 0.1592  0.0550  -0.1474 51  LEU   A O    
198  C  CB   . LEU   A 24  ? 0.7937 0.9313 0.8182 0.1104  0.0504  -0.1265 51  LEU   A CB   
199  C  CG   . LEU   A 24  ? 0.9423 1.0765 0.9630 0.1023  0.0720  -0.1026 51  LEU   A CG   
200  C  CD1  . LEU   A 24  ? 0.8808 0.9923 0.8913 0.0900  0.0740  -0.0815 51  LEU   A CD1  
201  C  CD2  . LEU   A 24  ? 1.0394 1.1805 1.1020 0.0908  0.0756  -0.1044 51  LEU   A CD2  
202  N  N    . ARG   A 25  ? 0.8717 1.0146 0.7864 0.1451  0.0702  -0.0984 52  ARG   A N    
203  C  CA   . ARG   A 25  ? 0.9299 1.0880 0.8000 0.1681  0.0893  -0.0859 52  ARG   A CA   
204  C  C    . ARG   A 25  ? 1.0145 1.1567 0.8891 0.1576  0.1180  -0.0564 52  ARG   A C    
205  O  O    . ARG   A 25  ? 1.1092 1.2247 0.9876 0.1440  0.1252  -0.0352 52  ARG   A O    
206  C  CB   . ARG   A 25  ? 1.0470 1.2055 0.8762 0.1852  0.0831  -0.0785 52  ARG   A CB   
207  C  CG   . ARG   A 25  ? 1.0775 1.2602 0.9032 0.1980  0.0563  -0.1120 52  ARG   A CG   
208  C  CD   . ARG   A 25  ? 1.1256 1.3478 0.9057 0.2323  0.0594  -0.1219 52  ARG   A CD   
209  N  NE   . ARG   A 25  ? 1.2888 1.5391 1.0694 0.2441  0.0327  -0.1586 52  ARG   A NE   
210  C  CZ   . ARG   A 25  ? 1.1668 1.4312 0.9851 0.2371  0.0166  -0.1971 52  ARG   A CZ   
211  N  NH1  . ARG   A 25  ? 1.0106 1.2648 0.8654 0.2214  0.0232  -0.2026 52  ARG   A NH1  
212  N  NH2  . ARG   A 25  ? 1.2009 1.4913 1.0240 0.2466  -0.0058 -0.2320 52  ARG   A NH2  
213  N  N    . GLU   A 26  ? 1.0225 1.1820 0.9008 0.1632  0.1355  -0.0572 53  GLU   A N    
214  C  CA   . GLU   A 26  ? 1.1657 1.3133 1.0595 0.1504  0.1642  -0.0335 53  GLU   A CA   
215  C  C    . GLU   A 26  ? 1.0867 1.2218 0.9417 0.1638  0.1911  -0.0014 53  GLU   A C    
216  O  O    . GLU   A 26  ? 1.1017 1.2466 0.9107 0.1897  0.1888  0.0028  53  GLU   A O    
217  C  CB   . GLU   A 26  ? 1.0776 1.2497 0.9877 0.1539  0.1767  -0.0438 53  GLU   A CB   
218  C  CG   . GLU   A 26  ? 1.1569 1.3398 1.1066 0.1443  0.1528  -0.0734 53  GLU   A CG   
219  C  CD   . GLU   A 26  ? 1.3566 1.5522 1.3430 0.1349  0.1668  -0.0762 53  GLU   A CD   
220  O  OE1  . GLU   A 26  ? 1.3859 1.5735 1.4149 0.1136  0.1593  -0.0778 53  GLU   A OE1  
221  O  OE2  . GLU   A 26  ? 1.4070 1.6243 1.3793 0.1504  0.1851  -0.0774 53  GLU   A OE2  
222  N  N    . ALA   A 27  ? 1.0560 1.1708 0.9333 0.1467  0.2178  0.0210  54  ALA   A N    
223  C  CA   . ALA   A 27  ? 1.1616 1.2551 1.0128 0.1556  0.2480  0.0551  54  ALA   A CA   
224  C  C    . ALA   A 27  ? 1.2492 1.3637 1.0509 0.1902  0.2704  0.0708  54  ALA   A C    
225  O  O    . ALA   A 27  ? 1.3038 1.4053 1.0683 0.2092  0.2892  0.0993  54  ALA   A O    
226  C  CB   . ALA   A 27  ? 1.0515 1.1227 0.9475 0.1285  0.2758  0.0704  54  ALA   A CB   
227  N  N    . SER   A 28  ? 1.2391 1.3871 1.0383 0.2013  0.2695  0.0534  55  SER   A N    
228  C  CA   . SER   A 28  ? 1.2879 1.4629 1.0377 0.2367  0.2903  0.0657  55  SER   A CA   
229  C  C    . SER   A 28  ? 1.3609 1.5573 1.0557 0.2694  0.2692  0.0582  55  SER   A C    
230  O  O    . SER   A 28  ? 1.4119 1.6342 1.0570 0.3042  0.2859  0.0715  55  SER   A O    
231  C  CB   . SER   A 28  ? 1.2732 1.4815 1.0383 0.2392  0.2923  0.0435  55  SER   A CB   
232  O  OG   . SER   A 28  ? 1.3406 1.5359 1.1663 0.2058  0.2975  0.0379  55  SER   A OG   
233  N  N    . SER   A 29  ? 1.2456 1.4357 0.9486 0.2605  0.2337  0.0368  56  SER   A N    
234  C  CA   . SER   A 29  ? 1.1647 1.3786 0.8236 0.2889  0.2109  0.0246  56  SER   A CA   
235  C  C    . SER   A 29  ? 1.3041 1.4910 0.9395 0.2951  0.2153  0.0536  56  SER   A C    
236  O  O    . SER   A 29  ? 1.4043 1.6063 1.0150 0.3114  0.1906  0.0407  56  SER   A O    
237  C  CB   . SER   A 29  ? 1.1492 1.3778 0.8359 0.2770  0.1699  -0.0211 56  SER   A CB   
238  O  OG   . SER   A 29  ? 1.2669 1.4595 0.9949 0.2445  0.1557  -0.0220 56  SER   A OG   
239  N  N    . VAL   A 30  ? 1.3639 1.5121 1.0107 0.2822  0.2470  0.0905  57  VAL   A N    
240  C  CA   . VAL   A 30  ? 1.3615 1.4788 0.9904 0.2879  0.2569  0.1207  57  VAL   A CA   
241  C  C    . VAL   A 30  ? 1.3429 1.4439 0.9502 0.3044  0.3058  0.1668  57  VAL   A C    
242  O  O    . VAL   A 30  ? 1.2964 1.3867 0.9337 0.2876  0.3336  0.1765  57  VAL   A O    
243  C  CB   . VAL   A 30  ? 1.3842 1.4609 1.0635 0.2483  0.2454  0.1156  57  VAL   A CB   
244  C  CG1  . VAL   A 30  ? 1.3287 1.3634 1.0044 0.2474  0.2737  0.1540  57  VAL   A CG1  
245  C  CG2  . VAL   A 30  ? 1.3224 1.4106 1.0067 0.2433  0.2013  0.0828  57  VAL   A CG2  
246  N  N    . SER   A 31  ? 1.4252 1.5259 0.9823 0.3387  0.3177  0.1961  58  SER   A N    
247  C  CA   . SER   A 31  ? 1.4806 1.5640 1.0131 0.3602  0.3679  0.2458  58  SER   A CA   
248  C  C    . SER   A 31  ? 1.5170 1.5453 1.1061 0.3228  0.4002  0.2666  58  SER   A C    
249  O  O    . SER   A 31  ? 1.4942 1.4909 1.1209 0.2929  0.3852  0.2561  58  SER   A O    
250  C  CB   . SER   A 31  ? 1.5200 1.6058 0.9950 0.4017  0.3720  0.2750  58  SER   A CB   
251  O  OG   . SER   A 31  ? 1.4411 1.4748 0.9400 0.3843  0.3816  0.2958  58  SER   A OG   
252  N  N    . GLU   A 32  ? 1.4546 1.4744 1.0522 0.3243  0.4455  0.2939  59  GLU   A N    
253  C  CA   . GLU   A 32  ? 1.5104 1.4799 1.1646 0.2912  0.4822  0.3143  59  GLU   A CA   
254  C  C    . GLU   A 32  ? 1.5852 1.5106 1.2312 0.2990  0.4997  0.3470  59  GLU   A C    
255  O  O    . GLU   A 32  ? 1.6070 1.4907 1.3064 0.2643  0.5076  0.3452  59  GLU   A O    
256  C  CB   . GLU   A 32  ? 1.6568 1.6272 1.3188 0.2969  0.5329  0.3416  59  GLU   A CB   
257  C  CG   . GLU   A 32  ? 1.7548 1.6727 1.4714 0.2716  0.5854  0.3724  59  GLU   A CG   
258  C  CD   . GLU   A 32  ? 1.8915 1.7775 1.6837 0.2199  0.5725  0.3453  59  GLU   A CD   
259  O  OE1  . GLU   A 32  ? 1.9239 1.7731 1.7676 0.1975  0.6148  0.3630  59  GLU   A OE1  
260  O  OE2  . GLU   A 32  ? 1.7330 1.6331 1.5379 0.2010  0.5230  0.3053  59  GLU   A OE2  
261  N  N    . GLU   A 33  ? 1.5957 1.5326 1.1755 0.3461  0.5057  0.3758  60  GLU   A N    
262  C  CA   . GLU   A 33  ? 1.6286 1.5263 1.1960 0.3592  0.5201  0.4077  60  GLU   A CA   
263  C  C    . GLU   A 33  ? 1.5315 1.4105 1.1331 0.3274  0.4803  0.3751  60  GLU   A C    
264  O  O    . GLU   A 33  ? 1.6716 1.5030 1.3005 0.3137  0.4979  0.3920  60  GLU   A O    
265  C  CB   . GLU   A 33  ? 1.6351 1.5641 1.1280 0.4163  0.5122  0.4291  60  GLU   A CB   
266  C  CG   . GLU   A 33  ? 1.8260 1.7663 1.3023 0.4484  0.5403  0.4594  60  GLU   A CG   
267  C  CD   . GLU   A 33  ? 1.8764 1.8440 1.3630 0.4378  0.5509  0.4463  60  GLU   A CD   
268  O  OE1  . GLU   A 33  ? 1.8342 1.8460 1.3051 0.4340  0.5197  0.4085  60  GLU   A OE1  
269  O  OE2  . GLU   A 33  ? 1.8386 1.7838 1.3521 0.4337  0.5908  0.4720  60  GLU   A OE2  
270  N  N    . LEU   A 34  ? 1.4099 1.3250 1.0136 0.3151  0.4290  0.3283  61  LEU   A N    
271  C  CA   . LEU   A 34  ? 1.3030 1.2041 0.9389 0.2856  0.3917  0.2976  61  LEU   A CA   
272  C  C    . LEU   A 34  ? 1.4616 1.3382 1.1701 0.2347  0.3947  0.2768  61  LEU   A C    
273  O  O    . LEU   A 34  ? 1.3144 1.1609 1.0571 0.2095  0.3868  0.2685  61  LEU   A O    
274  C  CB   . LEU   A 34  ? 1.3412 1.2896 0.9529 0.2946  0.3391  0.2582  61  LEU   A CB   
275  C  CG   . LEU   A 34  ? 1.2897 1.2289 0.9145 0.2800  0.3021  0.2356  61  LEU   A CG   
276  C  CD1  . LEU   A 34  ? 1.1654 1.0832 0.7581 0.3069  0.3145  0.2674  61  LEU   A CD1  
277  C  CD2  . LEU   A 34  ? 1.1524 1.1381 0.7640 0.2855  0.2550  0.1947  61  LEU   A CD2  
278  N  N    . HIS   A 35  ? 1.4874 1.3811 1.2201 0.2205  0.4047  0.2660  62  HIS   A N    
279  C  CA   . HIS   A 35  ? 1.3900 1.2691 1.1924 0.1750  0.4069  0.2447  62  HIS   A CA   
280  C  C    . HIS   A 35  ? 1.4348 1.2645 1.2773 0.1567  0.4475  0.2684  62  HIS   A C    
281  O  O    . HIS   A 35  ? 1.3708 1.1808 1.2608 0.1238  0.4370  0.2487  62  HIS   A O    
282  C  CB   . HIS   A 35  ? 1.5007 1.4083 1.3203 0.1683  0.4168  0.2341  62  HIS   A CB   
283  C  CG   . HIS   A 35  ? 1.4165 1.3686 1.2207 0.1733  0.3743  0.1994  62  HIS   A CG   
284  N  ND1  . HIS   A 35  ? 1.2665 1.2263 1.0956 0.1510  0.3321  0.1643  62  HIS   A ND1  
285  C  CD2  . HIS   A 35  ? 1.3440 1.3348 1.1140 0.1982  0.3700  0.1941  62  HIS   A CD2  
286  C  CE1  . HIS   A 35  ? 1.3522 1.3495 1.1661 0.1613  0.3051  0.1399  62  HIS   A CE1  
287  N  NE2  . HIS   A 35  ? 1.2950 1.3127 1.0737 0.1892  0.3263  0.1548  62  HIS   A NE2  
288  N  N    . LYS   A 36  ? 1.5482 1.3578 1.3734 0.1788  0.4959  0.3105  63  LYS   A N    
289  C  CA   . LYS   A 36  ? 1.5911 1.3501 1.4619 0.1612  0.5414  0.3339  63  LYS   A CA   
290  C  C    . LYS   A 36  ? 1.5285 1.2538 1.3987 0.1600  0.5308  0.3369  63  LYS   A C    
291  O  O    . LYS   A 36  ? 1.6244 1.3159 1.5524 0.1278  0.5438  0.3277  63  LYS   A O    
292  C  CB   . LYS   A 36  ? 1.5994 1.3428 1.4471 0.1909  0.5985  0.3841  63  LYS   A CB   
293  N  N    . GLU   A 37  ? 1.4580 1.1954 1.2657 0.1951  0.5068  0.3468  64  GLU   A N    
294  C  CA   . GLU   A 37  ? 1.4952 1.2025 1.2993 0.1978  0.4977  0.3517  64  GLU   A CA   
295  C  C    . GLU   A 37  ? 1.4388 1.1514 1.2813 0.1608  0.4542  0.3055  64  GLU   A C    
296  O  O    . GLU   A 37  ? 1.3620 1.0397 1.2416 0.1399  0.4607  0.3010  64  GLU   A O    
297  C  CB   . GLU   A 37  ? 1.4953 1.2227 1.2237 0.2467  0.4815  0.3717  64  GLU   A CB   
298  C  CG   . GLU   A 37  ? 1.7203 1.4124 1.4398 0.2592  0.4857  0.3902  64  GLU   A CG   
299  C  CD   . GLU   A 37  ? 1.8180 1.5373 1.4632 0.3109  0.4701  0.4100  64  GLU   A CD   
300  O  OE1  . GLU   A 37  ? 1.8984 1.6594 1.4972 0.3410  0.4671  0.4170  64  GLU   A OE1  
301  O  OE2  . GLU   A 37  ? 1.6353 1.3381 1.2693 0.3224  0.4602  0.4163  64  GLU   A OE2  
302  N  N    . VAL   A 38  ? 1.2973 1.0534 1.1319 0.1539  0.4114  0.2714  65  VAL   A N    
303  C  CA   . VAL   A 38  ? 1.2584 1.0226 1.1260 0.1226  0.3713  0.2312  65  VAL   A CA   
304  C  C    . VAL   A 38  ? 1.3213 1.0709 1.2595 0.0808  0.3866  0.2134  65  VAL   A C    
305  O  O    . VAL   A 38  ? 1.2906 1.0246 1.2638 0.0564  0.3758  0.1946  65  VAL   A O    
306  C  CB   . VAL   A 38  ? 1.2165 1.0285 1.0615 0.1277  0.3272  0.2026  65  VAL   A CB   
307  C  CG1  . VAL   A 38  ? 1.0448 0.8658 0.9304 0.0941  0.2927  0.1649  65  VAL   A CG1  
308  C  CG2  . VAL   A 38  ? 1.1496 0.9795 0.9343 0.1647  0.3057  0.2100  65  VAL   A CG2  
309  N  N    . GLN   A 39  ? 1.3214 1.0799 1.2827 0.0727  0.4120  0.2169  66  GLN   A N    
310  C  CA   . GLN   A 39  ? 1.3750 1.1294 1.4075 0.0332  0.4244  0.1949  66  GLN   A CA   
311  C  C    . GLN   A 39  ? 1.3935 1.1005 1.4679 0.0184  0.4642  0.2085  66  GLN   A C    
312  O  O    . GLN   A 39  ? 1.3505 1.0531 1.4848 -0.0160 0.4627  0.1805  66  GLN   A O    
313  C  CB   . GLN   A 39  ? 1.3131 1.0917 1.3609 0.0301  0.4430  0.1955  66  GLN   A CB   
314  C  CG   . GLN   A 39  ? 1.2315 1.0575 1.2565 0.0362  0.4023  0.1719  66  GLN   A CG   
315  C  CD   . GLN   A 39  ? 1.3567 1.2070 1.3890 0.0395  0.4226  0.1759  66  GLN   A CD   
316  O  OE1  . GLN   A 39  ? 1.4126 1.2486 1.4829 0.0273  0.4642  0.1883  66  GLN   A OE1  
317  N  NE2  . GLN   A 39  ? 1.2309 1.1179 1.2302 0.0556  0.3947  0.1638  66  GLN   A NE2  
318  N  N    . GLU   A 40  ? 1.4284 1.1011 1.4737 0.0453  0.5004  0.2503  67  GLU   A N    
319  C  CA   . GLU   A 40  ? 1.4155 1.0371 1.5014 0.0338  0.5399  0.2650  67  GLU   A CA   
320  C  C    . GLU   A 40  ? 1.3951 1.0004 1.4779 0.0298  0.5131  0.2506  67  GLU   A C    
321  O  O    . GLU   A 40  ? 1.4598 1.0351 1.5972 0.0041  0.5295  0.2376  67  GLU   A O    
322  C  CB   . GLU   A 40  ? 1.5150 1.1035 1.5699 0.0680  0.5909  0.3197  67  GLU   A CB   
323  C  CG   . GLU   A 40  ? 1.6689 1.2413 1.7718 0.0548  0.6458  0.3362  67  GLU   A CG   
324  C  CD   . GLU   A 40  ? 1.9092 1.4861 1.9577 0.0974  0.6734  0.3813  67  GLU   A CD   
325  O  OE1  . GLU   A 40  ? 1.8870 1.4740 1.9622 0.0916  0.6973  0.3836  67  GLU   A OE1  
326  O  OE2  . GLU   A 40  ? 1.8687 1.4459 1.8486 0.1386  0.6639  0.4086  67  GLU   A OE2  
327  N  N    . ALA   A 41  ? 1.2929 0.9190 1.3159 0.0544  0.4729  0.2503  68  ALA   A N    
328  C  CA   . ALA   A 41  ? 1.1845 0.8005 1.2047 0.0503  0.4449  0.2345  68  ALA   A CA   
329  C  C    . ALA   A 41  ? 1.2956 0.9338 1.3622 0.0120  0.4121  0.1864  68  ALA   A C    
330  O  O    . ALA   A 41  ? 1.3237 0.9448 1.4168 -0.0041 0.4055  0.1694  68  ALA   A O    
331  C  CB   . ALA   A 41  ? 1.2042 0.8424 1.1538 0.0855  0.4106  0.2437  68  ALA   A CB   
332  N  N    . PHE   A 42  ? 1.3196 0.9983 1.3952 -0.0004 0.3916  0.1644  69  PHE   A N    
333  C  CA   . PHE   A 42  ? 1.2580 0.9619 1.3800 -0.0341 0.3650  0.1219  69  PHE   A CA   
334  C  C    . PHE   A 42  ? 1.3137 0.9949 1.5060 -0.0651 0.3960  0.1076  69  PHE   A C    
335  O  O    . PHE   A 42  ? 1.2988 0.9806 1.5221 -0.0855 0.3806  0.0792  69  PHE   A O    
336  C  CB   . PHE   A 42  ? 1.2277 0.9757 1.3506 -0.0384 0.3468  0.1071  69  PHE   A CB   
337  C  CG   . PHE   A 42  ? 1.2017 0.9808 1.2771 -0.0211 0.3029  0.0998  69  PHE   A CG   
338  C  CD1  . PHE   A 42  ? 1.2673 1.0440 1.3205 -0.0157 0.2736  0.0923  69  PHE   A CD1  
339  C  CD2  . PHE   A 42  ? 1.2507 1.0607 1.3072 -0.0103 0.2934  0.0996  69  PHE   A CD2  
340  C  CE1  . PHE   A 42  ? 1.2535 1.0578 1.2712 -0.0018 0.2365  0.0842  69  PHE   A CE1  
341  C  CE2  . PHE   A 42  ? 1.2801 1.1164 1.3006 0.0042  0.2559  0.0902  69  PHE   A CE2  
342  C  CZ   . PHE   A 42  ? 1.1943 1.0272 1.1970 0.0079  0.2282  0.0827  69  PHE   A CZ   
343  N  N    . LEU   A 43  ? 1.2945 0.9572 1.5153 -0.0689 0.4414  0.1254  70  LEU   A N    
344  C  CA   . LEU   A 43  ? 1.3086 0.9501 1.6059 -0.1002 0.4756  0.1092  70  LEU   A CA   
345  C  C    . LEU   A 43  ? 1.3740 0.9623 1.6825 -0.0975 0.5026  0.1237  70  LEU   A C    
346  O  O    . LEU   A 43  ? 1.3574 0.9318 1.7315 -0.1266 0.5177  0.0969  70  LEU   A O    
347  C  CB   . LEU   A 43  ? 1.3266 0.9645 1.6551 -0.1051 0.5194  0.1253  70  LEU   A CB   
348  C  CG   . LEU   A 43  ? 1.3010 0.9917 1.6303 -0.1108 0.4973  0.1076  70  LEU   A CG   
349  C  CD1  . LEU   A 43  ? 1.2873 0.9728 1.6008 -0.0931 0.5348  0.1430  70  LEU   A CD1  
350  C  CD2  . LEU   A 43  ? 1.2760 0.9978 1.6819 -0.1498 0.4893  0.0601  70  LEU   A CD2  
351  N  N    . THR   A 44  ? 1.3307 0.8917 1.5791 -0.0622 0.5089  0.1633  71  THR   A N    
352  C  CA   . THR   A 44  ? 1.2760 0.7870 1.5316 -0.0559 0.5318  0.1783  71  THR   A CA   
353  C  C    . THR   A 44  ? 1.4091 0.9309 1.6740 -0.0711 0.4925  0.1408  71  THR   A C    
354  O  O    . THR   A 44  ? 1.4397 0.9331 1.7550 -0.0906 0.5102  0.1240  71  THR   A O    
355  C  CB   . THR   A 44  ? 1.3859 0.8743 1.5700 -0.0097 0.5437  0.2298  71  THR   A CB   
356  O  OG1  . THR   A 44  ? 1.4109 0.8705 1.6018 0.0034  0.5985  0.2700  71  THR   A OG1  
357  C  CG2  . THR   A 44  ? 1.4641 0.9157 1.6390 0.0020  0.5453  0.2385  71  THR   A CG2  
358  N  N    . LEU   A 45  ? 1.3656 0.9290 1.5853 -0.0627 0.4408  0.1263  72  LEU   A N    
359  C  CA   . LEU   A 45  ? 1.3218 0.8999 1.5474 -0.0756 0.4037  0.0925  72  LEU   A CA   
360  C  C    . LEU   A 45  ? 1.2736 0.8779 1.5655 -0.1143 0.3955  0.0450  72  LEU   A C    
361  O  O    . LEU   A 45  ? 1.2885 0.8906 1.6082 -0.1302 0.3856  0.0166  72  LEU   A O    
362  C  CB   . LEU   A 45  ? 1.1268 0.7423 1.2918 -0.0566 0.3548  0.0912  72  LEU   A CB   
363  C  CG   . LEU   A 45  ? 1.1296 0.7329 1.2279 -0.0168 0.3547  0.1304  72  LEU   A CG   
364  C  CD1  . LEU   A 45  ? 1.1027 0.7507 1.1558 -0.0031 0.3148  0.1256  72  LEU   A CD1  
365  C  CD2  . LEU   A 45  ? 1.2463 0.8226 1.3291 -0.0041 0.3515  0.1372  72  LEU   A CD2  
366  N  N    . HIS   A 46  ? 1.2921 0.9253 1.6098 -0.1285 0.3990  0.0340  73  HIS   A N    
367  C  CA   . HIS   A 46  ? 1.3757 1.0419 1.7581 -0.1630 0.3906  -0.0128 73  HIS   A CA   
368  C  C    . HIS   A 46  ? 1.4126 1.0442 1.8672 -0.1868 0.4332  -0.0270 73  HIS   A C    
369  O  O    . HIS   A 46  ? 1.3543 1.0035 1.8573 -0.2116 0.4225  -0.0704 73  HIS   A O    
370  C  CB   . HIS   A 46  ? 1.3490 1.0561 1.7423 -0.1696 0.3853  -0.0194 73  HIS   A CB   
371  C  CG   . HIS   A 46  ? 1.4005 1.1512 1.8580 -0.2014 0.3734  -0.0679 73  HIS   A CG   
372  N  ND1  . HIS   A 46  ? 1.4201 1.1817 1.9382 -0.2221 0.4020  -0.0808 73  HIS   A ND1  
373  C  CD2  . HIS   A 46  ? 1.3230 1.1141 1.7935 -0.2139 0.3361  -0.1071 73  HIS   A CD2  
374  C  CE1  . HIS   A 46  ? 1.3453 1.1548 1.9120 -0.2461 0.3807  -0.1284 73  HIS   A CE1  
375  N  NE2  . HIS   A 46  ? 1.3181 1.1468 1.8548 -0.2403 0.3406  -0.1441 73  HIS   A NE2  
376  N  N    . LYS   A 47  ? 1.3581 0.9417 1.8225 -0.1787 0.4833  0.0085  74  LYS   A N    
377  C  CA   . LYS   A 47  ? 1.4529 1.0034 1.9867 -0.1970 0.5250  -0.0036 74  LYS   A CA   
378  C  C    . LYS   A 47  ? 1.5025 1.0260 2.0346 -0.1923 0.5202  -0.0120 74  LYS   A C    
379  O  O    . LYS   A 47  ? 1.3983 0.9287 1.9864 -0.2101 0.5249  -0.0496 74  LYS   A O    
380  C  CB   . LYS   A 47  ? 1.4511 0.9676 1.9801 -0.1765 0.5713  0.0399  74  LYS   A CB   
381  N  N    . HIS   A 48  ? 1.3731 0.8686 1.8423 -0.1670 0.5109  0.0212  75  HIS   A N    
382  C  CA   . HIS   A 48  ? 1.3031 0.7749 1.7666 -0.1604 0.5041  0.0145  75  HIS   A CA   
383  C  C    . HIS   A 48  ? 1.3396 0.8531 1.8047 -0.1769 0.4560  -0.0319 75  HIS   A C    
384  O  O    . HIS   A 48  ? 1.3663 0.8637 1.8243 -0.1723 0.4471  -0.0400 75  HIS   A O    
385  C  CB   . HIS   A 48  ? 1.3143 0.7494 1.7056 -0.1208 0.5087  0.0673  75  HIS   A CB   
386  C  CG   . HIS   A 48  ? 1.4186 0.8182 1.8043 -0.0959 0.5542  0.1118  75  HIS   A CG   
387  N  ND1  . HIS   A 48  ? 1.4929 0.8565 1.8494 -0.0652 0.5705  0.1449  75  HIS   A ND1  
388  C  CD2  . HIS   A 48  ? 1.5480 0.9479 1.9525 -0.0945 0.5855  0.1282  75  HIS   A CD2  
389  C  CE1  . HIS   A 48  ? 1.4009 0.7451 1.7581 -0.0452 0.6100  0.1800  75  HIS   A CE1  
390  N  NE2  . HIS   A 48  ? 1.5247 0.8885 1.9105 -0.0626 0.6203  0.1708  75  HIS   A NE2  
391  N  N    . GLY   A 49  ? 1.2998 0.8718 1.7703 -0.1914 0.4235  -0.0609 76  GLY   A N    
392  C  CA   . GLY   A 49  ? 1.0777 0.6992 1.5483 -0.2031 0.3776  -0.1038 76  GLY   A CA   
393  C  C    . GLY   A 49  ? 1.1465 0.7754 1.5454 -0.1775 0.3402  -0.0879 76  GLY   A C    
394  O  O    . GLY   A 49  ? 1.0325 0.6704 1.4326 -0.1814 0.3202  -0.1121 76  GLY   A O    
395  N  N    . CYS   A 50  ? 1.2554 0.8840 1.5941 -0.1515 0.3305  -0.0499 77  CYS   A N    
396  C  CA   . CYS   A 50  ? 1.3239 0.9576 1.5984 -0.1263 0.2991  -0.0332 77  CYS   A CA   
397  C  C    . CYS   A 50  ? 1.2165 0.9055 1.4646 -0.1261 0.2533  -0.0492 77  CYS   A C    
398  O  O    . CYS   A 50  ? 1.2821 0.9795 1.4841 -0.1083 0.2263  -0.0398 77  CYS   A O    
399  C  CB   . CYS   A 50  ? 1.3458 0.9478 1.5707 -0.0947 0.3161  0.0159  77  CYS   A CB   
400  S  SG   . CYS   A 50  ? 1.4393 0.9722 1.6780 -0.0828 0.3653  0.0446  77  CYS   A SG   
401  N  N    . LEU   A 51  ? 1.1536 0.8805 1.4324 -0.1444 0.2456  -0.0724 78  LEU   A N    
402  C  CA   . LEU   A 51  ? 1.0341 0.8127 1.2929 -0.1431 0.2054  -0.0861 78  LEU   A CA   
403  C  C    . LEU   A 51  ? 0.9591 0.7741 1.2523 -0.1626 0.1862  -0.1284 78  LEU   A C    
404  O  O    . LEU   A 51  ? 1.0824 0.9050 1.4313 -0.1849 0.2026  -0.1565 78  LEU   A O    
405  C  CB   . LEU   A 51  ? 0.9256 0.7273 1.1897 -0.1447 0.2076  -0.0805 78  LEU   A CB   
406  C  CG   . LEU   A 51  ? 0.9680 0.7458 1.1897 -0.1215 0.2205  -0.0409 78  LEU   A CG   
407  C  CD1  . LEU   A 51  ? 1.0276 0.7796 1.2795 -0.1277 0.2634  -0.0275 78  LEU   A CD1  
408  C  CD2  . LEU   A 51  ? 1.2231 1.0375 1.4141 -0.1103 0.1916  -0.0374 78  LEU   A CD2  
409  N  N    . PHE   A 52  ? 0.8884 0.7286 1.1501 -0.1534 0.1526  -0.1339 79  PHE   A N    
410  C  CA   . PHE   A 52  ? 0.9945 0.8715 1.2781 -0.1657 0.1331  -0.1707 79  PHE   A CA   
411  C  C    . PHE   A 52  ? 0.8603 0.7896 1.1219 -0.1585 0.0977  -0.1755 79  PHE   A C    
412  O  O    . PHE   A 52  ? 0.8561 0.7834 1.0768 -0.1412 0.0845  -0.1491 79  PHE   A O    
413  C  CB   . PHE   A 52  ? 1.0697 0.9234 1.3389 -0.1600 0.1315  -0.1726 79  PHE   A CB   
414  C  CG   . PHE   A 52  ? 1.2402 1.0377 1.5285 -0.1628 0.1674  -0.1634 79  PHE   A CG   
415  C  CD1  . PHE   A 52  ? 1.2422 0.9950 1.4949 -0.1428 0.1823  -0.1232 79  PHE   A CD1  
416  C  CD2  . PHE   A 52  ? 1.1528 0.9441 1.4962 -0.1837 0.1868  -0.1961 79  PHE   A CD2  
417  C  CE1  . PHE   A 52  ? 1.3008 1.0011 1.5703 -0.1415 0.2177  -0.1105 79  PHE   A CE1  
418  C  CE2  . PHE   A 52  ? 1.2340 0.9692 1.6000 -0.1857 0.2236  -0.1862 79  PHE   A CE2  
419  C  CZ   . PHE   A 52  ? 1.3627 1.0511 1.6902 -0.1634 0.2398  -0.1406 79  PHE   A CZ   
420  N  N    . ARG   A 53  ? 0.8543 0.8323 1.1456 -0.1707 0.0834  -0.2106 80  ARG   A N    
421  C  CA   . ARG   A 53  ? 0.8657 0.8951 1.1363 -0.1608 0.0509  -0.2148 80  ARG   A CA   
422  C  C    . ARG   A 53  ? 0.9618 0.9936 1.2019 -0.1500 0.0338  -0.2144 80  ARG   A C    
423  O  O    . ARG   A 53  ? 0.9987 1.0225 1.2539 -0.1578 0.0404  -0.2348 80  ARG   A O    
424  C  CB   . ARG   A 53  ? 0.8767 0.9650 1.1895 -0.1740 0.0420  -0.2519 80  ARG   A CB   
425  C  CG   . ARG   A 53  ? 0.8723 0.9728 1.2111 -0.1808 0.0517  -0.2505 80  ARG   A CG   
426  C  CD   . ARG   A 53  ? 1.0060 1.1592 1.4013 -0.1989 0.0507  -0.2949 80  ARG   A CD   
427  N  NE   . ARG   A 53  ? 1.0775 1.2987 1.4640 -0.1884 0.0183  -0.3113 80  ARG   A NE   
428  C  CZ   . ARG   A 53  ? 1.1087 1.3862 1.5208 -0.1895 0.0073  -0.3286 80  ARG   A CZ   
429  N  NH1  . ARG   A 53  ? 1.0879 1.3633 1.5389 -0.2030 0.0258  -0.3341 80  ARG   A NH1  
430  N  NH2  . ARG   A 53  ? 1.0549 1.3941 1.4531 -0.1749 -0.0217 -0.3392 80  ARG   A NH2  
431  N  N    . ASP   A 54  ? 1.0063 1.0483 1.2067 -0.1324 0.0139  -0.1917 81  ASP   A N    
432  C  CA   . ASP   A 54  ? 0.8770 0.9207 1.0480 -0.1210 -0.0003 -0.1869 81  ASP   A CA   
433  C  C    . ASP   A 54  ? 0.8777 0.9813 1.0512 -0.1180 -0.0221 -0.2077 81  ASP   A C    
434  O  O    . ASP   A 54  ? 0.9542 1.0991 1.1395 -0.1173 -0.0320 -0.2146 81  ASP   A O    
435  C  CB   . ASP   A 54  ? 0.9129 0.9343 1.0445 -0.1036 -0.0072 -0.1520 81  ASP   A CB   
436  C  CG   . ASP   A 54  ? 1.0705 1.0384 1.1914 -0.1009 0.0118  -0.1319 81  ASP   A CG   
437  O  OD1  . ASP   A 54  ? 0.9766 0.9167 1.0924 -0.1000 0.0205  -0.1319 81  ASP   A OD1  
438  O  OD2  . ASP   A 54  ? 1.2410 1.1970 1.3577 -0.0975 0.0183  -0.1157 81  ASP   A OD2  
439  N  N    . LEU   A 55  ? 0.9813 1.0922 1.1427 -0.1138 -0.0290 -0.2171 82  LEU   A N    
440  C  CA   . LEU   A 55  ? 0.8740 1.0437 1.0307 -0.1066 -0.0486 -0.2348 82  LEU   A CA   
441  C  C    . LEU   A 55  ? 0.9547 1.1244 1.0708 -0.0867 -0.0610 -0.2041 82  LEU   A C    
442  O  O    . LEU   A 55  ? 1.0302 1.1946 1.1289 -0.0808 -0.0630 -0.2033 82  LEU   A O    
443  C  CB   . LEU   A 55  ? 0.9143 1.0978 1.0904 -0.1163 -0.0456 -0.2719 82  LEU   A CB   
444  C  CG   . LEU   A 55  ? 1.0042 1.2601 1.1810 -0.1093 -0.0651 -0.2996 82  LEU   A CG   
445  C  CD1  . LEU   A 55  ? 1.0603 1.3675 1.2566 -0.1096 -0.0752 -0.3111 82  LEU   A CD1  
446  C  CD2  . LEU   A 55  ? 1.0360 1.3034 1.2388 -0.1215 -0.0598 -0.3430 82  LEU   A CD2  
447  N  N    . VAL   A 56  ? 0.8140 0.9891 0.9187 -0.0767 -0.0674 -0.1794 83  VAL   A N    
448  C  CA   . VAL   A 56  ? 0.8949 1.0641 0.9695 -0.0597 -0.0749 -0.1489 83  VAL   A CA   
449  C  C    . VAL   A 56  ? 0.9100 1.1341 0.9736 -0.0452 -0.0895 -0.1508 83  VAL   A C    
450  O  O    . VAL   A 56  ? 0.9914 1.2628 1.0684 -0.0470 -0.0965 -0.1773 83  VAL   A O    
451  C  CB   . VAL   A 56  ? 0.8339 0.9832 0.9058 -0.0551 -0.0731 -0.1236 83  VAL   A CB   
452  C  CG1  . VAL   A 56  ? 0.8615 0.9620 0.9393 -0.0655 -0.0582 -0.1205 83  VAL   A CG1  
453  C  CG2  . VAL   A 56  ? 1.0135 1.2042 1.1008 -0.0525 -0.0803 -0.1287 83  VAL   A CG2  
454  N  N    . ARG   A 57  ? 0.8646 1.0852 0.9052 -0.0297 -0.0930 -0.1232 84  ARG   A N    
455  C  CA   . ARG   A 57  ? 0.8809 1.1502 0.9071 -0.0112 -0.1031 -0.1152 84  ARG   A CA   
456  C  C    . ARG   A 57  ? 1.1310 1.3933 1.1507 0.0029  -0.1030 -0.0806 84  ARG   A C    
457  O  O    . ARG   A 57  ? 1.0482 1.2680 1.0634 0.0026  -0.0959 -0.0603 84  ARG   A O    
458  C  CB   . ARG   A 57  ? 0.8903 1.1636 0.8976 -0.0049 -0.1027 -0.1161 84  ARG   A CB   
459  C  CG   . ARG   A 57  ? 1.0316 1.3635 1.0220 0.0161  -0.1116 -0.1113 84  ARG   A CG   
460  C  CD   . ARG   A 57  ? 1.0076 1.3505 0.9809 0.0209  -0.1107 -0.1198 84  ARG   A CD   
461  N  NE   . ARG   A 57  ? 1.1416 1.5525 1.0990 0.0410  -0.1201 -0.1248 84  ARG   A NE   
462  C  CZ   . ARG   A 57  ? 1.2640 1.7149 1.2170 0.0419  -0.1258 -0.1575 84  ARG   A CZ   
463  N  NH1  . ARG   A 57  ? 1.1714 1.5970 1.1382 0.0226  -0.1216 -0.1878 84  ARG   A NH1  
464  N  NH2  . ARG   A 57  ? 1.2557 1.7753 1.1904 0.0644  -0.1354 -0.1601 84  ARG   A NH2  
465  N  N    . ILE   A 58  ? 1.1118 1.4177 1.1343 0.0161  -0.1104 -0.0756 85  ILE   A N    
466  C  CA   . ILE   A 58  ? 1.0809 1.3833 1.1016 0.0317  -0.1086 -0.0429 85  ILE   A CA   
467  C  C    . ILE   A 58  ? 1.1658 1.5225 1.1717 0.0566  -0.1147 -0.0299 85  ILE   A C    
468  O  O    . ILE   A 58  ? 1.1340 1.5452 1.1418 0.0632  -0.1252 -0.0483 85  ILE   A O    
469  C  CB   . ILE   A 58  ? 1.0839 1.3824 1.1250 0.0266  -0.1089 -0.0446 85  ILE   A CB   
470  C  CG1  . ILE   A 58  ? 1.1947 1.4554 1.2493 0.0030  -0.1031 -0.0648 85  ILE   A CG1  
471  C  CG2  . ILE   A 58  ? 1.1463 1.4218 1.1900 0.0386  -0.1029 -0.0122 85  ILE   A CG2  
472  C  CD1  . ILE   A 58  ? 1.3062 1.5538 1.3784 -0.0017 -0.0998 -0.0617 85  ILE   A CD1  
473  N  N    . GLN   A 59  ? 1.2142 1.5591 1.2069 0.0716  -0.1070 0.0016  86  GLN   A N    
474  C  CA   . GLN   A 59  ? 1.1209 1.5123 1.0976 0.1003  -0.1079 0.0245  86  GLN   A CA   
475  C  C    . GLN   A 59  ? 1.1771 1.6266 1.1351 0.1083  -0.1184 0.0013  86  GLN   A C    
476  O  O    . GLN   A 59  ? 1.2954 1.8050 1.2418 0.1318  -0.1260 0.0055  86  GLN   A O    
477  C  CB   . GLN   A 59  ? 1.1544 1.5693 1.1418 0.1158  -0.1107 0.0396  86  GLN   A CB   
478  C  CG   . GLN   A 59  ? 1.2049 1.5676 1.2155 0.1043  -0.1028 0.0505  86  GLN   A CG   
479  C  CD   . GLN   A 59  ? 1.2874 1.6284 1.3026 0.1224  -0.0889 0.0915  86  GLN   A CD   
480  O  OE1  . GLN   A 59  ? 1.2823 1.6020 1.2910 0.1258  -0.0779 0.1096  86  GLN   A OE1  
481  N  NE2  . GLN   A 59  ? 1.2193 1.5650 1.2499 0.1336  -0.0873 0.1057  86  GLN   A NE2  
482  N  N    . GLY   A 60  ? 1.2038 1.6381 1.1592 0.0905  -0.1188 -0.0248 87  GLY   A N    
483  C  CA   . GLY   A 60  ? 1.2984 1.7835 1.2381 0.0966  -0.1271 -0.0506 87  GLY   A CA   
484  C  C    . GLY   A 60  ? 1.3666 1.8911 1.3223 0.0845  -0.1403 -0.0969 87  GLY   A C    
485  O  O    . GLY   A 60  ? 1.3399 1.9086 1.2874 0.0874  -0.1478 -0.1263 87  GLY   A O    
486  N  N    . LYS   A 61  ? 1.1756 1.6875 1.1569 0.0708  -0.1424 -0.1068 88  LYS   A N    
487  C  CA   . LYS   A 61  ? 1.1611 1.7084 1.1669 0.0564  -0.1520 -0.1520 88  LYS   A CA   
488  C  C    . LYS   A 61  ? 1.0389 1.5249 1.0706 0.0247  -0.1419 -0.1693 88  LYS   A C    
489  O  O    . LYS   A 61  ? 1.0112 1.4392 1.0447 0.0178  -0.1318 -0.1438 88  LYS   A O    
490  C  CB   . LYS   A 61  ? 1.1983 1.7947 1.2156 0.0697  -0.1620 -0.1507 88  LYS   A CB   
491  C  CG   . LYS   A 61  ? 1.0381 1.5918 1.0615 0.0722  -0.1540 -0.1141 88  LYS   A CG   
492  C  CD   . LYS   A 61  ? 1.1269 1.7244 1.1356 0.1056  -0.1591 -0.0825 88  LYS   A CD   
493  C  CE   . LYS   A 61  ? 1.0519 1.6081 1.0737 0.1068  -0.1506 -0.0518 88  LYS   A CE   
494  N  NZ   . LYS   A 61  ? 0.9740 1.5712 0.9863 0.1408  -0.1533 -0.0204 88  LYS   A NZ   
495  N  N    . ASP   A 62  ? 1.1512 1.6519 1.2041 0.0069  -0.1435 -0.2133 89  ASP   A N    
496  C  CA   . ASP   A 62  ? 1.0863 1.5306 1.1653 -0.0212 -0.1305 -0.2295 89  ASP   A CA   
497  C  C    . ASP   A 62  ? 0.9764 1.4291 1.0891 -0.0336 -0.1297 -0.2437 89  ASP   A C    
498  O  O    . ASP   A 62  ? 0.9494 1.4639 1.0824 -0.0328 -0.1402 -0.2747 89  ASP   A O    
499  C  CB   . ASP   A 62  ? 1.2496 1.6985 1.3405 -0.0348 -0.1277 -0.2689 89  ASP   A CB   
500  C  CG   . ASP   A 62  ? 1.1832 1.6496 1.2415 -0.0182 -0.1323 -0.2629 89  ASP   A CG   
501  O  OD1  . ASP   A 62  ? 1.1419 1.5584 1.1800 -0.0160 -0.1235 -0.2341 89  ASP   A OD1  
502  O  OD2  . ASP   A 62  ? 1.1374 1.6712 1.1909 -0.0066 -0.1446 -0.2881 89  ASP   A OD2  
503  N  N    . LEU   A 63  ? 0.8666 1.2615 0.9861 -0.0441 -0.1174 -0.2228 90  LEU   A N    
504  C  CA   . LEU   A 63  ? 0.9287 1.3254 1.0774 -0.0543 -0.1137 -0.2291 90  LEU   A CA   
505  C  C    . LEU   A 63  ? 0.8617 1.2033 1.0345 -0.0791 -0.0944 -0.2404 90  LEU   A C    
506  O  O    . LEU   A 63  ? 0.9938 1.2790 1.1506 -0.0824 -0.0835 -0.2231 90  LEU   A O    
507  C  CB   . LEU   A 63  ? 0.9656 1.3478 1.0997 -0.0399 -0.1148 -0.1902 90  LEU   A CB   
508  C  CG   . LEU   A 63  ? 0.9418 1.3696 1.0556 -0.0123 -0.1285 -0.1686 90  LEU   A CG   
509  C  CD1  . LEU   A 63  ? 0.9809 1.4076 1.1049 -0.0057 -0.1279 -0.1495 90  LEU   A CD1  
510  C  CD2  . LEU   A 63  ? 0.8538 1.3595 0.9711 -0.0020 -0.1437 -0.1968 90  LEU   A CD2  
511  N  N    . LEU   A 64  ? 0.8615 1.2214 1.0743 -0.0950 -0.0891 -0.2686 91  LEU   A N    
512  C  CA   . LEU   A 64  ? 0.8395 1.1475 1.0785 -0.1164 -0.0666 -0.2730 91  LEU   A CA   
513  C  C    . LEU   A 64  ? 0.9088 1.1944 1.1449 -0.1131 -0.0607 -0.2447 91  LEU   A C    
514  O  O    . LEU   A 64  ? 1.0630 1.3911 1.3115 -0.1073 -0.0700 -0.2477 91  LEU   A O    
515  C  CB   . LEU   A 64  ? 1.0676 1.4049 1.3587 -0.1374 -0.0595 -0.3198 91  LEU   A CB   
516  C  CG   . LEU   A 64  ? 1.0174 1.3206 1.3298 -0.1554 -0.0421 -0.3435 91  LEU   A CG   
517  C  CD1  . LEU   A 64  ? 0.7320 1.0533 1.1076 -0.1797 -0.0281 -0.3862 91  LEU   A CD1  
518  C  CD2  . LEU   A 64  ? 0.9612 1.1837 1.2518 -0.1563 -0.0223 -0.3087 91  LEU   A CD2  
519  N  N    . THR   A 65  ? 0.9550 1.1780 1.1745 -0.1147 -0.0458 -0.2184 92  THR   A N    
520  C  CA   . THR   A 65  ? 0.9834 1.1853 1.1978 -0.1103 -0.0397 -0.1934 92  THR   A CA   
521  C  C    . THR   A 65  ? 0.8828 1.0940 1.1391 -0.1265 -0.0255 -0.2118 92  THR   A C    
522  O  O    . THR   A 65  ? 0.9527 1.1468 1.2370 -0.1442 -0.0080 -0.2314 92  THR   A O    
523  C  CB   . THR   A 65  ? 0.9816 1.1211 1.1685 -0.1067 -0.0274 -0.1655 92  THR   A CB   
524  O  OG1  . THR   A 65  ? 0.9529 1.0558 1.1588 -0.1219 -0.0040 -0.1727 92  THR   A OG1  
525  C  CG2  . THR   A 65  ? 1.0490 1.1772 1.2052 -0.0965 -0.0369 -0.1558 92  THR   A CG2  
526  N  N    . PRO   A 66  ? 0.9268 1.1644 1.1923 -0.1210 -0.0305 -0.2065 93  PRO   A N    
527  C  CA   . PRO   A 66  ? 1.0403 1.2841 1.3471 -0.1366 -0.0140 -0.2216 93  PRO   A CA   
528  C  C    . PRO   A 66  ? 0.9404 1.1226 1.2448 -0.1446 0.0131  -0.2037 93  PRO   A C    
529  O  O    . PRO   A 66  ? 1.0287 1.2063 1.3708 -0.1607 0.0340  -0.2166 93  PRO   A O    
530  C  CB   . PRO   A 66  ? 1.0085 1.2907 1.3170 -0.1236 -0.0267 -0.2133 93  PRO   A CB   
531  C  CG   . PRO   A 66  ? 1.0140 1.3020 1.2822 -0.1011 -0.0466 -0.1902 93  PRO   A CG   
532  C  CD   . PRO   A 66  ? 1.0609 1.3271 1.3041 -0.1000 -0.0500 -0.1882 93  PRO   A CD   
533  N  N    . VAL   A 67  ? 0.7831 0.9209 1.0459 -0.1326 0.0144  -0.1745 94  VAL   A N    
534  C  CA   . VAL   A 67  ? 0.8857 0.9713 1.1368 -0.1328 0.0374  -0.1528 94  VAL   A CA   
535  C  C    . VAL   A 67  ? 0.8086 0.8530 1.0536 -0.1382 0.0516  -0.1521 94  VAL   A C    
536  O  O    . VAL   A 67  ? 0.9269 0.9703 1.1523 -0.1327 0.0379  -0.1536 94  VAL   A O    
537  C  CB   . VAL   A 67  ? 0.9108 0.9813 1.1217 -0.1131 0.0283  -0.1238 94  VAL   A CB   
538  C  CG1  . VAL   A 67  ? 0.9626 0.9859 1.1553 -0.1090 0.0498  -0.1027 94  VAL   A CG1  
539  C  CG2  . VAL   A 67  ? 0.8650 0.9722 1.0863 -0.1072 0.0177  -0.1242 94  VAL   A CG2  
540  N  N    . SER   A 68  ? 0.7864 0.7963 1.0493 -0.1477 0.0811  -0.1482 95  SER   A N    
541  C  CA   . SER   A 68  ? 0.7951 0.7588 1.0520 -0.1493 0.0995  -0.1412 95  SER   A CA   
542  C  C    . SER   A 68  ? 0.8894 0.8157 1.0975 -0.1287 0.1022  -0.1059 95  SER   A C    
543  O  O    . SER   A 68  ? 1.0258 0.9494 1.2194 -0.1194 0.1067  -0.0880 95  SER   A O    
544  C  CB   . SER   A 68  ? 0.8156 0.7580 1.1187 -0.1675 0.1342  -0.1511 95  SER   A CB   
545  O  OG   . SER   A 68  ? 0.8939 0.8779 1.2485 -0.1876 0.1309  -0.1896 95  SER   A OG   
546  N  N    . ARG   A 69  ? 0.9148 0.8164 1.0988 -0.1207 0.0991  -0.0983 96  ARG   A N    
547  C  CA   . ARG   A 69  ? 0.9009 0.7787 1.0385 -0.0992 0.0948  -0.0702 96  ARG   A CA   
548  C  C    . ARG   A 69  ? 0.9821 0.8165 1.1091 -0.0930 0.1137  -0.0575 96  ARG   A C    
549  O  O    . ARG   A 69  ? 0.8581 0.6807 1.0107 -0.1052 0.1244  -0.0726 96  ARG   A O    
550  C  CB   . ARG   A 69  ? 0.9544 0.8565 1.0664 -0.0891 0.0631  -0.0711 96  ARG   A CB   
551  C  CG   . ARG   A 69  ? 1.1523 1.0904 1.2670 -0.0876 0.0463  -0.0742 96  ARG   A CG   
552  C  CD   . ARG   A 69  ? 1.1348 1.0962 1.2342 -0.0800 0.0197  -0.0761 96  ARG   A CD   
553  N  NE   . ARG   A 69  ? 1.0638 1.0670 1.1821 -0.0843 0.0062  -0.0885 96  ARG   A NE   
554  C  CZ   . ARG   A 69  ? 1.1838 1.2029 1.3007 -0.0772 -0.0007 -0.0812 96  ARG   A CZ   
555  N  NH1  . ARG   A 69  ? 1.1293 1.1284 1.2274 -0.0667 0.0033  -0.0649 96  ARG   A NH1  
556  N  NH2  . ARG   A 69  ? 1.2086 1.2674 1.3438 -0.0789 -0.0121 -0.0917 96  ARG   A NH2  
557  N  N    . ILE   A 70  ? 0.9698 0.7830 1.0595 -0.0722 0.1176  -0.0306 97  ILE   A N    
558  C  CA   . ILE   A 70  ? 0.9053 0.6826 0.9746 -0.0584 0.1300  -0.0138 97  ILE   A CA   
559  C  C    . ILE   A 70  ? 0.9427 0.7228 0.9660 -0.0332 0.1155  0.0061  97  ILE   A C    
560  O  O    . ILE   A 70  ? 0.9693 0.7594 0.9780 -0.0238 0.1159  0.0166  97  ILE   A O    
561  C  CB   . ILE   A 70  ? 1.0246 0.7640 1.1115 -0.0597 0.1693  0.0003  97  ILE   A CB   
562  C  CG1  . ILE   A 70  ? 1.1300 0.8347 1.1848 -0.0357 0.1818  0.0270  97  ILE   A CG1  
563  C  CG2  . ILE   A 70  ? 1.0858 0.8305 1.1763 -0.0589 0.1846  0.0117  97  ILE   A CG2  
564  C  CD1  . ILE   A 70  ? 1.1532 0.8136 1.2325 -0.0381 0.2220  0.0389  97  ILE   A CD1  
565  N  N    . LEU   A 71  ? 0.9865 0.7614 0.9894 -0.0221 0.1026  0.0084  98  LEU   A N    
566  C  CA   . LEU   A 71  ? 0.8843 0.6674 0.8496 0.0009  0.0871  0.0214  98  LEU   A CA   
567  C  C    . LEU   A 71  ? 0.9958 0.7510 0.9363 0.0237  0.1073  0.0462  98  LEU   A C    
568  O  O    . LEU   A 71  ? 1.0756 0.8022 1.0238 0.0243  0.1248  0.0521  98  LEU   A O    
569  C  CB   . LEU   A 71  ? 0.8379 0.6360 0.7976 0.0011  0.0617  0.0096  98  LEU   A CB   
570  C  CG   . LEU   A 71  ? 0.8311 0.6475 0.7640 0.0193  0.0414  0.0139  98  LEU   A CG   
571  C  CD1  . LEU   A 71  ? 0.9516 0.7953 0.8905 0.0139  0.0272  0.0057  98  LEU   A CD1  
572  C  CD2  . LEU   A 71  ? 0.8029 0.6249 0.7330 0.0213  0.0252  0.0066  98  LEU   A CD2  
573  N  N    . ILE   A 72  ? 0.9906 0.7563 0.9018 0.0445  0.1055  0.0603  99  ILE   A N    
574  C  CA   . ILE   A 72  ? 0.9603 0.7091 0.8405 0.0730  0.1226  0.0864  99  ILE   A CA   
575  C  C    . ILE   A 72  ? 1.0505 0.8292 0.8968 0.0963  0.0978  0.0856  99  ILE   A C    
576  O  O    . ILE   A 72  ? 1.1156 0.9226 0.9596 0.0944  0.0816  0.0739  99  ILE   A O    
577  C  CB   . ILE   A 72  ? 0.9556 0.6907 0.8346 0.0781  0.1531  0.1059  99  ILE   A CB   
578  C  CG1  . ILE   A 72  ? 1.0413 0.7474 0.9631 0.0529  0.1802  0.1030  99  ILE   A CG1  
579  C  CG2  . ILE   A 72  ? 1.0717 0.7949 0.9119 0.1137  0.1705  0.1368  99  ILE   A CG2  
580  C  CD1  . ILE   A 72  ? 1.0135 0.7101 0.9452 0.0512  0.2105  0.1176  99  ILE   A CD1  
581  N  N    . GLY   A 73  ? 1.0021 0.7765 0.8261 0.1185  0.0951  0.0956  100 GLY   A N    
582  C  CA   . GLY   A 73  ? 0.9717 0.7799 0.7690 0.1405  0.0709  0.0899  100 GLY   A CA   
583  C  C    . GLY   A 73  ? 1.0878 0.8942 0.8614 0.1679  0.0696  0.1019  100 GLY   A C    
584  O  O    . GLY   A 73  ? 1.2441 1.0202 1.0095 0.1808  0.0944  0.1254  100 GLY   A O    
585  N  N    . ASN   A 74  ? 1.1536 0.9931 0.9196 0.1774  0.0419  0.0854  101 ASN   A N    
586  C  CA   . ASN   A 74  ? 1.0872 0.9347 0.8322 0.2052  0.0366  0.0930  101 ASN   A CA   
587  C  C    . ASN   A 74  ? 1.1060 0.9191 0.8673 0.1959  0.0476  0.0993  101 ASN   A C    
588  O  O    . ASN   A 74  ? 1.0789 0.8796 0.8705 0.1655  0.0446  0.0843  101 ASN   A O    
589  C  CB   . ASN   A 74  ? 1.0019 0.8939 0.7485 0.2102  0.0042  0.0670  101 ASN   A CB   
590  C  CG   . ASN   A 74  ? 1.0792 1.0107 0.8045 0.2303  -0.0065 0.0597  101 ASN   A CG   
591  O  OD1  . ASN   A 74  ? 1.1298 1.0574 0.8317 0.2455  0.0104  0.0778  101 ASN   A OD1  
592  N  ND2  . ASN   A 74  ? 1.0287 0.9997 0.7645 0.2306  -0.0333 0.0316  101 ASN   A ND2  
593  N  N    . PRO   A 75  ? 1.1015 0.9007 0.8432 0.2234  0.0609  0.1207  102 PRO   A N    
594  C  CA   . PRO   A 75  ? 0.9965 0.7640 0.7555 0.2163  0.0708  0.1238  102 PRO   A CA   
595  C  C    . PRO   A 75  ? 0.9287 0.7194 0.7048 0.2031  0.0431  0.0970  102 PRO   A C    
596  O  O    . PRO   A 75  ? 1.0279 0.8572 0.7928 0.2182  0.0201  0.0861  102 PRO   A O    
597  C  CB   . PRO   A 75  ? 1.1008 0.8580 0.8302 0.2567  0.0873  0.1536  102 PRO   A CB   
598  C  CG   . PRO   A 75  ? 1.0764 0.8450 0.7758 0.2788  0.0982  0.1730  102 PRO   A CG   
599  C  CD   . PRO   A 75  ? 1.2002 1.0118 0.9021 0.2647  0.0698  0.1450  102 PRO   A CD   
600  N  N    . GLY   A 76  ? 1.0050 0.7746 0.8105 0.1748  0.0464  0.0850  103 GLY   A N    
601  C  CA   . GLY   A 76  ? 1.0046 0.7928 0.8269 0.1618  0.0251  0.0629  103 GLY   A CA   
602  C  C    . GLY   A 76  ? 1.0693 0.8853 0.9073 0.1390  0.0045  0.0411  103 GLY   A C    
603  O  O    . GLY   A 76  ? 1.0145 0.8448 0.8686 0.1272  -0.0100 0.0251  103 GLY   A O    
604  N  N    . CYS   A 77  ? 0.9576 0.7811 0.7925 0.1337  0.0048  0.0415  104 CYS   A N    
605  C  CA   . CYS   A 77  ? 0.8935 0.7410 0.7448 0.1145  -0.0126 0.0231  104 CYS   A CA   
606  C  C    . CYS   A 77  ? 0.8823 0.7157 0.7579 0.0855  -0.0071 0.0156  104 CYS   A C    
607  O  O    . CYS   A 77  ? 1.0670 0.8730 0.9485 0.0784  0.0112  0.0218  104 CYS   A O    
608  C  CB   . CYS   A 77  ? 0.9010 0.7645 0.7403 0.1221  -0.0146 0.0247  104 CYS   A CB   
609  S  SG   . CYS   A 77  ? 1.0814 0.9827 0.9378 0.1126  -0.0395 0.0011  104 CYS   A SG   
610  N  N    . THR   A 78  ? 0.9347 0.7891 0.8270 0.0700  -0.0224 0.0011  105 THR   A N    
611  C  CA   . THR   A 78  ? 0.8367 0.6885 0.7491 0.0464  -0.0205 -0.0066 105 THR   A CA   
