data_9HRH
# 
_entry.id   9HRH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9HRH         pdb_00009hrh 10.2210/pdb9hrh/pdb 
WWPDB D_1292142963 ?            ?                   
# 
_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       2025-05-14 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HRH 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mita.bertoldi@univr.it 
_pdbx_contact_author.name_first         Mariarita 
_pdbx_contact_author.name_last          Bertoldi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2337-9928 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Perduca, M.'  1 0000-0001-8291-0523 
'Bisello, G.'  2 0000-0002-3803-9555 
'Bertoldi, M.' 3 0000-0002-2337-9928 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;The CRISPR-Cas9 knockout DDC SH-SY5Y in vitro model for AADC deficiency provides insight into the pathogenicity of R347Q and L353P variants: a cross-sectional structural and functional analysis.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.70120 
_citation.pdbx_database_id_PubMed   40318155 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Carmona-Carmona, C.A.' 1  ?                   
primary 'Bisello, G.'           2  ?                   
primary 'Franchini, R.'         3  ?                   
primary 'Lunardi, G.'           4  ?                   
primary 'Galavotti, R.'         5  ?                   
primary 'Perduca, M.'           6  ?                   
primary 'Ribeiro, R.P.'         7  ?                   
primary 'Belviso, B.D.'         8  ?                   
primary 'Giorgetti, A.'         9  ?                   
primary 'Caliandro, R.'         10 ?                   
primary 'Lievens, P.M.'         11 0000-0003-4439-1106 
primary 'Bertoldi, M.'          12 0000-0002-2337-9928 
# 
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 'Aromatic-L-amino-acid decarboxylase' 54162.246 1   4.1.1.28 ? ? ? 
2 non-polymer syn 'TETRAETHYLENE GLYCOL'                194.226   2   ?        ? ? ? 
3 water       nat water                                 18.015    353 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'DOPA decarboxylase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDVEKIIMPGVTHWHSPYFFAYF
PTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAAR
TKVIHRLQAASPELTQAAIMEKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPH(LLP)WLLVNFDCSAMWV
KKRTDLTGAFRLDPTYLKHSHQDSGLITDYQHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDP
RFEICVEVILGLVCFRLKGSNKVNEALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLR
AERE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDVEKIIMPGVTHWHSPYFFAYF
PTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAAR
TKVIHRLQAASPELTQAAIMEKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKKRT
DLTGAFRLDPTYLKHSHQDSGLITDYQHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEI
CVEVILGLVCFRLKGSNKVNEALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
;
_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 'TETRAETHYLENE GLYCOL' PG4 
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   ASN n 
1 3   ALA n 
1 4   SER n 
1 5   GLU n 
1 6   PHE n 
1 7   ARG n 
1 8   ARG n 
1 9   ARG n 
1 10  GLY n 
1 11  LYS n 
1 12  GLU n 
1 13  MET n 
1 14  VAL n 
1 15  ASP n 
1 16  TYR n 
1 17  VAL n 
1 18  ALA n 
1 19  ASN n 
1 20  TYR n 
1 21  MET n 
1 22  GLU n 
1 23  GLY n 
1 24  ILE n 
1 25  GLU n 
1 26  GLY n 
1 27  ARG n 
1 28  GLN n 
1 29  VAL n 
1 30  TYR n 
1 31  PRO n 
1 32  ASP n 
1 33  VAL n 
1 34  GLU n 
1 35  PRO n 
1 36  GLY n 
1 37  TYR n 
1 38  LEU n 
1 39  ARG n 
1 40  PRO n 
1 41  LEU n 
1 42  ILE n 
1 43  PRO n 
1 44  ALA n 
1 45  ALA n 
1 46  ALA n 
1 47  PRO n 
1 48  GLN n 
1 49  GLU n 
1 50  PRO n 
1 51  ASP n 
1 52  THR n 
1 53  PHE n 
1 54  GLU n 
1 55  ASP n 
1 56  ILE n 
1 57  ILE n 
1 58  ASN n 
1 59  ASP n 
1 60  VAL n 
1 61  GLU n 
1 62  LYS n 
1 63  ILE n 
1 64  ILE n 
1 65  MET n 
1 66  PRO n 
1 67  GLY n 
1 68  VAL n 
1 69  THR n 
1 70  HIS n 
1 71  TRP n 
1 72  HIS n 
1 73  SER n 
1 74  PRO n 
1 75  TYR n 
1 76  PHE n 
1 77  PHE n 
1 78  ALA n 
1 79  TYR n 
1 80  PHE n 
1 81  PRO n 
1 82  THR n 
1 83  ALA n 
1 84  SER n 
1 85  SER n 
1 86  TYR n 
1 87  PRO n 
1 88  ALA n 
1 89  MET n 
1 90  LEU n 
1 91  ALA n 
1 92  ASP n 
1 93  MET n 
1 94  LEU n 
1 95  CYS n 
1 96  GLY n 
1 97  ALA n 
1 98  ILE n 
1 99  GLY n 
1 100 CYS n 
1 101 ILE n 
1 102 GLY n 
1 103 PHE n 
1 104 SER n 
1 105 TRP n 
1 106 ALA n 
1 107 ALA n 
1 108 SER n 
1 109 PRO n 
1 110 ALA n 
1 111 CYS n 
1 112 THR n 
1 113 GLU n 
1 114 LEU n 
1 115 GLU n 
1 116 THR n 
1 117 VAL n 
1 118 MET n 
1 119 MET n 
1 120 ASP n 
1 121 TRP n 
1 122 LEU n 
1 123 GLY n 
1 124 LYS n 
1 125 MET n 
1 126 LEU n 
1 127 GLU n 
1 128 LEU n 
1 129 PRO n 
1 130 LYS n 
1 131 ALA n 
1 132 PHE n 
1 133 LEU n 
1 134 ASN n 
1 135 GLU n 
1 136 LYS n 
1 137 ALA n 
1 138 GLY n 
1 139 GLU n 
1 140 GLY n 
1 141 GLY n 
1 142 GLY n 
1 143 VAL n 
1 144 ILE n 
1 145 GLN n 
1 146 GLY n 
1 147 SER n 
1 148 ALA n 
1 149 SER n 
1 150 GLU n 
1 151 ALA n 
1 152 THR n 
1 153 LEU n 
1 154 VAL n 
1 155 ALA n 
1 156 LEU n 
1 157 LEU n 
1 158 ALA n 
1 159 ALA n 
1 160 ARG n 
1 161 THR n 
1 162 LYS n 
1 163 VAL n 
1 164 ILE n 
1 165 HIS n 
1 166 ARG n 
1 167 LEU n 
1 168 GLN n 
1 169 ALA n 
1 170 ALA n 
1 171 SER n 
1 172 PRO n 
1 173 GLU n 
1 174 LEU n 
1 175 THR n 
1 176 GLN n 
1 177 ALA n 
1 178 ALA n 
1 179 ILE n 
1 180 MET n 
1 181 GLU n 
1 182 LYS n 
1 183 LEU n 
1 184 VAL n 
1 185 ALA n 
1 186 TYR n 
1 187 SER n 
1 188 SER n 
1 189 ASP n 
1 190 GLN n 
1 191 ALA n 
1 192 HIS n 
1 193 SER n 
1 194 SER n 
1 195 VAL n 
1 196 GLU n 
1 197 ARG n 
1 198 ALA n 
1 199 GLY n 
1 200 LEU n 
1 201 ILE n 
1 202 GLY n 
1 203 GLY n 
1 204 VAL n 
1 205 LYS n 
1 206 LEU n 
1 207 LYS n 
1 208 ALA n 
1 209 ILE n 
1 210 PRO n 
1 211 SER n 
1 212 ASP n 
1 213 GLY n 
1 214 ASN n 
1 215 PHE n 
1 216 ALA n 
1 217 MET n 
1 218 ARG n 
1 219 ALA n 
1 220 SER n 
1 221 ALA n 
1 222 LEU n 
1 223 GLN n 
1 224 GLU n 
1 225 ALA n 
1 226 LEU n 
1 227 GLU n 
1 228 ARG n 
1 229 ASP n 
1 230 LYS n 
1 231 ALA n 
1 232 ALA n 
1 233 GLY n 
1 234 LEU n 
1 235 ILE n 
1 236 PRO n 
1 237 PHE n 
1 238 PHE n 
1 239 MET n 
1 240 VAL n 
1 241 ALA n 
1 242 THR n 
1 243 LEU n 
1 244 GLY n 
1 245 THR n 
1 246 THR n 
1 247 THR n 
1 248 CYS n 
1 249 CYS n 
1 250 SER n 
1 251 PHE n 
1 252 ASP n 
1 253 ASN n 
1 254 LEU n 
1 255 LEU n 
1 256 GLU n 
1 257 VAL n 
1 258 GLY n 
1 259 PRO n 
1 260 ILE n 
1 261 CYS n 
1 262 ASN n 
1 263 LYS n 
1 264 GLU n 
1 265 ASP n 
1 266 ILE n 
1 267 TRP n 
1 268 LEU n 
1 269 HIS n 
1 270 VAL n 
1 271 ASP n 
1 272 ALA n 
1 273 ALA n 
1 274 TYR n 
1 275 ALA n 
1 276 GLY n 
1 277 SER n 
1 278 ALA n 
1 279 PHE n 
1 280 ILE n 
1 281 CYS n 
1 282 PRO n 
1 283 GLU n 
1 284 PHE n 
1 285 ARG n 
1 286 HIS n 
1 287 LEU n 
1 288 LEU n 
1 289 ASN n 
1 290 GLY n 
1 291 VAL n 
1 292 GLU n 
1 293 PHE n 
1 294 ALA n 
1 295 ASP n 
1 296 SER n 
1 297 PHE n 
1 298 ASN n 
1 299 PHE n 
1 300 ASN n 
1 301 PRO n 
1 302 HIS n 
1 303 LLP n 
1 304 TRP n 
1 305 LEU n 
1 306 LEU n 
1 307 VAL n 
1 308 ASN n 
1 309 PHE n 
1 310 ASP n 
1 311 CYS n 
1 312 SER n 
1 313 ALA n 
1 314 MET n 
1 315 TRP n 
1 316 VAL n 
1 317 LYS n 
1 318 LYS n 
1 319 ARG n 
1 320 THR n 
1 321 ASP n 
1 322 LEU n 
1 323 THR n 
1 324 GLY n 
1 325 ALA n 
1 326 PHE n 
1 327 ARG n 
1 328 LEU n 
1 329 ASP n 
1 330 PRO n 
1 331 THR n 
1 332 TYR n 
1 333 LEU n 
1 334 LYS n 
1 335 HIS n 
1 336 SER n 
1 337 HIS n 
1 338 GLN n 
1 339 ASP n 
1 340 SER n 
1 341 GLY n 
1 342 LEU n 
1 343 ILE n 
1 344 THR n 
1 345 ASP n 
1 346 TYR n 
1 347 GLN n 
1 348 HIS n 
1 349 TRP n 
1 350 GLN n 
1 351 ILE n 
1 352 PRO n 
1 353 LEU n 
1 354 GLY n 
1 355 ARG n 
1 356 ARG n 
1 357 PHE n 
1 358 ARG n 
1 359 SER n 
1 360 LEU n 
1 361 LYS n 
1 362 MET n 
1 363 TRP n 
1 364 PHE n 
1 365 VAL n 
1 366 PHE n 
1 367 ARG n 
1 368 MET n 
1 369 TYR n 
1 370 GLY n 
1 371 VAL n 
1 372 LYS n 
1 373 GLY n 
1 374 LEU n 
1 375 GLN n 
1 376 ALA n 
1 377 TYR n 
1 378 ILE n 
1 379 ARG n 
1 380 LYS n 
1 381 HIS n 
1 382 VAL n 
1 383 GLN n 
1 384 LEU n 
1 385 SER n 
1 386 HIS n 
1 387 GLU n 
1 388 PHE n 
1 389 GLU n 
1 390 SER n 
1 391 LEU n 
1 392 VAL n 
1 393 ARG n 
1 394 GLN n 
1 395 ASP n 
1 396 PRO n 
1 397 ARG n 
1 398 PHE n 
1 399 GLU n 
1 400 ILE n 
1 401 CYS n 
1 402 VAL n 
1 403 GLU n 
1 404 VAL n 
1 405 ILE n 
1 406 LEU n 
1 407 GLY n 
1 408 LEU n 
1 409 VAL n 
1 410 CYS n 
1 411 PHE n 
1 412 ARG n 
1 413 LEU n 
1 414 LYS n 
1 415 GLY n 
1 416 SER n 
1 417 ASN n 
1 418 LYS n 
1 419 VAL n 
1 420 ASN n 
1 421 GLU n 
1 422 ALA n 
1 423 LEU n 
1 424 LEU n 
1 425 GLN n 
1 426 ARG n 
1 427 ILE n 
1 428 ASN n 
1 429 SER n 
1 430 ALA n 
1 431 LYS n 
1 432 LYS n 
1 433 ILE n 
1 434 HIS n 
1 435 LEU n 
1 436 VAL n 
1 437 PRO n 
1 438 CYS n 
1 439 HIS n 
1 440 LEU n 
1 441 ARG n 
1 442 ASP n 
1 443 LYS n 
1 444 PHE n 
1 445 VAL n 
1 446 LEU n 
1 447 ARG n 
1 448 PHE n 
1 449 ALA n 
1 450 ILE n 
1 451 CYS n 
1 452 SER n 
1 453 ARG n 
1 454 THR n 
1 455 VAL n 
1 456 GLU n 
1 457 SER n 
1 458 ALA n 
1 459 HIS n 
1 460 VAL n 
1 461 GLN n 
1 462 ARG n 
1 463 ALA n 
1 464 TRP n 
1 465 GLU n 
1 466 HIS n 
1 467 ILE n 
1 468 LYS n 
1 469 GLU n 
1 470 LEU n 
1 471 ALA n 
1 472 ALA n 
1 473 ASP n 
1 474 VAL n 
1 475 LEU n 
1 476 ARG n 
1 477 ALA n 
1 478 GLU n 
1 479 ARG n 
1 480 GLU 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                   480 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DDC, hCG_1811384, tcag7.584' 
_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 
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 
LLP 'L-peptide linking' n '(2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid' 
"N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE" 'C14 H22 N3 O7 P' 375.314 
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 
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL'                                                                                  
?                                      'C8 H18 O5'       194.226 
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   1   MET MET A . n 
A 1 2   ASN 2   2   2   ASN ASN A . n 
A 1 3   ALA 3   3   3   ALA ALA A . n 
A 1 4   SER 4   4   4   SER SER A . n 
A 1 5   GLU 5   5   5   GLU GLU A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   ARG 7   7   7   ARG ARG A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  TYR 16  16  16  TYR TYR A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  TYR 20  20  20  TYR TYR A . n 
A 1 21  MET 21  21  21  MET MET A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  PRO 31  31  31  PRO PRO A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PRO 50  50  50  PRO PRO A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  VAL 60  60  60  VAL VAL A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  MET 65  65  65  MET MET A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  HIS 70  70  70  HIS HIS A . n 
A 1 71  TRP 71  71  71  TRP TRP A . n 
A 1 72  HIS 72  72  72  HIS HIS A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  PHE 77  77  77  PHE PHE A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  PRO 81  81  81  PRO PRO A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  MET 89  89  89  MET MET A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  MET 93  93  93  MET MET A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  CYS 95  95  95  CYS CYS A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 CYS 100 100 100 CYS CYS A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 TRP 105 105 105 TRP TRP A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 PRO 109 109 109 PRO PRO A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 TRP 121 121 121 TRP TRP A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 MET 125 125 125 MET MET A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 LYS 130 130 130 LYS LYS A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 GLN 145 145 145 GLN GLN A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 VAL 154 154 154 VAL VAL A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 ARG 160 160 160 ARG ARG A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 HIS 165 165 165 HIS HIS A . n 
A 1 166 ARG 166 166 166 ARG ARG A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 GLN 168 168 168 GLN GLN A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 GLN 176 176 176 GLN GLN A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 MET 180 180 180 MET MET A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 LYS 182 182 182 LYS LYS A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 GLN 190 190 190 GLN GLN A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 HIS 192 192 192 HIS HIS A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 GLU 196 196 196 GLU GLU A . n 
A 1 197 ARG 197 197 197 ARG ARG A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 PRO 210 210 210 PRO PRO A . n 
A 1 211 SER 211 211 211 SER SER A . n 
A 1 212 ASP 212 212 212 ASP ASP A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 PHE 215 215 215 PHE PHE A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 MET 217 217 217 MET MET A . n 
A 1 218 ARG 218 218 218 ARG ARG A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 GLN 223 223 223 GLN GLN A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 PHE 237 237 237 PHE PHE A . n 
A 1 238 PHE 238 238 238 PHE PHE A . n 
A 1 239 MET 239 239 239 MET MET A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 THR 247 247 247 THR THR A . n 
A 1 248 CYS 248 248 248 CYS CYS A . n 
A 1 249 CYS 249 249 249 CYS CYS A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 PRO 259 259 259 PRO PRO A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 CYS 261 261 261 CYS CYS A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 LYS 263 263 263 LYS LYS A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 ASP 265 265 265 ASP ASP A . n 
A 1 266 ILE 266 266 266 ILE ILE A . n 
A 1 267 TRP 267 267 267 TRP TRP A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 HIS 269 269 269 HIS HIS A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 ASP 271 271 271 ASP ASP A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 TYR 274 274 274 TYR TYR A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 CYS 281 281 281 CYS CYS A . n 
A 1 282 PRO 282 282 282 PRO PRO A . n 
A 1 283 GLU 283 283 283 GLU GLU A . n 
A 1 284 PHE 284 284 284 PHE PHE A . n 
A 1 285 ARG 285 285 285 ARG ARG A . n 
A 1 286 HIS 286 286 286 HIS HIS A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 ASN 289 289 289 ASN ASN A . n 
A 1 290 GLY 290 290 290 GLY GLY A . n 
A 1 291 VAL 291 291 291 VAL VAL A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 PHE 293 293 293 PHE PHE A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 SER 296 296 296 SER SER A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 PHE 299 299 299 PHE PHE A . n 
A 1 300 ASN 300 300 300 ASN ASN A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 HIS 302 302 302 HIS HIS A . n 
A 1 303 LLP 303 303 501 LLP PLP A . n 
A 1 304 TRP 304 304 304 TRP TRP A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 VAL 307 307 307 VAL VAL A . n 
A 1 308 ASN 308 308 308 ASN ASN A . n 
A 1 309 PHE 309 309 309 PHE PHE A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 CYS 311 311 311 CYS CYS A . n 
A 1 312 SER 312 312 312 SER SER A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 MET 314 314 314 MET MET A . n 
A 1 315 TRP 315 315 315 TRP TRP A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 LYS 317 317 317 LYS LYS A . n 
A 1 318 LYS 318 318 318 LYS LYS A . n 
A 1 319 ARG 319 319 319 ARG ARG A . n 
A 1 320 THR 320 320 320 THR THR A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 THR 323 323 ?   ?   ?   A . n 
A 1 324 GLY 324 324 ?   ?   ?   A . n 
A 1 325 ALA 325 325 ?   ?   ?   A . n 
A 1 326 PHE 326 326 ?   ?   ?   A . n 
A 1 327 ARG 327 327 ?   ?   ?   A . n 
A 1 328 LEU 328 328 ?   ?   ?   A . n 
A 1 329 ASP 329 329 ?   ?   ?   A . n 
A 1 330 PRO 330 330 ?   ?   ?   A . n 
A 1 331 THR 331 331 ?   ?   ?   A . n 
A 1 332 TYR 332 332 ?   ?   ?   A . n 
A 1 333 LEU 333 333 ?   ?   ?   A . n 
A 1 334 LYS 334 334 ?   ?   ?   A . n 
A 1 335 HIS 335 335 ?   ?   ?   A . n 
A 1 336 SER 336 336 ?   ?   ?   A . n 
A 1 337 HIS 337 337 ?   ?   ?   A . n 
A 1 338 GLN 338 338 ?   ?   ?   A . n 
A 1 339 ASP 339 339 ?   ?   ?   A . n 
A 1 340 SER 340 340 ?   ?   ?   A . n 
A 1 341 GLY 341 341 ?   ?   ?   A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 ILE 343 343 343 ILE ILE A . n 
A 1 344 THR 344 344 344 THR THR A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 TYR 346 346 346 TYR TYR A . n 
A 1 347 GLN 347 347 347 GLN GLN A . n 
A 1 348 HIS 348 348 348 HIS HIS A . n 
A 1 349 TRP 349 349 349 TRP TRP A . n 
A 1 350 GLN 350 350 350 GLN GLN A . n 
A 1 351 ILE 351 351 351 ILE ILE A . n 
A 1 352 PRO 352 352 352 PRO PRO A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 ARG 355 355 355 ARG ARG A . n 
A 1 356 ARG 356 356 356 ARG ARG A . n 
A 1 357 PHE 357 357 357 PHE PHE A . n 
A 1 358 ARG 358 358 358 ARG ARG A . n 
A 1 359 SER 359 359 359 SER SER A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 LYS 361 361 361 LYS LYS A . n 
A 1 362 MET 362 362 362 MET MET A . n 
A 1 363 TRP 363 363 363 TRP TRP A . n 
A 1 364 PHE 364 364 364 PHE PHE A . n 
A 1 365 VAL 365 365 365 VAL VAL A . n 
A 1 366 PHE 366 366 366 PHE PHE A . n 
A 1 367 ARG 367 367 367 ARG ARG A . n 
A 1 368 MET 368 368 368 MET MET A . n 
A 1 369 TYR 369 369 369 TYR TYR A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 LYS 372 372 372 LYS LYS A . n 
A 1 373 GLY 373 373 373 GLY GLY A . n 
A 1 374 LEU 374 374 374 LEU LEU A . n 
A 1 375 GLN 375 375 375 GLN GLN A . n 
A 1 376 ALA 376 376 376 ALA ALA A . n 
A 1 377 TYR 377 377 377 TYR TYR A . n 
A 1 378 ILE 378 378 378 ILE ILE A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 LYS 380 380 380 LYS LYS A . n 
A 1 381 HIS 381 381 381 HIS HIS A . n 
A 1 382 VAL 382 382 382 VAL VAL A . n 
A 1 383 GLN 383 383 383 GLN GLN A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 SER 385 385 385 SER SER A . n 
A 1 386 HIS 386 386 386 HIS HIS A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 PHE 388 388 388 PHE PHE A . n 
A 1 389 GLU 389 389 389 GLU GLU A . n 
A 1 390 SER 390 390 390 SER SER A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 VAL 392 392 392 VAL VAL A . n 
A 1 393 ARG 393 393 393 ARG ARG A . n 
A 1 394 GLN 394 394 394 GLN GLN A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 PRO 396 396 396 PRO PRO A . n 
A 1 397 ARG 397 397 397 ARG ARG A . n 
A 1 398 PHE 398 398 398 PHE PHE A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 ILE 400 400 400 ILE ILE A . n 
A 1 401 CYS 401 401 401 CYS CYS A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 GLU 403 403 403 GLU GLU A . n 
A 1 404 VAL 404 404 404 VAL VAL A . n 
A 1 405 ILE 405 405 405 ILE ILE A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 GLY 407 407 407 GLY GLY A . n 
A 1 408 LEU 408 408 408 LEU LEU A . n 
A 1 409 VAL 409 409 409 VAL VAL A . n 
A 1 410 CYS 410 410 410 CYS CYS A . n 
A 1 411 PHE 411 411 411 PHE PHE A . n 
A 1 412 ARG 412 412 412 ARG ARG A . n 
A 1 413 LEU 413 413 413 LEU LEU A . n 
A 1 414 LYS 414 414 414 LYS LYS A . n 
A 1 415 GLY 415 415 415 GLY GLY A . n 
A 1 416 SER 416 416 416 SER SER A . n 
A 1 417 ASN 417 417 417 ASN ASN A . n 
A 1 418 LYS 418 418 418 LYS LYS A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 ASN 420 420 420 ASN ASN A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 ALA 422 422 422 ALA ALA A . n 
A 1 423 LEU 423 423 423 LEU LEU A . n 
A 1 424 LEU 424 424 424 LEU LEU A . n 
A 1 425 GLN 425 425 425 GLN GLN A . n 
A 1 426 ARG 426 426 426 ARG ARG A . n 
A 1 427 ILE 427 427 427 ILE ILE A . n 
A 1 428 ASN 428 428 428 ASN ASN A . n 
A 1 429 SER 429 429 429 SER SER A . n 
A 1 430 ALA 430 430 430 ALA ALA A . n 
A 1 431 LYS 431 431 431 LYS LYS A . n 
A 1 432 LYS 432 432 432 LYS LYS A . n 
A 1 433 ILE 433 433 433 ILE ILE A . n 
A 1 434 HIS 434 434 434 HIS HIS A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 VAL 436 436 436 VAL VAL A . n 
A 1 437 PRO 437 437 437 PRO PRO A . n 
A 1 438 CYS 438 438 438 CYS CYS A . n 
A 1 439 HIS 439 439 439 HIS HIS A . n 
A 1 440 LEU 440 440 440 LEU LEU A . n 
A 1 441 ARG 441 441 441 ARG ARG A . n 
A 1 442 ASP 442 442 442 ASP ASP A . n 
A 1 443 LYS 443 443 443 LYS LYS A . n 
A 1 444 PHE 444 444 444 PHE PHE A . n 
A 1 445 VAL 445 445 445 VAL VAL A . n 
A 1 446 LEU 446 446 446 LEU LEU A . n 
A 1 447 ARG 447 447 447 ARG ARG A . n 
A 1 448 PHE 448 448 448 PHE PHE A . n 
A 1 449 ALA 449 449 449 ALA ALA A . n 
A 1 450 ILE 450 450 450 ILE ILE A . n 
A 1 451 CYS 451 451 451 CYS CYS A . n 
A 1 452 SER 452 452 452 SER SER A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 THR 454 454 454 THR THR A . n 
A 1 455 VAL 455 455 455 VAL VAL A . n 
A 1 456 GLU 456 456 456 GLU GLU A . n 
A 1 457 SER 457 457 457 SER SER A . n 
A 1 458 ALA 458 458 458 ALA ALA A . n 
A 1 459 HIS 459 459 459 HIS HIS A . n 
A 1 460 VAL 460 460 460 VAL VAL A . n 
A 1 461 GLN 461 461 461 GLN GLN A . n 
A 1 462 ARG 462 462 462 ARG ARG A . n 
A 1 463 ALA 463 463 463 ALA ALA A . n 
A 1 464 TRP 464 464 464 TRP TRP A . n 
A 1 465 GLU 465 465 465 GLU GLU A . n 
A 1 466 HIS 466 466 466 HIS HIS A . n 
A 1 467 ILE 467 467 467 ILE ILE A . n 
A 1 468 LYS 468 468 468 LYS LYS A . n 
A 1 469 GLU 469 469 469 GLU GLU A . n 
A 1 470 LEU 470 470 470 LEU LEU A . n 
A 1 471 ALA 471 471 471 ALA ALA A . n 
A 1 472 ALA 472 472 472 ALA ALA A . n 
A 1 473 ASP 473 473 473 ASP ASP A . n 
A 1 474 VAL 474 474 474 VAL VAL A . n 
A 1 475 LEU 475 475 475 LEU LEU A . n 
A 1 476 ARG 476 476 476 ARG ARG A . n 
A 1 477 ALA 477 477 477 ALA ALA A . n 
A 1 478 GLU 478 478 478 GLU GLU A . n 
A 1 479 ARG 479 479 479 ARG ARG A . n 
A 1 480 GLU 480 480 480 GLU GLU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        LLP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   LLP 
_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 PG4 1   601  601  PG4 PG4 A . 
C 2 PG4 1   602  602  PG4 PG4 A . 
D 3 HOH 1   701  956  HOH HOH A . 
D 3 HOH 2   702  858  HOH HOH A . 
D 3 HOH 3   703  976  HOH HOH A . 
D 3 HOH 4   704  983  HOH HOH A . 
D 3 HOH 5   705  701  HOH HOH A . 
D 3 HOH 6   706  1036 HOH HOH A . 
D 3 HOH 7   707  903  HOH HOH A . 
D 3 HOH 8   708  707  HOH HOH A . 
D 3 HOH 9   709  1005 HOH HOH A . 
D 3 HOH 10  710  1000 HOH HOH A . 
D 3 HOH 11  711  991  HOH HOH A . 
D 3 HOH 12  712  743  HOH HOH A . 
D 3 HOH 13  713  926  HOH HOH A . 
D 3 HOH 14  714  923  HOH HOH A . 
D 3 HOH 15  715  713  HOH HOH A . 
D 3 HOH 16  716  792  HOH HOH A . 
D 3 HOH 17  717  787  HOH HOH A . 
D 3 HOH 18  718  993  HOH HOH A . 
D 3 HOH 19  719  730  HOH HOH A . 
D 3 HOH 20  720  806  HOH HOH A . 
D 3 HOH 21  721  941  HOH HOH A . 
D 3 HOH 22  722  871  HOH HOH A . 
D 3 HOH 23  723  1001 HOH HOH A . 
D 3 HOH 24  724  765  HOH HOH A . 
D 3 HOH 25  725  1049 HOH HOH A . 
D 3 HOH 26  726  826  HOH HOH A . 
D 3 HOH 27  727  768  HOH HOH A . 
D 3 HOH 28  728  915  HOH HOH A . 
D 3 HOH 29  729  869  HOH HOH A . 
D 3 HOH 30  730  898  HOH HOH A . 
D 3 HOH 31  731  947  HOH HOH A . 
D 3 HOH 32  732  1032 HOH HOH A . 
D 3 HOH 33  733  880  HOH HOH A . 
D 3 HOH 34  734  740  HOH HOH A . 
D 3 HOH 35  735  917  HOH HOH A . 
D 3 HOH 36  736  884  HOH HOH A . 
D 3 HOH 37  737  913  HOH HOH A . 
D 3 HOH 38  738  1006 HOH HOH A . 
D 3 HOH 39  739  1004 HOH HOH A . 
D 3 HOH 40  740  948  HOH HOH A . 
D 3 HOH 41  741  876  HOH HOH A . 
D 3 HOH 42  742  821  HOH HOH A . 
D 3 HOH 43  743  873  HOH HOH A . 
D 3 HOH 44  744  852  HOH HOH A . 
D 3 HOH 45  745  825  HOH HOH A . 
D 3 HOH 46  746  954  HOH HOH A . 
D 3 HOH 47  747  818  HOH HOH A . 
D 3 HOH 48  748  896  HOH HOH A . 
D 3 HOH 49  749  779  HOH HOH A . 
D 3 HOH 50  750  911  HOH HOH A . 
D 3 HOH 51  751  772  HOH HOH A . 
D 3 HOH 52  752  762  HOH HOH A . 
D 3 HOH 53  753  928  HOH HOH A . 
D 3 HOH 54  754  790  HOH HOH A . 
D 3 HOH 55  755  943  HOH HOH A . 
D 3 HOH 56  756  1051 HOH HOH A . 
D 3 HOH 57  757  809  HOH HOH A . 
D 3 HOH 58  758  777  HOH HOH A . 
D 3 HOH 59  759  703  HOH HOH A . 
D 3 HOH 60  760  789  HOH HOH A . 
D 3 HOH 61  761  894  HOH HOH A . 
D 3 HOH 62  762  780  HOH HOH A . 
D 3 HOH 63  763  801  HOH HOH A . 
D 3 HOH 64  764  968  HOH HOH A . 
D 3 HOH 65  765  945  HOH HOH A . 
D 3 HOH 66  766  922  HOH HOH A . 
D 3 HOH 67  767  997  HOH HOH A . 
D 3 HOH 68  768  853  HOH HOH A . 
D 3 HOH 69  769  837  HOH HOH A . 
D 3 HOH 70  770  759  HOH HOH A . 
D 3 HOH 71  771  802  HOH HOH A . 
D 3 HOH 72  772  857  HOH HOH A . 
D 3 HOH 73  773  796  HOH HOH A . 
D 3 HOH 74  774  883  HOH HOH A . 
D 3 HOH 75  775  761  HOH HOH A . 
D 3 HOH 76  776  791  HOH HOH A . 
D 3 HOH 77  777  989  HOH HOH A . 
D 3 HOH 78  778  829  HOH HOH A . 
D 3 HOH 79  779  832  HOH HOH A . 
D 3 HOH 80  780  827  HOH HOH A . 
D 3 HOH 81  781  890  HOH HOH A . 
D 3 HOH 82  782  760  HOH HOH A . 
D 3 HOH 83  783  887  HOH HOH A . 
D 3 HOH 84  784  939  HOH HOH A . 
D 3 HOH 85  785  1030 HOH HOH A . 
D 3 HOH 86  786  925  HOH HOH A . 
D 3 HOH 87  787  865  HOH HOH A . 
D 3 HOH 88  788  799  HOH HOH A . 
D 3 HOH 89  789  895  HOH HOH A . 
D 3 HOH 90  790  877  HOH HOH A . 
D 3 HOH 91  791  892  HOH HOH A . 
D 3 HOH 92  792  794  HOH HOH A . 
D 3 HOH 93  793  849  HOH HOH A . 
D 3 HOH 94  794  893  HOH HOH A . 
D 3 HOH 95  795  770  HOH HOH A . 
D 3 HOH 96  796  722  HOH HOH A . 
D 3 HOH 97  797  786  HOH HOH A . 
D 3 HOH 98  798  867  HOH HOH A . 
D 3 HOH 99  799  909  HOH HOH A . 
D 3 HOH 100 800  781  HOH HOH A . 
D 3 HOH 101 801  920  HOH HOH A . 
D 3 HOH 102 802  773  HOH HOH A . 
D 3 HOH 103 803  985  HOH HOH A . 
D 3 HOH 104 804  870  HOH HOH A . 
D 3 HOH 105 805  848  HOH HOH A . 
D 3 HOH 106 806  797  HOH HOH A . 
D 3 HOH 107 807  844  HOH HOH A . 
D 3 HOH 108 808  840  HOH HOH A . 
D 3 HOH 109 809  978  HOH HOH A . 
D 3 HOH 110 810  817  HOH HOH A . 
D 3 HOH 111 811  971  HOH HOH A . 
D 3 HOH 112 812  839  HOH HOH A . 
D 3 HOH 113 813  718  HOH HOH A . 
D 3 HOH 114 814  1033 HOH HOH A . 
D 3 HOH 115 815  763  HOH HOH A . 
D 3 HOH 116 816  838  HOH HOH A . 
D 3 HOH 117 817  714  HOH HOH A . 
D 3 HOH 118 818  974  HOH HOH A . 
D 3 HOH 119 819  1008 HOH HOH A . 
D 3 HOH 120 820  940  HOH HOH A . 
D 3 HOH 121 821  766  HOH HOH A . 
D 3 HOH 122 822  795  HOH HOH A . 
D 3 HOH 123 823  819  HOH HOH A . 
D 3 HOH 124 824  739  HOH HOH A . 
D 3 HOH 125 825  987  HOH HOH A . 
D 3 HOH 126 826  830  HOH HOH A . 
D 3 HOH 127 827  805  HOH HOH A . 
D 3 HOH 128 828  783  HOH HOH A . 
D 3 HOH 129 829  738  HOH HOH A . 
D 3 HOH 130 830  1012 HOH HOH A . 
D 3 HOH 131 831  711  HOH HOH A . 
D 3 HOH 132 832  900  HOH HOH A . 
D 3 HOH 133 833  906  HOH HOH A . 
D 3 HOH 134 834  834  HOH HOH A . 
D 3 HOH 135 835  785  HOH HOH A . 
D 3 HOH 136 836  764  HOH HOH A . 
D 3 HOH 137 837  988  HOH HOH A . 
D 3 HOH 138 838  804  HOH HOH A . 
D 3 HOH 139 839  927  HOH HOH A . 
D 3 HOH 140 840  882  HOH HOH A . 
D 3 HOH 141 841  1003 HOH HOH A . 
D 3 HOH 142 842  775  HOH HOH A . 
D 3 HOH 143 843  778  HOH HOH A . 
D 3 HOH 144 844  929  HOH HOH A . 
D 3 HOH 145 845  910  HOH HOH A . 
D 3 HOH 146 846  966  HOH HOH A . 
D 3 HOH 147 847  899  HOH HOH A . 
D 3 HOH 148 848  828  HOH HOH A . 
D 3 HOH 149 849  1002 HOH HOH A . 
D 3 HOH 150 850  757  HOH HOH A . 
D 3 HOH 151 851  1040 HOH HOH A . 
D 3 HOH 152 852  957  HOH HOH A . 
D 3 HOH 153 853  1029 HOH HOH A . 
D 3 HOH 154 854  916  HOH HOH A . 
D 3 HOH 155 855  905  HOH HOH A . 
D 3 HOH 156 856  769  HOH HOH A . 
D 3 HOH 157 857  816  HOH HOH A . 
D 3 HOH 158 858  866  HOH HOH A . 
D 3 HOH 159 859  776  HOH HOH A . 
D 3 HOH 160 860  979  HOH HOH A . 
D 3 HOH 161 861  800  HOH HOH A . 
D 3 HOH 162 862  878  HOH HOH A . 
D 3 HOH 163 863  912  HOH HOH A . 
D 3 HOH 164 864  811  HOH HOH A . 
D 3 HOH 165 865  955  HOH HOH A . 
D 3 HOH 166 866  904  HOH HOH A . 
D 3 HOH 167 867  807  HOH HOH A . 
D 3 HOH 168 868  1027 HOH HOH A . 
D 3 HOH 169 869  846  HOH HOH A . 
D 3 HOH 170 870  959  HOH HOH A . 
D 3 HOH 171 871  864  HOH HOH A . 
D 3 HOH 172 872  1022 HOH HOH A . 
D 3 HOH 173 873  854  HOH HOH A . 
D 3 HOH 174 874  874  HOH HOH A . 
D 3 HOH 175 875  771  HOH HOH A . 
D 3 HOH 176 876  1014 HOH HOH A . 
D 3 HOH 177 877  969  HOH HOH A . 
D 3 HOH 178 878  1037 HOH HOH A . 
D 3 HOH 179 879  728  HOH HOH A . 
D 3 HOH 180 880  813  HOH HOH A . 
D 3 HOH 181 881  924  HOH HOH A . 
D 3 HOH 182 882  810  HOH HOH A . 
D 3 HOH 183 883  856  HOH HOH A . 
D 3 HOH 184 884  824  HOH HOH A . 
D 3 HOH 185 885  861  HOH HOH A . 
D 3 HOH 186 886  855  HOH HOH A . 
D 3 HOH 187 887  788  HOH HOH A . 
D 3 HOH 188 888  1053 HOH HOH A . 
D 3 HOH 189 889  1035 HOH HOH A . 
D 3 HOH 190 890  881  HOH HOH A . 
D 3 HOH 191 891  1011 HOH HOH A . 
D 3 HOH 192 892  731  HOH HOH A . 
D 3 HOH 193 893  744  HOH HOH A . 
D 3 HOH 194 894  774  HOH HOH A . 
D 3 HOH 195 895  808  HOH HOH A . 
D 3 HOH 196 896  950  HOH HOH A . 
D 3 HOH 197 897  822  HOH HOH A . 
D 3 HOH 198 898  942  HOH HOH A . 
D 3 HOH 199 899  733  HOH HOH A . 
D 3 HOH 200 900  984  HOH HOH A . 
D 3 HOH 201 901  944  HOH HOH A . 
D 3 HOH 202 902  734  HOH HOH A . 
D 3 HOH 203 903  868  HOH HOH A . 
D 3 HOH 204 904  970  HOH HOH A . 
D 3 HOH 205 905  859  HOH HOH A . 
D 3 HOH 206 906  1018 HOH HOH A . 
D 3 HOH 207 907  798  HOH HOH A . 
D 3 HOH 208 908  951  HOH HOH A . 
D 3 HOH 209 909  930  HOH HOH A . 
D 3 HOH 210 910  1016 HOH HOH A . 
D 3 HOH 211 911  705  HOH HOH A . 
D 3 HOH 212 912  1052 HOH HOH A . 
D 3 HOH 213 913  889  HOH HOH A . 
D 3 HOH 214 914  841  HOH HOH A . 
D 3 HOH 215 915  908  HOH HOH A . 
D 3 HOH 216 916  820  HOH HOH A . 
D 3 HOH 217 917  901  HOH HOH A . 
D 3 HOH 218 918  815  HOH HOH A . 
D 3 HOH 219 919  850  HOH HOH A . 
D 3 HOH 220 920  709  HOH HOH A . 
D 3 HOH 221 921  1015 HOH HOH A . 
D 3 HOH 222 922  962  HOH HOH A . 
D 3 HOH 223 923  717  HOH HOH A . 
D 3 HOH 224 924  938  HOH HOH A . 
D 3 HOH 225 925  835  HOH HOH A . 
D 3 HOH 226 926  736  HOH HOH A . 
D 3 HOH 227 927  784  HOH HOH A . 
D 3 HOH 228 928  921  HOH HOH A . 
D 3 HOH 229 929  1038 HOH HOH A . 
D 3 HOH 230 930  1026 HOH HOH A . 
D 3 HOH 231 931  897  HOH HOH A . 
D 3 HOH 232 932  1047 HOH HOH A . 
D 3 HOH 233 933  999  HOH HOH A . 
D 3 HOH 234 934  986  HOH HOH A . 
D 3 HOH 235 935  715  HOH HOH A . 
D 3 HOH 236 936  727  HOH HOH A . 
D 3 HOH 237 937  1031 HOH HOH A . 
D 3 HOH 238 938  833  HOH HOH A . 
D 3 HOH 239 939  1050 HOH HOH A . 
D 3 HOH 240 940  1024 HOH HOH A . 
D 3 HOH 241 941  1043 HOH HOH A . 
D 3 HOH 242 942  902  HOH HOH A . 
D 3 HOH 243 943  704  HOH HOH A . 
D 3 HOH 244 944  992  HOH HOH A . 
D 3 HOH 245 945  710  HOH HOH A . 
D 3 HOH 246 946  961  HOH HOH A . 
D 3 HOH 247 947  932  HOH HOH A . 
D 3 HOH 248 948  863  HOH HOH A . 
D 3 HOH 249 949  946  HOH HOH A . 
D 3 HOH 250 950  998  HOH HOH A . 
D 3 HOH 251 951  1019 HOH HOH A . 
D 3 HOH 252 952  721  HOH HOH A . 
D 3 HOH 253 953  888  HOH HOH A . 
D 3 HOH 254 954  935  HOH HOH A . 
D 3 HOH 255 955  814  HOH HOH A . 
D 3 HOH 256 956  995  HOH HOH A . 
D 3 HOH 257 957  975  HOH HOH A . 
D 3 HOH 258 958  812  HOH HOH A . 
D 3 HOH 259 959  891  HOH HOH A . 
D 3 HOH 260 960  706  HOH HOH A . 
D 3 HOH 261 961  845  HOH HOH A . 
D 3 HOH 262 962  1009 HOH HOH A . 
D 3 HOH 263 963  712  HOH HOH A . 
D 3 HOH 264 964  843  HOH HOH A . 
D 3 HOH 265 965  720  HOH HOH A . 
D 3 HOH 266 966  782  HOH HOH A . 
D 3 HOH 267 967  767  HOH HOH A . 
D 3 HOH 268 968  937  HOH HOH A . 
D 3 HOH 269 969  719  HOH HOH A . 
D 3 HOH 270 970  702  HOH HOH A . 
D 3 HOH 271 971  907  HOH HOH A . 
D 3 HOH 272 972  803  HOH HOH A . 
D 3 HOH 273 973  949  HOH HOH A . 
D 3 HOH 274 974  729  HOH HOH A . 
D 3 HOH 275 975  885  HOH HOH A . 
D 3 HOH 276 976  933  HOH HOH A . 
D 3 HOH 277 977  953  HOH HOH A . 
D 3 HOH 278 978  1007 HOH HOH A . 
D 3 HOH 279 979  851  HOH HOH A . 
D 3 HOH 280 980  745  HOH HOH A . 
D 3 HOH 281 981  1017 HOH HOH A . 
D 3 HOH 282 982  823  HOH HOH A . 
D 3 HOH 283 983  994  HOH HOH A . 
D 3 HOH 284 984  1025 HOH HOH A . 
D 3 HOH 285 985  732  HOH HOH A . 
D 3 HOH 286 986  918  HOH HOH A . 
D 3 HOH 287 987  1013 HOH HOH A . 
D 3 HOH 288 988  963  HOH HOH A . 
D 3 HOH 289 989  1048 HOH HOH A . 
D 3 HOH 290 990  936  HOH HOH A . 
D 3 HOH 291 991  831  HOH HOH A . 
D 3 HOH 292 992  1021 HOH HOH A . 
D 3 HOH 293 993  960  HOH HOH A . 
D 3 HOH 294 994  990  HOH HOH A . 
D 3 HOH 295 995  1010 HOH HOH A . 
D 3 HOH 296 996  726  HOH HOH A . 
D 3 HOH 297 997  1042 HOH HOH A . 
D 3 HOH 298 998  973  HOH HOH A . 
D 3 HOH 299 999  716  HOH HOH A . 
D 3 HOH 300 1000 934  HOH HOH A . 
D 3 HOH 301 1001 964  HOH HOH A . 
D 3 HOH 302 1002 793  HOH HOH A . 
D 3 HOH 303 1003 996  HOH HOH A . 
D 3 HOH 304 1004 931  HOH HOH A . 
D 3 HOH 305 1005 952  HOH HOH A . 
D 3 HOH 306 1006 1034 HOH HOH A . 
D 3 HOH 307 1007 836  HOH HOH A . 
D 3 HOH 308 1008 972  HOH HOH A . 
D 3 HOH 309 1009 1039 HOH HOH A . 
D 3 HOH 310 1010 860  HOH HOH A . 
D 3 HOH 311 1011 967  HOH HOH A . 
D 3 HOH 312 1012 914  HOH HOH A . 
D 3 HOH 313 1013 862  HOH HOH A . 
D 3 HOH 314 1014 751  HOH HOH A . 
D 3 HOH 315 1015 725  HOH HOH A . 
D 3 HOH 316 1016 1020 HOH HOH A . 
D 3 HOH 317 1017 1044 HOH HOH A . 
D 3 HOH 318 1018 1023 HOH HOH A . 
D 3 HOH 319 1019 875  HOH HOH A . 
D 3 HOH 320 1020 748  HOH HOH A . 
D 3 HOH 321 1021 754  HOH HOH A . 
D 3 HOH 322 1022 886  HOH HOH A . 
D 3 HOH 323 1023 723  HOH HOH A . 
D 3 HOH 324 1024 977  HOH HOH A . 
D 3 HOH 325 1025 755  HOH HOH A . 
D 3 HOH 326 1026 756  HOH HOH A . 
D 3 HOH 327 1027 741  HOH HOH A . 
D 3 HOH 328 1028 958  HOH HOH A . 
D 3 HOH 329 1029 982  HOH HOH A . 
D 3 HOH 330 1030 847  HOH HOH A . 
D 3 HOH 331 1031 750  HOH HOH A . 
D 3 HOH 332 1032 919  HOH HOH A . 
D 3 HOH 333 1033 1045 HOH HOH A . 
D 3 HOH 334 1034 747  HOH HOH A . 
D 3 HOH 335 1035 752  HOH HOH A . 
D 3 HOH 336 1036 965  HOH HOH A . 
D 3 HOH 337 1037 724  HOH HOH A . 
D 3 HOH 338 1038 980  HOH HOH A . 
D 3 HOH 339 1039 758  HOH HOH A . 
D 3 HOH 340 1040 753  HOH HOH A . 
D 3 HOH 341 1041 1028 HOH HOH A . 
D 3 HOH 342 1042 872  HOH HOH A . 
D 3 HOH 343 1043 749  HOH HOH A . 
D 3 HOH 344 1044 879  HOH HOH A . 
D 3 HOH 345 1045 746  HOH HOH A . 
D 3 HOH 346 1046 1041 HOH HOH A . 
D 3 HOH 347 1047 981  HOH HOH A . 
D 3 HOH 348 1048 842  HOH HOH A . 
D 3 HOH 349 1049 742  HOH HOH A . 
D 3 HOH 350 1050 735  HOH HOH A . 
D 3 HOH 351 1051 737  HOH HOH A . 
D 3 HOH 352 1052 1046 HOH HOH A . 
D 3 HOH 353 1053 708  HOH HOH A . 
# 
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' ? ? ? ? ? ? ? ? ? ? ? MOSFLM ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? FFT    ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HRH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     107.270 
_cell.length_a_esd                 ? 
_cell.length_b                     107.270 
_cell.length_b_esd                 ? 
_cell.length_c                     218.852 
_cell.length_c_esd                 ? 
_cell.volume                       2180909.844 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9HRH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_Hall            'P 61 2 (x,y,z+5/12)' 
_symmetry.space_group_name_H-M             'P 61 2 2' 
_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                   9HRH 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.34 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Hepes, 40% PEG 200' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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         2020-01-28 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          19.24 
_reflns.entry_id                                       9HRH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               72.95 
_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                                     82318 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.090 
_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                                    1.70 
_reflns_shell.d_res_low                                     1.79 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             95933 
_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                               8.1 
_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                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.472 
_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                               23.61 
_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                                 9HRH 
_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                            1.70 
_refine.ls_d_res_low                             53.64 
_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                     82221 
_refine.ls_number_reflns_R_free                  4125 
_refine.ls_number_reflns_R_work                  78096 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1999 
_refine.ls_R_factor_R_free                       0.2063 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1996 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_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                 19.7454 
_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                            0.2093 
_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                       1.70 
_refine_hist.d_res_low                        53.64 
_refine_hist.number_atoms_solvent             353 
_refine_hist.number_atoms_total               4032 
_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        3638 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         41 
_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' ? 0.0029 ? 3785 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6314 ? 5118 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0428 ? 555  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0053 ? 654  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.6686 ? 527  ? 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' 1.70 1.72  . . 162 2628 100.00 . . . . 0.3808 . . . . . . . . . . . 0.4145 
'X-RAY DIFFRACTION' 1.72 1.74  . . 132 2653 99.96  . . . . 0.3563 . . . . . . . . . . . 0.3582 
'X-RAY DIFFRACTION' 1.74 1.76  . . 134 2654 100.00 . . . . 0.3231 . . . . . . . . . . . 0.3473 
'X-RAY DIFFRACTION' 1.76 1.79  . . 141 2641 99.93  . . . . 0.2819 . . . . . . . . . . . 0.2991 
'X-RAY DIFFRACTION' 1.79 1.81  . . 122 2662 99.89  . . . . 0.2822 . . . . . . . . . . . 0.2898 
'X-RAY DIFFRACTION' 1.81 1.84  . . 141 2642 99.89  . . . . 0.2550 . . . . . . . . . . . 0.2875 
'X-RAY DIFFRACTION' 1.84 1.86  . . 126 2642 99.89  . . . . 0.2459 . . . . . . . . . . . 0.2359 
'X-RAY DIFFRACTION' 1.86 1.89  . . 146 2661 100.00 . . . . 0.2330 . . . . . . . . . . . 0.2347 
'X-RAY DIFFRACTION' 1.89 1.92  . . 143 2650 100.00 . . . . 0.2369 . . . . . . . . . . . 0.2293 
'X-RAY DIFFRACTION' 1.92 1.96  . . 120 2689 100.00 . . . . 0.2180 . . . . . . . . . . . 0.2027 
'X-RAY DIFFRACTION' 1.96 1.99  . . 152 2636 100.00 . . . . 0.2284 . . . . . . . . . . . 0.2254 
'X-RAY DIFFRACTION' 1.99 2.03  . . 152 2660 100.00 . . . . 0.2304 . . . . . . . . . . . 0.2296 
'X-RAY DIFFRACTION' 2.03 2.07  . . 138 2667 100.00 . . . . 0.2342 . . . . . . . . . . . 0.2620 
'X-RAY DIFFRACTION' 2.07 2.12  . . 156 2636 99.89  . . . . 0.2041 . . . . . . . . . . . 0.2266 
'X-RAY DIFFRACTION' 2.12 2.17  . . 135 2666 99.82  . . . . 0.2078 . . . . . . . . . . . 0.1983 
'X-RAY DIFFRACTION' 2.17 2.22  . . 149 2673 100.00 . . . . 0.1979 . . . . . . . . . . . 0.1854 
'X-RAY DIFFRACTION' 2.22 2.28  . . 154 2674 100.00 . . . . 0.1899 . . . . . . . . . . . 0.2292 
'X-RAY DIFFRACTION' 2.28 2.35  . . 133 2684 100.00 . . . . 0.1927 . . . . . . . . . . . 0.2338 
'X-RAY DIFFRACTION' 2.35 2.42  . . 157 2658 100.00 . . . . 0.1867 . . . . . . . . . . . 0.2243 
'X-RAY DIFFRACTION' 2.42 2.51  . . 155 2694 100.00 . . . . 0.1897 . . . . . . . . . . . 0.2018 
'X-RAY DIFFRACTION' 2.51 2.61  . . 128 2704 100.00 . . . . 0.1840 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 2.61 2.73  . . 142 2701 99.96  . . . . 0.1803 . . . . . . . . . . . 0.1967 
'X-RAY DIFFRACTION' 2.73 2.87  . . 134 2700 100.00 . . . . 0.1887 . . . . . . . . . . . 0.1975 
'X-RAY DIFFRACTION' 2.87 3.05  . . 136 2743 99.90  . . . . 0.1869 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 3.05 3.29  . . 148 2714 99.97  . . . . 0.1895 . . . . . . . . . . . 0.1966 
'X-RAY DIFFRACTION' 3.29 3.62  . . 156 2742 100.00 . . . . 0.1840 . . . . . . . . . . . 0.1933 
'X-RAY DIFFRACTION' 3.62 4.14  . . 143 2784 99.97  . . . . 0.1719 . . . . . . . . . . . 0.1431 
'X-RAY DIFFRACTION' 4.15 5.22  . . 139 2820 99.97  . . . . 0.1612 . . . . . . . . . . . 0.1854 
'X-RAY DIFFRACTION' 5.22 53.64 . . 151 3018 99.94  . . . . 0.1942 . . . . . . . . . . . 0.1853 
# 
_struct.entry_id                     9HRH 
_struct.title                        'Human holo aromatic L-amino acid decarboxylase (AADC) R347Q variant native structure' 
_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        9HRH 
_struct_keywords.text            'dopa decarboxylase, DDC, aromatic L-amino acid decarboxylase, AADC, R347Q variant, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 2 ? 
D N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q53Y41_HUMAN 
_struct_ref.pdbx_db_accession          Q53Y41 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDVEKIIMPGVTHWHSPYFFAYF
PTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAAR
TKVIHRLQAASPELTQAAIMEKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKKRT
DLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEI
CVEVILGLVCFRLKGSNKVNEALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE

;
_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              9HRH 
_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                 480 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q53Y41 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  480 
_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       480 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9HRH 
_struct_ref_seq_dif.mon_id                       GLN 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      347 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q53Y41 
_struct_ref_seq_dif.db_mon_id                    ARG 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          347 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            347 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 12480 ? 
1 MORE         -58   ? 
1 'SSA (A^2)'  30980 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                'Functional Dimer' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z        1.0000000000 0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 10_554 -y,-x,-z-1/6 0.5000000000 -0.8660254038 0.0000000000 0.0000000000 -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -36.4753333333 
# 
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 ASN A 2   ? GLY A 23  ? ASN A 2   GLY A 23  1 ? 22 
HELX_P HELX_P2  AA2 ILE A 24  ? ARG A 27  ? ILE A 24  ARG A 27  5 ? 4  
HELX_P HELX_P3  AA3 LEU A 38  ? ILE A 42  ? LEU A 38  ILE A 42  5 ? 5  
HELX_P HELX_P4  AA4 THR A 52  ? ILE A 63  ? THR A 52  ILE A 63  1 ? 12 
HELX_P HELX_P5  AA5 ILE A 64  ? VAL A 68  ? ILE A 64  VAL A 68  5 ? 5  
HELX_P HELX_P6  AA6 SER A 85  ? GLY A 99  ? SER A 85  GLY A 99  1 ? 15 
HELX_P HELX_P7  AA7 SER A 108 ? LEU A 126 ? SER A 108 LEU A 126 1 ? 19 
HELX_P HELX_P8  AA8 PRO A 129 ? LEU A 133 ? PRO A 129 LEU A 133 5 ? 5  
HELX_P HELX_P9  AA9 SER A 147 ? SER A 171 ? SER A 147 SER A 171 1 ? 25 
HELX_P HELX_P10 AB1 THR A 175 ? GLU A 181 ? THR A 175 GLU A 181 1 ? 7  
HELX_P HELX_P11 AB2 HIS A 192 ? GLY A 203 ? HIS A 192 GLY A 203 1 ? 12 
HELX_P HELX_P12 AB3 ARG A 218 ? ALA A 232 ? ARG A 218 ALA A 232 1 ? 15 
HELX_P HELX_P13 AB4 ASN A 253 ? ASP A 265 ? ASN A 253 ASP A 265 1 ? 13 
HELX_P HELX_P14 AB5 TYR A 274 ? CYS A 281 ? TYR A 274 CYS A 281 5 ? 8  
HELX_P HELX_P15 AB6 PHE A 284 ? ASN A 289 ? PHE A 284 ASN A 289 5 ? 6  
HELX_P HELX_P16 AB7 GLY A 290 ? ALA A 294 ? GLY A 290 ALA A 294 5 ? 5  
HELX_P HELX_P17 AB8 ASN A 300 ? LEU A 305 ? ASN A 300 LEU A 305 1 ? 6  
HELX_P HELX_P18 AB9 LYS A 318 ? LEU A 322 ? LYS A 318 LEU A 322 5 ? 5  
HELX_P HELX_P19 AC1 ARG A 358 ? ARG A 393 ? ARG A 358 ARG A 393 1 ? 36 
HELX_P HELX_P20 AC2 SER A 416 ? LYS A 431 ? SER A 416 LYS A 431 1 ? 16 
HELX_P HELX_P21 AC3 GLU A 456 ? GLU A 480 ? GLU A 456 GLU A 480 1 ? 25 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A HIS 302 C ? ? ? 1_555 A LLP 303 N ? ? A HIS 302 A LLP 303 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale2 covale both ? A LLP 303 C ? ? ? 1_555 A TRP 304 N ? ? A LLP 303 A TRP 304 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      LLP 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       303 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       LLP 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        303 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                LYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        LLP 
_pdbx_modification_feature.type                               'Pyridoxal phosphate' 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PHE 
_struct_mon_prot_cis.label_seq_id           309 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PHE 
_struct_mon_prot_cis.auth_seq_id            309 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   ASP 
_struct_mon_prot_cis.pdbx_label_seq_id_2    310 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    ASP 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     310 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       6.50 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 4 ? 
# 
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 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? 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 GLY A 141 ? GLN A 145 ? GLY A 141 GLN A 145 
AA1 2 SER A 312 ? VAL A 316 ? SER A 312 VAL A 316 
AA1 3 SER A 296 ? PHE A 299 ? SER A 296 PHE A 299 
AA1 4 TRP A 267 ? ASP A 271 ? TRP A 267 ASP A 271 
AA1 5 ILE A 235 ? THR A 242 ? ILE A 235 THR A 242 
AA1 6 LEU A 183 ? SER A 188 ? LEU A 183 SER A 188 
AA1 7 LYS A 205 ? ILE A 209 ? LYS A 205 ILE A 209 
AA2 1 PHE A 398 ? ILE A 400 ? PHE A 398 ILE A 400 
AA2 2 LEU A 408 ? LEU A 413 ? LEU A 408 LEU A 413 
AA2 3 LYS A 443 ? ALA A 449 ? LYS A 443 ALA A 449 
AA2 4 PRO A 437 ? LEU A 440 ? PRO A 437 LEU A 440 
# 
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 GLN A 145 ? N GLN A 145 O SER A 312 ? O SER A 312 
AA1 2 3 O TRP A 315 ? O TRP A 315 N PHE A 297 ? N PHE A 297 
AA1 3 4 O SER A 296 ? O SER A 296 N VAL A 270 ? N VAL A 270 
AA1 4 5 O HIS A 269 ? O HIS A 269 N MET A 239 ? N MET A 239 
AA1 5 6 O VAL A 240 ? O VAL A 240 N TYR A 186 ? N TYR A 186 
AA1 6 7 N SER A 187 ? N SER A 187 O ILE A 209 ? O ILE A 209 
AA2 1 2 N GLU A 399 ? N GLU A 399 O ARG A 412 ? O ARG A 412 
AA2 2 3 N PHE A 411 ? N PHE A 411 O LEU A 446 ? O LEU A 446 
AA2 3 4 O VAL A 445 ? O VAL A 445 N CYS A 438 ? N CYS A 438 
# 
_pdbx_entry_details.entry_id                   9HRH 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG  A SER 149  ? ? O A HOH 701  ? ? 2.00 
2 1 O   A HOH 902  ? ? O A HOH 910  ? ? 2.12 
3 1 O   A HOH 818  ? ? O A HOH 1005 ? ? 2.16 
4 1 O   A HOH 789  ? ? O A HOH 926  ? ? 2.18 
5 1 O   A HOH 1005 ? ? O A HOH 1016 ? ? 2.19 
6 1 OD1 A ASP 55   ? ? O A HOH 702  ? ? 2.19 
7 1 O   A HOH 739  ? ? O A HOH 820  ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     902 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     902 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   10_554 
_pdbx_validate_symm_contact.dist              2.12 
# 
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 TYR A 79  ? ? 50.68   -114.58 
2 1 SER A 108 ? ? 174.14  97.52   
3 1 LLP A 303 ? ? -93.48  -64.49  
4 1 CYS A 311 ? ? -164.13 101.02  
5 1 LEU A 406 ? ? -117.33 -143.87 
6 1 ARG A 441 ? ? 57.61   -123.23 
7 1 CYS A 451 ? ? -122.77 -56.92  
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    LLP 
_pdbx_struct_mod_residue.label_seq_id     303 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     LLP 
_pdbx_struct_mod_residue.auth_seq_id      303 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   LYS 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 921  ? D HOH . 
2 1 A HOH 1022 ? D HOH . 
3 1 A HOH 1042 ? D HOH . 
4 1 A HOH 1050 ? D HOH . 
5 1 A HOH 1051 ? D HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z          
2  x-y,x,z+1/6    
3  y,-x+y,z+5/6   
4  -y,x-y,z+1/3   
5  -x+y,-x,z+2/3  
6  x-y,-y,-z      
7  -x,-x+y,-z+2/3 
8  -x,-y,z+1/2    
9  y,x,-z+1/3     
10 -y,-x,-z+5/6   
11 -x+y,y,-z+1/2  
12 x,x-y,-z+1/6   
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         35.896035732 
_pdbx_refine_tls.origin_y         -33.6393345331 
_pdbx_refine_tls.origin_z         -9.21334617989 
_pdbx_refine_tls.T[1][1]          0.126797542252 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0096653948884 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0103906510245 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.116389985895 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0139457224749 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.121980987041 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.499057212936 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0352282273058 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0345547078578 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.446301685425 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0423318115924 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.503234329172 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0225377131616 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0253847967415 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0757603757794 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0559043323974 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.00848244145252 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0342570818846 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0703481792874 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.00771172531905 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0331059319451 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   A 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     714 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '(chain A and resseq 1:714)' 
# 
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 THR 323 ? A THR 323 
2  1 Y 1 A GLY 324 ? A GLY 324 
3  1 Y 1 A ALA 325 ? A ALA 325 
4  1 Y 1 A PHE 326 ? A PHE 326 
5  1 Y 1 A ARG 327 ? A ARG 327 
6  1 Y 1 A LEU 328 ? A LEU 328 
7  1 Y 1 A ASP 329 ? A ASP 329 
8  1 Y 1 A PRO 330 ? A PRO 330 
9  1 Y 1 A THR 331 ? A THR 331 
10 1 Y 1 A TYR 332 ? A TYR 332 
11 1 Y 1 A LEU 333 ? A LEU 333 
12 1 Y 1 A LYS 334 ? A LYS 334 
13 1 Y 1 A HIS 335 ? A HIS 335 
14 1 Y 1 A SER 336 ? A SER 336 
15 1 Y 1 A HIS 337 ? A HIS 337 
16 1 Y 1 A GLN 338 ? A GLN 338 
17 1 Y 1 A ASP 339 ? A ASP 339 
18 1 Y 1 A SER 340 ? A SER 340 
19 1 Y 1 A GLY 341 ? A GLY 341 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
GLN N      N N N 88  
GLN CA     C N S 89  
GLN C      C N N 90  
GLN O      O N N 91  
GLN CB     C N N 92  
GLN CG     C N N 93  
GLN CD     C N N 94  
GLN OE1    O N N 95  
GLN NE2    N N N 96  
GLN OXT    O N N 97  
GLN H      H N N 98  
GLN H2     H N N 99  
GLN HA     H N N 100 
GLN HB2    H N N 101 
GLN HB3    H N N 102 
GLN HG2    H N N 103 
GLN HG3    H N N 104 
GLN HE21   H N N 105 
GLN HE22   H N N 106 
GLN HXT    H N N 107 
GLU N      N N N 108 
GLU CA     C N S 109 
GLU C      C N N 110 
GLU O      O N N 111 
GLU CB     C N N 112 
GLU CG     C N N 113 
GLU CD     C N N 114 
GLU OE1    O N N 115 
GLU OE2    O N N 116 
GLU OXT    O N N 117 
GLU H      H N N 118 
GLU H2     H N N 119 
GLU HA     H N N 120 
GLU HB2    H N N 121 
GLU HB3    H N N 122 
GLU HG2    H N N 123 
GLU HG3    H N N 124 
GLU HE2    H N N 125 
GLU HXT    H N N 126 
GLY N      N N N 127 
GLY CA     C N N 128 
GLY C      C N N 129 
GLY O      O N N 130 
GLY OXT    O N N 131 
GLY H      H N N 132 
GLY H2     H N N 133 
GLY HA2    H N N 134 
GLY HA3    H N N 135 
GLY HXT    H N N 136 
HIS N      N N N 137 
HIS CA     C N S 138 
HIS C      C N N 139 
HIS O      O N N 140 
HIS CB     C N N 141 
HIS CG     C Y N 142 
HIS ND1    N Y N 143 
HIS CD2    C Y N 144 
HIS CE1    C Y N 145 
HIS NE2    N Y N 146 
HIS OXT    O N N 147 
HIS H      H N N 148 
HIS H2     H N N 149 
HIS HA     H N N 150 
HIS HB2    H N N 151 
HIS HB3    H N N 152 
HIS HD1    H N N 153 
HIS HD2    H N N 154 
HIS HE1    H N N 155 
HIS HE2    H N N 156 
HIS HXT    H N N 157 
HOH O      O N N 158 
HOH H1     H N N 159 
HOH H2     H N N 160 
ILE N      N N N 161 
ILE CA     C N S 162 
ILE C      C N N 163 
ILE O      O N N 164 
ILE CB     C N S 165 
ILE CG1    C N N 166 
ILE CG2    C N N 167 
ILE CD1    C N N 168 
ILE OXT    O N N 169 
ILE H      H N N 170 
ILE H2     H N N 171 
ILE HA     H N N 172 
ILE HB     H N N 173 
ILE HG12   H N N 174 
ILE HG13   H N N 175 
ILE HG21   H N N 176 
ILE HG22   H N N 177 
ILE HG23   H N N 178 
ILE HD11   H N N 179 
ILE HD12   H N N 180 
ILE HD13   H N N 181 
ILE HXT    H N N 182 
LEU N      N N N 183 
LEU CA     C N S 184 
LEU C      C N N 185 
LEU O      O N N 186 
LEU CB     C N N 187 
LEU CG     C N N 188 
LEU CD1    C N N 189 
LEU CD2    C N N 190 
LEU OXT    O N N 191 
LEU H      H N N 192 
LEU H2     H N N 193 
LEU HA     H N N 194 
LEU HB2    H N N 195 
LEU HB3    H N N 196 
LEU HG     H N N 197 
LEU HD11   H N N 198 
LEU HD12   H N N 199 
LEU HD13   H N N 200 
LEU HD21   H N N 201 
LEU HD22   H N N 202 
LEU HD23   H N N 203 
LEU HXT    H N N 204 
LLP N1     N Y N 205 
LLP C2     C Y N 206 
LLP "C2'"  C N N 207 
LLP C3     C Y N 208 
LLP O3     O N N 209 
LLP C4     C Y N 210 
LLP "C4'"  C N N 211 
LLP C5     C Y N 212 
LLP C6     C Y N 213 
LLP "C5'"  C N N 214 
LLP OP4    O N N 215 
LLP P      P N N 216 
LLP OP1    O N N 217 
LLP OP2    O N N 218 
LLP OP3    O N N 219 
LLP N      N N N 220 
LLP CA     C N S 221 
LLP CB     C N N 222 
LLP CG     C N N 223 
LLP CD     C N N 224 
LLP CE     C N N 225 
LLP NZ     N N N 226 
LLP C      C N N 227 
LLP O      O N N 228 
LLP OXT    O N N 229 
LLP "H2'1" H N N 230 
LLP "H2'2" H N N 231 
LLP "H2'3" H N N 232 
LLP HO3    H N N 233 
LLP "H4'1" H N N 234 
LLP H6     H N N 235 
LLP "H5'1" H N N 236 
LLP "H5'2" H N N 237 
LLP HOP2   H N N 238 
LLP HOP3   H N N 239 
LLP H      H N N 240 
LLP H2     H N N 241 
LLP HA     H N N 242 
LLP HB2    H N N 243 
LLP HB3    H N N 244 
LLP HG2    H N N 245 
LLP HG3    H N N 246 
LLP HD2    H N N 247 
LLP HD3    H N N 248 
LLP HE2    H N N 249 
LLP HE3    H N N 250 
LLP HXT    H N N 251 
LYS N      N N N 252 
LYS CA     C N S 253 
LYS C      C N N 254 
LYS O      O N N 255 
LYS CB     C N N 256 
LYS CG     C N N 257 
LYS CD     C N N 258 
LYS CE     C N N 259 
LYS NZ     N N N 260 
LYS OXT    O N N 261 
LYS H      H N N 262 
LYS H2     H N N 263 
LYS HA     H N N 264 
LYS HB2    H N N 265 
LYS HB3    H N N 266 
LYS HG2    H N N 267 
LYS HG3    H N N 268 
LYS HD2    H N N 269 
LYS HD3    H N N 270 
LYS HE2    H N N 271 
LYS HE3    H N N 272 
LYS HZ1    H N N 273 
LYS HZ2    H N N 274 
LYS HZ3    H N N 275 
LYS HXT    H N N 276 
MET N      N N N 277 
MET CA     C N S 278 
MET C      C N N 279 
MET O      O N N 280 
MET CB     C N N 281 
MET CG     C N N 282 
MET SD     S N N 283 
MET CE     C N N 284 
MET OXT    O N N 285 
MET H      H N N 286 
MET H2     H N N 287 
MET HA     H N N 288 
MET HB2    H N N 289 
MET HB3    H N N 290 
MET HG2    H N N 291 
MET HG3    H N N 292 
MET HE1    H N N 293 
MET HE2    H N N 294 
MET HE3    H N N 295 
MET HXT    H N N 296 
PG4 O1     O N N 297 
PG4 C1     C N N 298 
PG4 C2     C N N 299 
PG4 O2     O N N 300 
PG4 C3     C N N 301 
PG4 C4     C N N 302 
PG4 O3     O N N 303 
PG4 C5     C N N 304 
PG4 C6     C N N 305 
PG4 O4     O N N 306 
PG4 C7     C N N 307 
PG4 C8     C N N 308 
PG4 O5     O N N 309 
PG4 HO1    H N N 310 
PG4 H11    H N N 311 
PG4 H12    H N N 312 
PG4 H21    H N N 313 
PG4 H22    H N N 314 
PG4 H31    H N N 315 
PG4 H32    H N N 316 
PG4 H41    H N N 317 
PG4 H42    H N N 318 
PG4 H51    H N N 319 
PG4 H52    H N N 320 
PG4 H61    H N N 321 
PG4 H62    H N N 322 
PG4 H71    H N N 323 
PG4 H72    H N N 324 
PG4 H81    H N N 325 
PG4 H82    H N N 326 
PG4 HO5    H N N 327 
PHE N      N N N 328 
PHE CA     C N S 329 
PHE C      C N N 330 
PHE O      O N N 331 
PHE CB     C N N 332 
PHE CG     C Y N 333 
PHE CD1    C Y N 334 
PHE CD2    C Y N 335 
PHE CE1    C Y N 336 
PHE CE2    C Y N 337 
PHE CZ     C Y N 338 
PHE OXT    O N N 339 
PHE H      H N N 340 
PHE H2     H N N 341 
PHE HA     H N N 342 
PHE HB2    H N N 343 
PHE HB3    H N N 344 
PHE HD1    H N N 345 
PHE HD2    H N N 346 
PHE HE1    H N N 347 
PHE HE2    H N N 348 
PHE HZ     H N N 349 
PHE HXT    H N N 350 
PRO N      N N N 351 
PRO CA     C N S 352 
PRO C      C N N 353 
PRO O      O N N 354 
PRO CB     C N N 355 
PRO CG     C N N 356 
PRO CD     C N N 357 
PRO OXT    O N N 358 
PRO H      H N N 359 
PRO HA     H N N 360 
PRO HB2    H N N 361 
PRO HB3    H N N 362 
PRO HG2    H N N 363 
PRO HG3    H N N 364 
PRO HD2    H N N 365 
PRO HD3    H N N 366 
PRO HXT    H N N 367 
SER N      N N N 368 
SER CA     C N S 369 
SER C      C N N 370 
SER O      O N N 371 
SER CB     C N N 372 
SER OG     O N N 373 
SER OXT    O N N 374 
SER H      H N N 375 
SER H2     H N N 376 
SER HA     H N N 377 
SER HB2    H N N 378 
SER HB3    H N N 379 
SER HG     H N N 380 
SER HXT    H N N 381 
THR N      N N N 382 
THR CA     C N S 383 
THR C      C N N 384 
THR O      O N N 385 
THR CB     C N R 386 
THR OG1    O N N 387 
THR CG2    C N N 388 
THR OXT    O N N 389 
THR H      H N N 390 
THR H2     H N N 391 
THR HA     H N N 392 
THR HB     H N N 393 
THR HG1    H N N 394 
THR HG21   H N N 395 
THR HG22   H N N 396 
THR HG23   H N N 397 
THR HXT    H N N 398 
TRP N      N N N 399 
TRP CA     C N S 400 
TRP C      C N N 401 
TRP O      O N N 402 
TRP CB     C N N 403 
TRP CG     C Y N 404 
TRP CD1    C Y N 405 
TRP CD2    C Y N 406 
TRP NE1    N Y N 407 
TRP CE2    C Y N 408 
TRP CE3    C Y N 409 
TRP CZ2    C Y N 410 
TRP CZ3    C Y N 411 
TRP CH2    C Y N 412 
TRP OXT    O N N 413 
TRP H      H N N 414 
TRP H2     H N N 415 
TRP HA     H N N 416 
TRP HB2    H N N 417 
TRP HB3    H N N 418 
TRP HD1    H N N 419 
TRP HE1    H N N 420 
TRP HE3    H N N 421 
TRP HZ2    H N N 422 
TRP HZ3    H N N 423 
TRP HH2    H N N 424 
TRP HXT    H N N 425 
TYR N      N N N 426 
TYR CA     C N S 427 
TYR C      C N N 428 
TYR O      O N N 429 
TYR CB     C N N 430 
TYR CG     C Y N 431 
TYR CD1    C Y N 432 
TYR CD2    C Y N 433 
TYR CE1    C Y N 434 
TYR CE2    C Y N 435 
TYR CZ     C Y N 436 
TYR OH     O N N 437 
TYR OXT    O N N 438 
TYR H      H N N 439 
TYR H2     H N N 440 
TYR HA     H N N 441 
TYR HB2    H N N 442 
TYR HB3    H N N 443 
TYR HD1    H N N 444 
TYR HD2    H N N 445 
TYR HE1    H N N 446 
TYR HE2    H N N 447 
TYR HH     H N N 448 
TYR HXT    H N N 449 
VAL N      N N N 450 
VAL CA     C N S 451 
VAL C      C N N 452 
VAL O      O N N 453 
VAL CB     C N N 454 
VAL CG1    C N N 455 
VAL CG2    C N N 456 
VAL OXT    O N N 457 
VAL H      H N N 458 
VAL H2     H N N 459 
VAL HA     H N N 460 
VAL HB     H N N 461 
VAL HG11   H N N 462 
VAL HG12   H N N 463 
VAL HG13   H N N 464 
VAL HG21   H N N 465 
VAL HG22   H N N 466 
VAL HG23   H N N 467 
VAL HXT    H N N 468 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LLP N1    C2     doub Y N 194 
LLP N1    C6     sing Y N 195 
LLP C2    "C2'"  sing N N 196 
LLP C2    C3     sing Y N 197 
LLP C3    O3     sing N N 198 
LLP C3    C4     doub Y N 199 
LLP C4    "C4'"  sing N N 200 
LLP C4    C5     sing Y N 201 
LLP "C4'" NZ     doub N N 202 
LLP C5    C6     doub Y N 203 
LLP C5    "C5'"  sing N N 204 
LLP "C5'" OP4    sing N N 205 
LLP OP4   P      sing N N 206 
LLP P     OP1    doub N N 207 
LLP P     OP2    sing N N 208 
LLP P     OP3    sing N N 209 
LLP N     CA     sing N N 210 
LLP CA    CB     sing N N 211 
LLP CA    C      sing N N 212 
LLP CB    CG     sing N N 213 
LLP CG    CD     sing N N 214 
LLP CD    CE     sing N N 215 
LLP CE    NZ     sing N N 216 
LLP C     O      doub N N 217 
LLP C     OXT    sing N N 218 
LLP "C2'" "H2'1" sing N N 219 
LLP "C2'" "H2'2" sing N N 220 
LLP "C2'" "H2'3" sing N N 221 
LLP O3    HO3    sing N N 222 
LLP "C4'" "H4'1" sing N N 223 
LLP C6    H6     sing N N 224 
LLP "C5'" "H5'1" sing N N 225 
LLP "C5'" "H5'2" sing N N 226 
LLP OP2   HOP2   sing N N 227 
LLP OP3   HOP3   sing N N 228 
LLP N     H      sing N N 229 
LLP N     H2     sing N N 230 
LLP CA    HA     sing N N 231 
LLP CB    HB2    sing N N 232 
LLP CB    HB3    sing N N 233 
LLP CG    HG2    sing N N 234 
LLP CG    HG3    sing N N 235 
LLP CD    HD2    sing N N 236 
LLP CD    HD3    sing N N 237 
LLP CE    HE2    sing N N 238 
LLP CE    HE3    sing N N 239 
LLP OXT   HXT    sing N N 240 
LYS N     CA     sing N N 241 
LYS N     H      sing N N 242 
LYS N     H2     sing N N 243 
LYS CA    C      sing N N 244 
LYS CA    CB     sing N N 245 
LYS CA    HA     sing N N 246 
LYS C     O      doub N N 247 
LYS C     OXT    sing N N 248 
LYS CB    CG     sing N N 249 
LYS CB    HB2    sing N N 250 
LYS CB    HB3    sing N N 251 
LYS CG    CD     sing N N 252 
LYS CG    HG2    sing N N 253 
LYS CG    HG3    sing N N 254 
LYS CD    CE     sing N N 255 
LYS CD    HD2    sing N N 256 
LYS CD    HD3    sing N N 257 
LYS CE    NZ     sing N N 258 
LYS CE    HE2    sing N N 259 
LYS CE    HE3    sing N N 260 
LYS NZ    HZ1    sing N N 261 
LYS NZ    HZ2    sing N N 262 
LYS NZ    HZ3    sing N N 263 
LYS OXT   HXT    sing N N 264 
MET N     CA     sing N N 265 
MET N     H      sing N N 266 
MET N     H2     sing N N 267 
MET CA    C      sing N N 268 
MET CA    CB     sing N N 269 
MET CA    HA     sing N N 270 
MET C     O      doub N N 271 
MET C     OXT    sing N N 272 
MET CB    CG     sing N N 273 
MET CB    HB2    sing N N 274 
MET CB    HB3    sing N N 275 
MET CG    SD     sing N N 276 
MET CG    HG2    sing N N 277 
MET CG    HG3    sing N N 278 
MET SD    CE     sing N N 279 
MET CE    HE1    sing N N 280 
MET CE    HE2    sing N N 281 
MET CE    HE3    sing N N 282 
MET OXT   HXT    sing N N 283 
PG4 O1    C1     sing N N 284 
PG4 O1    HO1    sing N N 285 
PG4 C1    C2     sing N N 286 
PG4 C1    H11    sing N N 287 
PG4 C1    H12    sing N N 288 
PG4 C2    O2     sing N N 289 
PG4 C2    H21    sing N N 290 
PG4 C2    H22    sing N N 291 
PG4 O2    C3     sing N N 292 
PG4 C3    C4     sing N N 293 
PG4 C3    H31    sing N N 294 
PG4 C3    H32    sing N N 295 
PG4 C4    O3     sing N N 296 
PG4 C4    H41    sing N N 297 
PG4 C4    H42    sing N N 298 
PG4 O3    C5     sing N N 299 
PG4 C5    C6     sing N N 300 
PG4 C5    H51    sing N N 301 
PG4 C5    H52    sing N N 302 
PG4 C6    O4     sing N N 303 
PG4 C6    H61    sing N N 304 
PG4 C6    H62    sing N N 305 
PG4 O4    C7     sing N N 306 
PG4 C7    C8     sing N N 307 
PG4 C7    H71    sing N N 308 
PG4 C7    H72    sing N N 309 
PG4 C8    O5     sing N N 310 
PG4 C8    H81    sing N N 311 
PG4 C8    H82    sing N N 312 
PG4 O5    HO5    sing N N 313 
PHE N     CA     sing N N 314 
PHE N     H      sing N N 315 
PHE N     H2     sing N N 316 
PHE CA    C      sing N N 317 
PHE CA    CB     sing N N 318 
PHE CA    HA     sing N N 319 
PHE C     O      doub N N 320 
PHE C     OXT    sing N N 321 
PHE CB    CG     sing N N 322 
PHE CB    HB2    sing N N 323 
PHE CB    HB3    sing N N 324 
PHE CG    CD1    doub Y N 325 
PHE CG    CD2    sing Y N 326 
PHE CD1   CE1    sing Y N 327 
PHE CD1   HD1    sing N N 328 
PHE CD2   CE2    doub Y N 329 
PHE CD2   HD2    sing N N 330 
PHE CE1   CZ     doub Y N 331 
PHE CE1   HE1    sing N N 332 
PHE CE2   CZ     sing Y N 333 
PHE CE2   HE2    sing N N 334 
PHE CZ    HZ     sing N N 335 
PHE OXT   HXT    sing N N 336 
PRO N     CA     sing N N 337 
PRO N     CD     sing N N 338 
PRO N     H      sing N N 339 
PRO CA    C      sing N N 340 
PRO CA    CB     sing N N 341 
PRO CA    HA     sing N N 342 
PRO C     O      doub N N 343 
PRO C     OXT    sing N N 344 
PRO CB    CG     sing N N 345 
PRO CB    HB2    sing N N 346 
PRO CB    HB3    sing N N 347 
PRO CG    CD     sing N N 348 
PRO CG    HG2    sing N N 349 
PRO CG    HG3    sing N N 350 
PRO CD    HD2    sing N N 351 
PRO CD    HD3    sing N N 352 
PRO OXT   HXT    sing N N 353 
SER N     CA     sing N N 354 
SER N     H      sing N N 355 
SER N     H2     sing N N 356 
SER CA    C      sing N N 357 
SER CA    CB     sing N N 358 
SER CA    HA     sing N N 359 
SER C     O      doub N N 360 
SER C     OXT    sing N N 361 
SER CB    OG     sing N N 362 
SER CB    HB2    sing N N 363 
SER CB    HB3    sing N N 364 
SER OG    HG     sing N N 365 
SER OXT   HXT    sing N N 366 
THR N     CA     sing N N 367 
THR N     H      sing N N 368 
THR N     H2     sing N N 369 
THR CA    C      sing N N 370 
THR CA    CB     sing N N 371 
THR CA    HA     sing N N 372 
THR C     O      doub N N 373 
THR C     OXT    sing N N 374 
THR CB    OG1    sing N N 375 
THR CB    CG2    sing N N 376 
THR CB    HB     sing N N 377 
THR OG1   HG1    sing N N 378 
THR CG2   HG21   sing N N 379 
THR CG2   HG22   sing N N 380 
THR CG2   HG23   sing N N 381 
THR OXT   HXT    sing N N 382 
TRP N     CA     sing N N 383 
TRP N     H      sing N N 384 
TRP N     H2     sing N N 385 
TRP CA    C      sing N N 386 
TRP CA    CB     sing N N 387 
TRP CA    HA     sing N N 388 
TRP C     O      doub N N 389 
TRP C     OXT    sing N N 390 
TRP CB    CG     sing N N 391 
TRP CB    HB2    sing N N 392 
TRP CB    HB3    sing N N 393 
TRP CG    CD1    doub Y N 394 
TRP CG    CD2    sing Y N 395 
TRP CD1   NE1    sing Y N 396 
TRP CD1   HD1    sing N N 397 
TRP CD2   CE2    doub Y N 398 
TRP CD2   CE3    sing Y N 399 
TRP NE1   CE2    sing Y N 400 
TRP NE1   HE1    sing N N 401 
TRP CE2   CZ2    sing Y N 402 
TRP CE3   CZ3    doub Y N 403 
TRP CE3   HE3    sing N N 404 
TRP CZ2   CH2    doub Y N 405 
TRP CZ2   HZ2    sing N N 406 
TRP CZ3   CH2    sing Y N 407 
TRP CZ3   HZ3    sing N N 408 
TRP CH2   HH2    sing N N 409 
TRP OXT   HXT    sing N N 410 
TYR N     CA     sing N N 411 
TYR N     H      sing N N 412 
TYR N     H2     sing N N 413 
TYR CA    C      sing N N 414 
TYR CA    CB     sing N N 415 
TYR CA    HA     sing N N 416 
TYR C     O      doub N N 417 
TYR C     OXT    sing N N 418 
TYR CB    CG     sing N N 419 
TYR CB    HB2    sing N N 420 
TYR CB    HB3    sing N N 421 
TYR CG    CD1    doub Y N 422 
TYR CG    CD2    sing Y N 423 
TYR CD1   CE1    sing Y N 424 
TYR CD1   HD1    sing N N 425 
TYR CD2   CE2    doub Y N 426 
TYR CD2   HD2    sing N N 427 
TYR CE1   CZ     doub Y N 428 
TYR CE1   HE1    sing N N 429 
TYR CE2   CZ     sing Y N 430 
TYR CE2   HE2    sing N N 431 
TYR CZ    OH     sing N N 432 
TYR OH    HH     sing N N 433 
TYR OXT   HXT    sing N N 434 
VAL N     CA     sing N N 435 
VAL N     H      sing N N 436 
VAL N     H2     sing N N 437 
VAL CA    C      sing N N 438 
VAL CA    CB     sing N N 439 
VAL CA    HA     sing N N 440 
VAL C     O      doub N N 441 
VAL C     OXT    sing N N 442 
VAL CB    CG1    sing N N 443 
VAL CB    CG2    sing N N 444 
VAL CB    HB     sing N N 445 
VAL CG1   HG11   sing N N 446 
VAL CG1   HG12   sing N N 447 
VAL CG1   HG13   sing N N 448 
VAL CG2   HG21   sing N N 449 
VAL CG2   HG22   sing N N 450 
VAL CG2   HG23   sing N N 451 
VAL OXT   HXT    sing N N 452 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           IIS154 
_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   8OR9 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 61 2 2' 
_space_group.name_Hall        'P 61 2 (x,y,z+5/12)' 
_space_group.IT_number        178 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9HRH 
_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]   0.009322 
_atom_sites.fract_transf_matrix[1][2]   0.005382 
_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]   0.010764 
_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]   0.004569 
_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.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . MET A 1 1   ? 27.22280 -6.71206  -32.03838 1.000 28.62796 ? 1    MET A N     1 
ATOM   2    C CA    . MET A 1 1   ? 26.17903 -6.35149  -31.08601 1.000 26.05562 ? 1    MET A CA    1 
ATOM   3    C C     . MET A 1 1   ? 26.63709 -5.25117  -30.13549 1.000 22.75270 ? 1    MET A C     1 
ATOM   4    O O     . MET A 1 1   ? 27.75707 -5.29285  -29.63222 1.000 22.25009 ? 1    MET A O     1 
ATOM   5    C CB    . MET A 1 1   ? 25.73654 -7.57464  -30.28029 1.000 21.85236 ? 1    MET A CB    1 
ATOM   6    C CG    . MET A 1 1   ? 24.43754 -7.36606  -29.52115 1.000 24.13997 ? 1    MET A CG    1 
ATOM   7    S SD    . MET A 1 1   ? 23.80714 -8.84081  -28.69352 1.000 30.09382 ? 1    MET A SD    1 
ATOM   8    C CE    . MET A 1 1   ? 24.72420 -10.11203 -29.53669 1.000 27.17191 ? 1    MET A CE    1 
ATOM   9    N N     . ASN A 1 2   ? 25.77115 -4.27113  -29.89004 1.000 21.99760 ? 2    ASN A N     1 
ATOM   10   C CA    . ASN A 1 2   ? 26.06947 -3.23272  -28.91935 1.000 22.91377 ? 2    ASN A CA    1 
ATOM   11   C C     . ASN A 1 2   ? 25.29776 -3.51004  -27.62813 1.000 24.03679 ? 2    ASN A C     1 
ATOM   12   O O     . ASN A 1 2   ? 24.49562 -4.44379  -27.54241 1.000 22.12108 ? 2    ASN A O     1 
ATOM   13   C CB    . ASN A 1 2   ? 25.77121 -1.84265  -29.50435 1.000 24.69359 ? 2    ASN A CB    1 
ATOM   14   C CG    . ASN A 1 2   ? 24.29147 -1.60495  -29.78485 1.000 28.95594 ? 2    ASN A CG    1 
ATOM   15   O OD1   . ASN A 1 2   ? 23.41143 -2.12999  -29.10897 1.000 28.27484 ? 2    ASN A OD1   1 
ATOM   16   N ND2   . ASN A 1 2   ? 24.01744 -0.80756  -30.81307 1.000 33.19696 ? 2    ASN A ND2   1 
ATOM   17   N N     . ALA A 1 3   ? 25.53877 -2.67661  -26.61201 1.000 23.58706 ? 3    ALA A N     1 
ATOM   18   C CA    . ALA A 1 3   ? 24.99206 -2.95182  -25.28613 1.000 21.92600 ? 3    ALA A CA    1 
ATOM   19   C C     . ALA A 1 3   ? 23.47125 -2.86624  -25.25547 1.000 22.98821 ? 3    ALA A C     1 
ATOM   20   O O     . ALA A 1 3   ? 22.83160 -3.59615  -24.48961 1.000 22.65794 ? 3    ALA A O     1 
ATOM   21   C CB    . ALA A 1 3   ? 25.59026 -1.99376  -24.25838 1.000 22.13498 ? 3    ALA A CB    1 
ATOM   22   N N     . SER A 1 4   ? 22.87582 -1.98716  -26.06512 1.000 24.06630 ? 4    SER A N     1 
ATOM   23   C CA    . SER A 1 4   ? 21.42063 -1.87207  -26.07955 1.000 24.33330 ? 4    SER A CA    1 
ATOM   24   C C     . SER A 1 4   ? 20.77241 -3.16681  -26.55290 1.000 23.52348 ? 4    SER A C     1 
ATOM   25   O O     . SER A 1 4   ? 19.77170 -3.61669  -25.98048 1.000 23.22054 ? 4    SER A O     1 
ATOM   26   C CB    . SER A 1 4   ? 20.99440 -0.70112  -26.96395 1.000 27.59227 ? 4    SER A CB    1 
ATOM   27   O OG    . SER A 1 4   ? 19.60157 -0.73850  -27.21406 1.000 37.04740 ? 4    SER A OG    1 
ATOM   28   N N     . GLU A 1 5   ? 21.32578 -3.77745  -27.60320 1.000 23.29138 ? 5    GLU A N     1 
ATOM   29   C CA    A GLU A 1 5   ? 20.80996 -5.06379  -28.05673 0.511 24.52024 ? 5    GLU A CA    1 
ATOM   30   C CA    B GLU A 1 5   ? 20.81675 -5.06447  -28.06295 0.489 24.52342 ? 5    GLU A CA    1 
ATOM   31   C C     . GLU A 1 5   ? 21.10978 -6.16952  -27.05495 1.000 21.34181 ? 5    GLU A C     1 
ATOM   32   O O     . GLU A 1 5   ? 20.31286 -7.10379  -26.91093 1.000 21.41913 ? 5    GLU A O     1 
ATOM   33   C CB    A GLU A 1 5   ? 21.38550 -5.41208  -29.43149 0.511 26.63791 ? 5    GLU A CB    1 
ATOM   34   C CB    B GLU A 1 5   ? 21.41655 -5.39486  -29.43137 0.489 26.60150 ? 5    GLU A CB    1 
ATOM   35   C CG    A GLU A 1 5   ? 20.91551 -6.74890  -29.99172 0.511 25.61220 ? 5    GLU A CG    1 
ATOM   36   C CG    B GLU A 1 5   ? 21.54846 -4.18541  -30.34371 0.489 26.30864 ? 5    GLU A CG    1 
ATOM   37   C CD    A GLU A 1 5   ? 19.54823 -6.67144  -30.63853 0.511 29.12655 ? 5    GLU A CD    1 
ATOM   38   C CD    B GLU A 1 5   ? 22.08902 -4.53064  -31.71319 0.489 27.78396 ? 5    GLU A CD    1 
ATOM   39   O OE1   A GLU A 1 5   ? 18.94064 -5.58013  -30.63007 0.511 29.57583 ? 5    GLU A OE1   1 
ATOM   40   O OE1   B GLU A 1 5   ? 23.27434 -4.91266  -31.80619 0.489 25.57380 ? 5    GLU A OE1   1 
ATOM   41   O OE2   A GLU A 1 5   ? 19.07895 -7.70727  -31.15363 0.511 28.45332 ? 5    GLU A OE2   1 
ATOM   42   O OE2   B GLU A 1 5   ? 21.33228 -4.40680  -32.69754 0.489 30.36367 ? 5    GLU A OE2   1 
ATOM   43   N N     . PHE A 1 6   ? 22.23704 -6.07686  -26.34437 1.000 20.99084 ? 6    PHE A N     1 
ATOM   44   C CA    . PHE A 1 6   ? 22.52495 -7.05905  -25.30507 1.000 19.93272 ? 6    PHE A CA    1 
ATOM   45   C C     . PHE A 1 6   ? 21.53322 -6.95199  -24.15474 1.000 19.84818 ? 6    PHE A C     1 
ATOM   46   O O     . PHE A 1 6   ? 21.17923 -7.96635  -23.54172 1.000 18.25267 ? 6    PHE A O     1 
ATOM   47   C CB    . PHE A 1 6   ? 23.95204 -6.89689  -24.78576 1.000 19.86910 ? 6    PHE A CB    1 
ATOM   48   C CG    . PHE A 1 6   ? 24.28972 -7.83396  -23.65719 1.000 17.60217 ? 6    PHE A CG    1 
ATOM   49   C CD1   . PHE A 1 6   ? 24.43230 -9.19443  -23.88214 1.000 16.34538 ? 6    PHE A CD1   1 
ATOM   50   C CD2   . PHE A 1 6   ? 24.45585 -7.35352  -22.36791 1.000 16.17327 ? 6    PHE A CD2   1 
ATOM   51   C CE1   . PHE A 1 6   ? 24.73931 -10.05562 -22.84217 1.000 15.45375 ? 6    PHE A CE1   1 
ATOM   52   C CE2   . PHE A 1 6   ? 24.76284 -8.20974  -21.32608 1.000 15.19868 ? 6    PHE A CE2   1 
ATOM   53   C CZ    . PHE A 1 6   ? 24.90439 -9.56159  -21.56377 1.000 15.86521 ? 6    PHE A CZ    1 
ATOM   54   N N     . ARG A 1 7   ? 21.08417 -5.73196  -23.83924 1.000 17.86670 ? 7    ARG A N     1 
ATOM   55   C CA    . ARG A 1 7   ? 20.04427 -5.56851  -22.82696 1.000 21.46666 ? 7    ARG A CA    1 
ATOM   56   C C     . ARG A 1 7   ? 18.81476 -6.39763  -23.16860 1.000 18.82301 ? 7    ARG A C     1 
ATOM   57   O O     . ARG A 1 7   ? 18.21734 -7.02863  -22.28966 1.000 21.45218 ? 7    ARG A O     1 
ATOM   58   C CB    . ARG A 1 7   ? 19.66097 -4.09510  -22.68590 1.000 20.81815 ? 7    ARG A CB    1 
ATOM   59   C CG    . ARG A 1 7   ? 20.71387 -3.21766  -22.04423 1.000 23.17471 ? 7    ARG A CG    1 
ATOM   60   C CD    . ARG A 1 7   ? 20.15053 -1.83794  -21.74508 1.000 23.71911 ? 7    ARG A CD    1 
ATOM   61   N NE    . ARG A 1 7   ? 21.19208 -0.87042  -21.42195 1.000 24.51879 ? 7    ARG A NE    1 
ATOM   62   C CZ    . ARG A 1 7   ? 21.68670 -0.67572  -20.20685 1.000 22.27361 ? 7    ARG A CZ    1 
ATOM   63   N NH1   . ARG A 1 7   ? 21.25824 -1.37086  -19.16491 1.000 20.78159 ? 7    ARG A NH1   1 
ATOM   64   N NH2   . ARG A 1 7   ? 22.63410 0.24116   -20.03186 1.000 22.24413 ? 7    ARG A NH2   1 
ATOM   65   N N     . ARG A 1 8   ? 18.42481 -6.41237  -24.44371 1.000 18.92804 ? 8    ARG A N     1 
ATOM   66   C CA    . ARG A 1 8   ? 17.28902 -7.22521  -24.86434 1.000 17.93863 ? 8    ARG A CA    1 
ATOM   67   C C     . ARG A 1 8   ? 17.63801 -8.70815  -24.86071 1.000 20.12594 ? 8    ARG A C     1 
ATOM   68   O O     . ARG A 1 8   ? 16.98131 -9.51366  -24.19087 1.000 18.55051 ? 8    ARG A O     1 
ATOM   69   C CB    . ARG A 1 8   ? 16.82181 -6.80213  -26.25585 1.000 21.27150 ? 8    ARG A CB    1 
ATOM   70   C CG    . ARG A 1 8   ? 15.66924 -7.64717  -26.76319 1.000 26.47376 ? 8    ARG A CG    1 
ATOM   71   C CD    . ARG A 1 8   ? 15.31531 -7.33629  -28.20171 1.000 29.08509 ? 8    ARG A CD    1 
ATOM   72   N NE    . ARG A 1 8   ? 14.37506 -8.32207  -28.72095 1.000 31.29480 ? 8    ARG A NE    1 
ATOM   73   C CZ    . ARG A 1 8   ? 13.95323 -8.37165  -29.97628 1.000 34.90128 ? 8    ARG A CZ    1 
ATOM   74   N NH1   . ARG A 1 8   ? 14.37230 -7.50194  -30.88010 1.000 35.92168 ? 8    ARG A NH1   1 
ATOM   75   N NH2   . ARG A 1 8   ? 13.09360 -9.32168  -30.33461 1.000 36.71112 ? 8    ARG A NH2   1 
ATOM   76   N N     . ARG A 1 9   ? 18.66779 -9.08843  -25.62130 1.000 18.98703 ? 9    ARG A N     1 
ATOM   77   C CA    . ARG A 1 9   ? 18.97278 -10.50310 -25.80714 1.000 18.01283 ? 9    ARG A CA    1 
ATOM   78   C C     . ARG A 1 9   ? 19.47311 -11.14940 -24.52241 1.000 16.64748 ? 9    ARG A C     1 
ATOM   79   O O     . ARG A 1 9   ? 19.21975 -12.33761 -24.29117 1.000 18.02824 ? 9    ARG A O     1 
ATOM   80   C CB    . ARG A 1 9   ? 20.00009 -10.67494 -26.92712 1.000 18.34831 ? 9    ARG A CB    1 
ATOM   81   C CG    . ARG A 1 9   ? 19.60182 -10.00980 -28.23512 1.000 20.25242 ? 9    ARG A CG    1 
ATOM   82   C CD    . ARG A 1 9   ? 18.20729 -10.43964 -28.65887 1.000 23.53842 ? 9    ARG A CD    1 
ATOM   83   N NE    . ARG A 1 9   ? 17.93911 -10.15255 -30.06247 1.000 24.75325 ? 9    ARG A NE    1 
ATOM   84   C CZ    . ARG A 1 9   ? 16.88735 -10.60765 -30.72934 1.000 25.29215 ? 9    ARG A CZ    1 
ATOM   85   N NH1   . ARG A 1 9   ? 15.97024 -11.35958 -30.14298 1.000 25.12877 ? 9    ARG A NH1   1 
ATOM   86   N NH2   . ARG A 1 9   ? 16.75104 -10.29890 -32.01622 1.000 27.07686 ? 9    ARG A NH2   1 
ATOM   87   N N     . GLY A 1 10  ? 20.17666 -10.39084 -23.67955 1.000 16.47536 ? 10   GLY A N     1 
ATOM   88   C CA    . GLY A 1 10  ? 20.64840 -10.94537 -22.42103 1.000 15.60981 ? 10   GLY A CA    1 
ATOM   89   C C     . GLY A 1 10  ? 19.51388 -11.35776 -21.50400 1.000 16.22274 ? 10   GLY A C     1 
ATOM   90   O O     . GLY A 1 10  ? 19.54941 -12.43229 -20.89905 1.000 15.51744 ? 10   GLY A O     1 
ATOM   91   N N     . LYS A 1 11  ? 18.48932 -10.51136 -21.38893 1.000 16.34511 ? 11   LYS A N     1 
ATOM   92   C CA    . LYS A 1 11  ? 17.33042 -10.87753 -20.58369 1.000 16.78766 ? 11   LYS A CA    1 
ATOM   93   C C     . LYS A 1 11  ? 16.53140 -12.00045 -21.23162 1.000 16.95273 ? 11   LYS A C     1 
ATOM   94   O O     . LYS A 1 11  ? 15.92327 -12.81196 -20.52473 1.000 17.87919 ? 11   LYS A O     1 
ATOM   95   C CB    . LYS A 1 11  ? 16.45314 -9.64885  -20.34000 1.000 18.25120 ? 11   LYS A CB    1 
ATOM   96   C CG    . LYS A 1 11  ? 17.20827 -8.48590  -19.71327 1.000 17.30569 ? 11   LYS A CG    1 
ATOM   97   C CD    . LYS A 1 11  ? 16.28507 -7.33437  -19.35936 1.000 19.46052 ? 11   LYS A CD    1 
ATOM   98   C CE    . LYS A 1 11  ? 17.07466 -6.15518  -18.80948 1.000 18.11185 ? 11   LYS A CE    1 
ATOM   99   N NZ    . LYS A 1 11  ? 16.19081 -5.08274  -18.27585 1.000 22.22171 ? 11   LYS A NZ    1 
ATOM   100  N N     . GLU A 1 12  ? 16.52661 -12.07170 -22.56469 1.000 16.10189 ? 12   GLU A N     1 
ATOM   101  C CA    . GLU A 1 12  ? 15.89172 -13.20186 -23.23377 1.000 16.38802 ? 12   GLU A CA    1 
ATOM   102  C C     . GLU A 1 12  ? 16.63927 -14.49789 -22.94339 1.000 17.07138 ? 12   GLU A C     1 
ATOM   103  O O     . GLU A 1 12  ? 16.01744 -15.54833 -22.74010 1.000 15.95216 ? 12   GLU A O     1 
ATOM   104  C CB    . GLU A 1 12  ? 15.81179 -12.94808 -24.73869 1.000 20.16491 ? 12   GLU A CB    1 
ATOM   105  C CG    . GLU A 1 12  ? 14.84386 -11.83887 -25.11712 1.000 22.22436 ? 12   GLU A CG    1 
ATOM   106  C CD    . GLU A 1 12  ? 14.85289 -11.52850 -26.60053 1.000 26.53316 ? 12   GLU A CD    1 
ATOM   107  O OE1   . GLU A 1 12  ? 15.74407 -12.03494 -27.31341 1.000 27.18967 ? 12   GLU A OE1   1 
ATOM   108  O OE2   . GLU A 1 12  ? 13.96606 -10.77461 -27.05306 1.000 26.35588 ? 12   GLU A OE2   1 
ATOM   109  N N     . MET A 1 13  ? 17.97475 -14.44173 -22.91610 1.000 15.40639 ? 13   MET A N     1 
ATOM   110  C CA    . MET A 1 13  ? 18.76357 -15.61921 -22.56258 1.000 13.63039 ? 13   MET A CA    1 
ATOM   111  C C     . MET A 1 13  ? 18.53717 -16.02177 -21.11116 1.000 16.16305 ? 13   MET A C     1 
ATOM   112  O O     . MET A 1 13  ? 18.52604 -17.21609 -20.78931 1.000 16.45549 ? 13   MET A O     1 
ATOM   113  C CB    . MET A 1 13  ? 20.24816 -15.35438 -22.81207 1.000 15.05358 ? 13   MET A CB    1 
ATOM   114  C CG    . MET A 1 13  ? 21.15393 -16.56532 -22.59296 1.000 13.75834 ? 13   MET A CG    1 
ATOM   115  S SD    . MET A 1 13  ? 20.68556 -18.03365 -23.53242 1.000 17.57835 ? 13   MET A SD    1 
ATOM   116  C CE    . MET A 1 13  ? 21.55494 -17.71112 -25.06445 1.000 16.84512 ? 13   MET A CE    1 
ATOM   117  N N     . VAL A 1 14  ? 18.37444 -15.04018 -20.21828 1.000 13.56689 ? 14   VAL A N     1 
ATOM   118  C CA    . VAL A 1 14  ? 18.06206 -15.35082 -18.82523 1.000 14.78286 ? 14   VAL A CA    1 
ATOM   119  C C     . VAL A 1 14  ? 16.78010 -16.16553 -18.74338 1.000 16.42643 ? 14   VAL A C     1 
ATOM   120  O O     . VAL A 1 14  ? 16.70728 -17.17198 -18.02658 1.000 15.87407 ? 14   VAL A O     1 
ATOM   121  C CB    . VAL A 1 14  ? 17.96033 -14.05878 -17.99167 1.000 15.95906 ? 14   VAL A CB    1 
ATOM   122  C CG1   . VAL A 1 14  ? 17.30255 -14.34441 -16.65028 1.000 14.75238 ? 14   VAL A CG1   1 
ATOM   123  C CG2   . VAL A 1 14  ? 19.33194 -13.44087 -17.78605 1.000 14.68263 ? 14   VAL A CG2   1 
ATOM   124  N N     . ASP A 1 15  ? 15.75216 -15.74930 -19.48540 1.000 16.06433 ? 15   ASP A N     1 
ATOM   125  C CA    . ASP A 1 15  ? 14.48867 -16.47763 -19.47412 1.000 16.94052 ? 15   ASP A CA    1 
ATOM   126  C C     . ASP A 1 15  ? 14.63901 -17.85822 -20.09889 1.000 16.26730 ? 15   ASP A C     1 
ATOM   127  O O     . ASP A 1 15  ? 14.01622 -18.82212 -19.63911 1.000 17.74164 ? 15   ASP A O     1 
ATOM   128  C CB    . ASP A 1 15  ? 13.41394 -15.67100 -20.19887 1.000 17.37163 ? 15   ASP A CB    1 
ATOM   129  C CG    . ASP A 1 15  ? 12.71773 -14.68573 -19.28454 1.000 19.45253 ? 15   ASP A CG    1 
ATOM   130  O OD1   . ASP A 1 15  ? 12.68442 -14.93322 -18.05989 1.000 20.57591 ? 15   ASP A OD1   1 
ATOM   131  O OD2   . ASP A 1 15  ? 12.21160 -13.66143 -19.78695 1.000 23.82594 ? 15   ASP A OD2   1 
ATOM   132  N N     . TYR A 1 16  ? 15.45898 -17.97563 -21.14633 1.000 15.63645 ? 16   TYR A N     1 
ATOM   133  C CA    . TYR A 1 16  ? 15.67617 -19.27847 -21.76834 1.000 16.32176 ? 16   TYR A CA    1 
ATOM   134  C C     . TYR A 1 16  ? 16.37001 -20.23325 -20.80616 1.000 16.76877 ? 16   TYR A C     1 
ATOM   135  O O     . TYR A 1 16  ? 15.98928 -21.40512 -20.69290 1.000 16.73658 ? 16   TYR A O     1 
ATOM   136  C CB    . TYR A 1 16  ? 16.49981 -19.12807 -23.04626 1.000 18.21424 ? 16   TYR A CB    1 
ATOM   137  C CG    . TYR A 1 16  ? 16.73535 -20.44195 -23.75528 1.000 19.60041 ? 16   TYR A CG    1 
ATOM   138  C CD1   . TYR A 1 16  ? 15.72601 -21.04279 -24.49497 1.000 21.15449 ? 16   TYR A CD1   1 
ATOM   139  C CD2   . TYR A 1 16  ? 17.95501 -21.09818 -23.65738 1.000 21.43353 ? 16   TYR A CD2   1 
ATOM   140  C CE1   . TYR A 1 16  ? 15.93173 -22.24856 -25.13724 1.000 22.56156 ? 16   TYR A CE1   1 
ATOM   141  C CE2   . TYR A 1 16  ? 18.16956 -22.30637 -24.29369 1.000 21.45918 ? 16   TYR A CE2   1 
ATOM   142  C CZ    . TYR A 1 16  ? 17.15360 -22.87639 -25.03251 1.000 23.87644 ? 16   TYR A CZ    1 
ATOM   143  O OH    . TYR A 1 16  ? 17.36088 -24.07912 -25.66827 1.000 25.42966 ? 16   TYR A OH    1 
ATOM   144  N N     . VAL A 1 17  ? 17.40624 -19.74912 -20.11733 1.000 14.79388 ? 17   VAL A N     1 
ATOM   145  C CA    . VAL A 1 17  ? 18.11842 -20.57949 -19.15070 1.000 16.41892 ? 17   VAL A CA    1 
ATOM   146  C C     . VAL A 1 17  ? 17.18786 -21.00590 -18.02514 1.000 16.47405 ? 17   VAL A C     1 
ATOM   147  O O     . VAL A 1 17  ? 17.18103 -22.17269 -17.61161 1.000 14.80017 ? 17   VAL A O     1 
ATOM   148  C CB    . VAL A 1 17  ? 19.35024 -19.82922 -18.61362 1.000 17.72437 ? 17   VAL A CB    1 
ATOM   149  C CG1   . VAL A 1 17  ? 19.92248 -20.54758 -17.40521 1.000 18.61092 ? 17   VAL A CG1   1 
ATOM   150  C CG2   . VAL A 1 17  ? 20.40044 -19.70520 -19.69982 1.000 17.45174 ? 17   VAL A CG2   1 
ATOM   151  N N     . ALA A 1 18  ? 16.38712 -20.06899 -17.51329 1.000 15.85263 ? 18   ALA A N     1 
ATOM   152  C CA    . ALA A 1 18  ? 15.45698 -20.39782 -16.43960 1.000 16.68228 ? 18   ALA A CA    1 
ATOM   153  C C     . ALA A 1 18  ? 14.40194 -21.39292 -16.90679 1.000 19.42003 ? 18   ALA A C     1 
ATOM   154  O O     . ALA A 1 18  ? 14.02602 -22.30443 -16.16010 1.000 16.72007 ? 18   ALA A O     1 
ATOM   155  C CB    . ALA A 1 18  ? 14.80227 -19.12413 -15.90799 1.000 17.57665 ? 18   ALA A CB    1 
ATOM   156  N N     . ASN A 1 19  ? 13.91358 -21.23631 -18.14147 1.000 16.49083 ? 19   ASN A N     1 
ATOM   157  C CA    . ASN A 1 19  ? 12.94984 -22.19039 -18.68246 1.000 18.35344 ? 19   ASN A CA    1 
ATOM   158  C C     . ASN A 1 19  ? 13.55831 -23.58028 -18.80416 1.000 19.56400 ? 19   ASN A C     1 
ATOM   159  O O     . ASN A 1 19  ? 12.90437 -24.58239 -18.49011 1.000 18.46515 ? 19   ASN A O     1 
ATOM   160  C CB    . ASN A 1 19  ? 12.44105 -21.71798 -20.04474 1.000 17.77081 ? 19   ASN A CB    1 
ATOM   161  C CG    . ASN A 1 19  ? 11.54866 -20.50122 -19.94522 1.000 19.97313 ? 19   ASN A CG    1 
ATOM   162  O OD1   . ASN A 1 19  ? 11.07544 -20.15235 -18.86551 1.000 21.69346 ? 19   ASN A OD1   1 
ATOM   163  N ND2   . ASN A 1 19  ? 11.30567 -19.85107 -21.07818 1.000 20.66459 ? 19   ASN A ND2   1 
ATOM   164  N N     . TYR A 1 20  ? 14.80772 -23.66008 -19.26839 1.000 16.53417 ? 20   TYR A N     1 
ATOM   165  C CA    . TYR A 1 20  ? 15.46923 -24.95300 -19.41166 1.000 16.61505 ? 20   TYR A CA    1 
ATOM   166  C C     . TYR A 1 20  ? 15.60269 -25.64903 -18.06330 1.000 17.29583 ? 20   TYR A C     1 
ATOM   167  O O     . TYR A 1 20  ? 15.30785 -26.84315 -17.93342 1.000 18.32992 ? 20   TYR A O     1 
ATOM   168  C CB    . TYR A 1 20  ? 16.84355 -24.76492 -20.05482 1.000 16.44075 ? 20   TYR A CB    1 
ATOM   169  C CG    . TYR A 1 20  ? 17.75994 -25.95922 -19.90745 1.000 17.29423 ? 20   TYR A CG    1 
ATOM   170  C CD1   . TYR A 1 20  ? 17.48410 -27.15381 -20.56008 1.000 17.49109 ? 20   TYR A CD1   1 
ATOM   171  C CD2   . TYR A 1 20  ? 18.89167 -25.89796 -19.10463 1.000 16.30881 ? 20   TYR A CD2   1 
ATOM   172  C CE1   . TYR A 1 20  ? 18.31722 -28.24892 -20.43044 1.000 17.06656 ? 20   TYR A CE1   1 
ATOM   173  C CE2   . TYR A 1 20  ? 19.72994 -26.99033 -18.96554 1.000 18.50289 ? 20   TYR A CE2   1 
ATOM   174  C CZ    . TYR A 1 20  ? 19.43623 -28.16319 -19.63068 1.000 16.73966 ? 20   TYR A CZ    1 
ATOM   175  O OH    . TYR A 1 20  ? 20.26341 -29.25647 -19.49930 1.000 17.55380 ? 20   TYR A OH    1 
ATOM   176  N N     . MET A 1 21  ? 16.04579 -24.90905 -17.04359 1.000 16.69220 ? 21   MET A N     1 
ATOM   177  C CA    . MET A 1 21  ? 16.21189 -25.48815 -15.71364 1.000 18.05651 ? 21   MET A CA    1 
ATOM   178  C C     . MET A 1 21  ? 14.88045 -25.91897 -15.11322 1.000 19.70808 ? 21   MET A C     1 
ATOM   179  O O     . MET A 1 21  ? 14.78864 -26.98990 -14.50245 1.000 18.52966 ? 21   MET A O     1 
ATOM   180  C CB    . MET A 1 21  ? 16.90833 -24.48954 -14.79194 1.000 18.51218 ? 21   MET A CB    1 
ATOM   181  C CG    . MET A 1 21  ? 18.40467 -24.42961 -14.97370 1.000 19.73437 ? 21   MET A CG    1 
ATOM   182  S SD    . MET A 1 21  ? 19.12893 -26.01870 -14.53290 1.000 24.91534 ? 21   MET A SD    1 
ATOM   183  C CE    . MET A 1 21  ? 20.72156 -25.89485 -15.32756 1.000 23.47747 ? 21   MET A CE    1 
ATOM   184  N N     . GLU A 1 22  ? 13.83965 -25.10006 -15.26816 1.000 18.38956 ? 22   GLU A N     1 
ATOM   185  C CA    . GLU A 1 22  ? 12.56741 -25.41159 -14.62664 1.000 20.78893 ? 22   GLU A CA    1 
ATOM   186  C C     . GLU A 1 22  ? 11.88981 -26.61845 -15.26033 1.000 21.83963 ? 22   GLU A C     1 
ATOM   187  O O     . GLU A 1 22  ? 11.10740 -27.30642 -14.59617 1.000 24.33850 ? 22   GLU A O     1 
ATOM   188  C CB    . GLU A 1 22  ? 11.64639 -24.19489 -14.67078 1.000 23.38630 ? 22   GLU A CB    1 
ATOM   189  C CG    . GLU A 1 22  ? 11.96406 -23.18340 -13.58553 1.000 25.64683 ? 22   GLU A CG    1 
ATOM   190  C CD    . GLU A 1 22  ? 10.92336 -22.08975 -13.45950 1.000 28.07201 ? 22   GLU A CD    1 
ATOM   191  O OE1   . GLU A 1 22  ? 10.30780 -21.73254 -14.48494 1.000 30.69190 ? 22   GLU A OE1   1 
ATOM   192  O OE2   . GLU A 1 22  ? 10.72893 -21.58029 -12.33412 1.000 32.37405 ? 22   GLU A OE2   1 
ATOM   193  N N     . GLY A 1 23  ? 12.17677 -26.90008 -16.52571 1.000 19.13426 ? 23   GLY A N     1 
ATOM   194  C CA    . GLY A 1 23  ? 11.54277 -28.01697 -17.19370 1.000 22.47092 ? 23   GLY A CA    1 
ATOM   195  C C     . GLY A 1 23  ? 12.49495 -29.16643 -17.45162 1.000 21.46405 ? 23   GLY A C     1 
ATOM   196  O O     . GLY A 1 23  ? 12.20631 -30.05235 -18.26264 1.000 23.28863 ? 23   GLY A O     1 
ATOM   197  N N     . ILE A 1 24  ? 13.63129 -29.17157 -16.74703 1.000 19.35038 ? 24   ILE A N     1 
ATOM   198  C CA    . ILE A 1 24  ? 14.68410 -30.14737 -17.01831 1.000 20.09327 ? 24   ILE A CA    1 
ATOM   199  C C     . ILE A 1 24  ? 14.25035 -31.57475 -16.71116 1.000 22.63538 ? 24   ILE A C     1 
ATOM   200  O O     . ILE A 1 24  ? 14.80165 -32.52169 -17.28409 1.000 22.96590 ? 24   ILE A O     1 
ATOM   201  C CB    . ILE A 1 24  ? 15.96494 -29.78652 -16.24219 1.000 18.32712 ? 24   ILE A CB    1 
ATOM   202  C CG1   . ILE A 1 24  ? 17.17624 -30.49138 -16.85860 1.000 19.68647 ? 24   ILE A CG1   1 
ATOM   203  C CG2   . ILE A 1 24  ? 15.82904 -30.13680 -14.75953 1.000 19.19977 ? 24   ILE A CG2   1 
ATOM   204  C CD1   . ILE A 1 24  ? 18.49454 -29.93483 -16.40728 1.000 17.59778 ? 24   ILE A CD1   1 
ATOM   205  N N     . GLU A 1 25  ? 13.25859 -31.76074 -15.83895 1.000 19.75313 ? 25   GLU A N     1 
ATOM   206  C CA    . GLU A 1 25  ? 12.77627 -33.10610 -15.56313 1.000 22.72872 ? 25   GLU A CA    1 
ATOM   207  C C     . GLU A 1 25  ? 12.00080 -33.68413 -16.73757 1.000 25.40936 ? 25   GLU A C     1 
ATOM   208  O O     . GLU A 1 25  ? 11.76157 -34.89361 -16.76858 1.000 30.37373 ? 25   GLU A O     1 
ATOM   209  C CB    . GLU A 1 25  ? 11.91729 -33.11265 -14.30087 1.000 25.29907 ? 25   GLU A CB    1 
ATOM   210  C CG    . GLU A 1 25  ? 12.71923 -33.26225 -13.01773 1.000 26.52815 ? 25   GLU A CG    1 
ATOM   211  C CD    . GLU A 1 25  ? 11.84824 -33.30499 -11.77298 1.000 30.71201 ? 25   GLU A CD    1 
ATOM   212  O OE1   . GLU A 1 25  ? 12.13971 -32.55439 -10.81464 1.000 34.79274 ? 25   GLU A OE1   1 
ATOM   213  O OE2   . GLU A 1 25  ? 10.86974 -34.07958 -11.75254 1.000 29.85204 ? 25   GLU A OE2   1 
ATOM   214  N N     . GLY A 1 26  ? 11.59990 -32.85302 -17.69994 1.000 23.95870 ? 26   GLY A N     1 
ATOM   215  C CA    . GLY A 1 26  ? 10.96867 -33.34824 -18.90998 1.000 25.30604 ? 26   GLY A CA    1 
ATOM   216  C C     . GLY A 1 26  ? 11.93128 -33.76610 -19.99314 1.000 24.82960 ? 26   GLY A C     1 
ATOM   217  O O     . GLY A 1 26  ? 11.49906 -34.26842 -21.03437 1.000 27.93591 ? 26   GLY A O     1 
ATOM   218  N N     . ARG A 1 27  ? 13.22843 -33.56492 -19.76984 1.000 23.64346 ? 27   ARG A N     1 
ATOM   219  C CA    . ARG A 1 27  ? 14.25994 -33.95876 -20.71806 1.000 24.80816 ? 27   ARG A CA    1 
ATOM   220  C C     . ARG A 1 27  ? 14.70712 -35.39000 -20.46059 1.000 23.55842 ? 27   ARG A C     1 
ATOM   221  O O     . ARG A 1 27  ? 14.87659 -35.80717 -19.31077 1.000 25.28187 ? 27   ARG A O     1 
ATOM   222  C CB    . ARG A 1 27  ? 15.47075 -33.02848 -20.62627 1.000 23.14941 ? 27   ARG A CB    1 
ATOM   223  C CG    . ARG A 1 27  ? 15.16642 -31.54727 -20.70736 1.000 24.57722 ? 27   ARG A CG    1 
ATOM   224  C CD    . ARG A 1 27  ? 15.64716 -30.99781 -22.03844 1.000 20.90456 ? 27   ARG A CD    1 
ATOM   225  N NE    . ARG A 1 27  ? 15.18619 -29.63807 -22.28545 1.000 19.38588 ? 27   ARG A NE    1 
ATOM   226  C CZ    . ARG A 1 27  ? 15.13381 -29.07312 -23.48411 1.000 21.41262 ? 27   ARG A CZ    1 
ATOM   227  N NH1   . ARG A 1 27  ? 15.47358 -29.73735 -24.57730 1.000 21.51387 ? 27   ARG A NH1   1 
ATOM   228  N NH2   . ARG A 1 27  ? 14.73494 -27.80866 -23.58835 1.000 22.03365 ? 27   ARG A NH2   1 
ATOM   229  N N     . GLN A 1 28  ? 14.89850 -36.13705 -21.54195 1.000 20.93458 ? 28   GLN A N     1 
ATOM   230  C CA    . GLN A 1 28  ? 15.56956 -37.42569 -21.45212 1.000 20.58820 ? 28   GLN A CA    1 
ATOM   231  C C     . GLN A 1 28  ? 17.02331 -37.19233 -21.05864 1.000 19.00432 ? 28   GLN A C     1 
ATOM   232  O O     . GLN A 1 28  ? 17.74356 -36.45264 -21.73751 1.000 19.31668 ? 28   GLN A O     1 
ATOM   233  C CB    . GLN A 1 28  ? 15.47169 -38.16387 -22.78320 1.000 22.18204 ? 28   GLN A CB    1 
ATOM   234  C CG    . GLN A 1 28  ? 16.25476 -39.46124 -22.84427 1.000 24.81168 ? 28   GLN A CG    1 
ATOM   235  C CD    . GLN A 1 28  ? 15.97977 -40.23990 -24.11583 1.000 28.21772 ? 28   GLN A CD    1 
ATOM   236  O OE1   . GLN A 1 28  ? 14.85358 -40.67413 -24.35717 1.000 34.82595 ? 28   GLN A OE1   1 
ATOM   237  N NE2   . GLN A 1 28  ? 17.00672 -40.41385 -24.94055 1.000 22.60043 ? 28   GLN A NE2   1 
ATOM   238  N N     . VAL A 1 29  ? 17.45124 -37.81374 -19.95691 1.000 19.99338 ? 29   VAL A N     1 
ATOM   239  C CA    . VAL A 1 29  ? 18.72640 -37.44444 -19.34600 1.000 17.88731 ? 29   VAL A CA    1 
ATOM   240  C C     . VAL A 1 29  ? 19.88893 -37.74751 -20.28447 1.000 17.62332 ? 29   VAL A C     1 
ATOM   241  O O     . VAL A 1 29  ? 20.84716 -36.96977 -20.37843 1.000 16.07723 ? 29   VAL A O     1 
ATOM   242  C CB    . VAL A 1 29  ? 18.88946 -38.14053 -17.97993 1.000 16.23640 ? 29   VAL A CB    1 
ATOM   243  C CG1   . VAL A 1 29  ? 18.79677 -39.65593 -18.11787 1.000 20.90548 ? 29   VAL A CG1   1 
ATOM   244  C CG2   . VAL A 1 29  ? 20.20422 -37.73379 -17.33252 1.000 16.52881 ? 29   VAL A CG2   1 
ATOM   245  N N     . TYR A 1 30  ? 19.81753 -38.86194 -21.01047 1.000 17.61586 ? 30   TYR A N     1 
ATOM   246  C CA    . TYR A 1 30  ? 20.90443 -39.21540 -21.90124 1.000 18.95479 ? 30   TYR A CA    1 
ATOM   247  C C     . TYR A 1 30  ? 20.40053 -39.27286 -23.33884 1.000 18.67969 ? 30   TYR A C     1 
ATOM   248  O O     . TYR A 1 30  ? 19.31084 -39.79772 -23.59211 1.000 18.68043 ? 30   TYR A O     1 
ATOM   249  C CB    . TYR A 1 30  ? 21.52056 -40.56499 -21.50606 1.000 18.52070 ? 30   TYR A CB    1 
ATOM   250  C CG    . TYR A 1 30  ? 22.76415 -40.92595 -22.28341 1.000 20.31512 ? 30   TYR A CG    1 
ATOM   251  C CD1   . TYR A 1 30  ? 24.01256 -40.47187 -21.87704 1.000 23.32609 ? 30   TYR A CD1   1 
ATOM   252  C CD2   . TYR A 1 30  ? 22.69335 -41.71782 -23.42110 1.000 20.87447 ? 30   TYR A CD2   1 
ATOM   253  C CE1   . TYR A 1 30  ? 25.15485 -40.79837 -22.58173 1.000 25.22408 ? 30   TYR A CE1   1 
ATOM   254  C CE2   . TYR A 1 30  ? 23.82965 -42.04833 -24.13260 1.000 22.98088 ? 30   TYR A CE2   1 
ATOM   255  C CZ    . TYR A 1 30  ? 25.05713 -41.58708 -23.70852 1.000 24.99994 ? 30   TYR A CZ    1 
ATOM   256  O OH    . TYR A 1 30  ? 26.18944 -41.91662 -24.41639 1.000 31.54054 ? 30   TYR A OH    1 
ATOM   257  N N     . PRO A 1 31  ? 21.16027 -38.74530 -24.29296 1.000 18.97666 ? 31   PRO A N     1 
ATOM   258  C CA    . PRO A 1 31  ? 20.63781 -38.56919 -25.64949 1.000 16.78719 ? 31   PRO A CA    1 
ATOM   259  C C     . PRO A 1 31  ? 20.58072 -39.86693 -26.44462 1.000 20.20403 ? 31   PRO A C     1 
ATOM   260  O O     . PRO A 1 31  ? 21.24081 -40.86071 -26.13601 1.000 17.94739 ? 31   PRO A O     1 
ATOM   261  C CB    . PRO A 1 31  ? 21.64209 -37.59158 -26.26869 1.000 18.71989 ? 31   PRO A CB    1 
ATOM   262  C CG    . PRO A 1 31  ? 22.91952 -37.94807 -25.59181 1.000 19.05999 ? 31   PRO A CG    1 
ATOM   263  C CD    . PRO A 1 31  ? 22.50263 -38.15340 -24.15660 1.000 17.37266 ? 31   PRO A CD    1 
ATOM   264  N N     . ASP A 1 32  ? 19.76175 -39.83079 -27.49479 1.000 16.56198 ? 32   ASP A N     1 
ATOM   265  C CA    . ASP A 1 32  ? 19.62876 -40.93013 -28.43985 1.000 18.25739 ? 32   ASP A CA    1 
ATOM   266  C C     . ASP A 1 32  ? 20.44198 -40.71971 -29.70982 1.000 19.71797 ? 32   ASP A C     1 
ATOM   267  O O     . ASP A 1 32  ? 20.38262 -41.56045 -30.61314 1.000 20.58077 ? 32   ASP A O     1 
ATOM   268  C CB    . ASP A 1 32  ? 18.15529 -41.13787 -28.80682 1.000 20.85119 ? 32   ASP A CB    1 
ATOM   269  C CG    . ASP A 1 32  ? 17.41903 -42.00288 -27.80238 1.000 29.25016 ? 32   ASP A CG    1 
ATOM   270  O OD1   . ASP A 1 32  ? 16.37288 -41.55427 -27.29017 1.000 32.00672 ? 32   ASP A OD1   1 
ATOM   271  O OD2   . ASP A 1 32  ? 17.87965 -43.13136 -27.53040 1.000 32.48830 ? 32   ASP A OD2   1 
ATOM   272  N N     . VAL A 1 33  ? 21.19117 -39.61888 -29.80700 1.000 17.08664 ? 33   VAL A N     1 
ATOM   273  C CA    . VAL A 1 33  ? 22.00824 -39.38972 -30.99227 1.000 17.91978 ? 33   VAL A CA    1 
ATOM   274  C C     . VAL A 1 33  ? 23.17496 -40.37228 -31.02051 1.000 18.77362 ? 33   VAL A C     1 
ATOM   275  O O     . VAL A 1 33  ? 23.57049 -40.95439 -30.00340 1.000 19.39618 ? 33   VAL A O     1 
ATOM   276  C CB    . VAL A 1 33  ? 22.50996 -37.93688 -31.04546 1.000 16.86128 ? 33   VAL A CB    1 
ATOM   277  C CG1   . VAL A 1 33  ? 21.34182 -36.96665 -31.09589 1.000 16.07724 ? 33   VAL A CG1   1 
ATOM   278  C CG2   . VAL A 1 33  ? 23.41137 -37.63987 -29.85368 1.000 16.64191 ? 33   VAL A CG2   1 
ATOM   279  N N     . GLU A 1 34  ? 23.72724 -40.56035 -32.21057 1.000 17.59773 ? 34   GLU A N     1 
ATOM   280  C CA    . GLU A 1 34  ? 24.91884 -41.36403 -32.41638 1.000 20.84845 ? 34   GLU A CA    1 
ATOM   281  C C     . GLU A 1 34  ? 26.08735 -40.47946 -32.83299 1.000 18.90655 ? 34   GLU A C     1 
ATOM   282  O O     . GLU A 1 34  ? 25.88835 -39.34931 -33.29204 1.000 18.80019 ? 34   GLU A O     1 
ATOM   283  C CB    . GLU A 1 34  ? 24.66594 -42.44484 -33.47685 1.000 22.27517 ? 34   GLU A CB    1 
ATOM   284  C CG    . GLU A 1 34  ? 23.52769 -43.38466 -33.11720 1.000 27.46383 ? 34   GLU A CG    1 
ATOM   285  C CD    . GLU A 1 34  ? 23.93474 -44.39983 -32.06550 1.000 34.15038 ? 34   GLU A CD    1 
ATOM   286  O OE1   . GLU A 1 34  ? 25.15301 -44.57427 -31.84837 1.000 36.18865 ? 34   GLU A OE1   1 
ATOM   287  O OE2   . GLU A 1 34  ? 23.04056 -45.02178 -31.45384 1.000 38.57122 ? 34   GLU A OE2   1 
ATOM   288  N N     . PRO A 1 35  ? 27.32320 -40.94768 -32.65629 1.000 22.39396 ? 35   PRO A N     1 
ATOM   289  C CA    . PRO A 1 35  ? 28.48488 -40.10983 -32.97490 1.000 19.19959 ? 35   PRO A CA    1 
ATOM   290  C C     . PRO A 1 35  ? 28.45148 -39.58251 -34.40210 1.000 20.78236 ? 35   PRO A C     1 
ATOM   291  O O     . PRO A 1 35  ? 28.27672 -40.33721 -35.36271 1.000 23.85254 ? 35   PRO A O     1 
ATOM   292  C CB    . PRO A 1 35  ? 29.65928 -41.06376 -32.74778 1.000 22.52898 ? 35   PRO A CB    1 
ATOM   293  C CG    . PRO A 1 35  ? 29.18612 -41.90352 -31.61631 1.000 22.79199 ? 35   PRO A CG    1 
ATOM   294  C CD    . PRO A 1 35  ? 27.73943 -42.18482 -31.96897 1.000 22.13396 ? 35   PRO A CD    1 
ATOM   295  N N     . GLY A 1 36  ? 28.60886 -38.26666 -34.52830 1.000 18.44139 ? 36   GLY A N     1 
ATOM   296  C CA    . GLY A 1 36  ? 28.60934 -37.60646 -35.81583 1.000 19.32385 ? 36   GLY A CA    1 
ATOM   297  C C     . GLY A 1 36  ? 27.26739 -37.08216 -36.27549 1.000 18.43783 ? 36   GLY A C     1 
ATOM   298  O O     . GLY A 1 36  ? 27.09918 -36.83631 -37.47576 1.000 21.12296 ? 36   GLY A O     1 
ATOM   299  N N     . TYR A 1 37  ? 26.30655 -36.88507 -35.36562 1.000 15.82613 ? 37   TYR A N     1 
ATOM   300  C CA    . TYR A 1 37  ? 24.95891 -36.55621 -35.81441 1.000 14.58634 ? 37   TYR A CA    1 
ATOM   301  C C     . TYR A 1 37  ? 24.88074 -35.10550 -36.25634 1.000 15.04999 ? 37   TYR A C     1 
ATOM   302  O O     . TYR A 1 37  ? 24.01659 -34.74417 -37.06377 1.000 16.68586 ? 37   TYR A O     1 
ATOM   303  C CB    . TYR A 1 37  ? 23.93023 -36.76102 -34.69774 1.000 16.58653 ? 37   TYR A CB    1 
ATOM   304  C CG    . TYR A 1 37  ? 23.94432 -35.65875 -33.65040 1.000 16.57892 ? 37   TYR A CG    1 
ATOM   305  C CD1   . TYR A 1 37  ? 24.79821 -35.68566 -32.55791 1.000 15.63771 ? 37   TYR A CD1   1 
ATOM   306  C CD2   . TYR A 1 37  ? 23.04322 -34.60099 -33.75283 1.000 16.77141 ? 37   TYR A CD2   1 
ATOM   307  C CE1   . TYR A 1 37  ? 24.78116 -34.66121 -31.61682 1.000 17.09524 ? 37   TYR A CE1   1 
ATOM   308  C CE2   . TYR A 1 37  ? 23.01782 -33.58681 -32.82557 1.000 15.02583 ? 37   TYR A CE2   1 
ATOM   309  C CZ    . TYR A 1 37  ? 23.88052 -33.61524 -31.76140 1.000 15.77169 ? 37   TYR A CZ    1 
ATOM   310  O OH    . TYR A 1 37  ? 23.82896 -32.58801 -30.84821 1.000 15.58178 ? 37   TYR A OH    1 
ATOM   311  N N     . LEU A 1 38  ? 25.76674 -34.26286 -35.71628 1.000 16.21595 ? 38   LEU A N     1 
ATOM   312  C CA    . LEU A 1 38  ? 25.58883 -32.81446 -35.77911 1.000 14.41011 ? 38   LEU A CA    1 
ATOM   313  C C     . LEU A 1 38  ? 26.04478 -32.23217 -37.10851 1.000 14.05501 ? 38   LEU A C     1 
ATOM   314  O O     . LEU A 1 38  ? 25.38940 -31.33107 -37.64253 1.000 16.53202 ? 38   LEU A O     1 
ATOM   315  C CB    . LEU A 1 38  ? 26.34012 -32.14503 -34.62993 1.000 15.09277 ? 38   LEU A CB    1 
ATOM   316  C CG    . LEU A 1 38  ? 26.02440 -30.65984 -34.42279 1.000 16.79032 ? 38   LEU A CG    1 
ATOM   317  C CD1   . LEU A 1 38  ? 24.52466 -30.45572 -34.28161 1.000 18.45102 ? 38   LEU A CD1   1 
ATOM   318  C CD2   . LEU A 1 38  ? 26.75669 -30.12012 -33.20601 1.000 20.39441 ? 38   LEU A CD2   1 
ATOM   319  N N     . ARG A 1 39  ? 27.16135 -32.71957 -37.64657 1.000 16.11376 ? 39   ARG A N     1 
ATOM   320  C CA    . ARG A 1 39  ? 27.68739 -32.16763 -38.89315 1.000 16.74546 ? 39   ARG A CA    1 
ATOM   321  C C     . ARG A 1 39  ? 26.65975 -32.08675 -40.01847 1.000 17.37477 ? 39   ARG A C     1 
ATOM   322  O O     . ARG A 1 39  ? 26.61272 -31.04076 -40.68772 1.000 17.23366 ? 39   ARG A O     1 
ATOM   323  C CB    . ARG A 1 39  ? 28.91728 -32.96790 -39.35102 1.000 17.72924 ? 39   ARG A CB    1 
ATOM   324  C CG    . ARG A 1 39  ? 29.74679 -32.26219 -40.41760 1.000 19.67236 ? 39   ARG A CG    1 
ATOM   325  C CD    . ARG A 1 39  ? 30.92929 -33.10816 -40.86343 1.000 20.11245 ? 39   ARG A CD    1 
ATOM   326  N NE    . ARG A 1 39  ? 32.00673 -33.12664 -39.88191 1.000 23.02819 ? 39   ARG A NE    1 
ATOM   327  C CZ    . ARG A 1 39  ? 32.90539 -32.16305 -39.72653 1.000 28.65827 ? 39   ARG A CZ    1 
ATOM   328  N NH1   . ARG A 1 39  ? 32.88164 -31.06658 -40.46735 1.000 25.12362 ? 39   ARG A NH1   1 
ATOM   329  N NH2   . ARG A 1 39  ? 33.85464 -32.30409 -38.80505 1.000 27.28545 ? 39   ARG A NH2   1 
ATOM   330  N N     . PRO A 1 40  ? 25.82643 -33.10076 -40.28793 1.000 17.41246 ? 40   PRO A N     1 
ATOM   331  C CA    . PRO A 1 40  ? 24.83553 -32.94260 -41.36797 1.000 18.44599 ? 40   PRO A CA    1 
ATOM   332  C C     . PRO A 1 40  ? 23.79034 -31.87246 -41.09431 1.000 16.74208 ? 40   PRO A C     1 
ATOM   333  O O     . PRO A 1 40  ? 23.15746 -31.39627 -42.04439 1.000 15.93974 ? 40   PRO A O     1 
ATOM   334  C CB    . PRO A 1 40  ? 24.18886 -34.33236 -41.47640 1.000 20.22015 ? 40   PRO A CB    1 
ATOM   335  C CG    . PRO A 1 40  ? 25.10620 -35.26453 -40.79219 1.000 20.65274 ? 40   PRO A CG    1 
ATOM   336  C CD    . PRO A 1 40  ? 25.85920 -34.48286 -39.76953 1.000 17.92207 ? 40   PRO A CD    1 
ATOM   337  N N     . LEU A 1 41  ? 23.59589 -31.47129 -39.83804 1.000 14.76181 ? 41   LEU A N     1 
ATOM   338  C CA    . LEU A 1 41  ? 22.54579 -30.53026 -39.46740 1.000 16.86624 ? 41   LEU A CA    1 
ATOM   339  C C     . LEU A 1 41  ? 23.01402 -29.07962 -39.45542 1.000 19.25323 ? 41   LEU A C     1 
ATOM   340  O O     . LEU A 1 41  ? 22.18589 -28.17802 -39.27855 1.000 19.21720 ? 41   LEU A O     1 
ATOM   341  C CB    . LEU A 1 41  ? 21.98837 -30.89959 -38.08839 1.000 16.31924 ? 41   LEU A CB    1 
ATOM   342  C CG    . LEU A 1 41  ? 21.57293 -32.36459 -37.91046 1.000 16.54180 ? 41   LEU A CG    1 
ATOM   343  C CD1   . LEU A 1 41  ? 21.07149 -32.62309 -36.49836 1.000 14.88742 ? 41   LEU A CD1   1 
ATOM   344  C CD2   . LEU A 1 41  ? 20.51502 -32.76856 -38.93351 1.000 15.12263 ? 41   LEU A CD2   1 
ATOM   345  N N     . ILE A 1 42  ? 24.30761 -28.83972 -39.64697 1.000 16.25963 ? 42   ILE A N     1 
ATOM   346  C CA    . ILE A 1 42  ? 24.90576 -27.50862 -39.58401 1.000 18.21059 ? 42   ILE A CA    1 
ATOM   347  C C     . ILE A 1 42  ? 25.56238 -27.22709 -40.93075 1.000 15.40803 ? 42   ILE A C     1 
ATOM   348  O O     . ILE A 1 42  ? 26.10332 -28.15347 -41.55259 1.000 17.15841 ? 42   ILE A O     1 
ATOM   349  C CB    . ILE A 1 42  ? 25.91012 -27.42168 -38.42142 1.000 17.02886 ? 42   ILE A CB    1 
ATOM   350  C CG1   . ILE A 1 42  ? 25.16218 -27.25207 -37.10187 1.000 22.74282 ? 42   ILE A CG1   1 
ATOM   351  C CG2   . ILE A 1 42  ? 26.90719 -26.28287 -38.60505 1.000 23.29593 ? 42   ILE A CG2   1 
ATOM   352  C CD1   . ILE A 1 42  ? 26.06543 -27.22246 -35.89974 1.000 24.08659 ? 42   ILE A CD1   1 
ATOM   353  N N     . PRO A 1 43  ? 25.51770 -25.99198 -41.43494 1.000 17.20954 ? 43   PRO A N     1 
ATOM   354  C CA    . PRO A 1 43  ? 26.21826 -25.68038 -42.68446 1.000 17.53350 ? 43   PRO A CA    1 
ATOM   355  C C     . PRO A 1 43  ? 27.70661 -25.98115 -42.59052 1.000 17.30131 ? 43   PRO A C     1 
ATOM   356  O O     . PRO A 1 43  ? 28.29992 -26.02041 -41.51057 1.000 15.53993 ? 43   PRO A O     1 
ATOM   357  C CB    . PRO A 1 43  ? 25.96108 -24.17914 -42.85667 1.000 19.53631 ? 43   PRO A CB    1 
