data_8YI6
# 
_entry.id   8YI6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YI6         pdb_00008yi6 10.2210/pdb8yi6/pdb 
WWPDB D_1300045653 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-05 
_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                        8YI6 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              tfujishiro@mail.saitama-u.ac.jp 
_pdbx_contact_author.name_first         Takashi 
_pdbx_contact_author.name_last          Fujishiro 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7967-8380 
# 
_audit_author.name               'Fujishiro, T.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0001-7967-8380 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Structure-guided understanding enzymatic mechanism and substrate specificity of ATP-dependent alkyne-containing dipeptide synthetase BesA
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Otsuka, H.'    1 ?                   
primary 'Gouda, A.'     2 ?                   
primary 'Fujishiro, T.' 3 0000-0001-7967-8380 
# 
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 'L-propargylglycine--L-glutamate ligase' 51673.223 2 6.3.2.- ? ? ? 
2 non-polymer syn ADENINE                                  135.127   2 ?       ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MTDPGSTKILIYAFNYADRMLEEVPYLRYSAERSLCFLGDLRDPGTRLVVITSEAVDPATLDYHLRDVFRFDEPALADVR
RRLTLLTPASRAARPLDSLVLEDEALVETLRRAVAERPAGTIVDFSASPATDELGRRTGATPEEGDHAFVARWGSKSGGK
EICLRAGVAVPGGTSEVLRSEAEVVEAIHRLSCGTAAARRAMVKLDAITWAASIGNVLIDRDKLRHTGDLVGSAEVIRLP
AEEFRRELAEQGAIVEEFLEEITDSPSGLGHIERDGTVRVVACHDQVLSGGQYWGCRFPADERWRPEITDAVRRTGEVLS
GLGHRGAFGVDFVVAGERGLLAVEINLRKVGPSHVVRYAEALVGARVGADGMLRGADGRPVYYTHGRLLEPETLGKLNPR
TAVERLRAEGLLYRHDTGEGVALHVLGALNACGFVELTALARSPEAADGYSRAAQALLTGPYPSAVDLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTDPGSTKILIYAFNYADRMLEEVPYLRYSAERSLCFLGDLRDPGTRLVVITSEAVDPATLDYHLRDVFRFDEPALADVR
RRLTLLTPASRAARPLDSLVLEDEALVETLRRAVAERPAGTIVDFSASPATDELGRRTGATPEEGDHAFVARWGSKSGGK
EICLRAGVAVPGGTSEVLRSEAEVVEAIHRLSCGTAAARRAMVKLDAITWAASIGNVLIDRDKLRHTGDLVGSAEVIRLP
AEEFRRELAEQGAIVEEFLEEITDSPSGLGHIERDGTVRVVACHDQVLSGGQYWGCRFPADERWRPEITDAVRRTGEVLS
GLGHRGAFGVDFVVAGERGLLAVEINLRKVGPSHVVRYAEALVGARVGADGMLRGADGRPVYYTHGRLLEPETLGKLNPR
TAVERLRAEGLLYRHDTGEGVALHVLGALNACGFVELTALARSPEAADGYSRAAQALLTGPYPSAVDLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        ADENINE 
_pdbx_entity_nonpoly.comp_id     ADE 
# 
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   THR n 
1 3   ASP n 
1 4   PRO n 
1 5   GLY n 
1 6   SER n 
1 7   THR n 
1 8   LYS n 
1 9   ILE n 
1 10  LEU n 
1 11  ILE n 
1 12  TYR n 
1 13  ALA n 
1 14  PHE n 
1 15  ASN n 
1 16  TYR n 
1 17  ALA n 
1 18  ASP n 
1 19  ARG n 
1 20  MET n 
1 21  LEU n 
1 22  GLU n 
1 23  GLU n 
1 24  VAL n 
1 25  PRO n 
1 26  TYR n 
1 27  LEU n 
1 28  ARG n 
1 29  TYR n 
1 30  SER n 
1 31  ALA n 
1 32  GLU n 
1 33  ARG n 
1 34  SER n 
1 35  LEU n 
1 36  CYS n 
1 37  PHE n 
1 38  LEU n 
1 39  GLY n 
1 40  ASP n 
1 41  LEU n 
1 42  ARG n 
1 43  ASP n 
1 44  PRO n 
1 45  GLY n 
1 46  THR n 
1 47  ARG n 
1 48  LEU n 
1 49  VAL n 
1 50  VAL n 
1 51  ILE n 
1 52  THR n 
1 53  SER n 
1 54  GLU n 
1 55  ALA n 
1 56  VAL n 
1 57  ASP n 
1 58  PRO n 
1 59  ALA n 
1 60  THR n 
1 61  LEU n 
1 62  ASP n 
1 63  TYR n 
1 64  HIS n 
1 65  LEU n 
1 66  ARG n 
1 67  ASP n 
1 68  VAL n 
1 69  PHE n 
1 70  ARG n 
1 71  PHE n 
1 72  ASP n 
1 73  GLU n 
1 74  PRO n 
1 75  ALA n 
1 76  LEU n 
1 77  ALA n 
1 78  ASP n 
1 79  VAL n 
1 80  ARG n 
1 81  ARG n 
1 82  ARG n 
1 83  LEU n 
1 84  THR n 
1 85  LEU n 
1 86  LEU n 
1 87  THR n 
1 88  PRO n 
1 89  ALA n 
1 90  SER n 
1 91  ARG n 
1 92  ALA n 
1 93  ALA n 
1 94  ARG n 
1 95  PRO n 
1 96  LEU n 
1 97  ASP n 
1 98  SER n 
1 99  LEU n 
1 100 VAL n 
1 101 LEU n 
1 102 GLU n 
1 103 ASP n 
1 104 GLU n 
1 105 ALA n 
1 106 LEU n 
1 107 VAL n 
1 108 GLU n 
1 109 THR n 
1 110 LEU n 
1 111 ARG n 
1 112 ARG n 
1 113 ALA n 
1 114 VAL n 
1 115 ALA n 
1 116 GLU n 
1 117 ARG n 
1 118 PRO n 
1 119 ALA n 
1 120 GLY n 
1 121 THR n 
1 122 ILE n 
1 123 VAL n 
1 124 ASP n 
1 125 PHE n 
1 126 SER n 
1 127 ALA n 
1 128 SER n 
1 129 PRO n 
1 130 ALA n 
1 131 THR n 
1 132 ASP n 
1 133 GLU n 
1 134 LEU n 
1 135 GLY n 
1 136 ARG n 
1 137 ARG n 
1 138 THR n 
1 139 GLY n 
1 140 ALA n 
1 141 THR n 
1 142 PRO n 
1 143 GLU n 
1 144 GLU n 
1 145 GLY n 
1 146 ASP n 
1 147 HIS n 
1 148 ALA n 
1 149 PHE n 
1 150 VAL n 
1 151 ALA n 
1 152 ARG n 
1 153 TRP n 
1 154 GLY n 
1 155 SER n 
1 156 LYS n 
1 157 SER n 
1 158 GLY n 
1 159 GLY n 
1 160 LYS n 
1 161 GLU n 
1 162 ILE n 
1 163 CYS n 
1 164 LEU n 
1 165 ARG n 
1 166 ALA n 
1 167 GLY n 
1 168 VAL n 
1 169 ALA n 
1 170 VAL n 
1 171 PRO n 
1 172 GLY n 
1 173 GLY n 
1 174 THR n 
1 175 SER n 
1 176 GLU n 
1 177 VAL n 
1 178 LEU n 
1 179 ARG n 
1 180 SER n 
1 181 GLU n 
1 182 ALA n 
1 183 GLU n 
1 184 VAL n 
1 185 VAL n 
1 186 GLU n 
1 187 ALA n 
1 188 ILE n 
1 189 HIS n 
1 190 ARG n 
1 191 LEU n 
1 192 SER n 
1 193 CYS n 
1 194 GLY n 
1 195 THR n 
1 196 ALA n 
1 197 ALA n 
1 198 ALA n 
1 199 ARG n 
1 200 ARG n 
1 201 ALA n 
1 202 MET n 
1 203 VAL n 
1 204 LYS n 
1 205 LEU n 
1 206 ASP n 
1 207 ALA n 
1 208 ILE n 
1 209 THR n 
1 210 TRP n 
1 211 ALA n 
1 212 ALA n 
1 213 SER n 
1 214 ILE n 
1 215 GLY n 
1 216 ASN n 
1 217 VAL n 
1 218 LEU n 
1 219 ILE n 
1 220 ASP n 
1 221 ARG n 
1 222 ASP n 
1 223 LYS n 
1 224 LEU n 
1 225 ARG n 
1 226 HIS n 
1 227 THR n 
1 228 GLY n 
1 229 ASP n 
1 230 LEU n 
1 231 VAL n 
1 232 GLY n 
1 233 SER n 
1 234 ALA n 
1 235 GLU n 
1 236 VAL n 
1 237 ILE n 
1 238 ARG n 
1 239 LEU n 
1 240 PRO n 
1 241 ALA n 
1 242 GLU n 
1 243 GLU n 
1 244 PHE n 
1 245 ARG n 
1 246 ARG n 
1 247 GLU n 
1 248 LEU n 
1 249 ALA n 
1 250 GLU n 
1 251 GLN n 
1 252 GLY n 
1 253 ALA n 
1 254 ILE n 
1 255 VAL n 
1 256 GLU n 
1 257 GLU n 
1 258 PHE n 
1 259 LEU n 
1 260 GLU n 
1 261 GLU n 
1 262 ILE n 
1 263 THR n 
1 264 ASP n 
1 265 SER n 
1 266 PRO n 
1 267 SER n 
1 268 GLY n 
1 269 LEU n 
1 270 GLY n 
1 271 HIS n 
1 272 ILE n 
1 273 GLU n 
1 274 ARG n 
1 275 ASP n 
1 276 GLY n 
1 277 THR n 
1 278 VAL n 
1 279 ARG n 
1 280 VAL n 
1 281 VAL n 
1 282 ALA n 
1 283 CYS n 
1 284 HIS n 
1 285 ASP n 
1 286 GLN n 
1 287 VAL n 
1 288 LEU n 
1 289 SER n 
1 290 GLY n 
1 291 GLY n 
1 292 GLN n 
1 293 TYR n 
1 294 TRP n 
1 295 GLY n 
1 296 CYS n 
1 297 ARG n 
1 298 PHE n 
1 299 PRO n 
1 300 ALA n 
1 301 ASP n 
1 302 GLU n 
1 303 ARG n 
1 304 TRP n 
1 305 ARG n 
1 306 PRO n 
1 307 GLU n 
1 308 ILE n 
1 309 THR n 
1 310 ASP n 
1 311 ALA n 
1 312 VAL n 
1 313 ARG n 
1 314 ARG n 
1 315 THR n 
1 316 GLY n 
1 317 GLU n 
1 318 VAL n 
1 319 LEU n 
1 320 SER n 
1 321 GLY n 
1 322 LEU n 
1 323 GLY n 
1 324 HIS n 
1 325 ARG n 
1 326 GLY n 
1 327 ALA n 
1 328 PHE n 
1 329 GLY n 
1 330 VAL n 
1 331 ASP n 
1 332 PHE n 
1 333 VAL n 
1 334 VAL n 
1 335 ALA n 
1 336 GLY n 
1 337 GLU n 
1 338 ARG n 
1 339 GLY n 
1 340 LEU n 
1 341 LEU n 
1 342 ALA n 
1 343 VAL n 
1 344 GLU n 
1 345 ILE n 
1 346 ASN n 
1 347 LEU n 
1 348 ARG n 
1 349 LYS n 
1 350 VAL n 
1 351 GLY n 
1 352 PRO n 
1 353 SER n 
1 354 HIS n 
1 355 VAL n 
1 356 VAL n 
1 357 ARG n 
1 358 TYR n 
1 359 ALA n 
1 360 GLU n 
1 361 ALA n 
1 362 LEU n 
1 363 VAL n 
1 364 GLY n 
1 365 ALA n 
1 366 ARG n 
1 367 VAL n 
1 368 GLY n 
1 369 ALA n 
1 370 ASP n 
1 371 GLY n 
1 372 MET n 
1 373 LEU n 
1 374 ARG n 
1 375 GLY n 
1 376 ALA n 
1 377 ASP n 
1 378 GLY n 
1 379 ARG n 
1 380 PRO n 
1 381 VAL n 
1 382 TYR n 
1 383 TYR n 
1 384 THR n 
1 385 HIS n 
1 386 GLY n 
1 387 ARG n 
1 388 LEU n 
1 389 LEU n 
1 390 GLU n 
1 391 PRO n 
1 392 GLU n 
1 393 THR n 
1 394 LEU n 
1 395 GLY n 
1 396 LYS n 
1 397 LEU n 
1 398 ASN n 
1 399 PRO n 
1 400 ARG n 
1 401 THR n 
1 402 ALA n 
1 403 VAL n 
1 404 GLU n 
1 405 ARG n 
1 406 LEU n 
1 407 ARG n 
1 408 ALA n 
1 409 GLU n 
1 410 GLY n 
1 411 LEU n 
1 412 LEU n 
1 413 TYR n 
1 414 ARG n 
1 415 HIS n 
1 416 ASP n 
1 417 THR n 
1 418 GLY n 
1 419 GLU n 
1 420 GLY n 
1 421 VAL n 
1 422 ALA n 
1 423 LEU n 
1 424 HIS n 
1 425 VAL n 
1 426 LEU n 
1 427 GLY n 
1 428 ALA n 
1 429 LEU n 
1 430 ASN n 
1 431 ALA n 
1 432 CYS n 
1 433 GLY n 
1 434 PHE n 
1 435 VAL n 
1 436 GLU n 
1 437 LEU n 
1 438 THR n 
1 439 ALA n 
1 440 LEU n 
1 441 ALA n 
1 442 ARG n 
1 443 SER n 
1 444 PRO n 
1 445 GLU n 
1 446 ALA n 
1 447 ALA n 
1 448 ASP n 
1 449 GLY n 
1 450 TYR n 
1 451 SER n 
1 452 ARG n 
1 453 ALA n 
1 454 ALA n 
1 455 GLN n 
1 456 ALA n 
1 457 LEU n 
1 458 LEU n 
1 459 THR n 
1 460 GLY n 
1 461 PRO n 
1 462 TYR n 
1 463 PRO n 
1 464 SER n 
1 465 ALA n 
1 466 VAL n 
1 467 ASP n 
1 468 LEU n 
1 469 GLU n 
1 470 HIS n 
1 471 HIS n 
1 472 HIS n 
1 473 HIS n 
1 474 HIS n 
1 475 HIS 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                   475 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'besA, SCATT_p06910' 
_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      'Streptantibioticus cattleyicolor' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     29303 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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              C41 
_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 
ADE non-polymer         . ADENINE         ? 'C5 H5 N5'       135.127 
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 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   ASP 3   3   ?   ?   ?   A . n 
A 1 4   PRO 4   4   ?   ?   ?   A . n 
A 1 5   GLY 5   5   5   GLY GLY A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   THR 7   7   7   THR THR A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  TYR 12  12  12  TYR TYR A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  PHE 14  14  14  PHE PHE A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  TYR 16  16  16  TYR TYR A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  MET 20  20  20  MET MET A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  TYR 26  26  26  TYR TYR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  SER 30  30  30  SER SER A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  CYS 36  36  36  CYS CYS A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  THR 46  46  46  THR THR A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  PHE 69  69  69  PHE PHE A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  PHE 71  71  71  PHE PHE A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  PRO 88  88  88  PRO PRO A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  ARG 94  94  94  ARG ARG A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 PHE 125 125 125 PHE PHE A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 HIS 147 147 147 HIS HIS A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 TRP 153 153 153 TRP TRP A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 CYS 163 163 163 CYS CYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 PRO 171 171 171 PRO PRO A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 GLU 176 176 176 GLU GLU A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 HIS 189 189 189 HIS HIS A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 CYS 193 193 193 CYS CYS A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 THR 195 195 195 THR THR A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 ARG 199 199 199 ARG ARG A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 MET 202 202 202 MET MET A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ASP 206 206 206 ASP ASP A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 TRP 210 210 210 TRP TRP A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 ILE 214 214 214 ILE ILE A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 HIS 226 226 226 HIS HIS A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 ILE 237 237 237 ILE ILE A . n 
A 1 238 ARG 238 238 238 ARG ARG A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 ARG 246 246 246 ARG ARG A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 GLU 250 250 250 GLU GLU A . n 
A 1 251 GLN 251 251 251 GLN GLN A . n 
A 1 252 GLY 252 252 252 GLY GLY A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 ILE 254 254 254 ILE ILE A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 GLU 260 260 260 GLU GLU A . n 
A 1 261 GLU 261 261 261 GLU GLU A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 THR 263 263 263 THR THR A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 PRO 266 266 266 PRO PRO A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 HIS 271 271 271 HIS HIS A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 ARG 274 274 274 ARG ARG A . n 
A 1 275 ASP 275 275 275 ASP ASP A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 VAL 278 278 278 VAL VAL A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 VAL 281 281 281 VAL VAL A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 CYS 283 283 283 CYS CYS A . n 
A 1 284 HIS 284 284 284 HIS HIS A . n 
A 1 285 ASP 285 285 285 ASP ASP A . n 
A 1 286 GLN 286 286 286 GLN GLN A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 GLY 290 290 290 GLY GLY A . n 
A 1 291 GLY 291 291 291 GLY GLY A . n 
A 1 292 GLN 292 292 292 GLN GLN A . n 
A 1 293 TYR 293 293 293 TYR TYR A . n 
A 1 294 TRP 294 294 294 TRP TRP A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 CYS 296 296 296 CYS CYS A . n 
A 1 297 ARG 297 297 297 ARG ARG A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 ALA 300 300 300 ALA ALA A . n 
A 1 301 ASP 301 301 301 ASP ASP A . n 
A 1 302 GLU 302 302 302 GLU GLU A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 TRP 304 304 304 TRP TRP A . n 
A 1 305 ARG 305 305 305 ARG ARG A . n 
A 1 306 PRO 306 306 306 PRO PRO A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 ILE 308 308 308 ILE ILE A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 ALA 311 311 311 ALA ALA A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 ARG 313 313 313 ARG ARG A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 THR 315 315 315 THR THR A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 GLU 317 317 317 GLU GLU A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 SER 320 320 320 SER SER A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 HIS 324 324 324 HIS HIS A . n 
A 1 325 ARG 325 325 325 ARG ARG A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 ALA 327 327 327 ALA ALA A . n 
A 1 328 PHE 328 328 328 PHE PHE A . n 
A 1 329 GLY 329 329 329 GLY GLY A . n 
A 1 330 VAL 330 330 330 VAL VAL A . n 
A 1 331 ASP 331 331 331 ASP ASP A . n 
A 1 332 PHE 332 332 332 PHE PHE A . n 
A 1 333 VAL 333 333 333 VAL VAL A . n 
A 1 334 VAL 334 334 334 VAL VAL A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 GLY 336 336 336 GLY GLY A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 ARG 338 338 338 ARG ARG A . n 
A 1 339 GLY 339 339 339 GLY GLY A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 VAL 343 343 343 VAL VAL A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 ASN 346 346 346 ASN ASN A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 ARG 348 348 348 ARG ARG A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 GLY 351 351 351 GLY GLY A . n 
A 1 352 PRO 352 352 352 PRO PRO A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 HIS 354 354 354 HIS HIS A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 VAL 356 356 356 VAL VAL A . n 
A 1 357 ARG 357 357 357 ARG ARG A . n 
A 1 358 TYR 358 358 358 TYR TYR A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 GLU 360 360 360 GLU GLU A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 ALA 365 365 365 ALA ALA A . n 
A 1 366 ARG 366 366 366 ARG ARG A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 ASP 370 370 370 ASP ASP A . n 
A 1 371 GLY 371 371 371 GLY GLY A . n 
A 1 372 MET 372 372 372 MET MET A . n 
A 1 373 LEU 373 373 373 LEU LEU A . n 
A 1 374 ARG 374 374 374 ARG ARG A . n 
A 1 375 GLY 375 375 375 GLY GLY A . n 
A 1 376 ALA 376 376 376 ALA ALA A . n 
A 1 377 ASP 377 377 377 ASP ASP A . n 
A 1 378 GLY 378 378 378 GLY GLY A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 PRO 380 380 380 PRO PRO A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 TYR 382 382 382 TYR TYR A . n 
A 1 383 TYR 383 383 383 TYR TYR A . n 
A 1 384 THR 384 384 384 THR THR A . n 
A 1 385 HIS 385 385 385 HIS HIS A . n 
A 1 386 GLY 386 386 386 GLY GLY A . n 
A 1 387 ARG 387 387 387 ARG ARG A . n 
A 1 388 LEU 388 388 388 LEU LEU A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 PRO 391 391 391 PRO PRO A . n 
A 1 392 GLU 392 392 392 GLU GLU A . n 
A 1 393 THR 393 393 393 THR THR A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 GLY 395 395 395 GLY GLY A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 LEU 397 397 397 LEU LEU A . n 
A 1 398 ASN 398 398 398 ASN ASN A . n 
A 1 399 PRO 399 399 399 PRO PRO A . n 
A 1 400 ARG 400 400 400 ARG ARG A . n 
A 1 401 THR 401 401 401 THR THR A . n 
A 1 402 ALA 402 402 402 ALA ALA A . n 
A 1 403 VAL 403 403 403 VAL VAL A . n 
A 1 404 GLU 404 404 404 GLU GLU A . n 
A 1 405 ARG 405 405 405 ARG ARG A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 ARG 407 407 407 ARG ARG A . n 
A 1 408 ALA 408 408 408 ALA ALA A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 TYR 413 413 413 TYR TYR A . n 
A 1 414 ARG 414 414 414 ARG ARG A . n 
A 1 415 HIS 415 415 415 HIS HIS A . n 
A 1 416 ASP 416 416 416 ASP ASP A . n 
A 1 417 THR 417 417 417 THR THR A . n 
A 1 418 GLY 418 418 418 GLY GLY A . n 
A 1 419 GLU 419 419 419 GLU GLU A . n 
A 1 420 GLY 420 420 420 GLY GLY A . n 
A 1 421 VAL 421 421 421 VAL VAL 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 HIS 424 424 424 HIS HIS A . n 
A 1 425 VAL 425 425 425 VAL VAL A . n 
A 1 426 LEU 426 426 426 LEU LEU A . n 
A 1 427 GLY 427 427 427 GLY GLY A . n 
A 1 428 ALA 428 428 428 ALA ALA A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 ASN 430 430 430 ASN ASN A . n 
A 1 431 ALA 431 431 431 ALA ALA A . n 
A 1 432 CYS 432 432 432 CYS CYS A . n 
A 1 433 GLY 433 433 433 GLY GLY A . n 
A 1 434 PHE 434 434 434 PHE PHE A . n 
A 1 435 VAL 435 435 435 VAL VAL A . n 
A 1 436 GLU 436 436 436 GLU GLU A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 ALA 439 439 439 ALA ALA A . n 
A 1 440 LEU 440 440 440 LEU LEU A . n 
A 1 441 ALA 441 441 441 ALA ALA A . n 
A 1 442 ARG 442 442 442 ARG ARG A . n 
A 1 443 SER 443 443 443 SER SER A . n 
A 1 444 PRO 444 444 444 PRO PRO A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 ALA 446 446 446 ALA ALA A . n 
A 1 447 ALA 447 447 447 ALA ALA A . n 
A 1 448 ASP 448 448 448 ASP ASP A . n 
A 1 449 GLY 449 449 449 GLY GLY A . n 
A 1 450 TYR 450 450 450 TYR TYR A . n 
A 1 451 SER 451 451 451 SER SER A . n 
A 1 452 ARG 452 452 452 ARG ARG A . n 
A 1 453 ALA 453 453 453 ALA ALA A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 GLN 455 455 455 GLN GLN A . n 
A 1 456 ALA 456 456 456 ALA ALA A . n 
A 1 457 LEU 457 457 457 LEU LEU A . n 
A 1 458 LEU 458 458 458 LEU LEU A . n 
A 1 459 THR 459 459 459 THR THR A . n 
A 1 460 GLY 460 460 460 GLY GLY A . n 
A 1 461 PRO 461 461 461 PRO PRO A . n 
A 1 462 TYR 462 462 462 TYR TYR A . n 
A 1 463 PRO 463 463 ?   ?   ?   A . n 
A 1 464 SER 464 464 ?   ?   ?   A . n 
A 1 465 ALA 465 465 ?   ?   ?   A . n 
A 1 466 VAL 466 466 ?   ?   ?   A . n 
A 1 467 ASP 467 467 ?   ?   ?   A . n 
A 1 468 LEU 468 468 ?   ?   ?   A . n 
A 1 469 GLU 469 469 ?   ?   ?   A . n 
A 1 470 HIS 470 470 ?   ?   ?   A . n 
A 1 471 HIS 471 471 ?   ?   ?   A . n 
A 1 472 HIS 472 472 ?   ?   ?   A . n 
A 1 473 HIS 473 473 ?   ?   ?   A . n 
A 1 474 HIS 474 474 ?   ?   ?   A . n 
A 1 475 HIS 475 475 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   ASP 3   3   ?   ?   ?   B . n 
B 1 4   PRO 4   4   ?   ?   ?   B . n 
B 1 5   GLY 5   5   5   GLY GLY B . n 
B 1 6   SER 6   6   6   SER SER B . n 
B 1 7   THR 7   7   7   THR THR B . n 
B 1 8   LYS 8   8   8   LYS LYS B . n 
B 1 9   ILE 9   9   9   ILE ILE B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  ILE 11  11  11  ILE ILE B . n 
B 1 12  TYR 12  12  12  TYR TYR B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  PHE 14  14  14  PHE PHE B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  TYR 16  16  16  TYR TYR B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  ASP 18  18  18  ASP ASP B . n 
B 1 19  ARG 19  19  19  ARG ARG B . n 
B 1 20  MET 20  20  20  MET MET B . n 
B 1 21  LEU 21  21  21  LEU LEU B . n 
B 1 22  GLU 22  22  22  GLU GLU B . n 
B 1 23  GLU 23  23  23  GLU GLU B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  TYR 26  26  26  TYR TYR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ARG 28  28  28  ARG ARG B . n 
B 1 29  TYR 29  29  29  TYR TYR B . n 
B 1 30  SER 30  30  30  SER SER B . n 
B 1 31  ALA 31  31  31  ALA ALA B . n 
B 1 32  GLU 32  32  32  GLU GLU B . n 
B 1 33  ARG 33  33  33  ARG ARG B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  CYS 36  36  36  CYS CYS B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  GLY 39  39  39  GLY GLY B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  LEU 41  41  41  LEU LEU B . n 
B 1 42  ARG 42  42  42  ARG ARG B . n 
B 1 43  ASP 43  43  43  ASP ASP B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  THR 46  46  46  THR THR B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  LEU 48  48  48  LEU LEU B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  VAL 50  50  50  VAL VAL B . n 
B 1 51  ILE 51  51  51  ILE ILE B . n 
B 1 52  THR 52  52  52  THR THR B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  ASP 57  57  57  ASP ASP B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  TYR 63  63  63  TYR TYR B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  LEU 65  65  65  LEU LEU B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  PHE 69  69  69  PHE PHE B . n 
B 1 70  ARG 70  70  70  ARG ARG B . n 
B 1 71  PHE 71  71  71  PHE PHE B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  GLU 73  73  73  GLU GLU B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  ASP 78  78  78  ASP ASP B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  ARG 80  80  80  ARG ARG B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  ARG 82  82  82  ARG ARG B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  PRO 88  88  88  PRO PRO B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  SER 90  90  90  SER SER B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  ARG 94  94  94  ARG ARG B . n 
B 1 95  PRO 95  95  95  PRO PRO B . n 
B 1 96  LEU 96  96  96  LEU LEU B . n 
B 1 97  ASP 97  97  97  ASP ASP B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 GLU 108 108 108 GLU GLU B . n 
B 1 109 THR 109 109 109 THR THR B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 ARG 111 111 111 ARG ARG B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 PRO 118 118 118 PRO PRO B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 THR 121 121 121 THR THR B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 PHE 125 125 125 PHE PHE B . n 
B 1 126 SER 126 126 126 SER SER B . n 
B 1 127 ALA 127 127 127 ALA ALA B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 PRO 129 129 129 PRO PRO B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 ASP 132 132 132 ASP ASP B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 LEU 134 134 134 LEU LEU B . n 
B 1 135 GLY 135 135 135 GLY GLY B . n 
B 1 136 ARG 136 136 136 ARG ARG B . n 
B 1 137 ARG 137 137 137 ARG ARG B . n 
B 1 138 THR 138 138 138 THR THR B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 THR 141 141 141 THR THR B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 GLU 143 143 143 GLU GLU B . n 
B 1 144 GLU 144 144 144 GLU GLU B . n 
B 1 145 GLY 145 145 145 GLY GLY B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 HIS 147 147 147 HIS HIS B . n 
B 1 148 ALA 148 148 148 ALA ALA B . n 
B 1 149 PHE 149 149 149 PHE PHE B . n 
B 1 150 VAL 150 150 150 VAL VAL B . n 
B 1 151 ALA 151 151 151 ALA ALA B . n 
B 1 152 ARG 152 152 152 ARG ARG B . n 
B 1 153 TRP 153 153 153 TRP TRP B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 LYS 156 156 156 LYS LYS B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 GLY 158 158 158 GLY GLY B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 LYS 160 160 160 LYS LYS B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 ILE 162 162 162 ILE ILE B . n 
B 1 163 CYS 163 163 163 CYS CYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 ARG 165 165 165 ARG ARG B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 GLY 167 167 167 GLY GLY B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 ALA 169 169 169 ALA ALA B . n 
B 1 170 VAL 170 170 170 VAL VAL B . n 
B 1 171 PRO 171 171 171 PRO PRO B . n 
B 1 172 GLY 172 172 172 GLY GLY B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 THR 174 174 174 THR THR B . n 
B 1 175 SER 175 175 175 SER SER B . n 
B 1 176 GLU 176 176 176 GLU GLU B . n 
B 1 177 VAL 177 177 177 VAL VAL B . n 
B 1 178 LEU 178 178 178 LEU LEU B . n 
B 1 179 ARG 179 179 179 ARG ARG B . n 
B 1 180 SER 180 180 180 SER SER B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 VAL 184 184 184 VAL VAL B . n 
B 1 185 VAL 185 185 185 VAL VAL B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 ALA 187 187 187 ALA ALA B . n 
B 1 188 ILE 188 188 188 ILE ILE B . n 
B 1 189 HIS 189 189 189 HIS HIS B . n 
B 1 190 ARG 190 190 190 ARG ARG B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 SER 192 192 192 SER SER B . n 
B 1 193 CYS 193 193 193 CYS CYS B . n 
B 1 194 GLY 194 194 194 GLY GLY B . n 
B 1 195 THR 195 195 195 THR THR B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 ALA 198 198 198 ALA ALA B . n 
B 1 199 ARG 199 199 199 ARG ARG B . n 
B 1 200 ARG 200 200 200 ARG ARG B . n 
B 1 201 ALA 201 201 201 ALA ALA B . n 
B 1 202 MET 202 202 202 MET MET B . n 
B 1 203 VAL 203 203 203 VAL VAL B . n 
B 1 204 LYS 204 204 204 LYS LYS B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ASP 206 206 206 ASP ASP B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 ILE 208 208 208 ILE ILE B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 TRP 210 210 210 TRP TRP B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 SER 213 213 213 SER SER B . n 
B 1 214 ILE 214 214 214 ILE ILE B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 ARG 221 221 221 ARG ARG B . n 
B 1 222 ASP 222 222 222 ASP ASP B . n 
B 1 223 LYS 223 223 223 LYS LYS B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 ARG 225 225 225 ARG ARG B . n 
B 1 226 HIS 226 226 226 HIS HIS B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 GLY 228 228 228 GLY GLY B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 VAL 231 231 231 VAL VAL B . n 
B 1 232 GLY 232 232 232 GLY GLY B . n 
B 1 233 SER 233 233 233 SER SER B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 VAL 236 236 236 VAL VAL B . n 
B 1 237 ILE 237 237 237 ILE ILE B . n 
B 1 238 ARG 238 238 238 ARG ARG B . n 
B 1 239 LEU 239 239 239 LEU LEU B . n 
B 1 240 PRO 240 240 240 PRO PRO B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 GLU 242 242 242 GLU GLU B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 PHE 244 244 244 PHE PHE B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 ARG 246 246 246 ARG ARG B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 ALA 249 249 249 ALA ALA B . n 
B 1 250 GLU 250 250 250 GLU GLU B . n 
B 1 251 GLN 251 251 251 GLN GLN B . n 
B 1 252 GLY 252 252 252 GLY GLY B . n 
B 1 253 ALA 253 253 253 ALA ALA B . n 
B 1 254 ILE 254 254 254 ILE ILE B . n 
B 1 255 VAL 255 255 255 VAL VAL B . n 
B 1 256 GLU 256 256 256 GLU GLU B . n 
B 1 257 GLU 257 257 257 GLU GLU B . n 
B 1 258 PHE 258 258 258 PHE PHE B . n 
B 1 259 LEU 259 259 259 LEU LEU B . n 
B 1 260 GLU 260 260 260 GLU GLU B . n 
B 1 261 GLU 261 261 261 GLU GLU B . n 
B 1 262 ILE 262 262 262 ILE ILE B . n 
B 1 263 THR 263 263 263 THR THR B . n 
B 1 264 ASP 264 264 264 ASP ASP B . n 
B 1 265 SER 265 265 265 SER SER B . n 
B 1 266 PRO 266 266 266 PRO PRO B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 GLY 268 268 268 GLY GLY B . n 
B 1 269 LEU 269 269 269 LEU LEU B . n 
B 1 270 GLY 270 270 270 GLY GLY B . n 
B 1 271 HIS 271 271 271 HIS HIS B . n 
B 1 272 ILE 272 272 272 ILE ILE B . n 
B 1 273 GLU 273 273 273 GLU GLU B . n 
B 1 274 ARG 274 274 274 ARG ARG B . n 
B 1 275 ASP 275 275 275 ASP ASP B . n 
B 1 276 GLY 276 276 276 GLY GLY B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 VAL 278 278 278 VAL VAL B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 VAL 280 280 280 VAL VAL B . n 
B 1 281 VAL 281 281 281 VAL VAL B . n 
B 1 282 ALA 282 282 282 ALA ALA B . n 
B 1 283 CYS 283 283 283 CYS CYS B . n 
B 1 284 HIS 284 284 284 HIS HIS B . n 
B 1 285 ASP 285 285 285 ASP ASP B . n 
B 1 286 GLN 286 286 286 GLN GLN B . n 
B 1 287 VAL 287 287 287 VAL VAL B . n 
B 1 288 LEU 288 288 288 LEU LEU B . n 
B 1 289 SER 289 289 289 SER SER B . n 
B 1 290 GLY 290 290 290 GLY GLY B . n 
B 1 291 GLY 291 291 291 GLY GLY B . n 
B 1 292 GLN 292 292 292 GLN GLN B . n 
B 1 293 TYR 293 293 293 TYR TYR B . n 
B 1 294 TRP 294 294 294 TRP TRP B . n 
B 1 295 GLY 295 295 295 GLY GLY B . n 
B 1 296 CYS 296 296 296 CYS CYS B . n 
B 1 297 ARG 297 297 297 ARG ARG B . n 
B 1 298 PHE 298 298 298 PHE PHE B . n 
B 1 299 PRO 299 299 299 PRO PRO B . n 
B 1 300 ALA 300 300 300 ALA ALA B . n 
B 1 301 ASP 301 301 301 ASP ASP B . n 
B 1 302 GLU 302 302 302 GLU GLU B . n 
B 1 303 ARG 303 303 303 ARG ARG B . n 
B 1 304 TRP 304 304 304 TRP TRP B . n 
B 1 305 ARG 305 305 305 ARG ARG B . n 
B 1 306 PRO 306 306 306 PRO PRO B . n 
B 1 307 GLU 307 307 307 GLU GLU B . n 
B 1 308 ILE 308 308 308 ILE ILE B . n 
B 1 309 THR 309 309 309 THR THR B . n 
B 1 310 ASP 310 310 310 ASP ASP B . n 
B 1 311 ALA 311 311 311 ALA ALA B . n 
B 1 312 VAL 312 312 312 VAL VAL B . n 
B 1 313 ARG 313 313 313 ARG ARG B . n 
B 1 314 ARG 314 314 314 ARG ARG B . n 
B 1 315 THR 315 315 315 THR THR B . n 
B 1 316 GLY 316 316 316 GLY GLY B . n 
B 1 317 GLU 317 317 317 GLU GLU B . n 
B 1 318 VAL 318 318 318 VAL VAL B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 SER 320 320 320 SER SER B . n 
B 1 321 GLY 321 321 321 GLY GLY B . n 
B 1 322 LEU 322 322 322 LEU LEU B . n 
B 1 323 GLY 323 323 323 GLY GLY B . n 
B 1 324 HIS 324 324 324 HIS HIS B . n 
B 1 325 ARG 325 325 325 ARG ARG B . n 
B 1 326 GLY 326 326 326 GLY GLY B . n 
B 1 327 ALA 327 327 327 ALA ALA B . n 
B 1 328 PHE 328 328 328 PHE PHE B . n 
B 1 329 GLY 329 329 329 GLY GLY B . n 
B 1 330 VAL 330 330 330 VAL VAL B . n 
B 1 331 ASP 331 331 331 ASP ASP B . n 
B 1 332 PHE 332 332 332 PHE PHE B . n 
B 1 333 VAL 333 333 333 VAL VAL B . n 
B 1 334 VAL 334 334 334 VAL VAL B . n 
B 1 335 ALA 335 335 335 ALA ALA B . n 
B 1 336 GLY 336 336 336 GLY GLY B . n 
B 1 337 GLU 337 337 337 GLU GLU B . n 
B 1 338 ARG 338 338 338 ARG ARG B . n 
B 1 339 GLY 339 339 339 GLY GLY B . n 
B 1 340 LEU 340 340 340 LEU LEU B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 ALA 342 342 342 ALA ALA B . n 
B 1 343 VAL 343 343 343 VAL VAL B . n 
B 1 344 GLU 344 344 344 GLU GLU B . n 
B 1 345 ILE 345 345 345 ILE ILE B . n 
B 1 346 ASN 346 346 346 ASN ASN B . n 
B 1 347 LEU 347 347 347 LEU LEU B . n 
B 1 348 ARG 348 348 348 ARG ARG B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 VAL 350 350 350 VAL VAL B . n 
B 1 351 GLY 351 351 351 GLY GLY B . n 
B 1 352 PRO 352 352 352 PRO PRO B . n 
B 1 353 SER 353 353 353 SER SER B . n 
B 1 354 HIS 354 354 354 HIS HIS B . n 
B 1 355 VAL 355 355 355 VAL VAL B . n 
B 1 356 VAL 356 356 356 VAL VAL B . n 
B 1 357 ARG 357 357 357 ARG ARG B . n 
B 1 358 TYR 358 358 358 TYR TYR B . n 
B 1 359 ALA 359 359 359 ALA ALA B . n 
B 1 360 GLU 360 360 360 GLU GLU B . n 
B 1 361 ALA 361 361 361 ALA ALA B . n 
B 1 362 LEU 362 362 362 LEU LEU B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 ALA 365 365 365 ALA ALA B . n 
B 1 366 ARG 366 366 366 ARG ARG B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 GLY 368 368 368 GLY GLY B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 ASP 370 370 370 ASP ASP B . n 
B 1 371 GLY 371 371 371 GLY GLY B . n 
B 1 372 MET 372 372 372 MET MET B . n 
B 1 373 LEU 373 373 373 LEU LEU B . n 
B 1 374 ARG 374 374 374 ARG ARG B . n 
B 1 375 GLY 375 375 375 GLY GLY B . n 
B 1 376 ALA 376 376 376 ALA ALA B . n 
B 1 377 ASP 377 377 377 ASP ASP B . n 
B 1 378 GLY 378 378 378 GLY GLY B . n 
B 1 379 ARG 379 379 379 ARG ARG B . n 
B 1 380 PRO 380 380 380 PRO PRO B . n 
B 1 381 VAL 381 381 381 VAL VAL B . n 
B 1 382 TYR 382 382 382 TYR TYR B . n 
B 1 383 TYR 383 383 383 TYR TYR B . n 
B 1 384 THR 384 384 384 THR THR B . n 
B 1 385 HIS 385 385 385 HIS HIS B . n 
B 1 386 GLY 386 386 386 GLY GLY B . n 
B 1 387 ARG 387 387 387 ARG ARG B . n 
B 1 388 LEU 388 388 388 LEU LEU B . n 
B 1 389 LEU 389 389 389 LEU LEU B . n 
B 1 390 GLU 390 390 390 GLU GLU B . n 
B 1 391 PRO 391 391 391 PRO PRO B . n 
B 1 392 GLU 392 392 392 GLU GLU B . n 
B 1 393 THR 393 393 393 THR THR B . n 
B 1 394 LEU 394 394 394 LEU LEU B . n 
B 1 395 GLY 395 395 395 GLY GLY B . n 
B 1 396 LYS 396 396 396 LYS LYS B . n 
B 1 397 LEU 397 397 397 LEU LEU B . n 
B 1 398 ASN 398 398 398 ASN ASN B . n 
B 1 399 PRO 399 399 399 PRO PRO B . n 
B 1 400 ARG 400 400 400 ARG ARG B . n 
B 1 401 THR 401 401 401 THR THR B . n 
B 1 402 ALA 402 402 402 ALA ALA B . n 
B 1 403 VAL 403 403 403 VAL VAL B . n 
B 1 404 GLU 404 404 404 GLU GLU B . n 
B 1 405 ARG 405 405 405 ARG ARG B . n 
B 1 406 LEU 406 406 406 LEU LEU B . n 
B 1 407 ARG 407 407 407 ARG ARG B . n 
B 1 408 ALA 408 408 408 ALA ALA B . n 
B 1 409 GLU 409 409 409 GLU GLU B . n 
B 1 410 GLY 410 410 410 GLY GLY B . n 
B 1 411 LEU 411 411 411 LEU LEU B . n 
B 1 412 LEU 412 412 412 LEU LEU B . n 
B 1 413 TYR 413 413 413 TYR TYR B . n 
B 1 414 ARG 414 414 414 ARG ARG B . n 
B 1 415 HIS 415 415 415 HIS HIS B . n 
B 1 416 ASP 416 416 416 ASP ASP B . n 
B 1 417 THR 417 417 417 THR THR B . n 
B 1 418 GLY 418 418 418 GLY GLY B . n 
B 1 419 GLU 419 419 419 GLU GLU B . n 
B 1 420 GLY 420 420 420 GLY GLY B . n 
B 1 421 VAL 421 421 421 VAL VAL B . n 
B 1 422 ALA 422 422 422 ALA ALA B . n 
B 1 423 LEU 423 423 423 LEU LEU B . n 
B 1 424 HIS 424 424 424 HIS HIS B . n 
B 1 425 VAL 425 425 425 VAL VAL B . n 
B 1 426 LEU 426 426 426 LEU LEU B . n 
B 1 427 GLY 427 427 427 GLY GLY B . n 
B 1 428 ALA 428 428 428 ALA ALA B . n 
B 1 429 LEU 429 429 429 LEU LEU B . n 
B 1 430 ASN 430 430 430 ASN ASN B . n 
B 1 431 ALA 431 431 431 ALA ALA B . n 
B 1 432 CYS 432 432 432 CYS CYS B . n 
B 1 433 GLY 433 433 433 GLY GLY B . n 
B 1 434 PHE 434 434 434 PHE PHE B . n 
B 1 435 VAL 435 435 435 VAL VAL B . n 
B 1 436 GLU 436 436 436 GLU GLU B . n 
B 1 437 LEU 437 437 437 LEU LEU B . n 
B 1 438 THR 438 438 438 THR THR B . n 
B 1 439 ALA 439 439 439 ALA ALA B . n 
B 1 440 LEU 440 440 440 LEU LEU B . n 
B 1 441 ALA 441 441 441 ALA ALA B . n 
B 1 442 ARG 442 442 442 ARG ARG B . n 
B 1 443 SER 443 443 443 SER SER B . n 
B 1 444 PRO 444 444 444 PRO PRO B . n 
B 1 445 GLU 445 445 445 GLU GLU B . n 
B 1 446 ALA 446 446 446 ALA ALA B . n 
B 1 447 ALA 447 447 447 ALA ALA B . n 
B 1 448 ASP 448 448 448 ASP ASP B . n 
B 1 449 GLY 449 449 449 GLY GLY B . n 
B 1 450 TYR 450 450 450 TYR TYR B . n 
B 1 451 SER 451 451 451 SER SER B . n 
B 1 452 ARG 452 452 452 ARG ARG B . n 
B 1 453 ALA 453 453 453 ALA ALA B . n 
B 1 454 ALA 454 454 454 ALA ALA B . n 
B 1 455 GLN 455 455 455 GLN GLN B . n 
B 1 456 ALA 456 456 456 ALA ALA B . n 
B 1 457 LEU 457 457 457 LEU LEU B . n 
B 1 458 LEU 458 458 458 LEU LEU B . n 
B 1 459 THR 459 459 459 THR THR B . n 
B 1 460 GLY 460 460 460 GLY GLY B . n 
B 1 461 PRO 461 461 461 PRO PRO B . n 
B 1 462 TYR 462 462 462 TYR TYR B . n 
B 1 463 PRO 463 463 ?   ?   ?   B . n 
B 1 464 SER 464 464 ?   ?   ?   B . n 
B 1 465 ALA 465 465 ?   ?   ?   B . n 
B 1 466 VAL 466 466 ?   ?   ?   B . n 
B 1 467 ASP 467 467 ?   ?   ?   B . n 
B 1 468 LEU 468 468 ?   ?   ?   B . n 
B 1 469 GLU 469 469 ?   ?   ?   B . n 
B 1 470 HIS 470 470 ?   ?   ?   B . n 
B 1 471 HIS 471 471 ?   ?   ?   B . n 
B 1 472 HIS 472 472 ?   ?   ?   B . n 
B 1 473 HIS 473 473 ?   ?   ?   B . n 
B 1 474 HIS 474 474 ?   ?   ?   B . n 
B 1 475 HIS 475 475 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ADE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ADE 
_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 
C 2 ADE 1 501 1 ADE ADE A . 
D 2 ADE 1 501 1 ADE ADE B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 2.8.3    3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YI6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     138.680 
_cell.length_a_esd                 ? 
_cell.length_b                     138.680 
_cell.length_b_esd                 ? 
_cell.length_c                     144.980 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         8YI6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                94 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 42 21 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                   8YI6 
_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             3.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.53 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.2 M lithium sulfate, 50% (v/v) PEG 400, 0.1 M sodium acetate, 5 mM ATP, 4 mM L-glutamic acid, 4 mM L-propargylglycine' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-02 
_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                    'Cryo-cooled channel-cut Si(111)' 
_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   2.700 
_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                        'PHOTON FACTORY BEAMLINE BL-1A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        2.700 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL-1A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YI6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.6 
_reflns.d_resolution_low                               46.45 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     16959 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.32 
_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                                0.105 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.099 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
3.60  3.7   ? ? ? ? ? ? 1311 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.855 ? ? 1 1 0.7190000000000001 ? ? ? ? 1.745              ? ? ? ? ? ? 
? ? ? 
3.70  3.8   ? ? ? ? ? ? 1170 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.271 ? ? 2 1 0.752              ? ? ? ? 1.196              ? ? ? ? ? ? 
? ? ? 
3.80  3.9   ? ? ? ? ? ? 1054 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.892 ? ? 3 1 0.88               ? ? ? ? 0.8390000000000001 ? ? ? ? ? ? 
? ? ? 
3.90  4.0   ? ? ? ? ? ? 959  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.644 ? ? 4 1 0.9259999999999999 ? ? ? ? 0.606              ? ? ? ? ? ? 
? ? ? 
4.00  6.0   ? ? ? ? ? ? 8621 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.195 ? ? 5 1 0.992              ? ? ? ? 0.183              ? ? ? ? ? ? 
? ? ? 
6.00  10.0  ? ? ? ? ? ? 2962 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.047 ? ? 6 1 0.9990000000000001 ? ? ? ? 0.045              ? ? ? ? ? ? 
? ? ? 
10.00 46.45 ? ? ? ? ? ? 882  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.042 ? ? 7 1 0.998              ? ? ? ? 0.039              ? ? ? ? ? ? 
? ? ? 
# 
_refine.aniso_B[1][1]                            6.17 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            6.17 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -12.34 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               170.526 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.942 
_refine.correlation_coeff_Fo_to_Fc_free          0.910 
_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                                 8YI6 
_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                            3.60 
_refine.ls_d_res_low                             46.45 
_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                     16111 
_refine.ls_number_reflns_R_free                  848 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.24158 
_refine.ls_R_factor_R_free                       0.29012 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.23897 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.701 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             113.350 
_refine.overall_SU_ML                            0.702 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.60 
_refine_hist.d_res_low                        46.45 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               7010 
_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        6990 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_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' ? 0.006  0.012  7136  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.960  1.849  9680  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.110  5.000  914   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 7.759  5.000  98    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.800 10.000 1142  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.159  0.200  1090  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  5456  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 14.176 12.184 3662  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 22.369 21.890 4574  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 17.327 13.226 3474  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 37.065 153.75 29674 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       3.600 
_refine_ls_shell.d_res_low                        3.693 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             61 
_refine_ls_shell.number_reflns_R_work             1165 
_refine_ls_shell.percent_reflns_obs               99.92 
_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                  0.416 
_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   20 
_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                  0.449 
# 
_struct.entry_id                     8YI6 
_struct.title                        'BesA wild-type from Streptomyces cattleyicolor' 
_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        8YI6 
_struct_keywords.text            'ATP-grasp protein superfamily, amino acid-ligase, BIOSYNTHETIC PROTEIN, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BESA_STREN 
_struct_ref.pdbx_db_accession          G8XHD8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTDPGSTKILIYAFNYADRMLEEVPYLRYSAERSLCFLGDLRDPGTRLVVITSEAVDPATLDYHLRDVFRFDEPALADVR
RRLTLLTPASRAARPLDSLVLEDEALVETLRRAVAERPAGTIVDFSASPATDELGRRTGATPEEGDHAFVARWGSKSGGK
EICLRAGVAVPGGTSEVLRSEAEVVEAIHRLSCGTAAARRAMVKLDAITWAASIGNVLIDRDKLRHTGDLVGSAEVIRLP
AEEFRRELAEQGAIVEEFLEEITDSPSGLGHIERDGTVRVVACHDQVLSGGQYWGCRFPADERWRPEITDAVRRTGEVLS
GLGHRGAFGVDFVVAGERGLLAVEINLRKVGPSHVVRYAEALVGARVGADGMLRGADGRPVYYTHGRLLEPETLGKLNPR
TAVERLRAEGLLYRHDTGEGVALHVLGALNACGFVELTALARSPEAADGYSRAAQALLTGPYPSA
;
_struct_ref.pdbx_align_begin           18 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8YI6 A 1 ? 465 ? G8XHD8 18 ? 482 ? 1 465 
2 1 8YI6 B 1 ? 465 ? G8XHD8 18 ? 482 ? 1 465 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8YI6 VAL A 466 ? UNP G8XHD8 ? ? 'expression tag' 466 1  
1 8YI6 ASP A 467 ? UNP G8XHD8 ? ? 'expression tag' 467 2  
1 8YI6 LEU A 468 ? UNP G8XHD8 ? ? 'expression tag' 468 3  
1 8YI6 GLU A 469 ? UNP G8XHD8 ? ? 'expression tag' 469 4  
1 8YI6 HIS A 470 ? UNP G8XHD8 ? ? 'expression tag' 470 5  
1 8YI6 HIS A 471 ? UNP G8XHD8 ? ? 'expression tag' 471 6  
1 8YI6 HIS A 472 ? UNP G8XHD8 ? ? 'expression tag' 472 7  
1 8YI6 HIS A 473 ? UNP G8XHD8 ? ? 'expression tag' 473 8  
1 8YI6 HIS A 474 ? UNP G8XHD8 ? ? 'expression tag' 474 9  
1 8YI6 HIS A 475 ? UNP G8XHD8 ? ? 'expression tag' 475 10 
2 8YI6 VAL B 466 ? UNP G8XHD8 ? ? 'expression tag' 466 11 
2 8YI6 ASP B 467 ? UNP G8XHD8 ? ? 'expression tag' 467 12 
2 8YI6 LEU B 468 ? UNP G8XHD8 ? ? 'expression tag' 468 13 
2 8YI6 GLU B 469 ? UNP G8XHD8 ? ? 'expression tag' 469 14 
2 8YI6 HIS B 470 ? UNP G8XHD8 ? ? 'expression tag' 470 15 
2 8YI6 HIS B 471 ? UNP G8XHD8 ? ? 'expression tag' 471 16 
2 8YI6 HIS B 472 ? UNP G8XHD8 ? ? 'expression tag' 472 17 
2 8YI6 HIS B 473 ? UNP G8XHD8 ? ? 'expression tag' 473 18 
2 8YI6 HIS B 474 ? UNP G8XHD8 ? ? 'expression tag' 474 19 
2 8YI6 HIS B 475 ? UNP G8XHD8 ? ? 'expression tag' 475 20 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ARG A 19  ? GLU A 23  ? ARG A 19  GLU A 23  5 ? 5  
HELX_P HELX_P2  AA2 PRO A 25  ? ASP A 43  ? PRO A 25  ASP A 43  5 ? 19 
HELX_P HELX_P3  AA3 ASP A 57  ? ASP A 67  ? ASP A 57  ASP A 67  1 ? 11 
HELX_P HELX_P4  AA4 ASP A 72  ? ARG A 82  ? ASP A 72  ARG A 82  1 ? 11 
HELX_P HELX_P5  AA5 PRO A 95  ? ASP A 103 ? PRO A 95  ASP A 103 1 ? 9  
HELX_P HELX_P6  AA6 ASP A 103 ? ARG A 117 ? ASP A 103 ARG A 117 1 ? 15 
HELX_P HELX_P7  AA7 SER A 128 ? GLY A 139 ? SER A 128 GLY A 139 1 ? 12 
HELX_P HELX_P8  AA8 ASP A 146 ? GLY A 154 ? ASP A 146 GLY A 154 1 ? 9  
HELX_P HELX_P9  AA9 SER A 155 ? GLY A 167 ? SER A 155 GLY A 167 1 ? 13 
HELX_P HELX_P10 AB1 SER A 180 ? HIS A 189 ? SER A 180 HIS A 189 1 ? 10 
HELX_P HELX_P11 AB2 ARG A 221 ? THR A 227 ? ARG A 221 THR A 227 1 ? 7  
HELX_P HELX_P12 AB3 ASP A 229 ? GLY A 232 ? ASP A 229 GLY A 232 5 ? 4  
HELX_P HELX_P13 AB4 PRO A 240 ? GLN A 251 ? PRO A 240 GLN A 251 1 ? 12 
HELX_P HELX_P14 AB5 ARG A 303 ? GLY A 323 ? ARG A 303 GLY A 323 1 ? 21 
HELX_P HELX_P15 AB6 VAL A 350 ? GLY A 364 ? VAL A 350 GLY A 364 1 ? 15 
HELX_P HELX_P16 AB7 GLU A 390 ? GLY A 395 ? GLU A 390 GLY A 395 1 ? 6  
HELX_P HELX_P17 AB8 ASN A 398 ? GLU A 409 ? ASN A 398 GLU A 409 1 ? 12 
HELX_P HELX_P18 AB9 GLY A 427 ? GLY A 433 ? GLY A 427 GLY A 433 1 ? 7  
HELX_P HELX_P19 AC1 SER A 443 ? THR A 459 ? SER A 443 THR A 459 1 ? 17 
HELX_P HELX_P20 AC2 ARG B 19  ? GLU B 23  ? ARG B 19  GLU B 23  5 ? 5  
HELX_P HELX_P21 AC3 VAL B 24  ? ASP B 43  ? VAL B 24  ASP B 43  5 ? 20 
HELX_P HELX_P22 AC4 ASP B 57  ? ASP B 67  ? ASP B 57  ASP B 67  1 ? 11 
HELX_P HELX_P23 AC5 ASP B 72  ? ARG B 82  ? ASP B 72  ARG B 82  1 ? 11 
HELX_P HELX_P24 AC6 PRO B 95  ? ASP B 103 ? PRO B 95  ASP B 103 1 ? 9  
HELX_P HELX_P25 AC7 ASP B 103 ? ARG B 117 ? ASP B 103 ARG B 117 1 ? 15 
HELX_P HELX_P26 AC8 SER B 128 ? GLY B 139 ? SER B 128 GLY B 139 1 ? 12 
HELX_P HELX_P27 AC9 ASP B 146 ? GLY B 154 ? ASP B 146 GLY B 154 1 ? 9  
HELX_P HELX_P28 AD1 SER B 155 ? GLY B 167 ? SER B 155 GLY B 167 1 ? 13 
HELX_P HELX_P29 AD2 SER B 180 ? ARG B 190 ? SER B 180 ARG B 190 1 ? 11 
HELX_P HELX_P30 AD3 ARG B 221 ? THR B 227 ? ARG B 221 THR B 227 1 ? 7  
HELX_P HELX_P31 AD4 ASP B 229 ? GLY B 232 ? ASP B 229 GLY B 232 5 ? 4  
HELX_P HELX_P32 AD5 PRO B 240 ? GLN B 251 ? PRO B 240 GLN B 251 1 ? 12 
HELX_P HELX_P33 AD6 ARG B 303 ? GLY B 323 ? ARG B 303 GLY B 323 1 ? 21 
HELX_P HELX_P34 AD7 VAL B 350 ? GLY B 364 ? VAL B 350 GLY B 364 1 ? 15 
HELX_P HELX_P35 AD8 GLU B 390 ? GLY B 395 ? GLU B 390 GLY B 395 1 ? 6  
HELX_P HELX_P36 AD9 ASN B 398 ? GLU B 409 ? ASN B 398 GLU B 409 1 ? 12 
HELX_P HELX_P37 AE1 GLY B 427 ? GLY B 433 ? GLY B 427 GLY B 433 1 ? 7  
HELX_P HELX_P38 AE2 SER B 443 ? THR B 459 ? SER B 443 THR B 459 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 193 SG ? ? ? 1_555 A CYS 193 SG ? ? A CYS 193 A CYS 193 8_555 ? ? ? ? ? ? ? 2.305 ? ? 
disulf2 disulf ? ? B CYS 193 SG ? ? ? 1_555 B CYS 193 SG ? ? B CYS 193 B CYS 193 7_555 ? ? ? ? ? ? ? 2.778 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 193 ? CYS A 193 ? CYS A 193 ? 1_555 CYS A 193 ? 8_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 193 ? CYS B 193 ? CYS B 193 ? 1_555 CYS B 193 ? 7_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 298 A . ? PHE 298 A PRO 299 A ? PRO 299 A 1 -7.02 
2 PHE 298 B . ? PHE 298 B PRO 299 B ? PRO 299 B 1 -8.13 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 8 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA6 7 8 ? 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 LEU A 83  ? LEU A 86  ? LEU A 83  LEU A 86  
AA1 2 THR A 46  ? ILE A 51  ? THR A 46  ILE A 51  
AA1 3 SER A 6   ? ILE A 11  ? SER A 6   ILE A 11  
AA1 4 ALA A 119 ? ASP A 124 ? ALA A 119 ASP A 124 
AA1 5 THR A 141 ? PRO A 142 ? THR A 141 PRO A 142 
AA2 1 ALA A 234 ? VAL A 236 ? ALA A 234 VAL A 236 
AA2 2 VAL A 217 ? ASP A 220 ? VAL A 217 ASP A 220 
AA2 3 ARG A 200 ? LEU A 205 ? ARG A 200 LEU A 205 
AA2 4 ALA A 253 ? GLU A 257 ? ALA A 253 GLU A 257 
AA3 1 LEU A 340 ? LEU A 347 ? LEU A 340 LEU A 347 
AA3 2 GLY A 326 ? VAL A 334 ? GLY A 326 VAL A 334 
AA3 3 SER A 265 ? ILE A 272 ? SER A 265 ILE A 272 
AA3 4 VAL A 278 ? GLN A 286 ? VAL A 278 GLN A 286 
AA3 5 GLY A 295 ? PHE A 298 ? GLY A 295 PHE A 298 
AA3 6 TYR A 382 ? LEU A 389 ? TYR A 382 LEU A 389 
AA3 7 PHE A 434 ? ALA A 441 ? PHE A 434 ALA A 441 
AA3 8 GLY A 420 ? HIS A 424 ? GLY A 420 HIS A 424 
AA4 1 LEU B 83  ? LEU B 86  ? LEU B 83  LEU B 86  
AA4 2 THR B 46  ? ILE B 51  ? THR B 46  ILE B 51  
AA4 3 SER B 6   ? LEU B 10  ? SER B 6   LEU B 10  
AA4 4 GLY B 120 ? VAL B 123 ? GLY B 120 VAL B 123 
AA4 5 THR B 141 ? PRO B 142 ? THR B 141 PRO B 142 
AA5 1 ALA B 234 ? VAL B 236 ? ALA B 234 VAL B 236 
AA5 2 VAL B 217 ? ASP B 220 ? VAL B 217 ASP B 220 
AA5 3 ARG B 200 ? LEU B 205 ? ARG B 200 LEU B 205 
AA5 4 ALA B 253 ? GLU B 257 ? ALA B 253 GLU B 257 
AA6 1 LEU B 340 ? LEU B 347 ? LEU B 340 LEU B 347 
AA6 2 GLY B 326 ? VAL B 334 ? GLY B 326 VAL B 334 
AA6 3 SER B 267 ? ILE B 272 ? SER B 267 ILE B 272 
AA6 4 VAL B 278 ? GLN B 286 ? VAL B 278 GLN B 286 
AA6 5 GLY B 295 ? PHE B 298 ? GLY B 295 PHE B 298 
AA6 6 TYR B 382 ? LEU B 389 ? TYR B 382 LEU B 389 
AA6 7 PHE B 434 ? ALA B 441 ? PHE B 434 ALA B 441 
AA6 8 GLY B 420 ? HIS B 424 ? GLY B 420 HIS B 424 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O THR A 84  ? O THR A 84  N VAL A 50  ? N VAL A 50  
AA1 2 3 O VAL A 49  ? O VAL A 49  N LEU A 10  ? N LEU A 10  
AA1 3 4 N ILE A 9   ? N ILE A 9   O VAL A 123 ? O VAL A 123 
AA1 4 5 N GLY A 120 ? N GLY A 120 O THR A 141 ? O THR A 141 
AA2 1 2 O GLU A 235 ? O GLU A 235 N LEU A 218 ? N LEU A 218 
AA2 2 3 O VAL A 217 ? O VAL A 217 N VAL A 203 ? N VAL A 203 
AA2 3 4 N LYS A 204 ? N LYS A 204 O ILE A 254 ? O ILE A 254 
AA3 1 2 O ASN A 346 ? O ASN A 346 N GLY A 329 ? N GLY A 329 
AA3 2 3 O GLY A 326 ? O GLY A 326 N ILE A 272 ? N ILE A 272 
AA3 3 4 N SER A 267 ? N SER A 267 O HIS A 284 ? O HIS A 284 
AA3 4 5 N ASP A 285 ? N ASP A 285 O ARG A 297 ? O ARG A 297 
AA3 5 6 N CYS A 296 ? N CYS A 296 O HIS A 385 ? O HIS A 385 
AA3 6 7 N LEU A 388 ? N LEU A 388 O VAL A 435 ? O VAL A 435 
AA3 7 8 O LEU A 440 ? O LEU A 440 N GLY A 420 ? N GLY A 420 
AA4 1 2 O THR B 84  ? O THR B 84  N VAL B 50  ? N VAL B 50  
AA4 2 3 O VAL B 49  ? O VAL B 49  N LEU B 10  ? N LEU B 10  
AA4 3 4 N ILE B 9   ? N ILE B 9   O VAL B 123 ? O VAL B 123 
AA4 4 5 N GLY B 120 ? N GLY B 120 O THR B 141 ? O THR B 141 
AA5 1 2 O GLU B 235 ? O GLU B 235 N LEU B 218 ? N LEU B 218 
AA5 2 3 O VAL B 217 ? O VAL B 217 N VAL B 203 ? N VAL B 203 
AA5 3 4 N LYS B 204 ? N LYS B 204 O ILE B 254 ? O ILE B 254 
AA6 1 2 O ASN B 346 ? O ASN B 346 N GLY B 329 ? N GLY B 329 
AA6 2 3 O GLY B 326 ? O GLY B 326 N ILE B 272 ? N ILE B 272 
AA6 3 4 N SER B 267 ? N SER B 267 O HIS B 284 ? O HIS B 284 
AA6 4 5 N ASP B 285 ? N ASP B 285 O ARG B 297 ? O ARG B 297 
AA6 5 6 N CYS B 296 ? N CYS B 296 O HIS B 385 ? O HIS B 385 
AA6 6 7 N LEU B 388 ? N LEU B 388 O VAL B 435 ? O VAL B 435 
AA6 7 8 O LEU B 440 ? O LEU B 440 N GLY B 420 ? N GLY B 420 
# 
_pdbx_entry_details.entry_id                   8YI6 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 N  A ARG 80  ? ? CA A ARG 80  ? ? CB  A ARG 80  ? ? 125.97 110.60 15.37  1.80 N 
2  1 CD A ARG 80  ? ? NE A ARG 80  ? ? CZ  A ARG 80  ? ? 133.18 123.60 9.58   1.40 N 
3  1 NE A ARG 80  ? ? CZ A ARG 80  ? ? NH1 A ARG 80  ? ? 124.34 120.30 4.04   0.50 N 
4  1 CB A ARG 165 ? ? CA A ARG 165 ? ? C   A ARG 165 ? ? 126.16 110.40 15.76  2.00 N 
5  1 N  A TYR 358 ? ? CA A TYR 358 ? ? CB  A TYR 358 ? ? 122.97 110.60 12.37  1.80 N 
6  1 NE A ARG 407 ? ? CZ A ARG 407 ? ? NH2 A ARG 407 ? ? 115.89 120.30 -4.41  0.50 N 
7  1 CB A LEU 423 ? ? CG A LEU 423 ? ? CD1 A LEU 423 ? ? 100.29 111.00 -10.71 1.70 N 
8  1 CG B MET 20  ? ? SD B MET 20  ? ? CE  B MET 20  ? ? 112.51 100.20 12.31  1.60 N 
9  1 N  B ARG 80  ? ? CA B ARG 80  ? ? CB  B ARG 80  ? ? 124.90 110.60 14.30  1.80 N 
10 1 CD B ARG 80  ? ? NE B ARG 80  ? ? CZ  B ARG 80  ? ? 132.89 123.60 9.29   1.40 N 
11 1 NE B ARG 80  ? ? CZ B ARG 80  ? ? NH1 B ARG 80  ? ? 125.34 120.30 5.04   0.50 N 
12 1 CB B HIS 189 ? ? CA B HIS 189 ? ? C   B HIS 189 ? ? 123.52 110.40 13.12  2.00 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 TYR A 12  ? ? -102.33 43.10   
2  1 GLU A 23  ? ? -115.94 -86.48  
3  1 TYR A 26  ? ? -66.73  0.69    
4  1 VAL A 68  ? ? -99.49  -71.26  
5  1 PHE A 125 ? ? -79.70  -70.77  
6  1 GLU A 144 ? ? -151.92 31.92   
7  1 ASP A 146 ? ? 145.21  71.02   
8  1 ARG A 190 ? ? 172.36  27.07   
9  1 LEU A 191 ? ? -106.86 -163.01 
10 1 CYS A 193 ? ? 39.53   -123.03 
11 1 ALA A 212 ? ? 58.66   -149.33 
12 1 SER A 213 ? ? -101.13 53.91   
13 1 TYR A 293 ? ? 38.97   51.91   
14 1 TRP A 294 ? ? -53.93  4.29    
15 1 ALA A 335 ? ? -116.18 75.27   
16 1 ARG A 348 ? ? 172.94  168.13  
17 1 ALA A 369 ? ? 19.86   -115.45 
18 1 MET A 372 ? ? 80.73   109.80  
19 1 THR A 459 ? ? -104.41 42.98   
20 1 TYR B 12  ? ? -102.77 42.84   
21 1 GLU B 23  ? ? -115.87 -86.29  
22 1 VAL B 68  ? ? -99.21  -71.12  
23 1 PHE B 125 ? ? -82.18  -70.39  
24 1 GLU B 144 ? ? -153.17 43.74   
25 1 ASP B 146 ? ? 113.57  83.55   
26 1 CYS B 193 ? ? 40.70   -124.77 
27 1 ALA B 212 ? ? 59.53   -148.96 
28 1 SER B 213 ? ? -100.25 68.38   
29 1 TYR B 293 ? ? 39.50   51.65   
30 1 TRP B 294 ? ? -55.28  8.85    
31 1 ALA B 335 ? ? -119.05 74.68   
32 1 ARG B 348 ? ? 172.14  169.07  
33 1 ALA B 369 ? ? 40.15   -149.17 
34 1 MET B 372 ? ? 132.27  -57.30  
35 1 LEU B 373 ? ? 73.66   118.93  
36 1 THR B 459 ? ? -103.45 43.34   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 19  ? ? 0.131 'SIDE CHAIN' 
2 1 ARG A 190 ? ? 0.095 'SIDE CHAIN' 
3 1 ARG A 297 ? ? 0.087 'SIDE CHAIN' 
4 1 ARG A 407 ? ? 0.140 'SIDE CHAIN' 
5 1 ARG B 19  ? ? 0.102 'SIDE CHAIN' 
6 1 ARG B 297 ? ? 0.089 'SIDE CHAIN' 
7 1 ARG B 407 ? ? 0.142 'SIDE CHAIN' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -0.6612 -37.3229 -23.2682 0.0934 ? -0.0570 ? -0.0244 ? 0.1022 ? -0.2304 ? 1.0376 ? 0.5019 ? 0.3988 
? 0.8442 ? 1.7211 ? 0.7977  ? 1.8901 ? -0.0396 ? 0.0455  ? -0.2607 ? -0.2823 ? 0.2876 ? -0.2709 ? -0.2577 ? 0.1382  ? -0.2481 ? 