612  C  C    . THR   A 78  ? 0.8490 0.7225 0.7714 0.0382  -0.0317 -0.0133 105 THR   A C    
613  O  O    . THR   A 78  ? 0.8626 0.7537 0.7829 0.0471  -0.0433 -0.0169 105 THR   A O    
614  C  CB   . THR   A 78  ? 0.7733 0.6280 0.6978 0.0373  -0.0254 -0.0155 105 THR   A CB   
615  O  OG1  . THR   A 78  ? 0.6817 0.5591 0.6101 0.0413  -0.0413 -0.0211 105 THR   A OG1  
616  C  CG2  . THR   A 78  ? 0.8450 0.6768 0.7638 0.0451  -0.0132 -0.0111 105 THR   A CG2  
617  N  N    . TYR   A 79  ? 0.8929 0.7666 0.8293 0.0217  -0.0278 -0.0168 106 TYR   A N    
618  C  CA   . TYR   A 79  ? 0.8056 0.6984 0.7543 0.0140  -0.0365 -0.0216 106 TYR   A CA   
619  C  C    . TYR   A 79  ? 0.8800 0.7828 0.8453 -0.0012 -0.0392 -0.0281 106 TYR   A C    
620  O  O    . TYR   A 79  ? 0.9104 0.8062 0.8814 -0.0105 -0.0302 -0.0318 106 TYR   A O    
621  C  CB   . TYR   A 79  ? 0.8002 0.6896 0.7460 0.0146  -0.0280 -0.0175 106 TYR   A CB   
622  C  CG   . TYR   A 79  ? 0.9164 0.8243 0.8769 0.0076  -0.0355 -0.0224 106 TYR   A CG   
623  C  CD1  . TYR   A 79  ? 0.8738 0.7962 0.8383 0.0141  -0.0472 -0.0265 106 TYR   A CD1  
624  C  CD2  . TYR   A 79  ? 0.8268 0.7390 0.8013 -0.0049 -0.0300 -0.0246 106 TYR   A CD2  
625  C  CE1  . TYR   A 79  ? 0.8508 0.7866 0.8317 0.0091  -0.0516 -0.0298 106 TYR   A CE1  
626  C  CE2  . TYR   A 79  ? 0.7974 0.7273 0.7855 -0.0085 -0.0364 -0.0274 106 TYR   A CE2  
627  C  CZ   . TYR   A 79  ? 0.8627 0.8019 0.8534 -0.0010 -0.0463 -0.0286 106 TYR   A CZ   
628  O  OH   . TYR   A 79  ? 0.8578 0.8112 0.8650 -0.0032 -0.0504 -0.0304 106 TYR   A OH   
629  N  N    . LYS   A 80  ? 0.9548 0.8759 0.9298 -0.0027 -0.0504 -0.0302 107 LYS   A N    
630  C  CA   . LYS   A 80  ? 0.8521 0.7889 0.8380 -0.0115 -0.0537 -0.0336 107 LYS   A CA   
631  C  C    . LYS   A 80  ? 0.7746 0.7286 0.7729 -0.0148 -0.0577 -0.0318 107 LYS   A C    
632  O  O    . LYS   A 80  ? 0.9202 0.8780 0.9248 -0.0098 -0.0620 -0.0279 107 LYS   A O    
633  C  CB   . LYS   A 80  ? 0.7399 0.6841 0.7268 -0.0077 -0.0595 -0.0326 107 LYS   A CB   
634  C  CG   . LYS   A 80  ? 0.6965 0.6602 0.6888 -0.0128 -0.0615 -0.0342 107 LYS   A CG   
635  C  CD   . LYS   A 80  ? 0.6206 0.5878 0.6105 -0.0087 -0.0628 -0.0335 107 LYS   A CD   
636  C  CE   . LYS   A 80  ? 0.7531 0.7412 0.7418 -0.0116 -0.0631 -0.0375 107 LYS   A CE   
637  N  NZ   . LYS   A 80  ? 0.9628 0.9619 0.9520 -0.0059 -0.0636 -0.0315 107 LYS   A NZ   
638  N  N    . TYR   A 81  ? 0.9062 0.8726 0.9112 -0.0227 -0.0559 -0.0367 108 TYR   A N    
639  C  CA   . TYR   A 81  ? 1.0003 0.9882 1.0175 -0.0236 -0.0601 -0.0345 108 TYR   A CA   
640  C  C    . TYR   A 81  ? 0.9203 0.9339 0.9424 -0.0281 -0.0629 -0.0418 108 TYR   A C    
641  O  O    . TYR   A 81  ? 0.9860 0.9986 1.0088 -0.0359 -0.0585 -0.0545 108 TYR   A O    
642  C  CB   . TYR   A 81  ? 0.9589 0.9419 0.9811 -0.0259 -0.0551 -0.0357 108 TYR   A CB   
643  C  CG   . TYR   A 81  ? 1.0064 0.9911 1.0348 -0.0361 -0.0471 -0.0459 108 TYR   A CG   
644  C  CD1  . TYR   A 81  ? 1.0026 0.9627 1.0249 -0.0395 -0.0357 -0.0487 108 TYR   A CD1  
645  C  CD2  . TYR   A 81  ? 1.1464 1.1583 1.1905 -0.0414 -0.0497 -0.0531 108 TYR   A CD2  
646  C  CE1  . TYR   A 81  ? 1.1680 1.1267 1.2040 -0.0506 -0.0246 -0.0592 108 TYR   A CE1  
647  C  CE2  . TYR   A 81  ? 1.1223 1.1390 1.1800 -0.0528 -0.0416 -0.0669 108 TYR   A CE2  
648  C  CZ   . TYR   A 81  ? 1.2350 1.2229 1.2908 -0.0586 -0.0279 -0.0703 108 TYR   A CZ   
649  O  OH   . TYR   A 81  ? 1.3256 1.3153 1.4027 -0.0717 -0.0162 -0.0852 108 TYR   A OH   
650  N  N    . LEU   A 82  ? 0.8124 0.8505 0.8392 -0.0219 -0.0691 -0.0342 109 LEU   A N    
651  C  CA   . LEU   A 82  ? 0.7587 0.8317 0.7868 -0.0209 -0.0739 -0.0401 109 LEU   A CA   
652  C  C    . LEU   A 82  ? 0.7933 0.8682 0.8121 -0.0238 -0.0735 -0.0511 109 LEU   A C    
653  O  O    . LEU   A 82  ? 0.9614 1.0543 0.9841 -0.0302 -0.0742 -0.0697 109 LEU   A O    
654  C  CB   . LEU   A 82  ? 0.8071 0.8999 0.8479 -0.0273 -0.0745 -0.0530 109 LEU   A CB   
655  C  CG   . LEU   A 82  ? 1.0404 1.1367 1.0919 -0.0232 -0.0749 -0.0436 109 LEU   A CG   
656  C  CD1  . LEU   A 82  ? 0.9392 1.0587 1.0063 -0.0305 -0.0748 -0.0590 109 LEU   A CD1  
657  C  CD2  . LEU   A 82  ? 0.8753 0.9897 0.9271 -0.0086 -0.0797 -0.0251 109 LEU   A CD2  
658  N  N    . ASN   A 83  ? 0.8127 0.8701 0.8225 -0.0193 -0.0719 -0.0422 110 ASN   A N    
659  C  CA   . ASN   A 83  ? 0.8058 0.8647 0.8065 -0.0195 -0.0710 -0.0503 110 ASN   A CA   
660  C  C    . ASN   A 83  ? 0.7704 0.8116 0.7731 -0.0300 -0.0653 -0.0691 110 ASN   A C    
661  O  O    . ASN   A 83  ? 1.0497 1.0996 1.0504 -0.0323 -0.0644 -0.0836 110 ASN   A O    
662  C  CB   . ASN   A 83  ? 0.8718 0.9720 0.8676 -0.0127 -0.0761 -0.0524 110 ASN   A CB   
663  C  CG   . ASN   A 83  ? 1.1837 1.2991 1.1789 0.0002  -0.0774 -0.0288 110 ASN   A CG   
664  O  OD1  . ASN   A 83  ? 1.2390 1.3751 1.2397 0.0054  -0.0805 -0.0225 110 ASN   A OD1  
665  N  ND2  . ASN   A 83  ? 1.3069 1.4118 1.2987 0.0061  -0.0730 -0.0150 110 ASN   A ND2  
666  N  N    . THR   A 84  ? 0.7609 0.7766 0.7687 -0.0353 -0.0592 -0.0689 111 THR   A N    
667  C  CA   . THR   A 84  ? 0.7429 0.7356 0.7559 -0.0438 -0.0487 -0.0817 111 THR   A CA   
668  C  C    . THR   A 84  ? 0.8696 0.8258 0.8733 -0.0386 -0.0417 -0.0685 111 THR   A C    
669  O  O    . THR   A 84  ? 0.8742 0.8239 0.8772 -0.0361 -0.0412 -0.0589 111 THR   A O    
670  C  CB   . THR   A 84  ? 0.8454 0.8489 0.8769 -0.0548 -0.0442 -0.0952 111 THR   A CB   
671  O  OG1  . THR   A 84  ? 0.8566 0.9036 0.8957 -0.0562 -0.0537 -0.1091 111 THR   A OG1  
672  C  CG2  . THR   A 84  ? 0.7262 0.7031 0.7697 -0.0647 -0.0287 -0.1085 111 THR   A CG2  
673  N  N    . ARG   A 85  ? 0.7124 0.6485 0.7084 -0.0348 -0.0367 -0.0689 112 ARG   A N    
674  C  CA   . ARG   A 85  ? 0.8462 0.7534 0.8308 -0.0256 -0.0308 -0.0567 112 ARG   A CA   
675  C  C    . ARG   A 85  ? 0.7500 0.6311 0.7397 -0.0296 -0.0140 -0.0578 112 ARG   A C    
676  O  O    . ARG   A 85  ? 0.9210 0.7932 0.9228 -0.0375 -0.0039 -0.0701 112 ARG   A O    
677  C  CB   . ARG   A 85  ? 0.7473 0.6473 0.7227 -0.0169 -0.0325 -0.0551 112 ARG   A CB   
678  C  CG   . ARG   A 85  ? 0.7559 0.6371 0.7181 -0.0029 -0.0307 -0.0428 112 ARG   A CG   
679  C  CD   . ARG   A 85  ? 0.7283 0.6080 0.6848 0.0061  -0.0335 -0.0430 112 ARG   A CD   
680  N  NE   . ARG   A 85  ? 0.8574 0.7620 0.8186 0.0058  -0.0454 -0.0438 112 ARG   A NE   
681  C  CZ   . ARG   A 85  ? 0.8202 0.7351 0.7834 0.0116  -0.0535 -0.0383 112 ARG   A CZ   
682  N  NH1  . ARG   A 85  ? 0.7020 0.6097 0.6591 0.0196  -0.0542 -0.0340 112 ARG   A NH1  
683  N  NH2  . ARG   A 85  ? 0.6927 0.6269 0.6660 0.0099  -0.0596 -0.0380 112 ARG   A NH2  
684  N  N    . LEU   A 86  ? 0.8676 0.7373 0.8507 -0.0239 -0.0092 -0.0457 113 LEU   A N    
685  C  CA   . LEU   A 86  ? 0.8331 0.6761 0.8194 -0.0246 0.0107  -0.0406 113 LEU   A CA   
686  C  C    . LEU   A 86  ? 0.8498 0.6681 0.8153 -0.0062 0.0181  -0.0246 113 LEU   A C    
687  O  O    . LEU   A 86  ? 0.8799 0.7077 0.8280 0.0076  0.0061  -0.0169 113 LEU   A O    
688  C  CB   . LEU   A 86  ? 0.8536 0.7034 0.8446 -0.0280 0.0139  -0.0365 113 LEU   A CB   
689  C  CG   . LEU   A 86  ? 1.0258 0.8908 1.0440 -0.0463 0.0178  -0.0519 113 LEU   A CG   
690  C  CD1  . LEU   A 86  ? 1.0503 0.9461 1.0784 -0.0542 0.0018  -0.0685 113 LEU   A CD1  
691  C  CD2  . LEU   A 86  ? 0.9205 0.7972 0.9414 -0.0468 0.0176  -0.0466 113 LEU   A CD2  
692  N  N    . PHE   A 87  ? 0.8394 0.6279 0.8098 -0.0050 0.0388  -0.0207 114 PHE   A N    
693  C  CA   . PHE   A 87  ? 0.8744 0.6390 0.8250 0.0159  0.0486  -0.0030 114 PHE   A CA   
694  C  C    . PHE   A 87  ? 0.9685 0.7130 0.9116 0.0251  0.0692  0.0158  114 PHE   A C    
695  O  O    . PHE   A 87  ? 1.0379 0.7675 1.0026 0.0113  0.0883  0.0135  114 PHE   A O    
696  C  CB   . PHE   A 87  ? 0.9389 0.6812 0.9007 0.0145  0.0602  -0.0087 114 PHE   A CB   
697  C  CG   . PHE   A 87  ? 0.9395 0.7036 0.9068 0.0071  0.0421  -0.0267 114 PHE   A CG   
698  C  CD1  . PHE   A 87  ? 0.9256 0.7064 0.9154 -0.0135 0.0382  -0.0489 114 PHE   A CD1  
699  C  CD2  . PHE   A 87  ? 0.8728 0.6456 0.8231 0.0222  0.0292  -0.0220 114 PHE   A CD2  
700  C  CE1  . PHE   A 87  ? 0.8776 0.6817 0.8685 -0.0171 0.0232  -0.0631 114 PHE   A CE1  
701  C  CE2  . PHE   A 87  ? 0.8433 0.6366 0.7990 0.0162  0.0155  -0.0364 114 PHE   A CE2  
702  C  CZ   . PHE   A 87  ? 0.9024 0.7107 0.8762 -0.0027 0.0131  -0.0555 114 PHE   A CZ   
703  N  N    . THR   A 88  ? 1.0092 0.7567 0.9230 0.0490  0.0659  0.0332  115 THR   A N    
704  C  CA   . THR   A 88  ? 0.9927 0.7292 0.8927 0.0618  0.0836  0.0528  115 THR   A CA   
705  C  C    . THR   A 88  ? 1.0800 0.7756 0.9838 0.0698  0.1164  0.0714  115 THR   A C    
706  O  O    . THR   A 88  ? 1.1974 0.8759 1.0953 0.0828  0.1216  0.0784  115 THR   A O    
707  C  CB   . THR   A 88  ? 1.0977 0.8562 0.9635 0.0885  0.0695  0.0630  115 THR   A CB   
708  O  OG1  . THR   A 88  ? 1.0025 0.7479 0.8476 0.1142  0.0767  0.0794  115 THR   A OG1  
709  C  CG2  . THR   A 88  ? 1.0867 0.8804 0.9548 0.0823  0.0386  0.0433  115 THR   A CG2  
710  N  N    . VAL   A 89  ? 1.0693 0.7485 0.9863 0.0623  0.1405  0.0799  116 VAL   A N    
711  C  CA   . VAL   A 89  ? 1.1976 0.8383 1.1122 0.0774  0.1766  0.1071  116 VAL   A CA   
712  C  C    . VAL   A 89  ? 1.2249 0.8781 1.0927 0.1133  0.1738  0.1328  116 VAL   A C    
713  O  O    . VAL   A 89  ? 1.2711 0.9516 1.1233 0.1169  0.1628  0.1321  116 VAL   A O    
714  C  CB   . VAL   A 89  ? 1.1148 0.7377 1.0621 0.0572  0.2048  0.1074  116 VAL   A CB   
715  C  CG1  . VAL   A 89  ? 1.2430 0.8206 1.1926 0.0730  0.2476  0.1386  116 VAL   A CG1  
716  C  CG2  . VAL   A 89  ? 1.1013 0.7270 1.0954 0.0219  0.2003  0.0738  116 VAL   A CG2  
717  N  N    . PRO   A 90  ? 1.2330 0.8712 1.0776 0.1421  0.1823  0.1540  117 PRO   A N    
718  C  CA   . PRO   A 90  ? 1.2199 0.8849 1.0178 0.1787  0.1703  0.1709  117 PRO   A CA   
719  C  C    . PRO   A 90  ? 1.2490 0.9100 1.0251 0.1981  0.1948  0.1986  117 PRO   A C    
720  O  O    . PRO   A 90  ? 1.3226 0.9451 1.1144 0.1954  0.2321  0.2192  117 PRO   A O    
721  C  CB   . PRO   A 90  ? 1.2245 0.8735 1.0089 0.2041  0.1755  0.1860  117 PRO   A CB   
722  C  CG   . PRO   A 90  ? 1.2092 0.8067 1.0293 0.1878  0.2084  0.1923  117 PRO   A CG   
723  C  CD   . PRO   A 90  ? 1.1896 0.7869 1.0512 0.1446  0.2050  0.1630  117 PRO   A CD   
724  N  N    . TRP   A 91  ? 1.2517 0.9546 0.9940 0.2179  0.1748  0.1975  118 TRP   A N    
725  C  CA   . TRP   A 91  ? 1.3971 1.1048 1.1079 0.2453  0.1957  0.2254  118 TRP   A CA   
726  C  C    . TRP   A 91  ? 1.4434 1.1722 1.1061 0.2932  0.1909  0.2464  118 TRP   A C    
727  O  O    . TRP   A 91  ? 1.4282 1.1853 1.0819 0.3017  0.1603  0.2287  118 TRP   A O    
728  C  CB   . TRP   A 91  ? 1.3215 1.0646 1.0290 0.2350  0.1803  0.2079  118 TRP   A CB   
729  C  CG   . TRP   A 91  ? 1.1807 0.9711 0.8824 0.2321  0.1371  0.1750  118 TRP   A CG   
730  C  CD1  . TRP   A 91  ? 1.1786 0.9937 0.8654 0.2485  0.1112  0.1642  118 TRP   A CD1  
731  C  CD2  . TRP   A 91  ? 1.1177 0.9353 0.8339 0.2111  0.1176  0.1485  118 TRP   A CD2  
732  N  NE1  . TRP   A 91  ? 1.2298 1.0841 0.9241 0.2375  0.0784  0.1320  118 TRP   A NE1  
733  C  CE2  . TRP   A 91  ? 1.1291 0.9839 0.8405 0.2153  0.0821  0.1230  118 TRP   A CE2  
734  C  CE3  . TRP   A 91  ? 1.1754 0.9898 0.9114 0.1897  0.1280  0.1438  118 TRP   A CE3  
735  C  CZ2  . TRP   A 91  ? 1.1337 1.0178 0.8603 0.1991  0.0590  0.0947  118 TRP   A CZ2  
736  C  CZ3  . TRP   A 91  ? 1.1195 0.9655 0.8669 0.1755  0.1028  0.1162  118 TRP   A CZ3  
737  C  CH2  . TRP   A 91  ? 1.1601 1.0383 0.9031 0.1803  0.0697  0.0928  118 TRP   A CH2  
738  N  N    . PRO   A 92  ? 1.5891 1.3069 1.2214 0.3267  0.2220  0.2849  119 PRO   A N    
739  C  CA   . PRO   A 92  ? 1.6705 1.4068 1.2568 0.3768  0.2211  0.3094  119 PRO   A CA   
740  C  C    . PRO   A 92  ? 1.6960 1.5012 1.2456 0.4014  0.1827  0.2889  119 PRO   A C    
741  O  O    . PRO   A 92  ? 1.8387 1.6740 1.3541 0.4265  0.1870  0.2997  119 PRO   A O    
742  C  CB   . PRO   A 92  ? 1.6755 1.3820 1.2405 0.4048  0.2688  0.3582  119 PRO   A CB   
743  C  CG   . PRO   A 92  ? 1.6545 1.3107 1.2700 0.3621  0.2986  0.3575  119 PRO   A CG   
744  C  CD   . PRO   A 92  ? 1.6461 1.3306 1.2879 0.3217  0.2638  0.3111  119 PRO   A CD   
745  N  N    . VAL   A 93  ? 1.7272 1.5596 1.2863 0.3946  0.1465  0.2577  120 VAL   A N    
746  C  CA   . VAL   A 93  ? 1.8441 1.7422 1.3729 0.4234  0.1121  0.2382  120 VAL   A CA   
747  C  C    . VAL   A 93  ? 1.8753 1.7816 1.3717 0.4696  0.1169  0.2640  120 VAL   A C    
748  O  O    . VAL   A 93  ? 1.8363 1.6995 1.3481 0.4668  0.1333  0.2812  120 VAL   A O    
749  C  CB   . VAL   A 93  ? 1.8555 1.7804 1.4178 0.3910  0.0728  0.1900  120 VAL   A CB   
750  C  CG1  . VAL   A 93  ? 1.7531 1.6500 1.3438 0.3743  0.0690  0.1851  120 VAL   A CG1  
751  C  CG2  . VAL   A 93  ? 1.9249 1.9205 1.4649 0.4168  0.0390  0.1636  120 VAL   A CG2  
752  N  N    . LYS   A 94  ? 1.8637 1.8278 1.3155 0.5142  0.1030  0.2662  121 LYS   A N    
753  C  CA   . LYS   A 94  ? 1.9305 1.9095 1.3456 0.5658  0.1099  0.2953  121 LYS   A CA   
754  C  C    . LYS   A 94  ? 2.0469 2.0219 1.4849 0.5602  0.0914  0.2809  121 LYS   A C    
755  O  O    . LYS   A 94  ? 1.9482 1.9509 1.4151 0.5334  0.0573  0.2370  121 LYS   A O    
756  C  CB   . LYS   A 94  ? 1.7743 1.8342 1.1609 0.5996  0.0904  0.2758  121 LYS   A CB   
757  N  N    . GLY   A 95  ? 1.8580 1.7996 1.2963 0.5772  0.1180  0.3114  122 GLY   A N    
758  C  CA   . GLY   A 95  ? 1.8533 1.7872 1.3110 0.5760  0.1055  0.3029  122 GLY   A CA   
759  C  C    . GLY   A 95  ? 1.7890 1.6693 1.2944 0.5258  0.1067  0.2879  122 GLY   A C    
760  O  O    . GLY   A 95  ? 1.7880 1.6170 1.3144 0.4956  0.1331  0.2981  122 GLY   A O    
761  N  N    . GLU   A 102 ? 1.7692 1.0325 1.9886 0.0676  0.5986  0.2633  129 GLU   A N    
762  C  CA   . GLU   A 102 ? 1.8036 1.0846 1.9543 0.0886  0.5582  0.2736  129 GLU   A CA   
763  C  C    . GLU   A 102 ? 1.9084 1.2014 1.9928 0.1318  0.5634  0.3220  129 GLU   A C    
764  O  O    . GLU   A 102 ? 2.0222 1.3374 2.0462 0.1534  0.5310  0.3326  129 GLU   A O    
765  C  CB   . GLU   A 102 ? 1.7607 1.0297 1.9009 0.1005  0.5430  0.2681  129 GLU   A CB   
766  C  CG   . GLU   A 102 ? 1.7875 1.0754 1.8935 0.0975  0.4952  0.2480  129 GLU   A CG   
767  C  CD   . GLU   A 102 ? 1.8592 1.1587 1.8908 0.1439  0.4756  0.2827  129 GLU   A CD   
768  O  OE1  . GLU   A 102 ? 1.8069 1.1044 1.8102 0.1790  0.4977  0.3221  129 GLU   A OE1  
769  O  OE2  . GLU   A 102 ? 1.7727 1.1152 1.7771 0.1434  0.4277  0.2582  129 GLU   A OE2  
770  N  N    . ALA   A 103 ? 1.8433 1.1250 1.9405 0.1458  0.6044  0.3492  130 ALA   A N    
771  C  CA   . ALA   A 103 ? 1.7485 1.0469 1.7868 0.1875  0.6128  0.3925  130 ALA   A CA   
772  C  C    . ALA   A 103 ? 1.8052 1.1278 1.8354 0.1747  0.6073  0.3891  130 ALA   A C    
773  O  O    . ALA   A 103 ? 1.8225 1.1747 1.7897 0.2026  0.5886  0.4092  130 ALA   A O    
774  C  CB   . ALA   A 103 ? 1.6596 0.9347 1.7142 0.2124  0.6618  0.4256  130 ALA   A CB   
775  N  N    . GLU   A 104 ? 1.7734 1.0885 1.8681 0.1335  0.6228  0.3616  131 GLU   A N    
776  C  CA   . GLU   A 104 ? 1.6130 0.9539 1.7060 0.1157  0.6137  0.3520  131 GLU   A CA   
777  C  C    . GLU   A 104 ? 1.6820 1.0475 1.7441 0.1032  0.5663  0.3299  131 GLU   A C    
778  O  O    . GLU   A 104 ? 1.6180 1.0214 1.6456 0.1085  0.5458  0.3300  131 GLU   A O    
779  C  CB   . GLU   A 104 ? 1.5864 0.9193 1.7619 0.0729  0.6374  0.3209  131 GLU   A CB   
780  C  CG   . GLU   A 104 ? 1.7120 1.0316 1.9111 0.0850  0.6847  0.3463  131 GLU   A CG   
781  C  CD   . GLU   A 104 ? 1.7327 1.0466 2.0191 0.0426  0.7064  0.3104  131 GLU   A CD   
782  O  OE1  . GLU   A 104 ? 1.5410 0.8802 1.8531 0.0076  0.6827  0.2730  131 GLU   A OE1  
783  O  OE2  . GLU   A 104 ? 1.7987 1.0854 2.1297 0.0453  0.7473  0.3184  131 GLU   A OE2  
784  N  N    . ILE   A 105 ? 1.6821 1.0408 1.7580 0.0884  0.5414  0.3023  132 ILE   A N    
785  C  CA   . ILE   A 105 ? 1.4636 0.8752 1.5158 0.0784  0.4809  0.2644  132 ILE   A CA   
786  C  C    . ILE   A 105 ? 1.5786 1.0185 1.5537 0.1204  0.4520  0.2868  132 ILE   A C    
787  O  O    . ILE   A 105 ? 1.5350 1.0236 1.4795 0.1220  0.4140  0.2711  132 ILE   A O    
788  C  CB   . ILE   A 105 ? 1.5095 0.9136 1.6006 0.0519  0.4627  0.2256  132 ILE   A CB   
789  C  CG1  . ILE   A 105 ? 1.5841 0.9618 1.7561 0.0125  0.4948  0.2008  132 ILE   A CG1  
790  C  CG2  . ILE   A 105 ? 1.3764 0.8348 1.4469 0.0407  0.4043  0.1888  132 ILE   A CG2  
791  C  CD1  . ILE   A 105 ? 1.3771 0.7996 1.5812 -0.0234 0.4679  0.1561  132 ILE   A CD1  
792  N  N    . ALA   A 106 ? 1.6484 1.0605 1.5944 0.1555  0.4693  0.3213  133 ALA   A N    
793  C  CA   . ALA   A 106 ? 1.5542 0.9985 1.4287 0.1991  0.4444  0.3425  133 ALA   A CA   
794  C  C    . ALA   A 106 ? 1.4393 0.9160 1.2765 0.2171  0.4460  0.3597  133 ALA   A C    
795  O  O    . ALA   A 106 ? 1.5518 1.0794 1.3501 0.2275  0.4053  0.3443  133 ALA   A O    
796  C  CB   . ALA   A 106 ? 1.6529 1.0608 1.5044 0.2385  0.4722  0.3841  133 ALA   A CB   
797  N  N    . ALA   A 107 ? 1.5838 1.0320 1.4375 0.2189  0.4940  0.3886  134 ALA   A N    
798  C  CA   . ALA   A 107 ? 1.6875 1.1655 1.5066 0.2374  0.5009  0.4070  134 ALA   A CA   
799  C  C    . ALA   A 107 ? 1.5921 1.1179 1.4200 0.2083  0.4615  0.3640  134 ALA   A C    
800  O  O    . ALA   A 107 ? 1.5923 1.1612 1.3757 0.2291  0.4427  0.3662  134 ALA   A O    
801  C  CB   . ALA   A 107 ? 1.5909 1.0359 1.4443 0.2355  0.5569  0.4338  134 ALA   A CB   
802  N  N    . ALA   A 108 ? 1.5190 1.0402 1.4041 0.1623  0.4490  0.3243  135 ALA   A N    
803  C  CA   . ALA   A 108 ? 1.4746 1.0411 1.3683 0.1373  0.4107  0.2852  135 ALA   A CA   
804  C  C    . ALA   A 108 ? 1.5222 1.1302 1.3728 0.1519  0.3587  0.2667  135 ALA   A C    
805  O  O    . ALA   A 108 ? 1.4164 1.0666 1.2452 0.1554  0.3326  0.2528  135 ALA   A O    
806  C  CB   . ALA   A 108 ? 1.4063 0.9630 1.3689 0.0894  0.4087  0.2479  135 ALA   A CB   
807  N  N    . CYS   A 109 ? 1.5211 1.1177 1.3627 0.1605  0.3450  0.2652  136 CYS   A N    
808  C  CA   . CYS   A 109 ? 1.4571 1.0925 1.2635 0.1739  0.2986  0.2474  136 CYS   A CA   
809  C  C    . CYS   A 109 ? 1.5181 1.1843 1.2645 0.2173  0.2931  0.2694  136 CYS   A C    
810  O  O    . CYS   A 109 ? 1.4142 1.1254 1.1385 0.2227  0.2567  0.2478  136 CYS   A O    
811  C  CB   . CYS   A 109 ? 1.3983 1.0144 1.2106 0.1749  0.2894  0.2427  136 CYS   A CB   
812  S  SG   . CYS   A 109 ? 1.2606 0.8523 1.1400 0.1260  0.2889  0.2085  136 CYS   A SG   
813  N  N    . GLU   A 110 ? 1.4348 1.0793 1.1555 0.2501  0.3297  0.3116  137 GLU   A N    
814  C  CA   . GLU   A 110 ? 1.4704 1.1509 1.1317 0.2943  0.3267  0.3326  137 GLU   A CA   
815  C  C    . GLU   A 110 ? 1.4297 1.1440 1.0877 0.2856  0.3199  0.3185  137 GLU   A C    
816  O  O    . GLU   A 110 ? 1.4141 1.1777 1.0344 0.3069  0.2921  0.3065  137 GLU   A O    
817  C  CB   . GLU   A 110 ? 1.5870 1.2363 1.2224 0.3322  0.3737  0.3858  137 GLU   A CB   
818  C  CG   . GLU   A 110 ? 1.8725 1.4627 1.5408 0.3245  0.4030  0.4035  137 GLU   A CG   
819  C  CD   . GLU   A 110 ? 2.0922 1.6530 1.7323 0.3684  0.4485  0.4592  137 GLU   A CD   
820  O  OE1  . GLU   A 110 ? 2.0948 1.6890 1.6902 0.4101  0.4319  0.4690  137 GLU   A OE1  
821  O  OE2  . GLU   A 110 ? 2.0538 1.5791 1.7366 0.3546  0.4908  0.4726  137 GLU   A OE2  
822  N  N    . THR   A 111 ? 1.4105 1.1011 1.1114 0.2543  0.3452  0.3168  138 THR   A N    
823  C  CA   . THR   A 111 ? 1.4144 1.1357 1.1175 0.2445  0.3407  0.3030  138 THR   A CA   
824  C  C    . THR   A 111 ? 1.3849 1.1486 1.0914 0.2279  0.2898  0.2584  138 THR   A C    
825  O  O    . THR   A 111 ? 1.3736 1.1793 1.0520 0.2434  0.2719  0.2480  138 THR   A O    
826  C  CB   . THR   A 111 ? 1.4126 1.1023 1.1715 0.2092  0.3743  0.3035  138 THR   A CB   
827  O  OG1  . THR   A 111 ? 1.5554 1.2057 1.3130 0.2267  0.4272  0.3478  138 THR   A OG1  
828  C  CG2  . THR   A 111 ? 1.3843 1.1084 1.1503 0.1969  0.3662  0.2853  138 THR   A CG2  
829  N  N    . PHE   A 112 ? 1.2410 0.9944 0.9828 0.1977  0.2675  0.2317  139 PHE   A N    
830  C  CA   . PHE   A 112 ? 1.2414 1.0302 0.9913 0.1816  0.2237  0.1931  139 PHE   A CA   
831  C  C    . PHE   A 112 ? 1.2937 1.1141 1.0043 0.2091  0.1923  0.1852  139 PHE   A C    
832  O  O    . PHE   A 112 ? 1.2894 1.1442 1.0014 0.2032  0.1598  0.1560  139 PHE   A O    
833  C  CB   . PHE   A 112 ? 1.0944 0.8656 0.8931 0.1429  0.2125  0.1694  139 PHE   A CB   
834  C  CG   . PHE   A 112 ? 1.0635 0.8211 0.9073 0.1123  0.2331  0.1636  139 PHE   A CG   
835  C  CD1  . PHE   A 112 ? 1.1009 0.8870 0.9576 0.0993  0.2213  0.1452  139 PHE   A CD1  
836  C  CD2  . PHE   A 112 ? 1.2249 0.9428 1.1018 0.0972  0.2653  0.1749  139 PHE   A CD2  
837  C  CE1  . PHE   A 112 ? 1.0885 0.8678 0.9886 0.0725  0.2394  0.1384  139 PHE   A CE1  
838  C  CE2  . PHE   A 112 ? 1.2411 0.9519 1.1651 0.0684  0.2841  0.1652  139 PHE   A CE2  
839  C  CZ   . PHE   A 112 ? 1.1842 0.9277 1.1188 0.0565  0.2703  0.1471  139 PHE   A CZ   
840  N  N    . LEU   A 113 ? 1.2828 1.0932 0.9624 0.2393  0.2021  0.2096  140 LEU   A N    
841  C  CA   . LEU   A 113 ? 1.2520 1.1026 0.8906 0.2723  0.1751  0.2031  140 LEU   A CA   
842  C  C    . LEU   A 113 ? 1.2387 1.1290 0.8406 0.2998  0.1759  0.2063  140 LEU   A C    
843  O  O    . LEU   A 113 ? 1.2192 1.1558 0.8064 0.3104  0.1443  0.1792  140 LEU   A O    
844  C  CB   . LEU   A 113 ? 1.3226 1.1555 0.9365 0.3014  0.1869  0.2306  140 LEU   A CB   
845  C  CG   . LEU   A 113 ? 1.2953 1.1695 0.8747 0.3338  0.1568  0.2210  140 LEU   A CG   
846  C  CD1  . LEU   A 113 ? 1.4003 1.3163 0.9261 0.3802  0.1600  0.2363  140 LEU   A CD1  
847  C  CD2  . LEU   A 113 ? 1.1429 1.0478 0.7464 0.3097  0.1148  0.1755  140 LEU   A CD2  
848  N  N    . LYS   A 114 ? 1.2979 1.1717 0.8881 0.3111  0.2136  0.2376  141 LYS   A N    
849  C  CA   . LYS   A 114 ? 1.4203 1.3326 0.9750 0.3376  0.2180  0.2417  141 LYS   A CA   
850  C  C    . LYS   A 114 ? 1.3234 1.2613 0.9041 0.3106  0.1960  0.2041  141 LYS   A C    
851  O  O    . LYS   A 114 ? 1.3046 1.2904 0.8610 0.3291  0.1756  0.1842  141 LYS   A O    
852  C  CB   . LYS   A 114 ? 1.3819 1.2656 0.9244 0.3524  0.2682  0.2864  141 LYS   A CB   
853  C  CG   . LYS   A 114 ? 1.4966 1.4217 0.9881 0.3927  0.2783  0.3010  141 LYS   A CG   
854  C  CD   . LYS   A 114 ? 1.4932 1.3850 0.9787 0.4046  0.3333  0.3487  141 LYS   A CD   
855  C  CE   . LYS   A 114 ? 1.5690 1.4818 0.9880 0.4641  0.3525  0.3889  141 LYS   A CE   
856  N  NZ   . LYS   A 114 ? 1.6349 1.5335 1.0473 0.4783  0.4010  0.4273  141 LYS   A NZ   
857  N  N    . LEU   A 115 ? 1.2966 1.2056 0.9281 0.2682  0.2003  0.1927  142 LEU   A N    
858  C  CA   . LEU   A 115 ? 1.1518 1.0835 0.8113 0.2431  0.1783  0.1581  142 LEU   A CA   
859  C  C    . LEU   A 115 ? 1.1511 1.1117 0.8140 0.2402  0.1353  0.1228  142 LEU   A C    
860  O  O    . LEU   A 115 ? 1.1488 1.1432 0.8152 0.2392  0.1149  0.0954  142 LEU   A O    
861  C  CB   . LEU   A 115 ? 1.1223 1.0213 0.8353 0.2014  0.1905  0.1538  142 LEU   A CB   
862  C  CG   . LEU   A 115 ? 1.1486 1.0677 0.8952 0.1750  0.1700  0.1216  142 LEU   A CG   
863  C  CD1  . LEU   A 115 ? 1.0043 0.9439 0.7420 0.1844  0.1857  0.1248  142 LEU   A CD1  
864  C  CD2  . LEU   A 115 ? 0.9577 0.8504 0.7554 0.1366  0.1728  0.1134  142 LEU   A CD2  
865  N  N    . ASN   A 116 ? 1.1993 1.1464 0.8645 0.2389  0.1232  0.1227  143 ASN   A N    
866  C  CA   . ASN   A 116 ? 1.1927 1.1660 0.8652 0.2359  0.0857  0.0907  143 ASN   A CA   
867  C  C    . ASN   A 116 ? 1.2670 1.2903 0.9033 0.2703  0.0688  0.0771  143 ASN   A C    
868  O  O    . ASN   A 116 ? 1.2325 1.2870 0.8835 0.2644  0.0417  0.0423  143 ASN   A O    
869  C  CB   . ASN   A 116 ? 1.1568 1.1074 0.8359 0.2317  0.0800  0.0964  143 ASN   A CB   
870  C  CG   . ASN   A 116 ? 1.1598 1.1281 0.8626 0.2165  0.0459  0.0637  143 ASN   A CG   
871  O  OD1  . ASN   A 116 ? 1.2348 1.1932 0.9747 0.1854  0.0377  0.0478  143 ASN   A OD1  
872  N  ND2  . ASN   A 116 ? 1.2084 1.2053 0.8912 0.2399  0.0271  0.0538  143 ASN   A ND2  
873  N  N    . ASP   A 117 ? 1.3231 1.3567 0.9136 0.3079  0.0854  0.1033  144 ASP   A N    
874  C  CA   . ASP   A 117 ? 1.3273 1.4173 0.8800 0.3446  0.0689  0.0883  144 ASP   A CA   
875  C  C    . ASP   A 117 ? 1.3833 1.5019 0.9386 0.3423  0.0667  0.0676  144 ASP   A C    
876  O  O    . ASP   A 117 ? 1.3202 1.4842 0.8769 0.3496  0.0397  0.0303  144 ASP   A O    
877  C  CB   . ASP   A 117 ? 1.4665 1.5631 0.9653 0.3896  0.0903  0.1262  144 ASP   A CB   
878  C  CG   . ASP   A 117 ? 1.6038 1.6722 1.1003 0.3953  0.0935  0.1470  144 ASP   A CG   
879  O  OD1  . ASP   A 117 ? 1.5698 1.6563 1.0787 0.3919  0.0636  0.1211  144 ASP   A OD1  
880  O  OD2  . ASP   A 117 ? 1.6417 1.6697 1.1271 0.4035  0.1276  0.1890  144 ASP   A OD2  
881  N  N    . TYR   A 118 ? 1.2879 1.3812 0.8487 0.3313  0.0957  0.0888  145 TYR   A N    
882  C  CA   . TYR   A 118 ? 1.1617 1.2814 0.7254 0.3302  0.0962  0.0709  145 TYR   A CA   
883  C  C    . TYR   A 118 ? 1.1694 1.2966 0.7808 0.2980  0.0681  0.0286  145 TYR   A C    
884  O  O    . TYR   A 118 ? 1.2231 1.3919 0.8339 0.3072  0.0487  -0.0047 145 TYR   A O    
885  C  CB   . TYR   A 118 ? 1.1870 1.2753 0.7552 0.3210  0.1348  0.1027  145 TYR   A CB   
886  C  CG   . TYR   A 118 ? 1.1411 1.2553 0.7125 0.3206  0.1395  0.0877  145 TYR   A CG   
887  C  CD1  . TYR   A 118 ? 1.1648 1.2779 0.7827 0.2877  0.1241  0.0571  145 TYR   A CD1  
888  C  CD2  . TYR   A 118 ? 1.2596 1.3987 0.7870 0.3549  0.1620  0.1069  145 TYR   A CD2  
889  C  CE1  . TYR   A 118 ? 1.2484 1.3845 0.8713 0.2883  0.1293  0.0434  145 TYR   A CE1  
890  C  CE2  . TYR   A 118 ? 1.2810 1.4450 0.8114 0.3552  0.1673  0.0923  145 TYR   A CE2  
891  C  CZ   . TYR   A 118 ? 1.3204 1.4819 0.9000 0.3212  0.1506  0.0596  145 TYR   A CZ   
892  O  OH   . TYR   A 118 ? 1.4303 1.6161 1.0151 0.3224  0.1564  0.0448  145 TYR   A OH   
893  N  N    . LEU   A 119 ? 1.1322 1.2203 0.7863 0.2616  0.0669  0.0292  146 LEU   A N    
894  C  CA   . LEU   A 119 ? 1.1055 1.1976 0.8046 0.2334  0.0437  -0.0047 146 LEU   A CA   
895  C  C    . LEU   A 119 ? 1.1546 1.2769 0.8575 0.2413  0.0123  -0.0367 146 LEU   A C    
896  O  O    . LEU   A 119 ? 1.0288 1.1683 0.7619 0.2295  -0.0055 -0.0694 146 LEU   A O    
897  C  CB   . LEU   A 119 ? 0.9849 1.0347 0.7232 0.1979  0.0484  0.0047  146 LEU   A CB   
898  C  CG   . LEU   A 119 ? 1.0209 1.0404 0.7670 0.1850  0.0793  0.0320  146 LEU   A CG   
899  C  CD1  . LEU   A 119 ? 0.8441 0.8361 0.6350 0.1495  0.0764  0.0286  146 LEU   A CD1  
900  C  CD2  . LEU   A 119 ? 1.0848 1.1232 0.8276 0.1911  0.0923  0.0295  146 LEU   A CD2  
901  N  N    . GLN   A 120 ? 1.1192 1.2485 0.7956 0.2615  0.0067  -0.0285 147 GLN   A N    
902  C  CA   . GLN   A 120 ? 1.1324 1.2966 0.8145 0.2707  -0.0224 -0.0613 147 GLN   A CA   
903  C  C    . GLN   A 120 ? 1.1711 1.3896 0.8377 0.2950  -0.0339 -0.0918 147 GLN   A C    
904  O  O    . GLN   A 120 ? 1.1192 1.3619 0.8186 0.2857  -0.0554 -0.1322 147 GLN   A O    
905  C  CB   . GLN   A 120 ? 1.1901 1.3541 0.8454 0.2907  -0.0246 -0.0442 147 GLN   A CB   
906  C  CG   . GLN   A 120 ? 1.2606 1.4333 0.9460 0.2790  -0.0504 -0.0707 147 GLN   A CG   
907  C  CD   . GLN   A 120 ? 1.4003 1.5743 1.0612 0.2993  -0.0527 -0.0544 147 GLN   A CD   
908  O  OE1  . GLN   A 120 ? 1.4771 1.6206 1.1128 0.3080  -0.0310 -0.0162 147 GLN   A OE1  
909  N  NE2  . GLN   A 120 ? 1.3529 1.5621 1.0256 0.3066  -0.0778 -0.0842 147 GLN   A NE2  
910  N  N    . ILE   A 121 ? 1.2084 1.4474 0.8270 0.3270  -0.0181 -0.0735 148 ILE   A N    
911  C  CA   . ILE   A 121 ? 1.1568 1.4534 0.7560 0.3534  -0.0285 -0.1039 148 ILE   A CA   
912  C  C    . ILE   A 121 ? 1.1626 1.4582 0.7989 0.3305  -0.0291 -0.1292 148 ILE   A C    
913  O  O    . ILE   A 121 ? 1.1603 1.4972 0.8119 0.3358  -0.0478 -0.1730 148 ILE   A O    
914  C  CB   . ILE   A 121 ? 1.2940 1.6123 0.8294 0.3953  -0.0075 -0.0728 148 ILE   A CB   
915  C  CG1  . ILE   A 121 ? 1.2530 1.5503 0.7565 0.4132  0.0042  -0.0319 148 ILE   A CG1  
916  C  CG2  . ILE   A 121 ? 1.2193 1.6112 0.7266 0.4313  -0.0253 -0.1086 148 ILE   A CG2  
917  C  CD1  . ILE   A 121 ? 1.3316 1.6575 0.8359 0.4252  -0.0241 -0.0537 148 ILE   A CD1  
918  N  N    . GLU   A 122 ? 1.1787 1.4292 0.8332 0.3052  -0.0083 -0.1041 149 GLU   A N    
919  C  CA   . GLU   A 122 ? 1.1325 1.3805 0.8244 0.2841  -0.0082 -0.1251 149 GLU   A CA   
920  C  C    . GLU   A 122 ? 1.0946 1.3381 0.8412 0.2580  -0.0318 -0.1597 149 GLU   A C    
921  O  O    . GLU   A 122 ? 1.1413 1.4057 0.9158 0.2539  -0.0416 -0.1946 149 GLU   A O    
922  C  CB   . GLU   A 122 ? 1.1311 1.3356 0.8335 0.2631  0.0181  -0.0910 149 GLU   A CB   
923  C  CG   . GLU   A 122 ? 1.2087 1.4188 0.8688 0.2858  0.0469  -0.0613 149 GLU   A CG   
924  C  CD   . GLU   A 122 ? 1.4861 1.7243 1.1485 0.2923  0.0522  -0.0802 149 GLU   A CD   
925  O  OE1  . GLU   A 122 ? 1.5264 1.8087 1.1831 0.3094  0.0335  -0.1167 149 GLU   A OE1  
926  O  OE2  . GLU   A 122 ? 1.5256 1.7438 1.1987 0.2799  0.0752  -0.0612 149 GLU   A OE2  
927  N  N    . THR   A 123 ? 1.0996 1.3151 0.8637 0.2410  -0.0390 -0.1500 150 THR   A N    
928  C  CA   . THR   A 123 ? 1.0624 1.2708 0.8788 0.2170  -0.0573 -0.1772 150 THR   A CA   
929  C  C    . THR   A 123 ? 1.0591 1.3136 0.8856 0.2316  -0.0794 -0.2219 150 THR   A C    
930  O  O    . THR   A 123 ? 1.1267 1.3881 0.9993 0.2179  -0.0892 -0.2552 150 THR   A O    
931  C  CB   . THR   A 123 ? 1.0634 1.2364 0.8908 0.1993  -0.0586 -0.1556 150 THR   A CB   
932  O  OG1  . THR   A 123 ? 0.9717 1.1063 0.7950 0.1847  -0.0385 -0.1203 150 THR   A OG1  
933  C  CG2  . THR   A 123 ? 0.8836 1.0481 0.7643 0.1756  -0.0735 -0.1789 150 THR   A CG2  
934  N  N    . ILE   A 124 ? 1.0852 1.3734 0.8723 0.2605  -0.0867 -0.2242 151 ILE   A N    
935  C  CA   . ILE   A 124 ? 1.0707 1.4116 0.8688 0.2760  -0.1094 -0.2715 151 ILE   A CA   
936  C  C    . ILE   A 124 ? 1.1338 1.5109 0.9391 0.2857  -0.1115 -0.3069 151 ILE   A C    
937  O  O    . ILE   A 124 ? 1.0967 1.4989 0.9465 0.2789  -0.1271 -0.3546 151 ILE   A O    
938  C  CB   . ILE   A 124 ? 1.1070 1.4831 0.8552 0.3103  -0.1164 -0.2638 151 ILE   A CB   
939  C  CG1  . ILE   A 124 ? 1.1064 1.4479 0.8571 0.2991  -0.1166 -0.2362 151 ILE   A CG1  
940  C  CG2  . ILE   A 124 ? 1.0577 1.5013 0.8149 0.3307  -0.1409 -0.3180 151 ILE   A CG2  
941  C  CD1  . ILE   A 124 ? 1.0521 1.3995 0.7431 0.3307  -0.1078 -0.2001 151 ILE   A CD1  
942  N  N    . GLN   A 125 ? 1.1424 1.5223 0.9082 0.3013  -0.0938 -0.2854 152 GLN   A N    
943  C  CA   . GLN   A 125 ? 1.1915 1.6071 0.9611 0.3123  -0.0942 -0.3184 152 GLN   A CA   
944  C  C    . GLN   A 125 ? 1.2290 1.6152 1.0615 0.2795  -0.0926 -0.3366 152 GLN   A C    
945  O  O    . GLN   A 125 ? 1.3102 1.7254 1.1770 0.2796  -0.1032 -0.3840 152 GLN   A O    
946  C  CB   . GLN   A 125 ? 1.2966 1.7194 1.0092 0.3363  -0.0719 -0.2859 152 GLN   A CB   
947  C  CG   . GLN   A 125 ? 1.4231 1.8484 1.1518 0.3305  -0.0607 -0.2992 152 GLN   A CG   
948  C  CD   . GLN   A 125 ? 1.6334 2.0550 1.3122 0.3483  -0.0332 -0.2589 152 GLN   A CD   
949  O  OE1  . GLN   A 125 ? 1.6350 2.0088 1.3124 0.3319  -0.0131 -0.2151 152 GLN   A OE1  
950  N  NE2  . GLN   A 125 ? 1.6486 2.1233 1.2885 0.3822  -0.0312 -0.2751 152 GLN   A NE2  
951  N  N    . ALA   A 126 ? 1.3121 1.6427 1.1623 0.2528  -0.0789 -0.3007 153 ALA   A N    
952  C  CA   . ALA   A 126 ? 1.0851 1.3882 0.9926 0.2252  -0.0765 -0.3123 153 ALA   A CA   
953  C  C    . ALA   A 126 ? 1.0725 1.3733 1.0364 0.2083  -0.0932 -0.3450 153 ALA   A C    
954  O  O    . ALA   A 126 ? 1.1057 1.4019 1.1205 0.1952  -0.0940 -0.3716 153 ALA   A O    
955  C  CB   . ALA   A 126 ? 0.9768 1.2291 0.8872 0.2039  -0.0596 -0.2667 153 ALA   A CB   
956  N  N    . LEU   A 127 ? 1.0709 1.3735 1.0300 0.2087  -0.1044 -0.3426 154 LEU   A N    
957  C  CA   . LEU   A 127 ? 1.0787 1.3833 1.0934 0.1938  -0.1184 -0.3751 154 LEU   A CA   
958  C  C    . LEU   A 127 ? 1.2038 1.5642 1.2356 0.2099  -0.1336 -0.4330 154 LEU   A C    
959  O  O    . LEU   A 127 ? 1.1076 1.4701 1.2020 0.1949  -0.1402 -0.4700 154 LEU   A O    
960  C  CB   . LEU   A 127 ? 1.0595 1.3507 1.0652 0.1891  -0.1247 -0.3547 154 LEU   A CB   
961  C  CG   . LEU   A 127 ? 0.9925 1.2283 1.0070 0.1651  -0.1135 -0.3116 154 LEU   A CG   
962  C  CD1  . LEU   A 127 ? 0.9710 1.1995 0.9544 0.1695  -0.1167 -0.2863 154 LEU   A CD1  
963  C  CD2  . LEU   A 127 ? 0.9427 1.1547 1.0240 0.1397  -0.1136 -0.3251 154 LEU   A CD2  
964  N  N    . GLU   A 128 ? 1.1858 1.5935 1.1651 0.2413  -0.1382 -0.4422 155 GLU   A N    
965  C  CA   . GLU   A 128 ? 1.2001 1.6701 1.1931 0.2596  -0.1538 -0.5020 155 GLU   A CA   
966  C  C    . GLU   A 128 ? 1.2562 1.7291 1.2830 0.2539  -0.1467 -0.5312 155 GLU   A C    
967  O  O    . GLU   A 128 ? 1.3079 1.8073 1.3898 0.2486  -0.1562 -0.5818 155 GLU   A O    
968  C  CB   . GLU   A 128 ? 1.1827 1.7077 1.1032 0.2997  -0.1605 -0.5000 155 GLU   A CB   
969  C  CG   . GLU   A 128 ? 1.2359 1.7940 1.1533 0.3114  -0.1783 -0.5080 155 GLU   A CG   
970  C  CD   . GLU   A 128 ? 1.2372 1.8203 1.0766 0.3473  -0.1760 -0.4713 155 GLU   A CD   
971  O  OE1  . GLU   A 128 ? 1.3202 1.8989 1.1067 0.3642  -0.1599 -0.4437 155 GLU   A OE1  
972  O  OE2  . GLU   A 128 ? 1.1614 1.7678 0.9953 0.3593  -0.1877 -0.4681 155 GLU   A OE2  
973  N  N    . GLU   A 129 ? 1.2703 1.7152 1.2717 0.2530  -0.1283 -0.4958 156 GLU   A N    
974  C  CA   . GLU   A 129 ? 1.3023 1.7458 1.3371 0.2474  -0.1198 -0.5195 156 GLU   A CA   
975  C  C    . GLU   A 129 ? 1.3585 1.7585 1.4722 0.2151  -0.1166 -0.5300 156 GLU   A C    
976  O  O    . GLU   A 129 ? 1.4785 1.8862 1.6408 0.2106  -0.1150 -0.5692 156 GLU   A O    
977  C  CB   . GLU   A 129 ? 1.2820 1.7059 1.2734 0.2532  -0.0997 -0.4760 156 GLU   A CB   
978  C  CG   . GLU   A 129 ? 1.4034 1.8719 1.3204 0.2885  -0.0968 -0.4670 156 GLU   A CG   
979  C  CD   . GLU   A 129 ? 1.4088 1.8461 1.2830 0.2897  -0.0735 -0.4099 156 GLU   A CD   
980  O  OE1  . GLU   A 129 ? 1.3463 1.7339 1.2510 0.2633  -0.0620 -0.3842 156 GLU   A OE1  
981  O  OE2  . GLU   A 129 ? 1.4807 1.9453 1.2925 0.3180  -0.0655 -0.3910 156 GLU   A OE2  
982  N  N    . LEU   A 130 ? 1.3403 1.6953 1.4682 0.1942  -0.1141 -0.4950 157 LEU   A N    
983  C  CA   . LEU   A 130 ? 1.2748 1.5877 1.4733 0.1667  -0.1080 -0.4973 157 LEU   A CA   
984  C  C    . LEU   A 130 ? 1.3836 1.7171 1.6438 0.1602  -0.1193 -0.5508 157 LEU   A C    
985  O  O    . LEU   A 130 ? 1.4552 1.7738 1.7817 0.1467  -0.1125 -0.5770 157 LEU   A O    
986  C  CB   . LEU   A 130 ? 1.2298 1.4947 1.4205 0.1494  -0.1018 -0.4443 157 LEU   A CB   
987  C  CG   . LEU   A 130 ? 1.2621 1.4863 1.5191 0.1244  -0.0958 -0.4401 157 LEU   A CG   
988  C  CD1  . LEU   A 130 ? 1.2223 1.4180 1.5078 0.1165  -0.0805 -0.4280 157 LEU   A CD1  
989  C  CD2  . LEU   A 130 ? 1.1118 1.3062 1.3532 0.1128  -0.0956 -0.3983 157 LEU   A CD2  
990  N  N    . ALA   A 131 ? 1.2927 1.6612 1.5364 0.1699  -0.1353 -0.5684 158 ALA   A N    
991  C  CA   . ALA   A 131 ? 1.3206 1.7148 1.6284 0.1621  -0.1457 -0.6182 158 ALA   A CA   
992  C  C    . ALA   A 131 ? 1.4734 1.9153 1.8111 0.1704  -0.1486 -0.6567 158 ALA   A C    
993  O  O    . ALA   A 131 ? 1.4802 1.9279 1.8949 0.1547  -0.1465 -0.6859 158 ALA   A O    
994  C  CB   . ALA   A 131 ? 1.1904 1.6169 1.4729 0.1715  -0.1616 -0.6169 158 ALA   A CB   
995  N  N    . ALA   A 132 ? 1.4904 1.9677 1.7701 0.1953  -0.1517 -0.6566 159 ALA   A N    
996  C  CA   . ALA   A 132 ? 1.4167 1.9413 1.7222 0.2044  -0.1550 -0.6936 159 ALA   A CA   
997  C  C    . ALA   A 132 ? 1.4917 1.9792 1.8470 0.1874  -0.1388 -0.7013 159 ALA   A C    
998  O  O    . ALA   A 132 ? 1.5519 2.0611 1.9692 0.1804  -0.1389 -0.7378 159 ALA   A O    
999  C  CB   . ALA   A 132 ? 1.3663 1.9378 1.5928 0.2375  -0.1608 -0.6861 159 ALA   A CB   
1000 N  N    . LYS   A 133 ? 1.4485 1.8820 1.7806 0.1821  -0.1239 -0.6675 160 LYS   A N    
1001 C  CA   . LYS   A 133 ? 1.4259 1.8214 1.8071 0.1682  -0.1071 -0.6697 160 LYS   A CA   
1002 C  C    . LYS   A 133 ? 1.5387 1.8991 2.0066 0.1413  -0.1002 -0.6778 160 LYS   A C    
1003 O  O    . LYS   A 133 ? 1.5770 1.9255 2.1050 0.1310  -0.0893 -0.6942 160 LYS   A O    
1004 C  CB   . LYS   A 133 ? 1.2881 1.6398 1.6275 0.1718  -0.0925 -0.6304 160 LYS   A CB   
1005 C  CG   . LYS   A 133 ? 1.2731 1.5954 1.6525 0.1650  -0.0753 -0.6286 160 LYS   A CG   
1006 C  CD   . LYS   A 133 ? 1.1853 1.4577 1.5468 0.1540  -0.0619 -0.5629 160 LYS   A CD   
1007 C  CE   . LYS   A 133 ? 1.2208 1.4471 1.6291 0.1318  -0.0580 -0.5402 160 LYS   A CE   
1008 N  NZ   . LYS   A 133 ? 1.1506 1.3360 1.5421 0.1233  -0.0469 -0.4805 160 LYS   A NZ   
1009 N  N    . GLU   A 134 ? 1.5856 1.9291 2.0616 0.1306  -0.1044 -0.6645 161 GLU   A N    
1010 C  CA   . GLU   A 134 ? 1.5491 1.8594 2.1054 0.1062  -0.0945 -0.6667 161 GLU   A CA   
1011 C  C    . GLU   A 134 ? 1.4984 1.8554 2.1139 0.1010  -0.1017 -0.7096 161 GLU   A C    
1012 O  O    . GLU   A 134 ? 1.5163 1.8527 2.2109 0.0821  -0.0883 -0.7192 161 GLU   A O    
1013 C  CB   . GLU   A 134 ? 1.5531 1.8256 2.0951 0.0968  -0.0940 -0.6330 161 GLU   A CB   
1014 C  CG   . GLU   A 134 ? 1.6164 1.8327 2.1354 0.0930  -0.0801 -0.5837 161 GLU   A CG   
1015 C  CD   . GLU   A 134 ? 1.6212 1.8065 2.1286 0.0807  -0.0789 -0.5377 161 GLU   A CD   
1016 O  OE1  . GLU   A 134 ? 1.6761 1.8843 2.1711 0.0815  -0.0921 -0.5490 161 GLU   A OE1  
1017 O  OE2  . GLU   A 134 ? 1.5498 1.6913 2.0599 0.0718  -0.0653 -0.4914 161 GLU   A OE2  
1018 N  N    . LYS   A 135 ? 1.5104 1.9318 2.0920 0.1192  -0.1208 -0.7346 162 LYS   A N    
1019 C  CA   . LYS   A 135 ? 1.5072 1.9822 2.1488 0.1175  -0.1284 -0.7802 162 LYS   A CA   
1020 C  C    . LYS   A 135 ? 1.4990 1.9913 2.1905 0.1156  -0.1214 -0.8139 162 LYS   A C    
1021 O  O    . LYS   A 135 ? 1.4806 1.9756 2.2577 0.0993  -0.1123 -0.8413 162 LYS   A O    
1022 C  CB   . LYS   A 135 ? 1.3878 1.9306 1.9770 0.1422  -0.1510 -0.7948 162 LYS   A CB   
1023 N  N    . ALA   A 136 ? 1.4113 1.9155 2.0518 0.1323  -0.1238 -0.8124 163 ALA   A N    
1024 C  CA   . ALA   A 136 ? 1.4198 1.9394 2.1013 0.1319  -0.1174 -0.8432 163 ALA   A CA   
1025 C  C    . ALA   A 136 ? 1.3552 1.8090 2.0420 0.1221  -0.0968 -0.8143 163 ALA   A C    