ATOM   358  C CG    . PRO A 1 43  ? 24.62399 -24.00430 -42.20256 1.000 20.50155 ? 43   PRO A CG    1 
ATOM   359  C CD    . PRO A 1 43  ? 24.78359 -24.81276 -40.94463 1.000 16.68785 ? 43   PRO A CD    1 
ATOM   360  N N     . ALA A 1 44  ? 28.31121 -26.19392 -43.75815 1.000 18.11862 ? 44   ALA A N     1 
ATOM   361  C CA    . ALA A 1 44  ? 29.71526 -26.57061 -43.83428 1.000 20.81572 ? 44   ALA A CA    1 
ATOM   362  C C     . ALA A 1 44  ? 30.66438 -25.39507 -43.64375 1.000 21.53595 ? 44   ALA A C     1 
ATOM   363  O O     . ALA A 1 44  ? 31.86126 -25.61883 -43.43237 1.000 19.89379 ? 44   ALA A O     1 
ATOM   364  C CB    . ALA A 1 44  ? 30.00251 -27.24934 -45.17573 1.000 23.55683 ? 44   ALA A CB    1 
ATOM   365  N N     . ALA A 1 45  ? 30.17108 -24.15978 -43.70743 1.000 19.12983 ? 45   ALA A N     1 
ATOM   366  C CA    . ALA A 1 45  ? 31.01649 -22.98603 -43.55134 1.000 18.00992 ? 45   ALA A CA    1 
ATOM   367  C C     . ALA A 1 45  ? 30.27709 -21.92342 -42.75169 1.000 16.53937 ? 45   ALA A C     1 
ATOM   368  O O     . ALA A 1 45  ? 29.04504 -21.90572 -42.68884 1.000 15.82309 ? 45   ALA A O     1 
ATOM   369  C CB    . ALA A 1 45  ? 31.45104 -22.41658 -44.90831 1.000 19.75991 ? 45   ALA A CB    1 
ATOM   370  N N     . ALA A 1 46  ? 31.05343 -21.03278 -42.13794 1.000 16.18058 ? 46   ALA A N     1 
ATOM   371  C CA    . ALA A 1 46  ? 30.47706 -19.94536 -41.36653 1.000 15.73757 ? 46   ALA A CA    1 
ATOM   372  C C     . ALA A 1 46  ? 29.69272 -19.00771 -42.28275 1.000 17.04090 ? 46   ALA A C     1 
ATOM   373  O O     . ALA A 1 46  ? 30.03700 -18.84044 -43.45689 1.000 16.07145 ? 46   ALA A O     1 
ATOM   374  C CB    . ALA A 1 46  ? 31.57024 -19.16803 -40.63582 1.000 15.68025 ? 46   ALA A CB    1 
ATOM   375  N N     . PRO A 1 47  ? 28.62715 -18.39057 -41.77640 1.000 15.53133 ? 47   PRO A N     1 
ATOM   376  C CA    . PRO A 1 47  ? 27.86199 -17.45612 -42.60649 1.000 16.92878 ? 47   PRO A CA    1 
ATOM   377  C C     . PRO A 1 47  ? 28.65489 -16.18696 -42.87363 1.000 18.60740 ? 47   PRO A C     1 
ATOM   378  O O     . PRO A 1 47  ? 29.37960 -15.68988 -42.00849 1.000 16.02508 ? 47   PRO A O     1 
ATOM   379  C CB    . PRO A 1 47  ? 26.62012 -17.17714 -41.75407 1.000 18.79606 ? 47   PRO A CB    1 
ATOM   380  C CG    . PRO A 1 47  ? 27.14832 -17.31106 -40.35385 1.000 16.43015 ? 47   PRO A CG    1 
ATOM   381  C CD    . PRO A 1 47  ? 28.01720 -18.53922 -40.44369 1.000 17.26123 ? 47   PRO A CD    1 
ATOM   382  N N     . GLN A 1 48  ? 28.51644 -15.66676 -44.09331 1.000 18.43563 ? 48   GLN A N     1 
ATOM   383  C CA    . GLN A 1 48  ? 29.20456 -14.42960 -44.44250 1.000 18.42115 ? 48   GLN A CA    1 
ATOM   384  C C     . GLN A 1 48  ? 28.49134 -13.21821 -43.85036 1.000 21.01151 ? 48   GLN A C     1 
ATOM   385  O O     . GLN A 1 48  ? 29.14266 -12.28155 -43.37398 1.000 18.78691 ? 48   GLN A O     1 
ATOM   386  C CB    . GLN A 1 48  ? 29.32114 -14.30761 -45.96269 1.000 20.13246 ? 48   GLN A CB    1 
ATOM   387  C CG    . GLN A 1 48  ? 30.32549 -15.28127 -46.57213 1.000 20.36355 ? 48   GLN A CG    1 
ATOM   388  C CD    . GLN A 1 48  ? 31.76502 -14.84786 -46.38048 1.000 22.31013 ? 48   GLN A CD    1 
ATOM   389  O OE1   . GLN A 1 48  ? 32.09633 -13.67035 -46.51761 1.000 23.96248 ? 48   GLN A OE1   1 
ATOM   390  N NE2   . GLN A 1 48  ? 32.62932 -15.80149 -46.05233 1.000 19.67206 ? 48   GLN A NE2   1 
ATOM   391  N N     . GLU A 1 49  ? 27.12992 -13.22287 -43.86810 1.000 21.18799 ? 49   GLU A N     1 
ATOM   392  C CA    . GLU A 1 49  ? 26.22039 -12.27757 -43.23895 1.000 22.58886 ? 49   GLU A CA    1 
ATOM   393  C C     . GLU A 1 49  ? 25.75806 -12.81456 -41.88675 1.000 19.06278 ? 49   GLU A C     1 
ATOM   394  O O     . GLU A 1 49  ? 25.69377 -14.03134 -41.68425 1.000 20.08701 ? 49   GLU A O     1 
ATOM   395  C CB    . GLU A 1 49  ? 25.00039 -12.02124 -44.13323 1.000 23.10632 ? 49   GLU A CB    1 
ATOM   396  C CG    . GLU A 1 49  ? 25.31620 -11.46690 -45.53081 1.000 31.28478 ? 49   GLU A CG    1 
ATOM   397  C CD    . GLU A 1 49  ? 26.01427 -10.10973 -45.51577 1.000 36.41374 ? 49   GLU A CD    1 
ATOM   398  O OE1   . GLU A 1 49  ? 25.94010 -9.41105  -44.48392 1.000 38.82277 ? 49   GLU A OE1   1 
ATOM   399  O OE2   . GLU A 1 49  ? 26.63685 -9.73451  -46.53579 1.000 44.31209 ? 49   GLU A OE2   1 
ATOM   400  N N     . PRO A 1 50  ? 25.43892 -11.93642 -40.93777 1.000 18.48502 ? 50   PRO A N     1 
ATOM   401  C CA    . PRO A 1 50  ? 25.01461 -12.40381 -39.61433 1.000 20.51922 ? 50   PRO A CA    1 
ATOM   402  C C     . PRO A 1 50  ? 23.69299 -13.15755 -39.64947 1.000 21.87481 ? 50   PRO A C     1 
ATOM   403  O O     . PRO A 1 50  ? 22.78810 -12.85337 -40.43156 1.000 20.25055 ? 50   PRO A O     1 
ATOM   404  C CB    . PRO A 1 50  ? 24.89222 -11.10281 -38.80761 1.000 22.15221 ? 50   PRO A CB    1 
ATOM   405  C CG    . PRO A 1 50  ? 25.78158 -10.13430 -39.53796 1.000 22.36451 ? 50   PRO A CG    1 
ATOM   406  C CD    . PRO A 1 50  ? 25.53705 -10.46886 -40.97613 1.000 23.93444 ? 50   PRO A CD    1 
ATOM   407  N N     . ASP A 1 51  ? 23.60616 -14.17197 -38.79542 1.000 20.52363 ? 51   ASP A N     1 
ATOM   408  C CA    . ASP A 1 51  ? 22.35719 -14.85622 -38.50410 1.000 18.73679 ? 51   ASP A CA    1 
ATOM   409  C C     . ASP A 1 51  ? 21.62126 -14.11487 -37.39088 1.000 21.24941 ? 51   ASP A C     1 
ATOM   410  O O     . ASP A 1 51  ? 22.20075 -13.30316 -36.66584 1.000 22.72667 ? 51   ASP A O     1 
ATOM   411  C CB    . ASP A 1 51  ? 22.61643 -16.30919 -38.09064 1.000 20.15370 ? 51   ASP A CB    1 
ATOM   412  C CG    . ASP A 1 51  ? 22.94611 -17.21159 -39.27120 1.000 22.09189 ? 51   ASP A CG    1 
ATOM   413  O OD1   . ASP A 1 51  ? 22.62037 -16.84185 -40.41816 1.000 23.22068 ? 51   ASP A OD1   1 
ATOM   414  O OD2   . ASP A 1 51  ? 23.53072 -18.29580 -39.05007 1.000 20.91598 ? 51   ASP A OD2   1 
ATOM   415  N N     . THR A 1 52  ? 20.32988 -14.39881 -37.26012 1.000 21.02095 ? 52   THR A N     1 
ATOM   416  C CA    . THR A 1 52  ? 19.52965 -13.77424 -36.21633 1.000 21.34921 ? 52   THR A CA    1 
ATOM   417  C C     . THR A 1 52  ? 19.63624 -14.56054 -34.91423 1.000 19.76849 ? 52   THR A C     1 
ATOM   418  O O     . THR A 1 52  ? 19.87233 -15.77232 -34.91136 1.000 18.58029 ? 52   THR A O     1 
ATOM   419  C CB    . THR A 1 52  ? 18.05857 -13.66834 -36.62964 1.000 22.73284 ? 52   THR A CB    1 
ATOM   420  O OG1   . THR A 1 52  ? 17.48877 -14.97777 -36.72364 1.000 23.75489 ? 52   THR A OG1   1 
ATOM   421  C CG2   . THR A 1 52  ? 17.92392 -12.96516 -37.97461 1.000 26.07137 ? 52   THR A CG2   1 
ATOM   422  N N     . PHE A 1 53  ? 19.46094 -13.84858 -33.79854 1.000 19.08823 ? 53   PHE A N     1 
ATOM   423  C CA    . PHE A 1 53  ? 19.44230 -14.50376 -32.49477 1.000 19.23467 ? 53   PHE A CA    1 
ATOM   424  C C     . PHE A 1 53  ? 18.31068 -15.52127 -32.41485 1.000 19.54425 ? 53   PHE A C     1 
ATOM   425  O O     . PHE A 1 53  ? 18.45255 -16.57493 -31.78205 1.000 19.28354 ? 53   PHE A O     1 
ATOM   426  C CB    . PHE A 1 53  ? 19.30961 -13.44908 -31.39460 1.000 20.91273 ? 53   PHE A CB    1 
ATOM   427  C CG    . PHE A 1 53  ? 19.31416 -14.00812 -30.00072 1.000 19.34824 ? 53   PHE A CG    1 
ATOM   428  C CD1   . PHE A 1 53  ? 20.48116 -14.50016 -29.43657 1.000 20.71505 ? 53   PHE A CD1   1 
ATOM   429  C CD2   . PHE A 1 53  ? 18.15250 -14.02529 -29.24774 1.000 22.79130 ? 53   PHE A CD2   1 
ATOM   430  C CE1   . PHE A 1 53  ? 20.48645 -15.00611 -28.14704 1.000 20.25553 ? 53   PHE A CE1   1 
ATOM   431  C CE2   . PHE A 1 53  ? 18.14950 -14.52877 -27.96093 1.000 22.40155 ? 53   PHE A CE2   1 
ATOM   432  C CZ    . PHE A 1 53  ? 19.31804 -15.01918 -27.40825 1.000 22.41599 ? 53   PHE A CZ    1 
ATOM   433  N N     . GLU A 1 54  ? 17.18129 -15.22420 -33.06387 1.000 18.79814 ? 54   GLU A N     1 
ATOM   434  C CA    . GLU A 1 54  ? 16.06092 -16.15960 -33.08809 1.000 18.99875 ? 54   GLU A CA    1 
ATOM   435  C C     . GLU A 1 54  ? 16.44021 -17.44752 -33.80578 1.000 18.76863 ? 54   GLU A C     1 
ATOM   436  O O     . GLU A 1 54  ? 16.08562 -18.54658 -33.36190 1.000 18.14018 ? 54   GLU A O     1 
ATOM   437  C CB    . GLU A 1 54  ? 14.85742 -15.50755 -33.76851 1.000 21.17910 ? 54   GLU A CB    1 
ATOM   438  C CG    . GLU A 1 54  ? 14.14997 -14.45268 -32.93081 1.000 23.90116 ? 54   GLU A CG    1 
ATOM   439  C CD    . GLU A 1 54  ? 14.76665 -13.07300 -33.07943 1.000 25.62961 ? 54   GLU A CD    1 
ATOM   440  O OE1   . GLU A 1 54  ? 15.67588 -12.91057 -33.92177 1.000 27.76957 ? 54   GLU A OE1   1 
ATOM   441  O OE2   . GLU A 1 54  ? 14.33626 -12.14920 -32.35572 1.000 29.80186 ? 54   GLU A OE2   1 
ATOM   442  N N     . ASP A 1 55  ? 17.16174 -17.32608 -34.92135 1.000 18.75349 ? 55   ASP A N     1 
ATOM   443  C CA    . ASP A 1 55  ? 17.62555 -18.50168 -35.64844 1.000 19.40870 ? 55   ASP A CA    1 
ATOM   444  C C     . ASP A 1 55  ? 18.56098 -19.34505 -34.78967 1.000 17.94913 ? 55   ASP A C     1 
ATOM   445  O O     . ASP A 1 55  ? 18.48907 -20.57894 -34.80484 1.000 18.35083 ? 55   ASP A O     1 
ATOM   446  C CB    . ASP A 1 55  ? 18.32099 -18.06017 -36.93674 1.000 22.88912 ? 55   ASP A CB    1 
ATOM   447  C CG    . ASP A 1 55  ? 18.68651 -19.22121 -37.83545 1.000 24.82729 ? 55   ASP A CG    1 
ATOM   448  O OD1   . ASP A 1 55  ? 18.10957 -20.31333 -37.66414 1.000 32.62161 ? 55   ASP A OD1   1 
ATOM   449  O OD2   . ASP A 1 55  ? 19.55414 -19.03974 -38.71486 1.000 32.01387 ? 55   ASP A OD2   1 
ATOM   450  N N     . ILE A 1 56  ? 19.43336 -18.69507 -34.01884 1.000 16.38855 ? 56   ILE A N     1 
ATOM   451  C CA    . ILE A 1 56  ? 20.42623 -19.42342 -33.23398 1.000 15.20830 ? 56   ILE A CA    1 
ATOM   452  C C     . ILE A 1 56  ? 19.76628 -20.16055 -32.07500 1.000 14.79963 ? 56   ILE A C     1 
ATOM   453  O O     . ILE A 1 56  ? 20.03412 -21.34429 -31.84175 1.000 13.83887 ? 56   ILE A O     1 
ATOM   454  C CB    . ILE A 1 56  ? 21.52568 -18.46401 -32.74711 1.000 13.88714 ? 56   ILE A CB    1 
ATOM   455  C CG1   . ILE A 1 56  ? 22.31311 -17.93434 -33.94295 1.000 17.40044 ? 56   ILE A CG1   1 
ATOM   456  C CG2   . ILE A 1 56  ? 22.44117 -19.15121 -31.74939 1.000 14.42807 ? 56   ILE A CG2   1 
ATOM   457  C CD1   . ILE A 1 56  ? 23.03726 -16.66326 -33.66264 1.000 17.07002 ? 56   ILE A CD1   1 
ATOM   458  N N     . ILE A 1 57  ? 18.89650 -19.47437 -31.32916 1.000 14.95224 ? 57   ILE A N     1 
ATOM   459  C CA    . ILE A 1 57  ? 18.23551 -20.11119 -30.19310 1.000 16.28261 ? 57   ILE A CA    1 
ATOM   460  C C     . ILE A 1 57  ? 17.33196 -21.23871 -30.66434 1.000 15.56019 ? 57   ILE A C     1 
ATOM   461  O O     . ILE A 1 57  ? 17.20658 -22.27104 -29.99278 1.000 16.39046 ? 57   ILE A O     1 
ATOM   462  C CB    . ILE A 1 57  ? 17.45972 -19.06568 -29.37043 1.000 20.60582 ? 57   ILE A CB    1 
ATOM   463  C CG1   . ILE A 1 57  ? 18.44120 -18.12241 -28.68522 1.000 24.13088 ? 57   ILE A CG1   1 
ATOM   464  C CG2   . ILE A 1 57  ? 16.57631 -19.73860 -28.32688 1.000 21.80511 ? 57   ILE A CG2   1 
ATOM   465  C CD1   . ILE A 1 57  ? 19.20731 -18.77725 -27.56802 1.000 24.92101 ? 57   ILE A CD1   1 
ATOM   466  N N     . ASN A 1 58  ? 16.69745 -21.06978 -31.82454 1.000 15.51671 ? 58   ASN A N     1 
ATOM   467  C CA    . ASN A 1 58  ? 15.93574 -22.16596 -32.40750 1.000 16.88400 ? 58   ASN A CA    1 
ATOM   468  C C     . ASN A 1 58  ? 16.83323 -23.36748 -32.67721 1.000 16.25500 ? 58   ASN A C     1 
ATOM   469  O O     . ASN A 1 58  ? 16.45206 -24.51186 -32.40720 1.000 16.16673 ? 58   ASN A O     1 
ATOM   470  C CB    . ASN A 1 58  ? 15.25748 -21.69914 -33.69248 1.000 19.16676 ? 58   ASN A CB    1 
ATOM   471  C CG    . ASN A 1 58  ? 14.30298 -22.72667 -34.24507 1.000 24.03180 ? 58   ASN A CG    1 
ATOM   472  O OD1   . ASN A 1 58  ? 13.36860 -23.15168 -33.56540 1.000 28.37961 ? 58   ASN A OD1   1 
ATOM   473  N ND2   . ASN A 1 58  ? 14.54402 -23.15135 -35.47680 1.000 25.79281 ? 58   ASN A ND2   1 
ATOM   474  N N     . ASP A 1 59  ? 18.03783 -23.12376 -33.19901 1.000 13.70090 ? 59   ASP A N     1 
ATOM   475  C CA    . ASP A 1 59  ? 18.98570 -24.21102 -33.42228 1.000 14.66375 ? 59   ASP A CA    1 
ATOM   476  C C     . ASP A 1 59  ? 19.42937 -24.85493 -32.11512 1.000 15.43789 ? 59   ASP A C     1 
ATOM   477  O O     . ASP A 1 59  ? 19.65125 -26.06969 -32.07304 1.000 14.92947 ? 59   ASP A O     1 
ATOM   478  C CB    . ASP A 1 59  ? 20.19688 -23.70443 -34.20030 1.000 15.57226 ? 59   ASP A CB    1 
ATOM   479  C CG    . ASP A 1 59  ? 19.91430 -23.55527 -35.68006 1.000 20.31535 ? 59   ASP A CG    1 
ATOM   480  O OD1   . ASP A 1 59  ? 18.85529 -24.04091 -36.13251 1.000 18.59123 ? 59   ASP A OD1   1 
ATOM   481  O OD2   . ASP A 1 59  ? 20.74407 -22.94908 -36.38811 1.000 18.18823 ? 59   ASP A OD2   1 
ATOM   482  N N     . VAL A 1 60  ? 19.57053 -24.07008 -31.04328 1.000 14.80644 ? 60   VAL A N     1 
ATOM   483  C CA    . VAL A 1 60  ? 19.92994 -24.65171 -29.75175 1.000 14.91960 ? 60   VAL A CA    1 
ATOM   484  C C     . VAL A 1 60  ? 18.90326 -25.69658 -29.33905 1.000 15.68041 ? 60   VAL A C     1 
ATOM   485  O O     . VAL A 1 60  ? 19.25451 -26.78846 -28.87593 1.000 15.15128 ? 60   VAL A O     1 
ATOM   486  C CB    . VAL A 1 60  ? 20.07892 -23.54887 -28.68713 1.000 15.46958 ? 60   VAL A CB    1 
ATOM   487  C CG1   . VAL A 1 60  ? 20.22312 -24.16416 -27.30444 1.000 15.07955 ? 60   VAL A CG1   1 
ATOM   488  C CG2   . VAL A 1 60  ? 21.27732 -22.67185 -29.00294 1.000 15.53089 ? 60   VAL A CG2   1 
ATOM   489  N N     . GLU A 1 61  ? 17.62058 -25.38861 -29.52583 1.000 14.91450 ? 61   GLU A N     1 
ATOM   490  C CA    . GLU A 1 61  ? 16.57017 -26.31780 -29.13079 1.000 17.48223 ? 61   GLU A CA    1 
ATOM   491  C C     . GLU A 1 61  ? 16.49192 -27.50652 -30.08079 1.000 18.30017 ? 61   GLU A C     1 
ATOM   492  O O     . GLU A 1 61  ? 16.25394 -28.63996 -29.64758 1.000 17.67933 ? 61   GLU A O     1 
ATOM   493  C CB    . GLU A 1 61  ? 15.22706 -25.59021 -29.08188 1.000 18.62248 ? 61   GLU A CB    1 
ATOM   494  C CG    . GLU A 1 61  ? 14.89330 -24.97111 -27.73737 1.000 27.07314 ? 61   GLU A CG    1 
ATOM   495  C CD    . GLU A 1 61  ? 14.69474 -26.00745 -26.65213 1.000 27.79564 ? 61   GLU A CD    1 
ATOM   496  O OE1   . GLU A 1 61  ? 13.84704 -26.90726 -26.83120 1.000 33.88235 ? 61   GLU A OE1   1 
ATOM   497  O OE2   . GLU A 1 61  ? 15.38629 -25.91949 -25.61658 1.000 30.30061 ? 61   GLU A OE2   1 
ATOM   498  N N     . LYS A 1 62  ? 16.69693 -27.27119 -31.37648 1.000 17.20435 ? 62   LYS A N     1 
ATOM   499  C CA    . LYS A 1 62  ? 16.40437 -28.28490 -32.38141 1.000 15.67024 ? 62   LYS A CA    1 
ATOM   500  C C     . LYS A 1 62  ? 17.57238 -29.22320 -32.66598 1.000 18.73384 ? 62   LYS A C     1 
ATOM   501  O O     . LYS A 1 62  ? 17.34530 -30.41170 -32.92687 1.000 18.72027 ? 62   LYS A O     1 
ATOM   502  C CB    . LYS A 1 62  ? 15.95047 -27.61753 -33.68067 1.000 19.25682 ? 62   LYS A CB    1 
ATOM   503  C CG    . LYS A 1 62  ? 14.63241 -26.85906 -33.55417 1.000 23.11385 ? 62   LYS A CG    1 
ATOM   504  C CD    . LYS A 1 62  ? 13.59540 -27.39014 -34.52513 1.000 28.16973 ? 62   LYS A CD    1 
ATOM   505  C CE    . LYS A 1 62  ? 12.21083 -27.32573 -33.90899 1.000 32.04714 ? 62   LYS A CE    1 
ATOM   506  N NZ    . LYS A 1 62  ? 11.51585 -28.64095 -33.97178 1.000 31.57580 ? 62   LYS A NZ    1 
ATOM   507  N N     . ILE A 1 63  ? 18.81102 -28.73767 -32.63401 1.000 15.37144 ? 63   ILE A N     1 
ATOM   508  C CA    . ILE A 1 63  ? 19.94859 -29.58906 -32.97038 1.000 15.13819 ? 63   ILE A CA    1 
ATOM   509  C C     . ILE A 1 63  ? 20.97265 -29.71363 -31.85057 1.000 16.59837 ? 63   ILE A C     1 
ATOM   510  O O     . ILE A 1 63  ? 21.73039 -30.70034 -31.83126 1.000 15.19549 ? 63   ILE A O     1 
ATOM   511  C CB    . ILE A 1 63  ? 20.63099 -29.10217 -34.27076 1.000 22.12661 ? 63   ILE A CB    1 
ATOM   512  C CG1   . ILE A 1 63  ? 21.11941 -27.66971 -34.13560 1.000 21.74181 ? 63   ILE A CG1   1 
ATOM   513  C CG2   . ILE A 1 63  ? 19.65864 -29.18893 -35.45222 1.000 21.27885 ? 63   ILE A CG2   1 
ATOM   514  C CD1   . ILE A 1 63  ? 21.98467 -27.19556 -35.28522 1.000 27.17089 ? 63   ILE A CD1   1 
ATOM   515  N N     . ILE A 1 64  ? 21.05844 -28.78097 -30.89837 1.000 13.98248 ? 64   ILE A N     1 
ATOM   516  C CA    . ILE A 1 64  ? 22.02461 -28.92280 -29.81225 1.000 13.08767 ? 64   ILE A CA    1 
ATOM   517  C C     . ILE A 1 64  ? 21.44667 -29.75699 -28.67856 1.000 14.23594 ? 64   ILE A C     1 
ATOM   518  O O     . ILE A 1 64  ? 22.05471 -30.74110 -28.24176 1.000 13.90554 ? 64   ILE A O     1 
ATOM   519  C CB    . ILE A 1 64  ? 22.49689 -27.54716 -29.30626 1.000 14.09520 ? 64   ILE A CB    1 
ATOM   520  C CG1   . ILE A 1 64  ? 23.11636 -26.73564 -30.44192 1.000 13.73553 ? 64   ILE A CG1   1 
ATOM   521  C CG2   . ILE A 1 64  ? 23.48847 -27.70967 -28.13781 1.000 14.39330 ? 64   ILE A CG2   1 
ATOM   522  C CD1   . ILE A 1 64  ? 24.31102 -27.41368 -31.08407 1.000 16.23722 ? 64   ILE A CD1   1 
ATOM   523  N N     . MET A 1 65  ? 20.27621 -29.36672 -28.17778 1.000 12.80981 ? 65   MET A N     1 
ATOM   524  C CA    . MET A 1 65  ? 19.64958 -30.07599 -27.06403 1.000 14.81534 ? 65   MET A CA    1 
ATOM   525  C C     . MET A 1 65  ? 19.47531 -31.57546 -27.29331 1.000 17.44744 ? 65   MET A C     1 
ATOM   526  O O     . MET A 1 65  ? 19.68047 -32.33846 -26.33353 1.000 13.78632 ? 65   MET A O     1 
ATOM   527  C CB    . MET A 1 65  ? 18.30004 -29.41602 -26.74473 1.000 17.90979 ? 65   MET A CB    1 
ATOM   528  C CG    . MET A 1 65  ? 18.40747 -28.13335 -25.93580 1.000 16.96146 ? 65   MET A CG    1 
ATOM   529  S SD    . MET A 1 65  ? 19.25722 -28.36512 -24.36170 1.000 17.96050 ? 65   MET A SD    1 
ATOM   530  C CE    . MET A 1 65  ? 19.53399 -26.66670 -23.87194 1.000 22.01900 ? 65   MET A CE    1 
ATOM   531  N N     . PRO A 1 66  ? 19.10388 -32.06725 -28.48330 1.000 14.32751 ? 66   PRO A N     1 
ATOM   532  C CA    . PRO A 1 66  ? 19.02939 -33.52597 -28.66809 1.000 16.28069 ? 66   PRO A CA    1 
ATOM   533  C C     . PRO A 1 66  ? 20.33410 -34.25322 -28.40429 1.000 17.13615 ? 66   PRO A C     1 
ATOM   534  O O     . PRO A 1 66  ? 20.30615 -35.46090 -28.14771 1.000 18.77785 ? 66   PRO A O     1 
ATOM   535  C CB    . PRO A 1 66  ? 18.60098 -33.65777 -30.13384 1.000 17.08202 ? 66   PRO A CB    1 
ATOM   536  C CG    . PRO A 1 66  ? 17.72216 -32.47049 -30.30618 1.000 16.81584 ? 66   PRO A CG    1 
ATOM   537  C CD    . PRO A 1 66  ? 18.54542 -31.38093 -29.66458 1.000 16.60690 ? 66   PRO A CD    1 
ATOM   538  N N     . GLY A 1 67  ? 21.47228 -33.56912 -28.45322 1.000 14.88417 ? 67   GLY A N     1 
ATOM   539  C CA    . GLY A 1 67  ? 22.75063 -34.21735 -28.23985 1.000 15.76826 ? 67   GLY A CA    1 
ATOM   540  C C     . GLY A 1 67  ? 23.38560 -33.83121 -26.92218 1.000 14.76707 ? 67   GLY A C     1 
ATOM   541  O O     . GLY A 1 67  ? 24.59432 -33.99467 -26.73081 1.000 15.72723 ? 67   GLY A O     1 
ATOM   542  N N     . VAL A 1 68  ? 22.57488 -33.32422 -26.00071 1.000 13.99692 ? 68   VAL A N     1 
ATOM   543  C CA    . VAL A 1 68  ? 23.03880 -32.89387 -24.68620 1.000 15.45524 ? 68   VAL A CA    1 
ATOM   544  C C     . VAL A 1 68  ? 22.76199 -33.99851 -23.67744 1.000 15.32599 ? 68   VAL A C     1 
ATOM   545  O O     . VAL A 1 68  ? 21.64916 -34.53871 -23.62331 1.000 17.14299 ? 68   VAL A O     1 
ATOM   546  C CB    . VAL A 1 68  ? 22.36322 -31.57871 -24.25587 1.000 16.09372 ? 68   VAL A CB    1 
ATOM   547  C CG1   . VAL A 1 68  ? 22.57177 -31.34131 -22.76977 1.000 14.88095 ? 68   VAL A CG1   1 
ATOM   548  C CG2   . VAL A 1 68  ? 22.90711 -30.41474 -25.06032 1.000 16.37651 ? 68   VAL A CG2   1 
ATOM   549  N N     . THR A 1 69  ? 23.77896 -34.35009 -22.89689 1.000 14.84790 ? 69   THR A N     1 
ATOM   550  C CA    . THR A 1 69  ? 23.59817 -35.14645 -21.69310 1.000 16.27223 ? 69   THR A CA    1 
ATOM   551  C C     . THR A 1 69  ? 23.34466 -34.18156 -20.54238 1.000 18.47179 ? 69   THR A C     1 
ATOM   552  O O     . THR A 1 69  ? 24.20734 -33.35882 -20.22061 1.000 16.72825 ? 69   THR A O     1 
ATOM   553  C CB    . THR A 1 69  ? 24.83022 -36.00350 -21.41587 1.000 16.81959 ? 69   THR A CB    1 
ATOM   554  O OG1   . THR A 1 69  ? 25.00577 -36.94935 -22.47815 1.000 17.07363 ? 69   THR A OG1   1 
ATOM   555  C CG2   . THR A 1 69  ? 24.66613 -36.75148 -20.10348 1.000 19.27918 ? 69   THR A CG2   1 
ATOM   556  N N     . HIS A 1 70  ? 22.16320 -34.26562 -19.93607 1.000 15.18836 ? 70   HIS A N     1 
ATOM   557  C CA    . HIS A 1 70  ? 21.73175 -33.26238 -18.96262 1.000 15.54902 ? 70   HIS A CA    1 
ATOM   558  C C     . HIS A 1 70  ? 22.27927 -33.62404 -17.58835 1.000 16.03882 ? 70   HIS A C     1 
ATOM   559  O O     . HIS A 1 70  ? 21.64371 -34.32843 -16.79947 1.000 15.89202 ? 70   HIS A O     1 
ATOM   560  C CB    . HIS A 1 70  ? 20.21677 -33.13272 -18.97549 1.000 15.08547 ? 70   HIS A CB    1 
ATOM   561  C CG    . HIS A 1 70  ? 19.66544 -32.83103 -20.33260 1.000 15.92301 ? 70   HIS A CG    1 
ATOM   562  N ND1   . HIS A 1 70  ? 19.48251 -31.54323 -20.78828 1.000 17.70109 ? 70   HIS A ND1   1 
ATOM   563  C CD2   . HIS A 1 70  ? 19.27073 -33.64641 -21.33899 1.000 17.50283 ? 70   HIS A CD2   1 
ATOM   564  C CE1   . HIS A 1 70  ? 18.99511 -31.57832 -22.01551 1.000 18.72791 ? 70   HIS A CE1   1 
ATOM   565  N NE2   . HIS A 1 70  ? 18.85468 -32.84238 -22.37253 1.000 15.62230 ? 70   HIS A NE2   1 
ATOM   566  N N     . TRP A 1 71  ? 23.47917 -33.10587 -17.30196 1.000 14.45202 ? 71   TRP A N     1 
ATOM   567  C CA    . TRP A 1 71  ? 24.15681 -33.34716 -16.03270 1.000 14.86831 ? 71   TRP A CA    1 
ATOM   568  C C     . TRP A 1 71  ? 23.34634 -32.86146 -14.84084 1.000 14.53201 ? 71   TRP A C     1 
ATOM   569  O O     . TRP A 1 71  ? 23.56679 -33.33485 -13.71882 1.000 15.45772 ? 71   TRP A O     1 
ATOM   570  C CB    . TRP A 1 71  ? 25.52659 -32.65866 -16.04350 1.000 16.23402 ? 71   TRP A CB    1 
ATOM   571  C CG    . TRP A 1 71  ? 26.58795 -33.40649 -16.78412 1.000 18.36087 ? 71   TRP A CG    1 
ATOM   572  C CD1   . TRP A 1 71  ? 26.67990 -33.58266 -18.13295 1.000 19.79602 ? 71   TRP A CD1   1 
ATOM   573  C CD2   . TRP A 1 71  ? 27.72563 -34.06036 -16.21374 1.000 19.25370 ? 71   TRP A CD2   1 
ATOM   574  N NE1   . TRP A 1 71  ? 27.80000 -34.31925 -18.43743 1.000 18.58335 ? 71   TRP A NE1   1 
ATOM   575  C CE2   . TRP A 1 71  ? 28.46061 -34.62287 -17.27533 1.000 20.44764 ? 71   TRP A CE2   1 
ATOM   576  C CE3   . TRP A 1 71  ? 28.19152 -34.22786 -14.90539 1.000 17.48771 ? 71   TRP A CE3   1 
ATOM   577  C CZ2   . TRP A 1 71  ? 29.63722 -35.34322 -17.06869 1.000 20.76982 ? 71   TRP A CZ2   1 
ATOM   578  C CZ3   . TRP A 1 71  ? 29.35804 -34.94163 -14.70051 1.000 19.42123 ? 71   TRP A CZ3   1 
ATOM   579  C CH2   . TRP A 1 71  ? 30.06813 -35.49142 -15.77651 1.000 20.19594 ? 71   TRP A CH2   1 
ATOM   580  N N     . HIS A 1 72  ? 22.41057 -31.93800 -15.05517 1.000 13.32468 ? 72   HIS A N     1 
ATOM   581  C CA    . HIS A 1 72  ? 21.67572 -31.31945 -13.96315 1.000 13.10138 ? 72   HIS A CA    1 
ATOM   582  C C     . HIS A 1 72  ? 20.24111 -31.80162 -13.87207 1.000 14.80137 ? 72   HIS A C     1 
ATOM   583  O O     . HIS A 1 72  ? 19.48013 -31.30265 -13.03493 1.000 13.72871 ? 72   HIS A O     1 
ATOM   584  C CB    . HIS A 1 72  ? 21.74625 -29.79437 -14.11111 1.000 15.54379 ? 72   HIS A CB    1 
ATOM   585  C CG    . HIS A 1 72  ? 23.14670 -29.29688 -14.28789 1.000 17.96064 ? 72   HIS A CG    1 
ATOM   586  N ND1   . HIS A 1 72  ? 24.12017 -29.46412 -13.32716 1.000 18.14655 ? 72   HIS A ND1   1 
ATOM   587  C CD2   . HIS A 1 72  ? 23.74123 -28.65038 -15.31658 1.000 19.46696 ? 72   HIS A CD2   1 
ATOM   588  C CE1   . HIS A 1 72  ? 25.25425 -28.94175 -13.75703 1.000 19.06190 ? 72   HIS A CE1   1 
ATOM   589  N NE2   . HIS A 1 72  ? 25.04911 -28.43417 -14.95812 1.000 24.81899 ? 72   HIS A NE2   1 
ATOM   590  N N     . SER A 1 73  ? 19.86833 -32.76585 -14.69953 1.000 13.48783 ? 73   SER A N     1 
ATOM   591  C CA    . SER A 1 73  ? 18.64046 -33.49685 -14.45359 1.000 13.17291 ? 73   SER A CA    1 
ATOM   592  C C     . SER A 1 73  ? 18.75996 -34.28384 -13.15033 1.000 13.52654 ? 73   SER A C     1 
ATOM   593  O O     . SER A 1 73  ? 19.80794 -34.85034 -12.85147 1.000 12.19580 ? 73   SER A O     1 
ATOM   594  C CB    . SER A 1 73  ? 18.31738 -34.42638 -15.61264 1.000 15.94327 ? 73   SER A CB    1 
ATOM   595  O OG    . SER A 1 73  ? 17.43774 -35.46125 -15.22517 1.000 16.09893 ? 73   SER A OG    1 
ATOM   596  N N     . PRO A 1 74  ? 17.70385 -34.30504 -12.34814 1.000 13.26057 ? 74   PRO A N     1 
ATOM   597  C CA    . PRO A 1 74  ? 17.69014 -35.11680 -11.12287 1.000 14.66073 ? 74   PRO A CA    1 
ATOM   598  C C     . PRO A 1 74  ? 17.88389 -36.60463 -11.37008 1.000 15.58297 ? 74   PRO A C     1 
ATOM   599  O O     . PRO A 1 74  ? 18.21012 -37.33003 -10.41885 1.000 15.86550 ? 74   PRO A O     1 
ATOM   600  C CB    . PRO A 1 74  ? 16.30224 -34.84149 -10.51583 1.000 16.80675 ? 74   PRO A CB    1 
ATOM   601  C CG    . PRO A 1 74  ? 15.72713 -33.75367 -11.34915 1.000 23.32856 ? 74   PRO A CG    1 
ATOM   602  C CD    . PRO A 1 74  ? 16.46207 -33.59826 -12.60598 1.000 17.40600 ? 74   PRO A CD    1 
ATOM   603  N N     . TYR A 1 75  ? 17.72698 -37.07143 -12.60187 1.000 13.36770 ? 75   TYR A N     1 
ATOM   604  C CA    . TYR A 1 75  ? 17.90663 -38.46956 -12.94821 1.000 14.30159 ? 75   TYR A CA    1 
ATOM   605  C C     . TYR A 1 75  ? 19.29856 -38.76307 -13.48628 1.000 15.43954 ? 75   TYR A C     1 
ATOM   606  O O     . TYR A 1 75  ? 19.55008 -39.88344 -13.94553 1.000 14.57735 ? 75   TYR A O     1 
ATOM   607  C CB    . TYR A 1 75  ? 16.84267 -38.90469 -13.95713 1.000 15.74345 ? 75   TYR A CB    1 
ATOM   608  C CG    . TYR A 1 75  ? 15.44236 -38.77662 -13.40111 1.000 17.02477 ? 75   TYR A CG    1 
ATOM   609  C CD1   . TYR A 1 75  ? 15.02067 -39.57562 -12.35055 1.000 16.46108 ? 75   TYR A CD1   1 
ATOM   610  C CD2   . TYR A 1 75  ? 14.55064 -37.84089 -13.91405 1.000 18.50137 ? 75   TYR A CD2   1 
ATOM   611  C CE1   . TYR A 1 75  ? 13.74910 -39.46663 -11.83164 1.000 19.56738 ? 75   TYR A CE1   1 
ATOM   612  C CE2   . TYR A 1 75  ? 13.27623 -37.72160 -13.39912 1.000 20.48401 ? 75   TYR A CE2   1 
ATOM   613  C CZ    . TYR A 1 75  ? 12.88056 -38.53674 -12.35863 1.000 21.30061 ? 75   TYR A CZ    1 
ATOM   614  O OH    . TYR A 1 75  ? 11.61140 -38.42114 -11.84169 1.000 24.56568 ? 75   TYR A OH    1 
ATOM   615  N N     . PHE A 1 76  ? 20.20222 -37.78564 -13.44175 1.000 13.11340 ? 76   PHE A N     1 
ATOM   616  C CA    . PHE A 1 76  ? 21.60846 -37.99593 -13.76558 1.000 13.53731 ? 76   PHE A CA    1 
ATOM   617  C C     . PHE A 1 76  ? 22.30209 -38.47817 -12.49742 1.000 14.26987 ? 76   PHE A C     1 
ATOM   618  O O     . PHE A 1 76  ? 22.45198 -37.71637 -11.53644 1.000 14.68017 ? 76   PHE A O     1 
ATOM   619  C CB    . PHE A 1 76  ? 22.24164 -36.70836 -14.28917 1.000 13.43006 ? 76   PHE A CB    1 
ATOM   620  C CG    . PHE A 1 76  ? 23.66800 -36.86622 -14.73270 1.000 12.32512 ? 76   PHE A CG    1 
ATOM   621  C CD1   . PHE A 1 76  ? 23.96134 -37.20826 -16.04216 1.000 14.15961 ? 76   PHE A CD1   1 
ATOM   622  C CD2   . PHE A 1 76  ? 24.71382 -36.66561 -13.84668 1.000 14.13189 ? 76   PHE A CD2   1 
ATOM   623  C CE1   . PHE A 1 76  ? 25.27568 -37.34964 -16.46387 1.000 16.42195 ? 76   PHE A CE1   1 
ATOM   624  C CE2   . PHE A 1 76  ? 26.03350 -36.80784 -14.25870 1.000 15.05418 ? 76   PHE A CE2   1 
ATOM   625  C CZ    . PHE A 1 76  ? 26.31444 -37.15067 -15.56999 1.000 15.32403 ? 76   PHE A CZ    1 
ATOM   626  N N     . PHE A 1 77  ? 22.70019 -39.74875 -12.47912 1.000 13.09946 ? 77   PHE A N     1 
ATOM   627  C CA    . PHE A 1 77  ? 23.37055 -40.33390 -11.32423 1.000 14.90689 ? 77   PHE A CA    1 
ATOM   628  C C     . PHE A 1 77  ? 24.73864 -40.89035 -11.70093 1.000 15.98863 ? 77   PHE A C     1 
ATOM   629  O O     . PHE A 1 77  ? 25.19823 -41.87514 -11.11859 1.000 17.97982 ? 77   PHE A O     1 
ATOM   630  C CB    . PHE A 1 77  ? 22.51509 -41.42666 -10.68522 1.000 15.71239 ? 77   PHE A CB    1 
ATOM   631  C CG    . PHE A 1 77  ? 21.16692 -40.95918 -10.22932 1.000 14.88261 ? 77   PHE A CG    1 
ATOM   632  C CD1   . PHE A 1 77  ? 21.03338 -40.17415 -9.09657  1.000 15.89799 ? 77   PHE A CD1   1 
ATOM   633  C CD2   . PHE A 1 77  ? 20.02735 -41.33285 -10.91891 1.000 16.98193 ? 77   PHE A CD2   1 
ATOM   634  C CE1   . PHE A 1 77  ? 19.78602 -39.75471 -8.67196  1.000 15.08685 ? 77   PHE A CE1   1 
ATOM   635  C CE2   . PHE A 1 77  ? 18.78007 -40.91929 -10.50003 1.000 15.76603 ? 77   PHE A CE2   1 
ATOM   636  C CZ    . PHE A 1 77  ? 18.65885 -40.13049 -9.37396  1.000 16.58760 ? 77   PHE A CZ    1 
ATOM   637  N N     . ALA A 1 78  ? 25.40318 -40.25669 -12.66210 1.000 14.35758 ? 78   ALA A N     1 
ATOM   638  C CA    . ALA A 1 78  ? 26.64577 -40.75171 -13.23320 1.000 17.47958 ? 78   ALA A CA    1 
ATOM   639  C C     . ALA A 1 78  ? 27.84558 -39.95801 -12.72977 1.000 16.68678 ? 78   ALA A C     1 
ATOM   640  O O     . ALA A 1 78  ? 27.72882 -38.80159 -12.31634 1.000 21.42367 ? 78   ALA A O     1 
ATOM   641  C CB    . ALA A 1 78  ? 26.59428 -40.69674 -14.76347 1.000 17.69739 ? 78   ALA A CB    1 
ATOM   642  N N     . TYR A 1 79  ? 29.01208 -40.60633 -12.78806 1.000 21.77567 ? 79   TYR A N     1 
ATOM   643  C CA    . TYR A 1 79  ? 30.29057 -40.01643 -12.39923 1.000 18.59408 ? 79   TYR A CA    1 
ATOM   644  C C     . TYR A 1 79  ? 30.20819 -39.38181 -11.01579 1.000 17.80915 ? 79   TYR A C     1 
ATOM   645  O O     . TYR A 1 79  ? 30.01741 -40.07836 -10.01301 1.000 19.41980 ? 79   TYR A O     1 
ATOM   646  C CB    . TYR A 1 79  ? 30.74429 -38.98449 -13.43962 1.000 17.47105 ? 79   TYR A CB    1 
ATOM   647  C CG    . TYR A 1 79  ? 30.63481 -39.47131 -14.87133 1.000 21.82390 ? 79   TYR A CG    1 
ATOM   648  C CD1   . TYR A 1 79  ? 31.58392 -40.33107 -15.40947 1.000 24.25744 ? 79   TYR A CD1   1 
ATOM   649  C CD2   . TYR A 1 79  ? 29.58897 -39.05772 -15.68887 1.000 22.39496 ? 79   TYR A CD2   1 
ATOM   650  C CE1   . TYR A 1 79  ? 31.48575 -40.78058 -16.71587 1.000 23.62063 ? 79   TYR A CE1   1 
ATOM   651  C CE2   . TYR A 1 79  ? 29.48440 -39.49976 -16.99771 1.000 22.13642 ? 79   TYR A CE2   1 
ATOM   652  C CZ    . TYR A 1 79  ? 30.43519 -40.36011 -17.50502 1.000 24.69791 ? 79   TYR A CZ    1 
ATOM   653  O OH    . TYR A 1 79  ? 30.33273 -40.79990 -18.80582 1.000 23.84928 ? 79   TYR A OH    1 
ATOM   654  N N     . PHE A 1 80  ? 30.35392 -38.06620 -10.95986 1.000 19.44063 ? 80   PHE A N     1 
ATOM   655  C CA    . PHE A 1 80  ? 30.17990 -37.27072 -9.75636  1.000 18.12767 ? 80   PHE A CA    1 
ATOM   656  C C     . PHE A 1 80  ? 29.39807 -36.02572 -10.13620 1.000 16.10523 ? 80   PHE A C     1 
ATOM   657  O O     . PHE A 1 80  ? 29.31658 -35.67801 -11.31939 1.000 19.31228 ? 80   PHE A O     1 
ATOM   658  C CB    . PHE A 1 80  ? 31.52462 -36.87762 -9.12795  1.000 17.05434 ? 80   PHE A CB    1 
ATOM   659  C CG    . PHE A 1 80  ? 32.10881 -37.92648 -8.22633  1.000 17.06400 ? 80   PHE A CG    1 
ATOM   660  C CD1   . PHE A 1 80  ? 31.30144 -38.63867 -7.35344  1.000 15.47395 ? 80   PHE A CD1   1 
ATOM   661  C CD2   . PHE A 1 80  ? 33.46963 -38.18288 -8.23457  1.000 19.89589 ? 80   PHE A CD2   1 
ATOM   662  C CE1   . PHE A 1 80  ? 31.83915 -39.59734 -6.51601  1.000 15.81483 ? 80   PHE A CE1   1 
ATOM   663  C CE2   . PHE A 1 80  ? 34.01432 -39.13901 -7.40115  1.000 17.12604 ? 80   PHE A CE2   1 
ATOM   664  C CZ    . PHE A 1 80  ? 33.19933 -39.84705 -6.53901  1.000 16.11802 ? 80   PHE A CZ    1 
ATOM   665  N N     . PRO A 1 81  ? 28.79691 -35.34259 -9.16148  1.000 14.17470 ? 81   PRO A N     1 
ATOM   666  C CA    . PRO A 1 81  ? 28.10120 -34.09135 -9.47578  1.000 13.66806 ? 81   PRO A CA    1 
ATOM   667  C C     . PRO A 1 81  ? 29.04974 -33.08303 -10.10270 1.000 17.71110 ? 81   PRO A C     1 
ATOM   668  O O     . PRO A 1 81  ? 30.24790 -33.06236 -9.81518  1.000 15.80365 ? 81   PRO A O     1 
ATOM   669  C CB    . PRO A 1 81  ? 27.60173 -33.60324 -8.10673  1.000 15.69241 ? 81   PRO A CB    1 
ATOM   670  C CG    . PRO A 1 81  ? 28.34442 -34.44192 -7.09326  1.000 16.06775 ? 81   PRO A CG    1 
ATOM   671  C CD    . PRO A 1 81  ? 28.54211 -35.75473 -7.77343  1.000 14.86417 ? 81   PRO A CD    1 
ATOM   672  N N     . THR A 1 82  ? 28.50272 -32.26247 -10.99215 1.000 15.08005 ? 82   THR A N     1 
ATOM   673  C CA    . THR A 1 82  ? 29.14657 -31.03371 -11.42498 1.000 13.46586 ? 82   THR A CA    1 
ATOM   674  C C     . THR A 1 82  ? 28.28660 -29.85296 -10.99327 1.000 15.03906 ? 82   THR A C     1 
ATOM   675  O O     . THR A 1 82  ? 27.05934 -29.95542 -10.89786 1.000 15.41814 ? 82   THR A O     1 
ATOM   676  C CB    . THR A 1 82  ? 29.38964 -31.02006 -12.94080 1.000 17.45951 ? 82   THR A CB    1 
ATOM   677  O OG1   . THR A 1 82  ? 30.47420 -30.13161 -13.24206 1.000 21.95353 ? 82   THR A OG1   1 
ATOM   678  C CG2   . THR A 1 82  ? 28.15745 -30.58311 -13.70118 1.000 18.65607 ? 82   THR A CG2   1 
ATOM   679  N N     . ALA A 1 83  ? 28.94725 -28.73974 -10.69870 1.000 11.40075 ? 83   ALA A N     1 
ATOM   680  C CA    . ALA A 1 83  ? 28.29268 -27.62780 -10.02853 1.000 13.31467 ? 83   ALA A CA    1 
ATOM   681  C C     . ALA A 1 83  ? 27.43471 -26.81923 -10.99213 1.000 15.09678 ? 83   ALA A C     1 
ATOM   682  O O     . ALA A 1 83  ? 27.84444 -26.52229 -12.11789 1.000 15.68467 ? 83   ALA A O     1 
ATOM   683  C CB    . ALA A 1 83  ? 29.33461 -26.72018 -9.37677  1.000 13.96844 ? 83   ALA A CB    1 
ATOM   684  N N     . SER A 1 84  ? 26.23742 -26.45696 -10.53361 1.000 14.18703 ? 84   SER A N     1 
ATOM   685  C CA    . SER A 1 84  ? 25.38467 -25.51636 -11.25606 1.000 18.30613 ? 84   SER A CA    1 
ATOM   686  C C     . SER A 1 84  ? 24.55900 -24.75668 -10.23067 1.000 16.32527 ? 84   SER A C     1 
ATOM   687  O O     . SER A 1 84  ? 23.64372 -25.32391 -9.62672  1.000 16.72717 ? 84   SER A O     1 
ATOM   688  C CB    . SER A 1 84  ? 24.48095 -26.22569 -12.25555 1.000 19.96710 ? 84   SER A CB    1 
ATOM   689  O OG    . SER A 1 84  ? 23.50491 -25.33521 -12.77092 1.000 21.45127 ? 84   SER A OG    1 
ATOM   690  N N     . SER A 1 85  ? 24.88361 -23.48336 -10.03444 1.000 13.22340 ? 85   SER A N     1 
ATOM   691  C CA    . SER A 1 85  ? 24.11665 -22.62008 -9.15338  1.000 13.63126 ? 85   SER A CA    1 
ATOM   692  C C     . SER A 1 85  ? 23.96980 -21.25918 -9.81300  1.000 13.56844 ? 85   SER A C     1 
ATOM   693  O O     . SER A 1 85  ? 24.85364 -20.80712 -10.54548 1.000 13.97278 ? 85   SER A O     1 
ATOM   694  C CB    . SER A 1 85  ? 24.77424 -22.48410 -7.77076  1.000 13.76860 ? 85   SER A CB    1 
ATOM   695  O OG    . SER A 1 85  ? 25.88082 -21.59991 -7.81188  1.000 12.83833 ? 85   SER A OG    1 
ATOM   696  N N     . TYR A 1 86  ? 22.83742 -20.61946 -9.56086  1.000 13.85409 ? 86   TYR A N     1 
ATOM   697  C CA    . TYR A 1 86  ? 22.58716 -19.30286 -10.13002 1.000 13.62888 ? 86   TYR A CA    1 
ATOM   698  C C     . TYR A 1 86  ? 23.52873 -18.22751 -9.58739  1.000 12.68703 ? 86   TYR A C     1 
ATOM   699  O O     . TYR A 1 86  ? 23.89065 -17.31816 -10.34487 1.000 12.29906 ? 86   TYR A O     1 
ATOM   700  C CB    . TYR A 1 86  ? 21.12462 -18.90896 -9.91793  1.000 15.67830 ? 86   TYR A CB    1 
ATOM   701  C CG    . TYR A 1 86  ? 20.16975 -19.88031 -10.57344 1.000 18.34384 ? 86   TYR A CG    1 
ATOM   702  C CD1   . TYR A 1 86  ? 20.20042 -20.08643 -11.94813 1.000 16.91283 ? 86   TYR A CD1   1 
ATOM   703  C CD2   . TYR A 1 86  ? 19.24374 -20.59221 -9.82497  1.000 19.08100 ? 86   TYR A CD2   1 
ATOM   704  C CE1   . TYR A 1 86  ? 19.33611 -20.97402 -12.55812 1.000 17.40282 ? 86   TYR A CE1   1 
ATOM   705  C CE2   . TYR A 1 86  ? 18.37457 -21.48235 -10.42598 1.000 18.10834 ? 86   TYR A CE2   1 
ATOM   706  C CZ    . TYR A 1 86  ? 18.42552 -21.66812 -11.79212 1.000 21.46222 ? 86   TYR A CZ    1 
ATOM   707  O OH    . TYR A 1 86  ? 17.56283 -22.55251 -12.39596 1.000 20.46075 ? 86   TYR A OH    1 
ATOM   708  N N     . PRO A 1 87  ? 23.94981 -18.26596 -8.31055  1.000 12.69927 ? 87   PRO A N     1 
ATOM   709  C CA    . PRO A 1 87  ? 24.97923 -17.30153 -7.88437  1.000 13.09870 ? 87   PRO A CA    1 
ATOM   710  C C     . PRO A 1 87  ? 26.23325 -17.36768 -8.73395  1.000 12.25088 ? 87   PRO A C     1 
ATOM   711  O O     . PRO A 1 87  ? 26.79593 -16.32526 -9.09145  1.000 13.08977 ? 87   PRO A O     1 
ATOM   712  C CB    . PRO A 1 87  ? 25.25661 -17.70989 -6.43265  1.000 14.86767 ? 87   PRO A CB    1 
ATOM   713  C CG    . PRO A 1 87  ? 23.97239 -18.24969 -5.96345  1.000 15.94385 ? 87   PRO A CG    1 
ATOM   714  C CD    . PRO A 1 87  ? 23.39788 -18.99241 -7.14821  1.000 14.96365 ? 87   PRO A CD    1 
ATOM   715  N N     . ALA A 1 88  ? 26.68050 -18.57703 -9.08094  1.000 14.07272 ? 88   ALA A N     1 
ATOM   716  C CA    . ALA A 1 88  ? 27.87310 -18.71031 -9.90984  1.000 13.08767 ? 88   ALA A CA    1 
ATOM   717  C C     . ALA A 1 88  ? 27.61387 -18.22687 -11.33099 1.000 12.55453 ? 88   ALA A C     1 
ATOM   718  O O     . ALA A 1 88  ? 28.49512 -17.62424 -11.95444 1.000 12.45637 ? 88   ALA A O     1 
ATOM   719  C CB    . ALA A 1 88  ? 28.35659 -20.15962 -9.90920  1.000 13.41838 ? 88   ALA A CB    1 
ATOM   720  N N     . MET A 1 89  ? 26.41204 -18.47925 -11.86048 1.000 13.57109 ? 89   MET A N     1 
ATOM   721  C CA    . MET A 1 89  ? 26.06785 -17.96005 -13.18161 1.000 13.91834 ? 89   MET A CA    1 
ATOM   722  C C     . MET A 1 89  ? 26.08615 -16.43791 -13.20196 1.000 13.16952 ? 89   MET A C     1 
ATOM   723  O O     . MET A 1 89  ? 26.55807 -15.82890 -14.16950 1.000 14.30782 ? 89   MET A O     1 
ATOM   724  C CB    . MET A 1 89  ? 24.69610 -18.47352 -13.61954 1.000 14.02955 ? 89   MET A CB    1 
ATOM   725  C CG    . MET A 1 89  ? 24.59261 -19.97771 -13.76076 1.000 16.15608 ? 89   MET A CG    1 
ATOM   726  S SD    . MET A 1 89  ? 23.04155 -20.43770 -14.56255 1.000 21.24287 ? 89   MET A SD    1 
ATOM   727  C CE    . MET A 1 89  ? 22.94968 -22.17401 -14.15037 1.000 23.02803 ? 89   MET A CE    1 
ATOM   728  N N     . LEU A 1 90  ? 25.56704 -15.80558 -12.14667 1.000 12.16708 ? 90   LEU A N     1 
ATOM   729  C CA    . LEU A 1 90  ? 25.57297 -14.34796 -12.08498 1.000 12.68673 ? 90   LEU A CA    1 
ATOM   730  C C     . LEU A 1 90  ? 26.99562 -13.80600 -12.04533 1.000 12.07983 ? 90   LEU A C     1 
ATOM   731  O O     . LEU A 1 90  ? 27.31608 -12.83086 -12.73534 1.000 13.10878 ? 90   LEU A O     1 
ATOM   732  C CB    . LEU A 1 90  ? 24.78352 -13.87356 -10.86497 1.000 11.94206 ? 90   LEU A CB    1 
ATOM   733  C CG    . LEU A 1 90  ? 23.27353 -14.11727 -10.89481 1.000 14.41004 ? 90   LEU A CG    1 
ATOM   734  C CD1   . LEU A 1 90  ? 22.68765 -13.99741 -9.49715  1.000 16.30974 ? 90   LEU A CD1   1 
ATOM   735  C CD2   . LEU A 1 90  ? 22.58753 -13.15487 -11.85044 1.000 16.29573 ? 90   LEU A CD2   1 
ATOM   736  N N     . ALA A 1 91  ? 27.86358 -14.42769 -11.24225 1.000 12.81073 ? 91   ALA A N     1 
ATOM   737  C CA    . ALA A 1 91  ? 29.25208 -13.98665 -11.17041 1.000 12.56051 ? 91   ALA A CA    1 
ATOM   738  C C     . ALA A 1 91  ? 29.96452 -14.20802 -12.49754 1.000 14.78154 ? 91   ALA A C     1 
ATOM   739  O O     . ALA A 1 91  ? 30.79931 -13.39378 -12.90779 1.000 14.87201 ? 91   ALA A O     1 
ATOM   740  C CB    . ALA A 1 91  ? 29.97876 -14.72238 -10.04537 1.000 13.51745 ? 91   ALA A CB    1 
ATOM   741  N N     . ASP A 1 92  ? 29.63754 -15.30284 -13.18943 1.000 13.28981 ? 92   ASP A N     1 
ATOM   742  C CA    . ASP A 1 92  ? 30.28480 -15.59167 -14.46134 1.000 15.43171 ? 92   ASP A CA    1 
ATOM   743  C C     . ASP A 1 92  ? 29.90938 -14.56035 -15.51786 1.000 17.86300 ? 92   ASP A C     1 
ATOM   744  O O     . ASP A 1 92  ? 30.72300 -14.24672 -16.39508 1.000 15.95152 ? 92   ASP A O     1 
ATOM   745  C CB    . ASP A 1 92  ? 29.91302 -16.99811 -14.92653 1.000 16.52356 ? 92   ASP A CB    1 
ATOM   746  C CG    . ASP A 1 92  ? 31.12781 -17.82123 -15.31592 1.000 25.90055 ? 92   ASP A CG    1 
ATOM   747  O OD1   . ASP A 1 92  ? 30.96970 -19.04142 -15.53026 1.000 32.15967 ? 92   ASP A OD1   1 
ATOM   748  O OD2   . ASP A 1 92  ? 32.24337 -17.25951 -15.36200 1.000 28.46349 ? 92   ASP A OD2   1 
ATOM   749  N N     . MET A 1 93  ? 28.68881 -14.02212 -15.44811 1.000 14.27414 ? 93   MET A N     1 
ATOM   750  C CA    . MET A 1 93  ? 28.31610 -12.92210 -16.33036 1.000 14.79181 ? 93   MET A CA    1 
ATOM   751  C C     . MET A 1 93  ? 29.18157 -11.69602 -16.06812 1.000 16.19484 ? 93   MET A C     1 
ATOM   752  O O     . MET A 1 93  ? 29.65352 -11.04590 -17.00792 1.000 15.37967 ? 93   MET A O     1 
ATOM   753  C CB    . MET A 1 93  ? 26.83477 -12.58152 -16.15496 1.000 15.20552 ? 93   MET A CB    1 
ATOM   754  C CG    . MET A 1 93  ? 25.88077 -13.68208 -16.59917 1.000 13.66052 ? 93   MET A CG    1 
ATOM   755  S SD    . MET A 1 93  ? 24.19399 -13.43718 -16.00268 1.000 20.65951 ? 93   MET A SD    1 
ATOM   756  C CE    . MET A 1 93  ? 23.70090 -12.01938 -16.97381 1.000 17.42037 ? 93   MET A CE    1 
ATOM   757  N N     . LEU A 1 94  ? 29.40274 -11.36789 -14.79263 1.000 14.55571 ? 94   LEU A N     1 
ATOM   758  C CA    . LEU A 1 94  ? 30.27770 -10.25173 -14.44479 1.000 14.77973 ? 94   LEU A CA    1 
ATOM   759  C C     . LEU A 1 94  ? 31.72272 -10.53394 -14.83504 1.000 17.46467 ? 94   LEU A C     1 
ATOM   760  O O     . LEU A 1 94  ? 32.43640 -9.63144  -15.28921 1.000 17.75426 ? 94   LEU A O     1 
ATOM   761  C CB    . LEU A 1 94  ? 30.18212 -9.96851  -12.94828 1.000 15.12882 ? 94   LEU A CB    1 
ATOM   762  C CG    . LEU A 1 94  ? 30.86923 -8.70496  -12.43421 1.000 18.54961 ? 94   LEU A CG    1 
ATOM   763  C CD1   . LEU A 1 94  ? 30.43017 -7.46948  -13.21132 1.000 20.52763 ? 94   LEU A CD1   1 
ATOM   764  C CD2   . LEU A 1 94  ? 30.60119 -8.55284  -10.95062 1.000 19.85429 ? 94   LEU A CD2   1 
ATOM   765  N N     . CYS A 1 95  ? 32.17011 -11.77927 -14.64932 1.000 16.09458 ? 95   CYS A N     1 
ATOM   766  C CA    . CYS A 1 95  ? 33.53722 -12.15215 -14.99891 1.000 15.75453 ? 95   CYS A CA    1 
ATOM   767  C C     . CYS A 1 95  ? 33.82211 -11.90106 -16.47444 1.000 19.49579 ? 95   CYS A C     1 
ATOM   768  O O     . CYS A 1 95  ? 34.88605 -11.37745 -16.82836 1.000 20.77052 ? 95   CYS A O     1 
ATOM   769  C CB    . CYS A 1 95  ? 33.77652 -13.62063 -14.64699 1.000 18.94696 ? 95   CYS A CB    1 
ATOM   770  S SG    . CYS A 1 95  ? 35.41760 -14.24279 -15.06328 1.000 21.90312 ? 95   CYS A SG    1 
ATOM   771  N N     . GLY A 1 96  ? 32.88690 -12.27541 -17.35179 1.000 19.01970 ? 96   GLY A N     1 
ATOM   772  C CA    . GLY A 1 96  ? 33.06541 -12.00846 -18.76787 1.000 22.60074 ? 96   GLY A CA    1 
ATOM   773  C C     . GLY A 1 96  ? 32.96367 -10.53688 -19.10568 1.000 22.34734 ? 96   GLY A C     1 
ATOM   774  O O     . GLY A 1 96  ? 33.52155 -10.08801 -20.11098 1.000 23.95739 ? 96   GLY A O     1 
ATOM   775  N N     . ALA A 1 97  ? 32.26537 -9.76541  -18.27074 1.000 20.13648 ? 97   ALA A N     1 
ATOM   776  C CA    . ALA A 1 97  ? 32.12721 -8.33495  -18.50815 1.000 19.99335 ? 97   ALA A CA    1 
ATOM   777  C C     . ALA A 1 97  ? 33.41001 -7.59528  -18.15473 1.000 19.72199 ? 97   ALA A C     1 
ATOM   778  O O     . ALA A 1 97  ? 33.95531 -6.85848  -18.98240 1.000 22.19519 ? 97   ALA A O     1 
ATOM   779  C CB    . ALA A 1 97  ? 30.94479 -7.78780  -17.70836 1.000 22.53475 ? 97   ALA A CB    1 
ATOM   780  N N     . ILE A 1 98  ? 33.90279 -7.77528  -16.92599 1.000 19.72779 ? 98   ILE A N     1 
ATOM   781  C CA    . ILE A 1 98  ? 35.20234 -7.21560  -16.56591 1.000 20.21460 ? 98   ILE A CA    1 
ATOM   782  C C     . ILE A 1 98  ? 36.27117 -7.71345  -17.52928 1.000 20.66747 ? 98   ILE A C     1 
ATOM   783  O O     . ILE A 1 98  ? 37.10514 -6.93753  -18.01293 1.000 23.49186 ? 98   ILE A O     1 
ATOM   784  C CB    . ILE A 1 98  ? 35.54725 -7.55175  -15.10360 1.000 17.83697 ? 98   ILE A CB    1 
ATOM   785  C CG1   . ILE A 1 98  ? 34.59762 -6.82114  -14.15472 1.000 22.31446 ? 98   ILE A CG1   1 
ATOM   786  C CG2   . ILE A 1 98  ? 36.98553 -7.17618  -14.79901 1.000 22.82301 ? 98   ILE A CG2   1 
ATOM   787  C CD1   . ILE A 1 98  ? 34.60922 -7.36524  -12.74802 1.000 18.36349 ? 98   ILE A CD1   1 
ATOM   788  N N     . GLY A 1 99  ? 36.25244 -9.00788  -17.83222 1.000 22.34502 ? 99   GLY A N     1 
ATOM   789  C CA    . GLY A 1 99  ? 37.05591 -9.55027  -18.91842 1.000 22.36898 ? 99   GLY A CA    1 
ATOM   790  C C     . GLY A 1 99  ? 38.54599 -9.33566  -18.78174 1.000 23.63659 ? 99   GLY A C     1 
ATOM   791  O O     . GLY A 1 99  ? 39.22896 -9.10141  -19.78620 1.000 24.13835 ? 99   GLY A O     1 
ATOM   792  N N     . CYS A 1 100 ? 39.06768 -9.41152  -17.56253 1.000 23.41289 ? 100  CYS A N     1 
ATOM   793  C CA    . CYS A 1 100 ? 40.49448 -9.26394  -17.32498 1.000 24.15924 ? 100  CYS A CA    1 
ATOM   794  C C     . CYS A 1 100 ? 41.20782 -10.59939 -17.50252 1.000 26.67453 ? 100  CYS A C     1 
ATOM   795  O O     . CYS A 1 100 ? 40.62946 -11.67286 -17.32066 1.000 27.45209 ? 100  CYS A O     1 
ATOM   796  C CB    . CYS A 1 100 ? 40.76360 -8.72192  -15.91702 1.000 26.67656 ? 100  CYS A CB    1 
ATOM   797  S SG    . CYS A 1 100 ? 40.03741 -9.68951  -14.56305 1.000 29.60923 ? 100  CYS A SG    1 
ATOM   798  N N     . ILE A 1 101 ? 42.48655 -10.51589 -17.86164 1.000 24.84493 ? 101  ILE A N     1 
ATOM   799  C CA    . ILE A 1 101 ? 43.35527 -11.68445 -17.92427 1.000 24.35189 ? 101  ILE A CA    1 
ATOM   800  C C     . ILE A 1 101 ? 44.40362 -11.51682 -16.83600 1.000 24.40815 ? 101  ILE A C     1 
ATOM   801  O O     . ILE A 1 101 ? 45.43705 -10.87483 -17.04888 1.000 26.28956 ? 101  ILE A O     1 
ATOM   802  C CB    . ILE A 1 101 ? 44.00111 -11.83760 -19.31255 1.000 25.80999 ? 101  ILE A CB    1 
ATOM   803  C CG1   . ILE A 1 101 ? 42.92199 -11.89572 -20.39306 1.000 25.43589 ? 101  ILE A CG1   1 
ATOM   804  C CG2   . ILE A 1 101 ? 44.85329 -13.09371 -19.36350 1.000 26.43504 ? 101  ILE A CG2   1 
ATOM   805  C CD1   . ILE A 1 101 ? 41.96719 -13.06195 -20.23397 1.000 25.98524 ? 101  ILE A CD1   1 
ATOM   806  N N     . GLY A 1 102 ? 44.13950 -12.07627 -15.66024 1.000 24.11409 ? 102  GLY A N     1 
ATOM   807  C CA    . GLY A 1 102 ? 44.98424 -11.82351 -14.51028 1.000 25.70832 ? 102  GLY A CA    1 
ATOM   808  C C     . GLY A 1 102 ? 46.26288 -12.63495 -14.45515 1.000 26.19953 ? 102  GLY A C     1 
ATOM   809  O O     . GLY A 1 102 ? 46.50668 -13.33902 -13.47080 1.000 27.62781 ? 102  GLY A O     1 
ATOM   810  N N     . PHE A 1 103 ? 47.09645 -12.54599 -15.49561 1.000 24.28233 ? 103  PHE A N     1 
ATOM   811  C CA    . PHE A 1 103 ? 48.38331 -13.23207 -15.45486 1.000 26.24927 ? 103  PHE A CA    1 
ATOM   812  C C     . PHE A 1 103 ? 49.36047 -12.55591 -14.50290 1.000 32.37122 ? 103  PHE A C     1 
ATOM   813  O O     . PHE A 1 103 ? 50.37378 -13.16077 -14.13466 1.000 35.34355 ? 103  PHE A O     1 
ATOM   814  C CB    . PHE A 1 103 ? 48.99841 -13.31830 -16.85509 1.000 28.79415 ? 103  PHE A CB    1 
ATOM   815  C CG    . PHE A 1 103 ? 49.02811 -12.01137 -17.59416 1.000 28.46274 ? 103  PHE A CG    1 
ATOM   816  C CD1   . PHE A 1 103 ? 50.07925 -11.12552 -17.42512 1.000 31.44438 ? 103  PHE A CD1   1 
ATOM   817  C CD2   . PHE A 1 103 ? 48.02072 -11.68422 -18.48514 1.000 28.93384 ? 103  PHE A CD2   1 
ATOM   818  C CE1   . PHE A 1 103 ? 50.11101 -9.92547  -18.11111 1.000 27.44631 ? 103  PHE A CE1   1 
ATOM   819  C CE2   . PHE A 1 103 ? 48.04726 -10.48814 -19.17580 1.000 26.43566 ? 103  PHE A CE2   1 
ATOM   820  C CZ    . PHE A 1 103 ? 49.09251 -9.60825  -18.98975 1.000 26.55753 ? 103  PHE A CZ    1 
ATOM   821  N N     . SER A 1 104 ? 49.07910 -11.31859 -14.10380 1.000 27.42291 ? 104  SER A N     1 
ATOM   822  C CA    . SER A 1 104 ? 49.88931 -10.59177 -13.14030 1.000 26.37352 ? 104  SER A CA    1 
ATOM   823  C C     . SER A 1 104 ? 48.96107 -9.77914  -12.25032 1.000 24.67535 ? 104  SER A C     1 
ATOM   824  O O     . SER A 1 104 ? 47.77270 -9.61745  -12.54074 1.000 20.99462 ? 104  SER A O     1 
ATOM   825  C CB    . SER A 1 104 ? 50.91002 -9.68066  -13.83409 1.000 27.92995 ? 104  SER A CB    1 
ATOM   826  O OG    . SER A 1 104 ? 50.26455 -8.58301  -14.45719 1.000 24.41396 ? 104  SER A OG    1 
ATOM   827  N N     . TRP A 1 105 ? 49.51366 -9.26643  -11.14889 1.000 26.22948 ? 105  TRP A N     1 
ATOM   828  C CA    . TRP A 1 105 ? 48.72561 -8.40309  -10.27604 1.000 25.43511 ? 105  TRP A CA    1 
ATOM   829  C C     . TRP A 1 105 ? 48.31250 -7.12998  -11.00328 1.000 21.94944 ? 105  TRP A C     1 
ATOM   830  O O     . TRP A 1 105 ? 47.16869 -6.67747  -10.87990 1.000 21.76906 ? 105  TRP A O     1 
ATOM   831  C CB    . TRP A 1 105 ? 49.51680 -8.06773  -9.01110  1.000 25.38557 ? 105  TRP A CB    1 
ATOM   832  C CG    . TRP A 1 105 ? 48.78797 -7.16153  -8.06157  1.000 22.03229 ? 105  TRP A CG    1 
ATOM   833  C CD1   . TRP A 1 105 ? 47.97463 -7.54078  -7.03263  1.000 21.88706 ? 105  TRP A CD1   1 
ATOM   834  C CD2   . TRP A 1 105 ? 48.80353 -5.72808  -8.05316  1.000 20.07664 ? 105  TRP A CD2   1 
ATOM   835  N NE1   . TRP A 1 105 ? 47.48522 -6.43384  -6.38255  1.000 19.99142 ? 105  TRP A NE1   1 
ATOM   836  C CE2   . TRP A 1 105 ? 47.97897 -5.30828  -6.98966  1.000 20.79421 ? 105  TRP A CE2   1 
ATOM   837  C CE3   . TRP A 1 105 ? 49.43447 -4.75957  -8.84039  1.000 20.32352 ? 105  TRP A CE3   1 
ATOM   838  C CZ2   . TRP A 1 105 ? 47.76866 -3.96185  -6.69473  1.000 20.13761 ? 105  TRP A CZ2   1 
ATOM   839  C CZ3   . TRP A 1 105 ? 49.22429 -3.42344  -8.54558  1.000 22.22973 ? 105  TRP A CZ3   1 
ATOM   840  C CH2   . TRP A 1 105 ? 48.39826 -3.03736  -7.48183  1.000 21.44036 ? 105  TRP A CH2   1 
ATOM   841  N N     . ALA A 1 106 ? 49.22880 -6.54548  -11.77930 1.000 22.86745 ? 106  ALA A N     1 
ATOM   842  C CA    . ALA A 1 106 ? 48.92217 -5.32469  -12.51464 1.000 21.86578 ? 106  ALA A CA    1 
ATOM   843  C C     . ALA A 1 106 ? 47.90189 -5.54963  -13.62197 1.000 22.59573 ? 106  ALA A C     1 
ATOM   844  O O     . ALA A 1 106 ? 47.26555 -4.58651  -14.06229 1.000 24.12613 ? 106  ALA A O     1 
ATOM   845  C CB    . ALA A 1 106 ? 50.20080 -4.73091  -13.10673 1.000 23.77992 ? 106  ALA A CB    1 
ATOM   846  N N     . ALA A 1 107 ? 47.73688 -6.79067  -14.08815 1.000 21.39023 ? 107  ALA A N     1 
ATOM   847  C CA    . ALA A 1 107 ? 46.75886 -7.06234  -15.13528 1.000 20.90790 ? 107  ALA A CA    1 
ATOM   848  C C     . ALA A 1 107 ? 45.33498 -6.80764  -14.66166 1.000 24.89881 ? 107  ALA A C     1 
ATOM   849  O O     . ALA A 1 107 ? 44.45194 -6.56010  -15.49147 1.000 25.80675 ? 107  ALA A O     1 
ATOM   850  C CB    . ALA A 1 107 ? 46.90234 -8.50315  -15.62949 1.000 24.83541 ? 107  ALA A CB    1 
ATOM   851  N N     . SER A 1 108 ? 45.10127 -6.88266  -13.34646 1.000 24.19321 ? 108  SER A N     1 
ATOM   852  C CA    . SER A 1 108 ? 43.87163 -6.53611  -12.64100 1.000 21.71373 ? 108  SER A CA    1 
ATOM   853  C C     . SER A 1 108 ? 44.03241 -6.92460  -11.17645 1.000 19.41535 ? 108  SER A C     1 
ATOM   854  O O     . SER A 1 108 ? 43.84667 -8.09590  -10.82253 1.000 20.20081 ? 108  SER A O     1 
ATOM   855  C CB    . SER A 1 108 ? 42.64802 -7.22803  -13.24298 1.000 22.90753 ? 108  SER A CB    1 
ATOM   856  O OG    . SER A 1 108 ? 41.79215 -6.28205  -13.86131 1.000 23.65783 ? 108  SER A OG    1 
ATOM   857  N N     . PRO A 1 109 ? 44.38952 -5.97533  -10.30480 1.000 19.02696 ? 109  PRO A N     1 
ATOM   858  C CA    . PRO A 1 109 ? 44.63200 -6.31680  -8.88984  1.000 18.38892 ? 109  PRO A CA    1 
ATOM   859  C C     . PRO A 1 109 ? 43.50627 -7.09067  -8.22261  1.000 18.84646 ? 109  PRO A C     1 
ATOM   860  O O     . PRO A 1 109 ? 43.77391 -8.07197  -7.51878  1.000 19.17364 ? 109  PRO A O     1 
ATOM   861  C CB    . PRO A 1 109 ? 44.82661 -4.93967  -8.24523  1.000 17.11238 ? 109  PRO A CB    1 
ATOM   862  C CG    . PRO A 1 109 ? 45.42557 -4.11918  -9.33977  1.000 18.24857 ? 109  PRO A CG    1 
ATOM   863  C CD    . PRO A 1 109 ? 44.71541 -4.56705  -10.59314 1.000 19.77445 ? 109  PRO A CD    1 
ATOM   864  N N     . ALA A 1 110 ? 42.25185 -6.68351  -8.43054  1.000 17.07430 ? 110  ALA A N     1 
ATOM   865  C CA    . ALA A 1 110 ? 41.13744 -7.34304  -7.75516  1.000 18.10925 ? 110  ALA A CA    1 
ATOM   866  C C     . ALA A 1 110 ? 41.03152 -8.81671  -8.13071  1.000 20.12986 ? 110  ALA A C     1 
ATOM   867  O O     . ALA A 1 110 ? 40.58509 -9.63320  -7.31545  1.000 17.11929 ? 110  ALA A O     1 
ATOM   868  C CB    . ALA A 1 110 ? 39.83118 -6.61817  -8.07577  1.000 17.35470 ? 110  ALA A CB    1 
ATOM   869  N N     . CYS A 1 111 ? 41.43388 -9.17695  -9.35243  1.000 17.98617 ? 111  CYS A N     1 
ATOM   870  C CA    . CYS A 1 111 ? 41.33974 -10.56930 -9.78126  1.000 19.10986 ? 111  CYS A CA    1 
ATOM   871  C C     . CYS A 1 111 ? 42.23406 -11.46652 -8.93477  1.000 20.24456 ? 111  CYS A C     1 
ATOM   872  O O     . CYS A 1 111 ? 41.85928 -12.59725 -8.60283  1.000 22.44587 ? 111  CYS A O     1 
ATOM   873  C CB    . CYS A 1 111 ? 41.70110 -10.68420 -11.26348 1.000 17.88382 ? 111  CYS A CB    1 
ATOM   874  S SG    . CYS A 1 111 ? 41.65876 -12.37010 -11.93862 1.000 28.93203 ? 111  CYS A SG    1 
ATOM   875  N N     . THR A 1 112 ? 43.41495 -10.97304 -8.56213  1.000 17.96695 ? 112  THR A N     1 
ATOM   876  C CA    . THR A 1 112 ? 44.33302 -11.76440 -7.75176  1.000 17.98657 ? 112  THR A CA    1 
ATOM   877  C C     . THR A 1 112 ? 43.98981 -11.67560 -6.26830  1.000 18.88750 ? 112  THR A C     1 
ATOM   878  O O     . THR A 1 112 ? 44.05267 -12.68112 -5.55121  1.000 18.51038 ? 112  THR A O     1 
ATOM   879  C CB    . THR A 1 112 ? 45.77125 -11.30148 -8.00087  1.000 26.16121 ? 112  THR A CB    1 
ATOM   880  O OG1   . THR A 1 112 ? 46.17556 -11.68576 -9.32151  1.000 25.15568 ? 112  THR A OG1   1 
ATOM   881  C CG2   . THR A 1 112 ? 46.72635 -11.91783 -6.98815  1.000 28.44055 ? 112  THR A CG2   1 
ATOM   882  N N     . GLU A 1 113 ? 43.60266 -10.48790 -5.79759  1.000 17.42572 ? 113  GLU A N     1 
ATOM   883  C CA    . GLU A 1 113 ? 43.41260 -10.28651 -4.36418  1.000 17.30803 ? 113  GLU A CA    1 
ATOM   884  C C     . GLU A 1 113 ? 42.15696 -10.98545 -3.85449  1.000 15.20634 ? 113  GLU A C     1 
ATOM   885  O O     . GLU A 1 113 ? 42.16768 -11.56403 -2.76175  1.000 14.47241 ? 113  GLU A O     1 
ATOM   886  C CB    . GLU A 1 113 ? 43.36921 -8.79276  -4.05306  1.000 18.00786 ? 113  GLU A CB    1 
ATOM   887  C CG    . GLU A 1 113 ? 44.60616 -8.05100  -4.52880  1.000 19.65100 ? 113  GLU A CG    1 
ATOM   888  C CD    . GLU A 1 113 ? 45.07256 -7.00797  -3.54213  1.000 17.31757 ? 113  GLU A CD    1 
ATOM   889  O OE1   . GLU A 1 113 ? 44.46860 -6.91067  -2.45390  1.000 19.65030 ? 113  GLU A OE1   1 
ATOM   890  O OE2   . GLU A 1 113 ? 46.04760 -6.29137  -3.85168  1.000 21.43357 ? 113  GLU A OE2   1 
ATOM   891  N N     . LEU A 1 114 ? 41.06274 -10.93726 -4.61927  1.000 15.71426 ? 114  LEU A N     1 
ATOM   892  C CA    . LEU A 1 114 ? 39.85572 -11.64842 -4.20587  1.000 13.73422 ? 114  LEU A CA    1 
ATOM   893  C C     . LEU A 1 114 ? 40.09862 -13.15051 -4.13938  1.000 13.75360 ? 114  LEU A C     1 
ATOM   894  O O     . LEU A 1 114 ? 39.56456 -13.83439 -3.25826  1.000 13.09924 ? 114  LEU A O     1 
ATOM   895  C CB    . LEU A 1 114 ? 38.69845 -11.33647 -5.15474  1.000 12.32347 ? 114  LEU A CB    1 
ATOM   896  C CG    . LEU A 1 114 ? 37.34660 -11.90899 -4.71984  1.000 13.45344 ? 114  LEU A CG    1 
ATOM   897  C CD1   . LEU A 1 114 ? 36.90725 -11.32057 -3.38505  1.000 14.04010 ? 114  LEU A CD1   1 
ATOM   898  C CD2   . LEU A 1 114 ? 36.28692 -11.67855 -5.78680  1.000 13.03388 ? 114  LEU A CD2   1 
ATOM   899  N N     . GLU A 1 115 ? 40.91231 -13.67816 -5.05822  1.000 14.07512 ? 115  GLU A N     1 
ATOM   900  C CA    . GLU A 1 115 ? 41.20837 -15.10690 -5.05714  1.000 15.20228 ? 115  GLU A CA    1 
ATOM   901  C C     . GLU A 1 115 ? 41.92213 -15.52231 -3.77850  1.000 15.29006 ? 115  GLU A C     1 
ATOM   902  O O     . GLU A 1 115 ? 41.58423 -16.54835 -3.17508  1.000 14.33402 ? 115  GLU A O     1 
ATOM   903  C CB    . GLU A 1 115 ? 42.04659 -15.46965 -6.28156  1.000 14.13958 ? 115  GLU A CB    1 
ATOM   904  C CG    . GLU A 1 115 ? 42.28938 -16.95981 -6.43598  1.000 15.92110 ? 115  GLU A CG    1 
ATOM   905  C CD    . GLU A 1 115 ? 42.71764 -17.34026 -7.83814  1.000 20.85995 ? 115  GLU A CD    1 
ATOM   906  O OE1   . GLU A 1 115 ? 42.14536 -16.79268 -8.80588  1.000 17.30691 ? 115  GLU A OE1   1 
ATOM   907  O OE2   . GLU A 1 115 ? 43.61747 -18.19572 -7.97021  1.000 19.70942 ? 115  GLU A OE2   1 
ATOM   908  N N     . THR A 1 116 ? 42.90895 -14.73227 -3.34609  1.000 14.87241 ? 116  THR A N     1 
ATOM   909  C CA    . THR A 1 116 ? 43.64421 -15.06062 -2.12903  1.000 16.19862 ? 116  THR A CA    1 
ATOM   910  C C     . THR A 1 116 ? 42.72667 -15.05705 -0.91413  1.000 16.76671 ? 116  THR A C     1 
ATOM   911  O O     . THR A 1 116 ? 42.82673 -15.93401 -0.04790  1.000 16.67621 ? 116  THR A O     1 
ATOM   912  C CB    . THR A 1 116 ? 44.79387 -14.07483 -1.93067  1.000 24.06119 ? 116  THR A CB    1 
ATOM   913  O OG1   . THR A 1 116 ? 45.66901 -14.12557 -3.06292  1.000 25.87408 ? 116  THR A OG1   1 
ATOM   914  C CG2   . THR A 1 116 ? 45.57987 -14.41950 -0.67572  1.000 26.18394 ? 116  THR A CG2   1 
ATOM   915  N N     . VAL A 1 117 ? 41.81570 -14.08472 -0.83805  1.000 14.31945 ? 117  VAL A N     1 
ATOM   916  C CA    . VAL A 1 117 ? 40.90427 -14.01956 0.30052   1.000 14.44419 ? 117  VAL A CA    1 
ATOM   917  C C     . VAL A 1 117 ? 39.89535 -15.16245 0.25463   1.000 12.72876 ? 117  VAL A C     1 
ATOM   918  O O     . VAL A 1 117 ? 39.56505 -15.75371 1.28742   1.000 12.63478 ? 117  VAL A O     1 
ATOM   919  C CB    . VAL A 1 117 ? 40.20467 -12.65000 0.35217   1.000 13.74105 ? 117  VAL A CB    1 
ATOM   920  C CG1   . VAL A 1 117 ? 39.25163 -12.58983 1.53730   1.000 15.91899 ? 117  VAL A CG1   1 
ATOM   921  C CG2   . VAL A 1 117 ? 41.23585 -11.53705 0.45211   1.000 15.78720 ? 117  VAL A CG2   1 
ATOM   922  N N     . MET A 1 118 ? 39.38748 -15.49558 -0.93439  1.000 12.02380 ? 118  MET A N     1 
ATOM   923  C CA    . MET A 1 118 ? 38.40770 -16.57557 -1.02499  1.000 12.59192 ? 118  MET A CA    1 
ATOM   924  C C     . MET A 1 118 ? 39.01724 -17.92748 -0.68099  1.000 12.40536 ? 118  MET A C     1 
ATOM   925  O O     . MET A 1 118 ? 38.33067 -18.79357 -0.12580  1.000 12.64929 ? 118  MET A O     1 
ATOM   926  C CB    . MET A 1 118 ? 37.77886 -16.62649 -2.41488  1.000 12.45563 ? 118  MET A CB    1 
ATOM   927  C CG    . MET A 1 118 ? 36.84039 -15.47270 -2.77180  1.000 12.52128 ? 118  MET A CG    1 
ATOM   928  S SD    . MET A 1 118 ? 35.45062 -15.23304 -1.63048  1.000 13.61145 ? 118  MET A SD    1 
ATOM   929  C CE    . MET A 1 118 ? 36.13255 -14.08540 -0.42520  1.000 12.67152 ? 118  MET A CE    1 
ATOM   930  N N     . MET A 1 119 ? 40.29458 -18.13365 -0.99802  1.000 11.90060 ? 119  MET A N     1 
ATOM   931  C CA    . MET A 1 119 ? 40.93074 -19.38672 -0.61554  1.000 13.18797 ? 119  MET A CA    1 
ATOM   932  C C     . MET A 1 119 ? 41.15101 -19.45607 0.88964   1.000 13.19926 ? 119  MET A C     1 
ATOM   933  O O     . MET A 1 119 ? 41.17592 -20.55350 1.45879   1.000 16.45857 ? 119  MET A O     1 
ATOM   934  C CB    . MET A 1 119 ? 42.24252 -19.56192 -1.37574  1.000 13.44686 ? 119  MET A CB    1 
ATOM   935  C CG    . MET A 1 119 ? 42.03337 -19.82477 -2.86471  1.000 11.46223 ? 119  MET A CG    1 
ATOM   936  S SD    . MET A 1 119 ? 41.21323 -21.40214 -3.19164  1.000 16.25025 ? 119  MET A SD    1 
ATOM   937  C CE    . MET A 1 119 ? 42.57143 -22.52798 -2.88406  1.000 13.61600 ? 119  MET A CE    1 
ATOM   938  N N     . ASP A 1 120 ? 41.28820 -18.30307 1.55312   1.000 13.66051 ? 120  ASP A N     1 
ATOM   939  C CA    . ASP A 1 120 ? 41.32089 -18.30055 3.01261   1.000 14.65037 ? 120  ASP A CA    1 
ATOM   940  C C     . ASP A 1 120 ? 39.93618 -18.55672 3.59482   1.000 15.44635 ? 120  ASP A C     1 
ATOM   941  O O     . ASP A 1 120 ? 39.79969 -19.32580 4.55283   1.000 15.16331 ? 120  ASP A O     1 
ATOM   942  C CB    . ASP A 1 120 ? 41.89142 -16.98219 3.53906   1.000 17.45301 ? 120  ASP A CB    1 
ATOM   943  C CG    . ASP A 1 120 ? 43.39216 -16.88046 3.35021   1.000 24.50667 ? 120  ASP A CG    1 
ATOM   944  O OD1   . ASP A 1 120 ? 44.04412 -17.93780 3.20882   1.000 23.46022 ? 120  ASP A OD1   1 
ATOM   945  O OD2   . ASP A 1 120 ? 43.92350 -15.75057 3.36692   1.000 25.94549 ? 120  ASP A OD2   1 
ATOM   946  N N     . TRP A 1 121 ? 38.90082 -17.91930 3.03574   1.000 13.58126 ? 121  TRP A N     1 
ATOM   947  C CA    . TRP A 1 121 ? 37.52838 -18.23925 3.42535   1.000 13.81964 ? 121  TRP A CA    1 
ATOM   948  C C     . TRP A 1 121 ? 37.28087 -19.73944 3.36178   1.000 13.50727 ? 121  TRP A C     1 
ATOM   949  O O     . TRP A 1 121 ? 36.80715 -20.34975 4.32698   1.000 14.37474 ? 121  TRP A O     1 
ATOM   950  C CB    . TRP A 1 121 ? 36.52796 -17.52184 2.51600   1.000 14.38253 ? 121  TRP A CB    1 
ATOM   951  C CG    . TRP A 1 121 ? 36.18815 -16.10967 2.88782   1.000 12.09391 ? 121  TRP A CG    1 
ATOM   952  C CD1   . TRP A 1 121 ? 36.91598 -15.25953 3.66681   1.000 14.19028 ? 121  TRP A CD1   1 
ATOM   953  C CD2   . TRP A 1 121 ? 35.01593 -15.38828 2.49079   1.000 14.16138 ? 121  TRP A CD2   1 
ATOM   954  N NE1   . TRP A 1 121 ? 36.27214 -14.04811 3.77172   1.000 14.90616 ? 121  TRP A NE1   1 
ATOM   955  C CE2   . TRP A 1 121 ? 35.10378 -14.10225 3.05727   1.000 14.58248 ? 121  TRP A CE2   1 
ATOM   956  C CE3   . TRP A 1 121 ? 33.90537 -15.70358 1.69980   1.000 15.50394 ? 121  TRP A CE3   1 
ATOM   957  C CZ2   . TRP A 1 121 ? 34.11881 -13.13333 2.86585   1.000 16.53073 ? 121  TRP A CZ2   1 
ATOM   958  C CZ3   . TRP A 1 121 ? 32.93014 -14.74201 1.50972   1.000 14.77814 ? 121  TRP A CZ3   1 
ATOM   959  C CH2   . TRP A 1 121 ? 33.04280 -13.47199 2.09008   1.000 13.65682 ? 121  TRP A CH2   1 
ATOM   960  N N     . LEU A 1 122 ? 37.60349 -20.34870 2.22146   1.000 13.50494 ? 122  LEU A N     1 
ATOM   961  C CA    . LEU A 1 122 ? 37.31683 -21.76330 2.02557   1.000 14.02004 ? 122  LEU A CA    1 
ATOM   962  C C     . LEU A 1 122 ? 38.19093 -22.63148 2.92185   1.000 13.11314 ? 122  LEU A C     1 
ATOM   963  O O     . LEU A 1 122 ? 37.71298 -23.61481 3.49896   1.000 14.51585 ? 122  LEU A O     1 
ATOM   964  C CB    . LEU A 1 122 ? 37.50937 -22.12201 0.55389   1.000 14.58863 ? 122  LEU A CB    1 
ATOM   965  C CG    . LEU A 1 122 ? 37.11602 -23.52930 0.11675   1.000 12.38973 ? 122  LEU A CG    1 
ATOM   966  C CD1   . LEU A 1 122 ? 35.68006 -23.81995 0.51751   1.000 14.89989 ? 122  LEU A CD1   1 
ATOM   967  C CD2   . LEU A 1 122 ? 37.29211 -23.66530 -1.38553  1.000 13.03145 ? 122  LEU A CD2   1 
ATOM   968  N N     . GLY A 1 123 ? 39.46997 -22.27563 3.06167   1.000 13.26351 ? 123  GLY A N     1 
ATOM   969  C CA    . GLY A 1 123 ? 40.34018 -23.01742 3.96160   1.000 14.70921 ? 123  GLY A CA    1 
ATOM   970  C C     . GLY A 1 123 ? 39.84602 -23.00335 5.39643   1.000 19.09348 ? 123  GLY A C     1 
ATOM   971  O O     . GLY A 1 123 ? 39.95301 -24.00250 6.11148   1.000 16.92746 ? 123  GLY A O     1 
ATOM   972  N N     . LYS A 1 124 ? 39.28864 -21.87235 5.83451   1.000 15.38245 ? 124  LYS A N     1 
ATOM   973  C CA    . LYS A 1 124 ? 38.73016 -21.79642 7.17993   1.000 17.09696 ? 124  LYS A CA    1 
ATOM   974  C C     . LYS A 1 124 ? 37.43469 -22.58877 7.29637   1.000 16.54553 ? 124  LYS A C     1 
ATOM   975  O O     . LYS A 1 124 ? 37.15988 -23.16595 8.35371   1.000 16.85530 ? 124  LYS A O     1 
ATOM   976  C CB    . LYS A 1 124 ? 38.51244 -20.33637 7.57326   1.000 17.55388 ? 124  LYS A CB    1 
ATOM   977  C CG    . LYS A 1 124 ? 39.81779 -19.55576 7.67619   1.000 20.60000 ? 124  LYS A CG    1 
ATOM   978  C CD    . LYS A 1 124 ? 39.59937 -18.05159 7.73655   1.000 24.26518 ? 124  LYS A CD    1 
ATOM   979  C CE    . LYS A 1 124 ? 38.66643 -17.65964 8.86657   1.000 29.86806 ? 124  LYS A CE    1 
ATOM   980  N NZ    . LYS A 1 124 ? 39.09590 -16.37761 9.49981   1.000 39.74029 ? 124  LYS A NZ    1 
ATOM   981  N N     . MET A 1 125 ? 36.63373 -22.63713 6.22769   1.000 15.23604 ? 125  MET A N     1 
ATOM   982  C CA    . MET A 1 125 ? 35.41668 -23.44381 6.25092   1.000 15.00391 ? 125  MET A CA    1 
ATOM   983  C C     . MET A 1 125 ? 35.73206 -24.92906 6.37370   1.000 17.74212 ? 125  MET A C     1 
ATOM   984  O O     . MET A 1 125 ? 34.94897 -25.68678 6.95916   1.000 18.18376 ? 125  MET A O     1 
ATOM   985  C CB    . MET A 1 125 ? 34.59019 -23.18098 4.99520   1.000 14.76259 ? 125  MET A CB    1 
ATOM   986  C CG    . MET A 1 125 ? 34.00355 -21.78785 4.92406   1.000 16.93086 ? 125  MET A CG    1 
ATOM   987  S SD    . MET A 1 125 ? 33.38307 -21.39790 3.27607   1.000 22.12923 ? 125  MET A SD    1 
ATOM   988  C CE    . MET A 1 125 ? 32.33220 -22.81572 2.96725   1.000 12.60716 ? 125  MET A CE    1 
ATOM   989  N N     . LEU A 1 126 ? 36.86246 -25.36426 5.82437   1.000 16.01313 ? 126  LEU A N     1 
ATOM   990  C CA    . LEU A 1 126 ? 37.30323 -26.74610 5.94705   1.000 15.19769 ? 126  LEU A CA    1 
ATOM   991  C C     . LEU A 1 126 ? 38.14847 -26.98923 7.18897   1.000 18.21971 ? 126  LEU A C     1 
ATOM   992  O O     . LEU A 1 126 ? 38.59430 -28.12196 7.39990   1.000 19.01890 ? 126  LEU A O     1 
ATOM   993  C CB    . LEU A 1 126 ? 38.08873 -27.16932 4.70035   1.000 17.38707 ? 126  LEU A CB    1 
ATOM   994  C CG    . LEU A 1 126 ? 37.25891 -27.61873 3.49458   1.000 17.96930 ? 126  LEU A CG    1 
ATOM   995  C CD1   . LEU A 1 126 ? 37.02815 -26.48408 2.52135   1.000 21.42074 ? 126  LEU A CD1   1 
ATOM   996  C CD2   . LEU A 1 126 ? 37.93957 -28.78404 2.79835   1.000 22.06092 ? 126  LEU A CD2   1 
ATOM   997  N N     . GLU A 1 127 ? 38.36070 -25.96451 8.01775   1.000 17.20000 ? 127  GLU A N     1 
ATOM   998  C CA    . GLU A 1 127 ? 39.22969 -26.06113 9.19437   1.000 19.43903 ? 127  GLU A CA    1 
ATOM   999  C C     . GLU A 1 127 ? 40.58835 -26.64742 8.82259   1.000 18.50448 ? 127  GLU A C     1 
ATOM   1000 O O     . GLU A 1 127 ? 41.12110 -27.52973 9.49959   1.000 19.56906 ? 127  GLU A O     1 
ATOM   1001 C CB    . GLU A 1 127 ? 38.56513 -26.86667 10.31291  1.000 21.92524 ? 127  GLU A CB    1 
ATOM   1002 C CG    . GLU A 1 127 ? 37.31490 -26.20654 10.87253  1.000 28.61582 ? 127  GLU A CG    1 
ATOM   1003 C CD    . GLU A 1 127 ? 36.68729 -26.99265 12.00640  1.000 42.60632 ? 127  GLU A CD    1 
ATOM   1004 O OE1   . GLU A 1 127 ? 36.17798 -28.10386 11.75153  1.000 43.05106 ? 127  GLU A OE1   1 
ATOM   1005 O OE2   . GLU A 1 127 ? 36.68857 -26.49154 13.15074  1.000 46.31307 ? 127  GLU A OE2   1 
ATOM   1006 N N     . LEU A 1 128 ? 41.14135 -26.15472 7.71900   1.000 15.78932 ? 128  LEU A N     1 
ATOM   1007 C CA    . LEU A 1 128 ? 42.46059 -26.57095 7.28548   1.000 18.65735 ? 128  LEU A CA    1 
ATOM   1008 C C     . LEU A 1 128 ? 43.50927 -26.09770 8.29020   1.000 19.06319 ? 128  LEU A C     1 
ATOM   1009 O O     . LEU A 1 128 ? 43.32374 -25.07383 8.95406   1.000 20.85337 ? 128  LEU A O     1 
ATOM   1010 C CB    . LEU A 1 128 ? 42.77244 -25.99084 5.90893   1.000 17.03229 ? 128  LEU A CB    1 
ATOM   1011 C CG    . LEU A 1 128 ? 42.19466 -26.67921 4.67002   1.000 16.68812 ? 128  LEU A CG    1 
ATOM   1012 C CD1   . LEU A 1 128 ? 42.82995 -26.09953 3.41584   1.000 16.58828 ? 128  LEU A CD1   1 
ATOM   1013 C CD2   . LEU A 1 128 ? 42.38429 -28.18912 4.72458   1.000 15.67868 ? 128  LEU A CD2   1 
ATOM   1014 N N     . PRO A 1 129 ? 44.60890 -26.83491 8.43556   1.000 21.69914 ? 129  PRO A N     1 
ATOM   1015 C CA    . PRO A 1 129 ? 45.72344 -26.33688 9.24738   1.000 21.52610 ? 129  PRO A CA    1 
ATOM   1016 C C     . PRO A 1 129 ? 46.17198 -24.96681 8.76006   1.000 21.99080 ? 129  PRO A C     1 
ATOM   1017 O O     . PRO A 1 129 ? 46.20833 -24.69737 7.55749   1.000 19.96064 ? 129  PRO A O     1 
ATOM   1018 C CB    . PRO A 1 129 ? 46.80702 -27.39837 9.04141   1.000 21.30369 ? 129  PRO A CB    1 
ATOM   1019 C CG    . PRO A 1 129 ? 46.03508 -28.65328 8.79881   1.000 21.21205 ? 129  PRO A CG    1 
ATOM   1020 C CD    . PRO A 1 129 ? 44.81342 -28.23225 8.01472   1.000 18.96045 ? 129  PRO A CD    1 
ATOM   1021 N N     . LYS A 1 130 ? 46.50312 -24.09124 9.71340   1.000 22.76806 ? 130  LYS A N     1 
ATOM   1022 C CA    . LYS A 1 130 ? 46.85413 -22.71421 9.38092   1.000 25.20523 ? 130  LYS A CA    1 
ATOM   1023 C C     . LYS A 1 130 ? 48.05002 -22.62378 8.44131   1.000 23.97502 ? 130  LYS A C     1 
ATOM   1024 O O     . LYS A 1 130 ? 48.21331 -21.60289 7.76389   1.000 25.15558 ? 130  LYS A O     1 
ATOM   1025 C CB    . LYS A 1 130 ? 47.13628 -21.92146 10.65959  1.000 29.85027 ? 130  LYS A CB    1 
ATOM   1026 C CG    . LYS A 1 130 ? 45.94234 -21.79478 11.59639  1.000 34.54902 ? 130  LYS A CG    1 
ATOM   1027 C CD    . LYS A 1 130 ? 44.67548 -21.41970 10.83996  1.000 38.37884 ? 130  LYS A CD    1 
ATOM   1028 C CE    . LYS A 1 130 ? 43.46424 -21.41209 11.75983  1.000 42.58798 ? 130  LYS A CE    1 
ATOM   1029 N NZ    . LYS A 1 130 ? 42.22047 -21.04497 11.02671  1.000 43.18044 ? 130  LYS A NZ    1 
ATOM   1030 N N     . ALA A 1 131 ? 48.88373 -23.66556 8.37713   1.000 22.41440 ? 131  ALA A N     1 
ATOM   1031 C CA    . ALA A 1 131 ? 50.03125 -23.64382 7.47806   1.000 24.77461 ? 131  ALA A CA    1 
ATOM   1032 C C     . ALA A 1 131 ? 49.61803 -23.57589 6.01317   1.000 23.36205 ? 131  ALA A C     1 
ATOM   1033 O O     . ALA A 1 131 ? 50.43870 -23.20832 5.16542   1.000 22.40848 ? 131  ALA A O     1 
ATOM   1034 C CB    . ALA A 1 131 ? 50.91058 -24.87213 7.71937   1.000 25.55891 ? 131  ALA A CB    1 
ATOM   1035 N N     . PHE A 1 132 ? 48.36933 -23.91506 5.69681   1.000 20.62113 ? 132  PHE A N     1 
ATOM   1036 C CA    . PHE A 1 132 ? 47.87131 -23.85634 4.32974   1.000 20.09388 ? 132  PHE A CA    1 
ATOM   1037 C C     . PHE A 1 132 ? 47.29533 -22.49609 3.96151   1.000 23.74428 ? 132  PHE A C     1 
ATOM   1038 O O     . PHE A 1 132 ? 47.07789 -22.23531 2.77331   1.000 23.32734 ? 132  PHE A O     1 
ATOM   1039 C CB    . PHE A 1 132 ? 46.79480 -24.92635 4.11344   1.000 19.12294 ? 132  PHE A CB    1 
ATOM   1040 C CG    . PHE A 1 132 ? 47.33396 -26.32500 4.04077   1.000 18.89244 ? 132  PHE A CG    1 
ATOM   1041 C CD1   . PHE A 1 132 ? 48.05479 -26.74891 2.93768   1.000 19.71693 ? 132  PHE A CD1   1 
ATOM   1042 C CD2   . PHE A 1 132 ? 47.11631 -27.21820 5.07743   1.000 19.47333 ? 132  PHE A CD2   1 
ATOM   1043 C CE1   . PHE A 1 132 ? 48.55070 -28.03748 2.86991   1.000 19.57548 ? 132  PHE A CE1   1 
ATOM   1044 C CE2   . PHE A 1 132 ? 47.60972 -28.50745 5.01507   1.000 18.65695 ? 132  PHE A CE2   1 
ATOM   1045 C CZ    . PHE A 1 132 ? 48.32734 -28.91714 3.90915   1.000 17.88007 ? 132  PHE A CZ    1 
ATOM   1046 N N     . LEU A 1 133 ? 47.04721 -21.63185 4.94025   1.000 24.71880 ? 133  LEU A N     1 
ATOM   1047 C CA    . LEU A 1 133 ? 46.37256 -20.36453 4.70787   1.000 27.47582 ? 133  LEU A CA    1 
ATOM   1048 C C     . LEU A 1 133 ? 47.38334 -19.24830 4.47285   1.000 33.40070 ? 133  LEU A C     1 
ATOM   1049 O O     . LEU A 1 133 ? 48.50727 -19.28129 4.98052   1.000 36.27923 ? 133  LEU A O     1 
ATOM   1050 C CB    . LEU A 1 133 ? 45.47348 -20.01478 5.89437   1.000 26.47618 ? 133  LEU A CB    1 
ATOM   1051 C CG    . LEU A 1 133 ? 44.46910 -21.09772 6.30204   1.000 27.88395 ? 133  LEU A CG    1 
ATOM   1052 C CD1   . LEU A 1 133 ? 43.52185 -20.59116 7.38096   1.000 32.78074 ? 133  LEU A CD1   1 
ATOM   1053 C CD2   . LEU A 1 133 ? 43.69389 -21.60767 5.09456   1.000 24.91128 ? 133  LEU A CD2   1 
ATOM   1054 N N     . ASN A 1 134 ? 46.96642 -18.24952 3.69555   1.000 35.18415 ? 134  ASN A N     1 
ATOM   1055 C CA    . ASN A 1 134 ? 47.83470 -17.12667 3.36311   1.000 40.31717 ? 134  ASN A CA    1 
ATOM   1056 C C     . ASN A 1 134 ? 47.76005 -15.98938 4.37208   1.000 48.84401 ? 134  ASN A C     1 
ATOM   1057 O O     . ASN A 1 134 ? 48.73022 -15.23462 4.51132   1.000 57.49043 ? 134  ASN A O     1 
ATOM   1058 C CB    . ASN A 1 134 ? 47.49055 -16.58849 1.97262   1.000 37.14640 ? 134  ASN A CB    1 
ATOM   1059 C CG    . ASN A 1 134 ? 48.41832 -15.47299 1.53779   1.000 47.01919 ? 134  ASN A CG    1 
ATOM   1060 O OD1   . ASN A 1 134 ? 49.53107 -15.71849 1.07274   1.000 50.18931 ? 134  ASN A OD1   1 
ATOM   1061 N ND2   . ASN A 1 134 ? 47.96563 -14.23459 1.69634   1.000 44.87563 ? 134  ASN A ND2   1 
ATOM   1062 N N     . GLU A 1 135 ? 46.63700 -15.84997 5.07342   1.000 53.11082 ? 135  GLU A N     1 
ATOM   1063 C CA    . GLU A 1 135 ? 46.45733 -14.75093 6.01322   1.000 57.77241 ? 135  GLU A CA    1 
ATOM   1064 C C     . GLU A 1 135 ? 47.54738 -14.75266 7.08031   1.000 74.55470 ? 135  GLU A C     1 
ATOM   1065 O O     . GLU A 1 135 ? 48.06522 -15.80238 7.47091   1.000 73.68670 ? 135  GLU A O     1 
ATOM   1066 C CB    . GLU A 1 135 ? 45.08362 -14.84793 6.67645   1.000 54.95869 ? 135  GLU A CB    1 
ATOM   1067 C CG    . GLU A 1 135 ? 44.74812 -16.24416 7.17697   1.000 58.38353 ? 135  GLU A CG    1 
ATOM   1068 C CD    . GLU A 1 135 ? 43.68456 -16.24028 8.25435   1.000 66.16147 ? 135  GLU A CD    1 
ATOM   1069 O OE1   . GLU A 1 135 ? 42.75881 -15.40458 8.17750   1.000 63.65388 ? 135  GLU A OE1   1 
ATOM   1070 O OE2   . GLU A 1 135 ? 43.77002 -17.08054 9.17375   1.000 68.52385 ? 135  GLU A OE2   1 
ATOM   1071 N N     . LYS A 1 136 ? 47.90141 -13.54953 7.53954   1.000 79.36661 ? 136  LYS A N     1 
ATOM   1072 C CA    . LYS A 1 136 ? 48.86136 -13.35284 8.63161   1.000 83.31387 ? 136  LYS A CA    1 
ATOM   1073 C C     . LYS A 1 136 ? 50.25506 -13.87187 8.27572   1.000 83.31928 ? 136  LYS A C     1 
ATOM   1074 O O     . LYS A 1 136 ? 50.86425 -14.64509 9.01778   1.000 85.95570 ? 136  LYS A O     1 
ATOM   1075 C CB    . LYS A 1 136 ? 48.35453 -13.98933 9.93003   1.000 83.49322 ? 136  LYS A CB    1 
ATOM   1076 C CG    . LYS A 1 136 ? 47.44112 -13.08828 10.74625  1.000 82.26270 ? 136  LYS A CG    1 
ATOM   1077 C CD    . LYS A 1 136 ? 47.85711 -11.63270 10.60669  1.000 81.00192 ? 136  LYS A CD    1 
ATOM   1078 C CE    . LYS A 1 136 ? 46.85212 -10.69877 11.25380  1.000 73.75872 ? 136  LYS A CE    1 
ATOM   1079 N NZ    . LYS A 1 136 ? 46.04146 -9.94838  10.25586  1.000 64.03858 ? 136  LYS A NZ    1 
ATOM   1080 N N     . ALA A 1 137 ? 50.75427 -13.43413 7.11922   1.000 78.60795 ? 137  ALA A N     1 
ATOM   1081 C CA    . ALA A 1 137 ? 52.14357 -13.64853 6.69946   1.000 78.70087 ? 137  ALA A CA    1 
ATOM   1082 C C     . ALA A 1 137 ? 52.57448 -15.11414 6.75568   1.000 76.68989 ? 137  ALA A C     1 
ATOM   1083 O O     . ALA A 1 137 ? 53.75523 -15.40845 6.95497   1.000 74.98559 ? 137  ALA A O     1 
ATOM   1084 C CB    . ALA A 1 137 ? 53.10344 -12.79471 7.53139   1.000 77.42771 ? 137  ALA A CB    1 
ATOM   1085 N N     . GLY A 1 138 ? 51.64235 -16.04698 6.58004   1.000 72.99570 ? 138  GLY A N     1 
ATOM   1086 C CA    . GLY A 1 138 ? 52.01994 -17.44329 6.49697   1.000 66.36969 ? 138  GLY A CA    1 
ATOM   1087 C C     . GLY A 1 138 ? 52.72013 -17.76193 5.18924   1.000 60.66787 ? 138  GLY A C     1 
ATOM   1088 O O     . GLY A 1 138 ? 52.46240 -17.15593 4.14914   1.000 59.09433 ? 138  GLY A O     1 
ATOM   1089 N N     . GLU A 1 139 ? 53.63296 -18.73229 5.24856   1.000 52.73050 ? 139  GLU A N     1 
ATOM   1090 C CA    . GLU A 1 139 ? 54.36653 -19.14105 4.05545   1.000 48.75438 ? 139  GLU A CA    1 
ATOM   1091 C C     . GLU A 1 139 ? 53.52186 -19.95576 3.08385   1.000 42.99211 ? 139  GLU A C     1 
ATOM   1092 O O     . GLU A 1 139 ? 53.93522 -20.14224 1.93484   1.000 40.08611 ? 139  GLU A O     1 
ATOM   1093 C CB    . GLU A 1 139 ? 55.61773 -19.93031 4.45147   1.000 50.84713 ? 139  GLU A CB    1 
ATOM   1094 C CG    . GLU A 1 139 ? 56.18547 -19.53877 5.81192   1.000 56.78643 ? 139  GLU A CG    1 
ATOM   1095 C CD    . GLU A 1 139 ? 57.50194 -20.21341 6.11632   1.000 61.17443 ? 139  GLU A CD    1 
ATOM   1096 O OE1   . GLU A 1 139 ? 58.51078 -19.49983 6.27108   1.000 63.82234 ? 139  GLU A OE1   1 
ATOM   1097 O OE2   . GLU A 1 139 ? 57.51786 -21.45131 6.24704   1.000 63.30484 ? 139  GLU A OE2   1 
ATOM   1098 N N     . GLY A 1 140 ? 52.35666 -20.44505 3.51101   1.000 37.39749 ? 140  GLY A N     1 
ATOM   1099 C CA    . GLY A 1 140 ? 51.47169 -21.17671 2.63126   1.000 33.73335 ? 140  GLY A CA    1 
ATOM   1100 C C     . GLY A 1 140 ? 50.43332 -20.28319 1.97569   1.000 36.09763 ? 140  GLY A C     1 
ATOM   1101 O O     . GLY A 1 140 ? 50.40337 -19.06667 2.15497   1.000 38.26316 ? 140  GLY A O     1 
ATOM   1102 N N     . GLY A 1 141 ? 49.56159 -20.91567 1.20256   1.000 28.30669 ? 141  GLY A N     1 
ATOM   1103 C CA    . GLY A 1 141 ? 48.51841 -20.18582 0.51273   1.000 29.06619 ? 141  GLY A CA    1 
ATOM   1104 C C     . GLY A 1 141 ? 47.78488 -21.08699 -0.45472  1.000 24.56730 ? 141  GLY A C     1 
ATOM   1105 O O     . GLY A 1 141 ? 48.14283 -22.25098 -0.65781  1.000 21.28017 ? 141  GLY A O     1 
ATOM   1106 N N     . GLY A 1 142 ? 46.74196 -20.51610 -1.05699  1.000 20.21930 ? 142  GLY A N     1 
ATOM   1107 C CA    . GLY A 1 142 ? 45.90384 -21.25092 -1.97392  1.000 16.99220 ? 142  GLY A CA    1 
ATOM   1108 C C     . GLY A 1 142 ? 45.75859 -20.52429 -3.29679  1.000 21.03476 ? 142  GLY A C     1 
ATOM   1109 O O     . GLY A 1 142 ? 45.95073 -19.31228 -3.39646  1.000 20.22035 ? 142  GLY A O     1 
ATOM   1110 N N     . VAL A 1 143 ? 45.40948 -21.30107 -4.32188  1.000 14.52841 ? 143  VAL A N     1 
ATOM   1111 C CA    . VAL A 1 143 ? 45.20341 -20.79656 -5.67336  1.000 17.15522 ? 143  VAL A CA    1 
ATOM   1112 C C     . VAL A 1 143 ? 44.06682 -21.58095 -6.31246  1.000 16.27880 ? 143  VAL A C     1 
ATOM   1113 O O     . VAL A 1 143 ? 43.83430 -22.75007 -5.98852  1.000 14.80041 ? 143  VAL A O     1 
ATOM   1114 C CB    . VAL A 1 143 ? 46.48435 -20.91158 -6.53246  1.000 21.92288 ? 143  VAL A CB    1 
ATOM   1115 C CG1   . VAL A 1 143 ? 46.86360 -22.37532 -6.72509  1.000 21.38384 ? 143  VAL A CG1   1 
ATOM   1116 C CG2   . VAL A 1 143 ? 46.30652 -20.21962 -7.88030  1.000 24.80645 ? 143  VAL A CG2   1 
ATOM   1117 N N     . ILE A 1 144 ? 43.34852 -20.92772 -7.21967  1.000 14.12695 ? 144  ILE A N     1 
ATOM   1118 C CA    . ILE A 1 144 ? 42.37692 -21.62474 -8.05193  1.000 14.66532 ? 144  ILE A CA    1 
ATOM   1119 C C     . ILE A 1 144 ? 43.09822 -22.25752 -9.23284  1.000 16.44432 ? 144  ILE A C     1 
ATOM   1120 O O     . ILE A 1 144 ? 43.84446 -21.58637 -9.95505  1.000 16.98687 ? 144  ILE A O     1 
ATOM   1121 C CB    . ILE A 1 144 ? 41.27519 -20.67035 -8.53572  1.000 13.86910 ? 144  ILE A CB    1 
ATOM   1122 C CG1   . ILE A 1 144 ? 40.52310 -20.05878 -7.35585  1.000 16.94454 ? 144  ILE A CG1   1 
ATOM   1123 C CG2   . ILE A 1 144 ? 40.31655 -21.40297 -9.46255  1.000 15.71316 ? 144  ILE A CG2   1 
ATOM   1124 C CD1   . ILE A 1 144 ? 39.60124 -18.93460 -7.76486  1.000 17.62548 ? 144  ILE A CD1   1 
ATOM   1125 N N     . GLN A 1 145 ? 42.87942 -23.55071 -9.43135  1.000 14.90582 ? 145  GLN A N     1 
ATOM   1126 C CA    . GLN A 1 145 ? 43.32385 -24.24552 -10.62670 1.000 14.47620 ? 145  GLN A CA    1 
ATOM   1127 C C     . GLN A 1 145 ? 42.12705 -24.53184 -11.52364 1.000 14.20398 ? 145  GLN A C     1 
ATOM   1128 O O     . GLN A 1 145 ? 40.97160 -24.47277 -11.09466 1.000 13.14464 ? 145  GLN A O     1 
ATOM   1129 C CB    . GLN A 1 145 ? 44.05401 -25.54592 -10.27145 1.000 15.21593 ? 145  GLN A CB    1 
ATOM   1130 C CG    . GLN A 1 145 ? 45.18692 -25.36800 -9.26730  1.000 13.91591 ? 145  GLN A CG    1 
ATOM   1131 C CD    . GLN A 1 145 ? 46.50451 -25.02661 -9.93675  1.000 23.03646 ? 145  GLN A CD    1 
ATOM   1132 O OE1   . GLN A 1 145 ? 46.59443 -24.97415 -11.16399 1.000 24.19712 ? 145  GLN A OE1   1 
ATOM   1133 N NE2   . GLN A 1 145 ? 47.53563 -24.79060 -9.13160  1.000 22.57072 ? 145  GLN A NE2   1 
ATOM   1134 N N     . GLY A 1 146 ? 42.41723 -24.82975 -12.79118 1.000 14.84962 ? 146  GLY A N     1 
ATOM   1135 C CA    . GLY A 1 146 ? 41.35447 -25.14640 -13.72716 1.000 15.21543 ? 146  GLY A CA    1 
ATOM   1136 C C     . GLY A 1 146 ? 40.67531 -26.47205 -13.46080 1.000 15.40232 ? 146  GLY A C     1 
ATOM   1137 O O     . GLY A 1 146 ? 39.51527 -26.65190 -13.84694 1.000 13.53403 ? 146  GLY A O     1 
ATOM   1138 N N     . SER A 1 147 ? 41.36351 -27.39595 -12.79784 1.000 11.11711 ? 147  SER A N     1 
ATOM   1139 C CA    . SER A 1 147 ? 40.84527 -28.73879 -12.58547 1.000 11.38921 ? 147  SER A CA    1 
ATOM   1140 C C     . SER A 1 147 ? 41.72403 -29.43899 -11.56218 1.000 12.66884 ? 147  SER A C     1 
ATOM   1141 O O     . SER A 1 147 ? 42.87044 -29.04315 -11.33062 1.000 13.80745 ? 147  SER A O     1 
ATOM   1142 C CB    . SER A 1 147 ? 40.80765 -29.53386 -13.89327 1.000 14.40104 ? 147  SER A CB    1 
ATOM   1143 O OG    . SER A 1 147 ? 42.12144 -29.81204 -14.34401 1.000 14.97622 ? 147  SER A OG    1 
ATOM   1144 N N     . ALA A 1 148 ? 41.16672 -30.48660 -10.94693 1.000 12.20223 ? 148  ALA A N     1 
ATOM   1145 C CA    . ALA A 1 148 ? 41.95810 -31.29969 -10.02985 1.000 11.54650 ? 148  ALA A CA    1 
ATOM   1146 C C     . ALA A 1 148 ? 43.07520 -32.02363 -10.76423 1.000 12.31766 ? 148  ALA A C     1 
ATOM   1147 O O     . ALA A 1 148 ? 44.14376 -32.26646 -10.18991 1.000 13.44222 ? 148  ALA A O     1 
ATOM   1148 C CB    . ALA A 1 148 ? 41.06418 -32.30222 -9.29936  1.000 11.58819 ? 148  ALA A CB    1 
ATOM   1149 N N     . SER A 1 149 ? 42.84354 -32.37648 -12.03135 1.000 13.97118 ? 149  SER A N     1 
ATOM   1150 C CA    . SER A 1 149 ? 43.89709 -32.97180 -12.84543 1.000 14.84518 ? 149  SER A CA    1 
ATOM   1151 C C     . SER A 1 149 ? 45.06899 -32.01975 -13.00439 1.000 14.80229 ? 149  SER A C     1 
ATOM   1152 O O     . SER A 1 149 ? 46.23118 -32.42835 -12.89269 1.000 15.23179 ? 149  SER A O     1 
ATOM   1153 C CB    . SER A 1 149 ? 43.34414 -33.35743 -14.21294 1.000 15.08460 ? 149  SER A CB    1 
ATOM   1154 O OG    . SER A 1 149 ? 42.33429 -34.33017 -14.06875 1.000 18.40922 ? 149  SER A OG    1 
ATOM   1155 N N     . GLU A 1 150 ? 44.78118 -30.74325 -13.27137 1.000 13.91157 ? 150  GLU A N     1 
ATOM   1156 C CA    . GLU A 1 150 ? 45.84454 -29.75074 -13.36799 1.000 14.14787 ? 150  GLU A CA    1 
ATOM   1157 C C     . GLU A 1 150 ? 46.53083 -29.55328 -12.02393 1.000 14.73413 ? 150  GLU A C     1 
ATOM   1158 O O     . GLU A 1 150 ? 47.75207 -29.36947 -11.96354 1.000 13.88371 ? 150  GLU A O     1 
ATOM   1159 C CB    . GLU A 1 150 ? 45.28108 -28.42784 -13.89418 1.000 15.82171 ? 150  GLU A CB    1 
ATOM   1160 C CG    . GLU A 1 150 ? 44.95356 -28.46413 -15.38221 1.000 23.09257 ? 150  GLU A CG    1 
ATOM   1161 C CD    . GLU A 1 150 ? 43.99458 -27.37832 -15.81373 1.000 24.55695 ? 150  GLU A CD    1 
ATOM   1162 O OE1   . GLU A 1 150 ? 44.48262 -26.30234 -16.21460 1.000 34.97589 ? 150  GLU A OE1   1 
ATOM   1163 O OE2   . GLU A 1 150 ? 42.76569 -27.59099 -15.74444 1.000 24.75871 ? 150  GLU A OE2   1 
ATOM   1164 N N     . ALA A 1 151 ? 45.76297 -29.60372 -10.93200 1.000 12.11608 ? 151  ALA A N     1 
ATOM   1165 C CA    . ALA A 1 151 ? 46.35121 -29.43637 -9.60696  1.000 14.12500 ? 151  ALA A CA    1 
ATOM   1166 C C     . ALA A 1 151 ? 47.31891 -30.56877 -9.28694  1.000 13.43042 ? 151  ALA A C     1 
ATOM   1167 O O     . ALA A 1 151 ? 48.39215 -30.33850 -8.71670  1.000 13.28944 ? 151  ALA A O     1 
ATOM   1168 C CB    . ALA A 1 151 ? 45.24836 -29.35497 -8.55202  1.000 11.29288 ? 151  ALA A CB    1 
ATOM   1169 N N     . THR A 1 152 ? 46.95806 -31.80068 -9.65224  1.000 12.05635 ? 152  THR A N     1 
ATOM   1170 C CA    . THR A 1 152 ? 47.84880 -32.93175 -9.41615  1.000 12.63010 ? 152  THR A CA    1 
ATOM   1171 C C     . THR A 1 152 ? 49.12739 -32.80160 -10.23706 1.000 12.21969 ? 152  THR A C     1 
ATOM   1172 O O     . THR A 1 152 ? 50.22157 -33.10500 -9.74652  1.000 12.38191 ? 152  THR A O     1 
ATOM   1173 C CB    . THR A 1 152 ? 47.12253 -34.23790 -9.73756  1.000 12.68011 ? 152  THR A CB    1 
ATOM   1174 O OG1   . THR A 1 152 ? 46.11172 -34.47317 -8.74979  1.000 11.92396 ? 152  THR A OG1   1 
ATOM   1175 C CG2   . THR A 1 152 ? 48.09220 -35.40826 -9.73241  1.000 14.46438 ? 152  THR A CG2   1 
ATOM   1176 N N     . LEU A 1 153 ? 49.00881 -32.33579 -11.48449 1.000 12.49005 ? 153  LEU A N     1 
ATOM   1177 C CA    . LEU A 1 153 ? 50.19125 -32.11109 -12.31111 1.000 13.18917 ? 153  LEU A CA    1 
ATOM   1178 C C     . LEU A 1 153 ? 51.08419 -31.02721 -11.72099 1.000 13.78280 ? 153  LEU A C     1 
ATOM   1179 O O     . LEU A 1 153 ? 52.31157 -31.17898 -11.68259 1.000 14.01159 ? 153  LEU A O     1 
ATOM   1180 C CB    . LEU A 1 153 ? 49.77705 -31.74294 -13.73389 1.000 13.54046 ? 153  LEU A CB    1 
ATOM   1181 C CG    . LEU A 1 153 ? 50.92698 -31.39594 -14.68537 1.000 14.73103 ? 153  LEU A CG    1 
ATOM   1182 C CD1   . LEU A 1 153 ? 51.88947 -32.56449 -14.82957 1.000 16.02553 ? 153  LEU A CD1   1 
ATOM   1183 C CD2   . LEU A 1 153 ? 50.39222 -30.97633 -16.04381 1.000 17.95064 ? 153  LEU A CD2   1 
ATOM   1184 N N     . VAL A 1 154 ? 50.48713 -29.92245 -11.26207 1.000 14.94360 ? 154  VAL A N     1 
ATOM   1185 C CA    . VAL A 1 154 ? 51.26930 -28.84712 -10.65556 1.000 14.13406 ? 154  VAL A CA    1 
ATOM   1186 C C     . VAL A 1 154 ? 52.04634 -29.36388 -9.45244  1.000 14.93987 ? 154  VAL A C     1 
ATOM   1187 O O     . VAL A 1 154 ? 53.22862 -29.04520 -9.27314  1.000 14.81910 ? 154  VAL A O     1 
ATOM   1188 C CB    . VAL A 1 154 ? 50.35359 -27.67079 -10.27024 1.000 15.68518 ? 154  VAL A CB    1 
ATOM   1189 C CG1   . VAL A 1 154 ? 51.09283 -26.70455 -9.36186  1.000 19.93395 ? 154  VAL A CG1   1 
ATOM   1190 C CG2   . VAL A 1 154 ? 49.85983 -26.95460 -11.51119 1.000 15.90452 ? 154  VAL A CG2   1 
ATOM   1191 N N     . ALA A 1 155 ? 51.39757 -30.17493 -8.61342  1.000 14.13658 ? 155  ALA A N     1 
ATOM   1192 C CA    . ALA A 1 155 ? 52.07019 -30.71416 -7.43607  1.000 14.63963 ? 155  ALA A CA    1 
ATOM   1193 C C     . ALA A 1 155 ? 53.19499 -31.66541 -7.82610  1.000 13.35417 ? 155  ALA A C     1 
ATOM   1194 O O     . ALA A 1 155 ? 54.26769 -31.65195 -7.20967  1.000 14.73462 ? 155  ALA A O     1 
ATOM   1195 C CB    . ALA A 1 155 ? 51.05775 -31.41614 -6.53097  1.000 14.51126 ? 155  ALA A CB    1 
ATOM   1196 N N     . LEU A 1 156 ? 52.97016 -32.49828 -8.84617  1.000 13.54608 ? 156  LEU A N     1 
ATOM   1197 C CA    . LEU A 1 156 ? 54.01741 -33.40966 -9.29791  1.000 13.18614 ? 156  LEU A CA    1 
ATOM   1198 C C     . LEU A 1 156 ? 55.21899 -32.64137 -9.83285  1.000 15.42031 ? 156  LEU A C     1 
ATOM   1199 O O     . LEU A 1 156 ? 56.36922 -32.98804 -9.53859  1.000 14.50162 ? 156  LEU A O     1 
ATOM   1200 C CB    . LEU A 1 156 ? 53.46710 -34.35621 -10.36695 1.000 13.86211 ? 156  LEU A CB    1 
ATOM   1201 C CG    . LEU A 1 156 ? 54.40512 -35.46656 -10.85240 1.000 15.29637 ? 156  LEU A CG    1 
ATOM   1202 C CD1   . LEU A 1 156 ? 53.64474 -36.77020 -11.04090 1.000 13.32653 ? 156  LEU A CD1   1 
ATOM   1203 C CD2   . LEU A 1 156 ? 55.11455 -35.06651 -12.14285 1.000 17.28401 ? 156  LEU A CD2   1 
ATOM   1204 N N     . LEU A 1 157 ? 54.97065 -31.59219 -10.62059 1.000 12.63176 ? 157  LEU A N     1 
ATOM   1205 C CA    . LEU A 1 157 ? 56.06766 -30.81122 -11.18274 1.000 15.36095 ? 157  LEU A CA    1 
ATOM   1206 C C     . LEU A 1 157 ? 56.84897 -30.08944 -10.09256 1.000 16.43768 ? 157  LEU A C     1 
ATOM   1207 O O     . LEU A 1 157 ? 58.08000 -29.99547 -10.16044 1.000 16.06427 ? 157  LEU A O     1 
ATOM   1208 C CB    . LEU A 1 157 ? 55.52557 -29.81764 -12.21128 1.000 14.62725 ? 157  LEU A CB    1 
ATOM   1209 C CG    . LEU A 1 157 ? 54.93089 -30.44763 -13.47210 1.000 15.99669 ? 157  LEU A CG    1 
ATOM   1210 C CD1   . LEU A 1 157 ? 54.29011 -29.39176 -14.35706 1.000 15.31894 ? 157  LEU A CD1   1 
ATOM   1211 C CD2   . LEU A 1 157 ? 55.99992 -31.21364 -14.23602 1.000 16.59487 ? 157  LEU A CD2   1 
ATOM   1212 N N     . ALA A 1 158 ? 56.15157 -29.56953 -9.08011  1.000 14.99622 ? 158  ALA A N     1 
ATOM   1213 C CA    . ALA A 1 158 ? 56.84214 -28.94748 -7.95602  1.000 16.09706 ? 158  ALA A CA    1 
ATOM   1214 C C     . ALA A 1 158 ? 57.67837 -29.96878 -7.19615  1.000 16.84080 ? 158  ALA A C     1 
ATOM   1215 O O     . ALA A 1 158 ? 58.82379 -29.69114 -6.82047  1.000 16.29999 ? 158  ALA A O     1 
ATOM   1216 C CB    . ALA A 1 158 ? 55.83081 -28.27591 -7.02678  1.000 18.15306 ? 158  ALA A CB    1 
ATOM   1217 N N     . ALA A 1 159 ? 57.12364 -31.16093 -6.96786  1.000 16.70770 ? 159  ALA A N     1 
ATOM   1218 C CA    . ALA A 1 159 ? 57.88250 -32.21821 -6.30768  1.000 15.37134 ? 159  ALA A CA    1 
ATOM   1219 C C     . ALA A 1 159 ? 59.08067 -32.64062 -7.14445  1.000 18.41396 ? 159  ALA A C     1 
ATOM   1220 O O     . ALA A 1 159 ? 60.15579 -32.93005 -6.60545  1.000 18.87057 ? 159  ALA A O     1 
ATOM   1221 C CB    . ALA A 1 159 ? 56.97815 -33.41883 -6.03677  1.000 14.48000 ? 159  ALA A CB    1 
ATOM   1222 N N     . ARG A 1 160 ? 58.90812 -32.69096 -8.46591  1.000 17.32335 ? 160  ARG A N     1 
ATOM   1223 C CA    . ARG A 1 160 ? 60.00265 -33.07307 -9.35068  1.000 18.33532 ? 160  ARG A CA    1 
ATOM   1224 C C     . ARG A 1 160 ? 61.14632 -32.06987 -9.27096  1.000 18.63432 ? 160  ARG A C     1 
ATOM   1225 O O     . ARG A 1 160 ? 62.31635 -32.45030 -9.14447  1.000 18.21871 ? 160  ARG A O     1 
ATOM   1226 C CB    . ARG A 1 160 ? 59.48709 -33.18809 -10.78411 1.000 16.60267 ? 160  ARG A CB    1 
ATOM   1227 C CG    . ARG A 1 160 ? 60.44111 -33.87722 -11.73068 1.000 19.88906 ? 160  ARG A CG    1 
ATOM   1228 C CD    . ARG A 1 160 ? 59.94846 -33.76955 -13.15964 1.000 21.75646 ? 160  ARG A CD    1 
ATOM   1229 N NE    . ARG A 1 160 ? 59.99619 -32.39281 -13.63754 1.000 18.44438 ? 160  ARG A NE    1 
ATOM   1230 C CZ    . ARG A 1 160 ? 59.62092 -32.00449 -14.84849 1.000 18.59568 ? 160  ARG A CZ    1 
ATOM   1231 N NH1   . ARG A 1 160 ? 59.14850 -32.86528 -15.73511 1.000 17.72660 ? 160  ARG A NH1   1 
ATOM   1232 N NH2   . ARG A 1 160 ? 59.72375 -30.72008 -15.17875 1.000 19.89382 ? 160  ARG A NH2   1 
ATOM   1233 N N     . THR A 1 161 ? 60.82226 -30.77576 -9.34192  1.000 18.79562 ? 161  THR A N     1 
ATOM   1234 C CA    . THR A 1 161 ? 61.85500 -29.74774 -9.26115  1.000 19.82466 ? 161  THR A CA    1 
ATOM   1235 C C     . THR A 1 161 ? 62.58579 -29.80309 -7.92641  1.000 21.46961 ? 161  THR A C     1 
ATOM   1236 O O     . THR A 1 161 ? 63.80651 -29.61406 -7.86873  1.000 21.98706 ? 161  THR A O     1 
ATOM   1237 C CB    . THR A 1 161 ? 61.23771 -28.36465 -9.47022  1.000 21.68194 ? 161  THR A CB    1 
ATOM   1238 O OG1   . THR A 1 161 ? 60.46589 -28.35857 -10.67740 1.000 23.00942 ? 161  THR A OG1   1 
ATOM   1239 C CG2   . THR A 1 161 ? 62.32508 -27.30416 -9.56374  1.000 26.45946 ? 161  THR A CG2   1 
ATOM   1240 N N     . LYS A 1 162 ? 61.85698 -30.07228 -6.84198  1.000 19.01726 ? 162  LYS A N     1 
ATOM   1241 C CA    . LYS A 1 162 ? 62.47919 -30.06828 -5.52268  1.000 22.08097 ? 162  LYS A CA    1 
ATOM   1242 C C     . LYS A 1 162 ? 63.43182 -31.24510 -5.34792  1.000 22.25830 ? 162  LYS A C     1 
ATOM   1243 O O     . LYS A 1 162 ? 64.52695 -31.08363 -4.79649  1.000 20.62782 ? 162  LYS A O     1 
ATOM   1244 C CB    . LYS A 1 162 ? 61.40668 -30.07891 -4.43433  1.000 23.10189 ? 162  LYS A CB    1 
ATOM   1245 C CG    . LYS A 1 162 ? 61.95755 -29.87491 -3.03096  1.000 26.98951 ? 162  LYS A CG    1 
ATOM   1246 C CD    . LYS A 1 162 ? 60.83977 -29.71333 -2.01462  1.000 30.64720 ? 162  LYS A CD    1 
ATOM   1247 C CE    . LYS A 1 162 ? 61.37503 -29.77432 -0.59330  1.000 34.73614 ? 162  LYS A CE    1 
ATOM   1248 N NZ    . LYS A 1 162 ? 60.31037 -29.51387 0.41603   1.000 43.54537 ? 162  LYS A NZ    1 
ATOM   1249 N N     . VAL A 1 163 ? 63.04018 -32.43543 -5.81031  1.000 20.32170 ? 163  VAL A N     1 
ATOM   1250 C CA    . VAL A 1 163 ? 63.89242 -33.60094 -5.60037  1.000 19.87483 ? 163  VAL A CA    1 
ATOM   1251 C C     . VAL A 1 163 ? 65.12198 -33.54582 -6.50011  1.000 22.77594 ? 163  VAL A C     1 
ATOM   1252 O O     . VAL A 1 163 ? 66.20273 -33.99961 -6.10595  1.000 22.08387 ? 163  VAL A O     1 
ATOM   1253 C CB    . VAL A 1 163 ? 63.09262 -34.90336 -5.79531  1.000 21.93738 ? 163  VAL A CB    1 
ATOM   1254 C CG1   . VAL A 1 163 ? 62.64075 -35.06154 -7.23875  1.000 20.26466 ? 163  VAL A CG1   1 
ATOM   1255 C CG2   . VAL A 1 163 ? 63.92028 -36.10348 -5.35757  1.000 22.44545 ? 163  VAL A CG2   1 
ATOM   1256 N N     . ILE A 1 164 ? 64.99497 -32.98248 -7.70542  1.000 21.95002 ? 164  ILE A N     1 
ATOM   1257 C CA    . ILE A 1 164 ? 66.16260 -32.81488 -8.56903  1.000 23.21758 ? 164  ILE A CA    1 
ATOM   1258 C C     . ILE A 1 164 ? 67.17806 -31.89879 -7.90295  1.000 21.89574 ? 164  ILE A C     1 
ATOM   1259 O O     . ILE A 1 164 ? 68.37819 -32.19451 -7.85682  1.000 22.88403 ? 164  ILE A O     1 
ATOM   1260 C CB    . ILE A 1 164 ? 65.74886 -32.26075 -9.94283  1.000 23.99548 ? 164  ILE A CB    1 
ATOM   1261 C CG1   . ILE A 1 164 ? 64.97889 -33.29613 -10.75180 1.000 23.07230 ? 164  ILE A CG1   1 
ATOM   1262 C CG2   . ILE A 1 164 ? 66.97473 -31.80734 -10.72236 1.000 24.78444 ? 164  ILE A CG2   1 
ATOM   1263 C CD1   . ILE A 1 164 ? 64.17798 -32.65870 -11.85751 1.000 25.67601 ? 164  ILE A CD1   1 
ATOM   1264 N N     . HIS A 1 165 ? 66.70575 -30.76361 -7.38478  1.000 21.40006 ? 165  HIS A N     1 
ATOM   1265 C CA    . HIS A 1 165 ? 67.59946 -29.81041 -6.73891  1.000 24.91124 ? 165  HIS A CA    1 
ATOM   1266 C C     . HIS A 1 165 ? 68.23515 -30.41069 -5.49189  1.000 22.75645 ? 165  HIS A C     1 
ATOM   1267 O O     . HIS A 1 165 ? 69.41635 -30.17297 -5.21275  1.000 22.83607 ? 165  HIS A O     1 
ATOM   1268 C CB    . HIS A 1 165 ? 66.83449 -28.53315 -6.39301  1.000 25.12733 ? 165  HIS A CB    1 
ATOM   1269 C CG    . HIS A 1 165 ? 66.62068 -27.61901 -7.55996  1.000 35.21963 ? 165  HIS A CG    1 
ATOM   1270 N ND1   . HIS A 1 165 ? 65.67855 -26.61277 -7.55353  1.000 39.70282 ? 165  HIS A ND1   1 
ATOM   1271 C CD2   . HIS A 1 165 ? 67.23214 -27.55312 -8.76645  1.000 37.28522 ? 165  HIS A CD2   1 
ATOM   1272 C CE1   . HIS A 1 165 ? 65.71591 -25.96924 -8.70672  1.000 35.06298 ? 165  HIS A CE1   1 
ATOM   1273 N NE2   . HIS A 1 165 ? 66.64942 -26.52065 -9.46107  1.000 40.94854 ? 165  HIS A NE2   1 
ATOM   1274 N N     . ARG A 1 166 ? 67.46833 -31.19480 -4.73013  1.000 21.95804 ? 166  ARG A N     1 
ATOM   1275 C CA    . ARG A 1 166 ? 68.02356 -31.84303 -3.54614  1.000 21.98983 ? 166  ARG A CA    1 
ATOM   1276 C C     . ARG A 1 166 ? 69.10175 -32.84830 -3.92897  1.000 23.86378 ? 166  ARG A C     1 
ATOM   1277 O O     . ARG A 1 166 ? 70.19153 -32.86325 -3.34458  1.000 23.53725 ? 166  ARG A O     1 
ATOM   1278 C CB    . ARG A 1 166 ? 66.91562 -32.53001 -2.74580  1.000 22.39442 ? 166  ARG A CB    1 
ATOM   1279 C CG    . ARG A 1 166 ? 67.45071 -33.42560 -1.63482  1.000 22.92407 ? 166  ARG A CG    1 
ATOM   1280 C CD    . ARG A 1 166 ? 66.40424 -33.74807 -0.57851  1.000 24.32606 ? 166  ARG A CD    1 
ATOM   1281 N NE    . ARG A 1 166 ? 65.16826 -34.26928 -1.14886  1.000 29.16052 ? 166  ARG A NE    1 
ATOM   1282 C CZ    . ARG A 1 166 ? 64.94889 -35.54963 -1.41667  1.000 26.90056 ? 166  ARG A CZ    1 
ATOM   1283 N NH1   . ARG A 1 166 ? 65.87564 -36.47001 -1.20261  1.000 26.54750 ? 166  ARG A NH1   1 
ATOM   1284 N NH2   . ARG A 1 166 ? 63.77079 -35.91582 -1.91331  1.000 24.32011 ? 166  ARG A NH2   1 
ATOM   1285 N N     . LEU A 1 167 ? 68.81191 -33.70063 -4.91511  1.000 22.91634 ? 167  LEU A N     1 
ATOM   1286 C CA    . LEU A 1 167 ? 69.76382 -34.73314 -5.30771  1.000 24.65008 ? 167  LEU A CA    1 
ATOM   1287 C C     . LEU A 1 167 ? 70.99962 -34.13761 -5.96844  1.000 24.94525 ? 167  LEU A C     1 
ATOM   1288 O O     . LEU A 1 167 ? 72.10607 -34.66190 -5.79528  1.000 24.97568 ? 167  LEU A O     1 
ATOM   1289 C CB    . LEU A 1 167 ? 69.09062 -35.73501 -6.24393  1.000 26.10802 ? 167  LEU A CB    1 
ATOM   1290 C CG    . LEU A 1 167 ? 67.97945 -36.57725 -5.61256  1.000 28.88889 ? 167  LEU A CG    1 
ATOM   1291 C CD1   . LEU A 1 167 ? 67.48211 -37.63694 -6.57715  1.000 29.46536 ? 167  LEU A CD1   1 
ATOM   1292 C CD2   . LEU A 1 167 ? 68.44573 -37.20723 -4.31944  1.000 25.83409 ? 167  LEU A CD2   1 
ATOM   1293 N N     . GLN A 1 168 ? 70.83430 -33.04901 -6.72461  1.000 24.91116 ? 168  GLN A N     1 
ATOM   1294 C CA    . GLN A 1 168 ? 71.98491 -32.39808 -7.34104  1.000 27.54043 ? 168  GLN A CA    1 
ATOM   1295 C C     . GLN A 1 168 ? 72.82285 -31.65001 -6.31316  1.000 29.49614 ? 168  GLN A C     1 
ATOM   1296 O O     . GLN A 1 168 ? 74.03309 -31.48834 -6.50284  1.000 32.66563 ? 168  GLN A O     1 
ATOM   1297 C CB    . GLN A 1 168 ? 71.52429 -31.45195 -8.44993  1.000 27.42983 ? 168  GLN A CB    1 
ATOM   1298 C CG    . GLN A 1 168 ? 71.19486 -32.16323 -9.75283  1.000 28.83526 ? 168  GLN A CG    1 
ATOM   1299 C CD    . GLN A 1 168 ? 70.78090 -31.21272 -10.85805 1.000 29.64954 ? 168  GLN A CD    1 
ATOM   1300 O OE1   . GLN A 1 168 ? 70.21861 -30.14794 -10.60263 1.000 28.89345 ? 168  GLN A OE1   1 
ATOM   1301 N NE2   . GLN A 1 168 ? 71.06064 -31.59520 -12.09891 1.000 34.37575 ? 168  GLN A NE2   1 
ATOM   1302 N N     . ALA A 1 169 ? 72.20477 -31.18535 -5.22600  1.000 26.30215 ? 169  ALA A N     1 
ATOM   1303 C CA    . ALA A 1 169 ? 72.97906 -30.57993 -4.14842  1.000 26.93514 ? 169  ALA A CA    1 
ATOM   1304 C C     . ALA A 1 169 ? 73.79156 -31.63025 -3.40338  1.000 29.26480 ? 169  ALA A C     1 
ATOM   1305 O O     . ALA A 1 169 ? 74.92920 -31.36960 -2.99461  1.000 28.05413 ? 169  ALA A O     1 
ATOM   1306 C CB    . ALA A 1 169 ? 72.05308 -29.83472 -3.18806  1.000 25.52305 ? 169  ALA A CB    1 
ATOM   1307 N N     . ALA A 1 170 ? 73.22766 -32.82747 -3.22677  1.000 29.33728 ? 170  ALA A N     1 
ATOM   1308 C CA    . ALA A 1 170 ? 73.94232 -33.88349 -2.51756  1.000 28.01100 ? 170  ALA A CA    1 
ATOM   1309 C C     . ALA A 1 170 ? 75.06963 -34.45523 -3.36865  1.000 30.81251 ? 170  ALA A C     1 
ATOM   1310 O O     . ALA A 1 170 ? 76.16105 -34.73466 -2.85843  1.000 30.23818 ? 170  ALA A O     1 
ATOM   1311 C CB    . ALA A 1 170 ? 72.96831 -34.98665 -2.10063  1.000 25.14856 ? 170  ALA A CB    1 
ATOM   1312 N N     . SER A 1 171 ? 74.82703 -34.63257 -4.66748  1.000 31.34308 ? 171  SER A N     1 
ATOM   1313 C CA    . SER A 1 171 ? 75.81900 -35.16760 -5.60017  1.000 38.56197 ? 171  SER A CA    1 
ATOM   1314 C C     . SER A 1 171 ? 75.81220 -34.29279 -6.84386  1.000 37.74163 ? 171  SER A C     1 
ATOM   1315 O O     . SER A 1 171 ? 75.02156 -34.51876 -7.77166  1.000 41.97495 ? 171  SER A O     1 
ATOM   1316 C CB    . SER A 1 171 ? 75.53131 -36.62709 -5.94935  1.000 37.15891 ? 171  SER A CB    1 
ATOM   1317 O OG    . SER A 1 171 ? 75.32944 -37.39845 -4.78144  1.000 36.75172 ? 171  SER A OG    1 
ATOM   1318 N N     . PRO A 1 172 ? 76.69875 -33.29246 -6.90923  1.000 44.08042 ? 172  PRO A N     1 
ATOM   1319 C CA    . PRO A 1 172 ? 76.67420 -32.35614 -8.03915  1.000 44.37639 ? 172  PRO A CA    1 
ATOM   1320 C C     . PRO A 1 172 ? 77.11085 -33.00226 -9.34380  1.000 51.08049 ? 172  PRO A C     1 
ATOM   1321 O O     . PRO A 1 172 ? 77.14417 -32.34692 -10.38994 1.000 51.59849 ? 172  PRO A O     1 
ATOM   1322 C CB    . PRO A 1 172 ? 77.65076 -31.25599 -7.60019  1.000 44.26177 ? 172  PRO A CB    1 
ATOM   1323 C CG    . PRO A 1 172 ? 77.78779 -31.42953 -6.10810  1.000 39.92509 ? 172  PRO A CG    1 
ATOM   1324 C CD    . PRO A 1 172 ? 77.69537 -32.90211 -5.89981  1.000 43.04538 ? 172  PRO A CD    1 
ATOM   1325 N N     . GLU A 1 173 ? 77.44774 -34.28659 -9.29459  1.000 67.41958 ? 173  GLU A N     1 
ATOM   1326 C CA    . GLU A 1 173 ? 77.85467 -35.02693 -10.47878 1.000 66.59908 ? 173  GLU A CA    1 
ATOM   1327 C C     . GLU A 1 173 ? 76.66956 -35.59859 -11.24855 1.000 70.98587 ? 173  GLU A C     1 
ATOM   1328 O O     . GLU A 1 173 ? 76.86510 -36.44718 -12.12535 1.000 75.22670 ? 173  GLU A O     1 
ATOM   1329 C CB    . GLU A 1 173 ? 78.80221 -36.16364 -10.08551 1.000 68.19926 ? 173  GLU A CB    1 
ATOM   1330 C CG    . GLU A 1 173 ? 80.05547 -35.69712 -9.37067  1.000 76.83522 ? 173  GLU A CG    1 
ATOM   1331 C CD    . GLU A 1 173 ? 79.98677 -35.95048 -7.87673  1.000 77.26526 ? 173  GLU A CD    1 
ATOM   1332 O OE1   . GLU A 1 173 ? 78.87437 -36.20189 -7.36500  1.000 70.32598 ? 173  GLU A OE1   1 
ATOM   1333 O OE2   . GLU A 1 173 ? 81.04442 -35.89784 -7.21199  1.000 81.28346 ? 173  GLU A OE2   1 
ATOM   1334 N N     . LEU A 1 174 ? 75.45276 -35.15775 -10.94610 1.000 56.25220 ? 174  LEU A N     1 
ATOM   1335 C CA    . LEU A 1 174 ? 74.24000 -35.78923 -11.44587 1.000 48.62324 ? 174  LEU A CA    1 
ATOM   1336 C C     . LEU A 1 174 ? 73.51705 -34.85478 -12.40345 1.000 47.54787 ? 174  LEU A C     1 
ATOM   1337 O O     . LEU A 1 174 ? 73.29487 -33.68186 -12.08499 1.000 47.40890 ? 174  LEU A O     1 
ATOM   1338 C CB    . LEU A 1 174 ? 73.31726 -36.17067 -10.28667 1.000 47.72308 ? 174  LEU A CB    1 
ATOM   1339 C CG    . LEU A 1 174 ? 73.18980 -37.65434 -9.94427  1.000 46.88941 ? 174  LEU A CG    1 
ATOM   1340 C CD1   . LEU A 1 174 ? 74.56032 -38.26220 -9.70240  1.000 55.06304 ? 174  LEU A CD1   1 
ATOM   1341 C CD2   . LEU A 1 174 ? 72.30078 -37.83376 -8.72717  1.000 43.07125 ? 174  LEU A CD2   1 
ATOM   1342 N N     . THR A 1 175 ? 73.14879 -35.37840 -13.56824 1.000 41.04800 ? 175  THR A N     1 
ATOM   1343 C CA    . THR A 1 175 ? 72.29751 -34.63623 -14.48089 1.000 43.99741 ? 175  THR A CA    1 
ATOM   1344 C C     . THR A 1 175 ? 70.83909 -34.76894 -14.05628 1.000 42.05155 ? 175  THR A C     1 
ATOM   1345 O O     . THR A 1 175 ? 70.46911 -35.66158 -13.28833 1.000 44.60108 ? 175  THR A O     1 
ATOM   1346 C CB    . THR A 1 175 ? 72.46261 -35.13745 -15.91576 1.000 44.50053 ? 175  THR A CB    1 
ATOM   1347 O OG1   . THR A 1 175 ? 71.61371 -36.27303 -16.12682 1.000 42.85589 ? 175  THR A OG1   1 
ATOM   1348 C CG2   . THR A 1 175 ? 73.90530 -35.54001 -16.17117 1.000 46.64693 ? 175  THR A CG2   1 
ATOM   1349 N N     . GLN A 1 176 ? 70.00559 -33.85583 -14.56303 1.000 41.87606 ? 176  GLN A N     1 
ATOM   1350 C CA    . GLN A 1 176 ? 68.57164 -33.96337 -14.31723 1.000 39.99136 ? 176  GLN A CA    1 
ATOM   1351 C C     . GLN A 1 176 ? 68.02775 -35.28251 -14.85054 1.000 47.03257 ? 176  GLN A C     1 
ATOM   1352 O O     . GLN A 1 176 ? 67.24743 -35.95824 -14.16976 1.000 40.40863 ? 176  GLN A O     1 
ATOM   1353 C CB    . GLN A 1 176 ? 67.83185 -32.77893 -14.94591 1.000 42.52729 ? 176  GLN A CB    1 
ATOM   1354 C CG    . GLN A 1 176 ? 66.31952 -32.96966 -15.06248 1.000 40.21481 ? 176  GLN A CG    1 
ATOM   1355 C CD    . GLN A 1 176 ? 65.56577 -31.65555 -15.19271 1.000 42.65062 ? 176  GLN A CD    1 
ATOM   1356 O OE1   . GLN A 1 176 ? 65.93876 -30.65134 -14.58633 1.000 37.53969 ? 176  GLN A OE1   1 
ATOM   1357 N NE2   . GLN A 1 176 ? 64.49198 -31.66110 -15.97723 1.000 40.37377 ? 176  GLN A NE2   1 
ATOM   1358 N N     . ALA A 1 177 ? 68.45733 -35.68196 -16.05212 1.000 58.46656 ? 177  ALA A N     1 
ATOM   1359 C CA    . ALA A 1 177 ? 67.92004 -36.89116 -16.66722 1.000 58.66265 ? 177  ALA A CA    1 
ATOM   1360 C C     . ALA A 1 177 ? 68.35038 -38.14313 -15.91192 1.000 55.00501 ? 177  ALA A C     1 
ATOM   1361 O O     . ALA A 1 177 ? 67.59375 -39.11824 -15.83768 1.000 57.48459 ? 177  ALA A O     1 
ATOM   1362 C CB    . ALA A 1 177 ? 68.35660 -36.97363 -18.13123 1.000 60.64163 ? 177  ALA A CB    1 
ATOM   1363 N N     . ALA A 1 178 ? 69.56508 -38.14433 -15.35625 1.000 42.85181 ? 178  ALA A N     1 
ATOM   1364 C CA    . ALA A 1 178 ? 70.00554 -39.29340 -14.57382 1.000 39.98928 ? 178  ALA A CA    1 
ATOM   1365 C C     . ALA A 1 178 ? 69.13395 -39.48784 -13.33950 1.000 39.21257 ? 178  ALA A C     1 
ATOM   1366 O O     . ALA A 1 178 ? 68.89879 -40.62556 -12.91727 1.000 38.21659 ? 178  ALA A O     1 
ATOM   1367 C CB    . ALA A 1 178 ? 71.47608 -39.13029 -14.18588 1.000 43.29000 ? 178  ALA A CB    1 
ATOM   1368 N N     . ILE A 1 179 ? 68.64757 -38.39299 -12.75181 1.000 36.46603 ? 179  ILE A N     1 
ATOM   1369 C CA    . ILE A 1 179 ? 67.69817 -38.49126 -11.64800 1.000 32.60771 ? 179  ILE A CA    1 
ATOM   1370 C C     . ILE A 1 179 ? 66.33070 -38.92330 -12.16572 1.000 33.26480 ? 179  ILE A C     1 
ATOM   1371 O O     . ILE A 1 179 ? 65.60901 -39.68052 -11.50218 1.000 25.90185 ? 179  ILE A O     1 
ATOM   1372 C CB    . ILE A 1 179 ? 67.62750 -37.14688 -10.89765 1.000 31.52211 ? 179  ILE A CB    1 
ATOM   1373 C CG1   . ILE A 1 179 ? 68.92914 -36.90057 -10.12887 1.000 32.24082 ? 179  ILE A CG1   1 
ATOM   1374 C CG2   . ILE A 1 179 ? 66.41878 -37.10338 -9.97303  1.000 28.57538 ? 179  ILE A CG2   1 
ATOM   1375 C CD1   . ILE A 1 179 ? 69.27737 -35.43964 -9.96382  1.000 32.31893 ? 179  ILE A CD1   1 
ATOM   1376 N N     . MET A 1 180 ? 65.97977 -38.48106 -13.37900 1.000 33.54769 ? 180  MET A N     1 
ATOM   1377 C CA    A MET A 1 180 ? 64.66888 -38.76632 -13.95873 0.119 34.08566 ? 180  MET A CA    1 
ATOM   1378 C CA    B MET A 1 180 ? 64.65795 -38.76243 -13.93105 0.881 34.03554 ? 180  MET A CA    1 
ATOM   1379 C C     . MET A 1 180 ? 64.39194 -40.25950 -14.03917 1.000 32.65707 ? 180  MET A C     1 
ATOM   1380 O O     . MET A 1 180 ? 63.31087 -40.72931 -13.66574 1.000 32.17364 ? 180  MET A O     1 
ATOM   1381 C CB    A MET A 1 180 ? 64.57884 -38.13302 -15.34867 0.119 39.15877 ? 180  MET A CB    1 
ATOM   1382 C CB    B MET A 1 180 ? 64.51126 -38.09466 -15.29533 0.881 39.21726 ? 180  MET A CB    1 
ATOM   1383 C CG    A MET A 1 180 ? 64.34562 -36.64072 -15.34780 0.119 38.33104 ? 180  MET A CG    1 
