data_8VTF
# 
_entry.id   8VTF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8VTF         pdb_00008vtf 10.2210/pdb8vtf/pdb 
WWPDB D_1000281199 ?            ?                   
# 
_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       2025-01-29 
# 
_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                        8VTF 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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                 2 
_pdbx_contact_author.email              yxf423@med.miami.edu 
_pdbx_contact_author.name_first         Yangbo 
_pdbx_contact_author.name_last          Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5894-9476 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Park, H.' 1 ? 
'Feng, Y.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'A structural study of selectivity mechanisms for JNK3 and p38 alpha with indazole scaffold probing compounds' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Park, H.' 1 ? 
primary 'Feng, Y.' 2 ? 
# 
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 'Mitogen-activated protein kinase 10'                                                           52649.332 1  
2.7.11.24 ? ? ? 
2 non-polymer syn '(4P)-4-[6-fluoro-5-(2-methoxyanilino)-1H-indazol-1-yl]-N-(oxetan-3-yl)thiophene-2-carboxamide' 438.475   1  ? ? 
? ? 
3 water       nat water                                                                                           18.015    48 ? ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;MAPK 10,MAP kinase p49 3F12,Stress-activated protein kinase 1b,SAPK1b,Stress-activated protein kinase JNK3,c-Jun N-terminal kinase 3
;
# 
_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       
;MSLHFLYYCSEPTLDVKIAFCQGFDKQVDVSYIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCA
AYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQME
LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGY
KENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPA
DSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMN
SEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSLHFLYYCSEPTLDVKIAFCQGFDKQVDVSYIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCA
AYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQME
LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGY
KENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPA
DSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMN
SEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR
;
_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 '(4P)-4-[6-fluoro-5-(2-methoxyanilino)-1H-indazol-1-yl]-N-(oxetan-3-yl)thiophene-2-carboxamide' A1ACP 
3 water                                                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LEU n 
1 4   HIS n 
1 5   PHE n 
1 6   LEU n 
1 7   TYR n 
1 8   TYR n 
1 9   CYS n 
1 10  SER n 
1 11  GLU n 
1 12  PRO n 
1 13  THR n 
1 14  LEU n 
1 15  ASP n 
1 16  VAL n 
1 17  LYS n 
1 18  ILE n 
1 19  ALA n 
1 20  PHE n 
1 21  CYS n 
1 22  GLN n 
1 23  GLY n 
1 24  PHE n 
1 25  ASP n 
1 26  LYS n 
1 27  GLN n 
1 28  VAL n 
1 29  ASP n 
1 30  VAL n 
1 31  SER n 
1 32  TYR n 
1 33  ILE n 
1 34  ALA n 
1 35  LYS n 
1 36  HIS n 
1 37  TYR n 
1 38  ASN n 
1 39  MET n 
1 40  SER n 
1 41  LYS n 
1 42  SER n 
1 43  LYS n 
1 44  VAL n 
1 45  ASP n 
1 46  ASN n 
1 47  GLN n 
1 48  PHE n 
1 49  TYR n 
1 50  SER n 
1 51  VAL n 
1 52  GLU n 
1 53  VAL n 
1 54  GLY n 
1 55  ASP n 
1 56  SER n 
1 57  THR n 
1 58  PHE n 
1 59  THR n 
1 60  VAL n 
1 61  LEU n 
1 62  LYS n 
1 63  ARG n 
1 64  TYR n 
1 65  GLN n 
1 66  ASN n 
1 67  LEU n 
1 68  LYS n 
1 69  PRO n 
1 70  ILE n 
1 71  GLY n 
1 72  SER n 
1 73  GLY n 
1 74  ALA n 
1 75  GLN n 
1 76  GLY n 
1 77  ILE n 
1 78  VAL n 
1 79  CYS n 
1 80  ALA n 
1 81  ALA n 
1 82  TYR n 
1 83  ASP n 
1 84  ALA n 
1 85  VAL n 
1 86  LEU n 
1 87  ASP n 
1 88  ARG n 
1 89  ASN n 
1 90  VAL n 
1 91  ALA n 
1 92  ILE n 
1 93  LYS n 
1 94  LYS n 
1 95  LEU n 
1 96  SER n 
1 97  ARG n 
1 98  PRO n 
1 99  PHE n 
1 100 GLN n 
1 101 ASN n 
1 102 GLN n 
1 103 THR n 
1 104 HIS n 
1 105 ALA n 
1 106 LYS n 
1 107 ARG n 
1 108 ALA n 
1 109 TYR n 
1 110 ARG n 
1 111 GLU n 
1 112 LEU n 
1 113 VAL n 
1 114 LEU n 
1 115 MET n 
1 116 LYS n 
1 117 CYS n 
1 118 VAL n 
1 119 ASN n 
1 120 HIS n 
1 121 LYS n 
1 122 ASN n 
1 123 ILE n 
1 124 ILE n 
1 125 SER n 
1 126 LEU n 
1 127 LEU n 
1 128 ASN n 
1 129 VAL n 
1 130 PHE n 
1 131 THR n 
1 132 PRO n 
1 133 GLN n 
1 134 LYS n 
1 135 THR n 
1 136 LEU n 
1 137 GLU n 
1 138 GLU n 
1 139 PHE n 
1 140 GLN n 
1 141 ASP n 
1 142 VAL n 
1 143 TYR n 
1 144 LEU n 
1 145 VAL n 
1 146 MET n 
1 147 GLU n 
1 148 LEU n 
1 149 MET n 
1 150 ASP n 
1 151 ALA n 
1 152 ASN n 
1 153 LEU n 
1 154 CYS n 
1 155 GLN n 
1 156 VAL n 
1 157 ILE n 
1 158 GLN n 
1 159 MET n 
1 160 GLU n 
1 161 LEU n 
1 162 ASP n 
1 163 HIS n 
1 164 GLU n 
1 165 ARG n 
1 166 MET n 
1 167 SER n 
1 168 TYR n 
1 169 LEU n 
1 170 LEU n 
1 171 TYR n 
1 172 GLN n 
1 173 MET n 
1 174 LEU n 
1 175 CYS n 
1 176 GLY n 
1 177 ILE n 
1 178 LYS n 
1 179 HIS n 
1 180 LEU n 
1 181 HIS n 
1 182 SER n 
1 183 ALA n 
1 184 GLY n 
1 185 ILE n 
1 186 ILE n 
1 187 HIS n 
1 188 ARG n 
1 189 ASP n 
1 190 LEU n 
1 191 LYS n 
1 192 PRO n 
1 193 SER n 
1 194 ASN n 
1 195 ILE n 
1 196 VAL n 
1 197 VAL n 
1 198 LYS n 
1 199 SER n 
1 200 ASP n 
1 201 CYS n 
1 202 THR n 
1 203 LEU n 
1 204 LYS n 
1 205 ILE n 
1 206 LEU n 
1 207 ASP n 
1 208 PHE n 
1 209 GLY n 
1 210 LEU n 
1 211 ALA n 
1 212 ARG n 
1 213 THR n 
1 214 ALA n 
1 215 GLY n 
1 216 THR n 
1 217 SER n 
1 218 PHE n 
1 219 MET n 
1 220 MET n 
1 221 THR n 
1 222 PRO n 
1 223 TYR n 
1 224 VAL n 
1 225 VAL n 
1 226 THR n 
1 227 ARG n 
1 228 TYR n 
1 229 TYR n 
1 230 ARG n 
1 231 ALA n 
1 232 PRO n 
1 233 GLU n 
1 234 VAL n 
1 235 ILE n 
1 236 LEU n 
1 237 GLY n 
1 238 MET n 
1 239 GLY n 
1 240 TYR n 
1 241 LYS n 
1 242 GLU n 
1 243 ASN n 
1 244 VAL n 
1 245 ASP n 
1 246 ILE n 
1 247 TRP n 
1 248 SER n 
1 249 VAL n 
1 250 GLY n 
1 251 CYS n 
1 252 ILE n 
1 253 MET n 
1 254 GLY n 
1 255 GLU n 
1 256 MET n 
1 257 VAL n 
1 258 ARG n 
1 259 HIS n 
1 260 LYS n 
1 261 ILE n 
1 262 LEU n 
1 263 PHE n 
1 264 PRO n 
1 265 GLY n 
1 266 ARG n 
1 267 ASP n 
1 268 TYR n 
1 269 ILE n 
1 270 ASP n 
1 271 GLN n 
1 272 TRP n 
1 273 ASN n 
1 274 LYS n 
1 275 VAL n 
1 276 ILE n 
1 277 GLU n 
1 278 GLN n 
1 279 LEU n 
1 280 GLY n 
1 281 THR n 
1 282 PRO n 
1 283 CYS n 
1 284 PRO n 
1 285 GLU n 
1 286 PHE n 
1 287 MET n 
1 288 LYS n 
1 289 LYS n 
1 290 LEU n 
1 291 GLN n 
1 292 PRO n 
1 293 THR n 
1 294 VAL n 
1 295 ARG n 
1 296 ASN n 
1 297 TYR n 
1 298 VAL n 
1 299 GLU n 
1 300 ASN n 
1 301 ARG n 
1 302 PRO n 
1 303 LYS n 
1 304 TYR n 
1 305 ALA n 
1 306 GLY n 
1 307 LEU n 
1 308 THR n 
1 309 PHE n 
1 310 PRO n 
1 311 LYS n 
1 312 LEU n 
1 313 PHE n 
1 314 PRO n 
1 315 ASP n 
1 316 SER n 
1 317 LEU n 
1 318 PHE n 
1 319 PRO n 
1 320 ALA n 
1 321 ASP n 
1 322 SER n 
1 323 GLU n 
1 324 HIS n 
1 325 ASN n 
1 326 LYS n 
1 327 LEU n 
1 328 LYS n 
1 329 ALA n 
1 330 SER n 
1 331 GLN n 
1 332 ALA n 
1 333 ARG n 
1 334 ASP n 
1 335 LEU n 
1 336 LEU n 
1 337 SER n 
1 338 LYS n 
1 339 MET n 
1 340 LEU n 
1 341 VAL n 
1 342 ILE n 
1 343 ASP n 
1 344 PRO n 
1 345 ALA n 
1 346 LYS n 
1 347 ARG n 
1 348 ILE n 
1 349 SER n 
1 350 VAL n 
1 351 ASP n 
1 352 ASP n 
1 353 ALA n 
1 354 LEU n 
1 355 GLN n 
1 356 HIS n 
1 357 PRO n 
1 358 TYR n 
1 359 ILE n 
1 360 ASN n 
1 361 VAL n 
1 362 TRP n 
1 363 TYR n 
1 364 ASP n 
1 365 PRO n 
1 366 ALA n 
1 367 GLU n 
1 368 VAL n 
1 369 GLU n 
1 370 ALA n 
1 371 PRO n 
1 372 PRO n 
1 373 PRO n 
1 374 GLN n 
1 375 ILE n 
1 376 TYR n 
1 377 ASP n 
1 378 LYS n 
1 379 GLN n 
1 380 LEU n 
1 381 ASP n 
1 382 GLU n 
1 383 ARG n 
1 384 GLU n 
1 385 HIS n 
1 386 THR n 
1 387 ILE n 
1 388 GLU n 
1 389 GLU n 
1 390 TRP n 
1 391 LYS n 
1 392 GLU n 
1 393 LEU n 
1 394 ILE n 
1 395 TYR n 
1 396 LYS n 
1 397 GLU n 
1 398 VAL n 
1 399 MET n 
1 400 ASN n 
1 401 SER n 
1 402 GLU n 
1 403 GLU n 
1 404 LYS n 
1 405 THR n 
1 406 LYS n 
1 407 ASN n 
1 408 GLY n 
1 409 VAL n 
1 410 VAL n 
1 411 LYS n 
1 412 GLY n 
1 413 GLN n 
1 414 PRO n 
1 415 SER n 
1 416 PRO n 
1 417 SER n 
1 418 GLY n 
1 419 ALA n 
1 420 ALA n 
1 421 VAL n 
1 422 ASN n 
1 423 SER n 
1 424 SER n 
1 425 GLU n 
1 426 SER n 
1 427 LEU n 
1 428 PRO n 
1 429 PRO n 
1 430 SER n 
1 431 SER n 
1 432 SER n 
1 433 VAL n 
1 434 ASN n 
1 435 ASP n 
1 436 ILE n 
1 437 SER n 
1 438 SER n 
1 439 MET n 
1 440 SER n 
1 441 THR n 
1 442 ASP n 
1 443 GLN n 
1 444 THR n 
1 445 LEU n 
1 446 ALA n 
1 447 SER n 
1 448 ASP n 
1 449 THR n 
1 450 ASP n 
1 451 SER n 
1 452 SER n 
1 453 LEU n 
1 454 GLU n 
1 455 ALA n 
1 456 SER n 
1 457 ALA n 
1 458 GLY n 
1 459 PRO n 
1 460 LEU n 
1 461 GLY n 
1 462 CYS n 
1 463 CYS n 
1 464 ARG 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                   464 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MAPK10, JNK3, JNK3A, PRKM10, SAPK1B' 
_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 
A1ACP non-polymer         . '(4P)-4-[6-fluoro-5-(2-methoxyanilino)-1H-indazol-1-yl]-N-(oxetan-3-yl)thiophene-2-carboxamide' ? 
'C22 H19 F N4 O3 S' 438.475 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   ?   ?   ?   A . n 
A 1 5   PHE 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   ?   ?   ?   A . n 
A 1 7   TYR 7   7   ?   ?   ?   A . n 
A 1 8   TYR 8   8   ?   ?   ?   A . n 
A 1 9   CYS 9   9   ?   ?   ?   A . n 
A 1 10  SER 10  10  ?   ?   ?   A . n 
A 1 11  GLU 11  11  ?   ?   ?   A . n 
A 1 12  PRO 12  12  ?   ?   ?   A . n 
A 1 13  THR 13  13  ?   ?   ?   A . n 
A 1 14  LEU 14  14  ?   ?   ?   A . n 
A 1 15  ASP 15  15  ?   ?   ?   A . n 
A 1 16  VAL 16  16  ?   ?   ?   A . n 
A 1 17  LYS 17  17  ?   ?   ?   A . n 
A 1 18  ILE 18  18  ?   ?   ?   A . n 
A 1 19  ALA 19  19  ?   ?   ?   A . n 
A 1 20  PHE 20  20  ?   ?   ?   A . n 
A 1 21  CYS 21  21  ?   ?   ?   A . n 
A 1 22  GLN 22  22  ?   ?   ?   A . n 
A 1 23  GLY 23  23  ?   ?   ?   A . n 
A 1 24  PHE 24  24  ?   ?   ?   A . n 
A 1 25  ASP 25  25  ?   ?   ?   A . n 
A 1 26  LYS 26  26  ?   ?   ?   A . n 
A 1 27  GLN 27  27  ?   ?   ?   A . n 
A 1 28  VAL 28  28  ?   ?   ?   A . n 
A 1 29  ASP 29  29  ?   ?   ?   A . n 
A 1 30  VAL 30  30  ?   ?   ?   A . n 
A 1 31  SER 31  31  ?   ?   ?   A . n 
A 1 32  TYR 32  32  ?   ?   ?   A . n 
A 1 33  ILE 33  33  ?   ?   ?   A . n 
A 1 34  ALA 34  34  ?   ?   ?   A . n 
A 1 35  LYS 35  35  ?   ?   ?   A . n 
A 1 36  HIS 36  36  ?   ?   ?   A . n 
A 1 37  TYR 37  37  ?   ?   ?   A . n 
A 1 38  ASN 38  38  ?   ?   ?   A . n 
A 1 39  MET 39  39  ?   ?   ?   A . n 
A 1 40  SER 40  40  ?   ?   ?   A . n 
A 1 41  LYS 41  41  ?   ?   ?   A . n 
A 1 42  SER 42  42  ?   ?   ?   A . n 
A 1 43  LYS 43  43  ?   ?   ?   A . n 
A 1 44  VAL 44  44  ?   ?   ?   A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  GLN 47  47  47  GLN GLN A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  PHE 58  58  58  PHE PHE A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  VAL 60  60  60  VAL VAL A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  ARG 63  63  63  ARG ARG A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  GLN 75  75  75  GLN GLN A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  CYS 79  79  79  CYS CYS A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 GLN 100 100 100 GLN GLN A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 GLN 102 102 102 GLN GLN A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 MET 115 115 115 MET MET A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 GLN 140 140 140 GLN GLN A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 TYR 143 143 143 TYR TYR A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 MET 146 146 146 MET MET A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 MET 149 149 149 MET MET A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 CYS 154 154 154 CYS CYS A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 MET 159 159 159 MET MET A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 MET 166 166 166 MET MET A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 TYR 168 168 168 TYR TYR A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 TYR 171 171 171 TYR TYR A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 MET 173 173 173 MET MET A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 CYS 175 175 175 CYS CYS A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 LYS 178 178 178 LYS LYS A . n 
A 1 179 HIS 179 179 179 HIS HIS A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 HIS 181 181 181 HIS HIS A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 HIS 187 187 187 HIS HIS A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 LYS 198 198 198 LYS LYS A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 CYS 201 201 201 CYS CYS A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ASP 207 207 207 ASP ASP A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 ARG 212 212 ?   ?   ?   A . n 
A 1 213 THR 213 213 ?   ?   ?   A . n 
A 1 214 ALA 214 214 ?   ?   ?   A . n 
A 1 215 GLY 215 215 ?   ?   ?   A . n 
A 1 216 THR 216 216 ?   ?   ?   A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 MET 219 219 219 MET MET A . n 
A 1 220 MET 220 220 220 MET MET A . n 
A 1 221 THR 221 221 221 THR THR A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 TYR 223 223 223 TYR TYR A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 TYR 228 228 228 TYR TYR A . n 
A 1 229 TYR 229 229 229 TYR TYR A . n 
A 1 230 ARG 230 230 230 ARG ARG A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 MET 238 238 238 MET MET A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 TRP 247 247 247 TRP TRP A . n 
A 1 248 SER 248 248 248 SER SER A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 GLY 250 250 250 GLY GLY A . n 
A 1 251 CYS 251 251 251 CYS CYS A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 MET 253 253 253 MET MET A . n 
A 1 254 GLY 254 254 254 GLY GLY A . n 
A 1 255 GLU 255 255 255 GLU GLU A . n 
A 1 256 MET 256 256 256 MET MET A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 ARG 258 258 258 ARG ARG A . n 
A 1 259 HIS 259 259 259 HIS HIS A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 PHE 263 263 263 PHE PHE A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 ARG 266 266 266 ARG ARG A . n 
A 1 267 ASP 267 267 267 ASP ASP A . n 
A 1 268 TYR 268 268 268 TYR TYR A . n 
A 1 269 ILE 269 269 269 ILE ILE A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 GLN 271 271 271 GLN GLN A . n 
A 1 272 TRP 272 272 272 TRP TRP A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 ILE 276 276 276 ILE ILE A . n 
A 1 277 GLU 277 277 277 GLU GLU A . n 
A 1 278 GLN 278 278 278 GLN GLN A . n 
A 1 279 LEU 279 279 279 LEU LEU A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 THR 281 281 281 THR THR A . n 
A 1 282 PRO 282 282 282 PRO PRO A . n 
A 1 283 CYS 283 283 283 CYS CYS A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 GLU 285 285 285 GLU GLU A . n 
A 1 286 PHE 286 286 286 PHE PHE A . n 
A 1 287 MET 287 287 287 MET MET A . n 
A 1 288 LYS 288 288 288 LYS LYS A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 GLN 291 291 291 GLN GLN A . n 
A 1 292 PRO 292 292 292 PRO PRO A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 VAL 294 294 294 VAL VAL A . n 
A 1 295 ARG 295 295 295 ARG ARG A . n 
A 1 296 ASN 296 296 296 ASN ASN A . n 
A 1 297 TYR 297 297 297 TYR TYR A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 ASN 300 300 300 ASN ASN A . n 
A 1 301 ARG 301 301 301 ARG ARG A . n 
A 1 302 PRO 302 302 302 PRO PRO A . n 
A 1 303 LYS 303 303 303 LYS LYS A . n 
A 1 304 TYR 304 304 304 TYR TYR A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 THR 308 308 308 THR THR A . n 
A 1 309 PHE 309 309 309 PHE PHE A . n 
A 1 310 PRO 310 310 310 PRO PRO A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 PHE 313 313 313 PHE PHE A . n 
A 1 314 PRO 314 314 314 PRO PRO A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 SER 316 316 316 SER SER A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 PHE 318 318 318 PHE PHE A . n 
A 1 319 PRO 319 319 319 PRO PRO A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 SER 322 322 322 SER SER A . n 
A 1 323 GLU 323 323 323 GLU GLU A . n 
A 1 324 HIS 324 324 324 HIS HIS A . n 
A 1 325 ASN 325 325 325 ASN ASN A . n 
A 1 326 LYS 326 326 326 LYS LYS A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 LYS 328 328 328 LYS LYS A . n 
A 1 329 ALA 329 329 329 ALA ALA A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 GLN 331 331 331 GLN GLN A . n 
A 1 332 ALA 332 332 332 ALA ALA A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 ASP 334 334 334 ASP ASP A . n 
A 1 335 LEU 335 335 335 LEU LEU A . n 
A 1 336 LEU 336 336 336 LEU LEU A . n 
A 1 337 SER 337 337 337 SER SER A . n 
A 1 338 LYS 338 338 338 LYS LYS A . n 
A 1 339 MET 339 339 339 MET MET A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 PRO 344 344 344 PRO PRO A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 LYS 346 346 346 LYS LYS A . n 
A 1 347 ARG 347 347 347 ARG ARG A . n 
A 1 348 ILE 348 348 348 ILE ILE A . n 
A 1 349 SER 349 349 349 SER SER A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 ASP 351 351 351 ASP ASP A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 GLN 355 355 355 GLN GLN A . n 
A 1 356 HIS 356 356 356 HIS HIS A . n 
A 1 357 PRO 357 357 357 PRO PRO A . n 
A 1 358 TYR 358 358 358 TYR TYR A . n 
A 1 359 ILE 359 359 359 ILE ILE A . n 
A 1 360 ASN 360 360 360 ASN ASN A . n 
A 1 361 VAL 361 361 361 VAL VAL A . n 
A 1 362 TRP 362 362 362 TRP TRP A . n 
A 1 363 TYR 363 363 363 TYR TYR A . n 
A 1 364 ASP 364 364 364 ASP ASP A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 ALA 366 366 366 ALA ALA A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 VAL 368 368 368 VAL VAL A . n 
A 1 369 GLU 369 369 369 GLU GLU A . n 
A 1 370 ALA 370 370 370 ALA ALA A . n 
A 1 371 PRO 371 371 371 PRO PRO A . n 
A 1 372 PRO 372 372 372 PRO PRO A . n 
A 1 373 PRO 373 373 373 PRO PRO A . n 
A 1 374 GLN 374 374 ?   ?   ?   A . n 
A 1 375 ILE 375 375 ?   ?   ?   A . n 
A 1 376 TYR 376 376 ?   ?   ?   A . n 
A 1 377 ASP 377 377 ?   ?   ?   A . n 
A 1 378 LYS 378 378 ?   ?   ?   A . n 
A 1 379 GLN 379 379 379 GLN GLN A . n 
A 1 380 LEU 380 380 380 LEU LEU A . n 
A 1 381 ASP 381 381 381 ASP ASP A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 ARG 383 383 383 ARG ARG A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 HIS 385 385 385 HIS HIS A . n 
A 1 386 THR 386 386 386 THR THR A . n 
A 1 387 ILE 387 387 387 ILE ILE A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 GLU 389 389 389 GLU GLU A . n 
A 1 390 TRP 390 390 390 TRP TRP A . n 
A 1 391 LYS 391 391 391 LYS LYS A . n 
A 1 392 GLU 392 392 392 GLU GLU A . n 
A 1 393 LEU 393 393 393 LEU LEU A . n 
A 1 394 ILE 394 394 394 ILE ILE A . n 
A 1 395 TYR 395 395 395 TYR TYR A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 GLU 397 397 397 GLU GLU A . n 
A 1 398 VAL 398 398 398 VAL VAL A . n 
A 1 399 MET 399 399 399 MET MET A . n 
A 1 400 ASN 400 400 400 ASN ASN A . n 
A 1 401 SER 401 401 ?   ?   ?   A . n 
A 1 402 GLU 402 402 ?   ?   ?   A . n 
A 1 403 GLU 403 403 ?   ?   ?   A . n 
A 1 404 LYS 404 404 ?   ?   ?   A . n 
A 1 405 THR 405 405 ?   ?   ?   A . n 
A 1 406 LYS 406 406 ?   ?   ?   A . n 
A 1 407 ASN 407 407 ?   ?   ?   A . n 
A 1 408 GLY 408 408 ?   ?   ?   A . n 
A 1 409 VAL 409 409 ?   ?   ?   A . n 
A 1 410 VAL 410 410 ?   ?   ?   A . n 
A 1 411 LYS 411 411 ?   ?   ?   A . n 
A 1 412 GLY 412 412 ?   ?   ?   A . n 
A 1 413 GLN 413 413 ?   ?   ?   A . n 
A 1 414 PRO 414 414 ?   ?   ?   A . n 
A 1 415 SER 415 415 ?   ?   ?   A . n 
A 1 416 PRO 416 416 ?   ?   ?   A . n 
A 1 417 SER 417 417 ?   ?   ?   A . n 
A 1 418 GLY 418 418 ?   ?   ?   A . n 
A 1 419 ALA 419 419 ?   ?   ?   A . n 
A 1 420 ALA 420 420 ?   ?   ?   A . n 
A 1 421 VAL 421 421 ?   ?   ?   A . n 
A 1 422 ASN 422 422 ?   ?   ?   A . n 
A 1 423 SER 423 423 ?   ?   ?   A . n 
A 1 424 SER 424 424 ?   ?   ?   A . n 
A 1 425 GLU 425 425 ?   ?   ?   A . n 
A 1 426 SER 426 426 ?   ?   ?   A . n 
A 1 427 LEU 427 427 ?   ?   ?   A . n 
A 1 428 PRO 428 428 ?   ?   ?   A . n 
A 1 429 PRO 429 429 ?   ?   ?   A . n 
A 1 430 SER 430 430 ?   ?   ?   A . n 
A 1 431 SER 431 431 ?   ?   ?   A . n 
A 1 432 SER 432 432 ?   ?   ?   A . n 
A 1 433 VAL 433 433 ?   ?   ?   A . n 
A 1 434 ASN 434 434 ?   ?   ?   A . n 
A 1 435 ASP 435 435 ?   ?   ?   A . n 
A 1 436 ILE 436 436 ?   ?   ?   A . n 
A 1 437 SER 437 437 ?   ?   ?   A . n 
A 1 438 SER 438 438 ?   ?   ?   A . n 
A 1 439 MET 439 439 ?   ?   ?   A . n 
A 1 440 SER 440 440 ?   ?   ?   A . n 
A 1 441 THR 441 441 ?   ?   ?   A . n 
A 1 442 ASP 442 442 ?   ?   ?   A . n 
A 1 443 GLN 443 443 ?   ?   ?   A . n 
A 1 444 THR 444 444 ?   ?   ?   A . n 
A 1 445 LEU 445 445 ?   ?   ?   A . n 
A 1 446 ALA 446 446 ?   ?   ?   A . n 
A 1 447 SER 447 447 ?   ?   ?   A . n 
A 1 448 ASP 448 448 ?   ?   ?   A . n 
A 1 449 THR 449 449 ?   ?   ?   A . n 
A 1 450 ASP 450 450 ?   ?   ?   A . n 
A 1 451 SER 451 451 ?   ?   ?   A . n 
A 1 452 SER 452 452 ?   ?   ?   A . n 
A 1 453 LEU 453 453 ?   ?   ?   A . n 
A 1 454 GLU 454 454 ?   ?   ?   A . n 
A 1 455 ALA 455 455 ?   ?   ?   A . n 
A 1 456 SER 456 456 ?   ?   ?   A . n 
A 1 457 ALA 457 457 ?   ?   ?   A . n 
A 1 458 GLY 458 458 ?   ?   ?   A . n 
A 1 459 PRO 459 459 ?   ?   ?   A . n 
A 1 460 LEU 460 460 ?   ?   ?   A . n 
A 1 461 GLY 461 461 ?   ?   ?   A . n 
A 1 462 CYS 462 462 ?   ?   ?   A . n 
A 1 463 CYS 463 463 ?   ?   ?   A . n 
A 1 464 ARG 464 464 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ACP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ACP 
_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 A1ACP 1  1101 1101 A1ACP 23M A . 
C 3 HOH   1  1201 27   HOH   HOH A . 
C 3 HOH   2  1202 7    HOH   HOH A . 
C 3 HOH   3  1203 49   HOH   HOH A . 
C 3 HOH   4  1204 20   HOH   HOH A . 
C 3 HOH   5  1205 30   HOH   HOH A . 
C 3 HOH   6  1206 47   HOH   HOH A . 
C 3 HOH   7  1207 44   HOH   HOH A . 
C 3 HOH   8  1208 29   HOH   HOH A . 
C 3 HOH   9  1209 28   HOH   HOH A . 
C 3 HOH   10 1210 13   HOH   HOH A . 
C 3 HOH   11 1211 45   HOH   HOH A . 
C 3 HOH   12 1212 3    HOH   HOH A . 
C 3 HOH   13 1213 19   HOH   HOH A . 
C 3 HOH   14 1214 14   HOH   HOH A . 
C 3 HOH   15 1215 41   HOH   HOH A . 
C 3 HOH   16 1216 1    HOH   HOH A . 
C 3 HOH   17 1217 37   HOH   HOH A . 
C 3 HOH   18 1218 8    HOH   HOH A . 
C 3 HOH   19 1219 25   HOH   HOH A . 
C 3 HOH   20 1220 23   HOH   HOH A . 
C 3 HOH   21 1221 4    HOH   HOH A . 
C 3 HOH   22 1222 36   HOH   HOH A . 
C 3 HOH   23 1223 6    HOH   HOH A . 
C 3 HOH   24 1224 2    HOH   HOH A . 
C 3 HOH   25 1225 22   HOH   HOH A . 
C 3 HOH   26 1226 12   HOH   HOH A . 
C 3 HOH   27 1227 46   HOH   HOH A . 
C 3 HOH   28 1228 39   HOH   HOH A . 
C 3 HOH   29 1229 9    HOH   HOH A . 
C 3 HOH   30 1230 43   HOH   HOH A . 
C 3 HOH   31 1231 38   HOH   HOH A . 
C 3 HOH   32 1232 40   HOH   HOH A . 
C 3 HOH   33 1233 5    HOH   HOH A . 
C 3 HOH   34 1234 50   HOH   HOH A . 
C 3 HOH   35 1235 24   HOH   HOH A . 
C 3 HOH   36 1236 17   HOH   HOH A . 
C 3 HOH   37 1237 26   HOH   HOH A . 
C 3 HOH   38 1238 16   HOH   HOH A . 
C 3 HOH   39 1239 51   HOH   HOH A . 
C 3 HOH   40 1240 10   HOH   HOH A . 
C 3 HOH   41 1241 31   HOH   HOH A . 
C 3 HOH   42 1242 21   HOH   HOH A . 
C 3 HOH   43 1243 42   HOH   HOH A . 
C 3 HOH   44 1244 34   HOH   HOH A . 
C 3 HOH   45 1245 33   HOH   HOH A . 
C 3 HOH   46 1246 32   HOH   HOH A . 
C 3 HOH   47 1247 35   HOH   HOH A . 
C 3 HOH   48 1248 48   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 GLU 285 ? CG  ? A GLU 285 CG  
2 1 Y 1 A GLU 285 ? CD  ? A GLU 285 CD  
3 1 Y 1 A GLU 285 ? OE1 ? A GLU 285 OE1 
4 1 Y 1 A GLU 285 ? OE2 ? A GLU 285 OE2 
5 1 Y 1 A GLN 379 ? CG  ? A GLN 379 CG  
6 1 Y 1 A GLN 379 ? CD  ? A GLN 379 CD  
7 1 Y 1 A GLN 379 ? OE1 ? A GLN 379 OE1 
8 1 Y 1 A GLN 379 ? NE2 ? A GLN 379 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? iMOSFLM ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VTF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.762 
_cell.length_a_esd                 ? 
_cell.length_b                     71.242 
_cell.length_b_esd                 ? 
_cell.length_c                     107.769 
_cell.length_c_esd                 ? 
_cell.volume                       397412.025 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8VTF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8VTF 
_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             1.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          34.82 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M ammonium tartrate pH 7.2, 18 % PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-09-19 
_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   0.9795 
_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                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          38.66 
_reflns.entry_id                                       8VTF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.02 
_reflns.d_resolution_low                               53.885 
_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                                     15518 
_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                           87.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.02 
_reflns_shell.d_res_low                                     2.055 
_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                             1198 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.734 
_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                               55.22 
_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                                 8VTF 
_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                            2.40 
_refine.ls_d_res_low                             53.88 
_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                     15322 
_refine.ls_number_reflns_R_free                  770 
_refine.ls_number_reflns_R_work                  14552 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.68 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2576 
_refine.ls_R_factor_R_free                       0.2971 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2555 
_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                          1.38 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 32.6383 
_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                            0.3744 
_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                       2.40 
_refine_hist.d_res_low                        53.88 
_refine_hist.number_atoms_solvent             48 
_refine_hist.number_atoms_total               2879 
_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        2800 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0022 ? 2899 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4941 ? 3927 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0401 ? 430  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0039 ? 499  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 7.2472 ? 380  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.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' 2.40 2.59  . . 160 2978 98.59 . . . . 0.3373 . . . . . . . . . . . 0.3915 
'X-RAY DIFFRACTION' 2.59 2.85  . . 130 2428 80.26 . . . . 0.3361 . . . . . . . . . . . 0.3552 
'X-RAY DIFFRACTION' 2.85 3.26  . . 149 2986 98.21 . . . . 0.2886 . . . . . . . . . . . 0.3339 
'X-RAY DIFFRACTION' 3.26 4.10  . . 162 3023 99.01 . . . . 0.2443 . . . . . . . . . . . 0.2971 
'X-RAY DIFFRACTION' 4.10 53.88 . . 169 3137 97.12 . . . . 0.2151 . . . . . . . . . . . 0.2519 
# 
_struct.entry_id                     8VTF 
_struct.title                        
'A structural study of selectivity mechanisms for JNK3 and p38 alpha with indazole scaffold probing compounds' 
_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        8VTF 
_struct_keywords.text            'C-Jun terminal kinase 3, JNK3, p38 alpha, Kinase, selectivity, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MK10_HUMAN 
_struct_ref.pdbx_db_accession          P53779 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSLHFLYYCSEPTLDVKIAFCQGFDKQVDVSYIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCA
AYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQME
LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGY
KENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPA
DSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMN
SEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8VTF 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 464 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P53779 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  464 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       464 
# 
_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 
# 
_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 PRO A 98  ? GLN A 100 ? PRO A 98  GLN A 100 5 ? 3  
HELX_P HELX_P2  AA2 ASN A 101 ? MET A 115 ? ASN A 101 MET A 115 1 ? 15 
HELX_P HELX_P3  AA3 LEU A 153 ? GLN A 158 ? LEU A 153 GLN A 158 1 ? 6  
HELX_P HELX_P4  AA4 ASP A 162 ? ALA A 183 ? ASP A 162 ALA A 183 1 ? 22 
HELX_P HELX_P5  AA5 LYS A 191 ? SER A 193 ? LYS A 191 SER A 193 5 ? 3  
HELX_P HELX_P6  AA6 ALA A 231 ? GLY A 237 ? ALA A 231 GLY A 237 1 ? 7  
HELX_P HELX_P7  AA7 ASN A 243 ? HIS A 259 ? ASN A 243 HIS A 259 1 ? 17 
HELX_P HELX_P8  AA8 ASP A 267 ? GLY A 280 ? ASP A 267 GLY A 280 1 ? 14 
HELX_P HELX_P9  AA9 CYS A 283 ? LYS A 289 ? CYS A 283 LYS A 289 1 ? 7  
HELX_P HELX_P10 AB1 GLN A 291 ? ASN A 300 ? GLN A 291 ASN A 300 1 ? 10 
HELX_P HELX_P11 AB2 THR A 308 ? PHE A 313 ? THR A 308 PHE A 313 1 ? 6  
HELX_P HELX_P12 AB3 PRO A 314 ? PHE A 318 ? PRO A 314 PHE A 318 5 ? 5  
HELX_P HELX_P13 AB4 SER A 322 ? LEU A 340 ? SER A 322 LEU A 340 1 ? 19 
HELX_P HELX_P14 AB5 SER A 349 ? GLN A 355 ? SER A 349 GLN A 355 1 ? 7  
HELX_P HELX_P15 AB6 ILE A 359 ? TYR A 363 ? ILE A 359 TYR A 363 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 364 ? GLU A 369 ? ASP A 364 GLU A 369 1 ? 6  
HELX_P HELX_P17 AB8 THR A 386 ? ASN A 400 ? THR A 386 ASN A 400 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? 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 PHE A 48  ? VAL A 53  ? PHE A 48  VAL A 53  
AA1 2 SER A 56  ? LEU A 61  ? SER A 56  LEU A 61  
AA2 1 TYR A 64  ? SER A 72  ? TYR A 64  SER A 72  
AA2 2 ILE A 77  ? ASP A 83  ? ILE A 77  ASP A 83  
AA2 3 ARG A 88  ? SER A 96  ? ARG A 88  SER A 96  
AA2 4 ASP A 141 ? GLU A 147 ? ASP A 141 GLU A 147 
AA2 5 ASN A 128 ? PHE A 130 ? ASN A 128 PHE A 130 
AA3 1 ALA A 151 ? ASN A 152 ? ALA A 151 ASN A 152 
AA3 2 ILE A 195 ? VAL A 197 ? ILE A 195 VAL A 197 
AA3 3 LEU A 203 ? ILE A 205 ? LEU A 203 ILE A 205 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 51  ? N VAL A 51  O PHE A 58  ? O PHE A 58  
AA2 1 2 N LYS A 68  ? N LYS A 68  O ALA A 80  ? O ALA A 80  
AA2 2 3 N CYS A 79  ? N CYS A 79  O ILE A 92  ? O ILE A 92  
AA2 3 4 N LEU A 95  ? N LEU A 95  O VAL A 142 ? O VAL A 142 
AA2 4 5 O TYR A 143 ? O TYR A 143 N PHE A 130 ? N PHE A 130 
AA3 1 2 N ALA A 151 ? N ALA A 151 O VAL A 197 ? O VAL A 197 
AA3 2 3 N VAL A 196 ? N VAL A 196 O LYS A 204 ? O LYS A 204 
# 
_pdbx_entry_details.entry_id                   8VTF 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    164 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    1201 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
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 GLN A 140 ? ? -131.62 -68.08  
2 1 ARG A 188 ? ? 73.64   -1.60   
3 1 LYS A 241 ? ? -128.04 -154.69 
4 1 ASN A 243 ? ? -68.33  10.00   
5 1 PRO A 319 ? ? -55.39  106.86  
6 1 ASN A 360 ? ? -68.55  2.49    
7 1 LEU A 380 ? ? 56.74   96.21   
8 1 ASP A 381 ? ? -118.45 58.84   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 15.8263207411 10.2535547453 29.0525154101 0.347452462252 ? -0.0641469145383 ? -0.00512148913248 ? 
0.237941014312 ? -0.0459993727234  ? 0.300142590191 ? 1.54799109735  ? -0.264175930171 ? 0.840424468923   ? 2.2399604016  ? 
0.297067232246   ? 2.26728184781 ? 0.0546945235384  ? 0.127339126945     ? -0.0317351243624 ? 0.162170095925  ? -0.257110648093   
? 0.386973574653    ? 0.221233449155  ? 0.0573274938228 ? 0.147588829858 ? 
2 'X-RAY DIFFRACTION' ? refined 21.6088081896 21.5702882314 27.4139555333 0.660656468656 ? 0.0926430911501  ? -0.0355308516756  ? 
0.529985879948 ? -0.110671296649   ? 0.230767732319 ? 1.79961983141  ? -0.83960629077  ? 0.713143754738   ? 1.68842573279 ? 
-0.0577464289186 ? 1.31477124678 ? -0.0638359879207 ? -0.0812667593865   ? 0.697034782515   ? 0.485439274869  ? -0.00749940141951 
? -0.0943553765142  ? -0.457165275148 ? 0.190952403699  ? 0.156666226679 ? 
3 'X-RAY DIFFRACTION' ? refined 16.4176842498 17.4801233402 6.86935492699 0.894820551388 ? 0.164745481919   ? -0.262424470423   ? 
0.416968513338 ? -0.0386884547536  ? 0.334476763108 ? 1.31426858388  ? -0.520851227888 ? -0.0066513812715 ? 2.21535480483 ? 
1.45447214073    ? 1.3249215912  ? 0.527160426019   ? 0.4536272746       ? 0.119185403121   ? -1.55878964685  ? -0.451399081562   
? -0.0130361741182  ? -0.392162692002 ? -0.102759536078 ? 0.578111574062 ? 
4 'X-RAY DIFFRACTION' ? refined 7.73270459595 18.8065231801 31.9358958337 0.663640124823 ? 0.151074466959   ? -0.0598151437736  ? 
0.525623389829 ? -0.245146813841   ? 0.786743010845 ? 0.177611188153 ? 0.441840469975  ? 0.430463220538   ? 2.54378621004 ? 
2.13634885962    ? 1.85859251357 ? -0.154215856792  ? -0.000456524926437 ? 0.32866495089    ? -0.192024972186 ? -0.850573317116   
? 1.54342471466     ? -0.221866468569 ? -0.77200078276  ? 0.738374762313 ? 
5 'X-RAY DIFFRACTION' ? refined 20.2457789854 13.4553648719 40.713464785  0.470982321529 ? -0.0834092832901 ? 0.0688775910908   ? 
0.347281636205 ? -0.00793976371688 ? 0.339752385006 ? 1.41494452269  ? -0.207492506288 ? 1.05468427555    ? 2.86875298549 ? 
1.26403273811    ? 2.32257156457 ? -0.127138382649  ? 0.0122378281651    ? 0.0432077592508  ? 0.795158341358  ? -0.0748056996801  
? -0.00388769398417 ? 0.510082698073  ? 0.224994442981  ? 0.18774205965  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 82  A 126 ? A 158 A 202 ? ? 
;chain 'A' and (resid 126 through 202 )
;
2 'X-RAY DIFFRACTION' 2 A 159 A 203 ? A 176 A 225 ? ? 
;chain 'A' and (resid 203 through 225 )
;
3 'X-RAY DIFFRACTION' 3 A 177 A 226 ? A 306 A 355 ? ? 
;chain 'A' and (resid 226 through 355 )
;
4 'X-RAY DIFFRACTION' 4 A 307 A 356 ? A 346 A 400 ? ? 
;chain 'A' and (resid 356 through 400 )
;
5 'X-RAY DIFFRACTION' 5 A 1   A 45  ? A 81  A 125 ? ? 
;chain 'A' and (resid 45 through 125 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A SER 2   ? A SER 2   
3   1 Y 1 A LEU 3   ? A LEU 3   
4   1 Y 1 A HIS 4   ? A HIS 4   
5   1 Y 1 A PHE 5   ? A PHE 5   
6   1 Y 1 A LEU 6   ? A LEU 6   
7   1 Y 1 A TYR 7   ? A TYR 7   
8   1 Y 1 A TYR 8   ? A TYR 8   
9   1 Y 1 A CYS 9   ? A CYS 9   
10  1 Y 1 A SER 10  ? A SER 10  
11  1 Y 1 A GLU 11  ? A GLU 11  
12  1 Y 1 A PRO 12  ? A PRO 12  
13  1 Y 1 A THR 13  ? A THR 13  
14  1 Y 1 A LEU 14  ? A LEU 14  
15  1 Y 1 A ASP 15  ? A ASP 15  
16  1 Y 1 A VAL 16  ? A VAL 16  
17  1 Y 1 A LYS 17  ? A LYS 17  
18  1 Y 1 A ILE 18  ? A ILE 18  
19  1 Y 1 A ALA 19  ? A ALA 19  
20  1 Y 1 A PHE 20  ? A PHE 20  
21  1 Y 1 A CYS 21  ? A CYS 21  
22  1 Y 1 A GLN 22  ? A GLN 22  
23  1 Y 1 A GLY 23  ? A GLY 23  
24  1 Y 1 A PHE 24  ? A PHE 24  
25  1 Y 1 A ASP 25  ? A ASP 25  
26  1 Y 1 A LYS 26  ? A LYS 26  
27  1 Y 1 A GLN 27  ? A GLN 27  
28  1 Y 1 A VAL 28  ? A VAL 28  
29  1 Y 1 A ASP 29  ? A ASP 29  
30  1 Y 1 A VAL 30  ? A VAL 30  
31  1 Y 1 A SER 31  ? A SER 31  
32  1 Y 1 A TYR 32  ? A TYR 32  
33  1 Y 1 A ILE 33  ? A ILE 33  
34  1 Y 1 A ALA 34  ? A ALA 34  
35  1 Y 1 A LYS 35  ? A LYS 35  
36  1 Y 1 A HIS 36  ? A HIS 36  
37  1 Y 1 A TYR 37  ? A TYR 37  
38  1 Y 1 A ASN 38  ? A ASN 38  
39  1 Y 1 A MET 39  ? A MET 39  
40  1 Y 1 A SER 40  ? A SER 40  
41  1 Y 1 A LYS 41  ? A LYS 41  
42  1 Y 1 A SER 42  ? A SER 42  
43  1 Y 1 A LYS 43  ? A LYS 43  
44  1 Y 1 A VAL 44  ? A VAL 44  
45  1 Y 1 A ARG 212 ? A ARG 212 
46  1 Y 1 A THR 213 ? A THR 213 
47  1 Y 1 A ALA 214 ? A ALA 214 
48  1 Y 1 A GLY 215 ? A GLY 215 
49  1 Y 1 A THR 216 ? A THR 216 
50  1 Y 1 A GLN 374 ? A GLN 374 
51  1 Y 1 A ILE 375 ? A ILE 375 
52  1 Y 1 A TYR 376 ? A TYR 376 
53  1 Y 1 A ASP 377 ? A ASP 377 
54  1 Y 1 A LYS 378 ? A LYS 378 
55  1 Y 1 A SER 401 ? A SER 401 
56  1 Y 1 A GLU 402 ? A GLU 402 
57  1 Y 1 A GLU 403 ? A GLU 403 
58  1 Y 1 A LYS 404 ? A LYS 404 
59  1 Y 1 A THR 405 ? A THR 405 
60  1 Y 1 A LYS 406 ? A LYS 406 
61  1 Y 1 A ASN 407 ? A ASN 407 
62  1 Y 1 A GLY 408 ? A GLY 408 
63  1 Y 1 A VAL 409 ? A VAL 409 
64  1 Y 1 A VAL 410 ? A VAL 410 
65  1 Y 1 A LYS 411 ? A LYS 411 
66  1 Y 1 A GLY 412 ? A GLY 412 
67  1 Y 1 A GLN 413 ? A GLN 413 
68  1 Y 1 A PRO 414 ? A PRO 414 
69  1 Y 1 A SER 415 ? A SER 415 
70  1 Y 1 A PRO 416 ? A PRO 416 
71  1 Y 1 A SER 417 ? A SER 417 
72  1 Y 1 A GLY 418 ? A GLY 418 
73  1 Y 1 A ALA 419 ? A ALA 419 
74  1 Y 1 A ALA 420 ? A ALA 420 
75  1 Y 1 A VAL 421 ? A VAL 421 
76  1 Y 1 A ASN 422 ? A ASN 422 
77  1 Y 1 A SER 423 ? A SER 423 
78  1 Y 1 A SER 424 ? A SER 424 
79  1 Y 1 A GLU 425 ? A GLU 425 
80  1 Y 1 A SER 426 ? A SER 426 
81  1 Y 1 A LEU 427 ? A LEU 427 
82  1 Y 1 A PRO 428 ? A PRO 428 
83  1 Y 1 A PRO 429 ? A PRO 429 
84  1 Y 1 A SER 430 ? A SER 430 
85  1 Y 1 A SER 431 ? A SER 431 
86  1 Y 1 A SER 432 ? A SER 432 
87  1 Y 1 A VAL 433 ? A VAL 433 
88  1 Y 1 A ASN 434 ? A ASN 434 
89  1 Y 1 A ASP 435 ? A ASP 435 
90  1 Y 1 A ILE 436 ? A ILE 436 
91  1 Y 1 A SER 437 ? A SER 437 
92  1 Y 1 A SER 438 ? A SER 438 
93  1 Y 1 A MET 439 ? A MET 439 
94  1 Y 1 A SER 440 ? A SER 440 
95  1 Y 1 A THR 441 ? A THR 441 
96  1 Y 1 A ASP 442 ? A ASP 442 
97  1 Y 1 A GLN 443 ? A GLN 443 
98  1 Y 1 A THR 444 ? A THR 444 
99  1 Y 1 A LEU 445 ? A LEU 445 
100 1 Y 1 A ALA 446 ? A ALA 446 
101 1 Y 1 A SER 447 ? A SER 447 
102 1 Y 1 A ASP 448 ? A ASP 448 
103 1 Y 1 A THR 449 ? A THR 449 
104 1 Y 1 A ASP 450 ? A ASP 450 
105 1 Y 1 A SER 451 ? A SER 451 
106 1 Y 1 A SER 452 ? A SER 452 
107 1 Y 1 A LEU 453 ? A LEU 453 
108 1 Y 1 A GLU 454 ? A GLU 454 
109 1 Y 1 A ALA 455 ? A ALA 455 
110 1 Y 1 A SER 456 ? A SER 456 
111 1 Y 1 A ALA 457 ? A ALA 457 
112 1 Y 1 A GLY 458 ? A GLY 458 
113 1 Y 1 A PRO 459 ? A PRO 459 
114 1 Y 1 A LEU 460 ? A LEU 460 
115 1 Y 1 A GLY 461 ? A GLY 461 
116 1 Y 1 A CYS 462 ? A CYS 462 
117 1 Y 1 A CYS 463 ? A CYS 463 
118 1 Y 1 A ARG 464 ? A ARG 464 
# 
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 
A1ACP C1   C Y N 1   
A1ACP C2   C Y N 2   
A1ACP N3   N N N 3   
A1ACP C4   C Y N 4   
A1ACP C5   C Y N 5   
A1ACP C6   C Y N 6   
A1ACP C7   C Y N 7   
A1ACP C8   C Y N 8   
A1ACP C9   C Y N 9   
A1ACP C10  C Y N 10  
A1ACP C11  C Y N 11  
A1ACP C12  C Y N 12  
A1ACP C13  C N N 13  
A1ACP C14  C N N 14  
A1ACP C15  C Y N 15  
A1ACP C16  C Y N 16  
A1ACP C17  C Y N 17  
A1ACP C18  C Y N 18  
A1ACP C19  C Y N 19  
A1ACP C20  C N N 20  
A1ACP C21  C N N 21  
A1ACP C22  C N N 22  
A1ACP C3   C Y N 23  
A1ACP F1   F N N 24  
A1ACP N1   N Y N 25  
A1ACP N2   N Y N 26  
A1ACP N4   N N N 27  
A1ACP O1   O N N 28  
A1ACP O2   O N N 29  
A1ACP O3   O N N 30  
A1ACP S1   S Y N 31  
A1ACP H4   H N N 32  
A1ACP H1   H N N 33  
A1ACP H2   H N N 34  
A1ACP H3   H N N 35  
A1ACP H5   H N N 36  
A1ACP H6   H N N 37  
A1ACP H8   H N N 38  
A1ACP H9   H N N 39  
A1ACP H10  H N N 40  
A1ACP H11  H N N 41  
A1ACP H12  H N N 42  
A1ACP H13  H N N 43  
A1ACP H14  H N N 44  
A1ACP H16  H N N 45  
A1ACP H15  H N N 46  
A1ACP H17  H N N 47  
A1ACP H18  H N N 48  
A1ACP H19  H N N 49  
A1ACP H7   H N N 50  
ALA   N    N N N 51  
ALA   CA   C N S 52  
ALA   C    C N N 53  
ALA   O    O N N 54  
ALA   CB   C N N 55  
ALA   OXT  O N N 56  
ALA   H    H N N 57  
ALA   H2   H N N 58  
ALA   HA   H N N 59  
ALA   HB1  H N N 60  
ALA   HB2  H N N 61  
ALA   HB3  H N N 62  
ALA   HXT  H N N 63  
ARG   N    N N N 64  
ARG   CA   C N S 65  
ARG   C    C N N 66  
ARG   O    O N N 67  
ARG   CB   C N N 68  
ARG   CG   C N N 69  
ARG   CD   C N N 70  
ARG   NE   N N N 71  
ARG   CZ   C N N 72  
ARG   NH1  N N N 73  
ARG   NH2  N N N 74  
ARG   OXT  O N N 75  
ARG   H    H N N 76  
ARG   H2   H N N 77  
ARG   HA   H N N 78  
ARG   HB2  H N N 79  
ARG   HB3  H N N 80  
ARG   HG2  H N N 81  
ARG   HG3  H N N 82  
ARG   HD2  H N N 83  
ARG   HD3  H N N 84  
ARG   HE   H N N 85  
ARG   HH11 H N N 86  
ARG   HH12 H N N 87  
ARG   HH21 H N N 88  
ARG   HH22 H N N 89  
ARG   HXT  H N N 90  
ASN   N    N N N 91  
ASN   CA   C N S 92  
ASN   C    C N N 93  
ASN   O    O N N 94  
ASN   CB   C N N 95  
ASN   CG   C N N 96  
ASN   OD1  O N N 97  
ASN   ND2  N N N 98  
ASN   OXT  O N N 99  
ASN   H    H N N 100 
ASN   H2   H N N 101 
ASN   HA   H N N 102 
ASN   HB2  H N N 103 
ASN   HB3  H N N 104 
ASN   HD21 H N N 105 
ASN   HD22 H N N 106 
ASN   HXT  H N N 107 
ASP   N    N N N 108 
ASP   CA   C N S 109 
ASP   C    C N N 110 
ASP   O    O N N 111 
ASP   CB   C N N 112 
ASP   CG   C N N 113 
ASP   OD1  O N N 114 
ASP   OD2  O N N 115 
ASP   OXT  O N N 116 
ASP   H    H N N 117 
ASP   H2   H N N 118 
ASP   HA   H N N 119 
ASP   HB2  H N N 120 
ASP   HB3  H N N 121 
ASP   HD2  H N N 122 
ASP   HXT  H N N 123 
CYS   N    N N N 124 
CYS   CA   C N R 125 
CYS   C    C N N 126 
CYS   O    O N N 127 
CYS   CB   C N N 128 
CYS   SG   S N N 129 
CYS   OXT  O N N 130 
CYS   H    H N N 131 
CYS   H2   H N N 132 
CYS   HA   H N N 133 
CYS   HB2  H N N 134 
CYS   HB3  H N N 135 
CYS   HG   H N N 136 
CYS   HXT  H N N 137 
GLN   N    N N N 138 
GLN   CA   C N S 139 
GLN   C    C N N 140 
GLN   O    O N N 141 
GLN   CB   C N N 142 
GLN   CG   C N N 143 
GLN   CD   C N N 144 
GLN   OE1  O N N 145 
GLN   NE2  N N N 146 
GLN   OXT  O N N 147 
GLN   H    H N N 148 
GLN   H2   H N N 149 
GLN   HA   H N N 150 
GLN   HB2  H N N 151 
GLN   HB3  H N N 152 
GLN   HG2  H N N 153 
GLN   HG3  H N N 154 
GLN   HE21 H N N 155 
GLN   HE22 H N N 156 
GLN   HXT  H N N 157 
GLU   N    N N N 158 
GLU   CA   C N S 159 
GLU   C    C N N 160 
GLU   O    O N N 161 
GLU   CB   C N N 162 
GLU   CG   C N N 163 
GLU   CD   C N N 164 
GLU   OE1  O N N 165 
GLU   OE2  O N N 166 
GLU   OXT  O N N 167 
GLU   H    H N N 168 
GLU   H2   H N N 169 
GLU   HA   H N N 170 
GLU   HB2  H N N 171 
GLU   HB3  H N N 172 
GLU   HG2  H N N 173 
GLU   HG3  H N N 174 
GLU   HE2  H N N 175 
GLU   HXT  H N N 176 
GLY   N    N N N 177 
GLY   CA   C N N 178 
GLY   C    C N N 179 
GLY   O    O N N 180 
GLY   OXT  O N N 181 
GLY   H    H N N 182 
GLY   H2   H N N 183 
GLY   HA2  H N N 184 
GLY   HA3  H N N 185 
GLY   HXT  H N N 186 
HIS   N    N N N 187 
HIS   CA   C N S 188 
HIS   C    C N N 189 
HIS   O    O N N 190 
HIS   CB   C N N 191 
HIS   CG   C Y N 192 
HIS   ND1  N Y N 193 
HIS   CD2  C Y N 194 
HIS   CE1  C Y N 195 
HIS   NE2  N Y N 196 
HIS   OXT  O N N 197 
HIS   H    H N N 198 
HIS   H2   H N N 199 
HIS   HA   H N N 200 
HIS   HB2  H N N 201 
HIS   HB3  H N N 202 
HIS   HD1  H N N 203 
HIS   HD2  H N N 204 
HIS   HE1  H N N 205 
HIS   HE2  H N N 206 
HIS   HXT  H N N 207 
HOH   O    O N N 208 
HOH   H1   H N N 209 
HOH   H2   H N N 210 
ILE   N    N N N 211 
ILE   CA   C N S 212 
ILE   C    C N N 213 
ILE   O    O N N 214 
ILE   CB   C N S 215 
ILE   CG1  C N N 216 
ILE   CG2  C N N 217 
ILE   CD1  C N N 218 
ILE   OXT  O N N 219 
ILE   H    H N N 220 
ILE   H2   H N N 221 
ILE   HA   H N N 222 
ILE   HB   H N N 223 
ILE   HG12 H N N 224 
ILE   HG13 H N N 225 
ILE   HG21 H N N 226 
ILE   HG22 H N N 227 
ILE   HG23 H N N 228 
ILE   HD11 H N N 229 
ILE   HD12 H N N 230 
ILE   HD13 H N N 231 
ILE   HXT  H N N 232 
LEU   N    N N N 233 
LEU   CA   C N S 234 
LEU   C    C N N 235 
LEU   O    O N N 236 
LEU   CB   C N N 237 
LEU   CG   C N N 238 
LEU   CD1  C N N 239 
LEU   CD2  C N N 240 
LEU   OXT  O N N 241 
LEU   H    H N N 242 
LEU   H2   H N N 243 
LEU   HA   H N N 244 
LEU   HB2  H N N 245 
LEU   HB3  H N N 246 
LEU   HG   H N N 247 
LEU   HD11 H N N 248 
LEU   HD12 H N N 249 
LEU   HD13 H N N 250 
LEU   HD21 H N N 251 
LEU   HD22 H N N 252 
LEU   HD23 H N N 253 
LEU   HXT  H N N 254 
LYS   N    N N N 255 
LYS   CA   C N S 256 
LYS   C    C N N 257 
LYS   O    O N N 258 
LYS   CB   C N N 259 
LYS   CG   C N N 260 
LYS   CD   C N N 261 
LYS   CE   C N N 262 
LYS   NZ   N N N 263 
LYS   OXT  O N N 264 
LYS   H    H N N 265 
LYS   H2   H N N 266 
LYS   HA   H N N 267 
LYS   HB2  H N N 268 
LYS   HB3  H N N 269 
LYS   HG2  H N N 270 
LYS   HG3  H N N 271 
LYS   HD2  H N N 272 
LYS   HD3  H N N 273 
LYS   HE2  H N N 274 
LYS   HE3  H N N 275 
LYS   HZ1  H N N 276 
LYS   HZ2  H N N 277 
LYS   HZ3  H N N 278 
LYS   HXT  H N N 279 
MET   N    N N N 280 
MET   CA   C N S 281 
MET   C    C N N 282 
MET   O    O N N 283 
MET   CB   C N N 284 
MET   CG   C N N 285 
MET   SD   S N N 286 
MET   CE   C N N 287 
MET   OXT  O N N 288 
MET   H    H N N 289 
MET   H2   H N N 290 
MET   HA   H N N 291 
MET   HB2  H N N 292 
MET   HB3  H N N 293 
MET   HG2  H N N 294 
MET   HG3  H N N 295 
MET   HE1  H N N 296 
MET   HE2  H N N 297 
MET   HE3  H N N 298 
MET   HXT  H N N 299 
PHE   N    N N N 300 
PHE   CA   C N S 301 
PHE   C    C N N 302 
PHE   O    O N N 303 
PHE   CB   C N N 304 
PHE   CG   C Y N 305 
PHE   CD1  C Y N 306 
PHE   CD2  C Y N 307 
PHE   CE1  C Y N 308 
PHE   CE2  C Y N 309 
PHE   CZ   C Y N 310 
PHE   OXT  O N N 311 
PHE   H    H N N 312 
PHE   H2   H N N 313 
PHE   HA   H N N 314 
PHE   HB2  H N N 315 
PHE   HB3  H N N 316 
PHE   HD1  H N N 317 
PHE   HD2  H N N 318 
PHE   HE1  H N N 319 
PHE   HE2  H N N 320 
PHE   HZ   H N N 321 
PHE   HXT  H N N 322 
PRO   N    N N N 323 
PRO   CA   C N S 324 
PRO   C    C N N 325 
PRO   O    O N N 326 
PRO   CB   C N N 327 
PRO   CG   C N N 328 
PRO   CD   C N N 329 
PRO   OXT  O N N 330 
PRO   H    H N N 331 
PRO   HA   H N N 332 
PRO   HB2  H N N 333 
PRO   HB3  H N N 334 
PRO   HG2  H N N 335 
PRO   HG3  H N N 336 
PRO   HD2  H N N 337 
PRO   HD3  H N N 338 
PRO   HXT  H N N 339 
SER   N    N N N 340 
SER   CA   C N S 341 
SER   C    C N N 342 
SER   O    O N N 343 
SER   CB   C N N 344 
SER   OG   O N N 345 
SER   OXT  O N N 346 
SER   H    H N N 347 
SER   H2   H N N 348 
SER   HA   H N N 349 
SER   HB2  H N N 350 
SER   HB3  H N N 351 
SER   HG   H N N 352 
SER   HXT  H N N 353 
THR   N    N N N 354 
THR   CA   C N S 355 
THR   C    C N N 356 
THR   O    O N N 357 
THR   CB   C N R 358 
THR   OG1  O N N 359 
THR   CG2  C N N 360 
THR   OXT  O N N 361 
THR   H    H N N 362 
THR   H2   H N N 363 
THR   HA   H N N 364 
THR   HB   H N N 365 
THR   HG1  H N N 366 
THR   HG21 H N N 367 
THR   HG22 H N N 368 
THR   HG23 H N N 369 
THR   HXT  H N N 370 
TRP   N    N N N 371 
TRP   CA   C N S 372 
TRP   C    C N N 373 
TRP   O    O N N 374 
TRP   CB   C N N 375 
TRP   CG   C Y N 376 
TRP   CD1  C Y N 377 
TRP   CD2  C Y N 378 
TRP   NE1  N Y N 379 
TRP   CE2  C Y N 380 
TRP   CE3  C Y N 381 
TRP   CZ2  C Y N 382 
TRP   CZ3  C Y N 383 
TRP   CH2  C Y N 384 
TRP   OXT  O N N 385 
TRP   H    H N N 386 
TRP   H2   H N N 387 
TRP   HA   H N N 388 
TRP   HB2  H N N 389 
TRP   HB3  H N N 390 
TRP   HD1  H N N 391 
TRP   HE1  H N N 392 
TRP   HE3  H N N 393 
TRP   HZ2  H N N 394 
TRP   HZ3  H N N 395 
TRP   HH2  H N N 396 
TRP   HXT  H N N 397 
TYR   N    N N N 398 
TYR   CA   C N S 399 
TYR   C    C N N 400 
TYR   O    O N N 401 
TYR   CB   C N N 402 
TYR   CG   C Y N 403 
TYR   CD1  C Y N 404 
TYR   CD2  C Y N 405 
TYR   CE1  C Y N 406 
TYR   CE2  C Y N 407 
TYR   CZ   C Y N 408 
TYR   OH   O N N 409 
TYR   OXT  O N N 410 
TYR   H    H N N 411 
TYR   H2   H N N 412 
TYR   HA   H N N 413 
TYR   HB2  H N N 414 
TYR   HB3  H N N 415 
TYR   HD1  H N N 416 
TYR   HD2  H N N 417 
TYR   HE1  H N N 418 
TYR   HE2  H N N 419 
TYR   HH   H N N 420 
TYR   HXT  H N N 421 
VAL   N    N N N 422 
VAL   CA   C N S 423 
VAL   C    C N N 424 
VAL   O    O N N 425 
VAL   CB   C N N 426 
VAL   CG1  C N N 427 
VAL   CG2  C N N 428 
VAL   OXT  O N N 429 
VAL   H    H N N 430 
VAL   H2   H N N 431 
VAL   HA   H N N 432 
VAL   HB   H N N 433 
VAL   HG11 H N N 434 
VAL   HG12 H N N 435 
VAL   HG13 H N N 436 
VAL   HG21 H N N 437 
VAL   HG22 H N N 438 
VAL   HG23 H N N 439 
VAL   HXT  H N N 440 
# 
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 
A1ACP C1  N1   sing N N 1   
A1ACP C1  C10  sing Y N 2   
A1ACP C1  C12  doub Y N 3   
A1ACP N1  C2   sing Y N 4   
A1ACP N1  N2   sing Y N 5   
A1ACP C2  C3   doub Y N 6   
A1ACP C2  C5   sing Y N 7   
A1ACP C3  C4   sing Y N 8   
A1ACP C3  C8   sing Y N 9   
A1ACP C4  N2   doub Y N 10  
A1ACP C5  C6   doub Y N 11  
A1ACP C6  C7   sing Y N 12  
A1ACP C6  F1   sing N N 13  
A1ACP C7  C8   doub Y N 14  
A1ACP C7  N3   sing N N 15  
A1ACP N3  C9   sing N N 16  
A1ACP C9  C15  doub Y N 17  
A1ACP C9  C19  sing Y N 18  
A1ACP C10 C11  doub Y N 19  
A1ACP C11 S1   sing Y N 20  
A1ACP C11 C13  sing N N 21  
A1ACP S1  C12  sing Y N 22  
A1ACP C13 O1   doub N N 23  
A1ACP C13 N4   sing N N 24  
A1ACP N4  C14  sing N N 25  
A1ACP C14 C20  sing N N 26  
A1ACP C14 C21  sing N N 27  
A1ACP C15 O3   sing N N 28  
A1ACP C15 C16  sing Y N 29  
A1ACP C16 C17  doub Y N 30  
A1ACP C17 C18  sing Y N 31  
A1ACP C18 C19  doub Y N 32  
A1ACP C20 O2   sing N N 33  
A1ACP O2  C21  sing N N 34  
A1ACP O3  C22  sing N N 35  
A1ACP N3  H4   sing N N 36  
A1ACP C4  H1   sing N N 37  
A1ACP C5  H2   sing N N 38  
A1ACP C8  H3   sing N N 39  
A1ACP C10 H5   sing N N 40  
A1ACP C12 H6   sing N N 41  
A1ACP C14 H8   sing N N 42  
A1ACP C16 H9   sing N N 43  
A1ACP C17 H10  sing N N 44  
A1ACP C18 H11  sing N N 45  
A1ACP C19 H12  sing N N 46  
A1ACP C20 H13  sing N N 47  
A1ACP C20 H14  sing N N 48  
A1ACP C21 H16  sing N N 49  
A1ACP C21 H15  sing N N 50  
A1ACP C22 H17  sing N N 51  
A1ACP C22 H18  sing N N 52  
A1ACP C22 H19  sing N N 53  
A1ACP N4  H7   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 Institutes of Health/National Institute on Aging (NIH/NIA)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_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   1JNK 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8VTF 
_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]   0.019319 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014037 
_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]   0.009279 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F   ? ? 8.95735 ?       ? ? 7.27484  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 45  ? 24.63253 8.77488   62.44586 1.000 78.71064  ?  45   ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 45  ? 23.31935 9.38715   62.60341 1.000 84.91551  ?  45   ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 45  ? 23.02094 10.33552  61.44584 1.000 79.15679  ?  45   ASP   A C   1 
ATOM   4    O O   . ASP   A 1 45  ? 21.86021 10.61060  61.14039 1.000 76.18480  ?  45   ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 45  ? 23.22948 10.13337  63.93580 1.000 85.25800  ?  45   ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 45  ? 21.86500 10.00505  64.58350 1.000 90.46008  ?  45   ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 45  ? 21.80632 9.83489   65.81947 1.000 105.11025 ?  45   ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 45  ? 20.85136 10.07509  63.85729 1.000 86.05318  -1 45   ASP   A OD2 1 
ATOM   9    N N   . ASN   A 1 46  ? 24.07788 10.83593  60.81080 1.000 70.62054  ?  46   ASN   A N   1 
ATOM   10   C CA  . ASN   A 1 46  ? 23.92109 11.66751  59.62506 1.000 66.37532  ?  46   ASN   A CA  1 
ATOM   11   C C   . ASN   A 1 46  ? 23.32786 10.83136  58.49744 1.000 62.58009  ?  46   ASN   A C   1 
ATOM   12   O O   . ASN   A 1 46  ? 23.93742 9.85166   58.05309 1.000 60.11807  ?  46   ASN   A O   1 
ATOM   13   C CB  . ASN   A 1 46  ? 25.26624 12.25700  59.20901 1.000 71.74788  ?  46   ASN   A CB  1 
ATOM   14   C CG  . ASN   A 1 46  ? 25.14822 13.21765  58.03974 1.000 70.31720  ?  46   ASN   A CG  1 
ATOM   15   O OD1 . ASN   A 1 46  ? 24.06846 13.73130  57.74716 1.000 66.66889  ?  46   ASN   A OD1 1 
ATOM   16   N ND2 . ASN   A 1 46  ? 26.26456 13.46331  57.36255 1.000 66.48439  ?  46   ASN   A ND2 1 
ATOM   17   N N   . GLN   A 1 47  ? 22.13895 11.21303  58.03575 1.000 57.82929  ?  47   GLN   A N   1 
ATOM   18   C CA  . GLN   A 1 47  ? 21.44453 10.46930  56.99237 1.000 58.82091  ?  47   GLN   A CA  1 
ATOM   19   C C   . GLN   A 1 47  ? 22.03183 10.70085  55.60280 1.000 51.08329  ?  47   GLN   A C   1 
ATOM   20   O O   . GLN   A 1 47  ? 21.41461 10.29654  54.61217 1.000 49.66839  ?  47   GLN   A O   1 
ATOM   21   C CB  . GLN   A 1 47  ? 19.95429 10.82293  56.99970 1.000 53.87443  ?  47   GLN   A CB  1 
ATOM   22   C CG  . GLN   A 1 47  ? 19.64402 12.24162  56.56217 1.000 52.55819  ?  47   GLN   A CG  1 
ATOM   23   C CD  . GLN   A 1 47  ? 18.26115 12.69511  56.98604 1.000 52.16818  ?  47   GLN   A CD  1 
ATOM   24   O OE1 . GLN   A 1 47  ? 17.25421 12.10443  56.59444 1.000 52.19143  ?  47   GLN   A OE1 1 
ATOM   25   N NE2 . GLN   A 1 47  ? 18.20499 13.75299  57.78666 1.000 52.87244  ?  47   GLN   A NE2 1 
ATOM   26   N N   . PHE   A 1 48  ? 23.20099 11.33189  55.50938 1.000 51.34039  ?  48   PHE   A N   1 
ATOM   27   C CA  . PHE   A 1 48  ? 23.88909 11.54220  54.24556 1.000 49.62241  ?  48   PHE   A CA  1 
ATOM   28   C C   . PHE   A 1 48  ? 25.34008 11.10058  54.37470 1.000 49.47613  ?  48   PHE   A C   1 
ATOM   29   O O   . PHE   A 1 48  ? 25.87971 10.97559  55.47657 1.000 51.62420  ?  48   PHE   A O   1 
ATOM   30   C CB  . PHE   A 1 48  ? 23.84012 13.01374  53.80366 1.000 51.18009  ?  48   PHE   A CB  1 
ATOM   31   C CG  . PHE   A 1 48  ? 22.46692 13.49716  53.43890 1.000 47.21647  ?  48   PHE   A CG  1 
ATOM   32   C CD1 . PHE   A 1 48  ? 21.66225 14.11283  54.38160 1.000 46.33078  ?  48   PHE   A CD1 1 
ATOM   33   C CD2 . PHE   A 1 48  ? 21.98461 13.34500  52.14955 1.000 43.42290  ?  48   PHE   A CD2 1 
ATOM   34   C CE1 . PHE   A 1 48  ? 20.39895 14.56310  54.04768 1.000 46.78333  ?  48   PHE   A CE1 1 
ATOM   35   C CE2 . PHE   A 1 48  ? 20.72241 13.79325  51.80931 1.000 43.31502  ?  48   PHE   A CE2 1 
ATOM   36   C CZ  . PHE   A 1 48  ? 19.92832 14.40242  52.76038 1.000 46.86117  ?  48   PHE   A CZ  1 
ATOM   37   N N   . TYR   A 1 49  ? 25.96804 10.86779  53.22484 1.000 48.12557  ?  49   TYR   A N   1 
ATOM   38   C CA  . TYR   A 1 49  ? 27.38936 10.56114  53.16776 1.000 49.03848  ?  49   TYR   A CA  1 
ATOM   39   C C   . TYR   A 1 49  ? 27.92419 11.02359  51.82047 1.000 47.03527  ?  49   TYR   A C   1 
ATOM   40   O O   . TYR   A 1 49  ? 27.18212 11.12775  50.84034 1.000 45.14167  ?  49   TYR   A O   1 
ATOM   41   C CB  . TYR   A 1 49  ? 27.66082 9.06699   53.39135 1.000 50.85313  ?  49   TYR   A CB  1 
ATOM   42   C CG  . TYR   A 1 49  ? 27.29204 8.18004   52.22445 1.000 49.68804  ?  49   TYR   A CG  1 
ATOM   43   C CD1 . TYR   A 1 49  ? 25.96516 7.99183   51.86001 1.000 48.61645  ?  49   TYR   A CD1 1 
ATOM   44   C CD2 . TYR   A 1 49  ? 28.27113 7.52284   51.49290 1.000 49.86381  ?  49   TYR   A CD2 1 
ATOM   45   C CE1 . TYR   A 1 49  ? 25.62482 7.17886   50.79564 1.000 47.68166  ?  49   TYR   A CE1 1 
ATOM   46   C CE2 . TYR   A 1 49  ? 27.93964 6.70583   50.42946 1.000 48.94214  ?  49   TYR   A CE2 1 
ATOM   47   C CZ  . TYR   A 1 49  ? 26.61683 6.53948   50.08333 1.000 47.81833  ?  49   TYR   A CZ  1 
ATOM   48   O OH  . TYR   A 1 49  ? 26.28706 5.72950   49.02257 1.000 47.01403  ?  49   TYR   A OH  1 
ATOM   49   N N   . SER   A 1 50  ? 29.22349 11.30594  51.78183 1.000 47.68661  ?  50   SER   A N   1 
ATOM   50   C CA  . SER   A 1 50  ? 29.85983 11.92520  50.62658 1.000 48.25815  ?  50   SER   A CA  1 
ATOM   51   C C   . SER   A 1 50  ? 30.78906 10.93635  49.93642 1.000 48.99626  ?  50   SER   A C   1 
ATOM   52   O O   . SER   A 1 50  ? 31.59954 10.27455  50.59337 1.000 51.01779  ?  50   SER   A O   1 
ATOM   53   C CB  . SER   A 1 50  ? 30.63906 13.17464  51.04254 1.000 46.76609  ?  50   SER   A CB  1 
ATOM   54   O OG  . SER   A 1 50  ? 29.92264 13.92217  52.00963 1.000 52.16694  ?  50   SER   A OG  1 
ATOM   55   N N   . VAL   A 1 51  ? 30.66802 10.84369  48.61330 1.000 51.98665  ?  51   VAL   A N   1 
ATOM   56   C CA  . VAL   A 1 51  ? 31.55617 10.04450  47.77816 1.000 55.04507  ?  51   VAL   A CA  1 
ATOM   57   C C   . VAL   A 1 51  ? 32.16000 10.95471  46.71961 1.000 58.00493  ?  51   VAL   A C   1 
ATOM   58   O O   . VAL   A 1 51  ? 31.49729 11.87614  46.23011 1.000 57.06053  ?  51   VAL   A O   1 
ATOM   59   C CB  . VAL   A 1 51  ? 30.82281 8.86173   47.11125 1.000 52.00711  ?  51   VAL   A CB  1 
ATOM   60   C CG1 . VAL   A 1 51  ? 31.81173 7.77010   46.73375 1.000 55.71457  ?  51   VAL   A CG1 1 
ATOM   61   C CG2 . VAL   A 1 51  ? 29.74153 8.31891   48.02217 1.000 45.73751  ?  51   VAL   A CG2 1 
ATOM   62   N N   . GLU   A 1 52  ? 33.41399 10.69142  46.36236 1.000 61.22800  ?  52   GLU   A N   1 
ATOM   63   C CA  . GLU   A 1 52  ? 34.12518 11.47144  45.35211 1.000 67.47795  ?  52   GLU   A CA  1 
ATOM   64   C C   . GLU   A 1 52  ? 34.11776 10.67870  44.04878 1.000 71.45102  ?  52   GLU   A C   1 
ATOM   65   O O   . GLU   A 1 52  ? 34.95567 9.79799   43.83898 1.000 73.98329  ?  52   GLU   A O   1 
ATOM   66   C CB  . GLU   A 1 52  ? 35.54582 11.78922  45.80757 1.000 69.82624  ?  52   GLU   A CB  1 
ATOM   67   C CG  . GLU   A 1 52  ? 35.67481 13.08071  46.60353 1.000 71.97490  ?  52   GLU   A CG  1 
ATOM   68   C CD  . GLU   A 1 52  ? 34.54256 13.27252  47.59311 1.000 72.86279  ?  52   GLU   A CD  1 
ATOM   69   O OE1 . GLU   A 1 52  ? 34.54349 12.59437  48.64199 1.000 76.47826  ?  52   GLU   A OE1 1 
ATOM   70   O OE2 . GLU   A 1 52  ? 33.64908 14.09581  47.31969 1.000 65.14601  -1 52   GLU   A OE2 1 
ATOM   71   N N   . VAL   A 1 53  ? 33.16530 10.99071  43.17563 1.000 68.75635  ?  53   VAL   A N   1 
ATOM   72   C CA  . VAL   A 1 53  ? 33.05291 10.36045  41.86555 1.000 66.83112  ?  53   VAL   A CA  1 
ATOM   73   C C   . VAL   A 1 53  ? 33.71534 11.28600  40.85515 1.000 69.71064  ?  53   VAL   A C   1 
ATOM   74   O O   . VAL   A 1 53  ? 33.18122 12.35205  40.53233 1.000 70.15179  ?  53   VAL   A O   1 
ATOM   75   C CB  . VAL   A 1 53  ? 31.59178 10.07837  41.49427 1.000 60.81181  ?  53   VAL   A CB  1 
ATOM   76   C CG1 . VAL   A 1 53  ? 31.52515 9.01955   40.40988 1.000 56.47148  ?  53   VAL   A CG1 1 
ATOM   77   C CG2 . VAL   A 1 53  ? 30.80187 9.64834   42.72137 1.000 57.30856  ?  53   VAL   A CG2 1 
ATOM   78   N N   . GLY   A 1 54  ? 34.87741 10.87943  40.34982 1.000 68.89408  ?  54   GLY   A N   1 
ATOM   79   C CA  . GLY   A 1 54  ? 35.66188 11.74111  39.48808 1.000 69.00626  ?  54   GLY   A CA  1 
ATOM   80   C C   . GLY   A 1 54  ? 36.15568 12.96722  40.22500 1.000 71.79108  ?  54   GLY   A C   1 
ATOM   81   O O   . GLY   A 1 54  ? 36.91983 12.85292  41.18680 1.000 72.39034  ?  54   GLY   A O   1 
ATOM   82   N N   . ASP   A 1 55  ? 35.72442 14.14787  39.78702 1.000 74.07913  ?  55   ASP   A N   1 
ATOM   83   C CA  . ASP   A 1 55  ? 36.05930 15.38995  40.46852 1.000 74.21394  ?  55   ASP   A CA  1 
ATOM   84   C C   . ASP   A 1 55  ? 34.90217 15.95289  41.28018 1.000 72.18432  ?  55   ASP   A C   1 
ATOM   85   O O   . ASP   A 1 55  ? 35.10466 16.91217  42.03072 1.000 71.35923  ?  55   ASP   A O   1 
ATOM   86   C CB  . ASP   A 1 55  ? 36.52587 16.44490  39.45701 1.000 79.06052  ?  55   ASP   A CB  1 
ATOM   87   C CG  . ASP   A 1 55  ? 37.27999 15.83969  38.28974 1.000 77.69017  ?  55   ASP   A CG  1 
ATOM   88   O OD1 . ASP   A 1 55  ? 36.82222 16.00311  37.13938 1.000 77.24238  ?  55   ASP   A OD1 1 
ATOM   89   O OD2 . ASP   A 1 55  ? 38.33243 15.20714  38.52096 1.000 79.65368  -1 55   ASP   A OD2 1 
ATOM   90   N N   . SER   A 1 56  ? 33.70737 15.38267  41.15474 1.000 71.68345  ?  56   SER   A N   1 
ATOM   91   C CA  . SER   A 1 56  ? 32.51625 15.89828  41.81322 1.000 68.16685  ?  56   SER   A CA  1 
ATOM   92   C C   . SER   A 1 56  ? 32.25108 15.14107  43.10743 1.000 69.17250  ?  56   SER   A C   1 
ATOM   93   O O   . SER   A 1 56  ? 32.39449 13.91607  43.16535 1.000 67.52007  ?  56   SER   A O   1 
ATOM   94   C CB  . SER   A 1 56  ? 31.29962 15.79335  40.89178 1.000 65.27371  ?  56   SER   A CB  1 
ATOM   95   O OG  . SER   A 1 56  ? 31.64956 16.10291  39.55412 1.000 75.75029  ?  56   SER   A OG  1 
ATOM   96   N N   . THR   A 1 57  ? 31.85996 15.88017  44.14234 1.000 62.29704  ?  57   THR   A N   1 
ATOM   97   C CA  . THR   A 1 57  ? 31.51571 15.29947  45.43362 1.000 56.70114  ?  57   THR   A CA  1 
ATOM   98   C C   . THR   A 1 57  ? 30.03162 14.95464  45.44489 1.000 52.78256  ?  57   THR   A C   1 
ATOM   99   O O   . THR   A 1 57  ? 29.18154 15.84648  45.34882 1.000 52.44557  ?  57   THR   A O   1 
ATOM   100  C CB  . THR   A 1 57  ? 31.85105 16.26513  46.56988 1.000 56.42749  ?  57   THR   A CB  1 
ATOM   101  O OG1 . THR   A 1 57  ? 33.27304 16.32944  46.73874 1.000 59.71933  ?  57   THR   A OG1 1 
ATOM   102  C CG2 . THR   A 1 57  ? 31.21347 15.79890  47.87217 1.000 54.10044  ?  57   THR   A CG2 1 
ATOM   103  N N   . PHE   A 1 58  ? 29.72308 13.66602  45.56059 1.000 50.46275  ?  58   PHE   A N   1 
ATOM   104  C CA  . PHE   A 1 58  ? 28.34469 13.18206  45.56237 1.000 45.35103  ?  58   PHE   A CA  1 
ATOM   105  C C   . PHE   A 1 58  ? 27.92285 12.93613  47.00718 1.000 44.71292  ?  58   PHE   A C   1 
ATOM   106  O O   . PHE   A 1 58  ? 28.31213 11.93831  47.61938 1.000 45.87518  ?  58   PHE   A O   1 
ATOM   107  C CB  . PHE   A 1 58  ? 28.21328 11.91852  44.71899 1.000 43.85321  ?  58   PHE   A CB  1 
ATOM   108  C CG  . PHE   A 1 58  ? 27.64845 12.15990  43.34873 1.000 41.81188  ?  58   PHE   A CG  1 
ATOM   109  C CD1 . PHE   A 1 58  ? 28.42869 12.72267  42.35225 1.000 44.70111  ?  58   PHE   A CD1 1 
ATOM   110  C CD2 . PHE   A 1 58  ? 26.33675 11.82426  43.05680 1.000 38.71384  ?  58   PHE   A CD2 1 
ATOM   111  C CE1 . PHE   A 1 58  ? 27.91146 12.94640  41.09027 1.000 42.09638  ?  58   PHE   A CE1 1 
ATOM   112  C CE2 . PHE   A 1 58  ? 25.81348 12.04549  41.79642 1.000 39.11792  ?  58   PHE   A CE2 1 
ATOM   113  C CZ  . PHE   A 1 58  ? 26.60201 12.60740  40.81234 1.000 39.34317  ?  58   PHE   A CZ  1 
ATOM   114  N N   . THR   A 1 59  ? 27.12725 13.85324  47.55212 1.000 42.91628  ?  59   THR   A N   1 
ATOM   115  C CA  . THR   A 1 59  ? 26.56034 13.71526  48.89222 1.000 40.62477  ?  59   THR   A CA  1 
ATOM   116  C C   . THR   A 1 59  ? 25.10592 13.28901  48.72820 1.000 39.89155  ?  59   THR   A C   1 
ATOM   117  O O   . THR   A 1 59  ? 24.24139 14.10422  48.39682 1.000 38.65905  ?  59   THR   A O   1 
ATOM   118  C CB  . THR   A 1 59  ? 26.67974 15.01688  49.67844 1.000 40.93965  ?  59   THR   A CB  1 
ATOM   119  O OG1 . THR   A 1 59  ? 28.03519 15.48123  49.63426 1.000 41.55573  ?  59   THR   A OG1 1 
ATOM   120  C CG2 . THR   A 1 59  ? 26.27312 14.80014  51.12761 1.000 42.63154  ?  59   THR   A CG2 1 
ATOM   121  N N   . VAL   A 1 60  ? 24.83835 12.00460  48.95368 1.000 40.84577  ?  60   VAL   A N   1 
ATOM   122  C CA  . VAL   A 1 60  ? 23.52236 11.42949  48.72360 1.000 40.43356  ?  60   VAL   A CA  1 
ATOM   123  C C   . VAL   A 1 60  ? 23.02768 10.78067  50.01148 1.000 42.44527  ?  60   VAL   A C   1 
ATOM   124  O O   . VAL   A 1 60  ? 23.77338 10.60112  50.97469 1.000 44.15057  ?  60   VAL   A O   1 
ATOM   125  C CB  . VAL   A 1 60  ? 23.52692 10.40997  47.56723 1.000 39.75247  ?  60   VAL   A CB  1 
ATOM   126  C CG1 . VAL   A 1 60  ? 24.12435 11.02915  46.31429 1.000 38.11915  ?  60   VAL   A CG1 1 
ATOM   127  C CG2 . VAL   A 1 60  ? 24.29129 9.15646   47.96735 1.000 41.50985  ?  60   VAL   A CG2 1 
ATOM   128  N N   . LEU   A 1 61  ? 21.74404 10.42916  50.01033 1.000 42.43365  ?  61   LEU   A N   1 
ATOM   129  C CA  . LEU   A 1 61  ? 21.15040 9.73111   51.13935 1.000 44.56355  ?  61   LEU   A CA  1 
ATOM   130  C C   . LEU   A 1 61  ? 21.78826 8.35507   51.31310 1.000 46.14392  ?  61   LEU   A C   1 
ATOM   131  O O   . LEU   A 1 61  ? 22.37020 7.78512   50.38570 1.000 45.40175  ?  61   LEU   A O   1 
ATOM   132  C CB  . LEU   A 1 61  ? 19.64158 9.58420   50.94359 1.000 44.34289  ?  61   LEU   A CB  1 
ATOM   133  C CG  . LEU   A 1 61  ? 18.81800 10.86902  51.02362 1.000 44.59618  ?  61   LEU   A CG  1 
ATOM   134  C CD1 . LEU   A 1 61  ? 17.62258 10.79731  50.08749 1.000 45.61855  ?  61   LEU   A CD1 1 
ATOM   135  C CD2 . LEU   A 1 61  ? 18.37283 11.13016  52.45416 1.000 45.50778  ?  61   LEU   A CD2 1 
ATOM   136  N N   . LYS   A 1 62  ? 21.66436 7.81724   52.52857 1.000 48.56332  ?  62   LYS   A N   1 
ATOM   137  C CA  . LYS   A 1 62  ? 22.24383 6.51491   52.83292 1.000 50.49520  ?  62   LYS   A CA  1 
ATOM   138  C C   . LYS   A 1 62  ? 21.53550 5.37557   52.11445 1.000 50.48820  ?  62   LYS   A C   1 
ATOM   139  O O   . LYS   A 1 62  ? 22.06612 4.26544   52.07081 1.000 51.78001  ?  62   LYS   A O   1 
ATOM   140  C CB  . LYS   A 1 62  ? 22.21576 6.26038   54.34083 1.000 53.35649  ?  62   LYS   A CB  1 
ATOM   141  C CG  . LYS   A 1 62  ? 23.16249 7.13621   55.14177 1.000 53.95444  ?  62   LYS   A CG  1 
ATOM   142  C CD  . LYS   A 1 62  ? 24.60792 6.69928   54.96924 1.000 54.48826  ?  62   LYS   A CD  1 
ATOM   143  C CE  . LYS   A 1 62  ? 25.48678 7.27127   56.07141 1.000 56.12553  ?  62   LYS   A CE  1 
ATOM   144  N NZ  . LYS   A 1 62  ? 24.69920 7.61594   57.28954 1.000 60.77050  ?  62   LYS   A NZ  1 
ATOM   145  N N   . ARG   A 1 63  ? 20.34713 5.60864   51.56488 1.000 49.26385  ?  63   ARG   A N   1 
ATOM   146  C CA  . ARG   A 1 63  ? 19.67027 4.54586   50.83336 1.000 49.30976  ?  63   ARG   A CA  1 
ATOM   147  C C   . ARG   A 1 63  ? 20.36727 4.21397   49.51917 1.000 47.65111  ?  63   ARG   A C   1 
ATOM   148  O O   . ARG   A 1 63  ? 20.14199 3.13059   48.96957 1.000 48.10430  ?  63   ARG   A O   1 
ATOM   149  C CB  . ARG   A 1 63  ? 18.21701 4.93805   50.57050 1.000 48.57357  ?  63   ARG   A CB  1 
ATOM   150  C CG  . ARG   A 1 63  ? 18.07178 6.11724   49.63155 1.000 45.83169  ?  63   ARG   A CG  1 
ATOM   151  C CD  . ARG   A 1 63  ? 16.63155 6.56826   49.54663 1.000 45.52563  ?  63   ARG   A CD  1 
ATOM   152  N NE  . ARG   A 1 63  ? 15.83005 5.65680   48.74130 1.000 45.49863  ?  63   ARG   A NE  1 
ATOM   153  C CZ  . ARG   A 1 63  ? 14.53327 5.80651   48.51338 1.000 45.86756  ?  63   ARG   A CZ  1 
ATOM   154  N NH1 . ARG   A 1 63  ? 13.85629 6.82417   49.01922 1.000 51.06134  ?  63   ARG   A NH1 1 
ATOM   155  N NH2 . ARG   A 1 63  ? 13.89957 4.91225   47.76044 1.000 46.48229  ?  63   ARG   A NH2 1 
ATOM   156  N N   . TYR   A 1 64  ? 21.21555 5.10773   49.01553 1.000 45.96947  ?  64   TYR   A N   1 
ATOM   157  C CA  . TYR   A 1 64  ? 21.88738 4.92923   47.73451 1.000 44.48529  ?  64   TYR   A CA  1 
ATOM   158  C C   . TYR   A 1 64  ? 23.33471 4.51458   47.97400 1.000 45.63193  ?  64   TYR   A C   1 
ATOM   159  O O   . TYR   A 1 64  ? 24.10750 5.26428   48.58089 1.000 45.90594  ?  64   TYR   A O   1 
ATOM   160  C CB  . TYR   A 1 64  ? 21.81919 6.21441   46.90982 1.000 42.07067  ?  64   TYR   A CB  1 
ATOM   161  C CG  . TYR   A 1 64  ? 20.40829 6.71017   46.68833 1.000 41.08993  ?  64   TYR   A CG  1 
ATOM   162  C CD1 . TYR   A 1 64  ? 19.48595 5.94214   45.99014 1.000 40.89804  ?  64   TYR   A CD1 1 
ATOM   163  C CD2 . TYR   A 1 64  ? 19.99537 7.93979   47.18497 1.000 40.55364  ?  64   TYR   A CD2 1 
ATOM   164  C CE1 . TYR   A 1 64  ? 18.19482 6.38557   45.78739 1.000 40.23668  ?  64   TYR   A CE1 1 
ATOM   165  C CE2 . TYR   A 1 64  ? 18.70442 8.39281   46.98693 1.000 39.88917  ?  64   TYR   A CE2 1 
ATOM   166  C CZ  . TYR   A 1 64  ? 17.80881 7.61098   46.28743 1.000 39.75643  ?  64   TYR   A CZ  1 
ATOM   167  O OH  . TYR   A 1 64  ? 16.52184 8.05399   46.08595 1.000 39.31190  ?  64   TYR   A OH  1 
ATOM   168  N N   . GLN   A 1 65  ? 23.69643 3.32786   47.48991 1.000 46.44666  ?  65   GLN   A N   1 
ATOM   169  C CA  . GLN   A 1 65  ? 25.01837 2.75327   47.68424 1.000 47.91389  ?  65   GLN   A CA  1 
ATOM   170  C C   . GLN   A 1 65  ? 25.65655 2.40250   46.34719 1.000 46.92530  ?  65   GLN   A C   1 
ATOM   171  O O   . GLN   A 1 65  ? 24.98667 2.32477   45.31350 1.000 45.42540  ?  65   GLN   A O   1 
ATOM   172  C CB  . GLN   A 1 65  ? 24.95304 1.50023   48.56437 1.000 50.65424  ?  65   GLN   A CB  1 
ATOM   173  C CG  . GLN   A 1 65  ? 24.06271 1.66159   49.77576 1.000 51.88344  ?  65   GLN   A CG  1 
ATOM   174  C CD  . GLN   A 1 65  ? 24.80375 2.29767   50.93056 1.000 53.10483  ?  65   GLN   A CD  1 
ATOM   175  O OE1 . GLN   A 1 65  ? 24.36262 3.29063   51.49245 1.000 52.57902  ?  65   GLN   A OE1 1 
ATOM   176  N NE2 . GLN   A 1 65  ? 25.93840 1.71932   51.29366 1.000 54.91487  ?  65   GLN   A NE2 1 
ATOM   177  N N   . ASN   A 1 66  ? 26.97294 2.18659   46.39126 1.000 48.00401  ?  66   ASN   A N   1 
ATOM   178  C CA  . ASN   A 1 66  ? 27.75629 1.73274   45.24231 1.000 47.72035  ?  66   ASN   A CA  1 
ATOM   179  C C   . ASN   A 1 66  ? 27.62765 2.70247   44.06571 1.000 45.21992  ?  66   ASN   A C   1 
ATOM   180  O O   . ASN   A 1 66  ? 27.22973 2.33603   42.95828 1.000 44.22065  ?  66   ASN   A O   1 
ATOM   181  C CB  . ASN   A 1 66  ? 27.35176 0.31179   44.83565 1.000 48.72823  ?  66   ASN   A CB  1 
ATOM   182  C CG  . ASN   A 1 66  ? 28.51004 -0.48261  44.26909 1.000 49.97349  ?  66   ASN   A CG  1 
ATOM   183  O OD1 . ASN   A 1 66  ? 29.67372 -0.17262  44.52409 1.000 50.82719  ?  66   ASN   A OD1 1 
ATOM   184  N ND2 . ASN   A 1 66  ? 28.19703 -1.51146  43.48973 1.000 50.24743  ?  66   ASN   A ND2 1 
ATOM   185  N N   . LEU   A 1 67  ? 27.98067 3.95736   44.32774 1.000 44.39825  ?  67   LEU   A N   1 
ATOM   186  C CA  . LEU   A 1 67  ? 27.90868 4.97947   43.29428 1.000 42.29912  ?  67   LEU   A CA  1 
ATOM   187  C C   . LEU   A 1 67  ? 29.01261 4.77468   42.26378 1.000 42.48873  ?  67   LEU   A C   1 
ATOM   188  O O   . LEU   A 1 67  ? 30.16600 4.50311   42.60830 1.000 44.11757  ?  67   LEU   A O   1 
ATOM   189  C CB  . LEU   A 1 67  ? 28.01097 6.37255   43.91317 1.000 41.67068  ?  67   LEU   A CB  1 
ATOM   190  C CG  . LEU   A 1 67  ? 26.68454 7.01721   44.32703 1.000 41.11198  ?  67   LEU   A CG  1 
ATOM   191  C CD1 . LEU   A 1 67  ? 26.12931 6.37070   45.58895 1.000 42.09792  ?  67   LEU   A CD1 1 
ATOM   192  C CD2 . LEU   A 1 67  ? 26.84656 8.51732   44.51607 1.000 39.60729  ?  67   LEU   A CD2 1 
ATOM   193  N N   . LYS   A 1 68  ? 28.64798 4.90175   40.98590 1.000 41.01192  ?  68   LYS   A N   1 
ATOM   194  C CA  . LYS   A 1 68  ? 29.57341 4.71461   39.88113 1.000 41.33760  ?  68   LYS   A CA  1 
ATOM   195  C C   . LYS   A 1 68  ? 29.19661 5.67755   38.76650 1.000 41.87487  ?  68   LYS   A C   1 
ATOM   196  O O   . LYS   A 1 68  ? 28.00093 5.85187   38.49051 1.000 39.61196  ?  68   LYS   A O   1 
ATOM   197  C CB  . LYS   A 1 68  ? 29.55152 3.27519   39.35550 1.000 42.21556  ?  68   LYS   A CB  1 
ATOM   198  C CG  . LYS   A 1 68  ? 30.44730 2.31605   40.12220 1.000 44.62756  ?  68   LYS   A CG  1 
ATOM   199  C CD  . LYS   A 1 68  ? 30.08736 0.86926   39.82527 1.000 45.62095  ?  68   LYS   A CD  1 
ATOM   200  C CE  . LYS   A 1 68  ? 30.45899 -0.04151  40.98433 1.000 47.98040  ?  68   LYS   A CE  1 
ATOM   201  N NZ  . LYS   A 1 68  ? 31.92604 -0.28871  41.04739 1.000 49.90442  ?  68   LYS   A NZ  1 
ATOM   202  N N   . PRO   A 1 69  ? 30.17228 6.30573   38.11212 1.000 41.16448  ?  69   PRO   A N   1 
ATOM   203  C CA  . PRO   A 1 69  ? 29.84316 7.25210   37.04025 1.000 44.94265  ?  69   PRO   A CA  1 
ATOM   204  C C   . PRO   A 1 69  ? 29.38278 6.52257   35.78814 1.000 44.91665  ?  69   PRO   A C   1 
ATOM   205  O O   . PRO   A 1 69  ? 29.87377 5.43927   35.46207 1.000 45.03427  ?  69   PRO   A O   1 
ATOM   206  C CB  . PRO   A 1 69  ? 31.16277 7.99390   36.80670 1.000 43.59562  ?  69   PRO   A CB  1 
ATOM   207  C CG  . PRO   A 1 69  ? 32.21239 7.00364   37.19162 1.000 48.25533  ?  69   PRO   A CG  1 
ATOM   208  C CD  . PRO   A 1 69  ? 31.62665 6.13791   38.28275 1.000 41.96726  ?  69   PRO   A CD  1 
ATOM   209  N N   . ILE   A 1 70  ? 28.42686 7.12831   35.08462 1.000 44.41815  ?  70   ILE   A N   1 
ATOM   210  C CA  . ILE   A 1 70  ? 27.83431 6.50177   33.90777 1.000 50.20062  ?  70   ILE   A CA  1 
ATOM   211  C C   . ILE   A 1 70  ? 27.71541 7.50787   32.77090 1.000 59.91738  ?  70   ILE   A C   1 
ATOM   212  O O   . ILE   A 1 70  ? 27.76452 7.13613   31.59294 1.000 65.86712  ?  70   ILE   A O   1 
ATOM   213  C CB  . ILE   A 1 70  ? 26.46107 5.89018   34.23878 1.000 46.25203  ?  70   ILE   A CB  1 
ATOM   214  C CG1 . ILE   A 1 70  ? 25.60266 6.89344   35.01192 1.000 42.54071  ?  70   ILE   A CG1 1 
ATOM   215  C CG2 . ILE   A 1 70  ? 26.62894 4.59721   35.02196 1.000 44.43938  ?  70   ILE   A CG2 1 
ATOM   216  C CD1 . ILE   A 1 70  ? 24.22418 6.37893   35.35495 1.000 45.10738  ?  70   ILE   A CD1 1 
ATOM   217  N N   . GLY   A 1 71  ? 27.55257 8.78396   33.10984 1.000 62.82406  ?  71   GLY   A N   1 
ATOM   218  C CA  . GLY   A 1 71  ? 27.38950 9.79931   32.08605 1.000 69.19789  ?  71   GLY   A CA  1 
ATOM   219  C C   . GLY   A 1 71  ? 27.71100 11.17562  32.62013 1.000 81.51073  ?  71   GLY   A C   1 
ATOM   220  O O   . GLY   A 1 71  ? 27.92441 11.37354  33.81859 1.000 65.07239  ?  71   GLY   A O   1 
ATOM   221  N N   . SER   A 1 72  ? 27.74151 12.13504  31.69775 1.000 84.80628  ?  72   SER   A N   1 
ATOM   222  C CA  . SER   A 1 72  ? 28.03637 13.52328  32.04280 1.000 91.98688  ?  72   SER   A CA  1 
ATOM   223  C C   . SER   A 1 72  ? 27.50722 14.41635  30.93425 1.000 95.87877  ?  72   SER   A C   1 
ATOM   224  O O   . SER   A 1 72  ? 27.98200 14.33607  29.79676 1.000 95.22247  ?  72   SER   A O   1 
ATOM   225  C CB  . SER   A 1 72  ? 29.53846 13.73346  32.23666 1.000 93.37256  ?  72   SER   A CB  1 
ATOM   226  O OG  . SER   A 1 72  ? 29.91000 15.06658  31.93129 1.000 94.20418  ?  72   SER   A OG  1 
ATOM   227  N N   . GLY   A 1 73  ? 26.52961 15.25723  31.25898 1.000 94.91917  ?  73   GLY   A N   1 
ATOM   228  C CA  . GLY   A 1 73  ? 26.00347 16.20466  30.29787 1.000 97.95558  ?  73   GLY   A CA  1 
ATOM   229  C C   . GLY   A 1 73  ? 26.60658 17.58272  30.46783 1.000 100.25440 ?  73   GLY   A C   1 
ATOM   230  O O   . GLY   A 1 73  ? 27.82913 17.72520  30.56517 1.000 100.67398 ?  73   GLY   A O   1 
ATOM   231  N N   . ALA   A 1 74  ? 25.75654 18.60925  30.50522 1.000 101.99234 ?  74   ALA   A N   1 
ATOM   232  C CA  . ALA   A 1 74  ? 26.19982 19.97399  30.74087 1.000 106.45661 ?  74   ALA   A CA  1 
ATOM   233  C C   . ALA   A 1 74  ? 25.60238 20.60555  31.98729 1.000 108.05954 ?  74   ALA   A C   1 
ATOM   234  O O   . ALA   A 1 74  ? 26.12697 21.62464  32.44982 1.000 107.92541 ?  74   ALA   A O   1 
ATOM   235  C CB  . ALA   A 1 74  ? 25.87205 20.86515  29.53187 1.000 108.48848 ?  74   ALA   A CB  1 
ATOM   236  N N   . GLN   A 1 75  ? 24.53353 20.03620  32.54349 1.000 116.05773 ?  75   GLN   A N   1 
ATOM   237  C CA  . GLN   A 1 75  ? 23.88812 20.57937  33.72913 1.000 108.44415 ?  75   GLN   A CA  1 
ATOM   238  C C   . GLN   A 1 75  ? 24.26373 19.84410  35.00775 1.000 106.45154 ?  75   GLN   A C   1 
ATOM   239  O O   . GLN   A 1 75  ? 23.89528 20.30076  36.09501 1.000 104.17569 ?  75   GLN   A O   1 