1026 O  O    . ALA   A 136 ? 1.2756 1.6766 2.0183 0.1014  -0.0798 -0.7989 163 ALA   A O    
1027 C  CB   . ALA   A 136 ? 1.5120 2.0982 2.1386 0.1597  -0.1335 -0.8652 163 ALA   A CB   
1028 N  N    . GLN   A 161 ? 1.5123 2.2195 1.8067 0.2523  -0.2562 -0.6649 188 GLN   A N    
1029 C  CA   . GLN   A 161 ? 1.5612 2.2256 1.9310 0.2131  -0.2438 -0.6778 188 GLN   A CA   
1030 C  C    . GLN   A 161 ? 1.6736 2.2678 2.0172 0.1936  -0.2333 -0.6413 188 GLN   A C    
1031 O  O    . GLN   A 161 ? 1.6199 2.1637 1.9665 0.1731  -0.2274 -0.6150 188 GLN   A O    
1032 C  CB   . GLN   A 161 ? 1.4391 2.1411 1.8800 0.2082  -0.2407 -0.7275 188 GLN   A CB   
1033 C  CG   . GLN   A 161 ? 1.4519 2.2300 1.9241 0.2286  -0.2511 -0.7703 188 GLN   A CG   
1034 C  CD   . GLN   A 161 ? 1.6404 2.4715 2.1541 0.2373  -0.2530 -0.8166 188 GLN   A CD   
1035 O  OE1  . GLN   A 161 ? 1.7304 2.5353 2.2727 0.2197  -0.2433 -0.8222 188 GLN   A OE1  
1036 N  NE2  . GLN   A 161 ? 1.5463 2.4547 2.0645 0.2657  -0.2654 -0.8511 188 GLN   A NE2  
1037 N  N    . ASP   A 162 ? 1.6556 2.2494 1.9747 0.2010  -0.2309 -0.6413 189 ASP   A N    
1038 C  CA   . ASP   A 162 ? 1.7665 2.2994 2.0557 0.1871  -0.2208 -0.6094 189 ASP   A CA   
1039 C  C    . ASP   A 162 ? 1.7670 2.2999 1.9619 0.2135  -0.2242 -0.5761 189 ASP   A C    
1040 O  O    . ASP   A 162 ? 1.6213 2.1025 1.7818 0.2041  -0.2164 -0.5441 189 ASP   A O    
1041 C  CB   . ASP   A 162 ? 1.9014 2.4217 2.2416 0.1710  -0.2098 -0.6320 189 ASP   A CB   
1042 C  CG   . ASP   A 162 ? 2.0151 2.4985 2.4410 0.1374  -0.1964 -0.6422 189 ASP   A CG   
1043 O  OD1  . ASP   A 162 ? 2.0869 2.5324 2.5177 0.1219  -0.1924 -0.6186 189 ASP   A OD1  
1044 O  OD2  . ASP   A 162 ? 1.8733 2.3660 2.3624 0.1274  -0.1882 -0.6723 189 ASP   A OD2  
1045 N  N    . GLU   A 163 ? 1.7092 2.2990 1.8633 0.2476  -0.2336 -0.5817 190 GLU   A N    
1046 C  CA   . GLU   A 163 ? 1.5255 2.1137 1.5893 0.2754  -0.2330 -0.5420 190 GLU   A CA   
1047 C  C    . GLU   A 163 ? 1.4299 1.9879 1.4589 0.2752  -0.2342 -0.5056 190 GLU   A C    
1048 O  O    . GLU   A 163 ? 1.3244 1.8587 1.2842 0.2894  -0.2282 -0.4648 190 GLU   A O    
1049 C  CB   . GLU   A 163 ? 1.4033 2.0613 1.4365 0.3146  -0.2409 -0.5536 190 GLU   A CB   
1050 N  N    . VAL   A 164 ? 1.4627 2.0217 1.5404 0.2598  -0.2400 -0.5192 191 VAL   A N    
1051 C  CA   . VAL   A 164 ? 1.3819 1.9089 1.4363 0.2549  -0.2411 -0.4869 191 VAL   A CA   
1052 C  C    . VAL   A 164 ? 1.3804 1.8302 1.4476 0.2223  -0.2213 -0.4480 191 VAL   A C    
1053 O  O    . VAL   A 164 ? 1.3670 1.7752 1.3907 0.2232  -0.2094 -0.3969 191 VAL   A O    
1054 C  CB   . VAL   A 164 ? 1.3176 1.8691 1.4266 0.2476  -0.2486 -0.5103 191 VAL   A CB   
1055 C  CG1  . VAL   A 164 ? 1.0930 1.6029 1.1957 0.2330  -0.2477 -0.4799 191 VAL   A CG1  
1056 C  CG2  . VAL   A 164 ? 1.0990 1.7169 1.1887 0.2838  -0.2581 -0.5245 191 VAL   A CG2  
1057 N  N    . ASP   A 165 ? 1.4321 1.8616 1.5625 0.1939  -0.2151 -0.4701 192 ASP   A N    
1058 C  CA   . ASP   A 165 ? 1.3227 1.6842 1.4677 0.1659  -0.1954 -0.4320 192 ASP   A CA   
1059 C  C    . ASP   A 165 ? 1.2130 1.5488 1.3049 0.1737  -0.1833 -0.3966 192 ASP   A C    
1060 O  O    . ASP   A 165 ? 1.2098 1.4968 1.2824 0.1619  -0.1695 -0.3517 192 ASP   A O    
1061 C  CB   . ASP   A 165 ? 1.3638 1.7126 1.5877 0.1392  -0.1896 -0.4626 192 ASP   A CB   
1062 C  CG   . ASP   A 165 ? 1.5051 1.8639 1.7901 0.1243  -0.1940 -0.4874 192 ASP   A CG   
1063 O  OD1  . ASP   A 165 ? 1.6996 2.0937 1.9693 0.1388  -0.2077 -0.4967 192 ASP   A OD1  
1064 O  OD2  . ASP   A 165 ? 1.4843 1.8161 1.8344 0.0992  -0.1821 -0.4962 192 ASP   A OD2  
1065 N  N    . ILE   A 166 ? 1.3003 1.6716 1.3701 0.1937  -0.1877 -0.4183 193 ILE   A N    
1066 C  CA   . ILE   A 166 ? 1.1941 1.5450 1.2160 0.2019  -0.1743 -0.3861 193 ILE   A CA   
1067 C  C    . ILE   A 166 ? 1.1853 1.5253 1.1408 0.2204  -0.1686 -0.3406 193 ILE   A C    
1068 O  O    . ILE   A 166 ? 1.2373 1.5343 1.1680 0.2130  -0.1518 -0.2989 193 ILE   A O    
1069 C  CB   . ILE   A 166 ? 1.2097 1.6067 1.2234 0.2215  -0.1798 -0.4224 193 ILE   A CB   
1070 C  CG1  . ILE   A 166 ? 1.1494 1.5385 1.2312 0.1987  -0.1774 -0.4579 193 ILE   A CG1  
1071 C  CG2  . ILE   A 166 ? 1.1408 1.5286 1.0921 0.2388  -0.1661 -0.3871 193 ILE   A CG2  
1072 C  CD1  . ILE   A 166 ? 1.2195 1.6459 1.2952 0.2149  -0.1793 -0.4914 193 ILE   A CD1  
1073 N  N    . LYS   A 167 ? 1.1905 1.5698 1.1202 0.2450  -0.1816 -0.3487 194 LYS   A N    
1074 C  CA   . LYS   A 167 ? 1.0646 1.4321 0.9342 0.2654  -0.1739 -0.3046 194 LYS   A CA   
1075 C  C    . LYS   A 167 ? 1.0390 1.3502 0.9195 0.2414  -0.1636 -0.2687 194 LYS   A C    
1076 O  O    . LYS   A 167 ? 1.0730 1.3491 0.9161 0.2444  -0.1477 -0.2255 194 LYS   A O    
1077 C  CB   . LYS   A 167 ? 1.1572 1.5840 0.9996 0.3003  -0.1912 -0.3227 194 LYS   A CB   
1078 N  N    . SER   A 168 ? 1.0108 1.3138 0.9446 0.2176  -0.1710 -0.2869 195 SER   A N    
1079 C  CA   . SER   A 168 ? 0.8933 1.1492 0.8365 0.1969  -0.1621 -0.2557 195 SER   A CA   
1080 C  C    . SER   A 168 ? 0.9408 1.1468 0.8944 0.1717  -0.1454 -0.2307 195 SER   A C    
1081 O  O    . SER   A 168 ? 0.9661 1.1344 0.9003 0.1642  -0.1334 -0.1948 195 SER   A O    
1082 C  CB   . SER   A 168 ? 0.9339 1.2003 0.9301 0.1816  -0.1731 -0.2815 195 SER   A CB   
1083 O  OG   . SER   A 168 ? 1.0925 1.3789 1.1412 0.1697  -0.1792 -0.3224 195 SER   A OG   
1084 N  N    . ARG   A 169 ? 1.0074 1.2148 0.9937 0.1595  -0.1444 -0.2510 196 ARG   A N    
1085 C  CA   . ARG   A 169 ? 0.9689 1.1357 0.9661 0.1389  -0.1298 -0.2290 196 ARG   A CA   
1086 C  C    . ARG   A 169 ? 1.0081 1.1633 0.9587 0.1496  -0.1170 -0.2018 196 ARG   A C    
1087 O  O    . ARG   A 169 ? 0.8979 1.0228 0.8551 0.1338  -0.1049 -0.1824 196 ARG   A O    
1088 C  CB   . ARG   A 169 ? 0.9485 1.1204 0.9962 0.1257  -0.1310 -0.2581 196 ARG   A CB   
1089 C  CG   . ARG   A 169 ? 0.8582 1.0278 0.9636 0.1084  -0.1357 -0.2775 196 ARG   A CG   
1090 C  CD   . ARG   A 169 ? 0.8185 1.0067 0.9751 0.1037  -0.1385 -0.3182 196 ARG   A CD   
1091 N  NE   . ARG   A 169 ? 0.9082 1.0939 1.1258 0.0874  -0.1394 -0.3373 196 ARG   A NE   
1092 C  CZ   . ARG   A 169 ? 1.0159 1.2049 1.2942 0.0767  -0.1362 -0.3686 196 ARG   A CZ   
1093 N  NH1  . ARG   A 169 ? 1.0331 1.2291 1.3192 0.0807  -0.1337 -0.3865 196 ARG   A NH1  
1094 N  NH2  . ARG   A 169 ? 0.9075 1.0915 1.2429 0.0616  -0.1333 -0.3821 196 ARG   A NH2  
1095 N  N    . ALA   A 170 ? 0.9080 1.0887 0.8134 0.1770  -0.1182 -0.1992 197 ALA   A N    
1096 C  CA   . ALA   A 170 ? 0.9180 1.0858 0.7795 0.1886  -0.1016 -0.1692 197 ALA   A CA   
1097 C  C    . ALA   A 170 ? 1.0770 1.2301 0.8986 0.2023  -0.0932 -0.1364 197 ALA   A C    
1098 O  O    . ALA   A 170 ? 1.1200 1.2530 0.9121 0.2078  -0.0744 -0.1067 197 ALA   A O    
1099 C  CB   . ALA   A 170 ? 0.9165 1.1245 0.7541 0.2135  -0.1033 -0.1875 197 ALA   A CB   
1100 N  N    . ALA   A 171 ? 1.0777 1.2391 0.9016 0.2075  -0.1044 -0.1409 198 ALA   A N    
1101 C  CA   . ALA   A 171 ? 1.0711 1.2194 0.8592 0.2235  -0.0963 -0.1111 198 ALA   A CA   
1102 C  C    . ALA   A 171 ? 1.1236 1.2195 0.9221 0.1985  -0.0807 -0.0824 198 ALA   A C    
1103 O  O    . ALA   A 171 ? 1.0522 1.1325 0.8696 0.1850  -0.0853 -0.0809 198 ALA   A O    
1104 C  CB   . ALA   A 171 ? 1.0423 1.2202 0.8338 0.2373  -0.1144 -0.1284 198 ALA   A CB   
1105 N  N    . TYR   A 172 ? 1.0646 1.1364 0.8519 0.1927  -0.0615 -0.0614 199 TYR   A N    
1106 C  CA   . TYR   A 172 ? 0.9407 0.9687 0.7393 0.1701  -0.0461 -0.0382 199 TYR   A CA   
1107 C  C    . TYR   A 172 ? 0.9899 0.9985 0.7677 0.1809  -0.0373 -0.0154 199 TYR   A C    
1108 O  O    . TYR   A 172 ? 0.9411 0.9568 0.6828 0.2090  -0.0284 0.0005  199 TYR   A O    
1109 C  CB   . TYR   A 172 ? 0.8753 0.8877 0.6677 0.1647  -0.0260 -0.0226 199 TYR   A CB   
1110 C  CG   . TYR   A 172 ? 0.8899 0.9211 0.7006 0.1573  -0.0322 -0.0431 199 TYR   A CG   
1111 C  CD1  . TYR   A 172 ? 0.9555 0.9882 0.8060 0.1358  -0.0460 -0.0634 199 TYR   A CD1  
1112 C  CD2  . TYR   A 172 ? 1.0727 1.1196 0.8614 0.1735  -0.0221 -0.0406 199 TYR   A CD2  
1113 C  CE1  . TYR   A 172 ? 0.9806 1.0276 0.8509 0.1305  -0.0497 -0.0812 199 TYR   A CE1  
1114 C  CE2  . TYR   A 172 ? 0.9766 1.0407 0.7838 0.1675  -0.0270 -0.0608 199 TYR   A CE2  
1115 C  CZ   . TYR   A 172 ? 0.9074 0.9703 0.7567 0.1459  -0.0409 -0.0814 199 TYR   A CZ   
1116 O  OH   . TYR   A 172 ? 0.8872 0.9643 0.7577 0.1413  -0.0440 -0.1007 199 TYR   A OH   
1117 N  N    . ASN   A 173 ? 0.9806 0.9656 0.7808 0.1605  -0.0386 -0.0131 200 ASN   A N    
1118 C  CA   . ASN   A 173 ? 0.9410 0.9038 0.7276 0.1679  -0.0292 0.0063  200 ASN   A CA   
1119 C  C    . ASN   A 173 ? 0.9583 0.8801 0.7537 0.1495  -0.0072 0.0259  200 ASN   A C    
1120 O  O    . ASN   A 173 ? 1.0173 0.9158 0.7996 0.1587  0.0079  0.0453  200 ASN   A O    
1121 C  CB   . ASN   A 173 ? 0.9128 0.8837 0.7176 0.1624  -0.0468 -0.0082 200 ASN   A CB   
1122 C  CG   . ASN   A 173 ? 0.8828 0.8511 0.7260 0.1326  -0.0564 -0.0246 200 ASN   A CG   
1123 O  OD1  . ASN   A 173 ? 1.0187 0.9700 0.8751 0.1135  -0.0478 -0.0201 200 ASN   A OD1  
1124 N  ND2  . ASN   A 173 ? 0.9466 0.9336 0.8093 0.1299  -0.0732 -0.0429 200 ASN   A ND2  
1125 N  N    . VAL   A 174 ? 0.9448 0.8588 0.7649 0.1245  -0.0047 0.0195  201 VAL   A N    
1126 C  CA   . VAL   A 174 ? 0.9154 0.7983 0.7504 0.1052  0.0143  0.0312  201 VAL   A CA   
1127 C  C    . VAL   A 174 ? 0.9531 0.8395 0.7988 0.0942  0.0226  0.0297  201 VAL   A C    
1128 O  O    . VAL   A 174 ? 0.8783 0.7889 0.7253 0.0969  0.0108  0.0172  201 VAL   A O    
1129 C  CB   . VAL   A 174 ? 0.9984 0.8729 0.8610 0.0821  0.0056  0.0206  201 VAL   A CB   
1130 C  CG1  . VAL   A 174 ? 0.7928 0.6641 0.6473 0.0922  -0.0013 0.0215  201 VAL   A CG1  
1131 C  CG2  . VAL   A 174 ? 0.8447 0.7409 0.7296 0.0676  -0.0129 0.0020  201 VAL   A CG2  
1132 N  N    . THR   A 175 ? 0.9213 0.7837 0.7788 0.0813  0.0443  0.0408  202 THR   A N    
1133 C  CA   . THR   A 175 ? 0.8929 0.7590 0.7701 0.0656  0.0523  0.0368  202 THR   A CA   
1134 C  C    . THR   A 175 ? 0.9715 0.8212 0.8806 0.0401  0.0605  0.0325  202 THR   A C    
1135 O  O    . THR   A 175 ? 0.9255 0.7507 0.8372 0.0382  0.0747  0.0405  202 THR   A O    
1136 C  CB   . THR   A 175 ? 0.9986 0.8604 0.8579 0.0802  0.0756  0.0541  202 THR   A CB   
1137 O  OG1  . THR   A 175 ? 1.0583 0.9267 0.9412 0.0636  0.0827  0.0479  202 THR   A OG1  
1138 C  CG2  . THR   A 175 ? 0.9776 0.8067 0.8290 0.0872  0.1040  0.0775  202 THR   A CG2  
1139 N  N    . LEU   A 176 ? 0.9232 0.7891 0.8579 0.0221  0.0512  0.0179  203 LEU   A N    
1140 C  CA   . LEU   A 176 ? 0.8268 0.6896 0.7931 -0.0008 0.0544  0.0079  203 LEU   A CA   
1141 C  C    . LEU   A 176 ? 0.8609 0.7261 0.8482 -0.0117 0.0722  0.0077  203 LEU   A C    
1142 O  O    . LEU   A 176 ? 1.0603 0.9475 1.0551 -0.0135 0.0644  0.0014  203 LEU   A O    
1143 C  CB   . LEU   A 176 ? 0.8268 0.7122 0.8063 -0.0099 0.0297  -0.0076 203 LEU   A CB   
1144 C  CG   . LEU   A 176 ? 0.9111 0.8051 0.9202 -0.0300 0.0286  -0.0209 203 LEU   A CG   
1145 C  CD1  . LEU   A 176 ? 0.9348 0.8088 0.9458 -0.0347 0.0364  -0.0225 203 LEU   A CD1  
1146 C  CD2  . LEU   A 176 ? 0.8968 0.8176 0.9139 -0.0329 0.0062  -0.0303 203 LEU   A CD2  
1147 N  N    . LEU   A 177 ? 1.0418 0.8839 1.0423 -0.0188 0.0978  0.0140  204 LEU   A N    
1148 C  CA   . LEU   A 177 ? 0.9493 0.7922 0.9755 -0.0303 0.1192  0.0137  204 LEU   A CA   
1149 C  C    . LEU   A 177 ? 0.9743 0.8388 1.0413 -0.0544 0.1108  -0.0105 204 LEU   A C    
1150 O  O    . LEU   A 177 ? 1.0884 0.9538 1.1675 -0.0642 0.1014  -0.0237 204 LEU   A O    
1151 C  CB   . LEU   A 177 ? 0.9678 0.7752 0.9980 -0.0283 0.1543  0.0309  204 LEU   A CB   
1152 C  CG   . LEU   A 177 ? 1.0082 0.8008 1.0029 -0.0028 0.1735  0.0592  204 LEU   A CG   
1153 C  CD1  . LEU   A 177 ? 1.1011 0.9028 1.0506 0.0224  0.1510  0.0661  204 LEU   A CD1  
1154 C  CD2  . LEU   A 177 ? 1.1068 0.8595 1.1095 -0.0004 0.2106  0.0790  204 LEU   A CD2  
1155 N  N    . ASN   A 178 ? 0.9188 0.8049 1.0065 -0.0621 0.1138  -0.0172 205 ASN   A N    
1156 C  CA   . ASN   A 178 ? 0.9192 0.8358 1.0449 -0.0810 0.1037  -0.0409 205 ASN   A CA   
1157 C  C    . ASN   A 178 ? 0.9713 0.8908 1.1352 -0.0957 0.1293  -0.0467 205 ASN   A C    
1158 O  O    . ASN   A 178 ? 0.9971 0.9021 1.1537 -0.0885 0.1511  -0.0299 205 ASN   A O    
1159 C  CB   . ASN   A 178 ? 0.9174 0.8678 1.0366 -0.0747 0.0767  -0.0465 205 ASN   A CB   
1160 C  CG   . ASN   A 178 ? 1.0912 1.0385 1.1788 -0.0610 0.0546  -0.0406 205 ASN   A CG   
1161 O  OD1  . ASN   A 178 ? 1.1845 1.1389 1.2747 -0.0653 0.0404  -0.0492 205 ASN   A OD1  
1162 N  ND2  . ASN   A 178 ? 1.0327 0.9725 1.0922 -0.0442 0.0523  -0.0277 205 ASN   A ND2  
1163 N  N    . PHE   A 179 ? 1.0302 0.9723 1.2363 -0.1156 0.1270  -0.0721 206 PHE   A N    
1164 C  CA   . PHE   A 179 ? 0.8525 0.8058 1.1055 -0.1328 0.1492  -0.0845 206 PHE   A CA   
1165 C  C    . PHE   A 179 ? 0.9147 0.9169 1.2057 -0.1477 0.1297  -0.1172 206 PHE   A C    
1166 O  O    . PHE   A 179 ? 0.9253 0.9402 1.2165 -0.1509 0.1113  -0.1329 206 PHE   A O    
1167 C  CB   . PHE   A 179 ? 0.9689 0.8835 1.2466 -0.1442 0.1847  -0.0817 206 PHE   A CB   
1168 C  CG   . PHE   A 179 ? 0.9134 0.8420 1.2524 -0.1671 0.2083  -0.1019 206 PHE   A CG   
1169 C  CD1  . PHE   A 179 ? 0.9762 0.9069 1.3261 -0.1662 0.2295  -0.0898 206 PHE   A CD1  
1170 C  CD2  . PHE   A 179 ? 0.9508 0.8940 1.3397 -0.1894 0.2096  -0.1357 206 PHE   A CD2  
1171 C  CE1  . PHE   A 179 ? 0.9910 0.9365 1.4029 -0.1884 0.2528  -0.1095 206 PHE   A CE1  
1172 C  CE2  . PHE   A 179 ? 0.8748 0.8352 1.3276 -0.2120 0.2314  -0.1590 206 PHE   A CE2  
1173 C  CZ   . PHE   A 179 ? 0.9729 0.9336 1.4385 -0.2120 0.2536  -0.1452 206 PHE   A CZ   
1174 N  N    . MET   A 180 ? 0.9001 0.9334 1.2220 -0.1547 0.1339  -0.1274 207 MET   A N    
1175 C  CA   . MET   A 180 ? 0.8976 0.9845 1.2611 -0.1676 0.1181  -0.1602 207 MET   A CA   
1176 C  C    . MET   A 180 ? 1.0271 1.1325 1.4406 -0.1823 0.1405  -0.1726 207 MET   A C    
1177 O  O    . MET   A 180 ? 0.8788 0.9762 1.2824 -0.1743 0.1527  -0.1536 207 MET   A O    
1178 C  CB   . MET   A 180 ? 0.9973 1.1229 1.3371 -0.1516 0.0835  -0.1592 207 MET   A CB   
1179 C  CG   . MET   A 180 ? 0.9313 1.1199 1.3117 -0.1595 0.0675  -0.1900 207 MET   A CG   
1180 S  SD   . MET   A 180 ? 1.2227 1.4547 1.5765 -0.1409 0.0275  -0.1923 207 MET   A SD   
1181 C  CE   . MET   A 180 ? 0.9174 1.2055 1.2973 -0.1338 0.0177  -0.1991 207 MET   A CE   
1182 N  N    . ASP   A 181 ? 1.0536 1.1862 1.5228 -0.2038 0.1461  -0.2071 208 ASP   A N    
1183 C  CA   . ASP   A 181 ? 1.0369 1.2021 1.5635 -0.2195 0.1620  -0.2273 208 ASP   A CA   
1184 C  C    . ASP   A 181 ? 1.0367 1.2736 1.5783 -0.2157 0.1284  -0.2527 208 ASP   A C    
1185 O  O    . ASP   A 181 ? 1.0777 1.3512 1.6403 -0.2229 0.1105  -0.2840 208 ASP   A O    
1186 C  CB   . ASP   A 181 ? 1.0657 1.2196 1.6540 -0.2467 0.1918  -0.2536 208 ASP   A CB   
1187 C  CG   . ASP   A 181 ? 1.1993 1.3983 1.8585 -0.2662 0.2050  -0.2840 208 ASP   A CG   
1188 O  OD1  . ASP   A 181 ? 1.3379 1.6014 2.0289 -0.2722 0.1798  -0.3215 208 ASP   A OD1  
1189 O  OD2  . ASP   A 181 ? 1.2040 1.3771 1.8877 -0.2742 0.2413  -0.2705 208 ASP   A OD2  
1190 N  N    . PRO   A 182 ? 1.0145 1.2755 1.5451 -0.2020 0.1188  -0.2404 209 PRO   A N    
1191 C  CA   . PRO   A 182 ? 0.9606 1.2889 1.4995 -0.1923 0.0860  -0.2588 209 PRO   A CA   
1192 C  C    . PRO   A 182 ? 1.1869 1.5758 1.7931 -0.2112 0.0846  -0.3041 209 PRO   A C    
1193 O  O    . PRO   A 182 ? 1.1865 1.6350 1.7974 -0.2025 0.0547  -0.3245 209 PRO   A O    
1194 C  CB   . PRO   A 182 ? 0.7996 1.1322 1.3228 -0.1764 0.0860  -0.2360 209 PRO   A CB   
1195 C  CG   . PRO   A 182 ? 0.9036 1.1853 1.4279 -0.1841 0.1228  -0.2168 209 PRO   A CG   
1196 C  CD   . PRO   A 182 ? 1.0060 1.2342 1.5107 -0.1908 0.1363  -0.2077 209 PRO   A CD   
1197 N  N    . GLN   A 183 ? 1.1049 1.4830 1.7652 -0.2356 0.1170  -0.3209 210 GLN   A N    
1198 C  CA   . GLN   A 183 ? 1.2087 1.6476 1.9427 -0.2563 0.1174  -0.3700 210 GLN   A CA   
1199 C  C    . GLN   A 183 ? 1.3032 1.7629 2.0513 -0.2655 0.1024  -0.4043 210 GLN   A C    
1200 O  O    . GLN   A 183 ? 1.3492 1.8723 2.1479 -0.2757 0.0919  -0.4492 210 GLN   A O    
1201 C  CB   . GLN   A 183 ? 1.1765 1.5917 1.9702 -0.2819 0.1615  -0.3778 210 GLN   A CB   
1202 C  CG   . GLN   A 183 ? 1.2846 1.7121 2.0903 -0.2771 0.1747  -0.3624 210 GLN   A CG   
1203 C  CD   . GLN   A 183 ? 1.3588 1.8497 2.1478 -0.2549 0.1378  -0.3652 210 GLN   A CD   
1204 O  OE1  . GLN   A 183 ? 1.1923 1.6654 1.9322 -0.2328 0.1311  -0.3302 210 GLN   A OE1  
1205 N  NE2  . GLN   A 183 ? 1.3071 1.8748 2.1400 -0.2597 0.1149  -0.4080 210 GLN   A NE2  
1206 N  N    . LYS   A 184 ? 1.3174 1.7265 2.0185 -0.2594 0.1005  -0.3850 211 LYS   A N    
1207 C  CA   . LYS   A 184 ? 1.2981 1.7227 2.0085 -0.2668 0.0878  -0.4164 211 LYS   A CA   
1208 C  C    . LYS   A 184 ? 1.3068 1.7910 1.9823 -0.2443 0.0443  -0.4244 211 LYS   A C    
1209 O  O    . LYS   A 184 ? 1.2730 1.7788 1.9512 -0.2470 0.0307  -0.4514 211 LYS   A O    
1210 C  CB   . LYS   A 184 ? 1.3454 1.6909 2.0213 -0.2683 0.1057  -0.3914 211 LYS   A CB   
1211 C  CG   . LYS   A 184 ? 1.3225 1.6205 2.0506 -0.2948 0.1490  -0.4015 211 LYS   A CG   
1212 C  CD   . LYS   A 184 ? 1.3699 1.5851 2.0529 -0.2882 0.1681  -0.3635 211 LYS   A CD   
1213 C  CE   . LYS   A 184 ? 1.2626 1.4776 1.9151 -0.2812 0.1452  -0.3736 211 LYS   A CE   
1214 N  NZ   . LYS   A 184 ? 1.2240 1.4363 1.7989 -0.2524 0.1150  -0.3390 211 LYS   A NZ   
1215 N  N    . MET   A 185 ? 1.3214 1.8320 1.9648 -0.2210 0.0243  -0.4011 212 MET   A N    
1216 C  CA   . MET   A 185 ? 1.3354 1.8953 1.9408 -0.1955 -0.0127 -0.3993 212 MET   A CA   
1217 C  C    . MET   A 185 ? 1.4283 2.0795 2.0707 -0.1887 -0.0328 -0.4295 212 MET   A C    
1218 O  O    . MET   A 185 ? 1.4205 2.0847 2.0869 -0.1893 -0.0248 -0.4248 212 MET   A O    
1219 C  CB   . MET   A 185 ? 1.2205 1.7394 1.7592 -0.1699 -0.0208 -0.3471 212 MET   A CB   
1220 C  CG   . MET   A 185 ? 1.2850 1.7223 1.7833 -0.1723 -0.0054 -0.3179 212 MET   A CG   
1221 S  SD   . MET   A 185 ? 1.4327 1.8676 1.9005 -0.1677 -0.0218 -0.3265 212 MET   A SD   
1222 C  CE   . MET   A 185 ? 1.2077 1.7347 1.6690 -0.1445 -0.0591 -0.3421 212 MET   A CE   
1223 N  N    . PRO   A 186 ? 1.3400 2.0598 1.9872 -0.1801 -0.0593 -0.4610 213 PRO   A N    
1224 C  CA   . PRO   A 186 ? 1.1233 1.9158 1.7842 -0.1634 -0.0761 -0.4803 213 PRO   A CA   
1225 C  C    . PRO   A 186 ? 1.1107 1.9370 1.7469 -0.1351 -0.0960 -0.4494 213 PRO   A C    
1226 O  O    . PRO   A 186 ? 1.0167 1.8788 1.6771 -0.1290 -0.0967 -0.4544 213 PRO   A O    
1227 C  CB   . PRO   A 186 ? 0.8973 1.7292 1.5404 -0.1516 -0.0945 -0.5072 213 PRO   A CB   
1228 C  CG   . PRO   A 186 ? 0.8220 1.5956 1.4617 -0.1716 -0.0788 -0.5123 213 PRO   A CG   
1229 C  CD   . PRO   A 186 ? 1.1148 1.8273 1.7359 -0.1782 -0.0683 -0.4723 213 PRO   A CD   
1230 N  N    . TYR   A 187 ? 1.2180 2.0169 1.7957 -0.1134 -0.1077 -0.4106 214 TYR   A N    
1231 C  CA   . TYR   A 187 ? 1.1080 1.9168 1.6506 -0.0814 -0.1209 -0.3718 214 TYR   A CA   
1232 C  C    . TYR   A 187 ? 1.1658 1.8903 1.6513 -0.0732 -0.1125 -0.3233 214 TYR   A C    
1233 O  O    . TYR   A 187 ? 1.0936 1.7998 1.5439 -0.0676 -0.1193 -0.3150 214 TYR   A O    
1234 C  CB   . TYR   A 187 ? 1.0398 1.9345 1.5693 -0.0507 -0.1521 -0.3807 214 TYR   A CB   
1235 C  CG   . TYR   A 187 ? 1.1185 2.0232 1.6140 -0.0145 -0.1637 -0.3382 214 TYR   A CG   
1236 C  CD1  . TYR   A 187 ? 1.0103 1.9513 1.5342 -0.0048 -0.1649 -0.3376 214 TYR   A CD1  
1237 C  CD2  . TYR   A 187 ? 1.1094 1.9867 1.5486 0.0101  -0.1713 -0.2990 214 TYR   A CD2  
1238 C  CE1  . TYR   A 187 ? 1.0992 2.0462 1.5955 0.0294  -0.1733 -0.2985 214 TYR   A CE1  
1239 C  CE2  . TYR   A 187 ? 1.1834 2.0651 1.5974 0.0429  -0.1779 -0.2595 214 TYR   A CE2  
1240 C  CZ   . TYR   A 187 ? 1.2561 2.1715 1.6986 0.0529  -0.1788 -0.2592 214 TYR   A CZ   
1241 O  OH   . TYR   A 187 ? 1.3971 2.3139 1.8180 0.0865  -0.1832 -0.2197 214 TYR   A OH   
1242 N  N    . LEU   A 188 ? 1.1904 1.8673 1.6693 -0.0725 -0.0975 -0.2944 215 LEU   A N    
1243 C  CA   . LEU   A 188 ? 1.0077 1.6113 1.4378 -0.0639 -0.0903 -0.2523 215 LEU   A CA   
1244 C  C    . LEU   A 188 ? 0.9881 1.6093 1.3876 -0.0304 -0.1072 -0.2217 215 LEU   A C    
1245 O  O    . LEU   A 188 ? 1.0083 1.6781 1.4261 -0.0148 -0.1156 -0.2226 215 LEU   A O    
1246 C  CB   . LEU   A 188 ? 0.9265 1.4726 1.3638 -0.0782 -0.0652 -0.2388 215 LEU   A CB   
1247 C  CG   . LEU   A 188 ? 0.9302 1.4301 1.3812 -0.1069 -0.0418 -0.2516 215 LEU   A CG   
1248 C  CD1  . LEU   A 188 ? 0.8776 1.3229 1.3250 -0.1134 -0.0172 -0.2308 215 LEU   A CD1  
1249 C  CD2  . LEU   A 188 ? 0.9126 1.3765 1.3283 -0.1075 -0.0455 -0.2443 215 LEU   A CD2  
1250 N  N    . LYS   A 189 ? 0.9745 1.5557 1.3304 -0.0189 -0.1103 -0.1942 216 LYS   A N    
1251 C  CA   . LYS   A 189 ? 0.8575 1.4488 1.1870 0.0125  -0.1220 -0.1625 216 LYS   A CA   
1252 C  C    . LYS   A 189 ? 0.8288 1.3976 1.1649 0.0213  -0.1132 -0.1414 216 LYS   A C    
1253 O  O    . LYS   A 189 ? 0.8823 1.3980 1.2191 0.0061  -0.0966 -0.1366 216 LYS   A O    
1254 C  CB   . LYS   A 189 ? 0.9340 1.4790 1.2219 0.0185  -0.1220 -0.1382 216 LYS   A CB   
1255 C  CG   . LYS   A 189 ? 1.0034 1.5492 1.2681 0.0496  -0.1284 -0.1023 216 LYS   A CG   
1256 C  CD   . LYS   A 189 ? 1.0620 1.5995 1.2936 0.0593  -0.1338 -0.0881 216 LYS   A CD   
1257 C  CE   . LYS   A 189 ? 1.1636 1.6891 1.3765 0.0880  -0.1332 -0.0481 216 LYS   A CE   
1258 N  NZ   . LYS   A 189 ? 1.0279 1.6231 1.2380 0.1188  -0.1468 -0.0404 216 LYS   A NZ   
1259 N  N    . GLU   A 190 ? 0.8214 1.4335 1.1624 0.0483  -0.1239 -0.1291 217 GLU   A N    
1260 C  CA   . GLU   A 190 ? 0.7930 1.3865 1.1418 0.0605  -0.1161 -0.1089 217 GLU   A CA   
1261 C  C    . GLU   A 190 ? 0.8125 1.3472 1.1307 0.0731  -0.1102 -0.0738 217 GLU   A C    
1262 O  O    . GLU   A 190 ? 0.7489 1.2807 1.0422 0.0856  -0.1167 -0.0579 217 GLU   A O    
1263 C  CB   . GLU   A 190 ? 0.8398 1.5030 1.2086 0.0870  -0.1287 -0.1083 217 GLU   A CB   
1264 C  CG   . GLU   A 190 ? 0.9152 1.5767 1.3107 0.0905  -0.1194 -0.1056 217 GLU   A CG   
1265 C  CD   . GLU   A 190 ? 0.7746 1.4828 1.2116 0.0726  -0.1183 -0.1417 217 GLU   A CD   
1266 O  OE1  . GLU   A 190 ? 1.0950 1.8378 1.5436 0.0570  -0.1250 -0.1709 217 GLU   A OE1  
1267 O  OE2  . GLU   A 190 ? 0.7729 1.4839 1.2344 0.0736  -0.1095 -0.1426 217 GLU   A OE2  
1268 N  N    . GLU   A 191 ? 0.7921 1.2821 1.1147 0.0697  -0.0968 -0.0639 218 GLU   A N    
1269 C  CA   . GLU   A 191 ? 0.6529 1.0916 0.9566 0.0815  -0.0905 -0.0358 218 GLU   A CA   
1270 C  C    . GLU   A 191 ? 0.6348 1.1013 0.9420 0.1143  -0.0968 -0.0116 218 GLU   A C    
1271 O  O    . GLU   A 191 ? 0.7178 1.2186 1.0481 0.1281  -0.0982 -0.0123 218 GLU   A O    
1272 C  CB   . GLU   A 191 ? 0.6965 1.0913 1.0077 0.0720  -0.0758 -0.0369 218 GLU   A CB   
1273 C  CG   . GLU   A 191 ? 0.6663 1.0032 0.9599 0.0751  -0.0684 -0.0190 218 GLU   A CG   
1274 C  CD   . GLU   A 191 ? 0.7941 1.1286 1.0980 0.1012  -0.0673 0.0041  218 GLU   A CD   
1275 O  OE1  . GLU   A 191 ? 0.6970 1.0460 1.0234 0.1115  -0.0636 0.0035  218 GLU   A OE1  
1276 O  OE2  . GLU   A 191 ? 0.6945 1.0119 0.9865 0.1118  -0.0680 0.0234  218 GLU   A OE2  
1277 N  N    . PRO   A 192 ? 0.6185 1.0717 0.9049 0.1290  -0.0987 0.0119  219 PRO   A N    
1278 C  CA   . PRO   A 192 ? 0.6288 1.1187 0.9160 0.1633  -0.1040 0.0371  219 PRO   A CA   
1279 C  C    . PRO   A 192 ? 0.7054 1.1620 1.0048 0.1842  -0.0914 0.0663  219 PRO   A C    
1280 O  O    . PRO   A 192 ? 0.8667 1.3531 1.1692 0.2159  -0.0929 0.0909  219 PRO   A O    
1281 C  CB   . PRO   A 192 ? 0.6397 1.1322 0.8979 0.1679  -0.1092 0.0482  219 PRO   A CB   
1282 C  CG   . PRO   A 192 ? 0.5810 1.0110 0.8265 0.1407  -0.1007 0.0412  219 PRO   A CG   
1283 C  CD   . PRO   A 192 ? 0.6739 1.0842 0.9350 0.1157  -0.0957 0.0159  219 PRO   A CD   
1284 N  N    . TYR   A 193 ? 0.7163 1.1153 1.0238 0.1699  -0.0784 0.0639  220 TYR   A N    
1285 C  CA   . TYR   A 193 ? 0.7534 1.1160 1.0771 0.1876  -0.0647 0.0878  220 TYR   A CA   
1286 C  C    . TYR   A 193 ? 0.6641 1.0216 1.0157 0.1885  -0.0577 0.0775  220 TYR   A C    
1287 O  O    . TYR   A 193 ? 0.7472 1.1065 1.1196 0.2133  -0.0506 0.0967  220 TYR   A O    
1288 C  CB   . TYR   A 193 ? 0.6701 0.9703 0.9851 0.1741  -0.0542 0.0930  220 TYR   A CB   
1289 C  CG   . TYR   A 193 ? 0.8474 1.1490 1.1355 0.1718  -0.0592 0.1024  220 TYR   A CG   
1290 C  CD1  . TYR   A 193 ? 0.7269 1.0569 1.0073 0.1983  -0.0606 0.1302  220 TYR   A CD1  
1291 C  CD2  . TYR   A 193 ? 0.6503 0.9268 0.9196 0.1455  -0.0616 0.0846  220 TYR   A CD2  
1292 C  CE1  . TYR   A 193 ? 0.7871 1.1212 1.0417 0.1974  -0.0642 0.1383  220 TYR   A CE1  
1293 C  CE2  . TYR   A 193 ? 0.7077 0.9863 0.9536 0.1438  -0.0656 0.0920  220 TYR   A CE2  
1294 C  CZ   . TYR   A 193 ? 0.7974 1.1052 1.0362 0.1691  -0.0668 0.1179  220 TYR   A CZ   
1295 O  OH   . TYR   A 193 ? 0.8131 1.1258 1.0276 0.1688  -0.0699 0.1249  220 TYR   A OH   
1296 N  N    . PHE   A 194 ? 0.6224 0.9731 0.9753 0.1637  -0.0577 0.0491  221 PHE   A N    
1297 C  CA   . PHE   A 194 ? 0.6261 0.9670 1.0026 0.1631  -0.0487 0.0382  221 PHE   A CA   
1298 C  C    . PHE   A 194 ? 0.7963 1.1854 1.1854 0.1568  -0.0542 0.0173  221 PHE   A C    
1299 O  O    . PHE   A 194 ? 0.8083 1.1921 1.2149 0.1532  -0.0460 0.0051  221 PHE   A O    
1300 C  CB   . PHE   A 194 ? 0.7734 1.0604 1.1427 0.1425  -0.0390 0.0244  221 PHE   A CB   
1301 C  CG   . PHE   A 194 ? 0.7593 1.0014 1.1205 0.1439  -0.0339 0.0384  221 PHE   A CG   
1302 C  CD1  . PHE   A 194 ? 0.7386 0.9603 1.1222 0.1643  -0.0242 0.0580  221 PHE   A CD1  
1303 C  CD2  . PHE   A 194 ? 0.5463 0.7665 0.8818 0.1250  -0.0371 0.0317  221 PHE   A CD2  
1304 C  CE1  . PHE   A 194 ? 0.7447 0.9256 1.1283 0.1636  -0.0168 0.0692  221 PHE   A CE1  
1305 C  CE2  . PHE   A 194 ? 0.5965 0.7792 0.9289 0.1255  -0.0320 0.0426  221 PHE   A CE2  
1306 C  CZ   . PHE   A 194 ? 0.7995 0.9629 1.1575 0.1438  -0.0215 0.0605  221 PHE   A CZ   
1307 N  N    . GLY   A 195 ? 0.8445 1.2830 1.2282 0.1553  -0.0671 0.0106  222 GLY   A N    
1308 C  CA   . GLY   A 195 ? 0.5615 1.0482 0.9645 0.1463  -0.0712 -0.0134 222 GLY   A CA   
1309 C  C    . GLY   A 195 ? 0.6348 1.0967 1.0364 0.1154  -0.0616 -0.0369 222 GLY   A C    
1310 O  O    . GLY   A 195 ? 0.5634 1.0464 0.9879 0.1092  -0.0557 -0.0527 222 GLY   A O    
1311 N  N    . MET   A 196 ? 0.8120 1.2304 1.1874 0.0975  -0.0583 -0.0378 223 MET   A N    
1312 C  CA   . MET   A 196 ? 0.6704 1.0606 1.0394 0.0722  -0.0469 -0.0544 223 MET   A CA   
1313 C  C    . MET   A 196 ? 0.6607 1.0839 1.0401 0.0523  -0.0478 -0.0761 223 MET   A C    
1314 O  O    . MET   A 196 ? 0.6421 1.0443 1.0200 0.0324  -0.0346 -0.0877 223 MET   A O    
1315 C  CB   . MET   A 196 ? 0.6728 1.0085 1.0108 0.0636  -0.0437 -0.0470 223 MET   A CB   
1316 C  CG   . MET   A 196 ? 0.8039 1.1016 1.1389 0.0772  -0.0387 -0.0334 223 MET   A CG   
1317 S  SD   . MET   A 196 ? 0.7716 1.0129 1.0757 0.0643  -0.0345 -0.0328 223 MET   A SD   
1318 C  CE   . MET   A 196 ? 0.7723 0.9861 1.0847 0.0696  -0.0224 -0.0400 223 MET   A CE   
1319 N  N    . GLY   A 197 ? 0.6906 1.1659 1.0818 0.0581  -0.0616 -0.0824 224 GLY   A N    
1320 C  CA   . GLY   A 197 ? 0.6392 1.1503 1.0496 0.0381  -0.0621 -0.1088 224 GLY   A CA   
1321 C  C    . GLY   A 197 ? 0.6991 1.1927 1.0893 0.0214  -0.0648 -0.1156 224 GLY   A C    
1322 O  O    . GLY   A 197 ? 0.6743 1.1487 1.0361 0.0308  -0.0730 -0.0997 224 GLY   A O    
1323 N  N    . LYS   A 198 ? 0.7289 1.2271 1.1366 -0.0036 -0.0553 -0.1390 225 LYS   A N    
1324 C  CA   . LYS   A 198 ? 0.7197 1.2099 1.1172 -0.0197 -0.0576 -0.1507 225 LYS   A CA   
1325 C  C    . LYS   A 198 ? 0.6659 1.0869 1.0260 -0.0256 -0.0484 -0.1330 225 LYS   A C    
1326 O  O    . LYS   A 198 ? 0.8310 1.2109 1.1823 -0.0288 -0.0334 -0.1230 225 LYS   A O    
1327 C  CB   . LYS   A 198 ? 0.8062 1.3186 1.2421 -0.0453 -0.0461 -0.1819 225 LYS   A CB   
1328 C  CG   . LYS   A 198 ? 0.7025 1.2901 1.1703 -0.0446 -0.0625 -0.2105 225 LYS   A CG   
1329 C  CD   . LYS   A 198 ? 0.7133 1.3578 1.2046 -0.0245 -0.0729 -0.2114 225 LYS   A CD   
1330 C  CE   . LYS   A 198 ? 0.7237 1.4527 1.2452 -0.0201 -0.0920 -0.2420 225 LYS   A CE   
1331 N  NZ   . LYS   A 198 ? 0.7752 1.5236 1.2630 -0.0004 -0.1134 -0.2332 225 LYS   A NZ   
1332 N  N    . MET   A 199 ? 0.7607 1.1735 1.0984 -0.0257 -0.0579 -0.1308 226 MET   A N    
1333 C  CA   . MET   A 199 ? 0.8057 1.1603 1.1086 -0.0288 -0.0526 -0.1151 226 MET   A CA   
1334 C  C    . MET   A 199 ? 0.8131 1.1532 1.1158 -0.0498 -0.0457 -0.1310 226 MET   A C    
1335 O  O    . MET   A 199 ? 0.9540 1.3329 1.2743 -0.0565 -0.0534 -0.1522 226 MET   A O    
1336 C  CB   . MET   A 199 ? 0.7894 1.1411 1.0664 -0.0092 -0.0671 -0.0952 226 MET   A CB   
1337 C  CG   . MET   A 199 ? 0.7356 1.0642 1.0038 0.0084  -0.0657 -0.0723 226 MET   A CG   
1338 S  SD   . MET   A 199 ? 0.8116 1.1310 1.0558 0.0285  -0.0765 -0.0479 226 MET   A SD   
1339 C  CE   . MET   A 199 ? 0.8196 1.1974 1.0650 0.0318  -0.0916 -0.0600 226 MET   A CE   
1340 N  N    . ALA   A 200 ? 0.6683 0.9546 0.9519 -0.0585 -0.0311 -0.1219 227 ALA   A N    
1341 C  CA   . ALA   A 200 ? 0.7176 0.9787 0.9947 -0.0741 -0.0233 -0.1301 227 ALA   A CA   
1342 C  C    . ALA   A 200 ? 0.7252 0.9614 0.9671 -0.0656 -0.0336 -0.1163 227 ALA   A C    
1343 O  O    . ALA   A 200 ? 0.8409 1.0819 1.0808 -0.0724 -0.0378 -0.1273 227 ALA   A O    
1344 C  CB   . ALA   A 200 ? 0.7166 0.9355 0.9936 -0.0859 0.0014  -0.1260 227 ALA   A CB   
1345 N  N    . VAL   A 201 ? 0.6022 0.8134 0.8198 -0.0513 -0.0367 -0.0948 228 VAL   A N    
1346 C  CA   . VAL   A 201 ? 0.7781 0.9699 0.9681 -0.0420 -0.0462 -0.0811 228 VAL   A CA   
1347 C  C    . VAL   A 201 ? 0.7215 0.9270 0.9099 -0.0230 -0.0565 -0.0660 228 VAL   A C    
1348 O  O    . VAL   A 201 ? 0.7729 0.9723 0.9681 -0.0168 -0.0518 -0.0600 228 VAL   A O    
1349 C  CB   . VAL   A 201 ? 0.6761 0.8175 0.8421 -0.0444 -0.0361 -0.0714 228 VAL   A CB   
1350 C  CG1  . VAL   A 201 ? 0.7367 0.8628 0.8802 -0.0370 -0.0456 -0.0611 228 VAL   A CG1  
1351 C  CG2  . VAL   A 201 ? 0.8524 0.9762 1.0226 -0.0604 -0.0206 -0.0817 228 VAL   A CG2  
1352 N  N    . SER   A 202 ? 0.6914 0.9151 0.8721 -0.0125 -0.0685 -0.0591 229 SER   A N    
1353 C  CA   . SER   A 202 ? 0.8154 1.0528 0.9985 0.0075  -0.0751 -0.0415 229 SER   A CA   
1354 C  C    . SER   A 202 ? 0.7419 0.9358 0.9129 0.0135  -0.0703 -0.0248 229 SER   A C    
1355 O  O    . SER   A 202 ? 0.6057 0.7646 0.7633 0.0038  -0.0647 -0.0278 229 SER   A O    
1356 C  CB   . SER   A 202 ? 0.6777 0.9541 0.8562 0.0196  -0.0870 -0.0375 229 SER   A CB   
1357 O  OG   . SER   A 202 ? 1.0608 1.3392 1.2279 0.0079  -0.0896 -0.0510 229 SER   A OG   
1358 N  N    . TRP   A 203 ? 0.8297 1.0278 1.0083 0.0308  -0.0718 -0.0079 230 TRP   A N    
1359 C  CA   . TRP   A 203 ? 0.6851 0.8457 0.8634 0.0360  -0.0659 0.0037  230 TRP   A CA   
1360 C  C    . TRP   A 203 ? 0.7377 0.8756 0.8982 0.0318  -0.0666 0.0083  230 TRP   A C    
1361 O  O    . TRP   A 203 ? 0.7124 0.8675 0.8642 0.0366  -0.0716 0.0157  230 TRP   A O    
1362 C  CB   . TRP   A 203 ? 0.6646 0.8342 0.8608 0.0560  -0.0644 0.0222  230 TRP   A CB   
1363 C  CG   . TRP   A 203 ? 0.6359 0.8241 0.8522 0.0623  -0.0626 0.0184  230 TRP   A CG   
1364 C  CD1  . TRP   A 203 ? 0.7274 0.9585 0.9548 0.0751  -0.0679 0.0228  230 TRP   A CD1  
1365 C  CD2  . TRP   A 203 ? 0.6957 0.8644 0.9236 0.0582  -0.0553 0.0084  230 TRP   A CD2  
1366 N  NE1  . TRP   A 203 ? 0.6234 0.8609 0.8707 0.0780  -0.0637 0.0167  230 TRP   A NE1  
1367 C  CE2  . TRP   A 203 ? 0.7316 0.9303 0.9788 0.0676  -0.0554 0.0079  230 TRP   A CE2  
1368 C  CE3  . TRP   A 203 ? 0.7132 0.8467 0.9360 0.0494  -0.0492 -0.0014 230 TRP   A CE3  
1369 C  CZ2  . TRP   A 203 ? 0.6241 0.8156 0.8860 0.0673  -0.0482 -0.0016 230 TRP   A CZ2  
1370 C  CZ3  . TRP   A 203 ? 0.7440 0.8732 0.9790 0.0504  -0.0428 -0.0115 230 TRP   A CZ3  
1371 C  CH2  . TRP   A 203 ? 0.6451 0.8015 0.8996 0.0586  -0.0417 -0.0112 230 TRP   A CH2  
1372 N  N    . HIS   A 204 ? 0.5813 0.6847 0.7363 0.0247  -0.0619 0.0030  231 HIS   A N    
1373 C  CA   . HIS   A 204 ? 0.6673 0.7504 0.8079 0.0203  -0.0626 0.0047  231 HIS   A CA   
1374 C  C    . HIS   A 204 ? 0.6910 0.7439 0.8341 0.0183  -0.0582 -0.0015 231 HIS   A C    
1375 O  O    . HIS   A 204 ? 0.6845 0.7326 0.8347 0.0187  -0.0549 -0.0099 231 HIS   A O    
1376 C  CB   . HIS   A 204 ? 0.6306 0.7173 0.7518 0.0083  -0.0653 -0.0060 231 HIS   A CB   
1377 C  CG   . HIS   A 204 ? 0.7048 0.7761 0.8191 -0.0018 -0.0601 -0.0191 231 HIS   A CG   
1378 N  ND1  . HIS   A 204 ? 0.7810 0.8642 0.9047 -0.0049 -0.0560 -0.0262 231 HIS   A ND1  
1379 C  CD2  . HIS   A 204 ? 0.6890 0.7353 0.7875 -0.0070 -0.0567 -0.0241 231 HIS   A CD2  
1380 C  CE1  . HIS   A 204 ? 0.6371 0.7015 0.7503 -0.0117 -0.0484 -0.0332 231 HIS   A CE1  
1381 N  NE2  . HIS   A 204 ? 0.7442 0.7865 0.8405 -0.0118 -0.0492 -0.0315 231 HIS   A NE2  
1382 N  N    . HIS   A 205 ? 0.8210 0.8578 0.9591 0.0172  -0.0585 0.0007  232 HIS   A N    
1383 C  CA   . HIS   A 205 ? 0.6534 0.6688 0.7880 0.0138  -0.0576 -0.0111 232 HIS   A CA   
1384 C  C    . HIS   A 205 ? 0.6961 0.7062 0.8040 0.0063  -0.0601 -0.0172 232 HIS   A C    
1385 O  O    . HIS   A 205 ? 0.7544 0.7726 0.8518 0.0027  -0.0621 -0.0124 232 HIS   A O    
1386 C  CB   . HIS   A 205 ? 0.5936 0.5964 0.7472 0.0174  -0.0552 -0.0076 232 HIS   A CB   
1387 C  CG   . HIS   A 205 ? 0.5803 0.5844 0.7640 0.0260  -0.0488 0.0044  232 HIS   A CG   
1388 N  ND1  . HIS   A 205 ? 0.7085 0.7051 0.9172 0.0297  -0.0441 -0.0043 232 HIS   A ND1  
1389 C  CD2  . HIS   A 205 ? 0.6798 0.6916 0.8730 0.0338  -0.0446 0.0255  232 HIS   A CD2  
1390 C  CE1  . HIS   A 205 ? 0.6802 0.6760 0.9154 0.0387  -0.0362 0.0118  232 HIS   A CE1  
1391 N  NE2  . HIS   A 205 ? 0.7019 0.7075 0.9266 0.0425  -0.0360 0.0320  232 HIS   A NE2  
1392 N  N    . ASP   A 206 ? 0.9007 0.8989 0.9979 0.0058  -0.0593 -0.0282 233 ASP   A N    
1393 C  CA   . ASP   A 206 ? 0.8590 0.8485 0.9319 0.0023  -0.0596 -0.0312 233 ASP   A CA   
1394 C  C    . ASP   A 206 ? 0.7916 0.7748 0.8653 0.0033  -0.0636 -0.0301 233 ASP   A C    
1395 O  O    . ASP   A 206 ? 0.7978 0.7776 0.8847 0.0074  -0.0654 -0.0366 233 ASP   A O    
1396 C  CB   . ASP   A 206 ? 0.8754 0.8583 0.9333 0.0064  -0.0563 -0.0398 233 ASP   A CB   
1397 C  CG   . ASP   A 206 ? 0.9721 0.9596 1.0260 0.0039  -0.0486 -0.0390 233 ASP   A CG   
1398 O  OD1  . ASP   A 206 ? 1.0607 1.0586 1.1257 -0.0024 -0.0476 -0.0348 233 ASP   A OD1  
1399 O  OD2  . ASP   A 206 ? 0.9882 0.9722 1.0285 0.0092  -0.0430 -0.0428 233 ASP   A OD2  
1400 N  N    . GLU   A 207 ? 0.8734 0.8574 0.9368 -0.0009 -0.0645 -0.0244 234 GLU   A N    
1401 C  CA   . GLU   A 207 ? 0.7426 0.7230 0.8072 0.0000  -0.0669 -0.0222 234 GLU   A CA   
1402 C  C    . GLU   A 207 ? 0.8877 0.8575 0.9367 0.0024  -0.0684 -0.0305 234 GLU   A C    
1403 O  O    . GLU   A 207 ? 0.6849 0.6488 0.7165 0.0041  -0.0661 -0.0341 234 GLU   A O    
1404 C  CB   . GLU   A 207 ? 0.8576 0.8470 0.9153 -0.0035 -0.0672 -0.0146 234 GLU   A CB   
1405 C  CG   . GLU   A 207 ? 0.8924 0.8981 0.9645 0.0000  -0.0666 -0.0028 234 GLU   A CG   
1406 C  CD   . GLU   A 207 ? 1.0643 1.0866 1.1251 -0.0007 -0.0683 0.0013  234 GLU   A CD   
1407 O  OE1  . GLU   A 207 ? 1.2539 1.2966 1.3206 0.0055  -0.0684 0.0120  234 GLU   A OE1  
1408 O  OE2  . GLU   A 207 ? 1.0327 1.0495 1.0786 -0.0057 -0.0691 -0.0065 234 GLU   A OE2  
1409 N  N    . ASN   A 208 ? 0.8906 0.8596 0.9473 0.0042  -0.0710 -0.0321 235 ASN   A N    
1410 C  CA   . ASN   A 208 ? 0.8760 0.8401 0.9187 0.0085  -0.0738 -0.0388 235 ASN   A CA   
1411 C  C    . ASN   A 208 ? 0.8217 0.7862 0.8546 0.0168  -0.0758 -0.0493 235 ASN   A C    
1412 O  O    . ASN   A 208 ? 0.9126 0.8714 0.9206 0.0226  -0.0739 -0.0482 235 ASN   A O    
1413 C  CB   . ASN   A 208 ? 0.9227 0.8801 0.9438 0.0058  -0.0711 -0.0331 235 ASN   A CB   
1414 C  CG   . ASN   A 208 ? 1.0676 1.0181 1.0723 0.0133  -0.0722 -0.0371 235 ASN   A CG   
1415 O  OD1  . ASN   A 208 ? 1.0847 1.0252 1.0696 0.0174  -0.0676 -0.0354 235 ASN   A OD1  
1416 N  ND2  . ASN   A 208 ? 1.1052 1.0617 1.1202 0.0162  -0.0766 -0.0413 235 ASN   A ND2  
1417 N  N    . LEU   A 209 ? 0.7471 0.7193 0.8007 0.0189  -0.0782 -0.0593 236 LEU   A N    
1418 C  CA   . LEU   A 209 ? 0.7253 0.7059 0.7717 0.0291  -0.0817 -0.0737 236 LEU   A CA   
1419 C  C    . LEU   A 209 ? 0.7524 0.7461 0.8242 0.0324  -0.0886 -0.0926 236 LEU   A C    
1420 O  O    . LEU   A 209 ? 0.6107 0.6032 0.7152 0.0246  -0.0869 -0.0935 236 LEU   A O    
1421 C  CB   . LEU   A 209 ? 0.8771 0.8599 0.9284 0.0292  -0.0782 -0.0761 236 LEU   A CB   
1422 C  CG   . LEU   A 209 ? 0.9932 0.9680 1.0292 0.0243  -0.0705 -0.0614 236 LEU   A CG   
1423 C  CD1  . LEU   A 209 ? 0.7984 0.7794 0.8422 0.0265  -0.0675 -0.0669 236 LEU   A CD1  
1424 C  CD2  . LEU   A 209 ? 0.8042 0.7708 0.8078 0.0285  -0.0657 -0.0538 236 LEU   A CD2  
1425 N  N    . VAL   A 210 ? 0.6838 0.6925 0.7420 0.0452  -0.0952 -0.1079 237 VAL   A N    
1426 C  CA   . VAL   A 210 ? 0.6957 0.7247 0.7831 0.0487  -0.1032 -0.1336 237 VAL   A CA   
1427 C  C    . VAL   A 210 ? 0.8012 0.8320 0.9265 0.0419  -0.1003 -0.1468 237 VAL   A C    
1428 O  O    . VAL   A 210 ? 0.7236 0.7494 0.8406 0.0426  -0.0961 -0.1423 237 VAL   A O    
1429 C  CB   . VAL   A 210 ? 0.7531 0.8063 0.8148 0.0679  -0.1123 -0.1494 237 VAL   A CB   
1430 C  CG1  . VAL   A 210 ? 0.6669 0.7490 0.7633 0.0713  -0.1226 -0.1821 237 VAL   A CG1  
1431 C  CG2  . VAL   A 210 ? 0.8170 0.8632 0.8410 0.0768  -0.1116 -0.1314 237 VAL   A CG2  
1432 N  N    . ASP   A 211 ? 0.7765 0.8128 0.9476 0.0351  -0.1004 -0.1626 238 ASP   A N    
1433 C  CA   . ASP   A 211 ? 0.6070 0.6404 0.8224 0.0283  -0.0943 -0.1748 238 ASP   A CA   
1434 C  C    . ASP   A 211 ? 0.8184 0.8698 1.0284 0.0382  -0.0999 -0.1989 238 ASP   A C    
1435 O  O    . ASP   A 211 ? 0.7691 0.8473 0.9673 0.0498  -0.1108 -0.2226 238 ASP   A O    
1436 C  CB   . ASP   A 211 ? 0.7165 0.7546 0.9871 0.0202  -0.0914 -0.1924 238 ASP   A CB   
1437 C  CG   . ASP   A 211 ? 0.8866 0.9069 1.2068 0.0104  -0.0771 -0.1893 238 ASP   A CG   
1438 O  OD1  . ASP   A 211 ? 0.9701 0.9689 1.2889 0.0053  -0.0664 -0.1577 238 ASP   A OD1  
1439 O  OD2  . ASP   A 211 ? 0.7855 0.8150 1.1470 0.0093  -0.0761 -0.2190 238 ASP   A OD2  