ATOM   1384 C CG    B MET A 1 180 ? 64.48027 -36.59015 -15.23630 0.881 38.22118 ? 180  MET A CG    1 
ATOM   1385 S SD    A MET A 1 180 ? 62.72015 -36.24062 -14.68670 0.119 33.85633 ? 180  MET A SD    1 
ATOM   1386 S SD    B MET A 1 180 ? 63.05531 -35.96703 -14.33486 0.881 34.28701 ? 180  MET A SD    1 
ATOM   1387 C CE    A MET A 1 180 ? 63.14820 -35.71117 -13.04102 0.119 31.86602 ? 180  MET A CE    1 
ATOM   1388 C CE    B MET A 1 180 ? 62.50221 -34.68109 -15.45725 0.881 32.59898 ? 180  MET A CE    1 
ATOM   1389 N N     . GLU A 1 181 ? 65.35522 -41.02413 -14.55319 1.000 33.67939 ? 181  GLU A N     1 
ATOM   1390 C CA    . GLU A 1 181 ? 65.11070 -42.45102 -14.73898 1.000 36.07559 ? 181  GLU A CA    1 
ATOM   1391 C C     . GLU A 1 181 ? 65.00549 -43.21762 -13.42575 1.000 29.53563 ? 181  GLU A C     1 
ATOM   1392 O O     . GLU A 1 181 ? 64.65079 -44.40214 -13.44782 1.000 30.96343 ? 181  GLU A O     1 
ATOM   1393 C CB    . GLU A 1 181 ? 66.19611 -43.06889 -15.62652 1.000 40.52073 ? 181  GLU A CB    1 
ATOM   1394 C CG    . GLU A 1 181 ? 67.58298 -43.11089 -15.01735 1.000 42.30154 ? 181  GLU A CG    1 
ATOM   1395 C CD    . GLU A 1 181 ? 68.62512 -43.56045 -16.02124 1.000 49.04730 ? 181  GLU A CD    1 
ATOM   1396 O OE1   . GLU A 1 181 ? 68.23161 -44.01637 -17.11579 1.000 45.67350 ? 181  GLU A OE1   1 
ATOM   1397 O OE2   . GLU A 1 181 ? 69.83220 -43.46837 -15.71601 1.000 53.40432 ? 181  GLU A OE2   1 
ATOM   1398 N N     . LYS A 1 182 ? 65.28259 -42.57633 -12.29152 1.000 25.89770 ? 182  LYS A N     1 
ATOM   1399 C CA    . LYS A 1 182 ? 65.13122 -43.21331 -10.98948 1.000 25.62303 ? 182  LYS A CA    1 
ATOM   1400 C C     . LYS A 1 182 ? 63.86929 -42.80388 -10.24339 1.000 22.71824 ? 182  LYS A C     1 
ATOM   1401 O O     . LYS A 1 182 ? 63.40632 -43.56873 -9.39017  1.000 20.98045 ? 182  LYS A O     1 
ATOM   1402 C CB    . LYS A 1 182 ? 66.34895 -42.91698 -10.10281 1.000 24.82809 ? 182  LYS A CB    1 
ATOM   1403 C CG    . LYS A 1 182 ? 67.65191 -43.56248 -10.55511 1.000 27.99944 ? 182  LYS A CG    1 
ATOM   1404 C CD    . LYS A 1 182 ? 67.39744 -44.82891 -11.34728 1.000 35.39220 ? 182  LYS A CD    1 
ATOM   1405 C CE    . LYS A 1 182 ? 68.69367 -45.49404 -11.72028 1.000 43.15173 ? 182  LYS A CE    1 
ATOM   1406 N NZ    . LYS A 1 182 ? 68.51714 -46.96694 -11.71425 1.000 43.20444 ? 182  LYS A NZ    1 
ATOM   1407 N N     . LEU A 1 183 ? 63.30088 -41.63819 -10.54031 1.000 19.22793 ? 183  LEU A N     1 
ATOM   1408 C CA    . LEU A 1 183 ? 62.16311 -41.14925 -9.77339  1.000 20.34605 ? 183  LEU A CA    1 
ATOM   1409 C C     . LEU A 1 183 ? 60.94851 -42.04877 -9.95413  1.000 19.52946 ? 183  LEU A C     1 
ATOM   1410 O O     . LEU A 1 183 ? 60.68262 -42.55213 -11.04888 1.000 18.63907 ? 183  LEU A O     1 
ATOM   1411 C CB    . LEU A 1 183 ? 61.80347 -39.72574 -10.19142 1.000 16.33018 ? 183  LEU A CB    1 
ATOM   1412 C CG    . LEU A 1 183 ? 62.80206 -38.61863 -9.86392  1.000 20.69698 ? 183  LEU A CG    1 
ATOM   1413 C CD1   . LEU A 1 183 ? 62.14506 -37.27705 -10.10411 1.000 20.33635 ? 183  LEU A CD1   1 
ATOM   1414 C CD2   . LEU A 1 183 ? 63.31346 -38.72741 -8.43496  1.000 20.89791 ? 183  LEU A CD2   1 
ATOM   1415 N N     . VAL A 1 184 ? 60.20364 -42.24243 -8.86976  1.000 17.22193 ? 184  VAL A N     1 
ATOM   1416 C CA    . VAL A 1 184 ? 58.94790 -42.98067 -8.91006  1.000 17.87634 ? 184  VAL A CA    1 
ATOM   1417 C C     . VAL A 1 184 ? 57.92091 -42.24031 -8.06424  1.000 16.28693 ? 184  VAL A C     1 
ATOM   1418 O O     . VAL A 1 184 ? 58.22997 -41.74537 -6.97460  1.000 16.01831 ? 184  VAL A O     1 
ATOM   1419 C CB    . VAL A 1 184 ? 59.12236 -44.44398 -8.44083  1.000 19.32822 ? 184  VAL A CB    1 
ATOM   1420 C CG1   . VAL A 1 184 ? 59.51281 -44.51411 -6.96700  1.000 19.76837 ? 184  VAL A CG1   1 
ATOM   1421 C CG2   . VAL A 1 184 ? 57.85397 -45.23988 -8.70304  1.000 18.02428 ? 184  VAL A CG2   1 
ATOM   1422 N N     . ALA A 1 185 ? 56.70792 -42.12859 -8.59319  1.000 15.07310 ? 185  ALA A N     1 
ATOM   1423 C CA    . ALA A 1 185 ? 55.57229 -41.57090 -7.88063  1.000 14.61135 ? 185  ALA A CA    1 
ATOM   1424 C C     . ALA A 1 185 ? 54.62154 -42.69604 -7.49809  1.000 14.63798 ? 185  ALA A C     1 
ATOM   1425 O O     . ALA A 1 185 ? 54.63732 -43.77836 -8.09101  1.000 15.66536 ? 185  ALA A O     1 
ATOM   1426 C CB    . ALA A 1 185 ? 54.84397 -40.52378 -8.73137  1.000 15.00545 ? 185  ALA A CB    1 
ATOM   1427 N N     . TYR A 1 186 ? 53.79009 -42.43246 -6.49359  1.000 14.41357 ? 186  TYR A N     1 
ATOM   1428 C CA    . TYR A 1 186 ? 52.87727 -43.43578 -5.97075  1.000 14.48222 ? 186  TYR A CA    1 
ATOM   1429 C C     . TYR A 1 186 ? 51.45289 -42.90793 -5.92017  1.000 13.96472 ? 186  TYR A C     1 
ATOM   1430 O O     . TYR A 1 186 ? 51.21508 -41.70462 -5.78490  1.000 13.60378 ? 186  TYR A O     1 
ATOM   1431 C CB    . TYR A 1 186 ? 53.27276 -43.90249 -4.56368  1.000 14.89058 ? 186  TYR A CB    1 
ATOM   1432 C CG    . TYR A 1 186 ? 54.56153 -44.68447 -4.49037  1.000 16.80586 ? 186  TYR A CG    1 
ATOM   1433 C CD1   . TYR A 1 186 ? 54.70665 -45.88570 -5.17133  1.000 18.45075 ? 186  TYR A CD1   1 
ATOM   1434 C CD2   . TYR A 1 186 ? 55.62545 -44.23309 -3.72207  1.000 22.17595 ? 186  TYR A CD2   1 
ATOM   1435 C CE1   . TYR A 1 186 ? 55.88160 -46.60848 -5.09996  1.000 17.68145 ? 186  TYR A CE1   1 
ATOM   1436 C CE2   . TYR A 1 186 ? 56.80249 -44.94806 -3.64374  1.000 24.90856 ? 186  TYR A CE2   1 
ATOM   1437 C CZ    . TYR A 1 186 ? 56.92535 -46.13475 -4.33357  1.000 21.46675 ? 186  TYR A CZ    1 
ATOM   1438 O OH    . TYR A 1 186 ? 58.09907 -46.84793 -4.25641  1.000 22.56678 ? 186  TYR A OH    1 
ATOM   1439 N N     A SER A 1 187 ? 50.50638 -43.83480 -6.03883  0.652 14.43714 ? 187  SER A N     1 
ATOM   1440 N N     B SER A 1 187 ? 50.50677 -43.83499 -6.02377  0.348 14.46367 ? 187  SER A N     1 
ATOM   1441 C CA    A SER A 1 187 ? 49.09127 -43.54888 -5.85156  0.652 14.19099 ? 187  SER A CA    1 
ATOM   1442 C CA    B SER A 1 187 ? 49.09351 -43.54186 -5.84072  0.348 14.04285 ? 187  SER A CA    1 
ATOM   1443 C C     A SER A 1 187 ? 48.39780 -44.85762 -5.50640  0.652 15.20385 ? 187  SER A C     1 
ATOM   1444 C C     B SER A 1 187 ? 48.39191 -44.85460 -5.52775  0.348 14.87486 ? 187  SER A C     1 
ATOM   1445 O O     A SER A 1 187 ? 48.98971 -45.93603 -5.58560  0.652 15.51664 ? 187  SER A O     1 
ATOM   1446 O O     B SER A 1 187 ? 48.97540 -45.93430 -5.64511  0.348 15.82883 ? 187  SER A O     1 
ATOM   1447 C CB    A SER A 1 187 ? 48.46857 -42.90412 -7.09560  0.652 14.77409 ? 187  SER A CB    1 
ATOM   1448 C CB    B SER A 1 187 ? 48.49323 -42.86283 -7.07643  0.348 14.73151 ? 187  SER A CB    1 
ATOM   1449 O OG    A SER A 1 187 ? 48.27793 -43.85570 -8.12802  0.652 15.30633 ? 187  SER A OG    1 
ATOM   1450 O OG    B SER A 1 187 ? 47.48429 -41.93925 -6.70833  0.348 13.88660 ? 187  SER A OG    1 
ATOM   1451 N N     . SER A 1 188 ? 47.13432 -44.75019 -5.11168  1.000 14.58542 ? 188  SER A N     1 
ATOM   1452 C CA    . SER A 1 188 ? 46.35880 -45.94517 -4.82904  1.000 14.22829 ? 188  SER A CA    1 
ATOM   1453 C C     . SER A 1 188 ? 46.00224 -46.65307 -6.13207  1.000 15.71797 ? 188  SER A C     1 
ATOM   1454 O O     . SER A 1 188 ? 46.01418 -46.05937 -7.21391  1.000 15.18201 ? 188  SER A O     1 
ATOM   1455 C CB    . SER A 1 188 ? 45.08791 -45.59309 -4.05691  1.000 15.87373 ? 188  SER A CB    1 
ATOM   1456 O OG    . SER A 1 188 ? 44.30515 -46.74871 -3.81395  1.000 17.52743 ? 188  SER A OG    1 
ATOM   1457 N N     . ASP A 1 189 ? 45.68235 -47.94405 -6.02467  1.000 16.29790 ? 189  ASP A N     1 
ATOM   1458 C CA    . ASP A 1 189 ? 45.14079 -48.61864 -7.19805  1.000 18.03816 ? 189  ASP A CA    1 
ATOM   1459 C C     . ASP A 1 189 ? 43.73018 -48.14889 -7.53117  1.000 17.16944 ? 189  ASP A C     1 
ATOM   1460 O O     . ASP A 1 189 ? 43.18059 -48.55799 -8.55967  1.000 16.53710 ? 189  ASP A O     1 
ATOM   1461 C CB    . ASP A 1 189 ? 45.18254 -50.14241 -7.01282  1.000 19.43012 ? 189  ASP A CB    1 
ATOM   1462 C CG    . ASP A 1 189 ? 44.45687 -50.61730 -5.76463  1.000 17.75730 ? 189  ASP A CG    1 
ATOM   1463 O OD1   . ASP A 1 189 ? 43.67192 -49.84765 -5.17379  1.000 18.93470 ? 189  ASP A OD1   1 
ATOM   1464 O OD2   . ASP A 1 189 ? 44.68913 -51.77978 -5.36737  1.000 20.32608 ? 189  ASP A OD2   1 
ATOM   1465 N N     . GLN A 1 190 ? 43.14942 -47.29081 -6.69434  1.000 15.03752 ? 190  GLN A N     1 
ATOM   1466 C CA    . GLN A 1 190 ? 41.86268 -46.66276 -6.94986  1.000 16.18347 ? 190  GLN A CA    1 
ATOM   1467 C C     . GLN A 1 190 ? 42.00531 -45.23255 -7.45444  1.000 14.40988 ? 190  GLN A C     1 
ATOM   1468 O O     . GLN A 1 190 ? 41.00664 -44.51000 -7.53075  1.000 15.38711 ? 190  GLN A O     1 
ATOM   1469 C CB    . GLN A 1 190 ? 41.01258 -46.68012 -5.67755  1.000 15.38593 ? 190  GLN A CB    1 
ATOM   1470 C CG    . GLN A 1 190 ? 40.79139 -48.06751 -5.09836  1.000 17.74717 ? 190  GLN A CG    1 
ATOM   1471 C CD    . GLN A 1 190 ? 40.11943 -49.00332 -6.08115  1.000 19.28089 ? 190  GLN A CD    1 
ATOM   1472 O OE1   . GLN A 1 190 ? 39.01530 -48.73383 -6.55370  1.000 21.69148 ? 190  GLN A OE1   1 
ATOM   1473 N NE2   . GLN A 1 190 ? 40.78301 -50.11012 -6.39594  1.000 19.50844 ? 190  GLN A NE2   1 
ATOM   1474 N N     . ALA A 1 191 ? 43.21794 -44.81027 -7.80163  1.000 15.10790 ? 191  ALA A N     1 
ATOM   1475 C CA    . ALA A 1 191 ? 43.45856 -43.41401 -8.13194  1.000 15.09268 ? 191  ALA A CA    1 
ATOM   1476 C C     . ALA A 1 191 ? 42.81891 -43.03806 -9.46358  1.000 14.33116 ? 191  ALA A C     1 
ATOM   1477 O O     . ALA A 1 191 ? 42.65150 -43.86851 -10.36161 1.000 15.02345 ? 191  ALA A O     1 
ATOM   1478 C CB    . ALA A 1 191 ? 44.95698 -43.12834 -8.18460  1.000 15.65238 ? 191  ALA A CB    1 
ATOM   1479 N N     . HIS A 1 192 ? 42.46392 -41.76181 -9.57847  1.000 14.29903 ? 192  HIS A N     1 
ATOM   1480 C CA    . HIS A 1 192 ? 41.92689 -41.22439 -10.81810 1.000 14.80446 ? 192  HIS A CA    1 
ATOM   1481 C C     . HIS A 1 192 ? 43.01110 -41.21177 -11.89110 1.000 15.65857 ? 192  HIS A C     1 
ATOM   1482 O O     . HIS A 1 192 ? 44.20574 -41.12064 -11.59615 1.000 14.59818 ? 192  HIS A O     1 
ATOM   1483 C CB    . HIS A 1 192 ? 41.38193 -39.81365 -10.57724 1.000 15.94179 ? 192  HIS A CB    1 
ATOM   1484 C CG    . HIS A 1 192 ? 40.68587 -39.21281 -11.75850 1.000 18.67704 ? 192  HIS A CG    1 
ATOM   1485 N ND1   . HIS A 1 192 ? 41.29846 -38.31959 -12.61068 1.000 16.70262 ? 192  HIS A ND1   1 
ATOM   1486 C CD2   . HIS A 1 192 ? 39.42136 -39.36399 -12.21823 1.000 20.62935 ? 192  HIS A CD2   1 
ATOM   1487 C CE1   . HIS A 1 192 ? 40.44429 -37.95339 -13.54970 1.000 20.11174 ? 192  HIS A CE1   1 
ATOM   1488 N NE2   . HIS A 1 192 ? 39.29731 -38.57136 -13.33338 1.000 20.54259 ? 192  HIS A NE2   1 
ATOM   1489 N N     . SER A 1 193 ? 42.58352 -41.31303 -13.15223 1.000 14.81397 ? 193  SER A N     1 
ATOM   1490 C CA    . SER A 1 193 ? 43.52537 -41.35881 -14.26733 1.000 15.96229 ? 193  SER A CA    1 
ATOM   1491 C C     . SER A 1 193 ? 44.39427 -40.11178 -14.36659 1.000 15.52085 ? 193  SER A C     1 
ATOM   1492 O O     . SER A 1 193 ? 45.40868 -40.14136 -15.07334 1.000 15.70148 ? 193  SER A O     1 
ATOM   1493 C CB    . SER A 1 193 ? 42.76855 -41.56867 -15.57920 1.000 18.92497 ? 193  SER A CB    1 
ATOM   1494 O OG    . SER A 1 193 ? 41.87477 -40.49987 -15.82577 1.000 21.52500 ? 193  SER A OG    1 
ATOM   1495 N N     . SER A 1 194 ? 44.03355 -39.03026 -13.67018 1.000 15.52445 ? 194  SER A N     1 
ATOM   1496 C CA    . SER A 1 194 ? 44.83804 -37.81354 -13.70320 1.000 16.95675 ? 194  SER A CA    1 
ATOM   1497 C C     . SER A 1 194 ? 46.23677 -38.03477 -13.14039 1.000 14.30637 ? 194  SER A C     1 
ATOM   1498 O O     . SER A 1 194 ? 47.17469 -37.32803 -13.52589 1.000 14.53068 ? 194  SER A O     1 
ATOM   1499 C CB    . SER A 1 194 ? 44.12807 -36.70343 -12.93177 1.000 15.70749 ? 194  SER A CB    1 
ATOM   1500 O OG    . SER A 1 194 ? 43.81268 -37.12697 -11.61698 1.000 15.59470 ? 194  SER A OG    1 
ATOM   1501 N N     . VAL A 1 195 ? 46.40182 -38.99701 -12.22943 1.000 15.75637 ? 195  VAL A N     1 
ATOM   1502 C CA    . VAL A 1 195 ? 47.72804 -39.26506 -11.67934 1.000 14.70185 ? 195  VAL A CA    1 
ATOM   1503 C C     . VAL A 1 195 ? 48.63116 -39.87560 -12.74397 1.000 15.79688 ? 195  VAL A C     1 
ATOM   1504 O O     . VAL A 1 195 ? 49.78136 -39.45572 -12.91979 1.000 15.71143 ? 195  VAL A O     1 
ATOM   1505 C CB    . VAL A 1 195 ? 47.62839 -40.16654 -10.43632 1.000 15.60619 ? 195  VAL A CB    1 
ATOM   1506 C CG1   . VAL A 1 195 ? 48.97252 -40.23074 -9.72603  1.000 15.95237 ? 195  VAL A CG1   1 
ATOM   1507 C CG2   . VAL A 1 195 ? 46.55061 -39.65145 -9.49482  1.000 13.64945 ? 195  VAL A CG2   1 
ATOM   1508 N N     . GLU A 1 196 ? 48.12404 -40.87624 -13.46985 1.000 16.99021 ? 196  GLU A N     1 
ATOM   1509 C CA    . GLU A 1 196 ? 48.90152 -41.47061 -14.55327 1.000 19.15222 ? 196  GLU A CA    1 
ATOM   1510 C C     . GLU A 1 196 ? 49.26326 -40.43135 -15.60473 1.000 18.27426 ? 196  GLU A C     1 
ATOM   1511 O O     . GLU A 1 196 ? 50.40048 -40.39681 -16.09002 1.000 18.79061 ? 196  GLU A O     1 
ATOM   1512 C CB    . GLU A 1 196 ? 48.12738 -42.62378 -15.19131 1.000 18.34825 ? 196  GLU A CB    1 
ATOM   1513 C CG    . GLU A 1 196 ? 48.79780 -43.19415 -16.43425 1.000 24.46087 ? 196  GLU A CG    1 
ATOM   1514 C CD    . GLU A 1 196 ? 48.06041 -44.38720 -17.00456 1.000 36.23193 ? 196  GLU A CD    1 
ATOM   1515 O OE1   . GLU A 1 196 ? 46.81071 -44.37171 -16.99907 1.000 37.47528 ? 196  GLU A OE1   1 
ATOM   1516 O OE2   . GLU A 1 196 ? 48.72852 -45.33549 -17.46555 1.000 44.61364 ? 196  GLU A OE2   1 
ATOM   1517 N N     . ARG A 1 197 ? 48.30997 -39.56875 -15.96309 1.000 16.00147 ? 197  ARG A N     1 
ATOM   1518 C CA    . ARG A 1 197 ? 48.58702 -38.54234 -16.96204 1.000 16.12426 ? 197  ARG A CA    1 
ATOM   1519 C C     . ARG A 1 197 ? 49.63994 -37.56008 -16.46526 1.000 15.85155 ? 197  ARG A C     1 
ATOM   1520 O O     . ARG A 1 197 ? 50.49333 -37.11115 -17.23945 1.000 15.66273 ? 197  ARG A O     1 
ATOM   1521 C CB    . ARG A 1 197 ? 47.29376 -37.81957 -17.33793 1.000 20.22858 ? 197  ARG A CB    1 
ATOM   1522 C CG    . ARG A 1 197 ? 46.25834 -38.74037 -17.96525 1.000 27.36023 ? 197  ARG A CG    1 
ATOM   1523 C CD    . ARG A 1 197 ? 44.95547 -38.02042 -18.26456 1.000 32.92007 ? 197  ARG A CD    1 
ATOM   1524 N NE    . ARG A 1 197 ? 45.17823 -36.74125 -18.92607 1.000 37.71848 ? 197  ARG A NE    1 
ATOM   1525 C CZ    . ARG A 1 197 ? 44.86818 -36.48707 -20.19020 1.000 41.55946 ? 197  ARG A CZ    1 
ATOM   1526 N NH1   . ARG A 1 197 ? 44.37885 -37.42551 -20.98460 1.000 41.31740 ? 197  ARG A NH1   1 
ATOM   1527 N NH2   . ARG A 1 197 ? 45.06277 -35.26280 -20.67249 1.000 38.83369 ? 197  ARG A NH2   1 
ATOM   1528 N N     . ALA A 1 198 ? 49.60722 -37.22816 -15.17216 1.000 13.86071 ? 198  ALA A N     1 
ATOM   1529 C CA    . ALA A 1 198 ? 50.61747 -36.33517 -14.61392 1.000 13.91056 ? 198  ALA A CA    1 
ATOM   1530 C C     . ALA A 1 198 ? 51.99856 -36.97749 -14.64378 1.000 15.13559 ? 198  ALA A C     1 
ATOM   1531 O O     . ALA A 1 198 ? 52.99433 -36.30766 -14.94151 1.000 14.80459 ? 198  ALA A O     1 
ATOM   1532 C CB    . ALA A 1 198 ? 50.23819 -35.93880 -13.18724 1.000 15.57362 ? 198  ALA A CB    1 
ATOM   1533 N N     . GLY A 1 199 ? 52.07872 -38.27429 -14.34086 1.000 15.87271 ? 199  GLY A N     1 
ATOM   1534 C CA    . GLY A 1 199 ? 53.35884 -38.95979 -14.41051 1.000 15.87191 ? 199  GLY A CA    1 
ATOM   1535 C C     . GLY A 1 199 ? 53.89891 -39.04117 -15.82576 1.000 16.23101 ? 199  GLY A C     1 
ATOM   1536 O O     . GLY A 1 199 ? 55.10775 -38.92465 -16.04665 1.000 17.04733 ? 199  GLY A O     1 
ATOM   1537 N N     . LEU A 1 200 ? 53.01168 -39.24175 -16.80383 1.000 17.67533 ? 200  LEU A N     1 
ATOM   1538 C CA    . LEU A 1 200 ? 53.44119 -39.27350 -18.19810 1.000 17.15872 ? 200  LEU A CA    1 
ATOM   1539 C C     . LEU A 1 200 ? 53.92706 -37.90420 -18.65520 1.000 16.97215 ? 200  LEU A C     1 
ATOM   1540 O O     . LEU A 1 200 ? 54.95773 -37.79972 -19.33096 1.000 19.47412 ? 200  LEU A O     1 
ATOM   1541 C CB    . LEU A 1 200 ? 52.30084 -39.76203 -19.08825 1.000 18.04194 ? 200  LEU A CB    1 
ATOM   1542 C CG    . LEU A 1 200 ? 51.94617 -41.24492 -18.96649 1.000 20.47234 ? 200  LEU A CG    1 
ATOM   1543 C CD1   . LEU A 1 200 ? 50.61585 -41.53533 -19.64211 1.000 24.18194 ? 200  LEU A CD1   1 
ATOM   1544 C CD2   . LEU A 1 200 ? 53.05011 -42.11173 -19.55444 1.000 24.67485 ? 200  LEU A CD2   1 
ATOM   1545 N N     . ILE A 1 201 ? 53.20057 -36.84357 -18.29353 1.000 15.61417 ? 201  ILE A N     1 
ATOM   1546 C CA    . ILE A 1 201 ? 53.62319 -35.49176 -18.65159 1.000 16.31965 ? 201  ILE A CA    1 
ATOM   1547 C C     . ILE A 1 201 ? 54.94814 -35.15623 -17.97847 1.000 16.12559 ? 201  ILE A C     1 
ATOM   1548 O O     . ILE A 1 201 ? 55.87225 -34.63063 -18.61048 1.000 16.36806 ? 201  ILE A O     1 
ATOM   1549 C CB    . ILE A 1 201 ? 52.52914 -34.47267 -18.28439 1.000 15.80096 ? 201  ILE A CB    1 
ATOM   1550 C CG1   . ILE A 1 201 ? 51.30018 -34.65807 -19.17543 1.000 17.78999 ? 201  ILE A CG1   1 
ATOM   1551 C CG2   . ILE A 1 201 ? 53.05869 -33.04963 -18.39856 1.000 16.46368 ? 201  ILE A CG2   1 
ATOM   1552 C CD1   . ILE A 1 201 ? 50.10646 -33.83684 -18.73632 1.000 18.23697 ? 201  ILE A CD1   1 
ATOM   1553 N N     . GLY A 1 202 ? 55.06310 -35.46467 -16.68649 1.000 15.82211 ? 202  GLY A N     1 
ATOM   1554 C CA    . GLY A 1 202 ? 56.27963 -35.18103 -15.94550 1.000 16.95723 ? 202  GLY A CA    1 
ATOM   1555 C C     . GLY A 1 202 ? 57.45324 -36.07882 -16.28077 1.000 17.09053 ? 202  GLY A C     1 
ATOM   1556 O O     . GLY A 1 202 ? 58.58005 -35.76384 -15.88209 1.000 18.19410 ? 202  GLY A O     1 
ATOM   1557 N N     . GLY A 1 203 ? 57.22000 -37.17834 -16.99312 1.000 17.18446 ? 203  GLY A N     1 
ATOM   1558 C CA    . GLY A 1 203 ? 58.29945 -38.06169 -17.38644 1.000 19.31823 ? 203  GLY A CA    1 
ATOM   1559 C C     . GLY A 1 203 ? 58.85137 -38.92662 -16.27818 1.000 20.81483 ? 203  GLY A C     1 
ATOM   1560 O O     . GLY A 1 203 ? 60.04850 -39.22937 -16.27847 1.000 21.17368 ? 203  GLY A O     1 
ATOM   1561 N N     . VAL A 1 204 ? 58.01135 -39.34150 -15.32906 1.000 18.01580 ? 204  VAL A N     1 
ATOM   1562 C CA    . VAL A 1 204 ? 58.44937 -40.14009 -14.19355 1.000 16.48157 ? 204  VAL A CA    1 
ATOM   1563 C C     . VAL A 1 204 ? 57.61877 -41.41392 -14.12073 1.000 19.02267 ? 204  VAL A C     1 
ATOM   1564 O O     . VAL A 1 204 ? 56.51616 -41.50240 -14.66585 1.000 21.18150 ? 204  VAL A O     1 
ATOM   1565 C CB    . VAL A 1 204 ? 58.35104 -39.36771 -12.86128 1.000 18.87748 ? 204  VAL A CB    1 
ATOM   1566 C CG1   . VAL A 1 204 ? 59.24639 -38.13712 -12.89163 1.000 17.70440 ? 204  VAL A CG1   1 
ATOM   1567 C CG2   . VAL A 1 204 ? 56.90539 -38.98596 -12.57817 1.000 16.45767 ? 204  VAL A CG2   1 
ATOM   1568 N N     . LYS A 1 205 ? 58.16740 -42.40513 -13.42342 1.000 19.02057 ? 205  LYS A N     1 
ATOM   1569 C CA    . LYS A 1 205 ? 57.46637 -43.66168 -13.21355 1.000 18.25761 ? 205  LYS A CA    1 
ATOM   1570 C C     . LYS A 1 205 ? 56.36531 -43.49166 -12.17270 1.000 17.28975 ? 205  LYS A C     1 
ATOM   1571 O O     . LYS A 1 205 ? 56.46498 -42.67209 -11.25601 1.000 17.88826 ? 205  LYS A O     1 
ATOM   1572 C CB    . LYS A 1 205 ? 58.44120 -44.75001 -12.76082 1.000 17.72208 ? 205  LYS A CB    1 
ATOM   1573 C CG    . LYS A 1 205 ? 59.44377 -45.18332 -13.81721 1.000 23.21092 ? 205  LYS A CG    1 
ATOM   1574 C CD    . LYS A 1 205 ? 60.68981 -45.76750 -13.16785 1.000 23.39773 ? 205  LYS A CD    1 
ATOM   1575 C CE    . LYS A 1 205 ? 61.72000 -46.18318 -14.20485 1.000 27.33893 ? 205  LYS A CE    1 
ATOM   1576 N NZ    . LYS A 1 205 ? 62.16055 -45.04133 -15.05144 1.000 27.70171 ? 205  LYS A NZ    1 
ATOM   1577 N N     . LEU A 1 206 ? 55.30445 -44.28176 -12.32278 1.000 18.75808 ? 206  LEU A N     1 
ATOM   1578 C CA    . LEU A 1 206 ? 54.18831 -44.28481 -11.38632 1.000 18.37114 ? 206  LEU A CA    1 
ATOM   1579 C C     . LEU A 1 206 ? 53.83489 -45.72202 -11.03966 1.000 20.96409 ? 206  LEU A C     1 
ATOM   1580 O O     . LEU A 1 206 ? 53.71262 -46.56692 -11.93263 1.000 21.18607 ? 206  LEU A O     1 
ATOM   1581 C CB    . LEU A 1 206 ? 52.96324 -43.56660 -11.96559 1.000 18.42261 ? 206  LEU A CB    1 
ATOM   1582 C CG    . LEU A 1 206 ? 51.69408 -43.67326 -11.11233 1.000 17.23540 ? 206  LEU A CG    1 
ATOM   1583 C CD1   . LEU A 1 206 ? 51.81626 -42.85083 -9.83554  1.000 16.68416 ? 206  LEU A CD1   1 
ATOM   1584 C CD2   . LEU A 1 206 ? 50.45593 -43.27853 -11.89954 1.000 20.93913 ? 206  LEU A CD2   1 
ATOM   1585 N N     . LYS A 1 207 ? 53.67125 -45.99562 -9.74688  1.000 16.74671 ? 207  LYS A N     1 
ATOM   1586 C CA    . LYS A 1 207 ? 53.30681 -47.32001 -9.26838  1.000 18.20819 ? 207  LYS A CA    1 
ATOM   1587 C C     . LYS A 1 207 ? 52.09993 -47.21704 -8.34981  1.000 18.21406 ? 207  LYS A C     1 
ATOM   1588 O O     . LYS A 1 207 ? 51.97748 -46.26693 -7.57047  1.000 16.21260 ? 207  LYS A O     1 
ATOM   1589 C CB    . LYS A 1 207 ? 54.47394 -47.99123 -8.53461  1.000 18.92707 ? 207  LYS A CB    1 
ATOM   1590 C CG    . LYS A 1 207 ? 55.62767 -48.37616 -9.44765  1.000 20.76568 ? 207  LYS A CG    1 
ATOM   1591 C CD    . LYS A 1 207 ? 56.59777 -49.31817 -8.75691  1.000 19.45237 ? 207  LYS A CD    1 
ATOM   1592 C CE    . LYS A 1 207 ? 57.71779 -49.73355 -9.69623  1.000 25.11732 ? 207  LYS A CE    1 
ATOM   1593 N NZ    . LYS A 1 207 ? 58.39566 -50.97837 -9.23806  1.000 32.07218 ? 207  LYS A NZ    1 
ATOM   1594 N N     . ALA A 1 208 ? 51.21162 -48.20117 -8.44793  1.000 18.87860 ? 208  ALA A N     1 
ATOM   1595 C CA    . ALA A 1 208 ? 49.99847 -48.22942 -7.64608  1.000 16.87561 ? 208  ALA A CA    1 
ATOM   1596 C C     . ALA A 1 208 ? 50.24016 -48.99696 -6.35373  1.000 16.85771 ? 208  ALA A C     1 
ATOM   1597 O O     . ALA A 1 208 ? 50.84022 -50.07726 -6.36530  1.000 19.39276 ? 208  ALA A O     1 
ATOM   1598 C CB    . ALA A 1 208 ? 48.84765 -48.86259 -8.42717  1.000 17.94633 ? 208  ALA A CB    1 
ATOM   1599 N N     . ILE A 1 209 ? 49.77047 -48.43392 -5.24540  1.000 15.38879 ? 209  ILE A N     1 
ATOM   1600 C CA    . ILE A 1 209 ? 49.82769 -49.09646 -3.94626  1.000 15.80898 ? 209  ILE A CA    1 
ATOM   1601 C C     . ILE A 1 209 ? 48.56733 -49.93816 -3.79349  1.000 18.69734 ? 209  ILE A C     1 
ATOM   1602 O O     . ILE A 1 209 ? 47.45465 -49.41094 -3.93816  1.000 17.65064 ? 209  ILE A O     1 
ATOM   1603 C CB    . ILE A 1 209 ? 49.95308 -48.08229 -2.79914  1.000 16.66202 ? 209  ILE A CB    1 
ATOM   1604 C CG1   . ILE A 1 209 ? 51.13422 -47.13945 -3.03740  1.000 17.47267 ? 209  ILE A CG1   1 
ATOM   1605 C CG2   . ILE A 1 209 ? 50.09476 -48.80467 -1.46807  1.000 19.72106 ? 209  ILE A CG2   1 
ATOM   1606 C CD1   . ILE A 1 209 ? 52.47873 -47.80551 -2.93227  1.000 18.42165 ? 209  ILE A CD1   1 
ATOM   1607 N N     . PRO A 1 210 ? 48.68692 -51.23462 -3.51400  1.000 18.25573 ? 210  PRO A N     1 
ATOM   1608 C CA    . PRO A 1 210 ? 47.48774 -52.06557 -3.34071  1.000 19.97591 ? 210  PRO A CA    1 
ATOM   1609 C C     . PRO A 1 210 ? 46.65303 -51.59013 -2.16104  1.000 19.45612 ? 210  PRO A C     1 
ATOM   1610 O O     . PRO A 1 210 ? 47.17105 -51.33966 -1.07033  1.000 19.36270 ? 210  PRO A O     1 
ATOM   1611 C CB    . PRO A 1 210 ? 48.05754 -53.46916 -3.10101  1.000 21.22550 ? 210  PRO A CB    1 
ATOM   1612 C CG    . PRO A 1 210 ? 49.44484 -53.42707 -3.65284  1.000 25.72203 ? 210  PRO A CG    1 
ATOM   1613 C CD    . PRO A 1 210 ? 49.92778 -52.02417 -3.45456  1.000 20.10154 ? 210  PRO A CD    1 
ATOM   1614 N N     . SER A 1 211 ? 45.35020 -51.46731 -2.38896  1.000 17.90122 ? 211  SER A N     1 
ATOM   1615 C CA    . SER A 1 211 ? 44.43727 -51.01403 -1.35333  1.000 18.52841 ? 211  SER A CA    1 
ATOM   1616 C C     . SER A 1 211 ? 43.94809 -52.19394 -0.51872  1.000 20.53572 ? 211  SER A C     1 
ATOM   1617 O O     . SER A 1 211 ? 44.04424 -53.35645 -0.92031  1.000 20.09684 ? 211  SER A O     1 
ATOM   1618 C CB    . SER A 1 211 ? 43.25137 -50.27097 -1.96853  1.000 19.40025 ? 211  SER A CB    1 
ATOM   1619 O OG    . SER A 1 211 ? 42.63129 -51.04122 -2.98343  1.000 21.26420 ? 211  SER A OG    1 
ATOM   1620 N N     . ASP A 1 212 ? 43.41766 -51.87902 0.65892   1.000 18.71337 ? 212  ASP A N     1 
ATOM   1621 C CA    . ASP A 1 212 ? 42.95838 -52.90488 1.58185   1.000 19.18583 ? 212  ASP A CA    1 
ATOM   1622 C C     . ASP A 1 212 ? 41.51619 -53.29675 1.25560   1.000 20.92074 ? 212  ASP A C     1 
ATOM   1623 O O     . ASP A 1 212 ? 40.96669 -52.92559 0.21497   1.000 20.39383 ? 212  ASP A O     1 
ATOM   1624 C CB    . ASP A 1 212 ? 43.13475 -52.43118 3.02602   1.000 19.67155 ? 212  ASP A CB    1 
ATOM   1625 C CG    . ASP A 1 212 ? 42.16364 -51.32351 3.42135   1.000 21.08111 ? 212  ASP A CG    1 
ATOM   1626 O OD1   . ASP A 1 212 ? 41.35252 -50.87081 2.58536   1.000 20.35052 ? 212  ASP A OD1   1 
ATOM   1627 O OD2   . ASP A 1 212 ? 42.21801 -50.90073 4.59561   1.000 21.83389 ? 212  ASP A OD2   1 
ATOM   1628 N N     . GLY A 1 213 ? 40.88800 -54.05715 2.15617   1.000 21.50564 ? 213  GLY A N     1 
ATOM   1629 C CA    . GLY A 1 213 ? 39.52601 -54.51526 1.94155   1.000 21.91466 ? 213  GLY A CA    1 
ATOM   1630 C C     . GLY A 1 213 ? 38.50833 -53.39956 1.84171   1.000 23.08200 ? 213  GLY A C     1 
ATOM   1631 O O     . GLY A 1 213 ? 37.43562 -53.60085 1.26263   1.000 23.00735 ? 213  GLY A O     1 
ATOM   1632 N N     . ASN A 1 214 ? 38.81341 -52.23032 2.40089   1.000 19.16530 ? 214  ASN A N     1 
ATOM   1633 C CA    . ASN A 1 214 ? 37.97937 -51.04657 2.25698   1.000 21.89269 ? 214  ASN A CA    1 
ATOM   1634 C C     . ASN A 1 214 ? 38.43911 -50.15643 1.11043   1.000 20.10682 ? 214  ASN A C     1 
ATOM   1635 O O     . ASN A 1 214 ? 37.95633 -49.02573 0.98341   1.000 20.09812 ? 214  ASN A O     1 
ATOM   1636 C CB    . ASN A 1 214 ? 37.95997 -50.25306 3.56502   1.000 22.64995 ? 214  ASN A CB    1 
ATOM   1637 C CG    . ASN A 1 214 ? 37.21944 -50.97434 4.67271   1.000 26.86759 ? 214  ASN A CG    1 
ATOM   1638 O OD1   . ASN A 1 214 ? 36.12258 -51.49267 4.46712   1.000 28.35195 ? 214  ASN A OD1   1 
ATOM   1639 N ND2   . ASN A 1 214 ? 37.82219 -51.01921 5.85529   1.000 26.59436 ? 214  ASN A ND2   1 
ATOM   1640 N N     . PHE A 1 215 ? 39.36588 -50.64502 0.28264   1.000 19.14284 ? 215  PHE A N     1 
ATOM   1641 C CA    . PHE A 1 215 ? 39.89700 -49.90702 -0.86521  1.000 19.07494 ? 215  PHE A CA    1 
ATOM   1642 C C     . PHE A 1 215 ? 40.58433 -48.61512 -0.42788  1.000 19.19172 ? 215  PHE A C     1 
ATOM   1643 O O     . PHE A 1 215 ? 40.46345 -47.57208 -1.07296  1.000 17.60247 ? 215  PHE A O     1 
ATOM   1644 C CB    . PHE A 1 215 ? 38.80444 -49.64016 -1.90272  1.000 20.41036 ? 215  PHE A CB    1 
ATOM   1645 C CG    . PHE A 1 215 ? 38.22833 -50.89461 -2.49098  1.000 20.66873 ? 215  PHE A CG    1 
ATOM   1646 C CD1   . PHE A 1 215 ? 38.85228 -51.52584 -3.55446  1.000 23.10753 ? 215  PHE A CD1   1 
ATOM   1647 C CD2   . PHE A 1 215 ? 37.08293 -51.46218 -1.95870  1.000 23.32306 ? 215  PHE A CD2   1 
ATOM   1648 C CE1   . PHE A 1 215 ? 38.33456 -52.68881 -4.08842  1.000 24.84069 ? 215  PHE A CE1   1 
ATOM   1649 C CE2   . PHE A 1 215 ? 36.55975 -52.62687 -2.48822  1.000 23.12787 ? 215  PHE A CE2   1 
ATOM   1650 C CZ    . PHE A 1 215 ? 37.18757 -53.24104 -3.55397  1.000 22.63505 ? 215  PHE A CZ    1 
ATOM   1651 N N     . ALA A 1 216 ? 41.33207 -48.69873 0.66992   1.000 18.90393 ? 216  ALA A N     1 
ATOM   1652 C CA    . ALA A 1 216 ? 42.07235 -47.57943 1.22776   1.000 18.19952 ? 216  ALA A CA    1 
ATOM   1653 C C     . ALA A 1 216 ? 43.56129 -47.89244 1.22079   1.000 17.76372 ? 216  ALA A C     1 
ATOM   1654 O O     . ALA A 1 216 ? 43.96891 -49.04178 1.41465   1.000 18.41984 ? 216  ALA A O     1 
ATOM   1655 C CB    . ALA A 1 216 ? 41.62178 -47.27999 2.66093   1.000 20.29590 ? 216  ALA A CB    1 
ATOM   1656 N N     . MET A 1 217 ? 44.37234 -46.86069 0.99794   1.000 15.34662 ? 217  MET A N     1 
ATOM   1657 C CA    . MET A 1 217 ? 45.81625 -46.99552 1.13210   1.000 15.18657 ? 217  MET A CA    1 
ATOM   1658 C C     . MET A 1 217 ? 46.19261 -47.06212 2.60584   1.000 17.45330 ? 217  MET A C     1 
ATOM   1659 O O     . MET A 1 217 ? 45.73612 -46.24340 3.41115   1.000 17.41553 ? 217  MET A O     1 
ATOM   1660 C CB    . MET A 1 217 ? 46.53955 -45.83101 0.46008   1.000 17.64930 ? 217  MET A CB    1 
ATOM   1661 C CG    . MET A 1 217 ? 48.04738 -46.01537 0.42130   1.000 18.77981 ? 217  MET A CG    1 
ATOM   1662 S SD    . MET A 1 217 ? 48.92735 -44.62468 -0.30825  1.000 18.92060 ? 217  MET A SD    1 
ATOM   1663 C CE    . MET A 1 217 ? 47.90748 -44.29376 -1.74435  1.000 19.00595 ? 217  MET A CE    1 
ATOM   1664 N N     . ARG A 1 218 ? 47.02681 -48.03720 2.95644   1.000 17.05954 ? 218  ARG A N     1 
ATOM   1665 C CA    . ARG A 1 218 ? 47.42637 -48.26224 4.33597   1.000 18.89736 ? 218  ARG A CA    1 
ATOM   1666 C C     . ARG A 1 218 ? 48.94479 -48.26483 4.43665   1.000 19.44887 ? 218  ARG A C     1 
ATOM   1667 O O     . ARG A 1 218 ? 49.65668 -48.41992 3.44067   1.000 20.34390 ? 218  ARG A O     1 
ATOM   1668 C CB    . ARG A 1 218 ? 46.85381 -49.58006 4.87661   1.000 19.82633 ? 218  ARG A CB    1 
ATOM   1669 C CG    . ARG A 1 218 ? 45.34930 -49.70764 4.70058   1.000 19.18724 ? 218  ARG A CG    1 
ATOM   1670 C CD    . ARG A 1 218 ? 44.59876 -48.72159 5.58141   1.000 21.24299 ? 218  ARG A CD    1 
ATOM   1671 N NE    . ARG A 1 218 ? 44.97194 -48.85760 6.98430   1.000 22.66921 ? 218  ARG A NE    1 
ATOM   1672 C CZ    . ARG A 1 218 ? 44.41775 -49.72122 7.82409   1.000 27.04625 ? 218  ARG A CZ    1 
ATOM   1673 N NH1   . ARG A 1 218 ? 43.46169 -50.54813 7.43365   1.000 25.66661 ? 218  ARG A NH1   1 
ATOM   1674 N NH2   . ARG A 1 218 ? 44.83727 -49.76044 9.08557   1.000 27.05395 ? 218  ARG A NH2   1 
ATOM   1675 N N     . ALA A 1 219 ? 49.43123 -48.09610 5.66836   1.000 19.54351 ? 219  ALA A N     1 
ATOM   1676 C CA    . ALA A 1 219 ? 50.86990 -48.00400 5.89505   1.000 23.59889 ? 219  ALA A CA    1 
ATOM   1677 C C     . ALA A 1 219 ? 51.58702 -49.28223 5.47628   1.000 20.67497 ? 219  ALA A C     1 
ATOM   1678 O O     . ALA A 1 219 ? 52.68169 -49.22637 4.90308   1.000 22.76872 ? 219  ALA A O     1 
ATOM   1679 C CB    . ALA A 1 219 ? 51.14649 -47.68925 7.36575   1.000 21.57591 ? 219  ALA A CB    1 
ATOM   1680 N N     . SER A 1 220 ? 50.98102 -50.44371 5.74427   1.000 21.46907 ? 220  SER A N     1 
ATOM   1681 C CA    . SER A 1 220 ? 51.65367 -51.71280 5.47804   1.000 23.78594 ? 220  SER A CA    1 
ATOM   1682 C C     . SER A 1 220 ? 51.93549 -51.89534 3.99200   1.000 24.92395 ? 220  SER A C     1 
ATOM   1683 O O     . SER A 1 220 ? 53.03494 -52.31313 3.60767   1.000 22.49614 ? 220  SER A O     1 
ATOM   1684 C CB    . SER A 1 220 ? 50.81475 -52.87454 6.00775   1.000 26.86005 ? 220  SER A CB    1 
ATOM   1685 O OG    . SER A 1 220 ? 49.44696 -52.70384 5.68209   1.000 32.01733 ? 220  SER A OG    1 
ATOM   1686 N N     . ALA A 1 221 ? 50.95482 -51.59149 3.13938   1.000 21.82795 ? 221  ALA A N     1 
ATOM   1687 C CA    . ALA A 1 221 ? 51.16620 -51.73379 1.70284   1.000 21.73046 ? 221  ALA A CA    1 
ATOM   1688 C C     . ALA A 1 221 ? 52.16737 -50.70754 1.18738   1.000 19.66211 ? 221  ALA A C     1 
ATOM   1689 O O     . ALA A 1 221 ? 52.97688 -51.01212 0.30340   1.000 20.73604 ? 221  ALA A O     1 
ATOM   1690 C CB    . ALA A 1 221 ? 49.83679 -51.61062 0.96069   1.000 21.35369 ? 221  ALA A CB    1 
ATOM   1691 N N     . LEU A 1 222 ? 52.12813 -49.48641 1.72707   1.000 17.52054 ? 222  LEU A N     1 
ATOM   1692 C CA    . LEU A 1 222 ? 53.07616 -48.46058 1.30270   1.000 17.87586 ? 222  LEU A CA    1 
ATOM   1693 C C     . LEU A 1 222 ? 54.50114 -48.82755 1.70014   1.000 20.38851 ? 222  LEU A C     1 
ATOM   1694 O O     . LEU A 1 222 ? 55.43192 -48.68075 0.89893   1.000 18.05124 ? 222  LEU A O     1 
ATOM   1695 C CB    . LEU A 1 222 ? 52.68192 -47.10657 1.89454   1.000 16.86253 ? 222  LEU A CB    1 
ATOM   1696 C CG    . LEU A 1 222 ? 53.65919 -45.94312 1.70321   1.000 19.83853 ? 222  LEU A CG    1 
ATOM   1697 C CD1   . LEU A 1 222 ? 54.01365 -45.76562 0.23327   1.000 21.13925 ? 222  LEU A CD1   1 
ATOM   1698 C CD2   . LEU A 1 222 ? 53.07760 -44.65837 2.27417   1.000 18.65520 ? 222  LEU A CD2   1 
ATOM   1699 N N     . GLN A 1 223 ? 54.68978 -49.31067 2.93105   1.000 20.72635 ? 223  GLN A N     1 
ATOM   1700 C CA    . GLN A 1 223 ? 56.02633 -49.69048 3.37830   1.000 21.41403 ? 223  GLN A CA    1 
ATOM   1701 C C     . GLN A 1 223 ? 56.56933 -50.85626 2.56216   1.000 21.39050 ? 223  GLN A C     1 
ATOM   1702 O O     . GLN A 1 223 ? 57.77269 -50.92275 2.28136   1.000 20.01546 ? 223  GLN A O     1 
ATOM   1703 C CB    . GLN A 1 223 ? 56.00455 -50.04206 4.86663   1.000 22.93089 ? 223  GLN A CB    1 
ATOM   1704 C CG    . GLN A 1 223 ? 55.83044 -48.84262 5.78547   1.000 24.80341 ? 223  GLN A CG    1 
ATOM   1705 C CD    . GLN A 1 223 ? 55.30844 -49.22351 7.15845   1.000 34.68560 ? 223  GLN A CD    1 
ATOM   1706 O OE1   . GLN A 1 223 ? 54.53006 -50.16710 7.30340   1.000 34.64790 ? 223  GLN A OE1   1 
ATOM   1707 N NE2   . GLN A 1 223 ? 55.73745 -48.48646 8.17698   1.000 37.17445 ? 223  GLN A NE2   1 
ATOM   1708 N N     . GLU A 1 224 ? 55.69541 -51.78514 2.16956   1.000 19.60051 ? 224  GLU A N     1 
ATOM   1709 C CA    . GLU A 1 224 ? 56.13415 -52.91365 1.35576   1.000 22.01714 ? 224  GLU A CA    1 
ATOM   1710 C C     . GLU A 1 224 ? 56.59692 -52.45099 -0.02074  1.000 21.46960 ? 224  GLU A C     1 
ATOM   1711 O O     . GLU A 1 224 ? 57.60362 -52.94498 -0.54360  1.000 21.23200 ? 224  GLU A O     1 
ATOM   1712 C CB    . GLU A 1 224 ? 55.00395 -53.93698 1.24120   1.000 26.10718 ? 224  GLU A CB    1 
ATOM   1713 C CG    . GLU A 1 224 ? 55.05596 -54.80928 0.00205   1.000 33.97535 ? 224  GLU A CG    1 
ATOM   1714 C CD    . GLU A 1 224 ? 53.97355 -55.87061 -0.00099  1.000 40.32996 ? 224  GLU A CD    1 
ATOM   1715 O OE1   . GLU A 1 224 ? 52.77963 -55.50092 0.00338   1.000 43.34166 ? 224  GLU A OE1   1 
ATOM   1716 O OE2   . GLU A 1 224 ? 54.31518 -57.07189 -0.00911  1.000 46.58029 ? 224  GLU A OE2   1 
ATOM   1717 N N     . ALA A 1 225 ? 55.88588 -51.49041 -0.61636  1.000 20.30651 ? 225  ALA A N     1 
ATOM   1718 C CA    . ALA A 1 225 ? 56.29413 -50.97828 -1.92052  1.000 18.90961 ? 225  ALA A CA    1 
ATOM   1719 C C     . ALA A 1 225 ? 57.59589 -50.19297 -1.82276  1.000 18.98946 ? 225  ALA A C     1 
ATOM   1720 O O     . ALA A 1 225 ? 58.47194 -50.32545 -2.68576  1.000 18.96060 ? 225  ALA A O     1 
ATOM   1721 C CB    . ALA A 1 225 ? 55.18763 -50.11072 -2.51681  1.000 19.92374 ? 225  ALA A CB    1 
ATOM   1722 N N     . LEU A 1 226 ? 57.74013 -49.37233 -0.77756  1.000 18.66002 ? 226  LEU A N     1 
ATOM   1723 C CA    . LEU A 1 226 ? 58.96738 -48.60098 -0.59998  1.000 21.06274 ? 226  LEU A CA    1 
ATOM   1724 C C     . LEU A 1 226 ? 60.17534 -49.51425 -0.43123  1.000 19.65645 ? 226  LEU A C     1 
ATOM   1725 O O     . LEU A 1 226 ? 61.23771 -49.26484 -1.01370  1.000 19.91110 ? 226  LEU A O     1 
ATOM   1726 C CB    . LEU A 1 226 ? 58.83124 -47.67031 0.60496   1.000 18.74795 ? 226  LEU A CB    1 
ATOM   1727 C CG    . LEU A 1 226 ? 57.87552 -46.48545 0.46065   1.000 23.41856 ? 226  LEU A CG    1 
ATOM   1728 C CD1   . LEU A 1 226 ? 57.59874 -45.87080 1.81999   1.000 24.21650 ? 226  LEU A CD1   1 
ATOM   1729 C CD2   . LEU A 1 226 ? 58.44259 -45.44851 -0.48943  1.000 22.72031 ? 226  LEU A CD2   1 
ATOM   1730 N N     . GLU A 1 227 ? 60.03048 -50.57457 0.36903   1.000 20.15388 ? 227  GLU A N     1 
ATOM   1731 C CA    . GLU A 1 227 ? 61.12053 -51.52682 0.55972   1.000 20.98559 ? 227  GLU A CA    1 
ATOM   1732 C C     . GLU A 1 227 ? 61.56954 -52.12166 -0.76790  1.000 21.29463 ? 227  GLU A C     1 
ATOM   1733 O O     . GLU A 1 227 ? 62.77193 -52.23558 -1.03542  1.000 22.43537 ? 227  GLU A O     1 
ATOM   1734 C CB    . GLU A 1 227 ? 60.67929 -52.63017 1.51907   1.000 22.94819 ? 227  GLU A CB    1 
ATOM   1735 C CG    . GLU A 1 227 ? 61.67832 -53.76158 1.68622   1.000 23.95605 ? 227  GLU A CG    1 
ATOM   1736 C CD    . GLU A 1 227 ? 61.21207 -54.79838 2.68950   1.000 31.39838 ? 227  GLU A CD    1 
ATOM   1737 O OE1   . GLU A 1 227 ? 60.29139 -54.49160 3.47652   1.000 36.50332 ? 227  GLU A OE1   1 
ATOM   1738 O OE2   . GLU A 1 227 ? 61.76342 -55.91942 2.68942   1.000 30.04232 ? 227  GLU A OE2   1 
ATOM   1739 N N     . ARG A 1 228 ? 60.61182 -52.49371 -1.61764  1.000 20.79147 ? 228  ARG A N     1 
ATOM   1740 C CA    . ARG A 1 228 ? 60.93497 -53.07376 -2.91728  1.000 20.96336 ? 228  ARG A CA    1 
ATOM   1741 C C     . ARG A 1 228 ? 61.61908 -52.06226 -3.82902  1.000 20.68564 ? 228  ARG A C     1 
ATOM   1742 O O     . ARG A 1 228 ? 62.67049 -52.34910 -4.41385  1.000 21.16338 ? 228  ARG A O     1 
ATOM   1743 C CB    . ARG A 1 228 ? 59.66016 -53.60384 -3.57166  1.000 23.10911 ? 228  ARG A CB    1 
ATOM   1744 C CG    . ARG A 1 228 ? 59.84178 -54.09794 -4.99295  1.000 23.84176 ? 228  ARG A CG    1 
ATOM   1745 C CD    . ARG A 1 228 ? 58.50116 -54.14335 -5.71026  1.000 24.50404 ? 228  ARG A CD    1 
ATOM   1746 N NE    . ARG A 1 228 ? 57.89465 -52.82063 -5.81402  1.000 21.84821 ? 228  ARG A NE    1 
ATOM   1747 C CZ    . ARG A 1 228 ? 56.61155 -52.56763 -5.59433  1.000 24.52229 ? 228  ARG A CZ    1 
ATOM   1748 N NH1   . ARG A 1 228 ? 55.76486 -53.52895 -5.26227  1.000 22.41294 ? 228  ARG A NH1   1 
ATOM   1749 N NH2   . ARG A 1 228 ? 56.16746 -51.31908 -5.70648  1.000 22.41442 ? 228  ARG A NH2   1 
ATOM   1750 N N     . ASP A 1 229 ? 61.03401 -50.87035 -3.96376  1.000 20.74435 ? 229  ASP A N     1 
ATOM   1751 C CA    . ASP A 1 229 ? 61.49018 -49.93717 -4.98905  1.000 19.65237 ? 229  ASP A CA    1 
ATOM   1752 C C     . ASP A 1 229 ? 62.80682 -49.27294 -4.60077  1.000 21.73726 ? 229  ASP A C     1 
ATOM   1753 O O     . ASP A 1 229 ? 63.64926 -49.00546 -5.46627  1.000 20.15993 ? 229  ASP A O     1 
ATOM   1754 C CB    . ASP A 1 229 ? 60.40692 -48.89428 -5.25799  1.000 20.93047 ? 229  ASP A CB    1 
ATOM   1755 C CG    . ASP A 1 229 ? 59.14954 -49.50480 -5.85332  1.000 20.54999 ? 229  ASP A CG    1 
ATOM   1756 O OD1   . ASP A 1 229 ? 59.26281 -50.52880 -6.56204  1.000 21.16360 ? 229  ASP A OD1   1 
ATOM   1757 O OD2   . ASP A 1 229 ? 58.04936 -48.96616 -5.60871  1.000 19.66236 ? 229  ASP A OD2   1 
ATOM   1758 N N     . LYS A 1 230 ? 63.00730 -48.99907 -3.30856  1.000 20.14480 ? 230  LYS A N     1 
ATOM   1759 C CA    . LYS A 1 230 ? 64.27856 -48.42446 -2.87569  1.000 21.41827 ? 230  LYS A CA    1 
ATOM   1760 C C     . LYS A 1 230 ? 65.42096 -49.41360 -3.06602  1.000 22.03884 ? 230  LYS A C     1 
ATOM   1761 O O     . LYS A 1 230 ? 66.53560 -49.02095 -3.43087  1.000 22.69331 ? 230  LYS A O     1 
ATOM   1762 C CB    . LYS A 1 230 ? 64.18619 -47.96902 -1.41962  1.000 20.58245 ? 230  LYS A CB    1 
ATOM   1763 C CG    . LYS A 1 230 ? 63.28445 -46.76027 -1.23275  1.000 21.96701 ? 230  LYS A CG    1 
ATOM   1764 C CD    . LYS A 1 230 ? 62.74506 -46.65650 0.18280   1.000 24.09781 ? 230  LYS A CD    1 
ATOM   1765 C CE    . LYS A 1 230 ? 63.83358 -46.27582 1.16847   1.000 23.43170 ? 230  LYS A CE    1 
ATOM   1766 N NZ    . LYS A 1 230 ? 63.27608 -46.11596 2.54056   1.000 22.42445 ? 230  LYS A NZ    1 
ATOM   1767 N N     . ALA A 1 231 ? 65.16033 -50.70312 -2.83830  1.000 21.79912 ? 231  ALA A N     1 
ATOM   1768 C CA    . ALA A 1 231 ? 66.17863 -51.71559 -3.09344  1.000 22.63644 ? 231  ALA A CA    1 
ATOM   1769 C C     . ALA A 1 231 ? 66.47790 -51.84663 -4.58139  1.000 22.89236 ? 231  ALA A C     1 
ATOM   1770 O O     . ALA A 1 231 ? 67.59739 -52.21221 -4.95701  1.000 23.57938 ? 231  ALA A O     1 
ATOM   1771 C CB    . ALA A 1 231 ? 65.74032 -53.06146 -2.51770  1.000 23.07081 ? 231  ALA A CB    1 
ATOM   1772 N N     . ALA A 1 232 ? 65.50083 -51.55074 -5.43915  1.000 21.96967 ? 232  ALA A N     1 
ATOM   1773 C CA    . ALA A 1 232 ? 65.70688 -51.61934 -6.87934  1.000 23.57285 ? 232  ALA A CA    1 
ATOM   1774 C C     . ALA A 1 232 ? 66.41645 -50.39357 -7.43771  1.000 24.50672 ? 232  ALA A C     1 
ATOM   1775 O O     . ALA A 1 232 ? 66.73682 -50.37546 -8.63079  1.000 28.23498 ? 232  ALA A O     1 
ATOM   1776 C CB    . ALA A 1 232 ? 64.36719 -51.80346 -7.59705  1.000 24.52543 ? 232  ALA A CB    1 
ATOM   1777 N N     . GLY A 1 233 ? 66.67207 -49.37933 -6.61695  1.000 21.62398 ? 233  GLY A N     1 
ATOM   1778 C CA    . GLY A 1 233 ? 67.32068 -48.17303 -7.08243  1.000 22.95763 ? 233  GLY A CA    1 
ATOM   1779 C C     . GLY A 1 233 ? 66.38936 -47.04103 -7.44760  1.000 23.97724 ? 233  GLY A C     1 
ATOM   1780 O O     . GLY A 1 233 ? 66.86070 -46.01373 -7.94994  1.000 21.80874 ? 233  GLY A O     1 
ATOM   1781 N N     . LEU A 1 234 ? 65.08766 -47.19469 -7.22198  1.000 20.82285 ? 234  LEU A N     1 
ATOM   1782 C CA    . LEU A 1 234 ? 64.13857 -46.12616 -7.48850  1.000 19.79672 ? 234  LEU A CA    1 
ATOM   1783 C C     . LEU A 1 234 ? 64.13042 -45.12598 -6.33958  1.000 20.35354 ? 234  LEU A C     1 
ATOM   1784 O O     . LEU A 1 234 ? 64.40671 -45.46832 -5.18664  1.000 20.90273 ? 234  LEU A O     1 
ATOM   1785 C CB    . LEU A 1 234 ? 62.73379 -46.69492 -7.69758  1.000 20.85339 ? 234  LEU A CB    1 
ATOM   1786 C CG    . LEU A 1 234 ? 62.53716 -47.57640 -8.93246  1.000 21.47200 ? 234  LEU A CG    1 
ATOM   1787 C CD1   . LEU A 1 234 ? 61.10042 -48.06249 -9.02381  1.000 22.08665 ? 234  LEU A CD1   1 
ATOM   1788 C CD2   . LEU A 1 234 ? 62.92750 -46.82066 -10.19088 1.000 23.95240 ? 234  LEU A CD2   1 
ATOM   1789 N N     . ILE A 1 235 ? 63.81244 -43.87810 -6.66787  1.000 18.46189 ? 235  ILE A N     1 
ATOM   1790 C CA    . ILE A 1 235 ? 63.76901 -42.79976 -5.68415  1.000 19.42153 ? 235  ILE A CA    1 
ATOM   1791 C C     . ILE A 1 235 ? 62.33710 -42.29296 -5.56576  1.000 18.65619 ? 235  ILE A C     1 
ATOM   1792 O O     . ILE A 1 235 ? 61.87163 -41.53100 -6.42694  1.000 17.03675 ? 235  ILE A O     1 
ATOM   1793 C CB    . ILE A 1 235 ? 64.73543 -41.66436 -6.05490  1.000 20.87391 ? 235  ILE A CB    1 
ATOM   1794 C CG1   . ILE A 1 235 ? 66.13188 -42.23195 -6.32366  1.000 22.02941 ? 235  ILE A CG1   1 
ATOM   1795 C CG2   . ILE A 1 235 ? 64.76759 -40.61326 -4.95549  1.000 21.15493 ? 235  ILE A CG2   1 
ATOM   1796 C CD1   . ILE A 1 235 ? 67.09814 -41.23244 -6.89709  1.000 26.52611 ? 235  ILE A CD1   1 
ATOM   1797 N N     . PRO A 1 236 ? 61.60312 -42.69820 -4.53298  1.000 17.84419 ? 236  PRO A N     1 
ATOM   1798 C CA    . PRO A 1 236 ? 60.25715 -42.15092 -4.32233  1.000 18.13568 ? 236  PRO A CA    1 
ATOM   1799 C C     . PRO A 1 236 ? 60.31234 -40.65443 -4.05076  1.000 17.79830 ? 236  PRO A C     1 
ATOM   1800 O O     . PRO A 1 236 ? 61.09312 -40.18564 -3.22008  1.000 21.41280 ? 236  PRO A O     1 
ATOM   1801 C CB    . PRO A 1 236 ? 59.74917 -42.93149 -3.10393  1.000 18.02974 ? 236  PRO A CB    1 
ATOM   1802 C CG    . PRO A 1 236 ? 60.55599 -44.19968 -3.11496  1.000 19.58066 ? 236  PRO A CG    1 
ATOM   1803 C CD    . PRO A 1 236 ? 61.91583 -43.77059 -3.57459  1.000 18.27720 ? 236  PRO A CD    1 
ATOM   1804 N N     . PHE A 1 237 ? 59.47226 -39.90024 -4.76117  1.000 15.95911 ? 237  PHE A N     1 
ATOM   1805 C CA    . PHE A 1 237 ? 59.47927 -38.44880 -4.62019  1.000 17.36619 ? 237  PHE A CA    1 
ATOM   1806 C C     . PHE A 1 237 ? 58.09789 -37.81964 -4.54803  1.000 14.99667 ? 237  PHE A C     1 
ATOM   1807 O O     . PHE A 1 237 ? 58.00384 -36.64882 -4.16653  1.000 15.57406 ? 237  PHE A O     1 
ATOM   1808 C CB    . PHE A 1 237 ? 60.24671 -37.80393 -5.78512  1.000 16.26229 ? 237  PHE A CB    1 
ATOM   1809 C CG    . PHE A 1 237 ? 59.42180 -37.63077 -7.03126  1.000 16.73040 ? 237  PHE A CG    1 
ATOM   1810 C CD1   . PHE A 1 237 ? 59.13121 -38.71259 -7.84595  1.000 18.48656 ? 237  PHE A CD1   1 
ATOM   1811 C CD2   . PHE A 1 237 ? 58.95063 -36.37840 -7.39399  1.000 15.82660 ? 237  PHE A CD2   1 
ATOM   1812 C CE1   . PHE A 1 237 ? 58.37294 -38.55077 -8.99304  1.000 15.70229 ? 237  PHE A CE1   1 
ATOM   1813 C CE2   . PHE A 1 237 ? 58.19385 -36.21098 -8.53956  1.000 16.11037 ? 237  PHE A CE2   1 
ATOM   1814 C CZ    . PHE A 1 237 ? 57.90650 -37.29889 -9.33976  1.000 16.89559 ? 237  PHE A CZ    1 
ATOM   1815 N N     . PHE A 1 238 ? 57.03031 -38.53466 -4.89278  1.000 14.71700 ? 238  PHE A N     1 
ATOM   1816 C CA    . PHE A 1 238 ? 55.71378 -37.92511 -4.99952  1.000 14.14968 ? 238  PHE A CA    1 
ATOM   1817 C C     . PHE A 1 238 ? 54.65509 -38.97614 -4.70964  1.000 14.06294 ? 238  PHE A C     1 
ATOM   1818 O O     . PHE A 1 238 ? 54.78202 -40.12894 -5.13008  1.000 14.69563 ? 238  PHE A O     1 
ATOM   1819 C CB    . PHE A 1 238 ? 55.50739 -37.31766 -6.39261  1.000 14.33547 ? 238  PHE A CB    1 
ATOM   1820 C CG    . PHE A 1 238 ? 54.19525 -36.60845 -6.56678  1.000 14.16452 ? 238  PHE A CG    1 
ATOM   1821 C CD1   . PHE A 1 238 ? 53.91678 -35.45213 -5.85661  1.000 13.16874 ? 238  PHE A CD1   1 
ATOM   1822 C CD2   . PHE A 1 238 ? 53.25120 -37.08254 -7.46171  1.000 13.36324 ? 238  PHE A CD2   1 
ATOM   1823 C CE1   . PHE A 1 238 ? 52.71280 -34.79147 -6.02183  1.000 13.62425 ? 238  PHE A CE1   1 
ATOM   1824 C CE2   . PHE A 1 238 ? 52.04847 -36.42334 -7.63596  1.000 13.24597 ? 238  PHE A CE2   1 
ATOM   1825 C CZ    . PHE A 1 238 ? 51.77659 -35.27891 -6.91352  1.000 13.75109 ? 238  PHE A CZ    1 
ATOM   1826 N N     . MET A 1 239 ? 53.61840 -38.57049 -3.98272  1.000 13.77118 ? 239  MET A N     1 
ATOM   1827 C CA    . MET A 1 239 ? 52.52188 -39.45902 -3.62844  1.000 13.69932 ? 239  MET A CA    1 
ATOM   1828 C C     . MET A 1 239 ? 51.21089 -38.70497 -3.76554  1.000 13.17908 ? 239  MET A C     1 
ATOM   1829 O O     . MET A 1 239 ? 51.09260 -37.57272 -3.28806  1.000 14.60925 ? 239  MET A O     1 
ATOM   1830 C CB    . MET A 1 239 ? 52.67316 -39.98643 -2.19633  1.000 14.96189 ? 239  MET A CB    1 
ATOM   1831 C CG    . MET A 1 239 ? 51.35974 -40.40185 -1.55396  1.000 16.75176 ? 239  MET A CG    1 
ATOM   1832 S SD    . MET A 1 239 ? 50.83896 -42.04985 -2.05361  1.000 23.96916 ? 239  MET A SD    1 
ATOM   1833 C CE    . MET A 1 239 ? 52.08936 -43.04059 -1.24249  1.000 14.84263 ? 239  MET A CE    1 
ATOM   1834 N N     . VAL A 1 240 ? 50.23397 -39.32949 -4.41476  1.000 13.89996 ? 240  VAL A N     1 
ATOM   1835 C CA    . VAL A 1 240 ? 48.86749 -38.82479 -4.44955  1.000 12.58340 ? 240  VAL A CA    1 
ATOM   1836 C C     . VAL A 1 240 ? 48.02927 -39.72349 -3.55302  1.000 13.38051 ? 240  VAL A C     1 
ATOM   1837 O O     . VAL A 1 240 ? 47.75968 -40.88225 -3.89391  1.000 13.73082 ? 240  VAL A O     1 
ATOM   1838 C CB    . VAL A 1 240 ? 48.29679 -38.77747 -5.87270  1.000 12.73067 ? 240  VAL A CB    1 
ATOM   1839 C CG1   . VAL A 1 240 ? 46.81613 -38.41704 -5.82886  1.000 14.39200 ? 240  VAL A CG1   1 
ATOM   1840 C CG2   . VAL A 1 240 ? 49.05632 -37.77506 -6.71151  1.000 13.97291 ? 240  VAL A CG2   1 
ATOM   1841 N N     . ALA A 1 241 ? 47.63696 -39.19959 -2.39617  1.000 12.69583 ? 241  ALA A N     1 
ATOM   1842 C CA    . ALA A 1 241 ? 46.66650 -39.85985 -1.53854  1.000 12.80614 ? 241  ALA A CA    1 
ATOM   1843 C C     . ALA A 1 241 ? 45.28493 -39.30300 -1.84663  1.000 13.62308 ? 241  ALA A C     1 
ATOM   1844 O O     . ALA A 1 241 ? 45.11583 -38.09152 -2.00841  1.000 12.96438 ? 241  ALA A O     1 
ATOM   1845 C CB    . ALA A 1 241 ? 47.00815 -39.65451 -0.06287  1.000 13.10661 ? 241  ALA A CB    1 
ATOM   1846 N N     . THR A 1 242 ? 44.30141 -40.19207 -1.94221  1.000 12.42476 ? 242  THR A N     1 
ATOM   1847 C CA    . THR A 1 242 ? 42.96726 -39.83224 -2.40267  1.000 12.08362 ? 242  THR A CA    1 
ATOM   1848 C C     . THR A 1 242 ? 41.96139 -39.94080 -1.26687  1.000 12.95833 ? 242  THR A C     1 
ATOM   1849 O O     . THR A 1 242 ? 41.89960 -40.96477 -0.57769  1.000 12.67543 ? 242  THR A O     1 
ATOM   1850 C CB    . THR A 1 242 ? 42.53037 -40.71854 -3.57096  1.000 12.04903 ? 242  THR A CB    1 
ATOM   1851 O OG1   . THR A 1 242 ? 43.51370 -40.66049 -4.61045  1.000 13.40478 ? 242  THR A OG1   1 
ATOM   1852 C CG2   . THR A 1 242 ? 41.19071 -40.24885 -4.12254  1.000 12.26293 ? 242  THR A CG2   1 
ATOM   1853 N N     . LEU A 1 243 ? 41.17742 -38.88302 -1.08308  1.000 13.41617 ? 243  LEU A N     1 
ATOM   1854 C CA    . LEU A 1 243 ? 40.05351 -38.86246 -0.15235  1.000 12.03942 ? 243  LEU A CA    1 
ATOM   1855 C C     . LEU A 1 243 ? 38.78665 -38.78796 -0.99870  1.000 13.86666 ? 243  LEU A C     1 
ATOM   1856 O O     . LEU A 1 243 ? 38.46775 -37.73746 -1.56341  1.000 15.17612 ? 243  LEU A O     1 
ATOM   1857 C CB    . LEU A 1 243 ? 40.16326 -37.68655 0.81420   1.000 13.41501 ? 243  LEU A CB    1 
ATOM   1858 C CG    . LEU A 1 243 ? 41.38322 -37.66989 1.73970   1.000 15.54470 ? 243  LEU A CG    1 
ATOM   1859 C CD1   . LEU A 1 243 ? 41.33511 -36.46155 2.66140   1.000 16.22748 ? 243  LEU A CD1   1 
ATOM   1860 C CD2   . LEU A 1 243 ? 41.47057 -38.95836 2.54620   1.000 15.41652 ? 243  LEU A CD2   1 
ATOM   1861 N N     . GLY A 1 244 ? 38.07618 -39.90937 -1.09621  1.000 13.43290 ? 244  GLY A N     1 
ATOM   1862 C CA    . GLY A 1 244 ? 36.90745 -39.99418 -1.95047  1.000 13.63925 ? 244  GLY A CA    1 
ATOM   1863 C C     . GLY A 1 244 ? 37.24156 -40.46086 -3.35289  1.000 14.03794 ? 244  GLY A C     1 
ATOM   1864 O O     . GLY A 1 244 ? 37.10431 -39.70036 -4.31556  1.000 13.98277 ? 244  GLY A O     1 
ATOM   1865 N N     . THR A 1 245 ? 37.67692 -41.71322 -3.47904  1.000 14.04528 ? 245  THR A N     1 
ATOM   1866 C CA    . THR A 1 245 ? 38.11786 -42.23460 -4.76683  1.000 12.11496 ? 245  THR A CA    1 
ATOM   1867 C C     . THR A 1 245 ? 36.98230 -42.22398 -5.78557  1.000 14.74053 ? 245  THR A C     1 
ATOM   1868 O O     . THR A 1 245 ? 35.80459 -42.35979 -5.44304  1.000 15.02281 ? 245  THR A O     1 
ATOM   1869 C CB    . THR A 1 245 ? 38.66391 -43.65475 -4.60612  1.000 13.96655 ? 245  THR A CB    1 
ATOM   1870 O OG1   . THR A 1 245 ? 37.62617 -44.51605 -4.11977  1.000 15.46661 ? 245  THR A OG1   1 
ATOM   1871 C CG2   . THR A 1 245 ? 39.82916 -43.66530 -3.62612  1.000 12.55952 ? 245  THR A CG2   1 
ATOM   1872 N N     . THR A 1 246 ? 37.35400 -42.04981 -7.05785  1.000 16.63158 ? 246  THR A N     1 
ATOM   1873 C CA    . THR A 1 246 ? 36.35988 -42.01270 -8.12685  1.000 16.91160 ? 246  THR A CA    1 
ATOM   1874 C C     . THR A 1 246 ? 35.62203 -43.33596 -8.25529  1.000 16.58236 ? 246  THR A C     1 
ATOM   1875 O O     . THR A 1 246 ? 34.46163 -43.36135 -8.68125  1.000 17.90402 ? 246  THR A O     1 
ATOM   1876 C CB    . THR A 1 246 ? 37.02542 -41.66348 -9.45807  1.000 19.55049 ? 246  THR A CB    1 
ATOM   1877 O OG1   . THR A 1 246 ? 38.10124 -42.57754 -9.71030  1.000 23.66778 ? 246  THR A OG1   1 
ATOM   1878 C CG2   . THR A 1 246 ? 37.56980 -40.25386 -9.42154  1.000 19.26005 ? 246  THR A CG2   1 
ATOM   1879 N N     . THR A 1 247 ? 36.27330 -44.44164 -7.89517  1.000 16.67341 ? 247  THR A N     1 
ATOM   1880 C CA    . THR A 1 247 ? 35.64879 -45.75104 -8.03739  1.000 18.71823 ? 247  THR A CA    1 
ATOM   1881 C C     . THR A 1 247 ? 34.53901 -45.94638 -7.01107  1.000 17.06945 ? 247  THR A C     1 
ATOM   1882 O O     . THR A 1 247 ? 33.38111 -46.19158 -7.36938  1.000 17.40143 ? 247  THR A O     1 
ATOM   1883 C CB    . THR A 1 247 ? 36.70281 -46.85102 -7.90280  1.000 19.02762 ? 247  THR A CB    1 
ATOM   1884 O OG1   . THR A 1 247 ? 37.55677 -46.56005 -6.79001  1.000 17.85557 ? 247  THR A OG1   1 
ATOM   1885 C CG2   . THR A 1 247 ? 37.54573 -46.93378 -9.16515  1.000 19.92534 ? 247  THR A CG2   1 
ATOM   1886 N N     . CYS A 1 248 ? 34.87192 -45.83357 -5.72050  1.000 14.68648 ? 248  CYS A N     1 
ATOM   1887 C CA    . CYS A 1 248 ? 33.92576 -46.22038 -4.68219  1.000 15.06851 ? 248  CYS A CA    1 
ATOM   1888 C C     . CYS A 1 248 ? 33.85671 -45.24402 -3.51409  1.000 16.80793 ? 248  CYS A C     1 
ATOM   1889 O O     . CYS A 1 248 ? 33.27476 -45.59200 -2.47684  1.000 16.26463 ? 248  CYS A O     1 
ATOM   1890 C CB    . CYS A 1 248 ? 34.26868 -47.61392 -4.15118  1.000 18.22837 ? 248  CYS A CB    1 
ATOM   1891 S SG    . CYS A 1 248 ? 35.96031 -47.77461 -3.54368  1.000 19.51456 ? 248  CYS A SG    1 
ATOM   1892 N N     . CYS A 1 249 ? 34.41705 -44.04330 -3.64671  1.000 15.17713 ? 249  CYS A N     1 
ATOM   1893 C CA    . CYS A 1 249 ? 34.44197 -43.05469 -2.56955  1.000 14.03728 ? 249  CYS A CA    1 
ATOM   1894 C C     . CYS A 1 249 ? 35.03692 -43.64824 -1.29427  1.000 15.16751 ? 249  CYS A C     1 
ATOM   1895 O O     . CYS A 1 249 ? 34.46592 -43.55534 -0.20513  1.000 16.62230 ? 249  CYS A O     1 
ATOM   1896 C CB    . CYS A 1 249 ? 33.04716 -42.47887 -2.31219  1.000 15.22750 ? 249  CYS A CB    1 
ATOM   1897 S SG    . CYS A 1 249 ? 33.04884 -40.91216 -1.39540  1.000 15.58793 ? 249  CYS A SG    1 
ATOM   1898 N N     . SER A 1 250 ? 36.19191 -44.28869 -1.44672  1.000 14.18487 ? 250  SER A N     1 
ATOM   1899 C CA    . SER A 1 250 ? 36.98278 -44.73056 -0.31065  1.000 14.98964 ? 250  SER A CA    1 
ATOM   1900 C C     . SER A 1 250 ? 38.00180 -43.65258 0.05490   1.000 14.17453 ? 250  SER A C     1 
ATOM   1901 O O     . SER A 1 250 ? 38.20974 -42.68326 -0.67774  1.000 12.74812 ? 250  SER A O     1 
ATOM   1902 C CB    . SER A 1 250 ? 37.67417 -46.06015 -0.61662  1.000 17.56891 ? 250  SER A CB    1 
ATOM   1903 O OG    . SER A 1 250 ? 38.50788 -45.95770 -1.75685  1.000 17.04044 ? 250  SER A OG    1 
ATOM   1904 N N     . PHE A 1 251 ? 38.64299 -43.82850 1.20832   1.000 15.08315 ? 251  PHE A N     1 
ATOM   1905 C CA    . PHE A 1 251 ? 39.49751 -42.79796 1.78724   1.000 14.62464 ? 251  PHE A CA    1 
ATOM   1906 C C     . PHE A 1 251 ? 40.83640 -43.40353 2.17686   1.000 16.55128 ? 251  PHE A C     1 
ATOM   1907 O O     . PHE A 1 251 ? 40.88960 -44.29816 3.02596   1.000 16.87929 ? 251  PHE A O     1 
ATOM   1908 C CB    . PHE A 1 251 ? 38.82971 -42.16023 3.00979   1.000 16.82063 ? 251  PHE A CB    1 
ATOM   1909 C CG    . PHE A 1 251 ? 37.56069 -41.42431 2.69182   1.000 15.72453 ? 251  PHE A CG    1 
ATOM   1910 C CD1   . PHE A 1 251 ? 36.35702 -42.10348 2.60019   1.000 18.12528 ? 251  PHE A CD1   1 
ATOM   1911 C CD2   . PHE A 1 251 ? 37.57037 -40.05476 2.48361   1.000 17.47494 ? 251  PHE A CD2   1 
ATOM   1912 C CE1   . PHE A 1 251 ? 35.18610 -41.43133 2.30532   1.000 15.92452 ? 251  PHE A CE1   1 
ATOM   1913 C CE2   . PHE A 1 251 ? 36.40274 -39.37546 2.18924   1.000 16.93641 ? 251  PHE A CE2   1 
ATOM   1914 C CZ    . PHE A 1 251 ? 35.20874 -40.06442 2.10026   1.000 16.84936 ? 251  PHE A CZ    1 
ATOM   1915 N N     . ASP A 1 252 ? 41.91203 -42.91020 1.56831   1.000 16.81526 ? 252  ASP A N     1 
ATOM   1916 C CA    . ASP A 1 252 ? 43.24950 -43.29684 1.99040   1.000 15.68107 ? 252  ASP A CA    1 
ATOM   1917 C C     . ASP A 1 252 ? 43.51877 -42.79809 3.40827   1.000 17.76505 ? 252  ASP A C     1 
ATOM   1918 O O     . ASP A 1 252 ? 43.04345 -41.73597 3.81908   1.000 17.56149 ? 252  ASP A O     1 
ATOM   1919 C CB    . ASP A 1 252 ? 44.29278 -42.74302 1.01833   1.000 15.12544 ? 252  ASP A CB    1 
ATOM   1920 C CG    . ASP A 1 252 ? 44.24233 -43.42001 -0.34290  1.000 15.68839 ? 252  ASP A CG    1 
ATOM   1921 O OD1   . ASP A 1 252 ? 43.60059 -44.48655 -0.45828  1.000 15.74670 ? 252  ASP A OD1   1 
ATOM   1922 O OD2   . ASP A 1 252 ? 44.83719 -42.88097 -1.30215  1.000 15.49887 ? 252  ASP A OD2   1 
ATOM   1923 N N     . ASN A 1 253 ? 44.28318 -43.58507 4.16340   1.000 18.11400 ? 253  ASN A N     1 
ATOM   1924 C CA    . ASN A 1 253 ? 44.54091 -43.30249 5.57558   1.000 18.29608 ? 253  ASN A CA    1 
ATOM   1925 C C     . ASN A 1 253 ? 45.70517 -42.32455 5.67936   1.000 20.17211 ? 253  ASN A C     1 
ATOM   1926 O O     . ASN A 1 253 ? 46.87171 -42.72608 5.67096   1.000 18.86725 ? 253  ASN A O     1 
ATOM   1927 C CB    . ASN A 1 253 ? 44.82725 -44.59087 6.33798   1.000 17.28531 ? 253  ASN A CB    1 
ATOM   1928 C CG    . ASN A 1 253 ? 44.75235 -44.40700 7.84064   1.000 22.34698 ? 253  ASN A CG    1 
ATOM   1929 O OD1   . ASN A 1 253 ? 45.26733 -43.42994 8.38526   1.000 19.11210 ? 253  ASN A OD1   1 
ATOM   1930 N ND2   . ASN A 1 253 ? 44.10663 -45.34838 8.52041   1.000 26.18445 ? 253  ASN A ND2   1 
ATOM   1931 N N     . LEU A 1 254 ? 45.38499 -41.03255 5.80169   1.000 18.52447 ? 254  LEU A N     1 
ATOM   1932 C CA    . LEU A 1 254 ? 46.42574 -40.01193 5.88624   1.000 17.52913 ? 254  LEU A CA    1 
ATOM   1933 C C     . LEU A 1 254 ? 47.20046 -40.09306 7.19376   1.000 19.67259 ? 254  LEU A C     1 
ATOM   1934 O O     . LEU A 1 254 ? 48.39034 -39.75989 7.22746   1.000 16.98535 ? 254  LEU A O     1 
ATOM   1935 C CB    . LEU A 1 254 ? 45.81715 -38.61907 5.73147   1.000 19.56143 ? 254  LEU A CB    1 
ATOM   1936 C CG    . LEU A 1 254 ? 45.10079 -38.31934 4.41679   1.000 18.73475 ? 254  LEU A CG    1 
ATOM   1937 C CD1   . LEU A 1 254 ? 44.74487 -36.84443 4.33899   1.000 15.86755 ? 254  LEU A CD1   1 
ATOM   1938 C CD2   . LEU A 1 254 ? 45.96879 -38.72798 3.24315   1.000 15.19390 ? 254  LEU A CD2   1 
ATOM   1939 N N     . LEU A 1 255 ? 46.54866 -40.51729 8.27715   1.000 18.63905 ? 255  LEU A N     1 
ATOM   1940 C CA    . LEU A 1 255 ? 47.24176 -40.63705 9.55282   1.000 18.96546 ? 255  LEU A CA    1 
ATOM   1941 C C     . LEU A 1 255 ? 48.33387 -41.69626 9.51081   1.000 20.19641 ? 255  LEU A C     1 
ATOM   1942 O O     . LEU A 1 255 ? 49.26854 -41.63968 10.31752  1.000 22.27908 ? 255  LEU A O     1 
ATOM   1943 C CB    . LEU A 1 255 ? 46.24012 -40.95230 10.66308  1.000 20.96697 ? 255  LEU A CB    1 
ATOM   1944 C CG    . LEU A 1 255 ? 45.30961 -39.79394 11.03353  1.000 24.51866 ? 255  LEU A CG    1 
ATOM   1945 C CD1   . LEU A 1 255 ? 44.25191 -40.24322 12.03283  1.000 28.17692 ? 255  LEU A CD1   1 
ATOM   1946 C CD2   . LEU A 1 255 ? 46.09599 -38.60394 11.56704  1.000 22.08943 ? 255  LEU A CD2   1 
ATOM   1947 N N     . GLU A 1 256 ? 48.24071 -42.64916 8.58356   1.000 19.09226 ? 256  GLU A N     1 
ATOM   1948 C CA    . GLU A 1 256 ? 49.25579 -43.67895 8.40917   1.000 19.85605 ? 256  GLU A CA    1 
ATOM   1949 C C     . GLU A 1 256 ? 50.26324 -43.30923 7.32427   1.000 20.98912 ? 256  GLU A C     1 
ATOM   1950 O O     . GLU A 1 256 ? 51.47489 -43.40349 7.54205   1.000 19.70700 ? 256  GLU A O     1 
ATOM   1951 C CB    . GLU A 1 256 ? 48.59076 -45.01928 8.07880   1.000 19.98825 ? 256  GLU A CB    1 
ATOM   1952 C CG    . GLU A 1 256 ? 47.92900 -45.70390 9.26606   1.000 21.34953 ? 256  GLU A CG    1 
ATOM   1953 C CD    . GLU A 1 256 ? 47.29385 -47.03097 8.89210   1.000 23.14875 ? 256  GLU A CD    1 
ATOM   1954 O OE1   . GLU A 1 256 ? 47.44428 -47.45894 7.72764   1.000 22.51949 ? 256  GLU A OE1   1 
ATOM   1955 O OE2   . GLU A 1 256 ? 46.64585 -47.64784 9.76372   1.000 26.19654 ? 256  GLU A OE2   1 
ATOM   1956 N N     . VAL A 1 257 ? 49.78261 -42.88346 6.15430   1.000 18.47529 ? 257  VAL A N     1 
ATOM   1957 C CA    . VAL A 1 257 ? 50.68975 -42.62299 5.04192   1.000 19.94179 ? 257  VAL A CA    1 
ATOM   1958 C C     . VAL A 1 257 ? 51.36273 -41.26089 5.15359   1.000 17.79030 ? 257  VAL A C     1 
ATOM   1959 O O     . VAL A 1 257 ? 52.43944 -41.06212 4.57731   1.000 19.40558 ? 257  VAL A O     1 
ATOM   1960 C CB    . VAL A 1 257 ? 49.94543 -42.74486 3.70138   1.000 20.68691 ? 257  VAL A CB    1 
ATOM   1961 C CG1   . VAL A 1 257 ? 49.17710 -44.05573 3.64758   1.000 21.50443 ? 257  VAL A CG1   1 
ATOM   1962 C CG2   . VAL A 1 257 ? 49.01287 -41.56526 3.49227   1.000 22.81068 ? 257  VAL A CG2   1 
ATOM   1963 N N     . GLY A 1 258 ? 50.76715 -40.32272 5.88508   1.000 17.40641 ? 258  GLY A N     1 
ATOM   1964 C CA    . GLY A 1 258 ? 51.32518 -39.00051 6.04135   1.000 16.44486 ? 258  GLY A CA    1 
ATOM   1965 C C     . GLY A 1 258 ? 52.68964 -39.00156 6.70237   1.000 18.80459 ? 258  GLY A C     1 
ATOM   1966 O O     . GLY A 1 258 ? 53.66696 -38.47727 6.15828   1.000 17.48790 ? 258  GLY A O     1 
ATOM   1967 N N     . PRO A 1 259 ? 52.77543 -39.57145 7.90954   1.000 18.65965 ? 259  PRO A N     1 
ATOM   1968 C CA    . PRO A 1 259 ? 54.08522 -39.66378 8.57639   1.000 19.16192 ? 259  PRO A CA    1 
ATOM   1969 C C     . PRO A 1 259 ? 55.13967 -40.38990 7.75892   1.000 20.94364 ? 259  PRO A C     1 
ATOM   1970 O O     . PRO A 1 259 ? 56.31949 -40.01586 7.80996   1.000 19.86611 ? 259  PRO A O     1 
ATOM   1971 C CB    . PRO A 1 259 ? 53.74576 -40.41506 9.86897   1.000 22.77318 ? 259  PRO A CB    1 
ATOM   1972 C CG    . PRO A 1 259 ? 52.36503 -39.95038 10.17814  1.000 20.77682 ? 259  PRO A CG    1 
ATOM   1973 C CD    . PRO A 1 259 ? 51.67605 -39.90366 8.83500   1.000 19.84771 ? 259  PRO A CD    1 
ATOM   1974 N N     . ILE A 1 260 ? 54.75060 -41.42204 7.00689   1.000 18.74970 ? 260  ILE A N     1 
ATOM   1975 C CA    . ILE A 1 260 ? 55.71736 -42.14438 6.18561   1.000 19.87444 ? 260  ILE A CA    1 
ATOM   1976 C C     . ILE A 1 260 ? 56.25172 -41.24796 5.07583   1.000 17.04037 ? 260  ILE A C     1 
ATOM   1977 O O     . ILE A 1 260 ? 57.46335 -41.18610 4.83699   1.000 17.36748 ? 260  ILE A O     1 
ATOM   1978 C CB    . ILE A 1 260 ? 55.09145 -43.43080 5.62076   1.000 21.78388 ? 260  ILE A CB    1 
ATOM   1979 C CG1   . ILE A 1 260 ? 54.69401 -44.37086 6.76035   1.000 23.54527 ? 260  ILE A CG1   1 
ATOM   1980 C CG2   . ILE A 1 260 ? 56.05446 -44.11406 4.65860   1.000 22.75423 ? 260  ILE A CG2   1 
ATOM   1981 C CD1   . ILE A 1 260 ? 53.90662 -45.57213 6.30886   1.000 24.04192 ? 260  ILE A CD1   1 
ATOM   1982 N N     . CYS A 1 261 ? 55.35728 -40.53972 4.38075   1.000 17.20411 ? 261  CYS A N     1 
ATOM   1983 C CA    . CYS A 1 261 ? 55.79848 -39.64001 3.31867   1.000 16.07605 ? 261  CYS A CA    1 
ATOM   1984 C C     . CYS A 1 261 ? 56.72819 -38.56143 3.85881   1.000 18.19831 ? 261  CYS A C     1 
ATOM   1985 O O     . CYS A 1 261 ? 57.72710 -38.21490 3.21638   1.000 19.69430 ? 261  CYS A O     1 
ATOM   1986 C CB    . CYS A 1 261 ? 54.59202 -39.00844 2.62239   1.000 15.40331 ? 261  CYS A CB    1 
ATOM   1987 S SG    . CYS A 1 261 ? 53.65481 -40.14831 1.58452   1.000 16.98465 ? 261  CYS A SG    1 
ATOM   1988 N N     . ASN A 1 262 ? 56.42233 -38.02529 5.04409   1.000 18.51571 ? 262  ASN A N     1 
ATOM   1989 C CA    . ASN A 1 262 ? 57.29000 -37.01324 5.63775   1.000 20.77966 ? 262  ASN A CA    1 
ATOM   1990 C C     . ASN A 1 262 ? 58.67070 -37.58036 5.93729   1.000 20.47811 ? 262  ASN A C     1 
ATOM   1991 O O     . ASN A 1 262 ? 59.68971 -36.93487 5.65936   1.000 22.47523 ? 262  ASN A O     1 
ATOM   1992 C CB    . ASN A 1 262 ? 56.66299 -36.45447 6.91520   1.000 19.92028 ? 262  ASN A CB    1 
ATOM   1993 C CG    . ASN A 1 262 ? 55.37419 -35.70044 6.65683   1.000 20.70818 ? 262  ASN A CG    1 
ATOM   1994 O OD1   . ASN A 1 262 ? 55.06290 -35.33955 5.52028   1.000 20.70705 ? 262  ASN A OD1   1 
ATOM   1995 N ND2   . ASN A 1 262 ? 54.62266 -35.44285 7.71990   1.000 18.45334 ? 262  ASN A ND2   1 
ATOM   1996 N N     . LYS A 1 263 ? 58.72323 -38.78971 6.50282   1.000 20.45455 ? 263  LYS A N     1 
ATOM   1997 C CA    . LYS A 1 263 ? 60.00553 -39.39048 6.85599   1.000 22.05727 ? 263  LYS A CA    1 
ATOM   1998 C C     . LYS A 1 263 ? 60.82814 -39.71347 5.61520   1.000 23.15090 ? 263  LYS A C     1 
ATOM   1999 O O     . LYS A 1 263 ? 62.05995 -39.60409 5.63349   1.000 24.17781 ? 263  LYS A O     1 
ATOM   2000 C CB    . LYS A 1 263 ? 59.77388 -40.65694 7.68236   1.000 23.26326 ? 263  LYS A CB    1 
ATOM   2001 C CG    . LYS A 1 263 ? 59.36860 -40.39966 9.12194   1.000 31.36282 ? 263  LYS A CG    1 
ATOM   2002 C CD    . LYS A 1 263 ? 59.28699 -41.70187 9.90193   1.000 36.43806 ? 263  LYS A CD    1 
ATOM   2003 C CE    . LYS A 1 263 ? 58.73679 -41.48257 11.30393  1.000 44.72298 ? 263  LYS A CE    1 
ATOM   2004 N NZ    . LYS A 1 263 ? 57.67562 -42.47007 11.65026  1.000 43.83865 ? 263  LYS A NZ    1 
ATOM   2005 N N     . GLU A 1 264 ? 60.16632 -40.11204 4.53243   1.000 20.36920 ? 264  GLU A N     1 
ATOM   2006 C CA    . GLU A 1 264 ? 60.83724 -40.48477 3.29663   1.000 21.96914 ? 264  GLU A CA    1 
ATOM   2007 C C     . GLU A 1 264 ? 61.12219 -39.28912 2.39618   1.000 20.57321 ? 264  GLU A C     1 
ATOM   2008 O O     . GLU A 1 264 ? 61.70593 -39.46936 1.32083   1.000 19.40637 ? 264  GLU A O     1 
ATOM   2009 C CB    . GLU A 1 264 ? 59.99097 -41.50899 2.53069   1.000 21.78622 ? 264  GLU A CB    1 
ATOM   2010 C CG    . GLU A 1 264 ? 59.71205 -42.79815 3.29462   1.000 20.76186 ? 264  GLU A CG    1 
ATOM   2011 C CD    . GLU A 1 264 ? 60.83439 -43.80821 3.18756   1.000 22.12702 ? 264  GLU A CD    1 
ATOM   2012 O OE1   . GLU A 1 264 ? 61.63123 -43.71853 2.23084   1.000 24.43211 ? 264  GLU A OE1   1 
ATOM   2013 O OE2   . GLU A 1 264 ? 60.91278 -44.69854 4.06032   1.000 27.07506 ? 264  GLU A OE2   1 
ATOM   2014 N N     . ASP A 1 265 ? 60.73256 -38.08131 2.81454   1.000 19.94547 ? 265  ASP A N     1 
ATOM   2015 C CA    . ASP A 1 265 ? 60.83212 -36.87266 1.99114   1.000 19.46192 ? 265  ASP A CA    1 
ATOM   2016 C C     . ASP A 1 265 ? 60.06983 -37.03025 0.67813   1.000 20.36706 ? 265  ASP A C     1 
ATOM   2017 O O     . ASP A 1 265 ? 60.51683 -36.58322 -0.38154  1.000 20.23011 ? 265  ASP A O     1 
ATOM   2018 C CB    . ASP A 1 265 ? 62.28867 -36.48090 1.73375   1.000 22.34356 ? 265  ASP A CB    1 
ATOM   2019 C CG    . ASP A 1 265 ? 62.50354 -34.98182 1.80005   1.000 31.28295 ? 265  ASP A CG    1 
ATOM   2020 O OD1   . ASP A 1 265 ? 61.67656 -34.28931 2.43046   1.000 33.93023 ? 265  ASP A OD1   1 
ATOM   2021 O OD2   . ASP A 1 265 ? 63.49330 -34.49447 1.21333   1.000 31.30400 ? 265  ASP A OD2   1 
ATOM   2022 N N     . ILE A 1 266 ? 58.91162 -37.67626 0.75395   1.000 16.62665 ? 266  ILE A N     1 
ATOM   2023 C CA    . ILE A 1 266 ? 58.00619 -37.80555 -0.37992  1.000 16.17908 ? 266  ILE A CA    1 
ATOM   2024 C C     . ILE A 1 266 ? 56.99045 -36.67530 -0.31067  1.000 15.10136 ? 266  ILE A C     1 
ATOM   2025 O O     . ILE A 1 266 ? 56.32627 -36.48874 0.71598   1.000 16.70366 ? 266  ILE A O     1 
ATOM   2026 C CB    . ILE A 1 266 ? 57.30210 -39.17282 -0.36949  1.000 15.92429 ? 266  ILE A CB    1 
ATOM   2027 C CG1   . ILE A 1 266 ? 58.31244 -40.30987 -0.53539  1.000 19.09926 ? 266  ILE A CG1   1 
ATOM   2028 C CG2   . ILE A 1 266 ? 56.23667 -39.23176 -1.45905  1.000 15.11237 ? 266  ILE A CG2   1 
ATOM   2029 C CD1   . ILE A 1 266 ? 57.70036 -41.68439 -0.36367  1.000 17.22229 ? 266  ILE A CD1   1 
ATOM   2030 N N     . TRP A 1 267 ? 56.87386 -35.91277 -1.39432  1.000 14.73671 ? 267  TRP A N     1 
ATOM   2031 C CA    . TRP A 1 267 ? 55.83957 -34.88917 -1.46922  1.000 14.40053 ? 267  TRP A CA    1 
ATOM   2032 C C     . TRP A 1 267 ? 54.47092 -35.55272 -1.43710  1.000 15.16563 ? 267  TRP A C     1 
ATOM   2033 O O     . TRP A 1 267 ? 54.14808 -36.37144 -2.30399  1.000 13.78578 ? 267  TRP A O     1 
ATOM   2034 C CB    . TRP A 1 267 ? 56.00938 -34.06021 -2.74181  1.000 13.96099 ? 267  TRP A CB    1 
ATOM   2035 C CG    . TRP A 1 267 ? 55.01780 -32.93101 -2.91463  1.000 15.87223 ? 267  TRP A CG    1 
ATOM   2036 C CD1   . TRP A 1 267 ? 53.65575 -33.03004 -3.00380  1.000 15.09033 ? 267  TRP A CD1   1 
ATOM   2037 C CD2   . TRP A 1 267 ? 55.32379 -31.53738 -3.04369  1.000 15.69377 ? 267  TRP A CD2   1 
ATOM   2038 N NE1   . TRP A 1 267 ? 53.09848 -31.78444 -3.16781  1.000 14.69082 ? 267  TRP A NE1   1 
ATOM   2039 C CE2   . TRP A 1 267 ? 54.10101 -30.85169 -3.19687  1.000 18.41863 ? 267  TRP A CE2   1 
ATOM   2040 C CE3   . TRP A 1 267 ? 56.51347 -30.80221 -3.03921  1.000 16.30175 ? 267  TRP A CE3   1 
ATOM   2041 C CZ2   . TRP A 1 267 ? 54.03458 -29.46812 -3.34357  1.000 17.38433 ? 267  TRP A CZ2   1 
ATOM   2042 C CZ3   . TRP A 1 267 ? 56.44505 -29.42858 -3.18541  1.000 21.49036 ? 267  TRP A CZ3   1 
ATOM   2043 C CH2   . TRP A 1 267 ? 55.21449 -28.77616 -3.33495  1.000 20.84167 ? 267  TRP A CH2   1 
ATOM   2044 N N     . LEU A 1 268 ? 53.66820 -35.20058 -0.43534  1.000 15.02918 ? 268  LEU A N     1 
ATOM   2045 C CA    . LEU A 1 268 ? 52.34021 -35.77416 -0.24961  1.000 13.55758 ? 268  LEU A CA    1 
ATOM   2046 C C     . LEU A 1 268 ? 51.30034 -34.79624 -0.78415  1.000 13.27441 ? 268  LEU A C     1 
ATOM   2047 O O     . LEU A 1 268 ? 51.09394 -33.72186 -0.21029  1.000 15.06547 ? 268  LEU A O     1 
ATOM   2048 C CB    . LEU A 1 268 ? 52.08534 -36.09083 1.22219   1.000 14.48584 ? 268  LEU A CB    1 
ATOM   2049 C CG    . LEU A 1 268 ? 50.68153 -36.59134 1.57217   1.000 13.92371 ? 268  LEU A CG    1 
ATOM   2050 C CD1   . LEU A 1 268 ? 50.27225 -37.75312 0.67940   1.000 13.56377 ? 268  LEU A CD1   1 
ATOM   2051 C CD2   . LEU A 1 268 ? 50.60938 -36.98500 3.03766   1.000 17.64590 ? 268  LEU A CD2   1 
ATOM   2052 N N     . HIS A 1 269 ? 50.64906 -35.17118 -1.88008  1.000 12.72700 ? 269  HIS A N     1 
ATOM   2053 C CA    . HIS A 1 269 ? 49.53759 -34.41628 -2.43899  1.000 12.26237 ? 269  HIS A CA    1 
ATOM   2054 C C     . HIS A 1 269 ? 48.24824 -35.16190 -2.13254  1.000 12.15211 ? 269  HIS A C     1 
ATOM   2055 O O     . HIS A 1 269 ? 48.16457 -36.37557 -2.34986  1.000 12.99603 ? 269  HIS A O     1 
ATOM   2056 C CB    . HIS A 1 269 ? 49.69463 -34.23244 -3.94986  1.000 12.03541 ? 269  HIS A CB    1 
ATOM   2057 C CG    . HIS A 1 269 ? 48.52748 -33.55603 -4.59825  1.000 11.59712 ? 269  HIS A CG    1 
ATOM   2058 N ND1   . HIS A 1 269 ? 48.20620 -32.23793 -4.35649  1.000 13.18919 ? 269  HIS A ND1   1 
ATOM   2059 C CD2   . HIS A 1 269 ? 47.59530 -34.01798 -5.46533  1.000 11.87124 ? 269  HIS A CD2   1 
ATOM   2060 C CE1   . HIS A 1 269 ? 47.13214 -31.91331 -5.05424  1.000 13.04391 ? 269  HIS A CE1   1 
ATOM   2061 N NE2   . HIS A 1 269 ? 46.74025 -32.97601 -5.73441  1.000 11.39702 ? 269  HIS A NE2   1 
ATOM   2062 N N     . VAL A 1 270 ? 47.25298 -34.44463 -1.62257  1.000 11.92959 ? 270  VAL A N     1 
ATOM   2063 C CA    . VAL A 1 270 ? 45.96199 -35.03267 -1.28562  1.000 11.83913 ? 270  VAL A CA    1 
ATOM   2064 C C     . VAL A 1 270 ? 44.95218 -34.63809 -2.35176  1.000 13.90763 ? 270  VAL A C     1 
ATOM   2065 O O     . VAL A 1 270 ? 44.64167 -33.45206 -2.52334  1.000 12.79414 ? 270  VAL A O     1 
ATOM   2066 C CB    . VAL A 1 270 ? 45.48933 -34.60400 0.11055   1.000 11.97677 ? 270  VAL A CB    1 
ATOM   2067 C CG1   . VAL A 1 270 ? 44.09767 -35.14919 0.37776   1.000 13.28611 ? 270  VAL A CG1   1 
ATOM   2068 C CG2   . VAL A 1 270 ? 46.45729 -35.11329 1.16054   1.000 13.51342 ? 270  VAL A CG2   1 
ATOM   2069 N N     . ASP A 1 271 ? 44.44550 -35.63751 -3.06568  1.000 11.37461 ? 271  ASP A N     1 
ATOM   2070 C CA    . ASP A 1 271 ? 43.39861 -35.46158 -4.06367  1.000 13.48146 ? 271  ASP A CA    1 
ATOM   2071 C C     . ASP A 1 271 ? 42.06429 -35.77121 -3.39429  1.000 13.07584 ? 271  ASP A C     1 
ATOM   2072 O O     . ASP A 1 271 ? 41.75761 -36.93423 -3.11392  1.000 12.14639 ? 271  ASP A O     1 
ATOM   2073 C CB    . ASP A 1 271 ? 43.65583 -36.37400 -5.26219  1.000 13.66660 ? 271  ASP A CB    1 
ATOM   2074 C CG    . ASP A 1 271 ? 42.52661 -36.36276 -6.28189  1.000 15.32449 ? 271  ASP A CG    1 
ATOM   2075 O OD1   . ASP A 1 271 ? 41.52443 -35.63477 -6.10533  1.000 13.98109 ? 271  ASP A OD1   1 
ATOM   2076 O OD2   . ASP A 1 271 ? 42.64854 -37.10753 -7.27637  1.000 12.86156 ? 271  ASP A OD2   1 
ATOM   2077 N N     . ALA A 1 272 ? 41.27459 -34.73222 -3.14012  1.000 10.92338 ? 272  ALA A N     1 
ATOM   2078 C CA    . ALA A 1 272 ? 39.94371 -34.87639 -2.56336  1.000 11.21128 ? 272  ALA A CA    1 
ATOM   2079 C C     . ALA A 1 272 ? 38.90932 -34.18330 -3.43705  1.000 11.89623 ? 272  ALA A C     1 
ATOM   2080 O O     . ALA A 1 272 ? 37.96076 -33.57220 -2.93896  1.000 12.15294 ? 272  ALA A O     1 
ATOM   2081 C CB    . ALA A 1 272 ? 39.90365 -34.33088 -1.13795  1.000 13.38626 ? 272  ALA A CB    1 
ATOM   2082 N N     . ALA A 1 273 ? 39.07427 -34.30930 -4.75986  1.000 11.29244 ? 273  ALA A N     1 
ATOM   2083 C CA    . ALA A 1 273 ? 38.31487 -33.51520 -5.72698  1.000 13.75432 ? 273  ALA A CA    1 
ATOM   2084 C C     . ALA A 1 273 ? 36.81805 -33.50410 -5.43780  1.000 12.49728 ? 273  ALA A C     1 
ATOM   2085 O O     . ALA A 1 273 ? 36.17918 -32.44541 -5.47248  1.000 11.49678 ? 273  ALA A O     1 
ATOM   2086 C CB    . ALA A 1 273 ? 38.57234 -34.03999 -7.13780  1.000 14.19788 ? 273  ALA A CB    1 
ATOM   2087 N N     . TYR A 1 274 ? 36.23888 -34.66786 -5.15394  1.000 10.98463 ? 274  TYR A N     1 
ATOM   2088 C CA    . TYR A 1 274 ? 34.81266 -34.73619 -4.86457  1.000 13.16569 ? 274  TYR A CA    1 
ATOM   2089 C C     . TYR A 1 274 ? 34.52687 -34.60798 -3.37215  1.000 15.19506 ? 274  TYR A C     1 
ATOM   2090 O O     . TYR A 1 274 ? 33.73248 -33.75744 -2.95719  1.000 13.58214 ? 274  TYR A O     1 
ATOM   2091 C CB    . TYR A 1 274 ? 34.23013 -36.04993 -5.39383  1.000 15.06600 ? 274  TYR A CB    1 
ATOM   2092 C CG    . TYR A 1 274 ? 32.89222 -36.40122 -4.78440  1.000 13.54404 ? 274  TYR A CG    1 
ATOM   2093 C CD1   . TYR A 1 274 ? 31.75622 -35.66522 -5.09461  1.000 13.81151 ? 274  TYR A CD1   1 
ATOM   2094 C CD2   . TYR A 1 274 ? 32.76674 -37.45459 -3.88752  1.000 13.82483 ? 274  TYR A CD2   1 
ATOM   2095 C CE1   . TYR A 1 274 ? 30.52821 -35.97606 -4.53915  1.000 13.89135 ? 274  TYR A CE1   1 
ATOM   2096 C CE2   . TYR A 1 274 ? 31.54192 -37.77142 -3.32402  1.000 13.62923 ? 274  TYR A CE2   1 
ATOM   2097 C CZ    . TYR A 1 274 ? 30.42794 -37.02699 -3.65607  1.000 15.59147 ? 274  TYR A CZ    1 
ATOM   2098 O OH    . TYR A 1 274 ? 29.20659 -37.33297 -3.10352  1.000 13.80203 ? 274  TYR A OH    1 
ATOM   2099 N N     . ALA A 1 275 ? 35.17597 -35.44097 -2.55590  1.000 11.43888 ? 275  ALA A N     1 
ATOM   2100 C CA    . ALA A 1 275 ? 34.83472 -35.53148 -1.14107  1.000 12.44598 ? 275  ALA A CA    1 
ATOM   2101 C C     . ALA A 1 275 ? 35.15820 -34.25888 -0.36786  1.000 12.16149 ? 275  ALA A C     1 
ATOM   2102 O O     . ALA A 1 275 ? 34.56841 -34.03205 0.69398   1.000 11.37234 ? 275  ALA A O     1 
ATOM   2103 C CB    . ALA A 1 275 ? 35.56064 -36.72087 -0.50615  1.000 13.19764 ? 275  ALA A CB    1 
ATOM   2104 N N     . GLY A 1 276 ? 36.07656 -33.42959 -0.86957  1.000 12.02983 ? 276  GLY A N     1 
ATOM   2105 C CA    . GLY A 1 276 ? 36.54293 -32.28990 -0.09424  1.000 12.78085 ? 276  GLY A CA    1 
ATOM   2106 C C     . GLY A 1 276 ? 35.44356 -31.33204 0.32296   1.000 12.93962 ? 276  GLY A C     1 
ATOM   2107 O O     . GLY A 1 276 ? 35.52583 -30.71408 1.38882   1.000 12.60175 ? 276  GLY A O     1 
ATOM   2108 N N     . SER A 1 277 ? 34.40046 -31.19771 -0.49965  1.000 11.15912 ? 277  SER A N     1 
ATOM   2109 C CA    . SER A 1 277 ? 33.32431 -30.26425 -0.18162  1.000 13.15628 ? 277  SER A CA    1 
ATOM   2110 C C     . SER A 1 277 ? 32.58846 -30.65528 1.09336   1.000 14.04536 ? 277  SER A C     1 
ATOM   2111 O O     . SER A 1 277 ? 32.10628 -29.78059 1.82236   1.000 14.60093 ? 277  SER A O     1 
ATOM   2112 C CB    . SER A 1 277 ? 32.34122 -30.17899 -1.34781  1.000 13.52167 ? 277  SER A CB    1 
ATOM   2113 O OG    . SER A 1 277 ? 32.95409 -29.62430 -2.49760  1.000 13.48388 ? 277  SER A OG    1 
ATOM   2114 N N     . ALA A 1 278 ? 32.49129 -31.95515 1.38187   1.000 14.01382 ? 278  ALA A N     1 
ATOM   2115 C CA    . ALA A 1 278 ? 31.79096 -32.39651 2.58169   1.000 14.25159 ? 278  ALA A CA    1 
ATOM   2116 C C     . ALA A 1 278 ? 32.53727 -32.03639 3.85752   1.000 14.00903 ? 278  ALA A C     1 
ATOM   2117 O O     . ALA A 1 278 ? 31.92948 -32.02944 4.93365   1.000 15.72609 ? 278  ALA A O     1 
ATOM   2118 C CB    . ALA A 1 278 ? 31.55703 -33.90741 2.53626   1.000 14.44251 ? 278  ALA A CB    1 
ATOM   2119 N N     . PHE A 1 279 ? 33.83215 -31.73426 3.76742   1.000 14.54508 ? 279  PHE A N     1 
ATOM   2120 C CA    . PHE A 1 279 ? 34.61211 -31.44762 4.96578   1.000 14.28199 ? 279  PHE A CA    1 
ATOM   2121 C C     . PHE A 1 279 ? 34.28937 -30.09025 5.58304   1.000 15.71756 ? 279  PHE A C     1 
ATOM   2122 O O     . PHE A 1 279 ? 34.83365 -29.77818 6.64771   1.000 16.62519 ? 279  PHE A O     1 
ATOM   2123 C CB    . PHE A 1 279 ? 36.10992 -31.55158 4.65595   1.000 14.31544 ? 279  PHE A CB    1 
ATOM   2124 C CG    . PHE A 1 279 ? 36.51677 -32.86788 4.03659   1.000 15.22789 ? 279  PHE A CG    1 
ATOM   2125 C CD1   . PHE A 1 279 ? 35.77741 -34.02116 4.26284   1.000 17.38288 ? 279  PHE A CD1   1 
ATOM   2126 C CD2   . PHE A 1 279 ? 37.64189 -32.95058 3.23233   1.000 15.41181 ? 279  PHE A CD2   1 
ATOM   2127 C CE1   . PHE A 1 279 ? 36.15023 -35.22810 3.69485   1.000 17.08763 ? 279  PHE A CE1   1 
ATOM   2128 C CE2   . PHE A 1 279 ? 38.01977 -34.15635 2.66208   1.000 13.99404 ? 279  PHE A CE2   1 
ATOM   2129 C CZ    . PHE A 1 279 ? 37.27269 -35.29450 2.89379   1.000 16.75634 ? 279  PHE A CZ    1 
ATOM   2130 N N     . ILE A 1 280 ? 33.42463 -29.28411 4.95986   1.000 12.82310 ? 280  ILE A N     1 
ATOM   2131 C CA    . ILE A 1 280 ? 32.90056 -28.09759 5.62615   1.000 16.27489 ? 280  ILE A CA    1 
ATOM   2132 C C     . ILE A 1 280 ? 31.86509 -28.44795 6.68072   1.000 17.10818 ? 280  ILE A C     1 
ATOM   2133 O O     . ILE A 1 280 ? 31.46062 -27.57415 7.45718   1.000 16.22942 ? 280  ILE A O     1 
ATOM   2134 C CB    . ILE A 1 280 ? 32.28122 -27.10410 4.62179   1.000 15.13513 ? 280  ILE A CB    1 
ATOM   2135 C CG1   . ILE A 1 280 ? 30.98310 -27.66680 4.04024   1.000 16.76366 ? 280  ILE A CG1   1 
ATOM   2136 C CG2   . ILE A 1 280 ? 33.27056 -26.77095 3.51496   1.000 17.05515 ? 280  ILE A CG2   1 
ATOM   2137 C CD1   . ILE A 1 280 ? 30.13940 -26.63436 3.32739   1.000 18.31411 ? 280  ILE A CD1   1 
ATOM   2138 N N     . CYS A 1 281 ? 31.42072 -29.71362 6.72410   1.000 14.97481 ? 281  CYS A N     1 
ATOM   2139 C CA    . CYS A 1 281 ? 30.49152 -30.22179 7.72393   1.000 15.43457 ? 281  CYS A CA    1 
ATOM   2140 C C     . CYS A 1 281 ? 31.26704 -30.89505 8.84386   1.000 16.64829 ? 281  CYS A C     1 
ATOM   2141 O O     . CYS A 1 281 ? 32.09764 -31.77458 8.56815   1.000 18.97544 ? 281  CYS A O     1 
ATOM   2142 C CB    . CYS A 1 281 ? 29.51984 -31.21647 7.09575   1.000 16.00624 ? 281  CYS A CB    1 
ATOM   2143 S SG    . CYS A 1 281 ? 28.41516 -30.50118 5.85302   1.000 17.44469 ? 281  CYS A SG    1 
ATOM   2144 N N     . PRO A 1 282 ? 31.03327 -30.51381 10.10304  1.000 17.84955 ? 282  PRO A N     1 
ATOM   2145 C CA    . PRO A 1 282 ? 31.83102 -31.08357 11.20405  1.000 19.07907 ? 282  PRO A CA    1 
ATOM   2146 C C     . PRO A 1 282 ? 31.75103 -32.59657 11.30497  1.000 18.80950 ? 282  PRO A C     1 
ATOM   2147 O O     . PRO A 1 282 ? 32.72664 -33.22902 11.72856  1.000 19.47974 ? 282  PRO A O     1 
ATOM   2148 C CB    . PRO A 1 282 ? 31.24725 -30.40582 12.45483  1.000 18.34743 ? 282  PRO A CB    1 
ATOM   2149 C CG    . PRO A 1 282 ? 29.97331 -29.74446 12.01165  1.000 24.61538 ? 282  PRO A CG    1 
ATOM   2150 C CD    . PRO A 1 282 ? 30.12711 -29.44891 10.55887  1.000 18.60886 ? 282  PRO A CD    1 
ATOM   2151 N N     . GLU A 1 283 ? 30.62495 -33.20166 10.92192  1.000 19.22618 ? 283  GLU A N     1 
ATOM   2152 C CA    . GLU A 1 283 ? 30.48400 -34.64928 11.03050  1.000 17.65544 ? 283  GLU A CA    1 
ATOM   2153 C C     . GLU A 1 283 ? 31.32135 -35.40617 10.00868  1.000 22.81710 ? 283  GLU A C     1 
ATOM   2154 O O     . GLU A 1 283 ? 31.49070 -36.62140 10.15520  1.000 21.97573 ? 283  GLU A O     1 
ATOM   2155 C CB    . GLU A 1 283 ? 29.01295 -35.04676 10.88922  1.000 18.47202 ? 283  GLU A CB    1 
ATOM   2156 C CG    . GLU A 1 283 ? 28.43123 -34.81552 9.50587   1.000 20.38490 ? 283  GLU A CG    1 
ATOM   2157 C CD    . GLU A 1 283 ? 27.72283 -33.48131 9.38941   1.000 18.73220 ? 283  GLU A CD    1 
ATOM   2158 O OE1   . GLU A 1 283 ? 28.11785 -32.53060 10.09862  1.000 18.31474 ? 283  GLU A OE1   1 
ATOM   2159 O OE2   . GLU A 1 283 ? 26.76593 -33.38510 8.59337   1.000 20.28199 ? 283  GLU A OE2   1 
ATOM   2160 N N     . PHE A 1 284 ? 31.84332 -34.72850 8.98466   1.000 18.73392 ? 284  PHE A N     1 
ATOM   2161 C CA    . PHE A 1 284 ? 32.70324 -35.35796 7.99227   1.000 19.34323 ? 284  PHE A CA    1 
ATOM   2162 C C     . PHE A 1 284 ? 34.14814 -34.88405 8.05980   1.000 19.10217 ? 284  PHE A C     1 
ATOM   2163 O O     . PHE A 1 284 ? 34.99400 -35.43431 7.34712   1.000 20.00986 ? 284  PHE A O     1 
ATOM   2164 C CB    . PHE A 1 284 ? 32.16072 -35.10561 6.57685   1.000 18.65349 ? 284  PHE A CB    1 
ATOM   2165 C CG    . PHE A 1 284 ? 30.75046 -35.58233 6.37093   1.000 18.03526 ? 284  PHE A CG    1 
ATOM   2166 C CD1   . PHE A 1 284 ? 30.40504 -36.90106 6.61834   1.000 22.82959 ? 284  PHE A CD1   1 
ATOM   2167 C CD2   . PHE A 1 284 ? 29.77010 -34.70938 5.92680   1.000 18.10193 ? 284  PHE A CD2   1 
ATOM   2168 C CE1   . PHE A 1 284 ? 29.10831 -37.33877 6.42766   1.000 22.25297 ? 284  PHE A CE1   1 
ATOM   2169 C CE2   . PHE A 1 284 ? 28.47147 -35.14103 5.73544   1.000 20.04879 ? 284  PHE A CE2   1 
ATOM   2170 C CZ    . PHE A 1 284 ? 28.14036 -36.45782 5.98677   1.000 20.51104 ? 284  PHE A CZ    1 
ATOM   2171 N N     . ARG A 1 285 ? 34.45130 -33.88985 8.90107   1.000 18.16049 ? 285  ARG A N     1 
ATOM   2172 C CA    . ARG A 1 285 ? 35.79549 -33.31847 8.95439   1.000 18.72662 ? 285  ARG A CA    1 
ATOM   2173 C C     . ARG A 1 285 ? 36.83642 -34.34260 9.39088   1.000 19.50959 ? 285  ARG A C     1 
ATOM   2174 O O     . ARG A 1 285 ? 38.01661 -34.21143 9.04501   1.000 18.52046 ? 285  ARG A O     1 
ATOM   2175 C CB    . ARG A 1 285 ? 35.79135 -32.10633 9.88836   1.000 20.86295 ? 285  ARG A CB    1 
ATOM   2176 C CG    . ARG A 1 285 ? 37.11124 -31.35028 10.04633  1.000 18.16090 ? 285  ARG A CG    1 
ATOM   2177 C CD    . ARG A 1 285 ? 37.80232 -31.05298 8.72484   1.000 19.41062 ? 285  ARG A CD    1 
ATOM   2178 N NE    . ARG A 1 285 ? 39.12741 -30.48116 8.94047   1.000 19.30879 ? 285  ARG A NE    1 
ATOM   2179 C CZ    . ARG A 1 285 ? 40.20727 -31.17444 9.27632   1.000 19.71525 ? 285  ARG A CZ    1 
ATOM   2180 N NH1   . ARG A 1 285 ? 40.16245 -32.48518 9.45219   1.000 18.81121 ? 285  ARG A NH1   1 
ATOM   2181 N NH2   . ARG A 1 285 ? 41.36149 -30.53483 9.44335   1.000 17.14728 ? 285  ARG A NH2   1 
ATOM   2182 N N     . HIS A 1 286 ? 36.42496 -35.37242 10.13319  1.000 19.08893 ? 286  HIS A N     1 
ATOM   2183 C CA    . HIS A 1 286 ? 37.37397 -36.39530 10.55433  1.000 19.81599 ? 286  HIS A CA    1 
ATOM   2184 C C     . HIS A 1 286 ? 37.97059 -37.14777 9.37204   1.000 18.91841 ? 286  HIS A C     1 
ATOM   2185 O O     . HIS A 1 286 ? 39.07498 -37.68946 9.48935   1.000 19.83797 ? 286  HIS A O     1 
ATOM   2186 C CB    . HIS A 1 286 ? 36.70160 -37.38110 11.51197  1.000 21.52666 ? 286  HIS A CB    1 
ATOM   2187 C CG    . HIS A 1 286 ? 35.70341 -38.27795 10.84946  1.000 21.62110 ? 286  HIS A CG    1 
ATOM   2188 N ND1   . HIS A 1 286 ? 34.41007 -37.88416 10.58137  1.000 24.43461 ? 286  HIS A ND1   1 
ATOM   2189 C CD2   . HIS A 1 286 ? 35.81059 -39.55011 10.39839  1.000 21.36489 ? 286  HIS A CD2   1 
ATOM   2190 C CE1   . HIS A 1 286 ? 33.76310 -38.87635 9.99571   1.000 25.18635 ? 286  HIS A CE1   1 
ATOM   2191 N NE2   . HIS A 1 286 ? 34.59060 -39.89837 9.87243   1.000 22.16730 ? 286  HIS A NE2   1 
ATOM   2192 N N     . LEU A 1 287 ? 37.27305 -37.18411 8.23390   1.000 19.03683 ? 287  LEU A N     1 
ATOM   2193 C CA    . LEU A 1 287 ? 37.79964 -37.85811 7.05286   1.000 19.75657 ? 287  LEU A CA    1 
ATOM   2194 C C     . LEU A 1 287 ? 39.01571 -37.14479 6.47609   1.000 19.99707 ? 287  LEU A C     1 
ATOM   2195 O O     . LEU A 1 287 ? 39.75103 -37.74160 5.68153   1.000 19.01257 ? 287  LEU A O     1 
ATOM   2196 C CB    . LEU A 1 287 ? 36.70890 -37.97236 5.98822   1.000 21.65300 ? 287  LEU A CB    1 
ATOM   2197 C CG    . LEU A 1 287 ? 35.49169 -38.81651 6.37152   1.000 22.52128 ? 287  LEU A CG    1 
ATOM   2198 C CD1   . LEU A 1 287 ? 34.30998 -38.49619 5.46843   1.000 21.90141 ? 287  LEU A CD1   1 
ATOM   2199 C CD2   . LEU A 1 287 ? 35.82446 -40.29917 6.32178   1.000 23.27961 ? 287  LEU A CD2   1 
ATOM   2200 N N     . LEU A 1 288 ? 39.23949 -35.88817 6.85588   1.000 17.46636 ? 288  LEU A N     1 
ATOM   2201 C CA    . LEU A 1 288 ? 40.37838 -35.10705 6.39785   1.000 17.48069 ? 288  LEU A CA    1 
ATOM   2202 C C     . LEU A 1 288 ? 41.55019 -35.15433 7.37329   1.000 17.53622 ? 288  LEU A C     1 
ATOM   2203 O O     . LEU A 1 288 ? 42.62125 -34.61953 7.06608   1.000 17.78960 ? 288  LEU A O     1 
ATOM   2204 C CB    . LEU A 1 288 ? 39.93840 -33.65325 6.15794   1.000 16.23087 ? 288  LEU A CB    1 
ATOM   2205 C CG    . LEU A 1 288 ? 40.90498 -32.63371 5.54767   1.000 15.37652 ? 288  LEU A CG    1 
ATOM   2206 C CD1   . LEU A 1 288 ? 41.42665 -33.11375 4.20449   1.000 16.40841 ? 288  LEU A CD1   1 
ATOM   2207 C CD2   . LEU A 1 288 ? 40.22968 -31.27688 5.41138   1.000 16.78566 ? 288  LEU A CD2   1 
ATOM   2208 N N     . ASN A 1 289 ? 41.37682 -35.79149 8.53210   1.000 18.29388 ? 289  ASN A N     1 
ATOM   2209 C CA    . ASN A 1 289 ? 42.44444 -35.86654 9.52247   1.000 17.62799 ? 289  ASN A CA    1 
ATOM   2210 C C     . ASN A 1 289 ? 43.69798 -36.48337 8.91730   1.000 18.83122 ? 289  ASN A C     1 
ATOM   2211 O O     . ASN A 1 289 ? 43.63794 -37.51743 8.24540   1.000 18.29213 ? 289  ASN A O     1 
ATOM   2212 C CB    . ASN A 1 289 ? 41.98740 -36.68006 10.73265  1.000 20.08625 ? 289  ASN A CB    1 
ATOM   2213 C CG    . ASN A 1 289 ? 40.99037 -35.93268 11.59219  1.000 22.63835 ? 289  ASN A CG    1 
ATOM   2214 O OD1   . ASN A 1 289 ? 40.77139 -34.73592 11.40964  1.000 23.79724 ? 289  ASN A OD1   1 
ATOM   2215 N ND2   . ASN A 1 289 ? 40.38574 -36.63504 12.54431  1.000 24.39510 ? 289  ASN A ND2   1 
ATOM   2216 N N     . GLY A 1 290 ? 44.83562 -35.84036 9.15967   1.000 19.76772 ? 290  GLY A N     1 
ATOM   2217 C CA    . GLY A 1 290 ? 46.08981 -36.20755 8.53859   1.000 18.19783 ? 290  GLY A CA    1 
ATOM   2218 C C     . GLY A 1 290 ? 46.53090 -35.26931 7.43951   1.000 18.81988 ? 290  GLY A C     1 
ATOM   2219 O O     . GLY A 1 290 ? 47.67121 -35.38440 6.97244   1.000 16.94803 ? 290  GLY A O     1 
ATOM   2220 N N     . VAL A 1 291 ? 45.67019 -34.34016 7.01296   1.000 18.00799 ? 291  VAL A N     1 
ATOM   2221 C CA    . VAL A 1 291 ? 46.05272 -33.37533 5.98903   1.000 15.34878 ? 291  VAL A CA    1 
ATOM   2222 C C     . VAL A 1 291 ? 47.17768 -32.47667 6.48031   1.000 17.49365 ? 291  VAL A C     1 
ATOM   2223 O O     . VAL A 1 291 ? 47.90289 -31.88824 5.67037   1.000 15.72839 ? 291  VAL A O     1 
ATOM   2224 C CB    . VAL A 1 291 ? 44.82204 -32.55090 5.54929   1.000 16.44556 ? 291  VAL A CB    1 
ATOM   2225 C CG1   . VAL A 1 291 ? 44.34665 -31.65088 6.68077   1.000 17.76997 ? 291  VAL A CG1   1 
ATOM   2226 C CG2   . VAL A 1 291 ? 45.12388 -31.74719 4.28962   1.000 15.63495 ? 291  VAL A CG2   1 
ATOM   2227 N N     . GLU A 1 292 ? 47.35188 -32.36972 7.80094   1.000 18.01165 ? 292  GLU A N     1 
ATOM   2228 C CA    . GLU A 1 292 ? 48.47364 -31.62741 8.36412   1.000 17.35876 ? 292  GLU A CA    1 
ATOM   2229 C C     . GLU A 1 292 ? 49.81558 -32.18993 7.91932   1.000 19.04915 ? 292  GLU A C     1 
ATOM   2230 O O     . GLU A 1 292 ? 50.82228 -31.47518 7.96324   1.000 19.66045 ? 292  GLU A O     1 
ATOM   2231 C CB    . GLU A 1 292 ? 48.38628 -31.64231 9.89098   1.000 19.42436 ? 292  GLU A CB    1 
ATOM   2232 C CG    . GLU A 1 292 ? 48.35552 -33.04245 10.49353  1.000 19.78233 ? 292  GLU A CG    1 
ATOM   2233 C CD    . GLU A 1 292 ? 46.94639 -33.52716 10.78815  1.000 23.82697 ? 292  GLU A CD    1 
ATOM   2234 O OE1   . GLU A 1 292 ? 45.99971 -33.06222 10.11729  1.000 21.27156 ? 292  GLU A OE1   1 
ATOM   2235 O OE2   . GLU A 1 292 ? 46.78534 -34.37900 11.68930  1.000 28.88676 ? 292  GLU A OE2   1 
ATOM   2236 N N     . PHE A 1 293 ? 49.85281 -33.45383 7.50173   1.000 17.97660 ? 293  PHE A N     1 
ATOM   2237 C CA    . PHE A 1 293 ? 51.06976 -34.07776 7.00494   1.000 17.75628 ? 293  PHE A CA    1 
ATOM   2238 C C     . PHE A 1 293 ? 51.30006 -33.82445 5.52219   1.000 17.91183 ? 293  PHE A C     1 
ATOM   2239 O O     . PHE A 1 293 ? 52.39288 -34.11147 5.02192   1.000 16.92598 ? 293  PHE A O     1 
ATOM   2240 C CB    . PHE A 1 293 ? 51.02141 -35.58901 7.25289   1.000 18.63723 ? 293  PHE A CB    1 
ATOM   2241 C CG    . PHE A 1 293 ? 50.90705 -35.96393 8.70274   1.000 19.18864 ? 293  PHE A CG    1 
ATOM   2242 C CD1   . PHE A 1 293 ? 51.89956 -35.62128 9.60417   1.000 22.96290 ? 293  PHE A CD1   1 
ATOM   2243 C CD2   . PHE A 1 293 ? 49.80028 -36.65856 9.16337   1.000 19.56118 ? 293  PHE A CD2   1 
ATOM   2244 C CE1   . PHE A 1 293 ? 51.79296 -35.96771 10.93743  1.000 24.58222 ? 293  PHE A CE1   1 
ATOM   2245 C CE2   . PHE A 1 293 ? 49.68763 -37.00593 10.49588  1.000 20.86880 ? 293  PHE A CE2   1 
ATOM   2246 C CZ    . PHE A 1 293 ? 50.68537 -36.66008 11.38340  1.000 23.19589 ? 293  PHE A CZ    1 
ATOM   2247 N N     . ALA A 1 294 ? 50.30660 -33.29671 4.81480   1.000 15.75137 ? 294  ALA A N     1 
ATOM   2248 C CA    . ALA A 1 294 ? 50.39565 -33.14856 3.37188   1.000 16.89017 ? 294  ALA A CA    1 
ATOM   2249 C C     . ALA A 1 294 ? 51.17198 -31.89350 2.99505   1.000 17.38948 ? 294  ALA A C     1 
ATOM   2250 O O     . ALA A 1 294 ? 51.20041 -30.90529 3.73244   1.000 19.64580 ? 294  ALA A O     1 
ATOM   2251 C CB    . ALA A 1 294 ? 48.99981 -33.09228 2.75227   1.000 15.30550 ? 294  ALA A CB    1 
ATOM   2252 N N     . ASP A 1 295 ? 51.80547 -31.94341 1.82583   1.000 14.81393 ? 295  ASP A N     1 
ATOM   2253 C CA    . ASP A 1 295 ? 52.46548 -30.77540 1.26326   1.000 17.89433 ? 295  ASP A CA    1 
ATOM   2254 C C     . ASP A 1 295 ? 51.54399 -29.96270 0.36624   1.000 16.53926 ? 295  ASP A C     1 
ATOM   2255 O O     . ASP A 1 295 ? 51.76860 -28.75848 0.19240   1.000 15.53081 ? 295  ASP A O     1 
ATOM   2256 C CB    . ASP A 1 295 ? 53.70935 -31.20910 0.48414   1.000 15.47514 ? 295  ASP A CB    1 
ATOM   2257 C CG    . ASP A 1 295 ? 54.70629 -31.94318 1.35599   1.000 19.63910 ? 295  ASP A CG    1 
ATOM   2258 O OD1   . ASP A 1 295 ? 55.32577 -31.29176 2.22096   1.000 22.23268 ? 295  ASP A OD1   1 
ATOM   2259 O OD2   . ASP A 1 295 ? 54.85367 -33.17269 1.19535   1.000 16.81622 ? 295  ASP A OD2   1 
ATOM   2260 N N     . SER A 1 296 ? 50.51072 -30.58892 -0.19136  1.000 14.28742 ? 296  SER A N     1 
ATOM   2261 C CA    . SER A 1 296 ? 49.51363 -29.88938 -0.98482  1.000 15.28033 ? 296  SER A CA    1 
ATOM   2262 C C     . SER A 1 296 ? 48.17989 -30.60818 -0.83736  1.000 14.26132 ? 296  SER A C     1 
ATOM   2263 O O     . SER A 1 296 ? 48.13171 -31.82341 -0.62642  1.000 12.08486 ? 296  SER A O     1 
ATOM   2264 C CB    . SER A 1 296 ? 49.92847 -29.79271 -2.46070  1.000 15.57702 ? 296  SER A CB    1 
ATOM   2265 O OG    . SER A 1 296 ? 50.25069 -31.06459 -2.99860  1.000 13.30268 ? 296  SER A OG    1 
ATOM   2266 N N     . PHE A 1 297 ? 47.09721 -29.83927 -0.93874  1.000 12.55958 ? 297  PHE A N     1 
ATOM   2267 C CA    . PHE A 1 297 ? 45.74588 -30.35353 -0.77189  1.000 12.24065 ? 297  PHE A CA    1 
ATOM   2268 C C     . PHE A 1 297 ? 44.85222 -29.71782 -1.82382  1.000 11.00572 ? 297  PHE A C     1 
ATOM   2269 O O     . PHE A 1 297 ? 44.97618 -28.52342 -2.10752  1.000 13.00908 ? 297  PHE A O     1 
ATOM   2270 C CB    . PHE A 1 297 ? 45.19872 -30.05439 0.62997   1.000 12.87997 ? 297  PHE A CB    1 
ATOM   2271 C CG    . PHE A 1 297 ? 43.72323 -30.29766 0.76710   1.000 13.03365 ? 297  PHE A CG    1 
ATOM   2272 C CD1   . PHE A 1 297 ? 43.21611 -31.58641 0.73609   1.000 13.47187 ? 297  PHE A CD1   1 
ATOM   2273 C CD2   . PHE A 1 297 ? 42.84255 -29.23790 0.90585   1.000 14.22729 ? 297  PHE A CD2   1 
ATOM   2274 C CE1   . PHE A 1 297 ? 41.85913 -31.81497 0.85521   1.000 14.71286 ? 297  PHE A CE1   1 
ATOM   2275 C CE2   . PHE A 1 297 ? 41.48437 -29.45908 1.02308   1.000 13.62981 ? 297  PHE A CE2   1 
ATOM   2276 C CZ    . PHE A 1 297 ? 40.99173 -30.74925 0.99780   1.000 13.56025 ? 297  PHE A CZ    1 
ATOM   2277 N N     . ASN A 1 298 ? 43.94439 -30.51157 -2.38944  1.000 12.74765 ? 298  ASN A N     1 
ATOM   2278 C CA    . ASN A 1 298 ? 43.14193 -30.05414 -3.51535  1.000 11.66361 ? 298  ASN A CA    1 
ATOM   2279 C C     . ASN A 1 298 ? 41.75350 -30.67582 -3.46206  1.000 11.56423 ? 298  ASN A C     1 
ATOM   2280 O O     . ASN A 1 298 ? 41.60726 -31.86174 -3.15533  1.000 11.50291 ? 298  ASN A O     1 
ATOM   2281 C CB    . ASN A 1 298 ? 43.81882 -30.40670 -4.84550  1.000 11.42646 ? 298  ASN A CB    1 
ATOM   2282 C CG    . ASN A 1 298 ? 42.96503 -30.05829 -6.04845  1.000 13.43483 ? 298  ASN A CG    1 
ATOM   2283 O OD1   . ASN A 1 298 ? 42.64351 -30.92385 -6.86180  1.000 12.84911 ? 298  ASN A OD1   1 
ATOM   2284 N ND2   . ASN A 1 298 ? 42.60989 -28.78398 -6.17899  1.000 12.09171 ? 298  ASN A ND2   1 
ATOM   2285 N N     . PHE A 1 299 ? 40.73971 -29.86802 -3.76583  1.000 10.85342 ? 299  PHE A N     1 
ATOM   2286 C CA    . PHE A 1 299 ? 39.40101 -30.38389 -4.00620  1.000 11.03142 ? 299  PHE A CA    1 
ATOM   2287 C C     . PHE A 1 299 ? 38.70258 -29.45214 -4.98537  1.000 11.17950 ? 299  PHE A C     1 
ATOM   2288 O O     . PHE A 1 299 ? 39.15402 -28.33218 -5.22925  1.000 10.24407 ? 299  PHE A O     1 
ATOM   2289 C CB    . PHE A 1 299 ? 38.61641 -30.55628 -2.69261  1.000 11.48721 ? 299  PHE A CB    1 
ATOM   2290 C CG    . PHE A 1 299 ? 37.83429 -29.34375 -2.26396  1.000 11.01841 ? 299  PHE A CG    1 
ATOM   2291 C CD1   . PHE A 1 299 ? 38.43220 -28.35751 -1.49720  1.000 14.73707 ? 299  PHE A CD1   1 
ATOM   2292 C CD2   . PHE A 1 299 ? 36.49025 -29.21275 -2.58668  1.000 11.08054 ? 299  PHE A CD2   1 
ATOM   2293 C CE1   . PHE A 1 299 ? 37.71673 -27.25143 -1.08262  1.000 12.64262 ? 299  PHE A CE1   1 
ATOM   2294 C CE2   . PHE A 1 299 ? 35.76797 -28.10520 -2.17566  1.000 12.30459 ? 299  PHE A CE2   1 
ATOM   2295 C CZ    . PHE A 1 299 ? 36.38351 -27.12425 -1.42093  1.000 13.51817 ? 299  PHE A CZ    1 
ATOM   2296 N N     . ASN A 1 300 ? 37.60504 -29.93356 -5.56205  1.000 11.55047 ? 300  ASN A N     1 
ATOM   2297 C CA    . ASN A 1 300 ? 36.90015 -29.19623 -6.60540  1.000 12.17099 ? 300  ASN A CA    1 
ATOM   2298 C C     . ASN A 1 300 ? 35.61758 -28.57720 -6.06851  1.000 10.85569 ? 300  ASN A C     1 
ATOM   2299 O O     . ASN A 1 300 ? 34.62000 -29.29598 -5.90136  1.000 12.83475 ? 300  ASN A O     1 
ATOM   2300 C CB    . ASN A 1 300 ? 36.56953 -30.12081 -7.78242  1.000 12.40420 ? 300  ASN A CB    1 
ATOM   2301 C CG    . ASN A 1 300 ? 37.78931 -30.51719 -8.58861  1.000 13.84669 ? 300  ASN A CG    1 
ATOM   2302 O OD1   . ASN A 1 300 ? 38.83254 -29.86508 -8.52749  1.000 14.22117 ? 300  ASN A OD1   1 
ATOM   2303 N ND2   . ASN A 1 300 ? 37.65551 -31.58565 -9.36814  1.000 13.55091 ? 300  ASN A ND2   1 
ATOM   2304 N N     . PRO A 1 301 ? 35.56816 -27.26901 -5.80515  1.000 11.14570 ? 301  PRO A N     1 
ATOM   2305 C CA    . PRO A 1 301 ? 34.25962 -26.60484 -5.69989  1.000 11.36620 ? 301  PRO A CA    1 
ATOM   2306 C C     . PRO A 1 301 ? 33.35356 -26.84458 -6.89963  1.000 11.59357 ? 301  PRO A C     1 
ATOM   2307 O O     . PRO A 1 301 ? 32.12688 -26.79950 -6.74316  1.000 11.34647 ? 301  PRO A O     1 
ATOM   2308 C CB    . PRO A 1 301 ? 34.63800 -25.12325 -5.55493  1.000 12.60906 ? 301  PRO A CB    1 
ATOM   2309 C CG    . PRO A 1 301 ? 35.95200 -25.16930 -4.84195  1.000 10.67961 ? 301  PRO A CG    1 
ATOM   2310 C CD    . PRO A 1 301 ? 36.66958 -26.35877 -5.43501  1.000 11.10002 ? 301  PRO A CD    1 
ATOM   2311 N N     . HIS A 1 302 ? 33.90700 -27.11476 -8.08342  1.000 11.11607 ? 302  HIS A N     1 
ATOM   2312 C CA    . HIS A 1 302 ? 33.09236 -27.31823 -9.27451  1.000 9.87866  ? 302  HIS A CA    1 
ATOM   2313 C C     . HIS A 1 302 ? 32.57082 -28.73922 -9.42316  1.000 14.98958 ? 302  HIS A C     1 
ATOM   2314 O O     . HIS A 1 302 ? 31.89633 -29.03477 -10.41706 1.000 14.30092 ? 302  HIS A O     1 
ATOM   2315 C CB    . HIS A 1 302 ? 33.86804 -26.85046 -10.51488 1.000 13.16702 ? 302  HIS A CB    1 
ATOM   2316 C CG    . HIS A 1 302 ? 35.00715 -27.73282 -10.92478 1.000 13.18125 ? 302  HIS A CG    1 
ATOM   2317 N ND1   . HIS A 1 302 ? 36.21059 -27.21205 -11.34817 1.000 14.41304 ? 302  HIS A ND1   1 
ATOM   2318 C CD2   . HIS A 1 302 ? 35.13105 -29.07867 -11.00730 1.000 13.24858 ? 302  HIS A CD2   1 
ATOM   2319 C CE1   . HIS A 1 302 ? 37.03681 -28.19826 -11.64393 1.000 14.14553 ? 302  HIS A CE1   1 
ATOM   2320 N NE2   . HIS A 1 302 ? 36.40448 -29.34152 -11.45105 1.000 13.72179 ? 302  HIS A NE2   1 
HETATM 2321 N N1    . LLP A 1 303 ? 40.35168 -36.98808 -8.82518  1.000 16.66849 ? 303  LLP A N1    1 
HETATM 2322 C C2    . LLP A 1 303 ? 39.19774 -37.32502 -8.22950  1.000 16.48348 ? 303  LLP A C2    1 
HETATM 2323 C "C2'" . LLP A 1 303 ? 39.18549 -38.05068 -7.04140  1.000 16.13597 ? 303  LLP A "C2'" 1 
HETATM 2324 C C3    . LLP A 1 303 ? 38.00551 -36.93636 -8.81625  1.000 17.92919 ? 303  LLP A C3    1 
HETATM 2325 O O3    . LLP A 1 303 ? 36.84407 -37.28195 -8.20527  1.000 17.74067 ? 303  LLP A O3    1 
HETATM 2326 C C4    . LLP A 1 303 ? 37.95705 -36.21041 -9.99566  1.000 15.13673 ? 303  LLP A C4    1 
HETATM 2327 C "C4'" . LLP A 1 303 ? 36.74528 -35.83363 -10.56363 1.000 21.28187 ? 303  LLP A "C4'" 1 
HETATM 2328 C C5    . LLP A 1 303 ? 39.14952 -35.86694 -10.60862 1.000 18.08148 ? 303  LLP A C5    1 
HETATM 2329 C C6    . LLP A 1 303 ? 40.35420 -36.25263 -10.02560 1.000 16.30593 ? 303  LLP A C6    1 
HETATM 2330 C "C5'" . LLP A 1 303 ? 39.11136 -35.14099 -11.79314 1.000 18.28161 ? 303  LLP A "C5'" 1 
HETATM 2331 O OP4   . LLP A 1 303 ? 39.19641 -33.74588 -11.50215 1.000 19.03235 ? 303  LLP A OP4   1 
HETATM 2332 P P     . LLP A 1 303 ? 38.86370 -32.66582 -12.64840 1.000 15.69501 ? 303  LLP A P     1 
HETATM 2333 O OP1   . LLP A 1 303 ? 38.66253 -31.34265 -12.01382 1.000 13.03777 ? 303  LLP A OP1   1 
HETATM 2334 O OP2   . LLP A 1 303 ? 40.26026 -32.64186 -13.41584 1.000 14.47665 ? 303  LLP A OP2   1 
HETATM 2335 O OP3   . LLP A 1 303 ? 37.82250 -33.20850 -13.54421 1.000 21.75336 ? 303  LLP A OP3   1 
HETATM 2336 N N     . LLP A 1 303 ? 32.81404 -29.61713 -8.45762  1.000 12.83443 ? 303  LLP A N     1 
HETATM 2337 C CA    . LLP A 1 303 ? 31.96593 -30.80675 -8.35236  1.000 10.75362 ? 303  LLP A CA    1 
HETATM 2338 C CB    . LLP A 1 303 ? 32.76810 -32.05167 -7.97676  1.000 16.34501 ? 303  LLP A CB    1 
HETATM 2339 C CG    . LLP A 1 303 ? 33.71308 -32.53466 -9.05424  1.000 20.26380 ? 303  LLP A CG    1 
HETATM 2340 C CD    . LLP A 1 303 ? 34.46188 -33.76938 -8.58630  1.000 20.07660 ? 303  LLP A CD    1 
HETATM 2341 C CE    . LLP A 1 303 ? 34.84285 -34.63237 -9.77957  1.000 19.46770 ? 303  LLP A CE    1 
HETATM 2342 N NZ    . LLP A 1 303 ? 35.87400 -35.64651 -9.44669  1.000 18.30964 ? 303  LLP A NZ    1 
HETATM 2343 C C     . LLP A 1 303 ? 30.81005 -30.58190 -7.38337  1.000 12.29369 ? 303  LLP A C     1 
HETATM 2344 O O     . LLP A 1 303 ? 29.64633 -30.58534 -7.79205  1.000 14.28246 ? 303  LLP A O     1 
ATOM   2345 N N     . TRP A 1 304 ? 31.10764 -30.37694 -6.10339  1.000 12.01555 ? 304  TRP A N     1 
ATOM   2346 C CA    . TRP A 1 304 ? 30.04904 -30.55879 -5.11852  1.000 11.94787 ? 304  TRP A CA    1 
ATOM   2347 C C     . TRP A 1 304 ? 30.07517 -29.45068 -4.06236  1.000 12.04765 ? 304  TRP A C     1 
ATOM   2348 O O     . TRP A 1 304 ? 29.71824 -29.65844 -2.89809  1.000 13.22217 ? 304  TRP A O     1 
ATOM   2349 C CB    . TRP A 1 304 ? 30.14106 -31.99251 -4.57818  1.000 15.79446 ? 304  TRP A CB    1 
ATOM   2350 C CG    . TRP A 1 304 ? 29.11496 -32.46847 -3.61162  1.000 12.98345 ? 304  TRP A CG    1 
ATOM   2351 C CD1   . TRP A 1 304 ? 27.76774 -32.48994 -3.81830  1.000 14.59736 ? 304  TRP A CD1   1 
ATOM   2352 C CD2   . TRP A 1 304 ? 29.34473 -33.31689 -2.47253  1.000 13.33333 ? 304  TRP A CD2   1 
ATOM   2353 N NE1   . TRP A 1 304 ? 27.13605 -33.12641 -2.78033  1.000 12.71699 ? 304  TRP A NE1   1 
ATOM   2354 C CE2   . TRP A 1 304 ? 28.08288 -33.66501 -1.95066  1.000 11.65434 ? 304  TRP A CE2   1 
ATOM   2355 C CE3   . TRP A 1 304 ? 30.49316 -33.74805 -1.79993  1.000 15.99396 ? 304  TRP A CE3   1 
ATOM   2356 C CZ2   . TRP A 1 304 ? 27.93515 -34.42156 -0.78759  1.000 16.36153 ? 304  TRP A CZ2   1 
ATOM   2357 C CZ3   . TRP A 1 304 ? 30.34493 -34.50263 -0.64524  1.000 15.47460 ? 304  TRP A CZ3   1 
ATOM   2358 C CH2   . TRP A 1 304 ? 29.07506 -34.82999 -0.15074  1.000 18.07092 ? 304  TRP A CH2   1 
ATOM   2359 N N     . LEU A 1 305 ? 30.44406 -28.22969 -4.48651  1.000 12.57478 ? 305  LEU A N     1 
ATOM   2360 C CA    . LEU A 1 305 ? 30.24416 -27.01713 -3.69558  1.000 11.97741 ? 305  LEU A CA    1 
ATOM   2361 C C     . LEU A 1 305 ? 29.63363 -25.88305 -4.52439  1.000 12.93739 ? 305  LEU A C     1 
ATOM   2362 O O     . LEU A 1 305 ? 29.80779 -24.70881 -4.18175  1.000 10.59086 ? 305  LEU A O     1 
ATOM   2363 C CB    . LEU A 1 305 ? 31.55515 -26.55644 -3.04867  1.000 12.28048 ? 305  LEU A CB    1 
ATOM   2364 C CG    . LEU A 1 305 ? 31.38266 -25.77556 -1.74035  1.000 12.56974 ? 305  LEU A CG    1 
ATOM   2365 C CD1   . LEU A 1 305 ? 30.72392 -26.66057 -0.69188  1.000 15.76566 ? 305  LEU A CD1   1 
ATOM   2366 C CD2   . LEU A 1 305 ? 32.70400 -25.23046 -1.23296  1.000 14.15047 ? 305  LEU A CD2   1 
ATOM   2367 N N     . LEU A 1 306 ? 28.94584 -26.20667 -5.62239  1.000 10.85669 ? 306  LEU A N     1 
ATOM   2368 C CA    . LEU A 1 306 ? 28.04777 -25.29872 -6.33888  1.000 10.80684 ? 306  LEU A CA    1 
ATOM   2369 C C     . LEU A 1 306 ? 28.75389 -24.12753 -7.02040  1.000 12.01044 ? 306  LEU A C     1 
ATOM   2370 O O     . LEU A 1 306 ? 28.09892 -23.14768 -7.38507  1.000 12.36108 ? 306  LEU A O     1 
ATOM   2371 C CB    . LEU A 1 306 ? 26.94985 -24.76397 -5.41473  1.000 10.33977 ? 306  LEU A CB    1 
ATOM   2372 C CG    . LEU A 1 306 ? 25.95996 -25.81600 -4.91511  1.000 13.82610 ? 306  LEU A CG    1 
ATOM   2373 C CD1   . LEU A 1 306 ? 25.00918 -25.21546 -3.88943  1.000 14.87204 ? 306  LEU A CD1   1 
ATOM   2374 C CD2   . LEU A 1 306 ? 25.19646 -26.42053 -6.08708  1.000 14.84987 ? 306  LEU A CD2   1 
ATOM   2375 N N     . VAL A 1 307 ? 30.06500 -24.20019 -7.23132  1.000 12.55931 ? 307  VAL A N     1 
ATOM   2376 C CA    . VAL A 1 307 ? 30.80716 -23.18272 -7.97323  1.000 11.91705 ? 307  VAL A CA    1 
ATOM   2377 C C     . VAL A 1 307 ? 31.05193 -23.71370 -9.38026  1.000 12.89934 ? 307  VAL A C     1 
ATOM   2378 O O     . VAL A 1 307 ? 31.92646 -24.56031 -9.57964  1.000 12.06519 ? 307  VAL A O     1 
ATOM   2379 C CB    . VAL A 1 307 ? 32.12849 -22.82641 -7.27814  1.000 11.70244 ? 307  VAL A CB    1 
ATOM   2380 C CG1   . VAL A 1 307 ? 32.79968 -21.65215 -7.97547  1.000 12.08977 ? 307  VAL A CG1   1 
ATOM   2381 C CG2   . VAL A 1 307 ? 31.88010 -22.48381 -5.81744  1.000 12.05480 ? 307  VAL A CG2   1 
ATOM   2382 N N     . ASN A 1 308 ? 30.30057 -23.19831 -10.35870 1.000 12.74814 ? 308  ASN A N     1 
ATOM   2383 C CA    . ASN A 1 308 ? 30.33688 -23.72305 -11.72326 1.000 13.46500 ? 308  ASN A CA    1 
ATOM   2384 C C     . ASN A 1 308 ? 31.76446 -23.86584 -12.24332 1.000 13.05727 ? 308  ASN A C     1 
ATOM   2385 O O     . ASN A 1 308 ? 32.62203 -23.01323 -11.99972 1.000 14.05121 ? 308  ASN A O     1 
ATOM   2386 C CB    . ASN A 1 308 ? 29.54033 -22.81203 -12.66168 1.000 13.58586 ? 308  ASN A CB    1 
ATOM   2387 C CG    . ASN A 1 308 ? 28.08575 -22.66612 -12.25062 1.000 16.30181 ? 308  ASN A CG    1 
ATOM   2388 O OD1   . ASN A 1 308 ? 27.66899 -23.15340 -11.20087 1.000 15.29555 ? 308  ASN A OD1   1 
ATOM   2389 N ND2   . ASN A 1 308 ? 27.30737 -21.97683 -13.07814 1.000 21.63382 ? 308  ASN A ND2   1 
ATOM   2390 N N     . PHE A 1 309 ? 32.00540 -24.96669 -12.95870 1.000 14.99875 ? 309  PHE A N     1 
ATOM   2391 C CA    . PHE A 1 309 ? 33.28470 -25.21723 -13.61670 1.000 13.07477 ? 309  PHE A CA    1 
ATOM   2392 C C     . PHE A 1 309 ? 33.64851 -24.03550 -14.51039 1.000 15.89270 ? 309  PHE A C     1 
ATOM   2393 O O     . PHE A 1 309 ? 32.79849 -23.51932 -15.24092 1.000 18.38283 ? 309  PHE A O     1 
ATOM   2394 C CB    . PHE A 1 309 ? 33.16654 -26.51515 -14.42904 1.000 17.27196 ? 309  PHE A CB    1 
ATOM   2395 C CG    . PHE A 1 309 ? 34.44680 -26.98159 -15.07141 1.000 19.26412 ? 309  PHE A CG    1 
ATOM   2396 C CD1   . PHE A 1 309 ? 34.86059 -26.46863 -16.28511 1.000 20.81217 ? 309  PHE A CD1   1 
ATOM   2397 C CD2   . PHE A 1 309 ? 35.20686 -27.97939 -14.48151 1.000 19.63074 ? 309  PHE A CD2   1 
ATOM   2398 C CE1   . PHE A 1 309 ? 36.02300 -26.91119 -16.88669 1.000 20.47548 ? 309  PHE A CE1   1 
ATOM   2399 C CE2   . PHE A 1 309 ? 36.37316 -28.42825 -15.07779 1.000 21.72074 ? 309  PHE A CE2   1 
ATOM   2400 C CZ    . PHE A 1 309 ? 36.77972 -27.89126 -16.28364 1.000 21.86799 ? 309  PHE A CZ    1 
ATOM   2401 N N     . ASP A 1 310 ? 34.90999 -23.59931 -14.45842 1.000 14.74486 ? 310  ASP A N     1 
ATOM   2402 C CA    . ASP A 1 310 ? 35.98983 -24.25096 -13.71690 1.000 13.34835 ? 310  ASP A CA    1 
ATOM   2403 C C     . ASP A 1 310 ? 36.35422 -23.56257 -12.39918 1.000 14.66977 ? 310  ASP A C     1 
ATOM   2404 O O     . ASP A 1 310 ? 36.43518 -22.33692 -12.32493 1.000 16.22096 ? 310  ASP A O     1 
ATOM   2405 C CB    . ASP A 1 310 ? 37.23710 -24.33410 -14.60245 1.000 15.86582 ? 310  ASP A CB    1 
ATOM   2406 C CG    . ASP A 1 310 ? 37.60065 -22.99499 -15.22575 1.000 21.55254 ? 310  ASP A CG    1 
ATOM   2407 O OD1   . ASP A 1 310 ? 36.67670 -22.20741 -15.52472 1.000 22.79833 ? 310  ASP A OD1   1 
ATOM   2408 O OD2   . ASP A 1 310 ? 38.80553 -22.72615 -15.41630 1.000 18.12851 ? 310  ASP A OD2   1 
ATOM   2409 N N     . CYS A 1 311 ? 36.58404 -24.37689 -11.36398 1.000 11.65117 ? 311  CYS A N     1 
ATOM   2410 C CA    . CYS A 1 311 ? 37.03014 -23.88181 -10.05983 1.000 11.68101 ? 311  CYS A CA    1 