ATOM   240  C CB  . GLN   A 1 75  ? 22.36399 20.55331  33.55957 1.000 107.30772 ?  75   GLN   A CB  1 
ATOM   241  C CG  . GLN   A 1 75  ? 21.87175 21.25537  32.30580 1.000 109.72256 ?  75   GLN   A CG  1 
ATOM   242  C CD  . GLN   A 1 75  ? 22.21906 22.73071  32.29183 1.000 110.14567 ?  75   GLN   A CD  1 
ATOM   243  O OE1 . GLN   A 1 75  ? 21.61817 23.52809  33.01174 1.000 106.15370 ?  75   GLN   A OE1 1 
ATOM   244  N NE2 . GLN   A 1 75  ? 23.19521 23.10162  31.47101 1.000 106.57731 ?  75   GLN   A NE2 1 
ATOM   245  N N   . GLY   A 1 76  ? 24.97753 18.73097  34.91137 1.000 88.99868  ?  76   GLY   A N   1 
ATOM   246  C CA  . GLY   A 1 76  ? 25.36285 18.00066  36.10041 1.000 78.12398  ?  76   GLY   A CA  1 
ATOM   247  C C   . GLY   A 1 76  ? 26.04574 16.69815  35.74602 1.000 78.58476  ?  76   GLY   A C   1 
ATOM   248  O O   . GLY   A 1 76  ? 26.21374 16.34690  34.57331 1.000 79.49662  ?  76   GLY   A O   1 
ATOM   249  N N   . ILE   A 1 77  ? 26.43596 15.98325  36.79793 1.000 56.84193  ?  77   ILE   A N   1 
ATOM   250  C CA  . ILE   A 1 77  ? 27.13311 14.70819  36.68836 1.000 54.43443  ?  77   ILE   A CA  1 
ATOM   251  C C   . ILE   A 1 77  ? 26.17107 13.61152  37.11991 1.000 47.59305  ?  77   ILE   A C   1 
ATOM   252  O O   . ILE   A 1 77  ? 25.44220 13.76623  38.10608 1.000 44.88895  ?  77   ILE   A O   1 
ATOM   253  C CB  . ILE   A 1 77  ? 28.43175 14.66855  37.52618 1.000 54.60817  ?  77   ILE   A CB  1 
ATOM   254  C CG1 . ILE   A 1 77  ? 29.39013 15.81984  37.17667 1.000 57.48332  ?  77   ILE   A CG1 1 
ATOM   255  C CG2 . ILE   A 1 77  ? 29.14351 13.33386  37.35360 1.000 52.87251  ?  77   ILE   A CG2 1 
ATOM   256  C CD1 . ILE   A 1 77  ? 29.03733 17.18547  37.75733 1.000 57.42064  ?  77   ILE   A CD1 1 
ATOM   257  N N   . VAL   A 1 78  ? 26.16078 12.50921  36.37484 1.000 52.61823  ?  78   VAL   A N   1 
ATOM   258  C CA  . VAL   A 1 78  ? 25.21392 11.41979  36.58340 1.000 47.19057  ?  78   VAL   A CA  1 
ATOM   259  C C   . VAL   A 1 78  ? 25.96323 10.19493  37.08776 1.000 45.34934  ?  78   VAL   A C   1 
ATOM   260  O O   . VAL   A 1 78  ? 27.06485 9.88792   36.61665 1.000 46.38766  ?  78   VAL   A O   1 
ATOM   261  C CB  . VAL   A 1 78  ? 24.43908 11.09864  35.29086 1.000 46.40760  ?  78   VAL   A CB  1 
ATOM   262  C CG1 . VAL   A 1 78  ? 23.32636 10.10244  35.56796 1.000 39.94852  ?  78   VAL   A CG1 1 
ATOM   263  C CG2 . VAL   A 1 78  ? 23.87974 12.37816  34.68988 1.000 47.58057  ?  78   VAL   A CG2 1 
ATOM   264  N N   . CYS   A 1 79  ? 25.36125 9.49605   38.04822 1.000 38.53128  ?  79   CYS   A N   1 
ATOM   265  C CA  . CYS   A 1 79  ? 25.94103 8.29748   38.63131 1.000 38.96151  ?  79   CYS   A CA  1 
ATOM   266  C C   . CYS   A 1 79  ? 24.88641 7.20625   38.72559 1.000 38.88783  ?  79   CYS   A C   1 
ATOM   267  O O   . CYS   A 1 79  ? 23.69706 7.48265   38.90088 1.000 36.89313  ?  79   CYS   A O   1 
ATOM   268  C CB  . CYS   A 1 79  ? 26.51464 8.56811   40.02947 1.000 35.67051  ?  79   CYS   A CB  1 
ATOM   269  S SG  . CYS   A 1 79  ? 28.05546 9.50214   40.04426 1.000 46.36726  ?  79   CYS   A SG  1 
ATOM   270  N N   . ALA   A 1 80  ? 25.33562 5.96192   38.60363 1.000 36.61787  ?  80   ALA   A N   1 
ATOM   271  C CA  . ALA   A 1 80  ? 24.50271 4.81134   38.91167 1.000 39.17249  ?  80   ALA   A CA  1 
ATOM   272  C C   . ALA   A 1 80  ? 24.74020 4.38715   40.35371 1.000 38.18853  ?  80   ALA   A C   1 
ATOM   273  O O   . ALA   A 1 80  ? 25.83354 4.56064   40.89758 1.000 39.12214  ?  80   ALA   A O   1 
ATOM   274  C CB  . ALA   A 1 80  ? 24.79946 3.64551   37.96868 1.000 37.19112  ?  80   ALA   A CB  1 
ATOM   275  N N   . ALA   A 1 81  ? 23.70342 3.83167   40.97342 1.000 41.48638  ?  81   ALA   A N   1 
ATOM   276  C CA  . ALA   A 1 81  ? 23.80106 3.40489   42.36218 1.000 42.58539  ?  81   ALA   A CA  1 
ATOM   277  C C   . ALA   A 1 81  ? 22.70990 2.38382   42.64455 1.000 41.44966  ?  81   ALA   A C   1 
ATOM   278  O O   . ALA   A 1 81  ? 21.78332 2.19552   41.85269 1.000 40.56489  ?  81   ALA   A O   1 
ATOM   279  C CB  . ALA   A 1 81  ? 23.69821 4.59441   43.32216 1.000 40.17773  ?  81   ALA   A CB  1 
ATOM   280  N N   . TYR   A 1 82  ? 22.83552 1.72545   43.79265 1.000 43.49210  ?  82   TYR   A N   1 
ATOM   281  C CA  . TYR   A 1 82  ? 21.85151 0.75930   44.25985 1.000 44.92956  ?  82   TYR   A CA  1 
ATOM   282  C C   . TYR   A 1 82  ? 21.00895 1.40239   45.35364 1.000 45.30545  ?  82   TYR   A C   1 
ATOM   283  O O   . TYR   A 1 82  ? 21.54349 1.83060   46.38363 1.000 46.20004  ?  82   TYR   A O   1 
ATOM   284  C CB  . TYR   A 1 82  ? 22.53025 -0.50745  44.78030 1.000 47.38706  ?  82   TYR   A CB  1 
ATOM   285  C CG  . TYR   A 1 82  ? 21.58701 -1.45406  45.48731 1.000 49.37466  ?  82   TYR   A CG  1 
ATOM   286  C CD1 . TYR   A 1 82  ? 20.51215 -2.02237  44.81676 1.000 49.13845  ?  82   TYR   A CD1 1 
ATOM   287  C CD2 . TYR   A 1 82  ? 21.76896 -1.77692  46.82622 1.000 51.71309  ?  82   TYR   A CD2 1 
ATOM   288  C CE1 . TYR   A 1 82  ? 19.64603 -2.88774  45.45797 1.000 51.21801  ?  82   TYR   A CE1 1 
ATOM   289  C CE2 . TYR   A 1 82  ? 20.90756 -2.64195  47.47638 1.000 53.83466  ?  82   TYR   A CE2 1 
ATOM   290  C CZ  . TYR   A 1 82  ? 19.84834 -3.19401  46.78692 1.000 53.59591  ?  82   TYR   A CZ  1 
ATOM   291  O OH  . TYR   A 1 82  ? 18.98735 -4.05469  47.42703 1.000 55.95231  ?  82   TYR   A OH  1 
ATOM   292  N N   . ASP   A 1 83  ? 19.69951 1.47694   45.12434 1.000 44.78674  ?  83   ASP   A N   1 
ATOM   293  C CA  . ASP   A 1 83  ? 18.77266 2.00026   46.12128 1.000 45.44410  ?  83   ASP   A CA  1 
ATOM   294  C C   . ASP   A 1 83  ? 18.39866 0.87070   47.07201 1.000 48.23472  ?  83   ASP   A C   1 
ATOM   295  O O   . ASP   A 1 83  ? 17.65353 -0.04069  46.69972 1.000 49.01174  ?  83   ASP   A O   1 
ATOM   296  C CB  . ASP   A 1 83  ? 17.54020 2.59007   45.44217 1.000 43.93605  ?  83   ASP   A CB  1 
ATOM   297  C CG  . ASP   A 1 83  ? 16.59086 3.25787   46.42323 1.000 44.63871  ?  83   ASP   A CG  1 
ATOM   298  O OD1 . ASP   A 1 83  ? 16.93090 3.35846   47.62178 1.000 46.14409  ?  83   ASP   A OD1 1 
ATOM   299  O OD2 . ASP   A 1 83  ? 15.50002 3.68523   45.99085 1.000 43.84340  -1 83   ASP   A OD2 1 
ATOM   300  N N   . ALA   A 1 84  ? 18.91669 0.92784   48.30130 1.000 49.93540  ?  84   ALA   A N   1 
ATOM   301  C CA  . ALA   A 1 84  ? 18.66549 -0.13715  49.26387 1.000 52.93217  ?  84   ALA   A CA  1 
ATOM   302  C C   . ALA   A 1 84  ? 17.23215 -0.13002  49.77824 1.000 54.01572  ?  84   ALA   A C   1 
ATOM   303  O O   . ALA   A 1 84  ? 16.79473 -1.12234  50.36979 1.000 56.60012  ?  84   ALA   A O   1 
ATOM   304  C CB  . ALA   A 1 84  ? 19.64088 -0.02885  50.43683 1.000 54.62247  ?  84   ALA   A CB  1 
ATOM   305  N N   . VAL   A 1 85  ? 16.49497 0.96078   49.57467 1.000 52.34405  ?  85   VAL   A N   1 
ATOM   306  C CA  . VAL   A 1 85  ? 15.10101 1.00654   50.00149 1.000 53.48890  ?  85   VAL   A CA  1 
ATOM   307  C C   . VAL   A 1 85  ? 14.20230 0.34444   48.96585 1.000 53.07600  ?  85   VAL   A C   1 
ATOM   308  O O   . VAL   A 1 85  ? 13.40728 -0.54541  49.28815 1.000 55.30118  ?  85   VAL   A O   1 
ATOM   309  C CB  . VAL   A 1 85  ? 14.67445 2.46124   50.27384 1.000 52.18603  ?  85   VAL   A CB  1 
ATOM   310  C CG1 . VAL   A 1 85  ? 13.15753 2.57868   50.27600 1.000 52.81790  ?  85   VAL   A CG1 1 
ATOM   311  C CG2 . VAL   A 1 85  ? 15.25407 2.94477   51.59286 1.000 53.58446  ?  85   VAL   A CG2 1 
ATOM   312  N N   . LEU   A 1 86  ? 14.31797 0.76385   47.70614 1.000 50.42298  ?  86   LEU   A N   1 
ATOM   313  C CA  . LEU   A 1 86  ? 13.47994 0.22851   46.64221 1.000 49.91295  ?  86   LEU   A CA  1 
ATOM   314  C C   . LEU   A 1 86  ? 14.00550 -1.08170  46.07038 1.000 51.68731  ?  86   LEU   A C   1 
ATOM   315  O O   . LEU   A 1 86  ? 13.30804 -1.70409  45.26132 1.000 50.67288  ?  86   LEU   A O   1 
ATOM   316  C CB  . LEU   A 1 86  ? 13.34137 1.26112   45.52048 1.000 46.97674  ?  86   LEU   A CB  1 
ATOM   317  C CG  . LEU   A 1 86  ? 12.43615 2.46869   45.77816 1.000 47.93167  ?  86   LEU   A CG  1 
ATOM   318  C CD1 . LEU   A 1 86  ? 11.84799 2.98232   44.47300 1.000 48.92033  ?  86   LEU   A CD1 1 
ATOM   319  C CD2 . LEU   A 1 86  ? 11.33093 2.12622   46.76701 1.000 48.94572  ?  86   LEU   A CD2 1 
ATOM   320  N N   . ASP   A 1 87  ? 15.20135 -1.50990  46.47257 1.000 51.37665  ?  87   ASP   A N   1 
ATOM   321  C CA  . ASP   A 1 87  ? 15.82629 -2.74006  45.98752 1.000 52.27971  ?  87   ASP   A CA  1 
ATOM   322  C C   . ASP   A 1 87  ? 15.90290 -2.74855  44.46037 1.000 50.08456  ?  87   ASP   A C   1 
ATOM   323  O O   . ASP   A 1 87  ? 15.42216 -3.65919  43.78315 1.000 50.67098  ?  87   ASP   A O   1 
ATOM   324  C CB  . ASP   A 1 87  ? 15.09013 -3.97556  46.51280 1.000 55.26063  ?  87   ASP   A CB  1 
ATOM   325  C CG  . ASP   A 1 87  ? 15.87149 -5.25574  46.29048 1.000 56.75016  ?  87   ASP   A CG  1 
ATOM   326  O OD1 . ASP   A 1 87  ? 17.10486 -5.24132  46.48738 1.000 56.70995  ?  87   ASP   A OD1 1 
ATOM   327  O OD2 . ASP   A 1 87  ? 15.25341 -6.27429  45.91558 1.000 58.11005  -1 87   ASP   A OD2 1 
ATOM   328  N N   . ARG   A 1 88  ? 16.52103 -1.69882  43.92646 1.000 47.69589  ?  88   ARG   A N   1 
ATOM   329  C CA  . ARG   A 1 88  ? 16.70416 -1.56335  42.48930 1.000 45.66535  ?  88   ARG   A CA  1 
ATOM   330  C C   . ARG   A 1 88  ? 17.82728 -0.57060  42.23748 1.000 43.90797  ?  88   ARG   A C   1 
ATOM   331  O O   . ARG   A 1 88  ? 18.22386 0.18614   43.12776 1.000 43.94801  ?  88   ARG   A O   1 
ATOM   332  C CB  . ARG   A 1 88  ? 15.41598 -1.10951  41.79403 1.000 46.17178  ?  88   ARG   A CB  1 
ATOM   333  C CG  . ARG   A 1 88  ? 14.70604 0.02727   42.50341 1.000 48.57695  ?  88   ARG   A CG  1 
ATOM   334  C CD  . ARG   A 1 88  ? 13.36103 0.33782   41.86726 1.000 52.92919  ?  88   ARG   A CD  1 
ATOM   335  N NE  . ARG   A 1 88  ? 13.38660 0.17803   40.41870 1.000 57.20265  ?  88   ARG   A NE  1 
ATOM   336  C CZ  . ARG   A 1 88  ? 12.55047 0.78144   39.58487 1.000 61.03167  ?  88   ARG   A CZ  1 
ATOM   337  N NH1 . ARG   A 1 88  ? 11.60714 1.59930   40.02314 1.000 56.17997  ?  88   ARG   A NH1 1 
ATOM   338  N NH2 . ARG   A 1 88  ? 12.66440 0.56001   38.27834 1.000 64.77122  ?  88   ARG   A NH2 1 
ATOM   339  N N   . ASN   A 1 89  ? 18.33540 -0.58699  41.00952 1.000 42.55875  ?  89   ASN   A N   1 
ATOM   340  C CA  . ASN   A 1 89  ? 19.40101 0.31593   40.60398 1.000 41.06675  ?  89   ASN   A CA  1 
ATOM   341  C C   . ASN   A 1 89  ? 18.80959 1.61262   40.06749 1.000 38.97937  ?  89   ASN   A C   1 
ATOM   342  O O   . ASN   A 1 89  ? 17.82110 1.60113   39.32818 1.000 38.28340  ?  89   ASN   A O   1 
ATOM   343  C CB  . ASN   A 1 89  ? 20.28893 -0.34147  39.54712 1.000 40.98907  ?  89   ASN   A CB  1 
ATOM   344  C CG  . ASN   A 1 89  ? 21.01209 -1.56536  40.07635 1.000 43.19843  ?  89   ASN   A CG  1 
ATOM   345  O OD1 . ASN   A 1 89  ? 21.31525 -1.65410  41.26619 1.000 45.46939  ?  89   ASN   A OD1 1 
ATOM   346  N ND2 . ASN   A 1 89  ? 21.29004 -2.51731  39.19434 1.000 43.70467  ?  89   ASN   A ND2 1 
ATOM   347  N N   . VAL   A 1 90  ? 19.41998 2.73433   40.45099 1.000 38.15751  ?  90   VAL   A N   1 
ATOM   348  C CA  . VAL   A 1 90  ? 18.92222 4.05593   40.09928 1.000 36.43322  ?  90   VAL   A CA  1 
ATOM   349  C C   . VAL   A 1 90  ? 20.04950 4.87129   39.48162 1.000 35.28131  ?  90   VAL   A C   1 
ATOM   350  O O   . VAL   A 1 90  ? 21.22883 4.52628   39.58082 1.000 36.77879  ?  90   VAL   A O   1 
ATOM   351  C CB  . VAL   A 1 90  ? 18.33383 4.80002   41.31853 1.000 36.81374  ?  90   VAL   A CB  1 
ATOM   352  C CG1 . VAL   A 1 90  ? 17.14275 4.04269   41.88557 1.000 38.19073  ?  90   VAL   A CG1 1 
ATOM   353  C CG2 . VAL   A 1 90  ? 19.40167 4.99995   42.38173 1.000 37.72795  ?  90   VAL   A CG2 1 
ATOM   354  N N   . ALA   A 1 91  ? 19.66430 5.97020   38.83700 1.000 33.74161  ?  91   ALA   A N   1 
ATOM   355  C CA  . ALA   A 1 91  ? 20.59783 6.93471   38.27216 1.000 34.49833  ?  91   ALA   A CA  1 
ATOM   356  C C   . ALA   A 1 91  ? 20.41572 8.26536   38.98612 1.000 32.22838  ?  91   ALA   A C   1 
ATOM   357  O O   . ALA   A 1 91  ? 19.29599 8.78082   39.06652 1.000 36.60445  ?  91   ALA   A O   1 
ATOM   358  C CB  . ALA   A 1 91  ? 20.38235 7.10286   36.76546 1.000 36.75489  ?  91   ALA   A CB  1 
ATOM   359  N N   . ILE   A 1 92  ? 21.51090 8.81836   39.50050 1.000 32.51419  ?  92   ILE   A N   1 
ATOM   360  C CA  . ILE   A 1 92  ? 21.47823 10.03266  40.30925 1.000 33.03594  ?  92   ILE   A CA  1 
ATOM   361  C C   . ILE   A 1 92  ? 22.24951 11.12263  39.57985 1.000 34.64981  ?  92   ILE   A C   1 
ATOM   362  O O   . ILE   A 1 92  ? 23.43540 10.95153  39.26982 1.000 36.33700  ?  92   ILE   A O   1 
ATOM   363  C CB  . ILE   A 1 92  ? 22.05683 9.80036   41.71386 1.000 33.73855  ?  92   ILE   A CB  1 
ATOM   364  C CG1 . ILE   A 1 92  ? 21.13447 8.88804   42.52207 1.000 34.82163  ?  92   ILE   A CG1 1 
ATOM   365  C CG2 . ILE   A 1 92  ? 22.25663 11.12379  42.43572 1.000 33.57978  ?  92   ILE   A CG2 1 
ATOM   366  C CD1 . ILE   A 1 92  ? 21.84484 7.72335   43.16684 1.000 36.52315  ?  92   ILE   A CD1 1 
ATOM   367  N N   . LYS   A 1 93  ? 21.57933 12.24075  39.31487 1.000 33.80776  ?  93   LYS   A N   1 
ATOM   368  C CA  . LYS   A 1 93  ? 22.18565 13.40681  38.68781 1.000 35.99252  ?  93   LYS   A CA  1 
ATOM   369  C C   . LYS   A 1 93  ? 22.30537 14.52013  39.71906 1.000 34.13707  ?  93   LYS   A C   1 
ATOM   370  O O   . LYS   A 1 93  ? 21.34928 14.79817  40.45036 1.000 30.65046  ?  93   LYS   A O   1 
ATOM   371  C CB  . LYS   A 1 93  ? 21.35782 13.87682  37.48977 1.000 39.95531  ?  93   LYS   A CB  1 
ATOM   372  C CG  . LYS   A 1 93  ? 21.90819 15.11317  36.79773 1.000 40.93362  ?  93   LYS   A CG  1 
ATOM   373  C CD  . LYS   A 1 93  ? 21.16640 15.39393  35.50156 1.000 43.29555  ?  93   LYS   A CD  1 
ATOM   374  C CE  . LYS   A 1 93  ? 21.98052 16.28838  34.58031 1.000 56.46236  ?  93   LYS   A CE  1 
ATOM   375  N NZ  . LYS   A 1 93  ? 21.13739 16.89653  33.51511 1.000 57.35984  ?  93   LYS   A NZ  1 
ATOM   376  N N   . LYS   A 1 94  ? 23.47375 15.15320  39.77463 1.000 32.86989  ?  94   LYS   A N   1 
ATOM   377  C CA  . LYS   A 1 94  ? 23.76322 16.19649  40.75080 1.000 36.43488  ?  94   LYS   A CA  1 
ATOM   378  C C   . LYS   A 1 94  ? 23.85268 17.54173  40.04243 1.000 38.73520  ?  94   LYS   A C   1 
ATOM   379  O O   . LYS   A 1 94  ? 24.73280 17.74510  39.19975 1.000 42.37515  ?  94   LYS   A O   1 
ATOM   380  C CB  . LYS   A 1 94  ? 25.06324 15.89795  41.49778 1.000 36.38902  ?  94   LYS   A CB  1 
ATOM   381  C CG  . LYS   A 1 94  ? 25.52099 17.01870  42.41693 1.000 33.87441  ?  94   LYS   A CG  1 
ATOM   382  C CD  . LYS   A 1 94  ? 27.03417 17.04027  42.55271 1.000 35.06510  ?  94   LYS   A CD  1 
ATOM   383  C CE  . LYS   A 1 94  ? 27.48041 18.07328  43.57456 1.000 40.50285  ?  94   LYS   A CE  1 
ATOM   384  N NZ  . LYS   A 1 94  ? 28.94549 18.32806  43.50357 1.000 44.53572  ?  94   LYS   A NZ  1 
ATOM   385  N N   . LEU   A 1 95  ? 22.94884 18.45608  40.39037 1.000 36.68054  ?  95   LEU   A N   1 
ATOM   386  C CA  . LEU   A 1 95  ? 22.95205 19.81617  39.86100 1.000 38.34882  ?  95   LEU   A CA  1 
ATOM   387  C C   . LEU   A 1 95  ? 23.67345 20.71766  40.85784 1.000 37.83238  ?  95   LEU   A C   1 
ATOM   388  O O   . LEU   A 1 95  ? 23.13883 21.02161  41.92915 1.000 34.23454  ?  95   LEU   A O   1 
ATOM   389  C CB  . LEU   A 1 95  ? 21.52872 20.30814  39.60717 1.000 37.63803  ?  95   LEU   A CB  1 
ATOM   390  C CG  . LEU   A 1 95  ? 20.58397 19.37595  38.84658 1.000 36.51308  ?  95   LEU   A CG  1 
ATOM   391  C CD1 . LEU   A 1 95  ? 19.20108 19.99881  38.73584 1.000 33.10278  ?  95   LEU   A CD1 1 
ATOM   392  C CD2 . LEU   A 1 95  ? 21.13862 19.04967  37.47005 1.000 46.62902  ?  95   LEU   A CD2 1 
ATOM   393  N N   . SER   A 1 96  ? 24.88312 21.14693  40.50279 1.000 35.11152  ?  96   SER   A N   1 
ATOM   394  C CA  . SER   A 1 96  ? 25.70874 21.96004  41.39121 1.000 33.46860  ?  96   SER   A CA  1 
ATOM   395  C C   . SER   A 1 96  ? 25.28202 23.41945  41.28620 1.000 37.35415  ?  96   SER   A C   1 
ATOM   396  O O   . SER   A 1 96  ? 25.56214 24.08371  40.28206 1.000 35.23500  ?  96   SER   A O   1 
ATOM   397  C CB  . SER   A 1 96  ? 27.18573 21.79932  41.04317 1.000 34.46671  ?  96   SER   A CB  1 
ATOM   398  O OG  . SER   A 1 96  ? 27.52839 20.43439  40.87832 1.000 38.62955  ?  96   SER   A OG  1 
ATOM   399  N N   . ARG   A 1 97  ? 24.61100 23.91726  42.33067 1.000 36.56526  ?  97   ARG   A N   1 
ATOM   400  C CA  . ARG   A 1 97  ? 24.17232 25.30396  42.46279 1.000 36.64319  ?  97   ARG   A CA  1 
ATOM   401  C C   . ARG   A 1 97  ? 23.50483 25.79429  41.18384 1.000 36.84532  ?  97   ARG   A C   1 
ATOM   402  O O   . ARG   A 1 97  ? 24.05948 26.64738  40.47915 1.000 37.94159  ?  97   ARG   A O   1 
ATOM   403  C CB  . ARG   A 1 97  ? 25.35604 26.19795  42.83699 1.000 37.93328  ?  97   ARG   A CB  1 
ATOM   404  C CG  . ARG   A 1 97  ? 25.78522 26.03842  44.28816 1.000 42.13198  ?  97   ARG   A CG  1 
ATOM   405  C CD  . ARG   A 1 97  ? 27.04098 26.82821  44.60904 1.000 43.18075  ?  97   ARG   A CD  1 
ATOM   406  N NE  . ARG   A 1 97  ? 26.96129 28.20974  44.15472 1.000 58.41577  ?  97   ARG   A NE  1 
ATOM   407  C CZ  . ARG   A 1 97  ? 26.48135 29.21035  44.88008 1.000 64.85371  ?  97   ARG   A CZ  1 
ATOM   408  N NH1 . ARG   A 1 97  ? 25.99438 29.01326  46.09396 1.000 54.42406  ?  97   ARG   A NH1 1 
ATOM   409  N NH2 . ARG   A 1 97  ? 26.49013 30.43970  44.37438 1.000 56.53727  ?  97   ARG   A NH2 1 
ATOM   410  N N   . PRO   A 1 98  ? 22.31323 25.28571  40.85521 1.000 38.64001  ?  98   PRO   A N   1 
ATOM   411  C CA  . PRO   A 1 98  ? 21.68041 25.65256  39.57910 1.000 38.67594  ?  98   PRO   A CA  1 
ATOM   412  C C   . PRO   A 1 98  ? 21.22000 27.09781  39.51405 1.000 40.78697  ?  98   PRO   A C   1 
ATOM   413  O O   . PRO   A 1 98  ? 20.92247 27.58313  38.41579 1.000 40.20869  ?  98   PRO   A O   1 
ATOM   414  C CB  . PRO   A 1 98  ? 20.49145 24.68998  39.49273 1.000 38.30600  ?  98   PRO   A CB  1 
ATOM   415  C CG  . PRO   A 1 98  ? 20.15392 24.39343  40.91618 1.000 36.02351  ?  98   PRO   A CG  1 
ATOM   416  C CD  . PRO   A 1 98  ? 21.45855 24.40110  41.66742 1.000 36.53689  ?  98   PRO   A CD  1 
ATOM   417  N N   . PHE   A 1 99  ? 21.15168 27.79686  40.64151 1.000 42.90705  ?  99   PHE   A N   1 
ATOM   418  C CA  . PHE   A 1 99  ? 20.73475 29.19155  40.67548 1.000 39.65983  ?  99   PHE   A CA  1 
ATOM   419  C C   . PHE   A 1 99  ? 21.87089 30.15731  40.36494 1.000 39.53924  ?  99   PHE   A C   1 
ATOM   420  O O   . PHE   A 1 99  ? 21.67865 31.37230  40.48489 1.000 44.10807  ?  99   PHE   A O   1 
ATOM   421  C CB  . PHE   A 1 99  ? 20.14171 29.51846  42.04768 1.000 41.60879  ?  99   PHE   A CB  1 
ATOM   422  C CG  . PHE   A 1 99  ? 20.93511 28.95838  43.19359 1.000 41.55117  ?  99   PHE   A CG  1 
ATOM   423  C CD1 . PHE   A 1 99  ? 22.01848 29.65225  43.70618 1.000 41.98084  ?  99   PHE   A CD1 1 
ATOM   424  C CD2 . PHE   A 1 99  ? 20.60437 27.73355  43.75205 1.000 41.61297  ?  99   PHE   A CD2 1 
ATOM   425  C CE1 . PHE   A 1 99  ? 22.75449 29.13867  44.75778 1.000 46.31739  ?  99   PHE   A CE1 1 
ATOM   426  C CE2 . PHE   A 1 99  ? 21.33679 27.21431  44.80300 1.000 41.20911  ?  99   PHE   A CE2 1 
ATOM   427  C CZ  . PHE   A 1 99  ? 22.41306 27.91812  45.30660 1.000 43.75446  ?  99   PHE   A CZ  1 
ATOM   428  N N   . GLN   A 1 100 ? 23.04101 29.65008  39.96652 1.000 37.42121  ?  100  GLN   A N   1 
ATOM   429  C CA  . GLN   A 1 100 ? 24.21094 30.51113  39.82518 1.000 42.57424  ?  100  GLN   A CA  1 
ATOM   430  C C   . GLN   A 1 100 ? 24.06973 31.48725  38.66295 1.000 43.12300  ?  100  GLN   A C   1 
ATOM   431  O O   . GLN   A 1 100 ? 24.68470 32.55919  38.68313 1.000 44.45631  ?  100  GLN   A O   1 
ATOM   432  C CB  . GLN   A 1 100 ? 25.47258 29.66158  39.66566 1.000 41.68337  ?  100  GLN   A CB  1 
ATOM   433  C CG  . GLN   A 1 100 ? 25.49219 28.77589  38.43300 1.000 42.84739  ?  100  GLN   A CG  1 
ATOM   434  C CD  . GLN   A 1 100 ? 26.67021 27.82077  38.42985 1.000 42.40542  ?  100  GLN   A CD  1 
ATOM   435  O OE1 . GLN   A 1 100 ? 27.79275 28.20270  38.09967 1.000 42.90410  ?  100  GLN   A OE1 1 
ATOM   436  N NE2 . GLN   A 1 100 ? 26.42018 26.57096  38.80241 1.000 39.18248  ?  100  GLN   A NE2 1 
ATOM   437  N N   . ASN   A 1 101 ? 23.27612 31.14602  37.65021 1.000 43.54595  ?  101  ASN   A N   1 
ATOM   438  C CA  . ASN   A 1 101 ? 23.00023 32.07050  36.56007 1.000 47.16478  ?  101  ASN   A CA  1 
ATOM   439  C C   . ASN   A 1 101 ? 21.60597 31.79311  36.01717 1.000 49.53833  ?  101  ASN   A C   1 
ATOM   440  O O   . ASN   A 1 101 ? 20.93713 30.83773  36.41809 1.000 47.07809  ?  101  ASN   A O   1 
ATOM   441  C CB  . ASN   A 1 101 ? 24.05665 31.97742  35.44974 1.000 47.86967  ?  101  ASN   A CB  1 
ATOM   442  C CG  . ASN   A 1 101 ? 24.19160 30.57862  34.87991 1.000 48.84879  ?  101  ASN   A CG  1 
ATOM   443  O OD1 . ASN   A 1 101 ? 23.27983 30.06657  34.23023 1.000 50.06414  ?  101  ASN   A OD1 1 
ATOM   444  N ND2 . ASN   A 1 101 ? 25.34206 29.95740  35.11036 1.000 47.30973  ?  101  ASN   A ND2 1 
ATOM   445  N N   . GLN   A 1 102 ? 21.17541 32.64950  35.08782 1.000 51.60703  ?  102  GLN   A N   1 
ATOM   446  C CA  . GLN   A 1 102 ? 19.82396 32.54454  34.54636 1.000 51.80057  ?  102  GLN   A CA  1 
ATOM   447  C C   . GLN   A 1 102 ? 19.65050 31.28096  33.71274 1.000 50.63512  ?  102  GLN   A C   1 
ATOM   448  O O   . GLN   A 1 102 ? 18.60289 30.62723  33.77953 1.000 51.83587  ?  102  GLN   A O   1 
ATOM   449  C CB  . GLN   A 1 102 ? 19.49876 33.78248  33.71143 1.000 55.96149  ?  102  GLN   A CB  1 
ATOM   450  C CG  . GLN   A 1 102 ? 18.85837 34.91396  34.49518 1.000 59.44901  ?  102  GLN   A CG  1 
ATOM   451  C CD  . GLN   A 1 102 ? 17.34640 34.82958  34.50271 1.000 66.48051  ?  102  GLN   A CD  1 
ATOM   452  O OE1 . GLN   A 1 102 ? 16.72766 34.67075  35.55394 1.000 67.55324  ?  102  GLN   A OE1 1 
ATOM   453  N NE2 . GLN   A 1 102 ? 16.74253 34.92899  33.32452 1.000 71.34549  ?  102  GLN   A NE2 1 
ATOM   454  N N   . THR   A 1 103 ? 20.66262 30.92383  32.91914 1.000 51.74708  ?  103  THR   A N   1 
ATOM   455  C CA  . THR   A 1 103 ? 20.54887 29.75594  32.05032 1.000 53.22293  ?  103  THR   A CA  1 
ATOM   456  C C   . THR   A 1 103 ? 20.39171 28.47767  32.86502 1.000 52.51097  ?  103  THR   A C   1 
ATOM   457  O O   . THR   A 1 103 ? 19.52764 27.64280  32.57310 1.000 55.89538  ?  103  THR   A O   1 
ATOM   458  C CB  . THR   A 1 103 ? 21.76895 29.66339  31.13289 1.000 54.77645  ?  103  THR   A CB  1 
ATOM   459  O OG1 . THR   A 1 103 ? 22.01374 30.94023  30.53002 1.000 58.59533  ?  103  THR   A OG1 1 
ATOM   460  C CG2 . THR   A 1 103 ? 21.53654 28.62979  30.04174 1.000 57.78011  ?  103  THR   A CG2 1 
ATOM   461  N N   . HIS   A 1 104 ? 21.22210 28.30818  33.89583 1.000 51.38003  ?  104  HIS   A N   1 
ATOM   462  C CA  . HIS   A 1 104 ? 21.11547 27.12373  34.74119 1.000 50.87625  ?  104  HIS   A CA  1 
ATOM   463  C C   . HIS   A 1 104 ? 19.81505 27.12694  35.53613 1.000 49.09375  ?  104  HIS   A C   1 
ATOM   464  O O   . HIS   A 1 104 ? 19.17657 26.08038  35.69619 1.000 48.73465  ?  104  HIS   A O   1 
ATOM   465  C CB  . HIS   A 1 104 ? 22.31693 27.04161  35.68332 1.000 49.32989  ?  104  HIS   A CB  1 
ATOM   466  C CG  . HIS   A 1 104 ? 23.52273 26.39352  35.07777 1.000 55.36697  ?  104  HIS   A CG  1 
ATOM   467  N ND1 . HIS   A 1 104 ? 24.75362 27.01172  35.03027 1.000 54.53210  ?  104  HIS   A ND1 1 
ATOM   468  C CD2 . HIS   A 1 104 ? 23.69003 25.17862  34.50413 1.000 68.34822  ?  104  HIS   A CD2 1 
ATOM   469  C CE1 . HIS   A 1 104 ? 25.62578 26.20844  34.44805 1.000 58.96324  ?  104  HIS   A CE1 1 
ATOM   470  N NE2 . HIS   A 1 104 ? 25.00587 25.08944  34.11924 1.000 73.04804  ?  104  HIS   A NE2 1 
ATOM   471  N N   . ALA   A 1 105 ? 19.40213 28.29580  36.03327 1.000 48.70271  ?  105  ALA   A N   1 
ATOM   472  C CA  . ALA   A 1 105 ? 18.21732 28.36357  36.88361 1.000 49.22683  ?  105  ALA   A CA  1 
ATOM   473  C C   . ALA   A 1 105 ? 16.93859 28.16644  36.08030 1.000 50.32780  ?  105  ALA   A C   1 
ATOM   474  O O   . ALA   A 1 105 ? 16.00308 27.50674  36.54796 1.000 51.37662  ?  105  ALA   A O   1 
ATOM   475  C CB  . ALA   A 1 105 ? 18.18153 29.69670  37.62883 1.000 49.02222  ?  105  ALA   A CB  1 
ATOM   476  N N   . LYS   A 1 106 ? 16.87286 28.73911  34.87599 1.000 51.34881  ?  106  LYS   A N   1 
ATOM   477  C CA  . LYS   A 1 106 ? 15.68931 28.56151  34.04069 1.000 51.86764  ?  106  LYS   A CA  1 
ATOM   478  C C   . LYS   A 1 106 ? 15.49565 27.09838  33.66727 1.000 51.41896  ?  106  LYS   A C   1 
ATOM   479  O O   . LYS   A 1 106 ? 14.36774 26.59216  33.66951 1.000 53.25267  ?  106  LYS   A O   1 
ATOM   480  C CB  . LYS   A 1 106 ? 15.79842 29.42178  32.78193 1.000 54.18860  ?  106  LYS   A CB  1 
ATOM   481  C CG  . LYS   A 1 106 ? 15.01090 30.71933  32.83563 1.000 58.12795  ?  106  LYS   A CG  1 
ATOM   482  C CD  . LYS   A 1 106 ? 15.26240 31.55855  31.59252 1.000 63.30653  ?  106  LYS   A CD  1 
ATOM   483  C CE  . LYS   A 1 106 ? 14.50235 32.87314  31.64460 1.000 70.20396  ?  106  LYS   A CE  1 
ATOM   484  N NZ  . LYS   A 1 106 ? 13.02846 32.66806  31.58026 1.000 78.39814  ?  106  LYS   A NZ  1 
ATOM   485  N N   . ARG   A 1 107 ? 16.58780 26.40080  33.35033 1.000 51.97732  ?  107  ARG   A N   1 
ATOM   486  C CA  . ARG   A 1 107 ? 16.48304 25.00207  32.95006 1.000 55.03104  ?  107  ARG   A CA  1 
ATOM   487  C C   . ARG   A 1 107 ? 16.17852 24.10525  34.14299 1.000 53.21715  ?  107  ARG   A C   1 
ATOM   488  O O   . ARG   A 1 107 ? 15.35989 23.18445  34.04045 1.000 53.10608  ?  107  ARG   A O   1 
ATOM   489  C CB  . ARG   A 1 107 ? 17.77325 24.56167  32.26060 1.000 61.97357  ?  107  ARG   A CB  1 
ATOM   490  C CG  . ARG   A 1 107 ? 17.82776 23.08557  31.90458 1.000 68.15172  ?  107  ARG   A CG  1 
ATOM   491  C CD  . ARG   A 1 107 ? 18.86498 22.80166  30.82216 1.000 78.91222  ?  107  ARG   A CD  1 
ATOM   492  N NE  . ARG   A 1 107 ? 18.77965 23.72608  29.69642 1.000 82.84318  ?  107  ARG   A NE  1 
ATOM   493  C CZ  . ARG   A 1 107 ? 19.58556 24.76389  29.51221 1.000 81.90977  ?  107  ARG   A CZ  1 
ATOM   494  N NH1 . ARG   A 1 107 ? 20.55228 25.04990  30.36968 1.000 79.08572  ?  107  ARG   A NH1 1 
ATOM   495  N NH2 . ARG   A 1 107 ? 19.41497 25.53626  28.44300 1.000 84.28021  ?  107  ARG   A NH2 1 
ATOM   496  N N   . ALA   A 1 108 ? 16.82583 24.35792  35.28249 1.000 55.07256  ?  108  ALA   A N   1 
ATOM   497  C CA  . ALA   A 1 108 ? 16.59852 23.53000  36.46240 1.000 52.32226  ?  108  ALA   A CA  1 
ATOM   498  C C   . ALA   A 1 108 ? 15.16735 23.67026  36.96407 1.000 53.29627  ?  108  ALA   A C   1 
ATOM   499  O O   . ALA   A 1 108 ? 14.49781 22.67186  37.25161 1.000 55.50987  ?  108  ALA   A O   1 
ATOM   500  C CB  . ALA   A 1 108 ? 17.59410 23.89803  37.56097 1.000 48.69146  ?  108  ALA   A CB  1 
ATOM   501  N N   . TYR   A 1 109 ? 14.67948 24.90855  37.07325 1.000 52.01252  ?  109  TYR   A N   1 
ATOM   502  C CA  . TYR   A 1 109 ? 13.31182 25.12530  37.53438 1.000 53.24306  ?  109  TYR   A CA  1 
ATOM   503  C C   . TYR   A 1 109 ? 12.30059 24.54407  36.55516 1.000 54.14094  ?  109  TYR   A C   1 
ATOM   504  O O   . TYR   A 1 109 ? 11.24762 24.04112  36.96412 1.000 55.25986  ?  109  TYR   A O   1 
ATOM   505  C CB  . TYR   A 1 109 ? 13.05632 26.61785  37.74272 1.000 51.62864  ?  109  TYR   A CB  1 
ATOM   506  C CG  . TYR   A 1 109 ? 11.69161 26.92802  38.31487 1.000 52.38685  ?  109  TYR   A CG  1 
ATOM   507  C CD1 . TYR   A 1 109 ? 11.30660 26.42863  39.55215 1.000 53.12754  ?  109  TYR   A CD1 1 
ATOM   508  C CD2 . TYR   A 1 109 ? 10.78689 27.71722  37.61654 1.000 55.45878  ?  109  TYR   A CD2 1 
ATOM   509  C CE1 . TYR   A 1 109 ? 10.06000 26.70849  40.07986 1.000 54.57460  ?  109  TYR   A CE1 1 
ATOM   510  C CE2 . TYR   A 1 109 ? 9.53742  28.00245  38.13607 1.000 60.20458  ?  109  TYR   A CE2 1 
ATOM   511  C CZ  . TYR   A 1 109 ? 9.17972  27.49536  39.36774 1.000 58.20547  ?  109  TYR   A CZ  1 
ATOM   512  O OH  . TYR   A 1 109 ? 7.93770  27.77516  39.88974 1.000 61.75009  ?  109  TYR   A OH  1 
ATOM   513  N N   . ARG   A 1 110 ? 12.60326 24.60352  35.25727 1.000 58.22920  ?  110  ARG   A N   1 
ATOM   514  C CA  . ARG   A 1 110 ? 11.69839 24.05587  34.25227 1.000 57.98480  ?  110  ARG   A CA  1 
ATOM   515  C C   . ARG   A 1 110 ? 11.52724 22.55233  34.43200 1.000 59.86088  ?  110  ARG   A C   1 
ATOM   516  O O   . ARG   A 1 110 ? 10.42277 22.06455  34.69582 1.000 62.00174  ?  110  ARG   A O   1 
ATOM   517  C CB  . ARG   A 1 110 ? 12.22050 24.37719  32.85051 1.000 56.98533  ?  110  ARG   A CB  1 
ATOM   518  C CG  . ARG   A 1 110 ? 11.16029 24.33436  31.76369 1.000 60.09326  ?  110  ARG   A CG  1 
ATOM   519  C CD  . ARG   A 1 110 ? 11.79122 24.34401  30.38058 1.000 66.80504  ?  110  ARG   A CD  1 
ATOM   520  N NE  . ARG   A 1 110 ? 10.91897 23.74424  29.37795 1.000 59.68743  ?  110  ARG   A NE  1 
ATOM   521  C CZ  . ARG   A 1 110 ? 10.32517 24.41829  28.40270 1.000 60.07205  ?  110  ARG   A CZ  1 
ATOM   522  N NH1 . ARG   A 1 110 ? 10.48735 25.72398  28.26703 1.000 67.72378  ?  110  ARG   A NH1 1 
ATOM   523  N NH2 . ARG   A 1 110 ? 9.54787  23.76618  27.54287 1.000 55.99836  ?  110  ARG   A NH2 1 
ATOM   524  N N   . GLU   A 1 111 ? 12.62276 21.80032  34.30671 1.000 55.60909  ?  111  GLU   A N   1 
ATOM   525  C CA  . GLU   A 1 111 ? 12.54251 20.34531  34.35592 1.000 57.81095  ?  111  GLU   A CA  1 
ATOM   526  C C   . GLU   A 1 111 ? 12.19127 19.82074  35.74286 1.000 58.66178  ?  111  GLU   A C   1 
ATOM   527  O O   . GLU   A 1 111 ? 11.75805 18.66979  35.86152 1.000 60.64329  ?  111  GLU   A O   1 
ATOM   528  C CB  . GLU   A 1 111 ? 13.86151 19.73599  33.87817 1.000 59.46459  ?  111  GLU   A CB  1 
ATOM   529  C CG  . GLU   A 1 111 ? 14.46498 20.45530  32.67995 1.000 59.30600  ?  111  GLU   A CG  1 
ATOM   530  C CD  . GLU   A 1 111 ? 15.14014 19.51266  31.70420 1.000 54.63453  ?  111  GLU   A CD  1 
ATOM   531  O OE1 . GLU   A 1 111 ? 15.43374 18.36233  32.09131 1.000 57.61295  ?  111  GLU   A OE1 1 
ATOM   532  O OE2 . GLU   A 1 111 ? 15.37777 19.92354  30.54866 1.000 51.81984  -1 111  GLU   A OE2 1 
ATOM   533  N N   . LEU   A 1 112 ? 12.36399 20.62942  36.79148 1.000 58.03404  ?  112  LEU   A N   1 
ATOM   534  C CA  . LEU   A 1 112 ? 11.96084 20.19033  38.12362 1.000 58.43570  ?  112  LEU   A CA  1 
ATOM   535  C C   . LEU   A 1 112 ? 10.44643 20.20458  38.28250 1.000 61.59596  ?  112  LEU   A C   1 
ATOM   536  O O   . LEU   A 1 112 ? 9.89647  19.40189  39.04526 1.000 67.63856  ?  112  LEU   A O   1 
ATOM   537  C CB  . LEU   A 1 112 ? 12.61164 21.06848  39.19257 1.000 55.43835  ?  112  LEU   A CB  1 
ATOM   538  C CG  . LEU   A 1 112 ? 13.60053 20.38532  40.14003 1.000 52.26627  ?  112  LEU   A CG  1 
ATOM   539  C CD1 . LEU   A 1 112 ? 13.86802 21.25901  41.35636 1.000 50.82900  ?  112  LEU   A CD1 1 
ATOM   540  C CD2 . LEU   A 1 112 ? 13.09007 19.01557  40.56174 1.000 50.34044  ?  112  LEU   A CD2 1 
ATOM   541  N N   . VAL   A 1 113 ? 9.75965  21.10202  37.57511 1.000 61.19585  ?  113  VAL   A N   1 
ATOM   542  C CA  . VAL   A 1 113 ? 8.30622  21.17682  37.67294 1.000 62.37167  ?  113  VAL   A CA  1 
ATOM   543  C C   . VAL   A 1 113 ? 7.64869  20.18364  36.72345 1.000 68.57870  ?  113  VAL   A C   1 
ATOM   544  O O   . VAL   A 1 113 ? 6.65823  19.53299  37.07546 1.000 74.20697  ?  113  VAL   A O   1 
ATOM   545  C CB  . VAL   A 1 113 ? 7.83331  22.61740  37.40255 1.000 62.13127  ?  113  VAL   A CB  1 
ATOM   546  C CG1 . VAL   A 1 113 ? 6.31333  22.68852  37.37953 1.000 62.18267  ?  113  VAL   A CG1 1 
ATOM   547  C CG2 . VAL   A 1 113 ? 8.39959  23.56690  38.44517 1.000 59.97156  ?  113  VAL   A CG2 1 
ATOM   548  N N   . LEU   A 1 114 ? 8.19372  20.03960  35.51337 1.000 67.41465  ?  114  LEU   A N   1 
ATOM   549  C CA  . LEU   A 1 114 ? 7.54192  19.21614  34.50108 1.000 70.04123  ?  114  LEU   A CA  1 
ATOM   550  C C   . LEU   A 1 114 ? 7.65115  17.73166  34.81690 1.000 73.86259  ?  114  LEU   A C   1 
ATOM   551  O O   . LEU   A 1 114 ? 6.80739  16.94078  34.38102 1.000 76.77894  ?  114  LEU   A O   1 
ATOM   552  C CB  . LEU   A 1 114 ? 8.13982  19.51243  33.12618 1.000 63.89922  ?  114  LEU   A CB  1 
ATOM   553  C CG  . LEU   A 1 114 ? 8.16743  20.98829  32.72028 1.000 61.15569  ?  114  LEU   A CG  1 
ATOM   554  C CD1 . LEU   A 1 114 ? 9.10160  21.21117  31.54069 1.000 59.13496  ?  114  LEU   A CD1 1 
ATOM   555  C CD2 . LEU   A 1 114 ? 6.76806  21.49629  32.40670 1.000 61.52681  ?  114  LEU   A CD2 1 
ATOM   556  N N   . MET   A 1 115 ? 8.66324  17.33282  35.57553 1.000 69.92353  ?  115  MET   A N   1 
ATOM   557  C CA  . MET   A 1 115 ? 8.87709  15.91435  35.80506 1.000 73.12173  ?  115  MET   A CA  1 
ATOM   558  C C   . MET   A 1 115 ? 7.97017  15.35611  36.89634 1.000 81.94593  ?  115  MET   A C   1 
ATOM   559  O O   . MET   A 1 115 ? 7.84588  14.13197  37.02052 1.000 80.56135  ?  115  MET   A O   1 
ATOM   560  C CB  . MET   A 1 115 ? 10.34947 15.68327  36.13278 1.000 68.38897  ?  115  MET   A CB  1 
ATOM   561  C CG  . MET   A 1 115 ? 11.08860 14.95104  35.03797 1.000 68.30249  ?  115  MET   A CG  1 
ATOM   562  S SD  . MET   A 1 115 ? 12.86906 14.95196  35.25751 1.000 76.97467  ?  115  MET   A SD  1 
ATOM   563  C CE  . MET   A 1 115 ? 13.03234 13.75468  36.57169 1.000 59.92289  ?  115  MET   A CE  1 
ATOM   564  N N   . LYS   A 1 116 ? 7.33172  16.22278  37.67707 1.000 100.62914 ?  116  LYS   A N   1 
ATOM   565  C CA  . LYS   A 1 116 ? 6.21852  15.84442  38.53230 1.000 102.68435 ?  116  LYS   A CA  1 
ATOM   566  C C   . LYS   A 1 116 ? 4.87653  16.21401  37.91745 1.000 103.61894 ?  116  LYS   A C   1 
ATOM   567  O O   . LYS   A 1 116 ? 3.83192  15.90111  38.49727 1.000 104.32083 ?  116  LYS   A O   1 
ATOM   568  C CB  . LYS   A 1 116 ? 6.36041  16.50048  39.90841 1.000 104.05005 ?  116  LYS   A CB  1 
ATOM   569  C CG  . LYS   A 1 116 ? 7.59072  16.05790  40.68113 1.000 103.49174 ?  116  LYS   A CG  1 
ATOM   570  C CD  . LYS   A 1 116 ? 8.26636  17.23546  41.36226 1.000 104.06965 ?  116  LYS   A CD  1 
ATOM   571  C CE  . LYS   A 1 116 ? 7.48598  17.68259  42.58765 1.000 113.68995 ?  116  LYS   A CE  1 
ATOM   572  N NZ  . LYS   A 1 116 ? 8.03702  18.93729  43.16922 1.000 104.29390 ?  116  LYS   A NZ  1 
ATOM   573  N N   . CYS   A 1 117 ? 4.88608  16.87018  36.75641 1.000 92.40971  ?  117  CYS   A N   1 
ATOM   574  C CA  . CYS   A 1 117 ? 3.67219  17.27158  36.06126 1.000 84.37075  ?  117  CYS   A CA  1 
ATOM   575  C C   . CYS   A 1 117 ? 3.34430  16.37972  34.87037 1.000 83.89987  ?  117  CYS   A C   1 
ATOM   576  O O   . CYS   A 1 117 ? 2.16904  16.26848  34.50522 1.000 88.24269  ?  117  CYS   A O   1 
ATOM   577  C CB  . CYS   A 1 117 ? 3.80067  18.73175  35.59832 1.000 88.24467  ?  117  CYS   A CB  1 
ATOM   578  S SG  . CYS   A 1 117 ? 2.77271  19.22718  34.19412 1.000 111.22028 ?  117  CYS   A SG  1 
ATOM   579  N N   . VAL   A 1 118 ? 4.34128  15.72341  34.28029 1.000 87.10421  ?  118  VAL   A N   1 
ATOM   580  C CA  . VAL   A 1 118 ? 4.16419  14.89813  33.09101 1.000 82.63769  ?  118  VAL   A CA  1 
ATOM   581  C C   . VAL   A 1 118 ? 4.66472  13.49275  33.39667 1.000 82.90636  ?  118  VAL   A C   1 
ATOM   582  O O   . VAL   A 1 118 ? 5.77485  13.32349  33.91543 1.000 80.33219  ?  118  VAL   A O   1 
ATOM   583  C CB  . VAL   A 1 118 ? 4.90717  15.49398  31.87961 1.000 77.34073  ?  118  VAL   A CB  1 
ATOM   584  C CG1 . VAL   A 1 118 ? 5.31313  14.40260  30.89569 1.000 71.74950  ?  118  VAL   A CG1 1 
ATOM   585  C CG2 . VAL   A 1 118 ? 4.04975  16.54546  31.19618 1.000 76.40866  ?  118  VAL   A CG2 1 
ATOM   586  N N   . ASN   A 1 119 ? 3.84560  12.48873  33.08118 1.000 82.13934  ?  119  ASN   A N   1 
ATOM   587  C CA  . ASN   A 1 119 ? 4.24669  11.09408  33.19529 1.000 84.01593  ?  119  ASN   A CA  1 
ATOM   588  C C   . ASN   A 1 119 ? 3.99025  10.37942  31.87483 1.000 84.68424  ?  119  ASN   A C   1 
ATOM   589  O O   . ASN   A 1 119 ? 3.06144  10.72036  31.13453 1.000 86.90839  ?  119  ASN   A O   1 
ATOM   590  C CB  . ASN   A 1 119 ? 3.52344  10.37229  34.35681 1.000 88.70813  ?  119  ASN   A CB  1 
ATOM   591  C CG  . ASN   A 1 119 ? 2.06250  10.06340  34.05612 1.000 95.78626  ?  119  ASN   A CG  1 
ATOM   592  O OD1 . ASN   A 1 119 ? 1.42124  10.72383  33.23967 1.000 95.30127  ?  119  ASN   A OD1 1 
ATOM   593  N ND2 . ASN   A 1 119 ? 1.53272  9.04242   34.72119 1.000 96.93369  ?  119  ASN   A ND2 1 
ATOM   594  N N   . HIS   A 1 120 ? 4.83505  9.39107   31.58572 1.000 69.68201  ?  120  HIS   A N   1 
ATOM   595  C CA  . HIS   A 1 120 ? 4.74696  8.59890   30.36610 1.000 62.35752  ?  120  HIS   A CA  1 
ATOM   596  C C   . HIS   A 1 120 ? 5.79723  7.50467   30.44093 1.000 56.11635  ?  120  HIS   A C   1 
ATOM   597  O O   . HIS   A 1 120 ? 6.79876  7.63037   31.15302 1.000 54.32715  ?  120  HIS   A O   1 
ATOM   598  C CB  . HIS   A 1 120 ? 4.95559  9.45360   29.10914 1.000 60.00137  ?  120  HIS   A CB  1 
ATOM   599  C CG  . HIS   A 1 120 ? 4.39495  8.84351   27.86217 1.000 60.84485  ?  120  HIS   A CG  1 
ATOM   600  N ND1 . HIS   A 1 120 ? 5.15980  8.10178   26.98814 1.000 56.96679  ?  120  HIS   A ND1 1 
ATOM   601  C CD2 . HIS   A 1 120 ? 3.14378  8.86082   27.34478 1.000 65.30291  ?  120  HIS   A CD2 1 
ATOM   602  C CE1 . HIS   A 1 120 ? 4.40604  7.69231   25.98372 1.000 59.92596  ?  120  HIS   A CE1 1 
ATOM   603  N NE2 . HIS   A 1 120 ? 3.17808  8.13876   26.17637 1.000 67.98007  ?  120  HIS   A NE2 1 
ATOM   604  N N   . LYS   A 1 121 ? 5.55459  6.42772   29.69104 1.000 53.22890  ?  121  LYS   A N   1 
ATOM   605  C CA  . LYS   A 1 121 ? 6.53115  5.34856   29.63094 1.000 50.81343  ?  121  LYS   A CA  1 
ATOM   606  C C   . LYS   A 1 121 ? 7.78021  5.76608   28.86558 1.000 48.14149  ?  121  LYS   A C   1 
ATOM   607  O O   . LYS   A 1 121 ? 8.86865  5.24085   29.12519 1.000 45.04419  ?  121  LYS   A O   1 
ATOM   608  C CB  . LYS   A 1 121 ? 5.90846  4.10959   28.99125 1.000 52.93836  ?  121  LYS   A CB  1 
ATOM   609  C CG  . LYS   A 1 121 ? 5.06844  4.40128   27.75946 1.000 56.91928  ?  121  LYS   A CG  1 
ATOM   610  C CD  . LYS   A 1 121 ? 4.92418  3.16886   26.88264 1.000 74.65313  ?  121  LYS   A CD  1 
ATOM   611  C CE  . LYS   A 1 121 ? 4.23732  3.50450   25.57044 1.000 86.52544  ?  121  LYS   A CE  1 
ATOM   612  N NZ  . LYS   A 1 121 ? 5.19655  3.55719   24.43192 1.000 80.40347  ?  121  LYS   A NZ  1 
ATOM   613  N N   . ASN   A 1 122 ? 7.64830  6.70223   27.92786 1.000 51.08694  ?  122  ASN   A N   1 
ATOM   614  C CA  . ASN   A 1 122 ? 8.76731  7.16666   27.11992 1.000 45.92967  ?  122  ASN   A CA  1 
ATOM   615  C C   . ASN   A 1 122 ? 9.31411  8.51127   27.57849 1.000 44.63441  ?  122  ASN   A C   1 
ATOM   616  O O   . ASN   A 1 122 ? 10.29480 8.99417   27.00566 1.000 48.73185  ?  122  ASN   A O   1 
ATOM   617  C CB  . ASN   A 1 122 ? 8.35496  7.24791   25.64798 1.000 49.73635  ?  122  ASN   A CB  1 
ATOM   618  C CG  . ASN   A 1 122 ? 8.12047  5.88198   25.03646 1.000 49.81921  ?  122  ASN   A CG  1 
ATOM   619  O OD1 . ASN   A 1 122 ? 7.14513  5.67058   24.31814 1.000 51.80499  ?  122  ASN   A OD1 1 
ATOM   620  N ND2 . ASN   A 1 122 ? 9.01591  4.94373   25.32273 1.000 46.08390  ?  122  ASN   A ND2 1 
ATOM   621  N N   . ILE   A 1 123 ? 8.70003  9.13117   28.58133 1.000 47.89243  ?  123  ILE   A N   1 
ATOM   622  C CA  . ILE   A 1 123 ? 9.23567  10.32165  29.22868 1.000 47.20614  ?  123  ILE   A CA  1 
ATOM   623  C C   . ILE   A 1 123 ? 9.70547  9.91737   30.61537 1.000 46.90812  ?  123  ILE   A C   1 
ATOM   624  O O   . ILE   A 1 123 ? 8.94212  9.32443   31.38772 1.000 50.38844  ?  123  ILE   A O   1 
ATOM   625  C CB  . ILE   A 1 123 ? 8.19637  11.45216  29.30451 1.000 47.48514  ?  123  ILE   A CB  1 
ATOM   626  C CG1 . ILE   A 1 123 ? 7.63063  11.74488  27.91387 1.000 47.68280  ?  123  ILE   A CG1 1 
ATOM   627  C CG2 . ILE   A 1 123 ? 8.81567  12.70395  29.90989 1.000 46.61892  ?  123  ILE   A CG2 1 
ATOM   628  C CD1 . ILE   A 1 123 ? 8.64452  12.32581  26.95367 1.000 44.16050  ?  123  ILE   A CD1 1 
ATOM   629  N N   . ILE   A 1 124 ? 10.96520 10.22674  30.92571 1.000 44.41593  ?  124  ILE   A N   1 
ATOM   630  C CA  . ILE   A 1 124 ? 11.54483 9.77338   32.18218 1.000 48.02031  ?  124  ILE   A CA  1 
ATOM   631  C C   . ILE   A 1 124 ? 10.78308 10.38116  33.35401 1.000 49.87052  ?  124  ILE   A C   1 
ATOM   632  O O   . ILE   A 1 124 ? 10.28916 11.51375  33.28483 1.000 53.86645  ?  124  ILE   A O   1 
ATOM   633  C CB  . ILE   A 1 124 ? 13.04851 10.10229  32.21807 1.000 49.98191  ?  124  ILE   A CB  1 
ATOM   634  C CG1 . ILE   A 1 124 ? 13.31513 11.57563  32.49897 1.000 50.92780  ?  124  ILE   A CG1 1 
ATOM   635  C CG2 . ILE   A 1 124 ? 13.72967 9.69147   30.94119 1.000 49.23505  ?  124  ILE   A CG2 1 
ATOM   636  C CD1 . ILE   A 1 124 ? 13.71451 11.80478  33.90272 1.000 50.00162  ?  124  ILE   A CD1 1 
ATOM   637  N N   . SER   A 1 125 ? 10.65644 9.61096   34.42859 1.000 54.76402  ?  125  SER   A N   1 
ATOM   638  C CA  . SER   A 1 125 ? 9.91005  10.02176  35.60523 1.000 56.29253  ?  125  SER   A CA  1 
ATOM   639  C C   . SER   A 1 125 ? 10.84795 10.20673  36.79313 1.000 51.53116  ?  125  SER   A C   1 
ATOM   640  O O   . SER   A 1 125 ? 11.93036 9.62275   36.85942 1.000 52.73747  ?  125  SER   A O   1 
ATOM   641  C CB  . SER   A 1 125 ? 8.81835  8.99763   35.93760 1.000 62.89491  ?  125  SER   A CB  1 
ATOM   642  O OG  . SER   A 1 125 ? 7.79475  9.00473   34.95312 1.000 59.90628  ?  125  SER   A OG  1 
ATOM   643  N N   . LEU   A 1 126 ? 10.41290 11.04445  37.73037 1.000 52.65879  ?  126  LEU   A N   1 
ATOM   644  C CA  . LEU   A 1 126 ? 11.15060 11.34787  38.95349 1.000 49.39360  ?  126  LEU   A CA  1 
ATOM   645  C C   . LEU   A 1 126 ? 10.90531 10.28425  40.01613 1.000 45.03530  ?  126  LEU   A C   1 
ATOM   646  O O   . LEU   A 1 126 ? 9.75598  9.94525   40.31800 1.000 43.36350  ?  126  LEU   A O   1 
ATOM   647  C CB  . LEU   A 1 126 ? 10.74716 12.73063  39.47353 1.000 52.45038  ?  126  LEU   A CB  1 
ATOM   648  C CG  . LEU   A 1 126 ? 11.63176 13.64388  40.32270 1.000 50.06321  ?  126  LEU   A CG  1 
ATOM   649  C CD1 . LEU   A 1 126 ? 13.10568 13.60302  40.00763 1.000 45.28642  ?  126  LEU   A CD1 1 
ATOM   650  C CD2 . LEU   A 1 126 ? 11.09583 15.07844  40.12692 1.000 62.44165  ?  126  LEU   A CD2 1 
ATOM   651  N N   . LEU   A 1 127 ? 11.99255 9.76154   40.57835 1.000 41.96430  ?  127  LEU   A N   1 
ATOM   652  C CA  . LEU   A 1 127 ? 11.93062 8.80744   41.67624 1.000 42.62300  ?  127  LEU   A CA  1 
ATOM   653  C C   . LEU   A 1 127 ? 12.10121 9.46482   43.03836 1.000 41.32833  ?  127  LEU   A C   1 
ATOM   654  O O   . LEU   A 1 127 ? 11.40475 9.09287   43.98690 1.000 41.04235  ?  127  LEU   A O   1 
ATOM   655  C CB  . LEU   A 1 127 ? 12.99648 7.72197   41.49501 1.000 41.59665  ?  127  LEU   A CB  1 
ATOM   656  C CG  . LEU   A 1 127 ? 12.66025 6.58388   40.52754 1.000 40.57257  ?  127  LEU   A CG  1 
ATOM   657  C CD1 . LEU   A 1 127 ? 13.66437 5.44657   40.65666 1.000 40.46160  ?  127  LEU   A CD1 1 
ATOM   658  C CD2 . LEU   A 1 127 ? 11.24318 6.08006   40.75368 1.000 41.60177  ?  127  LEU   A CD2 1 
ATOM   659  N N   . ASN   A 1 128 ? 13.00504 10.43719  43.15667 1.000 37.18901  ?  128  ASN   A N   1 
ATOM   660  C CA  . ASN   A 1 128 ? 13.23318 11.12579  44.41952 1.000 38.63784  ?  128  ASN   A CA  1 
ATOM   661  C C   . ASN   A 1 128 ? 14.05451 12.38081  44.16565 1.000 42.49407  ?  128  ASN   A C   1 
ATOM   662  O O   . ASN   A 1 128 ? 14.93650 12.38503  43.30414 1.000 39.20215  ?  128  ASN   A O   1 
ATOM   663  C CB  . ASN   A 1 128 ? 13.95445 10.21872  45.42616 1.000 39.33544  ?  128  ASN   A CB  1 
ATOM   664  C CG  . ASN   A 1 128 ? 14.00233 10.81583  46.81818 1.000 42.07658  ?  128  ASN   A CG  1 
ATOM   665  O OD1 . ASN   A 1 128 ? 13.21478 11.70034  47.15431 1.000 44.37105  ?  128  ASN   A OD1 1 
ATOM   666  N ND2 . ASN   A 1 128 ? 14.92960 10.33338  47.63731 1.000 43.10671  ?  128  ASN   A ND2 1 
ATOM   667  N N   . VAL   A 1 129 ? 13.75346 13.43847  44.91651 1.000 42.82805  ?  129  VAL   A N   1 
ATOM   668  C CA  . VAL   A 1 129 ? 14.52710 14.67409  44.90926 1.000 40.43430  ?  129  VAL   A CA  1 
ATOM   669  C C   . VAL   A 1 129 ? 14.97515 14.95692  46.33411 1.000 39.26088  ?  129  VAL   A C   1 
ATOM   670  O O   . VAL   A 1 129 ? 14.22868 14.70718  47.28741 1.000 37.52065  ?  129  VAL   A O   1 
ATOM   671  C CB  . VAL   A 1 129 ? 13.71992 15.86682  44.35469 1.000 39.19585  ?  129  VAL   A CB  1 
ATOM   672  C CG1 . VAL   A 1 129 ? 14.63703 17.05160  44.08208 1.000 38.49645  ?  129  VAL   A CG1 1 
ATOM   673  C CG2 . VAL   A 1 129 ? 12.98330 15.47040  43.10002 1.000 38.84414  ?  129  VAL   A CG2 1 
ATOM   674  N N   . PHE   A 1 130 ? 16.19010 15.48040  46.47859 1.000 36.31913  ?  130  PHE   A N   1 
ATOM   675  C CA  . PHE   A 1 130 ? 16.70166 15.81428  47.79880 1.000 38.32918  ?  130  PHE   A CA  1 
ATOM   676  C C   . PHE   A 1 130 ? 17.90015 16.73811  47.65857 1.000 36.39541  ?  130  PHE   A C   1 
ATOM   677  O O   . PHE   A 1 130 ? 18.55960 16.78483  46.61660 1.000 38.55313  ?  130  PHE   A O   1 
ATOM   678  C CB  . PHE   A 1 130 ? 17.08947 14.55960  48.59071 1.000 36.65747  ?  130  PHE   A CB  1 
ATOM   679  C CG  . PHE   A 1 130 ? 18.09739 13.68712  47.89738 1.000 34.27938  ?  130  PHE   A CG  1 
ATOM   680  C CD1 . PHE   A 1 130 ? 19.45445 13.85447  48.12448 1.000 33.39951  ?  130  PHE   A CD1 1 
ATOM   681  C CD2 . PHE   A 1 130 ? 17.68774 12.69257  47.02617 1.000 35.77292  ?  130  PHE   A CD2 1 
ATOM   682  C CE1 . PHE   A 1 130 ? 20.38201 13.04955  47.49112 1.000 32.37576  ?  130  PHE   A CE1 1 
ATOM   683  C CE2 . PHE   A 1 130 ? 18.61005 11.88591  46.39000 1.000 34.33189  ?  130  PHE   A CE2 1 
ATOM   684  C CZ  . PHE   A 1 130 ? 19.95834 12.06312  46.62281 1.000 31.19109  ?  130  PHE   A CZ  1 
ATOM   685  N N   . THR   A 1 131 ? 18.16609 17.47546  48.73266 1.000 38.22188  ?  131  THR   A N   1 
ATOM   686  C CA  . THR   A 1 131 ? 19.37801 18.25428  48.89142 1.000 38.72771  ?  131  THR   A CA  1 
ATOM   687  C C   . THR   A 1 131 ? 19.99199 17.92526  50.24486 1.000 41.46641  ?  131  THR   A C   1 
ATOM   688  O O   . THR   A 1 131 ? 19.27093 17.81692  51.24444 1.000 41.48625  ?  131  THR   A O   1 
ATOM   689  C CB  . THR   A 1 131 ? 19.10017 19.76403  48.79146 1.000 39.77914  ?  131  THR   A CB  1 
ATOM   690  O OG1 . THR   A 1 131 ? 20.24666 20.49610  49.24363 1.000 35.51423  ?  131  THR   A OG1 1 
ATOM   691  C CG2 . THR   A 1 131 ? 17.88724 20.15148  49.62800 1.000 41.56933  ?  131  THR   A CG2 1 
ATOM   692  N N   . PRO   A 1 132 ? 21.31272 17.73525  50.31012 1.000 43.63534  ?  132  PRO   A N   1 
ATOM   693  C CA  . PRO   A 1 132 ? 21.94800 17.45303  51.60687 1.000 48.41848  ?  132  PRO   A CA  1 
ATOM   694  C C   . PRO   A 1 132 ? 21.91462 18.63068  52.56362 1.000 52.41489  ?  132  PRO   A C   1 
ATOM   695  O O   . PRO   A 1 132 ? 22.17110 18.44091  53.75974 1.000 51.77219  ?  132  PRO   A O   1 
ATOM   696  C CB  . PRO   A 1 132 ? 23.39234 17.08787  51.22902 1.000 48.38288  ?  132  PRO   A CB  1 
ATOM   697  C CG  . PRO   A 1 132 ? 23.40893 16.94421  49.73431 1.000 43.08764  ?  132  PRO   A CG  1 
ATOM   698  C CD  . PRO   A 1 132 ? 22.28397 17.76699  49.20710 1.000 44.51603  ?  132  PRO   A CD  1 
ATOM   699  N N   . GLN   A 1 133 ? 21.60399 19.82876  52.08080 1.000 45.19992  ?  133  GLN   A N   1 
ATOM   700  C CA  . GLN   A 1 133 ? 21.56212 21.02003  52.91180 1.000 47.84736  ?  133  GLN   A CA  1 
ATOM   701  C C   . GLN   A 1 133 ? 20.18789 21.16981  53.55432 1.000 50.73022  ?  133  GLN   A C   1 
ATOM   702  O O   . GLN   A 1 133 ? 19.16938 20.74932  52.99825 1.000 48.69242  ?  133  GLN   A O   1 
ATOM   703  C CB  . GLN   A 1 133 ? 21.90855 22.25730  52.08434 1.000 45.64998  ?  133  GLN   A CB  1 
ATOM   704  C CG  . GLN   A 1 133 ? 23.31588 22.22077  51.49535 1.000 44.15306  ?  133  GLN   A CG  1 
ATOM   705  C CD  . GLN   A 1 133 ? 23.39393 21.45800  50.18396 1.000 42.56727  ?  133  GLN   A CD  1 
ATOM   706  O OE1 . GLN   A 1 133 ? 22.50141 21.55320  49.34165 1.000 40.88977  ?  133  GLN   A OE1 1 
ATOM   707  N NE2 . GLN   A 1 133 ? 24.46977 20.69987  50.00395 1.000 40.35343  ?  133  GLN   A NE2 1 
ATOM   708  N N   . LYS   A 1 134 ? 20.17049 21.78318  54.73731 1.000 62.21072  ?  134  LYS   A N   1 
ATOM   709  C CA  . LYS   A 1 134 ? 18.99321 21.77712  55.59740 1.000 60.74135  ?  134  LYS   A CA  1 
ATOM   710  C C   . LYS   A 1 134 ? 18.12286 23.01992  55.46924 1.000 56.60106  ?  134  LYS   A C   1 
ATOM   711  O O   . LYS   A 1 134 ? 16.90047 22.91709  55.61509 1.000 54.52301  ?  134  LYS   A O   1 
ATOM   712  C CB  . LYS   A 1 134 ? 19.41566 21.61235  57.06230 1.000 58.39562  ?  134  LYS   A CB  1 
ATOM   713  C CG  . LYS   A 1 134 ? 20.04958 20.26358  57.37591 1.000 62.52205  ?  134  LYS   A CG  1 
ATOM   714  C CD  . LYS   A 1 134 ? 21.56917 20.33558  57.32852 1.000 63.39012  ?  134  LYS   A CD  1 
ATOM   715  C CE  . LYS   A 1 134 ? 22.19764 18.97277  57.57555 1.000 64.14306  ?  134  LYS   A CE  1 
ATOM   716  N NZ  . LYS   A 1 134 ? 21.95063 18.03034  56.44827 1.000 62.77765  ?  134  LYS   A NZ  1 
ATOM   717  N N   . THR   A 1 135 ? 18.70558 24.18705  55.21312 1.000 53.45779  ?  135  THR   A N   1 
ATOM   718  C CA  . THR   A 1 135 ? 17.94826 25.42742  55.12657 1.000 53.50358  ?  135  THR   A CA  1 
ATOM   719  C C   . THR   A 1 135 ? 18.15686 26.08351  53.76719 1.000 50.27385  ?  135  THR   A C   1 
ATOM   720  O O   . THR   A 1 135 ? 18.97125 25.64431  52.95114 1.000 54.00273  ?  135  THR   A O   1 
ATOM   721  C CB  . THR   A 1 135 ? 18.34254 26.40304  56.24443 1.000 54.72541  ?  135  THR   A CB  1 
ATOM   722  O OG1 . THR   A 1 135 ? 19.69263 26.84066  56.04728 1.000 54.81337  ?  135  THR   A OG1 1 
ATOM   723  C CG2 . THR   A 1 135 ? 18.21834 25.73826  57.60990 1.000 52.03334  ?  135  THR   A CG2 1 
ATOM   724  N N   . LEU   A 1 136 ? 17.39691 27.15678  53.53578 1.000 49.71155  ?  136  LEU   A N   1 
ATOM   725  C CA  . LEU   A 1 136 ? 17.50486 27.89053  52.27891 1.000 47.67857  ?  136  LEU   A CA  1 
ATOM   726  C C   . LEU   A 1 136 ? 18.84556 28.60639  52.16868 1.000 50.63765  ?  136  LEU   A C   1 
ATOM   727  O O   . LEU   A 1 136 ? 19.41504 28.70446  51.07532 1.000 47.99694  ?  136  LEU   A O   1 
ATOM   728  C CB  . LEU   A 1 136 ? 16.34951 28.88582  52.15731 1.000 45.89703  ?  136  LEU   A CB  1 
ATOM   729  C CG  . LEU   A 1 136 ? 16.42176 29.93810  51.04790 1.000 44.47093  ?  136  LEU   A CG  1 
ATOM   730  C CD1 . LEU   A 1 136 ? 16.24320 29.29922  49.67965 1.000 45.16803  ?  136  LEU   A CD1 1 
ATOM   731  C CD2 . LEU   A 1 136 ? 15.38307 31.02662  51.27471 1.000 47.41754  ?  136  LEU   A CD2 1 
ATOM   732  N N   . GLU   A 1 137 ? 19.36725 29.10846  53.29053 1.000 48.52250  ?  137  GLU   A N   1 
ATOM   733  C CA  . GLU   A 1 137 ? 20.63774 29.82628  53.26024 1.000 50.95083  ?  137  GLU   A CA  1 
ATOM   734  C C   . GLU   A 1 137 ? 21.79372 28.89775  52.90823 1.000 51.28595  ?  137  GLU   A C   1 
ATOM   735  O O   . GLU   A 1 137 ? 22.68130 29.26992  52.13198 1.000 52.72334  ?  137  GLU   A O   1 
ATOM   736  C CB  . GLU   A 1 137 ? 20.88675 30.50704  54.60604 1.000 56.36898  ?  137  GLU   A CB  1 
ATOM   737  C CG  . GLU   A 1 137 ? 20.22547 31.86865  54.74616 1.000 54.09272  ?  137  GLU   A CG  1 
ATOM   738  C CD  . GLU   A 1 137 ? 18.77272 31.77282  55.17124 1.000 59.29489  ?  137  GLU   A CD  1 
ATOM   739  O OE1 . GLU   A 1 137 ? 18.28986 30.64376  55.39971 1.000 59.49465  ?  137  GLU   A OE1 1 
ATOM   740  O OE2 . GLU   A 1 137 ? 18.11310 32.82828  55.27736 1.000 69.49729  -1 137  GLU   A OE2 1 
ATOM   741  N N   . GLU   A 1 138 ? 21.80359 27.68816  53.46795 1.000 55.39632  ?  138  GLU   A N   1 
ATOM   742  C CA  . GLU   A 1 138 ? 22.85963 26.72778  53.17688 1.000 49.54226  ?  138  GLU   A CA  1 
ATOM   743  C C   . GLU   A 1 138 ? 22.63338 25.97200  51.87488 1.000 47.97564  ?  138  GLU   A C   1 
ATOM   744  O O   . GLU   A 1 138 ? 23.54618 25.27193  51.42563 1.000 47.46686  ?  138  GLU   A O   1 
ATOM   745  C CB  . GLU   A 1 138 ? 22.99534 25.72800  54.32876 1.000 51.68455  ?  138  GLU   A CB  1 
ATOM   746  C CG  . GLU   A 1 138 ? 22.89344 26.35131  55.71086 1.000 56.43330  ?  138  GLU   A CG  1 
ATOM   747  C CD  . GLU   A 1 138 ? 22.42206 25.36457  56.76194 1.000 68.38867  ?  138  GLU   A CD  1 
ATOM   748  O OE1 . GLU   A 1 138 ? 23.27174 24.64604  57.32888 1.000 71.28155  ?  138  GLU   A OE1 1 
ATOM   749  O OE2 . GLU   A 1 138 ? 21.20169 25.30678  57.02101 1.000 71.58359  -1 138  GLU   A OE2 1 
ATOM   750  N N   . PHE   A 1 139 ? 21.45618 26.11187  51.26415 1.000 46.09659  ?  139  PHE   A N   1 
ATOM   751  C CA  . PHE   A 1 139 ? 21.09326 25.35181  50.07224 1.000 44.29769  ?  139  PHE   A CA  1 
ATOM   752  C C   . PHE   A 1 139 ? 22.15632 25.47027  48.98683 1.000 43.21028  ?  139  PHE   A C   1 
ATOM   753  O O   . PHE   A 1 139 ? 22.60434 26.57079  48.65278 1.000 47.23444  ?  139  PHE   A O   1 
ATOM   754  C CB  . PHE   A 1 139 ? 19.74328 25.84522  49.54791 1.000 44.15568  ?  139  PHE   A CB  1 
ATOM   755  C CG  . PHE   A 1 139 ? 19.28741 25.15952  48.29419 1.000 42.60789  ?  139  PHE   A CG  1 
ATOM   756  C CD1 . PHE   A 1 139 ? 18.78330 25.89653  47.23561 1.000 42.52079  ?  139  PHE   A CD1 1 
ATOM   757  C CD2 . PHE   A 1 139 ? 19.34935 23.78115  48.17645 1.000 39.79135  ?  139  PHE   A CD2 1 
ATOM   758  C CE1 . PHE   A 1 139 ? 18.35777 25.27463  46.08079 1.000 40.15527  ?  139  PHE   A CE1 1 
ATOM   759  C CE2 . PHE   A 1 139 ? 18.92499 23.15363  47.02232 1.000 38.56263  ?  139  PHE   A CE2 1 
ATOM   760  C CZ  . PHE   A 1 139 ? 18.42780 23.90322  45.97485 1.000 40.38012  ?  139  PHE   A CZ  1 
ATOM   761  N N   . GLN   A 1 140 ? 22.55645 24.32309  48.43614 1.000 38.23149  ?  140  GLN   A N   1 
ATOM   762  C CA  . GLN   A 1 140 ? 23.62290 24.29004  47.44353 1.000 37.80300  ?  140  GLN   A CA  1 
ATOM   763  C C   . GLN   A 1 140 ? 23.24068 23.46610  46.21894 1.000 38.21283  ?  140  GLN   A C   1 
ATOM   764  O O   . GLN   A 1 140 ? 23.06402 24.01718  45.12855 1.000 36.70602  ?  140  GLN   A O   1 
ATOM   765  C CB  . GLN   A 1 140 ? 24.90893 23.73747  48.06253 1.000 38.73660  ?  140  GLN   A CB  1 
ATOM   766  C CG  . GLN   A 1 140 ? 25.73505 24.77110  48.81114 1.000 47.26450  ?  140  GLN   A CG  1 
ATOM   767  C CD  . GLN   A 1 140 ? 26.88177 25.31281  47.98016 1.000 54.11331  ?  140  GLN   A CD  1 
ATOM   768  O OE1 . GLN   A 1 140 ? 27.05428 26.52530  47.85459 1.000 54.04775  ?  140  GLN   A OE1 1 
ATOM   769  N NE2 . GLN   A 1 140 ? 27.67317 24.41340  47.40610 1.000 54.36755  ?  140  GLN   A NE2 1 
ATOM   770  N N   . ASP   A 1 141 ? 23.10761 22.15131  46.38145 1.000 37.40918  ?  141  ASP   A N   1 
ATOM   771  C CA  . ASP   A 1 141 ? 22.98151 21.24062  45.25320 1.000 34.57897  ?  141  ASP   A CA  1 
ATOM   772  C C   . ASP   A 1 141 ? 21.64450 20.51179  45.27741 1.000 33.86888  ?  141  ASP   A C   1 
ATOM   773  O O   . ASP   A 1 141 ? 21.02552 20.34459  46.33209 1.000 35.81610  ?  141  ASP   A O   1 
ATOM   774  C CB  . ASP   A 1 141 ? 24.12495 20.22124  45.25017 1.000 34.62670  ?  141  ASP   A CB  1 
ATOM   775  C CG  . ASP   A 1 141 ? 25.46269 20.85104  45.58479 1.000 35.59476  ?  141  ASP   A CG  1 
ATOM   776  O OD1 . ASP   A 1 141 ? 25.78950 21.90005  44.99280 1.000 33.82046  ?  141  ASP   A OD1 1 
ATOM   777  O OD2 . ASP   A 1 141 ? 26.18350 20.30274  46.44564 1.000 36.82608  -1 141  ASP   A OD2 1 
ATOM   778  N N   . VAL   A 1 142 ? 21.20897 20.08081  44.09503 1.000 31.81180  ?  142  VAL   A N   1 
ATOM   779  C CA  . VAL   A 1 142 ? 19.98392 19.31056  43.91812 1.000 30.63196  ?  142  VAL   A CA  1 
ATOM   780  C C   . VAL   A 1 142 ? 20.35388 17.97913  43.28348 1.000 33.66800  ?  142  VAL   A C   1 
ATOM   781  O O   . VAL   A 1 142 ? 21.10005 17.94314  42.29827 1.000 31.95224  ?  142  VAL   A O   1 
ATOM   782  C CB  . VAL   A 1 142 ? 18.95903 20.05976  43.04615 1.000 30.95896  ?  142  VAL   A CB  1 
ATOM   783  C CG1 . VAL   A 1 142 ? 17.77266 19.16251  42.72213 1.000 29.86271  ?  142  VAL   A CG1 1 
ATOM   784  C CG2 . VAL   A 1 142 ? 18.49834 21.32668  43.73626 1.000 34.30567  ?  142  VAL   A CG2 1 
ATOM   785  N N   . TYR   A 1 143 ? 19.83571 16.89163  43.84407 1.000 31.17056  ?  143  TYR   A N   1 
ATOM   786  C CA  . TYR   A 1 143 ? 20.06813 15.55236  43.32327 1.000 30.31512  ?  143  TYR   A CA  1 
ATOM   787  C C   . TYR   A 1 143 ? 18.76372 14.99090  42.77684 1.000 30.75663  ?  143  TYR   A C   1 
ATOM   788  O O   . TYR   A 1 143 ? 17.75233 14.95700  43.48573 1.000 35.12462  ?  143  TYR   A O   1 
ATOM   789  C CB  . TYR   A 1 143 ? 20.62948 14.62961  44.40579 1.000 28.67940  ?  143  TYR   A CB  1 
ATOM   790  C CG  . TYR   A 1 143 ? 22.01942 14.99593  44.87568 1.000 28.95891  ?  143  TYR   A CG  1 
ATOM   791  C CD1 . TYR   A 1 143 ? 22.21519 16.01186  45.80226 1.000 30.81216  ?  143  TYR   A CD1 1 
ATOM   792  C CD2 . TYR   A 1 143 ? 23.13524 14.32066  44.39947 1.000 30.04850  ?  143  TYR   A CD2 1 
ATOM   793  C CE1 . TYR   A 1 143 ? 23.48273 16.34860  46.23573 1.000 30.26838  ?  143  TYR   A CE1 1 
ATOM   794  C CE2 . TYR   A 1 143 ? 24.40784 14.65008  44.82923 1.000 34.05937  ?  143  TYR   A CE2 1 
ATOM   795  C CZ  . TYR   A 1 143 ? 24.57477 15.66546  45.74762 1.000 33.25560  ?  143  TYR   A CZ  1 
ATOM   796  O OH  . TYR   A 1 143 ? 25.83819 15.99880  46.18039 1.000 35.93643  ?  143  TYR   A OH  1 
ATOM   797  N N   . LEU   A 1 144 ? 18.78867 14.55883  41.51976 1.000 30.02570  ?  144  LEU   A N   1 
ATOM   798  C CA  . LEU   A 1 144 ? 17.63532 13.95572  40.86770 1.000 30.19087  ?  144  LEU   A CA  1 
ATOM   799  C C   . LEU   A 1 144 ? 17.88066 12.46367  40.70506 1.000 32.88955  ?  144  LEU   A C   1 
ATOM   800  O O   . LEU   A 1 144 ? 18.93692 12.05460  40.21115 1.000 32.30719  ?  144  LEU   A O   1 
ATOM   801  C CB  . LEU   A 1 144 ? 17.36891 14.60077  39.50617 1.000 31.20654  ?  144  LEU   A CB  1 
ATOM   802  C CG  . LEU   A 1 144 ? 17.29096 16.12700  39.46209 1.000 30.78003  ?  144  LEU   A CG  1 
ATOM   803  C CD1 . LEU   A 1 144 ? 17.32355 16.61801  38.02255 1.000 32.47185  ?  144  LEU   A CD1 1 
ATOM   804  C CD2 . LEU   A 1 144 ? 16.04258 16.62383  40.17324 1.000 32.45254  ?  144  LEU   A CD2 1 
ATOM   805  N N   . VAL   A 1 145 ? 16.90806 11.65750  41.12055 1.000 33.48286  ?  145  VAL   A N   1 
ATOM   806  C CA  . VAL   A 1 145 ? 17.00354 10.20409  41.06718 1.000 32.58451  ?  145  VAL   A CA  1 
ATOM   807  C C   . VAL   A 1 145 ? 15.98632 9.69253   40.05946 1.000 36.54879  ?  145  VAL   A C   1 
ATOM   808  O O   . VAL   A 1 145 ? 14.80329 10.04758  40.12591 1.000 40.54295  ?  145  VAL   A O   1 
ATOM   809  C CB  . VAL   A 1 145 ? 16.77185 9.57158   42.45019 1.000 37.27110  ?  145  VAL   A CB  1 
ATOM   810  C CG1 . VAL   A 1 145 ? 16.85651 8.05280   42.36229 1.000 34.43868  ?  145  VAL   A CG1 1 
ATOM   811  C CG2 . VAL   A 1 145 ? 17.77841 10.11013  43.45180 1.000 33.72885  ?  145  VAL   A CG2 1 
ATOM   812  N N   . MET   A 1 146 ? 16.44634 8.86381   39.12662 1.000 35.00840  ?  146  MET   A N   1 
ATOM   813  C CA  . MET   A 1 146 ? 15.57005 8.23495   38.15346 1.000 38.83793  ?  146  MET   A CA  1 
ATOM   814  C C   . MET   A 1 146 ? 15.97859 6.77981   37.97133 1.000 39.77833  ?  146  MET   A C   1 
ATOM   815  O O   . MET   A 1 146 ? 17.05534 6.34971   38.39446 1.000 36.94063  ?  146  MET   A O   1 
ATOM   816  C CB  . MET   A 1 146 ? 15.58211 8.98357   36.81238 1.000 42.03254  ?  146  MET   A CB  1 
ATOM   817  C CG  . MET   A 1 146 ? 16.52606 8.40338   35.77199 1.000 44.12865  ?  146  MET   A CG  1 
ATOM   818  S SD  . MET   A 1 146 ? 16.09588 8.90426   34.09593 1.000 46.89709  ?  146  MET   A SD  1 
ATOM   819  C CE  . MET   A 1 146 ? 15.00595 7.55651   33.64583 1.000 46.02231  ?  146  MET   A CE  1 
ATOM   820  N N   . GLU   A 1 147 ? 15.08466 6.02085   37.34331 1.000 45.00721  ?  147  GLU   A N   1 
ATOM   821  C CA  . GLU   A 1 147 ? 15.32906 4.61206   37.06915 1.000 43.86139  ?  147  GLU   A CA  1 
ATOM   822  C C   . GLU   A 1 147 ? 16.53750 4.45198   36.15467 1.000 42.58609  ?  147  GLU   A C   1 
ATOM   823  O O   . GLU   A 1 147 ? 16.65152 5.13023   35.12935 1.000 45.61603  ?  147  GLU   A O   1 
ATOM   824  C CB  . GLU   A 1 147 ? 14.08572 3.98043   36.43214 1.000 44.32027  ?  147  GLU   A CB  1 
ATOM   825  C CG  . GLU   A 1 147 ? 13.34980 4.85288   35.39859 1.000 55.10174  ?  147  GLU   A CG  1 
ATOM   826  C CD  . GLU   A 1 147 ? 12.51590 5.98400   36.00411 1.000 59.38369  ?  147  GLU   A CD  1 
ATOM   827  O OE1 . GLU   A 1 147 ? 12.87162 6.49564   37.08687 1.000 58.47792  ?  147  GLU   A OE1 1 
ATOM   828  O OE2 . GLU   A 1 147 ? 11.50254 6.36883   35.38519 1.000 65.03575  -1 147  GLU   A OE2 1 
ATOM   829  N N   . LEU   A 1 148 ? 17.44172 3.55267   36.53178 1.000 38.90746  ?  148  LEU   A N   1 
ATOM   830  C CA  . LEU   A 1 148 ? 18.68663 3.39122   35.79485 1.000 38.10041  ?  148  LEU   A CA  1 
ATOM   831  C C   . LEU   A 1 148 ? 18.44177 2.72789   34.44511 1.000 36.75698  ?  148  LEU   A C   1 
ATOM   832  O O   . LEU   A 1 148 ? 17.69857 1.74862   34.33813 1.000 38.25453  ?  148  LEU   A O   1 
ATOM   833  C CB  . LEU   A 1 148 ? 19.68365 2.56594   36.60703 1.000 36.78489  ?  148  LEU   A CB  1 
ATOM   834  C CG  . LEU   A 1 148 ? 21.03492 2.32582   35.93027 1.000 38.13269  ?  148  LEU   A CG  1 
ATOM   835  C CD1 . LEU   A 1 148 ? 21.79862 3.63304   35.79353 1.000 38.97338  ?  148  LEU   A CD1 1 
ATOM   836  C CD2 . LEU   A 1 148 ? 21.85769 1.29525   36.68735 1.000 38.31445  ?  148  LEU   A CD2 1 
ATOM   837  N N   . MET   A 1 149 ? 19.07673 3.26959   33.41054 1.000 36.51784  ?  149  MET   A N   1 
ATOM   838  C CA  . MET   A 1 149 ? 19.03252 2.71541   32.06884 1.000 36.87772  ?  149  MET   A CA  1 
ATOM   839  C C   . MET   A 1 149 ? 20.36659 2.04013   31.75668 1.000 38.72440  ?  149  MET   A C   1 
ATOM   840  O O   . MET   A 1 149 ? 21.24753 1.92540   32.61693 1.000 42.20975  ?  149  MET   A O   1 
ATOM   841  C CB  . MET   A 1 149 ? 18.68949 3.80932   31.05759 1.000 34.94181  ?  149  MET   A CB  1 
ATOM   842  C CG  . MET   A 1 149 ? 17.40853 4.55852   31.37610 1.000 32.04753  ?  149  MET   A CG  1 
ATOM   843  S SD  . MET   A 1 149 ? 15.94624 3.52399   31.19095 1.000 35.69097  ?  149  MET   A SD  1 
ATOM   844  C CE  . MET   A 1 149 ? 15.29061 4.14768   29.64572 1.000 37.43138  ?  149  MET   A CE  1 
ATOM   845  N N   . ASP   A 1 150 ? 20.52220 1.59606   30.51087 1.000 40.23517  ?  150  ASP   A N   1 
ATOM   846  C CA  . ASP   A 1 150 ? 21.68075 0.80283   30.12425 1.000 38.09251  ?  150  ASP   A CA  1 
ATOM   847  C C   . ASP   A 1 150 ? 22.67195 1.53281   29.23190 1.000 40.98552  ?  150  ASP   A C   1 
ATOM   848  O O   . ASP   A 1 150 ? 23.86640 1.23580   29.29888 1.000 40.56310  ?  150  ASP   A O   1 
ATOM   849  C CB  . ASP   A 1 150 ? 21.22973 -0.48085  29.41740 1.000 42.35190  ?  150  ASP   A CB  1 
ATOM   850  C CG  . ASP   A 1 150 ? 20.47596 -1.41608  30.34001 1.000 40.81585  ?  150  ASP   A CG  1 
ATOM   851  O OD1 . ASP   A 1 150 ? 20.98060 -1.69056  31.44847 1.000 38.23120  ?  150  ASP   A OD1 1 
ATOM   852  O OD2 . ASP   A 1 150 ? 19.37858 -1.87418  29.95961 1.000 41.93412  -1 150  ASP   A OD2 1 
ATOM   853  N N   . ALA   A 1 151 ? 22.22192 2.47312   28.40379 1.000 42.08725  ?  151  ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 151 ? 23.12742 3.15218   27.48616 1.000 40.92834  ?  151  ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 151 ? 22.48326 4.43945   26.99093 1.000 40.42028  ?  151  ALA   A C   1 
ATOM   856  O O   . ALA   A 1 151 ? 21.28148 4.66477   27.15188 1.000 44.38505  ?  151  ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 151 ? 23.50655 2.24950   26.30682 1.000 46.09041  ?  151  ALA   A CB  1 
ATOM   858  N N   . ASN   A 1 152 ? 23.31220 5.28419   26.38694 1.000 41.11699  ?  152  ASN   A N   1 
ATOM   859  C CA  . ASN   A 1 152 ? 22.87329 6.48841   25.70081 1.000 38.50631  ?  152  ASN   A CA  1 
ATOM   860  C C   . ASN   A 1 152 ? 22.52777 6.16021   24.25193 1.000 39.60851  ?  152  ASN   A C   1 
ATOM   861  O O   . ASN   A 1 152 ? 22.96091 5.14611   23.69997 1.000 37.97670  ?  152  ASN   A O   1 
ATOM   862  C CB  . ASN   A 1 152 ? 23.96586 7.55923   25.75193 1.000 39.09282  ?  152  ASN   A CB  1 
ATOM   863  C CG  . ASN   A 1 152 ? 23.41231 8.96483   25.76670 1.000 44.45290  ?  152  ASN   A CG  1 
ATOM   864  O OD1 . ASN   A 1 152 ? 22.20072 9.16920   25.78828 1.000 49.37895  ?  152  ASN   A OD1 1 
ATOM   865  N ND2 . ASN   A 1 152 ? 24.30454 9.94813   25.75742 1.000 44.67796  ?  152  ASN   A ND2 1 
ATOM   866  N N   . LEU   A 1 153 ? 21.73396 7.03693   23.63315 1.000 36.66193  ?  153  LEU   A N   1 
ATOM   867  C CA  . LEU   A 1 153 ? 21.39318 6.83930   22.22943 1.000 33.91982  ?  153  LEU   A CA  1 
ATOM   868  C C   . LEU   A 1 153 ? 22.59480 7.03761   21.31509 1.000 33.01842  ?  153  LEU   A C   1 
ATOM   869  O O   . LEU   A 1 153 ? 22.59276 6.52547   20.19038 1.000 32.80283  ?  153  LEU   A O   1 
ATOM   870  C CB  . LEU   A 1 153 ? 20.25867 7.77811   21.81809 1.000 31.16038  ?  153  LEU   A CB  1 
ATOM   871  C CG  . LEU   A 1 153 ? 19.44982 7.34327   20.59363 1.000 29.23195  ?  153  LEU   A CG  1 
ATOM   872  C CD1 . LEU   A 1 153 ? 18.73676 6.02667   20.86083 1.000 26.76962  ?  153  LEU   A CD1 1 
ATOM   873  C CD2 . LEU   A 1 153 ? 18.45587 8.42155   20.19271 1.000 29.30086  ?  153  LEU   A CD2 1 
ATOM   874  N N   . CYS   A 1 154 ? 23.61795 7.76556   21.77079 1.000 34.34908  ?  154  CYS   A N   1 
ATOM   875  C CA  . CYS   A 1 154 ? 24.84431 7.88349   20.98919 1.000 31.62457  ?  154  CYS   A CA  1 
ATOM   876  C C   . CYS   A 1 154 ? 25.54216 6.53563   20.86045 1.000 35.72878  ?  154  CYS   A C   1 
ATOM   877  O O   . CYS   A 1 154 ? 26.10428 6.21704   19.80651 1.000 35.04666  ?  154  CYS   A O   1 
ATOM   878  C CB  . CYS   A 1 154 ? 25.77984 8.91148   21.62599 1.000 32.70556  ?  154  CYS   A CB  1 
ATOM   879  S SG  . CYS   A 1 154 ? 25.00832 10.49918  22.01237 1.000 35.66532  ?  154  CYS   A SG  1 
ATOM   880  N N   . GLN   A 1 155 ? 25.51667 5.72876   21.92510 1.000 35.65970  ?  155  GLN   A N   1 
ATOM   881  C CA  . GLN   A 1 155 ? 26.11807 4.40058   21.86108 1.000 35.60513  ?  155  GLN   A CA  1 
ATOM   882  C C   . GLN   A 1 155 ? 25.31816 3.46356   20.96663 1.000 35.42379  ?  155  GLN   A C   1 
ATOM   883  O O   . GLN   A 1 155 ? 25.88491 2.53481   20.38009 1.000 38.40001  ?  155  GLN   A O   1 
ATOM   884  C CB  . GLN   A 1 155 ? 26.24377 3.80103   23.26228 1.000 34.23568  ?  155  GLN   A CB  1 
ATOM   885  C CG  . GLN   A 1 155 ? 26.91810 4.69845   24.28547 1.000 38.36540  ?  155  GLN   A CG  1 
ATOM   886  C CD  . GLN   A 1 155 ? 26.48167 4.38834   25.70544 1.000 47.38577  ?  155  GLN   A CD  1 
ATOM   887  O OE1 . GLN   A 1 155 ? 25.80699 5.18719   26.34949 1.000 42.19477  ?  155  GLN   A OE1 1 
ATOM   888  N NE2 . GLN   A 1 155 ? 26.86183 3.21515   26.19689 1.000 47.29201  ?  155  GLN   A NE2 1 
ATOM   889  N N   . VAL   A 1 156 ? 24.00858 3.68380   20.85468 1.000 37.05338  ?  156  VAL   A N   1 
ATOM   890  C CA  . VAL   A 1 156 ? 23.17478 2.82398   20.02173 1.000 35.64210  ?  156  VAL   A CA  1 
ATOM   891  C C   . VAL   A 1 156 ? 23.32270 3.19007   18.54958 1.000 35.80923  ?  156  VAL   A C   1 
ATOM   892  O O   . VAL   A 1 156 ? 23.30028 2.31592   17.67498 1.000 37.76832  ?  156  VAL   A O   1 
ATOM   893  C CB  . VAL   A 1 156 ? 21.71074 2.90523   20.49232 1.000 35.55106  ?  156  VAL   A CB  1 
ATOM   894  C CG1 . VAL   A 1 156 ? 20.78440 2.20948   19.51011 1.000 39.13900  ?  156  VAL   A CG1 1 
ATOM   895  C CG2 . VAL   A 1 156 ? 21.57422 2.29481   21.87470 1.000 39.42526  ?  156  VAL   A CG2 1 
ATOM   896  N N   . ILE   A 1 157 ? 23.48794 4.48145   18.25396 1.000 35.11553  ?  157  ILE   A N   1 
ATOM   897  C CA  . ILE   A 1 157 ? 23.66707 4.91752   16.87121 1.000 33.55511  ?  157  ILE   A CA  1 
ATOM   898  C C   . ILE   A 1 157 ? 24.93885 4.31761   16.28365 1.000 35.49170  ?  157  ILE   A C   1 
ATOM   899  O O   . ILE   A 1 157 ? 24.98779 3.96197   15.09901 1.000 34.04212  ?  157  ILE   A O   1 
ATOM   900  C CB  . ILE   A 1 157 ? 23.66959 6.45661   16.80018 1.000 33.09140  ?  157  ILE   A CB  1 
ATOM   901  C CG1 . ILE   A 1 157 ? 22.24294 6.99113   16.92593 1.000 31.99281  ?  157  ILE   A CG1 1 
ATOM   902  C CG2 . ILE   A 1 157 ? 24.31094 6.94889   15.51103 1.000 35.49722  ?  157  ILE   A CG2 1 
ATOM   903  C CD1 . ILE   A 1 157 ? 22.17099 8.40810   17.42913 1.000 32.02611  ?  157  ILE   A CD1 1 
ATOM   904  N N   . GLN   A 1 158 ? 25.97999 4.17215   17.10733 1.000 35.79456  ?  158  GLN   A N   1 
ATOM   905  C CA  . GLN   A 1 158 ? 27.22468 3.56955   16.64475 1.000 38.08569  ?  158  GLN   A CA  1 
ATOM   906  C C   . GLN   A 1 158 ? 27.05833 2.10413   16.26439 1.000 38.95475  ?  158  GLN   A C   1 
ATOM   907  O O   . GLN   A 1 158 ? 27.92854 1.55214   15.58274 1.000 40.29066  ?  158  GLN   A O   1 
ATOM   908  C CB  . GLN   A 1 158 ? 28.30425 3.69891   17.71984 1.000 38.09401  ?  158  GLN   A CB  1 
ATOM   909  C CG  . GLN   A 1 158 ? 28.77180 5.12089   17.97180 1.000 39.25577  ?  158  GLN   A CG  1 
ATOM   910  C CD  . GLN   A 1 158 ? 29.88067 5.19088   19.00382 1.000 45.88113  ?  158  GLN   A CD  1 
ATOM   911  O OE1 . GLN   A 1 158 ? 29.67042 4.89201   20.17995 1.000 47.04523  ?  158  GLN   A OE1 1 
ATOM   912  N NE2 . GLN   A 1 158 ? 31.07148 5.58426   18.56689 1.000 60.67810  ?  158  GLN   A NE2 1 
ATOM   913  N N   . MET   A 1 159 ? 25.97303 1.46553   16.68633 1.000 38.30544  ?  159  MET   A N   1 
ATOM   914  C CA  . MET   A 1 159 ? 25.74843 0.05792   16.40269 1.000 39.37360  ?  159  MET   A CA  1 
ATOM   915  C C   . MET   A 1 159 ? 24.92512 -0.11475  15.13080 1.000 41.02008  ?  159  MET   A C   1 
ATOM   916  O O   . MET   A 1 159 ? 24.26690 0.81166   14.65134 1.000 37.33213  ?  159  MET   A O   1 
ATOM   917  C CB  . MET   A 1 159 ? 25.03755 -0.62023  17.57370 1.000 41.03451  ?  159  MET   A CB  1 
ATOM   918  C CG  . MET   A 1 159 ? 25.79774 -0.56641  18.88660 1.000 41.55666  ?  159  MET   A CG  1 
ATOM   919  S SD  . MET   A 1 159 ? 24.67915 -0.60539  20.29692 1.000 58.77100  ?  159  MET   A SD  1 
ATOM   920  C CE  . MET   A 1 159 ? 23.44685 -1.75147  19.69104 1.000 50.67282  ?  159  MET   A CE  1 
ATOM   921  N N   . GLU   A 1 160 ? 24.97240 -1.32637  14.58631 1.000 40.19680  ?  160  GLU   A N   1 
ATOM   922  C CA  . GLU   A 1 160 ? 24.15783 -1.70642  13.44092 1.000 40.32424  ?  160  GLU   A CA  1 
ATOM   923  C C   . GLU   A 1 160 ? 22.90282 -2.40112  13.95182 1.000 42.32028  ?  160  GLU   A C   1 
ATOM   924  O O   . GLU   A 1 160 ? 22.99106 -3.41891  14.64730 1.000 40.32262  ?  160  GLU   A O   1 
ATOM   925  C CB  . GLU   A 1 160 ? 24.93569 -2.61583  12.49148 1.000 44.08922  ?  160  GLU   A CB  1 
ATOM   926  C CG  . GLU   A 1 160 ? 25.30973 -1.95167  11.17910 1.000 50.59088  ?  160  GLU   A CG  1 
ATOM   927  C CD  . GLU   A 1 160 ? 26.48375 -2.62539  10.50227 1.000 56.37243  ?  160  GLU   A CD  1 
ATOM   928  O OE1 . GLU   A 1 160 ? 26.80559 -3.77340  10.87515 1.000 56.95884  ?  160  GLU   A OE1 1 
ATOM   929  O OE2 . GLU   A 1 160 ? 27.08251 -2.01034  9.59484  1.000 63.78134  -1 160  GLU   A OE2 1 
ATOM   930  N N   . LEU   A 1 161 ? 21.74222 -1.84919  13.61342 1.000 43.69829  ?  161  LEU   A N   1 
ATOM   931  C CA  . LEU   A 1 161 ? 20.46926 -2.34670  14.10676 1.000 44.06813  ?  161  LEU   A CA  1 
ATOM   932  C C   . LEU   A 1 161 ? 19.62131 -2.86806  12.95538 1.000 46.37073  ?  161  LEU   A C   1 
ATOM   933  O O   . LEU   A 1 161 ? 19.70173 -2.37560  11.82578 1.000 44.41795  ?  161  LEU   A O   1 
ATOM   934  C CB  . LEU   A 1 161 ? 19.69897 -1.25388  14.85430 1.000 44.34218  ?  161  LEU   A CB  1 
ATOM   935  C CG  . LEU   A 1 161 ? 20.30987 -0.67394  16.12894 1.000 41.60221  ?  161  LEU   A CG  1 
ATOM   936  C CD1 . LEU   A 1 161 ? 19.29684 0.21510   16.82758 1.000 42.10954  ?  161  LEU   A CD1 1 
ATOM   937  C CD2 . LEU   A 1 161 ? 20.78072 -1.78277  17.05310 1.000 43.89332  ?  161  LEU   A CD2 1 
ATOM   938  N N   . ASP   A 1 162 ? 18.80479 -3.87278  13.25885 1.000 45.70532  ?  162  ASP   A N   1 
ATOM   939  C CA  . ASP   A 1 162 ? 17.84770 -4.39656  12.29959 1.000 46.77543  ?  162  ASP   A CA  1 
ATOM   940  C C   . ASP   A 1 162 ? 16.66878 -3.43414  12.16438 1.000 46.89941  ?  162  ASP   A C   1 
ATOM   941  O O   . ASP   A 1 162 ? 16.59520 -2.39553  12.82579 1.000 45.32680  ?  162  ASP   A O   1 
ATOM   942  C CB  . ASP   A 1 162 ? 17.37522 -5.78017  12.73393 1.000 46.66834  ?  162  ASP   A CB  1 
ATOM   943  C CG  . ASP   A 1 162 ? 17.14091 -5.86661  14.22802 1.000 47.53498  ?  162  ASP   A CG  1 
ATOM   944  O OD1 . ASP   A 1 162 ? 15.96549 -5.84680  14.64798 1.000 46.79438  ?  162  ASP   A OD1 1 
ATOM   945  O OD2 . ASP   A 1 162 ? 18.13189 -5.94655  14.98381 1.000 51.81784  -1 162  ASP   A OD2 1 
ATOM   946  N N   . HIS   A 1 163 ? 15.72105 -3.79194  11.29650 1.000 47.20163  ?  163  HIS   A N   1 
ATOM   947  C CA  . HIS   A 1 163 ? 14.55583 -2.93674  11.10097 1.000 46.35937  ?  163  HIS   A CA  1 
ATOM   948  C C   . HIS   A 1 163 ? 13.59259 -3.01593  12.27795 1.000 45.47899  ?  163  HIS   A C   1 
ATOM   949  O O   . HIS   A 1 163 ? 12.83445 -2.07022  12.51843 1.000 45.13810  ?  163  HIS   A O   1 
ATOM   950  C CB  . HIS   A 1 163 ? 13.84452 -3.30696  9.80112  1.000 45.06832  ?  163  HIS   A CB  1 
ATOM   951  C CG  . HIS   A 1 163 ? 14.52454 -2.78303  8.57557  1.000 48.27229  ?  163  HIS   A CG  1 
ATOM   952  N ND1 . HIS   A 1 163 ? 14.71740 -1.43687  8.35040  1.000 44.53718  ?  163  HIS   A ND1 1 
ATOM   953  C CD2 . HIS   A 1 163 ? 15.06281 -3.42366  7.51115  1.000 49.76077  ?  163  HIS   A CD2 1 
ATOM   954  C CE1 . HIS   A 1 163 ? 15.34284 -1.27061  7.19884  1.000 48.88372  ?  163  HIS   A CE1 1 
ATOM   955  N NE2 . HIS   A 1 163 ? 15.56307 -2.46041  6.66899  1.000 51.65532  ?  163  HIS   A NE2 1 
ATOM   956  N N   . GLU   A 1 164 ? 13.60845 -4.12379  13.02137 1.000 45.24870  ?  164  GLU   A N   1 
ATOM   957  C CA  . GLU   A 1 164 ? 12.72137 -4.25659  14.17280 1.000 45.90826  ?  164  GLU   A CA  1 
ATOM   958  C C   . GLU   A 1 164 ? 13.09124 -3.26474  15.26917 1.000 44.85163  ?  164  GLU   A C   1 
ATOM   959  O O   . GLU   A 1 164 ? 12.22677 -2.55562  15.79713 1.000 43.40385  ?  164  GLU   A O   1 
ATOM   960  C CB  . GLU   A 1 164 ? 12.76662 -5.68906  14.70745 1.000 47.21288  ?  164  GLU   A CB  1 
ATOM   961  C CG  . GLU   A 1 164 ? 11.64023 -6.58091  14.21295 1.000 49.57647  ?  164  GLU   A CG  1 
ATOM   962  C CD  . GLU   A 1 164 ? 10.39947 -6.48650  15.07870 1.000 53.36985  ?  164  GLU   A CD  1 
ATOM   963  O OE1 . GLU   A 1 164 ? 10.53014 -6.56673  16.31840 1.000 58.49604  ?  164  GLU   A OE1 1 
ATOM   964  O OE2 . GLU   A 1 164 ? 9.29299  -6.33403  14.51935 1.000 52.05866  -1 164  GLU   A OE2 1 
ATOM   965  N N   . ARG   A 1 165 ? 14.37670 -3.19584  15.62044 1.000 45.37422  ?  165  ARG   A N   1 
ATOM   966  C CA  . ARG   A 1 165 ? 14.79930 -2.34139  16.72453 1.000 47.57061  ?  165  ARG   A CA  1 
ATOM   967  C C   . ARG   A 1 165 ? 14.84576 -0.87175  16.32061 1.000 44.60421  ?  165  ARG   A C   1 
ATOM   968  O O   . ARG   A 1 165 ? 14.52172 0.00294   17.13112 1.000 42.34734  ?  165  ARG   A O   1 
ATOM   969  C CB  . ARG   A 1 165 ? 16.15805 -2.80286  17.25203 1.000 48.59447  ?  165  ARG   A CB  1 
ATOM   970  C CG  . ARG   A 1 165 ? 16.08092 -4.06122  18.10482 1.000 51.85296  ?  165  ARG   A CG  1 