1440 N  N    . ARG   A 212 ? 0.8066 0.8465 1.0230 0.0358  -0.0926 -0.1925 239 ARG   A N    
1441 C  CA   . ARG   A 212 ? 0.7410 0.7967 0.9548 0.0447  -0.0953 -0.2143 239 ARG   A CA   
1442 C  C    . ARG   A 212 ? 0.7260 0.7975 0.8828 0.0600  -0.1019 -0.2115 239 ARG   A C    
1443 O  O    . ARG   A 212 ? 0.7343 0.8300 0.8827 0.0724  -0.1069 -0.2350 239 ARG   A O    
1444 C  CB   . ARG   A 212 ? 0.7602 0.8372 1.0221 0.0451  -0.0997 -0.2562 239 ARG   A CB   
1445 C  CG   . ARG   A 212 ? 0.8176 0.8747 1.1434 0.0304  -0.0877 -0.2582 239 ARG   A CG   
1446 C  CD   . ARG   A 212 ? 0.9037 0.9817 1.2858 0.0285  -0.0901 -0.3046 239 ARG   A CD   
1447 N  NE   . ARG   A 212 ? 1.0634 1.1298 1.4900 0.0244  -0.0789 -0.3174 239 ARG   A NE   
1448 C  CZ   . ARG   A 212 ? 1.1328 1.1684 1.6072 0.0133  -0.0613 -0.3015 239 ARG   A CZ   
1449 N  NH1  . ARG   A 212 ? 1.1221 1.1376 1.6047 0.0052  -0.0528 -0.2721 239 ARG   A NH1  
1450 N  NH2  . ARG   A 212 ? 1.0206 1.0459 1.5350 0.0124  -0.0507 -0.3140 239 ARG   A NH2  
1451 N  N    . SER   A 213 ? 0.7984 0.8570 0.9168 0.0605  -0.1001 -0.1832 240 SER   A N    
1452 C  CA   . SER   A 213 ? 0.8287 0.8953 0.8955 0.0752  -0.1007 -0.1740 240 SER   A CA   
1453 C  C    . SER   A 213 ? 0.9321 0.9876 0.9836 0.0741  -0.0905 -0.1586 240 SER   A C    
1454 O  O    . SER   A 213 ? 0.8063 0.8430 0.8759 0.0608  -0.0835 -0.1444 240 SER   A O    
1455 C  CB   . SER   A 213 ? 0.7895 0.8439 0.8279 0.0759  -0.1002 -0.1516 240 SER   A CB   
1456 O  OG   . SER   A 213 ? 0.7734 0.8008 0.8087 0.0625  -0.0906 -0.1249 240 SER   A OG   
1457 N  N    . ALA   A 214 ? 0.7810 0.8516 0.7988 0.0901  -0.0889 -0.1612 241 ALA   A N    
1458 C  CA   . ALA   A 214 ? 0.8598 0.9240 0.8650 0.0902  -0.0776 -0.1492 241 ALA   A CA   
1459 C  C    . ALA   A 214 ? 0.8365 0.8775 0.8170 0.0841  -0.0664 -0.1171 241 ALA   A C    
1460 O  O    . ALA   A 214 ? 0.8153 0.8459 0.7815 0.0835  -0.0671 -0.1047 241 ALA   A O    
1461 C  CB   . ALA   A 214 ? 0.8550 0.9467 0.8341 0.1111  -0.0776 -0.1640 241 ALA   A CB   
1462 N  N    . VAL   A 215 ? 0.6802 0.7141 0.6602 0.0791  -0.0552 -0.1062 242 VAL   A N    
1463 C  CA   . VAL   A 215 ? 0.7673 0.7826 0.7318 0.0718  -0.0422 -0.0812 242 VAL   A CA   
1464 C  C    . VAL   A 215 ? 0.6535 0.6749 0.6027 0.0790  -0.0284 -0.0761 242 VAL   A C    
1465 O  O    . VAL   A 215 ? 0.7181 0.7496 0.6852 0.0777  -0.0279 -0.0866 242 VAL   A O    
1466 C  CB   . VAL   A 215 ? 0.8076 0.8092 0.8003 0.0521  -0.0423 -0.0727 242 VAL   A CB   
1467 C  CG1  . VAL   A 215 ? 0.7426 0.7333 0.7278 0.0438  -0.0284 -0.0554 242 VAL   A CG1  
1468 C  CG2  . VAL   A 215 ? 0.8214 0.8152 0.8219 0.0461  -0.0515 -0.0716 242 VAL   A CG2  
1469 N  N    . ALA   A 216 ? 0.7990 0.8132 0.7167 0.0876  -0.0150 -0.0589 243 ALA   A N    
1470 C  CA   . ALA   A 216 ? 0.9685 0.9865 0.8704 0.0953  0.0030  -0.0494 243 ALA   A CA   
1471 C  C    . ALA   A 216 ? 0.8641 0.8596 0.7731 0.0799  0.0208  -0.0288 243 ALA   A C    
1472 O  O    . ALA   A 216 ? 0.9556 0.9322 0.8599 0.0745  0.0241  -0.0171 243 ALA   A O    
1473 C  CB   . ALA   A 216 ? 0.8547 0.8857 0.7147 0.1221  0.0087  -0.0446 243 ALA   A CB   
1474 N  N    . VAL   A 217 ? 0.7725 0.7719 0.6964 0.0727  0.0328  -0.0273 244 VAL   A N    
1475 C  CA   . VAL   A 217 ? 0.8734 0.8580 0.8149 0.0553  0.0492  -0.0146 244 VAL   A CA   
1476 C  C    . VAL   A 217 ? 0.9010 0.8875 0.8321 0.0626  0.0744  -0.0029 244 VAL   A C    
1477 O  O    . VAL   A 217 ? 0.8252 0.8310 0.7556 0.0709  0.0754  -0.0108 244 VAL   A O    
1478 C  CB   . VAL   A 217 ? 0.8899 0.8823 0.8703 0.0364  0.0390  -0.0254 244 VAL   A CB   
1479 C  CG1  . VAL   A 217 ? 0.8971 0.8840 0.8993 0.0195  0.0556  -0.0183 244 VAL   A CG1  
1480 C  CG2  . VAL   A 217 ? 0.7644 0.7534 0.7543 0.0301  0.0185  -0.0320 244 VAL   A CG2  
1481 N  N    . TYR   A 218 ? 0.9380 0.9036 0.8635 0.0596  0.0969  0.0160  245 TYR   A N    
1482 C  CA   . TYR   A 218 ? 0.8679 0.8306 0.7926 0.0621  0.1269  0.0307  245 TYR   A CA   
1483 C  C    . TYR   A 218 ? 0.8778 0.8362 0.8479 0.0350  0.1368  0.0265  245 TYR   A C    
1484 O  O    . TYR   A 218 ? 0.9700 0.9101 0.9571 0.0198  0.1403  0.0285  245 TYR   A O    
1485 C  CB   . TYR   A 218 ? 0.8608 0.8018 0.7541 0.0783  0.1503  0.0563  245 TYR   A CB   
1486 C  CG   . TYR   A 218 ? 0.9460 0.8816 0.8358 0.0847  0.1866  0.0766  245 TYR   A CG   
1487 C  CD1  . TYR   A 218 ? 0.9049 0.8245 0.8344 0.0616  0.2108  0.0818  245 TYR   A CD1  
1488 C  CD2  . TYR   A 218 ? 1.1040 1.0536 0.9527 0.1144  0.1978  0.0895  245 TYR   A CD2  
1489 C  CE1  . TYR   A 218 ? 1.1272 1.0408 1.0589 0.0663  0.2475  0.1012  245 TYR   A CE1  
1490 C  CE2  . TYR   A 218 ? 1.1388 1.0838 0.9831 0.1220  0.2342  0.1115  245 TYR   A CE2  
1491 C  CZ   . TYR   A 218 ? 1.2430 1.1677 1.1306 0.0970  0.2602  0.1183  245 TYR   A CZ   
1492 O  OH   . TYR   A 218 ? 1.1377 1.0565 1.0263 0.1032  0.3000  0.1409  245 TYR   A OH   
1493 N  N    . SER   A 219 ? 0.9795 0.9582 0.9709 0.0297  0.1406  0.0181  246 SER   A N    
1494 C  CA   . SER   A 219 ? 0.9766 0.9615 1.0142 0.0059  0.1478  0.0100  246 SER   A CA   
1495 C  C    . SER   A 219 ? 1.1070 1.0827 1.1558 0.0023  0.1849  0.0246  246 SER   A C    
1496 O  O    . SER   A 219 ? 1.1013 1.0829 1.1295 0.0186  0.2012  0.0353  246 SER   A O    
1497 C  CB   . SER   A 219 ? 0.9836 0.9987 1.0433 0.0029  0.1299  -0.0079 246 SER   A CB   
1498 O  OG   . SER   A 219 ? 1.0853 1.1139 1.1896 -0.0173 0.1358  -0.0169 246 SER   A OG   
1499 N  N    . TYR   A 220 ? 1.0609 1.0235 1.1446 -0.0190 0.1998  0.0237  247 TYR   A N    
1500 C  CA   . TYR   A 220 ? 1.1240 1.0736 1.2301 -0.0268 0.2394  0.0365  247 TYR   A CA   
1501 C  C    . TYR   A 220 ? 1.1377 1.1051 1.3050 -0.0555 0.2416  0.0147  247 TYR   A C    
1502 O  O    . TYR   A 220 ? 1.1676 1.1241 1.3634 -0.0737 0.2431  0.0052  247 TYR   A O    
1503 C  CB   . TYR   A 220 ? 1.1593 1.0691 1.2493 -0.0218 0.2627  0.0585  247 TYR   A CB   
1504 C  CG   . TYR   A 220 ? 1.2810 1.1705 1.4064 -0.0346 0.3072  0.0710  247 TYR   A CG   
1505 C  CD1  . TYR   A 220 ? 1.2996 1.1984 1.4315 -0.0296 0.3353  0.0825  247 TYR   A CD1  
1506 C  CD2  . TYR   A 220 ? 1.3240 1.1842 1.4794 -0.0515 0.3236  0.0709  247 TYR   A CD2  
1507 C  CE1  . TYR   A 220 ? 1.4049 1.2836 1.5748 -0.0422 0.3800  0.0950  247 TYR   A CE1  
1508 C  CE2  . TYR   A 220 ? 1.2406 1.0791 1.4362 -0.0647 0.3678  0.0810  247 TYR   A CE2  
1509 C  CZ   . TYR   A 220 ? 1.3724 1.2196 1.5760 -0.0603 0.3968  0.0941  247 TYR   A CZ   
1510 O  OH   . TYR   A 220 ? 1.4709 1.2952 1.7200 -0.0744 0.4446  0.1052  247 TYR   A OH   
1511 N  N    . SER   A 221 ? 1.1333 1.1320 1.3220 -0.0581 0.2408  0.0042  248 SER   A N    
1512 C  CA   . SER   A 221 ? 1.1336 1.1566 1.3829 -0.0826 0.2464  -0.0167 248 SER   A CA   
1513 C  C    . SER   A 221 ? 1.1645 1.1690 1.4450 -0.0945 0.2915  -0.0060 248 SER   A C    
1514 O  O    . SER   A 221 ? 1.1842 1.1770 1.4441 -0.0803 0.3189  0.0166  248 SER   A O    
1515 C  CB   . SER   A 221 ? 1.1013 1.1651 1.3636 -0.0788 0.2314  -0.0300 248 SER   A CB   
1516 O  OG   . SER   A 221 ? 1.0104 1.0899 1.2561 -0.0709 0.1927  -0.0408 248 SER   A OG   
1517 N  N    . CYS   A 222 ? 1.2386 1.2417 1.5706 -0.1200 0.3009  -0.0231 249 CYS   A N    
1518 C  CA   . CYS   A 222 ? 1.3496 1.3276 1.7188 -0.1338 0.3475  -0.0134 249 CYS   A CA   
1519 C  C    . CYS   A 222 ? 1.4195 1.4206 1.8216 -0.1384 0.3733  -0.0134 249 CYS   A C    
1520 O  O    . CYS   A 222 ? 1.5664 1.5423 1.9692 -0.1338 0.4157  0.0116  249 CYS   A O    
1521 C  CB   . CYS   A 222 ? 1.3497 1.3260 1.7751 -0.1621 0.3496  -0.0399 249 CYS   A CB   
1522 S  SG   . CYS   A 222 ? 1.3146 1.2374 1.7136 -0.1586 0.3546  -0.0258 249 CYS   A SG   
1523 N  N    . GLU   A 223 ? 1.3226 1.3721 1.7520 -0.1454 0.3499  -0.0393 250 GLU   A N    
1524 C  CA   . GLU   A 223 ? 1.3682 1.4452 1.8318 -0.1495 0.3717  -0.0422 250 GLU   A CA   
1525 C  C    . GLU   A 223 ? 1.3113 1.4392 1.7778 -0.1437 0.3353  -0.0631 250 GLU   A C    
1526 O  O    . GLU   A 223 ? 1.3496 1.4826 1.7719 -0.1208 0.3238  -0.0504 250 GLU   A O    
1527 C  CB   . GLU   A 223 ? 1.2233 1.3058 1.7668 -0.1804 0.4043  -0.0603 250 GLU   A CB   
1528 N  N    . LEU   A 235 ? 1.0746 1.7164 1.7274 0.0586  0.0668  -0.1692 262 LEU   A N    
1529 C  CA   . LEU   A 235 ? 1.1005 1.7116 1.7346 0.0807  0.0687  -0.1569 262 LEU   A CA   
1530 C  C    . LEU   A 235 ? 1.2140 1.8136 1.8327 0.1026  0.0462  -0.1413 262 LEU   A C    
1531 O  O    . LEU   A 235 ? 1.2907 1.8559 1.8941 0.1192  0.0472  -0.1311 262 LEU   A O    
1532 C  CB   . LEU   A 235 ? 0.9136 1.5619 1.5853 0.0934  0.0794  -0.1659 262 LEU   A CB   
1533 N  N    . GLU   A 236 ? 1.2438 1.8738 1.8688 0.1030  0.0274  -0.1403 263 GLU   A N    
1534 C  CA   . GLU   A 236 ? 1.1146 1.7395 1.7260 0.1256  0.0081  -0.1220 263 GLU   A CA   
1535 C  C    . GLU   A 236 ? 1.1975 1.7554 1.7659 0.1222  0.0089  -0.1076 263 GLU   A C    
1536 O  O    . GLU   A 236 ? 1.1659 1.6883 1.7263 0.1368  0.0137  -0.0978 263 GLU   A O    
1537 C  CB   . GLU   A 236 ? 1.0354 1.7115 1.6572 0.1259  -0.0113 -0.1262 263 GLU   A CB   
1538 N  N    . GLY   A 237 ? 1.0178 1.5598 1.5624 0.1028  0.0046  -0.1088 264 GLY   A N    
1539 C  CA   . GLY   A 237 ? 0.9961 1.4798 1.5018 0.0986  0.0045  -0.0971 264 GLY   A CA   
1540 C  C    . GLY   A 237 ? 0.9713 1.4216 1.4552 0.0743  0.0193  -0.1057 264 GLY   A C    
1541 O  O    . GLY   A 237 ? 0.9986 1.4421 1.4866 0.0709  0.0361  -0.1131 264 GLY   A O    
1542 N  N    . ARG   A 238 ? 0.8706 1.3013 1.3303 0.0597  0.0144  -0.1034 265 ARG   A N    
1543 C  CA   . ARG   A 238 ? 0.9225 1.3208 1.3598 0.0394  0.0288  -0.1078 265 ARG   A CA   
1544 C  C    . ARG   A 238 ? 0.8684 1.2966 1.3295 0.0190  0.0386  -0.1221 265 ARG   A C    
1545 O  O    . ARG   A 238 ? 0.8709 1.3441 1.3602 0.0171  0.0281  -0.1315 265 ARG   A O    
1546 C  CB   . ARG   A 238 ? 0.8791 1.2387 1.2806 0.0347  0.0204  -0.0982 265 ARG   A CB   
1547 C  CG   . ARG   A 238 ? 0.7784 1.1590 1.1829 0.0278  0.0057  -0.0992 265 ARG   A CG   
1548 C  CD   . ARG   A 238 ? 0.8032 1.1718 1.1997 0.0039  0.0151  -0.1075 265 ARG   A CD   
1549 N  NE   . ARG   A 238 ? 0.7241 1.1128 1.1233 -0.0025 0.0008  -0.1125 265 ARG   A NE   
1550 C  CZ   . ARG   A 238 ? 0.7284 1.1095 1.1259 -0.0225 0.0065  -0.1218 265 ARG   A CZ   
1551 N  NH1  . ARG   A 238 ? 0.7713 1.1231 1.1642 -0.0375 0.0280  -0.1234 265 ARG   A NH1  
1552 N  NH2  . ARG   A 238 ? 0.7706 1.1745 1.1713 -0.0259 -0.0082 -0.1292 265 ARG   A NH2  
1553 N  N    . ASP   A 239 ? 0.8681 1.2729 1.3197 0.0048  0.0602  -0.1244 266 ASP   A N    
1554 C  CA   . ASP   A 239 ? 0.9176 1.3413 1.3957 -0.0169 0.0764  -0.1368 266 ASP   A CA   
1555 C  C    . ASP   A 239 ? 0.8774 1.2962 1.3511 -0.0322 0.0677  -0.1407 266 ASP   A C    
1556 O  O    . ASP   A 239 ? 0.8542 1.2288 1.2919 -0.0364 0.0702  -0.1303 266 ASP   A O    
1557 C  CB   . ASP   A 239 ? 0.9252 1.3187 1.3890 -0.0241 0.1054  -0.1316 266 ASP   A CB   
1558 C  CG   . ASP   A 239 ? 1.0209 1.4328 1.5215 -0.0459 0.1291  -0.1427 266 ASP   A CG   
1559 O  OD1  . ASP   A 239 ? 0.9987 1.4468 1.5376 -0.0582 0.1214  -0.1589 266 ASP   A OD1  
1560 O  OD2  . ASP   A 239 ? 1.1073 1.4993 1.6004 -0.0499 0.1570  -0.1357 266 ASP   A OD2  
1561 N  N    . PRO   A 240 ? 0.9079 1.3736 1.4175 -0.0397 0.0570  -0.1577 267 PRO   A N    
1562 C  CA   . PRO   A 240 ? 0.8693 1.3331 1.3751 -0.0533 0.0479  -0.1651 267 PRO   A CA   
1563 C  C    . PRO   A 240 ? 0.8651 1.3001 1.3766 -0.0781 0.0728  -0.1707 267 PRO   A C    
1564 O  O    . PRO   A 240 ? 0.8172 1.2358 1.3182 -0.0888 0.0687  -0.1738 267 PRO   A O    
1565 C  CB   . PRO   A 240 ? 0.8568 1.3899 1.4044 -0.0521 0.0303  -0.1868 267 PRO   A CB   
1566 C  CG   . PRO   A 240 ? 0.7031 1.2707 1.2716 -0.0340 0.0280  -0.1855 267 PRO   A CG   
1567 C  CD   . PRO   A 240 ? 0.7565 1.2839 1.3133 -0.0354 0.0525  -0.1737 267 PRO   A CD   
1568 N  N    . ASP   A 241 ? 0.8140 1.2416 1.3426 -0.0864 0.1006  -0.1704 268 ASP   A N    
1569 C  CA   . ASP   A 241 ? 0.8243 1.2218 1.3614 -0.1079 0.1298  -0.1711 268 ASP   A CA   
1570 C  C    . ASP   A 241 ? 0.8551 1.1900 1.3371 -0.1017 0.1403  -0.1458 268 ASP   A C    
1571 O  O    . ASP   A 241 ? 0.9530 1.2563 1.4329 -0.1159 0.1600  -0.1421 268 ASP   A O    
1572 C  CB   . ASP   A 241 ? 0.8695 1.2854 1.4486 -0.1178 0.1594  -0.1781 268 ASP   A CB   
1573 C  CG   . ASP   A 241 ? 0.9920 1.4655 1.6389 -0.1355 0.1586  -0.2100 268 ASP   A CG   
1574 O  OD1  . ASP   A 241 ? 1.0443 1.5491 1.7019 -0.1366 0.1320  -0.2273 268 ASP   A OD1  
1575 O  OD2  . ASP   A 241 ? 1.0680 1.5590 1.7587 -0.1477 0.1850  -0.2190 268 ASP   A OD2  
1576 N  N    . ILE   A 242 ? 0.9369 1.2548 1.3773 -0.0800 0.1283  -0.1298 269 ILE   A N    
1577 C  CA   . ILE   A 242 ? 0.8741 1.1418 1.2631 -0.0708 0.1364  -0.1092 269 ILE   A CA   
1578 C  C    . ILE   A 242 ? 0.7563 1.0059 1.1130 -0.0638 0.1101  -0.1043 269 ILE   A C    
1579 O  O    . ILE   A 242 ? 0.7074 0.9798 1.0690 -0.0551 0.0852  -0.1093 269 ILE   A O    
1580 C  CB   . ILE   A 242 ? 0.8315 1.0961 1.2003 -0.0520 0.1429  -0.1000 269 ILE   A CB   
1581 C  CG1  . ILE   A 242 ? 0.7139 0.9952 1.1121 -0.0581 0.1729  -0.1024 269 ILE   A CG1  
1582 C  CG2  . ILE   A 242 ? 0.8129 1.0352 1.1276 -0.0393 0.1460  -0.0832 269 ILE   A CG2  
1583 C  CD1  . ILE   A 242 ? 0.9277 1.2015 1.3537 -0.0806 0.2006  -0.1038 269 ILE   A CD1  
1584 N  N    . TRP   A 243 ? 0.7254 0.9347 1.0500 -0.0662 0.1172  -0.0929 270 TRP   A N    
1585 C  CA   . TRP   A 243 ? 0.8553 1.0462 1.1497 -0.0599 0.0948  -0.0879 270 TRP   A CA   
1586 C  C    . TRP   A 243 ? 0.8040 0.9847 1.0674 -0.0391 0.0817  -0.0792 270 TRP   A C    
1587 O  O    . TRP   A 243 ? 0.7291 0.8998 0.9761 -0.0291 0.0945  -0.0732 270 TRP   A O    
1588 C  CB   . TRP   A 243 ? 0.8386 0.9911 1.1104 -0.0673 0.1072  -0.0789 270 TRP   A CB   
1589 C  CG   . TRP   A 243 ? 0.8541 1.0134 1.1596 -0.0885 0.1155  -0.0915 270 TRP   A CG   
1590 C  CD1  . TRP   A 243 ? 0.7349 0.9031 1.0794 -0.1047 0.1410  -0.0996 270 TRP   A CD1  
1591 C  CD2  . TRP   A 243 ? 0.8431 1.0030 1.1509 -0.0966 0.0996  -0.1005 270 TRP   A CD2  
1592 N  NE1  . TRP   A 243 ? 0.8009 0.9749 1.1750 -0.1233 0.1414  -0.1161 270 TRP   A NE1  
1593 C  CE2  . TRP   A 243 ? 0.8894 1.0596 1.2393 -0.1179 0.1154  -0.1172 270 TRP   A CE2  
1594 C  CE3  . TRP   A 243 ? 0.8131 0.9669 1.0937 -0.0879 0.0749  -0.0973 270 TRP   A CE3  
1595 C  CZ2  . TRP   A 243 ? 0.9131 1.0894 1.2767 -0.1299 0.1057  -0.1331 270 TRP   A CZ2  
1596 C  CZ3  . TRP   A 243 ? 0.8796 1.0392 1.1705 -0.0988 0.0661  -0.1095 270 TRP   A CZ3  
1597 C  CH2  . TRP   A 243 ? 0.9187 1.0904 1.2498 -0.1192 0.0805  -0.1284 270 TRP   A CH2  
1598 N  N    . HIS   A 244 ? 0.8483 1.0331 1.1059 -0.0321 0.0575  -0.0797 271 HIS   A N    
1599 C  CA   . HIS   A 244 ? 0.6643 0.8385 0.9021 -0.0146 0.0453  -0.0745 271 HIS   A CA   
1600 C  C    . HIS   A 244 ? 0.7320 0.8829 0.9452 -0.0127 0.0308  -0.0686 271 HIS   A C    
1601 O  O    . HIS   A 244 ? 0.7911 0.9403 1.0045 -0.0231 0.0267  -0.0689 271 HIS   A O    
1602 C  CB   . HIS   A 244 ? 0.6741 0.8780 0.9382 -0.0046 0.0331  -0.0788 271 HIS   A CB   
1603 C  CG   . HIS   A 244 ? 0.7963 1.0253 1.0857 -0.0034 0.0459  -0.0854 271 HIS   A CG   
1604 N  ND1  . HIS   A 244 ? 0.7614 1.0126 1.0768 -0.0177 0.0587  -0.0929 271 HIS   A ND1  
1605 C  CD2  . HIS   A 244 ? 0.6602 0.8969 0.9569 0.0101  0.0490  -0.0875 271 HIS   A CD2  
1606 C  CE1  . HIS   A 244 ? 0.7181 0.9906 1.0544 -0.0129 0.0691  -0.0978 271 HIS   A CE1  
1607 N  NE2  . HIS   A 244 ? 0.7194 0.9833 1.0431 0.0046  0.0631  -0.0944 271 HIS   A NE2  
1608 N  N    . VAL   A 245 ? 0.7320 0.8670 0.9273 0.0005  0.0239  -0.0658 272 VAL   A N    
1609 C  CA   . VAL   A 245 ? 0.7564 0.8751 0.9378 0.0042  0.0089  -0.0616 272 VAL   A CA   
1610 C  C    . VAL   A 245 ? 0.7122 0.8394 0.9113 0.0164  -0.0018 -0.0618 272 VAL   A C    
1611 O  O    . VAL   A 245 ? 0.7476 0.8773 0.9541 0.0257  0.0027  -0.0671 272 VAL   A O    
1612 C  CB   . VAL   A 245 ? 0.8724 0.9633 1.0210 0.0083  0.0119  -0.0599 272 VAL   A CB   
1613 C  CG1  . VAL   A 245 ? 0.7157 0.8063 0.8565 0.0207  0.0186  -0.0663 272 VAL   A CG1  
1614 C  CG2  . VAL   A 245 ? 0.7165 0.7935 0.8569 0.0108  -0.0029 -0.0574 272 VAL   A CG2  
1615 N  N    . GLY   A 246 ? 0.6637 0.7963 0.8709 0.0176  -0.0141 -0.0554 273 GLY   A N    
1616 C  CA   . GLY   A 246 ? 0.6529 0.7918 0.8800 0.0308  -0.0209 -0.0503 273 GLY   A CA   
1617 C  C    . GLY   A 246 ? 0.6902 0.8021 0.9099 0.0362  -0.0253 -0.0473 273 GLY   A C    
1618 O  O    . GLY   A 246 ? 0.7127 0.8076 0.9115 0.0297  -0.0279 -0.0469 273 GLY   A O    
1619 N  N    . PHE   A 247 ? 0.6618 0.7699 0.9033 0.0482  -0.0248 -0.0461 274 PHE   A N    
1620 C  CA   . PHE   A 247 ? 0.6717 0.7550 0.9174 0.0524  -0.0264 -0.0463 274 PHE   A CA   
1621 C  C    . PHE   A 247 ? 0.7624 0.8460 1.0398 0.0654  -0.0249 -0.0344 274 PHE   A C    
1622 O  O    . PHE   A 247 ? 0.6875 0.7856 0.9852 0.0746  -0.0210 -0.0334 274 PHE   A O    
1623 C  CB   . PHE   A 247 ? 0.6410 0.7107 0.8822 0.0532  -0.0221 -0.0657 274 PHE   A CB   
1624 C  CG   . PHE   A 247 ? 0.6251 0.6870 0.8327 0.0452  -0.0237 -0.0724 274 PHE   A CG   
1625 C  CD1  . PHE   A 247 ? 0.7515 0.7978 0.9496 0.0419  -0.0296 -0.0714 274 PHE   A CD1  
1626 C  CD2  . PHE   A 247 ? 0.7094 0.7795 0.8960 0.0426  -0.0175 -0.0776 274 PHE   A CD2  
1627 C  CE1  . PHE   A 247 ? 0.7197 0.7602 0.8869 0.0375  -0.0310 -0.0760 274 PHE   A CE1  
1628 C  CE2  . PHE   A 247 ? 0.8444 0.9061 0.9994 0.0389  -0.0166 -0.0795 274 PHE   A CE2  
1629 C  CZ   . PHE   A 247 ? 0.8392 0.8866 0.9838 0.0370  -0.0243 -0.0788 274 PHE   A CZ   
1630 N  N    . LYS   A 248 ? 0.7643 0.8317 1.0472 0.0673  -0.0261 -0.0239 275 LYS   A N    
1631 C  CA   . LYS   A 248 ? 0.7177 0.7797 1.0315 0.0813  -0.0205 -0.0074 275 LYS   A CA   
1632 C  C    . LYS   A 248 ? 0.7098 0.7428 1.0352 0.0790  -0.0164 -0.0071 275 LYS   A C    
1633 O  O    . LYS   A 248 ? 0.7818 0.8064 1.0864 0.0677  -0.0215 -0.0152 275 LYS   A O    
1634 C  CB   . LYS   A 248 ? 0.7096 0.7969 1.0189 0.0901  -0.0247 0.0165  275 LYS   A CB   
1635 C  CG   . LYS   A 248 ? 0.7159 0.8029 1.0017 0.0836  -0.0309 0.0265  275 LYS   A CG   
1636 C  CD   . LYS   A 248 ? 0.7435 0.8652 1.0211 0.0937  -0.0370 0.0447  275 LYS   A CD   
1637 C  CE   . LYS   A 248 ? 0.8882 1.0119 1.1889 0.1164  -0.0293 0.0711  275 LYS   A CE   
1638 N  NZ   . LYS   A 248 ? 0.7593 0.8552 1.0641 0.1184  -0.0213 0.0865  275 LYS   A NZ   
1639 N  N    . ILE   A 249 ? 0.7051 0.7230 1.0675 0.0903  -0.0056 0.0023  276 ILE   A N    
1640 C  CA   . ILE   A 249 ? 0.7853 0.7763 1.1686 0.0883  0.0020  0.0053  276 ILE   A CA   
1641 C  C    . ILE   A 249 ? 0.7941 0.7904 1.1647 0.0931  0.0020  0.0356  276 ILE   A C    
1642 O  O    . ILE   A 249 ? 0.7944 0.8114 1.1593 0.1065  0.0015  0.0587  276 ILE   A O    
1643 C  CB   . ILE   A 249 ? 0.6653 0.6343 1.1004 0.0979  0.0181  0.0029  276 ILE   A CB   
1644 C  CG1  . ILE   A 249 ? 0.7347 0.7047 1.1801 0.0950  0.0173  -0.0302 276 ILE   A CG1  
1645 C  CG2  . ILE   A 249 ? 0.7001 0.6407 1.1653 0.0928  0.0288  0.0021  276 ILE   A CG2  
1646 C  CD1  . ILE   A 249 ? 0.8036 0.7539 1.3033 0.1049  0.0336  -0.0363 276 ILE   A CD1  
1647 N  N    . SER   A 250 ? 0.6669 0.6491 1.0321 0.0837  0.0019  0.0345  277 SER   A N    
1648 C  CA   . SER   A 250 ? 0.7387 0.7259 1.0923 0.0891  0.0037  0.0626  277 SER   A CA   
1649 C  C    . SER   A 250 ? 0.7195 0.6983 1.1062 0.1085  0.0210  0.0929  277 SER   A C    
1650 O  O    . SER   A 250 ? 0.9086 0.8620 1.3386 0.1117  0.0358  0.0889  277 SER   A O    
1651 C  CB   . SER   A 250 ? 0.6707 0.6415 1.0208 0.0761  0.0037  0.0544  277 SER   A CB   
1652 O  OG   . SER   A 250 ? 0.6613 0.6316 0.9946 0.0614  -0.0075 0.0231  277 SER   A OG   
1653 N  N    . TRP   A 251 ? 0.7476 0.7497 1.1145 0.1232  0.0198  0.1227  278 TRP   A N    
1654 C  CA   . TRP   A 251 ? 0.7474 0.7489 1.1360 0.1476  0.0363  0.1596  278 TRP   A CA   
1655 C  C    . TRP   A 251 ? 0.7458 0.7513 1.1588 0.1633  0.0417  0.1635  278 TRP   A C    
1656 O  O    . TRP   A 251 ? 1.0185 1.0191 1.4549 0.1865  0.0584  0.1953  278 TRP   A O    
1657 C  CB   . TRP   A 251 ? 0.6847 0.6477 1.1111 0.1479  0.0590  0.1729  278 TRP   A CB   
1658 C  CG   . TRP   A 251 ? 0.8286 0.7834 1.2406 0.1304  0.0555  0.1635  278 TRP   A CG   
1659 C  CD1  . TRP   A 251 ? 0.6282 0.5623 1.0532 0.1083  0.0527  0.1306  278 TRP   A CD1  
1660 C  CD2  . TRP   A 251 ? 0.7328 0.7036 1.1151 0.1356  0.0545  0.1865  278 TRP   A CD2  
1661 N  NE1  . TRP   A 251 ? 0.6811 0.6161 1.0878 0.0992  0.0500  0.1325  278 TRP   A NE1  
1662 C  CE2  . TRP   A 251 ? 0.6620 0.6178 1.0425 0.1149  0.0517  0.1664  278 TRP   A CE2  
1663 C  CE3  . TRP   A 251 ? 0.7445 0.7454 1.1007 0.1576  0.0552  0.2208  278 TRP   A CE3  
1664 C  CZ2  . TRP   A 251 ? 0.8107 0.7769 1.1660 0.1143  0.0508  0.1799  278 TRP   A CZ2  
1665 C  CZ3  . TRP   A 251 ? 0.8565 0.8697 1.1855 0.1574  0.0538  0.2329  278 TRP   A CZ3  
1666 C  CH2  . TRP   A 251 ? 0.8159 0.8099 1.1453 0.1351  0.0523  0.2127  278 TRP   A CH2  
1667 N  N    . ASP   A 252 ? 0.7941 0.8087 1.2027 0.1533  0.0300  0.1343  279 ASP   A N    
1668 C  CA   . ASP   A 252 ? 0.8653 0.8800 1.3024 0.1659  0.0366  0.1325  279 ASP   A CA   
1669 C  C    . ASP   A 252 ? 0.7764 0.8346 1.1867 0.1690  0.0196  0.1253  279 ASP   A C    
1670 O  O    . ASP   A 252 ? 0.8275 0.8943 1.2181 0.1504  0.0071  0.0965  279 ASP   A O    
1671 C  CB   . ASP   A 252 ? 1.0139 0.9965 1.4822 0.1514  0.0431  0.0995  279 ASP   A CB   
1672 C  CG   . ASP   A 252 ? 0.8563 0.8290 1.3659 0.1670  0.0566  0.1008  279 ASP   A CG   
1673 O  OD1  . ASP   A 252 ? 0.8949 0.8895 1.4044 0.1888  0.0583  0.1262  279 ASP   A OD1  
1674 O  OD2  . ASP   A 252 ? 0.9457 0.8914 1.4893 0.1586  0.0654  0.0747  279 ASP   A OD2  
1675 N  N    . ILE   A 253 ? 0.6911 0.7784 1.1027 0.1938  0.0206  0.1518  280 ILE   A N    
1676 C  CA   . ILE   A 253 ? 0.7922 0.9234 1.1927 0.1998  0.0074  0.1437  280 ILE   A CA   
1677 C  C    . ILE   A 253 ? 0.8287 0.9571 1.2652 0.2179  0.0181  0.1480  280 ILE   A C    
1678 O  O    . ILE   A 253 ? 0.8735 1.0397 1.3077 0.2250  0.0091  0.1416  280 ILE   A O    
1679 C  CB   . ILE   A 253 ? 0.6806 0.8623 1.0530 0.2152  -0.0047 0.1636  280 ILE   A CB   
1680 C  CG1  . ILE   A 253 ? 0.7536 0.9362 1.1379 0.2477  0.0092  0.2064  280 ILE   A CG1  
1681 C  CG2  . ILE   A 253 ? 0.7457 0.9334 1.0827 0.1950  -0.0166 0.1523  280 ILE   A CG2  
1682 C  CD1  . ILE   A 253 ? 0.6288 0.8727 0.9867 0.2708  -0.0034 0.2255  280 ILE   A CD1  
1683 N  N    . GLU   A 254 ? 0.8001 0.8853 1.2742 0.2252  0.0383  0.1572  281 GLU   A N    
1684 C  CA   . GLU   A 254 ? 0.9402 1.0167 1.4532 0.2413  0.0506  0.1576  281 GLU   A CA   
1685 C  C    . GLU   A 254 ? 0.9607 1.0234 1.4842 0.2205  0.0481  0.1157  281 GLU   A C    
1686 O  O    . GLU   A 254 ? 1.0016 1.0826 1.5367 0.2280  0.0469  0.1053  281 GLU   A O    
1687 C  CB   . GLU   A 254 ? 0.9781 1.0123 1.5334 0.2588  0.0769  0.1847  281 GLU   A CB   
1688 C  CG   . GLU   A 254 ? 1.1210 1.1675 1.6650 0.2837  0.0838  0.2316  281 GLU   A CG   
1689 C  CD   . GLU   A 254 ? 1.3589 1.3871 1.9448 0.3171  0.1092  0.2677  281 GLU   A CD   
1690 O  OE1  . GLU   A 254 ? 1.5096 1.4846 2.1409 0.3141  0.1336  0.2691  281 GLU   A OE1  
1691 O  OE2  . GLU   A 254 ? 1.4677 1.5359 2.0441 0.3472  0.1054  0.2939  281 GLU   A OE2  
1692 N  N    . THR   A 255 ? 0.8801 0.9144 1.3994 0.1965  0.0476  0.0913  282 THR   A N    
1693 C  CA   . THR   A 255 ? 0.8482 0.8764 1.3689 0.1789  0.0436  0.0513  282 THR   A CA   
1694 C  C    . THR   A 255 ? 0.8533 0.9209 1.3340 0.1690  0.0258  0.0386  282 THR   A C    
1695 O  O    . THR   A 255 ? 0.9911 1.0720 1.4368 0.1577  0.0141  0.0420  282 THR   A O    
1696 C  CB   . THR   A 255 ? 0.9102 0.9068 1.4325 0.1587  0.0453  0.0288  282 THR   A CB   
1697 O  OG1  . THR   A 255 ? 0.9753 0.9364 1.5391 0.1659  0.0637  0.0427  282 THR   A OG1  
1698 C  CG2  . THR   A 255 ? 0.8824 0.8751 1.4105 0.1472  0.0436  -0.0121 282 THR   A CG2  
1699 N  N    . PRO   A 256 ? 1.0285 1.1152 1.5165 0.1725  0.0252  0.0237  283 PRO   A N    
1700 C  CA   . PRO   A 256 ? 0.8795 1.0032 1.3364 0.1623  0.0123  0.0126  283 PRO   A CA   
1701 C  C    . PRO   A 256 ? 0.8642 0.9778 1.2893 0.1382  0.0058  -0.0093 283 PRO   A C    
1702 O  O    . PRO   A 256 ? 0.9425 1.0297 1.3725 0.1307  0.0106  -0.0291 283 PRO   A O    
1703 C  CB   . PRO   A 256 ? 0.9197 1.0579 1.3989 0.1709  0.0181  -0.0013 283 PRO   A CB   
1704 C  CG   . PRO   A 256 ? 0.9387 1.0414 1.4563 0.1807  0.0329  -0.0064 283 PRO   A CG   
1705 C  CD   . PRO   A 256 ? 0.9085 0.9843 1.4378 0.1872  0.0386  0.0177  283 PRO   A CD   
1706 N  N    . GLY   A 257 ? 0.6828 0.8200 1.0766 0.1276  -0.0050 -0.0067 284 GLY   A N    
1707 C  CA   . GLY   A 257 ? 0.7158 0.8438 1.0783 0.1074  -0.0097 -0.0226 284 GLY   A CA   
1708 C  C    . GLY   A 257 ? 0.6787 0.8192 1.0316 0.0992  -0.0071 -0.0433 284 GLY   A C    
1709 O  O    . GLY   A 257 ? 0.8619 1.0242 1.2314 0.1067  -0.0032 -0.0461 284 GLY   A O    
1710 N  N    . LEU   A 258 ? 0.5881 0.7158 0.9137 0.0853  -0.0079 -0.0562 285 LEU   A N    
1711 C  CA   . LEU   A 258 ? 0.5963 0.7327 0.9074 0.0789  -0.0023 -0.0724 285 LEU   A CA   
1712 C  C    . LEU   A 258 ? 0.7146 0.8662 1.0032 0.0655  -0.0040 -0.0683 285 LEU   A C    
1713 O  O    . LEU   A 258 ? 0.7534 0.8960 1.0238 0.0571  -0.0102 -0.0615 285 LEU   A O    
1714 C  CB   . LEU   A 258 ? 0.6733 0.7880 0.9687 0.0769  0.0002  -0.0898 285 LEU   A CB   
1715 C  CG   . LEU   A 258 ? 0.8078 0.9092 1.1294 0.0877  0.0041  -0.1048 285 LEU   A CG   
1716 C  CD1  . LEU   A 258 ? 0.7137 0.8076 1.0148 0.0860  0.0047  -0.1276 285 LEU   A CD1  
1717 C  CD2  . LEU   A 258 ? 0.5844 0.7017 0.9335 0.0988  0.0118  -0.1086 285 LEU   A CD2  
1718 N  N    . ALA   A 259 ? 0.7528 0.9272 1.0467 0.0631  0.0034  -0.0738 286 ALA   A N    
1719 C  CA   . ALA   A 259 ? 0.7195 0.9063 0.9999 0.0486  0.0074  -0.0740 286 ALA   A CA   
1720 C  C    . ALA   A 259 ? 0.7774 0.9563 1.0400 0.0458  0.0215  -0.0834 286 ALA   A C    
1721 O  O    . ALA   A 259 ? 0.8116 1.0052 1.0875 0.0517  0.0310  -0.0905 286 ALA   A O    
1722 C  CB   . ALA   A 259 ? 0.8569 1.0815 1.1639 0.0477  0.0067  -0.0730 286 ALA   A CB   
1723 N  N    . ILE   A 260 ? 0.7569 0.9147 0.9886 0.0392  0.0235  -0.0822 287 ILE   A N    
1724 C  CA   . ILE   A 260 ? 0.7710 0.9214 0.9785 0.0414  0.0371  -0.0874 287 ILE   A CA   
1725 C  C    . ILE   A 260 ? 0.8926 1.0496 1.0963 0.0288  0.0520  -0.0811 287 ILE   A C    
1726 O  O    . ILE   A 260 ? 0.8182 0.9634 1.0113 0.0180  0.0504  -0.0742 287 ILE   A O    
1727 C  CB   . ILE   A 260 ? 0.8606 0.9872 1.0369 0.0457  0.0316  -0.0892 287 ILE   A CB   
1728 C  CG1  . ILE   A 260 ? 0.8588 0.9774 1.0490 0.0542  0.0180  -0.0972 287 ILE   A CG1  
1729 C  CG2  . ILE   A 260 ? 0.9236 1.0505 1.0724 0.0544  0.0448  -0.0946 287 ILE   A CG2  
1730 C  CD1  . ILE   A 260 ? 0.7841 0.9150 1.0035 0.0646  0.0202  -0.1073 287 ILE   A CD1  
1731 N  N    . PRO   A 261 ? 0.8499 1.0245 1.0655 0.0292  0.0683  -0.0840 288 PRO   A N    
1732 C  CA   . PRO   A 261 ? 0.8882 1.0664 1.1071 0.0157  0.0870  -0.0783 288 PRO   A CA   
1733 C  C    . PRO   A 261 ? 0.7960 0.9483 0.9762 0.0171  0.1001  -0.0686 288 PRO   A C    
1734 O  O    . PRO   A 261 ? 0.8497 0.9944 1.0007 0.0323  0.1019  -0.0693 288 PRO   A O    
1735 C  CB   . PRO   A 261 ? 0.7483 0.9518 0.9898 0.0191  0.1028  -0.0839 288 PRO   A CB   
1736 C  CG   . PRO   A 261 ? 0.7449 0.9622 1.0032 0.0322  0.0875  -0.0929 288 PRO   A CG   
1737 C  CD   . PRO   A 261 ? 0.7447 0.9373 0.9774 0.0412  0.0720  -0.0933 288 PRO   A CD   
1738 N  N    . LEU   A 262 ? 0.7265 0.8676 0.9082 0.0026  0.1094  -0.0607 289 LEU   A N    
1739 C  CA   . LEU   A 262 ? 0.9394 1.0537 1.0868 0.0049  0.1236  -0.0475 289 LEU   A CA   
1740 C  C    . LEU   A 262 ? 1.0195 1.1329 1.1818 -0.0056 0.1548  -0.0390 289 LEU   A C    
1741 O  O    . LEU   A 262 ? 0.8787 1.0010 1.0786 -0.0245 0.1592  -0.0446 289 LEU   A O    
1742 C  CB   . LEU   A 262 ? 0.7864 0.8804 0.9231 -0.0019 0.1088  -0.0445 289 LEU   A CB   
1743 C  CG   . LEU   A 262 ? 0.8481 0.9387 0.9699 0.0083  0.0822  -0.0505 289 LEU   A CG   
1744 C  CD1  . LEU   A 262 ? 0.7931 0.8703 0.9141 -0.0012 0.0682  -0.0486 289 LEU   A CD1  
1745 C  CD2  . LEU   A 262 ? 0.7960 0.8776 0.8800 0.0273  0.0834  -0.0489 289 LEU   A CD2  
1746 N  N    . HIS   A 263 ? 0.9619 1.0671 1.0966 0.0074  0.1775  -0.0264 290 HIS   A N    
1747 C  CA   . HIS   A 263 ? 0.9983 1.0982 1.1457 0.0001  0.2132  -0.0135 290 HIS   A CA   
1748 C  C    . HIS   A 263 ? 1.0510 1.1162 1.1712 0.0018  0.2292  0.0066  290 HIS   A C    
1749 O  O    . HIS   A 263 ? 1.2021 1.2509 1.2987 0.0058  0.2099  0.0075  290 HIS   A O    
1750 C  CB   . HIS   A 263 ? 1.0983 1.2150 1.2340 0.0163  0.2323  -0.0093 290 HIS   A CB   
1751 C  CG   . HIS   A 263 ? 1.2066 1.3562 1.3716 0.0160  0.2190  -0.0287 290 HIS   A CG   
1752 N  ND1  . HIS   A 263 ? 1.2039 1.3676 1.3475 0.0360  0.2057  -0.0380 290 HIS   A ND1  
1753 C  CD2  . HIS   A 263 ? 1.1000 1.2730 1.3162 -0.0006 0.2173  -0.0417 290 HIS   A CD2  
1754 C  CE1  . HIS   A 263 ? 1.0821 1.2720 1.2622 0.0321  0.1979  -0.0532 290 HIS   A CE1  
1755 N  NE2  . HIS   A 263 ? 1.0571 1.2551 1.2800 0.0110  0.2039  -0.0549 290 HIS   A NE2  
1756 N  N    . GLN   A 264 ? 1.1775 1.2308 1.3035 -0.0002 0.2669  0.0241  291 GLN   A N    
1757 C  CA   . GLN   A 264 ? 1.1805 1.1980 1.2854 0.0030  0.2885  0.0472  291 GLN   A CA   
1758 C  C    . GLN   A 264 ? 1.2097 1.2209 1.2502 0.0353  0.2863  0.0638  291 GLN   A C    
1759 O  O    . GLN   A 264 ? 1.2572 1.2774 1.2735 0.0547  0.3078  0.0778  291 GLN   A O    
1760 C  CB   . GLN   A 264 ? 1.2719 1.2775 1.4088 -0.0085 0.3340  0.0624  291 GLN   A CB   
1761 C  CG   . GLN   A 264 ? 1.2916 1.2555 1.4181 -0.0075 0.3613  0.0874  291 GLN   A CG   
1762 C  CD   . GLN   A 264 ? 1.3974 1.3464 1.5662 -0.0215 0.4105  0.1018  291 GLN   A CD   
1763 O  OE1  . GLN   A 264 ? 1.4494 1.4032 1.6807 -0.0514 0.4168  0.0824  291 GLN   A OE1  
1764 N  NE2  . GLN   A 264 ? 1.3913 1.3246 1.5278 0.0010  0.4469  0.1353  291 GLN   A NE2  
1765 N  N    . GLY   A 265 ? 1.1589 1.1591 1.1719 0.0425  0.2599  0.0610  292 GLY   A N    
1766 C  CA   . GLY   A 265 ? 1.1020 1.1009 1.0571 0.0731  0.2546  0.0729  292 GLY   A CA   
1767 C  C    . GLY   A 265 ? 1.0975 1.1215 1.0336 0.0854  0.2179  0.0500  292 GLY   A C    
1768 O  O    . GLY   A 265 ? 1.1432 1.1738 1.0343 0.1112  0.2105  0.0536  292 GLY   A O    
1769 N  N    . ASP   A 266 ? 1.0793 1.1192 1.0502 0.0693  0.1957  0.0261  293 ASP   A N    
1770 C  CA   . ASP   A 266 ? 1.0667 1.1257 1.0278 0.0794  0.1643  0.0043  293 ASP   A CA   
1771 C  C    . ASP   A 266 ? 0.9571 1.0023 0.9048 0.0797  0.1400  0.0003  293 ASP   A C    
1772 O  O    . ASP   A 266 ? 0.9175 0.9419 0.8786 0.0640  0.1394  0.0070  293 ASP   A O    
1773 C  CB   . ASP   A 266 ? 1.0079 1.0846 1.0126 0.0641  0.1510  -0.0155 293 ASP   A CB   
1774 C  CG   . ASP   A 266 ? 1.1353 1.2344 1.1493 0.0703  0.1686  -0.0183 293 ASP   A CG   
1775 O  OD1  . ASP   A 266 ? 1.0930 1.1943 1.0779 0.0864  0.1919  -0.0044 293 ASP   A OD1  
1776 O  OD2  . ASP   A 266 ? 1.1111 1.2270 1.1607 0.0610  0.1598  -0.0332 293 ASP   A OD2  
1777 N  N    . CYS   A 267 ? 0.9678 1.0270 0.8916 0.0977  0.1204  -0.0134 294 CYS   A N    
1778 C  CA   . CYS   A 267 ? 0.9429 0.9944 0.8578 0.0989  0.0964  -0.0210 294 CYS   A CA   
1779 C  C    . CYS   A 267 ? 0.9396 1.0077 0.8747 0.0979  0.0711  -0.0478 294 CYS   A C    
1780 O  O    . CYS   A 267 ? 0.9337 1.0237 0.8646 0.1112  0.0698  -0.0627 294 CYS   A O    
1781 C  CB   . CYS   A 267 ? 0.9729 1.0265 0.8402 0.1243  0.0987  -0.0122 294 CYS   A CB   
1782 S  SG   . CYS   A 267 ? 1.1112 1.1408 0.9521 0.1318  0.1334  0.0250  294 CYS   A SG   
1783 N  N    . TYR   A 268 ? 0.8536 0.9109 0.8120 0.0830  0.0532  -0.0538 295 TYR   A N    
1784 C  CA   . TYR   A 268 ? 0.8447 0.9117 0.8250 0.0826  0.0321  -0.0757 295 TYR   A CA   
1785 C  C    . TYR   A 268 ? 0.8632 0.9223 0.8347 0.0847  0.0152  -0.0808 295 TYR   A C    
1786 O  O    . TYR   A 268 ? 0.8267 0.8699 0.7840 0.0806  0.0172  -0.0661 295 TYR   A O    
1787 C  CB   . TYR   A 268 ? 0.7631 0.8286 0.7852 0.0654  0.0279  -0.0773 295 TYR   A CB   
1788 C  CG   . TYR   A 268 ? 0.8091 0.8593 0.8443 0.0486  0.0226  -0.0662 295 TYR   A CG   
1789 C  CD1  . TYR   A 268 ? 0.8079 0.8522 0.8475 0.0365  0.0361  -0.0527 295 TYR   A CD1  
1790 C  CD2  . TYR   A 268 ? 0.8732 0.9168 0.9198 0.0449  0.0054  -0.0712 295 TYR   A CD2  
1791 C  CE1  . TYR   A 268 ? 0.8785 0.9140 0.9310 0.0221  0.0303  -0.0475 295 TYR   A CE1  
1792 C  CE2  . TYR   A 268 ? 0.7964 0.8302 0.8521 0.0318  0.0008  -0.0618 295 TYR   A CE2  
1793 C  CZ   . TYR   A 268 ? 0.7618 0.7932 0.8194 0.0209  0.0121  -0.0514 295 TYR   A CZ   
1794 O  OH   . TYR   A 268 ? 0.9151 0.9416 0.9824 0.0088  0.0066  -0.0467 295 TYR   A OH   
1795 N  N    . PHE   A 269 ? 0.8065 0.8775 0.7907 0.0908  -0.0001 -0.1035 296 PHE   A N    
1796 C  CA   . PHE   A 269 ? 0.7941 0.8644 0.7741 0.0946  -0.0155 -0.1139 296 PHE   A CA   
1797 C  C    . PHE   A 269 ? 0.8486 0.9143 0.8710 0.0833  -0.0281 -0.1277 296 PHE   A C    
1798 O  O    . PHE   A 269 ? 0.8292 0.9033 0.8779 0.0841  -0.0283 -0.1425 296 PHE   A O    
1799 C  CB   . PHE   A 269 ? 0.8293 0.9249 0.7834 0.1171  -0.0202 -0.1328 296 PHE   A CB   
1800 C  CG   . PHE   A 269 ? 0.8889 0.9913 0.7968 0.1341  -0.0055 -0.1155 296 PHE   A CG   
1801 C  CD1  . PHE   A 269 ? 0.9467 1.0543 0.8457 0.1383  0.0127  -0.1061 296 PHE   A CD1  
1802 C  CD2  . PHE   A 269 ? 1.0577 1.1619 0.9322 0.1477  -0.0079 -0.1071 296 PHE   A CD2  
1803 C  CE1  . PHE   A 269 ? 0.9196 1.0314 0.7773 0.1554  0.0305  -0.0863 296 PHE   A CE1  
1804 C  CE2  . PHE   A 269 ? 1.0362 1.1448 0.8679 0.1668  0.0089  -0.0866 296 PHE   A CE2  
1805 C  CZ   . PHE   A 269 ? 0.9113 1.0226 0.7346 0.1706  0.0292  -0.0751 296 PHE   A CZ   
1806 N  N    . MET   A 270 ? 0.7717 0.8236 0.8020 0.0743  -0.0364 -0.1217 297 MET   A N    
1807 C  CA   . MET   A 270 ? 0.7583 0.8046 0.8272 0.0661  -0.0457 -0.1318 297 MET   A CA   
1808 C  C    . MET   A 270 ? 0.7412 0.7970 0.8110 0.0733  -0.0568 -0.1527 297 MET   A C    
1809 O  O    . MET   A 270 ? 0.8200 0.8717 0.8714 0.0736  -0.0614 -0.1457 297 MET   A O    
1810 C  CB   . MET   A 270 ? 0.7609 0.7896 0.8404 0.0518  -0.0458 -0.1106 297 MET   A CB   
1811 C  CG   . MET   A 270 ? 0.8617 0.8877 0.9378 0.0448  -0.0363 -0.0926 297 MET   A CG   
1812 S  SD   . MET   A 270 ? 1.0551 1.0725 1.1530 0.0316  -0.0396 -0.0759 297 MET   A SD   
1813 C  CE   . MET   A 270 ? 0.8196 0.8255 0.9010 0.0290  -0.0468 -0.0726 297 MET   A CE   
1814 N  N    . LEU   A 271 ? 0.6708 0.7411 0.7654 0.0790  -0.0609 -0.1809 298 LEU   A N    
1815 C  CA   . LEU   A 271 ? 0.7337 0.8219 0.8345 0.0867  -0.0720 -0.2091 298 LEU   A CA   
1816 C  C    . LEU   A 271 ? 0.8302 0.9065 0.9807 0.0742  -0.0758 -0.2190 298 LEU   A C    
1817 O  O    . LEU   A 271 ? 0.7638 0.8231 0.9497 0.0648  -0.0690 -0.2122 298 LEU   A O    
1818 C  CB   . LEU   A 271 ? 0.7927 0.9101 0.8939 0.1015  -0.0739 -0.2412 298 LEU   A CB   
1819 C  CG   . LEU   A 271 ? 0.8440 0.9764 0.8993 0.1166  -0.0664 -0.2325 298 LEU   A CG   
1820 C  CD1  . LEU   A 271 ? 0.6962 0.8648 0.7512 0.1340  -0.0709 -0.2698 298 LEU   A CD1  
1821 C  CD2  . LEU   A 271 ? 0.8089 0.9408 0.8145 0.1251  -0.0653 -0.2088 298 LEU   A CD2  
1822 N  N    . ASP   A 272 ? 0.8963 0.9829 1.0502 0.0759  -0.0853 -0.2337 299 ASP   A N    
1823 C  CA   . ASP   A 272 ? 0.7770 0.8586 0.9834 0.0658  -0.0877 -0.2510 299 ASP   A CA   
1824 C  C    . ASP   A 272 ? 0.8626 0.9121 1.0872 0.0512  -0.0788 -0.2188 299 ASP   A C    
1825 O  O    . ASP   A 272 ? 0.7558 0.7947 0.9482 0.0486  -0.0787 -0.1909 299 ASP   A O    
1826 C  CB   . ASP   A 272 ? 0.8132 0.9092 1.0624 0.0682  -0.0870 -0.2887 299 ASP   A CB   
1827 C  CG   . ASP   A 272 ? 0.8721 0.9721 1.1780 0.0601  -0.0895 -0.3179 299 ASP   A CG   
1828 O  OD1  . ASP   A 272 ? 0.9920 1.1136 1.2905 0.0640  -0.1006 -0.3343 299 ASP   A OD1  
1829 O  OD2  . ASP   A 272 ? 0.8171 0.8988 1.1780 0.0505  -0.0789 -0.3242 299 ASP   A OD2  
1830 N  N    . ASP   A 273 ? 0.8584 0.8930 1.1335 0.0433  -0.0703 -0.2213 300 ASP   A N    
1831 C  CA   . ASP   A 273 ? 0.8531 0.8623 1.1459 0.0338  -0.0612 -0.1904 300 ASP   A CA   
1832 C  C    . ASP   A 273 ? 0.8312 0.8301 1.1131 0.0349  -0.0539 -0.1644 300 ASP   A C    
1833 O  O    . ASP   A 273 ? 0.8029 0.7858 1.1071 0.0312  -0.0453 -0.1422 300 ASP   A O    
1834 C  CB   . ASP   A 273 ? 0.8385 0.8364 1.1954 0.0271  -0.0525 -0.2032 300 ASP   A CB   
1835 C  CG   . ASP   A 273 ? 0.8837 0.8820 1.2813 0.0299  -0.0457 -0.2276 300 ASP   A CG   
1836 O  OD1  . ASP   A 273 ? 0.9136 0.9278 1.2870 0.0381  -0.0509 -0.2412 300 ASP   A OD1  
1837 O  OD2  . ASP   A 273 ? 0.8640 0.8459 1.3194 0.0245  -0.0332 -0.2328 300 ASP   A OD2  
1838 N  N    . LEU   A 274 ? 0.6581 0.6687 0.9068 0.0414  -0.0562 -0.1661 301 LEU   A N    
1839 C  CA   . LEU   A 274 ? 0.7027 0.7088 0.9449 0.0421  -0.0496 -0.1449 301 LEU   A CA   
1840 C  C    . LEU   A 274 ? 0.7206 0.7185 0.9435 0.0363  -0.0492 -0.1133 301 LEU   A C    
1841 O  O    . LEU   A 274 ? 0.7304 0.7242 0.9664 0.0360  -0.0438 -0.0944 301 LEU   A O    
1842 C  CB   . LEU   A 274 ? 0.7490 0.7707 0.9595 0.0494  -0.0501 -0.1530 301 LEU   A CB   
1843 C  CG   . LEU   A 274 ? 0.7485 0.7709 0.9587 0.0502  -0.0427 -0.1372 301 LEU   A CG   
1844 C  CD1  . LEU   A 274 ? 0.7949 0.8126 1.0511 0.0533  -0.0363 -0.1447 301 LEU   A CD1  
1845 C  CD2  . LEU   A 274 ? 0.8990 0.9363 1.0750 0.0564  -0.0405 -0.1419 301 LEU   A CD2  
1846 N  N    . ASN   A 275 ? 0.8336 0.8323 1.0260 0.0333  -0.0551 -0.1087 302 ASN   A N    
1847 C  CA   . ASN   A 275 ? 0.7282 0.7217 0.9035 0.0276  -0.0551 -0.0840 302 ASN   A CA   
1848 C  C    . ASN   A 275 ? 0.6932 0.6776 0.8966 0.0247  -0.0520 -0.0707 302 ASN   A C    
1849 O  O    . ASN   A 275 ? 0.7183 0.7037 0.9140 0.0230  -0.0508 -0.0497 302 ASN   A O    
1850 C  CB   . ASN   A 275 ? 0.7510 0.7449 0.8911 0.0263  -0.0604 -0.0841 302 ASN   A CB   
1851 C  CG   . ASN   A 275 ? 0.7307 0.7206 0.8538 0.0199  -0.0600 -0.0635 302 ASN   A CG   
1852 O  OD1  . ASN   A 275 ? 0.8547 0.8489 0.9705 0.0174  -0.0567 -0.0536 302 ASN   A OD1  
1853 N  ND2  . ASN   A 275 ? 0.8960 0.8808 1.0155 0.0171  -0.0633 -0.0600 302 ASN   A ND2  