ATOM   2411 C C     . CYS A 1 311 ? 37.56590 -25.07269 -9.26560  1.000 12.40149 ? 311  CYS A C     1 
ATOM   2412 O O     . CYS A 1 311 ? 36.78310 -25.84148 -8.70210  1.000 13.03340 ? 311  CYS A O     1 
ATOM   2413 C CB    . CYS A 1 311 ? 35.90967 -23.18266 -9.30746  1.000 11.43220 ? 311  CYS A CB    1 
ATOM   2414 S SG    . CYS A 1 311 ? 36.44597 -22.48791 -7.71826  1.000 14.27035 ? 311  CYS A SG    1 
ATOM   2415 N N     . SER A 1 312 ? 38.88866 -25.20489 -9.22154  1.000 11.87125 ? 312  SER A N     1 
ATOM   2416 C CA    . SER A 1 312 ? 39.56114 -26.19556 -8.39238  1.000 12.18624 ? 312  SER A CA    1 
ATOM   2417 C C     . SER A 1 312 ? 40.43015 -25.46436 -7.37999  1.000 12.59247 ? 312  SER A C     1 
ATOM   2418 O O     . SER A 1 312 ? 41.20250 -24.57418 -7.75016  1.000 17.39334 ? 312  SER A O     1 
ATOM   2419 C CB    . SER A 1 312 ? 40.40708 -27.14894 -9.24138  1.000 13.05814 ? 312  SER A CB    1 
ATOM   2420 O OG    . SER A 1 312 ? 40.89538 -28.22853 -8.46289  1.000 13.00870 ? 312  SER A OG    1 
ATOM   2421 N N     . ALA A 1 313 ? 40.29954 -25.83596 -6.10820  1.000 12.43287 ? 313  ALA A N     1 
ATOM   2422 C CA    . ALA A 1 313 ? 40.95397 -25.13505 -5.01000  1.000 11.66138 ? 313  ALA A CA    1 
ATOM   2423 C C     . ALA A 1 313 ? 42.15533 -25.94106 -4.53131  1.000 13.14497 ? 313  ALA A C     1 
ATOM   2424 O O     . ALA A 1 313 ? 42.00214 -27.08679 -4.09367  1.000 12.76837 ? 313  ALA A O     1 
ATOM   2425 C CB    . ALA A 1 313 ? 39.97225 -24.90211 -3.86182  1.000 11.74666 ? 313  ALA A CB    1 
ATOM   2426 N N     . MET A 1 314 ? 43.34280 -25.33827 -4.59956  1.000 10.48941 ? 314  MET A N     1 
ATOM   2427 C CA    . MET A 1 314 ? 44.58249 -26.00945 -4.22908  1.000 12.66035 ? 314  MET A CA    1 
ATOM   2428 C C     . MET A 1 314 ? 45.33851 -25.17200 -3.20796  1.000 14.27901 ? 314  MET A C     1 
ATOM   2429 O O     . MET A 1 314 ? 45.56261 -23.97729 -3.42653  1.000 13.74626 ? 314  MET A O     1 
ATOM   2430 C CB    . MET A 1 314 ? 45.46055 -26.25508 -5.46015  1.000 12.68009 ? 314  MET A CB    1 
ATOM   2431 C CG    . MET A 1 314 ? 46.85886 -26.73548 -5.13100  1.000 17.37711 ? 314  MET A CG    1 
ATOM   2432 S SD    . MET A 1 314 ? 47.68458 -27.48796 -6.54370  1.000 27.29807 ? 314  MET A SD    1 
ATOM   2433 C CE    . MET A 1 314 ? 49.26349 -27.91354 -5.80930  1.000 19.35356 ? 314  MET A CE    1 
ATOM   2434 N N     . TRP A 1 315 ? 45.73124 -25.80051 -2.10027  1.000 13.90039 ? 315  TRP A N     1 
ATOM   2435 C CA    . TRP A 1 315 ? 46.54258 -25.16751 -1.07148  1.000 16.48815 ? 315  TRP A CA    1 
ATOM   2436 C C     . TRP A 1 315 ? 47.90300 -25.84842 -1.00314  1.000 17.02284 ? 315  TRP A C     1 
ATOM   2437 O O     . TRP A 1 315 ? 48.02328 -27.05067 -1.25490  1.000 15.07258 ? 315  TRP A O     1 
ATOM   2438 C CB    . TRP A 1 315 ? 45.87963 -25.24314 0.31353   1.000 14.32969 ? 315  TRP A CB    1 
ATOM   2439 C CG    . TRP A 1 315 ? 44.63572 -24.42860 0.45552   1.000 14.25799 ? 315  TRP A CG    1 
ATOM   2440 C CD1   . TRP A 1 315 ? 44.53089 -23.18485 1.00310   1.000 17.41019 ? 315  TRP A CD1   1 
ATOM   2441 C CD2   . TRP A 1 315 ? 43.30666 -24.82077 0.09144   1.000 13.80707 ? 315  TRP A CD2   1 
ATOM   2442 N NE1   . TRP A 1 315 ? 43.22288 -22.76513 0.97843   1.000 15.79538 ? 315  TRP A NE1   1 
ATOM   2443 C CE2   . TRP A 1 315 ? 42.45053 -23.75358 0.42759   1.000 13.50232 ? 315  TRP A CE2   1 
ATOM   2444 C CE3   . TRP A 1 315 ? 42.75944 -25.96619 -0.49484  1.000 15.72288 ? 315  TRP A CE3   1 
ATOM   2445 C CZ2   . TRP A 1 315 ? 41.07804 -23.79587 0.19516   1.000 13.65913 ? 315  TRP A CZ2   1 
ATOM   2446 C CZ3   . TRP A 1 315 ? 41.39548 -26.00725 -0.72373  1.000 13.33008 ? 315  TRP A CZ3   1 
ATOM   2447 C CH2   . TRP A 1 315 ? 40.57039 -24.92890 -0.37766  1.000 13.89637 ? 315  TRP A CH2   1 
ATOM   2448 N N     . VAL A 1 316 ? 48.92792 -25.07077 -0.65042  1.000 16.77575 ? 316  VAL A N     1 
ATOM   2449 C CA    . VAL A 1 316 ? 50.27507 -25.58363 -0.42784  1.000 18.48970 ? 316  VAL A CA    1 
ATOM   2450 C C     . VAL A 1 316 ? 50.79545 -25.01663 0.88546   1.000 22.17762 ? 316  VAL A C     1 
ATOM   2451 O O     . VAL A 1 316 ? 50.37449 -23.94334 1.32737   1.000 24.79670 ? 316  VAL A O     1 
ATOM   2452 C CB    . VAL A 1 316 ? 51.23589 -25.22825 -1.58632  1.000 21.61694 ? 316  VAL A CB    1 
ATOM   2453 C CG1   . VAL A 1 316 ? 50.85441 -25.97983 -2.85611  1.000 19.76803 ? 316  VAL A CG1   1 
ATOM   2454 C CG2   . VAL A 1 316 ? 51.24460 -23.72655 -1.82639  1.000 26.36851 ? 316  VAL A CG2   1 
ATOM   2455 N N     . LYS A 1 317 ? 51.72117 -25.74569 1.51412   1.000 22.44027 ? 317  LYS A N     1 
ATOM   2456 C CA    . LYS A 1 317 ? 52.30210 -25.26563 2.76275   1.000 26.89183 ? 317  LYS A CA    1 
ATOM   2457 C C     . LYS A 1 317 ? 53.41509 -24.25224 2.52566   1.000 31.36910 ? 317  LYS A C     1 
ATOM   2458 O O     . LYS A 1 317 ? 53.61593 -23.35807 3.35640   1.000 31.86157 ? 317  LYS A O     1 
ATOM   2459 C CB    . LYS A 1 317 ? 52.82810 -26.43623 3.59433   1.000 28.23510 ? 317  LYS A CB    1 
ATOM   2460 C CG    . LYS A 1 317 ? 51.74738 -27.18557 4.35319   1.000 24.47415 ? 317  LYS A CG    1 
ATOM   2461 C CD    . LYS A 1 317 ? 52.25368 -27.65106 5.70643   1.000 30.80185 ? 317  LYS A CD    1 
ATOM   2462 C CE    . LYS A 1 317 ? 51.59378 -28.94609 6.14011   1.000 26.35428 ? 317  LYS A CE    1 
ATOM   2463 N NZ    . LYS A 1 317 ? 52.57563 -30.05333 6.31295   1.000 26.31300 ? 317  LYS A NZ    1 
ATOM   2464 N N     . LYS A 1 318 ? 54.14229 -24.37094 1.41427   1.000 30.95444 ? 318  LYS A N     1 
ATOM   2465 C CA    . LYS A 1 318 ? 55.21950 -23.44675 1.06669   1.000 37.37600 ? 318  LYS A CA    1 
ATOM   2466 C C     . LYS A 1 318 ? 55.00441 -22.97861 -0.36457  1.000 36.76000 ? 318  LYS A C     1 
ATOM   2467 O O     . LYS A 1 318 ? 55.16520 -23.76198 -1.30719  1.000 37.85489 ? 318  LYS A O     1 
ATOM   2468 C CB    . LYS A 1 318 ? 56.59200 -24.10736 1.21159   1.000 40.89187 ? 318  LYS A CB    1 
ATOM   2469 C CG    . LYS A 1 318 ? 56.82433 -24.79793 2.54402   1.000 44.54124 ? 318  LYS A CG    1 
ATOM   2470 C CD    . LYS A 1 318 ? 56.65938 -23.83588 3.70040   1.000 45.30585 ? 318  LYS A CD    1 
ATOM   2471 C CE    . LYS A 1 318 ? 57.50505 -24.26439 4.87851   1.000 50.04426 ? 318  LYS A CE    1 
ATOM   2472 N NZ    . LYS A 1 318 ? 56.68045 -24.82347 5.98259   1.000 50.51259 ? 318  LYS A NZ    1 
ATOM   2473 N N     . ARG A 1 319 ? 54.65720 -21.69947 -0.52604  1.000 38.95742 ? 319  ARG A N     1 
ATOM   2474 C CA    . ARG A 1 319 ? 54.44550 -21.15283 -1.86275  1.000 42.83624 ? 319  ARG A CA    1 
ATOM   2475 C C     . ARG A 1 319 ? 55.73944 -21.10425 -2.66477  1.000 45.00749 ? 319  ARG A C     1 
ATOM   2476 O O     . ARG A 1 319 ? 55.70240 -21.15752 -3.89943  1.000 45.85688 ? 319  ARG A O     1 
ATOM   2477 C CB    . ARG A 1 319 ? 53.82825 -19.75739 -1.76698  1.000 40.66297 ? 319  ARG A CB    1 
ATOM   2478 C CG    . ARG A 1 319 ? 52.61041 -19.68467 -0.85947  1.000 42.50513 ? 319  ARG A CG    1 
ATOM   2479 C CD    . ARG A 1 319 ? 52.06960 -18.26877 -0.75826  1.000 44.89648 ? 319  ARG A CD    1 
ATOM   2480 N NE    . ARG A 1 319 ? 53.11028 -17.31935 -0.38719  1.000 47.06107 ? 319  ARG A NE    1 
ATOM   2481 C CZ    . ARG A 1 319 ? 53.13082 -16.64764 0.75487   1.000 48.94994 ? 319  ARG A CZ    1 
ATOM   2482 N NH1   . ARG A 1 319 ? 52.18174 -16.80197 1.66401   1.000 47.84134 ? 319  ARG A NH1   1 
ATOM   2483 N NH2   . ARG A 1 319 ? 54.13037 -15.80430 0.99306   1.000 52.34238 ? 319  ARG A NH2   1 
ATOM   2484 N N     . THR A 1 320 ? 56.88509 -21.00441 -1.98562  1.000 48.99361 ? 320  THR A N     1 
ATOM   2485 C CA    . THR A 1 320 ? 58.16592 -20.99737 -2.68475  1.000 53.17277 ? 320  THR A CA    1 
ATOM   2486 C C     . THR A 1 320 ? 58.36813 -22.28223 -3.47753  1.000 56.53419 ? 320  THR A C     1 
ATOM   2487 O O     . THR A 1 320 ? 58.98274 -22.27057 -4.55134  1.000 57.97845 ? 320  THR A O     1 
ATOM   2488 C CB    . THR A 1 320 ? 59.30617 -20.80545 -1.68740  1.000 53.52452 ? 320  THR A CB    1 
ATOM   2489 O OG1   . THR A 1 320 ? 58.99850 -21.49510 -0.46983  1.000 61.67738 ? 320  THR A OG1   1 
ATOM   2490 C CG2   . THR A 1 320 ? 59.51230 -19.33056 -1.38998  1.000 55.60362 ? 320  THR A CG2   1 
ATOM   2491 N N     . ASP A 1 321 ? 57.85406 -23.40216 -2.96462  1.000 51.87385 ? 321  ASP A N     1 
ATOM   2492 C CA    . ASP A 1 321 ? 57.97946 -24.67051 -3.67114  1.000 53.51090 ? 321  ASP A CA    1 
ATOM   2493 C C     . ASP A 1 321 ? 57.23592 -24.65880 -5.00090  1.000 52.50690 ? 321  ASP A C     1 
ATOM   2494 O O     . ASP A 1 321 ? 57.55149 -25.46285 -5.88571  1.000 49.88471 ? 321  ASP A O     1 
ATOM   2495 C CB    . ASP A 1 321 ? 57.46938 -25.80803 -2.78713  1.000 51.56553 ? 321  ASP A CB    1 
ATOM   2496 C CG    . ASP A 1 321 ? 58.48886 -26.24328 -1.75711  1.000 53.93745 ? 321  ASP A CG    1 
ATOM   2497 O OD1   . ASP A 1 321 ? 59.67001 -25.85777 -1.88893  1.000 54.28965 ? 321  ASP A OD1   1 
ATOM   2498 O OD2   . ASP A 1 321 ? 58.10678 -26.96773 -0.81509  1.000 54.03967 ? 321  ASP A OD2   1 
ATOM   2499 N N     . LEU A 1 322 ? 56.25781 -23.77208 -5.15987  1.000 52.58641 ? 322  LEU A N     1 
ATOM   2500 C CA    . LEU A 1 322 ? 55.60393 -23.57691 -6.44935  1.000 52.62207 ? 322  LEU A CA    1 
ATOM   2501 C C     . LEU A 1 322 ? 56.32527 -22.50280 -7.25457  1.000 55.56362 ? 322  LEU A C     1 
ATOM   2502 O O     . LEU A 1 322 ? 56.57680 -22.67219 -8.44764  1.000 57.99147 ? 322  LEU A O     1 
ATOM   2503 C CB    . LEU A 1 322 ? 54.13103 -23.19624 -6.27377  1.000 54.27879 ? 322  LEU A CB    1 
ATOM   2504 C CG    . LEU A 1 322 ? 53.19670 -24.23421 -5.65377  1.000 48.67166 ? 322  LEU A CG    1 
ATOM   2505 C CD1   . LEU A 1 322 ? 51.75086 -23.77902 -5.77218  1.000 44.35219 ? 322  LEU A CD1   1 
ATOM   2506 C CD2   . LEU A 1 322 ? 53.39051 -25.58568 -6.32080  1.000 44.86550 ? 322  LEU A CD2   1 
ATOM   2507 N N     . LEU A 1 342 ? 52.29755 -11.73521 1.15382   1.000 61.68147 ? 342  LEU A N     1 
ATOM   2508 C CA    . LEU A 1 342 ? 51.37007 -11.24505 0.14086   1.000 60.07191 ? 342  LEU A CA    1 
ATOM   2509 C C     . LEU A 1 342 ? 51.56038 -11.94531 -1.19874  1.000 61.08449 ? 342  LEU A C     1 
ATOM   2510 O O     . LEU A 1 342 ? 52.66853 -11.99990 -1.73224  1.000 60.58107 ? 342  LEU A O     1 
ATOM   2511 C CB    . LEU A 1 342 ? 51.52705 -9.73736  -0.04589  1.000 61.12529 ? 342  LEU A CB    1 
ATOM   2512 C CG    . LEU A 1 342 ? 50.65695 -9.11835  -1.14000  1.000 56.84090 ? 342  LEU A CG    1 
ATOM   2513 C CD1   . LEU A 1 342 ? 49.17382 -9.27276  -0.82788  1.000 52.21452 ? 342  LEU A CD1   1 
ATOM   2514 C CD2   . LEU A 1 342 ? 51.02147 -7.66088  -1.30713  1.000 48.80258 ? 342  LEU A CD2   1 
ATOM   2515 N N     . ILE A 1 343 ? 50.47040 -12.48263 -1.73538  1.000 55.34039 ? 343  ILE A N     1 
ATOM   2516 C CA    . ILE A 1 343 ? 50.47532 -13.09199 -3.05939  1.000 56.89564 ? 343  ILE A CA    1 
ATOM   2517 C C     . ILE A 1 343 ? 50.13935 -12.01776 -4.08457  1.000 59.26822 ? 343  ILE A C     1 
ATOM   2518 O O     . ILE A 1 343 ? 49.04256 -11.44870 -4.06484  1.000 56.53858 ? 343  ILE A O     1 
ATOM   2519 C CB    . ILE A 1 343 ? 49.48102 -14.25895 -3.14448  1.000 52.85080 ? 343  ILE A CB    1 
ATOM   2520 C CG1   . ILE A 1 343 ? 49.85746 -15.36710 -2.15848  1.000 51.15496 ? 343  ILE A CG1   1 
ATOM   2521 C CG2   . ILE A 1 343 ? 49.41459 -14.78691 -4.56894  1.000 52.09116 ? 343  ILE A CG2   1 
ATOM   2522 C CD1   . ILE A 1 343 ? 48.81791 -16.45984 -2.05438  1.000 48.96453 ? 343  ILE A CD1   1 
ATOM   2523 N N     . THR A 1 344 ? 51.08096 -11.73873 -4.98008  1.000 60.23587 ? 344  THR A N     1 
ATOM   2524 C CA    . THR A 1 344 ? 50.85426 -10.81840 -6.08721  1.000 59.50498 ? 344  THR A CA    1 
ATOM   2525 C C     . THR A 1 344 ? 50.76125 -11.51600 -7.43303  1.000 60.48319 ? 344  THR A C     1 
ATOM   2526 O O     . THR A 1 344 ? 49.96260 -11.10812 -8.27895  1.000 54.14157 ? 344  THR A O     1 
ATOM   2527 C CB    . THR A 1 344 ? 51.96625 -9.76304  -6.14385  1.000 57.83754 ? 344  THR A CB    1 
ATOM   2528 O OG1   . THR A 1 344 ? 53.22723 -10.37302 -5.83938  1.000 63.69790 ? 344  THR A OG1   1 
ATOM   2529 C CG2   . THR A 1 344 ? 51.68903 -8.64167  -5.15201  1.000 52.36149 ? 344  THR A CG2   1 
ATOM   2530 N N     . ASP A 1 345 ? 51.54980 -12.56473 -7.65034  1.000 77.50748 ? 345  ASP A N     1 
ATOM   2531 C CA    . ASP A 1 345 ? 51.55522 -13.29267 -8.90864  1.000 77.77166 ? 345  ASP A CA    1 
ATOM   2532 C C     . ASP A 1 345 ? 51.09046 -14.72598 -8.69314  1.000 80.35351 ? 345  ASP A C     1 
ATOM   2533 O O     . ASP A 1 345 ? 51.29187 -15.31250 -7.62501  1.000 82.72635 ? 345  ASP A O     1 
ATOM   2534 C CB    . ASP A 1 345 ? 52.94757 -13.28937 -9.55355  1.000 78.18200 ? 345  ASP A CB    1 
ATOM   2535 C CG    . ASP A 1 345 ? 52.91142 -12.87609 -11.01488 1.000 80.60915 ? 345  ASP A CG    1 
ATOM   2536 O OD1   . ASP A 1 345 ? 51.84744 -13.03223 -11.65114 1.000 85.80193 ? 345  ASP A OD1   1 
ATOM   2537 O OD2   . ASP A 1 345 ? 53.94558 -12.39917 -11.52862 1.000 87.35111 ? 345  ASP A OD2   1 
ATOM   2538 N N     . TYR A 1 346 ? 50.46078 -15.27877 -9.72730  1.000 66.28832 ? 346  TYR A N     1 
ATOM   2539 C CA    . TYR A 1 346 ? 49.93513 -16.63628 -9.71430  1.000 60.11037 ? 346  TYR A CA    1 
ATOM   2540 C C     . TYR A 1 346 ? 50.50119 -17.43848 -10.88089 1.000 62.11284 ? 346  TYR A C     1 
ATOM   2541 O O     . TYR A 1 346 ? 49.90673 -18.42652 -11.31523 1.000 54.73206 ? 346  TYR A O     1 
ATOM   2542 C CB    . TYR A 1 346 ? 48.40567 -16.61869 -9.76050  1.000 51.42175 ? 346  TYR A CB    1 
ATOM   2543 C CG    . TYR A 1 346 ? 47.73151 -16.64815 -8.40490  1.000 45.83126 ? 346  TYR A CG    1 
ATOM   2544 C CD1   . TYR A 1 346 ? 48.27462 -17.36672 -7.34844  1.000 44.40754 ? 346  TYR A CD1   1 
ATOM   2545 C CD2   . TYR A 1 346 ? 46.54525 -15.95771 -8.18513  1.000 36.49735 ? 346  TYR A CD2   1 
ATOM   2546 C CE1   . TYR A 1 346 ? 47.65492 -17.39681 -6.10729  1.000 40.73824 ? 346  TYR A CE1   1 
ATOM   2547 C CE2   . TYR A 1 346 ? 45.91894 -15.97962 -6.94938  1.000 31.37656 ? 346  TYR A CE2   1 
ATOM   2548 C CZ    . TYR A 1 346 ? 46.47842 -16.70069 -5.91340  1.000 36.78614 ? 346  TYR A CZ    1 
ATOM   2549 O OH    . TYR A 1 346 ? 45.86232 -16.72874 -4.68076  1.000 30.77410 ? 346  TYR A OH    1 
ATOM   2550 N N     . GLN A 1 347 ? 51.65477 -17.01278 -11.39509 1.000 70.83524 ? 347  GLN A N     1 
ATOM   2551 C CA    . GLN A 1 347 ? 52.20980 -17.60043 -12.60850 1.000 71.00591 ? 347  GLN A CA    1 
ATOM   2552 C C     . GLN A 1 347 ? 52.76532 -18.99883 -12.35900 1.000 70.80091 ? 347  GLN A C     1 
ATOM   2553 O O     . GLN A 1 347 ? 52.37826 -19.95735 -13.03602 1.000 70.50548 ? 347  GLN A O     1 
ATOM   2554 C CB    . GLN A 1 347 ? 53.30071 -16.68670 -13.16708 1.000 71.80674 ? 347  GLN A CB    1 
ATOM   2555 C CG    . GLN A 1 347 ? 52.79778 -15.35370 -13.68591 1.000 72.76702 ? 347  GLN A CG    1 
ATOM   2556 C CD    . GLN A 1 347 ? 53.92943 -14.47077 -14.15741 1.000 79.87209 ? 347  GLN A CD    1 
ATOM   2557 O OE1   . GLN A 1 347 ? 55.06457 -14.61669 -13.70793 1.000 80.81782 ? 347  GLN A OE1   1 
ATOM   2558 N NE2   . GLN A 1 347 ? 53.62939 -13.54582 -15.06312 1.000 76.49617 ? 347  GLN A NE2   1 
ATOM   2559 N N     . HIS A 1 348 ? 53.67512 -19.13310 -11.39340 1.000 61.49254 ? 348  HIS A N     1 
ATOM   2560 C CA    . HIS A 1 348 ? 54.34393 -20.39629 -11.10271 1.000 60.77719 ? 348  HIS A CA    1 
ATOM   2561 C C     . HIS A 1 348 ? 53.47085 -21.34891 -10.29401 1.000 57.81117 ? 348  HIS A C     1 
ATOM   2562 O O     . HIS A 1 348 ? 53.94104 -22.42189 -9.89886  1.000 57.54109 ? 348  HIS A O     1 
ATOM   2563 C CB    . HIS A 1 348 ? 55.66083 -20.12145 -10.37082 1.000 63.40238 ? 348  HIS A CB    1 
ATOM   2564 C CG    . HIS A 1 348 ? 56.54192 -19.14060 -11.07887 1.000 68.52863 ? 348  HIS A CG    1 
ATOM   2565 N ND1   . HIS A 1 348 ? 57.08904 -19.39176 -12.31886 1.000 69.31854 ? 348  HIS A ND1   1 
ATOM   2566 C CD2   . HIS A 1 348 ? 56.94841 -17.89631 -10.73255 1.000 71.00057 ? 348  HIS A CD2   1 
ATOM   2567 C CE1   . HIS A 1 348 ? 57.80704 -18.34998 -12.69874 1.000 73.29162 ? 348  HIS A CE1   1 
ATOM   2568 N NE2   . HIS A 1 348 ? 57.73719 -17.42844 -11.75482 1.000 74.74817 ? 348  HIS A NE2   1 
ATOM   2569 N N     . TRP A 1 349 ? 52.21508 -20.96543 -10.04926 1.000 54.59737 ? 349  TRP A N     1 
ATOM   2570 C CA    . TRP A 1 349 ? 51.23198 -21.77680 -9.34321  1.000 48.49219 ? 349  TRP A CA    1 
ATOM   2571 C C     . TRP A 1 349 ? 50.47171 -22.72311 -10.26130 1.000 39.00827 ? 349  TRP A C     1 
ATOM   2572 O O     . TRP A 1 349 ? 49.98545 -23.76246 -9.80048  1.000 37.84784 ? 349  TRP A O     1 
ATOM   2573 C CB    . TRP A 1 349 ? 50.21593 -20.87597 -8.63411  1.000 46.01347 ? 349  TRP A CB    1 
ATOM   2574 C CG    . TRP A 1 349 ? 50.78019 -20.00646 -7.55818  1.000 49.59514 ? 349  TRP A CG    1 
ATOM   2575 C CD1   . TRP A 1 349 ? 51.62328 -18.94560 -7.71593  1.000 51.97727 ? 349  TRP A CD1   1 
ATOM   2576 C CD2   . TRP A 1 349 ? 50.49870 -20.08925 -6.15696  1.000 46.38465 ? 349  TRP A CD2   1 
ATOM   2577 N NE1   . TRP A 1 349 ? 51.90655 -18.38178 -6.49593  1.000 51.30448 ? 349  TRP A NE1   1 
ATOM   2578 C CE2   . TRP A 1 349 ? 51.22532 -19.06438 -5.52318  1.000 48.88938 ? 349  TRP A CE2   1 
ATOM   2579 C CE3   . TRP A 1 349 ? 49.71196 -20.94021 -5.37419  1.000 42.16154 ? 349  TRP A CE3   1 
ATOM   2580 C CZ2   . TRP A 1 349 ? 51.18722 -18.86710 -4.14447  1.000 45.61360 ? 349  TRP A CZ2   1 
ATOM   2581 C CZ3   . TRP A 1 349 ? 49.67407 -20.74204 -4.00707  1.000 38.14576 ? 349  TRP A CZ3   1 
ATOM   2582 C CH2   . TRP A 1 349 ? 50.40453 -19.71434 -3.40716  1.000 40.88471 ? 349  TRP A CH2   1 
ATOM   2583 N N     . GLN A 1 350 ? 50.33143 -22.37735 -11.53777 1.000 36.74075 ? 350  GLN A N     1 
ATOM   2584 C CA    . GLN A 1 350 ? 49.49204 -23.12479 -12.46159 1.000 33.56612 ? 350  GLN A CA    1 
ATOM   2585 C C     . GLN A 1 350 ? 50.30157 -23.49370 -13.69746 1.000 34.68165 ? 350  GLN A C     1 
ATOM   2586 O O     . GLN A 1 350 ? 51.50256 -23.21739 -13.79476 1.000 37.47555 ? 350  GLN A O     1 
ATOM   2587 C CB    . GLN A 1 350 ? 48.24602 -22.32508 -12.86152 1.000 34.60943 ? 350  GLN A CB    1 
ATOM   2588 C CG    . GLN A 1 350 ? 48.49879 -20.83148 -13.00175 1.000 41.80766 ? 350  GLN A CG    1 
ATOM   2589 C CD    . GLN A 1 350 ? 47.26150 -20.04566 -13.40365 1.000 39.93714 ? 350  GLN A CD    1 
ATOM   2590 O OE1   . GLN A 1 350 ? 46.29174 -19.95732 -12.65157 1.000 36.03808 ? 350  GLN A OE1   1 
ATOM   2591 N NE2   . GLN A 1 350 ? 47.29615 -19.46264 -14.59894 1.000 37.02712 ? 350  GLN A NE2   1 
ATOM   2592 N N     . ILE A 1 351 ? 49.62503 -24.11629 -14.65641 1.000 28.35634 ? 351  ILE A N     1 
ATOM   2593 C CA    . ILE A 1 351 ? 50.26966 -24.53278 -15.89634 1.000 30.80730 ? 351  ILE A CA    1 
ATOM   2594 C C     . ILE A 1 351 ? 50.09094 -23.42712 -16.93743 1.000 30.33804 ? 351  ILE A C     1 
ATOM   2595 O O     . ILE A 1 351 ? 51.07232 -23.08136 -17.61116 1.000 30.77779 ? 351  ILE A O     1 
ATOM   2596 C CB    . ILE A 1 351 ? 49.73682 -25.89453 -16.37816 1.000 31.59694 ? 351  ILE A CB    1 
ATOM   2597 C CG1   . ILE A 1 351 ? 49.93227 -26.96977 -15.30624 1.000 30.19303 ? 351  ILE A CG1   1 
ATOM   2598 C CG2   . ILE A 1 351 ? 50.49243 -26.35010 -17.61393 1.000 34.29344 ? 351  ILE A CG2   1 
ATOM   2599 C CD1   . ILE A 1 351 ? 51.34255 -27.03531 -14.73248 1.000 29.88365 ? 351  ILE A CD1   1 
ATOM   2600 N N     . PRO A 1 352 ? 48.90985 -22.82355 -17.11092 1.000 29.65201 ? 352  PRO A N     1 
ATOM   2601 C CA    . PRO A 1 352 ? 48.81975 -21.65329 -17.99317 1.000 26.53636 ? 352  PRO A CA    1 
ATOM   2602 C C     . PRO A 1 352 ? 49.30575 -20.38895 -17.28911 1.000 30.39918 ? 352  PRO A C     1 
ATOM   2603 O O     . PRO A 1 352 ? 49.50016 -20.35139 -16.07378 1.000 30.57123 ? 352  PRO A O     1 
ATOM   2604 C CB    . PRO A 1 352 ? 47.32293 -21.56387 -18.32819 1.000 25.45339 ? 352  PRO A CB    1 
ATOM   2605 C CG    . PRO A 1 352 ? 46.65306 -22.21906 -17.19846 1.000 27.62749 ? 352  PRO A CG    1 
ATOM   2606 C CD    . PRO A 1 352 ? 47.56244 -23.33548 -16.77767 1.000 27.89036 ? 352  PRO A CD    1 
ATOM   2607 N N     . LEU A 1 353 ? 49.52110 -19.34171 -18.08941 1.000 28.00473 ? 353  LEU A N     1 
ATOM   2608 C CA    . LEU A 1 353 ? 49.80192 -18.02275 -17.52778 1.000 29.02238 ? 353  LEU A CA    1 
ATOM   2609 C C     . LEU A 1 353 ? 48.54822 -17.16421 -17.38768 1.000 29.07604 ? 353  LEU A C     1 
ATOM   2610 O O     . LEU A 1 353 ? 48.38911 -16.46792 -16.37984 1.000 30.35585 ? 353  LEU A O     1 
ATOM   2611 C CB    . LEU A 1 353 ? 50.85488 -17.28726 -18.36269 1.000 30.69553 ? 353  LEU A CB    1 
ATOM   2612 C CG    . LEU A 1 353 ? 52.29623 -17.79059 -18.27521 1.000 34.92198 ? 353  LEU A CG    1 
ATOM   2613 C CD1   . LEU A 1 353 ? 53.14102 -17.16601 -19.39834 1.000 34.59093 ? 353  LEU A CD1   1 
ATOM   2614 C CD2   . LEU A 1 353 ? 52.86760 -17.40591 -16.91397 1.000 42.91874 ? 353  LEU A CD2   1 
ATOM   2615 N N     . GLY A 1 354 ? 47.64452 -17.21082 -18.36739 1.000 27.54999 ? 354  GLY A N     1 
ATOM   2616 C CA    . GLY A 1 354 ? 46.42685 -16.43821 -18.28473 1.000 28.19145 ? 354  GLY A CA    1 
ATOM   2617 C C     . GLY A 1 354 ? 45.35375 -17.12672 -17.45947 1.000 24.59692 ? 354  GLY A C     1 
ATOM   2618 O O     . GLY A 1 354 ? 45.35884 -18.34343 -17.28247 1.000 25.38166 ? 354  GLY A O     1 
ATOM   2619 N N     . ARG A 1 355 ? 44.42613 -16.32123 -16.94031 1.000 24.15234 ? 355  ARG A N     1 
ATOM   2620 C CA    . ARG A 1 355 ? 43.35814 -16.84235 -16.09734 1.000 21.71160 ? 355  ARG A CA    1 
ATOM   2621 C C     . ARG A 1 355 ? 42.21540 -15.83826 -16.03923 1.000 25.40813 ? 355  ARG A C     1 
ATOM   2622 O O     . ARG A 1 355 ? 42.40028 -14.64208 -16.27913 1.000 23.52028 ? 355  ARG A O     1 
ATOM   2623 C CB    . ARG A 1 355 ? 43.86422 -17.15551 -14.68508 1.000 23.94144 ? 355  ARG A CB    1 
ATOM   2624 C CG    . ARG A 1 355 ? 44.58302 -15.99429 -14.01568 1.000 26.68957 ? 355  ARG A CG    1 
ATOM   2625 C CD    . ARG A 1 355 ? 45.76318 -16.48989 -13.19681 1.000 27.79219 ? 355  ARG A CD    1 
ATOM   2626 N NE    . ARG A 1 355 ? 45.39782 -17.62677 -12.36317 1.000 29.27365 ? 355  ARG A NE    1 
ATOM   2627 C CZ    . ARG A 1 355 ? 44.72351 -17.53774 -11.22512 1.000 28.76983 ? 355  ARG A CZ    1 
ATOM   2628 N NH1   . ARG A 1 355 ? 44.33986 -16.36835 -10.73772 1.000 25.39607 ? 355  ARG A NH1   1 
ATOM   2629 N NH2   . ARG A 1 355 ? 44.42363 -18.65073 -10.56035 1.000 21.00380 ? 355  ARG A NH2   1 
ATOM   2630 N N     . ARG A 1 356 ? 41.02875 -16.34954 -15.71142 1.000 22.47638 ? 356  ARG A N     1 
ATOM   2631 C CA    . ARG A 1 356 ? 39.82472 -15.54666 -15.55046 1.000 23.50588 ? 356  ARG A CA    1 
ATOM   2632 C C     . ARG A 1 356 ? 39.64844 -15.10836 -14.10028 1.000 20.38965 ? 356  ARG A C     1 
ATOM   2633 O O     . ARG A 1 356 ? 40.34242 -15.56558 -13.18997 1.000 22.42070 ? 356  ARG A O     1 
ATOM   2634 C CB    . ARG A 1 356 ? 38.58154 -16.32274 -15.98844 1.000 26.36095 ? 356  ARG A CB    1 
ATOM   2635 C CG    . ARG A 1 356 ? 38.57488 -16.76517 -17.42489 1.000 28.38598 ? 356  ARG A CG    1 
ATOM   2636 C CD    . ARG A 1 356 ? 37.18225 -17.18010 -17.86268 1.000 20.87355 ? 356  ARG A CD    1 
ATOM   2637 N NE    . ARG A 1 356 ? 36.78384 -18.47098 -17.31191 1.000 21.30473 ? 356  ARG A NE    1 
ATOM   2638 C CZ    . ARG A 1 356 ? 35.54425 -18.77601 -16.95320 1.000 22.29451 ? 356  ARG A CZ    1 
ATOM   2639 N NH1   . ARG A 1 356 ? 34.55806 -17.90111 -17.06531 1.000 24.61325 ? 356  ARG A NH1   1 
ATOM   2640 N NH2   . ARG A 1 356 ? 35.28790 -19.98742 -16.46801 1.000 22.52204 ? 356  ARG A NH2   1 
ATOM   2641 N N     . PHE A 1 357 ? 38.66996 -14.22494 -13.89613 1.000 19.60810 ? 357  PHE A N     1 
ATOM   2642 C CA    . PHE A 1 357 ? 38.29144 -13.73684 -12.57062 1.000 18.10271 ? 357  PHE A CA    1 
ATOM   2643 C C     . PHE A 1 357 ? 37.36870 -14.75404 -11.88912 1.000 17.36307 ? 357  PHE A C     1 
ATOM   2644 O O     . PHE A 1 357 ? 36.24485 -14.45791 -11.48364 1.000 17.49949 ? 357  PHE A O     1 
ATOM   2645 C CB    . PHE A 1 357 ? 37.62372 -12.37221 -12.70616 1.000 16.00553 ? 357  PHE A CB    1 
ATOM   2646 C CG    . PHE A 1 357 ? 37.66472 -11.52439 -11.45625 1.000 18.97313 ? 357  PHE A CG    1 
ATOM   2647 C CD1   . PHE A 1 357 ? 37.94877 -12.07415 -10.21466 1.000 16.11220 ? 357  PHE A CD1   1 
ATOM   2648 C CD2   . PHE A 1 357 ? 37.40888 -10.16307 -11.53361 1.000 21.29635 ? 357  PHE A CD2   1 
ATOM   2649 C CE1   . PHE A 1 357 ? 37.97827 -11.27972 -9.07734  1.000 16.37096 ? 357  PHE A CE1   1 
ATOM   2650 C CE2   . PHE A 1 357 ? 37.43867 -9.36561  -10.40151 1.000 20.70117 ? 357  PHE A CE2   1 
ATOM   2651 C CZ    . PHE A 1 357 ? 37.72367 -9.92471  -9.17307  1.000 20.73217 ? 357  PHE A CZ    1 
ATOM   2652 N N     . ARG A 1 358 ? 37.87364 -15.98534 -11.77110 1.000 15.53159 ? 358  ARG A N     1 
ATOM   2653 C CA    . ARG A 1 358 ? 37.05922 -17.09008 -11.27390 1.000 16.03070 ? 358  ARG A CA    1 
ATOM   2654 C C     . ARG A 1 358 ? 36.71823 -16.96116 -9.79477  1.000 16.63758 ? 358  ARG A C     1 
ATOM   2655 O O     . ARG A 1 358 ? 35.75677 -17.59131 -9.34108  1.000 16.39276 ? 358  ARG A O     1 
ATOM   2656 C CB    . ARG A 1 358 ? 37.76729 -18.42216 -11.53323 1.000 18.91990 ? 358  ARG A CB    1 
ATOM   2657 C CG    . ARG A 1 358 ? 37.94766 -18.74020 -13.01100 1.000 21.39891 ? 358  ARG A CG    1 
ATOM   2658 C CD    . ARG A 1 358 ? 38.79722 -19.98447 -13.22889 1.000 18.15353 ? 358  ARG A CD    1 
ATOM   2659 N NE    . ARG A 1 358 ? 40.16647 -19.79719 -12.76389 1.000 17.09600 ? 358  ARG A NE    1 
ATOM   2660 C CZ    . ARG A 1 358 ? 41.19069 -20.56119 -13.12000 1.000 19.50709 ? 358  ARG A CZ    1 
ATOM   2661 N NH1   . ARG A 1 358 ? 41.03484 -21.59002 -13.93718 1.000 17.38312 ? 358  ARG A NH1   1 
ATOM   2662 N NH2   . ARG A 1 358 ? 42.40270 -20.28275 -12.64852 1.000 16.95596 ? 358  ARG A NH2   1 
ATOM   2663 N N     . SER A 1 359 ? 37.46925 -16.16257 -9.03322  1.000 13.42135 ? 359  SER A N     1 
ATOM   2664 C CA    . SER A 1 359 ? 37.15711 -16.00294 -7.61819  1.000 14.09035 ? 359  SER A CA    1 
ATOM   2665 C C     . SER A 1 359 ? 35.82210 -15.30403 -7.40157  1.000 13.29834 ? 359  SER A C     1 
ATOM   2666 O O     . SER A 1 359 ? 35.25169 -15.40874 -6.31048  1.000 12.79691 ? 359  SER A O     1 
ATOM   2667 C CB    . SER A 1 359 ? 38.26473 -15.22543 -6.91037  1.000 13.51682 ? 359  SER A CB    1 
ATOM   2668 O OG    . SER A 1 359 ? 38.54248 -14.00931 -7.57734  1.000 15.72753 ? 359  SER A OG    1 
ATOM   2669 N N     . LEU A 1 360 ? 35.31730 -14.58913 -8.41049  1.000 11.98647 ? 360  LEU A N     1 
ATOM   2670 C CA    . LEU A 1 360 ? 33.99506 -13.98474 -8.29459  1.000 14.24772 ? 360  LEU A CA    1 
ATOM   2671 C C     . LEU A 1 360 ? 32.92557 -15.04842 -8.08509  1.000 13.25079 ? 360  LEU A C     1 
ATOM   2672 O O     . LEU A 1 360 ? 31.96227 -14.83111 -7.34083  1.000 12.67053 ? 360  LEU A O     1 
ATOM   2673 C CB    . LEU A 1 360 ? 33.68229 -13.15768 -9.54093  1.000 14.53726 ? 360  LEU A CB    1 
ATOM   2674 C CG    . LEU A 1 360 ? 34.24023 -11.73683 -9.60031  1.000 17.68432 ? 360  LEU A CG    1 
ATOM   2675 C CD1   . LEU A 1 360 ? 33.99792 -11.14977 -10.98104 1.000 17.79344 ? 360  LEU A CD1   1 
ATOM   2676 C CD2   . LEU A 1 360 ? 33.62938 -10.85434 -8.52042  1.000 16.58615 ? 360  LEU A CD2   1 
ATOM   2677 N N     . LYS A 1 361 ? 33.08045 -16.20918 -8.73211  1.000 11.35313 ? 361  LYS A N     1 
ATOM   2678 C CA    . LYS A 1 361 ? 32.11097 -17.28601 -8.55785  1.000 12.99183 ? 361  LYS A CA    1 
ATOM   2679 C C     . LYS A 1 361 ? 32.09580 -17.79426 -7.12205  1.000 13.51805 ? 361  LYS A C     1 
ATOM   2680 O O     . LYS A 1 361 ? 31.02122 -17.99144 -6.54434  1.000 12.52536 ? 361  LYS A O     1 
ATOM   2681 C CB    . LYS A 1 361 ? 32.39378 -18.43374 -9.52794  1.000 13.32739 ? 361  LYS A CB    1 
ATOM   2682 C CG    . LYS A 1 361 ? 32.05142 -18.13478 -10.97884 1.000 16.51289 ? 361  LYS A CG    1 
ATOM   2683 C CD    . LYS A 1 361 ? 32.31546 -19.35181 -11.85173 1.000 13.33950 ? 361  LYS A CD    1 
ATOM   2684 C CE    . LYS A 1 361 ? 33.79650 -19.69429 -11.91630 1.000 14.43539 ? 361  LYS A CE    1 
ATOM   2685 N NZ    . LYS A 1 361 ? 34.04642 -20.80858 -12.87678 1.000 15.25036 ? 361  LYS A NZ    1 
ATOM   2686 N N     . MET A 1 362 ? 33.27339 -18.01566 -6.52575  1.000 12.36480 ? 362  MET A N     1 
ATOM   2687 C CA    . MET A 1 362 ? 33.30563 -18.43999 -5.12810  1.000 12.32611 ? 362  MET A CA    1 
ATOM   2688 C C     . MET A 1 362 ? 32.70710 -17.37574 -4.21907  1.000 11.79672 ? 362  MET A C     1 
ATOM   2689 O O     . MET A 1 362 ? 31.93792 -17.69197 -3.30466  1.000 12.06417 ? 362  MET A O     1 
ATOM   2690 C CB    . MET A 1 362 ? 34.73346 -18.77654 -4.69052  1.000 12.32894 ? 362  MET A CB    1 
ATOM   2691 C CG    . MET A 1 362 ? 35.51406 -19.67755 -5.63420  1.000 11.41360 ? 362  MET A CG    1 
ATOM   2692 S SD    . MET A 1 362 ? 37.26823 -19.77391 -5.20714  1.000 15.13516 ? 362  MET A SD    1 
ATOM   2693 C CE    . MET A 1 362 ? 37.21786 -20.80293 -3.74806  1.000 15.45844 ? 362  MET A CE    1 
ATOM   2694 N N     . TRP A 1 363 ? 33.03555 -16.10692 -4.46750  1.000 11.71577 ? 363  TRP A N     1 
ATOM   2695 C CA    . TRP A 1 363 ? 32.52219 -15.02186 -3.63713  1.000 12.21633 ? 363  TRP A CA    1 
ATOM   2696 C C     . TRP A 1 363 ? 30.99860 -14.95706 -3.70181  1.000 12.34146 ? 363  TRP A C     1 
ATOM   2697 O O     . TRP A 1 363 ? 30.32657 -14.86052 -2.66893  1.000 12.95785 ? 363  TRP A O     1 
ATOM   2698 C CB    . TRP A 1 363 ? 33.16694 -13.70507 -4.08041  1.000 11.80962 ? 363  TRP A CB    1 
ATOM   2699 C CG    . TRP A 1 363 ? 33.07246 -12.54820 -3.12092  1.000 13.88573 ? 363  TRP A CG    1 
ATOM   2700 C CD1   . TRP A 1 363 ? 33.23598 -12.58247 -1.76526  1.000 15.10203 ? 363  TRP A CD1   1 
ATOM   2701 C CD2   . TRP A 1 363 ? 32.88862 -11.16808 -3.46632  1.000 15.97744 ? 363  TRP A CD2   1 
ATOM   2702 N NE1   . TRP A 1 363 ? 33.11975 -11.31477 -1.24182  1.000 15.94173 ? 363  TRP A NE1   1 
ATOM   2703 C CE2   . TRP A 1 363 ? 32.90931 -10.42913 -2.26662  1.000 16.53524 ? 363  TRP A CE2   1 
ATOM   2704 C CE3   . TRP A 1 363 ? 32.68884 -10.48942 -4.67292  1.000 16.36691 ? 363  TRP A CE3   1 
ATOM   2705 C CZ2   . TRP A 1 363 ? 32.73860 -9.04492  -2.23930  1.000 18.38024 ? 363  TRP A CZ2   1 
ATOM   2706 C CZ3   . TRP A 1 363 ? 32.51785 -9.11497  -4.64274  1.000 18.09994 ? 363  TRP A CZ3   1 
ATOM   2707 C CH2   . TRP A 1 363 ? 32.54367 -8.40902  -3.43466  1.000 18.63579 ? 363  TRP A CH2   1 
ATOM   2708 N N     . PHE A 1 364 ? 30.43195 -15.05032 -4.90901  1.000 11.70643 ? 364  PHE A N     1 
ATOM   2709 C CA    . PHE A 1 364 ? 28.97820 -14.98976 -5.05129  1.000 12.03075 ? 364  PHE A CA    1 
ATOM   2710 C C     . PHE A 1 364 ? 28.30218 -16.19369 -4.40055  1.000 12.93019 ? 364  PHE A C     1 
ATOM   2711 O O     . PHE A 1 364 ? 27.27933 -16.04505 -3.72089  1.000 12.51483 ? 364  PHE A O     1 
ATOM   2712 C CB    . PHE A 1 364 ? 28.59243 -14.90388 -6.53039  1.000 11.93658 ? 364  PHE A CB    1 
ATOM   2713 C CG    . PHE A 1 364 ? 28.60785 -13.50556 -7.08878  1.000 11.72488 ? 364  PHE A CG    1 
ATOM   2714 C CD1   . PHE A 1 364 ? 29.64096 -12.63270 -6.78829  1.000 14.01826 ? 364  PHE A CD1   1 
ATOM   2715 C CD2   . PHE A 1 364 ? 27.58069 -13.06216 -7.90631  1.000 14.94391 ? 364  PHE A CD2   1 
ATOM   2716 C CE1   . PHE A 1 364 ? 29.65487 -11.34658 -7.30267  1.000 14.43056 ? 364  PHE A CE1   1 
ATOM   2717 C CE2   . PHE A 1 364 ? 27.58765 -11.77761 -8.42049  1.000 15.20594 ? 364  PHE A CE2   1 
ATOM   2718 C CZ    . PHE A 1 364 ? 28.62594 -10.92001 -8.11786  1.000 14.57743 ? 364  PHE A CZ    1 
ATOM   2719 N N     . VAL A 1 365 ? 28.85409 -17.39409 -4.60252  1.000 12.19803 ? 365  VAL A N     1 
ATOM   2720 C CA    . VAL A 1 365 ? 28.24110 -18.60551 -4.05866  1.000 11.23080 ? 365  VAL A CA    1 
ATOM   2721 C C     . VAL A 1 365 ? 28.31753 -18.61124 -2.53766  1.000 14.35387 ? 365  VAL A C     1 
ATOM   2722 O O     . VAL A 1 365 ? 27.32226 -18.87517 -1.85153  1.000 13.98131 ? 365  VAL A O     1 
ATOM   2723 C CB    . VAL A 1 365 ? 28.90624 -19.85821 -4.65632  1.000 10.88010 ? 365  VAL A CB    1 
ATOM   2724 C CG1   . VAL A 1 365 ? 28.47871 -21.10320 -3.88870  1.000 13.07372 ? 365  VAL A CG1   1 
ATOM   2725 C CG2   . VAL A 1 365 ? 28.55278 -19.99435 -6.12570  1.000 12.48011 ? 365  VAL A CG2   1 
ATOM   2726 N N     . PHE A 1 366 ? 29.50497 -18.33756 -1.98858  1.000 11.50222 ? 366  PHE A N     1 
ATOM   2727 C CA    . PHE A 1 366 ? 29.66622 -18.33663 -0.53676  1.000 14.57057 ? 366  PHE A CA    1 
ATOM   2728 C C     . PHE A 1 366 ? 28.75243 -17.31163 0.12150   1.000 12.98492 ? 366  PHE A C     1 
ATOM   2729 O O     . PHE A 1 366 ? 28.19949 -17.56181 1.19840   1.000 13.43754 ? 366  PHE A O     1 
ATOM   2730 C CB    . PHE A 1 366 ? 31.12348 -18.06015 -0.15850  1.000 11.90899 ? 366  PHE A CB    1 
ATOM   2731 C CG    . PHE A 1 366 ? 32.09501 -19.10651 -0.63316  1.000 14.79459 ? 366  PHE A CG    1 
ATOM   2732 C CD1   . PHE A 1 366 ? 31.66005 -20.36415 -1.01986  1.000 14.73263 ? 366  PHE A CD1   1 
ATOM   2733 C CD2   . PHE A 1 366 ? 33.45155 -18.82954 -0.67994  1.000 13.82223 ? 366  PHE A CD2   1 
ATOM   2734 C CE1   . PHE A 1 366 ? 32.56071 -21.32223 -1.45081  1.000 17.82850 ? 366  PHE A CE1   1 
ATOM   2735 C CE2   . PHE A 1 366 ? 34.35743 -19.78323 -1.10817  1.000 12.99336 ? 366  PHE A CE2   1 
ATOM   2736 C CZ    . PHE A 1 366 ? 33.91178 -21.03032 -1.49386  1.000 15.38484 ? 366  PHE A CZ    1 
ATOM   2737 N N     . ARG A 1 367 ? 28.57386 -16.15324 -0.51319  1.000 12.87237 ? 367  ARG A N     1 
ATOM   2738 C CA    . ARG A 1 367 ? 27.78539 -15.09346 0.10601   1.000 13.51011 ? 367  ARG A CA    1 
ATOM   2739 C C     . ARG A 1 367 ? 26.28722 -15.31449 -0.06562  1.000 15.37665 ? 367  ARG A C     1 
ATOM   2740 O O     . ARG A 1 367 ? 25.51201 -15.01233 0.84606   1.000 16.01323 ? 367  ARG A O     1 
ATOM   2741 C CB    . ARG A 1 367 ? 28.18760 -13.73320 -0.46685  1.000 13.58918 ? 367  ARG A CB    1 
ATOM   2742 C CG    . ARG A 1 367 ? 29.59666 -13.29425 -0.09242  1.000 14.59649 ? 367  ARG A CG    1 
ATOM   2743 C CD    . ARG A 1 367 ? 29.87235 -11.85610 -0.51550  1.000 14.32056 ? 367  ARG A CD    1 
ATOM   2744 N NE    . ARG A 1 367 ? 29.04200 -10.88668 0.18775   1.000 14.52169 ? 367  ARG A NE    1 
ATOM   2745 C CZ    . ARG A 1 367 ? 29.08554 -9.57745  -0.02098  1.000 18.94048 ? 367  ARG A CZ    1 
ATOM   2746 N NH1   . ARG A 1 367 ? 29.89138 -9.04926  -0.92728  1.000 16.87874 ? 367  ARG A NH1   1 
ATOM   2747 N NH2   . ARG A 1 367 ? 28.29818 -8.77840  0.69451   1.000 17.50071 ? 367  ARG A NH2   1 
ATOM   2748 N N     . MET A 1 368 ? 25.85164 -15.83069 -1.21515  1.000 15.42294 ? 368  MET A N     1 
ATOM   2749 C CA    . MET A 1 368 ? 24.41910 -15.95474 -1.44021  1.000 14.66974 ? 368  MET A CA    1 
ATOM   2750 C C     . MET A 1 368 ? 23.83879 -17.22187 -0.82979  1.000 17.07849 ? 368  MET A C     1 
ATOM   2751 O O     . MET A 1 368 ? 22.62580 -17.28840 -0.60332  1.000 17.24389 ? 368  MET A O     1 
ATOM   2752 C CB    . MET A 1 368 ? 24.10779 -15.90704 -2.93390  1.000 15.73381 ? 368  MET A CB    1 
ATOM   2753 C CG    . MET A 1 368 ? 24.32644 -14.52635 -3.50845  1.000 16.80756 ? 368  MET A CG    1 
ATOM   2754 S SD    . MET A 1 368 ? 23.77177 -14.26203 -5.19580  1.000 20.12685 ? 368  MET A SD    1 
ATOM   2755 C CE    . MET A 1 368 ? 22.08517 -13.74907 -4.86976  1.000 27.36144 ? 368  MET A CE    1 
ATOM   2756 N N     . TYR A 1 369 ? 24.67013 -18.22540 -0.57008  1.000 13.11992 ? 369  TYR A N     1 
ATOM   2757 C CA    . TYR A 1 369 ? 24.24552 -19.40758 0.16266   1.000 15.47408 ? 369  TYR A CA    1 
ATOM   2758 C C     . TYR A 1 369 ? 24.57114 -19.33568 1.64346   1.000 14.88422 ? 369  TYR A C     1 
ATOM   2759 O O     . TYR A 1 369 ? 23.78037 -19.81099 2.46421   1.000 15.80813 ? 369  TYR A O     1 
ATOM   2760 C CB    . TYR A 1 369 ? 24.89084 -20.66373 -0.42462  1.000 15.20362 ? 369  TYR A CB    1 
ATOM   2761 C CG    . TYR A 1 369 ? 24.14147 -21.23009 -1.60333  1.000 15.25774 ? 369  TYR A CG    1 
ATOM   2762 C CD1   . TYR A 1 369 ? 23.05561 -22.07585 -1.41718  1.000 18.17464 ? 369  TYR A CD1   1 
ATOM   2763 C CD2   . TYR A 1 369 ? 24.50544 -20.90521 -2.90027  1.000 15.80203 ? 369  TYR A CD2   1 
ATOM   2764 C CE1   . TYR A 1 369 ? 22.36324 -22.59565 -2.49322  1.000 18.89779 ? 369  TYR A CE1   1 
ATOM   2765 C CE2   . TYR A 1 369 ? 23.81965 -21.41583 -3.98043  1.000 14.90598 ? 369  TYR A CE2   1 
ATOM   2766 C CZ    . TYR A 1 369 ? 22.74926 -22.26082 -3.77363  1.000 19.18261 ? 369  TYR A CZ    1 
ATOM   2767 O OH    . TYR A 1 369 ? 22.06476 -22.77039 -4.85465  1.000 19.69654 ? 369  TYR A OH    1 
ATOM   2768 N N     . GLY A 1 370 ? 25.70894 -18.75337 2.00831   1.000 16.18785 ? 370  GLY A N     1 
ATOM   2769 C CA    . GLY A 1 370 ? 26.16431 -18.80720 3.38076   1.000 15.19177 ? 370  GLY A CA    1 
ATOM   2770 C C     . GLY A 1 370 ? 26.78403 -20.15708 3.67922   1.000 14.37006 ? 370  GLY A C     1 
ATOM   2771 O O     . GLY A 1 370 ? 26.49504 -21.13363 2.97490   1.000 16.18860 ? 370  GLY A O     1 
ATOM   2772 N N     . VAL A 1 371 ? 27.60675 -20.24416 4.72901   1.000 13.27267 ? 371  VAL A N     1 
ATOM   2773 C CA    . VAL A 1 371 ? 28.17910 -21.53634 5.09660   1.000 14.28744 ? 371  VAL A CA    1 
ATOM   2774 C C     . VAL A 1 371 ? 27.07385 -22.53075 5.42418   1.000 16.57352 ? 371  VAL A C     1 
ATOM   2775 O O     . VAL A 1 371 ? 27.13678 -23.70586 5.03933   1.000 15.31975 ? 371  VAL A O     1 
ATOM   2776 C CB    . VAL A 1 371 ? 29.16646 -21.37383 6.26603   1.000 16.46683 ? 371  VAL A CB    1 
ATOM   2777 C CG1   . VAL A 1 371 ? 29.69076 -22.72635 6.71197   1.000 16.68328 ? 371  VAL A CG1   1 
ATOM   2778 C CG2   . VAL A 1 371 ? 30.32522 -20.46556 5.86742   1.000 17.34641 ? 371  VAL A CG2   1 
ATOM   2779 N N     . LYS A 1 372 ? 26.03335 -22.06977 6.11858   1.000 16.86747 ? 372  LYS A N     1 
ATOM   2780 C CA    . LYS A 1 372 ? 24.94734 -22.96092 6.50723   1.000 16.46161 ? 372  LYS A CA    1 
ATOM   2781 C C     . LYS A 1 372 ? 24.15490 -23.44670 5.30090   1.000 17.34622 ? 372  LYS A C     1 
ATOM   2782 O O     . LYS A 1 372 ? 23.66464 -24.58207 5.30155   1.000 17.91192 ? 372  LYS A O     1 
ATOM   2783 C CB    . LYS A 1 372 ? 24.02973 -22.25479 7.50508   1.000 17.56369 ? 372  LYS A CB    1 
ATOM   2784 C CG    . LYS A 1 372 ? 24.65455 -22.08652 8.87882   1.000 18.89333 ? 372  LYS A CG    1 
ATOM   2785 C CD    . LYS A 1 372 ? 23.77904 -21.26413 9.80441   1.000 25.44524 ? 372  LYS A CD    1 
ATOM   2786 C CE    . LYS A 1 372 ? 24.53091 -20.90410 11.07667  1.000 33.61616 ? 372  LYS A CE    1 
ATOM   2787 N NZ    . LYS A 1 372 ? 23.76552 -21.28076 12.29606  1.000 40.99893 ? 372  LYS A NZ    1 
ATOM   2788 N N     . GLY A 1 373 ? 24.01586 -22.61113 4.27015   1.000 15.43181 ? 373  GLY A N     1 
ATOM   2789 C CA    . GLY A 1 373 ? 23.34243 -23.05720 3.06222   1.000 17.66350 ? 373  GLY A CA    1 
ATOM   2790 C C     . GLY A 1 373 ? 24.11838 -24.13795 2.33445   1.000 16.65879 ? 373  GLY A C     1 
ATOM   2791 O O     . GLY A 1 373 ? 23.53606 -25.10607 1.83640   1.000 15.25876 ? 373  GLY A O     1 
ATOM   2792 N N     . LEU A 1 374 ? 25.44294 -23.99057 2.26505   1.000 14.81490 ? 374  LEU A N     1 
ATOM   2793 C CA    . LEU A 1 374 ? 26.26945 -25.01529 1.63752   1.000 14.40972 ? 374  LEU A CA    1 
ATOM   2794 C C     . LEU A 1 374 ? 26.27427 -26.29856 2.45977   1.000 14.62040 ? 374  LEU A C     1 
ATOM   2795 O O     . LEU A 1 374 ? 26.26785 -27.40077 1.89912   1.000 13.60270 ? 374  LEU A O     1 
ATOM   2796 C CB    . LEU A 1 374 ? 27.69284 -24.49194 1.44217   1.000 14.38925 ? 374  LEU A CB    1 
ATOM   2797 C CG    . LEU A 1 374 ? 27.84774 -23.29826 0.49703   1.000 13.66898 ? 374  LEU A CG    1 
ATOM   2798 C CD1   . LEU A 1 374 ? 29.30177 -22.85055 0.41545   1.000 15.83486 ? 374  LEU A CD1   1 
ATOM   2799 C CD2   . LEU A 1 374 ? 27.31310 -23.64213 -0.88352  1.000 16.15730 ? 374  LEU A CD2   1 
ATOM   2800 N N     . GLN A 1 375 ? 26.28443 -26.17651 3.79047   1.000 13.22187 ? 375  GLN A N     1 
ATOM   2801 C CA    . GLN A 1 375 ? 26.23444 -27.36276 4.63965   1.000 14.80509 ? 375  GLN A CA    1 
ATOM   2802 C C     . GLN A 1 375 ? 24.92362 -28.11623 4.45553   1.000 15.79190 ? 375  GLN A C     1 
ATOM   2803 O O     . GLN A 1 375 ? 24.90994 -29.35183 4.41861   1.000 15.13895 ? 375  GLN A O     1 
ATOM   2804 C CB    . GLN A 1 375 ? 26.42502 -26.97560 6.10804   1.000 16.45518 ? 375  GLN A CB    1 
ATOM   2805 C CG    . GLN A 1 375 ? 27.84320 -26.56525 6.48009   1.000 15.36390 ? 375  GLN A CG    1 
ATOM   2806 C CD    . GLN A 1 375 ? 27.94041 -26.00415 7.88958   1.000 19.57067 ? 375  GLN A CD    1 
ATOM   2807 O OE1   . GLN A 1 375 ? 27.03484 -25.31463 8.36138   1.000 17.07219 ? 375  GLN A OE1   1 
ATOM   2808 N NE2   . GLN A 1 375 ? 29.04109 -26.30138 8.56996   1.000 17.05171 ? 375  GLN A NE2   1 
ATOM   2809 N N     . ALA A 1 376 ? 23.80966 -27.38847 4.33731   1.000 15.32931 ? 376  ALA A N     1 
ATOM   2810 C CA    . ALA A 1 376 ? 22.52233 -28.04079 4.11953   1.000 14.42356 ? 376  ALA A CA    1 
ATOM   2811 C C     . ALA A 1 376 ? 22.48687 -28.74805 2.77068   1.000 15.17435 ? 376  ALA A C     1 
ATOM   2812 O O     . ALA A 1 376 ? 21.87336 -29.81376 2.63431   1.000 15.16999 ? 376  ALA A O     1 
ATOM   2813 C CB    . ALA A 1 376 ? 21.39109 -27.01779 4.22372   1.000 16.22031 ? 376  ALA A CB    1 
ATOM   2814 N N     . TYR A 1 377 ? 23.14316 -28.16660 1.76428   1.000 14.30189 ? 377  TYR A N     1 
ATOM   2815 C CA    . TYR A 1 377 ? 23.24210 -28.79838 0.45140   1.000 13.92408 ? 377  TYR A CA    1 
ATOM   2816 C C     . TYR A 1 377 ? 23.99024 -30.12510 0.52947   1.000 14.55122 ? 377  TYR A C     1 
ATOM   2817 O O     . TYR A 1 377 ? 23.52510 -31.14494 0.00713   1.000 14.94659 ? 377  TYR A O     1 
ATOM   2818 C CB    . TYR A 1 377 ? 23.92468 -27.83332 -0.51955  1.000 14.89941 ? 377  TYR A CB    1 
ATOM   2819 C CG    . TYR A 1 377 ? 24.46916 -28.45398 -1.78757  1.000 13.06344 ? 377  TYR A CG    1 
ATOM   2820 C CD1   . TYR A 1 377 ? 23.63424 -28.78263 -2.84892  1.000 13.71262 ? 377  TYR A CD1   1 
ATOM   2821 C CD2   . TYR A 1 377 ? 25.83101 -28.68961 -1.92855  1.000 11.26520 ? 377  TYR A CD2   1 
ATOM   2822 C CE1   . TYR A 1 377 ? 24.14347 -29.34078 -4.01158  1.000 14.31658 ? 377  TYR A CE1   1 
ATOM   2823 C CE2   . TYR A 1 377 ? 26.34609 -29.24534 -3.08215  1.000 14.84277 ? 377  TYR A CE2   1 
ATOM   2824 C CZ    . TYR A 1 377 ? 25.50224 -29.56846 -4.11943  1.000 14.54459 ? 377  TYR A CZ    1 
ATOM   2825 O OH    . TYR A 1 377 ? 26.02802 -30.12088 -5.26422  1.000 12.92091 ? 377  TYR A OH    1 
ATOM   2826 N N     . ILE A 1 378 ? 25.15424 -30.12852 1.18294   1.000 12.64619 ? 378  ILE A N     1 
ATOM   2827 C CA    . ILE A 1 378 ? 25.93425 -31.35649 1.33119   1.000 13.86747 ? 378  ILE A CA    1 
ATOM   2828 C C     . ILE A 1 378 ? 25.12825 -32.41296 2.07797   1.000 15.55826 ? 378  ILE A C     1 
ATOM   2829 O O     . ILE A 1 378 ? 25.04744 -33.57505 1.65988   1.000 13.93717 ? 378  ILE A O     1 
ATOM   2830 C CB    . ILE A 1 378 ? 27.26553 -31.05770 2.04611   1.000 14.60192 ? 378  ILE A CB    1 
ATOM   2831 C CG1   . ILE A 1 378 ? 28.15609 -30.15566 1.18556   1.000 14.84335 ? 378  ILE A CG1   1 
ATOM   2832 C CG2   . ILE A 1 378 ? 27.98640 -32.34929 2.40602   1.000 13.83994 ? 378  ILE A CG2   1 
ATOM   2833 C CD1   . ILE A 1 378 ? 28.61004 -30.79577 -0.09950  1.000 15.89416 ? 378  ILE A CD1   1 
ATOM   2834 N N     . ARG A 1 379 ? 24.50867 -32.01577 3.19106   1.000 14.72929 ? 379  ARG A N     1 
ATOM   2835 C CA    . ARG A 1 379 ? 23.82992 -32.96850 4.06403   1.000 14.94861 ? 379  ARG A CA    1 
ATOM   2836 C C     . ARG A 1 379 ? 22.60472 -33.57064 3.38828   1.000 15.53829 ? 379  ARG A C     1 
ATOM   2837 O O     . ARG A 1 379 ? 22.28067 -34.74155 3.62060   1.000 16.69904 ? 379  ARG A O     1 
ATOM   2838 C CB    . ARG A 1 379 ? 23.44998 -32.26787 5.36485   1.000 15.13852 ? 379  ARG A CB    1 
ATOM   2839 C CG    . ARG A 1 379 ? 24.66493 -31.95329 6.22593   1.000 16.31020 ? 379  ARG A CG    1 
ATOM   2840 C CD    . ARG A 1 379 ? 24.32621 -31.05375 7.39755   1.000 17.44405 ? 379  ARG A CD    1 
ATOM   2841 N NE    . ARG A 1 379 ? 25.42350 -30.98497 8.35401   1.000 17.49543 ? 379  ARG A NE    1 
ATOM   2842 C CZ    . ARG A 1 379 ? 25.62006 -29.97409 9.18842   1.000 20.16618 ? 379  ARG A CZ    1 
ATOM   2843 N NH1   . ARG A 1 379 ? 24.81056 -28.92765 9.20649   1.000 19.41318 ? 379  ARG A NH1   1 
ATOM   2844 N NH2   . ARG A 1 379 ? 26.66272 -30.00710 10.01437  1.000 19.87395 ? 379  ARG A NH2   1 
ATOM   2845 N N     . LYS A 1 380 ? 21.91960 -32.79308 2.54472   1.000 13.95546 ? 380  LYS A N     1 
ATOM   2846 C CA    . LYS A 1 380 ? 20.78908 -33.32939 1.79148   1.000 15.46782 ? 380  LYS A CA    1 
ATOM   2847 C C     . LYS A 1 380 ? 21.23993 -34.41012 0.81582   1.000 15.99221 ? 380  LYS A C     1 
ATOM   2848 O O     . LYS A 1 380 ? 20.59739 -35.46135 0.69964   1.000 14.50875 ? 380  LYS A O     1 
ATOM   2849 C CB    . LYS A 1 380 ? 20.07588 -32.20156 1.04735   1.000 16.46838 ? 380  LYS A CB    1 
ATOM   2850 C CG    . LYS A 1 380 ? 18.79567 -32.62377 0.34659   1.000 18.03953 ? 380  LYS A CG    1 
ATOM   2851 C CD    . LYS A 1 380 ? 18.09699 -31.43073 -0.28686  1.000 21.96086 ? 380  LYS A CD    1 
ATOM   2852 C CE    . LYS A 1 380 ? 16.95098 -31.86915 -1.18419  1.000 25.02195 ? 380  LYS A CE    1 
ATOM   2853 N NZ    . LYS A 1 380 ? 16.23770 -30.69933 -1.76458  1.000 31.96089 ? 380  LYS A NZ    1 
ATOM   2854 N N     . HIS A 1 381 ? 22.34723 -34.17153 0.10758   1.000 12.85960 ? 381  HIS A N     1 
ATOM   2855 C CA    . HIS A 1 381 ? 22.84556 -35.16516 -0.83880  1.000 15.16105 ? 381  HIS A CA    1 
ATOM   2856 C C     . HIS A 1 381 ? 23.27366 -36.44426 -0.13156  1.000 15.45696 ? 381  HIS A C     1 
ATOM   2857 O O     . HIS A 1 381 ? 22.97988 -37.54850 -0.60336  1.000 13.91924 ? 381  HIS A O     1 
ATOM   2858 C CB    . HIS A 1 381 ? 24.00481 -34.58894 -1.65260  1.000 13.00162 ? 381  HIS A CB    1 
ATOM   2859 C CG    . HIS A 1 381 ? 23.57434 -33.86936 -2.89292  1.000 14.77855 ? 381  HIS A CG    1 
ATOM   2860 N ND1   . HIS A 1 381 ? 24.46468 -33.46162 -3.86264  1.000 16.26511 ? 381  HIS A ND1   1 
ATOM   2861 C CD2   . HIS A 1 381 ? 22.34759 -33.49662 -3.32826  1.000 14.64596 ? 381  HIS A CD2   1 
ATOM   2862 C CE1   . HIS A 1 381 ? 23.80662 -32.86331 -4.83900  1.000 15.60441 ? 381  HIS A CE1   1 
ATOM   2863 N NE2   . HIS A 1 381 ? 22.52012 -32.87284 -4.54026  1.000 13.31371 ? 381  HIS A NE2   1 
ATOM   2864 N N     . VAL A 1 382 ? 23.97125 -36.31951 0.99917   1.000 13.55658 ? 382  VAL A N     1 
ATOM   2865 C CA    . VAL A 1 382 ? 24.40210 -37.50861 1.72852   1.000 16.37577 ? 382  VAL A CA    1 
ATOM   2866 C C     . VAL A 1 382 ? 23.19442 -38.26346 2.27405   1.000 16.34946 ? 382  VAL A C     1 
ATOM   2867 O O     . VAL A 1 382 ? 23.16410 -39.50058 2.27281   1.000 15.25267 ? 382  VAL A O     1 
ATOM   2868 C CB    . VAL A 1 382 ? 25.39265 -37.12160 2.84300   1.000 15.87280 ? 382  VAL A CB    1 
ATOM   2869 C CG1   . VAL A 1 382 ? 25.74230 -38.33219 3.69704   1.000 17.84801 ? 382  VAL A CG1   1 
ATOM   2870 C CG2   . VAL A 1 382 ? 26.65040 -36.50157 2.24296   1.000 15.29352 ? 382  VAL A CG2   1 
ATOM   2871 N N     . GLN A 1 383 ? 22.17698 -37.53221 2.73840   1.000 13.59595 ? 383  GLN A N     1 
ATOM   2872 C CA    . GLN A 1 383 ? 20.93516 -38.16794 3.16748   1.000 17.06125 ? 383  GLN A CA    1 
ATOM   2873 C C     . GLN A 1 383 ? 20.29256 -38.94794 2.02844   1.000 16.48784 ? 383  GLN A C     1 
ATOM   2874 O O     . GLN A 1 383 ? 19.81023 -40.06996 2.22802   1.000 16.24680 ? 383  GLN A O     1 
ATOM   2875 C CB    . GLN A 1 383 ? 19.96796 -37.11570 3.70520   1.000 16.55119 ? 383  GLN A CB    1 
ATOM   2876 C CG    . GLN A 1 383 ? 18.56175 -37.62775 3.98100   1.000 20.72387 ? 383  GLN A CG    1 
ATOM   2877 C CD    . GLN A 1 383 ? 18.52216 -38.74964 5.00383   1.000 25.50464 ? 383  GLN A CD    1 
ATOM   2878 O OE1   . GLN A 1 383 ? 19.39588 -38.85000 5.86740   1.000 29.56095 ? 383  GLN A OE1   1 
ATOM   2879 N NE2   . GLN A 1 383 ? 17.50492 -39.59868 4.91262   1.000 27.82963 ? 383  GLN A NE2   1 
ATOM   2880 N N     . LEU A 1 384 ? 20.27792 -38.37083 0.82529   1.000 14.36964 ? 384  LEU A N     1 
ATOM   2881 C CA    . LEU A 1 384 ? 19.68576 -39.05862 -0.31507  1.000 15.35538 ? 384  LEU A CA    1 
ATOM   2882 C C     . LEU A 1 384 ? 20.49617 -40.29142 -0.69337  1.000 16.21539 ? 384  LEU A C     1 
ATOM   2883 O O     . LEU A 1 384 ? 19.93240 -41.30646 -1.11818  1.000 14.02792 ? 384  LEU A O     1 
ATOM   2884 C CB    . LEU A 1 384 ? 19.57677 -38.09593 -1.49788  1.000 15.45220 ? 384  LEU A CB    1 
ATOM   2885 C CG    . LEU A 1 384 ? 18.50315 -37.01602 -1.34562  1.000 14.62212 ? 384  LEU A CG    1 
ATOM   2886 C CD1   . LEU A 1 384 ? 18.61408 -35.97659 -2.44985  1.000 15.89431 ? 384  LEU A CD1   1 
ATOM   2887 C CD2   . LEU A 1 384 ? 17.11597 -37.63923 -1.32282  1.000 18.88263 ? 384  LEU A CD2   1 
ATOM   2888 N N     . SER A 1 385 ? 21.82036 -40.21816 -0.55185  1.000 14.13315 ? 385  SER A N     1 
ATOM   2889 C CA    . SER A 1 385 ? 22.66217 -41.37855 -0.82132  1.000 14.95547 ? 385  SER A CA    1 
ATOM   2890 C C     . SER A 1 385 ? 22.32851 -42.52302 0.12522   1.000 16.57311 ? 385  SER A C     1 
ATOM   2891 O O     . SER A 1 385 ? 22.20258 -43.67956 -0.29492  1.000 16.62887 ? 385  SER A O     1 
ATOM   2892 C CB    . SER A 1 385 ? 24.13709 -40.99335 -0.69911  1.000 14.49856 ? 385  SER A CB    1 
ATOM   2893 O OG    . SER A 1 385 ? 24.97662 -42.07796 -1.04697  1.000 17.81552 ? 385  SER A OG    1 
ATOM   2894 N N     . HIS A 1 386 ? 22.17805 -42.21481 1.41453   1.000 15.48869 ? 386  HIS A N     1 
ATOM   2895 C CA    . HIS A 1 386 ? 21.80464 -43.24030 2.37829   1.000 15.75921 ? 386  HIS A CA    1 
ATOM   2896 C C     . HIS A 1 386 ? 20.39339 -43.75194 2.12443   1.000 15.99647 ? 386  HIS A C     1 
ATOM   2897 O O     . HIS A 1 386 ? 20.08092 -44.90002 2.46086   1.000 15.70456 ? 386  HIS A O     1 
ATOM   2898 C CB    . HIS A 1 386 ? 21.93589 -42.68924 3.79681   1.000 16.52543 ? 386  HIS A CB    1 
ATOM   2899 C CG    . HIS A 1 386 ? 23.35225 -42.58407 4.27033   1.000 19.80141 ? 386  HIS A CG    1 
ATOM   2900 N ND1   . HIS A 1 386 ? 24.23250 -43.64375 4.22492   1.000 21.53865 ? 386  HIS A ND1   1 
ATOM   2901 C CD2   . HIS A 1 386 ? 24.04536 -41.54159 4.78661   1.000 21.37451 ? 386  HIS A CD2   1 
ATOM   2902 C CE1   . HIS A 1 386 ? 25.40533 -43.25999 4.69728   1.000 22.83351 ? 386  HIS A CE1   1 
ATOM   2903 N NE2   . HIS A 1 386 ? 25.31834 -41.98885 5.04508   1.000 22.38785 ? 386  HIS A NE2   1 
ATOM   2904 N N     . GLU A 1 387 ? 19.53387 -42.92291 1.52756   1.000 15.19646 ? 387  GLU A N     1 
ATOM   2905 C CA    . GLU A 1 387 ? 18.19514 -43.38001 1.17256   1.000 15.35812 ? 387  GLU A CA    1 
ATOM   2906 C C     . GLU A 1 387 ? 18.24370 -44.42023 0.06012   1.000 17.17996 ? 387  GLU A C     1 
ATOM   2907 O O     . GLU A 1 387 ? 17.50220 -45.40889 0.09731   1.000 17.96578 ? 387  GLU A O     1 
ATOM   2908 C CB    . GLU A 1 387 ? 17.32463 -42.18958 0.77068   1.000 17.67205 ? 387  GLU A CB    1 
ATOM   2909 C CG    . GLU A 1 387 ? 16.81887 -41.38953 1.96058   1.000 18.72333 ? 387  GLU A CG    1 
ATOM   2910 C CD    . GLU A 1 387 ? 15.97435 -40.19905 1.55647   1.000 22.76443 ? 387  GLU A CD    1 
ATOM   2911 O OE1   . GLU A 1 387 ? 15.21942 -40.30827 0.56765   1.000 20.49362 ? 387  GLU A OE1   1 
ATOM   2912 O OE2   . GLU A 1 387 ? 16.06034 -39.15550 2.23741   1.000 22.37571 ? 387  GLU A OE2   1 
ATOM   2913 N N     . PHE A 1 388 ? 19.10799 -44.21897 -0.93774  1.000 15.22979 ? 388  PHE A N     1 
ATOM   2914 C CA    . PHE A 1 388 ? 19.28560 -45.23630 -1.96967  1.000 17.94723 ? 388  PHE A CA    1 
ATOM   2915 C C     . PHE A 1 388 ? 19.91450 -46.49597 -1.38589  1.000 17.61148 ? 388  PHE A C     1 
ATOM   2916 O O     . PHE A 1 388 ? 19.48470 -47.61566 -1.68917  1.000 17.91662 ? 388  PHE A O     1 
ATOM   2917 C CB    . PHE A 1 388 ? 20.14012 -44.68876 -3.11286  1.000 15.52762 ? 388  PHE A CB    1 
ATOM   2918 C CG    . PHE A 1 388 ? 20.36051 -45.67359 -4.22815  1.000 16.84749 ? 388  PHE A CG    1 
ATOM   2919 C CD1   . PHE A 1 388 ? 19.40076 -45.85800 -5.21101  1.000 15.45249 ? 388  PHE A CD1   1 
ATOM   2920 C CD2   . PHE A 1 388 ? 21.52296 -46.42816 -4.28289  1.000 16.39102 ? 388  PHE A CD2   1 
ATOM   2921 C CE1   . PHE A 1 388 ? 19.60292 -46.76889 -6.23699  1.000 20.42775 ? 388  PHE A CE1   1 
ATOM   2922 C CE2   . PHE A 1 388 ? 21.73043 -47.34191 -5.30149  1.000 17.73021 ? 388  PHE A CE2   1 
ATOM   2923 C CZ    . PHE A 1 388 ? 20.76975 -47.51176 -6.28142  1.000 17.93972 ? 388  PHE A CZ    1 
ATOM   2924 N N     . GLU A 1 389 ? 20.94468 -46.32665 -0.55109  1.000 17.03377 ? 389  GLU A N     1 
ATOM   2925 C CA    . GLU A 1 389 ? 21.56636 -47.46247 0.12238   1.000 16.79979 ? 389  GLU A CA    1 
ATOM   2926 C C     . GLU A 1 389 ? 20.53723 -48.28392 0.88514   1.000 19.81877 ? 389  GLU A C     1 
ATOM   2927 O O     . GLU A 1 389 ? 20.55718 -49.52030 0.84117   1.000 19.32802 ? 389  GLU A O     1 
ATOM   2928 C CB    . GLU A 1 389 ? 22.65239 -46.97514 1.07882   1.000 18.27347 ? 389  GLU A CB    1 
ATOM   2929 C CG    . GLU A 1 389 ? 23.26228 -48.08247 1.91786   1.000 20.99949 ? 389  GLU A CG    1 
ATOM   2930 C CD    . GLU A 1 389 ? 24.06681 -47.55080 3.08497   1.000 22.46987 ? 389  GLU A CD    1 
ATOM   2931 O OE1   . GLU A 1 389 ? 24.03664 -46.32299 3.31595   1.000 23.71884 ? 389  GLU A OE1   1 
ATOM   2932 O OE2   . GLU A 1 389 ? 24.72216 -48.35970 3.77379   1.000 24.62250 ? 389  GLU A OE2   1 
ATOM   2933 N N     . SER A 1 390 ? 19.62748 -47.60844 1.59272   1.000 17.90523 ? 390  SER A N     1 
ATOM   2934 C CA    . SER A 1 390 ? 18.60736 -48.31247 2.36297   1.000 19.87971 ? 390  SER A CA    1 
ATOM   2935 C C     . SER A 1 390 ? 17.74710 -49.19350 1.46664   1.000 21.11537 ? 390  SER A C     1 
ATOM   2936 O O     . SER A 1 390 ? 17.41781 -50.32854 1.82986   1.000 21.66548 ? 390  SER A O     1 
ATOM   2937 C CB    . SER A 1 390 ? 17.74130 -47.30668 3.11922   1.000 20.15472 ? 390  SER A CB    1 
ATOM   2938 O OG    . SER A 1 390 ? 16.67610 -47.95641 3.79135   1.000 25.93815 ? 390  SER A OG    1 
ATOM   2939 N N     . LEU A 1 391 ? 17.38353 -48.69246 0.28517   1.000 19.98079 ? 391  LEU A N     1 
ATOM   2940 C CA    . LEU A 1 391 ? 16.55879 -49.47650 -0.62746  1.000 20.16459 ? 391  LEU A CA    1 
ATOM   2941 C C     . LEU A 1 391 ? 17.31150 -50.69614 -1.14518  1.000 22.86623 ? 391  LEU A C     1 
ATOM   2942 O O     . LEU A 1 391 ? 16.74554 -51.79336 -1.22425  1.000 19.30931 ? 391  LEU A O     1 
ATOM   2943 C CB    . LEU A 1 391 ? 16.08857 -48.60048 -1.78778  1.000 19.42712 ? 391  LEU A CB    1 
ATOM   2944 C CG    . LEU A 1 391 ? 15.16491 -47.44098 -1.40746  1.000 17.92786 ? 391  LEU A CG    1 
ATOM   2945 C CD1   . LEU A 1 391 ? 15.00435 -46.48141 -2.57424  1.000 20.24144 ? 391  LEU A CD1   1 
ATOM   2946 C CD2   . LEU A 1 391 ? 13.81020 -47.95605 -0.93774  1.000 22.90656 ? 391  LEU A CD2   1 
ATOM   2947 N N     . VAL A 1 392 ? 18.58820 -50.52614 -1.49891  1.000 19.38752 ? 392  VAL A N     1 
ATOM   2948 C CA    . VAL A 1 392 ? 19.38046 -51.65082 -1.99138  1.000 19.73958 ? 392  VAL A CA    1 
ATOM   2949 C C     . VAL A 1 392 ? 19.53309 -52.70730 -0.90592  1.000 20.73283 ? 392  VAL A C     1 
ATOM   2950 O O     . VAL A 1 392 ? 19.44758 -53.91298 -1.17204  1.000 20.45420 ? 392  VAL A O     1 
ATOM   2951 C CB    . VAL A 1 392 ? 20.75158 -51.16270 -2.49673  1.000 21.81246 ? 392  VAL A CB    1 
ATOM   2952 C CG1   . VAL A 1 392 ? 21.65287 -52.34761 -2.81441  1.000 20.30364 ? 392  VAL A CG1   1 
ATOM   2953 C CG2   . VAL A 1 392 ? 20.58561 -50.27228 -3.71469  1.000 18.68347 ? 392  VAL A CG2   1 
ATOM   2954 N N     . ARG A 1 393 ? 19.74701 -52.27216 0.33731   1.000 19.61874 ? 393  ARG A N     1 
ATOM   2955 C CA    . ARG A 1 393 ? 19.93517 -53.19525 1.44853   1.000 22.26801 ? 393  ARG A CA    1 
ATOM   2956 C C     . ARG A 1 393 ? 18.65903 -53.93996 1.81897   1.000 24.87153 ? 393  ARG A C     1 
ATOM   2957 O O     . ARG A 1 393 ? 18.70840 -54.82392 2.68020   1.000 25.14940 ? 393  ARG A O     1 
ATOM   2958 C CB    . ARG A 1 393 ? 20.47064 -52.43759 2.66535   1.000 22.01596 ? 393  ARG A CB    1 
ATOM   2959 C CG    . ARG A 1 393 ? 21.91951 -51.99993 2.52189   1.000 24.42293 ? 393  ARG A CG    1 
ATOM   2960 C CD    . ARG A 1 393 ? 22.46142 -51.38809 3.80213   1.000 27.40761 ? 393  ARG A CD    1 
ATOM   2961 N NE    . ARG A 1 393 ? 23.89289 -51.12460 3.70968   1.000 27.37197 ? 393  ARG A NE    1 
ATOM   2962 C CZ    . ARG A 1 393 ? 24.83782 -52.04258 3.86039   1.000 29.59673 ? 393  ARG A CZ    1 
ATOM   2963 N NH1   . ARG A 1 393 ? 24.53990 -53.30513 4.11989   1.000 33.58148 ? 393  ARG A NH1   1 
ATOM   2964 N NH2   . ARG A 1 393 ? 26.11387 -51.68443 3.74757   1.000 31.30055 ? 393  ARG A NH2   1 
ATOM   2965 N N     . GLN A 1 394 ? 17.52681 -53.60683 1.20289   1.000 21.58945 ? 394  GLN A N     1 
ATOM   2966 C CA    . GLN A 1 394 ? 16.28056 -54.32520 1.42577   1.000 24.72602 ? 394  GLN A CA    1 
ATOM   2967 C C     . GLN A 1 394 ? 16.05221 -55.43762 0.41262   1.000 25.55787 ? 394  GLN A C     1 
ATOM   2968 O O     . GLN A 1 394 ? 15.05580 -56.16125 0.52031   1.000 27.11661 ? 394  GLN A O     1 
ATOM   2969 C CB    . GLN A 1 394 ? 15.09352 -53.35643 1.39592   1.000 23.95875 ? 394  GLN A CB    1 
ATOM   2970 C CG    . GLN A 1 394 ? 15.08904 -52.34537 2.52832   1.000 21.55781 ? 394  GLN A CG    1 
ATOM   2971 C CD    . GLN A 1 394 ? 14.05228 -51.25597 2.33322   1.000 23.54123 ? 394  GLN A CD    1 
ATOM   2972 O OE1   . GLN A 1 394 ? 13.01031 -51.47781 1.71603   1.000 24.22616 ? 394  GLN A OE1   1 
ATOM   2973 N NE2   . GLN A 1 394 ? 14.33670 -50.06813 2.85441   1.000 21.29310 ? 394  GLN A NE2   1 
ATOM   2974 N N     . ASP A 1 395 ? 16.95101 -55.59579 -0.55439  1.000 22.51047 ? 395  ASP A N     1 
ATOM   2975 C CA    . ASP A 1 395 ? 16.80150 -56.57330 -1.63166  1.000 24.01191 ? 395  ASP A CA    1 
ATOM   2976 C C     . ASP A 1 395 ? 17.99525 -57.51810 -1.59618  1.000 24.27845 ? 395  ASP A C     1 
ATOM   2977 O O     . ASP A 1 395 ? 19.10268 -57.14015 -2.01938  1.000 24.21645 ? 395  ASP A O     1 
ATOM   2978 C CB    . ASP A 1 395 ? 16.70504 -55.86124 -2.98058  1.000 24.33244 ? 395  ASP A CB    1 
ATOM   2979 C CG    . ASP A 1 395 ? 16.25412 -56.77534 -4.10481  1.000 27.13903 ? 395  ASP A CG    1 
ATOM   2980 O OD1   . ASP A 1 395 ? 16.46280 -58.00308 -4.01734  1.000 27.11641 ? 395  ASP A OD1   1 
ATOM   2981 O OD2   . ASP A 1 395 ? 15.69292 -56.25401 -5.09145  1.000 29.78569 ? 395  ASP A OD2   1 
ATOM   2982 N N     . PRO A 1 396 ? 17.82670 -58.75235 -1.10909  1.000 25.23288 ? 396  PRO A N     1 
ATOM   2983 C CA    . PRO A 1 396 ? 18.96710 -59.67285 -0.99267  1.000 24.64213 ? 396  PRO A CA    1 
ATOM   2984 C C     . PRO A 1 396 ? 19.49466 -60.19317 -2.31965  1.000 24.59447 ? 396  PRO A C     1 
ATOM   2985 O O     . PRO A 1 396 ? 20.44180 -60.98752 -2.31416  1.000 26.71097 ? 396  PRO A O     1 
ATOM   2986 C CB    . PRO A 1 396 ? 18.39370 -60.81221 -0.14125  1.000 27.90210 ? 396  PRO A CB    1 
ATOM   2987 C CG    . PRO A 1 396 ? 16.95224 -60.83822 -0.53049  1.000 26.14493 ? 396  PRO A CG    1 
ATOM   2988 C CD    . PRO A 1 396 ? 16.57712 -59.37674 -0.64486  1.000 26.74508 ? 396  PRO A CD    1 
ATOM   2989 N N     . ARG A 1 397 ? 18.91245 -59.79325 -3.45138  1.000 22.75845 ? 397  ARG A N     1 
ATOM   2990 C CA    . ARG A 1 397 ? 19.53211 -60.08224 -4.73733  1.000 25.40114 ? 397  ARG A CA    1 
ATOM   2991 C C     . ARG A 1 397 ? 20.74272 -59.19558 -4.98873  1.000 22.99778 ? 397  ARG A C     1 
ATOM   2992 O O     . ARG A 1 397 ? 21.55244 -59.50347 -5.87034  1.000 24.51581 ? 397  ARG A O     1 
ATOM   2993 C CB    . ARG A 1 397 ? 18.52038 -59.89668 -5.86850  1.000 22.22313 ? 397  ARG A CB    1 
ATOM   2994 C CG    . ARG A 1 397 ? 17.38097 -60.89836 -5.86366  1.000 27.23781 ? 397  ARG A CG    1 
ATOM   2995 C CD    . ARG A 1 397 ? 16.31610 -60.51456 -6.87829  1.000 26.89064 ? 397  ARG A CD    1 
ATOM   2996 N NE    . ARG A 1 397 ? 15.71299 -59.22424 -6.56824  1.000 32.49779 ? 397  ARG A NE    1 
ATOM   2997 C CZ    . ARG A 1 397 ? 14.85153 -58.59102 -7.35261  1.000 33.36896 ? 397  ARG A CZ    1 
ATOM   2998 N NH1   . ARG A 1 397 ? 14.44952 -59.11191 -8.50048  1.000 35.05923 ? 397  ARG A NH1   1 
ATOM   2999 N NH2   . ARG A 1 397 ? 14.38171 -57.40482 -6.97608  1.000 33.61118 ? 397  ARG A NH2   1 
ATOM   3000 N N     . PHE A 1 398 ? 20.87931 -58.10920 -4.23320  1.000 25.07121 ? 398  PHE A N     1 
ATOM   3001 C CA    . PHE A 1 398 ? 21.92874 -57.11874 -4.40679  1.000 21.70641 ? 398  PHE A CA    1 
ATOM   3002 C C     . PHE A 1 398 ? 22.89562 -57.16812 -3.22996  1.000 22.93595 ? 398  PHE A C     1 
ATOM   3003 O O     . PHE A 1 398 ? 22.60587 -57.75564 -2.18340  1.000 23.67345 ? 398  PHE A O     1 
ATOM   3004 C CB    . PHE A 1 398 ? 21.33067 -55.71130 -4.51676  1.000 18.41524 ? 398  PHE A CB    1 
ATOM   3005 C CG    . PHE A 1 398 ? 20.58592 -55.45944 -5.79671  1.000 21.80406 ? 398  PHE A CG    1 
ATOM   3006 C CD1   . PHE A 1 398 ? 19.24061 -55.77974 -5.90102  1.000 21.81583 ? 398  PHE A CD1   1 
ATOM   3007 C CD2   . PHE A 1 398 ? 21.22119 -54.88724 -6.88727  1.000 21.71932 ? 398  PHE A CD2   1 
ATOM   3008 C CE1   . PHE A 1 398 ? 18.54489 -55.54447 -7.07347  1.000 23.99152 ? 398  PHE A CE1   1 
ATOM   3009 C CE2   . PHE A 1 398 ? 20.53141 -54.64805 -8.06472  1.000 23.09249 ? 398  PHE A CE2   1 
ATOM   3010 C CZ    . PHE A 1 398 ? 19.19182 -54.97677 -8.15769  1.000 24.05714 ? 398  PHE A CZ    1 
ATOM   3011 N N     . GLU A 1 399 ? 24.05360 -56.53349 -3.41088  1.000 20.54956 ? 399  GLU A N     1 
ATOM   3012 C CA    . GLU A 1 399 ? 25.00544 -56.33188 -2.32790  1.000 24.09349 ? 399  GLU A CA    1 
ATOM   3013 C C     . GLU A 1 399 ? 25.57880 -54.92551 -2.41940  1.000 20.58266 ? 399  GLU A C     1 
ATOM   3014 O O     . GLU A 1 399 ? 25.71560 -54.36550 -3.51005  1.000 23.81417 ? 399  GLU A O     1 
ATOM   3015 C CB    . GLU A 1 399 ? 26.16532 -57.33955 -2.35811  1.000 23.64260 ? 399  GLU A CB    1 
ATOM   3016 C CG    . GLU A 1 399 ? 26.92185 -57.38981 -3.67682  1.000 24.63395 ? 399  GLU A CG    1 
ATOM   3017 C CD    . GLU A 1 399 ? 27.80778 -58.61537 -3.79708  1.000 31.64744 ? 399  GLU A CD    1 
ATOM   3018 O OE1   . GLU A 1 399 ? 28.11641 -59.23055 -2.75558  1.000 34.85104 ? 399  GLU A OE1   1 
ATOM   3019 O OE2   . GLU A 1 399 ? 28.20306 -58.96028 -4.93020  1.000 33.46049 ? 399  GLU A OE2   1 
ATOM   3020 N N     . ILE A 1 400 ? 25.90548 -54.35999 -1.25970  1.000 22.08105 ? 400  ILE A N     1 
ATOM   3021 C CA    . ILE A 1 400 ? 26.67820 -53.12528 -1.17865  1.000 21.57353 ? 400  ILE A CA    1 
ATOM   3022 C C     . ILE A 1 400 ? 28.15062 -53.50093 -1.10032  1.000 22.15595 ? 400  ILE A C     1 
ATOM   3023 O O     . ILE A 1 400 ? 28.55179 -54.29507 -0.24173  1.000 23.14794 ? 400  ILE A O     1 
ATOM   3024 C CB    . ILE A 1 400 ? 26.25478 -52.28153 0.03640   1.000 23.11988 ? 400  ILE A CB    1 
ATOM   3025 C CG1   . ILE A 1 400 ? 24.78866 -51.85900 -0.07796  1.000 25.07025 ? 400  ILE A CG1   1 
ATOM   3026 C CG2   . ILE A 1 400 ? 27.14874 -51.05813 0.17237   1.000 20.39484 ? 400  ILE A CG2   1 
ATOM   3027 C CD1   . ILE A 1 400 ? 24.52059 -50.89068 -1.21255  1.000 22.08334 ? 400  ILE A CD1   1 
ATOM   3028 N N     . CYS A 1 401 ? 28.95724 -52.94373 -2.00243  1.000 21.24887 ? 401  CYS A N     1 
ATOM   3029 C CA    . CYS A 1 401 ? 30.34403 -53.37374 -2.12605  1.000 22.48466 ? 401  CYS A CA    1 
ATOM   3030 C C     . CYS A 1 401 ? 31.29268 -52.58188 -1.23660  1.000 25.37801 ? 401  CYS A C     1 
ATOM   3031 O O     . CYS A 1 401 ? 32.31517 -53.12267 -0.79886  1.000 26.15324 ? 401  CYS A O     1 
ATOM   3032 C CB    . CYS A 1 401 ? 30.79548 -53.26903 -3.58707  1.000 26.33020 ? 401  CYS A CB    1 
ATOM   3033 S SG    . CYS A 1 401 ? 29.95445 -54.41761 -4.71265  1.000 30.96648 ? 401  CYS A SG    1 
ATOM   3034 N N     . VAL A 1 402 ? 30.98410 -51.31416 -0.96421  1.000 21.19531 ? 402  VAL A N     1 
ATOM   3035 C CA    . VAL A 1 402 ? 31.84133 -50.44058 -0.17139  1.000 21.88473 ? 402  VAL A CA    1 
ATOM   3036 C C     . VAL A 1 402 ? 30.95859 -49.63009 0.76753   1.000 23.30354 ? 402  VAL A C     1 
ATOM   3037 O O     . VAL A 1 402 ? 29.81239 -49.30864 0.44222   1.000 19.93406 ? 402  VAL A O     1 
ATOM   3038 C CB    . VAL A 1 402 ? 32.69941 -49.51306 -1.07001  1.000 25.52693 ? 402  VAL A CB    1 
ATOM   3039 C CG1   . VAL A 1 402 ? 33.61630 -48.62680 -0.23490  1.000 26.20692 ? 402  VAL A CG1   1 
ATOM   3040 C CG2   . VAL A 1 402 ? 33.51874 -50.33178 -2.05741  1.000 26.44690 ? 402  VAL A CG2   1 
ATOM   3041 N N     . GLU A 1 403 ? 31.49387 -49.31678 1.94847   1.000 22.30835 ? 403  GLU A N     1 
ATOM   3042 C CA    . GLU A 1 403 ? 30.76979 -48.50010 2.91498   1.000 19.98786 ? 403  GLU A CA    1 
ATOM   3043 C C     . GLU A 1 403 ? 30.30974 -47.19169 2.28679   1.000 20.18567 ? 403  GLU A C     1 
ATOM   3044 O O     . GLU A 1 403 ? 31.08230 -46.49847 1.62169   1.000 19.41386 ? 403  GLU A O     1 
ATOM   3045 C CB    . GLU A 1 403 ? 31.64912 -48.20969 4.13334   1.000 23.76735 ? 403  GLU A CB    1 
ATOM   3046 C CG    . GLU A 1 403 ? 30.89601 -47.55336 5.28601   1.000 26.42797 ? 403  GLU A CG    1 
ATOM   3047 C CD    . GLU A 1 403 ? 31.79690 -47.19246 6.45238   1.000 35.68689 ? 403  GLU A CD    1 
ATOM   3048 O OE1   . GLU A 1 403 ? 32.92920 -47.71392 6.51408   1.000 41.38617 ? 403  GLU A OE1   1 
ATOM   3049 O OE2   . GLU A 1 403 ? 31.37443 -46.37906 7.30321   1.000 39.97208 ? 403  GLU A OE2   1 
ATOM   3050 N N     . VAL A 1 404 ? 29.04126 -46.86353 2.49950   1.000 18.49272 ? 404  VAL A N     1 
ATOM   3051 C CA    . VAL A 1 404 ? 28.46304 -45.61450 2.01800   1.000 18.14825 ? 404  VAL A CA    1 
ATOM   3052 C C     . VAL A 1 404 ? 28.75663 -44.52719 3.04281   1.000 19.72864 ? 404  VAL A C     1 
ATOM   3053 O O     . VAL A 1 404 ? 28.35476 -44.63522 4.20670   1.000 20.17863 ? 404  VAL A O     1 
ATOM   3054 C CB    . VAL A 1 404 ? 26.95213 -45.75642 1.77854   1.000 18.77872 ? 404  VAL A CB    1 
ATOM   3055 C CG1   . VAL A 1 404 ? 26.35735 -44.42996 1.34193   1.000 16.84068 ? 404  VAL A CG1   1 
ATOM   3056 C CG2   . VAL A 1 404 ? 26.67720 -46.84304 0.74267   1.000 15.91134 ? 404  VAL A CG2   1 
ATOM   3057 N N     . ILE A 1 405 ? 29.45377 -43.47686 2.61039   1.000 17.33229 ? 405  ILE A N     1 
ATOM   3058 C CA    . ILE A 1 405 ? 29.85880 -42.39437 3.50168   1.000 20.15940 ? 405  ILE A CA    1 
ATOM   3059 C C     . ILE A 1 405 ? 29.32973 -41.06758 2.97285   1.000 16.88707 ? 405  ILE A C     1 
ATOM   3060 O O     . ILE A 1 405 ? 28.75633 -40.26997 3.72348   1.000 17.94778 ? 405  ILE A O     1 
ATOM   3061 C CB    . ILE A 1 405 ? 31.38997 -42.35449 3.66040   1.000 19.54336 ? 405  ILE A CB    1 
ATOM   3062 C CG1   . ILE A 1 405 ? 31.89136 -43.67185 4.25369   1.000 25.63610 ? 405  ILE A CG1   1 
ATOM   3063 C CG2   . ILE A 1 405 ? 31.80780 -41.18040 4.53452   1.000 20.97138 ? 405  ILE A CG2   1 
ATOM   3064 C CD1   . ILE A 1 405 ? 33.39389 -43.76355 4.35545   1.000 29.31280 ? 405  ILE A CD1   1 
ATOM   3065 N N     . LEU A 1 406 ? 29.51705 -40.82299 1.67736   1.000 14.10135 ? 406  LEU A N     1 
ATOM   3066 C CA    . LEU A 1 406 ? 29.07384 -39.57404 1.07305   1.000 15.47634 ? 406  LEU A CA    1 
ATOM   3067 C C     . LEU A 1 406 ? 28.01683 -39.85812 0.01194   1.000 14.27256 ? 406  LEU A C     1 
ATOM   3068 O O     . LEU A 1 406 ? 27.20551 -40.77395 0.17884   1.000 14.89678 ? 406  LEU A O     1 
ATOM   3069 C CB    . LEU A 1 406 ? 30.26916 -38.81609 0.49508   1.000 14.30344 ? 406  LEU A CB    1 
ATOM   3070 C CG    . LEU A 1 406 ? 31.29741 -38.43089 1.56644   1.000 13.32194 ? 406  LEU A CG    1 
ATOM   3071 C CD1   . LEU A 1 406 ? 32.47215 -37.68836 0.96043   1.000 14.89027 ? 406  LEU A CD1   1 
ATOM   3072 C CD2   . LEU A 1 406 ? 30.65696 -37.60960 2.68083   1.000 14.44428 ? 406  LEU A CD2   1 
ATOM   3073 N N     . GLY A 1 407 ? 28.01581 -39.09826 -1.08041  1.000 13.80538 ? 407  GLY A N     1 
ATOM   3074 C CA    . GLY A 1 407 ? 26.94099 -39.19450 -2.05159  1.000 14.34498 ? 407  GLY A CA    1 
ATOM   3075 C C     . GLY A 1 407 ? 27.11200 -40.25863 -3.11695  1.000 15.51318 ? 407  GLY A C     1 
ATOM   3076 O O     . GLY A 1 407 ? 26.63492 -40.09445 -4.24382  1.000 18.95936 ? 407  GLY A O     1 
ATOM   3077 N N     . LEU A 1 408 ? 27.77377 -41.36018 -2.77756  1.000 14.99426 ? 408  LEU A N     1 
ATOM   3078 C CA    . LEU A 1 408 ? 28.01262 -42.44245 -3.72037  1.000 15.51227 ? 408  LEU A CA    1 
ATOM   3079 C C     . LEU A 1 408 ? 27.63616 -43.77196 -3.08487  1.000 14.50960 ? 408  LEU A C     1 
ATOM   3080 O O     . LEU A 1 408 ? 27.92496 -44.01110 -1.90884  1.000 14.49558 ? 408  LEU A O     1 
ATOM   3081 C CB    . LEU A 1 408 ? 29.47700 -42.48004 -4.16455  1.000 15.81796 ? 408  LEU A CB    1 
ATOM   3082 C CG    . LEU A 1 408 ? 29.80811 -43.49500 -5.25923  1.000 16.21826 ? 408  LEU A CG    1 
ATOM   3083 C CD1   . LEU A 1 408 ? 29.11904 -43.13302 -6.57098  1.000 15.85549 ? 408  LEU A CD1   1 
ATOM   3084 C CD2   . LEU A 1 408 ? 31.31409 -43.62009 -5.44158  1.000 14.71167 ? 408  LEU A CD2   1 
ATOM   3085 N N     . VAL A 1 409 ? 26.98732 -44.63225 -3.86704  1.000 14.83818 ? 409  VAL A N     1 
ATOM   3086 C CA    . VAL A 1 409 ? 26.64231 -45.98569 -3.44472  1.000 14.89884 ? 409  VAL A CA    1 
ATOM   3087 C C     . VAL A 1 409 ? 27.12216 -46.95137 -4.51753  1.000 16.19760 ? 409  VAL A C     1 
ATOM   3088 O O     . VAL A 1 409 ? 26.70277 -46.85278 -5.67732  1.000 15.74415 ? 409  VAL A O     1 
ATOM   3089 C CB    . VAL A 1 409 ? 25.13269 -46.16051 -3.20819  1.000 14.03099 ? 409  VAL A CB    1 
ATOM   3090 C CG1   . VAL A 1 409 ? 24.82867 -47.59907 -2.82709  1.000 15.37221 ? 409  VAL A CG1   1 
ATOM   3091 C CG2   . VAL A 1 409 ? 24.64122 -45.21161 -2.12741  1.000 15.14711 ? 409  VAL A CG2   1 
ATOM   3092 N N     . CYS A 1 410 ? 27.99336 -47.88099 -4.13539  1.000 14.63023 ? 410  CYS A N     1 
ATOM   3093 C CA    . CYS A 1 410 ? 28.45981 -48.93299 -5.02978  1.000 16.25628 ? 410  CYS A CA    1 
ATOM   3094 C C     . CYS A 1 410 ? 27.71545 -50.22186 -4.71655  1.000 19.91062 ? 410  CYS A C     1 
ATOM   3095 O O     . CYS A 1 410 ? 27.76043 -50.71653 -3.58460  1.000 19.46142 ? 410  CYS A O     1 
ATOM   3096 C CB    . CYS A 1 410 ? 29.96704 -49.13819 -4.91068  1.000 19.36459 ? 410  CYS A CB    1 
ATOM   3097 S SG    . CYS A 1 410 ? 30.90330 -47.68459 -5.36263  1.000 20.48250 ? 410  CYS A SG    1 
ATOM   3098 N N     . PHE A 1 411 ? 27.04395 -50.76399 -5.72547  1.000 16.06329 ? 411  PHE A N     1 
ATOM   3099 C CA    . PHE A 1 411 ? 26.17401 -51.91280 -5.54689  1.000 17.59094 ? 411  PHE A CA    1 
ATOM   3100 C C     . PHE A 1 411 ? 26.25795 -52.78959 -6.78404  1.000 18.46284 ? 411  PHE A C     1 
ATOM   3101 O O     . PHE A 1 411 ? 26.72590 -52.36245 -7.84292  1.000 20.01120 ? 411  PHE A O     1 
ATOM   3102 C CB    . PHE A 1 411 ? 24.72704 -51.47799 -5.30072  1.000 18.92230 ? 411  PHE A CB    1 
ATOM   3103 C CG    . PHE A 1 411 ? 24.06421 -50.89934 -6.51561  1.000 20.09806 ? 411  PHE A CG    1 
ATOM   3104 C CD1   . PHE A 1 411 ? 24.41844 -49.64066 -6.97928  1.000 16.23332 ? 411  PHE A CD1   1 
ATOM   3105 C CD2   . PHE A 1 411 ? 23.10411 -51.61688 -7.20586  1.000 19.59207 ? 411  PHE A CD2   1 
ATOM   3106 C CE1   . PHE A 1 411 ? 23.81937 -49.10514 -8.10244  1.000 18.06096 ? 411  PHE A CE1   1 
ATOM   3107 C CE2   . PHE A 1 411 ? 22.49975 -51.08819 -8.32937  1.000 19.62616 ? 411  PHE A CE2   1 
ATOM   3108 C CZ    . PHE A 1 411 ? 22.85741 -49.82995 -8.77869  1.000 18.79808 ? 411  PHE A CZ    1 
ATOM   3109 N N     . ARG A 1 412 ? 25.78714 -54.02386 -6.63983  1.000 19.45452 ? 412  ARG A N     1 
ATOM   3110 C CA    . ARG A 1 412 ? 25.75811 -54.94715 -7.76255  1.000 20.07445 ? 412  ARG A CA    1 
ATOM   3111 C C     . ARG A 1 412 ? 24.82809 -56.10089 -7.43095  1.000 22.92579 ? 412  ARG A C     1 
ATOM   3112 O O     . ARG A 1 412 ? 24.55153 -56.38908 -6.26377  1.000 21.15737 ? 412  ARG A O     1 
ATOM   3113 C CB    . ARG A 1 412 ? 27.15428 -55.47664 -8.09954  1.000 23.09133 ? 412  ARG A CB    1 
ATOM   3114 C CG    . ARG A 1 412 ? 27.70555 -56.43220 -7.06498  1.000 25.67177 ? 412  ARG A CG    1 
ATOM   3115 C CD    . ARG A 1 412 ? 29.16800 -56.71318 -7.31845  1.000 26.67626 ? 412  ARG A CD    1 
ATOM   3116 N NE    . ARG A 1 412 ? 29.39912 -57.39684 -8.58579  1.000 27.50998 ? 412  ARG A NE    1 
ATOM   3117 C CZ    . ARG A 1 412 ? 29.28040 -58.70587 -8.76137  1.000 31.94526 ? 412  ARG A CZ    1 
ATOM   3118 N NH1   . ARG A 1 412 ? 28.92388 -59.50682 -7.77023  1.000 28.42783 ? 412  ARG A NH1   1 
ATOM   3119 N NH2   . ARG A 1 412 ? 29.53673 -59.22623 -9.95826  1.000 31.80766 ? 412  ARG A NH2   1 
ATOM   3120 N N     . LEU A 1 413 ? 24.34542 -56.75315 -8.48166  1.000 20.75832 ? 413  LEU A N     1 
ATOM   3121 C CA    . LEU A 1 413 ? 23.63471 -58.01079 -8.31754  1.000 23.37566 ? 413  LEU A CA    1 
ATOM   3122 C C     . LEU A 1 413 ? 24.60953 -59.07826 -7.83756  1.000 24.17952 ? 413  LEU A C     1 
ATOM   3123 O O     . LEU A 1 413 ? 25.72259 -59.19187 -8.36094  1.000 25.94261 ? 413  LEU A O     1 
ATOM   3124 C CB    . LEU A 1 413 ? 23.00162 -58.42948 -9.64325  1.000 23.48432 ? 413  LEU A CB    1 
ATOM   3125 C CG    . LEU A 1 413 ? 21.67535 -57.78178 -10.04543 1.000 27.57291 ? 413  LEU A CG    1 
ATOM   3126 C CD1   . LEU A 1 413 ? 21.31609 -58.14632 -11.47733 1.000 27.48749 ? 413  LEU A CD1   1 
ATOM   3127 C CD2   . LEU A 1 413 ? 20.56647 -58.19777 -9.09413  1.000 24.63034 ? 413  LEU A CD2   1 
ATOM   3128 N N     . LYS A 1 414 ? 24.20763 -59.85248 -6.83220  1.000 22.85889 ? 414  LYS A N     1 
ATOM   3129 C CA    . LYS A 1 414 ? 25.01842 -60.99806 -6.44552  1.000 24.53763 ? 414  LYS A CA    1 
ATOM   3130 C C     . LYS A 1 414 ? 25.10221 -61.97838 -7.60634  1.000 26.74156 ? 414  LYS A C     1 
ATOM   3131 O O     . LYS A 1 414 ? 24.09150 -62.30573 -8.23579  1.000 29.64622 ? 414  LYS A O     1 
ATOM   3132 C CB    . LYS A 1 414 ? 24.44611 -61.68581 -5.20727  1.000 27.02187 ? 414  LYS A CB    1 
ATOM   3133 C CG    . LYS A 1 414 ? 24.54276 -60.85893 -3.93822  1.000 28.92712 ? 414  LYS A CG    1 
ATOM   3134 C CD    . LYS A 1 414 ? 24.31543 -61.73230 -2.72044  1.000 33.20129 ? 414  LYS A CD    1 
ATOM   3135 C CE    . LYS A 1 414 ? 23.97599 -60.91310 -1.49224  1.000 36.41729 ? 414  LYS A CE    1 
ATOM   3136 N NZ    . LYS A 1 414 ? 22.87664 -61.52587 -0.70148  1.000 36.65583 ? 414  LYS A NZ    1 
ATOM   3137 N N     . GLY A 1 415 ? 26.31678 -62.42556 -7.90497  1.000 29.90762 ? 415  GLY A N     1 
ATOM   3138 C CA    . GLY A 1 415 ? 26.52444 -63.31180 -9.03055  1.000 28.06161 ? 415  GLY A CA    1 
ATOM   3139 C C     . GLY A 1 415 ? 27.60351 -62.85687 -9.99019  1.000 28.88392 ? 415  GLY A C     1 
ATOM   3140 O O     . GLY A 1 415 ? 28.55758 -62.18112 -9.59227  1.000 28.31470 ? 415  GLY A O     1 
ATOM   3141 N N     . SER A 1 416 ? 27.44070 -63.19486 -11.26660 1.000 31.42661 ? 416  SER A N     1 
ATOM   3142 C CA    . SER A 1 416 ? 28.49753 -63.00835 -12.24781 1.000 28.59824 ? 416  SER A CA    1 
ATOM   3143 C C     . SER A 1 416 ? 28.68214 -61.53470 -12.59435 1.000 28.84671 ? 416  SER A C     1 
ATOM   3144 O O     . SER A 1 416 ? 27.79181 -60.70552 -12.40361 1.000 24.25785 ? 416  SER A O     1 
ATOM   3145 C CB    . SER A 1 416 ? 28.18351 -63.79968 -13.51872 1.000 31.16894 ? 416  SER A CB    1 
ATOM   3146 O OG    . SER A 1 416 ? 27.10375 -63.21393 -14.22674 1.000 30.26142 ? 416  SER A OG    1 
ATOM   3147 N N     . ASN A 1 417 ? 29.86973 -61.21824 -13.11635 1.000 25.15230 ? 417  ASN A N     1 
ATOM   3148 C CA    . ASN A 1 417 ? 30.09668 -59.89673 -13.68871 1.000 27.57677 ? 417  ASN A CA    1 
ATOM   3149 C C     . ASN A 1 417 ? 29.18738 -59.65697 -14.88689 1.000 27.96621 ? 417  ASN A C     1 
ATOM   3150 O O     . ASN A 1 417 ? 28.73720 -58.52897 -15.11836 1.000 28.14803 ? 417  ASN A O     1 
ATOM   3151 C CB    . ASN A 1 417 ? 31.56541 -59.74467 -14.09495 1.000 28.58408 ? 417  ASN A CB    1 
ATOM   3152 C CG    . ASN A 1 417 ? 32.47705 -59.43775 -12.91709 1.000 30.52572 ? 417  ASN A CG    1 
ATOM   3153 O OD1   . ASN A 1 417 ? 32.01863 -59.02900 -11.85055 1.000 28.18163 ? 417  ASN A OD1   1 
ATOM   3154 N ND2   . ASN A 1 417 ? 33.77863 -59.62800 -13.11117 1.000 32.31292 ? 417  ASN A ND2   1 
ATOM   3155 N N     . LYS A 1 418 ? 28.90709 -60.70966 -15.66008 1.000 26.72752 ? 418  LYS A N     1 
ATOM   3156 C CA    . LYS A 1 418 ? 28.09350 -60.56204 -16.86438 1.000 29.37175 ? 418  LYS A CA    1 
ATOM   3157 C C     . LYS A 1 418 ? 26.69566 -60.05919 -16.52046 1.000 29.27370 ? 418  LYS A C     1 
ATOM   3158 O O     . LYS A 1 418 ? 26.16758 -59.16119 -17.18585 1.000 30.96328 ? 418  LYS A O     1 
ATOM   3159 C CB    . LYS A 1 418 ? 28.06291 -61.89892 -17.63374 1.000 33.29586 ? 418  LYS A CB    1 
ATOM   3160 C CG    . LYS A 1 418 ? 26.95527 -62.13533 -18.70537 1.000 38.14047 ? 418  LYS A CG    1 
ATOM   3161 C CD    . LYS A 1 418 ? 25.51553 -62.21809 -18.18296 1.000 42.97850 ? 418  LYS A CD    1 
ATOM   3162 C CE    . LYS A 1 418 ? 24.51864 -62.47483 -19.28192 1.000 50.44367 ? 418  LYS A CE    1 
ATOM   3163 N NZ    . LYS A 1 418 ? 23.12837 -62.24053 -18.79821 1.000 49.50050 ? 418  LYS A NZ    1 
ATOM   3164 N N     . VAL A 1 419 ? 26.07328 -60.63576 -15.48886 1.000 27.40104 ? 419  VAL A N     1 
ATOM   3165 C CA    . VAL A 1 419 ? 24.70777 -60.24898 -15.15240 1.000 29.98201 ? 419  VAL A CA    1 
ATOM   3166 C C     . VAL A 1 419 ? 24.66147 -58.78635 -14.73607 1.000 27.09167 ? 419  VAL A C     1 
ATOM   3167 O O     . VAL A 1 419 ? 23.64784 -58.10583 -14.93528 1.000 28.08542 ? 419  VAL A O     1 
ATOM   3168 C CB    . VAL A 1 419 ? 24.13973 -61.18557 -14.06284 1.000 31.11490 ? 419  VAL A CB    1 
ATOM   3169 C CG1   . VAL A 1 419 ? 24.71527 -60.85566 -12.69643 1.000 31.98136 ? 419  VAL A CG1   1 
ATOM   3170 C CG2   . VAL A 1 419 ? 22.62897 -61.13063 -14.03921 1.000 34.59596 ? 419  VAL A CG2   1 
ATOM   3171 N N     . ASN A 1 420 ? 25.76257 -58.26924 -14.18964 1.000 25.27875 ? 420  ASN A N     1 
ATOM   3172 C CA    . ASN A 1 420 ? 25.81867 -56.86398 -13.81144 1.000 23.90245 ? 420  ASN A CA    1 
ATOM   3173 C C     . ASN A 1 420 ? 26.11968 -55.97770 -15.01317 1.000 24.59470 ? 420  ASN A C     1 
ATOM   3174 O O     . ASN A 1 420 ? 25.56952 -54.87609 -15.12626 1.000 22.83716 ? 420  ASN A O     1 
ATOM   3175 C CB    . ASN A 1 420 ? 26.85773 -56.66944 -12.71125 1.000 24.48090 ? 420  ASN A CB    1 
ATOM   3176 C CG    . ASN A 1 420 ? 26.32142 -57.04009 -11.34812 1.000 26.35969 ? 420  ASN A CG    1 
ATOM   3177 O OD1   . ASN A 1 420 ? 25.41706 -56.38835 -10.82863 1.000 24.86325 ? 420  ASN A OD1   1 
ATOM   3178 N ND2   . ASN A 1 420 ? 26.85775 -58.10851 -10.77069 1.000 25.57350 ? 420  ASN A ND2   1 
ATOM   3179 N N     . GLU A 1 421 ? 26.98444 -56.43883 -15.92174 1.000 26.28734 ? 421  GLU A N     1 
ATOM   3180 C CA    . GLU A 1 421 ? 27.15082 -55.72935 -17.18547 1.000 27.19627 ? 421  GLU A CA    1 
ATOM   3181 C C     . GLU A 1 421 ? 25.82412 -55.62753 -17.92462 1.000 24.46010 ? 421  GLU A C     1 
ATOM   3182 O O     . GLU A 1 421 ? 25.46368 -54.55518 -18.41878 1.000 28.90691 ? 421  GLU A O     1 
ATOM   3183 C CB    . GLU A 1 421 ? 28.20471 -56.41742 -18.05801 1.000 27.38463 ? 421  GLU A CB    1 
ATOM   3184 C CG    . GLU A 1 421 ? 29.61692 -56.39302 -17.48234 1.000 30.60572 ? 421  GLU A CG    1 
ATOM   3185 C CD    . GLU A 1 421 ? 30.50862 -57.49257 -18.04139 1.000 36.40068 ? 421  GLU A CD    1 
ATOM   3186 O OE1   . GLU A 1 421 ? 30.10601 -58.15429 -19.02179 1.000 39.84376 ? 421  GLU A OE1   1 
ATOM   3187 O OE2   . GLU A 1 421 ? 31.61560 -57.69434 -17.49762 1.000 42.30341 ? 421  GLU A OE2   1 
ATOM   3188 N N     . ALA A 1 422 ? 25.06768 -56.72680 -17.97785 1.000 26.48090 ? 422  ALA A N     1 
ATOM   3189 C CA    . ALA A 1 422 ? 23.77035 -56.70755 -18.64726 1.000 28.23542 ? 422  ALA A CA    1 
ATOM   3190 C C     . ALA A 1 422 ? 22.81452 -55.71966 -17.98583 1.000 27.49911 ? 422  ALA A C     1 
ATOM   3191 O O     . ALA A 1 422 ? 22.04732 -55.03393 -18.67202 1.000 28.02974 ? 422  ALA A O     1 
ATOM   3192 C CB    . ALA A 1 422 ? 23.16807 -58.11345 -18.65981 1.000 28.72213 ? 422  ALA A CB    1 
ATOM   3193 N N     . LEU A 1 423 ? 22.84794 -55.63053 -16.65288 1.000 26.55039 ? 423  LEU A N     1 
ATOM   3194 C CA    . LEU A 1 423 ? 21.98284 -54.68668 -15.94963 1.000 26.84262 ? 423  LEU A CA    1 
ATOM   3195 C C     . LEU A 1 423 ? 22.32379 -53.24604 -16.31131 1.000 25.18102 ? 423  LEU A C     1 
ATOM   3196 O O     . LEU A 1 423 ? 21.42600 -52.42793 -16.54788 1.000 25.32213 ? 423  LEU A O     1 
ATOM   3197 C CB    . LEU A 1 423 ? 22.08966 -54.89941 -14.43887 1.000 23.07071 ? 423  LEU A CB    1 
ATOM   3198 C CG    . LEU A 1 423 ? 21.28866 -53.94183 -13.54953 1.000 23.25890 ? 423  LEU A CG    1 
ATOM   3199 C CD1   . LEU A 1 423 ? 19.82737 -53.88200 -13.97792 1.000 21.92891 ? 423  LEU A CD1   1 
ATOM   3200 C CD2   . LEU A 1 423 ? 21.40103 -54.33569 -12.08524 1.000 20.90342 ? 423  LEU A CD2   1 
ATOM   3201 N N     . LEU A 1 424 ? 23.61841 -52.91741 -16.36179 1.000 24.32697 ? 424  LEU A N     1 
ATOM   3202 C CA    . LEU A 1 424 ? 24.03088 -51.55465 -16.68780 1.000 25.58491 ? 424  LEU A CA    1 
ATOM   3203 C C     . LEU A 1 424 ? 23.62824 -51.17491 -18.10813 1.000 27.75875 ? 424  LEU A C     1 
ATOM   3204 O O     . LEU A 1 424 ? 23.09651 -50.08122 -18.33632 1.000 26.82365 ? 424  LEU A O     1 
ATOM   3205 C CB    . LEU A 1 424 ? 25.53861 -51.40897 -16.50703 1.000 27.01307 ? 424  LEU A CB    1 
ATOM   3206 C CG    . LEU A 1 424 ? 26.08377 -50.04490 -16.93314 1.000 28.84869 ? 424  LEU A CG    1 
ATOM   3207 C CD1   . LEU A 1 424 ? 25.98528 -49.04635 -15.78820 1.000 27.96615 ? 424  LEU A CD1   1 
ATOM   3208 C CD2   . LEU A 1 424 ? 27.50436 -50.16571 -17.45562 1.000 31.90057 ? 424  LEU A CD2   1 
ATOM   3209 N N     . GLN A 1 425 ? 23.88430 -52.06156 -19.07606 1.000 27.16431 ? 425  GLN A N     1 
ATOM   3210 C CA    . GLN A 1 425 ? 23.47917 -51.79884 -20.45461 1.000 31.12162 ? 425  GLN A CA    1 
ATOM   3211 C C     . GLN A 1 425 ? 21.97641 -51.58011 -20.54836 1.000 30.18568 ? 425  GLN A C     1 
ATOM   3212 O O     . GLN A 1 425 ? 21.51706 -50.66450 -21.24160 1.000 29.47158 ? 425  GLN A O     1 
ATOM   3213 C CB    . GLN A 1 425 ? 23.90567 -52.95825 -21.35737 1.000 33.30595 ? 425  GLN A CB    1 
ATOM   3214 C CG    . GLN A 1 425 ? 25.33633 -53.40034 -21.14209 1.000 40.82215 ? 425  GLN A CG    1 
ATOM   3215 C CD    . GLN A 1 425 ? 25.88683 -54.26810 -22.25397 1.000 49.60308 ? 425  GLN A CD    1 
ATOM   3216 O OE1   . GLN A 1 425 ? 25.20323 -55.15042 -22.77531 1.000 53.23563 ? 425  GLN A OE1   1 
ATOM   3217 N NE2   . GLN A 1 425 ? 27.14373 -54.03492 -22.60700 1.000 52.13810 ? 425  GLN A NE2   1 
ATOM   3218 N N     . ARG A 1 426 ? 21.19909 -52.40884 -19.84334 1.000 27.05295 ? 426  ARG A N     1 
ATOM   3219 C CA    . ARG A 1 426 ? 19.74643 -52.27021 -19.84185 1.000 27.02371 ? 426  ARG A CA    1 
ATOM   3220 C C     . ARG A 1 426 ? 19.31371 -50.92037 -19.28029 1.000 26.18525 ? 426  ARG A C     1 
ATOM   3221 O O     . ARG A 1 426 ? 18.38848 -50.28943 -19.80514 1.000 27.42064 ? 426  ARG A O     1 
ATOM   3222 C CB    . ARG A 1 426 ? 19.12468 -53.41247 -19.03631 1.000 30.72131 ? 426  ARG A CB    1 
ATOM   3223 C CG    . ARG A 1 426 ? 17.70555 -53.79023 -19.44931 1.000 37.54715 ? 426  ARG A CG    1 
ATOM   3224 C CD    . ARG A 1 426 ? 17.70286 -54.85302 -20.54975 1.000 40.32726 ? 426  ARG A CD    1 
ATOM   3225 N NE    . ARG A 1 426 ? 16.40180 -55.50076 -20.69368 1.000 50.25178 ? 426  ARG A NE    1 
ATOM   3226 C CZ    . ARG A 1 426 ? 16.20940 -56.81446 -20.71533 1.000 48.32460 ? 426  ARG A CZ    1 
ATOM   3227 N NH1   . ARG A 1 426 ? 17.23023 -57.66310 -20.61789 1.000 50.26587 ? 426  ARG A NH1   1 
ATOM   3228 N NH2   . ARG A 1 426 ? 14.96124 -57.28811 -20.81275 1.000 54.60504 ? 426  ARG A NH2   1 
ATOM   3229 N N     . ILE A 1 427 ? 19.97823 -50.45550 -18.22271 1.000 23.79126 ? 427  ILE A N     1 
ATOM   3230 C CA    . ILE A 1 427 ? 19.61691 -49.17619 -17.61642 1.000 24.92281 ? 427  ILE A CA    1 
ATOM   3231 C C     . ILE A 1 427 ? 19.96528 -48.02529 -18.55136 1.000 26.26113 ? 427  ILE A C     1 
ATOM   3232 O O     . ILE A 1 427 ? 19.10980 -47.20653 -18.90698 1.000 26.47787 ? 427  ILE A O     1 
ATOM   3233 C CB    . ILE A 1 427 ? 20.30315 -49.01098 -16.24935 1.000 23.67755 ? 427  ILE A CB    1 
ATOM   3234 C CG1   . ILE A 1 427 ? 19.71156 -49.98547 -15.22557 1.000 22.65479 ? 427  ILE A CG1   1 
ATOM   3235 C CG2   . ILE A 1 427 ? 20.18319 -47.57567 -15.77100 1.000 20.59012 ? 427  ILE A CG2   1 
ATOM   3236 C CD1   . ILE A 1 427 ? 20.61676 -50.21990 -14.03483 1.000 24.43019 ? 427  ILE A CD1   1 
ATOM   3237 N N     . ASN A 1 428 ? 21.23171 -47.94477 -18.96292 1.000 25.62981 ? 428  ASN A N     1 
ATOM   3238 C CA    . ASN A 1 428 ? 21.67720 -46.80941 -19.76237 1.000 25.18069 ? 428  ASN A CA    1 
ATOM   3239 C C     . ASN A 1 428 ? 21.04868 -46.79855 -21.14867 1.000 27.57503 ? 428  ASN A C     1 
ATOM   3240 O O     . ASN A 1 428 ? 20.94887 -45.72956 -21.75782 1.000 32.84970 ? 428  ASN A O     1 
ATOM   3241 C CB    . ASN A 1 428 ? 23.20244 -46.81200 -19.86211 1.000 23.59390 ? 428  ASN A CB    1 
ATOM   3242 C CG    . ASN A 1 428 ? 23.86591 -46.21220 -18.63016 1.000 27.76612 ? 428  ASN A CG    1 
ATOM   3243 O OD1   . ASN A 1 428 ? 23.21486 -45.54688 -17.82187 1.000 22.66359 ? 428  ASN A OD1   1 
ATOM   3244 N ND2   . ASN A 1 428 ? 25.16484 -46.45170 -18.47861 1.000 27.83412 ? 428  ASN A ND2   1 
ATOM   3245 N N     . SER A 1 429 ? 20.60693 -47.95470 -21.65437 1.000 26.10588 ? 429  SER A N     1 
ATOM   3246 C CA    . SER A 1 429 ? 19.90258 -47.97728 -22.93304 1.000 30.77848 ? 429  SER A CA    1 
ATOM   3247 C C     . SER A 1 429 ? 18.46343 -47.49262 -22.79995 1.000 30.99465 ? 429  SER A C     1 
ATOM   3248 O O     . SER A 1 429 ? 17.90760 -46.94724 -23.76034 1.000 32.39218 ? 429  SER A O     1 
ATOM   3249 C CB    . SER A 1 429 ? 19.92205 -49.38307 -23.53396 1.000 33.00701 ? 429  SER A CB    1 
ATOM   3250 O OG    . SER A 1 429 ? 21.22152 -49.74182 -23.97208 1.000 40.33844 ? 429  SER A OG    1 
ATOM   3251 N N     . ALA A 1 430 ? 17.84405 -47.68321 -21.63080 1.000 27.91398 ? 430  ALA A N     1 
ATOM   3252 C CA    . ALA A 1 430 ? 16.49690 -47.16286 -21.41539 1.000 27.92397 ? 430  ALA A CA    1 
ATOM   3253 C C     . ALA A 1 430 ? 16.48708 -45.64180 -21.34333 1.000 27.08316 ? 430  ALA A C     1 
ATOM   3254 O O     . ALA A 1 430 ? 15.47928 -45.01579 -21.69047 1.000 27.40834 ? 430  ALA A O     1 
ATOM   3255 C CB    . ALA A 1 430 ? 15.89802 -47.75670 -20.14099 1.000 26.71267 ? 430  ALA A CB    1 
ATOM   3256 N N     . LYS A 1 431 ? 17.58796 -45.04045 -20.88349 1.000 22.43685 ? 431  LYS A N     1 
ATOM   3257 C CA    . LYS A 1 431 ? 17.79066 -43.58924 -20.89946 1.000 24.67188 ? 431  LYS A CA    1 
ATOM   3258 C C     . LYS A 1 431 ? 16.75953 -42.85019 -20.04924 1.000 24.93823 ? 431  LYS A C     1 
ATOM   3259 O O     . LYS A 1 431 ? 16.44058 -41.68669 -20.30904 1.000 26.42567 ? 431  LYS A O     1 
ATOM   3260 C CB    . LYS A 1 431 ? 17.80590 -43.05261 -22.33422 1.000 26.75970 ? 431  LYS A CB    1 
ATOM   3261 C CG    . LYS A 1 431 ? 18.79419 -43.79305 -23.22154 1.000 25.96685 ? 431  LYS A CG    1 
ATOM   3262 C CD    . LYS A 1 431 ? 19.31200 -42.94282 -24.36453 1.000 28.16314 ? 431  LYS A CD    1 
ATOM   3263 C CE    . LYS A 1 431 ? 20.11633 -43.79279 -25.33755 1.000 28.59376 ? 431  LYS A CE    1 
ATOM   3264 N NZ    . LYS A 1 431 ? 19.32859 -44.93707 -25.87944 1.000 32.07921 ? 431  LYS A NZ    1 
ATOM   3265 N N     . LYS A 1 432 ? 16.23347 -43.51951 -19.02430 1.000 22.40062 ? 432  LYS A N     1 
ATOM   3266 C CA    . LYS A 1 432 ? 15.42841 -42.85276 -18.00841 1.000 21.57498 ? 432  LYS A CA    1 
ATOM   3267 C C     . LYS A 1 432 ? 16.29843 -42.28998 -16.89231 1.000 20.00299 ? 432  LYS A C     1 
ATOM   3268 O O     . LYS A 1 432 ? 16.05676 -41.17601 -16.41443 1.000 19.41677 ? 432  LYS A O     1 
ATOM   3269 C CB    . LYS A 1 432 ? 14.39475 -43.82276 -17.43421 1.000 22.61750 ? 432  LYS A CB    1 
ATOM   3270 C CG    . LYS A 1 432 ? 13.36247 -44.28578 -18.44410 1.000 26.57825 ? 432  LYS A CG    1 
ATOM   3271 C CD    . LYS A 1 432 ? 12.33364 -45.19778 -17.80077 1.000 28.14100 ? 432  LYS A CD    1 
ATOM   3272 C CE    . LYS A 1 432 ? 10.96612 -44.98706 -18.41870 1.000 41.17176 ? 432  LYS A CE    1 
ATOM   3273 N NZ    . LYS A 1 432 ? 11.08429 -44.63308 -19.85923 1.000 46.72029 ? 432  LYS A NZ    1 
ATOM   3274 N N     . ILE A 1 433 ? 17.30596 -43.05247 -16.46896 1.000 17.05460 ? 433  ILE A N     1 
ATOM   3275 C CA    . ILE A 1 433 ? 18.36147 -42.58092 -15.58465 1.000 17.44678 ? 433  ILE A CA    1 
ATOM   3276 C C     . ILE A 1 433 ? 19.69603 -42.91350 -16.24256 1.000 18.57822 ? 433  ILE A C     1 
ATOM   3277 O O     . ILE A 1 433 ? 19.75923 -43.65056 -17.22712 1.000 18.86278 ? 433  ILE A O     1 
ATOM   3278 C CB    . ILE A 1 433 ? 18.27174 -43.20320 -14.17579 1.000 17.93920 ? 433  ILE A CB    1 
ATOM   3279 C CG1   . ILE A 1 433 ? 18.70403 -44.66802 -14.21947 1.000 18.26935 ? 433  ILE A CG1   1 
ATOM   3280 C CG2   . ILE A 1 433 ? 16.85896 -43.07569 -13.61781 1.000 16.97635 ? 433  ILE A CG2   1 
ATOM   3281 C CD1   . ILE A 1 433 ? 18.76508 -45.32527 -12.86205 1.000 20.62888 ? 433  ILE A CD1   1 
ATOM   3282 N N     . HIS A 1 434 ? 20.77280 -42.35674 -15.69114 1.000 14.09563 ? 434  HIS A N     1 
ATOM   3283 C CA    . HIS A 1 434 ? 22.10629 -42.56673 -16.24168 1.000 17.09204 ? 434  HIS A CA    1 
ATOM   3284 C C     . HIS A 1 434 ? 23.07267 -42.92390 -15.12273 1.000 17.49470 ? 434  HIS A C     1 
ATOM   3285 O O     . HIS A 1 434 ? 23.18072 -42.19189 -14.13311 1.000 14.91144 ? 434  HIS A O     1 
ATOM   3286 C CB    . HIS A 1 434 ? 22.59561 -41.32584 -16.99955 1.000 17.03959 ? 434  HIS A CB    1 
ATOM   3287 C CG    . HIS A 1 434 ? 23.81789 -41.56689 -17.83208 1.000 17.94978 ? 434  HIS A CG    1 
ATOM   3288 N ND1   . HIS A 1 434 ? 23.86395 -42.51966 -18.82704 1.000 22.79704 ? 434  HIS A ND1   1 
ATOM   3289 C CD2   . HIS A 1 434 ? 25.02888 -40.96039 -17.83703 1.000 19.88956 ? 434  HIS A CD2   1 
ATOM   3290 C CE1   . HIS A 1 434 ? 25.05601 -42.50203 -19.39685 1.000 24.78091 ? 434  HIS A CE1   1 
ATOM   3291 N NE2   . HIS A 1 434 ? 25.78139 -41.56347 -18.81578 1.000 20.28799 ? 434  HIS A NE2   1 
ATOM   3292 N N     . LEU A 1 435 ? 23.76612 -44.05069 -15.28688 1.000 19.27849 ? 435  LEU A N     1 
ATOM   3293 C CA    . LEU A 1 435 ? 24.75785 -44.53743 -14.33952 1.000 19.07244 ? 435  LEU A CA    1 
ATOM   3294 C C     . LEU A 1 435 ? 26.03459 -44.89532 -15.08574 1.000 18.54324 ? 435  LEU A C     1 
ATOM   3295 O O     . LEU A 1 435 ? 26.02563 -45.12343 -16.29814 1.000 20.07363 ? 435  LEU A O     1 
ATOM   3296 C CB    . LEU A 1 435 ? 24.26455 -45.77687 -13.57762 1.000 22.56001 ? 435  LEU A CB    1 
ATOM   3297 C CG    . LEU A 1 435 ? 22.91018 -45.76241 -12.87396 1.000 23.24655 ? 435  LEU A CG    1 
ATOM   3298 C CD1   . LEU A 1 435 ? 22.58771 -47.15853 -12.37629 1.000 24.64948 ? 435  LEU A CD1   1 
ATOM   3299 C CD2   . LEU A 1 435 ? 22.92780 -44.78607 -11.71755 1.000 26.52573 ? 435  LEU A CD2   1 
ATOM   3300 N N     . VAL A 1 436 ? 27.13914 -44.94650 -14.34654 1.000 17.53151 ? 436  VAL A N     1 
ATOM   3301 C CA    . VAL A 1 436 ? 28.39349 -45.47767 -14.87864 1.000 17.18552 ? 436  VAL A CA    1 
ATOM   3302 C C     . VAL A 1 436 ? 28.91034 -46.54683 -13.92266 1.000 21.18262 ? 436  VAL A C     1 
ATOM   3303 O O     . VAL A 1 436 ? 28.59785 -46.51137 -12.72296 1.000 20.83707 ? 436  VAL A O     1 
ATOM   3304 C CB    . VAL A 1 436 ? 29.44076 -44.37244 -15.10796 1.000 22.69346 ? 436  VAL A CB    1 
ATOM   3305 C CG1   . VAL A 1 436 ? 28.84436 -43.21262 -15.88730 1.000 23.99887 ? 436  VAL A CG1   1 
ATOM   3306 C CG2   . VAL A 1 436 ? 30.02762 -43.89209 -13.78674 1.000 22.58973 ? 436  VAL A CG2   1 
ATOM   3307 N N     . PRO A 1 437 ? 29.67278 -47.52770 -14.40649 1.000 20.13728 ? 437  PRO A N     1 
ATOM   3308 C CA    . PRO A 1 437 ? 30.19403 -48.56129 -13.50974 1.000 19.23223 ? 437  PRO A CA    1 
ATOM   3309 C C     . PRO A 1 437 ? 31.64471 -48.34174 -13.12241 1.000 20.51466 ? 437  PRO A C     1 
ATOM   3310 O O     . PRO A 1 437 ? 32.25816 -47.33009 -13.47641 1.000 21.55189 ? 437  PRO A O     1 
ATOM   3311 C CB    . PRO A 1 437 ? 30.04599 -49.82596 -14.35324 1.000 19.07075 ? 437  PRO A CB    1 
ATOM   3312 C CG    . PRO A 1 437 ? 30.43087 -49.33021 -15.72554 1.000 17.64643 ? 437  PRO A CG    1 
ATOM   3313 C CD    . PRO A 1 437 ? 29.89474 -47.89524 -15.81742 1.000 21.75173 ? 437  PRO A CD    1 
ATOM   3314 N N     . CYS A 1 438 ? 32.19651 -49.31034 -12.39748 1.000 19.94941 ? 438  CYS A N     1 
ATOM   3315 C CA    . CYS A 1 438 ? 33.61820 -49.35309 -12.09995 1.000 21.07792 ? 438  CYS A CA    1 
ATOM   3316 C C     . CYS A 1 438 ? 34.00385 -50.80227 -11.85048 1.000 24.21631 ? 438  CYS A C     1 
ATOM   3317 O O     . CYS A 1 438 ? 33.14829 -51.67725 -11.69269 1.000 21.53130 ? 438  CYS A O     1 
ATOM   3318 C CB    . CYS A 1 438 ? 33.97367 -48.48002 -10.89277 1.000 20.12660 ? 438  CYS A CB    1 
ATOM   3319 S SG    . CYS A 1 438 ? 33.26372 -49.05530 -9.33232  1.000 24.78662 ? 438  CYS A SG    1 
ATOM   3320 N N     . HIS A 1 439 ? 35.30797 -51.05265 -11.83096 1.000 22.63413 ? 439  HIS A N     1 
ATOM   3321 C CA    . HIS A 1 439 ? 35.84828 -52.35564 -11.46462 1.000 24.87639 ? 439  HIS A CA    1 
ATOM   3322 C C     . HIS A 1 439 ? 36.52627 -52.24926 -10.10777 1.000 25.42179 ? 439  HIS A C     1 
ATOM   3323 O O     . HIS A 1 439 ? 37.42426 -51.42244 -9.92227  1.000 24.96087 ? 439  HIS A O     1 
ATOM   3324 C CB    . HIS A 1 439 ? 36.82640 -52.87877 -12.51773 1.000 26.23846 ? 439  HIS A CB    1 
ATOM   3325 C CG    . HIS A 1 439 ? 36.15675 -53.54144 -13.67942 1.000 30.51803 ? 439  HIS A CG    1 
ATOM   3326 N ND1   . HIS A 1 439 ? 35.85856 -52.87604 -14.84814 1.000 33.73537 ? 439  HIS A ND1   1 
ATOM   3327 C CD2   . HIS A 1 439 ? 35.71091 -54.80918 -13.84338 1.000 32.48680 ? 439  HIS A CD2   1 
ATOM   3328 C CE1   . HIS A 1 439 ? 35.26777 -53.70825 -15.68667 1.000 32.27322 ? 439  HIS A CE1   1 
ATOM   3329 N NE2   . HIS A 1 439 ? 35.16562 -54.88752 -15.10105 1.000 34.70069 ? 439  HIS A NE2   1 
ATOM   3330 N N     . LEU A 1 440 ? 36.08392 -53.07320 -9.16509  1.000 23.13158 ? 440  LEU A N     1 
ATOM   3331 C CA    . LEU A 1 440 ? 36.70896 -53.20296 -7.85351  1.000 25.39527 ? 440  LEU A CA    1 
ATOM   3332 C C     . LEU A 1 440 ? 37.37361 -54.57447 -7.82329  1.000 26.80023 ? 440  LEU A C     1 
ATOM   3333 O O     . LEU A 1 440 ? 36.69173 -55.59482 -7.70982  1.000 25.54728 ? 440  LEU A O     1 
ATOM   3334 C CB    . LEU A 1 440 ? 35.67783 -53.04148 -6.74425  1.000 23.02964 ? 440  LEU A CB    1 
ATOM   3335 C CG    . LEU A 1 440 ? 35.02971 -51.65617 -6.63920  1.000 22.94499 ? 440  LEU A CG    1 
ATOM   3336 C CD1   . LEU A 1 440 ? 34.04831 -51.58937 -5.47961  1.000 21.65414 ? 440  LEU A CD1   1 
ATOM   3337 C CD2   . LEU A 1 440 ? 36.09441 -50.57224 -6.50894  1.000 22.80898 ? 440  LEU A CD2   1 
ATOM   3338 N N     . ARG A 1 441 ? 38.70250 -54.59472 -7.93278  1.000 26.65725 ? 441  ARG A N     1 
ATOM   3339 C CA    . ARG A 1 441 ? 39.46307 -55.81846 -8.19542  1.000 29.14871 ? 441  ARG A CA    1 
ATOM   3340 C C     . ARG A 1 441 ? 38.94199 -56.40927 -9.49762  1.000 30.98574 ? 441  ARG A C     1 
ATOM   3341 O O     . ARG A 1 441 ? 38.97711 -55.71603 -10.52748 1.000 32.63799 ? 441  ARG A O     1 
ATOM   3342 C CB    . ARG A 1 441 ? 39.37862 -56.75804 -6.99119  1.000 32.36202 ? 441  ARG A CB    1 
ATOM   3343 C CG    . ARG A 1 441 ? 39.52054 -56.11854 -5.64221  1.000 35.49703 ? 441  ARG A CG    1 
ATOM   3344 C CD    . ARG A 1 441 ? 40.94758 -55.77684 -5.26806  1.000 30.29509 ? 441  ARG A CD    1 
ATOM   3345 N NE    . ARG A 1 441 ? 41.03391 -55.14874 -3.94882  1.000 30.49410 ? 441  ARG A NE    1 
ATOM   3346 C CZ    . ARG A 1 441 ? 41.73494 -54.05377 -3.66751  1.000 27.85450 ? 441  ARG A CZ    1 
ATOM   3347 N NH1   . ARG A 1 441 ? 42.40900 -53.40102 -4.60215  1.000 30.87000 ? 441  ARG A NH1   1 
ATOM   3348 N NH2   . ARG A 1 441 ? 41.72146 -53.57417 -2.42461  1.000 28.03782 ? 441  ARG A NH2   1 
ATOM   3349 N N     . ASP A 1 442 ? 38.47729 -57.65331 -9.51011  1.000 32.82976 ? 442  ASP A N     1 
ATOM   3350 C CA    . ASP A 1 442 ? 37.91900 -58.33073 -10.67956 1.000 36.02028 ? 442  ASP A CA    1 
ATOM   3351 C C     . ASP A 1 442 ? 36.40994 -58.20687 -10.76050 1.000 32.81874 ? 442  ASP A C     1 
ATOM   3352 O O     . ASP A 1 442 ? 35.79186 -58.90712 -11.56535 1.000 31.99987 ? 442  ASP A O     1 
ATOM   3353 C CB    . ASP A 1 442 ? 38.30626 -59.81612 -10.64263 1.000 39.23775 ? 442  ASP A CB    1 
ATOM   3354 C CG    . ASP A 1 442 ? 37.81076 -60.49955 -9.38766  1.000 45.05695 ? 442  ASP A CG    1 
ATOM   3355 O OD1   . ASP A 1 442 ? 37.29793 -61.63770 -9.46672  1.000 54.62623 ? 442  ASP A OD1   1 
ATOM   3356 O OD2   . ASP A 1 442 ? 37.93400 -59.88029 -8.30528  1.000 44.52695 ? 442  ASP A OD2   1 
ATOM   3357 N N     . LYS A 1 443 ? 35.80967 -57.32906 -9.95870  1.000 28.10479 ? 443  LYS A N     1 
ATOM   3358 C CA    . LYS A 1 443 ? 34.36486 -57.28389 -9.76613  1.000 26.61526 ? 443  LYS A CA    1 
ATOM   3359 C C     . LYS A 1 443 ? 33.78297 -56.07835 -10.49745 1.000 24.63216 ? 443  LYS A C     1 
ATOM   3360 O O     . LYS A 1 443 ? 34.19234 -54.93982 -10.24706 1.000 23.22269 ? 443  LYS A O     1 
ATOM   3361 C CB    . LYS A 1 443 ? 34.03278 -57.21968 -8.27504  1.000 26.05559 ? 443  LYS A CB    1 
ATOM   3362 C CG    . LYS A 1 443 ? 32.62387 -57.60059 -7.92265  1.000 31.32334 ? 443  LYS A CG    1 
ATOM   3363 C CD    . LYS A 1 443 ? 32.46095 -57.76197 -6.42099  1.000 33.91629 ? 443  LYS A CD    1 
ATOM   3364 C CE    . LYS A 1 443 ? 32.69222 -56.45107 -5.69468  1.000 34.72007 ? 443  LYS A CE    1 
ATOM   3365 N NZ    . LYS A 1 443 ? 32.22198 -56.50473 -4.28304  1.000 36.65758 ? 443  LYS A NZ    1 
ATOM   3366 N N     . PHE A 1 444 ? 32.83583 -56.33271 -11.39872 1.000 23.12841 ? 444  PHE A N     1 
ATOM   3367 C CA    . PHE A 1 444 ? 32.11826 -55.27056 -12.09437 1.000 23.92496 ? 444  PHE A CA    1 
ATOM   3368 C C     . PHE A 1 444 ? 31.04087 -54.72051 -11.16750 1.000 21.93186 ? 444  PHE A C     1 
ATOM   3369 O O     . PHE A 1 444 ? 30.18845 -55.47358 -10.68495 1.000 21.62105 ? 444  PHE A O     1 
ATOM   3370 C CB    . PHE A 1 444 ? 31.51510 -55.81183 -13.39118 1.000 23.57767 ? 444  PHE A CB    1 
ATOM   3371 C CG    . PHE A 1 444 ? 30.82355 -54.77528 -14.22970 1.000 26.15698 ? 444  PHE A CG    1 
ATOM   3372 C CD1   . PHE A 1 444 ? 29.47910 -54.49536 -14.04482 1.000 23.03895 ? 444  PHE A CD1   1 
ATOM   3373 C CD2   . PHE A 1 444 ? 31.51719 -54.08903 -15.21446 1.000 25.45131 ? 444  PHE A CD2   1 
ATOM   3374 C CE1   . PHE A 1 444 ? 28.83744 -53.54499 -14.82342 1.000 22.08232 ? 444  PHE A CE1   1 
ATOM   3375 C CE2   . PHE A 1 444 ? 30.88315 -53.13896 -15.99708 1.000 25.57308 ? 444  PHE A CE2   1 
ATOM   3376 C CZ    . PHE A 1 444 ? 29.53995 -52.86888 -15.80296 1.000 23.52118 ? 444  PHE A CZ    1 
ATOM   3377 N N     . VAL A 1 445 ? 31.08050 -53.41537 -10.91387 1.000 20.57749 ? 445  VAL A N     1 
ATOM   3378 C CA    . VAL A 1 445 ? 30.26723 -52.78996 -9.87877  1.000 20.38038 ? 445  VAL A CA    1 
ATOM   3379 C C     . VAL A 1 445 ? 29.54409 -51.58779 -10.46904 1.000 20.20353 ? 445  VAL A C     1 
ATOM   3380 O O     . VAL A 1 445 ? 30.12415 -50.82591 -11.24996 1.000 20.61220 ? 445  VAL A O     1 
ATOM   3381 C CB    . VAL A 1 445 ? 31.13433 -52.36749 -8.67153  1.000 21.63643 ? 445  VAL A CB    1 
ATOM   3382 C CG1   . VAL A 1 445 ? 30.32127 -51.55430 -7.67194  1.000 22.66357 ? 445  VAL A CG1   1 
ATOM   3383 C CG2   . VAL A 1 445 ? 31.75635 -53.58861 -8.00373  1.000 20.08963 ? 445  VAL A CG2   1 
ATOM   3384 N N     . LEU A 1 446 ? 28.27758 -51.41685 -10.09271 1.000 19.41485 ? 446  LEU A N     1 
ATOM   3385 C CA    . LEU A 1 446 ? 27.50390 -50.25509 -10.50360 1.000 18.04946 ? 446  LEU A CA    1 
ATOM   3386 C C     . LEU A 1 446 ? 27.62880 -49.14168 -9.47017  1.000 18.51505 ? 446  LEU A C     1 
ATOM   3387 O O     . LEU A 1 446 ? 27.69778 -49.40074 -8.26486  1.000 18.47615 ? 446  LEU A O     1 
ATOM   3388 C CB    . LEU A 1 446 ? 26.02966 -50.61876 -10.69336 1.000 19.02104 ? 446  LEU A CB    1 
ATOM   3389 C CG    . LEU A 1 446 ? 25.61184 -51.36847 -11.96097 1.000 22.42813 ? 446  LEU A CG    1 
ATOM   3390 C CD1   . LEU A 1 446 ? 26.03384 -52.83232 -11.92949 1.000 21.32678 ? 446  LEU A CD1   1 
ATOM   3391 C CD2   . LEU A 1 446 ? 24.11005 -51.23470 -12.17485 1.000 24.32978 ? 446  LEU A CD2   1 
ATOM   3392 N N     . ARG A 1 447 ? 27.65688 -47.90027 -9.95095  1.000 15.43645 ? 447  ARG A N     1 
ATOM   3393 C CA    . ARG A 1 447 ? 27.73721 -46.71982 -9.10104  1.000 17.54884 ? 447  ARG A CA    1 
ATOM   3394 C C     . ARG A 1 447 ? 26.42910 -45.94446 -9.17176  1.000 17.70675 ? 447  ARG A C     1 
ATOM   3395 O O     . ARG A 1 447 ? 25.82723 -45.81737 -10.24305 1.000 18.13393 ? 447  ARG A O     1 
ATOM   3396 C CB    . ARG A 1 447 ? 28.89907 -45.80520 -9.51630  1.000 14.78620 ? 447  ARG A CB    1 
ATOM   3397 C CG    . ARG A 1 447 ? 30.28598 -46.42957 -9.40900  1.000 16.76485 ? 447  ARG A CG    1 
ATOM   3398 C CD    . ARG A 1 447 ? 31.37969 -45.58481 -10.08605 1.000 17.41386 ? 447  ARG A CD    1 
ATOM   3399 N NE    . ARG A 1 447 ? 31.75800 -44.37845 -9.35398  1.000 17.87753 ? 447  ARG A NE    1 
ATOM   3400 C CZ    . ARG A 1 447 ? 31.19086 -43.18756 -9.49875  1.000 18.82956 ? 447  ARG A CZ    1 
ATOM   3401 N NH1   . ARG A 1 447 ? 30.19071 -42.99381 -10.34266 1.000 15.63846 ? 447  ARG A NH1   1 
ATOM   3402 N NH2   . ARG A 1 447 ? 31.65299 -42.15938 -8.79221  1.000 16.71784 ? 447  ARG A NH2   1 
ATOM   3403 N N     . PHE A 1 448 ? 25.99272 -45.43083 -8.02469  1.000 14.85574 ? 448  PHE A N     1 
ATOM   3404 C CA    . PHE A 1 448 ? 24.84388 -44.53469 -7.94652  1.000 14.78491 ? 448  PHE A CA    1 
ATOM   3405 C C     . PHE A 1 448 ? 25.29893 -43.26881 -7.23523  1.000 12.47878 ? 448  PHE A C     1 
ATOM   3406 O O     . PHE A 1 448 ? 25.49241 -43.27485 -6.01561  1.000 13.86653 ? 448  PHE A O     1 
ATOM   3407 C CB    . PHE A 1 448 ? 23.67446 -45.18981 -7.21259  1.000 13.90183 ? 448  PHE A CB    1 
ATOM   3408 C CG    . PHE A 1 448 ? 22.39239 -44.41098 -7.29652  1.000 16.27307 ? 448  PHE A CG    1 
ATOM   3409 C CD1   . PHE A 1 448 ? 21.51081 -44.61779 -8.34511  1.000 16.46850 ? 448  PHE A CD1   1 
ATOM   3410 C CD2   . PHE A 1 448 ? 22.06384 -43.47935 -6.32381  1.000 14.96529 ? 448  PHE A CD2   1 
ATOM   3411 C CE1   . PHE A 1 448 ? 20.32662 -43.90537 -8.42645  1.000 18.92092 ? 448  PHE A CE1   1 
ATOM   3412 C CE2   . PHE A 1 448 ? 20.88265 -42.76453 -6.39972  1.000 16.88210 ? 448  PHE A CE2   1 
ATOM   3413 C CZ    . PHE A 1 448 ? 20.01277 -42.97824 -7.45064  1.000 16.04836 ? 448  PHE A CZ    1 
ATOM   3414 N N     . ALA A 1 449 ? 25.47472 -42.19116 -7.99255  1.000 13.18035 ? 449  ALA A N     1 
ATOM   3415 C CA    . ALA A 1 449 ? 25.99533 -40.93674 -7.46957  1.000 14.40139 ? 449  ALA A CA    1 
ATOM   3416 C C     . ALA A 1 449 ? 24.88467 -39.89732 -7.41785  1.000 14.50261 ? 449  ALA A C     1 
ATOM   3417 O O     . ALA A 1 449 ? 24.16986 -39.69529 -8.40216  1.000 14.49304 ? 449  ALA A O     1 
ATOM   3418 C CB    . ALA A 1 449 ? 27.15685 -40.42877 -8.32454  1.000 13.89003 ? 449  ALA A CB    1 
ATOM   3419 N N     . ILE A 1 450 ? 24.74081 -39.24672 -6.26841  1.000 13.63636 ? 450  ILE A N     1 
ATOM   3420 C CA    . ILE A 1 450 ? 23.81347 -38.12852 -6.11619  1.000 14.56601 ? 450  ILE A CA    1 
ATOM   3421 C C     . ILE A 1 450 ? 24.45814 -36.89689 -6.74419  1.000 12.96356 ? 450  ILE A C     1 
ATOM   3422 O O     . ILE A 1 450 ? 25.52895 -36.45759 -6.31179  1.000 15.43765 ? 450  ILE A O     1 
ATOM   3423 C CB    . ILE A 1 450 ? 23.47841 -37.88437 -4.63678  1.000 14.91791 ? 450  ILE A CB    1 
ATOM   3424 C CG1   . ILE A 1 450 ? 22.91368 -39.14964 -3.98653  1.000 14.74510 ? 450  ILE A CG1   1 
ATOM   3425 C CG2   . ILE A 1 450 ? 22.47762 -36.76093 -4.50069  1.000 14.39784 ? 450  ILE A CG2   1 
ATOM   3426 C CD1   . ILE A 1 450 ? 21.68695 -39.70302 -4.67344  1.000 14.56541 ? 450  ILE A CD1   1 
ATOM   3427 N N     . CYS A 1 451 ? 23.80862 -36.32995 -7.76426  1.000 13.86423 ? 451  CYS A N     1 
ATOM   3428 C CA    . CYS A 1 451 ? 24.44827 -35.30654 -8.58867  1.000 12.40341 ? 451  CYS A CA    1 
ATOM   3429 C C     . CYS A 1 451 ? 23.68049 -33.99133 -8.62657  1.000 12.46129 ? 451  CYS A C     1 
ATOM   3430 O O     . CYS A 1 451 ? 24.24922 -32.94721 -8.29023  1.000 14.31565 ? 451  CYS A O     1 
ATOM   3431 C CB    . CYS A 1 451 ? 24.65419 -35.84116 -10.01268 1.000 12.51254 ? 451  CYS A CB    1 
ATOM   3432 S SG    . CYS A 1 451 ? 25.83016 -37.20889 -10.13725 1.000 14.09085 ? 451  CYS A SG    1 
ATOM   3433 N N     . SER A 1 452 ? 22.41491 -34.00097 -9.03632  1.000 12.78617 ? 452  SER A N     1 
ATOM   3434 C CA    . SER A 1 452 ? 21.73378 -32.75944 -9.37798  1.000 13.42093 ? 452  SER A CA    1 
ATOM   3435 C C     . SER A 1 452 ? 21.45246 -31.91526 -8.14174  1.000 13.72651 ? 452  SER A C     1 
ATOM   3436 O O     . SER A 1 452 ? 21.14017 -32.43509 -7.06736  1.000 13.39709 ? 452  SER A O     1 