2 'X-RAY DIFFRACTION' ? refined 1.8864  -33.9482 24.8701  0.0964 ? 0.1640  ? -0.0059 ? 0.3038 ? 0.1136  ? 0.8047 ? 0.8841 ? 
-0.4521 ? 1.4738 ? 1.4979 ? -1.1306 ? 2.6156 ? -0.2342 ? -0.4459 ? -0.1250 ? 0.0749  ? 0.1930 ? -0.1893 ? -0.4198 ? -0.7484 ? 
0.0412  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1 ? ? A 5   ? ? ? A 138 ? ? ? 
2  'X-RAY DIFFRACTION' 1 ? ? A 139 ? ? ? A 226 ? ? ? 
3  'X-RAY DIFFRACTION' 1 ? ? A 227 ? ? ? A 277 ? ? ? 
4  'X-RAY DIFFRACTION' 1 ? ? A 278 ? ? ? A 350 ? ? ? 
5  'X-RAY DIFFRACTION' 1 ? ? A 351 ? ? ? A 462 ? ? ? 
6  'X-RAY DIFFRACTION' 2 ? ? B 5   ? ? ? B 138 ? ? ? 
7  'X-RAY DIFFRACTION' 2 ? ? B 139 ? ? ? B 189 ? ? ? 
8  'X-RAY DIFFRACTION' 2 ? ? B 190 ? ? ? B 277 ? ? ? 
9  'X-RAY DIFFRACTION' 2 ? ? B 278 ? ? ? B 350 ? ? ? 
10 'X-RAY DIFFRACTION' 2 ? ? B 351 ? ? ? B 462 ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A ASP 3   ? A ASP 3   
4  1 Y 1 A PRO 4   ? A PRO 4   
5  1 Y 1 A PRO 463 ? A PRO 463 
6  1 Y 1 A SER 464 ? A SER 464 
7  1 Y 1 A ALA 465 ? A ALA 465 
8  1 Y 1 A VAL 466 ? A VAL 466 
9  1 Y 1 A ASP 467 ? A ASP 467 
10 1 Y 1 A LEU 468 ? A LEU 468 
11 1 Y 1 A GLU 469 ? A GLU 469 
12 1 Y 1 A HIS 470 ? A HIS 470 
13 1 Y 1 A HIS 471 ? A HIS 471 
14 1 Y 1 A HIS 472 ? A HIS 472 
15 1 Y 1 A HIS 473 ? A HIS 473 
16 1 Y 1 A HIS 474 ? A HIS 474 
17 1 Y 1 A HIS 475 ? A HIS 475 
18 1 Y 1 B MET 1   ? B MET 1   
19 1 Y 1 B THR 2   ? B THR 2   
20 1 Y 1 B ASP 3   ? B ASP 3   
21 1 Y 1 B PRO 4   ? B PRO 4   
22 1 Y 1 B PRO 463 ? B PRO 463 
23 1 Y 1 B SER 464 ? B SER 464 
24 1 Y 1 B ALA 465 ? B ALA 465 
25 1 Y 1 B VAL 466 ? B VAL 466 
26 1 Y 1 B ASP 467 ? B ASP 467 
27 1 Y 1 B LEU 468 ? B LEU 468 
28 1 Y 1 B GLU 469 ? B GLU 469 
29 1 Y 1 B HIS 470 ? B HIS 470 
30 1 Y 1 B HIS 471 ? B HIS 471 
31 1 Y 1 B HIS 472 ? B HIS 472 
32 1 Y 1 B HIS 473 ? B HIS 473 
33 1 Y 1 B HIS 474 ? B HIS 474 
34 1 Y 1 B HIS 475 ? B HIS 475 
# 
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 
ADE N9   N Y N 1   
ADE C8   C Y N 2   
ADE N7   N Y N 3   
ADE C5   C Y N 4   
ADE C6   C Y N 5   
ADE N6   N N N 6   
ADE N1   N Y N 7   
ADE C2   C Y N 8   
ADE N3   N Y N 9   
ADE C4   C Y N 10  
ADE HN9  H N N 11  
ADE H8   H N N 12  
ADE HN61 H N N 13  
ADE HN62 H N N 14  
ADE H2   H N N 15  
ALA N    N N N 16  
ALA CA   C N S 17  
ALA C    C N N 18  
ALA O    O N N 19  
ALA CB   C N N 20  
ALA OXT  O N N 21  
ALA H    H N N 22  
ALA H2   H N N 23  
ALA HA   H N N 24  
ALA HB1  H N N 25  
ALA HB2  H N N 26  
ALA HB3  H N N 27  
ALA HXT  H N N 28  
ARG N    N N N 29  
ARG CA   C N S 30  
ARG C    C N N 31  
ARG O    O N N 32  
ARG CB   C N N 33  
ARG CG   C N N 34  
ARG CD   C N N 35  
ARG NE   N N N 36  
ARG CZ   C N N 37  
ARG NH1  N N N 38  
ARG NH2  N N N 39  
ARG OXT  O N N 40  
ARG H    H N N 41  
ARG H2   H N N 42  
ARG HA   H N N 43  
ARG HB2  H N N 44  
ARG HB3  H N N 45  
ARG HG2  H N N 46  
ARG HG3  H N N 47  
ARG HD2  H N N 48  
ARG HD3  H N N 49  
ARG HE   H N N 50  
ARG HH11 H N N 51  
ARG HH12 H N N 52  
ARG HH21 H N N 53  
ARG HH22 H N N 54  
ARG HXT  H N N 55  
ASN N    N N N 56  
ASN CA   C N S 57  
ASN C    C N N 58  
ASN O    O N N 59  
ASN CB   C N N 60  
ASN CG   C N N 61  
ASN OD1  O N N 62  
ASN ND2  N N N 63  
ASN OXT  O N N 64  
ASN H    H N N 65  
ASN H2   H N N 66  
ASN HA   H N N 67  
ASN HB2  H N N 68  
ASN HB3  H N N 69  
ASN HD21 H N N 70  
ASN HD22 H N N 71  
ASN HXT  H N N 72  
ASP N    N N N 73  
ASP CA   C N S 74  
ASP C    C N N 75  
ASP O    O N N 76  
ASP CB   C N N 77  
ASP CG   C N N 78  
ASP OD1  O N N 79  
ASP OD2  O N N 80  
ASP OXT  O N N 81  
ASP H    H N N 82  
ASP H2   H N N 83  
ASP HA   H N N 84  
ASP HB2  H N N 85  
ASP HB3  H N N 86  
ASP HD2  H N N 87  
ASP HXT  H N N 88  
CYS N    N N N 89  
CYS CA   C N R 90  
CYS C    C N N 91  
CYS O    O N N 92  
CYS CB   C N N 93  
CYS SG   S N N 94  
CYS OXT  O N N 95  
CYS H    H N N 96  
CYS H2   H N N 97  
CYS HA   H N N 98  
CYS HB2  H N N 99  
CYS HB3  H N N 100 
CYS HG   H N N 101 
CYS HXT  H N N 102 
GLN N    N N N 103 
GLN CA   C N S 104 
GLN C    C N N 105 
GLN O    O N N 106 
GLN CB   C N N 107 
GLN CG   C N N 108 
GLN CD   C N N 109 
GLN OE1  O N N 110 
GLN NE2  N N N 111 
GLN OXT  O N N 112 
GLN H    H N N 113 
GLN H2   H N N 114 
GLN HA   H N N 115 
GLN HB2  H N N 116 
GLN HB3  H N N 117 
GLN HG2  H N N 118 
GLN HG3  H N N 119 
GLN HE21 H N N 120 
GLN HE22 H N N 121 
GLN HXT  H N N 122 
GLU N    N N N 123 
GLU CA   C N S 124 
GLU C    C N N 125 
GLU O    O N N 126 
GLU CB   C N N 127 
GLU CG   C N N 128 
GLU CD   C N N 129 
GLU OE1  O N N 130 
GLU OE2  O N N 131 
GLU OXT  O N N 132 
GLU H    H N N 133 
GLU H2   H N N 134 
GLU HA   H N N 135 
GLU HB2  H N N 136 
GLU HB3  H N N 137 
GLU HG2  H N N 138 
GLU HG3  H N N 139 
GLU HE2  H N N 140 
GLU HXT  H N N 141 
GLY N    N N N 142 
GLY CA   C N N 143 
GLY C    C N N 144 
GLY O    O N N 145 
GLY OXT  O N N 146 
GLY H    H N N 147 
GLY H2   H N N 148 
GLY HA2  H N N 149 
GLY HA3  H N N 150 
GLY HXT  H N N 151 
HIS N    N N N 152 
HIS CA   C N S 153 
HIS C    C N N 154 
HIS O    O N N 155 
HIS CB   C N N 156 
HIS CG   C Y N 157 
HIS ND1  N Y N 158 
HIS CD2  C Y N 159 
HIS CE1  C Y N 160 
HIS NE2  N Y N 161 
HIS OXT  O N N 162 
HIS H    H N N 163 
HIS H2   H N N 164 
HIS HA   H N N 165 
HIS HB2  H N N 166 
HIS HB3  H N N 167 
HIS HD1  H N N 168 
HIS HD2  H N N 169 
HIS HE1  H N N 170 
HIS HE2  H N N 171 
HIS HXT  H N N 172 
ILE N    N N N 173 
ILE CA   C N S 174 
ILE C    C N N 175 
ILE O    O N N 176 
ILE CB   C N S 177 
ILE CG1  C N N 178 
ILE CG2  C N N 179 
ILE CD1  C N N 180 
ILE OXT  O N N 181 
ILE H    H N N 182 
ILE H2   H N N 183 
ILE HA   H N N 184 
ILE HB   H N N 185 
ILE HG12 H N N 186 
ILE HG13 H N N 187 
ILE HG21 H N N 188 
ILE HG22 H N N 189 
ILE HG23 H N N 190 
ILE HD11 H N N 191 
ILE HD12 H N N 192 
ILE HD13 H N N 193 
ILE HXT  H N N 194 
LEU N    N N N 195 
LEU CA   C N S 196 
LEU C    C N N 197 
LEU O    O N N 198 
LEU CB   C N N 199 
LEU CG   C N N 200 
LEU CD1  C N N 201 
LEU CD2  C N N 202 
LEU OXT  O N N 203 
LEU H    H N N 204 
LEU H2   H N N 205 
LEU HA   H N N 206 
LEU HB2  H N N 207 
LEU HB3  H N N 208 
LEU HG   H N N 209 
LEU HD11 H N N 210 
LEU HD12 H N N 211 
LEU HD13 H N N 212 
LEU HD21 H N N 213 
LEU HD22 H N N 214 
LEU HD23 H N N 215 
LEU HXT  H N N 216 
LYS N    N N N 217 
LYS CA   C N S 218 
LYS C    C N N 219 
LYS O    O N N 220 
LYS CB   C N N 221 
LYS CG   C N N 222 
LYS CD   C N N 223 
LYS CE   C N N 224 
LYS NZ   N N N 225 
LYS OXT  O N N 226 
LYS H    H N N 227 
LYS H2   H N N 228 
LYS HA   H N N 229 
LYS HB2  H N N 230 
LYS HB3  H N N 231 
LYS HG2  H N N 232 
LYS HG3  H N N 233 
LYS HD2  H N N 234 
LYS HD3  H N N 235 
LYS HE2  H N N 236 
LYS HE3  H N N 237 
LYS HZ1  H N N 238 
LYS HZ2  H N N 239 
LYS HZ3  H N N 240 
LYS HXT  H N N 241 
MET N    N N N 242 
MET CA   C N S 243 
MET C    C N N 244 
MET O    O N N 245 
MET CB   C N N 246 
MET CG   C N N 247 
MET SD   S N N 248 
MET CE   C N N 249 
MET OXT  O N N 250 
MET H    H N N 251 
MET H2   H N N 252 
MET HA   H N N 253 
MET HB2  H N N 254 
MET HB3  H N N 255 
MET HG2  H N N 256 
MET HG3  H N N 257 
MET HE1  H N N 258 
MET HE2  H N N 259 
MET HE3  H N N 260 
MET HXT  H N N 261 
PHE N    N N N 262 
PHE CA   C N S 263 
PHE C    C N N 264 
PHE O    O N N 265 
PHE CB   C N N 266 
PHE CG   C Y N 267 
PHE CD1  C Y N 268 
PHE CD2  C Y N 269 
PHE CE1  C Y N 270 
PHE CE2  C Y N 271 
PHE CZ   C Y N 272 
PHE OXT  O N N 273 
PHE H    H N N 274 
PHE H2   H N N 275 
PHE HA   H N N 276 
PHE HB2  H N N 277 
PHE HB3  H N N 278 
PHE HD1  H N N 279 
PHE HD2  H N N 280 
PHE HE1  H N N 281 
PHE HE2  H N N 282 
PHE HZ   H N N 283 
PHE HXT  H N N 284 
PRO N    N N N 285 
PRO CA   C N S 286 
PRO C    C N N 287 
PRO O    O N N 288 
PRO CB   C N N 289 
PRO CG   C N N 290 
PRO CD   C N N 291 
PRO OXT  O N N 292 
PRO H    H N N 293 
PRO HA   H N N 294 
PRO HB2  H N N 295 
PRO HB3  H N N 296 
PRO HG2  H N N 297 
PRO HG3  H N N 298 
PRO HD2  H N N 299 
PRO HD3  H N N 300 
PRO HXT  H N N 301 
SER N    N N N 302 
SER CA   C N S 303 
SER C    C N N 304 
SER O    O N N 305 
SER CB   C N N 306 
SER OG   O N N 307 
SER OXT  O N N 308 
SER H    H N N 309 
SER H2   H N N 310 
SER HA   H N N 311 
SER HB2  H N N 312 
SER HB3  H N N 313 
SER HG   H N N 314 
SER HXT  H N N 315 
THR N    N N N 316 
THR CA   C N S 317 
THR C    C N N 318 
THR O    O N N 319 
THR CB   C N R 320 
THR OG1  O N N 321 
THR CG2  C N N 322 
THR OXT  O N N 323 
THR H    H N N 324 
THR H2   H N N 325 
THR HA   H N N 326 
THR HB   H N N 327 
THR HG1  H N N 328 
THR HG21 H N N 329 
THR HG22 H N N 330 
THR HG23 H N N 331 
THR HXT  H N N 332 
TRP N    N N N 333 
TRP CA   C N S 334 
TRP C    C N N 335 
TRP O    O N N 336 
TRP CB   C N N 337 
TRP CG   C Y N 338 
TRP CD1  C Y N 339 
TRP CD2  C Y N 340 
TRP NE1  N Y N 341 
TRP CE2  C Y N 342 
TRP CE3  C Y N 343 
TRP CZ2  C Y N 344 
TRP CZ3  C Y N 345 
TRP CH2  C Y N 346 
TRP OXT  O N N 347 
TRP H    H N N 348 
TRP H2   H N N 349 
TRP HA   H N N 350 
TRP HB2  H N N 351 
TRP HB3  H N N 352 
TRP HD1  H N N 353 
TRP HE1  H N N 354 
TRP HE3  H N N 355 
TRP HZ2  H N N 356 
TRP HZ3  H N N 357 
TRP HH2  H N N 358 
TRP HXT  H N N 359 
TYR N    N N N 360 
TYR CA   C N S 361 
TYR C    C N N 362 
TYR O    O N N 363 
TYR CB   C N N 364 
TYR CG   C Y N 365 
TYR CD1  C Y N 366 
TYR CD2  C Y N 367 
TYR CE1  C Y N 368 
TYR CE2  C Y N 369 
TYR CZ   C Y N 370 
TYR OH   O N N 371 
TYR OXT  O N N 372 
TYR H    H N N 373 
TYR H2   H N N 374 
TYR HA   H N N 375 
TYR HB2  H N N 376 
TYR HB3  H N N 377 
TYR HD1  H N N 378 
TYR HD2  H N N 379 
TYR HE1  H N N 380 
TYR HE2  H N N 381 
TYR HH   H N N 382 
TYR HXT  H N N 383 
VAL N    N N N 384 
VAL CA   C N S 385 
VAL C    C N N 386 
VAL O    O N N 387 
VAL CB   C N N 388 
VAL CG1  C N N 389 
VAL CG2  C N N 390 
VAL OXT  O N N 391 
VAL H    H N N 392 
VAL H2   H N N 393 
VAL HA   H N N 394 
VAL HB   H N N 395 
VAL HG11 H N N 396 
VAL HG12 H N N 397 
VAL HG13 H N N 398 
VAL HG21 H N N 399 
VAL HG22 H N N 400 
VAL HG23 H N N 401 
VAL HXT  H N N 402 
# 
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 
ADE N9  C8   sing Y N 1   
ADE N9  C4   sing Y N 2   
ADE N9  HN9  sing N N 3   
ADE C8  N7   doub Y N 4   
ADE C8  H8   sing N N 5   
ADE N7  C5   sing Y N 6   
ADE C5  C6   sing Y N 7   
ADE C5  C4   doub Y N 8   
ADE C6  N6   sing N N 9   
ADE C6  N1   doub Y N 10  
ADE N6  HN61 sing N N 11  
ADE N6  HN62 sing N N 12  
ADE N1  C2   sing Y N 13  
ADE C2  N3   doub Y N 14  
ADE C2  H2   sing N N 15  
ADE N3  C4   sing Y N 16  
ALA N   CA   sing N N 17  
ALA N   H    sing N N 18  
ALA N   H2   sing N N 19  
ALA CA  C    sing N N 20  
ALA CA  CB   sing N N 21  
ALA CA  HA   sing N N 22  
ALA C   O    doub N N 23  
ALA C   OXT  sing N N 24  
ALA CB  HB1  sing N N 25  
ALA CB  HB2  sing N N 26  
ALA CB  HB3  sing N N 27  
ALA OXT HXT  sing N N 28  
ARG N   CA   sing N N 29  
ARG N   H    sing N N 30  
ARG N   H2   sing N N 31  
ARG CA  C    sing N N 32  
ARG CA  CB   sing N N 33  
ARG CA  HA   sing N N 34  
ARG C   O    doub N N 35  
ARG C   OXT  sing N N 36  
ARG CB  CG   sing N N 37  
ARG CB  HB2  sing N N 38  
ARG CB  HB3  sing N N 39  
ARG CG  CD   sing N N 40  
ARG CG  HG2  sing N N 41  
ARG CG  HG3  sing N N 42  
ARG CD  NE   sing N N 43  
ARG CD  HD2  sing N N 44  
ARG CD  HD3  sing N N 45  
ARG NE  CZ   sing N N 46  
ARG NE  HE   sing N N 47  
ARG CZ  NH1  sing N N 48  
ARG CZ  NH2  doub N N 49  
ARG NH1 HH11 sing N N 50  
ARG NH1 HH12 sing N N 51  
ARG NH2 HH21 sing N N 52  
ARG NH2 HH22 sing N N 53  
ARG OXT HXT  sing N N 54  
ASN N   CA   sing N N 55  
ASN N   H    sing N N 56  
ASN N   H2   sing N N 57  
ASN CA  C    sing N N 58  
ASN CA  CB   sing N N 59  
ASN CA  HA   sing N N 60  
ASN C   O    doub N N 61  
ASN C   OXT  sing N N 62  
ASN CB  CG   sing N N 63  
ASN CB  HB2  sing N N 64  
ASN CB  HB3  sing N N 65  
ASN CG  OD1  doub N N 66  
ASN CG  ND2  sing N N 67  
ASN ND2 HD21 sing N N 68  
ASN ND2 HD22 sing N N 69  
ASN OXT HXT  sing N N 70  
ASP N   CA   sing N N 71  
ASP N   H    sing N N 72  
ASP N   H2   sing N N 73  
ASP CA  C    sing N N 74  
ASP CA  CB   sing N N 75  
ASP CA  HA   sing N N 76  
ASP C   O    doub N N 77  
ASP C   OXT  sing N N 78  
ASP CB  CG   sing N N 79  
ASP CB  HB2  sing N N 80  
ASP CB  HB3  sing N N 81  
ASP CG  OD1  doub N N 82  
ASP CG  OD2  sing N N 83  
ASP OD2 HD2  sing N N 84  
ASP OXT HXT  sing N N 85  
CYS N   CA   sing N N 86  
CYS N   H    sing N N 87  
CYS N   H2   sing N N 88  
CYS CA  C    sing N N 89  
CYS CA  CB   sing N N 90  
CYS CA  HA   sing N N 91  
CYS C   O    doub N N 92  
CYS C   OXT  sing N N 93  
CYS CB  SG   sing N N 94  
CYS CB  HB2  sing N N 95  
CYS CB  HB3  sing N N 96  
CYS SG  HG   sing N N 97  
CYS OXT HXT  sing N N 98  
GLN N   CA   sing N N 99  
GLN N   H    sing N N 100 
GLN N   H2   sing N N 101 
GLN CA  C    sing N N 102 
GLN CA  CB   sing N N 103 
GLN CA  HA   sing N N 104 
GLN C   O    doub N N 105 
GLN C   OXT  sing N N 106 
GLN CB  CG   sing N N 107 
GLN CB  HB2  sing N N 108 
GLN CB  HB3  sing N N 109 
GLN CG  CD   sing N N 110 
GLN CG  HG2  sing N N 111 
GLN CG  HG3  sing N N 112 
GLN CD  OE1  doub N N 113 
GLN CD  NE2  sing N N 114 
GLN NE2 HE21 sing N N 115 
GLN NE2 HE22 sing N N 116 
GLN OXT HXT  sing N N 117 
GLU N   CA   sing N N 118 
GLU N   H    sing N N 119 
GLU N   H2   sing N N 120 
GLU CA  C    sing N N 121 
GLU CA  CB   sing N N 122 
GLU CA  HA   sing N N 123 
GLU C   O    doub N N 124 
GLU C   OXT  sing N N 125 
GLU CB  CG   sing N N 126 
GLU CB  HB2  sing N N 127 
GLU CB  HB3  sing N N 128 
GLU CG  CD   sing N N 129 
GLU CG  HG2  sing N N 130 
GLU CG  HG3  sing N N 131 
GLU CD  OE1  doub N N 132 
GLU CD  OE2  sing N N 133 
GLU OE2 HE2  sing N N 134 
GLU OXT HXT  sing N N 135 
GLY N   CA   sing N N 136 
GLY N   H    sing N N 137 
GLY N   H2   sing N N 138 
GLY CA  C    sing N N 139 
GLY CA  HA2  sing N N 140 
GLY CA  HA3  sing N N 141 
GLY C   O    doub N N 142 
GLY C   OXT  sing N N 143 
GLY OXT HXT  sing N N 144 
HIS N   CA   sing N N 145 
HIS N   H    sing N N 146 
HIS N   H2   sing N N 147 
HIS CA  C    sing N N 148 
HIS CA  CB   sing N N 149 
HIS CA  HA   sing N N 150 
HIS C   O    doub N N 151 
HIS C   OXT  sing N N 152 
HIS CB  CG   sing N N 153 
HIS CB  HB2  sing N N 154 
HIS CB  HB3  sing N N 155 
HIS CG  ND1  sing Y N 156 
HIS CG  CD2  doub Y N 157 
HIS ND1 CE1  doub Y N 158 
HIS ND1 HD1  sing N N 159 
HIS CD2 NE2  sing Y N 160 
HIS CD2 HD2  sing N N 161 
HIS CE1 NE2  sing Y N 162 
HIS CE1 HE1  sing N N 163 
HIS NE2 HE2  sing N N 164 
HIS OXT HXT  sing N N 165 
ILE N   CA   sing N N 166 
ILE N   H    sing N N 167 
ILE N   H2   sing N N 168 
ILE CA  C    sing N N 169 
ILE CA  CB   sing N N 170 
ILE CA  HA   sing N N 171 
ILE C   O    doub N N 172 
ILE C   OXT  sing N N 173 
ILE CB  CG1  sing N N 174 
ILE CB  CG2  sing N N 175 
ILE CB  HB   sing N N 176 
ILE CG1 CD1  sing N N 177 
ILE CG1 HG12 sing N N 178 
ILE CG1 HG13 sing N N 179 
ILE CG2 HG21 sing N N 180 
ILE CG2 HG22 sing N N 181 
ILE CG2 HG23 sing N N 182 
ILE CD1 HD11 sing N N 183 
ILE CD1 HD12 sing N N 184 
ILE CD1 HD13 sing N N 185 
ILE OXT HXT  sing N N 186 
LEU N   CA   sing N N 187 
LEU N   H    sing N N 188 
LEU N   H2   sing N N 189 
LEU CA  C    sing N N 190 
LEU CA  CB   sing N N 191 
LEU CA  HA   sing N N 192 
LEU C   O    doub N N 193 
LEU C   OXT  sing N N 194 
LEU CB  CG   sing N N 195 
LEU CB  HB2  sing N N 196 
LEU CB  HB3  sing N N 197 
LEU CG  CD1  sing N N 198 
LEU CG  CD2  sing N N 199 
LEU CG  HG   sing N N 200 
LEU CD1 HD11 sing N N 201 
LEU CD1 HD12 sing N N 202 
LEU CD1 HD13 sing N N 203 
LEU CD2 HD21 sing N N 204 
LEU CD2 HD22 sing N N 205 
LEU CD2 HD23 sing N N 206 
LEU OXT HXT  sing N N 207 
LYS N   CA   sing N N 208 
LYS N   H    sing N N 209 
LYS N   H2   sing N N 210 
LYS CA  C    sing N N 211 
LYS CA  CB   sing N N 212 
LYS CA  HA   sing N N 213 
LYS C   O    doub N N 214 
LYS C   OXT  sing N N 215 
LYS CB  CG   sing N N 216 
LYS CB  HB2  sing N N 217 
LYS CB  HB3  sing N N 218 
LYS CG  CD   sing N N 219 
LYS CG  HG2  sing N N 220 
LYS CG  HG3  sing N N 221 
LYS CD  CE   sing N N 222 
LYS CD  HD2  sing N N 223 
LYS CD  HD3  sing N N 224 
LYS CE  NZ   sing N N 225 
LYS CE  HE2  sing N N 226 
LYS CE  HE3  sing N N 227 
LYS NZ  HZ1  sing N N 228 
LYS NZ  HZ2  sing N N 229 
LYS NZ  HZ3  sing N N 230 
LYS OXT HXT  sing N N 231 
MET N   CA   sing N N 232 
MET N   H    sing N N 233 
MET N   H2   sing N N 234 
MET CA  C    sing N N 235 
MET CA  CB   sing N N 236 
MET CA  HA   sing N N 237 
MET C   O    doub N N 238 
MET C   OXT  sing N N 239 
MET CB  CG   sing N N 240 
MET CB  HB2  sing N N 241 
MET CB  HB3  sing N N 242 
MET CG  SD   sing N N 243 
MET CG  HG2  sing N N 244 
MET CG  HG3  sing N N 245 
MET SD  CE   sing N N 246 
MET CE  HE1  sing N N 247 
MET CE  HE2  sing N N 248 
MET CE  HE3  sing N N 249 
MET OXT HXT  sing N N 250 
PHE N   CA   sing N N 251 
PHE N   H    sing N N 252 
PHE N   H2   sing N N 253 
PHE CA  C    sing N N 254 
PHE CA  CB   sing N N 255 
PHE CA  HA   sing N N 256 
PHE C   O    doub N N 257 
PHE C   OXT  sing N N 258 
PHE CB  CG   sing N N 259 
PHE CB  HB2  sing N N 260 
PHE CB  HB3  sing N N 261 
PHE CG  CD1  doub Y N 262 
PHE CG  CD2  sing Y N 263 
PHE CD1 CE1  sing Y N 264 
PHE CD1 HD1  sing N N 265 
PHE CD2 CE2  doub Y N 266 
PHE CD2 HD2  sing N N 267 
PHE CE1 CZ   doub Y N 268 
PHE CE1 HE1  sing N N 269 
PHE CE2 CZ   sing Y N 270 
PHE CE2 HE2  sing N N 271 
PHE CZ  HZ   sing N N 272 
PHE OXT HXT  sing N N 273 
PRO N   CA   sing N N 274 
PRO N   CD   sing N N 275 
PRO N   H    sing N N 276 
PRO CA  C    sing N N 277 
PRO CA  CB   sing N N 278 
PRO CA  HA   sing N N 279 
PRO C   O    doub N N 280 
PRO C   OXT  sing N N 281 
PRO CB  CG   sing N N 282 
PRO CB  HB2  sing N N 283 
PRO CB  HB3  sing N N 284 
PRO CG  CD   sing N N 285 
PRO CG  HG2  sing N N 286 
PRO CG  HG3  sing N N 287 
PRO CD  HD2  sing N N 288 
PRO CD  HD3  sing N N 289 
PRO OXT HXT  sing N N 290 
SER N   CA   sing N N 291 
SER N   H    sing N N 292 
SER N   H2   sing N N 293 
SER CA  C    sing N N 294 
SER CA  CB   sing N N 295 
SER CA  HA   sing N N 296 
SER C   O    doub N N 297 
SER C   OXT  sing N N 298 
SER CB  OG   sing N N 299 
SER CB  HB2  sing N N 300 
SER CB  HB3  sing N N 301 
SER OG  HG   sing N N 302 
SER OXT HXT  sing N N 303 
THR N   CA   sing N N 304 
THR N   H    sing N N 305 
THR N   H2   sing N N 306 
THR CA  C    sing N N 307 
THR CA  CB   sing N N 308 
THR CA  HA   sing N N 309 
THR C   O    doub N N 310 
THR C   OXT  sing N N 311 
THR CB  OG1  sing N N 312 
THR CB  CG2  sing N N 313 
THR CB  HB   sing N N 314 
THR OG1 HG1  sing N N 315 
THR CG2 HG21 sing N N 316 
THR CG2 HG22 sing N N 317 
THR CG2 HG23 sing N N 318 
THR OXT HXT  sing N N 319 
TRP N   CA   sing N N 320 
TRP N   H    sing N N 321 
TRP N   H2   sing N N 322 
TRP CA  C    sing N N 323 
TRP CA  CB   sing N N 324 
TRP CA  HA   sing N N 325 
TRP C   O    doub N N 326 
TRP C   OXT  sing N N 327 
TRP CB  CG   sing N N 328 
TRP CB  HB2  sing N N 329 
TRP CB  HB3  sing N N 330 
TRP CG  CD1  doub Y N 331 
TRP CG  CD2  sing Y N 332 
TRP CD1 NE1  sing Y N 333 
TRP CD1 HD1  sing N N 334 
TRP CD2 CE2  doub Y N 335 
TRP CD2 CE3  sing Y N 336 
TRP NE1 CE2  sing Y N 337 
TRP NE1 HE1  sing N N 338 
TRP CE2 CZ2  sing Y N 339 
TRP CE3 CZ3  doub Y N 340 
TRP CE3 HE3  sing N N 341 
TRP CZ2 CH2  doub Y N 342 
TRP CZ2 HZ2  sing N N 343 
TRP CZ3 CH2  sing Y N 344 
TRP CZ3 HZ3  sing N N 345 
TRP CH2 HH2  sing N N 346 
TRP OXT HXT  sing N N 347 
TYR N   CA   sing N N 348 
TYR N   H    sing N N 349 
TYR N   H2   sing N N 350 
TYR CA  C    sing N N 351 
TYR CA  CB   sing N N 352 
TYR CA  HA   sing N N 353 
TYR C   O    doub N N 354 
TYR C   OXT  sing N N 355 
TYR CB  CG   sing N N 356 
TYR CB  HB2  sing N N 357 
TYR CB  HB3  sing N N 358 
TYR CG  CD1  doub Y N 359 
TYR CG  CD2  sing Y N 360 
TYR CD1 CE1  sing Y N 361 
TYR CD1 HD1  sing N N 362 
TYR CD2 CE2  doub Y N 363 
TYR CD2 HD2  sing N N 364 
TYR CE1 CZ   doub Y N 365 
TYR CE1 HE1  sing N N 366 
TYR CE2 CZ   sing Y N 367 
TYR CE2 HE2  sing N N 368 
TYR CZ  OH   sing N N 369 
TYR OH  HH   sing N N 370 
TYR OXT HXT  sing N N 371 
VAL N   CA   sing N N 372 
VAL N   H    sing N N 373 
VAL N   H2   sing N N 374 
VAL CA  C    sing N N 375 
VAL CA  CB   sing N N 376 
VAL CA  HA   sing N N 377 
VAL C   O    doub N N 378 
VAL C   OXT  sing N N 379 
VAL CB  CG1  sing N N 380 
VAL CB  CG2  sing N N 381 
VAL CB  HB   sing N N 382 
VAL CG1 HG11 sing N N 383 
VAL CG1 HG12 sing N N 384 
VAL CG1 HG13 sing N N 385 
VAL CG2 HG21 sing N N 386 
VAL CG2 HG22 sing N N 387 
VAL CG2 HG23 sing N N 388 
VAL OXT HXT  sing N N 389 
# 
_pdbx_audit_support.funding_organization   'Japan Society for the Promotion of Science (JSPS)' 
_pdbx_audit_support.country                Japan 
_pdbx_audit_support.grant_number           23H04542 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-G8XHD8-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YI6 
_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]   0.007211 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007211 
_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]   0.006898 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY A 1 5   ? 1.467   -51.953 -48.579 1.00 192.39 ? 5   GLY A N   1 
ATOM   2    C CA  . GLY A 1 5   ? 0.654   -52.609 -47.539 1.00 192.36 ? 5   GLY A CA  1 
ATOM   3    C C   . GLY A 1 5   ? 1.206   -52.282 -46.159 1.00 191.96 ? 5   GLY A C   1 
ATOM   4    O O   . GLY A 1 5   ? 2.391   -52.467 -45.901 1.00 211.27 ? 5   GLY A O   1 
ATOM   5    N N   . SER A 1 6   ? 0.315   -51.782 -45.294 1.00 182.01 ? 6   SER A N   1 
ATOM   6    C CA  . SER A 1 6   ? 0.624   -51.483 -43.906 1.00 167.43 ? 6   SER A CA  1 
ATOM   7    C C   . SER A 1 6   ? -0.373  -52.153 -42.961 1.00 164.16 ? 6   SER A C   1 
ATOM   8    O O   . SER A 1 6   ? -1.590  -52.213 -43.189 1.00 202.79 ? 6   SER A O   1 
ATOM   9    C CB  . SER A 1 6   ? 0.675   -49.995 -43.620 1.00 155.44 ? 6   SER A CB  1 
ATOM   10   O OG  . SER A 1 6   ? 1.258   -49.251 -44.680 1.00 150.26 ? 6   SER A OG  1 
ATOM   11   N N   . THR A 1 7   ? 0.166   -52.578 -41.816 1.00 150.61 ? 7   THR A N   1 
ATOM   12   C CA  . THR A 1 7   ? -0.604  -53.006 -40.647 1.00 162.42 ? 7   THR A CA  1 
ATOM   13   C C   . THR A 1 7   ? -0.156  -52.232 -39.408 1.00 168.34 ? 7   THR A C   1 
ATOM   14   O O   . THR A 1 7   ? 1.032   -52.173 -39.100 1.00 204.43 ? 7   THR A O   1 
ATOM   15   C CB  . THR A 1 7   ? -0.512  -54.529 -40.472 1.00 163.62 ? 7   THR A CB  1 
ATOM   16   O OG1 . THR A 1 7   ? -1.323  -55.014 -41.537 1.00 179.57 ? 7   THR A OG1 1 
ATOM   17   C CG2 . THR A 1 7   ? -1.012  -55.057 -39.136 1.00 147.35 ? 7   THR A CG2 1 
ATOM   18   N N   . LYS A 1 8   ? -1.141  -51.618 -38.738 1.00 158.51 ? 8   LYS A N   1 
ATOM   19   C CA  . LYS A 1 8   ? -0.938  -50.823 -37.541 1.00 137.78 ? 8   LYS A CA  1 
ATOM   20   C C   . LYS A 1 8   ? -1.878  -51.305 -36.433 1.00 138.73 ? 8   LYS A C   1 
ATOM   21   O O   . LYS A 1 8   ? -3.088  -51.487 -36.626 1.00 134.79 ? 8   LYS A O   1 
ATOM   22   C CB  . LYS A 1 8   ? -1.141  -49.313 -37.738 1.00 121.66 ? 8   LYS A CB  1 
ATOM   23   C CG  . LYS A 1 8   ? -0.428  -48.726 -38.943 1.00 132.27 ? 8   LYS A CG  1 
ATOM   24   C CD  . LYS A 1 8   ? -0.484  -47.224 -39.183 1.00 138.91 ? 8   LYS A CD  1 
ATOM   25   C CE  . LYS A 1 8   ? 0.064   -46.915 -40.551 1.00 146.68 ? 8   LYS A CE  1 
ATOM   26   N NZ  . LYS A 1 8   ? 1.280   -47.664 -40.893 1.00 155.20 ? 8   LYS A NZ  1 
ATOM   27   N N   . ILE A 1 9   ? -1.269  -51.508 -35.256 1.00 141.39 ? 9   ILE A N   1 
ATOM   28   C CA  . ILE A 1 9   ? -1.916  -52.120 -34.098 1.00 134.08 ? 9   ILE A CA  1 
ATOM   29   C C   . ILE A 1 9   ? -1.886  -51.147 -32.910 1.00 145.01 ? 9   ILE A C   1 
ATOM   30   O O   . ILE A 1 9   ? -0.804  -50.741 -32.505 1.00 153.59 ? 9   ILE A O   1 
ATOM   31   C CB  . ILE A 1 9   ? -1.190  -53.451 -33.763 1.00 114.26 ? 9   ILE A CB  1 
ATOM   32   C CG1 . ILE A 1 9   ? -1.320  -54.485 -34.893 1.00 105.74 ? 9   ILE A CG1 1 
ATOM   33   C CG2 . ILE A 1 9   ? -1.546  -54.027 -32.380 1.00 101.70 ? 9   ILE A CG2 1 
ATOM   34   C CD1 . ILE A 1 9   ? -0.594  -55.790 -34.640 1.00 110.18 ? 9   ILE A CD1 1 
ATOM   35   N N   . LEU A 1 10  ? -3.077  -50.781 -32.386 1.00 142.93 ? 10  LEU A N   1 
ATOM   36   C CA  . LEU A 1 10  ? -3.218  -49.612 -31.529 1.00 136.15 ? 10  LEU A CA  1 
ATOM   37   C C   . LEU A 1 10  ? -3.500  -50.056 -30.098 1.00 135.07 ? 10  LEU A C   1 
ATOM   38   O O   . LEU A 1 10  ? -4.569  -50.600 -29.847 1.00 124.64 ? 10  LEU A O   1 
ATOM   39   C CB  . LEU A 1 10  ? -4.334  -48.686 -32.023 1.00 135.23 ? 10  LEU A CB  1 
ATOM   40   C CG  . LEU A 1 10  ? -4.388  -48.387 -33.525 1.00 137.89 ? 10  LEU A CG  1 
ATOM   41   C CD1 . LEU A 1 10  ? -5.638  -47.605 -33.891 1.00 147.23 ? 10  LEU A CD1 1 
ATOM   42   C CD2 . LEU A 1 10  ? -3.158  -47.643 -33.984 1.00 123.95 ? 10  LEU A CD2 1 
ATOM   43   N N   . ILE A 1 11  ? -2.510  -49.854 -29.215 1.00 129.42 ? 11  ILE A N   1 
ATOM   44   C CA  . ILE A 1 11  ? -2.586  -50.252 -27.830 1.00 133.01 ? 11  ILE A CA  1 
ATOM   45   C C   . ILE A 1 11  ? -2.088  -49.027 -27.072 1.00 144.15 ? 11  ILE A C   1 
ATOM   46   O O   . ILE A 1 11  ? -0.893  -48.808 -27.068 1.00 160.83 ? 11  ILE A O   1 
ATOM   47   C CB  . ILE A 1 11  ? -1.658  -51.462 -27.561 1.00 121.99 ? 11  ILE A CB  1 
ATOM   48   C CG1 . ILE A 1 11  ? -1.638  -52.490 -28.707 1.00 126.41 ? 11  ILE A CG1 1 
ATOM   49   C CG2 . ILE A 1 11  ? -1.951  -52.122 -26.212 1.00 119.53 ? 11  ILE A CG2 1 
ATOM   50   C CD1 . ILE A 1 11  ? -0.551  -53.546 -28.579 1.00 125.54 ? 11  ILE A CD1 1 
ATOM   51   N N   . TYR A 1 12  ? -3.029  -48.184 -26.635 1.00 135.30 ? 12  TYR A N   1 
ATOM   52   C CA  . TYR A 1 12  ? -2.720  -46.889 -26.059 1.00 134.06 ? 12  TYR A CA  1 
ATOM   53   C C   . TYR A 1 12  ? -2.858  -47.028 -24.552 1.00 135.86 ? 12  TYR A C   1 
ATOM   54   O O   . TYR A 1 12  ? -3.444  -46.175 -23.895 1.00 166.57 ? 12  TYR A O   1 
ATOM   55   C CB  . TYR A 1 12  ? -3.692  -45.908 -26.726 1.00 140.45 ? 12  TYR A CB  1 
ATOM   56   C CG  . TYR A 1 12  ? -3.239  -44.469 -26.956 1.00 123.69 ? 12  TYR A CG  1 
ATOM   57   C CD1 . TYR A 1 12  ? -3.393  -43.505 -25.964 1.00 118.73 ? 12  TYR A CD1 1 
ATOM   58   C CD2 . TYR A 1 12  ? -2.701  -44.065 -28.181 1.00 114.52 ? 12  TYR A CD2 1 
ATOM   59   C CE1 . TYR A 1 12  ? -2.997  -42.193 -26.178 1.00 133.16 ? 12  TYR A CE1 1 
ATOM   60   C CE2 . TYR A 1 12  ? -2.301  -42.757 -28.407 1.00 111.03 ? 12  TYR A CE2 1 
ATOM   61   C CZ  . TYR A 1 12  ? -2.458  -41.815 -27.403 1.00 131.72 ? 12  TYR A CZ  1 
ATOM   62   O OH  . TYR A 1 12  ? -2.078  -40.510 -27.581 1.00 137.73 ? 12  TYR A OH  1 
ATOM   63   N N   . ALA A 1 13  ? -2.334  -48.143 -24.036 1.00 125.90 ? 13  ALA A N   1 
ATOM   64   C CA  . ALA A 1 13  ? -2.341  -48.457 -22.615 1.00 127.74 ? 13  ALA A CA  1 
ATOM   65   C C   . ALA A 1 13  ? -1.498  -47.455 -21.817 1.00 133.77 ? 13  ALA A C   1 
ATOM   66   O O   . ALA A 1 13  ? -0.394  -47.068 -22.213 1.00 140.92 ? 13  ALA A O   1 
ATOM   67   C CB  . ALA A 1 13  ? -1.844  -49.870 -22.425 1.00 141.80 ? 13  ALA A CB  1 
ATOM   68   N N   . PHE A 1 14  ? -2.038  -47.041 -20.665 1.00 143.22 ? 14  PHE A N   1 
ATOM   69   C CA  . PHE A 1 14  ? -1.326  -46.189 -19.720 1.00 153.17 ? 14  PHE A CA  1 
ATOM   70   C C   . PHE A 1 14  ? -0.631  -47.123 -18.738 1.00 147.72 ? 14  PHE A C   1 
ATOM   71   O O   . PHE A 1 14  ? -1.227  -47.558 -17.745 1.00 144.65 ? 14  PHE A O   1 
ATOM   72   C CB  . PHE A 1 14  ? -2.178  -45.129 -18.999 1.00 191.52 ? 14  PHE A CB  1 
ATOM   73   C CG  . PHE A 1 14  ? -2.638  -43.902 -19.787 1.00 211.05 ? 14  PHE A CG  1 
ATOM   74   C CD1 . PHE A 1 14  ? -2.879  -43.950 -21.164 1.00 202.73 ? 14  PHE A CD1 1 
ATOM   75   C CD2 . PHE A 1 14  ? -2.864  -42.693 -19.135 1.00 217.34 ? 14  PHE A CD2 1 
ATOM   76   C CE1 . PHE A 1 14  ? -3.319  -42.826 -21.866 1.00 168.93 ? 14  PHE A CE1 1 
ATOM   77   C CE2 . PHE A 1 14  ? -3.287  -41.567 -19.841 1.00 207.58 ? 14  PHE A CE2 1 
ATOM   78   C CZ  . PHE A 1 14  ? -3.526  -41.636 -21.202 1.00 176.16 ? 14  PHE A CZ  1 
ATOM   79   N N   . ASN A 1 15  ? 0.615   -47.462 -19.088 1.00 157.45 ? 15  ASN A N   1 
ATOM   80   C CA  . ASN A 1 15  ? 1.417   -48.478 -18.417 1.00 160.53 ? 15  ASN A CA  1 
ATOM   81   C C   . ASN A 1 15  ? 2.135   -47.841 -17.228 1.00 159.11 ? 15  ASN A C   1 
ATOM   82   O O   . ASN A 1 15  ? 2.271   -48.461 -16.172 1.00 161.10 ? 15  ASN A O   1 
ATOM   83   C CB  . ASN A 1 15  ? 2.299   -49.249 -19.411 1.00 148.49 ? 15  ASN A CB  1 
ATOM   84   C CG  . ASN A 1 15  ? 2.613   -48.460 -20.668 1.00 151.51 ? 15  ASN A CG  1 
ATOM   85   O OD1 . ASN A 1 15  ? 2.912   -47.262 -20.594 1.00 155.72 ? 15  ASN A OD1 1 
ATOM   86   N ND2 . ASN A 1 15  ? 2.531   -49.091 -21.836 1.00 144.17 ? 15  ASN A ND2 1 
ATOM   87   N N   . TYR A 1 16  ? 2.544   -46.579 -17.406 1.00 170.76 ? 16  TYR A N   1 
ATOM   88   C CA  . TYR A 1 16  ? 3.305   -45.821 -16.425 1.00 186.78 ? 16  TYR A CA  1 
ATOM   89   C C   . TYR A 1 16  ? 2.400   -45.424 -15.252 1.00 206.22 ? 16  TYR A C   1 
ATOM   90   O O   . TYR A 1 16  ? 2.869   -44.818 -14.291 1.00 214.19 ? 16  TYR A O   1 
ATOM   91   C CB  . TYR A 1 16  ? 3.966   -44.654 -17.174 1.00 182.64 ? 16  TYR A CB  1 
ATOM   92   C CG  . TYR A 1 16  ? 2.955   -43.631 -17.678 1.00 195.36 ? 16  TYR A CG  1 
ATOM   93   C CD1 . TYR A 1 16  ? 2.243   -43.849 -18.855 1.00 199.07 ? 16  TYR A CD1 1 
ATOM   94   C CD2 . TYR A 1 16  ? 2.687   -42.467 -16.959 1.00 191.83 ? 16  TYR A CD2 1 
ATOM   95   C CE1 . TYR A 1 16  ? 1.293   -42.943 -19.296 1.00 200.66 ? 16  TYR A CE1 1 
ATOM   96   C CE2 . TYR A 1 16  ? 1.735   -41.558 -17.391 1.00 184.62 ? 16  TYR A CE2 1 
ATOM   97   C CZ  . TYR A 1 16  ? 1.041   -41.794 -18.566 1.00 204.20 ? 16  TYR A CZ  1 
ATOM   98   O OH  . TYR A 1 16  ? 0.115   -40.889 -19.003 1.00 227.99 ? 16  TYR A OH  1 
ATOM   99   N N   . ALA A 1 17  ? 1.102   -45.761 -15.345 1.00 235.76 ? 17  ALA A N   1 
ATOM   100  C CA  . ALA A 1 17  ? 0.143   -45.534 -14.275 1.00 238.86 ? 17  ALA A CA  1 
ATOM   101  C C   . ALA A 1 17  ? -0.203  -46.877 -13.633 1.00 234.47 ? 17  ALA A C   1 
ATOM   102  O O   . ALA A 1 17  ? -1.126  -47.563 -14.068 1.00 221.12 ? 17  ALA A O   1 
ATOM   103  C CB  . ALA A 1 17  ? -1.089  -44.804 -14.799 1.00 218.42 ? 17  ALA A CB  1 
ATOM   104  N N   . ASP A 1 18  ? 0.582   -47.258 -12.618 1.00 235.53 ? 18  ASP A N   1 
ATOM   105  C CA  . ASP A 1 18  ? 0.413   -48.528 -11.928 1.00 247.83 ? 18  ASP A CA  1 
ATOM   106  C C   . ASP A 1 18  ? -0.651  -48.405 -10.841 1.00 238.45 ? 18  ASP A C   1 
ATOM   107  O O   . ASP A 1 18  ? -1.324  -49.389 -10.540 1.00 238.40 ? 18  ASP A O   1 
ATOM   108  C CB  . ASP A 1 18  ? 1.728   -49.078 -11.388 1.00 255.12 ? 18  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 18  ? 2.293   -50.311 -12.084 1.00 237.40 ? 18  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 18  ? 1.667   -50.772 -13.067 1.00 221.29 ? 18  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 18  ? 3.327   -50.830 -11.603 1.00 219.59 ? 18  ASP A OD2 1 
ATOM   112  N N   . ARG A 1 19  ? -0.778  -47.196 -10.271 1.00 226.64 ? 19  ARG A N   1 
ATOM   113  C CA  . ARG A 1 19  ? -1.707  -46.896 -9.185  1.00 244.98 ? 19  ARG A CA  1 
ATOM   114  C C   . ARG A 1 19  ? -2.980  -46.285 -9.773  1.00 262.23 ? 19  ARG A C   1 
ATOM   115  O O   . ARG A 1 19  ? -4.081  -46.735 -9.485  1.00 249.59 ? 19  ARG A O   1 
ATOM   116  C CB  . ARG A 1 19  ? -1.042  -46.113 -8.031  1.00 261.03 ? 19  ARG A CB  1 
ATOM   117  C CG  . ARG A 1 19  ? -1.836  -45.122 -7.180  1.00 245.19 ? 19  ARG A CG  1 
ATOM   118  C CD  . ARG A 1 19  ? -0.935  -44.277 -6.287  1.00 222.48 ? 19  ARG A CD  1 
ATOM   119  N NE  . ARG A 1 19  ? 0.431   -44.515 -6.769  1.00 218.87 ? 19  ARG A NE  1 
ATOM   120  C CZ  . ARG A 1 19  ? 1.287   -45.316 -6.148  1.00 218.38 ? 19  ARG A CZ  1 
ATOM   121  N NH1 . ARG A 1 19  ? 1.251   -45.473 -4.843  1.00 206.25 ? 19  ARG A NH1 1 
ATOM   122  N NH2 . ARG A 1 19  ? 2.266   -45.884 -6.829  1.00 218.16 ? 19  ARG A NH2 1 
ATOM   123  N N   . MET A 1 20  ? -2.807  -45.296 -10.649 1.00 282.73 ? 20  MET A N   1 
ATOM   124  C CA  . MET A 1 20  ? -3.910  -44.433 -11.027 1.00 273.60 ? 20  MET A CA  1 
ATOM   125  C C   . MET A 1 20  ? -5.042  -45.236 -11.668 1.00 319.55 ? 20  MET A C   1 
ATOM   126  O O   . MET A 1 20  ? -6.207  -44.975 -11.377 1.00 371.67 ? 20  MET A O   1 
ATOM   127  C CB  . MET A 1 20  ? -3.416  -43.213 -11.809 1.00 231.09 ? 20  MET A CB  1 
ATOM   128  C CG  . MET A 1 20  ? -2.516  -42.358 -10.941 1.00 213.21 ? 20  MET A CG  1 
ATOM   129  S SD  . MET A 1 20  ? -2.798  -40.582 -11.081 1.00 250.19 ? 20  MET A SD  1 
ATOM   130  C CE  . MET A 1 20  ? -4.416  -40.195 -10.390 1.00 233.05 ? 20  MET A CE  1 
ATOM   131  N N   . LEU A 1 21  ? -4.687  -46.272 -12.445 1.00 310.54 ? 21  LEU A N   1 
ATOM   132  C CA  . LEU A 1 21  ? -5.640  -47.197 -13.051 1.00 277.15 ? 21  LEU A CA  1 
ATOM   133  C C   . LEU A 1 21  ? -6.602  -47.728 -11.981 1.00 282.96 ? 21  LEU A C   1 
ATOM   134  O O   . LEU A 1 21  ? -7.808  -47.823 -12.214 1.00 282.10 ? 21  LEU A O   1 
ATOM   135  C CB  . LEU A 1 21  ? -4.859  -48.292 -13.794 1.00 198.79 ? 21  LEU A CB  1 
ATOM   136  C CG  . LEU A 1 21  ? -5.569  -49.148 -14.861 1.00 152.10 ? 21  LEU A CG  1 
ATOM   137  C CD1 . LEU A 1 21  ? -6.950  -48.701 -15.364 1.00 158.52 ? 21  LEU A CD1 1 
ATOM   138  C CD2 . LEU A 1 21  ? -4.635  -49.265 -16.067 1.00 109.84 ? 21  LEU A CD2 1 
ATOM   139  N N   . GLU A 1 22  ? -6.077  -47.993 -10.776 1.00 272.62 ? 22  GLU A N   1 
ATOM   140  C CA  . GLU A 1 22  ? -6.879  -48.523 -9.682  1.00 258.39 ? 22  GLU A CA  1 
ATOM   141  C C   . GLU A 1 22  ? -7.660  -47.416 -8.965  1.00 280.01 ? 22  GLU A C   1 
ATOM   142  O O   . GLU A 1 22  ? -8.426  -47.711 -8.050  1.00 299.75 ? 22  GLU A O   1 
ATOM   143  C CB  . GLU A 1 22  ? -6.027  -49.324 -8.697  1.00 236.08 ? 22  GLU A CB  1 
ATOM   144  C CG  . GLU A 1 22  ? -5.176  -50.412 -9.343  1.00 244.48 ? 22  GLU A CG  1 
ATOM   145  C CD  . GLU A 1 22  ? -4.344  -51.170 -8.326  1.00 254.41 ? 22  GLU A CD  1 
ATOM   146  O OE1 . GLU A 1 22  ? -3.695  -50.533 -7.468  1.00 250.67 ? 22  GLU A OE1 1 
ATOM   147  O OE2 . GLU A 1 22  ? -4.321  -52.410 -8.416  1.00 280.84 ? 22  GLU A OE2 1 
ATOM   148  N N   . GLU A 1 23  ? -7.470  -46.150 -9.371  1.00 284.70 ? 23  GLU A N   1 
ATOM   149  C CA  . GLU A 1 23  ? -8.126  -45.010 -8.735  1.00 261.55 ? 23  GLU A CA  1 
ATOM   150  C C   . GLU A 1 23  ? -9.069  -44.324 -9.730  1.00 222.06 ? 23  GLU A C   1 
ATOM   151  O O   . GLU A 1 23  ? -10.263 -44.614 -9.758  1.00 207.00 ? 23  GLU A O   1 
ATOM   152  C CB  . GLU A 1 23  ? -7.137  -44.018 -8.113  1.00 279.53 ? 23  GLU A CB  1 
ATOM   153  C CG  . GLU A 1 23  ? -6.095  -44.640 -7.186  1.00 288.65 ? 23  GLU A CG  1 
ATOM   154  C CD  . GLU A 1 23  ? -6.587  -45.615 -6.132  1.00 309.21 ? 23  GLU A CD  1 
ATOM   155  O OE1 . GLU A 1 23  ? -7.411  -45.208 -5.292  1.00 305.97 ? 23  GLU A OE1 1 
ATOM   156  O OE2 . GLU A 1 23  ? -6.146  -46.780 -6.142  1.00 327.36 ? 23  GLU A OE2 1 
ATOM   157  N N   . VAL A 1 24  ? -8.534  -43.392 -10.529 1.00 205.38 ? 24  VAL A N   1 
ATOM   158  C CA  . VAL A 1 24  ? -9.295  -42.789 -11.615 1.00 176.41 ? 24  VAL A CA  1 
ATOM   159  C C   . VAL A 1 24  ? -9.814  -43.918 -12.497 1.00 173.61 ? 24  VAL A C   1 
ATOM   160  O O   . VAL A 1 24  ? -9.027  -44.716 -13.002 1.00 164.87 ? 24  VAL A O   1 
ATOM   161  C CB  . VAL A 1 24  ? -8.526  -41.728 -12.422 1.00 173.39 ? 24  VAL A CB  1 
ATOM   162  C CG1 . VAL A 1 24  ? -8.447  -40.416 -11.647 1.00 175.75 ? 24  VAL A CG1 1 
ATOM   163  C CG2 . VAL A 1 24  ? -7.140  -42.212 -12.826 1.00 163.09 ? 24  VAL A CG2 1 
ATOM   164  N N   . PRO A 1 25  ? -11.154 -44.081 -12.606 1.00 182.21 ? 25  PRO A N   1 
ATOM   165  C CA  . PRO A 1 25  ? -11.738 -45.307 -13.159 1.00 179.60 ? 25  PRO A CA  1 
ATOM   166  C C   . PRO A 1 25  ? -11.977 -45.213 -14.662 1.00 159.72 ? 25  PRO A C   1 
ATOM   167  O O   . PRO A 1 25  ? -11.983 -46.223 -15.371 1.00 148.16 ? 25  PRO A O   1 
ATOM   168  C CB  . PRO A 1 25  ? -13.046 -45.445 -12.372 1.00 155.61 ? 25  PRO A CB  1 
ATOM   169  C CG  . PRO A 1 25  ? -13.415 -44.008 -12.035 1.00 172.37 ? 25  PRO A CG  1 
ATOM   170  C CD  . PRO A 1 25  ? -12.178 -43.120 -12.173 1.00 160.91 ? 25  PRO A CD  1 
ATOM   171  N N   . TYR A 1 26  ? -12.156 -43.977 -15.134 1.00 141.25 ? 26  TYR A N   1 
ATOM   172  C CA  . TYR A 1 26  ? -12.418 -43.714 -16.537 1.00 135.82 ? 26  TYR A CA  1 
ATOM   173  C C   . TYR A 1 26  ? -11.178 -44.082 -17.338 1.00 134.67 ? 26  TYR A C   1 
ATOM   174  O O   . TYR A 1 26  ? -11.153 -43.900 -18.553 1.00 131.69 ? 26  TYR A O   1 
ATOM   175  C CB  . TYR A 1 26  ? -12.824 -42.246 -16.717 1.00 143.41 ? 26  TYR A CB  1 
ATOM   176  C CG  . TYR A 1 26  ? -11.747 -41.235 -16.359 1.00 139.01 ? 26  TYR A CG  1 
ATOM   177  C CD1 . TYR A 1 26  ? -10.810 -40.829 -17.300 1.00 136.88 ? 26  TYR A CD1 1 
ATOM   178  C CD2 . TYR A 1 26  ? -11.655 -40.715 -15.075 1.00 145.10 ? 26  TYR A CD2 1 
ATOM   179  C CE1 . TYR A 1 26  ? -9.818  -39.918 -16.975 1.00 167.19 ? 26  TYR A CE1 1 
ATOM   180  C CE2 . TYR A 1 26  ? -10.672 -39.801 -14.739 1.00 176.67 ? 26  TYR A CE2 1 
ATOM   181  C CZ  . TYR A 1 26  ? -9.753  -39.397 -15.693 1.00 191.05 ? 26  TYR A CZ  1 
ATOM   182  O OH  . TYR A 1 26  ? -8.787  -38.485 -15.360 1.00 234.07 ? 26  TYR A OH  1 
ATOM   183  N N   . LEU A 1 27  ? -10.148 -44.565 -16.630 1.00 141.13 ? 27  LEU A N   1 
ATOM   184  C CA  . LEU A 1 27  ? -8.877  -44.905 -17.245 1.00 144.90 ? 27  LEU A CA  1 
ATOM   185  C C   . LEU A 1 27  ? -9.055  -46.142 -18.115 1.00 137.78 ? 27  LEU A C   1 
ATOM   186  O O   . LEU A 1 27  ? -8.420  -46.264 -19.162 1.00 137.42 ? 27  LEU A O   1 
ATOM   187  C CB  . LEU A 1 27  ? -7.704  -45.067 -16.279 1.00 139.20 ? 27  LEU A CB  1 
ATOM   188  C CG  . LEU A 1 27  ? -6.888  -43.805 -15.968 1.00 158.48 ? 27  LEU A CG  1 
ATOM   189  C CD1 . LEU A 1 27  ? -5.394  -44.148 -15.855 1.00 182.72 ? 27  LEU A CD1 1 
ATOM   190  C CD2 . LEU A 1 27  ? -7.106  -42.609 -16.887 1.00 183.49 ? 27  LEU A CD2 1 
ATOM   191  N N   . ARG A 1 28  ? -9.923  -47.056 -17.684 1.00 133.37 ? 28  ARG A N   1 
ATOM   192  C CA  . ARG A 1 28  ? -10.086 -48.246 -18.497 1.00 144.64 ? 28  ARG A CA  1 
ATOM   193  C C   . ARG A 1 28  ? -10.513 -47.853 -19.918 1.00 145.20 ? 28  ARG A C   1 
ATOM   194  O O   . ARG A 1 28  ? -10.161 -48.543 -20.876 1.00 145.87 ? 28  ARG A O   1 