ATOM   971  C CD  . ARG   A 1 165 ? 17.45859 -4.55498  18.51390 1.000 59.30158  ?  165  ARG   A CD  1 
ATOM   972  N NE  . ARG   A 1 165 ? 17.40905 -5.91505  19.03739 1.000 63.45767  ?  165  ARG   A NE  1 
ATOM   973  C CZ  . ARG   A 1 165 ? 18.29544 -6.86020  18.75511 1.000 65.21627  ?  165  ARG   A CZ  1 
ATOM   974  N NH1 . ARG   A 1 165 ? 19.32614 -6.62616  17.95907 1.000 66.21890  ?  165  ARG   A NH1 1 
ATOM   975  N NH2 . ARG   A 1 165 ? 18.14368 -8.07108  19.28424 1.000 67.18192  ?  165  ARG   A NH2 1 
ATOM   976  N N   . MET   A 1 166 ? 15.24556 -0.57703  15.08078 1.000 48.56626  ?  166  MET   A N   1 
ATOM   977  C CA  . MET   A 1 166 ? 15.22328 0.80600   14.61128 1.000 45.48940  ?  166  MET   A CA  1 
ATOM   978  C C   . MET   A 1 166 ? 13.80361 1.35679   14.60948 1.000 42.24721  ?  166  MET   A C   1 
ATOM   979  O O   . MET   A 1 166 ? 13.55709 2.47350   15.07819 1.000 43.09160  ?  166  MET   A O   1 
ATOM   980  C CB  . MET   A 1 166 ? 15.84001 0.90632   13.21493 1.000 45.35140  ?  166  MET   A CB  1 
ATOM   981  C CG  . MET   A 1 166 ? 17.32973 0.62757   13.17050 1.000 49.98157  ?  166  MET   A CG  1 
ATOM   982  S SD  . MET   A 1 166 ? 18.14627 1.23473   11.68097 1.000 66.65372  ?  166  MET   A SD  1 
ATOM   983  C CE  . MET   A 1 166 ? 17.24253 2.75150   11.38707 1.000 49.84072  ?  166  MET   A CE  1 
ATOM   984  N N   . SER   A 1 167 ? 12.85166 0.57884   14.08978 1.000 42.21056  ?  167  SER   A N   1 
ATOM   985  C CA  . SER   A 1 167 ? 11.46300 1.02442   14.07086 1.000 44.61136  ?  167  SER   A CA  1 
ATOM   986  C C   . SER   A 1 167 ? 10.88946 1.14701   15.47616 1.000 40.11477  ?  167  SER   A C   1 
ATOM   987  O O   . SER   A 1 167 ? 10.05825 2.02639   15.72781 1.000 40.33017  ?  167  SER   A O   1 
ATOM   988  C CB  . SER   A 1 167 ? 10.61351 0.06626   13.23600 1.000 41.60969  ?  167  SER   A CB  1 
ATOM   989  O OG  . SER   A 1 167 ? 10.00531 -0.91711  14.05476 1.000 39.99731  ?  167  SER   A OG  1 
ATOM   990  N N   . TYR   A 1 168 ? 11.31594 0.28328   16.40083 1.000 42.80943  ?  168  TYR   A N   1 
ATOM   991  C CA  . TYR   A 1 168 ? 10.78933 0.34591   17.76045 1.000 42.52522  ?  168  TYR   A CA  1 
ATOM   992  C C   . TYR   A 1 168 ? 11.30553 1.57441   18.49877 1.000 39.95857  ?  168  TYR   A C   1 
ATOM   993  O O   . TYR   A 1 168 ? 10.53988 2.25457   19.19178 1.000 40.07402  ?  168  TYR   A O   1 
ATOM   994  C CB  . TYR   A 1 168 ? 11.14518 -0.92729  18.52611 1.000 41.54000  ?  168  TYR   A CB  1 
ATOM   995  C CG  . TYR   A 1 168 ? 10.48403 -1.01650  19.88245 1.000 40.69222  ?  168  TYR   A CG  1 
ATOM   996  C CD1 . TYR   A 1 168 ? 11.16666 -1.52556  20.97886 1.000 41.01896  ?  168  TYR   A CD1 1 
ATOM   997  C CD2 . TYR   A 1 168 ? 9.17652  -0.58661  20.06683 1.000 42.90765  ?  168  TYR   A CD2 1 
ATOM   998  C CE1 . TYR   A 1 168 ? 10.56434 -1.60686  22.22139 1.000 41.01792  ?  168  TYR   A CE1 1 
ATOM   999  C CE2 . TYR   A 1 168 ? 8.56654  -0.66283  21.30441 1.000 48.02902  ?  168  TYR   A CE2 1 
ATOM   1000 C CZ  . TYR   A 1 168 ? 9.26440  -1.17331  22.37780 1.000 41.51363  ?  168  TYR   A CZ  1 
ATOM   1001 O OH  . TYR   A 1 168 ? 8.65847  -1.25058  23.61072 1.000 41.65897  ?  168  TYR   A OH  1 
ATOM   1002 N N   . LEU   A 1 169 ? 12.60125 1.87043   18.37008 1.000 40.45804  ?  169  LEU   A N   1 
ATOM   1003 C CA  . LEU   A 1 169 ? 13.14703 3.06882   18.99826 1.000 39.72425  ?  169  LEU   A CA  1 
ATOM   1004 C C   . LEU   A 1 169 ? 12.49976 4.32585   18.43195 1.000 39.36321  ?  169  LEU   A C   1 
ATOM   1005 O O   . LEU   A 1 169 ? 12.17228 5.25554   19.17853 1.000 40.11999  ?  169  LEU   A O   1 
ATOM   1006 C CB  . LEU   A 1 169 ? 14.66423 3.11564   18.81592 1.000 39.59769  ?  169  LEU   A CB  1 
ATOM   1007 C CG  . LEU   A 1 169 ? 15.47584 2.02662   19.52087 1.000 39.76435  ?  169  LEU   A CG  1 
ATOM   1008 C CD1 . LEU   A 1 169 ? 16.92727 2.06278   19.06897 1.000 39.68859  ?  169  LEU   A CD1 1 
ATOM   1009 C CD2 . LEU   A 1 169 ? 15.37926 2.17120   21.03128 1.000 39.90632  ?  169  LEU   A CD2 1 
ATOM   1010 N N   . LEU   A 1 170 ? 12.29847 4.36837   17.11237 1.000 38.82380  ?  170  LEU   A N   1 
ATOM   1011 C CA  . LEU   A 1 170 ? 11.63350 5.51446   16.50260 1.000 39.32822  ?  170  LEU   A CA  1 
ATOM   1012 C C   . LEU   A 1 170 ? 10.16765 5.59464   16.90798 1.000 40.47326  ?  170  LEU   A C   1 
ATOM   1013 O O   . LEU   A 1 170 ? 9.59787  6.69075   16.95097 1.000 41.06264  ?  170  LEU   A O   1 
ATOM   1014 C CB  . LEU   A 1 170 ? 11.76235 5.44776   14.98139 1.000 39.75861  ?  170  LEU   A CB  1 
ATOM   1015 C CG  . LEU   A 1 170 ? 13.17325 5.63153   14.42025 1.000 38.80743  ?  170  LEU   A CG  1 
ATOM   1016 C CD1 . LEU   A 1 170 ? 13.28120 5.01752   13.03495 1.000 39.72323  ?  170  LEU   A CD1 1 
ATOM   1017 C CD2 . LEU   A 1 170 ? 13.55264 7.10271   14.39059 1.000 34.48789  ?  170  LEU   A CD2 1 
ATOM   1018 N N   . TYR   A 1 171 ? 9.54212  4.45358   17.20627 1.000 40.42099  ?  171  TYR   A N   1 
ATOM   1019 C CA  . TYR   A 1 171 ? 8.15822  4.47359   17.66835 1.000 43.17392  ?  171  TYR   A CA  1 
ATOM   1020 C C   . TYR   A 1 171 ? 8.05732  5.03943   19.07882 1.000 44.83132  ?  171  TYR   A C   1 
ATOM   1021 O O   . TYR   A 1 171 ? 7.11426  5.77503   19.39340 1.000 43.35156  ?  171  TYR   A O   1 
ATOM   1022 C CB  . TYR   A 1 171 ? 7.56322  3.06673   17.61213 1.000 43.85025  ?  171  TYR   A CB  1 
ATOM   1023 C CG  . TYR   A 1 171 ? 6.26036  2.92162   18.36805 1.000 47.64856  ?  171  TYR   A CG  1 
ATOM   1024 C CD1 . TYR   A 1 171 ? 5.07369  3.42060   17.84684 1.000 50.15622  ?  171  TYR   A CD1 1 
ATOM   1025 C CD2 . TYR   A 1 171 ? 6.21692  2.28453   19.60189 1.000 50.02566  ?  171  TYR   A CD2 1 
ATOM   1026 C CE1 . TYR   A 1 171 ? 3.88047  3.29044   18.53305 1.000 56.51360  ?  171  TYR   A CE1 1 
ATOM   1027 C CE2 . TYR   A 1 171 ? 5.02848  2.15009   20.29565 1.000 56.58241  ?  171  TYR   A CE2 1 
ATOM   1028 C CZ  . TYR   A 1 171 ? 3.86393  2.65469   19.75642 1.000 61.87664  ?  171  TYR   A CZ  1 
ATOM   1029 O OH  . TYR   A 1 171 ? 2.67856  2.52297   20.44313 1.000 85.06663  ?  171  TYR   A OH  1 
ATOM   1030 N N   . GLN   A 1 172 ? 9.01980  4.70658   19.94222 1.000 43.37093  ?  172  GLN   A N   1 
ATOM   1031 C CA  . GLN   A 1 172 ? 8.98535  5.20137   21.31370 1.000 42.22932  ?  172  GLN   A CA  1 
ATOM   1032 C C   . GLN   A 1 172 ? 9.29928  6.68981   21.38438 1.000 41.56376  ?  172  GLN   A C   1 
ATOM   1033 O O   . GLN   A 1 172 ? 8.78466  7.38752   22.26562 1.000 48.58370  ?  172  GLN   A O   1 
ATOM   1034 C CB  . GLN   A 1 172 ? 9.96169  4.40918   22.18270 1.000 39.20701  ?  172  GLN   A CB  1 
ATOM   1035 C CG  . GLN   A 1 172 ? 9.63533  2.92923   22.28694 1.000 38.26574  ?  172  GLN   A CG  1 
ATOM   1036 C CD  . GLN   A 1 172 ? 10.57474 2.18943   23.21741 1.000 38.73366  ?  172  GLN   A CD  1 
ATOM   1037 O OE1 . GLN   A 1 172 ? 10.44450 2.26666   24.43895 1.000 36.13317  ?  172  GLN   A OE1 1 
ATOM   1038 N NE2 . GLN   A 1 172 ? 11.52862 1.46565   22.64311 1.000 41.47285  ?  172  GLN   A NE2 1 
ATOM   1039 N N   . MET   A 1 173 ? 10.13752 7.19292   20.47500 1.000 40.96550  ?  173  MET   A N   1 
ATOM   1040 C CA  . MET   A 1 173 ? 10.43183 8.62210   20.45960 1.000 39.66552  ?  173  MET   A CA  1 
ATOM   1041 C C   . MET   A 1 173 ? 9.19583  9.43511   20.09894 1.000 43.71775  ?  173  MET   A C   1 
ATOM   1042 O O   . MET   A 1 173 ? 8.93248  10.47775  20.70844 1.000 44.08504  ?  173  MET   A O   1 
ATOM   1043 C CB  . MET   A 1 173 ? 11.57063 8.91867   19.48395 1.000 37.93272  ?  173  MET   A CB  1 
ATOM   1044 C CG  . MET   A 1 173 ? 12.90621 8.31401   19.87917 1.000 37.48315  ?  173  MET   A CG  1 
ATOM   1045 S SD  . MET   A 1 173 ? 14.14059 8.42905   18.57066 1.000 39.89651  ?  173  MET   A SD  1 
ATOM   1046 C CE  . MET   A 1 173 ? 13.82378 10.07768  17.95257 1.000 31.15729  ?  173  MET   A CE  1 
ATOM   1047 N N   . LEU   A 1 174 ? 8.42276  8.97150   19.11479 1.000 43.95988  ?  174  LEU   A N   1 
ATOM   1048 C CA  . LEU   A 1 174 ? 7.22652  9.70089   18.71024 1.000 45.27012  ?  174  LEU   A CA  1 
ATOM   1049 C C   . LEU   A 1 174 ? 6.11993  9.59237   19.75101 1.000 47.54164  ?  174  LEU   A C   1 
ATOM   1050 O O   . LEU   A 1 174 ? 5.26383  10.47987  19.83619 1.000 50.19150  ?  174  LEU   A O   1 
ATOM   1051 C CB  . LEU   A 1 174 ? 6.73747  9.19164   17.35509 1.000 47.58849  ?  174  LEU   A CB  1 
ATOM   1052 C CG  . LEU   A 1 174 ? 7.71858  9.37404   16.19594 1.000 46.97681  ?  174  LEU   A CG  1 
ATOM   1053 C CD1 . LEU   A 1 174 ? 7.36441  8.45630   15.03660 1.000 47.28597  ?  174  LEU   A CD1 1 
ATOM   1054 C CD2 . LEU   A 1 174 ? 7.74945  10.82715  15.74755 1.000 45.30877  ?  174  LEU   A CD2 1 
ATOM   1055 N N   . CYS   A 1 175 ? 6.11729  8.52103   20.54649 1.000 47.21919  ?  175  CYS   A N   1 
ATOM   1056 C CA  . CYS   A 1 175 ? 5.11275  8.38237   21.59578 1.000 51.19599  ?  175  CYS   A CA  1 
ATOM   1057 C C   . CYS   A 1 175 ? 5.33791  9.40512   22.70319 1.000 51.83947  ?  175  CYS   A C   1 
ATOM   1058 O O   . CYS   A 1 175 ? 4.40208  10.09169  23.12901 1.000 53.68247  ?  175  CYS   A O   1 
ATOM   1059 C CB  . CYS   A 1 175 ? 5.13416  6.96093   22.15881 1.000 54.98704  ?  175  CYS   A CB  1 
ATOM   1060 S SG  . CYS   A 1 175 ? 4.03677  5.80281   21.30667 1.000 67.12144  ?  175  CYS   A SG  1 
ATOM   1061 N N   . GLY   A 1 176 ? 6.57815  9.52132   23.18316 1.000 49.21599  ?  176  GLY   A N   1 
ATOM   1062 C CA  . GLY   A 1 176 ? 6.88100  10.52110  24.19216 1.000 51.34866  ?  176  GLY   A CA  1 
ATOM   1063 C C   . GLY   A 1 176 ? 6.77650  11.93962  23.67608 1.000 52.38743  ?  176  GLY   A C   1 
ATOM   1064 O O   . GLY   A 1 176 ? 6.38465  12.84469  24.42010 1.000 61.04895  ?  176  GLY   A O   1 
ATOM   1065 N N   . ILE   A 1 177 ? 7.12086  12.15462  22.40351 1.000 47.80812  ?  177  ILE   A N   1 
ATOM   1066 C CA  . ILE   A 1 177 ? 7.00608  13.48606  21.81368 1.000 47.68552  ?  177  ILE   A CA  1 
ATOM   1067 C C   . ILE   A 1 177 ? 5.55000  13.93259  21.78339 1.000 50.65116  ?  177  ILE   A C   1 
ATOM   1068 O O   . ILE   A 1 177 ? 5.22600  15.07515  22.13394 1.000 51.28073  ?  177  ILE   A O   1 
ATOM   1069 C CB  . ILE   A 1 177 ? 7.63165  13.50186  20.40631 1.000 46.44511  ?  177  ILE   A CB  1 
ATOM   1070 C CG1 . ILE   A 1 177 ? 9.14667  13.68409  20.49210 1.000 43.56446  ?  177  ILE   A CG1 1 
ATOM   1071 C CG2 . ILE   A 1 177 ? 7.01932  14.59960  19.54993 1.000 45.30762  ?  177  ILE   A CG2 1 
ATOM   1072 C CD1 . ILE   A 1 177 ? 9.82553  13.71310  19.14070 1.000 40.64147  ?  177  ILE   A CD1 1 
ATOM   1073 N N   . LYS   A 1 178 ? 4.64747  13.03694  21.37574 1.000 51.82739  ?  178  LYS   A N   1 
ATOM   1074 C CA  . LYS   A 1 178 ? 3.23591  13.39700  21.30966 1.000 55.56276  ?  178  LYS   A CA  1 
ATOM   1075 C C   . LYS   A 1 178 ? 2.64903  13.62860  22.69626 1.000 55.80621  ?  178  LYS   A C   1 
ATOM   1076 O O   . LYS   A 1 178 ? 1.71019  14.41935  22.84308 1.000 58.52645  ?  178  LYS   A O   1 
ATOM   1077 C CB  . LYS   A 1 178 ? 2.44845  12.31884  20.56371 1.000 59.26120  ?  178  LYS   A CB  1 
ATOM   1078 C CG  . LYS   A 1 178 ? 1.76959  11.30238  21.46083 1.000 68.25298  ?  178  LYS   A CG  1 
ATOM   1079 C CD  . LYS   A 1 178 ? 0.86107  10.39085  20.66858 1.000 79.12048  ?  178  LYS   A CD  1 
ATOM   1080 C CE  . LYS   A 1 178 ? -0.18320 11.16915  19.89080 1.000 78.98154  ?  178  LYS   A CE  1 
ATOM   1081 N NZ  . LYS   A 1 178 ? -1.34747 10.30721  19.54566 1.000 85.33334  ?  178  LYS   A NZ  1 
ATOM   1082 N N   . HIS   A 1 179 ? 3.18291  12.95905  23.72168 1.000 55.39741  ?  179  HIS   A N   1 
ATOM   1083 C CA  . HIS   A 1 179 ? 2.73196  13.23416  25.08099 1.000 57.19642  ?  179  HIS   A CA  1 
ATOM   1084 C C   . HIS   A 1 179 ? 3.21603  14.59954  25.54591 1.000 54.66458  ?  179  HIS   A C   1 
ATOM   1085 O O   . HIS   A 1 179 ? 2.50471  15.30297  26.27275 1.000 56.64965  ?  179  HIS   A O   1 
ATOM   1086 C CB  . HIS   A 1 179 ? 3.21136  12.14214  26.03464 1.000 58.86191  ?  179  HIS   A CB  1 
ATOM   1087 C CG  . HIS   A 1 179 ? 2.80267  12.36642  27.45697 1.000 63.37987  ?  179  HIS   A CG  1 
ATOM   1088 N ND1 . HIS   A 1 179 ? 1.48410  12.46665  27.84460 1.000 75.02970  ?  179  HIS   A ND1 1 
ATOM   1089 C CD2 . HIS   A 1 179 ? 3.53810  12.51889  28.58339 1.000 65.05078  ?  179  HIS   A CD2 1 
ATOM   1090 C CE1 . HIS   A 1 179 ? 1.42430  12.66450  29.14935 1.000 78.52803  ?  179  HIS   A CE1 1 
ATOM   1091 N NE2 . HIS   A 1 179 ? 2.65712  12.70064  29.62177 1.000 70.70042  ?  179  HIS   A NE2 1 
ATOM   1092 N N   . LEU   A 1 180 ? 4.42724  14.98699  25.14072 1.000 52.97247  ?  180  LEU   A N   1 
ATOM   1093 C CA  . LEU   A 1 180 ? 4.89682  16.34284  25.40067 1.000 51.76064  ?  180  LEU   A CA  1 
ATOM   1094 C C   . LEU   A 1 180 ? 3.98204  17.36318  24.73653 1.000 50.52508  ?  180  LEU   A C   1 
ATOM   1095 O O   . LEU   A 1 180 ? 3.59350  18.36245  25.35157 1.000 50.18727  ?  180  LEU   A O   1 
ATOM   1096 C CB  . LEU   A 1 180 ? 6.33601  16.50190  24.90739 1.000 49.52095  ?  180  LEU   A CB  1 
ATOM   1097 C CG  . LEU   A 1 180 ? 7.42626  15.74540  25.67073 1.000 48.02464  ?  180  LEU   A CG  1 
ATOM   1098 C CD1 . LEU   A 1 180 ? 8.78430  16.39353  25.44923 1.000 45.02325  ?  180  LEU   A CD1 1 
ATOM   1099 C CD2 . LEU   A 1 180 ? 7.10166  15.67174  27.15444 1.000 48.16554  ?  180  LEU   A CD2 1 
ATOM   1100 N N   . HIS   A 1 181 ? 3.62056  17.11986  23.47464 1.000 52.57880  ?  181  HIS   A N   1 
ATOM   1101 C CA  . HIS   A 1 181 ? 2.68186  18.00180  22.78968 1.000 50.71048  ?  181  HIS   A CA  1 
ATOM   1102 C C   . HIS   A 1 181 ? 1.30578  17.95122  23.44095 1.000 52.29479  ?  181  HIS   A C   1 
ATOM   1103 O O   . HIS   A 1 181 ? 0.63092  18.98115  23.55917 1.000 51.64884  ?  181  HIS   A O   1 
ATOM   1104 C CB  . HIS   A 1 181 ? 2.58809  17.62462  21.31087 1.000 49.65148  ?  181  HIS   A CB  1 
ATOM   1105 C CG  . HIS   A 1 181 ? 3.88813  17.72442  20.57509 1.000 47.95332  ?  181  HIS   A CG  1 
ATOM   1106 N ND1 . HIS   A 1 181 ? 4.03893  17.29769  19.27339 1.000 47.07126  ?  181  HIS   A ND1 1 
ATOM   1107 C CD2 . HIS   A 1 181 ? 5.09643  18.20211  20.95654 1.000 45.80089  ?  181  HIS   A CD2 1 
ATOM   1108 C CE1 . HIS   A 1 181 ? 5.28355  17.50832  18.88443 1.000 45.41664  ?  181  HIS   A CE1 1 
ATOM   1109 N NE2 . HIS   A 1 181 ? 5.94652  18.05506  19.88746 1.000 44.37290  ?  181  HIS   A NE2 1 
ATOM   1110 N N   . SER   A 1 182 ? 0.87507  16.76097  23.87139 1.000 53.24934  ?  182  SER   A N   1 
ATOM   1111 C CA  . SER   A 1 182 ? -0.41500 16.63544  24.54199 1.000 60.14945  ?  182  SER   A CA  1 
ATOM   1112 C C   . SER   A 1 182 ? -0.44990 17.42731  25.84190 1.000 58.72228  ?  182  SER   A C   1 
ATOM   1113 O O   . SER   A 1 182 ? -1.52356 17.85811  26.27833 1.000 64.52133  ?  182  SER   A O   1 
ATOM   1114 C CB  . SER   A 1 182 ? -0.72723 15.16272  24.80852 1.000 65.61487  ?  182  SER   A CB  1 
ATOM   1115 O OG  . SER   A 1 182 ? -1.89045 15.02133  25.60604 1.000 82.08628  ?  182  SER   A OG  1 
ATOM   1116 N N   . ALA   A 1 183 ? 0.70553  17.62849  26.47191 1.000 56.74107  ?  183  ALA   A N   1 
ATOM   1117 C CA  . ALA   A 1 183 ? 0.81253  18.43368  27.67888 1.000 56.48727  ?  183  ALA   A CA  1 
ATOM   1118 C C   . ALA   A 1 183 ? 1.21972  19.87112  27.38586 1.000 52.44704  ?  183  ALA   A C   1 
ATOM   1119 O O   . ALA   A 1 183 ? 1.52873  20.61961  28.31821 1.000 49.24687  ?  183  ALA   A O   1 
ATOM   1120 C CB  . ALA   A 1 183 ? 1.80572  17.79646  28.65182 1.000 57.72145  ?  183  ALA   A CB  1 
ATOM   1121 N N   . GLY   A 1 184 ? 1.22882  20.27124  26.11703 1.000 52.09263  ?  184  GLY   A N   1 
ATOM   1122 C CA  . GLY   A 1 184 ? 1.61132  21.62443  25.76317 1.000 49.42161  ?  184  GLY   A CA  1 
ATOM   1123 C C   . GLY   A 1 184 ? 3.09134  21.90688  25.87851 1.000 46.82740  ?  184  GLY   A C   1 
ATOM   1124 O O   . GLY   A 1 184 ? 3.47594  23.03276  26.20834 1.000 46.73476  ?  184  GLY   A O   1 
ATOM   1125 N N   . ILE   A 1 185 ? 3.93614  20.91394  25.61488 1.000 45.76795  ?  185  ILE   A N   1 
ATOM   1126 C CA  . ILE   A 1 185 ? 5.38450  21.05548  25.71213 1.000 44.40282  ?  185  ILE   A CA  1 
ATOM   1127 C C   . ILE   A 1 185 ? 5.98527  20.69958  24.36053 1.000 43.28299  ?  185  ILE   A C   1 
ATOM   1128 O O   . ILE   A 1 185 ? 5.76329  19.59635  23.84631 1.000 44.91478  ?  185  ILE   A O   1 
ATOM   1129 C CB  . ILE   A 1 185 ? 5.97421  20.17050  26.82184 1.000 46.01800  ?  185  ILE   A CB  1 
ATOM   1130 C CG1 . ILE   A 1 185 ? 5.73972  20.80483  28.19351 1.000 46.71270  ?  185  ILE   A CG1 1 
ATOM   1131 C CG2 . ILE   A 1 185 ? 7.46115  19.94062  26.59160 1.000 44.04961  ?  185  ILE   A CG2 1 
ATOM   1132 C CD1 . ILE   A 1 185 ? 5.75355  19.80885  29.33083 1.000 48.42208  ?  185  ILE   A CD1 1 
ATOM   1133 N N   . ILE   A 1 186 ? 6.74110  21.63033  23.78690 1.000 41.77226  ?  186  ILE   A N   1 
ATOM   1134 C CA  . ILE   A 1 186 ? 7.46043  21.41409  22.53812 1.000 40.05124  ?  186  ILE   A CA  1 
ATOM   1135 C C   . ILE   A 1 186 ? 8.95086  21.45780  22.84488 1.000 41.09551  ?  186  ILE   A C   1 
ATOM   1136 O O   . ILE   A 1 186 ? 9.42139  22.36612  23.54095 1.000 38.91646  ?  186  ILE   A O   1 
ATOM   1137 C CB  . ILE   A 1 186 ? 7.07052  22.45600  21.47609 1.000 42.14184  ?  186  ILE   A CB  1 
ATOM   1138 C CG1 . ILE   A 1 186 ? 5.56975  22.37533  21.18517 1.000 41.95789  ?  186  ILE   A CG1 1 
ATOM   1139 C CG2 . ILE   A 1 186 ? 7.86016  22.23749  20.20415 1.000 41.23183  ?  186  ILE   A CG2 1 
ATOM   1140 C CD1 . ILE   A 1 186 ? 5.09458  23.35609  20.13484 1.000 45.95000  ?  186  ILE   A CD1 1 
ATOM   1141 N N   . HIS   A 1 187 ? 9.69098  20.47467  22.32986 1.000 37.42931  ?  187  HIS   A N   1 
ATOM   1142 C CA  . HIS   A 1 187 ? 11.08452 20.28625  22.73702 1.000 39.56245  ?  187  HIS   A CA  1 
ATOM   1143 C C   . HIS   A 1 187 ? 12.02514 21.23793  22.00117 1.000 36.08007  ?  187  HIS   A C   1 
ATOM   1144 O O   . HIS   A 1 187 ? 12.61041 22.14003  22.60769 1.000 38.87934  ?  187  HIS   A O   1 
ATOM   1145 C CB  . HIS   A 1 187 ? 11.49444 18.82688  22.51449 1.000 36.09484  ?  187  HIS   A CB  1 
ATOM   1146 C CG  . HIS   A 1 187 ? 12.64511 18.38658  23.36382 1.000 34.82637  ?  187  HIS   A CG  1 
ATOM   1147 N ND1 . HIS   A 1 187 ? 13.93743 18.81259  23.14560 1.000 34.53161  ?  187  HIS   A ND1 1 
ATOM   1148 C CD2 . HIS   A 1 187 ? 12.69709 17.56113  24.43575 1.000 36.33737  ?  187  HIS   A CD2 1 
ATOM   1149 C CE1 . HIS   A 1 187 ? 14.73683 18.26456  24.04329 1.000 35.19488  ?  187  HIS   A CE1 1 
ATOM   1150 N NE2 . HIS   A 1 187 ? 14.00897 17.50156  24.83858 1.000 38.55768  ?  187  HIS   A NE2 1 
ATOM   1151 N N   . ARG   A 1 188 ? 12.19611 21.02738  20.69478 1.000 35.07686  ?  188  ARG   A N   1 
ATOM   1152 C CA  . ARG   A 1 188 ? 13.03273 21.80329  19.77883 1.000 31.69582  ?  188  ARG   A CA  1 
ATOM   1153 C C   . ARG   A 1 188 ? 14.52633 21.55621  19.95973 1.000 30.29231  ?  188  ARG   A C   1 
ATOM   1154 O O   . ARG   A 1 188 ? 15.32375 22.13732  19.21439 1.000 35.09583  ?  188  ARG   A O   1 
ATOM   1155 C CB  . ARG   A 1 188 ? 12.78195 23.31560  19.87984 1.000 39.10518  ?  188  ARG   A CB  1 
ATOM   1156 C CG  . ARG   A 1 188 ? 11.33393 23.72618  19.70475 1.000 41.90857  ?  188  ARG   A CG  1 
ATOM   1157 C CD  . ARG   A 1 188 ? 11.04138 24.99758  20.47971 1.000 44.20703  ?  188  ARG   A CD  1 
ATOM   1158 N NE  . ARG   A 1 188 ? 12.14379 25.94818  20.39726 1.000 47.33074  ?  188  ARG   A NE  1 
ATOM   1159 C CZ  . ARG   A 1 188 ? 12.17820 27.11413  21.02803 1.000 49.79938  ?  188  ARG   A CZ  1 
ATOM   1160 N NH1 . ARG   A 1 188 ? 11.18201 27.51060  21.80298 1.000 52.75499  ?  188  ARG   A NH1 1 
ATOM   1161 N NH2 . ARG   A 1 188 ? 13.23803 27.90323  20.87574 1.000 48.84206  ?  188  ARG   A NH2 1 
ATOM   1162 N N   . ASP   A 1 189 ? 14.93896 20.72111  20.91133 1.000 30.85455  ?  189  ASP   A N   1 
ATOM   1163 C CA  . ASP   A 1 189 ? 16.35668 20.43760  21.11580 1.000 31.96499  ?  189  ASP   A CA  1 
ATOM   1164 C C   . ASP   A 1 189 ? 16.57588 18.95508  21.38182 1.000 31.90746  ?  189  ASP   A C   1 
ATOM   1165 O O   . ASP   A 1 189 ? 17.37673 18.57175  22.24093 1.000 31.31897  ?  189  ASP   A O   1 
ATOM   1166 C CB  . ASP   A 1 189 ? 16.93380 21.27863  22.25434 1.000 32.64604  ?  189  ASP   A CB  1 
ATOM   1167 C CG  . ASP   A 1 189 ? 18.39738 21.62033  22.04212 1.000 34.59096  ?  189  ASP   A CG  1 
ATOM   1168 O OD1 . ASP   A 1 189 ? 18.91112 21.37772  20.92958 1.000 34.40746  ?  189  ASP   A OD1 1 
ATOM   1169 O OD2 . ASP   A 1 189 ? 19.03528 22.13166  22.98700 1.000 35.67073  -1 189  ASP   A OD2 1 
ATOM   1170 N N   . LEU   A 1 190 ? 15.86867 18.10079  20.64750 1.000 32.03753  ?  190  LEU   A N   1 
ATOM   1171 C CA  . LEU   A 1 190 ? 16.06964 16.66495  20.77855 1.000 29.21727  ?  190  LEU   A CA  1 
ATOM   1172 C C   . LEU   A 1 190 ? 17.44116 16.27240  20.24537 1.000 27.95008  ?  190  LEU   A C   1 
ATOM   1173 O O   . LEU   A 1 190 ? 17.88994 16.77270  19.21129 1.000 27.49827  ?  190  LEU   A O   1 
ATOM   1174 C CB  . LEU   A 1 190 ? 14.97775 15.90102  20.03165 1.000 28.70577  ?  190  LEU   A CB  1 
ATOM   1175 C CG  . LEU   A 1 190 ? 14.01404 15.06943  20.87989 1.000 31.78814  ?  190  LEU   A CG  1 
ATOM   1176 C CD1 . LEU   A 1 190 ? 13.32117 14.02508  20.02252 1.000 29.97971  ?  190  LEU   A CD1 1 
ATOM   1177 C CD2 . LEU   A 1 190 ? 14.74070 14.41358  22.04367 1.000 30.90590  ?  190  LEU   A CD2 1 
ATOM   1178 N N   . LYS   A 1 191 ? 18.11040 15.37221  20.96266 1.000 29.10753  ?  191  LYS   A N   1 
ATOM   1179 C CA  . LYS   A 1 191 ? 19.44901 14.93244  20.59514 1.000 28.51951  ?  191  LYS   A CA  1 
ATOM   1180 C C   . LYS   A 1 191 ? 19.70651 13.58354  21.24641 1.000 30.09584  ?  191  LYS   A C   1 
ATOM   1181 O O   . LYS   A 1 191 ? 19.09532 13.27337  22.27517 1.000 28.89563  ?  191  LYS   A O   1 
ATOM   1182 C CB  . LYS   A 1 191 ? 20.50776 15.95777  21.02973 1.000 25.80450  ?  191  LYS   A CB  1 
ATOM   1183 C CG  . LYS   A 1 191 ? 20.51474 16.25868  22.51587 1.000 29.76102  ?  191  LYS   A CG  1 
ATOM   1184 C CD  . LYS   A 1 191 ? 21.36856 17.47913  22.82137 1.000 30.91543  ?  191  LYS   A CD  1 
ATOM   1185 C CE  . LYS   A 1 191 ? 20.69807 18.75399  22.33886 1.000 30.09144  ?  191  LYS   A CE  1 
ATOM   1186 N NZ  . LYS   A 1 191 ? 21.39774 19.97015  22.83683 1.000 41.97301  ?  191  LYS   A NZ  1 
ATOM   1187 N N   . PRO   A 1 192 ? 20.59363 12.76145  20.67770 1.000 28.99598  ?  192  PRO   A N   1 
ATOM   1188 C CA  . PRO   A 1 192 ? 20.80288 11.41550  21.23788 1.000 30.32162  ?  192  PRO   A CA  1 
ATOM   1189 C C   . PRO   A 1 192 ? 21.38001 11.41971  22.64198 1.000 28.54000  ?  192  PRO   A C   1 
ATOM   1190 O O   . PRO   A 1 192 ? 21.12836 10.47894  23.40545 1.000 32.42776  ?  192  PRO   A O   1 
ATOM   1191 C CB  . PRO   A 1 192 ? 21.76884 10.76304  20.23649 1.000 27.07730  ?  192  PRO   A CB  1 
ATOM   1192 C CG  . PRO   A 1 192 ? 21.68762 11.60012  19.00205 1.000 26.49572  ?  192  PRO   A CG  1 
ATOM   1193 C CD  . PRO   A 1 192 ? 21.39291 12.98488  19.46253 1.000 26.69832  ?  192  PRO   A CD  1 
ATOM   1194 N N   . SER   A 1 193 ? 22.14856 12.44755  23.00842 1.000 31.55287  ?  193  SER   A N   1 
ATOM   1195 C CA  . SER   A 1 193 ? 22.75108 12.49115  24.33540 1.000 30.21639  ?  193  SER   A CA  1 
ATOM   1196 C C   . SER   A 1 193 ? 21.71366 12.61580  25.44328 1.000 30.70734  ?  193  SER   A C   1 
ATOM   1197 O O   . SER   A 1 193 ? 21.99513 12.23183  26.58327 1.000 32.15289  ?  193  SER   A O   1 
ATOM   1198 C CB  . SER   A 1 193 ? 23.74856 13.64708  24.42241 1.000 29.68048  ?  193  SER   A CB  1 
ATOM   1199 O OG  . SER   A 1 193 ? 23.12762 14.88078  24.10581 1.000 29.00096  ?  193  SER   A OG  1 
ATOM   1200 N N   . ASN   A 1 194 ? 20.52665 13.14024  25.13795 1.000 30.41686  ?  194  ASN   A N   1 
ATOM   1201 C CA  . ASN   A 1 194 ? 19.44773 13.27182  26.10869 1.000 26.10512  ?  194  ASN   A CA  1 
ATOM   1202 C C   . ASN   A 1 194 ? 18.36791 12.21255  25.91391 1.000 30.98125  ?  194  ASN   A C   1 
ATOM   1203 O O   . ASN   A 1 194 ? 17.20398 12.43542  26.26474 1.000 47.43990  ?  194  ASN   A O   1 
ATOM   1204 C CB  . ASN   A 1 194 ? 18.84197 14.67318  26.03867 1.000 32.49436  ?  194  ASN   A CB  1 
ATOM   1205 C CG  . ASN   A 1 194 ? 19.81260 15.74919  26.48628 1.000 31.80881  ?  194  ASN   A CG  1 
ATOM   1206 O OD1 . ASN   A 1 194 ? 20.90152 15.45316  26.98068 1.000 28.60092  ?  194  ASN   A OD1 1 
ATOM   1207 N ND2 . ASN   A 1 194 ? 19.42405 17.00677  26.31129 1.000 41.17850  ?  194  ASN   A ND2 1 
ATOM   1208 N N   . ILE   A 1 195 ? 18.73358 11.06434  25.34897 1.000 28.24338  ?  195  ILE   A N   1 
ATOM   1209 C CA  . ILE   A 1 195 ? 17.82716 9.93903   25.15808 1.000 31.60760  ?  195  ILE   A CA  1 
ATOM   1210 C C   . ILE   A 1 195 ? 18.54434 8.67806   25.61582 1.000 30.72159  ?  195  ILE   A C   1 
ATOM   1211 O O   . ILE   A 1 195 ? 19.65472 8.39061   25.15573 1.000 30.91759  ?  195  ILE   A O   1 
ATOM   1212 C CB  . ILE   A 1 195 ? 17.37828 9.80251   23.69063 1.000 32.13078  ?  195  ILE   A CB  1 
ATOM   1213 C CG1 . ILE   A 1 195 ? 16.52734 11.00318  23.27194 1.000 29.34035  ?  195  ILE   A CG1 1 
ATOM   1214 C CG2 . ILE   A 1 195 ? 16.60809 8.51060   23.48888 1.000 28.61116  ?  195  ILE   A CG2 1 
ATOM   1215 C CD1 . ILE   A 1 195 ? 16.17616 11.01112  21.80057 1.000 27.13572  ?  195  ILE   A CD1 1 
ATOM   1216 N N   . VAL   A 1 196 ? 17.91449 7.92887   26.51626 1.000 29.95374  ?  196  VAL   A N   1 
ATOM   1217 C CA  . VAL   A 1 196 ? 18.51970 6.73848   27.09782 1.000 35.35586  ?  196  VAL   A CA  1 
ATOM   1218 C C   . VAL   A 1 196 ? 17.66265 5.52698   26.76273 1.000 33.52018  ?  196  VAL   A C   1 
ATOM   1219 O O   . VAL   A 1 196 ? 16.44107 5.62683   26.60624 1.000 38.19799  ?  196  VAL   A O   1 
ATOM   1220 C CB  . VAL   A 1 196 ? 18.69657 6.87814   28.62441 1.000 33.62974  ?  196  VAL   A CB  1 
ATOM   1221 C CG1 . VAL   A 1 196 ? 19.91635 7.73057   28.93759 1.000 33.78517  ?  196  VAL   A CG1 1 
ATOM   1222 C CG2 . VAL   A 1 196 ? 17.44689 7.47745   29.24485 1.000 32.54290  ?  196  VAL   A CG2 1 
ATOM   1223 N N   . VAL   A 1 197 ? 18.31953 4.37044   26.64926 1.000 38.03099  ?  197  VAL   A N   1 
ATOM   1224 C CA  . VAL   A 1 197 ? 17.66412 3.12189   26.28746 1.000 35.30556  ?  197  VAL   A CA  1 
ATOM   1225 C C   . VAL   A 1 197 ? 18.10141 2.02381   27.24792 1.000 37.68599  ?  197  VAL   A C   1 
ATOM   1226 O O   . VAL   A 1 197 ? 19.08918 2.15168   27.97453 1.000 38.96171  ?  197  VAL   A O   1 
ATOM   1227 C CB  . VAL   A 1 197 ? 17.96683 2.69751   24.83290 1.000 38.48940  ?  197  VAL   A CB  1 
ATOM   1228 C CG1 . VAL   A 1 197 ? 17.74091 3.85498   23.86838 1.000 34.81269  ?  197  VAL   A CG1 1 
ATOM   1229 C CG2 . VAL   A 1 197 ? 19.38796 2.17309   24.72475 1.000 36.46492  ?  197  VAL   A CG2 1 
ATOM   1230 N N   . LYS   A 1 198 ? 17.34407 0.93240   27.23849 1.000 36.16089  ?  198  LYS   A N   1 
ATOM   1231 C CA  . LYS   A 1 198 ? 17.67284 -0.28162  27.97099 1.000 43.08815  ?  198  LYS   A CA  1 
ATOM   1232 C C   . LYS   A 1 198 ? 17.99850 -1.40127  26.99063 1.000 43.40331  ?  198  LYS   A C   1 
ATOM   1233 O O   . LYS   A 1 198 ? 17.84324 -1.26057  25.77462 1.000 44.39334  ?  198  LYS   A O   1 
ATOM   1234 C CB  . LYS   A 1 198 ? 16.51937 -0.69924  28.89096 1.000 40.57964  ?  198  LYS   A CB  1 
ATOM   1235 C CG  . LYS   A 1 198 ? 16.72873 -0.37978  30.36062 1.000 37.97252  ?  198  LYS   A CG  1 
ATOM   1236 C CD  . LYS   A 1 198 ? 15.52362 -0.80408  31.18581 1.000 37.78515  ?  198  LYS   A CD  1 
ATOM   1237 C CE  . LYS   A 1 198 ? 14.42085 0.24037   31.13165 1.000 39.43178  ?  198  LYS   A CE  1 
ATOM   1238 N NZ  . LYS   A 1 198 ? 13.20094 -0.19087  31.86935 1.000 40.67085  ?  198  LYS   A NZ  1 
ATOM   1239 N N   . SER   A 1 199 ? 18.45218 -2.53133  27.53862 1.000 45.31366  ?  199  SER   A N   1 
ATOM   1240 C CA  . SER   A 1 199 ? 18.80328 -3.66398  26.68866 1.000 51.04714  ?  199  SER   A CA  1 
ATOM   1241 C C   . SER   A 1 199 ? 17.57457 -4.26383  26.01569 1.000 49.83083  ?  199  SER   A C   1 
ATOM   1242 O O   . SER   A 1 199 ? 17.69227 -4.88483  24.95345 1.000 58.72232  ?  199  SER   A O   1 
ATOM   1243 C CB  . SER   A 1 199 ? 19.53341 -4.73015  27.50621 1.000 54.01938  ?  199  SER   A CB  1 
ATOM   1244 O OG  . SER   A 1 199 ? 20.71101 -4.19849  28.09204 1.000 55.02131  ?  199  SER   A OG  1 
ATOM   1245 N N   . ASP   A 1 200 ? 16.39284 -4.08848  26.60900 1.000 45.53410  ?  200  ASP   A N   1 
ATOM   1246 C CA  . ASP   A 1 200 ? 15.14740 -4.58816  26.04310 1.000 43.45012  ?  200  ASP   A CA  1 
ATOM   1247 C C   . ASP   A 1 200 ? 14.52239 -3.61604  25.04521 1.000 42.61123  ?  200  ASP   A C   1 
ATOM   1248 O O   . ASP   A 1 200 ? 13.32618 -3.72841  24.75233 1.000 40.59849  ?  200  ASP   A O   1 
ATOM   1249 C CB  . ASP   A 1 200 ? 14.15418 -4.91314  27.16219 1.000 42.14816  ?  200  ASP   A CB  1 
ATOM   1250 C CG  . ASP   A 1 200 ? 13.61059 -3.67049  27.84667 1.000 43.51493  ?  200  ASP   A CG  1 
ATOM   1251 O OD1 . ASP   A 1 200 ? 14.25184 -2.60257  27.76507 1.000 38.66151  ?  200  ASP   A OD1 1 
ATOM   1252 O OD2 . ASP   A 1 200 ? 12.53358 -3.76528  28.47322 1.000 45.63399  -1 200  ASP   A OD2 1 
ATOM   1253 N N   . CYS   A 1 201 ? 15.30325 -2.66008  24.53826 1.000 44.39991  ?  201  CYS   A N   1 
ATOM   1254 C CA  . CYS   A 1 201 ? 14.91640 -1.68084  23.52415 1.000 42.31739  ?  201  CYS   A CA  1 
ATOM   1255 C C   . CYS   A 1 201 ? 13.93528 -0.63203  24.03355 1.000 40.11750  ?  201  CYS   A C   1 
ATOM   1256 O O   . CYS   A 1 201 ? 13.40719 0.14677   23.22948 1.000 41.35443  ?  201  CYS   A O   1 
ATOM   1257 C CB  . CYS   A 1 201 ? 14.33563 -2.35454  22.27403 1.000 44.14107  ?  201  CYS   A CB  1 
ATOM   1258 S SG  . CYS   A 1 201 ? 14.75014 -1.52792  20.72356 1.000 46.88864  ?  201  CYS   A SG  1 
ATOM   1259 N N   . THR   A 1 202 ? 13.67814 -0.57537  25.33797 1.000 39.15961  ?  202  THR   A N   1 
ATOM   1260 C CA  . THR   A 1 202 ? 12.82050 0.47252   25.87527 1.000 38.83659  ?  202  THR   A CA  1 
ATOM   1261 C C   . THR   A 1 202 ? 13.55662 1.80721   25.86573 1.000 36.76295  ?  202  THR   A C   1 
ATOM   1262 O O   . THR   A 1 202 ? 14.74023 1.88385   26.20451 1.000 37.20745  ?  202  THR   A O   1 
ATOM   1263 C CB  . THR   A 1 202 ? 12.37033 0.12781   27.29493 1.000 40.06349  ?  202  THR   A CB  1 
ATOM   1264 O OG1 . THR   A 1 202 ? 13.49462 -0.31977  28.06095 1.000 40.38768  ?  202  THR   A OG1 1 
ATOM   1265 C CG2 . THR   A 1 202 ? 11.31447 -0.96865  27.26815 1.000 41.59969  ?  202  THR   A CG2 1 
ATOM   1266 N N   . LEU   A 1 203 ? 12.84782 2.86408   25.47552 1.000 36.79031  ?  203  LEU   A N   1 
ATOM   1267 C CA  . LEU   A 1 203 ? 13.44162 4.17632   25.26773 1.000 36.50848  ?  203  LEU   A CA  1 
ATOM   1268 C C   . LEU   A 1 203 ? 12.75143 5.21844   26.13876 1.000 36.17185  ?  203  LEU   A C   1 
ATOM   1269 O O   . LEU   A 1 203 ? 11.54580 5.13831   26.39405 1.000 38.71593  ?  203  LEU   A O   1 
ATOM   1270 C CB  . LEU   A 1 203 ? 13.35039 4.58599   23.79074 1.000 35.30491  ?  203  LEU   A CB  1 
ATOM   1271 C CG  . LEU   A 1 203 ? 13.95380 5.92457   23.36232 1.000 35.19893  ?  203  LEU   A CG  1 
ATOM   1272 C CD1 . LEU   A 1 203 ? 14.65674 5.77596   22.02392 1.000 34.53946  ?  203  LEU   A CD1 1 
ATOM   1273 C CD2 . LEU   A 1 203 ? 12.88553 7.00755   23.29136 1.000 35.60622  ?  203  LEU   A CD2 1 
ATOM   1274 N N   . LYS   A 1 204 ? 13.52778 6.20724   26.58331 1.000 35.71749  ?  204  LYS   A N   1 
ATOM   1275 C CA  . LYS   A 1 204 ? 13.00488 7.29904   27.39314 1.000 38.06484  ?  204  LYS   A CA  1 
ATOM   1276 C C   . LYS   A 1 204 ? 13.75776 8.58307   27.06448 1.000 36.93559  ?  204  LYS   A C   1 
ATOM   1277 O O   . LYS   A 1 204 ? 14.96522 8.55528   26.81134 1.000 28.86208  ?  204  LYS   A O   1 
ATOM   1278 C CB  . LYS   A 1 204 ? 13.11386 6.98124   28.88928 1.000 39.10330  ?  204  LYS   A CB  1 
ATOM   1279 C CG  . LYS   A 1 204 ? 12.08048 5.98573   29.39569 1.000 40.90016  ?  204  LYS   A CG  1 
ATOM   1280 C CD  . LYS   A 1 204 ? 12.17046 5.79314   30.89857 1.000 41.11534  ?  204  LYS   A CD  1 
ATOM   1281 C CE  . LYS   A 1 204 ? 11.39306 4.56291   31.33708 1.000 37.96064  ?  204  LYS   A CE  1 
ATOM   1282 N NZ  . LYS   A 1 204 ? 9.92462  4.81000   31.34482 1.000 43.34324  ?  204  LYS   A NZ  1 
ATOM   1283 N N   . ILE   A 1 205 ? 13.03613 9.70468   27.07578 1.000 36.82868  ?  205  ILE   A N   1 
ATOM   1284 C CA  . ILE   A 1 205 ? 13.58779 11.01755  26.74789 1.000 34.93219  ?  205  ILE   A CA  1 
ATOM   1285 C C   . ILE   A 1 205 ? 13.88841 11.76147  28.04176 1.000 36.14077  ?  205  ILE   A C   1 
ATOM   1286 O O   . ILE   A 1 205 ? 13.02134 11.87422  28.91688 1.000 40.12054  ?  205  ILE   A O   1 
ATOM   1287 C CB  . ILE   A 1 205 ? 12.61919 11.82287  25.86497 1.000 37.20408  ?  205  ILE   A CB  1 
ATOM   1288 C CG1 . ILE   A 1 205 ? 12.40464 11.11696  24.52406 1.000 32.56935  ?  205  ILE   A CG1 1 
ATOM   1289 C CG2 . ILE   A 1 205 ? 13.13753 13.23901  25.65461 1.000 33.67397  ?  205  ILE   A CG2 1 
ATOM   1290 C CD1 . ILE   A 1 205 ? 11.41382 11.81654  23.62053 1.000 32.39137  ?  205  ILE   A CD1 1 
ATOM   1291 N N   . LEU   A 1 206 ? 15.10529 12.30184  28.14920 1.000 35.26778  ?  206  LEU   A N   1 
ATOM   1292 C CA  . LEU   A 1 206 ? 15.58358 12.83178  29.42344 1.000 38.91684  ?  206  LEU   A CA  1 
ATOM   1293 C C   . LEU   A 1 206 ? 15.05409 14.23645  29.70651 1.000 43.23225  ?  206  LEU   A C   1 
ATOM   1294 O O   . LEU   A 1 206 ? 14.44537 14.47267  30.75550 1.000 41.42473  ?  206  LEU   A O   1 
ATOM   1295 C CB  . LEU   A 1 206 ? 17.11389 12.82320  29.45005 1.000 38.12210  ?  206  LEU   A CB  1 
ATOM   1296 C CG  . LEU   A 1 206 ? 17.78805 11.47121  29.70118 1.000 38.43434  ?  206  LEU   A CG  1 
ATOM   1297 C CD1 . LEU   A 1 206 ? 19.29506 11.63482  29.83019 1.000 34.36083  ?  206  LEU   A CD1 1 
ATOM   1298 C CD2 . LEU   A 1 206 ? 17.21406 10.79939  30.93834 1.000 36.60447  ?  206  LEU   A CD2 1 
ATOM   1299 N N   . ASP   A 1 207 ? 15.28279 15.18394  28.79859 1.000 46.50108  ?  207  ASP   A N   1 
ATOM   1300 C CA  . ASP   A 1 207 ? 15.01004 16.59343  29.05844 1.000 48.82953  ?  207  ASP   A CA  1 
ATOM   1301 C C   . ASP   A 1 207 ? 13.75268 17.05152  28.31924 1.000 45.71075  ?  207  ASP   A C   1 
ATOM   1302 O O   . ASP   A 1 207 ? 13.11458 16.28987  27.58635 1.000 41.32794  ?  207  ASP   A O   1 
ATOM   1303 C CB  . ASP   A 1 207 ? 16.22110 17.45179  28.68200 1.000 44.79578  ?  207  ASP   A CB  1 
ATOM   1304 C CG  . ASP   A 1 207 ? 16.23126 17.84154  27.21693 1.000 48.52824  ?  207  ASP   A CG  1 
ATOM   1305 O OD1 . ASP   A 1 207 ? 16.63865 18.98296  26.91149 1.000 46.38628  ?  207  ASP   A OD1 1 
ATOM   1306 O OD2 . ASP   A 1 207 ? 15.84154 17.00780  26.37166 1.000 44.92617  -1 207  ASP   A OD2 1 
ATOM   1307 N N   . PHE   A 1 208 ? 13.40342 18.32593  28.52123 1.000 45.27973  ?  208  PHE   A N   1 
ATOM   1308 C CA  . PHE   A 1 208 ? 12.14888 18.88775  28.03155 1.000 43.69980  ?  208  PHE   A CA  1 
ATOM   1309 C C   . PHE   A 1 208 ? 12.33735 19.99241  26.99734 1.000 41.26148  ?  208  PHE   A C   1 
ATOM   1310 O O   . PHE   A 1 208 ? 11.34804 20.61141  26.58753 1.000 42.60980  ?  208  PHE   A O   1 
ATOM   1311 C CB  . PHE   A 1 208 ? 11.31488 19.42198  29.20049 1.000 48.50947  ?  208  PHE   A CB  1 
ATOM   1312 C CG  . PHE   A 1 208 ? 10.79921 18.35227  30.11883 1.000 50.45556  ?  208  PHE   A CG  1 
ATOM   1313 C CD1 . PHE   A 1 208 ? 9.78279  17.50306  29.71256 1.000 49.51922  ?  208  PHE   A CD1 1 
ATOM   1314 C CD2 . PHE   A 1 208 ? 11.32467 18.19999  31.39132 1.000 51.11783  ?  208  PHE   A CD2 1 
ATOM   1315 C CE1 . PHE   A 1 208 ? 9.30380  16.51808  30.55630 1.000 52.50226  ?  208  PHE   A CE1 1 
ATOM   1316 C CE2 . PHE   A 1 208 ? 10.84995 17.21768  32.24025 1.000 56.01581  ?  208  PHE   A CE2 1 
ATOM   1317 C CZ  . PHE   A 1 208 ? 9.83808  16.37573  31.82218 1.000 56.71358  ?  208  PHE   A CZ  1 
ATOM   1318 N N   . GLY   A 1 209 ? 13.56418 20.27165  26.57687 1.000 40.48759  ?  209  GLY   A N   1 
ATOM   1319 C CA  . GLY   A 1 209 ? 13.79617 21.19499  25.48111 1.000 41.25740  ?  209  GLY   A CA  1 
ATOM   1320 C C   . GLY   A 1 209 ? 14.13747 22.60200  25.93108 1.000 43.09576  ?  209  GLY   A C   1 
ATOM   1321 O O   . GLY   A 1 209 ? 14.46510 22.87227  27.09045 1.000 41.89687  ?  209  GLY   A O   1 
ATOM   1322 N N   . LEU   A 1 210 ? 14.04911 23.51733  24.96775 1.000 41.63178  ?  210  LEU   A N   1 
ATOM   1323 C CA  . LEU   A 1 210 ? 14.43380 24.90455  25.16864 1.000 47.02532  ?  210  LEU   A CA  1 
ATOM   1324 C C   . LEU   A 1 210 ? 13.29158 25.70422  25.79382 1.000 53.06917  ?  210  LEU   A C   1 
ATOM   1325 O O   . LEU   A 1 210 ? 12.14656 25.25239  25.88041 1.000 56.87759  ?  210  LEU   A O   1 
ATOM   1326 C CB  . LEU   A 1 210 ? 14.85649 25.53770  23.84365 1.000 44.52398  ?  210  LEU   A CB  1 
ATOM   1327 C CG  . LEU   A 1 210 ? 15.88662 24.76607  23.01679 1.000 46.38990  ?  210  LEU   A CG  1 
ATOM   1328 C CD1 . LEU   A 1 210 ? 15.87569 25.23192  21.56816 1.000 44.09946  ?  210  LEU   A CD1 1 
ATOM   1329 C CD2 . LEU   A 1 210 ? 17.27425 24.91356  23.62043 1.000 44.70575  ?  210  LEU   A CD2 1 
ATOM   1330 N N   . ALA   A 1 211 ? 13.62064 26.91717  26.22814 1.000 52.20898  ?  211  ALA   A N   1 
ATOM   1331 C CA  . ALA   A 1 211 ? 12.64669 27.80727  26.85028 1.000 55.95802  ?  211  ALA   A CA  1 
ATOM   1332 C C   . ALA   A 1 211 ? 11.66504 28.35767  25.82091 1.000 56.83380  ?  211  ALA   A C   1 
ATOM   1333 O O   . ALA   A 1 211 ? 11.99923 28.50449  24.64500 1.000 53.97433  ?  211  ALA   A O   1 
ATOM   1334 C CB  . ALA   A 1 211 ? 13.35439 28.94483  27.56917 1.000 53.69940  ?  211  ALA   A CB  1 
ATOM   1335 N N   . SER   A 1 217 ? 21.41500 33.84004  26.09644 1.000 67.81288  ?  217  SER   A N   1 
ATOM   1336 C CA  . SER   A 1 217 ? 21.76685 32.66450  26.88371 1.000 69.09364  ?  217  SER   A CA  1 
ATOM   1337 C C   . SER   A 1 217 ? 23.27490 32.43778  26.88695 1.000 69.37451  ?  217  SER   A C   1 
ATOM   1338 O O   . SER   A 1 217 ? 23.76380 31.44587  26.34573 1.000 70.97981  ?  217  SER   A O   1 
ATOM   1339 C CB  . SER   A 1 217 ? 21.04965 31.42422  26.34636 1.000 71.24251  ?  217  SER   A CB  1 
ATOM   1340 O OG  . SER   A 1 217 ? 21.59440 30.23995  26.90196 1.000 66.90084  ?  217  SER   A OG  1 
ATOM   1341 N N   . PHE   A 1 218 ? 24.00689 33.36432  27.49973 1.000 69.72433  ?  218  PHE   A N   1 
ATOM   1342 C CA  . PHE   A 1 218 ? 25.45629 33.24697  27.56975 1.000 69.70242  ?  218  PHE   A CA  1 
ATOM   1343 C C   . PHE   A 1 218 ? 25.85604 32.10925  28.50106 1.000 71.88884  ?  218  PHE   A C   1 
ATOM   1344 O O   . PHE   A 1 218 ? 25.30658 31.95660  29.59576 1.000 70.06036  ?  218  PHE   A O   1 
ATOM   1345 C CB  . PHE   A 1 218 ? 26.07275 34.56040  28.04776 1.000 63.45859  ?  218  PHE   A CB  1 
ATOM   1346 C CG  . PHE   A 1 218 ? 27.52826 34.45379  28.39865 1.000 61.55687  ?  218  PHE   A CG  1 
ATOM   1347 C CD1 . PHE   A 1 218 ? 28.47169 34.18689  27.42122 1.000 58.86468  ?  218  PHE   A CD1 1 
ATOM   1348 C CD2 . PHE   A 1 218 ? 27.95378 34.62242  29.70550 1.000 65.13646  ?  218  PHE   A CD2 1 
ATOM   1349 C CE1 . PHE   A 1 218 ? 29.81195 34.08870  27.74096 1.000 59.89627  ?  218  PHE   A CE1 1 
ATOM   1350 C CE2 . PHE   A 1 218 ? 29.29303 34.52596  30.03086 1.000 63.09564  ?  218  PHE   A CE2 1 
ATOM   1351 C CZ  . PHE   A 1 218 ? 30.22279 34.25961  29.04668 1.000 62.20934  ?  218  PHE   A CZ  1 
ATOM   1352 N N   . MET   A 1 219 ? 26.82326 31.30964  28.06042 1.000 73.22420  ?  219  MET   A N   1 
ATOM   1353 C CA  . MET   A 1 219 ? 27.28249 30.13966  28.79821 1.000 76.18486  ?  219  MET   A CA  1 
ATOM   1354 C C   . MET   A 1 219 ? 28.70584 30.37763  29.28445 1.000 80.87213  ?  219  MET   A C   1 
ATOM   1355 O O   . MET   A 1 219 ? 29.62526 30.53557  28.47367 1.000 77.17053  ?  219  MET   A O   1 
ATOM   1356 C CB  . MET   A 1 219 ? 27.21290 28.88462  27.92787 1.000 79.63794  ?  219  MET   A CB  1 
ATOM   1357 C CG  . MET   A 1 219 ? 25.79698 28.42222  27.62345 1.000 77.96350  ?  219  MET   A CG  1 
ATOM   1358 S SD  . MET   A 1 219 ? 25.58342 27.89357  25.91269 1.000 79.13415  ?  219  MET   A SD  1 
ATOM   1359 C CE  . MET   A 1 219 ? 26.41938 29.21555  25.04019 1.000 75.05560  ?  219  MET   A CE  1 
ATOM   1360 N N   . MET   A 1 220 ? 28.88091 30.40239  30.60435 1.000 103.36315 ?  220  MET   A N   1 
ATOM   1361 C CA  . MET   A 1 220 ? 30.20084 30.54096  31.22034 1.000 101.90920 ?  220  MET   A CA  1 
ATOM   1362 C C   . MET   A 1 220 ? 30.79245 29.16133  31.51327 1.000 102.08277 ?  220  MET   A C   1 
ATOM   1363 O O   . MET   A 1 220 ? 31.02837 28.77407  32.65716 1.000 100.17017 ?  220  MET   A O   1 
ATOM   1364 C CB  . MET   A 1 220 ? 30.10307 31.38146  32.48723 1.000 102.85153 ?  220  MET   A CB  1 
ATOM   1365 C CG  . MET   A 1 220 ? 31.41654 31.98827  32.94535 1.000 105.00146 ?  220  MET   A CG  1 
ATOM   1366 S SD  . MET   A 1 220 ? 32.09727 33.16131  31.76210 1.000 110.39777 ?  220  MET   A SD  1 
ATOM   1367 C CE  . MET   A 1 220 ? 33.80925 32.64724  31.74906 1.000 107.41937 ?  220  MET   A CE  1 
ATOM   1368 N N   . THR   A 1 221 ? 31.03180 28.41504  30.43936 1.000 99.15175  ?  221  THR   A N   1 
ATOM   1369 C CA  . THR   A 1 221 ? 31.44968 27.02640  30.54417 1.000 101.58728 ?  221  THR   A CA  1 
ATOM   1370 C C   . THR   A 1 221 ? 32.30472 26.68199  29.33431 1.000 102.56569 ?  221  THR   A C   1 
ATOM   1371 O O   . THR   A 1 221 ? 32.15365 27.30453  28.27627 1.000 98.35618  ?  221  THR   A O   1 
ATOM   1372 C CB  . THR   A 1 221 ? 30.22947 26.09210  30.64343 1.000 103.46004 ?  221  THR   A CB  1 
ATOM   1373 O OG1 . THR   A 1 221 ? 30.58951 24.88052  31.31910 1.000 102.39575 ?  221  THR   A OG1 1 
ATOM   1374 C CG2 . THR   A 1 221 ? 29.66704 25.76779  29.26897 1.000 99.99910  ?  221  THR   A CG2 1 
ATOM   1375 N N   . PRO   A 1 222 ? 33.23282 25.72661  29.46529 1.000 97.51184  ?  222  PRO   A N   1 
ATOM   1376 C CA  . PRO   A 1 222 ? 34.02136 25.31633  28.29423 1.000 95.49653  ?  222  PRO   A CA  1 
ATOM   1377 C C   . PRO   A 1 222 ? 33.32225 24.29096  27.42100 1.000 94.62647  ?  222  PRO   A C   1 
ATOM   1378 O O   . PRO   A 1 222 ? 33.64764 24.19548  26.23029 1.000 91.47901  ?  222  PRO   A O   1 
ATOM   1379 C CB  . PRO   A 1 222 ? 35.30474 24.73532  28.91024 1.000 91.96773  ?  222  PRO   A CB  1 
ATOM   1380 C CG  . PRO   A 1 222 ? 35.01991 24.53797  30.37832 1.000 93.51478  ?  222  PRO   A CG  1 
ATOM   1381 C CD  . PRO   A 1 222 ? 33.63126 25.00728  30.68620 1.000 95.84683  ?  222  PRO   A CD  1 
ATOM   1382 N N   . TYR   A 1 223 ? 32.37559 23.53175  27.96618 1.000 93.55162  ?  223  TYR   A N   1 
ATOM   1383 C CA  . TYR   A 1 223 ? 31.65947 22.52539  27.19522 1.000 91.63419  ?  223  TYR   A CA  1 
ATOM   1384 C C   . TYR   A 1 223 ? 30.64273 23.19216  26.27724 1.000 87.96920  ?  223  TYR   A C   1 
ATOM   1385 O O   . TYR   A 1 223 ? 29.79977 23.97045  26.73159 1.000 87.97433  ?  223  TYR   A O   1 
ATOM   1386 C CB  . TYR   A 1 223 ? 30.96378 21.53693  28.13080 1.000 93.75147  ?  223  TYR   A CB  1 
ATOM   1387 C CG  . TYR   A 1 223 ? 30.67440 20.19884  27.49449 1.000 94.68382  ?  223  TYR   A CG  1 
ATOM   1388 C CD1 . TYR   A 1 223 ? 31.53441 19.65962  26.54733 1.000 94.73602  ?  223  TYR   A CD1 1 
ATOM   1389 C CD2 . TYR   A 1 223 ? 29.54165 19.47452  27.84009 1.000 96.41771  ?  223  TYR   A CD2 1 
ATOM   1390 C CE1 . TYR   A 1 223 ? 31.27467 18.43612  25.96224 1.000 96.68430  ?  223  TYR   A CE1 1 
ATOM   1391 C CE2 . TYR   A 1 223 ? 29.27298 18.24970  27.26049 1.000 97.61772  ?  223  TYR   A CE2 1 
ATOM   1392 C CZ  . TYR   A 1 223 ? 30.14330 17.73529  26.32180 1.000 98.27923  ?  223  TYR   A CZ  1 
ATOM   1393 O OH  . TYR   A 1 223 ? 29.88055 16.51586  25.74094 1.000 98.72872  ?  223  TYR   A OH  1 
ATOM   1394 N N   . VAL   A 1 224 ? 30.71762 22.88157  24.99185 1.000 87.28417  ?  224  VAL   A N   1 
ATOM   1395 C CA  . VAL   A 1 224 ? 29.83899 23.48599  23.99848 1.000 77.62036  ?  224  VAL   A CA  1 
ATOM   1396 C C   . VAL   A 1 224 ? 28.56839 22.65822  23.87570 1.000 69.22987  ?  224  VAL   A C   1 
ATOM   1397 O O   . VAL   A 1 224 ? 28.54672 21.45594  24.15983 1.000 71.57225  ?  224  VAL   A O   1 
ATOM   1398 C CB  . VAL   A 1 224 ? 30.55337 23.62402  22.63853 1.000 77.87787  ?  224  VAL   A CB  1 
ATOM   1399 C CG1 . VAL   A 1 224 ? 31.39067 24.89325  22.60733 1.000 84.54541  ?  224  VAL   A CG1 1 
ATOM   1400 C CG2 . VAL   A 1 224 ? 31.41553 22.40135  22.36604 1.000 78.54251  ?  224  VAL   A CG2 1 
ATOM   1401 N N   . VAL   A 1 225 ? 27.49413 23.31395  23.44700 1.000 64.50351  ?  225  VAL   A N   1 
ATOM   1402 C CA  . VAL   A 1 225 ? 26.21471 22.65240  23.24511 1.000 55.44391  ?  225  VAL   A CA  1 
ATOM   1403 C C   . VAL   A 1 225 ? 26.18598 22.04139  21.84878 1.000 49.12682  ?  225  VAL   A C   1 
ATOM   1404 O O   . VAL   A 1 225 ? 26.97436 22.39590  20.96844 1.000 49.65461  ?  225  VAL   A O   1 
ATOM   1405 C CB  . VAL   A 1 225 ? 25.03832 23.62968  23.45861 1.000 52.58838  ?  225  VAL   A CB  1 
ATOM   1406 C CG1 . VAL   A 1 225 ? 24.77169 24.43592  22.19417 1.000 47.85876  ?  225  VAL   A CG1 1 
ATOM   1407 C CG2 . VAL   A 1 225 ? 23.78844 22.88256  23.90927 1.000 48.80655  ?  225  VAL   A CG2 1 
ATOM   1408 N N   . THR   A 1 226 ? 25.26754 21.10063  21.64676 1.000 46.80092  ?  226  THR   A N   1 
ATOM   1409 C CA  . THR   A 1 226 ? 25.12458 20.39354  20.37991 1.000 40.96934  ?  226  THR   A CA  1 
ATOM   1410 C C   . THR   A 1 226 ? 23.90488 20.93280  19.64202 1.000 38.06633  ?  226  THR   A C   1 
ATOM   1411 O O   . THR   A 1 226 ? 22.79002 20.90350  20.17569 1.000 37.84165  ?  226  THR   A O   1 
ATOM   1412 C CB  . THR   A 1 226 ? 24.99401 18.88741  20.61073 1.000 37.54618  ?  226  THR   A CB  1 
ATOM   1413 O OG1 . THR   A 1 226 ? 26.25625 18.35820  21.03627 1.000 40.56627  ?  226  THR   A OG1 1 
ATOM   1414 C CG2 . THR   A 1 226 ? 24.56182 18.18541  19.33214 1.000 33.61752  ?  226  THR   A CG2 1 
ATOM   1415 N N   . ARG   A 1 227 ? 24.11765 21.41989  18.41740 1.000 35.34681  ?  227  ARG   A N   1 
ATOM   1416 C CA  . ARG   A 1 227 ? 23.05552 22.02950  17.62502 1.000 34.32478  ?  227  ARG   A CA  1 
ATOM   1417 C C   . ARG   A 1 227 ? 22.78637 21.28649  16.32195 1.000 33.46119  ?  227  ARG   A C   1 
ATOM   1418 O O   . ARG   A 1 227 ? 21.98221 21.75751  15.50858 1.000 31.62658  ?  227  ARG   A O   1 
ATOM   1419 C CB  . ARG   A 1 227 ? 23.39486 23.49241  17.31509 1.000 40.24005  ?  227  ARG   A CB  1 
ATOM   1420 C CG  . ARG   A 1 227 ? 24.46104 24.09642  18.21005 1.000 40.74126  ?  227  ARG   A CG  1 
ATOM   1421 C CD  . ARG   A 1 227 ? 24.56162 25.60140  18.00091 1.000 42.58924  ?  227  ARG   A CD  1 
ATOM   1422 N NE  . ARG   A 1 227 ? 25.59240 26.20874  18.83516 1.000 50.53065  ?  227  ARG   A NE  1 
ATOM   1423 C CZ  . ARG   A 1 227 ? 26.89630 26.10827  18.61301 1.000 50.98252  ?  227  ARG   A CZ  1 
ATOM   1424 N NH1 . ARG   A 1 227 ? 27.37261 25.43713  17.57655 1.000 49.32580  ?  227  ARG   A NH1 1 
ATOM   1425 N NH2 . ARG   A 1 227 ? 27.74433 26.69778  19.45111 1.000 53.24138  ?  227  ARG   A NH2 1 
ATOM   1426 N N   . TYR   A 1 228 ? 23.42532 20.13593  16.10337 1.000 31.68926  ?  228  TYR   A N   1 
ATOM   1427 C CA  . TYR   A 1 228 ? 23.31858 19.43196  14.82955 1.000 31.94057  ?  228  TYR   A CA  1 
ATOM   1428 C C   . TYR   A 1 228 ? 21.92090 18.89690  14.54899 1.000 31.72862  ?  228  TYR   A C   1 
ATOM   1429 O O   . TYR   A 1 228 ? 21.64449 18.51463  13.40670 1.000 33.19535  ?  228  TYR   A O   1 
ATOM   1430 C CB  . TYR   A 1 228 ? 24.31957 18.27540  14.78472 1.000 31.88716  ?  228  TYR   A CB  1 
ATOM   1431 C CG  . TYR   A 1 228 ? 25.69164 18.62477  15.31167 1.000 31.85039  ?  228  TYR   A CG  1 
ATOM   1432 C CD1 . TYR   A 1 228 ? 26.35519 17.77585  16.18750 1.000 32.04692  ?  228  TYR   A CD1 1 
ATOM   1433 C CD2 . TYR   A 1 228 ? 26.32526 19.80055  14.93191 1.000 35.23705  ?  228  TYR   A CD2 1 
ATOM   1434 C CE1 . TYR   A 1 228 ? 27.60995 18.08941  16.67162 1.000 33.21710  ?  228  TYR   A CE1 1 
ATOM   1435 C CE2 . TYR   A 1 228 ? 27.57923 20.12290  15.41158 1.000 39.70048  ?  228  TYR   A CE2 1 
ATOM   1436 C CZ  . TYR   A 1 228 ? 28.21693 19.26360  16.28056 1.000 36.85534  ?  228  TYR   A CZ  1 
ATOM   1437 O OH  . TYR   A 1 228 ? 29.46665 19.58033  16.76018 1.000 46.98641  ?  228  TYR   A OH  1 
ATOM   1438 N N   . TYR   A 1 229 ? 21.03890 18.86457  15.54547 1.000 30.11135  ?  229  TYR   A N   1 
ATOM   1439 C CA  . TYR   A 1 229 ? 19.72965 18.24092  15.40978 1.000 29.88291  ?  229  TYR   A CA  1 
ATOM   1440 C C   . TYR   A 1 229 ? 18.58794 19.24709  15.48160 1.000 30.03451  ?  229  TYR   A C   1 
ATOM   1441 O O   . TYR   A 1 229 ? 17.41995 18.84493  15.50994 1.000 29.82970  ?  229  TYR   A O   1 
ATOM   1442 C CB  . TYR   A 1 229 ? 19.55479 17.16017  16.48022 1.000 28.11230  ?  229  TYR   A CB  1 
ATOM   1443 C CG  . TYR   A 1 229 ? 20.70777 16.18163  16.53863 1.000 27.94218  ?  229  TYR   A CG  1 
ATOM   1444 C CD1 . TYR   A 1 229 ? 20.66522 14.98659  15.83280 1.000 28.58880  ?  229  TYR   A CD1 1 
ATOM   1445 C CD2 . TYR   A 1 229 ? 21.84155 16.45500  17.29468 1.000 27.26655  ?  229  TYR   A CD2 1 
ATOM   1446 C CE1 . TYR   A 1 229 ? 21.71701 14.09176  15.87821 1.000 28.54740  ?  229  TYR   A CE1 1 
ATOM   1447 C CE2 . TYR   A 1 229 ? 22.89903 15.56725  17.34488 1.000 27.27391  ?  229  TYR   A CE2 1 
ATOM   1448 C CZ  . TYR   A 1 229 ? 22.83067 14.38695  16.63482 1.000 27.90559  ?  229  TYR   A CZ  1 
ATOM   1449 O OH  . TYR   A 1 229 ? 23.87999 13.49837  16.68265 1.000 28.01145  ?  229  TYR   A OH  1 
ATOM   1450 N N   . ARG   A 1 230 ? 18.89281 20.54127  15.50261 1.000 30.53128  ?  230  ARG   A N   1 
ATOM   1451 C CA  . ARG   A 1 230 ? 17.85776 21.56226  15.56361 1.000 30.82616  ?  230  ARG   A CA  1 
ATOM   1452 C C   . ARG   A 1 230 ? 17.29593 21.83600  14.17406 1.000 33.02076  ?  230  ARG   A C   1 
ATOM   1453 O O   . ARG   A 1 230 ? 18.03349 21.87572  13.18544 1.000 34.60727  ?  230  ARG   A O   1 
ATOM   1454 C CB  . ARG   A 1 230 ? 18.41585 22.84758  16.17429 1.000 30.58151  ?  230  ARG   A CB  1 
ATOM   1455 C CG  . ARG   A 1 230 ? 19.34036 22.60500  17.35558 1.000 32.06444  ?  230  ARG   A CG  1 
ATOM   1456 C CD  . ARG   A 1 230 ? 19.63787 23.88855  18.10948 1.000 35.13342  ?  230  ARG   A CD  1 
ATOM   1457 N NE  . ARG   A 1 230 ? 20.04377 23.62489  19.48492 1.000 35.77432  ?  230  ARG   A NE  1 
ATOM   1458 C CZ  . ARG   A 1 230 ? 20.40423 24.56084  20.35212 1.000 36.72479  ?  230  ARG   A CZ  1 
ATOM   1459 N NH1 . ARG   A 1 230 ? 20.42651 25.84121  20.01822 1.000 36.28373  ?  230  ARG   A NH1 1 
ATOM   1460 N NH2 . ARG   A 1 230 ? 20.75154 24.20346  21.58504 1.000 39.04566  ?  230  ARG   A NH2 1 
ATOM   1461 N N   . ALA   A 1 231 ? 15.98009 22.02920  14.10931 1.000 33.25736  ?  231  ALA   A N   1 
ATOM   1462 C CA  . ALA   A 1 231 ? 15.29250 22.20763  12.84294 1.000 35.41247  ?  231  ALA   A CA  1 
ATOM   1463 C C   . ALA   A 1 231 ? 15.72812 23.50592  12.16427 1.000 37.22231  ?  231  ALA   A C   1 
ATOM   1464 O O   . ALA   A 1 231 ? 16.25630 24.41097  12.81522 1.000 36.65155  ?  231  ALA   A O   1 
ATOM   1465 C CB  . ALA   A 1 231 ? 13.78222 22.20538  13.06432 1.000 35.27891  ?  231  ALA   A CB  1 
ATOM   1466 N N   . PRO   A 1 232 ? 15.53056 23.61248  10.84313 1.000 39.58600  ?  232  PRO   A N   1 
ATOM   1467 C CA  . PRO   A 1 232 ? 15.90184 24.86191  10.15555 1.000 41.63120  ?  232  PRO   A CA  1 
ATOM   1468 C C   . PRO   A 1 232 ? 15.20498 26.08856  10.71520 1.000 41.53029  ?  232  PRO   A C   1 
ATOM   1469 O O   . PRO   A 1 232 ? 15.80933 27.16692  10.76697 1.000 42.21870  ?  232  PRO   A O   1 
ATOM   1470 C CB  . PRO   A 1 232 ? 15.49708 24.59257  8.69933  1.000 44.19270  ?  232  PRO   A CB  1 
ATOM   1471 C CG  . PRO   A 1 232 ? 15.51478 23.11393  8.56539  1.000 43.42410  ?  232  PRO   A CG  1 
ATOM   1472 C CD  . PRO   A 1 232 ? 15.10002 22.56751  9.89719  1.000 40.66939  ?  232  PRO   A CD  1 
ATOM   1473 N N   . GLU   A 1 233 ? 13.94495 25.95430  11.13805 1.000 40.80970  ?  233  GLU   A N   1 
ATOM   1474 C CA  . GLU   A 1 233 ? 13.24255 27.08675  11.73148 1.000 40.92787  ?  233  GLU   A CA  1 
ATOM   1475 C C   . GLU   A 1 233 ? 13.92204 27.55614  13.01114 1.000 41.24372  ?  233  GLU   A C   1 
ATOM   1476 O O   . GLU   A 1 233 ? 13.87448 28.74740  13.33755 1.000 45.05838  ?  233  GLU   A O   1 
ATOM   1477 C CB  . GLU   A 1 233 ? 11.78259 26.72002  12.00277 1.000 41.90979  ?  233  GLU   A CB  1 
ATOM   1478 C CG  . GLU   A 1 233 ? 11.58749 25.35222  12.63315 1.000 40.01874  ?  233  GLU   A CG  1 
ATOM   1479 C CD  . GLU   A 1 233 ? 11.26092 24.27978  11.61192 1.000 40.43930  ?  233  GLU   A CD  1 
ATOM   1480 O OE1 . GLU   A 1 233 ? 12.05810 24.09286  10.66880 1.000 40.81418  ?  233  GLU   A OE1 1 
ATOM   1481 O OE2 . GLU   A 1 233 ? 10.20703 23.62403  11.75261 1.000 39.85630  -1 233  GLU   A OE2 1 
ATOM   1482 N N   . VAL   A 1 234 ? 14.55903 26.64196  13.74378 1.000 36.67472  ?  234  VAL   A N   1 
ATOM   1483 C CA  . VAL   A 1 234 ? 15.33243 27.03531  14.91621 1.000 40.32894  ?  234  VAL   A CA  1 
ATOM   1484 C C   . VAL   A 1 234 ? 16.67769 27.61520  14.49856 1.000 39.73159  ?  234  VAL   A C   1 
ATOM   1485 O O   . VAL   A 1 234 ? 17.15375 28.59359  15.08598 1.000 44.66076  ?  234  VAL   A O   1 
ATOM   1486 C CB  . VAL   A 1 234 ? 15.50086 25.83619  15.86728 1.000 36.77797  ?  234  VAL   A CB  1 
ATOM   1487 C CG1 . VAL   A 1 234 ? 16.38858 26.20974  17.04577 1.000 36.91092  ?  234  VAL   A CG1 1 
ATOM   1488 C CG2 . VAL   A 1 234 ? 14.14439 25.34343  16.34686 1.000 34.72398  ?  234  VAL   A CG2 1 
ATOM   1489 N N   . ILE   A 1 235 ? 17.30563 27.02429  13.47813 1.000 37.30619  ?  235  ILE   A N   1 
ATOM   1490 C CA  . ILE   A 1 235 ? 18.58268 27.53053  12.98098 1.000 40.58993  ?  235  ILE   A CA  1 
ATOM   1491 C C   . ILE   A 1 235 ? 18.44473 28.97975  12.53173 1.000 40.78888  ?  235  ILE   A C   1 
ATOM   1492 O O   . ILE   A 1 235 ? 19.32688 29.81124  12.78008 1.000 41.00112  ?  235  ILE   A O   1 
ATOM   1493 C CB  . ILE   A 1 235 ? 19.10016 26.63421  11.83905 1.000 40.04100  ?  235  ILE   A CB  1 
ATOM   1494 C CG1 . ILE   A 1 235 ? 19.53128 25.26822  12.37471 1.000 38.17231  ?  235  ILE   A CG1 1 
ATOM   1495 C CG2 . ILE   A 1 235 ? 20.25010 27.30557  11.09869 1.000 42.12145  ?  235  ILE   A CG2 1 
ATOM   1496 C CD1 . ILE   A 1 235 ? 19.95637 24.30070  11.29011 1.000 39.46017  ?  235  ILE   A CD1 1 
ATOM   1497 N N   . LEU   A 1 236 ? 17.33186 29.30873  11.88052 1.000 41.94800  ?  236  LEU   A N   1 
ATOM   1498 C CA  . LEU   A 1 236 ? 17.12803 30.62400  11.29235 1.000 48.63474  ?  236  LEU   A CA  1 
ATOM   1499 C C   . LEU   A 1 236 ? 16.17415 31.50089  12.09291 1.000 51.31508  ?  236  LEU   A C   1 
ATOM   1500 O O   . LEU   A 1 236 ? 15.96373 32.65844  11.71938 1.000 47.15885  ?  236  LEU   A O   1 
ATOM   1501 C CB  . LEU   A 1 236 ? 16.61183 30.47551  9.85707  1.000 46.83588  ?  236  LEU   A CB  1 
ATOM   1502 C CG  . LEU   A 1 236 ? 17.46705 29.59434  8.94404  1.000 47.87532  ?  236  LEU   A CG  1 
ATOM   1503 C CD1 . LEU   A 1 236 ? 16.82527 29.43915  7.57462  1.000 50.49759  ?  236  LEU   A CD1 1 
ATOM   1504 C CD2 . LEU   A 1 236 ? 18.87295 30.15971  8.81946  1.000 48.84121  ?  236  LEU   A CD2 1 
ATOM   1505 N N   . GLY   A 1 237 ? 15.59854 30.98605  13.17798 1.000 61.49416  ?  237  GLY   A N   1 
ATOM   1506 C CA  . GLY   A 1 237 ? 14.66684 31.75432  13.98232 1.000 59.13833  ?  237  GLY   A CA  1 
ATOM   1507 C C   . GLY   A 1 237 ? 13.43502 32.18656  13.21370 1.000 64.70074  ?  237  GLY   A C   1 
ATOM   1508 O O   . GLY   A 1 237 ? 13.32667 33.34806  12.80901 1.000 69.78206  ?  237  GLY   A O   1 
ATOM   1509 N N   . MET   A 1 238 ? 12.49588 31.26126  13.00455 1.000 54.22447  ?  238  MET   A N   1 
ATOM   1510 C CA  . MET   A 1 238 ? 11.31688 31.52961  12.19491 1.000 57.49285  ?  238  MET   A CA  1 
ATOM   1511 C C   . MET   A 1 238 ? 9.99554  31.26077  12.89890 1.000 54.85938  ?  238  MET   A C   1 
ATOM   1512 O O   . MET   A 1 238 ? 8.94270  31.55423  12.32116 1.000 59.84844  ?  238  MET   A O   1 
ATOM   1513 C CB  . MET   A 1 238 ? 11.34544 30.69219  10.90578 1.000 58.61886  ?  238  MET   A CB  1 
ATOM   1514 C CG  . MET   A 1 238 ? 12.71796 30.50160  10.28639 1.000 55.98778  ?  238  MET   A CG  1 
ATOM   1515 S SD  . MET   A 1 238 ? 12.70048 29.24392  8.99158  1.000 58.22663  ?  238  MET   A SD  1 
ATOM   1516 C CE  . MET   A 1 238 ? 10.97504 29.26795  8.50800  1.000 49.75183  ?  238  MET   A CE  1 
ATOM   1517 N N   . GLY   A 1 239 ? 10.00811 30.72238  14.10647 1.000 55.87911  ?  239  GLY   A N   1 
ATOM   1518 C CA  . GLY   A 1 239 ? 8.74859  30.24940  14.65981 1.000 56.50793  ?  239  GLY   A CA  1 
ATOM   1519 C C   . GLY   A 1 239 ? 8.44899  28.82745  14.23298 1.000 56.56552  ?  239  GLY   A C   1 
ATOM   1520 O O   . GLY   A 1 239 ? 8.85459  28.36457  13.16751 1.000 55.17873  ?  239  GLY   A O   1 
ATOM   1521 N N   . TYR   A 1 240 ? 7.71324  28.11820  15.08528 1.000 57.17636  ?  240  TYR   A N   1 
ATOM   1522 C CA  . TYR   A 1 240 ? 7.57018  26.67788  14.94313 1.000 53.48926  ?  240  TYR   A CA  1 
ATOM   1523 C C   . TYR   A 1 240 ? 6.15296  26.24509  15.28970 1.000 55.09314  ?  240  TYR   A C   1 
ATOM   1524 O O   . TYR   A 1 240 ? 5.33084  27.03188  15.76948 1.000 56.95499  ?  240  TYR   A O   1 
ATOM   1525 C CB  . TYR   A 1 240 ? 8.57535  25.94222  15.83598 1.000 50.82657  ?  240  TYR   A CB  1 
ATOM   1526 C CG  . TYR   A 1 240 ? 8.59771  26.45899  17.25787 1.000 53.48790  ?  240  TYR   A CG  1 
ATOM   1527 C CD1 . TYR   A 1 240 ? 7.60045  26.11122  18.16192 1.000 52.71551  ?  240  TYR   A CD1 1 
ATOM   1528 C CD2 . TYR   A 1 240 ? 9.60245  27.31363  17.68988 1.000 53.69923  ?  240  TYR   A CD2 1 
ATOM   1529 C CE1 . TYR   A 1 240 ? 7.60938  26.58914  19.45607 1.000 52.77466  ?  240  TYR   A CE1 1 
ATOM   1530 C CE2 . TYR   A 1 240 ? 9.61831  27.79854  18.98348 1.000 54.33605  ?  240  TYR   A CE2 1 
ATOM   1531 C CZ  . TYR   A 1 240 ? 8.62118  27.42948  19.86345 1.000 53.03428  ?  240  TYR   A CZ  1 
ATOM   1532 O OH  . TYR   A 1 240 ? 8.63264  27.90279  21.15491 1.000 54.14069  ?  240  TYR   A OH  1 
ATOM   1533 N N   . LYS   A 1 241 ? 5.88278  24.96870  15.03675 1.000 53.84142  ?  241  LYS   A N   1 
ATOM   1534 C CA  . LYS   A 1 241 ? 4.66516  24.31266  15.49687 1.000 53.82447  ?  241  LYS   A CA  1 
ATOM   1535 C C   . LYS   A 1 241 ? 5.08744  23.03810  16.22450 1.000 52.15022  ?  241  LYS   A C   1 
ATOM   1536 O O   . LYS   A 1 241 ? 6.20497  22.92078  16.74129 1.000 52.08629  ?  241  LYS   A O   1 
ATOM   1537 C CB  . LYS   A 1 241 ? 3.70565  24.03650  14.33173 1.000 60.23716  ?  241  LYS   A CB  1 
ATOM   1538 C CG  . LYS   A 1 241 ? 3.59767  25.16619  13.32041 1.000 64.61437  ?  241  LYS   A CG  1 
ATOM   1539 C CD  . LYS   A 1 241 ? 2.21117  25.21482  12.70006 1.000 64.00712  ?  241  LYS   A CD  1 
ATOM   1540 C CE  . LYS   A 1 241 ? 1.75946  26.64706  12.46661 1.000 64.01950  ?  241  LYS   A CE  1 
ATOM   1541 N NZ  . LYS   A 1 241 ? 1.57084  27.39069  13.74269 1.000 54.56321  ?  241  LYS   A NZ  1 
ATOM   1542 N N   . GLU   A 1 242 ? 4.18866  22.05351  16.26563 1.000 52.61105  ?  242  GLU   A N   1 
ATOM   1543 C CA  . GLU   A 1 242 ? 4.50492  20.79651  16.93654 1.000 50.34348  ?  242  GLU   A CA  1 
ATOM   1544 C C   . GLU   A 1 242 ? 5.56804  20.01270  16.17641 1.000 48.89583  ?  242  GLU   A C   1 
ATOM   1545 O O   . GLU   A 1 242 ? 6.49638  19.46568  16.78293 1.000 47.81557  ?  242  GLU   A O   1 
ATOM   1546 C CB  . GLU   A 1 242 ? 3.23770  19.95624  17.10131 1.000 51.70602  ?  242  GLU   A CB  1 
ATOM   1547 C CG  . GLU   A 1 242 ? 2.48046  20.21326  18.39357 1.000 56.61286  ?  242  GLU   A CG  1 
ATOM   1548 C CD  . GLU   A 1 242 ? 1.52777  21.38879  18.29090 1.000 57.74081  ?  242  GLU   A CD  1 
ATOM   1549 O OE1 . GLU   A 1 242 ? 1.60435  22.13612  17.29361 1.000 56.05426  ?  242  GLU   A OE1 1 
ATOM   1550 O OE2 . GLU   A 1 242 ? 0.69922  21.56453  19.20874 1.000 59.53676  -1 242  GLU   A OE2 1 
ATOM   1551 N N   . ASN   A 1 243 ? 5.45851  19.95907  14.85026 1.000 52.75023  ?  243  ASN   A N   1 
ATOM   1552 C CA  . ASN   A 1 243 ? 6.33601  19.16254  13.99219 1.000 53.02854  ?  243  ASN   A CA  1 
ATOM   1553 C C   . ASN   A 1 243 ? 7.77677  19.67415  13.93896 1.000 51.22895  ?  243  ASN   A C   1 
ATOM   1554 O O   . ASN   A 1 243 ? 8.53144  19.17864  13.09080 1.000 53.94113  ?  243  ASN   A O   1 
ATOM   1555 C CB  . ASN   A 1 243 ? 5.75684  19.10161  12.57844 1.000 54.02108  ?  243  ASN   A CB  1 
ATOM   1556 C CG  . ASN   A 1 243 ? 5.87480  20.42171  11.84339 1.000 53.92895  ?  243  ASN   A CG  1 
ATOM   1557 O OD1 . ASN   A 1 243 ? 5.84013  21.49071  12.45259 1.000 52.06009  ?  243  ASN   A OD1 1 
ATOM   1558 N ND2 . ASN   A 1 243 ? 6.01413  20.35356  10.52492 1.000 58.79706  ?  243  ASN   A ND2 1 
ATOM   1559 N N   . VAL   A 1 244 ? 8.19630  20.62518  14.77651 1.000 47.23817  ?  244  VAL   A N   1 
ATOM   1560 C CA  . VAL   A 1 244 ? 9.59444  21.04218  14.77076 1.000 43.78440  ?  244  VAL   A CA  1 
ATOM   1561 C C   . VAL   A 1 244 ? 10.48497 19.93034  15.31307 1.000 40.17766  ?  244  VAL   A C   1 
ATOM   1562 O O   . VAL   A 1 244 ? 11.66099 19.82827  14.94211 1.000 36.90813  ?  244  VAL   A O   1 
ATOM   1563 C CB  . VAL   A 1 244 ? 9.75967  22.35305  15.56506 1.000 45.81924  ?  244  VAL   A CB  1 
ATOM   1564 C CG1 . VAL   A 1 244 ? 9.43440  22.13509  17.02882 1.000 43.35904  ?  244  VAL   A CG1 1 
ATOM   1565 C CG2 . VAL   A 1 244 ? 11.16415 22.91352  15.40543 1.000 41.55492  ?  244  VAL   A CG2 1 
ATOM   1566 N N   . ASP   A 1 245 ? 9.94406  19.07228  16.18085 1.000 39.78588  ?  245  ASP   A N   1 
ATOM   1567 C CA  . ASP   A 1 245 ? 10.70521 17.95205  16.71796 1.000 38.95743  ?  245  ASP   A CA  1 
ATOM   1568 C C   . ASP   A 1 245 ? 10.83196 16.80475  15.72761 1.000 41.21109  ?  245  ASP   A C   1 
ATOM   1569 O O   . ASP   A 1 245 ? 11.69285 15.93750  15.91130 1.000 38.47485  ?  245  ASP   A O   1 
ATOM   1570 C CB  . ASP   A 1 245 ? 10.05597 17.44423  18.00688 1.000 41.17545  ?  245  ASP   A CB  1 
ATOM   1571 C CG  . ASP   A 1 245 ? 9.84776  18.54533  19.02480 1.000 35.28306  ?  245  ASP   A CG  1 
ATOM   1572 O OD1 . ASP   A 1 245 ? 10.82439 19.25877  19.33347 1.000 34.31352  ?  245  ASP   A OD1 1 
ATOM   1573 O OD2 . ASP   A 1 245 ? 8.70838  18.69836  19.51370 1.000 34.21337  -1 245  ASP   A OD2 1 
ATOM   1574 N N   . ILE   A 1 246 ? 9.99323  16.78059  14.68997 1.000 47.39818  ?  246  ILE   A N   1 
ATOM   1575 C CA  . ILE   A 1 246 ? 10.07391 15.72417  13.68603 1.000 41.25262  ?  246  ILE   A CA  1 
ATOM   1576 C C   . ILE   A 1 246 ? 11.40734 15.79134  12.95108 1.000 40.24523  ?  246  ILE   A C   1 
ATOM   1577 O O   . ILE   A 1 246 ? 12.00486 14.75874  12.62097 1.000 41.03565  ?  246  ILE   A O   1 
ATOM   1578 C CB  . ILE   A 1 246 ? 8.87380  15.82074  12.72336 1.000 42.14690  ?  246  ILE   A CB  1 
ATOM   1579 C CG1 . ILE   A 1 246 ? 7.71804  14.94968  13.22183 1.000 44.47357  ?  246  ILE   A CG1 1 
ATOM   1580 C CG2 . ILE   A 1 246 ? 9.26631  15.42937  11.31259 1.000 43.95704  ?  246  ILE   A CG2 1 
ATOM   1581 C CD1 . ILE   A 1 246 ? 7.94490  13.46325  13.03519 1.000 44.18381  ?  246  ILE   A CD1 1 
ATOM   1582 N N   . TRP   A 1 247 ? 11.90468 17.00574  12.70211 1.000 38.47956  ?  247  TRP   A N   1 
ATOM   1583 C CA  . TRP   A 1 247 ? 13.20288 17.15888  12.05226 1.000 35.96526  ?  247  TRP   A CA  1 
ATOM   1584 C C   . TRP   A 1 247 ? 14.30666 16.50804  12.87563 1.000 33.61387  ?  247  TRP   A C   1 
ATOM   1585 O O   . TRP   A 1 247 ? 15.14614 15.77548  12.33950 1.000 33.70771  ?  247  TRP   A O   1 
ATOM   1586 C CB  . TRP   A 1 247 ? 13.50488 18.64106  11.82297 1.000 35.75504  ?  247  TRP   A CB  1 
ATOM   1587 C CG  . TRP   A 1 247 ? 14.91035 18.91035  11.36088 1.000 36.33029  ?  247  TRP   A CG  1 
ATOM   1588 C CD1 . TRP   A 1 247 ? 16.03077 18.99141  12.13927 1.000 34.97444  ?  247  TRP   A CD1 1 
ATOM   1589 C CD2 . TRP   A 1 247 ? 15.34266 19.13891  10.01410 1.000 38.61583  ?  247  TRP   A CD2 1 
ATOM   1590 N NE1 . TRP   A 1 247 ? 17.13118 19.25232  11.36068 1.000 36.27515  ?  247  TRP   A NE1 1 
ATOM   1591 C CE2 . TRP   A 1 247 ? 16.73607 19.34842  10.05238 1.000 38.52450  ?  247  TRP   A CE2 1 
ATOM   1592 C CE3 . TRP   A 1 247 ? 14.68697 19.18797  8.77999  1.000 40.88951  ?  247  TRP   A CE3 1 
ATOM   1593 C CZ2 . TRP   A 1 247 ? 17.48440 19.60198  8.90553  1.000 40.63567  ?  247  TRP   A CZ2 1 
ATOM   1594 C CZ3 . TRP   A 1 247 ? 15.43226 19.43974  7.64192  1.000 42.97573  ?  247  TRP   A CZ3 1 
ATOM   1595 C CH2 . TRP   A 1 247 ? 16.81588 19.64417  7.71299  1.000 42.84051  ?  247  TRP   A CH2 1 
ATOM   1596 N N   . SER   A 1 248 ? 14.32370 16.77267  14.18577 1.000 33.35392  ?  248  SER   A N   1 
ATOM   1597 C CA  . SER   A 1 248 ? 15.33921 16.17985  15.05110 1.000 31.43056  ?  248  SER   A CA  1 
ATOM   1598 C C   . SER   A 1 248 ? 15.28007 14.65877  15.00761 1.000 30.53158  ?  248  SER   A C   1 
ATOM   1599 O O   . SER   A 1 248 ? 16.31565 13.98741  15.07802 1.000 31.67306  ?  248  SER   A O   1 
ATOM   1600 C CB  . SER   A 1 248 ? 15.16693 16.68342  16.48344 1.000 30.77368  ?  248  SER   A CB  1 
ATOM   1601 O OG  . SER   A 1 248 ? 15.13663 18.09954  16.52615 1.000 33.04754  ?  248  SER   A OG  1 
ATOM   1602 N N   . VAL   A 1 249 ? 14.07461 14.09769  14.89299 1.000 30.44158  ?  249  VAL   A N   1 
ATOM   1603 C CA  . VAL   A 1 249 ? 13.93972 12.65757  14.69717 1.000 32.01528  ?  249  VAL   A CA  1 
ATOM   1604 C C   . VAL   A 1 249 ? 14.58637 12.24240  13.38173 1.000 31.90001  ?  249  VAL   A C   1 
ATOM   1605 O O   . VAL   A 1 249 ? 15.20963 11.17781  13.28585 1.000 32.52030  ?  249  VAL   A O   1 
ATOM   1606 C CB  . VAL   A 1 249 ? 12.45511 12.24936  14.75510 1.000 34.62825  ?  249  VAL   A CB  1 
ATOM   1607 C CG1 . VAL   A 1 249 ? 12.29563 10.75702  14.49294 1.000 34.40384  ?  249  VAL   A CG1 1 
ATOM   1608 C CG2 . VAL   A 1 249 ? 11.85061 12.63085  16.09768 1.000 32.46271  ?  249  VAL   A CG2 1 
ATOM   1609 N N   . GLY   A 1 250 ? 14.46207 13.08433  12.35320 1.000 33.34012  ?  250  GLY   A N   1 
ATOM   1610 C CA  . GLY   A 1 250 ? 15.04340 12.75627  11.06147 1.000 35.01023  ?  250  GLY   A CA  1 
ATOM   1611 C C   . GLY   A 1 250 ? 16.55882 12.70883  11.08668 1.000 34.72719  ?  250  GLY   A C   1 
ATOM   1612 O O   . GLY   A 1 250 ? 17.16792 11.80088  10.51339 1.000 35.38264  ?  250  GLY   A O   1 
ATOM   1613 N N   . CYS   A 1 251 ? 17.18995 13.68614  11.74372 1.000 33.87132  ?  251  CYS   A N   1 
ATOM   1614 C CA  . CYS   A 1 251 ? 18.64588 13.67933  11.84536 1.000 33.67793  ?  251  CYS   A CA  1 
ATOM   1615 C C   . CYS   A 1 251 ? 19.13638 12.48192  12.64958 1.000 32.31514  ?  251  CYS   A C   1 
ATOM   1616 O O   . CYS   A 1 251 ? 20.19282 11.91344  12.34934 1.000 32.71839  ?  251  CYS   A O   1 
ATOM   1617 C CB  . CYS   A 1 251 ? 19.14146 14.98563  12.46638 1.000 33.08301  ?  251  CYS   A CB  1 
ATOM   1618 S SG  . CYS   A 1 251 ? 18.22883 16.46398  11.95883 1.000 34.24607  ?  251  CYS   A SG  1 
ATOM   1619 N N   . ILE   A 1 252 ? 18.38323 12.08352  13.67576 1.000 30.85334  ?  252  ILE   A N   1 
ATOM   1620 C CA  . ILE   A 1 252 ? 18.75027 10.90193  14.45018 1.000 30.97592  ?  252  ILE   A CA  1 
ATOM   1621 C C   . ILE   A 1 252 ? 18.57342 9.64436   13.61007 1.000 30.81606  ?  252  ILE   A C   1 
ATOM   1622 O O   . ILE   A 1 252 ? 19.46784 8.79370   13.53729 1.000 30.91860  ?  252  ILE   A O   1 
ATOM   1623 C CB  . ILE   A 1 252 ? 17.92514 10.83181  15.74746 1.000 30.39650  ?  252  ILE   A CB  1 
ATOM   1624 C CG1 . ILE   A 1 252 ? 18.26498 12.00874  16.66519 1.000 28.00763  ?  252  ILE   A CG1 1 
ATOM   1625 C CG2 . ILE   A 1 252 ? 18.16283 9.51035   16.45963 1.000 31.11143  ?  252  ILE   A CG2 1 
ATOM   1626 C CD1 . ILE   A 1 252 ? 17.47388 12.02176  17.95683 1.000 25.68335  ?  252  ILE   A CD1 1 
ATOM   1627 N N   . MET   A 1 253 ? 17.41680 9.51394   12.95702 1.000 31.73334  ?  253  MET   A N   1 
ATOM   1628 C CA  . MET   A 1 253 ? 17.15616 8.33889   12.13333 1.000 34.17473  ?  253  MET   A CA  1 
ATOM   1629 C C   . MET   A 1 253 ? 18.16514 8.22592   10.99862 1.000 34.34048  ?  253  MET   A C   1 
ATOM   1630 O O   . MET   A 1 253 ? 18.61992 7.12375   10.66811 1.000 34.84153  ?  253  MET   A O   1 
ATOM   1631 C CB  . MET   A 1 253 ? 15.73377 8.39527   11.58149 1.000 33.84257  ?  253  MET   A CB  1 
ATOM   1632 C CG  . MET   A 1 253 ? 15.33187 7.15918   10.81075 1.000 35.05088  ?  253  MET   A CG  1 
ATOM   1633 S SD  . MET   A 1 253 ? 13.63508 7.24899   10.22397 1.000 43.85626  ?  253  MET   A SD  1 
ATOM   1634 C CE  . MET   A 1 253 ? 13.80078 6.43940   8.64395  1.000 40.84250  ?  253  MET   A CE  1 
ATOM   1635 N N   . GLY   A 1 254 ? 18.52757 9.35578   10.39016 1.000 35.22664  ?  254  GLY   A N   1 
ATOM   1636 C CA  . GLY   A 1 254 ? 19.55158 9.32744   9.36098  1.000 36.75522  ?  254  GLY   A CA  1 
ATOM   1637 C C   . GLY   A 1 254 ? 20.91120 8.94216   9.91016  1.000 35.98853  ?  254  GLY   A C   1 
ATOM   1638 O O   . GLY   A 1 254 ? 21.69393 8.26460   9.23736  1.000 37.03584  ?  254  GLY   A O   1 
ATOM   1639 N N   . GLU   A 1 255 ? 21.20757 9.35730   11.14433 1.000 34.26518  ?  255  GLU   A N   1 
ATOM   1640 C CA  . GLU   A 1 255 ? 22.49488 9.02278   11.74230 1.000 33.61354  ?  255  GLU   A CA  1 
ATOM   1641 C C   . GLU   A 1 255 ? 22.59524 7.53958   12.07345 1.000 33.16496  ?  255  GLU   A C   1 
ATOM   1642 O O   . GLU   A 1 255 ? 23.68431 6.96299   11.98765 1.000 33.74188  ?  255  GLU   A O   1 
ATOM   1643 C CB  . GLU   A 1 255 ? 22.73191 9.86712   12.99357 1.000 32.01789  ?  255  GLU   A CB  1 
ATOM   1644 C CG  . GLU   A 1 255 ? 24.19798 10.00037  13.37337 1.000 31.90107  ?  255  GLU   A CG  1 
ATOM   1645 C CD  . GLU   A 1 255 ? 24.41571 10.94273  14.53963 1.000 30.54078  ?  255  GLU   A CD  1 
ATOM   1646 O OE1 . GLU   A 1 255 ? 23.62197 11.89367  14.69142 1.000 30.20210  ?  255  GLU   A OE1 1 
ATOM   1647 O OE2 . GLU   A 1 255 ? 25.38210 10.73429  15.30330 1.000 34.13874  -1 255  GLU   A OE2 1 
ATOM   1648 N N   . MET   A 1 256 ? 21.48240 6.90633   12.45463 1.000 32.52667  ?  256  MET   A N   1 
ATOM   1649 C CA  . MET   A 1 256 ? 21.50207 5.46342   12.67723 1.000 33.74288  ?  256  MET   A CA  1 
ATOM   1650 C C   . MET   A 1 256 ? 21.82672 4.70755   11.39637 1.000 34.82685  ?  256  MET   A C   1 
ATOM   1651 O O   . MET   A 1 256 ? 22.42790 3.63141   11.44490 1.000 34.32877  ?  256  MET   A O   1 
ATOM   1652 C CB  . MET   A 1 256 ? 20.15953 4.98979   13.23533 1.000 31.69417  ?  256  MET   A CB  1 
ATOM   1653 C CG  . MET   A 1 256 ? 19.74937 5.64108   14.54185 1.000 34.68294  ?  256  MET   A CG  1 
ATOM   1654 S SD  . MET   A 1 256 ? 18.01071 5.34808   14.92075 1.000 44.89585  ?  256  MET   A SD  1 
ATOM   1655 C CE  . MET   A 1 256 ? 18.15151 4.21704   16.30140 1.000 34.45940  ?  256  MET   A CE  1 
ATOM   1656 N N   . VAL   A 1 257 ? 21.43910 5.25262   10.24888 1.000 35.57694  ?  257  VAL   A N   1 
ATOM   1657 C CA  . VAL   A 1 257 ? 21.70331 4.62027   8.96159  1.000 37.45994  ?  257  VAL   A CA  1 
ATOM   1658 C C   . VAL   A 1 257 ? 23.09138 4.97121   8.44177  1.000 39.11473  ?  257  VAL   A C   1 
ATOM   1659 O O   . VAL   A 1 257 ? 23.80277 4.10571   7.92561  1.000 39.35327  ?  257  VAL   A O   1 
ATOM   1660 C CB  . VAL   A 1 257 ? 20.60254 5.01608   7.95427  1.000 38.81966  ?  257  VAL   A CB  1 
ATOM   1661 C CG1 . VAL   A 1 257 ? 20.97832 4.57800   6.54674  1.000 45.41470  ?  257  VAL   A CG1 1 
ATOM   1662 C CG2 . VAL   A 1 257 ? 19.26265 4.43336   8.37025  1.000 39.98155  ?  257  VAL   A CG2 1 
ATOM   1663 N N   . ARG   A 1 258 ? 23.49464 6.23132   8.57487  1.000 38.27215  ?  258  ARG   A N   1 
ATOM   1664 C CA  . ARG   A 1 258 ? 24.75865 6.69384   8.02008  1.000 39.45886  ?  258  ARG   A CA  1 
ATOM   1665 C C   . ARG   A 1 258 ? 25.92535 6.56987   8.99034  1.000 38.38479  ?  258  ARG   A C   1 
ATOM   1666 O O   . ARG   A 1 258 ? 27.07790 6.51657   8.54236  1.000 39.50738  ?  258  ARG   A O   1 
ATOM   1667 C CB  . ARG   A 1 258 ? 24.63094 8.15467   7.56707  1.000 40.26139  ?  258  ARG   A CB  1 
ATOM   1668 C CG  . ARG   A 1 258 ? 25.70325 8.60943   6.59083  1.000 43.69246  ?  258  ARG   A CG  1 
ATOM   1669 C CD  . ARG   A 1 258 ? 25.53409 10.07832  6.23120  1.000 43.13454  ?  258  ARG   A CD  1 
ATOM   1670 N NE  . ARG   A 1 258 ? 24.56180 10.27209  5.16246  1.000 44.71196  ?  258  ARG   A NE  1 
ATOM   1671 C CZ  . ARG   A 1 258 ? 24.00767 11.43748  4.85682  1.000 46.18721  ?  258  ARG   A CZ  1 
ATOM   1672 N NH1 . ARG   A 1 258 ? 24.30043 12.53919  5.52830  1.000 44.68668  ?  258  ARG   A NH1 1 
ATOM   1673 N NH2 . ARG   A 1 258 ? 23.13857 11.49945  3.85158  1.000 47.08162  ?  258  ARG   A NH2 1 
ATOM   1674 N N   . HIS   A 1 259 ? 25.65534 6.51557   10.29723 1.000 36.41053  ?  259  HIS   A N   1 
ATOM   1675 C CA  . HIS   A 1 259 ? 26.70062 6.46645   11.32204 1.000 35.40585  ?  259  HIS   A CA  1 
ATOM   1676 C C   . HIS   A 1 259 ? 27.62888 7.67271   11.20977 1.000 35.98745  ?  259  HIS   A C   1 
ATOM   1677 O O   . HIS   A 1 259 ? 28.84098 7.57646   11.41249 1.000 36.31986  ?  259  HIS   A O   1 
ATOM   1678 C CB  . HIS   A 1 259 ? 27.47920 5.15253   11.25505 1.000 35.87660  ?  259  HIS   A CB  1 
ATOM   1679 C CG  . HIS   A 1 259 ? 26.60452 3.93947   11.30386 1.000 35.56321  ?  259  HIS   A CG  1 
ATOM   1680 N ND1 . HIS   A 1 259 ? 25.83462 3.62234   12.40196 1.000 34.64201  ?  259  HIS   A ND1 1 
ATOM   1681 C CD2 . HIS   A 1 259 ? 26.35886 2.97876   10.38230 1.000 36.79297  ?  259  HIS   A CD2 1 
ATOM   1682 C CE1 . HIS   A 1 259 ? 25.16301 2.51087   12.16026 1.000 38.40137  ?  259  HIS   A CE1 1 
ATOM   1683 N NE2 . HIS   A 1 259 ? 25.46261 2.10023   10.94133 1.000 39.58791  ?  259  HIS   A NE2 1 
ATOM   1684 N N   . LYS   A 1 260 ? 27.04284 8.82023   10.87925 1.000 36.26247  ?  260  LYS   A N   1 
ATOM   1685 C CA  . LYS   A 1 260 ? 27.76216 10.07920  10.76465 1.000 36.93147  ?  260  LYS   A CA  1 
ATOM   1686 C C   . LYS   A 1 260 ? 26.76529 11.20509  10.98757 1.000 36.33051  ?  260  LYS   A C   1 
ATOM   1687 O O   . LYS   A 1 260 ? 25.59827 11.08349  10.60448 1.000 36.38393  ?  260  LYS   A O   1 
ATOM   1688 C CB  . LYS   A 1 260 ? 28.43505 10.21955  9.39338  1.000 39.35679  ?  260  LYS   A CB  1 
ATOM   1689 C CG  . LYS   A 1 260 ? 29.67214 11.10235  9.39027  1.000 40.27806  ?  260  LYS   A CG  1 
ATOM   1690 C CD  . LYS   A 1 260 ? 30.62452 10.71263  8.27156  1.000 42.55922  ?  260  LYS   A CD  1 
ATOM   1691 C CE  . LYS   A 1 260 ? 31.43865 9.48488   8.64166  1.000 42.24770  ?  260  LYS   A CE  1 
ATOM   1692 N NZ  . LYS   A 1 260 ? 31.95554 8.77828   7.43766  1.000 47.31632  ?  260  LYS   A NZ  1 
ATOM   1693 N N   . ILE   A 1 261 ? 27.22505 12.28916  11.61777 1.000 35.85479  ?  261  ILE   A N   1 
ATOM   1694 C CA  . ILE   A 1 261 ? 26.34433 13.42234  11.86824 1.000 35.35583  ?  261  ILE   A CA  1 
ATOM   1695 C C   . ILE   A 1 261 ? 25.88486 14.00162  10.53928 1.000 37.33599  ?  261  ILE   A C   1 
ATOM   1696 O O   . ILE   A 1 261 ? 26.70025 14.33859  9.67098  1.000 39.19543  ?  261  ILE   A O   1 
ATOM   1697 C CB  . ILE   A 1 261 ? 27.05480 14.46935  12.73679 1.000 34.71773  ?  261  ILE   A CB  1 
ATOM   1698 C CG1 . ILE   A 1 261 ? 27.21586 13.94435  14.16437 1.000 32.66084  ?  261  ILE   A CG1 1 
ATOM   1699 C CG2 . ILE   A 1 261 ? 26.28060 15.77863  12.73652 1.000 34.76367  ?  261  ILE   A CG2 1 
ATOM   1700 C CD1 . ILE   A 1 261 ? 28.40301 14.51922  14.90042 1.000 32.45748  ?  261  ILE   A CD1 1 