ATOM   3437 C CB    . SER A 1 452 ? 20.42724 -33.05596 -10.11121 1.000 14.64448 ? 452  SER A CB    1 
ATOM   3438 O OG    . SER A 1 452 ? 19.68200 -31.86782 -10.32032 1.000 15.86602 ? 452  SER A OG    1 
ATOM   3439 N N     . ARG A 1 453 ? 21.56379 -30.59396 -8.30686  1.000 11.89046 ? 453  ARG A N     1 
ATOM   3440 C CA    . ARG A 1 453 ? 21.24017 -29.67300 -7.22111  1.000 12.63780 ? 453  ARG A CA    1 
ATOM   3441 C C     . ARG A 1 453 ? 19.80197 -29.83687 -6.75250  1.000 15.47448 ? 453  ARG A C     1 
ATOM   3442 O O     . ARG A 1 453 ? 19.50228 -29.61080 -5.57381  1.000 14.61776 ? 453  ARG A O     1 
ATOM   3443 C CB    . ARG A 1 453 ? 21.48345 -28.23165 -7.66948  1.000 15.34958 ? 453  ARG A CB    1 
ATOM   3444 C CG    . ARG A 1 453 ? 21.19630 -27.18840 -6.60182  1.000 15.35108 ? 453  ARG A CG    1 
ATOM   3445 C CD    . ARG A 1 453 ? 21.62471 -25.80366 -7.05645  1.000 18.55593 ? 453  ARG A CD    1 
ATOM   3446 N NE    . ARG A 1 453 ? 20.97678 -25.41299 -8.30235  1.000 19.45035 ? 453  ARG A NE    1 
ATOM   3447 C CZ    . ARG A 1 453 ? 19.72181 -24.99669 -8.40313  1.000 20.05300 ? 453  ARG A CZ    1 
ATOM   3448 N NH1   . ARG A 1 453 ? 18.94579 -24.87252 -7.33861  1.000 22.45610 ? 453  ARG A NH1   1 
ATOM   3449 N NH2   . ARG A 1 453 ? 19.23395 -24.69354 -9.60271  1.000 21.71171 ? 453  ARG A NH2   1 
ATOM   3450 N N     . THR A 1 454 ? 18.90342 -30.24347 -7.65066  1.000 13.60275 ? 454  THR A N     1 
ATOM   3451 C CA    . THR A 1 454 ? 17.47501 -30.28725 -7.36684  1.000 14.82414 ? 454  THR A CA    1 
ATOM   3452 C C     . THR A 1 454 ? 16.93872 -31.70720 -7.20326  1.000 16.74147 ? 454  THR A C     1 
ATOM   3453 O O     . THR A 1 454 ? 15.72181 -31.90979 -7.26748  1.000 17.46705 ? 454  THR A O     1 
ATOM   3454 C CB    . THR A 1 454 ? 16.70020 -29.56071 -8.46691  1.000 16.58018 ? 454  THR A CB    1 
ATOM   3455 O OG1   . THR A 1 454 ? 16.81610 -30.28655 -9.69761  1.000 17.43237 ? 454  THR A OG1   1 
ATOM   3456 C CG2   . THR A 1 454 ? 17.23338 -28.14778 -8.65737  1.000 16.66443 ? 454  THR A CG2   1 
ATOM   3457 N N     . VAL A 1 455 ? 17.81099 -32.69554 -6.98845  1.000 15.27496 ? 455  VAL A N     1 
ATOM   3458 C CA    . VAL A 1 455 ? 17.33851 -34.06369 -6.80673  1.000 15.66152 ? 455  VAL A CA    1 
ATOM   3459 C C     . VAL A 1 455 ? 16.62685 -34.18408 -5.46256  1.000 16.99643 ? 455  VAL A C     1 
ATOM   3460 O O     . VAL A 1 455 ? 17.00531 -33.53866 -4.47524  1.000 16.20598 ? 455  VAL A O     1 
ATOM   3461 C CB    . VAL A 1 455 ? 18.50605 -35.06069 -6.93096  1.000 15.36124 ? 455  VAL A CB    1 
ATOM   3462 C CG1   . VAL A 1 455 ? 19.54973 -34.82419 -5.85055  1.000 16.15288 ? 455  VAL A CG1   1 
ATOM   3463 C CG2   . VAL A 1 455 ? 17.99629 -36.49929 -6.88718  1.000 17.15734 ? 455  VAL A CG2   1 
ATOM   3464 N N     . GLU A 1 456 ? 15.57256 -34.99903 -5.42265  1.000 14.93963 ? 456  GLU A N     1 
ATOM   3465 C CA    . GLU A 1 456 ? 14.74873 -35.17751 -4.23599  1.000 17.01329 ? 456  GLU A CA    1 
ATOM   3466 C C     . GLU A 1 456 ? 14.58068 -36.66731 -3.96398  1.000 15.69872 ? 456  GLU A C     1 
ATOM   3467 O O     . GLU A 1 456 ? 14.99549 -37.51623 -4.75715  1.000 16.74312 ? 456  GLU A O     1 
ATOM   3468 C CB    . GLU A 1 456 ? 13.37415 -34.51167 -4.40292  1.000 17.28728 ? 456  GLU A CB    1 
ATOM   3469 C CG    . GLU A 1 456 ? 13.42666 -33.01261 -4.68622  1.000 21.10334 ? 456  GLU A CG    1 
ATOM   3470 C CD    . GLU A 1 456 ? 13.80634 -32.18054 -3.47245  1.000 24.66942 ? 456  GLU A CD    1 
ATOM   3471 O OE1   . GLU A 1 456 ? 14.06730 -30.96918 -3.64860  1.000 33.69209 ? 456  GLU A OE1   1 
ATOM   3472 O OE2   . GLU A 1 456 ? 13.83934 -32.71872 -2.34929  1.000 27.37891 ? 456  GLU A OE2   1 
ATOM   3473 N N     . SER A 1 457 ? 13.94965 -36.98201 -2.82910  1.000 16.48767 ? 457  SER A N     1 
ATOM   3474 C CA    . SER A 1 457 ? 13.74078 -38.38129 -2.46507  1.000 14.59410 ? 457  SER A CA    1 
ATOM   3475 C C     . SER A 1 457 ? 12.91653 -39.11087 -3.51732  1.000 15.79986 ? 457  SER A C     1 
ATOM   3476 O O     . SER A 1 457 ? 13.15442 -40.29259 -3.79359  1.000 15.39089 ? 457  SER A O     1 
ATOM   3477 C CB    . SER A 1 457 ? 13.06320 -38.47643 -1.09747  1.000 17.43922 ? 457  SER A CB    1 
ATOM   3478 O OG    . SER A 1 457 ? 13.91666 -38.01247 -0.06652  1.000 21.24995 ? 457  SER A OG    1 
ATOM   3479 N N     . ALA A 1 458 ? 11.94698 -38.41946 -4.12089  1.000 17.10305 ? 458  ALA A N     1 
ATOM   3480 C CA    . ALA A 1 458 ? 11.09509 -39.05299 -5.12241  1.000 18.96371 ? 458  ALA A CA    1 
ATOM   3481 C C     . ALA A 1 458 ? 11.90354 -39.52095 -6.32757  1.000 16.37992 ? 458  ALA A C     1 
ATOM   3482 O O     . ALA A 1 458 ? 11.62930 -40.58728 -6.89090  1.000 16.03120 ? 458  ALA A O     1 
ATOM   3483 C CB    . ALA A 1 458 ? 9.99267  -38.08740 -5.55540  1.000 23.00313 ? 458  ALA A CB    1 
ATOM   3484 N N     . HIS A 1 459 ? 12.90683 -38.73912 -6.73637  1.000 16.13145 ? 459  HIS A N     1 
ATOM   3485 C CA    . HIS A 1 459 ? 13.74212 -39.13503 -7.86721  1.000 17.24946 ? 459  HIS A CA    1 
ATOM   3486 C C     . HIS A 1 459 ? 14.55495 -40.38182 -7.54554  1.000 17.77400 ? 459  HIS A C     1 
ATOM   3487 O O     . HIS A 1 459 ? 14.66952 -41.28885 -8.37939  1.000 15.59878 ? 459  HIS A O     1 
ATOM   3488 C CB    . HIS A 1 459 ? 14.66994 -37.98786 -8.26440  1.000 17.00176 ? 459  HIS A CB    1 
ATOM   3489 C CG    . HIS A 1 459 ? 13.95402 -36.71088 -8.57075  1.000 17.19827 ? 459  HIS A CG    1 
ATOM   3490 N ND1   . HIS A 1 459 ? 14.17840 -35.54589 -7.87050  1.000 18.84556 ? 459  HIS A ND1   1 
ATOM   3491 C CD2   . HIS A 1 459 ? 13.02211 -36.41376 -9.50650  1.000 21.98688 ? 459  HIS A CD2   1 
ATOM   3492 C CE1   . HIS A 1 459 ? 13.41257 -34.58656 -8.35823  1.000 21.64972 ? 459  HIS A CE1   1 
ATOM   3493 N NE2   . HIS A 1 459 ? 12.70098 -35.08716 -9.35176  1.000 19.25274 ? 459  HIS A NE2   1 
ATOM   3494 N N     . VAL A 1 460 ? 15.13501 -40.43777 -6.34435  1.000 15.20247 ? 460  VAL A N     1 
ATOM   3495 C CA    . VAL A 1 460 ? 15.93362 -41.59497 -5.95049  1.000 15.51003 ? 460  VAL A CA    1 
ATOM   3496 C C     . VAL A 1 460 ? 15.05622 -42.83545 -5.85558  1.000 16.23476 ? 460  VAL A C     1 
ATOM   3497 O O     . VAL A 1 460 ? 15.44727 -43.92905 -6.28302  1.000 16.23163 ? 460  VAL A O     1 
ATOM   3498 C CB    . VAL A 1 460 ? 16.65943 -41.30487 -4.62320  1.000 14.53177 ? 460  VAL A CB    1 
ATOM   3499 C CG1   . VAL A 1 460 ? 17.33805 -42.55769 -4.09456  1.000 14.53538 ? 460  VAL A CG1   1 
ATOM   3500 C CG2   . VAL A 1 460 ? 17.66376 -40.17324 -4.80414  1.000 14.24158 ? 460  VAL A CG2   1 
ATOM   3501 N N     . GLN A 1 461 ? 13.84936 -42.68065 -5.30721  1.000 15.57558 ? 461  GLN A N     1 
ATOM   3502 C CA    . GLN A 1 461 ? 12.93450 -43.81009 -5.18299  1.000 16.21529 ? 461  GLN A CA    1 
ATOM   3503 C C     . GLN A 1 461 ? 12.49200 -44.31568 -6.55020  1.000 17.63348 ? 461  GLN A C     1 
ATOM   3504 O O     . GLN A 1 461 ? 12.36203 -45.52833 -6.75906  1.000 19.06019 ? 461  GLN A O     1 
ATOM   3505 C CB    . GLN A 1 461 ? 11.72545 -43.40321 -4.34306  1.000 17.71705 ? 461  GLN A CB    1 
ATOM   3506 C CG    . GLN A 1 461 ? 12.04711 -43.17947 -2.87509  1.000 16.32014 ? 461  GLN A CG    1 
ATOM   3507 C CD    . GLN A 1 461 ? 10.93995 -42.45081 -2.14134  1.000 19.06404 ? 461  GLN A CD    1 
ATOM   3508 O OE1   . GLN A 1 461 ? 9.87346  -42.19559 -2.70082  1.000 21.12758 ? 461  GLN A OE1   1 
ATOM   3509 N NE2   . GLN A 1 461 ? 11.19311 -42.09734 -0.88640  1.000 18.40490 ? 461  GLN A NE2   1 
ATOM   3510 N N     . ARG A 1 462 ? 12.25123 -43.40085 -7.49162  1.000 17.27661 ? 462  ARG A N     1 
ATOM   3511 C CA    . ARG A 1 462 ? 11.88694 -43.81032 -8.84395  1.000 18.06858 ? 462  ARG A CA    1 
ATOM   3512 C C     . ARG A 1 462 ? 13.03961 -44.53285 -9.52801  1.000 18.70879 ? 462  ARG A C     1 
ATOM   3513 O O     . ARG A 1 462 ? 12.82893 -45.53851 -10.21639 1.000 18.98952 ? 462  ARG A O     1 
ATOM   3514 C CB    . ARG A 1 462 ? 11.46834 -42.59309 -9.66490  1.000 21.81839 ? 462  ARG A CB    1 
ATOM   3515 C CG    . ARG A 1 462 ? 10.06826 -42.10029 -9.37575  1.000 23.53995 ? 462  ARG A CG    1 
ATOM   3516 C CD    . ARG A 1 462 ? 9.74154  -40.89371 -10.23210 1.000 28.06297 ? 462  ARG A CD    1 
ATOM   3517 N NE    . ARG A 1 462 ? 8.58631  -40.16700 -9.72073  1.000 36.63817 ? 462  ARG A NE    1 
ATOM   3518 C CZ    . ARG A 1 462 ? 8.56925  -38.86215 -9.48712  1.000 36.72261 ? 462  ARG A CZ    1 
ATOM   3519 N NH1   . ARG A 1 462 ? 9.63038  -38.10549 -9.71591  1.000 33.24742 ? 462  ARG A NH1   1 
ATOM   3520 N NH2   . ARG A 1 462 ? 7.46032  -38.30229 -9.01235  1.000 39.97905 ? 462  ARG A NH2   1 
ATOM   3521 N N     . ALA A 1 463 ? 14.26445 -44.02901 -9.35459  1.000 16.66677 ? 463  ALA A N     1 
ATOM   3522 C CA    . ALA A 1 463 ? 15.42464 -44.66436 -9.97053  1.000 18.77827 ? 463  ALA A CA    1 
ATOM   3523 C C     . ALA A 1 463 ? 15.60740 -46.08920 -9.46531  1.000 19.04410 ? 463  ALA A C     1 
ATOM   3524 O O     . ALA A 1 463 ? 15.90932 -46.99894 -10.24647 1.000 18.98850 ? 463  ALA A O     1 
ATOM   3525 C CB    . ALA A 1 463 ? 16.67918 -43.83516 -9.70139  1.000 16.44616 ? 463  ALA A CB    1 
ATOM   3526 N N     . TRP A 1 464 ? 15.42590 -46.30474 -8.16048  1.000 19.34990 ? 464  TRP A N     1 
ATOM   3527 C CA    . TRP A 1 464 ? 15.57980 -47.64885 -7.61481  1.000 17.94746 ? 464  TRP A CA    1 
ATOM   3528 C C     . TRP A 1 464 ? 14.51722 -48.59404 -8.15968  1.000 20.95506 ? 464  TRP A C     1 
ATOM   3529 O O     . TRP A 1 464 ? 14.81615 -49.74859 -8.48721  1.000 20.61624 ? 464  TRP A O     1 
ATOM   3530 C CB    . TRP A 1 464 ? 15.52883 -47.61517 -6.08909  1.000 17.86976 ? 464  TRP A CB    1 
ATOM   3531 C CG    . TRP A 1 464 ? 15.40923 -48.98154 -5.49638  1.000 16.82056 ? 464  TRP A CG    1 
ATOM   3532 C CD1   . TRP A 1 464 ? 14.35787 -49.47689 -4.78271  1.000 20.58643 ? 464  TRP A CD1   1 
ATOM   3533 C CD2   . TRP A 1 464 ? 16.36308 -50.04602 -5.59847  1.000 20.68907 ? 464  TRP A CD2   1 
ATOM   3534 N NE1   . TRP A 1 464 ? 14.60536 -50.77864 -4.41754  1.000 22.59496 ? 464  TRP A NE1   1 
ATOM   3535 C CE2   . TRP A 1 464 ? 15.82968 -51.15183 -4.90749  1.000 19.88852 ? 464  TRP A CE2   1 
ATOM   3536 C CE3   . TRP A 1 464 ? 17.61951 -50.16824 -6.20039  1.000 21.16604 ? 464  TRP A CE3   1 
ATOM   3537 C CZ2   . TRP A 1 464 ? 16.50920 -52.36431 -4.80147  1.000 23.04773 ? 464  TRP A CZ2   1 
ATOM   3538 C CZ3   . TRP A 1 464 ? 18.29147 -51.37275 -6.09625  1.000 22.05426 ? 464  TRP A CZ3   1 
ATOM   3539 C CH2   . TRP A 1 464 ? 17.73626 -52.45379 -5.40112  1.000 23.79410 ? 464  TRP A CH2   1 
ATOM   3540 N N     . GLU A 1 465 ? 13.26992 -48.12671 -8.25420  1.000 19.21389 ? 465  GLU A N     1 
ATOM   3541 C CA    . GLU A 1 465 ? 12.21768 -48.94834 -8.84265  1.000 21.11907 ? 465  GLU A CA    1 
ATOM   3542 C C     . GLU A 1 465 ? 12.57619 -49.35448 -10.26556 1.000 24.29408 ? 465  GLU A C     1 
ATOM   3543 O O     . GLU A 1 465 ? 12.38085 -50.51051 -10.65930 1.000 22.42650 ? 465  GLU A O     1 
ATOM   3544 C CB    . GLU A 1 465 ? 10.88953 -48.19352 -8.81789  1.000 24.57579 ? 465  GLU A CB    1 
ATOM   3545 C CG    . GLU A 1 465 ? 9.73873  -48.95516 -9.44802  1.000 31.22086 ? 465  GLU A CG    1 
ATOM   3546 C CD    . GLU A 1 465 ? 8.53010  -48.07897 -9.70892  1.000 39.89430 ? 465  GLU A CD    1 
ATOM   3547 O OE1   . GLU A 1 465 ? 8.27387  -47.15432 -8.90936  1.000 44.15948 ? 465  GLU A OE1   1 
ATOM   3548 O OE2   . GLU A 1 465 ? 7.83362  -48.31890 -10.71760 1.000 46.21209 ? 465  GLU A OE2   1 
ATOM   3549 N N     . HIS A 1 466 ? 13.11276 -48.41326 -11.04426 1.000 20.59459 ? 466  HIS A N     1 
ATOM   3550 C CA    . HIS A 1 466 ? 13.58361 -48.71425 -12.39265 1.000 22.39314 ? 466  HIS A CA    1 
ATOM   3551 C C     . HIS A 1 466 ? 14.68559 -49.76703 -12.37264 1.000 24.15345 ? 466  HIS A C     1 
ATOM   3552 O O     . HIS A 1 466 ? 14.64185 -50.74400 -13.13009 1.000 23.62887 ? 466  HIS A O     1 
ATOM   3553 C CB    . HIS A 1 466 ? 14.07316 -47.42700 -13.05730 1.000 22.06444 ? 466  HIS A CB    1 
ATOM   3554 C CG    . HIS A 1 466 ? 14.43682 -47.58690 -14.49938 1.000 23.35591 ? 466  HIS A CG    1 
ATOM   3555 N ND1   . HIS A 1 466 ? 13.56164 -48.09023 -15.43720 1.000 24.60052 ? 466  HIS A ND1   1 
ATOM   3556 C CD2   . HIS A 1 466 ? 15.57665 -47.29179 -15.16789 1.000 22.76636 ? 466  HIS A CD2   1 
ATOM   3557 C CE1   . HIS A 1 466 ? 14.15122 -48.10941 -16.61943 1.000 27.08689 ? 466  HIS A CE1   1 
ATOM   3558 N NE2   . HIS A 1 466 ? 15.37381 -47.62807 -16.48386 1.000 25.40281 ? 466  HIS A NE2   1 
ATOM   3559 N N     . ILE A 1 467 ? 15.68557 -49.58167 -11.50761 1.000 20.23783 ? 467  ILE A N     1 
ATOM   3560 C CA    . ILE A 1 467 ? 16.79857 -50.52614 -11.43039 1.000 21.44063 ? 467  ILE A CA    1 
ATOM   3561 C C     . ILE A 1 467 ? 16.29848 -51.91131 -11.03995 1.000 24.74905 ? 467  ILE A C     1 
ATOM   3562 O O     . ILE A 1 467 ? 16.72665 -52.92678 -11.60348 1.000 23.55578 ? 467  ILE A O     1 
ATOM   3563 C CB    . ILE A 1 467 ? 17.86445 -50.00945 -10.44473 1.000 19.60744 ? 467  ILE A CB    1 
ATOM   3564 C CG1   . ILE A 1 467 ? 18.52840 -48.74125 -10.98906 1.000 19.28942 ? 467  ILE A CG1   1 
ATOM   3565 C CG2   . ILE A 1 467 ? 18.90428 -51.08440 -10.15923 1.000 21.84374 ? 467  ILE A CG2   1 
ATOM   3566 C CD1   . ILE A 1 467 ? 19.30853 -47.96758 -9.94790  1.000 17.09007 ? 467  ILE A CD1   1 
ATOM   3567 N N     . LYS A 1 468 ? 15.37445 -51.97318 -10.07925 1.000 20.63370 ? 468  LYS A N     1 
ATOM   3568 C CA    . LYS A 1 468 ? 14.86707 -53.25946 -9.61350  1.000 24.43071 ? 468  LYS A CA    1 
ATOM   3569 C C     . LYS A 1 468 ? 14.09999 -53.98728 -10.71175 1.000 23.40162 ? 468  LYS A C     1 
ATOM   3570 O O     . LYS A 1 468 ? 14.19380 -55.21445 -10.83381 1.000 26.12969 ? 468  LYS A O     1 
ATOM   3571 C CB    . LYS A 1 468 ? 13.98042 -53.05207 -8.38737  1.000 25.02880 ? 468  LYS A CB    1 
ATOM   3572 C CG    . LYS A 1 468 ? 14.25414 -54.02626 -7.26027  1.000 32.85801 ? 468  LYS A CG    1 
ATOM   3573 C CD    . LYS A 1 468 ? 12.97807 -54.37822 -6.51858  1.000 33.76965 ? 468  LYS A CD    1 
ATOM   3574 C CE    . LYS A 1 468 ? 12.23923 -53.13225 -6.06180  1.000 34.19696 ? 468  LYS A CE    1 
ATOM   3575 N NZ    . LYS A 1 468 ? 11.33857 -53.43284 -4.91169  1.000 33.01313 ? 468  LYS A NZ    1 
ATOM   3576 N N     . GLU A 1 469 ? 13.33640 -53.24747 -11.52099 1.000 22.45879 ? 469  GLU A N     1 
ATOM   3577 C CA    . GLU A 1 469 ? 12.57469 -53.86803 -12.60080 1.000 27.13217 ? 469  GLU A CA    1 
ATOM   3578 C C     . GLU A 1 469 ? 13.49360 -54.43427 -13.67414 1.000 28.70907 ? 469  GLU A C     1 
ATOM   3579 O O     . GLU A 1 469 ? 13.27616 -55.55041 -14.16101 1.000 28.16841 ? 469  GLU A O     1 
ATOM   3580 C CB    . GLU A 1 469 ? 11.61075 -52.85318 -13.21144 1.000 31.70372 ? 469  GLU A CB    1 
ATOM   3581 C CG    . GLU A 1 469 ? 10.51932 -52.39476 -12.26653 1.000 36.40611 ? 469  GLU A CG    1 
ATOM   3582 C CD    . GLU A 1 469 ? 9.28234  -51.89675 -12.98704 1.000 48.86536 ? 469  GLU A CD    1 
ATOM   3583 O OE1   . GLU A 1 469 ? 8.19764  -51.89719 -12.36601 1.000 49.37681 ? 469  GLU A OE1   1 
ATOM   3584 O OE2   . GLU A 1 469 ? 9.39249  -51.49691 -14.16637 1.000 53.11713 ? 469  GLU A OE2   1 
ATOM   3585 N N     . LEU A 1 470 ? 14.51985 -53.67679 -14.06236 1.000 26.49557 ? 470  LEU A N     1 
ATOM   3586 C CA    . LEU A 1 470 ? 15.44528 -54.16302 -15.07749 1.000 27.76370 ? 470  LEU A CA    1 
ATOM   3587 C C     . LEU A 1 470 ? 16.28111 -55.32672 -14.56176 1.000 30.08513 ? 470  LEU A C     1 
ATOM   3588 O O     . LEU A 1 470 ? 16.65818 -56.20830 -15.34204 1.000 29.88330 ? 470  LEU A O     1 
ATOM   3589 C CB    . LEU A 1 470 ? 16.34004 -53.02004 -15.55343 1.000 27.14072 ? 470  LEU A CB    1 
ATOM   3590 C CG    . LEU A 1 470 ? 15.61097 -51.91917 -16.32584 1.000 28.74720 ? 470  LEU A CG    1 
ATOM   3591 C CD1   . LEU A 1 470 ? 16.60961 -50.99638 -16.98425 1.000 25.95678 ? 470  LEU A CD1   1 
ATOM   3592 C CD2   . LEU A 1 470 ? 14.67331 -52.51590 -17.36739 1.000 33.42997 ? 470  LEU A CD2   1 
ATOM   3593 N N     . ALA A 1 471 ? 16.57164 -55.35301 -13.25806 1.000 26.06824 ? 471  ALA A N     1 
ATOM   3594 C CA    . ALA A 1 471 ? 17.30019 -56.48061 -12.68575 1.000 26.64198 ? 471  ALA A CA    1 
ATOM   3595 C C     . ALA A 1 471 ? 16.49678 -57.76885 -12.80304 1.000 32.43187 ? 471  ALA A C     1 
ATOM   3596 O O     . ALA A 1 471 ? 17.06073 -58.84263 -13.04446 1.000 31.76913 ? 471  ALA A O     1 
ATOM   3597 C CB    . ALA A 1 471 ? 17.64617 -56.19647 -11.22458 1.000 25.22701 ? 471  ALA A CB    1 
ATOM   3598 N N     . ALA A 1 472 ? 15.17619 -57.68149 -12.62875 1.000 30.21731 ? 472  ALA A N     1 
ATOM   3599 C CA    . ALA A 1 472 ? 14.32384 -58.85337 -12.79856 1.000 33.67787 ? 472  ALA A CA    1 
ATOM   3600 C C     . ALA A 1 472 ? 14.40513 -59.37841 -14.22621 1.000 35.96463 ? 472  ALA A C     1 
ATOM   3601 O O     . ALA A 1 472 ? 14.50886 -60.59142 -14.45155 1.000 39.05738 ? 472  ALA A O     1 
ATOM   3602 C CB    . ALA A 1 472 ? 12.88080 -58.50801 -12.42760 1.000 30.64875 ? 472  ALA A CB    1 
ATOM   3603 N N     . ASP A 1 473 ? 14.36369 -58.46906 -15.20615 1.000 33.05594 ? 473  ASP A N     1 
ATOM   3604 C CA    . ASP A 1 473 ? 14.51889 -58.86034 -16.60556 1.000 39.16296 ? 473  ASP A CA    1 
ATOM   3605 C C     . ASP A 1 473 ? 15.85776 -59.55126 -16.83441 1.000 40.82720 ? 473  ASP A C     1 
ATOM   3606 O O     . ASP A 1 473 ? 15.92805 -60.61209 -17.46706 1.000 43.79208 ? 473  ASP A O     1 
ATOM   3607 C CB    . ASP A 1 473 ? 14.40580 -57.63028 -17.51235 1.000 41.36068 ? 473  ASP A CB    1 
ATOM   3608 C CG    . ASP A 1 473 ? 13.04567 -56.96518 -17.44249 1.000 44.15801 ? 473  ASP A CG    1 
ATOM   3609 O OD1   . ASP A 1 473 ? 12.15780 -57.48552 -16.73761 1.000 44.68121 ? 473  ASP A OD1   1 
ATOM   3610 O OD2   . ASP A 1 473 ? 12.87365 -55.90595 -18.08568 1.000 46.03488 ? 473  ASP A OD2   1 
ATOM   3611 N N     . VAL A 1 474 ? 16.93531 -58.95844 -16.31813 1.000 35.82115 ? 474  VAL A N     1 
ATOM   3612 C CA    . VAL A 1 474 ? 18.27453 -59.45431 -16.61422 1.000 37.83048 ? 474  VAL A CA    1 
ATOM   3613 C C     . VAL A 1 474 ? 18.52136 -60.78310 -15.90791 1.000 41.55764 ? 474  VAL A C     1 
ATOM   3614 O O     . VAL A 1 474 ? 19.12585 -61.70063 -16.47777 1.000 42.59796 ? 474  VAL A O     1 
ATOM   3615 C CB    . VAL A 1 474 ? 19.32284 -58.38979 -16.23673 1.000 34.41203 ? 474  VAL A CB    1 
ATOM   3616 C CG1   . VAL A 1 474 ? 20.67104 -59.02748 -15.96727 1.000 38.43021 ? 474  VAL A CG1   1 
ATOM   3617 C CG2   . VAL A 1 474 ? 19.43204 -57.33961 -17.33533 1.000 33.01343 ? 474  VAL A CG2   1 
ATOM   3618 N N     . LEU A 1 475 ? 18.04303 -60.91613 -14.66689 1.000 38.78353 ? 475  LEU A N     1 
ATOM   3619 C CA    . LEU A 1 475 ? 18.17586 -62.18011 -13.94681 1.000 39.37930 ? 475  LEU A CA    1 
ATOM   3620 C C     . LEU A 1 475 ? 17.38757 -63.28401 -14.64083 1.000 52.41547 ? 475  LEU A C     1 
ATOM   3621 O O     . LEU A 1 475 ? 17.86823 -64.41589 -14.77903 1.000 53.69420 ? 475  LEU A O     1 
ATOM   3622 C CB    . LEU A 1 475 ? 17.70875 -62.00826 -12.50030 1.000 37.92486 ? 475  LEU A CB    1 
ATOM   3623 C CG    . LEU A 1 475 ? 18.67031 -61.28317 -11.55646 1.000 36.87798 ? 475  LEU A CG    1 
ATOM   3624 C CD1   . LEU A 1 475 ? 17.99433 -61.00229 -10.22558 1.000 35.52688 ? 475  LEU A CD1   1 
ATOM   3625 C CD2   . LEU A 1 475 ? 19.94631 -62.08908 -11.35756 1.000 32.07115 ? 475  LEU A CD2   1 
ATOM   3626 N N     . ARG A 1 476 ? 16.16072 -62.96915 -15.06590 1.000 51.01890 ? 476  ARG A N     1 
ATOM   3627 C CA    . ARG A 1 476 ? 15.39238 -63.86329 -15.92532 1.000 57.18270 ? 476  ARG A CA    1 
ATOM   3628 C C     . ARG A 1 476 ? 16.21646 -64.34549 -17.11216 1.000 60.39124 ? 476  ARG A C     1 
ATOM   3629 O O     . ARG A 1 476 ? 16.29393 -65.54820 -17.38492 1.000 65.51150 ? 476  ARG A O     1 
ATOM   3630 C CB    . ARG A 1 476 ? 14.13652 -63.13599 -16.41150 1.000 57.77757 ? 476  ARG A CB    1 
ATOM   3631 C CG    . ARG A 1 476 ? 13.21569 -63.96132 -17.28189 1.000 66.38265 ? 476  ARG A CG    1 
ATOM   3632 C CD    . ARG A 1 476 ? 11.95932 -63.17814 -17.61986 1.000 69.18930 ? 476  ARG A CD    1 
ATOM   3633 N NE    . ARG A 1 476 ? 11.10010 -63.88447 -18.56304 1.000 77.60311 ? 476  ARG A NE    1 
ATOM   3634 C CZ    . ARG A 1 476 ? 10.17186 -64.76607 -18.21851 1.000 80.15782 ? 476  ARG A CZ    1 
ATOM   3635 N NH1   . ARG A 1 476 ? 9.94967  -65.07828 -16.95044 1.000 80.28234 ? 476  ARG A NH1   1 
ATOM   3636 N NH2   . ARG A 1 476 ? 9.44657  -65.34824 -19.16901 1.000 79.09379 ? 476  ARG A NH2   1 
ATOM   3637 N N     . ALA A 1 477 ? 16.85347 -63.41349 -17.82313 1.000 56.47511 ? 477  ALA A N     1 
ATOM   3638 C CA    . ALA A 1 477 ? 17.53005 -63.75666 -19.06723 1.000 58.30418 ? 477  ALA A CA    1 
ATOM   3639 C C     . ALA A 1 477 ? 18.77543 -64.60639 -18.85045 1.000 62.67762 ? 477  ALA A C     1 
ATOM   3640 O O     . ALA A 1 477 ? 19.22726 -65.26772 -19.79215 1.000 68.05084 ? 477  ALA A O     1 
ATOM   3641 C CB    . ALA A 1 477 ? 17.89652 -62.48476 -19.83343 1.000 49.23994 ? 477  ALA A CB    1 
ATOM   3642 N N     . GLU A 1 478 ? 19.34141 -64.60997 -17.64243 1.000 60.91901 ? 478  GLU A N     1 
ATOM   3643 C CA    . GLU A 1 478 ? 20.53982 -65.40304 -17.39623 1.000 65.54747 ? 478  GLU A CA    1 
ATOM   3644 C C     . GLU A 1 478 ? 20.23526 -66.86798 -17.11059 1.000 68.36741 ? 478  GLU A C     1 
ATOM   3645 O O     . GLU A 1 478 ? 21.11606 -67.71517 -17.30007 1.000 72.81429 ? 478  GLU A O     1 
ATOM   3646 C CB    . GLU A 1 478 ? 21.35034 -64.81245 -16.24004 1.000 62.41245 ? 478  GLU A CB    1 
ATOM   3647 C CG    . GLU A 1 478 ? 22.85416 -64.97145 -16.42905 1.000 64.20889 ? 478  GLU A CG    1 
ATOM   3648 C CD    . GLU A 1 478 ? 23.62754 -64.89678 -15.12956 1.000 63.96215 ? 478  GLU A CD    1 
ATOM   3649 O OE1   . GLU A 1 478 ? 22.99101 -64.87372 -14.05508 1.000 68.65152 ? 478  GLU A OE1   1 
ATOM   3650 O OE2   . GLU A 1 478 ? 24.87502 -64.86843 -15.18456 1.000 57.26834 ? 478  GLU A OE2   1 
ATOM   3651 N N     . ARG A 1 479 ? 19.02066 -67.18936 -16.66111 1.000 68.41764 ? 479  ARG A N     1 
ATOM   3652 C CA    . ARG A 1 479 ? 18.60650 -68.57891 -16.49248 1.000 72.68300 ? 479  ARG A CA    1 
ATOM   3653 C C     . ARG A 1 479 ? 17.83779 -69.11081 -17.69418 1.000 76.26464 ? 479  ARG A C     1 
ATOM   3654 O O     . ARG A 1 479 ? 18.01265 -70.27445 -18.06762 1.000 76.54646 ? 479  ARG A O     1 
ATOM   3655 C CB    . ARG A 1 479 ? 17.75842 -68.74844 -15.22700 1.000 71.56483 ? 479  ARG A CB    1 
ATOM   3656 C CG    . ARG A 1 479 ? 16.67390 -67.69666 -15.02318 1.000 72.02662 ? 479  ARG A CG    1 
ATOM   3657 C CD    . ARG A 1 479 ? 15.98662 -67.88623 -13.67527 1.000 76.65542 ? 479  ARG A CD    1 
ATOM   3658 N NE    . ARG A 1 479 ? 14.82524 -67.02009 -13.50555 1.000 79.21153 ? 479  ARG A NE    1 
ATOM   3659 C CZ    . ARG A 1 479 ? 14.78060 -65.98111 -12.68248 1.000 77.19043 ? 479  ARG A CZ    1 
ATOM   3660 N NH1   . ARG A 1 479 ? 15.81929 -65.64733 -11.93446 1.000 73.52246 ? 479  ARG A NH1   1 
ATOM   3661 N NH2   . ARG A 1 479 ? 13.66360 -65.26320 -12.60226 1.000 75.78116 ? 479  ARG A NH2   1 
ATOM   3662 N N     . GLU A 1 480 ? 16.99942 -68.28718 -18.31714 1.000 76.57431 ? 480  GLU A N     1 
ATOM   3663 C CA    . GLU A 1 480 ? 16.31705 -68.68846 -19.54182 1.000 76.46622 ? 480  GLU A CA    1 
ATOM   3664 C C     . GLU A 1 480 ? 17.21314 -68.45139 -20.75393 1.000 78.07239 ? 480  GLU A C     1 
ATOM   3665 O O     . GLU A 1 480 ? 18.42288 -68.26459 -20.61540 1.000 77.26947 ? 480  GLU A O     1 
ATOM   3666 C CB    . GLU A 1 480 ? 14.99373 -67.93603 -19.70290 1.000 74.89691 ? 480  GLU A CB    1 
ATOM   3667 C CG    . GLU A 1 480 ? 15.07683 -66.71597 -20.60835 1.000 77.17616 ? 480  GLU A CG    1 
ATOM   3668 C CD    . GLU A 1 480 ? 13.72983 -66.05705 -20.83457 1.000 82.22486 ? 480  GLU A CD    1 
ATOM   3669 O OE1   . GLU A 1 480 ? 13.43378 -65.69150 -21.99126 1.000 88.27118 ? 480  GLU A OE1   1 
ATOM   3670 O OE2   . GLU A 1 480 ? 12.96163 -65.91869 -19.85936 1.000 80.88544 ? 480  GLU A OE2   1 
HETATM 3671 O O1    . PG4 B 2 .   ? 10.47749 -51.09881 -4.20212  1.000 28.40599 ? 601  PG4 A O1    1 
HETATM 3672 C C1    . PG4 B 2 .   ? 10.84856 -50.54566 -2.93665  1.000 28.97609 ? 601  PG4 A C1    1 
HETATM 3673 C C2    . PG4 B 2 .   ? 11.53828 -51.61828 -2.08867  1.000 28.64244 ? 601  PG4 A C2    1 
HETATM 3674 O O2    . PG4 B 2 .   ? 12.70634 -52.07607 -2.77698  1.000 31.07912 ? 601  PG4 A O2    1 
HETATM 3675 C C3    . PG4 B 2 .   ? 13.54947 -52.81610 -1.88970  1.000 26.95150 ? 601  PG4 A C3    1 
HETATM 3676 C C4    . PG4 B 2 .   ? 12.94578 -54.18836 -1.58738  1.000 30.75893 ? 601  PG4 A C4    1 
HETATM 3677 O O3    . PG4 B 2 .   ? 12.81006 -54.93332 -2.80122  1.000 30.65207 ? 601  PG4 A O3    1 
HETATM 3678 C C5    . PG4 B 2 .   ? 12.48820 -56.29078 -2.48157  1.000 28.98055 ? 601  PG4 A C5    1 
HETATM 3679 C C6    . PG4 B 2 .   ? 12.21108 -57.08744 -3.76075  1.000 33.97572 ? 601  PG4 A C6    1 
HETATM 3680 O O4    . PG4 B 2 .   ? 11.11206 -56.50383 -4.46724  1.000 35.63819 ? 601  PG4 A O4    1 
HETATM 3681 C C7    . PG4 B 2 .   ? 10.65124 -57.42030 -5.46274  1.000 35.28460 ? 601  PG4 A C7    1 
HETATM 3682 C C8    . PG4 B 2 .   ? 9.50280  -56.78689 -6.24840  1.000 34.60374 ? 601  PG4 A C8    1 
HETATM 3683 O O5    . PG4 B 2 .   ? 9.96528  -55.59407 -6.88561  1.000 37.59472 ? 601  PG4 A O5    1 
HETATM 3684 O O1    . PG4 C 2 .   ? 65.80267 -49.25946 -11.19132 1.000 35.74602 ? 602  PG4 A O1    1 
HETATM 3685 C C1    . PG4 C 2 .   ? 65.31793 -48.47431 -12.28523 1.000 42.54308 ? 602  PG4 A C1    1 
HETATM 3686 C C2    . PG4 C 2 .   ? 66.29942 -48.63760 -13.44197 1.000 40.06211 ? 602  PG4 A C2    1 
HETATM 3687 O O2    . PG4 C 2 .   ? 65.90367 -47.89816 -14.60054 1.000 48.39067 ? 602  PG4 A O2    1 
HETATM 3688 C C3    . PG4 C 2 .   ? 67.02681 -47.95600 -15.48321 1.000 46.65430 ? 602  PG4 A C3    1 
HETATM 3689 C C4    . PG4 C 2 .   ? 68.16535 -47.14921 -14.85433 1.000 44.86050 ? 602  PG4 A C4    1 
HETATM 3690 O O3    . PG4 C 2 .   ? 69.31296 -47.19061 -15.70343 1.000 52.32831 ? 602  PG4 A O3    1 
HETATM 3691 C C5    . PG4 C 2 .   ? 70.38685 -47.82177 -15.00721 1.000 50.86074 ? 602  PG4 A C5    1 
HETATM 3692 C C6    . PG4 C 2 .   ? 71.02134 -46.83477 -14.03157 1.000 51.27585 ? 602  PG4 A C6    1 
HETATM 3693 O O4    . PG4 C 2 .   ? 72.07076 -47.50429 -13.32887 1.000 58.01748 ? 602  PG4 A O4    1 
HETATM 3694 C C7    . PG4 C 2 .   ? 71.79386 -47.48652 -11.92319 1.000 55.83359 ? 602  PG4 A C7    1 
HETATM 3695 C C8    . PG4 C 2 .   ? 71.08070 -48.77124 -11.50159 1.000 54.77634 ? 602  PG4 A C8    1 
HETATM 3696 O O5    . PG4 C 2 .   ? 70.82711 -48.68641 -10.10046 1.000 57.36278 ? 602  PG4 A O5    1 
HETATM 3697 O O     . HOH D 3 .   ? 40.73231 -35.23473 -14.84219 1.000 41.45016 ? 701  HOH A O     1 
HETATM 3698 O O     . HOH D 3 .   ? 16.92401 -21.88988 -36.71713 1.000 33.32753 ? 702  HOH A O     1 
HETATM 3699 O O     . HOH D 3 .   ? 36.28988 -34.88890 -13.95248 1.000 33.81942 ? 703  HOH A O     1 
HETATM 3700 O O     . HOH D 3 .   ? 20.56060 -9.29029  -32.05692 1.000 31.84785 ? 704  HOH A O     1 
HETATM 3701 O O     . HOH D 3 .   ? 38.00140 -15.60863 11.43306  1.000 44.07356 ? 705  HOH A O     1 
HETATM 3702 O O     . HOH D 3 .   ? 43.67139 -24.36210 -17.27985 1.000 36.35100 ? 706  HOH A O     1 
HETATM 3703 O O     . HOH D 3 .   ? 10.35017 -36.23433 -12.56891 1.000 33.24430 ? 707  HOH A O     1 
HETATM 3704 O O     . HOH D 3 .   ? 9.78322  -50.76407 -6.50558  1.000 33.08402 ? 708  HOH A O     1 
HETATM 3705 O O     . HOH D 3 .   ? 39.206   -5.830    -17.497   1.000 22.98712 ? 709  HOH A O     1 
HETATM 3706 O O     . HOH D 3 .   ? 44.71972 -24.72542 -14.37634 1.000 25.23941 ? 710  HOH A O     1 
HETATM 3707 O O     . HOH D 3 .   ? 32.65352 -20.82848 -15.42237 1.000 20.08246 ? 711  HOH A O     1 
HETATM 3708 O O     . HOH D 3 .   ? 27.24764 -60.34358 -0.69587  1.000 39.15079 ? 712  HOH A O     1 
HETATM 3709 O O     . HOH D 3 .   ? 59.61867 -26.85051 -6.20785  1.000 30.32775 ? 713  HOH A O     1 
HETATM 3710 O O     . HOH D 3 .   ? 41.62618 -22.92019 9.46055   1.000 27.02676 ? 714  HOH A O     1 
HETATM 3711 O O     . HOH D 3 .   ? 48.23244 -12.35843 0.04348   1.000 47.27683 ? 715  HOH A O     1 
HETATM 3712 O O     . HOH D 3 .   ? 34.10982 -35.30188 12.08432  1.000 23.39798 ? 716  HOH A O     1 
HETATM 3713 O O     . HOH D 3 .   ? 24.50302 -30.49156 -7.23466  1.000 12.38654 ? 717  HOH A O     1 
HETATM 3714 O O     . HOH D 3 .   ? 40.48856 -32.08536 -15.87090 1.000 21.57997 ? 718  HOH A O     1 
HETATM 3715 O O     . HOH D 3 .   ? 39.38730 -49.94281 -9.33108  1.000 34.70726 ? 719  HOH A O     1 
HETATM 3716 O O     . HOH D 3 .   ? 13.77728 -42.31271 -0.00409  1.000 24.33832 ? 720  HOH A O     1 
HETATM 3717 O O     . HOH D 3 .   ? 18.892   -55.438   5.137     1.000 30.34750 ? 721  HOH A O     1 
HETATM 3718 O O     . HOH D 3 .   ? 76.705   -34.394   -0.391    1.000 32.05662 ? 722  HOH A O     1 
HETATM 3719 O O     . HOH D 3 .   ? 34.30837 -17.13227 -13.85770 1.000 23.71999 ? 723  HOH A O     1 
HETATM 3720 O O     . HOH D 3 .   ? 42.35697 -45.90518 -2.38476  1.000 14.84815 ? 724  HOH A O     1 
HETATM 3721 O O     . HOH D 3 .   ? 46.66216 -11.62224 -3.13967  1.000 33.34259 ? 725  HOH A O     1 
HETATM 3722 O O     . HOH D 3 .   ? 31.17642 -45.49253 -1.01143  1.000 23.38537 ? 726  HOH A O     1 
HETATM 3723 O O     . HOH D 3 .   ? 44.41243 -20.03291 1.78142   1.000 26.51721 ? 727  HOH A O     1 
HETATM 3724 O O     . HOH D 3 .   ? 15.44393 -35.14801 -16.80880 1.000 28.06998 ? 728  HOH A O     1 
HETATM 3725 O O     . HOH D 3 .   ? 61.25701 -42.29816 -13.59691 1.000 22.92472 ? 729  HOH A O     1 
HETATM 3726 O O     . HOH D 3 .   ? 22.42466 -23.94790 -38.08933 1.000 25.27520 ? 730  HOH A O     1 
HETATM 3727 O O     . HOH D 3 .   ? 12.19274 -13.19278 -22.33906 1.000 31.43378 ? 731  HOH A O     1 
HETATM 3728 O O     . HOH D 3 .   ? 39.56242 -24.34263 -17.30320 1.000 30.62204 ? 732  HOH A O     1 
HETATM 3729 O O     . HOH D 3 .   ? 62.31649 -42.49245 0.04559   1.000 24.81041 ? 733  HOH A O     1 
HETATM 3730 O O     . HOH D 3 .   ? 70.24525 -27.98220 -9.16836  1.000 39.74452 ? 734  HOH A O     1 
HETATM 3731 O O     . HOH D 3 .   ? 62.924   -44.286   5.653     1.000 30.59328 ? 735  HOH A O     1 
HETATM 3732 O O     . HOH D 3 .   ? 13.82397 -34.80206 -0.78711  1.000 29.18557 ? 736  HOH A O     1 
HETATM 3733 O O     . HOH D 3 .   ? 28.01781 -40.31090 -19.90095 1.000 27.21578 ? 737  HOH A O     1 
HETATM 3734 O O     . HOH D 3 .   ? 47.00285 -25.24285 -13.72578 1.000 25.30031 ? 738  HOH A O     1 
HETATM 3735 O O     . HOH D 3 .   ? 20.78547 -25.27673 -11.61804 1.000 25.17449 ? 739  HOH A O     1 
HETATM 3736 O O     . HOH D 3 .   ? 26.17015 -40.78115 -36.83791 1.000 30.86244 ? 740  HOH A O     1 
HETATM 3737 O O     . HOH D 3 .   ? 45.42718 -10.10880 -11.33687 1.000 22.21129 ? 741  HOH A O     1 
HETATM 3738 O O     . HOH D 3 .   ? 16.68877 -24.56231 -10.97349 1.000 21.62782 ? 742  HOH A O     1 
HETATM 3739 O O     . HOH D 3 .   ? 10.27842 -19.05276 -12.84075 1.000 30.60810 ? 743  HOH A O     1 
HETATM 3740 O O     . HOH D 3 .   ? 27.46108 -40.61303 5.97643   1.000 22.40952 ? 744  HOH A O     1 
HETATM 3741 O O     . HOH D 3 .   ? 8.24135  -44.22686 -3.00718  1.000 25.35851 ? 745  HOH A O     1 
HETATM 3742 O O     . HOH D 3 .   ? 14.42393 -25.25534 -23.06506 1.000 35.54180 ? 746  HOH A O     1 
HETATM 3743 O O     . HOH D 3 .   ? 27.31289 -48.62910 4.11144   1.000 23.35319 ? 747  HOH A O     1 
HETATM 3744 O O     . HOH D 3 .   ? 28.77489 -20.44051 -15.15747 1.000 29.87338 ? 748  HOH A O     1 
HETATM 3745 O O     . HOH D 3 .   ? 43.49843 -32.37788 10.55231  1.000 24.31768 ? 749  HOH A O     1 
HETATM 3746 O O     . HOH D 3 .   ? 62.52525 -39.14091 -1.26846  1.000 27.87021 ? 750  HOH A O     1 
HETATM 3747 O O     . HOH D 3 .   ? 56.23510 -34.98453 2.88241   1.000 18.45455 ? 751  HOH A O     1 
HETATM 3748 O O     . HOH D 3 .   ? 44.66453 -36.65498 -9.08765  1.000 15.56503 ? 752  HOH A O     1 
HETATM 3749 O O     . HOH D 3 .   ? 52.59543 -44.21984 9.79051   1.000 32.46047 ? 753  HOH A O     1 
HETATM 3750 O O     . HOH D 3 .   ? 44.35288 -8.33189  -0.22973  1.000 22.12106 ? 754  HOH A O     1 
HETATM 3751 O O     . HOH D 3 .   ? 55.32198 -28.68485 2.65759   1.000 31.96084 ? 755  HOH A O     1 
HETATM 3752 O O     . HOH D 3 .   ? 52.74661 -22.28442 -19.49498 1.000 32.47322 ? 756  HOH A O     1 
HETATM 3753 O O     . HOH D 3 .   ? 18.12154 -33.87247 -24.84772 1.000 20.56533 ? 757  HOH A O     1 
HETATM 3754 O O     . HOH D 3 .   ? 37.18302 -37.07752 -3.77819  1.000 14.54850 ? 758  HOH A O     1 
HETATM 3755 O O     . HOH D 3 .   ? 24.07504 -25.50274 -15.34875 1.000 23.12207 ? 759  HOH A O     1 
HETATM 3756 O O     . HOH D 3 .   ? 45.62241 -42.44377 -3.98162  1.000 14.26523 ? 760  HOH A O     1 
HETATM 3757 O O     . HOH D 3 .   ? 14.66580 -29.38348 -27.29670 1.000 33.15224 ? 761  HOH A O     1 
HETATM 3758 O O     . HOH D 3 .   ? 26.85695 -36.15333 -4.03888  1.000 12.18977 ? 762  HOH A O     1 
HETATM 3759 O O     . HOH D 3 .   ? 46.64066 -50.41828 1.36166   1.000 18.03126 ? 763  HOH A O     1 
HETATM 3760 O O     . HOH D 3 .   ? 11.65869 -31.79303 -8.31651  1.000 40.97787 ? 764  HOH A O     1 
HETATM 3761 O O     . HOH D 3 .   ? 60.36194 -35.65335 -2.86444  1.000 31.37637 ? 765  HOH A O     1 
HETATM 3762 O O     . HOH D 3 .   ? 39.44060 -55.62939 -1.87815  1.000 34.85958 ? 766  HOH A O     1 
HETATM 3763 O O     . HOH D 3 .   ? 43.45140 -20.18159 -17.05252 1.000 25.32600 ? 767  HOH A O     1 
HETATM 3764 O O     . HOH D 3 .   ? 19.38631 -36.15841 -23.80870 1.000 21.69729 ? 768  HOH A O     1 
HETATM 3765 O O     . HOH D 3 .   ? 11.36416 -29.94952 -14.43424 1.000 24.76152 ? 769  HOH A O     1 
HETATM 3766 O O     . HOH D 3 .   ? 31.88134 -18.58414 -45.35831 1.000 19.90059 ? 770  HOH A O     1 
HETATM 3767 O O     . HOH D 3 .   ? 64.298   -56.730   2.804     1.000 21.74292 ? 771  HOH A O     1 
HETATM 3768 O O     . HOH D 3 .   ? 40.51436 -49.24588 5.80542   1.000 22.62335 ? 772  HOH A O     1 
HETATM 3769 O O     . HOH D 3 .   ? 29.81666 -43.02864 -0.30577  1.000 16.41205 ? 773  HOH A O     1 
HETATM 3770 O O     . HOH D 3 .   ? 32.991   -27.895   -42.616   1.000 25.57103 ? 774  HOH A O     1 
HETATM 3771 O O     . HOH D 3 .   ? 33.62279 -31.38707 -4.39237  1.000 14.88827 ? 775  HOH A O     1 
HETATM 3772 O O     . HOH D 3 .   ? 21.07206 -36.65312 -9.49723  1.000 14.86390 ? 776  HOH A O     1 
HETATM 3773 O O     . HOH D 3 .   ? 30.16770 -27.25890 -13.23752 1.000 18.40516 ? 777  HOH A O     1 
HETATM 3774 O O     . HOH D 3 .   ? 25.88344 -38.46751 -39.22369 1.000 22.17820 ? 778  HOH A O     1 
HETATM 3775 O O     . HOH D 3 .   ? 63.40058 -54.78765 -5.26587  1.000 25.41096 ? 779  HOH A O     1 
HETATM 3776 O O     . HOH D 3 .   ? 41.17622 -44.80754 5.64690   1.000 23.13383 ? 780  HOH A O     1 
HETATM 3777 O O     . HOH D 3 .   ? 26.89130 -26.35502 -46.03540 1.000 31.40300 ? 781  HOH A O     1 
HETATM 3778 O O     . HOH D 3 .   ? 40.26110 -14.83875 -9.47280  1.000 16.84236 ? 782  HOH A O     1 
HETATM 3779 O O     . HOH D 3 .   ? 58.72466 -55.37845 -0.28979  1.000 29.27988 ? 783  HOH A O     1 
HETATM 3780 O O     . HOH D 3 .   ? 11.533   -31.185   -33.086   1.000 26.59768 ? 784  HOH A O     1 
HETATM 3781 O O     . HOH D 3 .   ? 53.09178 -23.00916 5.97758   1.000 36.33032 ? 785  HOH A O     1 
HETATM 3782 O O     . HOH D 3 .   ? 12.66355 -9.20086  -25.29362 1.000 32.57787 ? 786  HOH A O     1 
HETATM 3783 O O     . HOH D 3 .   ? 25.11559 -35.33054 7.71704   1.000 28.92390 ? 787  HOH A O     1 
HETATM 3784 O O     . HOH D 3 .   ? 27.57947 -23.67600 10.43479  1.000 23.41512 ? 788  HOH A O     1 
HETATM 3785 O O     . HOH D 3 .   ? 35.21281 -28.06172 8.69544   1.000 27.28377 ? 789  HOH A O     1 
HETATM 3786 O O     . HOH D 3 .   ? 54.53224 -42.76954 -15.99032 1.000 29.20086 ? 790  HOH A O     1 
HETATM 3787 O O     . HOH D 3 .   ? 14.43948 -30.47815 -10.97075 1.000 27.53566 ? 791  HOH A O     1 
HETATM 3788 O O     . HOH D 3 .   ? 21.94287 -36.39550 -37.59891 1.000 14.01379 ? 792  HOH A O     1 
HETATM 3789 O O     . HOH D 3 .   ? 13.53944 -30.40378 -6.73082  1.000 32.03544 ? 793  HOH A O     1 
HETATM 3790 O O     . HOH D 3 .   ? 32.49228 -24.93633 7.81135   1.000 23.49374 ? 794  HOH A O     1 
HETATM 3791 O O     . HOH D 3 .   ? 17.17975 -45.78875 -17.63621 1.000 18.96617 ? 795  HOH A O     1 
HETATM 3792 O O     . HOH D 3 .   ? 13.59415 -62.62486 -11.97874 1.000 48.24653 ? 796  HOH A O     1 
HETATM 3793 O O     . HOH D 3 .   ? 18.45197 -37.43810 -28.00690 1.000 19.65502 ? 797  HOH A O     1 
HETATM 3794 O O     . HOH D 3 .   ? 22.91457 -42.44595 -27.82760 1.000 27.67511 ? 798  HOH A O     1 
HETATM 3795 O O     . HOH D 3 .   ? 35.34115 -47.88648 5.26927   1.000 37.92664 ? 799  HOH A O     1 
HETATM 3796 O O     . HOH D 3 .   ? 14.21289 -28.16490 -20.04529 1.000 20.54344 ? 800  HOH A O     1 
HETATM 3797 O O     . HOH D 3 .   ? 23.20665 -15.34392 -42.61526 1.000 27.24243 ? 801  HOH A O     1 
HETATM 3798 O O     . HOH D 3 .   ? 22.04500 -30.18570 -17.66088 1.000 14.64860 ? 802  HOH A O     1 
HETATM 3799 O O     . HOH D 3 .   ? 41.16925 -17.59663 -11.50817 1.000 17.97091 ? 803  HOH A O     1 
HETATM 3800 O O     . HOH D 3 .   ? 44.31121 -35.11084 12.58851  1.000 31.09258 ? 804  HOH A O     1 
HETATM 3801 O O     . HOH D 3 .   ? 67.70698 -46.57674 -3.07113  1.000 26.61343 ? 805  HOH A O     1 
HETATM 3802 O O     . HOH D 3 .   ? 21.32586 -55.77292 -0.46529  1.000 23.01525 ? 806  HOH A O     1 
HETATM 3803 O O     . HOH D 3 .   ? 46.22118 -42.81833 -12.33778 1.000 19.66627 ? 807  HOH A O     1 
HETATM 3804 O O     . HOH D 3 .   ? 11.551   -53.780   1.459     1.000 23.82287 ? 808  HOH A O     1 
HETATM 3805 O O     . HOH D 3 .   ? 17.72536 -2.09579  -24.97973 1.000 39.92055 ? 809  HOH A O     1 
HETATM 3806 O O     . HOH D 3 .   ? 18.30328 -29.16344 -11.79326 1.000 17.61558 ? 810  HOH A O     1 
HETATM 3807 O O     . HOH D 3 .   ? 14.894   -31.436   -32.250   1.000 26.25128 ? 811  HOH A O     1 
HETATM 3808 O O     . HOH D 3 .   ? 21.46298 -61.69280 -7.74322  1.000 27.05180 ? 812  HOH A O     1 
HETATM 3809 O O     . HOH D 3 .   ? 28.823   -10.177   -41.643   1.000 28.77055 ? 813  HOH A O     1 
HETATM 3810 O O     . HOH D 3 .   ? 14.97842 -15.17406 -37.81776 1.000 36.93490 ? 814  HOH A O     1 
HETATM 3811 O O     . HOH D 3 .   ? 27.24371 -43.65858 -11.54152 1.000 16.29690 ? 815  HOH A O     1 
HETATM 3812 O O     . HOH D 3 .   ? 14.99797 -44.89389 1.10388   1.000 22.38583 ? 816  HOH A O     1 
HETATM 3813 O O     . HOH D 3 .   ? 39.35921 -41.35644 -16.52690 1.000 41.06961 ? 817  HOH A O     1 
HETATM 3814 O O     . HOH D 3 .   ? 25.33744 -15.08335 -44.80751 1.000 32.03342 ? 818  HOH A O     1 
HETATM 3815 O O     . HOH D 3 .   ? 28.86073 -45.06307 6.87468   1.000 33.18370 ? 819  HOH A O     1 
HETATM 3816 O O     . HOH D 3 .   ? 22.00509 -23.46957 -11.41904 1.000 28.92133 ? 820  HOH A O     1 
HETATM 3817 O O     . HOH D 3 .   ? 20.04968 -24.51578 -4.16993  1.000 20.91812 ? 821  HOH A O     1 
HETATM 3818 O O     . HOH D 3 .   ? 29.25351 -47.63174 -1.66777  1.000 19.08299 ? 822  HOH A O     1 
HETATM 3819 O O     . HOH D 3 .   ? 29.45787 -7.40625  -29.15316 1.000 17.21098 ? 823  HOH A O     1 
HETATM 3820 O O     . HOH D 3 .   ? 13.35036 -37.20943 -17.49138 1.000 35.83102 ? 824  HOH A O     1 
HETATM 3821 O O     . HOH D 3 .   ? 40.97440 -19.06415 -16.20318 1.000 21.30113 ? 825  HOH A O     1 
HETATM 3822 O O     . HOH D 3 .   ? 53.32283 -51.03757 -5.63781  1.000 23.61521 ? 826  HOH A O     1 
HETATM 3823 O O     . HOH D 3 .   ? 46.08691 -48.09279 -1.93368  1.000 16.75583 ? 827  HOH A O     1 
HETATM 3824 O O     . HOH D 3 .   ? 44.32273 -33.10624 -7.08409  1.000 12.26104 ? 828  HOH A O     1 
HETATM 3825 O O     . HOH D 3 .   ? 17.61821 -3.59943  -29.22889 1.000 40.75451 ? 829  HOH A O     1 
HETATM 3826 O O     . HOH D 3 .   ? 31.72929 -63.25544 -13.29038 1.000 31.31159 ? 830  HOH A O     1 
HETATM 3827 O O     . HOH D 3 .   ? 57.89942 -46.92157 7.45418   1.000 41.51447 ? 831  HOH A O     1 
HETATM 3828 O O     . HOH D 3 .   ? 15.23819 -36.51527 2.21771   1.000 34.59617 ? 832  HOH A O     1 
HETATM 3829 O O     . HOH D 3 .   ? 42.92362 -39.93907 7.11633   1.000 28.83116 ? 833  HOH A O     1 
HETATM 3830 O O     . HOH D 3 .   ? 31.07432 -29.67336 -42.03155 1.000 21.66055 ? 834  HOH A O     1 
HETATM 3831 O O     . HOH D 3 .   ? 27.94236 -28.60404 -6.83867  1.000 12.12503 ? 835  HOH A O     1 
HETATM 3832 O O     . HOH D 3 .   ? 11.41762 -47.14528 -4.70194  1.000 21.83948 ? 836  HOH A O     1 
HETATM 3833 O O     . HOH D 3 .   ? 30.24567 -24.08842 -16.18870 1.000 24.68551 ? 837  HOH A O     1 
HETATM 3834 O O     . HOH D 3 .   ? 25.51660 -32.77289 -11.81354 1.000 15.60651 ? 838  HOH A O     1 
HETATM 3835 O O     . HOH D 3 .   ? 9.041    -27.698   -33.114   1.000 37.53399 ? 839  HOH A O     1 
HETATM 3836 O O     . HOH D 3 .   ? 16.39041 -27.17467 -12.23003 1.000 20.70114 ? 840  HOH A O     1 
HETATM 3837 O O     . HOH D 3 .   ? 54.90244 -56.94858 -2.73165  1.000 44.72073 ? 841  HOH A O     1 
HETATM 3838 O O     . HOH D 3 .   ? 25.60079 -55.88106 1.05901   1.000 24.91584 ? 842  HOH A O     1 
HETATM 3839 O O     . HOH D 3 .   ? 42.69927 -39.96705 -7.18742  1.000 14.01038 ? 843  HOH A O     1 
HETATM 3840 O O     . HOH D 3 .   ? 12.50486 -56.88016 -9.36317  1.000 33.18312 ? 844  HOH A O     1 
HETATM 3841 O O     . HOH D 3 .   ? 14.40126 -59.66768 -3.12226  1.000 33.02167 ? 845  HOH A O     1 
HETATM 3842 O O     . HOH D 3 .   ? 52.28516 -7.48459  -16.05173 1.000 31.44337 ? 846  HOH A O     1 
HETATM 3843 O O     . HOH D 3 .   ? 61.78314 -38.83721 -18.44495 1.000 37.03138 ? 847  HOH A O     1 
HETATM 3844 O O     . HOH D 3 .   ? 40.06050 -42.46383 -13.56495 1.000 23.19075 ? 848  HOH A O     1 
HETATM 3845 O O     . HOH D 3 .   ? 44.80099 -13.59689 -11.25723 1.000 26.69512 ? 849  HOH A O     1 
HETATM 3846 O O     . HOH D 3 .   ? 8.05384  -44.78323 -7.42411  1.000 36.50443 ? 850  HOH A O     1 
HETATM 3847 O O     . HOH D 3 .   ? 9.14443  -35.47737 -8.85860  1.000 41.33822 ? 851  HOH A O     1 
HETATM 3848 O O     . HOH D 3 .   ? 22.62858 -25.74094 7.64003   1.000 24.59828 ? 852  HOH A O     1 
HETATM 3849 O O     . HOH D 3 .   ? 60.43951 -32.73867 0.44138   1.000 34.43453 ? 853  HOH A O     1 
HETATM 3850 O O     . HOH D 3 .   ? 69.59609 -45.40937 -8.16692  1.000 36.01175 ? 854  HOH A O     1 
HETATM 3851 O O     . HOH D 3 .   ? 54.38156 -31.74680 4.98213   1.000 27.01512 ? 855  HOH A O     1 
HETATM 3852 O O     . HOH D 3 .   ? 23.26541 -35.95516 5.95683   1.000 22.30620 ? 856  HOH A O     1 
HETATM 3853 O O     . HOH D 3 .   ? 61.50215 -30.10410 -12.62391 1.000 22.63678 ? 857  HOH A O     1 
HETATM 3854 O O     . HOH D 3 .   ? 65.85824 -44.76327 -2.88216  1.000 25.39983 ? 858  HOH A O     1 
HETATM 3855 O O     . HOH D 3 .   ? 22.71008 -29.44626 -10.60762 1.000 14.80336 ? 859  HOH A O     1 
HETATM 3856 O O     . HOH D 3 .   ? 13.81716 -40.65625 -20.31131 1.000 33.73450 ? 860  HOH A O     1 
HETATM 3857 O O     . HOH D 3 .   ? 26.50828 -20.88779 -42.00085 1.000 19.19440 ? 861  HOH A O     1 
HETATM 3858 O O     . HOH D 3 .   ? 40.32842 -52.30758 -8.21775  1.000 32.80966 ? 862  HOH A O     1 
HETATM 3859 O O     . HOH D 3 .   ? 42.12228 -46.79654 7.13214   1.000 27.03438 ? 863  HOH A O     1 
HETATM 3860 O O     . HOH D 3 .   ? 25.05024 -28.83895 -9.25909  1.000 14.29426 ? 864  HOH A O     1 
HETATM 3861 O O     . HOH D 3 .   ? 60.11571 -52.53147 5.50236   1.000 38.99762 ? 865  HOH A O     1 
HETATM 3862 O O     . HOH D 3 .   ? 11.061   -49.567   0.990     1.000 21.55970 ? 866  HOH A O     1 
HETATM 3863 O O     . HOH D 3 .   ? 15.28271 -38.97649 -18.01117 1.000 21.91538 ? 867  HOH A O     1 
HETATM 3864 O O     . HOH D 3 .   ? 10.77295 -49.23214 -15.14328 1.000 38.25269 ? 868  HOH A O     1 
HETATM 3865 O O     . HOH D 3 .   ? 21.02656 -43.54699 -19.75175 1.000 25.09707 ? 869  HOH A O     1 
HETATM 3866 O O     . HOH D 3 .   ? 22.98141 -10.89068 -35.41428 1.000 39.56874 ? 870  HOH A O     1 
HETATM 3867 O O     . HOH D 3 .   ? 52.56255 -53.09607 -1.56302  1.000 22.59554 ? 871  HOH A O     1 
HETATM 3868 O O     . HOH D 3 .   ? 47.05917 -52.85218 7.19063   1.000 36.22385 ? 872  HOH A O     1 
HETATM 3869 O O     . HOH D 3 .   ? 26.36246 -17.03998 -16.71882 1.000 20.40916 ? 873  HOH A O     1 
HETATM 3870 O O     . HOH D 3 .   ? 19.84114 -30.49874 4.48093   1.000 21.91770 ? 874  HOH A O     1 
HETATM 3871 O O     . HOH D 3 .   ? 19.30547 -31.89537 -3.91239  1.000 18.50971 ? 875  HOH A O     1 
HETATM 3872 O O     . HOH D 3 .   ? 66.98023 -52.55617 -10.42316 1.000 36.56263 ? 876  HOH A O     1 
HETATM 3873 O O     . HOH D 3 .   ? 9.03253  -22.64887 -16.84472 1.000 36.67390 ? 877  HOH A O     1 
HETATM 3874 O O     . HOH D 3 .   ? 38.51571 -12.93602 -18.73998 1.000 35.34476 ? 878  HOH A O     1 
HETATM 3875 O O     . HOH D 3 .   ? 26.00649 -44.91895 -29.15923 1.000 39.93063 ? 879  HOH A O     1 
HETATM 3876 O O     . HOH D 3 .   ? 37.81458 -45.89514 2.97514   1.000 20.70303 ? 880  HOH A O     1 
HETATM 3877 O O     . HOH D 3 .   ? 33.94524 -50.56167 2.88957   1.000 31.27613 ? 881  HOH A O     1 
HETATM 3878 O O     . HOH D 3 .   ? 28.73668 -29.05746 -40.96546 1.000 18.40034 ? 882  HOH A O     1 
HETATM 3879 O O     . HOH D 3 .   ? 59.36398 -49.28792 3.98944   1.000 22.94440 ? 883  HOH A O     1 
HETATM 3880 O O     . HOH D 3 .   ? 35.68019 -32.03983 -12.07060 1.000 23.13630 ? 884  HOH A O     1 
HETATM 3881 O O     . HOH D 3 .   ? 33.88430 -45.64228 1.64931   1.000 26.17848 ? 885  HOH A O     1 
HETATM 3882 O O     . HOH D 3 .   ? 21.07971 -25.04596 0.38859   1.000 22.56501 ? 886  HOH A O     1 
HETATM 3883 O O     . HOH D 3 .   ? 47.11789 -34.65215 -14.51294 1.000 14.60432 ? 887  HOH A O     1 
HETATM 3884 O O     . HOH D 3 .   ? 12.32252 -20.57203 -23.64469 1.000 35.13434 ? 888  HOH A O     1 
HETATM 3885 O O     . HOH D 3 .   ? 16.33008 -51.32004 -21.49390 1.000 38.16661 ? 889  HOH A O     1 
HETATM 3886 O O     . HOH D 3 .   ? 63.14953 -29.20552 -16.54217 1.000 28.39701 ? 890  HOH A O     1 
HETATM 3887 O O     . HOH D 3 .   ? 52.78902 -46.84471 -14.62239 1.000 33.77773 ? 891  HOH A O     1 
HETATM 3888 O O     . HOH D 3 .   ? 48.33431 -12.93801 -10.71667 1.000 42.15889 ? 892  HOH A O     1 
HETATM 3889 O O     . HOH D 3 .   ? 39.32766 -44.50556 -11.43215 1.000 36.05975 ? 893  HOH A O     1 
HETATM 3890 O O     . HOH D 3 .   ? 35.290   -18.759   6.159     1.000 18.11411 ? 894  HOH A O     1 
HETATM 3891 O O     . HOH D 3 .   ? 24.965   -20.689   -39.688   1.000 18.20324 ? 895  HOH A O     1 
HETATM 3892 O O     . HOH D 3 .   ? 34.74766 -52.64097 1.04773   1.000 32.93417 ? 896  HOH A O     1 
HETATM 3893 O O     . HOH D 3 .   ? 22.40115 -28.35658 7.76891   1.000 22.89047 ? 897  HOH A O     1 
HETATM 3894 O O     . HOH D 3 .   ? 40.96220 -40.32526 5.91862   1.000 31.31961 ? 898  HOH A O     1 
HETATM 3895 O O     . HOH D 3 .   ? 37.77644 -35.15363 -15.64597 1.000 35.96312 ? 899  HOH A O     1 
HETATM 3896 O O     . HOH D 3 .   ? 38.89596 -20.53525 -17.26080 1.000 24.18643 ? 900  HOH A O     1 
HETATM 3897 O O     . HOH D 3 .   ? 11.53059 -21.21155 -9.60695  1.000 34.67106 ? 901  HOH A O     1 
HETATM 3898 O O     . HOH D 3 .   ? 30.81378 -16.58534 -18.05496 1.000 40.70334 ? 902  HOH A O     1 
HETATM 3899 O O     . HOH D 3 .   ? 25.22516 -64.89036 -11.94460 1.000 36.75211 ? 903  HOH A O     1 
HETATM 3900 O O     . HOH D 3 .   ? 12.31512 -36.34993 1.64083   1.000 31.54048 ? 904  HOH A O     1 
HETATM 3901 O O     . HOH D 3 .   ? 60.08152 -33.42169 -3.77490  1.000 27.35468 ? 905  HOH A O     1 
HETATM 3902 O O     . HOH D 3 .   ? 52.15700 -42.59536 -15.50261 1.000 28.81927 ? 906  HOH A O     1 
HETATM 3903 O O     . HOH D 3 .   ? 40.27622 -41.74813 -7.15914  1.000 16.82285 ? 907  HOH A O     1 
HETATM 3904 O O     . HOH D 3 .   ? 16.50871 -10.47058 -35.20958 1.000 36.83023 ? 908  HOH A O     1 
HETATM 3905 O O     . HOH D 3 .   ? 14.09381 -6.24368  -16.67308 1.000 36.68316 ? 909  HOH A O     1 
HETATM 3906 O O     . HOH D 3 .   ? 32.23619 -15.15038 -18.70057 1.000 33.29591 ? 910  HOH A O     1 
HETATM 3907 O O     . HOH D 3 .   ? 48.17619 -35.55024 13.95310  1.000 38.65632 ? 911  HOH A O     1 
HETATM 3908 O O     . HOH D 3 .   ? 60.28833 -34.16577 5.02215   1.000 37.30822 ? 912  HOH A O     1 
HETATM 3909 O O     . HOH D 3 .   ? 14.35549 -8.57710  -23.37260 1.000 25.69488 ? 913  HOH A O     1 
HETATM 3910 O O     . HOH D 3 .   ? 19.64519 -10.96210 -34.07789 1.000 25.61374 ? 914  HOH A O     1 
HETATM 3911 O O     . HOH D 3 .   ? 26.42330 -29.67982 -44.00571 1.000 32.93419 ? 915  HOH A O     1 
HETATM 3912 O O     . HOH D 3 .   ? 56.32944 -53.02881 -9.30322  1.000 34.87272 ? 916  HOH A O     1 
HETATM 3913 O O     . HOH D 3 .   ? 20.95628 -20.43796 2.12197   1.000 29.49175 ? 917  HOH A O     1 
HETATM 3914 O O     . HOH D 3 .   ? 52.00013 -50.38395 -10.20922 1.000 28.16427 ? 918  HOH A O     1 
HETATM 3915 O O     . HOH D 3 .   ? 53.06949 -53.26029 -4.18551  1.000 25.46911 ? 919  HOH A O     1 
HETATM 3916 O O     . HOH D 3 .   ? 33.36737 -46.38565 -16.00243 1.000 39.74160 ? 920  HOH A O     1 
HETATM 3917 O O     . HOH D 3 .   ? 46.51084 -26.85305 -18.23767 0.50  28.19574 ? 921  HOH A O     1 
HETATM 3918 O O     . HOH D 3 .   ? 37.13151 -55.84192 -0.58428  1.000 35.38767 ? 922  HOH A O     1 
HETATM 3919 O O     . HOH D 3 .   ? 51.05368 -43.35980 11.86895  1.000 39.58847 ? 923  HOH A O     1 
HETATM 3920 O O     . HOH D 3 .   ? 46.64696 -53.25648 -6.97236  1.000 36.97675 ? 924  HOH A O     1 
HETATM 3921 O O     . HOH D 3 .   ? 14.03438 -34.94175 -24.08629 1.000 28.75253 ? 925  HOH A O     1 
HETATM 3922 O O     . HOH D 3 .   ? 33.78628 -28.78732 10.17720  1.000 32.49836 ? 926  HOH A O     1 
HETATM 3923 O O     . HOH D 3 .   ? 32.34246 -10.08494 1.32489   1.000 16.95264 ? 927  HOH A O     1 
HETATM 3924 O O     . HOH D 3 .   ? 28.50700 -61.85285 -6.00859  1.000 37.17496 ? 928  HOH A O     1 
HETATM 3925 O O     . HOH D 3 .   ? 29.06828 -36.71166 -39.67362 1.000 32.50992 ? 929  HOH A O     1 
HETATM 3926 O O     . HOH D 3 .   ? 60.55071 -57.01188 5.15404   1.000 39.16824 ? 930  HOH A O     1 
HETATM 3927 O O     . HOH D 3 .   ? 40.69452 -39.55760 12.88402  1.000 35.28677 ? 931  HOH A O     1 
HETATM 3928 O O     . HOH D 3 .   ? 16.03657 -24.59320 -6.86516  1.000 30.37223 ? 932  HOH A O     1 
HETATM 3929 O O     . HOH D 3 .   ? 34.55517 -15.20850 -18.29905 1.000 24.45101 ? 933  HOH A O     1 
HETATM 3930 O O     . HOH D 3 .   ? 40.16687 -26.76207 -16.90285 1.000 24.61645 ? 934  HOH A O     1 
HETATM 3931 O O     . HOH D 3 .   ? 56.51172 -19.32680 0.71475   1.000 46.00688 ? 935  HOH A O     1 
HETATM 3932 O O     . HOH D 3 .   ? 44.59215 -10.82100 -1.22380  1.000 31.17869 ? 936  HOH A O     1 
HETATM 3933 O O     . HOH D 3 .   ? 34.09453 -55.39742 -1.47871  1.000 35.78371 ? 937  HOH A O     1 
HETATM 3934 O O     . HOH D 3 .   ? 52.08355 -7.20865  -11.31661 1.000 26.87513 ? 938  HOH A O     1 
HETATM 3935 O O     . HOH D 3 .   ? 52.44114 -9.53723  -10.72673 1.000 41.65313 ? 939  HOH A O     1 
HETATM 3936 O O     . HOH D 3 .   ? 58.85040 -46.54832 5.13523   1.000 33.90528 ? 940  HOH A O     1 
HETATM 3937 O O     . HOH D 3 .   ? 22.73566 -19.06640 -42.38600 1.000 36.98743 ? 941  HOH A O     1 
HETATM 3938 O O     . HOH D 3 .   ? 54.31167 -27.22045 0.32559   1.000 27.73522 ? 942  HOH A O     1 
HETATM 3939 O O     . HOH D 3 .   ? 30.65213 -60.72318 -3.19626  1.000 44.28301 ? 943  HOH A O     1 
HETATM 3940 O O     . HOH D 3 .   ? 41.44694 -55.01783 4.91844   1.000 33.53339 ? 944  HOH A O     1 
HETATM 3941 O O     . HOH D 3 .   ? 53.51469 -21.00561 7.17194   1.000 45.23129 ? 945  HOH A O     1 
HETATM 3942 O O     . HOH D 3 .   ? 64.34563 -28.91560 -12.75894 1.000 35.30587 ? 946  HOH A O     1 
HETATM 3943 O O     . HOH D 3 .   ? 23.46477 -32.05841 -44.93667 1.000 31.78587 ? 947  HOH A O     1 
HETATM 3944 O O     . HOH D 3 .   ? 29.77410 -25.57450 11.36965  1.000 34.14001 ? 948  HOH A O     1 
HETATM 3945 O O     . HOH D 3 .   ? 22.16295 -10.69953 -42.40183 1.000 31.04399 ? 949  HOH A O     1 
HETATM 3946 O O     . HOH D 3 .   ? 37.91338 -12.30999 -16.25363 1.000 26.43355 ? 950  HOH A O     1 
HETATM 3947 O O     . HOH D 3 .   ? 49.66813 -52.71849 -7.12452  1.000 34.75622 ? 951  HOH A O     1 
HETATM 3948 O O     . HOH D 3 .   ? 28.30011 -43.28478 -35.89713 1.000 36.18678 ? 952  HOH A O     1 
HETATM 3949 O O     . HOH D 3 .   ? 46.85060 -25.11240 12.50930  1.000 37.92243 ? 953  HOH A O     1 
HETATM 3950 O O     . HOH D 3 .   ? 49.46855 -40.04071 12.84472  1.000 30.37152 ? 954  HOH A O     1 
HETATM 3951 O O     . HOH D 3 .   ? 38.66130 -33.22788 12.91600  1.000 35.38567 ? 955  HOH A O     1 
HETATM 3952 O O     . HOH D 3 .   ? 33.36047 -42.49151 8.98470   1.000 38.09437 ? 956  HOH A O     1 
HETATM 3953 O O     . HOH D 3 .   ? 55.80624 -36.25499 10.36507  1.000 35.07503 ? 957  HOH A O     1 
HETATM 3954 O O     . HOH D 3 .   ? 19.34032 -16.15250 -39.54884 1.000 25.88917 ? 958  HOH A O     1 
HETATM 3955 O O     . HOH D 3 .   ? 37.32478 -48.94409 -12.59286 1.000 31.28757 ? 959  HOH A O     1 
HETATM 3956 O O     . HOH D 3 .   ? 54.70243 -53.86619 5.58373   1.000 40.76207 ? 960  HOH A O     1 
HETATM 3957 O O     . HOH D 3 .   ? 62.45368 -33.15462 -1.84682  1.000 30.64777 ? 961  HOH A O     1 
HETATM 3958 O O     . HOH D 3 .   ? 45.15853 -17.84870 0.00402   1.000 29.12439 ? 962  HOH A O     1 
HETATM 3959 O O     . HOH D 3 .   ? 65.23963 -28.97983 -10.50402 1.000 35.08784 ? 963  HOH A O     1 
HETATM 3960 O O     . HOH D 3 .   ? 27.02638 -27.93574 12.18395  1.000 31.63714 ? 964  HOH A O     1 
HETATM 3961 O O     . HOH D 3 .   ? 54.63998 -32.51248 8.45835   1.000 36.21464 ? 965  HOH A O     1 
HETATM 3962 O O     . HOH D 3 .   ? 21.87140 -39.59634 -34.39854 1.000 18.39184 ? 966  HOH A O     1 
HETATM 3963 O O     . HOH D 3 .   ? 49.42495 -25.57201 10.66551  1.000 28.96595 ? 967  HOH A O     1 
HETATM 3964 O O     . HOH D 3 .   ? 45.53277 -44.80238 -14.28494 1.000 36.54048 ? 968  HOH A O     1 
HETATM 3965 O O     . HOH D 3 .   ? 44.50984 -45.35301 11.52865  1.000 40.94937 ? 969  HOH A O     1 
HETATM 3966 O O     . HOH D 3 .   ? 17.47992 -28.54967 -3.53143  1.000 33.10744 ? 970  HOH A O     1 
HETATM 3967 O O     . HOH D 3 .   ? 54.99642 -45.22952 -15.20554 1.000 26.91517 ? 971  HOH A O     1 
HETATM 3968 O O     . HOH D 3 .   ? 27.81748 -0.67983  -27.00349 1.000 26.56810 ? 972  HOH A O     1 
HETATM 3969 O O     . HOH D 3 .   ? 43.34883 -22.74684 -15.56287 1.000 25.34770 ? 973  HOH A O     1 
HETATM 3970 O O     . HOH D 3 .   ? 10.61370 -24.35798 -33.02246 1.000 40.85873 ? 974  HOH A O     1 
HETATM 3971 O O     . HOH D 3 .   ? 48.70379 -50.47792 7.79168   1.000 27.79362 ? 975  HOH A O     1 
HETATM 3972 O O     . HOH D 3 .   ? 28.21250 -25.02596 -14.76586 1.000 26.73147 ? 976  HOH A O     1 
HETATM 3973 O O     . HOH D 3 .   ? 61.19086 -52.24754 -9.06644  1.000 37.39083 ? 977  HOH A O     1 
HETATM 3974 O O     . HOH D 3 .   ? 28.78263 -4.32327  -33.18671 1.000 30.40735 ? 978  HOH A O     1 
HETATM 3975 O O     . HOH D 3 .   ? 21.06345 -30.89400 -1.83183  1.000 18.29060 ? 979  HOH A O     1 
HETATM 3976 O O     . HOH D 3 .   ? 19.18512 -27.84069 -38.64907 1.000 35.25038 ? 980  HOH A O     1 
HETATM 3977 O O     . HOH D 3 .   ? 71.16940 -31.15394 -15.50931 1.000 41.67864 ? 981  HOH A O     1 
HETATM 3978 O O     . HOH D 3 .   ? 76.719   -37.491   -1.576    1.000 27.17278 ? 982  HOH A O     1 
HETATM 3979 O O     . HOH D 3 .   ? 30.91102 -63.06471 -15.66844 1.000 30.29768 ? 983  HOH A O     1 
HETATM 3980 O O     . HOH D 3 .   ? 34.35861 -60.06593 -16.11805 1.000 39.08539 ? 984  HOH A O     1 
HETATM 3981 O O     . HOH D 3 .   ? 14.22200 -23.11442 -22.57169 1.000 31.53299 ? 985  HOH A O     1 
HETATM 3982 O O     . HOH D 3 .   ? 15.93564 -32.78591 -24.84157 1.000 29.44478 ? 986  HOH A O     1 
HETATM 3983 O O     . HOH D 3 .   ? 40.01171 -40.53340 10.28678  1.000 35.94720 ? 987  HOH A O     1 
HETATM 3984 O O     . HOH D 3 .   ? 55.95998 -56.55814 -5.93132  1.000 37.27674 ? 988  HOH A O     1 
HETATM 3985 O O     . HOH D 3 .   ? 20.97229 -46.43185 5.01815   1.000 30.87461 ? 989  HOH A O     1 
HETATM 3986 O O     . HOH D 3 .   ? 19.90486 -28.58094 -2.66203  1.000 32.16200 ? 990  HOH A O     1 
HETATM 3987 O O     . HOH D 3 .   ? 29.62265 -39.11474 9.99628   1.000 38.50245 ? 991  HOH A O     1 
HETATM 3988 O O     . HOH D 3 .   ? 37.36824 -37.60119 -15.59733 1.000 36.21571 ? 992  HOH A O     1 
HETATM 3989 O O     . HOH D 3 .   ? 14.57936 -62.10769 -9.40761  1.000 35.99762 ? 993  HOH A O     1 
HETATM 3990 O O     . HOH D 3 .   ? 60.42874 -43.88691 -17.39659 1.000 38.41303 ? 994  HOH A O     1 
HETATM 3991 O O     . HOH D 3 .   ? 69.25341 -33.61521 -18.27304 1.000 39.81853 ? 995  HOH A O     1 
HETATM 3992 O O     . HOH D 3 .   ? 44.82206 -55.78951 -2.74129  1.000 39.07095 ? 996  HOH A O     1 
HETATM 3993 O O     . HOH D 3 .   ? 57.14387 -38.32340 10.32495  1.000 32.12567 ? 997  HOH A O     1 
HETATM 3994 O O     . HOH D 3 .   ? 26.58924 -47.92202 -20.86168 1.000 41.70246 ? 998  HOH A O     1 
HETATM 3995 O O     . HOH D 3 .   ? 74.91314 -28.51827 -7.08176  1.000 43.59823 ? 999  HOH A O     1 
HETATM 3996 O O     . HOH D 3 .   ? 13.54099 -18.72962 -31.50921 1.000 32.45200 ? 1000 HOH A O     1 
HETATM 3997 O O     . HOH D 3 .   ? 61.48701 -42.01787 -16.62006 1.000 39.37772 ? 1001 HOH A O     1 
HETATM 3998 O O     . HOH D 3 .   ? 24.08526 -25.86354 9.49985   1.000 31.79380 ? 1002 HOH A O     1 
HETATM 3999 O O     . HOH D 3 .   ? 28.22165 -20.34192 -45.57360 1.000 31.00300 ? 1003 HOH A O     1 
HETATM 4000 O O     . HOH D 3 .   ? 35.76240 -16.26639 -45.82209 1.000 33.97255 ? 1004 HOH A O     1 
HETATM 4001 O O     . HOH D 3 .   ? 26.29467 -16.36822 -46.25501 1.000 36.99994 ? 1005 HOH A O     1 
HETATM 4002 O O     . HOH D 3 .   ? 38.20037 -35.45125 14.55143  1.000 37.70371 ? 1006 HOH A O     1 
HETATM 4003 O O     . HOH D 3 .   ? 35.63956 -47.27850 2.34082   1.000 25.53212 ? 1007 HOH A O     1 
HETATM 4004 O O     . HOH D 3 .   ? 9.70257  -24.47131 -18.41747 1.000 35.34561 ? 1008 HOH A O     1 
HETATM 4005 O O     . HOH D 3 .   ? 58.22197 -31.93300 0.02161   1.000 31.51202 ? 1009 HOH A O     1 
HETATM 4006 O O     . HOH D 3 .   ? 30.36427 -13.81373 -19.56732 1.000 29.81985 ? 1010 HOH A O     1 
HETATM 4007 O O     . HOH D 3 .   ? 71.39434 -27.97741 -6.51525  1.000 39.57362 ? 1011 HOH A O     1 
HETATM 4008 O O     . HOH D 3 .   ? 25.24237 -43.68297 -26.95082 1.000 28.73227 ? 1012 HOH A O     1 
HETATM 4009 O O     . HOH D 3 .   ? 25.56939 -46.35383 6.22390   1.000 34.17241 ? 1013 HOH A O     1 
HETATM 4010 O O     . HOH D 3 .   ? 37.26057 -39.91899 -15.52353 1.000 40.35811 ? 1014 HOH A O     1 
HETATM 4011 O O     . HOH D 3 .   ? 28.11622 -52.95306 -19.56192 1.000 40.81943 ? 1015 HOH A O     1 
HETATM 4012 O O     . HOH D 3 .   ? 27.86125 -17.87676 -46.48877 1.000 35.79036 ? 1016 HOH A O     1 
HETATM 4013 O O     . HOH D 3 .   ? 9.87415  -52.17941 -9.14452  1.000 35.13231 ? 1017 HOH A O     1 
HETATM 4014 O O     . HOH D 3 .   ? 27.87932 -23.29554 -46.12612 1.000 33.48930 ? 1018 HOH A O     1 
HETATM 4015 O O     . HOH D 3 .   ? 20.59500 -27.71678 -10.95643 1.000 18.69277 ? 1019 HOH A O     1 
HETATM 4016 O O     . HOH D 3 .   ? 43.14220 -56.79069 -0.72794  1.000 40.34552 ? 1020 HOH A O     1 
HETATM 4017 O O     . HOH D 3 .   ? 33.18299 -26.62108 10.52705  1.000 35.39900 ? 1021 HOH A O     1 
HETATM 4018 O O     . HOH D 3 .   ? 28.10334 -16.22547 -18.23767 0.50  21.75683 ? 1022 HOH A O     1 
HETATM 4019 O O     . HOH D 3 .   ? 4.971    -48.453   -8.203    1.000 40.43035 ? 1023 HOH A O     1 
HETATM 4020 O O     . HOH D 3 .   ? 22.98106 -38.66844 6.34575   1.000 27.08432 ? 1024 HOH A O     1 
HETATM 4021 O O     . HOH D 3 .   ? 11.76153 -25.17853 -31.02758 1.000 39.12348 ? 1025 HOH A O     1 
HETATM 4022 O O     . HOH D 3 .   ? 37.23812 -42.05842 -13.19842 1.000 33.26706 ? 1026 HOH A O     1 
HETATM 4023 O O     . HOH D 3 .   ? 28.269   -7.721    -42.259   1.000 39.12317 ? 1027 HOH A O     1 
HETATM 4024 O O     . HOH D 3 .   ? 47.29302 -30.33586 -15.94518 1.000 39.78655 ? 1028 HOH A O     1 
HETATM 4025 O O     . HOH D 3 .   ? 31.09653 -40.47007 8.79904   1.000 36.65192 ? 1029 HOH A O     1 
HETATM 4026 O O     . HOH D 3 .   ? 39.13850 -46.84667 5.15925   1.000 26.76079 ? 1030 HOH A O     1 
HETATM 4027 O O     . HOH D 3 .   ? 42.88204 -57.24218 1.94994   1.000 45.71021 ? 1031 HOH A O     1 
HETATM 4028 O O     . HOH D 3 .   ? 15.49212 -32.35438 -27.45356 1.000 28.17827 ? 1032 HOH A O     1 
HETATM 4029 O O     . HOH D 3 .   ? 29.749   -8.398    4.161     1.000 30.61497 ? 1033 HOH A O     1 
HETATM 4030 O O     . HOH D 3 .   ? 53.53094 -32.00659 10.67605  1.000 41.62507 ? 1034 HOH A O     1 
HETATM 4031 O O     . HOH D 3 .   ? 41.86945 -41.97029 9.57191   1.000 38.91353 ? 1035 HOH A O     1 
HETATM 4032 O O     . HOH D 3 .   ? 34.33680 -20.03864 8.32065   1.000 25.11826 ? 1036 HOH A O     1 
HETATM 4033 O O     . HOH D 3 .   ? 42.57097 -43.55029 11.82161  1.000 42.78352 ? 1037 HOH A O     1 
HETATM 4034 O O     . HOH D 3 .   ? 56.96289 -48.46764 -13.50314 1.000 37.93331 ? 1038 HOH A O     1 
HETATM 4035 O O     . HOH D 3 .   ? 7.84512  -42.64143 -6.29648  1.000 37.38169 ? 1039 HOH A O     1 
HETATM 4036 O O     . HOH D 3 .   ? 46.85300 -44.69352 12.69367  1.000 39.82684 ? 1040 HOH A O     1 
HETATM 4037 O O     . HOH D 3 .   ? 28.47220 -42.23924 7.79075   1.000 39.14757 ? 1041 HOH A O     1 
HETATM 4038 O O     . HOH D 3 .   ? 23.32062 -40.39249 -36.47533 0.50  19.57225 ? 1042 HOH A O     1 
HETATM 4039 O O     . HOH D 3 .   ? 42.57616 -47.48940 11.83585  1.000 43.65691 ? 1043 HOH A O     1 
HETATM 4040 O O     . HOH D 3 .   ? 20.95446 -25.90379 -2.23451  1.000 26.88645 ? 1044 HOH A O     1 
HETATM 4041 O O     . HOH D 3 .   ? 19.65571 -23.21965 5.33434   1.000 40.00990 ? 1045 HOH A O     1 
HETATM 4042 O O     . HOH D 3 .   ? 57.88178 -26.71900 -13.61871 1.000 34.97374 ? 1046 HOH A O     1 
HETATM 4043 O O     . HOH D 3 .   ? 26.01834 -38.83236 7.80282   1.000 32.17003 ? 1047 HOH A O     1 
HETATM 4044 O O     . HOH D 3 .   ? 25.04739 -20.15915 -44.05086 1.000 31.95273 ? 1048 HOH A O     1 
HETATM 4045 O O     . HOH D 3 .   ? 73.21701 -26.73553 -5.87084  1.000 45.65941 ? 1049 HOH A O     1 
HETATM 4046 O O     . HOH D 3 .   ? 25.73330 -44.57138 -36.47533 0.50  39.83639 ? 1050 HOH A O     1 
HETATM 4047 O O     . HOH D 3 .   ? 63.61770 -36.72969 -18.23767 0.50  38.96935 ? 1051 HOH A O     1 
HETATM 4048 O O     . HOH D 3 .   ? 8.962    -29.958   -30.022   1.000 35.45242 ? 1052 HOH A O     1 
HETATM 4049 O O     . HOH D 3 .   ? 48.63867 -38.05738 14.56155  1.000 44.72492 ? 1053 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N     . MET A 1   ? 0.37045 0.37325 0.34403 0.01008  -0.01761 0.05568  1    MET A N     
2    C CA    . MET A 1   ? 0.33697 0.33842 0.31461 0.01347  -0.01947 0.05312  1    MET A CA    
3    C C     . MET A 1   ? 0.29739 0.28935 0.27776 0.01389  -0.01966 0.05387  1    MET A C     
4    O O     . MET A 1   ? 0.29198 0.28023 0.27320 0.01075  -0.01782 0.05341  1    MET A O     
5    C CB    . MET A 1   ? 0.28084 0.28808 0.26137 0.01302  -0.01841 0.04726  1    MET A CB    
6    C CG    . MET A 1   ? 0.30808 0.31670 0.29243 0.01678  -0.02014 0.04469  1    MET A CG    
7    S SD    . MET A 1   ? 0.37988 0.39610 0.36745 0.01596  -0.01879 0.03851  1    MET A SD    
8    C CE    . MET A 1   ? 0.34269 0.36319 0.32653 0.01156  -0.01672 0.03804  1    MET A CE    
9    N N     . ASN A 2   ? 0.28862 0.27670 0.27049 0.01786  -0.02201 0.05487  2    ASN A N     
10   C CA    . ASN A 2   ? 0.30256 0.28115 0.28690 0.01869  -0.02244 0.05475  2    ASN A CA    
11   C C     . ASN A 2   ? 0.31510 0.29486 0.30332 0.02109  -0.02244 0.04928  2    ASN A C     
12   O O     . ASN A 2   ? 0.28773 0.27567 0.27710 0.02207  -0.02216 0.04620  2    ASN A O     
13   C CB    . ASN A 2   ? 0.32783 0.29951 0.31090 0.02153  -0.02482 0.05986  2    ASN A CB    
14   C CG    . ASN A 2   ? 0.38030 0.35570 0.36419 0.02686  -0.02732 0.05999  2    ASN A CG    
15   O OD1   . ASN A 2   ? 0.36894 0.34946 0.35591 0.02912  -0.02741 0.05558  2    ASN A OD1   
16   N ND2   . ASN A 2   ? 0.43563 0.40883 0.41686 0.02889  -0.02938 0.06542  2    ASN A ND2   
17   N N     . ALA A 3   ? 0.31156 0.28296 0.30168 0.02193  -0.02272 0.04805  3    ALA A N     
18   C CA    . ALA A 3   ? 0.28931 0.26137 0.28241 0.02375  -0.02218 0.04269  3    ALA A CA    
19   C C     . ALA A 3   ? 0.30052 0.27728 0.29565 0.02889  -0.02350 0.04141  3    ALA A C     
20   O O     . ALA A 3   ? 0.29371 0.27605 0.29114 0.02986  -0.02246 0.03713  3    ALA A O     
21   C CB    . ALA A 3   ? 0.29520 0.25672 0.28911 0.02366  -0.02245 0.04158  3    ALA A CB    
22   N N     . SER A 4   ? 0.31498 0.28986 0.30957 0.03225  -0.02575 0.04524  4    SER A N     
23   C CA    . SER A 4   ? 0.31572 0.29586 0.31298 0.03746  -0.02723 0.04428  4    SER A CA    
24   C C     . SER A 4   ? 0.30107 0.29369 0.29902 0.03654  -0.02678 0.04270  4    SER A C     
25   O O     . SER A 4   ? 0.29391 0.29293 0.29544 0.03891  -0.02651 0.03924  4    SER A O     
26   C CB    . SER A 4   ? 0.35879 0.33449 0.35509 0.04117  -0.03002 0.04935  4    SER A CB    
27   O OG    . SER A 4   ? 0.47519 0.45821 0.47423 0.04598  -0.03170 0.04900  4    SER A OG    
28   N N     . GLU A 5   ? 0.29805 0.29429 0.29263 0.03304  -0.02662 0.04512  5    GLU A N     
29   C CA    A GLU A 5   ? 0.30989 0.31711 0.30467 0.03160  -0.02624 0.04317  5    GLU A CA    
30   C CA    B GLU A 5   ? 0.30994 0.31715 0.30469 0.03157  -0.02624 0.04319  5    GLU A CA    
31   C C     . GLU A 5   ? 0.26809 0.27817 0.26463 0.02862  -0.02350 0.03821  5    GLU A C     
32   O O     . GLU A 5   ? 0.26552 0.28395 0.26436 0.02868  -0.02316 0.03526  5    GLU A O     
33   C CB    A GLU A 5   ? 0.33753 0.34713 0.32745 0.02874  -0.02661 0.04672  5    GLU A CB    
34   C CB    B GLU A 5   ? 0.33717 0.34654 0.32702 0.02869  -0.02659 0.04678  5    GLU A CB    
35   C CG    A GLU A 5   ? 0.32120 0.34135 0.31060 0.02695  -0.02644 0.04448  5    GLU A CG    
36   C CG    B GLU A 5   ? 0.33635 0.34005 0.32321 0.03061  -0.02873 0.05263  5    GLU A CG    
37   C CD    A GLU A 5   ? 0.36282 0.39025 0.35361 0.03055  -0.02944 0.04528  5    GLU A CD    
38   C CD    B GLU A 5   ? 0.35591 0.36249 0.33727 0.02792  -0.02884 0.05624  5    GLU A CD    
39   O OE1   A GLU A 5   ? 0.36895 0.39343 0.36136 0.03488  -0.03156 0.04766  5    GLU A OE1   
40   O OE1   B GLU A 5   ? 0.32944 0.33389 0.30836 0.02371  -0.02645 0.05648  5    GLU A OE1   
41   O OE2   A GLU A 5   ? 0.35152 0.38760 0.34197 0.02907  -0.02983 0.04344  5    GLU A OE2   
42   O OE2   B GLU A 5   ? 0.38769 0.39889 0.36710 0.03017  -0.03132 0.05885  5    GLU A OE2   
43   N N     . PHE A 6   ? 0.26619 0.26950 0.26186 0.02594  -0.02169 0.03738  6    PHE A N     
44   C CA    . PHE A 6   ? 0.25160 0.25697 0.24878 0.02353  -0.01930 0.03295  6    PHE A CA    
45   C C     . PHE A 6   ? 0.24882 0.25553 0.24979 0.02682  -0.01906 0.02940  6    PHE A C     
46   O O     . PHE A 6   ? 0.22613 0.23850 0.22889 0.02574  -0.01747 0.02595  6    PHE A O     
47   C CB    . PHE A 6   ? 0.25376 0.25178 0.24939 0.02023  -0.01787 0.03306  6    PHE A CB    
48   C CG    . PHE A 6   ? 0.22414 0.22362 0.22104 0.01808  -0.01571 0.02886  6    PHE A CG    
49   C CD1   . PHE A 6   ? 0.20615 0.21219 0.20271 0.01527  -0.01419 0.02727  6    PHE A CD1   
50   C CD2   . PHE A 6   ? 0.20751 0.20142 0.20557 0.01897  -0.01530 0.02649  6    PHE A CD2   
51   C CE1   . PHE A 6   ? 0.19422 0.20114 0.19181 0.01345  -0.01230 0.02385  6    PHE A CE1   
52   C CE2   . PHE A 6   ? 0.19452 0.18979 0.19317 0.01711  -0.01346 0.02298  6    PHE A CE2   
53   C CZ    . PHE A 6   ? 0.20084 0.20259 0.19937 0.01438  -0.01196 0.02189  6    PHE A CZ    
54   N N     . ARG A 7   ? 0.22512 0.22646 0.22727 0.03089  -0.02044 0.03023  7    ARG A N     
55   C CA    . ARG A 7   ? 0.26885 0.27217 0.27461 0.03471  -0.02004 0.02691  7    ARG A CA    
56   C C     . ARG A 7   ? 0.23048 0.24532 0.23939 0.03595  -0.02020 0.02575  7    ARG A C     
57   O O     . ARG A 7   ? 0.26116 0.28100 0.27292 0.03631  -0.01850 0.02217  7    ARG A O     
58   C CB    . ARG A 7   ? 0.26282 0.25886 0.26931 0.03954  -0.02180 0.02836  7    ARG A CB    
59   C CG    . ARG A 7   ? 0.29738 0.28151 0.30164 0.03859  -0.02164 0.02839  7    ARG A CG    
60   C CD    . ARG A 7   ? 0.30631 0.28320 0.31171 0.04391  -0.02322 0.02882  7    ARG A CD    
61   N NE    . ARG A 7   ? 0.32138 0.28587 0.32435 0.04263  -0.02380 0.02975  7    ARG A NE    
62   C CZ    . ARG A 7   ? 0.29516 0.25362 0.29751 0.04190  -0.02273 0.02610  7    ARG A CZ    
63   N NH1   . ARG A 7   ? 0.27424 0.23764 0.27772 0.04248  -0.02077 0.02144  7    ARG A NH1   
64   N NH2   . ARG A 7   ? 0.29920 0.24639 0.29958 0.04038  -0.02373 0.02721  7    ARG A NH2   
65   N N     . ARG A 8   ? 0.23048 0.24984 0.23886 0.03642  -0.02230 0.02881  8    ARG A N     
66   C CA    . ARG A 8   ? 0.21313 0.24385 0.22461 0.03707  -0.02295 0.02773  8    ARG A CA    
67   C C     . ARG A 8   ? 0.23926 0.27546 0.24997 0.03205  -0.02107 0.02537  8    ARG A C     
68   O O     . ARG A 8   ? 0.21607 0.25853 0.23023 0.03159  -0.01963 0.02211  8    ARG A O     
69   C CB    . ARG A 8   ? 0.25467 0.28844 0.26510 0.03893  -0.02616 0.03172  8    ARG A CB    
70   C CG    . ARG A 8   ? 0.31541 0.36136 0.32911 0.03921  -0.02737 0.03056  8    ARG A CG    
71   C CD    . ARG A 8   ? 0.34807 0.39735 0.35968 0.04050  -0.03083 0.03449  8    ARG A CD    
72   N NE    . ARG A 8   ? 0.37126 0.43235 0.38545 0.03953  -0.03211 0.03291  8    ARG A NE    
73   C CZ    . ARG A 8   ? 0.41575 0.48222 0.42811 0.03992  -0.03528 0.03541  8    ARG A CZ    
74   N NH1   . ARG A 8   ? 0.43199 0.49327 0.43960 0.04141  -0.03735 0.04002  8    ARG A NH1   
75   N NH2   . ARG A 8   ? 0.43414 0.51141 0.44931 0.03860  -0.03650 0.03330  8    ARG A NH2   
76   N N     . ARG A 9   ? 0.22710 0.26096 0.23336 0.02830  -0.02094 0.02708  9    ARG A N     
77   C CA    . ARG A 9   ? 0.21341 0.25231 0.21869 0.02391  -0.01945 0.02501  9    ARG A CA    
78   C C     . ARG A 9   ? 0.19651 0.23322 0.20280 0.02171  -0.01650 0.02165  9    ARG A C     
79   O O     . ARG A 9   ? 0.21173 0.25390 0.21936 0.01930  -0.01517 0.01905  9    ARG A O     
80   C CB    . ARG A 9   ? 0.22015 0.25678 0.22023 0.02098  -0.01973 0.02762  9    ARG A CB    
81   C CG    . ARG A 9   ? 0.24446 0.28271 0.24233 0.02302  -0.02265 0.03147  9    ARG A CG    
82   C CD    . ARG A 9   ? 0.28184 0.32981 0.28271 0.02475  -0.02471 0.03036  9    ARG A CD    
83   N NE    . ARG A 9   ? 0.29734 0.34825 0.29492 0.02567  -0.02759 0.03373  9    ARG A NE    
84   C CZ    . ARG A 9   ? 0.30071 0.36058 0.29969 0.02641  -0.02995 0.03318  9    ARG A CZ    
85   N NH1   . ARG A 9   ? 0.29449 0.36151 0.29877 0.02620  -0.02967 0.02952  9    ARG A NH1   
86   N NH2   . ARG A 9   ? 0.32397 0.38589 0.31893 0.02722  -0.03272 0.03650  9    ARG A NH2   
87   N N     . GLY A 10  ? 0.19729 0.22589 0.20280 0.02241  -0.01564 0.02171  10   GLY A N     
88   C CA    . GLY A 10  ? 0.18688 0.21336 0.19286 0.02059  -0.01317 0.01868  10   GLY A CA    
89   C C     . GLY A 10  ? 0.19146 0.22356 0.20137 0.02230  -0.01206 0.01562  10   GLY A C     
90   O O     . GLY A 10  ? 0.18130 0.21641 0.19188 0.01979  -0.01007 0.01325  10   GLY A O     
91   N N     . LYS A 11  ? 0.19154 0.22522 0.20428 0.02670  -0.01320 0.01580  11   LYS A N     
92   C CA    . LYS A 11  ? 0.19348 0.23380 0.21058 0.02854  -0.01190 0.01310  11   LYS A CA    
93   C C     . LYS A 11  ? 0.19123 0.24181 0.21108 0.02657  -0.01213 0.01258  11   LYS A C     
94   O O     . LYS A 11  ? 0.20009 0.25628 0.22296 0.02559  -0.01022 0.01015  11   LYS A O     
95   C CB    . LYS A 11  ? 0.21134 0.25097 0.23115 0.03419  -0.01300 0.01342  11   LYS A CB    
96   C CG    . LYS A 11  ? 0.20399 0.23257 0.22098 0.03613  -0.01305 0.01363  11   LYS A CG    
97   C CD    . LYS A 11  ? 0.23071 0.25821 0.25049 0.04212  -0.01382 0.01332  11   LYS A CD    
98   C CE    . LYS A 11  ? 0.21874 0.23410 0.23533 0.04375  -0.01420 0.01338  11   LYS A CE    
99   N NZ    . LYS A 11  ? 0.27060 0.28403 0.28969 0.04988  -0.01449 0.01223  11   LYS A NZ    
100  N N     . GLU A 12  ? 0.18004 0.23308 0.19868 0.02577  -0.01447 0.01482  12   GLU A N     
101  C CA    . GLU A 12  ? 0.18003 0.24209 0.20055 0.02323  -0.01499 0.01397  12   GLU A CA    
102  C C     . GLU A 12  ? 0.18960 0.25092 0.20812 0.01825  -0.01273 0.01205  12   GLU A C     
103  O O     . GLU A 12  ? 0.17231 0.24008 0.19372 0.01609  -0.01177 0.00997  12   GLU A O     
104  C CB    . GLU A 12  ? 0.22786 0.29201 0.24631 0.02354  -0.01816 0.01672  12   GLU A CB    
105  C CG    . GLU A 12  ? 0.25212 0.31890 0.27340 0.02862  -0.02082 0.01874  12   GLU A CG    
106  C CD    . GLU A 12  ? 0.30729 0.37538 0.32547 0.02901  -0.02411 0.02198  12   GLU A CD    
107  O OE1   . GLU A 12  ? 0.31807 0.38380 0.33121 0.02550  -0.02401 0.02273  12   GLU A OE1   
108  O OE2   . GLU A 12  ? 0.30304 0.37467 0.32370 0.03305  -0.02677 0.02384  12   GLU A OE2   
109  N N     . MET A 13  ? 0.17264 0.22616 0.18657 0.01637  -0.01188 0.01284  13   MET A N     
110  C CA    . MET A 13  ? 0.15119 0.20333 0.16337 0.01221  -0.00970 0.01115  13   MET A CA    
111  C C     . MET A 13  ? 0.18250 0.23464 0.19698 0.01200  -0.00718 0.00876  13   MET A C     
112  O O     . MET A 13  ? 0.18515 0.23980 0.20028 0.00895  -0.00555 0.00702  13   MET A O     
113  C CB    . MET A 13  ? 0.17335 0.21773 0.18089 0.01073  -0.00939 0.01274  13   MET A CB    
114  C CG    . MET A 13  ? 0.15800 0.20099 0.16377 0.00681  -0.00737 0.01129  13   MET A CG    
115  S SD    . MET A 13  ? 0.20403 0.25390 0.20996 0.00367  -0.00751 0.00973  13   MET A SD    
116  C CE    . MET A 13  ? 0.19705 0.24490 0.19809 0.00311  -0.00895 0.01223  13   MET A CE    
117  N N     . VAL A 14  ? 0.15042 0.19933 0.16573 0.01524  -0.00678 0.00865  14   VAL A N     
118  C CA    . VAL A 14  ? 0.16510 0.21454 0.18205 0.01547  -0.00429 0.00639  14   VAL A CA    
119  C C     . VAL A 14  ? 0.18117 0.24010 0.20286 0.01496  -0.00348 0.00498  14   VAL A C     
120  O O     . VAL A 14  ? 0.17327 0.23416 0.19571 0.01239  -0.00122 0.00344  14   VAL A O     
121  C CB    . VAL A 14  ? 0.18160 0.22635 0.19843 0.01962  -0.00423 0.00619  14   VAL A CB    
122  C CG1   . VAL A 14  ? 0.16473 0.21224 0.18356 0.02057  -0.00161 0.00376  14   VAL A CG1   
123  C CG2   . VAL A 14  ? 0.17018 0.20514 0.18255 0.01904  -0.00463 0.00706  14   VAL A CG2   
124  N N     . ASP A 15  ? 0.17336 0.23847 0.19854 0.01726  -0.00542 0.00570  15   ASP A N     
125  C CA    . ASP A 15  ? 0.17930 0.25444 0.20993 0.01661  -0.00496 0.00447  15   ASP A CA    
126  C C     . ASP A 15  ? 0.16987 0.24809 0.20013 0.01159  -0.00502 0.00383  15   ASP A C     
127  O O     . ASP A 15  ? 0.18562 0.26925 0.21923 0.00920  -0.00336 0.00231  15   ASP A O     
128  C CB    . ASP A 15  ? 0.18136 0.26265 0.21602 0.02041  -0.00755 0.00558  15   ASP A CB    
129  C CG    . ASP A 15  ? 0.20642 0.28845 0.24424 0.02537  -0.00649 0.00507  15   ASP A CG    
130  O OD1   . ASP A 15  ? 0.22072 0.30208 0.25899 0.02519  -0.00338 0.00329  15   ASP A OD1   
131  O OD2   . ASP A 15  ? 0.26088 0.34395 0.30045 0.02963  -0.00873 0.00646  15   ASP A OD2   
132  N N     . TYR A 16  ? 0.16444 0.23910 0.19057 0.00991  -0.00678 0.00495  16   TYR A N     
133  C CA    . TYR A 16  ? 0.17283 0.24940 0.19793 0.00539  -0.00680 0.00394  16   TYR A CA    
134  C C     . TYR A 16  ? 0.18036 0.25277 0.20401 0.00234  -0.00378 0.00257  16   TYR A C     
135  O O     . TYR A 16  ? 0.17811 0.25406 0.20374 -0.00095 -0.00275 0.00107  16   TYR A O     
136  C CB    . TYR A 16  ? 0.19955 0.27272 0.21979 0.00471  -0.00889 0.00538  16   TYR A CB    
137  C CG    . TYR A 16  ? 0.21713 0.29184 0.23575 0.00044  -0.00895 0.00392  16   TYR A CG    
138  C CD1   . TYR A 16  ? 0.23330 0.31580 0.25467 -0.00103 -0.01080 0.00278  16   TYR A CD1   
139  C CD2   . TYR A 16  ? 0.24379 0.31220 0.25838 -0.00207 -0.00723 0.00346  16   TYR A CD2   
140  C CE1   . TYR A 16  ? 0.25150 0.33467 0.27107 -0.00498 -0.01096 0.00099  16   TYR A CE1   
141  C CE2   . TYR A 16  ? 0.24439 0.31356 0.25740 -0.00561 -0.00716 0.00181  16   TYR A CE2   
142  C CZ    . TYR A 16  ? 0.27192 0.34810 0.28718 -0.00712 -0.00902 0.00045  16   TYR A CZ    
143  O OH    . TYR A 16  ? 0.29221 0.36844 0.30557 -0.01069 -0.00908 -0.00162 16   TYR A OH    
144  N N     . VAL A 17  ? 0.15907 0.22377 0.17926 0.00328  -0.00254 0.00319  17   VAL A N     
145  C CA    . VAL A 17  ? 0.18158 0.24214 0.20012 0.00083  0.00004  0.00223  17   VAL A CA    
146  C C     . VAL A 17  ? 0.17961 0.24448 0.20185 0.00067  0.00225  0.00098  17   VAL A C     
147  O O     . VAL A 17  ? 0.15800 0.22358 0.18076 -0.00255 0.00400  0.00007  17   VAL A O     
148  C CB    . VAL A 17  ? 0.20224 0.25443 0.21678 0.00218  0.00043  0.00318  17   VAL A CB    
149  C CG1   . VAL A 17  ? 0.21507 0.26377 0.22829 0.00044  0.00289  0.00229  17   VAL A CG1   
150  C CG2   . VAL A 17  ? 0.20124 0.24955 0.21230 0.00126  -0.00103 0.00452  17   VAL A CG2   
151  N N     . ALA A 18  ? 0.16992 0.23764 0.19477 0.00422  0.00237  0.00101  18   ALA A N     
152  C CA    . ALA A 18  ? 0.17757 0.25024 0.20604 0.00439  0.00487  -0.00007 18   ALA A CA    
153  C C     . ALA A 18  ? 0.20765 0.28903 0.24119 0.00157  0.00486  -0.00074 18   ALA A C     
154  O O     . ALA A 18  ? 0.17196 0.25591 0.20742 -0.00097 0.00732  -0.00144 18   ALA A O     
155  C CB    . ALA A 18  ? 0.18776 0.26197 0.21811 0.00932  0.00498  -0.00011 18   ALA A CB    
156  N N     . ASN A 19  ? 0.16832 0.25430 0.20396 0.00178  0.00199  -0.00042 19   ASN A N     
157  C CA    . ASN A 19  ? 0.18755 0.28180 0.22799 -0.00133 0.00137  -0.00129 19   ASN A CA    
158  C C     . ASN A 19  ? 0.20474 0.29570 0.24290 -0.00644 0.00226  -0.00216 19   ASN A C     
159  O O     . ASN A 19  ? 0.18811 0.28353 0.22995 -0.00974 0.00363  -0.00308 19   ASN A O     
160  C CB    . ASN A 19  ? 0.17802 0.27716 0.22003 -0.00003 -0.00243 -0.00077 19   ASN A CB    
161  C CG    . ASN A 19  ? 0.20288 0.30712 0.24889 0.00499  -0.00342 0.00006  19   ASN A CG    
162  O OD1   . ASN A 19  ? 0.22313 0.32917 0.27195 0.00716  -0.00100 -0.00027 19   ASN A OD1   
163  N ND2   . ASN A 19  ? 0.21082 0.31742 0.25692 0.00709  -0.00695 0.00116  19   ASN A ND2   
164  N N     . TYR A 20  ? 0.17091 0.25405 0.20327 -0.00713 0.00157  -0.00181 20   TYR A N     
165  C CA    . TYR A 20  ? 0.17402 0.25327 0.20400 -0.01138 0.00242  -0.00273 20   TYR A CA    
166  C C     . TYR A 20  ? 0.18338 0.26013 0.21366 -0.01304 0.00578  -0.00286 20   TYR A C     
167  O O     . TYR A 20  ? 0.19547 0.27345 0.22753 -0.01684 0.00689  -0.00371 20   TYR A O     
168  C CB    . TYR A 20  ? 0.17634 0.24800 0.20034 -0.01102 0.00147  -0.00215 20   TYR A CB    
169  C CG    . TYR A 20  ? 0.19000 0.25597 0.21113 -0.01431 0.00299  -0.00292 20   TYR A CG    
170  C CD1   . TYR A 20  ? 0.19166 0.25931 0.21361 -0.01796 0.00256  -0.00457 20   TYR A CD1   
171  C CD2   . TYR A 20  ? 0.18101 0.23987 0.19878 -0.01367 0.00468  -0.00211 20   TYR A CD2   
172  C CE1   . TYR A 20  ? 0.18906 0.25091 0.20848 -0.02058 0.00397  -0.00533 20   TYR A CE1   
173  C CE2   . TYR A 20  ? 0.21122 0.26505 0.22676 -0.01623 0.00596  -0.00264 20   TYR A CE2   
174  C CZ    . TYR A 20  ? 0.18818 0.24329 0.20456 -0.01952 0.00571  -0.00423 20   TYR A CZ    
175  O OH    . TYR A 20  ? 0.20107 0.25058 0.21531 -0.02170 0.00700  -0.00482 20   TYR A OH    
176  N N     . MET A 21  ? 0.17769 0.25060 0.20594 -0.01028 0.00731  -0.00198 21   MET A N     
177  C CA    . MET A 21  ? 0.19604 0.26643 0.22360 -0.01149 0.01041  -0.00184 21   MET A CA    
178  C C     . MET A 21  ? 0.21253 0.29072 0.24557 -0.01271 0.01230  -0.00218 21   MET A C     
179  O O     . MET A 21  ? 0.19756 0.27532 0.23117 -0.01598 0.01448  -0.00213 21   MET A O     
180  C CB    . MET A 21  ? 0.20478 0.26992 0.22868 -0.00805 0.01121  -0.00113 21   MET A CB    
181  C CG    . MET A 21  ? 0.22481 0.28154 0.24346 -0.00812 0.01035  -0.00058 21   MET A CG    
182  S SD    . MET A 21  ? 0.29256 0.34487 0.30924 -0.01222 0.01215  -0.00054 21   MET A SD    
183  C CE    . MET A 21  ? 0.27817 0.32335 0.29052 -0.01203 0.01039  -0.00010 21   MET A CE    
184  N N     . GLU A 22  ? 0.19197 0.27742 0.22933 -0.01008 0.01161  -0.00233 22   GLU A N     
185  C CA    . GLU A 22  ? 0.21760 0.31145 0.26084 -0.01089 0.01377  -0.00253 22   GLU A CA    
186  C C     . GLU A 22  ? 0.22764 0.32679 0.27538 -0.01577 0.01324  -0.00316 22   GLU A C     
187  O O     . GLU A 22  ? 0.25624 0.36037 0.30814 -0.01827 0.01570  -0.00305 22   GLU A O     
188  C CB    . GLU A 22  ? 0.24690 0.34752 0.29415 -0.00633 0.01306  -0.00259 22   GLU A CB    
189  C CG    . GLU A 22  ? 0.27791 0.37460 0.32196 -0.00198 0.01492  -0.00239 22   GLU A CG    
190  C CD    . GLU A 22  ? 0.30476 0.40843 0.35342 0.00271  0.01492  -0.00268 22   GLU A CD    
191  O OE1   . GLU A 22  ? 0.33473 0.44393 0.38749 0.00383  0.01215  -0.00261 22   GLU A OE1   
192  O OE2   . GLU A 22  ? 0.35951 0.46309 0.40747 0.00551  0.01765  -0.00302 22   GLU A OE2   
193  N N     . GLY A 23  ? 0.19404 0.29212 0.24086 -0.01735 0.01014  -0.00386 23   GLY A N     
194  C CA    . GLY A 23  ? 0.23348 0.33610 0.28421 -0.02207 0.00916  -0.00495 23   GLY A CA    
195  C C     . GLY A 23  ? 0.22490 0.31941 0.27123 -0.02592 0.00929  -0.00557 23   GLY A C     
196  O O     . GLY A 23  ? 0.24692 0.34303 0.29491 -0.02969 0.00773  -0.00697 23   GLY A O     
197  N N     . ILE A 24  ? 0.20289 0.28865 0.24369 -0.02491 0.01107  -0.00468 24   ILE A N     
198  C CA    . ILE A 24  ? 0.21653 0.29402 0.25290 -0.02757 0.01110  -0.00516 24   ILE A CA    
199  C C     . ILE A 24  ? 0.24783 0.32536 0.28686 -0.03261 0.01270  -0.00562 24   ILE A C     
200  O O     . ILE A 24  ? 0.25447 0.32680 0.29133 -0.03537 0.01200  -0.00673 24   ILE A O     
201  C CB    . ILE A 24  ? 0.19887 0.26794 0.22953 -0.02513 0.01252  -0.00387 24   ILE A CB    
202  C CG1   . ILE A 24  ? 0.22019 0.28145 0.24636 -0.02654 0.01174  -0.00444 24   ILE A CG1   
203  C CG2   . ILE A 24  ? 0.21020 0.27821 0.24109 -0.02573 0.01587  -0.00256 24   ILE A CG2   
204  C CD1   . ILE A 24  ? 0.19776 0.25199 0.21889 -0.02375 0.01216  -0.00327 24   ILE A CD1   
205  N N     . GLU A 25  ? 0.20783 0.29107 0.25162 -0.03391 0.01494  -0.00481 25   GLU A N     
206  C CA    . GLU A 25  ? 0.24444 0.32787 0.29128 -0.03914 0.01648  -0.00492 25   GLU A CA    
207  C C     . GLU A 25  ? 0.27521 0.36378 0.32645 -0.04273 0.01379  -0.00706 25   GLU A C     
208  O O     . GLU A 25  ? 0.33800 0.42494 0.39113 -0.04760 0.01433  -0.00770 25   GLU A O     
209  C CB    . GLU A 25  ? 0.27390 0.36267 0.32468 -0.03967 0.01994  -0.00317 25   GLU A CB    
210  C CG    . GLU A 25  ? 0.29356 0.37510 0.33929 -0.03866 0.02307  -0.00112 25   GLU A CG    
211  C CD    . GLU A 25  ? 0.34363 0.43071 0.39257 -0.03927 0.02682  0.00068  25   GLU A CD    
212  O OE1   . GLU A 25  ? 0.39681 0.48278 0.44237 -0.03561 0.02868  0.00183  25   GLU A OE1   
213  O OE2   . GLU A 25  ? 0.32893 0.42160 0.38371 -0.04350 0.02794  0.00087  25   GLU A OE2   
214  N N     . GLY A 26  ? 0.25436 0.34884 0.30712 -0.04050 0.01072  -0.00816 26   GLY A N     
215  C CA    . GLY A 26  ? 0.26886 0.36794 0.32471 -0.04364 0.00750  -0.01042 26   GLY A CA    
216  C C     . GLY A 26  ? 0.26729 0.35894 0.31719 -0.04429 0.00516  -0.01232 26   GLY A C     
217  O O     . GLY A 26  ? 0.30527 0.39964 0.35653 -0.04710 0.00236  -0.01462 26   GLY A O     
218  N N     . ARG A 27  ? 0.25744 0.34010 0.30080 -0.04172 0.00625  -0.01151 27   ARG A N     
219  C CA    . ARG A 27  ? 0.27655 0.35197 0.31407 -0.04191 0.00471  -0.01316 27   ARG A CA    
220  C C     . ARG A 27  ? 0.26367 0.33152 0.29992 -0.04587 0.00630  -0.01413 27   ARG A C     
221  O O     . ARG A 27  ? 0.28651 0.35081 0.32328 -0.04664 0.00924  -0.01237 27   ARG A O     
222  C CB    . ARG A 27  ? 0.25924 0.32925 0.29108 -0.03723 0.00511  -0.01169 27   ARG A CB    
223  C CG    . ARG A 27  ? 0.27526 0.35074 0.30783 -0.03292 0.00391  -0.01029 27   ARG A CG    
224  C CD    . ARG A 27  ? 0.23022 0.30524 0.25881 -0.03106 0.00102  -0.01106 27   ARG A CD    
225  N NE    . ARG A 27  ? 0.20872 0.28933 0.23852 -0.02727 -0.00067 -0.00969 27   ARG A NE    
226  C CZ    . ARG A 27  ? 0.23417 0.31737 0.26205 -0.02583 -0.00367 -0.00997 27   ARG A CZ    
227  N NH1   . ARG A 27  ? 0.23721 0.31858 0.26164 -0.02791 -0.00529 -0.01189 27   ARG A NH1   
228  N NH2   . ARG A 27  ? 0.24022 0.32765 0.26931 -0.02206 -0.00504 -0.00828 27   ARG A NH2   
229  N N     . GLN A 28  ? 0.23205 0.29712 0.26625 -0.04823 0.00432  -0.01695 28   GLN A N     
230  C CA    . GLN A 28  ? 0.23154 0.28746 0.26326 -0.05105 0.00562  -0.01815 28   GLN A CA    
231  C C     . GLN A 28  ? 0.21610 0.26379 0.24219 -0.04743 0.00737  -0.01665 28   GLN A C     
232  O O     . GLN A 28  ? 0.22160 0.26864 0.24370 -0.04411 0.00619  -0.01689 28   GLN A O     
233  C CB    . GLN A 28  ? 0.25263 0.30741 0.28278 -0.05380 0.00292  -0.02203 28   GLN A CB    
234  C CG    . GLN A 28  ? 0.29048 0.33483 0.31743 -0.05606 0.00407  -0.02380 28   GLN A CG    
235  C CD    . GLN A 28  ? 0.33432 0.37785 0.35998 -0.05922 0.00134  -0.02821 28   GLN A CD    
236  O OE1   . GLN A 28  ? 0.41477 0.46340 0.44506 -0.06338 -0.00034 -0.02982 28   GLN A OE1   
237  N NE2   . GLN A 28  ? 0.26730 0.30473 0.28669 -0.05730 0.00089  -0.03031 28   GLN A NE2   
238  N N     . VAL A 29  ? 0.23066 0.27242 0.25658 -0.04816 0.01012  -0.01487 29   VAL A N     
239  C CA    . VAL A 29  ? 0.20745 0.24308 0.22910 -0.04450 0.01170  -0.01284 29   VAL A CA    
240  C C     . VAL A 29  ? 0.20781 0.23717 0.22462 -0.04316 0.01086  -0.01473 29   VAL A C     
241  O O     . VAL A 29  ? 0.18981 0.21769 0.20336 -0.03945 0.01086  -0.01373 29   VAL A O     
242  C CB    . VAL A 29  ? 0.18796 0.21872 0.21023 -0.04572 0.01454  -0.01044 29   VAL A CB    
243  C CG1   . VAL A 29  ? 0.24882 0.27368 0.27182 -0.04997 0.01504  -0.01188 29   VAL A CG1   
244  C CG2   . VAL A 29  ? 0.19495 0.22006 0.21300 -0.04191 0.01570  -0.00836 29   VAL A CG2   
245  N N     . TYR A 30  ? 0.20906 0.23483 0.22543 -0.04618 0.01020  -0.01761 30   TYR A N     
246  C CA    . TYR A 30  ? 0.22954 0.24944 0.24121 -0.04473 0.00979  -0.01972 30   TYR A CA    
247  C C     . TYR A 30  ? 0.22523 0.24870 0.23581 -0.04614 0.00715  -0.02335 30   TYR A C     
248  O O     . TYR A 30  ? 0.22314 0.24977 0.23686 -0.04997 0.00584  -0.02517 30   TYR A O     
249  C CB    . TYR A 30  ? 0.22753 0.23792 0.23825 -0.04629 0.01151  -0.02028 30   TYR A CB    
250  C CG    . TYR A 30  ? 0.25388 0.25801 0.25999 -0.04402 0.01168  -0.02225 30   TYR A CG    
251  C CD1   . TYR A 30  ? 0.29376 0.29494 0.29759 -0.04004 0.01302  -0.02006 30   TYR A CD1   
252  C CD2   . TYR A 30  ? 0.26250 0.26399 0.26664 -0.04584 0.01052  -0.02646 30   TYR A CD2   
253  C CE1   . TYR A 30  ? 0.32059 0.31694 0.32087 -0.03781 0.01348  -0.02176 30   TYR A CE1   
254  C CE2   . TYR A 30  ? 0.29240 0.28852 0.29225 -0.04344 0.01107  -0.02843 30   TYR A CE2   
255  C CZ    . TYR A 30  ? 0.31927 0.31313 0.31748 -0.03936 0.01269  -0.02595 30   TYR A CZ    
256  O OH    . TYR A 30  ? 0.40481 0.39419 0.39940 -0.03684 0.01352  -0.02784 30   TYR A OH    
257  N N     . PRO A 31  ? 0.23050 0.25387 0.23666 -0.04329 0.00628  -0.02439 31   PRO A N     
258  C CA    . PRO A 31  ? 0.20181 0.22985 0.20617 -0.04411 0.00352  -0.02734 31   PRO A CA    
259  C C     . PRO A 31  ? 0.24733 0.27057 0.24976 -0.04724 0.00279  -0.03176 31   PRO A C     
260  O O     . PRO A 31  ? 0.22185 0.23685 0.22322 -0.04784 0.00462  -0.03269 31   PRO A O     
261  C CB    . PRO A 31  ? 0.22770 0.25617 0.22740 -0.03982 0.00353  -0.02633 31   PRO A CB    
262  C CG    . PRO A 31  ? 0.23501 0.25595 0.23323 -0.03789 0.00630  -0.02500 31   PRO A CG    
263  C CD    . PRO A 31  ? 0.21243 0.23247 0.21517 -0.03913 0.00769  -0.02250 31   PRO A CD    
264  N N     . ASP A 32  ? 0.19965 0.22812 0.20151 -0.04913 -0.00016 -0.03457 32   ASP A N     
265  C CA    . ASP A 32  ? 0.22326 0.24797 0.22247 -0.05211 -0.00154 -0.03947 32   ASP A CA    
266  C C     . ASP A 32  ? 0.24460 0.26806 0.23653 -0.04944 -0.00222 -0.04190 32   ASP A C     
267  O O     . ASP A 32  ? 0.25768 0.27807 0.24622 -0.05145 -0.00347 -0.04647 32   ASP A O     
268  C CB    . ASP A 32  ? 0.25251 0.28402 0.25572 -0.05647 -0.00472 -0.04148 32   ASP A CB    
269  C CG    . ASP A 32  ? 0.35734 0.38710 0.36694 -0.06081 -0.00374 -0.04096 32   ASP A CG    
270  O OD1   . ASP A 32  ? 0.38764 0.42527 0.40319 -0.06236 -0.00452 -0.03891 32   ASP A OD1   
271  O OD2   . ASP A 32  ? 0.40170 0.42225 0.41046 -0.06260 -0.00209 -0.04248 32   ASP A OD2   
272  N N     . VAL A 33  ? 0.21139 0.23712 0.20071 -0.04511 -0.00136 -0.03903 33   VAL A N     
273  C CA    . VAL A 33  ? 0.22453 0.24947 0.20687 -0.04257 -0.00150 -0.04084 33   VAL A CA    
274  C C     . VAL A 33  ? 0.23953 0.25512 0.21867 -0.04160 0.00126  -0.04299 33   VAL A C     
275  O O     . VAL A 33  ? 0.24831 0.25812 0.23054 -0.04177 0.00349  -0.04176 33   VAL A O     
276  C CB    . VAL A 33  ? 0.21003 0.23965 0.19097 -0.03852 -0.00115 -0.03673 33   VAL A CB    
277  C CG1   . VAL A 33  ? 0.19612 0.23466 0.18008 -0.03898 -0.00404 -0.03479 33   VAL A CG1   
278  C CG2   . VAL A 33  ? 0.20766 0.23351 0.19114 -0.03613 0.00192  -0.03296 33   VAL A CG2   
279  N N     . GLU A 34  ? 0.22724 0.24147 0.19993 -0.04035 0.00114  -0.04619 34   GLU A N     
280  C CA    . GLU A 34  ? 0.27225 0.27854 0.24136 -0.03849 0.00392  -0.04842 34   GLU A CA    
281  C C     . GLU A 34  ? 0.24833 0.25642 0.21361 -0.03401 0.00589  -0.04612 34   GLU A C     
282  O O     . GLU A 34  ? 0.24521 0.26018 0.20893 -0.03283 0.00457  -0.04386 34   GLU A O     
283  C CB    . GLU A 34  ? 0.29315 0.29566 0.25754 -0.04070 0.00266  -0.05472 34   GLU A CB    
284  C CG    . GLU A 34  ? 0.35825 0.35855 0.32670 -0.04573 0.00061  -0.05722 34   GLU A CG    
285  C CD    . GLU A 34  ? 0.44470 0.43592 0.41694 -0.04647 0.00310  -0.05687 34   GLU A CD    
286  O OE1   . GLU A 34  ? 0.47286 0.45870 0.44345 -0.04292 0.00614  -0.05606 34   GLU A OE1   
287  O OE2   . GLU A 34  ? 0.49961 0.48928 0.47664 -0.05058 0.00203  -0.05716 34   GLU A OE2   
288  N N     . PRO A 35  ? 0.29483 0.29702 0.25902 -0.03142 0.00907  -0.04632 35   PRO A N     
289  C CA    . PRO A 35  ? 0.25448 0.25890 0.21611 -0.02741 0.01123  -0.04377 35   PRO A CA    
290  C C     . PRO A 35  ? 0.27515 0.28446 0.23003 -0.02660 0.01023  -0.04545 35   PRO A C     
291  O O     . PRO A 35  ? 0.31637 0.32373 0.26619 -0.02755 0.00962  -0.05039 35   PRO A O     
292  C CB    . PRO A 35  ? 0.29920 0.29613 0.26066 -0.02530 0.01448  -0.04533 35   PRO A CB    
293  C CG    . PRO A 35  ? 0.30260 0.29413 0.26926 -0.02762 0.01420  -0.04524 35   PRO A CG    
294  C CD    . PRO A 35  ? 0.29369 0.28713 0.26017 -0.03189 0.01095  -0.04794 35   PRO A CD    
295  N N     . GLY A 36  ? 0.24359 0.25900 0.19810 -0.02488 0.00997  -0.04125 36   GLY A N     
296  C CA    . GLY A 36  ? 0.25525 0.27570 0.20327 -0.02390 0.00909  -0.04163 36   GLY A CA    
297  C C     . GLY A 36  ? 0.24237 0.26871 0.18947 -0.02609 0.00495  -0.04166 36   GLY A C     
298  O O     . GLY A 36  ? 0.27739 0.30718 0.21800 -0.02582 0.00362  -0.04318 36   GLY A O     
299  N N     . TYR A 37  ? 0.20663 0.23470 0.15998 -0.02806 0.00290  -0.03989 37   TYR A N     
300  C CA    . TYR A 37  ? 0.18897 0.22297 0.14227 -0.03024 -0.00119 -0.04052 37   TYR A CA    
301  C C     . TYR A 37  ? 0.19329 0.23379 0.14475 -0.02807 -0.00248 -0.03625 37   TYR A C     
302  O O     . TYR A 37  ? 0.21311 0.25901 0.16187 -0.02886 -0.00583 -0.03685 37   TYR A O     
303  C CB    . TYR A 37  ? 0.21146 0.24618 0.17257 -0.03288 -0.00267 -0.03975 37   TYR A CB    
304  C CG    . TYR A 37  ? 0.20872 0.24605 0.17515 -0.03114 -0.00204 -0.03425 37   TYR A CG    
305  C CD1   . TYR A 37  ? 0.19722 0.22996 0.16698 -0.02976 0.00102  -0.03188 37   TYR A CD1   
306  C CD2   . TYR A 37  ? 0.20822 0.25267 0.17635 -0.03085 -0.00480 -0.03165 37   TYR A CD2   
307  C CE1   . TYR A 37  ? 0.21352 0.24848 0.18754 -0.02827 0.00133  -0.02733 37   TYR A CE1   
308  C CE2   . TYR A 37  ? 0.18398 0.23034 0.15660 -0.02911 -0.00429 -0.02712 37   TYR A CE2   
309  C CZ    . TYR A 37  ? 0.19414 0.23565 0.16946 -0.02795 -0.00125 -0.02513 37   TYR A CZ    
310  O OH    . TYR A 37  ? 0.18985 0.23309 0.16910 -0.02629 -0.00098 -0.02105 37   TYR A OH    
311  N N     . LEU A 38  ? 0.20772 0.24762 0.16079 -0.02541 -0.00006 -0.03181 38   LEU A N     
312  C CA    . LEU A 38  ? 0.18303 0.22804 0.13645 -0.02361 -0.00133 -0.02698 38   LEU A CA    
313  C C     . LEU A 38  ? 0.18020 0.22793 0.12589 -0.02190 -0.00141 -0.02623 38   LEU A C     
314  O O     . LEU A 38  ? 0.21044 0.26331 0.15439 -0.02138 -0.00416 -0.02397 38   LEU A O     
315  C CB    . LEU A 38  ? 0.19077 0.23358 0.14910 -0.02184 0.00106  -0.02272 38   LEU A CB    
316  C CG    . LEU A 38  ? 0.21030 0.25721 0.17045 -0.02024 -0.00043 -0.01782 38   LEU A CG    
317  C CD1   . LEU A 38  ? 0.22871 0.28031 0.19203 -0.02157 -0.00404 -0.01809 38   LEU A CD1   
318  C CD2   . LEU A 38  ? 0.25532 0.29929 0.22029 -0.01891 0.00174  -0.01442 38   LEU A CD2   
319  N N     . ARG A 39  ? 0.20891 0.25341 0.14993 -0.02081 0.00166  -0.02787 39   ARG A N     
320  C CA    . ARG A 39  ? 0.21860 0.26578 0.15187 -0.01912 0.00225  -0.02684 39   ARG A CA    
321  C C     . ARG A 39  ? 0.22693 0.27884 0.15440 -0.02014 -0.00164 -0.02868 39   ARG A C     
322  O O     . ARG A 39  ? 0.22504 0.28109 0.14867 -0.01873 -0.00277 -0.02507 39   ARG A O     
323  C CB    . ARG A 39  ? 0.23374 0.27706 0.16283 -0.01800 0.00627  -0.02962 39   ARG A CB    
324  C CG    . ARG A 39  ? 0.25974 0.30583 0.18189 -0.01586 0.00822  -0.02729 39   ARG A CG    
325  C CD    . ARG A 39  ? 0.26761 0.31052 0.18606 -0.01451 0.01250  -0.03040 39   ARG A CD    
326  N NE    . ARG A 39  ? 0.30343 0.34328 0.22826 -0.01320 0.01602  -0.02823 39   ARG A NE    
327  C CZ    . ARG A 39  ? 0.37351 0.41528 0.30009 -0.01161 0.01828  -0.02318 39   ARG A CZ    
328  N NH1   . ARG A 39  ? 0.32866 0.37484 0.25108 -0.01108 0.01770  -0.01935 39   ARG A NH1   
329  N NH2   . ARG A 39  ? 0.35496 0.39409 0.28767 -0.01063 0.02105  -0.02180 39   ARG A NH2   
330  N N     . PRO A 40  ? 0.22783 0.27943 0.15434 -0.02260 -0.00400 -0.03389 40   PRO A N     
331  C CA    . PRO A 40  ? 0.24096 0.29788 0.16202 -0.02359 -0.00826 -0.03542 40   PRO A CA    
332  C C     . PRO A 40  ? 0.21600 0.27880 0.14132 -0.02350 -0.01201 -0.03125 40   PRO A C     
333  O O     . PRO A 40  ? 0.20574 0.27376 0.12613 -0.02328 -0.01540 -0.03074 40   PRO A O     
334  C CB    . PRO A 40  ? 0.26424 0.31879 0.18524 -0.02676 -0.00995 -0.04208 40   PRO A CB    
335  C CG    . PRO A 40  ? 0.27136 0.31848 0.19487 -0.02672 -0.00581 -0.04430 40   PRO A CG    
336  C CD    . PRO A 40  ? 0.23524 0.28123 0.16449 -0.02456 -0.00285 -0.03883 40   PRO A CD    
337  N N     . LEU A 41  ? 0.18823 0.25040 0.12225 -0.02339 -0.01153 -0.02827 41   LEU A N     
338  C CA    . LEU A 41  ? 0.21144 0.27897 0.15043 -0.02307 -0.01487 -0.02481 41   LEU A CA    
339  C C     . LEU A 41  ? 0.24144 0.31022 0.17987 -0.01994 -0.01417 -0.01864 41   LEU A C     
340  O O     . LEU A 41  ? 0.23848 0.31153 0.18016 -0.01900 -0.01699 -0.01551 41   LEU A O     
341  C CB    . LEU A 41  ? 0.20174 0.26805 0.15028 -0.02468 -0.01467 -0.02523 41   LEU A CB    
342  C CG    . LEU A 41  ? 0.20478 0.26866 0.15508 -0.02817 -0.01494 -0.03084 41   LEU A CG    
343  C CD1   . LEU A 41  ? 0.18108 0.24392 0.14065 -0.02963 -0.01429 -0.03025 41   LEU A CD1   
344  C CD2   . LEU A 41  ? 0.18620 0.25512 0.13328 -0.03036 -0.01935 -0.03440 41   LEU A CD2   
345  N N     . ILE A 42  ? 0.20597 0.27117 0.14066 -0.01833 -0.01050 -0.01684 42   ILE A N     
346  C CA    . ILE A 42  ? 0.23071 0.29602 0.16519 -0.01582 -0.00936 -0.01093 42   ILE A CA    
347  C C     . ILE A 42  ? 0.19797 0.26446 0.12300 -0.01468 -0.00851 -0.00988 42   ILE A C     
348  O O     . ILE A 42  ? 0.22240 0.28735 0.14219 -0.01538 -0.00662 -0.01375 42   ILE A O     
349  C CB    . ILE A 42  ? 0.21560 0.27588 0.15554 -0.01525 -0.00552 -0.00920 42   ILE A CB    
350  C CG1   . ILE A 42  ? 0.28516 0.34524 0.23372 -0.01571 -0.00676 -0.00853 42   ILE A CG1   
351  C CG2   . ILE A 42  ? 0.29591 0.35529 0.23394 -0.01320 -0.00346 -0.00399 42   ILE A CG2   
352  C CD1   . ILE A 42  ? 0.30210 0.35736 0.25572 -0.01529 -0.00351 -0.00716 42   ILE A CD1   
353  N N     . PRO A 43  ? 0.22086 0.28989 0.14313 -0.01288 -0.00978 -0.00478 43   PRO A N     
354  C CA    . PRO A 43  ? 0.22770 0.29780 0.14069 -0.01184 -0.00845 -0.00309 43   PRO A CA    
355  C C     . PRO A 43  ? 0.22642 0.29261 0.13833 -0.01152 -0.00305 -0.00310 43   PRO A C     
356  O O     . PRO A 43  ? 0.20302 0.26566 0.12177 -0.01158 -0.00059 -0.00246 43   PRO A O     
357  C CB    . PRO A 43  ? 0.25246 0.32458 0.16525 -0.00995 -0.01040 0.00350  43   PRO A CB    
358  C CG    . PRO A 43  ? 0.26170 0.33624 0.18103 -0.01011 -0.01461 0.00311  43   PRO A CG    
359  C CD    . PRO A 43  ? 0.21199 0.28302 0.13906 -0.01156 -0.01253 -0.00023 43   PRO A CD    
360  N N     . ALA A 44  ? 0.23935 0.30668 0.14240 -0.01107 -0.00123 -0.00382 44   ALA A N     
361  C CA    . ALA A 44  ? 0.27486 0.33962 0.17643 -0.01057 0.00409  -0.00429 44   ALA A CA    
362  C C     . ALA A 44  ? 0.28352 0.34780 0.18695 -0.00940 0.00677  0.00228  44   ALA A C     
363  O O     . ALA A 44  ? 0.26283 0.32528 0.16777 -0.00908 0.01120  0.00247  44   ALA A O     
364  C CB    . ALA A 44  ? 0.31250 0.37899 0.20357 -0.01036 0.00538  -0.00779 44   ALA A CB    
365  N N     . ALA A 45  ? 0.25244 0.31825 0.15615 -0.00878 0.00416  0.00763  45   ALA A N     
366  C CA    . ALA A 45  ? 0.23803 0.30278 0.14348 -0.00804 0.00635  0.01403  45   ALA A CA    
367  C C     . ALA A 45  ? 0.21772 0.28137 0.12934 -0.00762 0.00297  0.01796  45   ALA A C     
368  O O     . ALA A 45  ? 0.20784 0.27316 0.12021 -0.00745 -0.00125 0.01677  45   ALA A O     
369  C CB    . ALA A 45  ? 0.26242 0.32998 0.15839 -0.00731 0.00762  0.01764  45   ALA A CB    
370  N N     . ALA A 46  ? 0.21253 0.27346 0.12880 -0.00742 0.00491  0.02253  46   ALA A N     
371  C CA    . ALA A 46  ? 0.20571 0.26470 0.12754 -0.00677 0.00212  0.02629  46   ALA A CA    
372  C C     . ALA A 46  ? 0.22330 0.28453 0.13965 -0.00551 -0.00124 0.03036  46   ALA A C     
373  O O     . ALA A 46  ? 0.21296 0.27633 0.12135 -0.00531 -0.00028 0.03249  46   ALA A O     
374  C CB    . ALA A 46  ? 0.20450 0.25976 0.13152 -0.00708 0.00487  0.03025  46   ALA A CB    
375  N N     . PRO A 47  ? 0.20293 0.26394 0.12325 -0.00443 -0.00517 0.03158  47   PRO A N     
376  C CA    . PRO A 47  ? 0.22151 0.28453 0.13718 -0.00279 -0.00869 0.03582  47   PRO A CA    
377  C C     . PRO A 47  ? 0.24437 0.30420 0.15843 -0.00226 -0.00714 0.04275  47   PRO A C     
378  O O     . PRO A 47  ? 0.21121 0.26665 0.13102 -0.00278 -0.00504 0.04465  47   PRO A O     
379  C CB    . PRO A 47  ? 0.24281 0.30612 0.16523 -0.00158 -0.01266 0.03493  47   PRO A CB    
380  C CG    . PRO A 47  ? 0.21152 0.27056 0.14220 -0.00241 -0.01026 0.03336  47   PRO A CG    
381  C CD    . PRO A 47  ? 0.22252 0.28180 0.15153 -0.00440 -0.00662 0.02913  47   PRO A CD    
382  N N     . GLN A 48  ? 0.24417 0.30618 0.15012 -0.00139 -0.00831 0.04662  48   GLN A N     
383  C CA    . GLN A 48  ? 0.24574 0.30456 0.14962 -0.00108 -0.00699 0.05381  48   GLN A CA    
384  C C     . GLN A 48  ? 0.27808 0.33331 0.18696 0.00080  -0.01048 0.05789  48   GLN A C     
385  O O     . GLN A 48  ? 0.25045 0.30048 0.16288 0.00052  -0.00904 0.06217  48   GLN A O     
386  C CB    . GLN A 48  ? 0.26997 0.33223 0.16274 -0.00077 -0.00681 0.05688  48   GLN A CB    
387  C CG    . GLN A 48  ? 0.27381 0.33861 0.16130 -0.00245 -0.00216 0.05393  48   GLN A CG    
388  C CD    . GLN A 48  ? 0.29871 0.36062 0.18835 -0.00393 0.00298  0.05756  48   GLN A CD    
389  O OE1   . GLN A 48  ? 0.32063 0.37970 0.21014 -0.00390 0.00324  0.06426  48   GLN A OE1   
390  N NE2   . GLN A 48  ? 0.26427 0.32687 0.15631 -0.00529 0.00702  0.05321  48   GLN A NE2   
391  N N     . GLU A 49  ? 0.27916 0.33720 0.18868 0.00278  -0.01521 0.05644  49   GLU A N     
392  C CA    . GLU A 49  ? 0.29584 0.35156 0.21087 0.00520  -0.01889 0.05881  49   GLU A CA    
393  C C     . GLU A 49  ? 0.24828 0.30355 0.17247 0.00506  -0.01922 0.05351  49   GLU A C     
394  O O     . GLU A 49  ? 0.25988 0.31837 0.18497 0.00349  -0.01824 0.04776  49   GLU A O     
395  C CB    . GLU A 49  ? 0.30237 0.36280 0.21277 0.00764  -0.02381 0.06041  49   GLU A CB    
396  C CG    . GLU A 49  ? 0.40907 0.47032 0.30929 0.00810  -0.02404 0.06607  49   GLU A CG    
397  C CD    . GLU A 49  ? 0.47630 0.53076 0.37650 0.00863  -0.02269 0.07352  49   GLU A CD    
398  O OE1   . GLU A 49  ? 0.50597 0.55516 0.41396 0.00952  -0.02309 0.07459  49   GLU A OE1   
399  O OE2   . GLU A 49  ? 0.57907 0.63328 0.47131 0.00806  -0.02117 0.07832  49   GLU A OE2   
400  N N     . PRO A 50  ? 0.24018 0.29118 0.17099 0.00670  -0.02047 0.05530  50   PRO A N     
401  C CA    . PRO A 50  ? 0.26332 0.31394 0.20237 0.00665  -0.02048 0.05052  50   PRO A CA    
402  C C     . PRO A 50  ? 0.27776 0.33502 0.21836 0.00755  -0.02365 0.04628  50   PRO A C     
403  O O     . PRO A 50  ? 0.25680 0.31812 0.19451 0.00950  -0.02729 0.04802  50   PRO A O     
404  C CB    . PRO A 50  ? 0.28433 0.32888 0.22847 0.00879  -0.02151 0.05409  50   PRO A CB    
405  C CG    . PRO A 50  ? 0.29014 0.33017 0.22943 0.00850  -0.02038 0.06034  50   PRO A CG    
406  C CD    . PRO A 50  ? 0.31096 0.35650 0.24194 0.00857  -0.02156 0.06175  50   PRO A CD    
407  N N     . ASP A 51  ? 0.25864 0.31718 0.20398 0.00593  -0.02228 0.04081  51   ASP A N     
408  C CA    . ASP A 51  ? 0.23285 0.29705 0.18201 0.00634  -0.02489 0.03663  51   ASP A CA    
409  C C     . ASP A 51  ? 0.26260 0.32528 0.21950 0.00879  -0.02628 0.03721  51   ASP A C     
410  O O     . ASP A 51  ? 0.28254 0.33895 0.24201 0.00958  -0.02473 0.03952  51   ASP A O     
411  C CB    . ASP A 51  ? 0.24982 0.31554 0.20039 0.00329  -0.02254 0.03074  51   ASP A CB    
412  C CG    . ASP A 51  ? 0.27584 0.34467 0.21888 0.00136  -0.02208 0.02881  51   ASP A CG    
413  O OD1   . ASP A 51  ? 0.29114 0.36301 0.22813 0.00241  -0.02449 0.03125  51   ASP A OD1   
414  O OD2   . ASP A 51  ? 0.26124 0.32932 0.20416 -0.00104 -0.01932 0.02478  51   ASP A OD2   
415  N N     . THR A 52  ? 0.25645 0.32512 0.21713 0.00997  -0.02923 0.03493  52   THR A N     
416  C CA    . THR A 52  ? 0.25821 0.32657 0.22640 0.01261  -0.03035 0.03499  52   THR A CA    
417  C C     . THR A 52  ? 0.23659 0.30398 0.21054 0.01073  -0.02759 0.03050  52   THR A C     
418  O O     . THR A 52  ? 0.22113 0.29050 0.19434 0.00759  -0.02603 0.02668  52   THR A O     
419  C CB    . THR A 52  ? 0.27232 0.34850 0.24293 0.01500  -0.03470 0.03489  52   THR A CB    
420  O OG1   . THR A 52  ? 0.28256 0.36553 0.25449 0.01234  -0.03522 0.02998  52   THR A OG1   
421  C CG2   . THR A 52  ? 0.31628 0.39386 0.28046 0.01691  -0.03780 0.03947  52   THR A CG2   
422  N N     . PHE A 53  ? 0.22732 0.29124 0.20670 0.01280  -0.02701 0.03103  53   PHE A N     
423  C CA    . PHE A 53  ? 0.22760 0.29092 0.21231 0.01145  -0.02461 0.02713  53   PHE A CA    
424  C C     . PHE A 53  ? 0.22754 0.29906 0.21599 0.01042  -0.02582 0.02328  53   PHE A C     
425  O O     . PHE A 53  ? 0.22339 0.29546 0.21383 0.00764  -0.02366 0.01963  53   PHE A O     
426  C CB    . PHE A 53  ? 0.24892 0.30758 0.23809 0.01440  -0.02422 0.02839  53   PHE A CB    
427  C CG    . PHE A 53  ? 0.22785 0.28555 0.22175 0.01332  -0.02169 0.02479  53   PHE A CG    
428  C CD1   . PHE A 53  ? 0.24735 0.29990 0.23983 0.01054  -0.01865 0.02355  53   PHE A CD1   
429  C CD2   . PHE A 53  ? 0.26798 0.33024 0.26774 0.01521  -0.02233 0.02285  53   PHE A CD2   
430  C CE1   . PHE A 53  ? 0.24061 0.29217 0.23684 0.00966  -0.01650 0.02057  53   PHE A CE1   
431  C CE2   . PHE A 53  ? 0.26208 0.32353 0.26555 0.01422  -0.01981 0.01984  53   PHE A CE2   
432  C CZ    . PHE A 53  ? 0.26483 0.32068 0.26620 0.01144  -0.01700 0.01877  53   PHE A CZ    
433  N N     . GLU A 54  ? 0.21552 0.29356 0.20517 0.01254  -0.02940 0.02422  54   GLU A N     
434  C CA    . GLU A 54  ? 0.21382 0.30054 0.20750 0.01124  -0.03097 0.02074  54   GLU A CA    
435  C C     . GLU A 54  ? 0.21177 0.30031 0.20104 0.00701  -0.03053 0.01781  54   GLU A C     
436  O O     . GLU A 54  ? 0.20169 0.29334 0.19422 0.00421  -0.02962 0.01386  54   GLU A O     
437  C CB    . GLU A 54  ? 0.23847 0.33216 0.23407 0.01452  -0.03535 0.02277  54   GLU A CB    
438  C CG    . GLU A 54  ? 0.27079 0.36459 0.27275 0.01895  -0.03588 0.02444  54   GLU A CG    
439  C CD    . GLU A 54  ? 0.29638 0.38239 0.29504 0.02236  -0.03609 0.02910  54   GLU A CD    