1854 N  N    . ALA   A 276 ? 0.6525 0.6303 0.8902 0.0248  -0.0494 -0.0832 303 ALA   A N    
1855 C  CA   . ALA   A 276 ? 0.6171 0.5839 0.8845 0.0229  -0.0419 -0.0680 303 ALA   A CA   
1856 C  C    . ALA   A 276 ? 0.6396 0.5991 0.9420 0.0284  -0.0306 -0.0564 303 ALA   A C    
1857 O  O    . ALA   A 276 ? 0.9420 0.8983 1.2501 0.0319  -0.0238 -0.0297 303 ALA   A O    
1858 C  CB   . ALA   A 276 ? 0.5815 0.5440 0.8754 0.0187  -0.0416 -0.0871 303 ALA   A CB   
1859 N  N    . THR   A 277 ? 0.6850 0.6438 1.0104 0.0315  -0.0277 -0.0758 304 THR   A N    
1860 C  CA   . THR   A 277 ? 0.7145 0.6641 1.0774 0.0385  -0.0152 -0.0658 304 THR   A CA   
1861 C  C    . THR   A 277 ? 0.7846 0.7460 1.1264 0.0457  -0.0166 -0.0480 304 THR   A C    
1862 O  O    . THR   A 277 ? 0.7032 0.6600 1.0709 0.0548  -0.0066 -0.0319 304 THR   A O    
1863 C  CB   . THR   A 277 ? 0.8249 0.7695 1.2267 0.0389  -0.0106 -0.0979 304 THR   A CB   
1864 O  OG1  . THR   A 277 ? 0.7795 0.7418 1.1512 0.0399  -0.0215 -0.1209 304 THR   A OG1  
1865 C  CG2  . THR   A 277 ? 0.5663 0.5025 1.0026 0.0314  -0.0075 -0.1186 304 THR   A CG2  
1866 N  N    . HIS   A 278 ? 0.7763 0.7534 1.0756 0.0427  -0.0271 -0.0506 305 HIS   A N    
1867 C  CA   . HIS   A 278 ? 0.7364 0.7290 1.0209 0.0474  -0.0283 -0.0396 305 HIS   A CA   
1868 C  C    . HIS   A 278 ? 0.7930 0.7986 1.0401 0.0423  -0.0359 -0.0267 305 HIS   A C    
1869 O  O    . HIS   A 278 ? 0.7769 0.7789 1.0012 0.0348  -0.0412 -0.0322 305 HIS   A O    
1870 C  CB   . HIS   A 278 ? 0.7953 0.7959 1.0741 0.0484  -0.0292 -0.0613 305 HIS   A CB   
1871 C  CG   . HIS   A 278 ? 0.8018 0.7938 1.1194 0.0542  -0.0218 -0.0785 305 HIS   A CG   
1872 N  ND1  . HIS   A 278 ? 0.8976 0.8761 1.2418 0.0518  -0.0194 -0.0968 305 HIS   A ND1  
1873 C  CD2  . HIS   A 278 ? 0.9638 0.9600 1.3023 0.0622  -0.0156 -0.0828 305 HIS   A CD2  
1874 C  CE1  . HIS   A 278 ? 0.9238 0.8975 1.3049 0.0572  -0.0116 -0.1134 305 HIS   A CE1  
1875 N  NE2  . HIS   A 278 ? 0.8289 0.8121 1.2058 0.0643  -0.0091 -0.1042 305 HIS   A NE2  
1876 N  N    . GLN   A 279 ? 0.7824 0.8053 1.0263 0.0472  -0.0362 -0.0114 306 GLN   A N    
1877 C  CA   . GLN   A 279 ? 0.6822 0.7230 0.8973 0.0415  -0.0430 -0.0061 306 GLN   A CA   
1878 C  C    . GLN   A 279 ? 0.6669 0.7201 0.8723 0.0376  -0.0431 -0.0183 306 GLN   A C    
1879 O  O    . GLN   A 279 ? 0.7767 0.8324 0.9986 0.0433  -0.0386 -0.0246 306 GLN   A O    
1880 C  CB   . GLN   A 279 ? 0.6718 0.7328 0.8913 0.0503  -0.0442 0.0150  306 GLN   A CB   
1881 C  CG   . GLN   A 279 ? 0.7171 0.7669 0.9489 0.0580  -0.0395 0.0331  306 GLN   A CG   
1882 C  CD   . GLN   A 279 ? 0.7375 0.8128 0.9706 0.0727  -0.0396 0.0567  306 GLN   A CD   
1883 O  OE1  . GLN   A 279 ? 0.8577 0.9402 1.1120 0.0871  -0.0341 0.0685  306 GLN   A OE1  
1884 N  NE2  . GLN   A 279 ? 0.8709 0.9630 1.0810 0.0712  -0.0459 0.0631  306 GLN   A NE2  
1885 N  N    . HIS   A 280 ? 0.6843 0.7442 0.8654 0.0280  -0.0460 -0.0219 307 HIS   A N    
1886 C  CA   . HIS   A 280 ? 0.7178 0.7889 0.8928 0.0231  -0.0422 -0.0309 307 HIS   A CA   
1887 C  C    . HIS   A 280 ? 0.7251 0.8162 0.8935 0.0152  -0.0447 -0.0288 307 HIS   A C    
1888 O  O    . HIS   A 280 ? 0.7169 0.8081 0.8751 0.0117  -0.0499 -0.0241 307 HIS   A O    
1889 C  CB   . HIS   A 280 ? 0.7114 0.7658 0.8666 0.0191  -0.0377 -0.0425 307 HIS   A CB   
1890 C  CG   . HIS   A 280 ? 0.7660 0.8074 0.8971 0.0121  -0.0399 -0.0415 307 HIS   A CG   
1891 N  ND1  . HIS   A 280 ? 0.8316 0.8618 0.9605 0.0130  -0.0459 -0.0378 307 HIS   A ND1  
1892 C  CD2  . HIS   A 280 ? 0.7633 0.8000 0.8743 0.0050  -0.0347 -0.0429 307 HIS   A CD2  
1893 C  CE1  . HIS   A 280 ? 0.9853 1.0064 1.0920 0.0073  -0.0462 -0.0380 307 HIS   A CE1  
1894 N  NE2  . HIS   A 280 ? 0.9133 0.9365 1.0090 0.0028  -0.0390 -0.0404 307 HIS   A NE2  
1895 N  N    . CYS   A 281 ? 0.6252 0.7355 0.8028 0.0122  -0.0404 -0.0348 308 CYS   A N    
1896 C  CA   . CYS   A 281 ? 0.6424 0.7765 0.8230 0.0030  -0.0414 -0.0395 308 CYS   A CA   
1897 C  C    . CYS   A 281 ? 0.7388 0.8717 0.9208 -0.0069 -0.0291 -0.0496 308 CYS   A C    
1898 O  O    . CYS   A 281 ? 0.8293 0.9463 1.0054 -0.0037 -0.0209 -0.0507 308 CYS   A O    
1899 C  CB   . CYS   A 281 ? 0.5719 0.7437 0.7734 0.0119  -0.0489 -0.0358 308 CYS   A CB   
1900 S  SG   . CYS   A 281 ? 0.6676 0.8586 0.8951 0.0210  -0.0436 -0.0383 308 CYS   A SG   
1901 N  N    . VAL   A 282 ? 0.6648 0.8168 0.8568 -0.0186 -0.0264 -0.0582 309 VAL   A N    
1902 C  CA   . VAL   A 282 ? 0.7053 0.8570 0.9060 -0.0297 -0.0106 -0.0666 309 VAL   A CA   
1903 C  C    . VAL   A 282 ? 0.6588 0.8533 0.8927 -0.0333 -0.0117 -0.0776 309 VAL   A C    
1904 O  O    . VAL   A 282 ? 0.8280 1.0497 1.0742 -0.0380 -0.0208 -0.0862 309 VAL   A O    
1905 C  CB   . VAL   A 282 ? 0.8531 0.9830 1.0421 -0.0431 -0.0011 -0.0695 309 VAL   A CB   
1906 C  CG1  . VAL   A 282 ? 0.8166 0.9448 1.0203 -0.0543 0.0201  -0.0753 309 VAL   A CG1  
1907 C  CG2  . VAL   A 282 ? 0.7668 0.8597 0.9228 -0.0367 -0.0012 -0.0589 309 VAL   A CG2  
1908 N  N    . LEU   A 283 ? 0.6419 0.8467 0.8911 -0.0299 -0.0030 -0.0794 310 LEU   A N    
1909 C  CA   . LEU   A 283 ? 0.7165 0.9654 1.0008 -0.0324 -0.0032 -0.0912 310 LEU   A CA   
1910 C  C    . LEU   A 283 ? 0.7754 1.0270 1.0791 -0.0518 0.0154  -0.1043 310 LEU   A C    
1911 O  O    . LEU   A 283 ? 0.7809 1.0046 1.0753 -0.0557 0.0345  -0.0990 310 LEU   A O    
1912 C  CB   . LEU   A 283 ? 0.6347 0.8946 0.9297 -0.0179 -0.0023 -0.0868 310 LEU   A CB   
1913 C  CG   . LEU   A 283 ? 0.6977 0.9478 0.9802 0.0012  -0.0153 -0.0732 310 LEU   A CG   
1914 C  CD1  . LEU   A 283 ? 0.7542 1.0204 1.0564 0.0154  -0.0134 -0.0719 310 LEU   A CD1  
1915 C  CD2  . LEU   A 283 ? 0.6587 0.9297 0.9412 0.0069  -0.0321 -0.0689 310 LEU   A CD2  
1916 N  N    . ALA   A 284 ? 0.8037 1.0913 1.1365 -0.0629 0.0111  -0.1220 311 ALA   A N    
1917 C  CA   . ALA   A 284 ? 0.7014 0.9895 1.0607 -0.0845 0.0305  -0.1375 311 ALA   A CA   
1918 C  C    . ALA   A 284 ? 0.8460 1.1556 1.2388 -0.0888 0.0468  -0.1447 311 ALA   A C    
1919 O  O    . ALA   A 284 ? 0.7578 1.1057 1.1679 -0.0779 0.0361  -0.1486 311 ALA   A O    
1920 C  CB   . ALA   A 284 ? 0.7721 1.0954 1.1562 -0.0958 0.0195  -0.1605 311 ALA   A CB   
1921 N  N    . GLY   A 285 ? 0.9046 1.1891 1.3072 -0.1033 0.0745  -0.1446 312 GLY   A N    
1922 C  CA   . GLY   A 285 ? 0.6924 0.9964 1.1332 -0.1120 0.0959  -0.1531 312 GLY   A CA   
1923 C  C    . GLY   A 285 ? 0.7762 1.1096 1.2709 -0.1355 0.1055  -0.1806 312 GLY   A C    
1924 O  O    . GLY   A 285 ? 0.8094 1.1698 1.3171 -0.1406 0.0866  -0.1993 312 GLY   A O    
1925 N  N    . SER   A 286 ? 0.8635 1.1936 1.3923 -0.1499 0.1365  -0.1849 313 SER   A N    
1926 C  CA   . SER   A 286 ? 0.8615 1.2178 1.4523 -0.1755 0.1511  -0.2144 313 SER   A CA   
1927 C  C    . SER   A 286 ? 0.9583 1.2635 1.5543 -0.1932 0.1823  -0.2091 313 SER   A C    
1928 O  O    . SER   A 286 ? 1.0090 1.3260 1.6466 -0.2136 0.1865  -0.2356 313 SER   A O    
1929 C  CB   . SER   A 286 ? 0.8715 1.2670 1.5133 -0.1823 0.1675  -0.2273 313 SER   A CB   
1930 O  OG   . SER   A 286 ? 0.9495 1.3791 1.5779 -0.1608 0.1450  -0.2226 313 SER   A OG   
1931 N  N    . GLN   A 287 ? 0.8829 1.1344 1.4394 -0.1844 0.2045  -0.1769 314 GLN   A N    
1932 C  CA   . GLN   A 287 ? 0.9279 1.1269 1.4838 -0.1956 0.2364  -0.1648 314 GLN   A CA   
1933 C  C    . GLN   A 287 ? 1.0627 1.2246 1.5652 -0.1847 0.2193  -0.1504 314 GLN   A C    
1934 O  O    . GLN   A 287 ? 0.9669 1.1334 1.4237 -0.1653 0.1893  -0.1407 314 GLN   A O    
1935 C  CB   . GLN   A 287 ? 0.9808 1.1466 1.5220 -0.1882 0.2732  -0.1351 314 GLN   A CB   
1936 C  CG   . GLN   A 287 ? 1.0934 1.2906 1.6931 -0.2016 0.2986  -0.1477 314 GLN   A CG   
1937 N  N    . PRO   A 288 ? 1.0553 1.1796 1.5664 -0.1968 0.2392  -0.1493 315 PRO   A N    
1938 C  CA   . PRO   A 288 ? 0.8842 0.9722 1.3450 -0.1854 0.2252  -0.1344 315 PRO   A CA   
1939 C  C    . PRO   A 288 ? 1.0013 1.0567 1.3973 -0.1595 0.2262  -0.0979 315 PRO   A C    
1940 O  O    . PRO   A 288 ? 0.9684 1.0204 1.3573 -0.1511 0.2451  -0.0815 315 PRO   A O    
1941 C  CB   . PRO   A 288 ? 0.9696 1.0206 1.4613 -0.2035 0.2565  -0.1383 315 PRO   A CB   
1942 C  CG   . PRO   A 288 ? 0.8259 0.9094 1.3950 -0.2294 0.2746  -0.1697 315 PRO   A CG   
1943 C  CD   . PRO   A 288 ? 1.0509 1.1657 1.6248 -0.2225 0.2758  -0.1645 315 PRO   A CD   
1944 N  N    . ARG   A 289 ? 0.9591 0.9943 1.3086 -0.1462 0.2053  -0.0875 316 ARG   A N    
1945 C  CA   . ARG   A 289 ? 1.0260 1.0390 1.3160 -0.1210 0.2001  -0.0597 316 ARG   A CA   
1946 C  C    . ARG   A 289 ? 0.8873 0.8668 1.1400 -0.1125 0.1917  -0.0485 316 ARG   A C    
1947 O  O    . ARG   A 289 ? 0.8485 0.8370 1.1068 -0.1194 0.1699  -0.0643 316 ARG   A O    
1948 C  CB   . ARG   A 289 ? 0.8548 0.9019 1.1284 -0.1079 0.1694  -0.0646 316 ARG   A CB   
1949 C  CG   . ARG   A 289 ? 0.9327 0.9617 1.1499 -0.0837 0.1569  -0.0451 316 ARG   A CG   
1950 C  CD   . ARG   A 289 ? 0.7990 0.8532 1.0064 -0.0754 0.1216  -0.0545 316 ARG   A CD   
1951 N  NE   . ARG   A 289 ? 0.9837 1.0237 1.1466 -0.0545 0.1108  -0.0414 316 ARG   A NE   
1952 C  CZ   . ARG   A 289 ? 0.9583 0.9911 1.0987 -0.0473 0.0885  -0.0409 316 ARG   A CZ   
1953 N  NH1  . ARG   A 289 ? 0.9994 1.0369 1.1519 -0.0573 0.0746  -0.0497 316 ARG   A NH1  
1954 N  NH2  . ARG   A 289 ? 0.8834 0.9071 0.9904 -0.0295 0.0807  -0.0332 316 ARG   A NH2  
1955 N  N    . PHE   A 290 ? 0.9749 0.9199 1.1891 -0.0957 0.2091  -0.0213 317 PHE   A N    
1956 C  CA   . PHE   A 290 ? 1.0433 0.9605 1.2158 -0.0817 0.1996  -0.0080 317 PHE   A CA   
1957 C  C    . PHE   A 290 ? 0.9840 0.9127 1.1105 -0.0592 0.1738  -0.0007 317 PHE   A C    
1958 O  O    . PHE   A 290 ? 0.9951 0.9428 1.1155 -0.0506 0.1725  0.0007  317 PHE   A O    
1959 C  CB   . PHE   A 290 ? 1.0421 0.9170 1.2010 -0.0735 0.2353  0.0180  317 PHE   A CB   
1960 C  CG   . PHE   A 290 ? 1.1171 0.9721 1.3258 -0.0961 0.2644  0.0109  317 PHE   A CG   
1961 C  CD1  . PHE   A 290 ? 1.1812 1.0422 1.4351 -0.1114 0.2936  0.0067  317 PHE   A CD1  
1962 C  CD2  . PHE   A 290 ? 1.0354 0.8660 1.2499 -0.1025 0.2642  0.0063  317 PHE   A CD2  
1963 C  CE1  . PHE   A 290 ? 0.9306 0.7732 1.2388 -0.1342 0.3226  -0.0037 317 PHE   A CE1  
1964 C  CE2  . PHE   A 290 ? 1.0476 0.8590 1.3138 -0.1242 0.2925  -0.0043 317 PHE   A CE2  
1965 C  CZ   . PHE   A 290 ? 1.1099 0.9270 1.4250 -0.1407 0.3221  -0.0101 317 PHE   A CZ   
1966 N  N    . SER   A 291 ? 0.8304 0.7479 0.9282 -0.0501 0.1543  0.0016  318 SER   A N    
1967 C  CA   . SER   A 291 ? 0.9160 0.8422 0.9752 -0.0297 0.1319  0.0059  318 SER   A CA   
1968 C  C    . SER   A 291 ? 0.9320 0.8351 0.9588 -0.0173 0.1263  0.0163  318 SER   A C    
1969 O  O    . SER   A 291 ? 0.9243 0.8126 0.9623 -0.0277 0.1263  0.0128  318 SER   A O    
1970 C  CB   . SER   A 291 ? 0.8982 0.8543 0.9710 -0.0347 0.1018  -0.0125 318 SER   A CB   
1971 O  OG   . SER   A 291 ? 0.9852 0.9418 1.0691 -0.0455 0.0863  -0.0227 318 SER   A OG   
1972 N  N    . SER   A 292 ? 0.9454 0.8490 0.9336 0.0059  0.1212  0.0266  319 SER   A N    
1973 C  CA   . SER   A 292 ? 0.9625 0.8516 0.9182 0.0219  0.1138  0.0354  319 SER   A CA   
1974 C  C    . SER   A 292 ? 0.9697 0.8813 0.9095 0.0330  0.0843  0.0231  319 SER   A C    
1975 O  O    . SER   A 292 ? 1.0289 0.9560 0.9494 0.0495  0.0824  0.0231  319 SER   A O    
1976 C  CB   . SER   A 292 ? 1.0223 0.8938 0.9472 0.0432  0.1395  0.0601  319 SER   A CB   
1977 O  OG   . SER   A 292 ? 1.0733 0.9374 0.9657 0.0623  0.1300  0.0677  319 SER   A OG   
1978 N  N    . THR   A 293 ? 0.8908 0.8051 0.8412 0.0240  0.0629  0.0114  320 THR   A N    
1979 C  CA   . THR   A 293 ? 0.9795 0.9123 0.9260 0.0305  0.0376  -0.0015 320 THR   A CA   
1980 C  C    . THR   A 293 ? 0.9844 0.9110 0.9055 0.0452  0.0286  0.0014  320 THR   A C    
1981 O  O    . THR   A 293 ? 0.8832 0.7966 0.8073 0.0388  0.0254  0.0031  320 THR   A O    
1982 C  CB   . THR   A 293 ? 0.9156 0.8583 0.8923 0.0130  0.0223  -0.0137 320 THR   A CB   
1983 O  OG1  . THR   A 293 ? 1.0199 0.9518 0.9969 0.0072  0.0154  -0.0136 320 THR   A OG1  
1984 C  CG2  . THR   A 293 ? 0.9686 0.9173 0.9724 -0.0027 0.0335  -0.0157 320 THR   A CG2  
1985 N  N    . HIS   A 294 ? 0.9413 0.8814 0.8385 0.0658  0.0240  -0.0005 321 HIS   A N    
1986 C  CA   . HIS   A 294 ? 0.8650 0.8075 0.7382 0.0833  0.0146  -0.0001 321 HIS   A CA   
1987 C  C    . HIS   A 294 ? 0.8312 0.7911 0.7200 0.0805  -0.0100 -0.0209 321 HIS   A C    
1988 O  O    . HIS   A 294 ? 0.8649 0.8420 0.7681 0.0791  -0.0182 -0.0356 321 HIS   A O    
1989 C  CB   . HIS   A 294 ? 0.8759 0.8309 0.7138 0.1107  0.0231  0.0073  321 HIS   A CB   
1990 C  CG   . HIS   A 294 ? 1.0041 0.9404 0.8280 0.1156  0.0523  0.0316  321 HIS   A CG   
1991 N  ND1  . HIS   A 294 ? 0.9505 0.8761 0.7423 0.1377  0.0675  0.0533  321 HIS   A ND1  
1992 C  CD2  . HIS   A 294 ? 1.1238 1.0505 0.9648 0.1018  0.0712  0.0385  321 HIS   A CD2  
1993 C  CE1  . HIS   A 294 ? 1.0954 1.0018 0.8863 0.1367  0.0970  0.0742  321 HIS   A CE1  
1994 N  NE2  . HIS   A 294 ? 1.1025 1.0104 0.9246 0.1138  0.0994  0.0640  321 HIS   A NE2  
1995 N  N    . ARG   A 295 ? 0.8850 0.8392 0.7743 0.0795  -0.0195 -0.0220 322 ARG   A N    
1996 C  CA   . ARG   A 295 ? 0.8342 0.8009 0.7449 0.0738  -0.0387 -0.0393 322 ARG   A CA   
1997 C  C    . ARG   A 295 ? 0.9799 0.9560 0.8761 0.0892  -0.0487 -0.0445 322 ARG   A C    
1998 O  O    . ARG   A 295 ? 0.9102 0.8787 0.7797 0.1030  -0.0411 -0.0312 322 ARG   A O    
1999 C  CB   . ARG   A 295 ? 0.8009 0.7550 0.7366 0.0526  -0.0407 -0.0368 322 ARG   A CB   
2000 C  CG   . ARG   A 295 ? 0.9224 0.8701 0.8713 0.0384  -0.0303 -0.0306 322 ARG   A CG   
2001 C  CD   . ARG   A 295 ? 0.8579 0.7915 0.8144 0.0244  -0.0256 -0.0236 322 ARG   A CD   
2002 N  NE   . ARG   A 295 ? 0.8966 0.8319 0.8703 0.0108  -0.0177 -0.0227 322 ARG   A NE   
2003 C  CZ   . ARG   A 295 ? 0.9853 0.9340 0.9815 0.0011  -0.0257 -0.0281 322 ARG   A CZ   
2004 N  NH1  . ARG   A 295 ? 0.9822 0.9391 0.9876 0.0025  -0.0390 -0.0321 322 ARG   A NH1  
2005 N  NH2  . ARG   A 295 ? 1.0520 1.0078 1.0638 -0.0090 -0.0190 -0.0289 322 ARG   A NH2  
2006 N  N    . VAL   A 296 ? 0.9173 0.9105 0.8348 0.0875  -0.0645 -0.0641 323 VAL   A N    
2007 C  CA   . VAL   A 296 ? 0.8504 0.8563 0.7657 0.0976  -0.0760 -0.0734 323 VAL   A CA   
2008 C  C    . VAL   A 296 ? 0.8454 0.8371 0.7849 0.0795  -0.0788 -0.0707 323 VAL   A C    
2009 O  O    . VAL   A 296 ? 0.8103 0.8087 0.7817 0.0688  -0.0860 -0.0832 323 VAL   A O    
2010 C  CB   . VAL   A 296 ? 0.9330 0.9717 0.8611 0.1079  -0.0899 -0.1012 323 VAL   A CB   
2011 C  CG1  . VAL   A 296 ? 0.7977 0.8557 0.7220 0.1212  -0.1015 -0.1121 323 VAL   A CG1  
2012 C  CG2  . VAL   A 296 ? 0.8374 0.8932 0.7426 0.1246  -0.0863 -0.1055 323 VAL   A CG2  
2013 N  N    . ALA   A 297 ? 0.7988 0.7706 0.7243 0.0770  -0.0711 -0.0538 324 ALA   A N    
2014 C  CA   . ALA   A 297 ? 0.7853 0.7460 0.7291 0.0615  -0.0723 -0.0507 324 ALA   A CA   
2015 C  C    . ALA   A 297 ? 0.9024 0.8779 0.8601 0.0653  -0.0840 -0.0631 324 ALA   A C    
2016 O  O    . ALA   A 297 ? 0.7775 0.7664 0.7216 0.0821  -0.0894 -0.0691 324 ALA   A O    
2017 C  CB   . ALA   A 297 ? 0.7585 0.6964 0.6860 0.0589  -0.0607 -0.0344 324 ALA   A CB   
2018 N  N    . GLU   A 298 ? 0.8630 0.8388 0.8493 0.0510  -0.0868 -0.0664 325 GLU   A N    
2019 C  CA   . GLU   A 298 ? 0.8594 0.8468 0.8652 0.0513  -0.0940 -0.0764 325 GLU   A CA   
2020 C  C    . GLU   A 298 ? 0.7998 0.7756 0.7900 0.0523  -0.0906 -0.0652 325 GLU   A C    
2021 O  O    . GLU   A 298 ? 0.9317 0.8950 0.9250 0.0407  -0.0849 -0.0550 325 GLU   A O    
2022 C  CB   . GLU   A 298 ? 0.8335 0.8231 0.8768 0.0373  -0.0936 -0.0802 325 GLU   A CB   
2023 C  CG   . GLU   A 298 ? 0.9323 0.9263 0.9987 0.0321  -0.0941 -0.0818 325 GLU   A CG   
2024 C  CD   . GLU   A 298 ? 1.0284 1.0402 1.0984 0.0426  -0.1021 -0.0973 325 GLU   A CD   
2025 O  OE1  . GLU   A 298 ? 0.9892 1.0031 1.0713 0.0395  -0.1010 -0.0958 325 GLU   A OE1  
2026 O  OE2  . GLU   A 298 ? 1.0136 1.0415 1.0759 0.0550  -0.1097 -0.1121 325 GLU   A OE2  
2027 N  N    . CYS   A 299 ? 0.8579 0.8408 0.8309 0.0684  -0.0942 -0.0679 326 CYS   A N    
2028 C  CA   . CYS   A 299 ? 0.8637 0.8327 0.8191 0.0731  -0.0891 -0.0566 326 CYS   A CA   
2029 C  C    . CYS   A 299 ? 0.7599 0.7465 0.7256 0.0815  -0.0972 -0.0665 326 CYS   A C    
2030 O  O    . CYS   A 299 ? 0.9020 0.8846 0.8495 0.0948  -0.0954 -0.0603 326 CYS   A O    
2031 C  CB   . CYS   A 299 ? 0.8752 0.8309 0.7972 0.0881  -0.0807 -0.0440 326 CYS   A CB   
2032 S  SG   . CYS   A 299 ? 1.1174 1.1005 1.0202 0.1156  -0.0891 -0.0521 326 CYS   A SG   
2033 N  N    . SER   A 300 ? 0.7619 0.7680 0.7606 0.0743  -0.1045 -0.0819 327 SER   A N    
2034 C  CA   . SER   A 300 ? 0.8140 0.8401 0.8301 0.0799  -0.1112 -0.0937 327 SER   A CA   
2035 C  C    . SER   A 300 ? 0.8063 0.8181 0.8203 0.0744  -0.1044 -0.0820 327 SER   A C    
2036 O  O    . SER   A 300 ? 0.7719 0.7962 0.7888 0.0840  -0.1081 -0.0872 327 SER   A O    
2037 C  CB   . SER   A 300 ? 0.7500 0.7966 0.8107 0.0697  -0.1160 -0.1130 327 SER   A CB   
2038 O  OG   . SER   A 300 ? 0.7158 0.7467 0.7968 0.0510  -0.1066 -0.1028 327 SER   A OG   
2039 N  N    . THR   A 301 ? 0.7671 0.7574 0.7770 0.0603  -0.0952 -0.0686 328 THR   A N    
2040 C  CA   . THR   A 301 ? 0.6941 0.6720 0.6972 0.0562  -0.0883 -0.0596 328 THR   A CA   
2041 C  C    . THR   A 301 ? 0.6983 0.6514 0.6756 0.0542  -0.0798 -0.0479 328 THR   A C    
2042 O  O    . THR   A 301 ? 0.8717 0.8159 0.8485 0.0442  -0.0735 -0.0435 328 THR   A O    
2043 C  CB   . THR   A 301 ? 0.7023 0.6859 0.7300 0.0417  -0.0845 -0.0580 328 THR   A CB   
2044 O  OG1  . THR   A 301 ? 0.9540 0.9303 0.9827 0.0309  -0.0809 -0.0509 328 THR   A OG1  
2045 C  CG2  . THR   A 301 ? 0.6650 0.6704 0.7274 0.0411  -0.0887 -0.0701 328 THR   A CG2  
2046 N  N    . GLY   A 302 ? 0.6814 0.6258 0.6393 0.0641  -0.0784 -0.0442 329 GLY   A N    
2047 C  CA   . GLY   A 302 ? 0.7219 0.6419 0.6630 0.0602  -0.0672 -0.0342 329 GLY   A CA   
2048 C  C    . GLY   A 302 ? 0.8308 0.7363 0.7482 0.0779  -0.0599 -0.0252 329 GLY   A C    
2049 O  O    . GLY   A 302 ? 0.7779 0.6660 0.6850 0.0761  -0.0494 -0.0169 329 GLY   A O    
2050 N  N    . THR   A 303 ? 0.7821 0.6957 0.6918 0.0964  -0.0639 -0.0254 330 THR   A N    
2051 C  CA   . THR   A 303 ? 0.8827 0.7821 0.7679 0.1181  -0.0546 -0.0121 330 THR   A CA   
2052 C  C    . THR   A 303 ? 0.8525 0.7374 0.7373 0.1242  -0.0477 -0.0082 330 THR   A C    
2053 O  O    . THR   A 303 ? 0.9059 0.8033 0.8067 0.1175  -0.0551 -0.0185 330 THR   A O    
2054 C  CB   . THR   A 303 ? 0.7482 0.6754 0.6199 0.1426  -0.0654 -0.0147 330 THR   A CB   
2055 O  OG1  . THR   A 303 ? 0.7589 0.7120 0.6424 0.1511  -0.0784 -0.0269 330 THR   A OG1  
2056 C  CG2  . THR   A 303 ? 0.7851 0.7316 0.6634 0.1356  -0.0743 -0.0250 330 THR   A CG2  
2057 N  N    . LEU   A 304 ? 0.9758 0.8330 0.8440 0.1375  -0.0311 0.0079  331 LEU   A N    
2058 C  CA   . LEU   A 304 ? 0.9004 0.7400 0.7694 0.1460  -0.0220 0.0122  331 LEU   A CA   
2059 C  C    . LEU   A 304 ? 0.9016 0.7700 0.7685 0.1666  -0.0360 0.0074  331 LEU   A C    
2060 O  O    . LEU   A 304 ? 0.9714 0.8408 0.8503 0.1647  -0.0371 0.0006  331 LEU   A O    
2061 C  CB   . LEU   A 304 ? 0.9350 0.7377 0.7893 0.1602  0.0016  0.0331  331 LEU   A CB   
2062 C  CG   . LEU   A 304 ? 1.0669 0.8442 0.9257 0.1694  0.0154  0.0384  331 LEU   A CG   
2063 C  CD1  . LEU   A 304 ? 0.9036 0.6718 0.7874 0.1417  0.0172  0.0201  331 LEU   A CD1  
2064 C  CD2  . LEU   A 304 ? 1.0087 0.7464 0.8562 0.1858  0.0427  0.0627  331 LEU   A CD2  
2065 N  N    . ASP   A 305 ? 0.9644 0.8605 0.8175 0.1871  -0.0471 0.0083  332 ASP   A N    
2066 C  CA   . ASP   A 305 ? 0.8919 0.8239 0.7473 0.2072  -0.0625 -0.0010 332 ASP   A CA   
2067 C  C    . ASP   A 305 ? 0.8517 0.8081 0.7386 0.1862  -0.0765 -0.0233 332 ASP   A C    
2068 O  O    . ASP   A 305 ? 0.8530 0.8253 0.7519 0.1931  -0.0819 -0.0308 332 ASP   A O    
2069 C  CB   . ASP   A 305 ? 0.9305 0.8960 0.7674 0.2320  -0.0738 -0.0016 332 ASP   A CB   
2070 C  CG   . ASP   A 305 ? 1.2195 1.1657 1.0215 0.2611  -0.0580 0.0253  332 ASP   A CG   
2071 O  OD1  . ASP   A 305 ? 1.2563 1.1605 1.0536 0.2617  -0.0372 0.0439  332 ASP   A OD1  
2072 O  OD2  . ASP   A 305 ? 1.3868 1.3607 1.1673 0.2841  -0.0649 0.0275  332 ASP   A OD2  
2073 N  N    . TYR   A 306 ? 0.8438 0.8033 0.7458 0.1617  -0.0805 -0.0325 333 TYR   A N    
2074 C  CA   . TYR   A 306 ? 0.8046 0.7835 0.7378 0.1425  -0.0891 -0.0489 333 TYR   A CA   
2075 C  C    . TYR   A 306 ? 0.8532 0.8149 0.7946 0.1315  -0.0801 -0.0465 333 TYR   A C    
2076 O  O    . TYR   A 306 ? 0.9061 0.8866 0.8657 0.1317  -0.0847 -0.0557 333 TYR   A O    
2077 C  CB   . TYR   A 306 ? 0.7519 0.7319 0.6980 0.1211  -0.0913 -0.0541 333 TYR   A CB   
2078 C  CG   . TYR   A 306 ? 0.7408 0.7266 0.7155 0.0996  -0.0914 -0.0614 333 TYR   A CG   
2079 C  CD1  . TYR   A 306 ? 0.6269 0.6422 0.6318 0.0969  -0.1001 -0.0763 333 TYR   A CD1  
2080 C  CD2  . TYR   A 306 ? 0.6873 0.6518 0.6604 0.0832  -0.0816 -0.0537 333 TYR   A CD2  
2081 C  CE1  . TYR   A 306 ? 0.5994 0.6183 0.6306 0.0794  -0.0960 -0.0782 333 TYR   A CE1  
2082 C  CE2  . TYR   A 306 ? 0.6832 0.6565 0.6776 0.0680  -0.0803 -0.0568 333 TYR   A CE2  
2083 C  CZ   . TYR   A 306 ? 0.6878 0.6861 0.7103 0.0666  -0.0861 -0.0665 333 TYR   A CZ   
2084 O  OH   . TYR   A 306 ? 0.7838 0.7890 0.8277 0.0535  -0.0808 -0.0650 333 TYR   A OH   
2085 N  N    . ILE   A 307 ? 0.7567 0.6853 0.6871 0.1218  -0.0666 -0.0366 334 ILE   A N    
2086 C  CA   . ILE   A 307 ? 0.7195 0.6365 0.6586 0.1096  -0.0588 -0.0393 334 ILE   A CA   
2087 C  C    . ILE   A 307 ? 0.9547 0.8646 0.8890 0.1276  -0.0534 -0.0369 334 ILE   A C    
2088 O  O    . ILE   A 307 ? 0.7988 0.7128 0.7446 0.1226  -0.0512 -0.0438 334 ILE   A O    
2089 C  CB   . ILE   A 307 ? 0.7179 0.6086 0.6524 0.0928  -0.0474 -0.0358 334 ILE   A CB   
2090 C  CG1  . ILE   A 307 ? 0.7727 0.6623 0.7175 0.0794  -0.0425 -0.0442 334 ILE   A CG1  
2091 C  CG2  . ILE   A 307 ? 0.9683 0.8275 0.8863 0.1039  -0.0338 -0.0241 334 ILE   A CG2  
2092 C  CD1  . ILE   A 307 ? 0.7369 0.6545 0.6968 0.0674  -0.0509 -0.0505 334 ILE   A CD1  
2093 N  N    . LEU   A 308 ? 0.9025 0.8029 0.8191 0.1511  -0.0500 -0.0258 335 LEU   A N    
2094 C  CA   . LEU   A 308 ? 0.8042 0.7002 0.7171 0.1726  -0.0451 -0.0217 335 LEU   A CA   
2095 C  C    . LEU   A 308 ? 0.9122 0.8496 0.8398 0.1823  -0.0606 -0.0338 335 LEU   A C    
2096 O  O    . LEU   A 308 ? 1.0016 0.9425 0.9387 0.1878  -0.0582 -0.0382 335 LEU   A O    
2097 C  CB   . LEU   A 308 ? 0.7725 0.6496 0.6614 0.1995  -0.0355 -0.0023 335 LEU   A CB   
2098 C  CG   . LEU   A 308 ? 0.9562 0.7854 0.8371 0.1938  -0.0128 0.0116  335 LEU   A CG   
2099 C  CD1  . LEU   A 308 ? 0.7660 0.5789 0.6231 0.2250  -0.0009 0.0357  335 LEU   A CD1  
2100 C  CD2  . LEU   A 308 ? 0.8236 0.6273 0.7200 0.1827  0.0006  0.0048  335 LEU   A CD2  
2101 N  N    . GLN   A 309 ? 0.8933 0.8637 0.8266 0.1840  -0.0758 -0.0420 336 GLN   A N    
2102 C  CA   . GLN   A 309 ? 0.8889 0.9022 0.8459 0.1891  -0.0899 -0.0586 336 GLN   A CA   
2103 C  C    . GLN   A 309 ? 0.8482 0.8657 0.8323 0.1645  -0.0873 -0.0685 336 GLN   A C    
2104 O  O    . GLN   A 309 ? 0.9058 0.9412 0.9069 0.1691  -0.0883 -0.0761 336 GLN   A O    
2105 C  CB   . GLN   A 309 ? 0.9149 0.9619 0.8779 0.1930  -0.1052 -0.0700 336 GLN   A CB   
2106 C  CG   . GLN   A 309 ? 1.1089 1.2080 1.0991 0.2040  -0.1214 -0.0918 336 GLN   A CG   
2107 C  CD   . GLN   A 309 ? 1.4101 1.5240 1.4384 0.1865  -0.1205 -0.1051 336 GLN   A CD   
2108 O  OE1  . GLN   A 309 ? 1.3522 1.4962 1.3977 0.1997  -0.1265 -0.1160 336 GLN   A OE1  
2109 N  NE2  . GLN   A 309 ? 1.1314 1.2295 1.1751 0.1581  -0.1131 -0.1044 336 GLN   A NE2  
2110 N  N    . ARG   A 310 ? 0.8438 0.8471 0.8313 0.1403  -0.0829 -0.0671 337 ARG   A N    
2111 C  CA   . ARG   A 310 ? 0.7785 0.7864 0.7864 0.1202  -0.0781 -0.0719 337 ARG   A CA   
2112 C  C    . ARG   A 310 ? 0.7817 0.7763 0.7844 0.1233  -0.0679 -0.0701 337 ARG   A C    
2113 O  O    . ARG   A 310 ? 0.8186 0.8304 0.8398 0.1186  -0.0658 -0.0764 337 ARG   A O    
2114 C  CB   . ARG   A 310 ? 0.7108 0.7040 0.7156 0.0994  -0.0741 -0.0669 337 ARG   A CB   
2115 C  CG   . ARG   A 310 ? 0.8152 0.8226 0.8321 0.0936  -0.0826 -0.0709 337 ARG   A CG   
2116 C  CD   . ARG   A 310 ? 0.6682 0.7013 0.7208 0.0827  -0.0840 -0.0795 337 ARG   A CD   
2117 N  NE   . ARG   A 310 ? 0.7744 0.7995 0.8307 0.0666  -0.0739 -0.0714 337 ARG   A NE   
2118 C  CZ   . ARG   A 310 ? 0.7939 0.8353 0.8778 0.0577  -0.0683 -0.0720 337 ARG   A CZ   
2119 N  NH1  . ARG   A 310 ? 0.6512 0.7163 0.7681 0.0597  -0.0710 -0.0831 337 ARG   A NH1  
2120 N  NH2  . ARG   A 310 ? 0.6814 0.7176 0.7611 0.0476  -0.0587 -0.0616 337 ARG   A NH2  
2121 N  N    . CYS   A 311 ? 0.8103 0.7739 0.7907 0.1315  -0.0595 -0.0620 338 CYS   A N    
2122 C  CA   . CYS   A 311 ? 0.8689 0.8179 0.8474 0.1357  -0.0487 -0.0634 338 CYS   A CA   
2123 C  C    . CYS   A 311 ? 0.9434 0.9116 0.9305 0.1570  -0.0523 -0.0668 338 CYS   A C    
2124 O  O    . CYS   A 311 ? 0.9123 0.8896 0.9114 0.1559  -0.0479 -0.0740 338 CYS   A O    
2125 C  CB   . CYS   A 311 ? 0.8460 0.7544 0.8062 0.1393  -0.0360 -0.0553 338 CYS   A CB   
2126 S  SG   . CYS   A 311 ? 0.9318 0.8216 0.8890 0.1123  -0.0292 -0.0581 338 CYS   A SG   
2127 N  N    . GLN   A 312 ? 0.8848 0.8635 0.8653 0.1783  -0.0604 -0.0623 339 GLN   A N    
2128 C  CA   . GLN   A 312 ? 0.8406 0.8449 0.8300 0.2017  -0.0662 -0.0666 339 GLN   A CA   
2129 C  C    . GLN   A 312 ? 0.7554 0.8004 0.7773 0.1911  -0.0743 -0.0828 339 GLN   A C    
2130 O  O    . GLN   A 312 ? 0.9105 0.9722 0.9470 0.2004  -0.0730 -0.0893 339 GLN   A O    
2131 C  CB   . GLN   A 312 ? 0.8708 0.8883 0.8451 0.2283  -0.0757 -0.0600 339 GLN   A CB   
2132 C  CG   . GLN   A 312 ? 0.9422 1.0095 0.9344 0.2482  -0.0906 -0.0728 339 GLN   A CG   
2133 C  CD   . GLN   A 312 ? 1.1851 1.2638 1.1540 0.2852  -0.0966 -0.0627 339 GLN   A CD   
2134 O  OE1  . GLN   A 312 ? 1.3164 1.3751 1.2691 0.3089  -0.0866 -0.0477 339 GLN   A OE1  
2135 N  NE2  . GLN   A 312 ? 1.2055 1.3177 1.1728 0.2922  -0.1121 -0.0707 339 GLN   A NE2  
2136 N  N    . LEU   A 313 ? 0.9131 0.9732 0.9498 0.1717  -0.0805 -0.0891 340 LEU   A N    
2137 C  CA   . LEU   A 313 ? 0.9233 1.0183 0.9971 0.1599  -0.0836 -0.1027 340 LEU   A CA   
2138 C  C    . LEU   A 313 ? 0.7586 0.8463 0.8399 0.1464  -0.0701 -0.1013 340 LEU   A C    
2139 O  O    . LEU   A 313 ? 0.7572 0.8718 0.8659 0.1463  -0.0681 -0.1100 340 LEU   A O    
2140 C  CB   . LEU   A 313 ? 0.7886 0.8946 0.8790 0.1423  -0.0893 -0.1077 340 LEU   A CB   
2141 C  CG   . LEU   A 313 ? 0.8347 0.9670 0.9681 0.1249  -0.0859 -0.1179 340 LEU   A CG   
2142 C  CD1  . LEU   A 313 ? 0.7574 0.9314 0.9243 0.1372  -0.0933 -0.1359 340 LEU   A CD1  
2143 C  CD2  . LEU   A 313 ? 0.7618 0.8948 0.9103 0.1079  -0.0879 -0.1199 340 LEU   A CD2  
2144 N  N    . ALA   A 314 ? 0.7132 0.7688 0.7719 0.1358  -0.0605 -0.0922 341 ALA   A N    
2145 C  CA   . ALA   A 314 ? 0.8332 0.8872 0.8946 0.1259  -0.0485 -0.0930 341 ALA   A CA   
2146 C  C    . ALA   A 314 ? 0.8527 0.9040 0.9111 0.1424  -0.0429 -0.0973 341 ALA   A C    
2147 O  O    . ALA   A 314 ? 0.7567 0.8226 0.8270 0.1394  -0.0351 -0.1025 341 ALA   A O    
2148 C  CB   . ALA   A 314 ? 0.9619 0.9899 1.0015 0.1115  -0.0420 -0.0871 341 ALA   A CB   
2149 N  N    . LEU   A 315 ? 0.8701 0.9030 0.9130 0.1614  -0.0449 -0.0938 342 LEU   A N    
2150 C  CA   . LEU   A 315 ? 0.8010 0.8266 0.8419 0.1798  -0.0379 -0.0961 342 LEU   A CA   
2151 C  C    . LEU   A 315 ? 0.8883 0.9492 0.9496 0.1993  -0.0460 -0.1019 342 LEU   A C    
2152 O  O    . LEU   A 315 ? 0.9255 0.9843 0.9877 0.2176  -0.0407 -0.1034 342 LEU   A O    
2153 C  CB   . LEU   A 315 ? 0.8171 0.8017 0.8341 0.1933  -0.0315 -0.0862 342 LEU   A CB   
2154 C  CG   . LEU   A 315 ? 0.8230 0.7723 0.8259 0.1751  -0.0210 -0.0852 342 LEU   A CG   
2155 C  CD1  . LEU   A 315 ? 0.9366 0.8446 0.9243 0.1894  -0.0108 -0.0748 342 LEU   A CD1  
2156 C  CD2  . LEU   A 315 ? 0.8470 0.7990 0.8567 0.1626  -0.0114 -0.0984 342 LEU   A CD2  
2157 N  N    . GLN   A 316 ? 0.7875 0.8826 0.8685 0.1962  -0.0584 -0.1075 343 GLN   A N    
2158 C  CA   . GLN   A 316 ? 0.7410 0.8788 0.8499 0.2114  -0.0664 -0.1190 343 GLN   A CA   
2159 C  C    . GLN   A 316 ? 0.8388 0.9952 0.9731 0.2030  -0.0562 -0.1273 343 GLN   A C    
2160 O  O    . GLN   A 316 ? 0.8742 1.0629 1.0319 0.2176  -0.0594 -0.1371 343 GLN   A O    
2161 C  CB   . GLN   A 316 ? 0.7752 0.9478 0.9070 0.2063  -0.0809 -0.1289 343 GLN   A CB   
2162 C  CG   . GLN   A 316 ? 0.7163 0.8970 0.8308 0.2306  -0.0954 -0.1276 343 GLN   A CG   
2163 C  CD   . GLN   A 316 ? 0.8302 1.0309 0.9568 0.2197  -0.1076 -0.1367 343 GLN   A CD   
2164 O  OE1  . GLN   A 316 ? 0.9718 1.1603 1.0714 0.2288  -0.1139 -0.1293 343 GLN   A OE1  
2165 N  NE2  . GLN   A 316 ? 0.8866 1.1176 1.0562 0.2006  -0.1088 -0.1531 343 GLN   A NE2  
2166 N  N    . ASN   A 317 ? 0.7820 0.9223 0.9114 0.1817  -0.0440 -0.1236 344 ASN   A N    
2167 C  CA   . ASN   A 317 ? 0.8180 0.9743 0.9644 0.1749  -0.0313 -0.1286 344 ASN   A CA   
2168 C  C    . ASN   A 317 ? 0.9283 1.0631 1.0555 0.1868  -0.0211 -0.1294 344 ASN   A C    
2169 O  O    . ASN   A 317 ? 0.8312 0.9755 0.9644 0.1811  -0.0091 -0.1338 344 ASN   A O    
2170 C  CB   . ASN   A 317 ? 0.7020 0.8572 0.8502 0.1499  -0.0225 -0.1228 344 ASN   A CB   
2171 C  CG   . ASN   A 317 ? 0.8626 1.0486 1.0398 0.1430  -0.0098 -0.1260 344 ASN   A CG   
2172 O  OD1  . ASN   A 317 ? 1.0449 1.2629 1.2586 0.1472  -0.0114 -0.1344 344 ASN   A OD1  
2173 N  ND2  . ASN   A 317 ? 0.8186 0.9986 0.9808 0.1334  0.0037  -0.1199 344 ASN   A ND2  
2174 N  N    . VAL   A 318 ? 0.9090 1.0151 1.0146 0.2040  -0.0237 -0.1253 345 VAL   A N    
2175 C  CA   . VAL   A 318 ? 0.9098 0.9872 1.0004 0.2140  -0.0116 -0.1270 345 VAL   A CA   
2176 C  C    . VAL   A 318 ? 0.8952 0.9743 0.9901 0.2446  -0.0139 -0.1260 345 VAL   A C    
2177 O  O    . VAL   A 318 ? 0.8809 0.9639 0.9717 0.2601  -0.0251 -0.1183 345 VAL   A O    
2178 C  CB   . VAL   A 318 ? 0.8413 0.8733 0.9045 0.2051  -0.0064 -0.1212 345 VAL   A CB   
2179 C  CG1  . VAL   A 318 ? 0.8543 0.8568 0.9106 0.2126  0.0085  -0.1282 345 VAL   A CG1  
2180 C  CG2  . VAL   A 318 ? 0.8826 0.9185 0.9407 0.1781  -0.0067 -0.1213 345 VAL   A CG2  
2181 N  N    . CYS   A 319 ? 0.8495 0.9286 0.9519 0.2557  -0.0032 -0.1336 346 CYS   A N    
2182 C  CA   A CYS   A 319 ? 0.9373 1.0126 1.0423 0.2878  -0.0022 -0.1307 346 CYS   A CA   
2183 C  CA   B CYS   A 319 ? 1.0232 1.0985 1.1283 0.2878  -0.0022 -0.1307 346 CYS   A CA   
2184 C  C    . CYS   A 319 ? 0.9647 0.9868 1.0447 0.2986  0.0053  -0.1176 346 CYS   A C    
2185 O  O    . CYS   A 319 ? 1.0390 1.0241 1.1120 0.2920  0.0208  -0.1219 346 CYS   A O    
2186 C  CB   A CYS   A 319 ? 1.0054 1.0920 1.1265 0.2953  0.0096  -0.1433 346 CYS   A CB   
2187 C  CB   B CYS   A 319 ? 1.1021 1.1883 1.2230 0.2952  0.0097  -0.1433 346 CYS   A CB   
2188 S  SG   A CYS   A 319 ? 0.8729 1.0213 1.0277 0.2826  0.0066  -0.1566 346 CYS   A SG   
2189 S  SG   B CYS   A 319 ? 0.9260 0.9900 1.0465 0.3349  0.0180  -0.1382 346 CYS   A SG   
2190 N  N    . ASP   A 320 ? 1.0512 1.0713 1.1197 0.3155  -0.0044 -0.1028 347 ASP   A N    
2191 C  CA   . ASP   A 320 ? 0.9665 0.9371 1.0114 0.3250  0.0043  -0.0855 347 ASP   A CA   
2192 C  C    . ASP   A 320 ? 0.9605 0.9110 1.0021 0.3629  0.0145  -0.0724 347 ASP   A C    
2193 O  O    . ASP   A 320 ? 1.0380 0.9678 1.0614 0.3840  0.0164  -0.0515 347 ASP   A O    
2194 C  CB   . ASP   A 320 ? 0.9276 0.9073 0.9578 0.3223  -0.0098 -0.0745 347 ASP   A CB   
2195 C  CG   . ASP   A 320 ? 0.9020 0.9296 0.9374 0.3487  -0.0278 -0.0723 347 ASP   A CG   
2196 O  OD1  . ASP   A 320 ? 0.8863 0.9584 0.9467 0.3501  -0.0362 -0.0875 347 ASP   A OD1  
2197 O  OD2  . ASP   A 320 ? 1.0455 1.0697 1.0612 0.3687  -0.0333 -0.0566 347 ASP   A OD2  
2198 N  N    . ASP   A 321 ? 0.9333 0.8893 0.9919 0.3743  0.0228  -0.0824 348 ASP   A N    
2199 C  CA   . ASP   A 321 ? 1.0658 0.9976 1.1232 0.4118  0.0356  -0.0684 348 ASP   A CA   
2200 C  C    . ASP   A 321 ? 1.0429 0.9048 1.0912 0.4094  0.0602  -0.0583 348 ASP   A C    
2201 O  O    . ASP   A 321 ? 1.0094 0.8400 1.0458 0.4377  0.0707  -0.0337 348 ASP   A O    
2202 C  CB   . ASP   A 321 ? 0.9141 0.8694 0.9951 0.4237  0.0395  -0.0838 348 ASP   A CB   
2203 C  CG   . ASP   A 321 ? 0.9764 1.0016 1.0733 0.4326  0.0180  -0.0924 348 ASP   A CG   
2204 O  OD1  . ASP   A 321 ? 0.9042 0.9607 0.9972 0.4226  -0.0002 -0.0919 348 ASP   A OD1  
2205 O  OD2  . ASP   A 321 ? 0.9989 1.0488 1.1160 0.4494  0.0202  -0.1018 348 ASP   A OD2  
2206 N  N    . VAL   A 322 ? 1.0881 0.9270 1.1438 0.3768  0.0707  -0.0772 349 VAL   A N    
2207 C  CA   . VAL   A 322 ? 1.1626 0.9388 1.2212 0.3711  0.0959  -0.0769 349 VAL   A CA   
2208 C  C    . VAL   A 322 ? 1.1279 0.8976 1.1851 0.3295  0.0951  -0.0953 349 VAL   A C    
2209 O  O    . VAL   A 322 ? 1.1883 0.9990 1.2460 0.3078  0.0803  -0.1117 349 VAL   A O    
2210 C  CB   . VAL   A 322 ? 1.1974 0.9544 1.2776 0.3859  0.1149  -0.0897 349 VAL   A CB   
2211 C  CG1  . VAL   A 322 ? 1.0842 0.8808 1.1773 0.3654  0.1076  -0.1207 349 VAL   A CG1  
2212 C  CG2  . VAL   A 322 ? 1.2400 0.9290 1.3314 0.3817  0.1440  -0.0912 349 VAL   A CG2  
2213 N  N    . ASP   A 323 ? 1.2040 0.9230 1.2613 0.3198  0.1124  -0.0914 350 ASP   A N    
2214 C  CA   . ASP   A 323 ? 1.2443 0.9567 1.3018 0.2829  0.1123  -0.1092 350 ASP   A CA   
2215 C  C    . ASP   A 323 ? 1.3530 1.0479 1.4327 0.2688  0.1290  -0.1408 350 ASP   A C    
2216 O  O    . ASP   A 323 ? 1.4931 1.1376 1.5898 0.2715  0.1528  -0.1440 350 ASP   A O    
2217 C  CB   . ASP   A 323 ? 1.2683 0.9414 1.3172 0.2790  0.1214  -0.0898 350 ASP   A CB   
2218 C  CG   . ASP   A 323 ? 1.4438 1.1189 1.4927 0.2421  0.1175  -0.1072 350 ASP   A CG   
2219 O  OD1  . ASP   A 323 ? 1.5066 1.2199 1.5559 0.2222  0.1041  -0.1296 350 ASP   A OD1  
2220 O  OD2  . ASP   A 323 ? 1.5559 1.1961 1.6050 0.2346  0.1289  -0.0974 350 ASP   A OD2  
2221 N  N    . ASN   A 324 ? 1.3188 1.0564 1.4003 0.2543  0.1181  -0.1650 351 ASN   A N    
2222 C  CA   . ASN   A 324 ? 1.3841 1.1177 1.4825 0.2390  0.1301  -0.2002 351 ASN   A CA   
2223 C  C    . ASN   A 324 ? 1.5324 1.3176 1.6193 0.2149  0.1132  -0.2180 351 ASN   A C    
2224 O  O    . ASN   A 324 ? 1.5457 1.3598 1.6156 0.2081  0.0955  -0.2019 351 ASN   A O    
2225 C  CB   . ASN   A 324 ? 1.4691 1.1970 1.5851 0.2616  0.1430  -0.2102 351 ASN   A CB   
2226 C  CG   . ASN   A 324 ? 1.4137 1.1891 1.5222 0.2790  0.1277  -0.1997 351 ASN   A CG   
2227 O  OD1  . ASN   A 324 ? 1.4093 1.2319 1.5060 0.2657  0.1100  -0.2015 351 ASN   A OD1  
2228 N  ND2  . ASN   A 324 ? 1.2801 1.0434 1.3990 0.3097  0.1362  -0.1891 351 ASN   A ND2  
2229 N  N    . ASP   A 325 ? 1.5120 1.3099 1.6087 0.2037  0.1200  -0.2516 352 ASP   A N    
2230 C  CA   . ASP   A 325 ? 1.4692 1.3171 1.5528 0.1845  0.1074  -0.2680 352 ASP   A CA   
2231 C  C    . ASP   A 325 ? 1.4279 1.3240 1.5046 0.1943  0.0986  -0.2632 352 ASP   A C    
2232 O  O    . ASP   A 325 ? 1.4104 1.3495 1.4747 0.1819  0.0902  -0.2699 352 ASP   A O    
2233 C  CB   . ASP   A 325 ? 1.6239 1.4726 1.7193 0.1703  0.1178  -0.3089 352 ASP   A CB   
2234 C  CG   . ASP   A 325 ? 1.7672 1.5634 1.8828 0.1617  0.1326  -0.3192 352 ASP   A CG   
2235 O  OD1  . ASP   A 325 ? 1.8342 1.5821 1.9654 0.1774  0.1475  -0.3050 352 ASP   A OD1  
2236 O  OD2  . ASP   A 325 ? 1.7742 1.5786 1.8919 0.1403  0.1306  -0.3410 352 ASP   A OD2  
2237 N  N    . ASP   A 326 ? 1.4532 1.3448 1.5391 0.2175  0.1018  -0.2508 353 ASP   A N    
2238 C  CA   . ASP   A 326 ? 1.4455 1.3838 1.5316 0.2268  0.0951  -0.2466 353 ASP   A CA   
2239 C  C    . ASP   A 326 ? 1.3594 1.3186 1.4371 0.2249  0.0783  -0.2189 353 ASP   A C    
2240 O  O    . ASP   A 326 ? 1.4186 1.3787 1.5029 0.2430  0.0731  -0.2015 353 ASP   A O    
2241 C  CB   . ASP   A 326 ? 1.3608 1.2898 1.4646 0.2529  0.1054  -0.2489 353 ASP   A CB   
2242 N  N    . VAL   A 327 ? 1.1727 1.1518 1.2372 0.2037  0.0696  -0.2168 354 VAL   A N    
2243 C  CA   . VAL   A 327 ? 1.1212 1.1183 1.1812 0.1984  0.0551  -0.1943 354 VAL   A CA   
2244 C  C    . VAL   A 327 ? 1.0576 1.1028 1.1280 0.2008  0.0524  -0.1918 354 VAL   A C    
2245 O  O    . VAL   A 327 ? 1.1601 1.2335 1.2272 0.1920  0.0580  -0.2018 354 VAL   A O    
2246 C  CB   . VAL   A 327 ? 1.1941 1.1889 1.2385 0.1760  0.0491  -0.1919 354 VAL   A CB   
2247 C  CG1  . VAL   A 327 ? 1.0281 1.0490 1.0719 0.1689  0.0365  -0.1727 354 VAL   A CG1  
2248 C  CG2  . VAL   A 327 ? 1.2391 1.1867 1.2788 0.1737  0.0517  -0.1902 354 VAL   A CG2  
2249 N  N    . SER   A 328 ? 1.0866 1.1444 1.1712 0.2139  0.0450  -0.1792 355 SER   A N    
2250 C  CA   . SER   A 328 ? 1.1214 1.2250 1.2255 0.2159  0.0438  -0.1778 355 SER   A CA   
2251 C  C    . SER   A 328 ? 0.9721 1.0921 1.0850 0.2085  0.0304  -0.1632 355 SER   A C    
2252 O  O    . SER   A 328 ? 1.1030 1.2102 1.2162 0.2189  0.0200  -0.1554 355 SER   A O    
2253 C  CB   . SER   A 328 ? 1.0531 1.1659 1.1761 0.2401  0.0477  -0.1837 355 SER   A CB   
2254 O  OG   . SER   A 328 ? 1.2795 1.4036 1.4166 0.2537  0.0352  -0.1732 355 SER   A OG   
2255 N  N    . LEU   A 329 ? 0.9701 1.1193 1.0909 0.1920  0.0322  -0.1596 356 LEU   A N    
2256 C  CA   . LEU   A 329 ? 0.9900 1.1531 1.1236 0.1811  0.0224  -0.1486 356 LEU   A CA   
2257 C  C    . LEU   A 329 ? 0.9598 1.1619 1.1315 0.1877  0.0207  -0.1513 356 LEU   A C    
2258 O  O    . LEU   A 329 ? 0.9596 1.1884 1.1487 0.1891  0.0326  -0.1565 356 LEU   A O    
2259 C  CB   . LEU   A 329 ? 0.9265 1.0963 1.0514 0.1602  0.0280  -0.1410 356 LEU   A CB   
2260 C  CG   . LEU   A 329 ? 0.9776 1.1205 1.0687 0.1517  0.0296  -0.1418 356 LEU   A CG   
2261 C  CD1  . LEU   A 329 ? 1.0264 1.1779 1.1121 0.1344  0.0296  -0.1294 356 LEU   A CD1  
2262 C  CD2  . LEU   A 329 ? 0.9754 1.0793 1.0519 0.1574  0.0206  -0.1431 356 LEU   A CD2  
2263 N  N    . LYS   A 330 ? 0.9982 1.2075 1.1847 0.1915  0.0063  -0.1496 357 LYS   A N    
2264 C  CA   . LYS   A 330 ? 0.9570 1.2083 1.1852 0.1987  0.0021  -0.1580 357 LYS   A CA   
2265 C  C    . LYS   A 330 ? 0.9045 1.1856 1.1659 0.1785  0.0129  -0.1570 357 LYS   A C    
2266 O  O    . LYS   A 330 ? 0.9764 1.2925 1.2738 0.1813  0.0209  -0.1649 357 LYS   A O    
2267 C  CB   . LYS   A 330 ? 0.8682 1.1250 1.1023 0.2091  -0.0175 -0.1601 357 LYS   A CB   