ATOM   195  C CB  . ARG A 1 28  ? -10.848 -49.358 -17.767 1.00 140.19 ? 28  ARG A CB  1 
ATOM   196  C CG  . ARG A 1 28  ? -12.264 -49.007 -17.356 1.00 153.62 ? 28  ARG A CG  1 
ATOM   197  C CD  . ARG A 1 28  ? -13.016 -50.321 -17.276 1.00 172.73 ? 28  ARG A CD  1 
ATOM   198  N NE  . ARG A 1 28  ? -12.370 -51.283 -16.377 1.00 193.25 ? 28  ARG A NE  1 
ATOM   199  C CZ  . ARG A 1 28  ? -12.805 -52.525 -16.178 1.00 214.15 ? 28  ARG A CZ  1 
ATOM   200  N NH1 . ARG A 1 28  ? -13.859 -52.990 -16.838 1.00 217.71 ? 28  ARG A NH1 1 
ATOM   201  N NH2 . ARG A 1 28  ? -12.168 -53.299 -15.321 1.00 208.91 ? 28  ARG A NH2 1 
ATOM   202  N N   . TYR A 1 29  ? -11.216 -46.716 -20.060 1.00 134.17 ? 29  TYR A N   1 
ATOM   203  C CA  . TYR A 1 29  ? -11.727 -46.270 -21.351 1.00 118.75 ? 29  TYR A CA  1 
ATOM   204  C C   . TYR A 1 29  ? -10.716 -45.402 -22.101 1.00 108.87 ? 29  TYR A C   1 
ATOM   205  O O   . TYR A 1 29  ? -11.012 -44.952 -23.212 1.00 90.23  ? 29  TYR A O   1 
ATOM   206  C CB  . TYR A 1 29  ? -13.104 -45.623 -21.221 1.00 104.96 ? 29  TYR A CB  1 
ATOM   207  C CG  . TYR A 1 29  ? -14.186 -46.610 -20.797 1.00 129.45 ? 29  TYR A CG  1 
ATOM   208  C CD1 . TYR A 1 29  ? -14.451 -46.841 -19.448 1.00 143.26 ? 29  TYR A CD1 1 
ATOM   209  C CD2 . TYR A 1 29  ? -14.948 -47.310 -21.735 1.00 147.16 ? 29  TYR A CD2 1 
ATOM   210  C CE1 . TYR A 1 29  ? -15.431 -47.739 -19.044 1.00 162.75 ? 29  TYR A CE1 1 
ATOM   211  C CE2 . TYR A 1 29  ? -15.944 -48.194 -21.336 1.00 181.44 ? 29  TYR A CE2 1 
ATOM   212  C CZ  . TYR A 1 29  ? -16.194 -48.413 -19.988 1.00 179.83 ? 29  TYR A CZ  1 
ATOM   213  O OH  . TYR A 1 29  ? -17.178 -49.302 -19.607 1.00 161.45 ? 29  TYR A OH  1 
ATOM   214  N N   . SER A 1 30  ? -9.518  -45.231 -21.519 1.00 107.79 ? 30  SER A N   1 
ATOM   215  C CA  . SER A 1 30  ? -8.473  -44.372 -22.062 1.00 113.06 ? 30  SER A CA  1 
ATOM   216  C C   . SER A 1 30  ? -8.130  -44.737 -23.501 1.00 114.69 ? 30  SER A C   1 
ATOM   217  O O   . SER A 1 30  ? -7.955  -43.838 -24.327 1.00 108.58 ? 30  SER A O   1 
ATOM   218  C CB  . SER A 1 30  ? -7.221  -44.417 -21.233 1.00 121.13 ? 30  SER A CB  1 
ATOM   219  O OG  . SER A 1 30  ? -7.432  -43.741 -20.007 1.00 146.95 ? 30  SER A OG  1 
ATOM   220  N N   . ALA A 1 31  ? -8.004  -46.045 -23.773 1.00 113.44 ? 31  ALA A N   1 
ATOM   221  C CA  . ALA A 1 31  ? -7.491  -46.488 -25.058 1.00 116.82 ? 31  ALA A CA  1 
ATOM   222  C C   . ALA A 1 31  ? -8.289  -45.854 -26.189 1.00 127.12 ? 31  ALA A C   1 
ATOM   223  O O   . ALA A 1 31  ? -7.742  -45.663 -27.270 1.00 148.17 ? 31  ALA A O   1 
ATOM   224  C CB  . ALA A 1 31  ? -7.504  -47.991 -25.165 1.00 106.29 ? 31  ALA A CB  1 
ATOM   225  N N   . GLU A 1 32  ? -9.571  -45.549 -25.929 1.00 116.03 ? 32  GLU A N   1 
ATOM   226  C CA  . GLU A 1 32  ? -10.433 -45.026 -26.976 1.00 120.12 ? 32  GLU A CA  1 
ATOM   227  C C   . GLU A 1 32  ? -9.751  -43.838 -27.677 1.00 116.54 ? 32  GLU A C   1 
ATOM   228  O O   . GLU A 1 32  ? -10.026 -43.517 -28.846 1.00 100.07 ? 32  GLU A O   1 
ATOM   229  C CB  . GLU A 1 32  ? -11.829 -44.757 -26.413 1.00 130.86 ? 32  GLU A CB  1 
ATOM   230  C CG  . GLU A 1 32  ? -12.842 -45.872 -26.658 1.00 161.98 ? 32  GLU A CG  1 
ATOM   231  C CD  . GLU A 1 32  ? -14.302 -45.446 -26.520 1.00 210.94 ? 32  GLU A CD  1 
ATOM   232  O OE1 . GLU A 1 32  ? -14.751 -44.457 -27.159 1.00 201.93 ? 32  GLU A OE1 1 
ATOM   233  O OE2 . GLU A 1 32  ? -15.016 -46.139 -25.759 1.00 246.85 ? 32  GLU A OE2 1 
ATOM   234  N N   . ARG A 1 33  ? -8.809  -43.203 -26.962 1.00 104.79 ? 33  ARG A N   1 
ATOM   235  C CA  . ARG A 1 33  ? -8.090  -42.059 -27.506 1.00 97.34  ? 33  ARG A CA  1 
ATOM   236  C C   . ARG A 1 33  ? -7.559  -42.417 -28.890 1.00 92.77  ? 33  ARG A C   1 
ATOM   237  O O   . ARG A 1 33  ? -7.552  -41.584 -29.793 1.00 89.15  ? 33  ARG A O   1 
ATOM   238  C CB  . ARG A 1 33  ? -6.996  -41.521 -26.572 1.00 91.12  ? 33  ARG A CB  1 
ATOM   239  C CG  . ARG A 1 33  ? -7.572  -40.914 -25.299 1.00 91.63  ? 33  ARG A CG  1 
ATOM   240  C CD  . ARG A 1 33  ? -6.554  -40.329 -24.332 1.00 104.27 ? 33  ARG A CD  1 
ATOM   241  N NE  . ARG A 1 33  ? -7.184  -39.502 -23.293 1.00 115.49 ? 33  ARG A NE  1 
ATOM   242  C CZ  . ARG A 1 33  ? -7.280  -39.787 -21.990 1.00 124.93 ? 33  ARG A CZ  1 
ATOM   243  N NH1 . ARG A 1 33  ? -6.769  -40.903 -21.494 1.00 131.53 ? 33  ARG A NH1 1 
ATOM   244  N NH2 . ARG A 1 33  ? -7.919  -38.961 -21.181 1.00 140.22 ? 33  ARG A NH2 1 
ATOM   245  N N   . SER A 1 34  ? -7.163  -43.683 -29.041 1.00 92.44  ? 34  SER A N   1 
ATOM   246  C CA  . SER A 1 34  ? -6.474  -44.138 -30.234 1.00 102.00 ? 34  SER A CA  1 
ATOM   247  C C   . SER A 1 34  ? -7.335  -43.938 -31.476 1.00 108.92 ? 34  SER A C   1 
ATOM   248  O O   . SER A 1 34  ? -6.834  -44.041 -32.599 1.00 118.82 ? 34  SER A O   1 
ATOM   249  C CB  . SER A 1 34  ? -5.946  -45.555 -30.113 1.00 112.52 ? 34  SER A CB  1 
ATOM   250  O OG  . SER A 1 34  ? -6.831  -46.436 -29.433 1.00 125.61 ? 34  SER A OG  1 
ATOM   251  N N   . LEU A 1 35  ? -8.618  -43.608 -31.269 1.00 103.24 ? 35  LEU A N   1 
ATOM   252  C CA  . LEU A 1 35  ? -9.561  -43.564 -32.377 1.00 113.99 ? 35  LEU A CA  1 
ATOM   253  C C   . LEU A 1 35  ? -9.342  -42.319 -33.233 1.00 115.27 ? 35  LEU A C   1 
ATOM   254  O O   . LEU A 1 35  ? -10.094 -42.059 -34.171 1.00 123.10 ? 35  LEU A O   1 
ATOM   255  C CB  . LEU A 1 35  ? -10.966 -43.615 -31.795 1.00 120.78 ? 35  LEU A CB  1 
ATOM   256  C CG  . LEU A 1 35  ? -11.428 -45.000 -31.346 1.00 111.35 ? 35  LEU A CG  1 
ATOM   257  C CD1 . LEU A 1 35  ? -12.643 -44.860 -30.465 1.00 127.97 ? 35  LEU A CD1 1 
ATOM   258  C CD2 . LEU A 1 35  ? -11.798 -45.696 -32.629 1.00 98.84  ? 35  LEU A CD2 1 
ATOM   259  N N   . CYS A 1 36  ? -8.307  -41.551 -32.893 1.00 98.48  ? 36  CYS A N   1 
ATOM   260  C CA  . CYS A 1 36  ? -7.955  -40.373 -33.655 1.00 98.40  ? 36  CYS A CA  1 
ATOM   261  C C   . CYS A 1 36  ? -7.141  -40.782 -34.871 1.00 104.78 ? 36  CYS A C   1 
ATOM   262  O O   . CYS A 1 36  ? -6.942  -39.980 -35.784 1.00 108.77 ? 36  CYS A O   1 
ATOM   263  C CB  . CYS A 1 36  ? -7.077  -39.477 -32.810 1.00 102.99 ? 36  CYS A CB  1 
ATOM   264  S SG  . CYS A 1 36  ? -6.056  -40.479 -31.718 1.00 101.32 ? 36  CYS A SG  1 
ATOM   265  N N   . PHE A 1 37  ? -6.705  -42.046 -34.876 1.00 120.99 ? 37  PHE A N   1 
ATOM   266  C CA  . PHE A 1 37  ? -5.767  -42.538 -35.873 1.00 145.05 ? 37  PHE A CA  1 
ATOM   267  C C   . PHE A 1 37  ? -6.477  -43.065 -37.122 1.00 150.87 ? 37  PHE A C   1 
ATOM   268  O O   . PHE A 1 37  ? -5.843  -43.293 -38.160 1.00 165.09 ? 37  PHE A O   1 
ATOM   269  C CB  . PHE A 1 37  ? -4.836  -43.571 -35.239 1.00 147.76 ? 37  PHE A CB  1 
ATOM   270  C CG  . PHE A 1 37  ? -3.854  -42.990 -34.232 1.00 144.05 ? 37  PHE A CG  1 
ATOM   271  C CD1 . PHE A 1 37  ? -2.653  -42.430 -34.651 1.00 158.23 ? 37  PHE A CD1 1 
ATOM   272  C CD2 . PHE A 1 37  ? -4.121  -43.029 -32.868 1.00 137.41 ? 37  PHE A CD2 1 
ATOM   273  C CE1 . PHE A 1 37  ? -1.756  -41.921 -33.717 1.00 165.48 ? 37  PHE A CE1 1 
ATOM   274  C CE2 . PHE A 1 37  ? -3.220  -42.519 -31.941 1.00 138.61 ? 37  PHE A CE2 1 
ATOM   275  C CZ  . PHE A 1 37  ? -2.037  -41.969 -32.364 1.00 142.13 ? 37  PHE A CZ  1 
ATOM   276  N N   . LEU A 1 38  ? -7.799  -43.229 -37.010 1.00 141.92 ? 38  LEU A N   1 
ATOM   277  C CA  . LEU A 1 38  ? -8.600  -43.789 -38.087 1.00 140.63 ? 38  LEU A CA  1 
ATOM   278  C C   . LEU A 1 38  ? -8.359  -43.029 -39.399 1.00 132.53 ? 38  LEU A C   1 
ATOM   279  O O   . LEU A 1 38  ? -8.599  -43.570 -40.477 1.00 124.84 ? 38  LEU A O   1 
ATOM   280  C CB  . LEU A 1 38  ? -10.079 -43.850 -37.685 1.00 139.91 ? 38  LEU A CB  1 
ATOM   281  C CG  . LEU A 1 38  ? -10.412 -44.572 -36.366 1.00 123.53 ? 38  LEU A CG  1 
ATOM   282  C CD1 . LEU A 1 38  ? -11.877 -44.507 -36.026 1.00 105.88 ? 38  LEU A CD1 1 
ATOM   283  C CD2 . LEU A 1 38  ? -10.002 -46.025 -36.336 1.00 144.81 ? 38  LEU A CD2 1 
ATOM   284  N N   . GLY A 1 39  ? -7.878  -41.778 -39.306 1.00 139.80 ? 39  GLY A N   1 
ATOM   285  C CA  . GLY A 1 39  ? -7.541  -40.980 -40.477 1.00 151.52 ? 39  GLY A CA  1 
ATOM   286  C C   . GLY A 1 39  ? -6.638  -41.753 -41.442 1.00 160.40 ? 39  GLY A C   1 
ATOM   287  O O   . GLY A 1 39  ? -6.722  -41.594 -42.664 1.00 147.44 ? 39  GLY A O   1 
ATOM   288  N N   . ASP A 1 40  ? -5.782  -42.603 -40.856 1.00 175.03 ? 40  ASP A N   1 
ATOM   289  C CA  . ASP A 1 40  ? -4.789  -43.371 -41.592 1.00 175.39 ? 40  ASP A CA  1 
ATOM   290  C C   . ASP A 1 40  ? -5.467  -44.237 -42.650 1.00 170.96 ? 40  ASP A C   1 
ATOM   291  O O   . ASP A 1 40  ? -4.909  -44.448 -43.725 1.00 203.61 ? 40  ASP A O   1 
ATOM   292  C CB  . ASP A 1 40  ? -3.869  -44.162 -40.671 1.00 182.24 ? 40  ASP A CB  1 
ATOM   293  C CG  . ASP A 1 40  ? -2.975  -43.334 -39.754 1.00 181.29 ? 40  ASP A CG  1 
ATOM   294  O OD1 . ASP A 1 40  ? -3.173  -42.098 -39.689 1.00 184.17 ? 40  ASP A OD1 1 
ATOM   295  O OD2 . ASP A 1 40  ? -2.071  -43.927 -39.120 1.00 167.16 ? 40  ASP A OD2 1 
ATOM   296  N N   . LEU A 1 41  ? -6.682  -44.712 -42.355 1.00 156.70 ? 41  LEU A N   1 
ATOM   297  C CA  . LEU A 1 41  ? -7.386  -45.597 -43.272 1.00 151.04 ? 41  LEU A CA  1 
ATOM   298  C C   . LEU A 1 41  ? -7.644  -44.912 -44.620 1.00 155.01 ? 41  LEU A C   1 
ATOM   299  O O   . LEU A 1 41  ? -8.097  -45.573 -45.553 1.00 160.24 ? 41  LEU A O   1 
ATOM   300  C CB  . LEU A 1 41  ? -8.659  -46.180 -42.663 1.00 144.86 ? 41  LEU A CB  1 
ATOM   301  C CG  . LEU A 1 41  ? -8.478  -47.336 -41.672 1.00 144.54 ? 41  LEU A CG  1 
ATOM   302  C CD1 . LEU A 1 41  ? -9.753  -47.636 -40.889 1.00 133.40 ? 41  LEU A CD1 1 
ATOM   303  C CD2 . LEU A 1 41  ? -8.036  -48.583 -42.400 1.00 148.03 ? 41  LEU A CD2 1 
ATOM   304  N N   . ARG A 1 42  ? -7.314  -43.610 -44.727 1.00 147.13 ? 42  ARG A N   1 
ATOM   305  C CA  . ARG A 1 42  ? -7.372  -42.869 -45.983 1.00 146.90 ? 42  ARG A CA  1 
ATOM   306  C C   . ARG A 1 42  ? -6.415  -43.447 -47.032 1.00 169.47 ? 42  ARG A C   1 
ATOM   307  O O   . ARG A 1 42  ? -6.713  -43.371 -48.223 1.00 161.71 ? 42  ARG A O   1 
ATOM   308  C CB  . ARG A 1 42  ? -7.154  -41.361 -45.826 1.00 156.42 ? 42  ARG A CB  1 
ATOM   309  C CG  . ARG A 1 42  ? -8.360  -40.635 -45.243 1.00 198.51 ? 42  ARG A CG  1 
ATOM   310  C CD  . ARG A 1 42  ? -8.451  -39.153 -45.607 1.00 214.68 ? 42  ARG A CD  1 
ATOM   311  N NE  . ARG A 1 42  ? -9.753  -38.576 -45.242 1.00 235.58 ? 42  ARG A NE  1 
ATOM   312  C CZ  . ARG A 1 42  ? -10.958 -38.898 -45.729 1.00 244.25 ? 42  ARG A CZ  1 
ATOM   313  N NH1 . ARG A 1 42  ? -11.092 -39.769 -46.715 1.00 249.11 ? 42  ARG A NH1 1 
ATOM   314  N NH2 . ARG A 1 42  ? -12.044 -38.335 -45.237 1.00 239.00 ? 42  ARG A NH2 1 
ATOM   315  N N   . ASP A 1 43  ? -5.258  -43.979 -46.595 1.00 198.84 ? 43  ASP A N   1 
ATOM   316  C CA  . ASP A 1 43  ? -4.374  -44.753 -47.464 1.00 184.05 ? 43  ASP A CA  1 
ATOM   317  C C   . ASP A 1 43  ? -5.024  -46.100 -47.760 1.00 166.26 ? 43  ASP A C   1 
ATOM   318  O O   . ASP A 1 43  ? -5.309  -46.853 -46.828 1.00 154.64 ? 43  ASP A O   1 
ATOM   319  C CB  . ASP A 1 43  ? -2.970  -44.957 -46.906 1.00 173.68 ? 43  ASP A CB  1 
ATOM   320  C CG  . ASP A 1 43  ? -2.170  -46.099 -47.534 1.00 174.55 ? 43  ASP A CG  1 
ATOM   321  O OD1 . ASP A 1 43  ? -2.031  -46.132 -48.783 1.00 174.78 ? 43  ASP A OD1 1 
ATOM   322  O OD2 . ASP A 1 43  ? -1.695  -46.971 -46.776 1.00 166.41 ? 43  ASP A OD2 1 
ATOM   323  N N   . PRO A 1 44  ? -5.254  -46.427 -49.055 1.00 163.17 ? 44  PRO A N   1 
ATOM   324  C CA  . PRO A 1 44  ? -5.898  -47.682 -49.446 1.00 157.62 ? 44  PRO A CA  1 
ATOM   325  C C   . PRO A 1 44  ? -5.261  -48.912 -48.808 1.00 167.77 ? 44  PRO A C   1 
ATOM   326  O O   . PRO A 1 44  ? -5.918  -49.942 -48.667 1.00 175.89 ? 44  PRO A O   1 
ATOM   327  C CB  . PRO A 1 44  ? -5.772  -47.741 -50.989 1.00 155.27 ? 44  PRO A CB  1 
ATOM   328  C CG  . PRO A 1 44  ? -5.262  -46.380 -51.435 1.00 163.21 ? 44  PRO A CG  1 
ATOM   329  C CD  . PRO A 1 44  ? -4.889  -45.587 -50.208 1.00 165.89 ? 44  PRO A CD  1 
ATOM   330  N N   . GLY A 1 45  ? -3.977  -48.787 -48.448 1.00 157.79 ? 45  GLY A N   1 
ATOM   331  C CA  . GLY A 1 45  ? -3.168  -49.907 -47.998 1.00 142.47 ? 45  GLY A CA  1 
ATOM   332  C C   . GLY A 1 45  ? -3.311  -50.181 -46.504 1.00 125.41 ? 45  GLY A C   1 
ATOM   333  O O   . GLY A 1 45  ? -3.408  -51.340 -46.096 1.00 123.78 ? 45  GLY A O   1 
ATOM   334  N N   . THR A 1 46  ? -3.304  -49.103 -45.715 1.00 118.32 ? 46  THR A N   1 
ATOM   335  C CA  . THR A 1 46  ? -3.325  -49.183 -44.267 1.00 121.41 ? 46  THR A CA  1 
ATOM   336  C C   . THR A 1 46  ? -4.470  -50.090 -43.818 1.00 126.95 ? 46  THR A C   1 
ATOM   337  O O   . THR A 1 46  ? -5.609  -50.025 -44.266 1.00 144.24 ? 46  THR A O   1 
ATOM   338  C CB  . THR A 1 46  ? -3.336  -47.819 -43.574 1.00 129.92 ? 46  THR A CB  1 
ATOM   339  O OG1 . THR A 1 46  ? -2.242  -47.112 -44.151 1.00 144.71 ? 46  THR A OG1 1 
ATOM   340  C CG2 . THR A 1 46  ? -3.186  -47.936 -42.061 1.00 116.74 ? 46  THR A CG2 1 
ATOM   341  N N   . ARG A 1 47  ? -4.135  -50.930 -42.849 1.00 131.62 ? 47  ARG A N   1 
ATOM   342  C CA  . ARG A 1 47  ? -5.067  -51.749 -42.081 1.00 136.75 ? 47  ARG A CA  1 
ATOM   343  C C   . ARG A 1 47  ? -4.797  -51.539 -40.594 1.00 135.10 ? 47  ARG A C   1 
ATOM   344  O O   . ARG A 1 47  ? -3.675  -51.669 -40.109 1.00 160.77 ? 47  ARG A O   1 
ATOM   345  C CB  . ARG A 1 47  ? -4.905  -53.157 -42.665 1.00 143.04 ? 47  ARG A CB  1 
ATOM   346  C CG  . ARG A 1 47  ? -5.496  -54.368 -41.964 1.00 159.30 ? 47  ARG A CG  1 
ATOM   347  C CD  . ARG A 1 47  ? -5.038  -55.590 -42.732 1.00 173.84 ? 47  ARG A CD  1 
ATOM   348  N NE  . ARG A 1 47  ? -5.524  -56.868 -42.193 1.00 215.55 ? 47  ARG A NE  1 
ATOM   349  C CZ  . ARG A 1 47  ? -4.838  -58.007 -42.102 1.00 238.74 ? 47  ARG A CZ  1 
ATOM   350  N NH1 . ARG A 1 47  ? -3.575  -58.056 -42.491 1.00 213.01 ? 47  ARG A NH1 1 
ATOM   351  N NH2 . ARG A 1 47  ? -5.431  -59.095 -41.635 1.00 260.44 ? 47  ARG A NH2 1 
ATOM   352  N N   . LEU A 1 48  ? -5.877  -51.258 -39.853 1.00 123.60 ? 48  LEU A N   1 
ATOM   353  C CA  . LEU A 1 48  ? -5.838  -50.878 -38.454 1.00 126.23 ? 48  LEU A CA  1 
ATOM   354  C C   . LEU A 1 48  ? -6.477  -51.958 -37.576 1.00 136.43 ? 48  LEU A C   1 
ATOM   355  O O   . LEU A 1 48  ? -7.533  -52.543 -37.888 1.00 147.24 ? 48  LEU A O   1 
ATOM   356  C CB  . LEU A 1 48  ? -6.455  -49.518 -38.124 1.00 131.42 ? 48  LEU A CB  1 
ATOM   357  C CG  . LEU A 1 48  ? -5.885  -48.308 -38.868 1.00 149.90 ? 48  LEU A CG  1 
ATOM   358  C CD1 . LEU A 1 48  ? -6.683  -47.065 -38.521 1.00 157.72 ? 48  LEU A CD1 1 
ATOM   359  C CD2 . LEU A 1 48  ? -4.431  -48.114 -38.489 1.00 171.46 ? 48  LEU A CD2 1 
ATOM   360  N N   . VAL A 1 49  ? -5.817  -52.169 -36.433 1.00 140.95 ? 49  VAL A N   1 
ATOM   361  C CA  . VAL A 1 49  ? -6.369  -52.968 -35.337 1.00 148.16 ? 49  VAL A CA  1 
ATOM   362  C C   . VAL A 1 49  ? -6.400  -52.171 -34.036 1.00 162.71 ? 49  VAL A C   1 
ATOM   363  O O   . VAL A 1 49  ? -5.384  -51.645 -33.623 1.00 172.39 ? 49  VAL A O   1 
ATOM   364  C CB  . VAL A 1 49  ? -5.592  -54.279 -35.185 1.00 134.19 ? 49  VAL A CB  1 
ATOM   365  C CG1 . VAL A 1 49  ? -5.993  -55.013 -33.909 1.00 126.60 ? 49  VAL A CG1 1 
ATOM   366  C CG2 . VAL A 1 49  ? -5.767  -55.144 -36.425 1.00 142.65 ? 49  VAL A CG2 1 
ATOM   367  N N   . VAL A 1 50  ? -7.608  -52.048 -33.478 1.00 160.50 ? 50  VAL A N   1 
ATOM   368  C CA  . VAL A 1 50  ? -7.848  -51.321 -32.248 1.00 150.55 ? 50  VAL A CA  1 
ATOM   369  C C   . VAL A 1 50  ? -8.102  -52.308 -31.108 1.00 134.77 ? 50  VAL A C   1 
ATOM   370  O O   . VAL A 1 50  ? -8.868  -53.268 -31.215 1.00 115.43 ? 50  VAL A O   1 
ATOM   371  C CB  . VAL A 1 50  ? -8.988  -50.296 -32.378 1.00 151.12 ? 50  VAL A CB  1 
ATOM   372  C CG1 . VAL A 1 50  ? -9.382  -49.697 -31.028 1.00 157.99 ? 50  VAL A CG1 1 
ATOM   373  C CG2 . VAL A 1 50  ? -8.643  -49.217 -33.399 1.00 138.18 ? 50  VAL A CG2 1 
ATOM   374  N N   . ILE A 1 51  ? -7.403  -52.032 -30.007 1.00 129.56 ? 51  ILE A N   1 
ATOM   375  C CA  . ILE A 1 51  ? -7.488  -52.801 -28.775 1.00 121.79 ? 51  ILE A CA  1 
ATOM   376  C C   . ILE A 1 51  ? -7.752  -51.854 -27.601 1.00 116.68 ? 51  ILE A C   1 
ATOM   377  O O   . ILE A 1 51  ? -7.075  -50.840 -27.410 1.00 133.84 ? 51  ILE A O   1 
ATOM   378  C CB  . ILE A 1 51  ? -6.191  -53.616 -28.612 1.00 123.99 ? 51  ILE A CB  1 
ATOM   379  C CG1 . ILE A 1 51  ? -5.851  -54.355 -29.913 1.00 112.16 ? 51  ILE A CG1 1 
ATOM   380  C CG2 . ILE A 1 51  ? -6.254  -54.553 -27.404 1.00 115.18 ? 51  ILE A CG2 1 
ATOM   381  C CD1 . ILE A 1 51  ? -4.464  -54.962 -29.936 1.00 132.33 ? 51  ILE A CD1 1 
ATOM   382  N N   . THR A 1 52  ? -8.788  -52.207 -26.831 1.00 104.92 ? 52  THR A N   1 
ATOM   383  C CA  . THR A 1 52  ? -9.234  -51.439 -25.689 1.00 117.14 ? 52  THR A CA  1 
ATOM   384  C C   . THR A 1 52  ? -9.568  -52.483 -24.637 1.00 127.16 ? 52  THR A C   1 
ATOM   385  O O   . THR A 1 52  ? -9.871  -53.639 -24.968 1.00 126.89 ? 52  THR A O   1 
ATOM   386  C CB  . THR A 1 52  ? -10.407 -50.528 -26.067 1.00 120.77 ? 52  THR A CB  1 
ATOM   387  O OG1 . THR A 1 52  ? -11.428 -51.321 -26.666 1.00 125.53 ? 52  THR A OG1 1 
ATOM   388  C CG2 . THR A 1 52  ? -10.062 -49.515 -27.141 1.00 121.16 ? 52  THR A CG2 1 
ATOM   389  N N   . SER A 1 53  ? -9.474  -52.062 -23.379 1.00 133.01 ? 53  SER A N   1 
ATOM   390  C CA  . SER A 1 53  ? -9.807  -52.893 -22.226 1.00 150.34 ? 53  SER A CA  1 
ATOM   391  C C   . SER A 1 53  ? -11.308 -53.219 -22.184 1.00 153.81 ? 53  SER A C   1 
ATOM   392  O O   . SER A 1 53  ? -11.729 -54.236 -21.619 1.00 171.02 ? 53  SER A O   1 
ATOM   393  C CB  . SER A 1 53  ? -9.334  -52.218 -20.954 1.00 162.45 ? 53  SER A CB  1 
ATOM   394  O OG  . SER A 1 53  ? -9.137  -53.160 -19.907 1.00 180.06 ? 53  SER A OG  1 
ATOM   395  N N   . GLU A 1 54  ? -12.105 -52.328 -22.794 1.00 151.16 ? 54  GLU A N   1 
ATOM   396  C CA  . GLU A 1 54  ? -13.552 -52.408 -22.919 1.00 133.59 ? 54  GLU A CA  1 
ATOM   397  C C   . GLU A 1 54  ? -13.943 -52.093 -24.364 1.00 127.37 ? 54  GLU A C   1 
ATOM   398  O O   . GLU A 1 54  ? -13.348 -51.214 -25.001 1.00 120.74 ? 54  GLU A O   1 
ATOM   399  C CB  . GLU A 1 54  ? -14.149 -51.331 -22.009 1.00 151.66 ? 54  GLU A CB  1 
ATOM   400  C CG  . GLU A 1 54  ? -14.230 -51.736 -20.540 1.00 150.91 ? 54  GLU A CG  1 
ATOM   401  C CD  . GLU A 1 54  ? -15.175 -52.906 -20.353 1.00 156.26 ? 54  GLU A CD  1 
ATOM   402  O OE1 . GLU A 1 54  ? -16.351 -52.809 -20.770 1.00 166.02 ? 54  GLU A OE1 1 
ATOM   403  O OE2 . GLU A 1 54  ? -14.719 -53.924 -19.804 1.00 162.90 ? 54  GLU A OE2 1 
ATOM   404  N N   . ALA A 1 55  ? -14.992 -52.761 -24.861 1.00 113.85 ? 55  ALA A N   1 
ATOM   405  C CA  . ALA A 1 55  ? -15.314 -52.760 -26.284 1.00 122.20 ? 55  ALA A CA  1 
ATOM   406  C C   . ALA A 1 55  ? -15.772 -51.389 -26.802 1.00 133.85 ? 55  ALA A C   1 
ATOM   407  O O   . ALA A 1 55  ? -16.726 -50.825 -26.280 1.00 176.95 ? 55  ALA A O   1 
ATOM   408  C CB  . ALA A 1 55  ? -16.388 -53.795 -26.507 1.00 120.24 ? 55  ALA A CB  1 
ATOM   409  N N   . VAL A 1 56  ? -15.144 -50.875 -27.870 1.00 121.78 ? 56  VAL A N   1 
ATOM   410  C CA  . VAL A 1 56  ? -15.592 -49.648 -28.528 1.00 114.65 ? 56  VAL A CA  1 
ATOM   411  C C   . VAL A 1 56  ? -17.036 -49.805 -29.008 1.00 136.49 ? 56  VAL A C   1 
ATOM   412  O O   . VAL A 1 56  ? -17.364 -50.811 -29.645 1.00 137.33 ? 56  VAL A O   1 
ATOM   413  C CB  . VAL A 1 56  ? -14.678 -49.367 -29.733 1.00 111.94 ? 56  VAL A CB  1 
ATOM   414  C CG1 . VAL A 1 56  ? -15.246 -48.316 -30.685 1.00 96.19  ? 56  VAL A CG1 1 
ATOM   415  C CG2 . VAL A 1 56  ? -13.256 -49.040 -29.309 1.00 122.65 ? 56  VAL A CG2 1 
ATOM   416  N N   . ASP A 1 57  ? -17.877 -48.788 -28.728 1.00 148.95 ? 57  ASP A N   1 
ATOM   417  C CA  . ASP A 1 57  ? -19.314 -48.820 -29.000 1.00 135.60 ? 57  ASP A CA  1 
ATOM   418  C C   . ASP A 1 57  ? -19.642 -48.448 -30.451 1.00 122.88 ? 57  ASP A C   1 
ATOM   419  O O   . ASP A 1 57  ? -19.158 -47.441 -30.969 1.00 104.60 ? 57  ASP A O   1 
ATOM   420  C CB  . ASP A 1 57  ? -20.086 -47.920 -28.049 1.00 127.03 ? 57  ASP A CB  1 
ATOM   421  C CG  . ASP A 1 57  ? -21.578 -47.823 -28.330 1.00 136.25 ? 57  ASP A CG  1 
ATOM   422  O OD1 . ASP A 1 57  ? -21.964 -47.533 -29.487 1.00 117.90 ? 57  ASP A OD1 1 
ATOM   423  O OD2 . ASP A 1 57  ? -22.345 -48.032 -27.382 1.00 171.78 ? 57  ASP A OD2 1 
ATOM   424  N N   . PRO A 1 58  ? -20.536 -49.202 -31.137 1.00 119.34 ? 58  PRO A N   1 
ATOM   425  C CA  . PRO A 1 58  ? -20.770 -49.006 -32.569 1.00 107.82 ? 58  PRO A CA  1 
ATOM   426  C C   . PRO A 1 58  ? -21.071 -47.545 -32.860 1.00 98.67  ? 58  PRO A C   1 
ATOM   427  O O   . PRO A 1 58  ? -20.626 -47.051 -33.886 1.00 82.65  ? 58  PRO A O   1 
ATOM   428  C CB  . PRO A 1 58  ? -21.943 -49.929 -32.902 1.00 102.34 ? 58  PRO A CB  1 
ATOM   429  C CG  . PRO A 1 58  ? -22.597 -50.152 -31.552 1.00 113.65 ? 58  PRO A CG  1 
ATOM   430  C CD  . PRO A 1 58  ? -21.438 -50.214 -30.561 1.00 124.40 ? 58  PRO A CD  1 
ATOM   431  N N   . ALA A 1 59  ? -21.844 -46.912 -31.976 1.00 101.68 ? 59  ALA A N   1 
ATOM   432  C CA  . ALA A 1 59  ? -22.274 -45.535 -32.135 1.00 108.14 ? 59  ALA A CA  1 
ATOM   433  C C   . ALA A 1 59  ? -21.072 -44.607 -32.292 1.00 103.52 ? 59  ALA A C   1 
ATOM   434  O O   . ALA A 1 59  ? -21.009 -43.752 -33.187 1.00 98.66  ? 59  ALA A O   1 
ATOM   435  C CB  . ALA A 1 59  ? -23.053 -45.122 -30.897 1.00 117.23 ? 59  ALA A CB  1 
ATOM   436  N N   . THR A 1 60  ? -20.130 -44.810 -31.372 1.00 99.82  ? 60  THR A N   1 
ATOM   437  C CA  . THR A 1 60  ? -18.883 -44.052 -31.298 1.00 95.30  ? 60  THR A CA  1 
ATOM   438  C C   . THR A 1 60  ? -18.138 -44.158 -32.631 1.00 89.51  ? 60  THR A C   1 
ATOM   439  O O   . THR A 1 60  ? -17.667 -43.157 -33.204 1.00 81.83  ? 60  THR A O   1 
ATOM   440  C CB  . THR A 1 60  ? -18.039 -44.743 -30.226 1.00 98.95  ? 60  THR A CB  1 
ATOM   441  O OG1 . THR A 1 60  ? -18.835 -44.953 -29.070 1.00 112.11 ? 60  THR A OG1 1 
ATOM   442  C CG2 . THR A 1 60  ? -16.761 -44.009 -29.863 1.00 114.87 ? 60  THR A CG2 1 
ATOM   443  N N   . LEU A 1 61  ? -18.035 -45.413 -33.080 1.00 89.09  ? 61  LEU A N   1 
ATOM   444  C CA  . LEU A 1 61  ? -17.337 -45.747 -34.317 1.00 99.50  ? 61  LEU A CA  1 
ATOM   445  C C   . LEU A 1 61  ? -17.970 -45.006 -35.494 1.00 91.38  ? 61  LEU A C   1 
ATOM   446  O O   . LEU A 1 61  ? -17.265 -44.419 -36.327 1.00 75.98  ? 61  LEU A O   1 
ATOM   447  C CB  . LEU A 1 61  ? -17.257 -47.263 -34.486 1.00 101.20 ? 61  LEU A CB  1 
ATOM   448  C CG  . LEU A 1 61  ? -16.634 -47.798 -35.778 1.00 103.12 ? 61  LEU A CG  1 
ATOM   449  C CD1 . LEU A 1 61  ? -15.326 -47.180 -36.200 1.00 101.41 ? 61  LEU A CD1 1 
ATOM   450  C CD2 . LEU A 1 61  ? -16.396 -49.243 -35.432 1.00 119.80 ? 61  LEU A CD2 1 
ATOM   451  N N   . ASP A 1 62  ? -19.298 -45.047 -35.525 1.00 92.14  ? 62  ASP A N   1 
ATOM   452  C CA  . ASP A 1 62  ? -20.094 -44.404 -36.563 1.00 106.48 ? 62  ASP A CA  1 
ATOM   453  C C   . ASP A 1 62  ? -19.791 -42.910 -36.605 1.00 101.61 ? 62  ASP A C   1 
ATOM   454  O O   . ASP A 1 62  ? -19.570 -42.333 -37.678 1.00 95.69  ? 62  ASP A O   1 
ATOM   455  C CB  . ASP A 1 62  ? -21.573 -44.668 -36.330 1.00 128.79 ? 62  ASP A CB  1 
ATOM   456  C CG  . ASP A 1 62  ? -22.501 -44.232 -37.457 1.00 156.83 ? 62  ASP A CG  1 
ATOM   457  O OD1 . ASP A 1 62  ? -21.984 -43.987 -38.568 1.00 155.20 ? 62  ASP A OD1 1 
ATOM   458  O OD2 . ASP A 1 62  ? -23.731 -44.128 -37.220 1.00 169.84 ? 62  ASP A OD2 1 
ATOM   459  N N   . TYR A 1 63  ? -19.785 -42.317 -35.409 1.00 98.17  ? 63  TYR A N   1 
ATOM   460  C CA  . TYR A 1 63  ? -19.522 -40.893 -35.221 1.00 97.94  ? 63  TYR A CA  1 
ATOM   461  C C   . TYR A 1 63  ? -18.159 -40.536 -35.816 1.00 102.65 ? 63  TYR A C   1 
ATOM   462  O O   . TYR A 1 63  ? -18.014 -39.548 -36.573 1.00 104.84 ? 63  TYR A O   1 
ATOM   463  C CB  . TYR A 1 63  ? -19.457 -40.506 -33.729 1.00 97.40  ? 63  TYR A CB  1 
ATOM   464  C CG  . TYR A 1 63  ? -18.935 -39.112 -33.376 1.00 104.29 ? 63  TYR A CG  1 
ATOM   465  C CD1 . TYR A 1 63  ? -19.172 -38.007 -34.208 1.00 110.14 ? 63  TYR A CD1 1 
ATOM   466  C CD2 . TYR A 1 63  ? -18.191 -38.889 -32.216 1.00 103.03 ? 63  TYR A CD2 1 
ATOM   467  C CE1 . TYR A 1 63  ? -18.669 -36.741 -33.913 1.00 118.38 ? 63  TYR A CE1 1 
ATOM   468  C CE2 . TYR A 1 63  ? -17.709 -37.617 -31.901 1.00 119.44 ? 63  TYR A CE2 1 
ATOM   469  C CZ  . TYR A 1 63  ? -17.940 -36.536 -32.749 1.00 117.24 ? 63  TYR A CZ  1 
ATOM   470  O OH  . TYR A 1 63  ? -17.471 -35.271 -32.476 1.00 91.13  ? 63  TYR A OH  1 
ATOM   471  N N   . HIS A 1 64  ? -17.177 -41.374 -35.450 1.00 100.11 ? 64  HIS A N   1 
ATOM   472  C CA  . HIS A 1 64  ? -15.797 -41.179 -35.874 1.00 97.47  ? 64  HIS A CA  1 
ATOM   473  C C   . HIS A 1 64  ? -15.720 -41.206 -37.407 1.00 101.60 ? 64  HIS A C   1 
ATOM   474  O O   . HIS A 1 64  ? -15.069 -40.351 -38.036 1.00 102.79 ? 64  HIS A O   1 
ATOM   475  C CB  . HIS A 1 64  ? -14.844 -42.106 -35.115 1.00 96.15  ? 64  HIS A CB  1 
ATOM   476  C CG  . HIS A 1 64  ? -14.529 -41.763 -33.693 1.00 103.96 ? 64  HIS A CG  1 
ATOM   477  N ND1 . HIS A 1 64  ? -15.159 -42.355 -32.613 1.00 107.92 ? 64  HIS A ND1 1 
ATOM   478  C CD2 . HIS A 1 64  ? -13.575 -40.969 -33.170 1.00 101.48 ? 64  HIS A CD2 1 
ATOM   479  C CE1 . HIS A 1 64  ? -14.628 -41.903 -31.471 1.00 105.73 ? 64  HIS A CE1 1 
ATOM   480  N NE2 . HIS A 1 64  ? -13.662 -41.062 -31.784 1.00 102.17 ? 64  HIS A NE2 1 
ATOM   481  N N   . LEU A 1 65  ? -16.412 -42.193 -37.981 1.00 101.58 ? 65  LEU A N   1 
ATOM   482  C CA  . LEU A 1 65  ? -16.390 -42.438 -39.406 1.00 104.22 ? 65  LEU A CA  1 
ATOM   483  C C   . LEU A 1 65  ? -16.988 -41.232 -40.116 1.00 112.98 ? 65  LEU A C   1 
ATOM   484  O O   . LEU A 1 65  ? -16.406 -40.821 -41.136 1.00 108.87 ? 65  LEU A O   1 
ATOM   485  C CB  . LEU A 1 65  ? -17.023 -43.785 -39.691 1.00 103.13 ? 65  LEU A CB  1 
ATOM   486  C CG  . LEU A 1 65  ? -16.165 -44.932 -39.147 1.00 113.13 ? 65  LEU A CG  1 
ATOM   487  C CD1 . LEU A 1 65  ? -16.792 -46.304 -39.331 1.00 134.31 ? 65  LEU A CD1 1 
ATOM   488  C CD2 . LEU A 1 65  ? -14.730 -44.890 -39.689 1.00 111.27 ? 65  LEU A CD2 1 
ATOM   489  N N   . ARG A 1 66  ? -18.089 -40.670 -39.561 1.00 118.75 ? 66  ARG A N   1 
ATOM   490  C CA  . ARG A 1 66  ? -18.889 -39.803 -40.427 1.00 131.06 ? 66  ARG A CA  1 
ATOM   491  C C   . ARG A 1 66  ? -18.733 -38.342 -40.017 1.00 140.60 ? 66  ARG A C   1 
ATOM   492  O O   . ARG A 1 66  ? -18.522 -37.452 -40.841 1.00 139.54 ? 66  ARG A O   1 
ATOM   493  C CB  . ARG A 1 66  ? -20.331 -40.312 -40.541 1.00 130.20 ? 66  ARG A CB  1 
ATOM   494  C CG  . ARG A 1 66  ? -20.504 -41.753 -40.997 1.00 123.93 ? 66  ARG A CG  1 
ATOM   495  C CD  . ARG A 1 66  ? -21.946 -42.045 -41.383 1.00 127.48 ? 66  ARG A CD  1 
ATOM   496  N NE  . ARG A 1 66  ? -22.257 -43.462 -41.155 1.00 119.04 ? 66  ARG A NE  1 
ATOM   497  C CZ  . ARG A 1 66  ? -22.408 -44.405 -42.081 1.00 117.69 ? 66  ARG A CZ  1 
ATOM   498  N NH1 . ARG A 1 66  ? -22.191 -44.145 -43.359 1.00 117.57 ? 66  ARG A NH1 1 
ATOM   499  N NH2 . ARG A 1 66  ? -22.755 -45.622 -41.716 1.00 118.83 ? 66  ARG A NH2 1 
ATOM   500  N N   . ASP A 1 67  ? -18.825 -38.129 -38.707 1.00 137.61 ? 67  ASP A N   1 
ATOM   501  C CA  . ASP A 1 67  ? -18.988 -36.800 -38.163 1.00 134.01 ? 67  ASP A CA  1 
ATOM   502  C C   . ASP A 1 67  ? -17.615 -36.302 -37.715 1.00 134.68 ? 67  ASP A C   1 
ATOM   503  O O   . ASP A 1 67  ? -17.420 -35.110 -37.476 1.00 130.56 ? 67  ASP A O   1 
ATOM   504  C CB  . ASP A 1 67  ? -20.151 -36.807 -37.181 1.00 137.12 ? 67  ASP A CB  1 
ATOM   505  C CG  . ASP A 1 67  ? -21.436 -37.453 -37.700 1.00 146.57 ? 67  ASP A CG  1 
ATOM   506  O OD1 . ASP A 1 67  ? -22.044 -36.939 -38.662 1.00 135.85 ? 67  ASP A OD1 1 
ATOM   507  O OD2 . ASP A 1 67  ? -21.819 -38.503 -37.168 1.00 173.17 ? 67  ASP A OD2 1 
ATOM   508  N N   . VAL A 1 68  ? -16.657 -37.230 -37.629 1.00 131.97 ? 68  VAL A N   1 
ATOM   509  C CA  . VAL A 1 68  ? -15.293 -36.852 -37.295 1.00 122.26 ? 68  VAL A CA  1 
ATOM   510  C C   . VAL A 1 68  ? -14.481 -36.782 -38.583 1.00 117.51 ? 68  VAL A C   1 
ATOM   511  O O   . VAL A 1 68  ? -14.165 -35.699 -39.051 1.00 121.02 ? 68  VAL A O   1 
ATOM   512  C CB  . VAL A 1 68  ? -14.584 -37.691 -36.214 1.00 113.96 ? 68  VAL A CB  1 
ATOM   513  C CG1 . VAL A 1 68  ? -13.132 -37.247 -36.052 1.00 108.18 ? 68  VAL A CG1 1 
ATOM   514  C CG2 . VAL A 1 68  ? -15.327 -37.648 -34.879 1.00 108.68 ? 68  VAL A CG2 1 
ATOM   515  N N   . PHE A 1 69  ? -14.198 -37.940 -39.177 1.00 120.82 ? 69  PHE A N   1 
ATOM   516  C CA  . PHE A 1 69  ? -13.228 -38.016 -40.255 1.00 122.63 ? 69  PHE A CA  1 
ATOM   517  C C   . PHE A 1 69  ? -13.873 -37.723 -41.607 1.00 127.35 ? 69  PHE A C   1 
ATOM   518  O O   . PHE A 1 69  ? -13.148 -37.576 -42.587 1.00 119.91 ? 69  PHE A O   1 
ATOM   519  C CB  . PHE A 1 69  ? -12.541 -39.383 -40.284 1.00 122.96 ? 69  PHE A CB  1 
ATOM   520  C CG  . PHE A 1 69  ? -11.667 -39.640 -39.068 1.00 120.69 ? 69  PHE A CG  1 
ATOM   521  C CD1 . PHE A 1 69  ? -10.362 -39.172 -39.042 1.00 130.30 ? 69  PHE A CD1 1 
ATOM   522  C CD2 . PHE A 1 69  ? -12.136 -40.369 -37.972 1.00 115.45 ? 69  PHE A CD2 1 
ATOM   523  C CE1 . PHE A 1 69  ? -9.550  -39.407 -37.937 1.00 135.91 ? 69  PHE A CE1 1 
ATOM   524  C CE2 . PHE A 1 69  ? -11.334 -40.611 -36.865 1.00 109.90 ? 69  PHE A CE2 1 
ATOM   525  C CZ  . PHE A 1 69  ? -10.034 -40.138 -36.861 1.00 127.16 ? 69  PHE A CZ  1 
ATOM   526  N N   . ARG A 1 70  ? -15.214 -37.670 -41.650 1.00 143.76 ? 70  ARG A N   1 
ATOM   527  C CA  . ARG A 1 70  ? -15.985 -37.291 -42.831 1.00 175.37 ? 70  ARG A CA  1 
ATOM   528  C C   . ARG A 1 70  ? -15.660 -38.187 -44.038 1.00 161.50 ? 70  ARG A C   1 
ATOM   529  O O   . ARG A 1 70  ? -15.357 -37.725 -45.144 1.00 157.61 ? 70  ARG A O   1 
ATOM   530  C CB  . ARG A 1 70  ? -15.938 -35.783 -43.117 1.00 197.13 ? 70  ARG A CB  1 
ATOM   531  C CG  . ARG A 1 70  ? -14.641 -35.256 -43.714 1.00 214.87 ? 70  ARG A CG  1 
ATOM   532  C CD  . ARG A 1 70  ? -14.713 -33.942 -44.465 1.00 221.11 ? 70  ARG A CD  1 
ATOM   533  N NE  . ARG A 1 70  ? -13.506 -33.928 -45.303 1.00 235.90 ? 70  ARG A NE  1 
ATOM   534  C CZ  . ARG A 1 70  ? -12.366 -33.311 -45.019 1.00 226.94 ? 70  ARG A CZ  1 
ATOM   535  N NH1 . ARG A 1 70  ? -12.300 -32.522 -43.962 1.00 208.80 ? 70  ARG A NH1 1 
ATOM   536  N NH2 . ARG A 1 70  ? -11.310 -33.492 -45.796 1.00 219.52 ? 70  ARG A NH2 1 
ATOM   537  N N   . PHE A 1 71  ? -15.764 -39.496 -43.835 1.00 150.26 ? 71  PHE A N   1 
ATOM   538  C CA  . PHE A 1 71  ? -15.565 -40.411 -44.944 1.00 164.62 ? 71  PHE A CA  1 
ATOM   539  C C   . PHE A 1 71  ? -16.717 -40.279 -45.931 1.00 201.44 ? 71  PHE A C   1 
ATOM   540  O O   . PHE A 1 71  ? -17.874 -40.293 -45.514 1.00 253.37 ? 71  PHE A O   1 
ATOM   541  C CB  . PHE A 1 71  ? -15.517 -41.863 -44.466 1.00 146.84 ? 71  PHE A CB  1 
ATOM   542  C CG  . PHE A 1 71  ? -14.153 -42.184 -43.889 1.00 134.60 ? 71  PHE A CG  1 
ATOM   543  C CD1 . PHE A 1 71  ? -13.027 -42.163 -44.712 1.00 133.51 ? 71  PHE A CD1 1 
ATOM   544  C CD2 . PHE A 1 71  ? -14.003 -42.484 -42.536 1.00 123.70 ? 71  PHE A CD2 1 
ATOM   545  C CE1 . PHE A 1 71  ? -11.773 -42.425 -44.187 1.00 143.21 ? 71  PHE A CE1 1 
ATOM   546  C CE2 . PHE A 1 71  ? -12.751 -42.749 -42.016 1.00 129.85 ? 71  PHE A CE2 1 
ATOM   547  C CZ  . PHE A 1 71  ? -11.640 -42.716 -42.838 1.00 146.10 ? 71  PHE A CZ  1 
ATOM   548  N N   . ASP A 1 72  ? -16.391 -40.185 -47.229 1.00 212.38 ? 72  ASP A N   1 
ATOM   549  C CA  . ASP A 1 72  ? -17.410 -40.237 -48.270 1.00 214.27 ? 72  ASP A CA  1 
ATOM   550  C C   . ASP A 1 72  ? -18.080 -41.617 -48.265 1.00 185.78 ? 72  ASP A C   1 
ATOM   551  O O   . ASP A 1 72  ? -17.447 -42.617 -47.933 1.00 171.26 ? 72  ASP A O   1 
ATOM   552  C CB  . ASP A 1 72  ? -16.876 -39.756 -49.613 1.00 235.57 ? 72  ASP A CB  1 
ATOM   553  C CG  . ASP A 1 72  ? -15.728 -40.564 -50.202 1.00 258.21 ? 72  ASP A CG  1 
ATOM   554  O OD1 . ASP A 1 72  ? -15.956 -41.751 -50.524 1.00 242.34 ? 72  ASP A OD1 1 
ATOM   555  O OD2 . ASP A 1 72  ? -14.617 -40.000 -50.330 1.00 276.48 ? 72  ASP A OD2 1 
ATOM   556  N N   . GLU A 1 73  ? -19.370 -41.655 -48.627 1.00 163.55 ? 73  GLU A N   1 
ATOM   557  C CA  . GLU A 1 73  ? -20.205 -42.833 -48.452 1.00 149.47 ? 73  GLU A CA  1 
ATOM   558  C C   . GLU A 1 73  ? -19.725 -43.991 -49.319 1.00 142.66 ? 73  GLU A C   1 
ATOM   559  O O   . GLU A 1 73  ? -19.701 -45.126 -48.855 1.00 138.22 ? 73  GLU A O   1 
ATOM   560  C CB  . GLU A 1 73  ? -21.679 -42.514 -48.685 1.00 154.44 ? 73  GLU A CB  1 
ATOM   561  C CG  . GLU A 1 73  ? -22.354 -41.918 -47.451 1.00 170.73 ? 73  GLU A CG  1 
ATOM   562  C CD  . GLU A 1 73  ? -22.075 -42.641 -46.139 1.00 176.15 ? 73  GLU A CD  1 
ATOM   563  O OE1 . GLU A 1 73  ? -22.185 -43.891 -46.111 1.00 175.21 ? 73  GLU A OE1 1 
ATOM   564  O OE2 . GLU A 1 73  ? -21.772 -41.955 -45.132 1.00 162.48 ? 73  GLU A OE2 1 
ATOM   565  N N   . PRO A 1 74  ? -19.375 -43.758 -50.604 1.00 149.48 ? 74  PRO A N   1 
ATOM   566  C CA  . PRO A 1 74  ? -18.724 -44.789 -51.414 1.00 160.91 ? 74  PRO A CA  1 
ATOM   567  C C   . PRO A 1 74  ? -17.596 -45.568 -50.733 1.00 167.67 ? 74  PRO A C   1 
ATOM   568  O O   . PRO A 1 74  ? -17.693 -46.782 -50.584 1.00 186.48 ? 74  PRO A O   1 
ATOM   569  C CB  . PRO A 1 74  ? -18.259 -43.991 -52.646 1.00 165.56 ? 74  PRO A CB  1 
ATOM   570  C CG  . PRO A 1 74  ? -19.325 -42.916 -52.797 1.00 151.69 ? 74  PRO A CG  1 
ATOM   571  C CD  . PRO A 1 74  ? -19.631 -42.521 -51.364 1.00 146.62 ? 74  PRO A CD  1 
ATOM   572  N N   . ALA A 1 75  ? -16.545 -44.874 -50.282 1.00 156.04 ? 75  ALA A N   1 
ATOM   573  C CA  . ALA A 1 75  ? -15.337 -45.549 -49.828 1.00 162.73 ? 75  ALA A CA  1 
ATOM   574  C C   . ALA A 1 75  ? -15.522 -46.216 -48.458 1.00 163.38 ? 75  ALA A C   1 
ATOM   575  O O   . ALA A 1 75  ? -14.732 -47.082 -48.062 1.00 164.80 ? 75  ALA A O   1 
ATOM   576  C CB  . ALA A 1 75  ? -14.187 -44.569 -49.836 1.00 161.55 ? 75  ALA A CB  1 
ATOM   577  N N   . LEU A 1 76  ? -16.599 -45.834 -47.760 1.00 154.89 ? 76  LEU A N   1 
ATOM   578  C CA  . LEU A 1 76  ? -16.715 -46.060 -46.330 1.00 158.52 ? 76  LEU A CA  1 
ATOM   579  C C   . LEU A 1 76  ? -16.673 -47.549 -46.017 1.00 167.28 ? 76  LEU A C   1 
ATOM   580  O O   . LEU A 1 76  ? -16.053 -47.936 -45.020 1.00 167.03 ? 76  LEU A O   1 
ATOM   581  C CB  . LEU A 1 76  ? -17.916 -45.388 -45.666 1.00 149.52 ? 76  LEU A CB  1 
ATOM   582  C CG  . LEU A 1 76  ? -18.212 -45.871 -44.238 1.00 147.38 ? 76  LEU A CG  1 
ATOM   583  C CD1 . LEU A 1 76  ? -17.216 -45.366 -43.215 1.00 133.26 ? 76  LEU A CD1 1 
ATOM   584  C CD2 . LEU A 1 76  ? -19.630 -45.612 -43.782 1.00 169.33 ? 76  LEU A CD2 1 
ATOM   585  N N   . ALA A 1 77  ? -17.353 -48.344 -46.851 1.00 168.75 ? 77  ALA A N   1 
ATOM   586  C CA  . ALA A 1 77  ? -17.438 -49.782 -46.664 1.00 186.13 ? 77  ALA A CA  1 
ATOM   587  C C   . ALA A 1 77  ? -16.038 -50.402 -46.649 1.00 197.82 ? 77  ALA A C   1 
ATOM   588  O O   . ALA A 1 77  ? -15.709 -51.227 -45.777 1.00 211.77 ? 77  ALA A O   1 
ATOM   589  C CB  . ALA A 1 77  ? -18.309 -50.392 -47.738 1.00 197.69 ? 77  ALA A CB  1 
ATOM   590  N N   . ASP A 1 78  ? -15.240 -49.965 -47.632 1.00 187.50 ? 78  ASP A N   1 
ATOM   591  C CA  . ASP A 1 78  ? -13.870 -50.440 -47.793 1.00 184.45 ? 78  ASP A CA  1 
ATOM   592  C C   . ASP A 1 78  ? -13.061 -50.147 -46.527 1.00 148.71 ? 78  ASP A C   1 
ATOM   593  O O   . ASP A 1 78  ? -12.329 -51.007 -46.023 1.00 141.43 ? 78  ASP A O   1 
ATOM   594  C CB  . ASP A 1 78  ? -13.226 -49.850 -49.037 1.00 201.41 ? 78  ASP A CB  1 
ATOM   595  C CG  . ASP A 1 78  ? -11.732 -50.106 -49.150 1.00 217.23 ? 78  ASP A CG  1 
ATOM   596  O OD1 . ASP A 1 78  ? -11.350 -51.284 -49.291 1.00 220.39 ? 78  ASP A OD1 1 
ATOM   597  O OD2 . ASP A 1 78  ? -10.964 -49.128 -49.054 1.00 215.64 ? 78  ASP A OD2 1 
ATOM   598  N N   . VAL A 1 79  ? -13.219 -48.918 -46.046 1.00 124.49 ? 79  VAL A N   1 
ATOM   599  C CA  . VAL A 1 79  ? -12.531 -48.435 -44.856 1.00 126.16 ? 79  VAL A CA  1 
ATOM   600  C C   . VAL A 1 79  ? -12.881 -49.322 -43.657 1.00 123.05 ? 79  VAL A C   1 
ATOM   601  O O   . VAL A 1 79  ? -11.999 -49.737 -42.889 1.00 130.78 ? 79  VAL A O   1 
ATOM   602  C CB  . VAL A 1 79  ? -12.923 -46.964 -44.655 1.00 137.23 ? 79  VAL A CB  1 
ATOM   603  C CG1 . VAL A 1 79  ? -12.330 -46.390 -43.371 1.00 139.80 ? 79  VAL A CG1 1 
ATOM   604  C CG2 . VAL A 1 79  ? -12.581 -46.104 -45.875 1.00 135.17 ? 79  VAL A CG2 1 
ATOM   605  N N   . ARG A 1 80  ? -14.181 -49.593 -43.533 1.00 122.04 ? 80  ARG A N   1 
ATOM   606  C CA  . ARG A 1 80  ? -14.695 -50.420 -42.442 1.00 128.21 ? 80  ARG A CA  1 
ATOM   607  C C   . ARG A 1 80  ? -14.073 -51.807 -42.487 1.00 125.08 ? 80  ARG A C   1 
ATOM   608  O O   . ARG A 1 80  ? -13.664 -52.335 -41.451 1.00 113.45 ? 80  ARG A O   1 
ATOM   609  C CB  . ARG A 1 80  ? -16.160 -50.530 -42.010 1.00 128.36 ? 80  ARG A CB  1 
ATOM   610  C CG  . ARG A 1 80  ? -16.321 -51.560 -40.887 1.00 111.93 ? 80  ARG A CG  1 
ATOM   611  C CD  . ARG A 1 80  ? -15.666 -51.350 -39.505 1.00 113.76 ? 80  ARG A CD  1 
ATOM   612  N NE  . ARG A 1 80  ? -16.070 -52.177 -38.348 1.00 136.51 ? 80  ARG A NE  1 
ATOM   613  C CZ  . ARG A 1 80  ? -17.132 -52.126 -37.485 1.00 167.95 ? 80  ARG A CZ  1 
ATOM   614  N NH1 . ARG A 1 80  ? -18.164 -51.296 -37.613 1.00 168.86 ? 80  ARG A NH1 1 
ATOM   615  N NH2 . ARG A 1 80  ? -17.174 -52.954 -36.452 1.00 164.89 ? 80  ARG A NH2 1 
ATOM   616  N N   . ARG A 1 81  ? -14.014 -52.359 -43.699 1.00 136.05 ? 81  ARG A N   1 
ATOM   617  C CA  . ARG A 1 81  ? -13.413 -53.667 -43.948 1.00 146.97 ? 81  ARG A CA  1 
ATOM   618  C C   . ARG A 1 81  ? -11.974 -53.723 -43.409 1.00 145.19 ? 81  ARG A C   1 
ATOM   619  O O   . ARG A 1 81  ? -11.622 -54.711 -42.769 1.00 143.72 ? 81  ARG A O   1 
ATOM   620  C CB  . ARG A 1 81  ? -13.550 -53.994 -45.443 1.00 162.36 ? 81  ARG A CB  1 
ATOM   621  C CG  . ARG A 1 81  ? -12.639 -55.039 -46.072 1.00 178.29 ? 81  ARG A CG  1 
ATOM   622  C CD  . ARG A 1 81  ? -12.742 -54.969 -47.605 1.00 187.40 ? 81  ARG A CD  1 
ATOM   623  N NE  . ARG A 1 81  ? -13.760 -55.821 -48.233 1.00 192.37 ? 81  ARG A NE  1 
ATOM   624  C CZ  . ARG A 1 81  ? -13.606 -57.119 -48.520 1.00 204.14 ? 81  ARG A CZ  1 
ATOM   625  N NH1 . ARG A 1 81  ? -12.471 -57.736 -48.235 1.00 204.11 ? 81  ARG A NH1 1 
ATOM   626  N NH2 . ARG A 1 81  ? -14.588 -57.801 -49.085 1.00 198.24 ? 81  ARG A NH2 1 