ATOM   1701 N N   . LEU   A 1 262 ? 24.56440 14.10796  10.37213 1.000 37.11702  ?  262  LEU   A N   1 
ATOM   1702 C CA  . LEU   A 1 262 ? 24.00501 14.48468  9.07812  1.000 39.13999  ?  262  LEU   A CA  1 
ATOM   1703 C C   . LEU   A 1 262 ? 24.36763 15.91602  8.70333  1.000 40.45270  ?  262  LEU   A C   1 
ATOM   1704 O O   . LEU   A 1 262 ? 24.73284 16.18791  7.55337  1.000 42.71349  ?  262  LEU   A O   1 
ATOM   1705 C CB  . LEU   A 1 262 ? 22.48755 14.30270  9.09316  1.000 38.62808  ?  262  LEU   A CB  1 
ATOM   1706 C CG  . LEU   A 1 262 ? 21.93762 13.06314  8.38455  1.000 39.29268  ?  262  LEU   A CG  1 
ATOM   1707 C CD1 . LEU   A 1 262 ? 22.72548 11.82126  8.77121  1.000 38.49693  ?  262  LEU   A CD1 1 
ATOM   1708 C CD2 . LEU   A 1 262 ? 20.46259 12.88041  8.69810  1.000 38.50105  ?  262  LEU   A CD2 1 
ATOM   1709 N N   . PHE   A 1 263 ? 24.27482 16.84321  9.65338  1.000 39.21607  ?  263  PHE   A N   1 
ATOM   1710 C CA  . PHE   A 1 263 ? 24.51843 18.26258  9.40237  1.000 40.41081  ?  263  PHE   A CA  1 
ATOM   1711 C C   . PHE   A 1 263 ? 25.47564 18.79715  10.45849 1.000 39.28731  ?  263  PHE   A C   1 
ATOM   1712 O O   . PHE   A 1 263 ? 25.05932 19.47185  11.41019 1.000 37.88024  ?  263  PHE   A O   1 
ATOM   1713 C CB  . PHE   A 1 263 ? 23.20501 19.04460  9.38728  1.000 40.38574  ?  263  PHE   A CB  1 
ATOM   1714 C CG  . PHE   A 1 263 ? 22.12221 18.38678  8.58024  1.000 41.15257  ?  263  PHE   A CG  1 
ATOM   1715 C CD1 . PHE   A 1 263 ? 22.21799 18.31293  7.19925  1.000 43.63806  ?  263  PHE   A CD1 1 
ATOM   1716 C CD2 . PHE   A 1 263 ? 21.01446 17.83317  9.20093  1.000 39.55607  ?  263  PHE   A CD2 1 
ATOM   1717 C CE1 . PHE   A 1 263 ? 21.22626 17.70523  6.45118  1.000 44.48389  ?  263  PHE   A CE1 1 
ATOM   1718 C CE2 . PHE   A 1 263 ? 20.01872 17.22344  8.45804  1.000 40.41673  ?  263  PHE   A CE2 1 
ATOM   1719 C CZ  . PHE   A 1 263 ? 20.12522 17.16022  7.08052  1.000 42.86710  ?  263  PHE   A CZ  1 
ATOM   1720 N N   . PRO   A 1 264 ? 26.76525 18.51743  10.32218 1.000 39.98788  ?  264  PRO   A N   1 
ATOM   1721 C CA  . PRO   A 1 264 ? 27.75156 19.01863  11.28093 1.000 39.19987  ?  264  PRO   A CA  1 
ATOM   1722 C C   . PRO   A 1 264 ? 28.13773 20.45699  10.95125 1.000 40.78456  ?  264  PRO   A C   1 
ATOM   1723 O O   . PRO   A 1 264 ? 27.70784 21.03468  9.95420  1.000 42.60166  ?  264  PRO   A O   1 
ATOM   1724 C CB  . PRO   A 1 264 ? 28.92833 18.06285  11.09235 1.000 39.72641  ?  264  PRO   A CB  1 
ATOM   1725 C CG  . PRO   A 1 264 ? 28.85270 17.68052  9.64993  1.000 41.87643  ?  264  PRO   A CG  1 
ATOM   1726 C CD  . PRO   A 1 264 ? 27.38864 17.69695  9.26761  1.000 41.68220  ?  264  PRO   A CD  1 
ATOM   1727 N N   . GLY   A 1 265 ? 28.96859 21.03194  11.81504 1.000 40.21779  ?  265  GLY   A N   1 
ATOM   1728 C CA  . GLY   A 1 265 ? 29.44339 22.38369  11.60278 1.000 42.04126  ?  265  GLY   A CA  1 
ATOM   1729 C C   . GLY   A 1 265 ? 29.87139 23.08799  12.87164 1.000 43.02043  ?  265  GLY   A C   1 
ATOM   1730 O O   . GLY   A 1 265 ? 29.38750 22.77327  13.96239 1.000 40.81179  ?  265  GLY   A O   1 
ATOM   1731 N N   . ARG   A 1 266 ? 30.78772 24.04858  12.73581 1.000 43.81931  ?  266  ARG   A N   1 
ATOM   1732 C CA  . ARG   A 1 266 ? 31.22543 24.82197  13.89230 1.000 44.86223  ?  266  ARG   A CA  1 
ATOM   1733 C C   . ARG   A 1 266 ? 30.11463 25.73476  14.39482 1.000 45.65608  ?  266  ARG   A C   1 
ATOM   1734 O O   . ARG   A 1 266 ? 29.95686 25.92388  15.60677 1.000 46.52552  ?  266  ARG   A O   1 
ATOM   1735 C CB  . ARG   A 1 266 ? 32.46853 25.63815  13.53700 1.000 46.95266  ?  266  ARG   A CB  1 
ATOM   1736 C CG  . ARG   A 1 266 ? 33.48181 24.89463  12.68111 1.000 49.17090  ?  266  ARG   A CG  1 
ATOM   1737 C CD  . ARG   A 1 266 ? 34.40520 25.85700  11.94603 1.000 53.15923  ?  266  ARG   A CD  1 
ATOM   1738 N NE  . ARG   A 1 266 ? 33.76929 26.44496  10.77253 1.000 55.44969  ?  266  ARG   A NE  1 
ATOM   1739 C CZ  . ARG   A 1 266 ? 34.28285 27.43875  10.05990 1.000 58.85706  ?  266  ARG   A CZ  1 
ATOM   1740 N NH1 . ARG   A 1 266 ? 35.44354 27.98935  10.37697 1.000 57.96390  ?  266  ARG   A NH1 1 
ATOM   1741 N NH2 . ARG   A 1 266 ? 33.61567 27.89085  9.00162  1.000 54.95501  ?  266  ARG   A NH2 1 
ATOM   1742 N N   . ASP   A 1 267 ? 29.33207 26.30064  13.47859 1.000 43.75437  ?  267  ASP   A N   1 
ATOM   1743 C CA  . ASP   A 1 267 ? 28.27973 27.24857  13.80850 1.000 45.62404  ?  267  ASP   A CA  1 
ATOM   1744 C C   . ASP   A 1 267 ? 27.09094 26.98080  12.89299 1.000 43.14895  ?  267  ASP   A C   1 
ATOM   1745 O O   . ASP   A 1 267 ? 27.10609 26.05298  12.07816 1.000 43.10836  ?  267  ASP   A O   1 
ATOM   1746 C CB  . ASP   A 1 267 ? 28.79144 28.69065  13.67662 1.000 46.05760  ?  267  ASP   A CB  1 
ATOM   1747 C CG  . ASP   A 1 267 ? 27.87450 29.70282  14.33291 1.000 47.33270  ?  267  ASP   A CG  1 
ATOM   1748 O OD1 . ASP   A 1 267 ? 28.14612 30.91666  14.21673 1.000 46.48287  ?  267  ASP   A OD1 1 
ATOM   1749 O OD2 . ASP   A 1 267 ? 26.87708 29.28414  14.95625 1.000 54.61937  -1 267  ASP   A OD2 1 
ATOM   1750 N N   . TYR   A 1 268 ? 26.04583 27.80107  13.03205 1.000 44.88708  ?  268  TYR   A N   1 
ATOM   1751 C CA  . TYR   A 1 268 ? 24.90697 27.71752  12.12542 1.000 43.43027  ?  268  TYR   A CA  1 
ATOM   1752 C C   . TYR   A 1 268 ? 25.29716 28.02458  10.68606 1.000 45.34294  ?  268  TYR   A C   1 
ATOM   1753 O O   . TYR   A 1 268 ? 24.55946 27.65870  9.76479  1.000 46.40363  ?  268  TYR   A O   1 
ATOM   1754 C CB  . TYR   A 1 268 ? 23.80140 28.67313  12.57712 1.000 41.75000  ?  268  TYR   A CB  1 
ATOM   1755 C CG  . TYR   A 1 268 ? 22.98381 28.16324  13.74140 1.000 42.24868  ?  268  TYR   A CG  1 
ATOM   1756 C CD1 . TYR   A 1 268 ? 22.82121 26.80097  13.95799 1.000 39.83783  ?  268  TYR   A CD1 1 
ATOM   1757 C CD2 . TYR   A 1 268 ? 22.37472 29.04450  14.62515 1.000 40.44382  ?  268  TYR   A CD2 1 
ATOM   1758 C CE1 . TYR   A 1 268 ? 22.07396 26.33071  15.02170 1.000 38.00112  ?  268  TYR   A CE1 1 
ATOM   1759 C CE2 . TYR   A 1 268 ? 21.62668 28.58415  15.69195 1.000 40.06713  ?  268  TYR   A CE2 1 
ATOM   1760 C CZ  . TYR   A 1 268 ? 21.47975 27.22657  15.88546 1.000 42.63108  ?  268  TYR   A CZ  1 
ATOM   1761 O OH  . TYR   A 1 268 ? 20.73528 26.76423  16.94656 1.000 40.00374  ?  268  TYR   A OH  1 
ATOM   1762 N N   . ILE   A 1 269 ? 26.43515 28.68963  10.47450 1.000 46.97694  ?  269  ILE   A N   1 
ATOM   1763 C CA  . ILE   A 1 269 ? 26.89061 28.98585  9.11975  1.000 50.17186  ?  269  ILE   A CA  1 
ATOM   1764 C C   . ILE   A 1 269 ? 27.22748 27.69703  8.37896  1.000 50.59990  ?  269  ILE   A C   1 
ATOM   1765 O O   . ILE   A 1 269 ? 26.79826 27.48593  7.23816  1.000 52.45350  ?  269  ILE   A O   1 
ATOM   1766 C CB  . ILE   A 1 269 ? 28.09284 29.94691  9.15808  1.000 51.84952  ?  269  ILE   A CB  1 
ATOM   1767 C CG1 . ILE   A 1 269 ? 27.72378 31.23785  9.89245  1.000 51.49439  ?  269  ILE   A CG1 1 
ATOM   1768 C CG2 . ILE   A 1 269 ? 28.57983 30.25110  7.74907  1.000 55.40620  ?  269  ILE   A CG2 1 
ATOM   1769 C CD1 . ILE   A 1 269 ? 26.59477 32.00922  9.24528  1.000 52.92038  ?  269  ILE   A CD1 1 
ATOM   1770 N N   . ASP   A 1 270 ? 27.99988 26.81394  9.01776  1.000 49.00551  ?  270  ASP   A N   1 
ATOM   1771 C CA  . ASP   A 1 270 ? 28.34578 25.54709  8.38333  1.000 49.33631  ?  270  ASP   A CA  1 
ATOM   1772 C C   . ASP   A 1 270 ? 27.17298 24.57514  8.38868  1.000 47.76698  ?  270  ASP   A C   1 
ATOM   1773 O O   . ASP   A 1 270 ? 27.05170 23.74842  7.47748  1.000 48.79184  ?  270  ASP   A O   1 
ATOM   1774 C CB  . ASP   A 1 270 ? 29.54887 24.91716  9.08363  1.000 48.28336  ?  270  ASP   A CB  1 
ATOM   1775 C CG  . ASP   A 1 270 ? 30.82731 25.69760  8.86662  1.000 50.35239  ?  270  ASP   A CG  1 
ATOM   1776 O OD1 . ASP   A 1 270 ? 30.91984 26.42293  7.85378  1.000 53.08199  ?  270  ASP   A OD1 1 
ATOM   1777 O OD2 . ASP   A 1 270 ? 31.74198 25.58287  9.70975  1.000 50.62443  -1 270  ASP   A OD2 1 
ATOM   1778 N N   . GLN   A 1 271 ? 26.30439 24.65699  9.39914  1.000 45.42466  ?  271  GLN   A N   1 
ATOM   1779 C CA  . GLN   A 1 271 ? 25.20351 23.70519  9.51334  1.000 43.92408  ?  271  GLN   A CA  1 
ATOM   1780 C C   . GLN   A 1 271 ? 24.19068 23.89248  8.39080  1.000 45.72726  ?  271  GLN   A C   1 
ATOM   1781 O O   . GLN   A 1 271 ? 23.79400 22.92343  7.73289  1.000 46.09941  ?  271  GLN   A O   1 
ATOM   1782 C CB  . GLN   A 1 271 ? 24.52713 23.84639  10.87677 1.000 41.25957  ?  271  GLN   A CB  1 
ATOM   1783 C CG  . GLN   A 1 271 ? 23.91040 22.55805  11.39555 1.000 39.23195  ?  271  GLN   A CG  1 
ATOM   1784 C CD  . GLN   A 1 271 ? 23.26216 22.73177  12.75353 1.000 36.82902  ?  271  GLN   A CD  1 
ATOM   1785 O OE1 . GLN   A 1 271 ? 23.85189 23.31265  13.66504 1.000 35.92970  ?  271  GLN   A OE1 1 
ATOM   1786 N NE2 . GLN   A 1 271 ? 22.04241 22.22696  12.89659 1.000 35.91321  ?  271  GLN   A NE2 1 
ATOM   1787 N N   . TRP   A 1 272 ? 23.75416 25.13450  8.16068  1.000 46.98581  ?  272  TRP   A N   1 
ATOM   1788 C CA  . TRP   A 1 272 ? 22.78729 25.38632  7.09719  1.000 48.95029  ?  272  TRP   A CA  1 
ATOM   1789 C C   . TRP   A 1 272 ? 23.35317 25.02517  5.73148  1.000 51.64742  ?  272  TRP   A C   1 
ATOM   1790 O O   . TRP   A 1 272 ? 22.59696 24.65923  4.82466  1.000 52.97564  ?  272  TRP   A O   1 
ATOM   1791 C CB  . TRP   A 1 272 ? 22.34200 26.84835  7.11726  1.000 50.04678  ?  272  TRP   A CB  1 
ATOM   1792 C CG  . TRP   A 1 272 ? 21.40944 27.19406  5.99641  1.000 52.42153  ?  272  TRP   A CG  1 
ATOM   1793 C CD1 . TRP   A 1 272 ? 21.70037 27.93016  4.88545  1.000 55.62717  ?  272  TRP   A CD1 1 
ATOM   1794 C CD2 . TRP   A 1 272 ? 20.03597 26.80473  5.87120  1.000 51.99368  ?  272  TRP   A CD2 1 
ATOM   1795 N NE1 . TRP   A 1 272 ? 20.59257 28.02856  4.07951  1.000 57.21942  ?  272  TRP   A NE1 1 
ATOM   1796 C CE2 . TRP   A 1 272 ? 19.55741 27.34602  4.66191  1.000 55.02828  ?  272  TRP   A CE2 1 
ATOM   1797 C CE3 . TRP   A 1 272 ? 19.16415 26.05401  6.66582  1.000 49.51380  ?  272  TRP   A CE3 1 
ATOM   1798 C CZ2 . TRP   A 1 272 ? 18.24650 27.16094  4.22818  1.000 55.62715  ?  272  TRP   A CZ2 1 
ATOM   1799 C CZ3 . TRP   A 1 272 ? 17.86323 25.87087  6.23334  1.000 50.11266  ?  272  TRP   A CZ3 1 
ATOM   1800 C CH2 . TRP   A 1 272 ? 17.41712 26.42171  5.02579  1.000 53.12976  ?  272  TRP   A CH2 1 
ATOM   1801 N N   . ASN   A 1 273 ? 24.67443 25.11879  5.56582  1.000 52.62141  ?  273  ASN   A N   1 
ATOM   1802 C CA  . ASN   A 1 273 ? 25.29669 24.69055  4.31780  1.000 55.18407  ?  273  ASN   A CA  1 
ATOM   1803 C C   . ASN   A 1 273 ? 25.07601 23.20155  4.08401  1.000 54.27450  ?  273  ASN   A C   1 
ATOM   1804 O O   . ASN   A 1 273 ? 24.61617 22.79066  3.01287  1.000 56.04020  ?  273  ASN   A O   1 
ATOM   1805 C CB  . ASN   A 1 273 ? 26.78991 25.01939  4.33582  1.000 56.23252  ?  273  ASN   A CB  1 
ATOM   1806 C CG  . ASN   A 1 273 ? 27.06934 26.47764  4.03106  1.000 58.47830  ?  273  ASN   A CG  1 
ATOM   1807 O OD1 . ASN   A 1 273 ? 26.15492 27.25005  3.74318  1.000 59.38572  ?  273  ASN   A OD1 1 
ATOM   1808 N ND2 . ASN   A 1 273 ? 28.33912 26.86216  4.09196  1.000 59.54060  ?  273  ASN   A ND2 1 
ATOM   1809 N N   . LYS   A 1 274 ? 25.38421 22.37620  5.08845  1.000 51.62881  ?  274  LYS   A N   1 
ATOM   1810 C CA  . LYS   A 1 274 ? 25.20776 20.93470  4.95313  1.000 50.72478  ?  274  LYS   A CA  1 
ATOM   1811 C C   . LYS   A 1 274 ? 23.74891 20.54490  4.75465  1.000 50.26115  ?  274  LYS   A C   1 
ATOM   1812 O O   . LYS   A 1 274 ? 23.47489 19.45180  4.24754  1.000 50.44500  ?  274  LYS   A O   1 
ATOM   1813 C CB  . LYS   A 1 274 ? 25.77693 20.21970  6.17931  1.000 48.03540  ?  274  LYS   A CB  1 
ATOM   1814 C CG  . LYS   A 1 274 ? 27.26077 20.46085  6.40488  1.000 48.52613  ?  274  LYS   A CG  1 
ATOM   1815 C CD  . LYS   A 1 274 ? 28.09928 19.79362  5.32743  1.000 50.66338  ?  274  LYS   A CD  1 
ATOM   1816 C CE  . LYS   A 1 274 ? 29.56127 19.71679  5.73494  1.000 50.74137  ?  274  LYS   A CE  1 
ATOM   1817 N NZ  . LYS   A 1 274 ? 30.37225 18.95126  4.74907  1.000 52.73001  ?  274  LYS   A NZ  1 
ATOM   1818 N N   . VAL   A 1 275 ? 22.80945 21.40932  5.13725  1.000 49.78781  ?  275  VAL   A N   1 
ATOM   1819 C CA  . VAL   A 1 275 ? 21.39592 21.11107  4.93426  1.000 49.60320  ?  275  VAL   A CA  1 
ATOM   1820 C C   . VAL   A 1 275 ? 21.01302 21.29159  3.47022  1.000 52.70466  ?  275  VAL   A C   1 
ATOM   1821 O O   . VAL   A 1 275 ? 20.40972 20.40373  2.85640  1.000 53.24993  ?  275  VAL   A O   1 
ATOM   1822 C CB  . VAL   A 1 275 ? 20.52824 21.98601  5.85824  1.000 48.17396  ?  275  VAL   A CB  1 
ATOM   1823 C CG1 . VAL   A 1 275 ? 19.07741 21.96429  5.40478  1.000 48.86240  ?  275  VAL   A CG1 1 
ATOM   1824 C CG2 . VAL   A 1 275 ? 20.64787 21.51758  7.30068  1.000 45.03894  ?  275  VAL   A CG2 1 
ATOM   1825 N N   . ILE   A 1 276 ? 21.36196 22.43908  2.88585  1.000 54.94145  ?  276  ILE   A N   1 
ATOM   1826 C CA  . ILE   A 1 276 ? 20.98495 22.69840  1.50024  1.000 58.16336  ?  276  ILE   A CA  1 
ATOM   1827 C C   . ILE   A 1 276 ? 21.85922 21.91014  0.53115  1.000 59.92377  ?  276  ILE   A C   1 
ATOM   1828 O O   . ILE   A 1 276 ? 21.41267 21.56696  -0.56905 1.000 62.09124  ?  276  ILE   A O   1 
ATOM   1829 C CB  . ILE   A 1 276 ? 21.03537 24.20619  1.19919  1.000 60.20854  ?  276  ILE   A CB  1 
ATOM   1830 C CG1 . ILE   A 1 276 ? 22.39076 24.79121  1.59903  1.000 60.20378  ?  276  ILE   A CG1 1 
ATOM   1831 C CG2 . ILE   A 1 276 ? 19.90629 24.92982  1.91607  1.000 58.98770  ?  276  ILE   A CG2 1 
ATOM   1832 C CD1 . ILE   A 1 276 ? 22.55646 26.24861  1.22939  1.000 62.56431  ?  276  ILE   A CD1 1 
ATOM   1833 N N   . GLU   A 1 277 ? 23.10386 21.60634  0.90892  1.000 59.16924  ?  277  GLU   A N   1 
ATOM   1834 C CA  . GLU   A 1 277 ? 23.95652 20.78976  0.05223  1.000 60.75411  ?  277  GLU   A CA  1 
ATOM   1835 C C   . GLU   A 1 277 ? 23.43821 19.36514  -0.09007 1.000 59.75755  ?  277  GLU   A C   1 
ATOM   1836 O O   . GLU   A 1 277 ? 23.86420 18.65274  -1.00533 1.000 66.25916  ?  277  GLU   A O   1 
ATOM   1837 C CB  . GLU   A 1 277 ? 25.38740 20.75932  0.59178  1.000 60.08126  ?  277  GLU   A CB  1 
ATOM   1838 C CG  . GLU   A 1 277 ? 26.16944 22.04558  0.38700  1.000 62.03821  ?  277  GLU   A CG  1 
ATOM   1839 C CD  . GLU   A 1 277 ? 27.53891 21.99537  1.03592  1.000 61.24897  ?  277  GLU   A CD  1 
ATOM   1840 O OE1 . GLU   A 1 277 ? 28.26386 23.01076  0.98216  1.000 62.74421  ?  277  GLU   A OE1 1 
ATOM   1841 O OE2 . GLU   A 1 277 ? 27.89092 20.93631  1.59852  1.000 59.27547  -1 277  GLU   A OE2 1 
ATOM   1842 N N   . GLN   A 1 278 ? 22.53526 18.93529  0.78923  1.000 57.17830  ?  278  GLN   A N   1 
ATOM   1843 C CA  . GLN   A 1 278 ? 21.97838 17.59006  0.75699  1.000 56.17426  ?  278  GLN   A CA  1 
ATOM   1844 C C   . GLN   A 1 278 ? 20.49183 17.57503  0.43576  1.000 56.58862  ?  278  GLN   A C   1 
ATOM   1845 O O   . GLN   A 1 278 ? 20.05860 16.83202  -0.45030 1.000 58.02425  ?  278  GLN   A O   1 
ATOM   1846 C CB  . GLN   A 1 278 ? 22.23251 16.88924  2.10030  1.000 52.90159  ?  278  GLN   A CB  1 
ATOM   1847 C CG  . GLN   A 1 278 ? 23.69454 16.54896  2.34651  1.000 52.59455  ?  278  GLN   A CG  1 
ATOM   1848 C CD  . GLN   A 1 278 ? 23.97933 16.19351  3.79210  1.000 49.53944  ?  278  GLN   A CD  1 
ATOM   1849 O OE1 . GLN   A 1 278 ? 24.12377 15.02128  4.13837  1.000 48.29421  ?  278  GLN   A OE1 1 
ATOM   1850 N NE2 . GLN   A 1 278 ? 24.06580 17.20828  4.64528  1.000 48.45032  ?  278  GLN   A NE2 1 
ATOM   1851 N N   . LEU   A 1 279 ? 19.69251 18.38553  1.13264  1.000 55.48651  ?  279  LEU   A N   1 
ATOM   1852 C CA  . LEU   A 1 279 ? 18.25556 18.40387  0.88341  1.000 55.94728  ?  279  LEU   A CA  1 
ATOM   1853 C C   . LEU   A 1 279 ? 17.88215 19.32625  -0.27075 1.000 59.17986  ?  279  LEU   A C   1 
ATOM   1854 O O   . LEU   A 1 279 ? 16.85957 19.10388  -0.92900 1.000 60.55533  ?  279  LEU   A O   1 
ATOM   1855 C CB  . LEU   A 1 279 ? 17.50676 18.82190  2.15015  1.000 53.45486  ?  279  LEU   A CB  1 
ATOM   1856 C CG  . LEU   A 1 279 ? 17.66225 17.90627  3.36720  1.000 50.33415  ?  279  LEU   A CG  1 
ATOM   1857 C CD1 . LEU   A 1 279 ? 16.66922 18.28582  4.45209  1.000 48.38283  ?  279  LEU   A CD1 1 
ATOM   1858 C CD2 . LEU   A 1 279 ? 17.49603 16.44569  2.97324  1.000 50.33786  ?  279  LEU   A CD2 1 
ATOM   1859 N N   . GLY   A 1 280 ? 18.67995 20.35028  -0.52895 1.000 60.58413  ?  280  GLY   A N   1 
ATOM   1860 C CA  . GLY   A 1 280 ? 18.40843 21.28207  -1.60072 1.000 63.87055  ?  280  GLY   A CA  1 
ATOM   1861 C C   . GLY   A 1 280 ? 17.92933 22.62758  -1.07834 1.000 63.74618  ?  280  GLY   A C   1 
ATOM   1862 O O   . GLY   A 1 280 ? 17.42774 22.75807  0.04213  1.000 61.16807  ?  280  GLY   A O   1 
ATOM   1863 N N   . THR   A 1 281 ? 18.09832 23.64224  -1.91786 1.000 66.74666  ?  281  THR   A N   1 
ATOM   1864 C CA  . THR   A 1 281 ? 17.64337 24.98038  -1.57349 1.000 67.16225  ?  281  THR   A CA  1 
ATOM   1865 C C   . THR   A 1 281 ? 16.12536 24.98048  -1.41625 1.000 66.76090  ?  281  THR   A C   1 
ATOM   1866 O O   . THR   A 1 281 ? 15.41709 24.45886  -2.28894 1.000 68.48658  ?  281  THR   A O   1 
ATOM   1867 C CB  . THR   A 1 281 ? 18.06701 25.98207  -2.64845 1.000 70.95551  ?  281  THR   A CB  1 
ATOM   1868 O OG1 . THR   A 1 281 ? 19.48704 26.16821  -2.59626 1.000 71.19419  ?  281  THR   A OG1 1 
ATOM   1869 C CG2 . THR   A 1 281 ? 17.37822 27.32359  -2.44010 1.000 71.82854  ?  281  THR   A CG2 1 
ATOM   1870 N N   . PRO   A 1 282 ? 15.59141 25.53284  -0.32983 1.000 64.64430  ?  282  PRO   A N   1 
ATOM   1871 C CA  . PRO   A 1 282 ? 14.13948 25.50996  -0.12687 1.000 65.99375  ?  282  PRO   A CA  1 
ATOM   1872 C C   . PRO   A 1 282 ? 13.40373 26.34643  -1.16388 1.000 71.25607  ?  282  PRO   A C   1 
ATOM   1873 O O   . PRO   A 1 282 ? 13.97784 27.19034  -1.85577 1.000 70.32049  ?  282  PRO   A O   1 
ATOM   1874 C CB  . PRO   A 1 282 ? 13.96677 26.09224  1.27984  1.000 61.78650  ?  282  PRO   A CB  1 
ATOM   1875 C CG  . PRO   A 1 282 ? 15.21046 26.88523  1.52121  1.000 61.53495  ?  282  PRO   A CG  1 
ATOM   1876 C CD  . PRO   A 1 282 ? 16.30153 26.15689  0.79942  1.000 62.49189  ?  282  PRO   A CD  1 
ATOM   1877 N N   . CYS   A 1 283 ? 12.10161 26.09237  -1.25771 1.000 79.14934  ?  283  CYS   A N   1 
ATOM   1878 C CA  . CYS   A 1 283 ? 11.24165 26.74305  -2.23126 1.000 81.56189  ?  283  CYS   A CA  1 
ATOM   1879 C C   . CYS   A 1 283 ? 10.91078 28.16979  -1.79442 1.000 82.03913  ?  283  CYS   A C   1 
ATOM   1880 O O   . CYS   A 1 283 ? 11.03945 28.51403  -0.61638 1.000 77.76670  ?  283  CYS   A O   1 
ATOM   1881 C CB  . CYS   A 1 283 ? 9.96642  25.92416  -2.41741 1.000 79.58300  ?  283  CYS   A CB  1 
ATOM   1882 S SG  . CYS   A 1 283 ? 8.56547  26.46857  -1.42143 1.000 100.15080 ?  283  CYS   A SG  1 
ATOM   1883 N N   . PRO   A 1 284 ? 10.49044 29.02774  -2.73250 1.000 75.44141  ?  284  PRO   A N   1 
ATOM   1884 C CA  . PRO   A 1 284 ? 10.23783 30.43468  -2.37162 1.000 76.18885  ?  284  PRO   A CA  1 
ATOM   1885 C C   . PRO   A 1 284 ? 9.13798  30.62597  -1.34095 1.000 74.49069  ?  284  PRO   A C   1 
ATOM   1886 O O   . PRO   A 1 284 ? 9.17344  31.61506  -0.59787 1.000 75.82601  ?  284  PRO   A O   1 
ATOM   1887 C CB  . PRO   A 1 284 ? 9.86716  31.08162  -3.71552 1.000 80.75088  ?  284  PRO   A CB  1 
ATOM   1888 C CG  . PRO   A 1 284 ? 9.48590  29.94437  -4.60736 1.000 81.97448  ?  284  PRO   A CG  1 
ATOM   1889 C CD  . PRO   A 1 284 ? 10.35094 28.80464  -4.18138 1.000 79.14473  ?  284  PRO   A CD  1 
ATOM   1890 N N   . GLU   A 1 285 ? 8.15497  29.72402  -1.27508 1.000 73.29335  ?  285  GLU   A N   1 
ATOM   1891 C CA  . GLU   A 1 285 ? 7.12155  29.84667  -0.25061 1.000 73.52851  ?  285  GLU   A CA  1 
ATOM   1892 C C   . GLU   A 1 285 ? 7.72704  29.76972  1.14558  1.000 71.97597  ?  285  GLU   A C   1 
ATOM   1893 O O   . GLU   A 1 285 ? 7.30133  30.48837  2.05788  1.000 73.11061  ?  285  GLU   A O   1 
ATOM   1894 C CB  . GLU   A 1 285 ? 6.05768  28.76525  -0.44003 1.000 74.35748  ?  285  GLU   A CB  1 
ATOM   1895 N N   . PHE   A 1 286 ? 8.72807  28.90486  1.32744  1.000 68.63013  ?  286  PHE   A N   1 
ATOM   1896 C CA  . PHE   A 1 286 ? 9.47144  28.87354  2.58192  1.000 69.69159  ?  286  PHE   A CA  1 
ATOM   1897 C C   . PHE   A 1 286 ? 10.35023 30.10802  2.73531  1.000 68.33642  ?  286  PHE   A C   1 
ATOM   1898 O O   . PHE   A 1 286 ? 10.58639 30.56344  3.86087  1.000 65.15496  ?  286  PHE   A O   1 
ATOM   1899 C CB  . PHE   A 1 286 ? 10.31128 27.59420  2.64889  1.000 62.07999  ?  286  PHE   A CB  1 
ATOM   1900 C CG  . PHE   A 1 286 ? 11.25848 27.53488  3.81808  1.000 57.56009  ?  286  PHE   A CG  1 
ATOM   1901 C CD1 . PHE   A 1 286 ? 12.54334 28.04838  3.71988  1.000 57.94049  ?  286  PHE   A CD1 1 
ATOM   1902 C CD2 . PHE   A 1 286 ? 10.87040 26.94478  5.00858  1.000 54.51199  ?  286  PHE   A CD2 1 
ATOM   1903 C CE1 . PHE   A 1 286 ? 13.41480 27.98781  4.78906  1.000 55.31947  ?  286  PHE   A CE1 1 
ATOM   1904 C CE2 . PHE   A 1 286 ? 11.73934 26.87882  6.08137  1.000 51.89960  ?  286  PHE   A CE2 1 
ATOM   1905 C CZ  . PHE   A 1 286 ? 13.01233 27.40310  5.97158  1.000 52.29143  ?  286  PHE   A CZ  1 
ATOM   1906 N N   . MET   A 1 287 ? 10.84160 30.65475  1.61981  1.000 69.62119  ?  287  MET   A N   1 
ATOM   1907 C CA  . MET   A 1 287 ? 11.70090 31.83383  1.67181  1.000 70.71363  ?  287  MET   A CA  1 
ATOM   1908 C C   . MET   A 1 287 ? 10.97016 33.01752  2.29150  1.000 72.31914  ?  287  MET   A C   1 
ATOM   1909 O O   . MET   A 1 287 ? 11.46795 33.64719  3.23206  1.000 68.43271  ?  287  MET   A O   1 
ATOM   1910 C CB  . MET   A 1 287 ? 12.18161 32.18814  0.26393  1.000 70.90045  ?  287  MET   A CB  1 
ATOM   1911 C CG  . MET   A 1 287 ? 13.35031 31.36198  -0.24202 1.000 72.09260  ?  287  MET   A CG  1 
ATOM   1912 S SD  . MET   A 1 287 ? 14.53669 30.87521  1.02117  1.000 67.07049  ?  287  MET   A SD  1 
ATOM   1913 C CE  . MET   A 1 287 ? 16.01456 30.76609  0.01545  1.000 69.42245  ?  287  MET   A CE  1 
ATOM   1914 N N   . LYS   A 1 288 ? 9.77656  33.32939  1.77665  1.000 86.96736  ?  288  LYS   A N   1 
ATOM   1915 C CA  . LYS   A 1 288 ? 9.04288  34.50562  2.23027  1.000 84.77634  ?  288  LYS   A CA  1 
ATOM   1916 C C   . LYS   A 1 288 ? 8.64011  34.41046  3.69633  1.000 83.13651  ?  288  LYS   A C   1 
ATOM   1917 O O   . LYS   A 1 288 ? 8.32846  35.43786  4.30800  1.000 87.32295  ?  288  LYS   A O   1 
ATOM   1918 C CB  . LYS   A 1 288 ? 7.81403  34.72632  1.33463  1.000 86.01797  ?  288  LYS   A CB  1 
ATOM   1919 C CG  . LYS   A 1 288 ? 6.61405  33.80954  1.59381  1.000 87.78735  ?  288  LYS   A CG  1 
ATOM   1920 C CD  . LYS   A 1 288 ? 5.65826  34.37516  2.64211  1.000 89.45739  ?  288  LYS   A CD  1 
ATOM   1921 C CE  . LYS   A 1 288 ? 4.39179  33.55301  2.74130  1.000 91.94582  ?  288  LYS   A CE  1 
ATOM   1922 N NZ  . LYS   A 1 288 ? 3.21714  34.39323  3.09990  1.000 94.08915  ?  288  LYS   A NZ  1 
ATOM   1923 N N   . LYS   A 1 289 ? 8.63368  33.20973  4.27358  1.000 74.72169  ?  289  LYS   A N   1 
ATOM   1924 C CA  . LYS   A 1 289 ? 8.29631  33.04607  5.68181  1.000 73.05250  ?  289  LYS   A CA  1 
ATOM   1925 C C   . LYS   A 1 289 ? 9.43371  33.44168  6.61419  1.000 67.30724  ?  289  LYS   A C   1 
ATOM   1926 O O   . LYS   A 1 289 ? 9.25892  33.38392  7.83571  1.000 64.31859  ?  289  LYS   A O   1 
ATOM   1927 C CB  . LYS   A 1 289 ? 7.87983  31.59870  5.95850  1.000 72.73015  ?  289  LYS   A CB  1 
ATOM   1928 C CG  . LYS   A 1 289 ? 6.38039  31.34785  5.86071  1.000 77.37211  ?  289  LYS   A CG  1 
ATOM   1929 C CD  . LYS   A 1 289 ? 5.58350  32.48163  6.49036  1.000 80.42724  ?  289  LYS   A CD  1 
ATOM   1930 C CE  . LYS   A 1 289 ? 4.11390  32.11520  6.64175  1.000 83.44124  ?  289  LYS   A CE  1 
ATOM   1931 N NZ  . LYS   A 1 289 ? 3.41971  31.96377  5.33482  1.000 85.43934  ?  289  LYS   A NZ  1 
ATOM   1932 N N   . LEU   A 1 290 ? 10.58064 33.83999  6.07608  1.000 69.08025  ?  290  LEU   A N   1 
ATOM   1933 C CA  . LEU   A 1 290 ? 11.72130 34.24643  6.88039  1.000 65.38253  ?  290  LEU   A CA  1 
ATOM   1934 C C   . LEU   A 1 290 ? 11.67845 35.74496  7.16220  1.000 63.46435  ?  290  LEU   A C   1 
ATOM   1935 O O   . LEU   A 1 290 ? 11.03704 36.52057  6.44977  1.000 61.32068  ?  290  LEU   A O   1 
ATOM   1936 C CB  . LEU   A 1 290 ? 13.03101 33.89245  6.17424  1.000 60.96312  ?  290  LEU   A CB  1 
ATOM   1937 C CG  . LEU   A 1 290 ? 13.37484 32.41085  6.03029  1.000 59.31057  ?  290  LEU   A CG  1 
ATOM   1938 C CD1 . LEU   A 1 290 ? 14.10120 32.15463  4.71911  1.000 59.68022  ?  290  LEU   A CD1 1 
ATOM   1939 C CD2 . LEU   A 1 290 ? 14.21804 31.95842  7.20573  1.000 56.14685  ?  290  LEU   A CD2 1 
ATOM   1940 N N   . GLN   A 1 291 ? 12.37353 36.14393  8.22385  1.000 61.32983  ?  291  GLN   A N   1 
ATOM   1941 C CA  . GLN   A 1 291 ? 12.56499 37.55717  8.49248  1.000 60.94614  ?  291  GLN   A CA  1 
ATOM   1942 C C   . GLN   A 1 291 ? 13.42698 38.17333  7.39092  1.000 60.88479  ?  291  GLN   A C   1 
ATOM   1943 O O   . GLN   A 1 291 ? 14.30948 37.50816  6.84367  1.000 61.23091  ?  291  GLN   A O   1 
ATOM   1944 C CB  . GLN   A 1 291 ? 13.22444 37.75984  9.85427  1.000 61.86104  ?  291  GLN   A CB  1 
ATOM   1945 C CG  . GLN   A 1 291 ? 12.36524 37.32461  11.03266 1.000 65.10391  ?  291  GLN   A CG  1 
ATOM   1946 C CD  . GLN   A 1 291 ? 11.19481 38.25807  11.27883 1.000 70.75691  ?  291  GLN   A CD  1 
ATOM   1947 O OE1 . GLN   A 1 291 ? 11.32790 39.47857  11.18607 1.000 65.85065  ?  291  GLN   A OE1 1 
ATOM   1948 N NE2 . GLN   A 1 291 ? 10.03853 37.68604  11.59468 1.000 73.26263  ?  291  GLN   A NE2 1 
ATOM   1949 N N   . PRO   A 1 292 ? 13.19069 39.44405  7.04773  1.000 63.40290  ?  292  PRO   A N   1 
ATOM   1950 C CA  . PRO   A 1 292 ? 13.88415 40.02853  5.88495  1.000 66.95792  ?  292  PRO   A CA  1 
ATOM   1951 C C   . PRO   A 1 292 ? 15.39970 39.97911  5.97995  1.000 66.66388  ?  292  PRO   A C   1 
ATOM   1952 O O   . PRO   A 1 292 ? 16.06740 39.81221  4.95139  1.000 68.98769  ?  292  PRO   A O   1 
ATOM   1953 C CB  . PRO   A 1 292 ? 13.37018 41.47619  5.85915  1.000 69.15073  ?  292  PRO   A CB  1 
ATOM   1954 C CG  . PRO   A 1 292 ? 12.83649 41.72741  7.23617  1.000 66.21095  ?  292  PRO   A CG  1 
ATOM   1955 C CD  . PRO   A 1 292 ? 12.29810 40.41325  7.70311  1.000 63.29380  ?  292  PRO   A CD  1 
ATOM   1956 N N   . THR   A 1 293 ? 15.96587 40.11125  7.18116  1.000 64.01593  ?  293  THR   A N   1 
ATOM   1957 C CA  . THR   A 1 293 ? 17.41733 40.05501  7.32417  1.000 63.77637  ?  293  THR   A CA  1 
ATOM   1958 C C   . THR   A 1 293 ? 17.94635 38.65932  7.01357  1.000 62.64206  ?  293  THR   A C   1 
ATOM   1959 O O   . THR   A 1 293 ? 18.83057 38.49399  6.16519  1.000 64.59395  ?  293  THR   A O   1 
ATOM   1960 C CB  . THR   A 1 293 ? 17.82348 40.48345  8.73444  1.000 61.19105  ?  293  THR   A CB  1 
ATOM   1961 O OG1 . THR   A 1 293 ? 17.50885 41.86846  8.92518  1.000 62.68609  ?  293  THR   A OG1 1 
ATOM   1962 C CG2 . THR   A 1 293 ? 19.31474 40.27121  8.94637  1.000 60.75503  ?  293  THR   A CG2 1 
ATOM   1963 N N   . VAL   A 1 294 ? 17.41389 37.63873  7.69116  1.000 59.62370  ?  294  VAL   A N   1 
ATOM   1964 C CA  . VAL   A 1 294 ? 17.86942 36.27337  7.45679  1.000 59.80183  ?  294  VAL   A CA  1 
ATOM   1965 C C   . VAL   A 1 294 ? 17.41045 35.75405  6.09910  1.000 60.84518  ?  294  VAL   A C   1 
ATOM   1966 O O   . VAL   A 1 294 ? 18.04728 34.85586  5.53498  1.000 61.11446  ?  294  VAL   A O   1 
ATOM   1967 C CB  . VAL   A 1 294 ? 17.39718 35.35047  8.59910  1.000 54.73890  ?  294  VAL   A CB  1 
ATOM   1968 C CG1 . VAL   A 1 294 ? 15.88953 35.14365  8.54385  1.000 54.49476  ?  294  VAL   A CG1 1 
ATOM   1969 C CG2 . VAL   A 1 294 ? 18.13380 34.01725  8.55664  1.000 53.37309  ?  294  VAL   A CG2 1 
ATOM   1970 N N   . ARG   A 1 295 ? 16.32392 36.30416  5.55043  1.000 62.72867  ?  295  ARG   A N   1 
ATOM   1971 C CA  . ARG   A 1 295 ? 15.88926 35.90569  4.21569  1.000 65.38350  ?  295  ARG   A CA  1 
ATOM   1972 C C   . ARG   A 1 295 ? 16.91443 36.30963  3.16414  1.000 68.58546  ?  295  ARG   A C   1 
ATOM   1973 O O   . ARG   A 1 295 ? 17.15263 35.57159  2.20123  1.000 70.03455  ?  295  ARG   A O   1 
ATOM   1974 C CB  . ARG   A 1 295 ? 14.52263 36.51997  3.90624  1.000 66.94286  ?  295  ARG   A CB  1 
ATOM   1975 C CG  . ARG   A 1 295 ? 14.21896 36.68965  2.42777  1.000 70.88653  ?  295  ARG   A CG  1 
ATOM   1976 C CD  . ARG   A 1 295 ? 12.78411 36.30433  2.11005  1.000 71.30324  ?  295  ARG   A CD  1 
ATOM   1977 N NE  . ARG   A 1 295 ? 11.83851 36.90829  3.04135  1.000 70.19712  ?  295  ARG   A NE  1 
ATOM   1978 C CZ  . ARG   A 1 295 ? 10.82438 37.68360  2.68176  1.000 72.07505  ?  295  ARG   A CZ  1 
ATOM   1979 N NH1 . ARG   A 1 295 ? 10.58373 37.96211  1.41069  1.000 75.82155  ?  295  ARG   A NH1 1 
ATOM   1980 N NH2 . ARG   A 1 295 ? 10.03102 38.19164  3.62077  1.000 70.58986  ?  295  ARG   A NH2 1 
ATOM   1981 N N   . ASN   A 1 296 ? 17.54489 37.47261  3.34184  1.000 69.82682  ?  296  ASN   A N   1 
ATOM   1982 C CA  . ASN   A 1 296 ? 18.53049 37.93709  2.37136  1.000 73.13998  ?  296  ASN   A CA  1 
ATOM   1983 C C   . ASN   A 1 296 ? 19.77566 37.05875  2.37811  1.000 72.15209  ?  296  ASN   A C   1 
ATOM   1984 O O   . ASN   A 1 296 ? 20.29144 36.69881  1.31393  1.000 74.53217  ?  296  ASN   A O   1 
ATOM   1985 C CB  . ASN   A 1 296 ? 18.89948 39.39287  2.65551  1.000 74.65190  ?  296  ASN   A CB  1 
ATOM   1986 C CG  . ASN   A 1 296 ? 20.12194 39.84554  1.88192  1.000 77.71903  ?  296  ASN   A CG  1 
ATOM   1987 O OD1 . ASN   A 1 296 ? 21.24604 39.77918  2.37950  1.000 76.69178  ?  296  ASN   A OD1 1 
ATOM   1988 N ND2 . ASN   A 1 296 ? 19.90760 40.31077  0.65649  1.000 81.69014  ?  296  ASN   A ND2 1 
ATOM   1989 N N   . TYR   A 1 297 ? 20.27529 36.70672  3.56557  1.000 68.80277  ?  297  TYR   A N   1 
ATOM   1990 C CA  . TYR   A 1 297 ? 21.47511 35.87875  3.64533  1.000 67.85643  ?  297  TYR   A CA  1 
ATOM   1991 C C   . TYR   A 1 297 ? 21.23540 34.49941  3.04774  1.000 67.39225  ?  297  TYR   A C   1 
ATOM   1992 O O   . TYR   A 1 297 ? 22.07827 33.97907  2.30732  1.000 68.83746  ?  297  TYR   A O   1 
ATOM   1993 C CB  . TYR   A 1 297 ? 21.93671 35.75367  5.09825  1.000 64.34686  ?  297  TYR   A CB  1 
ATOM   1994 C CG  . TYR   A 1 297 ? 22.81559 34.54747  5.35515  1.000 62.52184  ?  297  TYR   A CG  1 
ATOM   1995 C CD1 . TYR   A 1 297 ? 22.30214 33.40151  5.95134  1.000 59.51275  ?  297  TYR   A CD1 1 
ATOM   1996 C CD2 . TYR   A 1 297 ? 24.15762 34.55382  4.99808  1.000 63.98526  ?  297  TYR   A CD2 1 
ATOM   1997 C CE1 . TYR   A 1 297 ? 23.10105 32.29748  6.18415  1.000 60.78692  ?  297  TYR   A CE1 1 
ATOM   1998 C CE2 . TYR   A 1 297 ? 24.96426 33.45469  5.22803  1.000 62.46171  ?  297  TYR   A CE2 1 
ATOM   1999 C CZ  . TYR   A 1 297 ? 24.43074 32.32967  5.82106  1.000 62.51629  ?  297  TYR   A CZ  1 
ATOM   2000 O OH  . TYR   A 1 297 ? 25.22914 31.23254  6.05240  1.000 61.75650  ?  297  TYR   A OH  1 
ATOM   2001 N N   . VAL   A 1 298 ? 20.08999 33.89132  3.35857  1.000 65.50164  ?  298  VAL   A N   1 
ATOM   2002 C CA  . VAL   A 1 298 ? 19.82217 32.53559  2.89272  1.000 64.86762  ?  298  VAL   A CA  1 
ATOM   2003 C C   . VAL   A 1 298 ? 19.54489 32.53196  1.39275  1.000 68.50034  ?  298  VAL   A C   1 
ATOM   2004 O O   . VAL   A 1 298 ? 19.99839 31.63888  0.66679  1.000 69.31525  ?  298  VAL   A O   1 
ATOM   2005 C CB  . VAL   A 1 298 ? 18.66540 31.92132  3.70464  1.000 61.95356  ?  298  VAL   A CB  1 
ATOM   2006 C CG1 . VAL   A 1 298 ? 17.93647 30.86462  2.90404  1.000 64.48163  ?  298  VAL   A CG1 1 
ATOM   2007 C CG2 . VAL   A 1 298 ? 19.18919 31.33654  5.00986  1.000 58.34637  ?  298  VAL   A CG2 1 
ATOM   2008 N N   . GLU   A 1 299 ? 18.81769 33.53883  0.89894  1.000 70.89751  ?  299  GLU   A N   1 
ATOM   2009 C CA  . GLU   A 1 299 ? 18.58030 33.65096  -0.53625 1.000 74.73899  ?  299  GLU   A CA  1 
ATOM   2010 C C   . GLU   A 1 299 ? 19.85599 33.95406  -1.31171 1.000 77.49408  ?  299  GLU   A C   1 
ATOM   2011 O O   . GLU   A 1 299 ? 19.93236 33.63488  -2.50300 1.000 80.31531  ?  299  GLU   A O   1 
ATOM   2012 C CB  . GLU   A 1 299 ? 17.53945 34.73457  -0.82407 1.000 76.83164  ?  299  GLU   A CB  1 
ATOM   2013 C CG  . GLU   A 1 299 ? 16.09934 34.25567  -0.74135 1.000 75.83557  ?  299  GLU   A CG  1 
ATOM   2014 C CD  . GLU   A 1 299 ? 15.10665 35.39604  -0.63261 1.000 77.09475  ?  299  GLU   A CD  1 
ATOM   2015 O OE1 . GLU   A 1 299 ? 15.54413 36.56373  -0.55402 1.000 78.54168  ?  299  GLU   A OE1 1 
ATOM   2016 O OE2 . GLU   A 1 299 ? 13.88734 35.12421  -0.62015 1.000 76.73926  -1 299  GLU   A OE2 1 
ATOM   2017 N N   . ASN   A 1 300 ? 20.85308 34.56218  -0.67103 1.000 76.90257  ?  300  ASN   A N   1 
ATOM   2018 C CA  . ASN   A 1 300 ? 22.11094 34.89459  -1.32672 1.000 79.58212  ?  300  ASN   A CA  1 
ATOM   2019 C C   . ASN   A 1 300 ? 23.10316 33.74058  -1.32972 1.000 78.35105  ?  300  ASN   A C   1 
ATOM   2020 O O   . ASN   A 1 300 ? 24.22582 33.91077  -1.81529 1.000 80.42850  ?  300  ASN   A O   1 
ATOM   2021 C CB  . ASN   A 1 300 ? 22.74683 36.11738  -0.66010 1.000 79.82578  ?  300  ASN   A CB  1 
ATOM   2022 C CG  . ASN   A 1 300 ? 22.50374 37.39516  -1.43725 1.000 83.79995  ?  300  ASN   A CG  1 
ATOM   2023 O OD1 . ASN   A 1 300 ? 21.37003 37.71162  -1.79579 1.000 84.84657  ?  300  ASN   A OD1 1 
ATOM   2024 N ND2 . ASN   A 1 300 ? 23.57250 38.13759  -1.70333 1.000 86.21165  ?  300  ASN   A ND2 1 
ATOM   2025 N N   . ARG   A 1 301 ? 22.72426 32.58415  -0.79858 1.000 75.19147  ?  301  ARG   A N   1 
ATOM   2026 C CA  . ARG   A 1 301 ? 23.57788 31.41122  -0.84032 1.000 75.49840  ?  301  ARG   A CA  1 
ATOM   2027 C C   . ARG   A 1 301 ? 23.45532 30.71901  -2.19428 1.000 76.85917  ?  301  ARG   A C   1 
ATOM   2028 O O   . ARG   A 1 301 ? 22.45433 30.88304  -2.89659 1.000 78.43847  ?  301  ARG   A O   1 
ATOM   2029 C CB  . ARG   A 1 301 ? 23.20310 30.45039  0.28457  1.000 73.91515  ?  301  ARG   A CB  1 
ATOM   2030 C CG  . ARG   A 1 301 ? 23.82335 30.79732  1.62992  1.000 69.97373  ?  301  ARG   A CG  1 
ATOM   2031 C CD  . ARG   A 1 301 ? 25.32540 30.55820  1.62410  1.000 72.79203  ?  301  ARG   A CD  1 
ATOM   2032 N NE  . ARG   A 1 301 ? 26.04100 31.55276  2.41465  1.000 74.84399  ?  301  ARG   A NE  1 
ATOM   2033 C CZ  . ARG   A 1 301 ? 27.18570 31.32717  3.04507  1.000 71.83659  ?  301  ARG   A CZ  1 
ATOM   2034 N NH1 . ARG   A 1 301 ? 27.78021 30.14625  2.99736  1.000 69.08842  ?  301  ARG   A NH1 1 
ATOM   2035 N NH2 . ARG   A 1 301 ? 27.74856 32.31147  3.74040  1.000 69.26754  ?  301  ARG   A NH2 1 
ATOM   2036 N N   . PRO   A 1 302 ? 24.47168 29.95291  -2.59429 1.000 91.45081  ?  302  PRO   A N   1 
ATOM   2037 C CA  . PRO   A 1 302 ? 24.38719 29.23076  -3.86998 1.000 85.98971  ?  302  PRO   A CA  1 
ATOM   2038 C C   . PRO   A 1 302 ? 23.22341 28.25047  -3.88011 1.000 86.30188  ?  302  PRO   A C   1 
ATOM   2039 O O   . PRO   A 1 302 ? 22.91030 27.61553  -2.87082 1.000 81.72954  ?  302  PRO   A O   1 
ATOM   2040 C CB  . PRO   A 1 302 ? 25.73491 28.50606  -3.95773 1.000 83.32782  ?  302  PRO   A CB  1 
ATOM   2041 C CG  . PRO   A 1 302 ? 26.65036 29.30611  -3.09759 1.000 85.60837  ?  302  PRO   A CG  1 
ATOM   2042 C CD  . PRO   A 1 302 ? 25.80206 29.82356  -1.97441 1.000 89.88137  ?  302  PRO   A CD  1 
ATOM   2043 N N   . LYS   A 1 303 ? 22.58065 28.13539  -5.03959 1.000 80.83666  ?  303  LYS   A N   1 
ATOM   2044 C CA  . LYS   A 1 303 ? 21.42393 27.26362  -5.18679 1.000 79.80421  ?  303  LYS   A CA  1 
ATOM   2045 C C   . LYS   A 1 303 ? 21.87186 25.82098  -5.38355 1.000 78.77127  ?  303  LYS   A C   1 
ATOM   2046 O O   . LYS   A 1 303 ? 22.73567 25.53655  -6.21946 1.000 81.02052  ?  303  LYS   A O   1 
ATOM   2047 C CB  . LYS   A 1 303 ? 20.56264 27.71429  -6.36625 1.000 83.43286  ?  303  LYS   A CB  1 
ATOM   2048 C CG  . LYS   A 1 303 ? 19.93335 29.08750  -6.19175 1.000 84.53929  ?  303  LYS   A CG  1 
ATOM   2049 C CD  . LYS   A 1 303 ? 18.56160 28.99142  -5.54280 1.000 82.33616  ?  303  LYS   A CD  1 
ATOM   2050 C CE  . LYS   A 1 303 ? 18.19875 30.28192  -4.82424 1.000 81.92112  ?  303  LYS   A CE  1 
ATOM   2051 N NZ  . LYS   A 1 303 ? 16.72521 30.48143  -4.74084 1.000 81.82261  ?  303  LYS   A NZ  1 
ATOM   2052 N N   . TYR   A 1 304 ? 21.28200 24.91314  -4.61126 1.000 75.50108  ?  304  TYR   A N   1 
ATOM   2053 C CA  . TYR   A 1 304 ? 21.55087 23.48745  -4.71538 1.000 74.32851  ?  304  TYR   A CA  1 
ATOM   2054 C C   . TYR   A 1 304 ? 20.26516 22.75376  -5.06320 1.000 74.21941  ?  304  TYR   A C   1 
ATOM   2055 O O   . TYR   A 1 304 ? 19.20049 23.05433  -4.51516 1.000 72.91618  ?  304  TYR   A O   1 
ATOM   2056 C CB  . TYR   A 1 304 ? 22.12609 22.93030  -3.40836 1.000 70.52199  ?  304  TYR   A CB  1 
ATOM   2057 C CG  . TYR   A 1 304 ? 23.50837 23.43744  -3.06969 1.000 70.61716  ?  304  TYR   A CG  1 
ATOM   2058 C CD1 . TYR   A 1 304 ? 24.63933 22.85235  -3.62371 1.000 71.89315  ?  304  TYR   A CD1 1 
ATOM   2059 C CD2 . TYR   A 1 304 ? 23.68277 24.49758  -2.19021 1.000 69.53939  ?  304  TYR   A CD2 1 
ATOM   2060 C CE1 . TYR   A 1 304 ? 25.90535 23.31160  -3.31350 1.000 72.15701  ?  304  TYR   A CE1 1 
ATOM   2061 C CE2 . TYR   A 1 304 ? 24.94431 24.96382  -1.87385 1.000 70.76354  ?  304  TYR   A CE2 1 
ATOM   2062 C CZ  . TYR   A 1 304 ? 26.05184 24.36715  -2.43826 1.000 71.85987  ?  304  TYR   A CZ  1 
ATOM   2063 O OH  . TYR   A 1 304 ? 27.31005 24.82814  -2.12592 1.000 74.85134  ?  304  TYR   A OH  1 
ATOM   2064 N N   . ALA   A 1 305 ? 20.36766 21.79367  -5.98143 1.000 75.72698  ?  305  ALA   A N   1 
ATOM   2065 C CA  . ALA   A 1 305 ? 19.21746 20.97263  -6.33344 1.000 75.71388  ?  305  ALA   A CA  1 
ATOM   2066 C C   . ALA   A 1 305 ? 18.88083 19.95037  -5.25876 1.000 72.04639  ?  305  ALA   A C   1 
ATOM   2067 O O   . ALA   A 1 305 ? 17.72473 19.52391  -5.16787 1.000 71.26650  ?  305  ALA   A O   1 
ATOM   2068 C CB  . ALA   A 1 305 ? 19.46374 20.25724  -7.66332 1.000 78.65997  ?  305  ALA   A CB  1 
ATOM   2069 N N   . GLY   A 1 306 ? 19.85551 19.55767  -4.44404 1.000 69.58938  ?  306  GLY   A N   1 
ATOM   2070 C CA  . GLY   A 1 306 ? 19.63038 18.55457  -3.42531 1.000 66.20058  ?  306  GLY   A CA  1 
ATOM   2071 C C   . GLY   A 1 306 ? 19.74588 17.14368  -3.95912 1.000 66.66898  ?  306  GLY   A C   1 
ATOM   2072 O O   . GLY   A 1 306 ? 19.23708 16.83701  -5.04159 1.000 74.78134  ?  306  GLY   A O   1 
ATOM   2073 N N   . LEU   A 1 307 ? 20.41701 16.27667  -3.20879 1.000 65.16384  ?  307  LEU   A N   1 
ATOM   2074 C CA  . LEU   A 1 307 ? 20.57701 14.89106  -3.61739 1.000 64.47661  ?  307  LEU   A CA  1 
ATOM   2075 C C   . LEU   A 1 307 ? 19.32378 14.09457  -3.27849 1.000 66.92976  ?  307  LEU   A C   1 
ATOM   2076 O O   . LEU   A 1 307 ? 18.65970 14.34028  -2.26728 1.000 64.94244  ?  307  LEU   A O   1 
ATOM   2077 C CB  . LEU   A 1 307 ? 21.79414 14.25903  -2.93812 1.000 64.40118  ?  307  LEU   A CB  1 
ATOM   2078 C CG  . LEU   A 1 307 ? 23.21112 14.49941  -3.47872 1.000 66.23834  ?  307  LEU   A CG  1 
ATOM   2079 C CD1 . LEU   A 1 307 ? 23.41037 15.90448  -4.04182 1.000 72.41631  ?  307  LEU   A CD1 1 
ATOM   2080 C CD2 . LEU   A 1 307 ? 24.24204 14.20599  -2.39711 1.000 62.75814  ?  307  LEU   A CD2 1 
ATOM   2081 N N   . THR   A 1 308 ? 19.00077 13.13419  -4.14003 1.000 64.68661  ?  308  THR   A N   1 
ATOM   2082 C CA  . THR   A 1 308 ? 17.84961 12.28240  -3.89229 1.000 63.20332  ?  308  THR   A CA  1 
ATOM   2083 C C   . THR   A 1 308 ? 18.10533 11.38666  -2.68210 1.000 59.98840  ?  308  THR   A C   1 
ATOM   2084 O O   . THR   A 1 308 ? 19.24666 11.15238  -2.27411 1.000 59.65776  ?  308  THR   A O   1 
ATOM   2085 C CB  . THR   A 1 308 ? 17.52326 11.43921  -5.12707 1.000 65.71022  ?  308  THR   A CB  1 
ATOM   2086 O OG1 . THR   A 1 308 ? 16.25047 10.80373  -4.95240 1.000 68.44905  ?  308  THR   A OG1 1 
ATOM   2087 C CG2 . THR   A 1 308 ? 18.58670 10.37996  -5.35484 1.000 65.68721  ?  308  THR   A CG2 1 
ATOM   2088 N N   . PHE   A 1 309 ? 17.01869 10.89207  -2.10040 1.000 59.25863  ?  309  PHE   A N   1 
ATOM   2089 C CA  . PHE   A 1 309 ? 17.10151 10.13211  -0.85882 1.000 58.01313  ?  309  PHE   A CA  1 
ATOM   2090 C C   . PHE   A 1 309 ? 17.72739 8.75096   -1.05114 1.000 59.16065  ?  309  PHE   A C   1 
ATOM   2091 O O   . PHE   A 1 309 ? 18.43135 8.27868   -0.14921 1.000 59.21548  ?  309  PHE   A O   1 
ATOM   2092 C CB  . PHE   A 1 309 ? 15.71720 10.02300  -0.21597 1.000 54.44873  ?  309  PHE   A CB  1 
ATOM   2093 C CG  . PHE   A 1 309 ? 15.42324 11.13157  0.75441  1.000 52.82003  ?  309  PHE   A CG  1 
ATOM   2094 C CD1 . PHE   A 1 309 ? 15.87906 11.06489  2.06084  1.000 50.09182  ?  309  PHE   A CD1 1 
ATOM   2095 C CD2 . PHE   A 1 309 ? 14.71519 12.25278  0.35345  1.000 54.20244  ?  309  PHE   A CD2 1 
ATOM   2096 C CE1 . PHE   A 1 309 ? 15.62120 12.08814  2.95403  1.000 48.71021  ?  309  PHE   A CE1 1 
ATOM   2097 C CE2 . PHE   A 1 309 ? 14.45478 13.28038  1.24201  1.000 52.81836  ?  309  PHE   A CE2 1 
ATOM   2098 C CZ  . PHE   A 1 309 ? 14.90959 13.19781  2.54425  1.000 50.04156  ?  309  PHE   A CZ  1 
ATOM   2099 N N   . PRO   A 1 310 ? 17.50576 8.05946   -2.17579 1.000 60.99752  ?  310  PRO   A N   1 
ATOM   2100 C CA  . PRO   A 1 310 ? 18.32126 6.86306   -2.44785 1.000 60.82045  ?  310  PRO   A CA  1 
ATOM   2101 C C   . PRO   A 1 310 ? 19.80410 7.15967   -2.59855 1.000 61.86431  ?  310  PRO   A C   1 
ATOM   2102 O O   . PRO   A 1 310 ? 20.61874 6.23956   -2.45868 1.000 60.49102  ?  310  PRO   A O   1 
ATOM   2103 C CB  . PRO   A 1 310 ? 17.72047 6.30546   -3.74866 1.000 60.59230  ?  310  PRO   A CB  1 
ATOM   2104 C CG  . PRO   A 1 310 ? 16.83997 7.38854   -4.28292 1.000 62.18952  ?  310  PRO   A CG  1 
ATOM   2105 C CD  . PRO   A 1 310 ? 16.34818 8.12220   -3.08455 1.000 60.14184  ?  310  PRO   A CD  1 
ATOM   2106 N N   . LYS   A 1 311 ? 20.18397 8.40720   -2.87788 1.000 68.47918  ?  311  LYS   A N   1 
ATOM   2107 C CA  . LYS   A 1 311 ? 21.59354 8.77832   -2.92874 1.000 67.25211  ?  311  LYS   A CA  1 
ATOM   2108 C C   . LYS   A 1 311 ? 22.12015 9.21481   -1.56710 1.000 68.99654  ?  311  LYS   A C   1 
ATOM   2109 O O   . LYS   A 1 311 ? 23.25666 8.88690   -1.20921 1.000 70.36294  ?  311  LYS   A O   1 
ATOM   2110 C CB  . LYS   A 1 311 ? 21.81305 9.89471   -3.95289 1.000 71.74220  ?  311  LYS   A CB  1 
ATOM   2111 C CG  . LYS   A 1 311 ? 23.16999 9.85388   -4.63567 1.000 78.05906  ?  311  LYS   A CG  1 
ATOM   2112 C CD  . LYS   A 1 311 ? 23.09076 10.39671  -6.05337 1.000 83.64947  ?  311  LYS   A CD  1 
ATOM   2113 C CE  . LYS   A 1 311 ? 24.36445 11.13313  -6.43505 1.000 86.62512  ?  311  LYS   A CE  1 
ATOM   2114 N NZ  . LYS   A 1 311 ? 24.74082 10.89163  -7.85568 1.000 84.48692  ?  311  LYS   A NZ  1 
ATOM   2115 N N   . LEU   A 1 312 ? 21.31524 9.95484   -0.80006 1.000 61.12187  ?  312  LEU   A N   1 
ATOM   2116 C CA  . LEU   A 1 312 ? 21.72133 10.32584  0.55107  1.000 56.63594  ?  312  LEU   A CA  1 
ATOM   2117 C C   . LEU   A 1 312 ? 21.76582 9.11384   1.47186  1.000 55.93934  ?  312  LEU   A C   1 
ATOM   2118 O O   . LEU   A 1 312 ? 22.52072 9.10608   2.45101  1.000 53.68078  ?  312  LEU   A O   1 
ATOM   2119 C CB  . LEU   A 1 312 ? 20.77265 11.38364  1.11526  1.000 54.87902  ?  312  LEU   A CB  1 
ATOM   2120 C CG  . LEU   A 1 312 ? 20.93786 12.81076  0.58891  1.000 55.49521  ?  312  LEU   A CG  1 
ATOM   2121 C CD1 . LEU   A 1 312 ? 19.80551 13.69888  1.08182  1.000 53.25787  ?  312  LEU   A CD1 1 
ATOM   2122 C CD2 . LEU   A 1 312 ? 22.28709 13.37955  0.99764  1.000 53.31662  ?  312  LEU   A CD2 1 
ATOM   2123 N N   . PHE   A 1 313 ? 20.97084 8.08818   1.17662  1.000 57.06809  ?  313  PHE   A N   1 
ATOM   2124 C CA  . PHE   A 1 313 ? 20.92780 6.86141   1.97253  1.000 56.35071  ?  313  PHE   A CA  1 
ATOM   2125 C C   . PHE   A 1 313 ? 20.89013 5.67565   1.02207  1.000 58.29646  ?  313  PHE   A C   1 
ATOM   2126 O O   . PHE   A 1 313 ? 19.82466 5.11231   0.74307  1.000 58.79671  ?  313  PHE   A O   1 
ATOM   2127 C CB  . PHE   A 1 313 ? 19.72117 6.85892   2.91376  1.000 53.99797  ?  313  PHE   A CB  1 
ATOM   2128 C CG  . PHE   A 1 313 ? 19.63123 8.07974   3.78400  1.000 52.34707  ?  313  PHE   A CG  1 
ATOM   2129 C CD1 . PHE   A 1 313 ? 20.36435 8.16739   4.95568  1.000 44.53073  ?  313  PHE   A CD1 1 
ATOM   2130 C CD2 . PHE   A 1 313 ? 18.81995 9.14388   3.42538  1.000 48.13237  ?  313  PHE   A CD2 1 
ATOM   2131 C CE1 . PHE   A 1 313 ? 20.28540 9.29086   5.75769  1.000 43.66891  ?  313  PHE   A CE1 1 
ATOM   2132 C CE2 . PHE   A 1 313 ? 18.73674 10.26970  4.22217  1.000 48.25053  ?  313  PHE   A CE2 1 
ATOM   2133 C CZ  . PHE   A 1 313 ? 19.47049 10.34340  5.39045  1.000 44.81631  ?  313  PHE   A CZ  1 
ATOM   2134 N N   . PRO   A 1 314 ? 22.04516 5.27118   0.49359  1.000 57.69285  ?  314  PRO   A N   1 
ATOM   2135 C CA  . PRO   A 1 314 ? 22.07207 4.15911   -0.46327 1.000 59.93977  ?  314  PRO   A CA  1 
ATOM   2136 C C   . PRO   A 1 314 ? 21.60840 2.85378   0.16662  1.000 60.08739  ?  314  PRO   A C   1 
ATOM   2137 O O   . PRO   A 1 314 ? 21.55674 2.69903   1.38891  1.000 58.35993  ?  314  PRO   A O   1 
ATOM   2138 C CB  . PRO   A 1 314 ? 23.54683 4.08174   -0.88107 1.000 59.86142  ?  314  PRO   A CB  1 
ATOM   2139 C CG  . PRO   A 1 314 ? 24.10742 5.43197   -0.56176 1.000 59.32079  ?  314  PRO   A CG  1 
ATOM   2140 C CD  . PRO   A 1 314 ? 23.36993 5.89170   0.65789  1.000 58.27140  ?  314  PRO   A CD  1 
ATOM   2141 N N   . ASP   A 1 315 ? 21.26568 1.90016   -0.70323 1.000 62.73911  ?  315  ASP   A N   1 
ATOM   2142 C CA  . ASP   A 1 315 ? 20.78352 0.60189   -0.24752 1.000 59.67534  ?  315  ASP   A CA  1 
ATOM   2143 C C   . ASP   A 1 315 ? 21.85098 -0.18744  0.49772  1.000 57.99183  ?  315  ASP   A C   1 
ATOM   2144 O O   . ASP   A 1 315 ? 21.50793 -1.06082  1.30166  1.000 59.41195  ?  315  ASP   A O   1 
ATOM   2145 C CB  . ASP   A 1 315 ? 20.27194 -0.21446  -1.43550 1.000 71.01080  ?  315  ASP   A CB  1 
ATOM   2146 C CG  . ASP   A 1 315 ? 18.76427 -0.15288  -1.57923 1.000 75.67303  ?  315  ASP   A CG  1 
ATOM   2147 O OD1 . ASP   A 1 315 ? 18.28503 0.34603   -2.61931 1.000 77.54517  ?  315  ASP   A OD1 1 
ATOM   2148 O OD2 . ASP   A 1 315 ? 18.05860 -0.60315  -0.65216 1.000 75.97520  -1 315  ASP   A OD2 1 
ATOM   2149 N N   . SER   A 1 316 ? 23.13207 0.09997   0.25389  1.000 59.24194  ?  316  SER   A N   1 
ATOM   2150 C CA  . SER   A 1 316 ? 24.20381 -0.61667  0.93520  1.000 59.11839  ?  316  SER   A CA  1 
ATOM   2151 C C   . SER   A 1 316 ? 24.22961 -0.34093  2.43323  1.000 58.41660  ?  316  SER   A C   1 
ATOM   2152 O O   . SER   A 1 316 ? 24.84124 -1.11147  3.18080  1.000 56.89849  ?  316  SER   A O   1 
ATOM   2153 C CB  . SER   A 1 316 ? 25.55450 -0.25285  0.31667  1.000 60.12873  ?  316  SER   A CB  1 
ATOM   2154 O OG  . SER   A 1 316 ? 25.92448 1.07517   0.64431  1.000 64.52283  ?  316  SER   A OG  1 
ATOM   2155 N N   . LEU   A 1 317 ? 23.58727 0.73319   2.88620  1.000 58.68056  ?  317  LEU   A N   1 
ATOM   2156 C CA  . LEU   A 1 317 ? 23.51248 1.05981   4.30344  1.000 56.57767  ?  317  LEU   A CA  1 
ATOM   2157 C C   . LEU   A 1 317 ? 22.31732 0.42080   4.99691  1.000 57.64184  ?  317  LEU   A C   1 
ATOM   2158 O O   . LEU   A 1 317 ? 22.15039 0.60532   6.20673  1.000 54.28299  ?  317  LEU   A O   1 
ATOM   2159 C CB  . LEU   A 1 317 ? 23.45698 2.57898   4.49399  1.000 54.31245  ?  317  LEU   A CB  1 
ATOM   2160 C CG  . LEU   A 1 317 ? 24.64109 3.39252   3.97061  1.000 52.82445  ?  317  LEU   A CG  1 
ATOM   2161 C CD1 . LEU   A 1 317 ? 24.32477 4.87815   4.02086  1.000 48.80219  ?  317  LEU   A CD1 1 
ATOM   2162 C CD2 . LEU   A 1 317 ? 25.89928 3.08208   4.76558  1.000 49.26665  ?  317  LEU   A CD2 1 
ATOM   2163 N N   . PHE   A 1 318 ? 21.48578 -0.32009  4.26688  1.000 62.22497  ?  318  PHE   A N   1 
ATOM   2164 C CA  . PHE   A 1 318 ? 20.29225 -0.92198  4.82810  1.000 61.05668  ?  318  PHE   A CA  1 
ATOM   2165 C C   . PHE   A 1 318 ? 20.37805 -2.44096  4.76702  1.000 65.16263  ?  318  PHE   A C   1 
ATOM   2166 O O   . PHE   A 1 318 ? 20.95369 -2.98976  3.82064  1.000 64.24888  ?  318  PHE   A O   1 
ATOM   2167 C CB  . PHE   A 1 318 ? 19.03663 -0.46149  4.07384  1.000 63.11619  ?  318  PHE   A CB  1 
ATOM   2168 C CG  . PHE   A 1 318 ? 18.59283 0.92833   4.42240  1.000 64.65180  ?  318  PHE   A CG  1 
ATOM   2169 C CD1 . PHE   A 1 318 ? 17.96941 1.18823   5.63089  1.000 59.80231  ?  318  PHE   A CD1 1 
ATOM   2170 C CD2 . PHE   A 1 318 ? 18.79452 1.97493   3.53828  1.000 62.87822  ?  318  PHE   A CD2 1 
ATOM   2171 C CE1 . PHE   A 1 318 ? 17.55707 2.46652   5.95231  1.000 62.68799  ?  318  PHE   A CE1 1 
ATOM   2172 C CE2 . PHE   A 1 318 ? 18.38555 3.25567   3.85390  1.000 63.58626  ?  318  PHE   A CE2 1 
ATOM   2173 C CZ  . PHE   A 1 318 ? 17.76609 3.50218   5.06284  1.000 65.15648  ?  318  PHE   A CZ  1 
ATOM   2174 N N   . PRO   A 1 319 ? 19.83463 -3.14562  5.76474  1.000 61.83355  ?  319  PRO   A N   1 
ATOM   2175 C CA  . PRO   A 1 319 ? 19.67818 -4.60019  5.63557  1.000 62.26113  ?  319  PRO   A CA  1 
ATOM   2176 C C   . PRO   A 1 319 ? 18.88965 -4.94784  4.38446  1.000 62.92451  ?  319  PRO   A C   1 
ATOM   2177 O O   . PRO   A 1 319 ? 17.67663 -4.72502  4.32562  1.000 58.92749  ?  319  PRO   A O   1 
ATOM   2178 C CB  . PRO   A 1 319 ? 18.92353 -5.00101  6.91297  1.000 57.14365  ?  319  PRO   A CB  1 
ATOM   2179 C CG  . PRO   A 1 319 ? 18.54577 -3.71524  7.59957  1.000 56.39394  ?  319  PRO   A CG  1 
ATOM   2180 C CD  . PRO   A 1 319 ? 19.47744 -2.66301  7.10705  1.000 58.58324  ?  319  PRO   A CD  1 
ATOM   2181 N N   . ALA   A 1 320 ? 19.57930 -5.47494  3.36337  1.000 72.42084  ?  320  ALA   A N   1 
ATOM   2182 C CA  . ALA   A 1 320 ? 18.97920 -5.75745  2.06607  1.000 74.57358  ?  320  ALA   A CA  1 
ATOM   2183 C C   . ALA   A 1 320 ? 19.46019 -7.13074  1.58803  1.000 82.69088  ?  320  ALA   A C   1 
ATOM   2184 O O   . ALA   A 1 320 ? 20.21832 -7.26330  0.62852  1.000 83.20020  ?  320  ALA   A O   1 
ATOM   2185 C CB  . ALA   A 1 320 ? 19.30985 -4.66297  1.04849  1.000 71.09079  ?  320  ALA   A CB  1 
ATOM   2186 N N   . ASP   A 1 321 ? 19.00991 -8.17528  2.27700  1.000 96.58134  ?  321  ASP   A N   1 
ATOM   2187 C CA  . ASP   A 1 321 ? 19.30257 -9.54981  1.89766  1.000 98.33936  ?  321  ASP   A CA  1 
ATOM   2188 C C   . ASP   A 1 321 ? 18.06082 -10.37136 1.59394  1.000 96.05371  ?  321  ASP   A C   1 
ATOM   2189 O O   . ASP   A 1 321 ? 18.12858 -11.27933 0.76303  1.000 97.81413  ?  321  ASP   A O   1 
ATOM   2190 C CB  . ASP   A 1 321 ? 20.10471 -10.25346 3.00360  1.000 93.59291  ?  321  ASP   A CB  1 
ATOM   2191 C CG  . ASP   A 1 321 ? 21.07740 -9.32284  3.69903  1.000 96.95209  ?  321  ASP   A CG  1 
ATOM   2192 O OD1 . ASP   A 1 321 ? 21.94266 -8.74212  3.01013  1.000 99.59215  ?  321  ASP   A OD1 1 
ATOM   2193 O OD2 . ASP   A 1 321 ? 20.97692 -9.17149  4.93451  1.000 107.75712 -1 321  ASP   A OD2 1 
ATOM   2194 N N   . SER   A 1 322 ? 16.93667 -10.07864 2.23786  1.000 77.13257  ?  322  SER   A N   1 
ATOM   2195 C CA  . SER   A 1 322 ? 15.67295 -10.75630 1.99761  1.000 70.40534  ?  322  SER   A CA  1 
ATOM   2196 C C   . SER   A 1 322 ? 14.67692 -9.79048  1.36811  1.000 65.69350  ?  322  SER   A C   1 
ATOM   2197 O O   . SER   A 1 322 ? 14.94026 -8.59487  1.21497  1.000 61.20079  ?  322  SER   A O   1 
ATOM   2198 C CB  . SER   A 1 322 ? 15.11048 -11.33367 3.30104  1.000 64.74850  ?  322  SER   A CB  1 
ATOM   2199 O OG  . SER   A 1 322 ? 13.69363 -11.31475 3.29731  1.000 61.11359  ?  322  SER   A OG  1 
ATOM   2200 N N   . GLU   A 1 323 ? 13.51316 -10.32885 0.99877  1.000 67.29876  ?  323  GLU   A N   1 
ATOM   2201 C CA  . GLU   A 1 323 ? 12.47154 -9.48733  0.41948  1.000 68.24094  ?  323  GLU   A CA  1 
ATOM   2202 C C   . GLU   A 1 323 ? 11.80970 -8.62056  1.48250  1.000 66.46522  ?  323  GLU   A C   1 
ATOM   2203 O O   . GLU   A 1 323 ? 11.49331 -7.45196  1.22925  1.000 66.43221  ?  323  GLU   A O   1 
ATOM   2204 C CB  . GLU   A 1 323 ? 11.43269 -10.34888 -0.29548 1.000 70.46173  ?  323  GLU   A CB  1 
ATOM   2205 C CG  . GLU   A 1 323 ? 10.89211 -9.72270  -1.56886 1.000 72.54329  ?  323  GLU   A CG  1 
ATOM   2206 C CD  . GLU   A 1 323 ? 11.73816 -10.04860 -2.78442 1.000 74.30036  ?  323  GLU   A CD  1 
ATOM   2207 O OE1 . GLU   A 1 323 ? 12.06401 -11.23795 -2.98105 1.000 75.08561  ?  323  GLU   A OE1 1 
ATOM   2208 O OE2 . GLU   A 1 323 ? 12.07616 -9.11644  -3.54389 1.000 75.01866  -1 323  GLU   A OE2 1 
ATOM   2209 N N   . HIS   A 1 324 ? 11.58789 -9.17672  2.67642  1.000 58.04266  ?  324  HIS   A N   1 
ATOM   2210 C CA  . HIS   A 1 324 ? 11.04643 -8.38032  3.77279  1.000 57.28781  ?  324  HIS   A CA  1 
ATOM   2211 C C   . HIS   A 1 324 ? 11.99366 -7.24747  4.14355  1.000 51.59732  ?  324  HIS   A C   1 
ATOM   2212 O O   . HIS   A 1 324 ? 11.55370 -6.13324  4.44944  1.000 49.89087  ?  324  HIS   A O   1 
ATOM   2213 C CB  . HIS   A 1 324 ? 10.77314 -9.27290  4.98416  1.000 54.20258  ?  324  HIS   A CB  1 
ATOM   2214 C CG  . HIS   A 1 324 ? 10.52919 -8.51567  6.25302  1.000 52.81989  ?  324  HIS   A CG  1 
ATOM   2215 N ND1 . HIS   A 1 324 ? 11.54894 -8.11404  7.08936  1.000 50.92153  ?  324  HIS   A ND1 1 
ATOM   2216 C CD2 . HIS   A 1 324 ? 9.38063  -8.08942  6.82978  1.000 52.08926  ?  324  HIS   A CD2 1 
ATOM   2217 C CE1 . HIS   A 1 324 ? 11.03947 -7.47129  8.12492  1.000 48.34113  ?  324  HIS   A CE1 1 
ATOM   2218 N NE2 . HIS   A 1 324 ? 9.72567  -7.44299  7.99199  1.000 51.47261  ?  324  HIS   A NE2 1 
ATOM   2219 N N   . ASN   A 1 325 ? 13.30126 -7.51328  4.11603  1.000 51.11595  ?  325  ASN   A N   1 
ATOM   2220 C CA  . ASN   A 1 325 ? 14.27513 -6.47105  4.41711  1.000 51.51969  ?  325  ASN   A CA  1 
ATOM   2221 C C   . ASN   A 1 325 ? 14.36613 -5.44508  3.29503  1.000 52.45169  ?  325  ASN   A C   1 
ATOM   2222 O O   . ASN   A 1 325 ? 14.65377 -4.27081  3.55379  1.000 52.15886  ?  325  ASN   A O   1 
ATOM   2223 C CB  . ASN   A 1 325 ? 15.64405 -7.09626  4.68081  1.000 57.19471  ?  325  ASN   A CB  1 
ATOM   2224 C CG  . ASN   A 1 325 ? 15.83590 -7.48637  6.13279  1.000 52.13581  ?  325  ASN   A CG  1 
ATOM   2225 O OD1 . ASN   A 1 325 ? 14.92895 -7.34014  6.95215  1.000 45.09217  ?  325  ASN   A OD1 1 
ATOM   2226 N ND2 . ASN   A 1 325 ? 17.02211 -7.98510  6.45923  1.000 55.56999  ?  325  ASN   A ND2 1 
ATOM   2227 N N   . LYS   A 1 326 ? 14.12927 -5.86498  2.04970  1.000 54.61720  ?  326  LYS   A N   1 
ATOM   2228 C CA  . LYS   A 1 326 ? 14.14280 -4.92215  0.93589  1.000 53.05045  ?  326  LYS   A CA  1 
ATOM   2229 C C   . LYS   A 1 326 ? 12.99236 -3.92954  1.04115  1.000 53.02535  ?  326  LYS   A C   1 
ATOM   2230 O O   . LYS   A 1 326 ? 13.16118 -2.74008  0.74752  1.000 53.09331  ?  326  LYS   A O   1 
ATOM   2231 C CB  . LYS   A 1 326 ? 14.07505 -5.67556  -0.39259 1.000 55.59553  ?  326  LYS   A CB  1 
ATOM   2232 C CG  . LYS   A 1 326 ? 15.41431 -6.17830  -0.90692 1.000 56.25016  ?  326  LYS   A CG  1 
ATOM   2233 C CD  . LYS   A 1 326 ? 15.21797 -7.26869  -1.95248 1.000 58.47081  ?  326  LYS   A CD  1 
ATOM   2234 C CE  . LYS   A 1 326 ? 16.34773 -7.27984  -2.97038 1.000 59.93822  ?  326  LYS   A CE  1 
ATOM   2235 N NZ  . LYS   A 1 326 ? 17.65020 -7.66134  -2.35862 1.000 62.63688  ?  326  LYS   A NZ  1 
ATOM   2236 N N   . LEU   A 1 327 ? 11.81539 -4.40057  1.45771  1.000 53.07570  ?  327  LEU   A N   1 
ATOM   2237 C CA  . LEU   A 1 327 ? 10.66183 -3.51610  1.57975  1.000 53.20070  ?  327  LEU   A CA  1 
ATOM   2238 C C   . LEU   A 1 327 ? 10.84972 -2.52367  2.72053  1.000 50.89105  ?  327  LEU   A C   1 
ATOM   2239 O O   . LEU   A 1 327 ? 10.59392 -1.32485  2.56058  1.000 50.93811  ?  327  LEU   A O   1 
ATOM   2240 C CB  . LEU   A 1 327 ? 9.39012  -4.34055  1.78263  1.000 53.96537  ?  327  LEU   A CB  1 
ATOM   2241 C CG  . LEU   A 1 327 ? 8.13078  -3.57417  2.19192  1.000 53.99366  ?  327  LEU   A CG  1 
ATOM   2242 C CD1 . LEU   A 1 327 ? 7.69800  -2.61794  1.08990  1.000 55.70041  ?  327  LEU   A CD1 1 
ATOM   2243 C CD2 . LEU   A 1 327 ? 7.00721  -4.53754  2.54282  1.000 55.13766  ?  327  LEU   A CD2 1 
ATOM   2244 N N   . LYS   A 1 328 ? 11.30352 -3.00598  3.88143  1.000 48.97389  ?  328  LYS   A N   1 
ATOM   2245 C CA  . LYS   A 1 328 ? 11.49756 -2.12216  5.02690  1.000 47.78544  ?  328  LYS   A CA  1 
ATOM   2246 C C   . LYS   A 1 328 ? 12.54045 -1.05005  4.74171  1.000 46.37772  ?  328  LYS   A C   1 
ATOM   2247 O O   . LYS   A 1 328 ? 12.44516 0.06283   5.27126  1.000 47.80796  ?  328  LYS   A O   1 
ATOM   2248 C CB  . LYS   A 1 328 ? 11.89896 -2.93582  6.25765  1.000 47.41854  ?  328  LYS   A CB  1 
ATOM   2249 C CG  . LYS   A 1 328 ? 10.82732 -3.89335  6.75031  1.000 49.72042  ?  328  LYS   A CG  1 
ATOM   2250 C CD  . LYS   A 1 328 ? 10.10352 -3.33723  7.96514  1.000 50.57800  ?  328  LYS   A CD  1 
ATOM   2251 C CE  . LYS   A 1 328 ? 8.64154  -3.75284  7.97196  1.000 61.18593  ?  328  LYS   A CE  1 
ATOM   2252 N NZ  . LYS   A 1 328 ? 8.17377  -4.11777  9.33769  1.000 58.70518  ?  328  LYS   A NZ  1 
ATOM   2253 N N   . ALA   A 1 329 ? 13.54004 -1.36246  3.91376  1.000 47.32729  ?  329  ALA   A N   1 
ATOM   2254 C CA  . ALA   A 1 329 ? 14.53659 -0.36080  3.55061  1.000 47.28465  ?  329  ALA   A CA  1 
ATOM   2255 C C   . ALA   A 1 329 ? 13.90943 0.77477   2.75324  1.000 49.75545  ?  329  ALA   A C   1 
ATOM   2256 O O   . ALA   A 1 329 ? 14.30967 1.93675   2.89193  1.000 50.23918  ?  329  ALA   A O   1 
ATOM   2257 C CB  . ALA   A 1 329 ? 15.67178 -1.01111  2.76065  1.000 51.27794  ?  329  ALA   A CB  1 
ATOM   2258 N N   . SER   A 1 330 ? 12.92237 0.45889   1.91309  1.000 50.48658  ?  330  SER   A N   1 
ATOM   2259 C CA  . SER   A 1 330 ? 12.22914 1.49657   1.16011  1.000 51.97931  ?  330  SER   A CA  1 
ATOM   2260 C C   . SER   A 1 330 ? 11.23711 2.26148   2.02668  1.000 50.82721  ?  330  SER   A C   1 
ATOM   2261 O O   . SER   A 1 330 ? 11.05722 3.46912   1.83311  1.000 51.17042  ?  330  SER   A O   1 
ATOM   2262 C CB  . SER   A 1 330 ? 11.51365 0.88656   -0.04708 1.000 54.59320  ?  330  SER   A CB  1 
ATOM   2263 O OG  . SER   A 1 330 ? 10.46837 0.02169   0.36039  1.000 54.52481  ?  330  SER   A OG  1 
ATOM   2264 N N   . GLN   A 1 331 ? 10.58609 1.58557   2.97750  1.000 49.61043  ?  331  GLN   A N   1 
ATOM   2265 C CA  . GLN   A 1 331 ? 9.69452  2.28773   3.89517  1.000 48.46222  ?  331  GLN   A CA  1 
ATOM   2266 C C   . GLN   A 1 331 ? 10.47585 3.21104   4.82006  1.000 47.45237  ?  331  GLN   A C   1 
ATOM   2267 O O   . GLN   A 1 331 ? 10.02410 4.32149   5.12412  1.000 45.97839  ?  331  GLN   A O   1 
ATOM   2268 C CB  . GLN   A 1 331 ? 8.87267  1.28808   4.70751  1.000 49.21724  ?  331  GLN   A CB  1 
ATOM   2269 C CG  . GLN   A 1 331 ? 8.21213  0.20298   3.88059  1.000 50.05605  ?  331  GLN   A CG  1 
ATOM   2270 C CD  . GLN   A 1 331 ? 7.19227  -0.58914  4.67143  1.000 52.88583  ?  331  GLN   A CD  1 
ATOM   2271 O OE1 . GLN   A 1 331 ? 7.52013  -1.21060  5.68219  1.000 51.80440  ?  331  GLN   A OE1 1 
ATOM   2272 N NE2 . GLN   A 1 331 ? 5.94736  -0.57710  4.21050  1.000 54.89098  ?  331  GLN   A NE2 1 
ATOM   2273 N N   . ALA   A 1 332 ? 11.64724 2.76706   5.28116  1.000 48.49414  ?  332  ALA   A N   1 
ATOM   2274 C CA  . ALA   A 1 332 ? 12.49440 3.62657   6.10053  1.000 45.59689  ?  332  ALA   A CA  1 
ATOM   2275 C C   . ALA   A 1 332 ? 12.92131 4.86473   5.32368  1.000 47.97724  ?  332  ALA   A C   1 
ATOM   2276 O O   . ALA   A 1 332 ? 12.76795 5.99487   5.79963  1.000 47.77942  ?  332  ALA   A O   1 
ATOM   2277 C CB  . ALA   A 1 332 ? 13.71461 2.84796   6.59278  1.000 47.17771  ?  332  ALA   A CB  1 
ATOM   2278 N N   . ARG   A 1 333 ? 13.44640 4.67052   4.11138  1.000 46.43558  ?  333  ARG   A N   1 
ATOM   2279 C CA  . ARG   A 1 333 ? 13.84116 5.80949   3.29013  1.000 48.48702  ?  333  ARG   A CA  1 
ATOM   2280 C C   . ARG   A 1 333 ? 12.66062 6.72594   2.99779  1.000 48.38334  ?  333  ARG   A C   1 
ATOM   2281 O O   . ARG   A 1 333 ? 12.84216 7.93738   2.83156  1.000 48.74387  ?  333  ARG   A O   1 
ATOM   2282 C CB  . ARG   A 1 333 ? 14.47322 5.32328   1.98676  1.000 49.52746  ?  333  ARG   A CB  1 
ATOM   2283 C CG  . ARG   A 1 333 ? 15.30710 6.37571   1.28068  1.000 52.53235  ?  333  ARG   A CG  1 
ATOM   2284 C CD  . ARG   A 1 333 ? 15.84826 5.85638   -0.03664 1.000 55.54109  ?  333  ARG   A CD  1 
ATOM   2285 N NE  . ARG   A 1 333 ? 16.97393 4.94993   0.15389  1.000 57.83408  ?  333  ARG   A NE  1 
ATOM   2286 C CZ  . ARG   A 1 333 ? 17.01887 3.70541   -0.30177 1.000 60.38953  ?  333  ARG   A CZ  1 
ATOM   2287 N NH1 . ARG   A 1 333 ? 16.01409 3.18278   -0.98599 1.000 57.12297  ?  333  ARG   A NH1 1 
ATOM   2288 N NH2 . ARG   A 1 333 ? 18.09949 2.96687   -0.06601 1.000 60.39209  ?  333  ARG   A NH2 1 
ATOM   2289 N N   . ASP   A 1 334 ? 11.44745 6.17191   2.93940  1.000 48.97012  ?  334  ASP   A N   1 
ATOM   2290 C CA  . ASP   A 1 334 ? 10.26718 7.00137   2.72165  1.000 49.99192  ?  334  ASP   A CA  1 
ATOM   2291 C C   . ASP   A 1 334 ? 9.96728  7.86430   3.94098  1.000 47.99988  ?  334  ASP   A C   1 
ATOM   2292 O O   . ASP   A 1 334 ? 9.55758  9.02269   3.80264  1.000 50.59783  ?  334  ASP   A O   1 
ATOM   2293 C CB  . ASP   A 1 334 ? 9.06570  6.12301   2.37372  1.000 51.25572  ?  334  ASP   A CB  1 
ATOM   2294 C CG  . ASP   A 1 334 ? 7.79664  6.92567   2.17201  1.000 52.46388  ?  334  ASP   A CG  1 
ATOM   2295 O OD1 . ASP   A 1 334 ? 7.55269  7.37783   1.03371  1.000 54.83422  ?  334  ASP   A OD1 1 
ATOM   2296 O OD2 . ASP   A 1 334 ? 7.04289  7.10473   3.15177  1.000 51.95828  -1 334  ASP   A OD2 1 
ATOM   2297 N N   . LEU   A 1 335 ? 10.16414 7.31876   5.14364  1.000 47.21589  ?  335  LEU   A N   1 
ATOM   2298 C CA  . LEU   A 1 335 ? 9.96051  8.11005   6.35295  1.000 45.25167  ?  335  LEU   A CA  1 
ATOM   2299 C C   . LEU   A 1 335 ? 11.02983 9.18752   6.48931  1.000 45.02410  ?  335  LEU   A C   1 
ATOM   2300 O O   . LEU   A 1 335 ? 10.75040 10.28959  6.97485  1.000 43.91851  ?  335  LEU   A O   1 
ATOM   2301 C CB  . LEU   A 1 335 ? 9.94706  7.19999   7.58075  1.000 46.65441  ?  335  LEU   A CB  1 
ATOM   2302 C CG  . LEU   A 1 335 ? 9.60534  7.86608   8.91519  1.000 46.56384  ?  335  LEU   A CG  1 
ATOM   2303 C CD1 . LEU   A 1 335 ? 8.24347  8.54373   8.85412  1.000 47.61934  ?  335  LEU   A CD1 1 
ATOM   2304 C CD2 . LEU   A 1 335 ? 9.65637  6.85763   10.05295 1.000 45.52133  ?  335  LEU   A CD2 1 
ATOM   2305 N N   . LEU   A 1 336 ? 12.26229 8.88527   6.07041  1.000 43.94768  ?  336  LEU   A N   1 
ATOM   2306 C CA  . LEU   A 1 336 ? 13.29481 9.91421   5.99887  1.000 43.19400  ?  336  LEU   A CA  1 
ATOM   2307 C C   . LEU   A 1 336 ? 12.89712 11.03195  5.04636  1.000 45.65206  ?  336  LEU   A C   1 
ATOM   2308 O O   . LEU   A 1 336 ? 13.21826 12.20100  5.29102  1.000 44.92781  ?  336  LEU   A O   1 
ATOM   2309 C CB  . LEU   A 1 336 ? 14.62477 9.30096   5.55964  1.000 43.48306  ?  336  LEU   A CB  1 
ATOM   2310 C CG  . LEU   A 1 336 ? 15.56317 8.75063   6.63343  1.000 43.63554  ?  336  LEU   A CG  1 
ATOM   2311 C CD1 . LEU   A 1 336 ? 16.70619 7.96983   6.00239  1.000 42.16155  ?  336  LEU   A CD1 1 
ATOM   2312 C CD2 . LEU   A 1 336 ? 16.09289 9.86065   7.52716  1.000 39.94040  ?  336  LEU   A CD2 1 
ATOM   2313 N N   . SER   A 1 337 ? 12.19313 10.69403  3.96312  1.000 47.36217  ?  337  SER   A N   1 
ATOM   2314 C CA  . SER   A 1 337 ? 11.79435 11.70509  2.99000  1.000 49.60904  ?  337  SER   A CA  1 
ATOM   2315 C C   . SER   A 1 337 ? 10.71604 12.62417  3.55055  1.000 49.24340  ?  337  SER   A C   1 
ATOM   2316 O O   . SER   A 1 337 ? 10.69438 13.82257  3.24636  1.000 50.23205  ?  337  SER   A O   1 
ATOM   2317 C CB  . SER   A 1 337 ? 11.31286 11.03178  1.70514  1.000 52.14247  ?  337  SER   A CB  1 
ATOM   2318 O OG  . SER   A 1 337 ? 9.98034  10.56765  1.84051  1.000 52.37599  ?  337  SER   A OG  1 
ATOM   2319 N N   . LYS   A 1 338 ? 9.81200  12.08390  4.36803  1.000 47.97837  ?  338  LYS   A N   1 
ATOM   2320 C CA  . LYS   A 1 338 ? 8.74672  12.89262  4.94528  1.000 47.67236  ?  338  LYS   A CA  1 
ATOM   2321 C C   . LYS   A 1 338 ? 9.20429  13.68722  6.16011  1.000 45.41389  ?  338  LYS   A C   1 
ATOM   2322 O O   . LYS   A 1 338 ? 8.59342  14.71348  6.47776  1.000 45.45702  ?  338  LYS   A O   1 
ATOM   2323 C CB  . LYS   A 1 338 ? 7.56022  12.00567  5.33000  1.000 47.47023  ?  338  LYS   A CB  1 
ATOM   2324 C CG  . LYS   A 1 338 ? 6.68088  11.60289  4.15746  1.000 50.12234  ?  338  LYS   A CG  1 
ATOM   2325 C CD  . LYS   A 1 338 ? 5.79148  10.42155  4.51126  1.000 49.90507  ?  338  LYS   A CD  1 
ATOM   2326 C CE  . LYS   A 1 338 ? 4.84659  10.08122  3.37024  1.000 52.77486  ?  338  LYS   A CE  1 
ATOM   2327 N NZ  . LYS   A 1 338 ? 5.55638  10.02045  2.06249  1.000 54.63151  ?  338  LYS   A NZ  1 
ATOM   2328 N N   . MET   A 1 339 ? 10.26219 13.24464  6.83778  1.000 43.57378  ?  339  MET   A N   1 
ATOM   2329 C CA  . MET   A 1 339 ? 10.73098 13.90807  8.04744  1.000 42.86294  ?  339  MET   A CA  1 
ATOM   2330 C C   . MET   A 1 339 ? 11.80614 14.95141  7.75437  1.000 41.83913  ?  339  MET   A C   1 
ATOM   2331 O O   . MET   A 1 339 ? 11.74475 16.07036  8.27325  1.000 41.27350  ?  339  MET   A O   1 
ATOM   2332 C CB  . MET   A 1 339 ? 11.24742 12.86553  9.04732  1.000 42.01618  ?  339  MET   A CB  1 
ATOM   2333 C CG  . MET   A 1 339 ? 10.16595 12.33698  9.98399  1.000 46.94211  ?  339  MET   A CG  1 
ATOM   2334 S SD  . MET   A 1 339 ? 10.48994 10.74572  10.76946 1.000 44.81031  ?  339  MET   A SD  1 
ATOM   2335 C CE  . MET   A 1 339 ? 12.27159 10.65193  10.68194 1.000 38.17371  ?  339  MET   A CE  1 
ATOM   2336 N N   . LEU   A 1 340 ? 12.78690 14.60942  6.91968  1.000 42.82472  ?  340  LEU   A N   1 
ATOM   2337 C CA  . LEU   A 1 340 ? 13.90840 15.50649  6.63372  1.000 43.33665  ?  340  LEU   A CA  1 
ATOM   2338 C C   . LEU   A 1 340 ? 13.55996 16.42304  5.45880  1.000 45.97750  ?  340  LEU   A C   1 
ATOM   2339 O O   . LEU   A 1 340 ? 14.02875 16.26196  4.33044  1.000 47.97531  ?  340  LEU   A O   1 
ATOM   2340 C CB  . LEU   A 1 340 ? 15.17278 14.70298  6.35855  1.000 43.28084  ?  340  LEU   A CB  1 
ATOM   2341 C CG  . LEU   A 1 340 ? 16.01679 14.30274  7.56924  1.000 40.86899  ?  340  LEU   A CG  1 
ATOM   2342 C CD1 . LEU   A 1 340 ? 17.21616 13.48505  7.12566  1.000 41.26651  ?  340  LEU   A CD1 1 
ATOM   2343 C CD2 . LEU   A 1 340 ? 16.46111 15.53048  8.34945  1.000 39.88123  ?  340  LEU   A CD2 1 
ATOM   2344 N N   . VAL   A 1 341 ? 12.71578 17.41006  5.75078  1.000 46.09357  ?  341  VAL   A N   1 
ATOM   2345 C CA  . VAL   A 1 341 ? 12.35074 18.44603  4.79220  1.000 48.58350  ?  341  VAL   A CA  1 
ATOM   2346 C C   . VAL   A 1 341 ? 12.43636 19.79720  5.48620  1.000 47.91787  ?  341  VAL   A C   1 
ATOM   2347 O O   . VAL   A 1 341 ? 12.05392 19.93362  6.65378  1.000 45.83111  ?  341  VAL   A O   1 
ATOM   2348 C CB  . VAL   A 1 341 ? 10.94363 18.22109  4.19941  1.000 50.14128  ?  341  VAL   A CB  1 
ATOM   2349 C CG1 . VAL   A 1 341 ? 10.98798 17.14818  3.12120  1.000 51.77420  ?  341  VAL   A CG1 1 
ATOM   2350 C CG2 . VAL   A 1 341 ? 9.96579  17.83869  5.28917  1.000 48.19966  ?  341  VAL   A CG2 1 
ATOM   2351 N N   . ILE   A 1 342 ? 12.93873 20.79795  4.76148  1.000 49.84019  ?  342  ILE   A N   1 
ATOM   2352 C CA  . ILE   A 1 342 ? 13.20060 22.09811  5.37008  1.000 49.38106  ?  342  ILE   A CA  1 
ATOM   2353 C C   . ILE   A 1 342 ? 11.89723 22.81306  5.70650  1.000 49.51976  ?  342  ILE   A C   1 
ATOM   2354 O O   . ILE   A 1 342 ? 11.74978 23.38074  6.79563  1.000 47.75657  ?  342  ILE   A O   1 
ATOM   2355 C CB  . ILE   A 1 342 ? 14.09194 22.94588  4.44504  1.000 51.72499  ?  342  ILE   A CB  1 
ATOM   2356 C CG1 . ILE   A 1 342 ? 15.39509 22.20508  4.13954  1.000 51.65265  ?  342  ILE   A CG1 1 
ATOM   2357 C CG2 . ILE   A 1 342 ? 14.38589 24.29461  5.07779  1.000 51.36914  ?  342  ILE   A CG2 1 
ATOM   2358 C CD1 . ILE   A 1 342 ? 16.27979 22.91573  3.14072  1.000 54.27208  ?  342  ILE   A CD1 1 
ATOM   2359 N N   . ASP   A 1 343 ? 10.93803 22.79778  4.79227  1.000 51.70611  ?  343  ASP   A N   1 
ATOM   2360 C CA  . ASP   A 1 343 ? 9.68734  23.51863  5.00667  1.000 52.24298  ?  343  ASP   A CA  1 
ATOM   2361 C C   . ASP   A 1 343 ? 8.83272  22.80380  6.04508  1.000 49.99576  ?  343  ASP   A C   1 
ATOM   2362 O O   . ASP   A 1 343 ? 8.53702  21.61344  5.87776  1.000 51.99894  ?  343  ASP   A O   1 
ATOM   2363 C CB  . ASP   A 1 343 ? 8.92094  23.65822  3.69545  1.000 55.47718  ?  343  ASP   A CB  1 
ATOM   2364 C CG  . ASP   A 1 343 ? 7.83212  24.71243  3.76787  1.000 56.64591  ?  343  ASP   A CG  1 
ATOM   2365 O OD1 . ASP   A 1 343 ? 7.52157  25.32281  2.72306  1.000 59.62524  ?  343  ASP   A OD1 1 
ATOM   2366 O OD2 . ASP   A 1 343 ? 7.28635  24.93111  4.87000  1.000 54.71307  -1 343  ASP   A OD2 1 
ATOM   2367 N N   . PRO   A 1 344 ? 8.41755  23.47617  7.12216  1.000 48.47985  ?  344  PRO   A N   1 
ATOM   2368 C CA  . PRO   A 1 344 ? 7.56966  22.80062  8.11633  1.000 48.36680  ?  344  PRO   A CA  1 
ATOM   2369 C C   . PRO   A 1 344 ? 6.16762  22.51132  7.61240  1.000 49.60913  ?  344  PRO   A C   1 
ATOM   2370 O O   . PRO   A 1 344 ? 5.57004  21.51099  8.02852  1.000 51.51743  ?  344  PRO   A O   1 
ATOM   2371 C CB  . PRO   A 1 344 ? 7.54974  23.78437  9.29792  1.000 46.45065  ?  344  PRO   A CB  1 
ATOM   2372 C CG  . PRO   A 1 344 ? 8.62790  24.79483  9.00861  1.000 45.59269  ?  344  PRO   A CG  1 
ATOM   2373 C CD  . PRO   A 1 344 ? 8.76193  24.84799  7.52530  1.000 48.44769  ?  344  PRO   A CD  1 
ATOM   2374 N N   . ALA   A 1 345 ? 5.62263  23.35592  6.73185  1.000 50.76032  ?  345  ALA   A N   1 
ATOM   2375 C CA  . ALA   A 1 345 ? 4.26721  23.13731  6.23725  1.000 52.54482  ?  345  ALA   A CA  1 
ATOM   2376 C C   . ALA   A 1 345 ? 4.16207  21.84591  5.43769  1.000 54.07973  ?  345  ALA   A C   1 
ATOM   2377 O O   . ALA   A 1 345 ? 3.10389  21.20664  5.42810  1.000 54.54615  ?  345  ALA   A O   1 
ATOM   2378 C CB  . ALA   A 1 345 ? 3.81805  24.32767  5.38991  1.000 55.39629  ?  345  ALA   A CB  1 
ATOM   2379 N N   . LYS   A 1 346 ? 5.23954  21.44760  4.76386  1.000 57.06513  ?  346  LYS   A N   1 
ATOM   2380 C CA  . LYS   A 1 346 ? 5.27871  20.18377  4.04231  1.000 57.11048  ?  346  LYS   A CA  1 
ATOM   2381 C C   . LYS   A 1 346 ? 5.75317  19.02391  4.90622  1.000 60.12248  ?  346  LYS   A C   1 
ATOM   2382 O O   . LYS   A 1 346 ? 5.67524  17.87159  4.46630  1.000 58.79186  ?  346  LYS   A O   1 
ATOM   2383 C CB  . LYS   A 1 346 ? 6.19121  20.29993  2.81592  1.000 60.55402  ?  346  LYS   A CB  1 
ATOM   2384 C CG  . LYS   A 1 346 ? 5.70807  21.28012  1.76008  1.000 65.45993  ?  346  LYS   A CG  1 
ATOM   2385 C CD  . LYS   A 1 346 ? 6.85173  21.71538  0.85699  1.000 65.75663  ?  346  LYS   A CD  1 
ATOM   2386 C CE  . LYS   A 1 346 ? 6.71457  23.17367  0.45244  1.000 75.84250  ?  346  LYS   A CE  1 
ATOM   2387 N NZ  . LYS   A 1 346 ? 8.03395  23.86414  0.40500  1.000 69.33856  ?  346  LYS   A NZ  1 
ATOM   2388 N N   . ARG   A 1 347 ? 6.23323  19.29730  6.11638  1.000 53.41068  ?  347  ARG   A N   1 
ATOM   2389 C CA  . ARG   A 1 347 ? 6.82144  18.26403  6.95476  1.000 51.14654  ?  347  ARG   A CA  1 
ATOM   2390 C C   . ARG   A 1 347 ? 5.74475  17.38908  7.58220  1.000 50.63204  ?  347  ARG   A C   1 
ATOM   2391 O O   . ARG   A 1 347 ? 4.66927  17.86780  7.95527  1.000 49.77228  ?  347  ARG   A O   1 
ATOM   2392 C CB  . ARG   A 1 347 ? 7.68593  18.89548  8.04575  1.000 50.31268  ?  347  ARG   A CB  1 
ATOM   2393 C CG  . ARG   A 1 347 ? 8.67926  17.93903  8.68226  1.000 46.88095  ?  347  ARG   A CG  1 
ATOM   2394 C CD  . ARG   A 1 347 ? 9.45049  18.61190  9.80398  1.000 45.60166  ?  347  ARG   A CD  1 
ATOM   2395 N NE  . ARG   A 1 347 ? 10.40829 19.59088  9.30534  1.000 45.94813  ?  347  ARG   A NE  1 
ATOM   2396 C CZ  . ARG   A 1 347 ? 10.63634 20.76765  9.87184  1.000 42.34469  ?  347  ARG   A CZ  1 
ATOM   2397 N NH1 . ARG   A 1 347 ? 9.98924  21.14666  10.96178 1.000 44.25598  ?  347  ARG   A NH1 1 
ATOM   2398 N NH2 . ARG   A 1 347 ? 11.53732 21.58362  9.33264  1.000 41.90366  ?  347  ARG   A NH2 1 
ATOM   2399 N N   . ILE   A 1 348 ? 6.04700  16.09439  7.69565  1.000 47.88283  ?  348  ILE   A N   1 
ATOM   2400 C CA  . ILE   A 1 348 ? 5.11422  15.15211  8.29641  1.000 49.78665  ?  348  ILE   A CA  1 
ATOM   2401 C C   . ILE   A 1 348 ? 4.96082  15.45761  9.78321  1.000 51.31847  ?  348  ILE   A C   1 
ATOM   2402 O O   . ILE   A 1 348 ? 5.88281  15.96016  10.44097 1.000 49.93288  ?  348  ILE   A O   1 
ATOM   2403 C CB  . ILE   A 1 348 ? 5.59370  13.70718  8.05878  1.000 50.40660  ?  348  ILE   A CB  1 
ATOM   2404 C CG1 . ILE   A 1 348 ? 4.48619  12.70281  8.37992  1.000 53.64970  ?  348  ILE   A CG1 1 
ATOM   2405 C CG2 . ILE   A 1 348 ? 6.84356  13.40998  8.87504  1.000 49.46789  ?  348  ILE   A CG2 1 
ATOM   2406 C CD1 . ILE   A 1 348 ? 4.94978  11.26308  8.37579  1.000 54.44260  ?  348  ILE   A CD1 1 
ATOM   2407 N N   . SER   A 1 349 ? 3.77743  15.17156  10.31605 1.000 53.33102  ?  349  SER   A N   1 
ATOM   2408 C CA  . SER   A 1 349 ? 3.48733  15.42271  11.71800 1.000 54.63459  ?  349  SER   A CA  1 
ATOM   2409 C C   . SER   A 1 349 ? 3.78796  14.18495  12.55984 1.000 56.36706  ?  349  SER   A C   1 
ATOM   2410 O O   . SER   A 1 349 ? 4.07547  13.10173  12.04595 1.000 56.47855  ?  349  SER   A O   1 
ATOM   2411 C CB  . SER   A 1 349 ? 2.02945  15.84703  11.89560 1.000 58.20133  ?  349  SER   A CB  1 
ATOM   2412 O OG  . SER   A 1 349 ? 1.17992  14.71789  12.00353 1.000 63.73869  ?  349  SER   A OG  1 
ATOM   2413 N N   . VAL   A 1 350 ? 3.71725  14.36150  13.88084 1.000 57.12813  ?  350  VAL   A N   1 
ATOM   2414 C CA  . VAL   A 1 350 ? 3.96694  13.24926  14.79194 1.000 57.01805  ?  350  VAL   A CA  1 
ATOM   2415 C C   . VAL   A 1 350 ? 2.87847  12.19208  14.65667 1.000 60.12626  ?  350  VAL   A C   1 
ATOM   2416 O O   . VAL   A 1 350 ? 3.15948  10.98755  14.66745 1.000 59.34521  ?  350  VAL   A O   1 
ATOM   2417 C CB  . VAL   A 1 350 ? 4.08295  13.76130  16.23876 1.000 53.68188  ?  350  VAL   A CB  1 
ATOM   2418 C CG1 . VAL   A 1 350 ? 4.48042  12.62890  17.17312 1.000 52.52665  ?  350  VAL   A CG1 1 
ATOM   2419 C CG2 . VAL   A 1 350 ? 5.08406  14.90346  16.31770 1.000 52.25675  ?  350  VAL   A CG2 1 
ATOM   2420 N N   . ASP   A 1 351 ? 1.62145  12.62210  14.52236 1.000 65.69624  ?  351  ASP   A N   1 
ATOM   2421 C CA  . ASP   A 1 351 ? 0.52400  11.66920  14.39025 1.000 67.41089  ?  351  ASP   A CA  1 
ATOM   2422 C C   . ASP   A 1 351 ? 0.61234  10.90093  13.07743 1.000 70.40533  ?  351  ASP   A C   1 
ATOM   2423 O O   . ASP   A 1 351 ? 0.34536  9.69409   13.03923 1.000 66.88171  ?  351  ASP   A O   1 
ATOM   2424 C CB  . ASP   A 1 351 ? -0.81645 12.39506  14.49903 1.000 73.77254  ?  351  ASP   A CB  1 
ATOM   2425 C CG  . ASP   A 1 351 ? -1.15965 12.77333  15.92601 1.000 73.93856  ?  351  ASP   A CG  1 
ATOM   2426 O OD1 . ASP   A 1 351 ? -1.43174 13.96609  16.17629 1.000 78.51871  ?  351  ASP   A OD1 1 
ATOM   2427 O OD2 . ASP   A 1 351 ? -1.15697 11.87837  16.79745 1.000 70.10732  -1 351  ASP   A OD2 1 
ATOM   2428 N N   . ASP   A 1 352 ? 0.98463  11.58155  11.99061 1.000 69.23861  ?  352  ASP   A N   1 
ATOM   2429 C CA  . ASP   A 1 352 ? 1.12963  10.89908  10.70966 1.000 63.70398  ?  352  ASP   A CA  1 
ATOM   2430 C C   . ASP   A 1 352 ? 2.32840  9.95991   10.70701 1.000 60.91729  ?  352  ASP   A C   1 
ATOM   2431 O O   . ASP   A 1 352 ? 2.29809  8.92100   10.03753 1.000 64.40323  ?  352  ASP   A O   1 