2268 C  CG   . LYS   A 330 ? 0.8519 1.0765 1.0518 0.2311  -0.0252 -0.1547 357 LYS   A CG   
2269 C  CD   . LYS   A 330 ? 1.0710 1.3249 1.2866 0.2570  -0.0405 -0.1613 357 LYS   A CD   
2270 C  CE   . LYS   A 330 ? 0.8841 1.1202 1.0741 0.2666  -0.0545 -0.1527 357 LYS   A CE   
2271 N  NZ   . LYS   A 330 ? 1.1000 1.2881 1.2510 0.2834  -0.0482 -0.1383 357 LYS   A NZ   
2272 N  N    . SER   A 331 ? 0.8732 1.1410 1.1263 0.1591  0.0152  -0.1463 358 SER   A N    
2273 C  CA   . SER   A 331 ? 0.7878 1.0785 1.0748 0.1411  0.0281  -0.1411 358 SER   A CA   
2274 C  C    . SER   A 331 ? 0.9069 1.1800 1.1651 0.1284  0.0420  -0.1246 358 SER   A C    
2275 O  O    . SER   A 331 ? 1.0245 1.2675 1.2423 0.1275  0.0354  -0.1195 358 SER   A O    
2276 C  CB   . SER   A 331 ? 0.7550 1.0552 1.0732 0.1314  0.0169  -0.1450 358 SER   A CB   
2277 O  OG   . SER   A 331 ? 0.7294 1.0468 1.0866 0.1133  0.0335  -0.1391 358 SER   A OG   
2278 N  N    . PHE   A 332 ? 0.8899 1.1851 1.1711 0.1198  0.0624  -0.1161 359 PHE   A N    
2279 C  CA   . PHE   A 332 ? 0.9427 1.2306 1.2006 0.1105  0.0771  -0.0972 359 PHE   A CA   
2280 C  C    . PHE   A 332 ? 0.8725 1.1687 1.1668 0.0951  0.0889  -0.0829 359 PHE   A C    
2281 O  O    . PHE   A 332 ? 0.8362 1.1374 1.1247 0.0905  0.1087  -0.0633 359 PHE   A O    
2282 C  CB   . PHE   A 332 ? 0.8277 1.1330 1.0712 0.1183  0.0958  -0.0945 359 PHE   A CB   
2283 C  CG   . PHE   A 332 ? 0.9401 1.2320 1.1451 0.1317  0.0873  -0.1087 359 PHE   A CG   
2284 C  CD1  . PHE   A 332 ? 1.0459 1.3156 1.2058 0.1309  0.0817  -0.1075 359 PHE   A CD1  
2285 C  CD2  . PHE   A 332 ? 0.9676 1.2698 1.1859 0.1452  0.0859  -0.1248 359 PHE   A CD2  
2286 C  CE1  . PHE   A 332 ? 0.9745 1.2300 1.1068 0.1413  0.0765  -0.1239 359 PHE   A CE1  
2287 C  CE2  . PHE   A 332 ? 0.9450 1.2308 1.1327 0.1576  0.0811  -0.1381 359 PHE   A CE2  
2288 C  CZ   . PHE   A 332 ? 0.9323 1.1934 1.0787 0.1547  0.0772  -0.1385 359 PHE   A CZ   
2289 N  N    . GLU   A 333 ? 0.8727 1.1721 1.2058 0.0886  0.0784  -0.0927 360 GLU   A N    
2290 C  CA   . GLU   A 333 ? 0.9199 1.2225 1.2936 0.0727  0.0898  -0.0828 360 GLU   A CA   
2291 C  C    . GLU   A 333 ? 0.9708 1.2449 1.3077 0.0665  0.0880  -0.0643 360 GLU   A C    
2292 O  O    . GLU   A 333 ? 0.9156 1.1678 1.2148 0.0702  0.0674  -0.0698 360 GLU   A O    
2293 C  CB   . GLU   A 333 ? 0.9380 1.2538 1.3598 0.0685  0.0746  -0.1055 360 GLU   A CB   
2294 C  CG   . GLU   A 333 ? 1.0329 1.3573 1.5160 0.0509  0.0859  -0.1063 360 GLU   A CG   
2295 C  CD   . GLU   A 333 ? 1.2259 1.5207 1.6921 0.0407  0.0870  -0.0890 360 GLU   A CD   
2296 O  OE1  . GLU   A 333 ? 1.2308 1.5125 1.6827 0.0410  0.0646  -0.1000 360 GLU   A OE1  
2297 O  OE2  . GLU   A 333 ? 1.1599 1.4475 1.6314 0.0336  0.1115  -0.0642 360 GLU   A OE2  
2298 N  N    . PRO   A 334 ? 1.1108 1.3854 1.4567 0.0591  0.1108  -0.0405 361 PRO   A N    
2299 C  CA   . PRO   A 334 ? 0.9004 1.1524 1.2121 0.0558  0.1097  -0.0215 361 PRO   A CA   
2300 C  C    . PRO   A 334 ? 0.9015 1.1308 1.2077 0.0500  0.0865  -0.0315 361 PRO   A C    
2301 O  O    . PRO   A 334 ? 0.9539 1.1650 1.2122 0.0536  0.0738  -0.0282 361 PRO   A O    
2302 C  CB   . PRO   A 334 ? 0.9756 1.2351 1.3236 0.0486  0.1402  0.0039  361 PRO   A CB   
2303 C  CG   . PRO   A 334 ? 1.0726 1.3593 1.4400 0.0542  0.1604  0.0048  361 PRO   A CG   
2304 C  CD   . PRO   A 334 ? 0.9868 1.2844 1.3709 0.0567  0.1413  -0.0272 361 PRO   A CD   
2305 N  N    . ALA   A 335 ? 0.8222 1.0549 1.1765 0.0413  0.0809  -0.0458 362 ALA   A N    
2306 C  CA   . ALA   A 335 ? 0.8367 1.0500 1.1832 0.0369  0.0611  -0.0535 362 ALA   A CA   
2307 C  C    . ALA   A 335 ? 0.8636 1.0674 1.1676 0.0480  0.0355  -0.0690 362 ALA   A C    
2308 O  O    . ALA   A 335 ? 0.8219 1.0041 1.0948 0.0478  0.0221  -0.0672 362 ALA   A O    
2309 C  CB   . ALA   A 335 ? 0.5732 0.7976 0.9837 0.0259  0.0611  -0.0696 362 ALA   A CB   
2310 N  N    . VAL   A 336 ? 0.8876 1.1064 1.1914 0.0588  0.0306  -0.0829 363 VAL   A N    
2311 C  CA   . VAL   A 336 ? 0.9595 1.1654 1.2238 0.0719  0.0110  -0.0934 363 VAL   A CA   
2312 C  C    . VAL   A 336 ? 0.9094 1.0925 1.1208 0.0748  0.0132  -0.0812 363 VAL   A C    
2313 O  O    . VAL   A 336 ? 0.7608 0.9212 0.9391 0.0788  0.0001  -0.0834 363 VAL   A O    
2314 C  CB   . VAL   A 336 ? 0.7286 0.9566 1.0083 0.0854  0.0069  -0.1098 363 VAL   A CB   
2315 C  CG1  . VAL   A 336 ? 0.7527 0.9643 0.9955 0.1015  -0.0110 -0.1173 363 VAL   A CG1  
2316 C  CG2  . VAL   A 336 ? 0.8486 1.1081 1.1875 0.0815  0.0050  -0.1262 363 VAL   A CG2  
2317 N  N    . LEU   A 337 ? 0.9242 1.1160 1.1288 0.0734  0.0308  -0.0694 364 LEU   A N    
2318 C  CA   . LEU   A 337 ? 0.7740 0.9531 0.9319 0.0764  0.0323  -0.0629 364 LEU   A CA   
2319 C  C    . LEU   A 337 ? 0.8073 0.9722 0.9488 0.0677  0.0306  -0.0491 364 LEU   A C    
2320 O  O    . LEU   A 337 ? 0.8278 0.9770 0.9336 0.0688  0.0224  -0.0511 364 LEU   A O    
2321 C  CB   . LEU   A 337 ? 0.7172 0.9182 0.8707 0.0813  0.0508  -0.0568 364 LEU   A CB   
2322 C  CG   . LEU   A 337 ? 0.7134 0.9297 0.8809 0.0913  0.0538  -0.0711 364 LEU   A CG   
2323 C  CD1  . LEU   A 337 ? 0.7839 1.0244 0.9464 0.0961  0.0743  -0.0637 364 LEU   A CD1  
2324 C  CD2  . LEU   A 337 ? 0.8792 1.0759 1.0206 0.1011  0.0389  -0.0878 364 LEU   A CD2  
2325 N  N    . LYS   A 338 ? 0.9580 1.1287 1.1294 0.0591  0.0397  -0.0360 365 LYS   A N    
2326 C  CA   . LYS   A 338 ? 0.8127 0.9689 0.9742 0.0521  0.0372  -0.0233 365 LYS   A CA   
2327 C  C    . LYS   A 338 ? 0.7863 0.9207 0.9349 0.0504  0.0162  -0.0360 365 LYS   A C    
2328 O  O    . LYS   A 338 ? 0.8547 0.9745 0.9725 0.0493  0.0092  -0.0324 365 LYS   A O    
2329 C  CB   . LYS   A 338 ? 0.8343 0.9966 1.0406 0.0435  0.0521  -0.0097 365 LYS   A CB   
2330 C  CG   . LYS   A 338 ? 0.8842 1.0375 1.0806 0.0401  0.0591  0.0121  365 LYS   A CG   
2331 C  CD   . LYS   A 338 ? 0.9500 1.1042 1.1991 0.0317  0.0772  0.0248  365 LYS   A CD   
2332 C  CE   . LYS   A 338 ? 0.9316 1.0711 1.1754 0.0291  0.0805  0.0436  365 LYS   A CE   
2333 N  NZ   . LYS   A 338 ? 1.0234 1.1733 1.2430 0.0389  0.0992  0.0736  365 LYS   A NZ   
2334 N  N    . GLN   A 339 ? 0.7533 0.8889 0.9256 0.0517  0.0064  -0.0513 366 GLN   A N    
2335 C  CA   . GLN   A 339 ? 0.7553 0.8737 0.9139 0.0539  -0.0119 -0.0615 366 GLN   A CA   
2336 C  C    . GLN   A 339 ? 0.8600 0.9613 0.9768 0.0623  -0.0188 -0.0657 366 GLN   A C    
2337 O  O    . GLN   A 339 ? 0.8983 0.9792 0.9926 0.0616  -0.0277 -0.0656 366 GLN   A O    
2338 C  CB   . GLN   A 339 ? 0.7551 0.8880 0.9466 0.0581  -0.0208 -0.0781 366 GLN   A CB   
2339 C  CG   . GLN   A 339 ? 0.7814 0.9032 0.9584 0.0645  -0.0389 -0.0876 366 GLN   A CG   
2340 C  CD   . GLN   A 339 ? 0.7394 0.8863 0.9508 0.0708  -0.0488 -0.1064 366 GLN   A CD   
2341 O  OE1  . GLN   A 339 ? 0.8408 0.9950 1.0750 0.0652  -0.0549 -0.1147 366 GLN   A OE1  
2342 N  NE2  . GLN   A 339 ? 0.6876 0.8515 0.9049 0.0834  -0.0508 -0.1157 366 GLN   A NE2  
2343 N  N    . GLY   A 340 ? 0.6689 0.7775 0.7784 0.0699  -0.0128 -0.0702 367 GLY   A N    
2344 C  CA   . GLY   A 340 ? 0.7832 0.8733 0.8608 0.0774  -0.0164 -0.0770 367 GLY   A CA   
2345 C  C    . GLY   A 340 ? 0.8112 0.8903 0.8609 0.0706  -0.0140 -0.0726 367 GLY   A C    
2346 O  O    . GLY   A 340 ? 0.8550 0.9113 0.8852 0.0706  -0.0199 -0.0771 367 GLY   A O    
2347 N  N    . GLU   A 341 ? 0.8173 0.9149 0.8661 0.0659  -0.0043 -0.0638 368 GLU   A N    
2348 C  CA   . GLU   A 341 ? 0.8509 0.9483 0.8735 0.0620  -0.0035 -0.0619 368 GLU   A CA   
2349 C  C    . GLU   A 341 ? 0.8686 0.9548 0.8890 0.0538  -0.0103 -0.0528 368 GLU   A C    
2350 O  O    . GLU   A 341 ? 0.8896 0.9715 0.8894 0.0508  -0.0138 -0.0560 368 GLU   A O    
2351 C  CB   . GLU   A 341 ? 0.8641 0.9912 0.8821 0.0649  0.0094  -0.0534 368 GLU   A CB   
2352 C  CG   . GLU   A 341 ? 0.8646 1.0058 0.8817 0.0737  0.0173  -0.0643 368 GLU   A CG   
2353 C  CD   . GLU   A 341 ? 0.9431 1.0676 0.9434 0.0771  0.0112  -0.0863 368 GLU   A CD   
2354 O  OE1  . GLU   A 341 ? 0.9885 1.1122 0.9680 0.0744  0.0082  -0.0953 368 GLU   A OE1  
2355 O  OE2  . GLU   A 341 ? 0.9863 1.0993 0.9975 0.0831  0.0103  -0.0954 368 GLU   A OE2  
2356 N  N    . GLU   A 342 ? 0.8178 0.9016 0.8620 0.0501  -0.0120 -0.0444 369 GLU   A N    
2357 C  CA   . GLU   A 342 ? 0.8058 0.8773 0.8493 0.0433  -0.0187 -0.0380 369 GLU   A CA   
2358 C  C    . GLU   A 342 ? 0.8460 0.8934 0.8766 0.0439  -0.0302 -0.0488 369 GLU   A C    
2359 O  O    . GLU   A 342 ? 0.7833 0.8194 0.7990 0.0392  -0.0344 -0.0479 369 GLU   A O    
2360 C  CB   . GLU   A 342 ? 0.7684 0.8451 0.8460 0.0390  -0.0156 -0.0296 369 GLU   A CB   
2361 C  CG   . GLU   A 342 ? 0.7425 0.8365 0.8342 0.0374  0.0001  -0.0115 369 GLU   A CG   
2362 C  CD   . GLU   A 342 ? 0.8883 0.9857 1.0252 0.0321  0.0076  -0.0071 369 GLU   A CD   
2363 O  OE1  . GLU   A 342 ? 0.7074 0.7994 0.8636 0.0300  -0.0024 -0.0222 369 GLU   A OE1  
2364 O  OE2  . GLU   A 342 ? 0.9840 1.0911 1.1389 0.0310  0.0246  0.0109  369 GLU   A OE2  
2365 N  N    . ILE   A 343 ? 0.8563 0.8973 0.8929 0.0513  -0.0342 -0.0576 370 ILE   A N    
2366 C  CA   . ILE   A 343 ? 0.7348 0.7523 0.7560 0.0563  -0.0411 -0.0638 370 ILE   A CA   
2367 C  C    . ILE   A 343 ? 0.7995 0.8033 0.7991 0.0553  -0.0365 -0.0699 370 ILE   A C    
2368 O  O    . ILE   A 343 ? 0.8381 0.8208 0.8256 0.0531  -0.0382 -0.0714 370 ILE   A O    
2369 C  CB   . ILE   A 343 ? 0.7032 0.7222 0.7340 0.0694  -0.0450 -0.0698 370 ILE   A CB   
2370 C  CG1  . ILE   A 343 ? 0.7919 0.8290 0.8492 0.0691  -0.0513 -0.0705 370 ILE   A CG1  
2371 C  CG2  . ILE   A 343 ? 0.7039 0.6973 0.7155 0.0791  -0.0481 -0.0711 370 ILE   A CG2  
2372 C  CD1  . ILE   A 343 ? 0.7354 0.7876 0.8077 0.0830  -0.0563 -0.0798 370 ILE   A CD1  
2373 N  N    . HIS   A 344 ? 0.9003 0.9176 0.8977 0.0567  -0.0295 -0.0753 371 HIS   A N    
2374 C  CA   . HIS   A 344 ? 0.8815 0.8921 0.8635 0.0545  -0.0251 -0.0873 371 HIS   A CA   
2375 C  C    . HIS   A 344 ? 0.8234 0.8362 0.7960 0.0440  -0.0278 -0.0864 371 HIS   A C    
2376 O  O    . HIS   A 344 ? 0.9328 0.9285 0.8989 0.0396  -0.0273 -0.0967 371 HIS   A O    
2377 C  CB   . HIS   A 344 ? 0.8424 0.8763 0.8236 0.0586  -0.0178 -0.0944 371 HIS   A CB   
2378 C  CG   . HIS   A 344 ? 0.8922 0.9235 0.8620 0.0577  -0.0133 -0.1136 371 HIS   A CG   
2379 N  ND1  . HIS   A 344 ? 0.9031 0.9562 0.8697 0.0629  -0.0067 -0.1250 371 HIS   A ND1  
2380 C  CD2  . HIS   A 344 ? 0.9501 0.9616 0.9151 0.0517  -0.0134 -0.1264 371 HIS   A CD2  
2381 C  CE1  . HIS   A 344 ? 0.8783 0.9262 0.8388 0.0601  -0.0042 -0.1466 371 HIS   A CE1  
2382 N  NE2  . HIS   A 344 ? 0.9673 0.9893 0.9292 0.0524  -0.0076 -0.1480 371 HIS   A NE2  
2383 N  N    . ASN   A 345 ? 0.7513 0.7852 0.7265 0.0404  -0.0291 -0.0740 372 ASN   A N    
2384 C  CA   . ASN   A 345 ? 0.7359 0.7764 0.7030 0.0332  -0.0324 -0.0718 372 ASN   A CA   
2385 C  C    . ASN   A 345 ? 0.7359 0.7519 0.7056 0.0280  -0.0382 -0.0685 372 ASN   A C    
2386 O  O    . ASN   A 345 ? 0.9559 0.9684 0.9194 0.0217  -0.0403 -0.0742 372 ASN   A O    
2387 C  CB   . ASN   A 345 ? 0.6953 0.7629 0.6652 0.0345  -0.0298 -0.0549 372 ASN   A CB   
2388 C  CG   . ASN   A 345 ? 0.8730 0.9708 0.8334 0.0413  -0.0225 -0.0566 372 ASN   A CG   
2389 O  OD1  . ASN   A 345 ? 0.8546 0.9558 0.8057 0.0435  -0.0214 -0.0751 372 ASN   A OD1  
2390 N  ND2  . ASN   A 345 ? 0.8221 0.9422 0.7858 0.0459  -0.0157 -0.0371 372 ASN   A ND2  
2391 N  N    . GLU   A 346 ? 0.7222 0.7252 0.7022 0.0314  -0.0409 -0.0613 373 GLU   A N    
2392 C  CA   . GLU   A 346 ? 0.8690 0.8538 0.8493 0.0289  -0.0460 -0.0575 373 GLU   A CA   
2393 C  C    . GLU   A 346 ? 0.8717 0.8309 0.8417 0.0291  -0.0435 -0.0659 373 GLU   A C    
2394 O  O    . GLU   A 346 ? 0.8092 0.7587 0.7755 0.0226  -0.0439 -0.0660 373 GLU   A O    
2395 C  CB   . GLU   A 346 ? 0.7536 0.7379 0.7476 0.0348  -0.0503 -0.0524 373 GLU   A CB   
2396 C  CG   . GLU   A 346 ? 0.7419 0.7188 0.7386 0.0322  -0.0560 -0.0479 373 GLU   A CG   
2397 C  CD   . GLU   A 346 ? 0.9294 0.9114 0.9406 0.0395  -0.0618 -0.0496 373 GLU   A CD   
2398 O  OE1  . GLU   A 346 ? 0.7558 0.7510 0.7807 0.0443  -0.0612 -0.0531 373 GLU   A OE1  
2399 O  OE2  . GLU   A 346 ? 0.8229 0.7993 0.8330 0.0408  -0.0670 -0.0496 373 GLU   A OE2  
2400 N  N    . VAL   A 347 ? 0.7029 0.6500 0.6710 0.0370  -0.0388 -0.0722 374 VAL   A N    
2401 C  CA   . VAL   A 347 ? 0.7873 0.7047 0.7500 0.0388  -0.0318 -0.0771 374 VAL   A CA   
2402 C  C    . VAL   A 347 ? 0.7974 0.7146 0.7609 0.0269  -0.0262 -0.0915 374 VAL   A C    
2403 O  O    . VAL   A 347 ? 0.7473 0.6445 0.7126 0.0210  -0.0207 -0.0946 374 VAL   A O    
2404 C  CB   . VAL   A 347 ? 0.8836 0.7874 0.8464 0.0529  -0.0264 -0.0785 374 VAL   A CB   
2405 C  CG1  . VAL   A 347 ? 1.0401 0.9648 1.0077 0.0542  -0.0253 -0.0874 374 VAL   A CG1  
2406 C  CG2  . VAL   A 347 ? 0.8340 0.7036 0.7955 0.0550  -0.0138 -0.0825 374 VAL   A CG2  
2407 N  N    . GLU   A 348 ? 0.7776 0.7206 0.7414 0.0238  -0.0271 -0.1019 375 GLU   A N    
2408 C  CA   . GLU   A 348 ? 0.8545 0.8068 0.8206 0.0142  -0.0238 -0.1217 375 GLU   A CA   
2409 C  C    . GLU   A 348 ? 0.8418 0.8046 0.8085 0.0042  -0.0291 -0.1203 375 GLU   A C    
2410 O  O    . GLU   A 348 ? 0.8327 0.7843 0.8077 -0.0047 -0.0244 -0.1334 375 GLU   A O    
2411 C  CB   . GLU   A 348 ? 0.9169 0.9034 0.8787 0.0169  -0.0249 -0.1324 375 GLU   A CB   
2412 C  CG   . GLU   A 348 ? 0.9030 0.9116 0.8665 0.0088  -0.0247 -0.1573 375 GLU   A CG   
2413 C  CD   . GLU   A 348 ? 0.9204 0.9648 0.8765 0.0149  -0.0246 -0.1710 375 GLU   A CD   
2414 O  OE1  . GLU   A 348 ? 0.9488 0.9961 0.9003 0.0244  -0.0223 -0.1602 375 GLU   A OE1  
2415 O  OE2  . GLU   A 348 ? 0.9416 1.0151 0.8972 0.0109  -0.0267 -0.1940 375 GLU   A OE2  
2416 N  N    . PHE   A 349 ? 0.7965 0.7806 0.7582 0.0056  -0.0371 -0.1047 376 PHE   A N    
2417 C  CA   . PHE   A 349 ? 0.7958 0.7979 0.7577 -0.0012 -0.0426 -0.1033 376 PHE   A CA   
2418 C  C    . PHE   A 349 ? 0.8682 0.8490 0.8338 -0.0042 -0.0441 -0.0907 376 PHE   A C    
2419 O  O    . PHE   A 349 ? 0.9895 0.9715 0.9597 -0.0122 -0.0444 -0.0966 376 PHE   A O    
2420 C  CB   . PHE   A 349 ? 0.8033 0.8411 0.7591 0.0044  -0.0476 -0.0915 376 PHE   A CB   
2421 C  CG   . PHE   A 349 ? 0.9273 0.9937 0.8755 0.0096  -0.0457 -0.1030 376 PHE   A CG   
2422 C  CD1  . PHE   A 349 ? 0.8513 0.9328 0.7990 0.0054  -0.0457 -0.1293 376 PHE   A CD1  
2423 C  CD2  . PHE   A 349 ? 0.9500 1.0301 0.8943 0.0188  -0.0427 -0.0897 376 PHE   A CD2  
2424 C  CE1  . PHE   A 349 ? 0.8323 0.9449 0.7716 0.0118  -0.0444 -0.1432 376 PHE   A CE1  
2425 C  CE2  . PHE   A 349 ? 0.9789 1.0877 0.9137 0.0254  -0.0396 -0.0996 376 PHE   A CE2  
2426 C  CZ   . PHE   A 349 ? 0.8680 0.9943 0.7983 0.0227  -0.0413 -0.1268 376 PHE   A CZ   
2427 N  N    . GLU   A 350 ? 0.8206 0.7859 0.7856 0.0024  -0.0452 -0.0757 377 GLU   A N    
2428 C  CA   . GLU   A 350 ? 0.7855 0.7349 0.7520 0.0016  -0.0469 -0.0659 377 GLU   A CA   
2429 C  C    . GLU   A 350 ? 0.7974 0.7154 0.7622 0.0020  -0.0387 -0.0691 377 GLU   A C    
2430 O  O    . GLU   A 350 ? 0.9341 0.8407 0.8983 0.0011  -0.0378 -0.0623 377 GLU   A O    
2431 C  CB   . GLU   A 350 ? 0.8207 0.7718 0.7901 0.0094  -0.0519 -0.0534 377 GLU   A CB   
2432 C  CG   . GLU   A 350 ? 0.8888 0.8645 0.8662 0.0083  -0.0557 -0.0452 377 GLU   A CG   
2433 C  CD   . GLU   A 350 ? 1.0895 1.0761 1.0682 0.0023  -0.0578 -0.0420 377 GLU   A CD   
2434 O  OE1  . GLU   A 350 ? 0.7897 0.7634 0.7684 -0.0009 -0.0588 -0.0422 377 GLU   A OE1  
2435 O  OE2  . GLU   A 350 ? 1.0000 1.0104 0.9788 0.0026  -0.0579 -0.0382 377 GLU   A OE2  
2436 N  N    . TRP   A 351 ? 0.8029 0.7060 0.7681 0.0044  -0.0305 -0.0779 378 TRP   A N    
2437 C  CA   . TRP   A 351 ? 0.8795 0.7484 0.8449 0.0078  -0.0184 -0.0760 378 TRP   A CA   
2438 C  C    . TRP   A 351 ? 0.9129 0.7695 0.8911 -0.0014 -0.0060 -0.0944 378 TRP   A C    
2439 O  O    . TRP   A 351 ? 0.9991 0.8407 0.9878 -0.0102 0.0037  -0.0985 378 TRP   A O    
2440 C  CB   . TRP   A 351 ? 0.8032 0.6581 0.7601 0.0250  -0.0172 -0.0653 378 TRP   A CB   
2441 C  CG   . TRP   A 351 ? 0.7605 0.6269 0.7101 0.0338  -0.0280 -0.0524 378 TRP   A CG   
2442 C  CD1  . TRP   A 351 ? 0.7634 0.6562 0.7169 0.0340  -0.0397 -0.0517 378 TRP   A CD1  
2443 C  CD2  . TRP   A 351 ? 0.7706 0.6244 0.7109 0.0436  -0.0267 -0.0403 378 TRP   A CD2  
2444 N  NE1  . TRP   A 351 ? 0.7835 0.6811 0.7348 0.0417  -0.0467 -0.0441 378 TRP   A NE1  
2445 C  CE2  . TRP   A 351 ? 0.8105 0.6870 0.7508 0.0488  -0.0402 -0.0374 378 TRP   A CE2  
2446 C  CE3  . TRP   A 351 ? 0.8821 0.7087 0.8154 0.0494  -0.0137 -0.0316 378 TRP   A CE3  
2447 C  CZ2  . TRP   A 351 ? 0.7804 0.6577 0.7119 0.0601  -0.0438 -0.0300 378 TRP   A CZ2  
2448 C  CZ3  . TRP   A 351 ? 0.9103 0.7370 0.8305 0.0625  -0.0159 -0.0194 378 TRP   A CZ3  
2449 C  CH2  . TRP   A 351 ? 0.9135 0.7676 0.8318 0.0679  -0.0323 -0.0205 378 TRP   A CH2  
2450 N  N    . LEU   A 352 ? 0.8280 0.6922 0.8092 -0.0001 -0.0050 -0.1077 379 LEU   A N    
2451 C  CA   . LEU   A 352 ? 0.9001 0.7515 0.8982 -0.0081 0.0080  -0.1298 379 LEU   A CA   
2452 C  C    . LEU   A 352 ? 0.9261 0.8005 0.9381 -0.0249 0.0058  -0.1502 379 LEU   A C    
2453 O  O    . LEU   A 352 ? 0.8576 0.7132 0.8884 -0.0351 0.0180  -0.1593 379 LEU   A O    
2454 C  CB   . LEU   A 352 ? 0.8959 0.7569 0.8935 -0.0020 0.0080  -0.1424 379 LEU   A CB   
2455 C  CG   . LEU   A 352 ? 0.9359 0.7669 0.9296 0.0141  0.0166  -0.1302 379 LEU   A CG   
2456 C  CD1  . LEU   A 352 ? 0.9219 0.7657 0.9176 0.0192  0.0170  -0.1454 379 LEU   A CD1  
2457 C  CD2  . LEU   A 352 ? 0.8479 0.6337 0.8544 0.0151  0.0366  -0.1272 379 LEU   A CD2  
2458 N  N    . ARG   A 353 ? 0.8864 0.8041 0.8911 -0.0267 -0.0087 -0.1571 380 ARG   A N    
2459 C  CA   . ARG   A 353 ? 0.9114 0.8606 0.9279 -0.0390 -0.0132 -0.1781 380 ARG   A CA   
2460 C  C    . ARG   A 353 ? 0.9961 0.9412 1.0173 -0.0456 -0.0143 -0.1672 380 ARG   A C    
2461 O  O    . ARG   A 353 ? 0.9173 0.8742 0.9580 -0.0579 -0.0117 -0.1867 380 ARG   A O    
2462 C  CB   . ARG   A 353 ? 0.8290 0.8283 0.8313 -0.0337 -0.0275 -0.1823 380 ARG   A CB   
2463 C  CG   . ARG   A 353 ? 0.8742 0.8819 0.8700 -0.0259 -0.0259 -0.1922 380 ARG   A CG   
2464 C  CD   . ARG   A 353 ? 0.8571 0.9204 0.8425 -0.0217 -0.0360 -0.2052 380 ARG   A CD   
2465 N  NE   . ARG   A 353 ? 0.9537 1.0266 0.9347 -0.0150 -0.0323 -0.2199 380 ARG   A NE   
2466 C  CZ   . ARG   A 353 ? 1.1169 1.1845 1.1147 -0.0208 -0.0246 -0.2526 380 ARG   A CZ   
2467 N  NH1  . ARG   A 353 ? 1.1699 1.2228 1.1933 -0.0348 -0.0183 -0.2750 380 ARG   A NH1  
2468 N  NH2  . ARG   A 353 ? 1.0438 1.1207 1.0361 -0.0128 -0.0212 -0.2642 380 ARG   A NH2  
2469 N  N    . GLN   A 354 ? 0.8829 0.8144 0.8894 -0.0376 -0.0181 -0.1391 381 GLN   A N    
2470 C  CA   . GLN   A 354 ? 0.8018 0.7270 0.8125 -0.0425 -0.0175 -0.1289 381 GLN   A CA   
2471 C  C    . GLN   A 354 ? 0.9549 0.8430 0.9821 -0.0492 0.0010  -0.1328 381 GLN   A C    
2472 O  O    . GLN   A 354 ? 1.0455 0.9365 1.0890 -0.0601 0.0059  -0.1399 381 GLN   A O    
2473 C  CB   . GLN   A 354 ? 0.8014 0.7208 0.7947 -0.0315 -0.0247 -0.1021 381 GLN   A CB   
2474 C  CG   . GLN   A 354 ? 0.7425 0.6968 0.7285 -0.0281 -0.0391 -0.0950 381 GLN   A CG   
2475 C  CD   . GLN   A 354 ? 0.8310 0.8039 0.8238 -0.0341 -0.0438 -0.0944 381 GLN   A CD   
2476 O  OE1  . GLN   A 354 ? 0.8527 0.8146 0.8567 -0.0423 -0.0369 -0.1010 381 GLN   A OE1  
2477 N  NE2  . GLN   A 354 ? 0.8388 0.8395 0.8270 -0.0291 -0.0537 -0.0851 381 GLN   A NE2  
2478 N  N    . PHE   A 355 ? 1.0168 0.8700 1.0420 -0.0417 0.0135  -0.1268 382 PHE   A N    
2479 C  CA   . PHE   A 355 ? 0.8862 0.6989 0.9270 -0.0446 0.0359  -0.1243 382 PHE   A CA   
2480 C  C    . PHE   A 355 ? 0.9046 0.7185 0.9802 -0.0626 0.0480  -0.1556 382 PHE   A C    
2481 O  O    . PHE   A 355 ? 1.0395 0.8447 1.1374 -0.0745 0.0603  -0.1610 382 PHE   A O    
2482 C  CB   . PHE   A 355 ? 0.9608 0.7385 0.9901 -0.0280 0.0465  -0.1082 382 PHE   A CB   
2483 C  CG   . PHE   A 355 ? 0.9412 0.6734 0.9836 -0.0258 0.0732  -0.0981 382 PHE   A CG   
2484 C  CD1  . PHE   A 355 ? 0.8823 0.5971 0.9090 -0.0144 0.0796  -0.0706 382 PHE   A CD1  
2485 C  CD2  . PHE   A 355 ? 0.9693 0.6765 1.0410 -0.0338 0.0938  -0.1158 382 PHE   A CD2  
2486 C  CE1  . PHE   A 355 ? 1.0864 0.7593 1.1232 -0.0093 0.1076  -0.0563 382 PHE   A CE1  
2487 C  CE2  . PHE   A 355 ? 1.0052 0.6662 1.0927 -0.0308 0.1230  -0.1028 382 PHE   A CE2  
2488 C  CZ   . PHE   A 355 ? 0.8935 0.5371 0.9618 -0.0176 0.1306  -0.0706 382 PHE   A CZ   
2489 N  N    . TRP   A 356 ? 0.9170 0.7443 1.0006 -0.0650 0.0455  -0.1792 383 TRP   A N    
2490 C  CA   . TRP   A 356 ? 1.0028 0.8334 1.1242 -0.0818 0.0573  -0.2156 383 TRP   A CA   
2491 C  C    . TRP   A 356 ? 0.9664 0.8476 1.1016 -0.0956 0.0435  -0.2407 383 TRP   A C    
2492 O  O    . TRP   A 356 ? 1.0685 0.9577 1.2414 -0.1118 0.0531  -0.2745 383 TRP   A O    
2493 C  CB   . TRP   A 356 ? 1.1009 0.9325 1.2258 -0.0779 0.0588  -0.2356 383 TRP   A CB   
2494 C  CG   . TRP   A 356 ? 1.1570 0.9369 1.2779 -0.0647 0.0766  -0.2158 383 TRP   A CG   
2495 C  CD1  . TRP   A 356 ? 1.0801 0.8560 1.1740 -0.0466 0.0695  -0.1989 383 TRP   A CD1  
2496 C  CD2  . TRP   A 356 ? 1.1722 0.8986 1.3184 -0.0664 0.1059  -0.2093 383 TRP   A CD2  
2497 N  NE1  . TRP   A 356 ? 1.1063 0.8326 1.2050 -0.0353 0.0904  -0.1829 383 TRP   A NE1  
2498 C  CE2  . TRP   A 356 ? 1.1375 0.8308 1.2669 -0.0462 0.1141  -0.1869 383 TRP   A CE2  
2499 C  CE3  . TRP   A 356 ? 1.1679 0.8719 1.3518 -0.0823 0.1280  -0.2193 383 TRP   A CE3  
2500 C  CZ2  . TRP   A 356 ? 1.3361 0.9739 1.4814 -0.0387 0.1437  -0.1710 383 TRP   A CZ2  
2501 C  CZ3  . TRP   A 356 ? 1.2621 0.9078 1.4645 -0.0770 0.1598  -0.2034 383 TRP   A CZ3  
2502 C  CH2  . TRP   A 356 ? 1.3674 0.9801 1.5487 -0.0540 0.1675  -0.1780 383 TRP   A CH2  
2503 N  N    . PHE   A 357 ? 1.0055 0.9225 1.1144 -0.0889 0.0222  -0.2263 384 PHE   A N    
2504 C  CA   . PHE   A 357 ? 1.0972 1.0618 1.2177 -0.0982 0.0099  -0.2443 384 PHE   A CA   
2505 C  C    . PHE   A 357 ? 1.1198 1.0681 1.2684 -0.1116 0.0236  -0.2461 384 PHE   A C    
2506 O  O    . PHE   A 357 ? 1.0970 1.0816 1.2712 -0.1238 0.0195  -0.2728 384 PHE   A O    
2507 C  CB   . PHE   A 357 ? 0.9656 0.9631 1.0532 -0.0855 -0.0114 -0.2213 384 PHE   A CB   
2508 C  CG   . PHE   A 357 ? 0.9095 0.9610 1.0047 -0.0895 -0.0255 -0.2367 384 PHE   A CG   
2509 C  CD1  . PHE   A 357 ? 1.0272 1.1302 1.1250 -0.0884 -0.0368 -0.2653 384 PHE   A CD1  
2510 C  CD2  . PHE   A 357 ? 0.8972 0.9520 0.9958 -0.0918 -0.0277 -0.2227 384 PHE   A CD2  
2511 C  CE1  . PHE   A 357 ? 1.0174 1.1762 1.1203 -0.0880 -0.0508 -0.2786 384 PHE   A CE1  
2512 C  CE2  . PHE   A 357 ? 0.9003 1.0073 1.0066 -0.0929 -0.0408 -0.2359 384 PHE   A CE2  
2513 C  CZ   . PHE   A 357 ? 1.0317 1.1919 1.1397 -0.0902 -0.0528 -0.2632 384 PHE   A CZ   
2514 N  N    . GLN   A 358 ? 1.0462 0.9443 1.1906 -0.1081 0.0402  -0.2184 385 GLN   A N    
2515 C  CA   . GLN   A 358 ? 1.1784 1.0575 1.3496 -0.1197 0.0579  -0.2171 385 GLN   A CA   
2516 C  C    . GLN   A 358 ? 1.2871 1.1418 1.5053 -0.1359 0.0835  -0.2447 385 GLN   A C    
2517 O  O    . GLN   A 358 ? 1.3851 1.2447 1.6410 -0.1523 0.0957  -0.2614 385 GLN   A O    
2518 C  CB   . GLN   A 358 ? 1.1874 1.0271 1.3331 -0.1063 0.0668  -0.1759 385 GLN   A CB   
2519 C  CG   . GLN   A 358 ? 1.2120 1.0783 1.3323 -0.0989 0.0475  -0.1572 385 GLN   A CG   
2520 C  CD   . GLN   A 358 ? 1.1631 1.0078 1.2457 -0.0793 0.0432  -0.1232 385 GLN   A CD   
2521 O  OE1  . GLN   A 358 ? 0.9966 0.8649 1.0560 -0.0703 0.0229  -0.1143 385 GLN   A OE1  
2522 N  NE2  . GLN   A 358 ? 1.2958 1.0975 1.3742 -0.0716 0.0633  -0.1046 385 GLN   A NE2  
2523 N  N    . GLY   A 359 ? 1.3157 1.1445 1.5368 -0.1320 0.0934  -0.2512 386 GLY   A N    
2524 C  CA   . GLY   A 359 ? 1.2850 1.0956 1.5565 -0.1483 0.1165  -0.2849 386 GLY   A CA   
2525 C  C    . GLY   A 359 ? 1.5160 1.2605 1.8108 -0.1495 0.1534  -0.2655 386 GLY   A C    
2526 O  O    . GLY   A 359 ? 1.4894 1.2215 1.8358 -0.1686 0.1767  -0.2868 386 GLY   A O    
2527 N  N    . ASN   A 360 ? 1.7548 1.4587 2.0139 -0.1281 0.1602  -0.2252 387 ASN   A N    
2528 C  CA   . ASN   A 360 ? 1.8603 1.5005 2.1329 -0.1216 0.1965  -0.1990 387 ASN   A CA   
2529 C  C    . ASN   A 360 ? 1.9181 1.5454 2.2112 -0.1311 0.2162  -0.1862 387 ASN   A C    
2530 O  O    . ASN   A 360 ? 1.9502 1.5293 2.2753 -0.1342 0.2533  -0.1762 387 ASN   A O    
2531 C  CB   . ASN   A 360 ? 1.6233 1.2309 1.9421 -0.1308 0.2226  -0.2254 387 ASN   A CB   
2532 N  N    . ARG   A 361 ? 1.7176 1.3869 1.9945 -0.1349 0.1938  -0.1852 388 ARG   A N    
2533 C  CA   . ARG   A 361 ? 1.5301 1.1900 1.8211 -0.1411 0.2111  -0.1700 388 ARG   A CA   
2534 C  C    . ARG   A 361 ? 1.6178 1.2428 1.8658 -0.1159 0.2218  -0.1189 388 ARG   A C    
2535 O  O    . ARG   A 361 ? 1.5939 1.1925 1.8551 -0.1163 0.2492  -0.0992 388 ARG   A O    
2536 C  CB   . ARG   A 361 ? 1.5120 1.2302 1.8017 -0.1519 0.1838  -0.1871 388 ARG   A CB   
2537 C  CG   . ARG   A 361 ? 1.4100 1.1703 1.6537 -0.1393 0.1443  -0.1854 388 ARG   A CG   
2538 C  CD   . ARG   A 361 ? 1.2483 1.0543 1.4837 -0.1426 0.1231  -0.1865 388 ARG   A CD   
2539 N  NE   . ARG   A 361 ? 1.4208 1.2189 1.6108 -0.1233 0.1143  -0.1483 388 ARG   A NE   
2540 C  CZ   . ARG   A 361 ? 1.4118 1.2473 1.5785 -0.1176 0.0885  -0.1432 388 ARG   A CZ   
2541 N  NH1  . ARG   A 361 ? 1.3046 1.1888 1.4841 -0.1268 0.0689  -0.1688 388 ARG   A NH1  
2542 N  NH2  . ARG   A 361 ? 1.1906 1.0160 1.3213 -0.1007 0.0831  -0.1123 388 ARG   A NH2  
2543 N  N    . TYR   A 362 ? 1.6613 1.2895 1.8591 -0.0930 0.2010  -0.0983 389 TYR   A N    
2544 C  CA   . TYR   A 362 ? 1.7017 1.3012 1.8593 -0.0659 0.2105  -0.0540 389 TYR   A CA   
2545 C  C    . TYR   A 362 ? 1.7701 1.3118 1.9451 -0.0566 0.2504  -0.0351 389 TYR   A C    
2546 O  O    . TYR   A 362 ? 1.7720 1.2866 1.9255 -0.0363 0.2701  0.0026  389 TYR   A O    
2547 C  CB   . TYR   A 362 ? 1.5219 1.1416 1.6310 -0.0451 0.1796  -0.0430 389 TYR   A CB   
2548 N  N    . ARG   A 363 ? 1.7883 1.3115 2.0028 -0.0696 0.2643  -0.0606 390 ARG   A N    
2549 C  CA   . ARG   A 363 ? 1.7702 1.2341 2.0119 -0.0631 0.3068  -0.0452 390 ARG   A CA   
2550 C  C    . ARG   A 363 ? 1.7220 1.1573 2.0047 -0.0761 0.3455  -0.0371 390 ARG   A C    
2551 O  O    . ARG   A 363 ? 1.6834 1.0644 1.9909 -0.0692 0.3871  -0.0178 390 ARG   A O    
2552 C  CB   . ARG   A 363 ? 1.6976 1.1524 1.9786 -0.0771 0.3112  -0.0822 390 ARG   A CB   
2553 N  N    . LYS   A 364 ? 1.7158 1.1855 2.0089 -0.0940 0.3353  -0.0502 391 LYS   A N    
2554 C  CA   . LYS   A 364 ? 1.8042 1.2502 2.1337 -0.1048 0.3725  -0.0390 391 LYS   A CA   
2555 C  C    . LYS   A 364 ? 1.8662 1.2958 2.1467 -0.0753 0.3842  0.0145  391 LYS   A C    
2556 O  O    . LYS   A 364 ? 1.9669 1.3560 2.2682 -0.0714 0.4274  0.0408  391 LYS   A O    
2557 C  CB   . LYS   A 364 ? 1.7473 1.2412 2.1117 -0.1352 0.3572  -0.0771 391 LYS   A CB   
2558 C  CG   . LYS   A 364 ? 1.8172 1.2910 2.2305 -0.1511 0.3967  -0.0726 391 LYS   A CG   
2559 C  CD   . LYS   A 364 ? 1.5365 1.0664 1.9697 -0.1736 0.3753  -0.1025 391 LYS   A CD   
2560 C  CE   . LYS   A 364 ? 1.4695 1.0191 1.9800 -0.2090 0.3813  -0.1594 391 LYS   A CE   
2561 N  NZ   . LYS   A 364 ? 1.5387 1.1109 2.0485 -0.2131 0.3532  -0.1954 391 LYS   A NZ   
2562 N  N    . CYS   A 365 ? 1.7751 1.2366 1.9927 -0.0538 0.3482  0.0303  392 CYS   A N    
2563 C  CA   . CYS   A 365 ? 1.7890 1.2472 1.9566 -0.0244 0.3530  0.0745  392 CYS   A CA   
2564 C  C    . CYS   A 365 ? 1.8174 1.2503 1.9398 0.0131  0.3576  0.1103  392 CYS   A C    
2565 O  O    . CYS   A 365 ? 1.8967 1.3041 1.9964 0.0392  0.3850  0.1516  392 CYS   A O    
2566 C  CB   . CYS   A 365 ? 1.6663 1.1797 1.7981 -0.0242 0.3113  0.0662  392 CYS   A CB   
2567 S  SG   . CYS   A 365 ? 1.7852 1.3450 1.9611 -0.0640 0.2873  0.0151  392 CYS   A SG   
2568 N  N    . THR   A 366 ? 1.6294 1.0723 1.7377 0.0184  0.3320  0.0961  393 THR   A N    
2569 C  CA   . THR   A 366 ? 1.6513 1.0772 1.7184 0.0549  0.3329  0.1269  393 THR   A CA   
2570 C  C    . THR   A 366 ? 1.5831 1.0060 1.6638 0.0495  0.3194  0.1023  393 THR   A C    
2571 O  O    . THR   A 366 ? 1.6289 1.0763 1.7355 0.0213  0.2988  0.0620  393 THR   A O    
2572 C  CB   . THR   A 366 ? 1.4906 0.9568 1.4965 0.0811  0.3008  0.1442  393 THR   A CB   
2573 O  OG1  . THR   A 366 ? 1.5803 1.0299 1.5481 0.1213  0.3100  0.1798  393 THR   A OG1  
2574 C  CG2  . THR   A 366 ? 1.3992 0.9121 1.3951 0.0685  0.2541  0.1114  393 THR   A CG2  
2575 N  N    . ASP   A 367 ? 1.5961 0.9911 1.6577 0.0792  0.3320  0.1280  394 ASP   A N    
2576 C  CA   . ASP   A 367 ? 1.5130 0.9067 1.5793 0.0812  0.3185  0.1099  394 ASP   A CA   
2577 C  C    . ASP   A 367 ? 1.4572 0.8853 1.4693 0.1100  0.2841  0.1219  394 ASP   A C    
2578 O  O    . ASP   A 367 ? 1.4131 0.8348 1.4203 0.1240  0.2793  0.1208  394 ASP   A O    
2579 C  CB   . ASP   A 367 ? 1.5685 0.9023 1.6651 0.0916  0.3613  0.1250  394 ASP   A CB   
2580 C  CG   . ASP   A 367 ? 1.7141 1.0135 1.7854 0.1280  0.3946  0.1790  394 ASP   A CG   
2581 O  OD1  . ASP   A 367 ? 1.7731 1.1021 1.7935 0.1514  0.3778  0.2035  394 ASP   A OD1  
2582 O  OD2  . ASP   A 367 ? 1.7248 0.9771 1.8273 0.1333  0.4359  0.1949  394 ASP   A OD2  
2583 N  N    . TRP   A 368 ? 1.3144 0.7807 1.2898 0.1183  0.2606  0.1308  395 TRP   A N    
2584 C  CA   . TRP   A 368 ? 1.2612 0.7624 1.1901 0.1462  0.2303  0.1408  395 TRP   A CA   
2585 C  C    . TRP   A 368 ? 1.2048 0.7344 1.1393 0.1335  0.1985  0.1092  395 TRP   A C    
2586 O  O    . TRP   A 368 ? 1.2174 0.7596 1.1298 0.1566  0.1844  0.1153  395 TRP   A O    
2587 C  CB   . TRP   A 368 ? 1.1167 0.6552 1.0150 0.1517  0.2118  0.1477  395 TRP   A CB   
2588 C  CG   . TRP   A 368 ? 1.0645 0.6362 0.9172 0.1859  0.1888  0.1619  395 TRP   A CG   
2589 C  CD1  . TRP   A 368 ? 1.1983 0.7688 1.0152 0.2243  0.2009  0.1962  395 TRP   A CD1  
2590 C  CD2  . TRP   A 368 ? 1.0683 0.6836 0.9090 0.1857  0.1502  0.1403  395 TRP   A CD2  
2591 N  NE1  . TRP   A 368 ? 1.0897 0.7045 0.8741 0.2476  0.1697  0.1931  395 TRP   A NE1  
2592 C  CE2  . TRP   A 368 ? 1.0017 0.6424 0.8032 0.2230  0.1395  0.1588  395 TRP   A CE2  
2593 C  CE3  . TRP   A 368 ? 0.9864 0.6238 0.8469 0.1589  0.1253  0.1077  395 TRP   A CE3  
2594 C  CZ2  . TRP   A 368 ? 0.9002 0.5862 0.6883 0.2308  0.1051  0.1421  395 TRP   A CZ2  
2595 C  CZ3  . TRP   A 368 ? 0.9928 0.6706 0.8379 0.1677  0.0941  0.0962  395 TRP   A CZ3  
2596 C  CH2  . TRP   A 368 ? 0.9129 0.6140 0.7253 0.2017  0.0843  0.1117  395 TRP   A CH2  
2597 N  N    . TRP   A 369 ? 1.1657 0.7089 1.1296 0.0988  0.1875  0.0757  396 TRP   A N    
2598 C  CA   . TRP   A 369 ? 1.0963 0.6712 1.0633 0.0867  0.1582  0.0473  396 TRP   A CA   
2599 C  C    . TRP   A 369 ? 1.1100 0.6618 1.1056 0.0790  0.1704  0.0297  396 TRP   A C    
2600 O  O    . TRP   A 369 ? 1.1214 0.6988 1.1182 0.0721  0.1490  0.0078  396 TRP   A O    
2601 C  CB   . TRP   A 369 ? 1.0198 0.6289 0.9986 0.0578  0.1382  0.0219  396 TRP   A CB   
2602 C  CG   . TRP   A 369 ? 1.0101 0.6504 0.9613 0.0649  0.1184  0.0323  396 TRP   A CG   
2603 C  CD1  . TRP   A 369 ? 1.1044 0.7441 1.0528 0.0621  0.1267  0.0429  396 TRP   A CD1  
2604 C  CD2  . TRP   A 369 ? 1.0208 0.6981 0.9479 0.0754  0.0885  0.0304  396 TRP   A CD2  
2605 N  NE1  . TRP   A 369 ? 0.9743 0.6481 0.8968 0.0709  0.1029  0.0466  396 TRP   A NE1  
2606 C  CE2  . TRP   A 369 ? 1.0174 0.7141 0.9288 0.0783  0.0798  0.0384  396 TRP   A CE2  
2607 C  CE3  . TRP   A 369 ? 0.9799 0.6760 0.9008 0.0820  0.0701  0.0215  396 TRP   A CE3  
2608 C  CZ2  . TRP   A 369 ? 0.9715 0.7042 0.8650 0.0867  0.0536  0.0354  396 TRP   A CZ2  
2609 C  CZ3  . TRP   A 369 ? 0.9785 0.7106 0.8825 0.0897  0.0450  0.0203  396 TRP   A CZ3  
2610 C  CH2  . TRP   A 369 ? 1.1045 0.8538 0.9965 0.0915  0.0371  0.0262  396 TRP   A CH2  
2611 N  N    . CYS   A 370 ? 1.1341 0.6380 1.1547 0.0807  0.2061  0.0386  397 CYS   A N    
2612 C  CA   . CYS   A 370 ? 1.2218 0.7023 1.2769 0.0708  0.2200  0.0164  397 CYS   A CA   
2613 C  C    . CYS   A 370 ? 1.1358 0.6217 1.1707 0.0945  0.2081  0.0216  397 CYS   A C    
2614 O  O    . CYS   A 370 ? 1.1780 0.6833 1.2234 0.0831  0.1928  -0.0070 397 CYS   A O    
2615 C  CB   . CYS   A 370 ? 1.3502 0.7731 1.4406 0.0699  0.2652  0.0281  397 CYS   A CB   
2616 S  SG   . CYS   A 370 ? 1.6559 1.0733 1.7911 0.0332  0.2829  0.0075  397 CYS   A SG   
2617 N  N    . GLN   A 371 ? 1.1663 0.6387 1.1718 0.1293  0.2153  0.0578  398 GLN   A N    
2618 C  CA   . GLN   A 371 ? 1.1840 0.6653 1.1710 0.1550  0.2039  0.0639  398 GLN   A CA   
2619 C  C    . GLN   A 371 ? 1.1435 0.6822 1.1084 0.1513  0.1628  0.0474  398 GLN   A C    
2620 O  O    . GLN   A 371 ? 1.2194 0.7726 1.1898 0.1508  0.1508  0.0298  398 GLN   A O    
2621 C  CB   . GLN   A 371 ? 1.2861 0.7472 1.2450 0.1968  0.2200  0.1071  398 GLN   A CB   
2622 C  CG   . GLN   A 371 ? 1.3465 0.8132 1.2919 0.2269  0.2132  0.1149  398 GLN   A CG   
2623 C  CD   . GLN   A 371 ? 1.4808 1.0068 1.3940 0.2385  0.1735  0.1100  398 GLN   A CD   
2624 O  OE1  . GLN   A 371 ? 1.4598 1.0166 1.3515 0.2370  0.1561  0.1138  398 GLN   A OE1  
2625 N  NE2  . GLN   A 371 ? 1.5137 1.0564 1.4278 0.2492  0.1604  0.0993  398 GLN   A NE2  
2626 N  N    . PRO   A 372 ? 1.0494 0.6210 0.9919 0.1491  0.1427  0.0524  399 PRO   A N    
2627 C  CA   . PRO   A 372 ? 0.9315 0.5537 0.8621 0.1425  0.1077  0.0350  399 PRO   A CA   
2628 C  C    . PRO   A 372 ? 1.0456 0.6826 1.0003 0.1121  0.0982  0.0018  399 PRO   A C    
2629 O  O    . PRO   A 372 ? 1.1129 0.7753 1.0663 0.1128  0.0815  -0.0115 399 PRO   A O    
2630 C  CB   . PRO   A 372 ? 1.1286 0.7738 1.0397 0.1419  0.0952  0.0446  399 PRO   A CB   
2631 C  CG   . PRO   A 372 ? 0.9639 0.5792 0.8612 0.1646  0.1189  0.0753  399 PRO   A CG   
2632 C  CD   . PRO   A 372 ? 1.0221 0.5878 0.9477 0.1575  0.1516  0.0764  399 PRO   A CD   
2633 N  N    . MET   A 373 ? 1.1492 0.7748 1.1263 0.0866  0.1087  -0.0127 400 MET   A N    
2634 C  CA   . MET   A 373 ? 1.1411 0.7879 1.1387 0.0611  0.0989  -0.0456 400 MET   A CA   
2635 C  C    . MET   A 373 ? 1.0131 0.6458 1.0278 0.0633  0.1086  -0.0616 400 MET   A C    
2636 O  O    . MET   A 373 ? 0.9897 0.6513 1.0086 0.0534  0.0941  -0.0848 400 MET   A O    
2637 C  CB   . MET   A 373 ? 1.0405 0.6814 1.0622 0.0357  0.1091  -0.0605 400 MET   A CB   
2638 C  CG   . MET   A 373 ? 1.0503 0.7212 1.0595 0.0266  0.0919  -0.0568 400 MET   A CG   
2639 S  SD   . MET   A 373 ? 1.1030 0.8287 1.0974 0.0211  0.0579  -0.0700 400 MET   A SD   
2640 C  CE   . MET   A 373 ? 0.9335 0.6703 0.8966 0.0422  0.0439  -0.0419 400 MET   A CE   
2641 N  N    . ALA   A 374 ? 1.1417 0.7301 1.1664 0.0779  0.1347  -0.0485 401 ALA   A N    
2642 C  CA   . ALA   A 374 ? 1.1670 0.7394 1.2087 0.0832  0.1452  -0.0626 401 ALA   A CA   
2643 C  C    . ALA   A 374 ? 1.1250 0.7196 1.1422 0.1067  0.1279  -0.0524 401 ALA   A C    
2644 O  O    . ALA   A 374 ? 1.0588 0.6627 1.0856 0.1062  0.1247  -0.0717 401 ALA   A O    
2645 C  CB   . ALA   A 374 ? 1.0543 0.5683 1.1189 0.0927  0.1820  -0.0498 401 ALA   A CB   
2646 N  N    . GLN   A 375 ? 1.0075 0.6146 0.9953 0.1276  0.1166  -0.0250 402 GLN   A N    
2647 C  CA   . GLN   A 375 ? 1.0522 0.6879 1.0220 0.1485  0.0984  -0.0192 402 GLN   A CA   
2648 C  C    . GLN   A 375 ? 1.0881 0.7724 1.0551 0.1314  0.0716  -0.0394 402 GLN   A C    
2649 O  O    . GLN   A 375 ? 0.9712 0.6762 0.9402 0.1365  0.0626  -0.0497 402 GLN   A O    
2650 C  CB   . GLN   A 375 ? 1.0301 0.6707 0.9723 0.1772  0.0940  0.0117  402 GLN   A CB   
2651 C  CG   . GLN   A 375 ? 1.2841 0.9478 1.2143 0.2050  0.0818  0.0182  402 GLN   A CG   
2652 C  CD   . GLN   A 375 ? 1.4461 1.1316 1.3486 0.2323  0.0704  0.0411  402 GLN   A CD   
2653 O  OE1  . GLN   A 375 ? 1.4443 1.1133 1.3332 0.2398  0.0807  0.0606  402 GLN   A OE1  
2654 N  NE2  . GLN   A 375 ? 1.4705 1.1968 1.3662 0.2478  0.0495  0.0368  402 GLN   A NE2  
2655 N  N    . LEU   A 376 ? 0.9701 0.6725 0.9337 0.1124  0.0606  -0.0435 403 LEU   A N    
2656 C  CA   . LEU   A 376 ? 0.8836 0.6287 0.8463 0.0974  0.0391  -0.0589 403 LEU   A CA   
2657 C  C    . LEU   A 376 ? 0.9683 0.7204 0.9479 0.0813  0.0422  -0.0854 403 LEU   A C    
2658 O  O    . LEU   A 376 ? 0.9269 0.7110 0.9050 0.0794  0.0298  -0.0952 403 LEU   A O    
2659 C  CB   . LEU   A 376 ? 0.9418 0.7015 0.8990 0.0828  0.0294  -0.0559 403 LEU   A CB   
2660 C  CG   . LEU   A 376 ? 0.9045 0.6733 0.8437 0.0977  0.0199  -0.0357 403 LEU   A CG   
2661 C  CD1  . LEU   A 376 ? 0.8490 0.6233 0.7862 0.0828  0.0159  -0.0338 403 LEU   A CD1  
2662 C  CD2  . LEU   A 376 ? 0.9040 0.7087 0.8389 0.1065  0.0010  -0.0372 403 LEU   A CD2  
2663 N  N    . GLU   A 377 ? 0.9761 0.7009 0.9739 0.0699  0.0599  -0.0987 404 GLU   A N    
2664 C  CA   . GLU   A 377 ? 0.9958 0.7305 1.0110 0.0569  0.0632  -0.1291 404 GLU   A CA   
2665 C  C    . GLU   A 377 ? 1.0969 0.8268 1.1144 0.0732  0.0680  -0.1327 404 GLU   A C    
2666 O  O    . GLU   A 377 ? 1.0043 0.7634 1.0233 0.0691  0.0604  -0.1518 404 GLU   A O    
2667 C  CB   . GLU   A 377 ? 1.0564 0.7631 1.0984 0.0409  0.0826  -0.1471 404 GLU   A CB   
2668 C  CG   . GLU   A 377 ? 1.0552 0.7744 1.1189 0.0286  0.0867  -0.1848 404 GLU   A CG   
2669 C  CD   . GLU   A 377 ? 1.2499 0.9698 1.3402 0.0051  0.0943  -0.2119 404 GLU   A CD   
2670 O  OE1  . GLU   A 377 ? 1.3098 1.0142 1.4042 -0.0018 0.0996  -0.1989 404 GLU   A OE1  
2671 O  OE2  . GLU   A 377 ? 1.3230 1.0631 1.4317 -0.0059 0.0947  -0.2483 404 GLU   A OE2  
2672 N  N    . ALA   A 378 ? 1.0046 0.6999 1.0216 0.0939  0.0815  -0.1134 405 ALA   A N    
2673 C  CA   . ALA   A 378 ? 0.9153 0.6073 0.9345 0.1129  0.0856  -0.1142 405 ALA   A CA   
2674 C  C    . ALA   A 378 ? 1.0511 0.7873 1.0535 0.1215  0.0634  -0.1089 405 ALA   A C    
2675 O  O    . ALA   A 378 ? 0.9995 0.7548 1.0069 0.1244  0.0608  -0.1232 405 ALA   A O    
2676 C  CB   . ALA   A 378 ? 0.8535 0.5021 0.8729 0.1379  0.1044  -0.0892 405 ALA   A CB   
2677 N  N    . LEU   A 379 ? 1.0605 0.8144 1.0463 0.1252  0.0488  -0.0901 406 LEU   A N    
2678 C  CA   . LEU   A 379 ? 0.9418 0.7381 0.9199 0.1299  0.0295  -0.0878 406 LEU   A CA   
2679 C  C    . LEU   A 379 ? 0.9687 0.7975 0.9510 0.1094  0.0212  -0.1064 406 LEU   A C    
2680 O  O    . LEU   A 379 ? 1.0271 0.8856 1.0116 0.1128  0.0143  -0.1113 406 LEU   A O    
2681 C  CB   . LEU   A 379 ? 0.9517 0.7599 0.9164 0.1357  0.0168  -0.0691 406 LEU   A CB   
2682 C  CG   . LEU   A 379 ? 1.0195 0.8126 0.9738 0.1636  0.0201  -0.0484 406 LEU   A CG   