ATOM   627  N N   . ARG A 1 82  ? -11.214 -52.621 -43.490 1.00 150.01 ? 82  ARG A N   1 
ATOM   628  C CA  . ARG A 1 82  ? -9.813  -52.605 -43.072 1.00 139.10 ? 82  ARG A CA  1 
ATOM   629  C C   . ARG A 1 82  ? -9.620  -52.202 -41.610 1.00 130.26 ? 82  ARG A C   1 
ATOM   630  O O   . ARG A 1 82  ? -8.545  -51.703 -41.261 1.00 121.19 ? 82  ARG A O   1 
ATOM   631  C CB  . ARG A 1 82  ? -8.991  -51.718 -44.020 1.00 123.14 ? 82  ARG A CB  1 
ATOM   632  C CG  . ARG A 1 82  ? -8.868  -52.325 -45.407 1.00 122.94 ? 82  ARG A CG  1 
ATOM   633  C CD  . ARG A 1 82  ? -8.116  -51.405 -46.331 1.00 127.98 ? 82  ARG A CD  1 
ATOM   634  N NE  . ARG A 1 82  ? -8.952  -50.279 -46.754 1.00 126.93 ? 82  ARG A NE  1 
ATOM   635  C CZ  . ARG A 1 82  ? -8.674  -49.016 -46.500 1.00 134.45 ? 82  ARG A CZ  1 
ATOM   636  N NH1 . ARG A 1 82  ? -7.605  -48.697 -45.802 1.00 128.45 ? 82  ARG A NH1 1 
ATOM   637  N NH2 . ARG A 1 82  ? -9.449  -48.061 -46.972 1.00 155.63 ? 82  ARG A NH2 1 
ATOM   638  N N   . LEU A 1 83  ? -10.644 -52.441 -40.792 1.00 125.84 ? 83  LEU A N   1 
ATOM   639  C CA  . LEU A 1 83  ? -10.632 -52.074 -39.390 1.00 126.08 ? 83  LEU A CA  1 
ATOM   640  C C   . LEU A 1 83  ? -11.136 -53.239 -38.549 1.00 132.32 ? 83  LEU A C   1 
ATOM   641  O O   . LEU A 1 83  ? -12.190 -53.821 -38.823 1.00 147.28 ? 83  LEU A O   1 
ATOM   642  C CB  . LEU A 1 83  ? -11.415 -50.784 -39.133 1.00 131.22 ? 83  LEU A CB  1 
ATOM   643  C CG  . LEU A 1 83  ? -11.516 -50.359 -37.663 1.00 127.66 ? 83  LEU A CG  1 
ATOM   644  C CD1 . LEU A 1 83  ? -10.135 -50.037 -37.108 1.00 151.58 ? 83  LEU A CD1 1 
ATOM   645  C CD2 . LEU A 1 83  ? -12.438 -49.182 -37.491 1.00 111.20 ? 83  LEU A CD2 1 
ATOM   646  N N   . THR A 1 84  ? -10.377 -53.538 -37.492 1.00 127.22 ? 84  THR A N   1 
ATOM   647  C CA  . THR A 1 84  ? -10.715 -54.570 -36.523 1.00 132.04 ? 84  THR A CA  1 
ATOM   648  C C   . THR A 1 84  ? -10.593 -54.034 -35.105 1.00 126.36 ? 84  THR A C   1 
ATOM   649  O O   . THR A 1 84  ? -9.609  -53.369 -34.737 1.00 114.26 ? 84  THR A O   1 
ATOM   650  C CB  . THR A 1 84  ? -9.867  -55.826 -36.697 1.00 134.83 ? 84  THR A CB  1 
ATOM   651  O OG1 . THR A 1 84  ? -9.848  -56.040 -38.102 1.00 151.91 ? 84  THR A OG1 1 
ATOM   652  C CG2 . THR A 1 84  ? -10.486 -57.024 -36.005 1.00 128.82 ? 84  THR A CG2 1 
ATOM   653  N N   . LEU A 1 85  ? -11.569 -54.447 -34.281 1.00 121.56 ? 85  LEU A N   1 
ATOM   654  C CA  . LEU A 1 85  ? -11.678 -54.024 -32.888 1.00 131.72 ? 85  LEU A CA  1 
ATOM   655  C C   . LEU A 1 85  ? -11.708 -55.235 -31.951 1.00 128.07 ? 85  LEU A C   1 
ATOM   656  O O   . LEU A 1 85  ? -12.535 -56.104 -32.127 1.00 143.91 ? 85  LEU A O   1 
ATOM   657  C CB  . LEU A 1 85  ? -12.927 -53.172 -32.632 1.00 136.82 ? 85  LEU A CB  1 
ATOM   658  C CG  . LEU A 1 85  ? -13.258 -52.003 -33.574 1.00 139.63 ? 85  LEU A CG  1 
ATOM   659  C CD1 . LEU A 1 85  ? -14.472 -51.303 -32.979 1.00 132.16 ? 85  LEU A CD1 1 
ATOM   660  C CD2 . LEU A 1 85  ? -12.157 -50.982 -33.878 1.00 126.10 ? 85  LEU A CD2 1 
ATOM   661  N N   . LEU A 1 86  ? -10.780 -55.259 -30.991 1.00 124.14 ? 86  LEU A N   1 
ATOM   662  C CA  . LEU A 1 86  ? -10.487 -56.430 -30.192 1.00 115.90 ? 86  LEU A CA  1 
ATOM   663  C C   . LEU A 1 86  ? -10.288 -56.047 -28.731 1.00 123.31 ? 86  LEU A C   1 
ATOM   664  O O   . LEU A 1 86  ? -9.705  -54.995 -28.380 1.00 116.08 ? 86  LEU A O   1 
ATOM   665  C CB  . LEU A 1 86  ? -9.239  -57.074 -30.775 1.00 112.53 ? 86  LEU A CB  1 
ATOM   666  C CG  . LEU A 1 86  ? -9.292  -57.332 -32.281 1.00 119.55 ? 86  LEU A CG  1 
ATOM   667  C CD1 . LEU A 1 86  ? -7.891  -57.472 -32.827 1.00 142.55 ? 86  LEU A CD1 1 
ATOM   668  C CD2 . LEU A 1 86  ? -10.108 -58.580 -32.565 1.00 138.54 ? 86  LEU A CD2 1 
ATOM   669  N N   . THR A 1 87  ? -10.728 -56.967 -27.865 1.00 125.87 ? 87  THR A N   1 
ATOM   670  C CA  . THR A 1 87  ? -10.638 -56.823 -26.416 1.00 141.52 ? 87  THR A CA  1 
ATOM   671  C C   . THR A 1 87  ? -9.962  -58.036 -25.792 1.00 138.23 ? 87  THR A C   1 
ATOM   672  O O   . THR A 1 87  ? -10.367 -59.159 -26.036 1.00 158.41 ? 87  THR A O   1 
ATOM   673  C CB  . THR A 1 87  ? -12.026 -56.549 -25.836 1.00 148.72 ? 87  THR A CB  1 
ATOM   674  O OG1 . THR A 1 87  ? -12.237 -55.216 -26.290 1.00 198.84 ? 87  THR A OG1 1 
ATOM   675  C CG2 . THR A 1 87  ? -12.031 -56.493 -24.321 1.00 153.40 ? 87  THR A CG2 1 
ATOM   676  N N   . PRO A 1 88  ? -8.869  -57.800 -25.038 1.00 127.47 ? 88  PRO A N   1 
ATOM   677  C CA  . PRO A 1 88  ? -8.305  -58.781 -24.123 1.00 120.72 ? 88  PRO A CA  1 
ATOM   678  C C   . PRO A 1 88  ? -9.361  -59.492 -23.289 1.00 133.01 ? 88  PRO A C   1 
ATOM   679  O O   . PRO A 1 88  ? -10.333 -58.889 -22.821 1.00 149.45 ? 88  PRO A O   1 
ATOM   680  C CB  . PRO A 1 88  ? -7.397  -57.969 -23.219 1.00 113.30 ? 88  PRO A CB  1 
ATOM   681  C CG  . PRO A 1 88  ? -6.950  -56.848 -24.108 1.00 133.03 ? 88  PRO A CG  1 
ATOM   682  C CD  . PRO A 1 88  ? -8.126  -56.532 -25.011 1.00 129.90 ? 88  PRO A CD  1 
ATOM   683  N N   . ALA A 1 89  ? -9.111  -60.783 -23.078 1.00 128.87 ? 89  ALA A N   1 
ATOM   684  C CA  . ALA A 1 89  ? -9.970  -61.653 -22.288 1.00 137.32 ? 89  ALA A CA  1 
ATOM   685  C C   . ALA A 1 89  ? -9.965  -61.234 -20.820 1.00 151.50 ? 89  ALA A C   1 
ATOM   686  O O   . ALA A 1 89  ? -10.901 -61.566 -20.092 1.00 170.89 ? 89  ALA A O   1 
ATOM   687  C CB  . ALA A 1 89  ? -9.547  -63.086 -22.461 1.00 150.99 ? 89  ALA A CB  1 
ATOM   688  N N   . SER A 1 90  ? -8.922  -60.505 -20.394 1.00 158.62 ? 90  SER A N   1 
ATOM   689  C CA  . SER A 1 90  ? -8.867  -59.995 -19.032 1.00 161.64 ? 90  SER A CA  1 
ATOM   690  C C   . SER A 1 90  ? -9.678  -58.709 -18.914 1.00 160.25 ? 90  SER A C   1 
ATOM   691  O O   . SER A 1 90  ? -9.579  -57.814 -19.755 1.00 157.47 ? 90  SER A O   1 
ATOM   692  C CB  . SER A 1 90  ? -7.458  -59.808 -18.547 1.00 174.63 ? 90  SER A CB  1 
ATOM   693  O OG  . SER A 1 90  ? -7.455  -59.242 -17.241 1.00 198.18 ? 90  SER A OG  1 
ATOM   694  N N   . ARG A 1 91  ? -10.493 -58.647 -17.859 1.00 157.47 ? 91  ARG A N   1 
ATOM   695  C CA  . ARG A 1 91  ? -11.277 -57.459 -17.593 1.00 173.10 ? 91  ARG A CA  1 
ATOM   696  C C   . ARG A 1 91  ? -10.843 -56.889 -16.243 1.00 173.87 ? 91  ARG A C   1 
ATOM   697  O O   . ARG A 1 91  ? -11.474 -55.972 -15.722 1.00 170.22 ? 91  ARG A O   1 
ATOM   698  C CB  . ARG A 1 91  ? -12.763 -57.800 -17.760 1.00 182.49 ? 91  ARG A CB  1 
ATOM   699  C CG  . ARG A 1 91  ? -13.665 -56.635 -18.143 1.00 186.28 ? 91  ARG A CG  1 
ATOM   700  C CD  . ARG A 1 91  ? -15.103 -57.078 -18.349 1.00 209.71 ? 91  ARG A CD  1 
ATOM   701  N NE  . ARG A 1 91  ? -16.023 -55.937 -18.438 1.00 230.71 ? 91  ARG A NE  1 
ATOM   702  C CZ  . ARG A 1 91  ? -17.054 -55.696 -17.634 1.00 236.96 ? 91  ARG A CZ  1 
ATOM   703  N NH1 . ARG A 1 91  ? -17.355 -56.535 -16.662 1.00 261.31 ? 91  ARG A NH1 1 
ATOM   704  N NH2 . ARG A 1 91  ? -17.800 -54.620 -17.808 1.00 226.39 ? 91  ARG A NH2 1 
ATOM   705  N N   . ALA A 1 92  ? -9.736  -57.419 -15.699 1.00 163.96 ? 92  ALA A N   1 
ATOM   706  C CA  . ALA A 1 92  ? -9.094  -56.824 -14.535 1.00 158.33 ? 92  ALA A CA  1 
ATOM   707  C C   . ALA A 1 92  ? -8.513  -55.470 -14.929 1.00 180.82 ? 92  ALA A C   1 
ATOM   708  O O   . ALA A 1 92  ? -8.075  -55.294 -16.067 1.00 180.65 ? 92  ALA A O   1 
ATOM   709  C CB  . ALA A 1 92  ? -8.021  -57.737 -13.996 1.00 138.13 ? 92  ALA A CB  1 
ATOM   710  N N   . ALA A 1 93  ? -8.516  -54.524 -13.977 1.00 199.82 ? 93  ALA A N   1 
ATOM   711  C CA  . ALA A 1 93  ? -8.072  -53.158 -14.229 1.00 189.52 ? 93  ALA A CA  1 
ATOM   712  C C   . ALA A 1 93  ? -6.552  -53.080 -14.121 1.00 164.57 ? 93  ALA A C   1 
ATOM   713  O O   . ALA A 1 93  ? -6.005  -52.779 -13.065 1.00 145.22 ? 93  ALA A O   1 
ATOM   714  C CB  . ALA A 1 93  ? -8.760  -52.177 -13.296 1.00 192.17 ? 93  ALA A CB  1 
ATOM   715  N N   . ARG A 1 94  ? -5.885  -53.385 -15.237 1.00 163.05 ? 94  ARG A N   1 
ATOM   716  C CA  . ARG A 1 94  ? -4.437  -53.351 -15.326 1.00 152.97 ? 94  ARG A CA  1 
ATOM   717  C C   . ARG A 1 94  ? -4.055  -52.700 -16.649 1.00 158.48 ? 94  ARG A C   1 
ATOM   718  O O   . ARG A 1 94  ? -4.904  -52.546 -17.528 1.00 189.83 ? 94  ARG A O   1 
ATOM   719  C CB  . ARG A 1 94  ? -3.918  -54.786 -15.301 1.00 156.03 ? 94  ARG A CB  1 
ATOM   720  C CG  . ARG A 1 94  ? -4.416  -55.602 -14.115 1.00 167.52 ? 94  ARG A CG  1 
ATOM   721  C CD  . ARG A 1 94  ? -3.934  -57.036 -14.217 1.00 159.72 ? 94  ARG A CD  1 
ATOM   722  N NE  . ARG A 1 94  ? -2.602  -56.945 -14.817 1.00 172.07 ? 94  ARG A NE  1 
ATOM   723  C CZ  . ARG A 1 94  ? -1.776  -57.945 -15.000 1.00 173.88 ? 94  ARG A CZ  1 
ATOM   724  N NH1 . ARG A 1 94  ? -2.102  -59.136 -14.544 1.00 176.97 ? 94  ARG A NH1 1 
ATOM   725  N NH2 . ARG A 1 94  ? -0.627  -57.725 -15.606 1.00 186.89 ? 94  ARG A NH2 1 
ATOM   726  N N   . PRO A 1 95  ? -2.788  -52.260 -16.824 1.00 146.79 ? 95  PRO A N   1 
ATOM   727  C CA  . PRO A 1 95  ? -2.351  -51.719 -18.111 1.00 146.99 ? 95  PRO A CA  1 
ATOM   728  C C   . PRO A 1 95  ? -2.748  -52.646 -19.252 1.00 130.61 ? 95  PRO A C   1 
ATOM   729  O O   . PRO A 1 95  ? -2.722  -53.859 -19.113 1.00 109.43 ? 95  PRO A O   1 
ATOM   730  C CB  . PRO A 1 95  ? -0.845  -51.573 -17.930 1.00 157.36 ? 95  PRO A CB  1 
ATOM   731  C CG  . PRO A 1 95  ? -0.730  -51.233 -16.453 1.00 172.39 ? 95  PRO A CG  1 
ATOM   732  C CD  . PRO A 1 95  ? -1.744  -52.179 -15.789 1.00 157.12 ? 95  PRO A CD  1 
ATOM   733  N N   . LEU A 1 96  ? -3.160  -52.037 -20.365 1.00 144.57 ? 96  LEU A N   1 
ATOM   734  C CA  . LEU A 1 96  ? -3.801  -52.753 -21.451 1.00 127.74 ? 96  LEU A CA  1 
ATOM   735  C C   . LEU A 1 96  ? -2.810  -53.693 -22.115 1.00 122.11 ? 96  LEU A C   1 
ATOM   736  O O   . LEU A 1 96  ? -3.209  -54.794 -22.502 1.00 107.69 ? 96  LEU A O   1 
ATOM   737  C CB  . LEU A 1 96  ? -4.415  -51.776 -22.452 1.00 134.91 ? 96  LEU A CB  1 
ATOM   738  C CG  . LEU A 1 96  ? -4.908  -52.398 -23.762 1.00 134.76 ? 96  LEU A CG  1 
ATOM   739  C CD1 . LEU A 1 96  ? -6.019  -53.374 -23.489 1.00 125.98 ? 96  LEU A CD1 1 
ATOM   740  C CD2 . LEU A 1 96  ? -5.388  -51.335 -24.733 1.00 161.78 ? 96  LEU A CD2 1 
ATOM   741  N N   . ASP A 1 97  ? -1.566  -53.218 -22.292 1.00 123.14 ? 97  ASP A N   1 
ATOM   742  C CA  . ASP A 1 97  ? -0.539  -53.974 -22.988 1.00 120.69 ? 97  ASP A CA  1 
ATOM   743  C C   . ASP A 1 97  ? -0.303  -55.315 -22.290 1.00 121.31 ? 97  ASP A C   1 
ATOM   744  O O   . ASP A 1 97  ? -0.224  -56.363 -22.945 1.00 112.06 ? 97  ASP A O   1 
ATOM   745  C CB  . ASP A 1 97  ? 0.694   -53.122 -23.222 1.00 118.08 ? 97  ASP A CB  1 
ATOM   746  C CG  . ASP A 1 97  ? 1.194   -52.378 -21.990 1.00 141.87 ? 97  ASP A CG  1 
ATOM   747  O OD1 . ASP A 1 97  ? 0.620   -52.578 -20.894 1.00 127.55 ? 97  ASP A OD1 1 
ATOM   748  O OD2 . ASP A 1 97  ? 2.160   -51.601 -22.127 1.00 171.41 ? 97  ASP A OD2 1 
ATOM   749  N N   . SER A 1 98  ? -0.207  -55.241 -20.959 1.00 128.01 ? 98  SER A N   1 
ATOM   750  C CA  . SER A 1 98  ? 0.013   -56.412 -20.115 1.00 126.29 ? 98  SER A CA  1 
ATOM   751  C C   . SER A 1 98  ? -1.099  -57.435 -20.333 1.00 135.73 ? 98  SER A C   1 
ATOM   752  O O   . SER A 1 98  ? -0.846  -58.637 -20.502 1.00 147.75 ? 98  SER A O   1 
ATOM   753  C CB  . SER A 1 98  ? 0.074   -56.035 -18.653 1.00 123.99 ? 98  SER A CB  1 
ATOM   754  O OG  . SER A 1 98  ? 1.180   -55.186 -18.382 1.00 154.87 ? 98  SER A OG  1 
ATOM   755  N N   . LEU A 1 99  ? -2.327  -56.912 -20.316 1.00 147.48 ? 99  LEU A N   1 
ATOM   756  C CA  . LEU A 1 99  ? -3.536  -57.714 -20.496 1.00 137.22 ? 99  LEU A CA  1 
ATOM   757  C C   . LEU A 1 99  ? -3.481  -58.444 -21.837 1.00 130.75 ? 99  LEU A C   1 
ATOM   758  O O   . LEU A 1 99  ? -3.762  -59.649 -21.922 1.00 135.88 ? 99  LEU A O   1 
ATOM   759  C CB  . LEU A 1 99  ? -4.792  -56.851 -20.354 1.00 137.23 ? 99  LEU A CB  1 
ATOM   760  C CG  . LEU A 1 99  ? -4.973  -56.125 -19.015 1.00 143.99 ? 99  LEU A CG  1 
ATOM   761  C CD1 . LEU A 1 99  ? -6.225  -55.266 -18.934 1.00 128.98 ? 99  LEU A CD1 1 
ATOM   762  C CD2 . LEU A 1 99  ? -4.966  -57.153 -17.906 1.00 163.49 ? 99  LEU A CD2 1 
ATOM   763  N N   . VAL A 1 100 ? -3.109  -57.682 -22.866 1.00 117.09 ? 100 VAL A N   1 
ATOM   764  C CA  . VAL A 1 100 ? -2.995  -58.180 -24.234 1.00 112.48 ? 100 VAL A CA  1 
ATOM   765  C C   . VAL A 1 100 ? -2.010  -59.346 -24.280 1.00 130.75 ? 100 VAL A C   1 
ATOM   766  O O   . VAL A 1 100 ? -2.281  -60.395 -24.880 1.00 156.89 ? 100 VAL A O   1 
ATOM   767  C CB  . VAL A 1 100 ? -2.473  -57.059 -25.158 1.00 109.32 ? 100 VAL A CB  1 
ATOM   768  C CG1 . VAL A 1 100 ? -1.969  -57.622 -26.485 1.00 102.68 ? 100 VAL A CG1 1 
ATOM   769  C CG2 . VAL A 1 100 ? -3.486  -55.927 -25.376 1.00 115.17 ? 100 VAL A CG2 1 
ATOM   770  N N   . LEU A 1 101 ? -0.864  -59.117 -23.638 1.00 140.89 ? 101 LEU A N   1 
ATOM   771  C CA  . LEU A 1 101 ? 0.219   -60.095 -23.575 1.00 131.54 ? 101 LEU A CA  1 
ATOM   772  C C   . LEU A 1 101 ? -0.283  -61.392 -22.942 1.00 140.17 ? 101 LEU A C   1 
ATOM   773  O O   . LEU A 1 101 ? -0.020  -62.490 -23.460 1.00 145.25 ? 101 LEU A O   1 
ATOM   774  C CB  . LEU A 1 101 ? 1.405   -59.510 -22.821 1.00 127.06 ? 101 LEU A CB  1 
ATOM   775  C CG  . LEU A 1 101 ? 2.769   -60.101 -23.178 1.00 139.45 ? 101 LEU A CG  1 
ATOM   776  C CD1 . LEU A 1 101 ? 3.013   -60.203 -24.681 1.00 141.72 ? 101 LEU A CD1 1 
ATOM   777  C CD2 . LEU A 1 101 ? 3.804   -59.205 -22.525 1.00 158.73 ? 101 LEU A CD2 1 
ATOM   778  N N   . GLU A 1 102 ? -1.007  -61.222 -21.832 1.00 147.65 ? 102 GLU A N   1 
ATOM   779  C CA  . GLU A 1 102 ? -1.587  -62.343 -21.100 1.00 148.21 ? 102 GLU A CA  1 
ATOM   780  C C   . GLU A 1 102 ? -2.479  -63.197 -22.003 1.00 148.89 ? 102 GLU A C   1 
ATOM   781  O O   . GLU A 1 102 ? -2.374  -64.421 -21.948 1.00 163.48 ? 102 GLU A O   1 
ATOM   782  C CB  . GLU A 1 102 ? -2.269  -62.024 -19.778 1.00 159.81 ? 102 GLU A CB  1 
ATOM   783  C CG  . GLU A 1 102 ? -1.273  -61.584 -18.713 1.00 187.34 ? 102 GLU A CG  1 
ATOM   784  C CD  . GLU A 1 102 ? -2.036  -61.019 -17.532 1.00 224.46 ? 102 GLU A CD  1 
ATOM   785  O OE1 . GLU A 1 102 ? -3.294  -61.057 -17.528 1.00 217.45 ? 102 GLU A OE1 1 
ATOM   786  O OE2 . GLU A 1 102 ? -1.352  -60.518 -16.614 1.00 248.75 ? 102 GLU A OE2 1 
ATOM   787  N N   . ASP A 1 103 ? -3.242  -62.587 -22.914 1.00 149.15 ? 103 ASP A N   1 
ATOM   788  C CA  . ASP A 1 103 ? -4.100  -63.329 -23.833 1.00 163.30 ? 103 ASP A CA  1 
ATOM   789  C C   . ASP A 1 103 ? -3.286  -63.868 -25.015 1.00 170.92 ? 103 ASP A C   1 
ATOM   790  O O   . ASP A 1 103 ? -3.097  -63.196 -26.036 1.00 152.05 ? 103 ASP A O   1 
ATOM   791  C CB  . ASP A 1 103 ? -5.321  -62.495 -24.203 1.00 172.94 ? 103 ASP A CB  1 
ATOM   792  C CG  . ASP A 1 103 ? -6.378  -63.121 -25.101 1.00 170.95 ? 103 ASP A CG  1 
ATOM   793  O OD1 . ASP A 1 103 ? -6.229  -64.306 -25.463 1.00 179.63 ? 103 ASP A OD1 1 
ATOM   794  O OD2 . ASP A 1 103 ? -7.343  -62.401 -25.437 1.00 166.59 ? 103 ASP A OD2 1 
ATOM   795  N N   . GLU A 1 104 ? -2.852  -65.127 -24.888 1.00 181.72 ? 104 GLU A N   1 
ATOM   796  C CA  . GLU A 1 104 ? -1.949  -65.749 -25.843 1.00 180.79 ? 104 GLU A CA  1 
ATOM   797  C C   . GLU A 1 104 ? -2.570  -65.712 -27.240 1.00 173.78 ? 104 GLU A C   1 
ATOM   798  O O   . GLU A 1 104 ? -1.886  -65.418 -28.226 1.00 153.69 ? 104 GLU A O   1 
ATOM   799  C CB  . GLU A 1 104 ? -1.722  -67.194 -25.399 1.00 177.18 ? 104 GLU A CB  1 
ATOM   800  C CG  . GLU A 1 104 ? -0.891  -67.307 -24.125 1.00 192.10 ? 104 GLU A CG  1 
ATOM   801  C CD  . GLU A 1 104 ? 0.562   -66.894 -24.298 1.00 207.88 ? 104 GLU A CD  1 
ATOM   802  O OE1 . GLU A 1 104 ? 0.862   -65.680 -24.437 1.00 202.31 ? 104 GLU A OE1 1 
ATOM   803  O OE2 . GLU A 1 104 ? 1.405   -67.817 -24.326 1.00 238.92 ? 104 GLU A OE2 1 
ATOM   804  N N   . ALA A 1 105 ? -3.849  -66.095 -27.287 1.00 178.88 ? 105 ALA A N   1 
ATOM   805  C CA  . ALA A 1 105 ? -4.589  -66.236 -28.528 1.00 186.29 ? 105 ALA A CA  1 
ATOM   806  C C   . ALA A 1 105 ? -4.595  -64.914 -29.292 1.00 170.60 ? 105 ALA A C   1 
ATOM   807  O O   . ALA A 1 105 ? -4.342  -64.876 -30.507 1.00 160.50 ? 105 ALA A O   1 
ATOM   808  C CB  . ALA A 1 105 ? -5.997  -66.708 -28.222 1.00 203.07 ? 105 ALA A CB  1 
ATOM   809  N N   . LEU A 1 106 ? -4.889  -63.848 -28.543 1.00 158.70 ? 106 LEU A N   1 
ATOM   810  C CA  . LEU A 1 106 ? -4.959  -62.496 -29.094 1.00 152.55 ? 106 LEU A CA  1 
ATOM   811  C C   . LEU A 1 106 ? -3.620  -62.121 -29.726 1.00 147.15 ? 106 LEU A C   1 
ATOM   812  O O   . LEU A 1 106 ? -3.569  -61.593 -30.850 1.00 144.34 ? 106 LEU A O   1 
ATOM   813  C CB  . LEU A 1 106 ? -5.415  -61.469 -28.051 1.00 157.21 ? 106 LEU A CB  1 
ATOM   814  C CG  . LEU A 1 106 ? -5.292  -59.974 -28.406 1.00 152.38 ? 106 LEU A CG  1 
ATOM   815  C CD1 . LEU A 1 106 ? -5.941  -59.507 -29.707 1.00 146.71 ? 106 LEU A CD1 1 
ATOM   816  C CD2 . LEU A 1 106 ? -5.810  -59.107 -27.278 1.00 139.08 ? 106 LEU A CD2 1 
ATOM   817  N N   . VAL A 1 107 ? -2.555  -62.416 -28.969 1.00 137.92 ? 107 VAL A N   1 
ATOM   818  C CA  . VAL A 1 107 ? -1.188  -62.122 -29.393 1.00 133.59 ? 107 VAL A CA  1 
ATOM   819  C C   . VAL A 1 107 ? -0.889  -62.833 -30.713 1.00 138.23 ? 107 VAL A C   1 
ATOM   820  O O   . VAL A 1 107 ? -0.332  -62.234 -31.647 1.00 116.50 ? 107 VAL A O   1 
ATOM   821  C CB  . VAL A 1 107 ? -0.054  -62.364 -28.377 1.00 125.56 ? 107 VAL A CB  1 
ATOM   822  C CG1 . VAL A 1 107 ? 1.248   -61.752 -28.876 1.00 130.39 ? 107 VAL A CG1 1 
ATOM   823  C CG2 . VAL A 1 107 ? -0.358  -61.805 -27.001 1.00 119.32 ? 107 VAL A CG2 1 
ATOM   824  N N   . GLU A 1 108 ? -1.273  -64.109 -30.752 1.00 145.53 ? 108 GLU A N   1 
ATOM   825  C CA  . GLU A 1 108 ? -1.077  -64.964 -31.916 1.00 150.65 ? 108 GLU A CA  1 
ATOM   826  C C   . GLU A 1 108 ? -1.759  -64.354 -33.137 1.00 150.47 ? 108 GLU A C   1 
ATOM   827  O O   . GLU A 1 108 ? -1.168  -64.273 -34.227 1.00 149.20 ? 108 GLU A O   1 
ATOM   828  C CB  . GLU A 1 108 ? -1.722  -66.313 -31.600 1.00 158.62 ? 108 GLU A CB  1 
ATOM   829  C CG  . GLU A 1 108 ? -0.783  -67.308 -30.923 1.00 205.43 ? 108 GLU A CG  1 
ATOM   830  C CD  . GLU A 1 108 ? 0.330   -67.797 -31.836 1.00 235.55 ? 108 GLU A CD  1 
ATOM   831  O OE1 . GLU A 1 108 ? 0.019   -68.013 -33.033 1.00 265.73 ? 108 GLU A OE1 1 
ATOM   832  O OE2 . GLU A 1 108 ? 1.479   -67.976 -31.363 1.00 212.68 ? 108 GLU A OE2 1 
ATOM   833  N N   . THR A 1 109 ? -3.008  -63.930 -32.911 1.00 136.93 ? 109 THR A N   1 
ATOM   834  C CA  . THR A 1 109 ? -3.833  -63.326 -33.954 1.00 129.74 ? 109 THR A CA  1 
ATOM   835  C C   . THR A 1 109 ? -3.142  -62.090 -34.515 1.00 131.39 ? 109 THR A C   1 
ATOM   836  O O   . THR A 1 109 ? -3.069  -61.904 -35.738 1.00 127.95 ? 109 THR A O   1 
ATOM   837  C CB  . THR A 1 109 ? -5.281  -63.039 -33.561 1.00 131.16 ? 109 THR A CB  1 
ATOM   838  O OG1 . THR A 1 109 ? -5.767  -64.170 -32.847 1.00 158.01 ? 109 THR A OG1 1 
ATOM   839  C CG2 . THR A 1 109 ? -6.151  -62.863 -34.796 1.00 129.75 ? 109 THR A CG2 1 
ATOM   840  N N   . LEU A 1 110 ? -2.644  -61.267 -33.589 1.00 138.83 ? 110 LEU A N   1 
ATOM   841  C CA  . LEU A 1 110 ? -1.949  -60.024 -33.920 1.00 140.13 ? 110 LEU A CA  1 
ATOM   842  C C   . LEU A 1 110 ? -0.749  -60.319 -34.816 1.00 134.23 ? 110 LEU A C   1 
ATOM   843  O O   . LEU A 1 110 ? -0.533  -59.649 -35.843 1.00 109.31 ? 110 LEU A O   1 
ATOM   844  C CB  . LEU A 1 110 ? -1.525  -59.220 -32.685 1.00 136.31 ? 110 LEU A CB  1 
ATOM   845  C CG  . LEU A 1 110 ? -2.645  -58.590 -31.841 1.00 131.71 ? 110 LEU A CG  1 
ATOM   846  C CD1 . LEU A 1 110 ? -2.162  -58.040 -30.511 1.00 116.69 ? 110 LEU A CD1 1 
ATOM   847  C CD2 . LEU A 1 110 ? -3.373  -57.499 -32.611 1.00 127.97 ? 110 LEU A CD2 1 
ATOM   848  N N   . ARG A 1 111 ? 0.010   -61.333 -34.393 1.00 148.53 ? 111 ARG A N   1 
ATOM   849  C CA  . ARG A 1 111 ? 1.211   -61.773 -35.098 1.00 158.92 ? 111 ARG A CA  1 
ATOM   850  C C   . ARG A 1 111 ? 0.861   -62.162 -36.533 1.00 155.31 ? 111 ARG A C   1 
ATOM   851  O O   . ARG A 1 111 ? 1.540   -61.761 -37.495 1.00 147.08 ? 111 ARG A O   1 
ATOM   852  C CB  . ARG A 1 111 ? 1.845   -62.973 -34.377 1.00 157.20 ? 111 ARG A CB  1 
ATOM   853  C CG  . ARG A 1 111 ? 3.065   -63.551 -35.085 1.00 174.95 ? 111 ARG A CG  1 
ATOM   854  C CD  . ARG A 1 111 ? 3.800   -64.700 -34.384 1.00 174.90 ? 111 ARG A CD  1 
ATOM   855  N NE  . ARG A 1 111 ? 3.041   -65.950 -34.310 1.00 188.19 ? 111 ARG A NE  1 
ATOM   856  C CZ  . ARG A 1 111 ? 2.521   -66.643 -35.322 1.00 201.37 ? 111 ARG A CZ  1 
ATOM   857  N NH1 . ARG A 1 111 ? 2.753   -66.309 -36.579 1.00 212.40 ? 111 ARG A NH1 1 
ATOM   858  N NH2 . ARG A 1 111 ? 1.773   -67.705 -35.071 1.00 192.96 ? 111 ARG A NH2 1 
ATOM   859  N N   . ARG A 1 112 ? -0.211  -62.950 -36.635 1.00 158.77 ? 112 ARG A N   1 
ATOM   860  C CA  . ARG A 1 112 ? -0.705  -63.449 -37.915 1.00 175.36 ? 112 ARG A CA  1 
ATOM   861  C C   . ARG A 1 112 ? -1.044  -62.280 -38.836 1.00 176.03 ? 112 ARG A C   1 
ATOM   862  O O   . ARG A 1 112 ? -0.670  -62.274 -40.013 1.00 185.17 ? 112 ARG A O   1 
ATOM   863  C CB  . ARG A 1 112 ? -1.853  -64.438 -37.698 1.00 189.24 ? 112 ARG A CB  1 
ATOM   864  C CG  . ARG A 1 112 ? -1.354  -65.589 -36.831 1.00 179.10 ? 112 ARG A CG  1 
ATOM   865  C CD  . ARG A 1 112 ? -2.394  -66.633 -36.518 1.00 170.64 ? 112 ARG A CD  1 
ATOM   866  N NE  . ARG A 1 112 ? -2.744  -67.354 -37.743 1.00 194.28 ? 112 ARG A NE  1 
ATOM   867  C CZ  . ARG A 1 112 ? -3.868  -68.037 -37.927 1.00 225.94 ? 112 ARG A CZ  1 
ATOM   868  N NH1 . ARG A 1 112 ? -4.830  -68.014 -37.014 1.00 228.49 ? 112 ARG A NH1 1 
ATOM   869  N NH2 . ARG A 1 112 ? -4.042  -68.714 -39.049 1.00 253.10 ? 112 ARG A NH2 1 
ATOM   870  N N   . ALA A 1 113 ? -1.748  -61.307 -38.260 1.00 163.36 ? 113 ALA A N   1 
ATOM   871  C CA  . ALA A 1 113 ? -2.177  -60.109 -38.973 1.00 168.60 ? 113 ALA A CA  1 
ATOM   872  C C   . ALA A 1 113 ? -0.967  -59.371 -39.534 1.00 158.59 ? 113 ALA A C   1 
ATOM   873  O O   . ALA A 1 113 ? -0.955  -58.966 -40.716 1.00 154.14 ? 113 ALA A O   1 
ATOM   874  C CB  . ALA A 1 113 ? -2.975  -59.209 -38.064 1.00 210.74 ? 113 ALA A CB  1 
ATOM   875  N N   . VAL A 1 114 ? 0.036   -59.222 -38.663 1.00 141.27 ? 114 VAL A N   1 
ATOM   876  C CA  . VAL A 1 114 ? 1.271   -58.525 -39.012 1.00 136.91 ? 114 VAL A CA  1 
ATOM   877  C C   . VAL A 1 114 ? 1.942   -59.223 -40.199 1.00 168.53 ? 114 VAL A C   1 
ATOM   878  O O   . VAL A 1 114 ? 2.377   -58.565 -41.163 1.00 171.57 ? 114 VAL A O   1 
ATOM   879  C CB  . VAL A 1 114 ? 2.267   -58.299 -37.862 1.00 132.04 ? 114 VAL A CB  1 
ATOM   880  C CG1 . VAL A 1 114 ? 3.524   -57.558 -38.334 1.00 139.85 ? 114 VAL A CG1 1 
ATOM   881  C CG2 . VAL A 1 114 ? 1.616   -57.605 -36.673 1.00 115.07 ? 114 VAL A CG2 1 
ATOM   882  N N   . ALA A 1 115 ? 1.997   -60.554 -40.100 1.00 180.26 ? 115 ALA A N   1 
ATOM   883  C CA  . ALA A 1 115 ? 2.603   -61.393 -41.127 1.00 174.60 ? 115 ALA A CA  1 
ATOM   884  C C   . ALA A 1 115 ? 1.906   -61.181 -42.465 1.00 170.98 ? 115 ALA A C   1 
ATOM   885  O O   . ALA A 1 115 ? 2.549   -61.019 -43.505 1.00 204.62 ? 115 ALA A O   1 
ATOM   886  C CB  . ALA A 1 115 ? 2.598   -62.839 -40.701 1.00 177.55 ? 115 ALA A CB  1 
ATOM   887  N N   . GLU A 1 116 ? 0.578   -61.173 -42.400 1.00 174.41 ? 116 GLU A N   1 
ATOM   888  C CA  . GLU A 1 116 ? -0.290  -61.002 -43.560 1.00 214.41 ? 116 GLU A CA  1 
ATOM   889  C C   . GLU A 1 116 ? 0.100   -59.736 -44.321 1.00 198.26 ? 116 GLU A C   1 
ATOM   890  O O   . GLU A 1 116 ? 0.135   -59.770 -45.549 1.00 186.52 ? 116 GLU A O   1 
ATOM   891  C CB  . GLU A 1 116 ? -1.722  -61.136 -43.037 1.00 255.77 ? 116 GLU A CB  1 
ATOM   892  C CG  . GLU A 1 116 ? -2.550  -62.220 -43.725 1.00 265.38 ? 116 GLU A CG  1 
ATOM   893  C CD  . GLU A 1 116 ? -3.109  -61.820 -45.071 1.00 272.58 ? 116 GLU A CD  1 
ATOM   894  O OE1 . GLU A 1 116 ? -3.860  -60.826 -45.113 1.00 294.45 ? 116 GLU A OE1 1 
ATOM   895  O OE2 . GLU A 1 116 ? -2.804  -62.502 -46.068 1.00 280.84 ? 116 GLU A OE2 1 
ATOM   896  N N   . ARG A 1 117 ? 0.650   -58.741 -43.624 1.00 199.55 ? 117 ARG A N   1 
ATOM   897  C CA  . ARG A 1 117 ? 1.008   -57.520 -44.324 1.00 188.52 ? 117 ARG A CA  1 
ATOM   898  C C   . ARG A 1 117 ? 2.522   -57.308 -44.432 1.00 165.24 ? 117 ARG A C   1 
ATOM   899  O O   . ARG A 1 117 ? 3.300   -57.742 -43.575 1.00 129.47 ? 117 ARG A O   1 
ATOM   900  C CB  . ARG A 1 117 ? 0.254   -56.330 -43.725 1.00 196.48 ? 117 ARG A CB  1 
ATOM   901  C CG  . ARG A 1 117 ? -1.206  -56.254 -44.141 1.00 193.16 ? 117 ARG A CG  1 
ATOM   902  C CD  . ARG A 1 117 ? -1.440  -56.156 -45.642 1.00 195.11 ? 117 ARG A CD  1 
ATOM   903  N NE  . ARG A 1 117 ? -2.889  -56.188 -45.860 1.00 218.76 ? 117 ARG A NE  1 
ATOM   904  C CZ  . ARG A 1 117 ? -3.605  -55.129 -46.219 1.00 234.91 ? 117 ARG A CZ  1 
ATOM   905  N NH1 . ARG A 1 117 ? -2.981  -53.993 -46.479 1.00 253.03 ? 117 ARG A NH1 1 
ATOM   906  N NH2 . ARG A 1 117 ? -4.925  -55.195 -46.322 1.00 224.16 ? 117 ARG A NH2 1 
ATOM   907  N N   . PRO A 1 118 ? 2.966   -56.615 -45.512 1.00 164.72 ? 118 PRO A N   1 
ATOM   908  C CA  . PRO A 1 118 ? 4.333   -56.093 -45.610 1.00 166.83 ? 118 PRO A CA  1 
ATOM   909  C C   . PRO A 1 118 ? 4.992   -55.551 -44.341 1.00 168.36 ? 118 PRO A C   1 
ATOM   910  O O   . PRO A 1 118 ? 6.120   -55.930 -44.038 1.00 193.99 ? 118 PRO A O   1 
ATOM   911  C CB  . PRO A 1 118 ? 4.191   -55.008 -46.707 1.00 158.12 ? 118 PRO A CB  1 
ATOM   912  C CG  . PRO A 1 118 ? 3.112   -55.554 -47.629 1.00 159.45 ? 118 PRO A CG  1 
ATOM   913  C CD  . PRO A 1 118 ? 2.167   -56.325 -46.721 1.00 158.94 ? 118 PRO A CD  1 
ATOM   914  N N   . ALA A 1 119 ? 4.275   -54.691 -43.615 1.00 160.28 ? 119 ALA A N   1 
ATOM   915  C CA  . ALA A 1 119 ? 4.855   -53.822 -42.605 1.00 162.30 ? 119 ALA A CA  1 
ATOM   916  C C   . ALA A 1 119 ? 4.017   -53.806 -41.325 1.00 180.41 ? 119 ALA A C   1 
ATOM   917  O O   . ALA A 1 119 ? 2.777   -53.803 -41.356 1.00 245.35 ? 119 ALA A O   1 
ATOM   918  C CB  . ALA A 1 119 ? 5.017   -52.415 -43.156 1.00 147.90 ? 119 ALA A CB  1 
ATOM   919  N N   . GLY A 1 120 ? 4.736   -53.739 -40.199 1.00 170.08 ? 120 GLY A N   1 
ATOM   920  C CA  . GLY A 1 120 ? 4.154   -53.777 -38.870 1.00 168.72 ? 120 GLY A CA  1 
ATOM   921  C C   . GLY A 1 120 ? 4.615   -52.598 -38.020 1.00 181.72 ? 120 GLY A C   1 
ATOM   922  O O   . GLY A 1 120 ? 5.788   -52.300 -37.929 1.00 213.09 ? 120 GLY A O   1 
ATOM   923  N N   . THR A 1 121 ? 3.640   -51.903 -37.447 1.00 168.97 ? 121 THR A N   1 
ATOM   924  C CA  . THR A 1 121 ? 3.827   -50.795 -36.526 1.00 149.44 ? 121 THR A CA  1 
ATOM   925  C C   . THR A 1 121 ? 2.857   -50.992 -35.374 1.00 132.17 ? 121 THR A C   1 
ATOM   926  O O   . THR A 1 121 ? 1.646   -51.139 -35.577 1.00 141.41 ? 121 THR A O   1 
ATOM   927  C CB  . THR A 1 121 ? 3.522   -49.451 -37.205 1.00 145.93 ? 121 THR A CB  1 
ATOM   928  O OG1 . THR A 1 121 ? 4.162   -49.393 -38.474 1.00 167.08 ? 121 THR A OG1 1 
ATOM   929  C CG2 . THR A 1 121 ? 3.971   -48.252 -36.397 1.00 118.59 ? 121 THR A CG2 1 
ATOM   930  N N   . ILE A 1 122 ? 3.374   -50.797 -34.145 1.00 116.77 ? 122 ILE A N   1 
ATOM   931  C CA  . ILE A 1 122 ? 2.562   -50.766 -32.928 1.00 127.21 ? 122 ILE A CA  1 
ATOM   932  C C   . ILE A 1 122 ? 2.451   -49.335 -32.401 1.00 146.31 ? 122 ILE A C   1 
ATOM   933  O O   . ILE A 1 122 ? 3.456   -48.671 -32.167 1.00 148.91 ? 122 ILE A O   1 
ATOM   934  C CB  . ILE A 1 122 ? 3.038   -51.777 -31.851 1.00 132.95 ? 122 ILE A CB  1 
ATOM   935  C CG1 . ILE A 1 122 ? 2.695   -53.227 -32.199 1.00 148.90 ? 122 ILE A CG1 1 
ATOM   936  C CG2 . ILE A 1 122 ? 2.523   -51.441 -30.447 1.00 123.82 ? 122 ILE A CG2 1 
ATOM   937  C CD1 . ILE A 1 122 ? 3.083   -54.241 -31.127 1.00 159.38 ? 122 ILE A CD1 1 
ATOM   938  N N   . VAL A 1 123 ? 1.196   -48.887 -32.213 1.00 159.72 ? 123 VAL A N   1 
ATOM   939  C CA  . VAL A 1 123 ? 0.879   -47.513 -31.847 1.00 140.88 ? 123 VAL A CA  1 
ATOM   940  C C   . VAL A 1 123 ? 0.511   -47.416 -30.363 1.00 144.02 ? 123 VAL A C   1 
ATOM   941  O O   . VAL A 1 123 ? -0.531  -47.912 -29.958 1.00 140.60 ? 123 VAL A O   1 
ATOM   942  C CB  . VAL A 1 123 ? -0.260  -46.962 -32.733 1.00 124.14 ? 123 VAL A CB  1 
ATOM   943  C CG1 . VAL A 1 123 ? -0.576  -45.499 -32.415 1.00 133.08 ? 123 VAL A CG1 1 
ATOM   944  C CG2 . VAL A 1 123 ? 0.019   -47.150 -34.224 1.00 122.95 ? 123 VAL A CG2 1 
ATOM   945  N N   . ASP A 1 124 ? 1.408   -46.795 -29.581 1.00 146.94 ? 124 ASP A N   1 
ATOM   946  C CA  . ASP A 1 124 ? 1.381   -46.872 -28.129 1.00 150.73 ? 124 ASP A CA  1 
ATOM   947  C C   . ASP A 1 124 ? 1.564   -45.514 -27.458 1.00 152.33 ? 124 ASP A C   1 
ATOM   948  O O   . ASP A 1 124 ? 2.081   -44.528 -28.003 1.00 160.19 ? 124 ASP A O   1 
ATOM   949  C CB  . ASP A 1 124 ? 2.446   -47.792 -27.537 1.00 144.94 ? 124 ASP A CB  1 
ATOM   950  C CG  . ASP A 1 124 ? 3.862   -47.646 -28.087 1.00 155.53 ? 124 ASP A CG  1 
ATOM   951  O OD1 . ASP A 1 124 ? 4.025   -46.999 -29.151 1.00 170.50 ? 124 ASP A OD1 1 
ATOM   952  O OD2 . ASP A 1 124 ? 4.804   -48.196 -27.465 1.00 152.86 ? 124 ASP A OD2 1 
ATOM   953  N N   . PHE A 1 125 ? 1.230   -45.483 -26.169 1.00 148.61 ? 125 PHE A N   1 
ATOM   954  C CA  . PHE A 1 125 ? 1.393   -44.233 -25.451 1.00 151.56 ? 125 PHE A CA  1 
ATOM   955  C C   . PHE A 1 125 ? 2.862   -44.035 -25.050 1.00 157.65 ? 125 PHE A C   1 
ATOM   956  O O   . PHE A 1 125 ? 3.556   -43.150 -25.575 1.00 136.70 ? 125 PHE A O   1 
ATOM   957  C CB  . PHE A 1 125 ? 0.338   -44.064 -24.352 1.00 134.25 ? 125 PHE A CB  1 
ATOM   958  C CG  . PHE A 1 125 ? 0.369   -42.644 -23.819 1.00 136.32 ? 125 PHE A CG  1 
ATOM   959  C CD1 . PHE A 1 125 ? -0.218  -41.603 -24.546 1.00 147.36 ? 125 PHE A CD1 1 
ATOM   960  C CD2 . PHE A 1 125 ? 1.055   -42.343 -22.644 1.00 129.61 ? 125 PHE A CD2 1 
ATOM   961  C CE1 . PHE A 1 125 ? -0.157  -40.290 -24.096 1.00 150.55 ? 125 PHE A CE1 1 
ATOM   962  C CE2 . PHE A 1 125 ? 1.141   -41.024 -22.206 1.00 146.12 ? 125 PHE A CE2 1 
ATOM   963  C CZ  . PHE A 1 125 ? 0.521   -40.006 -22.921 1.00 157.00 ? 125 PHE A CZ  1 
ATOM   964  N N   . SER A 1 126 ? 3.312   -44.847 -24.086 1.00 154.75 ? 126 SER A N   1 
ATOM   965  C CA  . SER A 1 126 ? 4.702   -44.860 -23.664 1.00 157.75 ? 126 SER A CA  1 
ATOM   966  C C   . SER A 1 126 ? 5.245   -46.261 -23.870 1.00 163.11 ? 126 SER A C   1 
ATOM   967  O O   . SER A 1 126 ? 4.494   -47.226 -23.712 1.00 147.15 ? 126 SER A O   1 
ATOM   968  C CB  . SER A 1 126 ? 4.873   -44.439 -22.229 1.00 179.57 ? 126 SER A CB  1 
ATOM   969  O OG  . SER A 1 126 ? 3.931   -45.106 -21.400 1.00 193.52 ? 126 SER A OG  1 
ATOM   970  N N   . ALA A 1 127 ? 6.527   -46.319 -24.263 1.00 170.96 ? 127 ALA A N   1 
ATOM   971  C CA  . ALA A 1 127 ? 7.258   -47.559 -24.459 1.00 151.86 ? 127 ALA A CA  1 
ATOM   972  C C   . ALA A 1 127 ? 7.363   -48.269 -23.117 1.00 145.01 ? 127 ALA A C   1 
ATOM   973  O O   . ALA A 1 127 ? 7.567   -47.615 -22.092 1.00 111.68 ? 127 ALA A O   1 
ATOM   974  C CB  . ALA A 1 127 ? 8.614   -47.238 -25.003 1.00 140.70 ? 127 ALA A CB  1 
ATOM   975  N N   . SER A 1 128 ? 7.157   -49.593 -23.135 1.00 153.76 ? 128 SER A N   1 
ATOM   976  C CA  . SER A 1 128 ? 7.012   -50.351 -21.901 1.00 166.29 ? 128 SER A CA  1 
ATOM   977  C C   . SER A 1 128 ? 7.491   -51.774 -22.128 1.00 157.19 ? 128 SER A C   1 
ATOM   978  O O   . SER A 1 128 ? 7.627   -52.205 -23.268 1.00 166.44 ? 128 SER A O   1 
ATOM   979  C CB  . SER A 1 128 ? 5.581   -50.358 -21.365 1.00 186.13 ? 128 SER A CB  1 
ATOM   980  O OG  . SER A 1 128 ? 4.795   -51.431 -21.878 1.00 140.97 ? 128 SER A OG  1 
ATOM   981  N N   . PRO A 1 129 ? 7.740   -52.547 -21.048 1.00 142.46 ? 129 PRO A N   1 
ATOM   982  C CA  . PRO A 1 129 ? 8.212   -53.917 -21.222 1.00 136.81 ? 129 PRO A CA  1 
ATOM   983  C C   . PRO A 1 129 ? 7.216   -54.642 -22.132 1.00 149.56 ? 129 PRO A C   1 
ATOM   984  O O   . PRO A 1 129 ? 7.620   -55.344 -23.064 1.00 157.66 ? 129 PRO A O   1 
ATOM   985  C CB  . PRO A 1 129 ? 8.157   -54.451 -19.782 1.00 132.82 ? 129 PRO A CB  1 
ATOM   986  C CG  . PRO A 1 129 ? 8.368   -53.236 -18.916 1.00 129.81 ? 129 PRO A CG  1 
ATOM   987  C CD  . PRO A 1 129 ? 7.649   -52.125 -19.637 1.00 136.71 ? 129 PRO A CD  1 
ATOM   988  N N   . ALA A 1 130 ? 5.938   -54.538 -21.741 1.00 152.49 ? 130 ALA A N   1 
ATOM   989  C CA  . ALA A 1 130 ? 4.873   -55.319 -22.345 1.00 162.99 ? 130 ALA A CA  1 
ATOM   990  C C   . ALA A 1 130 ? 4.788   -55.015 -23.842 1.00 172.26 ? 130 ALA A C   1 
ATOM   991  O O   . ALA A 1 130 ? 4.693   -55.938 -24.675 1.00 182.56 ? 130 ALA A O   1 
ATOM   992  C CB  . ALA A 1 130 ? 3.569   -55.061 -21.609 1.00 182.92 ? 130 ALA A CB  1 
ATOM   993  N N   . THR A 1 131 ? 4.833   -53.704 -24.144 1.00 157.76 ? 131 THR A N   1 
ATOM   994  C CA  . THR A 1 131 ? 4.734   -53.248 -25.531 1.00 145.14 ? 131 THR A CA  1 
ATOM   995  C C   . THR A 1 131 ? 5.890   -53.815 -26.351 1.00 169.83 ? 131 THR A C   1 
ATOM   996  O O   . THR A 1 131 ? 5.680   -54.291 -27.474 1.00 190.74 ? 131 THR A O   1 
ATOM   997  C CB  . THR A 1 131 ? 4.586   -51.741 -25.725 1.00 148.78 ? 131 THR A CB  1 
ATOM   998  O OG1 . THR A 1 131 ? 5.790   -51.082 -25.321 1.00 171.35 ? 131 THR A OG1 1 
ATOM   999  C CG2 . THR A 1 131 ? 3.342   -51.177 -25.059 1.00 161.78 ? 131 THR A CG2 1 
ATOM   1000 N N   . ASP A 1 132 ? 7.088   -53.764 -25.754 1.00 181.68 ? 132 ASP A N   1 
ATOM   1001 C CA  . ASP A 1 132 ? 8.299   -54.269 -26.394 1.00 151.38 ? 132 ASP A CA  1 
ATOM   1002 C C   . ASP A 1 132 ? 8.144   -55.748 -26.724 1.00 155.81 ? 132 ASP A C   1 
ATOM   1003 O O   . ASP A 1 132 ? 8.477   -56.188 -27.831 1.00 150.16 ? 132 ASP A O   1 
ATOM   1004 C CB  . ASP A 1 132 ? 9.559   -53.877 -25.646 1.00 152.32 ? 132 ASP A CB  1 
ATOM   1005 C CG  . ASP A 1 132 ? 10.036  -52.468 -25.948 1.00 181.85 ? 132 ASP A CG  1 
ATOM   1006 O OD1 . ASP A 1 132 ? 9.517   -51.866 -26.915 1.00 191.39 ? 132 ASP A OD1 1 
ATOM   1007 O OD2 . ASP A 1 132 ? 10.915  -51.985 -25.215 1.00 210.84 ? 132 ASP A OD2 1 
ATOM   1008 N N   . GLU A 1 133 ? 7.630   -56.484 -25.740 1.00 179.12 ? 133 GLU A N   1 
ATOM   1009 C CA  . GLU A 1 133 ? 7.401   -57.923 -25.858 1.00 193.43 ? 133 GLU A CA  1 
ATOM   1010 C C   . GLU A 1 133 ? 6.466   -58.206 -27.033 1.00 176.32 ? 133 GLU A C   1 
ATOM   1011 O O   . GLU A 1 133 ? 6.725   -59.098 -27.853 1.00 163.74 ? 133 GLU A O   1 
ATOM   1012 C CB  . GLU A 1 133 ? 6.874   -58.467 -24.528 1.00 206.56 ? 133 GLU A CB  1 
ATOM   1013 C CG  . GLU A 1 133 ? 6.514   -59.950 -24.553 1.00 226.12 ? 133 GLU A CG  1 
ATOM   1014 C CD  . GLU A 1 133 ? 7.691   -60.889 -24.724 1.00 246.03 ? 133 GLU A CD  1 
ATOM   1015 O OE1 . GLU A 1 133 ? 8.267   -60.924 -25.833 1.00 264.31 ? 133 GLU A OE1 1 
ATOM   1016 O OE2 . GLU A 1 133 ? 8.033   -61.576 -23.739 1.00 246.24 ? 133 GLU A OE2 1 
ATOM   1017 N N   . LEU A 1 134 ? 5.387   -57.423 -27.078 1.00 163.72 ? 134 LEU A N   1 
ATOM   1018 C CA  . LEU A 1 134 ? 4.370   -57.542 -28.121 1.00 158.79 ? 134 LEU A CA  1 
ATOM   1019 C C   . LEU A 1 134 ? 5.008   -57.339 -29.498 1.00 173.68 ? 134 LEU A C   1 
ATOM   1020 O O   . LEU A 1 134 ? 4.754   -58.104 -30.434 1.00 194.66 ? 134 LEU A O   1 
ATOM   1021 C CB  . LEU A 1 134 ? 3.112   -56.705 -27.894 1.00 138.94 ? 134 LEU A CB  1 
ATOM   1022 C CG  . LEU A 1 134 ? 2.232   -57.145 -26.716 1.00 132.15 ? 134 LEU A CG  1 
ATOM   1023 C CD1 . LEU A 1 134 ? 1.267   -56.072 -26.221 1.00 127.81 ? 134 LEU A CD1 1 
ATOM   1024 C CD2 . LEU A 1 134 ? 1.462   -58.397 -27.045 1.00 132.07 ? 134 LEU A CD2 1 
ATOM   1025 N N   . GLY A 1 135 ? 5.832   -56.298 -29.579 1.00 181.64 ? 135 GLY A N   1 
ATOM   1026 C CA  . GLY A 1 135 ? 6.539   -55.937 -30.802 1.00 176.80 ? 135 GLY A CA  1 
ATOM   1027 C C   . GLY A 1 135 ? 7.407   -57.103 -31.275 1.00 169.98 ? 135 GLY A C   1 
ATOM   1028 O O   . GLY A 1 135 ? 7.407   -57.466 -32.458 1.00 167.61 ? 135 GLY A O   1 
ATOM   1029 N N   . ARG A 1 136 ? 8.130   -57.672 -30.313 1.00 169.92 ? 136 ARG A N   1 
ATOM   1030 C CA  . ARG A 1 136 ? 9.033   -58.790 -30.562 1.00 180.98 ? 136 ARG A CA  1 
ATOM   1031 C C   . ARG A 1 136 ? 8.243   -59.977 -31.116 1.00 175.36 ? 136 ARG A C   1 
ATOM   1032 O O   . ARG A 1 136 ? 8.623   -60.615 -32.109 1.00 180.10 ? 136 ARG A O   1 
ATOM   1033 C CB  . ARG A 1 136 ? 9.977   -59.099 -29.393 1.00 199.49 ? 136 ARG A CB  1 
ATOM   1034 C CG  . ARG A 1 136 ? 11.082  -58.058 -29.253 1.00 231.80 ? 136 ARG A CG  1 
ATOM   1035 C CD  . ARG A 1 136 ? 12.083  -58.380 -28.149 1.00 237.30 ? 136 ARG A CD  1 
ATOM   1036 N NE  . ARG A 1 136 ? 11.492  -58.382 -26.805 1.00 242.77 ? 136 ARG A NE  1 
ATOM   1037 C CZ  . ARG A 1 136 ? 11.123  -59.471 -26.132 1.00 244.02 ? 136 ARG A CZ  1 
ATOM   1038 N NH1 . ARG A 1 136 ? 11.222  -60.671 -26.689 1.00 211.06 ? 136 ARG A NH1 1 
ATOM   1039 N NH2 . ARG A 1 136 ? 10.629  -59.353 -24.910 1.00 258.17 ? 136 ARG A NH2 1 
ATOM   1040 N N   . ARG A 1 137 ? 7.172   -60.300 -30.376 1.00 169.08 ? 137 ARG A N   1 
ATOM   1041 C CA  . ARG A 1 137 ? 6.430   -61.547 -30.489 1.00 168.13 ? 137 ARG A CA  1 
ATOM   1042 C C   . ARG A 1 137 ? 5.377   -61.469 -31.592 1.00 166.51 ? 137 ARG A C   1 
ATOM   1043 O O   . ARG A 1 137 ? 4.717   -62.471 -31.858 1.00 161.49 ? 137 ARG A O   1 
ATOM   1044 C CB  . ARG A 1 137 ? 5.706   -61.901 -29.185 1.00 156.14 ? 137 ARG A CB  1 
ATOM   1045 C CG  . ARG A 1 137 ? 6.553   -62.556 -28.105 1.00 153.88 ? 137 ARG A CG  1 
ATOM   1046 C CD  . ARG A 1 137 ? 5.740   -62.959 -26.887 1.00 155.50 ? 137 ARG A CD  1 
ATOM   1047 N NE  . ARG A 1 137 ? 4.597   -63.833 -27.155 1.00 162.39 ? 137 ARG A NE  1 
ATOM   1048 C CZ  . ARG A 1 137 ? 3.757   -64.301 -26.235 1.00 179.30 ? 137 ARG A CZ  1 
ATOM   1049 N NH1 . ARG A 1 137 ? 3.949   -64.067 -24.944 1.00 165.46 ? 137 ARG A NH1 1 
ATOM   1050 N NH2 . ARG A 1 137 ? 2.729   -65.033 -26.628 1.00 204.71 ? 137 ARG A NH2 1 
ATOM   1051 N N   . THR A 1 138 ? 5.214   -60.290 -32.210 1.00 169.33 ? 138 THR A N   1 
ATOM   1052 C CA  . THR A 1 138 ? 4.237   -60.104 -33.274 1.00 176.81 ? 138 THR A CA  1 
ATOM   1053 C C   . THR A 1 138 ? 4.924   -59.656 -34.566 1.00 169.23 ? 138 THR A C   1 
ATOM   1054 O O   . THR A 1 138 ? 4.347   -59.767 -35.648 1.00 175.62 ? 138 THR A O   1 
ATOM   1055 C CB  . THR A 1 138 ? 3.109   -59.149 -32.860 1.00 180.22 ? 138 THR A CB  1 
ATOM   1056 O OG1 . THR A 1 138 ? 3.676   -57.859 -32.660 1.00 169.86 ? 138 THR A OG1 1 
ATOM   1057 C CG2 . THR A 1 138 ? 2.338   -59.618 -31.635 1.00 175.37 ? 138 THR A CG2 1 