440  O OE1   . GLU A 54  ? 0.32733 0.40890 0.31889 0.02121  -0.03603 0.03151  54   GLU A OE1   
441  O OE2   . GLU A 54  ? 0.34831 0.43253 0.35149 0.02618  -0.03621 0.03033  54   GLU A OE2   
442  N N     . ASP A 55  ? 0.21484 0.30122 0.19649 0.00654  -0.03105 0.01970  55   ASP A N     
443  C CA    . ASP A 55  ? 0.22455 0.31182 0.20108 0.00291  -0.03034 0.01673  55   ASP A CA    
444  C C     . ASP A 55  ? 0.20753 0.28949 0.18497 0.00014  -0.02607 0.01393  55   ASP A C     
445  O O     . ASP A 55  ? 0.21202 0.29570 0.18954 -0.00294 -0.02537 0.00986  55   ASP A O     
446  C CB    . ASP A 55  ? 0.27214 0.35763 0.23992 0.00344  -0.03108 0.01980  55   ASP A CB    
447  C CG    . ASP A 55  ? 0.29818 0.38528 0.25986 0.00026  -0.03071 0.01650  55   ASP A CG    
448  O OD1   . ASP A 55  ? 0.39477 0.48559 0.35911 -0.00219 -0.03124 0.01195  55   ASP A OD1   
449  O OD2   . ASP A 55  ? 0.39258 0.47706 0.34674 0.00016  -0.02976 0.01844  55   ASP A OD2   
450  N N     . ILE A 56  ? 0.18970 0.26501 0.16797 0.00120  -0.02340 0.01605  56   ILE A N     
451  C CA    . ILE A 56  ? 0.17628 0.24650 0.15507 -0.00112 -0.01959 0.01392  56   ILE A CA    
452  C C     . ILE A 56  ? 0.16833 0.24033 0.15366 -0.00233 -0.01874 0.01058  56   ILE A C     
453  O O     . ILE A 56  ? 0.15632 0.22773 0.14176 -0.00520 -0.01698 0.00728  56   ILE A O     
454  C CB    . ILE A 56  ? 0.16214 0.22529 0.14022 0.00021  -0.01746 0.01723  56   ILE A CB    
455  C CG1   . ILE A 56  ? 0.20948 0.27088 0.18078 0.00055  -0.01759 0.02049  56   ILE A CG1   
456  C CG2   . ILE A 56  ? 0.16992 0.22849 0.14979 -0.00178 -0.01396 0.01512  56   ILE A CG2   
457  C CD1   . ILE A 56  ? 0.20725 0.26290 0.17843 0.00229  -0.01682 0.02479  56   ILE A CD1   
458  N N     . ILE A 57  ? 0.16775 0.24183 0.15854 -0.00004 -0.01980 0.01149  57   ILE A N     
459  C CA    . ILE A 57  ? 0.18181 0.25808 0.17878 -0.00109 -0.01865 0.00871  57   ILE A CA    
460  C C     . ILE A 57  ? 0.16989 0.25291 0.16841 -0.00376 -0.02020 0.00547  57   ILE A C     
461  O O     . ILE A 57  ? 0.17937 0.26263 0.18076 -0.00647 -0.01846 0.00256  57   ILE A O     
462  C CB    . ILE A 57  ? 0.23435 0.31200 0.23658 0.00238  -0.01933 0.01035  57   ILE A CB    
463  C CG1   . ILE A 57  ? 0.28209 0.35176 0.28302 0.00424  -0.01745 0.01265  57   ILE A CG1   
464  C CG2   . ILE A 57  ? 0.24600 0.32783 0.25467 0.00133  -0.01825 0.00761  57   ILE A CG2   
465  C CD1   . ILE A 57  ? 0.29339 0.35836 0.29513 0.00216  -0.01409 0.01075  57   ILE A CD1   
466  N N     . ASN A 58  ? 0.16821 0.25662 0.16474 -0.00320 -0.02363 0.00600  58   ASN A N     
467  C CA    . ASN A 58  ? 0.18326 0.27777 0.18048 -0.00621 -0.02551 0.00265  58   ASN A CA    
468  C C     . ASN A 58  ? 0.17827 0.26840 0.17094 -0.00982 -0.02339 -0.00031 58   ASN A C     
469  O O     . ASN A 58  ? 0.17575 0.26749 0.17102 -0.01307 -0.02293 -0.00382 58   ASN A O     
470  C CB    . ASN A 58  ? 0.21107 0.31159 0.20560 -0.00479 -0.02987 0.00397  58   ASN A CB    
471  C CG    . ASN A 58  ? 0.26970 0.37752 0.26588 -0.00785 -0.03254 0.00038  58   ASN A CG    
472  O OD1   . ASN A 58  ? 0.32064 0.43349 0.32417 -0.00907 -0.03282 -0.00144 58   ASN A OD1   
473  N ND2   . ASN A 58  ? 0.29408 0.40256 0.28337 -0.00931 -0.03443 -0.00077 58   ASN A ND2   
474  N N     . ASP A 59  ? 0.15000 0.23445 0.13613 -0.00928 -0.02194 0.00114  59   ASP A N     
475  C CA    . ASP A 59  ? 0.16507 0.24505 0.14704 -0.01205 -0.01953 -0.00159 59   ASP A CA    
476  C C     . ASP A 59  ? 0.17503 0.25044 0.16110 -0.01350 -0.01612 -0.00307 59   ASP A C     
477  O O     . ASP A 59  ? 0.16937 0.24299 0.15489 -0.01635 -0.01481 -0.00641 59   ASP A O     
478  C CB    . ASP A 59  ? 0.18039 0.25605 0.15524 -0.01080 -0.01833 0.00075  59   ASP A CB    
479  C CG    . ASP A 59  ? 0.24121 0.32087 0.20981 -0.01046 -0.02125 0.00109  59   ASP A CG    
480  O OD1   . ASP A 59  ? 0.21713 0.30260 0.18665 -0.01169 -0.02431 -0.00127 59   ASP A OD1   
481  O OD2   . ASP A 59  ? 0.21702 0.29426 0.17978 -0.00911 -0.02055 0.00383  59   ASP A OD2   
482  N N     . VAL A 60  ? 0.16655 0.23966 0.15637 -0.01151 -0.01473 -0.00069 60   VAL A N     
483  C CA    . VAL A 60  ? 0.16812 0.23729 0.16147 -0.01274 -0.01175 -0.00188 60   VAL A CA    
484  C C     . VAL A 60  ? 0.17489 0.24803 0.17286 -0.01545 -0.01212 -0.00497 60   VAL A C     
485  O O     . VAL A 60  ? 0.16912 0.23902 0.16754 -0.01801 -0.01008 -0.00722 60   VAL A O     
486  C CB    . VAL A 60  ? 0.17488 0.24168 0.17121 -0.01001 -0.01075 0.00093  60   VAL A CB    
487  C CG1   . VAL A 60  ? 0.16967 0.23363 0.16965 -0.01126 -0.00810 -0.00036 60   VAL A CG1   
488  C CG2   . VAL A 60  ? 0.17879 0.24046 0.17086 -0.00823 -0.00997 0.00380  60   VAL A CG2   
489  N N     . GLU A 61  ? 0.16155 0.24186 0.16327 -0.01499 -0.01479 -0.00495 61   GLU A N     
490  C CA    . GLU A 61  ? 0.19071 0.27577 0.19777 -0.01785 -0.01519 -0.00759 61   GLU A CA    
491  C C     . GLU A 61  ? 0.20175 0.28759 0.20598 -0.02144 -0.01647 -0.01103 61   GLU A C     
492  O O     . GLU A 61  ? 0.19327 0.27840 0.20007 -0.02484 -0.01537 -0.01367 61   GLU A O     
493  C CB    . GLU A 61  ? 0.20050 0.29397 0.21310 -0.01607 -0.01774 -0.00648 61   GLU A CB    
494  C CG    . GLU A 61  ? 0.30560 0.39943 0.32363 -0.01395 -0.01576 -0.00486 61   GLU A CG    
495  C CD    . GLU A 61  ? 0.31364 0.40677 0.33571 -0.01705 -0.01299 -0.00675 61   GLU A CD    
496  O OE1   . GLU A 61  ? 0.38782 0.48610 0.41346 -0.02033 -0.01396 -0.00897 61   GLU A OE1   
497  O OE2   . GLU A 61  ? 0.34743 0.43483 0.36903 -0.01634 -0.00997 -0.00591 61   GLU A OE2   
498  N N     . LYS A 62  ? 0.18941 0.27629 0.18798 -0.02078 -0.01876 -0.01106 62   LYS A N     
499  C CA    . LYS A 62  ? 0.17030 0.25913 0.16597 -0.02393 -0.02076 -0.01469 62   LYS A CA    
500  C C     . LYS A 62  ? 0.21351 0.29480 0.20349 -0.02565 -0.01831 -0.01704 62   LYS A C     
501  O O     . LYS A 62  ? 0.21364 0.29432 0.20332 -0.02909 -0.01867 -0.02091 62   LYS A O     
502  C CB    . LYS A 62  ? 0.21516 0.30954 0.20697 -0.02235 -0.02475 -0.01380 62   LYS A CB    
503  C CG    . LYS A 62  ? 0.25906 0.36210 0.25706 -0.02078 -0.02787 -0.01206 62   LYS A CG    
504  C CD    . LYS A 62  ? 0.32047 0.43111 0.31874 -0.02312 -0.03221 -0.01473 62   LYS A CD    
505  C CE    . LYS A 62  ? 0.36350 0.48267 0.37147 -0.02367 -0.03397 -0.01475 62   LYS A CE    
506  N NZ    . LYS A 62  ? 0.35530 0.47772 0.36671 -0.02883 -0.03512 -0.01910 62   LYS A NZ    
507  N N     . ILE A 63  ? 0.17423 0.24982 0.16000 -0.02337 -0.01586 -0.01493 63   ILE A N     
508  C CA    . ILE A 63  ? 0.17512 0.24431 0.15575 -0.02447 -0.01345 -0.01710 63   ILE A CA    
509  C C     . ILE A 63  ? 0.19524 0.25779 0.17763 -0.02383 -0.00956 -0.01588 63   ILE A C     
510  O O     . ILE A 63  ? 0.17988 0.23723 0.16025 -0.02517 -0.00741 -0.01821 63   ILE A O     
511  C CB    . ILE A 63  ? 0.26631 0.33538 0.23902 -0.02272 -0.01408 -0.01627 63   ILE A CB    
512  C CG1   . ILE A 63  ? 0.26169 0.33055 0.23385 -0.01925 -0.01358 -0.01129 63   ILE A CG1   
513  C CG2   . ILE A 63  ? 0.25445 0.32978 0.22426 -0.02370 -0.01818 -0.01810 63   ILE A CG2   
514  C CD1   . ILE A 63  ? 0.33335 0.40121 0.29781 -0.01768 -0.01326 -0.00977 63   ILE A CD1   
515  N N     . ILE A 64  ? 0.16101 0.22326 0.14699 -0.02171 -0.00864 -0.01247 64   ILE A N     
516  C CA    . ILE A 64  ? 0.15119 0.20744 0.13864 -0.02124 -0.00536 -0.01145 64   ILE A CA    
517  C C     . ILE A 64  ? 0.16419 0.21976 0.15695 -0.02342 -0.00436 -0.01290 64   ILE A C     
518  O O     . ILE A 64  ? 0.16176 0.21224 0.15435 -0.02488 -0.00222 -0.01444 64   ILE A O     
519  C CB    . ILE A 64  ? 0.16403 0.21940 0.15213 -0.01814 -0.00484 -0.00738 64   ILE A CB    
520  C CG1   . ILE A 64  ? 0.16115 0.21679 0.14394 -0.01632 -0.00557 -0.00545 64   ILE A CG1   
521  C CG2   . ILE A 64  ? 0.16921 0.21878 0.15888 -0.01783 -0.00187 -0.00651 64   ILE A CG2   
522  C CD1   . ILE A 64  ? 0.19573 0.24752 0.17369 -0.01693 -0.00351 -0.00677 64   ILE A CD1   
523  N N     . MET A 65  ? 0.14279 0.20352 0.14041 -0.02350 -0.00576 -0.01221 65   MET A N     
524  C CA    . MET A 65  ? 0.16638 0.22729 0.16925 -0.02563 -0.00455 -0.01309 65   MET A CA    
525  C C     . MET A 65  ? 0.20035 0.25934 0.20324 -0.02950 -0.00428 -0.01659 65   MET A C     
526  O O     . MET A 65  ? 0.15465 0.20953 0.15963 -0.03103 -0.00202 -0.01687 65   MET A O     
527  C CB    . MET A 65  ? 0.20129 0.26975 0.20945 -0.02507 -0.00628 -0.01208 65   MET A CB    
528  C CG    . MET A 65  ? 0.18873 0.25731 0.19842 -0.02148 -0.00554 -0.00887 65   MET A CG    
529  S SD    . MET A 65  ? 0.20340 0.26518 0.21384 -0.02128 -0.00182 -0.00781 65   MET A SD    
530  C CE    . MET A 65  ? 0.25501 0.31638 0.26523 -0.01679 -0.00195 -0.00459 65   MET A CE    
531  N N     . PRO A 66  ? 0.16087 0.22216 0.16135 -0.03126 -0.00653 -0.01932 66   PRO A N     
532  C CA    . PRO A 66  ? 0.18681 0.24478 0.18700 -0.03503 -0.00619 -0.02300 66   PRO A CA    
533  C C     . PRO A 66  ? 0.20170 0.25081 0.19859 -0.03480 -0.00323 -0.02366 66   PRO A C     
534  O O     . PRO A 66  ? 0.22358 0.26847 0.22143 -0.03765 -0.00228 -0.02601 66   PRO A O     
535  C CB    . PRO A 66  ? 0.19693 0.25868 0.19342 -0.03605 -0.00941 -0.02571 66   PRO A CB    
536  C CG    . PRO A 66  ? 0.18999 0.25995 0.18898 -0.03417 -0.01195 -0.02332 66   PRO A CG    
537  C CD    . PRO A 66  ? 0.18842 0.25582 0.18675 -0.03025 -0.00986 -0.01938 66   PRO A CD    
538  N N     . GLY A 67  ? 0.17530 0.22148 0.16874 -0.03155 -0.00180 -0.02157 67   GLY A N     
539  C CA    . GLY A 67  ? 0.18986 0.22855 0.18072 -0.03094 0.00091  -0.02207 67   GLY A CA    
540  C C     . GLY A 67  ? 0.17734 0.21297 0.17077 -0.02922 0.00318  -0.01886 67   GLY A C     
541  O O     . GLY A 67  ? 0.19183 0.22242 0.18332 -0.02770 0.00519  -0.01823 67   GLY A O     
542  N N     . VAL A 68  ? 0.16501 0.20399 0.16282 -0.02937 0.00284  -0.01693 68   VAL A N     
543  C CA    . VAL A 68  ? 0.18359 0.22017 0.18347 -0.02780 0.00469  -0.01406 68   VAL A CA    
544  C C     . VAL A 68  ? 0.18209 0.21540 0.18484 -0.03026 0.00624  -0.01463 68   VAL A C     
545  O O     . VAL A 68  ? 0.20312 0.23937 0.20887 -0.03306 0.00552  -0.01595 68   VAL A O     
546  C CB    . VAL A 68  ? 0.18910 0.23099 0.19140 -0.02594 0.00363  -0.01159 68   VAL A CB    
547  C CG1   . VAL A 68  ? 0.17374 0.21337 0.17830 -0.02503 0.00547  -0.00942 68   VAL A CG1   
548  C CG2   . VAL A 68  ? 0.19330 0.23647 0.19246 -0.02314 0.00252  -0.01010 68   VAL A CG2   
549  N N     . THR A 69  ? 0.17827 0.20565 0.18024 -0.02934 0.00830  -0.01346 69   THR A N     
550  C CA    . THR A 69  ? 0.19658 0.22070 0.20099 -0.03098 0.00993  -0.01273 69   THR A CA    
551  C C     . THR A 69  ? 0.22293 0.24965 0.22927 -0.02936 0.01043  -0.00980 69   THR A C     
552  O O     . THR A 69  ? 0.20182 0.22722 0.20656 -0.02657 0.01070  -0.00798 69   THR A O     
553  C CB    . THR A 69  ? 0.20672 0.22321 0.20914 -0.03041 0.01163  -0.01275 69   THR A CB    
554  O OG1   . THR A 69  ? 0.21151 0.22519 0.21201 -0.03177 0.01135  -0.01595 69   THR A OG1   
555  C CG2   . THR A 69  ? 0.23839 0.25127 0.24287 -0.03185 0.01323  -0.01129 69   THR A CG2   
556  N N     . HIS A 70  ? 0.17889 0.20949 0.18871 -0.03115 0.01058  -0.00950 70   HIS A N     
557  C CA    . HIS A 70  ? 0.18170 0.21586 0.19323 -0.02938 0.01102  -0.00727 70   HIS A CA    
558  C C     . HIS A 70  ? 0.18971 0.21908 0.20062 -0.02912 0.01317  -0.00534 70   HIS A C     
559  O O     . HIS A 70  ? 0.18716 0.21656 0.20010 -0.03135 0.01459  -0.00484 70   HIS A O     
560  C CB    . HIS A 70  ? 0.17194 0.21348 0.18775 -0.03103 0.01040  -0.00780 70   HIS A CB    
561  C CG    . HIS A 70  ? 0.18074 0.22724 0.19702 -0.03130 0.00784  -0.00962 70   HIS A CG    
562  N ND1   . HIS A 70  ? 0.20188 0.25277 0.21792 -0.02837 0.00620  -0.00884 70   HIS A ND1   
563  C CD2   . HIS A 70  ? 0.20034 0.24779 0.21689 -0.03409 0.00646  -0.01216 70   HIS A CD2   
564  C CE1   . HIS A 70  ? 0.21360 0.26833 0.22964 -0.02925 0.00388  -0.01054 70   HIS A CE1   
565  N NE2   . HIS A 70  ? 0.17481 0.22771 0.19106 -0.03277 0.00393  -0.01277 70   HIS A NE2   
566  N N     . TRP A 71  ? 0.17185 0.19735 0.17991 -0.02645 0.01332  -0.00405 71   TRP A N     
567  C CA    . TRP A 71  ? 0.17906 0.20002 0.18585 -0.02574 0.01483  -0.00211 71   TRP A CA    
568  C C     . TRP A 71  ? 0.17336 0.19742 0.18138 -0.02547 0.01584  -0.00066 71   TRP A C     
569  O O     . TRP A 71  ? 0.18645 0.20739 0.19349 -0.02581 0.01734  0.00089  71   TRP A O     
570  C CB    . TRP A 71  ? 0.19828 0.21611 0.20243 -0.02286 0.01424  -0.00113 71   TRP A CB    
571  C CG    . TRP A 71  ? 0.22712 0.24061 0.22989 -0.02290 0.01425  -0.00198 71   TRP A CG    
572  C CD1   . TRP A 71  ? 0.24519 0.25949 0.24748 -0.02329 0.01350  -0.00394 71   TRP A CD1   
573  C CD2   . TRP A 71  ? 0.24069 0.24862 0.24225 -0.02218 0.01509  -0.00092 71   TRP A CD2   
574  N NE1   . TRP A 71  ? 0.23187 0.24141 0.23280 -0.02279 0.01414  -0.00438 71   TRP A NE1   
575  C CE2   . TRP A 71  ? 0.25680 0.26247 0.25764 -0.02202 0.01505  -0.00246 71   TRP A CE2   
576  C CE3   . TRP A 71  ? 0.21958 0.22442 0.22045 -0.02148 0.01580  0.00120  71   TRP A CE3   
577  C CZ2   . TRP A 71  ? 0.26279 0.26342 0.26295 -0.02097 0.01579  -0.00195 71   TRP A CZ2   
578  C CZ3   . TRP A 71  ? 0.24602 0.24585 0.24605 -0.02058 0.01619  0.00193  71   TRP A CZ3   
579  C CH2   . TRP A 71  ? 0.25648 0.25434 0.25653 -0.02024 0.01623  0.00036  71   TRP A CH2   
580  N N     . HIS A 72  ? 0.15536 0.18557 0.16534 -0.02466 0.01511  -0.00106 72   HIS A N     
581  C CA    . HIS A 72  ? 0.15107 0.18465 0.16207 -0.02367 0.01624  0.00004  72   HIS A CA    
582  C C     . HIS A 72  ? 0.16928 0.20865 0.18446 -0.02617 0.01725  -0.00045 72   HIS A C     
583  O O     . HIS A 72  ? 0.15386 0.19729 0.17048 -0.02531 0.01851  0.00029  72   HIS A O     
584  C CB    . HIS A 72  ? 0.18145 0.21735 0.19180 -0.02022 0.01486  0.00014  72   HIS A CB    
585  C CG    . HIS A 72  ? 0.21490 0.24564 0.22188 -0.01828 0.01376  0.00069  72   HIS A CG    
586  N ND1   . HIS A 72  ? 0.21985 0.24553 0.22411 -0.01766 0.01449  0.00190  72   HIS A ND1   
587  C CD2   . HIS A 72  ? 0.23443 0.26470 0.24052 -0.01700 0.01200  0.00038  72   HIS A CD2   
588  C CE1   . HIS A 72  ? 0.23304 0.25571 0.23551 -0.01618 0.01317  0.00218  72   HIS A CE1   
589  N NE2   . HIS A 72  ? 0.30475 0.33004 0.30822 -0.01580 0.01184  0.00137  72   HIS A NE2   
590  N N     . SER A 73  ? 0.15178 0.19170 0.16900 -0.02929 0.01676  -0.00180 73   SER A N     
591  C CA    . SER A 73  ? 0.14489 0.18926 0.16636 -0.03262 0.01797  -0.00199 73   SER A CA    
592  C C     . SER A 73  ? 0.15098 0.19151 0.17146 -0.03413 0.02072  0.00000  73   SER A C     
593  O O     . SER A 73  ? 0.13776 0.17090 0.15472 -0.03403 0.02112  0.00082  73   SER A O     
594  C CB    . SER A 73  ? 0.17924 0.22388 0.20265 -0.03600 0.01657  -0.00413 73   SER A CB    
595  O OG    . SER A 73  ? 0.17949 0.22567 0.20652 -0.04013 0.01803  -0.00403 73   SER A OG    
596  N N     . PRO A 74  ? 0.14485 0.19061 0.16838 -0.03532 0.02270  0.00102  74   PRO A N     
597  C CA    . PRO A 74  ? 0.16398 0.20660 0.18646 -0.03719 0.02555  0.00328  74   PRO A CA    
598  C C     . PRO A 74  ? 0.17743 0.21436 0.20029 -0.04128 0.02590  0.00335  74   PRO A C     
599  O O     . PRO A 74  ? 0.18341 0.21531 0.20409 -0.04239 0.02789  0.00561  74   PRO A O     
600  C CB    . PRO A 74  ? 0.18675 0.23813 0.21370 -0.03811 0.02761  0.00393  74   PRO A CB    
601  C CG    . PRO A 74  ? 0.26596 0.32449 0.29594 -0.03583 0.02556  0.00204  74   PRO A CG    
602  C CD    . PRO A 74  ? 0.19260 0.24783 0.22092 -0.03496 0.02239  0.00022  74   PRO A CD    
603  N N     . TYR A 75  ? 0.14860 0.18565 0.17366 -0.04337 0.02393  0.00094  75   TYR A N     
604  C CA    . TYR A 75  ? 0.16237 0.19330 0.18772 -0.04717 0.02400  0.00037  75   TYR A CA    
605  C C     . TYR A 75  ? 0.18111 0.20358 0.20195 -0.04531 0.02268  -0.00052 75   TYR A C     
606  O O     . TYR A 75  ? 0.17217 0.18882 0.19288 -0.04783 0.02245  -0.00162 75   TYR A O     
607  C CB    . TYR A 75  ? 0.17723 0.21329 0.20765 -0.05097 0.02260  -0.00216 75   TYR A CB    
608  C CG    . TYR A 75  ? 0.18863 0.23358 0.22465 -0.05329 0.02415  -0.00111 75   TYR A CG    
609  C CD1   . TYR A 75  ? 0.18142 0.22510 0.21893 -0.05640 0.02711  0.00142  75   TYR A CD1   
610  C CD2   . TYR A 75  ? 0.20270 0.25760 0.24266 -0.05219 0.02276  -0.00238 75   TYR A CD2   
611  C CE1   . TYR A 75  ? 0.21599 0.26850 0.25898 -0.05858 0.02894  0.00254  75   TYR A CE1   
612  C CE2   . TYR A 75  ? 0.22289 0.28674 0.26867 -0.05402 0.02436  -0.00142 75   TYR A CE2   
613  C CZ    . TYR A 75  ? 0.23302 0.29590 0.28041 -0.05730 0.02759  0.00099  75   TYR A CZ    
614  O OH    . TYR A 75  ? 0.26910 0.34163 0.32265 -0.05919 0.02958  0.00208  75   TYR A OH    
615  N N     . PHE A 76  ? 0.15304 0.17474 0.17047 -0.04098 0.02188  -0.00014 76   PHE A N     
616  C CA    . PHE A 76  ? 0.16213 0.17656 0.17567 -0.03886 0.02107  -0.00042 76   PHE A CA    
617  C C     . PHE A 76  ? 0.17429 0.18272 0.18517 -0.03819 0.02281  0.00256  76   PHE A C     
618  O O     . PHE A 76  ? 0.17953 0.18955 0.18869 -0.03594 0.02348  0.00454  76   PHE A O     
619  C CB    . PHE A 76  ? 0.16059 0.17742 0.17226 -0.03497 0.01939  -0.00109 76   PHE A CB    
620  C CG    . PHE A 76  ? 0.14967 0.16045 0.15818 -0.03287 0.01865  -0.00144 76   PHE A CG    
621  C CD1   . PHE A 76  ? 0.17340 0.18300 0.18160 -0.03330 0.01743  -0.00403 76   PHE A CD1   
622  C CD2   . PHE A 76  ? 0.17477 0.18154 0.18063 -0.03042 0.01917  0.00073  76   PHE A CD2   
623  C CE1   . PHE A 76  ? 0.20451 0.20928 0.21016 -0.03117 0.01715  -0.00437 76   PHE A CE1   
624  C CE2   . PHE A 76  ? 0.18866 0.19082 0.19250 -0.02843 0.01855  0.00050  76   PHE A CE2   
625  C CZ    . PHE A 76  ? 0.19235 0.19364 0.19626 -0.02874 0.01774  -0.00202 76   PHE A CZ    
626  N N     . PHE A 77  ? 0.16202 0.16336 0.17234 -0.04008 0.02342  0.00283  77   PHE A N     
627  C CA    . PHE A 77  ? 0.18787 0.18297 0.19556 -0.03946 0.02483  0.00596  77   PHE A CA    
628  C C     . PHE A 77  ? 0.20488 0.19239 0.21023 -0.03745 0.02398  0.00559  77   PHE A C     
629  O O     . PHE A 77  ? 0.23279 0.21344 0.23692 -0.03794 0.02488  0.00750  77   PHE A O     
630  C CB    . PHE A 77  ? 0.19815 0.19126 0.20759 -0.04359 0.02682  0.00768  77   PHE A CB    
631  C CG    . PHE A 77  ? 0.18397 0.18519 0.19631 -0.04562 0.02814  0.00833  77   PHE A CG    
632  C CD1   . PHE A 77  ? 0.19625 0.20105 0.20675 -0.04364 0.02947  0.01075  77   PHE A CD1   
633  C CD2   . PHE A 77  ? 0.20758 0.21304 0.22462 -0.04950 0.02807  0.00641  77   PHE A CD2   
634  C CE1   . PHE A 77  ? 0.18239 0.19505 0.19580 -0.04516 0.03106  0.01124  77   PHE A CE1   
635  C CE2   . PHE A 77  ? 0.18822 0.20202 0.20879 -0.05124 0.02941  0.00710  77   PHE A CE2   
636  C CZ    . PHE A 77  ? 0.19799 0.21545 0.21681 -0.04892 0.03110  0.00955  77   PHE A CZ    
637  N N     . ALA A 78  ? 0.18395 0.17280 0.18877 -0.03503 0.02236  0.00338  78   ALA A N     
638  C CA    . ALA A 78  ? 0.22593 0.20893 0.22929 -0.03306 0.02173  0.00245  78   ALA A CA    
639  C C     . ALA A 78  ? 0.21666 0.19949 0.21787 -0.02906 0.02109  0.00423  78   ALA A C     
640  O O     . ALA A 78  ? 0.27519 0.26296 0.27585 -0.02767 0.02060  0.00510  78   ALA A O     
641  C CB    . ALA A 78  ? 0.22786 0.21257 0.23199 -0.03338 0.02057  -0.00138 78   ALA A CB    
642  N N     . TYR A 79  ? 0.28336 0.26038 0.28364 -0.02720 0.02102  0.00463  79   TYR A N     
643  C CA    . TYR A 79  ? 0.24361 0.22029 0.24259 -0.02357 0.02019  0.00620  79   TYR A CA    
644  C C     . TYR A 79  ? 0.23364 0.21206 0.23097 -0.02286 0.02011  0.00926  79   TYR A C     
645  O O     . TYR A 79  ? 0.25559 0.23052 0.25176 -0.02375 0.02100  0.01170  79   TYR A O     
646  C CB    . TYR A 79  ? 0.22770 0.20899 0.22713 -0.02182 0.01908  0.00414  79   TYR A CB    
647  C CG    . TYR A 79  ? 0.28274 0.26352 0.28295 -0.02269 0.01920  0.00077  79   TYR A CG    
648  C CD1   . TYR A 79  ? 0.31520 0.29109 0.31538 -0.02130 0.01964  -0.00030 79   TYR A CD1   
649  C CD2   . TYR A 79  ? 0.28824 0.27363 0.28904 -0.02467 0.01880  -0.00146 79   TYR A CD2   
650  C CE1   . TYR A 79  ? 0.30738 0.28260 0.30750 -0.02197 0.01984  -0.00377 79   TYR A CE1   
651  C CE2   . TYR A 79  ? 0.28511 0.27011 0.28586 -0.02551 0.01866  -0.00472 79   TYR A CE2   
652  C CZ    . TYR A 79  ? 0.31952 0.29927 0.31962 -0.02419 0.01926  -0.00599 79   TYR A CZ    
653  O OH    . TYR A 79  ? 0.30922 0.28841 0.30854 -0.02490 0.01920  -0.00960 79   TYR A OH    
654  N N     . PHE A 80  ? 0.25279 0.23621 0.24965 -0.02127 0.01906  0.00915  80   PHE A N     
655  C CA    . PHE A 80  ? 0.23608 0.22174 0.23095 -0.02050 0.01884  0.01120  80   PHE A CA    
656  C C     . PHE A 80  ? 0.20816 0.20005 0.20372 -0.02061 0.01841  0.00961  80   PHE A C     
657  O O     . PHE A 80  ? 0.24742 0.24168 0.24468 -0.02068 0.01783  0.00743  80   PHE A O     
658  C CB    . PHE A 80  ? 0.22354 0.20761 0.21684 -0.01762 0.01739  0.01292  80   PHE A CB    
659  C CG    . PHE A 80  ? 0.22598 0.20460 0.21777 -0.01713 0.01765  0.01558  80   PHE A CG    
660  C CD1   . PHE A 80  ? 0.20713 0.18358 0.19723 -0.01900 0.01914  0.01747  80   PHE A CD1   
661  C CD2   . PHE A 80  ? 0.26259 0.23855 0.25481 -0.01471 0.01643  0.01647  80   PHE A CD2   
662  C CE1   . PHE A 80  ? 0.21385 0.18487 0.20218 -0.01844 0.01928  0.02038  80   PHE A CE1   
663  C CE2   . PHE A 80  ? 0.22962 0.20057 0.22053 -0.01388 0.01640  0.01919  80   PHE A CE2   
664  C CZ    . PHE A 80  ? 0.21854 0.18667 0.20721 -0.01573 0.01776  0.02124  80   PHE A CZ    
665  N N     . PRO A 81  ? 0.18333 0.17789 0.17736 -0.02045 0.01874  0.01067  81   PRO A N     
666  C CA    . PRO A 81  ? 0.17481 0.17491 0.16960 -0.01993 0.01825  0.00921  81   PRO A CA    
667  C C     . PRO A 81  ? 0.22578 0.22656 0.22060 -0.01771 0.01631  0.00838  81   PRO A C     
668  O O     . PRO A 81  ? 0.20293 0.20088 0.19665 -0.01621 0.01530  0.00939  81   PRO A O     
669  C CB    . PRO A 81  ? 0.20082 0.20232 0.19310 -0.01940 0.01904  0.01065  81   PRO A CB    
670  C CG    . PRO A 81  ? 0.20818 0.20467 0.19766 -0.01922 0.01935  0.01313  81   PRO A CG    
671  C CD    . PRO A 81  ? 0.19351 0.18629 0.18497 -0.02088 0.01991  0.01315  81   PRO A CD    
672  N N     . THR A 82  ? 0.19060 0.19538 0.18699 -0.01759 0.01573  0.00672  82   THR A N     
673  C CA    . THR A 82  ? 0.16980 0.17582 0.16603 -0.01565 0.01405  0.00633  82   THR A CA    
674  C C     . THR A 82  ? 0.18871 0.19817 0.18453 -0.01473 0.01379  0.00599  82   THR A C     
675  O O     . THR A 82  ? 0.19211 0.20471 0.18900 -0.01567 0.01490  0.00544  82   THR A O     
676  C CB    . THR A 82  ? 0.21944 0.22658 0.21736 -0.01587 0.01347  0.00496  82   THR A CB    
677  O OG1   . THR A 82  ? 0.27659 0.28333 0.27422 -0.01418 0.01211  0.00542  82   THR A OG1   
678  C CG2   . THR A 82  ? 0.23261 0.24427 0.23196 -0.01661 0.01340  0.00356  82   THR A CG2   
679  N N     . ALA A 83  ? 0.14328 0.15208 0.13782 -0.01287 0.01234  0.00628  83   ALA A N     
680  C CA    . ALA A 83  ? 0.16729 0.17789 0.16071 -0.01151 0.01210  0.00591  83   ALA A CA    
681  C C     . ALA A 83  ? 0.18788 0.20228 0.18345 -0.01101 0.01167  0.00474  83   ALA A C     
682  O O     . ALA A 83  ? 0.19483 0.20951 0.19161 -0.01095 0.01058  0.00453  83   ALA A O     
683  C CB    . ALA A 83  ? 0.17725 0.18504 0.16844 -0.00990 0.01037  0.00638  83   ALA A CB    
684  N N     . SER A 84  ? 0.17514 0.19277 0.17113 -0.01049 0.01261  0.00414  84   SER A N     
685  C CA    . SER A 84  ? 0.22537 0.24678 0.22340 -0.00930 0.01194  0.00322  84   SER A CA    
686  C C     . SER A 84  ? 0.19996 0.22312 0.19720 -0.00743 0.01275  0.00270  84   SER A C     
687  O O     . SER A 84  ? 0.20381 0.22996 0.20178 -0.00817 0.01475  0.00260  84   SER A O     
688  C CB    . SER A 84  ? 0.24393 0.26959 0.24515 -0.01104 0.01245  0.00261  84   SER A CB    
689  O OG    . SER A 84  ? 0.26053 0.29064 0.26389 -0.00960 0.01177  0.00193  84   SER A OG    
690  N N     . SER A 85  ? 0.16182 0.18301 0.15760 -0.00507 0.01135  0.00233  85   SER A N     
691  C CA    . SER A 85  ? 0.16690 0.18932 0.16171 -0.00272 0.01203  0.00135  85   SER A CA    
692  C C     . SER A 85  ? 0.16582 0.18802 0.16169 -0.00032 0.01021  0.00078  85   SER A C     
693  O O     . SER A 85  ? 0.17204 0.19114 0.16772 -0.00045 0.00824  0.00141  85   SER A O     
694  C CB    . SER A 85  ? 0.17153 0.18982 0.16179 -0.00205 0.01225  0.00126  85   SER A CB    
695  O OG    . SER A 85  ? 0.16201 0.17542 0.15037 -0.00113 0.00983  0.00117  85   SER A OG    
696  N N     . TYR A 86  ? 0.16785 0.19348 0.16506 0.00193  0.01101  -0.00024 86   TYR A N     
697  C CA    . TYR A 86  ? 0.16481 0.18991 0.16311 0.00466  0.00930  -0.00065 86   TYR A CA    
698  C C     . TYR A 86  ? 0.15635 0.17460 0.15109 0.00623  0.00767  -0.00111 86   TYR A C     
699  O O     . TYR A 86  ? 0.15214 0.16772 0.14745 0.00719  0.00560  -0.00060 86   TYR A O     
700  C CB    . TYR A 86  ? 0.18798 0.21871 0.18901 0.00712  0.01067  -0.00171 86   TYR A CB    
701  C CG    . TYR A 86  ? 0.21785 0.25587 0.22326 0.00526  0.01178  -0.00126 86   TYR A CG    
702  C CD1   . TYR A 86  ? 0.19833 0.23812 0.20615 0.00396  0.01004  -0.00038 86   TYR A CD1   
703  C CD2   . TYR A 86  ? 0.22495 0.26812 0.23192 0.00459  0.01452  -0.00173 86   TYR A CD2   
704  C CE1   . TYR A 86  ? 0.20110 0.24737 0.21276 0.00200  0.01065  -0.00033 86   TYR A CE1   
705  C CE2   . TYR A 86  ? 0.20892 0.25874 0.22038 0.00240  0.01531  -0.00139 86   TYR A CE2   
706  C CZ    . TYR A 86  ? 0.25016 0.30137 0.26394 0.00109  0.01318  -0.00087 86   TYR A CZ    
707  O OH    . TYR A 86  ? 0.23389 0.29156 0.25197 -0.00132 0.01359  -0.00088 86   TYR A OH    
708  N N     . PRO A 87  ? 0.15882 0.17395 0.14974 0.00640  0.00833  -0.00200 87   PRO A N     
709  C CA    . PRO A 87  ? 0.16722 0.17558 0.15490 0.00723  0.00621  -0.00255 87   PRO A CA    
710  C C     . PRO A 87  ? 0.15728 0.16255 0.14565 0.00502  0.00411  -0.00088 87   PRO A C     
711  O O     . PRO A 87  ? 0.16933 0.17047 0.15756 0.00571  0.00202  -0.00074 87   PRO A O     
712  C CB    . PRO A 87  ? 0.19166 0.19833 0.17492 0.00701  0.00728  -0.00351 87   PRO A CB    
713  C CG    . PRO A 87  ? 0.20315 0.21546 0.18719 0.00783  0.01030  -0.00408 87   PRO A CG    
714  C CD    . PRO A 87  ? 0.18727 0.20489 0.17639 0.00623  0.01095  -0.00266 87   PRO A CD    
715  N N     . ALA A 88  ? 0.17943 0.18656 0.16871 0.00239  0.00477  0.00044  88   ALA A N     
716  C CA    . ALA A 88  ? 0.16734 0.17236 0.15757 0.00051  0.00323  0.00197  88   ALA A CA    
717  C C     . ALA A 88  ? 0.15914 0.16571 0.15216 0.00077  0.00244  0.00292  88   ALA A C     
718  O O     . ALA A 88  ? 0.15873 0.16247 0.15208 0.00026  0.00082  0.00404  88   ALA A O     
719  C CB    . ALA A 88  ? 0.17097 0.17743 0.16144 -0.00186 0.00435  0.00289  88   ALA A CB    
720  N N     . MET A 89  ? 0.16973 0.18110 0.16481 0.00145  0.00351  0.00267  89   MET A N     
721  C CA    . MET A 89  ? 0.17284 0.18597 0.17003 0.00204  0.00246  0.00364  89   MET A CA    
722  C C     . MET A 89  ? 0.16480 0.17411 0.16147 0.00444  0.00075  0.00376  89   MET A C     
723  O O     . MET A 89  ? 0.17964 0.18720 0.17679 0.00428  -0.00072 0.00536  89   MET A O     
724  C CB    . MET A 89  ? 0.17128 0.19079 0.17100 0.00245  0.00355  0.00314  89   MET A CB    
725  C CG    . MET A 89  ? 0.19681 0.21967 0.19738 -0.00024 0.00507  0.00300  89   MET A CG    
726  S SD    . MET A 89  ? 0.25741 0.28803 0.26170 -0.00029 0.00555  0.00250  89   MET A SD    
727  C CE    . MET A 89  ? 0.27922 0.31176 0.28397 -0.00363 0.00771  0.00193  89   MET A CE    
728  N N     . LEU A 90  ? 0.15301 0.16075 0.14853 0.00672  0.00102  0.00211  90   LEU A N     
729  C CA    . LEU A 90  ? 0.16139 0.16441 0.15623 0.00920  -0.00064 0.00187  90   LEU A CA    
730  C C     . LEU A 90  ? 0.15641 0.15301 0.14957 0.00761  -0.00246 0.00271  90   LEU A C     
731  O O     . LEU A 90  ? 0.17042 0.16354 0.16412 0.00808  -0.00416 0.00404  90   LEU A O     
732  C CB    . LEU A 90  ? 0.15263 0.15505 0.14606 0.01207  0.00032  -0.00061 90   LEU A CB    
733  C CG    . LEU A 90  ? 0.18077 0.18994 0.17680 0.01424  0.00210  -0.00141 90   LEU A CG    
734  C CD1   . LEU A 90  ? 0.20544 0.21479 0.19946 0.01636  0.00392  -0.00391 90   LEU A CD1   
735  C CD2   . LEU A 90  ? 0.20353 0.21341 0.20222 0.01695  0.00071  -0.00054 90   LEU A CD2   
736  N N     . ALA A 91  ? 0.16676 0.16189 0.15810 0.00564  -0.00221 0.00217  91   ALA A N     
737  C CA    . ALA A 91  ? 0.16555 0.15562 0.15607 0.00383  -0.00406 0.00297  91   ALA A CA    
738  C C     . ALA A 91  ? 0.19249 0.18382 0.18533 0.00172  -0.00447 0.00564  91   ALA A C     
739  O O     . ALA A 91  ? 0.19474 0.18225 0.18808 0.00083  -0.00609 0.00699  91   ALA A O     
740  C CB    . ALA A 91  ? 0.17863 0.16798 0.16700 0.00235  -0.00384 0.00200  91   ALA A CB    
741  N N     . ASP A 92  ? 0.17139 0.16801 0.16555 0.00082  -0.00293 0.00636  92   ASP A N     
742  C CA    . ASP A 92  ? 0.19749 0.19566 0.19318 -0.00097 -0.00298 0.00856  92   ASP A CA    
743  C C     . ASP A 92  ? 0.22831 0.22572 0.22469 0.00019  -0.00403 0.01017  92   ASP A C     
744  O O     . ASP A 92  ? 0.20427 0.20062 0.20120 -0.00118 -0.00462 0.01235  92   ASP A O     
745  C CB    . ASP A 92  ? 0.20932 0.21276 0.20574 -0.00200 -0.00117 0.00839  92   ASP A CB    
746  C CG    . ASP A 92  ? 0.32777 0.33159 0.32475 -0.00432 -0.00068 0.00944  92   ASP A CG    
747  O OD1   . ASP A 92  ? 0.40590 0.41282 0.40320 -0.00522 0.00077  0.00897  92   ASP A OD1   
748  O OD2   . ASP A 92  ? 0.36104 0.36204 0.35841 -0.00523 -0.00171 0.01065  92   ASP A OD2   
749  N N     . MET A 93  ? 0.18259 0.18074 0.17902 0.00282  -0.00421 0.00933  93   MET A N     
750  C CA    . MET A 93  ? 0.18951 0.18609 0.18642 0.00444  -0.00557 0.01105  93   MET A CA    
751  C C     . MET A 93  ? 0.20992 0.19927 0.20615 0.00428  -0.00728 0.01193  93   MET A C     
752  O O     . MET A 93  ? 0.20017 0.18745 0.19674 0.00359  -0.00826 0.01459  93   MET A O     
753  C CB    . MET A 93  ? 0.19371 0.19268 0.19135 0.00776  -0.00549 0.00979  93   MET A CB    
754  C CG    . MET A 93  ? 0.17112 0.17772 0.17019 0.00763  -0.00417 0.00924  93   MET A CG    
755  S SD    . MET A 93  ? 0.25781 0.26843 0.25873 0.01129  -0.00359 0.00723  93   MET A SD    
756  C CE    . MET A 93  ? 0.21715 0.22583 0.21891 0.01444  -0.00587 0.00933  93   MET A CE    
757  N N     . LEU A 94  ? 0.19088 0.17622 0.18595 0.00472  -0.00770 0.00975  94   LEU A N     
758  C CA    . LEU A 94  ? 0.19634 0.17442 0.19081 0.00407  -0.00961 0.01010  94   LEU A CA    
759  C C     . LEU A 94  ? 0.23016 0.20780 0.22563 0.00039  -0.00995 0.01210  94   LEU A C     
760  O O     . LEU A 94  ? 0.23501 0.20835 0.23123 -0.00085 -0.01133 0.01412  94   LEU A O     
761  C CB    . LEU A 94  ? 0.20268 0.17709 0.19506 0.00527  -0.01003 0.00679  94   LEU A CB    
762  C CG    . LEU A 94  ? 0.24912 0.21519 0.24048 0.00500  -0.01235 0.00622  94   LEU A CG    
763  C CD1   . LEU A 94  ? 0.27538 0.23705 0.26753 0.00688  -0.01356 0.00785  94   LEU A CD1   
764  C CD2   . LEU A 94  ? 0.26757 0.23085 0.25595 0.00660  -0.01255 0.00237  94   LEU A CD2   
765  N N     . CYS A 95  ? 0.21123 0.19328 0.20701 -0.00134 -0.00862 0.01167  95   CYS A N     
766  C CA    . CYS A 95  ? 0.20619 0.18888 0.20352 -0.00444 -0.00866 0.01344  95   CYS A CA    
767  C C     . CYS A 95  ? 0.25266 0.23675 0.25134 -0.00545 -0.00831 0.01670  95   CYS A C     
768  O O     . CYS A 95  ? 0.26902 0.25099 0.26917 -0.00759 -0.00903 0.01878  95   CYS A O     
769  C CB    . CYS A 95  ? 0.24501 0.23242 0.24247 -0.00538 -0.00707 0.01245  95   CYS A CB    
770  S SG    . CYS A 95  ? 0.28096 0.27032 0.28095 -0.00852 -0.00678 0.01441  95   CYS A SG    
771  N N     . GLY A 96  ? 0.24550 0.23349 0.24368 -0.00406 -0.00722 0.01725  96   GLY A N     
772  C CA    . GLY A 96  ? 0.29030 0.27968 0.28875 -0.00473 -0.00695 0.02036  96   GLY A CA    
773  C C     . GLY A 96  ? 0.28895 0.27296 0.28719 -0.00393 -0.00866 0.02244  96   GLY A C     
774  O O     . GLY A 96  ? 0.30943 0.29292 0.30792 -0.00527 -0.00867 0.02569  96   GLY A O     
775  N N     . ALA A 97  ? 0.26259 0.24228 0.26022 -0.00166 -0.01000 0.02067  97   ALA A N     
776  C CA    . ALA A 97  ? 0.26295 0.23633 0.26037 -0.00055 -0.01178 0.02240  97   ALA A CA    
777  C C     . ALA A 97  ? 0.26112 0.22865 0.25958 -0.00336 -0.01301 0.02343  97   ALA A C     
778  O O     . ALA A 97  ? 0.29313 0.25793 0.29225 -0.00485 -0.01356 0.02690  97   ALA A O     
779  C CB    . ALA A 97  ? 0.29632 0.26703 0.29287 0.00319  -0.01261 0.01975  97   ALA A CB    
780  N N     . ILE A 98  ? 0.26175 0.22745 0.26036 -0.00428 -0.01356 0.02058  98   ILE A N     
781  C CA    . ILE A 98  ? 0.26887 0.23018 0.26902 -0.00749 -0.01496 0.02133  98   ILE A CA    
782  C C     . ILE A 98  ? 0.27235 0.23808 0.27484 -0.01073 -0.01370 0.02464  98   ILE A C     
783  O O     . ILE A 98  ? 0.30855 0.27121 0.31282 -0.01320 -0.01444 0.02751  98   ILE A O     
784  C CB    . ILE A 98  ? 0.23933 0.19952 0.23887 -0.00790 -0.01581 0.01760  98   ILE A CB    
785  C CG1   . ILE A 98  ? 0.29874 0.25349 0.29562 -0.00474 -0.01703 0.01437  98   ILE A CG1   
786  C CG2   . ILE A 98  ? 0.30261 0.26011 0.30445 -0.01170 -0.01740 0.01844  98   ILE A CG2   
787  C CD1   . ILE A 98  ? 0.24923 0.20438 0.24412 -0.00430 -0.01725 0.01048  98   ILE A CD1   
788  N N     . GLY A 99  ? 0.29117 0.26408 0.29376 -0.01077 -0.01163 0.02428  99   GLY A N     
789  C CA    . GLY A 99  ? 0.28930 0.26710 0.29352 -0.01297 -0.00989 0.02721  99   GLY A CA    
790  C C     . GLY A 99  ? 0.30441 0.28170 0.31198 -0.01650 -0.01030 0.02875  99   GLY A C     
791  O O     . GLY A 99  ? 0.30971 0.28856 0.31887 -0.01848 -0.00929 0.03221  99   GLY A O     
792  N N     . CYS A 100 ? 0.30177 0.27735 0.31047 -0.01738 -0.01176 0.02633  100  CYS A N     
793  C CA    . CYS A 100 ? 0.30980 0.28576 0.32239 -0.02081 -0.01254 0.02750  100  CYS A CA    
794  C C     . CYS A 100 ? 0.33843 0.32191 0.35316 -0.02154 -0.01050 0.02760  100  CYS A C     
795  O O     . CYS A 100 ? 0.34780 0.33462 0.36064 -0.01950 -0.00921 0.02563  100  CYS A O     
796  C CB    . CYS A 100 ? 0.34340 0.31418 0.35601 -0.02143 -0.01551 0.02472  100  CYS A CB    
797  S SG    . CYS A 100 ? 0.38130 0.35322 0.39050 -0.01863 -0.01577 0.02010  100  CYS A SG    
798  N N     . ILE A 101 ? 0.31296 0.29902 0.33201 -0.02451 -0.01018 0.02999  101  ILE A N     
799  C CA    . ILE A 101 ? 0.30343 0.29637 0.32547 -0.02515 -0.00850 0.03006  101  ILE A CA    
800  C C     . ILE A 101 ? 0.30306 0.29553 0.32882 -0.02728 -0.01098 0.02918  101  ILE A C     
801  O O     . ILE A 101 ? 0.32524 0.31819 0.35545 -0.03036 -0.01169 0.03146  101  ILE A O     
802  C CB    . ILE A 101 ? 0.31944 0.31739 0.34383 -0.02651 -0.00565 0.03358  101  ILE A CB    
803  C CG1   . ILE A 101 ? 0.31615 0.31418 0.33611 -0.02448 -0.00376 0.03442  101  ILE A CG1   
804  C CG2   . ILE A 101 ? 0.32397 0.32896 0.35148 -0.02652 -0.00370 0.03325  101  ILE A CG2   
805  C CD1   . ILE A 101 ? 0.32353 0.32371 0.34008 -0.02152 -0.00272 0.03143  101  ILE A CD1   
806  N N     . GLY A 102 ? 0.30019 0.29190 0.32414 -0.02580 -0.01242 0.02600  102  GLY A N     
807  C CA    . GLY A 102 ? 0.31999 0.31050 0.34630 -0.02756 -0.01548 0.02478  102  GLY A CA    
808  C C     . GLY A 102 ? 0.32219 0.31942 0.35385 -0.02894 -0.01511 0.02585  102  GLY A C     
809  O O     . GLY A 102 ? 0.33985 0.33852 0.37136 -0.02810 -0.01644 0.02398  102  GLY A O     
810  N N     . PHE A 103 ? 0.29484 0.29647 0.33131 -0.03090 -0.01324 0.02902  103  PHE A N     
811  C CA    . PHE A 103 ? 0.31539 0.32400 0.35796 -0.03210 -0.01284 0.03015  103  PHE A CA    
812  C C     . PHE A 103 ? 0.39175 0.39960 0.43862 -0.03507 -0.01675 0.02994  103  PHE A C     
813  O O     . PHE A 103 ? 0.42582 0.43938 0.47769 -0.03567 -0.01741 0.03026  103  PHE A O     
814  C CB    . PHE A 103 ? 0.34445 0.35862 0.39097 -0.03325 -0.00932 0.03357  103  PHE A CB    
815  C CG    . PHE A 103 ? 0.34109 0.35204 0.38832 -0.03596 -0.00931 0.03629  103  PHE A CG    
816  C CD1   . PHE A 103 ? 0.37681 0.38806 0.42988 -0.03991 -0.01122 0.03820  103  PHE A CD1   
817  C CD2   . PHE A 103 ? 0.34977 0.35753 0.39205 -0.03468 -0.00746 0.03717  103  PHE A CD2   
818  C CE1   . PHE A 103 ? 0.32716 0.33478 0.38089 -0.04262 -0.01113 0.04106  103  PHE A CE1   
819  C CE2   . PHE A 103 ? 0.31914 0.32349 0.36181 -0.03700 -0.00749 0.04012  103  PHE A CE2   
820  C CZ    . PHE A 103 ? 0.31893 0.32288 0.36725 -0.04102 -0.00921 0.04215  103  PHE A CZ    
821  N N     . SER A 104 ? 0.33197 0.33286 0.37712 -0.03684 -0.01952 0.02930  104  SER A N     
822  C CA    . SER A 104 ? 0.31827 0.31720 0.36660 -0.03986 -0.02377 0.02846  104  SER A CA    
823  C C     . SER A 104 ? 0.30196 0.29161 0.34398 -0.03910 -0.02669 0.02529  104  SER A C     
824  O O     . SER A 104 ? 0.25869 0.24386 0.29515 -0.03661 -0.02519 0.02449  104  SER A O     
825  C CB    . SER A 104 ? 0.33516 0.33568 0.39037 -0.04432 -0.02395 0.03184  104  SER A CB    
826  O OG    . SER A 104 ? 0.29381 0.28748 0.34633 -0.04524 -0.02351 0.03305  104  SER A OG    
827  N N     . TRP A 105 ? 0.32221 0.30925 0.36514 -0.04113 -0.03096 0.02332  105  TRP A N     
828  C CA    . TRP A 105 ? 0.31723 0.29507 0.35412 -0.04050 -0.03382 0.01996  105  TRP A CA    
829  C C     . TRP A 105 ? 0.27555 0.24645 0.31198 -0.04193 -0.03354 0.02130  105  TRP A C     
830  O O     . TRP A 105 ? 0.27749 0.24167 0.30796 -0.03940 -0.03335 0.01944  105  TRP A O     
831  C CB    . TRP A 105 ? 0.31668 0.29320 0.35466 -0.04282 -0.03873 0.01752  105  TRP A CB    
832  C CG    . TRP A 105 ? 0.27962 0.24647 0.31104 -0.04217 -0.04175 0.01357  105  TRP A CG    
833  C CD1   . TRP A 105 ? 0.28115 0.24526 0.30521 -0.03880 -0.04252 0.00986  105  TRP A CD1   
834  C CD2   . TRP A 105 ? 0.25765 0.21606 0.28911 -0.04484 -0.04422 0.01287  105  TRP A CD2   
835  N NE1   . TRP A 105 ? 0.26178 0.21663 0.28117 -0.03894 -0.04518 0.00662  105  TRP A NE1   
836  C CE2   . TRP A 105 ? 0.27183 0.22260 0.29565 -0.04258 -0.04640 0.00828  105  TRP A CE2   
837  C CE3   . TRP A 105 ? 0.25958 0.21591 0.29672 -0.04895 -0.04466 0.01577  105  TRP A CE3   
838  C CZ2   . TRP A 105 ? 0.26758 0.20831 0.28925 -0.04402 -0.04912 0.00616  105  TRP A CZ2   
839  C CZ3   . TRP A 105 ? 0.28780 0.23387 0.32296 -0.05070 -0.04749 0.01400  105  TRP A CZ3   
840  C CH2   . TRP A 105 ? 0.28300 0.22116 0.31047 -0.04811 -0.04975 0.00905  105  TRP A CH2   
841  N N     . ALA A 106 ? 0.28445 0.25706 0.32735 -0.04587 -0.03340 0.02477  106  ALA A N     
842  C CA    . ALA A 106 ? 0.27411 0.23984 0.31685 -0.04752 -0.03316 0.02676  106  ALA A CA    
843  C C     . ALA A 106 ? 0.28451 0.25030 0.32372 -0.04433 -0.02907 0.02875  106  ALA A C     
844  O O     . ALA A 106 ? 0.30709 0.26573 0.34387 -0.04414 -0.02910 0.02965  106  ALA A O     
845  C CB    . ALA A 106 ? 0.29472 0.26318 0.34562 -0.05286 -0.03361 0.03055  106  ALA A CB    
846  N N     . ALA A 107 ? 0.26678 0.24027 0.30568 -0.04182 -0.02578 0.02944  107  ALA A N     
847  C CA    . ALA A 107 ? 0.26168 0.23571 0.29702 -0.03891 -0.02223 0.03101  107  ALA A CA    
848  C C     . ALA A 107 ? 0.31676 0.28413 0.34516 -0.03518 -0.02293 0.02795  107  ALA A C     
849  O O     . ALA A 107 ? 0.32985 0.29528 0.35541 -0.03325 -0.02110 0.02935  107  ALA A O     
850  C CB    . ALA A 107 ? 0.30805 0.29126 0.34433 -0.03710 -0.01890 0.03166  107  ALA A CB    
851  N N     . SER A 108 ? 0.30974 0.27413 0.33536 -0.03402 -0.02548 0.02388  108  SER A N     
852  C CA    . SER A 108 ? 0.28254 0.24050 0.30198 -0.03070 -0.02648 0.02042  108  SER A CA    
853  C C     . SER A 108 ? 0.25427 0.21186 0.27156 -0.03019 -0.02893 0.01641  108  SER A C     
854  O O     . SER A 108 ? 0.26292 0.22586 0.27876 -0.02823 -0.02759 0.01532  108  SER A O     
855  C CB    . SER A 108 ? 0.29801 0.25856 0.31381 -0.02674 -0.02328 0.02051  108  SER A CB    
856  O OG    . SER A 108 ? 0.31008 0.26502 0.32379 -0.02536 -0.02302 0.02151  108  SER A OG    
857  N N     . PRO A 109 ? 0.25169 0.20283 0.26842 -0.03199 -0.03260 0.01419  109  PRO A N     
858  C CA    . PRO A 109 ? 0.24453 0.19549 0.25867 -0.03171 -0.03528 0.01041  109  PRO A CA    
859  C C     . PRO A 109 ? 0.25218 0.20388 0.26002 -0.02729 -0.03378 0.00753  109  PRO A C     
860  O O     . PRO A 109 ? 0.25507 0.21148 0.26196 -0.02670 -0.03397 0.00648  109  PRO A O     
861  C CB    . PRO A 109 ? 0.23183 0.17354 0.24483 -0.03370 -0.03918 0.00808  109  PRO A CB    
862  C CG    . PRO A 109 ? 0.24488 0.18499 0.26350 -0.03717 -0.03902 0.01198  109  PRO A CG    
863  C CD    . PRO A 109 ? 0.26296 0.20672 0.28166 -0.03481 -0.03468 0.01525  109  PRO A CD    
864  N N     . ALA A 110 ? 0.23252 0.17993 0.23630 -0.02414 -0.03224 0.00648  110  ALA A N     
865  C CA    . ALA A 110 ? 0.24720 0.19550 0.24537 -0.02013 -0.03068 0.00373  110  ALA A CA    
866  C C     . ALA A 110 ? 0.26961 0.22642 0.26882 -0.01907 -0.02764 0.00546  110  ALA A C     
867  O O     . ALA A 110 ? 0.23197 0.19095 0.22753 -0.01706 -0.02698 0.00350  110  ALA A O     
868  C CB    . ALA A 110 ? 0.24036 0.18362 0.23542 -0.01694 -0.02938 0.00279  110  ALA A CB    
869  N N     . CYS A 111 ? 0.23938 0.20077 0.24324 -0.02040 -0.02570 0.00909  111  CYS A N     
870  C CA    . CYS A 111 ? 0.25085 0.21960 0.25564 -0.01936 -0.02281 0.01046  111  CYS A CA    
871  C C     . CYS A 111 ? 0.26362 0.23625 0.26933 -0.02033 -0.02398 0.00990  111  CYS A C     
872  O O     . CYS A 111 ? 0.29098 0.26716 0.29471 -0.01850 -0.02237 0.00933  111  CYS A O     
873  C CB    . CYS A 111 ? 0.23260 0.20510 0.24180 -0.02068 -0.02065 0.01419  111  CYS A CB    
874  S SG    . CYS A 111 ? 0.36933 0.35019 0.37976 -0.01951 -0.01707 0.01559  111  CYS A SG    
875  N N     . THR A 112 ? 0.23394 0.20591 0.24281 -0.02325 -0.02695 0.01017  112  THR A N     
876  C CA    . THR A 112 ? 0.23241 0.20839 0.24261 -0.02409 -0.02860 0.00987  112  THR A CA    
877  C C     . THR A 112 ? 0.24705 0.21932 0.25127 -0.02283 -0.03110 0.00632  112  THR A C     
878  O O     . THR A 112 ? 0.24190 0.21733 0.24408 -0.02157 -0.03106 0.00579  112  THR A O     
879  C CB    . THR A 112 ? 0.33304 0.31107 0.34990 -0.02791 -0.03087 0.01179  112  THR A CB    
880  O OG1   . THR A 112 ? 0.31678 0.30004 0.33898 -0.02872 -0.02790 0.01527  112  THR A OG1   
881  C CG2   . THR A 112 ? 0.36027 0.34190 0.37844 -0.02871 -0.03361 0.01111  112  THR A CG2   
882  N N     . GLU A 113 ? 0.23196 0.19722 0.23291 -0.02298 -0.03318 0.00386  113  GLU A N     
883  C CA    . GLU A 113 ? 0.23373 0.19523 0.22866 -0.02204 -0.03585 0.00016  113  GLU A CA    
884  C C     . GLU A 113 ? 0.20912 0.17091 0.19774 -0.01820 -0.03319 -0.00151 113  GLU A C     
885  O O     . GLU A 113 ? 0.20096 0.16367 0.18525 -0.01721 -0.03417 -0.00310 113  GLU A O     
886  C CB    . GLU A 113 ? 0.24589 0.19922 0.23911 -0.02321 -0.03872 -0.00232 113  GLU A CB    
887  C CG    . GLU A 113 ? 0.26469 0.21745 0.26451 -0.02757 -0.04143 -0.00053 113  GLU A CG    
888  C CD    . GLU A 113 ? 0.23807 0.18426 0.23565 -0.02962 -0.04616 -0.00389 113  GLU A CD    
889  O OE1   . GLU A 113 ? 0.27133 0.21365 0.26165 -0.02736 -0.04729 -0.00778 113  GLU A OE1   
890  O OE2   . GLU A 113 ? 0.28879 0.23378 0.29181 -0.03361 -0.04871 -0.00271 113  GLU A OE2   
891  N N     . LEU A 114 ? 0.21591 0.17720 0.20395 -0.01610 -0.02990 -0.00101 114  LEU A N     
892  C CA    . LEU A 114 ? 0.19203 0.15464 0.17516 -0.01279 -0.02711 -0.00228 114  LEU A CA    
893  C C     . LEU A 114 ? 0.18987 0.15887 0.17384 -0.01261 -0.02544 -0.00042 114  LEU A C     
894  O O     . LEU A 114 ? 0.18286 0.15276 0.16209 -0.01083 -0.02456 -0.00165 114  LEU A O     
895  C CB    . LEU A 114 ? 0.17424 0.13616 0.15784 -0.01083 -0.02418 -0.00176 114  LEU A CB    
896  C CG    . LEU A 114 ? 0.18955 0.15293 0.16869 -0.00753 -0.02133 -0.00330 114  LEU A CG    
897  C CD1   . LEU A 114 ? 0.20062 0.15940 0.17344 -0.00579 -0.02267 -0.00713 114  LEU A CD1   
898  C CD2   . LEU A 114 ? 0.18343 0.14750 0.16430 -0.00580 -0.01874 -0.00235 114  LEU A CD2   
899  N N     . GLU A 115 ? 0.19053 0.16384 0.18041 -0.01436 -0.02486 0.00260  115  GLU A N     
900  C CA    . GLU A 115 ? 0.20259 0.18134 0.19369 -0.01401 -0.02331 0.00435  115  GLU A CA    
901  C C     . GLU A 115 ? 0.20437 0.18354 0.19304 -0.01430 -0.02605 0.00356  115  GLU A C     
902  O O     . GLU A 115 ? 0.19273 0.17371 0.17819 -0.01277 -0.02485 0.00366  115  GLU A O     
903  C CB    . GLU A 115 ? 0.18542 0.16843 0.18339 -0.01566 -0.02229 0.00739  115  GLU A CB    
904  C CG    . GLU A 115 ? 0.20579 0.19384 0.20530 -0.01489 -0.02031 0.00905  115  GLU A CG    
905  C CD    . GLU A 115 ? 0.26516 0.25714 0.27028 -0.01567 -0.01807 0.01151  115  GLU A CD    
906  O OE1   . GLU A 115 ? 0.22027 0.21136 0.22595 -0.01572 -0.01646 0.01187  115  GLU A OE1   
907  O OE2   . GLU A 115 ? 0.24804 0.24406 0.25677 -0.01599 -0.01788 0.01307  115  GLU A OE2   
908  N N     . THR A 116 ? 0.19918 0.17663 0.18927 -0.01639 -0.02989 0.00289  116  THR A N     
909  C CA    . THR A 116 ? 0.21655 0.19467 0.20425 -0.01676 -0.03314 0.00212  116  THR A CA    
910  C C     . THR A 116 ? 0.22781 0.20251 0.20674 -0.01457 -0.03324 -0.00072 116  THR A C     
911  O O     . THR A 116 ? 0.22721 0.20379 0.20261 -0.01354 -0.03366 -0.00044 116  THR A O     
912  C CB    . THR A 116 ? 0.31547 0.29223 0.30652 -0.01977 -0.03755 0.00154  116  THR A CB    
913  O OG1   . THR A 116 ? 0.33424 0.31508 0.33378 -0.02187 -0.03699 0.00452  116  THR A OG1   
914  C CG2   . THR A 116 ? 0.34274 0.32078 0.33135 -0.02018 -0.04142 0.00073  116  THR A CG2   
915  N N     . VAL A 117 ? 0.19971 0.16942 0.17494 -0.01362 -0.03269 -0.00332 117  VAL A N     
916  C CA    . VAL A 117 ? 0.20508 0.17184 0.17189 -0.01128 -0.03232 -0.00624 117  VAL A CA    
917  C C     . VAL A 117 ? 0.18299 0.15304 0.14761 -0.00896 -0.02802 -0.00498 117  VAL A C     
918  O O     . VAL A 117 ? 0.18363 0.15411 0.14233 -0.00757 -0.02765 -0.00566 117  VAL A O     
919  C CB    . VAL A 117 ? 0.19920 0.15972 0.16319 -0.01050 -0.03271 -0.00951 117  VAL A CB    
920  C CG1   . VAL A 117 ? 0.23056 0.18855 0.18574 -0.00775 -0.03190 -0.01275 117  VAL A CG1   
921  C CG2   . VAL A 117 ? 0.22574 0.18226 0.19185 -0.01327 -0.03723 -0.01080 117  VAL A CG2   
922  N N     . MET A 118 ? 0.17175 0.14416 0.14093 -0.00867 -0.02475 -0.00306 118  MET A N     
923  C CA    . MET A 118 ? 0.17843 0.15390 0.14610 -0.00692 -0.02082 -0.00198 118  MET A CA    
924  C C     . MET A 118 ? 0.17476 0.15381 0.14277 -0.00729 -0.02073 0.00039  118  MET A C     
925  O O     . MET A 118 ? 0.17875 0.15897 0.14290 -0.00597 -0.01854 0.00077  118  MET A O     
926  C CB    . MET A 118 ? 0.17449 0.15178 0.14698 -0.00676 -0.01786 -0.00064 118  MET A CB    
927  C CG    . MET A 118 ? 0.17663 0.15078 0.14835 -0.00551 -0.01714 -0.00260 118  MET A CG    
928  S SD    . MET A 118 ? 0.19349 0.16581 0.15787 -0.00249 -0.01541 -0.00576 118  MET A SD    
929  C CE    . MET A 118 ? 0.18527 0.15161 0.14458 -0.00269 -0.01958 -0.00903 118  MET A CE    
930  N N     . MET A 119 ? 0.16616 0.14704 0.13897 -0.00902 -0.02300 0.00219  119  MET A N     
931  C CA    . MET A 119 ? 0.18130 0.16524 0.15455 -0.00893 -0.02325 0.00446  119  MET A CA    
932  C C     . MET A 119 ? 0.18415 0.16662 0.15075 -0.00833 -0.02587 0.00343  119  MET A C     
933  O O     . MET A 119 ? 0.22573 0.20973 0.18990 -0.00743 -0.02523 0.00515  119  MET A O     
934  C CB    . MET A 119 ? 0.18105 0.16805 0.16182 -0.01057 -0.02483 0.00660  119  MET A CB    
935  C CG    . MET A 119 ? 0.15328 0.14247 0.13976 -0.01086 -0.02165 0.00808  119  MET A CG    
936  S SD    . MET A 119 ? 0.21352 0.20470 0.19922 -0.00924 -0.01740 0.00966  119  MET A SD    
937  C CE    . MET A 119 ? 0.17807 0.17225 0.16702 -0.00917 -0.01905 0.01220  119  MET A CE    
938  N N     . ASP A 120 ? 0.19226 0.17138 0.15540 -0.00878 -0.02885 0.00063  120  ASP A N     
939  C CA    . ASP A 120 ? 0.20801 0.18539 0.16325 -0.00797 -0.03113 -0.00091 120  ASP A CA    
940  C C     . ASP A 120 ? 0.22089 0.19698 0.16902 -0.00575 -0.02760 -0.00209 120  ASP A C     
941  O O     . ASP A 120 ? 0.21897 0.19575 0.16142 -0.00472 -0.02733 -0.00125 120  ASP A O     
942  C CB    . ASP A 120 ? 0.24531 0.21911 0.19872 -0.00925 -0.03554 -0.00404 120  ASP A CB    
943  C CG    . ASP A 120 ? 0.33185 0.30788 0.29141 -0.01169 -0.03974 -0.00267 120  ASP A CG    
944  O OD1   . ASP A 120 ? 0.31593 0.29635 0.27910 -0.01171 -0.03976 0.00050  120  ASP A OD1   
945  O OD2   . ASP A 120 ? 0.35048 0.32388 0.31145 -0.01356 -0.04305 -0.00476 120  ASP A OD2   
946  N N     . TRP A 121 ? 0.19768 0.17219 0.14615 -0.00493 -0.02484 -0.00380 121  TRP A N     
947  C CA    . TRP A 121 ? 0.20233 0.17700 0.14575 -0.00284 -0.02087 -0.00455 121  TRP A CA    
948  C C     . TRP A 121 ? 0.19694 0.17524 0.14104 -0.00265 -0.01800 -0.00116 121  TRP A C     
949  O O     . TRP A 121 ? 0.20987 0.18852 0.14779 -0.00159 -0.01664 -0.00076 121  TRP A O     
950  C CB    . TRP A 121 ? 0.20873 0.18265 0.15509 -0.00203 -0.01821 -0.00596 121  TRP A CB    
951  C CG    . TRP A 121 ? 0.18239 0.15177 0.12535 -0.00101 -0.01957 -0.00985 121  TRP A CG    
952  C CD1   . TRP A 121 ? 0.21151 0.17690 0.15076 -0.00155 -0.02361 -0.01238 121  TRP A CD1   
953  C CD2   . TRP A 121 ? 0.20896 0.17710 0.15201 0.00090  -0.01700 -0.01179 121  TRP A CD2   
954  N NE1   . TRP A 121 ? 0.22286 0.18385 0.15965 -0.00009 -0.02358 -0.01595 121  TRP A NE1   
955  C CE2   . TRP A 121 ? 0.21737 0.18011 0.15659 0.00164  -0.01950 -0.01553 121  TRP A CE2   
956  C CE3   . TRP A 121 ? 0.22389 0.19505 0.17013 0.00207  -0.01303 -0.01079 121  TRP A CE3   
957  C CZ2   . TRP A 121 ? 0.24320 0.20319 0.18170 0.00391  -0.01796 -0.01816 121  TRP A CZ2   
958  C CZ3   . TRP A 121 ? 0.21547 0.18474 0.16129 0.00424  -0.01168 -0.01323 121  TRP A CZ3   
959  C CH2   . TRP A 121 ? 0.20443 0.16803 0.14644 0.00533  -0.01404 -0.01682 121  TRP A CH2   
960  N N     . LEU A 122 ? 0.19368 0.17441 0.14504 -0.00370 -0.01697 0.00132  122  LEU A N     
961  C CA    . LEU A 122 ? 0.19894 0.18228 0.15149 -0.00360 -0.01412 0.00427  122  LEU A CA    
962  C C     . LEU A 122 ? 0.18826 0.17191 0.13807 -0.00363 -0.01621 0.00642  122  LEU A C     
963  O O     . LEU A 122 ? 0.20711 0.19121 0.15322 -0.00298 -0.01415 0.00818  122  LEU A O     
964  C CB    . LEU A 122 ? 0.20277 0.18817 0.16336 -0.00458 -0.01277 0.00583  122  LEU A CB    
965  C CG    . LEU A 122 ? 0.17357 0.16101 0.13617 -0.00463 -0.00962 0.00833  122  LEU A CG    
966  C CD1   . LEU A 122 ? 0.20661 0.19433 0.16519 -0.00385 -0.00612 0.00779  122  LEU A CD1   
967  C CD2   . LEU A 122 ? 0.17873 0.16789 0.14852 -0.00548 -0.00853 0.00903  122  LEU A CD2   
968  N N     . GLY A 123 ? 0.18957 0.17309 0.14129 -0.00444 -0.02040 0.00652  123  GLY A N     
969  C CA    . GLY A 123 ? 0.20854 0.19267 0.15767 -0.00420 -0.02301 0.00857  123  GLY A CA    
970  C C     . GLY A 123 ? 0.26796 0.25030 0.20720 -0.00306 -0.02339 0.00768  123  GLY A C     
971  O O     . GLY A 123 ? 0.24162 0.22440 0.17715 -0.00235 -0.02326 0.01024  123  GLY A O     
972  N N     . LYS A 124 ? 0.22328 0.20336 0.15783 -0.00271 -0.02373 0.00407  124  LYS A N     
973  C CA    . LYS A 124 ? 0.24889 0.22740 0.17332 -0.00139 -0.02356 0.00277  124  LYS A CA    
974  C C     . LYS A 124 ? 0.24255 0.22206 0.16404 -0.00033 -0.01823 0.00414  124  LYS A C     
975  O O     . LYS A 124 ? 0.24896 0.22840 0.16306 0.00054  -0.01745 0.00536  124  LYS A O     
976  C CB    . LYS A 124 ? 0.25704 0.23247 0.17746 -0.00107 -0.02531 -0.00191 124  LYS A CB    
977  C CG    . LYS A 124 ? 0.29540 0.26954 0.21777 -0.00257 -0.03106 -0.00335 124  LYS A CG    
978  C CD    . LYS A 124 ? 0.34377 0.31392 0.26428 -0.00266 -0.03260 -0.00805 124  LYS A CD    
979  C CE    . LYS A 124 ? 0.41909 0.38670 0.32906 -0.00056 -0.03123 -0.01121 124  LYS A CE    
980  N NZ    . LYS A 124 ? 0.54712 0.51023 0.45261 -0.00090 -0.03551 -0.01579 124  LYS A NZ    
981  N N     . MET A 125 ? 0.22368 0.20438 0.15084 -0.00054 -0.01460 0.00414  125  MET A N     
982  C CA    . MET A 125 ? 0.22068 0.20300 0.14640 -0.00002 -0.00963 0.00561  125  MET A CA    
983  C C     . MET A 125 ? 0.25487 0.23812 0.18114 -0.00058 -0.00880 0.00996  125  MET A C     
984  O O     . MET A 125 ? 0.26170 0.24550 0.18370 -0.00028 -0.00565 0.01170  125  MET A O     
985  C CB    . MET A 125 ? 0.21490 0.19868 0.14734 -0.00031 -0.00665 0.00469  125  MET A CB    
986  C CG    . MET A 125 ? 0.24308 0.22570 0.17451 0.00077  -0.00664 0.00071  125  MET A CG    
987  S SD    . MET A 125 ? 0.30540 0.28965 0.24576 0.00036  -0.00462 0.00016  125  MET A SD    
988  C CE    . MET A 125 ? 0.18290 0.17094 0.12518 -0.00014 0.00022  0.00298  125  MET A CE    
989  N N     . LEU A 126 ? 0.23111 0.21451 0.16280 -0.00135 -0.01141 0.01185  126  LEU A N     
990  C CA    . LEU A 126 ? 0.22048 0.20404 0.15293 -0.00149 -0.01114 0.01592  126  LEU A CA    
991  C C     . LEU A 126 ? 0.26117 0.24374 0.18735 -0.00072 -0.01468 0.01749  126  LEU A C     
992  O O     . LEU A 126 ? 0.27134 0.25363 0.19767 -0.00047 -0.01492 0.02116  126  LEU A O     
993  C CB    . LEU A 126 ? 0.24480 0.22933 0.18650 -0.00223 -0.01185 0.01719  126  LEU A CB    
994  C CG    . LEU A 126 ? 0.24999 0.23544 0.19732 -0.00301 -0.00783 0.01731  126  LEU A CG    
995  C CD1   . LEU A 126 ? 0.29191 0.27838 0.24359 -0.00349 -0.00777 0.01427  126  LEU A CD1   
996  C CD2   . LEU A 126 ? 0.29994 0.28543 0.25284 -0.00323 -0.00766 0.02012  126  LEU A CD2   
997  N N     . GLU A 127 ? 0.25043 0.23222 0.17087 -0.00025 -0.01755 0.01475  127  GLU A N     
998  C CA    . GLU A 127 ? 0.28110 0.26225 0.19524 0.00040  -0.02172 0.01577  127  GLU A CA    
999  C C     . GLU A 127 ? 0.26676 0.24912 0.18720 0.00016  -0.02530 0.01848  127  GLU A C     
1000 O O     . GLU A 127 ? 0.28121 0.26355 0.19877 0.00097  -0.02693 0.02184  127  GLU A O     
1001 C CB    . GLU A 127 ? 0.31588 0.29626 0.22092 0.00135  -0.01944 0.01822  127  GLU A CB    
1002 C CG    . GLU A 127 ? 0.40311 0.38304 0.30112 0.00192  -0.01615 0.01532  127  GLU A CG    
1003 C CD    . GLU A 127 ? 0.58348 0.56314 0.47223 0.00270  -0.01361 0.01805  127  GLU A CD    
1004 O OE1   . GLU A 127 ? 0.58830 0.56833 0.47912 0.00219  -0.00999 0.02172  127  GLU A OE1   
1005 O OE2   . GLU A 127 ? 0.63387 0.61278 0.51303 0.00371  -0.01517 0.01647  127  GLU A OE2   
1006 N N     . LEU A 128 ? 0.22901 0.21263 0.15828 -0.00082 -0.02638 0.01718  128  LEU A N     
1007 C CA    . LEU A 128 ? 0.26233 0.24797 0.19860 -0.00097 -0.02959 0.01931  128  LEU A CA    
1008 C C     . LEU A 128 ? 0.26844 0.25474 0.20113 -0.00085 -0.03542 0.01885  128  LEU A C     
1009 O O     . LEU A 128 ? 0.29351 0.27844 0.22039 -0.00125 -0.03733 0.01557  128  LEU A O     
1010 C CB    . LEU A 128 ? 0.23803 0.22523 0.18389 -0.00222 -0.02918 0.01776  128  LEU A CB    
1011 C CG    . LEU A 128 ? 0.23152 0.21914 0.18341 -0.00235 -0.02456 0.01891  128  LEU A CG    
1012 C CD1   . LEU A 128 ? 0.22657 0.21628 0.18743 -0.00347 -0.02517 0.01784  128  LEU A CD1   
1013 C CD2   . LEU A 128 ? 0.21846 0.20600 0.17125 -0.00125 -0.02325 0.02283  128  LEU A CD2   
1014 N N     . PRO A 129 ? 0.30005 0.28841 0.23601 -0.00019 -0.03847 0.02197  129  PRO A N     
1015 C CA    . PRO A 129 ? 0.29785 0.28787 0.23217 -0.00035 -0.04466 0.02146  129  PRO A CA    
1016 C C     . PRO A 129 ? 0.30188 0.29280 0.24087 -0.00241 -0.04721 0.01758  129  PRO A C     
1017 O O     . PRO A 129 ? 0.27304 0.26500 0.22037 -0.00346 -0.04521 0.01696  129  PRO A O     
1018 C CB    . PRO A 129 ? 0.29187 0.28491 0.23266 0.00082  -0.04659 0.02564  129  PRO A CB    
1019 C CG    . PRO A 129 ? 0.29174 0.28266 0.23156 0.00220  -0.04164 0.02879  129  PRO A CG    
1020 C CD    . PRO A 129 ? 0.26373 0.25269 0.20399 0.00103  -0.03648 0.02620  129  PRO A CD    
1021 N N     . LYS A 130 ? 0.31393 0.30409 0.24705 -0.00308 -0.05170 0.01494  130  LYS A N     
1022 C CA    . LYS A 130 ? 0.34382 0.33362 0.28025 -0.00531 -0.05431 0.01099  130  LYS A CA    
1023 C C     . LYS A 130 ? 0.32275 0.31684 0.27135 -0.00683 -0.05658 0.01224  130  LYS A C     
1024 O O     . LYS A 130 ? 0.33612 0.32988 0.28980 -0.00894 -0.05709 0.00976  130  LYS A O     
1025 C CB    . LYS A 130 ? 0.40610 0.39422 0.33386 -0.00579 -0.05942 0.00800  130  LYS A CB    
1026 C CG    . LYS A 130 ? 0.47117 0.45514 0.38639 -0.00433 -0.05700 0.00598  130  LYS A CG    
1027 C CD    . LYS A 130 ? 0.52038 0.50162 0.43622 -0.00414 -0.05111 0.00408  130  LYS A CD    
1028 C CE    . LYS A 130 ? 0.57859 0.55680 0.48275 -0.00240 -0.04806 0.00250  130  LYS A CE    
1029 N NZ    . LYS A 130 ? 0.58624 0.56263 0.49179 -0.00202 -0.04249 0.00072  130  LYS A NZ    
1030 N N     . ALA A 131 ? 0.30002 0.29811 0.25352 -0.00570 -0.05778 0.01616  131  ALA A N     
1031 C CA    . ALA A 131 ? 0.32425 0.32732 0.28976 -0.00683 -0.05946 0.01750  131  ALA A CA    
1032 C C     . ALA A 131 ? 0.30387 0.30697 0.27681 -0.00749 -0.05441 0.01743  131  ALA A C     
1033 O O     . ALA A 131 ? 0.28741 0.29417 0.26984 -0.00903 -0.05529 0.01764  131  ALA A O     
1034 C CB    . ALA A 131 ? 0.33162 0.33887 0.30063 -0.00471 -0.06124 0.02180  131  ALA A CB    
1035 N N     . PHE A 132 ? 0.27172 0.27123 0.24056 -0.00646 -0.04918 0.01720  132  PHE A N     
1036 C CA    . PHE A 132 ? 0.26311 0.26250 0.23787 -0.00701 -0.04452 0.01698  132  PHE A CA    
1037 C C     . PHE A 132 ? 0.31058 0.30716 0.28443 -0.00894 -0.04396 0.01337  132  PHE A C     
1038 O O     . PHE A 132 ? 0.30327 0.30028 0.28279 -0.00976 -0.04105 0.01319  132  PHE A O     
1039 C CB    . PHE A 132 ? 0.25261 0.24984 0.22413 -0.00514 -0.03937 0.01854  132  PHE A CB    
1040 C CG    . PHE A 132 ? 0.24791 0.24725 0.22266 -0.00326 -0.03882 0.02232  132  PHE A CG    
1041 C CD1   . PHE A 132 ? 0.25402 0.25680 0.23833 -0.00311 -0.03774 0.02382  132  PHE A CD1   
1042 C CD2   . PHE A 132 ? 0.25810 0.25573 0.22607 -0.00147 -0.03925 0.02444  132  PHE A CD2   
1043 C CE1   . PHE A 132 ? 0.25075 0.25494 0.23809 -0.00097 -0.03718 0.02705  132  PHE A CE1   
1044 C CE2   . PHE A 132 ? 0.24639 0.24513 0.21735 0.00047  -0.03884 0.02807  132  PHE A CE2   
1045 C CZ    . PHE A 132 ? 0.23224 0.23411 0.21302 0.00085  -0.03783 0.02922  132  PHE A CZ    
1046 N N     . LEU A 133 ? 0.32637 0.31985 0.29298 -0.00951 -0.04670 0.01051  133  LEU A N     
1047 C CA    . LEU A 133 ? 0.36324 0.35287 0.32785 -0.01078 -0.04602 0.00692  133  LEU A CA    
1048 C C     . LEU A 133 ? 0.43618 0.42654 0.40635 -0.01355 -0.05025 0.00540  133  LEU A C     
1049 O O     . LEU A 133 ? 0.47089 0.46421 0.44334 -0.01453 -0.05485 0.00610  133  LEU A O     
1050 C CB    . LEU A 133 ? 0.35580 0.34110 0.30908 -0.00962 -0.04624 0.00420  133  LEU A CB    
1051 C CG    . LEU A 133 ? 0.37585 0.36061 0.32300 -0.00721 -0.04219 0.00589  133  LEU A CG    
1052 C CD1   . LEU A 133 ? 0.44279 0.42368 0.37905 -0.00613 -0.04177 0.00289  133  LEU A CD1   
1053 C CD2   . LEU A 133 ? 0.33632 0.32174 0.28846 -0.00677 -0.03677 0.00731  133  LEU A CD2   
1054 N N     . ASN A 134 ? 0.45887 0.44654 0.43143 -0.01492 -0.04877 0.00347  134  ASN A N     
1055 C CA    . ASN A 134 ? 0.52202 0.50963 0.50022 -0.01797 -0.05227 0.00222  134  ASN A CA    
1056 C C     . ASN A 134 ? 0.63396 0.61644 0.60545 -0.01906 -0.05627 -0.00189 134  ASN A C     
1057 O O     . ASN A 134 ? 0.74212 0.72496 0.71730 -0.02186 -0.06081 -0.00289 134  ASN A O     
1058 C CB    . ASN A 134 ? 0.48012 0.46694 0.46433 -0.01902 -0.04884 0.00260  134  ASN A CB    
1059 C CG    . ASN A 134 ? 0.60298 0.58979 0.59375 -0.02252 -0.05204 0.00203  134  ASN A CG    
1060 O OD1   . ASN A 134 ? 0.63858 0.63081 0.63758 -0.02418 -0.05339 0.00445  134  ASN A OD1   
1061 N ND2   . ASN A 134 ? 0.57901 0.55967 0.56638 -0.02365 -0.05320 -0.00116 134  ASN A ND2   
1062 N N     . GLU A 135 ? 0.69276 0.67059 0.65462 -0.01698 -0.05464 -0.00442 135  GLU A N     
1063 C CA    . GLU A 135 ? 0.75609 0.72833 0.71067 -0.01756 -0.05795 -0.00892 135  GLU A CA    
1064 C C     . GLU A 135 ? 0.96878 0.94272 0.92123 -0.01891 -0.06408 -0.00960 135  GLU A C     
1065 O O     . GLU A 135 ? 0.95610 0.93489 0.90877 -0.01800 -0.06508 -0.00673 135  GLU A O     
1066 C CB    . GLU A 135 ? 0.72514 0.69357 0.66946 -0.01445 -0.05463 -0.01109 135  GLU A CB    
1067 C CG    . GLU A 135 ? 0.76870 0.74070 0.70890 -0.01203 -0.05226 -0.00825 135  GLU A CG    
1068 C CD    . GLU A 135 ? 0.87218 0.84089 0.80076 -0.00953 -0.05061 -0.01075 135  GLU A CD    
1069 O OE1   . GLU A 135 ? 0.84292 0.80734 0.76830 -0.00866 -0.04849 -0.01397 135  GLU A OE1   
1070 O OE2   . GLU A 135 ? 0.90346 0.87401 0.82612 -0.00828 -0.05128 -0.00932 135  GLU A OE2   
1071 N N     . LYS A 136 ? 1.03181 1.00148 0.98228 -0.02112 -0.06843 -0.01345 136  LYS A N     
1072 C CA    . LYS A 136 ? 1.08256 1.05306 1.02993 -0.02271 -0.07496 -0.01509 136  LYS A CA    
1073 C C     . LYS A 136 ? 1.07669 1.05475 1.03431 -0.02491 -0.07818 -0.01139 136  LYS A C     
1074 O O     . LYS A 136 ? 1.10918 1.09167 1.06508 -0.02415 -0.08115 -0.00973 136  LYS A O     
1075 C CB    . LYS A 136 ? 1.08905 1.05891 1.02440 -0.01974 -0.07526 -0.01602 136  LYS A CB    
1076 C CG    . LYS A 136 ? 1.07972 1.04207 1.00381 -0.01858 -0.07525 -0.02142 136  LYS A CG    
1077 C CD    . LYS A 136 ? 1.06472 1.02178 0.99120 -0.02176 -0.07910 -0.02559 136  LYS A CD    
1078 C CE    . LYS A 136 ? 0.97923 0.92803 0.89523 -0.02009 -0.07829 -0.03119 136  LYS A CE    
1079 N NZ    . LYS A 136 ? 0.85641 0.80049 0.77627 -0.01971 -0.07410 -0.03219 136  LYS A NZ    
1080 N N     . ALA A 137 ? 1.01286 0.99260 0.98128 -0.02751 -0.07746 -0.00993 137  ALA A N     
1081 C CA    . ALA A 137 ? 1.00793 0.99491 0.98743 -0.03018 -0.08062 -0.00698 137  ALA A CA    
1082 C C     . ALA A 137 ? 0.97907 0.97355 0.96125 -0.02772 -0.07973 -0.00264 137  ALA A C     
1083 O O     . ALA A 137 ? 0.95333 0.95412 0.94166 -0.02904 -0.08386 -0.00081 137  ALA A O     
1084 C CB    . ALA A 137 ? 0.99198 0.97851 0.97141 -0.03364 -0.08801 -0.00984 137  ALA A CB    
1085 N N     . GLY A 138 ? 0.93385 0.92775 0.91190 -0.02416 -0.07448 -0.00090 138  GLY A N     
1086 C CA    . GLY A 138 ? 0.84683 0.84683 0.82808 -0.02181 -0.07317 0.00336  138  GLY A CA    
1087 C C     . GLY A 138 ? 0.76844 0.77423 0.76243 -0.02278 -0.07097 0.00665  138  GLY A C     
1088 O O     . GLY A 138 ? 0.74744 0.75176 0.74611 -0.02431 -0.06801 0.00629  138  GLY A O     
1089 N N     . GLU A 139 ? 0.66381 0.67638 0.66333 -0.02166 -0.07243 0.01001  139  GLU A N     
1090 C CA    . GLU A 139 ? 0.60732 0.62619 0.61893 -0.02208 -0.07017 0.01314  139  GLU A CA    
1091 C C     . GLU A 139 ? 0.53458 0.55238 0.54654 -0.01954 -0.06330 0.01493  139  GLU A C     
1092 O O     . GLU A 139 ? 0.49345 0.51529 0.51435 -0.01996 -0.06050 0.01687  139  GLU A O     
1093 C CB    . GLU A 139 ? 0.62917 0.65587 0.64691 -0.02120 -0.07395 0.01603  139  GLU A CB    
1094 C CG    . GLU A 139 ? 0.70578 0.73290 0.71894 -0.02230 -0.08107 0.01439  139  GLU A CG    
1095 C CD    . GLU A 139 ? 0.75591 0.79175 0.77669 -0.02162 -0.08528 0.01739  139  GLU A CD    
1096 O OE1   . GLU A 139 ? 0.78580 0.82612 0.81304 -0.02485 -0.09033 0.01667  139  GLU A OE1   
1097 O OE2   . GLU A 139 ? 0.78233 0.82040 0.80257 -0.01784 -0.08377 0.02047  139  GLU A OE2   
1098 N N     . GLY A 140 ? 0.46858 0.48130 0.47106 -0.01705 -0.06052 0.01428  140  GLY A N     
1099 C CA    . GLY A 140 ? 0.42266 0.43399 0.42507 -0.01503 -0.05434 0.01558  140  GLY A CA    
1100 C C     . GLY A 140 ? 0.45507 0.46141 0.45507 -0.01622 -0.05107 0.01315  140  GLY A C     
1101 O O     . GLY A 140 ? 0.48393 0.48733 0.48256 -0.01851 -0.05334 0.01051  140  GLY A O     
1102 N N     . GLY A 141 ? 0.35693 0.36213 0.35647 -0.01455 -0.04578 0.01407  141  GLY A N     
1103 C CA    . GLY A 141 ? 0.36856 0.36967 0.36616 -0.01519 -0.04251 0.01218  141  GLY A CA    
1104 C C     . GLY A 141 ? 0.31098 0.31259 0.30987 -0.01347 -0.03710 0.01373  141  GLY A C     
1105 O O     . GLY A 141 ? 0.26737 0.27208 0.26910 -0.01192 -0.03577 0.01612  141  GLY A O     
1106 N N     . GLY A 142 ? 0.25772 0.25601 0.25450 -0.01370 -0.03416 0.01219  142  GLY A N     
1107 C CA    . GLY A 142 ? 0.21662 0.21506 0.21395 -0.01237 -0.02931 0.01311  142  GLY A CA    
1108 C C     . GLY A 142 ? 0.26618 0.26489 0.26815 -0.01373 -0.02727 0.01295  142  GLY A C     
1109 O O     . GLY A 142 ? 0.25608 0.25315 0.25905 -0.01556 -0.02915 0.01174  142  GLY A O     
1110 N N     . VAL A 143 ? 0.18234 0.18284 0.18684 -0.01283 -0.02344 0.01423  143  VAL A N     
1111 C CA    . VAL A 143 ? 0.21413 0.21532 0.22237 -0.01378 -0.02106 0.01446  143  VAL A CA    
1112 C C     . VAL A 143 ? 0.20398 0.20458 0.20996 -0.01225 -0.01699 0.01440  143  VAL A C     
1113 O O     . VAL A 143 ? 0.18570 0.18667 0.18998 -0.01076 -0.01568 0.01497  143  VAL A O     
1114 C CB    . VAL A 143 ? 0.27019 0.27632 0.28647 -0.01488 -0.02111 0.01652  143  VAL A CB    
1115 C CG1   . VAL A 143 ? 0.26148 0.27093 0.28008 -0.01300 -0.01927 0.01810  143  VAL A CG1   
1116 C CG2   . VAL A 143 ? 0.30554 0.31215 0.32484 -0.01614 -0.01888 0.01694  143  VAL A CG2   
1117 N N     . ILE A 144 ? 0.17708 0.17660 0.18307 -0.01272 -0.01517 0.01379  144  ILE A N     
1118 C CA    . ILE A 144 ? 0.18408 0.18401 0.18913 -0.01168 -0.01155 0.01379  144  ILE A CA    
1119 C C     . ILE A 144 ? 0.20358 0.20731 0.21392 -0.01186 -0.00966 0.01541  144  ILE A C     
1120 O O     . ILE A 144 ? 0.20844 0.21406 0.22292 -0.01316 -0.01006 0.01635  144  ILE A O     
1121 C CB    . ILE A 144 ? 0.17552 0.17315 0.17829 -0.01179 -0.01065 0.01254  144  ILE A CB    
1122 C CG1   . ILE A 144 ? 0.21748 0.21143 0.21491 -0.01114 -0.01212 0.01059  144  ILE A CG1   
1123 C CG2   . ILE A 144 ? 0.19861 0.19747 0.20095 -0.01096 -0.00730 0.01254  144  ILE A CG2   
1124 C CD1   . ILE A 144 ? 0.22742 0.21891 0.22336 -0.01096 -0.01177 0.00936  144  ILE A CD1   
1125 N N     . GLN A 145 ? 0.18385 0.18853 0.19397 -0.01059 -0.00747 0.01572  145  GLN A N     
1126 C CA    . GLN A 145 ? 0.17611 0.18380 0.19012 -0.01031 -0.00505 0.01661  145  GLN A CA    
1127 C C     . GLN A 145 ? 0.17372 0.18062 0.18535 -0.01003 -0.00224 0.01560  145  GLN A C     
1128 O O     . GLN A 145 ? 0.16246 0.16697 0.17001 -0.00981 -0.00201 0.01444  145  GLN A O     
1129 C CB    . GLN A 145 ? 0.18441 0.19339 0.20034 -0.00891 -0.00478 0.01753  145  GLN A CB    
1130 C CG    . GLN A 145 ? 0.16679 0.17702 0.18493 -0.00894 -0.00801 0.01861  145  GLN A CG    
1131 C CD    . GLN A 145 ? 0.27850 0.29337 0.30341 -0.00963 -0.00843 0.01993  145  GLN A CD    
1132 O OE1   . GLN A 145 ? 0.29161 0.30865 0.31913 -0.00992 -0.00595 0.02015  145  GLN A OE1   
1133 N NE2   . GLN A 145 ? 0.27099 0.28782 0.29877 -0.00996 -0.01158 0.02087  145  GLN A NE2   
1134 N N     . GLY A 146 ? 0.18017 0.18959 0.19446 -0.01005 -0.00012 0.01600  146  GLY A N     
1135 C CA    . GLY A 146 ? 0.18563 0.19476 0.19772 -0.00990 0.00223  0.01494  146  GLY A CA    
1136 C C     . GLY A 146 ? 0.18924 0.19680 0.19918 -0.00899 0.00367  0.01395  146  GLY A C     
1137 O O     . GLY A 146 ? 0.16668 0.17345 0.17409 -0.00919 0.00489  0.01276  146  GLY A O     
1138 N N     . SER A 147 ? 0.13474 0.14181 0.14585 -0.00807 0.00342  0.01457  147  SER A N     
1139 C CA    . SER A 147 ? 0.13945 0.14437 0.14891 -0.00731 0.00488  0.01399  147  SER A CA    
1140 C C     . SER A 147 ? 0.15561 0.15958 0.16617 -0.00614 0.00365  0.01534  147  SER A C     
1141 O O     . SER A 147 ? 0.16827 0.17438 0.18197 -0.00578 0.00203  0.01652  147  SER A O     
1142 C CB    . SER A 147 ? 0.17692 0.18271 0.18755 -0.00699 0.00745  0.01302  147  SER A CB    
1143 O OG    . SER A 147 ? 0.18211 0.19019 0.19672 -0.00593 0.00790  0.01384  147  SER A OG    
1144 N N     . ALA A 148 ? 0.15154 0.15242 0.15967 -0.00565 0.00432  0.01535  148  ALA A N     
1145 C CA    . ALA A 148 ? 0.14345 0.14298 0.15228 -0.00423 0.00323  0.01698  148  ALA A CA    
1146 C C     . ALA A 148 ? 0.15114 0.15226 0.16462 -0.00265 0.00417  0.01742  148  ALA A C     
1147 O O     . ALA A 148 ? 0.16417 0.16631 0.18026 -0.00123 0.00259  0.01902  148  ALA A O     
1148 C CB    . ALA A 148 ? 0.14661 0.14202 0.15167 -0.00422 0.00410  0.01724  148  ALA A CB    
1149 N N     . SER A 149 ? 0.17157 0.17318 0.18608 -0.00270 0.00669  0.01592  149  SER A N     
1150 C CA    . SER A 149 ? 0.18056 0.18414 0.19936 -0.00097 0.00803  0.01593  149  SER A CA    
1151 C C     . SER A 149 ? 0.17682 0.18558 0.20002 -0.00085 0.00677  0.01709  149  SER A C     
1152 O O     . SER A 149 ? 0.18007 0.19105 0.20762 0.00095  0.00642  0.01826  149  SER A O     
1153 C CB    . SER A 149 ? 0.18394 0.18726 0.20195 -0.00130 0.01090  0.01370  149  SER A CB    
1154 O OG    . SER A 149 ? 0.22872 0.22729 0.24346 -0.00167 0.01192  0.01258  149  SER A OG    
1155 N N     . GLU A 150 ? 0.16509 0.17587 0.18761 -0.00279 0.00605  0.01689  150  GLU A N     
1156 C CA    . GLU A 150 ? 0.16515 0.18046 0.19194 -0.00333 0.00467  0.01817  150  GLU A CA    
1157 C C     . GLU A 150 ? 0.17204 0.18763 0.20016 -0.00306 0.00133  0.01973  150  GLU A C     
1158 O O     . GLU A 150 ? 0.15816 0.17784 0.19153 -0.00259 0.00019  0.02107  150  GLU A O     
1159 C CB    . GLU A 150 ? 0.18662 0.20272 0.21182 -0.00554 0.00448  0.01775  150  GLU A CB    
1160 C CG    . GLU A 150 ? 0.27835 0.29586 0.30320 -0.00575 0.00746  0.01674  150  GLU A CG    
1161 C CD    . GLU A 150 ? 0.29821 0.31497 0.31987 -0.00755 0.00723  0.01626  150  GLU A CD    
1162 O OE1   . GLU A 150 ? 0.42868 0.44787 0.45238 -0.00875 0.00669  0.01743  150  GLU A OE1   
1163 O OE2   . GLU A 150 ? 0.30314 0.31696 0.32062 -0.00777 0.00754  0.01490  150  GLU A OE2   
1164 N N     . ALA A 151 ? 0.14175 0.15344 0.16517 -0.00336 -0.00029 0.01960  151  ALA A N     
1165 C CA    . ALA A 151 ? 0.16717 0.17887 0.19064 -0.00306 -0.00368 0.02094  151  ALA A CA    
1166 C C     . ALA A 151 ? 0.15690 0.16961 0.18379 -0.00061 -0.00402 0.02246  151  ALA A C     
1167 O O     . ALA A 151 ? 0.15283 0.16873 0.18338 -0.00014 -0.00669 0.02389  151  ALA A O     
1168 C CB    . ALA A 151 ? 0.13498 0.14226 0.15184 -0.00363 -0.00472 0.02042  151  ALA A CB    
1169 N N     . THR A 152 ? 0.14071 0.15068 0.16670 0.00099  -0.00149 0.02214  152  THR A N     
1170 C CA    . THR A 152 ? 0.14678 0.15699 0.17612 0.00379  -0.00160 0.02358  152  THR A CA    
1171 C C     . THR A 152 ? 0.13710 0.15333 0.17386 0.00492  -0.00099 0.02399  152  THR A C     
1172 O O     . THR A 152 ? 0.13666 0.15586 0.17794 0.00679  -0.00283 0.02573  152  THR A O     
1173 C CB    . THR A 152 ? 0.15002 0.15506 0.17671 0.00502  0.00119  0.02283  152  THR A CB    
1174 O OG1   . THR A 152 ? 0.14410 0.14421 0.16474 0.00412  0.00039  0.02324  152  THR A OG1   
1175 C CG2   . THR A 152 ? 0.17127 0.17623 0.20208 0.00835  0.00155  0.02407  152  THR A CG2   
1176 N N     . LEU A 153 ? 0.13928 0.15784 0.17744 0.00384  0.00158  0.02257  153  LEU A N     
1177 C CA    . LEU A 153 ? 0.14369 0.16866 0.18878 0.00461  0.00263  0.02309  153  LEU A CA    
1178 C C     . LEU A 153 ? 0.14815 0.17812 0.19741 0.00313  -0.00071 0.02474  153  LEU A C     
1179 O O     . LEU A 153 ? 0.14702 0.18235 0.20301 0.00455  -0.00146 0.02617  153  LEU A O     
1180 C CB    . LEU A 153 ? 0.14795 0.17413 0.19239 0.00343  0.00602  0.02144  153  LEU A CB    
1181 C CG    . LEU A 153 ? 0.15845 0.19172 0.20954 0.00383  0.00773  0.02210  153  LEU A CG    
1182 C CD1   . LEU A 153 ? 0.17244 0.20794 0.22852 0.00754  0.00918  0.02243  153  LEU A CD1   
1183 C CD2   . LEU A 153 ? 0.19975 0.23369 0.24861 0.00248  0.01093  0.02067  153  LEU A CD2   
1184 N N     . VAL A 154 ? 0.16459 0.19297 0.21023 0.00028  -0.00279 0.02444  154  VAL A N     
1185 C CA    . VAL A 154 ? 0.15194 0.18409 0.20100 -0.00156 -0.00633 0.02563  154  VAL A CA    
1186 C C     . VAL A 154 ? 0.16109 0.19438 0.21218 0.00014  -0.00977 0.02716  154  VAL A C     
1187 O O     . VAL A 154 ? 0.15542 0.19453 0.21311 0.00002  -0.01188 0.02855  154  VAL A O     
1188 C CB    . VAL A 154 ? 0.17459 0.20315 0.21823 -0.00446 -0.00801 0.02460  154  VAL A CB    
1189 C CG1   . VAL A 154 ? 0.22688 0.25768 0.27284 -0.00625 -0.01238 0.02542  154  VAL A CG1   
1190 C CG2   . VAL A 154 ? 0.17739 0.20628 0.22063 -0.00618 -0.00526 0.02375  154  VAL A CG2   
1191 N N     . ALA A 155 ? 0.15450 0.18254 0.20009 0.00165  -0.01044 0.02714  155  ALA A N     
1192 C CA    . ALA A 155 ? 0.16037 0.18900 0.20688 0.00349  -0.01385 0.02892  155  ALA A CA    
1193 C C     . ALA A 155 ? 0.14016 0.17320 0.19403 0.00669  -0.01294 0.03038  155  ALA A C     
1194 O O     . ALA A 155 ? 0.15442 0.19213 0.21330 0.00766  -0.01615 0.03212  155  ALA A O     
1195 C CB    . ALA A 155 ? 0.16372 0.18542 0.20222 0.00436  -0.01416 0.02894  155  ALA A CB    
1196 N N     . LEU A 156 ? 0.14275 0.17450 0.19744 0.00848  -0.00868 0.02953  156  LEU A N     
1197 C CA    . LEU A 156 ? 0.13452 0.17026 0.19623 0.01198  -0.00730 0.03052  156  LEU A CA    
1198 C C     . LEU A 156 ? 0.15686 0.20172 0.22731 0.01124  -0.00765 0.03125  156  LEU A C     
1199 O O     . LEU A 156 ? 0.14107 0.19143 0.21850 0.01352  -0.00927 0.03299  156  LEU A O     
1200 C CB    . LEU A 156 ? 0.14487 0.17688 0.20495 0.01374  -0.00249 0.02879  156  LEU A CB    
1201 C CG    . LEU A 156 ? 0.16015 0.19463 0.22641 0.01805  -0.00049 0.02928  156  LEU A CG    
1202 C CD1   . LEU A 156 ? 0.13944 0.16589 0.20102 0.02029  0.00205  0.02811  156  LEU A CD1   
1203 C CD2   . LEU A 156 ? 0.18089 0.22244 0.25338 0.01809  0.00267  0.02840  156  LEU A CD2   
1204 N N     . LEU A 157 ? 0.12090 0.16769 0.19136 0.00804  -0.00616 0.03016  157  LEU A N     
1205 C CA    . LEU A 157 ? 0.14983 0.20523 0.22859 0.00675  -0.00612 0.03112  157  LEU A CA    
1206 C C     . LEU A 157 ? 0.16086 0.22031 0.24338 0.00513  -0.01140 0.03277  157  LEU A C     
1207 O O     . LEU A 157 ? 0.15046 0.21799 0.24192 0.00568  -0.01238 0.03432  157  LEU A O     
1208 C CB    . LEU A 157 ? 0.14118 0.19657 0.21801 0.00345  -0.00354 0.02995  157  LEU A CB    
1209 C CG    . LEU A 157 ? 0.16018 0.21335 0.23427 0.00487  0.00166  0.02827  157  LEU A CG    
1210 C CD1   . LEU A 157 ? 0.15280 0.20543 0.22383 0.00153  0.00345  0.02747  157  LEU A CD1   
1211 C CD2   . LEU A 157 ? 0.16323 0.22262 0.24467 0.00808  0.00468  0.02875  157  LEU A CD2   
1212 N N     . ALA A 158 ? 0.14654 0.20082 0.22243 0.00312  -0.01487 0.03233  158  ALA A N     
1213 C CA    . ALA A 158 ? 0.15868 0.21601 0.23693 0.00167  -0.02033 0.03348  158  ALA A CA    
1214 C C     . ALA A 158 ? 0.16587 0.22608 0.24793 0.00537  -0.02273 0.03537  158  ALA A C     
1215 O O     . ALA A 158 ? 0.15411 0.22156 0.24366 0.00518  -0.02599 0.03687  158  ALA A O     
1216 C CB    . ALA A 158 ? 0.19008 0.24051 0.25915 -0.00071 -0.02311 0.03220  158  ALA A CB    
1217 N N     . ALA A 159 ? 0.16764 0.22228 0.24491 0.00872  -0.02126 0.03546  159  ALA A N     
1218 C CA    . ALA A 159 ? 0.14894 0.20549 0.22961 0.01275  -0.02328 0.03757  159  ALA A CA    
1219 C C     . ALA A 159 ? 0.18106 0.24591 0.27268 0.01534  -0.02125 0.03857  159  ALA A C     
1220 O O     . ALA A 159 ? 0.18257 0.25347 0.28095 0.01749  -0.02435 0.04062  159  ALA A O     
1221 C CB    . ALA A 159 ? 0.14298 0.19092 0.21627 0.01557  -0.02146 0.03754  159  ALA A CB    
1222 N N     . ARG A 160 ? 0.16639 0.23199 0.25982 0.01535  -0.01603 0.03715  160  ARG A N     
1223 C CA    . ARG A 160 ? 0.17315 0.24689 0.27662 0.01792  -0.01331 0.03782  160  ARG A CA    
1224 C C     . ARG A 160 ? 0.17040 0.25450 0.28312 0.01548  -0.01602 0.03925  160  ARG A C     
1225 O O     . ARG A 160 ? 0.15939 0.25146 0.28138 0.01811  -0.01721 0.04103  160  ARG A O     
1226 C CB    . ARG A 160 ? 0.15225 0.22439 0.25419 0.01784  -0.00720 0.03573  160  ARG A CB    
1227 C CG    . ARG A 160 ? 0.18883 0.26764 0.29922 0.02159  -0.00336 0.03592  160  ARG A CG    
1228 C CD    . ARG A 160 ? 0.21353 0.29145 0.32166 0.02076  0.00234  0.03374  160  ARG A CD    
1229 N NE    . ARG A 160 ? 0.16965 0.25202 0.27913 0.01593  0.00251  0.03395  160  ARG A NE    
1230 C CZ    . ARG A 160 ? 0.17213 0.25479 0.27964 0.01432  0.00683  0.03263  160  ARG A CZ    
1231 N NH1   . ARG A 160 ? 0.16358 0.24256 0.26739 0.01699  0.01131  0.03057  160  ARG A NH1   
1232 N NH2   . ARG A 160 ? 0.18679 0.27324 0.29584 0.00989  0.00650  0.03342  160  ARG A NH2   
1233 N N     . THR A 161 ? 0.17311 0.25723 0.28381 0.01039  -0.01710 0.03855  161  THR A N     
1234 C CA    . THR A 161 ? 0.18023 0.27345 0.29958 0.00725  -0.01984 0.03985  161  THR A CA    
1235 C C     . THR A 161 ? 0.19888 0.29545 0.32141 0.00787  -0.02620 0.04149  161  THR A C     
1236 O O     . THR A 161 ? 0.19859 0.30515 0.33167 0.00785  -0.02819 0.04319  161  THR A O     
1237 C CB    . THR A 161 ? 0.20610 0.29645 0.32126 0.00168  -0.02023 0.03870  161  THR A CB    
1238 O OG1   . THR A 161 ? 0.22545 0.31221 0.33660 0.00137  -0.01464 0.03732  161  THR A OG1   
1239 C CG2   . THR A 161 ? 0.26031 0.35990 0.38513 -0.00202 -0.02241 0.04010  161  THR A CG2   
1240 N N     . LYS A 162 ? 0.17342 0.26219 0.28696 0.00843  -0.02948 0.04112  162  LYS A N     
1241 C CA    . LYS A 162 ? 0.21084 0.30230 0.32584 0.00883  -0.03593 0.04263  162  LYS A CA    
1242 C C     . LYS A 162 ? 0.20878 0.30583 0.33111 0.01419  -0.03651 0.04490  162  LYS A C     
1243 O O     . LYS A 162 ? 0.18264 0.28811 0.31302 0.01440  -0.04090 0.04666  162  LYS A O     
1244 C CB    . LYS A 162 ? 0.23122 0.31278 0.33377 0.00824  -0.03875 0.04173  162  LYS A CB    
1245 C CG    . LYS A 162 ? 0.27982 0.36363 0.38203 0.00789  -0.04582 0.04294  162  LYS A CG    
1246 C CD    . LYS A 162 ? 0.33372 0.40790 0.42283 0.00678  -0.04806 0.04175  162  LYS A CD    
1247 C CE    . LYS A 162 ? 0.38545 0.46143 0.47294 0.00747  -0.05488 0.04318  162  LYS A CE    
1248 N NZ    . LYS A 162 ? 0.50433 0.57151 0.57869 0.00617  -0.05691 0.04187  162  LYS A NZ    
1249 N N     . VAL A 163 ? 0.18656 0.27904 0.30653 0.01863  -0.03229 0.04486  163  VAL A N     
1250 C CA    . VAL A 163 ? 0.17741 0.27393 0.30381 0.02427  -0.03289 0.04702  163  VAL A CA    
1251 C C     . VAL A 163 ? 0.20565 0.31409 0.34564 0.02554  -0.03065 0.04780  163  VAL A C     
1252 O O     . VAL A 163 ? 0.19136 0.30758 0.34014 0.02881  -0.03335 0.05000  163  VAL A O     
1253 C CB    . VAL A 163 ? 0.20897 0.29597 0.32858 0.02855  -0.02917 0.04661  163  VAL A CB    
1254 C CG1   . VAL A 163 ? 0.18842 0.27358 0.30797 0.02863  -0.02224 0.04431  163  VAL A CG1   
1255 C CG2   . VAL A 163 ? 0.21271 0.30227 0.33785 0.03461  -0.03072 0.04914  163  VAL A CG2   
1256 N N     . ILE A 164 ? 0.19377 0.30436 0.33587 0.02306  -0.02574 0.04621  164  ILE A N     
1257 C CA    . ILE A 164 ? 0.20150 0.32419 0.35647 0.02370  -0.02328 0.04708  164  ILE A CA    
1258 C C     . ILE A 164 ? 0.17854 0.31124 0.34216 0.02047  -0.02887 0.04888  164  ILE A C     
1259 O O     . ILE A 164 ? 0.18361 0.32703 0.35886 0.02302  -0.03010 0.05082  164  ILE A O     
1260 C CB    . ILE A 164 ? 0.21172 0.33425 0.36575 0.02096  -0.01717 0.04526  164  ILE A CB    
1261 C CG1   . ILE A 164 ? 0.20466 0.31954 0.35245 0.02478  -0.01143 0.04338  164  ILE A CG1   
1262 C CG2   . ILE A 164 ? 0.21283 0.34880 0.38007 0.02024  -0.01511 0.04654  164  ILE A CG2   
1263 C CD1   . ILE A 164 ? 0.24057 0.35200 0.38300 0.02130  -0.00671 0.04132  164  ILE A CD1   
1264 N N     . HIS A 165 ? 0.17515 0.30454 0.33342 0.01478  -0.03240 0.04810  165  HIS A N     
1265 C CA    . HIS A 165 ? 0.21432 0.35218 0.38002 0.01093  -0.03809 0.04934  165  HIS A CA    
1266 C C     . HIS A 165 ? 0.18516 0.32611 0.35336 0.01411  -0.04435 0.05120  165  HIS A C     
1267 O O     . HIS A 165 ? 0.17862 0.33092 0.35813 0.01372  -0.04795 0.05298  165  HIS A O     
1268 C CB    . HIS A 165 ? 0.22184 0.35329 0.37959 0.00459  -0.04058 0.04762  165  HIS A CB    
1269 C CG    . HIS A 165 ? 0.34893 0.48114 0.50812 0.00040  -0.03598 0.04671  165  HIS A CG    
1270 N ND1   . HIS A 165 ? 0.41126 0.53543 0.56183 -0.00431 -0.03629 0.04490  165  HIS A ND1   
1271 C CD2   . HIS A 165 ? 0.36949 0.50961 0.53757 0.00035  -0.03092 0.04755  165  HIS A CD2   
1272 C CE1   . HIS A 165 ? 0.35050 0.47724 0.50449 -0.00711 -0.03184 0.04490  165  HIS A CE1   
1273 N NE2   . HIS A 165 ? 0.41834 0.55482 0.58269 -0.00449 -0.02842 0.04652  165  HIS A NE2   
1274 N N     . ARG A 166 ? 0.18172 0.31299 0.33960 0.01720  -0.04580 0.05104  166  ARG A N     
1275 C CA    . ARG A 166 ? 0.18097 0.31444 0.34010 0.02067  -0.05166 0.05321  166  ARG A CA    
1276 C C     . ARG A 166 ? 0.19773 0.34027 0.36872 0.02656  -0.05015 0.05545  166  ARG A C     
1277 O O     . ARG A 166 ? 0.18721 0.33963 0.36747 0.02773  -0.05507 0.05760  166  ARG A O     
1278 C CB    . ARG A 166 ? 0.19504 0.31569 0.34016 0.02282  -0.05259 0.05292  166  ARG A CB    
1279 C CG    . ARG A 166 ? 0.20108 0.32310 0.34683 0.02748  -0.05774 0.05573  166  ARG A CG    
1280 C CD    . ARG A 166 ? 0.22761 0.33788 0.35880 0.02780  -0.06020 0.05573  166  ARG A CD    
1281 N NE    . ARG A 166 ? 0.29565 0.39472 0.41760 0.02860  -0.05421 0.05416  166  ARG A NE    
1282 C CZ    . ARG A 166 ? 0.26905 0.36325 0.38980 0.03374  -0.05079 0.05527  166  ARG A CZ    
1283 N NH1   . ARG A 166 ? 0.26046 0.35961 0.38862 0.03909  -0.05240 0.05803  166  ARG A NH1   
1284 N NH2   . ARG A 166 ? 0.24262 0.32666 0.35477 0.03354  -0.04577 0.05352  166  ARG A NH2   
1285 N N     . LEU A 167 ? 0.18680 0.32621 0.35771 0.03048  -0.04344 0.05482  167  LEU A N     
1286 C CA    . LEU A 167 ? 0.20277 0.34961 0.38421 0.03682  -0.04144 0.05658  167  LEU A CA    
1287 C C     . LEU A 167 ? 0.19633 0.35846 0.39301 0.03547  -0.04058 0.05739  167  LEU A C     
1288 O O     . LEU A 167 ? 0.18960 0.36180 0.39757 0.03966  -0.04235 0.05960  167  LEU A O     
1289 C CB    . LEU A 167 ? 0.22548 0.36429 0.40222 0.04096  -0.03430 0.05505  167  LEU A CB    
1290 C CG    . LEU A 167 ? 0.26991 0.39433 0.43340 0.04320  -0.03479 0.05478  167  LEU A CG    
1291 C CD1   . LEU A 167 ? 0.28039 0.39797 0.44119 0.04747  -0.02801 0.05322  167  LEU A CD1   
1292 C CD2   . LEU A 167 ? 0.23094 0.35574 0.39490 0.04684  -0.04106 0.05782  167  LEU A CD2   
1293 N N     . GLN A 168 ? 0.19490 0.35919 0.39241 0.02972  -0.03785 0.05586  168  GLN A N     
1294 C CA    . GLN A 168 ? 0.21852 0.39744 0.43046 0.02760  -0.03691 0.05694  168  GLN A CA    
1295 C C     . GLN A 168 ? 0.23805 0.42565 0.45702 0.02416  -0.04484 0.05869  168  GLN A C     
1296 O O     . GLN A 168 ? 0.26865 0.47041 0.50208 0.02435  -0.04567 0.06049  168  GLN A O     
1297 C CB    . GLN A 168 ? 0.21813 0.39594 0.42813 0.02229  -0.03164 0.05519  168  GLN A CB    
1298 C CG    . GLN A 168 ? 0.23719 0.41257 0.44585 0.02599  -0.02321 0.05386  168  GLN A CG    
1299 C CD    . GLN A 168 ? 0.24833 0.42325 0.45497 0.02084  -0.01824 0.05255  168  GLN A CD    
1300 O OE1   . GLN A 168 ? 0.24223 0.41251 0.44308 0.01482  -0.02067 0.05193  168  GLN A OE1   
1301 N NE2   . GLN A 168 ? 0.30514 0.48470 0.51629 0.02339  -0.01122 0.05216  168  GLN A NE2   
1302 N N     . ALA A 169 ? 0.20352 0.38324 0.41260 0.02097  -0.05071 0.05806  169  ALA A N     
1303 C CA    . ALA A 169 ? 0.20723 0.39439 0.42179 0.01814  -0.05894 0.05941  169  ALA A CA    
1304 C C     . ALA A 169 ? 0.23264 0.42590 0.45339 0.02453  -0.06302 0.06205  169  ALA A C     
1305 O O     . ALA A 169 ? 0.20909 0.41504 0.44179 0.02394  -0.06788 0.06390  169  ALA A O     
1306 C CB    . ALA A 169 ? 0.19743 0.37381 0.39852 0.01345  -0.06384 0.05764  169  ALA A CB    
1307 N N     . ALA A 170 ? 0.23904 0.42349 0.45215 0.03066  -0.06121 0.06239  170  ALA A N     
1308 C CA    . ALA A 170 ? 0.21906 0.40797 0.43726 0.03726  -0.06500 0.06522  170  ALA A CA    
1309 C C     . ALA A 170 ? 0.24491 0.44672 0.47911 0.04202  -0.06123 0.06676  170  ALA A C     
1310 O O     . ALA A 170 ? 0.23018 0.44326 0.47547 0.04501  -0.06583 0.06935  170  ALA A O     
1311 C CB    . ALA A 170 ? 0.19195 0.36659 0.39698 0.04211  -0.06389 0.06533  170  ALA A CB    
1312 N N     . SER A 171 ? 0.25153 0.45226 0.48711 0.04294  -0.05291 0.06516  171  SER A N     
1313 C CA    . SER A 171 ? 0.33425 0.54678 0.58415 0.04761  -0.04808 0.06613  171  SER A CA    
1314 C C     . SER A 171 ? 0.32108 0.53811 0.57482 0.04266  -0.04187 0.06438  171  SER A C     
1315 O O     . SER A 171 ? 0.37987 0.58866 0.62632 0.04316  -0.03504 0.06218  171  SER A O     
1316 C CB    . SER A 171 ? 0.32000 0.52526 0.56660 0.05589  -0.04349 0.06602  171  SER A CB    
1317 O OG    . SER A 171 ? 0.31925 0.51754 0.55961 0.05984  -0.04904 0.06781  171  SER A OG    
1318 N N     . PRO A 172 ? 0.39308 0.62337 0.65840 0.03773  -0.04410 0.06546  172  PRO A N     
1319 C CA    . PRO A 172 ? 0.39453 0.62867 0.66290 0.03226  -0.03852 0.06429  172  PRO A CA    
1320 C C     . PRO A 172 ? 0.47469 0.71534 0.75079 0.03704  -0.02995 0.06416  172  PRO A C     
1321 O O     . PRO A 172 ? 0.47903 0.72359 0.75789 0.03332  -0.02445 0.06351  172  PRO A O     
1322 C CB    . PRO A 172 ? 0.38561 0.63179 0.66435 0.02616  -0.04387 0.06555  172  PRO A CB    
1323 C CG    . PRO A 172 ? 0.33250 0.57648 0.60799 0.02698  -0.05299 0.06632  172  PRO A CG    
1324 C CD    . PRO A 172 ? 0.37392 0.61414 0.64746 0.03604  -0.05204 0.06725  172  PRO A CD    
1325 N N     . GLU A 173 ? 0.68025 0.92183 0.95955 0.04541  -0.02870 0.06478  173  GLU A N     
1326 C CA    . GLU A 173 ? 0.66674 0.91250 0.95123 0.05078  -0.02050 0.06374  173  GLU A CA    
1327 C C     . GLU A 173 ? 0.73109 0.96304 1.00301 0.05304  -0.01412 0.06112  173  GLU A C     
1328 O O     . GLU A 173 ? 0.78341 1.01671 1.05815 0.05889  -0.00769 0.06006  173  GLU A O     
1329 C CB    . GLU A 173 ? 0.68350 0.93358 0.97417 0.05858  -0.02193 0.06424  173  GLU A CB    
1330 C CG    . GLU A 173 ? 0.78580 1.04757 1.08601 0.05645  -0.02787 0.06543  173  GLU A CG    
1331 C CD    . GLU A 173 ? 0.79400 1.05147 1.09026 0.05756  -0.03692 0.06707  173  GLU A CD    
1332 O OE1   . GLU A 173 ? 0.71376 0.95908 0.99923 0.05802  -0.03898 0.06747  173  GLU A OE1   
1333 O OE2   . GLU A 173 ? 0.83944 1.10579 1.14316 0.05796  -0.04198 0.06797  173  GLU A OE2   
1334 N N     . LEU A 174 ? 0.55407 0.77207 0.81119 0.04842  -0.01571 0.05948  174  LEU A N     
1335 C CA    . LEU A 174 ? 0.46719 0.66999 0.71029 0.05042  -0.01108 0.05666  174  LEU A CA    
1336 C C     . LEU A 174 ? 0.45694 0.65615 0.69352 0.04429  -0.00642 0.05467  174  LEU A C     
1337 O O     . LEU A 174 ? 0.45584 0.65512 0.69035 0.03726  -0.00972 0.05511  174  LEU A O     
1338 C CB    . LEU A 174 ? 0.46457 0.65350 0.69519 0.05076  -0.01653 0.05653  174  LEU A CB    
1339 C CG    . LEU A 174 ? 0.45740 0.63911 0.68507 0.05875  -0.01637 0.05668  174  LEU A CG    
1340 C CD1   . LEU A 174 ? 0.55168 0.74626 0.79421 0.06473  -0.01809 0.05926  174  LEU A CD1   
1341 C CD2   . LEU A 174 ? 0.41731 0.58643 0.63277 0.05775  -0.02210 0.05715  174  LEU A CD2   
1342 N N     . THR A 175 ? 0.37695 0.57268 0.61001 0.04708  0.00105  0.05244  175  THR A N     
1343 C CA    . THR A 175 ? 0.41893 0.60921 0.64357 0.04199  0.00542  0.05048  175  THR A CA    
1344 C C     . THR A 175 ? 0.40532 0.57867 0.61377 0.04044  0.00369  0.04845  175  THR A C     
1345 O O     . THR A 175 ? 0.44199 0.60727 0.64537 0.04431  0.00091  0.04823  175  THR A O     
1346 C CB    . THR A 175 ? 0.42362 0.61708 0.65013 0.04553  0.01401  0.04873  175  THR A CB    
1347 O OG1   . THR A 175 ? 0.41038 0.59125 0.62670 0.05045  0.01665  0.04594  175  THR A OG1   
1348 C CG2   . THR A 175 ? 0.44028 0.64930 0.68279 0.05018  0.01595  0.05049  175  THR A CG2   
1349 N N     . GLN A 176 ? 0.40745 0.57565 0.60800 0.03468  0.00540  0.04719  176  GLN A N     
1350 C CA    . GLN A 176 ? 0.39363 0.54661 0.57925 0.03323  0.00465  0.04506  176  GLN A CA    
1351 C C     . GLN A 176 ? 0.48753 0.63238 0.66711 0.03905  0.00912  0.04267  176  GLN A C     
1352 O O     . GLN A 176 ? 0.41006 0.54402 0.58127 0.04083  0.00681  0.04186  176  GLN A O     
1353 C CB    . GLN A 176 ? 0.42886 0.57882 0.60816 0.02670  0.00643  0.04416  176  GLN A CB    
1354 C CG    . GLN A 176 ? 0.40930 0.54480 0.57388 0.02584  0.00754  0.04155  176  GLN A CG    
1355 C CD    . GLN A 176 ? 0.44346 0.57527 0.60180 0.01909  0.00661  0.04129  176  GLN A CD    
1356 O OE1   . GLN A 176 ? 0.37612 0.51195 0.53826 0.01477  0.00236  0.04299  176  GLN A OE1   
1357 N NE2   . GLN A 176 ? 0.42048 0.54435 0.56919 0.01822  0.01035  0.03909  176  GLN A NE2   
1358 N N     . ALA A 177 ? 0.62919 0.77925 0.81303 0.04208  0.01556  0.04150  177  ALA A N     
1359 C CA    . ALA A 177 ? 0.63649 0.77830 0.81412 0.04728  0.02006  0.03861  177  ALA A CA    
1360 C C     . ALA A 177 ? 0.58969 0.72949 0.77076 0.05394  0.01784  0.03925  177  ALA A C     
1361 O O     . ALA A 177 ? 0.62763 0.75591 0.80061 0.05707  0.01863  0.03733  177  ALA A O     
1362 C CB    . ALA A 177 ? 0.65805 0.80664 0.83942 0.04904  0.02748  0.03705  177  ALA A CB    
1363 N N     . ALA A 178 ? 0.42799 0.57891 0.62127 0.05618  0.01499  0.04207  178  ALA A N     
1364 C CA    . ALA A 178 ? 0.39113 0.54035 0.58794 0.06269  0.01228  0.04321  178  ALA A CA    
1365 C C     . ALA A 178 ? 0.38848 0.52581 0.57561 0.06135  0.00643  0.04400  178  ALA A C     
1366 O O     . ALA A 178 ? 0.37974 0.50885 0.56347 0.06635  0.00573  0.04389  178  ALA A O     
1367 C CB    . ALA A 178 ? 0.42262 0.58730 0.63490 0.06484  0.00974  0.04635  178  ALA A CB    
1368 N N     . ILE A 179 ? 0.35567 0.49172 0.53815 0.05471  0.00234  0.04483  179  ILE A N     
1369 C CA    . ILE A 179 ? 0.31415 0.43871 0.48608 0.05297  -0.00251 0.04525  179  ILE A CA    
1370 C C     . ILE A 179 ? 0.33127 0.44218 0.49046 0.05234  0.00123  0.04221  179  ILE A C     
1371 O O     . ILE A 179 ? 0.24422 0.34432 0.39560 0.05404  -0.00056 0.04220  179  ILE A O     
1372 C CB    . ILE A 179 ? 0.29965 0.42737 0.47068 0.04625  -0.00778 0.04664  179  ILE A CB    
1373 C CG1   . ILE A 179 ? 0.30073 0.44062 0.48365 0.04717  -0.01289 0.04976  179  ILE A CG1   
1374 C CG2   . ILE A 179 ? 0.27087 0.38595 0.42891 0.04370  -0.01134 0.04627  179  ILE A CG2   
1375 C CD1   . ILE A 179 ? 0.29772 0.44553 0.48472 0.04045  -0.01592 0.05057  179  ILE A CD1   
1376 N N     . MET A 180 ? 0.33529 0.44687 0.49250 0.04994  0.00651  0.03974  180  MET A N     
1377 C CA    A MET A 180 ? 0.34994 0.44974 0.49542 0.04868  0.00987  0.03667  180  MET A CA    
1378 C CA    B MET A 180 ? 0.34938 0.44906 0.49475 0.04863  0.00975  0.03671  180  MET A CA    
1379 C C     . MET A 180 ? 0.33586 0.42687 0.47809 0.05453  0.01198  0.03525  180  MET A C     
1380 O O     . MET A 180 ? 0.33697 0.41609 0.46939 0.05386  0.01116  0.03426  180  MET A O     
1381 C CB    A MET A 180 ? 0.41278 0.51677 0.55831 0.04616  0.01535  0.03455  180  MET A CB    
1382 C CB    B MET A 180 ? 0.41389 0.51736 0.55883 0.04585  0.01508  0.03457  180  MET A CB    
1383 C CG    A MET A 180 ? 0.40149 0.50908 0.54583 0.03929  0.01364  0.03539  180  MET A CG    
1384 C CG    B MET A 180 ? 0.39932 0.50805 0.54486 0.03928  0.01307  0.03579  180  MET A CG    
1385 S SD    A MET A 180 ? 0.35393 0.44821 0.48424 0.03464  0.01056  0.03431  180  MET A SD    
1386 S SD    B MET A 180 ? 0.35743 0.45474 0.49057 0.03400  0.00867  0.03546  180  MET A SD    
1387 C CE    A MET A 180 ? 0.32697 0.42363 0.46016 0.03282  0.00280  0.03749  180  MET A CE    
1388 C CE    B MET A 180 ? 0.33674 0.43557 0.46630 0.02821  0.01200  0.03413  180  MET A CE    
1389 N N     . GLU A 181 ? 0.34415 0.44079 0.49473 0.06030  0.01494  0.03506  181  GLU A N     
1390 C CA    . GLU A 181 ? 0.37853 0.46608 0.52610 0.06605  0.01735  0.03331  181  GLU A CA    
1391 C C     . GLU A 181 ? 0.29872 0.37910 0.44439 0.06869  0.01233  0.03586  181  GLU A C     
1392 O O     . GLU A 181 ? 0.32133 0.39193 0.46320 0.07284  0.01376  0.03472  181  GLU A O     
1393 C CB    . GLU A 181 ? 0.42902 0.52443 0.58615 0.07208  0.02199  0.03226  181  GLU A CB    
1394 C CG    . GLU A 181 ? 0.44333 0.55047 0.61347 0.07586  0.01914  0.03572  181  GLU A CG    
1395 C CD    . GLU A 181 ? 0.52237 0.63886 0.70235 0.08137  0.02452  0.03442  181  GLU A CD    
1396 O OE1   . GLU A 181 ? 0.48269 0.59456 0.65813 0.08297  0.03032  0.03061  181  GLU A OE1   
1397 O OE2   . GLU A 181 ? 0.56942 0.69808 0.76162 0.08419  0.02295  0.03709  181  GLU A OE2   
1398 N N     . LYS A 182 ? 0.25060 0.33510 0.39829 0.06627  0.00646  0.03926  182  LYS A N     
1399 C CA    . LYS A 182 ? 0.25039 0.32816 0.39501 0.06829  0.00140  0.04204  182  LYS A CA    
1400 C C     . LYS A 182 ? 0.22077 0.28889 0.35353 0.06298  -0.00148 0.04220  182  LYS A C     
1401 O O     . LYS A 182 ? 0.20369 0.26264 0.33084 0.06469  -0.00394 0.04375  182  LYS A O     
1402 C CB    . LYS A 182 ? 0.23326 0.32216 0.38793 0.07001  -0.00379 0.04590  182  LYS A CB    
1403 C CG    . LYS A 182 ? 0.26613 0.36431 0.43340 0.07667  -0.00184 0.04658  182  LYS A CG    
1404 C CD    . LYS A 182 ? 0.36332 0.45303 0.52840 0.08218  0.00350  0.04398  182  LYS A CD    
1405 C CE    . LYS A 182 ? 0.45440 0.55314 0.63203 0.08944  0.00536  0.04464  182  LYS A CE    
1406 N NZ    . LYS A 182 ? 0.45966 0.54726 0.63465 0.09610  0.00699  0.04399  182  LYS A NZ    
1407 N N     . LEU A 183 ? 0.17730 0.24712 0.30615 0.05678  -0.00110 0.04078  183  LEU A N     
1408 C CA    . LEU A 183 ? 0.19753 0.25954 0.31598 0.05191  -0.00398 0.04098  183  LEU A CA    
1409 C C     . LEU A 183 ? 0.19493 0.24352 0.30358 0.05239  -0.00132 0.03909  183  LEU A C     
1410 O O     . LEU A 183 ? 0.18491 0.23049 0.29280 0.05378  0.00366  0.03615  183  LEU A O     
1411 C CB    . LEU A 183 ? 0.14580 0.21212 0.26255 0.04566  -0.00359 0.03957  183  LEU A CB    
1412 C CG    . LEU A 183 ? 0.19439 0.27267 0.31933 0.04334  -0.00701 0.04146  183  LEU A CG    
1413 C CD1   . LEU A 183 ? 0.19124 0.26980 0.31165 0.03684  -0.00705 0.04012  183  LEU A CD1   
1414 C CD2   . LEU A 183 ? 0.19587 0.27569 0.32247 0.04458  -0.01340 0.04473  183  LEU A CD2   
1415 N N     . VAL A 184 ? 0.17088 0.21157 0.27190 0.05103  -0.00468 0.04075  184  VAL A N     
1416 C CA    . VAL A 184 ? 0.18653 0.21467 0.27802 0.05035  -0.00261 0.03932  184  VAL A CA    
1417 C C     . VAL A 184 ? 0.17066 0.19474 0.25343 0.04512  -0.00542 0.03995  184  VAL A C     
1418 O O     . VAL A 184 ? 0.16625 0.19343 0.24894 0.04418  -0.01012 0.04264  184  VAL A O     
1419 C CB    . VAL A 184 ? 0.20744 0.22807 0.29887 0.05574  -0.00298 0.04116  184  VAL A CB    
1420 C CG1   . VAL A 184 ? 0.21293 0.23404 0.30414 0.05690  -0.00871 0.04565  184  VAL A CG1   
1421 C CG2   . VAL A 184 ? 0.19811 0.20596 0.28077 0.05470  -0.00009 0.03921  184  VAL A CG2   
1422 N N     . ALA A 185 ? 0.15982 0.17752 0.23537 0.04176  -0.00253 0.03726  185  ALA A N     
1423 C CA    . ALA A 185 ? 0.15849 0.17134 0.22533 0.03725  -0.00429 0.03746  185  ALA A CA    
1424 C C     . ALA A 185 ? 0.16496 0.16639 0.22482 0.03798  -0.00332 0.03789  185  ALA A C     
1425 O O     . ALA A 185 ? 0.17927 0.17568 0.24026 0.04101  -0.00046 0.03688  185  ALA A O     
1426 C CB    . ALA A 185 ? 0.16373 0.17847 0.22794 0.03264  -0.00197 0.03436  185  ALA A CB    
1427 N N     . TYR A 186 ? 0.16594 0.16317 0.21854 0.03511  -0.00562 0.03936  186  TYR A N     
1428 C CA    . TYR A 186 ? 0.17250 0.15934 0.21842 0.03523  -0.00497 0.04049  186  TYR A CA    
1429 C C     . TYR A 186 ? 0.16984 0.15279 0.20796 0.03023  -0.00378 0.03883  186  TYR A C     
1430 O O     . TYR A 186 ? 0.16415 0.15196 0.20077 0.02700  -0.00500 0.03798  186  TYR A O     
1431 C CB    . TYR A 186 ? 0.17893 0.16371 0.22314 0.03746  -0.00903 0.04503  186  TYR A CB    
1432 C CG    . TYR A 186 ? 0.20004 0.18700 0.25151 0.04308  -0.01037 0.04726  186  TYR A CG    
1433 C CD1   . TYR A 186 ? 0.22186 0.20320 0.27599 0.04676  -0.00735 0.04653  186  TYR A CD1   
1434 C CD2   . TYR A 186 ? 0.26408 0.25867 0.31983 0.04483  -0.01483 0.05000  186  TYR A CD2   
1435 C CE1   . TYR A 186 ? 0.20912 0.19247 0.27023 0.05243  -0.00848 0.04856  186  TYR A CE1   
1436 C CE2   . TYR A 186 ? 0.29535 0.29268 0.35839 0.05026  -0.01622 0.05221  186  TYR A CE2   
1437 C CZ    . TYR A 186 ? 0.25272 0.24442 0.31850 0.05424  -0.01292 0.05154  186  TYR A CZ    
1438 O OH    . TYR A 186 ? 0.26318 0.25767 0.33659 0.06015  -0.01420 0.05370  186  TYR A OH    
1439 N N     A SER A 187 ? 0.18032 0.15437 0.21386 0.02968  -0.00136 0.03834  187  SER A N     
1440 N N     B SER A 187 ? 0.18067 0.15471 0.21418 0.02969  -0.00140 0.03838  187  SER A N     
1441 C CA    A SER A 187 ? 0.18100 0.15086 0.20733 0.02527  -0.00025 0.03734  187  SER A CA    
1442 C CA    B SER A 187 ? 0.17911 0.14902 0.20543 0.02526  -0.00029 0.03736  187  SER A CA    
1443 C C     A SER A 187 ? 0.19855 0.15827 0.22085 0.02570  0.00109  0.03880  187  SER A C     
1444 C C     B SER A 187 ? 0.19437 0.15410 0.21670 0.02567  0.00114  0.03873  187  SER A C     
1445 O O     A SER A 187 ? 0.20299 0.15847 0.22810 0.02939  0.00145  0.04001  187  SER A O     
1446 O O     B SER A 187 ? 0.20691 0.16240 0.23211 0.02934  0.00160  0.03981  187  SER A O     
1447 C CB    A SER A 187 ? 0.18748 0.15977 0.21409 0.02240  0.00271  0.03303  187  SER A CB    
1448 C CB    B SER A 187 ? 0.18683 0.15940 0.21350 0.02239  0.00260  0.03307  187  SER A CB    
1449 O OG    A SER A 187 ? 0.19537 0.16291 0.22329 0.02354  0.00603  0.03063  187  SER A OG    
1450 O OG    B SER A 187 ? 0.17755 0.15102 0.19906 0.01828  0.00214  0.03249  187  SER A OG    
1451 N N     . SER A 188 ? 0.19414 0.14996 0.21008 0.02189  0.00189  0.03879  188  SER A N     
1452 C CA    . SER A 188 ? 0.19408 0.14027 0.20625 0.02138  0.00347  0.04017  188  SER A CA    
1453 C C     . SER A 188 ? 0.21368 0.15554 0.22799 0.02119  0.00696  0.03645  188  SER A C     
1454 O O     . SER A 188 ? 0.20448 0.15104 0.22133 0.02036  0.00845  0.03262  188  SER A O     
1455 C CB    . SER A 188 ? 0.21783 0.16217 0.22313 0.01715  0.00364  0.04119  188  SER A CB    
1456 O OG    . SER A 188 ? 0.24289 0.17811 0.24496 0.01610  0.00541  0.04272  188  SER A OG    
1457 N N     . ASP A 189 ? 0.22463 0.15706 0.23755 0.02189  0.00821  0.03761  189  ASP A N     
1458 C CA    . ASP A 189 ? 0.24810 0.17544 0.26183 0.02088  0.01138  0.03365  189  ASP A CA    
1459 C C     . ASP A 189 ? 0.23829 0.16589 0.24818 0.01544  0.01302  0.03116  189  ASP A C     
1460 O O     . ASP A 189 ? 0.23121 0.15569 0.24144 0.01393  0.01535  0.02741  189  ASP A O     
1461 C CB    . ASP A 189 ? 0.26950 0.18578 0.28298 0.02295  0.01216  0.03537  189  ASP A CB    
1462 C CG    . ASP A 189 ? 0.25213 0.16218 0.26039 0.02082  0.01130  0.03993  189  ASP A CG    
1463 O OD1   . ASP A 189 ? 0.26715 0.18083 0.27146 0.01709  0.01083  0.04090  189  ASP A OD1   
1464 O OD2   . ASP A 189 ? 0.28764 0.18895 0.29571 0.02307  0.01121  0.04269  189  ASP A OD2   
1465 N N     . GLN A 190 ? 0.21116 0.14270 0.21750 0.01267  0.01177  0.03299  190  GLN A N     
1466 C CA    . GLN A 190 ? 0.22597 0.15958 0.22935 0.00795  0.01309  0.03080  190  GLN A CA    
1467 C C     . GLN A 190 ? 0.19990 0.14297 0.20464 0.00724  0.01247  0.02834  190  GLN A C     
1468 O O     . GLN A 190 ? 0.21211 0.15806 0.21447 0.00380  0.01306  0.02695  190  GLN A O     
1469 C CB    . GLN A 190 ? 0.21832 0.14970 0.21658 0.00537  0.01258  0.03438  190  GLN A CB    
1470 C CG    . GLN A 190 ? 0.25209 0.17369 0.24853 0.00554  0.01326  0.03753  190  GLN A CG    
1471 C CD    . GLN A 190 ? 0.27329 0.18835 0.27095 0.00360  0.01583  0.03453  190  GLN A CD    
1472 O OE1   . GLN A 190 ? 0.30370 0.22010 0.30038 -0.00045 0.01738  0.03194  190  GLN A OE1   
1473 N NE2   . GLN A 190 ? 0.27779 0.18573 0.27772 0.00657  0.01614  0.03471  190  GLN A NE2   
1474 N N     . ALA A 191 ? 0.20574 0.15374 0.21455 0.01043  0.01135  0.02793  191  ALA A N     
1475 C CA    . ALA A 191 ? 0.20222 0.15886 0.21237 0.00970  0.01045  0.02640  191  ALA A CA    
1476 C C     . ALA A 191 ? 0.19172 0.15042 0.20238 0.00753  0.01269  0.02215  191  ALA A C     
1477 O O     . ALA A 191 ? 0.20152 0.15624 0.21306 0.00780  0.01477  0.01978  191  ALA A O     
1478 C CB    . ALA A 191 ? 0.20600 0.16761 0.22111 0.01340  0.00880  0.02729  191  ALA A CB    
1479 N N     . HIS A 192 ? 0.18958 0.15432 0.19940 0.00546  0.01208  0.02116  192  HIS A N     
1480 C CA    . HIS A 192 ? 0.19486 0.16260 0.20504 0.00362  0.01373  0.01758  192  HIS A CA    
1481 C C     . HIS A 192 ? 0.20318 0.17408 0.21769 0.00619  0.01459  0.01587  192  HIS A C     
1482 O O     . HIS A 192 ? 0.18772 0.16129 0.20565 0.00898  0.01341  0.01758  192  HIS A O     
1483 C CB    . HIS A 192 ? 0.20805 0.18120 0.21647 0.00130  0.01259  0.01749  192  HIS A CB    
1484 C CG    . HIS A 192 ? 0.24179 0.21787 0.24998 -0.00069 0.01397  0.01434  192  HIS A CG    
1485 N ND1   . HIS A 192 ? 0.21417 0.19571 0.22474 -0.00009 0.01395  0.01314  192  HIS A ND1   
1486 C CD2   . HIS A 192 ? 0.26778 0.24237 0.27367 -0.00334 0.01527  0.01239  192  HIS A CD2   
1487 C CE1   . HIS A 192 ? 0.25733 0.24027 0.26655 -0.00206 0.01512  0.01069  192  HIS A CE1   
1488 N NE2   . HIS A 192 ? 0.26497 0.24401 0.27154 -0.00402 0.01579  0.01006  192  HIS A NE2   
1489 N N     . SER A 193 ? 0.19251 0.16351 0.20684 0.00524  0.01669  0.01247  193  SER A N     
1490 C CA    . SER A 193 ? 0.20493 0.17890 0.22266 0.00763  0.01814  0.01056  193  SER A CA    
1491 C C     . SER A 193 ? 0.19565 0.17769 0.21639 0.00827  0.01709  0.01161  193  SER A C     
1492 O O     . SER A 193 ? 0.19555 0.18099 0.22004 0.01067  0.01821  0.01096  193  SER A O     
1493 C CB    . SER A 193 ? 0.24348 0.21641 0.25917 0.00603  0.02035  0.00661  193  SER A CB    
1494 O OG    . SER A 193 ? 0.27590 0.25271 0.28924 0.00287  0.01984  0.00592  193  SER A OG    
1495 N N     . SER A 194 ? 0.19515 0.18022 0.21449 0.00617  0.01509  0.01318  194  SER A N     
1496 C CA    . SER A 194 ? 0.21001 0.20200 0.23226 0.00630  0.01381  0.01424  194  SER A CA    
1497 C C     . SER A 194 ? 0.17408 0.16837 0.20112 0.00931  0.01248  0.01654  194  SER A C     
1498 O O     . SER A 194 ? 0.17348 0.17390 0.20471 0.01000  0.01225  0.01696  194  SER A O     
1499 C CB    . SER A 194 ? 0.19471 0.18805 0.21406 0.00365  0.01171  0.01527  194  SER A CB    
1500 O OG    . SER A 194 ? 0.19538 0.18486 0.21229 0.00362  0.01009  0.01722  194  SER A OG    
1501 N N     . VAL A 195 ? 0.19406 0.18380 0.22081 0.01108  0.01151  0.01829  195  VAL A N     
1502 C CA    . VAL A 195 ? 0.17828 0.17046 0.20986 0.01429  0.00992  0.02064  195  VAL A CA    
1503 C C     . VAL A 195 ? 0.18987 0.18396 0.22638 0.01739  0.01240  0.01921  195  VAL A C     
1504 O O     . VAL A 195 ? 0.18473 0.18537 0.22686 0.01911  0.01195  0.02011  195  VAL A O     
1505 C CB    . VAL A 195 ? 0.19238 0.17877 0.22181 0.01559  0.00818  0.02322  195  VAL A CB    
1506 C CG1   . VAL A 195 ? 0.19393 0.18397 0.22821 0.01871  0.00563  0.02606  195  VAL A CG1   
1507 C CG2   . VAL A 195 ? 0.17030 0.15444 0.19387 0.01241  0.00662  0.02415  195  VAL A CG2   
1508 N N     . GLU A 196 ? 0.20747 0.19602 0.24206 0.01809  0.01510  0.01683  196  GLU A N     
1509 C CA    . GLU A 196 ? 0.23312 0.22304 0.27153 0.02119  0.01787  0.01482  196  GLU A CA    
1510 C C     . GLU A 196 ? 0.21867 0.21645 0.25921 0.02018  0.01935  0.01339  196  GLU A C     
1511 O O     . GLU A 196 ? 0.22153 0.22486 0.26757 0.02285  0.02051  0.01353  196  GLU A O     
1512 C CB    . GLU A 196 ? 0.22682 0.20871 0.26162 0.02141  0.02036  0.01185  196  GLU A CB    
1513 C CG    . GLU A 196 ? 0.30300 0.28589 0.34051 0.02450  0.02360  0.00889  196  GLU A CG    
1514 C CD    . GLU A 196 ? 0.45631 0.43032 0.49002 0.02471  0.02568  0.00561  196  GLU A CD    
1515 O OE1   . GLU A 196 ? 0.47516 0.44497 0.50376 0.02096  0.02538  0.00444  196  GLU A OE1   
1516 O OE2   . GLU A 196 ? 0.56257 0.53389 0.59866 0.02861  0.02759  0.00407  196  GLU A OE2   
1517 N N     . ARG A 197 ? 0.19099 0.18957 0.22741 0.01640  0.01940  0.01223  197  ARG A N     
1518 C CA    . ARG A 197 ? 0.18980 0.19525 0.22760 0.01521  0.02073  0.01132  197  ARG A CA    
1519 C C     . ARG A 197 ? 0.18212 0.19492 0.22525 0.01531  0.01876  0.01419  197  ARG A C     
1520 O O     . ARG A 197 ? 0.17616 0.19545 0.22351 0.01609  0.02035  0.01417  197  ARG A O     
1521 C CB    . ARG A 197 ? 0.24403 0.24831 0.27625 0.01134  0.02069  0.00992  197  ARG A CB    
1522 C CG    . ARG A 197 ? 0.33801 0.33607 0.36549 0.01079  0.02254  0.00679  197  ARG A CG    
1523 C CD    . ARG A 197 ? 0.41016 0.40786 0.43279 0.00709  0.02209  0.00566  197  ARG A CD    
1524 N NE    . ARG A 197 ? 0.46854 0.47274 0.49185 0.00584  0.02224  0.00607  197  ARG A NE    
1525 C CZ    . ARG A 197 ? 0.51727 0.52345 0.53834 0.00508  0.02416  0.00395  197  ARG A CZ    
1526 N NH1   . ARG A 197 ? 0.51640 0.51897 0.53450 0.00552  0.02605  0.00079  197  ARG A NH1   
1527 N NH2   . ARG A 197 ? 0.48075 0.49242 0.50233 0.00380  0.02406  0.00506  197  ARG A NH2   
1528 N N     . ALA A 198 ? 0.15721 0.16923 0.20020 0.01443  0.01531  0.01664  198  ALA A N     
1529 C CA    . ALA A 198 ? 0.15393 0.17257 0.20203 0.01430  0.01286  0.01917  198  ALA A CA    