ATOM   2432 C CB  . ASP   A 1 352 ? 1.25545  11.92014  9.57960  1.000 63.40920  ?  352  ASP   A CB  1 
ATOM   2433 C CG  . ASP   A 1 352 ? -0.07237 12.54706  9.20841  1.000 77.42475  ?  352  ASP   A CG  1 
ATOM   2434 O OD1 . ASP   A 1 352 ? -1.07159 12.28658  9.91056  1.000 83.89611  ?  352  ASP   A OD1 1 
ATOM   2435 O OD2 . ASP   A 1 352 ? -0.11626 13.30146  8.21350  1.000 80.14488  -1 352  ASP   A OD2 1 
ATOM   2436 N N   . ALA   A 1 353 ? 3.38788  10.30442  11.44325 1.000 60.47571  ?  353  ALA   A N   1 
ATOM   2437 C CA  . ALA   A 1 353 ? 4.55671  9.43438   11.50576 1.000 58.99849  ?  353  ALA   A CA  1 
ATOM   2438 C C   . ALA   A 1 353 ? 4.27089  8.16559   12.29692 1.000 58.74265  ?  353  ALA   A C   1 
ATOM   2439 O O   . ALA   A 1 353 ? 4.84810  7.11234   12.00458 1.000 58.05147  ?  353  ALA   A O   1 
ATOM   2440 C CB  . ALA   A 1 353 ? 5.74128  10.18546  12.11265 1.000 57.99217  ?  353  ALA   A CB  1 
ATOM   2441 N N   . LEU   A 1 354 ? 3.38999  8.24256   13.29710 1.000 59.30182  ?  354  LEU   A N   1 
ATOM   2442 C CA  . LEU   A 1 354 ? 3.01594  7.05191   14.04987 1.000 58.69039  ?  354  LEU   A CA  1 
ATOM   2443 C C   . LEU   A 1 354 ? 2.15405  6.10115   13.23073 1.000 58.42796  ?  354  LEU   A C   1 
ATOM   2444 O O   . LEU   A 1 354 ? 2.07074  4.91486   13.56632 1.000 57.78405  ?  354  LEU   A O   1 
ATOM   2445 C CB  . LEU   A 1 354 ? 2.28380  7.44628   15.33326 1.000 58.80581  ?  354  LEU   A CB  1 
ATOM   2446 C CG  . LEU   A 1 354 ? 3.13436  8.10514   16.42084 1.000 56.97597  ?  354  LEU   A CG  1 
ATOM   2447 C CD1 . LEU   A 1 354 ? 2.31858  9.12712   17.19801 1.000 61.01137  ?  354  LEU   A CD1 1 
ATOM   2448 C CD2 . LEU   A 1 354 ? 3.71625  7.05588   17.35487 1.000 53.83193  ?  354  LEU   A CD2 1 
ATOM   2449 N N   . GLN   A 1 355 ? 1.51331  6.59255   12.17190 1.000 58.31138  ?  355  GLN   A N   1 
ATOM   2450 C CA  . GLN   A 1 355 ? 0.72358  5.76254   11.27382 1.000 59.55627  ?  355  GLN   A CA  1 
ATOM   2451 C C   . GLN   A 1 355 ? 1.48514  5.36710   10.01634 1.000 57.84022  ?  355  GLN   A C   1 
ATOM   2452 O O   . GLN   A 1 355 ? 0.92856  4.66440   9.16716  1.000 60.22739  ?  355  GLN   A O   1 
ATOM   2453 C CB  . GLN   A 1 355 ? -0.57150 6.48501   10.88758 1.000 61.57478  ?  355  GLN   A CB  1 
ATOM   2454 C CG  . GLN   A 1 355 ? -1.67912 6.37058   11.92240 1.000 65.09408  ?  355  GLN   A CG  1 
ATOM   2455 C CD  . GLN   A 1 355 ? -2.21898 4.95896   12.04608 1.000 74.58289  ?  355  GLN   A CD  1 
ATOM   2456 O OE1 . GLN   A 1 355 ? -2.64691 4.35617   11.06120 1.000 67.61094  ?  355  GLN   A OE1 1 
ATOM   2457 N NE2 . GLN   A 1 355 ? -2.20154 4.42362   13.26178 1.000 79.07500  ?  355  GLN   A NE2 1 
ATOM   2458 N N   . HIS   A 1 356 ? 2.73308  5.80293   9.87715  1.000 63.15835  ?  356  HIS   A N   1 
ATOM   2459 C CA  . HIS   A 1 356 ? 3.53141  5.42557   8.72150  1.000 61.85297  ?  356  HIS   A CA  1 
ATOM   2460 C C   . HIS   A 1 356 ? 3.76749  3.91624   8.72709  1.000 60.02986  ?  356  HIS   A C   1 
ATOM   2461 O O   . HIS   A 1 356 ? 3.90222  3.31455   9.79974  1.000 58.58902  ?  356  HIS   A O   1 
ATOM   2462 C CB  . HIS   A 1 356 ? 4.86590  6.17505   8.73163  1.000 59.68624  ?  356  HIS   A CB  1 
ATOM   2463 C CG  . HIS   A 1 356 ? 5.64161  6.05491   7.45652  1.000 58.96143  ?  356  HIS   A CG  1 
ATOM   2464 N ND1 . HIS   A 1 356 ? 6.38984  4.94105   7.14187  1.000 56.69041  ?  356  HIS   A ND1 1 
ATOM   2465 C CD2 . HIS   A 1 356 ? 5.78673  6.91077   6.41733  1.000 60.36674  ?  356  HIS   A CD2 1 
ATOM   2466 C CE1 . HIS   A 1 356 ? 6.96148  5.11520   5.96372  1.000 56.69783  ?  356  HIS   A CE1 1 
ATOM   2467 N NE2 . HIS   A 1 356 ? 6.61158  6.30234   5.50258  1.000 58.93453  ?  356  HIS   A NE2 1 
ATOM   2468 N N   . PRO   A 1 357 ? 3.80093  3.27209   7.55578  1.000 60.18961  ?  357  PRO   A N   1 
ATOM   2469 C CA  . PRO   A 1 357 ? 3.98652  1.80952   7.52490  1.000 58.59243  ?  357  PRO   A CA  1 
ATOM   2470 C C   . PRO   A 1 357 ? 5.22949  1.32385   8.25301  1.000 55.20280  ?  357  PRO   A C   1 
ATOM   2471 O O   . PRO   A 1 357 ? 5.21807  0.21201   8.79628  1.000 54.10136  ?  357  PRO   A O   1 
ATOM   2472 C CB  . PRO   A 1 357 ? 4.06071  1.48861   6.02258  1.000 59.16199  ?  357  PRO   A CB  1 
ATOM   2473 C CG  . PRO   A 1 357 ? 3.93152  2.79934   5.29145  1.000 61.12758  ?  357  PRO   A CG  1 
ATOM   2474 C CD  . PRO   A 1 357 ? 3.40432  3.81235   6.24658  1.000 62.45932  ?  357  PRO   A CD  1 
ATOM   2475 N N   . TYR   A 1 358 ? 6.30252  2.11688   8.28499  1.000 53.66963  ?  358  TYR   A N   1 
ATOM   2476 C CA  . TYR   A 1 358 ? 7.51510  1.68784   8.97243  1.000 51.21486  ?  358  TYR   A CA  1 
ATOM   2477 C C   . TYR   A 1 358 ? 7.37319  1.73308   10.48861 1.000 50.54806  ?  358  TYR   A C   1 
ATOM   2478 O O   . TYR   A 1 358 ? 8.17151  1.10302   11.19091 1.000 48.58411  ?  358  TYR   A O   1 
ATOM   2479 C CB  . TYR   A 1 358 ? 8.70240  2.55131   8.53826  1.000 49.37098  ?  358  TYR   A CB  1 
ATOM   2480 C CG  . TYR   A 1 358 ? 10.05197 1.99639   8.94334  1.000 48.41027  ?  358  TYR   A CG  1 
ATOM   2481 C CD1 . TYR   A 1 358 ? 10.62367 0.93383   8.25517  1.000 47.91103  ?  358  TYR   A CD1 1 
ATOM   2482 C CD2 . TYR   A 1 358 ? 10.75399 2.53580   10.01450 1.000 47.58488  ?  358  TYR   A CD2 1 
ATOM   2483 C CE1 . TYR   A 1 358 ? 11.85622 0.42439   8.62157  1.000 47.47319  ?  358  TYR   A CE1 1 
ATOM   2484 C CE2 . TYR   A 1 358 ? 11.98672 2.03256   10.38843 1.000 44.55989  ?  358  TYR   A CE2 1 
ATOM   2485 C CZ  . TYR   A 1 358 ? 12.53289 0.97755   9.68867  1.000 45.60860  ?  358  TYR   A CZ  1 
ATOM   2486 O OH  . TYR   A 1 358 ? 13.75926 0.47373   10.05717 1.000 45.30656  ?  358  TYR   A OH  1 
ATOM   2487 N N   . ILE   A 1 359 ? 6.37597  2.44613   11.00760 1.000 52.20968  ?  359  ILE   A N   1 
ATOM   2488 C CA  . ILE   A 1 359 ? 6.23445  2.66913   12.43766 1.000 51.93714  ?  359  ILE   A CA  1 
ATOM   2489 C C   . ILE   A 1 359 ? 5.00339  1.97144   13.00492 1.000 53.73866  ?  359  ILE   A C   1 
ATOM   2490 O O   . ILE   A 1 359 ? 5.05612  1.42141   14.10730 1.000 52.89027  ?  359  ILE   A O   1 
ATOM   2491 C CB  . ILE   A 1 359 ? 6.20384  4.18172   12.75107 1.000 52.87066  ?  359  ILE   A CB  1 
ATOM   2492 C CG1 . ILE   A 1 359 ? 7.47266  4.85891   12.23068 1.000 51.14750  ?  359  ILE   A CG1 1 
ATOM   2493 C CG2 . ILE   A 1 359 ? 6.04998  4.42367   14.24576 1.000 52.63695  ?  359  ILE   A CG2 1 
ATOM   2494 C CD1 . ILE   A 1 359 ? 8.74235  4.35791   12.88373 1.000 48.07414  ?  359  ILE   A CD1 1 
ATOM   2495 N N   . ASN   A 1 360 ? 3.89154  1.96417   12.26453 1.000 56.38623  ?  360  ASN   A N   1 
ATOM   2496 C CA  . ASN   A 1 360 ? 2.62150  1.50281   12.82110 1.000 58.64199  ?  360  ASN   A CA  1 
ATOM   2497 C C   . ASN   A 1 360 ? 2.58312  0.00472   13.11162 1.000 57.72331  ?  360  ASN   A C   1 
ATOM   2498 O O   . ASN   A 1 360 ? 1.53254  -0.48952  13.53550 1.000 59.69895  ?  360  ASN   A O   1 
ATOM   2499 C CB  . ASN   A 1 360 ? 1.46230  1.88958   11.89270 1.000 61.90682  ?  360  ASN   A CB  1 
ATOM   2500 C CG  . ASN   A 1 360 ? 1.54672  1.23463   10.51982 1.000 61.86951  ?  360  ASN   A CG  1 
ATOM   2501 O OD1 . ASN   A 1 360 ? 2.26293  0.25477   10.31548 1.000 59.66208  ?  360  ASN   A OD1 1 
ATOM   2502 N ND2 . ASN   A 1 360 ? 0.79867  1.78049   9.56864  1.000 64.47425  ?  360  ASN   A ND2 1 
ATOM   2503 N N   . VAL   A 1 361 ? 3.67679  -0.73118  12.89600 1.000 54.98775  ?  361  VAL   A N   1 
ATOM   2504 C CA  . VAL   A 1 361 ? 3.70287  -2.13437  13.29035 1.000 54.09436  ?  361  VAL   A CA  1 
ATOM   2505 C C   . VAL   A 1 361 ? 3.74367  -2.27983  14.80512 1.000 54.86282  ?  361  VAL   A C   1 
ATOM   2506 O O   . VAL   A 1 361 ? 3.47348  -3.36666  15.32957 1.000 54.04102  ?  361  VAL   A O   1 
ATOM   2507 C CB  . VAL   A 1 361 ? 4.89500  -2.86242  12.64213 1.000 51.41513  ?  361  VAL   A CB  1 
ATOM   2508 C CG1 . VAL   A 1 361 ? 4.70878  -2.94395  11.13434 1.000 53.62006  ?  361  VAL   A CG1 1 
ATOM   2509 C CG2 . VAL   A 1 361 ? 6.19918  -2.16315  12.98985 1.000 49.05241  ?  361  VAL   A CG2 1 
ATOM   2510 N N   . TRP   A 1 362 ? 4.07842  -1.20816  15.52242 1.000 55.31276  ?  362  TRP   A N   1 
ATOM   2511 C CA  . TRP   A 1 362 ? 4.05399  -1.17997  16.97744 1.000 56.67963  ?  362  TRP   A CA  1 
ATOM   2512 C C   . TRP   A 1 362 ? 2.83217  -0.45433  17.52267 1.000 65.74331  ?  362  TRP   A C   1 
ATOM   2513 O O   . TRP   A 1 362 ? 2.74540  -0.23408  18.73481 1.000 67.94762  ?  362  TRP   A O   1 
ATOM   2514 C CB  . TRP   A 1 362 ? 5.32310  -0.51463  17.51275 1.000 52.96678  ?  362  TRP   A CB  1 
ATOM   2515 C CG  . TRP   A 1 362 ? 6.58873  -1.16214  17.05768 1.000 48.38225  ?  362  TRP   A CG  1 
ATOM   2516 C CD1 . TRP   A 1 362 ? 7.40203  -0.74855  16.04356 1.000 46.76722  ?  362  TRP   A CD1 1 
ATOM   2517 C CD2 . TRP   A 1 362 ? 7.19667  -2.33579  17.60740 1.000 46.25134  ?  362  TRP   A CD2 1 
ATOM   2518 N NE1 . TRP   A 1 362 ? 8.47715  -1.59512  15.92442 1.000 45.82814  ?  362  TRP   A NE1 1 
ATOM   2519 C CE2 . TRP   A 1 362 ? 8.37467  -2.57795  16.87366 1.000 46.71786  ?  362  TRP   A CE2 1 
ATOM   2520 C CE3 . TRP   A 1 362 ? 6.85806  -3.20701  18.64743 1.000 46.77945  ?  362  TRP   A CE3 1 
ATOM   2521 C CZ2 . TRP   A 1 362 ? 9.21513  -3.65522  17.14597 1.000 48.13554  ?  362  TRP   A CZ2 1 
ATOM   2522 C CZ3 . TRP   A 1 362 ? 7.69398  -4.27527  18.91675 1.000 45.93283  ?  362  TRP   A CZ3 1 
ATOM   2523 C CH2 . TRP   A 1 362 ? 8.85847  -4.49000  18.16910 1.000 46.75729  ?  362  TRP   A CH2 1 
ATOM   2524 N N   . TYR   A 1 363 ? 1.89151  -0.08263  16.65628 1.000 70.99129  ?  363  TYR   A N   1 
ATOM   2525 C CA  . TYR   A 1 363 ? 0.78403  0.77635   17.05549 1.000 84.91885  ?  363  TYR   A CA  1 
ATOM   2526 C C   . TYR   A 1 363 ? -0.07973 0.10649   18.11679 1.000 102.62970 ?  363  TYR   A C   1 
ATOM   2527 O O   . TYR   A 1 363 ? -0.53418 -1.02818  17.94420 1.000 101.47378 ?  363  TYR   A O   1 
ATOM   2528 C CB  . TYR   A 1 363 ? -0.06089 1.13496   15.83291 1.000 85.05363  ?  363  TYR   A CB  1 
ATOM   2529 C CG  . TYR   A 1 363 ? -1.44259 1.64638   16.16519 1.000 97.24138  ?  363  TYR   A CG  1 
ATOM   2530 C CD1 . TYR   A 1 363 ? -1.61628 2.86689   16.80386 1.000 104.50360 ?  363  TYR   A CD1 1 
ATOM   2531 C CD2 . TYR   A 1 363 ? -2.57381 0.91170   15.83577 1.000 96.96072  ?  363  TYR   A CD2 1 
ATOM   2532 C CE1 . TYR   A 1 363 ? -2.87681 3.33984   17.10851 1.000 109.49754 ?  363  TYR   A CE1 1 
ATOM   2533 C CE2 . TYR   A 1 363 ? -3.83878 1.37674   16.13637 1.000 101.90361 ?  363  TYR   A CE2 1 
ATOM   2534 C CZ  . TYR   A 1 363 ? -3.98395 2.59172   16.77262 1.000 106.99804 ?  363  TYR   A CZ  1 
ATOM   2535 O OH  . TYR   A 1 363 ? -5.23942 3.06352   17.07516 1.000 107.07537 ?  363  TYR   A OH  1 
ATOM   2536 N N   . ASP   A 1 364 ? -0.30242 0.81849   19.22082 1.000 132.52154 ?  364  ASP   A N   1 
ATOM   2537 C CA  . ASP   A 1 364 ? -1.15474 0.33591   20.29991 1.000 140.23585 ?  364  ASP   A CA  1 
ATOM   2538 C C   . ASP   A 1 364 ? -1.82424 1.51229   21.00052 1.000 148.09311 ?  364  ASP   A C   1 
ATOM   2539 O O   . ASP   A 1 364 ? -1.13473 2.37704   21.55505 1.000 150.64009 ?  364  ASP   A O   1 
ATOM   2540 C CB  . ASP   A 1 364 ? -0.35130 -0.49649  21.29773 1.000 137.66539 ?  364  ASP   A CB  1 
ATOM   2541 C CG  . ASP   A 1 364 ? -1.23354 -1.18781  22.31104 1.000 142.85991 ?  364  ASP   A CG  1 
ATOM   2542 O OD1 . ASP   A 1 364 ? -0.81906 -1.33287  23.47925 1.000 148.95612 ?  364  ASP   A OD1 1 
ATOM   2543 O OD2 . ASP   A 1 364 ? -2.35817 -1.57002  21.93359 1.000 141.26636 -1 364  ASP   A OD2 1 
ATOM   2544 N N   . PRO   A 1 365 ? -3.16157 1.55928   21.01864 1.000 160.05538 ?  365  PRO   A N   1 
ATOM   2545 C CA  . PRO   A 1 365 ? -3.85058 2.78112   21.48524 1.000 158.75607 ?  365  PRO   A CA  1 
ATOM   2546 C C   . PRO   A 1 365 ? -3.45187 3.22793   22.88277 1.000 160.51541 ?  365  PRO   A C   1 
ATOM   2547 O O   . PRO   A 1 365 ? -3.20634 4.42189   23.10047 1.000 155.78433 ?  365  PRO   A O   1 
ATOM   2548 C CB  . PRO   A 1 365 ? -5.33320 2.38632   21.41180 1.000 156.22596 ?  365  PRO   A CB  1 
ATOM   2549 C CG  . PRO   A 1 365 ? -5.38541 1.27028   20.42027 1.000 155.04665 ?  365  PRO   A CG  1 
ATOM   2550 C CD  . PRO   A 1 365 ? -4.10562 0.51524   20.58860 1.000 153.62838 ?  365  PRO   A CD  1 
ATOM   2551 N N   . ALA   A 1 366 ? -3.37892 2.30250   23.84223 1.000 152.83052 ?  366  ALA   A N   1 
ATOM   2552 C CA  . ALA   A 1 366 ? -2.99638 2.67441   25.19942 1.000 150.14613 ?  366  ALA   A CA  1 
ATOM   2553 C C   . ALA   A 1 366 ? -1.54792 3.13624   25.28824 1.000 147.70356 ?  366  ALA   A C   1 
ATOM   2554 O O   . ALA   A 1 366 ? -1.18186 3.80281   26.26212 1.000 144.82515 ?  366  ALA   A O   1 
ATOM   2555 C CB  . ALA   A 1 366 ? -3.22813 1.50234   26.15374 1.000 145.98678 ?  366  ALA   A CB  1 
ATOM   2556 N N   . GLU   A 1 367 ? -0.72148 2.80361   24.29718 1.000 149.34690 ?  367  GLU   A N   1 
ATOM   2557 C CA  . GLU   A 1 367 ? 0.68112  3.19754   24.30225 1.000 142.54300 ?  367  GLU   A CA  1 
ATOM   2558 C C   . GLU   A 1 367 ? 0.92472  4.53400   23.61642 1.000 142.47383 ?  367  GLU   A C   1 
ATOM   2559 O O   . GLU   A 1 367 ? 1.83823  5.26617   24.01374 1.000 135.20310 ?  367  GLU   A O   1 
ATOM   2560 C CB  . GLU   A 1 367 ? 1.53239  2.11994   23.62497 1.000 136.82440 ?  367  GLU   A CB  1 
ATOM   2561 C CG  . GLU   A 1 367 ? 1.43743  0.75201   24.27739 1.000 141.07388 ?  367  GLU   A CG  1 
ATOM   2562 C CD  . GLU   A 1 367 ? 2.62439  0.44539   25.16649 1.000 135.57995 ?  367  GLU   A CD  1 
ATOM   2563 O OE1 . GLU   A 1 367 ? 3.75318  0.34930   24.64061 1.000 133.74051 ?  367  GLU   A OE1 1 
ATOM   2564 O OE2 . GLU   A 1 367 ? 2.42939  0.29998   26.39152 1.000 133.00109 -1 367  GLU   A OE2 1 
ATOM   2565 N N   . VAL   A 1 368 ? 0.13187  4.86998   22.59837 1.000 144.23137 ?  368  VAL   A N   1 
ATOM   2566 C CA  . VAL   A 1 368 ? 0.36601  6.09854   21.84349 1.000 135.47198 ?  368  VAL   A CA  1 
ATOM   2567 C C   . VAL   A 1 368 ? 0.04107  7.32002   22.69738 1.000 129.94346 ?  368  VAL   A C   1 
ATOM   2568 O O   . VAL   A 1 368 ? 0.90304  8.16688   22.95339 1.000 114.92582 ?  368  VAL   A O   1 
ATOM   2569 C CB  . VAL   A 1 368 ? -0.44329 6.09139   20.53362 1.000 128.70638 ?  368  VAL   A CB  1 
ATOM   2570 C CG1 . VAL   A 1 368 ? 0.03151  7.19068   19.61075 1.000 110.97394 ?  368  VAL   A CG1 1 
ATOM   2571 C CG2 . VAL   A 1 368 ? -0.30522 4.75521   19.83319 1.000 128.46553 ?  368  VAL   A CG2 1 
ATOM   2572 N N   . GLU   A 1 369 ? -1.19914 7.42196   23.16155 1.000 125.91408 ?  369  GLU   A N   1 
ATOM   2573 C CA  . GLU   A 1 369 ? -1.67743 8.60345   23.86587 1.000 119.55857 ?  369  GLU   A CA  1 
ATOM   2574 C C   . GLU   A 1 369 ? -1.58259 8.42368   25.37948 1.000 124.45187 ?  369  GLU   A C   1 
ATOM   2575 O O   . GLU   A 1 369 ? -1.39640 7.32004   25.89586 1.000 126.88402 ?  369  GLU   A O   1 
ATOM   2576 C CB  . GLU   A 1 369 ? -3.12031 8.92433   23.44750 1.000 118.68542 ?  369  GLU   A CB  1 
ATOM   2577 C CG  . GLU   A 1 369 ? -3.60449 10.35574  23.72775 1.000 114.93114 ?  369  GLU   A CG  1 
ATOM   2578 C CD  . GLU   A 1 369 ? -2.50685 11.41144  23.65046 1.000 108.55902 ?  369  GLU   A CD  1 
ATOM   2579 O OE1 . GLU   A 1 369 ? -1.70369 11.52974  24.60091 1.000 107.82623 ?  369  GLU   A OE1 1 
ATOM   2580 O OE2 . GLU   A 1 369 ? -2.45364 12.13355  22.63326 1.000 101.29371 -1 369  GLU   A OE2 1 
ATOM   2581 N N   . ALA   A 1 370 ? -1.71233 9.54294   26.08494 1.000 131.98588 ?  370  ALA   A N   1 
ATOM   2582 C CA  . ALA   A 1 370 ? -1.65180 9.60043   27.53732 1.000 129.33804 ?  370  ALA   A CA  1 
ATOM   2583 C C   . ALA   A 1 370 ? -2.47158 10.79816  27.99456 1.000 131.73601 ?  370  ALA   A C   1 
ATOM   2584 O O   . ALA   A 1 370 ? -2.73519 11.70919  27.20070 1.000 127.71237 ?  370  ALA   A O   1 
ATOM   2585 C CB  . ALA   A 1 370 ? -0.20086 9.70696   28.02828 1.000 116.51350 ?  370  ALA   A CB  1 
ATOM   2586 N N   . PRO   A 1 371 ? -2.90224 10.82413  29.25656 1.000 142.66966 ?  371  PRO   A N   1 
ATOM   2587 C CA  . PRO   A 1 371 ? -3.75757 11.92190  29.70637 1.000 149.27693 ?  371  PRO   A CA  1 
ATOM   2588 C C   . PRO   A 1 371 ? -3.01798 13.24244  29.64754 1.000 145.61554 ?  371  PRO   A C   1 
ATOM   2589 O O   . PRO   A 1 371 ? -1.78759 13.29851  29.81341 1.000 135.63986 ?  371  PRO   A O   1 
ATOM   2590 C CB  . PRO   A 1 371 ? -4.10289 11.53028  31.15164 1.000 151.32395 ?  371  PRO   A CB  1 
ATOM   2591 C CG  . PRO   A 1 371 ? -3.05220 10.55173  31.55141 1.000 148.30405 ?  371  PRO   A CG  1 
ATOM   2592 C CD  . PRO   A 1 371 ? -2.73871 9.79994   30.30184 1.000 147.88403 ?  371  PRO   A CD  1 
ATOM   2593 N N   . PRO   A 1 372 ? -3.73583 14.34018  29.40810 1.000 138.41141 ?  372  PRO   A N   1 
ATOM   2594 C CA  . PRO   A 1 372 ? -3.09194 15.65174  29.34259 1.000 127.21115 ?  372  PRO   A CA  1 
ATOM   2595 C C   . PRO   A 1 372 ? -3.19694 16.37943  30.67037 1.000 124.70330 ?  372  PRO   A C   1 
ATOM   2596 O O   . PRO   A 1 372 ? -4.29702 16.76378  31.09559 1.000 123.16730 ?  372  PRO   A O   1 
ATOM   2597 C CB  . PRO   A 1 372 ? -3.88880 16.37311  28.24583 1.000 125.80831 ?  372  PRO   A CB  1 
ATOM   2598 C CG  . PRO   A 1 372 ? -5.25259 15.69602  28.24463 1.000 133.38833 ?  372  PRO   A CG  1 
ATOM   2599 C CD  . PRO   A 1 372 ? -5.16047 14.41178  29.04538 1.000 139.10208 ?  372  PRO   A CD  1 
ATOM   2600 N N   . PRO   A 1 373 ? -2.06712 16.59930  31.35784 1.000 117.18432 ?  373  PRO   A N   1 
ATOM   2601 C CA  . PRO   A 1 373 ? -2.05864 17.29032  32.65099 1.000 111.40254 ?  373  PRO   A CA  1 
ATOM   2602 C C   . PRO   A 1 373 ? -2.23900 18.79940  32.51549 1.000 105.33535 ?  373  PRO   A C   1 
ATOM   2603 O O   . PRO   A 1 373 ? -2.01512 19.51556  33.49150 1.000 102.75451 ?  373  PRO   A O   1 
ATOM   2604 C CB  . PRO   A 1 373 ? -0.67613 16.95772  33.21015 1.000 106.59464 ?  373  PRO   A CB  1 
ATOM   2605 C CG  . PRO   A 1 373 ? 0.17399  16.78659  31.99966 1.000 101.21293 ?  373  PRO   A CG  1 
ATOM   2606 C CD  . PRO   A 1 373 ? -0.71400 16.19351  30.93767 1.000 107.84462 ?  373  PRO   A CD  1 
ATOM   2607 N N   . GLN   A 1 379 ? 0.59886  27.19387  36.57059 1.000 89.61702  ?  379  GLN   A N   1 
ATOM   2608 C CA  . GLN   A 1 379 ? 0.66604  26.99889  35.12684 1.000 92.03133  ?  379  GLN   A CA  1 
ATOM   2609 C C   . GLN   A 1 379 ? 1.44392  28.12706  34.45568 1.000 95.94975  ?  379  GLN   A C   1 
ATOM   2610 O O   . GLN   A 1 379 ? 1.21840  29.30297  34.74775 1.000 95.30651  ?  379  GLN   A O   1 
ATOM   2611 C CB  . GLN   A 1 379 ? -0.74139 26.90057  34.53383 1.000 82.16606  ?  379  GLN   A CB  1 
ATOM   2612 N N   . LEU   A 1 380 ? 2.35340  27.74879  33.55494 1.000 97.09245  ?  380  LEU   A N   1 
ATOM   2613 C CA  . LEU   A 1 380 ? 3.22669  28.67280  32.83652 1.000 100.81928 ?  380  LEU   A CA  1 
ATOM   2614 C C   . LEU   A 1 380 ? 4.04812  29.52911  33.79235 1.000 102.40632 ?  380  LEU   A C   1 
ATOM   2615 O O   . LEU   A 1 380 ? 3.57797  30.56652  34.26919 1.000 101.66484 ?  380  LEU   A O   1 
ATOM   2616 C CB  . LEU   A 1 380 ? 2.42299  29.57149  31.89220 1.000 104.24330 ?  380  LEU   A CB  1 
ATOM   2617 C CG  . LEU   A 1 380 ? 3.27231  30.20883  30.78874 1.000 108.72872 ?  380  LEU   A CG  1 
ATOM   2618 C CD1 . LEU   A 1 380 ? 2.61282  30.05487  29.42656 1.000 103.33040 ?  380  LEU   A CD1 1 
ATOM   2619 C CD2 . LEU   A 1 380 ? 3.56664  31.66877  31.08766 1.000 114.54928 ?  380  LEU   A CD2 1 
ATOM   2620 N N   . ASP   A 1 381 ? 5.28294  29.11172  34.06264 1.000 103.61020 ?  381  ASP   A N   1 
ATOM   2621 C CA  . ASP   A 1 381 ? 6.14494  29.83533  34.98762 1.000 103.13565 ?  381  ASP   A CA  1 
ATOM   2622 C C   . ASP   A 1 381 ? 7.40048  30.33969  34.28592 1.000 108.80602 ?  381  ASP   A C   1 
ATOM   2623 O O   . ASP   A 1 381 ? 8.51979  29.99562  34.67894 1.000 106.18034 ?  381  ASP   A O   1 
ATOM   2624 C CB  . ASP   A 1 381 ? 6.51391  28.94112  36.17305 1.000 95.23477  ?  381  ASP   A CB  1 
ATOM   2625 C CG  . ASP   A 1 381 ? 5.38825  28.00269  36.56624 1.000 93.75595  ?  381  ASP   A CG  1 
ATOM   2626 O OD1 . ASP   A 1 381 ? 4.28471  28.49581  36.88259 1.000 94.96728  ?  381  ASP   A OD1 1 
ATOM   2627 O OD2 . ASP   A 1 381 ? 5.60362  26.77251  36.55409 1.000 89.85234  -1 381  ASP   A OD2 1 
ATOM   2628 N N   . GLU   A 1 382 ? 7.22509  31.15593  33.24971 1.000 126.05018 ?  382  GLU   A N   1 
ATOM   2629 C CA  . GLU   A 1 382 ? 8.33530  31.71564  32.48885 1.000 126.56132 ?  382  GLU   A CA  1 
ATOM   2630 C C   . GLU   A 1 382 ? 8.52064  33.17730  32.87965 1.000 119.01645 ?  382  GLU   A C   1 
ATOM   2631 O O   . GLU   A 1 382 ? 7.61395  33.99523  32.68658 1.000 113.73469 ?  382  GLU   A O   1 
ATOM   2632 C CB  . GLU   A 1 382 ? 8.08722  31.58417  30.98626 1.000 124.98334 ?  382  GLU   A CB  1 
ATOM   2633 C CG  . GLU   A 1 382 ? 7.78126  30.16538  30.53016 1.000 120.37104 ?  382  GLU   A CG  1 
ATOM   2634 C CD  . GLU   A 1 382 ? 9.03494  29.34913  30.27983 1.000 120.54423 ?  382  GLU   A CD  1 
ATOM   2635 O OE1 . GLU   A 1 382 ? 9.93235  29.83887  29.56223 1.000 117.25550 ?  382  GLU   A OE1 1 
ATOM   2636 O OE2 . GLU   A 1 382 ? 9.12330  28.21770  30.80128 1.000 116.48277 -1 382  GLU   A OE2 1 
ATOM   2637 N N   . ARG   A 1 383 ? 9.69232  33.50032  33.42148 1.000 105.49789 ?  383  ARG   A N   1 
ATOM   2638 C CA  . ARG   A 1 383 ? 9.98357  34.84389  33.90547 1.000 96.92760  ?  383  ARG   A CA  1 
ATOM   2639 C C   . ARG   A 1 383 ? 11.49775 34.98595  34.02289 1.000 89.05031  ?  383  ARG   A C   1 
ATOM   2640 O O   . ARG   A 1 383 ? 12.25562 34.08664  33.64897 1.000 84.35947  ?  383  ARG   A O   1 
ATOM   2641 C CB  . ARG   A 1 383 ? 9.27411  35.10568  35.23972 1.000 95.11321  ?  383  ARG   A CB  1 
ATOM   2642 C CG  . ARG   A 1 383 ? 9.07662  36.57382  35.59171 1.000 93.43398  ?  383  ARG   A CG  1 
ATOM   2643 C CD  . ARG   A 1 383 ? 7.71350  36.81839  36.20599 1.000 96.78358  ?  383  ARG   A CD  1 
ATOM   2644 N NE  . ARG   A 1 383 ? 7.45725  35.95545  37.35265 1.000 92.11468  ?  383  ARG   A NE  1 
ATOM   2645 C CZ  . ARG   A 1 383 ? 7.06415  36.38946  38.54215 1.000 90.69866  ?  383  ARG   A CZ  1 
ATOM   2646 N NH1 . ARG   A 1 383 ? 6.88761  37.67832  38.78392 1.000 91.31689  ?  383  ARG   A NH1 1 
ATOM   2647 N NH2 . ARG   A 1 383 ? 6.83970  35.50831  39.51254 1.000 88.97680  ?  383  ARG   A NH2 1 
ATOM   2648 N N   . GLU   A 1 384 ? 11.93445 36.13453  34.53753 1.000 83.16215  ?  384  GLU   A N   1 
ATOM   2649 C CA  . GLU   A 1 384 ? 13.34445 36.41083  34.78615 1.000 82.83609  ?  384  GLU   A CA  1 
ATOM   2650 C C   . GLU   A 1 384 ? 13.49381 36.90157  36.21764 1.000 76.45041  ?  384  GLU   A C   1 
ATOM   2651 O O   . GLU   A 1 384 ? 12.89313 37.91344  36.59366 1.000 73.97337  ?  384  GLU   A O   1 
ATOM   2652 C CB  . GLU   A 1 384 ? 13.88981 37.44865  33.80035 1.000 83.03740  ?  384  GLU   A CB  1 
ATOM   2653 C CG  . GLU   A 1 384 ? 15.24645 38.01653  34.18596 1.000 82.81158  ?  384  GLU   A CG  1 
ATOM   2654 C CD  . GLU   A 1 384 ? 16.22323 38.02954  33.02707 1.000 82.10608  ?  384  GLU   A CD  1 
ATOM   2655 O OE1 . GLU   A 1 384 ? 15.76941 37.99852  31.86360 1.000 87.54338  ?  384  GLU   A OE1 1 
ATOM   2656 O OE2 . GLU   A 1 384 ? 17.44537 38.06846  33.27983 1.000 83.11268  -1 384  GLU   A OE2 1 
ATOM   2657 N N   . HIS   A 1 385 ? 14.28657 36.18752  37.01078 1.000 67.96035  ?  385  HIS   A N   1 
ATOM   2658 C CA  . HIS   A 1 385 ? 14.49397 36.50240  38.41591 1.000 63.86356  ?  385  HIS   A CA  1 
ATOM   2659 C C   . HIS   A 1 385 ? 15.97610 36.72291  38.69014 1.000 60.82093  ?  385  HIS   A C   1 
ATOM   2660 O O   . HIS   A 1 385 ? 16.83300 36.52482  37.82497 1.000 65.95724  ?  385  HIS   A O   1 
ATOM   2661 C CB  . HIS   A 1 385 ? 13.95910 35.38349  39.31995 1.000 59.52943  ?  385  HIS   A CB  1 
ATOM   2662 C CG  . HIS   A 1 385 ? 12.46549 35.32789  39.40245 1.000 65.35524  ?  385  HIS   A CG  1 
ATOM   2663 N ND1 . HIS   A 1 385 ? 11.65142 35.47480  38.30035 1.000 77.53100  ?  385  HIS   A ND1 1 
ATOM   2664 C CD2 . HIS   A 1 385 ? 11.63849 35.13768  40.45765 1.000 68.49128  ?  385  HIS   A CD2 1 
ATOM   2665 C CE1 . HIS   A 1 385 ? 10.38758 35.37928  38.67265 1.000 84.83284  ?  385  HIS   A CE1 1 
ATOM   2666 N NE2 . HIS   A 1 385 ? 10.35212 35.17462  39.97694 1.000 80.70857  ?  385  HIS   A NE2 1 
ATOM   2667 N N   . THR   A 1 386 ? 16.26895 37.14220  39.91788 1.000 55.78383  ?  386  THR   A N   1 
ATOM   2668 C CA  . THR   A 1 386 ? 17.64253 37.24169  40.37961 1.000 52.51033  ?  386  THR   A CA  1 
ATOM   2669 C C   . THR   A 1 386 ? 18.13704 35.87405  40.84663 1.000 53.13161  ?  386  THR   A C   1 
ATOM   2670 O O   . THR   A 1 386 ? 17.38732 34.89571  40.89834 1.000 49.52399  ?  386  THR   A O   1 
ATOM   2671 C CB  . THR   A 1 386 ? 17.75997 38.26348  41.50982 1.000 53.07498  ?  386  THR   A CB  1 
ATOM   2672 O OG1 . THR   A 1 386 ? 16.93862 37.85560  42.61121 1.000 52.74927  ?  386  THR   A OG1 1 
ATOM   2673 C CG2 . THR   A 1 386 ? 17.31322 39.63798  41.03420 1.000 52.43393  ?  386  THR   A CG2 1 
ATOM   2674 N N   . ILE   A 1 387 ? 19.42450 35.81122  41.19393 1.000 50.17032  ?  387  ILE   A N   1 
ATOM   2675 C CA  . ILE   A 1 387 ? 19.99044 34.54786  41.65556 1.000 47.33059  ?  387  ILE   A CA  1 
ATOM   2676 C C   . ILE   A 1 387 ? 19.45876 34.18886  43.03696 1.000 47.41724  ?  387  ILE   A C   1 
ATOM   2677 O O   . ILE   A 1 387 ? 19.38725 33.00654  43.39361 1.000 47.25674  ?  387  ILE   A O   1 
ATOM   2678 C CB  . ILE   A 1 387 ? 21.52841 34.60739  41.63925 1.000 44.71296  ?  387  ILE   A CB  1 
ATOM   2679 C CG1 . ILE   A 1 387 ? 22.03129 35.75851  42.50981 1.000 48.04447  ?  387  ILE   A CG1 1 
ATOM   2680 C CG2 . ILE   A 1 387 ? 22.04013 34.74918  40.21447 1.000 44.10726  ?  387  ILE   A CG2 1 
ATOM   2681 C CD1 . ILE   A 1 387 ? 23.53056 35.91061  42.49691 1.000 46.02988  ?  387  ILE   A CD1 1 
ATOM   2682 N N   . GLU   A 1 388 ? 19.07847 35.18737  43.83573 1.000 49.02202  ?  388  GLU   A N   1 
ATOM   2683 C CA  . GLU   A 1 388 ? 18.46748 34.90360  45.12898 1.000 53.07370  ?  388  GLU   A CA  1 
ATOM   2684 C C   . GLU   A 1 388 ? 17.01533 34.47078  44.97014 1.000 49.34827  ?  388  GLU   A C   1 
ATOM   2685 O O   . GLU   A 1 388 ? 16.55892 33.55340  45.66149 1.000 47.52714  ?  388  GLU   A O   1 
ATOM   2686 C CB  . GLU   A 1 388 ? 18.56547 36.12888  46.03892 1.000 55.94626  ?  388  GLU   A CB  1 
ATOM   2687 C CG  . GLU   A 1 388 ? 19.87482 36.23137  46.80656 1.000 55.48813  ?  388  GLU   A CG  1 
ATOM   2688 C CD  . GLU   A 1 388 ? 20.22162 34.95270  47.54445 1.000 55.83454  ?  388  GLU   A CD  1 
ATOM   2689 O OE1 . GLU   A 1 388 ? 21.29096 34.37196  47.26196 1.000 54.45589  ?  388  GLU   A OE1 1 
ATOM   2690 O OE2 . GLU   A 1 388 ? 19.42541 34.52854  48.40831 1.000 61.39432  -1 388  GLU   A OE2 1 
ATOM   2691 N N   . GLU   A 1 389 ? 16.27787 35.11818  44.06452 1.000 50.31613  ?  389  GLU   A N   1 
ATOM   2692 C CA  . GLU   A 1 389 ? 14.90080 34.71181  43.80549 1.000 50.96910  ?  389  GLU   A CA  1 
ATOM   2693 C C   . GLU   A 1 389 ? 14.84828 33.34229  43.14059 1.000 49.89597  ?  389  GLU   A C   1 
ATOM   2694 O O   . GLU   A 1 389 ? 13.95469 32.53837  43.43129 1.000 47.03335  ?  389  GLU   A O   1 
ATOM   2695 C CB  . GLU   A 1 389 ? 14.19941 35.75604  42.93744 1.000 53.51166  ?  389  GLU   A CB  1 
ATOM   2696 C CG  . GLU   A 1 389 ? 13.85237 37.04395  43.66422 1.000 53.88245  ?  389  GLU   A CG  1 
ATOM   2697 C CD  . GLU   A 1 389 ? 13.59426 38.19556  42.71265 1.000 54.68624  ?  389  GLU   A CD  1 
ATOM   2698 O OE1 . GLU   A 1 389 ? 14.03795 38.11573  41.54762 1.000 57.28838  ?  389  GLU   A OE1 1 
ATOM   2699 O OE2 . GLU   A 1 389 ? 12.94676 39.17947  43.12841 1.000 51.15295  -1 389  GLU   A OE2 1 
ATOM   2700 N N   . TRP   A 1 390 ? 15.79620 33.06039  42.24249 1.000 50.44090  ?  390  TRP   A N   1 
ATOM   2701 C CA  . TRP   A 1 390 ? 15.84843 31.74720  41.60965 1.000 49.03756  ?  390  TRP   A CA  1 
ATOM   2702 C C   . TRP   A 1 390 ? 16.19642 30.65720  42.61289 1.000 47.46066  ?  390  TRP   A C   1 
ATOM   2703 O O   . TRP   A 1 390 ? 15.75090 29.51391  42.46346 1.000 43.27269  ?  390  TRP   A O   1 
ATOM   2704 C CB  . TRP   A 1 390 ? 16.86455 31.74933  40.46741 1.000 47.23562  ?  390  TRP   A CB  1 
ATOM   2705 C CG  . TRP   A 1 390 ? 16.30529 32.16856  39.14009 1.000 52.08554  ?  390  TRP   A CG  1 
ATOM   2706 C CD1 . TRP   A 1 390 ? 16.79275 33.14465  38.32164 1.000 55.40000  ?  390  TRP   A CD1 1 
ATOM   2707 C CD2 . TRP   A 1 390 ? 15.16380 31.61618  38.46866 1.000 53.76283  ?  390  TRP   A CD2 1 
ATOM   2708 N NE1 . TRP   A 1 390 ? 16.02441 33.24034  37.18762 1.000 58.16560  ?  390  TRP   A NE1 1 
ATOM   2709 C CE2 . TRP   A 1 390 ? 15.01821 32.31322  37.25279 1.000 57.77881  ?  390  TRP   A CE2 1 
ATOM   2710 C CE3 . TRP   A 1 390 ? 14.25018 30.60318  38.77819 1.000 52.29310  ?  390  TRP   A CE3 1 
ATOM   2711 C CZ2 . TRP   A 1 390 ? 13.99717 32.03108  36.34762 1.000 59.22216  ?  390  TRP   A CZ2 1 
ATOM   2712 C CZ3 . TRP   A 1 390 ? 13.23685 30.32543  37.87865 1.000 52.16858  ?  390  TRP   A CZ3 1 
ATOM   2713 C CH2 . TRP   A 1 390 ? 13.11888 31.03638  36.67794 1.000 54.49961  ?  390  TRP   A CH2 1 
ATOM   2714 N N   . LYS   A 1 391 ? 16.99042 30.98982  43.63268 1.000 47.17430  ?  391  LYS   A N   1 
ATOM   2715 C CA  . LYS   A 1 391 ? 17.35241 30.00787  44.64919 1.000 45.33431  ?  391  LYS   A CA  1 
ATOM   2716 C C   . LYS   A 1 391 ? 16.12281 29.53307  45.41249 1.000 44.33575  ?  391  LYS   A C   1 
ATOM   2717 O O   . LYS   A 1 391 ? 15.89532 28.32663  45.55769 1.000 42.42828  ?  391  LYS   A O   1 
ATOM   2718 C CB  . LYS   A 1 391 ? 18.38516 30.60748  45.60377 1.000 42.25997  ?  391  LYS   A CB  1 
ATOM   2719 C CG  . LYS   A 1 391 ? 19.06778 29.59992  46.51168 1.000 41.40483  ?  391  LYS   A CG  1 
ATOM   2720 C CD  . LYS   A 1 391 ? 20.27558 30.22404  47.19106 1.000 41.12166  ?  391  LYS   A CD  1 
ATOM   2721 C CE  . LYS   A 1 391 ? 20.86094 29.30418  48.24599 1.000 44.45649  ?  391  LYS   A CE  1 
ATOM   2722 N NZ  . LYS   A 1 391 ? 22.05501 29.90742  48.90102 1.000 47.46773  ?  391  LYS   A NZ  1 
ATOM   2723 N N   . GLU   A 1 392 ? 15.31142 30.47437  45.90231 1.000 43.57367  ?  392  GLU   A N   1 
ATOM   2724 C CA  . GLU   A 1 392 ? 14.11508 30.10524  46.65280 1.000 45.49081  ?  392  GLU   A CA  1 
ATOM   2725 C C   . GLU   A 1 392 ? 13.11562 29.36313  45.77437 1.000 46.58811  ?  392  GLU   A C   1 
ATOM   2726 O O   . GLU   A 1 392 ? 12.46750 28.41188  46.22700 1.000 46.96942  ?  392  GLU   A O   1 
ATOM   2727 C CB  . GLU   A 1 392 ? 13.47042 31.35116  47.26054 1.000 46.36547  ?  392  GLU   A CB  1 
ATOM   2728 C CG  . GLU   A 1 392 ? 12.20175 31.06668  48.04882 1.000 48.23457  ?  392  GLU   A CG  1 
ATOM   2729 C CD  . GLU   A 1 392 ? 11.88679 32.14783  49.06389 1.000 50.14901  ?  392  GLU   A CD  1 
ATOM   2730 O OE1 . GLU   A 1 392 ? 12.01631 33.34236  48.72345 1.000 49.27667  ?  392  GLU   A OE1 1 
ATOM   2731 O OE2 . GLU   A 1 392 ? 11.50703 31.80172  50.20251 1.000 50.27217  -1 392  GLU   A OE2 1 
ATOM   2732 N N   . LEU   A 1 393 ? 12.97603 29.78416  44.51444 1.000 46.88431  ?  393  LEU   A N   1 
ATOM   2733 C CA  . LEU   A 1 393 ? 12.04042 29.12049  43.61163 1.000 47.36324  ?  393  LEU   A CA  1 
ATOM   2734 C C   . LEU   A 1 393 ? 12.42494 27.66261  43.39215 1.000 46.18565  ?  393  LEU   A C   1 
ATOM   2735 O O   . LEU   A 1 393 ? 11.55761 26.78212  43.35368 1.000 46.65672  ?  393  LEU   A O   1 
ATOM   2736 C CB  . LEU   A 1 393 ? 11.98051 29.86593  42.27833 1.000 47.74698  ?  393  LEU   A CB  1 
ATOM   2737 C CG  . LEU   A 1 393 ? 10.98072 31.01996  42.17861 1.000 50.59394  ?  393  LEU   A CG  1 
ATOM   2738 C CD1 . LEU   A 1 393 ? 10.97717 31.60526  40.77455 1.000 53.69189  ?  393  LEU   A CD1 1 
ATOM   2739 C CD2 . LEU   A 1 393 ? 9.58605  30.56147  42.57548 1.000 52.40904  ?  393  LEU   A CD2 1 
ATOM   2740 N N   . ILE   A 1 394 ? 13.72161 27.38790  43.25114 1.000 46.00102  ?  394  ILE   A N   1 
ATOM   2741 C CA  . ILE   A 1 394 ? 14.17692 26.01544  43.05920 1.000 46.22994  ?  394  ILE   A CA  1 
ATOM   2742 C C   . ILE   A 1 394 ? 14.15259 25.24976  44.37695 1.000 46.27404  ?  394  ILE   A C   1 
ATOM   2743 O O   . ILE   A 1 394 ? 13.79491 24.06654  44.41344 1.000 49.57165  ?  394  ILE   A O   1 
ATOM   2744 C CB  . ILE   A 1 394 ? 15.57821 26.01317  42.41986 1.000 42.11717  ?  394  ILE   A CB  1 
ATOM   2745 C CG1 . ILE   A 1 394 ? 15.50257 26.50668  40.97321 1.000 43.32413  ?  394  ILE   A CG1 1 
ATOM   2746 C CG2 . ILE   A 1 394 ? 16.20020 24.62545  42.47823 1.000 37.52378  ?  394  ILE   A CG2 1 
ATOM   2747 C CD1 . ILE   A 1 394 ? 16.83947 26.91979  40.39469 1.000 38.66553  ?  394  ILE   A CD1 1 
ATOM   2748 N N   . TYR   A 1 395 ? 14.51780 25.91405  45.47736 1.000 45.46715  ?  395  TYR   A N   1 
ATOM   2749 C CA  . TYR   A 1 395 ? 14.55310 25.24896  46.77693 1.000 44.87984  ?  395  TYR   A CA  1 
ATOM   2750 C C   . TYR   A 1 395 ? 13.16933 24.76573  47.19400 1.000 49.45835  ?  395  TYR   A C   1 
ATOM   2751 O O   . TYR   A 1 395 ? 13.02347 23.65327  47.71471 1.000 46.66641  ?  395  TYR   A O   1 
ATOM   2752 C CB  . TYR   A 1 395 ? 15.13133 26.19590  47.82928 1.000 45.43267  ?  395  TYR   A CB  1 
ATOM   2753 C CG  . TYR   A 1 395 ? 15.20818 25.61375  49.22369 1.000 47.11686  ?  395  TYR   A CG  1 
ATOM   2754 C CD1 . TYR   A 1 395 ? 16.18674 24.68698  49.55806 1.000 45.18140  ?  395  TYR   A CD1 1 
ATOM   2755 C CD2 . TYR   A 1 395 ? 14.30788 25.99939  50.20856 1.000 44.73892  ?  395  TYR   A CD2 1 
ATOM   2756 C CE1 . TYR   A 1 395 ? 16.26347 24.15620  50.83277 1.000 46.95622  ?  395  TYR   A CE1 1 
ATOM   2757 C CE2 . TYR   A 1 395 ? 14.37655 25.47391  51.48588 1.000 45.60657  ?  395  TYR   A CE2 1 
ATOM   2758 C CZ  . TYR   A 1 395 ? 15.35606 24.55324  51.79222 1.000 47.41685  ?  395  TYR   A CZ  1 
ATOM   2759 O OH  . TYR   A 1 395 ? 15.42820 24.02713  53.06160 1.000 48.77676  ?  395  TYR   A OH  1 
ATOM   2760 N N   . LYS   A 1 396 ? 12.13879 25.58591  46.97158 1.000 52.78518  ?  396  LYS   A N   1 
ATOM   2761 C CA  . LYS   A 1 396 ? 10.79014 25.18701  47.36013 1.000 55.70477  ?  396  LYS   A CA  1 
ATOM   2762 C C   . LYS   A 1 396 ? 10.25693 24.06675  46.47576 1.000 54.20117  ?  396  LYS   A C   1 
ATOM   2763 O O   . LYS   A 1 396 ? 9.41941  23.27430  46.92192 1.000 56.08804  ?  396  LYS   A O   1 
ATOM   2764 C CB  . LYS   A 1 396 ? 9.85126  26.39413  47.32775 1.000 60.48923  ?  396  LYS   A CB  1 
ATOM   2765 C CG  . LYS   A 1 396 ? 9.55474  26.93388  45.93872 1.000 56.68105  ?  396  LYS   A CG  1 
ATOM   2766 C CD  . LYS   A 1 396 ? 8.55732  28.08042  45.99831 1.000 59.13569  ?  396  LYS   A CD  1 
ATOM   2767 C CE  . LYS   A 1 396 ? 8.99893  29.14496  46.98945 1.000 55.01388  ?  396  LYS   A CE  1 
ATOM   2768 N NZ  . LYS   A 1 396 ? 8.24111  30.41524  46.81795 1.000 66.27674  ?  396  LYS   A NZ  1 
ATOM   2769 N N   . GLU   A 1 397 ? 10.72566 23.98021  45.22813 1.000 53.21912  ?  397  GLU   A N   1 
ATOM   2770 C CA  . GLU   A 1 397 ? 10.33430 22.86336  44.37594 1.000 56.82945  ?  397  GLU   A CA  1 
ATOM   2771 C C   . GLU   A 1 397 ? 10.95148 21.55760  44.85686 1.000 56.11735  ?  397  GLU   A C   1 
ATOM   2772 O O   . GLU   A 1 397 ? 10.33498 20.49462  44.72282 1.000 59.87698  ?  397  GLU   A O   1 
ATOM   2773 C CB  . GLU   A 1 397 ? 10.73244 23.14037  42.92658 1.000 55.25975  ?  397  GLU   A CB  1 
ATOM   2774 C CG  . GLU   A 1 397 ? 9.76789  22.56977  41.90060 1.000 57.40581  ?  397  GLU   A CG  1 
ATOM   2775 C CD  . GLU   A 1 397 ? 8.37790  23.16093  42.01942 1.000 60.92186  ?  397  GLU   A CD  1 
ATOM   2776 O OE1 . GLU   A 1 397 ? 8.18585  24.32104  41.59865 1.000 59.55301  ?  397  GLU   A OE1 1 
ATOM   2777 O OE2 . GLU   A 1 397 ? 7.47682  22.46588  42.53457 1.000 64.08465  -1 397  GLU   A OE2 1 
ATOM   2778 N N   . VAL   A 1 398 ? 12.16101 21.61812  45.41709 1.000 51.77609  ?  398  VAL   A N   1 
ATOM   2779 C CA  . VAL   A 1 398 ? 12.77784 20.42781  45.99198 1.000 52.04619  ?  398  VAL   A CA  1 
ATOM   2780 C C   . VAL   A 1 398 ? 12.03567 20.00094  47.25268 1.000 60.96068  ?  398  VAL   A C   1 
ATOM   2781 O O   . VAL   A 1 398 ? 11.82663 18.80528  47.49367 1.000 61.37377  ?  398  VAL   A O   1 
ATOM   2782 C CB  . VAL   A 1 398 ? 14.27064 20.68771  46.26750 1.000 47.69159  ?  398  VAL   A CB  1 
ATOM   2783 C CG1 . VAL   A 1 398 ? 14.86047 19.58729  47.13773 1.000 49.05916  ?  398  VAL   A CG1 1 
ATOM   2784 C CG2 . VAL   A 1 398 ? 15.03631 20.80798  44.96010 1.000 47.39977  ?  398  VAL   A CG2 1 
ATOM   2785 N N   . MET   A 1 399 ? 11.61499 20.96917  48.07088 1.000 60.28902  ?  399  MET   A N   1 
ATOM   2786 C CA  . MET   A 1 399 ? 10.89005 20.64056  49.29341 1.000 64.72670  ?  399  MET   A CA  1 
ATOM   2787 C C   . MET   A 1 399 ? 9.47653  20.15476  48.99878 1.000 75.09035  ?  399  MET   A C   1 
ATOM   2788 O O   . MET   A 1 399 ? 8.93216  19.35125  49.76432 1.000 78.19960  ?  399  MET   A O   1 
ATOM   2789 C CB  . MET   A 1 399 ? 10.85446 21.85372  50.22309 1.000 60.85635  ?  399  MET   A CB  1 
ATOM   2790 C CG  . MET   A 1 399 ? 12.19712 22.19175  50.85194 1.000 56.06854  ?  399  MET   A CG  1 
ATOM   2791 S SD  . MET   A 1 399 ? 13.32081 20.78142  50.90121 1.000 55.99477  ?  399  MET   A SD  1 
ATOM   2792 C CE  . MET   A 1 399 ? 13.09724 20.23117  52.59140 1.000 57.98651  ?  399  MET   A CE  1 
ATOM   2793 N N   . ASN   A 1 400 ? 8.87902  20.62660  47.90489 1.000 91.83044  ?  400  ASN   A N   1 
ATOM   2794 C CA  . ASN   A 1 400 ? 7.53530  20.23534  47.46737 1.000 91.07302  ?  400  ASN   A CA  1 
ATOM   2795 C C   . ASN   A 1 400 ? 6.51657  20.22872  48.60726 1.000 98.40207  ?  400  ASN   A C   1 
ATOM   2796 O O   . ASN   A 1 400 ? 5.74737  21.17548  48.77017 1.000 100.16181 ?  400  ASN   A O   1 
ATOM   2797 C CB  . ASN   A 1 400 ? 7.58184  18.86343  46.77266 1.000 94.06559  ?  400  ASN   A CB  1 
ATOM   2798 C CG  . ASN   A 1 400 ? 7.50023  17.69452  47.74429 1.000 102.19652 ?  400  ASN   A CG  1 
ATOM   2799 O OD1 . ASN   A 1 400 ? 6.43298  17.37277  48.26830 1.000 106.58496 ?  400  ASN   A OD1 1 
ATOM   2800 N ND2 . ASN   A 1 400 ? 8.63598  17.04620  47.97965 1.000 101.55337 ?  400  ASN   A ND2 1 
HETATM 2801 C C1  . A1ACP B 2 .   ? 22.52269 5.95764   31.66674 1.000 36.23971  ?  1101 A1ACP A C1  1 
HETATM 2802 C C2  . A1ACP B 2 .   ? 21.35043 8.15448   32.41185 1.000 34.97747  ?  1101 A1ACP A C2  1 
HETATM 2803 N N3  . A1ACP B 2 .   ? 20.43284 12.32046  33.18577 1.000 39.64016  ?  1101 A1ACP A N3  1 
HETATM 2804 C C4  . A1ACP B 2 .   ? 19.50672 7.16475   33.25598 1.000 36.80662  ?  1101 A1ACP A C4  1 
HETATM 2805 C C5  . A1ACP B 2 .   ? 22.24191 9.14953   32.04443 1.000 36.10074  ?  1101 A1ACP A C5  1 
HETATM 2806 C C6  . A1ACP B 2 .   ? 21.88228 10.46039  32.32310 1.000 34.70817  ?  1101 A1ACP A C6  1 
HETATM 2807 C C7  . A1ACP B 2 .   ? 20.67200 10.90599  32.95957 1.000 35.45942  ?  1101 A1ACP A C7  1 
HETATM 2808 C C8  . A1ACP B 2 .   ? 19.81047 9.85245   33.30802 1.000 38.18574  ?  1101 A1ACP A C8  1 
HETATM 2809 C C9  . A1ACP B 2 .   ? 19.22505 13.04943  33.51816 1.000 40.85421  ?  1101 A1ACP A C9  1 
HETATM 2810 C C10 . A1ACP B 2 .   ? 22.97667 4.63811   32.19861 1.000 38.79713  ?  1101 A1ACP A C10 1 
HETATM 2811 C C11 . A1ACP B 2 .   ? 24.01261 4.01084   31.53145 1.000 40.04618  ?  1101 A1ACP A C11 1 
HETATM 2812 C C12 . A1ACP B 2 .   ? 23.27656 6.28520   30.57176 1.000 38.04223  ?  1101 A1ACP A C12 1 
HETATM 2813 C C13 . A1ACP B 2 .   ? 24.62698 2.67464   31.88942 1.000 39.23418  ?  1101 A1ACP A C13 1 
HETATM 2814 C C14 . A1ACP B 2 .   ? 24.64268 0.34024   32.93007 1.000 42.04521  ?  1101 A1ACP A C14 1 
HETATM 2815 C C15 . A1ACP B 2 .   ? 18.37778 12.81700  34.66255 1.000 46.62000  ?  1101 A1ACP A C15 1 
HETATM 2816 C C16 . A1ACP B 2 .   ? 17.22414 13.59627  34.87961 1.000 44.71265  ?  1101 A1ACP A C16 1 
HETATM 2817 C C17 . A1ACP B 2 .   ? 16.85747 14.61745  33.99833 1.000 44.80142  ?  1101 A1ACP A C17 1 
HETATM 2818 C C18 . A1ACP B 2 .   ? 17.65061 14.86603  32.88725 1.000 43.09532  ?  1101 A1ACP A C18 1 
HETATM 2819 C C19 . A1ACP B 2 .   ? 18.79943 14.09365  32.66863 1.000 41.30000  ?  1101 A1ACP A C19 1 
HETATM 2820 C C20 . A1ACP B 2 .   ? 23.70449 -0.82121  33.43851 1.000 42.01148  ?  1101 A1ACP A C20 1 
HETATM 2821 C C21 . A1ACP B 2 .   ? 25.26882 0.22224   34.36822 1.000 43.62530  ?  1101 A1ACP A C21 1 
HETATM 2822 C C22 . A1ACP B 2 .   ? 17.97633 11.73085  36.77933 1.000 38.06884  ?  1101 A1ACP A C22 1 
HETATM 2823 C C3  . A1ACP B 2 .   ? 20.12034 8.48280   33.05004 1.000 35.11866  ?  1101 A1ACP A C3  1 
HETATM 2824 F F1  . A1ACP B 2 .   ? 22.80606 11.39425  31.93109 1.000 37.50200  ?  1101 A1ACP A F1  1 
HETATM 2825 N N1  . A1ACP B 2 .   ? 21.45835 6.75911   32.24955 1.000 35.06707  ?  1101 A1ACP A N1  1 
HETATM 2826 N N2  . A1ACP B 2 .   ? 20.30127 6.17763   32.78603 1.000 35.91757  ?  1101 A1ACP A N2  1 
HETATM 2827 N N4  . A1ACP B 2 .   ? 23.99607 1.62263   32.60773 1.000 41.34716  ?  1101 A1ACP A N4  1 
HETATM 2828 O O1  . A1ACP B 2 .   ? 25.78294 2.45531   31.53379 1.000 38.84104  ?  1101 A1ACP A O1  1 
HETATM 2829 O O2  . A1ACP B 2 .   ? 24.30018 -0.77850  34.75309 1.000 44.58601  ?  1101 A1ACP A O2  1 
HETATM 2830 O O3  . A1ACP B 2 .   ? 18.70412 11.81560  35.56188 1.000 39.60778  ?  1101 A1ACP A O3  1 
HETATM 2831 S S1  . A1ACP B 2 .   ? 24.46110 5.06020   30.20732 1.000 38.20567  ?  1101 A1ACP A S1  1 
HETATM 2832 O O   . HOH   C 3 .   ? 7.30340  -5.45246  14.39544 1.000 51.00687  ?  1201 HOH   A O   1 
HETATM 2833 O O   . HOH   C 3 .   ? 12.39108 -13.30684 -3.90810 1.000 45.26873  ?  1202 HOH   A O   1 
HETATM 2834 O O   . HOH   C 3 .   ? 20.99045 28.08718  -1.66861 1.000 72.13497  ?  1203 HOH   A O   1 
HETATM 2835 O O   . HOH   C 3 .   ? 26.79285 19.21238  39.02586 1.000 45.85644  ?  1204 HOH   A O   1 
HETATM 2836 O O   . HOH   C 3 .   ? 31.25526 18.85967  43.38438 1.000 56.26667  ?  1205 HOH   A O   1 
HETATM 2837 O O   . HOH   C 3 .   ? 28.22065 2.19662   51.90896 1.000 62.41232  ?  1206 HOH   A O   1 
HETATM 2838 O O   . HOH   C 3 .   ? 20.18977 15.19109  57.89792 1.000 47.55446  ?  1207 HOH   A O   1 
HETATM 2839 O O   . HOH   C 3 .   ? 29.59144 12.37097  12.35516 1.000 33.28218  ?  1208 HOH   A O   1 
HETATM 2840 O O   . HOH   C 3 .   ? 26.10013 23.90787  14.57156 1.000 38.74724  ?  1209 HOH   A O   1 
HETATM 2841 O O   . HOH   C 3 .   ? 22.21972 1.91762   13.73231 1.000 37.53401  ?  1210 HOH   A O   1 
HETATM 2842 O O   . HOH   C 3 .   ? 23.29866 16.08118  27.45643 1.000 37.41660  ?  1211 HOH   A O   1 
HETATM 2843 O O   . HOH   C 3 .   ? 15.14508 6.23721   44.94133 1.000 36.68483  ?  1212 HOH   A O   1 
HETATM 2844 O O   . HOH   C 3 .   ? 14.67117 12.11651  56.71986 1.000 56.05389  ?  1213 HOH   A O   1 
HETATM 2845 O O   . HOH   C 3 .   ? 7.86515  24.05994  12.76081 1.000 47.56573  ?  1214 HOH   A O   1 
HETATM 2846 O O   . HOH   C 3 .   ? 25.01827 16.56956  23.57213 1.000 31.91360  ?  1215 HOH   A O   1 
HETATM 2847 O O   . HOH   C 3 .   ? 22.36161 13.31993  12.69884 1.000 28.20902  ?  1216 HOH   A O   1 
HETATM 2848 O O   . HOH   C 3 .   ? 24.02250 1.50719   8.08136  1.000 41.86960  ?  1217 HOH   A O   1 
HETATM 2849 O O   . HOH   C 3 .   ? 17.60480 39.41693  44.61351 1.000 49.35445  ?  1218 HOH   A O   1 
HETATM 2850 O O   . HOH   C 3 .   ? 11.66022 4.38803   -0.55730 1.000 48.61758  ?  1219 HOH   A O   1 
HETATM 2851 O O   . HOH   C 3 .   ? 23.12309 22.42961  37.50678 1.000 50.35487  ?  1220 HOH   A O   1 
HETATM 2852 O O   . HOH   C 3 .   ? 29.92673 21.46087  8.52712  1.000 40.97802  ?  1221 HOH   A O   1 
HETATM 2853 O O   . HOH   C 3 .   ? 19.74902 8.24419   55.06268 1.000 47.63686  ?  1222 HOH   A O   1 
HETATM 2854 O O   . HOH   C 3 .   ? 26.94581 8.34054   18.20005 1.000 35.90208  ?  1223 HOH   A O   1 
HETATM 2855 O O   . HOH   C 3 .   ? 29.92700 2.44278   13.81170 1.000 38.88818  ?  1224 HOH   A O   1 
HETATM 2856 O O   . HOH   C 3 .   ? 22.18026 35.26041  35.40657 1.000 45.37655  ?  1225 HOH   A O   1 
HETATM 2857 O O   . HOH   C 3 .   ? 26.80473 13.11046  6.73648  1.000 41.23631  ?  1226 HOH   A O   1 
HETATM 2858 O O   . HOH   C 3 .   ? 29.59368 5.75815   7.34569  1.000 42.05555  ?  1227 HOH   A O   1 
HETATM 2859 O O   . HOH   C 3 .   ? 26.91779 10.05204  61.03158 1.000 64.69059  ?  1228 HOH   A O   1 
HETATM 2860 O O   . HOH   C 3 .   ? 27.86131 30.74196  36.56456 1.000 41.79612  ?  1229 HOH   A O   1 
HETATM 2861 O O   . HOH   C 3 .   ? 21.34282 2.74023   -3.55114 1.000 59.51312  ?  1230 HOH   A O   1 
HETATM 2862 O O   . HOH   C 3 .   ? 23.66221 11.23126  28.82956 1.000 28.71211  ?  1231 HOH   A O   1 
HETATM 2863 O O   . HOH   C 3 .   ? 28.67576 1.55105   20.66371 1.000 39.77372  ?  1232 HOH   A O   1 
HETATM 2864 O O   . HOH   C 3 .   ? 25.78521 10.53418  18.24926 1.000 30.92461  ?  1233 HOH   A O   1 
HETATM 2865 O O   . HOH   C 3 .   ? 9.20385  -6.92712  -0.61918 1.000 52.57002  ?  1234 HOH   A O   1 
HETATM 2866 O O   . HOH   C 3 .   ? 13.51236 4.54952   -1.90749 1.000 52.07157  ?  1235 HOH   A O   1 
HETATM 2867 O O   . HOH   C 3 .   ? 13.84656 -13.22474 0.17395  1.000 55.38065  ?  1236 HOH   A O   1 
HETATM 2868 O O   . HOH   C 3 .   ? 15.31470 30.09455  17.00162 1.000 40.27449  ?  1237 HOH   A O   1 
HETATM 2869 O O   . HOH   C 3 .   ? 19.66931 29.97990  -1.94691 1.000 72.00625  ?  1238 HOH   A O   1 
HETATM 2870 O O   . HOH   C 3 .   ? 15.60251 29.08805  55.45062 1.000 52.60553  ?  1239 HOH   A O   1 
HETATM 2871 O O   . HOH   C 3 .   ? 17.11115 -3.12327  39.62167 1.000 43.25869  ?  1240 HOH   A O   1 
HETATM 2872 O O   . HOH   C 3 .   ? 14.56676 -9.81032  8.89709  1.000 48.26349  ?  1241 HOH   A O   1 
HETATM 2873 O O   . HOH   C 3 .   ? 21.66562 19.34288  25.93174 1.000 35.30728  ?  1242 HOH   A O   1 
HETATM 2874 O O   . HOH   C 3 .   ? 24.17674 14.37488  20.96517 1.000 26.64213  ?  1243 HOH   A O   1 
HETATM 2875 O O   . HOH   C 3 .   ? 14.77771 13.91956  54.87344 1.000 49.51271  ?  1244 HOH   A O   1 
HETATM 2876 O O   . HOH   C 3 .   ? 12.95875 29.20887  17.57980 1.000 43.71775  ?  1245 HOH   A O   1 
HETATM 2877 O O   . HOH   C 3 .   ? 14.48121 -11.12396 6.89404  1.000 47.38088  ?  1246 HOH   A O   1 
HETATM 2878 O O   . HOH   C 3 .   ? 24.05224 9.02003   29.42610 1.000 34.83104  ?  1247 HOH   A O   1 
HETATM 2879 O O   . HOH   C 3 .   ? 31.11408 14.96081  11.61574 1.000 35.86998  ?  1248 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   . ASP A 45  ? 1.75918 0.67616 0.55531 0.04008  -0.05364 0.01344  45  ASP A N   
2    C CA  . ASP A 45  ? 1.82913 0.76460 0.63267 0.01553  -0.01391 0.01142  45  ASP A CA  
3    C C   . ASP A 45  ? 1.70802 0.71872 0.58086 0.00693  -0.00547 0.00625  45  ASP A C   
4    O O   . ASP A 45  ? 1.65414 0.69120 0.54933 -0.01508 0.03031  0.00354  45  ASP A O   
5    C CB  . ASP A 45  ? 1.85524 0.76343 0.62074 0.01920  -0.01627 0.00712  45  ASP A CB  
6    C CG  . ASP A 45  ? 1.93676 0.82542 0.67489 -0.00483 0.02664  0.00741  45  ASP A CG  
7    O OD1 . ASP A 45  ? 2.15957 0.99491 0.83924 -0.00235 0.02728  0.00843  45  ASP A OD1 
8    O OD2 . ASP A 45  ? 1.85498 0.78294 0.63172 -0.02611 0.05936  0.00563  45  ASP A OD2 
9    N N   . ASN A 46  ? 1.57634 0.62207 0.48486 0.02430  -0.03952 0.00333  46  ASN A N   
10   C CA  . ASN A 46  ? 1.47403 0.59257 0.45536 0.01676  -0.03530 -0.00196 46  ASN A CA  
11   C C   . ASN A 46  ? 1.40553 0.54874 0.42349 0.00240  -0.01031 0.00337  46  ASN A C   
12   O O   . ASN A 46  ? 1.37985 0.51034 0.39402 0.01243  -0.02412 0.00941  46  ASN A O   
13   C CB  . ASN A 46  ? 1.50886 0.67057 0.54666 0.03740  -0.07769 -0.00585 46  ASN A CB  
14   C CG  . ASN A 46  ? 1.42798 0.67651 0.56725 0.02818  -0.07340 -0.01060 46  ASN A CG  
15   O OD1 . ASN A 46  ? 1.36453 0.63927 0.52931 0.00927  -0.04373 -0.01369 46  ASN A OD1 
16   N ND2 . ASN A 46  ? 1.34529 0.63836 0.54245 0.04146  -0.10339 -0.01175 46  ASN A ND2 
17   N N   . GLN A 47  ? 1.32170 0.49985 0.37570 -0.01981 0.02485  -0.00041 47  GLN A N   
18   C CA  . GLN A 47  ? 1.31502 0.51615 0.40376 -0.03496 0.05006  0.00295  47  GLN A CA  
19   C C   . GLN A 47  ? 1.16398 0.43567 0.34128 -0.02854 0.03392  0.00206  47  GLN A C   
20   O O   . GLN A 47  ? 1.12268 0.42431 0.34018 -0.04093 0.05381  0.00273  47  GLN A O   
21   C CB  . GLN A 47  ? 1.24394 0.45981 0.34324 -0.06017 0.09186  -0.00320 47  GLN A CB  
22   C CG  . GLN A 47  ? 1.18112 0.46370 0.35215 -0.06402 0.09248  -0.01407 47  GLN A CG  
23   C CD  . GLN A 47  ? 1.17752 0.46241 0.34222 -0.08397 0.12908  -0.02362 47  GLN A CD  
24   O OE1 . GLN A 47  ? 1.17404 0.46257 0.34643 -0.10234 0.16092  -0.02455 47  GLN A OE1 
25   N NE2 . GLN A 47  ? 1.19045 0.47494 0.34353 -0.08008 0.12420  -0.03240 47  GLN A NE2 
26   N N   . PHE A 48  ? 1.14823 0.44668 0.35580 -0.01023 -0.00103 0.00012  48  PHE A N   
27   C CA  . PHE A 48  ? 1.07847 0.44203 0.36493 -0.00393 -0.01692 -0.00026 48  PHE A CA  
28   C C   . PHE A 48  ? 1.08388 0.43554 0.36045 0.02041  -0.05441 0.00148  48  PHE A C   
29   O O   . PHE A 48  ? 1.14791 0.44818 0.36540 0.03389  -0.07379 0.00142  48  PHE A O   
30   C CB  . PHE A 48  ? 1.05473 0.48091 0.40897 -0.00951 -0.02078 -0.00651 48  PHE A CB  
31   C CG  . PHE A 48  ? 0.98809 0.43795 0.36797 -0.03095 0.01225  -0.01068 48  PHE A CG  
32   C CD1 . PHE A 48  ? 0.99529 0.42207 0.34299 -0.03941 0.02725  -0.01684 48  PHE A CD1 
33   C CD2 . PHE A 48  ? 0.90564 0.40179 0.34245 -0.04140 0.02723  -0.01013 48  PHE A CD2 
34   C CE1 . PHE A 48  ? 0.98329 0.43519 0.35907 -0.05757 0.05644  -0.02347 48  PHE A CE1 
35   C CE2 . PHE A 48  ? 0.88817 0.40656 0.35104 -0.05945 0.05474  -0.01592 48  PHE A CE2 
36   C CZ  . PHE A 48  ? 0.94952 0.44707 0.38392 -0.06737 0.06924  -0.02317 48  PHE A CZ  
37   N N   . TYR A 49  ? 1.03078 0.43151 0.36626 0.02666  -0.06489 0.00178  49  TYR A N   
38   C CA  . TYR A 49  ? 1.03743 0.44386 0.38195 0.05004  -0.10060 0.00018  49  TYR A CA  
39   C C   . TYR A 49  ? 0.95536 0.44293 0.38884 0.04981  -0.10638 -0.00220 49  TYR A C   
40   O O   . TYR A 49  ? 0.90512 0.43054 0.37952 0.03411  -0.08256 -0.00056 49  TYR A O   
41   C CB  . TYR A 49  ? 1.09794 0.44788 0.38638 0.06292  -0.10703 0.00379  49  TYR A CB  
42   C CG  . TYR A 49  ? 1.06666 0.43783 0.38344 0.05695  -0.08969 0.00627  49  TYR A CG  
43   C CD1 . TYR A 49  ? 1.05424 0.42317 0.36979 0.03409  -0.05336 0.00970  49  TYR A CD1 
44   C CD2 . TYR A 49  ? 1.05150 0.44577 0.39733 0.07497  -0.11035 0.00343  49  TYR A CD2 
45   C CE1 . TYR A 49  ? 1.02801 0.41466 0.36901 0.02920  -0.03946 0.01096  49  TYR A CE1 
46   C CE2 . TYR A 49  ? 1.02607 0.43809 0.39542 0.07089  -0.09560 0.00452  49  TYR A CE2 
47   C CZ  . TYR A 49  ? 1.01466 0.42152 0.38070 0.04792  -0.06086 0.00866  49  TYR A CZ  
48   O OH  . TYR A 49  ? 0.99117 0.41451 0.38064 0.04439  -0.04811 0.00877  49  TYR A OH  
49   N N   . SER A 50  ? 0.94512 0.45904 0.40772 0.06708  -0.13837 -0.00664 50  SER A N   
50   C CA  . SER A 50  ? 0.89835 0.49082 0.44442 0.06569  -0.14517 -0.00911 50  SER A CA  
51   C C   . SER A 50  ? 0.89528 0.50571 0.46064 0.08291  -0.15937 -0.01197 50  SER A C   
52   O O   . SER A 50  ? 0.94436 0.51928 0.47480 0.10400  -0.18429 -0.01601 50  SER A O   
53   C CB  . SER A 50  ? 0.86019 0.47992 0.43679 0.06887  -0.16923 -0.01365 50  SER A CB  
54   O OG  . SER A 50  ? 0.95200 0.53765 0.49245 0.05988  -0.16305 -0.01340 50  SER A OG  
55   N N   . VAL A 51  ? 0.89700 0.56161 0.51665 0.07512  -0.14462 -0.01099 51  VAL A N   
56   C CA  . VAL A 51  ? 0.91534 0.61091 0.56521 0.09060  -0.15587 -0.01568 51  VAL A CA  
57   C C   . VAL A 51  ? 0.89818 0.67673 0.62902 0.08405  -0.15758 -0.01773 51  VAL A C   
58   O O   . VAL A 51  ? 0.86606 0.67486 0.62712 0.06359  -0.13991 -0.01271 51  VAL A O   
59   C CB  . VAL A 51  ? 0.88916 0.56641 0.52046 0.08821  -0.13473 -0.01295 51  VAL A CB  
60   C CG1 . VAL A 51  ? 0.93366 0.61452 0.56872 0.11201  -0.15378 -0.02011 51  VAL A CG1 
61   C CG2 . VAL A 51  ? 0.85956 0.46096 0.41730 0.08052  -0.11943 -0.00728 51  VAL A CG2 
62   N N   . GLU A 52  ? 0.91549 0.73011 0.68078 0.10123  -0.17887 -0.02562 52  GLU A N   
63   C CA  . GLU A 52  ? 0.94254 0.83731 0.78401 0.09486  -0.18021 -0.02795 52  GLU A CA  
64   C C   . GLU A 52  ? 0.97178 0.90249 0.84054 0.09683  -0.16507 -0.02945 52  GLU A C   
65   O O   . GLU A 52  ? 0.99894 0.93852 0.87357 0.11747  -0.17894 -0.03861 52  GLU A O   
66   C CB  . GLU A 52  ? 0.95522 0.87400 0.82386 0.11096  -0.21252 -0.03783 52  GLU A CB  
67   C CG  . GLU A 52  ? 0.98055 0.89822 0.85594 0.10137  -0.22504 -0.03625 52  GLU A CG  
68   C CD  . GLU A 52  ? 1.03513 0.88602 0.84730 0.09318  -0.21584 -0.02933 52  GLU A CD  
69   O OE1 . GLU A 52  ? 1.12238 0.91036 0.87309 0.10864  -0.22875 -0.03193 52  GLU A OE1 
70   O OE2 . GLU A 52  ? 0.93065 0.79128 0.75332 0.07157  -0.19573 -0.02188 52  GLU A OE2 
71   N N   . VAL A 53  ? 0.92572 0.87621 0.81049 0.07675  -0.13806 -0.02181 53  VAL A N   
72   C CA  . VAL A 53  ? 0.88100 0.86676 0.79152 0.07648  -0.12217 -0.02290 53  VAL A CA  
73   C C   . VAL A 53  ? 0.86920 0.93222 0.84726 0.06646  -0.12002 -0.02268 53  VAL A C   
74   O O   . VAL A 53  ? 0.86149 0.94401 0.85994 0.04518  -0.10814 -0.01451 53  VAL A O   
75   C CB  . VAL A 53  ? 0.82231 0.78060 0.70766 0.06128  -0.09523 -0.01575 53  VAL A CB  
76   C CG1 . VAL A 53  ? 0.75950 0.73324 0.65292 0.06867  -0.08484 -0.01960 53  VAL A CG1 
77   C CG2 . VAL A 53  ? 0.82517 0.70729 0.64500 0.06174  -0.09406 -0.01314 53  VAL A CG2 
78   N N   . GLY A 54  ? 0.83301 0.93946 0.84520 0.08156  -0.13142 -0.03215 54  GLY A N   
79   C CA  . GLY A 54  ? 0.78859 0.96913 0.86419 0.07164  -0.12988 -0.03263 54  GLY A CA  
80   C C   . GLY A 54  ? 0.81408 1.00439 0.90926 0.06230  -0.14538 -0.03040 54  GLY A C   
81   O O   . GLY A 54  ? 0.82961 1.00385 0.91704 0.07790  -0.16996 -0.03854 54  GLY A O   
82   N N   . ASP A 55  ? 0.82718 1.04100 0.94649 0.03757  -0.13331 -0.01995 55  ASP A N   
83   C CA  . ASP A 55  ? 0.82185 1.04007 0.95787 0.02627  -0.14769 -0.01697 55  ASP A CA  
84   C C   . ASP A 55  ? 0.82830 0.99138 0.92299 0.01556  -0.14417 -0.00913 55  ASP A C   
85   O O   . ASP A 55  ? 0.81896 0.97430 0.91807 0.00927  -0.15873 -0.00813 55  ASP A O   
86   C CB  . ASP A 55  ? 0.84193 1.12547 1.03654 0.00522  -0.14016 -0.01122 55  ASP A CB  
87   C CG  . ASP A 55  ? 0.79278 1.13437 1.02473 0.01055  -0.13080 -0.01690 55  ASP A CG  
88   O OD1 . ASP A 55  ? 0.77405 1.14184 1.01897 -0.00391 -0.10904 -0.00920 55  ASP A OD1 
89   O OD2 . ASP A 55  ? 0.80590 1.16690 1.05368 0.03011  -0.14593 -0.03017 55  ASP A OD2 
90   N N   . SER A 56  ? 0.84691 0.97315 0.90358 0.01349  -0.12549 -0.00502 56  SER A N   
91   C CA  . SER A 56  ? 0.82929 0.90963 0.85111 0.00217  -0.11786 0.00067  56  SER A CA  
92   C C   . SER A 56  ? 0.88357 0.89876 0.84590 0.01744  -0.12607 -0.00395 56  SER A C   
93   O O   . SER A 56  ? 0.87827 0.87242 0.81477 0.03343  -0.12655 -0.00841 56  SER A O   
94   C CB  . SER A 56  ? 0.79316 0.87449 0.81246 -0.01141 -0.09152 0.00677  56  SER A CB  
95   O OG  . SER A 56  ? 0.89143 1.02969 0.95704 -0.02069 -0.08339 0.01037  56  SER A OG  
96   N N   . THR A 57  ? 0.81604 0.79697 0.75399 0.01242  -0.13284 -0.00290 57  THR A N   
97   C CA  . THR A 57  ? 0.78828 0.70301 0.66310 0.02398  -0.13857 -0.00601 57  THR A CA  
98   C C   . THR A 57  ? 0.76283 0.64129 0.60137 0.01329  -0.11185 -0.00206 57  THR A C   
99   O O   . THR A 57  ? 0.75376 0.63702 0.60192 -0.00326 -0.09969 0.00096  57  THR A O   
100  C CB  . THR A 57  ? 0.79455 0.69049 0.65895 0.02478  -0.15913 -0.00847 57  THR A CB  
101  O OG1 . THR A 57  ? 0.81896 0.73998 0.71013 0.03838  -0.18676 -0.01469 57  THR A OG1 
102  C CG2 . THR A 57  ? 0.81345 0.63686 0.60526 0.03224  -0.15882 -0.01011 57  THR A CG2 
103  N N   . PHE A 58  ? 0.75884 0.60110 0.55742 0.02265  -0.10364 -0.00306 58  PHE A N   
104  C CA  . PHE A 58  ? 0.71654 0.52460 0.48199 0.01194  -0.07739 -0.00041 58  PHE A CA  
105  C C   . PHE A 58  ? 0.75321 0.49358 0.45210 0.01560  -0.07875 -0.00133 58  PHE A C   
106  O O   . PHE A 58  ? 0.79727 0.49470 0.45108 0.03042  -0.08829 -0.00250 58  PHE A O   
107  C CB  . PHE A 58  ? 0.69774 0.50725 0.46124 0.01720  -0.06611 -0.00055 58  PHE A CB  
108  C CG  . PHE A 58  ? 0.64103 0.49748 0.45015 0.00363  -0.04766 0.00161  58  PHE A CG  
109  C CD1 . PHE A 58  ? 0.63875 0.55635 0.50333 0.00300  -0.05471 0.00215  58  PHE A CD1 
110  C CD2 . PHE A 58  ? 0.61211 0.45098 0.40785 -0.00899 -0.02336 0.00263  58  PHE A CD2 
111  C CE1 . PHE A 58  ? 0.58110 0.53724 0.48113 -0.00900 -0.03871 0.00471  58  PHE A CE1 
112  C CE2 . PHE A 58  ? 0.59045 0.46981 0.42604 -0.01986 -0.00920 0.00365  58  PHE A CE2 
113  C CZ  . PHE A 58  ? 0.55802 0.49396 0.44288 -0.01937 -0.01732 0.00521  58  PHE A CZ  
114  N N   . THR A 59  ? 0.73697 0.46620 0.42745 0.00255  -0.06967 -0.00127 59  THR A N   
115  C CA  . THR A 59  ? 0.75023 0.41724 0.37608 0.00289  -0.06546 -0.00256 59  THR A CA  
116  C C   . THR A 59  ? 0.75358 0.40140 0.36071 -0.01297 -0.03244 -0.00179 59  THR A C   
117  O O   . THR A 59  ? 0.72074 0.39239 0.35573 -0.02805 -0.01710 -0.00370 59  THR A O   
118  C CB  . THR A 59  ? 0.75319 0.42085 0.38148 0.00061  -0.07820 -0.00568 59  THR A CB  
119  O OG1 . THR A 59  ? 0.74105 0.43723 0.40065 0.01256  -0.10857 -0.00708 59  THR A OG1 
120  C CG2 . THR A 59  ? 0.82137 0.42229 0.37615 0.00427  -0.07640 -0.00778 59  THR A CG2 
121  N N   . VAL A 60  ? 0.79556 0.39970 0.35668 -0.00956 -0.02264 0.00022  60  VAL A N   
122  C CA  . VAL A 60  ? 0.80086 0.38798 0.34745 -0.02532 0.00871  0.00048  60  VAL A CA  
123  C C   . VAL A 60  ? 0.87645 0.39128 0.34500 -0.02695 0.01881  0.00163  60  VAL A C   
124  O O   . VAL A 60  ? 0.92695 0.40153 0.34904 -0.01312 -0.00066 0.00306  60  VAL A O   
125  C CB  . VAL A 60  ? 0.77913 0.38354 0.34775 -0.02399 0.01521  0.00231  60  VAL A CB  
126  C CG1 . VAL A 60  ? 0.71168 0.38556 0.35111 -0.02160 0.00497  0.00172  60  VAL A CG1 
127  C CG2 . VAL A 60  ? 0.83194 0.39136 0.35389 -0.00698 0.00063  0.00491  60  VAL A CG2 
128  N N   . LEU A 61  ? 0.88659 0.38497 0.34073 -0.04470 0.04975  0.00056  61  LEU A N   
129  C CA  . LEU A 61  ? 0.96138 0.39130 0.34053 -0.05080 0.06547  0.00251  61  LEU A CA  
130  C C   . LEU A 61  ? 1.01422 0.39447 0.34457 -0.03837 0.05379  0.00925  61  LEU A C   
131  O O   . LEU A 61  ? 0.98714 0.39015 0.34777 -0.02867 0.04185  0.01055  61  LEU A O   
132  C CB  . LEU A 61  ? 0.95642 0.38751 0.34091 -0.07439 0.10279  -0.00133 61  LEU A CB  
133  C CG  . LEU A 61  ? 0.93600 0.40302 0.35543 -0.08668 0.11667  -0.01034 61  LEU A CG  
134  C CD1 . LEU A 61  ? 0.92190 0.42364 0.38775 -0.10462 0.14339  -0.01636 61  LEU A CD1 
135  C CD2 . LEU A 61  ? 0.98357 0.40358 0.34194 -0.09184 0.12831  -0.01313 61  LEU A CD2 
136  N N   . LYS A 62  ? 1.09509 0.40420 0.34589 -0.03831 0.05704  0.01311  62  LYS A N   
137  C CA  . LYS A 62  ? 1.15816 0.40837 0.35205 -0.02590 0.04353  0.01982  62  LYS A CA  
138  C C   . LYS A 62  ? 1.16201 0.40029 0.35602 -0.03813 0.06460  0.02275  62  LYS A C   
139  O O   . LYS A 62  ? 1.20270 0.40138 0.36332 -0.02633 0.05058  0.02735  62  LYS A O   
140  C CB  . LYS A 62  ? 1.25175 0.42247 0.35308 -0.02457 0.04259  0.02428  62  LYS A CB  
141  C CG  . LYS A 62  ? 1.26436 0.43273 0.35293 -0.00634 0.01278  0.02136  62  LYS A CG  
142  C CD  . LYS A 62  ? 1.27102 0.43655 0.36273 0.02167  -0.02809 0.02172  62  LYS A CD  
143  C CE  . LYS A 62  ? 1.31370 0.45127 0.36754 0.03988  -0.05848 0.01933  62  LYS A CE  
144  N NZ  . LYS A 62  ? 1.41205 0.49843 0.39852 0.02740  -0.03987 0.02089  62  LYS A NZ  
145  N N   . ARG A 63  ? 1.12393 0.39350 0.35438 -0.06071 0.09614  0.01906  63  ARG A N   
146  C CA  . ARG A 63  ? 1.12560 0.38656 0.36139 -0.07267 0.11461  0.02050  63  ARG A CA  
147  C C   . ARG A 63  ? 1.07079 0.37722 0.36251 -0.05803 0.09601  0.01867  63  ARG A C   
148  O O   . ARG A 63  ? 1.08461 0.37288 0.37026 -0.06041 0.10136  0.02026  63  ARG A O   
149  C CB  . ARG A 63  ? 1.09712 0.38478 0.36368 -0.09978 0.15141  0.01443  63  ARG A CB  
150  C CG  . ARG A 63  ? 1.00717 0.37648 0.35775 -0.10055 0.15051  0.00600  63  ARG A CG  
151  C CD  . ARG A 63  ? 0.98738 0.37851 0.36388 -0.12499 0.18408  -0.00232 63  ARG A CD  
152  N NE  . ARG A 63  ? 0.98022 0.37352 0.37500 -0.13882 0.20306  -0.00421 63  ARG A NE  
153  C CZ  . ARG A 63  ? 0.96913 0.38198 0.39165 -0.16050 0.23230  -0.01304 63  ARG A CZ  
154  N NH1 . ARG A 63  ? 1.02392 0.45679 0.45939 -0.17041 0.24712  -0.02150 63  ARG A NH1 
155  N NH2 . ARG A 63  ? 0.97124 0.38421 0.41066 -0.17170 0.24585  -0.01505 63  ARG A NH2 
156  N N   . TYR A 64  ? 1.01295 0.37655 0.35713 -0.04349 0.07464  0.01510  64  TYR A N   
157  C CA  . TYR A 64  ? 0.95828 0.37292 0.35904 -0.03068 0.05956  0.01241  64  TYR A CA  
158  C C   . TYR A 64  ? 0.98431 0.38350 0.36599 -0.00352 0.02506  0.01361  64  TYR A C   
159  O O   . TYR A 64  ? 0.98638 0.39196 0.36588 0.00761  0.00558  0.01298  64  TYR A O   
160  C CB  . TYR A 64  ? 0.87710 0.36903 0.35237 -0.03548 0.06129  0.00755  64  TYR A CB  
161  C CG  . TYR A 64  ? 0.85134 0.36079 0.34910 -0.05956 0.09162  0.00385  64  TYR A CG  
162  C CD1 . TYR A 64  ? 0.84602 0.35405 0.35388 -0.07241 0.11229  0.00176  64  TYR A CD1 
163  C CD2 . TYR A 64  ? 0.83442 0.36169 0.34474 -0.06849 0.09802  0.00070  64  TYR A CD2 
164  C CE1 . TYR A 64  ? 0.82318 0.34977 0.35586 -0.09343 0.13849  -0.00402 64  TYR A CE1 
165  C CE2 . TYR A 64  ? 0.81223 0.35735 0.34602 -0.08848 0.12415  -0.00530 64  TYR A CE2 
166  C CZ  . TYR A 64  ? 0.80616 0.35208 0.35232 -0.10087 0.14433  -0.00797 64  TYR A CZ  
167  O OH  . TYR A 64  ? 0.78449 0.35085 0.35834 -0.11988 0.16891  -0.01624 64  TYR A OH  
168  N N   . GLN A 65  ? 1.00494 0.38468 0.37514 0.00785  0.01619  0.01374  65  GLN A N   
169  C CA  . GLN A 65  ? 1.03597 0.39747 0.38707 0.03552  -0.01718 0.01244  65  GLN A CA  
170  C C   . GLN A 65  ? 0.98627 0.40218 0.39450 0.04936  -0.02809 0.00601  65  GLN A C   
171  O O   . GLN A 65  ? 0.94242 0.39356 0.38998 0.03733  -0.00924 0.00420  65  GLN A O   
172  C CB  . GLN A 65  ? 1.12902 0.39940 0.39621 0.04040  -0.02227 0.01783  65  GLN A CB  
173  C CG  . GLN A 65  ? 1.18499 0.39687 0.38948 0.02118  -0.00246 0.02495  65  GLN A CG  
174  C CD  . GLN A 65  ? 1.22033 0.40848 0.38893 0.03420  -0.02406 0.02584  65  GLN A CD  
175  O OE1 . GLN A 65  ? 1.21016 0.40857 0.37904 0.02184  -0.01177 0.02610  65  GLN A OE1 
176  N NE2 . GLN A 65  ? 1.26450 0.41995 0.40206 0.06066  -0.05820 0.02484  65  GLN A NE2 
177  N N   . ASN A 66  ? 0.99651 0.41906 0.40837 0.07574  -0.05947 0.00125  66  ASN A N   
178  C CA  . ASN A 66  ? 0.96144 0.43123 0.42049 0.09325  -0.07275 -0.00685 66  ASN A CA  
179  C C   . ASN A 66  ? 0.87487 0.43132 0.41196 0.08241  -0.05909 -0.00962 66  ASN A C   
180  O O   . ASN A 66  ? 0.84237 0.42778 0.41003 0.07776  -0.04608 -0.01224 66  ASN A O   
181  C CB  . ASN A 66  ? 0.99822 0.42556 0.42767 0.09626  -0.06817 -0.00748 66  ASN A CB  
182  C CG  . ASN A 66  ? 1.00450 0.44556 0.44871 0.12583  -0.09531 -0.01748 66  ASN A CG  
183  O OD1 . ASN A 66  ? 1.00348 0.46576 0.46196 0.14649  -0.12120 -0.02358 66  ASN A OD1 
184  N ND2 . ASN A 66  ? 1.01175 0.44241 0.45501 0.12852  -0.09015 -0.02089 66  ASN A ND2 
185  N N   . LEU A 67  ? 0.84209 0.43648 0.40836 0.07859  -0.06369 -0.00894 67  LEU A N   
186  C CA  . LEU A 67  ? 0.76703 0.43807 0.40208 0.06741  -0.05295 -0.00998 67  LEU A CA  
187  C C   . LEU A 67  ? 0.73435 0.46215 0.41787 0.08505  -0.06758 -0.01772 67  LEU A C   
188  O O   . LEU A 67  ? 0.75588 0.48348 0.43691 0.10664  -0.09280 -0.02367 67  LEU A O   
189  C CB  . LEU A 67  ? 0.74780 0.43801 0.39749 0.05830  -0.05600 -0.00705 67  LEU A CB  
190  C CG  . LEU A 67  ? 0.75171 0.42345 0.38691 0.03413  -0.03189 -0.00166 67  LEU A CG  
191  C CD1 . LEU A 67  ? 0.81534 0.40771 0.37648 0.03218  -0.02747 0.00164  67  LEU A CD1 
192  C CD2 . LEU A 67  ? 0.70880 0.41843 0.37767 0.02583  -0.03576 -0.00072 67  LEU A CD2 
193  N N   . LYS A 68  ? 0.68447 0.46166 0.41214 0.07621  -0.05165 -0.01880 68  LYS A N   
194  C CA  . LYS A 68  ? 0.65385 0.48902 0.42777 0.09027  -0.05993 -0.02646 68  LYS A CA  
195  C C   . LYS A 68  ? 0.62212 0.52017 0.44877 0.07269  -0.04251 -0.02354 68  LYS A C   
196  O O   . LYS A 68  ? 0.59819 0.48621 0.42068 0.05428  -0.02221 -0.01873 68  LYS A O   
197  C CB  . LYS A 68  ? 0.67884 0.49113 0.43403 0.10489  -0.06131 -0.03308 68  LYS A CB  
198  C CG  . LYS A 68  ? 0.73593 0.50531 0.45440 0.13083  -0.08745 -0.03964 68  LYS A CG  
199  C CD  . LYS A 68  ? 0.77458 0.49944 0.45937 0.14073  -0.08701 -0.04378 68  LYS A CD  
200  C CE  . LYS A 68  ? 0.85058 0.49943 0.47303 0.15818  -0.10915 -0.04474 68  LYS A CE  
201  N NZ  . LYS A 68  ? 0.86225 0.53294 0.50096 0.18846  -0.13993 -0.05708 68  LYS A NZ  
202  N N   . PRO A 69  ? 0.57556 0.53730 0.45121 0.07733  -0.05000 -0.02668 69  PRO A N   
203  C CA  . PRO A 69  ? 0.59013 0.60705 0.51044 0.05976  -0.03436 -0.02232 69  PRO A CA  
204  C C   . PRO A 69  ? 0.58136 0.61432 0.51094 0.06065  -0.02044 -0.02594 69  PRO A C   
205  O O   . PRO A 69  ? 0.58609 0.61609 0.50891 0.07939  -0.02718 -0.03462 69  PRO A O   
206  C CB  . PRO A 69  ? 0.53886 0.61405 0.50352 0.06524  -0.04761 -0.02498 69  PRO A CB  
207  C CG  . PRO A 69  ? 0.60460 0.67021 0.55867 0.09172  -0.06761 -0.03593 69  PRO A CG  
208  C CD  . PRO A 69  ? 0.57174 0.55825 0.46458 0.09878  -0.07309 -0.03524 69  PRO A CD  
209  N N   . ILE A 70  ? 0.56487 0.61342 0.50940 0.04146  -0.00274 -0.02037 70  ILE A N   
210  C CA  . ILE A 70  ? 0.63240 0.69194 0.58305 0.04082  0.01025  -0.02390 70  ILE A CA  
211  C C   . ILE A 70  ? 0.72422 0.83815 0.71421 0.02694  0.02030  -0.01951 70  ILE A C   
212  O O   . ILE A 70  ? 0.78482 0.92806 0.78977 0.03100  0.02660  -0.02363 70  ILE A O   
213  C CB  . ILE A 70  ? 0.61211 0.61685 0.52840 0.03187  0.02209  -0.02320 70  ILE A CB  
214  C CG1 . ILE A 70  ? 0.57337 0.55947 0.48352 0.01203  0.02957  -0.01570 70  ILE A CG1 
215  C CG2 . ILE A 70  ? 0.62148 0.57173 0.49529 0.04726  0.01313  -0.02800 70  ILE A CG2 
216  C CD1 . ILE A 70  ? 0.63115 0.56967 0.51306 0.00061  0.04398  -0.01633 70  ILE A CD1 
217  N N   . GLY A 71  ? 0.75290 0.87749 0.75663 0.01086  0.02097  -0.01123 71  GLY A N   
218  C CA  . GLY A 71  ? 0.80858 0.97661 0.84402 -0.00375 0.02883  -0.00545 71  GLY A CA  
219  C C   . GLY A 71  ? 0.95412 1.13633 1.00659 -0.01654 0.02233  0.00268  71  GLY A C   
220  O O   . GLY A 71  ? 0.75904 0.91557 0.79784 -0.01463 0.01255  0.00323  71  GLY A O   
221  N N   . SER A 72  ? 0.97378 1.19465 1.05382 -0.02978 0.02698  0.00911  72  SER A N   
222  C CA  . SER A 72  ? 1.05356 1.28921 1.15231 -0.04406 0.02023  0.01757  72  SER A CA  
223  C C   . SER A 72  ? 1.08952 1.34827 1.20517 -0.06072 0.02829  0.02519  72  SER A C   
224  O O   . SER A 72  ? 1.06350 1.35979 1.19473 -0.06086 0.03398  0.02647  72  SER A O   
225  C CB  . SER A 72  ? 1.05158 1.32273 1.17342 -0.03789 0.00885  0.01697  72  SER A CB  
226  O OG  . SER A 72  ? 1.04256 1.34468 1.19209 -0.05509 0.00632  0.02621  72  SER A OG  
227  N N   . GLY A 73  ? 1.08685 1.32215 1.19750 -0.07389 0.02827  0.02946  73  GLY A N   
228  C CA  . GLY A 73  ? 1.11584 1.36641 1.23962 -0.08909 0.03177  0.03677  73  GLY A CA  
229  C C   . GLY A 73  ? 1.13264 1.40054 1.27603 -0.10297 0.02185  0.04659  73  GLY A C   
230  O O   . GLY A 73  ? 1.12304 1.41919 1.28292 -0.10189 0.01640  0.04905  73  GLY A O   
231  N N   . ALA A 74  ? 1.16014 1.41136 1.30374 -0.11598 0.01838  0.05114  74  ALA A N   
232  C CA  . ALA A 74  ? 1.20872 1.46798 1.36817 -0.13003 0.00677  0.06032  74  ALA A CA  
233  C C   . ALA A 74  ? 1.24359 1.46760 1.39458 -0.13210 -0.00282 0.05715  74  ALA A C   
234  O O   . ALA A 74  ? 1.23689 1.46399 1.39979 -0.14076 -0.01531 0.06273  74  ALA A O   
235  C CB  . ALA A 74  ? 1.22734 1.49970 1.39503 -0.14507 0.00762  0.07014  74  ALA A CB  
236  N N   . GLN A 75  ? 1.36240 1.55372 1.49355 -0.12505 0.00309  0.04771  75  GLN A N   
237  C CA  . GLN A 75  ? 1.28043 1.43892 1.40103 -0.12639 -0.00305 0.04272  75  GLN A CA  
238  C C   . GLN A 75  ? 1.26895 1.40615 1.36957 -0.11458 -0.00408 0.03633  75  GLN A C   
239  O O   . GLN A 75  ? 1.25312 1.36344 1.34164 -0.11499 -0.00948 0.03222  75  GLN A O   
240  C CB  . GLN A 75  ? 1.27600 1.41243 1.38877 -0.12851 0.00525  0.03515  75  GLN A CB  
241  C CG  . GLN A 75  ? 1.29681 1.44752 1.42463 -0.13808 0.00351  0.04011  75  GLN A CG  
242  C CD  . GLN A 75  ? 1.29600 1.45130 1.43773 -0.14992 -0.01234 0.04902  75  GLN A CD  
243  O OE1 . GLN A 75  ? 1.25284 1.38665 1.39387 -0.15281 -0.02063 0.04447  75  GLN A OE1 
244  N NE2 . GLN A 75  ? 1.23741 1.42046 1.39158 -0.15734 -0.01631 0.06128  75  GLN A NE2 
245  N N   . GLY A 76  ? 1.04698 1.19321 1.14136 -0.10324 -0.00010 0.03475  76  GLY A N   
246  C CA  . GLY A 76  ? 0.92559 1.04652 0.99625 -0.09085 -0.00366 0.02915  76  GLY A CA  
247  C C   . GLY A 76  ? 0.92992 1.06105 0.99489 -0.07706 0.00016  0.02637  76  GLY A C   
248  O O   . GLY A 76  ? 0.92671 1.08687 1.00693 -0.07688 0.00697  0.02793  76  GLY A O   
249  N N   . ILE A 77  ? 0.67197 0.77600 0.71176 -0.06442 -0.00551 0.02152  77  ILE A N   
250  C CA  . ILE A 77  ? 0.64441 0.74975 0.67410 -0.04807 -0.00627 0.01706  77  ILE A CA  
251  C C   . ILE A 77  ? 0.58589 0.64514 0.57730 -0.04277 0.00498  0.01179  77  ILE A C   
252  O O   . ILE A 77  ? 0.57343 0.59366 0.53849 -0.04694 0.00763  0.01052  77  ILE A O   
253  C CB  . ILE A 77  ? 0.64595 0.75363 0.67528 -0.03588 -0.02508 0.01497  77  ILE A CB  
254  C CG1 . ILE A 77  ? 0.65316 0.80706 0.72389 -0.04416 -0.03605 0.01980  77  ILE A CG1 
255  C CG2 . ILE A 77  ? 0.62643 0.73567 0.64681 -0.01669 -0.02800 0.00843  77  ILE A CG2 
256  C CD1 . ILE A 77  ? 0.65390 0.79815 0.72967 -0.05869 -0.04279 0.02472  77  ILE A CD1 
257  N N   . VAL A 78  ? 0.64919 0.71281 0.63725 -0.03441 0.01224  0.00828  78  VAL A N   
258  C CA  . VAL A 78  ? 0.60515 0.62726 0.56063 -0.03193 0.02408  0.00366  78  VAL A CA  
259  C C   . VAL A 78  ? 0.59914 0.59669 0.52724 -0.01318 0.01528  -0.00065 78  VAL A C   
260  O O   . VAL A 78  ? 0.59664 0.62410 0.54178 -0.00022 0.00504  -0.00293 78  VAL A O   
261  C CB  . VAL A 78  ? 0.58406 0.62410 0.55512 -0.03758 0.03806  0.00188  78  VAL A CB  
262  C CG1 . VAL A 78  ? 0.52675 0.52307 0.46803 -0.03910 0.05090  -0.00330 78  VAL A CG1 
263  C CG2 . VAL A 78  ? 0.58041 0.64735 0.58008 -0.05361 0.04188  0.00617  78  VAL A CG2 
264  N N   . CYS A 79  ? 0.54563 0.48789 0.43050 -0.01184 0.01922  -0.00234 79  CYS A N   
265  C CA  . CYS A 79  ? 0.57497 0.48094 0.42445 0.00559  0.00943  -0.00577 79  CYS A CA  
266  C C   . CYS A 79  ? 0.60145 0.46031 0.41580 0.00183  0.02407  -0.00774 79  CYS A C   
267  O O   . CYS A 79  ? 0.58398 0.42621 0.39158 -0.01502 0.04079  -0.00666 79  CYS A O   
268  C CB  . CYS A 79  ? 0.55375 0.42757 0.37400 0.01210  -0.00594 -0.00433 79  CYS A CB  
269  S SG  . CYS A 79  ? 0.65986 0.58326 0.51863 0.02174  -0.02926 -0.00477 79  CYS A SG  
270  N N   . ALA A 80  ? 0.58647 0.42449 0.38035 0.01761  0.01708  -0.01173 80  ALA A N   
271  C CA  . ALA A 80  ? 0.65141 0.43346 0.40351 0.01508  0.02711  -0.01289 80  ALA A CA  
272  C C   . ALA A 80  ? 0.67824 0.39812 0.37463 0.02115  0.01771  -0.01007 80  ALA A C   
273  O O   . ALA A 80  ? 0.69173 0.41253 0.38220 0.03647  -0.00295 -0.01034 80  ALA A O   
274  C CB  . ALA A 80  ? 0.62340 0.41017 0.37953 0.02906  0.02331  -0.01912 80  ALA A CB  
275  N N   . ALA A 81  ? 0.75210 0.41728 0.40691 0.00849  0.03295  -0.00776 81  ALA A N   
276  C CA  . ALA A 81  ? 0.80888 0.40744 0.40173 0.01160  0.02686  -0.00373 81  ALA A CA  
277  C C   . ALA A 81  ? 0.82816 0.36866 0.37808 -0.00173 0.04545  -0.00205 81  ALA A C   
278  O O   . ALA A 81  ? 0.80380 0.35998 0.37750 -0.01558 0.06402  -0.00483 81  ALA A O   
279  C CB  . ALA A 81  ? 0.78046 0.37886 0.36725 0.00262  0.02827  -0.00015 81  ALA A CB  
280  N N   . TYR A 82  ? 0.89875 0.37001 0.38374 0.00208  0.03951  0.00246  82  TYR A N   
281  C CA  . TYR A 82  ? 0.95518 0.36196 0.38997 -0.01307 0.05751  0.00593  82  TYR A CA  
282  C C   . TYR A 82  ? 0.97905 0.35871 0.38364 -0.03378 0.07742  0.01038  82  TYR A C   
283  O O   . TYR A 82  ? 1.00981 0.36537 0.38021 -0.02667 0.06576  0.01402  82  TYR A O   
284  C CB  . TYR A 82  ? 1.02859 0.36834 0.40356 0.00442  0.03765  0.00868  82  TYR A CB  
285  C CG  . TYR A 82  ? 1.10095 0.36276 0.41230 -0.01337 0.05536  0.01491  82  TYR A CG  
286  C CD1 . TYR A 82  ? 1.09357 0.35423 0.41924 -0.03251 0.07831  0.01290  82  TYR A CD1 
287  C CD2 . TYR A 82  ? 1.18038 0.36840 0.41609 -0.01200 0.04908  0.02275  82  TYR A CD2 
288  C CE1 . TYR A 82  ? 1.16202 0.35233 0.43170 -0.05176 0.09610  0.01871  82  TYR A CE1 
289  C CE2 . TYR A 82  ? 1.25245 0.36674 0.42629 -0.03095 0.06731  0.02977  82  TYR A CE2 
290  C CZ  . TYR A 82  ? 1.24223 0.35913 0.43504 -0.05179 0.09160  0.02781  82  TYR A CZ  
291  O OH  . TYR A 82  ? 1.31593 0.36051 0.44949 -0.07348 0.11125  0.03485  82  TYR A OH  
292  N N   . ASP A 83  ? 0.96589 0.35125 0.38454 -0.05851 0.10683  0.00845  83  ASP A N   
293  C CA  . ASP A 83  ? 0.99114 0.35266 0.38286 -0.07966 0.12996  0.01021  83  ASP A CA  
294  C C   . ASP A 83  ? 1.08055 0.35745 0.39470 -0.08875 0.13975  0.01704  83  ASP A C   
295  O O   . ASP A 83  ? 1.09984 0.35454 0.40785 -0.10244 0.15558  0.01660  83  ASP A O   
296  C CB  . ASP A 83  ? 0.93832 0.34705 0.38400 -0.10133 0.15633  0.00268  83  ASP A CB  
297  C CG  . ASP A 83  ? 0.95793 0.35305 0.38508 -0.12174 0.18064  0.00117  83  ASP A CG  
298  O OD1 . ASP A 83  ? 1.01006 0.36136 0.38185 -0.11885 0.17696  0.00672  83  ASP A OD1 
299  O OD2 . ASP A 83  ? 0.92300 0.35179 0.39106 -0.13973 0.20283  -0.00690 83  ASP A OD2 
300  N N   . ALA A 84  ? 1.13920 0.36615 0.39197 -0.08168 0.12957  0.02352  84  ALA A N   
301  C CA  . ALA A 84  ? 1.23443 0.37318 0.40357 -0.08941 0.13637  0.03196  84  ALA A CA  
302  C C   . ALA A 84  ? 1.25282 0.38432 0.41521 -0.11975 0.17310  0.02782  84  ALA A C   
303  O O   . ALA A 84  ? 1.31424 0.40088 0.43543 -0.12816 0.18038  0.02722  84  ALA A O   
304  C CB  . ALA A 84  ? 1.29318 0.38317 0.39905 -0.07115 0.11221  0.03829  84  ALA A CB  
305  N N   . VAL A 85  ? 1.19679 0.38293 0.40912 -0.13370 0.19301  0.02056  85  VAL A N   
306  C CA  . VAL A 85  ? 1.20294 0.40068 0.42872 -0.15792 0.22375  0.00992  85  VAL A CA  
307  C C   . VAL A 85  ? 1.17389 0.39803 0.44473 -0.17173 0.23939  0.00302  85  VAL A C   
308  O O   . VAL A 85  ? 1.21658 0.41566 0.46895 -0.18586 0.25444  -0.00060 85  VAL A O   
309  C CB  . VAL A 85  ? 1.15941 0.40318 0.42024 -0.16415 0.23507  0.00255  85  VAL A CB  
310  C CG1 . VAL A 85  ? 1.14478 0.41842 0.44364 -0.18710 0.26520  -0.01156 85  VAL A CG1 
311  C CG2 . VAL A 85  ? 1.20767 0.41459 0.41370 -0.15524 0.22486  0.00699  85  VAL A CG2 
312  N N   . LEU A 86  ? 1.10397 0.37819 0.43369 -0.16801 0.23538  0.00098  86  LEU A N   
313  C CA  . LEU A 86  ? 1.07178 0.37537 0.44931 -0.17922 0.24748  -0.00714 86  LEU A CA  
314  C C   . LEU A 86  ? 1.11456 0.38034 0.46898 -0.17064 0.23340  -0.00046 86  LEU A C   
315  O O   . LEU A 86  ? 1.08608 0.36721 0.47206 -0.17986 0.24219  -0.00697 86  LEU A O   
316  C CB  . LEU A 86  ? 0.98714 0.35977 0.43800 -0.17885 0.24816  -0.01378 86  LEU A CB  
317  C CG  . LEU A 86  ? 0.96919 0.39037 0.46163 -0.18977 0.26402  -0.02584 86  LEU A CG  
318  C CD1 . LEU A 86  ? 0.93494 0.42025 0.50356 -0.19335 0.26721  -0.03664 86  LEU A CD1 
319  C CD2 . LEU A 86  ? 0.99551 0.39684 0.46736 -0.20576 0.28511  -0.03419 86  LEU A CD2 
320  N N   . ASP A 87  ? 1.14469 0.36138 0.44602 -0.15154 0.20957  0.01088  87  ASP A N   