ATOM   1058 N N   . GLY A 1 139 ? 6.151   -59.137 -34.447 1.00 160.30 ? 139 GLY A N   1 
ATOM   1059 C CA  . GLY A 1 139 ? 6.897   -58.684 -35.610 1.00 163.84 ? 139 GLY A CA  1 
ATOM   1060 C C   . GLY A 1 139 ? 6.499   -57.268 -36.020 1.00 159.72 ? 139 GLY A C   1 
ATOM   1061 O O   . GLY A 1 139 ? 6.841   -56.803 -37.108 1.00 148.84 ? 139 GLY A O   1 
ATOM   1062 N N   . ALA A 1 140 ? 5.758   -56.595 -35.134 1.00 162.69 ? 140 ALA A N   1 
ATOM   1063 C CA  . ALA A 1 140 ? 5.495   -55.175 -35.291 1.00 155.28 ? 140 ALA A CA  1 
ATOM   1064 C C   . ALA A 1 140 ? 6.431   -54.404 -34.371 1.00 168.08 ? 140 ALA A C   1 
ATOM   1065 O O   . ALA A 1 140 ? 6.608   -54.760 -33.207 1.00 173.37 ? 140 ALA A O   1 
ATOM   1066 C CB  . ALA A 1 140 ? 4.050   -54.848 -35.002 1.00 141.76 ? 140 ALA A CB  1 
ATOM   1067 N N   . THR A 1 141 ? 7.040   -53.357 -34.936 1.00 173.56 ? 141 THR A N   1 
ATOM   1068 C CA  . THR A 1 141 ? 8.000   -52.511 -34.254 1.00 163.00 ? 141 THR A CA  1 
ATOM   1069 C C   . THR A 1 141 ? 7.240   -51.338 -33.644 1.00 145.53 ? 141 THR A C   1 
ATOM   1070 O O   . THR A 1 141 ? 6.781   -50.484 -34.398 1.00 136.46 ? 141 THR A O   1 
ATOM   1071 C CB  . THR A 1 141 ? 9.017   -52.044 -35.294 1.00 182.96 ? 141 THR A CB  1 
ATOM   1072 O OG1 . THR A 1 141 ? 9.726   -53.223 -35.674 1.00 199.37 ? 141 THR A OG1 1 
ATOM   1073 C CG2 . THR A 1 141 ? 9.973   -50.994 -34.755 1.00 207.21 ? 141 THR A CG2 1 
ATOM   1074 N N   . PRO A 1 142 ? 7.082   -51.278 -32.292 1.00 145.10 ? 142 PRO A N   1 
ATOM   1075 C CA  . PRO A 1 142 ? 6.407   -50.154 -31.631 1.00 162.23 ? 142 PRO A CA  1 
ATOM   1076 C C   . PRO A 1 142 ? 6.863   -48.786 -32.140 1.00 178.01 ? 142 PRO A C   1 
ATOM   1077 O O   . PRO A 1 142 ? 8.060   -48.527 -32.254 1.00 177.45 ? 142 PRO A O   1 
ATOM   1078 C CB  . PRO A 1 142 ? 6.671   -50.382 -30.122 1.00 142.60 ? 142 PRO A CB  1 
ATOM   1079 C CG  . PRO A 1 142 ? 6.871   -51.881 -30.009 1.00 128.35 ? 142 PRO A CG  1 
ATOM   1080 C CD  . PRO A 1 142 ? 7.525   -52.299 -31.322 1.00 131.38 ? 142 PRO A CD  1 
ATOM   1081 N N   . GLU A 1 143 ? 5.880   -47.936 -32.466 1.00 188.38 ? 143 GLU A N   1 
ATOM   1082 C CA  . GLU A 1 143 ? 6.061   -46.629 -33.079 1.00 173.99 ? 143 GLU A CA  1 
ATOM   1083 C C   . GLU A 1 143 ? 6.689   -45.702 -32.042 1.00 160.76 ? 143 GLU A C   1 
ATOM   1084 O O   . GLU A 1 143 ? 7.262   -44.663 -32.387 1.00 145.79 ? 143 GLU A O   1 
ATOM   1085 C CB  . GLU A 1 143 ? 4.642   -46.216 -33.480 1.00 160.84 ? 143 GLU A CB  1 
ATOM   1086 C CG  . GLU A 1 143 ? 4.523   -45.031 -34.428 1.00 177.32 ? 143 GLU A CG  1 
ATOM   1087 C CD  . GLU A 1 143 ? 3.056   -44.639 -34.507 1.00 182.41 ? 143 GLU A CD  1 
ATOM   1088 O OE1 . GLU A 1 143 ? 2.513   -44.226 -33.463 1.00 164.55 ? 143 GLU A OE1 1 
ATOM   1089 O OE2 . GLU A 1 143 ? 2.451   -44.718 -35.596 1.00 204.91 ? 143 GLU A OE2 1 
ATOM   1090 N N   . GLU A 1 144 ? 6.579   -46.127 -30.773 1.00 160.59 ? 144 GLU A N   1 
ATOM   1091 C CA  . GLU A 1 144 ? 6.989   -45.329 -29.634 1.00 181.49 ? 144 GLU A CA  1 
ATOM   1092 C C   . GLU A 1 144 ? 7.392   -46.275 -28.500 1.00 184.28 ? 144 GLU A C   1 
ATOM   1093 O O   . GLU A 1 144 ? 7.188   -45.981 -27.326 1.00 202.67 ? 144 GLU A O   1 
ATOM   1094 C CB  . GLU A 1 144 ? 5.853   -44.353 -29.300 1.00 179.73 ? 144 GLU A CB  1 
ATOM   1095 C CG  . GLU A 1 144 ? 6.284   -42.901 -29.122 1.00 179.88 ? 144 GLU A CG  1 
ATOM   1096 C CD  . GLU A 1 144 ? 7.498   -42.669 -28.240 1.00 231.82 ? 144 GLU A CD  1 
ATOM   1097 O OE1 . GLU A 1 144 ? 7.510   -43.107 -27.061 1.00 223.32 ? 144 GLU A OE1 1 
ATOM   1098 O OE2 . GLU A 1 144 ? 8.452   -42.048 -28.772 1.00 286.30 ? 144 GLU A OE2 1 
ATOM   1099 N N   . GLY A 1 145 ? 7.931   -47.443 -28.870 1.00 171.49 ? 145 GLY A N   1 
ATOM   1100 C CA  . GLY A 1 145 ? 8.600   -48.357 -27.961 1.00 182.07 ? 145 GLY A CA  1 
ATOM   1101 C C   . GLY A 1 145 ? 10.117  -48.183 -28.057 1.00 198.54 ? 145 GLY A C   1 
ATOM   1102 O O   . GLY A 1 145 ? 10.635  -47.621 -29.028 1.00 202.71 ? 145 GLY A O   1 
ATOM   1103 N N   . ASP A 1 146 ? 10.816  -48.690 -27.037 1.00 181.60 ? 146 ASP A N   1 
ATOM   1104 C CA  . ASP A 1 146 ? 12.255  -48.574 -26.880 1.00 176.16 ? 146 ASP A CA  1 
ATOM   1105 C C   . ASP A 1 146 ? 12.521  -48.450 -25.388 1.00 166.41 ? 146 ASP A C   1 
ATOM   1106 O O   . ASP A 1 146 ? 12.880  -47.371 -24.923 1.00 188.54 ? 146 ASP A O   1 
ATOM   1107 C CB  . ASP A 1 146 ? 12.801  -47.313 -27.539 1.00 210.47 ? 146 ASP A CB  1 
ATOM   1108 C CG  . ASP A 1 146 ? 14.254  -47.370 -27.988 1.00 253.67 ? 146 ASP A CG  1 
ATOM   1109 O OD1 . ASP A 1 146 ? 15.062  -48.007 -27.284 1.00 258.96 ? 146 ASP A OD1 1 
ATOM   1110 O OD2 . ASP A 1 146 ? 14.558  -46.777 -29.043 1.00 284.38 ? 146 ASP A OD2 1 
ATOM   1111 N N   . HIS A 1 147 ? 12.329  -49.546 -24.638 1.00 152.32 ? 147 HIS A N   1 
ATOM   1112 C CA  . HIS A 1 147 ? 11.982  -49.411 -23.228 1.00 166.42 ? 147 HIS A CA  1 
ATOM   1113 C C   . HIS A 1 147 ? 13.190  -48.884 -22.459 1.00 159.62 ? 147 HIS A C   1 
ATOM   1114 O O   . HIS A 1 147 ? 13.061  -47.972 -21.632 1.00 156.68 ? 147 HIS A O   1 
ATOM   1115 C CB  . HIS A 1 147 ? 11.560  -50.750 -22.609 1.00 193.21 ? 147 HIS A CB  1 
ATOM   1116 C CG  . HIS A 1 147 ? 11.411  -50.712 -21.119 1.00 197.97 ? 147 HIS A CG  1 
ATOM   1117 N ND1 . HIS A 1 147 ? 10.855  -49.643 -20.443 1.00 167.58 ? 147 HIS A ND1 1 
ATOM   1118 C CD2 . HIS A 1 147 ? 11.738  -51.619 -20.180 1.00 197.97 ? 147 HIS A CD2 1 
ATOM   1119 C CE1 . HIS A 1 147 ? 10.834  -49.906 -19.145 1.00 157.16 ? 147 HIS A CE1 1 
ATOM   1120 N NE2 . HIS A 1 147 ? 11.379  -51.091 -18.962 1.00 192.64 ? 147 HIS A NE2 1 
ATOM   1121 N N   . ALA A 1 148 ? 14.330  -49.539 -22.714 1.00 149.64 ? 148 ALA A N   1 
ATOM   1122 C CA  . ALA A 1 148 ? 15.559  -49.268 -21.981 1.00 138.89 ? 148 ALA A CA  1 
ATOM   1123 C C   . ALA A 1 148 ? 15.967  -47.810 -22.161 1.00 143.61 ? 148 ALA A C   1 
ATOM   1124 O O   . ALA A 1 148 ? 16.317  -47.121 -21.193 1.00 139.25 ? 148 ALA A O   1 
ATOM   1125 C CB  . ALA A 1 148 ? 16.643  -50.210 -22.439 1.00 146.29 ? 148 ALA A CB  1 
ATOM   1126 N N   . PHE A 1 149 ? 15.905  -47.371 -23.421 1.00 150.52 ? 149 PHE A N   1 
ATOM   1127 C CA  . PHE A 1 149 ? 16.261  -46.005 -23.810 1.00 140.53 ? 149 PHE A CA  1 
ATOM   1128 C C   . PHE A 1 149 ? 15.387  -45.013 -23.043 1.00 140.67 ? 149 PHE A C   1 
ATOM   1129 O O   . PHE A 1 149 ? 15.888  -44.018 -22.495 1.00 153.50 ? 149 PHE A O   1 
ATOM   1130 C CB  . PHE A 1 149 ? 16.124  -45.761 -25.329 1.00 134.39 ? 149 PHE A CB  1 
ATOM   1131 C CG  . PHE A 1 149 ? 16.690  -44.477 -25.940 1.00 143.53 ? 149 PHE A CG  1 
ATOM   1132 C CD1 . PHE A 1 149 ? 16.651  -43.255 -25.268 1.00 149.97 ? 149 PHE A CD1 1 
ATOM   1133 C CD2 . PHE A 1 149 ? 17.268  -44.492 -27.207 1.00 156.05 ? 149 PHE A CD2 1 
ATOM   1134 C CE1 . PHE A 1 149 ? 17.163  -42.096 -25.845 1.00 149.82 ? 149 PHE A CE1 1 
ATOM   1135 C CE2 . PHE A 1 149 ? 17.804  -43.341 -27.774 1.00 173.44 ? 149 PHE A CE2 1 
ATOM   1136 C CZ  . PHE A 1 149 ? 17.743  -42.141 -27.099 1.00 170.65 ? 149 PHE A CZ  1 
ATOM   1137 N N   . VAL A 1 150 ? 14.086  -45.316 -23.030 1.00 128.22 ? 150 VAL A N   1 
ATOM   1138 C CA  . VAL A 1 150 ? 13.095  -44.480 -22.367 1.00 127.25 ? 150 VAL A CA  1 
ATOM   1139 C C   . VAL A 1 150 ? 13.430  -44.348 -20.879 1.00 132.07 ? 150 VAL A C   1 
ATOM   1140 O O   . VAL A 1 150 ? 13.399  -43.248 -20.317 1.00 142.70 ? 150 VAL A O   1 
ATOM   1141 C CB  . VAL A 1 150 ? 11.666  -44.958 -22.679 1.00 136.72 ? 150 VAL A CB  1 
ATOM   1142 C CG1 . VAL A 1 150 ? 10.637  -44.363 -21.726 1.00 162.96 ? 150 VAL A CG1 1 
ATOM   1143 C CG2 . VAL A 1 150 ? 11.294  -44.639 -24.127 1.00 151.18 ? 150 VAL A CG2 1 
ATOM   1144 N N   . ALA A 1 151 ? 13.754  -45.491 -20.280 1.00 134.62 ? 151 ALA A N   1 
ATOM   1145 C CA  . ALA A 1 151 ? 14.108  -45.576 -18.866 1.00 136.42 ? 151 ALA A CA  1 
ATOM   1146 C C   . ALA A 1 151 ? 15.307  -44.680 -18.573 1.00 144.55 ? 151 ALA A C   1 
ATOM   1147 O O   . ALA A 1 151 ? 15.320  -43.930 -17.596 1.00 148.22 ? 151 ALA A O   1 
ATOM   1148 C CB  . ALA A 1 151 ? 14.387  -47.009 -18.484 1.00 149.74 ? 151 ALA A CB  1 
ATOM   1149 N N   . ARG A 1 152 ? 16.305  -44.793 -19.448 1.00 165.92 ? 152 ARG A N   1 
ATOM   1150 C CA  . ARG A 1 152 ? 17.542  -44.023 -19.341 1.00 171.77 ? 152 ARG A CA  1 
ATOM   1151 C C   . ARG A 1 152 ? 17.236  -42.522 -19.364 1.00 165.31 ? 152 ARG A C   1 
ATOM   1152 O O   . ARG A 1 152 ? 17.768  -41.771 -18.544 1.00 153.36 ? 152 ARG A O   1 
ATOM   1153 C CB  . ARG A 1 152 ? 18.651  -44.487 -20.294 1.00 191.23 ? 152 ARG A CB  1 
ATOM   1154 C CG  . ARG A 1 152 ? 19.982  -43.910 -19.836 1.00 185.11 ? 152 ARG A CG  1 
ATOM   1155 C CD  . ARG A 1 152 ? 21.255  -44.273 -20.556 1.00 182.73 ? 152 ARG A CD  1 
ATOM   1156 N NE  . ARG A 1 152 ? 22.171  -43.324 -19.914 1.00 205.80 ? 152 ARG A NE  1 
ATOM   1157 C CZ  . ARG A 1 152 ? 23.123  -43.614 -19.043 1.00 240.42 ? 152 ARG A CZ  1 
ATOM   1158 N NH1 . ARG A 1 152 ? 23.499  -44.867 -18.862 1.00 277.89 ? 152 ARG A NH1 1 
ATOM   1159 N NH2 . ARG A 1 152 ? 23.717  -42.639 -18.382 1.00 238.99 ? 152 ARG A NH2 1 
ATOM   1160 N N   . TRP A 1 153 ? 16.427  -42.064 -20.331 1.00 171.60 ? 153 TRP A N   1 
ATOM   1161 C CA  . TRP A 1 153 ? 16.505  -40.669 -20.756 1.00 165.56 ? 153 TRP A CA  1 
ATOM   1162 C C   . TRP A 1 153 ? 15.239  -39.853 -20.493 1.00 157.10 ? 153 TRP A C   1 
ATOM   1163 O O   . TRP A 1 153 ? 15.285  -38.627 -20.520 1.00 145.68 ? 153 TRP A O   1 
ATOM   1164 C CB  . TRP A 1 153 ? 16.962  -40.572 -22.217 1.00 170.44 ? 153 TRP A CB  1 
ATOM   1165 C CG  . TRP A 1 153 ? 18.446  -40.776 -22.358 1.00 198.88 ? 153 TRP A CG  1 
ATOM   1166 C CD1 . TRP A 1 153 ? 19.110  -41.780 -23.002 1.00 191.56 ? 153 TRP A CD1 1 
ATOM   1167 C CD2 . TRP A 1 153 ? 19.462  -39.943 -21.760 1.00 209.23 ? 153 TRP A CD2 1 
ATOM   1168 N NE1 . TRP A 1 153 ? 20.467  -41.609 -22.881 1.00 175.19 ? 153 TRP A NE1 1 
ATOM   1169 C CE2 . TRP A 1 153 ? 20.708  -40.496 -22.120 1.00 172.52 ? 153 TRP A CE2 1 
ATOM   1170 C CE3 . TRP A 1 153 ? 19.432  -38.786 -20.968 1.00 222.85 ? 153 TRP A CE3 1 
ATOM   1171 C CZ2 . TRP A 1 153 ? 21.904  -39.929 -21.702 1.00 160.16 ? 153 TRP A CZ2 1 
ATOM   1172 C CZ3 . TRP A 1 153 ? 20.619  -38.231 -20.546 1.00 204.97 ? 153 TRP A CZ3 1 
ATOM   1173 C CH2 . TRP A 1 153 ? 21.835  -38.812 -20.900 1.00 183.98 ? 153 TRP A CH2 1 
ATOM   1174 N N   . GLY A 1 154 ? 14.122  -40.539 -20.245 1.00 154.21 ? 154 GLY A N   1 
ATOM   1175 C CA  . GLY A 1 154 ? 12.859  -39.891 -19.945 1.00 160.92 ? 154 GLY A CA  1 
ATOM   1176 C C   . GLY A 1 154 ? 12.759  -39.585 -18.454 1.00 170.60 ? 154 GLY A C   1 
ATOM   1177 O O   . GLY A 1 154 ? 11.818  -38.910 -18.036 1.00 197.78 ? 154 GLY A O   1 
ATOM   1178 N N   . SER A 1 155 ? 13.729  -40.099 -17.675 1.00 151.71 ? 155 SER A N   1 
ATOM   1179 C CA  . SER A 1 155 ? 13.827  -39.872 -16.239 1.00 164.51 ? 155 SER A CA  1 
ATOM   1180 C C   . SER A 1 155 ? 14.019  -38.383 -15.977 1.00 169.98 ? 155 SER A C   1 
ATOM   1181 O O   . SER A 1 155 ? 14.335  -37.640 -16.908 1.00 160.04 ? 155 SER A O   1 
ATOM   1182 C CB  . SER A 1 155 ? 14.943  -40.671 -15.613 1.00 174.49 ? 155 SER A CB  1 
ATOM   1183 O OG  . SER A 1 155 ? 16.152  -39.930 -15.577 1.00 183.08 ? 155 SER A OG  1 
ATOM   1184 N N   . LYS A 1 156 ? 13.841  -37.957 -14.714 1.00 164.87 ? 156 LYS A N   1 
ATOM   1185 C CA  . LYS A 1 156 ? 13.854  -36.528 -14.436 1.00 164.65 ? 156 LYS A CA  1 
ATOM   1186 C C   . LYS A 1 156 ? 15.244  -36.002 -14.806 1.00 168.73 ? 156 LYS A C   1 
ATOM   1187 O O   . LYS A 1 156 ? 15.382  -35.020 -15.545 1.00 182.89 ? 156 LYS A O   1 
ATOM   1188 C CB  . LYS A 1 156 ? 13.503  -36.190 -12.976 1.00 153.32 ? 156 LYS A CB  1 
ATOM   1189 C CG  . LYS A 1 156 ? 12.176  -36.680 -12.383 1.00 149.29 ? 156 LYS A CG  1 
ATOM   1190 C CD  . LYS A 1 156 ? 10.887  -36.192 -13.041 1.00 132.64 ? 156 LYS A CD  1 
ATOM   1191 C CE  . LYS A 1 156 ? 9.698   -36.775 -12.347 1.00 140.34 ? 156 LYS A CE  1 
ATOM   1192 N NZ  . LYS A 1 156 ? 8.563   -36.938 -13.252 1.00 153.20 ? 156 LYS A NZ  1 
ATOM   1193 N N   . SER A 1 157 ? 16.243  -36.659 -14.206 1.00 168.81 ? 157 SER A N   1 
ATOM   1194 C CA  . SER A 1 157 ? 17.634  -36.241 -14.313 1.00 163.08 ? 157 SER A CA  1 
ATOM   1195 C C   . SER A 1 157 ? 18.069  -36.227 -15.775 1.00 150.74 ? 157 SER A C   1 
ATOM   1196 O O   . SER A 1 157 ? 18.690  -35.264 -16.246 1.00 152.43 ? 157 SER A O   1 
ATOM   1197 C CB  . SER A 1 157 ? 18.540  -37.128 -13.492 1.00 171.20 ? 157 SER A CB  1 
ATOM   1198 O OG  . SER A 1 157 ? 18.488  -38.475 -13.936 1.00 185.89 ? 157 SER A OG  1 
ATOM   1199 N N   . GLY A 1 158 ? 17.725  -37.321 -16.458 1.00 142.18 ? 158 GLY A N   1 
ATOM   1200 C CA  . GLY A 1 158 ? 18.063  -37.509 -17.866 1.00 143.91 ? 158 GLY A CA  1 
ATOM   1201 C C   . GLY A 1 158 ? 17.479  -36.372 -18.703 1.00 145.40 ? 158 GLY A C   1 
ATOM   1202 O O   . GLY A 1 158 ? 18.167  -35.780 -19.557 1.00 151.08 ? 158 GLY A O   1 
ATOM   1203 N N   . GLY A 1 159 ? 16.199  -36.094 -18.418 1.00 154.50 ? 159 GLY A N   1 
ATOM   1204 C CA  . GLY A 1 159 ? 15.459  -35.046 -19.111 1.00 177.23 ? 159 GLY A CA  1 
ATOM   1205 C C   . GLY A 1 159 ? 16.155  -33.702 -18.942 1.00 184.45 ? 159 GLY A C   1 
ATOM   1206 O O   . GLY A 1 159 ? 16.338  -32.951 -19.910 1.00 185.88 ? 159 GLY A O   1 
ATOM   1207 N N   . LYS A 1 160 ? 16.535  -33.437 -17.693 1.00 191.95 ? 160 LYS A N   1 
ATOM   1208 C CA  . LYS A 1 160 ? 17.208  -32.197 -17.312 1.00 180.94 ? 160 LYS A CA  1 
ATOM   1209 C C   . LYS A 1 160 ? 18.502  -32.049 -18.106 1.00 174.58 ? 160 LYS A C   1 
ATOM   1210 O O   . LYS A 1 160 ? 18.788  -30.975 -18.644 1.00 150.95 ? 160 LYS A O   1 
ATOM   1211 C CB  . LYS A 1 160 ? 17.311  -32.108 -15.781 1.00 182.77 ? 160 LYS A CB  1 
ATOM   1212 C CG  . LYS A 1 160 ? 18.011  -30.861 -15.260 1.00 178.35 ? 160 LYS A CG  1 
ATOM   1213 C CD  . LYS A 1 160 ? 17.730  -30.489 -13.812 1.00 150.43 ? 160 LYS A CD  1 
ATOM   1214 C CE  . LYS A 1 160 ? 18.174  -29.086 -13.574 1.00 143.91 ? 160 LYS A CE  1 
ATOM   1215 N NZ  . LYS A 1 160 ? 17.410  -28.454 -12.500 1.00 157.32 ? 160 LYS A NZ  1 
ATOM   1216 N N   . GLU A 1 161 ? 19.255  -33.148 -18.162 1.00 178.70 ? 161 GLU A N   1 
ATOM   1217 C CA  . GLU A 1 161 ? 20.532  -33.202 -18.862 1.00 181.07 ? 161 GLU A CA  1 
ATOM   1218 C C   . GLU A 1 161 ? 20.336  -32.837 -20.335 1.00 162.58 ? 161 GLU A C   1 
ATOM   1219 O O   . GLU A 1 161 ? 21.091  -32.011 -20.903 1.00 172.88 ? 161 GLU A O   1 
ATOM   1220 C CB  . GLU A 1 161 ? 21.200  -34.574 -18.728 1.00 207.26 ? 161 GLU A CB  1 
ATOM   1221 C CG  . GLU A 1 161 ? 21.533  -34.928 -17.281 1.00 232.77 ? 161 GLU A CG  1 
ATOM   1222 C CD  . GLU A 1 161 ? 22.681  -35.891 -17.055 1.00 256.44 ? 161 GLU A CD  1 
ATOM   1223 O OE1 . GLU A 1 161 ? 23.293  -36.349 -18.049 1.00 241.26 ? 161 GLU A OE1 1 
ATOM   1224 O OE2 . GLU A 1 161 ? 22.973  -36.151 -15.869 1.00 292.80 ? 161 GLU A OE2 1 
ATOM   1225 N N   . ILE A 1 162 ? 19.302  -33.468 -20.914 1.00 147.39 ? 162 ILE A N   1 
ATOM   1226 C CA  . ILE A 1 162 ? 18.980  -33.264 -22.323 1.00 147.43 ? 162 ILE A CA  1 
ATOM   1227 C C   . ILE A 1 162 ? 18.663  -31.788 -22.578 1.00 161.11 ? 162 ILE A C   1 
ATOM   1228 O O   . ILE A 1 162 ? 19.144  -31.202 -23.557 1.00 150.96 ? 162 ILE A O   1 
ATOM   1229 C CB  . ILE A 1 162 ? 17.934  -34.240 -22.894 1.00 147.37 ? 162 ILE A CB  1 
ATOM   1230 C CG1 . ILE A 1 162 ? 18.382  -35.687 -22.734 1.00 152.39 ? 162 ILE A CG1 1 
ATOM   1231 C CG2 . ILE A 1 162 ? 17.635  -33.924 -24.362 1.00 132.88 ? 162 ILE A CG2 1 
ATOM   1232 C CD1 . ILE A 1 162 ? 17.234  -36.685 -22.777 1.00 160.12 ? 162 ILE A CD1 1 
ATOM   1233 N N   . CYS A 1 163 ? 17.868  -31.218 -21.674 1.00 180.09 ? 163 CYS A N   1 
ATOM   1234 C CA  . CYS A 1 163 ? 17.453  -29.822 -21.739 1.00 168.72 ? 163 CYS A CA  1 
ATOM   1235 C C   . CYS A 1 163 ? 18.673  -28.917 -21.739 1.00 182.15 ? 163 CYS A C   1 
ATOM   1236 O O   . CYS A 1 163 ? 18.767  -27.983 -22.540 1.00 232.78 ? 163 CYS A O   1 
ATOM   1237 C CB  . CYS A 1 163 ? 16.670  -29.408 -20.496 1.00 163.03 ? 163 CYS A CB  1 
ATOM   1238 S SG  . CYS A 1 163 ? 15.057  -30.207 -20.306 1.00 169.74 ? 163 CYS A SG  1 
ATOM   1239 N N   . LEU A 1 164 ? 19.591  -29.221 -20.818 1.00 167.04 ? 164 LEU A N   1 
ATOM   1240 C CA  . LEU A 1 164 ? 20.831  -28.466 -20.643 1.00 160.73 ? 164 LEU A CA  1 
ATOM   1241 C C   . LEU A 1 164 ? 21.622  -28.472 -21.954 1.00 150.05 ? 164 LEU A C   1 
ATOM   1242 O O   . LEU A 1 164 ? 22.106  -27.415 -22.420 1.00 125.57 ? 164 LEU A O   1 
ATOM   1243 C CB  . LEU A 1 164 ? 21.670  -29.007 -19.478 1.00 155.58 ? 164 LEU A CB  1 
ATOM   1244 C CG  . LEU A 1 164 ? 21.197  -28.690 -18.050 1.00 149.64 ? 164 LEU A CG  1 
ATOM   1245 C CD1 . LEU A 1 164 ? 21.838  -29.584 -17.001 1.00 137.39 ? 164 LEU A CD1 1 
ATOM   1246 C CD2 . LEU A 1 164 ? 21.448  -27.248 -17.665 1.00 146.02 ? 164 LEU A CD2 1 
ATOM   1247 N N   . ARG A 1 165 ? 21.724  -29.679 -22.524 1.00 160.55 ? 165 ARG A N   1 
ATOM   1248 C CA  . ARG A 1 165 ? 22.467  -29.874 -23.762 1.00 169.07 ? 165 ARG A CA  1 
ATOM   1249 C C   . ARG A 1 165 ? 21.860  -29.036 -24.885 1.00 183.39 ? 165 ARG A C   1 
ATOM   1250 O O   . ARG A 1 165 ? 22.585  -28.390 -25.641 1.00 186.41 ? 165 ARG A O   1 
ATOM   1251 C CB  . ARG A 1 165 ? 23.111  -31.244 -23.912 1.00 174.21 ? 165 ARG A CB  1 
ATOM   1252 C CG  . ARG A 1 165 ? 24.376  -31.117 -23.069 1.00 180.98 ? 165 ARG A CG  1 
ATOM   1253 C CD  . ARG A 1 165 ? 24.926  -32.399 -22.493 1.00 223.77 ? 165 ARG A CD  1 
ATOM   1254 N NE  . ARG A 1 165 ? 24.360  -32.860 -21.219 1.00 230.95 ? 165 ARG A NE  1 
ATOM   1255 C CZ  . ARG A 1 165 ? 24.680  -34.035 -20.671 1.00 244.08 ? 165 ARG A CZ  1 
ATOM   1256 N NH1 . ARG A 1 165 ? 25.367  -34.944 -21.352 1.00 271.17 ? 165 ARG A NH1 1 
ATOM   1257 N NH2 . ARG A 1 165 ? 24.297  -34.315 -19.442 1.00 224.33 ? 165 ARG A NH2 1 
ATOM   1258 N N   . ALA A 1 166 ? 20.530  -29.053 -24.952 1.00 195.04 ? 166 ALA A N   1 
ATOM   1259 C CA  . ALA A 1 166 ? 19.776  -28.337 -25.964 1.00 178.91 ? 166 ALA A CA  1 
ATOM   1260 C C   . ALA A 1 166 ? 20.015  -26.837 -25.821 1.00 168.34 ? 166 ALA A C   1 
ATOM   1261 O O   . ALA A 1 166 ? 19.712  -26.105 -26.760 1.00 148.15 ? 166 ALA A O   1 
ATOM   1262 C CB  . ALA A 1 166 ? 18.304  -28.714 -25.909 1.00 172.66 ? 166 ALA A CB  1 
ATOM   1263 N N   . GLY A 1 167 ? 20.363  -26.371 -24.610 1.00 153.62 ? 167 GLY A N   1 
ATOM   1264 C CA  . GLY A 1 167 ? 20.353  -24.953 -24.291 1.00 144.07 ? 167 GLY A CA  1 
ATOM   1265 C C   . GLY A 1 167 ? 18.931  -24.445 -24.052 1.00 144.09 ? 167 GLY A C   1 
ATOM   1266 O O   . GLY A 1 167 ? 18.613  -23.292 -24.322 1.00 153.54 ? 167 GLY A O   1 
ATOM   1267 N N   . VAL A 1 168 ? 18.072  -25.321 -23.537 1.00 136.06 ? 168 VAL A N   1 
ATOM   1268 C CA  . VAL A 1 168 ? 16.755  -24.905 -23.089 1.00 129.33 ? 168 VAL A CA  1 
ATOM   1269 C C   . VAL A 1 168 ? 16.825  -24.613 -21.586 1.00 133.63 ? 168 VAL A C   1 
ATOM   1270 O O   . VAL A 1 168 ? 17.389  -25.382 -20.802 1.00 143.50 ? 168 VAL A O   1 
ATOM   1271 C CB  . VAL A 1 168 ? 15.624  -25.885 -23.479 1.00 126.86 ? 168 VAL A CB  1 
ATOM   1272 C CG1 . VAL A 1 168 ? 15.689  -26.272 -24.950 1.00 114.38 ? 168 VAL A CG1 1 
ATOM   1273 C CG2 . VAL A 1 168 ? 15.580  -27.147 -22.626 1.00 130.38 ? 168 VAL A CG2 1 
ATOM   1274 N N   . ALA A 1 169 ? 16.281  -23.458 -21.202 1.00 130.29 ? 169 ALA A N   1 
ATOM   1275 C CA  . ALA A 1 169 ? 16.329  -23.001 -19.821 1.00 141.22 ? 169 ALA A CA  1 
ATOM   1276 C C   . ALA A 1 169 ? 15.692  -24.028 -18.887 1.00 136.09 ? 169 ALA A C   1 
ATOM   1277 O O   . ALA A 1 169 ? 14.551  -24.436 -19.097 1.00 179.48 ? 169 ALA A O   1 
ATOM   1278 C CB  . ALA A 1 169 ? 15.607  -21.676 -19.719 1.00 168.70 ? 169 ALA A CB  1 
ATOM   1279 N N   . VAL A 1 170 ? 16.427  -24.431 -17.846 1.00 122.65 ? 170 VAL A N   1 
ATOM   1280 C CA  . VAL A 1 170 ? 15.875  -25.319 -16.828 1.00 122.56 ? 170 VAL A CA  1 
ATOM   1281 C C   . VAL A 1 170 ? 15.773  -24.542 -15.518 1.00 116.24 ? 170 VAL A C   1 
ATOM   1282 O O   . VAL A 1 170 ? 16.335  -23.465 -15.415 1.00 114.74 ? 170 VAL A O   1 
ATOM   1283 C CB  . VAL A 1 170 ? 16.651  -26.647 -16.666 1.00 133.01 ? 170 VAL A CB  1 
ATOM   1284 C CG1 . VAL A 1 170 ? 16.762  -27.388 -17.994 1.00 128.64 ? 170 VAL A CG1 1 
ATOM   1285 C CG2 . VAL A 1 170 ? 18.030  -26.450 -16.042 1.00 142.82 ? 170 VAL A CG2 1 
ATOM   1286 N N   . PRO A 1 171 ? 15.046  -25.031 -14.487 1.00 128.60 ? 171 PRO A N   1 
ATOM   1287 C CA  . PRO A 1 171 ? 15.110  -24.424 -13.156 1.00 132.18 ? 171 PRO A CA  1 
ATOM   1288 C C   . PRO A 1 171 ? 16.466  -24.776 -12.560 1.00 135.21 ? 171 PRO A C   1 
ATOM   1289 O O   . PRO A 1 171 ? 17.038  -25.822 -12.876 1.00 136.77 ? 171 PRO A O   1 
ATOM   1290 C CB  . PRO A 1 171 ? 13.974  -25.094 -12.371 1.00 147.98 ? 171 PRO A CB  1 
ATOM   1291 C CG  . PRO A 1 171 ? 13.151  -25.791 -13.436 1.00 159.47 ? 171 PRO A CG  1 
ATOM   1292 C CD  . PRO A 1 171 ? 14.125  -26.180 -14.541 1.00 138.70 ? 171 PRO A CD  1 
ATOM   1293 N N   . GLY A 1 172 ? 16.975  -23.886 -11.711 1.00 139.91 ? 172 GLY A N   1 
ATOM   1294 C CA  . GLY A 1 172 ? 18.240  -24.130 -11.039 1.00 153.32 ? 172 GLY A CA  1 
ATOM   1295 C C   . GLY A 1 172 ? 18.231  -25.486 -10.336 1.00 144.85 ? 172 GLY A C   1 
ATOM   1296 O O   . GLY A 1 172 ? 17.356  -25.752 -9.516  1.00 134.51 ? 172 GLY A O   1 
ATOM   1297 N N   . GLY A 1 173 ? 19.188  -26.343 -10.712 1.00 139.57 ? 173 GLY A N   1 
ATOM   1298 C CA  . GLY A 1 173 ? 19.367  -27.635 -10.071 1.00 150.77 ? 173 GLY A CA  1 
ATOM   1299 C C   . GLY A 1 173 ? 20.415  -28.500 -10.770 1.00 162.21 ? 173 GLY A C   1 
ATOM   1300 O O   . GLY A 1 173 ? 20.867  -28.197 -11.878 1.00 162.89 ? 173 GLY A O   1 
ATOM   1301 N N   . THR A 1 174 ? 20.820  -29.587 -10.099 1.00 168.37 ? 174 THR A N   1 
ATOM   1302 C CA  . THR A 1 174 ? 21.726  -30.536 -10.727 1.00 165.81 ? 174 THR A CA  1 
ATOM   1303 C C   . THR A 1 174 ? 20.887  -31.561 -11.462 1.00 180.70 ? 174 THR A C   1 
ATOM   1304 O O   . THR A 1 174 ? 19.668  -31.649 -11.281 1.00 184.05 ? 174 THR A O   1 
ATOM   1305 C CB  . THR A 1 174 ? 22.579  -31.311 -9.730  1.00 167.15 ? 174 THR A CB  1 
ATOM   1306 O OG1 . THR A 1 174 ? 22.552  -30.576 -8.516  1.00 180.55 ? 174 THR A OG1 1 
ATOM   1307 C CG2 . THR A 1 174 ? 23.953  -31.649 -10.285 1.00 155.41 ? 174 THR A CG2 1 
ATOM   1308 N N   . SER A 1 175 ? 21.604  -32.365 -12.245 1.00 161.43 ? 175 SER A N   1 
ATOM   1309 C CA  . SER A 1 175 ? 21.029  -33.488 -12.953 1.00 152.33 ? 175 SER A CA  1 
ATOM   1310 C C   . SER A 1 175 ? 21.622  -34.783 -12.408 1.00 151.56 ? 175 SER A C   1 
ATOM   1311 O O   . SER A 1 175 ? 22.008  -35.654 -13.191 1.00 153.50 ? 175 SER A O   1 
ATOM   1312 C CB  . SER A 1 175 ? 21.241  -33.321 -14.436 1.00 143.95 ? 175 SER A CB  1 
ATOM   1313 O OG  . SER A 1 175 ? 22.580  -32.952 -14.736 1.00 165.39 ? 175 SER A OG  1 
ATOM   1314 N N   . GLU A 1 176 ? 21.674  -34.877 -11.071 1.00 156.32 ? 176 GLU A N   1 
ATOM   1315 C CA  . GLU A 1 176 ? 22.384  -35.944 -10.385 1.00 187.82 ? 176 GLU A CA  1 
ATOM   1316 C C   . GLU A 1 176 ? 21.473  -36.625 -9.361  1.00 180.49 ? 176 GLU A C   1 
ATOM   1317 O O   . GLU A 1 176 ? 20.842  -35.966 -8.543  1.00 182.98 ? 176 GLU A O   1 
ATOM   1318 C CB  . GLU A 1 176 ? 23.616  -35.352 -9.696  1.00 213.32 ? 176 GLU A CB  1 
ATOM   1319 C CG  . GLU A 1 176 ? 24.560  -36.381 -9.071  1.00 239.88 ? 176 GLU A CG  1 
ATOM   1320 C CD  . GLU A 1 176 ? 25.275  -37.285 -10.060 1.00 276.57 ? 176 GLU A CD  1 
ATOM   1321 O OE1 . GLU A 1 176 ? 26.010  -36.732 -10.906 1.00 292.89 ? 176 GLU A OE1 1 
ATOM   1322 O OE2 . GLU A 1 176 ? 25.124  -38.527 -9.988  1.00 300.39 ? 176 GLU A OE2 1 
ATOM   1323 N N   . VAL A 1 177 ? 21.425  -37.955 -9.464  1.00 165.31 ? 177 VAL A N   1 
ATOM   1324 C CA  . VAL A 1 177 ? 20.670  -38.806 -8.561  1.00 168.50 ? 177 VAL A CA  1 
ATOM   1325 C C   . VAL A 1 177 ? 21.198  -38.700 -7.134  1.00 165.97 ? 177 VAL A C   1 
ATOM   1326 O O   . VAL A 1 177 ? 22.405  -38.588 -6.901  1.00 210.03 ? 177 VAL A O   1 
ATOM   1327 C CB  . VAL A 1 177 ? 20.735  -40.270 -9.023  1.00 177.89 ? 177 VAL A CB  1 
ATOM   1328 C CG1 . VAL A 1 177 ? 19.485  -41.030 -8.569  1.00 200.95 ? 177 VAL A CG1 1 
ATOM   1329 C CG2 . VAL A 1 177 ? 20.969  -40.387 -10.530 1.00 172.35 ? 177 VAL A CG2 1 
ATOM   1330 N N   . LEU A 1 178 ? 20.261  -38.802 -6.190  1.00 155.11 ? 178 LEU A N   1 
ATOM   1331 C CA  . LEU A 1 178 ? 20.536  -38.664 -4.763  1.00 158.54 ? 178 LEU A CA  1 
ATOM   1332 C C   . LEU A 1 178 ? 20.013  -39.879 -3.986  1.00 173.64 ? 178 LEU A C   1 
ATOM   1333 O O   . LEU A 1 178 ? 18.911  -39.839 -3.435  1.00 196.48 ? 178 LEU A O   1 
ATOM   1334 C CB  . LEU A 1 178 ? 19.932  -37.381 -4.194  1.00 165.98 ? 178 LEU A CB  1 
ATOM   1335 C CG  . LEU A 1 178 ? 20.284  -36.073 -4.903  1.00 190.03 ? 178 LEU A CG  1 
ATOM   1336 C CD1 . LEU A 1 178 ? 19.207  -35.050 -4.605  1.00 202.51 ? 178 LEU A CD1 1 
ATOM   1337 C CD2 . LEU A 1 178 ? 21.639  -35.568 -4.461  1.00 187.31 ? 178 LEU A CD2 1 
ATOM   1338 N N   . ARG A 1 179 ? 20.850  -40.922 -3.949  1.00 166.83 ? 179 ARG A N   1 
ATOM   1339 C CA  . ARG A 1 179 ? 20.454  -42.221 -3.435  1.00 175.59 ? 179 ARG A CA  1 
ATOM   1340 C C   . ARG A 1 179 ? 20.268  -42.189 -1.916  1.00 183.18 ? 179 ARG A C   1 
ATOM   1341 O O   . ARG A 1 179 ? 19.896  -43.201 -1.354  1.00 190.88 ? 179 ARG A O   1 
ATOM   1342 C CB  . ARG A 1 179 ? 21.309  -43.334 -4.050  1.00 164.84 ? 179 ARG A CB  1 
ATOM   1343 C CG  . ARG A 1 179 ? 20.975  -43.454 -5.531  1.00 177.70 ? 179 ARG A CG  1 
ATOM   1344 C CD  . ARG A 1 179 ? 21.511  -44.703 -6.213  1.00 202.63 ? 179 ARG A CD  1 
ATOM   1345 N NE  . ARG A 1 179 ? 21.449  -44.618 -7.678  1.00 213.79 ? 179 ARG A NE  1 
ATOM   1346 C CZ  . ARG A 1 179 ? 22.142  -43.789 -8.466  1.00 220.78 ? 179 ARG A CZ  1 
ATOM   1347 N NH1 . ARG A 1 179 ? 22.953  -42.883 -7.948  1.00 235.41 ? 179 ARG A NH1 1 
ATOM   1348 N NH2 . ARG A 1 179 ? 22.015  -43.856 -9.782  1.00 211.42 ? 179 ARG A NH2 1 
ATOM   1349 N N   . SER A 1 180 ? 20.456  -41.036 -1.254  1.00 175.95 ? 180 SER A N   1 
ATOM   1350 C CA  . SER A 1 180 ? 20.261  -40.966 0.189   1.00 177.79 ? 180 SER A CA  1 
ATOM   1351 C C   . SER A 1 180 ? 19.659  -39.629 0.601   1.00 194.82 ? 180 SER A C   1 
ATOM   1352 O O   . SER A 1 180 ? 19.808  -38.632 -0.103  1.00 215.35 ? 180 SER A O   1 
ATOM   1353 C CB  . SER A 1 180 ? 21.545  -41.216 0.947   1.00 194.80 ? 180 SER A CB  1 
ATOM   1354 O OG  . SER A 1 180 ? 22.394  -40.074 0.950   1.00 190.80 ? 180 SER A OG  1 
ATOM   1355 N N   . GLU A 1 181 ? 19.063  -39.623 1.797   1.00 203.17 ? 181 GLU A N   1 
ATOM   1356 C CA  . GLU A 1 181 ? 18.445  -38.433 2.359   1.00 211.73 ? 181 GLU A CA  1 
ATOM   1357 C C   . GLU A 1 181 ? 19.486  -37.344 2.573   1.00 222.50 ? 181 GLU A C   1 
ATOM   1358 O O   . GLU A 1 181 ? 19.184  -36.177 2.316   1.00 195.54 ? 181 GLU A O   1 
ATOM   1359 C CB  . GLU A 1 181 ? 17.697  -38.695 3.665   1.00 201.74 ? 181 GLU A CB  1 
ATOM   1360 C CG  . GLU A 1 181 ? 16.720  -39.865 3.571   1.00 215.71 ? 181 GLU A CG  1 
ATOM   1361 C CD  . GLU A 1 181 ? 15.752  -39.953 4.731   1.00 224.82 ? 181 GLU A CD  1 
ATOM   1362 O OE1 . GLU A 1 181 ? 16.193  -40.028 5.899   1.00 235.58 ? 181 GLU A OE1 1 
ATOM   1363 O OE2 . GLU A 1 181 ? 14.542  -39.933 4.443   1.00 207.44 ? 181 GLU A OE2 1 
ATOM   1364 N N   . ALA A 1 182 ? 20.674  -37.739 3.044   1.00 212.66 ? 182 ALA A N   1 
ATOM   1365 C CA  . ALA A 1 182 ? 21.755  -36.809 3.316   1.00 175.24 ? 182 ALA A CA  1 
ATOM   1366 C C   . ALA A 1 182 ? 22.123  -36.036 2.045   1.00 187.04 ? 182 ALA A C   1 
ATOM   1367 O O   . ALA A 1 182 ? 22.277  -34.803 2.066   1.00 231.22 ? 182 ALA A O   1 
ATOM   1368 C CB  . ALA A 1 182 ? 22.923  -37.568 3.897   1.00 156.45 ? 182 ALA A CB  1 
ATOM   1369 N N   . GLU A 1 183 ? 22.245  -36.802 0.956   1.00 172.06 ? 183 GLU A N   1 
ATOM   1370 C CA  . GLU A 1 183 ? 22.596  -36.251 -0.350  1.00 192.72 ? 183 GLU A CA  1 
ATOM   1371 C C   . GLU A 1 183 ? 21.563  -35.210 -0.775  1.00 215.40 ? 183 GLU A C   1 
ATOM   1372 O O   . GLU A 1 183 ? 21.912  -34.115 -1.240  1.00 223.35 ? 183 GLU A O   1 
ATOM   1373 C CB  . GLU A 1 183 ? 22.725  -37.347 -1.404  1.00 199.81 ? 183 GLU A CB  1 
ATOM   1374 C CG  . GLU A 1 183 ? 23.900  -38.290 -1.166  1.00 223.38 ? 183 GLU A CG  1 
ATOM   1375 C CD  . GLU A 1 183 ? 23.925  -39.500 -2.086  1.00 237.24 ? 183 GLU A CD  1 
ATOM   1376 O OE1 . GLU A 1 183 ? 22.889  -40.199 -2.128  1.00 259.42 ? 183 GLU A OE1 1 
ATOM   1377 O OE2 . GLU A 1 183 ? 24.959  -39.752 -2.753  1.00 222.74 ? 183 GLU A OE2 1 
ATOM   1378 N N   . VAL A 1 184 ? 20.296  -35.584 -0.597  1.00 210.29 ? 184 VAL A N   1 
ATOM   1379 C CA  . VAL A 1 184 ? 19.158  -34.737 -0.940  1.00 195.24 ? 184 VAL A CA  1 
ATOM   1380 C C   . VAL A 1 184 ? 19.243  -33.420 -0.172  1.00 206.74 ? 184 VAL A C   1 
ATOM   1381 O O   . VAL A 1 184 ? 19.059  -32.341 -0.742  1.00 217.28 ? 184 VAL A O   1 
ATOM   1382 C CB  . VAL A 1 184 ? 17.810  -35.427 -0.667  1.00 189.02 ? 184 VAL A CB  1 
ATOM   1383 C CG1 . VAL A 1 184 ? 16.627  -34.480 -0.872  1.00 172.06 ? 184 VAL A CG1 1 
ATOM   1384 C CG2 . VAL A 1 184 ? 17.661  -36.705 -1.480  1.00 194.59 ? 184 VAL A CG2 1 
ATOM   1385 N N   . VAL A 1 185 ? 19.521  -33.547 1.122   1.00 202.41 ? 185 VAL A N   1 
ATOM   1386 C CA  . VAL A 1 185 ? 19.628  -32.405 2.024   1.00 199.20 ? 185 VAL A CA  1 
ATOM   1387 C C   . VAL A 1 185 ? 20.730  -31.463 1.537   1.00 209.38 ? 185 VAL A C   1 
ATOM   1388 O O   . VAL A 1 185 ? 20.538  -30.247 1.491   1.00 199.12 ? 185 VAL A O   1 
ATOM   1389 C CB  . VAL A 1 185 ? 19.698  -32.762 3.523   1.00 190.97 ? 185 VAL A CB  1 
ATOM   1390 C CG1 . VAL A 1 185 ? 20.068  -31.574 4.401   1.00 203.61 ? 185 VAL A CG1 1 
ATOM   1391 C CG2 . VAL A 1 185 ? 18.395  -33.378 3.995   1.00 184.28 ? 185 VAL A CG2 1 
ATOM   1392 N N   . GLU A 1 186 ? 21.865  -32.064 1.172   1.00 229.20 ? 186 GLU A N   1 
ATOM   1393 C CA  . GLU A 1 186 ? 23.022  -31.328 0.679   1.00 236.14 ? 186 GLU A CA  1 
ATOM   1394 C C   . GLU A 1 186 ? 22.638  -30.526 -0.570  1.00 221.85 ? 186 GLU A C   1 
ATOM   1395 O O   . GLU A 1 186 ? 22.971  -29.340 -0.696  1.00 220.08 ? 186 GLU A O   1 
ATOM   1396 C CB  . GLU A 1 186 ? 24.333  -32.126 0.692   1.00 253.60 ? 186 GLU A CB  1 
ATOM   1397 C CG  . GLU A 1 186 ? 24.570  -33.017 -0.522  1.00 262.32 ? 186 GLU A CG  1 
ATOM   1398 C CD  . GLU A 1 186 ? 25.126  -32.284 -1.715  1.00 278.54 ? 186 GLU A CD  1 
ATOM   1399 O OE1 . GLU A 1 186 ? 26.236  -31.719 -1.538  1.00 295.16 ? 186 GLU A OE1 1 
ATOM   1400 O OE2 . GLU A 1 186 ? 24.474  -32.247 -2.786  1.00 257.75 ? 186 GLU A OE2 1 
ATOM   1401 N N   . ALA A 1 187 ? 21.930  -31.210 -1.467  1.00 198.29 ? 187 ALA A N   1 
ATOM   1402 C CA  . ALA A 1 187 ? 21.466  -30.625 -2.719  1.00 194.07 ? 187 ALA A CA  1 
ATOM   1403 C C   . ALA A 1 187 ? 20.586  -29.401 -2.437  1.00 204.97 ? 187 ALA A C   1 
ATOM   1404 O O   . ALA A 1 187 ? 20.732  -28.340 -3.044  1.00 190.35 ? 187 ALA A O   1 
ATOM   1405 C CB  . ALA A 1 187 ? 20.761  -31.673 -3.547  1.00 175.87 ? 187 ALA A CB  1 
ATOM   1406 N N   . ILE A 1 188 ? 19.671  -29.597 -1.493  1.00 209.26 ? 188 ILE A N   1 
ATOM   1407 C CA  . ILE A 1 188 ? 18.710  -28.586 -1.067  1.00 185.29 ? 188 ILE A CA  1 
ATOM   1408 C C   . ILE A 1 188 ? 19.464  -27.358 -0.559  1.00 191.68 ? 188 ILE A C   1 
ATOM   1409 O O   . ILE A 1 188 ? 19.066  -26.239 -0.876  1.00 183.21 ? 188 ILE A O   1 
ATOM   1410 C CB  . ILE A 1 188 ? 17.749  -29.170 -0.004  1.00 158.22 ? 188 ILE A CB  1 
ATOM   1411 C CG1 . ILE A 1 188 ? 16.787  -30.212 -0.581  1.00 149.16 ? 188 ILE A CG1 1 
ATOM   1412 C CG2 . ILE A 1 188 ? 17.006  -28.077 0.772   1.00 167.31 ? 188 ILE A CG2 1 
ATOM   1413 C CD1 . ILE A 1 188 ? 15.760  -30.716 0.419   1.00 150.43 ? 188 ILE A CD1 1 
ATOM   1414 N N   . HIS A 1 189 ? 20.476  -27.596 0.289   1.00 176.26 ? 189 HIS A N   1 
ATOM   1415 C CA  . HIS A 1 189 ? 21.269  -26.530 0.868   1.00 157.96 ? 189 HIS A CA  1 
ATOM   1416 C C   . HIS A 1 189 ? 22.503  -26.317 0.004   1.00 162.88 ? 189 HIS A C   1 
ATOM   1417 O O   . HIS A 1 189 ? 23.587  -26.719 0.396   1.00 200.58 ? 189 HIS A O   1 
ATOM   1418 C CB  . HIS A 1 189 ? 21.834  -26.939 2.230   1.00 148.47 ? 189 HIS A CB  1 
ATOM   1419 C CG  . HIS A 1 189 ? 20.881  -27.390 3.284   1.00 167.08 ? 189 HIS A CG  1 
ATOM   1420 N ND1 . HIS A 1 189 ? 21.339  -27.965 4.454   1.00 163.56 ? 189 HIS A ND1 1 
ATOM   1421 C CD2 . HIS A 1 189 ? 19.551  -27.340 3.395   1.00 198.33 ? 189 HIS A CD2 1 
ATOM   1422 C CE1 . HIS A 1 189 ? 20.319  -28.239 5.249   1.00 176.10 ? 189 HIS A CE1 1 
ATOM   1423 N NE2 . HIS A 1 189 ? 19.220  -27.863 4.627   1.00 211.96 ? 189 HIS A NE2 1 
ATOM   1424 N N   . ARG A 1 190 ? 22.330  -25.684 -1.159  1.00 171.70 ? 190 ARG A N   1 
ATOM   1425 C CA  . ARG A 1 190 ? 23.397  -25.443 -2.116  1.00 177.39 ? 190 ARG A CA  1 
ATOM   1426 C C   . ARG A 1 190 ? 22.730  -24.877 -3.360  1.00 170.07 ? 190 ARG A C   1 
ATOM   1427 O O   . ARG A 1 190 ? 23.212  -25.029 -4.472  1.00 168.17 ? 190 ARG A O   1 
ATOM   1428 C CB  . ARG A 1 190 ? 24.098  -26.753 -2.501  1.00 190.54 ? 190 ARG A CB  1 
ATOM   1429 C CG  . ARG A 1 190 ? 25.621  -26.706 -2.514  1.00 205.16 ? 190 ARG A CG  1 
ATOM   1430 C CD  . ARG A 1 190 ? 26.259  -28.085 -2.434  1.00 203.29 ? 190 ARG A CD  1 
ATOM   1431 N NE  . ARG A 1 190 ? 26.053  -28.758 -3.719  1.00 229.05 ? 190 ARG A NE  1 
ATOM   1432 C CZ  . ARG A 1 190 ? 26.564  -29.959 -3.993  1.00 245.20 ? 190 ARG A CZ  1 
ATOM   1433 N NH1 . ARG A 1 190 ? 27.596  -30.415 -3.298  1.00 266.06 ? 190 ARG A NH1 1 
ATOM   1434 N NH2 . ARG A 1 190 ? 26.077  -30.682 -4.988  1.00 232.42 ? 190 ARG A NH2 1 
ATOM   1435 N N   . LEU A 1 191 ? 21.590  -24.229 -3.147  1.00 166.14 ? 191 LEU A N   1 
ATOM   1436 C CA  . LEU A 1 191 ? 20.730  -23.842 -4.246  1.00 169.22 ? 191 LEU A CA  1 
ATOM   1437 C C   . LEU A 1 191 ? 20.795  -22.347 -4.491  1.00 178.06 ? 191 LEU A C   1 
ATOM   1438 O O   . LEU A 1 191 ? 21.731  -21.705 -4.031  1.00 208.49 ? 191 LEU A O   1 
ATOM   1439 C CB  . LEU A 1 191 ? 19.321  -24.273 -3.863  1.00 174.84 ? 191 LEU A CB  1 
ATOM   1440 C CG  . LEU A 1 191 ? 18.653  -25.278 -4.802  1.00 181.81 ? 191 LEU A CG  1 
ATOM   1441 C CD1 . LEU A 1 191 ? 19.637  -26.054 -5.675  1.00 167.64 ? 191 LEU A CD1 1 
ATOM   1442 C CD2 . LEU A 1 191 ? 17.816  -26.217 -3.945  1.00 175.37 ? 191 LEU A CD2 1 
ATOM   1443 N N   . SER A 1 192 ? 19.800  -21.828 -5.227  1.00 175.05 ? 192 SER A N   1 
ATOM   1444 C CA  . SER A 1 192 ? 19.840  -20.485 -5.788  1.00 183.81 ? 192 SER A CA  1 
ATOM   1445 C C   . SER A 1 192 ? 19.099  -19.499 -4.894  1.00 192.83 ? 192 SER A C   1 
ATOM   1446 O O   . SER A 1 192 ? 19.246  -18.287 -5.053  1.00 224.97 ? 192 SER A O   1 
ATOM   1447 C CB  . SER A 1 192 ? 19.293  -20.454 -7.193  1.00 178.90 ? 192 SER A CB  1 
ATOM   1448 O OG  . SER A 1 192 ? 19.906  -21.461 -7.988  1.00 191.09 ? 192 SER A OG  1 
ATOM   1449 N N   . CYS A 1 193 ? 18.317  -20.035 -3.953  1.00 181.92 ? 193 CYS A N   1 
ATOM   1450 C CA  . CYS A 1 193 ? 17.353  -19.239 -3.215  1.00 203.41 ? 193 CYS A CA  1 
ATOM   1451 C C   . CYS A 1 193 ? 16.695  -18.248 -4.169  1.00 230.42 ? 193 CYS A C   1 
ATOM   1452 O O   . CYS A 1 193 ? 16.154  -18.644 -5.199  1.00 275.75 ? 193 CYS A O   1 
ATOM   1453 C CB  . CYS A 1 193 ? 18.000  -18.539 -2.030  1.00 177.52 ? 193 CYS A CB  1 
ATOM   1454 S SG  . CYS A 1 193 ? 18.439  -19.707 -0.724  1.00 177.98 ? 193 CYS A SG  1 
ATOM   1455 N N   . GLY A 1 194 ? 16.798  -16.959 -3.833  1.00 203.89 ? 194 GLY A N   1 
ATOM   1456 C CA  . GLY A 1 194 ? 16.035  -15.927 -4.509  1.00 185.80 ? 194 GLY A CA  1 
ATOM   1457 C C   . GLY A 1 194 ? 14.893  -15.482 -3.607  1.00 193.66 ? 194 GLY A C   1 
ATOM   1458 O O   . GLY A 1 194 ? 14.319  -16.299 -2.892  1.00 197.71 ? 194 GLY A O   1 
ATOM   1459 N N   . THR A 1 195 ? 14.606  -14.178 -3.617  1.00 215.27 ? 195 THR A N   1 
ATOM   1460 C CA  . THR A 1 195 ? 13.567  -13.624 -2.768  1.00 217.70 ? 195 THR A CA  1 
ATOM   1461 C C   . THR A 1 195 ? 12.294  -14.434 -2.986  1.00 228.01 ? 195 THR A C   1 
ATOM   1462 O O   . THR A 1 195 ? 11.839  -14.600 -4.114  1.00 234.70 ? 195 THR A O   1 
ATOM   1463 C CB  . THR A 1 195 ? 13.373  -12.143 -3.082  1.00 214.31 ? 195 THR A CB  1 
ATOM   1464 O OG1 . THR A 1 195 ? 12.869  -12.134 -4.415  1.00 224.40 ? 195 THR A OG1 1 
ATOM   1465 C CG2 . THR A 1 195 ? 14.662  -11.348 -2.957  1.00 196.71 ? 195 THR A CG2 1 
ATOM   1466 N N   . ALA A 1 196 ? 11.759  -14.967 -1.886  1.00 242.70 ? 196 ALA A N   1 
ATOM   1467 C CA  . ALA A 1 196 ? 10.598  -15.837 -1.909  1.00 235.52 ? 196 ALA A CA  1 
ATOM   1468 C C   . ALA A 1 196 ? 9.916   -15.758 -0.548  1.00 227.82 ? 196 ALA A C   1 
ATOM   1469 O O   . ALA A 1 196 ? 10.530  -16.073 0.470   1.00 234.93 ? 196 ALA A O   1 
ATOM   1470 C CB  . ALA A 1 196 ? 11.030  -17.255 -2.246  1.00 227.62 ? 196 ALA A CB  1 
ATOM   1471 N N   . ALA A 1 197 ? 8.658   -15.297 -0.550  1.00 213.93 ? 197 ALA A N   1 
ATOM   1472 C CA  . ALA A 1 197 ? 7.810   -15.318 0.631   1.00 231.70 ? 197 ALA A CA  1 
ATOM   1473 C C   . ALA A 1 197 ? 8.090   -16.576 1.452   1.00 276.20 ? 197 ALA A C   1 
ATOM   1474 O O   . ALA A 1 197 ? 8.413   -16.474 2.633   1.00 299.35 ? 197 ALA A O   1 
ATOM   1475 C CB  . ALA A 1 197 ? 6.353   -15.221 0.227   1.00 220.70 ? 197 ALA A CB  1 
ATOM   1476 N N   . ALA A 1 198 ? 8.004   -17.750 0.809   1.00 293.57 ? 198 ALA A N   1 
ATOM   1477 C CA  . ALA A 1 198 ? 8.264   -19.023 1.470   1.00 272.93 ? 198 ALA A CA  1 
ATOM   1478 C C   . ALA A 1 198 ? 9.230   -19.869 0.647   1.00 258.74 ? 198 ALA A C   1 
ATOM   1479 O O   . ALA A 1 198 ? 8.827   -20.814 -0.015  1.00 282.45 ? 198 ALA A O   1 
ATOM   1480 C CB  . ALA A 1 198 ? 6.957   -19.747 1.752   1.00 258.04 ? 198 ALA A CB  1 
ATOM   1481 N N   . ARG A 1 199 ? 10.515  -19.525 0.737   1.00 233.36 ? 199 ARG A N   1 
ATOM   1482 C CA  . ARG A 1 199 ? 11.589  -20.156 -0.011  1.00 215.77 ? 199 ARG A CA  1 
ATOM   1483 C C   . ARG A 1 199 ? 11.520  -21.680 0.122   1.00 205.45 ? 199 ARG A C   1 
ATOM   1484 O O   . ARG A 1 199 ? 11.456  -22.210 1.226   1.00 179.15 ? 199 ARG A O   1 
ATOM   1485 C CB  . ARG A 1 199 ? 12.894  -19.533 0.498   1.00 226.75 ? 199 ARG A CB  1 
ATOM   1486 C CG  . ARG A 1 199 ? 12.710  -18.964 1.903   1.00 245.41 ? 199 ARG A CG  1 
ATOM   1487 C CD  . ARG A 1 199 ? 14.017  -18.622 2.593   1.00 259.20 ? 199 ARG A CD  1 
ATOM   1488 N NE  . ARG A 1 199 ? 14.678  -19.860 3.022   1.00 261.11 ? 199 ARG A NE  1 
ATOM   1489 C CZ  . ARG A 1 199 ? 15.166  -20.134 4.232   1.00 234.07 ? 199 ARG A CZ  1 