1530 C C     . ALA A 198 ? 0.16569 0.18843 0.22097 0.01820  0.01332  0.02031  198  ALA A C     
1531 O O     . ALA A 198 ? 0.15694 0.18740 0.21816 0.01833  0.01329  0.02136  198  ALA A O     
1532 C CB    . ALA A 198 ? 0.17669 0.19295 0.22208 0.01272  0.00894  0.02113  198  ALA A CB    
1533 N N     . GLY A 199 ? 0.17672 0.19445 0.23192 0.02142  0.01377  0.02024  199  GLY A N     
1534 C CA    . GLY A 199 ? 0.17313 0.19454 0.23539 0.02578  0.01437  0.02120  199  GLY A CA    
1535 C C     . GLY A 199 ? 0.17499 0.20101 0.24070 0.02738  0.01858  0.01901  199  GLY A C     
1536 O O     . GLY A 199 ? 0.18032 0.21392 0.25349 0.02967  0.01915  0.02011  199  GLY A O     
1537 N N     . LEU A 200 ? 0.19643 0.21840 0.25675 0.02617  0.02158  0.01589  200  LEU A N     
1538 C CA    . LEU A 200 ? 0.18785 0.21409 0.25002 0.02750  0.02574  0.01358  200  LEU A CA    
1539 C C     . LEU A 200 ? 0.18139 0.21674 0.24673 0.02495  0.02594  0.01487  200  LEU A C     
1540 O O     . LEU A 200 ? 0.20869 0.25138 0.27987 0.02688  0.02834  0.01507  200  LEU A O     
1541 C CB    . LEU A 200 ? 0.20371 0.22330 0.25850 0.02640  0.02829  0.00987  200  LEU A CB    
1542 C CG    . LEU A 200 ? 0.23834 0.24886 0.29066 0.02916  0.02912  0.00792  200  LEU A CG    
1543 C CD1   . LEU A 200 ? 0.29011 0.29398 0.33471 0.02662  0.03047  0.00450  200  LEU A CD1   
1544 C CD2   . LEU A 200 ? 0.28919 0.30168 0.34666 0.03436  0.03205  0.00670  200  LEU A CD2   
1545 N N     . ILE A 201 ? 0.16552 0.20047 0.22727 0.02064  0.02359  0.01583  201  ILE A N     
1546 C CA    . ILE A 201 ? 0.17100 0.21347 0.23560 0.01787  0.02341  0.01735  201  ILE A CA    
1547 C C     . ILE A 201 ? 0.16321 0.21298 0.23650 0.01892  0.02137  0.02031  201  ILE A C     
1548 O O     . ILE A 201 ? 0.16160 0.21954 0.24077 0.01892  0.02311  0.02127  201  ILE A O     
1549 C CB    . ILE A 201 ? 0.16739 0.20673 0.22625 0.01345  0.02097  0.01768  201  ILE A CB    
1550 C CG1   . ILE A 201 ? 0.19673 0.23107 0.24814 0.01222  0.02321  0.01484  201  ILE A CG1   
1551 C CG2   . ILE A 201 ? 0.17232 0.21844 0.23478 0.01056  0.01994  0.01979  201  ILE A CG2   
1552 C CD1   . ILE A 201 ? 0.20549 0.23613 0.25130 0.00859  0.02082  0.01498  201  ILE A CD1   
1553 N N     . GLY A 202 ? 0.15987 0.20715 0.23415 0.01974  0.01761  0.02192  202  GLY A N     
1554 C CA    . GLY A 202 ? 0.16925 0.22342 0.25162 0.02069  0.01489  0.02470  202  GLY A CA    
1555 C C     . GLY A 202 ? 0.16671 0.22593 0.25673 0.02548  0.01701  0.02500  202  GLY A C     
1556 O O     . GLY A 202 ? 0.17532 0.24242 0.27355 0.02623  0.01522  0.02731  202  GLY A O     
1557 N N     . GLY A 203 ? 0.17005 0.22504 0.25783 0.02878  0.02064  0.02259  203  GLY A N     
1558 C CA    . GLY A 203 ? 0.19328 0.25262 0.28810 0.03389  0.02313  0.02244  203  GLY A CA    
1559 C C     . GLY A 203 ? 0.21150 0.26920 0.31017 0.03770  0.02008  0.02435  203  GLY A C     
1560 O O     . GLY A 203 ? 0.21071 0.27561 0.31818 0.04135  0.02046  0.02566  203  GLY A O     
1561 N N     . VAL A 204 ? 0.18114 0.22983 0.27354 0.03706  0.01710  0.02476  204  VAL A N     
1562 C CA    . VAL A 204 ? 0.16170 0.20798 0.25654 0.04046  0.01381  0.02709  204  VAL A CA    
1563 C C     . VAL A 204 ? 0.19993 0.23453 0.28832 0.04268  0.01502  0.02553  204  VAL A C     
1564 O O     . VAL A 204 ? 0.23192 0.25990 0.31298 0.04033  0.01715  0.02290  204  VAL A O     
1565 C CB    . VAL A 204 ? 0.19220 0.23923 0.28583 0.03738  0.00824  0.02999  204  VAL A CB    
1566 C CG1   . VAL A 204 ? 0.17124 0.22950 0.27195 0.03502  0.00665  0.03151  204  VAL A CG1   
1567 C CG2   . VAL A 204 ? 0.16767 0.20654 0.25111 0.03303  0.00747  0.02888  204  VAL A CG2   
1568 N N     . LYS A 205 ? 0.19970 0.23182 0.29117 0.04718  0.01343  0.02735  205  LYS A N     
1569 C CA    . LYS A 205 ? 0.19578 0.21619 0.28174 0.04933  0.01414  0.02652  205  LYS A CA    
1570 C C     . LYS A 205 ? 0.18867 0.20173 0.26654 0.04551  0.01090  0.02801  205  LYS A C     
1571 O O     . LYS A 205 ? 0.19498 0.21186 0.27284 0.04313  0.00704  0.03057  205  LYS A O     
1572 C CB    . LYS A 205 ? 0.18716 0.20704 0.27916 0.05563  0.01328  0.02851  205  LYS A CB    
1573 C CG    . LYS A 205 ? 0.25221 0.27785 0.35185 0.06042  0.01723  0.02658  205  LYS A CG    
1574 C CD    . LYS A 205 ? 0.25016 0.28027 0.35857 0.06621  0.01504  0.02971  205  LYS A CD    
1575 C CE    . LYS A 205 ? 0.29510 0.33187 0.41179 0.07137  0.01928  0.02776  205  LYS A CE    
1576 N NZ    . LYS A 205 ? 0.29431 0.34293 0.41529 0.06857  0.02154  0.02666  205  LYS A NZ    
1577 N N     . LEU A 206 ? 0.21309 0.21560 0.28403 0.04486  0.01258  0.02623  206  LEU A N     
1578 C CA    . LEU A 206 ? 0.21323 0.20831 0.27647 0.04149  0.01027  0.02758  206  LEU A CA    
1579 C C     . LEU A 206 ? 0.25067 0.23483 0.31104 0.04420  0.01075  0.02812  206  LEU A C     
1580 O O     . LEU A 206 ? 0.25514 0.23436 0.31547 0.04618  0.01414  0.02521  206  LEU A O     
1581 C CB    . LEU A 206 ? 0.21651 0.21001 0.27345 0.03623  0.01190  0.02480  206  LEU A CB    
1582 C CG    . LEU A 206 ? 0.20668 0.19242 0.25577 0.03284  0.01035  0.02575  206  LEU A CG    
1583 C CD1   . LEU A 206 ? 0.19883 0.18809 0.24700 0.03116  0.00612  0.02914  206  LEU A CD1   
1584 C CD2   . LEU A 206 ? 0.25617 0.23956 0.29987 0.02862  0.01267  0.02244  206  LEU A CD2   
1585 N N     . LYS A 207 ? 0.19952 0.17961 0.25717 0.04423  0.00736  0.03183  207  LYS A N     
1586 C CA    . LYS A 207 ? 0.22271 0.19186 0.27725 0.04639  0.00745  0.03324  207  LYS A CA    
1587 C C     . LYS A 207 ? 0.22756 0.19054 0.27394 0.04204  0.00588  0.03498  207  LYS A C     
1588 O O     . LYS A 207 ? 0.20131 0.16903 0.24567 0.03938  0.00309  0.03687  207  LYS A O     
1589 C CB    . LYS A 207 ? 0.22976 0.19971 0.28967 0.05199  0.00493  0.03700  207  LYS A CB    
1590 C CG    . LYS A 207 ? 0.24864 0.22338 0.31698 0.05719  0.00711  0.03525  207  LYS A CG    
1591 C CD    . LYS A 207 ? 0.23097 0.20401 0.30412 0.06332  0.00496  0.03886  207  LYS A CD    
1592 C CE    . LYS A 207 ? 0.29814 0.27617 0.38004 0.06890  0.00758  0.03686  207  LYS A CE    
1593 N NZ    . LYS A 207 ? 0.38688 0.35938 0.47234 0.07543  0.00660  0.03947  207  LYS A NZ    
1594 N N     . ALA A 208 ? 0.24104 0.19343 0.28283 0.04129  0.00777  0.03421  208  ALA A N     
1595 C CA    . ALA A 208 ? 0.22018 0.16649 0.25453 0.03711  0.00698  0.03584  208  ALA A CA    
1596 C C     . ALA A 208 ? 0.22238 0.16314 0.25500 0.03945  0.00429  0.04099  208  ALA A C     
1597 O O     . ALA A 208 ? 0.25532 0.19075 0.29077 0.04387  0.00451  0.04225  208  ALA A O     
1598 C CB    . ALA A 208 ? 0.23773 0.17591 0.26824 0.03435  0.01036  0.03246  208  ALA A CB    
1599 N N     . ILE A 209 ? 0.20505 0.14692 0.23274 0.03666  0.00180  0.04397  209  ILE A N     
1600 C CA    . ILE A 209 ? 0.21333 0.14973 0.23760 0.03816  -0.00074 0.04919  209  ILE A CA    
1601 C C     . ILE A 209 ? 0.25555 0.18113 0.27373 0.03519  0.00150  0.04966  209  ILE A C     
1602 O O     . ILE A 209 ? 0.24362 0.16941 0.25761 0.03028  0.00304  0.04768  209  ILE A O     
1603 C CB    . ILE A 209 ? 0.22295 0.16593 0.24420 0.03665  -0.00450 0.05204  209  ILE A CB    
1604 C CG1   . ILE A 209 ? 0.22730 0.18150 0.25509 0.03860  -0.00672 0.05109  209  ILE A CG1   
1605 C CG2   . ILE A 209 ? 0.26481 0.20241 0.28209 0.03862  -0.00725 0.05770  209  ILE A CG2   
1606 C CD1   . ILE A 209 ? 0.23657 0.19235 0.27102 0.04448  -0.00859 0.05344  209  ILE A CD1   
1607 N N     . PRO A 210 ? 0.25323 0.16930 0.27110 0.03792  0.00176  0.05230  210  PRO A N     
1608 C CA    . PRO A 210 ? 0.28038 0.18581 0.29280 0.03462  0.00388  0.05307  210  PRO A CA    
1609 C C     . PRO A 210 ? 0.27599 0.18190 0.28135 0.03068  0.00260  0.05653  210  PRO A C     
1610 O O     . PRO A 210 ? 0.27451 0.18324 0.27794 0.03240  -0.00059 0.06079  210  PRO A O     
1611 C CB    . PRO A 210 ? 0.29893 0.19460 0.31295 0.03923  0.00357  0.05620  210  PRO A CB    
1612 C CG    . PRO A 210 ? 0.35147 0.25277 0.37308 0.04497  0.00262  0.05487  210  PRO A CG    
1613 C CD    . PRO A 210 ? 0.27536 0.18983 0.29858 0.04425  0.00036  0.05443  210  PRO A CD    
1614 N N     . SER A 211 ? 0.25839 0.16190 0.25987 0.02544  0.00511  0.05457  211  SER A N     
1615 C CA    . SER A 211 ? 0.26831 0.17257 0.26312 0.02152  0.00467  0.05734  211  SER A CA    
1616 C C     . SER A 211 ? 0.29873 0.19240 0.28914 0.02097  0.00520  0.06225  211  SER A C     
1617 O O     . SER A 211 ? 0.29551 0.18014 0.28793 0.02249  0.00646  0.06256  211  SER A O     
1618 C CB    . SER A 211 ? 0.27867 0.18644 0.27200 0.01626  0.00714  0.05312  211  SER A CB    
1619 O OG    . SER A 211 ? 0.30377 0.20525 0.29892 0.01449  0.01014  0.04992  211  SER A OG    
1620 N N     . ASP A 212 ? 0.27746 0.17204 0.26153 0.01876  0.00430  0.06613  212  ASP A N     
1621 C CA    . ASP A 212 ? 0.28820 0.17346 0.26731 0.01800  0.00477  0.07163  212  ASP A CA    
1622 C C     . ASP A 212 ? 0.31259 0.19268 0.28962 0.01234  0.00859  0.07027  212  ASP A C     
1623 O O     . ASP A 212 ? 0.30400 0.18686 0.28402 0.00969  0.01063  0.06489  212  ASP A O     
1624 C CB    . ASP A 212 ? 0.29526 0.18409 0.26808 0.01859  0.00204  0.07670  212  ASP A CB    
1625 C CG    . ASP A 212 ? 0.31241 0.20817 0.28040 0.01408  0.00302  0.07527  212  ASP A CG    
1626 O OD1   . ASP A 212 ? 0.30164 0.20005 0.27154 0.01055  0.00564  0.07055  212  ASP A OD1   
1627 O OD2   . ASP A 212 ? 0.32299 0.22161 0.28499 0.01430  0.00106  0.07888  212  ASP A OD2   
1628 N N     . GLY A 213 ? 0.32414 0.19692 0.29605 0.01034  0.00951  0.07540  213  GLY A N     
1629 C CA    . GLY A 213 ? 0.33147 0.19931 0.30187 0.00470  0.01308  0.07479  213  GLY A CA    
1630 C C     . GLY A 213 ? 0.34381 0.22058 0.31262 0.00015  0.01468  0.07156  213  GLY A C     
1631 O O     . GLY A 213 ? 0.34303 0.21813 0.31301 -0.00441 0.01754  0.06903  213  GLY A O     
1632 N N     . ASN A 214 ? 0.29192 0.17805 0.25822 0.00132  0.01275  0.07155  214  ASN A N     
1633 C CA    . ASN A 214 ? 0.32384 0.21888 0.28911 -0.00208 0.01394  0.06803  214  ASN A CA    
1634 C C     . ASN A 214 ? 0.29705 0.19913 0.26779 -0.00078 0.01311  0.06195  214  ASN A C     
1635 O O     . ASN A 214 ? 0.29448 0.20451 0.26464 -0.00265 0.01341  0.05901  214  ASN A O     
1636 C CB    . ASN A 214 ? 0.33382 0.23433 0.29244 -0.00180 0.01250  0.07131  214  ASN A CB    
1637 C CG    . ASN A 214 ? 0.39118 0.28618 0.34348 -0.00415 0.01422  0.07708  214  ASN A CG    
1638 O OD1   . ASN A 214 ? 0.41108 0.30258 0.36358 -0.00842 0.01758  0.07716  214  ASN A OD1   
1639 N ND2   . ASN A 214 ? 0.38980 0.28420 0.33646 -0.00151 0.01186  0.08210  214  ASN A ND2   
1640 N N     . PHE A 215 ? 0.28407 0.18328 0.25999 0.00252  0.01219  0.06016  215  PHE A N     
1641 C CA    . PHE A 215 ? 0.27935 0.18483 0.26057 0.00397  0.01167  0.05476  215  PHE A CA    
1642 C C     . PHE A 215 ? 0.27789 0.19284 0.25846 0.00591  0.00892  0.05453  215  PHE A C     
1643 O O     . PHE A 215 ? 0.25472 0.17684 0.23725 0.00486  0.00903  0.05047  215  PHE A O     
1644 C CB    . PHE A 215 ? 0.29510 0.20231 0.27809 -0.00025 0.01441  0.04988  215  PHE A CB    
1645 C CG    . PHE A 215 ? 0.30095 0.19896 0.28541 -0.00224 0.01672  0.04920  215  PHE A CG    
1646 C CD1   . PHE A 215 ? 0.33170 0.22562 0.32066 0.00011  0.01697  0.04615  215  PHE A CD1   
1647 C CD2   . PHE A 215 ? 0.33718 0.23048 0.31851 -0.00649 0.01870  0.05161  215  PHE A CD2   
1648 C CE1   . PHE A 215 ? 0.35639 0.24105 0.34639 -0.00176 0.01888  0.04514  215  PHE A CE1   
1649 C CE2   . PHE A 215 ? 0.33716 0.22151 0.32008 -0.00874 0.02060  0.05095  215  PHE A CE2   
1650 C CZ    . PHE A 215 ? 0.33109 0.21075 0.31818 -0.00637 0.02055  0.04754  215  PHE A CZ    
1651 N N     . ALA A 216 ? 0.27528 0.18994 0.25305 0.00874  0.00622  0.05900  216  ALA A N     
1652 C CA    . ALA A 216 ? 0.26396 0.18674 0.24081 0.01061  0.00301  0.05921  216  ALA A CA    
1653 C C     . ALA A 216 ? 0.25689 0.18007 0.23799 0.01571  -0.00001 0.06070  216  ALA A C     
1654 O O     . ALA A 216 ? 0.26733 0.18346 0.24909 0.01822  -0.00024 0.06388  216  ALA A O     
1655 C CB    . ALA A 216 ? 0.29291 0.21633 0.26190 0.00935  0.00200  0.06313  216  ALA A CB    
1656 N N     . MET A 217 ? 0.22242 0.15393 0.20675 0.01723  -0.00234 0.05849  217  MET A N     
1657 C CA    . MET A 217 ? 0.21812 0.15208 0.20682 0.02194  -0.00563 0.06016  217  MET A CA    
1658 C C     . MET A 217 ? 0.24873 0.18240 0.23201 0.02352  -0.00913 0.06534  217  MET A C     
1659 O O     . MET A 217 ? 0.24907 0.18615 0.22650 0.02126  -0.01023 0.06581  217  MET A O     
1660 C CB    . MET A 217 ? 0.24436 0.18780 0.23844 0.02246  -0.00700 0.05640  217  MET A CB    
1661 C CG    . MET A 217 ? 0.25542 0.20235 0.25578 0.02724  -0.00997 0.05774  217  MET A CG    
1662 S SD    . MET A 217 ? 0.25111 0.20962 0.25817 0.02731  -0.01153 0.05388  217  MET A SD    
1663 C CE    . MET A 217 ? 0.25198 0.21000 0.26016 0.02370  -0.00672 0.04847  217  MET A CE    
1664 N N     . ARG A 218 ? 0.24455 0.17409 0.22954 0.02761  -0.01094 0.06918  218  ARG A N     
1665 C CA    . ARG A 218 ? 0.26996 0.19847 0.24958 0.02956  -0.01448 0.07467  218  ARG A CA    
1666 C C     . ARG A 218 ? 0.27338 0.20670 0.25889 0.03459  -0.01869 0.07610  218  ARG A C     
1667 O O     . ARG A 218 ? 0.28123 0.21662 0.27513 0.03703  -0.01813 0.07358  218  ARG A O     
1668 C CB    . ARG A 218 ? 0.28693 0.20460 0.26178 0.02965  -0.01283 0.07939  218  ARG A CB    
1669 C CG    . ARG A 218 ? 0.28188 0.19488 0.25226 0.02451  -0.00837 0.07811  218  ARG A CG    
1670 C CD    . ARG A 218 ? 0.30888 0.22663 0.27163 0.02108  -0.00866 0.07833  218  ARG A CD    
1671 N NE    . ARG A 218 ? 0.32942 0.24655 0.28535 0.02290  -0.01192 0.08387  218  ARG A NE    
1672 C CZ    . ARG A 218 ? 0.38948 0.29930 0.33885 0.02218  -0.01083 0.08906  218  ARG A CZ    
1673 N NH1   . ARG A 218 ? 0.37457 0.27688 0.32377 0.01943  -0.00660 0.08950  218  ARG A NH1   
1674 N NH2   . ARG A 218 ? 0.39171 0.30177 0.33445 0.02411  -0.01416 0.09405  218  ARG A NH2   
1675 N N     . ALA A 219 ? 0.27537 0.21088 0.25631 0.03617  -0.02295 0.08021  219  ALA A N     
1676 C CA    . ALA A 219 ? 0.32291 0.26434 0.30940 0.04071  -0.02765 0.08180  219  ALA A CA    
1677 C C     . ALA A 219 ? 0.28559 0.22166 0.27830 0.04565  -0.02736 0.08417  219  ALA A C     
1678 O O     . ALA A 219 ? 0.30730 0.24889 0.30892 0.04918  -0.02889 0.08288  219  ALA A O     
1679 C CB    . ALA A 219 ? 0.29895 0.24276 0.27808 0.04132  -0.03246 0.08605  219  ALA A CB    
1680 N N     . SER A 220 ? 0.30069 0.22594 0.28910 0.04597  -0.02524 0.08763  220  SER A N     
1681 C CA    . SER A 220 ? 0.33050 0.24925 0.32401 0.05105  -0.02526 0.09033  220  SER A CA    
1682 C C     . SER A 220 ? 0.34163 0.26092 0.34445 0.05230  -0.02203 0.08516  220  SER A C     
1683 O O     . SER A 220 ? 0.30763 0.22886 0.31826 0.05748  -0.02339 0.08545  220  SER A O     
1684 C CB    . SER A 220 ? 0.37597 0.28199 0.36260 0.05026  -0.02321 0.09480  220  SER A CB    
1685 O OG    . SER A 220 ? 0.44405 0.34638 0.42609 0.04445  -0.01880 0.09208  220  SER A OG    
1686 N N     . ALA A 221 ? 0.30313 0.22104 0.30520 0.04778  -0.01772 0.08041  221  ALA A N     
1687 C CA    . ALA A 221 ? 0.29913 0.21760 0.30893 0.04873  -0.01455 0.07526  221  ALA A CA    
1688 C C     . ALA A 221 ? 0.26636 0.19726 0.28346 0.05025  -0.01634 0.07214  221  ALA A C     
1689 O O     . ALA A 221 ? 0.27658 0.20953 0.30176 0.05393  -0.01540 0.07003  221  ALA A O     
1690 C CB    . ALA A 221 ? 0.29671 0.21125 0.30338 0.04329  -0.00999 0.07111  221  ALA A CB    
1691 N N     . LEU A 222 ? 0.23736 0.17656 0.25178 0.04742  -0.01878 0.07176  222  LEU A N     
1692 C CA    . LEU A 222 ? 0.23563 0.18657 0.25700 0.04826  -0.02072 0.06914  222  LEU A CA    
1693 C C     . LEU A 222 ? 0.26387 0.21915 0.29166 0.05404  -0.02470 0.07244  222  LEU A C     
1694 O O     . LEU A 222 ? 0.22902 0.19087 0.26598 0.05677  -0.02447 0.07028  222  LEU A O     
1695 C CB    . LEU A 222 ? 0.22226 0.17974 0.23870 0.04386  -0.02278 0.06817  222  LEU A CB    
1696 C CG    . LEU A 222 ? 0.25387 0.22330 0.27660 0.04403  -0.02566 0.06618  222  LEU A CG    
1697 C CD1   . LEU A 222 ? 0.26617 0.23961 0.29742 0.04449  -0.02235 0.06180  222  LEU A CD1   
1698 C CD2   . LEU A 222 ? 0.23955 0.21309 0.25618 0.03933  -0.02725 0.06480  222  LEU A CD2   
1699 N N     . GLN A 223 ? 0.27075 0.22284 0.29392 0.05606  -0.02833 0.07784  223  GLN A N     
1700 C CA    . GLN A 223 ? 0.27601 0.23241 0.30522 0.06182  -0.03261 0.08141  223  GLN A CA    
1701 C C     . GLN A 223 ? 0.27483 0.22644 0.31147 0.06707  -0.03018 0.08137  223  GLN A C     
1702 O O     . GLN A 223 ? 0.25202 0.21056 0.29792 0.07173  -0.03200 0.08158  223  GLN A O     
1703 C CB    . GLN A 223 ? 0.29901 0.25184 0.32042 0.06288  -0.03691 0.08751  223  GLN A CB    
1704 C CG    . GLN A 223 ? 0.32256 0.28216 0.33770 0.05906  -0.04054 0.08765  223  GLN A CG    
1705 C CD    . GLN A 223 ? 0.45351 0.40690 0.45748 0.05856  -0.04290 0.09293  223  GLN A CD    
1706 O OE1   . GLN A 223 ? 0.45840 0.40110 0.45696 0.05834  -0.04003 0.09539  223  GLN A OE1   
1707 N NE2   . GLN A 223 ? 0.48405 0.44413 0.48429 0.05820  -0.04815 0.09472  223  GLN A NE2   
1708 N N     . GLU A 224 ? 0.25731 0.19717 0.29026 0.06638  -0.02603 0.08094  224  GLU A N     
1709 C CA    . GLU A 224 ? 0.28777 0.22171 0.32708 0.07127  -0.02343 0.08026  224  GLU A CA    
1710 C C     . GLU A 224 ? 0.27549 0.21678 0.32347 0.07180  -0.02044 0.07438  224  GLU A C     
1711 O O     . GLU A 224 ? 0.26880 0.21257 0.32536 0.07738  -0.02024 0.07402  224  GLU A O     
1712 C CB    . GLU A 224 ? 0.34659 0.26590 0.37946 0.06945  -0.01975 0.08068  224  GLU A CB    
1713 C CG    . GLU A 224 ? 0.44660 0.35948 0.48483 0.07203  -0.01542 0.07695  224  GLU A CG    
1714 C CD    . GLU A 224 ? 0.53421 0.43200 0.56615 0.07001  -0.01244 0.07777  224  GLU A CD    
1715 O OE1   . GLU A 224 ? 0.57538 0.47064 0.60077 0.06375  -0.01042 0.07621  224  GLU A OE1   
1716 O OE2   . GLU A 224 ? 0.61583 0.50430 0.64971 0.07467  -0.01213 0.08000  224  GLU A OE2   
1717 N N     . ALA A 225 ? 0.26018 0.20533 0.30604 0.06625  -0.01804 0.06989  225  ALA A N     
1718 C CA    . ALA A 225 ? 0.23760 0.19004 0.29084 0.06637  -0.01514 0.06460  225  ALA A CA    
1719 C C     . ALA A 225 ? 0.23131 0.19737 0.29283 0.06886  -0.01847 0.06518  225  ALA A C     
1720 O O     . ALA A 225 ? 0.22618 0.19760 0.29664 0.07257  -0.01688 0.06312  225  ALA A O     
1721 C CB    . ALA A 225 ? 0.25180 0.20493 0.30028 0.05981  -0.01218 0.06023  225  ALA A CB    
1722 N N     . LEU A 226 ? 0.22609 0.19807 0.28483 0.06678  -0.02306 0.06787  226  LEU A N     
1723 C CA    . LEU A 226 ? 0.24950 0.23458 0.31620 0.06855  -0.02682 0.06856  226  LEU A CA    
1724 C C     . LEU A 226 ? 0.22844 0.21524 0.30318 0.07586  -0.02889 0.07178  226  LEU A C     
1725 O O     . LEU A 226 ? 0.22491 0.22161 0.31001 0.07875  -0.02897 0.07054  226  LEU A O     
1726 C CB    . LEU A 226 ? 0.22070 0.21003 0.28161 0.06503  -0.03180 0.07088  226  LEU A CB    
1727 C CG    . LEU A 226 ? 0.28136 0.27218 0.33626 0.05820  -0.03050 0.06745  226  LEU A CG    
1728 C CD1   . LEU A 226 ? 0.29383 0.28546 0.34083 0.05553  -0.03521 0.07014  226  LEU A CD1   
1729 C CD2   . LEU A 226 ? 0.26629 0.26781 0.32917 0.05658  -0.02946 0.06356  226  LEU A CD2   
1730 N N     . GLU A 227 ? 0.23935 0.21676 0.30964 0.07899  -0.03050 0.07616  227  GLU A N     
1731 C CA    . GLU A 227 ? 0.24732 0.22513 0.32491 0.08647  -0.03253 0.07957  227  GLU A CA    
1732 C C     . GLU A 227 ? 0.24843 0.22602 0.33465 0.09051  -0.02771 0.07591  227  GLU A C     
1733 O O     . GLU A 227 ? 0.25655 0.24261 0.35329 0.09573  -0.02878 0.07634  227  GLU A O     
1734 C CB    . GLU A 227 ? 0.27890 0.24413 0.34890 0.08865  -0.03416 0.08473  227  GLU A CB    
1735 C CG    . GLU A 227 ? 0.29011 0.25322 0.36689 0.09683  -0.03590 0.08849  227  GLU A CG    
1736 C CD    . GLU A 227 ? 0.39143 0.34161 0.45995 0.09859  -0.03772 0.09419  227  GLU A CD    
1737 O OE1   . GLU A 227 ? 0.46110 0.40687 0.51900 0.09352  -0.03877 0.09601  227  GLU A OE1   
1738 O OE2   . GLU A 227 ? 0.37483 0.31918 0.44747 0.10512  -0.03794 0.09696  227  GLU A OE2   
1739 N N     . ARG A 228 ? 0.24656 0.21493 0.32849 0.08813  -0.02236 0.07211  228  ARG A N     
1740 C CA    . ARG A 228 ? 0.24694 0.21404 0.33553 0.09171  -0.01746 0.06802  228  ARG A CA    
1741 C C     . ARG A 228 ? 0.23596 0.21716 0.33284 0.09088  -0.01593 0.06410  228  ARG A C     
1742 O O     . ARG A 228 ? 0.23659 0.22412 0.34340 0.09630  -0.01485 0.06328  228  ARG A O     
1743 C CB    . ARG A 228 ? 0.28093 0.23515 0.36196 0.08836  -0.01260 0.06461  228  ARG A CB    
1744 C CG    . ARG A 228 ? 0.28906 0.24160 0.37522 0.09109  -0.00727 0.05938  228  ARG A CG    
1745 C CD    . ARG A 228 ? 0.30298 0.24667 0.38140 0.08559  -0.00304 0.05503  228  ARG A CD    
1746 N NE    . ARG A 228 ? 0.26808 0.21911 0.34294 0.07875  -0.00307 0.05301  228  ARG A NE    
1747 C CZ    . ARG A 228 ? 0.30696 0.25190 0.37288 0.07267  -0.00246 0.05242  228  ARG A CZ    
1748 N NH1   . ARG A 228 ? 0.28677 0.21846 0.34635 0.07193  -0.00166 0.05372  228  ARG A NH1   
1749 N NH2   . ARG A 228 ? 0.27855 0.23092 0.34218 0.06721  -0.00263 0.05058  228  ARG A NH2   
1750 N N     . ASP A 229 ? 0.23628 0.22255 0.32936 0.08421  -0.01568 0.06178  229  ASP A N     
1751 C CA    . ASP A 229 ? 0.21643 0.21410 0.31617 0.08262  -0.01325 0.05776  229  ASP A CA    
1752 C C     . ASP A 229 ? 0.23478 0.24696 0.34418 0.08476  -0.01726 0.06007  229  ASP A C     
1753 O O     . ASP A 229 ? 0.20846 0.23026 0.32726 0.08684  -0.01507 0.05792  229  ASP A O     
1754 C CB    . ASP A 229 ? 0.23510 0.23261 0.32755 0.07495  -0.01179 0.05478  229  ASP A CB    
1755 C CG    . ASP A 229 ? 0.23708 0.22209 0.32163 0.07268  -0.00742 0.05180  229  ASP A CG    
1756 O OD1   . ASP A 229 ? 0.24615 0.22509 0.33289 0.07670  -0.00406 0.05007  229  ASP A OD1   
1757 O OD2   . ASP A 229 ? 0.22981 0.21113 0.30614 0.06693  -0.00741 0.05107  229  ASP A OD2   
1758 N N     . LYS A 230 ? 0.21461 0.22893 0.32188 0.08419  -0.02314 0.06442  230  LYS A N     
1759 C CA    . LYS A 230 ? 0.22297 0.25112 0.33971 0.08620  -0.02761 0.06673  230  LYS A CA    
1760 C C     . LYS A 230 ? 0.22640 0.25754 0.35344 0.09441  -0.02760 0.06855  230  LYS A C     
1761 O O     . LYS A 230 ? 0.22656 0.27072 0.36497 0.09669  -0.02813 0.06830  230  LYS A O     
1762 C CB    . LYS A 230 ? 0.21405 0.24296 0.32503 0.08383  -0.03419 0.07077  230  LYS A CB    
1763 C CG    . LYS A 230 ? 0.23417 0.26338 0.33710 0.07600  -0.03461 0.06866  230  LYS A CG    
1764 C CD    . LYS A 230 ? 0.26619 0.29037 0.35904 0.07384  -0.03952 0.07215  230  LYS A CD    
1765 C CE    . LYS A 230 ? 0.25279 0.28695 0.35057 0.07564  -0.04642 0.07571  230  LYS A CE    
1766 N NZ    . LYS A 230 ? 0.24532 0.27466 0.33205 0.07331  -0.05110 0.07880  230  LYS A NZ    
1767 N N     . ALA A 231 ? 0.22850 0.24769 0.35208 0.09897  -0.02685 0.07043  231  ALA A N     
1768 C CA    . ALA A 231 ? 0.23546 0.25603 0.36859 0.10734  -0.02631 0.07182  231  ALA A CA    
1769 C C     . ALA A 231 ? 0.23527 0.25907 0.37546 0.10944  -0.01986 0.06672  231  ALA A C     
1770 O O     . ALA A 231 ? 0.23763 0.26922 0.38906 0.11568  -0.01926 0.06699  231  ALA A O     
1771 C CB    . ALA A 231 ? 0.24812 0.25343 0.37503 0.11140  -0.02684 0.07499  231  ALA A CB    
1772 N N     . ALA A 232 ? 0.22752 0.24593 0.36129 0.10449  -0.01501 0.06208  232  ALA A N     
1773 C CA    . ALA A 232 ? 0.24515 0.26645 0.38406 0.10597  -0.00878 0.05700  232  ALA A CA    
1774 C C     . ALA A 232 ? 0.24878 0.28656 0.39580 0.10340  -0.00820 0.05533  232  ALA A C     
1775 O O     . ALA A 232 ? 0.29277 0.33509 0.44494 0.10488  -0.00304 0.05152  232  ALA A O     
1776 C CB    . ALA A 232 ? 0.26472 0.27383 0.39331 0.10165  -0.00412 0.05274  232  ALA A CB    
1777 N N     . GLY A 233 ? 0.20898 0.25557 0.35707 0.09951  -0.01326 0.05804  233  GLY A N     
1778 C CA    . GLY A 233 ? 0.21831 0.27995 0.37402 0.09636  -0.01306 0.05678  233  GLY A CA    
1779 C C     . GLY A 233 ? 0.23386 0.29498 0.38219 0.08814  -0.01158 0.05395  233  GLY A C     
1780 O O     . GLY A 233 ? 0.20060 0.27323 0.35480 0.08508  -0.01083 0.05273  233  GLY A O     
1781 N N     . LEU A 234 ? 0.20227 0.25059 0.33831 0.08451  -0.01106 0.05301  234  LEU A N     
1782 C CA    . LEU A 234 ? 0.19199 0.23943 0.32076 0.07699  -0.01001 0.05056  234  LEU A CA    
1783 C C     . LEU A 234 ? 0.19829 0.25027 0.32478 0.07257  -0.01602 0.05331  234  LEU A C     
1784 O O     . LEU A 234 ? 0.20588 0.25669 0.33165 0.07463  -0.02100 0.05711  234  LEU A O     
1785 C CB    . LEU A 234 ? 0.21417 0.24683 0.33133 0.07490  -0.00709 0.04841  234  LEU A CB    
1786 C CG    . LEU A 234 ? 0.22383 0.25069 0.34132 0.07802  -0.00098 0.04462  234  LEU A CG    
1787 C CD1   . LEU A 234 ? 0.24017 0.25282 0.34621 0.07502  0.00105  0.04269  234  LEU A CD1   
1788 C CD2   . LEU A 234 ? 0.25019 0.28679 0.37310 0.07662  0.00314  0.04113  234  LEU A CD2   
1789 N N     . ILE A 235 ? 0.17319 0.23009 0.29819 0.06655  -0.01560 0.05134  235  ILE A N     
1790 C CA    . ILE A 235 ? 0.18479 0.24582 0.30732 0.06186  -0.02097 0.05308  235  ILE A CA    
1791 C C     . ILE A 235 ? 0.18215 0.23418 0.29252 0.05617  -0.02011 0.05120  235  ILE A C     
1792 O O     . ILE A 235 ? 0.16165 0.21496 0.27071 0.05219  -0.01686 0.04814  235  ILE A O     
1793 C CB    . ILE A 235 ? 0.19516 0.27044 0.32751 0.05958  -0.02194 0.05273  235  ILE A CB    
1794 C CG1   . ILE A 235 ? 0.20218 0.28721 0.34763 0.06554  -0.02185 0.05431  235  ILE A CG1   
1795 C CG2   . ILE A 235 ? 0.19829 0.27725 0.32825 0.05505  -0.02812 0.05440  235  ILE A CG2   
1796 C CD1   . ILE A 235 ? 0.25068 0.35018 0.40701 0.06345  -0.02153 0.05384  235  ILE A CD1   
1797 N N     . PRO A 236 ? 0.17785 0.22093 0.27921 0.05576  -0.02279 0.05310  236  PRO A N     
1798 C CA    . PRO A 236 ? 0.18766 0.22341 0.27800 0.05037  -0.02219 0.05150  236  PRO A CA    
1799 C C     . PRO A 236 ? 0.18105 0.22390 0.27130 0.04517  -0.02502 0.05075  236  PRO A C     
1800 O O     . PRO A 236 ? 0.22346 0.27297 0.31716 0.04517  -0.03009 0.05294  236  PRO A O     
1801 C CB    . PRO A 236 ? 0.19194 0.21876 0.27435 0.05177  -0.02510 0.05466  236  PRO A CB    
1802 C CG    . PRO A 236 ? 0.20997 0.23572 0.29829 0.05839  -0.02502 0.05697  236  PRO A CG    
1803 C CD    . PRO A 236 ? 0.18506 0.22371 0.28568 0.06056  -0.02591 0.05690  236  PRO A CD    
1804 N N     . PHE A 237 ? 0.15966 0.20081 0.24590 0.04072  -0.02190 0.04759  237  PHE A N     
1805 C CA    . PHE A 237 ? 0.17559 0.22247 0.26177 0.03575  -0.02414 0.04658  237  PHE A CA    
1806 C C     . PHE A 237 ? 0.15130 0.19124 0.22726 0.03110  -0.02301 0.04451  237  PHE A C     
1807 O O     . PHE A 237 ? 0.15820 0.20106 0.23248 0.02719  -0.02563 0.04391  237  PHE A O     
1808 C CB    . PHE A 237 ? 0.15537 0.21157 0.25095 0.03496  -0.02160 0.04497  237  PHE A CB    
1809 C CG    . PHE A 237 ? 0.16344 0.21620 0.25604 0.03291  -0.01598 0.04174  237  PHE A CG    
1810 C CD1   . PHE A 237 ? 0.18754 0.23531 0.27955 0.03612  -0.01135 0.04046  237  PHE A CD1   
1811 C CD2   . PHE A 237 ? 0.15223 0.20658 0.24253 0.02784  -0.01555 0.03996  237  PHE A CD2   
1812 C CE1   . PHE A 237 ? 0.15428 0.19920 0.24314 0.03417  -0.00657 0.03737  237  PHE A CE1   
1813 C CE2   . PHE A 237 ? 0.15776 0.20925 0.24511 0.02611  -0.01072 0.03726  237  PHE A CE2   
1814 C CZ    . PHE A 237 ? 0.16945 0.21652 0.25599 0.02922  -0.00632 0.03593  237  PHE A CZ    
1815 N N     . PHE A 238 ? 0.15292 0.18392 0.22235 0.03134  -0.01934 0.04330  238  PHE A N     
1816 C CA    . PHE A 238 ? 0.15031 0.17594 0.21138 0.02707  -0.01772 0.04110  238  PHE A CA    
1817 C C     . PHE A 238 ? 0.15520 0.17058 0.20855 0.02798  -0.01585 0.04143  238  PHE A C     
1818 O O     . PHE A 238 ? 0.16378 0.17555 0.21903 0.03134  -0.01347 0.04175  238  PHE A O     
1819 C CB    . PHE A 238 ? 0.15085 0.17924 0.21459 0.02493  -0.01361 0.03801  238  PHE A CB    
1820 C CG    . PHE A 238 ? 0.15276 0.17660 0.20882 0.02075  -0.01216 0.03580  238  PHE A CG    
1821 C CD1   . PHE A 238 ? 0.14090 0.16596 0.19349 0.01732  -0.01528 0.03573  238  PHE A CD1   
1822 C CD2   . PHE A 238 ? 0.14555 0.16407 0.19811 0.02035  -0.00779 0.03360  238  PHE A CD2   
1823 C CE1   . PHE A 238 ? 0.15017 0.17129 0.19620 0.01396  -0.01387 0.03370  238  PHE A CE1   
1824 C CE2   . PHE A 238 ? 0.14731 0.16246 0.19352 0.01672  -0.00663 0.03169  238  PHE A CE2   
1825 C CZ    . PHE A 238 ? 0.15429 0.17080 0.19739 0.01371  -0.00956 0.03182  238  PHE A CZ    
1826 N N     . MET A 239 ? 0.15590 0.16661 0.20074 0.02494  -0.01687 0.04132  239  MET A N     
1827 C CA    . MET A 239 ? 0.16058 0.16202 0.19791 0.02496  -0.01511 0.04186  239  MET A CA    
1828 C C     . MET A 239 ? 0.15713 0.15581 0.18781 0.02064  -0.01339 0.03946  239  MET A C     
1829 O O     . MET A 239 ? 0.17493 0.17676 0.20339 0.01805  -0.01569 0.03893  239  MET A O     
1830 C CB    . MET A 239 ? 0.17897 0.17742 0.21210 0.02667  -0.01882 0.04562  239  MET A CB    
1831 C CG    . MET A 239 ? 0.20761 0.19770 0.23118 0.02488  -0.01764 0.04632  239  MET A CG    
1832 S SD    . MET A 239 ? 0.30237 0.28317 0.32519 0.02711  -0.01363 0.04700  239  MET A SD    
1833 C CE    . MET A 239 ? 0.18569 0.16623 0.21203 0.03247  -0.01710 0.05160  239  MET A CE    
1834 N N     . VAL A 240 ? 0.16918 0.16200 0.19695 0.01993  -0.00950 0.03790  240  VAL A N     
1835 C CA    . VAL A 240 ? 0.15571 0.14537 0.17703 0.01623  -0.00782 0.03604  240  VAL A CA    
1836 C C     . VAL A 240 ? 0.17049 0.15270 0.18520 0.01621  -0.00755 0.03811  240  VAL A C     
1837 O O     . VAL A 240 ? 0.17679 0.15339 0.19152 0.01749  -0.00521 0.03846  240  VAL A O     
1838 C CB    . VAL A 240 ? 0.15715 0.14651 0.18005 0.01486  -0.00381 0.03267  240  VAL A CB    
1839 C CG1   . VAL A 240 ? 0.18148 0.16740 0.19795 0.01140  -0.00224 0.03112  240  VAL A CG1   
1840 C CG2   . VAL A 240 ? 0.16849 0.16533 0.19709 0.01443  -0.00392 0.03104  240  VAL A CG2   
1841 N N     . ALA A 241 ? 0.16384 0.14578 0.17277 0.01475  -0.00990 0.03951  241  ALA A N     
1842 C CA    . ALA A 241 ? 0.16976 0.14529 0.17153 0.01394  -0.00916 0.04144  241  ALA A CA    
1843 C C     . ALA A 241 ? 0.18187 0.15627 0.17948 0.01031  -0.00649 0.03885  241  ALA A C     
1844 O O     . ALA A 241 ? 0.17214 0.15090 0.16955 0.00848  -0.00712 0.03663  241  ALA A O     
1845 C CB    . ALA A 241 ? 0.17494 0.15102 0.17203 0.01467  -0.01305 0.04454  241  ALA A CB    
1846 N N     . THR A 242 ? 0.16962 0.13815 0.16431 0.00928  -0.00357 0.03918  242  THR A N     
1847 C CA    . THR A 242 ? 0.16639 0.13423 0.15850 0.00600  -0.00073 0.03665  242  THR A CA    
1848 C C     . THR A 242 ? 0.18085 0.14571 0.16580 0.00427  -0.00033 0.03859  242  THR A C     
1849 O O     . THR A 242 ? 0.17984 0.13966 0.16211 0.00505  -0.00015 0.04181  242  THR A O     
1850 C CB    . THR A 242 ? 0.16617 0.13040 0.16123 0.00555  0.00258  0.03486  242  THR A CB    
1851 O OG1   . THR A 242 ? 0.18029 0.14746 0.18156 0.00751  0.00252  0.03312  242  THR A OG1   
1852 C CG2   . THR A 242 ? 0.16931 0.13414 0.16249 0.00214  0.00505  0.03207  242  THR A CG2   
1853 N N     . LEU A 243 ? 0.18663 0.15459 0.16853 0.00206  -0.00003 0.03675  243  LEU A N     
1854 C CA    . LEU A 243 ? 0.17196 0.13816 0.14732 0.00018  0.00118  0.03789  243  LEU A CA    
1855 C C     . LEU A 243 ? 0.19476 0.16107 0.17104 -0.00254 0.00461  0.03521  243  LEU A C     
1856 O O     . LEU A 243 ? 0.20952 0.17998 0.18713 -0.00352 0.00476  0.03218  243  LEU A O     
1857 C CB    . LEU A 243 ? 0.18963 0.15950 0.16058 0.00024  -0.00132 0.03770  243  LEU A CB    
1858 C CG    . LEU A 243 ? 0.21686 0.18734 0.18642 0.00265  -0.00533 0.04022  243  LEU A CG    
1859 C CD1   . LEU A 243 ? 0.22617 0.19980 0.19060 0.00223  -0.00769 0.03927  243  LEU A CD1   
1860 C CD2   . LEU A 243 ? 0.21803 0.18342 0.18431 0.00387  -0.00526 0.04459  243  LEU A CD2   
1861 N N     . GLY A 244 ? 0.19098 0.15264 0.16677 -0.00380 0.00717  0.03642  244  GLY A N     
1862 C CA    . GLY A 244 ? 0.19300 0.15483 0.17039 -0.00653 0.01016  0.03395  244  GLY A CA    
1863 C C     . GLY A 244 ? 0.19653 0.15733 0.17952 -0.00624 0.01094  0.03156  244  GLY A C     
1864 O O     . GLY A 244 ? 0.19359 0.15838 0.17931 -0.00680 0.01117  0.02833  244  GLY A O     
1865 N N     . THR A 245 ? 0.19802 0.15320 0.18243 -0.00522 0.01138  0.03315  245  THR A N     
1866 C CA    . THR A 245 ? 0.17246 0.12614 0.16171 -0.00439 0.01213  0.03073  245  THR A CA    
1867 C C     . THR A 245 ? 0.20510 0.15942 0.19555 -0.00745 0.01446  0.02738  245  THR A C     
1868 O O     . THR A 245 ? 0.20966 0.16328 0.19786 -0.01034 0.01597  0.02774  245  THR A O     
1869 C CB    . THR A 245 ? 0.19808 0.14449 0.18810 -0.00266 0.01236  0.03307  245  THR A CB    
1870 O OG1   . THR A 245 ? 0.21985 0.16083 0.20698 -0.00529 0.01422  0.03486  245  THR A OG1   
1871 C CG2   . THR A 245 ? 0.18053 0.12694 0.16974 0.00069  0.00965  0.03655  245  THR A CG2   
1872 N N     . THR A 246 ? 0.22721 0.18342 0.22129 -0.00678 0.01472  0.02415  246  THR A N     
1873 C CA    . THR A 246 ? 0.23005 0.18733 0.22518 -0.00945 0.01646  0.02075  246  THR A CA    
1874 C C     . THR A 246 ? 0.22816 0.17885 0.22304 -0.01156 0.01826  0.02076  246  THR A C     
1875 O O     . THR A 246 ? 0.24464 0.19616 0.23946 -0.01478 0.01954  0.01894  246  THR A O     
1876 C CB    . THR A 246 ? 0.26145 0.22157 0.25981 -0.00800 0.01639  0.01758  246  THR A CB    
1877 O OG1   . THR A 246 ? 0.31427 0.27026 0.31474 -0.00520 0.01641  0.01796  246  THR A OG1   
1878 C CG2   . THR A 246 ? 0.25536 0.22218 0.25425 -0.00684 0.01478  0.01747  246  THR A CG2   
1879 N N     . THR A 247 ? 0.23147 0.17555 0.22649 -0.00985 0.01824  0.02285  247  THR A N     
1880 C CA    . THR A 247 ? 0.25989 0.19648 0.25484 -0.01190 0.01986  0.02290  247  THR A CA    
1881 C C     . THR A 247 ? 0.24041 0.17570 0.23245 -0.01520 0.02079  0.02573  247  THR A C     
1882 O O     . THR A 247 ? 0.24457 0.17962 0.23699 -0.01898 0.02229  0.02419  247  THR A O     
1883 C CB    . THR A 247 ? 0.26590 0.19523 0.26184 -0.00868 0.01951  0.02461  247  THR A CB    
1884 O OG1   . THR A 247 ? 0.25112 0.18160 0.24571 -0.00580 0.01771  0.02855  247  THR A OG1   
1885 C CG2   . THR A 247 ? 0.27601 0.20580 0.27527 -0.00606 0.01960  0.02094  247  THR A CG2   
1886 N N     . CYS A 248 ? 0.21132 0.14626 0.20043 -0.01389 0.01992  0.02992  248  CYS A N     
1887 C CA    . CYS A 248 ? 0.21797 0.15069 0.20387 -0.01673 0.02120  0.03323  248  CYS A CA    
1888 C C     . CYS A 248 ? 0.23953 0.17757 0.22153 -0.01616 0.02039  0.03570  248  CYS A C     
1889 O O     . CYS A 248 ? 0.23446 0.17056 0.21296 -0.01778 0.02145  0.03919  248  CYS A O     
1890 C CB    . CYS A 248 ? 0.26149 0.18469 0.24642 -0.01615 0.02154  0.03682  248  CYS A CB    
1891 S SG    . CYS A 248 ? 0.27880 0.19957 0.26309 -0.01046 0.01887  0.03992  248  CYS A SG    
1892 N N     . CYS A 249 ? 0.21665 0.16107 0.19894 -0.01405 0.01863  0.03398  249  CYS A N     
1893 C CA    . CYS A 249 ? 0.20199 0.15104 0.18033 -0.01325 0.01751  0.03568  249  CYS A CA    
1894 C C     . CYS A 249 ? 0.21909 0.16385 0.19336 -0.01152 0.01646  0.04048  249  CYS A C     
1895 O O     . CYS A 249 ? 0.23897 0.18413 0.20847 -0.01262 0.01716  0.04316  249  CYS A O     
1896 C CB    . CYS A 249 ? 0.21621 0.16953 0.19283 -0.01640 0.01949  0.03488  249  CYS A CB    
1897 S SG    . CYS A 249 ? 0.21984 0.18006 0.19237 -0.01505 0.01811  0.03475  249  CYS A SG    
1898 N N     . SER A 250 ? 0.20735 0.14813 0.18348 -0.00860 0.01483  0.04165  250  SER A N     
1899 C CA    . SER A 250 ? 0.21977 0.15729 0.19249 -0.00611 0.01298  0.04618  250  SER A CA    
1900 C C     . SER A 250 ? 0.20770 0.15093 0.17994 -0.00323 0.00971  0.04582  250  SER A C     
1901 O O     . SER A 250 ? 0.18680 0.13550 0.16207 -0.00303 0.00904  0.04221  250  SER A O     
1902 C CB    . SER A 250 ? 0.25409 0.18400 0.22944 -0.00419 0.01285  0.04792  250  SER A CB    
1903 O OG    . SER A 250 ? 0.24506 0.17640 0.22600 -0.00198 0.01205  0.04457  250  SER A OG    
1904 N N     . PHE A 251 ? 0.22097 0.16283 0.18929 -0.00114 0.00752  0.04977  251  PHE A N     
1905 C CA    . PHE A 251 ? 0.21386 0.16111 0.18070 0.00101  0.00410  0.04974  251  PHE A CA    
1906 C C     . PHE A 251 ? 0.23858 0.18362 0.20668 0.00477  0.00105  0.05285  251  PHE A C     
1907 O O     . PHE A 251 ? 0.24567 0.18560 0.21006 0.00564  0.00075  0.05723  251  PHE A O     
1908 C CB    . PHE A 251 ? 0.24345 0.19283 0.20282 -0.00034 0.00399  0.05120  251  PHE A CB    
1909 C CG    . PHE A 251 ? 0.22873 0.18145 0.18728 -0.00347 0.00675  0.04806  251  PHE A CG    
1910 C CD1   . PHE A 251 ? 0.26036 0.21022 0.21810 -0.00637 0.01042  0.04874  251  PHE A CD1   
1911 C CD2   . PHE A 251 ? 0.24873 0.20750 0.20774 -0.00353 0.00561  0.04453  251  PHE A CD2   
1912 C CE1   . PHE A 251 ? 0.23119 0.18496 0.18891 -0.00902 0.01284  0.04594  251  PHE A CE1   
1913 C CE2   . PHE A 251 ? 0.24102 0.20290 0.19959 -0.00594 0.00805  0.04177  251  PHE A CE2   
1914 C CZ    . PHE A 251 ? 0.24078 0.20057 0.19886 -0.00857 0.01165  0.04246  251  PHE A CZ    
1915 N N     . ASP A 252 ? 0.23875 0.18792 0.21223 0.00703  -0.00119 0.05084  252  ASP A N     
1916 C CA    . ASP A 252 ? 0.22380 0.17283 0.19918 0.01084  -0.00456 0.05362  252  ASP A CA    
1917 C C     . ASP A 252 ? 0.25160 0.20277 0.22062 0.01151  -0.00785 0.05650  252  ASP A C     
1918 O O     . ASP A 252 ? 0.24900 0.20418 0.21408 0.00960  -0.00828 0.05478  252  ASP A O     
1919 C CB    . ASP A 252 ? 0.21242 0.16687 0.19541 0.01268  -0.00598 0.05064  252  ASP A CB    
1920 C CG    . ASP A 252 ? 0.21847 0.17031 0.20731 0.01293  -0.00300 0.04820  252  ASP A CG    
1921 O OD1   . ASP A 252 ? 0.22197 0.16685 0.20949 0.01225  -0.00053 0.04924  252  ASP A OD1   
1922 O OD2   . ASP A 252 ? 0.21257 0.16920 0.20712 0.01367  -0.00309 0.04518  252  ASP A OD2   
1923 N N     . ASN A 253 ? 0.25743 0.20565 0.22517 0.01444  -0.01028 0.06087  253  ASN A N     
1924 C CA    . ASN A 253 ? 0.26168 0.21112 0.22237 0.01528  -0.01361 0.06418  253  ASN A CA    
1925 C C     . ASN A 253 ? 0.28195 0.23872 0.24578 0.01706  -0.01813 0.06269  253  ASN A C     
1926 O O     . ASN A 253 ? 0.26350 0.22139 0.23198 0.02037  -0.02107 0.06453  253  ASN A O     
1927 C CB    . ASN A 253 ? 0.25205 0.19497 0.20974 0.01765  -0.01444 0.06992  253  ASN A CB    
1928 C CG    . ASN A 253 ? 0.31927 0.26235 0.26746 0.01780  -0.01694 0.07368  253  ASN A CG    
1929 O OD1   . ASN A 253 ? 0.27703 0.22603 0.22311 0.01829  -0.02052 0.07260  253  ASN A OD1   
1930 N ND2   . ASN A 253 ? 0.37212 0.30852 0.31425 0.01724  -0.01505 0.07810  253  ASN A ND2   
1931 N N     . LEU A 254 ? 0.26018 0.22198 0.22169 0.01484  -0.01878 0.05939  254  LEU A N     
1932 C CA    . LEU A 254 ? 0.24428 0.21288 0.20886 0.01578  -0.02310 0.05764  254  LEU A CA    
1933 C C     . LEU A 254 ? 0.27270 0.24228 0.23249 0.01794  -0.02799 0.06128  254  LEU A C     
1934 O O     . LEU A 254 ? 0.23543 0.20992 0.20001 0.01980  -0.03216 0.06131  254  LEU A O     
1935 C CB    . LEU A 254 ? 0.26938 0.24182 0.23205 0.01279  -0.02255 0.05322  254  LEU A CB    
1936 C CG    . LEU A 254 ? 0.25723 0.22995 0.22466 0.01066  -0.01841 0.04938  254  LEU A CG    
1937 C CD1   . LEU A 254 ? 0.21997 0.19685 0.18607 0.00841  -0.01893 0.04541  254  LEU A CD1   
1938 C CD2   . LEU A 254 ? 0.20868 0.18286 0.18576 0.01231  -0.01812 0.04867  254  LEU A CD2   
1939 N N     . LEU A 255 ? 0.26412 0.22956 0.21452 0.01762  -0.02762 0.06445  255  LEU A N     
1940 C CA    . LEU A 255 ? 0.26992 0.23607 0.21461 0.01975  -0.03239 0.06819  255  LEU A CA    
1941 C C     . LEU A 255 ? 0.28414 0.24903 0.23420 0.02365  -0.03484 0.07222  255  LEU A C     
1942 O O     . LEU A 255 ? 0.31001 0.27781 0.25868 0.02595  -0.03998 0.07467  255  LEU A O     
1943 C CB    . LEU A 255 ? 0.30065 0.26230 0.23369 0.01858  -0.03073 0.07107  255  LEU A CB    
1944 C CG    . LEU A 255 ? 0.34711 0.31105 0.27344 0.01554  -0.02937 0.06737  255  LEU A CG    
1945 C CD1   . LEU A 255 ? 0.39849 0.35814 0.31396 0.01445  -0.02667 0.07047  255  LEU A CD1   
1946 C CD2   . LEU A 255 ? 0.31491 0.28473 0.23966 0.01587  -0.03466 0.06487  255  LEU A CD2   
1947 N N     . GLU A 256 ? 0.26950 0.23020 0.22572 0.02457  -0.03144 0.07279  256  GLU A N     
1948 C CA    . GLU A 256 ? 0.27770 0.23677 0.23997 0.02870  -0.03324 0.07617  256  GLU A CA    
1949 C C     . GLU A 256 ? 0.28616 0.25135 0.25998 0.03021  -0.03426 0.07296  256  GLU A C     
1950 O O     . GLU A 256 ? 0.26692 0.23632 0.24554 0.03350  -0.03847 0.07477  256  GLU A O     
1951 C CB    . GLU A 256 ? 0.28257 0.23249 0.24441 0.02908  -0.02893 0.07872  256  GLU A CB    
1952 C CG    . GLU A 256 ? 0.30540 0.24888 0.25690 0.02872  -0.02862 0.08387  256  GLU A CG    
1953 C CD    . GLU A 256 ? 0.33125 0.26520 0.28310 0.02867  -0.02441 0.08639  256  GLU A CD    
1954 O OE1   . GLU A 256 ? 0.32114 0.25334 0.28116 0.02937  -0.02213 0.08396  256  GLU A OE1   
1955 O OE2   . GLU A 256 ? 0.37450 0.30257 0.31828 0.02782  -0.02335 0.09079  256  GLU A OE2   
1956 N N     . VAL A 257 ? 0.25244 0.21865 0.23089 0.02788  -0.03044 0.06838  257  VAL A N     
1957 C CA    . VAL A 257 ? 0.26560 0.23727 0.25483 0.02927  -0.03060 0.06560  257  VAL A CA    
1958 C C     . VAL A 257 ? 0.23452 0.21515 0.22628 0.02809  -0.03429 0.06309  257  VAL A C     
1959 O O     . VAL A 257 ? 0.24999 0.23661 0.25073 0.02988  -0.03597 0.06223  257  VAL A O     
1960 C CB    . VAL A 257 ? 0.27468 0.24381 0.26752 0.02735  -0.02516 0.06187  257  VAL A CB    
1961 C CG1   . VAL A 257 ? 0.28921 0.24887 0.27899 0.02776  -0.02166 0.06407  257  VAL A CG1   
1962 C CG2   . VAL A 257 ? 0.30197 0.27346 0.29127 0.02295  -0.02349 0.05795  257  VAL A CG2   
1963 N N     . GLY A 258 ? 0.23181 0.21349 0.21606 0.02512  -0.03553 0.06186  258  GLY A N     
1964 C CA    . GLY A 258 ? 0.21664 0.20564 0.20254 0.02358  -0.03913 0.05924  258  GLY A CA    
1965 C C     . GLY A 258 ? 0.24357 0.23799 0.23293 0.02631  -0.04506 0.06174  258  GLY A C     
1966 O O     . GLY A 258 ? 0.22164 0.22298 0.21984 0.02668  -0.04709 0.06021  258  GLY A O     
1967 N N     . PRO A 259 ? 0.24495 0.23671 0.22732 0.02816  -0.04805 0.06581  259  PRO A N     
1968 C CA    . PRO A 259 ? 0.24842 0.24556 0.23409 0.03111  -0.05417 0.06861  259  PRO A CA    
1969 C C     . PRO A 259 ? 0.26596 0.26620 0.26360 0.03480  -0.05420 0.06997  259  PRO A C     
1970 O O     . PRO A 259 ? 0.24727 0.25542 0.25213 0.03618  -0.05861 0.07014  259  PRO A O     
1971 C CB    . PRO A 259 ? 0.29953 0.29116 0.27459 0.03271  -0.05594 0.07332  259  PRO A CB    
1972 C CG    . PRO A 259 ? 0.27921 0.26616 0.24406 0.02902  -0.05256 0.07132  259  PRO A CG    
1973 C CD    . PRO A 259 ? 0.26625 0.25129 0.23658 0.02708  -0.04659 0.06777  259  PRO A CD    
1974 N N     . ILE A 260 ? 0.23929 0.23368 0.23943 0.03646  -0.04940 0.07079  260  ILE A N     
1975 C CA    . ILE A 260 ? 0.24900 0.24586 0.26028 0.04038  -0.04888 0.07167  260  ILE A CA    
1976 C C     . ILE A 260 ? 0.20720 0.21201 0.22825 0.03885  -0.04789 0.06736  260  ILE A C     
1977 O O     . ILE A 260 ? 0.20565 0.21804 0.23620 0.04129  -0.05056 0.06789  260  ILE A O     
1978 C CB    . ILE A 260 ? 0.27641 0.26406 0.28722 0.04220  -0.04379 0.07293  260  ILE A CB    
1979 C CG1   . ILE A 260 ? 0.30431 0.28418 0.30612 0.04387  -0.04506 0.07805  260  ILE A CG1   
1980 C CG2   . ILE A 260 ? 0.28404 0.27413 0.30639 0.04638  -0.04267 0.07293  260  ILE A CG2   
1981 C CD1   . ILE A 260 ? 0.31463 0.28420 0.31465 0.04463  -0.04006 0.07925  260  ILE A CD1   
1982 N N     . CYS A 261 ? 0.21037 0.21387 0.22944 0.03481  -0.04401 0.06329  261  CYS A N     
1983 C CA    . CYS A 261 ? 0.19092 0.20148 0.21841 0.03302  -0.04285 0.05950  261  CYS A CA    
1984 C C     . CYS A 261 ? 0.21376 0.23322 0.24447 0.03182  -0.04842 0.05915  261  CYS A C     
1985 O O     . CYS A 261 ? 0.22666 0.25399 0.26765 0.03244  -0.04928 0.05829  261  CYS A O     
1986 C CB    . CYS A 261 ? 0.18490 0.19207 0.20829 0.02884  -0.03832 0.05560  261  CYS A CB    
1987 S SG    . CYS A 261 ? 0.20788 0.20670 0.23076 0.02967  -0.03158 0.05483  261  CYS A SG    
1988 N N     . ASN A 262 ? 0.22100 0.23947 0.24304 0.02999  -0.05222 0.05974  262  ASN A N     
1989 C CA    . ASN A 262 ? 0.24628 0.27258 0.27067 0.02860  -0.05806 0.05918  262  ASN A CA    
1990 C C     . ASN A 262 ? 0.23761 0.27035 0.27011 0.03263  -0.06248 0.06254  262  ASN A C     
1991 O O     . ASN A 262 ? 0.25684 0.29858 0.29854 0.03207  -0.06532 0.06160  262  ASN A O     
1992 C CB    . ASN A 262 ? 0.24051 0.26361 0.25276 0.02637  -0.06126 0.05909  262  ASN A CB    
1993 C CG    . ASN A 262 ? 0.25444 0.27272 0.25965 0.02239  -0.05738 0.05540  262  ASN A CG    
1994 O OD1   . ASN A 262 ? 0.25270 0.27132 0.26275 0.02067  -0.05326 0.05257  262  ASN A OD1   
1995 N ND2   . ASN A 262 ? 0.23115 0.24521 0.22478 0.02108  -0.05870 0.05545  262  ASN A ND2   
1996 N N     . LYS A 263 ? 0.23974 0.26812 0.26932 0.03672  -0.06313 0.06668  263  LYS A N     
1997 C CA    . LYS A 263 ? 0.25559 0.28986 0.29262 0.04116  -0.06760 0.07029  263  LYS A CA    
1998 C C     . LYS A 263 ? 0.26297 0.30284 0.31382 0.04363  -0.06486 0.06958  263  LYS A C     
1999 O O     . LYS A 263 ? 0.26961 0.31882 0.33022 0.04565  -0.06866 0.07074  263  LYS A O     
2000 C CB    . LYS A 263 ? 0.27559 0.30253 0.30578 0.04515  -0.06838 0.07514  263  LYS A CB    
2001 C CG    . LYS A 263 ? 0.38328 0.40741 0.40096 0.04382  -0.07277 0.07703  263  LYS A CG    
2002 C CD    . LYS A 263 ? 0.45169 0.46917 0.46362 0.04810  -0.07371 0.08262  263  LYS A CD    
2003 C CE    . LYS A 263 ? 0.56250 0.57641 0.56036 0.04660  -0.07715 0.08457  263  LYS A CE    
2004 N NZ    . LYS A 263 ? 0.55830 0.56106 0.54631 0.04736  -0.07322 0.08769  263  LYS A NZ    
2005 N N     . GLU A 264 ? 0.22912 0.26383 0.28099 0.04351  -0.05827 0.06761  264  GLU A N     
2006 C CA    . GLU A 264 ? 0.24400 0.28307 0.30766 0.04603  -0.05482 0.06661  264  GLU A CA    
2007 C C     . GLU A 264 ? 0.22141 0.26832 0.29196 0.04222  -0.05349 0.06273  264  GLU A C     
2008 O O     . GLU A 264 ? 0.20177 0.25343 0.28215 0.04393  -0.05036 0.06168  264  GLU A O     
2009 C CB    . GLU A 264 ? 0.24579 0.27521 0.30677 0.04767  -0.04847 0.06608  264  GLU A CB    
2010 C CG    . GLU A 264 ? 0.23774 0.25839 0.29273 0.05148  -0.04910 0.07020  264  GLU A CG    
2011 C CD    . GLU A 264 ? 0.25109 0.27449 0.31514 0.05784  -0.05036 0.07324  264  GLU A CD    
2012 O OE1   . GLU A 264 ? 0.27424 0.30479 0.34928 0.05954  -0.04867 0.07147  264  GLU A OE1   
2013 O OE2   . GLU A 264 ? 0.31675 0.33512 0.37686 0.06129  -0.05291 0.07756  264  GLU A OE2   
2014 N N     . ASP A 265 ? 0.21476 0.26289 0.28019 0.03723  -0.05571 0.06065  265  ASP A N     
2015 C CA    . ASP A 265 ? 0.20509 0.25888 0.27550 0.03299  -0.05428 0.05706  265  ASP A CA    
2016 C C     . ASP A 265 ? 0.21792 0.26736 0.28858 0.03216  -0.04715 0.05440  265  ASP A C     
2017 O O     . ASP A 265 ? 0.21151 0.26678 0.29037 0.03120  -0.04460 0.05258  265  ASP A O     
2018 C CB    . ASP A 265 ? 0.23314 0.29917 0.31664 0.03377  -0.05731 0.05770  265  ASP A CB    
2019 C CG    . ASP A 265 ? 0.34389 0.41570 0.42902 0.02837  -0.06014 0.05530  265  ASP A CG    
2020 O OD1   . ASP A 265 ? 0.38250 0.44902 0.45767 0.02483  -0.06164 0.05373  265  ASP A OD1   
2021 O OD2   . ASP A 265 ? 0.33714 0.41865 0.43362 0.02764  -0.06070 0.05498  265  ASP A OD2   
2022 N N     . ILE A 266 ? 0.17694 0.21631 0.23849 0.03242  -0.04398 0.05429  266  ILE A N     
2023 C CA    . ILE A 266 ? 0.17346 0.20783 0.23344 0.03114  -0.03772 0.05155  266  ILE A CA    
2024 C C     . ILE A 266 ? 0.16312 0.19491 0.21576 0.02597  -0.03719 0.04876  266  ILE A C     
2025 O O     . ILE A 266 ? 0.18792 0.21523 0.23151 0.02454  -0.03943 0.04932  266  ILE A O     
2026 C CB    . ILE A 266 ? 0.17508 0.19998 0.22999 0.03408  -0.03462 0.05292  266  ILE A CB    
2027 C CG1   . ILE A 266 ? 0.21211 0.23885 0.27472 0.03970  -0.03480 0.05545  266  ILE A CG1   
2028 C CG2   . ILE A 266 ? 0.16751 0.18703 0.21966 0.03205  -0.02870 0.04974  266  ILE A CG2   
2029 C CD1   . ILE A 266 ? 0.19345 0.20998 0.25094 0.04269  -0.03254 0.05728  266  ILE A CD1   
2030 N N     . TRP A 267 ? 0.15629 0.19097 0.21267 0.02337  -0.03418 0.04587  267  TRP A N     
2031 C CA    . TRP A 267 ? 0.15526 0.18685 0.20504 0.01892  -0.03312 0.04317  267  TRP A CA    
2032 C C     . TRP A 267 ? 0.17103 0.19328 0.21191 0.01887  -0.02965 0.04267  267  TRP A C     
2033 O O     . TRP A 267 ? 0.15414 0.17327 0.19639 0.02040  -0.02537 0.04216  267  TRP A O     
2034 C CB    . TRP A 267 ? 0.14611 0.18235 0.20199 0.01660  -0.03027 0.04070  267  TRP A CB    
2035 C CG    . TRP A 267 ? 0.17317 0.20661 0.22329 0.01230  -0.02930 0.03803  267  TRP A CG    
2036 C CD1   . TRP A 267 ? 0.16841 0.19459 0.21037 0.01112  -0.02640 0.03655  267  TRP A CD1   
2037 C CD2   . TRP A 267 ? 0.16858 0.20647 0.22124 0.00872  -0.03123 0.03661  267  TRP A CD2   
2038 N NE1   . TRP A 267 ? 0.16430 0.19032 0.20356 0.00747  -0.02645 0.03431  267  TRP A NE1   
2039 C CE2   . TRP A 267 ? 0.20726 0.23984 0.25273 0.00591  -0.02938 0.03430  267  TRP A CE2   
2040 C CE3   . TRP A 267 ? 0.17097 0.21681 0.23162 0.00753  -0.03440 0.03714  267  TRP A CE3   
2041 C CZ2   . TRP A 267 ? 0.19358 0.22772 0.23922 0.00226  -0.03061 0.03254  267  TRP A CZ2   
2042 C CZ3   . TRP A 267 ? 0.23613 0.28344 0.29697 0.00341  -0.03561 0.03539  267  TRP A CZ3   
2043 C CH2   . TRP A 267 ? 0.23254 0.27362 0.28572 0.00096  -0.03373 0.03312  267  TRP A CH2   
2044 N N     . LEU A 268 ? 0.17375 0.19172 0.20557 0.01702  -0.03147 0.04269  268  LEU A N     
2045 C CA    . LEU A 268 ? 0.16066 0.17047 0.18399 0.01658  -0.02845 0.04253  268  LEU A CA    
2046 C C     . LEU A 268 ? 0.15869 0.16715 0.17853 0.01288  -0.02593 0.03919  268  LEU A C     
2047 O O     . LEU A 268 ? 0.18223 0.19178 0.19841 0.01048  -0.02832 0.03797  268  LEU A O     
2048 C CB    . LEU A 268 ? 0.17631 0.18251 0.19158 0.01725  -0.03160 0.04503  268  LEU A CB    
2049 C CG    . LEU A 268 ? 0.17483 0.17322 0.18099 0.01628  -0.02859 0.04520  268  LEU A CG    
2050 C CD1   . LEU A 268 ? 0.17106 0.16485 0.17945 0.01771  -0.02402 0.04546  268  LEU A CD1   
2051 C CD2   . LEU A 268 ? 0.22548 0.22099 0.22400 0.01736  -0.03171 0.04834  268  LEU A CD2   
2052 N N     . HIS A 269 ? 0.15225 0.15818 0.17314 0.01257  -0.02128 0.03761  269  HIS A N     
2053 C CA    . HIS A 269 ? 0.14812 0.15228 0.16551 0.00951  -0.01862 0.03475  269  HIS A CA    
2054 C C     . HIS A 269 ? 0.15141 0.14868 0.16164 0.00921  -0.01603 0.03497  269  HIS A C     
2055 O O     . HIS A 269 ? 0.16312 0.15677 0.17391 0.01108  -0.01402 0.03623  269  HIS A O     
2056 C CB    . HIS A 269 ? 0.14227 0.14921 0.16581 0.00907  -0.01540 0.03275  269  HIS A CB    
2057 C CG    . HIS A 269 ? 0.13851 0.14355 0.15858 0.00631  -0.01271 0.03010  269  HIS A CG    
2058 N ND1   . HIS A 269 ? 0.15899 0.16541 0.17674 0.00374  -0.01428 0.02869  269  HIS A ND1   
2059 C CD2   . HIS A 269 ? 0.14355 0.14537 0.16212 0.00582  -0.00880 0.02860  269  HIS A CD2   
2060 C CE1   . HIS A 269 ? 0.15867 0.16305 0.17389 0.00207  -0.01138 0.02667  269  HIS A CE1   
2061 N NE2   . HIS A 269 ? 0.13849 0.14038 0.15416 0.00316  -0.00814 0.02656  269  HIS A NE2   
2062 N N     . VAL A 270 ? 0.15136 0.14678 0.15513 0.00688  -0.01602 0.03374  270  VAL A N     
2063 C CA    . VAL A 270 ? 0.15425 0.14411 0.15147 0.00613  -0.01344 0.03397  270  VAL A CA    
2064 C C     . VAL A 270 ? 0.18048 0.16992 0.17802 0.00402  -0.00988 0.03104  270  VAL A C     
2065 O O     . VAL A 270 ? 0.16584 0.15758 0.16270 0.00223  -0.01031 0.02892  270  VAL A O     
2066 C CB    . VAL A 270 ? 0.15909 0.14751 0.14846 0.00537  -0.01560 0.03481  270  VAL A CB    
2067 C CG1   . VAL A 270 ? 0.17930 0.16291 0.16260 0.00427  -0.01234 0.03505  270  VAL A CG1   
2068 C CG2   . VAL A 270 ? 0.17878 0.16744 0.16722 0.00762  -0.01929 0.03802  270  VAL A CG2   
2069 N N     . ASP A 271 ? 0.14914 0.13538 0.14767 0.00429  -0.00659 0.03092  271  ASP A N     
2070 C CA    . ASP A 271 ? 0.17607 0.16166 0.17451 0.00235  -0.00332 0.02833  271  ASP A CA    
2071 C C     . ASP A 271 ? 0.17429 0.15603 0.16650 0.00083  -0.00174 0.02869  271  ASP A C     
2072 O O     . ASP A 271 ? 0.16450 0.14189 0.15512 0.00127  -0.00041 0.03042  271  ASP A O     
2073 C CB    . ASP A 271 ? 0.17719 0.16174 0.18034 0.00337  -0.00084 0.02760  271  ASP A CB    
2074 C CG    . ASP A 271 ? 0.19873 0.18227 0.20126 0.00135  0.00231  0.02498  271  ASP A CG    
2075 O OD1   . ASP A 271 ? 0.18268 0.16673 0.18181 -0.00073 0.00270  0.02387  271  ASP A OD1   
2076 O OD2   . ASP A 271 ? 0.16697 0.14927 0.17245 0.00202  0.00436  0.02392  271  ASP A OD2   
2077 N N     . ALA A 272 ? 0.14760 0.13091 0.13653 -0.00091 -0.00177 0.02714  272  ALA A N     
2078 C CA    . ALA A 272 ? 0.15379 0.13480 0.13739 -0.00242 0.00010  0.02720  272  ALA A CA    
2079 C C     . ALA A 272 ? 0.16158 0.14447 0.14595 -0.00427 0.00219  0.02429  272  ALA A C     
2080 O O     . ALA A 272 ? 0.16587 0.14939 0.14649 -0.00534 0.00279  0.02349  272  ALA A O     
2081 C CB    . ALA A 272 ? 0.18325 0.16436 0.16100 -0.00221 -0.00201 0.02837  272  ALA A CB    
2082 N N     . ALA A 273 ? 0.15200 0.13593 0.14113 -0.00444 0.00338  0.02273  273  ALA A N     
2083 C CA    . ALA A 273 ? 0.18193 0.16836 0.17231 -0.00584 0.00467  0.02009  273  ALA A CA    
2084 C C     . ALA A 273 ? 0.16729 0.15321 0.15434 -0.00749 0.00663  0.01941  273  ALA A C     
2085 O O     . ALA A 273 ? 0.15416 0.14251 0.14016 -0.00811 0.00655  0.01787  273  ALA A O     
2086 C CB    . ALA A 273 ? 0.18598 0.17270 0.18077 -0.00579 0.00618  0.01886  273  ALA A CB    
2087 N N     . TYR A 274 ? 0.14959 0.13244 0.13533 -0.00822 0.00844  0.02062  274  TYR A N     
2088 C CA    . TYR A 274 ? 0.17794 0.16102 0.16128 -0.01005 0.01054  0.02024  274  TYR A CA    
2089 C C     . TYR A 274 ? 0.20562 0.18798 0.18374 -0.00984 0.01026  0.02214  274  TYR A C     
2090 O O     . TYR A 274 ? 0.18515 0.17002 0.16090 -0.01026 0.01072  0.02110  274  TYR A O     
2091 C CB    . TYR A 274 ? 0.20245 0.18264 0.18735 -0.01157 0.01284  0.02046  274  TYR A CB    
2092 C CG    . TYR A 274 ? 0.18402 0.16405 0.16654 -0.01366 0.01501  0.02116  274  TYR A CG    
2093 C CD1   . TYR A 274 ? 0.18586 0.17005 0.16886 -0.01498 0.01612  0.01920  274  TYR A CD1   
2094 C CD2   . TYR A 274 ? 0.18976 0.16575 0.16977 -0.01424 0.01600  0.02404  274  TYR A CD2   
2095 C CE1   . TYR A 274 ? 0.18706 0.17212 0.16863 -0.01690 0.01833  0.01989  274  TYR A CE1   
2096 C CE2   . TYR A 274 ? 0.18779 0.16415 0.16591 -0.01643 0.01832  0.02497  274  TYR A CE2   
2097 C CZ    . TYR A 274 ? 0.21065 0.19192 0.18983 -0.01779 0.01954  0.02279  274  TYR A CZ    
2098 O OH    . TYR A 274 ? 0.18791 0.17053 0.16597 -0.01997 0.02205  0.02376  274  TYR A OH    
2099 N N     . ALA A 275 ? 0.15987 0.13884 0.13592 -0.00895 0.00953  0.02495  275  ALA A N     
2100 C CA    . ALA A 275 ? 0.17492 0.15280 0.14517 -0.00890 0.00963  0.02718  275  ALA A CA    
2101 C C     . ALA A 275 ? 0.17164 0.15205 0.13839 -0.00769 0.00734  0.02632  275  ALA A C     
2102 O O     . ALA A 275 ? 0.16337 0.14401 0.12472 -0.00782 0.00795  0.02707  275  ALA A O     
2103 C CB    . ALA A 275 ? 0.18643 0.15980 0.15521 -0.00795 0.00896  0.03072  275  ALA A CB    
2104 N N     . GLY A 276 ? 0.16843 0.15064 0.13800 -0.00663 0.00481  0.02473  276  GLY A N     
2105 C CA    . GLY A 276 ? 0.17852 0.16222 0.14488 -0.00564 0.00208  0.02393  276  GLY A CA    
2106 C C     . GLY A 276 ? 0.18119 0.16661 0.14385 -0.00615 0.00328  0.02191  276  GLY A C     
2107 O O     . GLY A 276 ? 0.17868 0.16406 0.13608 -0.00538 0.00180  0.02173  276  GLY A O     
2108 N N     . SER A 277 ? 0.15721 0.14429 0.12249 -0.00727 0.00589  0.02025  277  SER A N     
2109 C CA    . SER A 277 ? 0.18266 0.17189 0.14533 -0.00733 0.00717  0.01823  277  SER A CA    
2110 C C     . SER A 277 ? 0.19610 0.18488 0.15268 -0.00738 0.00900  0.01970  277  SER A C     
2111 O O     . SER A 277 ? 0.20414 0.19413 0.15649 -0.00656 0.00914  0.01822  277  SER A O     
2112 C CB    . SER A 277 ? 0.18495 0.17660 0.15221 -0.00844 0.00946  0.01656  277  SER A CB    
2113 O OG    . SER A 277 ? 0.18269 0.17508 0.15456 -0.00826 0.00787  0.01512  277  SER A OG    
2114 N N     . ALA A 278 ? 0.19660 0.18341 0.15245 -0.00828 0.01056  0.02263  278  ALA A N     
2115 C CA    . ALA A 278 ? 0.20173 0.18813 0.15164 -0.00859 0.01266  0.02462  278  ALA A CA    
2116 C C     . ALA A 278 ? 0.20143 0.18641 0.14444 -0.00692 0.01014  0.02558  278  ALA A C     
2117 O O     . ALA A 278 ? 0.22514 0.21051 0.16187 -0.00676 0.01174  0.02648  278  ALA A O     
2118 C CB    . ALA A 278 ? 0.20463 0.18847 0.15565 -0.01022 0.01480  0.02789  278  ALA A CB    
2119 N N     . PHE A 279 ? 0.20832 0.19204 0.15229 -0.00574 0.00625  0.02538  279  PHE A N     
2120 C CA    . PHE A 279 ? 0.20751 0.19005 0.14509 -0.00432 0.00324  0.02630  279  PHE A CA    
2121 C C     . PHE A 279 ? 0.22676 0.21087 0.15957 -0.00345 0.00240  0.02308  279  PHE A C     
2122 O O     . PHE A 279 ? 0.24067 0.22384 0.16717 -0.00237 -0.00014 0.02332  279  PHE A O     
2123 C CB    . PHE A 279 ? 0.20711 0.18861 0.14820 -0.00346 -0.00083 0.02708  279  PHE A CB    
2124 C CG    . PHE A 279 ? 0.21773 0.19728 0.16358 -0.00374 -0.00010 0.02992  279  PHE A CG    
2125 C CD1   . PHE A 279 ? 0.24627 0.22367 0.19053 -0.00465 0.00308  0.03265  279  PHE A CD1   
2126 C CD2   . PHE A 279 ? 0.21793 0.19769 0.16995 -0.00309 -0.00246 0.02982  279  PHE A CD2   
2127 C CE1   . PHE A 279 ? 0.24205 0.21668 0.19052 -0.00481 0.00366  0.03497  279  PHE A CE1   
2128 C CE2   . PHE A 279 ? 0.19928 0.17693 0.15550 -0.00292 -0.00165 0.03205  279  PHE A CE2   
2129 C CZ    . PHE A 279 ? 0.23590 0.21055 0.19021 -0.00373 0.00131  0.03451  279  PHE A CZ    
2130 N N     . ILE A 280 ? 0.18851 0.17477 0.12394 -0.00373 0.00430  0.02001  280  ILE A N     
2131 C CA    . ILE A 280 ? 0.23360 0.22082 0.16396 -0.00261 0.00431  0.01696  280  ILE A CA    
2132 C C     . ILE A 280 ? 0.24609 0.23423 0.16971 -0.00240 0.00778  0.01802  280  ILE A C     
2133 O O     . ILE A 280 ? 0.23669 0.22540 0.15455 -0.00108 0.00801  0.01564  280  ILE A O     
2134 C CB    . ILE A 280 ? 0.21682 0.20594 0.15231 -0.00256 0.00522  0.01356  280  ILE A CB    
2135 C CG1   . ILE A 280 ? 0.23537 0.22721 0.17437 -0.00359 0.00968  0.01410  280  ILE A CG1   
2136 C CG2   . ILE A 280 ? 0.23914 0.22762 0.18126 -0.00299 0.00226  0.01289  280  ILE A CG2   
2137 C CD1   . ILE A 280 ? 0.25303 0.24735 0.19547 -0.00299 0.01084  0.01088  280  ILE A CD1   
2138 N N     . CYS A 281 ? 0.21889 0.20703 0.14306 -0.00372 0.01065  0.02152  281  CYS A N     
2139 C CA    . CYS A 281 ? 0.22641 0.21554 0.14450 -0.00399 0.01428  0.02347  281  CYS A CA    
2140 C C     . CYS A 281 ? 0.24515 0.23134 0.15607 -0.00350 0.01246  0.02692  281  CYS A C     
2141 O O     . CYS A 281 ? 0.27462 0.25819 0.18817 -0.00402 0.01060  0.02981  281  CYS A O     
2142 C CB    . CYS A 281 ? 0.23141 0.22207 0.15469 -0.00619 0.01845  0.02551  281  CYS A CB    
2143 S SG    . CYS A 281 ? 0.24548 0.24061 0.17673 -0.00675 0.02076  0.02182  281  CYS A SG    
2144 N N     . PRO A 282 ? 0.26333 0.24987 0.16500 -0.00230 0.01288  0.02672  282  PRO A N     
2145 C CA    . PRO A 282 ? 0.28236 0.26620 0.17635 -0.00162 0.01055  0.03007  282  PRO A CA    
2146 C C     . PRO A 282 ? 0.27945 0.26133 0.17389 -0.00308 0.01257  0.03559  282  PRO A C     
2147 O O     . PRO A 282 ? 0.28977 0.26865 0.18171 -0.00251 0.00952  0.03879  282  PRO A O     
2148 C CB    . PRO A 282 ? 0.27605 0.26132 0.15975 -0.00024 0.01197  0.02851  282  PRO A CB    
2149 C CG    . PRO A 282 ? 0.35317 0.34211 0.23999 -0.00034 0.01618  0.02519  282  PRO A CG    
2150 C CD    . PRO A 282 ? 0.27337 0.26270 0.17098 -0.00109 0.01503  0.02306  282  PRO A CD    
2151 N N     . GLU A 283 ? 0.28308 0.26647 0.18096 -0.00497 0.01745  0.03688  283  GLU A N     
2152 C CA    . GLU A 283 ? 0.26392 0.24468 0.16223 -0.00672 0.01954  0.04215  283  GLU A CA    
2153 C C     . GLU A 283 ? 0.32778 0.30518 0.23398 -0.00730 0.01720  0.04345  283  GLU A C     
2154 O O     . GLU A 283 ? 0.31838 0.29213 0.22446 -0.00822 0.01785  0.04792  283  GLU A O     
2155 C CB    . GLU A 283 ? 0.27259 0.25625 0.17301 -0.00904 0.02537  0.04290  283  GLU A CB    
2156 C CG    . GLU A 283 ? 0.29255 0.27879 0.20319 -0.01041 0.02669  0.03973  283  GLU A CG    
2157 C CD    . GLU A 283 ? 0.26981 0.26110 0.18082 -0.00921 0.02775  0.03487  283  GLU A CD    
2158 O OE1   . GLU A 283 ? 0.26653 0.25805 0.17130 -0.00684 0.02569  0.03267  283  GLU A OE1   
2159 O OE2   . GLU A 283 ? 0.28607 0.28095 0.20360 -0.01057 0.03050  0.03319  283  GLU A OE2   
2160 N N     . PHE A 284 ? 0.27354 0.25188 0.18638 -0.00670 0.01465  0.03976  284  PHE A N     
2161 C CA    . PHE A 284 ? 0.27971 0.25540 0.19984 -0.00686 0.01251  0.04053  284  PHE A CA    
2162 C C     . PHE A 284 ? 0.27697 0.25179 0.19704 -0.00471 0.00722  0.03979  284  PHE A C     
2163 O O     . PHE A 284 ? 0.28721 0.26011 0.21296 -0.00438 0.00534  0.04072  284  PHE A O     
2164 C CB    . PHE A 284 ? 0.26734 0.24517 0.19623 -0.00822 0.01414  0.03729  284  PHE A CB    
2165 C CG    . PHE A 284 ? 0.25841 0.23787 0.18897 -0.01063 0.01897  0.03778  284  PHE A CG    
2166 C CD1   . PHE A 284 ? 0.32033 0.29670 0.25039 -0.01244 0.02136  0.04190  284  PHE A CD1   
2167 C CD2   . PHE A 284 ? 0.25689 0.24100 0.18990 -0.01114 0.02100  0.03423  284  PHE A CD2   
2168 C CE1   . PHE A 284 ? 0.31165 0.28995 0.24391 -0.01512 0.02571  0.04238  284  PHE A CE1   
2169 C CE2   . PHE A 284 ? 0.27994 0.26653 0.21529 -0.01343 0.02526  0.03469  284  PHE A CE2   
2170 C CZ    . PHE A 284 ? 0.28678 0.27065 0.22189 -0.01564 0.02763  0.03873  284  PHE A CZ    
2171 N N     . ARG A 285 ? 0.26658 0.24290 0.18053 -0.00327 0.00481  0.03801  285  ARG A N     
2172 C CA    . ARG A 285 ? 0.27359 0.24982 0.18812 -0.00166 -0.00049 0.03689  285  ARG A CA    
2173 C C     . ARG A 285 ? 0.28479 0.25817 0.19831 -0.00059 -0.00323 0.04131  285  ARG A C     
2174 O O     . ARG A 285 ? 0.27078 0.24440 0.18851 0.00049  -0.00720 0.04102  285  ARG A O     
2175 C CB    . ARG A 285 ? 0.30258 0.28041 0.20971 -0.00063 -0.00243 0.03402  285  ARG A CB    
2176 C CG    . ARG A 285 ? 0.26820 0.24632 0.17551 0.00058  -0.00820 0.03233  285  ARG A CG    
2177 C CD    . ARG A 285 ? 0.28026 0.25937 0.19788 0.00017  -0.00989 0.03051  285  ARG A CD    
2178 N NE    . ARG A 285 ? 0.27850 0.25829 0.19686 0.00100  -0.01540 0.02968  285  ARG A NE    
2179 C CZ    . ARG A 285 ? 0.28362 0.26296 0.20251 0.00199  -0.01870 0.03284  285  ARG A CZ    
2180 N NH1   . ARG A 285 ? 0.27303 0.25038 0.19133 0.00249  -0.01715 0.03721  285  ARG A NH1   
2181 N NH2   . ARG A 285 ? 0.25009 0.23101 0.17041 0.00247  -0.02380 0.03167  285  ARG A NH2   
2182 N N     . HIS A 286 ? 0.28203 0.25286 0.19041 -0.00083 -0.00112 0.04564  286  HIS A N     
2183 C CA    . HIS A 286 ? 0.29264 0.26025 0.20002 0.00050  -0.00371 0.05028  286  HIS A CA    
2184 C C     . HIS A 286 ? 0.27860 0.24441 0.19580 0.00061  -0.00404 0.05098  286  HIS A C     
2185 O O     . HIS A 286 ? 0.29027 0.25449 0.20900 0.00244  -0.00738 0.05353  286  HIS A O     
2186 C CB    . HIS A 286 ? 0.31776 0.28237 0.21778 -0.00006 -0.00084 0.05515  286  HIS A CB    
2187 C CG    . HIS A 286 ? 0.31820 0.28074 0.22256 -0.00235 0.00421  0.05660  286  HIS A CG    
2188 N ND1   . HIS A 286 ? 0.35279 0.31793 0.25768 -0.00447 0.00860  0.05416  286  HIS A ND1   
2189 C CD2   . HIS A 286 ? 0.31504 0.27310 0.22363 -0.00290 0.00537  0.06008  286  HIS A CD2   
2190 C CE1   . HIS A 286 ? 0.36162 0.32434 0.27101 -0.00656 0.01210  0.05610  286  HIS A CE1   
2191 N NE2   . HIS A 286 ? 0.32427 0.28223 0.23575 -0.00571 0.01026  0.05959  286  HIS A NE2   
2192 N N     . LEU A 287 ? 0.27775 0.24402 0.20155 -0.00112 -0.00074 0.04865  287  LEU A N     
2193 C CA    . LEU A 287 ? 0.28449 0.24908 0.21710 -0.00096 -0.00081 0.04870  287  LEU A CA    
2194 C C     . LEU A 287 ? 0.28481 0.25219 0.22280 0.00065  -0.00481 0.04624  287  LEU A C     
2195 O O     . LEU A 287 ? 0.27052 0.23677 0.21510 0.00159  -0.00557 0.04681  287  LEU A O     
2196 C CB    . LEU A 287 ? 0.30674 0.27165 0.24432 -0.00335 0.00343  0.04638  287  LEU A CB    
2197 C CG    . LEU A 287 ? 0.31964 0.28206 0.25400 -0.00552 0.00772  0.04893  287  LEU A CG    
2198 C CD1   . LEU A 287 ? 0.30952 0.27454 0.24809 -0.00798 0.01128  0.04562  287  LEU A CD1   
2199 C CD2   . LEU A 287 ? 0.33073 0.28721 0.26658 -0.00540 0.00819  0.05313  287  LEU A CD2   
2200 N N     . LEU A 288 ? 0.25243 0.22337 0.18785 0.00093  -0.00725 0.04348  288  LEU A N     
2201 C CA    . LEU A 288 ? 0.24995 0.22388 0.19035 0.00195  -0.01115 0.04125  288  LEU A CA    
2202 C C     . LEU A 288 ? 0.25157 0.22589 0.18884 0.00393  -0.01602 0.04358  288  LEU A C     
2203 O O     . LEU A 288 ? 0.25224 0.22942 0.19427 0.00473  -0.01963 0.04231  288  LEU A O     
2204 C CB    . LEU A 288 ? 0.23316 0.21025 0.17329 0.00081  -0.01118 0.03664  288  LEU A CB    
2205 C CG    . LEU A 288 ? 0.21944 0.19968 0.16513 0.00101  -0.01455 0.03380  288  LEU A CG    
2206 C CD1   . LEU A 288 ? 0.22916 0.21005 0.18423 0.00109  -0.01372 0.03382  288  LEU A CD1   
2207 C CD2   . LEU A 288 ? 0.23724 0.21912 0.18142 -0.00017 -0.01397 0.02964  288  LEU A CD2   
2208 N N     . ASN A 289 ? 0.26458 0.23640 0.19410 0.00466  -0.01626 0.04717  289  ASN A N     
2209 C CA    . ASN A 289 ? 0.25723 0.22958 0.18297 0.00665  -0.02122 0.04965  289  ASN A CA    
2210 C C     . ASN A 289 ? 0.26949 0.24241 0.20359 0.00854  -0.02388 0.05143  289  ASN A C     
2211 O O     . ASN A 289 ? 0.26202 0.23209 0.20091 0.00902  -0.02140 0.05339  289  ASN A O     
2212 C CB    . ASN A 289 ? 0.29268 0.26159 0.20891 0.00720  -0.02036 0.05407  289  ASN A CB    
2213 C CG    . ASN A 289 ? 0.32795 0.29750 0.23471 0.00595  -0.01868 0.05231  289  ASN A CG    
2214 O OD1   . ASN A 289 ? 0.34165 0.31403 0.24851 0.00508  -0.01904 0.04767  289  ASN A OD1   
2215 N ND2   . ASN A 289 ? 0.35390 0.32069 0.25232 0.00598  -0.01670 0.05612  289  ASN A ND2   
2216 N N     . GLY A 290 ? 0.27945 0.25617 0.21547 0.00962  -0.02895 0.05059  290  GLY A N     
2217 C CA    . GLY A 290 ? 0.25578 0.23476 0.20089 0.01144  -0.03161 0.05164  290  GLY A CA    
2218 C C     . GLY A 290 ? 0.25934 0.24268 0.21305 0.01032  -0.03201 0.04752  290  GLY A C     
2219 O O     . GLY A 290 ? 0.23194 0.21855 0.19346 0.01173  -0.03452 0.04806  290  GLY A O     
2220 N N     . VAL A 291 ? 0.24928 0.23299 0.20196 0.00793  -0.02955 0.04364  291  VAL A N     
2221 C CA    . VAL A 291 ? 0.21185 0.19932 0.17202 0.00669  -0.02993 0.04002  291  VAL A CA    
2222 C C     . VAL A 291 ? 0.23716 0.22891 0.19861 0.00673  -0.03554 0.03907  291  VAL A C     
2223 O O     . VAL A 291 ? 0.21087 0.20643 0.18030 0.00609  -0.03674 0.03733  291  VAL A O     
2224 C CB    . VAL A 291 ? 0.22685 0.21333 0.18468 0.00438  -0.02639 0.03641  291  VAL A CB    
2225 C CG1   . VAL A 291 ? 0.24678 0.23281 0.19559 0.00361  -0.02807 0.03476  291  VAL A CG1   
2226 C CG2   . VAL A 291 ? 0.21284 0.20236 0.17885 0.00317  -0.02593 0.03338  291  VAL A CG2   
2227 N N     . GLU A 292 ? 0.24644 0.23780 0.20012 0.00734  -0.03908 0.04025  292  GLU A N     
2228 C CA    . GLU A 292 ? 0.23648 0.23193 0.19115 0.00732  -0.04508 0.03953  292  GLU A CA    
2229 C C     . GLU A 292 ? 0.25328 0.25287 0.21763 0.00907  -0.04776 0.04193  292  GLU A C     
2230 O O     . GLU A 292 ? 0.25786 0.26227 0.22687 0.00847  -0.05219 0.04080  292  GLU A O     
2231 C CB    . GLU A 292 ? 0.26683 0.26078 0.21043 0.00804  -0.04830 0.04085  292  GLU A CB    
2232 C CG    . GLU A 292 ? 0.27358 0.26480 0.21326 0.01053  -0.04771 0.04599  292  GLU A CG    
2233 C CD    . GLU A 292 ? 0.32926 0.31528 0.26078 0.01010  -0.04254 0.04684  292  GLU A CD    
2234 O OE1   . GLU A 292 ? 0.29699 0.28189 0.22934 0.00827  -0.03832 0.04380  292  GLU A OE1   
2235 O OE2   . GLU A 292 ? 0.39659 0.37989 0.32109 0.01156  -0.04272 0.05077  292  GLU A OE2   
2236 N N     . PHE A 293 ? 0.23917 0.23700 0.20686 0.01122  -0.04518 0.04515  293  PHE A N     
2237 C CA    . PHE A 293 ? 0.23189 0.23354 0.20923 0.01348  -0.04700 0.04739  293  PHE A CA    
2238 C C     . PHE A 293 ? 0.22950 0.23394 0.21713 0.01265  -0.04407 0.04514  293  PHE A C     
2239 O O     . PHE A 293 ? 0.21248 0.22148 0.20915 0.01429  -0.04553 0.04628  293  PHE A O     
2240 C CB    . PHE A 293 ? 0.24486 0.24248 0.22079 0.01656  -0.04557 0.05186  293  PHE A CB    
2241 C CG    . PHE A 293 ? 0.25604 0.25108 0.22196 0.01773  -0.04852 0.05500  293  PHE A CG    
2242 C CD1   . PHE A 293 ? 0.30274 0.30208 0.26767 0.01872  -0.05480 0.05615  293  PHE A CD1   
2243 C CD2   . PHE A 293 ? 0.26575 0.25433 0.22316 0.01769  -0.04504 0.05691  293  PHE A CD2   
2244 C CE1   . PHE A 293 ? 0.32737 0.32440 0.28224 0.01989  -0.05762 0.05915  293  PHE A CE1   
2245 C CE2   . PHE A 293 ? 0.28635 0.27262 0.23395 0.01873  -0.04747 0.06014  293  PHE A CE2   
2246 C CZ    . PHE A 293 ? 0.31500 0.30539 0.26094 0.01996  -0.05380 0.06125  293  PHE A CZ    
2247 N N     . ALA A 294 ? 0.20328 0.20549 0.18971 0.01031  -0.03998 0.04211  294  ALA A N     
2248 C CA    . ALA A 294 ? 0.21420 0.21843 0.20912 0.00961  -0.03671 0.04025  294  ALA A CA    
2249 C C     . ALA A 294 ? 0.21665 0.22664 0.21743 0.00765  -0.03940 0.03790  294  ALA A C     
2250 O O     . ALA A 294 ? 0.24632 0.25708 0.24306 0.00587  -0.04277 0.03636  294  ALA A O     
2251 C CB    . ALA A 294 ? 0.19684 0.19660 0.18810 0.00792  -0.03154 0.03817  294  ALA A CB    
2252 N N     . ASP A 295 ? 0.17958 0.19343 0.18986 0.00791  -0.03777 0.03758  295  ASP A N     
2253 C CA    . ASP A 295 ? 0.21470 0.23386 0.23134 0.00561  -0.03934 0.03557  295  ASP A CA    
2254 C C     . ASP A 295 ? 0.19857 0.21565 0.21420 0.00300  -0.03568 0.03257  295  ASP A C     
2255 O O     . ASP A 295 ? 0.18440 0.20375 0.20196 0.00042  -0.03732 0.03065  295  ASP A O     
2256 C CB    . ASP A 295 ? 0.17826 0.20370 0.20603 0.00731  -0.03942 0.03708  295  ASP A CB    
2257 C CG    . ASP A 295 ? 0.22932 0.25770 0.25918 0.01018  -0.04353 0.04018  295  ASP A CG    
2258 O OD1   . ASP A 295 ? 0.26118 0.29289 0.29067 0.00914  -0.04874 0.04030  295  ASP A OD1   
2259 O OD2   . ASP A 295 ? 0.19341 0.22048 0.22506 0.01354  -0.04176 0.04244  295  ASP A OD2   
2260 N N     . SER A 296 ? 0.17250 0.18517 0.18518 0.00353  -0.03101 0.03222  296  SER A N     
2261 C CA    . SER A 296 ? 0.18634 0.19691 0.19733 0.00136  -0.02769 0.02959  296  SER A CA    
2262 C C     . SER A 296 ? 0.17766 0.18249 0.18172 0.00187  -0.02427 0.02952  296  SER A C     
2263 O O     . SER A 296 ? 0.15114 0.15377 0.15426 0.00390  -0.02315 0.03160  296  SER A O     
2264 C CB    . SER A 296 ? 0.18623 0.20029 0.20533 0.00100  -0.02495 0.02899  296  SER A CB    
2265 O OG    . SER A 296 ? 0.15608 0.17041 0.17895 0.00360  -0.02258 0.03058  296  SER A OG    
2266 N N     . PHE A 297 ? 0.15840 0.16085 0.15795 -0.00003 -0.02268 0.02722  297  PHE A N     
2267 C CA    . PHE A 297 ? 0.15795 0.15586 0.15128 -0.00004 -0.01947 0.02693  297  PHE A CA    
2268 C C     . PHE A 297 ? 0.14212 0.13973 0.13632 -0.00167 -0.01636 0.02444  297  PHE A C     
2269 O O     . PHE A 297 ? 0.16647 0.16576 0.16205 -0.00311 -0.01754 0.02267  297  PHE A O     
2270 C CB    . PHE A 297 ? 0.16972 0.16514 0.15452 -0.00023 -0.02132 0.02691  297  PHE A CB    
2271 C CG    . PHE A 297 ? 0.17482 0.16666 0.15373 -0.00075 -0.01777 0.02622  297  PHE A CG    
2272 C CD1   . PHE A 297 ? 0.18165 0.17081 0.15940 0.00007  -0.01498 0.02820  297  PHE A CD1   
2273 C CD2   . PHE A 297 ? 0.19145 0.18264 0.16648 -0.00209 -0.01718 0.02358  297  PHE A CD2   
2274 C CE1   . PHE A 297 ? 0.19977 0.18635 0.17290 -0.00079 -0.01169 0.02770  297  PHE A CE1   
2275 C CE2   . PHE A 297 ? 0.18615 0.17509 0.15663 -0.00247 -0.01381 0.02301  297  PHE A CE2   
2276 C CZ    . PHE A 297 ? 0.18619 0.17315 0.15589 -0.00201 -0.01106 0.02513  297  PHE A CZ    
2277 N N     . ASN A 298 ? 0.16523 0.16054 0.15858 -0.00153 -0.01259 0.02440  298  ASN A N     
2278 C CA    . ASN A 298 ? 0.15093 0.14651 0.14572 -0.00284 -0.00974 0.02229  298  ASN A CA    
2279 C C     . ASN A 298 ? 0.15214 0.14461 0.14264 -0.00322 -0.00661 0.02195  298  ASN A C     
2280 O O     . ASN A 298 ? 0.15259 0.14265 0.14182 -0.00242 -0.00545 0.02363  298  ASN A O     
2281 C CB    . ASN A 298 ? 0.14485 0.14283 0.14648 -0.00245 -0.00827 0.02231  298  ASN A CB    
2282 C CG    . ASN A 298 ? 0.16994 0.16814 0.17239 -0.00367 -0.00537 0.02037  298  ASN A CG    
2283 O OD1   . ASN A 298 ? 0.16234 0.15972 0.16615 -0.00333 -0.00268 0.02014  298  ASN A OD1   
2284 N ND2   . ASN A 298 ? 0.15293 0.15204 0.15447 -0.00503 -0.00611 0.01890  298  ASN A ND2   
2285 N N     . PHE A 299 ? 0.14373 0.13629 0.13236 -0.00448 -0.00531 0.01991  299  PHE A N     
2286 C CA    . PHE A 299 ? 0.14727 0.13823 0.13364 -0.00516 -0.00211 0.01931  299  PHE A CA    
2287 C C     . PHE A 299 ? 0.14805 0.14076 0.13596 -0.00620 -0.00093 0.01702  299  PHE A C     
2288 O O     . PHE A 299 ? 0.13520 0.12945 0.12458 -0.00640 -0.00264 0.01607  299  PHE A O     
2289 C CB    . PHE A 299 ? 0.15583 0.14479 0.13584 -0.00516 -0.00188 0.02001  299  PHE A CB    
2290 C CG    . PHE A 299 ? 0.15083 0.14052 0.12729 -0.00562 -0.00212 0.01802  299  PHE A CG    
2291 C CD1   . PHE A 299 ? 0.19865 0.18851 0.17279 -0.00519 -0.00520 0.01738  299  PHE A CD1   
2292 C CD2   . PHE A 299 ? 0.15179 0.14195 0.12727 -0.00639 0.00062  0.01669  299  PHE A CD2   
2293 C CE1   . PHE A 299 ? 0.17332 0.16311 0.14393 -0.00529 -0.00537 0.01523  299  PHE A CE1   
2294 C CE2   . PHE A 299 ? 0.16807 0.15891 0.14053 -0.00629 0.00053  0.01479  299  PHE A CE2   
2295 C CZ    . PHE A 299 ? 0.18451 0.17479 0.15433 -0.00563 -0.00238 0.01398  299  PHE A CZ    
2296 N N     . ASN A 300 ? 0.15290 0.14532 0.14065 -0.00694 0.00186  0.01629  300  ASN A N     
2297 C CA    . ASN A 300 ? 0.15955 0.15389 0.14899 -0.00772 0.00295  0.01439  300  ASN A CA    
2298 C C     . ASN A 300 ? 0.14397 0.13857 0.12992 -0.00805 0.00375  0.01324  300  ASN A C     
2299 O O     . ASN A 300 ? 0.16958 0.16391 0.15417 -0.00866 0.00589  0.01334  300  ASN A O     
2300 C CB    . ASN A 300 ? 0.16150 0.15608 0.15372 -0.00831 0.00524  0.01400  300  ASN A CB    
2301 C CG    . ASN A 300 ? 0.17830 0.17337 0.17444 -0.00766 0.00489  0.01449  300  ASN A CG    
2302 O OD1   . ASN A 300 ? 0.18202 0.17840 0.17992 -0.00708 0.00299  0.01502  300  ASN A OD1   
2303 N ND2   . ASN A 300 ? 0.17433 0.16850 0.17203 -0.00782 0.00680  0.01417  300  ASN A ND2   
2304 N N     . PRO A 301 ? 0.14788 0.14302 0.13259 -0.00769 0.00224  0.01209  301  PRO A N     
2305 C CA    . PRO A 301 ? 0.15100 0.14708 0.13378 -0.00763 0.00346  0.01056  301  PRO A CA    
2306 C C     . PRO A 301 ? 0.15221 0.15042 0.13787 -0.00836 0.00550  0.00982  301  PRO A C     
2307 O O     . PRO A 301 ? 0.14895 0.14859 0.13357 -0.00845 0.00712  0.00903  301  PRO A O     
2308 C CB    . PRO A 301 ? 0.16710 0.16268 0.14930 -0.00699 0.00114  0.00936  301  PRO A CB    
2309 C CG    . PRO A 301 ? 0.14341 0.13748 0.12489 -0.00687 -0.00139 0.01039  301  PRO A CG    
2310 C CD    . PRO A 301 ? 0.14741 0.14208 0.13226 -0.00727 -0.00075 0.01210  301  PRO A CD    
2311 N N     . HIS A 302 ? 0.14475 0.14365 0.13396 -0.00884 0.00550  0.01000  302  HIS A N     
2312 C CA    . HIS A 302 ? 0.12764 0.12866 0.11904 -0.00956 0.00704  0.00910  302  HIS A CA    
2313 C C     . HIS A 302 ? 0.19231 0.19308 0.18414 -0.01066 0.00905  0.00932  302  HIS A C     
2314 O O     . HIS A 302 ? 0.18242 0.18495 0.17600 -0.01153 0.01013  0.00836  302  HIS A O     
2315 C CB    . HIS A 302 ? 0.16804 0.17000 0.16225 -0.00956 0.00623  0.00904  302  HIS A CB    
2316 C CG    . HIS A 302 ? 0.16782 0.16903 0.16398 -0.00967 0.00636  0.00993  302  HIS A CG    
2317 N ND1   . HIS A 302 ? 0.18256 0.18425 0.18081 -0.00933 0.00513  0.01061  302  HIS A ND1   
2318 C CD2   . HIS A 302 ? 0.16889 0.16894 0.16555 -0.00997 0.00767  0.01023  302  HIS A CD2   
2319 C CE1   . HIS A 302 ? 0.17867 0.18006 0.17874 -0.00912 0.00577  0.01123  302  HIS A CE1   
2320 N NE2   . HIS A 302 ? 0.17415 0.17410 0.17312 -0.00938 0.00725  0.01093  302  HIS A NE2   
2321 N N1    . LLP A 303 ? 0.21649 0.19757 0.21926 -0.00230 0.00879  0.01929  303  LLP A N1    
2322 C C2    . LLP A 303 ? 0.21633 0.19456 0.21540 -0.00407 0.00964  0.01968  303  LLP A C2    
2323 C "C2'" . LLP A 303 ? 0.21408 0.18849 0.21053 -0.00361 0.00912  0.02241  303  LLP A "C2'" 
2324 C C3    . LLP A 303 ? 0.23456 0.21410 0.23257 -0.00638 0.01105  0.01756  303  LLP A C3    
2325 O O3    . LLP A 303 ? 0.23384 0.21135 0.22887 -0.00826 0.01208  0.01807  303  LLP A O3    
2326 C C4    . LLP A 303 ? 0.19732 0.18051 0.19730 -0.00681 0.01145  0.01518  303  LLP A C4    
2327 C "C4'" . LLP A 303 ? 0.27496 0.25972 0.27393 -0.00890 0.01252  0.01327  303  LLP A "C4'" 
2328 C C5    . LLP A 303 ? 0.23274 0.21838 0.23589 -0.00509 0.01076  0.01497  303  LLP A C5    
2329 C C6    . LLP A 303 ? 0.20993 0.19480 0.21482 -0.00288 0.00952  0.01695  303  LLP A C6    
2330 C "C5'" . LLP A 303 ? 0.23359 0.22280 0.23823 -0.00559 0.01132  0.01300  303  LLP A "C5'" 
2331 O OP4   . LLP A 303 ? 0.24200 0.23478 0.24637 -0.00598 0.00967  0.01342  303  LLP A OP4   
2332 P P     . LLP A 303 ? 0.19827 0.19481 0.20326 -0.00695 0.01001  0.01178  303  LLP A P     
2333 O OP1   . LLP A 303 ? 0.16443 0.16272 0.16822 -0.00750 0.00820  0.01236  303  LLP A OP1   
2334 O OP2   . LLP A 303 ? 0.18078 0.17967 0.18959 -0.00549 0.01018  0.01208  303  LLP A OP2   
2335 O OP3   . LLP A 303 ? 0.27561 0.27142 0.27949 -0.00814 0.01184  0.00979  303  LLP A OP3   
2336 N N     . LLP A 303 ? 0.16636 0.16481 0.15647 -0.01075 0.00946  0.01059  303  LLP A N     
2337 C CA    . LLP A 303 ? 0.14026 0.13811 0.13022 -0.01211 0.01156  0.01087  303  LLP A CA    
2338 C CB    . LLP A 303 ? 0.21239 0.20657 0.20208 -0.01214 0.01176  0.01254  303  LLP A CB    
2339 C CG    . LLP A 303 ? 0.26134 0.25461 0.25398 -0.01178 0.01146  0.01217  303  LLP A CG    
2340 C CD    . LLP A 303 ? 0.26033 0.24966 0.25283 -0.01130 0.01166  0.01389  303  LLP A CD    
2341 C CE    . LLP A 303 ? 0.25211 0.24014 0.24744 -0.01139 0.01257  0.01284  303  LLP A CE    
2342 N NZ    . LLP A 303 ? 0.23848 0.22276 0.23444 -0.01002 0.01238  0.01444  303  LLP A NZ    
2343 C C     . LLP A 303 ? 0.16014 0.15930 0.14767 -0.01245 0.01271  0.01092  303  LLP A C     
2344 O O     . LLP A 303 ? 0.18396 0.18589 0.17282 -0.01347 0.01409  0.00990  303  LLP A O     
2345 N N     . TRP A 304 ? 0.15830 0.15597 0.14226 -0.01155 0.01216  0.01206  304  TRP A N     
2346 C CA    . TRP A 304 ? 0.15803 0.15664 0.13930 -0.01204 0.01402  0.01255  304  TRP A CA    
2347 C C     . TRP A 304 ? 0.16051 0.15947 0.13778 -0.01035 0.01305  0.01211  304  TRP A C     
2348 O O     . TRP A 304 ? 0.17685 0.17539 0.15014 -0.01020 0.01411  0.01310  304  TRP A O     
2349 C CB    . TRP A 304 ? 0.20813 0.20374 0.18825 -0.01326 0.01533  0.01483  304  TRP A CB    
2350 C CG    . TRP A 304 ? 0.17315 0.16945 0.15072 -0.01435 0.01775  0.01608  304  TRP A CG    
2351 C CD1   . TRP A 304 ? 0.19175 0.19176 0.17113 -0.01579 0.02002  0.01525  304  TRP A CD1   
2352 C CD2   . TRP A 304 ? 0.17993 0.17306 0.15362 -0.01461 0.01846  0.01887  304  TRP A CD2   
2353 N NE1   . TRP A 304 ? 0.16889 0.16873 0.14557 -0.01688 0.02229  0.01723  304  TRP A NE1   
2354 C CE2   . TRP A 304 ? 0.15823 0.15353 0.13104 -0.01622 0.02141  0.01960  304  TRP A CE2   
2355 C CE3   . TRP A 304 ? 0.21593 0.20503 0.18674 -0.01349 0.01678  0.02101  304  TRP A CE3   
2356 C CZ2   . TRP A 304 ? 0.21995 0.21313 0.18858 -0.01688 0.02295  0.02255  304  TRP A CZ2   
2357 C CZ3   . TRP A 304 ? 0.21155 0.19837 0.17804 -0.01391 0.01797  0.02391  304  TRP A CZ3   
2358 C CH2   . TRP A 304 ? 0.24426 0.23292 0.20943 -0.01566 0.02114  0.02474  304  TRP A CH2   
2359 N N     . LEU A 305 ? 0.16669 0.16631 0.14478 -0.00911 0.01113  0.01050  305  LEU A N     
2360 C CA    . LEU A 305 ? 0.16013 0.16001 0.13494 -0.00751 0.01028  0.00921  305  LEU A CA    
2361 C C     . LEU A 305 ? 0.17068 0.17283 0.14805 -0.00672 0.01004  0.00717  305  LEU A C     
2362 O O     . LEU A 305 ? 0.14190 0.14305 0.11746 -0.00523 0.00852  0.00585  305  LEU A O     
2363 C CB    . LEU A 305 ? 0.16587 0.16270 0.13804 -0.00660 0.00736  0.00953  305  LEU A CB    
2364 C CG    . LEU A 305 ? 0.17172 0.16761 0.13826 -0.00522 0.00674  0.00855  305  LEU A CG    
2365 C CD1   . LEU A 305 ? 0.21345 0.20969 0.17589 -0.00548 0.00913  0.00995  305  LEU A CD1   
2366 C CD2   . LEU A 305 ? 0.19332 0.18647 0.15786 -0.00466 0.00322  0.00849  305  LEU A CD2   
2367 N N     . LEU A 306 ? 0.14208 0.14695 0.12348 -0.00766 0.01127  0.00690  306  LEU A N     
2368 C CA    . LEU A 306 ? 0.13966 0.14755 0.12341 -0.00681 0.01145  0.00534  306  LEU A CA    
2369 C C     . LEU A 306 ? 0.15508 0.16144 0.13982 -0.00573 0.00899  0.00465  306  LEU A C     
2370 O O     . LEU A 306 ? 0.15871 0.16652 0.14444 -0.00442 0.00873  0.00350  306  LEU A O     
2371 C CB    . LEU A 306 ? 0.13373 0.14375 0.11538 -0.00540 0.01301  0.00430  306  LEU A CB    
2372 C CG    . LEU A 306 ? 0.17687 0.18985 0.15861 -0.00674 0.01601  0.00511  306  LEU A CG    
2373 C CD1   . LEU A 306 ? 0.19016 0.20551 0.16939 -0.00501 0.01779  0.00411  306  LEU A CD1   
2374 C CD2   . LEU A 306 ? 0.18689 0.20360 0.17374 -0.00845 0.01697  0.00510  306  LEU A CD2   
2375 N N     . VAL A 307 ? 0.16291 0.16651 0.14778 -0.00624 0.00721  0.00550  307  VAL A N     
2376 C CA    . VAL A 307 ? 0.15468 0.15703 0.14108 -0.00581 0.00509  0.00531  307  VAL A CA    
2377 C C     . VAL A 307 ? 0.16541 0.16938 0.15532 -0.00698 0.00543  0.00603  307  VAL A C     
2378 O O     . VAL A 307 ? 0.15482 0.15801 0.14559 -0.00793 0.00543  0.00702  307  VAL A O     
2379 C CB    . VAL A 307 ? 0.15363 0.15266 0.13835 -0.00576 0.00286  0.00577  307  VAL A CB    
2380 C CG1   . VAL A 307 ? 0.15837 0.15608 0.14490 -0.00564 0.00079  0.00566  307  VAL A CG1   
2381 C CG2   . VAL A 307 ? 0.16017 0.15751 0.14035 -0.00470 0.00257  0.00485  307  VAL A CG2   
2382 N N     . ASN A 308 ? 0.16213 0.16837 0.15388 -0.00665 0.00564  0.00549  308  ASN A N     
2383 C CA    . ASN A 308 ? 0.16971 0.17794 0.16395 -0.00770 0.00609  0.00585  308  ASN A CA    
2384 C C     . ASN A 308 ? 0.16480 0.17136 0.15996 -0.00835 0.00523  0.00692  308  ASN A C     
2385 O O     . ASN A 308 ? 0.17811 0.18268 0.17309 -0.00795 0.00366  0.00747  308  ASN A O     
2386 C CB    . ASN A 308 ? 0.17008 0.18056 0.16556 -0.00686 0.00561  0.00544  308  ASN A CB    
2387 C CG    . ASN A 308 ? 0.20350 0.21678 0.19911 -0.00594 0.00654  0.00438  308  ASN A CG    
2388 O OD1   . ASN A 308 ? 0.19109 0.20454 0.18554 -0.00601 0.00776  0.00396  308  ASN A OD1   
2389 N ND2   . ASN A 308 ? 0.26969 0.28551 0.26678 -0.00498 0.00601  0.00414  308  ASN A ND2   
2390 N N     . PHE A 309 ? 0.18868 0.19615 0.18505 -0.00940 0.00633  0.00709  309  PHE A N     
2391 C CA    . PHE A 309 ? 0.16406 0.17092 0.16180 -0.00978 0.00607  0.00796  309  PHE A CA    
2392 C C     . PHE A 309 ? 0.19922 0.20679 0.19784 -0.00951 0.00501  0.00858  309  PHE A C     
2393 O O     . PHE A 309 ? 0.23025 0.23949 0.22872 -0.00927 0.00500  0.00822  309  PHE A O     
2394 C CB    . PHE A 309 ? 0.21663 0.22446 0.21517 -0.01064 0.00769  0.00740  309  PHE A CB    
2395 C CG    . PHE A 309 ? 0.24149 0.24897 0.24148 -0.01066 0.00801  0.00801  309  PHE A CG    
2396 C CD1   . PHE A 309 ? 0.26023 0.26948 0.26105 -0.01066 0.00803  0.00827  309  PHE A CD1   
2397 C CD2   . PHE A 309 ? 0.24659 0.25218 0.24710 -0.01051 0.00846  0.00846  309  PHE A CD2   
2398 C CE1   . PHE A 309 ? 0.25534 0.26496 0.25767 -0.01052 0.00876  0.00877  309  PHE A CE1   
2399 C CE2   . PHE A 309 ? 0.27238 0.27816 0.27475 -0.01011 0.00895  0.00892  309  PHE A CE2   
2400 C CZ    . PHE A 309 ? 0.27316 0.28120 0.27653 -0.01013 0.00925  0.00897  309  PHE A CZ    
2401 N N     . ASP A 310 ? 0.18467 0.19115 0.18442 -0.00962 0.00403  0.00974  310  ASP A N     
2402 C CA    . ASP A 310 ? 0.16710 0.17243 0.16765 -0.00975 0.00379  0.01034  310  ASP A CA    
2403 C C     . ASP A 310 ? 0.18493 0.18803 0.18442 -0.00945 0.00184  0.01053  310  ASP A C     
2404 O O     . ASP A 310 ? 0.20496 0.20704 0.20432 -0.00942 0.00034  0.01063  310  ASP A O     
2405 C CB    . ASP A 310 ? 0.19760 0.20434 0.20089 -0.01012 0.00405  0.01148  310  ASP A CB    
2406 C CG    . ASP A 310 ? 0.26913 0.27633 0.27345 -0.01055 0.00303  0.01252  310  ASP A CG    
2407 O OD1   . ASP A 310 ? 0.28552 0.29236 0.28835 -0.01035 0.00267  0.01220  310  ASP A OD1   
2408 O OD2   . ASP A 310 ? 0.22463 0.23263 0.23153 -0.01108 0.00258  0.01384  310  ASP A OD2   
2409 N N     . CYS A 311 ? 0.14743 0.14941 0.14586 -0.00922 0.00178  0.01059  311  CYS A N     
2410 C CA    . CYS A 311 ? 0.14902 0.14902 0.14578 -0.00893 -0.00026 0.01068  311  CYS A CA    
2411 C C     . CYS A 311 ? 0.15850 0.15793 0.15477 -0.00867 -0.00016 0.01149  311  CYS A C     
2412 O O     . CYS A 311 ? 0.16758 0.16623 0.16140 -0.00842 0.00110  0.01125  311  CYS A O     
2413 C CB    . CYS A 311 ? 0.14748 0.14611 0.14078 -0.00830 -0.00048 0.00935  311  CYS A CB    
2414 S SG    . CYS A 311 ? 0.18543 0.18124 0.17553 -0.00787 -0.00314 0.00889  311  CYS A SG    
2415 N N     . SER A 312 ? 0.15074 0.15072 0.14960 -0.00873 -0.00148 0.01265  312  SER A N     
2416 C CA    . SER A 312 ? 0.15500 0.15437 0.15365 -0.00811 -0.00204 0.01376  312  SER A CA    
2417 C C     . SER A 312 ? 0.16047 0.15937 0.15862 -0.00814 -0.00524 0.01416  312  SER A C     
2418 O O     . SER A 312 ? 0.21989 0.22000 0.22097 -0.00888 -0.00682 0.01429  312  SER A O     
2419 C CB    . SER A 312 ? 0.16413 0.16514 0.16688 -0.00775 -0.00086 0.01474  312  SER A CB    
2420 O OG    . SER A 312 ? 0.16398 0.16388 0.16641 -0.00676 -0.00120 0.01594  312  SER A OG    
2421 N N     . ALA A 313 ? 0.16033 0.15747 0.15460 -0.00753 -0.00626 0.01441  313  ALA A N     
2422 C CA    . ALA A 313 ? 0.15143 0.14781 0.14384 -0.00758 -0.00960 0.01434  313  ALA A CA    
2423 C C     . ALA A 313 ? 0.16915 0.16670 0.16360 -0.00695 -0.01133 0.01626  313  ALA A C     
2424 O O     . ALA A 313 ? 0.16527 0.16189 0.15797 -0.00593 -0.01033 0.01749  313  ALA A O     
2425 C CB    . ALA A 313 ? 0.15555 0.14944 0.14134 -0.00711 -0.00968 0.01321  313  ALA A CB    
2426 N N     . MET A 314 ? 0.13350 0.13313 0.13192 -0.00756 -0.01400 0.01668  314  MET A N     
2427 C CA    . MET A 314 ? 0.15918 0.16101 0.16084 -0.00680 -0.01596 0.01857  314  MET A CA    
2428 C C     . MET A 314 ? 0.17988 0.18208 0.18057 -0.00752 -0.02037 0.01830  314  MET A C     
2429 O O     . MET A 314 ? 0.17253 0.17501 0.17475 -0.00917 -0.02192 0.01707  314  MET A O     
2430 C CB    . MET A 314 ? 0.15569 0.16126 0.16484 -0.00685 -0.01475 0.01956  314  MET A CB    
2431 C CG    . MET A 314 ? 0.21245 0.22141 0.22638 -0.00598 -0.01706 0.02142  314  MET A CG    
2432 S SD    . MET A 314 ? 0.33402 0.34724 0.35594 -0.00498 -0.01425 0.02260  314  MET A SD    
2433 C CE    . MET A 314 ? 0.23019 0.24771 0.25745 -0.00364 -0.01777 0.02478  314  MET A CE    
2434 N N     . TRP A 315 ? 0.17608 0.17800 0.17407 -0.00638 -0.02254 0.01949  315  TRP A N     
2435 C CA    . TRP A 315 ? 0.20896 0.21166 0.20585 -0.00696 -0.02723 0.01929  315  TRP A CA    
2436 C C     . TRP A 315 ? 0.21238 0.21927 0.21514 -0.00607 -0.02945 0.02169  315  TRP A C     
2437 O O     . TRP A 315 ? 0.18685 0.19440 0.19145 -0.00420 -0.02753 0.02364  315  TRP A O     
2438 C CB    . TRP A 315 ? 0.18581 0.18505 0.17361 -0.00620 -0.02851 0.01869  315  TRP A CB    
2439 C CG    . TRP A 315 ? 0.18801 0.18370 0.17003 -0.00681 -0.02690 0.01606  315  TRP A CG    
2440 C CD1   . TRP A 315 ? 0.22971 0.22350 0.20830 -0.00788 -0.02937 0.01350  315  TRP A CD1   
2441 C CD2   . TRP A 315 ? 0.18395 0.17761 0.16305 -0.00621 -0.02256 0.01563  315  TRP A CD2   
2442 N NE1   . TRP A 315 ? 0.21182 0.20263 0.18570 -0.00760 -0.02663 0.01154  315  TRP A NE1   
2443 C CE2   . TRP A 315 ? 0.18251 0.17365 0.15686 -0.00667 -0.02249 0.01290  315  TRP A CE2   
2444 C CE3   . TRP A 315 ? 0.20778 0.20151 0.18811 -0.00539 -0.01884 0.01716  315  TRP A CE3   
2445 C CZ2   . TRP A 315 ? 0.18600 0.17562 0.15736 -0.00619 -0.01879 0.01188  315  TRP A CZ2   
2446 C CZ3   . TRP A 315 ? 0.17908 0.17110 0.15630 -0.00538 -0.01538 0.01606  315  TRP A CZ3   
2447 C CH2   . TRP A 315 ? 0.18818 0.17861 0.16121 -0.00571 -0.01536 0.01356  315  TRP A CH2   
2448 N N     . VAL A 316 ? 0.20724 0.21696 0.21321 -0.00741 -0.03363 0.02147  316  VAL A N     
2449 C CA    . VAL A 316 ? 0.22532 0.23997 0.23723 -0.00658 -0.03653 0.02368  316  VAL A CA    
2450 C C     . VAL A 316 ? 0.27313 0.28799 0.28153 -0.00736 -0.04207 0.02311  316  VAL A C     
2451 O O     . VAL A 316 ? 0.30883 0.32076 0.31257 -0.00922 -0.04375 0.02058  316  VAL A O     
2452 C CB    . VAL A 316 ? 0.25972 0.27975 0.28188 -0.00782 -0.03600 0.02426  316  VAL A CB    
2453 C CG1   . VAL A 316 ? 0.23517 0.25547 0.26045 -0.00655 -0.03071 0.02494  316  VAL A CG1   
2454 C CG2   . VAL A 316 ? 0.31973 0.33931 0.34284 -0.01110 -0.03746 0.02219  316  VAL A CG2   
2455 N N     . LYS A 317 ? 0.27464 0.29285 0.28514 -0.00575 -0.04510 0.02539  317  LYS A N     
2456 C CA    . LYS A 317 ? 0.33183 0.35090 0.33904 -0.00646 -0.05090 0.02495  317  LYS A CA    
2457 C C     . LYS A 317 ? 0.38429 0.40829 0.39930 -0.00924 -0.05469 0.02412  317  LYS A C     
2458 O O     . LYS A 317 ? 0.39197 0.41510 0.40352 -0.01119 -0.05915 0.02216  317  LYS A O     
2459 C CB    . LYS A 317 ? 0.34871 0.36947 0.35463 -0.00353 -0.05311 0.02799  317  LYS A CB    
2460 C CG    . LYS A 317 ? 0.30647 0.32150 0.30194 -0.00156 -0.05115 0.02865  317  LYS A CG    
2461 C CD    . LYS A 317 ? 0.38810 0.40376 0.37847 0.00005  -0.05587 0.03058  317  LYS A CD    
2462 C CE    . LYS A 317 ? 0.33510 0.34689 0.31935 0.00289  -0.05321 0.03340  317  LYS A CE    
2463 N NZ    . LYS A 317 ? 0.33190 0.34693 0.32094 0.00577  -0.05523 0.03736  317  LYS A NZ    
2464 N N     . LYS A 318 ? 0.37385 0.40303 0.39925 -0.00958 -0.05294 0.02549  318  LYS A N     
2465 C CA    . LYS A 318 ? 0.45048 0.48507 0.48457 -0.01256 -0.05590 0.02517  318  LYS A CA    
2466 C C     . LYS A 318 ? 0.44072 0.47573 0.48026 -0.01417 -0.05133 0.02479  318  LYS A C     
2467 O O     . LYS A 318 ? 0.45182 0.48981 0.49668 -0.01239 -0.04740 0.02659  318  LYS A O     
2468 C CB    . LYS A 318 ? 0.48940 0.53210 0.53220 -0.01123 -0.05884 0.02795  318  LYS A CB    
2469 C CG    . LYS A 318 ? 0.53739 0.58005 0.57493 -0.00886 -0.06310 0.02916  318  LYS A CG    
2470 C CD    . LYS A 318 ? 0.55070 0.59014 0.58058 -0.01122 -0.06820 0.02657  318  LYS A CD    
2471 C CE    . LYS A 318 ? 0.60971 0.65297 0.63877 -0.00987 -0.07424 0.02813  318  LYS A CE    
2472 N NZ    . LYS A 318 ? 0.62181 0.65919 0.63825 -0.00750 -0.07477 0.02821  318  LYS A NZ    
2473 N N     . ARG A 319 ? 0.47014 0.50196 0.50810 -0.01743 -0.05193 0.02246  319  ARG A N     
2474 C CA    . ARG A 319 ? 0.51773 0.54963 0.56023 -0.01912 -0.04792 0.02238  319  ARG A CA    
2475 C C     . ARG A 319 ? 0.53847 0.57864 0.59296 -0.02049 -0.04801 0.02455  319  ARG A C     
2476 O O     . ARG A 319 ? 0.54710 0.58913 0.60613 -0.02062 -0.04363 0.02555  319  ARG A O     
2477 C CB    . ARG A 319 ? 0.49361 0.51970 0.53170 -0.02215 -0.04904 0.01962  319  ARG A CB    
2478 C CG    . ARG A 319 ? 0.52330 0.54192 0.54978 -0.02080 -0.04925 0.01717  319  ARG A CG    
2479 C CD    . ARG A 319 ? 0.55681 0.56959 0.57946 -0.02340 -0.05049 0.01423  319  ARG A CD    
2480 N NE    . ARG A 319 ? 0.58214 0.59670 0.60927 -0.02684 -0.05557 0.01350  319  ARG A NE    
2481 C CZ    . ARG A 319 ? 0.60913 0.62007 0.63068 -0.02803 -0.06026 0.01080  319  ARG A CZ    
2482 N NH1   . ARG A 319 ? 0.60037 0.60599 0.61140 -0.02586 -0.06031 0.00866  319  ARG A NH1   
2483 N NH2   . ARG A 319 ? 0.64976 0.66263 0.67638 -0.03159 -0.06497 0.01015  319  ARG A NH2   
2484 N N     . THR A 320 ? 0.58540 0.63102 0.64511 -0.02151 -0.05293 0.02534  320  THR A N     
2485 C CA    . THR A 320 ? 0.63120 0.68590 0.70322 -0.02273 -0.05302 0.02758  320  THR A CA    
2486 C C     . THR A 320 ? 0.67080 0.72990 0.74734 -0.01889 -0.04845 0.02990  320  THR A C     
2487 O O     . THR A 320 ? 0.68428 0.74921 0.76943 -0.01948 -0.04550 0.03141  320  THR A O     
2488 C CB    . THR A 320 ? 0.63227 0.69253 0.70889 -0.02405 -0.05954 0.02801  320  THR A CB    
2489 O OG1   . THR A 320 ? 0.73914 0.79647 0.80785 -0.02120 -0.06250 0.02758  320  THR A OG1   
2490 C CG2   . THR A 320 ? 0.65909 0.71744 0.73615 -0.02917 -0.06354 0.02598  320  THR A CG2   
2491 N N     . ASP A 321 ? 0.61476 0.67086 0.68535 -0.01493 -0.04768 0.03020  321  ASP A N     
2492 C CA    . ASP A 321 ? 0.63342 0.69225 0.70750 -0.01107 -0.04343 0.03203  321  ASP A CA    
2493 C C     . ASP A 321 ? 0.62181 0.67809 0.69513 -0.01117 -0.03729 0.03142  321  ASP A C     
2494 O O     . ASP A 321 ? 0.58573 0.64563 0.66403 -0.00883 -0.03345 0.03265  321  ASP A O     
2495 C CB    . ASP A 321 ? 0.61261 0.66717 0.67948 -0.00726 -0.04403 0.03249  321  ASP A CB    
2496 C CG    . ASP A 321 ? 0.63989 0.69941 0.71008 -0.00571 -0.04925 0.03425  321  ASP A CG    
2497 O OD1   . ASP A 321 ? 0.63845 0.70604 0.71827 -0.00706 -0.05177 0.03528  321  ASP A OD1   
2498 O OD2   . ASP A 321 ? 0.64480 0.70041 0.70805 -0.00321 -0.05088 0.03481  321  ASP A OD2   
2499 N N     . LEU A 322 ? 0.62695 0.67710 0.69400 -0.01361 -0.03639 0.02947  322  LEU A N     
2500 C CA    . LEU A 322 ? 0.62815 0.67648 0.69478 -0.01416 -0.03122 0.02901  322  LEU A CA    
2501 C C     . LEU A 322 ? 0.66137 0.71435 0.73544 -0.01772 -0.03104 0.02972  322  LEU A C     
2502 O O     . LEU A 322 ? 0.68926 0.74598 0.76817 -0.01749 -0.02693 0.03081  322  LEU A O     
2503 C CB    . LEU A 322 ? 0.65540 0.69507 0.71187 -0.01462 -0.03014 0.02683  322  LEU A CB    
2504 C CG    . LEU A 322 ? 0.58869 0.62329 0.63732 -0.01153 -0.02917 0.02624  322  LEU A CG    
2505 C CD1   . LEU A 322 ? 0.53901 0.56668 0.57949 -0.01221 -0.02717 0.02420  322  LEU A CD1   
2506 C CD2   . LEU A 322 ? 0.53864 0.57566 0.59039 -0.00831 -0.02557 0.02761  322  LEU A CD2   
2507 N N     . LEU A 342 ? 0.78069 0.76859 0.79433 -0.03776 -0.06752 0.00016  342  LEU A N     
2508 C CA    . LEU A 342 ? 0.76199 0.74523 0.77524 -0.03720 -0.06291 0.00040  342  LEU A CA    
2509 C C     . LEU A 342 ? 0.77015 0.75963 0.79116 -0.03674 -0.05823 0.00469  342  LEU A C     
2510 O O     . LEU A 342 ? 0.75864 0.75431 0.78885 -0.03928 -0.05908 0.00731  342  LEU A O     
2511 C CB    . LEU A 342 ? 0.77690 0.75377 0.79180 -0.04092 -0.06535 -0.00151 342  LEU A CB    
2512 C CG    . LEU A 342 ? 0.72423 0.69613 0.73934 -0.04050 -0.06108 -0.00082 342  LEU A CG    
2513 C CD1   . LEU A 342 ? 0.67068 0.63713 0.67610 -0.03615 -0.05811 -0.00319 342  LEU A CD1   
2514 C CD2   . LEU A 342 ? 0.62359 0.58928 0.64140 -0.04460 -0.06401 -0.00210 342  LEU A CD2   
2515 N N     . ILE A 343 ? 0.69910 0.68722 0.71636 -0.03350 -0.05328 0.00527  343  ILE A N     
2516 C CA    . ILE A 343 ? 0.71526 0.70815 0.73837 -0.03283 -0.04858 0.00874  343  ILE A CA    
2517 C C     . ILE A 343 ? 0.74593 0.73478 0.77121 -0.03471 -0.04680 0.00918  343  ILE A C     
2518 O O     . ILE A 343 ? 0.71561 0.69774 0.73486 -0.03338 -0.04563 0.00719  343  ILE A O     
2519 C CB    . ILE A 343 ? 0.66545 0.65905 0.68359 -0.02868 -0.04443 0.00914  343  ILE A CB    
2520 C CG1   . ILE A 343 ? 0.64342 0.64071 0.65953 -0.02682 -0.04611 0.00935  343  ILE A CG1   
2521 C CG2   . ILE A 343 ? 0.65274 0.65034 0.67614 -0.02812 -0.03970 0.01211  343  ILE A CG2   
2522 C CD1   . ILE A 343 ? 0.61778 0.61451 0.62815 -0.02311 -0.04242 0.00951  343  ILE A CD1   
2523 N N     . THR A 344 ? 0.75385 0.74699 0.78784 -0.03768 -0.04650 0.01200  344  THR A N     
2524 C CA    . THR A 344 ? 0.74476 0.73483 0.78133 -0.03954 -0.04441 0.01341  344  THR A CA    
2525 C C     . THR A 344 ? 0.75414 0.74948 0.79447 -0.03831 -0.03927 0.01679  344  THR A C     
2526 O O     . THR A 344 ? 0.67566 0.66750 0.71398 -0.03766 -0.03640 0.01744  344  THR A O     
2527 C CB    . THR A 344 ? 0.72139 0.71144 0.76474 -0.04455 -0.04788 0.01420  344  THR A CB    
2528 O OG1   . THR A 344 ? 0.79054 0.78900 0.84070 -0.04605 -0.04998 0.01560  344  THR A OG1   
2529 C CG2   . THR A 344 ? 0.65674 0.63788 0.69488 -0.04601 -0.05229 0.01038  344  THR A CG2   
2530 N N     . ASP A 345 ? 0.96526 0.96888 1.01078 -0.03774 -0.03813 0.01883  345  ASP A N     
2531 C CA    . ASP A 345 ? 0.96571 0.97460 1.01466 -0.03646 -0.03327 0.02165  345  ASP A CA    
2532 C C     . ASP A 345 ? 0.99865 1.01019 1.04423 -0.03239 -0.03108 0.02115  345  ASP A C     
2533 O O     . ASP A 345 ? 1.02902 1.04140 1.07281 -0.03114 -0.03352 0.01988  345  ASP A O     
2534 C CB    . ASP A 345 ? 0.96494 0.98167 1.02395 -0.03926 -0.03304 0.02475  345  ASP A CB    
2535 C CG    . ASP A 345 ? 0.99429 1.01216 1.05633 -0.04054 -0.02907 0.02756  345  ASP A CG    
2536 O OD1   . ASP A 345 ? 1.06292 1.07753 1.11963 -0.03826 -0.02586 0.02739  345  ASP A OD1   
2537 O OD2   . ASP A 345 ? 1.07560 1.09798 1.14536 -0.04390 -0.02917 0.03008  345  ASP A OD2   
2538 N N     . TYR A 346 ? 0.82054 0.83309 0.86503 -0.03043 -0.02655 0.02224  346  TYR A N     
2539 C CA    . TYR A 346 ? 0.74269 0.75706 0.78417 -0.02685 -0.02398 0.02185  346  TYR A CA    
2540 C C     . TYR A 346 ? 0.76405 0.78499 0.81096 -0.02617 -0.02022 0.02424  346  TYR A C     
2541 O O     . TYR A 346 ? 0.67122 0.69277 0.71558 -0.02351 -0.01708 0.02404  346  TYR A O     
2542 C CB    . TYR A 346 ? 0.63718 0.64576 0.67085 -0.02480 -0.02216 0.02005  346  TYR A CB    
2543 C CG    . TYR A 346 ? 0.57011 0.57405 0.59721 -0.02345 -0.02460 0.01738  346  TYR A CG    
2544 C CD1   . TYR A 346 ? 0.55151 0.55743 0.57835 -0.02264 -0.02686 0.01697  346  TYR A CD1   
2545 C CD2   . TYR A 346 ? 0.45596 0.45379 0.47698 -0.02276 -0.02455 0.01538  346  TYR A CD2   
2546 C CE1   . TYR A 346 ? 0.50865 0.51050 0.52872 -0.02139 -0.02887 0.01470  346  TYR A CE1   
2547 C CE2   . TYR A 346 ? 0.39447 0.38848 0.40921 -0.02138 -0.02633 0.01286  346  TYR A CE2   
2548 C CZ    . TYR A 346 ? 0.46257 0.45858 0.47656 -0.02081 -0.02842 0.01256  346  TYR A CZ    
2549 O OH    . TYR A 346 ? 0.38994 0.38234 0.39699 -0.01943 -0.03000 0.01024  346  TYR A OH    
2550 N N     . GLN A 347 ? 0.87034 0.89627 0.92481 -0.02867 -0.02045 0.02640  347  GLN A N     
2551 C CA    . GLN A 347 ? 0.86866 0.90098 0.92826 -0.02815 -0.01646 0.02866  347  GLN A CA    
2552 C C     . GLN A 347 ? 0.86341 0.90100 0.92570 -0.02531 -0.01561 0.02877  347  GLN A C     
2553 O O     . GLN A 347 ? 0.85985 0.89853 0.92051 -0.02268 -0.01195 0.02870  347  GLN A O     
2554 C CB    . GLN A 347 ? 0.87484 0.91139 0.94210 -0.03186 -0.01683 0.03115  347  GLN A CB    
2555 C CG    . GLN A 347 ? 0.88948 0.92075 0.95458 -0.03460 -0.01687 0.03176  347  GLN A CG    
2556 C CD    . GLN A 347 ? 0.97547 1.01078 1.04853 -0.03873 -0.01735 0.03454  347  GLN A CD    
2557 O OE1   . GLN A 347 ? 0.98317 1.02430 1.06323 -0.04014 -0.01929 0.03529  347  GLN A OE1   
2558 N NE2   . GLN A 347 ? 0.93392 0.96639 1.00619 -0.04078 -0.01568 0.03632  347  GLN A NE2   
2559 N N     . HIS A 348 ? 0.74314 0.78379 0.80951 -0.02574 -0.01915 0.02891  348  HIS A N     
2560 C CA    . HIS A 348 ? 0.73117 0.77705 0.80104 -0.02292 -0.01885 0.02944  348  HIS A CA    
2561 C C     . HIS A 348 ? 0.69760 0.73875 0.76021 -0.01969 -0.01925 0.02767  348  HIS A C     
2562 O O     . HIS A 348 ? 0.69254 0.73665 0.75711 -0.01711 -0.01946 0.02814  348  HIS A O     
2563 C CB    . HIS A 348 ? 0.76006 0.81153 0.83741 -0.02467 -0.02293 0.03053  348  HIS A CB    
2564 C CG    . HIS A 348 ? 0.82079 0.87710 0.90589 -0.02846 -0.02274 0.03246  348  HIS A CG    
2565 N ND1   . HIS A 348 ? 0.82673 0.88932 0.91774 -0.02829 -0.01836 0.03454  348  HIS A ND1   
2566 C CD2   . HIS A 348 ? 0.85151 0.90698 0.93921 -0.03269 -0.02624 0.03266  348  HIS A CD2   
2567 C CE1   . HIS A 348 ? 0.87389 0.93978 0.97107 -0.03236 -0.01902 0.03631  348  HIS A CE1   
2568 N NE2   . HIS A 348 ? 0.89439 0.95580 0.98990 -0.03521 -0.02390 0.03520  348  HIS A NE2   
2569 N N     . TRP A 349 ? 0.66197 0.69596 0.71652 -0.01976 -0.01927 0.02584  349  TRP A N     
2570 C CA    . TRP A 349 ? 0.58864 0.61793 0.63591 -0.01715 -0.01912 0.02429  349  TRP A CA    
2571 C C     . TRP A 349 ? 0.46957 0.49810 0.51446 -0.01486 -0.01452 0.02409  349  TRP A C     
2572 O O     . TRP A 349 ? 0.45677 0.48325 0.49803 -0.01246 -0.01387 0.02350  349  TRP A O     
2573 C CB    . TRP A 349 ? 0.56187 0.58444 0.60199 -0.01827 -0.02114 0.02228  349  TRP A CB    
2574 C CG    . TRP A 349 ? 0.60741 0.62912 0.64786 -0.02031 -0.02603 0.02165  349  TRP A CG    
2575 C CD1   . TRP A 349 ? 0.63518 0.65881 0.68091 -0.02348 -0.02828 0.02228  349  TRP A CD1   
2576 C CD2   . TRP A 349 ? 0.56975 0.58812 0.60454 -0.01953 -0.02935 0.02011  349  TRP A CD2   
2577 N NE1   . TRP A 349 ? 0.62796 0.64955 0.67182 -0.02478 -0.03308 0.02092  349  TRP A NE1   
2578 C CE2   . TRP A 349 ? 0.60079 0.61921 0.63758 -0.02224 -0.03378 0.01954  349  TRP A CE2   
2579 C CE3   . TRP A 349 ? 0.51950 0.53487 0.54757 -0.01696 -0.02895 0.01925  349  TRP A CE3   
2580 C CZ2   . TRP A 349 ? 0.56193 0.57752 0.59365 -0.02222 -0.03792 0.01782  349  TRP A CZ2   
2581 C CZ3   . TRP A 349 ? 0.47117 0.48397 0.49423 -0.01690 -0.03274 0.01796  349  TRP A CZ3   
2582 C CH2   . TRP A 349 ? 0.50530 0.51822 0.52991 -0.01940 -0.03722 0.01710  349  TRP A CH2   
2583 N N     . GLN A 350 ? 0.43991 0.46971 0.48636 -0.01570 -0.01142 0.02457  350  GLN A N     
2584 C CA    . GLN A 350 ? 0.40116 0.42974 0.44446 -0.01394 -0.00740 0.02392  350  GLN A CA    
2585 C C     . GLN A 350 ? 0.41152 0.44581 0.46042 -0.01355 -0.00417 0.02528  350  GLN A C     
2586 O O     . GLN A 350 ? 0.44287 0.48250 0.49853 -0.01451 -0.00485 0.02691  350  GLN A O     
2587 C CB    . GLN A 350 ? 0.41777 0.44169 0.45553 -0.01500 -0.00664 0.02282  350  GLN A CB    
2588 C CG    . GLN A 350 ? 0.50858 0.53196 0.54796 -0.01788 -0.00841 0.02359  350  GLN A CG    
2589 C CD    . GLN A 350 ? 0.48824 0.50684 0.52235 -0.01839 -0.00775 0.02268  350  GLN A CD    
2590 O OE1   . GLN A 350 ? 0.44212 0.45620 0.47097 -0.01761 -0.00893 0.02093  350  GLN A OE1   
2591 N NE2   . GLN A 350 ? 0.45046 0.47038 0.48602 -0.01956 -0.00580 0.02405  350  GLN A NE2   
2592 N N     . ILE A 351 ? 0.33264 0.36609 0.37868 -0.01217 -0.00058 0.02448  351  ILE A N     
2593 C CA    . ILE A 351 ? 0.36069 0.39917 0.41068 -0.01142 0.00300  0.02531  351  ILE A CA    
2594 C C     . ILE A 351 ? 0.35461 0.39389 0.40421 -0.01375 0.00440  0.02629  351  ILE A C     
2595 O O     . ILE A 351 ? 0.35656 0.40126 0.41159 -0.01477 0.00577  0.02813  351  ILE A O     
2596 C CB    . ILE A 351 ? 0.37218 0.40921 0.41915 -0.00857 0.00599  0.02368  351  ILE A CB    
2597 C CG1   . ILE A 351 ? 0.35478 0.39029 0.40212 -0.00631 0.00449  0.02323  351  ILE A CG1   
2598 C CG2   . ILE A 351 ? 0.40328 0.44561 0.45410 -0.00744 0.00975  0.02416  351  ILE A CG2   
2599 C CD1   . ILE A 351 ? 0.34675 0.38740 0.40130 -0.00576 0.00265  0.02498  351  ILE A CD1   
2600 N N     . PRO A 352 ? 0.34948 0.38394 0.39322 -0.01465 0.00415  0.02544  352  PRO A N     
2601 C CA    . PRO A 352 ? 0.30995 0.34477 0.35354 -0.01690 0.00487  0.02694  352  PRO A CA    
2602 C C     . PRO A 352 ? 0.35825 0.39212 0.40466 -0.01967 0.00148  0.02826  352  PRO A C     
2603 O O     . PRO A 352 ? 0.36074 0.39299 0.40784 -0.01982 -0.00173 0.02752  352  PRO A O     
2604 C CB    . PRO A 352 ? 0.30026 0.33017 0.33668 -0.01632 0.00543  0.02541  352  PRO A CB    
2605 C CG    . PRO A 352 ? 0.33006 0.35624 0.36342 -0.01488 0.00369  0.02331  352  PRO A CG    
2606 C CD    . PRO A 352 ? 0.33113 0.36032 0.36826 -0.01331 0.00406  0.02324  352  PRO A CD    
2607 N N     . LEU A 353 ? 0.32718 0.36188 0.37500 -0.02198 0.00218  0.03030  353  LEU A N     
2608 C CA    . LEU A 353 ? 0.34028 0.37248 0.38996 -0.02495 -0.00106 0.03138  353  LEU A CA    
2609 C C     . LEU A 353 ? 0.34544 0.37045 0.38887 -0.02524 -0.00251 0.03040  353  LEU A C     
2610 O O     . LEU A 353 ? 0.36341 0.38405 0.40592 -0.02625 -0.00594 0.02941  353  LEU A O     
2611 C CB    . LEU A 353 ? 0.35793 0.39479 0.41357 -0.02775 0.00022  0.03459  353  LEU A CB    
2612 C CG    . LEU A 353 ? 0.40613 0.45076 0.46998 -0.02818 0.00074  0.03588  353  LEU A CG    
2613 C CD1   . LEU A 353 ? 0.39846 0.44840 0.46744 -0.03071 0.00341  0.03929  353  LEU A CD1   
2614 C CD2   . LEU A 353 ? 0.50653 0.55031 0.57387 -0.02976 -0.00396 0.03529  353  LEU A CD2   
2615 N N     . GLY A 354 ? 0.32798 0.35178 0.36702 -0.02416 -0.00005 0.03049  354  GLY A N     
2616 C CA    . GLY A 354 ? 0.33994 0.35761 0.37360 -0.02394 -0.00133 0.02967  354  GLY A CA    
2617 C C     . GLY A 354 ? 0.29704 0.31158 0.32594 -0.02149 -0.00216 0.02658  354  GLY A C     
2618 O O     . GLY A 354 ? 0.30627 0.32317 0.33494 -0.01977 -0.00094 0.02528  354  GLY A O     
2619 N N     . ARG A 355 ? 0.29448 0.30351 0.31969 -0.02132 -0.00417 0.02548  355  ARG A N     
2620 C CA    . ARG A 355 ? 0.26595 0.27223 0.28676 -0.01919 -0.00484 0.02271  355  ARG A CA    