2683 C  CD1  . LEU   A 379 ? 0.9901 0.7950 0.9304 0.1657  0.0090  -0.0350 406 LEU   A CD1  
2684 C  CD2  . LEU   A 379 ? 0.9569 0.7715 0.9143 0.1851  0.0140  -0.0484 406 LEU   A CD2  
2685 N  N    . TRP   A 380 ? 1.0270 0.8534 1.0110 0.0897  0.0228  -0.1162 407 TRP   A N    
2686 C  CA   . TRP   A 380 ? 0.9094 0.7705 0.8935 0.0741  0.0152  -0.1316 407 TRP   A CA   
2687 C  C    . TRP   A 380 ? 0.9874 0.8571 0.9795 0.0750  0.0226  -0.1540 407 TRP   A C    
2688 O  O    . TRP   A 380 ? 0.8881 0.7937 0.8763 0.0734  0.0164  -0.1603 407 TRP   A O    
2689 C  CB   . TRP   A 380 ? 0.9308 0.7905 0.9157 0.0560  0.0145  -0.1381 407 TRP   A CB   
2690 C  CG   . TRP   A 380 ? 0.9985 0.8939 0.9831 0.0434  0.0092  -0.1570 407 TRP   A CG   
2691 C  CD1  . TRP   A 380 ? 0.8917 0.8236 0.8666 0.0395  -0.0026 -0.1499 407 TRP   A CD1  
2692 C  CD2  . TRP   A 380 ? 0.9172 0.8181 0.9120 0.0353  0.0165  -0.1865 407 TRP   A CD2  
2693 N  NE1  . TRP   A 380 ? 0.9218 0.8839 0.8954 0.0324  -0.0036 -0.1698 407 TRP   A NE1  
2694 C  CE2  . TRP   A 380 ? 0.9666 0.9133 0.9523 0.0291  0.0065  -0.1953 407 TRP   A CE2  
2695 C  CE3  . TRP   A 380 ? 0.9323 0.8048 0.9454 0.0335  0.0316  -0.2074 407 TRP   A CE3  
2696 C  CZ2  . TRP   A 380 ? 0.9520 0.9234 0.9429 0.0226  0.0082  -0.2266 407 TRP   A CZ2  
2697 C  CZ3  . TRP   A 380 ? 1.0360 0.9297 1.0601 0.0237  0.0342  -0.2416 407 TRP   A CZ3  
2698 C  CH2  . TRP   A 380 ? 1.0985 1.0445 1.1097 0.0190  0.0211  -0.2521 407 TRP   A CH2  
2699 N  N    . LYS   A 381 ? 0.9689 0.8054 0.9736 0.0782  0.0380  -0.1661 408 LYS   A N    
2700 C  CA   . LYS   A 381 ? 0.9751 0.8184 0.9901 0.0799  0.0462  -0.1911 408 LYS   A CA   
2701 C  C    . LYS   A 381 ? 0.9961 0.8592 1.0064 0.0963  0.0422  -0.1838 408 LYS   A C    
2702 O  O    . LYS   A 381 ? 1.0085 0.9022 1.0185 0.0953  0.0413  -0.2002 408 LYS   A O    
2703 C  CB   . LYS   A 381 ? 0.9520 0.7491 0.9876 0.0821  0.0665  -0.2032 408 LYS   A CB   
2704 C  CG   . LYS   A 381 ? 1.0254 0.8264 1.0760 0.0847  0.0766  -0.2327 408 LYS   A CG   
2705 C  CD   . LYS   A 381 ? 1.2447 1.0055 1.3244 0.0769  0.0975  -0.2556 408 LYS   A CD   
2706 C  CE   . LYS   A 381 ? 1.1933 0.9580 1.2907 0.0804  0.1080  -0.2885 408 LYS   A CE   
2707 N  NZ   . LYS   A 381 ? 1.2651 1.0039 1.3658 0.1044  0.1184  -0.2728 408 LYS   A NZ   
2708 N  N    . LYS   A 382 ? 1.0927 0.9429 1.1000 0.1126  0.0401  -0.1604 409 LYS   A N    
2709 C  CA   . LYS   A 382 ? 0.8945 0.7684 0.9022 0.1279  0.0353  -0.1547 409 LYS   A CA   
2710 C  C    . LYS   A 382 ? 0.9075 0.8273 0.9096 0.1187  0.0232  -0.1535 409 LYS   A C    
2711 O  O    . LYS   A 382 ? 0.9568 0.9038 0.9631 0.1237  0.0240  -0.1600 409 LYS   A O    
2712 C  CB   . LYS   A 382 ? 0.9714 0.8315 0.9769 0.1478  0.0322  -0.1316 409 LYS   A CB   
2713 C  CG   . LYS   A 382 ? 1.0422 0.9289 1.0538 0.1652  0.0272  -0.1285 409 LYS   A CG   
2714 C  CD   . LYS   A 382 ? 1.0906 0.9654 1.1129 0.1775  0.0409  -0.1421 409 LYS   A CD   
2715 C  CE   . LYS   A 382 ? 1.0378 0.8627 1.0629 0.1912  0.0559  -0.1356 409 LYS   A CE   
2716 N  NZ   . LYS   A 382 ? 1.1943 1.0029 1.2343 0.2017  0.0719  -0.1515 409 LYS   A NZ   
2717 N  N    . MET   A 383 ? 0.9887 0.9170 0.9831 0.1059  0.0141  -0.1440 410 MET   A N    
2718 C  CA   . MET   A 383 ? 0.9532 0.9207 0.9451 0.0980  0.0061  -0.1392 410 MET   A CA   
2719 C  C    . MET   A 383 ? 0.9340 0.9258 0.9206 0.0897  0.0104  -0.1563 410 MET   A C    
2720 O  O    . MET   A 383 ? 0.9846 1.0108 0.9698 0.0898  0.0097  -0.1525 410 MET   A O    
2721 C  CB   . MET   A 383 ? 0.8569 0.8240 0.8439 0.0883  -0.0033 -0.1245 410 MET   A CB   
2722 C  CG   . MET   A 383 ? 0.8538 0.7987 0.8420 0.0977  -0.0077 -0.1109 410 MET   A CG   
2723 S  SD   . MET   A 383 ? 0.8631 0.8191 0.8506 0.0896  -0.0200 -0.0955 410 MET   A SD   
2724 C  CE   . MET   A 383 ? 0.9379 0.8555 0.9151 0.0952  -0.0187 -0.0879 410 MET   A CE   
2725 N  N    . GLU   A 384 ? 0.8883 0.8654 0.8735 0.0835  0.0160  -0.1759 411 GLU   A N    
2726 C  CA   . GLU   A 384 ? 0.8634 0.8696 0.8439 0.0795  0.0195  -0.1987 411 GLU   A CA   
2727 C  C    . GLU   A 384 ? 0.9515 0.9719 0.9363 0.0921  0.0269  -0.2074 411 GLU   A C    
2728 O  O    . GLU   A 384 ? 1.0411 1.1009 1.0176 0.0939  0.0278  -0.2125 411 GLU   A O    
2729 C  CB   . GLU   A 384 ? 1.0053 0.9932 0.9921 0.0701  0.0246  -0.2248 411 GLU   A CB   
2730 C  CG   . GLU   A 384 ? 0.9558 0.9510 0.9373 0.0558  0.0170  -0.2246 411 GLU   A CG   
2731 C  CD   . GLU   A 384 ? 0.9034 0.9511 0.8695 0.0533  0.0098  -0.2301 411 GLU   A CD   
2732 O  OE1  . GLU   A 384 ? 1.1151 1.1906 1.0786 0.0565  0.0133  -0.2551 411 GLU   A OE1  
2733 O  OE2  . GLU   A 384 ? 0.9017 0.9642 0.8580 0.0501  0.0015  -0.2094 411 GLU   A OE2  
2734 N  N    . GLY   A 385 ? 1.0651 1.0552 1.0622 0.1031  0.0333  -0.2076 412 GLY   A N    
2735 C  CA   . GLY   A 385 ? 1.0278 1.0313 1.0314 0.1167  0.0401  -0.2142 412 GLY   A CA   
2736 C  C    . GLY   A 385 ? 0.9746 1.0083 0.9789 0.1224  0.0352  -0.1938 412 GLY   A C    
2737 O  O    . GLY   A 385 ? 0.9979 1.0593 1.0052 0.1297  0.0410  -0.1996 412 GLY   A O    
2738 N  N    . VAL   A 386 ? 0.8451 0.8751 0.8503 0.1189  0.0260  -0.1717 413 VAL   A N    
2739 C  CA   . VAL   A 386 ? 0.8715 0.9309 0.8852 0.1209  0.0227  -0.1555 413 VAL   A CA   
2740 C  C    . VAL   A 386 ? 0.9636 1.0591 0.9687 0.1128  0.0261  -0.1533 413 VAL   A C    
2741 O  O    . VAL   A 386 ? 0.9363 1.0615 0.9493 0.1176  0.0330  -0.1493 413 VAL   A O    
2742 C  CB   . VAL   A 386 ? 0.9224 0.9701 0.9418 0.1184  0.0121  -0.1374 413 VAL   A CB   
2743 C  CG1  . VAL   A 386 ? 0.7005 0.7799 0.7330 0.1134  0.0101  -0.1240 413 VAL   A CG1  
2744 C  CG2  . VAL   A 386 ? 0.8487 0.8757 0.8770 0.1341  0.0095  -0.1355 413 VAL   A CG2  
2745 N  N    . THR   A 387 ? 0.9001 0.9956 0.8895 0.1022  0.0226  -0.1547 414 THR   A N    
2746 C  CA   . THR   A 387 ? 0.9359 1.0684 0.9123 0.0990  0.0262  -0.1510 414 THR   A CA   
2747 C  C    . THR   A 387 ? 0.8911 1.0496 0.8599 0.1076  0.0360  -0.1698 414 THR   A C    
2748 O  O    . THR   A 387 ? 0.9330 1.1275 0.8970 0.1127  0.0440  -0.1608 414 THR   A O    
2749 C  CB   . THR   A 387 ? 0.8972 1.0277 0.8581 0.0889  0.0191  -0.1532 414 THR   A CB   
2750 O  OG1  . THR   A 387 ? 0.8091 0.9153 0.7774 0.0817  0.0109  -0.1367 414 THR   A OG1  
2751 C  CG2  . THR   A 387 ? 0.8604 1.0332 0.8053 0.0902  0.0225  -0.1450 414 THR   A CG2  
2752 N  N    . ASN   A 388 ? 0.8961 1.0365 0.8654 0.1102  0.0376  -0.1958 415 ASN   A N    
2753 C  CA   . ASN   A 388 ? 0.8838 1.0481 0.8489 0.1193  0.0470  -0.2181 415 ASN   A CA   
2754 C  C    . ASN   A 388 ? 0.9987 1.1738 0.9778 0.1307  0.0553  -0.2089 415 ASN   A C    
2755 O  O    . ASN   A 388 ? 0.8955 1.1063 0.8683 0.1386  0.0648  -0.2149 415 ASN   A O    
2756 C  CB   . ASN   A 388 ? 0.8906 1.0270 0.8615 0.1186  0.0489  -0.2498 415 ASN   A CB   
2757 C  CG   . ASN   A 388 ? 0.8897 1.0504 0.8591 0.1281  0.0587  -0.2782 415 ASN   A CG   
2758 O  OD1  . ASN   A 388 ? 0.9823 1.1890 0.9339 0.1311  0.0606  -0.2855 415 ASN   A OD1  
2759 N  ND2  . ASN   A 388 ? 1.1656 1.2968 1.1529 0.1351  0.0660  -0.2936 415 ASN   A ND2  
2760 N  N    . ALA   A 389 ? 0.9273 1.0766 0.9256 0.1331  0.0521  -0.1955 416 ALA   A N    
2761 C  CA   . ALA   A 389 ? 0.8365 1.0013 0.8534 0.1435  0.0586  -0.1880 416 ALA   A CA   
2762 C  C    . ALA   A 389 ? 0.9509 1.1517 0.9716 0.1401  0.0638  -0.1668 416 ALA   A C    
2763 O  O    . ALA   A 389 ? 0.9936 1.2230 1.0238 0.1477  0.0754  -0.1656 416 ALA   A O    
2764 C  CB   . ALA   A 389 ? 0.8085 0.9443 0.8448 0.1488  0.0514  -0.1802 416 ALA   A CB   
2765 N  N    . VAL   A 390 ? 0.9677 1.1664 0.9838 0.1292  0.0577  -0.1490 417 VAL   A N    
2766 C  CA   . VAL   A 390 ? 0.8431 1.0714 0.8652 0.1261  0.0665  -0.1266 417 VAL   A CA   
2767 C  C    . VAL   A 390 ? 0.9173 1.1810 0.9149 0.1319  0.0781  -0.1286 417 VAL   A C    
2768 O  O    . VAL   A 390 ? 1.0432 1.3374 1.0477 0.1378  0.0936  -0.1161 417 VAL   A O    
2769 C  CB   . VAL   A 390 ? 0.9537 1.1680 0.9780 0.1143  0.0579  -0.1082 417 VAL   A CB   
2770 C  CG1  . VAL   A 390 ? 0.8696 1.1110 0.9004 0.1121  0.0708  -0.0835 417 VAL   A CG1  
2771 C  CG2  . VAL   A 390 ? 0.7683 0.9573 0.8174 0.1114  0.0473  -0.1066 417 VAL   A CG2  
2772 N  N    . LEU   A 391 ? 0.9828 1.2463 0.9527 0.1314  0.0717  -0.1452 418 LEU   A N    
2773 C  CA   . LEU   A 391 ? 0.8916 1.1961 0.8348 0.1402  0.0802  -0.1526 418 LEU   A CA   
2774 C  C    . LEU   A 391 ? 1.0532 1.3767 0.9992 0.1523  0.0917  -0.1705 418 LEU   A C    
2775 O  O    . LEU   A 391 ? 1.1190 1.4847 1.0483 0.1630  0.1042  -0.1684 418 LEU   A O    
2776 C  CB   . LEU   A 391 ? 0.8906 1.1944 0.8101 0.1365  0.0686  -0.1750 418 LEU   A CB   
2777 C  CG   . LEU   A 391 ? 0.9280 1.2246 0.8397 0.1272  0.0586  -0.1576 418 LEU   A CG   
2778 C  CD1  . LEU   A 391 ? 0.9061 1.2036 0.8015 0.1226  0.0470  -0.1858 418 LEU   A CD1  
2779 C  CD2  . LEU   A 391 ? 0.9846 1.3174 0.8842 0.1341  0.0687  -0.1263 418 LEU   A CD2  
2780 N  N    . HIS   A 392 ? 1.1034 1.3978 1.0694 0.1530  0.0887  -0.1871 419 HIS   A N    
2781 C  CA   . HIS   A 392 ? 1.1071 1.4174 1.0805 0.1653  0.1001  -0.2033 419 HIS   A CA   
2782 C  C    . HIS   A 392 ? 1.0990 1.4329 1.0925 0.1702  0.1141  -0.1797 419 HIS   A C    
2783 O  O    . HIS   A 392 ? 1.1422 1.5088 1.1330 0.1814  0.1287  -0.1853 419 HIS   A O    
2784 C  CB   . HIS   A 392 ? 1.1245 1.3946 1.1158 0.1671  0.0942  -0.2240 419 HIS   A CB   
2785 C  CG   . HIS   A 392 ? 1.3654 1.6482 1.3637 0.1808  0.1053  -0.2460 419 HIS   A CG   
2786 N  ND1  . HIS   A 392 ? 1.4677 1.7333 1.4928 0.1891  0.1076  -0.2466 419 HIS   A ND1  
2787 C  CD2  . HIS   A 392 ? 1.3994 1.7135 1.3817 0.1893  0.1145  -0.2696 419 HIS   A CD2  
2788 C  CE1  . HIS   A 392 ? 1.3547 1.6370 1.3813 0.2014  0.1187  -0.2685 419 HIS   A CE1  
2789 N  NE2  . HIS   A 392 ? 1.4458 1.7574 1.4466 0.2012  0.1233  -0.2838 419 HIS   A NE2  
2790 N  N    . GLU   A 393 ? 1.1237 1.4437 1.1404 0.1616  0.1109  -0.1554 420 GLU   A N    
2791 C  CA   . GLU   A 393 ? 1.1578 1.4987 1.2048 0.1634  0.1251  -0.1366 420 GLU   A CA   
2792 C  C    . GLU   A 393 ? 1.1479 1.5254 1.1837 0.1655  0.1436  -0.1131 420 GLU   A C    
2793 O  O    . GLU   A 393 ? 1.1560 1.5629 1.2058 0.1728  0.1630  -0.1054 420 GLU   A O    
2794 C  CB   . GLU   A 393 ? 1.0835 1.4008 1.1635 0.1531  0.1153  -0.1238 420 GLU   A CB   
2795 C  CG   . GLU   A 393 ? 1.1347 1.4747 1.2552 0.1508  0.1301  -0.1065 420 GLU   A CG   
2796 C  CD   . GLU   A 393 ? 1.2248 1.5803 1.3721 0.1610  0.1366  -0.1207 420 GLU   A CD   
2797 O  OE1  . GLU   A 393 ? 1.2919 1.6341 1.4275 0.1707  0.1278  -0.1424 420 GLU   A OE1  
2798 O  OE2  . GLU   A 393 ? 1.1585 1.5390 1.3421 0.1596  0.1521  -0.1102 420 GLU   A OE2  
2799 N  N    . VAL   A 394 ? 1.0660 1.4434 1.0770 0.1609  0.1394  -0.0998 421 VAL   A N    
2800 C  CA   . VAL   A 394 ? 1.0681 1.4796 1.0661 0.1667  0.1585  -0.0722 421 VAL   A CA   
2801 C  C    . VAL   A 394 ? 1.1396 1.5927 1.1046 0.1841  0.1706  -0.0833 421 VAL   A C    
2802 O  O    . VAL   A 394 ? 1.2026 1.6906 1.1604 0.1943  0.1928  -0.0592 421 VAL   A O    
2803 C  CB   . VAL   A 394 ? 1.0482 1.4508 1.0268 0.1607  0.1499  -0.0551 421 VAL   A CB   
2804 C  CG1  . VAL   A 394 ? 0.9785 1.3419 0.9895 0.1442  0.1380  -0.0468 421 VAL   A CG1  
2805 C  CG2  . VAL   A 394 ? 1.1502 1.5554 1.0888 0.1641  0.1327  -0.0808 421 VAL   A CG2  
2806 N  N    . LYS   A 395 ? 1.1883 1.6396 1.1347 0.1886  0.1586  -0.1196 422 LYS   A N    
2807 C  CA   . LYS   A 395 ? 1.2182 1.7113 1.1356 0.2054  0.1684  -0.1383 422 LYS   A CA   
2808 C  C    . LYS   A 395 ? 1.1973 1.6984 1.1371 0.2128  0.1811  -0.1513 422 LYS   A C    
2809 O  O    . LYS   A 395 ? 1.2602 1.7906 1.1798 0.2263  0.1870  -0.1755 422 LYS   A O    
2810 C  CB   . LYS   A 395 ? 1.2223 1.7126 1.1118 0.2058  0.1499  -0.1761 422 LYS   A CB   
2811 C  CG   . LYS   A 395 ? 1.2277 1.7301 1.0877 0.2041  0.1398  -0.1675 422 LYS   A CG   
2812 C  CD   . LYS   A 395 ? 1.2402 1.7157 1.0960 0.1936  0.1177  -0.2022 422 LYS   A CD   
2813 C  CE   . LYS   A 395 ? 1.2976 1.8033 1.1204 0.1968  0.1082  -0.2045 422 LYS   A CE   
2814 N  NZ   . LYS   A 395 ? 1.2398 1.7174 1.0699 0.1841  0.0991  -0.1761 422 LYS   A NZ   
2815 N  N    . ARG   A 396 ? 1.1373 1.6168 1.1197 0.2052  0.1847  -0.1385 423 ARG   A N    
2816 C  CA   . ARG   A 396 ? 1.2252 1.7148 1.2336 0.2128  0.1963  -0.1501 423 ARG   A CA   
2817 C  C    . ARG   A 396 ? 1.3174 1.8511 1.3308 0.2222  0.2252  -0.1255 423 ARG   A C    
2818 O  O    . ARG   A 396 ? 1.3062 1.8478 1.3249 0.2178  0.2373  -0.0913 423 ARG   A O    
2819 C  CB   . ARG   A 396 ? 1.2048 1.6598 1.2584 0.2029  0.1864  -0.1497 423 ARG   A CB   
2820 C  CG   . ARG   A 396 ? 1.1100 1.5717 1.1903 0.2127  0.1924  -0.1683 423 ARG   A CG   
2821 C  CD   . ARG   A 396 ? 1.0462 1.4840 1.1710 0.2060  0.1820  -0.1654 423 ARG   A CD   
2822 N  NE   . ARG   A 396 ? 1.1664 1.6136 1.3220 0.1945  0.1903  -0.1376 423 ARG   A NE   
2823 C  CZ   . ARG   A 396 ? 1.2459 1.7024 1.4512 0.1920  0.1947  -0.1344 423 ARG   A CZ   
2824 N  NH1  . ARG   A 396 ? 1.2848 1.7450 1.5118 0.2024  0.1906  -0.1544 423 ARG   A NH1  
2825 N  NH2  . ARG   A 396 ? 1.2275 1.6915 1.4648 0.1793  0.2039  -0.1121 423 ARG   A NH2  
2826 N  N    . GLU   A 397 ? 1.3665 1.9277 1.3801 0.2359  0.2386  -0.1423 424 GLU   A N    
2827 C  CA   . GLU   A 397 ? 1.3989 2.0064 1.4113 0.2479  0.2691  -0.1205 424 GLU   A CA   
2828 C  C    . GLU   A 397 ? 1.4642 2.0700 1.5329 0.2392  0.2862  -0.0956 424 GLU   A C    
2829 O  O    . GLU   A 397 ? 1.4461 2.0765 1.5227 0.2414  0.3126  -0.0623 424 GLU   A O    
2830 C  CB   . GLU   A 397 ? 1.4328 2.0728 1.4266 0.2661  0.2778  -0.1500 424 GLU   A CB   
2831 C  CG   . GLU   A 397 ? 1.4578 2.1100 1.3999 0.2754  0.2641  -0.1795 424 GLU   A CG   
2832 C  CD   . GLU   A 397 ? 1.5008 2.1920 1.4251 0.2946  0.2757  -0.2098 424 GLU   A CD   
2833 O  OE1  . GLU   A 397 ? 1.4515 2.1537 1.4049 0.3002  0.2924  -0.2092 424 GLU   A OE1  
2834 O  OE2  . GLU   A 397 ? 1.5656 2.2794 1.4491 0.3043  0.2679  -0.2369 424 GLU   A OE2  
2835 N  N    . GLY   A 398 ? 1.3859 1.9649 1.4962 0.2304  0.2728  -0.1114 425 GLY   A N    
2836 C  CA   . GLY   A 398 ? 1.3807 1.9639 1.5508 0.2220  0.2860  -0.0968 425 GLY   A CA   
2837 C  C    . GLY   A 398 ? 1.4727 2.0340 1.6721 0.2038  0.2828  -0.0724 425 GLY   A C    
2838 O  O    . GLY   A 398 ? 1.4796 2.0430 1.7360 0.1942  0.2900  -0.0672 425 GLY   A O    
2839 N  N    . LEU   A 399 ? 1.3752 1.9179 1.5404 0.1987  0.2723  -0.0599 426 LEU   A N    
2840 C  CA   . LEU   A 399 ? 1.2027 1.7226 1.3947 0.1819  0.2692  -0.0381 426 LEU   A CA   
2841 C  C    . LEU   A 399 ? 1.1863 1.7275 1.3839 0.1827  0.3018  0.0009  426 LEU   A C    
2842 O  O    . LEU   A 399 ? 1.2729 1.8328 1.4211 0.1961  0.3116  0.0147  426 LEU   A O    
2843 C  CB   . LEU   A 399 ? 1.2165 1.7033 1.3727 0.1762  0.2409  -0.0447 426 LEU   A CB   
2844 C  CG   . LEU   A 399 ? 1.1844 1.6441 1.3662 0.1592  0.2334  -0.0274 426 LEU   A CG   
2845 C  CD1  . LEU   A 399 ? 1.1359 1.5767 1.3642 0.1489  0.2162  -0.0460 426 LEU   A CD1  
2846 C  CD2  . LEU   A 399 ? 1.0839 1.5221 1.2196 0.1575  0.2142  -0.0258 426 LEU   A CD2  
2847 N  N    . PRO   A 400 ? 1.1876 1.7287 1.4453 0.1703  0.3205  0.0189  427 PRO   A N    
2848 C  CA   . PRO   A 400 ? 1.1288 1.6845 1.3967 0.1716  0.3566  0.0603  427 PRO   A CA   
2849 C  C    . PRO   A 400 ? 1.0733 1.6095 1.3040 0.1711  0.3497  0.0829  427 PRO   A C    
2850 O  O    . PRO   A 400 ? 1.1232 1.6292 1.3425 0.1618  0.3187  0.0678  427 PRO   A O    
2851 C  CB   . PRO   A 400 ? 1.0676 1.6190 1.4200 0.1533  0.3727  0.0651  427 PRO   A CB   
2852 C  CG   . PRO   A 400 ? 1.1070 1.6350 1.4817 0.1411  0.3357  0.0297  427 PRO   A CG   
2853 C  CD   . PRO   A 400 ? 1.1835 1.7130 1.5055 0.1553  0.3104  0.0011  427 PRO   A CD   
2854 N  N    . VAL   A 401 ? 1.0905 1.6464 1.3019 0.1834  0.3806  0.1212  428 VAL   A N    
2855 C  CA   . VAL   A 401 ? 1.2079 1.7526 1.3797 0.1882  0.3765  0.1459  428 VAL   A CA   
2856 C  C    . VAL   A 401 ? 1.1754 1.6808 1.3949 0.1666  0.3707  0.1551  428 VAL   A C    
2857 O  O    . VAL   A 401 ? 1.1302 1.6129 1.3235 0.1630  0.3468  0.1529  428 VAL   A O    
2858 C  CB   . VAL   A 401 ? 1.1994 1.7778 1.3429 0.2105  0.4147  0.1896  428 VAL   A CB   
2859 C  CG1  . VAL   A 401 ? 1.2127 1.7741 1.3491 0.2118  0.4236  0.2281  428 VAL   A CG1  
2860 C  CG2  . VAL   A 401 ? 1.1585 1.7764 1.2290 0.2354  0.4066  0.1752  428 VAL   A CG2  
2861 N  N    . GLU   A 402 ? 1.1989 1.6977 1.4925 0.1515  0.3925  0.1619  429 GLU   A N    
2862 C  CA   . GLU   A 402 ? 1.1577 1.6227 1.5037 0.1305  0.3892  0.1666  429 GLU   A CA   
2863 C  C    . GLU   A 402 ? 1.1630 1.6027 1.5056 0.1178  0.3437  0.1272  429 GLU   A C    
2864 O  O    . GLU   A 402 ? 1.1731 1.5847 1.5210 0.1074  0.3296  0.1299  429 GLU   A O    
2865 C  CB   . GLU   A 402 ? 1.2001 1.6691 1.6335 0.1159  0.4213  0.1730  429 GLU   A CB   
2866 C  CG   . GLU   A 402 ? 1.2337 1.7131 1.6852 0.1241  0.4727  0.2226  429 GLU   A CG   
2867 C  CD   . GLU   A 402 ? 1.3584 1.8081 1.8166 0.1202  0.4832  0.2551  429 GLU   A CD   
2868 O  OE1  . GLU   A 402 ? 1.3438 1.7671 1.8677 0.0978  0.4818  0.2454  429 GLU   A OE1  
2869 O  OE2  . GLU   A 402 ? 1.4511 1.9066 1.8497 0.1411  0.4926  0.2887  429 GLU   A OE2  
2870 N  N    . GLN   A 403 ? 1.1329 1.5822 1.4668 0.1201  0.3221  0.0918  430 GLN   A N    
2871 C  CA   . GLN   A 403 ? 1.1566 1.5823 1.4823 0.1122  0.2816  0.0583  430 GLN   A CA   
2872 C  C    . GLN   A 403 ? 1.1164 1.5286 1.3710 0.1208  0.2583  0.0563  430 GLN   A C    
2873 O  O    . GLN   A 403 ? 1.1342 1.5189 1.3822 0.1121  0.2325  0.0453  430 GLN   A O    
2874 C  CB   . GLN   A 403 ? 1.2321 1.6712 1.5719 0.1153  0.2688  0.0247  430 GLN   A CB   
2875 C  CG   . GLN   A 403 ? 1.2981 1.7403 1.7132 0.1012  0.2684  0.0085  430 GLN   A CG   
2876 C  CD   . GLN   A 403 ? 1.4412 1.8866 1.8581 0.1060  0.2406  -0.0278 430 GLN   A CD   
2877 O  OE1  . GLN   A 403 ? 1.3926 1.8635 1.8498 0.1082  0.2487  -0.0418 430 GLN   A OE1  
2878 N  NE2  . GLN   A 403 ? 1.4741 1.8941 1.8489 0.1091  0.2092  -0.0420 430 GLN   A NE2  
2879 N  N    . ARG   A 404 ? 1.0402 1.4751 1.2431 0.1383  0.2673  0.0648  431 ARG   A N    
2880 C  CA   . ARG   A 404 ? 1.1376 1.5673 1.2776 0.1465  0.2464  0.0591  431 ARG   A CA   
2881 C  C    . ARG   A 404 ? 1.0929 1.5049 1.2268 0.1415  0.2458  0.0846  431 ARG   A C    
2882 O  O    . ARG   A 404 ? 1.1111 1.5013 1.2222 0.1363  0.2193  0.0718  431 ARG   A O    
2883 C  CB   . ARG   A 404 ? 1.0809 1.5483 1.1718 0.1677  0.2590  0.0621  431 ARG   A CB   
2884 C  CG   . ARG   A 404 ? 1.1283 1.5992 1.1583 0.1766  0.2363  0.0467  431 ARG   A CG   
2885 C  CD   . ARG   A 404 ? 1.0855 1.6031 1.0679 0.1997  0.2503  0.0491  431 ARG   A CD   
2886 N  NE   . ARG   A 404 ? 1.1904 1.7317 1.1461 0.2136  0.2683  0.0872  431 ARG   A NE   
2887 C  CZ   . ARG   A 404 ? 1.1978 1.7486 1.1768 0.2184  0.3018  0.1288  431 ARG   A CZ   
2888 N  NH1  . ARG   A 404 ? 1.2766 1.8190 1.3103 0.2084  0.3218  0.1354  431 ARG   A NH1  
2889 N  NH2  . ARG   A 404 ? 1.1879 1.7589 1.1371 0.2349  0.3170  0.1650  431 ARG   A NH2  
2890 N  N    . ASN   A 405 ? 1.0569 1.4769 1.2137 0.1434  0.2771  0.1218  432 ASN   A N    
2891 C  CA   . ASN   A 405 ? 1.1373 1.5401 1.2916 0.1411  0.2803  0.1493  432 ASN   A CA   
2892 C  C    . ASN   A 405 ? 1.0923 1.4575 1.2927 0.1189  0.2641  0.1373  432 ASN   A C    
2893 O  O    . ASN   A 405 ? 1.0180 1.3638 1.2077 0.1157  0.2544  0.1475  432 ASN   A O    
2894 C  CB   . ASN   A 405 ? 1.1456 1.5641 1.3171 0.1511  0.3230  0.1952  432 ASN   A CB   
2895 C  CG   . ASN   A 405 ? 1.0958 1.5565 1.2101 0.1780  0.3384  0.2119  432 ASN   A CG   
2896 O  OD1  . ASN   A 405 ? 1.1139 1.5923 1.1744 0.1883  0.3148  0.1871  432 ASN   A OD1  
2897 N  ND2  . ASN   A 405 ? 0.9914 1.4702 1.1192 0.1903  0.3797  0.2530  432 ASN   A ND2  
2898 N  N    . GLU   A 406 ? 1.1404 1.4992 1.3916 0.1054  0.2606  0.1146  433 GLU   A N    
2899 C  CA   . GLU   A 406 ? 1.1743 1.5046 1.4639 0.0872  0.2405  0.0962  433 GLU   A CA   
2900 C  C    . GLU   A 406 ? 1.1396 1.4523 1.3839 0.0874  0.2029  0.0721  433 GLU   A C    
2901 O  O    . GLU   A 406 ? 1.1368 1.4251 1.3881 0.0776  0.1873  0.0688  433 GLU   A O    
2902 C  CB   . GLU   A 406 ? 1.2584 1.5963 1.6082 0.0768  0.2424  0.0730  433 GLU   A CB   
2903 C  CG   . GLU   A 406 ? 1.2896 1.6287 1.7142 0.0641  0.2727  0.0882  433 GLU   A CG   
2904 C  CD   . GLU   A 406 ? 1.3417 1.6777 1.8287 0.0477  0.2578  0.0555  433 GLU   A CD   
2905 O  OE1  . GLU   A 406 ? 1.1685 1.4850 1.6875 0.0347  0.2529  0.0532  433 GLU   A OE1  
2906 O  OE2  . GLU   A 406 ? 1.3260 1.6823 1.8300 0.0494  0.2505  0.0307  433 GLU   A OE2  
2907 N  N    . ILE   A 407 ? 1.1428 1.4671 1.3430 0.0984  0.1902  0.0546  434 ILE   A N    
2908 C  CA   . ILE   A 407 ? 1.1011 1.4070 1.2636 0.0983  0.1586  0.0310  434 ILE   A CA   
2909 C  C    . ILE   A 407 ? 1.1293 1.4329 1.2454 0.1036  0.1534  0.0445  434 ILE   A C    
2910 O  O    . ILE   A 407 ? 1.0589 1.3397 1.1623 0.0971  0.1324  0.0358  434 ILE   A O    
2911 C  CB   . ILE   A 407 ? 1.1177 1.4341 1.2597 0.1074  0.1498  0.0047  434 ILE   A CB   
2912 C  CG1  . ILE   A 407 ? 1.0277 1.3545 1.2174 0.1054  0.1580  -0.0057 434 ILE   A CG1  
2913 C  CG2  . ILE   A 407 ? 1.1084 1.3999 1.2229 0.1058  0.1210  -0.0195 434 ILE   A CG2  
2914 C  CD1  . ILE   A 407 ? 1.0294 1.3614 1.2054 0.1149  0.1474  -0.0328 434 ILE   A CD1  
2915 N  N    . LEU   A 408 ? 1.0554 1.3866 1.1453 0.1173  0.1726  0.0658  435 LEU   A N    
2916 C  CA   . LEU   A 408 ? 1.0407 1.3791 1.0861 0.1259  0.1671  0.0779  435 LEU   A CA   
2917 C  C    . LEU   A 408 ? 1.0753 1.3910 1.1404 0.1172  0.1679  0.0998  435 LEU   A C    
2918 O  O    . LEU   A 408 ? 1.0666 1.3709 1.1076 0.1154  0.1489  0.0946  435 LEU   A O    
2919 C  CB   . LEU   A 408 ? 0.9958 1.3753 1.0105 0.1464  0.1898  0.0996  435 LEU   A CB   
2920 C  CG   . LEU   A 408 ? 1.0295 1.4377 1.0253 0.1575  0.1939  0.0797  435 LEU   A CG   
2921 C  CD1  . LEU   A 408 ? 1.1300 1.5843 1.0821 0.1813  0.2110  0.0986  435 LEU   A CD1  
2922 C  CD2  . LEU   A 408 ? 1.0191 1.4148 0.9968 0.1522  0.1649  0.0370  435 LEU   A CD2  
2923 N  N    . THR   A 409 ? 1.0598 1.3685 1.1729 0.1113  0.1910  0.1226  436 THR   A N    
2924 C  CA   . THR   A 409 ? 1.0039 1.2891 1.1431 0.1028  0.1948  0.1420  436 THR   A CA   
2925 C  C    . THR   A 409 ? 1.0626 1.3171 1.2154 0.0864  0.1659  0.1146  436 THR   A C    
2926 O  O    . THR   A 409 ? 1.0894 1.3261 1.2417 0.0821  0.1585  0.1225  436 THR   A O    
2927 C  CB   . THR   A 409 ? 1.0334 1.3156 1.2321 0.0974  0.2281  0.1662  436 THR   A CB   
2928 O  OG1  . THR   A 409 ? 0.9727 1.2846 1.1564 0.1149  0.2579  0.1943  436 THR   A OG1  
2929 C  CG2  . THR   A 409 ? 0.9934 1.2511 1.2210 0.0907  0.2369  0.1884  436 THR   A CG2  
2930 N  N    . ALA   A 410 ? 1.0121 1.2619 1.1752 0.0795  0.1501  0.0835  437 ALA   A N    
2931 C  CA   . ALA   A 410 ? 0.9430 1.1671 1.1178 0.0675  0.1247  0.0597  437 ALA   A CA   
2932 C  C    . ALA   A 410 ? 0.9891 1.2036 1.1143 0.0705  0.1003  0.0463  437 ALA   A C    
2933 O  O    . ALA   A 410 ? 1.0719 1.2644 1.1992 0.0626  0.0842  0.0392  437 ALA   A O    
2934 C  CB   . ALA   A 410 ? 1.0283 1.2544 1.2324 0.0631  0.1177  0.0340  437 ALA   A CB   
2935 N  N    . ILE   A 411 ? 0.9328 1.1648 1.0163 0.0815  0.0984  0.0406  438 ILE   A N    
2936 C  CA   . ILE   A 411 ? 0.9911 1.2144 1.0367 0.0823  0.0766  0.0202  438 ILE   A CA   
2937 C  C    . ILE   A 411 ? 0.9403 1.1806 0.9482 0.0904  0.0762  0.0309  438 ILE   A C    
2938 O  O    . ILE   A 411 ? 1.0124 1.2460 0.9955 0.0885  0.0587  0.0134  438 ILE   A O    
2939 C  CB   . ILE   A 411 ? 0.9240 1.1522 0.9564 0.0873  0.0707  -0.0058 438 ILE   A CB   
2940 C  CG1  . ILE   A 411 ? 0.8974 1.1607 0.9042 0.1008  0.0845  -0.0023 438 ILE   A CG1  
2941 C  CG2  . ILE   A 411 ? 0.8459 1.0660 0.9157 0.0837  0.0723  -0.0144 438 ILE   A CG2  
2942 C  CD1  . ILE   A 411 ? 0.9523 1.2204 0.9393 0.1063  0.0769  -0.0321 438 ILE   A CD1  
2943 N  N    . LEU   A 412 ? 0.9430 1.2071 0.9471 0.1006  0.0957  0.0593  439 LEU   A N    
2944 C  CA   . LEU   A 412 ? 1.0178 1.3084 0.9818 0.1136  0.0944  0.0685  439 LEU   A CA   
2945 C  C    . LEU   A 412 ? 0.9814 1.2545 0.9426 0.1073  0.0805  0.0725  439 LEU   A C    
2946 O  O    . LEU   A 412 ? 0.9860 1.2721 0.9160 0.1111  0.0657  0.0590  439 LEU   A O    
2947 C  CB   . LEU   A 412 ? 1.0742 1.3954 1.0337 0.1303  0.1214  0.1035  439 LEU   A CB   
2948 C  CG   . LEU   A 412 ? 1.1008 1.4682 1.0116 0.1526  0.1242  0.1115  439 LEU   A CG   
2949 C  CD1  . LEU   A 412 ? 1.2074 1.5798 1.0974 0.1569  0.1109  0.1183  439 LEU   A CD1  
2950 C  CD2  . LEU   A 412 ? 1.0566 1.4466 0.9393 0.1567  0.1118  0.0746  439 LEU   A CD2  
2951 N  N    . ALA   A 413 ? 1.0598 1.3055 1.0565 0.0972  0.0853  0.0881  440 ALA   A N    
2952 C  CA   . ALA   A 413 ? 0.8618 1.0907 0.8582 0.0917  0.0734  0.0920  440 ALA   A CA   
2953 C  C    . ALA   A 413 ? 0.9951 1.2060 0.9794 0.0810  0.0482  0.0595  440 ALA   A C    
2954 O  O    . ALA   A 413 ? 0.9219 1.1322 0.8901 0.0803  0.0361  0.0564  440 ALA   A O    
2955 C  CB   . ALA   A 413 ? 0.7831 0.9854 0.8254 0.0821  0.0843  0.1093  440 ALA   A CB   
2956 N  N    . SER   A 414 ? 1.0226 1.2192 1.0158 0.0739  0.0418  0.0366  441 SER   A N    
2957 C  CA   . SER   A 414 ? 0.8886 1.0653 0.8716 0.0659  0.0224  0.0094  441 SER   A CA   
2958 C  C    . SER   A 414 ? 0.8719 1.0689 0.8215 0.0718  0.0159  -0.0099 441 SER   A C    
2959 O  O    . SER   A 414 ? 0.8667 1.0546 0.8053 0.0663  0.0028  -0.0260 441 SER   A O    
2960 C  CB   . SER   A 414 ? 0.8993 1.0549 0.9035 0.0604  0.0194  -0.0055 441 SER   A CB   
2961 O  OG   . SER   A 414 ? 1.1045 1.2550 1.1443 0.0569  0.0286  0.0082  441 SER   A OG   
2962 N  N    . LEU   A 415 ? 0.8416 1.0682 0.7780 0.0828  0.0258  -0.0107 442 LEU   A N    
2963 C  CA   . LEU   A 415 ? 0.8879 1.1402 0.7954 0.0891  0.0197  -0.0342 442 LEU   A CA   
2964 C  C    . LEU   A 415 ? 1.0412 1.3244 0.9262 0.0968  0.0155  -0.0268 442 LEU   A C    
2965 O  O    . LEU   A 415 ? 0.9493 1.2464 0.8185 0.0958  0.0036  -0.0527 442 LEU   A O    
2966 C  CB   . LEU   A 415 ? 0.7684 1.0479 0.6674 0.1006  0.0318  -0.0389 442 LEU   A CB   
2967 C  CG   . LEU   A 415 ? 0.8455 1.1011 0.7649 0.0958  0.0345  -0.0521 442 LEU   A CG   
2968 C  CD1  . LEU   A 415 ? 0.7545 1.0412 0.6625 0.1081  0.0458  -0.0610 442 LEU   A CD1  
2969 C  CD2  . LEU   A 415 ? 0.9042 1.1260 0.8281 0.0853  0.0201  -0.0792 442 LEU   A CD2  
2970 N  N    . THR   A 416 ? 1.0312 1.3266 0.9176 0.1052  0.0261  0.0074  443 THR   A N    
2971 C  CA   . THR   A 416 ? 1.0430 1.3677 0.9089 0.1155  0.0219  0.0186  443 THR   A CA   
2972 C  C    . THR   A 416 ? 0.9929 1.2940 0.8663 0.1019  0.0050  0.0057  443 THR   A C    
2973 O  O    . THR   A 416 ? 1.1347 1.4606 0.9907 0.1044  -0.0073 -0.0126 443 THR   A O    
2974 C  CB   . THR   A 416 ? 1.0411 1.3744 0.9128 0.1280  0.0406  0.0628  443 THR   A CB   
2975 O  OG1  . THR   A 416 ? 1.1292 1.4941 0.9877 0.1445  0.0584  0.0763  443 THR   A OG1  
2976 C  CG2  . THR   A 416 ? 1.1237 1.4810 0.9782 0.1396  0.0354  0.0779  443 THR   A CG2  
2977 N  N    . ALA   A 417 ? 0.9054 1.1622 0.8063 0.0878  0.0044  0.0129  444 ALA   A N    
2978 C  CA   . ALA   A 417 ? 0.9118 1.1450 0.8198 0.0755  -0.0095 0.0024  444 ALA   A CA   
2979 C  C    . ALA   A 417 ? 0.9769 1.2030 0.8786 0.0661  -0.0218 -0.0344 444 ALA   A C    
2980 O  O    . ALA   A 417 ? 0.9419 1.1688 0.8409 0.0603  -0.0324 -0.0477 444 ALA   A O    
2981 C  CB   . ALA   A 417 ? 0.7544 0.9458 0.6921 0.0643  -0.0071 0.0146  444 ALA   A CB   
2982 N  N    . ARG   A 418 ? 0.9636 1.1821 0.8665 0.0647  -0.0187 -0.0512 445 ARG   A N    
2983 C  CA   . ARG   A 418 ? 0.8775 1.0846 0.7794 0.0564  -0.0262 -0.0854 445 ARG   A CA   
2984 C  C    . ARG   A 418 ? 0.8707 1.1202 0.7550 0.0613  -0.0322 -0.1082 445 ARG   A C    
2985 O  O    . ARG   A 418 ? 0.9226 1.1671 0.8121 0.0517  -0.0405 -0.1316 445 ARG   A O    
2986 C  CB   . ARG   A 418 ? 0.8564 1.0481 0.7644 0.0571  -0.0197 -0.0966 445 ARG   A CB   
2987 C  CG   . ARG   A 418 ? 0.9694 1.1393 0.8827 0.0490  -0.0233 -0.1287 445 ARG   A CG   
2988 C  CD   . ARG   A 418 ? 0.9604 1.1114 0.8819 0.0522  -0.0160 -0.1357 445 ARG   A CD   
2989 N  NE   . ARG   A 418 ? 1.0052 1.1361 0.9392 0.0537  -0.0130 -0.1113 445 ARG   A NE   
2990 C  CZ   . ARG   A 418 ? 0.8322 0.9597 0.7743 0.0599  -0.0063 -0.1096 445 ARG   A CZ   
2991 N  NH1  . ARG   A 418 ? 0.8470 0.9858 0.7843 0.0658  -0.0010 -0.1286 445 ARG   A NH1  
2992 N  NH2  . ARG   A 418 ? 0.8860 1.0012 0.8444 0.0602  -0.0051 -0.0912 445 ARG   A NH2  
2993 N  N    . GLN   A 419 ? 0.9631 1.2583 0.8281 0.0772  -0.0275 -0.1028 446 GLN   A N    
2994 C  CA   . GLN   A 419 ? 0.9957 1.3424 0.8422 0.0853  -0.0350 -0.1273 446 GLN   A CA   
2995 C  C    . GLN   A 419 ? 0.9266 1.2927 0.7692 0.0869  -0.0445 -0.1191 446 GLN   A C    
2996 O  O    . GLN   A 419 ? 0.9374 1.3265 0.7806 0.0826  -0.0556 -0.1500 446 GLN   A O    
2997 C  CB   . GLN   A 419 ? 1.0477 1.4432 0.8698 0.1063  -0.0267 -0.1197 446 GLN   A CB   
2998 C  CG   . GLN   A 419 ? 1.2278 1.6897 1.0259 0.1204  -0.0356 -0.1434 446 GLN   A CG   
2999 C  CD   . GLN   A 419 ? 1.3168 1.7861 1.1240 0.1095  -0.0447 -0.1978 446 GLN   A CD   
3000 O  OE1  . GLN   A 419 ? 1.2541 1.6771 1.0827 0.0939  -0.0411 -0.2147 446 GLN   A OE1  
3001 N  NE2  . GLN   A 419 ? 1.3026 1.8321 1.0961 0.1187  -0.0555 -0.2265 446 GLN   A NE2  
3002 N  N    . ASN   A 420 ? 0.9654 1.3234 0.8086 0.0929  -0.0394 -0.0795 447 ASN   A N    
3003 C  CA   . ASN   A 420 ? 0.9045 1.2800 0.7451 0.0966  -0.0473 -0.0687 447 ASN   A CA   
3004 C  C    . ASN   A 420 ? 0.9034 1.2447 0.7652 0.0760  -0.0573 -0.0883 447 ASN   A C    
3005 O  O    . ASN   A 420 ? 1.0420 1.4100 0.9032 0.0752  -0.0681 -0.1057 447 ASN   A O    
3006 C  CB   . ASN   A 420 ? 0.9199 1.2858 0.7627 0.1067  -0.0360 -0.0215 447 ASN   A CB   
3007 C  CG   . ASN   A 420 ? 1.0729 1.4812 0.8929 0.1313  -0.0235 0.0033  447 ASN   A CG   
3008 O  OD1  . ASN   A 420 ? 1.1530 1.6042 0.9510 0.1426  -0.0254 -0.0159 447 ASN   A OD1  
3009 N  ND2  . ASN   A 420 ? 1.2111 1.6082 1.0381 0.1405  -0.0087 0.0458  447 ASN   A ND2  
3010 N  N    . LEU   A 421 ? 0.8967 1.1823 0.7777 0.0608  -0.0532 -0.0860 448 LEU   A N    
3011 C  CA   . LEU   A 421 ? 0.9252 1.1769 0.8242 0.0435  -0.0595 -0.1000 448 LEU   A CA   
3012 C  C    . LEU   A 421 ? 0.8958 1.1516 0.8011 0.0334  -0.0638 -0.1417 448 LEU   A C    
3013 O  O    . LEU   A 421 ? 0.9485 1.1975 0.8674 0.0220  -0.0690 -0.1579 448 LEU   A O    
3014 C  CB   . LEU   A 421 ? 0.8767 1.0736 0.7911 0.0345  -0.0537 -0.0846 448 LEU   A CB   
3015 C  CG   . LEU   A 421 ? 0.9626 1.1465 0.8841 0.0373  -0.0513 -0.0519 448 LEU   A CG   
3016 C  CD1  . LEU   A 421 ? 0.9682 1.1180 0.9025 0.0348  -0.0440 -0.0386 448 LEU   A CD1  
3017 C  CD2  . LEU   A 421 ? 0.8689 1.0389 0.8000 0.0283  -0.0581 -0.0538 448 LEU   A CD2  
3018 N  N    . ARG   A 422 ? 0.8925 1.1591 0.7922 0.0369  -0.0599 -0.1605 449 ARG   A N    
3019 C  CA   . ARG   A 422 ? 0.9561 1.2261 0.8677 0.0269  -0.0616 -0.2035 449 ARG   A CA   
3020 C  C    . ARG   A 422 ? 1.0277 1.3549 0.9365 0.0298  -0.0722 -0.2294 449 ARG   A C    
3021 O  O    . ARG   A 422 ? 1.1359 1.4614 1.0665 0.0158  -0.0750 -0.2628 449 ARG   A O    
3022 C  CB   . ARG   A 422 ? 0.9229 1.1943 0.8299 0.0319  -0.0544 -0.2188 449 ARG   A CB   
3023 C  CG   . ARG   A 422 ? 0.9733 1.1854 0.8935 0.0250  -0.0449 -0.2102 449 ARG   A CG   
3024 C  CD   . ARG   A 422 ? 1.0107 1.2274 0.9269 0.0321  -0.0376 -0.2244 449 ARG   A CD   
3025 N  NE   . ARG   A 422 ? 0.9675 1.1300 0.8990 0.0270  -0.0292 -0.2211 449 ARG   A NE   
3026 C  CZ   . ARG   A 422 ? 0.9152 1.0703 0.8479 0.0330  -0.0214 -0.2297 449 ARG   A CZ   
3027 N  NH1  . ARG   A 422 ? 0.9388 1.1359 0.8587 0.0429  -0.0202 -0.2441 449 ARG   A NH1  
3028 N  NH2  . ARG   A 422 ? 1.0772 1.1843 1.0232 0.0312  -0.0145 -0.2234 449 ARG   A NH2  
3029 N  N    . ARG   A 423 ? 0.9523 1.3326 0.8365 0.0490  -0.0772 -0.2143 450 ARG   A N    
3030 C  CA   . ARG   A 423 ? 0.9745 1.4187 0.8533 0.0565  -0.0895 -0.2377 450 ARG   A CA   
3031 C  C    . ARG   A 423 ? 0.9696 1.4052 0.8651 0.0467  -0.0963 -0.2333 450 ARG   A C    
3032 O  O    . ARG   A 423 ? 1.0767 1.5414 0.9889 0.0388  -0.1050 -0.2694 450 ARG   A O    
3033 C  CB   . ARG   A 423 ? 1.0261 1.5293 0.8704 0.0846  -0.0912 -0.2150 450 ARG   A CB   
3034 C  CG   . ARG   A 423 ? 1.0797 1.6219 0.9060 0.0970  -0.0888 -0.2372 450 ARG   A CG   
3035 C  CD   . ARG   A 423 ? 1.2406 1.8543 1.0303 0.1283  -0.0912 -0.2182 450 ARG   A CD   
3036 N  NE   . ARG   A 423 ? 1.4475 2.1157 1.2195 0.1414  -0.0930 -0.2517 450 ARG   A NE   
3037 C  CZ   . ARG   A 423 ? 1.4148 2.1521 1.1818 0.1492  -0.1074 -0.2953 450 ARG   A CZ   
3038 N  NH1  . ARG   A 423 ? 1.2690 2.0311 1.0492 0.1449  -0.1214 -0.3111 450 ARG   A NH1  
3039 N  NH2  . ARG   A 423 ? 1.3839 2.1705 1.1342 0.1620  -0.1080 -0.3266 450 ARG   A NH2  
3040 N  N    . GLU   A 424 ? 0.8881 1.2862 0.7830 0.0468  -0.0920 -0.1920 451 GLU   A N    
3041 C  CA   . GLU   A 424 ? 0.9536 1.3409 0.8646 0.0380  -0.0971 -0.1866 451 GLU   A CA   
3042 C  C    . GLU   A 424 ? 1.0557 1.4028 0.9971 0.0135  -0.0945 -0.2155 451 GLU   A C    
3043 O  O    . GLU   A 424 ? 1.1960 1.5606 1.1561 0.0044  -0.1005 -0.2379 451 GLU   A O    
3044 C  CB   . GLU   A 424 ? 1.0402 1.3917 0.9473 0.0425  -0.0912 -0.1397 451 GLU   A CB   
3045 C  CG   . GLU   A 424 ? 1.2986 1.6091 1.2276 0.0264  -0.0914 -0.1360 451 GLU   A CG   
3046 C  CD   . GLU   A 424 ? 1.4714 1.7507 1.3995 0.0312  -0.0861 -0.0953 451 GLU   A CD   
3047 O  OE1  . GLU   A 424 ? 1.4970 1.8018 1.4119 0.0488  -0.0848 -0.0689 451 GLU   A OE1  
3048 O  OE2  . GLU   A 424 ? 1.3216 1.5522 1.2636 0.0183  -0.0819 -0.0903 451 GLU   A OE2  
3049 N  N    . TRP   A 425 ? 0.9216 1.2156 0.8699 0.0037  -0.0839 -0.2144 452 TRP   A N    
3050 C  CA   . TRP   A 425 ? 1.0322 1.2824 1.0084 -0.0164 -0.0769 -0.2352 452 TRP   A CA   
3051 C  C    . TRP   A 425 ? 1.0130 1.2921 1.0097 -0.0257 -0.0780 -0.2848 452 TRP   A C    
3052 O  O    . TRP   A 425 ? 0.9948 1.2640 1.0208 -0.0417 -0.0753 -0.3066 452 TRP   A O    
3053 C  CB   . TRP   A 425 ? 0.9046 1.0967 0.8806 -0.0193 -0.0652 -0.2202 452 TRP   A CB   
3054 C  CG   . TRP   A 425 ? 0.7304 0.8844 0.7016 -0.0180 -0.0630 -0.1827 452 TRP   A CG   
3055 C  CD1  . TRP   A 425 ? 0.7760 0.9243 0.7313 -0.0067 -0.0629 -0.1518 452 TRP   A CD1  
3056 C  CD2  . TRP   A 425 ? 0.7875 0.9071 0.7728 -0.0283 -0.0598 -0.1752 452 TRP   A CD2  
3057 N  NE1  . TRP   A 425 ? 0.7456 0.8600 0.7057 -0.0097 -0.0614 -0.1292 452 TRP   A NE1  
3058 C  CE2  . TRP   A 425 ? 0.7817 0.8787 0.7569 -0.0217 -0.0598 -0.1419 452 TRP   A CE2  
3059 C  CE3  . TRP   A 425 ? 0.7635 0.8707 0.7715 -0.0425 -0.0553 -0.1945 452 TRP   A CE3  
3060 C  CZ2  . TRP   A 425 ? 0.7144 0.7800 0.6969 -0.0270 -0.0573 -0.1283 452 TRP   A CZ2  
3061 C  CZ3  . TRP   A 425 ? 0.8399 0.9134 0.8543 -0.0476 -0.0507 -0.1768 452 TRP   A CZ3  
3062 C  CH2  . TRP   A 425 ? 0.7617 0.8162 0.7611 -0.0390 -0.0527 -0.1445 452 TRP   A CH2  
3063 N  N    . HIS   A 426 ? 1.0479 1.3642 1.0328 -0.0162 -0.0808 -0.3050 453 HIS   A N    
3064 C  CA   . HIS   A 426 ? 1.1108 1.4625 1.1180 -0.0243 -0.0830 -0.3585 453 HIS   A CA   
3065 C  C    . HIS   A 426 ? 1.1977 1.6114 1.2130 -0.0231 -0.0971 -0.3791 453 HIS   A C    
3066 O  O    . HIS   A 426 ? 1.2052 1.6355 1.2556 -0.0383 -0.0974 -0.4241 453 HIS   A O    
3067 C  CB   . HIS   A 426 ? 1.0478 1.4327 1.0368 -0.0112 -0.0839 -0.3759 453 HIS   A CB   
3068 C  CG   . HIS   A 426 ? 1.0905 1.5164 1.1042 -0.0186 -0.0866 -0.4363 453 HIS   A CG   
3069 N  ND1  . HIS   A 426 ? 1.2187 1.7279 1.2248 -0.0075 -0.1023 -0.4653 453 HIS   A ND1  
3070 C  CD2  . HIS   A 426 ? 1.1922 1.5891 1.2410 -0.0352 -0.0748 -0.4753 453 HIS   A CD2  
3071 C  CE1  . HIS   A 426 ? 1.3543 1.8870 1.3915 -0.0185 -0.1016 -0.5238 453 HIS   A CE1  
3072 N  NE2  . HIS   A 426 ? 1.2663 1.7288 1.3319 -0.0363 -0.0837 -0.5306 453 HIS   A NE2  
3073 N  N    . ALA   A 427 ? 1.1564 1.6054 1.1433 -0.0048 -0.1077 -0.3474 454 ALA   A N    
3074 C  CA   . ALA   A 427 ? 1.0070 1.5162 1.0004 -0.0003 -0.1218 -0.3624 454 ALA   A CA   
3075 C  C    . ALA   A 427 ? 1.1226 1.5962 1.1468 -0.0191 -0.1183 -0.3589 454 ALA   A C    
3076 O  O    . ALA   A 427 ? 1.2102 1.7238 1.2604 -0.0264 -0.1259 -0.3913 454 ALA   A O    
3077 C  CB   . ALA   A 427 ? 0.9583 1.5127 0.9119 0.0285  -0.1311 -0.3246 454 ALA   A CB   
3078 N  N    . ARG   A 428 ? 1.0853 1.4885 1.1080 -0.0261 -0.1068 -0.3218 455 ARG   A N    
3079 C  CA   . ARG   A 428 ? 1.1256 1.4929 1.1750 -0.0428 -0.1011 -0.3170 455 ARG   A CA   
3080 C  C    . ARG   A 428 ? 1.1189 1.4647 1.2112 -0.0667 -0.0900 -0.3588 455 ARG   A C    
3081 O  O    . ARG   A 428 ? 1.2422 1.5964 1.3663 -0.0801 -0.0889 -0.3771 455 ARG   A O    
3082 C  CB   . ARG   A 428 ? 1.1813 1.4828 1.2169 -0.0423 -0.0916 -0.2708 455 ARG   A CB   
3083 C  CG   . ARG   A 428 ? 1.0209 1.3360 1.0325 -0.0254 -0.0993 -0.2311 455 ARG   A CG   
3084 C  CD   . ARG   A 428 ? 1.1490 1.4021 1.1556 -0.0279 -0.0902 -0.1946 455 ARG   A CD   
3085 N  NE   . ARG   A 428 ? 0.9908 1.2151 1.0197 -0.0422 -0.0848 -0.1960 455 ARG   A NE   
3086 C  CZ   . ARG   A 428 ? 1.0269 1.2042 1.0536 -0.0443 -0.0780 -0.1695 455 ARG   A CZ   
3087 N  NH1  . ARG   A 428 ? 0.9818 1.1352 0.9895 -0.0348 -0.0764 -0.1423 455 ARG   A NH1  
3088 N  NH2  . ARG   A 428 ? 1.0002 1.1576 1.0460 -0.0557 -0.0721 -0.1723 455 ARG   A NH2  
3089 N  N    . CYS   A 429 ? 1.0994 1.4163 1.1967 -0.0720 -0.0794 -0.3740 456 CYS   A N    
3090 C  CA   . CYS   A 429 ? 1.2125 1.5013 1.3551 -0.0942 -0.0640 -0.4115 456 CYS   A CA   
3091 C  C    . CYS   A 429 ? 1.3229 1.6780 1.4972 -0.1018 -0.0724 -0.4690 456 CYS   A C    
3092 O  O    . CYS   A 429 ? 1.3273 1.6701 1.5509 -0.1232 -0.0605 -0.5026 456 CYS   A O    
3093 C  CB   . CYS   A 429 ? 1.2325 1.4725 1.3722 -0.0949 -0.0496 -0.4108 456 CYS   A CB   
3094 S  SG   . CYS   A 429 ? 1.1387 1.3055 1.2474 -0.0859 -0.0400 -0.3504 456 CYS   A SG   
3095 N  N    . GLN   A 430 ? 1.3392 1.7671 1.4882 -0.0836 -0.0917 -0.4817 457 GLN   A N    
3096 C  CA   . GLN   A 430 ? 1.3515 1.8544 1.5278 -0.0867 -0.1029 -0.5391 457 GLN   A CA   