ATOM   1490 N NH1 . ARG A 1 199 ? 15.600  -21.356 4.496   1.00 205.78 ? 199 ARG A NH1 1 
ATOM   1491 N NH2 . ARG A 1 199 ? 15.182  -19.212 5.183   1.00 229.50 ? 199 ARG A NH2 1 
ATOM   1492 N N   . ARG A 1 200 ? 11.507  -22.359 -1.027  1.00 202.48 ? 200 ARG A N   1 
ATOM   1493 C CA  . ARG A 1 200 ? 11.186  -23.773 -1.119  1.00 177.40 ? 200 ARG A CA  1 
ATOM   1494 C C   . ARG A 1 200 ? 12.141  -24.517 -2.048  1.00 190.24 ? 200 ARG A C   1 
ATOM   1495 O O   . ARG A 1 200 ? 12.682  -24.016 -3.045  1.00 211.20 ? 200 ARG A O   1 
ATOM   1496 C CB  . ARG A 1 200 ? 9.726   -24.042 -1.511  1.00 179.68 ? 200 ARG A CB  1 
ATOM   1497 C CG  . ARG A 1 200 ? 8.746   -24.089 -0.345  1.00 196.25 ? 200 ARG A CG  1 
ATOM   1498 C CD  . ARG A 1 200 ? 7.267   -24.256 -0.667  1.00 177.34 ? 200 ARG A CD  1 
ATOM   1499 N NE  . ARG A 1 200 ? 6.659   -22.928 -0.767  1.00 180.95 ? 200 ARG A NE  1 
ATOM   1500 C CZ  . ARG A 1 200 ? 5.429   -22.651 -1.164  1.00 218.17 ? 200 ARG A CZ  1 
ATOM   1501 N NH1 . ARG A 1 200 ? 4.585   -23.630 -1.446  1.00 224.37 ? 200 ARG A NH1 1 
ATOM   1502 N NH2 . ARG A 1 200 ? 5.061   -21.386 -1.279  1.00 247.68 ? 200 ARG A NH2 1 
ATOM   1503 N N   . ALA A 1 201 ? 12.236  -25.818 -1.771  1.00 196.39 ? 201 ALA A N   1 
ATOM   1504 C CA  . ALA A 1 201 ? 12.972  -26.798 -2.563  1.00 178.70 ? 201 ALA A CA  1 
ATOM   1505 C C   . ALA A 1 201 ? 12.114  -28.022 -2.883  1.00 158.26 ? 201 ALA A C   1 
ATOM   1506 O O   . ALA A 1 201 ? 11.262  -28.468 -2.083  1.00 157.66 ? 201 ALA A O   1 
ATOM   1507 C CB  . ALA A 1 201 ? 14.234  -27.189 -1.838  1.00 206.04 ? 201 ALA A CB  1 
ATOM   1508 N N   . MET A 1 202 ? 12.379  -28.581 -4.068  1.00 149.23 ? 202 MET A N   1 
ATOM   1509 C CA  . MET A 1 202 ? 11.596  -29.676 -4.627  1.00 155.47 ? 202 MET A CA  1 
ATOM   1510 C C   . MET A 1 202 ? 12.509  -30.806 -5.077  1.00 146.55 ? 202 MET A C   1 
ATOM   1511 O O   . MET A 1 202 ? 13.471  -30.600 -5.799  1.00 148.81 ? 202 MET A O   1 
ATOM   1512 C CB  . MET A 1 202 ? 10.736  -29.207 -5.803  1.00 163.75 ? 202 MET A CB  1 
ATOM   1513 C CG  . MET A 1 202 ? 9.428   -29.958 -5.941  1.00 149.13 ? 202 MET A CG  1 
ATOM   1514 S SD  . MET A 1 202 ? 8.975   -30.051 -7.685  1.00 177.44 ? 202 MET A SD  1 
ATOM   1515 C CE  . MET A 1 202 ? 8.523   -28.359 -8.085  1.00 145.57 ? 202 MET A CE  1 
ATOM   1516 N N   . VAL A 1 203 ? 12.155  -32.016 -4.631  1.00 146.39 ? 203 VAL A N   1 
ATOM   1517 C CA  . VAL A 1 203 ? 12.903  -33.241 -4.893  1.00 142.53 ? 203 VAL A CA  1 
ATOM   1518 C C   . VAL A 1 203 ? 12.068  -34.172 -5.763  1.00 142.28 ? 203 VAL A C   1 
ATOM   1519 O O   . VAL A 1 203 ? 11.042  -34.643 -5.274  1.00 155.31 ? 203 VAL A O   1 
ATOM   1520 C CB  . VAL A 1 203 ? 13.053  -33.938 -3.519  1.00 153.14 ? 203 VAL A CB  1 
ATOM   1521 C CG1 . VAL A 1 203 ? 13.618  -35.352 -3.603  1.00 156.93 ? 203 VAL A CG1 1 
ATOM   1522 C CG2 . VAL A 1 203 ? 13.797  -33.109 -2.483  1.00 181.90 ? 203 VAL A CG2 1 
ATOM   1523 N N   . LYS A 1 204 ? 12.548  -34.491 -6.986  1.00 132.43 ? 204 LYS A N   1 
ATOM   1524 C CA  . LYS A 1 204 ? 11.744  -35.212 -7.959  1.00 132.96 ? 204 LYS A CA  1 
ATOM   1525 C C   . LYS A 1 204 ? 12.331  -36.593 -8.205  1.00 131.69 ? 204 LYS A C   1 
ATOM   1526 O O   . LYS A 1 204 ? 13.432  -36.663 -8.727  1.00 139.05 ? 204 LYS A O   1 
ATOM   1527 C CB  . LYS A 1 204 ? 11.717  -34.469 -9.300  1.00 137.54 ? 204 LYS A CB  1 
ATOM   1528 C CG  . LYS A 1 204 ? 10.975  -33.148 -9.399  1.00 142.79 ? 204 LYS A CG  1 
ATOM   1529 C CD  . LYS A 1 204 ? 10.764  -32.858 -10.881 1.00 146.93 ? 204 LYS A CD  1 
ATOM   1530 C CE  . LYS A 1 204 ? 9.962   -31.641 -11.182 1.00 144.82 ? 204 LYS A CE  1 
ATOM   1531 N NZ  . LYS A 1 204 ? 10.606  -30.463 -10.610 1.00 170.20 ? 204 LYS A NZ  1 
ATOM   1532 N N   . LEU A 1 205 ? 11.602  -37.638 -7.782  1.00 132.60 ? 205 LEU A N   1 
ATOM   1533 C CA  . LEU A 1 205 ? 12.075  -39.003 -7.855  1.00 131.09 ? 205 LEU A CA  1 
ATOM   1534 C C   . LEU A 1 205 ? 12.353  -39.368 -9.312  1.00 139.74 ? 205 LEU A C   1 
ATOM   1535 O O   . LEU A 1 205 ? 11.505  -39.196 -10.196 1.00 146.16 ? 205 LEU A O   1 
ATOM   1536 C CB  . LEU A 1 205 ? 11.070  -39.954 -7.211  1.00 114.40 ? 205 LEU A CB  1 
ATOM   1537 C CG  . LEU A 1 205 ? 10.831  -39.739 -5.712  1.00 114.33 ? 205 LEU A CG  1 
ATOM   1538 C CD1 . LEU A 1 205 ? 9.650   -40.545 -5.236  1.00 119.48 ? 205 LEU A CD1 1 
ATOM   1539 C CD2 . LEU A 1 205 ? 12.051  -40.076 -4.885  1.00 110.86 ? 205 LEU A CD2 1 
ATOM   1540 N N   . ASP A 1 206 ? 13.559  -39.906 -9.555  1.00 137.57 ? 206 ASP A N   1 
ATOM   1541 C CA  . ASP A 1 206 ? 14.165  -39.931 -10.881 1.00 141.79 ? 206 ASP A CA  1 
ATOM   1542 C C   . ASP A 1 206 ? 13.421  -40.829 -11.875 1.00 162.02 ? 206 ASP A C   1 
ATOM   1543 O O   . ASP A 1 206 ? 13.385  -40.524 -13.071 1.00 161.87 ? 206 ASP A O   1 
ATOM   1544 C CB  . ASP A 1 206 ? 15.649  -40.239 -10.780 1.00 160.51 ? 206 ASP A CB  1 
ATOM   1545 C CG  . ASP A 1 206 ? 16.372  -40.275 -12.115 1.00 206.93 ? 206 ASP A CG  1 
ATOM   1546 O OD1 . ASP A 1 206 ? 16.292  -39.270 -12.845 1.00 202.48 ? 206 ASP A OD1 1 
ATOM   1547 O OD2 . ASP A 1 206 ? 16.991  -41.315 -12.417 1.00 265.22 ? 206 ASP A OD2 1 
ATOM   1548 N N   . ALA A 1 207 ? 12.859  -41.947 -11.393 1.00 167.85 ? 207 ALA A N   1 
ATOM   1549 C CA  . ALA A 1 207 ? 12.221  -42.944 -12.247 1.00 149.81 ? 207 ALA A CA  1 
ATOM   1550 C C   . ALA A 1 207 ? 11.128  -42.320 -13.118 1.00 165.52 ? 207 ALA A C   1 
ATOM   1551 O O   . ALA A 1 207 ? 10.548  -41.293 -12.754 1.00 174.91 ? 207 ALA A O   1 
ATOM   1552 C CB  . ALA A 1 207 ? 11.679  -44.071 -11.397 1.00 143.72 ? 207 ALA A CB  1 
ATOM   1553 N N   . ILE A 1 208 ? 10.864  -42.953 -14.275 1.00 170.72 ? 208 ILE A N   1 
ATOM   1554 C CA  . ILE A 1 208 ? 9.810   -42.520 -15.191 1.00 188.52 ? 208 ILE A CA  1 
ATOM   1555 C C   . ILE A 1 208 ? 8.482   -43.161 -14.785 1.00 197.28 ? 208 ILE A C   1 
ATOM   1556 O O   . ILE A 1 208 ? 7.418   -42.721 -15.224 1.00 201.69 ? 208 ILE A O   1 
ATOM   1557 C CB  . ILE A 1 208 ? 10.144  -42.737 -16.687 1.00 175.45 ? 208 ILE A CB  1 
ATOM   1558 C CG1 . ILE A 1 208 ? 9.276   -43.813 -17.400 1.00 157.07 ? 208 ILE A CG1 1 
ATOM   1559 C CG2 . ILE A 1 208 ? 11.639  -42.959 -16.888 1.00 167.07 ? 208 ILE A CG2 1 
ATOM   1560 C CD1 . ILE A 1 208 ? 8.811   -43.440 -18.806 1.00 153.48 ? 208 ILE A CD1 1 
ATOM   1561 N N   . THR A 1 209 ? 8.564   -44.192 -13.935 1.00 185.42 ? 209 THR A N   1 
ATOM   1562 C CA  . THR A 1 209 ? 7.403   -44.848 -13.352 1.00 175.77 ? 209 THR A CA  1 
ATOM   1563 C C   . THR A 1 209 ? 6.606   -43.830 -12.531 1.00 216.46 ? 209 THR A C   1 
ATOM   1564 O O   . THR A 1 209 ? 5.393   -43.961 -12.372 1.00 238.26 ? 209 THR A O   1 
ATOM   1565 C CB  . THR A 1 209 ? 7.882   -45.994 -12.462 1.00 159.13 ? 209 THR A CB  1 
ATOM   1566 O OG1 . THR A 1 209 ? 8.049   -45.431 -11.164 1.00 135.53 ? 209 THR A OG1 1 
ATOM   1567 C CG2 . THR A 1 209 ? 9.176   -46.632 -12.944 1.00 165.78 ? 209 THR A CG2 1 
ATOM   1568 N N   . TRP A 1 210 ? 7.316   -42.814 -12.022 1.00 233.05 ? 210 TRP A N   1 
ATOM   1569 C CA  . TRP A 1 210 ? 6.785   -41.799 -11.126 1.00 198.26 ? 210 TRP A CA  1 
ATOM   1570 C C   . TRP A 1 210 ? 6.372   -40.549 -11.895 1.00 197.11 ? 210 TRP A C   1 
ATOM   1571 O O   . TRP A 1 210 ? 6.268   -39.479 -11.299 1.00 200.89 ? 210 TRP A O   1 
ATOM   1572 C CB  . TRP A 1 210 ? 7.851   -41.446 -10.078 1.00 179.52 ? 210 TRP A CB  1 
ATOM   1573 C CG  . TRP A 1 210 ? 7.790   -42.281 -8.829  1.00 170.38 ? 210 TRP A CG  1 
ATOM   1574 C CD1 . TRP A 1 210 ? 8.822   -42.620 -8.006  1.00 152.00 ? 210 TRP A CD1 1 
ATOM   1575 C CD2 . TRP A 1 210 ? 6.605   -42.861 -8.244  1.00 185.21 ? 210 TRP A CD2 1 
ATOM   1576 N NE1 . TRP A 1 210 ? 8.367   -43.380 -6.961  1.00 148.32 ? 210 TRP A NE1 1 
ATOM   1577 C CE2 . TRP A 1 210 ? 7.016   -43.549 -7.079  1.00 174.84 ? 210 TRP A CE2 1 
ATOM   1578 C CE3 . TRP A 1 210 ? 5.250   -42.867 -8.596  1.00 213.23 ? 210 TRP A CE3 1 
ATOM   1579 C CZ2 . TRP A 1 210 ? 6.118   -44.239 -6.266  1.00 203.33 ? 210 TRP A CZ2 1 
ATOM   1580 C CZ3 . TRP A 1 210 ? 4.367   -43.551 -7.798  1.00 238.26 ? 210 TRP A CZ3 1 
ATOM   1581 C CH2 . TRP A 1 210 ? 4.797   -44.224 -6.652  1.00 233.42 ? 210 TRP A CH2 1 
ATOM   1582 N N   . ALA A 1 211 ? 6.108   -40.705 -13.198 1.00 201.43 ? 211 ALA A N   1 
ATOM   1583 C CA  . ALA A 1 211 ? 5.841   -39.587 -14.088 1.00 217.83 ? 211 ALA A CA  1 
ATOM   1584 C C   . ALA A 1 211 ? 4.788   -38.665 -13.473 1.00 232.55 ? 211 ALA A C   1 
ATOM   1585 O O   . ALA A 1 211 ? 3.917   -39.096 -12.716 1.00 214.32 ? 211 ALA A O   1 
ATOM   1586 C CB  . ALA A 1 211 ? 5.441   -40.071 -15.472 1.00 200.67 ? 211 ALA A CB  1 
ATOM   1587 N N   . ALA A 1 212 ? 4.907   -37.378 -13.804 1.00 227.94 ? 212 ALA A N   1 
ATOM   1588 C CA  . ALA A 1 212 ? 4.049   -36.346 -13.250 1.00 221.55 ? 212 ALA A CA  1 
ATOM   1589 C C   . ALA A 1 212 ? 4.177   -36.333 -11.728 1.00 218.82 ? 212 ALA A C   1 
ATOM   1590 O O   . ALA A 1 212 ? 5.218   -36.684 -11.170 1.00 212.31 ? 212 ALA A O   1 
ATOM   1591 C CB  . ALA A 1 212 ? 2.608   -36.528 -13.697 1.00 195.21 ? 212 ALA A CB  1 
ATOM   1592 N N   . SER A 1 213 ? 3.083   -35.954 -11.060 1.00 197.57 ? 213 SER A N   1 
ATOM   1593 C CA  . SER A 1 213 ? 3.187   -35.351 -9.741  1.00 171.91 ? 213 SER A CA  1 
ATOM   1594 C C   . SER A 1 213 ? 2.872   -36.364 -8.648  1.00 159.47 ? 213 SER A C   1 
ATOM   1595 O O   . SER A 1 213 ? 2.025   -36.108 -7.804  1.00 166.06 ? 213 SER A O   1 
ATOM   1596 C CB  . SER A 1 213 ? 2.289   -34.143 -9.625  1.00 176.23 ? 213 SER A CB  1 
ATOM   1597 O OG  . SER A 1 213 ? 2.068   -33.553 -10.903 1.00 170.16 ? 213 SER A OG  1 
ATOM   1598 N N   . ILE A 1 214 ? 3.563   -37.502 -8.660  1.00 154.24 ? 214 ILE A N   1 
ATOM   1599 C CA  . ILE A 1 214 ? 3.477   -38.423 -7.541  1.00 156.31 ? 214 ILE A CA  1 
ATOM   1600 C C   . ILE A 1 214 ? 4.861   -38.488 -6.915  1.00 163.08 ? 214 ILE A C   1 
ATOM   1601 O O   . ILE A 1 214 ? 4.993   -38.604 -5.696  1.00 154.53 ? 214 ILE A O   1 
ATOM   1602 C CB  . ILE A 1 214 ? 3.040   -39.827 -7.986  1.00 166.67 ? 214 ILE A CB  1 
ATOM   1603 C CG1 . ILE A 1 214 ? 2.107   -39.820 -9.217  1.00 185.48 ? 214 ILE A CG1 1 
ATOM   1604 C CG2 . ILE A 1 214 ? 2.468   -40.583 -6.786  1.00 148.03 ? 214 ILE A CG2 1 
ATOM   1605 C CD1 . ILE A 1 214 ? 1.896   -41.187 -9.850  1.00 196.95 ? 214 ILE A CD1 1 
ATOM   1606 N N   . GLY A 1 215 ? 5.861   -38.399 -7.805  1.00 175.19 ? 215 GLY A N   1 
ATOM   1607 C CA  . GLY A 1 215 ? 7.272   -38.475 -7.458  1.00 198.52 ? 215 GLY A CA  1 
ATOM   1608 C C   . GLY A 1 215 ? 7.732   -37.178 -6.810  1.00 176.80 ? 215 GLY A C   1 
ATOM   1609 O O   . GLY A 1 215 ? 8.304   -37.191 -5.722  1.00 208.40 ? 215 GLY A O   1 
ATOM   1610 N N   . ASN A 1 216 ? 7.442   -36.069 -7.497  1.00 140.30 ? 216 ASN A N   1 
ATOM   1611 C CA  . ASN A 1 216 ? 7.788   -34.731 -7.041  1.00 132.91 ? 216 ASN A CA  1 
ATOM   1612 C C   . ASN A 1 216 ? 7.361   -34.547 -5.590  1.00 135.69 ? 216 ASN A C   1 
ATOM   1613 O O   . ASN A 1 216 ? 6.202   -34.735 -5.257  1.00 125.99 ? 216 ASN A O   1 
ATOM   1614 C CB  . ASN A 1 216 ? 7.154   -33.678 -7.944  1.00 131.49 ? 216 ASN A CB  1 
ATOM   1615 C CG  . ASN A 1 216 ? 7.382   -33.958 -9.408  1.00 155.89 ? 216 ASN A CG  1 
ATOM   1616 O OD1 . ASN A 1 216 ? 8.052   -34.940 -9.765  1.00 168.12 ? 216 ASN A OD1 1 
ATOM   1617 N ND2 . ASN A 1 216 ? 6.829   -33.107 -10.260 1.00 170.70 ? 216 ASN A ND2 1 
ATOM   1618 N N   . VAL A 1 217 ? 8.327   -34.194 -4.733  1.00 152.67 ? 217 VAL A N   1 
ATOM   1619 C CA  . VAL A 1 217 ? 8.119   -33.927 -3.325  1.00 148.16 ? 217 VAL A CA  1 
ATOM   1620 C C   . VAL A 1 217 ? 8.838   -32.618 -2.986  1.00 175.33 ? 217 VAL A C   1 
ATOM   1621 O O   . VAL A 1 217 ? 10.014  -32.393 -3.308  1.00 222.14 ? 217 VAL A O   1 
ATOM   1622 C CB  . VAL A 1 217 ? 8.483   -35.050 -2.326  1.00 138.90 ? 217 VAL A CB  1 
ATOM   1623 C CG1 . VAL A 1 217 ? 8.393   -34.583 -0.879  1.00 128.29 ? 217 VAL A CG1 1 
ATOM   1624 C CG2 . VAL A 1 217 ? 7.617   -36.294 -2.485  1.00 169.57 ? 217 VAL A CG2 1 
ATOM   1625 N N   . LEU A 1 218 ? 8.142   -31.793 -2.192  1.00 181.54 ? 218 LEU A N   1 
ATOM   1626 C CA  . LEU A 1 218 ? 8.486   -30.403 -1.951  1.00 170.12 ? 218 LEU A CA  1 
ATOM   1627 C C   . LEU A 1 218 ? 8.633   -30.127 -0.447  1.00 174.29 ? 218 LEU A C   1 
ATOM   1628 O O   . LEU A 1 218 ? 7.816   -30.523 0.383   1.00 172.74 ? 218 LEU A O   1 
ATOM   1629 C CB  . LEU A 1 218 ? 7.358   -29.586 -2.586  1.00 157.85 ? 218 LEU A CB  1 
ATOM   1630 C CG  . LEU A 1 218 ? 7.321   -28.094 -2.254  1.00 149.82 ? 218 LEU A CG  1 
ATOM   1631 C CD1 . LEU A 1 218 ? 8.162   -27.331 -3.221  1.00 146.09 ? 218 LEU A CD1 1 
ATOM   1632 C CD2 . LEU A 1 218 ? 5.926   -27.521 -2.253  1.00 142.20 ? 218 LEU A CD2 1 
ATOM   1633 N N   . ILE A 1 219 ? 9.758   -29.494 -0.128  1.00 174.90 ? 219 ILE A N   1 
ATOM   1634 C CA  . ILE A 1 219 ? 10.188  -29.202 1.229   1.00 187.64 ? 219 ILE A CA  1 
ATOM   1635 C C   . ILE A 1 219 ? 10.573  -27.725 1.334   1.00 209.60 ? 219 ILE A C   1 
ATOM   1636 O O   . ILE A 1 219 ? 11.361  -27.208 0.521   1.00 210.68 ? 219 ILE A O   1 
ATOM   1637 C CB  . ILE A 1 219 ? 11.365  -30.125 1.615   1.00 190.55 ? 219 ILE A CB  1 
ATOM   1638 C CG1 . ILE A 1 219 ? 10.907  -31.508 2.048   1.00 164.33 ? 219 ILE A CG1 1 
ATOM   1639 C CG2 . ILE A 1 219 ? 12.281  -29.497 2.665   1.00 228.67 ? 219 ILE A CG2 1 
ATOM   1640 C CD1 . ILE A 1 219 ? 11.085  -32.571 0.985   1.00 185.37 ? 219 ILE A CD1 1 
ATOM   1641 N N   . ASP A 1 220 ? 10.002  -27.070 2.362   1.00 242.95 ? 220 ASP A N   1 
ATOM   1642 C CA  . ASP A 1 220 ? 10.370  -25.693 2.693   1.00 257.61 ? 220 ASP A CA  1 
ATOM   1643 C C   . ASP A 1 220 ? 11.613  -25.704 3.570   1.00 250.66 ? 220 ASP A C   1 
ATOM   1644 O O   . ASP A 1 220 ? 11.598  -26.298 4.644   1.00 239.32 ? 220 ASP A O   1 
ATOM   1645 C CB  . ASP A 1 220 ? 9.222   -24.833 3.216   1.00 262.59 ? 220 ASP A CB  1 
ATOM   1646 C CG  . ASP A 1 220 ? 8.898   -24.926 4.704   1.00 242.23 ? 220 ASP A CG  1 
ATOM   1647 O OD1 . ASP A 1 220 ? 8.435   -26.002 5.129   1.00 263.95 ? 220 ASP A OD1 1 
ATOM   1648 O OD2 . ASP A 1 220 ? 9.107   -23.923 5.426   1.00 199.80 ? 220 ASP A OD2 1 
ATOM   1649 N N   . ARG A 1 221 ? 12.673  -25.015 3.114   1.00 235.42 ? 221 ARG A N   1 
ATOM   1650 C CA  . ARG A 1 221 ? 14.000  -25.124 3.680   1.00 217.02 ? 221 ARG A CA  1 
ATOM   1651 C C   . ARG A 1 221 ? 14.055  -24.679 5.131   1.00 212.85 ? 221 ARG A C   1 
ATOM   1652 O O   . ARG A 1 221 ? 14.922  -25.164 5.854   1.00 232.19 ? 221 ARG A O   1 
ATOM   1653 C CB  . ARG A 1 221 ? 15.014  -24.341 2.845   1.00 201.99 ? 221 ARG A CB  1 
ATOM   1654 C CG  . ARG A 1 221 ? 14.957  -24.721 1.377   1.00 185.63 ? 221 ARG A CG  1 
ATOM   1655 C CD  . ARG A 1 221 ? 16.273  -24.338 0.748   1.00 168.09 ? 221 ARG A CD  1 
ATOM   1656 N NE  . ARG A 1 221 ? 15.937  -23.782 -0.562  1.00 165.65 ? 221 ARG A NE  1 
ATOM   1657 C CZ  . ARG A 1 221 ? 16.820  -23.239 -1.369  1.00 175.58 ? 221 ARG A CZ  1 
ATOM   1658 N NH1 . ARG A 1 221 ? 18.102  -23.222 -1.051  1.00 165.19 ? 221 ARG A NH1 1 
ATOM   1659 N NH2 . ARG A 1 221 ? 16.413  -22.733 -2.511  1.00 198.58 ? 221 ARG A NH2 1 
ATOM   1660 N N   . ASP A 1 222 ? 13.143  -23.789 5.536   1.00 202.42 ? 222 ASP A N   1 
ATOM   1661 C CA  . ASP A 1 222 ? 13.067  -23.273 6.889   1.00 210.22 ? 222 ASP A CA  1 
ATOM   1662 C C   . ASP A 1 222 ? 12.911  -24.441 7.881   1.00 196.45 ? 222 ASP A C   1 
ATOM   1663 O O   . ASP A 1 222 ? 13.639  -24.554 8.888   1.00 196.79 ? 222 ASP A O   1 
ATOM   1664 C CB  . ASP A 1 222 ? 11.910  -22.278 6.979   1.00 249.36 ? 222 ASP A CB  1 
ATOM   1665 C CG  . ASP A 1 222 ? 12.040  -20.987 6.173   1.00 273.84 ? 222 ASP A CG  1 
ATOM   1666 O OD1 . ASP A 1 222 ? 12.845  -20.118 6.580   1.00 245.55 ? 222 ASP A OD1 1 
ATOM   1667 O OD2 . ASP A 1 222 ? 11.340  -20.844 5.133   1.00 319.28 ? 222 ASP A OD2 1 
ATOM   1668 N N   . LYS A 1 223 ? 11.953  -25.307 7.533   1.00 192.08 ? 223 LYS A N   1 
ATOM   1669 C CA  . LYS A 1 223 ? 11.621  -26.455 8.368   1.00 185.33 ? 223 LYS A CA  1 
ATOM   1670 C C   . LYS A 1 223 ? 12.821  -27.380 8.465   1.00 193.89 ? 223 LYS A C   1 
ATOM   1671 O O   . LYS A 1 223 ? 12.960  -28.056 9.476   1.00 208.12 ? 223 LYS A O   1 
ATOM   1672 C CB  . LYS A 1 223 ? 10.299  -27.174 8.071   1.00 173.98 ? 223 LYS A CB  1 
ATOM   1673 C CG  . LYS A 1 223 ? 9.015   -26.518 8.550   1.00 178.09 ? 223 LYS A CG  1 
ATOM   1674 C CD  . LYS A 1 223 ? 9.133   -25.636 9.789   1.00 204.72 ? 223 LYS A CD  1 
ATOM   1675 C CE  . LYS A 1 223 ? 9.548   -26.252 11.094  1.00 186.85 ? 223 LYS A CE  1 
ATOM   1676 N NZ  . LYS A 1 223 ? 9.387   -25.218 12.121  1.00 201.94 ? 223 LYS A NZ  1 
ATOM   1677 N N   . LEU A 1 224 ? 13.520  -27.576 7.346   1.00 197.26 ? 224 LEU A N   1 
ATOM   1678 C CA  . LEU A 1 224 ? 14.677  -28.446 7.264   1.00 209.46 ? 224 LEU A CA  1 
ATOM   1679 C C   . LEU A 1 224 ? 15.750  -27.919 8.219   1.00 206.56 ? 224 LEU A C   1 
ATOM   1680 O O   . LEU A 1 224 ? 16.347  -28.728 8.966   1.00 179.56 ? 224 LEU A O   1 
ATOM   1681 C CB  . LEU A 1 224 ? 15.142  -28.636 5.818   1.00 210.53 ? 224 LEU A CB  1 
ATOM   1682 C CG  . LEU A 1 224 ? 16.063  -29.834 5.535   1.00 199.36 ? 224 LEU A CG  1 
ATOM   1683 C CD1 . LEU A 1 224 ? 15.578  -31.157 6.108   1.00 217.29 ? 224 LEU A CD1 1 
ATOM   1684 C CD2 . LEU A 1 224 ? 16.297  -29.997 4.040   1.00 167.55 ? 224 LEU A CD2 1 
ATOM   1685 N N   . ARG A 1 225 ? 15.979  -26.590 8.170   1.00 217.60 ? 225 ARG A N   1 
ATOM   1686 C CA  . ARG A 1 225 ? 17.165  -26.022 8.793   1.00 224.74 ? 225 ARG A CA  1 
ATOM   1687 C C   . ARG A 1 225 ? 17.037  -26.183 10.296  1.00 234.50 ? 225 ARG A C   1 
ATOM   1688 O O   . ARG A 1 225 ? 18.005  -26.022 11.017  1.00 246.87 ? 225 ARG A O   1 
ATOM   1689 C CB  . ARG A 1 225 ? 17.407  -24.543 8.473   1.00 224.62 ? 225 ARG A CB  1 
ATOM   1690 C CG  . ARG A 1 225 ? 17.468  -24.206 6.993   1.00 213.69 ? 225 ARG A CG  1 
ATOM   1691 C CD  . ARG A 1 225 ? 18.402  -23.040 6.758   1.00 182.09 ? 225 ARG A CD  1 
ATOM   1692 N NE  . ARG A 1 225 ? 19.771  -23.524 6.964   1.00 181.34 ? 225 ARG A NE  1 
ATOM   1693 C CZ  . ARG A 1 225 ? 20.611  -23.827 5.984   1.00 184.27 ? 225 ARG A CZ  1 
ATOM   1694 N NH1 . ARG A 1 225 ? 20.291  -23.539 4.738   1.00 204.93 ? 225 ARG A NH1 1 
ATOM   1695 N NH2 . ARG A 1 225 ? 21.771  -24.387 6.259   1.00 174.19 ? 225 ARG A NH2 1 
ATOM   1696 N N   . HIS A 1 226 ? 15.829  -26.545 10.725  1.00 248.24 ? 226 HIS A N   1 
ATOM   1697 C CA  . HIS A 1 226 ? 15.492  -26.675 12.128  1.00 254.97 ? 226 HIS A CA  1 
ATOM   1698 C C   . HIS A 1 226 ? 15.453  -28.155 12.502  1.00 272.57 ? 226 HIS A C   1 
ATOM   1699 O O   . HIS A 1 226 ? 15.909  -28.528 13.576  1.00 303.92 ? 226 HIS A O   1 
ATOM   1700 C CB  . HIS A 1 226 ? 14.179  -25.931 12.393  1.00 250.79 ? 226 HIS A CB  1 
ATOM   1701 C CG  . HIS A 1 226 ? 13.700  -25.947 13.795  1.00 252.20 ? 226 HIS A CG  1 
ATOM   1702 N ND1 . HIS A 1 226 ? 12.437  -26.393 14.106  1.00 259.34 ? 226 HIS A ND1 1 
ATOM   1703 C CD2 . HIS A 1 226 ? 14.269  -25.615 14.952  1.00 253.98 ? 226 HIS A CD2 1 
ATOM   1704 C CE1 . HIS A 1 226 ? 12.240  -26.288 15.411  1.00 254.57 ? 226 HIS A CE1 1 
ATOM   1705 N NE2 . HIS A 1 226 ? 13.343  -25.819 15.947  1.00 254.89 ? 226 HIS A NE2 1 
ATOM   1706 N N   . THR A 1 227 ? 14.912  -28.988 11.600  1.00 265.67 ? 227 THR A N   1 
ATOM   1707 C CA  . THR A 1 227 ? 14.761  -30.421 11.814  1.00 253.37 ? 227 THR A CA  1 
ATOM   1708 C C   . THR A 1 227 ? 15.371  -31.157 10.623  1.00 226.51 ? 227 THR A C   1 
ATOM   1709 O O   . THR A 1 227 ? 14.859  -31.071 9.508   1.00 269.40 ? 227 THR A O   1 
ATOM   1710 C CB  . THR A 1 227 ? 13.273  -30.751 11.973  1.00 293.45 ? 227 THR A CB  1 
ATOM   1711 O OG1 . THR A 1 227 ? 12.665  -30.719 10.687  1.00 306.35 ? 227 THR A OG1 1 
ATOM   1712 C CG2 . THR A 1 227 ? 12.516  -29.730 12.801  1.00 295.45 ? 227 THR A CG2 1 
ATOM   1713 N N   . GLY A 1 228 ? 16.435  -31.923 10.872  1.00 184.61 ? 228 GLY A N   1 
ATOM   1714 C CA  . GLY A 1 228 ? 17.274  -32.448 9.805   1.00 186.51 ? 228 GLY A CA  1 
ATOM   1715 C C   . GLY A 1 228 ? 16.587  -33.364 8.779   1.00 201.04 ? 228 GLY A C   1 
ATOM   1716 O O   . GLY A 1 228 ? 17.159  -33.609 7.721   1.00 190.91 ? 228 GLY A O   1 
ATOM   1717 N N   . ASP A 1 229 ? 15.378  -33.871 9.067   1.00 228.79 ? 229 ASP A N   1 
ATOM   1718 C CA  . ASP A 1 229 ? 14.779  -34.951 8.279   1.00 228.11 ? 229 ASP A CA  1 
ATOM   1719 C C   . ASP A 1 229 ? 13.905  -34.439 7.128   1.00 217.76 ? 229 ASP A C   1 
ATOM   1720 O O   . ASP A 1 229 ? 13.083  -33.541 7.324   1.00 249.31 ? 229 ASP A O   1 
ATOM   1721 C CB  . ASP A 1 229 ? 14.052  -35.961 9.158   1.00 239.62 ? 229 ASP A CB  1 
ATOM   1722 C CG  . ASP A 1 229 ? 13.039  -35.394 10.146  1.00 262.41 ? 229 ASP A CG  1 
ATOM   1723 O OD1 . ASP A 1 229 ? 13.081  -34.170 10.412  1.00 294.31 ? 229 ASP A OD1 1 
ATOM   1724 O OD2 . ASP A 1 229 ? 12.204  -36.182 10.635  1.00 266.49 ? 229 ASP A OD2 1 
ATOM   1725 N N   . LEU A 1 230 ? 14.074  -35.050 5.940   1.00 177.08 ? 230 LEU A N   1 
ATOM   1726 C CA  . LEU A 1 230 ? 13.339  -34.718 4.721   1.00 164.26 ? 230 LEU A CA  1 
ATOM   1727 C C   . LEU A 1 230 ? 11.831  -34.765 4.935   1.00 172.16 ? 230 LEU A C   1 
ATOM   1728 O O   . LEU A 1 230 ? 11.118  -33.882 4.461   1.00 180.08 ? 230 LEU A O   1 
ATOM   1729 C CB  . LEU A 1 230 ? 13.658  -35.581 3.502   1.00 154.68 ? 230 LEU A CB  1 
ATOM   1730 C CG  . LEU A 1 230 ? 14.599  -35.002 2.443   1.00 162.55 ? 230 LEU A CG  1 
ATOM   1731 C CD1 . LEU A 1 230 ? 14.623  -33.488 2.287   1.00 152.48 ? 230 LEU A CD1 1 
ATOM   1732 C CD2 . LEU A 1 230 ? 15.961  -35.548 2.737   1.00 185.72 ? 230 LEU A CD2 1 
ATOM   1733 N N   . VAL A 1 231 ? 11.351  -35.841 5.563   1.00 164.54 ? 231 VAL A N   1 
ATOM   1734 C CA  . VAL A 1 231 ? 9.919   -36.095 5.595   1.00 155.48 ? 231 VAL A CA  1 
ATOM   1735 C C   . VAL A 1 231 ? 9.338   -35.472 6.867   1.00 163.01 ? 231 VAL A C   1 
ATOM   1736 O O   . VAL A 1 231 ? 8.169   -35.662 7.206   1.00 160.26 ? 231 VAL A O   1 
ATOM   1737 C CB  . VAL A 1 231 ? 9.578   -37.590 5.434   1.00 150.98 ? 231 VAL A CB  1 
ATOM   1738 C CG1 . VAL A 1 231 ? 8.080   -37.809 5.290   1.00 148.87 ? 231 VAL A CG1 1 
ATOM   1739 C CG2 . VAL A 1 231 ? 10.301  -38.218 4.246   1.00 155.79 ? 231 VAL A CG2 1 
ATOM   1740 N N   . GLY A 1 232 ? 10.187  -34.731 7.583   1.00 180.61 ? 232 GLY A N   1 
ATOM   1741 C CA  . GLY A 1 232 ? 9.766   -33.925 8.715   1.00 188.46 ? 232 GLY A CA  1 
ATOM   1742 C C   . GLY A 1 232 ? 9.410   -32.514 8.262   1.00 190.32 ? 232 GLY A C   1 
ATOM   1743 O O   . GLY A 1 232 ? 8.659   -31.818 8.943   1.00 206.03 ? 232 GLY A O   1 
ATOM   1744 N N   . SER A 1 233 ? 9.962   -32.114 7.110   1.00 173.72 ? 233 SER A N   1 
ATOM   1745 C CA  . SER A 1 233 ? 9.817   -30.768 6.582   1.00 186.71 ? 233 SER A CA  1 
ATOM   1746 C C   . SER A 1 233 ? 9.047   -30.759 5.261   1.00 176.23 ? 233 SER A C   1 
ATOM   1747 O O   . SER A 1 233 ? 9.050   -29.754 4.539   1.00 177.12 ? 233 SER A O   1 
ATOM   1748 C CB  . SER A 1 233 ? 11.167  -30.113 6.439   1.00 182.59 ? 233 SER A CB  1 
ATOM   1749 O OG  . SER A 1 233 ? 12.086  -30.970 5.782   1.00 162.95 ? 233 SER A OG  1 
ATOM   1750 N N   . ALA A 1 234 ? 8.380   -31.879 4.954   1.00 153.18 ? 234 ALA A N   1 
ATOM   1751 C CA  . ALA A 1 234 ? 7.650   -31.997 3.702   1.00 151.22 ? 234 ALA A CA  1 
ATOM   1752 C C   . ALA A 1 234 ? 6.355   -31.194 3.789   1.00 162.78 ? 234 ALA A C   1 
ATOM   1753 O O   . ALA A 1 234 ? 5.532   -31.416 4.679   1.00 164.52 ? 234 ALA A O   1 
ATOM   1754 C CB  . ALA A 1 234 ? 7.400   -33.452 3.354   1.00 154.81 ? 234 ALA A CB  1 
ATOM   1755 N N   . GLU A 1 235 ? 6.214   -30.225 2.875   1.00 156.26 ? 235 GLU A N   1 
ATOM   1756 C CA  . GLU A 1 235 ? 4.995   -29.448 2.749   1.00 143.34 ? 235 GLU A CA  1 
ATOM   1757 C C   . GLU A 1 235 ? 4.031   -30.162 1.810   1.00 150.92 ? 235 GLU A C   1 
ATOM   1758 O O   . GLU A 1 235 ? 2.824   -30.004 1.939   1.00 181.96 ? 235 GLU A O   1 
ATOM   1759 C CB  . GLU A 1 235 ? 5.255   -28.059 2.173   1.00 150.21 ? 235 GLU A CB  1 
ATOM   1760 C CG  . GLU A 1 235 ? 5.517   -26.969 3.211   1.00 152.87 ? 235 GLU A CG  1 
ATOM   1761 C CD  . GLU A 1 235 ? 5.534   -25.598 2.543   1.00 184.22 ? 235 GLU A CD  1 
ATOM   1762 O OE1 . GLU A 1 235 ? 5.217   -25.549 1.334   1.00 173.67 ? 235 GLU A OE1 1 
ATOM   1763 O OE2 . GLU A 1 235 ? 5.882   -24.592 3.217   1.00 220.14 ? 235 GLU A OE2 1 
ATOM   1764 N N   . VAL A 1 236 ? 4.573   -30.911 0.843   1.00 153.89 ? 236 VAL A N   1 
ATOM   1765 C CA  . VAL A 1 236 ? 3.741   -31.733 -0.022  1.00 161.08 ? 236 VAL A CA  1 
ATOM   1766 C C   . VAL A 1 236 ? 4.445   -33.058 -0.319  1.00 181.15 ? 236 VAL A C   1 
ATOM   1767 O O   . VAL A 1 236 ? 5.366   -33.098 -1.127  1.00 192.19 ? 236 VAL A O   1 
ATOM   1768 C CB  . VAL A 1 236 ? 3.288   -31.044 -1.320  1.00 133.08 ? 236 VAL A CB  1 
ATOM   1769 C CG1 . VAL A 1 236 ? 2.215   -31.876 -2.006  1.00 129.17 ? 236 VAL A CG1 1 
ATOM   1770 C CG2 . VAL A 1 236 ? 2.736   -29.656 -1.053  1.00 154.42 ? 236 VAL A CG2 1 
ATOM   1771 N N   . ILE A 1 237 ? 4.011   -34.132 0.352   1.00 176.02 ? 237 ILE A N   1 
ATOM   1772 C CA  . ILE A 1 237 ? 4.429   -35.479 0.004   1.00 161.44 ? 237 ILE A CA  1 
ATOM   1773 C C   . ILE A 1 237 ? 3.179   -36.307 -0.278  1.00 153.49 ? 237 ILE A C   1 
ATOM   1774 O O   . ILE A 1 237 ? 2.256   -36.346 0.536   1.00 159.69 ? 237 ILE A O   1 
ATOM   1775 C CB  . ILE A 1 237 ? 5.327   -36.096 1.095   1.00 171.93 ? 237 ILE A CB  1 
ATOM   1776 C CG1 . ILE A 1 237 ? 5.842   -37.473 0.663   1.00 187.07 ? 237 ILE A CG1 1 
ATOM   1777 C CG2 . ILE A 1 237 ? 4.627   -36.134 2.456   1.00 169.98 ? 237 ILE A CG2 1 
ATOM   1778 C CD1 . ILE A 1 237 ? 7.012   -37.991 1.480   1.00 212.17 ? 237 ILE A CD1 1 
ATOM   1779 N N   . ARG A 1 238 ? 3.155   -36.944 -1.453  1.00 140.93 ? 238 ARG A N   1 
ATOM   1780 C CA  . ARG A 1 238 ? 1.985   -37.709 -1.857  1.00 148.84 ? 238 ARG A CA  1 
ATOM   1781 C C   . ARG A 1 238 ? 2.315   -39.200 -1.850  1.00 166.18 ? 238 ARG A C   1 
ATOM   1782 O O   . ARG A 1 238 ? 1.456   -40.036 -2.104  1.00 157.98 ? 238 ARG A O   1 
ATOM   1783 C CB  . ARG A 1 238 ? 1.408   -37.138 -3.151  1.00 141.89 ? 238 ARG A CB  1 
ATOM   1784 C CG  . ARG A 1 238 ? 1.468   -35.623 -3.011  1.00 149.84 ? 238 ARG A CG  1 
ATOM   1785 C CD  . ARG A 1 238 ? 0.154   -34.906 -3.247  1.00 175.32 ? 238 ARG A CD  1 
ATOM   1786 N NE  . ARG A 1 238 ? -0.307  -34.995 -4.633  1.00 206.22 ? 238 ARG A NE  1 
ATOM   1787 C CZ  . ARG A 1 238 ? 0.278   -34.500 -5.724  1.00 221.46 ? 238 ARG A CZ  1 
ATOM   1788 N NH1 . ARG A 1 238 ? 1.449   -33.877 -5.690  1.00 186.57 ? 238 ARG A NH1 1 
ATOM   1789 N NH2 . ARG A 1 238 ? -0.340  -34.645 -6.882  1.00 257.25 ? 238 ARG A NH2 1 
ATOM   1790 N N   . LEU A 1 239 ? 3.562   -39.507 -1.478  1.00 177.37 ? 239 LEU A N   1 
ATOM   1791 C CA  . LEU A 1 239 ? 4.007   -40.871 -1.270  1.00 156.64 ? 239 LEU A CA  1 
ATOM   1792 C C   . LEU A 1 239 ? 3.940   -41.236 0.208   1.00 168.07 ? 239 LEU A C   1 
ATOM   1793 O O   . LEU A 1 239 ? 4.264   -40.422 1.077   1.00 169.69 ? 239 LEU A O   1 
ATOM   1794 C CB  . LEU A 1 239 ? 5.426   -40.999 -1.809  1.00 143.78 ? 239 LEU A CB  1 
ATOM   1795 C CG  . LEU A 1 239 ? 5.494   -41.344 -3.293  1.00 147.32 ? 239 LEU A CG  1 
ATOM   1796 C CD1 . LEU A 1 239 ? 6.919   -41.480 -3.776  1.00 175.80 ? 239 LEU A CD1 1 
ATOM   1797 C CD2 . LEU A 1 239 ? 4.745   -42.656 -3.422  1.00 147.17 ? 239 LEU A CD2 1 
ATOM   1798 N N   . PRO A 1 240 ? 3.511   -42.478 0.531   1.00 174.37 ? 240 PRO A N   1 
ATOM   1799 C CA  . PRO A 1 240 ? 3.758   -43.052 1.856   1.00 164.38 ? 240 PRO A CA  1 
ATOM   1800 C C   . PRO A 1 240 ? 5.254   -42.890 2.106   1.00 152.59 ? 240 PRO A C   1 
ATOM   1801 O O   . PRO A 1 240 ? 6.077   -43.184 1.235   1.00 136.08 ? 240 PRO A O   1 
ATOM   1802 C CB  . PRO A 1 240 ? 3.322   -44.517 1.730   1.00 157.15 ? 240 PRO A CB  1 
ATOM   1803 C CG  . PRO A 1 240 ? 2.300   -44.483 0.612   1.00 173.59 ? 240 PRO A CG  1 
ATOM   1804 C CD  . PRO A 1 240 ? 2.743   -43.374 -0.349  1.00 179.05 ? 240 PRO A CD  1 
ATOM   1805 N N   . ALA A 1 241 ? 5.585   -42.368 3.289   1.00 152.62 ? 241 ALA A N   1 
ATOM   1806 C CA  . ALA A 1 241 ? 6.941   -41.928 3.572   1.00 155.83 ? 241 ALA A CA  1 
ATOM   1807 C C   . ALA A 1 241 ? 7.931   -43.036 3.230   1.00 159.28 ? 241 ALA A C   1 
ATOM   1808 O O   . ALA A 1 241 ? 8.982   -42.794 2.636   1.00 149.76 ? 241 ALA A O   1 
ATOM   1809 C CB  . ALA A 1 241 ? 7.035   -41.540 5.029   1.00 166.96 ? 241 ALA A CB  1 
ATOM   1810 N N   . GLU A 1 242 ? 7.590   -44.242 3.687   1.00 175.33 ? 242 GLU A N   1 
ATOM   1811 C CA  . GLU A 1 242 ? 8.415   -45.431 3.548   1.00 176.15 ? 242 GLU A CA  1 
ATOM   1812 C C   . GLU A 1 242 ? 8.712   -45.681 2.073   1.00 175.71 ? 242 GLU A C   1 
ATOM   1813 O O   . GLU A 1 242 ? 9.868   -45.931 1.694   1.00 189.20 ? 242 GLU A O   1 
ATOM   1814 C CB  . GLU A 1 242 ? 7.577   -46.583 4.110   1.00 198.80 ? 242 GLU A CB  1 
ATOM   1815 C CG  . GLU A 1 242 ? 7.601   -47.879 3.297   1.00 221.06 ? 242 GLU A CG  1 
ATOM   1816 C CD  . GLU A 1 242 ? 8.853   -48.712 3.440   1.00 252.28 ? 242 GLU A CD  1 
ATOM   1817 O OE1 . GLU A 1 242 ? 9.073   -49.138 4.591   1.00 251.14 ? 242 GLU A OE1 1 
ATOM   1818 O OE2 . GLU A 1 242 ? 9.577   -48.958 2.448   1.00 291.90 ? 242 GLU A OE2 1 
ATOM   1819 N N   . GLU A 1 243 ? 7.641   -45.609 1.270   1.00 174.39 ? 243 GLU A N   1 
ATOM   1820 C CA  . GLU A 1 243 ? 7.752   -45.863 -0.165  1.00 157.28 ? 243 GLU A CA  1 
ATOM   1821 C C   . GLU A 1 243 ? 8.700   -44.852 -0.801  1.00 167.19 ? 243 GLU A C   1 
ATOM   1822 O O   . GLU A 1 243 ? 9.556   -45.230 -1.614  1.00 186.50 ? 243 GLU A O   1 
ATOM   1823 C CB  . GLU A 1 243 ? 6.423   -46.043 -0.890  1.00 144.99 ? 243 GLU A CB  1 
ATOM   1824 C CG  . GLU A 1 243 ? 6.590   -46.476 -2.343  1.00 137.82 ? 243 GLU A CG  1 
ATOM   1825 C CD  . GLU A 1 243 ? 5.237   -46.553 -3.044  1.00 175.37 ? 243 GLU A CD  1 
ATOM   1826 O OE1 . GLU A 1 243 ? 4.211   -46.387 -2.349  1.00 200.13 ? 243 GLU A OE1 1 
ATOM   1827 O OE2 . GLU A 1 243 ? 5.151   -46.757 -4.273  1.00 204.13 ? 243 GLU A OE2 1 
ATOM   1828 N N   . PHE A 1 244 ? 8.538   -43.587 -0.399  1.00 158.48 ? 244 PHE A N   1 
ATOM   1829 C CA  . PHE A 1 244 ? 9.365   -42.488 -0.890  1.00 166.85 ? 244 PHE A CA  1 
ATOM   1830 C C   . PHE A 1 244 ? 10.838  -42.774 -0.594  1.00 172.69 ? 244 PHE A C   1 
ATOM   1831 O O   . PHE A 1 244 ? 11.710  -42.615 -1.465  1.00 173.97 ? 244 PHE A O   1 
ATOM   1832 C CB  . PHE A 1 244 ? 8.962   -41.108 -0.337  1.00 166.22 ? 244 PHE A CB  1 
ATOM   1833 C CG  . PHE A 1 244 ? 10.012  -40.007 -0.512  1.00 162.69 ? 244 PHE A CG  1 
ATOM   1834 C CD1 . PHE A 1 244 ? 10.559  -39.730 -1.763  1.00 148.07 ? 244 PHE A CD1 1 
ATOM   1835 C CD2 . PHE A 1 244 ? 10.513  -39.301 0.590   1.00 163.33 ? 244 PHE A CD2 1 
ATOM   1836 C CE1 . PHE A 1 244 ? 11.554  -38.774 -1.912  1.00 155.40 ? 244 PHE A CE1 1 
ATOM   1837 C CE2 . PHE A 1 244 ? 11.519  -38.356 0.439   1.00 151.85 ? 244 PHE A CE2 1 
ATOM   1838 C CZ  . PHE A 1 244 ? 12.027  -38.083 -0.814  1.00 154.91 ? 244 PHE A CZ  1 
ATOM   1839 N N   . ARG A 1 245 ? 11.076  -43.191 0.652   1.00 178.36 ? 245 ARG A N   1 
ATOM   1840 C CA  . ARG A 1 245 ? 12.415  -43.501 1.141   1.00 179.38 ? 245 ARG A CA  1 
ATOM   1841 C C   . ARG A 1 245 ? 13.044  -44.595 0.279   1.00 178.32 ? 245 ARG A C   1 
ATOM   1842 O O   . ARG A 1 245 ? 14.208  -44.489 -0.139  1.00 176.38 ? 245 ARG A O   1 
ATOM   1843 C CB  . ARG A 1 245 ? 12.444  -43.842 2.637   1.00 181.16 ? 245 ARG A CB  1 
ATOM   1844 C CG  . ARG A 1 245 ? 12.229  -42.691 3.608   1.00 174.94 ? 245 ARG A CG  1 
ATOM   1845 C CD  . ARG A 1 245 ? 12.435  -43.096 5.065   1.00 175.79 ? 245 ARG A CD  1 
ATOM   1846 N NE  . ARG A 1 245 ? 12.495  -41.976 6.016   1.00 177.69 ? 245 ARG A NE  1 
ATOM   1847 C CZ  . ARG A 1 245 ? 11.455  -41.343 6.554   1.00 201.44 ? 245 ARG A CZ  1 
ATOM   1848 N NH1 . ARG A 1 245 ? 10.227  -41.752 6.305   1.00 221.97 ? 245 ARG A NH1 1 
ATOM   1849 N NH2 . ARG A 1 245 ? 11.645  -40.310 7.355   1.00 207.06 ? 245 ARG A NH2 1 
ATOM   1850 N N   . ARG A 1 246 ? 12.239  -45.631 0.034   1.00 178.88 ? 246 ARG A N   1 
ATOM   1851 C CA  . ARG A 1 246 ? 12.652  -46.785 -0.760  1.00 175.73 ? 246 ARG A CA  1 
ATOM   1852 C C   . ARG A 1 246 ? 13.073  -46.329 -2.158  1.00 171.59 ? 246 ARG A C   1 
ATOM   1853 O O   . ARG A 1 246 ? 14.121  -46.745 -2.673  1.00 183.19 ? 246 ARG A O   1 
ATOM   1854 C CB  . ARG A 1 246 ? 11.635  -47.942 -0.695  1.00 198.47 ? 246 ARG A CB  1 
ATOM   1855 C CG  . ARG A 1 246 ? 11.239  -48.560 -2.033  1.00 203.27 ? 246 ARG A CG  1 
ATOM   1856 C CD  . ARG A 1 246 ? 10.564  -49.922 -2.011  1.00 189.79 ? 246 ARG A CD  1 
ATOM   1857 N NE  . ARG A 1 246 ? 9.163   -49.807 -1.595  1.00 186.03 ? 246 ARG A NE  1 
ATOM   1858 C CZ  . ARG A 1 246 ? 8.694   -50.213 -0.421  1.00 202.39 ? 246 ARG A CZ  1 
ATOM   1859 N NH1 . ARG A 1 246 ? 9.488   -50.815 0.448   1.00 192.22 ? 246 ARG A NH1 1 
ATOM   1860 N NH2 . ARG A 1 246 ? 7.425   -50.010 -0.114  1.00 228.49 ? 246 ARG A NH2 1 
ATOM   1861 N N   . GLU A 1 247 ? 12.229  -45.472 -2.736  1.00 165.88 ? 247 GLU A N   1 
ATOM   1862 C CA  . GLU A 1 247 ? 12.451  -44.934 -4.073  1.00 165.05 ? 247 GLU A CA  1 
ATOM   1863 C C   . GLU A 1 247 ? 13.785  -44.190 -4.125  1.00 158.30 ? 247 GLU A C   1 
ATOM   1864 O O   . GLU A 1 247 ? 14.577  -44.370 -5.060  1.00 144.64 ? 247 GLU A O   1 
ATOM   1865 C CB  . GLU A 1 247 ? 11.258  -44.217 -4.703  1.00 171.20 ? 247 GLU A CB  1 
ATOM   1866 C CG  . GLU A 1 247 ? 11.499  -43.893 -6.176  1.00 182.84 ? 247 GLU A CG  1 
ATOM   1867 C CD  . GLU A 1 247 ? 11.510  -44.998 -7.214  1.00 177.45 ? 247 GLU A CD  1 
ATOM   1868 O OE1 . GLU A 1 247 ? 11.296  -46.180 -6.865  1.00 179.82 ? 247 GLU A OE1 1 
ATOM   1869 O OE2 . GLU A 1 247 ? 11.728  -44.641 -8.390  1.00 170.37 ? 247 GLU A OE2 1 
ATOM   1870 N N   . LEU A 1 248 ? 13.999  -43.366 -3.098  1.00 157.48 ? 248 LEU A N   1 
ATOM   1871 C CA  . LEU A 1 248 ? 15.212  -42.567 -2.966  1.00 139.34 ? 248 LEU A CA  1 
ATOM   1872 C C   . LEU A 1 248 ? 16.438  -43.476 -2.944  1.00 170.62 ? 248 LEU A C   1 
ATOM   1873 O O   . LEU A 1 248 ? 17.436  -43.221 -3.635  1.00 204.02 ? 248 LEU A O   1 
ATOM   1874 C CB  . LEU A 1 248 ? 15.128  -41.693 -1.719  1.00 125.56 ? 248 LEU A CB  1 
ATOM   1875 C CG  . LEU A 1 248 ? 15.888  -40.370 -1.797  1.00 126.57 ? 248 LEU A CG  1 
ATOM   1876 C CD1 . LEU A 1 248 ? 15.669  -39.667 -3.144  1.00 112.73 ? 248 LEU A CD1 1 
ATOM   1877 C CD2 . LEU A 1 248 ? 15.407  -39.547 -0.620  1.00 145.75 ? 248 LEU A CD2 1 
ATOM   1878 N N   . ALA A 1 249 ? 16.324  -44.538 -2.141  1.00 200.69 ? 249 ALA A N   1 
ATOM   1879 C CA  . ALA A 1 249 ? 17.391  -45.513 -1.961  1.00 201.96 ? 249 ALA A CA  1 
ATOM   1880 C C   . ALA A 1 249 ? 17.739  -46.145 -3.313  1.00 190.70 ? 249 ALA A C   1 
ATOM   1881 O O   . ALA A 1 249 ? 18.927  -46.265 -3.676  1.00 174.03 ? 249 ALA A O   1 
ATOM   1882 C CB  . ALA A 1 249 ? 16.989  -46.570 -0.947  1.00 203.55 ? 249 ALA A CB  1 
ATOM   1883 N N   . GLU A 1 250 ? 16.683  -46.520 -4.051  1.00 186.73 ? 250 GLU A N   1 
ATOM   1884 C CA  . GLU A 1 250 ? 16.835  -47.523 -5.105  1.00 177.52 ? 250 GLU A CA  1 
ATOM   1885 C C   . GLU A 1 250 ? 16.962  -46.856 -6.465  1.00 177.63 ? 250 GLU A C   1 
ATOM   1886 O O   . GLU A 1 250 ? 17.744  -47.308 -7.287  1.00 195.08 ? 250 GLU A O   1 
ATOM   1887 C CB  . GLU A 1 250 ? 15.732  -48.578 -5.030  1.00 174.02 ? 250 GLU A CB  1 
ATOM   1888 C CG  . GLU A 1 250 ? 15.875  -49.520 -3.838  1.00 182.19 ? 250 GLU A CG  1 
ATOM   1889 C CD  . GLU A 1 250 ? 14.590  -50.267 -3.507  1.00 202.38 ? 250 GLU A CD  1 
ATOM   1890 O OE1 . GLU A 1 250 ? 13.897  -50.752 -4.439  1.00 183.52 ? 250 GLU A OE1 1 
ATOM   1891 O OE2 . GLU A 1 250 ? 14.269  -50.342 -2.295  1.00 225.65 ? 250 GLU A OE2 1 
ATOM   1892 N N   . GLN A 1 251 ? 16.195  -45.785 -6.676  1.00 183.43 ? 251 GLN A N   1 
ATOM   1893 C CA  . GLN A 1 251 ? 16.192  -45.078 -7.945  1.00 197.33 ? 251 GLN A CA  1 
ATOM   1894 C C   . GLN A 1 251 ? 16.720  -43.665 -7.740  1.00 194.26 ? 251 GLN A C   1 
ATOM   1895 O O   . GLN A 1 251 ? 17.413  -43.124 -8.604  1.00 185.16 ? 251 GLN A O   1 
ATOM   1896 C CB  . GLN A 1 251 ? 14.796  -44.963 -8.556  1.00 206.40 ? 251 GLN A CB  1 
ATOM   1897 C CG  . GLN A 1 251 ? 14.313  -46.224 -9.266  1.00 218.97 ? 251 GLN A CG  1 
ATOM   1898 C CD  . GLN A 1 251 ? 15.127  -46.635 -10.473 1.00 217.52 ? 251 GLN A CD  1 
ATOM   1899 O OE1 . GLN A 1 251 ? 16.132  -46.005 -10.831 1.00 191.89 ? 251 GLN A OE1 1 
ATOM   1900 N NE2 . GLN A 1 251 ? 14.687  -47.716 -11.104 1.00 232.49 ? 251 GLN A NE2 1 
ATOM   1901 N N   . GLY A 1 252 ? 16.342  -43.089 -6.591  1.00 181.30 ? 252 GLY A N   1 
ATOM   1902 C CA  . GLY A 1 252 ? 16.740  -41.741 -6.217  1.00 159.81 ? 252 GLY A CA  1 
ATOM   1903 C C   . GLY A 1 252 ? 15.911  -40.625 -6.863  1.00 156.13 ? 252 GLY A C   1 
ATOM   1904 O O   . GLY A 1 252 ? 14.913  -40.835 -7.578  1.00 158.27 ? 252 GLY A O   1 
ATOM   1905 N N   . ALA A 1 253 ? 16.366  -39.400 -6.578  1.00 150.03 ? 253 ALA A N   1 
ATOM   1906 C CA  . ALA A 1 253 ? 15.696  -38.182 -6.968  1.00 157.75 ? 253 ALA A CA  1 
ATOM   1907 C C   . ALA A 1 253 ? 16.747  -37.226 -7.515  1.00 157.29 ? 253 ALA A C   1 
ATOM   1908 O O   . ALA A 1 253 ? 17.933  -37.505 -7.605  1.00 181.01 ? 253 ALA A O   1 
ATOM   1909 C CB  . ALA A 1 253 ? 14.951  -37.610 -5.782  1.00 158.49 ? 253 ALA A CB  1 
ATOM   1910 N N   . ILE A 1 254 ? 16.258  -36.049 -7.882  1.00 136.87 ? 254 ILE A N   1 
ATOM   1911 C CA  . ILE A 1 254 ? 17.021  -34.936 -8.414  1.00 119.01 ? 254 ILE A CA  1 
ATOM   1912 C C   . ILE A 1 254 ? 16.420  -33.694 -7.781  1.00 116.84 ? 254 ILE A C   1 
ATOM   1913 O O   . ILE A 1 254 ? 15.185  -33.563 -7.644  1.00 133.78 ? 254 ILE A O   1 
ATOM   1914 C CB  . ILE A 1 254 ? 17.001  -34.863 -9.961  1.00 119.20 ? 254 ILE A CB  1 
ATOM   1915 C CG1 . ILE A 1 254 ? 16.108  -33.747 -10.544 1.00 118.95 ? 254 ILE A CG1 1 
ATOM   1916 C CG2 . ILE A 1 254 ? 16.727  -36.214 -10.610 1.00 127.57 ? 254 ILE A CG2 1 
ATOM   1917 C CD1 . ILE A 1 254 ? 16.125  -33.629 -12.061 1.00 117.80 ? 254 ILE A CD1 1 
ATOM   1918 N N   . VAL A 1 255 ? 17.287  -32.688 -7.551  1.00 113.18 ? 255 VAL A N   1 
ATOM   1919 C CA  . VAL A 1 255 ? 16.877  -31.516 -6.777  1.00 117.19 ? 255 VAL A CA  1 
ATOM   1920 C C   . VAL A 1 255 ? 16.788  -30.225 -7.605  1.00 125.48 ? 255 VAL A C   1 