321  C CA  . ASP A 87  ? 1.17791 0.35415 0.45434 -0.13827 0.19068  0.01575  87  ASP A CA  
322  C C   . ASP A 87  ? 1.10829 0.34142 0.45327 -0.12969 0.18276  0.00734  87  ASP A C   
323  O O   . ASP A 87  ? 1.11684 0.33812 0.47030 -0.13673 0.18785  0.00393  87  ASP A O   
324  C CB  . ASP A 87  ? 1.24263 0.37601 0.48101 -0.15207 0.20171  0.01511  87  ASP A CB  
325  C CG  . ASP A 87  ? 1.29209 0.37325 0.49091 -0.13520 0.17728  0.02102  87  ASP A CG  
326  O OD1 . ASP A 87  ? 1.31019 0.36540 0.47912 -0.11018 0.14932  0.02698  87  ASP A OD1 
327  O OD2 . ASP A 87  ? 1.31363 0.38093 0.51336 -0.14555 0.18414  0.01855  87  ASP A OD2 
328  N N   . ARG A 88  ? 1.03898 0.33861 0.43463 -0.11366 0.16888  0.00294  88  ARG A N   
329  C CA  . ARG A 88  ? 0.97056 0.33298 0.43153 -0.10276 0.15936  -0.00544 88  ARG A CA  
330  C C   . ARG A 88  ? 0.92069 0.33514 0.41246 -0.08061 0.13733  -0.00567 88  ARG A C   
331  O O   . ARG A 88  ? 0.92859 0.33891 0.40232 -0.07788 0.13304  -0.00120 88  ARG A O   
332  C CB  . ARG A 88  ? 0.94476 0.35048 0.45907 -0.12499 0.18398  -0.01446 88  ARG A CB  
333  C CG  . ARG A 88  ? 0.96594 0.38978 0.48999 -0.14233 0.20366  -0.01585 88  ARG A CG  
334  C CD  . ARG A 88  ? 0.99178 0.45259 0.56669 -0.16387 0.22708  -0.02708 88  ARG A CD  
335  N NE  . ARG A 88  ? 1.01415 0.51872 0.64057 -0.15500 0.21677  -0.03436 88  ARG A NE  
336  C CZ  . ARG A 88  ? 1.02665 0.58178 0.71049 -0.16416 0.22600  -0.04515 88  ARG A CZ  
337  N NH1 . ARG A 88  ? 0.95307 0.52549 0.65603 -0.18189 0.24546  -0.05141 88  ARG A NH1 
338  N NH2 . ARG A 88  ? 1.05021 0.63870 0.77210 -0.15408 0.21442  -0.05090 88  ARG A NH2 
339  N N   . ASN A 89  ? 0.87202 0.33514 0.40989 -0.06553 0.12376  -0.01135 89  ASN A N   
340  C CA  . ASN A 89  ? 0.82294 0.34115 0.39626 -0.04679 0.10471  -0.01208 89  ASN A CA  
341  C C   . ASN A 89  ? 0.75762 0.33732 0.38610 -0.05947 0.11707  -0.01560 89  ASN A C   
342  O O   . ASN A 89  ? 0.73205 0.33166 0.39088 -0.07336 0.13265  -0.02146 89  ASN A O   
343  C CB  . ASN A 89  ? 0.80774 0.34874 0.40092 -0.02425 0.08524  -0.01692 89  ASN A CB  
344  C CG  . ASN A 89  ? 0.87336 0.35448 0.41351 -0.00713 0.06746  -0.01498 89  ASN A CG  
345  O OD1 . ASN A 89  ? 0.93477 0.36720 0.42566 -0.00505 0.06122  -0.00849 89  ASN A OD1 
346  N ND2 . ASN A 89  ? 0.87705 0.35892 0.42461 0.00635  0.05769  -0.02130 89  ASN A ND2 
347  N N   . VAL A 90  ? 0.73380 0.34128 0.37473 -0.05417 0.10805  -0.01267 90  VAL A N   
348  C CA  . VAL A 90  ? 0.67969 0.33803 0.36658 -0.06545 0.11660  -0.01509 90  VAL A CA  
349  C C   . VAL A 90  ? 0.63495 0.34679 0.35879 -0.05018 0.09708  -0.01384 90  VAL A C   
350  O O   . VAL A 90  ? 0.65867 0.36784 0.37092 -0.03152 0.07794  -0.01173 90  VAL A O   
351  C CB  . VAL A 90  ? 0.69924 0.33550 0.36402 -0.07970 0.12873  -0.01324 90  VAL A CB  
352  C CG1 . VAL A 90  ? 0.74349 0.33215 0.37543 -0.09852 0.15258  -0.01516 90  VAL A CG1 
353  C CG2 . VAL A 90  ? 0.73172 0.34255 0.35923 -0.06614 0.11094  -0.00689 90  VAL A CG2 
354  N N   . ALA A 91  ? 0.58407 0.34457 0.35338 -0.05883 0.10190  -0.01579 91  ALA A N   
355  C CA  . ALA A 91  ? 0.56436 0.37630 0.37012 -0.05011 0.08681  -0.01338 91  ALA A CA  
356  C C   . ALA A 91  ? 0.53021 0.35085 0.34347 -0.05951 0.08714  -0.01106 91  ALA A C   
357  O O   . ALA A 91  ? 0.58231 0.40324 0.40525 -0.07491 0.10185  -0.01462 91  ALA A O   
358  C CB  . ALA A 91  ? 0.56221 0.42197 0.41234 -0.05140 0.08932  -0.01672 91  ALA A CB  
359  N N   . ILE A 92  ? 0.53205 0.36049 0.34286 -0.04959 0.06985  -0.00673 92  ILE A N   
360  C CA  . ILE A 92  ? 0.53739 0.36791 0.34992 -0.05612 0.06642  -0.00492 92  ILE A CA  
361  C C   . ILE A 92  ? 0.52480 0.40916 0.38258 -0.05408 0.05281  -0.00195 92  ILE A C   
362  O O   . ILE A 92  ? 0.53586 0.44090 0.40388 -0.04133 0.03780  0.00027  92  ILE A O   
363  C CB  . ILE A 92  ? 0.57697 0.36267 0.34227 -0.04775 0.05648  -0.00266 92  ILE A CB  
364  C CG1 . ILE A 92  ? 0.62648 0.35443 0.34215 -0.05487 0.07351  -0.00414 92  ILE A CG1 
365  C CG2 . ILE A 92  ? 0.56983 0.36425 0.34179 -0.05123 0.04792  -0.00158 92  ILE A CG2 
366  C CD1 . ILE A 92  ? 0.68048 0.36068 0.34656 -0.04057 0.06282  -0.00141 92  ILE A CD1 
367  N N   . LYS A 93  ? 0.49776 0.40417 0.38261 -0.06695 0.05787  -0.00252 93  LYS A N   
368  C CA  . LYS A 93  ? 0.49742 0.44862 0.42151 -0.06895 0.04576  0.00167  93  LYS A CA  
369  C C   . LYS A 93  ? 0.47871 0.42043 0.39791 -0.07278 0.03658  0.00264  93  LYS A C   
370  O O   . LYS A 93  ? 0.44875 0.36451 0.35132 -0.08037 0.04614  -0.00195 93  LYS A O   
371  C CB  . LYS A 93  ? 0.52661 0.50740 0.48411 -0.07960 0.05458  0.00044  93  LYS A CB  
372  C CG  . LYS A 93  ? 0.51345 0.53509 0.50676 -0.08427 0.04283  0.00643  93  LYS A CG  
373  C CD  . LYS A 93  ? 0.52649 0.57264 0.54590 -0.09223 0.04963  0.00576  93  LYS A CD  
374  C CE  . LYS A 93  ? 0.67004 0.75650 0.71877 -0.09547 0.03866  0.01425  93  LYS A CE  
375  N NZ  . LYS A 93  ? 0.66969 0.77142 0.73830 -0.10488 0.04178  0.01429  93  LYS A NZ  
376  N N   . LYS A 94  ? 0.44995 0.41395 0.38501 -0.06770 0.01832  0.00735  94  LYS A N   
377  C CA  . LYS A 94  ? 0.49936 0.45447 0.43054 -0.06956 0.00549  0.00789  94  LYS A CA  
378  C C   . LYS A 94  ? 0.50197 0.49490 0.47489 -0.08017 -0.00201 0.01192  94  LYS A C   
379  O O   . LYS A 94  ? 0.52591 0.55606 0.52809 -0.07987 -0.01008 0.01745  94  LYS A O   
380  C CB  . LYS A 94  ? 0.50675 0.45324 0.42263 -0.05561 -0.01287 0.00904  94  LYS A CB  
381  C CG  . LYS A 94  ? 0.47641 0.41790 0.39276 -0.05659 -0.02999 0.00916  94  LYS A CG  
382  C CD  . LYS A 94  ? 0.48062 0.44129 0.41041 -0.04545 -0.05213 0.01067  94  LYS A CD  
383  C CE  . LYS A 94  ? 0.55414 0.50404 0.48075 -0.04543 -0.07115 0.00941  94  LYS A CE  
384  N NZ  . LYS A 94  ? 0.58534 0.56626 0.54055 -0.03833 -0.09341 0.01010  94  LYS A NZ  
385  N N   . LEU A 95  ? 0.47891 0.46134 0.45344 -0.08969 0.00070  0.00871  95  LEU A N   
386  C CA  . LEU A 95  ? 0.48016 0.48854 0.48839 -0.09984 -0.00917 0.01233  95  LEU A CA  
387  C C   . LEU A 95  ? 0.47747 0.47741 0.48258 -0.09836 -0.02827 0.01305  95  LEU A C   
388  O O   . LEU A 95  ? 0.45003 0.41910 0.43163 -0.09734 -0.02843 0.00636  95  LEU A O   
389  C CB  . LEU A 95  ? 0.47112 0.47317 0.48578 -0.10903 0.00181  0.00610  95  LEU A CB  
390  C CG  . LEU A 95  ? 0.45688 0.45949 0.47096 -0.11034 0.02107  0.00177  95  LEU A CG  
391  C CD1 . LEU A 95  ? 0.41173 0.40953 0.43650 -0.11849 0.02855  -0.00727 95  LEU A CD1 
392  C CD2 . LEU A 95  ? 0.56641 0.60239 0.60288 -0.11020 0.02012  0.00932  95  LEU A CD2 
393  N N   . SER A 96  ? 0.42543 0.45376 0.45489 -0.09865 -0.04396 0.02020  96  SER A N   
394  C CA  . SER A 96  ? 0.40579 0.42912 0.43674 -0.09712 -0.06478 0.02047  96  SER A CA  
395  C C   . SER A 96  ? 0.44697 0.47419 0.49813 -0.10972 -0.07374 0.02180  96  SER A C   
396  O O   . SER A 96  ? 0.39924 0.45663 0.48290 -0.12053 -0.07816 0.02973  96  SER A O   
397  C CB  . SER A 96  ? 0.40006 0.45556 0.45396 -0.09329 -0.07763 0.02584  96  SER A CB  
398  O OG  . SER A 96  ? 0.45711 0.51339 0.49725 -0.08096 -0.06949 0.02394  96  SER A OG  
399  N N   . ARG A 97  ? 0.45507 0.44973 0.48451 -0.10814 -0.07672 0.01376  97  ARG A N   
400  C CA  . ARG A 97  ? 0.45276 0.44334 0.49617 -0.11680 -0.08829 0.01188  97  ARG A CA  
401  C C   . ARG A 97  ? 0.43914 0.45066 0.51015 -0.12840 -0.08239 0.01631  97  ARG A C   
402  O O   . ARG A 97  ? 0.43648 0.46955 0.53558 -0.13840 -0.09537 0.02543  97  ARG A O   
403  C CB  . ARG A 97  ? 0.46089 0.45983 0.52057 -0.11893 -0.11366 0.01638  97  ARG A CB  
404  C CG  . ARG A 97  ? 0.53438 0.50342 0.56302 -0.10667 -0.12469 0.00875  97  ARG A CG  
405  C CD  . ARG A 97  ? 0.53702 0.51754 0.58611 -0.10827 -0.15139 0.01209  97  ARG A CD  
406  N NE  . ARG A 97  ? 0.71608 0.70774 0.79571 -0.12256 -0.16449 0.01618  97  ARG A NE  
407  C CZ  . ARG A 97  ? 0.80877 0.77520 0.88017 -0.12327 -0.17721 0.00906  97  ARG A CZ  
408  N NH1 . ARG A 97  ? 0.70134 0.63206 0.73446 -0.11105 -0.17627 -0.00293 97  ARG A NH1 
409  N NH2 . ARG A 97  ? 0.69097 0.66630 0.79089 -0.13658 -0.19133 0.01390  97  ARG A NH2 
410  N N   . PRO A 98  ? 0.46695 0.47123 0.52996 -0.12798 -0.06368 0.00994  98  PRO A N   
411  C CA  . PRO A 98  ? 0.45322 0.47595 0.54034 -0.13694 -0.05977 0.01335  98  PRO A CA  
412  C C   . PRO A 98  ? 0.47656 0.49373 0.57943 -0.14442 -0.07554 0.01162  98  PRO A C   
413  O O   . PRO A 98  ? 0.45825 0.48894 0.58056 -0.15242 -0.07853 0.01706  98  PRO A O   
414  C CB  . PRO A 98  ? 0.45659 0.46897 0.52989 -0.13283 -0.03733 0.00336  98  PRO A CB  
415  C CG  . PRO A 98  ? 0.44806 0.42974 0.49092 -0.12558 -0.03163 -0.00748 98  PRO A CG  
416  C CD  . PRO A 98  ? 0.46010 0.43710 0.49104 -0.12026 -0.04594 -0.00134 98  PRO A CD  
417  N N   . PHE A 99  ? 0.51420 0.50930 0.60677 -0.14128 -0.08702 0.00386  99  PHE A N   
418  C CA  . PHE A 99  ? 0.47163 0.45756 0.57770 -0.14653 -0.10483 0.00045  99  PHE A CA  
419  C C   . PHE A 99  ? 0.46015 0.45675 0.58541 -0.15613 -0.12789 0.01399  99  PHE A C   
420  O O   . PHE A 99  ? 0.51903 0.50341 0.65346 -0.16082 -0.14660 0.01222  99  PHE A O   
421  C CB  . PHE A 99  ? 0.51281 0.46996 0.59818 -0.13807 -0.10680 -0.01579 99  PHE A CB  
422  C CG  . PHE A 99  ? 0.52528 0.46921 0.58427 -0.13005 -0.10693 -0.01660 99  PHE A CG  
423  C CD1 . PHE A 99  ? 0.53071 0.47155 0.59282 -0.13063 -0.12988 -0.01139 99  PHE A CD1 
424  C CD2 . PHE A 99  ? 0.53965 0.47183 0.56963 -0.12219 -0.08553 -0.02262 99  PHE A CD2 
425  C CE1 . PHE A 99  ? 0.59876 0.52554 0.63554 -0.12149 -0.13304 -0.01328 99  PHE A CE1 
426  C CE2 . PHE A 99  ? 0.55025 0.46481 0.55070 -0.11376 -0.08806 -0.02299 99  PHE A CE2 
427  C CZ  . PHE A 99  ? 0.58216 0.49429 0.58602 -0.11238 -0.11261 -0.01885 99  PHE A CZ  
428  N N   . GLN A 100 ? 0.42318 0.44259 0.55607 -0.15948 -0.12712 0.02646  100 GLN A N   
429  C CA  . GLN A 100 ? 0.47768 0.50940 0.63055 -0.16992 -0.14744 0.03795  100 GLN A CA  
430  C C   . GLN A 100 ? 0.47638 0.51562 0.64648 -0.18146 -0.15304 0.04794  100 GLN A C   
431  O O   . GLN A 100 ? 0.49258 0.52799 0.66857 -0.18394 -0.16585 0.05323  100 GLN A O   
432  C CB  . GLN A 100 ? 0.45513 0.51403 0.61462 -0.16890 -0.14258 0.04592  100 GLN A CB  
433  C CG  . GLN A 100 ? 0.45834 0.54479 0.62488 -0.17132 -0.12357 0.05343  100 GLN A CG  
434  C CD  . GLN A 100 ? 0.44264 0.55459 0.61398 -0.16587 -0.11851 0.05671  100 GLN A CD  
435  O OE1 . GLN A 100 ? 0.43224 0.57045 0.62747 -0.17481 -0.12773 0.06532  100 GLN A OE1 
436  N NE2 . GLN A 100 ? 0.41173 0.51584 0.56119 -0.15135 -0.10420 0.04901  100 GLN A NE2 
437  N N   . ASN A 101 ? 0.47994 0.52522 0.64939 -0.18192 -0.13907 0.04908  101 ASN A N   
438  C CA  . ASN A 101 ? 0.52567 0.56863 0.69775 -0.18483 -0.14125 0.05590  101 ASN A CA  
439  C C   . ASN A 101 ? 0.55999 0.59475 0.72750 -0.18083 -0.13273 0.04742  101 ASN A C   
440  O O   . ASN A 101 ? 0.53001 0.56434 0.69440 -0.17725 -0.12201 0.03717  101 ASN A O   
441  C CB  . ASN A 101 ? 0.52328 0.59247 0.70308 -0.19273 -0.13503 0.07190  101 ASN A CB  
442  C CG  . ASN A 101 ? 0.52656 0.62162 0.70785 -0.19185 -0.11638 0.07383  101 ASN A CG  
443  O OD1 . ASN A 101 ? 0.54400 0.63830 0.71991 -0.18936 -0.10603 0.07059  101 ASN A OD1 
444  N ND2 . ASN A 101 ? 0.49617 0.61511 0.68628 -0.19325 -0.11318 0.07822  101 ASN A ND2 
445  N N   . GLN A 102 ? 0.58894 0.61574 0.75615 -0.18259 -0.13884 0.05186  102 GLN A N   
446  C CA  . GLN A 102 ? 0.59476 0.61279 0.76063 -0.17797 -0.13532 0.04216  102 GLN A CA  
447  C C   . GLN A 102 ? 0.57291 0.61143 0.73956 -0.17892 -0.11707 0.04419  102 GLN A C   
448  O O   . GLN A 102 ? 0.58834 0.62454 0.75665 -0.17410 -0.10851 0.03111  102 GLN A O   
449  C CB  . GLN A 102 ? 0.65356 0.65561 0.81711 -0.18019 -0.15050 0.04825  102 GLN A CB  
450  C CG  . GLN A 102 ? 0.70675 0.68226 0.86979 -0.17361 -0.16768 0.03705  102 GLN A CG  
451  C CD  . GLN A 102 ? 0.79801 0.76364 0.96431 -0.16400 -0.16704 0.01804  102 GLN A CD  
452  O OE1 . GLN A 102 ? 0.81257 0.77252 0.98163 -0.15663 -0.16465 0.00028  102 GLN A OE1 
453  N NE2 . GLN A 102 ? 0.86031 0.82399 1.02650 -0.16444 -0.16963 0.02080  102 GLN A NE2 
454  N N   . THR A 103 ? 0.58003 0.63959 0.74653 -0.18515 -0.11051 0.05938  103 THR A N   
455  C CA  . THR A 103 ? 0.59227 0.67177 0.75818 -0.18506 -0.09392 0.06153  103 THR A CA  
456  C C   . THR A 103 ? 0.58038 0.66770 0.74709 -0.18032 -0.08016 0.05203  103 THR A C   
457  O O   . THR A 103 ? 0.62329 0.71190 0.78858 -0.17641 -0.06849 0.04370  103 THR A O   
458  C CB  . THR A 103 ? 0.60434 0.70693 0.76999 -0.19227 -0.08922 0.07825  103 THR A CB  
459  O OG1 . THR A 103 ? 0.65758 0.74890 0.81988 -0.20031 -0.10298 0.08910  103 THR A OG1 
460  C CG2 . THR A 103 ? 0.63736 0.75809 0.79993 -0.19155 -0.07436 0.08024  103 THR A CG2 
461  N N   . HIS A 104 ? 0.56480 0.65527 0.73214 -0.18083 -0.08216 0.05313  104 HIS A N   
462  C CA  . HIS A 104 ? 0.56337 0.65122 0.71848 -0.16918 -0.06704 0.04272  104 HIS A CA  
463  C C   . HIS A 104 ? 0.55224 0.61458 0.69851 -0.16168 -0.06311 0.02521  104 HIS A C   
464  O O   . HIS A 104 ? 0.55226 0.61102 0.68842 -0.15423 -0.04555 0.01556  104 HIS A O   
465  C CB  . HIS A 104 ? 0.54339 0.63493 0.69599 -0.16719 -0.07260 0.04626  104 HIS A CB  
466  C CG  . HIS A 104 ? 0.60719 0.72924 0.76727 -0.16872 -0.06724 0.05698  104 HIS A CG  
467  N ND1 . HIS A 104 ? 0.58516 0.72559 0.76122 -0.17751 -0.07941 0.06765  104 HIS A ND1 
468  C CD2 . HIS A 104 ? 0.76745 0.90630 0.92317 -0.16221 -0.05115 0.05701  104 HIS A CD2 
469  C CE1 . HIS A 104 ? 0.62903 0.79939 0.81191 -0.17603 -0.06994 0.07296  104 HIS A CE1 
470  N NE2 . HIS A 104 ? 0.81242 0.98120 0.98186 -0.16591 -0.05344 0.06663  104 HIS A NE2 
471  N N   . ALA A 105 ? 0.55167 0.59644 0.70237 -0.16402 -0.07897 0.02008  105 ALA A N   
472  C CA  . ALA A 105 ? 0.56739 0.59135 0.71165 -0.15654 -0.07457 0.00115  105 ALA A CA  
473  C C   . ALA A 105 ? 0.57775 0.60337 0.73111 -0.15507 -0.06675 -0.00871 105 ALA A C   
474  O O   . ALA A 105 ? 0.59467 0.61417 0.74324 -0.14889 -0.05080 -0.02426 105 ALA A O   
475  C CB  . ALA A 105 ? 0.56982 0.57553 0.71727 -0.15770 -0.09560 -0.00334 105 ALA A CB  
476  N N   . LYS A 106 ? 0.58412 0.61691 0.74999 -0.16124 -0.07816 -0.00030 106 LYS A N   
477  C CA  . LYS A 106 ? 0.58730 0.62120 0.76223 -0.15855 -0.07421 -0.01027 106 LYS A CA  
478  C C   . LYS A 106 ? 0.57886 0.62611 0.74871 -0.15472 -0.05101 -0.01285 106 LYS A C   
479  O O   . LYS A 106 ? 0.60100 0.64607 0.77630 -0.14978 -0.04003 -0.02906 106 LYS A O   
480  C CB  . LYS A 106 ? 0.61438 0.64910 0.79544 -0.16495 -0.09195 0.00167  106 LYS A CB  
481  C CG  . LYS A 106 ? 0.66977 0.68453 0.85430 -0.15952 -0.11006 -0.00804 106 LYS A CG  
482  C CD  . LYS A 106 ? 0.73908 0.74856 0.91772 -0.16282 -0.12486 0.00659  106 LYS A CD  
483  C CE  . LYS A 106 ? 0.83380 0.81994 1.01369 -0.15650 -0.14526 -0.00174 106 LYS A CE  
484  N NZ  . LYS A 106 ? 0.93450 0.91803 1.12624 -0.14644 -0.14423 -0.02420 106 LYS A NZ  
485  N N   . ARG A 107 ? 0.58396 0.64572 0.74522 -0.15686 -0.04380 0.00172  107 ARG A N   
486  C CA  . ARG A 107 ? 0.62118 0.69351 0.77624 -0.15234 -0.02412 -0.00041 107 ARG A CA  
487  C C   . ARG A 107 ? 0.60643 0.66687 0.74871 -0.14626 -0.00745 -0.01217 107 ARG A C   
488  O O   . ARG A 107 ? 0.60610 0.66458 0.74710 -0.14307 0.00816  -0.02297 107 ARG A O   
489  C CB  . ARG A 107 ? 0.70386 0.79641 0.85445 -0.15492 -0.02256 0.01683  107 ARG A CB  
490  C CG  . ARG A 107 ? 0.78165 0.88383 0.92397 -0.14847 -0.00429 0.01457  107 ARG A CG  
491  C CD  . ARG A 107 ? 0.90953 1.03642 1.05236 -0.15057 -0.00410 0.02895  107 ARG A CD  
492  N NE  . ARG A 107 ? 0.95452 1.08829 1.10485 -0.15867 -0.01567 0.03756  107 ARG A NE  
493  C CZ  . ARG A 107 ? 0.93906 1.07919 1.09395 -0.16856 -0.02857 0.05130  107 ARG A CZ  
494  N NH1 . ARG A 107 ? 0.90121 1.04513 1.05856 -0.17116 -0.03274 0.05682  107 ARG A NH1 
495  N NH2 . ARG A 107 ? 0.96863 1.10918 1.12445 -0.17654 -0.03844 0.05964  107 ARG A NH2 
496  N N   . ALA A 108 ? 0.63714 0.68735 0.76802 -0.14526 -0.01095 -0.01017 108 ALA A N   
497  C CA  . ALA A 108 ? 0.61451 0.64801 0.72549 -0.13997 0.00432  -0.01965 108 ALA A CA  
498  C C   . ALA A 108 ? 0.62993 0.65036 0.74472 -0.13954 0.01322  -0.03875 108 ALA A C   
499  O O   . ALA A 108 ? 0.66332 0.67676 0.76905 -0.13829 0.03289  -0.04837 108 ALA A O   
500  C CB  . ALA A 108 ? 0.57702 0.59997 0.67307 -0.13804 -0.00501 -0.01408 108 ALA A CB  
501  N N   . TYR A 109 ? 0.60990 0.62712 0.73922 -0.14092 -0.00117 -0.04536 109 TYR A N   
502  C CA  . TYR A 109 ? 0.62504 0.63472 0.76323 -0.13941 0.00647  -0.06646 109 TYR A CA  
503  C C   . TYR A 109 ? 0.62621 0.64801 0.78289 -0.14015 0.01635  -0.07564 109 TYR A C   
504  O O   . TYR A 109 ? 0.63979 0.65910 0.80073 -0.13999 0.03356  -0.09312 109 TYR A O   
505  C CB  . TYR A 109 ? 0.60184 0.60602 0.75379 -0.13865 -0.01504 -0.07242 109 TYR A CB  
506  C CG  . TYR A 109 ? 0.60915 0.60849 0.77282 -0.13524 -0.00820 -0.09714 109 TYR A CG  
507  C CD1 . TYR A 109 ? 0.62800 0.61640 0.77420 -0.13371 0.01166  -0.10966 109 TYR A CD1 
508  C CD2 . TYR A 109 ? 0.63675 0.64229 0.82814 -0.13331 -0.02165 -0.10885 109 TYR A CD2 
509  C CE1 . TYR A 109 ? 0.64198 0.63046 0.80114 -0.13139 0.02064  -0.13394 109 TYR A CE1 
510  C CE2 . TYR A 109 ? 0.69155 0.69726 0.89869 -0.12901 -0.01560 -0.13440 109 TYR A CE2 
511  C CZ  . TYR A 109 ? 0.67316 0.67271 0.86568 -0.12859 0.00693  -0.14724 109 TYR A CZ  
512  O OH  . TYR A 109 ? 0.71065 0.71467 0.92091 -0.12512 0.01564  -0.17422 109 TYR A OH  
513  N N   . ARG A 110 ? 0.66993 0.70505 0.83747 -0.14153 0.00595  -0.06464 110 ARG A N   
514  C CA  . ARG A 110 ? 0.65797 0.70345 0.84174 -0.14103 0.01213  -0.07330 110 ARG A CA  
515  C C   . ARG A 110 ? 0.68546 0.73086 0.85813 -0.14115 0.03668  -0.07695 110 ARG A C   
516  O O   . ARG A 110 ? 0.70983 0.75378 0.89217 -0.14193 0.05141  -0.09474 110 ARG A O   
517  C CB  . ARG A 110 ? 0.63993 0.69639 0.82886 -0.14230 -0.00373 -0.05837 110 ARG A CB  
518  C CG  . ARG A 110 ? 0.67081 0.73366 0.87881 -0.14017 -0.00790 -0.06946 110 ARG A CG  
519  C CD  . ARG A 110 ? 0.75461 0.82623 0.95744 -0.14150 -0.01840 -0.05279 110 ARG A CD  
520  N NE  . ARG A 110 ? 0.65892 0.73664 0.87229 -0.13795 -0.01599 -0.06298 110 ARG A NE  
521  C CZ  . ARG A 110 ? 0.66111 0.73673 0.88462 -0.13583 -0.03426 -0.06662 110 ARG A CZ  
522  N NH1 . ARG A 110 ? 0.76144 0.82696 0.98480 -0.13763 -0.05626 -0.06006 110 ARG A NH1 
523  N NH2 . ARG A 110 ? 0.60476 0.68564 0.83729 -0.13154 -0.03215 -0.07736 110 ARG A NH2 
524  N N   . GLU A 111 ? 0.63767 0.68437 0.79085 -0.14067 0.04101  -0.06100 111 GLU A N   
525  C CA  . GLU A 111 ? 0.67113 0.71408 0.81135 -0.13996 0.06093  -0.06300 111 GLU A CA  
526  C C   . GLU A 111 ? 0.69486 0.71753 0.81649 -0.14157 0.07869  -0.07208 111 GLU A C   
527  O O   . GLU A 111 ? 0.72560 0.74019 0.83838 -0.14335 0.09689  -0.07782 111 GLU A O   
528  C CB  . GLU A 111 ? 0.69498 0.74475 0.81966 -0.13682 0.05834  -0.04511 111 GLU A CB  
529  C CG  . GLU A 111 ? 0.68239 0.75158 0.81938 -0.13718 0.04109  -0.03287 111 GLU A CG  
530  C CD  . GLU A 111 ? 0.62068 0.70360 0.75158 -0.13369 0.04511  -0.02387 111 GLU A CD  
531  O OE1 . GLU A 111 ? 0.66590 0.74197 0.78116 -0.12961 0.05765  -0.02452 111 GLU A OE1 
532  O OE2 . GLU A 111 ? 0.57694 0.67563 0.71635 -0.13469 0.03532  -0.01644 111 GLU A OE2 
533  N N   . LEU A 112 ? 0.69342 0.70528 0.80633 -0.14149 0.07378  -0.07343 112 LEU A N   
534  C CA  . LEU A 112 ? 0.71306 0.70348 0.80376 -0.14342 0.09164  -0.08276 112 LEU A CA  
535  C C   . LEU A 112 ? 0.74559 0.73876 0.85602 -0.14831 0.10639  -0.10466 112 LEU A C   
536  O O   . LEU A 112 ? 0.83225 0.81096 0.92674 -0.15324 0.12895  -0.11323 112 LEU A O   
537  C CB  . LEU A 112 ? 0.68507 0.66266 0.75868 -0.14064 0.08079  -0.07890 112 LEU A CB  
538  C CG  . LEU A 112 ? 0.66561 0.62088 0.69938 -0.13751 0.08510  -0.06845 112 LEU A CG  
539  C CD1 . LEU A 112 ? 0.65851 0.59756 0.67521 -0.13497 0.07706  -0.07112 112 LEU A CD1 
540  C CD2 . LEU A 112 ? 0.65548 0.59185 0.66538 -0.14079 0.11011  -0.07340 112 LEU A CD2 
541  N N   . VAL A 113 ? 0.72311 0.73410 0.86795 -0.14734 0.09380  -0.11443 113 VAL A N   
542  C CA  . VAL A 113 ? 0.72667 0.74555 0.89762 -0.15056 0.10554  -0.13835 113 VAL A CA  
543  C C   . VAL A 113 ? 0.79601 0.82576 0.98391 -0.15330 0.11568  -0.14393 113 VAL A C   
544  O O   . VAL A 113 ? 0.86612 0.89556 1.05784 -0.15542 0.13525  -0.15807 113 VAL A O   
545  C CB  . VAL A 113 ? 0.71014 0.74039 0.91018 -0.14569 0.08399  -0.14882 113 VAL A CB  
546  C CG1 . VAL A 113 ? 0.69600 0.73956 0.92709 -0.14464 0.09328  -0.17461 113 VAL A CG1 
547  C CG2 . VAL A 113 ? 0.69307 0.71004 0.87554 -0.14260 0.07436  -0.14562 113 VAL A CG2 
548  N N   . LEU A 114 ? 0.77693 0.81557 0.96895 -0.14906 0.10109  -0.13073 114 LEU A N   
549  C CA  . LEU A 114 ? 0.80335 0.85094 1.00695 -0.14514 0.10432  -0.13488 114 LEU A CA  
550  C C   . LEU A 114 ? 0.86338 0.89795 1.04511 -0.14975 0.12607  -0.13221 114 LEU A C   
551  O O   . LEU A 114 ? 0.89635 0.93363 1.08727 -0.14856 0.13457  -0.14177 114 LEU A O   
552  C CB  . LEU A 114 ? 0.71941 0.77825 0.93022 -0.14084 0.08338  -0.12239 114 LEU A CB  
553  C CG  . LEU A 114 ? 0.67747 0.74280 0.90337 -0.13720 0.05869  -0.12111 114 LEU A CG  
554  C CD1 . LEU A 114 ? 0.65044 0.72298 0.87343 -0.13765 0.04195  -0.10398 114 LEU A CD1 
555  C CD2 . LEU A 114 ? 0.67123 0.74338 0.92313 -0.13005 0.05220  -0.14023 114 LEU A CD2 
556  N N   . MET A 115 ? 0.82895 0.84684 0.98099 -0.15491 0.13397  -0.11981 115 MET A N   
557  C CA  . MET A 115 ? 0.88379 0.88400 1.01050 -0.15813 0.15107  -0.11514 115 MET A CA  
558  C C   . MET A 115 ? 1.00580 0.98834 1.11943 -0.16435 0.17379  -0.12752 115 MET A C   
559  O O   . MET A 115 ? 1.00033 0.96570 1.09493 -0.16734 0.18755  -0.12650 115 MET A O   
560  C CB  . MET A 115 ? 0.83960 0.82644 0.93243 -0.15334 0.14468  -0.09507 115 MET A CB  
561  C CG  . MET A 115 ? 0.83683 0.83134 0.92701 -0.14698 0.13688  -0.08389 115 MET A CG  
562  S SD  . MET A 115 ? 0.95766 0.94802 1.01901 -0.13738 0.12340  -0.06266 115 MET A SD  
563  C CE  . MET A 115 ? 0.76944 0.72015 0.78720 -0.13887 0.14066  -0.06168 115 MET A CE  
564  N N   . LYS A 116 ? 1.23818 1.22396 1.36132 -0.16713 0.17820  -0.13990 116 LYS A N   
565  C CA  . LYS A 116 ? 1.26786 1.24555 1.38813 -0.17359 0.20061  -0.15628 116 LYS A CA  
566  C C   . LYS A 116 ? 1.25707 1.26039 1.41958 -0.16970 0.19848  -0.17648 116 LYS A C   
567  O O   . LYS A 116 ? 1.26481 1.26665 1.43226 -0.17544 0.21716  -0.19312 116 LYS A O   
568  C CB  . LYS A 116 ? 1.29603 1.26003 1.39737 -0.18069 0.21135  -0.15975 116 LYS A CB  
569  C CG  . LYS A 116 ? 1.31594 1.24828 1.36800 -0.18289 0.21435  -0.14072 116 LYS A CG  
570  C CD  . LYS A 116 ? 1.32847 1.25783 1.36787 -0.17445 0.19798  -0.13586 116 LYS A CD  
571  C CE  . LYS A 116 ? 1.45617 1.37716 1.48638 -0.18017 0.21544  -0.15201 116 LYS A CE  
572  N NZ  . LYS A 116 ? 1.33977 1.25974 1.36318 -0.17087 0.19658  -0.15039 116 LYS A NZ  
573  N N   . CYS A 117 ? 1.09832 1.12325 1.28958 -0.16034 0.17583  -0.17554 117 CYS A N   
574  C CA  . CYS A 117 ? 0.97585 1.02341 1.20644 -0.15425 0.16973  -0.19379 117 CYS A CA  
575  C C   . CYS A 117 ? 0.96472 1.01756 1.20553 -0.15036 0.16557  -0.19331 117 CYS A C   
576  O O   . CYS A 117 ? 1.00607 1.07213 1.27461 -0.14801 0.16860  -0.21104 117 CYS A O   
577  C CB  . CYS A 117 ? 1.01229 1.07532 1.26529 -0.14576 0.14450  -0.19428 117 CYS A CB  
578  S SG  . CYS A 117 ? 1.28203 1.36776 1.57608 -0.13366 0.12418  -0.20691 117 CYS A SG  
579  N N   . VAL A 118 ? 1.01512 1.05865 1.23579 -0.14991 0.15944  -0.17532 118 VAL A N   
580  C CA  . VAL A 118 ? 0.95406 1.00226 1.18354 -0.14653 0.15418  -0.17489 118 VAL A CA  
581  C C   . VAL A 118 ? 0.97448 1.00109 1.17449 -0.15313 0.16958  -0.16626 118 VAL A C   
582  O O   . VAL A 118 ? 0.95676 0.96804 1.12746 -0.15584 0.17177  -0.15095 118 VAL A O   
583  C CB  . VAL A 118 ? 0.88095 0.94050 1.11714 -0.13940 0.12993  -0.16337 118 VAL A CB  
584  C CG1 . VAL A 118 ? 0.81312 0.87028 1.04275 -0.13903 0.12885  -0.15698 118 VAL A CG1 
585  C CG2 . VAL A 118 ? 0.85252 0.92989 1.12077 -0.13165 0.11276  -0.17544 118 VAL A CG2 
586  N N   . ASN A 119 ? 0.96279 0.98707 1.17106 -0.15561 0.17928  -0.17650 119 ASN A N   
587  C CA  . ASN A 119 ? 1.00252 1.00451 1.18519 -0.16153 0.19115  -0.16927 119 ASN A CA  
588  C C   . ASN A 119 ? 1.00210 1.01279 1.20273 -0.15798 0.18327  -0.17328 119 ASN A C   
589  O O   . ASN A 119 ? 1.01279 1.04333 1.24600 -0.15326 0.17540  -0.18675 119 ASN A O   
590  C CB  . ASN A 119 ? 1.07354 1.05584 1.24112 -0.17211 0.21475  -0.17743 119 ASN A CB  
591  C CG  . ASN A 119 ? 1.14834 1.14377 1.34733 -0.17457 0.22216  -0.19773 119 ASN A CG  
592  O OD1 . ASN A 119 ? 1.12167 1.14285 1.35649 -0.16706 0.20984  -0.20884 119 ASN A OD1 
593  N ND2 . ASN A 119 ? 1.17395 1.15026 1.35883 -0.18549 0.24202  -0.20261 119 ASN A ND2 
594  N N   . HIS A 120 ? 0.82458 0.81927 1.00375 -0.15994 0.18492  -0.16251 120 HIS A N   
595  C CA  . HIS A 120 ? 0.72588 0.72523 0.91820 -0.15769 0.17837  -0.16642 120 HIS A CA  
596  C C   . HIS A 120 ? 0.66537 0.63991 0.82689 -0.16171 0.18452  -0.15454 120 HIS A C   
597  O O   . HIS A 120 ? 0.65663 0.61724 0.79031 -0.16296 0.18773  -0.14090 120 HIS A O   
598  C CB  . HIS A 120 ? 0.67990 0.70478 0.89510 -0.14853 0.15681  -0.16688 120 HIS A CB  
599  C CG  . HIS A 120 ? 0.68044 0.71402 0.91737 -0.14541 0.14890  -0.17809 120 HIS A CG  
600  N ND1 . HIS A 120 ? 0.63514 0.66464 0.86470 -0.14493 0.14374  -0.17444 120 HIS A ND1 
601  C CD2 . HIS A 120 ? 0.72276 0.76907 0.98939 -0.14230 0.14476  -0.19438 120 HIS A CD2 
602  C CE1 . HIS A 120 ? 0.66264 0.70000 0.91426 -0.14137 0.13550  -0.18803 120 HIS A CE1 
603  N NE2 . HIS A 120 ? 0.75337 0.80145 1.02811 -0.13948 0.13568  -0.19934 120 HIS A NE2 
604  N N   . LYS A 121 ? 0.62920 0.59689 0.79636 -0.16327 0.18519  -0.16081 121 LYS A N   
605  C CA  . LYS A 121 ? 0.61694 0.55752 0.75621 -0.16639 0.18922  -0.15223 121 LYS A CA  
606  C C   . LYS A 121 ? 0.58203 0.53863 0.70850 -0.14782 0.16994  -0.13850 121 LYS A C   
607  O O   . LYS A 121 ? 0.55959 0.49984 0.65204 -0.13931 0.16782  -0.12509 121 LYS A O   
608  C CB  . LYS A 121 ? 0.64564 0.57356 0.79222 -0.16901 0.19094  -0.16320 121 LYS A CB  
609  C CG  . LYS A 121 ? 0.67288 0.63068 0.85911 -0.16280 0.17745  -0.17790 121 LYS A CG  
610  C CD  . LYS A 121 ? 0.90144 0.84519 1.08985 -0.16219 0.17323  -0.18679 121 LYS A CD  
611  C CE  . LYS A 121 ? 1.03058 1.00263 1.25436 -0.15376 0.15620  -0.20096 121 LYS A CE  
612  N NZ  . LYS A 121 ? 0.95482 0.93574 1.16440 -0.13590 0.13726  -0.19476 121 LYS A NZ  
613  N N   . ASN A 122 ? 0.60034 0.58842 0.75232 -0.14082 0.15526  -0.14176 122 ASN A N   
614  C CA  . ASN A 122 ? 0.53270 0.53897 0.67345 -0.12517 0.13855  -0.12872 122 ASN A CA  
615  C C   . ASN A 122 ? 0.51153 0.53273 0.65165 -0.12449 0.13325  -0.11761 122 ASN A C   
616  O O   . ASN A 122 ? 0.56102 0.59828 0.69229 -0.11436 0.12116  -0.10547 122 ASN A O   
617  C CB  . ASN A 122 ? 0.56742 0.59357 0.72876 -0.11751 0.12416  -0.13770 122 ASN A CB  
618  C CG  . ASN A 122 ? 0.57469 0.58664 0.73157 -0.11403 0.12503  -0.14660 122 ASN A CG  
619  O OD1 . ASN A 122 ? 0.59016 0.60682 0.77138 -0.11590 0.12055  -0.16242 122 ASN A OD1 
620  N ND2 . ASN A 122 ? 0.54386 0.53707 0.67005 -0.10803 0.12887  -0.13763 122 ASN A ND2 
621  N N   . ILE A 123 ? 0.55100 0.56785 0.70084 -0.13553 0.14226  -0.12224 123 ILE A N   
622  C CA  . ILE A 123 ? 0.54116 0.56574 0.68672 -0.13543 0.13781  -0.11223 123 ILE A CA  
623  C C   . ILE A 123 ? 0.55581 0.55464 0.67185 -0.14005 0.15123  -0.10492 123 ILE A C   
624  O O   . ILE A 123 ? 0.60773 0.58627 0.72054 -0.15091 0.16805  -0.11385 123 ILE A O   
625  C CB  . ILE A 123 ? 0.52913 0.56818 0.70692 -0.14181 0.13481  -0.12465 123 ILE A CB  
626  C CG1 . ILE A 123 ? 0.51639 0.57497 0.72037 -0.13640 0.11953  -0.13357 123 ILE A CG1 
627  C CG2 . ILE A 123 ? 0.51817 0.56305 0.69009 -0.14063 0.12726  -0.11401 123 ILE A CG2 
628  C CD1 . ILE A 123 ? 0.47081 0.54355 0.66354 -0.12567 0.10146  -0.11824 123 ILE A CD1 
629  N N   . ILE A 124 ? 0.53170 0.53058 0.62532 -0.13231 0.14369  -0.08897 124 ILE A N   
630  C CA  . ILE A 124 ? 0.59772 0.56880 0.65804 -0.13360 0.15248  -0.08141 124 ILE A CA  
631  C C   . ILE A 124 ? 0.62435 0.58436 0.68614 -0.14538 0.16424  -0.08804 124 ILE A C   
632  O O   . ILE A 124 ? 0.66005 0.63956 0.74707 -0.14829 0.15940  -0.09370 124 ILE A O   
633  C CB  . ILE A 124 ? 0.62576 0.60465 0.66868 -0.12189 0.13905  -0.06535 124 ILE A CB  
634  C CG1 . ILE A 124 ? 0.62770 0.62452 0.68280 -0.12330 0.12957  -0.06019 124 ILE A CG1 
635  C CG2 . ILE A 124 ? 0.60815 0.60681 0.65575 -0.11055 0.12851  -0.06120 124 ILE A CG2 
636  C CD1 . ILE A 124 ? 0.63114 0.60649 0.66220 -0.12525 0.13315  -0.05532 124 ILE A CD1 
637  N N   . SER A 125 ? 0.70715 0.63380 0.73983 -0.15204 0.17972  -0.08813 125 SER A N   
638  C CA  . SER A 125 ? 0.73251 0.64573 0.76063 -0.16410 0.19502  -0.09537 125 SER A CA  
639  C C   . SER A 125 ? 0.69347 0.58295 0.68153 -0.16025 0.19359  -0.08309 125 SER A C   
640  O O   . SER A 125 ? 0.72343 0.59754 0.68281 -0.15043 0.18517  -0.07079 125 SER A O   
641  C CB  . SER A 125 ? 0.82497 0.71755 0.84721 -0.17293 0.21261  -0.10646 125 SER A CB  
642  O OG  . SER A 125 ? 0.76591 0.68358 0.82668 -0.17144 0.20883  -0.12021 125 SER A OG  
643  N N   . LEU A 126 ? 0.74085 0.56815 0.69180 -0.12654 0.09773  -0.08606 126 LEU A N   
644  C CA  . LEU A 126 ? 0.71733 0.52613 0.63327 -0.12717 0.10211  -0.08026 126 LEU A CA  
645  C C   . LEU A 126 ? 0.67671 0.46587 0.56856 -0.13786 0.11955  -0.07737 126 LEU A C   
646  O O   . LEU A 126 ? 0.64847 0.44360 0.55555 -0.14674 0.13603  -0.08485 126 LEU A O   
647  C CB  . LEU A 126 ? 0.75092 0.56753 0.67442 -0.12370 0.10458  -0.08893 126 LEU A CB  
648  C CG  . LEU A 126 ? 0.73460 0.53755 0.63003 -0.11952 0.09908  -0.08531 126 LEU A CG  
649  C CD1 . LEU A 126 ? 0.68368 0.47785 0.55914 -0.11497 0.08162  -0.07221 126 LEU A CD1 
650  C CD2 . LEU A 126 ? 0.87927 0.69566 0.79757 -0.11294 0.09404  -0.09593 126 LEU A CD2 
651  N N   . LEU A 127 ? 0.65792 0.42404 0.51250 -0.13724 0.11556  -0.06607 127 LEU A N   
652  C CA  . LEU A 127 ? 0.68505 0.42633 0.50810 -0.14663 0.12989  -0.06083 127 LEU A CA  
653  C C   . LEU A 127 ? 0.68304 0.41125 0.47600 -0.14768 0.13846  -0.06099 127 LEU A C   
654  O O   . LEU A 127 ? 0.68756 0.40555 0.46631 -0.15734 0.15782  -0.06274 127 LEU A O   
655  C CB  . LEU A 127 ? 0.68751 0.40785 0.48512 -0.14399 0.11902  -0.04863 127 LEU A CB  
656  C CG  . LEU A 127 ? 0.66879 0.38948 0.48330 -0.14664 0.11659  -0.04834 127 LEU A CG  
657  C CD1 . LEU A 127 ? 0.68724 0.38065 0.46947 -0.14373 0.10840  -0.03704 127 LEU A CD1 
658  C CD2 . LEU A 127 ? 0.67517 0.39825 0.50726 -0.16089 0.13543  -0.05521 127 LEU A CD2 
659  N N   . ASN A 128 ? 0.63422 0.36233 0.41647 -0.13855 0.12454  -0.05928 128 ASN A N   
660  C CA  . ASN A 128 ? 0.66743 0.38134 0.41929 -0.13827 0.12947  -0.06065 128 ASN A CA  
661  C C   . ASN A 128 ? 0.71262 0.43369 0.46827 -0.12857 0.11067  -0.06137 128 ASN A C   
662  O O   . ASN A 128 ? 0.66583 0.39356 0.43011 -0.12299 0.09303  -0.05437 128 ASN A O   
663  C CB  . ASN A 128 ? 0.70255 0.38505 0.40697 -0.14184 0.13182  -0.04959 128 ASN A CB  
664  C CG  . ASN A 128 ? 0.75472 0.42031 0.42369 -0.14270 0.13971  -0.05220 128 ASN A CG  
665  O OD1 . ASN A 128 ? 0.77648 0.45312 0.45629 -0.14278 0.15007  -0.06383 128 ASN A OD1 
666  N ND2 . ASN A 128 ? 0.79152 0.42956 0.41678 -0.14211 0.13398  -0.04217 128 ASN A ND2 
667  N N   . VAL A 129 ? 0.71958 0.43909 0.46860 -0.12690 0.11486  -0.07002 129 VAL A N   
668  C CA  . VAL A 129 ? 0.68995 0.40963 0.43674 -0.11960 0.09715  -0.07083 129 VAL A CA  
669  C C   . VAL A 129 ? 0.69778 0.39276 0.40119 -0.11991 0.09935  -0.07104 129 VAL A C   
670  O O   . VAL A 129 ? 0.68535 0.37034 0.36992 -0.12418 0.11870  -0.07682 129 VAL A O   
671  C CB  . VAL A 129 ? 0.65621 0.39519 0.43786 -0.11509 0.09566  -0.08328 129 VAL A CB  
672  C CG1 . VAL A 129 ? 0.64745 0.38526 0.42999 -0.10903 0.07364  -0.08104 129 VAL A CG1 
673  C CG2 . VAL A 129 ? 0.63067 0.39270 0.45253 -0.11552 0.09740  -0.08530 129 VAL A CG2 
674  N N   . PHE A 130 ? 0.66888 0.35481 0.35628 -0.11579 0.07959  -0.06480 130 PHE A N   
675  C CA  . PHE A 130 ? 0.71663 0.37793 0.36177 -0.11526 0.07761  -0.06554 130 PHE A CA  
676  C C   . PHE A 130 ? 0.69313 0.35285 0.33688 -0.11093 0.05237  -0.06159 130 PHE A C   
677  O O   . PHE A 130 ? 0.70689 0.38264 0.37532 -0.10950 0.03764  -0.05390 130 PHE A O   
678  C CB  . PHE A 130 ? 0.71580 0.35505 0.32197 -0.11917 0.08430  -0.05589 130 PHE A CB  
679  C CG  . PHE A 130 ? 0.68379 0.32525 0.29342 -0.11774 0.07015  -0.04214 130 PHE A CG  
680  C CD1 . PHE A 130 ? 0.68124 0.31453 0.27326 -0.11344 0.04926  -0.03413 130 PHE A CD1 
681  C CD2 . PHE A 130 ? 0.69186 0.34426 0.32309 -0.12010 0.07725  -0.03821 130 PHE A CD2 
682  C CE1 . PHE A 130 ? 0.66485 0.30331 0.26197 -0.11034 0.03700  -0.02272 130 PHE A CE1 
683  C CE2 . PHE A 130 ? 0.67241 0.32643 0.30561 -0.11672 0.06441  -0.02721 130 PHE A CE2 
684  C CZ  . PHE A 130 ? 0.64009 0.28830 0.25672 -0.11123 0.04493  -0.01957 130 PHE A CZ  
685  N N   . THR A 131 ? 0.73267 0.37299 0.34660 -0.10939 0.04788  -0.06718 131 THR A N   
686  C CA  . THR A 131 ? 0.74458 0.37766 0.34924 -0.10734 0.02352  -0.06313 131 THR A CA  
687  C C   . THR A 131 ? 0.80549 0.41029 0.35976 -0.10739 0.02095  -0.06096 131 THR A C   
688  O O   . THR A 131 ? 0.82133 0.40897 0.34599 -0.10766 0.03756  -0.06897 131 THR A O   
689  C CB  . THR A 131 ? 0.75215 0.38685 0.37242 -0.10468 0.01487  -0.07439 131 THR A CB  
690  O OG1 . THR A 131 ? 0.70828 0.32950 0.31160 -0.10465 -0.00797 -0.07148 131 THR A OG1 
691  C CG2 . THR A 131 ? 0.78286 0.40716 0.38942 -0.10211 0.03393  -0.09068 131 THR A CG2 
692  N N   . PRO A 132 ? 0.83817 0.43854 0.38123 -0.10685 0.00064  -0.05019 132 PRO A N   
693  C CA  . PRO A 132 ? 0.92473 0.49669 0.41827 -0.10589 -0.00524 -0.04820 132 PRO A CA  
694  C C   . PRO A 132 ? 0.98981 0.54254 0.45917 -0.10433 -0.01203 -0.06022 132 PRO A C   
695  O O   . PRO A 132 ? 1.00623 0.53214 0.42874 -0.10308 -0.01302 -0.06158 132 PRO A O   
696  C CB  . PRO A 132 ? 0.91991 0.49934 0.41908 -0.10461 -0.02834 -0.03476 132 PRO A CB  
697  C CG  . PRO A 132 ? 0.82574 0.43744 0.37396 -0.10512 -0.02916 -0.02894 132 PRO A CG  
698  C CD  . PRO A 132 ? 0.83116 0.45388 0.40637 -0.10669 -0.01770 -0.03958 132 PRO A CD  
699  N N   . GLN A 133 ? 0.88570 0.44871 0.38298 -0.10378 -0.01762 -0.06917 133 GLN A N   
700  C CA  . GLN A 133 ? 0.93283 0.47591 0.40924 -0.10131 -0.02611 -0.08216 133 GLN A CA  
701  C C   . GLN A 133 ? 0.97768 0.51157 0.43827 -0.09800 -0.00077 -0.09744 133 GLN A C   
702  O O   . GLN A 133 ? 0.93793 0.48944 0.42271 -0.09856 0.02021  -0.09958 133 GLN A O   
703  C CB  . GLN A 133 ? 0.88877 0.44390 0.40183 -0.10229 -0.04584 -0.08408 133 GLN A CB  
704  C CG  . GLN A 133 ? 0.86014 0.42744 0.39003 -0.10674 -0.07045 -0.06921 133 GLN A CG  
705  C CD  . GLN A 133 ? 0.81691 0.41521 0.38525 -0.10868 -0.06534 -0.05669 133 GLN A CD  
706  O OE1 . GLN A 133 ? 0.78066 0.39470 0.37826 -0.10811 -0.05284 -0.05984 133 GLN A OE1 
707  N NE2 . GLN A 133 ? 0.78593 0.39325 0.35406 -0.10986 -0.07596 -0.04328 133 GLN A NE2 
708  N N   . LYS A 134 ? 1.14543 0.65272 0.56558 -0.09428 -0.00313 -0.10881 134 LYS A N   
709  C CA  . LYS A 134 ? 1.13909 0.63565 0.53315 -0.09049 0.02282  -0.12286 134 LYS A CA  
710  C C   . LYS A 134 ? 1.07728 0.57975 0.49355 -0.08379 0.02621  -0.14076 134 LYS A C   
711  O O   . LYS A 134 ? 1.04634 0.55778 0.46750 -0.08086 0.05205  -0.15132 134 LYS A O   
712  C CB  . LYS A 134 ? 1.13291 0.60709 0.47877 -0.08680 0.02081  -0.12103 134 LYS A CB  
713  C CG  . LYS A 134 ? 1.19683 0.66231 0.51641 -0.09140 0.02188  -0.10412 134 LYS A CG  
714  C CD  . LYS A 134 ? 1.21148 0.67006 0.52700 -0.09189 -0.01035 -0.09327 134 LYS A CD  
715  C CE  . LYS A 134 ? 1.23100 0.68186 0.52429 -0.09414 -0.01080 -0.07691 134 LYS A CE  
716  N NZ  . LYS A 134 ? 1.20071 0.66742 0.51714 -0.09974 -0.00021 -0.06887 134 LYS A NZ  
717  N N   . THR A 135 ? 1.03346 0.53237 0.46532 -0.08110 0.00075  -0.14415 135 THR A N   
718  C CA  . THR A 135 ? 1.02657 0.52777 0.47856 -0.07301 0.00028  -0.16083 135 THR A CA  
719  C C   . THR A 135 ? 0.96642 0.47989 0.46387 -0.07604 -0.01711 -0.15770 135 THR A C   
720  O O   . THR A 135 ? 1.00353 0.52858 0.51975 -0.08396 -0.02944 -0.14133 135 THR A O   
721  C CB  . THR A 135 ? 1.05742 0.53863 0.48326 -0.06563 -0.01461 -0.16946 135 THR A CB  
722  O OG1 . THR A 135 ? 1.05973 0.53344 0.48949 -0.07075 -0.04597 -0.15863 135 THR A OG1 
723  C CG2 . THR A 135 ? 1.04348 0.51174 0.42182 -0.06283 0.00093  -0.17054 135 THR A CG2 
724  N N   . LEU A 136 ? 0.95115 0.46687 0.47079 -0.06809 -0.01787 -0.17199 136 LEU A N   
725  C CA  . LEU A 136 ? 0.90802 0.43343 0.47013 -0.06998 -0.03482 -0.16864 136 LEU A CA  
726  C C   . LEU A 136 ? 0.94724 0.46426 0.51250 -0.07540 -0.06643 -0.15727 136 LEU A C   
727  O O   . LEU A 136 ? 0.90003 0.42885 0.49478 -0.08296 -0.08077 -0.14419 136 LEU A O   
728  C CB  . LEU A 136 ? 0.87816 0.40517 0.46055 -0.05831 -0.02919 -0.18736 136 LEU A CB  
729  C CG  . LEU A 136 ? 0.84563 0.37651 0.46755 -0.05756 -0.05018 -0.18540 136 LEU A CG  
730  C CD1 . LEU A 136 ? 0.83355 0.39011 0.49252 -0.06374 -0.04572 -0.17283 136 LEU A CD1 
731  C CD2 . LEU A 136 ? 0.88113 0.40687 0.51365 -0.04314 -0.04769 -0.20625 136 LEU A CD2 
732  N N   . GLU A 137 ? 0.93637 0.43479 0.47247 -0.07214 -0.07697 -0.16166 137 GLU A N   
733  C CA  . GLU A 137 ? 0.96800 0.45929 0.50861 -0.07811 -0.10641 -0.15156 137 GLU A CA  
734  C C   . GLU A 137 ? 0.96951 0.47002 0.50910 -0.08950 -0.11538 -0.13207 137 GLU A C   
735  O O   . GLU A 137 ? 0.97593 0.48600 0.54132 -0.09771 -0.13514 -0.11921 137 GLU A O   
736  C CB  . GLU A 137 ? 1.05519 0.52359 0.56299 -0.07167 -0.11484 -0.16202 137 GLU A CB  
737  C CG  . GLU A 137 ? 1.02625 0.48453 0.54449 -0.06222 -0.11986 -0.17822 137 GLU A CG  
738  C CD  . GLU A 137 ? 1.09465 0.55406 0.60423 -0.04972 -0.09340 -0.19767 137 GLU A CD  
739  O OE1 . GLU A 137 ? 1.09956 0.56728 0.59369 -0.04975 -0.07010 -0.19742 137 GLU A OE1 
740  O OE2 . GLU A 137 ? 1.22294 0.67568 0.74196 -0.03998 -0.09546 -0.21302 137 GLU A OE2 
741  N N   . GLU A 138 ? 1.03191 0.53060 0.54229 -0.08996 -0.10075 -0.12924 138 GLU A N   
742  C CA  . GLU A 138 ? 0.95592 0.46284 0.46362 -0.09869 -0.10898 -0.11221 138 GLU A CA  
743  C C   . GLU A 138 ? 0.91710 0.44891 0.45685 -0.10388 -0.09921 -0.10229 138 GLU A C   
744  O O   . GLU A 138 ? 0.90173 0.44980 0.45200 -0.10926 -0.10673 -0.08637 138 GLU A O   
745  C CB  . GLU A 138 ? 1.00273 0.49598 0.46507 -0.09591 -0.09860 -0.11161 138 GLU A CB  
746  C CG  . GLU A 138 ? 1.08168 0.55247 0.51006 -0.08805 -0.10058 -0.12323 138 GLU A CG  
747  C CD  . GLU A 138 ? 1.25121 0.71040 0.63685 -0.08354 -0.07904 -0.12549 138 GLU A CD  
748  O OE1 . GLU A 138 ? 1.29901 0.75009 0.65928 -0.08533 -0.08682 -0.11521 138 GLU A OE1 
749  O OE2 . GLU A 138 ? 1.29384 0.75319 0.67282 -0.07818 -0.05428 -0.13695 138 GLU A OE2 
750  N N   . PHE A 139 ? 0.88132 0.42501 0.44514 -0.09962 -0.08190 -0.10947 139 PHE A N   
751  C CA  . PHE A 139 ? 0.83613 0.41068 0.43630 -0.10141 -0.06923 -0.09927 139 PHE A CA  
752  C C   . PHE A 139 ? 0.80581 0.39931 0.43667 -0.10889 -0.08871 -0.08253 139 PHE A C   
753  O O   . PHE A 139 ? 0.85377 0.44248 0.49844 -0.11254 -0.10854 -0.08186 139 PHE A O   
754  C CB  . PHE A 139 ? 0.82336 0.40586 0.44850 -0.09546 -0.05518 -0.11148 139 PHE A CB  
755  C CG  . PHE A 139 ? 0.78119 0.39385 0.44387 -0.09679 -0.04413 -0.10294 139 PHE A CG  
756  C CD1 . PHE A 139 ? 0.76396 0.38871 0.46293 -0.09499 -0.04905 -0.10485 139 PHE A CD1 
757  C CD2 . PHE A 139 ? 0.74203 0.36819 0.40167 -0.09931 -0.03013 -0.09342 139 PHE A CD2 
758  C CE1 . PHE A 139 ? 0.71453 0.36570 0.44549 -0.09562 -0.04032 -0.09781 139 PHE A CE1 
759  C CE2 . PHE A 139 ? 0.70694 0.35873 0.39953 -0.10012 -0.02142 -0.08695 139 PHE A CE2 
760  C CZ  . PHE A 139 ? 0.71377 0.37876 0.44173 -0.09821 -0.02649 -0.08941 139 PHE A CZ  
761  N N   . GLN A 140 ? 0.73236 0.34702 0.37324 -0.11126 -0.08260 -0.06897 140 GLN A N   
762  C CA  . GLN A 140 ? 0.71061 0.34716 0.37858 -0.11747 -0.09831 -0.05284 140 GLN A CA  
763  C C   . GLN A 140 ? 0.69637 0.36141 0.39413 -0.11652 -0.08516 -0.04475 140 GLN A C   
764  O O   . GLN A 140 ? 0.66186 0.34200 0.39080 -0.11829 -0.08920 -0.04139 140 GLN A O   
765  C CB  . GLN A 140 ? 0.73012 0.36402 0.37768 -0.12028 -0.11110 -0.04353 140 GLN A CB  
766  C CG  . GLN A 140 ? 0.84964 0.46403 0.48217 -0.12472 -0.13476 -0.04639 140 GLN A CG  
767  C CD  . GLN A 140 ? 0.91942 0.55376 0.58288 -0.13378 -0.15611 -0.03306 140 GLN A CD  
768  O OE1 . GLN A 140 ? 0.91807 0.54364 0.59186 -0.13970 -0.17178 -0.03526 140 GLN A OE1 
769  N NE2 . GLN A 140 ? 0.90868 0.56991 0.58713 -0.13499 -0.15662 -0.01915 140 GLN A NE2 
770  N N   . ASP A 141 ? 0.68828 0.35836 0.37474 -0.11371 -0.07045 -0.04155 141 ASP A N   
771  C CA  . ASP A 141 ? 0.63570 0.33116 0.34698 -0.11279 -0.06149 -0.03299 141 ASP A CA  
772  C C   . ASP A 141 ? 0.62741 0.32179 0.33766 -0.10913 -0.03780 -0.04141 141 ASP A C   
773  O O   . ASP A 141 ? 0.66730 0.34246 0.35109 -0.10764 -0.02580 -0.05077 141 ASP A O   
774  C CB  . ASP A 141 ? 0.63589 0.34031 0.33946 -0.11274 -0.06757 -0.02032 141 ASP A CB  
775  C CG  . ASP A 141 ? 0.64979 0.35342 0.34923 -0.11678 -0.09037 -0.01370 141 ASP A CG  
776  O OD1 . ASP A 141 ? 0.61677 0.32965 0.33860 -0.12187 -0.10322 -0.01098 141 ASP A OD1 
777  O OD2 . ASP A 141 ? 0.67746 0.37048 0.35129 -0.11535 -0.09629 -0.01094 141 ASP A OD2 
778  N N   . VAL A 142 ? 0.58445 0.30049 0.32376 -0.10821 -0.03118 -0.03796 142 VAL A N   
779  C CA  . VAL A 142 ? 0.56606 0.28601 0.31181 -0.10622 -0.01044 -0.04468 142 VAL A CA  
780  C C   . VAL A 142 ? 0.59878 0.33133 0.34911 -0.10572 -0.00666 -0.03456 142 VAL A C   
781  O O   . VAL A 142 ? 0.56494 0.31556 0.33354 -0.10505 -0.01774 -0.02506 142 VAL A O   
782  C CB  . VAL A 142 ? 0.55531 0.28786 0.33313 -0.10438 -0.00755 -0.05259 142 VAL A CB  
783  C CG1 . VAL A 142 ? 0.53410 0.27597 0.32458 -0.10329 0.01202  -0.05849 142 VAL A CG1 
784  C CG2 . VAL A 142 ? 0.60486 0.32195 0.37665 -0.10273 -0.01063 -0.06473 142 VAL A CG2 
785  N N   . TYR A 143 ? 0.57643 0.29868 0.30922 -0.10607 0.00908  -0.03661 143 TYR A N   
786  C CA  . TYR A 143 ? 0.56308 0.29156 0.29720 -0.10503 0.01305  -0.02870 143 TYR A CA  
787  C C   . TYR A 143 ? 0.55979 0.29593 0.31290 -0.10639 0.02982  -0.03543 143 TYR A C   
788  O O   . TYR A 143 ? 0.62099 0.34722 0.36636 -0.10956 0.04551  -0.04437 143 TYR A O   
789  C CB  . TYR A 143 ? 0.56248 0.26864 0.25857 -0.10521 0.01497  -0.02357 143 TYR A CB  
790  C CG  . TYR A 143 ? 0.57319 0.27438 0.25274 -0.10315 -0.00401 -0.01625 143 TYR A CG  
791  C CD1 . TYR A 143 ? 0.60708 0.29437 0.26927 -0.10485 -0.01086 -0.02105 143 TYR A CD1 
792  C CD2 . TYR A 143 ? 0.58280 0.29392 0.26499 -0.09896 -0.01575 -0.00552 143 TYR A CD2 
793  C CE1 . TYR A 143 ? 0.60583 0.28924 0.25500 -0.10395 -0.02994 -0.01486 143 TYR A CE1 
794  C CE2 . TYR A 143 ? 0.63743 0.34789 0.30878 -0.09729 -0.03369 0.00073  143 TYR A CE2 
795  C CZ  . TYR A 143 ? 0.63721 0.33373 0.29261 -0.10056 -0.04122 -0.00372 143 TYR A CZ  
796  O OH  . TYR A 143 ? 0.67415 0.37056 0.32071 -0.09986 -0.06076 0.00201  143 TYR A OH  
797  N N   . LEU A 144 ? 0.53588 0.29086 0.31410 -0.10408 0.02649  -0.03158 144 LEU A N   
798  C CA  . LEU A 144 ? 0.52822 0.29185 0.32705 -0.10542 0.03901  -0.03765 144 LEU A CA  
799  C C   . LEU A 144 ? 0.56809 0.32532 0.35624 -0.10529 0.04282  -0.03145 144 LEU A C   
800  O O   . LEU A 144 ? 0.56024 0.32216 0.34513 -0.10023 0.03117  -0.02258 144 LEU A O   
801  C CB  . LEU A 144 ? 0.52167 0.30870 0.35533 -0.10217 0.03102  -0.03940 144 LEU A CB  
802  C CG  . LEU A 144 ? 0.51087 0.30252 0.35611 -0.10121 0.02252  -0.04348 144 LEU A CG  
803  C CD1 . LEU A 144 ? 0.51611 0.32816 0.38951 -0.09782 0.01155  -0.04064 144 LEU A CD1 
804  C CD2 . LEU A 144 ? 0.53301 0.31827 0.38177 -0.10285 0.03535  -0.05720 144 LEU A CD2 
805  N N   . VAL A 145 ? 0.58072 0.32739 0.36408 -0.11086 0.05907  -0.03628 145 VAL A N   
806  C CA  . VAL A 145 ? 0.57769 0.31191 0.34847 -0.11215 0.06321  -0.03101 145 VAL A CA  
807  C C   . VAL A 145 ? 0.61351 0.36100 0.41417 -0.11448 0.06942  -0.03712 145 VAL A C   
808  O O   . VAL A 145 ? 0.65538 0.41056 0.47450 -0.12004 0.08102  -0.04658 145 VAL A O   
809  C CB  . VAL A 145 ? 0.65808 0.36412 0.39392 -0.11903 0.07636  -0.02947 145 VAL A CB  
810  C CG1 . VAL A 145 ? 0.63258 0.32136 0.35458 -0.12084 0.07909  -0.02322 145 VAL A CG1 
811  C CG2 . VAL A 145 ? 0.62835 0.32027 0.33292 -0.11593 0.06793  -0.02439 145 VAL A CG2 
812  N N   . MET A 146 ? 0.59105 0.34205 0.39706 -0.10944 0.06104  -0.03269 146 MET A N   
813  C CA  . MET A 146 ? 0.62831 0.38837 0.45899 -0.11125 0.06435  -0.03852 146 MET A CA  
814  C C   . MET A 146 ? 0.65146 0.39391 0.46603 -0.10966 0.06207  -0.03320 146 MET A C   
815  O O   . MET A 146 ? 0.62913 0.35716 0.41728 -0.10430 0.05533  -0.02474 146 MET A O   
816  C CB  . MET A 146 ? 0.64977 0.43697 0.51030 -0.10411 0.05296  -0.04161 146 MET A CB  
817  C CG  . MET A 146 ? 0.67464 0.46813 0.53392 -0.09439 0.03985  -0.03567 146 MET A CG  
818  S SD  . MET A 146 ? 0.68938 0.51053 0.58196 -0.08852 0.03078  -0.04104 146 MET A SD  
819  C CE  . MET A 146 ? 0.67795 0.49023 0.58046 -0.09296 0.03708  -0.04938 146 MET A CE  
820  N N   . GLU A 147 ? 0.71191 0.45476 0.54339 -0.11407 0.06660  -0.03897 147 GLU A N   
821  C CA  . GLU A 147 ? 0.70827 0.43168 0.52659 -0.11275 0.06344  -0.03574 147 GLU A CA  
822  C C   . GLU A 147 ? 0.69046 0.42222 0.50539 -0.09743 0.04667  -0.03133 147 GLU A C   
823  O O   . GLU A 147 ? 0.71308 0.47059 0.54953 -0.09053 0.03878  -0.03427 147 GLU A O   
824  C CB  . GLU A 147 ? 0.70525 0.43087 0.54785 -0.12092 0.06922  -0.04443 147 GLU A CB  
825  C CG  . GLU A 147 ? 0.81857 0.57571 0.69933 -0.11903 0.06590  -0.05405 147 GLU A CG  
826  C CD  . GLU A 147 ? 0.86241 0.63426 0.75964 -0.12604 0.07691  -0.05971 147 GLU A CD  
827  O OE1 . GLU A 147 ? 0.86026 0.62398 0.73766 -0.12787 0.08321  -0.05540 147 GLU A OE1 
828  O OE2 . GLU A 147 ? 0.91658 0.70802 0.84647 -0.12857 0.07822  -0.06939 147 GLU A OE2 
829  N N   . LEU A 148 ? 0.66034 0.37047 0.44750 -0.09167 0.04141  -0.02414 148 LEU A N   
830  C CA  . LEU A 148 ? 0.64802 0.36840 0.43123 -0.07581 0.02675  -0.02008 148 LEU A CA  
831  C C   . LEU A 148 ? 0.62321 0.35123 0.42216 -0.06904 0.02066  -0.02642 148 LEU A C   
832  O O   . LEU A 148 ? 0.64899 0.35751 0.44700 -0.07454 0.02411  -0.03095 148 LEU A O   
833  C CB  . LEU A 148 ? 0.65107 0.34557 0.40102 -0.06983 0.02178  -0.01186 148 LEU A CB  
834  C CG  . LEU A 148 ? 0.66488 0.37221 0.41178 -0.05192 0.00715  -0.00823 148 LEU A CG  
835  C CD1 . LEU A 148 ? 0.66073 0.40001 0.42008 -0.04796 0.00189  -0.00463 148 LEU A CD1 
836  C CD2 . LEU A 148 ? 0.68765 0.36533 0.40279 -0.04478 0.00112  -0.00189 148 LEU A CD2 
837  N N   . MET A 149 ? 0.60644 0.36231 0.41876 -0.05763 0.01136  -0.02659 149 MET A N   
838  C CA  . MET A 149 ? 0.60444 0.36952 0.42723 -0.04816 0.00411  -0.03254 149 MET A CA  
839  C C   . MET A 149 ? 0.63358 0.39820 0.43958 -0.03135 -0.00577 -0.02827 149 MET A C   
840  O O   . MET A 149 ? 0.68686 0.44231 0.47460 -0.02793 -0.00756 -0.02083 149 MET A O   
841  C CB  . MET A 149 ? 0.56070 0.35775 0.40918 -0.04728 0.00175  -0.03608 149 MET A CB  
842  C CG  . MET A 149 ? 0.51666 0.31677 0.38423 -0.06138 0.01021  -0.04127 149 MET A CG  
843  S SD  . MET A 149 ? 0.56508 0.34726 0.44376 -0.07132 0.01565  -0.05225 149 MET A SD  
844  C CE  . MET A 149 ? 0.56808 0.37823 0.47592 -0.06652 0.00740  -0.06099 149 MET A CE  
845  N N   . ASP A 150 ? 0.64705 0.42257 0.45913 -0.01965 -0.01277 -0.03377 150 ASP A N   
846  C CA  . ASP A 150 ? 0.62498 0.40006 0.42230 -0.00164 -0.02143 -0.03245 150 ASP A CA  
847  C C   . ASP A 150 ? 0.64546 0.45942 0.45238 0.01098  -0.02639 -0.02926 150 ASP A C   
848  O O   . ASP A 150 ? 0.64083 0.46233 0.43805 0.02427  -0.03152 -0.02494 150 ASP A O   
849  C CB  . ASP A 150 ? 0.68815 0.44171 0.47932 0.00472  -0.02605 -0.04212 150 ASP A CB  
850  C CG  . ASP A 150 ? 0.68723 0.39863 0.46496 -0.00722 -0.02215 -0.04317 150 ASP A CG  
851  O OD1 . ASP A 150 ? 0.66760 0.35906 0.42596 -0.00856 -0.02095 -0.03554 150 ASP A OD1 
852  O OD2 . ASP A 150 ? 0.70299 0.40108 0.48924 -0.01594 -0.02065 -0.05120 150 ASP A OD2 
853  N N   . ALA A 151 ? 0.64474 0.48388 0.47050 0.00718  -0.02512 -0.03084 151 ALA A N   
854  C CA  . ALA A 151 ? 0.61546 0.49089 0.44874 0.01749  -0.02875 -0.02652 151 ALA A CA  
855  C C   . ALA A 151 ? 0.59621 0.49151 0.44806 0.00749  -0.02665 -0.02514 151 ALA A C   
856  O O   . ALA A 151 ? 0.64757 0.53048 0.50838 -0.00402 -0.02352 -0.03039 151 ALA A O   
857  C CB  . ALA A 151 ? 0.68102 0.56249 0.50771 0.03524  -0.03411 -0.03345 151 ALA A CB  
858  N N   . ASN A 152 ? 0.59243 0.51922 0.45061 0.01209  -0.02864 -0.01772 152 ASN A N   
859  C CA  . ASN A 152 ? 0.54816 0.49406 0.42085 0.00539  -0.02893 -0.01504 152 ASN A CA  
860  C C   . ASN A 152 ? 0.55896 0.51437 0.43161 0.01487  -0.03236 -0.02177 152 ASN A C   
861  O O   . ASN A 152 ? 0.54218 0.49720 0.40356 0.02866  -0.03442 -0.02685 152 ASN A O   
862  C CB  . ASN A 152 ? 0.54478 0.51792 0.42265 0.00381  -0.02973 -0.00218 152 ASN A CB  
863  C CG  . ASN A 152 ? 0.60640 0.58518 0.49743 -0.00924 -0.03011 0.00246  152 ASN A CG  
864  O OD1 . ASN A 152 ? 0.67147 0.63562 0.56908 -0.01603 -0.02943 -0.00453 152 ASN A OD1 
865  N ND2 . ASN A 152 ? 0.60040 0.60057 0.49658 -0.01278 -0.03186 0.01410  152 ASN A ND2 
866  N N   . LEU A 153 ? 0.51551 0.47807 0.39941 0.00843  -0.03408 -0.02244 153 LEU A N   
867  C CA  . LEU A 153 ? 0.47862 0.45004 0.36014 0.01730  -0.03882 -0.02832 153 LEU A CA  
868  C C   . LEU A 153 ? 0.46034 0.46093 0.33328 0.02880  -0.03913 -0.02038 153 LEU A C   
869  O O   . LEU A 153 ? 0.45870 0.46564 0.32202 0.04071  -0.04210 -0.02628 153 LEU A O   
870  C CB  . LEU A 153 ? 0.43914 0.41045 0.33436 0.00829  -0.04227 -0.03041 153 LEU A CB  
871  C CG  . LEU A 153 ? 0.41608 0.38511 0.30949 0.01536  -0.04919 -0.04112 153 LEU A CG  
872  C CD1 . LEU A 153 ? 0.39356 0.33785 0.28571 0.01650  -0.04999 -0.05491 153 LEU A CD1 
873  C CD2 . LEU A 153 ? 0.41120 0.38311 0.31899 0.00775  -0.05438 -0.04153 153 LEU A CD2 
874  N N   . CYS A 154 ? 0.46987 0.48913 0.34612 0.02521  -0.03602 -0.00751 154 CYS A N   
875  C CA  . CYS A 154 ? 0.42661 0.47760 0.29737 0.03523  -0.03429 0.00060  154 CYS A CA  
876  C C   . CYS A 154 ? 0.48241 0.53419 0.34093 0.05261  -0.03331 -0.00662 154 CYS A C   
877  O O   . CYS A 154 ? 0.46981 0.54223 0.31957 0.06638  -0.03234 -0.00779 154 CYS A O   
878  C CB  . CYS A 154 ? 0.43058 0.50088 0.31121 0.02557  -0.03203 0.01560  154 CYS A CB  
879  S SG  . CYS A 154 ? 0.46627 0.52870 0.36015 0.00551  -0.03486 0.02325  154 CYS A SG  
880  N N   . GLN A 155 ? 0.49027 0.51845 0.34619 0.05296  -0.03370 -0.01166 155 GLN A N   
881  C CA  . GLN A 155 ? 0.49570 0.51837 0.33877 0.07043  -0.03484 -0.01935 155 GLN A CA  
882  C C   . GLN A 155 ? 0.50323 0.50783 0.33489 0.08018  -0.03878 -0.03381 155 GLN A C   
883  O O   . GLN A 155 ? 0.54386 0.55217 0.36300 0.09853  -0.04041 -0.04086 155 GLN A O   
884  C CB  . GLN A 155 ? 0.48798 0.48478 0.32804 0.06727  -0.03567 -0.01979 155 GLN A CB  
885  C CG  . GLN A 155 ? 0.53312 0.54181 0.38278 0.05656  -0.03392 -0.00717 155 GLN A CG  
886  C CD  . GLN A 155 ? 0.66043 0.63488 0.50513 0.04694  -0.03447 -0.00809 155 GLN A CD  
887  O OE1 . GLN A 155 ? 0.59579 0.56027 0.44715 0.03075  -0.03241 -0.00496 155 GLN A OE1 
888  N NE2 . GLN A 155 ? 0.67027 0.62530 0.50132 0.05764  -0.03732 -0.01256 155 GLN A NE2 
889  N N   . VAL A 156 ? 0.52865 0.51398 0.36523 0.06889  -0.04119 -0.03934 156 VAL A N   
890  C CA  . VAL A 156 ? 0.51973 0.48691 0.34759 0.07625  -0.04695 -0.05374 156 VAL A CA  
891  C C   . VAL A 156 ? 0.51582 0.50774 0.33703 0.08634  -0.04888 -0.05468 156 VAL A C   
892  O O   . VAL A 156 ? 0.54727 0.53406 0.35369 0.10139  -0.05340 -0.06598 156 VAL A O   
893  C CB  . VAL A 156 ? 0.52371 0.46408 0.36298 0.05982  -0.04907 -0.05969 156 VAL A CB  
894  C CG1 . VAL A 156 ? 0.57557 0.50150 0.41003 0.06522  -0.05693 -0.07422 156 VAL A CG1 
895  C CG2 . VAL A 156 ? 0.58191 0.49465 0.42143 0.05170  -0.04615 -0.05988 156 VAL A CG2 
896  N N   . ILE A 157 ? 0.49592 0.51289 0.32542 0.07838  -0.04595 -0.04273 157 ILE A N   
897  C CA  . ILE A 157 ? 0.47159 0.51184 0.29151 0.08659  -0.04696 -0.04096 157 ILE A CA  
898  C C   . ILE A 157 ? 0.49311 0.55698 0.29843 0.10582  -0.04247 -0.04092 157 ILE A C   
899  O O   . ILE A 157 ? 0.47753 0.54971 0.26620 0.11984  -0.04426 -0.04769 157 ILE A O   
900  C CB  . ILE A 157 ? 0.45571 0.51490 0.28671 0.07248  -0.04484 -0.02571 157 ILE A CB  
901  C CG1 . ILE A 157 ? 0.44517 0.48294 0.28747 0.05927  -0.05148 -0.02998 157 ILE A CG1 
902  C CG2 . ILE A 157 ? 0.48047 0.56972 0.29854 0.08079  -0.04261 -0.01834 157 ILE A CG2 
903  C CD1 . ILE A 157 ? 0.43824 0.48325 0.29535 0.04323  -0.05016 -0.01647 157 ILE A CD1 
904  N N   . GLN A 158 ? 0.49121 0.56660 0.30223 0.10790  -0.03700 -0.03433 158 GLN A N   
905  C CA  . GLN A 158 ? 0.51495 0.61587 0.31626 0.12752  -0.03246 -0.03530 158 GLN A CA  
906  C C   . GLN A 158 ? 0.53937 0.61783 0.32290 0.14703  -0.03794 -0.05354 158 GLN A C   
907  O O   . GLN A 158 ? 0.55340 0.65233 0.32512 0.16718  -0.03503 -0.05810 158 GLN A O   
908  C CB  . GLN A 158 ? 0.50566 0.62167 0.32007 0.12531  -0.02797 -0.02544 158 GLN A CB  
909  C CG  . GLN A 158 ? 0.50547 0.64961 0.33646 0.10863  -0.02282 -0.00717 158 GLN A CG  
910  C CD  . GLN A 158 ? 0.57967 0.73968 0.42392 0.10738  -0.02045 0.00119  158 GLN A CD  
911  O OE1 . GLN A 158 ? 0.60192 0.73580 0.44979 0.10162  -0.02450 -0.00069 158 GLN A OE1 
912  N NE2 . GLN A 158 ? 0.75006 0.95395 0.60148 0.11253  -0.01394 0.01061  158 GLN A NE2 
913  N N   . MET A 159 ? 0.54543 0.58277 0.32723 0.14148  -0.04567 -0.06429 159 MET A N   
914  C CA  . MET A 159 ? 0.57380 0.58332 0.33890 0.15761  -0.05286 -0.08161 159 MET A CA  
915  C C   . MET A 159 ? 0.60152 0.60390 0.35316 0.16337  -0.05941 -0.09329 159 MET A C   
916  O O   . MET A 159 ? 0.55020 0.56096 0.30729 0.15181  -0.05997 -0.08845 159 MET A O   
917  C CB  . MET A 159 ? 0.60747 0.57431 0.37734 0.14693  -0.05792 -0.08632 159 MET A CB  
918  C CG  . MET A 159 ? 0.61110 0.57856 0.38930 0.14232  -0.05353 -0.07603 159 MET A CG  
919  S SD  . MET A 159 ? 0.83962 0.76588 0.62753 0.11844  -0.05497 -0.07428 159 MET A SD  
920  C CE  . MET A 159 ? 0.75385 0.64044 0.53105 0.12079  -0.06451 -0.09268 159 MET A CE  
921  N N   . GLU A 160 ? 0.60334 0.58801 0.33595 0.18238  -0.06597 -0.10942 160 GLU A N   
922  C CA  . GLU A 160 ? 0.61484 0.58557 0.33173 0.18941  -0.07522 -0.12377 160 GLU A CA  
923  C C   . GLU A 160 ? 0.65357 0.57831 0.37610 0.17747  -0.08608 -0.13470 160 GLU A C   
924  O O   . GLU A 160 ? 0.63893 0.53484 0.35830 0.18103  -0.08959 -0.14119 160 GLU A O   
925  C CB  . GLU A 160 ? 0.66880 0.64643 0.35996 0.21798  -0.07680 -0.13660 160 GLU A CB  
926  C CG  . GLU A 160 ? 0.74386 0.75786 0.42050 0.22811  -0.07172 -0.13396 160 GLU A CG  
927  C CD  . GLU A 160 ? 0.81673 0.85237 0.47279 0.25660  -0.06658 -0.14159 160 GLU A CD  
928  O OE1 . GLU A 160 ? 0.83358 0.84747 0.48313 0.27137  -0.07145 -0.15369 160 GLU A OE1 
929  O OE2 . GLU A 160 ? 0.90117 0.97526 0.54697 0.26455  -0.05753 -0.13546 160 GLU A OE2 
930  N N   . LEU A 161 ? 0.67018 0.58842 0.40174 0.16303  -0.09163 -0.13626 161 LEU A N   
931  C CA  . LEU A 161 ? 0.68324 0.56451 0.42664 0.14804  -0.10047 -0.14519 161 LEU A CA  
932  C C   . LEU A 161 ? 0.72176 0.58710 0.45302 0.15503  -0.11465 -0.16238 161 LEU A C   
933  O O   . LEU A 161 ? 0.69434 0.58037 0.41297 0.16454  -0.11709 -0.16363 161 LEU A O   
934  C CB  . LEU A 161 ? 0.67570 0.56269 0.44640 0.12344  -0.09587 -0.13376 161 LEU A CB  
935  C CG  . LEU A 161 ? 0.63311 0.53022 0.41737 0.11262  -0.08375 -0.11778 161 LEU A CG  
936  C CD1 . LEU A 161 ? 0.63199 0.52660 0.44137 0.08949  -0.08151 -0.11171 161 LEU A CD1 
937  C CD2 . LEU A 161 ? 0.67284 0.54468 0.45022 0.11670  -0.08270 -0.12047 161 LEU A CD2 
938  N N   . ASP A 162 ? 0.72509 0.55225 0.45925 0.14943  -0.12455 -0.17525 162 ASP A N   
939  C CA  . ASP A 162 ? 0.74738 0.55527 0.47461 0.15229  -0.14049 -0.19258 162 ASP A CA  
940  C C   . ASP A 162 ? 0.73785 0.55509 0.48903 0.13351  -0.14418 -0.18989 162 ASP A C   
941  O O   . ASP A 162 ? 0.70473 0.54100 0.47649 0.11911  -0.13413 -0.17526 162 ASP A O   
942  C CB  . ASP A 162 ? 0.76173 0.52468 0.48678 0.14996  -0.15025 -0.20617 162 ASP A CB  
943  C CG  . ASP A 162 ? 0.77090 0.51797 0.51725 0.12947  -0.14178 -0.19619 162 ASP A CG  
944  O OD1 . ASP A 162 ? 0.75887 0.49112 0.52798 0.10833  -0.14515 -0.19842 162 ASP A OD1 
945  O OD2 . ASP A 162 ? 0.82593 0.57665 0.56626 0.13466  -0.13168 -0.18621 162 ASP A OD2 
946  N N   . HIS A 163 ? 0.74732 0.55005 0.49607 0.13449  -0.16025 -0.20527 163 HIS A N   
947  C CA  . HIS A 163 ? 0.72563 0.53733 0.49849 0.11888  -0.16640 -0.20479 163 HIS A CA  
948  C C   . HIS A 163 ? 0.70779 0.50448 0.51572 0.09434  -0.16376 -0.20354 163 HIS A C   
949  O O   . HIS A 163 ? 0.68971 0.50134 0.52400 0.07979  -0.16225 -0.19798 163 HIS A O   
950  C CB  . HIS A 163 ? 0.71697 0.51863 0.47679 0.12808  -0.18626 -0.22234 163 HIS A CB  
951  C CG  . HIS A 163 ? 0.75997 0.58462 0.48954 0.14785  -0.18738 -0.22000 163 HIS A CG  
952  N ND1 . HIS A 163 ? 0.70165 0.55702 0.43353 0.14550  -0.18062 -0.20510 163 HIS A ND1 
953  C CD2 . HIS A 163 ? 0.78798 0.61250 0.49020 0.16775  -0.19041 -0.22487 163 HIS A CD2 
954  C CE1 . HIS A 163 ? 0.76323 0.63254 0.46159 0.16446  -0.18261 -0.20580 163 HIS A CE1 
955  N NE2 . HIS A 163 ? 0.80910 0.66192 0.49165 0.17803  -0.18689 -0.21684 163 HIS A NE2 
956  N N   . GLU A 164 ? 0.71480 0.48180 0.52265 0.08980  -0.16289 -0.20845 164 GLU A N   
957  C CA  . GLU A 164 ? 0.71771 0.47030 0.55629 0.06551  -0.15814 -0.20626 164 GLU A CA  
958  C C   . GLU A 164 ? 0.69252 0.46576 0.54587 0.05469  -0.13977 -0.18772 164 GLU A C   
959  O O   . GLU A 164 ? 0.66105 0.44427 0.54382 0.03699  -0.13549 -0.18395 164 GLU A O   
960  C CB  . GLU A 164 ? 0.75063 0.46331 0.57993 0.06345  -0.16125 -0.21365 164 GLU A CB  
961  C CG  . GLU A 164 ? 0.78082 0.47791 0.62494 0.05407  -0.17240 -0.22291 164 GLU A CG  
962  C CD  . GLU A 164 ? 0.81730 0.51137 0.69914 0.02605  -0.16747 -0.22069 164 GLU A CD  
963  O OE1 . GLU A 164 ? 0.88401 0.56659 0.77198 0.01318  -0.15504 -0.21255 164 GLU A OE1 
964  O OE2 . GLU A 164 ? 0.78960 0.49388 0.69451 0.01736  -0.17563 -0.22685 164 GLU A OE2 
965  N N   . ARG A 165 ? 0.70315 0.48384 0.53702 0.06587  -0.12943 -0.17691 165 ARG A N   
966  C CA  . ARG A 165 ? 0.72183 0.51833 0.56731 0.05577  -0.11358 -0.16008 165 ARG A CA  
967  C C   . ARG A 165 ? 0.66950 0.50103 0.52423 0.05539  -0.11027 -0.15073 165 ARG A C   
968  O O   . ARG A 165 ? 0.63053 0.47252 0.50596 0.04084  -0.10165 -0.14145 165 ARG A O   
969  C CB  . ARG A 165 ? 0.74346 0.53591 0.56700 0.06770  -0.10586 -0.15235 165 ARG A CB  
970  C CG  . ARG A 165 ? 0.79945 0.55359 0.61713 0.06277  -0.10637 -0.15645 165 ARG A CG  
971  C CD  . ARG A 165 ? 0.90286 0.65278 0.69755 0.07835  -0.10189 -0.15029 165 ARG A CD  
972  N NE  . ARG A 165 ? 0.97380 0.68126 0.75603 0.07841  -0.10701 -0.15665 165 ARG A NE  
973  C CZ  . ARG A 165 ? 1.00965 0.70147 0.76680 0.09908  -0.11317 -0.16236 165 ARG A CZ  
974  N NH1 . ARG A 165 ? 1.01812 0.73687 0.76102 0.12176  -0.11330 -0.16300 165 ARG A NH1 
975  N NH2 . ARG A 165 ? 1.05287 0.70086 0.79888 0.09708  -0.11918 -0.16749 165 ARG A NH2 
976  N N   . MET A 166 ? 0.71980 0.56798 0.55751 0.07132  -0.11709 -0.15290 166 MET A N   
977  C CA  . MET A 166 ? 0.66905 0.54619 0.51314 0.07013  -0.11585 -0.14344 166 MET A CA  
978  C C   . MET A 166 ? 0.61894 0.49512 0.49113 0.05544  -0.12292 -0.14870 166 MET A C   
979  O O   . MET A 166 ? 0.61855 0.50967 0.50906 0.04515  -0.11731 -0.13900 166 MET A O   
980  C CB  . MET A 166 ? 0.67142 0.56349 0.48823 0.08960  -0.12217 -0.14526 166 MET A CB  
981  C CG  . MET A 166 ? 0.73401 0.63796 0.52710 0.10499  -0.11287 -0.13821 166 MET A CG  
982  S SD  . MET A 166 ? 0.94454 0.87850 0.70950 0.12357  -0.11359 -0.13354 166 MET A SD  
983  C CE  . MET A 166 ? 0.72132 0.66876 0.50364 0.10908  -0.11806 -0.12448 166 MET A CE  
984  N N   . SER A 167 ? 0.62264 0.48136 0.49981 0.05470  -0.13619 -0.16492 167 SER A N   
985  C CA  . SER A 167 ? 0.64217 0.50262 0.55024 0.04133  -0.14405 -0.17168 167 SER A CA  
986  C C   . SER A 167 ? 0.57654 0.43279 0.51484 0.02128  -0.13221 -0.16774 167 SER A C   
987  O O   . SER A 167 ? 0.56573 0.43509 0.53154 0.01086  -0.13188 -0.16667 167 SER A O   
988  C CB  . SER A 167 ? 0.61013 0.45266 0.51820 0.04416  -0.16191 -0.19069 167 SER A CB  
989  O OG  . SER A 167 ? 0.59158 0.41114 0.51699 0.03015  -0.16025 -0.19826 167 SER A OG  
990  N N   . TYR A 168 ? 0.61891 0.45650 0.55115 0.01654  -0.12257 -0.16574 168 TYR A N   
991  C CA  . TYR A 168 ? 0.60919 0.44118 0.56539 -0.00265 -0.11001 -0.16152 168 TYR A CA  
992  C C   . TYR A 168 ? 0.56866 0.42049 0.52909 -0.00585 -0.09689 -0.14623 168 TYR A C   
993  O O   . TYR A 168 ? 0.55862 0.41860 0.54541 -0.01936 -0.09060 -0.14473 168 TYR A O   
994  C CB  . TYR A 168 ? 0.61081 0.41348 0.55404 -0.00639 -0.10450 -0.16227 168 TYR A CB  
995  C CG  . TYR A 168 ? 0.59597 0.38929 0.56085 -0.02752 -0.09169 -0.15882 168 TYR A CG  
996  C CD1 . TYR A 168 ? 0.61132 0.38649 0.56072 -0.03133 -0.07997 -0.14981 168 TYR A CD1 
997  C CD2 . TYR A 168 ? 0.60879 0.41247 0.60903 -0.04302 -0.09121 -0.16469 168 TYR A CD2 
998  C CE1 . TYR A 168 ? 0.60926 0.37505 0.57418 -0.05078 -0.06720 -0.14597 168 TYR A CE1 
999  C CE2 . TYR A 168 ? 0.66921 0.46712 0.68856 -0.06225 -0.07728 -0.16167 168 TYR A CE2 
1000 C CZ  . TYR A 168 ? 0.59982 0.37793 0.59959 -0.06644 -0.06483 -0.15191 168 TYR A CZ  
1001 O OH  . TYR A 168 ? 0.59889 0.37039 0.61357 -0.08571 -0.05000 -0.14827 168 TYR A OH  
1002 N N   . LEU A 169 ? 0.58038 0.44079 0.51605 0.00648  -0.09279 -0.13543 169 LEU A N   
1003 C CA  . LEU A 169 ? 0.56392 0.44245 0.50297 0.00318  -0.08259 -0.12098 169 LEU A CA  
1004 C C   . LEU A 169 ? 0.54711 0.44540 0.50311 0.00151  -0.08854 -0.12022 169 LEU A C   
1005 O O   . LEU A 169 ? 0.54809 0.45433 0.52196 -0.00839 -0.08191 -0.11459 169 LEU A O   
1006 C CB  . LEU A 169 ? 0.56844 0.45572 0.48038 0.01670  -0.07886 -0.11026 169 LEU A CB  
1007 C CG  . LEU A 169 ? 0.58224 0.45149 0.47713 0.02030  -0.07295 -0.10889 169 LEU A CG  
1008 C CD1 . LEU A 169 ? 0.58404 0.46829 0.45566 0.03682  -0.07162 -0.10100 169 LEU A CD1 
1009 C CD2 . LEU A 169 ? 0.58392 0.44351 0.48883 0.00547  -0.06125 -0.10194 169 LEU A CD2 
1010 N N   . LEU A 170 ? 0.54067 0.44509 0.48936 0.01203  -0.10199 -0.12632 170 LEU A N   
1011 C CA  . LEU A 170 ? 0.53737 0.45695 0.49996 0.01164  -0.11044 -0.12589 170 LEU A CA  
1012 C C   . LEU A 170 ? 0.54093 0.45794 0.53893 -0.00088 -0.11373 -0.13682 170 LEU A C   
1013 O O   . LEU A 170 ? 0.53804 0.46721 0.55494 -0.00446 -0.11618 -0.13480 170 LEU A O   
1014 C CB  . LEU A 170 ? 0.54819 0.47232 0.49014 0.02648  -0.12487 -0.13005 170 LEU A CB  
1015 C CG  . LEU A 170 ? 0.54359 0.47829 0.45262 0.03945  -0.12081 -0.11817 170 LEU A CG  
1016 C CD1 . LEU A 170 ? 0.56431 0.49690 0.44809 0.05504  -0.13298 -0.12692 170 LEU A CD1 
1017 C CD2 . LEU A 170 ? 0.48272 0.43519 0.39247 0.03721  -0.11795 -0.10246 170 LEU A CD2 
1018 N N   . TYR A 171 ? 0.54193 0.44355 0.55033 -0.00769 -0.11403 -0.14848 171 TYR A N   
1019 C CA  . TYR A 171 ? 0.56384 0.46683 0.60974 -0.02146 -0.11481 -0.15868 171 TYR A CA  
1020 C C   . TYR A 171 ? 0.57778 0.48493 0.64067 -0.03430 -0.09740 -0.15127 171 TYR A C   
1021 O O   . TYR A 171 ? 0.54472 0.46445 0.63799 -0.04149 -0.09666 -0.15523 171 TYR A O   
1022 C CB  . TYR A 171 ? 0.57658 0.46102 0.62851 -0.02748 -0.11944 -0.17193 171 TYR A CB  
1023 C CG  . TYR A 171 ? 0.61058 0.49714 0.70271 -0.04555 -0.11476 -0.18042 171 TYR A CG  
1024 C CD1 . TYR A 171 ? 0.62604 0.52879 0.75088 -0.04798 -0.12643 -0.19109 171 TYR A CD1 
1025 C CD2 . TYR A 171 ? 0.64331 0.51675 0.74069 -0.06005 -0.09856 -0.17759 171 TYR A CD2 
1026 C CE1 . TYR A 171 ? 0.69068 0.60046 0.85611 -0.06448 -0.12093 -0.19938 171 TYR A CE1 
1027 C CE2 . TYR A 171 ? 0.71245 0.59069 0.84674 -0.07762 -0.09193 -0.18468 171 TYR A CE2 
1028 C CZ  . TYR A 171 ? 0.76092 0.65947 0.93064 -0.07970 -0.10239 -0.19556 171 TYR A CZ  
1029 O OH  . TYR A 171 ? 1.03939 0.94966 1.24310 -0.09478 -0.09209 -0.19750 171 TYR A OH  
1030 N N   . GLN A 172 ? 0.56939 0.46614 0.61237 -0.03615 -0.08392 -0.14131 172 GLN A N   
1031 C CA  . GLN A 172 ? 0.55096 0.44899 0.60456 -0.04764 -0.06768 -0.13446 172 GLN A CA  
1032 C C   . GLN A 172 ? 0.53624 0.45121 0.59178 -0.04386 -0.06675 -0.12533 172 GLN A C   
1033 O O   . GLN A 172 ? 0.61685 0.53762 0.69149 -0.05246 -0.05809 -0.12494 172 GLN A O   
1034 C CB  . GLN A 172 ? 0.52703 0.40693 0.55573 -0.04951 -0.05622 -0.12634 172 GLN A CB  
1035 C CG  . GLN A 172 ? 0.52371 0.38091 0.54931 -0.05506 -0.05661 -0.13428 172 GLN A CG  
1036 C CD  . GLN A 172 ? 0.54509 0.38154 0.54507 -0.05629 -0.04639 -0.12558 172 GLN A CD  
1037 O OE1 . GLN A 172 ? 0.51310 0.34318 0.51662 -0.06812 -0.03280 -0.12046 172 GLN A OE1 
1038 N NE2 . GLN A 172 ? 0.59244 0.41808 0.56526 -0.04293 -0.05327 -0.12433 172 GLN A NE2 
1039 N N   . MET A 173 ? 0.53299 0.45529 0.56822 -0.03134 -0.07529 -0.11796 173 MET A N   
1040 C CA  . MET A 173 ? 0.51181 0.44724 0.54806 -0.02893 -0.07633 -0.10837 173 MET A CA  
1041 C C   . MET A 173 ? 0.55029 0.49561 0.61517 -0.03025 -0.08549 -0.11678 173 MET A C   
1042 O O   . MET A 173 ? 0.54837 0.49944 0.62722 -0.03418 -0.08179 -0.11386 173 MET A O   
1043 C CB  . MET A 173 ? 0.49708 0.43888 0.50531 -0.01677 -0.08302 -0.09788 173 MET A CB  
1044 C CG  . MET A 173 ? 0.50127 0.43870 0.48421 -0.01372 -0.07397 -0.08868 173 MET A CG  
1045 S SD  . MET A 173 ? 0.53770 0.48757 0.49062 0.00142  -0.08061 -0.07929 173 MET A SD  
1046 C CE  . MET A 173 ? 0.42010 0.38315 0.38058 0.00089  -0.08927 -0.07158 173 MET A CE  
1047 N N   . LEU A 174 ? 0.54986 0.49660 0.62382 -0.02606 -0.09877 -0.12819 174 LEU A N   
1048 C CA  . LEU A 174 ? 0.55325 0.51060 0.65621 -0.02568 -0.11000 -0.13726 174 LEU A CA  
1049 C C   . LEU A 174 ? 0.56854 0.52991 0.70792 -0.03807 -0.10040 -0.14752 174 LEU A C   
1050 O O   . LEU A 174 ? 0.58916 0.56229 0.75559 -0.03824 -0.10454 -0.15287 174 LEU A O   
1051 C CB  . LEU A 174 ? 0.58313 0.54068 0.68434 -0.01738 -0.12862 -0.14715 174 LEU A CB  
1052 C CG  . LEU A 174 ? 0.58818 0.54428 0.65245 -0.00390 -0.13833 -0.13794 174 LEU A CG  
1053 C CD1 . LEU A 174 ? 0.59671 0.54767 0.65227 0.00374  -0.15360 -0.14963 174 LEU A CD1 
1054 C CD2 . LEU A 174 ? 0.56493 0.52925 0.62735 0.00171  -0.14682 -0.12901 174 LEU A CD2 
1055 N N   . CYS A 175 ? 0.56737 0.51917 0.70757 -0.04816 -0.08741 -0.15025 175 CYS A N   
1056 C CA  . CYS A 175 ? 0.60530 0.56201 0.77790 -0.06163 -0.07505 -0.15848 175 CYS A CA  
1057 C C   . CYS A 175 ? 0.61140 0.57237 0.78590 -0.06474 -0.06138 -0.15110 175 CYS A C   
1058 O O   . CYS A 175 ? 0.62005 0.59454 0.82510 -0.06795 -0.05847 -0.15850 175 CYS A O   
1059 C CB  . CYS A 175 ? 0.66025 0.60141 0.82760 -0.07263 -0.06464 -0.16086 175 CYS A CB  
1060 S SG  . CYS A 175 ? 0.80659 0.74654 0.99718 -0.07739 -0.07800 -0.17749 175 CYS A SG  
1061 N N   . GLY A 176 ? 0.59244 0.54251 0.73504 -0.06308 -0.05361 -0.13745 176 GLY A N   
1062 C CA  . GLY A 176 ? 0.61962 0.57113 0.76027 -0.06535 -0.04312 -0.13058 176 GLY A CA  
1063 C C   . GLY A 176 ? 0.62694 0.58863 0.77491 -0.05657 -0.05474 -0.12877 176 GLY A C   
1064 O O   . GLY A 176 ? 0.73038 0.69664 0.89257 -0.05848 -0.04918 -0.13072 176 GLY A O   
1065 N N   . ILE A 177 ? 0.57222 0.53576 0.70851 -0.04649 -0.07119 -0.12507 177 ILE A N   
1066 C CA  . ILE A 177 ? 0.56731 0.53681 0.70772 -0.03835 -0.08432 -0.12201 177 ILE A CA  
1067 C C   . ILE A 177 ? 0.58809 0.56924 0.76718 -0.03767 -0.09032 -0.13690 177 ILE A C   
1068 O O   . ILE A 177 ? 0.59085 0.57515 0.78244 -0.03500 -0.09221 -0.13756 177 ILE A O   
1069 C CB  . ILE A 177 ? 0.55974 0.52827 0.67669 -0.02836 -0.09989 -0.11464 177 ILE A CB  
1070 C CG1 . ILE A 177 ? 0.53652 0.49929 0.61945 -0.02741 -0.09462 -0.09735 177 ILE A CG1 
1071 C CG2 . ILE A 177 ? 0.54004 0.51367 0.66777 -0.02009 -0.11766 -0.11632 177 ILE A CG2 
1072 C CD1 . ILE A 177 ? 0.50716 0.47176 0.56527 -0.01799 -0.10677 -0.08912 177 ILE A CD1 
1073 N N   . LYS A 178 ? 0.59375 0.58167 0.79379 -0.03979 -0.09414 -0.14983 178 LYS A N   
1074 C CA  . LYS A 178 ? 0.62197 0.62549 0.86367 -0.03902 -0.10056 -0.16512 178 LYS A CA  
1075 C C   . LYS A 178 ? 0.61427 0.62547 0.88064 -0.04776 -0.08182 -0.17143 178 LYS A C   
1076 O O   . LYS A 178 ? 0.63361 0.65873 0.93140 -0.04400 -0.08534 -0.18134 178 LYS A O   
1077 C CB  . LYS A 178 ? 0.66085 0.67045 0.92035 -0.04100 -0.10958 -0.17755 178 LYS A CB  
1078 C CG  . LYS A 178 ? 0.76491 0.77956 1.04883 -0.05572 -0.09310 -0.18710 178 LYS A CG  
1079 C CD  . LYS A 178 ? 0.89232 0.91405 1.19984 -0.05831 -0.10545 -0.20071 178 LYS A CD  
1080 C CE  . LYS A 178 ? 0.87401 0.91414 1.21278 -0.04845 -0.12421 -0.21104 178 LYS A CE  
1081 N NZ  . LYS A 178 ? 0.94091 0.99332 1.30804 -0.05242 -0.12728 -0.22106 178 LYS A NZ  
1082 N N   . HIS A 179 ? 0.61705 0.61924 0.86856 -0.05834 -0.06211 -0.16619 179 HIS A N   
1083 C CA  . HIS A 179 ? 0.63265 0.64028 0.90028 -0.06618 -0.04291 -0.17071 179 HIS A CA  
1084 C C   . HIS A 179 ? 0.60598 0.60902 0.86200 -0.05916 -0.04306 -0.16421 179 HIS A C   
1085 O O   . HIS A 179 ? 0.62035 0.63309 0.89899 -0.05867 -0.03596 -0.17280 179 HIS A O   
1086 C CB  . HIS A 179 ? 0.66392 0.65925 0.91331 -0.07915 -0.02325 -0.16552 179 HIS A CB  
1087 C CG  . HIS A 179 ? 0.71647 0.71561 0.97607 -0.08764 -0.00202 -0.16912 179 HIS A CG  
1088 N ND1 . HIS A 179 ? 0.84336 0.86347 1.14396 -0.09224 0.00588  -0.18365 179 HIS A ND1 
1089 C CD2 . HIS A 179 ? 0.75085 0.73653 0.98425 -0.09182 0.01297  -0.16053 179 HIS A CD2 
1090 C CE1 . HIS A 179 ? 0.88902 0.90833 1.18636 -0.09878 0.02638  -0.18375 179 HIS A CE1 
1091 N NE2 . HIS A 179 ? 0.81131 0.80826 1.06672 -0.09858 0.03024  -0.16986 179 HIS A NE2 
1092 N N   . LEU A 180 ? 0.60090 0.58952 0.82229 -0.05382 -0.05104 -0.14950 180 LEU A N   
1093 C CA  . LEU A 180 ? 0.59123 0.57339 0.80205 -0.04761 -0.05551 -0.14272 180 LEU A CA  
1094 C C   . LEU A 180 ? 0.56371 0.55534 0.80068 -0.03708 -0.07205 -0.15148 180 LEU A C   
1095 O O   . LEU A 180 ? 0.55498 0.54745 0.80446 -0.03333 -0.07069 -0.15657 180 LEU A O   
1096 C CB  . LEU A 180 ? 0.58017 0.54860 0.75280 -0.04522 -0.06248 -0.12481 180 LEU A CB  
1097 C CG  . LEU A 180 ? 0.57410 0.53195 0.71867 -0.05308 -0.04813 -0.11476 180 LEU A CG  
1098 C CD1 . LEU A 180 ? 0.54913 0.49784 0.66371 -0.05033 -0.05445 -0.09799 180 LEU A CD1 
1099 C CD2 . LEU A 180 ? 0.57471 0.52996 0.72541 -0.06112 -0.02948 -0.12046 180 LEU A CD2 
1100 N N   . HIS A 181 ? 0.58536 0.58280 0.82959 -0.03105 -0.08898 -0.15408 181 HIS A N   
1101 C CA  . HIS A 181 ? 0.55035 0.55632 0.82010 -0.02005 -0.10704 -0.16312 181 HIS A CA  
1102 C C   . HIS A 181 ? 0.54858 0.57469 0.86369 -0.02133 -0.09918 -0.18234 181 HIS A C   
1103 O O   . HIS A 181 ? 0.53111 0.56319 0.86813 -0.01236 -0.10632 -0.19047 181 HIS A O   
1104 C CB  . HIS A 181 ? 0.53815 0.54539 0.80299 -0.01363 -0.12702 -0.16226 181 HIS A CB  
1105 C CG  . HIS A 181 ? 0.53636 0.52777 0.75788 -0.01126 -0.13417 -0.14385 181 HIS A CG  
1106 N ND1 . HIS A 181 ? 0.53054 0.52071 0.73725 -0.00565 -0.14929 -0.14092 181 HIS A ND1 
1107 C CD2 . HIS A 181 ? 0.52381 0.50196 0.71446 -0.01391 -0.12791 -0.12777 181 HIS A CD2 
1108 C CE1 . HIS A 181 ? 0.52611 0.50466 0.69486 -0.00482 -0.15027 -0.12354 181 HIS A CE1 
1109 N NE2 . HIS A 181 ? 0.51792 0.48988 0.67816 -0.01034 -0.13776 -0.11511 181 HIS A NE2 
1110 N N   . SER A 182 ? 0.55204 0.58895 0.88224 -0.03246 -0.08436 -0.18979 182 SER A N   
1111 C CA  . SER A 182 ? 0.61680 0.67670 0.99191 -0.03621 -0.07355 -0.20730 182 SER A CA  
1112 C C   . SER A 182 ? 0.59781 0.65790 0.97547 -0.03640 -0.05678 -0.20958 182 SER A C   
1113 O O   . SER A 182 ? 0.65188 0.73228 1.06735 -0.03295 -0.05225 -0.22473 182 SER A O   
1114 C CB  . SER A 182 ? 0.68016 0.74740 1.06551 -0.05128 -0.05937 -0.21163 182 SER A CB  
1115 O OG  . SER A 182 ? 0.86677 0.95780 1.29434 -0.05796 -0.04435 -0.22660 182 SER A OG  
1116 N N   . ALA A 183 ? 0.59288 0.63166 0.93136 -0.03965 -0.04788 -0.19572 183 ALA A N   
1117 C CA  . ALA A 183 ? 0.59295 0.62692 0.92639 -0.03886 -0.03441 -0.19720 183 ALA A CA  
1118 C C   . ALA A 183 ? 0.55064 0.57053 0.87159 -0.02575 -0.05154 -0.19237 183 ALA A C   
1119 O O   . ALA A 183 ? 0.51761 0.52706 0.82649 -0.02432 -0.04381 -0.19173 183 ALA A O   
1120 C CB  . ALA A 183 ? 0.62573 0.64347 0.92395 -0.05086 -0.01532 -0.18580 183 ALA A CB  
1121 N N   . GLY A 184 ? 0.54692 0.56401 0.86835 -0.01652 -0.07526 -0.18874 184 GLY A N   
1122 C CA  . GLY A 184 ? 0.52317 0.52353 0.83109 -0.00535 -0.09304 -0.18235 184 GLY A CA  
1123 C C   . GLY A 184 ? 0.51341 0.48919 0.77663 -0.01021 -0.09336 -0.16248 184 GLY A C   
1124 O O   . GLY A 184 ? 0.52176 0.48125 0.77270 -0.00561 -0.09946 -0.15812 184 GLY A O   
1125 N N   . ILE A 185 ? 0.50879 0.48165 0.74853 -0.01921 -0.08767 -0.15083 185 ILE A N   
1126 C CA  . ILE A 185 ? 0.51058 0.46532 0.71121 -0.02438 -0.08695 -0.13212 185 ILE A CA  
1127 C C   . ILE A 185 ? 0.50276 0.45601 0.68578 -0.02266 -0.10069 -0.12000 185 ILE A C   
1128 O O   . ILE A 185 ? 0.51857 0.48199 0.70600 -0.02462 -0.09858 -0.12334 185 ILE A O   
1129 C CB  . ILE A 185 ? 0.53674 0.48945 0.72229 -0.03577 -0.06510 -0.12934 185 ILE A CB  
1130 C CG1 . ILE A 185 ? 0.54597 0.49358 0.73532 -0.03695 -0.05289 -0.13680 185 ILE A CG1 
1131 C CG2 . ILE A 185 ? 0.52783 0.46864 0.67722 -0.04053 -0.06653 -0.11042 185 ILE A CG2 
1132 C CD1 . ILE A 185 ? 0.56835 0.51857 0.75289 -0.04721 -0.02975 -0.14025 185 ILE A CD1 
1133 N N   . ILE A 186 ? 0.49510 0.43491 0.65714 -0.01934 -0.11461 -0.10603 186 ILE A N   
1134 C CA  . ILE A 186 ? 0.48132 0.41940 0.62104 -0.01795 -0.12589 -0.09224 186 ILE A CA  
1135 C C   . ILE A 186 ? 0.50793 0.43730 0.61621 -0.02576 -0.11911 -0.07432 186 ILE A C   
1136 O O   . ILE A 186 ? 0.48674 0.40409 0.58782 -0.02887 -0.11874 -0.06844 186 ILE A O   
1137 C CB  . ILE A 186 ? 0.50965 0.44073 0.65081 -0.00819 -0.14858 -0.08933 186 ILE A CB  
1138 C CG1 . ILE A 186 ? 0.49185 0.43448 0.66788 0.00067  -0.15673 -0.10855 186 ILE A CG1 
1139 C CG2 . ILE A 186 ? 0.50791 0.43728 0.62143 -0.00728 -0.15820 -0.07401 186 ILE A CG2 
1140 C CD1 . ILE A 186 ? 0.54459 0.47897 0.72233 0.01210  -0.18133 -0.10691 186 ILE A CD1 
1141 N N   . HIS A 187 ? 0.46521 0.40106 0.55587 -0.02839 -0.11455 -0.06659 187 HIS A N   
1142 C CA  . HIS A 187 ? 0.50143 0.43453 0.56723 -0.03557 -0.10563 -0.05198 187 HIS A CA  
1143 C C   . HIS A 187 ? 0.46604 0.39343 0.51141 -0.03601 -0.11703 -0.03361 187 HIS A C   
1144 O O   . HIS A 187 ? 0.50698 0.42429 0.54596 -0.04138 -0.11780 -0.02521 187 HIS A O   
1145 C CB  . HIS A 187 ? 0.45749 0.40013 0.51382 -0.03657 -0.09611 -0.05236 187 HIS A CB  
1146 C CG  . HIS A 187 ? 0.44751 0.38877 0.48696 -0.04334 -0.08341 -0.04377 187 HIS A CG  
1147 N ND1 . HIS A 187 ? 0.45027 0.39242 0.46935 -0.04582 -0.08550 -0.02692 187 HIS A ND1 