3097 C  C    . GLN   A 430 ? 1.3332 1.9048 1.4944 -0.0698 -0.1220 -0.5288 457 GLN   A C    
3098 O  O    . GLN   A 430 ? 1.3122 1.9497 1.4487 -0.0463 -0.1348 -0.5318 457 GLN   A O    
3099 C  CB   . GLN   A 430 ? 1.3110 1.8434 1.4735 -0.0734 -0.1039 -0.5585 457 GLN   A CB   
3100 C  CG   . GLN   A 430 ? 1.3704 1.8556 1.5737 -0.0918 -0.0828 -0.5878 457 GLN   A CG   
3101 C  CD   . GLN   A 430 ? 1.5839 2.0958 1.7711 -0.0779 -0.0842 -0.6045 457 GLN   A CD   
3102 O  OE1  . GLN   A 430 ? 1.5557 2.1404 1.7201 -0.0570 -0.0993 -0.6109 457 GLN   A OE1  
3103 N  NE2  . GLN   A 430 ? 1.6594 2.1127 1.8588 -0.0875 -0.0670 -0.6102 457 GLN   A NE2  
3104 N  N    . SER   A 431 ? 1.2546 1.8111 1.4306 -0.0797 -0.1222 -0.5145 458 SER   A N    
3105 C  CA   . SER   A 431 ? 1.2748 1.8918 1.4452 -0.0653 -0.1378 -0.5068 458 SER   A CA   
3106 C  C    . SER   A 431 ? 1.3983 2.0269 1.6261 -0.0834 -0.1298 -0.5400 458 SER   A C    
3107 O  O    . SER   A 431 ? 1.4388 2.0159 1.7090 -0.1090 -0.1101 -0.5580 458 SER   A O    
3108 C  CB   . SER   A 431 ? 1.2419 1.8267 1.3817 -0.0552 -0.1394 -0.4486 458 SER   A CB   
3109 O  OG   . SER   A 431 ? 1.2108 1.7273 1.3786 -0.0771 -0.1226 -0.4358 458 SER   A OG   
3110 N  N    . ARG   A 432 ? 1.3909 2.0881 1.6203 -0.0680 -0.1431 -0.5463 459 ARG   A N    
3111 C  CA   . ARG   A 432 ? 1.3305 2.0506 1.6151 -0.0824 -0.1363 -0.5820 459 ARG   A CA   
3112 C  C    . ARG   A 432 ? 1.2055 1.8667 1.5221 -0.1078 -0.1222 -0.5713 459 ARG   A C    
3113 O  O    . ARG   A 432 ? 1.2310 1.8703 1.6012 -0.1306 -0.1037 -0.5997 459 ARG   A O    
3114 C  CB   . ARG   A 432 ? 1.3990 2.2045 1.6740 -0.0575 -0.1542 -0.5870 459 ARG   A CB   
3115 C  CG   . ARG   A 432 ? 1.3838 2.2561 1.6374 -0.0324 -0.1642 -0.6057 459 ARG   A CG   
3116 C  CD   . ARG   A 432 ? 1.3529 2.3042 1.5830 -0.0010 -0.1816 -0.5969 459 ARG   A CD   
3117 N  NE   . ARG   A 432 ? 1.3922 2.4174 1.6212 0.0190  -0.1877 -0.6298 459 ARG   A NE   
3118 C  CZ   . ARG   A 432 ? 1.4798 2.5485 1.7582 0.0111  -0.1845 -0.6826 459 ARG   A CZ   
3119 N  NH1  . ARG   A 432 ? 1.3409 2.3854 1.6747 -0.0168 -0.1737 -0.7076 459 ARG   A NH1  
3120 N  NH2  . ARG   A 432 ? 1.5735 2.7139 1.8476 0.0322  -0.1912 -0.7114 459 ARG   A NH2  
3121 N  N    . ILE   A 433 ? 1.0349 1.6707 1.3216 -0.1034 -0.1288 -0.5297 460 ILE   A N    
3122 C  CA   . ILE   A 433 ? 0.9933 1.5735 1.3081 -0.1261 -0.1144 -0.5176 460 ILE   A CA   
3123 C  C    . ILE   A 433 ? 1.1785 1.6762 1.5080 -0.1482 -0.0909 -0.5168 460 ILE   A C    
3124 O  O    . ILE   A 433 ? 1.1756 1.6237 1.5406 -0.1688 -0.0696 -0.5147 460 ILE   A O    
3125 C  CB   . ILE   A 433 ? 0.9198 1.4894 1.1966 -0.1099 -0.1233 -0.4654 460 ILE   A CB   
3126 C  CG1  . ILE   A 433 ? 0.8369 1.3679 1.1456 -0.1271 -0.1081 -0.4540 460 ILE   A CG1  
3127 C  CG2  . ILE   A 433 ? 1.0425 1.5529 1.2689 -0.0973 -0.1179 -0.4175 460 ILE   A CG2  
3128 C  CD1  . ILE   A 433 ? 0.8991 1.4394 1.1818 -0.1089 -0.1177 -0.4127 460 ILE   A CD1  
3129 N  N    . ALA   A 434 ? 1.2491 1.7268 1.5494 -0.1401 -0.0902 -0.5115 461 ALA   A N    
3130 C  CA   . ALA   A 434 ? 1.2763 1.6723 1.5848 -0.1539 -0.0657 -0.5023 461 ALA   A CA   
3131 C  C    . ALA   A 434 ? 1.3547 1.7407 1.7230 -0.1763 -0.0459 -0.5488 461 ALA   A C    
3132 O  O    . ALA   A 434 ? 1.3734 1.6882 1.7626 -0.1917 -0.0206 -0.5431 461 ALA   A O    
3133 C  CB   . ALA   A 434 ? 1.3666 1.7474 1.6269 -0.1361 -0.0706 -0.4810 461 ALA   A CB   
3134 N  N    . ARG   A 435 ? 1.3570 1.8084 1.7505 -0.1723 -0.0524 -0.5843 462 ARG   A N    
3135 C  CA   . ARG   A 435 ? 1.3247 1.7676 1.7779 -0.1892 -0.0299 -0.6217 462 ARG   A CA   
3136 C  C    . ARG   A 435 ? 1.2181 1.6450 1.7211 -0.2078 -0.0119 -0.6263 462 ARG   A C    
3137 O  O    . ARG   A 435 ? 1.2571 1.6415 1.8089 -0.2259 0.0168  -0.6402 462 ARG   A O    
3138 C  CB   . ARG   A 435 ? 1.3134 1.8372 1.7774 -0.1771 -0.0434 -0.6629 462 ARG   A CB   
3139 C  CG   . ARG   A 435 ? 1.3769 1.9395 1.7840 -0.1521 -0.0662 -0.6549 462 ARG   A CG   
3140 C  CD   . ARG   A 435 ? 1.4305 2.0326 1.8587 -0.1480 -0.0644 -0.6969 462 ARG   A CD   
3141 N  NE   . ARG   A 435 ? 1.5324 2.1433 1.9101 -0.1292 -0.0762 -0.6851 462 ARG   A NE   
3142 C  CZ   . ARG   A 435 ? 1.4551 2.1269 1.7835 -0.1022 -0.0996 -0.6723 462 ARG   A CZ   
3143 N  NH1  . ARG   A 435 ? 1.4115 2.1410 1.7321 -0.0890 -0.1149 -0.6687 462 ARG   A NH1  
3144 N  NH2  . ARG   A 435 ? 1.4408 2.1152 1.7269 -0.0864 -0.1057 -0.6610 462 ARG   A NH2  
3145 N  N    . THR   A 436 ? 1.1888 1.6490 1.6814 -0.2023 -0.0265 -0.6132 463 THR   A N    
3146 C  CA   . THR   A 436 ? 1.1716 1.6270 1.7122 -0.2182 -0.0106 -0.6204 463 THR   A CA   
3147 C  C    . THR   A 436 ? 1.2607 1.6283 1.8147 -0.2360 0.0180  -0.5905 463 THR   A C    
3148 O  O    . THR   A 436 ? 1.3262 1.6777 1.9276 -0.2515 0.0403  -0.5976 463 THR   A O    
3149 C  CB   . THR   A 436 ? 1.2190 1.7336 1.7423 -0.2051 -0.0343 -0.6118 463 THR   A CB   
3150 O  OG1  . THR   A 436 ? 1.2278 1.7017 1.7203 -0.2049 -0.0366 -0.5678 463 THR   A OG1  
3151 C  CG2  . THR   A 436 ? 1.1586 1.7490 1.6421 -0.1783 -0.0650 -0.6206 463 THR   A CG2  
3152 N  N    . LEU   A 437 ? 1.2971 1.6093 1.8108 -0.2325 0.0193  -0.5569 464 LEU   A N    
3153 C  CA   . LEU   A 437 ? 1.2538 1.4817 1.7775 -0.2456 0.0488  -0.5272 464 LEU   A CA   
3154 C  C    . LEU   A 437 ? 1.4193 1.6045 1.9912 -0.2589 0.0827  -0.5443 464 LEU   A C    
3155 O  O    . LEU   A 437 ? 1.3574 1.5653 1.9420 -0.2569 0.0806  -0.5745 464 LEU   A O    
3156 C  CB   . LEU   A 437 ? 1.3549 1.5352 1.8192 -0.2317 0.0433  -0.4842 464 LEU   A CB   
3157 C  CG   . LEU   A 437 ? 1.2584 1.4640 1.6633 -0.2082 0.0169  -0.4444 464 LEU   A CG   
3158 C  CD1  . LEU   A 437 ? 1.2434 1.4900 1.6055 -0.1889 -0.0098 -0.4471 464 LEU   A CD1  
3159 C  CD2  . LEU   A 437 ? 1.1478 1.2850 1.5167 -0.1988 0.0303  -0.3879 464 LEU   A CD2  
3160 N  N    . PRO   A 438 ? 1.6783 1.8035 2.2785 -0.2712 0.1159  -0.5243 465 PRO   A N    
3161 C  CA   . PRO   A 438 ? 1.5119 1.5914 2.1577 -0.2812 0.1518  -0.5342 465 PRO   A CA   
3162 C  C    . PRO   A 438 ? 1.4895 1.5215 2.1079 -0.2729 0.1569  -0.5210 465 PRO   A C    
3163 O  O    . PRO   A 438 ? 1.4566 1.4794 2.0203 -0.2606 0.1369  -0.4995 465 PRO   A O    
3164 C  CB   . PRO   A 438 ? 1.5118 1.5362 2.1800 -0.2903 0.1854  -0.5035 465 PRO   A CB   
3165 C  CG   . PRO   A 438 ? 1.5029 1.5331 2.1302 -0.2847 0.1672  -0.4738 465 PRO   A CG   
3166 C  CD   . PRO   A 438 ? 1.4766 1.5798 2.0717 -0.2749 0.1233  -0.4927 465 PRO   A CD   
3167 N  N    . ALA   A 439 ? 1.5368 1.5386 2.1974 -0.2795 0.1856  -0.5349 466 ALA   A N    
3168 C  CA   . ALA   A 439 ? 1.4073 1.3782 2.0512 -0.2713 0.1888  -0.5335 466 ALA   A CA   
3169 C  C    . ALA   A 439 ? 1.4101 1.3057 2.0092 -0.2603 0.2000  -0.4824 466 ALA   A C    
3170 O  O    . ALA   A 439 ? 1.4828 1.3641 2.0459 -0.2484 0.1889  -0.4761 466 ALA   A O    
3171 C  CB   . ALA   A 439 ? 1.0356 0.9924 1.7420 -0.2812 0.2198  -0.5604 466 ALA   A CB   
3172 N  N    . ASP   A 440 ? 1.4810 1.3303 2.0811 -0.2619 0.2223  -0.4459 467 ASP   A N    
3173 C  CA   . ASP   A 440 ? 1.5817 1.3587 2.1420 -0.2479 0.2373  -0.3963 467 ASP   A CA   
3174 C  C    . ASP   A 440 ? 1.6567 1.4445 2.1512 -0.2333 0.2064  -0.3699 467 ASP   A C    
3175 O  O    . ASP   A 440 ? 1.6784 1.4225 2.1271 -0.2125 0.2122  -0.3218 467 ASP   A O    
3176 C  CB   . ASP   A 440 ? 1.6957 1.4209 2.2792 -0.2499 0.2768  -0.3627 467 ASP   A CB   
3177 C  CG   . ASP   A 440 ? 1.9212 1.5978 2.5389 -0.2475 0.3149  -0.3562 467 ASP   A CG   
3178 O  OD1  . ASP   A 440 ? 2.0458 1.7475 2.7024 -0.2561 0.3156  -0.3960 467 ASP   A OD1  
3179 O  OD2  . ASP   A 440 ? 1.8979 1.5139 2.5034 -0.2352 0.3445  -0.3107 467 ASP   A OD2  
3180 N  N    . GLN   A 441 ? 1.6040 1.4620 2.0828 -0.2340 0.1710  -0.3895 468 GLN   A N    
3181 C  CA   . GLN   A 441 ? 1.5584 1.4395 1.9673 -0.2110 0.1387  -0.3565 468 GLN   A CA   
3182 C  C    . GLN   A 441 ? 1.5267 1.4761 1.9208 -0.2076 0.1042  -0.3881 468 GLN   A C    
3183 O  O    . GLN   A 441 ? 1.4957 1.4826 1.8476 -0.1938 0.0767  -0.3708 468 GLN   A O    
3184 C  CB   . GLN   A 441 ? 1.5859 1.4769 1.9775 -0.2072 0.1334  -0.3277 468 GLN   A CB   
3185 C  CG   . GLN   A 441 ? 1.6546 1.5928 2.0927 -0.2265 0.1313  -0.3611 468 GLN   A CG   
3186 C  CD   . GLN   A 441 ? 1.6296 1.5368 2.0842 -0.2320 0.1560  -0.3360 468 GLN   A CD   
3187 O  OE1  . GLN   A 441 ? 1.5395 1.3939 1.9640 -0.2187 0.1721  -0.2923 468 GLN   A OE1  
3188 N  NE2  . GLN   A 441 ? 1.4546 1.3988 1.9549 -0.2495 0.1584  -0.3632 468 GLN   A NE2  
3189 N  N    . LYS   A 442 ? 1.4850 1.4519 1.9141 -0.2186 0.1066  -0.4343 469 LYS   A N    
3190 C  CA   . LYS   A 442 ? 1.4481 1.4802 1.8571 -0.2110 0.0755  -0.4625 469 LYS   A CA   
3191 C  C    . LYS   A 442 ? 1.4563 1.4701 1.8052 -0.1878 0.0637  -0.4279 469 LYS   A C    
3192 O  O    . LYS   A 442 ? 1.4452 1.4012 1.7910 -0.1838 0.0830  -0.4113 469 LYS   A O    
3193 C  CB   . LYS   A 442 ? 1.5365 1.5951 1.9954 -0.2240 0.0824  -0.5176 469 LYS   A CB   
3194 C  CG   . LYS   A 442 ? 1.6891 1.7997 2.1959 -0.2356 0.0834  -0.5476 469 LYS   A CG   
3195 C  CD   . LYS   A 442 ? 1.5491 1.7513 2.0424 -0.2254 0.0504  -0.5785 469 LYS   A CD   
3196 C  CE   . LYS   A 442 ? 1.5299 1.7548 2.0315 -0.2204 0.0490  -0.6102 469 LYS   A CE   
3197 N  NZ   . LYS   A 442 ? 1.4532 1.7714 1.9439 -0.2078 0.0203  -0.6401 469 LYS   A NZ   
3198 N  N    . PRO   A 443 ? 1.3303 1.3914 1.6335 -0.1713 0.0343  -0.4151 470 PRO   A N    
3199 C  CA   . PRO   A 443 ? 1.2459 1.2905 1.4971 -0.1506 0.0250  -0.3818 470 PRO   A CA   
3200 C  C    . PRO   A 443 ? 1.2062 1.2460 1.4639 -0.1495 0.0299  -0.4078 470 PRO   A C    
3201 O  O    . PRO   A 443 ? 1.1869 1.2754 1.4653 -0.1555 0.0217  -0.4533 470 PRO   A O    
3202 C  CB   . PRO   A 443 ? 1.1360 1.2412 1.3505 -0.1363 -0.0043 -0.3716 470 PRO   A CB   
3203 C  CG   . PRO   A 443 ? 1.0736 1.2102 1.3125 -0.1464 -0.0084 -0.3826 470 PRO   A CG   
3204 C  CD   . PRO   A 443 ? 1.3274 1.4574 1.6260 -0.1694 0.0105  -0.4262 470 PRO   A CD   
3205 N  N    . GLU   A 444 ? 1.1783 1.1623 1.4189 -0.1403 0.0431  -0.3802 471 GLU   A N    
3206 C  CA   . GLU   A 444 ? 1.2200 1.1963 1.4598 -0.1350 0.0471  -0.3976 471 GLU   A CA   
3207 C  C    . GLU   A 444 ? 1.2240 1.2228 1.4107 -0.1139 0.0265  -0.3719 471 GLU   A C    
3208 O  O    . GLU   A 444 ? 1.1701 1.1488 1.3245 -0.1023 0.0221  -0.3286 471 GLU   A O    
3209 C  CB   . GLU   A 444 ? 1.2486 1.1506 1.5072 -0.1361 0.0767  -0.3843 471 GLU   A CB   
3210 C  CG   . GLU   A 444 ? 1.4224 1.3162 1.7012 -0.1368 0.0867  -0.4168 471 GLU   A CG   
3211 C  CD   . GLU   A 444 ? 1.4691 1.2897 1.7528 -0.1288 0.1132  -0.3917 471 GLU   A CD   
3212 O  OE1  . GLU   A 444 ? 1.5857 1.3671 1.8500 -0.1197 0.1211  -0.3469 471 GLU   A OE1  
3213 O  OE2  . GLU   A 444 ? 1.4200 1.2248 1.7266 -0.1296 0.1261  -0.4173 471 GLU   A OE2  
3214 N  N    . CYS   A 445 ? 1.1860 1.2285 1.3662 -0.1090 0.0151  -0.4002 472 CYS   A N    
3215 C  CA   . CYS   A 445 ? 1.1345 1.2030 1.2685 -0.0894 -0.0015 -0.3779 472 CYS   A CA   
3216 C  C    . CYS   A 445 ? 1.2846 1.3068 1.4072 -0.0795 0.0101  -0.3605 472 CYS   A C    
3217 O  O    . CYS   A 445 ? 1.4254 1.4699 1.5327 -0.0693 0.0048  -0.3702 472 CYS   A O    
3218 C  CB   . CYS   A 445 ? 1.1214 1.2632 1.2496 -0.0849 -0.0180 -0.4134 472 CYS   A CB   
3219 S  SG   . CYS   A 445 ? 1.1407 1.3268 1.2129 -0.0602 -0.0376 -0.3807 472 CYS   A SG   
3220 N  N    . ARG   A 446 ? 1.2012 1.1621 1.3303 -0.0802 0.0264  -0.3341 473 ARG   A N    
3221 C  CA   . ARG   A 446 ? 1.0887 1.0053 1.2096 -0.0685 0.0383  -0.3166 473 ARG   A CA   
3222 C  C    . ARG   A 446 ? 1.1182 1.0430 1.1973 -0.0509 0.0241  -0.2790 473 ARG   A C    
3223 O  O    . ARG   A 446 ? 1.0870 1.0173 1.1493 -0.0488 0.0146  -0.2526 473 ARG   A O    
3224 C  CB   . ARG   A 446 ? 1.1214 0.9737 1.2632 -0.0719 0.0619  -0.3001 473 ARG   A CB   
3225 C  CG   . ARG   A 446 ? 1.1286 0.9357 1.2833 -0.0642 0.0820  -0.3018 473 ARG   A CG   
3226 C  CD   . ARG   A 446 ? 1.2139 0.9636 1.4026 -0.0713 0.1110  -0.2968 473 ARG   A CD   
3227 N  NE   . ARG   A 446 ? 1.2708 0.9688 1.4576 -0.0546 0.1298  -0.2751 473 ARG   A NE   
3228 C  CZ   . ARG   A 446 ? 1.3984 1.0399 1.6123 -0.0544 0.1599  -0.2645 473 ARG   A CZ   
3229 N  NH1  . ARG   A 446 ? 1.3218 0.9486 1.5703 -0.0724 0.1764  -0.2744 473 ARG   A NH1  
3230 N  NH2  . ARG   A 446 ? 1.5015 1.1011 1.7093 -0.0343 0.1753  -0.2420 473 ARG   A NH2  
3231 N  N    . PRO   A 447 ? 1.1002 1.0268 1.1659 -0.0385 0.0234  -0.2779 474 PRO   A N    
3232 C  CA   . PRO   A 447 ? 1.1817 1.1043 1.2669 -0.0395 0.0343  -0.3107 474 PRO   A CA   
3233 C  C    . PRO   A 447 ? 1.2087 1.1930 1.2906 -0.0414 0.0218  -0.3453 474 PRO   A C    
3234 O  O    . PRO   A 447 ? 1.1311 1.1583 1.1840 -0.0331 0.0053  -0.3318 474 PRO   A O    
3235 C  CB   . PRO   A 447 ? 1.0627 0.9600 1.1308 -0.0220 0.0383  -0.2868 474 PRO   A CB   
3236 C  CG   . PRO   A 447 ? 1.0080 0.9253 1.0441 -0.0125 0.0221  -0.2521 474 PRO   A CG   
3237 C  CD   . PRO   A 447 ? 1.0682 0.9989 1.1029 -0.0227 0.0137  -0.2446 474 PRO   A CD   
3238 N  N    . TYR   A 448 ? 1.1749 1.1649 1.2880 -0.0512 0.0309  -0.3899 475 TYR   A N    
3239 C  CA   . TYR   A 448 ? 1.1687 1.2234 1.2807 -0.0517 0.0191  -0.4297 475 TYR   A CA   
3240 C  C    . TYR   A 448 ? 1.2212 1.2669 1.3576 -0.0523 0.0324  -0.4684 475 TYR   A C    
3241 O  O    . TYR   A 448 ? 1.1643 1.1581 1.3379 -0.0618 0.0531  -0.4806 475 TYR   A O    
3242 C  CB   . TYR   A 448 ? 1.2544 1.3460 1.3873 -0.0668 0.0116  -0.4585 475 TYR   A CB   
3243 C  CG   . TYR   A 448 ? 1.3255 1.4983 1.4468 -0.0616 -0.0061 -0.4931 475 TYR   A CG   
3244 C  CD1  . TYR   A 448 ? 1.2615 1.4813 1.3376 -0.0444 -0.0238 -0.4665 475 TYR   A CD1  
3245 C  CD2  . TYR   A 448 ? 1.2524 1.4568 1.4094 -0.0725 -0.0039 -0.5530 475 TYR   A CD2  
3246 C  CE1  . TYR   A 448 ? 1.2723 1.5698 1.3332 -0.0349 -0.0387 -0.4943 475 TYR   A CE1  
3247 C  CE2  . TYR   A 448 ? 1.2565 1.5432 1.3997 -0.0643 -0.0216 -0.5866 475 TYR   A CE2  
3248 C  CZ   . TYR   A 448 ? 1.2673 1.6010 1.3594 -0.0439 -0.0390 -0.5549 475 TYR   A CZ   
3249 O  OH   . TYR   A 448 ? 1.1860 1.6049 1.2600 -0.0312 -0.0554 -0.5845 475 TYR   A OH   
3250 N  N    . TRP   A 449 ? 1.2486 1.3445 1.3648 -0.0409 0.0226  -0.4867 476 TRP   A N    
3251 C  CA   . TRP   A 449 ? 1.2732 1.3674 1.4096 -0.0393 0.0339  -0.5255 476 TRP   A CA   
3252 C  C    . TRP   A 449 ? 1.2999 1.4753 1.4193 -0.0317 0.0185  -0.5618 476 TRP   A C    
3253 O  O    . TRP   A 449 ? 1.2793 1.5044 1.3596 -0.0203 0.0012  -0.5407 476 TRP   A O    
3254 C  CB   . TRP   A 449 ? 1.3036 1.3541 1.4261 -0.0244 0.0444  -0.4948 476 TRP   A CB   
3255 C  CG   . TRP   A 449 ? 1.3231 1.4095 1.3989 -0.0061 0.0304  -0.4632 476 TRP   A CG   
3256 C  CD1  . TRP   A 449 ? 1.3205 1.4483 1.3781 0.0073  0.0271  -0.4777 476 TRP   A CD1  
3257 C  CD2  . TRP   A 449 ? 1.2633 1.3471 1.3090 0.0004  0.0205  -0.4125 476 TRP   A CD2  
3258 N  NE1  . TRP   A 449 ? 1.1820 1.3311 1.2016 0.0212  0.0176  -0.4366 476 TRP   A NE1  
3259 C  CE2  . TRP   A 449 ? 1.1736 1.2957 1.1874 0.0166  0.0133  -0.3978 476 TRP   A CE2  
3260 C  CE3  . TRP   A 449 ? 1.1875 1.2408 1.2323 -0.0058 0.0184  -0.3797 476 TRP   A CE3  
3261 C  CZ2  . TRP   A 449 ? 1.1784 1.3065 1.1652 0.0250  0.0054  -0.3527 476 TRP   A CZ2  
3262 C  CZ3  . TRP   A 449 ? 1.1737 1.2354 1.1890 0.0033  0.0083  -0.3374 476 TRP   A CZ3  
3263 C  CH2  . TRP   A 449 ? 1.0975 1.1951 1.0868 0.0177  0.0025  -0.3248 476 TRP   A CH2  
3264 N  N    . GLU   A 450 ? 1.3030 1.4921 1.4529 -0.0367 0.0263  -0.6165 477 GLU   A N    
3265 C  CA   . GLU   A 450 ? 1.3453 1.6147 1.4823 -0.0273 0.0126  -0.6451 477 GLU   A CA   
3266 C  C    . GLU   A 450 ? 1.2904 1.5707 1.3958 -0.0072 0.0147  -0.6400 477 GLU   A C    
3267 O  O    . GLU   A 450 ? 1.3874 1.6103 1.4934 -0.0029 0.0287  -0.6197 477 GLU   A O    
3268 C  CB   . GLU   A 450 ? 1.3038 1.5885 1.4960 -0.0418 0.0191  -0.6879 477 GLU   A CB   
3269 C  CG   . GLU   A 450 ? 1.1982 1.4861 1.4267 -0.0609 0.0178  -0.6976 477 GLU   A CG   
3270 C  CD   . GLU   A 450 ? 1.3563 1.7174 1.5552 -0.0535 -0.0061 -0.6933 477 GLU   A CD   
3271 O  OE1  . GLU   A 450 ? 1.2926 1.7139 1.4496 -0.0334 -0.0210 -0.6903 477 GLU   A OE1  
3272 O  OE2  . GLU   A 450 ? 1.3668 1.7254 1.5846 -0.0663 -0.0086 -0.6903 477 GLU   A OE2  
3273 N  N    . LYS   A 451 ? 1.2832 1.6404 1.3622 0.0071  0.0011  -0.6513 478 LYS   A N    
3274 C  CA   . LYS   A 451 ? 1.4844 1.8599 1.5402 0.0254  0.0051  -0.6525 478 LYS   A CA   
3275 C  C    . LYS   A 451 ? 1.5727 1.9088 1.6723 0.0178  0.0224  -0.6812 478 LYS   A C    
3276 O  O    . LYS   A 451 ? 1.4586 1.7807 1.5464 0.0305  0.0315  -0.6766 478 LYS   A O    
3277 C  CB   . LYS   A 451 ? 1.5379 2.0057 1.5640 0.0420  -0.0106 -0.6614 478 LYS   A CB   
3278 C  CG   . LYS   A 451 ? 1.6291 2.1418 1.6218 0.0489  -0.0274 -0.6365 478 LYS   A CG   
3279 C  CD   . LYS   A 451 ? 1.6380 2.2218 1.5798 0.0761  -0.0357 -0.6177 478 LYS   A CD   
3280 C  CE   . LYS   A 451 ? 1.6639 2.2822 1.5713 0.0856  -0.0487 -0.5834 478 LYS   A CE   
3281 N  NZ   . LYS   A 451 ? 1.5710 2.1933 1.4273 0.1056  -0.0442 -0.5366 478 LYS   A NZ   
3282 N  N    . ASP   A 452 ? 1.6885 2.0082 1.8406 -0.0019 0.0283  -0.7098 479 ASP   A N    
3283 C  CA   . ASP   A 452 ? 1.7929 2.0648 1.9929 -0.0109 0.0484  -0.7328 479 ASP   A CA   
3284 C  C    . ASP   A 452 ? 1.7631 1.9493 1.9630 -0.0081 0.0666  -0.7015 479 ASP   A C    
3285 O  O    . ASP   A 452 ? 1.5978 1.7577 1.8043 0.0008  0.0796  -0.7047 479 ASP   A O    
3286 C  CB   . ASP   A 452 ? 1.7605 2.0282 2.0191 -0.0339 0.0538  -0.7621 479 ASP   A CB   
3287 C  CG   . ASP   A 452 ? 1.9043 2.1019 2.2187 -0.0466 0.0803  -0.7743 479 ASP   A CG   
3288 O  OD1  . ASP   A 452 ? 1.8916 2.0501 2.2031 -0.0366 0.0935  -0.7671 479 ASP   A OD1  
3289 O  OD2  . ASP   A 452 ? 1.9707 2.1567 2.3360 -0.0660 0.0892  -0.7925 479 ASP   A OD2  
3290 N  N    . ASP   A 453 ? 1.6461 1.7913 1.8384 -0.0134 0.0674  -0.6705 480 ASP   A N    
3291 C  CA   . ASP   A 453 ? 1.5770 1.6393 1.7779 -0.0108 0.0860  -0.6412 480 ASP   A CA   
3292 C  C    . ASP   A 453 ? 1.5276 1.5850 1.6975 0.0115  0.0883  -0.6218 480 ASP   A C    
3293 O  O    . ASP   A 453 ? 1.4531 1.5472 1.5777 0.0237  0.0728  -0.5884 480 ASP   A O    
3294 C  CB   . ASP   A 453 ? 1.4808 1.5165 1.6688 -0.0168 0.0810  -0.6029 480 ASP   A CB   
3295 C  CG   . ASP   A 453 ? 1.4868 1.4368 1.6982 -0.0186 0.1021  -0.5707 480 ASP   A CG   
3296 O  OD1  . ASP   A 453 ? 1.4557 1.3707 1.6634 -0.0036 0.1132  -0.5517 480 ASP   A OD1  
3297 O  OD2  . ASP   A 453 ? 1.5027 1.4231 1.7358 -0.0331 0.1083  -0.5637 480 ASP   A OD2  
3298 N  N    . ALA   A 454 ? 1.5390 1.5519 1.7357 0.0167  0.1077  -0.6297 481 ALA   A N    
3299 C  CA   . ALA   A 454 ? 1.3991 1.4047 1.5742 0.0382  0.1118  -0.6089 481 ALA   A CA   
3300 C  C    . ALA   A 454 ? 1.4314 1.3767 1.5992 0.0471  0.1183  -0.5505 481 ALA   A C    
3301 O  O    . ALA   A 454 ? 1.5058 1.4524 1.6522 0.0651  0.1172  -0.5235 481 ALA   A O    
3302 C  CB   . ALA   A 454 ? 1.3147 1.3104 1.5204 0.0417  0.1271  -0.6416 481 ALA   A CB   
3303 N  N    . SER   A 455 ? 1.3754 1.2718 1.5614 0.0362  0.1254  -0.5318 482 SER   A N    
3304 C  CA   . SER   A 455 ? 1.3764 1.2244 1.5505 0.0475  0.1292  -0.4765 482 SER   A CA   
3305 C  C    . SER   A 455 ? 1.2843 1.1684 1.4135 0.0528  0.1067  -0.4365 482 SER   A C    
3306 O  O    . SER   A 455 ? 1.2126 1.0784 1.3253 0.0675  0.1051  -0.3962 482 SER   A O    
3307 C  CB   . SER   A 455 ? 1.3321 1.1216 1.5359 0.0360  0.1449  -0.4670 482 SER   A CB   
3308 O  OG   . SER   A 455 ? 1.4042 1.2188 1.6040 0.0175  0.1325  -0.4718 482 SER   A OG   
3309 N  N    . MET   A 456 ? 1.3716 1.3083 1.4834 0.0422  0.0898  -0.4479 483 MET   A N    
3310 C  CA   . MET   A 456 ? 1.2340 1.2070 1.3072 0.0475  0.0712  -0.4125 483 MET   A CA   
3311 C  C    . MET   A 456 ? 1.2486 1.2677 1.2994 0.0621  0.0662  -0.4147 483 MET   A C    
3312 O  O    . MET   A 456 ? 1.2080 1.2623 1.2622 0.0628  0.0679  -0.4536 483 MET   A O    
3313 C  CB   . MET   A 456 ? 1.1961 1.2065 1.2602 0.0334  0.0572  -0.4205 483 MET   A CB   
3314 C  CG   . MET   A 456 ? 1.2681 1.2430 1.3410 0.0214  0.0568  -0.3992 483 MET   A CG   
3315 S  SD   . MET   A 456 ? 1.3286 1.2430 1.3967 0.0314  0.0631  -0.3468 483 MET   A SD   
3316 C  CE   . MET   A 456 ? 1.3178 1.1660 1.4276 0.0296  0.0898  -0.3641 483 MET   A CE   
3317 N  N    . PRO   A 457 ? 1.0971 1.1196 1.1272 0.0739  0.0610  -0.3753 484 PRO   A N    
3318 C  CA   . PRO   A 457 ? 1.1376 1.2046 1.1491 0.0872  0.0591  -0.3743 484 PRO   A CA   
3319 C  C    . PRO   A 457 ? 1.1463 1.2736 1.1298 0.0862  0.0471  -0.3699 484 PRO   A C    
3320 O  O    . PRO   A 457 ? 0.9713 1.1416 0.9390 0.0974  0.0484  -0.3735 484 PRO   A O    
3321 C  CB   . PRO   A 457 ? 1.0003 1.0437 1.0096 0.0987  0.0601  -0.3348 484 PRO   A CB   
3322 C  CG   . PRO   A 457 ? 1.0780 1.0893 1.0880 0.0904  0.0539  -0.3079 484 PRO   A CG   
3323 C  CD   . PRO   A 457 ? 1.0677 1.0541 1.0945 0.0764  0.0584  -0.3329 484 PRO   A CD   
3324 N  N    . LEU   A 458 ? 1.0490 1.1816 1.0258 0.0751  0.0370  -0.3603 485 LEU   A N    
3325 C  CA   . LEU   A 458 ? 0.9944 1.1811 0.9444 0.0771  0.0265  -0.3495 485 LEU   A CA   
3326 C  C    . LEU   A 458 ? 1.0774 1.2810 1.0305 0.0649  0.0182  -0.3742 485 LEU   A C    
3327 O  O    . LEU   A 458 ? 1.1549 1.3175 1.1305 0.0516  0.0195  -0.3814 485 LEU   A O    
3328 C  CB   . LEU   A 458 ? 1.1202 1.2983 1.0590 0.0789  0.0217  -0.3009 485 LEU   A CB   
3329 C  CG   . LEU   A 458 ? 1.0131 1.1986 0.9469 0.0917  0.0282  -0.2765 485 LEU   A CG   
3330 C  CD1  . LEU   A 458 ? 0.9293 1.1026 0.8623 0.0900  0.0240  -0.2350 485 LEU   A CD1  
3331 C  CD2  . LEU   A 458 ? 0.8678 1.1114 0.7813 0.1037  0.0320  -0.2849 485 LEU   A CD2  
3332 N  N    . PRO   A 459 ? 1.1006 1.3669 1.0323 0.0706  0.0103  -0.3873 486 PRO   A N    
3333 C  CA   . PRO   A 459 ? 1.0291 1.3216 0.9655 0.0607  0.0005  -0.4146 486 PRO   A CA   
3334 C  C    . PRO   A 459 ? 1.0247 1.3018 0.9573 0.0529  -0.0078 -0.3806 486 PRO   A C    
3335 O  O    . PRO   A 459 ? 1.0292 1.2827 0.9527 0.0562  -0.0069 -0.3370 486 PRO   A O    
3336 C  CB   . PRO   A 459 ? 0.9495 1.3213 0.8574 0.0760  -0.0059 -0.4323 486 PRO   A CB   
3337 C  CG   . PRO   A 459 ? 1.0281 1.4104 0.9096 0.0925  -0.0003 -0.3902 486 PRO   A CG   
3338 C  CD   . PRO   A 459 ? 1.0279 1.3477 0.9297 0.0886  0.0110  -0.3753 486 PRO   A CD   
3339 N  N    . PHE   A 460 ? 1.0979 1.3911 1.0414 0.0420  -0.0159 -0.4046 487 PHE   A N    
3340 C  CA   . PHE   A 460 ? 1.0166 1.3018 0.9568 0.0355  -0.0242 -0.3762 487 PHE   A CA   
3341 C  C    . PHE   A 460 ? 1.1185 1.4614 1.0246 0.0507  -0.0340 -0.3523 487 PHE   A C    
3342 O  O    . PHE   A 460 ? 1.0031 1.3325 0.8996 0.0523  -0.0363 -0.3110 487 PHE   A O    
3343 C  CB   . PHE   A 460 ? 1.0459 1.3264 1.0151 0.0179  -0.0274 -0.4103 487 PHE   A CB   
3344 C  CG   . PHE   A 460 ? 1.1113 1.3843 1.0794 0.0109  -0.0352 -0.3841 487 PHE   A CG   
3345 C  CD1  . PHE   A 460 ? 1.1002 1.3099 1.0830 0.0006  -0.0286 -0.3583 487 PHE   A CD1  
3346 C  CD2  . PHE   A 460 ? 1.0548 1.3870 1.0060 0.0174  -0.0490 -0.3848 487 PHE   A CD2  
3347 C  CE1  . PHE   A 460 ? 0.9675 1.1717 0.9496 -0.0052 -0.0352 -0.3361 487 PHE   A CE1  
3348 C  CE2  . PHE   A 460 ? 1.0739 1.3990 1.0260 0.0119  -0.0555 -0.3612 487 PHE   A CE2  
3349 C  CZ   . PHE   A 460 ? 1.0448 1.3052 1.0130 -0.0003 -0.0484 -0.3378 487 PHE   A CZ   
3350 N  N    . ASP   A 461 ? 1.0345 1.4428 0.9227 0.0638  -0.0385 -0.3776 488 ASP   A N    
3351 C  CA   . ASP   A 461 ? 1.0492 1.5163 0.9016 0.0837  -0.0447 -0.3524 488 ASP   A CA   
3352 C  C    . ASP   A 461 ? 1.1326 1.5980 0.9649 0.0991  -0.0329 -0.3188 488 ASP   A C    
3353 O  O    . ASP   A 461 ? 1.1800 1.6582 1.0093 0.1059  -0.0260 -0.3401 488 ASP   A O    
3354 C  CB   . ASP   A 461 ? 1.1147 1.6604 0.9544 0.0946  -0.0550 -0.3951 488 ASP   A CB   
3355 C  CG   . ASP   A 461 ? 1.1604 1.7674 0.9652 0.1158  -0.0634 -0.3675 488 ASP   A CG   
3356 O  OD1  . ASP   A 461 ? 1.1281 1.7190 0.9161 0.1252  -0.0564 -0.3140 488 ASP   A OD1  
3357 O  OD2  . ASP   A 461 ? 1.3548 2.0280 1.1514 0.1242  -0.0761 -0.4001 488 ASP   A OD2  
3358 N  N    . LEU   A 462 ? 1.1658 1.6157 0.9883 0.1039  -0.0294 -0.2683 489 LEU   A N    
3359 C  CA   . LEU   A 462 ? 1.1804 1.6239 0.9928 0.1154  -0.0158 -0.2336 489 LEU   A CA   
3360 C  C    . LEU   A 462 ? 1.2834 1.7864 1.0628 0.1392  -0.0114 -0.2073 489 LEU   A C    
3361 O  O    . LEU   A 462 ? 1.1762 1.6731 0.9509 0.1481  0.0025  -0.1701 489 LEU   A O    
3362 C  CB   . LEU   A 462 ? 1.0577 1.4410 0.8896 0.1040  -0.0114 -0.1968 489 LEU   A CB   
3363 C  CG   . LEU   A 462 ? 1.0317 1.3532 0.8914 0.0886  -0.0089 -0.2063 489 LEU   A CG   
3364 C  CD1  . LEU   A 462 ? 1.2035 1.5125 1.0776 0.0773  -0.0140 -0.2512 489 LEU   A CD1  
3365 C  CD2  . LEU   A 462 ? 0.8782 1.1554 0.7527 0.0784  -0.0110 -0.1759 489 LEU   A CD2  
3366 N  N    . THR   A 463 ? 1.2881 1.8508 1.0464 0.1510  -0.0218 -0.2256 490 THR   A N    
3367 C  CA   . THR   A 463 ? 1.3161 1.9373 1.0394 0.1782  -0.0169 -0.1949 490 THR   A CA   
3368 C  C    . THR   A 463 ? 1.3366 1.9889 1.0395 0.1969  -0.0018 -0.1906 490 THR   A C    
3369 O  O    . THR   A 463 ? 1.3139 1.9787 1.0008 0.2140  0.0140  -0.1452 490 THR   A O    
3370 C  CB   . THR   A 463 ? 1.5225 2.2089 1.2269 0.1897  -0.0336 -0.2211 490 THR   A CB   
3371 O  OG1  . THR   A 463 ? 1.4601 2.1172 1.1863 0.1718  -0.0460 -0.2235 490 THR   A OG1  
3372 C  CG2  . THR   A 463 ? 1.4424 2.1915 1.1070 0.2228  -0.0276 -0.1840 490 THR   A CG2  
3373 N  N    . ASP   A 464 ? 1.3090 1.9733 1.0152 0.1940  -0.0040 -0.2375 491 ASP   A N    
3374 C  CA   . ASP   A 464 ? 1.3696 2.0648 1.0571 0.2119  0.0107  -0.2370 491 ASP   A CA   
3375 C  C    . ASP   A 464 ? 1.3038 1.9459 1.0100 0.2054  0.0291  -0.2004 491 ASP   A C    
3376 O  O    . ASP   A 464 ? 1.2429 1.9099 0.9323 0.2235  0.0467  -0.1731 491 ASP   A O    
3377 C  CB   . ASP   A 464 ? 1.2937 2.0080 0.9872 0.2082  0.0044  -0.2996 491 ASP   A CB   
3378 C  CG   . ASP   A 464 ? 1.3382 2.1196 1.0152 0.2171  -0.0131 -0.3427 491 ASP   A CG   
3379 O  OD1  . ASP   A 464 ? 1.3460 2.1822 0.9913 0.2384  -0.0170 -0.3198 491 ASP   A OD1  
3380 O  OD2  . ASP   A 464 ? 1.4686 2.2487 1.1675 0.2034  -0.0221 -0.3999 491 ASP   A OD2  
3381 N  N    . ILE   A 465 ? 1.2142 1.7870 0.9557 0.1811  0.0262  -0.2001 492 ILE   A N    
3382 C  CA   . ILE   A 465 ? 1.2545 1.7829 1.0169 0.1755  0.0413  -0.1685 492 ILE   A CA   
3383 C  C    . ILE   A 465 ? 1.2463 1.7731 1.0062 0.1819  0.0517  -0.1141 492 ILE   A C    
3384 O  O    . ILE   A 465 ? 1.2202 1.7631 0.9752 0.1951  0.0711  -0.0844 492 ILE   A O    
3385 C  CB   . ILE   A 465 ? 1.2438 1.7053 1.0417 0.1518  0.0340  -0.1850 492 ILE   A CB   
3386 C  CG1  . ILE   A 465 ? 1.2052 1.6681 1.0086 0.1486  0.0300  -0.2361 492 ILE   A CG1  
3387 C  CG2  . ILE   A 465 ? 1.2375 1.6599 1.0590 0.1470  0.0463  -0.1563 492 ILE   A CG2  
3388 C  CD1  . ILE   A 465 ? 1.0989 1.4979 0.9356 0.1322  0.0297  -0.2483 492 ILE   A CD1  
3389 N  N    . VAL   A 466 ? 1.1801 1.6903 0.9449 0.1738  0.0413  -0.1006 493 VAL   A N    
3390 C  CA   . VAL   A 466 ? 1.1768 1.6777 0.9464 0.1781  0.0523  -0.0505 493 VAL   A CA   
3391 C  C    . VAL   A 466 ? 1.2297 1.7860 0.9692 0.2060  0.0696  -0.0205 493 VAL   A C    
3392 O  O    . VAL   A 466 ? 1.2101 1.7571 0.9608 0.2116  0.0913  0.0201  493 VAL   A O    
3393 C  CB   . VAL   A 466 ? 1.2011 1.6859 0.9754 0.1687  0.0370  -0.0462 493 VAL   A CB   
3394 C  CG1  . VAL   A 466 ? 1.0879 1.5667 0.8674 0.1760  0.0502  0.0047  493 VAL   A CG1  
3395 C  CG2  . VAL   A 466 ? 1.0086 1.4352 0.8133 0.1429  0.0246  -0.0675 493 VAL   A CG2  
3396 N  N    . SER   A 467 ? 1.2034 1.8201 0.9060 0.2249  0.0618  -0.0405 494 SER   A N    
3397 C  CA   . SER   A 467 ? 1.2676 1.9434 0.9350 0.2565  0.0787  -0.0102 494 SER   A CA   
3398 C  C    . SER   A 467 ? 1.2760 1.9601 0.9432 0.2650  0.1011  -0.0024 494 SER   A C    
3399 O  O    . SER   A 467 ? 1.2508 1.9565 0.9062 0.2852  0.1257  0.0415  494 SER   A O    
3400 C  CB   . SER   A 467 ? 1.3377 2.0851 0.9647 0.2768  0.0624  -0.0405 494 SER   A CB   
3401 O  OG   . SER   A 467 ? 1.4018 2.1618 1.0291 0.2686  0.0496  -0.0985 494 SER   A OG   
3402 N  N    . GLU   A 468 ? 1.2462 1.9132 0.9279 0.2511  0.0953  -0.0428 495 GLU   A N    
3403 C  CA   . GLU   A 468 ? 1.1942 1.8681 0.8795 0.2583  0.1162  -0.0377 495 GLU   A CA   
3404 C  C    . GLU   A 468 ? 1.2769 1.9039 0.9999 0.2476  0.1370  0.0048  495 GLU   A C    
3405 O  O    . GLU   A 468 ? 1.2898 1.9363 1.0105 0.2625  0.1636  0.0377  495 GLU   A O    
3406 C  CB   . GLU   A 468 ? 1.1636 1.8249 0.8606 0.2457  0.1048  -0.0913 495 GLU   A CB   
3407 C  CG   . GLU   A 468 ? 1.2363 1.8839 0.9528 0.2452  0.1244  -0.0860 495 GLU   A CG   
3408 C  CD   . GLU   A 468 ? 1.4202 2.0964 1.1244 0.2524  0.1217  -0.1332 495 GLU   A CD   
3409 O  OE1  . GLU   A 468 ? 1.5689 2.2593 1.2619 0.2497  0.1021  -0.1772 495 GLU   A OE1  
3410 O  OE2  . GLU   A 468 ? 1.3456 2.0306 1.0553 0.2601  0.1402  -0.1281 495 GLU   A OE2  
3411 N  N    . LEU   A 469 ? 1.2455 1.8130 1.0056 0.2221  0.1264  0.0033  496 LEU   A N    
3412 C  CA   . LEU   A 469 ? 1.2694 1.7965 1.0709 0.2106  0.1438  0.0361  496 LEU   A CA   
3413 C  C    . LEU   A 469 ? 1.3123 1.8519 1.1123 0.2240  0.1661  0.0888  496 LEU   A C    
3414 O  O    . LEU   A 469 ? 1.3515 1.8816 1.1795 0.2242  0.1922  0.1191  496 LEU   A O    
3415 C  CB   . LEU   A 469 ? 1.2250 1.6935 1.0620 0.1840  0.1258  0.0221  496 LEU   A CB   
3416 C  CG   . LEU   A 469 ? 1.2458 1.6857 1.1005 0.1696  0.1125  -0.0174 496 LEU   A CG   
3417 C  CD1  . LEU   A 469 ? 1.1979 1.6488 1.0673 0.1757  0.1320  -0.0151 496 LEU   A CD1  
3418 C  CD2  . LEU   A 469 ? 1.2899 1.7401 1.1199 0.1694  0.0921  -0.0606 496 LEU   A CD2  
3419 N  N    . ARG   A 470 ? 1.2588 1.8209 1.0296 0.2363  0.1583  0.1007  497 ARG   A N    
3420 C  CA   . ARG   A 470 ? 1.3140 1.8932 1.0781 0.2554  0.1827  0.1538  497 ARG   A CA   
3421 C  C    . ARG   A 470 ? 1.3949 2.0270 1.1294 0.2839  0.2084  0.1735  497 ARG   A C    
3422 O  O    . ARG   A 470 ? 1.4811 2.1115 1.2311 0.2937  0.2412  0.2195  497 ARG   A O    
3423 C  CB   . ARG   A 470 ? 1.3305 1.9270 1.0675 0.2658  0.1668  0.1608  497 ARG   A CB   
3424 C  CG   . ARG   A 470 ? 1.3357 1.8943 1.1026 0.2597  0.1776  0.2015  497 ARG   A CG   
3425 C  CD   . ARG   A 470 ? 1.4073 1.9852 1.1477 0.2706  0.1596  0.2047  497 ARG   A CD   
3426 N  NE   . ARG   A 470 ? 1.3358 1.8679 1.1025 0.2430  0.1350  0.1798  497 ARG   A NE   
3427 C  CZ   . ARG   A 470 ? 1.4205 1.9638 1.1696 0.2365  0.1052  0.1402  497 ARG   A CZ   
3428 N  NH1  . ARG   A 470 ? 1.3616 1.9623 1.0696 0.2541  0.0936  0.1155  497 ARG   A NH1  
3429 N  NH2  . ARG   A 470 ? 1.3339 1.8322 1.1095 0.2120  0.0877  0.1234  497 ARG   A NH2  
3430 N  N    . GLY   A 471 ? 1.3968 2.0767 1.0911 0.2977  0.1957  0.1383  498 GLY   A N    
3431 C  CA   . GLY   A 471 ? 1.4602 2.1950 1.1232 0.3261  0.2192  0.1524  498 GLY   A CA   
3432 C  C    . GLY   A 471 ? 1.5186 2.2316 1.2170 0.3169  0.2442  0.1609  498 GLY   A C    
3433 O  O    . GLY   A 471 ? 1.6282 2.3710 1.3169 0.3381  0.2763  0.1958  498 GLY   A O    
3434 N  N    . GLN   A 472 ? 1.4598 2.1234 1.1999 0.2870  0.2309  0.1303  499 GLN   A N    
3435 C  CA   . GLN   A 472 ? 1.4736 2.1163 1.2549 0.2768  0.2527  0.1369  499 GLN   A CA   
3436 C  C    . GLN   A 472 ? 1.4794 2.0913 1.3050 0.2699  0.2807  0.1864  499 GLN   A C    
3437 O  O    . GLN   A 472 ? 1.5335 2.1414 1.3927 0.2674  0.3075  0.2017  499 GLN   A O    
3438 C  CB   . GLN   A 472 ? 1.4250 2.0268 1.2374 0.2504  0.2292  0.0912  499 GLN   A CB   
3439 C  CG   . GLN   A 472 ? 1.4236 2.0467 1.2027 0.2539  0.2040  0.0395  499 GLN   A CG   
3440 C  CD   . GLN   A 472 ? 1.5007 2.1036 1.3058 0.2418  0.1997  0.0045  499 GLN   A CD   
3441 O  OE1  . GLN   A 472 ? 1.6059 2.1805 1.4538 0.2301  0.2120  0.0168  499 GLN   A OE1  
3442 N  NE2  . GLN   A 472 ? 1.5224 2.1415 1.3047 0.2452  0.1827  -0.0411 499 GLN   A NE2  
3443 N  N    . LEU   A 473 ? 1.4482 2.0386 1.2789 0.2663  0.2761  0.2095  500 LEU   A N    
3444 C  CA   . LEU   A 473 ? 1.4423 2.0042 1.3172 0.2613  0.3052  0.2564  500 LEU   A CA   
3445 C  C    . LEU   A 473 ? 1.5599 2.1609 1.4098 0.2930  0.3422  0.3087  500 LEU   A C    
3446 O  O    . LEU   A 473 ? 1.6016 2.1844 1.4936 0.2916  0.3781  0.3494  500 LEU   A O    
3447 C  CB   . LEU   A 473 ? 1.5034 2.0249 1.3959 0.2452  0.2860  0.2583  500 LEU   A CB   
3448 C  CG   . LEU   A 473 ? 1.5886 2.0613 1.5448 0.2259  0.3027  0.2841  500 LEU   A CG   
3449 C  CD1  . LEU   A 473 ? 1.6899 2.1697 1.6585 0.2440  0.3454  0.3430  500 LEU   A CD1  
3450 C  CD2  . LEU   A 473 ? 1.3456 1.7903 1.3578 0.2007  0.3037  0.2597  500 LEU   A CD2  
3451 N  N    . LEU   A 474 ? 1.6248 2.2815 1.4089 0.3227  0.3357  0.3075  501 LEU   A N    
3452 C  CA   . LEU   A 474 ? 1.6376 2.3397 1.3892 0.3591  0.3712  0.3581  501 LEU   A CA   
3453 C  C    . LEU   A 474 ? 1.5998 2.3142 1.3702 0.3637  0.4053  0.3709  501 LEU   A C    
3454 O  O    . LEU   A 474 ? 1.5617 2.2522 1.3715 0.3640  0.4389  0.4146  501 LEU   A O    
3455 C  CB   . LEU   A 474 ? 1.5812 2.3420 1.2617 0.3881  0.3460  0.3412  501 LEU   A CB   
3456 C  CG   . LEU   A 474 ? 1.6790 2.4822 1.3295 0.4207  0.3574  0.3632  501 LEU   A CG   
3457 C  CD1  . LEU   A 474 ? 1.6429 2.4308 1.3086 0.4388  0.3840  0.4265  501 LEU   A CD1  
3458 C  CD2  . LEU   A 474 ? 1.6169 2.4782 1.2111 0.4411  0.3218  0.3248  501 LEU   A CD2  
3459 N  N    . GLU   A 475 ? 1.4908 2.2333 1.2411 0.3639  0.3923  0.3279  502 GLU   A N    
3460 C  CA   . GLU   A 475 ? 1.5324 2.2859 1.3006 0.3671  0.4186  0.3331  502 GLU   A CA   
3461 C  C    . GLU   A 475 ? 1.5583 2.2958 1.3562 0.3422  0.4031  0.2819  502 GLU   A C    
3462 O  O    . GLU   A 475 ? 1.3868 2.0739 1.2252 0.3119  0.3800  0.2580  502 GLU   A O    
3463 C  CB   . GLU   A 475 ? 1.4235 2.2277 1.1358 0.3985  0.4142  0.3337  502 GLU   A CB   
3464 C  C1   . AKG   B .   ? 1.3040 1.3028 1.3718 -0.0313 -0.0075 -0.0400 601 AKG   A C1   
3465 O  O1   . AKG   B .   ? 1.2521 1.2294 1.2989 -0.0263 -0.0041 -0.0347 601 AKG   A O1   
3466 O  O2   . AKG   B .   ? 1.2549 1.2681 1.3434 -0.0434 -0.0038 -0.0478 601 AKG   A O2   
3467 C  C2   . AKG   B .   ? 1.1185 1.1318 1.1935 -0.0221 -0.0165 -0.0399 601 AKG   A C2   
3468 O  O5   . AKG   B .   ? 1.0153 1.0304 1.0899 -0.0162 -0.0286 -0.0383 601 AKG   A O5   
3469 C  C3   . AKG   B .   ? 1.0758 1.0994 1.1616 -0.0208 -0.0073 -0.0420 601 AKG   A C3   
3470 C  C4   . AKG   B .   ? 1.0713 1.0779 1.1389 -0.0171 0.0092  -0.0377 601 AKG   A C4   
3471 C  C5   . AKG   B .   ? 1.1592 1.1717 1.2428 -0.0262 0.0271  -0.0387 601 AKG   A C5   
3472 O  O3   . AKG   B .   ? 1.0734 1.0798 1.1665 -0.0380 0.0375  -0.0397 601 AKG   A O3   
3473 O  O4   . AKG   B .   ? 1.1720 1.1972 1.2623 -0.0207 0.0319  -0.0402 601 AKG   A O4   
3474 N  N3   . A1EF5 C .   ? 0.9356 0.9320 0.9824 -0.0161 -0.0564 -0.0280 602 A1EF5 A N3   
3475 C  C5   . A1EF5 C .   ? 1.1159 1.1166 1.1676 -0.0275 -0.0438 -0.0367 602 A1EF5 A C5   
3476 C  C6   . A1EF5 C .   ? 1.1965 1.1879 1.2488 -0.0337 -0.0302 -0.0405 602 A1EF5 A C6   
3477 C  C7   . A1EF5 C .   ? 1.0266 1.0516 1.0896 -0.0267 -0.0528 -0.0360 602 A1EF5 A C7   
3478 C  C8   . A1EF5 C .   ? 1.0535 1.1083 1.1317 -0.0321 -0.0546 -0.0436 602 A1EF5 A C8   
3479 C  C10  . A1EF5 C .   ? 1.0744 1.1908 1.1799 -0.0272 -0.0645 -0.0482 602 A1EF5 A C10  
3480 C  C15  . A1EF5 C .   ? 1.2843 1.4810 1.4098 -0.0491 -0.0747 -0.1041 602 A1EF5 A C15  
3481 C  C22  . A1EF5 C .   ? 1.3540 1.4469 1.4561 -0.0490 -0.0519 -0.0698 602 A1EF5 A C22  
3482 C  C24  . A1EF5 C .   ? 1.1693 1.2277 1.2523 -0.0437 -0.0490 -0.0570 602 A1EF5 A C24  
3483 C  C1   . A1EF5 C .   ? 0.9323 0.9683 0.9977 -0.0125 -0.0656 -0.0194 602 A1EF5 A C1   
3484 C  C12  . A1EF5 C .   ? 1.2961 1.4221 1.4085 -0.0402 -0.0610 -0.0661 602 A1EF5 A C12  
3485 C  C14  . A1EF5 C .   ? 1.3142 1.5183 1.4519 -0.0449 -0.0736 -0.0966 602 A1EF5 A C14  
3486 C  C16  . A1EF5 C .   ? 1.2282 1.4722 1.3626 -0.0487 -0.0841 -0.1237 602 A1EF5 A C16  
3487 C  C18  . A1EF5 C .   ? 1.4590 1.7156 1.6154 -0.0410 -0.0824 -0.1090 602 A1EF5 A C18  
3488 C  C19  . A1EF5 C .   ? 1.3255 1.6045 1.4997 -0.0346 -0.0835 -0.1054 602 A1EF5 A C19  
3489 C  C2   . A1EF5 C .   ? 0.9783 0.9972 1.0364 -0.0189 -0.0589 -0.0280 602 A1EF5 A C2   
3490 C  C9   . A1EF5 C .   ? 1.0497 1.1310 1.1409 -0.0247 -0.0611 -0.0390 602 A1EF5 A C9   
3491 N  N13  . A1EF5 C .   ? 1.2941 1.4629 1.4271 -0.0435 -0.0654 -0.0814 602 A1EF5 A N13  
3492 N  N4   . A1EF5 C .   ? 1.0959 1.0825 1.1360 -0.0197 -0.0477 -0.0321 602 A1EF5 A N4   
3493 O  O20  . A1EF5 C .   ? 1.0582 1.3064 1.2268 -0.0298 -0.0775 -0.0870 602 A1EF5 A O20  
3494 O  O21  . A1EF5 C .   ? 1.2588 1.5892 1.4539 -0.0339 -0.0909 -0.1234 602 A1EF5 A O21  
3495 S  S17  . A1EF5 C .   ? 1.3166 1.6177 1.4742 -0.0419 -0.0930 -0.1327 602 A1EF5 A S17  
3496 CL CL11 . A1EF5 C .   ? 1.1961 1.3478 1.3157 -0.0126 -0.0724 -0.0387 602 A1EF5 A CL11 
3497 CL CL23 . A1EF5 C .   ? 1.8529 1.9496 1.9713 -0.0663 -0.0425 -0.0928 602 A1EF5 A CL23 
3498 O  O    . HOH   D .   ? 0.8699 0.8742 0.8563 0.0629  -0.0741 -0.0895 701 HOH   A O    
3499 O  O    . HOH   D .   ? 0.7662 0.9165 1.0507 -0.0639 0.1699  -0.0644 702 HOH   A O    
3500 O  O    . HOH   D .   ? 0.9435 1.1097 0.8747 0.0566  -0.0004 -0.2584 703 HOH   A O    
3501 O  O    . HOH   D .   ? 0.7092 0.6534 0.6889 0.0353  -0.0646 -0.0438 704 HOH   A O    
3502 O  O    . HOH   D .   ? 0.9676 1.0188 0.9635 0.0827  -0.0025 -0.1135 705 HOH   A O    
3503 O  O    . HOH   D .   ? 0.8232 0.8465 0.9525 0.0477  -0.0683 -0.1409 706 HOH   A O    
3504 O  O    . HOH   D .   ? 0.9709 1.1492 1.0867 0.3777  -0.0563 -0.1147 707 HOH   A O    
3505 O  O    . HOH   D .   ? 0.7802 0.7857 0.9085 0.0347  -0.0767 -0.1205 708 HOH   A O    
3506 O  O    . HOH   D .   ? 0.8982 0.9199 0.9633 -0.0679 -0.0162 -0.2555 709 HOH   A O    
3507 O  O    . HOH   D .   ? 1.0675 0.9860 1.1480 0.3289  0.0554  -0.1258 710 HOH   A O    
3508 O  O    . HOH   D .   ? 0.6865 0.6500 0.6874 0.0387  -0.0844 -0.0520 711 HOH   A O    
3509 O  O    . HOH   D .   ? 0.8212 1.1041 1.4127 0.2743  0.0283  0.0461  712 HOH   A O    
3510 O  O    . HOH   D .   ? 0.6655 1.1556 1.1615 -0.0709 0.0078  -0.1904 713 HOH   A O    
# 