ATOM   1921 O O   . VAL A 1 255 ? 17.710  -29.842 -8.309  1.00 127.58 ? 255 VAL A O   1 
ATOM   1922 C CB  . VAL A 1 255 ? 17.489  -31.428 -5.366  1.00 100.92 ? 255 VAL A CB  1 
ATOM   1923 C CG1 . VAL A 1 255 ? 16.970  -30.214 -4.597  1.00 85.78  ? 255 VAL A CG1 1 
ATOM   1924 C CG2 . VAL A 1 255 ? 17.235  -32.733 -4.591  1.00 91.51  ? 255 VAL A CG2 1 
ATOM   1925 N N   . GLU A 1 256 ? 15.580  -29.656 -7.588  1.00 132.99 ? 256 GLU A N   1 
ATOM   1926 C CA  . GLU A 1 256 ? 15.217  -28.475 -8.345  1.00 134.73 ? 256 GLU A CA  1 
ATOM   1927 C C   . GLU A 1 256 ? 14.527  -27.459 -7.445  1.00 136.06 ? 256 GLU A C   1 
ATOM   1928 O O   . GLU A 1 256 ? 13.690  -27.748 -6.567  1.00 130.86 ? 256 GLU A O   1 
ATOM   1929 C CB  . GLU A 1 256 ? 14.256  -28.708 -9.511  1.00 139.55 ? 256 GLU A CB  1 
ATOM   1930 C CG  . GLU A 1 256 ? 14.895  -29.474 -10.663 1.00 185.97 ? 256 GLU A CG  1 
ATOM   1931 C CD  . GLU A 1 256 ? 14.088  -29.427 -11.951 1.00 218.97 ? 256 GLU A CD  1 
ATOM   1932 O OE1 . GLU A 1 256 ? 12.915  -29.851 -11.965 1.00 215.35 ? 256 GLU A OE1 1 
ATOM   1933 O OE2 . GLU A 1 256 ? 14.644  -28.960 -12.962 1.00 268.76 ? 256 GLU A OE2 1 
ATOM   1934 N N   . GLU A 1 257 ? 14.799  -26.200 -7.784  1.00 137.29 ? 257 GLU A N   1 
ATOM   1935 C CA  . GLU A 1 257 ? 14.208  -25.068 -7.097  1.00 149.77 ? 257 GLU A CA  1 
ATOM   1936 C C   . GLU A 1 257 ? 12.750  -24.890 -7.513  1.00 151.85 ? 257 GLU A C   1 
ATOM   1937 O O   . GLU A 1 257 ? 12.405  -24.932 -8.697  1.00 147.91 ? 257 GLU A O   1 
ATOM   1938 C CB  . GLU A 1 257 ? 15.005  -23.795 -7.379  1.00 162.65 ? 257 GLU A CB  1 
ATOM   1939 C CG  . GLU A 1 257 ? 15.171  -23.487 -8.864  1.00 163.25 ? 257 GLU A CG  1 
ATOM   1940 C CD  . GLU A 1 257 ? 15.562  -22.047 -9.133  1.00 166.50 ? 257 GLU A CD  1 
ATOM   1941 O OE1 . GLU A 1 257 ? 15.412  -21.185 -8.231  1.00 154.21 ? 257 GLU A OE1 1 
ATOM   1942 O OE2 . GLU A 1 257 ? 16.022  -21.796 -10.269 1.00 163.62 ? 257 GLU A OE2 1 
ATOM   1943 N N   . PHE A 1 258 ? 11.917  -24.626 -6.503  1.00 151.07 ? 258 PHE A N   1 
ATOM   1944 C CA  . PHE A 1 258 ? 10.494  -24.408 -6.696  1.00 149.45 ? 258 PHE A CA  1 
ATOM   1945 C C   . PHE A 1 258 ? 10.203  -22.954 -7.074  1.00 140.14 ? 258 PHE A C   1 
ATOM   1946 O O   . PHE A 1 258 ? 10.011  -22.110 -6.201  1.00 148.65 ? 258 PHE A O   1 
ATOM   1947 C CB  . PHE A 1 258 ? 9.754   -24.878 -5.442  1.00 144.26 ? 258 PHE A CB  1 
ATOM   1948 C CG  . PHE A 1 258 ? 8.257   -24.696 -5.582  1.00 131.48 ? 258 PHE A CG  1 
ATOM   1949 C CD1 . PHE A 1 258 ? 7.509   -25.567 -6.361  1.00 139.62 ? 258 PHE A CD1 1 
ATOM   1950 C CD2 . PHE A 1 258 ? 7.622   -23.638 -4.962  1.00 137.73 ? 258 PHE A CD2 1 
ATOM   1951 C CE1 . PHE A 1 258 ? 6.143   -25.387 -6.497  1.00 186.59 ? 258 PHE A CE1 1 
ATOM   1952 C CE2 . PHE A 1 258 ? 6.255   -23.462 -5.110  1.00 189.96 ? 258 PHE A CE2 1 
ATOM   1953 C CZ  . PHE A 1 258 ? 5.518   -24.333 -5.874  1.00 205.79 ? 258 PHE A CZ  1 
ATOM   1954 N N   . LEU A 1 259 ? 10.143  -22.697 -8.388  1.00 123.21 ? 259 LEU A N   1 
ATOM   1955 C CA  . LEU A 1 259 ? 9.730   -21.427 -8.975  1.00 124.76 ? 259 LEU A CA  1 
ATOM   1956 C C   . LEU A 1 259 ? 8.344   -21.053 -8.454  1.00 132.45 ? 259 LEU A C   1 
ATOM   1957 O O   . LEU A 1 259 ? 7.414   -21.848 -8.550  1.00 147.54 ? 259 LEU A O   1 
ATOM   1958 C CB  . LEU A 1 259 ? 9.713   -21.602 -10.491 1.00 122.15 ? 259 LEU A CB  1 
ATOM   1959 C CG  . LEU A 1 259 ? 10.801  -22.521 -11.057 1.00 136.64 ? 259 LEU A CG  1 
ATOM   1960 C CD1 . LEU A 1 259 ? 10.525  -22.867 -12.505 1.00 146.31 ? 259 LEU A CD1 1 
ATOM   1961 C CD2 . LEU A 1 259 ? 12.195  -21.934 -10.914 1.00 155.66 ? 259 LEU A CD2 1 
ATOM   1962 N N   . GLU A 1 260 ? 8.214   -19.846 -7.895  1.00 132.09 ? 260 GLU A N   1 
ATOM   1963 C CA  . GLU A 1 260 ? 7.071   -19.525 -7.058  1.00 129.75 ? 260 GLU A CA  1 
ATOM   1964 C C   . GLU A 1 260 ? 5.899   -19.045 -7.908  1.00 142.50 ? 260 GLU A C   1 
ATOM   1965 O O   . GLU A 1 260 ? 4.792   -19.575 -7.810  1.00 149.93 ? 260 GLU A O   1 
ATOM   1966 C CB  . GLU A 1 260 ? 7.471   -18.458 -6.042  1.00 135.49 ? 260 GLU A CB  1 
ATOM   1967 C CG  . GLU A 1 260 ? 8.363   -18.991 -4.926  1.00 149.41 ? 260 GLU A CG  1 
ATOM   1968 C CD  . GLU A 1 260 ? 7.695   -19.940 -3.941  1.00 155.87 ? 260 GLU A CD  1 
ATOM   1969 O OE1 . GLU A 1 260 ? 6.446   -20.093 -3.958  1.00 140.04 ? 260 GLU A OE1 1 
ATOM   1970 O OE2 . GLU A 1 260 ? 8.459   -20.550 -3.154  1.00 170.26 ? 260 GLU A OE2 1 
ATOM   1971 N N   . GLU A 1 261 ? 6.157   -18.009 -8.710  1.00 147.37 ? 261 GLU A N   1 
ATOM   1972 C CA  . GLU A 1 261 ? 5.096   -17.292 -9.396  1.00 154.80 ? 261 GLU A CA  1 
ATOM   1973 C C   . GLU A 1 261 ? 5.003   -17.806 -10.826 1.00 140.59 ? 261 GLU A C   1 
ATOM   1974 O O   . GLU A 1 261 ? 5.826   -17.428 -11.671 1.00 146.76 ? 261 GLU A O   1 
ATOM   1975 C CB  . GLU A 1 261 ? 5.283   -15.776 -9.280  1.00 192.40 ? 261 GLU A CB  1 
ATOM   1976 C CG  . GLU A 1 261 ? 4.980   -15.232 -7.883  1.00 213.88 ? 261 GLU A CG  1 
ATOM   1977 C CD  . GLU A 1 261 ? 3.550   -15.377 -7.371  1.00 213.17 ? 261 GLU A CD  1 
ATOM   1978 O OE1 . GLU A 1 261 ? 2.627   -14.788 -7.984  1.00 190.66 ? 261 GLU A OE1 1 
ATOM   1979 O OE2 . GLU A 1 261 ? 3.355   -16.073 -6.347  1.00 200.62 ? 261 GLU A OE2 1 
ATOM   1980 N N   . ILE A 1 262 ? 4.034   -18.714 -11.047 1.00 124.05 ? 262 ILE A N   1 
ATOM   1981 C CA  . ILE A 1 262 ? 3.836   -19.350 -12.347 1.00 131.92 ? 262 ILE A CA  1 
ATOM   1982 C C   . ILE A 1 262 ? 2.556   -18.791 -12.976 1.00 136.40 ? 262 ILE A C   1 
ATOM   1983 O O   . ILE A 1 262 ? 1.512   -18.812 -12.338 1.00 149.31 ? 262 ILE A O   1 
ATOM   1984 C CB  . ILE A 1 262 ? 3.852   -20.899 -12.265 1.00 119.93 ? 262 ILE A CB  1 
ATOM   1985 C CG1 . ILE A 1 262 ? 5.100   -21.431 -11.542 1.00 108.07 ? 262 ILE A CG1 1 
ATOM   1986 C CG2 . ILE A 1 262 ? 3.700   -21.536 -13.656 1.00 120.82 ? 262 ILE A CG2 1 
ATOM   1987 C CD1 . ILE A 1 262 ? 5.175   -22.939 -11.382 1.00 100.82 ? 262 ILE A CD1 1 
ATOM   1988 N N   . THR A 1 263 ? 2.652   -18.278 -14.214 1.00 137.14 ? 263 THR A N   1 
ATOM   1989 C CA  . THR A 1 263 ? 1.541   -17.625 -14.895 1.00 144.63 ? 263 THR A CA  1 
ATOM   1990 C C   . THR A 1 263 ? 0.906   -18.569 -15.921 1.00 151.60 ? 263 THR A C   1 
ATOM   1991 O O   . THR A 1 263 ? -0.315  -18.725 -15.942 1.00 174.45 ? 263 THR A O   1 
ATOM   1992 C CB  . THR A 1 263 ? 1.989   -16.301 -15.516 1.00 140.56 ? 263 THR A CB  1 
ATOM   1993 O OG1 . THR A 1 263 ? 2.981   -16.659 -16.462 1.00 139.93 ? 263 THR A OG1 1 
ATOM   1994 C CG2 . THR A 1 263 ? 2.671   -15.357 -14.537 1.00 138.30 ? 263 THR A CG2 1 
ATOM   1995 N N   . ASP A 1 264 ? 1.743   -19.194 -16.759 1.00 149.40 ? 264 ASP A N   1 
ATOM   1996 C CA  . ASP A 1 264 ? 1.344   -20.214 -17.716 1.00 160.63 ? 264 ASP A CA  1 
ATOM   1997 C C   . ASP A 1 264 ? 2.257   -21.444 -17.638 1.00 135.39 ? 264 ASP A C   1 
ATOM   1998 O O   . ASP A 1 264 ? 3.395   -21.400 -17.147 1.00 148.29 ? 264 ASP A O   1 
ATOM   1999 C CB  . ASP A 1 264 ? 1.198   -19.638 -19.118 1.00 189.54 ? 264 ASP A CB  1 
ATOM   2000 C CG  . ASP A 1 264 ? 0.040   -18.666 -19.289 1.00 215.90 ? 264 ASP A CG  1 
ATOM   2001 O OD1 . ASP A 1 264 ? -1.126  -19.116 -19.214 1.00 213.56 ? 264 ASP A OD1 1 
ATOM   2002 O OD2 . ASP A 1 264 ? 0.315   -17.465 -19.473 1.00 240.77 ? 264 ASP A OD2 1 
ATOM   2003 N N   . SER A 1 265 ? 1.719   -22.548 -18.149 1.00 111.49 ? 265 SER A N   1 
ATOM   2004 C CA  . SER A 1 265 ? 2.428   -23.813 -18.262 1.00 118.73 ? 265 SER A CA  1 
ATOM   2005 C C   . SER A 1 265 ? 2.300   -24.380 -19.663 1.00 117.14 ? 265 SER A C   1 
ATOM   2006 O O   . SER A 1 265 ? 1.614   -25.395 -19.828 1.00 127.08 ? 265 SER A O   1 
ATOM   2007 C CB  . SER A 1 265 ? 1.974   -24.810 -17.191 1.00 126.39 ? 265 SER A CB  1 
ATOM   2008 O OG  . SER A 1 265 ? 2.600   -26.092 -17.315 1.00 126.38 ? 265 SER A OG  1 
ATOM   2009 N N   . PRO A 1 266 ? 3.006   -23.798 -20.667 1.00 115.37 ? 266 PRO A N   1 
ATOM   2010 C CA  . PRO A 1 266 ? 2.971   -24.311 -22.042 1.00 115.17 ? 266 PRO A CA  1 
ATOM   2011 C C   . PRO A 1 266 ? 3.665   -25.655 -22.292 1.00 115.69 ? 266 PRO A C   1 
ATOM   2012 O O   . PRO A 1 266 ? 4.530   -26.088 -21.514 1.00 110.85 ? 266 PRO A O   1 
ATOM   2013 C CB  . PRO A 1 266 ? 3.531   -23.186 -22.926 1.00 115.16 ? 266 PRO A CB  1 
ATOM   2014 C CG  . PRO A 1 266 ? 4.354   -22.341 -21.963 1.00 113.82 ? 266 PRO A CG  1 
ATOM   2015 C CD  . PRO A 1 266 ? 3.879   -22.618 -20.534 1.00 109.62 ? 266 PRO A CD  1 
ATOM   2016 N N   . SER A 1 267 ? 3.256   -26.295 -23.397 1.00 130.38 ? 267 SER A N   1 
ATOM   2017 C CA  . SER A 1 267 ? 3.806   -27.571 -23.811 1.00 157.84 ? 267 SER A CA  1 
ATOM   2018 C C   . SER A 1 267 ? 4.220   -27.557 -25.282 1.00 162.61 ? 267 SER A C   1 
ATOM   2019 O O   . SER A 1 267 ? 3.611   -26.922 -26.173 1.00 165.38 ? 267 SER A O   1 
ATOM   2020 C CB  . SER A 1 267 ? 2.940   -28.762 -23.470 1.00 172.51 ? 267 SER A CB  1 
ATOM   2021 O OG  . SER A 1 267 ? 1.775   -28.815 -24.282 1.00 163.66 ? 267 SER A OG  1 
ATOM   2022 N N   . GLY A 1 268 ? 5.261   -28.355 -25.524 1.00 155.62 ? 268 GLY A N   1 
ATOM   2023 C CA  . GLY A 1 268 ? 5.881   -28.513 -26.826 1.00 149.18 ? 268 GLY A CA  1 
ATOM   2024 C C   . GLY A 1 268 ? 6.004   -29.994 -27.180 1.00 136.83 ? 268 GLY A C   1 
ATOM   2025 O O   . GLY A 1 268 ? 6.481   -30.813 -26.389 1.00 124.50 ? 268 GLY A O   1 
ATOM   2026 N N   . LEU A 1 269 ? 5.586   -30.292 -28.418 1.00 130.04 ? 269 LEU A N   1 
ATOM   2027 C CA  . LEU A 1 269 ? 5.415   -31.655 -28.897 1.00 138.21 ? 269 LEU A CA  1 
ATOM   2028 C C   . LEU A 1 269 ? 6.218   -31.892 -30.180 1.00 133.26 ? 269 LEU A C   1 
ATOM   2029 O O   . LEU A 1 269 ? 6.124   -31.123 -31.128 1.00 136.25 ? 269 LEU A O   1 
ATOM   2030 C CB  . LEU A 1 269 ? 3.944   -31.972 -29.154 1.00 144.91 ? 269 LEU A CB  1 
ATOM   2031 C CG  . LEU A 1 269 ? 3.632   -33.453 -29.388 1.00 134.37 ? 269 LEU A CG  1 
ATOM   2032 C CD1 . LEU A 1 269 ? 3.316   -34.189 -28.072 1.00 122.22 ? 269 LEU A CD1 1 
ATOM   2033 C CD2 . LEU A 1 269 ? 2.496   -33.616 -30.376 1.00 131.59 ? 269 LEU A CD2 1 
ATOM   2034 N N   . GLY A 1 270 ? 7.009   -32.960 -30.139 1.00 132.16 ? 270 GLY A N   1 
ATOM   2035 C CA  . GLY A 1 270 ? 8.019   -33.246 -31.132 1.00 144.37 ? 270 GLY A CA  1 
ATOM   2036 C C   . GLY A 1 270 ? 7.957   -34.705 -31.577 1.00 144.07 ? 270 GLY A C   1 
ATOM   2037 O O   . GLY A 1 270 ? 7.737   -35.655 -30.806 1.00 125.29 ? 270 GLY A O   1 
ATOM   2038 N N   . HIS A 1 271 ? 8.252   -34.863 -32.867 1.00 159.46 ? 271 HIS A N   1 
ATOM   2039 C CA  . HIS A 1 271 ? 8.362   -36.150 -33.543 1.00 174.87 ? 271 HIS A CA  1 
ATOM   2040 C C   . HIS A 1 271 ? 9.711   -36.255 -34.264 1.00 187.97 ? 271 HIS A C   1 
ATOM   2041 O O   . HIS A 1 271 ? 10.105  -35.366 -35.017 1.00 168.69 ? 271 HIS A O   1 
ATOM   2042 C CB  . HIS A 1 271 ? 7.131   -36.334 -34.444 1.00 171.23 ? 271 HIS A CB  1 
ATOM   2043 C CG  . HIS A 1 271 ? 7.191   -37.453 -35.428 1.00 190.52 ? 271 HIS A CG  1 
ATOM   2044 N ND1 . HIS A 1 271 ? 7.483   -37.235 -36.757 1.00 205.40 ? 271 HIS A ND1 1 
ATOM   2045 C CD2 . HIS A 1 271 ? 6.966   -38.771 -35.307 1.00 214.84 ? 271 HIS A CD2 1 
ATOM   2046 C CE1 . HIS A 1 271 ? 7.455   -38.394 -37.404 1.00 224.84 ? 271 HIS A CE1 1 
ATOM   2047 N NE2 . HIS A 1 271 ? 7.145   -39.339 -36.543 1.00 236.98 ? 271 HIS A NE2 1 
ATOM   2048 N N   . ILE A 1 272 ? 10.430  -37.342 -33.956 1.00 202.82 ? 272 ILE A N   1 
ATOM   2049 C CA  . ILE A 1 272 ? 11.610  -37.754 -34.704 1.00 193.61 ? 272 ILE A CA  1 
ATOM   2050 C C   . ILE A 1 272 ? 11.217  -38.852 -35.691 1.00 194.58 ? 272 ILE A C   1 
ATOM   2051 O O   . ILE A 1 272 ? 10.701  -39.890 -35.265 1.00 177.55 ? 272 ILE A O   1 
ATOM   2052 C CB  . ILE A 1 272 ? 12.689  -38.297 -33.746 1.00 172.39 ? 272 ILE A CB  1 
ATOM   2053 C CG1 . ILE A 1 272 ? 12.582  -37.746 -32.319 1.00 149.00 ? 272 ILE A CG1 1 
ATOM   2054 C CG2 . ILE A 1 272 ? 14.092  -38.166 -34.341 1.00 173.26 ? 272 ILE A CG2 1 
ATOM   2055 C CD1 . ILE A 1 272 ? 13.709  -36.812 -31.922 1.00 149.53 ? 272 ILE A CD1 1 
ATOM   2056 N N   . GLU A 1 273 ? 11.505  -38.624 -36.988 1.00 193.91 ? 273 GLU A N   1 
ATOM   2057 C CA  . GLU A 1 273 ? 11.383  -39.639 -38.003 1.00 203.30 ? 273 GLU A CA  1 
ATOM   2058 C C   . GLU A 1 273 ? 12.532  -40.593 -37.716 1.00 241.68 ? 273 GLU A C   1 
ATOM   2059 O O   . GLU A 1 273 ? 13.351  -40.325 -36.841 1.00 249.94 ? 273 GLU A O   1 
ATOM   2060 C CB  . GLU A 1 273 ? 11.376  -39.007 -39.394 1.00 186.29 ? 273 GLU A CB  1 
ATOM   2061 C CG  . GLU A 1 273 ? 10.935  -39.983 -40.479 1.00 202.11 ? 273 GLU A CG  1 
ATOM   2062 C CD  . GLU A 1 273 ? 11.003  -39.393 -41.868 1.00 230.58 ? 273 GLU A CD  1 
ATOM   2063 O OE1 . GLU A 1 273 ? 11.233  -38.169 -41.965 1.00 266.21 ? 273 GLU A OE1 1 
ATOM   2064 O OE2 . GLU A 1 273 ? 10.827  -40.156 -42.841 1.00 205.59 ? 273 GLU A OE2 1 
ATOM   2065 N N   . ARG A 1 274 ? 12.527  -41.719 -38.423 1.00 250.13 ? 274 ARG A N   1 
ATOM   2066 C CA  . ARG A 1 274 ? 13.543  -42.753 -38.298 1.00 236.97 ? 274 ARG A CA  1 
ATOM   2067 C C   . ARG A 1 274 ? 14.852  -42.279 -38.930 1.00 252.95 ? 274 ARG A C   1 
ATOM   2068 O O   . ARG A 1 274 ? 15.908  -42.780 -38.573 1.00 268.09 ? 274 ARG A O   1 
ATOM   2069 C CB  . ARG A 1 274 ? 13.027  -44.043 -38.944 1.00 224.42 ? 274 ARG A CB  1 
ATOM   2070 C CG  . ARG A 1 274 ? 12.735  -43.826 -40.421 1.00 246.56 ? 274 ARG A CG  1 
ATOM   2071 C CD  . ARG A 1 274 ? 12.306  -45.093 -41.136 1.00 303.47 ? 274 ARG A CD  1 
ATOM   2072 N NE  . ARG A 1 274 ? 12.268  -44.866 -42.585 1.00 327.55 ? 274 ARG A NE  1 
ATOM   2073 C CZ  . ARG A 1 274 ? 11.472  -44.013 -43.218 1.00 321.73 ? 274 ARG A CZ  1 
ATOM   2074 N NH1 . ARG A 1 274 ? 10.578  -43.303 -42.551 1.00 303.55 ? 274 ARG A NH1 1 
ATOM   2075 N NH2 . ARG A 1 274 ? 11.569  -43.869 -44.528 1.00 323.39 ? 274 ARG A NH2 1 
ATOM   2076 N N   . ASP A 1 275 ? 14.792  -41.310 -39.853 1.00 249.14 ? 275 ASP A N   1 
ATOM   2077 C CA  . ASP A 1 275 ? 15.993  -40.769 -40.478 1.00 205.09 ? 275 ASP A CA  1 
ATOM   2078 C C   . ASP A 1 275 ? 16.441  -39.510 -39.741 1.00 192.38 ? 275 ASP A C   1 
ATOM   2079 O O   . ASP A 1 275 ? 17.100  -38.656 -40.324 1.00 185.92 ? 275 ASP A O   1 
ATOM   2080 C CB  . ASP A 1 275 ? 15.833  -40.555 -41.979 1.00 194.87 ? 275 ASP A CB  1 
ATOM   2081 C CG  . ASP A 1 275 ? 14.650  -39.700 -42.418 1.00 210.73 ? 275 ASP A CG  1 
ATOM   2082 O OD1 . ASP A 1 275 ? 14.492  -38.589 -41.879 1.00 209.15 ? 275 ASP A OD1 1 
ATOM   2083 O OD2 . ASP A 1 275 ? 13.901  -40.147 -43.312 1.00 236.10 ? 275 ASP A OD2 1 
ATOM   2084 N N   . GLY A 1 276 ? 16.056  -39.400 -38.462 1.00 195.78 ? 276 GLY A N   1 
ATOM   2085 C CA  . GLY A 1 276 ? 16.522  -38.338 -37.584 1.00 200.92 ? 276 GLY A CA  1 
ATOM   2086 C C   . GLY A 1 276 ? 15.763  -37.028 -37.746 1.00 208.93 ? 276 GLY A C   1 
ATOM   2087 O O   . GLY A 1 276 ? 16.016  -36.095 -36.975 1.00 209.03 ? 276 GLY A O   1 
ATOM   2088 N N   . THR A 1 277 ? 14.848  -36.989 -38.733 1.00 210.33 ? 277 THR A N   1 
ATOM   2089 C CA  . THR A 1 277 ? 14.129  -35.765 -39.055 1.00 216.16 ? 277 THR A CA  1 
ATOM   2090 C C   . THR A 1 277 ? 13.241  -35.396 -37.875 1.00 227.16 ? 277 THR A C   1 
ATOM   2091 O O   . THR A 1 277 ? 12.363  -36.169 -37.515 1.00 214.45 ? 277 THR A O   1 
ATOM   2092 C CB  . THR A 1 277 ? 13.343  -35.911 -40.358 1.00 202.48 ? 277 THR A CB  1 
ATOM   2093 O OG1 . THR A 1 277 ? 14.336  -35.895 -41.376 1.00 206.15 ? 277 THR A OG1 1 
ATOM   2094 C CG2 . THR A 1 277 ? 12.410  -34.746 -40.624 1.00 211.95 ? 277 THR A CG2 1 
ATOM   2095 N N   . VAL A 1 278 ? 13.521  -34.233 -37.272 1.00 233.50 ? 278 VAL A N   1 
ATOM   2096 C CA  . VAL A 1 278 ? 12.758  -33.701 -36.166 1.00 207.65 ? 278 VAL A CA  1 
ATOM   2097 C C   . VAL A 1 278 ? 11.680  -32.786 -36.736 1.00 197.98 ? 278 VAL A C   1 
ATOM   2098 O O   . VAL A 1 278 ? 11.940  -31.980 -37.643 1.00 216.76 ? 278 VAL A O   1 
ATOM   2099 C CB  . VAL A 1 278 ? 13.652  -32.939 -35.168 1.00 202.25 ? 278 VAL A CB  1 
ATOM   2100 C CG1 . VAL A 1 278 ? 12.851  -32.485 -33.956 1.00 191.85 ? 278 VAL A CG1 1 
ATOM   2101 C CG2 . VAL A 1 278 ? 14.868  -33.756 -34.742 1.00 186.83 ? 278 VAL A CG2 1 
ATOM   2102 N N   . ARG A 1 279 ? 10.475  -32.933 -36.178 1.00 173.20 ? 279 ARG A N   1 
ATOM   2103 C CA  . ARG A 1 279 ? 9.330   -32.107 -36.536 1.00 167.97 ? 279 ARG A CA  1 
ATOM   2104 C C   . ARG A 1 279 ? 8.695   -31.489 -35.285 1.00 159.35 ? 279 ARG A C   1 
ATOM   2105 O O   . ARG A 1 279 ? 8.414   -32.186 -34.312 1.00 152.27 ? 279 ARG A O   1 
ATOM   2106 C CB  . ARG A 1 279 ? 8.413   -32.882 -37.489 1.00 173.44 ? 279 ARG A CB  1 
ATOM   2107 C CG  . ARG A 1 279 ? 8.971   -32.923 -38.906 1.00 191.47 ? 279 ARG A CG  1 
ATOM   2108 C CD  . ARG A 1 279 ? 8.161   -33.769 -39.878 1.00 240.29 ? 279 ARG A CD  1 
ATOM   2109 N NE  . ARG A 1 279 ? 8.396   -35.216 -39.796 1.00 271.70 ? 279 ARG A NE  1 
ATOM   2110 C CZ  . ARG A 1 279 ? 7.678   -36.141 -40.434 1.00 275.28 ? 279 ARG A CZ  1 
ATOM   2111 N NH1 . ARG A 1 279 ? 6.665   -35.777 -41.201 1.00 283.83 ? 279 ARG A NH1 1 
ATOM   2112 N NH2 . ARG A 1 279 ? 7.978   -37.421 -40.332 1.00 257.82 ? 279 ARG A NH2 1 
ATOM   2113 N N   . VAL A 1 280 ? 8.569   -30.157 -35.311 1.00 157.86 ? 280 VAL A N   1 
ATOM   2114 C CA  . VAL A 1 280 ? 7.801   -29.420 -34.327 1.00 164.75 ? 280 VAL A CA  1 
ATOM   2115 C C   . VAL A 1 280 ? 6.356   -29.726 -34.686 1.00 178.59 ? 280 VAL A C   1 
ATOM   2116 O O   . VAL A 1 280 ? 5.863   -29.229 -35.696 1.00 186.01 ? 280 VAL A O   1 
ATOM   2117 C CB  . VAL A 1 280 ? 8.082   -27.908 -34.365 1.00 174.81 ? 280 VAL A CB  1 
ATOM   2118 C CG1 . VAL A 1 280 ? 7.900   -27.345 -35.769 1.00 181.95 ? 280 VAL A CG1 1 
ATOM   2119 C CG2 . VAL A 1 280 ? 7.213   -27.154 -33.368 1.00 199.40 ? 280 VAL A CG2 1 
ATOM   2120 N N   . VAL A 1 281 ? 5.737   -30.624 -33.916 1.00 172.49 ? 281 VAL A N   1 
ATOM   2121 C CA  . VAL A 1 281 ? 4.374   -31.003 -34.229 1.00 160.73 ? 281 VAL A CA  1 
ATOM   2122 C C   . VAL A 1 281 ? 3.479   -29.828 -33.839 1.00 167.63 ? 281 VAL A C   1 
ATOM   2123 O O   . VAL A 1 281 ? 2.840   -29.232 -34.699 1.00 191.22 ? 281 VAL A O   1 
ATOM   2124 C CB  . VAL A 1 281 ? 3.877   -32.313 -33.596 1.00 159.80 ? 281 VAL A CB  1 
ATOM   2125 C CG1 . VAL A 1 281 ? 2.490   -32.675 -34.113 1.00 161.78 ? 281 VAL A CG1 1 
ATOM   2126 C CG2 . VAL A 1 281 ? 4.836   -33.467 -33.858 1.00 197.61 ? 281 VAL A CG2 1 
ATOM   2127 N N   . ALA A 1 282 ? 3.480   -29.482 -32.552 1.00 157.78 ? 282 ALA A N   1 
ATOM   2128 C CA  . ALA A 1 282 ? 2.554   -28.484 -32.060 1.00 150.21 ? 282 ALA A CA  1 
ATOM   2129 C C   . ALA A 1 282 ? 3.033   -27.904 -30.741 1.00 148.01 ? 282 ALA A C   1 
ATOM   2130 O O   . ALA A 1 282 ? 3.809   -28.491 -29.966 1.00 144.49 ? 282 ALA A O   1 
ATOM   2131 C CB  . ALA A 1 282 ? 1.166   -29.074 -31.958 1.00 148.77 ? 282 ALA A CB  1 
ATOM   2132 N N   . CYS A 1 283 ? 2.475   -26.721 -30.457 1.00 143.38 ? 283 CYS A N   1 
ATOM   2133 C CA  . CYS A 1 283 ? 2.596   -26.050 -29.170 1.00 139.42 ? 283 CYS A CA  1 
ATOM   2134 C C   . CYS A 1 283 ? 1.217   -25.678 -28.636 1.00 128.01 ? 283 CYS A C   1 
ATOM   2135 O O   . CYS A 1 283 ? 0.390   -25.089 -29.334 1.00 121.44 ? 283 CYS A O   1 
ATOM   2136 C CB  . CYS A 1 283 ? 3.485   -24.831 -29.284 1.00 146.61 ? 283 CYS A CB  1 
ATOM   2137 S SG  . CYS A 1 283 ? 5.065   -25.260 -30.044 1.00 229.75 ? 283 CYS A SG  1 
ATOM   2138 N N   . HIS A 1 284 ? 1.003   -26.035 -27.369 1.00 122.70 ? 284 HIS A N   1 
ATOM   2139 C CA  . HIS A 1 284 ? -0.189  -25.699 -26.619 1.00 114.46 ? 284 HIS A CA  1 
ATOM   2140 C C   . HIS A 1 284 ? 0.173   -25.022 -25.295 1.00 127.23 ? 284 HIS A C   1 
ATOM   2141 O O   . HIS A 1 284 ? 1.340   -24.897 -24.867 1.00 129.05 ? 284 HIS A O   1 
ATOM   2142 C CB  . HIS A 1 284 ? -0.934  -26.955 -26.162 1.00 123.08 ? 284 HIS A CB  1 
ATOM   2143 C CG  . HIS A 1 284 ? -1.253  -27.985 -27.194 1.00 137.01 ? 284 HIS A CG  1 
ATOM   2144 N ND1 . HIS A 1 284 ? -0.276  -28.740 -27.805 1.00 144.20 ? 284 HIS A ND1 1 
ATOM   2145 C CD2 . HIS A 1 284 ? -2.430  -28.427 -27.679 1.00 131.12 ? 284 HIS A CD2 1 
ATOM   2146 C CE1 . HIS A 1 284 ? -0.849  -29.583 -28.646 1.00 133.87 ? 284 HIS A CE1 1 
ATOM   2147 N NE2 . HIS A 1 284 ? -2.158  -29.425 -28.568 1.00 121.91 ? 284 HIS A NE2 1 
ATOM   2148 N N   . ASP A 1 285 ? -0.918  -24.605 -24.639 1.00 135.72 ? 285 ASP A N   1 
ATOM   2149 C CA  . ASP A 1 285 ? -0.931  -24.017 -23.302 1.00 141.86 ? 285 ASP A CA  1 
ATOM   2150 C C   . ASP A 1 285 ? -1.762  -24.903 -22.367 1.00 130.50 ? 285 ASP A C   1 
ATOM   2151 O O   . ASP A 1 285 ? -2.945  -24.673 -22.143 1.00 127.51 ? 285 ASP A O   1 
ATOM   2152 C CB  . ASP A 1 285 ? -1.418  -22.575 -23.330 1.00 160.01 ? 285 ASP A CB  1 
ATOM   2153 C CG  . ASP A 1 285 ? -0.358  -21.507 -23.090 1.00 169.11 ? 285 ASP A CG  1 
ATOM   2154 O OD1 . ASP A 1 285 ? 0.146   -21.422 -21.944 1.00 161.98 ? 285 ASP A OD1 1 
ATOM   2155 O OD2 . ASP A 1 285 ? -0.059  -20.759 -24.045 1.00 167.71 ? 285 ASP A OD2 1 
ATOM   2156 N N   . GLN A 1 286 ? -1.092  -25.967 -21.910 1.00 138.45 ? 286 GLN A N   1 
ATOM   2157 C CA  . GLN A 1 286 ? -1.571  -26.862 -20.870 1.00 140.13 ? 286 GLN A CA  1 
ATOM   2158 C C   . GLN A 1 286 ? -1.874  -26.047 -19.621 1.00 136.73 ? 286 GLN A C   1 
ATOM   2159 O O   . GLN A 1 286 ? -1.333  -24.962 -19.432 1.00 144.68 ? 286 GLN A O   1 
ATOM   2160 C CB  . GLN A 1 286 ? -0.510  -27.882 -20.449 1.00 154.33 ? 286 GLN A CB  1 
ATOM   2161 C CG  . GLN A 1 286 ? -0.009  -28.798 -21.563 1.00 167.73 ? 286 GLN A CG  1 
ATOM   2162 C CD  . GLN A 1 286 ? 0.919   -29.872 -21.046 1.00 178.11 ? 286 GLN A CD  1 
ATOM   2163 O OE1 . GLN A 1 286 ? 1.138   -29.979 -19.832 1.00 162.13 ? 286 GLN A OE1 1 
ATOM   2164 N NE2 . GLN A 1 286 ? 1.459   -30.678 -21.955 1.00 206.86 ? 286 GLN A NE2 1 
ATOM   2165 N N   . VAL A 1 287 ? -2.763  -26.583 -18.791 1.00 145.90 ? 287 VAL A N   1 
ATOM   2166 C CA  . VAL A 1 287 ? -3.071  -25.996 -17.500 1.00 169.31 ? 287 VAL A CA  1 
ATOM   2167 C C   . VAL A 1 287 ? -3.091  -27.150 -16.501 1.00 160.11 ? 287 VAL A C   1 
ATOM   2168 O O   . VAL A 1 287 ? -4.064  -27.894 -16.440 1.00 155.87 ? 287 VAL A O   1 
ATOM   2169 C CB  . VAL A 1 287 ? -4.388  -25.182 -17.543 1.00 195.04 ? 287 VAL A CB  1 
ATOM   2170 C CG1 . VAL A 1 287 ? -5.460  -25.833 -18.419 1.00 192.39 ? 287 VAL A CG1 1 
ATOM   2171 C CG2 . VAL A 1 287 ? -4.921  -24.832 -16.156 1.00 207.22 ? 287 VAL A CG2 1 
ATOM   2172 N N   . LEU A 1 288 ? -1.983  -27.315 -15.766 1.00 167.03 ? 288 LEU A N   1 
ATOM   2173 C CA  . LEU A 1 288 ? -1.792  -28.476 -14.907 1.00 190.96 ? 288 LEU A CA  1 
ATOM   2174 C C   . LEU A 1 288 ? -3.096  -28.784 -14.174 1.00 198.51 ? 288 LEU A C   1 
ATOM   2175 O O   . LEU A 1 288 ? -3.542  -29.922 -14.185 1.00 177.52 ? 288 LEU A O   1 
ATOM   2176 C CB  . LEU A 1 288 ? -0.595  -28.336 -13.964 1.00 220.09 ? 288 LEU A CB  1 
ATOM   2177 C CG  . LEU A 1 288 ? 0.766   -28.070 -14.630 1.00 239.53 ? 288 LEU A CG  1 
ATOM   2178 C CD1 . LEU A 1 288 ? 1.907   -27.871 -13.632 1.00 204.04 ? 288 LEU A CD1 1 
ATOM   2179 C CD2 . LEU A 1 288 ? 1.138   -29.129 -15.669 1.00 248.66 ? 288 LEU A CD2 1 
ATOM   2180 N N   . SER A 1 289 ? -3.721  -27.746 -13.603 1.00 254.68 ? 289 SER A N   1 
ATOM   2181 C CA  . SER A 1 289 ? -5.029  -27.829 -12.965 1.00 306.74 ? 289 SER A CA  1 
ATOM   2182 C C   . SER A 1 289 ? -5.106  -29.059 -12.063 1.00 295.79 ? 289 SER A C   1 
ATOM   2183 O O   . SER A 1 289 ? -5.881  -29.983 -12.324 1.00 350.21 ? 289 SER A O   1 
ATOM   2184 C CB  . SER A 1 289 ? -6.153  -27.809 -13.982 1.00 338.22 ? 289 SER A CB  1 
ATOM   2185 O OG  . SER A 1 289 ? -6.086  -28.942 -14.833 1.00 380.18 ? 289 SER A OG  1 
ATOM   2186 N N   . GLY A 1 290 ? -4.272  -29.051 -11.016 1.00 250.64 ? 290 GLY A N   1 
ATOM   2187 C CA  . GLY A 1 290 ? -4.106  -30.192 -10.131 1.00 251.99 ? 290 GLY A CA  1 
ATOM   2188 C C   . GLY A 1 290 ? -3.401  -31.348 -10.837 1.00 269.35 ? 290 GLY A C   1 
ATOM   2189 O O   . GLY A 1 290 ? -3.454  -32.487 -10.374 1.00 282.41 ? 290 GLY A O   1 
ATOM   2190 N N   . GLY A 1 291 ? -2.767  -31.047 -11.977 1.00 262.62 ? 291 GLY A N   1 
ATOM   2191 C CA  . GLY A 1 291 ? -1.967  -32.018 -12.706 1.00 258.92 ? 291 GLY A CA  1 
ATOM   2192 C C   . GLY A 1 291 ? -2.793  -33.059 -13.467 1.00 268.01 ? 291 GLY A C   1 
ATOM   2193 O O   . GLY A 1 291 ? -2.223  -33.772 -14.290 1.00 293.70 ? 291 GLY A O   1 
ATOM   2194 N N   . GLN A 1 292 ? -4.110  -33.155 -13.194 1.00 265.26 ? 292 GLN A N   1 
ATOM   2195 C CA  . GLN A 1 292 ? -5.009  -34.061 -13.908 1.00 246.18 ? 292 GLN A CA  1 
ATOM   2196 C C   . GLN A 1 292 ? -5.342  -33.493 -15.291 1.00 241.67 ? 292 GLN A C   1 
ATOM   2197 O O   . GLN A 1 292 ? -6.219  -34.024 -15.982 1.00 214.81 ? 292 GLN A O   1 
ATOM   2198 C CB  . GLN A 1 292 ? -6.338  -34.345 -13.201 1.00 215.43 ? 292 GLN A CB  1 
ATOM   2199 C CG  . GLN A 1 292 ? -6.250  -34.601 -11.698 1.00 237.96 ? 292 GLN A CG  1 
ATOM   2200 C CD  . GLN A 1 292 ? -5.656  -35.939 -11.317 1.00 247.74 ? 292 GLN A CD  1 
ATOM   2201 O OE1 . GLN A 1 292 ? -4.603  -36.019 -10.681 1.00 258.04 ? 292 GLN A OE1 1 
ATOM   2202 N NE2 . GLN A 1 292 ? -6.333  -37.013 -11.690 1.00 258.60 ? 292 GLN A NE2 1 
ATOM   2203 N N   . TYR A 1 293 ? -4.641  -32.402 -15.664 1.00 214.83 ? 293 TYR A N   1 
ATOM   2204 C CA  . TYR A 1 293 ? -4.712  -31.747 -16.968 1.00 154.96 ? 293 TYR A CA  1 
ATOM   2205 C C   . TYR A 1 293 ? -6.155  -31.739 -17.458 1.00 117.99 ? 293 TYR A C   1 
ATOM   2206 O O   . TYR A 1 293 ? -6.450  -32.206 -18.554 1.00 114.97 ? 293 TYR A O   1 
ATOM   2207 C CB  . TYR A 1 293 ? -3.673  -32.430 -17.864 1.00 130.70 ? 293 TYR A CB  1 
ATOM   2208 C CG  . TYR A 1 293 ? -3.763  -32.202 -19.365 1.00 114.64 ? 293 TYR A CG  1 
ATOM   2209 C CD1 . TYR A 1 293 ? -4.578  -32.992 -20.172 1.00 116.89 ? 293 TYR A CD1 1 
ATOM   2210 C CD2 . TYR A 1 293 ? -2.981  -31.239 -19.980 1.00 114.97 ? 293 TYR A CD2 1 
ATOM   2211 C CE1 . TYR A 1 293 ? -4.652  -32.800 -21.541 1.00 126.92 ? 293 TYR A CE1 1 
ATOM   2212 C CE2 . TYR A 1 293 ? -3.033  -31.045 -21.349 1.00 125.77 ? 293 TYR A CE2 1 
ATOM   2213 C CZ  . TYR A 1 293 ? -3.866  -31.829 -22.128 1.00 134.51 ? 293 TYR A CZ  1 
ATOM   2214 O OH  . TYR A 1 293 ? -3.916  -31.676 -23.483 1.00 151.37 ? 293 TYR A OH  1 
ATOM   2215 N N   . TRP A 1 294 ? -7.066  -31.258 -16.613 1.00 104.06 ? 294 TRP A N   1 
ATOM   2216 C CA  . TRP A 1 294 ? -8.458  -31.339 -17.009 1.00 141.47 ? 294 TRP A CA  1 
ATOM   2217 C C   . TRP A 1 294 ? -8.637  -30.692 -18.383 1.00 153.93 ? 294 TRP A C   1 
ATOM   2218 O O   . TRP A 1 294 ? -9.769  -30.615 -18.875 1.00 214.29 ? 294 TRP A O   1 
ATOM   2219 C CB  . TRP A 1 294 ? -9.389  -30.801 -15.912 1.00 148.14 ? 294 TRP A CB  1 
ATOM   2220 C CG  . TRP A 1 294 ? -9.259  -31.573 -14.625 1.00 148.85 ? 294 TRP A CG  1 
ATOM   2221 C CD1 . TRP A 1 294 ? -8.595  -31.169 -13.506 1.00 129.62 ? 294 TRP A CD1 1 
ATOM   2222 C CD2 . TRP A 1 294 ? -9.757  -32.906 -14.348 1.00 185.88 ? 294 TRP A CD2 1 
ATOM   2223 N NE1 . TRP A 1 294 ? -8.684  -32.133 -12.535 1.00 151.25 ? 294 TRP A NE1 1 
ATOM   2224 C CE2 . TRP A 1 294 ? -9.371  -33.216 -13.028 1.00 204.13 ? 294 TRP A CE2 1 
ATOM   2225 C CE3 . TRP A 1 294 ? -10.478 -33.864 -15.069 1.00 185.24 ? 294 TRP A CE3 1 
ATOM   2226 C CZ2 . TRP A 1 294 ? -9.696  -34.436 -12.431 1.00 247.20 ? 294 TRP A CZ2 1 
ATOM   2227 C CZ3 . TRP A 1 294 ? -10.788 -35.070 -14.485 1.00 197.48 ? 294 TRP A CZ3 1 
ATOM   2228 C CH2 . TRP A 1 294 ? -10.396 -35.354 -13.181 1.00 226.96 ? 294 TRP A CH2 1 
ATOM   2229 N N   . GLY A 1 295 ? -7.501  -30.273 -18.978 1.00 111.47 ? 295 GLY A N   1 
ATOM   2230 C CA  . GLY A 1 295 ? -7.463  -29.928 -20.394 1.00 118.88 ? 295 GLY A CA  1 
ATOM   2231 C C   . GLY A 1 295 ? -6.299  -29.028 -20.837 1.00 112.62 ? 295 GLY A C   1 
ATOM   2232 O O   . GLY A 1 295 ? -5.265  -28.936 -20.188 1.00 99.33  ? 295 GLY A O   1 
ATOM   2233 N N   . CYS A 1 296 ? -6.508  -28.374 -21.978 1.00 111.63 ? 296 CYS A N   1 
ATOM   2234 C CA  . CYS A 1 296 ? -5.516  -27.584 -22.673 1.00 92.43  ? 296 CYS A CA  1 
ATOM   2235 C C   . CYS A 1 296 ? -6.120  -26.875 -23.892 1.00 103.95 ? 296 CYS A C   1 
ATOM   2236 O O   . CYS A 1 296 ? -7.203  -27.214 -24.419 1.00 116.72 ? 296 CYS A O   1 
ATOM   2237 C CB  . CYS A 1 296 ? -4.418  -28.485 -23.206 1.00 91.17  ? 296 CYS A CB  1 
ATOM   2238 S SG  . CYS A 1 296 ? -4.853  -29.375 -24.737 1.00 119.25 ? 296 CYS A SG  1 
ATOM   2239 N N   . ARG A 1 297 ? -5.356  -25.881 -24.367 1.00 98.85  ? 297 ARG A N   1 
ATOM   2240 C CA  . ARG A 1 297 ? -5.732  -25.044 -25.494 1.00 105.76 ? 297 ARG A CA  1 
ATOM   2241 C C   . ARG A 1 297 ? -4.604  -24.923 -26.513 1.00 110.38 ? 297 ARG A C   1 
ATOM   2242 O O   . ARG A 1 297 ? -3.400  -24.852 -26.199 1.00 117.66 ? 297 ARG A O   1 
ATOM   2243 C CB  . ARG A 1 297 ? -6.012  -23.570 -25.186 1.00 132.53 ? 297 ARG A CB  1 
ATOM   2244 C CG  . ARG A 1 297 ? -7.356  -23.286 -24.528 1.00 164.55 ? 297 ARG A CG  1 
ATOM   2245 C CD  . ARG A 1 297 ? -7.802  -21.836 -24.545 1.00 163.50 ? 297 ARG A CD  1 
ATOM   2246 N NE  . ARG A 1 297 ? -8.256  -21.381 -23.224 1.00 183.82 ? 297 ARG A NE  1 
ATOM   2247 C CZ  . ARG A 1 297 ? -8.567  -22.095 -22.135 1.00 209.72 ? 297 ARG A CZ  1 
ATOM   2248 N NH1 . ARG A 1 297 ? -8.582  -21.521 -20.946 1.00 240.70 ? 297 ARG A NH1 1 
ATOM   2249 N NH2 . ARG A 1 297 ? -8.788  -23.391 -22.198 1.00 243.50 ? 297 ARG A NH2 1 
ATOM   2250 N N   . PHE A 1 298 ? -5.049  -24.730 -27.760 1.00 109.07 ? 298 PHE A N   1 
ATOM   2251 C CA  . PHE A 1 298 ? -4.171  -24.456 -28.900 1.00 117.67 ? 298 PHE A CA  1 
ATOM   2252 C C   . PHE A 1 298 ? -4.613  -23.232 -29.709 1.00 133.66 ? 298 PHE A C   1 
ATOM   2253 O O   . PHE A 1 298 ? -5.812  -22.969 -29.905 1.00 157.52 ? 298 PHE A O   1 
ATOM   2254 C CB  . PHE A 1 298 ? -4.023  -25.714 -29.756 1.00 126.96 ? 298 PHE A CB  1 
ATOM   2255 C CG  . PHE A 1 298 ? -3.367  -25.513 -31.116 1.00 131.05 ? 298 PHE A CG  1 
ATOM   2256 C CD1 . PHE A 1 298 ? -4.127  -25.108 -32.214 1.00 127.68 ? 298 PHE A CD1 1 
ATOM   2257 C CD2 . PHE A 1 298 ? -1.997  -25.715 -31.288 1.00 143.75 ? 298 PHE A CD2 1 
ATOM   2258 C CE1 . PHE A 1 298 ? -3.535  -24.912 -33.448 1.00 137.03 ? 298 PHE A CE1 1 
ATOM   2259 C CE2 . PHE A 1 298 ? -1.408  -25.509 -32.528 1.00 158.40 ? 298 PHE A CE2 1 
ATOM   2260 C CZ  . PHE A 1 298 ? -2.182  -25.115 -33.597 1.00 147.42 ? 298 PHE A CZ  1 
ATOM   2261 N N   . PRO A 1 299 ? -3.662  -22.480 -30.334 1.00 143.28 ? 299 PRO A N   1 
ATOM   2262 C CA  . PRO A 1 299 ? -2.215  -22.679 -30.164 1.00 144.38 ? 299 PRO A CA  1 
ATOM   2263 C C   . PRO A 1 299 ? -1.694  -22.110 -28.854 1.00 149.27 ? 299 PRO A C   1 
ATOM   2264 O O   . PRO A 1 299 ? -2.462  -21.608 -28.042 1.00 161.71 ? 299 PRO A O   1 
ATOM   2265 C CB  . PRO A 1 299 ? -1.541  -21.985 -31.365 1.00 135.26 ? 299 PRO A CB  1 
ATOM   2266 C CG  . PRO A 1 299 ? -2.573  -21.002 -31.828 1.00 151.97 ? 299 PRO A CG  1 
ATOM   2267 C CD  . PRO A 1 299 ? -3.950  -21.428 -31.324 1.00 150.40 ? 299 PRO A CD  1 
ATOM   2268 N N   . ALA A 1 300 ? -0.375  -22.175 -28.673 1.00 156.01 ? 300 ALA A N   1 
ATOM   2269 C CA  . ALA A 1 300 ? 0.222   -21.574 -27.497 1.00 166.36 ? 300 ALA A CA  1 
ATOM   2270 C C   . ALA A 1 300 ? 0.029   -20.069 -27.586 1.00 167.52 ? 300 ALA A C   1 
ATOM   2271 O O   . ALA A 1 300 ? -0.296  -19.545 -28.656 1.00 175.90 ? 300 ALA A O   1 
ATOM   2272 C CB  . ALA A 1 300 ? 1.690   -21.928 -27.416 1.00 199.78 ? 300 ALA A CB  1 
ATOM   2273 N N   . ASP A 1 301 ? 0.269   -19.393 -26.459 1.00 169.70 ? 301 ASP A N   1 
ATOM   2274 C CA  . ASP A 1 301 ? 0.237   -17.943 -26.415 1.00 188.34 ? 301 ASP A CA  1 
ATOM   2275 C C   . ASP A 1 301 ? 1.235   -17.382 -27.429 1.00 200.52 ? 301 ASP A C   1 
ATOM   2276 O O   . ASP A 1 301 ? 2.370   -17.849 -27.521 1.00 220.41 ? 301 ASP A O   1 
ATOM   2277 C CB  . ASP A 1 301 ? 0.405   -17.437 -24.990 1.00 187.17 ? 301 ASP A CB  1 
ATOM   2278 C CG  . ASP A 1 301 ? 0.312   -15.929 -24.803 1.00 189.63 ? 301 ASP A CG  1 
ATOM   2279 O OD1 . ASP A 1 301 ? 0.365   -15.202 -25.824 1.00 198.44 ? 301 ASP A OD1 1 
ATOM   2280 O OD2 . ASP A 1 301 ? 0.155   -15.489 -23.645 1.00 192.61 ? 301 ASP A OD2 1 
ATOM   2281 N N   . GLU A 1 302 ? 0.773   -16.368 -28.172 1.00 205.45 ? 302 GLU A N   1 
ATOM   2282 C CA  . GLU A 1 302 ? 1.480   -15.752 -29.288 1.00 201.07 ? 302 GLU A CA  1 
ATOM   2283 C C   . GLU A 1 302 ? 2.903   -15.368 -28.893 1.00 175.49 ? 302 GLU A C   1 
ATOM   2284 O O   . GLU A 1 302 ? 3.828   -15.539 -29.684 1.00 153.15 ? 302 GLU A O   1 
ATOM   2285 C CB  . GLU A 1 302 ? 0.697   -14.556 -29.839 1.00 228.69 ? 302 GLU A CB  1 
ATOM   2286 C CG  . GLU A 1 302 ? 0.151   -13.619 -28.764 1.00 249.64 ? 302 GLU A CG  1 
ATOM   2287 C CD  . GLU A 1 302 ? -1.047  -12.779 -29.194 1.00 266.65 ? 302 GLU A CD  1 
ATOM   2288 O OE1 . GLU A 1 302 ? -0.835  -11.844 -29.992 1.00 288.64 ? 302 GLU A OE1 1 
ATOM   2289 O OE2 . GLU A 1 302 ? -2.191  -13.061 -28.761 1.00 248.12 ? 302 GLU A OE2 1 
ATOM   2290 N N   . ARG A 1 303 ? 3.049   -14.848 -27.667 1.00 166.69 ? 303 ARG A N   1 
ATOM   2291 C CA  . ARG A 1 303 ? 4.309   -14.355 -27.139 1.00 181.21 ? 303 ARG A CA  1 
ATOM   2292 C C   . ARG A 1 303 ? 5.346   -15.470 -27.086 1.00 184.06 ? 303 ARG A C   1 
ATOM   2293 O O   . ARG A 1 303 ? 6.415   -15.342 -27.678 1.00 207.62 ? 303 ARG A O   1 
ATOM   2294 C CB  . ARG A 1 303 ? 4.099   -13.741 -25.752 1.00 186.20 ? 303 ARG A CB  1 
ATOM   2295 C CG  . ARG A 1 303 ? 3.626   -12.295 -25.835 1.00 208.23 ? 303 ARG A CG  1 
ATOM   2296 C CD  . ARG A 1 303 ? 2.581   -11.984 -24.789 1.00 218.51 ? 303 ARG A CD  1 
ATOM   2297 N NE  . ARG A 1 303 ? 1.250   -12.476 -25.163 1.00 252.37 ? 303 ARG A NE  1 
ATOM   2298 C CZ  . ARG A 1 303 ? 0.179   -12.403 -24.382 1.00 269.20 ? 303 ARG A CZ  1 
ATOM   2299 N NH1 . ARG A 1 303 ? 0.280   -11.893 -23.169 1.00 281.28 ? 303 ARG A NH1 1 
ATOM   2300 N NH2 . ARG A 1 303 ? -0.991  -12.844 -24.807 1.00 272.27 ? 303 ARG A NH2 1 
ATOM   2301 N N   . TRP A 1 304 ? 5.030   -16.544 -26.356 1.00 176.93 ? 304 TRP A N   1 
ATOM   2302 C CA  . TRP A 1 304 ? 5.993   -17.619 -26.168 1.00 177.30 ? 304 TRP A CA  1 
ATOM   2303 C C   . TRP A 1 304 ? 5.746   -18.802 -27.099 1.00 161.01 ? 304 TRP A C   1 
ATOM   2304 O O   . TRP A 1 304 ? 6.277   -19.868 -26.842 1.00 137.13 ? 304 TRP A O   1 
ATOM   2305 C CB  . TRP A 1 304 ? 6.096   -18.087 -24.706 1.00 187.77 ? 304 TRP A CB  1 
ATOM   2306 C CG  . TRP A 1 304 ? 4.829   -18.041 -23.895 1.00 213.90 ? 304 TRP A CG  1 
ATOM   2307 C CD1 . TRP A 1 304 ? 3.850   -18.987 -23.778 1.00 207.24 ? 304 TRP A CD1 1 
ATOM   2308 C CD2 . TRP A 1 304 ? 4.443   -16.953 -23.029 1.00 243.67 ? 304 TRP A CD2 1 
ATOM   2309 N NE1 . TRP A 1 304 ? 2.869   -18.544 -22.929 1.00 242.00 ? 304 TRP A NE1 1 
ATOM   2310 C CE2 . TRP A 1 304 ? 3.204   -17.304 -22.449 1.00 267.80 ? 304 TRP A CE2 1 
ATOM   2311 C CE3 . TRP A 1 304 ? 5.018   -15.716 -22.710 1.00 264.05 ? 304 TRP A CE3 1 
ATOM   2312 C CZ2 . TRP A 1 304 ? 2.541   -16.459 -21.559 1.00 303.57 ? 304 TRP A CZ2 1 
ATOM   2313 C CZ3 . TRP A 1 304 ? 4.363   -14.885 -21.827 1.00 306.88 ? 304 TRP A CZ3 1 
ATOM   2314 C CH2 . TRP A 1 304 ? 3.142   -15.254 -21.261 1.00 310.11 ? 304 TRP A CH2 1 
ATOM   2315 N N   . ARG A 1 305 ? 4.981   -18.625 -28.185 1.00 180.18 ? 305 ARG A N   1 
ATOM   2316 C CA  . ARG A 1 305 ? 4.779   -19.766 -29.073 1.00 178.96 ? 305 ARG A CA  1 
ATOM   2317 C C   . ARG A 1 305 ? 6.071   -19.961 -29.864 1.00 159.47 ? 305 ARG A C   1 
ATOM   2318 O O   . ARG A 1 305 ? 6.611   -21.076 -29.946 1.00 131.44 ? 305 ARG A O   1 
ATOM   2319 C CB  . ARG A 1 305 ? 3.549   -19.615 -29.992 1.00 203.43 ? 305 ARG A CB  1 
ATOM   2320 C CG  . ARG A 1 305 ? 3.423   -20.523 -31.215 1.00 180.25 ? 305 ARG A CG  1 
ATOM   2321 C CD  . ARG A 1 305 ? 2.822   -19.826 -32.421 1.00 173.38 ? 305 ARG A CD  1 
ATOM   2322 N NE  . ARG A 1 305 ? 1.783   -18.913 -31.932 1.00 182.78 ? 305 ARG A NE  1 
ATOM   2323 C CZ  . ARG A 1 305 ? 0.891   -18.275 -32.668 1.00 179.90 ? 305 ARG A CZ  1 
ATOM   2324 N NH1 . ARG A 1 305 ? 0.817   -18.502 -33.968 1.00 195.15 ? 305 ARG A NH1 1 
ATOM   2325 N NH2 . ARG A 1 305 ? 0.041   -17.446 -32.091 1.00 163.92 ? 305 ARG A NH2 1 
ATOM   2326 N N   . PRO A 1 306 ? 6.491   -18.853 -30.524 1.00 172.96 ? 306 PRO A N   1 
ATOM   2327 C CA  . PRO A 1 306 ? 7.656   -18.873 -31.398 1.00 167.61 ? 306 PRO A CA  1 
ATOM   2328 C C   . PRO A 1 306 ? 8.894   -19.330 -30.633 1.00 158.14 ? 306 PRO A C   1 
ATOM   2329 O O   . PRO A 1 306 ? 9.662   -20.169 -31.123 1.00 129.04 ? 306 PRO A O   1 
ATOM   2330 C CB  . PRO A 1 306 ? 7.771   -17.413 -31.891 1.00 175.16 ? 306 PRO A CB  1 
ATOM   2331 C CG  . PRO A 1 306 ? 6.363   -16.862 -31.806 1.00 166.60 ? 306 PRO A CG  1 
ATOM   2332 C CD  . PRO A 1 306 ? 5.775   -17.560 -30.598 1.00 176.61 ? 306 PRO A CD  1 
ATOM   2333 N N   . GLU A 1 307 ? 9.047   -18.758 -29.431 1.00 153.34 ? 307 GLU A N   1 
ATOM   2334 C CA  . GLU A 1 307 ? 10.166  -19.055 -28.552 1.00 150.24 ? 307 GLU A CA  1 
ATOM   2335 C C   . GLU A 1 307 ? 10.208  -20.556 -28.243 1.00 141.21 ? 307 GLU A C   1 
ATOM   2336 O O   . GLU A 1 307 ? 11.262  -21.208 -28.315 1.00 119.15 ? 307 GLU A O   1 
ATOM   2337 C CB  . GLU A 1 307 ? 9.995   -18.261 -27.251 1.00 161.35 ? 307 GLU A CB  1 
ATOM   2338 C CG  . GLU A 1 307 ? 9.929   -16.745 -27.423 1.00 190.79 ? 307 GLU A CG  1 
ATOM   2339 C CD  . GLU A 1 307 ? 10.199  -15.878 -26.194 1.00 222.28 ? 307 GLU A CD  1 
ATOM   2340 O OE1 . GLU A 1 307 ? 9.611   -16.122 -25.118 1.00 251.62 ? 307 GLU A OE1 1 
ATOM   2341 O OE2 . GLU A 1 307 ? 10.982  -14.915 -26.318 1.00 229.50 ? 307 GLU A OE2 1 
ATOM   2342 N N   . ILE A 1 308 ? 9.022   -21.073 -27.903 1.00 161.23 ? 308 ILE A N   1 
ATOM   2343 C CA  . ILE A 1 308 ? 8.850   -22.471 -27.535 1.00 163.03 ? 308 ILE A CA  1 
ATOM   2344 C C   . ILE A 1 308 ? 9.265   -23.352 -28.700 1.00 154.08 ? 308 ILE A C   1 
ATOM   2345 O O   . ILE A 1 308 ? 9.901   -24.354 -28.444 1.00 141.10 ? 308 ILE A O   1 
ATOM   2346 C CB  . ILE A 1 308 ? 7.470   -22.850 -26.977 1.00 156.61 ? 308 ILE A CB  1 
ATOM   2347 C CG1 . ILE A 1 308 ? 7.212   -22.210 -25.611 1.00 171.49 ? 308 ILE A CG1 1 
ATOM   2348 C CG2 . ILE A 1 308 ? 7.369   -24.369 -26.873 1.00 156.08 ? 308 ILE A CG2 1 
ATOM   2349 C CD1 . ILE A 1 308 ? 5.912   -22.655 -24.958 1.00 188.73 ? 308 ILE A CD1 1 
ATOM   2350 N N   . THR A 1 309 ? 8.839   -22.975 -29.911 1.00 153.15 ? 309 THR A N   1 
ATOM   2351 C CA  . THR A 1 309 ? 9.006   -23.799 -31.094 1.00 153.28 ? 309 THR A CA  1 
ATOM   2352 C C   . THR A 1 309 ? 10.477  -24.133 -31.323 1.00 162.05 ? 309 THR A C   1 