1148 C CD2 . HIS A 187 ? 0.46712 0.40632 0.50721 -0.04824 -0.06917 -0.04941 187 HIS A CD2 
1149 C CE1 . HIS A 187 ? 0.46186 0.40381 0.47158 -0.05084 -0.07424 -0.02357 187 HIS A CE1 
1150 N NE2 . HIS A 187 ? 0.50226 0.44048 0.52228 -0.05208 -0.06453 -0.03669 187 HIS A NE2 
1151 N N   . ARG A 188 ? 0.45530 0.38856 0.48891 -0.03113 -0.12578 -0.02699 188 ARG A N   
1152 C CA  . ARG A 188 ? 0.42062 0.35091 0.43277 -0.03189 -0.13575 -0.00842 188 ARG A CA  
1153 C C   . ARG A 188 ? 0.40693 0.34485 0.39920 -0.03943 -0.12582 0.00725  188 ARG A C   
1154 O O   . ARG A 188 ? 0.47314 0.41236 0.44798 -0.04201 -0.13144 0.02411  188 ARG A O   
1155 C CB  . ARG A 188 ? 0.51914 0.43195 0.53473 -0.03296 -0.14882 -0.00323 188 ARG A CB  
1156 C CG  . ARG A 188 ? 0.54974 0.45561 0.58699 -0.02371 -0.16074 -0.01858 188 ARG A CG  
1157 C CD  . ARG A 188 ? 0.58165 0.46937 0.62865 -0.02473 -0.16735 -0.02019 188 ARG A CD  
1158 N NE  . ARG A 188 ? 0.63283 0.50717 0.65835 -0.03291 -0.17273 0.00002  188 ARG A NE  
1159 C CZ  . ARG A 188 ? 0.67015 0.52445 0.69755 -0.03576 -0.17989 0.00226  188 ARG A CZ  
1160 N NH1 . ARG A 188 ? 0.70326 0.54924 0.75194 -0.02929 -0.18183 -0.01510 188 ARG A NH1 
1161 N NH2 . ARG A 188 ? 0.66840 0.51107 0.67631 -0.04540 -0.18524 0.02199  188 ARG A NH2 
1162 N N   . ASP A 189 ? 0.41145 0.35505 0.40584 -0.04316 -0.11155 0.00279  189 ASP A N   
1163 C CA  . ASP A 189 ? 0.42759 0.38080 0.40613 -0.04883 -0.10317 0.01630  189 ASP A CA  
1164 C C   . ASP A 189 ? 0.42431 0.38757 0.40047 -0.04559 -0.09098 0.00866  189 ASP A C   
1165 O O   . ASP A 189 ? 0.41737 0.38328 0.38934 -0.05005 -0.08174 0.01180  189 ASP A O   
1166 C CB  . ASP A 189 ? 0.43873 0.38272 0.41894 -0.05849 -0.10144 0.02258  189 ASP A CB  
1167 C CG  . ASP A 189 ? 0.46483 0.41886 0.43061 -0.06570 -0.10077 0.04191  189 ASP A CG  
1168 O OD1 . ASP A 189 ? 0.46163 0.42996 0.41574 -0.06295 -0.10160 0.05152  189 ASP A OD1 
1169 O OD2 . ASP A 189 ? 0.48007 0.42884 0.44642 -0.07420 -0.09939 0.04714  189 ASP A OD2 
1170 N N   . LEU A 190 ? 0.42410 0.39104 0.40213 -0.03756 -0.09242 -0.00166 190 LEU A N   
1171 C CA  . LEU A 190 ? 0.38792 0.36067 0.36154 -0.03393 -0.08296 -0.00881 190 LEU A CA  
1172 C C   . LEU A 190 ? 0.37374 0.36106 0.32717 -0.03133 -0.07912 0.00384  190 LEU A C   
1173 O O   . LEU A 190 ? 0.36891 0.36528 0.31062 -0.02891 -0.08488 0.01453  190 LEU A O   
1174 C CB  . LEU A 190 ? 0.37946 0.35120 0.36002 -0.02647 -0.08793 -0.02314 190 LEU A CB  
1175 C CG  . LEU A 190 ? 0.41512 0.37922 0.41346 -0.02882 -0.08127 -0.03952 190 LEU A CG  
1176 C CD1 . LEU A 190 ? 0.39107 0.35651 0.39151 -0.02204 -0.08593 -0.05146 190 LEU A CD1 
1177 C CD2 . LEU A 190 ? 0.40721 0.36782 0.39925 -0.03406 -0.06780 -0.03747 190 LEU A CD2 
1178 N N   . LYS A 191 ? 0.38896 0.37899 0.33800 -0.03151 -0.06913 0.00275  191 LYS A N   
1179 C CA  . LYS A 191 ? 0.38113 0.38786 0.31463 -0.02767 -0.06454 0.01305  191 LYS A CA  
1180 C C   . LYS A 191 ? 0.40327 0.40683 0.33341 -0.02343 -0.05632 0.00484  191 LYS A C   
1181 O O   . LYS A 191 ? 0.39044 0.37832 0.32915 -0.02803 -0.05261 -0.00383 191 LYS A O   
1182 C CB  . LYS A 191 ? 0.34430 0.35933 0.27682 -0.03650 -0.06387 0.02924  191 LYS A CB  
1183 C CG  . LYS A 191 ? 0.39572 0.39788 0.33718 -0.04531 -0.06064 0.02752  191 LYS A CG  
1184 C CD  . LYS A 191 ? 0.40852 0.41538 0.35074 -0.05525 -0.06408 0.04254  191 LYS A CD  
1185 C CE  . LYS A 191 ? 0.39971 0.39685 0.34677 -0.05985 -0.07401 0.04624  191 LYS A CE  
1186 N NZ  . LYS A 191 ? 0.55053 0.54491 0.49934 -0.07141 -0.07871 0.05915  191 LYS A NZ  
1187 N N   . PRO A 192 ? 0.38926 0.40650 0.30595 -0.01428 -0.05324 0.00729  192 PRO A N   
1188 C CA  . PRO A 192 ? 0.41017 0.42013 0.32178 -0.00849 -0.04754 -0.00118 192 PRO A CA  
1189 C C   . PRO A 192 ? 0.38878 0.39275 0.30285 -0.01528 -0.04201 0.00284  192 PRO A C   
1190 O O   . PRO A 192 ? 0.44418 0.43185 0.35608 -0.01446 -0.03822 -0.00533 192 PRO A O   
1191 C CB  . PRO A 192 ? 0.36773 0.39698 0.26411 0.00454  -0.04648 0.00182  192 PRO A CB  
1192 C CG  . PRO A 192 ? 0.35713 0.40021 0.24938 0.00571  -0.05153 0.00847  192 PRO A CG  
1193 C CD  . PRO A 192 ? 0.35700 0.39609 0.26132 -0.00783 -0.05469 0.01714  192 PRO A CD  
1194 N N   . SER A 193 ? 0.42227 0.43718 0.33941 -0.02253 -0.04233 0.01550  193 SER A N   
1195 C CA  . SER A 193 ? 0.40711 0.41619 0.32479 -0.02855 -0.03909 0.01913  193 SER A CA  
1196 C C   . SER A 193 ? 0.41987 0.40354 0.34333 -0.03680 -0.03724 0.01062  193 SER A C   
1197 O O   . SER A 193 ? 0.44365 0.41592 0.36210 -0.03944 -0.03347 0.00971  193 SER A O   
1198 C CB  . SER A 193 ? 0.39336 0.41951 0.31485 -0.03594 -0.04179 0.03408  193 SER A CB  
1199 O OG  . SER A 193 ? 0.38363 0.40568 0.31259 -0.04416 -0.04707 0.03763  193 SER A OG  
1200 N N   . ASN A 194 ? 0.41564 0.39104 0.34902 -0.04028 -0.03975 0.00423  194 ASN A N   
1201 C CA  . ASN A 194 ? 0.36490 0.32048 0.30649 -0.04725 -0.03639 -0.00522 194 ASN A CA  
1202 C C   . ASN A 194 ? 0.42880 0.37393 0.37442 -0.04415 -0.03316 -0.01877 194 ASN A C   
1203 O O   . ASN A 194 ? 0.63612 0.57164 0.59474 -0.04919 -0.03131 -0.02787 194 ASN A O   
1204 C CB  . ASN A 194 ? 0.44223 0.39646 0.39594 -0.05323 -0.04193 -0.00406 194 ASN A CB  
1205 C CG  . ASN A 194 ? 0.43330 0.39156 0.38373 -0.05942 -0.04554 0.00841  194 ASN A CG  
1206 O OD1 . ASN A 194 ? 0.39402 0.35740 0.33529 -0.06007 -0.04338 0.01546  194 ASN A OD1 
1207 N ND2 . ASN A 194 ? 0.55031 0.50541 0.50887 -0.06390 -0.05249 0.01092  194 ASN A ND2 
1208 N N   . ILE A 195 ? 0.39661 0.34406 0.33245 -0.03584 -0.03282 -0.02081 195 ILE A N   
1209 C CA  . ILE A 195 ? 0.44257 0.37770 0.38068 -0.03365 -0.03114 -0.03328 195 ILE A CA  
1210 C C   . ILE A 195 ? 0.44013 0.36528 0.36187 -0.02892 -0.02705 -0.03317 195 ILE A C   
1211 O O   . ILE A 195 ? 0.44278 0.37940 0.35254 -0.01964 -0.02941 -0.02697 195 ILE A O   
1212 C CB  . ILE A 195 ? 0.44499 0.38945 0.38639 -0.02586 -0.03920 -0.03839 195 ILE A CB  
1213 C CG1 . ILE A 195 ? 0.40230 0.35259 0.35991 -0.02988 -0.04506 -0.03945 195 ILE A CG1 
1214 C CG2 . ILE A 195 ? 0.40474 0.33534 0.34701 -0.02359 -0.03913 -0.05131 195 ILE A CG2 
1215 C CD1 . ILE A 195 ? 0.37155 0.33078 0.32870 -0.02168 -0.05499 -0.04268 195 ILE A CD1 
1216 N N   . VAL A 196 ? 0.43764 0.34168 0.35879 -0.03506 -0.02085 -0.03981 196 VAL A N   
1217 C CA  . VAL A 196 ? 0.51726 0.40536 0.42074 -0.03146 -0.01786 -0.03919 196 VAL A CA  
1218 C C   . VAL A 196 ? 0.49964 0.37035 0.40362 -0.03106 -0.01810 -0.05034 196 VAL A C   
1219 O O   . VAL A 196 ? 0.55430 0.42204 0.47500 -0.03862 -0.01708 -0.05869 196 VAL A O   
1220 C CB  . VAL A 196 ? 0.50297 0.37613 0.39868 -0.04039 -0.01051 -0.03453 196 VAL A CB  
1221 C CG1 . VAL A 196 ? 0.50203 0.38982 0.39183 -0.03804 -0.01324 -0.02312 196 VAL A CG1 
1222 C CG2 . VAL A 196 ? 0.48643 0.35301 0.39704 -0.05316 -0.00380 -0.04023 196 VAL A CG2 
1223 N N   . VAL A 197 ? 0.56642 0.42555 0.45304 -0.02188 -0.02048 -0.05091 197 VAL A N   
1224 C CA  . VAL A 197 ? 0.53963 0.37843 0.42338 -0.02061 -0.02294 -0.06119 197 VAL A CA  
1225 C C   . VAL A 197 ? 0.58580 0.39642 0.44968 -0.02068 -0.01996 -0.05898 197 VAL A C   
1226 O O   . VAL A 197 ? 0.60644 0.41694 0.45698 -0.01731 -0.01825 -0.05000 197 VAL A O   
1227 C CB  . VAL A 197 ? 0.57789 0.42733 0.45721 -0.00541 -0.03268 -0.06683 197 VAL A CB  
1228 C CG1 . VAL A 197 ? 0.51756 0.39453 0.41063 -0.00392 -0.03654 -0.06605 197 VAL A CG1 
1229 C CG2 . VAL A 197 ? 0.55791 0.41079 0.41680 0.01018  -0.03522 -0.06156 197 VAL A CG2 
1230 N N   . LYS A 198 ? 0.57561 0.36085 0.43749 -0.02497 -0.02064 -0.06713 198 LYS A N   
1231 C CA  . LYS A 198 ? 0.68151 0.43381 0.52184 -0.02432 -0.02022 -0.06570 198 LYS A CA  
1232 C C   . LYS A 198 ? 0.69317 0.43403 0.52193 -0.00930 -0.03109 -0.07350 198 LYS A C   
1233 O O   . LYS A 198 ? 0.69716 0.45509 0.53449 -0.00103 -0.03785 -0.08081 198 LYS A O   
1234 C CB  . LYS A 198 ? 0.65672 0.38349 0.50163 -0.04395 -0.01140 -0.06768 198 LYS A CB  
1235 C CG  . LYS A 198 ? 0.63117 0.34712 0.46449 -0.05383 -0.00093 -0.05774 198 LYS A CG  
1236 C CD  . LYS A 198 ? 0.63467 0.32832 0.47267 -0.07390 0.00999  -0.05980 198 LYS A CD  
1237 C CE  . LYS A 198 ? 0.63712 0.35539 0.50572 -0.08584 0.01799  -0.06490 198 LYS A CE  
1238 N NZ  . LYS A 198 ? 0.65513 0.35745 0.53273 -0.10566 0.03023  -0.06784 198 LYS A NZ  
1239 N N   . SER A 199 ? 0.73528 0.44451 0.54192 -0.00501 -0.03354 -0.07222 199 SER A N   
1240 C CA  . SER A 199 ? 0.81770 0.51128 0.61058 0.01099  -0.04481 -0.08072 199 SER A CA  
1241 C C   . SER A 199 ? 0.80391 0.48178 0.60765 0.00273  -0.04933 -0.09306 199 SER A C   
1242 O O   . SER A 199 ? 0.91959 0.59406 0.71753 0.01657  -0.06006 -0.10314 199 SER A O   
1243 C CB  . SER A 199 ? 0.87585 0.53473 0.64191 0.01754  -0.04788 -0.07635 199 SER A CB  
1244 O OG  . SER A 199 ? 0.88589 0.56120 0.64347 0.02636  -0.04595 -0.06587 199 SER A OG  
1245 N N   . ASP A 200 ? 0.74682 0.41633 0.56693 -0.01937 -0.04152 -0.09321 200 ASP A N   
1246 C CA  . ASP A 200 ? 0.71879 0.37703 0.55509 -0.03015 -0.04573 -0.10478 200 ASP A CA  
1247 C C   . ASP A 200 ? 0.68773 0.38131 0.55000 -0.02999 -0.04839 -0.11165 200 ASP A C   
1248 O O   . ASP A 200 ? 0.65573 0.34747 0.53936 -0.04270 -0.05010 -0.12034 200 ASP A O   
1249 C CB  . ASP A 200 ? 0.70748 0.34248 0.55148 -0.05474 -0.03511 -0.10170 200 ASP A CB  
1250 C CG  . ASP A 200 ? 0.70886 0.37042 0.57408 -0.06886 -0.02111 -0.09606 200 ASP A CG  
1251 O OD1 . ASP A 200 ? 0.63731 0.32754 0.50411 -0.05978 -0.01941 -0.09092 200 ASP A OD1 
1252 O OD2 . ASP A 200 ? 0.73316 0.38683 0.61389 -0.08928 -0.01166 -0.09703 200 ASP A OD2 
1253 N N   . CYS A 201 ? 0.70011 0.42551 0.56138 -0.01657 -0.04922 -0.10737 201 CYS A N   
1254 C CA  . CYS A 201 ? 0.65695 0.41445 0.53647 -0.01333 -0.05334 -0.11169 201 CYS A CA  
1255 C C   . CYS A 201 ? 0.61448 0.38819 0.52161 -0.03059 -0.04495 -0.10972 201 CYS A C   
1256 O O   . CYS A 201 ? 0.61684 0.41307 0.54138 -0.02950 -0.04983 -0.11424 201 CYS A O   
1257 C CB  . CYS A 201 ? 0.68151 0.43251 0.56314 -0.00689 -0.06694 -0.12623 201 CYS A CB  
1258 S SG  . CYS A 201 ? 0.70575 0.49076 0.58504 0.01157  -0.07635 -0.12928 201 CYS A SG  
1259 N N   . THR A 202 ? 0.60504 0.36763 0.51521 -0.04533 -0.03281 -0.10342 202 THR A N   
1260 C CA  . THR A 202 ? 0.58685 0.36667 0.52210 -0.05935 -0.02370 -0.10232 202 THR A CA  
1261 C C   . THR A 202 ? 0.55205 0.35829 0.48648 -0.05199 -0.02207 -0.09357 202 THR A C   
1262 O O   . THR A 202 ? 0.56466 0.37058 0.47848 -0.04371 -0.02084 -0.08416 202 THR A O   
1263 C CB  . THR A 202 ? 0.60914 0.36917 0.54391 -0.07661 -0.00976 -0.09820 202 THR A CB  
1264 O OG1 . THR A 202 ? 0.62968 0.37092 0.53395 -0.07123 -0.00677 -0.08806 202 THR A OG1 
1265 C CG2 . THR A 202 ? 0.63215 0.37089 0.57755 -0.08949 -0.01023 -0.10709 202 THR A CG2 
1266 N N   . LEU A 203 ? 0.55629 0.57053 0.27104 0.12198  -0.00857 -0.04152 203 LEU A N   
1267 C CA  . LEU A 203 ? 0.55176 0.56602 0.26937 0.11793  -0.00673 -0.04317 203 LEU A CA  
1268 C C   . LEU A 203 ? 0.55426 0.56023 0.25988 0.11738  0.00523  -0.04553 203 LEU A C   
1269 O O   . LEU A 203 ? 0.58817 0.59314 0.28971 0.12392  0.01318  -0.04562 203 LEU A O   
1270 C CB  . LEU A 203 ? 0.52780 0.55289 0.26074 0.12557  -0.01220 -0.04285 203 LEU A CB  
1271 C CG  . LEU A 203 ? 0.52544 0.55151 0.26046 0.12325  -0.01119 -0.04334 203 LEU A CG  
1272 C CD1 . LEU A 203 ? 0.50826 0.54617 0.25791 0.12636  -0.01950 -0.04135 203 LEU A CD1 
1273 C CD2 . LEU A 203 ? 0.53277 0.55614 0.26397 0.13002  -0.00363 -0.04497 203 LEU A CD2 
1274 N N   . LYS A 204 ? 0.55215 0.55265 0.25230 0.11036  0.00690  -0.04797 204 LYS A N   
1275 C CA  . LYS A 204 ? 0.58857 0.58021 0.27751 0.11029  0.01728  -0.05187 204 LYS A CA  
1276 C C   . LYS A 204 ? 0.57490 0.56451 0.26397 0.10774  0.01501  -0.05463 204 LYS A C   
1277 O O   . LYS A 204 ? 0.47071 0.46330 0.16261 0.10167  0.00731  -0.05379 204 LYS A O   
1278 C CB  . LYS A 204 ? 0.60991 0.59278 0.28305 0.10413  0.02298  -0.05344 204 LYS A CB  
1279 C CG  . LYS A 204 ? 0.63452 0.61721 0.30230 0.10847  0.02983  -0.05050 204 LYS A CG  
1280 C CD  . LYS A 204 ? 0.64593 0.62036 0.29590 0.10337  0.03665  -0.05145 204 LYS A CD  
1281 C CE  . LYS A 204 ? 0.60810 0.58300 0.25124 0.10689  0.04199  -0.04609 204 LYS A CE  
1282 N NZ  . LYS A 204 ? 0.67539 0.65238 0.31907 0.11579  0.05595  -0.04514 204 LYS A NZ  
1283 N N   . ILE A 205 ? 0.57653 0.56088 0.26191 0.11314  0.02222  -0.05801 205 ILE A N   
1284 C CA  . ILE A 205 ? 0.55488 0.53502 0.23736 0.11296  0.02065  -0.06097 205 ILE A CA  
1285 C C   . ILE A 205 ? 0.57993 0.54706 0.24619 0.10809  0.02542  -0.06767 205 ILE A C   
1286 O O   . ILE A 205 ? 0.63512 0.59548 0.29379 0.11082  0.03478  -0.07111 205 ILE A O   
1287 C CB  . ILE A 205 ? 0.58161 0.56252 0.26946 0.12392  0.02445  -0.06110 205 ILE A CB  
1288 C CG1 . ILE A 205 ? 0.51300 0.50824 0.21625 0.12993  0.01778  -0.05515 205 ILE A CG1 
1289 C CG2 . ILE A 205 ? 0.54207 0.51491 0.22248 0.12478  0.02362  -0.06456 205 ILE A CG2 
1290 C CD1 . ILE A 205 ? 0.50816 0.50573 0.21683 0.14206  0.02066  -0.05498 205 ILE A CD1 
1291 N N   . LEU A 206 ? 0.57166 0.53601 0.23235 0.10190  0.01908  -0.06996 206 LEU A N   
1292 C CA  . LEU A 206 ? 0.62696 0.58000 0.27171 0.09705  0.02065  -0.07708 206 LEU A CA  
1293 C C   . LEU A 206 ? 0.68971 0.62892 0.32400 0.10339  0.02635  -0.08479 206 LEU A C   
1294 O O   . LEU A 206 ? 0.67316 0.60347 0.29732 0.10546  0.03391  -0.09042 206 LEU A O   
1295 C CB  . LEU A 206 ? 0.61668 0.57244 0.25935 0.08865  0.01081  -0.07730 206 LEU A CB  
1296 C CG  . LEU A 206 ? 0.61601 0.58040 0.26391 0.08155  0.00592  -0.07262 206 LEU A CG  
1297 C CD1 . LEU A 206 ? 0.56479 0.53116 0.20961 0.07412  -0.00281 -0.07412 206 LEU A CD1 
1298 C CD2 . LEU A 206 ? 0.59759 0.55695 0.23626 0.08065  0.01190  -0.07415 206 LEU A CD2 
1299 N N   . ASP A 207 ? 0.73170 0.66809 0.36704 0.10738  0.02289  -0.08537 207 ASP A N   
1300 C CA  . ASP A 207 ? 0.77117 0.68998 0.39415 0.11348  0.02596  -0.09400 207 ASP A CA  
1301 C C   . ASP A 207 ? 0.73007 0.64685 0.35987 0.12478  0.03321  -0.09284 207 ASP A C   
1302 O O   . ASP A 207 ? 0.66536 0.59561 0.30930 0.12786  0.03508  -0.08547 207 ASP A O   
1303 C CB  . ASP A 207 ? 0.72512 0.63733 0.33959 0.11074  0.01632  -0.09679 207 ASP A CB  
1304 C CG  . ASP A 207 ? 0.76848 0.68597 0.38941 0.11634  0.01338  -0.09042 207 ASP A CG  
1305 O OD1 . ASP A 207 ? 0.75018 0.65342 0.35887 0.11965  0.00949  -0.09468 207 ASP A OD1 
1306 O OD2 . ASP A 207 ? 0.71199 0.64645 0.34855 0.11804  0.01421  -0.08141 207 ASP A OD2 
1307 N N   . PHE A 208 ? 0.73418 0.63247 0.35377 0.13182  0.03651  -0.10117 208 PHE A N   
1308 C CA  . PHE A 208 ? 0.71379 0.60716 0.33945 0.14368  0.04463  -0.10212 208 PHE A CA  
1309 C C   . PHE A 208 ? 0.68813 0.56977 0.30985 0.15129  0.04053  -0.10283 208 PHE A C   
1310 O O   . PHE A 208 ? 0.70603 0.58038 0.33257 0.16243  0.04673  -0.10465 208 PHE A O   
1311 C CB  . PHE A 208 ? 0.78131 0.66156 0.40026 0.14812  0.05429  -0.11181 208 PHE A CB  
1312 C CG  . PHE A 208 ? 0.80098 0.69313 0.42297 0.14403  0.06149  -0.10973 208 PHE A CG  
1313 C CD1 . PHE A 208 ? 0.77912 0.68622 0.41617 0.14756  0.06833  -0.10273 208 PHE A CD1 
1314 C CD2 . PHE A 208 ? 0.81548 0.70289 0.42387 0.13756  0.06112  -0.11497 208 PHE A CD2 
1315 C CE1 . PHE A 208 ? 0.81392 0.72967 0.45126 0.14441  0.07531  -0.10058 208 PHE A CE1 
1316 C CE2 . PHE A 208 ? 0.87441 0.77133 0.48261 0.13482  0.06823  -0.11235 208 PHE A CE2 
1317 C CZ  . PHE A 208 ? 0.87410 0.78452 0.49624 0.13810  0.07564  -0.10495 208 PHE A CZ  
1318 N N   . GLY A 209 ? 0.68218 0.56121 0.29495 0.14623  0.03056  -0.10139 209 GLY A N   
1319 C CA  . GLY A 209 ? 0.69757 0.56637 0.30365 0.15359  0.02661  -0.09963 209 GLY A CA  
1320 C C   . GLY A 209 ? 0.73103 0.57226 0.33415 0.15048  0.02238  -0.10706 209 GLY A C   
1321 O O   . GLY A 209 ? 0.72765 0.55192 0.31232 0.14861  0.02117  -0.11989 209 GLY A O   
1322 N N   . LEU A 210 ? 0.70775 0.54384 0.33023 0.15013  0.01910  -0.09839 210 LEU A N   
1323 C CA  . LEU A 210 ? 0.78373 0.59330 0.40972 0.14553  0.01273  -0.10226 210 LEU A CA  
1324 C C   . LEU A 210 ? 0.86870 0.65481 0.49288 0.15639  0.01953  -0.11430 210 LEU A C   
1325 O O   . LEU A 210 ? 0.91419 0.70773 0.53917 0.16744  0.03013  -0.11687 210 LEU A O   
1326 C CB  . LEU A 210 ? 0.74344 0.55723 0.39104 0.14028  0.00647  -0.08557 210 LEU A CB  
1327 C CG  . LEU A 210 ? 0.75635 0.59782 0.40843 0.13210  0.00141  -0.07171 210 LEU A CG  
1328 C CD1 . LEU A 210 ? 0.71767 0.56797 0.38994 0.13234  -0.00027 -0.05346 210 LEU A CD1 
1329 C CD2 . LEU A 210 ? 0.73871 0.57615 0.38376 0.11880  -0.00783 -0.07530 210 LEU A CD2 
1330 N N   . ALA A 211 ? 0.86753 0.62528 0.49089 0.15332  0.01278  -0.12192 211 ALA A N   
1331 C CA  . ALA A 211 ? 0.92427 0.65681 0.54506 0.16443  0.01745  -0.13509 211 ALA A CA  
1332 C C   . ALA A 211 ? 0.92803 0.65997 0.57142 0.17285  0.02113  -0.12565 211 ALA A C   
1333 O O   . ALA A 211 ? 0.88310 0.62389 0.54379 0.16749  0.01604  -0.10917 211 ALA A O   
1334 C CB  . ALA A 211 ? 0.90865 0.60911 0.52258 0.15874  0.00637  -0.14670 211 ALA A CB  
1335 N N   . SER A 217 ? 1.07676 0.70782 0.79200 0.04988  -0.08932 -0.10403 217 SER A N   
1336 C CA  . SER A 217 ? 1.09393 0.74572 0.78559 0.05198  -0.08739 -0.11611 217 SER A CA  
1337 C C   . SER A 217 ? 1.08778 0.75663 0.79150 0.03420  -0.09848 -0.11004 217 SER A C   
1338 O O   . SER A 217 ? 1.09536 0.80074 0.80082 0.03100  -0.09301 -0.09764 217 SER A O   
1339 C CB  . SER A 217 ? 1.11392 0.79872 0.79425 0.06342  -0.07090 -0.10801 217 SER A CB  
1340 O OG  . SER A 217 ? 1.05712 0.76529 0.71951 0.06251  -0.07021 -0.11435 217 SER A OG  
1341 N N   . PHE A 218 ? 1.09787 0.74023 0.81111 0.02318  -0.11489 -0.11951 218 PHE A N   
1342 C CA  . PHE A 218 ? 1.08746 0.74489 0.81602 0.00558  -0.12712 -0.11497 218 PHE A CA  
1343 C C   . PHE A 218 ? 1.11849 0.79298 0.81998 0.00948  -0.12839 -0.13042 218 PHE A C   
1344 O O   . PHE A 218 ? 1.11158 0.76716 0.78323 0.02129  -0.12901 -0.15276 218 PHE A O   
1345 C CB  . PHE A 218 ? 1.01407 0.63581 0.76125 -0.00703 -0.14628 -0.12295 218 PHE A CB  
1346 C CG  . PHE A 218 ? 0.98119 0.61510 0.74259 -0.02420 -0.16134 -0.12404 218 PHE A CG  
1347 C CD1 . PHE A 218 ? 0.92587 0.59459 0.71612 -0.03882 -0.15961 -0.09964 218 PHE A CD1 
1348 C CD2 . PHE A 218 ? 1.03908 0.65079 0.78502 -0.02481 -0.17745 -0.14975 218 PHE A CD2 
1349 C CE1 . PHE A 218 ? 0.92893 0.61144 0.73542 -0.05447 -0.17338 -0.10056 218 PHE A CE1 
1350 C CE2 . PHE A 218 ? 1.00427 0.62788 0.76520 -0.04038 -0.19274 -0.15137 218 PHE A CE2 
1351 C CZ  . PHE A 218 ? 0.97039 0.63008 0.76321 -0.05562 -0.19057 -0.12658 218 PHE A CZ  
1352 N N   . MET A 219 ? 1.12000 0.83077 0.83141 0.00029  -0.12860 -0.11798 219 MET A N   
1353 C CA  . MET A 219 ? 1.15871 0.88929 0.84667 0.00363  -0.12998 -0.12924 219 MET A CA  
1354 C C   . MET A 219 ? 1.21257 0.94514 0.91506 -0.01229 -0.14851 -0.13412 219 MET A C   
1355 O O   . MET A 219 ? 1.14781 0.90211 0.88221 -0.02674 -0.15187 -0.11589 219 MET A O   
1356 C CB  . MET A 219 ? 1.18918 0.96167 0.87504 0.00847  -0.11590 -0.11293 219 MET A CB  
1357 C CG  . MET A 219 ? 1.17374 0.94648 0.84203 0.02541  -0.09905 -0.11164 219 MET A CG  
1358 S SD  . MET A 219 ? 1.16989 0.97930 0.85754 0.02693  -0.08528 -0.08344 219 MET A SD  
1359 C CE  . MET A 219 ? 1.10665 0.91118 0.83393 0.00942  -0.09325 -0.06475 219 MET A CE  
1360 N N   . MET A 220 ? 1.51232 1.22338 1.19162 -0.00909 -0.16045 -0.15850 220 MET A N   
1361 C CA  . MET A 220 ? 1.49009 1.20225 1.17974 -0.02239 -0.18015 -0.16692 220 MET A CA  
1362 C C   . MET A 220 ? 1.48701 1.23240 1.15927 -0.01943 -0.17906 -0.16873 220 MET A C   
1363 O O   . MET A 220 ? 1.47493 1.21101 1.12008 -0.01418 -0.18850 -0.18875 220 MET A O   
1364 C CB  . MET A 220 ? 1.52203 1.19058 1.19527 -0.01958 -0.19627 -0.19355 220 MET A CB  
1365 C CG  . MET A 220 ? 1.54425 1.20516 1.24017 -0.03643 -0.22033 -0.20082 220 MET A CG  
1366 S SD  . MET A 220 ? 1.59241 1.25464 1.34755 -0.05911 -0.22657 -0.17653 220 MET A SD  
1367 C CE  . MET A 220 ? 1.53341 1.23258 1.31545 -0.07718 -0.24069 -0.17021 220 MET A CE  
1368 N N   . THR A 221 ? 1.43192 1.21614 1.11926 -0.02187 -0.16777 -0.14729 221 THR A N   
1369 C CA  . THR A 221 ? 1.45725 1.27415 1.12845 -0.01681 -0.16456 -0.14682 221 THR A CA  
1370 C C   . THR A 221 ? 1.44495 1.30311 1.14897 -0.02703 -0.16109 -0.12331 221 THR A C   
1371 O O   . THR A 221 ? 1.38107 1.24428 1.11173 -0.03287 -0.15397 -0.10473 221 THR A O   
1372 C CB  . THR A 221 ? 1.49189 1.31028 1.12884 0.00170  -0.14774 -0.14986 221 THR A CB  
1373 O OG1 . THR A 221 ? 1.48177 1.31578 1.09302 0.00798  -0.15011 -0.15870 221 THR A OG1 
1374 C CG2 . THR A 221 ? 1.43523 1.27742 1.08686 0.00494  -0.13086 -0.12771 221 THR A CG2 
1375 N N   . PRO A 222 ? 1.37135 1.25957 1.07408 -0.02878 -0.16625 -0.12343 222 PRO A N   
1376 C CA  . PRO A 222 ? 1.32176 1.25288 1.05379 -0.03592 -0.16131 -0.10141 222 PRO A CA  
1377 C C   . PRO A 222 ? 1.30674 1.26258 1.02605 -0.02264 -0.14342 -0.08919 222 PRO A C   
1378 O O   . PRO A 222 ? 1.24895 1.23497 0.99187 -0.02605 -0.13570 -0.06867 222 PRO A O   
1379 C CB  . PRO A 222 ? 1.26935 1.22047 1.00453 -0.04183 -0.17619 -0.10964 222 PRO A CB  
1380 C CG  . PRO A 222 ? 1.31138 1.23214 1.00961 -0.03382 -0.18635 -0.13567 222 PRO A CG  
1381 C CD  . PRO A 222 ? 1.36097 1.24545 1.03532 -0.02358 -0.17729 -0.14352 222 PRO A CD  
1382 N N   . TYR A 223 ? 1.30894 1.25322 0.99238 -0.00751 -0.13683 -0.10084 223 TYR A N   
1383 C CA  . TYR A 223 ? 1.28152 1.24674 0.95342 0.00521  -0.12176 -0.09100 223 TYR A CA  
1384 C C   . TYR A 223 ? 1.23485 1.19076 0.91682 0.00828  -0.10910 -0.07846 223 TYR A C   
1385 O O   . TYR A 223 ? 1.24878 1.17109 0.92276 0.01060  -0.10777 -0.08673 223 TYR A O   
1386 C CB  . TYR A 223 ? 1.32493 1.27919 0.95801 0.01895  -0.11933 -0.10670 223 TYR A CB  
1387 C CG  . TYR A 223 ? 1.33063 1.31298 0.95394 0.02990  -0.10977 -0.09861 223 TYR A CG  
1388 C CD1 . TYR A 223 ? 1.31236 1.33226 0.95491 0.02726  -0.11015 -0.08486 223 TYR A CD1 
1389 C CD2 . TYR A 223 ? 1.36529 1.33694 0.96121 0.04320  -0.10067 -0.10485 223 TYR A CD2 
1390 C CE1 . TYR A 223 ? 1.33225 1.37600 0.96532 0.03844  -0.10319 -0.07911 223 TYR A CE1 
1391 C CE2 . TYR A 223 ? 1.37046 1.36589 0.97268 0.04835  -0.09025 -0.09434 223 TYR A CE2 
1392 C CZ  . TYR A 223 ? 1.36266 1.39092 0.98059 0.04679  -0.09271 -0.08280 223 TYR A CZ  
1393 O OH  . TYR A 223 ? 1.35807 1.40079 0.99238 0.04883  -0.08171 -0.07159 223 TYR A OH  
1394 N N   . VAL A 224 ? 1.21080 1.19653 0.90907 0.00963  -0.10023 -0.05909 224 VAL A N   
1395 C CA  . VAL A 224 ? 1.08670 1.06700 0.79551 0.01297  -0.08910 -0.04512 224 VAL A CA  
1396 C C   . VAL A 224 ? 0.98907 0.96753 0.67382 0.02977  -0.07798 -0.04869 224 VAL A C   
1397 O O   . VAL A 224 ? 1.02021 1.01295 0.68625 0.03797  -0.07716 -0.05513 224 VAL A O   
1398 C CB  . VAL A 224 ? 1.06932 1.08290 0.80679 0.00683  -0.08506 -0.02148 224 VAL A CB  
1399 C CG1 . VAL A 224 ? 1.14653 1.15152 0.91428 -0.01096 -0.09303 -0.01392 224 VAL A CG1 
1400 C CG2 . VAL A 224 ? 1.06505 1.11847 0.80074 0.00987  -0.08603 -0.01852 224 VAL A CG2 
1401 N N   . VAL A 225 ? 0.93453 0.89480 0.62151 0.03480  -0.07004 -0.04418 225 VAL A N   
1402 C CA  . VAL A 225 ? 0.82603 0.78472 0.49587 0.04999  -0.05955 -0.04631 225 VAL A CA  
1403 C C   . VAL A 225 ? 0.73191 0.72326 0.41142 0.05602  -0.05257 -0.02855 225 VAL A C   
1404 O O   . VAL A 225 ? 0.72534 0.73607 0.42525 0.04905  -0.05340 -0.01282 225 VAL A O   
1405 C CB  . VAL A 225 ? 0.80169 0.72654 0.46989 0.05417  -0.05492 -0.05108 225 VAL A CB  
1406 C CG1 . VAL A 225 ? 0.73342 0.66109 0.42390 0.05310  -0.05012 -0.03232 225 VAL A CG1 
1407 C CG2 . VAL A 225 ? 0.76376 0.68123 0.40943 0.06856  -0.04664 -0.06172 225 VAL A CG2 
1408 N N   . THR A 226 ? 0.52557 0.55081 0.70185 -0.06217 -0.06944 -0.05968 226 THR A N   
1409 C CA  . THR A 226 ? 0.48337 0.46803 0.60524 -0.04961 -0.07233 -0.05471 226 THR A CA  
1410 C C   . THR A 226 ? 0.47099 0.42425 0.55111 -0.04072 -0.08536 -0.04655 226 THR A C   
1411 O O   . THR A 226 ? 0.45972 0.42924 0.54885 -0.04323 -0.11082 -0.04721 226 THR A O   
1412 C CB  . THR A 226 ? 0.43622 0.43312 0.55724 -0.04886 -0.09466 -0.05896 226 THR A CB  
1413 O OG1 . THR A 226 ? 0.45815 0.47477 0.60841 -0.05289 -0.08094 -0.06670 226 THR A OG1 
1414 C CG2 . THR A 226 ? 0.41893 0.37513 0.48325 -0.03531 -0.10361 -0.05466 226 THR A CG2 
1415 N N   . ARG A 227 ? 0.46710 0.37493 0.50098 -0.02990 -0.06786 -0.03969 227 ARG A N   
1416 C CA  . ARG A 227 ? 0.48092 0.35323 0.47003 -0.01853 -0.07893 -0.03202 227 ARG A CA  
1417 C C   . ARG A 227 ? 0.50472 0.33470 0.43195 -0.00247 -0.08682 -0.02844 227 ARG A C   
1418 O O   . ARG A 227 ? 0.50830 0.30278 0.39058 0.01024  -0.09571 -0.02250 227 ARG A O   
1419 C CB  . ARG A 227 ? 0.56604 0.41488 0.54802 -0.01809 -0.05220 -0.02543 227 ARG A CB  
1420 C CG  . ARG A 227 ? 0.54344 0.42366 0.58088 -0.03294 -0.02635 -0.03045 227 ARG A CG  
1421 C CD  . ARG A 227 ? 0.57557 0.43337 0.60926 -0.03360 -0.00402 -0.02425 227 ARG A CD  
1422 N NE  . ARG A 227 ? 0.64734 0.53562 0.73698 -0.04794 0.02129  -0.03101 227 ARG A NE  
1423 C CZ  . ARG A 227 ? 0.65015 0.53634 0.75062 -0.05236 0.05187  -0.03503 227 ARG A CZ  
1424 N NH1 . ARG A 227 ? 0.65393 0.50830 0.71192 -0.04403 0.06299  -0.03221 227 ARG A NH1 
1425 N NH2 . ARG A 227 ? 0.64930 0.56739 0.80625 -0.06525 0.07172  -0.04372 227 ARG A NH2 
1426 N N   . TYR A 228 ? 0.48280 0.31525 0.40600 -0.00153 -0.08523 -0.03281 228 TYR A N   
1427 C CA  . TYR A 228 ? 0.51894 0.31098 0.38367 0.01398  -0.08951 -0.03061 228 TYR A CA  
1428 C C   . TYR A 228 ? 0.52732 0.31163 0.36659 0.02337  -0.12633 -0.03186 228 TYR A C   
1429 O O   . TYR A 228 ? 0.57655 0.32298 0.36174 0.03890  -0.13256 -0.03007 228 TYR A O   
1430 C CB  . TYR A 228 ? 0.51197 0.31383 0.38577 0.01200  -0.08130 -0.03717 228 TYR A CB  
1431 C CG  . TYR A 228 ? 0.49119 0.31359 0.40539 0.00083  -0.04966 -0.04080 228 TYR A CG  
1432 C CD1 . TYR A 228 ? 0.46570 0.32643 0.42550 -0.00828 -0.05270 -0.05013 228 TYR A CD1 
1433 C CD2 . TYR A 228 ? 0.54316 0.34554 0.45014 -0.00022 -0.01697 -0.03583 228 TYR A CD2 
1434 C CE1 . TYR A 228 ? 0.46036 0.34193 0.45981 -0.01709 -0.02571 -0.05619 228 TYR A CE1 
1435 C CE2 . TYR A 228 ? 0.57887 0.40217 0.52740 -0.01093 0.01226  -0.04178 228 TYR A CE2 
1436 C CZ  . TYR A 228 ? 0.51337 0.37776 0.50921 -0.01883 0.00694  -0.05285 228 TYR A CZ  
1437 O OH  . TYR A 228 ? 0.61945 0.50663 0.65919 -0.02813 0.03419  -0.06138 228 TYR A OH  
1438 N N   . TYR A 229 ? 0.48262 0.30193 0.35955 0.01452  -0.15023 -0.03612 229 TYR A N   
1439 C CA  . TYR A 229 ? 0.48423 0.30360 0.34758 0.02065  -0.18526 -0.04067 229 TYR A CA  
1440 C C   . TYR A 229 ? 0.48823 0.30448 0.34846 0.02444  -0.20007 -0.03954 229 TYR A C   
1441 O O   . TYR A 229 ? 0.48404 0.30688 0.34247 0.02787  -0.22987 -0.04583 229 TYR A O   
1442 C CB  . TYR A 229 ? 0.43259 0.29461 0.34094 0.00698  -0.20293 -0.04856 229 TYR A CB  
1443 C CG  . TYR A 229 ? 0.42582 0.29350 0.34236 0.00340  -0.19004 -0.05065 229 TYR A CG  
1444 C CD1 . TYR A 229 ? 0.44950 0.29940 0.33734 0.01205  -0.20197 -0.05429 229 TYR A CD1 
1445 C CD2 . TYR A 229 ? 0.39677 0.28805 0.35119 -0.00771 -0.16695 -0.05065 229 TYR A CD2 
1446 C CE1 . TYR A 229 ? 0.44470 0.29933 0.34064 0.00987  -0.19126 -0.05727 229 TYR A CE1 
1447 C CE2 . TYR A 229 ? 0.39193 0.28901 0.35535 -0.00942 -0.15673 -0.05447 229 TYR A CE2 
1448 C CZ  . TYR A 229 ? 0.41610 0.29437 0.34982 -0.00054 -0.16896 -0.05747 229 TYR A CZ  
1449 O OH  . TYR A 229 ? 0.41236 0.29614 0.35581 -0.00128 -0.15989 -0.06229 229 TYR A OH  
1450 N N   . ARG A 230 ? 0.49763 0.30379 0.35863 0.02403  -0.18008 -0.03288 230 ARG A N   
1451 C CA  . ARG A 230 ? 0.50392 0.30528 0.36205 0.02882  -0.19371 -0.03214 230 ARG A CA  
1452 C C   . ARG A 230 ? 0.57246 0.31985 0.36233 0.05149  -0.20200 -0.02774 230 ARG A C   
1453 O O   . ARG A 230 ? 0.62144 0.32823 0.36525 0.06162  -0.18175 -0.02034 230 ARG A O   
1454 C CB  . ARG A 230 ? 0.48780 0.29881 0.37535 0.01932  -0.16936 -0.02718 230 ARG A CB  
1455 C CG  . ARG A 230 ? 0.47176 0.32821 0.41834 -0.00029 -0.15389 -0.03096 230 ARG A CG  
1456 C CD  . ARG A 230 ? 0.49263 0.36602 0.47626 -0.01017 -0.13657 -0.02944 230 ARG A CD  
1457 N NE  . ARG A 230 ? 0.46200 0.38896 0.50830 -0.02815 -0.13520 -0.03667 230 ARG A NE  
1458 C CZ  . ARG A 230 ? 0.45139 0.40353 0.54045 -0.03904 -0.12134 -0.03839 230 ARG A CZ  
1459 N NH1 . ARG A 230 ? 0.45678 0.38579 0.53605 -0.03523 -0.10639 -0.03313 230 ARG A NH1 
1460 N NH2 . ARG A 230 ? 0.44730 0.44738 0.58888 -0.05354 -0.12285 -0.04577 230 ARG A NH2 
1461 N N   . ALA A 231 ? 0.57769 0.32495 0.36099 0.05990  -0.23203 -0.03337 231 ALA A N   
1462 C CA  . ALA A 231 ? 0.64258 0.34119 0.36175 0.08368  -0.24690 -0.03185 231 ALA A CA  
1463 C C   . ALA A 231 ? 0.69450 0.34700 0.37277 0.09428  -0.22335 -0.01891 231 ALA A C   
1464 O O   . ALA A 231 ? 0.67290 0.33756 0.38213 0.08228  -0.20152 -0.01360 231 ALA A O   
1465 C CB  . ALA A 231 ? 0.62297 0.34569 0.37178 0.08487  -0.26585 -0.04270 231 ALA A CB  
1466 N N   . PRO A 232 ? 0.76679 0.36385 0.37345 0.11704  -0.22675 -0.01375 232 PRO A N   
1467 C CA  . PRO A 232 ? 0.82485 0.37121 0.38574 0.12784  -0.20381 -0.00002 232 PRO A CA  
1468 C C   . PRO A 232 ? 0.81396 0.36692 0.39709 0.12723  -0.21229 0.00037  232 PRO A C   
1469 O O   . PRO A 232 ? 0.83001 0.36366 0.41045 0.12338  -0.18474 0.01102  232 PRO A O   
1470 C CB  . PRO A 232 ? 0.90375 0.39297 0.38240 0.15495  -0.21677 0.00247  232 PRO A CB  
1471 C CG  . PRO A 232 ? 0.88594 0.39483 0.36915 0.15387  -0.23076 -0.00746 232 PRO A CG  
1472 C CD  . PRO A 232 ? 0.80270 0.37811 0.36445 0.13354  -0.24810 -0.01964 232 PRO A CD  
1473 N N   . GLU A 233 ? 0.78778 0.36797 0.39483 0.13056  -0.24925 -0.01216 233 GLU A N   
1474 C CA  . GLU A 233 ? 0.77677 0.36803 0.41027 0.12979  -0.25914 -0.01422 233 GLU A CA  
1475 C C   . GLU A 233 ? 0.74301 0.37908 0.44498 0.10422  -0.23610 -0.01310 233 GLU A C   
1476 O O   . GLU A 233 ? 0.78892 0.41988 0.50321 0.10266  -0.22742 -0.00899 233 GLU A O   
1477 C CB  . GLU A 233 ? 0.76515 0.39315 0.43407 0.12992  -0.28791 -0.03367 233 GLU A CB  
1478 C CG  . GLU A 233 ? 0.70472 0.38675 0.42906 0.11202  -0.28728 -0.04507 233 GLU A CG  
1479 C CD  . GLU A 233 ? 0.72513 0.39038 0.42100 0.12275  -0.29019 -0.05032 233 GLU A CD  
1480 O OE1 . GLU A 233 ? 0.76423 0.38567 0.40086 0.13498  -0.28439 -0.04195 233 GLU A OE1 
1481 O OE2 . GLU A 233 ? 0.69600 0.39055 0.42780 0.11933  -0.29571 -0.06149 233 GLU A OE2 
1482 N N   . VAL A 234 ? 0.65615 0.33504 0.40228 0.08507  -0.22689 -0.01732 234 VAL A N   
1483 C CA  . VAL A 234 ? 0.66837 0.38798 0.47597 0.06231  -0.20395 -0.01679 234 VAL A CA  
1484 C C   . VAL A 234 ? 0.67787 0.36578 0.46597 0.05974  -0.16267 -0.00392 234 VAL A C   
1485 O O   . VAL A 234 ? 0.72689 0.42402 0.54599 0.04921  -0.14202 -0.00074 234 VAL A O   
1486 C CB  . VAL A 234 ? 0.58786 0.36256 0.44697 0.04446  -0.21110 -0.02641 234 VAL A CB  
1487 C CG1 . VAL A 234 ? 0.55630 0.37117 0.47498 0.02302  -0.18752 -0.02645 234 VAL A CG1 
1488 C CG2 . VAL A 234 ? 0.54341 0.35011 0.42583 0.04431  -0.24876 -0.03972 234 VAL A CG2 
1489 N N   . ILE A 235 ? 0.67622 0.32696 0.41428 0.06890  -0.14937 0.00240  235 ILE A N   
1490 C CA  . ILE A 235 ? 0.73597 0.35390 0.45236 0.06645  -0.10798 0.01355  235 ILE A CA  
1491 C C   . ILE A 235 ? 0.76392 0.33705 0.44882 0.07542  -0.09504 0.02411  235 ILE A C   
1492 O O   . ILE A 235 ? 0.76237 0.33041 0.46507 0.06454  -0.06183 0.02999  235 ILE A O   
1493 C CB  . ILE A 235 ? 0.75990 0.34150 0.41998 0.07775  -0.09941 0.01747  235 ILE A CB  
1494 C CG1 . ILE A 235 ? 0.70882 0.33474 0.40682 0.06591  -0.10452 0.00770  235 ILE A CG1 
1495 C CG2 . ILE A 235 ? 0.81341 0.34941 0.43761 0.07864  -0.05638 0.02964  235 ILE A CG2 
1496 C CD1 . ILE A 235 ? 0.75289 0.34722 0.39920 0.07748  -0.09994 0.00917  235 ILE A CD1 
1497 N N   . LEU A 236 ? 0.80497 0.34475 0.44412 0.09565  -0.12164 0.02568  236 LEU A N   
1498 C CA  . LEU A 236 ? 0.92150 0.40844 0.51796 0.10853  -0.11265 0.03682  236 LEU A CA  
1499 C C   . LEU A 236 ? 0.93469 0.44538 0.56967 0.10734  -0.13457 0.03072  236 LEU A C   
1500 O O   . LEU A 236 ? 0.90586 0.37483 0.51114 0.11763  -0.12894 0.03922  236 LEU A O   
1501 C CB  . LEU A 236 ? 0.94993 0.37256 0.45707 0.13627  -0.12616 0.04360  236 LEU A CB  
1502 C CG  . LEU A 236 ? 0.98763 0.38253 0.44888 0.14032  -0.10640 0.04887  236 LEU A CG  
1503 C CD1 . LEU A 236 ? 1.07074 0.40461 0.44333 0.16958  -0.12473 0.05369  236 LEU A CD1 
1504 C CD2 . LEU A 236 ? 1.00783 0.38126 0.46666 0.12749  -0.05568 0.06035  236 LEU A CD2 
1505 N N   . GLY A 237 ? 1.02096 0.59574 0.71980 0.09515  -0.15859 0.01618  237 GLY A N   
1506 C CA  . GLY A 237 ? 0.96845 0.57091 0.70763 0.09324  -0.17983 0.00807  237 GLY A CA  
1507 C C   . GLY A 237 ? 1.06798 0.63211 0.75825 0.11870  -0.21129 0.00679  237 GLY A C   
1508 O O   . GLY A 237 ? 1.15675 0.67789 0.81676 0.12998  -0.20468 0.01537  237 GLY A O   
1509 N N   . MET A 238 ? 0.93316 0.51145 0.61567 0.12847  -0.24624 -0.00479 238 MET A N   
1510 C CA  . MET A 238 ? 1.00236 0.54517 0.63694 0.15514  -0.27946 -0.00900 238 MET A CA  
1511 C C   . MET A 238 ? 0.93151 0.53134 0.62155 0.14904  -0.30923 -0.03212 238 MET A C   
1512 O O   . MET A 238 ? 1.00454 0.59155 0.67787 0.16189  -0.32198 -0.04296 238 MET A O   
1513 C CB  . MET A 238 ? 1.05102 0.55571 0.62051 0.17089  -0.28097 -0.00746 238 MET A CB  
1514 C CG  . MET A 238 ? 1.04675 0.50900 0.57152 0.17067  -0.24636 0.01127  238 MET A CG  
1515 S SD  . MET A 238 ? 1.10238 0.54062 0.56935 0.18449  -0.25128 0.00703  238 MET A SD  
1516 C CE  . MET A 238 ? 0.98954 0.44045 0.46035 0.19758  -0.28406 -0.01619 238 MET A CE  
1517 N N   . GLY A 239 ? 0.89941 0.56327 0.66047 0.12609  -0.30968 -0.04153 239 GLY A N   
1518 C CA  . GLY A 239 ? 0.87229 0.58666 0.68810 0.11614  -0.31453 -0.06066 239 GLY A CA  
1519 C C   . GLY A 239 ? 0.86976 0.59517 0.68430 0.11470  -0.31158 -0.06609 239 GLY A C   
1520 O O   . GLY A 239 ? 0.88351 0.56908 0.64395 0.12770  -0.31342 -0.06123 239 GLY A O   
1521 N N   . TYR A 240 ? 0.84046 0.61925 0.71274 0.09928  -0.30340 -0.07424 240 TYR A N   
1522 C CA  . TYR A 240 ? 0.78526 0.58151 0.66558 0.09370  -0.29702 -0.07628 240 TYR A CA  
1523 C C   . TYR A 240 ? 0.78369 0.61156 0.69804 0.09053  -0.29600 -0.08601 240 TYR A C   
1524 O O   . TYR A 240 ? 0.79544 0.63705 0.73154 0.09050  -0.29775 -0.09125 240 TYR A O   
1525 C CB  . TYR A 240 ? 0.73016 0.56024 0.64077 0.07324  -0.27937 -0.06947 240 TYR A CB  
1526 C CG  . TYR A 240 ? 0.73174 0.60671 0.69385 0.05517  -0.26437 -0.06835 240 TYR A CG  
1527 C CD1 . TYR A 240 ? 0.69527 0.61257 0.69511 0.04403  -0.25160 -0.07223 240 TYR A CD1 
1528 C CD2 . TYR A 240 ? 0.73326 0.60579 0.70127 0.04980  -0.26196 -0.06297 240 TYR A CD2 
1529 C CE1 . TYR A 240 ? 0.67174 0.62620 0.70726 0.02916  -0.23449 -0.07015 240 TYR A CE1 
1530 C CE2 . TYR A 240 ? 0.71202 0.62607 0.72644 0.03413  -0.24593 -0.06279 240 TYR A CE2 
1531 C CZ  . TYR A 240 ? 0.67249 0.62630 0.71627 0.02465  -0.23094 -0.06589 240 TYR A CZ  
1532 O OH  . TYR A 240 ? 0.66366 0.65386 0.73958 0.01088  -0.21210 -0.06428 240 TYR A OH  
1533 N N   . LYS A 241 ? 0.76374 0.60145 0.68053 0.08807  -0.29315 -0.08818 241 LYS A N   
1534 C CA  . LYS A 241 ? 0.74236 0.61137 0.69136 0.08197  -0.28993 -0.09570 241 LYS A CA  
1535 C C   . LYS A 241 ? 0.70547 0.59855 0.67745 0.06688  -0.27807 -0.09277 241 LYS A C   
1536 O O   . LYS A 241 ? 0.69879 0.60435 0.67590 0.05457  -0.26394 -0.08320 241 LYS A O   
1537 C CB  . LYS A 241 ? 0.84110 0.68239 0.76525 0.10145  -0.30862 -0.10629 241 LYS A CB  
1538 C CG  . LYS A 241 ? 0.92561 0.72150 0.80793 0.12359  -0.32620 -0.10975 241 LYS A CG  
1539 C CD  . LYS A 241 ? 0.92230 0.70854 0.80114 0.13934  -0.34211 -0.12354 241 LYS A CD  
1540 C CE  . LYS A 241 ? 0.93589 0.69746 0.79910 0.15434  -0.35542 -0.12890 241 LYS A CE  
1541 N NZ  . LYS A 241 ? 0.78952 0.58724 0.69640 0.13900  -0.34474 -0.12726 241 LYS A NZ  
1542 N N   . GLU A 242 ? 0.70473 0.60395 0.69029 0.06840  -0.28429 -0.10156 242 GLU A N   
1543 C CA  . GLU A 242 ? 0.66327 0.58219 0.66737 0.05514  -0.27426 -0.09871 242 GLU A CA  
1544 C C   . GLU A 242 ? 0.65902 0.56234 0.63646 0.05597  -0.27185 -0.09194 242 GLU A C   
1545 O O   . GLU A 242 ? 0.63768 0.55501 0.62409 0.04341  -0.25888 -0.08433 242 GLU A O   
1546 C CB  . GLU A 242 ? 0.67114 0.59914 0.69431 0.05709  -0.28245 -0.11010 242 GLU A CB  
1547 C CG  . GLU A 242 ? 0.71180 0.66847 0.77076 0.04726  -0.27614 -0.11409 242 GLU A CG  
1548 C CD  . GLU A 242 ? 0.72537 0.67869 0.78983 0.05765  -0.28600 -0.12324 242 GLU A CD  
1549 O OE1 . GLU A 242 ? 0.72105 0.64896 0.75980 0.07156  -0.29649 -0.12435 242 GLU A OE1 
1550 O OE2 . GLU A 242 ? 0.73153 0.70652 0.82408 0.05241  -0.28341 -0.12963 242 GLU A OE2 
1551 N N   . ASN A 243 ? 0.72932 0.60268 0.67227 0.07174  -0.28417 -0.09515 243 ASN A N   
1552 C CA  . ASN A 243 ? 0.74854 0.60408 0.66222 0.07524  -0.28324 -0.09054 243 ASN A CA  
1553 C C   . ASN A 243 ? 0.73615 0.58030 0.63001 0.07270  -0.27548 -0.08024 243 ASN A C   
1554 O O   . ASN A 243 ? 0.79116 0.60696 0.65140 0.08127  -0.27997 -0.07857 243 ASN A O   
1555 C CB  . ASN A 243 ? 0.78420 0.60637 0.66199 0.09576  -0.29956 -0.09788 243 ASN A CB  
1556 C CG  . ASN A 243 ? 0.80770 0.59313 0.64822 0.11281  -0.31016 -0.09797 243 ASN A CG  
1557 O OD1 . ASN A 243 ? 0.77736 0.57053 0.63016 0.10898  -0.30760 -0.09570 243 ASN A OD1 
1558 N ND2 . ASN A 243 ? 0.90059 0.64203 0.69140 0.13307  -0.32237 -0.10081 243 ASN A ND2 
1559 N N   . VAL A 244 ? 0.67549 0.53347 0.58587 0.06405  -0.26762 -0.07524 244 VAL A N   
1560 C CA  . VAL A 244 ? 0.64294 0.48495 0.53572 0.06292  -0.26459 -0.06767 244 VAL A CA  
1561 C C   . VAL A 244 ? 0.58455 0.44786 0.49416 0.04903  -0.25174 -0.06328 244 VAL A C   
1562 O O   . VAL A 244 ? 0.55810 0.40061 0.44363 0.05143  -0.25229 -0.05899 244 VAL A O   
1563 C CB  . VAL A 244 ? 0.65888 0.51217 0.56987 0.05699  -0.26070 -0.06477 244 VAL A CB  
1564 C CG1 . VAL A 244 ? 0.59262 0.49877 0.55605 0.03696  -0.24227 -0.06394 244 VAL A CG1 
1565 C CG2 . VAL A 244 ? 0.62113 0.45020 0.50758 0.05822  -0.26133 -0.05756 244 VAL A CG2 
1566 N N   . ASP A 245 ? 0.55492 0.45644 0.50033 0.03535  -0.23981 -0.06415 245 ASP A N   
1567 C CA  . ASP A 245 ? 0.53392 0.45367 0.49261 0.02367  -0.22783 -0.06036 245 ASP A CA  
1568 C C   . ASP A 245 ? 0.57787 0.47540 0.51256 0.03215  -0.23646 -0.06301 245 ASP A C   
1569 O O   . ASP A 245 ? 0.54105 0.44296 0.47786 0.02628  -0.23034 -0.06019 245 ASP A O   
1570 C CB  . ASP A 245 ? 0.54156 0.48644 0.53648 0.01294  -0.22280 -0.06243 245 ASP A CB  
1571 C CG  . ASP A 245 ? 0.45310 0.41681 0.47068 0.00638  -0.21568 -0.06123 245 ASP A CG  
1572 O OD1 . ASP A 245 ? 0.43781 0.40849 0.45745 0.00144  -0.20634 -0.05595 245 ASP A OD1 
1573 O OD2 . ASP A 245 ? 0.43134 0.40347 0.46514 0.00631  -0.21944 -0.06642 245 ASP A OD2 
1574 N N   . ILE A 246 ? 0.67173 0.54543 0.58376 0.04663  -0.25066 -0.06918 246 ILE A N   
1575 C CA  . ILE A 246 ? 0.60960 0.46090 0.49691 0.05635  -0.25906 -0.07275 246 ILE A CA  
1576 C C   . ILE A 246 ? 0.62078 0.43900 0.46935 0.06500  -0.26184 -0.06901 246 ILE A C   
1577 O O   . ILE A 246 ? 0.63625 0.44786 0.47506 0.06544  -0.26107 -0.06909 246 ILE A O   
1578 C CB  . ILE A 246 ? 0.63313 0.46510 0.50316 0.07193  -0.27400 -0.08135 246 ILE A CB  
1579 C CG1 . ILE A 246 ? 0.64607 0.49643 0.54729 0.06739  -0.27859 -0.08916 246 ILE A CG1 
1580 C CG2 . ILE A 246 ? 0.68583 0.47586 0.50849 0.09042  -0.28555 -0.08434 246 ILE A CG2 
1581 C CD1 . ILE A 246 ? 0.64246 0.49182 0.54450 0.06536  -0.27957 -0.09090 246 ILE A CD1 
1582 N N   . TRP A 247 ? 0.61461 0.40989 0.43755 0.07215  -0.26445 -0.06551 247 TRP A N   
1583 C CA  . TRP A 247 ? 0.60944 0.36980 0.38728 0.08033  -0.26416 -0.06064 247 TRP A CA  
1584 C C   . TRP A 247 ? 0.56354 0.34735 0.36628 0.06486  -0.25350 -0.05720 247 TRP A C   
1585 O O   . TRP A 247 ? 0.57936 0.34507 0.35631 0.06937  -0.25283 -0.05696 247 TRP A O   
1586 C CB  . TRP A 247 ? 0.62740 0.35896 0.37217 0.08896  -0.26607 -0.05538 247 TRP A CB  
1587 C CG  . TRP A 247 ? 0.66380 0.35879 0.35779 0.09529  -0.25980 -0.04709 247 TRP A CG  
1588 C CD1 . TRP A 247 ? 0.63768 0.34578 0.34541 0.08236  -0.25171 -0.04260 247 TRP A CD1 
1589 C CD2 . TRP A 247 ? 0.73770 0.37461 0.35492 0.11656  -0.25710 -0.04134 247 TRP A CD2 
1590 N NE1 . TRP A 247 ? 0.68253 0.35159 0.34418 0.09043  -0.22825 -0.03325 247 TRP A NE1 
1591 C CE2 . TRP A 247 ? 0.75018 0.36953 0.34405 0.11336  -0.23618 -0.03102 247 TRP A CE2 
1592 C CE3 . TRP A 247 ? 0.79325 0.39412 0.36624 0.13643  -0.26245 -0.04377 247 TRP A CE3 
1593 C CZ2 . TRP A 247 ? 0.81386 0.38303 0.34708 0.12717  -0.21268 -0.02171 247 TRP A CZ2 
1594 C CZ3 . TRP A 247 ? 0.86311 0.40841 0.36137 0.15384  -0.25063 -0.03477 247 TRP A CZ3 
1595 C CH2 . TRP A 247 ? 0.87929 0.40253 0.34592 0.15140  -0.22914 -0.02156 247 TRP A CH2 
1596 N N   . SER A 248 ? 0.53051 0.35440 0.38238 0.04741  -0.24407 -0.05511 248 SER A N   
1597 C CA  . SER A 248 ? 0.48893 0.33736 0.36792 0.03308  -0.23320 -0.05268 248 SER A CA  
1598 C C   . SER A 248 ? 0.47136 0.32953 0.35917 0.03046  -0.23086 -0.05489 248 SER A C   
1599 O O   . SER A 248 ? 0.48678 0.34391 0.37274 0.02735  -0.22767 -0.05443 248 SER A O   
1600 C CB  . SER A 248 ? 0.44992 0.34096 0.37838 0.01670  -0.22024 -0.05022 248 SER A CB  
1601 O OG  . SER A 248 ? 0.48295 0.36569 0.40702 0.01900  -0.22380 -0.04900 248 SER A OG  
1602 N N   . VAL A 249 ? 0.46429 0.33090 0.36145 0.03177  -0.23325 -0.05810 249 VAL A N   
1603 C CA  . VAL A 249 ? 0.48246 0.35168 0.38230 0.03110  -0.23384 -0.06069 249 VAL A CA  
1604 C C   . VAL A 249 ? 0.50867 0.33892 0.36446 0.04636  -0.24425 -0.06362 249 VAL A C   
1605 O O   . VAL A 249 ? 0.51761 0.34622 0.37180 0.04515  -0.24320 -0.06454 249 VAL A O   
1606 C CB  . VAL A 249 ? 0.50609 0.38860 0.42103 0.03022  -0.23612 -0.06474 249 VAL A CB  
1607 C CG1 . VAL A 249 ? 0.50477 0.38246 0.41995 0.03124  -0.24104 -0.06849 249 VAL A CG1 
1608 C CG2 . VAL A 249 ? 0.45828 0.36671 0.40844 0.01876  -0.23000 -0.06340 249 VAL A CG2 
1609 N N   . GLY A 250 ? 0.55194 0.34801 0.36683 0.06215  -0.25325 -0.06497 250 GLY A N   
1610 C CA  . GLY A 250 ? 0.60420 0.35927 0.36676 0.07905  -0.25952 -0.06705 250 GLY A CA  
1611 C C   . GLY A 250 ? 0.61173 0.35425 0.35350 0.07798  -0.25285 -0.06378 250 GLY A C   
1612 O O   . GLY A 250 ? 0.63200 0.35962 0.35275 0.08389  -0.25322 -0.06650 250 GLY A O   
1613 N N   . CYS A 251 ? 0.59744 0.34530 0.34421 0.07073  -0.24692 -0.05913 251 CYS A N   
1614 C CA  . CYS A 251 ? 0.60514 0.34177 0.33269 0.06846  -0.24022 -0.05826 251 CYS A CA  
1615 C C   . CYS A 251 ? 0.56143 0.33187 0.33452 0.05464  -0.23675 -0.06167 251 CYS A C   
1616 O O   . CYS A 251 ? 0.57825 0.33449 0.33041 0.05747  -0.23430 -0.06561 251 CYS A O   
1617 C CB  . CYS A 251 ? 0.59215 0.33417 0.33068 0.06053  -0.22691 -0.05233 251 CYS A CB  
1618 S SG  . CYS A 251 ? 0.62646 0.34161 0.33312 0.07255  -0.23121 -0.04629 251 CYS A SG  
1619 N N   . ILE A 252 ? 0.51030 0.32224 0.33974 0.04074  -0.23359 -0.06016 252 ILE A N   
1620 C CA  . ILE A 252 ? 0.49103 0.33001 0.35590 0.02973  -0.22759 -0.06071 252 ILE A CA  
1621 C C   . ILE A 252 ? 0.50111 0.32302 0.34674 0.03883  -0.23431 -0.06482 252 ILE A C   
1622 O O   . ILE A 252 ? 0.50492 0.32280 0.34705 0.03932  -0.23397 -0.06772 252 ILE A O   
1623 C CB  . ILE A 252 ? 0.45396 0.33371 0.36726 0.01501  -0.21755 -0.05643 252 ILE A CB  
1624 C CG1 . ILE A 252 ? 0.40955 0.30934 0.34526 0.00578  -0.20891 -0.05305 252 ILE A CG1 
1625 C CG2 . ILE A 252 ? 0.44888 0.34778 0.38544 0.00687  -0.21097 -0.05573 252 ILE A CG2 
1626 C CD1 . ILE A 252 ? 0.35537 0.29244 0.32804 -0.00639 -0.19548 -0.04916 252 ILE A CD1 
1627 N N   . MET A 253 ? 0.51969 0.33175 0.35428 0.04657  -0.24119 -0.06652 253 MET A N   
1628 C CA  . MET A 253 ? 0.56095 0.35762 0.37991 0.05536  -0.24859 -0.07156 253 MET A CA  
1629 C C   . MET A 253 ? 0.59194 0.35176 0.36108 0.07066  -0.25243 -0.07522 253 MET A C   
1630 O O   . MET A 253 ? 0.60230 0.35573 0.36580 0.07396  -0.25469 -0.07928 253 MET A O   
1631 C CB  . MET A 253 ? 0.55961 0.35139 0.37487 0.06211  -0.25636 -0.07465 253 MET A CB  
1632 C CG  . MET A 253 ? 0.58220 0.36190 0.38768 0.07007  -0.26485 -0.08091 253 MET A CG  
1633 S SD  . MET A 253 ? 0.69458 0.47145 0.50030 0.07780  -0.27529 -0.08681 253 MET A SD  
1634 C CE  . MET A 253 ? 0.68346 0.42301 0.44536 0.09852  -0.28758 -0.09487 253 MET A CE  
1635 N N   . GLY A 254 ? 0.62608 0.35866 0.35372 0.08092  -0.25147 -0.07364 254 GLY A N   
1636 C CA  . GLY A 254 ? 0.67772 0.37144 0.34737 0.09584  -0.24872 -0.07616 254 GLY A CA  
1637 C C   . GLY A 254 ? 0.66310 0.36434 0.33996 0.08800  -0.24119 -0.07941 254 GLY A C   
1638 O O   . GLY A 254 ? 0.69374 0.37401 0.33944 0.09699  -0.23835 -0.08554 254 GLY A O   
1639 N N   . GLU A 255 ? 0.61647 0.34874 0.33671 0.07135  -0.23716 -0.07730 255 GLU A N   
1640 C CA  . GLU A 255 ? 0.59531 0.34254 0.33931 0.06247  -0.22327 -0.08040 255 GLU A CA  
1641 C C   . GLU A 255 ? 0.57612 0.33904 0.34496 0.05878  -0.23445 -0.08609 255 GLU A C   
1642 O O   . GLU A 255 ? 0.58509 0.34453 0.35241 0.06032  -0.22676 -0.09255 255 GLU A O   
1643 C CB  . GLU A 255 ? 0.54739 0.32861 0.34053 0.04586  -0.21202 -0.07534 255 GLU A CB  
1644 C CG  . GLU A 255 ? 0.53277 0.32764 0.35168 0.03971  -0.18304 -0.07568 255 GLU A CG  
1645 C CD  . GLU A 255 ? 0.48936 0.31644 0.35461 0.02500  -0.17189 -0.07186 255 GLU A CD  
1646 O OE1 . GLU A 255 ? 0.48534 0.31294 0.34926 0.02283  -0.17585 -0.06632 255 GLU A OE1 
1647 O OE2 . GLU A 255 ? 0.51386 0.36599 0.41726 0.01655  -0.16014 -0.07557 255 GLU A OE2 
1648 N N   . MET A 256 ? 0.55000 0.33407 0.35180 0.05323  -0.23863 -0.08033 256 MET A N   
1649 C CA  . MET A 256 ? 0.55497 0.34930 0.37780 0.05057  -0.24111 -0.08210 256 MET A CA  
1650 C C   . MET A 256 ? 0.59309 0.35551 0.37466 0.06669  -0.24797 -0.08984 256 MET A C   
1651 O O   . MET A 256 ? 0.58391 0.34747 0.37295 0.06724  -0.24974 -0.09448 256 MET A O   
1652 C CB  . MET A 256 ? 0.51203 0.32668 0.36553 0.04224  -0.24134 -0.07664 256 MET A CB  
1653 C CG  . MET A 256 ? 0.52683 0.37353 0.41743 0.02719  -0.23124 -0.06933 256 MET A CG  
1654 S SD  . MET A 256 ? 0.64446 0.50696 0.55441 0.02106  -0.23032 -0.06621 256 MET A SD  
1655 C CE  . MET A 256 ? 0.49302 0.38058 0.43570 0.00747  -0.22113 -0.06198 256 MET A CE  
1656 N N   . VAL A 257 ? 0.62745 0.36043 0.36388 0.08096  -0.25107 -0.09120 257 VAL A N   
1657 C CA  . VAL A 257 ? 0.67681 0.37791 0.36859 0.09815  -0.25490 -0.09810 257 VAL A CA  
1658 C C   . VAL A 257 ? 0.72140 0.39645 0.36833 0.10689  -0.24392 -0.10510 257 VAL A C   
1659 O O   . VAL A 257 ? 0.73389 0.39663 0.36472 0.11445  -0.24243 -0.11366 257 VAL A O   
1660 C CB  . VAL A 257 ? 0.71104 0.39105 0.37289 0.11094  -0.26094 -0.09656 257 VAL A CB  
1661 C CG1 . VAL A 257 ? 0.82472 0.46843 0.43239 0.13079  -0.26184 -0.10279 257 VAL A CG1 
1662 C CG2 . VAL A 257 ? 0.70405 0.40714 0.40793 0.10299  -0.26944 -0.09539 257 VAL A CG2 
1663 N N   . ARG A 258 ? 0.71807 0.38601 0.35009 0.10498  -0.22876 -0.10116 258 ARG A N   
1664 C CA  . ARG A 258 ? 0.74340 0.39748 0.35838 0.10946  -0.19340 -0.09899 258 ARG A CA  
1665 C C   . ARG A 258 ? 0.70165 0.38765 0.36915 0.09544  -0.17470 -0.10092 258 ARG A C   
1666 O O   . ARG A 258 ? 0.72036 0.39930 0.38144 0.09910  -0.14882 -0.10468 258 ARG A O   
1667 C CB  . ARG A 258 ? 0.77039 0.40390 0.35545 0.11343  -0.17386 -0.08816 258 ARG A CB  
1668 C CG  . ARG A 258 ? 0.83607 0.44079 0.38325 0.12214  -0.13807 -0.08608 258 ARG A CG  
1669 C CD  . ARG A 258 ? 0.84642 0.42806 0.36444 0.12468  -0.11876 -0.07385 258 ARG A CD  
1670 N NE  . ARG A 258 ? 0.90106 0.44266 0.35513 0.14320  -0.13479 -0.07080 258 ARG A NE  
1671 C CZ  . ARG A 258 ? 0.93779 0.45590 0.36121 0.14869  -0.13093 -0.06046 258 ARG A CZ  
1672 N NH1 . ARG A 258 ? 0.90535 0.43568 0.35686 0.13614  -0.11078 -0.05176 258 ARG A NH1 
1673 N NH2 . ARG A 258 ? 0.98174 0.46244 0.34470 0.16820  -0.14874 -0.05964 258 ARG A NH2 
1674 N N   . HIS A 259 ? 0.64796 0.36883 0.36664 0.08016  -0.18730 -0.09965 259 HIS A N   
1675 C CA  . HIS A 259 ? 0.60757 0.36038 0.37732 0.06780  -0.17263 -0.10198 259 HIS A CA  
1676 C C   . HIS A 259 ? 0.61365 0.36649 0.38722 0.06530  -0.13621 -0.09801 259 HIS A C   
1677 O O   . HIS A 259 ? 0.60543 0.37125 0.40331 0.06239  -0.11495 -0.10417 259 HIS A O   
1678 C CB  . HIS A 259 ? 0.60966 0.36513 0.38837 0.07171  -0.17647 -0.11288 259 HIS A CB  
1679 C CG  . HIS A 259 ? 0.60865 0.36015 0.38244 0.07393  -0.21048 -0.11716 259 HIS A CG  
1680 N ND1 . HIS A 259 ? 0.57878 0.35244 0.38502 0.06171  -0.23373 -0.11477 259 HIS A ND1 
1681 C CD2 . HIS A 259 ? 0.64351 0.37065 0.38381 0.08641  -0.22429 -0.12427 259 HIS A CD2 
1682 C CE1 . HIS A 259 ? 0.62584 0.39825 0.43499 0.06497  -0.24345 -0.11083 259 HIS A CE1 
1683 N NE2 . HIS A 259 ? 0.66514 0.40741 0.43161 0.08017  -0.24545 -0.12001 259 HIS A NE2 
1684 N N   . LYS A 260 ? 0.62998 0.36754 0.38030 0.06664  -0.12925 -0.08862 260 LYS A N   
1685 C CA  . LYS A 260 ? 0.63945 0.37279 0.39099 0.06323  -0.09489 -0.08333 260 LYS A CA  
1686 C C   . LYS A 260 ? 0.63508 0.36482 0.38050 0.06016  -0.10122 -0.07282 260 LYS A C   
1687 O O   . LYS A 260 ? 0.65112 0.36464 0.36667 0.06780  -0.12610 -0.07001 260 LYS A O   
1688 C CB  . LYS A 260 ? 0.69991 0.39486 0.40062 0.07606  -0.06857 -0.08392 260 LYS A CB  
1689 C CG  . LYS A 260 ? 0.70530 0.40309 0.42199 0.06949  -0.02688 -0.08406 260 LYS A CG  
1690 C CD  . LYS A 260 ? 0.75410 0.42613 0.43682 0.07938  -0.00189 -0.09063 260 LYS A CD  
1691 C CE  . LYS A 260 ? 0.72960 0.42764 0.44798 0.07812  -0.00710 -0.10547 260 LYS A CE  
1692 N NZ  . LYS A 260 ? 0.81739 0.48729 0.49313 0.09163  0.00367  -0.11301 260 LYS A NZ  
1693 N N   . ILE A 261 ? 0.61332 0.35939 0.38961 0.04937  -0.07963 -0.06872 261 ILE A N   
1694 C CA  . ILE A 261 ? 0.60876 0.35218 0.38242 0.04640  -0.08428 -0.05946 261 ILE A CA  
1695 C C   . ILE A 261 ? 0.67280 0.36661 0.37919 0.06188  -0.07829 -0.05184 261 ILE A C   
1696 O O   . ILE A 261 ? 0.71645 0.38166 0.39114 0.06795  -0.04871 -0.04980 261 ILE A O   
1697 C CB  . ILE A 261 ? 0.57689 0.34561 0.39662 0.03241  -0.05953 -0.05789 261 ILE A CB  
1698 C CG1 . ILE A 261 ? 0.51330 0.33141 0.39626 0.01871  -0.07347 -0.06482 261 ILE A CG1 
1699 C CG2 . ILE A 261 ? 0.58553 0.34196 0.39337 0.03187  -0.05823 -0.04795 261 ILE A CG2 
1700 C CD1 . ILE A 261 ? 0.48544 0.33100 0.41680 0.00749  -0.04622 -0.06958 261 ILE A CD1 
1701 N N   . LEU A 262 ? 0.68140 0.36410 0.36478 0.06881  -0.10660 -0.04841 262 LEU A N   
1702 C CA  . LEU A 262 ? 0.74641 0.38003 0.36070 0.08710  -0.10834 -0.04273 262 LEU A CA  
1703 C C   . LEU A 262 ? 0.77942 0.38633 0.37127 0.08822  -0.07790 -0.03191 262 LEU A C   
1704 O O   . LEU A 262 ? 0.84169 0.40443 0.37680 0.10076  -0.05841 -0.02699 262 LEU A O   
1705 C CB  . LEU A 262 ? 0.74400 0.37689 0.34681 0.09408  -0.14774 -0.04427 262 LEU A CB  
1706 C CG  . LEU A 262 ? 0.76727 0.38643 0.33925 0.10709  -0.17442 -0.05272 262 LEU A CG  
1707 C CD1 . LEU A 262 ? 0.73878 0.38178 0.34215 0.09926  -0.17293 -0.06124 262 LEU A CD1 
1708 C CD2 . LEU A 262 ? 0.75060 0.38148 0.33079 0.10891  -0.21306 -0.05741 262 LEU A CD2 
1709 N N   . PHE A 263 ? 0.74158 0.37281 0.37564 0.07522  -0.07270 -0.02811 263 PHE A N   
1710 C CA  . PHE A 263 ? 0.77053 0.37694 0.38796 0.07499  -0.04573 -0.01779 263 PHE A CA  
1711 C C   . PHE A 263 ? 0.72276 0.36605 0.40393 0.05543  -0.02035 -0.01977 263 PHE A C   
1712 O O   . PHE A 263 ? 0.68251 0.35262 0.40414 0.04531  -0.02768 -0.01868 263 PHE A O   
1713 C CB  . PHE A 263 ? 0.78101 0.37395 0.37951 0.08238  -0.06933 -0.01176 263 PHE A CB  
1714 C CG  . PHE A 263 ? 0.81507 0.38376 0.36478 0.10080  -0.10261 -0.01427 263 PHE A CG  
1715 C CD1 . PHE A 263 ? 0.88838 0.40457 0.36510 0.11982  -0.09513 -0.01008 263 PHE A CD1 
1716 C CD2 . PHE A 263 ? 0.77578 0.37431 0.35286 0.09905  -0.14082 -0.02200 263 PHE A CD2 
1717 C CE1 . PHE A 263 ? 0.92088 0.41574 0.35357 0.13808  -0.12729 -0.01440 263 PHE A CE1 
1718 C CE2 . PHE A 263 ? 0.80696 0.38516 0.34353 0.11581  -0.17172 -0.02690 263 PHE A CE2 
1719 C CZ  . PHE A 263 ? 0.87908 0.40590 0.34377 0.13602  -0.16601 -0.02354 263 PHE A CZ  
1720 N N   . PRO A 264 ? 0.72645 0.37331 0.41959 0.05019  0.00930  -0.02438 264 PRO A N   
1721 C CA  . PRO A 264 ? 0.68391 0.36630 0.43920 0.03277  0.03402  -0.02898 264 PRO A CA  
1722 C C   . PRO A 264 ? 0.71752 0.37260 0.45951 0.02989  0.06809  -0.02016 264 PRO A C   
1723 O O   . PRO A 264 ? 0.77743 0.38302 0.45822 0.04188  0.07400  -0.00942 264 PRO A O   
1724 C CB  . PRO A 264 ? 0.68301 0.37575 0.45067 0.03133  0.05030  -0.03957 264 PRO A CB  
1725 C CG  . PRO A 264 ? 0.75101 0.39398 0.44613 0.04804  0.05504  -0.03558 264 PRO A CG  
1726 C CD  . PRO A 264 ? 0.77074 0.39063 0.42237 0.06069  0.02100  -0.02775 264 PRO A CD  
1727 N N   . GLY A 265 ? 0.68037 0.36726 0.48047 0.01410  0.09039  -0.02533 265 GLY A N   
1728 C CA  . GLY A 265 ? 0.71216 0.37650 0.50871 0.00859  0.12553  -0.01869 265 GLY A CA  
1729 C C   . GLY A 265 ? 0.68495 0.39425 0.55539 -0.00882 0.13490  -0.02521 265 GLY A C   
1730 O O   . GLY A 265 ? 0.62728 0.38050 0.54288 -0.01472 0.10695  -0.03080 265 GLY A O   
1731 N N   . ARG A 266 ? 0.69469 0.39266 0.57759 -0.01739 0.17522  -0.02516 266 ARG A N   
1732 C CA  . ARG A 266 ? 0.67084 0.40961 0.62411 -0.03347 0.18601  -0.03260 266 ARG A CA  
1733 C C   . ARG A 266 ? 0.68015 0.41862 0.63595 -0.03383 0.16618  -0.02376 266 ARG A C   
1734 O O   . ARG A 266 ? 0.65607 0.44124 0.67045 -0.04377 0.15205  -0.03100 266 ARG A O   
1735 C CB  . ARG A 266 ? 0.69830 0.42197 0.66372 -0.04285 0.23588  -0.03590 266 ARG A CB  
1736 C CG  . ARG A 266 ? 0.73837 0.44666 0.68323 -0.03986 0.26093  -0.04245 266 ARG A CG  
1737 C CD  . ARG A 266 ? 0.80576 0.47781 0.73624 -0.04640 0.31247  -0.04017 266 ARG A CD  
1738 N NE  . ARG A 266 ? 0.88513 0.48907 0.73264 -0.03503 0.32092  -0.02054 266 ARG A NE  
1739 C CZ  . ARG A 266 ? 0.95260 0.51180 0.77190 -0.03916 0.36320  -0.01289 266 ARG A CZ  
1740 N NH1 . ARG A 266 ? 0.91839 0.49482 0.78915 -0.05579 0.40291  -0.02418 266 ARG A NH1 
1741 N NH2 . ARG A 266 ? 0.95222 0.44663 0.68919 -0.02605 0.36581  0.00594  266 ARG A NH2 
1742 N N   . ASP A 267 ? 0.69492 0.38089 0.58665 -0.02205 0.16402  -0.00894 267 ASP A N   
1743 C CA  . ASP A 267 ? 0.72198 0.40101 0.61051 -0.02023 0.14674  -0.00079 267 ASP A CA  
1744 C C   . ASP A 267 ? 0.72866 0.36541 0.54539 -0.00095 0.11920  0.01019  267 ASP A C   
1745 O O   . ASP A 267 ? 0.74943 0.36562 0.52287 0.00990  0.11348  0.01091  267 ASP A O   
1746 C CB  . ASP A 267 ? 0.73487 0.38809 0.62702 -0.02757 0.18340  0.00500  267 ASP A CB  
1747 C CG  . ASP A 267 ? 0.74264 0.40287 0.65292 -0.02920 0.16636  0.00914  267 ASP A CG  
1748 O OD1 . ASP A 267 ? 0.74028 0.37553 0.65033 -0.03398 0.19275  0.01484  267 ASP A OD1 
1749 O OD2 . ASP A 267 ? 0.82014 0.51005 0.74510 -0.02596 0.12727  0.00616  267 ASP A OD2 
1750 N N   . TYR A 268 ? 0.75845 0.38312 0.56394 0.00418  0.10083  0.01718  268 TYR A N   
1751 C CA  . TYR A 268 ? 0.77730 0.35869 0.51417 0.02420  0.07514  0.02636  268 TYR A CA  
1752 C C   . TYR A 268 ? 0.85053 0.36247 0.50982 0.03715  0.10169  0.03846  268 TYR A C   
1753 O O   . TYR A 268 ? 0.89797 0.37212 0.49304 0.05609  0.08187  0.04418  268 TYR A O   
1754 C CB  . TYR A 268 ? 0.75341 0.33532 0.49758 0.02716  0.05324  0.02988  268 TYR A CB  
1755 C CG  . TYR A 268 ? 0.72175 0.36282 0.52069 0.02062  0.01628  0.01885  268 TYR A CG  
1756 C CD1 . TYR A 268 ? 0.67725 0.34872 0.48768 0.02043  -0.00623 0.01040  268 TYR A CD1 
1757 C CD2 . TYR A 268 ? 0.67769 0.34286 0.51613 0.01428  0.00495  0.01669  268 TYR A CD2 
1758 C CE1 . TYR A 268 ? 0.62123 0.34361 0.47902 0.01329  -0.03749 0.00103  268 TYR A CE1 
1759 C CE2 . TYR A 268 ? 0.63897 0.35760 0.52579 0.00749  -0.02655 0.00637  268 TYR A CE2 
1760 C CZ  . TYR A 268 ? 0.65944 0.40558 0.55477 0.00662  -0.04689 -0.00097 268 TYR A CZ  
1761 O OH  . TYR A 268 ? 0.59428 0.39054 0.53515 -0.00124 -0.07583 -0.01054 268 TYR A OH  
1762 N N   . ILE A 269 ? 0.87578 0.36980 0.53933 0.02737  0.14647  0.04164  269 ILE A N   
1763 C CA  . ILE A 269 ? 0.96378 0.39016 0.55236 0.03782  0.17671  0.05344  269 ILE A CA  
1764 C C   . ILE A 269 ? 0.98254 0.40243 0.53759 0.04629  0.17452  0.04917  269 ILE A C   
1765 O O   . ILE A 269 ? 1.04895 0.41745 0.52659 0.06513  0.16825  0.05778  269 ILE A O   
1766 C CB  . ILE A 269 ? 0.98192 0.39607 0.59205 0.02197  0.22812  0.05545  269 ILE A CB  
1767 C CG1 . ILE A 269 ? 0.96436 0.38393 0.60826 0.01413  0.22889  0.05905  269 ILE A CG1 
1768 C CG2 . ILE A 269 ? 1.07817 0.41947 0.60755 0.03153  0.26279  0.06828  269 ILE A CG2 
1769 C CD1 . ILE A 269 ? 1.02285 0.38700 0.60088 0.03243  0.21095  0.07428  269 ILE A CD1 
1770 N N   . ASP A 270 ? 0.92620 0.39750 0.53829 0.03360  0.17851  0.03505  270 ASP A N   
1771 C CA  . ASP A 270 ? 0.93986 0.40862 0.52607 0.04122  0.17528  0.02925  270 ASP A CA  
1772 C C   . ASP A 270 ? 0.92160 0.40201 0.49132 0.05469  0.12567  0.02652  270 ASP A C   
1773 O O   . ASP A 270 ? 0.96027 0.41501 0.47859 0.06883  0.11735  0.02660  270 ASP A O   
1774 C CB  . ASP A 270 ? 0.88718 0.40648 0.54089 0.02460  0.19372  0.01388  270 ASP A CB  
1775 C CG  . ASP A 270 ? 0.91404 0.41917 0.57995 0.01231  0.24620  0.01332  270 ASP A CG  
1776 O OD1 . ASP A 270 ? 0.98881 0.43469 0.59338 0.01883  0.27259  0.02591  270 ASP A OD1 
1777 O OD2 . ASP A 270 ? 0.87815 0.43062 0.61473 -0.00372 0.26123  -0.00039 270 ASP A OD2 
1778 N N   . GLN A 271 ? 0.86443 0.38356 0.47793 0.05016  0.09328  0.02300  271 GLN A N   
1779 C CA  . GLN A 271 ? 0.84195 0.37764 0.44933 0.05991  0.04753  0.01811  271 GLN A CA  
1780 C C   . GLN A 271 ? 0.90933 0.39036 0.43774 0.08253  0.02882  0.02722  271 GLN A C   
1781 O O   . GLN A 271 ? 0.93065 0.39912 0.42180 0.09600  0.00814  0.02389  271 GLN A O   
1782 C CB  . GLN A 271 ? 0.76851 0.35753 0.44164 0.04827  0.02126  0.01193  271 GLN A CB  
1783 C CG  . GLN A 271 ? 0.72192 0.34942 0.41930 0.04814  -0.01580 0.00169  271 GLN A CG  
1784 C CD  . GLN A 271 ? 0.65366 0.33218 0.41350 0.03559  -0.03839 -0.00407 271 GLN A CD  
1785 O OE1 . GLN A 271 ? 0.61467 0.32370 0.42680 0.02039  -0.02144 -0.00637 271 GLN A OE1 
1786 N NE2 . GLN A 271 ? 0.64010 0.32880 0.39563 0.04177  -0.07636 -0.00767 271 GLN A NE2 
1787 N N   . TRP A 272 ? 0.94535 0.39264 0.44726 0.08798  0.03446  0.03790  272 TRP A N   
1788 C CA  . TRP A 272 ? 1.01432 0.40692 0.43865 0.11176  0.01519  0.04616  272 TRP A CA  
1789 C C   . TRP A 272 ? 1.09148 0.43001 0.44088 0.12585  0.03591  0.05216  272 TRP A C   
1790 O O   . TRP A 272 ? 1.14098 0.44421 0.42764 0.14744  0.01231  0.05379  272 TRP A O   
1791 C CB  . TRP A 272 ? 1.04298 0.40599 0.45258 0.11502  0.02069  0.05698  272 TRP A CB  
1792 C CG  . TRP A 272 ? 1.12141 0.42323 0.44714 0.14155  0.00176  0.06571  272 TRP A CG  
1793 C CD1 . TRP A 272 ? 1.21092 0.44223 0.46043 0.15496  0.02675  0.08029  272 TRP A CD1 
1794 C CD2 . TRP A 272 ? 1.12079 0.42546 0.42927 0.15871  -0.04660 0.05937  272 TRP A CD2 
1795 N NE1 . TRP A 272 ? 1.26726 0.45627 0.45055 0.18110  -0.00494 0.08382  272 TRP A NE1 
1796 C CE2 . TRP A 272 ? 1.21186 0.44656 0.43240 0.18390  -0.05063 0.06999  272 TRP A CE2 
1797 C CE3 . TRP A 272 ? 1.05451 0.41340 0.41339 0.15506  -0.08620 0.04502  272 TRP A CE3 
1798 C CZ2 . TRP A 272 ? 1.23624 0.45635 0.42098 0.20657  -0.09485 0.06493  272 TRP A CZ2 
1799 C CZ3 . TRP A 272 ? 1.07771 0.42286 0.40349 0.17554  -0.12767 0.03988  272 TRP A CZ3 
1800 C CH2 . TRP A 272 ? 1.16670 0.44433 0.40765 0.20158  -0.13274 0.04892  272 TRP A CH2 
1801 N N   . ASN A 273 ? 1.10383 0.43614 0.45939 0.11426  0.07979  0.05399  273 ASN A N   
1802 C CA  . ASN A 273 ? 1.17404 0.45986 0.46285 0.12568  0.10227  0.05782  273 ASN A CA  
1803 C C   . ASN A 273 ? 1.15727 0.46328 0.44164 0.13390  0.07479  0.04606  273 ASN A C   
1804 O O   . ASN A 273 ? 1.21692 0.48158 0.43077 0.15484  0.06132  0.04848  273 ASN A O   
1805 C CB  . ASN A 273 ? 1.18008 0.46577 0.49073 0.10840  0.15520  0.05827  273 ASN A CB  
1806 C CG  . ASN A 273 ? 1.23317 0.47260 0.51614 0.10571  0.18977  0.07284  273 ASN A CG  
1807 O OD1 . ASN A 273 ? 1.27085 0.47360 0.51194 0.11874  0.17374  0.08386  273 ASN A OD1 
1808 N ND2 . ASN A 273 ? 1.23820 0.47850 0.54557 0.08888  0.23748  0.07202  273 ASN A ND2 
1809 N N   . LYS A 274 ? 1.07829 0.44666 0.43671 0.11830  0.06510  0.03288  274 LYS A N   
1810 C CA  . LYS A 274 ? 1.05954 0.44837 0.41941 0.12438  0.03940  0.02131  274 LYS A CA  
1811 C C   . LYS A 274 ? 1.06439 0.44758 0.39772 0.14097  -0.00878 0.01924  274 LYS A C   
1812 O O   . LYS A 274 ? 1.07526 0.45595 0.38547 0.15204  -0.02960 0.01155  274 LYS A O   
1813 C CB  . LYS A 274 ? 0.97490 0.42984 0.42039 0.10425  0.03722  0.00872  274 LYS A CB  
1814 C CG  . LYS A 274 ? 0.96586 0.43295 0.44497 0.08857  0.08200  0.00616  274 LYS A CG  
1815 C CD  . LYS A 274 ? 1.01732 0.45544 0.45222 0.09677  0.10479  0.00319  274 LYS A CD  
1816 C CE  . LYS A 274 ? 0.99230 0.45796 0.47768 0.07991  0.14245  -0.00567 274 LYS A CE  
1817 N NZ  . LYS A 274 ? 1.03700 0.48076 0.48574 0.08741  0.16275  -0.01152 274 LYS A NZ  
1818 N N   . VAL A 275 ? 1.05714 0.43911 0.39545 0.14308  -0.02708 0.02426  275 VAL A N   
1819 C CA  . VAL A 275 ? 1.06389 0.44122 0.37959 0.15928  -0.07269 0.02005  275 VAL A CA  
1820 C C   . VAL A 275 ? 1.15709 0.46740 0.37805 0.18605  -0.07614 0.02696  275 VAL A C   
1821 O O   . VAL A 275 ? 1.17791 0.47901 0.36634 0.20197  -0.10428 0.01913  275 VAL A O   
1822 C CB  . VAL A 275 ? 1.02444 0.42545 0.38050 0.15282  -0.09117 0.02100  275 VAL A CB  
1823 C CG1 . VAL A 275 ? 1.05128 0.43432 0.37095 0.17341  -0.13355 0.01739  275 VAL A CG1 
1824 C CG2 . VAL A 275 ? 0.93178 0.40227 0.37722 0.12961  -0.09886 0.01116  275 VAL A CG2 
1825 N N   . ILE A 276 ? 1.21759 0.47845 0.39148 0.19177  -0.04748 0.04143  276 ILE A N   
1826 C CA  . ILE A 276 ? 1.31367 0.50547 0.39081 0.21869  -0.05043 0.04956  276 ILE A CA  
1827 C C   . ILE A 276 ? 1.36025 0.52571 0.39087 0.22512  -0.02787 0.04879  276 ILE A C   
1828 O O   . ILE A 276 ? 1.41408 0.55017 0.39493 0.24505  -0.04093 0.04406  276 ILE A O   
1829 C CB  . ILE A 276 ? 1.36917 0.51156 0.40692 0.22309  -0.02715 0.06655  276 ILE A CB  
1830 C CG1 . ILE A 276 ? 1.35613 0.50439 0.42695 0.19990  0.02503  0.07384  276 ILE A CG1 
1831 C CG2 . ILE A 276 ? 1.33336 0.49905 0.40886 0.22292  -0.05793 0.06322  276 ILE A CG2 
1832 C CD1 . ILE A 276 ? 1.41805 0.51206 0.44704 0.20286  0.05336  0.09120  276 ILE A CD1 
1833 N N   . GLU A 277 ? 1.32826 0.51947 0.40043 0.20508  0.00731  0.04652  277 GLU A N   
1834 C CA  . GLU A 277 ? 1.36684 0.53921 0.40233 0.21009  0.02839  0.04308  277 GLU A CA  
1835 C C   . GLU A 277 ? 1.34505 0.54107 0.38440 0.21966  -0.00908 0.02788  277 GLU A C   
1836 O O   . GLU A 277 ? 1.45067 0.62265 0.44422 0.23073  -0.00080 0.02421  277 GLU A O   
1837 C CB  . GLU A 277 ? 1.33046 0.53222 0.42014 0.18592  0.07186  0.04061  277 GLU A CB  
1838 C CG  . GLU A 277 ? 1.37303 0.53958 0.44456 0.17765  0.11952  0.05453  277 GLU A CG  
1839 C CD  . GLU A 277 ? 1.32857 0.53273 0.46588 0.15280  0.15923  0.04804  277 GLU A CD  
1840 O OE1 . GLU A 277 ? 1.35545 0.53793 0.49061 0.14235  0.20072  0.05680  277 GLU A OE1 
1841 O OE2 . GLU A 277 ? 1.26864 0.52328 0.46027 0.14408  0.14858  0.03334  277 GLU A OE2 
1842 N N   . GLN A 278 ? 1.27922 0.52106 0.37224 0.21514  -0.04884 0.01843  278 GLN A N   
1843 C CA  . GLN A 278 ? 1.25473 0.52111 0.35853 0.22190  -0.08528 0.00331  278 GLN A CA  
1844 C C   . GLN A 278 ? 1.26222 0.52698 0.36092 0.23738  -0.12693 -0.00327 278 GLN A C   
1845 O O   . GLN A 278 ? 1.28770 0.54490 0.37206 0.25112  -0.14182 -0.01281 278 GLN A O   
1846 C CB  . GLN A 278 ? 1.15922 0.49427 0.35653 0.19804  -0.09261 -0.00703 278 GLN A CB  
1847 C CG  . GLN A 278 ? 1.13859 0.49191 0.36785 0.18190  -0.05468 -0.00886 278 GLN A CG  
1848 C CD  . GLN A 278 ? 1.04820 0.46535 0.36873 0.15835  -0.05877 -0.01611 278 GLN A CD  
1849 O OE1 . GLN A 278 ? 1.01128 0.45944 0.36424 0.15373  -0.07327 -0.02757 278 GLN A OE1 
1850 N NE2 . GLN A 278 ? 1.01495 0.45027 0.37567 0.14398  -0.04624 -0.00953 278 GLN A NE2 
1851 N N   . LEU A 279 ? 1.23228 0.51343 0.36253 0.23236  -0.14207 -0.00134 279 LEU A N   
1852 C CA  . LEU A 279 ? 1.22775 0.52041 0.37758 0.24204  -0.17525 -0.01274 279 LEU A CA  
1853 C C   . LEU A 279 ? 1.30624 0.54640 0.39593 0.26181  -0.16868 -0.00734 279 LEU A C   
1854 O O   . LEU A 279 ? 1.32641 0.56250 0.41192 0.27610  -0.19220 -0.01846 279 LEU A O   
1855 C CB  . LEU A 279 ? 1.15999 0.49721 0.37385 0.22745  -0.19443 -0.01616 279 LEU A CB  
1856 C CG  . LEU A 279 ? 1.07907 0.47294 0.36046 0.20730  -0.20567 -0.02362 279 LEU A CG  
1857 C CD1 . LEU A 279 ? 1.01830 0.45607 0.36396 0.19494  -0.22629 -0.02954 279 LEU A CD1 
1858 C CD2 . LEU A 279 ? 1.06824 0.47920 0.36517 0.20981  -0.21926 -0.03686 279 LEU A CD2 
1859 N N   . GLY A 280 ? 1.35280 0.55190 0.39722 0.26255  -0.13584 0.00920  280 GLY A N   
1860 C CA  . GLY A 280 ? 1.43159 0.57804 0.41716 0.28020  -0.12685 0.01526  280 GLY A CA  
1861 C C   . GLY A 280 ? 1.42851 0.57053 0.42302 0.27685  -0.12734 0.02248  280 GLY A C   
1862 O O   . GLY A 280 ? 1.36240 0.54740 0.41431 0.26425  -0.14527 0.01847  280 GLY A O   
1863 N N   . THR A 281 ? 1.50357 0.59208 0.44042 0.28829  -0.10674 0.03311  281 THR A N   
1864 C CA  . THR A 281 ? 1.51194 0.58957 0.45035 0.28747  -0.10636 0.04011  281 THR A CA  
1865 C C   . THR A 281 ? 1.48843 0.59200 0.45618 0.29652  -0.15026 0.02364  281 THR A C   
1866 O O   . THR A 281 ? 1.52105 0.61358 0.46755 0.31395  -0.17096 0.01131  281 THR A O   
1867 C CB  . THR A 281 ? 1.60590 0.61748 0.47260 0.29970  -0.07686 0.05307  281 THR A CB  
1868 O OG1 . THR A 281 ? 1.62025 0.61232 0.47248 0.28607  -0.03022 0.06844  281 THR A OG1 
1869 C CG2 . THR A 281 ? 1.62213 0.62029 0.48674 0.30305  -0.08362 0.05741  281 THR A CG2 
1870 N N   . PRO A 282 ? 1.43310 0.57128 0.45181 0.28512  -0.16421 0.02219  282 PRO A N   
1871 C CA  . PRO A 282 ? 1.42958 0.59566 0.48222 0.29176  -0.20323 0.00473  282 PRO A CA  
1872 C C   . PRO A 282 ? 1.52971 0.64893 0.52877 0.31432  -0.21114 0.00268  282 PRO A C   
1873 O O   . PRO A 282 ? 1.55497 0.62184 0.49504 0.32242  -0.18618 0.01692  282 PRO A O   
1874 C CB  . PRO A 282 ? 1.34232 0.54966 0.45562 0.27334  -0.20835 0.00709  282 PRO A CB  
1875 C CG  . PRO A 282 ? 1.35485 0.53586 0.44734 0.26349  -0.17008 0.02894  282 PRO A CG  
1876 C CD  . PRO A 282 ? 1.38891 0.54401 0.44149 0.26495  -0.14383 0.03566  282 PRO A CD  
1877 N N   . CYS A 283 ? 1.61573 0.75391 0.63767 0.32411  -0.24536 -0.01589 283 CYS A N   
1878 C CA  . CYS A 283 ? 1.67545 0.77277 0.65077 0.34768  -0.25934 -0.02195 283 CYS A CA  
1879 C C   . CYS A 283 ? 1.68570 0.77201 0.65941 0.34707  -0.25900 -0.01536 283 CYS A C   
1880 O O   . CYS A 283 ? 1.60248 0.72519 0.62710 0.32827  -0.25661 -0.01116 283 CYS A O   
1881 C CB  . CYS A 283 ? 1.63090 0.75476 0.63814 0.35737  -0.29447 -0.04514 283 CYS A CB  
1882 S SG  . CYS A 283 ? 1.85518 1.02215 0.92794 0.35197  -0.32411 -0.06042 283 CYS A SG  
1883 N N   . PRO A 284 ? 1.63889 0.67383 0.55371 0.36815  -0.26168 -0.01421 284 PRO A N   
1884 C CA  . PRO A 284 ? 1.65537 0.67517 0.56429 0.36832  -0.25979 -0.00652 284 PRO A CA  
1885 C C   . PRO A 284 ? 1.59439 0.66449 0.57143 0.36117  -0.28953 -0.02157 284 PRO A C   
1886 O O   . PRO A 284 ? 1.60280 0.67946 0.59878 0.35217  -0.28462 -0.01345 284 PRO A O   
1887 C CB  . PRO A 284 ? 1.76125 0.71565 0.59126 0.39560  -0.26216 -0.00624 284 PRO A CB  
1888 C CG  . PRO A 284 ? 1.78409 0.73359 0.59697 0.41099  -0.27805 -0.02099 284 PRO A CG  
1889 C CD  . PRO A 284 ? 1.72567 0.70946 0.57201 0.39296  -0.26356 -0.01771 284 PRO A CD  
1890 N N   . GLU A 285 ? 1.55439 0.65949 0.57093 0.36465  -0.31848 -0.04331 285 GLU A N   
1891 C CA  . GLU A 285 ? 1.51728 0.67253 0.60395 0.35572  -0.34293 -0.05843 285 GLU A CA  
1892 C C   . GLU A 285 ? 1.46022 0.66505 0.60949 0.32792  -0.33116 -0.05039 285 GLU A C   
1893 O O   . GLU A 285 ? 1.45261 0.68269 0.64257 0.31914  -0.33886 -0.05242 285 GLU A O   
1894 C CB  . GLU A 285 ? 1.50657 0.69035 0.62832 0.36215  -0.36939 -0.08168 285 GLU A CB  
1895 N N   . PHE A 286 ? 1.41065 0.62910 0.56788 0.31469  -0.31299 -0.04181 286 PHE A N   
1896 C CA  . PHE A 286 ? 1.39421 0.65205 0.60170 0.29007  -0.29924 -0.03209 286 PHE A CA  
1897 C C   . PHE A 286 ? 1.39800 0.62319 0.57529 0.28688  -0.27327 -0.01018 286 PHE A C   
1898 O O   . PHE A 286 ? 1.33261 0.58723 0.55576 0.27052  -0.26865 -0.00426 286 PHE A O   
1899 C CB  . PHE A 286 ? 1.28764 0.56419 0.50693 0.27904  -0.28742 -0.02967 286 PHE A CB  
1900 C CG  . PHE A 286 ? 1.20605 0.51455 0.46642 0.25596  -0.27063 -0.01807 286 PHE A CG  
1901 C CD1 . PHE A 286 ? 1.23406 0.50923 0.45819 0.25211  -0.23799 0.00339  286 PHE A CD1 
1902 C CD2 . PHE A 286 ? 1.12131 0.49184 0.45806 0.23780  -0.28494 -0.02868 286 PHE A CD2 
1903 C CE1 . PHE A 286 ? 1.17893 0.48062 0.44234 0.23218  -0.22230 0.01363  286 PHE A CE1 
1904 C CE2 . PHE A 286 ? 1.06662 0.46536 0.43997 0.21803  -0.27161 -0.01890 286 PHE A CE2 
1905 C CZ  . PHE A 286 ? 1.09570 0.45905 0.43208 0.21618  -0.24158 0.00226  286 PHE A CZ  
1906 N N   . MET A 287 ? 1.45954 0.62331 0.56244 0.30193  -0.25426 0.00217  287 MET A N   
1907 C CA  . MET A 287 ? 1.49504 0.62257 0.56919 0.29805  -0.22350 0.02414  287 MET A CA  
1908 C C   . MET A 287 ? 1.50493 0.63956 0.60330 0.29829  -0.23701 0.02285  287 MET A C   
1909 O O   . MET A 287 ? 1.43920 0.58844 0.57250 0.28277  -0.22229 0.03419  287 MET A O   
1910 C CB  . MET A 287 ? 1.54881 0.60750 0.53759 0.31540  -0.20197 0.03475  287 MET A CB  
1911 C CG  . MET A 287 ? 1.57855 0.62109 0.53954 0.31092  -0.17330 0.04374  287 MET A CG  
1912 S SD  . MET A 287 ? 1.48100 0.56619 0.50119 0.28177  -0.14847 0.05429  287 MET A SD  
1913 C CE  . MET A 287 ? 1.55064 0.58107 0.50602 0.28227  -0.09999 0.07128  287 MET A CE  
1914 N N   . LYS A 288 ? 1.69945 0.82323 0.78168 0.31641  -0.26518 0.00801  288 LYS A N   
1915 C CA  . LYS A 288 ? 1.66629 0.79078 0.76405 0.31969  -0.27887 0.00574  288 LYS A CA  
1916 C C   . LYS A 288 ? 1.59504 0.78508 0.77868 0.30103  -0.29426 -0.00356 288 LYS A C   
1917 O O   . LYS A 288 ? 1.63909 0.83415 0.84463 0.29867  -0.29859 -0.00152 288 LYS A O   
1918 C CB  . LYS A 288 ? 1.70192 0.80147 0.76491 0.34425  -0.30752 -0.01126 288 LYS A CB  
1919 C CG  . LYS A 288 ? 1.69220 0.83838 0.80494 0.34616  -0.34210 -0.03878 288 LYS A CG  
1920 C CD  . LYS A 288 ? 1.67885 0.86632 0.85380 0.33941  -0.36406 -0.05203 288 LYS A CD  
1921 C CE  . LYS A 288 ? 1.68308 0.90770 0.90274 0.34323  -0.39362 -0.07955 288 LYS A CE  
1922 N NZ  . LYS A 288 ? 1.69878 0.93271 0.94347 0.35047  -0.41689 -0.09493 288 LYS A NZ  
1923 N N   . LYS A 289 ? 1.45541 0.69510 0.68858 0.28781  -0.30222 -0.01402 289 LYS A N   
1924 C CA  . LYS A 289 ? 1.38592 0.68867 0.70107 0.26883  -0.31463 -0.02313 289 LYS A CA  
1925 C C   . LYS A 289 ? 1.30118 0.61414 0.64205 0.25044  -0.28957 -0.00407 289 LYS A C   
1926 O O   . LYS A 289 ? 1.22387 0.58763 0.63231 0.23451  -0.29836 -0.01031 289 LYS A O   
1927 C CB  . LYS A 289 ? 1.35086 0.70140 0.71116 0.26024  -0.32907 -0.04057 289 LYS A CB  
1928 C CG  . LYS A 289 ? 1.39334 0.76494 0.78151 0.26875  -0.35787 -0.06511 289 LYS A CG  
1929 C CD  . LYS A 289 ? 1.41909 0.80166 0.83512 0.26957  -0.37117 -0.07187 289 LYS A CD  
1930 C CE  . LYS A 289 ? 1.43218 0.84572 0.89249 0.27351  -0.39526 -0.09674 289 LYS A CE  
1931 N NZ  . LYS A 289 ? 1.48804 0.86094 0.89733 0.29836  -0.40912 -0.10685 289 LYS A NZ  
1932 N N   . LEU A 290 ? 1.35570 0.62124 0.64780 0.25168  -0.25652 0.01784  290 LEU A N   
1933 C CA  . LEU A 290 ? 1.29975 0.56719 0.61730 0.23425  -0.22660 0.03571  290 LEU A CA  
1934 C C   . LEU A 290 ? 1.28243 0.52717 0.60176 0.23517  -0.21692 0.04519  290 LEU A C   
1935 O O   . LEU A 290 ? 1.27987 0.49125 0.55879 0.25169  -0.22586 0.04390  290 LEU A O   
1936 C CB  . LEU A 290 ? 1.27240 0.50047 0.54345 0.23184  -0.18908 0.05261  290 LEU A CB  
1937 C CG  . LEU A 290 ? 1.24314 0.49309 0.51729 0.22773  -0.19192 0.04639  290 LEU A CG  
1938 C CD1 . LEU A 290 ? 1.28959 0.48703 0.49096 0.23809  -0.16678 0.05594  290 LEU A CD1 
1939 C CD2 . LEU A 290 ? 1.17185 0.45797 0.50350 0.20587  -0.17847 0.05126  290 LEU A CD2 
1940 N N   . GLN A 291 ? 1.23305 0.49529 0.60191 0.21714  -0.19838 0.05355  291 GLN A N   
1941 C CA  . GLN A 291 ? 1.23499 0.47224 0.60845 0.21497  -0.18105 0.06393  291 GLN A CA  
1942 C C   . GLN A 291 ? 1.27932 0.45014 0.58388 0.22028  -0.14277 0.08288  291 GLN A C   
1943 O O   . GLN A 291 ? 1.29959 0.45251 0.57440 0.21655  -0.11816 0.09064  291 GLN A O   
1944 C CB  . GLN A 291 ? 1.21180 0.48137 0.65727 0.19257  -0.16568 0.06588  291 GLN A CB  
1945 C CG  . GLN A 291 ? 1.20363 0.54534 0.72468 0.18453  -0.20135 0.04568  291 GLN A CG  
1946 C CD  . GLN A 291 ? 1.26898 0.61623 0.80323 0.19610  -0.23049 0.03600  291 GLN A CD  
1947 O OE1 . GLN A 291 ? 1.22201 0.53596 0.74405 0.19896  -0.21532 0.04495  291 GLN A OE1 
1948 N NE2 . GLN A 291 ? 1.27469 0.67018 0.83877 0.19984  -0.26937 0.01531  291 GLN A NE2 
1949 N N   . PRO A 292 ? 1.33211 0.46601 0.61090 0.22867  -0.13677 0.08982  292 PRO A N   
1950 C CA  . PRO A 292 ? 1.42264 0.49151 0.62995 0.23544  -0.10322 0.10625  292 PRO A CA  
1951 C C   . PRO A 292 ? 1.42170 0.47675 0.63447 0.21544  -0.05295 0.12069  292 PRO A C   
1952 O O   . PRO A 292 ? 1.48434 0.49811 0.63877 0.21954  -0.02696 0.12985  292 PRO A O   
1953 C CB  . PRO A 292 ? 1.46245 0.50410 0.66086 0.24347  -0.10676 0.11028  292 PRO A CB  
1954 C CG  . PRO A 292 ? 1.38090 0.47532 0.65949 0.23344  -0.12818 0.09943  292 PRO A CG  
1955 C CD  . PRO A 292 ? 1.31401 0.46321 0.62766 0.23218  -0.15970 0.08249  292 PRO A CD  
1956 N N   . THR A 293 ? 1.35336 0.44257 0.63638 0.19355  -0.03769 0.12063  293 THR A N   
1957 C CA  . THR A 293 ? 1.34823 0.42989 0.64509 0.17237  0.01166  0.13035  293 THR A CA  
1958 C C   . THR A 293 ? 1.33428 0.42748 0.61836 0.16984  0.01679  0.12795  293 THR A C   
1959 O O   . THR A 293 ? 1.38481 0.44450 0.62497 0.16833  0.05027  0.13671  293 THR A O   
1960 C CB  . THR A 293 ? 1.27466 0.39468 0.65564 0.14951  0.02403  0.12621  293 THR A CB  
1961 O OG1 . THR A 293 ? 1.29648 0.39942 0.68588 0.15086  0.02639  0.12986  293 THR A OG1 
1962 C CG2 . THR A 293 ? 1.25967 0.38310 0.66564 0.12569  0.07393  0.13097  293 THR A CG2 
1963 N N   . VAL A 294 ? 1.26740 0.40805 0.58998 0.16935  -0.01630 0.11522  294 VAL A N   
1964 C CA  . VAL A 294 ? 1.26831 0.42182 0.58207 0.16726  -0.01471 0.11215  294 VAL A CA  
1965 C C   . VAL A 294 ? 1.31679 0.43974 0.55531 0.18955  -0.02969 0.11163  294 VAL A C   
1966 O O   . VAL A 294 ? 1.33229 0.44627 0.54351 0.18936  -0.01530 0.11319  294 VAL A O   
1967 C CB  . VAL A 294 ? 1.14885 0.38766 0.54332 0.15465  -0.04577 0.09252  294 VAL A CB  
1968 C CG1 . VAL A 294 ? 1.14711 0.39358 0.52986 0.17520  -0.09890 0.08241  294 VAL A CG1 
1969 C CG2 . VAL A 294 ? 1.11696 0.38644 0.52454 0.14407  -0.03535 0.08699  294 VAL A CG2 
1970 N N   . ARG A 295 ? 1.35730 0.46344 0.56266 0.20893  -0.05776 0.10765  295 ARG A N   
1971 C CA  . ARG A 295 ? 1.42583 0.49874 0.55970 0.23043  -0.07005 0.10460  295 ARG A CA  
1972 C C   . ARG A 295 ? 1.50687 0.52107 0.57800 0.23188  -0.02613 0.11960  295 ARG A C   
1973 O O   . ARG A 295 ? 1.54905 0.54114 0.57081 0.24166  -0.02136 0.11847  295 ARG A O   
1974 C CB  . ARG A 295 ? 1.45366 0.51974 0.57013 0.24986  -0.10718 0.09512  295 ARG A CB  