2621 C C     . ARG A 355 ? 0.31575 0.31696 0.33268 -0.01865 -0.00595 0.02202  355  ARG A C     
2622 O O     . ARG A 355 ? 0.29249 0.29090 0.31027 -0.02008 -0.00719 0.02342  355  ARG A O     
2623 C CB    . ARG A 355 ? 0.29416 0.29972 0.31579 -0.01921 -0.00718 0.02128  355  ARG A CB    
2624 C CG    . ARG A 355 ? 0.32910 0.33207 0.35291 -0.02141 -0.01038 0.02168  355  ARG A CG    
2625 C CD    . ARG A 355 ? 0.34080 0.34677 0.36841 -0.02220 -0.01209 0.02173  355  ARG A CD    
2626 N NE    . ARG A 355 ? 0.36037 0.36670 0.38520 -0.01998 -0.01202 0.01999  355  ARG A NE    
2627 C CZ    . ARG A 355 ? 0.35684 0.35922 0.37706 -0.01901 -0.01387 0.01785  355  ARG A CZ    
2628 N NH1   . ARG A 355 ? 0.31653 0.31408 0.33433 -0.01979 -0.01607 0.01669  355  ARG A NH1   
2629 N NH2   . ARG A 355 ? 0.25907 0.26211 0.27687 -0.01715 -0.01337 0.01688  355  ARG A NH2   
2630 N N     . ARG A 356 ? 0.28031 0.28039 0.29330 -0.01653 -0.00544 0.01994  356  ARG A N     
2631 C CA    . ARG A 356 ? 0.29585 0.29188 0.30539 -0.01531 -0.00631 0.01890  356  ARG A CA    
2632 C C     . ARG A 356 ? 0.25834 0.25026 0.26611 -0.01488 -0.00872 0.01674  356  ARG A C     
2633 O O     . ARG A 356 ? 0.28363 0.27608 0.29218 -0.01543 -0.00976 0.01596  356  ARG A O     
2634 C CB    . ARG A 356 ? 0.33232 0.33022 0.33905 -0.01334 -0.00439 0.01778  356  ARG A CB    
2635 C CG    . ARG A 356 ? 0.35657 0.35819 0.36378 -0.01350 -0.00219 0.01933  356  ARG A CG    
2636 C CD    . ARG A 356 ? 0.26202 0.26473 0.26635 -0.01179 -0.00116 0.01811  356  ARG A CD    
2637 N NE    . ARG A 356 ? 0.26716 0.27162 0.27070 -0.01108 -0.00011 0.01603  356  ARG A NE    
2638 C CZ    . ARG A 356 ? 0.28038 0.28483 0.28188 -0.00980 0.00007  0.01429  356  ARG A CZ    
2639 N NH1   . ARG A 356 ? 0.31058 0.31381 0.31080 -0.00866 -0.00076 0.01414  356  ARG A NH1   
2640 N NH2   . ARG A 356 ? 0.28295 0.28876 0.28402 -0.00962 0.00117  0.01281  356  ARG A NH2   
2641 N N     . PHE A 357 ? 0.25069 0.23857 0.25575 -0.01360 -0.00958 0.01569  357  PHE A N     
2642 C CA    . PHE A 357 ? 0.23395 0.21758 0.23628 -0.01266 -0.01152 0.01316  357  PHE A CA    
2643 C C     . PHE A 357 ? 0.22492 0.21051 0.22429 -0.01064 -0.01013 0.01110  357  PHE A C     
2644 O O     . PHE A 357 ? 0.22817 0.21203 0.22469 -0.00863 -0.00991 0.00939  357  PHE A O     
2645 C CB    . PHE A 357 ? 0.20959 0.18803 0.21052 -0.01174 -0.01270 0.01288  357  PHE A CB    
2646 C CG    . PHE A 357 ? 0.24980 0.22256 0.24853 -0.01148 -0.01525 0.01044  357  PHE A CG    
2647 C CD1   . PHE A 357 ? 0.21410 0.18713 0.21097 -0.01146 -0.01613 0.00831  357  PHE A CD1   
2648 C CD2   . PHE A 357 ? 0.28143 0.24817 0.27956 -0.01113 -0.01684 0.01024  357  PHE A CD2   
2649 C CE1   . PHE A 357 ? 0.22008 0.18781 0.21413 -0.01117 -0.01856 0.00574  357  PHE A CE1   
2650 C CE2   . PHE A 357 ? 0.27665 0.23755 0.27234 -0.01080 -0.01922 0.00751  357  PHE A CE2   
2651 C CZ    . PHE A 357 ? 0.27757 0.23914 0.27102 -0.01085 -0.02008 0.00511  357  PHE A CZ    
2652 N N     . ARG A 358 ? 0.20014 0.18948 0.20051 -0.01118 -0.00907 0.01144  358  ARG A N     
2653 C CA    . ARG A 358 ? 0.20658 0.19791 0.20460 -0.00975 -0.00742 0.01012  358  ARG A CA    
2654 C C     . ARG A 358 ? 0.21636 0.20504 0.21075 -0.00875 -0.00859 0.00799  358  ARG A C     
2655 O O     . ARG A 358 ? 0.21373 0.20348 0.20564 -0.00739 -0.00706 0.00686  358  ARG A O     
2656 C CB    . ARG A 358 ? 0.24126 0.23631 0.24130 -0.01051 -0.00611 0.01118  358  ARG A CB    
2657 C CG    . ARG A 358 ? 0.27075 0.26889 0.27342 -0.01110 -0.00433 0.01280  358  ARG A CG    
2658 C CD    . ARG A 358 ? 0.22787 0.22912 0.23276 -0.01158 -0.00310 0.01357  358  ARG A CD    
2659 N NE    . ARG A 358 ? 0.21349 0.21492 0.22115 -0.01268 -0.00478 0.01455  358  ARG A NE    
2660 C CZ    . ARG A 358 ? 0.24189 0.24641 0.25288 -0.01308 -0.00400 0.01572  358  ARG A CZ    
2661 N NH1   . ARG A 358 ? 0.21403 0.22099 0.22547 -0.01243 -0.00148 0.01581  358  ARG A NH1   
2662 N NH2   . ARG A 358 ? 0.20828 0.21357 0.22240 -0.01411 -0.00586 0.01665  358  ARG A NH2   
2663 N N     . SER A 359 ? 0.17691 0.16227 0.17077 -0.00952 -0.01123 0.00737  359  SER A N     
2664 C CA    . SER A 359 ? 0.18773 0.17043 0.17721 -0.00846 -0.01242 0.00507  359  SER A CA    
2665 C C     . SER A 359 ? 0.17952 0.15989 0.16586 -0.00625 -0.01162 0.00310  359  SER A C     
2666 O O     . SER A 359 ? 0.17489 0.15426 0.15707 -0.00482 -0.01142 0.00112  359  SER A O     
2667 C CB    . SER A 359 ? 0.18153 0.16101 0.17103 -0.00997 -0.01584 0.00449  359  SER A CB    
2668 O OG    . SER A 359 ? 0.20976 0.18623 0.20159 -0.01103 -0.01718 0.00495  359  SER A OG    
2669 N N     . LEU A 360 ? 0.16251 0.14223 0.15070 -0.00575 -0.01111 0.00374  360  LEU A N     
2670 C CA    . LEU A 360 ? 0.19234 0.17065 0.17836 -0.00318 -0.01022 0.00207  360  LEU A CA    
2671 C C     . LEU A 360 ? 0.17864 0.16141 0.16342 -0.00179 -0.00746 0.00153  360  LEU A C     
2672 O O     . LEU A 360 ? 0.17239 0.15468 0.15435 0.00034  -0.00662 -0.00048 360  LEU A O     
2673 C CB    . LEU A 360 ? 0.19543 0.17287 0.18405 -0.00284 -0.01026 0.00351  360  LEU A CB    
2674 C CG    . LEU A 360 ? 0.23720 0.20852 0.22620 -0.00338 -0.01281 0.00352  360  LEU A CG    
2675 C CD1   . LEU A 360 ? 0.23773 0.20897 0.22937 -0.00329 -0.01253 0.00594  360  LEU A CD1   
2676 C CD2   . LEU A 360 ? 0.22622 0.19248 0.21150 -0.00110 -0.01387 0.00034  360  LEU A CD2   
2677 N N     . LYS A 361 ? 0.15243 0.13953 0.13941 -0.00303 -0.00591 0.00324  361  LYS A N     
2678 C CA    . LYS A 361 ? 0.17211 0.16317 0.15835 -0.00231 -0.00339 0.00289  361  LYS A CA    
2679 C C     . LYS A 361 ? 0.18025 0.17066 0.16272 -0.00196 -0.00310 0.00167  361  LYS A C     
2680 O O     . LYS A 361 ? 0.16786 0.15976 0.14828 -0.00051 -0.00135 0.00048  361  LYS A O     
2681 C CB    . LYS A 361 ? 0.17418 0.16893 0.16326 -0.00390 -0.00206 0.00469  361  LYS A CB    
2682 C CG    . LYS A 361 ? 0.21300 0.20961 0.20481 -0.00394 -0.00169 0.00574  361  LYS A CG    
2683 C CD    . LYS A 361 ? 0.17102 0.17103 0.16478 -0.00539 -0.00026 0.00691  361  LYS A CD    
2684 C CE    . LYS A 361 ? 0.18478 0.18390 0.17980 -0.00693 -0.00102 0.00816  361  LYS A CE    
2685 N NZ    . LYS A 361 ? 0.19351 0.19559 0.19034 -0.00791 0.00055  0.00901  361  LYS A NZ    
2686 N N     . MET A 362 ? 0.16655 0.15517 0.14808 -0.00323 -0.00480 0.00212  362  MET A N     
2687 C CA    . MET A 362 ? 0.16781 0.15557 0.14495 -0.00279 -0.00488 0.00117  362  MET A CA    
2688 C C     . MET A 362 ? 0.16350 0.14822 0.13650 -0.00089 -0.00551 -0.00145 362  MET A C     
2689 O O     . MET A 362 ? 0.16788 0.15344 0.13706 0.00041  -0.00388 -0.00257 362  MET A O     
2690 C CB    . MET A 362 ? 0.16821 0.15485 0.14539 -0.00434 -0.00718 0.00221  362  MET A CB    
2691 C CG    . MET A 362 ? 0.15423 0.14348 0.13596 -0.00588 -0.00676 0.00459  362  MET A CG    
2692 S SD    . MET A 362 ? 0.20111 0.18965 0.18431 -0.00736 -0.00992 0.00577  362  MET A SD    
2693 C CE    . MET A 362 ? 0.20690 0.19536 0.18509 -0.00661 -0.00985 0.00586  362  MET A CE    
2694 N N     . TRP A 363 ? 0.16351 0.14450 0.13713 -0.00067 -0.00768 -0.00244 363  TRP A N     
2695 C CA    . TRP A 363 ? 0.17248 0.14959 0.14209 0.00136  -0.00845 -0.00535 363  TRP A CA    
2696 C C     . TRP A 363 ? 0.17344 0.15293 0.14255 0.00397  -0.00552 -0.00644 363  TRP A C     
2697 O O     . TRP A 363 ? 0.18280 0.16201 0.14753 0.00589  -0.00437 -0.00855 363  TRP A O     
2698 C CB    . TRP A 363 ? 0.16845 0.14056 0.13970 0.00081  -0.01132 -0.00586 363  TRP A CB    
2699 C CG    . TRP A 363 ? 0.19815 0.16448 0.16496 0.00230  -0.01317 -0.00916 363  TRP A CG    
2700 C CD1   . TRP A 363 ? 0.21608 0.18054 0.17718 0.00282  -0.01408 -0.01150 363  TRP A CD1   
2701 C CD2   . TRP A 363 ? 0.22621 0.18721 0.19365 0.00337  -0.01460 -0.01053 363  TRP A CD2   
2702 N NE1   . TRP A 363 ? 0.22981 0.18815 0.18775 0.00423  -0.01588 -0.01469 363  TRP A NE1   
2703 C CE2   . TRP A 363 ? 0.23681 0.19264 0.19881 0.00460  -0.01623 -0.01411 363  TRP A CE2   
2704 C CE3   . TRP A 363 ? 0.23011 0.18993 0.20183 0.00352  -0.01467 -0.00899 363  TRP A CE3   
2705 C CZ2   . TRP A 363 ? 0.26277 0.21180 0.22380 0.00599  -0.01790 -0.01643 363  TRP A CZ2   
2706 C CZ3   . TRP A 363 ? 0.25456 0.20773 0.22543 0.00491  -0.01634 -0.01080 363  TRP A CZ3   
2707 C CH2   . TRP A 363 ? 0.26491 0.21253 0.23064 0.00614  -0.01792 -0.01460 363  TRP A CH2   
2708 N N     . PHE A 364 ? 0.16291 0.14537 0.13651 0.00410  -0.00422 -0.00496 364  PHE A N     
2709 C CA    . PHE A 364 ? 0.16573 0.15145 0.13993 0.00652  -0.00170 -0.00582 364  PHE A CA    
2710 C C     . PHE A 364 ? 0.17602 0.16653 0.14873 0.00645  0.00119  -0.00568 364  PHE A C     
2711 O O     . PHE A 364 ? 0.17088 0.16306 0.14157 0.00866  0.00316  -0.00735 364  PHE A O     
2712 C CB    . PHE A 364 ? 0.16199 0.15029 0.14125 0.00638  -0.00141 -0.00403 364  PHE A CB    
2713 C CG    . PHE A 364 ? 0.16037 0.14440 0.14073 0.00781  -0.00332 -0.00439 364  PHE A CG    
2714 C CD1   . PHE A 364 ? 0.19202 0.16975 0.17085 0.00701  -0.00603 -0.00493 364  PHE A CD1   
2715 C CD2   . PHE A 364 ? 0.19950 0.18573 0.18257 0.00989  -0.00257 -0.00406 364  PHE A CD2   
2716 C CE1   . PHE A 364 ? 0.19848 0.17146 0.17835 0.00811  -0.00777 -0.00502 364  PHE A CE1   
2717 C CE2   . PHE A 364 ? 0.20405 0.18574 0.18797 0.01139  -0.00439 -0.00401 364  PHE A CE2   
2718 C CZ    . PHE A 364 ? 0.19898 0.17368 0.18122 0.01043  -0.00690 -0.00444 364  PHE A CZ    
2719 N N     . VAL A 365 ? 0.16565 0.15835 0.13947 0.00398  0.00163  -0.00361 365  VAL A N     
2720 C CA    . VAL A 365 ? 0.15244 0.14911 0.12517 0.00347  0.00436  -0.00299 365  VAL A CA    
2721 C C     . VAL A 365 ? 0.19463 0.18943 0.16132 0.00434  0.00464  -0.00428 365  VAL A C     
2722 O O     . VAL A 365 ? 0.18969 0.18725 0.15429 0.00555  0.00731  -0.00500 365  VAL A O     
2723 C CB    . VAL A 365 ? 0.14665 0.14487 0.12187 0.00079  0.00450  -0.00054 365  VAL A CB    
2724 C CG1   . VAL A 365 ? 0.17429 0.17490 0.14755 -0.00001 0.00692  0.00033  365  VAL A CG1   
2725 C CG2   . VAL A 365 ? 0.16426 0.16531 0.14462 0.00011  0.00492  0.00040  365  VAL A CG2   
2726 N N     . PHE A 366 ? 0.16092 0.15144 0.12468 0.00363  0.00189  -0.00450 366  PHE A N     
2727 C CA    . PHE A 366 ? 0.20262 0.19120 0.15980 0.00439  0.00167  -0.00576 366  PHE A CA    
2728 C C     . PHE A 366 ? 0.18407 0.17157 0.13773 0.00733  0.00265  -0.00889 366  PHE A C     
2729 O O     . PHE A 366 ? 0.19110 0.17972 0.13974 0.00853  0.00462  -0.00984 366  PHE A O     
2730 C CB    . PHE A 366 ? 0.17095 0.15531 0.12622 0.00311  -0.00216 -0.00574 366  PHE A CB    
2731 C CG    . PHE A 366 ? 0.20601 0.19167 0.16445 0.00072  -0.00303 -0.00277 366  PHE A CG    
2732 C CD1   . PHE A 366 ? 0.20324 0.19259 0.16394 -0.00014 -0.00036 -0.00055 366  PHE A CD1   
2733 C CD2   . PHE A 366 ? 0.19420 0.17737 0.15361 -0.00065 -0.00653 -0.00231 366  PHE A CD2   
2734 C CE1   . PHE A 366 ? 0.24131 0.23128 0.20481 -0.00191 -0.00108 0.00191  366  PHE A CE1   
2735 C CE2   . PHE A 366 ? 0.18208 0.16683 0.14478 -0.00239 -0.00716 0.00033  366  PHE A CE2   
2736 C CZ    . PHE A 366 ? 0.21071 0.19858 0.17526 -0.00281 -0.00439 0.00235  366  PHE A CZ    
2737 N N     . ARG A 367 ? 0.18260 0.16781 0.13868 0.00869  0.00145  -0.01045 367  ARG A N     
2738 C CA    . ARG A 367 ? 0.19241 0.17569 0.14522 0.01194  0.00214  -0.01374 367  ARG A CA    
2739 C C     . ARG A 367 ? 0.21341 0.20239 0.16844 0.01404  0.00605  -0.01391 367  ARG A C     
2740 O O     . ARG A 367 ? 0.22253 0.21228 0.17362 0.01662  0.00813  -0.01617 367  ARG A O     
2741 C CB    . ARG A 367 ? 0.19468 0.17244 0.14921 0.01274  -0.00082 -0.01522 367  ARG A CB    
2742 C CG    . ARG A 367 ? 0.21022 0.18214 0.16225 0.01081  -0.00482 -0.01578 367  ARG A CG    
2743 C CD    . ARG A 367 ? 0.20840 0.17409 0.16163 0.01160  -0.00751 -0.01751 367  ARG A CD    
2744 N NE    . ARG A 367 ? 0.21339 0.17579 0.16258 0.01522  -0.00678 -0.02129 367  ARG A NE    
2745 C CZ    . ARG A 367 ? 0.27140 0.22744 0.22081 0.01663  -0.00880 -0.02334 367  ARG A CZ    
2746 N NH1   . ARG A 367 ? 0.24509 0.19758 0.19865 0.01446  -0.01157 -0.02166 367  ARG A NH1   
2747 N NH2   . ARG A 367 ? 0.25551 0.20855 0.20088 0.02036  -0.00784 -0.02709 367  ARG A NH2   
2748 N N     . MET A 368 ? 0.21043 0.20383 0.17174 0.01300  0.00712  -0.01167 368  MET A N     
2749 C CA    . MET A 368 ? 0.19789 0.19727 0.16223 0.01489  0.01039  -0.01190 368  MET A CA    
2750 C C     . MET A 368 ? 0.22688 0.23178 0.19025 0.01365  0.01378  -0.01060 368  MET A C     
2751 O O     . MET A 368 ? 0.22680 0.23692 0.19146 0.01537  0.01691  -0.01125 368  MET A O     
2752 C CB    . MET A 368 ? 0.20817 0.21021 0.17943 0.01438  0.00982  -0.01028 368  MET A CB    
2753 C CG    . MET A 368 ? 0.22302 0.22021 0.19538 0.01635  0.00721  -0.01142 368  MET A CG    
2754 S SD    . MET A 368 ? 0.26162 0.26203 0.24107 0.01668  0.00657  -0.00958 368  MET A SD    
2755 C CE    . MET A 368 ? 0.35099 0.35645 0.33217 0.02112  0.00928  -0.01157 368  MET A CE    
2756 N N     . TYR A 369 ? 0.17768 0.18164 0.13918 0.01073  0.01326  -0.00860 369  TYR A N     
2757 C CA    . TYR A 369 ? 0.20691 0.21462 0.16642 0.00942  0.01627  -0.00710 369  TYR A CA    
2758 C C     . TYR A 369 ? 0.20305 0.20802 0.15447 0.01033  0.01656  -0.00818 369  TYR A C     
2759 O O     . TYR A 369 ? 0.21445 0.22302 0.16316 0.01086  0.01995  -0.00799 369  TYR A O     
2760 C CB    . TYR A 369 ? 0.20245 0.21060 0.16462 0.00589  0.01574  -0.00401 369  TYR A CB    
2761 C CG    . TYR A 369 ? 0.19919 0.21226 0.16827 0.00457  0.01712  -0.00274 369  TYR A CG    
2762 C CD1   . TYR A 369 ? 0.23366 0.25233 0.20456 0.00369  0.02060  -0.00179 369  TYR A CD1   
2763 C CD2   . TYR A 369 ? 0.20481 0.21712 0.17847 0.00405  0.01490  -0.00251 369  TYR A CD2   
2764 C CE1   . TYR A 369 ? 0.23915 0.26245 0.21643 0.00220  0.02146  -0.00091 369  TYR A CE1   
2765 C CE2   . TYR A 369 ? 0.19006 0.20692 0.16938 0.00285  0.01585  -0.00160 369  TYR A CE2   
2766 C CZ    . TYR A 369 ? 0.24178 0.26409 0.22298 0.00188  0.01895  -0.00095 369  TYR A CZ    
2767 O OH    . TYR A 369 ? 0.24485 0.27178 0.23176 0.00041  0.01950  -0.00031 369  TYR A OH    
2768 N N     . GLY A 370 ? 0.22288 0.22187 0.17031 0.01041  0.01308  -0.00926 370  GLY A N     
2769 C CA    . GLY A 370 ? 0.21387 0.21019 0.15315 0.01085  0.01270  -0.01006 370  GLY A CA    
2770 C C     . GLY A 370 ? 0.20371 0.20065 0.14163 0.00808  0.01275  -0.00665 370  GLY A C     
2771 O O     . GLY A 370 ? 0.22395 0.22424 0.16691 0.00616  0.01440  -0.00400 370  GLY A O     
2772 N N     . VAL A 371 ? 0.19322 0.18685 0.12424 0.00794  0.01087  -0.00670 371  VAL A N     
2773 C CA    . VAL A 371 ? 0.20652 0.20048 0.13586 0.00576  0.01087  -0.00317 371  VAL A CA    
2774 C C     . VAL A 371 ? 0.23404 0.23267 0.16301 0.00529  0.01564  -0.00106 371  VAL A C     
2775 O O     . VAL A 371 ? 0.21662 0.21665 0.14881 0.00303  0.01667  0.00224  371  VAL A O     
2776 C CB    . VAL A 371 ? 0.23809 0.22815 0.15942 0.00609  0.00784  -0.00369 371  VAL A CB    
2777 C CG1   . VAL A 371 ? 0.24139 0.23181 0.16069 0.00430  0.00791  0.00031  371  VAL A CG1   
2778 C CG2   . VAL A 371 ? 0.25009 0.23592 0.17307 0.00583  0.00290  -0.00546 371  VAL A CG2   
2779 N N     . LYS A 372 ? 0.23814 0.23924 0.16350 0.00737  0.01875  -0.00300 372  LYS A N     
2780 C CA    . LYS A 372 ? 0.23139 0.23757 0.15650 0.00675  0.02360  -0.00090 372  LYS A CA    
2781 C C     . LYS A 372 ? 0.23797 0.24866 0.17245 0.00521  0.02567  0.00038  372  LYS A C     
2782 O O     . LYS A 372 ? 0.24349 0.25724 0.17984 0.00301  0.02847  0.00338  372  LYS A O     
2783 C CB    . LYS A 372 ? 0.24651 0.25492 0.16590 0.00967  0.02664  -0.00359 372  LYS A CB    
2784 C CG    . LYS A 372 ? 0.26817 0.27294 0.17675 0.01077  0.02542  -0.00433 372  LYS A CG    
2785 C CD    . LYS A 372 ? 0.35255 0.35916 0.25510 0.01410  0.02840  -0.00773 372  LYS A CD    
2786 C CE    . LYS A 372 ? 0.46133 0.46339 0.35254 0.01537  0.02618  -0.00937 372  LYS A CE    
2787 N NZ    . LYS A 372 ? 0.55635 0.56186 0.43956 0.01649  0.03076  -0.00874 372  LYS A NZ    
2788 N N     . GLY A 373 ? 0.21171 0.22267 0.15196 0.00621  0.02420  -0.00175 373  GLY A N     
2789 C CA    . GLY A 373 ? 0.23571 0.25090 0.18452 0.00469  0.02550  -0.00063 373  GLY A CA    
2790 C C     . GLY A 373 ? 0.22247 0.23586 0.17462 0.00148  0.02390  0.00228  373  GLY A C     
2791 O O     . GLY A 373 ? 0.20213 0.21889 0.15874 -0.00075 0.02602  0.00425  373  GLY A O     
2792 N N     . LEU A 374 ? 0.20150 0.20964 0.15176 0.00120  0.02015  0.00244  374  LEU A N     
2793 C CA    . LEU A 374 ? 0.19602 0.20230 0.14919 -0.00134 0.01872  0.00505  374  LEU A CA    
2794 C C     . LEU A 374 ? 0.19989 0.20594 0.14967 -0.00299 0.02063  0.00812  374  LEU A C     
2795 O O     . LEU A 374 ? 0.18566 0.19202 0.13916 -0.00528 0.02148  0.01041  374  LEU A O     
2796 C CB    . LEU A 374 ? 0.19761 0.19916 0.14995 -0.00102 0.01440  0.00453  374  LEU A CB    
2797 C CG    . LEU A 374 ? 0.18744 0.18835 0.14357 0.00006  0.01227  0.00219  374  LEU A CG    
2798 C CD1   . LEU A 374 ? 0.21655 0.21313 0.17198 -0.00013 0.00819  0.00205  374  LEU A CD1   
2799 C CD2   . LEU A 374 ? 0.21555 0.21957 0.17879 -0.00112 0.01332  0.00277  374  LEU A CD2   
2800 N N     . GLN A 375 ? 0.18496 0.19008 0.12732 -0.00183 0.02131  0.00823  375  GLN A N     
2801 C CA    . GLN A 375 ? 0.20644 0.21122 0.14486 -0.00329 0.02330  0.01160  375  GLN A CA    
2802 C C     . GLN A 375 ? 0.21615 0.22569 0.15818 -0.00502 0.02780  0.01305  375  GLN A C     
2803 O O     . GLN A 375 ? 0.20770 0.21657 0.15094 -0.00747 0.02910  0.01628  375  GLN A O     
2804 C CB    . GLN A 375 ? 0.23099 0.23431 0.15993 -0.00150 0.02322  0.01125  375  GLN A CB    
2805 C CG    . GLN A 375 ? 0.22018 0.21862 0.14496 -0.00058 0.01845  0.01073  375  GLN A CG    
2806 C CD    . GLN A 375 ? 0.27714 0.27437 0.19209 0.00137  0.01806  0.00948  375  GLN A CD    
2807 O OE1   . GLN A 375 ? 0.24571 0.24529 0.15767 0.00306  0.02057  0.00705  375  GLN A OE1   
2808 N NE2   . GLN A 375 ? 0.24812 0.24187 0.15790 0.00132  0.01484  0.01103  375  GLN A NE2   
2809 N N     . ALA A 376 ? 0.20797 0.22235 0.15212 -0.00378 0.03016  0.01073  376  ALA A N     
2810 C CA    . ALA A 376 ? 0.19310 0.21314 0.14179 -0.00559 0.03431  0.01196  376  ALA A CA    
2811 C C     . ALA A 376 ? 0.19974 0.22026 0.15655 -0.00825 0.03355  0.01282  376  ALA A C     
2812 O O     . ALA A 376 ? 0.19796 0.22058 0.15784 -0.01111 0.03605  0.01511  376  ALA A O     
2813 C CB    . ALA A 376 ? 0.21353 0.23922 0.16355 -0.00318 0.03664  0.00905  376  ALA A CB    
2814 N N     . TYR A 377 ? 0.18828 0.20672 0.14840 -0.00746 0.03013  0.01098  377  TYR A N     
2815 C CA    . TYR A 377 ? 0.18128 0.19969 0.14808 -0.00972 0.02910  0.01148  377  TYR A CA    
2816 C C     . TYR A 377 ? 0.19102 0.20499 0.15686 -0.01213 0.02871  0.01449  377  TYR A C     
2817 O O     . TYR A 377 ? 0.19436 0.20927 0.16427 -0.01490 0.03021  0.01588  377  TYR A O     
2818 C CB    . TYR A 377 ? 0.19341 0.21012 0.16258 -0.00811 0.02560  0.00918  377  TYR A CB    
2819 C CG    . TYR A 377 ? 0.16909 0.18416 0.14310 -0.01000 0.02386  0.00971  377  TYR A CG    
2820 C CD1   . TYR A 377 ? 0.17401 0.19298 0.15402 -0.01161 0.02481  0.00921  377  TYR A CD1   
2821 C CD2   . TYR A 377 ? 0.14852 0.15846 0.12105 -0.01004 0.02119  0.01053  377  TYR A CD2   
2822 C CE1   . TYR A 377 ? 0.18104 0.19830 0.16462 -0.01318 0.02326  0.00932  377  TYR A CE1   
2823 C CE2   . TYR A 377 ? 0.19291 0.20150 0.16955 -0.01142 0.01994  0.01079  377  TYR A CE2   
2824 C CZ    . TYR A 377 ? 0.18630 0.19828 0.16804 -0.01296 0.02103  0.01008  377  TYR A CZ    
2825 O OH    . TYR A 377 ? 0.16517 0.17559 0.15018 -0.01420 0.01984  0.01000  377  TYR A OH    
2826 N N     . ILE A 378 ? 0.17030 0.17928 0.13092 -0.01107 0.02652  0.01547  378  ILE A N     
2827 C CA    . ILE A 378 ? 0.18765 0.19208 0.14717 -0.01272 0.02593  0.01852  378  ILE A CA    
2828 C C     . ILE A 378 ? 0.20935 0.21462 0.16718 -0.01485 0.02953  0.02146  378  ILE A C     
2829 O O     . ILE A 378 ? 0.18839 0.19189 0.14927 -0.01741 0.03045  0.02348  378  ILE A O     
2830 C CB    . ILE A 378 ? 0.20025 0.20024 0.15431 -0.01082 0.02278  0.01909  378  ILE A CB    
2831 C CG1   . ILE A 378 ? 0.20270 0.20168 0.15960 -0.00944 0.01924  0.01666  378  ILE A CG1   
2832 C CG2   . ILE A 378 ? 0.19265 0.18821 0.14500 -0.01200 0.02240  0.02269  378  ILE A CG2   
2833 C CD1   . ILE A 378 ? 0.21439 0.21218 0.17734 -0.01080 0.01832  0.01695  378  ILE A CD1   
2834 N N     . ARG A 379 ? 0.19966 0.20749 0.15250 -0.01387 0.03177  0.02171  379  ARG A N     
2835 C CA    . ARG A 379 ? 0.20309 0.21166 0.15323 -0.01584 0.03538  0.02504  379  ARG A CA    
2836 C C     . ARG A 379 ? 0.20675 0.21980 0.16383 -0.01887 0.03853  0.02535  379  ARG A C     
2837 O O     . ARG A 379 ? 0.22171 0.23351 0.17927 -0.02181 0.04073  0.02859  379  ARG A O     
2838 C CB    . ARG A 379 ? 0.20712 0.21808 0.15000 -0.01374 0.03719  0.02476  379  ARG A CB    
2839 C CG    . ARG A 379 ? 0.22624 0.23226 0.16121 -0.01147 0.03405  0.02520  379  ARG A CG    
2840 C CD    . ARG A 379 ? 0.24240 0.25063 0.16977 -0.00897 0.03531  0.02373  379  ARG A CD    
2841 N NE    . ARG A 379 ? 0.24738 0.25096 0.16641 -0.00742 0.03242  0.02479  379  ARG A NE    
2842 C CZ    . ARG A 379 ? 0.28354 0.28710 0.19558 -0.00472 0.03132  0.02231  379  ARG A CZ    
2843 N NH1   . ARG A 379 ? 0.27262 0.28009 0.18490 -0.00293 0.03306  0.01860  379  ARG A NH1   
2844 N NH2   . ARG A 379 ? 0.28365 0.28309 0.18838 -0.00366 0.02819  0.02343  379  ARG A NH2   
2845 N N     . LYS A 380 ? 0.18315 0.20132 0.14577 -0.01831 0.03859  0.02213  380  LYS A N     
2846 C CA    . LYS A 380 ? 0.19824 0.22127 0.16820 -0.02128 0.04089  0.02210  380  LYS A CA    
2847 C C     . LYS A 380 ? 0.20491 0.22361 0.17911 -0.02414 0.03933  0.02309  380  LYS A C     
2848 O O     . LYS A 380 ? 0.18486 0.20414 0.16227 -0.02772 0.04151  0.02500  380  LYS A O     
2849 C CB    . LYS A 380 ? 0.20723 0.23646 0.18204 -0.01951 0.04053  0.01846  380  LYS A CB    
2850 C CG    . LYS A 380 ? 0.22233 0.25816 0.20492 -0.02233 0.04274  0.01821  380  LYS A CG    
2851 C CD    . LYS A 380 ? 0.26841 0.31064 0.25535 -0.01989 0.04220  0.01488  380  LYS A CD    
2852 C CE    . LYS A 380 ? 0.30212 0.35102 0.29759 -0.02277 0.04335  0.01446  380  LYS A CE    
2853 N NZ    . LYS A 380 ? 0.38637 0.44186 0.38613 -0.02001 0.04270  0.01156  380  LYS A NZ    
2854 N N     . HIS A 381 ? 0.16667 0.18095 0.14099 -0.02268 0.03566  0.02172  381  HIS A N     
2855 C CA    . HIS A 381 ? 0.19607 0.20601 0.17397 -0.02486 0.03426  0.02222  381  HIS A CA    
2856 C C     . HIS A 381 ? 0.20283 0.20687 0.17759 -0.02665 0.03522  0.02602  381  HIS A C     
2857 O O     . HIS A 381 ? 0.18291 0.18484 0.16112 -0.02980 0.03617  0.02715  381  HIS A O     
2858 C CB    . HIS A 381 ? 0.16960 0.17654 0.14787 -0.02257 0.03051  0.02016  381  HIS A CB    
2859 C CG    . HIS A 381 ? 0.18895 0.20015 0.17242 -0.02229 0.02942  0.01695  381  HIS A CG    
2860 N ND1   . HIS A 381 ? 0.20800 0.21716 0.19284 -0.02095 0.02651  0.01524  381  HIS A ND1   
2861 C CD2   . HIS A 381 ? 0.18372 0.20139 0.17137 -0.02313 0.03081  0.01540  381  HIS A CD2   
2862 C CE1   . HIS A 381 ? 0.19671 0.21045 0.18573 -0.02097 0.02611  0.01289  381  HIS A CE1   
2863 N NE2   . HIS A 381 ? 0.16530 0.18430 0.15626 -0.02219 0.02852  0.01289  381  HIS A NE2   
2864 N N     . VAL A 382 ? 0.18202 0.18301 0.15006 -0.02466 0.03479  0.02805  382  VAL A N     
2865 C CA    . VAL A 382 ? 0.22084 0.21599 0.18537 -0.02597 0.03550  0.03216  382  VAL A CA    
2866 C C     . VAL A 382 ? 0.21957 0.21701 0.18462 -0.02933 0.03966  0.03477  382  VAL A C     
2867 O O     . VAL A 382 ? 0.20686 0.19977 0.17291 -0.03212 0.04070  0.03763  382  VAL A O     
2868 C CB    . VAL A 382 ? 0.21803 0.21019 0.17487 -0.02293 0.03375  0.03374  382  VAL A CB    
2869 C CG1   . VAL A 382 ? 0.24634 0.23282 0.19899 -0.02406 0.03459  0.03854  382  VAL A CG1   
2870 C CG2   . VAL A 382 ? 0.21124 0.20112 0.16873 -0.02022 0.02956  0.03149  382  VAL A CG2   
2871 N N     . GLN A 383 ? 0.18248 0.18695 0.14716 -0.02913 0.04221  0.03384  383  GLN A N     
2872 C CA    . GLN A 383 ? 0.22450 0.23279 0.19096 -0.03255 0.04651  0.03612  383  GLN A CA    
2873 C C     . GLN A 383 ? 0.21421 0.22325 0.18900 -0.03649 0.04698  0.03537  383  GLN A C     
2874 O O     . GLN A 383 ? 0.21129 0.21844 0.18757 -0.04033 0.04930  0.03842  383  GLN A O     
2875 C CB    . GLN A 383 ? 0.21545 0.23225 0.18117 -0.03104 0.04907  0.03448  383  GLN A CB    
2876 C CG    . GLN A 383 ? 0.26498 0.28798 0.23445 -0.03458 0.05374  0.03626  383  GLN A CG    
2877 C CD    . GLN A 383 ? 0.32832 0.34749 0.29325 -0.03722 0.05656  0.04155  383  GLN A CD    
2878 O OE1   . GLN A 383 ? 0.38419 0.39786 0.34113 -0.03528 0.05562  0.04385  383  GLN A OE1   
2879 N NE2   . GLN A 383 ? 0.35507 0.37718 0.32515 -0.04178 0.05990  0.04368  383  GLN A NE2   
2880 N N     . LEU A 384 ? 0.18478 0.19637 0.16483 -0.03574 0.04469  0.03137  384  LEU A N     
2881 C CA    . LEU A 384 ? 0.19447 0.20698 0.18198 -0.03938 0.04464  0.03013  384  LEU A CA    
2882 C C     . LEU A 384 ? 0.20848 0.21177 0.19586 -0.04121 0.04320  0.03170  384  LEU A C     
2883 O O     . LEU A 384 ? 0.17983 0.18170 0.17147 -0.04536 0.04433  0.03244  384  LEU A O     
2884 C CB    . LEU A 384 ? 0.19268 0.20977 0.18467 -0.03766 0.04221  0.02565  384  LEU A CB    
2885 C CG    . LEU A 384 ? 0.17816 0.20495 0.17247 -0.03640 0.04383  0.02388  384  LEU A CG    
2886 C CD1   . LEU A 384 ? 0.19222 0.22207 0.18963 -0.03390 0.04088  0.01994  384  LEU A CD1   
2887 C CD2   . LEU A 384 ? 0.22817 0.26114 0.22815 -0.04059 0.04708  0.02493  384  LEU A CD2   
2888 N N     . SER A 385 ? 0.18573 0.18271 0.16856 -0.03813 0.04063  0.03211  385  SER A N     
2889 C CA    . SER A 385 ? 0.19925 0.18727 0.18172 -0.03909 0.03936  0.03375  385  SER A CA    
2890 C C     . SER A 385 ? 0.22189 0.20570 0.20210 -0.04201 0.04208  0.03849  385  SER A C     
2891 O O     . SER A 385 ? 0.22338 0.20195 0.20649 -0.04523 0.04253  0.03953  385  SER A O     
2892 C CB    . SER A 385 ? 0.19641 0.17983 0.17465 -0.03485 0.03625  0.03364  385  SER A CB    
2893 O OG    . SER A 385 ? 0.24104 0.21624 0.21963 -0.03519 0.03498  0.03489  385  SER A OG    
2894 N N     . HIS A 386 ? 0.20937 0.19509 0.18404 -0.04096 0.04394  0.04142  386  HIS A N     
2895 C CA    . HIS A 386 ? 0.21488 0.19711 0.18679 -0.04378 0.04687  0.04647  386  HIS A CA    
2896 C C     . HIS A 386 ? 0.21441 0.20115 0.19223 -0.04887 0.05022  0.04679  386  HIS A C     
2897 O O     . HIS A 386 ? 0.21214 0.19427 0.19029 -0.05258 0.05225  0.05053  386  HIS A O     
2898 C CB    . HIS A 386 ? 0.22660 0.21076 0.19053 -0.04128 0.04816  0.04922  386  HIS A CB    
2899 C CG    . HIS A 386 ? 0.27221 0.25030 0.22986 -0.03730 0.04493  0.05045  386  HIS A CG    
2900 N ND1   . HIS A 386 ? 0.29755 0.26658 0.25424 -0.03738 0.04328  0.05321  386  HIS A ND1   
2901 C CD2   . HIS A 386 ? 0.29327 0.27318 0.24568 -0.03312 0.04285  0.04918  386  HIS A CD2   
2902 C CE1   . HIS A 386 ? 0.31661 0.28289 0.26807 -0.03335 0.04030  0.05376  386  HIS A CE1   
2903 N NE2   . HIS A 386 ? 0.30973 0.28245 0.25846 -0.03094 0.03990  0.05129  386  HIS A NE2   
2904 N N     . GLU A 387 ? 0.19961 0.19532 0.18246 -0.04920 0.05071  0.04308  387  GLU A N     
2905 C CA    . GLU A 387 ? 0.19759 0.19866 0.18730 -0.05413 0.05341  0.04300  387  GLU A CA    
2906 C C     . GLU A 387 ? 0.22074 0.21608 0.21594 -0.05771 0.05180  0.04179  387  GLU A C     
2907 O O     . GLU A 387 ? 0.22990 0.22407 0.22865 -0.06275 0.05398  0.04393  387  GLU A O     
2908 C CB    . GLU A 387 ? 0.22172 0.23405 0.21568 -0.05295 0.05384  0.03922  387  GLU A CB    
2909 C CG    . GLU A 387 ? 0.23415 0.25325 0.22401 -0.05088 0.05694  0.04070  387  GLU A CG    
2910 C CD    . GLU A 387 ? 0.28026 0.31008 0.27460 -0.04913 0.05731  0.03689  387  GLU A CD    
2911 O OE1   . GLU A 387 ? 0.24726 0.28182 0.24959 -0.05174 0.05690  0.03463  387  GLU A OE1   
2912 O OE2   . GLU A 387 ? 0.27569 0.30904 0.26545 -0.04506 0.05788  0.03612  387  GLU A OE2   
2913 N N     . PHE A 388 ? 0.19704 0.18869 0.19293 -0.05529 0.04807  0.03831  388  PHE A N     
2914 C CA    . PHE A 388 ? 0.23231 0.21740 0.23220 -0.05814 0.04647  0.03686  388  PHE A CA    
2915 C C     . PHE A 388 ? 0.23291 0.20692 0.22932 -0.05938 0.04702  0.04107  388  PHE A C     
2916 O O     . PHE A 388 ? 0.23723 0.20647 0.23705 -0.06392 0.04787  0.04197  388  PHE A O     
2917 C CB    . PHE A 388 ? 0.20185 0.18575 0.20238 -0.05476 0.04271  0.03236  388  PHE A CB    
2918 C CG    . PHE A 388 ? 0.21963 0.19691 0.22359 -0.05716 0.04106  0.03019  388  PHE A CG    
2919 C CD1   . PHE A 388 ? 0.19849 0.17998 0.20865 -0.06097 0.04084  0.02705  388  PHE A CD1   
2920 C CD2   . PHE A 388 ? 0.21831 0.18522 0.21925 -0.05549 0.03964  0.03117  388  PHE A CD2   
2921 C CE1   . PHE A 388 ? 0.26284 0.23785 0.27548 -0.06319 0.03922  0.02460  388  PHE A CE1   
2922 C CE2   . PHE A 388 ? 0.23653 0.19689 0.24024 -0.05738 0.03831  0.02880  388  PHE A CE2   
2923 C CZ    . PHE A 388 ? 0.23607 0.20024 0.24531 -0.06132 0.03810  0.02536  388  PHE A CZ    
2924 N N     . GLU A 389 ? 0.22931 0.19890 0.21900 -0.05537 0.04631  0.04369  389  GLU A N     
2925 C CA    . GLU A 389 ? 0.23106 0.19035 0.21690 -0.05589 0.04672  0.04832  389  GLU A CA    
2926 C C     . GLU A 389 ? 0.26919 0.22820 0.25564 -0.06096 0.05054  0.05275  389  GLU A C     
2927 O O     . GLU A 389 ? 0.26549 0.21590 0.25298 -0.06412 0.05108  0.05523  389  GLU A O     
2928 C CB    . GLU A 389 ? 0.25293 0.21011 0.23126 -0.05082 0.04548  0.05078  389  GLU A CB    
2929 C CG    . GLU A 389 ? 0.29230 0.23955 0.26603 -0.05091 0.04586  0.05628  389  GLU A CG    
2930 C CD    . GLU A 389 ? 0.31357 0.26078 0.27940 -0.04657 0.04504  0.05932  389  GLU A CD    
2931 O OE1   . GLU A 389 ? 0.32747 0.28241 0.29132 -0.04399 0.04460  0.05711  389  GLU A OE1   
2932 O OE2   . GLU A 389 ? 0.34494 0.28418 0.30643 -0.04573 0.04467  0.06390  389  GLU A OE2   
2933 N N     . SER A 390 ? 0.24204 0.21033 0.22795 -0.06178 0.05340  0.05385  390  SER A N     
2934 C CA    . SER A 390 ? 0.26641 0.23586 0.25307 -0.06668 0.05755  0.05833  390  SER A CA    
2935 C C     . SER A 390 ? 0.27963 0.24814 0.27452 -0.07272 0.05820  0.05700  390  SER A C     
2936 O O     . SER A 390 ? 0.28839 0.25086 0.28394 -0.07716 0.06023  0.06106  390  SER A O     
2937 C CB    . SER A 390 ? 0.26635 0.24753 0.25191 -0.06606 0.06059  0.05868  390  SER A CB    
2938 O OG    . SER A 390 ? 0.33820 0.32194 0.32540 -0.07110 0.06502  0.06288  390  SER A OG    
2939 N N     . LEU A 391 ? 0.26133 0.23546 0.26239 -0.07308 0.05631  0.05139  391  LEU A N     
2940 C CA    . LEU A 391 ? 0.26116 0.23498 0.27003 -0.07888 0.05637  0.04948  391  LEU A CA    
2941 C C     . LEU A 391 ? 0.30002 0.26024 0.30855 -0.08021 0.05436  0.04968  391  LEU A C     
2942 O O     . LEU A 391 ? 0.25541 0.21075 0.26750 -0.08582 0.05567  0.05143  391  LEU A O     
2943 C CB    . LEU A 391 ? 0.24686 0.22981 0.26147 -0.07829 0.05427  0.04338  391  LEU A CB    
2944 C CG    . LEU A 391 ? 0.22259 0.21940 0.23918 -0.07732 0.05631  0.04276  391  LEU A CG    
2945 C CD1   . LEU A 391 ? 0.24809 0.25215 0.26885 -0.07518 0.05339  0.03691  391  LEU A CD1   
2946 C CD2   . LEU A 391 ? 0.28184 0.28476 0.30375 -0.08331 0.06026  0.04560  391  LEU A CD2   
2947 N N     . VAL A 392 ? 0.25940 0.21330 0.26393 -0.07511 0.05123  0.04787  392  VAL A N     
2948 C CA    . VAL A 392 ? 0.26835 0.20925 0.27241 -0.07547 0.04938  0.04779  392  VAL A CA    
2949 C C     . VAL A 392 ? 0.28524 0.21693 0.28558 -0.07729 0.05154  0.05437  392  VAL A C     
2950 O O     . VAL A 392 ? 0.28417 0.20634 0.28666 -0.08105 0.05169  0.05542  392  VAL A O     
2951 C CB    . VAL A 392 ? 0.29688 0.23435 0.29754 -0.06910 0.04597  0.04488  392  VAL A CB    
2952 C CG1   . VAL A 392 ? 0.28270 0.20648 0.28227 -0.06859 0.04451  0.04547  392  VAL A CG1   
2953 C CG2   . VAL A 392 ? 0.25341 0.19856 0.25792 -0.06794 0.04382  0.03854  392  VAL A CG2   
2954 N N     . ARG A 393 ? 0.27231 0.20638 0.26673 -0.07469 0.05320  0.05893  393  ARG A N     
2955 C CA    . ARG A 393 ? 0.31020 0.23592 0.29996 -0.07591 0.05519  0.06580  393  ARG A CA    
2956 C C     . ARG A 393 ? 0.34159 0.26833 0.33508 -0.08310 0.05900  0.06925  393  ARG A C     
2957 O O     . ARG A 393 ? 0.34879 0.26788 0.33889 -0.08502 0.06093  0.07535  393  ARG A O     
2958 C CB    . ARG A 393 ? 0.30853 0.23764 0.29033 -0.07115 0.05576  0.06938  393  ARG A CB    
2959 C CG    . ARG A 393 ? 0.34173 0.26699 0.31924 -0.06443 0.05193  0.06770  393  ARG A CG    
2960 C CD    . ARG A 393 ? 0.38154 0.30904 0.35079 -0.06027 0.05217  0.07159  393  ARG A CD    
2961 N NE    . ARG A 393 ? 0.38372 0.30683 0.34946 -0.05435 0.04831  0.07059  393  ARG A NE    
2962 C CZ    . ARG A 393 ? 0.41627 0.32854 0.37973 -0.05254 0.04661  0.07361  393  ARG A CZ    
2963 N NH1   . ARG A 393 ? 0.46959 0.37303 0.43332 -0.05612 0.04833  0.07796  393  ARG A NH1   
2964 N NH2   . ARG A 393 ? 0.43928 0.34954 0.40046 -0.04701 0.04310  0.07234  393  ARG A NH2   
2965 N N     . GLN A 394 ? 0.29454 0.23070 0.29506 -0.08714 0.06007  0.06578  394  GLN A N     
2966 C CA    . GLN A 394 ? 0.33194 0.26996 0.33758 -0.09454 0.06350  0.06858  394  GLN A CA    
2967 C C     . GLN A 394 ? 0.34322 0.27282 0.35504 -0.09966 0.06201  0.06623  394  GLN A C     
2968 O O     . GLN A 394 ? 0.36125 0.29104 0.37802 -0.10652 0.06450  0.06847  394  GLN A O     
2969 C CB    . GLN A 394 ? 0.31523 0.26930 0.32579 -0.09628 0.06564  0.06643  394  GLN A CB    
2970 C CG    . GLN A 394 ? 0.28400 0.24650 0.28861 -0.09220 0.06803  0.06910  394  GLN A CG    
2971 C CD    . GLN A 394 ? 0.30219 0.28037 0.31190 -0.09247 0.06951  0.06579  394  GLN A CD    
2972 O OE1   . GLN A 394 ? 0.30608 0.29011 0.32429 -0.09761 0.07034  0.06390  394  GLN A OE1   
2973 N NE2   . GLN A 394 ? 0.27311 0.25811 0.27783 -0.08685 0.06966  0.06497  394  GLN A NE2   
2974 N N     . ASP A 395 ? 0.30716 0.22939 0.31875 -0.09660 0.05813  0.06173  395  ASP A N     
2975 C CA    . ASP A 395 ? 0.32714 0.24120 0.34400 -0.10081 0.05629  0.05826  395  ASP A CA    
2976 C C     . ASP A 395 ? 0.33745 0.23532 0.34969 -0.09805 0.05460  0.06000  395  ASP A C     
2977 O O     . ASP A 395 ? 0.33871 0.23376 0.34765 -0.09185 0.05178  0.05708  395  ASP A O     
2978 C CB    . ASP A 395 ? 0.32745 0.24847 0.34860 -0.09956 0.05321  0.05038  395  ASP A CB    
2979 C CG    . ASP A 395 ? 0.36292 0.27821 0.39004 -0.10498 0.05154  0.04621  395  ASP A CG    
2980 O OD1   . ASP A 395 ? 0.36712 0.26930 0.39387 -0.10785 0.05175  0.04839  395  ASP A OD1   
2981 O OD2   . ASP A 395 ? 0.39201 0.31571 0.42400 -0.10627 0.04982  0.04062  395  ASP A OD2   
2982 N N     . PRO A 396 ? 0.35322 0.24014 0.36537 -0.10235 0.05625  0.06483  396  PRO A N     
2983 C CA    . PRO A 396 ? 0.35252 0.22355 0.36022 -0.09923 0.05473  0.06704  396  PRO A CA    
2984 C C     . PRO A 396 ? 0.35386 0.21633 0.36428 -0.09841 0.05139  0.06061  396  PRO A C     
2985 O O     . PRO A 396 ? 0.38614 0.23522 0.39353 -0.09552 0.05011  0.06189  396  PRO A O     
2986 C CB    . PRO A 396 ? 0.39655 0.25928 0.40432 -0.10514 0.05776  0.07404  396  PRO A CB    
2987 C CG    . PRO A 396 ? 0.36826 0.24087 0.38426 -0.11201 0.05867  0.07191  396  PRO A CG    
2988 C CD    . PRO A 396 ? 0.37040 0.25889 0.38690 -0.11037 0.05966  0.06871  396  PRO A CD    
2989 N N     . ARG A 397 ? 0.32642 0.19606 0.34224 -0.10068 0.04996  0.05380  397  ARG A N     
2990 C CA    . ARG A 397 ? 0.36168 0.22476 0.37869 -0.09864 0.04669  0.04708  397  ARG A CA    
2991 C C     . ARG A 397 ? 0.33173 0.19765 0.34443 -0.09016 0.04453  0.04454  397  ARG A C     
2992 O O     . ARG A 397 ? 0.35350 0.21229 0.36569 -0.08698 0.04219  0.04015  397  ARG A O     
2993 C CB    . ARG A 397 ? 0.31678 0.18727 0.34032 -0.10371 0.04559  0.04069  397  ARG A CB    
2994 C CG    . ARG A 397 ? 0.37979 0.24635 0.40877 -0.11265 0.04702  0.04197  397  ARG A CG    
2995 C CD    . ARG A 397 ? 0.36965 0.24675 0.40532 -0.11743 0.04572  0.03595  397  ARG A CD    
2996 N NE    . ARG A 397 ? 0.43439 0.32885 0.47153 -0.11635 0.04685  0.03641  397  ARG A NE    
2997 C CZ    . ARG A 397 ? 0.43961 0.34614 0.48212 -0.11885 0.04563  0.03167  397  ARG A CZ    
2998 N NH1   . ARG A 397 ? 0.46047 0.36437 0.50726 -0.12298 0.04310  0.02599  397  ARG A NH1   
2999 N NH2   . ARG A 397 ? 0.43738 0.35886 0.48083 -0.11699 0.04684  0.03255  397  ARG A NH2   
3000 N N     . PHE A 398 ? 0.35559 0.23173 0.36527 -0.08656 0.04537  0.04712  398  PHE A N     
3001 C CA    . PHE A 398 ? 0.31264 0.19330 0.31880 -0.07914 0.04340  0.04492  398  PHE A CA    
3002 C C     . PHE A 398 ? 0.33188 0.20770 0.33188 -0.07431 0.04381  0.05095  398  PHE A C     
3003 O O     . PHE A 398 ? 0.34334 0.21486 0.34128 -0.07669 0.04596  0.05719  398  PHE A O     
3004 C CB    . PHE A 398 ? 0.26517 0.16179 0.27274 -0.07862 0.04357  0.04251  398  PHE A CB    
3005 C CG    . PHE A 398 ? 0.30424 0.20689 0.31733 -0.08176 0.04227  0.03601  398  PHE A CG    
3006 C CD1   . PHE A 398 ? 0.30124 0.20803 0.31963 -0.08875 0.04373  0.03585  398  PHE A CD1   
3007 C CD2   . PHE A 398 ? 0.30247 0.20725 0.31552 -0.07779 0.03958  0.03026  398  PHE A CD2   
3008 C CE1   . PHE A 398 ? 0.32509 0.23794 0.34855 -0.09162 0.04212  0.02992  398  PHE A CE1   
3009 C CE2   . PHE A 398 ? 0.31650 0.22696 0.33394 -0.08057 0.03818  0.02448  398  PHE A CE2   
3010 C CZ    . PHE A 398 ? 0.32564 0.24016 0.34826 -0.08742 0.03925  0.02424  398  PHE A CZ    
3011 N N     . GLU A 399 ? 0.30225 0.17920 0.29934 -0.06758 0.04163  0.04919  399  GLU A N     
3012 C CA    . GLU A 399 ? 0.34967 0.22474 0.34103 -0.06246 0.04138  0.05428  399  GLU A CA    
3013 C C     . GLU A 399 ? 0.30224 0.18790 0.29191 -0.05732 0.03977  0.05167  399  GLU A C     
3014 O O     . GLU A 399 ? 0.34071 0.23091 0.33321 -0.05605 0.03821  0.04580  399  GLU A O     
3015 C CB    . GLU A 399 ? 0.34910 0.21056 0.33865 -0.05882 0.03987  0.05587  399  GLU A CB    
3016 C CG    . GLU A 399 ? 0.36174 0.22033 0.35390 -0.05561 0.03752  0.04941  399  GLU A CG    
3017 C CD    . GLU A 399 ? 0.45564 0.29959 0.44723 -0.05314 0.03663  0.05060  399  GLU A CD    
3018 O OE1   . GLU A 399 ? 0.49966 0.33649 0.48803 -0.05224 0.03718  0.05700  399  GLU A OE1   
3019 O OE2   . GLU A 399 ? 0.47924 0.31874 0.47337 -0.05185 0.03539  0.04518  399  GLU A OE2   
3020 N N     . ILE A 400 ? 0.32163 0.21098 0.30637 -0.05453 0.04013  0.05613  400  ILE A N     
3021 C CA    . ILE A 400 ? 0.31341 0.21053 0.29576 -0.04917 0.03823  0.05443  400  ILE A CA    
3022 C C     . ILE A 400 ? 0.32410 0.21362 0.30410 -0.04362 0.03580  0.05570  400  ILE A C     
3023 O O     . ILE A 400 ? 0.34041 0.22202 0.31709 -0.04275 0.03600  0.06107  400  ILE A O     
3024 C CB    . ILE A 400 ? 0.33174 0.23697 0.30974 -0.04904 0.03969  0.05805  400  ILE A CB    
3025 C CG1   . ILE A 400 ? 0.35250 0.26640 0.33365 -0.05408 0.04227  0.05655  400  ILE A CG1   
3026 C CG2   . ILE A 400 ? 0.29598 0.20773 0.27120 -0.04352 0.03735  0.05637  400  ILE A CG2   
3027 C CD1   . ILE A 400 ? 0.31036 0.23284 0.29587 -0.05367 0.04102  0.05002  400  ILE A CD1   
3028 N N     . CYS A 401 ? 0.31111 0.20322 0.29304 -0.03981 0.03354  0.05098  401  CYS A N     
3029 C CA    . CYS A 401 ? 0.32923 0.21458 0.31050 -0.03462 0.03136  0.05147  401  CYS A CA    
3030 C C     . CYS A 401 ? 0.36575 0.25551 0.34299 -0.02971 0.02953  0.05427  401  CYS A C     
3031 O O     . CYS A 401 ? 0.37822 0.26174 0.35374 -0.02589 0.02803  0.05738  401  CYS A O     
3032 C CB    . CYS A 401 ? 0.37641 0.26206 0.36196 -0.03299 0.03009  0.04505  401  CYS A CB    
3033 S SG    . CYS A 401 ? 0.43630 0.31420 0.42608 -0.03800 0.03142  0.04126  401  CYS A SG    
3034 N N     . VAL A 402 ? 0.30976 0.21000 0.28557 -0.02964 0.02944  0.05312  402  VAL A N     
3035 C CA    . VAL A 402 ? 0.31816 0.22320 0.29016 -0.02538 0.02741  0.05497  402  VAL A CA    
3036 C C     . VAL A 402 ? 0.33501 0.24733 0.30309 -0.02751 0.02889  0.05676  402  VAL A C     
3037 O O     . VAL A 402 ? 0.29008 0.20722 0.26010 -0.03132 0.03100  0.05457  402  VAL A O     
3038 C CB    . VAL A 402 ? 0.36143 0.27211 0.33637 -0.02182 0.02510  0.05014  402  VAL A CB    
3039 C CG1   . VAL A 402 ? 0.36964 0.28504 0.34107 -0.01780 0.02268  0.05199  402  VAL A CG1   
3040 C CG2   . VAL A 402 ? 0.37397 0.27800 0.35289 -0.01965 0.02419  0.04800  402  VAL A CG2   
3041 N N     . GLU A 403 ? 0.32397 0.23720 0.28645 -0.02489 0.02775  0.06072  403  GLU A N     
3042 C CA    . GLU A 403 ? 0.29387 0.21393 0.25164 -0.02618 0.02911  0.06224  403  GLU A CA    
3043 C C     . GLU A 403 ? 0.29233 0.22202 0.25262 -0.02653 0.02913  0.05689  403  GLU A C     
3044 O O     . GLU A 403 ? 0.28082 0.21337 0.24344 -0.02367 0.02668  0.05334  403  GLU A O     
3045 C CB    . GLU A 403 ? 0.34397 0.26400 0.29509 -0.02246 0.02693  0.06618  403  GLU A CB    
3046 C CG    . GLU A 403 ? 0.37792 0.30350 0.32272 -0.02372 0.02869  0.06834  403  GLU A CG    
3047 C CD    . GLU A 403 ? 0.49747 0.42338 0.43509 -0.01997 0.02605  0.07161  403  GLU A CD    
3048 O OE1   . GLU A 403 ? 0.57141 0.49214 0.50894 -0.01682 0.02313  0.07364  403  GLU A OE1   
3049 O OE2   . GLU A 403 ? 0.55170 0.48326 0.48380 -0.02003 0.02680  0.07197  403  GLU A OE2   
3050 N N     . VAL A 404 ? 0.26926 0.20403 0.22934 -0.03001 0.03201  0.05653  404  VAL A N     
3051 C CA    . VAL A 404 ? 0.26113 0.20509 0.22333 -0.03028 0.03226  0.05197  404  VAL A CA    
3052 C C     . VAL A 404 ? 0.28143 0.23049 0.23768 -0.02747 0.03128  0.05275  404  VAL A C     
3053 O O     . VAL A 404 ? 0.28887 0.23821 0.23961 -0.02814 0.03300  0.05649  404  VAL A O     
3054 C CB    . VAL A 404 ? 0.26681 0.21454 0.23216 -0.03503 0.03572  0.05116  404  VAL A CB    
3055 C CG1   . VAL A 404 ? 0.23836 0.19572 0.20579 -0.03472 0.03583  0.04676  404  VAL A CG1   
3056 C CG2   . VAL A 404 ? 0.23040 0.17267 0.20149 -0.03812 0.03626  0.04995  404  VAL A CG2   
3057 N N     . ILE A 405 ? 0.24949 0.20244 0.20662 -0.02446 0.02857  0.04920  405  ILE A N     
3058 C CA    . ILE A 405 ? 0.28573 0.24282 0.23742 -0.02169 0.02701  0.04925  405  ILE A CA    
3059 C C     . ILE A 405 ? 0.24100 0.20569 0.19494 -0.02154 0.02710  0.04451  405  ILE A C     
3060 O O     . ILE A 405 ? 0.25419 0.22356 0.20419 -0.02132 0.02822  0.04425  405  ILE A O     
3061 C CB    . ILE A 405 ? 0.27948 0.23341 0.22967 -0.01789 0.02302  0.05008  405  ILE A CB    
3062 C CG1   . ILE A 405 ? 0.36002 0.30627 0.30777 -0.01757 0.02283  0.05518  405  ILE A CG1   
3063 C CG2   . ILE A 405 ? 0.29794 0.25621 0.24267 -0.01539 0.02097  0.04955  405  ILE A CG2   
3064 C CD1   . ILE A 405 ? 0.40765 0.35106 0.35505 -0.01369 0.01887  0.05624  405  ILE A CD1   
3065 N N     . LEU A 406 ? 0.20333 0.16911 0.16334 -0.02147 0.02597  0.04078  406  LEU A N     
3066 C CA    . LEU A 406 ? 0.21774 0.19013 0.18016 -0.02113 0.02575  0.03653  406  LEU A CA    
3067 C C     . LEU A 406 ? 0.19981 0.17439 0.16809 -0.02418 0.02783  0.03428  406  LEU A C     
3068 O O     . LEU A 406 ? 0.20796 0.18101 0.17704 -0.02720 0.03040  0.03622  406  LEU A O     
3069 C CB    . LEU A 406 ? 0.20228 0.17504 0.16615 -0.01817 0.02222  0.03414  406  LEU A CB    
3070 C CG    . LEU A 406 ? 0.19207 0.16362 0.15048 -0.01535 0.01968  0.03604  406  LEU A CG    
3071 C CD1   . LEU A 406 ? 0.21081 0.18328 0.17167 -0.01292 0.01626  0.03376  406  LEU A CD1   
3072 C CD2   . LEU A 406 ? 0.20701 0.18219 0.15961 -0.01508 0.02065  0.03624  406  LEU A CD2   
3073 N N     . GLY A 407 ? 0.19133 0.16948 0.16373 -0.02361 0.02664  0.03038  407  GLY A N     
3074 C CA    . GLY A 407 ? 0.19534 0.17683 0.17287 -0.02632 0.02822  0.02800  407  GLY A CA    
3075 C C     . GLY A 407 ? 0.21021 0.18730 0.19192 -0.02809 0.02801  0.02720  407  GLY A C     
3076 O O     . GLY A 407 ? 0.25149 0.23139 0.23749 -0.02933 0.02788  0.02410  407  GLY A O     
3077 N N     . LEU A 408 ? 0.20649 0.17647 0.18675 -0.02812 0.02789  0.02990  408  LEU A N     
3078 C CA    . LEU A 408 ? 0.21372 0.17826 0.19741 -0.02945 0.02772  0.02902  408  LEU A CA    
3079 C C     . LEU A 408 ? 0.20340 0.16180 0.18610 -0.03209 0.02965  0.03259  408  LEU A C     
3080 O O     . LEU A 408 ? 0.20555 0.16133 0.18389 -0.03120 0.03003  0.03654  408  LEU A O     
3081 C CB    . LEU A 408 ? 0.21882 0.17963 0.20255 -0.02598 0.02523  0.02837  408  LEU A CB    
3082 C CG    . LEU A 408 ? 0.22457 0.17994 0.21170 -0.02663 0.02507  0.02664  408  LEU A CG    
3083 C CD1   . LEU A 408 ? 0.21729 0.17694 0.20821 -0.02844 0.02522  0.02225  408  LEU A CD1   
3084 C CD2   . LEU A 408 ? 0.20673 0.15854 0.19371 -0.02274 0.02305  0.02686  408  LEU A CD2   
3085 N N     . VAL A 409 ? 0.20711 0.16303 0.19365 -0.03548 0.03073  0.03124  409  VAL A N     
3086 C CA    . VAL A 409 ? 0.21027 0.15914 0.19667 -0.03849 0.03246  0.03437  409  VAL A CA    
3087 C C     . VAL A 409 ? 0.22810 0.16983 0.21750 -0.03887 0.03149  0.03217  409  VAL A C     
3088 O O     . VAL A 409 ? 0.22030 0.16444 0.21347 -0.04042 0.03111  0.02796  409  VAL A O     
3089 C CB    . VAL A 409 ? 0.19724 0.15019 0.18568 -0.04332 0.03521  0.03505  409  VAL A CB    
3090 C CG1   . VAL A 409 ? 0.21688 0.16171 0.20548 -0.04684 0.03694  0.03846  409  VAL A CG1   
3091 C CG2   . VAL A 409 ? 0.21005 0.17020 0.19527 -0.04256 0.03659  0.03701  409  VAL A CG2   
3092 N N     . CYS A 410 ? 0.21181 0.14475 0.19933 -0.03726 0.03102  0.03494  410  CYS A N     
3093 C CA    . CYS A 410 ? 0.23431 0.15910 0.22426 -0.03735 0.03043  0.03310  410  CYS A CA    
3094 C C     . CYS A 410 ? 0.28284 0.20025 0.27343 -0.04173 0.03234  0.03562  410  CYS A C     
3095 O O     . CYS A 410 ? 0.27957 0.19282 0.26705 -0.04195 0.03332  0.04077  410  CYS A O     
3096 C CB    . CYS A 410 ? 0.27594 0.19561 0.26422 -0.03224 0.02856  0.03425  410  CYS A CB    
3097 S SG    . CYS A 410 ? 0.28730 0.21526 0.27568 -0.02765 0.02630  0.03131  410  CYS A SG    
3098 N N     . PHE A 411 ? 0.23341 0.14906 0.22786 -0.04532 0.03275  0.03206  411  PHE A N     
3099 C CA    . PHE A 411 ? 0.25432 0.16374 0.25031 -0.05050 0.03453  0.03384  411  PHE A CA    
3100 C C     . PHE A 411 ? 0.26669 0.16907 0.26574 -0.05190 0.03369  0.02946  411  PHE A C     
3101 O O     . PHE A 411 ? 0.28515 0.18988 0.28531 -0.04952 0.03210  0.02466  411  PHE A O     
3102 C CB    . PHE A 411 ? 0.26764 0.18557 0.26575 -0.05537 0.03640  0.03411  411  PHE A CB    
3103 C CG    . PHE A 411 ? 0.27868 0.20399 0.28096 -0.05716 0.03553  0.02838  411  PHE A CG    
3104 C CD1   . PHE A 411 ? 0.22714 0.16063 0.22903 -0.05351 0.03402  0.02542  411  PHE A CD1   
3105 C CD2   . PHE A 411 ? 0.27135 0.19518 0.27787 -0.06256 0.03599  0.02604  411  PHE A CD2   
3106 C CE1   . PHE A 411 ? 0.24694 0.18706 0.25224 -0.05493 0.03305  0.02054  411  PHE A CE1   
3107 C CE2   . PHE A 411 ? 0.26825 0.19915 0.27830 -0.06408 0.03480  0.02086  411  PHE A CE2   
3108 C CZ    . PHE A 411 ? 0.25530 0.19437 0.26457 -0.06011 0.03335  0.01825  411  PHE A CZ    
3109 N N     . ARG A 412 ? 0.28184 0.17533 0.28201 -0.05592 0.03484  0.03115  412  ARG A N     
3110 C CA    . ARG A 412 ? 0.29140 0.17715 0.29419 -0.05785 0.03410  0.02677  412  ARG A CA    
3111 C C     . ARG A 412 ? 0.32932 0.20777 0.33398 -0.06408 0.03572  0.02912  412  ARG A C     
3112 O O     . ARG A 412 ? 0.30806 0.18467 0.31115 -0.06568 0.03746  0.03504  412  ARG A O     
3113 C CB    . ARG A 412 ? 0.33325 0.20985 0.33427 -0.05244 0.03277  0.02586  412  ARG A CB    
3114 C CG    . ARG A 412 ? 0.37031 0.23620 0.36891 -0.05112 0.03345  0.03170  412  ARG A CG    
3115 C CD    . ARG A 412 ? 0.38561 0.24511 0.38286 -0.04462 0.03199  0.03104  412  ARG A CD    
3116 N NE    . ARG A 412 ? 0.39772 0.25048 0.39706 -0.04445 0.03135  0.02530  412  ARG A NE    
3117 C CZ    . ARG A 412 ? 0.45786 0.29795 0.45796 -0.04655 0.03178  0.02515  412  ARG A CZ    
3118 N NH1   . ARG A 412 ? 0.41614 0.24863 0.41536 -0.04924 0.03291  0.03082  412  ARG A NH1   
3119 N NH2   . ARG A 412 ? 0.45752 0.29205 0.45898 -0.04590 0.03112  0.01920  412  ARG A NH2   
3120 N N     . LEU A 413 ? 0.30217 0.17651 0.31003 -0.06777 0.03509  0.02438  413  LEU A N     
3121 C CA    . LEU A 413 ? 0.33778 0.20268 0.34771 -0.07367 0.03622  0.02600  413  LEU A CA    
3122 C C     . LEU A 413 ? 0.35377 0.20405 0.36088 -0.07077 0.03633  0.02941  413  LEU A C     
3123 O O     . LEU A 413 ? 0.37834 0.22355 0.38381 -0.06535 0.03488  0.02685  413  LEU A O     
3124 C CB    . LEU A 413 ? 0.33836 0.20190 0.35203 -0.07790 0.03494  0.01930  413  LEU A CB    
3125 C CG    . LEU A 413 ? 0.38462 0.26054 0.40249 -0.08314 0.03494  0.01678  413  LEU A CG    
3126 C CD1   . LEU A 413 ? 0.38323 0.25746 0.40371 -0.08598 0.03287  0.00947  413  LEU A CD1   
3127 C CD2   . LEU A 413 ? 0.34609 0.22306 0.36669 -0.08948 0.03731  0.02187  413  LEU A CD2   
3128 N N     . LYS A 414 ? 0.33939 0.18312 0.34602 -0.07417 0.03814  0.03542  414  LYS A N     
3129 C CA    . LYS A 414 ? 0.36648 0.19498 0.37086 -0.07197 0.03811  0.03872  414  LYS A CA    
3130 C C     . LYS A 414 ? 0.39728 0.21480 0.40398 -0.07346 0.03690  0.03302  414  LYS A C     
3131 O O     . LYS A 414 ? 0.43280 0.25050 0.44313 -0.07979 0.03698  0.02954  414  LYS A O     
3132 C CB    . LYS A 414 ? 0.40004 0.22322 0.40345 -0.07616 0.04040  0.04642  414  LYS A CB    
3133 C CG    . LYS A 414 ? 0.42258 0.25436 0.42217 -0.07379 0.04166  0.05254  414  LYS A CG    
3134 C CD    . LYS A 414 ? 0.48033 0.30368 0.47749 -0.07644 0.04375  0.06068  414  LYS A CD    
3135 C CE    . LYS A 414 ? 0.51877 0.35245 0.51246 -0.07630 0.04565  0.06628  414  LYS A CE    
3136 N NZ    . LYS A 414 ? 0.52214 0.35408 0.51653 -0.08326 0.04882  0.07186  414  LYS A NZ    
3137 N N     . GLY A 415 ? 0.44109 0.24948 0.44578 -0.06747 0.03569  0.03177  415  GLY A N     
3138 C CA    . GLY A 415 ? 0.42078 0.21851 0.42693 -0.06778 0.03460  0.02578  415  GLY A CA    
3139 C C     . GLY A 415 ? 0.43083 0.23070 0.43593 -0.06095 0.03303  0.02006  415  GLY A C     
3140 O O     . GLY A 415 ? 0.42263 0.22755 0.42565 -0.05464 0.03269  0.02226  415  GLY A O     
3141 N N     . SER A 416 ? 0.46363 0.26030 0.47013 -0.06238 0.03207  0.01264  416  SER A N     
3142 C CA    . SER A 416 ? 0.42837 0.22461 0.43363 -0.05601 0.03099  0.00705  416  SER A CA    
3143 C C     . SER A 416 ? 0.42621 0.23878 0.43105 -0.05315 0.03041  0.00505  416  SER A C     
3144 O O     . SER A 416 ? 0.36396 0.18783 0.36989 -0.05698 0.03052  0.00588  416  SER A O     
3145 C CB    . SER A 416 ? 0.46335 0.25147 0.46946 -0.05877 0.03020  -0.00058 416  SER A CB    
3146 O OG    . SER A 416 ? 0.44797 0.24607 0.45575 -0.06427 0.02947  -0.00492 416  SER A OG    
3147 N N     . ASN A 417 ? 0.37953 0.19312 0.38302 -0.04622 0.02988  0.00245  417  ASN A N     
3148 C CA    . ASN A 417 ? 0.40566 0.23332 0.40881 -0.04364 0.02926  -0.00044 417  ASN A CA    
3149 C C     . ASN A 417 ? 0.40868 0.24127 0.41264 -0.04814 0.02851  -0.00709 417  ASN A C     
3150 O O     . ASN A 417 ? 0.40657 0.25203 0.41089 -0.04919 0.02803  -0.00803 417  ASN A O     
3151 C CB    . ASN A 417 ? 0.41904 0.24595 0.42108 -0.03570 0.02906  -0.00210 417  ASN A CB    
3152 C CG    . ASN A 417 ? 0.44332 0.27169 0.44483 -0.03078 0.02917  0.00454  417  ASN A CG    
3153 O OD1   . ASN A 417 ? 0.41229 0.24504 0.41344 -0.03293 0.02932  0.00998  417  ASN A OD1   
3154 N ND2   . ASN A 417 ? 0.46707 0.29218 0.46849 -0.02403 0.02905  0.00399  417  ASN A ND2   
3155 N N     . LYS A 418 ? 0.39638 0.21862 0.40052 -0.05077 0.02822  -0.01180 418  LYS A N     
3156 C CA    . LYS A 418 ? 0.42840 0.25473 0.43286 -0.05492 0.02708  -0.01858 418  LYS A CA    
3157 C C     . LYS A 418 ? 0.42327 0.25869 0.43030 -0.06183 0.02674  -0.01677 418  LYS A C     
3158 O O     . LYS A 418 ? 0.44074 0.28757 0.44815 -0.06324 0.02572  -0.01993 418  LYS A O     
3159 C CB    . LYS A 418 ? 0.48311 0.29498 0.48700 -0.05667 0.02670  -0.02383 418  LYS A CB    
3160 C CG    . LYS A 418 ? 0.54403 0.35663 0.54851 -0.06314 0.02515  -0.03046 418  LYS A CG    
3161 C CD    . LYS A 418 ? 0.60303 0.41883 0.61113 -0.07157 0.02476  -0.02787 418  LYS A CD    
3162 C CE    . LYS A 418 ? 0.69699 0.51367 0.70597 -0.07761 0.02279  -0.03468 418  LYS A CE    
3163 N NZ    . LYS A 418 ? 0.68098 0.50541 0.69440 -0.08523 0.02242  -0.03190 418  LYS A NZ    
3164 N N     . VAL A 419 ? 0.40050 0.23117 0.40944 -0.06614 0.02767  -0.01154 419  VAL A N     
3165 C CA    . VAL A 419 ? 0.42927 0.26859 0.44132 -0.07289 0.02771  -0.00982 419  VAL A CA    
3166 C C     . VAL A 419 ? 0.38754 0.24230 0.39951 -0.07052 0.02794  -0.00714 419  VAL A C     
3167 O O     . VAL A 419 ? 0.39574 0.26132 0.41007 -0.07442 0.02744  -0.00817 419  VAL A O     
3168 C CB    . VAL A 419 ? 0.44581 0.27669 0.45973 -0.07772 0.02916  -0.00410 419  VAL A CB    
3169 C CG1   . VAL A 419 ? 0.45696 0.28898 0.46920 -0.07393 0.03079  0.00368  419  VAL A CG1   
3170 C CG2   . VAL A 419 ? 0.48627 0.32380 0.50441 -0.08593 0.02913  -0.00415 419  VAL A CG2   
3171 N N     . ASN A 420 ? 0.36499 0.22105 0.37444 -0.06400 0.02850  -0.00393 420  ASN A N     
3172 C CA    . ASN A 420 ? 0.34317 0.21284 0.35218 -0.06142 0.02854  -0.00175 420  ASN A CA    
3173 C C     . ASN A 420 ? 0.34954 0.22725 0.35770 -0.05858 0.02711  -0.00734 420  ASN A C     
3174 O O     . ASN A 420 ? 0.32297 0.21274 0.33200 -0.05936 0.02663  -0.00764 420  ASN A O     
3175 C CB    . ASN A 420 ? 0.35186 0.21973 0.35857 -0.05606 0.02940  0.00395  420  ASN A CB    
3176 C CG    . ASN A 420 ? 0.37637 0.24182 0.38336 -0.05913 0.03092  0.01062  420  ASN A CG    
3177 O OD1   . ASN A 420 ? 0.35400 0.22851 0.36218 -0.06234 0.03163  0.01282  420  ASN A OD1   
3178 N ND2   . ASN A 420 ? 0.37092 0.22402 0.37674 -0.05809 0.03154  0.01393  420  ASN A ND2   
3179 N N     . GLU A 421 ? 0.37376 0.24492 0.38012 -0.05515 0.02655  -0.01170 421  GLU A N     
3180 C CA    . GLU A 421 ? 0.38334 0.26146 0.38853 -0.05331 0.02534  -0.01734 421  GLU A CA    
3181 C C     . GLU A 421 ? 0.34632 0.22977 0.35328 -0.05938 0.02405  -0.02120 421  GLU A C     
3182 O O     . GLU A 421 ? 0.39881 0.29365 0.40587 -0.05930 0.02308  -0.02275 421  GLU A O     
3183 C CB    . GLU A 421 ? 0.38944 0.25875 0.39230 -0.04912 0.02534  -0.02171 421  GLU A CB    
3184 C CG    . GLU A 421 ? 0.43170 0.29775 0.43343 -0.04232 0.02636  -0.01838 421  GLU A CG    
3185 C CD    . GLU A 421 ? 0.50957 0.36349 0.51000 -0.03892 0.02685  -0.02167 421  GLU A CD    
3186 O OE1   . GLU A 421 ? 0.55524 0.40381 0.55483 -0.04141 0.02636  -0.02739 421  GLU A OE1   
3187 O OE2   . GLU A 421 ? 0.58575 0.43557 0.58602 -0.03360 0.02763  -0.01866 421  GLU A OE2   
3188 N N     . ALA A 422 ? 0.37402 0.24945 0.38268 -0.06481 0.02387  -0.02252 422  ALA A N     
3189 C CA    . ALA A 422 ? 0.39371 0.27434 0.40476 -0.07108 0.02233  -0.02614 422  ALA A CA    
3190 C C     . ALA A 422 ? 0.37902 0.27258 0.39324 -0.07374 0.02250  -0.02232 422  ALA A C     
3191 O O     . ALA A 422 ? 0.38195 0.28551 0.39754 -0.07589 0.02094  -0.02521 422  ALA A O     
3192 C CB    . ALA A 422 ? 0.40317 0.27210 0.41604 -0.07682 0.02219  -0.02755 422  ALA A CB    
3193 N N     . LEU A 423 ? 0.36666 0.26028 0.38186 -0.07339 0.02438  -0.01584 423  LEU A N     
3194 C CA    . LEU A 423 ? 0.36544 0.27114 0.38332 -0.07535 0.02497  -0.01221 423  LEU A CA    
3195 C C     . LEU A 423 ? 0.34109 0.25825 0.35742 -0.07074 0.02414  -0.01312 423  LEU A C     
3196 O O     . LEU A 423 ? 0.33839 0.26661 0.35712 -0.07278 0.02333  -0.01393 423  LEU A O     
3197 C CB    . LEU A 423 ? 0.31866 0.22132 0.33661 -0.07522 0.02732  -0.00518 423  LEU A CB    
3198 C CG    . LEU A 423 ? 0.31640 0.23091 0.33643 -0.07655 0.02850  -0.00105 423  LEU A CG    
3199 C CD1   . LEU A 423 ? 0.29527 0.21758 0.32035 -0.08288 0.02789  -0.00319 423  LEU A CD1   
3200 C CD2   . LEU A 423 ? 0.28836 0.19836 0.30752 -0.07676 0.03092  0.00571  423  LEU A CD2   
3201 N N     . LEU A 424 ? 0.33230 0.24703 0.34499 -0.06450 0.02429  -0.01289 424  LEU A N     
3202 C CA    . LEU A 424 ? 0.34540 0.27011 0.35661 -0.06020 0.02357  -0.01344 424  LEU A CA    
3203 C C     . LEU A 424 ? 0.37114 0.30133 0.38223 -0.06116 0.02155  -0.01918 424  LEU A C     
3204 O O     . LEU A 424 ? 0.35535 0.29642 0.36740 -0.06113 0.02066  -0.01939 424  LEU A O     
3205 C CB    . LEU A 424 ? 0.36598 0.28646 0.37393 -0.05382 0.02411  -0.01216 424  LEU A CB    
3206 C CG    . LEU A 424 ? 0.38663 0.31640 0.39308 -0.04950 0.02335  -0.01289 424  LEU A CG    
3207 C CD1   . LEU A 424 ? 0.37295 0.30976 0.37987 -0.04824 0.02398  -0.00798 424  LEU A CD1   
3208 C CD2   . LEU A 424 ? 0.42772 0.35282 0.43153 -0.04420 0.02343  -0.01450 424  LEU A CD2   
3209 N N     . GLN A 425 ? 0.36666 0.28923 0.37623 -0.06181 0.02075  -0.02392 425  GLN A N     
3210 C CA    . GLN A 425 ? 0.41554 0.34277 0.42418 -0.06297 0.01866  -0.02960 425  GLN A CA    
3211 C C     . GLN A 425 ? 0.39969 0.33491 0.41232 -0.06875 0.01728  -0.03017 425  GLN A C     
3212 O O     . GLN A 425 ? 0.38731 0.33244 0.40003 -0.06861 0.01561  -0.03207 425  GLN A O     
3213 C CB    . GLN A 425 ? 0.44765 0.36405 0.45378 -0.06330 0.01818  -0.03476 425  GLN A CB    
3214 C CG    . GLN A 425 ? 0.54679 0.45419 0.55007 -0.05782 0.01984  -0.03391 425  GLN A CG    
3215 C CD    . GLN A 425 ? 0.66199 0.56069 0.66201 -0.05661 0.01946  -0.03989 425  GLN A CD    
3216 O OE1   . GLN A 425 ? 0.70978 0.60285 0.71007 -0.06110 0.01836  -0.04384 425  GLN A OE1   
3217 N NE2   . GLN A 425 ? 0.69551 0.59299 0.69250 -0.05052 0.02045  -0.04068 425  GLN A NE2   
3218 N N     . ARG A 426 ? 0.36013 0.29140 0.37636 -0.07383 0.01799  -0.02825 426  ARG A N     
3219 C CA    . ARG A 426 ? 0.35542 0.29480 0.37656 -0.07965 0.01692  -0.02840 426  ARG A CA    
3220 C C     . ARG A 426 ? 0.33981 0.29215 0.36296 -0.07798 0.01734  -0.02482 426  ARG A C     
3221 O O     . ARG A 426 ? 0.35116 0.31370 0.37700 -0.08002 0.01559  -0.02653 426  ARG A O     
3222 C CB    . ARG A 426 ? 0.40341 0.33568 0.42818 -0.08521 0.01824  -0.02602 426  ARG A CB    
3223 C CG    . ARG A 426 ? 0.48660 0.42343 0.51659 -0.09252 0.01657  -0.02843 426  ARG A CG    
3224 C CD    . ARG A 426 ? 0.52530 0.45305 0.55390 -0.09555 0.01442  -0.03463 426  ARG A CD    
3225 N NE    . ARG A 426 ? 0.64860 0.57792 0.68282 -0.10352 0.01307  -0.03616 426  ARG A NE    
3226 C CZ    . ARG A 426 ? 0.62764 0.54544 0.66304 -0.10841 0.01296  -0.03772 426  ARG A CZ    
3227 N NH1   . ARG A 426 ? 0.65849 0.56174 0.68965 -0.10582 0.01414  -0.03808 426  ARG A NH1   
3228 N NH2   . ARG A 426 ? 0.70414 0.62508 0.74552 -0.11609 0.01163  -0.03879 426  ARG A NH2   
3229 N N     . ILE A 427 ? 0.31004 0.26209 0.33183 -0.07410 0.01948  -0.01998 427  ILE A N     
3230 C CA    . ILE A 427 ? 0.32015 0.28343 0.34338 -0.07221 0.02002  -0.01674 427  ILE A CA    
3231 C C     . ILE A 427 ? 0.33547 0.30595 0.35638 -0.06815 0.01817  -0.01934 427  ILE A C     
3232 O O     . ILE A 427 ? 0.33395 0.31475 0.35734 -0.06910 0.01684  -0.02014 427  ILE A O     
3233 C CB    . ILE A 427 ? 0.30593 0.26622 0.32748 -0.06909 0.02253  -0.01126 427  ILE A CB    
3234 C CG1   . ILE A 427 ? 0.29374 0.24915 0.31789 -0.07360 0.02455  -0.00774 427  ILE A CG1   
3235 C CG2   . ILE A 427 ? 0.26329 0.23411 0.28493 -0.06592 0.02281  -0.00889 427  ILE A CG2   
3236 C CD1   . ILE A 427 ? 0.31955 0.26808 0.34061 -0.07053 0.02665  -0.00288 427  ILE A CD1   
3237 N N     . ASN A 428 ? 0.33072 0.29604 0.34706 -0.06350 0.01811  -0.02047 428  ASN A N     
3238 C CA    . ASN A 428 ? 0.32372 0.29549 0.33755 -0.05947 0.01676  -0.02212 428  ASN A CA    
3239 C C     . ASN A 428 ? 0.35275 0.32850 0.36648 -0.06165 0.01420  -0.02712 428  ASN A C     
3240 O O     . ASN A 428 ? 0.41717 0.40097 0.43000 -0.05956 0.01279  -0.02788 428  ASN A O     
3241 C CB    . ASN A 428 ? 0.30716 0.27263 0.31667 -0.05432 0.01759  -0.02199 428  ASN A CB    
3242 C CG    . ASN A 428 ? 0.35997 0.32589 0.36913 -0.05089 0.01923  -0.01699 428  ASN A CG    
3243 O OD1   . ASN A 428 ? 0.29258 0.26468 0.30385 -0.05163 0.01966  -0.01400 428  ASN A OD1   
3244 N ND2   . ASN A 428 ? 0.36382 0.32342 0.37033 -0.04703 0.02009  -0.01621 428  ASN A ND2   
3245 N N     . SER A 429 ? 0.33577 0.30589 0.35024 -0.06588 0.01338  -0.03050 429  SER A N     
3246 C CA    . SER A 429 ? 0.39360 0.36793 0.40791 -0.06849 0.01054  -0.03542 429  SER A CA    
3247 C C     . SER A 429 ? 0.39095 0.37598 0.41072 -0.07238 0.00912  -0.03459 429  SER A C     
3248 O O     . SER A 429 ? 0.40614 0.39875 0.42586 -0.07287 0.00648  -0.03734 429  SER A O     
3249 C CB    . SER A 429 ? 0.42559 0.38986 0.43867 -0.07184 0.00988  -0.03982 429  SER A CB    
3250 O OG    . SER A 429 ? 0.52304 0.47884 0.53080 -0.06765 0.01081  -0.04174 429  SER A OG    
3251 N N     . ALA A 430 ? 0.34997 0.33615 0.37449 -0.07503 0.01086  -0.03074 430  ALA A N     
3252 C CA    . ALA A 430 ? 0.34439 0.34180 0.37480 -0.07823 0.01000  -0.02958 430  ALA A CA    
3253 C C     . ALA A 430 ? 0.33042 0.33801 0.36061 -0.07372 0.00971  -0.02751 430  ALA A C     
3254 O O     . ALA A 430 ? 0.32983 0.34781 0.36376 -0.07505 0.00789  -0.02808 430  ALA A O     
3255 C CB    . ALA A 430 ? 0.32790 0.32394 0.36312 -0.08199 0.01253  -0.02571 430  ALA A CB    
3256 N N     . LYS A 431 ? 0.27389 0.27856 0.30005 -0.06843 0.01135  -0.02506 431  LYS A N     
3257 C CA    . LYS A 431 ? 0.30005 0.31235 0.32501 -0.06376 0.01097  -0.02340 431  LYS A CA    
3258 C C     . LYS A 431 ? 0.29856 0.32031 0.32867 -0.06444 0.01172  -0.02032 431  LYS A C     
3259 O O     . LYS A 431 ? 0.31438 0.34450 0.34517 -0.06188 0.01052  -0.01994 431  LYS A O     
3260 C CB    . LYS A 431 ? 0.32596 0.34245 0.34834 -0.06238 0.00796  -0.02702 431  LYS A CB    
3261 C CG    . LYS A 431 ? 0.32065 0.32831 0.33765 -0.06157 0.00752  -0.03046 431  LYS A CG    
3262 C CD    . LYS A 431 ? 0.34888 0.35989 0.36130 -0.05794 0.00575  -0.03235 431  LYS A CD    
3263 C CE    . LYS A 431 ? 0.35870 0.36175 0.36599 -0.05769 0.00542  -0.03648 431  LYS A CE    
3264 N NZ    . LYS A 431 ? 0.40330 0.40367 0.41189 -0.06291 0.00377  -0.04059 431  LYS A NZ    
3265 N N     . LYS A 432 ? 0.26569 0.28605 0.29939 -0.06776 0.01388  -0.01798 432  LYS A N     
3266 C CA    . LYS A 432 ? 0.25115 0.27956 0.28904 -0.06774 0.01556  -0.01458 432  LYS A CA    
3267 C C     . LYS A 432 ? 0.23345 0.25873 0.26785 -0.06337 0.01804  -0.01086 432  LYS A C     
3268 O O     . LYS A 432 ? 0.22349 0.25564 0.25862 -0.06044 0.01857  -0.00905 432  LYS A O     
3269 C CB    . LYS A 432 ? 0.26218 0.29149 0.30569 -0.07369 0.01696  -0.01359 432  LYS A CB    
3270 C CG    . LYS A 432 ? 0.30914 0.34340 0.35732 -0.07854 0.01423  -0.01718 432  LYS A CG    
3271 C CD    . LYS A 432 ? 0.32634 0.36203 0.38086 -0.08478 0.01583  -0.01577 432  LYS A CD    
3272 C CE    . LYS A 432 ? 0.48502 0.53263 0.54669 -0.08838 0.01350  -0.01774 432  LYS A CE    
3273 N NZ    . LYS A 432 ? 0.55537 0.60508 0.61471 -0.08699 0.00929  -0.02218 432  LYS A NZ    
3274 N N     . ILE A 433 ? 0.20085 0.21570 0.23145 -0.06282 0.01941  -0.00983 433  ILE A N     
3275 C CA    . ILE A 433 ? 0.20855 0.21940 0.23496 -0.05840 0.02100  -0.00685 433  ILE A CA    
3276 C C     . ILE A 433 ? 0.22726 0.22969 0.24894 -0.05581 0.02005  -0.00858 433  ILE A C     
3277 O O     . ILE A 433 ? 0.23222 0.23090 0.25358 -0.05769 0.01871  -0.01187 433  ILE A O     
3278 C CB    . ILE A 433 ? 0.21593 0.22299 0.24269 -0.06001 0.02396  -0.00290 433  ILE A CB    
3279 C CG1   . ILE A 433 ? 0.22404 0.22034 0.24978 -0.06281 0.02445  -0.00315 433  ILE A CG1   
3280 C CG2   . ILE A 433 ? 0.19910 0.21472 0.23120 -0.06336 0.02532  -0.00148 433  ILE A CG2   
3281 C CD1   . ILE A 433 ? 0.25581 0.24705 0.28094 -0.06407 0.02724  0.00123  433  ILE A CD1   
3282 N N     . HIS A 434 ? 0.17260 0.17232 0.19065 -0.05142 0.02074  -0.00648 434  HIS A N     
3283 C CA    . HIS A 434 ? 0.21411 0.20705 0.22826 -0.04845 0.02012  -0.00773 434  HIS A CA    
3284 C C     . HIS A 434 ? 0.22229 0.20837 0.23406 -0.04639 0.02178  -0.00438 434  HIS A C     
3285 O O     . HIS A 434 ? 0.18890 0.17772 0.19994 -0.04441 0.02260  -0.00138 434  HIS A O     
3286 C CB    . HIS A 434 ? 0.21240 0.21031 0.22471 -0.04467 0.01855  -0.00897 434  HIS A CB    
3287 C CG    . HIS A 434 ? 0.22683 0.21935 0.23583 -0.04218 0.01796  -0.01088 434  HIS A CG    
3288 N ND1   . HIS A 434 ? 0.28987 0.27809 0.29822 -0.04397 0.01733  -0.01436 434  HIS A ND1   
3289 C CD2   . HIS A 434 ? 0.25272 0.24392 0.25907 -0.03805 0.01799  -0.00995 434  HIS A CD2   
3290 C CE1   . HIS A 434 ? 0.31723 0.30182 0.32251 -0.04075 0.01730  -0.01545 434  HIS A CE1   
3291 N NE2   . HIS A 434 ? 0.25995 0.24657 0.26433 -0.03725 0.01769  -0.01266 434  HIS A NE2   
3292 N N     . LEU A 435 ? 0.24832 0.22543 0.25875 -0.04670 0.02213  -0.00501 435  LEU A N     
3293 C CA    . LEU A 435 ? 0.24885 0.21873 0.25708 -0.04454 0.02333  -0.00191 435  LEU A CA    
3294 C C     . LEU A 435 ? 0.24485 0.20883 0.25088 -0.04143 0.02270  -0.00388 435  LEU A C     
3295 O O     . LEU A 435 ? 0.26440 0.22795 0.27036 -0.04195 0.02176  -0.00781 435  LEU A O     
3296 C CB    . LEU A 435 ? 0.29474 0.25833 0.30410 -0.04819 0.02485  0.00017  435  LEU A CB    
3297 C CG    . LEU A 435 ? 0.30080 0.26941 0.31304 -0.05227 0.02607  0.00210  435  LEU A CG    
3298 C CD1   . LEU A 435 ? 0.32089 0.28154 0.33413 -0.05617 0.02748  0.00380  435  LEU A CD1   
3299 C CD2   . LEU A 435 ? 0.34105 0.31486 0.35195 -0.04992 0.02707  0.00573  435  LEU A CD2   
3300 N N     . VAL A 436 ? 0.23405 0.19384 0.23823 -0.03806 0.02322  -0.00114 436  VAL A N     
3301 C CA    . VAL A 436 ? 0.23219 0.18580 0.23498 -0.03497 0.02305  -0.00246 436  VAL A CA    
3302 C C     . VAL A 436 ? 0.28593 0.23076 0.28816 -0.03450 0.02405  0.00061  436  VAL A C     
3303 O O     . VAL A 436 ? 0.28161 0.22655 0.28355 -0.03534 0.02472  0.00451  436  VAL A O     
3304 C CB    . VAL A 436 ? 0.30083 0.25894 0.30248 -0.03055 0.02229  -0.00230 436  VAL A CB    
3305 C CG1   . VAL A 436 ? 0.31438 0.28112 0.31635 -0.03105 0.02129  -0.00437 436  VAL A CG1   
3306 C CG2   . VAL A 436 ? 0.29963 0.25823 0.30045 -0.02822 0.02240  0.00206  436  VAL A CG2   
3307 N N     . PRO A 437 ? 0.27544 0.21240 0.27729 -0.03307 0.02424  -0.00096 437  PRO A N     
3308 C CA    . PRO A 437 ? 0.26711 0.19515 0.26848 -0.03221 0.02501  0.00225  437  PRO A CA    
3309 C C     . PRO A 437 ? 0.28405 0.21090 0.28452 -0.02685 0.02466  0.00434  437  PRO A C     
3310 O O     . PRO A 437 ? 0.29508 0.22833 0.29547 -0.02405 0.02394  0.00352  437  PRO A O     
3311 C CB    . PRO A 437 ? 0.26770 0.18732 0.26959 -0.03403 0.02534  -0.00124 437  PRO A CB    
3312 C CG    . PRO A 437 ? 0.24846 0.17206 0.24996 -0.03216 0.02465  -0.00611 437  PRO A CG    
3313 C CD    . PRO A 437 ? 0.29657 0.23162 0.29828 -0.03274 0.02388  -0.00598 437  PRO A CD    
3314 N N     . CYS A 438 ? 0.27978 0.19836 0.27984 -0.02550 0.02508  0.00720  438  CYS A N     
3315 C CA    . CYS A 438 ? 0.29483 0.21129 0.29475 -0.02029 0.02459  0.00900  438  CYS A CA    
3316 C C     . CYS A 438 ? 0.33837 0.24337 0.33837 -0.01944 0.02517  0.01021  438  CYS A C     
3317 O O     . CYS A 438 ? 0.30650 0.20526 0.30633 -0.02322 0.02595  0.01051  438  CYS A O     
3318 C CB    . CYS A 438 ? 0.28145 0.20304 0.28022 -0.01856 0.02375  0.01350  438  CYS A CB    
3319 S SG    . CYS A 438 ? 0.34266 0.25981 0.33930 -0.02121 0.02435  0.01904  438  CYS A SG    
3320 N N     . HIS A 439 ? 0.31903 0.22128 0.31968 -0.01441 0.02478  0.01096  439  HIS A N     
3321 C CA    . HIS A 439 ? 0.35100 0.24234 0.35185 -0.01244 0.02511  0.01283  439  HIS A CA    
3322 C C     . HIS A 439 ? 0.35822 0.24946 0.35824 -0.00963 0.02411  0.01880  439  HIS A C     
3323 O O     . HIS A 439 ? 0.34995 0.24781 0.35064 -0.00604 0.02298  0.01978  439  HIS A O     
3324 C CB    . HIS A 439 ? 0.36894 0.25655 0.37146 -0.00835 0.02551  0.00893  439  HIS A CB    
3325 C CG    . HIS A 439 ? 0.42481 0.30756 0.42717 -0.01116 0.02651  0.00348  439  HIS A CG    
3326 N ND1   . HIS A 439 ? 0.46341 0.35276 0.46561 -0.01231 0.02668  -0.00148 439  HIS A ND1   
3327 C CD2   . HIS A 439 ? 0.45353 0.32522 0.45560 -0.01323 0.02719  0.00221  439  HIS A CD2   
3328 C CE1   . HIS A 439 ? 0.44723 0.33016 0.44885 -0.01489 0.02728  -0.00581 439  HIS A CE1   
3329 N NE2   . HIS A 439 ? 0.48159 0.35358 0.48329 -0.01561 0.02761  -0.00382 439  HIS A NE2   
3330 N N     . LEU A 440 ? 0.33218 0.21608 0.33063 -0.01149 0.02443  0.02285  440  LEU A N     
3331 C CA    . LEU A 440 ? 0.36200 0.24401 0.35890 -0.00880 0.02338  0.02885  440  LEU A CA    
3332 C C     . LEU A 440 ? 0.38345 0.25364 0.38120 -0.00590 0.02351  0.03018  440  LEU A C     
3333 O O     . LEU A 440 ? 0.37092 0.23185 0.36791 -0.00894 0.02458  0.03104  440  LEU A O     
3334 C CB    . LEU A 440 ? 0.33273 0.21576 0.32653 -0.01302 0.02383  0.03299  440  LEU A CB    
3335 C CG    . LEU A 440 ? 0.32814 0.22268 0.32098 -0.01530 0.02372  0.03198  440  LEU A CG    
3336 C CD1   . LEU A 440 ? 0.31261 0.20787 0.30228 -0.01899 0.02458  0.03622  440  LEU A CD1   
3337 C CD2   . LEU A 440 ? 0.32371 0.22612 0.31680 -0.01093 0.02185  0.03208  440  LEU A CD2   
3338 N N     . ARG A 441 ? 0.38086 0.25141 0.38058 -0.00002 0.02241  0.03038  441  ARG A N     
3339 C CA    . ARG A 441 ? 0.41529 0.27544 0.41679 0.00383  0.02262  0.03030  441  ARG A CA    
3340 C C     . ARG A 441 ? 0.43991 0.29487 0.44253 0.00165  0.02436  0.02417  441  ARG A C     
3341 O O     . ARG A 441 ? 0.45807 0.32013 0.46190 0.00163  0.02479  0.01915  441  ARG A O     
3342 C CB    . ARG A 441 ? 0.45988 0.31057 0.45916 0.00380  0.02219  0.03656  441  ARG A CB    
3343 C CG    . ARG A 441 ? 0.49868 0.35484 0.49520 0.00425  0.02057  0.04250  441  ARG A CG    
3344 C CD    . ARG A 441 ? 0.43075 0.29129 0.42904 0.01066  0.01831  0.04467  441  ARG A CD    
3345 N NE    . ARG A 441 ? 0.43268 0.29838 0.42758 0.01074  0.01643  0.05008  441  ARG A NE    
3346 C CZ    . ARG A 441 ? 0.39560 0.27166 0.39109 0.01311  0.01442  0.05040  441  ARG A CZ    
3347 N NH1   . ARG A 441 ? 0.43005 0.31315 0.42972 0.01541  0.01420  0.04601  441  ARG A NH1   
3348 N NH2   . ARG A 441 ? 0.39809 0.27761 0.38960 0.01283  0.01267  0.05513  441  ARG A NH2   
3349 N N     . ASP A 442 ? 0.46755 0.31025 0.46958 -0.00021 0.02525  0.02433  442  ASP A N     
3350 C CA    . ASP A 442 ? 0.50990 0.34621 0.51251 -0.00277 0.02662  0.01840  442  ASP A CA    
3351 C C     . ASP A 442 ? 0.46948 0.30685 0.47063 -0.01035 0.02729  0.01724  442  ASP A C     
3352 O O     . ASP A 442 ? 0.46124 0.29199 0.46262 -0.01349 0.02809  0.01295  442  ASP A O     
3353 C CB    . ASP A 442 ? 0.55552 0.37670 0.55864 -0.00045 0.02703  0.01908  442  ASP A CB    
3354 C CG    . ASP A 442 ? 0.63252 0.44568 0.63376 -0.00303 0.02680  0.02573  442  ASP A CG    
3355 O OD1   . ASP A 442 ? 0.75799 0.55868 0.75887 -0.00568 0.02757  0.02552  442  ASP A OD1   
3356 O OD2   . ASP A 442 ? 0.62422 0.44353 0.62407 -0.00254 0.02583  0.03127  442  ASP A OD2   
3357 N N     . LYS A 443 ? 0.40743 0.25319 0.40724 -0.01327 0.02693  0.02073  443  LYS A N     
3358 C CA    . LYS A 443 ? 0.38850 0.23534 0.38741 -0.02028 0.02771  0.02105  443  LYS A CA    
3359 C C     . LYS A 443 ? 0.35911 0.21827 0.35853 -0.02258 0.02761  0.01688  443  LYS A C     
3360 O O     . LYS A 443 ? 0.33804 0.20720 0.33711 -0.02022 0.02686  0.01789  443  LYS A O     
3361 C CB    . LYS A 443 ? 0.38205 0.22916 0.37879 -0.02183 0.02775  0.02824  443  LYS A CB    
3362 C CG    . LYS A 443 ? 0.44970 0.29450 0.44595 -0.02886 0.02906  0.02972  443  LYS A CG    
3363 C CD    . LYS A 443 ? 0.48406 0.32704 0.47756 -0.02965 0.02945  0.03732  443  LYS A CD    
3364 C CE    . LYS A 443 ? 0.49091 0.34591 0.48239 -0.02758 0.02871  0.03972  443  LYS A CE    
3365 N NZ    . LYS A 443 ? 0.51666 0.37144 0.50472 -0.02961 0.02949  0.04645  443  LYS A NZ    
3366 N N     . PHE A 444 ? 0.34012 0.19828 0.34037 -0.02717 0.02814  0.01224  444  PHE A N     
3367 C CA    . PHE A 444 ? 0.34633 0.21565 0.34707 -0.02984 0.02789  0.00857  444  PHE A CA    
3368 C C     . PHE A 444 ? 0.31913 0.19463 0.31956 -0.03428 0.02827  0.01237  444  PHE A C     
3369 O O     . PHE A 444 ? 0.31692 0.18694 0.31765 -0.03882 0.02914  0.01450  444  PHE A O     
3370 C CB    . PHE A 444 ? 0.34280 0.20866 0.34439 -0.03302 0.02798  0.00222  444  PHE A CB    
3371 C CG    . PHE A 444 ? 0.37162 0.24862 0.37360 -0.03535 0.02741  -0.00175 444  PHE A CG    
3372 C CD1   . PHE A 444 ? 0.33011 0.21212 0.33314 -0.04114 0.02744  -0.00134 444  PHE A CD1   
3373 C CD2   . PHE A 444 ? 0.36098 0.24362 0.36244 -0.03165 0.02692  -0.00570 444  PHE A CD2   
3374 C CE1   . PHE A 444 ? 0.31439 0.20667 0.31797 -0.04292 0.02667  -0.00480 444  PHE A CE1   
3375 C CE2   . PHE A 444 ? 0.35924 0.25170 0.36072 -0.03365 0.02626  -0.00896 444  PHE A CE2   
3376 C CZ    . PHE A 444 ? 0.33133 0.22849 0.33388 -0.03915 0.02599  -0.00854 444  PHE A CZ    
3377 N N     . VAL A 445 ? 0.29840 0.18514 0.29831 -0.03298 0.02777  0.01324  445  VAL A N     
3378 C CA    . VAL A 445 ? 0.29407 0.18709 0.29320 -0.03575 0.02829  0.01724  445  VAL A CA    
3379 C C     . VAL A 445 ? 0.28761 0.19226 0.28777 -0.03751 0.02793  0.01407  445  VAL A C     
3380 O O     . VAL A 445 ? 0.29100 0.20085 0.29132 -0.03451 0.02694  0.01091  445  VAL A O     
3381 C CB    . VAL A 445 ? 0.31034 0.20467 0.30708 -0.03164 0.02784  0.02248  445  VAL A CB    
3382 C CG1   . VAL A 445 ? 0.32130 0.22326 0.31655 -0.03401 0.02845  0.02582  445  VAL A CG1   
3383 C CG2   . VAL A 445 ? 0.29495 0.17775 0.29061 -0.02997 0.02804  0.02634  445  VAL A CG2   
3384 N N     . LEU A 446 ? 0.27593 0.18478 0.27697 -0.04230 0.02882  0.01513  446  LEU A N     
3385 C CA    . LEU A 446 ? 0.25447 0.17461 0.25671 -0.04379 0.02848  0.01282  446  LEU A CA    
3386 C C     . LEU A 446 ? 0.25854 0.18605 0.25889 -0.04160 0.02859  0.01638  446  LEU A C     
3387 O O     . LEU A 446 ? 0.25959 0.18446 0.25796 -0.04148 0.02949  0.02111  446  LEU A O     
3388 C CB    . LEU A 446 ? 0.26526 0.18720 0.27026 -0.05001 0.02932  0.01175  446  LEU A CB    
3389 C CG    . LEU A 446 ? 0.30897 0.22702 0.31618 -0.05307 0.02862  0.00665  446  LEU A CG    
3390 C CD1   . LEU A 446 ? 0.29962 0.20429 0.30641 -0.05376 0.02906  0.00709  446  LEU A CD1   
3391 C CD2   . LEU A 446 ? 0.32974 0.25435 0.34034 -0.05883 0.02887  0.00538  446  LEU A CD2   
3392 N N     . ARG A 447 ? 0.21650 0.15291 0.21711 -0.03986 0.02761  0.01406  447  ARG A N     
3393 C CA    . ARG A 447 ? 0.24145 0.18503 0.24029 -0.03778 0.02747  0.01648  447  ARG A CA    
3394 C C     . ARG A 447 ? 0.23991 0.19234 0.24052 -0.04079 0.02807  0.01539  447  ARG A C     
3395 O O     . ARG A 447 ? 0.24334 0.19912 0.24655 -0.04271 0.02753  0.01162  447  ARG A O     
3396 C CB    . ARG A 447 ? 0.20577 0.15237 0.20366 -0.03300 0.02579  0.01506  447  ARG A CB    
3397 C CG    . ARG A 447 ? 0.23354 0.17310 0.23035 -0.02931 0.02511  0.01625  447  ARG A CG    
3398 C CD    . ARG A 447 ? 0.24040 0.18372 0.23752 -0.02524 0.02364  0.01417  447  ARG A CD    
3399 N NE    . ARG A 447 ? 0.24475 0.19413 0.24038 -0.02303 0.02267  0.01612  447  ARG A NE    
3400 C CZ    . ARG A 447 ? 0.25424 0.21127 0.24993 -0.02367 0.02233  0.01488  447  ARG A CZ    
3401 N NH1   . ARG A 447 ? 0.21210 0.17265 0.20944 -0.02635 0.02278  0.01197  447  ARG A NH1   
3402 N NH2   . ARG A 447 ? 0.22666 0.18779 0.22076 -0.02147 0.02129  0.01653  447  ARG A NH2   
3403 N N     . PHE A 448 ? 0.20299 0.15938 0.20207 -0.04100 0.02915  0.01866  448  PHE A N     
3404 C CA    . PHE A 448 ? 0.19845 0.16412 0.19918 -0.04280 0.02985  0.01792  448  PHE A CA    
3405 C C     . PHE A 448 ? 0.16856 0.13925 0.16633 -0.03902 0.02931  0.01916  448  PHE A C     
3406 O O     . PHE A 448 ? 0.18768 0.15703 0.18216 -0.03810 0.03022  0.02276  448  PHE A O     
3407 C CB    . PHE A 448 ? 0.18671 0.15272 0.18878 -0.04726 0.03226  0.02047  448  PHE A CB    
3408 C CG    . PHE A 448 ? 0.21238 0.18842 0.21751 -0.04937 0.03313  0.01924  448  PHE A CG    
3409 C CD1   . PHE A 448 ? 0.21217 0.19152 0.22204 -0.05273 0.03266  0.01595  448  PHE A CD1   
3410 C CD2   . PHE A 448 ? 0.19436 0.17663 0.19763 -0.04782 0.03432  0.02124  448  PHE A CD2   
3411 C CE1   . PHE A 448 ? 0.23878 0.22800 0.25213 -0.05439 0.03329  0.01497  448  PHE A CE1   
3412 C CE2   . PHE A 448 ? 0.21441 0.20610 0.22093 -0.04928 0.03526  0.02006  448  PHE A CE2   
3413 C CZ    . PHE A 448 ? 0.20082 0.19624 0.21270 -0.05251 0.03472  0.01708  448  PHE A CZ    
3414 N N     . ALA A 449 ? 0.17536 0.15146 0.17397 -0.03690 0.02775  0.01623  449  ALA A N     
3415 C CA    . ALA A 449 ? 0.19035 0.17044 0.18640 -0.03333 0.02682  0.01680  449  ALA A CA    
3416 C C     . ALA A 449 ? 0.18832 0.17694 0.18578 -0.03398 0.02742  0.01571  449  ALA A C     
3417 O O     . ALA A 449 ? 0.18564 0.17845 0.18657 -0.03549 0.02705  0.01299  449  ALA A O     
3418 C CB    . ALA A 449 ? 0.18418 0.16348 0.18010 -0.03014 0.02460  0.01471  449  ALA A CB    
3419 N N     . ILE A 450 ? 0.17743 0.16863 0.17206 -0.03264 0.02826  0.01776  450  ILE A N     
3420 C CA    . ILE A 450 ? 0.18625 0.18536 0.18183 -0.03222 0.02885  0.01667  450  ILE A CA    
3421 C C     . ILE A 450 ? 0.16531 0.16668 0.16056 -0.02891 0.02645  0.01437  450  ILE A C     
3422 O O     . ILE A 450 ? 0.19867 0.19728 0.19062 -0.02615 0.02512  0.01514  450  ILE A O     
3423 C CB    . ILE A 450 ? 0.19145 0.19199 0.18338 -0.03169 0.03080  0.01942  450  ILE A CB    
3424 C CG1   . ILE A 450 ? 0.19018 0.18796 0.18212 -0.03517 0.03338  0.02238  450  ILE A CG1   
3425 C CG2   . ILE A 450 ? 0.18170 0.19039 0.17496 -0.03093 0.03170  0.01799  450  ILE A CG2   
3426 C CD1   . ILE A 450 ? 0.18479 0.18620 0.18243 -0.03926 0.03478  0.02123  450  ILE A CD1   
3427 N N     . CYS A 451 ? 0.17384 0.18032 0.17262 -0.02929 0.02576  0.01173  451  CYS A N     
3428 C CA    . CYS A 451 ? 0.15491 0.16267 0.15369 -0.02663 0.02345  0.00974  451  CYS A CA    
3429 C C     . CYS A 451 ? 0.15308 0.16748 0.15291 -0.02513 0.02321  0.00853  451  CYS A C     
3430 O O     . CYS A 451 ? 0.17736 0.19175 0.17482 -0.02226 0.02211  0.00851  451  CYS A O     
3431 C CB    . CYS A 451 ? 0.15589 0.16236 0.15718 -0.02785 0.02228  0.00764  451  CYS A CB    
3432 S SG    . CYS A 451 ? 0.17920 0.17703 0.17915 -0.02832 0.02220  0.00845  451  CYS A SG    
3433 N N     . SER A 452 ? 0.15406 0.17410 0.15766 -0.02694 0.02404  0.00748  452  SER A N     
3434 C CA    . SER A 452 ? 0.15940 0.18573 0.16481 -0.02510 0.02332  0.00603  452  SER A CA    
3435 C C     . SER A 452 ? 0.16335 0.19174 0.16646 -0.02286 0.02461  0.00695  452  SER A C     
3436 O O     . SER A 452 ? 0.15977 0.18784 0.16142 -0.02389 0.02687  0.00864  452  SER A O     
3437 C CB    . SER A 452 ? 0.17112 0.20362 0.18168 -0.02759 0.02371  0.00476  452  SER A CB    
3438 O OG    . SER A 452 ? 0.18374 0.22274 0.19636 -0.02544 0.02314  0.00371  452  SER A OG    
3439 N N     . ARG A 453 ? 0.13968 0.16993 0.14218 -0.01973 0.02319  0.00582  453  ARG A N     
3440 C CA    . ARG A 453 ? 0.14927 0.18142 0.14949 -0.01722 0.02426  0.00599  453  ARG A CA    
3441 C C     . ARG A 453 ? 0.18197 0.22079 0.18520 -0.01826 0.02699  0.00612  453  ARG A C     
3442 O O     . ARG A 453 ? 0.17165 0.21147 0.17229 -0.01717 0.02908  0.00685  453  ARG A O     
3443 C CB    . ARG A 453 ? 0.18352 0.21627 0.18342 -0.01391 0.02211  0.00448  453  ARG A CB    
3444 C CG    . ARG A 453 ? 0.18407 0.21791 0.18129 -0.01092 0.02296  0.00405  453  ARG A CG    
3445 C CD    . ARG A 453 ? 0.22533 0.25781 0.22190 -0.00784 0.02050  0.00270  453  ARG A CD    
3446 N NE    . ARG A 453 ? 0.23370 0.27039 0.23494 -0.00758 0.01935  0.00180  453  ARG A NE    
3447 C CZ    . ARG A 453 ? 0.23801 0.28107 0.24284 -0.00648 0.02033  0.00101  453  ARG A CZ    
3448 N NH1   . ARG A 453 ? 0.26750 0.31375 0.27197 -0.00544 0.02286  0.00084  453  ARG A NH1   
3449 N NH2   . ARG A 453 ? 0.25647 0.30317 0.26531 -0.00628 0.01875  0.00045  453  ARG A NH2   
3450 N N     . THR A 454 ? 0.15478 0.19858 0.16349 -0.02042 0.02704  0.00539  454  THR A N     
3451 C CA    . THR A 454 ? 0.16615 0.21787 0.17924 -0.02137 0.02936  0.00535  454  THR A CA    
3452 C C     . THR A 454 ? 0.18929 0.24187 0.20493 -0.02600 0.03145  0.00674  454  THR A C     
3453 O O     . THR A 454 ? 0.19428 0.25420 0.21519 -0.02779 0.03301  0.00663  454  THR A O     
3454 C CB    . THR A 454 ? 0.18453 0.24268 0.20277 -0.02028 0.02761  0.00351  454  THR A CB    
3455 O OG1   . THR A 454 ? 0.19472 0.25213 0.21551 -0.02309 0.02563  0.00283  454  THR A OG1   
3456 C CG2   . THR A 454 ? 0.18700 0.24343 0.20274 -0.01582 0.02552  0.00244  454  THR A CG2   
3457 N N     . VAL A 455 ? 0.17423 0.21951 0.18664 -0.02799 0.03148  0.00815  455  VAL A N     
3458 C CA    . VAL A 455 ? 0.17855 0.22336 0.19316 -0.03250 0.03343  0.00968  455  VAL A CA    
3459 C C     . VAL A 455 ? 0.19463 0.24275 0.20840 -0.03303 0.03717  0.01185  455  VAL A C     
3460 O O     . VAL A 455 ? 0.18673 0.23355 0.19547 -0.02999 0.03808  0.01261  455  VAL A O     
3461 C CB    . VAL A 455 ? 0.17901 0.21441 0.19023 -0.03390 0.03241  0.01068  455  VAL A CB    
3462 C CG1   . VAL A 455 ? 0.19315 0.22284 0.19775 -0.03125 0.03269  0.01249  455  VAL A CG1   
3463 C CG2   . VAL A 455 ? 0.20138 0.23528 0.21524 -0.03878 0.03412  0.01208  455  VAL A CG2   
3464 N N     . GLU A 456 ? 0.16542 0.21813 0.18409 -0.03701 0.03938  0.01278  456  GLU A N     
3465 C CA    . GLU A 456 ? 0.19014 0.24735 0.20894 -0.03806 0.04343  0.01503  456  GLU A CA    
3466 C C     . GLU A 456 ? 0.17430 0.22805 0.19413 -0.04328 0.04533  0.01769  456  GLU A C     
3467 O O     . GLU A 456 ? 0.18892 0.23725 0.21000 -0.04594 0.04339  0.01726  456  GLU A O     
3468 C CB    . GLU A 456 ? 0.18756 0.25635 0.21293 -0.03767 0.04482  0.01371  456  GLU A CB    
3469 C CG    . GLU A 456 ? 0.23497 0.30706 0.25981 -0.03234 0.04300  0.01118  456  GLU A CG    
3470 C CD    . GLU A 456 ? 0.28288 0.35334 0.30111 -0.02817 0.04469  0.01170  456  GLU A CD    
3471 O OE1   . GLU A 456 ? 0.39759 0.46831 0.41424 -0.02375 0.04290  0.00965  456  GLU A OE1   
3472 O OE2   . GLU A 456 ? 0.31906 0.38777 0.33344 -0.02930 0.04772  0.01413  456  GLU A OE2   
3473 N N     . SER A 457 ? 0.18351 0.24028 0.20267 -0.04472 0.04933  0.02047  457  SER A N     
3474 C CA    . SER A 457 ? 0.16042 0.21365 0.18043 -0.04988 0.05148  0.02360  457  SER A CA    
3475 C C     . SER A 457 ? 0.17171 0.22843 0.20018 -0.05479 0.05071  0.02233  457  SER A C     
3476 O O     . SER A 457 ? 0.16853 0.21862 0.19764 -0.05882 0.05029  0.02345  457  SER A O     
3477 C CB    . SER A 457 ? 0.19562 0.25314 0.21385 -0.05061 0.05628  0.02692  457  SER A CB    
3478 O OG    . SER A 457 ? 0.24846 0.30122 0.25771 -0.04666 0.05678  0.02830  457  SER A OG    
3479 N N     . ALA A 458 ? 0.18264 0.24955 0.21765 -0.05442 0.05031  0.01990  458  ALA A N     
3480 C CA    . ALA A 458 ? 0.20194 0.27333 0.24527 -0.05917 0.04920  0.01845  458  ALA A CA    
3481 C C     . ALA A 458 ? 0.17211 0.23561 0.21463 -0.06004 0.04498  0.01606  458  ALA A C     
3482 O O     . ALA A 458 ? 0.16724 0.22839 0.21348 -0.06506 0.04433  0.01579  458  ALA A O     
3483 C CB    . ALA A 458 ? 0.24654 0.33074 0.29672 -0.05764 0.04900  0.01625  458  ALA A CB    
3484 N N     . HIS A 459 ? 0.17200 0.23127 0.20965 -0.05528 0.04220  0.01421  459  HIS A N     
3485 C CA    . HIS A 459 ? 0.18899 0.24107 0.22534 -0.05561 0.03858  0.01194  459  HIS A CA    
3486 C C     . HIS A 459 ? 0.20062 0.24155 0.23316 -0.05805 0.03914  0.01390  459  HIS A C     
3487 O O     . HIS A 459 ? 0.17402 0.21030 0.20837 -0.06127 0.03752  0.01248  459  HIS A O     
3488 C CB    . HIS A 459 ? 0.18790 0.23823 0.21986 -0.05000 0.03599  0.01012  459  HIS A CB    
3489 C CG    . HIS A 459 ? 0.18611 0.24609 0.22126 -0.04703 0.03526  0.00840  459  HIS A CG    
3490 N ND1   . HIS A 459 ? 0.20749 0.26927 0.23928 -0.04224 0.03598  0.00881  459  HIS A ND1   
3491 C CD2   . HIS A 459 ? 0.24197 0.31008 0.28335 -0.04800 0.03366  0.00624  459  HIS A CD2   
3492 C CE1   . HIS A 459 ? 0.23883 0.30903 0.27474 -0.04021 0.03504  0.00707  459  HIS A CE1   
3493 N NE2   . HIS A 459 ? 0.20505 0.27956 0.24690 -0.04356 0.03356  0.00564  459  HIS A NE2   
3494 N N     . VAL A 460 ? 0.17144 0.20775 0.19844 -0.05635 0.04129  0.01709  460  VAL A N     
3495 C CA    . VAL A 460 ? 0.18020 0.20575 0.20337 -0.05811 0.04177  0.01948  460  VAL A CA    
3496 C C     . VAL A 460 ? 0.18799 0.21310 0.21575 -0.06435 0.04380  0.02115  460  VAL A C     
3497 O O     . VAL A 460 ? 0.19073 0.20748 0.21852 -0.06715 0.04285  0.02111  460  VAL A O     
3498 C CB    . VAL A 460 ? 0.17138 0.19326 0.18750 -0.05480 0.04344  0.02277  460  VAL A CB    
3499 C CG1   . VAL A 460 ? 0.17609 0.18752 0.18866 -0.05674 0.04421  0.02601  460  VAL A CG1   
3500 C CG2   . VAL A 460 ? 0.16946 0.19038 0.18127 -0.04917 0.04090  0.02088  460  VAL A CG2   
3501 N N     . GLN A 461 ? 0.17523 0.20934 0.20723 -0.06665 0.04667  0.02258  461  GLN A N     
3502 C CA    . GLN A 461 ? 0.18139 0.21613 0.21858 -0.07310 0.04881  0.02443  461  GLN A CA    
3503 C C     . GLN A 461 ? 0.19701 0.23250 0.24048 -0.07691 0.04597  0.02075  461  GLN A C     
3504 O O     . GLN A 461 ? 0.21641 0.24583 0.26196 -0.08195 0.04607  0.02138  461  GLN A O     
3505 C CB    . GLN A 461 ? 0.19540 0.24137 0.23640 -0.07437 0.05266  0.02656  461  GLN A CB    
3506 C CG    . GLN A 461 ? 0.18045 0.22491 0.21474 -0.07181 0.05610  0.03065  461  GLN A CG    
3507 C CD    . GLN A 461 ? 0.21007 0.26690 0.24737 -0.07131 0.05976  0.03171  461  GLN A CD    
3508 O OE1   . GLN A 461 ? 0.23015 0.29707 0.27554 -0.07325 0.05988  0.02977  461  GLN A OE1   
3509 N NE2   . GLN A 461 ? 0.20404 0.26048 0.23478 -0.06847 0.06269  0.03465  461  GLN A NE2   
3510 N N     . ARG A 462 ? 0.18919 0.23178 0.23546 -0.07459 0.04329  0.01688  462  ARG A N     
3511 C CA    . ARG A 462 ? 0.19727 0.24075 0.24850 -0.07778 0.04011  0.01306  462  ARG A CA    
3512 C C     . ARG A 462 ? 0.21108 0.24206 0.25771 -0.07750 0.03759  0.01136  462  ARG A C     
3513 O O     . ARG A 462 ? 0.21512 0.24186 0.26453 -0.08207 0.03632  0.00968  462  ARG A O     
3514 C CB    . ARG A 462 ? 0.24045 0.29396 0.29458 -0.07460 0.03766  0.00974  462  ARG A CB    
3515 C CG    . ARG A 462 ? 0.25528 0.32238 0.31675 -0.07609 0.03944  0.01032  462  ARG A CG    
3516 C CD    . ARG A 462 ? 0.30879 0.38475 0.37273 -0.07234 0.03660  0.00719  462  ARG A CD    
3517 N NE    . ARG A 462 ? 0.41114 0.50002 0.48093 -0.07167 0.03878  0.00818  462  ARG A NE    
3518 C CZ    . ARG A 462 ? 0.41075 0.50526 0.47928 -0.06595 0.03894  0.00789  462  ARG A CZ    
3519 N NH1   . ARG A 462 ? 0.37095 0.45955 0.43274 -0.06077 0.03695  0.00680  462  ARG A NH1   
3520 N NH2   . ARG A 462 ? 0.44608 0.55243 0.52051 -0.06542 0.04122  0.00870  462  ARG A NH2   
3521 N N     . ALA A 463 ? 0.18944 0.21457 0.22925 -0.07213 0.03683  0.01159  463  ALA A N     
3522 C CA    . ALA A 463 ? 0.22131 0.23523 0.25695 -0.07117 0.03474  0.01006  463  ALA A CA    
3523 C C     . ALA A 463 ? 0.22827 0.23218 0.26314 -0.07507 0.03636  0.01258  463  ALA A C     
3524 O O     . ALA A 463 ? 0.22999 0.22636 0.26512 -0.07730 0.03472  0.01036  463  ALA A O     
3525 C CB    . ALA A 463 ? 0.19503 0.20563 0.22423 -0.06485 0.03401  0.01054  463  ALA A CB    
3526 N N     . TRP A 464 ? 0.23277 0.23611 0.26633 -0.07584 0.03961  0.01723  464  TRP A N     
3527 C CA    . TRP A 464 ? 0.21862 0.21206 0.25124 -0.07952 0.04127  0.02033  464  TRP A CA    
3528 C C     . TRP A 464 ? 0.25422 0.24840 0.29358 -0.08654 0.04135  0.01912  464  TRP A C     
3529 O O     . TRP A 464 ? 0.25341 0.23731 0.29261 -0.08951 0.04068  0.01876  464  TRP A O     
3530 C CB    . TRP A 464 ? 0.21861 0.21231 0.24804 -0.07896 0.04485  0.02589  464  TRP A CB    
3531 C CG    . TRP A 464 ? 0.20822 0.19324 0.23765 -0.08362 0.04693  0.02974  464  TRP A CG    
3532 C CD1   . TRP A 464 ? 0.25354 0.24212 0.28653 -0.08874 0.05025  0.03324  464  TRP A CD1   
3533 C CD2   . TRP A 464 ? 0.26297 0.23413 0.28900 -0.08367 0.04589  0.03059  464  TRP A CD2   
3534 N NE1   . TRP A 464 ? 0.28320 0.26042 0.31488 -0.09218 0.05128  0.03648  464  TRP A NE1   
3535 C CE2   . TRP A 464 ? 0.25403 0.22020 0.28144 -0.08895 0.04856  0.03485  464  TRP A CE2   
3536 C CE3   . TRP A 464 ? 0.27314 0.23577 0.29531 -0.07962 0.04312  0.02830  464  TRP A CE3   
3537 C CZ2   . TRP A 464 ? 0.29954 0.25178 0.32439 -0.09011 0.04832  0.03685  464  TRP A CZ2   
3538 C CZ3   . TRP A 464 ? 0.28951 0.23901 0.30944 -0.08053 0.04300  0.03006  464  TRP A CZ3   
3539 C CH2   . TRP A 464 ? 0.31295 0.25700 0.33412 -0.08564 0.04547  0.03430  464  TRP A CH2   
3540 N N     . GLU A 465 ? 0.22608 0.23230 0.27167 -0.08927 0.04210  0.01843  465  GLU A N     
3541 C CA    . GLU A 465 ? 0.24708 0.25541 0.29995 -0.09622 0.04170  0.01690  465  GLU A CA    
3542 C C     . GLU A 465 ? 0.28895 0.29193 0.34218 -0.09698 0.03762  0.01153  465  GLU A C     
3543 O O     . GLU A 465 ? 0.26692 0.26278 0.32241 -0.10214 0.03697  0.01053  465  GLU A O     
3544 C CB    . GLU A 465 ? 0.28331 0.30722 0.34325 -0.09795 0.04264  0.01655  465  GLU A CB    
3545 C CG    . GLU A 465 ? 0.36327 0.39124 0.43174 -0.10535 0.04186  0.01481  465  GLU A CG    
3546 C CD    . GLU A 465 ? 0.46514 0.50955 0.54111 -0.10600 0.04168  0.01340  465  GLU A CD    
3547 O OE1   . GLU A 465 ? 0.51646 0.56922 0.59218 -0.10249 0.04424  0.01577  465  GLU A OE1   
3548 O OE2   . GLU A 465 ? 0.54160 0.59056 0.62369 -0.10990 0.03884  0.00979  465  GLU A OE2   
3549 N N     . HIS A 466 ? 0.24195 0.24794 0.29261 -0.09189 0.03493  0.00804  466  HIS A N     
3550 C CA    . HIS A 466 ? 0.26680 0.26768 0.31636 -0.09173 0.03127  0.00295  466  HIS A CA    
3551 C C     . HIS A 466 ? 0.29587 0.28146 0.34040 -0.09131 0.03124  0.00323  466  HIS A C     
3552 O O     . HIS A 466 ? 0.29116 0.26981 0.33683 -0.09496 0.02966  0.00027  466  HIS A O     
3553 C CB    . HIS A 466 ? 0.26163 0.26830 0.30841 -0.08575 0.02902  0.00028  466  HIS A CB    
3554 C CG    . HIS A 466 ? 0.27939 0.28308 0.32495 -0.08546 0.02541  -0.00500 466  HIS A CG    
3555 N ND1   . HIS A 466 ? 0.29263 0.29921 0.34287 -0.09047 0.02319  -0.00861 466  HIS A ND1   
3556 C CD2   . HIS A 466 ? 0.27549 0.27402 0.31551 -0.08076 0.02368  -0.00730 466  HIS A CD2   
3557 C CE1   . HIS A 466 ? 0.32645 0.32936 0.37336 -0.08872 0.02026  -0.01304 466  HIS A CE1   
3558 N NE2   . HIS A 466 ? 0.30873 0.30689 0.34957 -0.08282 0.02070  -0.01223 466  HIS A NE2   
3559 N N     . ILE A 467 ? 0.24994 0.23009 0.28891 -0.08674 0.03286  0.00664  467  ILE A N     
3560 C CA    . ILE A 467 ? 0.27141 0.23745 0.30578 -0.08547 0.03282  0.00728  467  ILE A CA    
3561 C C     . ILE A 467 ? 0.31512 0.27319 0.35204 -0.09160 0.03433  0.00938  467  ILE A C     
3562 O O     . ILE A 467 ? 0.30394 0.25112 0.33996 -0.09311 0.03315  0.00724  467  ILE A O     
3563 C CB    . ILE A 467 ? 0.25102 0.21437 0.27960 -0.07962 0.03416  0.01114  467  ILE A CB    
3564 C CG1   . ILE A 467 ? 0.24596 0.21502 0.27192 -0.07375 0.03225  0.00856  467  ILE A CG1   
3565 C CG2   . ILE A 467 ? 0.28536 0.23455 0.31005 -0.07857 0.03445  0.01287  467  ILE A CG2   
3566 C CD1   . ILE A 467 ? 0.21937 0.18921 0.24076 -0.06861 0.03341  0.01221  467  ILE A CD1   
3567 N N     . LYS A 468 ? 0.26017 0.22345 0.30036 -0.09527 0.03709  0.01356  468  LYS A N     
3568 C CA    . LYS A 468 ? 0.30986 0.26576 0.35264 -0.10150 0.03889  0.01637  468  LYS A CA    
3569 C C     . LYS A 468 ? 0.29526 0.25026 0.34363 -0.10760 0.03673  0.01176  468  LYS A C     
3570 O O     . LYS A 468 ? 0.33356 0.27699 0.38226 -0.11145 0.03661  0.01171  468  LYS A O     
3571 C CB    . LYS A 468 ? 0.31403 0.27763 0.35933 -0.10413 0.04261  0.02183  468  LYS A CB    
3572 C CG    . LYS A 468 ? 0.41755 0.37089 0.46002 -0.10597 0.04551  0.02783  468  LYS A CG    
3573 C CD    . LYS A 468 ? 0.42525 0.38465 0.47320 -0.11251 0.04887  0.03183  468  LYS A CD    
3574 C CE    . LYS A 468 ? 0.42453 0.40012 0.47469 -0.11083 0.05066  0.03265  468  LYS A CE    
3575 N NZ    . LYS A 468 ? 0.40715 0.38728 0.45992 -0.11527 0.05517  0.03844  468  LYS A NZ    
3576 N N     . GLU A 469 ? 0.27791 0.24479 0.33063 -0.10852 0.03480  0.00781  469  GLU A N     
3577 C CA    . GLU A 469 ? 0.33525 0.30245 0.39320 -0.11435 0.03221  0.00306  469  GLU A CA    
3578 C C     . GLU A 469 ? 0.36048 0.31625 0.41408 -0.11258 0.02921  -0.00198 469  GLU A C     
3579 O O     . GLU A 469 ? 0.35588 0.30311 0.41128 -0.11762 0.02808  -0.00435 469  GLU A O     
3580 C CB    . GLU A 469 ? 0.38606 0.36932 0.44921 -0.11485 0.03051  0.00023  469  GLU A CB    
3581 C CG    . GLU A 469 ? 0.43963 0.43509 0.50854 -0.11735 0.03352  0.00450  469  GLU A CG    
3582 C CD    . GLU A 469 ? 0.59005 0.59981 0.66680 -0.12063 0.03151  0.00139  469  GLU A CD    
3583 O OE1   . GLU A 469 ? 0.59121 0.61012 0.67477 -0.12484 0.03385  0.00430  469  GLU A OE1   
3584 O OE2   . GLU A 469 ? 0.64325 0.65555 0.71941 -0.11888 0.02765  -0.00378 469  GLU A OE2   
3585 N N     . LEU A 470 ? 0.33441 0.28991 0.38239 -0.10552 0.02799  -0.00381 470  LEU A N     
3586 C CA    . LEU A 470 ? 0.35529 0.30071 0.39890 -0.10323 0.02559  -0.00859 470  LEU A CA    
3587 C C     . LEU A 470 ? 0.39114 0.32059 0.43136 -0.10302 0.02706  -0.00636 470  LEU A C     
3588 O O     . LEU A 470 ? 0.39254 0.31163 0.43126 -0.10405 0.02545  -0.01037 470  LEU A O     
3589 C CB    . LEU A 470 ? 0.34748 0.29741 0.38633 -0.09581 0.02436  -0.01042 470  LEU A CB    
3590 C CG    . LEU A 470 ? 0.36225 0.32627 0.40375 -0.09557 0.02221  -0.01345 470  LEU A CG    
3591 C CD1   . LEU A 470 ? 0.32813 0.29374 0.36437 -0.08877 0.02077  -0.01573 470  LEU A CD1   
3592 C CD2   . LEU A 470 ? 0.41967 0.38519 0.46533 -0.10157 0.01952  -0.01834 470  LEU A CD2   
3593 N N     . ALA A 471 ? 0.34154 0.26864 0.38029 -0.10154 0.03002  -0.00006 471  ALA A N     
3594 C CA    . ALA A 471 ? 0.35481 0.26684 0.39063 -0.10140 0.03136  0.00283  471  ALA A CA    
3595 C C     . ALA A 471 ? 0.42930 0.33363 0.46933 -0.10922 0.03146  0.00238  471  ALA A C     
3596 O O     . ALA A 471 ? 0.42632 0.31641 0.46435 -0.10965 0.03096  0.00118  471  ALA A O     
3597 C CB    . ALA A 471 ? 0.33759 0.25003 0.37089 -0.09866 0.03434  0.01004  471  ALA A CB    
3598 N N     . ALA A 472 ? 0.39611 0.30967 0.44234 -0.11547 0.03211  0.00333  472  ALA A N     
3599 C CA    . ALA A 472 ? 0.44033 0.34776 0.49152 -0.12371 0.03196  0.00266  472  ALA A CA    
3600 C C     . ALA A 472 ? 0.47124 0.37280 0.52245 -0.12530 0.02828  -0.00509 472  ALA A C     
3601 O O     . ALA A 472 ? 0.51496 0.40291 0.56614 -0.12886 0.02776  -0.00648 472  ALA A O     
3602 C CB    . ALA A 472 ? 0.39492 0.31600 0.45359 -0.12980 0.03321  0.00476  472  ALA A CB    
3603 N N     . ASP A 473 ? 0.43125 0.34264 0.48208 -0.12258 0.02567  -0.01022 473  ASP A N     
3604 C CA    . ASP A 473 ? 0.51066 0.41723 0.56012 -0.12326 0.02211  -0.01786 473  ASP A CA    
3605 C C     . ASP A 473 ? 0.53921 0.42994 0.58209 -0.11849 0.02208  -0.01948 473  ASP A C     
3606 O O     . ASP A 473 ? 0.58085 0.45985 0.62319 -0.12145 0.02062  -0.02359 473  ASP A O     
3607 C CB    . ASP A 473 ? 0.53420 0.45429 0.58303 -0.11982 0.01966  -0.02201 473  ASP A CB    
3608 C CG    . ASP A 473 ? 0.56195 0.49800 0.61785 -0.12426 0.01919  -0.02121 473  ASP A CG    
3609 O OD1   . ASP A 473 ? 0.56627 0.50345 0.62797 -0.13045 0.02085  -0.01777 473  ASP A OD1   
3610 O OD2   . ASP A 473 ? 0.58188 0.52956 0.63768 -0.12140 0.01725  -0.02379 473  ASP A OD2   
3611 N N     . VAL A 474 ? 0.47758 0.36785 0.51560 -0.11099 0.02362  -0.01641 474  VAL A N     
3612 C CA    . VAL A 474 ? 0.50924 0.38672 0.54143 -0.10541 0.02348  -0.01820 474  VAL A CA    
3613 C C     . VAL A 474 ? 0.56176 0.42343 0.59381 -0.10770 0.02512  -0.01488 474  VAL A C     
3614 O O     . VAL A 474 ? 0.58022 0.42858 0.60973 -0.10681 0.02422  -0.01851 474  VAL A O     
3615 C CB    . VAL A 474 ? 0.46559 0.34840 0.49351 -0.09709 0.02447  -0.01562 474  VAL A CB    
3616 C CG1   . VAL A 474 ? 0.52248 0.39189 0.54580 -0.09172 0.02543  -0.01435 474  VAL A CG1   
3617 C CG2   . VAL A 474 ? 0.44492 0.33812 0.47132 -0.09387 0.02228  -0.02074 474  VAL A CG2   
3618 N N     . LEU A 475 ? 0.52546 0.38809 0.56005 -0.11062 0.02762  -0.00791 475  LEU A N     
3619 C CA    . LEU A 475 ? 0.53798 0.38568 0.57258 -0.11337 0.02924  -0.00395 475  LEU A CA    
3620 C C     . LEU A 475 ? 0.70455 0.54412 0.74287 -0.12111 0.02770  -0.00820 475  LEU A C     
3621 O O     . LEU A 475 ? 0.72673 0.55012 0.76329 -0.12152 0.02747  -0.00929 475  LEU A O     
3622 C CB    . LEU A 475 ? 0.51748 0.36965 0.55384 -0.11539 0.03237  0.00451  475  LEU A CB    
3623 C CG    . LEU A 475 ? 0.50496 0.35972 0.53651 -0.10789 0.03407  0.00978  475  LEU A CG    
3624 C CD1   . LEU A 475 ? 0.48503 0.34660 0.51823 -0.11060 0.03708  0.01727  475  LEU A CD1   
3625 C CD2   . LEU A 475 ? 0.45093 0.28994 0.47769 -0.10291 0.03415  0.01113  475  LEU A CD2   
3626 N N     . ARG A 476 ? 0.68137 0.53201 0.72511 -0.12733 0.02650  -0.01062 476  ARG A N     
3627 C CA    . ARG A 476 ? 0.75954 0.60614 0.80700 -0.13335 0.02349  -0.01564 476  ARG A CA    
3628 C C     . ARG A 476 ? 0.80548 0.64103 0.84808 -0.13023 0.02101  -0.02327 476  ARG A C     
3629 O O     . ARG A 476 ? 0.87461 0.69748 0.91705 -0.13156 0.01933  -0.02497 476  ARG A O     
3630 C CB    . ARG A 476 ? 0.75949 0.62298 0.81281 -0.13816 0.02177  -0.01812 476  ARG A CB    
3631 C CG    . ARG A 476 ? 0.86729 0.72973 0.92522 -0.14398 0.01788  -0.02285 476  ARG A CG    
3632 C CD    . ARG A 476 ? 0.89465 0.77516 0.95906 -0.14824 0.01632  -0.02419 476  ARG A CD    
3633 N NE    . ARG A 476 ? 0.99985 0.88020 1.06851 -0.15355 0.01205  -0.02931 476  ARG A NE    
3634 C CZ    . ARG A 476 ? 1.03041 0.90946 1.10577 -0.15950 0.01130  -0.02665 476  ARG A CZ    
3635 N NH1   . ARG A 476 ? 1.03129 0.90926 1.10982 -0.16101 0.01468  -0.01877 476  ARG A NH1   
3636 N NH2   . ARG A 476 ? 1.01578 0.89473 1.09469 -0.16409 0.00701  -0.03196 476  ARG A NH2   
3637 N N     . ALA A 477 ? 0.75524 0.59683 0.79373 -0.12470 0.02027  -0.02746 477  ALA A N     
3638 C CA    . ALA A 477 ? 0.78253 0.61637 0.81639 -0.12165 0.01789  -0.03529 477  ALA A CA    
3639 C C     . ALA A 477 ? 0.84524 0.66192 0.87430 -0.11648 0.01924  -0.03466 477  ALA A C     
3640 O O     . ALA A 477 ? 0.91780 0.72418 0.94364 -0.11535 0.01765  -0.04115 477  ALA A O     
3641 C CB    . ALA A 477 ? 0.66441 0.51134 0.69514 -0.11587 0.01654  -0.03871 477  ALA A CB    
3642 N N     . GLU A 478 ? 0.82429 0.63772 0.85263 -0.11311 0.02205  -0.02714 478  GLU A N     
3643 C CA    . GLU A 478 ? 0.88954 0.68720 0.91377 -0.10774 0.02318  -0.02608 478  GLU A CA    
3644 C C     . GLU A 478 ? 0.92954 0.71244 0.95567 -0.11201 0.02265  -0.02466 478  GLU A C     
3645 O O     . GLU A 478 ? 0.99155 0.76056 1.01451 -0.10778 0.02230  -0.02616 478  GLU A O     
3646 C CB    . GLU A 478 ? 0.84940 0.65030 0.87169 -0.10144 0.02560  -0.01846 478  GLU A CB    
3647 C CG    . GLU A 478 ? 0.87662 0.66908 0.89394 -0.09258 0.02590  -0.01959 478  GLU A CG    
3648 C CD    . GLU A 478 ? 0.87479 0.66480 0.89068 -0.08779 0.02804  -0.01140 478  GLU A CD    
3649 O OE1   . GLU A 478 ? 0.93257 0.72524 0.95064 -0.09165 0.02949  -0.00479 478  GLU A OE1   
3650 O OE2   . GLU A 478 ? 0.79255 0.57828 0.80511 -0.08013 0.02825  -0.01158 478  GLU A OE2   
3651 N N     . ARG A 479 ? 0.92683 0.71429 0.95843 -0.11911 0.02194  -0.02134 479  ARG A N     
3652 C CA    . ARG A 479 ? 0.98382 0.75979 1.01801 -0.12305 0.02030  -0.01999 479  ARG A CA    
3653 C C     . ARG A 479 ? 1.02865 0.80392 1.06514 -0.12800 0.01644  -0.02764 479  ARG A C     
3654 O O     . ARG A 479 ? 1.03699 0.79867 1.07276 -0.12842 0.01443  -0.03024 479  ARG A O     
3655 C CB    . ARG A 479 ? 0.96660 0.74683 1.00571 -0.12798 0.02191  -0.01125 479  ARG A CB    
3656 C CG    . ARG A 479 ? 0.96475 0.76345 1.00848 -0.13243 0.02273  -0.00971 479  ARG A CG    
3657 C CD    . ARG A 479 ? 1.02081 0.82309 1.06866 -0.13617 0.02503  -0.00058 479  ARG A CD    
3658 N NE    . ARG A 479 ? 1.04549 0.86538 1.09881 -0.14076 0.02572  0.00068  479  ARG A NE    
3659 C CZ    . ARG A 479 ? 1.01628 0.84744 1.06917 -0.13898 0.02878  0.00547  479  ARG A CZ    
3660 N NH1   . ARG A 479 ? 0.97313 0.80012 1.02027 -0.13301 0.03130  0.00962  479  ARG A NH1   
3661 N NH2   . ARG A 479 ? 0.99125 0.83836 1.04973 -0.14311 0.02921  0.00609  479  ARG A NH2   
3662 N N     . GLU A 480 ? 1.02694 0.81648 1.06605 -0.13155 0.01511  -0.03134 480  GLU A N     
3663 C CA    . GLU A 480 ? 1.02493 0.81489 1.06555 -0.13571 0.01104  -0.03907 480  GLU A CA    
3664 C C     . GLU A 480 ? 1.04872 0.83508 1.08259 -0.13024 0.00977  -0.04742 480  GLU A C     
3665 O O     . GLU A 480 ? 1.04231 0.82263 1.07095 -0.12329 0.01203  -0.04705 480  GLU A O     
3666 C CB    . GLU A 480 ? 0.99720 0.80465 1.04389 -0.14173 0.00976  -0.03927 480  GLU A CB    
3667 C CG    . GLU A 480 ? 1.02287 0.84263 1.06685 -0.13934 0.00889  -0.04485 480  GLU A CG    
3668 C CD    . GLU A 480 ? 1.07898 0.91578 1.12941 -0.14510 0.00703  -0.04528 480  GLU A CD    
3669 O OE1   . GLU A 480 ? 1.15383 0.99688 1.20320 -0.14577 0.00380  -0.05214 480  GLU A OE1   
3670 O OE2   . GLU A 480 ? 1.05753 0.90168 1.11407 -0.14874 0.00876  -0.03869 480  GLU A OE2   
3671 O O1    . PG4 B .   ? 0.33976 0.34564 0.39389 -0.10904 0.05784  0.03845  601  PG4 A O1    
3672 C C1    . PG4 B .   ? 0.34874 0.35591 0.39631 -0.10474 0.06092  0.04283  601  PG4 A C1    
3673 C C2    . PG4 B .   ? 0.35103 0.34461 0.39263 -0.10594 0.06262  0.04813  601  PG4 A C2    
3674 O O2    . PG4 B .   ? 0.38744 0.36834 0.42509 -0.10346 0.05888  0.04571  601  PG4 A O2    
3675 C C3    . PG4 B .   ? 0.34149 0.31031 0.37223 -0.10237 0.06010  0.05078  601  PG4 A C3    
3676 C C4    . PG4 B .   ? 0.39092 0.35278 0.42499 -0.10980 0.06238  0.05477  601  PG4 A C4    
3677 O O3    . PG4 B .   ? 0.38967 0.34585 0.42912 -0.11375 0.05947  0.05033  601  PG4 A O3    
3678 C C5    . PG4 B .   ? 0.37113 0.31755 0.41245 -0.12017 0.06120  0.05426  601  PG4 A C5    
3679 C C6    . PG4 B .   ? 0.43425 0.37503 0.48164 -0.12506 0.05814  0.04912  601  PG4 A C6    
3680 O O4    . PG4 B .   ? 0.44801 0.40273 0.50335 -0.12826 0.05745  0.04491  601  PG4 A O4    
3681 C C7    . PG4 B .   ? 0.44309 0.39300 0.50457 -0.13380 0.05476  0.04115  601  PG4 A C7    
3682 C C8    . PG4 B .   ? 0.42649 0.39179 0.49651 -0.13671 0.05337  0.03663  601  PG4 A C8    
3683 O O5    . PG4 B .   ? 0.46300 0.43504 0.53038 -0.13086 0.05116  0.03195  601  PG4 A O5    
3684 O O1    . PG4 C .   ? 0.38833 0.43384 0.53602 0.09721  0.00816  0.04142  602  PG4 A O1    
3685 C C1    . PG4 C .   ? 0.47445 0.52280 0.61919 0.09236  0.01250  0.03735  602  PG4 A C1    
3686 C C2    . PG4 C .   ? 0.43679 0.49445 0.59094 0.09703  0.01758  0.03482  602  PG4 A C2    
3687 O O2    . PG4 C .   ? 0.54210 0.60310 0.69342 0.09273  0.02219  0.03099  602  PG4 A O2    
3688 C C3    . PG4 C .   ? 0.51291 0.58521 0.67453 0.09730  0.02631  0.02972  602  PG4 A C3    
3689 C C4    . PG4 C .   ? 0.48124 0.56900 0.65426 0.09707  0.02254  0.03393  602  PG4 A C4    
3690 O O3    . PG4 C .   ? 0.56792 0.66816 0.75216 0.10154  0.02678  0.03300  602  PG4 A O3    
3691 C C5    . PG4 C .   ? 0.54399 0.64980 0.73869 0.10814  0.02394  0.03619  602  PG4 A C5    
3692 C C6    . PG4 C .   ? 0.54293 0.66054 0.74478 0.10466  0.01780  0.04082  602  PG4 A C6    
3693 O O4    . PG4 C .   ? 0.62297 0.74623 0.83519 0.11146  0.01459  0.04411  602  PG4 A O4    
3694 C C7    . PG4 C .   ? 0.59831 0.71647 0.80664 0.10981  0.00714  0.04797  602  PG4 A C7    
3695 C C8    . PG4 C .   ? 0.59358 0.69454 0.79314 0.11401  0.00660  0.04784  602  PG4 A C8    
3696 O O5    . PG4 C .   ? 0.62910 0.72594 0.82449 0.11210  -0.00063 0.05203  602  PG4 A O5    
3701 O O     . HOH D .   ? 0.60955 0.56804 0.49701 0.00252  -0.03468 -0.02189 705  HOH A O     
3704 O O     . HOH D .   ? 0.39298 0.40704 0.45702 -0.11141 0.05152  0.02842  708  HOH A O     
3711 O O     . HOH D .   ? 0.60766 0.58412 0.60453 -0.02811 -0.05286 -0.00118 715  HOH A O     
3755 O O     . HOH D .   ? 0.28103 0.31196 0.28554 -0.01090 0.00921  0.00168  759  HOH A O     
3813 O O     . HOH D .   ? 0.52767 0.49782 0.53498 -0.00265 0.02115  0.00165  817  HOH A O     
3827 O O     . HOH D .   ? 0.52523 0.50815 0.54398 0.06037  -0.05420 0.08993  831  HOH A O     
3907 O O     . HOH D .   ? 0.52411 0.50736 0.43730 0.01606  -0.05159 0.05927  911  HOH A O     
3916 O O     . HOH D .   ? 0.52297 0.46339 0.52364 -0.01991 0.02344  -0.00405 920  HOH A O     
3939 O O     . HOH D .   ? 0.62661 0.44191 0.61403 -0.04096 0.03371  0.05725  943  HOH A O     
3941 O O     . HOH D .   ? 0.57244 0.58687 0.55927 -0.01510 -0.07443 0.01394  945  HOH A O     
3956 O O     . HOH D .   ? 0.54094 0.45692 0.55091 0.06826  -0.03192 0.09851  960  HOH A O     
3959 O O     . HOH D .   ? 0.35241 0.47656 0.50421 0.00616  -0.01860 0.04427  963  HOH A O     
3966 O O     . HOH D .   ? 0.40230 0.45329 0.40234 -0.01383 0.03506  0.00662  970  HOH A O     
4049 O O     . HOH D .   ? 0.60349 0.58079 0.51506 0.02090  -0.05167 0.07034  1053 HOH A O     
# 