1975 C CG  . ARG A 295 ? 1.54954 0.56062 0.58320 0.27263  -0.10867 0.09579  295 ARG A CG  
1976 C CD  . ARG A 295 ? 1.55144 0.57815 0.57960 0.29168  -0.15657 0.07543  295 ARG A CD  
1977 N NE  . ARG A 295 ? 1.50850 0.56992 0.58874 0.28978  -0.18450 0.06606  295 ARG A NE  
1978 C CZ  . ARG A 295 ? 1.54537 0.58847 0.60469 0.30662  -0.20777 0.05859  295 ARG A CZ  
1979 N NH1 . ARG A 295 ? 1.63530 0.62423 0.62134 0.32758  -0.20826 0.05948  295 ARG A NH1 
1980 N NH2 . ARG A 295 ? 1.49667 0.57578 0.60964 0.30291  -0.23132 0.04906  295 ARG A NH2 
1981 N N   . ASN A 296 ? 1.52951 0.51899 0.60460 0.22141  0.00738  0.13237  296 ASN A N   
1982 C CA  . ASN A 296 ? 1.60837 0.54305 0.62757 0.22079  0.05190  0.14545  296 ASN A CA  
1983 C C   . ASN A 296 ? 1.58970 0.53296 0.61879 0.20494  0.08655  0.14786  296 ASN A C   
1984 O O   . ASN A 296 ? 1.65111 0.55802 0.62275 0.21239  0.10640  0.15117  296 ASN A O   
1985 C CB  . ASN A 296 ? 1.63120 0.54318 0.66205 0.21078  0.07958  0.15639  296 ASN A CB  
1986 C CG  . ASN A 296 ? 1.69918 0.56404 0.68975 0.20309  0.13275  0.16849  296 ASN A CG  
1987 O OD1 . ASN A 296 ? 1.66746 0.54815 0.69833 0.18035  0.17060  0.17111  296 ASN A OD1 
1988 N ND2 . ASN A 296 ? 1.79470 0.60192 0.70723 0.22193  0.13630  0.17411  296 ASN A ND2 
1989 N N   . TYR A 297 ? 1.50724 0.49753 0.60942 0.18340  0.09451  0.14501  297 TYR A N   
1990 C CA  . TYR A 297 ? 1.48645 0.48772 0.60406 0.16738  0.12776  0.14560  297 TYR A CA  
1991 C C   . TYR A 297 ? 1.48993 0.49614 0.57453 0.18077  0.10557  0.13852  297 TYR A C   
1992 O O   . TYR A 297 ? 1.52735 0.51128 0.57687 0.18008  0.13358  0.14119  297 TYR A O   
1993 C CB  . TYR A 297 ? 1.39506 0.44807 0.60175 0.14286  0.13562  0.14096  297 TYR A CB  
1994 C CG  . TYR A 297 ? 1.35286 0.43540 0.58729 0.12948  0.15119  0.13506  297 TYR A CG  
1995 C CD1 . TYR A 297 ? 1.27855 0.42469 0.55798 0.12866  0.11340  0.11903  297 TYR A CD1 
1996 C CD2 . TYR A 297 ? 1.37869 0.44436 0.60810 0.11522  0.20222  0.13940  297 TYR A CD2 
1997 C CE1 . TYR A 297 ? 1.26823 0.45741 0.58399 0.11538  0.12450  0.10867  297 TYR A CE1 
1998 C CE2 . TYR A 297 ? 1.33085 0.44280 0.59961 0.10209  0.21320  0.12732  297 TYR A CE2 
1999 C CZ  . TYR A 297 ? 1.29742 0.46989 0.60802 0.10290  0.17338  0.11247  297 TYR A CZ  
2000 O OH  . TYR A 297 ? 1.26095 0.47656 0.60895 0.09109  0.18291  0.10066  297 TYR A OH  
2001 N N   . VAL A 298 ? 1.45101 0.48832 0.54943 0.19255  0.05559  0.12770  298 VAL A N   
2002 C CA  . VAL A 298 ? 1.44589 0.49535 0.52343 0.20358  0.03198  0.11825  298 VAL A CA  
2003 C C   . VAL A 298 ? 1.53551 0.53570 0.53150 0.22613  0.03003  0.11818  298 VAL A C   
2004 O O   . VAL A 298 ? 1.56116 0.54887 0.52363 0.23142  0.03862  0.11595  298 VAL A O   
2005 C CB  . VAL A 298 ? 1.37582 0.47774 0.50040 0.20715  -0.01959 0.10385  298 VAL A CB  
2006 C CG1 . VAL A 298 ? 1.41779 0.52325 0.50897 0.22540  -0.05228 0.09083  298 VAL A CG1 
2007 C CG2 . VAL A 298 ? 1.28834 0.44094 0.48762 0.18520  -0.01582 0.10071  298 VAL A CG2 
2008 N N   . GLU A 299 ? 1.58722 0.55662 0.54994 0.24020  0.01931  0.12008  299 GLU A N   
2009 C CA  . GLU A 299 ? 1.67998 0.59623 0.56353 0.26224  0.01955  0.12021  299 GLU A CA  
2010 C C   . GLU A 299 ? 1.74601 0.61401 0.58441 0.25699  0.07175  0.13323  299 GLU A C   
2011 O O   . GLU A 299 ? 1.81595 0.64423 0.59143 0.27297  0.07657  0.13230  299 GLU A O   
2012 C CB  . GLU A 299 ? 1.72247 0.61474 0.58204 0.27803  -0.00270 0.11947  299 GLU A CB  
2013 C CG  . GLU A 299 ? 1.69505 0.61743 0.56893 0.29352  -0.05694 0.10116  299 GLU A CG  
2014 C CD  . GLU A 299 ? 1.71516 0.62709 0.58700 0.30365  -0.07860 0.09944  299 GLU A CD  
2015 O OE1 . GLU A 299 ? 1.74666 0.62931 0.60826 0.29807  -0.05259 0.11370  299 GLU A OE1 
2016 O OE2 . GLU A 299 ? 1.69966 0.63323 0.58286 0.31662  -0.12091 0.08267  299 GLU A OE2 
2017 N N   . ASN A 300 ? 1.72607 0.59741 0.59847 0.23461  0.11159  0.14360  300 ASN A N   
2018 C CA  . ASN A 300 ? 1.78434 0.61510 0.62432 0.22612  0.16487  0.15350  300 ASN A CA  
2019 C C   . ASN A 300 ? 1.75860 0.60703 0.61136 0.21493  0.18712  0.15020  300 ASN A C   
2020 O O   . ASN A 300 ? 1.79999 0.62135 0.63457 0.20552  0.23342  0.15576  300 ASN A O   
2021 C CB  . ASN A 300 ? 1.77573 0.60432 0.65296 0.20581  0.19973  0.16293  300 ASN A CB  
2022 C CG  . ASN A 300 ? 1.86283 0.63510 0.68609 0.21740  0.21011  0.17180  300 ASN A CG  
2023 O OD1 . ASN A 300 ? 1.89214 0.64866 0.68299 0.23805  0.17365  0.16981  300 ASN A OD1 
2024 N ND2 . ASN A 300 ? 1.90625 0.64816 0.72124 0.20394  0.26026  0.18033  300 ASN A ND2 
2025 N N   . ARG A 301 ? 1.69282 0.58617 0.57794 0.21535  0.15579  0.14040  301 ARG A N   
2026 C CA  . ARG A 301 ? 1.68872 0.59804 0.58184 0.20729  0.17220  0.13648  301 ARG A CA  
2027 C C   . ARG A 301 ? 1.74093 0.61504 0.56432 0.22876  0.16543  0.13224  301 ARG A C   
2028 O O   . ARG A 301 ? 1.78249 0.63398 0.56383 0.25091  0.13460  0.12861  301 ARG A O   
2029 C CB  . ARG A 301 ? 1.62807 0.59752 0.58284 0.19960  0.13992  0.12779  301 ARG A CB  
2030 C CG  . ARG A 301 ? 1.54083 0.54642 0.57143 0.17319  0.16030  0.13100  301 ARG A CG  
2031 C CD  . ARG A 301 ? 1.57267 0.57605 0.61704 0.15359  0.21309  0.13362  301 ARG A CD  
2032 N NE  . ARG A 301 ? 1.57363 0.59304 0.67706 0.12983  0.24777  0.13568  301 ARG A NE  
2033 C CZ  . ARG A 301 ? 1.49735 0.56209 0.67002 0.10520  0.27975  0.12555  301 ARG A CZ  
2034 N NH1 . ARG A 301 ? 1.44489 0.54312 0.63704 0.10072  0.28243  0.11326  301 ARG A NH1 
2035 N NH2 . ARG A 301 ? 1.44341 0.52027 0.66817 0.08535  0.30882  0.12651  301 ARG A NH2 
2036 N N   . PRO A 302 ? 1.93111 0.80015 0.74345 0.22267  0.19459  0.13137  302 PRO A N   
2037 C CA  . PRO A 302 ? 1.89324 0.73048 0.64349 0.24298  0.18782  0.12658  302 PRO A CA  
2038 C C   . PRO A 302 ? 1.88705 0.75184 0.64018 0.26022  0.13201  0.11350  302 PRO A C   
2039 O O   . PRO A 302 ? 1.79351 0.71030 0.60154 0.25156  0.10707  0.10662  302 PRO A O   
2040 C CB  . PRO A 302 ? 1.85458 0.69772 0.61378 0.22808  0.22800  0.12607  302 PRO A CB  
2041 C CG  . PRO A 302 ? 1.86263 0.71894 0.67116 0.20147  0.26931  0.13286  302 PRO A CG  
2042 C CD  . PRO A 302 ? 1.88995 0.77892 0.74622 0.19667  0.23932  0.13393  302 PRO A CD  
2043 N N   . LYS A 303 ? 1.84872 0.67808 0.54463 0.28443  0.11302  0.10911  303 LYS A N   
2044 C CA  . LYS A 303 ? 1.82616 0.67932 0.52672 0.30151  0.06146  0.09402  303 LYS A CA  
2045 C C   . LYS A 303 ? 1.80385 0.67812 0.51097 0.30132  0.05843  0.08538  303 LYS A C   
2046 O O   . LYS A 303 ? 1.85593 0.69888 0.52360 0.30382  0.08832  0.08935  303 LYS A O   
2047 C CB  . LYS A 303 ? 1.90808 0.71449 0.54750 0.32784  0.04330  0.09137  303 LYS A CB  
2048 C CG  . LYS A 303 ? 1.93105 0.71827 0.56278 0.33110  0.03841  0.09741  303 LYS A CG  
2049 C CD  . LYS A 303 ? 1.87527 0.70408 0.54905 0.33686  -0.01202 0.08386  303 LYS A CD  
2050 C CE  . LYS A 303 ? 1.86248 0.69325 0.55690 0.32959  -0.01214 0.09105  303 LYS A CE  
2051 N NZ  . LYS A 303 ? 1.85243 0.69814 0.55832 0.34430  -0.05883 0.07757  303 LYS A NZ  
2052 N N   . TYR A 304 ? 1.72733 0.65537 0.48600 0.29787  0.02244  0.07299  304 TYR A N   
2053 C CA  . TYR A 304 ? 1.69986 0.65342 0.47087 0.29824  0.01255  0.06266  304 TYR A CA  
2054 C C   . TYR A 304 ? 1.69020 0.66133 0.46846 0.31589  -0.03690 0.04589  304 TYR A C   
2055 O O   . TYR A 304 ? 1.65452 0.65028 0.46569 0.31711  -0.06855 0.03888  304 TYR A O   
2056 C CB  . TYR A 304 ? 1.61386 0.61916 0.44650 0.27527  0.01725  0.06167  304 TYR A CB  
2057 C CG  . TYR A 304 ? 1.61879 0.61213 0.45220 0.25596  0.06992  0.07507  304 TYR A CG  
2058 C CD1 . TYR A 304 ? 1.64689 0.62668 0.45804 0.25220  0.10399  0.07531  304 TYR A CD1 
2059 C CD2 . TYR A 304 ? 1.59349 0.59214 0.45655 0.24031  0.08699  0.08568  304 TYR A CD2 
2060 C CE1 . TYR A 304 ? 1.64865 0.62289 0.47010 0.23230  0.15540  0.08382  304 TYR A CE1 
2061 C CE2 . TYR A 304 ? 1.60795 0.59897 0.48177 0.22055  0.13793  0.09568  304 TYR A CE2 
2062 C CZ  . TYR A 304 ? 1.63192 0.61213 0.48630 0.21607  0.17282  0.09372  304 TYR A CZ  
2063 O OH  . TYR A 304 ? 1.66212 0.64251 0.53938 0.19426  0.22546  0.09889  304 TYR A OH  
2064 N N   . ALA A 305 ? 1.72229 0.68178 0.47320 0.32879  -0.04190 0.03868  305 ALA A N   
2065 C CA  . ALA A 305 ? 1.71154 0.68974 0.47550 0.34409  -0.08556 0.02161  305 ALA A CA  
2066 C C   . ALA A 305 ? 1.61893 0.66211 0.45639 0.33019  -0.11228 0.00906  305 ALA A C   
2067 O O   . ALA A 305 ? 1.58982 0.65913 0.45886 0.33669  -0.14923 -0.00533 305 ALA A O   
2068 C CB  . ALA A 305 ? 1.77696 0.72194 0.48981 0.36229  -0.08164 0.01842  305 ALA A CB  
2069 N N   . GLY A 306 ? 1.56959 0.63869 0.43581 0.31081  -0.09307 0.01353  306 GLY A N   
2070 C CA  . GLY A 306 ? 1.48467 0.61289 0.41775 0.29720  -0.11670 0.00202  306 GLY A CA  
2071 C C   . GLY A 306 ? 1.48612 0.62591 0.42108 0.30358  -0.12819 -0.00959 306 GLY A C   
2072 O O   . GLY A 306 ? 1.60748 0.72352 0.51035 0.32273  -0.14053 -0.01552 306 GLY A O   
2073 N N   . LEU A 307 ? 1.44277 0.61840 0.41476 0.28818  -0.12460 -0.01347 307 LEU A N   
2074 C CA  . LEU A 307 ? 1.42671 0.61694 0.40616 0.29246  -0.13557 -0.02510 307 LEU A CA  
2075 C C   . LEU A 307 ? 1.42578 0.65666 0.46059 0.29303  -0.17719 -0.04042 307 LEU A C   
2076 O O   . LEU A 307 ? 1.37162 0.63741 0.45848 0.28084  -0.19368 -0.04331 307 LEU A O   
2077 C CB  . LEU A 307 ? 1.41194 0.62468 0.41033 0.27579  -0.11508 -0.02577 307 LEU A CB  
2078 C CG  . LEU A 307 ? 1.46292 0.64164 0.41220 0.27463  -0.06896 -0.01736 307 LEU A CG  
2079 C CD1 . LEU A 307 ? 1.57472 0.70401 0.47276 0.27999  -0.03946 -0.00077 307 LEU A CD1 
2080 C CD2 . LEU A 307 ? 1.39677 0.60682 0.38093 0.25370  -0.04862 -0.02132 307 LEU A CD2 
2081 N N   . THR A 308 ? 1.40221 0.62854 0.42705 0.30654  -0.19179 -0.05033 308 THR A N   
2082 C CA  . THR A 308 ? 1.35347 0.61652 0.43145 0.30622  -0.22613 -0.06520 308 THR A CA  
2083 C C   . THR A 308 ? 1.27320 0.58832 0.41776 0.28447  -0.23275 -0.07090 308 THR A C   
2084 O O   . THR A 308 ? 1.26797 0.58812 0.41063 0.27408  -0.21384 -0.06665 308 THR A O   
2085 C CB  . THR A 308 ? 1.40116 0.64488 0.45064 0.32613  -0.23796 -0.07413 308 THR A CB  
2086 O OG1 . THR A 308 ? 1.40960 0.68355 0.50760 0.32701  -0.26892 -0.08814 308 THR A OG1 
2087 C CG2 . THR A 308 ? 1.40252 0.64939 0.44390 0.32380  -0.22599 -0.07589 308 THR A CG2 
2088 N N   . PHE A 309 ? 1.23149 0.58475 0.43532 0.27733  -0.25818 -0.08118 309 PHE A N   
2089 C CA  . PHE A 309 ? 1.17657 0.57961 0.44805 0.25532  -0.26461 -0.08560 309 PHE A CA  
2090 C C   . PHE A 309 ? 1.18538 0.59816 0.46429 0.25430  -0.26523 -0.09228 309 PHE A C   
2091 O O   . PHE A 309 ? 1.16627 0.60569 0.47796 0.23785  -0.25951 -0.09212 309 PHE A O   
2092 C CB  . PHE A 309 ? 1.09982 0.53824 0.43074 0.24720  -0.28644 -0.09355 309 PHE A CB  
2093 C CG  . PHE A 309 ? 1.06547 0.51986 0.42159 0.23462  -0.28372 -0.08735 309 PHE A CG  
2094 C CD1 . PHE A 309 ? 1.00309 0.49379 0.40637 0.21242  -0.27801 -0.08388 309 PHE A CD1 
2095 C CD2 . PHE A 309 ? 1.09863 0.53071 0.43011 0.24582  -0.28721 -0.08536 309 PHE A CD2 
2096 C CE1 . PHE A 309 ? 0.97253 0.47879 0.39945 0.20126  -0.27581 -0.07844 309 PHE A CE1 
2097 C CE2 . PHE A 309 ? 1.06840 0.51522 0.42324 0.23470  -0.28516 -0.08011 309 PHE A CE2 
2098 C CZ  . PHE A 309 ? 1.00455 0.48919 0.40761 0.21227  -0.27934 -0.07651 309 PHE A CZ  
2099 N N   . PRO A 310 ? 1.22471 0.61742 0.47550 0.27159  -0.27291 -0.09907 310 PRO A N   
2100 C CA  . PRO A 310 ? 1.22240 0.61830 0.47020 0.27213  -0.26956 -0.10432 310 PRO A CA  
2101 C C   . PRO A 310 ? 1.25725 0.63141 0.46190 0.27180  -0.24172 -0.09678 310 PRO A C   
2102 O O   . PRO A 310 ? 1.23273 0.61862 0.44704 0.26664  -0.23667 -0.10202 310 PRO A O   
2103 C CB  . PRO A 310 ? 1.23723 0.61011 0.45489 0.29368  -0.28262 -0.11226 310 PRO A CB  
2104 C CG  . PRO A 310 ? 1.27497 0.62310 0.46485 0.30685  -0.28764 -0.10936 310 PRO A CG  
2105 C CD  . PRO A 310 ? 1.22462 0.60055 0.45995 0.28940  -0.29010 -0.10568 310 PRO A CD  
2106 N N   . LYS A 311 ? 1.36730 0.70943 0.52517 0.27675  -0.22135 -0.08539 311 LYS A N   
2107 C CA  . LYS A 311 ? 1.37115 0.69319 0.49093 0.27345  -0.18811 -0.07832 311 LYS A CA  
2108 C C   . LYS A 311 ? 1.37229 0.72097 0.52830 0.25233  -0.17777 -0.07508 311 LYS A C   
2109 O O   . LYS A 311 ? 1.38693 0.74203 0.54451 0.24344  -0.15780 -0.07858 311 LYS A O   
2110 C CB  . LYS A 311 ? 1.46907 0.73893 0.51787 0.28831  -0.16516 -0.06647 311 LYS A CB  
2111 C CG  . LYS A 311 ? 1.57530 0.81614 0.57444 0.29159  -0.12882 -0.06303 311 LYS A CG  
2112 C CD  . LYS A 311 ? 1.68623 0.87539 0.61668 0.31197  -0.11655 -0.05532 311 LYS A CD  
2113 C CE  . LYS A 311 ? 1.75101 0.90627 0.63408 0.30876  -0.06874 -0.04444 311 LYS A CE  
2114 N NZ  . LYS A 311 ? 1.75575 0.87287 0.58150 0.32557  -0.05432 -0.04347 311 LYS A NZ  
2115 N N   . LEU A 312 ? 1.25675 0.62185 0.44376 0.24434  -0.19028 -0.07058 312 LEU A N   
2116 C CA  . LEU A 312 ? 1.17725 0.57130 0.40335 0.22418  -0.18443 -0.06845 312 LEU A CA  
2117 C C   . LEU A 312 ? 1.13153 0.57210 0.42181 0.20956  -0.20150 -0.07962 312 LEU A C   
2118 O O   . LEU A 312 ? 1.08763 0.54865 0.40334 0.19431  -0.19226 -0.08182 312 LEU A O   
2119 C CB  . LEU A 312 ? 1.14532 0.54775 0.39208 0.21965  -0.19529 -0.06148 312 LEU A CB  
2120 C CG  . LEU A 312 ? 1.18654 0.54530 0.37673 0.22864  -0.17356 -0.04779 312 LEU A CG  
2121 C CD1 . LEU A 312 ? 1.14503 0.51586 0.36266 0.22611  -0.19080 -0.04472 312 LEU A CD1 
2122 C CD2 . LEU A 312 ? 1.16690 0.51646 0.34243 0.21737  -0.13575 -0.03985 312 LEU A CD2 
2123 N N   . PHE A 313 ? 1.13174 0.58764 0.44895 0.21382  -0.22460 -0.08746 313 PHE A N   
2124 C CA  . PHE A 313 ? 1.08913 0.58530 0.46664 0.20043  -0.23910 -0.09619 313 PHE A CA  
2125 C C   . PHE A 313 ? 1.12156 0.60783 0.48561 0.21306  -0.24729 -0.10470 313 PHE A C   
2126 O O   . PHE A 313 ? 1.11805 0.61279 0.50316 0.21723  -0.26620 -0.10944 313 PHE A O   
2127 C CB  . PHE A 313 ? 1.02576 0.55915 0.46677 0.18689  -0.25745 -0.09614 313 PHE A CB  
2128 C CG  . PHE A 313 ? 0.99683 0.54050 0.45162 0.17588  -0.25144 -0.08808 313 PHE A CG  
2129 C CD1 . PHE A 313 ? 0.87856 0.44761 0.36580 0.15844  -0.24443 -0.08658 313 PHE A CD1 
2130 C CD2 . PHE A 313 ? 0.95522 0.48274 0.39085 0.18370  -0.25365 -0.08311 313 PHE A CD2 
2131 C CE1 . PHE A 313 ? 0.85979 0.43897 0.36045 0.14855  -0.23979 -0.07976 313 PHE A CE1 
2132 C CE2 . PHE A 313 ? 0.94926 0.48604 0.39800 0.17401  -0.24873 -0.07595 313 PHE A CE2 
2133 C CZ  . PHE A 313 ? 0.88617 0.44922 0.36743 0.15626  -0.24178 -0.07393 313 PHE A CZ  
2134 N N   . PRO A 314 ? 1.13161 0.59978 0.46068 0.21936  -0.23149 -0.10833 314 PRO A N   
2135 C CA  . PRO A 314 ? 1.16856 0.62656 0.48232 0.23233  -0.23884 -0.11674 314 PRO A CA  
2136 C C   . PRO A 314 ? 1.13826 0.63166 0.51313 0.22236  -0.26006 -0.12487 314 PRO A C   
2137 O O   . PRO A 314 ? 1.08804 0.61381 0.51557 0.20421  -0.26452 -0.12402 314 PRO A O   
2138 C CB  . PRO A 314 ? 1.18738 0.62571 0.46137 0.23622  -0.21198 -0.12000 314 PRO A CB  
2139 C CG  . PRO A 314 ? 1.19420 0.61718 0.44254 0.23120  -0.18615 -0.11119 314 PRO A CG  
2140 C CD  . PRO A 314 ? 1.15399 0.60727 0.45279 0.21578  -0.20198 -0.10647 314 PRO A CD  
2141 N N   . ASP A 315 ? 1.17761 0.66270 0.54349 0.23468  -0.27175 -0.13232 315 ASP A N   
2142 C CA  . ASP A 315 ? 1.11240 0.62477 0.53022 0.22687  -0.28958 -0.13974 315 ASP A CA  
2143 C C   . ASP A 315 ? 1.07612 0.60676 0.52054 0.21533  -0.28410 -0.14390 315 ASP A C   
2144 O O   . ASP A 315 ? 1.06804 0.62520 0.56414 0.20299  -0.29542 -0.14609 315 ASP A O   
2145 C CB  . ASP A 315 ? 1.26857 0.76433 0.66519 0.24441  -0.30211 -0.14793 315 ASP A CB  
2146 C CG  . ASP A 315 ? 1.31955 0.82035 0.73533 0.24717  -0.31921 -0.14948 315 ASP A CG  
2147 O OD1 . ASP A 315 ? 1.36558 0.84030 0.74048 0.26482  -0.32217 -0.15017 315 ASP A OD1 
2148 O OD2 . ASP A 315 ? 1.29532 0.82535 0.76604 0.23187  -0.32834 -0.15046 315 ASP A OD2 
2149 N N   . SER A 316 ? 1.10835 0.62408 0.51849 0.21906  -0.26478 -0.14573 316 SER A N   
2150 C CA  . SER A 316 ? 1.09244 0.62494 0.52885 0.20953  -0.25885 -0.15285 316 SER A CA  
2151 C C   . SER A 316 ? 1.05607 0.61918 0.54431 0.18906  -0.26021 -0.14812 316 SER A C   
2152 O O   . SER A 316 ? 1.01830 0.60097 0.54262 0.17973  -0.26200 -0.15341 316 SER A O   
2153 C CB  . SER A 316 ? 1.12842 0.63779 0.51841 0.21780  -0.23168 -0.15866 316 SER A CB  
2154 O OG  . SER A 316 ? 1.19326 0.69364 0.56467 0.21298  -0.21079 -0.15218 316 SER A OG  
2155 N N   . LEU A 317 ? 1.05616 0.62386 0.54956 0.18245  -0.25954 -0.13837 317 LEU A N   
2156 C CA  . LEU A 317 ? 1.00263 0.60106 0.54601 0.16292  -0.26078 -0.13299 317 LEU A CA  
2157 C C   . LEU A 317 ? 0.98944 0.61468 0.58601 0.15178  -0.27724 -0.12875 317 LEU A C   
2158 O O   . LEU A 317 ? 0.92322 0.57569 0.56360 0.13492  -0.27666 -0.12306 317 LEU A O   
2159 C CB  . LEU A 317 ? 0.98322 0.57384 0.50657 0.16056  -0.24933 -0.12520 317 LEU A CB  
2160 C CG  . LEU A 317 ? 0.99213 0.55300 0.46196 0.16852  -0.22368 -0.12882 317 LEU A CG  
2161 C CD1 . LEU A 317 ? 0.95415 0.50120 0.39891 0.16812  -0.21358 -0.11898 317 LEU A CD1 
2162 C CD2 . LEU A 317 ? 0.92748 0.50972 0.43471 0.15686  -0.20691 -0.13466 317 LEU A CD2 
2163 N N   . PHE A 318 ? 1.05142 0.66877 0.64408 0.16059  -0.28909 -0.13219 318 PHE A N   
2164 C CA  . PHE A 318 ? 1.01491 0.65304 0.65193 0.15055  -0.30009 -0.13040 318 PHE A CA  
2165 C C   . PHE A 318 ? 1.06013 0.70119 0.71457 0.15114  -0.30879 -0.13709 318 PHE A C   
2166 O O   . PHE A 318 ? 1.06529 0.68682 0.68906 0.16548  -0.31113 -0.14480 318 PHE A O   
2167 C CB  . PHE A 318 ? 1.04983 0.67690 0.67140 0.15987  -0.30754 -0.13079 318 PHE A CB  
2168 C CG  . PHE A 318 ? 1.06844 0.69940 0.68863 0.15538  -0.30182 -0.12334 318 PHE A CG  
2169 C CD1 . PHE A 318 ? 0.98149 0.64233 0.64839 0.13707  -0.30007 -0.11760 318 PHE A CD1 
2170 C CD2 . PHE A 318 ? 1.07215 0.67518 0.64175 0.17000  -0.29692 -0.12167 318 PHE A CD2 
2171 C CE1 . PHE A 318 ? 1.01645 0.68186 0.68356 0.13335  -0.29541 -0.11162 318 PHE A CE1 
2172 C CE2 . PHE A 318 ? 1.08135 0.68577 0.64887 0.16660  -0.29245 -0.11485 318 PHE A CE2 
2173 C CZ  . PHE A 318 ? 1.07344 0.71042 0.69179 0.14821  -0.29271 -0.11049 318 PHE A CZ  
2174 N N   . PRO A 319 ? 0.99500 0.65867 0.69572 0.13606  -0.31236 -0.13413 319 PRO A N   
2175 C CA  . PRO A 319 ? 0.99621 0.65858 0.71085 0.13756  -0.32211 -0.14012 319 PRO A CA  
2176 C C   . PRO A 319 ? 1.01866 0.66284 0.70935 0.15322  -0.33331 -0.14814 319 PRO A C   
2177 O O   . PRO A 319 ? 0.96321 0.61215 0.66361 0.15165  -0.33836 -0.14779 319 PRO A O   
2178 C CB  . PRO A 319 ? 0.90776 0.59445 0.66899 0.11849  -0.32145 -0.13341 319 PRO A CB  
2179 C CG  . PRO A 319 ? 0.88963 0.59183 0.66125 0.10828  -0.31201 -0.12485 319 PRO A CG  
2180 C CD  . PRO A 319 ? 0.93221 0.62227 0.67142 0.11702  -0.30553 -0.12481 319 PRO A CD  
2181 N N   . ALA A 320 ? 1.15630 0.78025 0.81511 0.16922  -0.33705 -0.15642 320 ALA A N   
2182 C CA  . ALA A 320 ? 1.19959 0.80414 0.82972 0.18693  -0.34731 -0.16470 320 ALA A CA  
2183 C C   . ALA A 320 ? 1.30556 0.90241 0.93390 0.19470  -0.35541 -0.17405 320 ALA A C   
2184 O O   . ALA A 320 ? 1.33043 0.90899 0.92181 0.21012  -0.35426 -0.18050 320 ALA A O   
2185 C CB  . ALA A 320 ? 1.18058 0.76230 0.75825 0.20296  -0.34100 -0.16458 320 ALA A CB  
2186 N N   . ASP A 321 ? 1.46396 1.07425 1.13144 0.18380  -0.36274 -0.17477 321 ASP A N   
2187 C CA  . ASP A 321 ? 1.48742 1.09085 1.15818 0.19022  -0.37249 -0.18366 321 ASP A CA  
2188 C C   . ASP A 321 ? 1.45313 1.05675 1.13973 0.19184  -0.38659 -0.18978 321 ASP A C   
2189 O O   . ASP A 321 ? 1.48326 1.07490 1.15833 0.20438  -0.39684 -0.19992 321 ASP A O   
2190 C CB  . ASP A 321 ? 1.41344 1.02852 1.11414 0.17709  -0.36905 -0.18002 321 ASP A CB  
2191 C CG  . ASP A 321 ? 1.45374 1.07688 1.15312 0.16981  -0.35485 -0.17275 321 ASP A CG  
2192 O OD1 . ASP A 321 ? 1.50234 1.11426 1.16745 0.18101  -0.34805 -0.17651 321 ASP A OD1 
2193 O OD2 . ASP A 321 ? 1.57417 1.21465 1.30546 0.15300  -0.34968 -0.16376 321 ASP A OD2 
2194 N N   . SER A 322 ? 1.19999 0.81786 0.91284 0.17965  -0.38710 -0.18496 322 SER A N   
2195 C CA  . SER A 322 ? 1.10839 0.72881 0.83788 0.18016  -0.39956 -0.19188 322 SER A CA  
2196 C C   . SER A 322 ? 1.05410 0.67257 0.76938 0.18826  -0.40242 -0.19421 322 SER A C   
2197 O O   . SER A 322 ? 1.00571 0.62033 0.69930 0.19192  -0.39424 -0.18886 322 SER A O   
2198 C CB  . SER A 322 ? 1.01605 0.65539 0.78871 0.15906  -0.39791 -0.18598 322 SER A CB  
2199 O OG  . SER A 322 ? 0.96142 0.60994 0.75068 0.15544  -0.40414 -0.18969 322 SER A OG  
2200 N N   . GLU A 323 ? 1.06961 0.69005 0.79738 0.19165  -0.41491 -0.20303 323 GLU A N   
2201 C CA  . GLU A 323 ? 1.08533 0.70450 0.80301 0.20041  -0.41997 -0.20701 323 GLU A CA  
2202 C C   . GLU A 323 ? 1.04727 0.68724 0.79086 0.18312  -0.41086 -0.19792 323 GLU A C   
2203 O O   . GLU A 323 ? 1.05274 0.69042 0.78096 0.18862  -0.40819 -0.19567 323 GLU A O   
2204 C CB  . GLU A 323 ? 1.11169 0.72837 0.83716 0.21003  -0.43707 -0.22119 323 GLU A CB  
2205 C CG  . GLU A 323 ? 1.15425 0.75500 0.84707 0.23256  -0.44686 -0.23003 323 GLU A CG  
2206 C CD  . GLU A 323 ? 1.19868 0.77484 0.84955 0.25395  -0.45187 -0.23635 323 GLU A CD  
2207 O OE1 . GLU A 323 ? 1.20723 0.78090 0.86478 0.25586  -0.45846 -0.24303 323 GLU A OE1 
2208 O OE2 . GLU A 323 ? 1.22737 0.78594 0.83705 0.26900  -0.44882 -0.23459 323 GLU A OE2 
2209 N N   . HIS A 324 ? 0.92160 0.58100 0.70275 0.16272  -0.40595 -0.19264 324 HIS A N   
2210 C CA  . HIS A 324 ? 0.89686 0.57776 0.70205 0.14543  -0.39537 -0.18343 324 HIS A CA  
2211 C C   . HIS A 324 ? 0.82979 0.51042 0.62025 0.14262  -0.38151 -0.17213 324 HIS A C   
2212 O O   . HIS A 324 ? 0.80430 0.49426 0.59707 0.13865  -0.37544 -0.16729 324 HIS A O   
2213 C CB  . HIS A 324 ? 0.83978 0.53777 0.68190 0.12535  -0.39213 -0.17947 324 HIS A CB  
2214 C CG  . HIS A 324 ? 0.80931 0.52495 0.67266 0.10900  -0.38144 -0.16908 324 HIS A CG  
2215 N ND1 . HIS A 324 ? 0.78278 0.50493 0.64708 0.09862  -0.36684 -0.15667 324 HIS A ND1 
2216 C CD2 . HIS A 324 ? 0.78836 0.51752 0.67327 0.10170  -0.38335 -0.17019 324 HIS A CD2 
2217 C CE1 . HIS A 324 ? 0.73804 0.47624 0.62246 0.08589  -0.36025 -0.15004 324 HIS A CE1 
2218 N NE2 . HIS A 324 ? 0.77197 0.51486 0.66890 0.08719  -0.36966 -0.15794 324 HIS A NE2 
2219 N N   . ASN A 325 ? 0.83198 0.50234 0.60786 0.14499  -0.37682 -0.16878 325 ASN A N   
2220 C CA  . ASN A 325 ? 0.84220 0.51190 0.60342 0.14306  -0.36418 -0.15972 325 ASN A CA  
2221 C C   . ASN A 325 ? 0.87391 0.52458 0.59443 0.16115  -0.36569 -0.16260 325 ASN A C   
2222 O O   . ASN A 325 ? 0.87281 0.52525 0.58374 0.15867  -0.35618 -0.15535 325 ASN A O   
2223 C CB  . ASN A 325 ? 0.91695 0.58149 0.67470 0.14150  -0.35970 -0.15743 325 ASN A CB  
2224 C CG  . ASN A 325 ? 0.83432 0.51865 0.62795 0.12119  -0.35185 -0.14874 325 ASN A CG  
2225 O OD1 . ASN A 325 ? 0.73039 0.43262 0.55029 0.10760  -0.34871 -0.14414 325 ASN A OD1 
2226 N ND2 . ASN A 325 ? 0.87909 0.55992 0.67240 0.11991  -0.34859 -0.14694 325 ASN A ND2 
2227 N N   . LYS A 326 ? 0.91656 0.54766 0.61098 0.17996  -0.37751 -0.17300 326 LYS A N   
2228 C CA  . LYS A 326 ? 0.91865 0.52791 0.56911 0.19903  -0.37922 -0.17542 326 LYS A CA  
2229 C C   . LYS A 326 ? 0.91367 0.52981 0.57124 0.19801  -0.38111 -0.17426 326 LYS A C   
2230 O O   . LYS A 326 ? 0.92745 0.53221 0.55765 0.20488  -0.37574 -0.16971 326 LYS A O   
2231 C CB  . LYS A 326 ? 0.96761 0.55531 0.58946 0.22000  -0.39206 -0.18727 326 LYS A CB  
2232 C CG  . LYS A 326 ? 0.99074 0.56258 0.58393 0.22879  -0.38807 -0.18868 326 LYS A CG  
2233 C CD  . LYS A 326 ? 1.02768 0.58624 0.60770 0.24491  -0.40213 -0.20134 326 LYS A CD  
2234 C CE  . LYS A 326 ? 1.07073 0.60529 0.60136 0.26242  -0.39789 -0.20406 326 LYS A CE  
2235 N NZ  . LYS A 326 ? 1.10082 0.64119 0.63791 0.25285  -0.38706 -0.20024 326 LYS A NZ  
2236 N N   . LEU A 327 ? 0.89652 0.53047 0.58964 0.18983  -0.38854 -0.17878 327 LEU A N   
2237 C CA  . LEU A 327 ? 0.89186 0.53459 0.59493 0.18912  -0.39120 -0.17954 327 LEU A CA  
2238 C C   . LEU A 327 ? 0.85074 0.51150 0.57138 0.17191  -0.37662 -0.16729 327 LEU A C   
2239 O O   . LEU A 327 ? 0.85790 0.51373 0.56379 0.17706  -0.37462 -0.16463 327 LEU A O   
2240 C CB  . LEU A 327 ? 0.88453 0.54363 0.62228 0.18387  -0.40179 -0.18854 327 LEU A CB  
2241 C CG  . LEU A 327 ? 0.87290 0.54700 0.63161 0.17962  -0.40446 -0.19040 327 LEU A CG  
2242 C CD1 . LEU A 327 ? 0.91220 0.56702 0.63714 0.20072  -0.41262 -0.19604 327 LEU A CD1 
2243 C CD2 . LEU A 327 ? 0.87128 0.55787 0.66582 0.17510  -0.41699 -0.20108 327 LEU A CD2 
2244 N N   . LYS A 328 ? 0.80966 0.49037 0.56076 0.15221  -0.36671 -0.15990 328 LYS A N   
2245 C CA  . LYS A 328 ? 0.78196 0.48193 0.55174 0.13572  -0.35275 -0.14862 328 LYS A CA  
2246 C C   . LYS A 328 ? 0.77996 0.46477 0.51740 0.14261  -0.34487 -0.14237 328 LYS A C   
2247 O O   . LYS A 328 ? 0.79347 0.48740 0.53562 0.13623  -0.33716 -0.13571 328 LYS A O   
2248 C CB  . LYS A 328 ? 0.75944 0.47979 0.56245 0.11597  -0.34414 -0.14221 328 LYS A CB  
2249 C CG  . LYS A 328 ? 0.77424 0.50638 0.60853 0.10813  -0.35207 -0.14751 328 LYS A CG  
2250 C CD  . LYS A 328 ? 0.76842 0.52091 0.63240 0.09362  -0.34709 -0.14240 328 LYS A CD  
2251 C CE  . LYS A 328 ? 0.89417 0.65217 0.77845 0.09418  -0.35976 -0.15246 328 LYS A CE  
2252 N NZ  . LYS A 328 ? 0.84481 0.62272 0.76299 0.07553  -0.35481 -0.14814 328 LYS A NZ  
2253 N N   . ALA A 329 ? 0.81108 0.47263 0.51452 0.15569  -0.34624 -0.14477 329 ALA A N   
2254 C CA  . ALA A 329 ? 0.82874 0.47262 0.49524 0.16354  -0.33798 -0.13959 329 ALA A CA  
2255 C C   . ALA A 329 ? 0.87637 0.50225 0.51186 0.17800  -0.34178 -0.14074 329 ALA A C   
2256 O O   . ALA A 329 ? 0.89036 0.51008 0.50843 0.17797  -0.33313 -0.13371 329 ALA A O   
2257 C CB  . ALA A 329 ? 0.89768 0.51970 0.53095 0.17581  -0.33797 -0.14328 329 ALA A CB  
2258 N N   . SER A 330 ? 0.89158 0.50759 0.51909 0.19124  -0.35529 -0.15000 330 SER A N   
2259 C CA  . SER A 330 ? 0.92606 0.52388 0.52505 0.20648  -0.36089 -0.15213 330 SER A CA  
2260 C C   . SER A 330 ? 0.89215 0.51333 0.52572 0.19416  -0.36027 -0.14958 330 SER A C   
2261 O O   . SER A 330 ? 0.90715 0.51683 0.52026 0.20078  -0.35872 -0.14641 330 SER A O   
2262 C CB  . SER A 330 ? 0.97197 0.55140 0.55092 0.22657  -0.37697 -0.16439 330 SER A CB  
2263 O OG  . SER A 330 ? 0.94872 0.55154 0.57144 0.21822  -0.38666 -0.17202 330 SER A OG  
2264 N N   . GLN A 331 ? 0.84974 0.50218 0.53304 0.17676  -0.36071 -0.15077 331 GLN A N   
2265 C CA  . GLN A 331 ? 0.81579 0.49307 0.53248 0.16370  -0.35753 -0.14791 331 GLN A CA  
2266 C C   . GLN A 331 ? 0.79748 0.48542 0.52008 0.15035  -0.34228 -0.13571 331 GLN A C   
2267 O O   . GLN A 331 ? 0.77586 0.46914 0.50197 0.14864  -0.33994 -0.13274 331 GLN A O   
2268 C CB  . GLN A 331 ? 0.80043 0.50607 0.56353 0.14847  -0.35944 -0.15150 331 GLN A CB  
2269 C CG  . GLN A 331 ? 0.81528 0.51047 0.57615 0.16085  -0.37566 -0.16462 331 GLN A CG  
2270 C CD  . GLN A 331 ? 0.83052 0.54512 0.63378 0.15048  -0.38288 -0.17104 331 GLN A CD  
2271 O OE1 . GLN A 331 ? 0.80291 0.53354 0.63188 0.13326  -0.37488 -0.16512 331 GLN A OE1 
2272 N NE2 . GLN A 331 ? 0.85438 0.56712 0.66411 0.16143  -0.39808 -0.18366 331 GLN A NE2 
2273 N N   . ALA A 332 ? 0.80884 0.50017 0.53354 0.14145  -0.33266 -0.12945 332 ALA A N   
2274 C CA  . ALA A 332 ? 0.76789 0.46808 0.49650 0.13045  -0.31915 -0.11910 332 ALA A CA  
2275 C C   . ALA A 332 ? 0.82265 0.49447 0.50580 0.14539  -0.31824 -0.11677 332 ALA A C   
2276 O O   . ALA A 332 ? 0.81657 0.49467 0.50415 0.14069  -0.31316 -0.11144 332 ALA A O   
2277 C CB  . ALA A 332 ? 0.78385 0.48931 0.51938 0.12161  -0.31133 -0.11514 332 ALA A CB  
2278 N N   . ARG A 333 ? 0.82988 0.46845 0.46601 0.16418  -0.32240 -0.12047 333 ARG A N   
2279 C CA  . ARG A 333 ? 0.88439 0.48981 0.46809 0.18015  -0.31945 -0.11721 333 ARG A CA  
2280 C C   . ARG A 333 ? 0.88647 0.48603 0.46585 0.18831  -0.32758 -0.11972 333 ARG A C   
2281 O O   . ARG A 333 ? 0.90654 0.48814 0.45736 0.19438  -0.32269 -0.11412 333 ARG A O   
2282 C CB  . ARG A 333 ? 0.92676 0.49683 0.45824 0.20011  -0.32126 -0.12107 333 ARG A CB  
2283 C CG  . ARG A 333 ? 0.99736 0.53057 0.46805 0.21376  -0.31026 -0.11417 333 ARG A CG  
2284 C CD  . ARG A 333 ? 1.06492 0.56323 0.48216 0.23398  -0.30983 -0.11780 333 ARG A CD  
2285 N NE  . ARG A 333 ? 1.09100 0.59539 0.51104 0.22798  -0.30213 -0.11830 333 ARG A NE  
2286 C CZ  . ARG A 333 ? 1.12143 0.62720 0.54590 0.23304  -0.31015 -0.12660 333 ARG A CZ  
2287 N NH1 . ARG A 333 ? 1.08086 0.58242 0.50714 0.24410  -0.32589 -0.13511 333 ARG A NH1 
2288 N NH2 . ARG A 333 ? 1.11866 0.62995 0.54601 0.22744  -0.30266 -0.12745 333 ARG A NH2 
2289 N N   . ASP A 334 ? 0.88028 0.49361 0.48674 0.18899  -0.33989 -0.12850 334 ASP A N   
2290 C CA  . ASP A 334 ? 0.89409 0.50452 0.50085 0.19687  -0.34893 -0.13286 334 ASP A CA  
2291 C C   . ASP A 334 ? 0.84732 0.48583 0.49063 0.17925  -0.34137 -0.12650 334 ASP A C   
2292 O O   . ASP A 334 ? 0.88864 0.51627 0.51758 0.18627  -0.34342 -0.12552 334 ASP A O   
2293 C CB  . ASP A 334 ? 0.90009 0.51949 0.52790 0.20208  -0.36384 -0.14523 334 ASP A CB  
2294 C CG  . ASP A 334 ? 0.91465 0.53283 0.54591 0.21097  -0.37458 -0.15183 334 ASP A CG  
2295 O OD1 . ASP A 334 ? 0.97016 0.55503 0.55825 0.23392  -0.38448 -0.15718 334 ASP A OD1 
2296 O OD2 . ASP A 334 ? 0.88300 0.53267 0.55851 0.19575  -0.37278 -0.15189 334 ASP A OD2 
2297 N N   . LEU A 335 ? 0.81045 0.48401 0.49953 0.15705  -0.33244 -0.12216 335 LEU A N   
2298 C CA  . LEU A 335 ? 0.76484 0.46646 0.48806 0.14006  -0.32340 -0.11561 335 LEU A CA  
2299 C C   . LEU A 335 ? 0.77469 0.46273 0.47329 0.14013  -0.31372 -0.10628 335 LEU A C   
2300 O O   . LEU A 335 ? 0.75579 0.45073 0.46218 0.13632  -0.31086 -0.10264 335 LEU A O   
2301 C CB  . LEU A 335 ? 0.75367 0.49300 0.52599 0.11775  -0.31470 -0.11270 335 LEU A CB  
2302 C CG  . LEU A 335 ? 0.72876 0.50121 0.53924 0.09954  -0.30400 -0.10653 335 LEU A CG  
2303 C CD1 . LEU A 335 ? 0.73945 0.51167 0.55820 0.10658  -0.31503 -0.11391 335 LEU A CD1 
2304 C CD2 . LEU A 335 ? 0.69547 0.49119 0.54294 0.08315  -0.29903 -0.10488 335 LEU A CD2 
2305 N N   . LEU A 336 ? 0.77784 0.44609 0.44587 0.14470  -0.30843 -0.10278 336 LEU A N   
2306 C CA  . LEU A 336 ? 0.78649 0.43427 0.42042 0.14811  -0.29919 -0.09465 336 LEU A CA  
2307 C C   . LEU A 336 ? 0.84521 0.45719 0.43217 0.16733  -0.30397 -0.09475 336 LEU A C   
2308 O O   . LEU A 336 ? 0.84416 0.44678 0.41611 0.16687  -0.29736 -0.08770 336 LEU A O   
2309 C CB  . LEU A 336 ? 0.80677 0.43572 0.40967 0.15244  -0.29231 -0.09259 336 LEU A CB  
2310 C CG  . LEU A 336 ? 0.78843 0.44460 0.42492 0.13401  -0.28304 -0.08888 336 LEU A CG  
2311 C CD1 . LEU A 336 ? 0.78752 0.42290 0.39153 0.14182  -0.27922 -0.09053 336 LEU A CD1 
2312 C CD2 . LEU A 336 ? 0.73494 0.40170 0.38091 0.12316  -0.27330 -0.08098 336 LEU A CD2 
2313 N N   . SER A 337 ? 0.88227 0.47260 0.44469 0.18496  -0.31562 -0.10275 337 SER A N   
2314 C CA  . SER A 337 ? 0.93952 0.49207 0.45333 0.20546  -0.32065 -0.10331 337 SER A CA  
2315 C C   . SER A 337 ? 0.92015 0.48889 0.46199 0.20147  -0.32716 -0.10531 337 SER A C   
2316 O O   . SER A 337 ? 0.95211 0.49542 0.46106 0.21131  -0.32602 -0.10126 337 SER A O   
2317 C CB  . SER A 337 ? 0.99062 0.51743 0.47312 0.22614  -0.33269 -0.11269 337 SER A CB  
2318 O OG  . SER A 337 ? 0.97283 0.52249 0.49473 0.22514  -0.34767 -0.12366 337 SER A OG  
2319 N N   . LYS A 338 ? 0.87120 0.48041 0.47135 0.18742  -0.33262 -0.11119 338 LYS A N   
2320 C CA  . LYS A 338 ? 0.85144 0.47896 0.48093 0.18320  -0.33765 -0.11401 338 LYS A CA  
2321 C C   . LYS A 338 ? 0.80588 0.45711 0.46253 0.16496  -0.32534 -0.10459 338 LYS A C   
2322 O O   . LYS A 338 ? 0.80240 0.45740 0.46736 0.16538  -0.32797 -0.10488 338 LYS A O   
2323 C CB  . LYS A 338 ? 0.82215 0.48213 0.49937 0.17580  -0.34550 -0.12366 338 LYS A CB  
2324 C CG  . LYS A 338 ? 0.87049 0.50826 0.52567 0.19682  -0.36245 -0.13607 338 LYS A CG  
2325 C CD  . LYS A 338 ? 0.84281 0.51124 0.54212 0.18795  -0.36774 -0.14471 338 LYS A CD  
2326 C CE  . LYS A 338 ? 0.89217 0.54023 0.57281 0.20979  -0.38640 -0.15876 338 LYS A CE  
2327 N NZ  . LYS A 338 ? 0.94987 0.55419 0.57169 0.23138  -0.39126 -0.15919 338 LYS A NZ  
2328 N N   . MET A 339 ? 0.77270 0.43955 0.44336 0.14997  -0.31290 -0.09714 339 MET A N   
2329 C CA  . MET A 339 ? 0.74543 0.43769 0.44547 0.13236  -0.30159 -0.08909 339 MET A CA  
2330 C C   . MET A 339 ? 0.75783 0.41855 0.41332 0.13937  -0.29507 -0.08048 339 MET A C   
2331 O O   . MET A 339 ? 0.74756 0.41177 0.40887 0.13569  -0.29261 -0.07625 339 MET A O   
2332 C CB  . MET A 339 ? 0.70883 0.43673 0.45086 0.11221  -0.29167 -0.08630 339 MET A CB  
2333 C CG  . MET A 339 ? 0.73975 0.50861 0.53522 0.09745  -0.29015 -0.08975 339 MET A CG  
2334 S SD  . MET A 339 ? 0.69127 0.48972 0.52160 0.08031  -0.28133 -0.08844 339 MET A SD  
2335 C CE  . MET A 339 ? 0.62037 0.40285 0.42720 0.08006  -0.27433 -0.08178 339 MET A CE  
2336 N N   . LEU A 340 ? 0.79692 0.42507 0.40515 0.14989  -0.29091 -0.07750 340 LEU A N   
2337 C CA  . LEU A 340 ? 0.83120 0.42551 0.38989 0.15624  -0.27961 -0.06741 340 LEU A CA  
2338 C C   . LEU A 340 ? 0.90110 0.44676 0.39909 0.17882  -0.28214 -0.06585 340 LEU A C   
2339 O O   . LEU A 340 ? 0.95907 0.46387 0.39990 0.19534  -0.27718 -0.06383 340 LEU A O   
2340 C CB  . LEU A 340 ? 0.84265 0.42474 0.37708 0.15621  -0.26934 -0.06428 340 LEU A CB  
2341 C CG  . LEU A 340 ? 0.78628 0.40359 0.36296 0.13543  -0.26178 -0.06175 340 LEU A CG  
2342 C CD1 . LEU A 340 ? 0.80723 0.40731 0.35340 0.13896  -0.25302 -0.06124 340 LEU A CD1 
2343 C CD2 . LEU A 340 ? 0.77174 0.39203 0.35154 0.12730  -0.25403 -0.05346 340 LEU A CD2 
2344 N N   . VAL A 341 ? 0.89682 0.44690 0.40763 0.17960  -0.28890 -0.06686 341 VAL A N   
2345 C CA  . VAL A 341 ? 0.96163 0.46637 0.41795 0.19998  -0.29132 -0.06491 341 VAL A CA  
2346 C C   . VAL A 341 ? 0.95200 0.45646 0.41220 0.19427  -0.28608 -0.05675 341 VAL A C   
2347 O O   . VAL A 341 ? 0.89132 0.43930 0.41076 0.17729  -0.29028 -0.05944 341 VAL A O   
2348 C CB  . VAL A 341 ? 0.97868 0.48358 0.44288 0.21248  -0.31059 -0.07840 341 VAL A CB  
2349 C CG1 . VAL A 341 ? 1.01537 0.50072 0.45109 0.22591  -0.31471 -0.08426 341 VAL A CG1 
2350 C CG2 . VAL A 341 ? 0.91076 0.47003 0.45058 0.19546  -0.31978 -0.08696 341 VAL A CG2 
2351 N N   . ILE A 342 ? 1.01437 0.46853 0.41079 0.20840  -0.27459 -0.04590 342 ILE A N   
2352 C CA  . ILE A 342 ? 1.01157 0.45902 0.40566 0.20352  -0.26593 -0.03498 342 ILE A CA  
2353 C C   . ILE A 342 ? 0.99747 0.46159 0.42246 0.20531  -0.28455 -0.04444 342 ILE A C   
2354 O O   . ILE A 342 ? 0.95015 0.44503 0.41935 0.19156  -0.28649 -0.04340 342 ILE A O   
2355 C CB  . ILE A 342 ? 1.08825 0.47280 0.40426 0.21759  -0.24216 -0.01824 342 ILE A CB  
2356 C CG1 . ILE A 342 ? 1.10201 0.47086 0.38969 0.21499  -0.21985 -0.00944 342 ILE A CG1 
2357 C CG2 . ILE A 342 ? 1.08688 0.46159 0.40332 0.21203  -0.22966 -0.00451 342 ILE A CG2 
2358 C CD1 . ILE A 342 ? 1.18147 0.48707 0.39355 0.22731  -0.18898 0.00699  342 ILE A CD1 
2359 N N   . ASP A 343 ? 1.03915 0.48332 0.44213 0.22274  -0.29854 -0.05447 343 ASP A N   
2360 C CA  . ASP A 343 ? 1.03485 0.48911 0.46103 0.22722  -0.31570 -0.06426 343 ASP A CA  
2361 C C   . ASP A 343 ? 0.95890 0.47464 0.46607 0.21004  -0.32691 -0.07664 343 ASP A C   
2362 O O   . ASP A 343 ? 0.97133 0.50546 0.49894 0.20793  -0.33142 -0.08447 343 ASP A O   
2363 C CB  . ASP A 343 ? 1.10584 0.51887 0.48317 0.25238  -0.32783 -0.07227 343 ASP A CB  
2364 C CG  . ASP A 343 ? 1.12036 0.52868 0.50325 0.26119  -0.34287 -0.07977 343 ASP A CG  
2365 O OD1 . ASP A 343 ? 1.19285 0.55379 0.51885 0.28315  -0.34802 -0.08076 343 ASP A OD1 
2366 O OD2 . ASP A 343 ? 1.06128 0.51274 0.50483 0.24650  -0.34899 -0.08496 343 ASP A OD2 
2367 N N   . PRO A 344 ? 0.91337 0.46126 0.46739 0.19738  -0.32908 -0.07779 344 PRO A N   
2368 C CA  . PRO A 344 ? 0.86790 0.47332 0.49650 0.18047  -0.33351 -0.08762 344 PRO A CA  
2369 C C   . PRO A 344 ? 0.87977 0.48723 0.51792 0.19234  -0.34930 -0.10223 344 PRO A C   
2370 O O   . PRO A 344 ? 0.87673 0.52099 0.55970 0.18210  -0.34989 -0.10907 344 PRO A O   
2371 C CB  . PRO A 344 ? 0.82196 0.45419 0.48876 0.16662  -0.32938 -0.08411 344 PRO A CB  
2372 C CG  . PRO A 344 ? 0.84168 0.43321 0.45742 0.17335  -0.32214 -0.07069 344 PRO A CG  
2373 C CD  . PRO A 344 ? 0.92193 0.45563 0.46324 0.19688  -0.32428 -0.06860 344 PRO A CD  
2374 N N   . ALA A 345 ? 0.92197 0.48941 0.51728 0.21408  -0.36148 -0.10697 345 ALA A N   
2375 C CA  . ALA A 345 ? 0.94156 0.50935 0.54555 0.22742  -0.37857 -0.12251 345 ALA A CA  
2376 C C   . ALA A 345 ? 0.96662 0.52872 0.55945 0.23466  -0.38280 -0.12833 345 ALA A C   
2377 O O   . ALA A 345 ? 0.95498 0.53823 0.57930 0.23628  -0.39295 -0.14074 345 ALA A O   
2378 C CB  . ALA A 345 ? 1.01031 0.53092 0.56358 0.25126  -0.39122 -0.12641 345 ALA A CB  
2379 N N   . LYS A 346 ? 1.02888 0.56239 0.57694 0.23938  -0.37455 -0.11969 346 LYS A N   
2380 C CA  . LYS A 346 ? 1.03432 0.56323 0.57239 0.24528  -0.37744 -0.12451 346 LYS A CA  
2381 C C   . LYS A 346 ? 1.04175 0.61436 0.62827 0.22193  -0.36621 -0.12088 346 LYS A C   
2382 O O   . LYS A 346 ? 1.02297 0.59902 0.61183 0.22414  -0.36931 -0.12596 346 LYS A O   
2383 C CB  . LYS A 346 ? 1.12164 0.59565 0.58348 0.26357  -0.37270 -0.11739 346 LYS A CB  
2384 C CG  . LYS A 346 ? 1.21992 0.64365 0.62361 0.28977  -0.38324 -0.12111 346 LYS A CG  
2385 C CD  . LYS A 346 ? 1.26700 0.63731 0.59414 0.30213  -0.36879 -0.10761 346 LYS A CD  
2386 C CE  . LYS A 346 ? 1.42486 0.75316 0.70365 0.31686  -0.36924 -0.10294 346 LYS A CE  
2387 N NZ  . LYS A 346 ? 1.36802 0.66572 0.60081 0.31330  -0.34461 -0.08301 346 LYS A NZ  
2388 N N   . ARG A 347 ? 0.93347 0.53835 0.55755 0.20043  -0.35368 -0.11261 347 ARG A N   
2389 C CA  . ARG A 347 ? 0.87911 0.52125 0.54297 0.17886  -0.34146 -0.10790 347 ARG A CA  
2390 C C   . ARG A 347 ? 0.83969 0.52456 0.55954 0.16729  -0.34436 -0.11662 347 ARG A C   
2391 O O   . ARG A 347 ? 0.81468 0.51586 0.56057 0.16696  -0.35027 -0.12332 347 ARG A O   
2392 C CB  . ARG A 347 ? 0.85563 0.51681 0.53921 0.16114  -0.32732 -0.09676 347 ARG A CB  
2393 C CG  . ARG A 347 ? 0.79692 0.48204 0.50231 0.14351  -0.31406 -0.09017 347 ARG A CG  
2394 C CD  . ARG A 347 ? 0.76607 0.47202 0.49457 0.12695  -0.30186 -0.08101 347 ARG A CD  
2395 N NE  . ARG A 347 ? 0.80107 0.46664 0.47811 0.13726  -0.29914 -0.07255 347 ARG A NE  
2396 C CZ  . ARG A 347 ? 0.75447 0.41996 0.43448 0.13342  -0.29600 -0.06686 347 ARG A CZ  
2397 N NH1 . ARG A 347 ? 0.74723 0.45295 0.48135 0.11962  -0.29554 -0.06982 347 ARG A NH1 
2398 N NH2 . ARG A 347 ? 0.78164 0.40403 0.40649 0.14394  -0.29067 -0.05680 347 ARG A NH2 
2399 N N   . ILE A 348 ? 0.79414 0.49536 0.52983 0.15806  -0.33927 -0.11632 348 ILE A N   
2400 C CA  . ILE A 348 ? 0.79020 0.52845 0.57302 0.14622  -0.33934 -0.12288 348 ILE A CA  
2401 C C   . ILE A 348 ? 0.78236 0.55609 0.61142 0.12681  -0.32968 -0.11943 348 ILE A C   
2402 O O   . ILE A 348 ? 0.75945 0.54463 0.59314 0.11419  -0.31520 -0.10817 348 ILE A O   
2403 C CB  . ILE A 348 ? 0.79757 0.53727 0.58038 0.14273  -0.33748 -0.12318 348 ILE A CB  
2404 C CG1 . ILE A 348 ? 0.82177 0.57782 0.63885 0.14120  -0.34783 -0.13521 348 ILE A CG1 
2405 C CG2 . ILE A 348 ? 0.77599 0.53284 0.57072 0.12435  -0.31998 -0.11108 348 ILE A CG2 
2406 C CD1 . ILE A 348 ? 0.82783 0.58928 0.65147 0.13459  -0.34501 -0.13475 348 ILE A CD1 
2407 N N   . SER A 349 ? 0.79064 0.58210 0.65359 0.12509  -0.33746 -0.12973 349 SER A N   
2408 C CA  . SER A 349 ? 0.78225 0.60645 0.68716 0.10814  -0.32828 -0.12764 349 SER A CA  
2409 C C   . SER A 349 ? 0.78767 0.63482 0.71920 0.09139  -0.31861 -0.12426 349 SER A C   
2410 O O   . SER A 349 ? 0.79527 0.63394 0.71672 0.09343  -0.32118 -0.12529 349 SER A O   
2411 C CB  . SER A 349 ? 0.81783 0.64954 0.74401 0.11526  -0.34043 -0.14083 349 SER A CB  
2412 O OG  . SER A 349 ? 0.87655 0.72009 0.82514 0.11440  -0.34742 -0.15115 349 SER A OG  
2413 N N   . VAL A 350 ? 0.77706 0.65234 0.74121 0.07526  -0.30740 -0.12023 350 VAL A N   
2414 C CA  . VAL A 350 ? 0.76117 0.65697 0.74829 0.05941  -0.29771 -0.11643 350 VAL A CA  
2415 C C   . VAL A 350 ? 0.79431 0.69425 0.79596 0.06191  -0.30839 -0.12793 350 VAL A C   
2416 O O   . VAL A 350 ? 0.78350 0.68437 0.78698 0.05669  -0.30709 -0.12690 350 VAL A O   
2417 C CB  . VAL A 350 ? 0.70080 0.62369 0.71517 0.04338  -0.28339 -0.10999 350 VAL A CB  
2418 C CG1 . VAL A 350 ? 0.67487 0.61483 0.70607 0.02803  -0.27288 -0.10469 350 VAL A CG1 
2419 C CG2 . VAL A 350 ? 0.68800 0.60740 0.69012 0.04215  -0.27441 -0.10050 350 VAL A CG2 
2420 N N   . ASP A 351 ? 0.86013 0.76284 0.87319 0.07024  -0.31960 -0.13991 351 ASP A N   
2421 C CA  . ASP A 351 ? 0.87417 0.78313 0.90401 0.07284  -0.33032 -0.15282 351 ASP A CA  
2422 C C   . ASP A 351 ? 0.92846 0.81282 0.93380 0.08737  -0.34316 -0.15860 351 ASP A C   
2423 O O   . ASP A 351 ? 0.87911 0.76781 0.89428 0.08413  -0.34663 -0.16345 351 ASP A O   
2424 C CB  . ASP A 351 ? 0.94564 0.86348 0.99389 0.08022  -0.33999 -0.16613 351 ASP A CB  
2425 C CG  . ASP A 351 ? 0.92762 0.87501 1.00670 0.06393  -0.32767 -0.16363 351 ASP A CG  
2426 O OD1 . ASP A 351 ? 0.98317 0.93387 1.06631 0.06728  -0.32723 -0.16478 351 ASP A OD1 
2427 O OD2 . ASP A 351 ? 0.86673 0.83286 0.96416 0.04811  -0.31858 -0.16068 351 ASP A OD2 
2428 N N   . ASP A 352 ? 0.93390 0.79138 0.90548 0.10363  -0.35026 -0.15831 352 ASP A N   
2429 C CA  . ASP A 352 ? 0.88165 0.71372 0.82509 0.11878  -0.36181 -0.16356 352 ASP A CA  
2430 C C   . ASP A 352 ? 0.85116 0.67986 0.78356 0.10968  -0.35171 -0.15311 352 ASP A C   
2431 O O   . ASP A 352 ? 0.90147 0.71997 0.82559 0.11586  -0.35937 -0.15861 352 ASP A O   
2432 C CB  . ASP A 352 ? 0.90089 0.70278 0.80558 0.13868  -0.37066 -0.16505 352 ASP A CB  
2433 C CG  . ASP A 352 ? 1.07793 0.87558 0.98828 0.15447  -0.38717 -0.18021 352 ASP A CG  
2434 O OD1 . ASP A 352 ? 1.13944 0.96110 1.08713 0.14848  -0.39016 -0.18944 352 ASP A OD1 
2435 O OD2 . ASP A 352 ? 1.13313 0.90272 1.00929 0.17336  -0.39707 -0.18336 352 ASP A OD2 
2436 N N   . ALA A 353 ? 0.84241 0.67986 0.77554 0.09586  -0.33521 -0.13911 353 ALA A N   
2437 C CA  . ALA A 353 ? 0.82707 0.66263 0.75197 0.08760  -0.32568 -0.13015 353 ALA A CA  
2438 C C   . ALA A 353 ? 0.80794 0.66229 0.76172 0.07441  -0.32322 -0.13167 353 ALA A C   
2439 O O   . ALA A 353 ? 0.80412 0.65140 0.75017 0.07333  -0.32297 -0.13018 353 ALA A O   
2440 C CB  . ALA A 353 ? 0.81377 0.65538 0.73428 0.07727  -0.30948 -0.11648 353 ALA A CB  
2441 N N   . LEU A 354 ? 0.79676 0.67423 0.78220 0.06440  -0.32122 -0.13476 354 LEU A N   
2442 C CA  . LEU A 354 ? 0.77523 0.66932 0.78542 0.05171  -0.31909 -0.13663 354 LEU A CA  
2443 C C   . LEU A 354 ? 0.77428 0.66012 0.78560 0.06143  -0.33480 -0.15020 354 LEU A C   
2444 O O   . LEU A 354 ? 0.75956 0.65227 0.78370 0.05266  -0.33435 -0.15144 354 LEU A O   
2445 C CB  . LEU A 354 ? 0.75762 0.67855 0.79819 0.03840  -0.31184 -0.13679 354 LEU A CB  
2446 C CG  . LEU A 354 ? 0.72844 0.66254 0.77384 0.02546  -0.29476 -0.12345 354 LEU A CG  
2447 C CD1 . LEU A 354 ? 0.76698 0.71946 0.83171 0.02149  -0.29168 -0.12628 354 LEU A CD1 
2448 C CD2 . LEU A 354 ? 0.68164 0.62669 0.73704 0.00988  -0.28426 -0.11574 354 LEU A CD2 
2449 N N   . GLN A 355 ? 0.78237 0.65304 0.78016 0.07983  -0.34916 -0.16088 355 GLN A N   
2450 C CA  . GLN A 355 ? 0.80150 0.66283 0.79854 0.09216  -0.36563 -0.17533 355 GLN A CA  
2451 C C   . GLN A 355 ? 0.80093 0.63411 0.76262 0.10660  -0.37211 -0.17493 355 GLN A C   
2452 O O   . GLN A 355 ? 0.83596 0.65897 0.79344 0.11883  -0.38640 -0.18707 355 GLN A O   
2453 C CB  . GLN A 355 ? 0.82386 0.68635 0.82935 0.10574  -0.37946 -0.19013 355 GLN A CB  
2454 C CG  . GLN A 355 ? 0.84538 0.73698 0.89093 0.09358  -0.37799 -0.19770 355 GLN A CG  
2455 C CD  . GLN A 355 ? 0.95525 0.85716 1.02140 0.08658  -0.38252 -0.20627 355 GLN A CD  
2456 O OE1 . GLN A 355 ? 0.87304 0.76266 0.93321 0.10053  -0.39747 -0.21852 355 GLN A OE1 
2457 N NE2 . GLN A 355 ? 0.99708 0.92092 1.08649 0.06502  -0.36977 -0.20019 355 GLN A NE2 
2458 N N   . HIS A 356 ? 0.81024 0.67156 0.91793 0.27041  -0.43446 -0.28882 356 HIS A N   
2459 C CA  . HIS A 356 ? 0.83028 0.65204 0.86781 0.26903  -0.44923 -0.25572 356 HIS A CA  
2460 C C   . HIS A 356 ? 0.79701 0.64602 0.83783 0.24715  -0.41254 -0.24910 356 HIS A C   
2461 O O   . HIS A 356 ? 0.76128 0.64108 0.82376 0.22681  -0.36798 -0.25099 356 HIS A O   
2462 C CB  . HIS A 356 ? 0.84742 0.61885 0.80153 0.26275  -0.44843 -0.21228 356 HIS A CB  
2463 C CG  . HIS A 356 ? 0.87889 0.60187 0.75950 0.25736  -0.45686 -0.18072 356 HIS A CG  
2464 N ND1 . HIS A 356 ? 0.85966 0.58620 0.70811 0.24071  -0.43627 -0.15855 356 HIS A ND1 
2465 C CD2 . HIS A 356 ? 0.92919 0.59937 0.76510 0.25939  -0.47075 -0.16934 356 HIS A CD2 
2466 C CE1 . HIS A 356 ? 0.89271 0.57527 0.68628 0.23282  -0.43569 -0.13548 356 HIS A CE1 
2467 N NE2 . HIS A 356 ? 0.93569 0.58345 0.72011 0.24343  -0.45668 -0.14198 356 HIS A NE2 
2468 N N   . PRO A 357 ? 0.81103 0.64696 0.82894 0.25076  -0.43070 -0.24213 357 PRO A N   
2469 C CA  . PRO A 357 ? 0.78092 0.64239 0.80294 0.23091  -0.39759 -0.23722 357 PRO A CA  
2470 C C   . PRO A 357 ? 0.75576 0.61105 0.73065 0.20565  -0.35433 -0.20298 357 PRO A C   
2471 O O   . PRO A 357 ? 0.72538 0.61031 0.71991 0.18725  -0.31752 -0.20712 357 PRO A O   
2472 C CB  . PRO A 357 ? 0.80926 0.64317 0.79545 0.24128  -0.43113 -0.22718 357 PRO A CB  
2473 C CG  . PRO A 357 ? 0.85907 0.64612 0.81738 0.26190  -0.47137 -0.22430 357 PRO A CG  
2474 C CD  . PRO A 357 ? 0.85759 0.65832 0.85726 0.27360  -0.48022 -0.24657 357 PRO A CD  
2475 N N   . TYR A 358 ? 0.77031 0.58634 0.68255 0.20416  -0.35818 -0.17066 358 TYR A N   
2476 C CA  . TYR A 358 ? 0.75545 0.56595 0.62454 0.18207  -0.31981 -0.14047 358 TYR A CA  
2477 C C   . TYR A 358 ? 0.72611 0.56397 0.63052 0.17073  -0.28431 -0.15168 358 TYR A C   
2478 O O   . TYR A 358 ? 0.70818 0.54893 0.58887 0.15168  -0.24872 -0.13404 358 TYR A O   
2479 C CB  . TYR A 358 ? 0.77337 0.53522 0.56728 0.18301  -0.33416 -0.10571 358 TYR A CB  
2480 C CG  . TYR A 358 ? 0.78013 0.53437 0.52487 0.16194  -0.30045 -0.07472 358 TYR A CG  
2481 C CD1 . TYR A 358 ? 0.78446 0.53635 0.49959 0.15160  -0.29199 -0.05988 358 TYR A CD1 
2482 C CD2 . TYR A 358 ? 0.77629 0.52609 0.50563 0.15339  -0.27845 -0.06203 358 TYR A CD2 
2483 C CE1 . TYR A 358 ? 0.79478 0.54090 0.46808 0.13417  -0.26365 -0.03487 358 TYR A CE1 
2484 C CE2 . TYR A 358 ? 0.75436 0.49760 0.44112 0.13612  -0.25035 -0.03668 358 TYR A CE2 
2485 C CZ  . TYR A 358 ? 0.77711 0.51894 0.43687 0.12700  -0.24361 -0.02400 358 TYR A CZ  
2486 O OH  . TYR A 358 ? 0.78822 0.52467 0.40856 0.11154  -0.21795 -0.00192 358 TYR A OH  
2487 N N   . ILE A 359 ? 0.72251 0.57914 0.68208 0.18210  -0.29375 -0.18189 359 ILE A N   
2488 C CA  . ILE A 359 ? 0.70186 0.57987 0.69165 0.17183  -0.26234 -0.19307 359 ILE A CA  
2489 C C   . ILE A 359 ? 0.68351 0.60893 0.74938 0.16606  -0.24278 -0.23391 359 ILE A C   
2490 O O   . ILE A 359 ? 0.66251 0.60621 0.74087 0.14645  -0.20199 -0.23832 359 ILE A O   
2491 C CB  . ILE A 359 ? 0.72009 0.58006 0.70869 0.18679  -0.28436 -0.19431 359 ILE A CB  
2492 C CG1 . ILE A 359 ? 0.74101 0.55202 0.65034 0.18870  -0.29949 -0.15417 359 ILE A CG1 
2493 C CG2 . ILE A 359 ? 0.69928 0.58142 0.71927 0.17571  -0.25124 -0.20648 359 ILE A CG2 
2494 C CD1 . ILE A 359 ? 0.72063 0.52337 0.58260 0.16702  -0.26229 -0.12311 359 ILE A CD1 
2495 N N   . ASN A 360 ? 0.69429 0.63830 0.80983 0.18200  -0.27095 -0.26543 360 ASN A N   
2496 C CA  . ASN A 360 ? 0.67990 0.67199 0.87623 0.17773  -0.25472 -0.31102 360 ASN A CA  
2497 C C   . ASN A 360 ? 0.65828 0.67286 0.86209 0.15345  -0.21465 -0.31443 360 ASN A C   
2498 O O   . ASN A 360 ? 0.64858 0.70258 0.91713 0.14622  -0.19751 -0.35340 360 ASN A O   
2499 C CB  . ASN A 360 ? 0.69898 0.70531 0.94788 0.20314  -0.29879 -0.34619 360 ASN A CB  
2500 C CG  . ASN A 360 ? 0.71152 0.70372 0.93552 0.21084  -0.32375 -0.33565 360 ASN A CG  
2501 O OD1 . ASN A 360 ? 0.69991 0.68389 0.88308 0.19425  -0.30203 -0.31005 360 ASN A OD1 
2502 N ND2 . ASN A 360 ? 0.73784 0.72574 0.98615 0.23705  -0.37128 -0.35678 360 ASN A ND2 
2503 N N   . VAL A 361 ? 0.65281 0.64329 0.79318 0.14031  -0.19934 -0.27716 361 VAL A N   
2504 C CA  . VAL A 361 ? 0.63592 0.64222 0.77720 0.11666  -0.16025 -0.27903 361 VAL A CA  
2505 C C   . VAL A 361 ? 0.63984 0.65551 0.78918 0.09532  -0.11600 -0.28556 361 VAL A C   
2506 O O   . VAL A 361 ? 0.62051 0.65126 0.78155 0.07436  -0.08116 -0.29746 361 VAL A O   
2507 C CB  . VAL A 361 ? 0.63529 0.61213 0.70612 0.11012  -0.15844 -0.23862 361 VAL A CB  
2508 C CG1 . VAL A 361 ? 0.66704 0.63702 0.73325 0.12732  -0.19740 -0.23691 361 VAL A CG1 
2509 C CG2 . VAL A 361 ? 0.63824 0.57978 0.64574 0.10922  -0.15691 -0.20086 361 VAL A CG2 
2510 N N   . TRP A 362 ? 0.65278 0.65638 0.79247 0.09947  -0.11653 -0.27797 362 TRP A N   
2511 C CA  . TRP A 362 ? 0.66495 0.67526 0.81335 0.08109  -0.07773 -0.28624 362 TRP A CA  
2512 C C   . TRP A 362 ? 0.74422 0.78721 0.96651 0.08667  -0.07947 -0.32977 362 TRP A C   
2513 O O   . TRP A 362 ? 0.76698 0.81523 0.99949 0.07286  -0.04990 -0.33924 362 TRP A O   
2514 C CB  . TRP A 362 ? 0.65025 0.62547 0.73678 0.08017  -0.07366 -0.24836 362 TRP A CB  
2515 C CG  . TRP A 362 ? 0.62558 0.57073 0.64199 0.07458  -0.07112 -0.20833 362 TRP A CG  
2516 C CD1 . TRP A 362 ? 0.62798 0.54817 0.60079 0.08854  -0.10164 -0.17987 362 TRP A CD1 
2517 C CD2 . TRP A 362 ? 0.61382 0.54910 0.59442 0.05310  -0.03633 -0.19420 362 TRP A CD2 
2518 N NE1 . TRP A 362 ? 0.64108 0.54159 0.55859 0.07707  -0.08720 -0.15066 362 TRP A NE1 
2519 C CE2 . TRP A 362 ? 0.64843 0.55709 0.56954 0.05670  -0.04889 -0.15858 362 TRP A CE2 
2520 C CE3 . TRP A 362 ? 0.61464 0.55787 0.60490 0.03061  0.00394  -0.20930 362 TRP A CE3 
2521 C CZ2 . TRP A 362 ? 0.68689 0.57958 0.56246 0.04114  -0.02501 -0.13885 362 TRP A CZ2 
2522 C CZ3 . TRP A 362 ? 0.62838 0.54988 0.56698 0.01487  0.02703  -0.18761 362 TRP A CZ3 
2523 C CH2 . TRP A 362 ? 0.66488 0.56278 0.54890 0.02145  0.01130  -0.15324 362 TRP A CH2 
2524 N N   . TYR A 363 ? 0.78644 0.85073 1.06018 0.10692  -0.11419 -0.35784 363 TYR A N   
2525 C CA  . TYR A 363 ? 0.92884 1.02350 1.27419 0.11763  -0.12433 -0.40025 363 TYR A CA  
2526 C C   . TYR A 363 ? 1.12303 1.25447 1.52196 0.09305  -0.07964 -0.43872 363 TYR A C   
2527 O O   . TYR A 363 ? 1.09594 1.24602 1.51357 0.07837  -0.06036 -0.45485 363 TYR A O   
2528 C CB  . TYR A 363 ? 0.91138 1.02019 1.30008 0.14497  -0.17252 -0.42498 363 TYR A CB  
2529 C CG  . TYR A 363 ? 1.02109 1.17323 1.50041 0.15410  -0.18012 -0.48097 363 TYR A CG  
2530 C CD1 . TYR A 363 ? 1.10586 1.25898 1.60581 0.16492  -0.18983 -0.49231 363 TYR A CD1 
2531 C CD2 . TYR A 363 ? 0.98130 1.17491 1.52786 0.15200  -0.17785 -0.52459 363 TYR A CD2 
2532 C CE1 . TYR A 363 ? 1.12632 1.32143 1.71266 0.17392  -0.19754 -0.54650 363 TYR A CE1 
2533 C CE2 . TYR A 363 ? 1.00011 1.23711 1.63465 0.16036  -0.18481 -0.58007 363 TYR A CE2 
2534 C CZ  . TYR A 363 ? 1.05758 1.29556 1.71229 0.17161  -0.19496 -0.59126 363 TYR A CZ  
2535 O OH  . TYR A 363 ? 1.01324 1.29963 1.75551 0.17784  -0.20223 -0.64142 363 TYR A OH  
2536 N N   . ASP A 364 ? 1.49118 1.63130 1.91274 0.08724  -0.06214 -0.45395 364 ASP A N   
2537 C CA  . ASP A 364 ? 1.56106 1.73400 2.03327 0.06236  -0.01853 -0.49363 364 ASP A CA  
2538 C C   . ASP A 364 ? 1.63504 1.82995 2.16187 0.07111  -0.02377 -0.52569 364 ASP A C   
2539 O O   . ASP A 364 ? 1.68712 1.85742 2.17910 0.07549  -0.02579 -0.50152 364 ASP A O   
2540 C CB  . ASP A 364 ? 1.55695 1.70398 1.96973 0.03090  0.03068  -0.46735 364 ASP A CB  
2541 C CG  . ASP A 364 ? 1.59962 1.77365 2.05475 0.00080  0.07859  -0.50773 364 ASP A CG  
2542 O OD1 . ASP A 364 ? 1.69473 1.84925 2.11568 -0.02213 0.11689  -0.49789 364 ASP A OD1 
2543 O OD2 . ASP A 364 ? 1.54375 1.75753 2.06619 -0.00031 0.07770  -0.55112 364 ASP A OD2 
2544 N N   . PRO A 365 ? 1.74150 1.98403 2.35584 0.07323  -0.02508 -0.58194 365 PRO A N   
2545 C CA  . PRO A 365 ? 1.69785 1.96510 2.36906 0.08676  -0.04051 -0.61135 365 PRO A CA  
2546 C C   . PRO A 365 ? 1.73097 1.98693 2.38095 0.06767  -0.00472 -0.60165 365 PRO A C   
2547 O O   . PRO A 365 ? 1.67596 1.92016 2.32297 0.08581  -0.02646 -0.59553 365 PRO A O   
2548 C CB  . PRO A 365 ? 1.61561 1.94520 2.37507 0.07737  -0.03664 -0.65605 365 PRO A CB  
2549 C CG  . PRO A 365 ? 1.60285 1.93292 2.35530 0.07703  -0.04165 -0.65522 365 PRO A CG  
2550 C CD  . PRO A 365 ? 1.63107 1.91030 2.29581 0.06238  -0.01459 -0.61602 365 PRO A CD  
2551 N N   . ALA A 366 ? 1.63994 1.89574 2.27118 0.03119  0.04869  -0.59876 366 ALA A N   
2552 C CA  . ALA A 366 ? 1.61944 1.86043 2.22500 0.01160  0.08305  -0.58794 366 ALA A CA  
2553 C C   . ALA A 366 ? 1.63423 1.82029 2.15755 0.02219  0.07565  -0.54173 366 ALA A C   
2554 O O   . ALA A 366 ? 1.60832 1.78048 2.11389 0.01641  0.09076  -0.53313 366 ALA A O   
2555 C CB  . ALA A 366 ? 1.56944 1.81433 2.16306 -0.03081 0.13870  -0.59078 366 ALA A CB  
2556 N N   . GLU A 367 ? 1.68235 1.84036 2.15179 0.03463  0.05067  -0.50166 367 GLU A N   
2557 C CA  . GLU A 367 ? 1.63916 1.74994 2.02689 0.04134  0.04067  -0.44671 367 GLU A CA  
2558 C C   . GLU A 367 ? 1.64176 1.74256 2.02904 0.07434  -0.00941 -0.43399 367 GLU A C   
2559 O O   . GLU A 367 ? 1.57567 1.64613 1.91530 0.07856  -0.01292 -0.40213 367 GLU A O   
2560 C CB  . GLU A 367 ? 1.59645 1.68023 1.92202 0.03510  0.04262  -0.41014 367 GLU A CB  
2561 C CG  . GLU A 367 ? 1.65530 1.73823 1.96664 0.00253  0.09047  -0.41681 367 GLU A CG  
2562 C CD  . GLU A 367 ? 1.62613 1.66607 1.85923 -0.01474 0.11889  -0.37834 367 GLU A CD  
2563 O OE1 . GLU A 367 ? 1.63371 1.64224 1.80558 -0.00574 0.10245  -0.33607 367 GLU A OE1 
2564 O OE2 . GLU A 367 ? 1.59479 1.63146 1.82718 -0.03748 0.15740  -0.39196 367 GLU A OE2 
2565 N N   . VAL A 368 ? 1.64027 1.76293 2.07693 0.09776  -0.04892 -0.45880 368 VAL A N   
2566 C CA  . VAL A 368 ? 1.53859 1.64301 1.96572 0.12952  -0.09991 -0.44568 368 VAL A CA  
2567 C C   . VAL A 368 ? 1.45504 1.56794 1.91427 0.13702  -0.10269 -0.46423 368 VAL A C   
2568 O O   . VAL A 368 ? 1.29148 1.37202 1.70315 0.14379  -0.11168 -0.43244 368 VAL A O   
2569 C CB  . VAL A 368 ? 1.43350 1.55452 1.90224 0.15331  -0.14343 -0.46956 368 VAL A CB  
2570 C CG1 . VAL A 368 ? 1.23240 1.31820 1.66590 0.18363  -0.19643 -0.44557 368 VAL A CG1 
2571 C CG2 . VAL A 368 ? 1.43697 1.55811 1.88602 0.14191  -0.13342 -0.45924 368 VAL A CG2 
2572 N N   . GLU A 369 ? 1.36167 1.51932 1.90317 0.13507  -0.09392 -0.51740 369 GLU A N   
2573 C CA  . GLU A 369 ? 1.26223 1.43410 1.84635 0.14521  -0.10128 -0.54276 369 GLU A CA  
2574 C C   . GLU A 369 ? 1.32198 1.50104 1.90559 0.11506  -0.04698 -0.54835 369 GLU A C   
2575 O O   . GLU A 369 ? 1.36005 1.53845 1.92251 0.08577  -0.00321 -0.54285 369 GLU A O   
2576 C CB  . GLU A 369 ? 1.20457 1.42609 1.87884 0.15951  -0.12825 -0.59249 369 GLU A CB  
2577 C CG  . GLU A 369 ? 1.14081 1.37474 1.85132 0.17782  -0.15792 -0.60683 369 GLU A CG  
2578 C CD  . GLU A 369 ? 1.09990 1.27901 1.74584 0.19862  -0.18282 -0.57073 369 GLU A CD  
2579 O OE1 . GLU A 369 ? 1.11147 1.26810 1.71734 0.18422  -0.15052 -0.55022 369 GLU A OE1 
2580 O OE2 . GLU A 369 ? 1.01994 1.17630 1.65246 0.22858  -0.23553 -0.56245 369 GLU A OE2 
2581 N N   . ALA A 370 ? 1.40976 1.59245 2.01266 0.12224  -0.05168 -0.55769 370 ALA A N   
2582 C CA  . ALA A 370 ? 1.37536 1.56344 1.97545 0.09507  -0.00597 -0.55882 370 ALA A CA  
2583 C C   . ALA A 370 ? 1.37579 1.59495 2.03463 0.10491  -0.02317 -0.58432 370 ALA A C   
2584 O O   . ALA A 370 ? 1.31704 1.53805 1.99740 0.13583  -0.07294 -0.59036 370 ALA A O   
2585 C CB  . ALA A 370 ? 1.25976 1.39566 1.77156 0.08859  0.00929  -0.50881 370 ALA A CB  
2586 N N   . PRO A 371 ? 1.49865 1.74036 2.18178 0.07861  0.01541  -0.59952 371 PRO A N   
2587 C CA  . PRO A 371 ? 1.55041 1.82638 2.29505 0.08610  -0.00026 -0.62776 371 PRO A CA  
2588 C C   . PRO A 371 ? 1.52655 1.76807 2.23810 0.11358  -0.03276 -0.60517 371 PRO A C   
2589 O O   . PRO A 371 ? 1.44058 1.63333 2.07980 0.11521  -0.02438 -0.56786 371 PRO A O   
2590 C CB  . PRO A 371 ? 1.56594 1.86039 2.32329 0.04743  0.05458  -0.64012 371 PRO A CB  
2591 C CG  . PRO A 371 ? 1.56822 1.81940 2.24726 0.02589  0.09340  -0.60552 371 PRO A CG  
2592 C CD  . PRO A 371 ? 1.57456 1.81233 2.23202 0.03927  0.07353  -0.59408 371 PRO A CD  
2593 N N   . PRO A 372 ? 1.41079 1.67544 2.17277 0.13529  -0.07167 -0.62735 372 PRO A N   
2594 C CA  . PRO A 372 ? 1.29116 1.52138 2.02090 0.16106  -0.10479 -0.60614 372 PRO A CA  
2595 C C   . PRO A 372 ? 1.25080 1.49199 1.99537 0.14748  -0.08017 -0.61351 372 PRO A C   
2596 O O   . PRO A 372 ? 1.19252 1.48032 2.00695 0.14211  -0.08149 -0.65058 372 PRO A O   
2597 C CB  . PRO A 372 ? 1.25337 1.50019 2.02658 0.19195  -0.16473 -0.62724 372 PRO A CB  
2598 C CG  . PRO A 372 ? 1.30124 1.61047 2.15643 0.17696  -0.15469 -0.67322 372 PRO A CG  
2599 C CD  . PRO A 372 ? 1.37193 1.69294 2.22038 0.13901  -0.09256 -0.67294 372 PRO A CD  
2600 N N   . PRO A 373 ? 1.19086 1.39015 1.87146 0.14139  -0.05825 -0.57989 373 PRO A N   
2601 C CA  . PRO A 373 ? 1.11392 1.31820 1.80067 0.12830  -0.03387 -0.58312 373 PRO A CA  
2602 C C   . PRO A 373 ? 1.03105 1.23418 1.73703 0.15595  -0.07729 -0.58804 373 PRO A C   
2603 O O   . PRO A 373 ? 1.00234 1.19999 1.70187 0.15013  -0.06278 -0.58383 373 PRO A O   
2604 C CB  . PRO A 373 ? 1.09742 1.25123 1.70147 0.11635  -0.00270 -0.54231 373 PRO A CB  
2605 C CG  . PRO A 373 ? 1.05912 1.17367 1.61285 0.13872  -0.03387 -0.51424 373 PRO A CG  
2606 C CD  . PRO A 373 ? 1.11816 1.26278 1.71666 0.14626  -0.05629 -0.53767 373 PRO A CD  
2607 N N   . GLN A 379 ? 0.91643 0.98553 1.50307 0.22217  -0.14400 -0.50591 379 GLN A N   
2608 C CA  . GLN A 379 ? 0.95939 1.00969 1.52769 0.24249  -0.18484 -0.49652 379 GLN A CA  
2609 C C   . GLN A 379 ? 1.04523 1.04371 1.55671 0.26779  -0.22918 -0.46508 379 GLN A C   
2610 O O   . GLN A 379 ? 1.03365 1.03138 1.55618 0.27842  -0.25039 -0.47101 379 GLN A O   
2611 C CB  . GLN A 379 ? 0.79370 0.89214 1.43610 0.24909  -0.21057 -0.53878 379 GLN A CB  
2612 N N   . LEU A 380 ? 1.09545 1.04982 1.54380 0.27529  -0.24232 -0.43161 380 LEU A N   
2613 C CA  . LEU A 380 ? 1.18403 1.08231 1.56433 0.29373  -0.28030 -0.39588 380 LEU A CA  
2614 C C   . LEU A 380 ? 1.22399 1.09742 1.56957 0.29006  -0.26543 -0.37407 380 LEU A C   
2615 O O   . LEU A 380 ? 1.20167 1.08705 1.57408 0.29618  -0.27824 -0.38869 380 LEU A O   
2616 C CB  . LEU A 380 ? 1.22162 1.11974 1.61941 0.31532  -0.33619 -0.41185 380 LEU A CB  
2617 C CG  . LEU A 380 ? 1.32659 1.16191 1.64270 0.32935  -0.37594 -0.37426 380 LEU A CG  
2618 C CD1 . LEU A 380 ? 1.25840 1.08984 1.57784 0.34264  -0.41857 -0.38686 380 LEU A CD1 
2619 C CD2 . LEU A 380 ? 1.41915 1.22669 1.70651 0.33711  -0.39659 -0.36273 380 LEU A CD2 
2620 N N   . ASP A 381 ? 1.27107 1.10937 1.55628 0.28043  -0.24006 -0.33966 381 ASP A N   
2621 C CA  . ASP A 381 ? 1.28528 1.09894 1.53447 0.27574  -0.22388 -0.31775 381 ASP A CA  
2622 C C   . ASP A 381 ? 1.40557 1.15926 1.56930 0.28364  -0.24659 -0.27160 381 ASP A C   
2623 O O   . ASP A 381 ? 1.39649 1.13247 1.50541 0.26488  -0.21785 -0.23610 381 ASP A O   
2624 C CB  . ASP A 381 ? 1.17929 1.01109 1.42810 0.24770  -0.16649 -0.31461 381 ASP A CB  
2625 C CG  . ASP A 381 ? 1.11963 1.00273 1.43993 0.23563  -0.13994 -0.35787 381 ASP A CG  
2626 O OD1 . ASP A 381 ? 1.10093 1.02244 1.48495 0.23847  -0.14678 -0.39238 381 ASP A OD1 
2627 O OD2 . ASP A 381 ? 1.07272 0.96314 1.37812 0.21568  -0.11047 -0.34913 381 ASP A OD2 
2628 N N   . GLU A 382 ? 1.63726 1.37046 1.78161 0.29892  -0.29249 -0.26480 382 GLU A N   
2629 C CA  . GLU A 382 ? 1.68998 1.36844 1.75034 0.30068  -0.31341 -0.22245 382 GLU A CA  
2630 C C   . GLU A 382 ? 1.60619 1.26711 1.64878 0.30492  -0.32874 -0.21531 382 GLU A C   
2631 O O   . GLU A 382 ? 1.52446 1.19718 1.59976 0.31684  -0.35830 -0.23947 382 GLU A O   
2632 C CB  . GLU A 382 ? 1.68334 1.34464 1.72081 0.30883  -0.35065 -0.21900 382 GLU A CB  
2633 C CG  . GLU A 382 ? 1.61049 1.29199 1.67108 0.30635  -0.33916 -0.22914 382 GLU A CG  
2634 C CD  . GLU A 382 ? 1.64428 1.29511 1.64074 0.29407  -0.31827 -0.19131 382 GLU A CD  
2635 O OE1 . GLU A 382 ? 1.64004 1.24992 1.56521 0.28961  -0.33321 -0.15749 382 GLU A OE1 
2636 O OE2 . GLU A 382 ? 1.57730 1.25783 1.59069 0.27628  -0.27940 -0.19286 382 GLU A OE2 
2637 N N   . ARG A 383 ? 1.46176 1.09468 1.45200 0.29474  -0.30924 -0.18326 383 ARG A N   
2638 C CA  . ARG A 383 ? 1.36497 0.98161 1.33622 0.29608  -0.31788 -0.17487 383 ARG A CA  
2639 C C   . ARG A 383 ? 1.30260 0.88250 1.19841 0.28121  -0.29979 -0.13213 383 ARG A C   
2640 O O   . ARG A 383 ? 1.25937 0.82732 1.11859 0.27074  -0.28445 -0.11031 383 ARG A O   
2641 C CB  . ARG A 383 ? 1.30714 0.96183 1.34489 0.29803  -0.29838 -0.20459 383 ARG A CB  
2642 C CG  . ARG A 383 ? 1.28756 0.93538 1.32712 0.30531  -0.31853 -0.20915 383 ARG A CG  
2643 C CD  . ARG A 383 ? 1.28597 0.98165 1.40972 0.31334  -0.32191 -0.25392 383 ARG A CD  
2644 N NE  . ARG A 383 ? 1.19722 0.93205 1.37067 0.30130  -0.27681 -0.27274 383 ARG A NE  
2645 C CZ  . ARG A 383 ? 1.15632 0.91821 1.37160 0.29673  -0.25649 -0.29227 383 ARG A CZ  
2646 N NH1 . ARG A 383 ? 1.16535 0.92123 1.38306 0.30566  -0.27819 -0.29537 383 ARG A NH1 
2647 N NH2 . ARG A 383 ? 1.11134 0.90577 1.36360 0.28079  -0.21235 -0.30949 383 ARG A NH2 
2648 N N   . GLU A 384 ? 1.24025 0.80520 1.11434 0.27903  -0.30133 -0.12161 384 GLU A N   
2649 C CA  . GLU A 384 ? 1.26606 0.80449 1.07685 0.26255  -0.28158 -0.08572 384 GLU A CA  
2650 C C   . GLU A 384 ? 1.17484 0.72389 1.00604 0.26140  -0.25900 -0.08868 384 GLU A C   
2651 O O   . GLU A 384 ? 1.13248 0.68767 0.99050 0.27081  -0.27414 -0.10535 384 GLU A O   
2652 C CB  . GLU A 384 ? 1.29924 0.80356 1.05224 0.25653  -0.30515 -0.06919 384 GLU A CB  
2653 C CG  . GLU A 384 ? 1.31912 0.80610 1.02124 0.23811  -0.28337 -0.04112 384 GLU A CG  
2654 C CD  . GLU A 384 ? 1.33783 0.80063 0.98120 0.22061  -0.28283 -0.02096 384 GLU A CD  
2655 O OE1 . GLU A 384 ? 1.41517 0.86295 1.04813 0.22501  -0.30711 -0.02851 384 GLU A OE1 
2656 O OE2 . GLU A 384 ? 1.36155 0.82261 0.97374 0.20189  -0.25673 -0.00068 384 GLU A OE2 
2657 N N   . HIS A 385 ? 1.07191 0.62181 0.88846 0.24956  -0.22323 -0.07349 385 HIS A N   
2658 C CA  . HIS A 385 ? 1.01276 0.56998 0.84378 0.24636  -0.19727 -0.07616 385 HIS A CA  
2659 C C   . HIS A 385 ? 1.00194 0.53803 0.77095 0.22916  -0.17849 -0.04034 385 HIS A C   
2660 O O   . HIS A 385 ? 1.08699 0.61023 0.80885 0.21710  -0.18085 -0.01728 385 HIS A O   
2661 C CB  . HIS A 385 ? 0.93151 0.52127 0.80907 0.24077  -0.16338 -0.09814 385 HIS A CB  
2662 C CG  . HIS A 385 ? 0.96788 0.59379 0.92153 0.25201  -0.17271 -0.14109 385 HIS A CG  
2663 N ND1 . HIS A 385 ? 1.11420 0.74201 1.08961 0.26808  -0.20984 -0.15731 385 HIS A ND1 
2664 C CD2 . HIS A 385 ? 0.97451 0.63972 0.98813 0.24645  -0.14804 -0.17230 385 HIS A CD2 
2665 C CE1 . HIS A 385 ? 1.16826 0.83761 1.21739 0.27322  -0.20864 -0.19768 385 HIS A CE1 
2666 N NE2 . HIS A 385 ? 1.10061 0.79065 1.17530 0.26173  -0.17136 -0.20971 385 HIS A NE2 
2667 N N   . THR A 386 ? 0.93561 0.47412 0.70980 0.22578  -0.15761 -0.03953 386 THR A N   
2668 C CA  . THR A 386 ? 0.91371 0.44180 0.63964 0.20818  -0.13516 -0.01059 386 THR A CA  
2669 C C   . THR A 386 ? 0.92503 0.45558 0.63815 0.19786  -0.10257 -0.00265 386 THR A C   
2670 O O   . THR A 386 ? 0.86155 0.41228 0.60786 0.19801  -0.09199 -0.02049 386 THR A O   
2671 C CB  . THR A 386 ? 0.91768 0.44642 0.65250 0.20881  -0.12712 -0.01283 386 THR A CB  
2672 O OG1 . THR A 386 ? 0.89386 0.43595 0.67442 0.21613  -0.10800 -0.03803 386 THR A OG1 
2673 C CG2 . THR A 386 ? 0.90899 0.43238 0.65088 0.21819  -0.15935 -0.01988 386 THR A CG2 
2674 N N   . ILE A 387 ? 0.90069 0.43083 0.57472 0.17985  -0.08257 0.02102  387 ILE A N   
2675 C CA  . ILE A 387 ? 0.86896 0.40271 0.52668 0.16804  -0.05245 0.02953  387 ILE A CA  
2676 C C   . ILE A 387 ? 0.85677 0.40139 0.54347 0.16641  -0.02417 0.01322  387 ILE A C   
2677 O O   . ILE A 387 ? 0.84778 0.40756 0.54020 0.15489  0.00033  0.00889  387 ILE A O   
2678 C CB  . ILE A 387 ? 0.84194 0.39030 0.46665 0.14642  -0.04027 0.04942  387 ILE A CB  
2679 C CG1 . ILE A 387 ? 0.88344 0.43459 0.50744 0.14297  -0.03612 0.05170  387 ILE A CG1 
2680 C CG2 . ILE A 387 ? 0.83606 0.39138 0.44843 0.13871  -0.05786 0.05534  387 ILE A CG2 
2681 C CD1 . ILE A 387 ? 0.85540 0.42775 0.46578 0.12377  -0.02557 0.06056  387 ILE A CD1 
2682 N N   . GLU A 388 ? 0.86904 0.41556 0.57801 0.17237  -0.02521 0.00209  388 GLU A N   
2683 C CA  . GLU A 388 ? 0.90090 0.46993 0.64573 0.16481  0.00325  -0.01810 388 GLU A CA  
2684 C C   . GLU A 388 ? 0.82355 0.42307 0.62839 0.16810  0.00172  -0.05122 388 GLU A C   
2685 O O   . GLU A 388 ? 0.78694 0.40595 0.61293 0.15511  0.03075  -0.06646 388 GLU A O   
2686 C CB  . GLU A 388 ? 0.93825 0.50000 0.68745 0.16957  0.00326  -0.01981 388 GLU A CB  
2687 C CG  . GLU A 388 ? 0.95506 0.49688 0.65635 0.16004  0.02182  0.00468  388 GLU A CG  
2688 C CD  . GLU A 388 ? 0.96227 0.50953 0.64966 0.14351  0.05580  0.00715  388 GLU A CD  
2689 O OE1 . GLU A 388 ? 0.96417 0.49713 0.60778 0.13735  0.06025  0.02894  388 GLU A OE1 
2690 O OE2 . GLU A 388 ? 1.01653 0.58078 0.73540 0.13614  0.07790  -0.01408 388 GLU A OE2 
2691 N N   . GLU A 389 ? 0.82626 0.42812 0.65741 0.18503  -0.03228 -0.06414 389 GLU A N   
2692 C CA  . GLU A 389 ? 0.80386 0.43697 0.69576 0.18998  -0.03729 -0.09849 389 GLU A CA  
2693 C C   . GLU A 389 ? 0.78877 0.43134 0.67571 0.18098  -0.02843 -0.09659 389 GLU A C   
2694 O O   . GLU A 389 ? 0.72854 0.40035 0.65817 0.17338  -0.01038 -0.12262 389 GLU A O   
2695 C CB  . GLU A 389 ? 0.82955 0.45775 0.74589 0.21310  -0.08102 -0.11234 389 GLU A CB  
2696 C CG  . GLU A 389 ? 0.82629 0.45424 0.76676 0.22362  -0.09009 -0.12605 389 GLU A CG  
2697 C CD  . GLU A 389 ? 0.84531 0.44988 0.78263 0.24718  -0.13824 -0.12757 389 GLU A CD  
2698 O OE1 . GLU A 389 ? 0.89807 0.48249 0.79614 0.24840  -0.15983 -0.10646 389 GLU A OE1 
2699 O OE2 . GLU A 389 ? 0.78374 0.40291 0.75693 0.25452  -0.14975 -0.14574 389 GLU A OE2 
2700 N N   . TRP A 390 ? 0.82105 0.43923 0.65625 0.18062  -0.03996 -0.06727 390 TRP A N   
2701 C CA  . TRP A 390 ? 0.80380 0.42923 0.63018 0.17189  -0.03139 -0.06323 390 TRP A CA  
2702 C C   . TRP A 390 ? 0.78459 0.41831 0.60039 0.15148  0.01031  -0.06056 390 TRP A C   
2703 O O   . TRP A 390 ? 0.72128 0.37118 0.55171 0.14254  0.02465  -0.07129 390 TRP A O   
2704 C CB  . TRP A 390 ? 0.80922 0.40540 0.58012 0.17488  -0.05176 -0.03274 390 TRP A CB  
2705 C CG  . TRP A 390 ? 0.87060 0.45870 0.64971 0.19134  -0.09108 -0.03868 390 TRP A CG  
2706 C CD1 . TRP A 390 ? 0.93613 0.49051 0.67831 0.20219  -0.12240 -0.02206 390 TRP A CD1 
2707 C CD2 . TRP A 390 ? 0.86975 0.47996 0.69303 0.19843  -0.10397 -0.06354 390 TRP A CD2 
2708 N NE1 . TRP A 390 ? 0.96753 0.51791 0.72459 0.21643  -0.15550 -0.03417 390 TRP A NE1 
2709 C CE2 . TRP A 390 ? 0.93316 0.51964 0.74253 0.21534  -0.14563 -0.06014 390 TRP A CE2 
2710 C CE3 . TRP A 390 ? 0.82317 0.46901 0.69472 0.19140  -0.08419 -0.08937 390 TRP A CE3 
2711 C CZ2 . TRP A 390 ? 0.93601 0.53427 0.77989 0.22750  -0.17007 -0.08181 390 TRP A CZ2 
2712 C CZ3 . TRP A 390 ? 0.80372 0.46519 0.71326 0.20235  -0.10656 -0.11179 390 TRP A CZ3 
2713 C CH2 . TRP A 390 ? 0.84531 0.48361 0.74182 0.22127  -0.15015 -0.10797 390 TRP A CH2 
2714 N N   . LYS A 391 ? 0.79502 0.41471 0.58268 0.14411  0.02906  -0.04668 391 LYS A N   
2715 C CA  . LYS A 391 ? 0.77753 0.39708 0.54789 0.12574  0.06638  -0.04399 391 LYS A CA  
2716 C C   . LYS A 391 ? 0.73956 0.38522 0.55978 0.11646  0.08967  -0.07746 391 LYS A C   
2717 O O   . LYS A 391 ? 0.71351 0.36562 0.53295 0.10258  0.11189  -0.08426 391 LYS A O   
2718 C CB  . LYS A 391 ? 0.75836 0.35622 0.49111 0.12230  0.07779  -0.02519 391 LYS A CB  
2719 C CG  . LYS A 391 ? 0.76326 0.34921 0.46072 0.10575  0.10997  -0.01563 391 LYS A CG  
2720 C CD  . LYS A 391 ? 0.78173 0.34383 0.43687 0.10590  0.11348  0.00615  391 LYS A CD  
2721 C CE  . LYS A 391 ? 0.84050 0.38713 0.46151 0.09142  0.14355  0.01180  391 LYS A CE  
2722 N NZ  . LYS A 391 ? 0.89916 0.42351 0.48088 0.09306  0.14501  0.03111  391 LYS A NZ  
2723 N N   . GLU A 392 ? 0.71045 0.37086 0.57429 0.12313  0.08540  -0.10029 392 GLU A N   
2724 C CA  . GLU A 392 ? 0.70841 0.39624 0.62380 0.11268  0.10925  -0.13639 392 GLU A CA  
2725 C C   . GLU A 392 ? 0.69969 0.41372 0.65673 0.11397  0.10177  -0.15958 392 GLU A C   
2726 O O   . GLU A 392 ? 0.69218 0.42236 0.67008 0.09727  0.13026  -0.18082 392 GLU A O   
2727 C CB  . GLU A 392 ? 0.70128 0.40187 0.65853 0.12170  0.10241  -0.15791 392 GLU A CB  
2728 C CG  . GLU A 392 ? 0.69493 0.42710 0.71066 0.10993  0.12794  -0.19976 392 GLU A CG  
2729 C CD  . GLU A 392 ? 0.70870 0.44679 0.74994 0.11198  0.13397  -0.21574 392 GLU A CD  
2730 O OE1 . GLU A 392 ? 0.69721 0.43035 0.74473 0.13192  0.10266  -0.21015 392 GLU A OE1 
2731 O OE2 . GLU A 392 ? 0.70417 0.44936 0.75658 0.09286  0.17033  -0.23421 392 GLU A OE2 
2732 N N   . LEU A 393 ? 0.69947 0.41537 0.66654 0.13295  0.06367  -0.15654 393 LEU A N   
2733 C CA  . LEU A 393 ? 0.68426 0.42429 0.69104 0.13648  0.05270  -0.17871 393 LEU A CA  
2734 C C   . LEU A 393 ? 0.68111 0.41645 0.65729 0.12009  0.07413  -0.16612 393 LEU A C   
2735 O O   . LEU A 393 ? 0.66739 0.42662 0.67874 0.11050  0.08917  -0.19142 393 LEU A O   
2736 C CB  . LEU A 393 ? 0.69070 0.42327 0.70020 0.16053  0.00520  -0.17287 393 LEU A CB  
2737 C CG  . LEU A 393 ? 0.70290 0.45159 0.76785 0.18005  -0.02276 -0.20278 393 LEU A CG  
2738 C CD1 . LEU A 393 ? 0.75118 0.48262 0.80624 0.20301  -0.07120 -0.19455 393 LEU A CD1 
2739 C CD2 . LEU A 393 ? 0.68653 0.47875 0.82603 0.17463  -0.00717 -0.24975 393 LEU A CD2 
2740 N N   . ILE A 394 ? 0.71034 0.41544 0.62204 0.11649  0.07582  -0.12892 394 ILE A N   
2741 C CA  . ILE A 394 ? 0.72664 0.42435 0.60554 0.10227  0.09426  -0.11596 394 ILE A CA  
2742 C C   . ILE A 394 ? 0.73177 0.42609 0.60035 0.08006  0.13687  -0.12366 394 ILE A C   
2743 O O   . ILE A 394 ? 0.77101 0.47123 0.64126 0.06565  0.15756  -0.13356 394 ILE A O   
2744 C CB  . ILE A 394 ? 0.70516 0.37334 0.52177 0.10701  0.07953  -0.07695 394 ILE A CB  
2745 C CG1 . ILE A 394 ? 0.71905 0.38664 0.54043 0.12486  0.04002  -0.07120 394 ILE A CG1 
2746 C CG2 . ILE A 394 ? 0.66349 0.32081 0.44144 0.09184  0.10155  -0.06297 394 ILE A CG2 
2747 C CD1 . ILE A 394 ? 0.68911 0.32692 0.45308 0.12999  0.02345  -0.03646 394 ILE A CD1 
2748 N N   . TYR A 395 ? 0.73039 0.41194 0.58521 0.07642  0.15045  -0.11964 395 TYR A N   
2749 C CA  . TYR A 395 ? 0.73312 0.40311 0.56900 0.05498  0.19009  -0.12553 395 TYR A CA  
2750 C C   . TYR A 395 ? 0.76443 0.46169 0.65307 0.04110  0.21327  -0.16541 395 TYR A C   
2751 O O   . TYR A 395 ? 0.73774 0.42637 0.60900 0.02045  0.24413  -0.17213 395 TYR A O   
2752 C CB  . TYR A 395 ? 0.75287 0.40506 0.56831 0.05580  0.19675  -0.11577 395 TYR A CB  
2753 C CG  . TYR A 395 ? 0.78931 0.42254 0.57838 0.03423  0.23597  -0.12096 395 TYR A CG  
2754 C CD1 . TYR A 395 ? 0.79234 0.40006 0.52429 0.02257  0.24555  -0.09458 395 TYR A CD1 
2755 C CD2 . TYR A 395 ? 0.73942 0.39254 0.56792 0.02308  0.25246  -0.14621 395 TYR A CD2 
2756 C CE1 . TYR A 395 ? 0.82240 0.42297 0.53876 0.00045  0.26508  -0.08963 395 TYR A CE1 
2757 C CE2 . TYR A 395 ? 0.75910 0.40585 0.56790 -0.00062 0.27537  -0.14082 395 TYR A CE2 
2758 C CZ  . TYR A 395 ? 0.81087 0.42808 0.56267 -0.01142 0.28065  -0.11202 395 TYR A CZ  
2759 O OH  . TYR A 395 ? 0.84008 0.44147 0.57174 -0.03363 0.29866  -0.10620 395 TYR A OH  
2760 N N   . LYS A 396 ? 0.77459 0.50368 0.72733 0.05176  0.19864  -0.19409 396 LYS A N   
2761 C CA  . LYS A 396 ? 0.78193 0.54223 0.79237 0.03827  0.22092  -0.23717 396 LYS A CA  
2762 C C   . LYS A 396 ? 0.75197 0.52836 0.77907 0.03340  0.22078  -0.24846 396 LYS A C   
2763 O O   . LYS A 396 ? 0.76141 0.55645 0.81323 0.01291  0.24692  -0.27308 396 LYS A O   
2764 C CB  . LYS A 396 ? 0.80920 0.60139 0.88772 0.05358  0.20179  -0.26764 396 LYS A CB  
2765 C CG  . LYS A 396 ? 0.74499 0.55360 0.85504 0.08009  0.15562  -0.26948 396 LYS A CG  
2766 C CD  . LYS A 396 ? 0.74339 0.58167 0.92183 0.09563  0.13643  -0.30412 396 LYS A CD  
2767 C CE  . LYS A 396 ? 0.70081 0.52437 0.86509 0.09741  0.14149  -0.29576 396 LYS A CE  
2768 N NZ  . LYS A 396 ? 0.81706 0.66251 1.03864 0.11908  0.11151  -0.32187 396 LYS A NZ  
2769 N N   . GLU A 397 ? 0.74599 0.51820 0.75789 0.05000  0.18862  -0.22668 397 GLU A N   
2770 C CA  . GLU A 397 ? 0.78462 0.56883 0.80581 0.04534  0.18837  -0.23369 397 GLU A CA  
2771 C C   . GLU A 397 ? 0.80321 0.56057 0.76843 0.02288  0.22071  -0.21696 397 GLU A C   
2772 O O   . GLU A 397 ? 0.84257 0.61100 0.82148 0.00833  0.23882  -0.23476 397 GLU A O   
2773 C CB  . GLU A 397 ? 0.76796 0.55013 0.78153 0.06836  0.14550  -0.21338 397 GLU A CB  
2774 C CG  . GLU A 397 ? 0.76998 0.58117 0.83002 0.07321  0.13177  -0.23742 397 GLU A CG  
2775 C CD  . GLU A 397 ? 0.77470 0.62498 0.91508 0.07941  0.12610  -0.28353 397 GLU A CD  
2776 O OE1 . GLU A 397 ? 0.74734 0.60313 0.91227 0.10204  0.09186  -0.28804 397 GLU A OE1 
2777 O OE2 . GLU A 397 ? 0.79401 0.66844 0.97247 0.06129  0.15577  -0.31689 397 GLU A OE2 
2778 N N   . VAL A 398 ? 0.78161 0.50237 0.68328 0.02027  0.22721  -0.18425 398 VAL A N   
2779 C CA  . VAL A 398 ? 0.81458 0.50407 0.65887 0.00046  0.25603  -0.16960 398 VAL A CA  
2780 C C   . VAL A 398 ? 0.91852 0.61879 0.77892 -0.02584 0.28506  -0.18669 398 VAL A C   
2781 O O   . VAL A 398 ? 0.92933 0.62611 0.77648 -0.04625 0.30132  -0.18572 398 VAL A O   
2782 C CB  . VAL A 398 ? 0.79400 0.44619 0.57187 0.00683  0.24867  -0.13071 398 VAL A CB  
2783 C CG1 . VAL A 398 ? 0.83484 0.46391 0.56527 -0.01465 0.26759  -0.11203 398 VAL A CG1 
2784 C CG2 . VAL A 398 ? 0.79565 0.44747 0.55786 0.02568  0.21381  -0.10477 398 VAL A CG2 
2785 N N   . MET A 399 ? 0.89624 0.60908 0.78539 -0.02659 0.28905  -0.20031 399 MET A N   
2786 C CA  . MET A 399 ? 0.94438 0.66644 0.84850 -0.05299 0.31454  -0.21452 399 MET A CA  
2787 C C   . MET A 399 ? 1.04209 0.80342 1.00758 -0.06436 0.32354  -0.25066 399 MET A C   
2788 O O   . MET A 399 ? 1.08151 0.84260 1.04712 -0.09185 0.34787  -0.25884 399 MET A O   
2789 C CB  . MET A 399 ? 0.88984 0.61496 0.80746 -0.05012 0.31561  -0.21897 399 MET A CB  
2790 C CG  . MET A 399 ? 0.86303 0.54869 0.71863 -0.04649 0.31260  -0.18370 399 MET A CG  
2791 S SD  . MET A 399 ? 0.90046 0.54403 0.68306 -0.05831 0.31642  -0.14813 399 MET A SD  
2792 C CE  . MET A 399 ? 0.93961 0.56014 0.70348 -0.08973 0.34214  -0.14766 399 MET A CE  
2793 N N   . ASN A 400 ? 1.22628 1.01881 1.24404 -0.04404 0.30256  -0.27254 400 ASN A N   
2794 C CA  . ASN A 400 ? 1.18047 1.01581 1.26408 -0.05082 0.30478  -0.30853 400 ASN A CA  
2795 C C   . ASN A 400 ? 1.25352 1.11156 1.37376 -0.07669 0.32974  -0.33338 400 ASN A C   
2796 O O   . ASN A 400 ? 1.24591 1.13655 1.42323 -0.06969 0.32184  -0.35926 400 ASN A O   
2797 C CB  . ASN A 400 ? 1.22745 1.05600 1.29061 -0.06016 0.31082  -0.30244 400 ASN A CB  
2798 C CG  . ASN A 400 ? 1.34760 1.15776 1.37764 -0.09439 0.34311  -0.29542 400 ASN A CG  
2799 O OD1 . ASN A 400 ? 1.38219 1.21590 1.45165 -0.11638 0.36215  -0.32175 400 ASN A OD1 
2800 N ND2 . ASN A 400 ? 1.37851 1.14404 1.33601 -0.09935 0.34738  -0.26006 400 ASN A ND2 
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