ATOM   2353 O O   . THR A 1 309 ? 10.866  -25.293 -31.548 1.00 155.26 ? 309 THR A O   1 
ATOM   2354 C CB  . THR A 1 309 ? 8.466   -23.040 -32.309 1.00 175.52 ? 309 THR A CB  1 
ATOM   2355 O OG1 . THR A 1 309 ? 7.052   -23.179 -32.264 1.00 195.99 ? 309 THR A OG1 1 
ATOM   2356 C CG2 . THR A 1 309 ? 8.992   -23.554 -33.638 1.00 176.09 ? 309 THR A CG2 1 
ATOM   2357 N N   . ASP A 1 310 ? 11.266  -23.057 -31.277 1.00 177.06 ? 310 ASP A N   1 
ATOM   2358 C CA  . ASP A 1 310 ? 12.707  -23.142 -31.509 1.00 186.18 ? 310 ASP A CA  1 
ATOM   2359 C C   . ASP A 1 310 ? 13.349  -24.082 -30.493 1.00 180.04 ? 310 ASP A C   1 
ATOM   2360 O O   . ASP A 1 310 ? 14.171  -24.943 -30.849 1.00 184.54 ? 310 ASP A O   1 
ATOM   2361 C CB  . ASP A 1 310 ? 13.359  -21.778 -31.644 1.00 202.27 ? 310 ASP A CB  1 
ATOM   2362 C CG  . ASP A 1 310 ? 13.329  -21.211 -33.057 1.00 217.22 ? 310 ASP A CG  1 
ATOM   2363 O OD1 . ASP A 1 310 ? 13.745  -21.935 -33.991 1.00 206.55 ? 310 ASP A OD1 1 
ATOM   2364 O OD2 . ASP A 1 310 ? 12.897  -20.050 -33.216 1.00 237.57 ? 310 ASP A OD2 1 
ATOM   2365 N N   . ALA A 1 311 ? 12.937  -23.891 -29.233 1.00 163.06 ? 311 ALA A N   1 
ATOM   2366 C CA  . ALA A 1 311 ? 13.425  -24.684 -28.109 1.00 140.66 ? 311 ALA A CA  1 
ATOM   2367 C C   . ALA A 1 311 ? 13.154  -26.163 -28.356 1.00 125.47 ? 311 ALA A C   1 
ATOM   2368 O O   . ALA A 1 311 ? 14.032  -27.022 -28.175 1.00 118.02 ? 311 ALA A O   1 
ATOM   2369 C CB  . ALA A 1 311 ? 12.726  -24.216 -26.849 1.00 138.05 ? 311 ALA A CB  1 
ATOM   2370 N N   . VAL A 1 312 ? 11.914  -26.427 -28.773 1.00 132.70 ? 312 VAL A N   1 
ATOM   2371 C CA  . VAL A 1 312 ? 11.438  -27.781 -29.047 1.00 142.11 ? 312 VAL A CA  1 
ATOM   2372 C C   . VAL A 1 312 ? 12.295  -28.413 -30.126 1.00 138.08 ? 312 VAL A C   1 
ATOM   2373 O O   . VAL A 1 312 ? 12.706  -29.555 -29.987 1.00 136.25 ? 312 VAL A O   1 
ATOM   2374 C CB  . VAL A 1 312 ? 9.930   -27.992 -29.301 1.00 166.81 ? 312 VAL A CB  1 
ATOM   2375 C CG1 . VAL A 1 312 ? 9.627   -29.142 -30.270 1.00 149.28 ? 312 VAL A CG1 1 
ATOM   2376 C CG2 . VAL A 1 312 ? 9.180   -28.168 -27.984 1.00 193.93 ? 312 VAL A CG2 1 
ATOM   2377 N N   . ARG A 1 313 ? 12.547  -27.641 -31.182 1.00 148.95 ? 313 ARG A N   1 
ATOM   2378 C CA  . ARG A 1 313 ? 13.341  -28.082 -32.325 1.00 155.18 ? 313 ARG A CA  1 
ATOM   2379 C C   . ARG A 1 313 ? 14.738  -28.491 -31.852 1.00 161.59 ? 313 ARG A C   1 
ATOM   2380 O O   . ARG A 1 313 ? 15.241  -29.567 -32.240 1.00 156.02 ? 313 ARG A O   1 
ATOM   2381 C CB  . ARG A 1 313 ? 13.345  -27.041 -33.454 1.00 154.85 ? 313 ARG A CB  1 
ATOM   2382 C CG  . ARG A 1 313 ? 14.227  -27.352 -34.656 1.00 163.97 ? 313 ARG A CG  1 
ATOM   2383 C CD  . ARG A 1 313 ? 14.952  -26.089 -35.171 1.00 196.72 ? 313 ARG A CD  1 
ATOM   2384 N NE  . ARG A 1 313 ? 15.687  -25.362 -34.120 1.00 203.57 ? 313 ARG A NE  1 
ATOM   2385 C CZ  . ARG A 1 313 ? 16.459  -24.289 -34.241 1.00 186.89 ? 313 ARG A CZ  1 
ATOM   2386 N NH1 . ARG A 1 313 ? 16.822  -23.880 -35.443 1.00 194.02 ? 313 ARG A NH1 1 
ATOM   2387 N NH2 . ARG A 1 313 ? 16.883  -23.651 -33.157 1.00 173.91 ? 313 ARG A NH2 1 
ATOM   2388 N N   . ARG A 1 314 ? 15.318  -27.622 -31.012 1.00 165.49 ? 314 ARG A N   1 
ATOM   2389 C CA  . ARG A 1 314 ? 16.659  -27.859 -30.480 1.00 142.11 ? 314 ARG A CA  1 
ATOM   2390 C C   . ARG A 1 314 ? 16.704  -29.190 -29.709 1.00 132.87 ? 314 ARG A C   1 
ATOM   2391 O O   . ARG A 1 314 ? 17.606  -30.055 -29.888 1.00 132.03 ? 314 ARG A O   1 
ATOM   2392 C CB  . ARG A 1 314 ? 17.260  -26.678 -29.705 1.00 148.34 ? 314 ARG A CB  1 
ATOM   2393 C CG  . ARG A 1 314 ? 17.559  -25.513 -30.638 1.00 163.23 ? 314 ARG A CG  1 
ATOM   2394 C CD  . ARG A 1 314 ? 18.101  -24.295 -29.915 1.00 167.59 ? 314 ARG A CD  1 
ATOM   2395 N NE  . ARG A 1 314 ? 17.091  -23.532 -29.172 1.00 161.31 ? 314 ARG A NE  1 
ATOM   2396 C CZ  . ARG A 1 314 ? 17.054  -23.384 -27.838 1.00 165.34 ? 314 ARG A CZ  1 
ATOM   2397 N NH1 . ARG A 1 314 ? 17.851  -24.099 -27.055 1.00 167.31 ? 314 ARG A NH1 1 
ATOM   2398 N NH2 . ARG A 1 314 ? 16.202  -22.527 -27.281 1.00 147.42 ? 314 ARG A NH2 1 
ATOM   2399 N N   . THR A 1 315 ? 15.673  -29.326 -28.860 1.00 131.75 ? 315 THR A N   1 
ATOM   2400 C CA  . THR A 1 315 ? 15.526  -30.501 -28.003 1.00 125.02 ? 315 THR A CA  1 
ATOM   2401 C C   . THR A 1 315 ? 15.405  -31.741 -28.862 1.00 124.94 ? 315 THR A C   1 
ATOM   2402 O O   . THR A 1 315 ? 16.018  -32.752 -28.570 1.00 123.79 ? 315 THR A O   1 
ATOM   2403 C CB  . THR A 1 315 ? 14.330  -30.346 -27.067 1.00 125.71 ? 315 THR A CB  1 
ATOM   2404 O OG1 . THR A 1 315 ? 14.349  -28.996 -26.619 1.00 140.57 ? 315 THR A OG1 1 
ATOM   2405 C CG2 . THR A 1 315 ? 14.412  -31.293 -25.885 1.00 128.52 ? 315 THR A CG2 1 
ATOM   2406 N N   . GLY A 1 316 ? 14.598  -31.647 -29.913 1.00 135.82 ? 316 GLY A N   1 
ATOM   2407 C CA  . GLY A 1 316 ? 14.338  -32.723 -30.856 1.00 148.89 ? 316 GLY A CA  1 
ATOM   2408 C C   . GLY A 1 316 ? 15.639  -33.169 -31.482 1.00 139.62 ? 316 GLY A C   1 
ATOM   2409 O O   . GLY A 1 316 ? 15.883  -34.363 -31.560 1.00 133.84 ? 316 GLY A O   1 
ATOM   2410 N N   . GLU A 1 317 ? 16.446  -32.194 -31.907 1.00 147.59 ? 317 GLU A N   1 
ATOM   2411 C CA  . GLU A 1 317 ? 17.734  -32.458 -32.541 1.00 151.72 ? 317 GLU A CA  1 
ATOM   2412 C C   . GLU A 1 317 ? 18.626  -33.267 -31.587 1.00 147.31 ? 317 GLU A C   1 
ATOM   2413 O O   . GLU A 1 317 ? 19.240  -34.288 -31.982 1.00 159.96 ? 317 GLU A O   1 
ATOM   2414 C CB  . GLU A 1 317 ? 18.350  -31.210 -33.168 1.00 171.52 ? 317 GLU A CB  1 
ATOM   2415 C CG  . GLU A 1 317 ? 17.624  -30.758 -34.433 1.00 194.76 ? 317 GLU A CG  1 
ATOM   2416 C CD  . GLU A 1 317 ? 17.800  -29.304 -34.841 1.00 252.61 ? 317 GLU A CD  1 
ATOM   2417 O OE1 . GLU A 1 317 ? 18.554  -28.565 -34.164 1.00 294.95 ? 317 GLU A OE1 1 
ATOM   2418 O OE2 . GLU A 1 317 ? 17.164  -28.904 -35.842 1.00 293.06 ? 317 GLU A OE2 1 
ATOM   2419 N N   . VAL A 1 318 ? 18.651  -32.788 -30.335 1.00 141.87 ? 318 VAL A N   1 
ATOM   2420 C CA  . VAL A 1 318 ? 19.453  -33.408 -29.288 1.00 142.86 ? 318 VAL A CA  1 
ATOM   2421 C C   . VAL A 1 318 ? 19.020  -34.871 -29.097 1.00 163.15 ? 318 VAL A C   1 
ATOM   2422 O O   . VAL A 1 318 ? 19.845  -35.787 -29.003 1.00 168.91 ? 318 VAL A O   1 
ATOM   2423 C CB  . VAL A 1 318 ? 19.407  -32.644 -27.952 1.00 154.82 ? 318 VAL A CB  1 
ATOM   2424 C CG1 . VAL A 1 318 ? 20.086  -33.417 -26.819 1.00 137.75 ? 318 VAL A CG1 1 
ATOM   2425 C CG2 . VAL A 1 318 ? 19.992  -31.248 -28.093 1.00 186.48 ? 318 VAL A CG2 1 
ATOM   2426 N N   . LEU A 1 319 ? 17.705  -35.053 -29.040 1.00 182.25 ? 319 LEU A N   1 
ATOM   2427 C CA  . LEU A 1 319 ? 17.128  -36.371 -28.824 1.00 180.70 ? 319 LEU A CA  1 
ATOM   2428 C C   . LEU A 1 319 ? 17.482  -37.292 -29.970 1.00 171.81 ? 319 LEU A C   1 
ATOM   2429 O O   . LEU A 1 319 ? 17.823  -38.435 -29.729 1.00 179.04 ? 319 LEU A O   1 
ATOM   2430 C CB  . LEU A 1 319 ? 15.688  -36.440 -28.329 1.00 195.59 ? 319 LEU A CB  1 
ATOM   2431 C CG  . LEU A 1 319 ? 15.586  -36.467 -26.801 1.00 208.54 ? 319 LEU A CG  1 
ATOM   2432 C CD1 . LEU A 1 319 ? 14.132  -36.395 -26.350 1.00 218.42 ? 319 LEU A CD1 1 
ATOM   2433 C CD2 . LEU A 1 319 ? 16.292  -37.716 -26.274 1.00 179.43 ? 319 LEU A CD2 1 
ATOM   2434 N N   . SER A 1 320 ? 17.424  -36.771 -31.194 1.00 172.42 ? 320 SER A N   1 
ATOM   2435 C CA  . SER A 1 320 ? 17.773  -37.527 -32.394 1.00 176.02 ? 320 SER A CA  1 
ATOM   2436 C C   . SER A 1 320 ? 19.215  -37.999 -32.301 1.00 187.78 ? 320 SER A C   1 
ATOM   2437 O O   . SER A 1 320 ? 19.505  -39.162 -32.598 1.00 184.56 ? 320 SER A O   1 
ATOM   2438 C CB  . SER A 1 320 ? 17.491  -36.775 -33.663 1.00 175.84 ? 320 SER A CB  1 
ATOM   2439 O OG  . SER A 1 320 ? 17.715  -37.630 -34.776 1.00 169.61 ? 320 SER A OG  1 
ATOM   2440 N N   . GLY A 1 321 ? 20.090  -37.078 -31.886 1.00 195.80 ? 321 GLY A N   1 
ATOM   2441 C CA  . GLY A 1 321 ? 21.510  -37.362 -31.719 1.00 195.15 ? 321 GLY A CA  1 
ATOM   2442 C C   . GLY A 1 321 ? 21.709  -38.512 -30.732 1.00 194.82 ? 321 GLY A C   1 
ATOM   2443 O O   . GLY A 1 321 ? 22.461  -39.470 -30.972 1.00 227.49 ? 321 GLY A O   1 
ATOM   2444 N N   . LEU A 1 322 ? 20.994  -38.394 -29.613 1.00 178.31 ? 322 LEU A N   1 
ATOM   2445 C CA  . LEU A 1 322 ? 21.030  -39.376 -28.527 1.00 167.62 ? 322 LEU A CA  1 
ATOM   2446 C C   . LEU A 1 322 ? 20.564  -40.725 -29.085 1.00 168.09 ? 322 LEU A C   1 
ATOM   2447 O O   . LEU A 1 322 ? 21.135  -41.777 -28.841 1.00 167.86 ? 322 LEU A O   1 
ATOM   2448 C CB  . LEU A 1 322 ? 20.203  -38.946 -27.310 1.00 162.13 ? 322 LEU A CB  1 
ATOM   2449 C CG  . LEU A 1 322 ? 20.938  -38.195 -26.192 1.00 168.69 ? 322 LEU A CG  1 
ATOM   2450 C CD1 . LEU A 1 322 ? 21.299  -36.755 -26.532 1.00 166.84 ? 322 LEU A CD1 1 
ATOM   2451 C CD2 . LEU A 1 322 ? 20.169  -38.240 -24.878 1.00 175.70 ? 322 LEU A CD2 1 
ATOM   2452 N N   . GLY A 1 323 ? 19.590  -40.594 -29.996 1.00 180.71 ? 323 GLY A N   1 
ATOM   2453 C CA  . GLY A 1 323 ? 19.129  -41.652 -30.875 1.00 178.39 ? 323 GLY A CA  1 
ATOM   2454 C C   . GLY A 1 323 ? 17.684  -42.048 -30.574 1.00 178.35 ? 323 GLY A C   1 
ATOM   2455 O O   . GLY A 1 323 ? 17.311  -43.206 -30.711 1.00 168.22 ? 323 GLY A O   1 
ATOM   2456 N N   . HIS A 1 324 ? 16.871  -41.093 -30.120 1.00 196.24 ? 324 HIS A N   1 
ATOM   2457 C CA  . HIS A 1 324 ? 15.476  -41.405 -29.860 1.00 196.87 ? 324 HIS A CA  1 
ATOM   2458 C C   . HIS A 1 324 ? 14.680  -41.169 -31.133 1.00 207.99 ? 324 HIS A C   1 
ATOM   2459 O O   . HIS A 1 324 ? 14.755  -40.100 -31.734 1.00 228.47 ? 324 HIS A O   1 
ATOM   2460 C CB  . HIS A 1 324 ? 14.877  -40.591 -28.706 1.00 198.43 ? 324 HIS A CB  1 
ATOM   2461 C CG  . HIS A 1 324 ? 13.562  -41.137 -28.268 1.00 189.89 ? 324 HIS A CG  1 
ATOM   2462 N ND1 . HIS A 1 324 ? 12.393  -40.413 -28.141 1.00 181.31 ? 324 HIS A ND1 1 
ATOM   2463 C CD2 . HIS A 1 324 ? 13.261  -42.406 -27.978 1.00 201.56 ? 324 HIS A CD2 1 
ATOM   2464 C CE1 . HIS A 1 324 ? 11.426  -41.234 -27.762 1.00 202.37 ? 324 HIS A CE1 1 
ATOM   2465 N NE2 . HIS A 1 324 ? 11.936  -42.447 -27.642 1.00 225.09 ? 324 HIS A NE2 1 
ATOM   2466 N N   . ARG A 1 325 ? 13.922  -42.193 -31.524 1.00 199.42 ? 325 ARG A N   1 
ATOM   2467 C CA  . ARG A 1 325 ? 13.015  -42.112 -32.654 1.00 181.30 ? 325 ARG A CA  1 
ATOM   2468 C C   . ARG A 1 325 ? 11.598  -42.264 -32.108 1.00 177.93 ? 325 ARG A C   1 
ATOM   2469 O O   . ARG A 1 325 ? 11.381  -42.992 -31.143 1.00 169.26 ? 325 ARG A O   1 
ATOM   2470 C CB  . ARG A 1 325 ? 13.518  -43.033 -33.773 1.00 188.40 ? 325 ARG A CB  1 
ATOM   2471 C CG  . ARG A 1 325 ? 14.755  -42.413 -34.421 1.00 202.62 ? 325 ARG A CG  1 
ATOM   2472 C CD  . ARG A 1 325 ? 15.854  -43.222 -35.069 1.00 225.27 ? 325 ARG A CD  1 
ATOM   2473 N NE  . ARG A 1 325 ? 16.700  -44.005 -34.162 1.00 256.99 ? 325 ARG A NE  1 
ATOM   2474 C CZ  . ARG A 1 325 ? 17.751  -44.736 -34.536 1.00 297.68 ? 325 ARG A CZ  1 
ATOM   2475 N NH1 . ARG A 1 325 ? 18.246  -44.631 -35.753 1.00 331.31 ? 325 ARG A NH1 1 
ATOM   2476 N NH2 . ARG A 1 325 ? 18.340  -45.543 -33.671 1.00 311.78 ? 325 ARG A NH2 1 
ATOM   2477 N N   . GLY A 1 326 ? 10.657  -41.509 -32.682 1.00 205.02 ? 326 GLY A N   1 
ATOM   2478 C CA  . GLY A 1 326 ? 9.296   -41.450 -32.180 1.00 214.76 ? 326 GLY A CA  1 
ATOM   2479 C C   . GLY A 1 326 ? 8.921   -40.028 -31.765 1.00 198.66 ? 326 GLY A C   1 
ATOM   2480 O O   . GLY A 1 326 ? 9.074   -39.107 -32.566 1.00 196.42 ? 326 GLY A O   1 
ATOM   2481 N N   . ALA A 1 327 ? 8.450   -39.885 -30.531 1.00 181.22 ? 327 ALA A N   1 
ATOM   2482 C CA  . ALA A 1 327 ? 7.804   -38.677 -30.062 1.00 161.44 ? 327 ALA A CA  1 
ATOM   2483 C C   . ALA A 1 327 ? 8.319   -38.295 -28.675 1.00 146.15 ? 327 ALA A C   1 
ATOM   2484 O O   . ALA A 1 327 ? 8.518   -39.110 -27.773 1.00 150.00 ? 327 ALA A O   1 
ATOM   2485 C CB  . ALA A 1 327 ? 6.309   -38.862 -30.083 1.00 173.42 ? 327 ALA A CB  1 
ATOM   2486 N N   . PHE A 1 328 ? 8.479   -36.990 -28.508 1.00 127.08 ? 328 PHE A N   1 
ATOM   2487 C CA  . PHE A 1 328 ? 8.969   -36.374 -27.284 1.00 119.63 ? 328 PHE A CA  1 
ATOM   2488 C C   . PHE A 1 328 ? 8.108   -35.163 -26.922 1.00 106.40 ? 328 PHE A C   1 
ATOM   2489 O O   . PHE A 1 328 ? 7.542   -34.414 -27.753 1.00 108.57 ? 328 PHE A O   1 
ATOM   2490 C CB  . PHE A 1 328 ? 10.475  -36.076 -27.342 1.00 140.66 ? 328 PHE A CB  1 
ATOM   2491 C CG  . PHE A 1 328 ? 10.756  -34.963 -28.344 1.00 148.92 ? 328 PHE A CG  1 
ATOM   2492 C CD1 . PHE A 1 328 ? 10.646  -33.634 -27.956 1.00 150.34 ? 328 PHE A CD1 1 
ATOM   2493 C CD2 . PHE A 1 328 ? 11.055  -35.237 -29.679 1.00 149.54 ? 328 PHE A CD2 1 
ATOM   2494 C CE1 . PHE A 1 328 ? 10.843  -32.614 -28.869 1.00 158.80 ? 328 PHE A CE1 1 
ATOM   2495 C CE2 . PHE A 1 328 ? 11.271  -34.208 -30.584 1.00 134.36 ? 328 PHE A CE2 1 
ATOM   2496 C CZ  . PHE A 1 328 ? 11.167  -32.904 -30.179 1.00 145.63 ? 328 PHE A CZ  1 
ATOM   2497 N N   . GLY A 1 329 ? 8.111   -34.910 -25.618 1.00 96.16  ? 329 GLY A N   1 
ATOM   2498 C CA  . GLY A 1 329 ? 7.351   -33.844 -24.983 1.00 96.32  ? 329 GLY A CA  1 
ATOM   2499 C C   . GLY A 1 329 ? 8.219   -33.054 -24.019 1.00 101.15 ? 329 GLY A C   1 
ATOM   2500 O O   . GLY A 1 329 ? 8.983   -33.616 -23.217 1.00 97.52  ? 329 GLY A O   1 
ATOM   2501 N N   . VAL A 1 330 ? 8.068   -31.723 -24.123 1.00 116.33 ? 330 VAL A N   1 
ATOM   2502 C CA  . VAL A 1 330 ? 8.677   -30.784 -23.174 1.00 121.34 ? 330 VAL A CA  1 
ATOM   2503 C C   . VAL A 1 330 ? 7.621   -29.913 -22.480 1.00 128.61 ? 330 VAL A C   1 
ATOM   2504 O O   . VAL A 1 330 ? 6.822   -29.276 -23.158 1.00 126.30 ? 330 VAL A O   1 
ATOM   2505 C CB  . VAL A 1 330 ? 9.687   -29.857 -23.854 1.00 117.57 ? 330 VAL A CB  1 
ATOM   2506 C CG1 . VAL A 1 330 ? 10.580  -29.222 -22.804 1.00 126.44 ? 330 VAL A CG1 1 
ATOM   2507 C CG2 . VAL A 1 330 ? 10.519  -30.588 -24.898 1.00 134.17 ? 330 VAL A CG2 1 
ATOM   2508 N N   . ASP A 1 331 ? 7.592   -30.021 -21.145 1.00 135.26 ? 331 ASP A N   1 
ATOM   2509 C CA  . ASP A 1 331 ? 6.712   -29.237 -20.314 1.00 158.36 ? 331 ASP A CA  1 
ATOM   2510 C C   . ASP A 1 331 ? 7.518   -28.066 -19.747 1.00 153.00 ? 331 ASP A C   1 
ATOM   2511 O O   . ASP A 1 331 ? 8.668   -28.200 -19.305 1.00 155.58 ? 331 ASP A O   1 
ATOM   2512 C CB  . ASP A 1 331 ? 5.969   -30.073 -19.279 1.00 192.51 ? 331 ASP A CB  1 
ATOM   2513 C CG  . ASP A 1 331 ? 4.733   -29.410 -18.671 1.00 247.06 ? 331 ASP A CG  1 
ATOM   2514 O OD1 . ASP A 1 331 ? 4.235   -28.410 -19.249 1.00 265.08 ? 331 ASP A OD1 1 
ATOM   2515 O OD2 . ASP A 1 331 ? 4.269   -29.885 -17.605 1.00 263.99 ? 331 ASP A OD2 1 
ATOM   2516 N N   . PHE A 1 332 ? 6.854   -26.909 -19.757 1.00 135.66 ? 332 PHE A N   1 
ATOM   2517 C CA  . PHE A 1 332 ? 7.419   -25.638 -19.362 1.00 114.09 ? 332 PHE A CA  1 
ATOM   2518 C C   . PHE A 1 332 ? 6.564   -24.925 -18.307 1.00 103.50 ? 332 PHE A C   1 
ATOM   2519 O O   . PHE A 1 332 ? 5.345   -25.061 -18.171 1.00 129.24 ? 332 PHE A O   1 
ATOM   2520 C CB  . PHE A 1 332 ? 7.469   -24.714 -20.582 1.00 120.67 ? 332 PHE A CB  1 
ATOM   2521 C CG  . PHE A 1 332 ? 8.255   -25.189 -21.799 1.00 134.00 ? 332 PHE A CG  1 
ATOM   2522 C CD1 . PHE A 1 332 ? 9.643   -25.182 -21.808 1.00 131.39 ? 332 PHE A CD1 1 
ATOM   2523 C CD2 . PHE A 1 332 ? 7.608   -25.591 -22.961 1.00 150.83 ? 332 PHE A CD2 1 
ATOM   2524 C CE1 . PHE A 1 332 ? 10.353  -25.584 -22.929 1.00 136.11 ? 332 PHE A CE1 1 
ATOM   2525 C CE2 . PHE A 1 332 ? 8.322   -25.997 -24.084 1.00 148.74 ? 332 PHE A CE2 1 
ATOM   2526 C CZ  . PHE A 1 332 ? 9.693   -25.986 -24.067 1.00 141.27 ? 332 PHE A CZ  1 
ATOM   2527 N N   . VAL A 1 333 ? 7.258   -24.049 -17.587 1.00 104.19 ? 333 VAL A N   1 
ATOM   2528 C CA  . VAL A 1 333 ? 6.691   -23.023 -16.719 1.00 115.01 ? 333 VAL A CA  1 
ATOM   2529 C C   . VAL A 1 333 ? 7.204   -21.631 -17.104 1.00 133.14 ? 333 VAL A C   1 
ATOM   2530 O O   . VAL A 1 333 ? 8.359   -21.400 -17.491 1.00 159.14 ? 333 VAL A O   1 
ATOM   2531 C CB  . VAL A 1 333 ? 6.846   -23.310 -15.206 1.00 108.96 ? 333 VAL A CB  1 
ATOM   2532 C CG1 . VAL A 1 333 ? 6.108   -24.564 -14.773 1.00 99.41  ? 333 VAL A CG1 1 
ATOM   2533 C CG2 . VAL A 1 333 ? 8.298   -23.412 -14.771 1.00 102.46 ? 333 VAL A CG2 1 
ATOM   2534 N N   . VAL A 1 334 ? 6.317   -20.650 -16.870 1.00 133.81 ? 334 VAL A N   1 
ATOM   2535 C CA  . VAL A 1 334 ? 6.608   -19.224 -17.038 1.00 121.17 ? 334 VAL A CA  1 
ATOM   2536 C C   . VAL A 1 334 ? 6.651   -18.527 -15.675 1.00 150.96 ? 334 VAL A C   1 
ATOM   2537 O O   . VAL A 1 334 ? 5.645   -18.485 -14.984 1.00 178.32 ? 334 VAL A O   1 
ATOM   2538 C CB  . VAL A 1 334 ? 5.640   -18.520 -18.018 1.00 101.89 ? 334 VAL A CB  1 
ATOM   2539 C CG1 . VAL A 1 334 ? 5.841   -17.029 -18.067 1.00 117.08 ? 334 VAL A CG1 1 
ATOM   2540 C CG2 . VAL A 1 334 ? 5.771   -18.998 -19.440 1.00 102.93 ? 334 VAL A CG2 1 
ATOM   2541 N N   . ALA A 1 335 ? 7.817   -17.959 -15.301 1.00 178.84 ? 335 ALA A N   1 
ATOM   2542 C CA  . ALA A 1 335 ? 8.149   -17.675 -13.913 1.00 184.24 ? 335 ALA A CA  1 
ATOM   2543 C C   . ALA A 1 335 ? 8.305   -16.171 -13.656 1.00 212.65 ? 335 ALA A C   1 
ATOM   2544 O O   . ALA A 1 335 ? 9.416   -15.657 -13.534 1.00 247.33 ? 335 ALA A O   1 
ATOM   2545 C CB  . ALA A 1 335 ? 9.391   -18.455 -13.508 1.00 154.63 ? 335 ALA A CB  1 
ATOM   2546 N N   . GLY A 1 336 ? 7.161   -15.482 -13.599 1.00 219.62 ? 336 GLY A N   1 
ATOM   2547 C CA  . GLY A 1 336 ? 7.131   -14.036 -13.455 1.00 233.32 ? 336 GLY A CA  1 
ATOM   2548 C C   . GLY A 1 336 ? 7.946   -13.378 -14.563 1.00 240.04 ? 336 GLY A C   1 
ATOM   2549 O O   . GLY A 1 336 ? 7.691   -13.609 -15.746 1.00 239.10 ? 336 GLY A O   1 
ATOM   2550 N N   . GLU A 1 337 ? 8.949   -12.592 -14.157 1.00 225.21 ? 337 GLU A N   1 
ATOM   2551 C CA  . GLU A 1 337 ? 9.784   -11.887 -15.115 1.00 231.22 ? 337 GLU A CA  1 
ATOM   2552 C C   . GLU A 1 337 ? 11.017  -12.717 -15.455 1.00 213.66 ? 337 GLU A C   1 
ATOM   2553 O O   . GLU A 1 337 ? 11.781  -12.357 -16.350 1.00 239.92 ? 337 GLU A O   1 
ATOM   2554 C CB  . GLU A 1 337 ? 10.153  -10.489 -14.619 1.00 253.78 ? 337 GLU A CB  1 
ATOM   2555 C CG  . GLU A 1 337 ? 8.973   -9.522  -14.643 1.00 265.87 ? 337 GLU A CG  1 
ATOM   2556 C CD  . GLU A 1 337 ? 9.380   -8.074  -14.865 1.00 279.68 ? 337 GLU A CD  1 
ATOM   2557 O OE1 . GLU A 1 337 ? 10.159  -7.524  -14.054 1.00 269.40 ? 337 GLU A OE1 1 
ATOM   2558 O OE2 . GLU A 1 337 ? 8.917   -7.503  -15.876 1.00 303.71 ? 337 GLU A OE2 1 
ATOM   2559 N N   . ARG A 1 338 ? 11.183  -13.837 -14.746 1.00 188.28 ? 338 ARG A N   1 
ATOM   2560 C CA  . ARG A 1 338 ? 12.356  -14.684 -14.886 1.00 189.25 ? 338 ARG A CA  1 
ATOM   2561 C C   . ARG A 1 338 ? 12.351  -15.426 -16.225 1.00 183.91 ? 338 ARG A C   1 
ATOM   2562 O O   . ARG A 1 338 ? 13.385  -15.936 -16.647 1.00 179.39 ? 338 ARG A O   1 
ATOM   2563 C CB  . ARG A 1 338 ? 12.424  -15.631 -13.686 1.00 164.43 ? 338 ARG A CB  1 
ATOM   2564 C CG  . ARG A 1 338 ? 13.551  -16.634 -13.835 1.00 138.83 ? 338 ARG A CG  1 
ATOM   2565 C CD  . ARG A 1 338 ? 13.532  -17.548 -12.652 1.00 140.37 ? 338 ARG A CD  1 
ATOM   2566 N NE  . ARG A 1 338 ? 14.594  -18.526 -12.906 1.00 150.40 ? 338 ARG A NE  1 
ATOM   2567 C CZ  . ARG A 1 338 ? 14.938  -19.493 -12.074 1.00 146.70 ? 338 ARG A CZ  1 
ATOM   2568 N NH1 . ARG A 1 338 ? 14.408  -19.530 -10.864 1.00 134.27 ? 338 ARG A NH1 1 
ATOM   2569 N NH2 . ARG A 1 338 ? 15.819  -20.403 -12.451 1.00 146.14 ? 338 ARG A NH2 1 
ATOM   2570 N N   . GLY A 1 339 ? 11.176  -15.507 -16.861 1.00 178.71 ? 339 GLY A N   1 
ATOM   2571 C CA  . GLY A 1 339 ? 11.000  -16.073 -18.186 1.00 169.26 ? 339 GLY A CA  1 
ATOM   2572 C C   . GLY A 1 339 ? 10.489  -17.515 -18.160 1.00 156.45 ? 339 GLY A C   1 
ATOM   2573 O O   . GLY A 1 339 ? 9.803   -17.981 -17.245 1.00 165.05 ? 339 GLY A O   1 
ATOM   2574 N N   . LEU A 1 340 ? 10.941  -18.274 -19.166 1.00 144.84 ? 340 LEU A N   1 
ATOM   2575 C CA  . LEU A 1 340 ? 10.361  -19.569 -19.529 1.00 132.50 ? 340 LEU A CA  1 
ATOM   2576 C C   . LEU A 1 340 ? 11.386  -20.699 -19.373 1.00 134.16 ? 340 LEU A C   1 
ATOM   2577 O O   . LEU A 1 340 ? 12.500  -20.603 -19.889 1.00 150.75 ? 340 LEU A O   1 
ATOM   2578 C CB  . LEU A 1 340 ? 9.763   -19.528 -20.933 1.00 128.16 ? 340 LEU A CB  1 
ATOM   2579 C CG  . LEU A 1 340 ? 9.061   -20.797 -21.429 1.00 131.99 ? 340 LEU A CG  1 
ATOM   2580 C CD1 . LEU A 1 340 ? 7.943   -20.343 -22.323 1.00 166.21 ? 340 LEU A CD1 1 
ATOM   2581 C CD2 . LEU A 1 340 ? 9.948   -21.681 -22.273 1.00 137.21 ? 340 LEU A CD2 1 
ATOM   2582 N N   . LEU A 1 341 ? 11.003  -21.699 -18.585 1.00 131.54 ? 341 LEU A N   1 
ATOM   2583 C CA  . LEU A 1 341 ? 11.900  -22.734 -18.100 1.00 131.85 ? 341 LEU A CA  1 
ATOM   2584 C C   . LEU A 1 341 ? 11.256  -24.107 -18.322 1.00 148.98 ? 341 LEU A C   1 
ATOM   2585 O O   . LEU A 1 341 ? 10.095  -24.354 -17.981 1.00 153.22 ? 341 LEU A O   1 
ATOM   2586 C CB  . LEU A 1 341 ? 12.239  -22.501 -16.623 1.00 112.48 ? 341 LEU A CB  1 
ATOM   2587 C CG  . LEU A 1 341 ? 12.393  -21.045 -16.167 1.00 109.22 ? 341 LEU A CG  1 
ATOM   2588 C CD1 . LEU A 1 341 ? 12.277  -20.916 -14.662 1.00 113.54 ? 341 LEU A CD1 1 
ATOM   2589 C CD2 . LEU A 1 341 ? 13.694  -20.443 -16.650 1.00 115.24 ? 341 LEU A CD2 1 
ATOM   2590 N N   . ALA A 1 342 ? 12.058  -24.996 -18.918 1.00 178.98 ? 342 ALA A N   1 
ATOM   2591 C CA  . ALA A 1 342 ? 11.692  -26.375 -19.183 1.00 152.59 ? 342 ALA A CA  1 
ATOM   2592 C C   . ALA A 1 342 ? 11.891  -27.200 -17.918 1.00 150.66 ? 342 ALA A C   1 
ATOM   2593 O O   . ALA A 1 342 ? 12.977  -27.230 -17.345 1.00 141.27 ? 342 ALA A O   1 
ATOM   2594 C CB  . ALA A 1 342 ? 12.550  -26.908 -20.311 1.00 146.67 ? 342 ALA A CB  1 
ATOM   2595 N N   . VAL A 1 343 ? 10.837  -27.942 -17.539 1.00 154.68 ? 343 VAL A N   1 
ATOM   2596 C CA  . VAL A 1 343 ? 10.732  -28.573 -16.231 1.00 155.52 ? 343 VAL A CA  1 
ATOM   2597 C C   . VAL A 1 343 ? 10.695  -30.097 -16.385 1.00 159.87 ? 343 VAL A C   1 
ATOM   2598 O O   . VAL A 1 343 ? 11.263  -30.816 -15.561 1.00 188.55 ? 343 VAL A O   1 
ATOM   2599 C CB  . VAL A 1 343 ? 9.464   -28.081 -15.510 1.00 137.05 ? 343 VAL A CB  1 
ATOM   2600 C CG1 . VAL A 1 343 ? 9.389   -26.567 -15.461 1.00 135.98 ? 343 VAL A CG1 1 
ATOM   2601 C CG2 . VAL A 1 343 ? 8.212   -28.604 -16.188 1.00 151.06 ? 343 VAL A CG2 1 
ATOM   2602 N N   . GLU A 1 344 ? 10.064  -30.537 -17.481 1.00 148.23 ? 344 GLU A N   1 
ATOM   2603 C CA  . GLU A 1 344 ? 9.895   -31.940 -17.778 1.00 157.11 ? 344 GLU A CA  1 
ATOM   2604 C C   . GLU A 1 344 ? 10.289  -32.232 -19.228 1.00 129.65 ? 344 GLU A C   1 
ATOM   2605 O O   . GLU A 1 344 ? 10.067  -31.482 -20.196 1.00 103.44 ? 344 GLU A O   1 
ATOM   2606 C CB  . GLU A 1 344 ? 8.563   -32.535 -17.311 1.00 217.56 ? 344 GLU A CB  1 
ATOM   2607 C CG  . GLU A 1 344 ? 8.621   -33.060 -15.877 1.00 257.48 ? 344 GLU A CG  1 
ATOM   2608 C CD  . GLU A 1 344 ? 7.618   -34.133 -15.511 1.00 289.44 ? 344 GLU A CD  1 
ATOM   2609 O OE1 . GLU A 1 344 ? 7.755   -35.276 -15.993 1.00 293.21 ? 344 GLU A OE1 1 
ATOM   2610 O OE2 . GLU A 1 344 ? 6.704   -33.823 -14.724 1.00 306.43 ? 344 GLU A OE2 1 
ATOM   2611 N N   . ILE A 1 345 ? 10.795  -33.468 -19.381 1.00 119.19 ? 345 ILE A N   1 
ATOM   2612 C CA  . ILE A 1 345 ? 10.966  -34.149 -20.659 1.00 126.29 ? 345 ILE A CA  1 
ATOM   2613 C C   . ILE A 1 345 ? 10.266  -35.505 -20.611 1.00 143.16 ? 345 ILE A C   1 
ATOM   2614 O O   . ILE A 1 345 ? 10.457  -36.307 -19.678 1.00 172.16 ? 345 ILE A O   1 
ATOM   2615 C CB  . ILE A 1 345 ? 12.439  -34.401 -21.001 1.00 138.14 ? 345 ILE A CB  1 
ATOM   2616 C CG1 . ILE A 1 345 ? 12.685  -34.251 -22.496 1.00 148.57 ? 345 ILE A CG1 1 
ATOM   2617 C CG2 . ILE A 1 345 ? 12.886  -35.774 -20.484 1.00 134.23 ? 345 ILE A CG2 1 
ATOM   2618 C CD1 . ILE A 1 345 ? 12.673  -32.804 -22.963 1.00 155.77 ? 345 ILE A CD1 1 
ATOM   2619 N N   . ASN A 1 346 ? 9.501   -35.755 -21.685 1.00 134.46 ? 346 ASN A N   1 
ATOM   2620 C CA  . ASN A 1 346 ? 8.717   -36.979 -21.824 1.00 131.51 ? 346 ASN A CA  1 
ATOM   2621 C C   . ASN A 1 346 ? 9.082   -37.732 -23.111 1.00 137.12 ? 346 ASN A C   1 
ATOM   2622 O O   . ASN A 1 346 ? 9.047   -37.132 -24.184 1.00 122.41 ? 346 ASN A O   1 
ATOM   2623 C CB  . ASN A 1 346 ? 7.230   -36.648 -21.801 1.00 136.87 ? 346 ASN A CB  1 
ATOM   2624 C CG  . ASN A 1 346 ? 6.784   -35.968 -20.524 1.00 143.02 ? 346 ASN A CG  1 
ATOM   2625 O OD1 . ASN A 1 346 ? 6.733   -36.612 -19.464 1.00 149.86 ? 346 ASN A OD1 1 
ATOM   2626 N ND2 . ASN A 1 346 ? 6.439   -34.685 -20.607 1.00 143.79 ? 346 ASN A ND2 1 
ATOM   2627 N N   . LEU A 1 347 ? 9.572   -38.965 -22.929 1.00 142.51 ? 347 LEU A N   1 
ATOM   2628 C CA  . LEU A 1 347 ? 9.910   -39.831 -24.035 1.00 150.07 ? 347 LEU A CA  1 
ATOM   2629 C C   . LEU A 1 347 ? 8.690   -40.720 -24.216 1.00 149.22 ? 347 LEU A C   1 
ATOM   2630 O O   . LEU A 1 347 ? 8.629   -41.820 -23.673 1.00 152.34 ? 347 LEU A O   1 
ATOM   2631 C CB  . LEU A 1 347 ? 11.187  -40.612 -23.724 1.00 161.20 ? 347 LEU A CB  1 
ATOM   2632 C CG  . LEU A 1 347 ? 12.487  -39.815 -23.571 1.00 152.32 ? 347 LEU A CG  1 
ATOM   2633 C CD1 . LEU A 1 347 ? 13.647  -40.795 -23.591 1.00 146.70 ? 347 LEU A CD1 1 
ATOM   2634 C CD2 . LEU A 1 347 ? 12.650  -38.753 -24.645 1.00 162.19 ? 347 LEU A CD2 1 
ATOM   2635 N N   . ARG A 1 348 ? 7.684   -40.159 -24.889 1.00 153.00 ? 348 ARG A N   1 
ATOM   2636 C CA  . ARG A 1 348 ? 6.372   -40.770 -25.061 1.00 148.43 ? 348 ARG A CA  1 
ATOM   2637 C C   . ARG A 1 348 ? 5.456   -39.746 -25.731 1.00 136.25 ? 348 ARG A C   1 
ATOM   2638 O O   . ARG A 1 348 ? 5.825   -38.573 -25.868 1.00 139.89 ? 348 ARG A O   1 
ATOM   2639 C CB  . ARG A 1 348 ? 5.759   -41.289 -23.751 1.00 130.41 ? 348 ARG A CB  1 
ATOM   2640 C CG  . ARG A 1 348 ? 5.556   -40.240 -22.668 1.00 119.03 ? 348 ARG A CG  1 
ATOM   2641 C CD  . ARG A 1 348 ? 4.949   -40.798 -21.393 1.00 128.69 ? 348 ARG A CD  1 
ATOM   2642 N NE  . ARG A 1 348 ? 4.759   -39.804 -20.329 1.00 128.87 ? 348 ARG A NE  1 
ATOM   2643 C CZ  . ARG A 1 348 ? 4.064   -38.668 -20.422 1.00 147.78 ? 348 ARG A CZ  1 
ATOM   2644 N NH1 . ARG A 1 348 ? 3.458   -38.304 -21.550 1.00 141.11 ? 348 ARG A NH1 1 
ATOM   2645 N NH2 . ARG A 1 348 ? 3.983   -37.888 -19.360 1.00 197.78 ? 348 ARG A NH2 1 
ATOM   2646 N N   . LYS A 1 349 ? 4.289   -40.218 -26.187 1.00 118.27 ? 349 LYS A N   1 
ATOM   2647 C CA  . LYS A 1 349 ? 3.258   -39.315 -26.664 1.00 120.47 ? 349 LYS A CA  1 
ATOM   2648 C C   . LYS A 1 349 ? 2.727   -38.552 -25.450 1.00 134.72 ? 349 LYS A C   1 
ATOM   2649 O O   . LYS A 1 349 ? 2.983   -38.931 -24.305 1.00 134.10 ? 349 LYS A O   1 
ATOM   2650 C CB  . LYS A 1 349 ? 2.189   -40.130 -27.395 1.00 104.63 ? 349 LYS A CB  1 
ATOM   2651 C CG  . LYS A 1 349 ? 2.707   -40.980 -28.532 1.00 111.18 ? 349 LYS A CG  1 
ATOM   2652 C CD  . LYS A 1 349 ? 1.627   -41.846 -29.173 1.00 118.80 ? 349 LYS A CD  1 
ATOM   2653 C CE  . LYS A 1 349 ? 2.115   -42.806 -30.224 1.00 121.87 ? 349 LYS A CE  1 
ATOM   2654 N NZ  . LYS A 1 349 ? 3.026   -42.204 -31.200 1.00 138.28 ? 349 LYS A NZ  1 
ATOM   2655 N N   . VAL A 1 350 ? 2.012   -37.449 -25.671 1.00 133.13 ? 350 VAL A N   1 
ATOM   2656 C CA  . VAL A 1 350 ? 1.476   -36.782 -24.499 1.00 127.43 ? 350 VAL A CA  1 
ATOM   2657 C C   . VAL A 1 350 ? 0.022   -36.455 -24.773 1.00 136.90 ? 350 VAL A C   1 
ATOM   2658 O O   . VAL A 1 350 ? -0.433  -36.645 -25.895 1.00 145.70 ? 350 VAL A O   1 
ATOM   2659 C CB  . VAL A 1 350 ? 2.224   -35.525 -24.041 1.00 128.47 ? 350 VAL A CB  1 
ATOM   2660 C CG1 . VAL A 1 350 ? 2.213   -35.456 -22.512 1.00 124.76 ? 350 VAL A CG1 1 
ATOM   2661 C CG2 . VAL A 1 350 ? 3.636   -35.468 -24.625 1.00 125.20 ? 350 VAL A CG2 1 
ATOM   2662 N N   . GLY A 1 351 ? -0.684  -36.003 -23.734 1.00 137.70 ? 351 GLY A N   1 
ATOM   2663 C CA  . GLY A 1 351 ? -2.104  -35.721 -23.855 1.00 146.08 ? 351 GLY A CA  1 
ATOM   2664 C C   . GLY A 1 351 ? -2.399  -34.985 -25.158 1.00 132.94 ? 351 GLY A C   1 
ATOM   2665 O O   . GLY A 1 351 ? -3.098  -35.490 -26.036 1.00 134.05 ? 351 GLY A O   1 
ATOM   2666 N N   . PRO A 1 352 ? -1.861  -33.760 -25.330 1.00 115.64 ? 352 PRO A N   1 
ATOM   2667 C CA  . PRO A 1 352 ? -2.115  -32.954 -26.504 1.00 116.14 ? 352 PRO A CA  1 
ATOM   2668 C C   . PRO A 1 352 ? -2.029  -33.720 -27.804 1.00 123.39 ? 352 PRO A C   1 
ATOM   2669 O O   . PRO A 1 352 ? -2.703  -33.293 -28.708 1.00 118.08 ? 352 PRO A O   1 
ATOM   2670 C CB  . PRO A 1 352 ? -1.050  -31.904 -26.376 1.00 106.59 ? 352 PRO A CB  1 
ATOM   2671 C CG  . PRO A 1 352 ? -0.129  -32.444 -25.318 1.00 121.86 ? 352 PRO A CG  1 
ATOM   2672 C CD  . PRO A 1 352 ? -1.094  -33.020 -24.324 1.00 106.60 ? 352 PRO A CD  1 
ATOM   2673 N N   . SER A 1 353 ? -1.207  -34.765 -27.886 1.00 138.41 ? 353 SER A N   1 
ATOM   2674 C CA  . SER A 1 353 ? -0.859  -35.378 -29.161 1.00 153.40 ? 353 SER A CA  1 
ATOM   2675 C C   . SER A 1 353 ? -2.132  -35.893 -29.858 1.00 134.56 ? 353 SER A C   1 
ATOM   2676 O O   . SER A 1 353 ? -2.436  -35.618 -31.039 1.00 139.48 ? 353 SER A O   1 
ATOM   2677 C CB  . SER A 1 353 ? 0.048   -36.565 -28.925 1.00 166.21 ? 353 SER A CB  1 
ATOM   2678 O OG  . SER A 1 353 ? -0.652  -37.528 -28.141 1.00 164.63 ? 353 SER A OG  1 
ATOM   2679 N N   . HIS A 1 354 ? -2.849  -36.680 -29.047 1.00 117.82 ? 354 HIS A N   1 
ATOM   2680 C CA  . HIS A 1 354 ? -4.069  -37.335 -29.524 1.00 132.87 ? 354 HIS A CA  1 
ATOM   2681 C C   . HIS A 1 354 ? -5.097  -36.278 -29.932 1.00 123.99 ? 354 HIS A C   1 
ATOM   2682 O O   . HIS A 1 354 ? -5.737  -36.417 -30.988 1.00 101.86 ? 354 HIS A O   1 
ATOM   2683 C CB  . HIS A 1 354 ? -4.545  -38.460 -28.596 1.00 142.08 ? 354 HIS A CB  1 
ATOM   2684 C CG  . HIS A 1 354 ? -5.669  -38.088 -27.681 1.00 118.85 ? 354 HIS A CG  1 
ATOM   2685 N ND1 . HIS A 1 354 ? -5.409  -37.519 -26.449 1.00 119.16 ? 354 HIS A ND1 1 
ATOM   2686 C CD2 . HIS A 1 354 ? -6.987  -38.180 -27.775 1.00 96.17  ? 354 HIS A CD2 1 
ATOM   2687 C CE1 . HIS A 1 354 ? -6.539  -37.275 -25.819 1.00 100.04 ? 354 HIS A CE1 1 
ATOM   2688 N NE2 . HIS A 1 354 ? -7.503  -37.675 -26.603 1.00 99.80  ? 354 HIS A NE2 1 
ATOM   2689 N N   . VAL A 1 355 ? -5.202  -35.232 -29.081 1.00 112.96 ? 355 VAL A N   1 
ATOM   2690 C CA  . VAL A 1 355 ? -6.144  -34.150 -29.326 1.00 106.05 ? 355 VAL A CA  1 
ATOM   2691 C C   . VAL A 1 355 ? -5.850  -33.479 -30.670 1.00 97.29  ? 355 VAL A C   1 
ATOM   2692 O O   . VAL A 1 355 ? -6.732  -33.199 -31.476 1.00 86.16  ? 355 VAL A O   1 
ATOM   2693 C CB  . VAL A 1 355 ? -6.133  -33.186 -28.125 1.00 112.99 ? 355 VAL A CB  1 
ATOM   2694 C CG1 . VAL A 1 355 ? -6.989  -31.953 -28.352 1.00 132.63 ? 355 VAL A CG1 1 
ATOM   2695 C CG2 . VAL A 1 355 ? -6.558  -33.893 -26.844 1.00 117.97 ? 355 VAL A CG2 1 
ATOM   2696 N N   . VAL A 1 356 ? -4.557  -33.233 -30.885 1.00 104.44 ? 356 VAL A N   1 
ATOM   2697 C CA  . VAL A 1 356 ? -4.011  -32.587 -32.061 1.00 109.60 ? 356 VAL A CA  1 
ATOM   2698 C C   . VAL A 1 356 ? -4.392  -33.386 -33.276 1.00 111.05 ? 356 VAL A C   1 
ATOM   2699 O O   . VAL A 1 356 ? -4.783  -32.744 -34.244 1.00 95.92  ? 356 VAL A O   1 
ATOM   2700 C CB  . VAL A 1 356 ? -2.479  -32.432 -32.025 1.00 99.10  ? 356 VAL A CB  1 
ATOM   2701 C CG1 . VAL A 1 356 ? -1.910  -32.176 -33.420 1.00 101.30 ? 356 VAL A CG1 1 
ATOM   2702 C CG2 . VAL A 1 356 ? -2.019  -31.399 -31.013 1.00 95.75  ? 356 VAL A CG2 1 
ATOM   2703 N N   . ARG A 1 357 ? -4.279  -34.725 -33.211 1.00 132.17 ? 357 ARG A N   1 
ATOM   2704 C CA  . ARG A 1 357 ? -4.619  -35.580 -34.336 1.00 149.52 ? 357 ARG A CA  1 
ATOM   2705 C C   . ARG A 1 357 ? -6.060  -35.339 -34.800 1.00 155.33 ? 357 ARG A C   1 
ATOM   2706 O O   . ARG A 1 357 ? -6.359  -35.133 -35.994 1.00 188.89 ? 357 ARG A O   1 
ATOM   2707 C CB  . ARG A 1 357 ? -4.477  -37.074 -34.045 1.00 141.88 ? 357 ARG A CB  1 
ATOM   2708 C CG  . ARG A 1 357 ? -2.997  -37.414 -34.018 1.00 169.42 ? 357 ARG A CG  1 
ATOM   2709 C CD  . ARG A 1 357 ? -2.680  -38.833 -34.368 1.00 158.51 ? 357 ARG A CD  1 
ATOM   2710 N NE  . ARG A 1 357 ? -2.311  -39.067 -35.769 1.00 159.26 ? 357 ARG A NE  1 
ATOM   2711 C CZ  . ARG A 1 357 ? -3.060  -39.660 -36.697 1.00 175.46 ? 357 ARG A CZ  1 
ATOM   2712 N NH1 . ARG A 1 357 ? -4.355  -39.833 -36.528 1.00 178.03 ? 357 ARG A NH1 1 
ATOM   2713 N NH2 . ARG A 1 357 ? -2.538  -40.027 -37.846 1.00 184.48 ? 357 ARG A NH2 1 
ATOM   2714 N N   . TYR A 1 358 ? -6.922  -35.358 -33.772 1.00 145.17 ? 358 TYR A N   1 
ATOM   2715 C CA  . TYR A 1 358 ? -8.363  -35.180 -33.975 1.00 136.24 ? 358 TYR A CA  1 
ATOM   2716 C C   . TYR A 1 358 ? -8.632  -33.827 -34.626 1.00 128.69 ? 358 TYR A C   1 
ATOM   2717 O O   . TYR A 1 358 ? -9.419  -33.731 -35.580 1.00 111.82 ? 358 TYR A O   1 
ATOM   2718 C CB  . TYR A 1 358 ? -9.380  -35.230 -32.828 1.00 122.84 ? 358 TYR A CB  1 
ATOM   2719 C CG  . TYR A 1 358 ? -9.835  -36.563 -32.253 1.00 107.30 ? 358 TYR A CG  1 
ATOM   2720 C CD1 . TYR A 1 358 ? -9.162  -37.139 -31.180 1.00 116.59 ? 358 TYR A CD1 1 
ATOM   2721 C CD2 . TYR A 1 358 ? -10.985 -37.191 -32.705 1.00 104.75 ? 358 TYR A CD2 1 
ATOM   2722 C CE1 . TYR A 1 358 ? -9.594  -38.328 -30.612 1.00 137.38 ? 358 TYR A CE1 1 
ATOM   2723 C CE2 . TYR A 1 358 ? -11.422 -38.387 -32.149 1.00 114.81 ? 358 TYR A CE2 1 
ATOM   2724 C CZ  . TYR A 1 358 ? -10.724 -38.970 -31.099 1.00 127.10 ? 358 TYR A CZ  1 
ATOM   2725 O OH  . TYR A 1 358 ? -11.127 -40.155 -30.507 1.00 109.63 ? 358 TYR A OH  1 
ATOM   2726 N N   . ALA A 1 359 ? -7.959  -32.806 -34.089 1.00 121.94 ? 359 ALA A N   1 
ATOM   2727 C CA  . ALA A 1 359 ? -8.087  -31.435 -34.561 1.00 119.67 ? 359 ALA A CA  1 
ATOM   2728 C C   . ALA A 1 359 ? -7.728  -31.354 -36.039 1.00 116.08 ? 359 ALA A C   1 
ATOM   2729 O O   . ALA A 1 359 ? -8.449  -30.740 -36.843 1.00 126.91 ? 359 ALA A O   1 
ATOM   2730 C CB  . ALA A 1 359 ? -7.185  -30.542 -33.743 1.00 121.66 ? 359 ALA A CB  1 
ATOM   2731 N N   . GLU A 1 360 ? -6.600  -31.989 -36.364 1.00 106.56 ? 360 GLU A N   1 
ATOM   2732 C CA  . GLU A 1 360 ? -6.063  -32.015 -37.720 1.00 119.56 ? 360 GLU A CA  1 
ATOM   2733 C C   . GLU A 1 360 ? -7.090  -32.631 -38.662 1.00 129.24 ? 360 GLU A C   1 
ATOM   2734 O O   . GLU A 1 360 ? -7.356  -32.093 -39.753 1.00 137.35 ? 360 GLU A O   1 
ATOM   2735 C CB  . GLU A 1 360 ? -4.729  -32.767 -37.737 1.00 129.72 ? 360 GLU A CB  1 
ATOM   2736 C CG  . GLU A 1 360 ? -3.478  -31.917 -37.503 1.00 156.42 ? 360 GLU A CG  1 
ATOM   2737 C CD  . GLU A 1 360 ? -2.164  -32.658 -37.746 1.00 191.17 ? 360 GLU A CD  1 
ATOM   2738 O OE1 . GLU A 1 360 ? -2.215  -33.903 -37.823 1.00 220.37 ? 360 GLU A OE1 1 
ATOM   2739 O OE2 . GLU A 1 360 ? -1.092  -32.024 -37.890 1.00 206.72 ? 360 GLU A OE2 1 
ATOM   2740 N N   . ALA A 1 361 ? -7.649  -33.758 -38.211 1.00 142.34 ? 361 ALA A N   1 
ATOM   2741 C CA  . ALA A 1 361 ? -8.642  -34.504 -38.976 1.00 173.08 ? 361 ALA A CA  1 
ATOM   2742 C C   . ALA A 1 361 ? -9.845  -33.612 -39.280 1.00 157.11 ? 361 ALA A C   1 
ATOM   2743 O O   . ALA A 1 361 ? -10.334 -33.562 -40.424 1.00 164.24 ? 361 ALA A O   1 
ATOM   2744 C CB  . ALA A 1 361 ? -9.024  -35.761 -38.222 1.00 217.80 ? 361 ALA A CB  1 
ATOM   2745 N N   . LEU A 1 362 ? -10.289 -32.912 -38.234 1.00 127.34 ? 362 LEU A N   1 
ATOM   2746 C CA  . LEU A 1 362 ? -11.443 -32.028 -38.316 1.00 122.92 ? 362 LEU A CA  1 
ATOM   2747 C C   . LEU A 1 362 ? -11.190 -30.941 -39.357 1.00 133.87 ? 362 LEU A C   1 
ATOM   2748 O O   . LEU A 1 362 ? -12.058 -30.656 -40.209 1.00 149.32 ? 362 LEU A O   1 
ATOM   2749 C CB  . LEU A 1 362 ? -11.799 -31.507 -36.927 1.00 121.02 ? 362 LEU A CB  1 
ATOM   2750 C CG  . LEU A 1 362 ? -12.409 -32.565 -35.999 1.00 128.06 ? 362 LEU A CG  1 
ATOM   2751 C CD1 . LEU A 1 362 ? -12.561 -32.156 -34.544 1.00 136.97 ? 362 LEU A CD1 1 
ATOM   2752 C CD2 . LEU A 1 362 ? -13.752 -33.003 -36.559 1.00 143.74 ? 362 LEU A CD2 1 
ATOM   2753 N N   . VAL A 1 363 ? -9.982  -30.374 -39.288 1.00 140.47 ? 363 VAL A N   1 
ATOM   2754 C CA  . VAL A 1 363 ? -9.603  -29.275 -40.163 1.00 139.90 ? 363 VAL A CA  1 
ATOM   2755 C C   . VAL A 1 363 ? -9.578  -29.789 -41.599 1.00 140.54 ? 363 VAL A C   1 
ATOM   2756 O O   . VAL A 1 363 ? -10.087 -29.149 -42.529 1.00 151.75 ? 363 VAL A O   1 
ATOM   2757 C CB  . VAL A 1 363 ? -8.305  -28.572 -39.739 1.00 148.81 ? 363 VAL A CB  1 
ATOM   2758 C CG1 . VAL A 1 363 ? -8.017  -27.369 -40.628 1.00 173.57 ? 363 VAL A CG1 1 
ATOM   2759 C CG2 . VAL A 1 363 ? -8.379  -28.137 -38.276 1.00 143.90 ? 363 VAL A CG2 1 
ATOM   2760 N N   . GLY A 1 364 ? -8.882  -30.921 -41.750 1.00 128.01 ? 364 GLY A N   1 
ATOM   2761 C CA  . GLY A 1 364 ? -8.594  -31.501 -43.046 1.00 146.60 ? 364 GLY A CA  1 
ATOM   2762 C C   . GLY A 1 364 ? -7.126  -31.341 -43.418 1.00 162.21 ? 364 GLY A C   1 
ATOM   2763 O O   . GLY A 1 364 ? -6.675  -31.917 -44.415 1.00 171.28 ? 364 GLY A O   1 
ATOM   2764 N N   . ALA A 1 365 ? -6.396  -30.575 -42.590 1.00 161.59 ? 365 ALA A N   1 
ATOM   2765 C CA  . ALA A 1 365 ? -4.998  -30.272 -42.863 1.00 171.25 ? 365 ALA A CA  1 
ATOM   2766 C C   . ALA A 1 365 ? -4.117  -30.582 -41.655 1.00 167.75 ? 365 ALA A C   1 
ATOM   2767 O O   . ALA A 1 365 ? -4.600  -30.730 -40.533 1.00 153.44 ? 365 ALA A O   1 
ATOM   2768 C CB  . ALA A 1 365 ? -4.844  -28.832 -43.309 1.00 183.78 ? 365 ALA A CB  1 
ATOM   2769 N N   . ARG A 1 366 ? -2.812  -30.676 -41.928 1.00 172.84 ? 366 ARG A N   1 
ATOM   2770 C CA  . ARG A 1 366 ? -1.779  -30.922 -40.940 1.00 169.11 ? 366 ARG A CA  1 
ATOM   2771 C C   . ARG A 1 366 ? -1.517  -29.608 -40.213 1.00 162.84 ? 366 ARG A C   1 
ATOM   2772 O O   . ARG A 1 366 ? -2.051  -28.580 -40.625 1.00 157.30 ? 366 ARG A O   1 
ATOM   2773 C CB  . ARG A 1 366 ? -0.513  -31.349 -41.690 1.00 184.51 ? 366 ARG A CB  1 
ATOM   2774 C CG  . ARG A 1 366 ? -0.777  -31.984 -43.053 1.00 187.23 ? 366 ARG A CG  1 
ATOM   2775 C CD  . ARG A 1 366 ? 0.421   -32.760 -43.520 1.00 183.53 ? 366 ARG A CD  1 
ATOM   2776 N NE  . ARG A 1 366 ? 0.672   -33.771 -42.489 1.00 187.50 ? 366 ARG A NE  1 
ATOM   2777 C CZ  . ARG A 1 366 ? 0.825   -35.064 -42.706 1.00 192.74 ? 366 ARG A CZ  1 
ATOM   2778 N NH1 . ARG A 1 366 ? 0.876   -35.514 -43.946 1.00 194.75 ? 366 ARG A NH1 1 
ATOM   2779 N NH2 . ARG A 1 366 ? 0.940   -35.880 -41.674 1.00 202.75 ? 366 ARG A NH2 1 
ATOM   2780 N N   . VAL A 1 367 ? -0.640  -29.653 -39.201 1.00 175.65 ? 367 VAL A N   1 
ATOM   2781 C CA  . VAL A 1 367 ? -0.424  -28.569 -38.249 1.00 197.07 ? 367 VAL A CA  1 
ATOM   2782 C C   . VAL A 1 367 ? -0.266  -27.209 -38.933 1.00 226.25 ? 367 VAL A C   1 
ATOM   2783 O O   . VAL A 1 367 ? -0.765  -26.222 -38.398 1.00 268.78 ? 367 VAL A O   1 
ATOM   2784 C CB  . VAL A 1 367 ? 0.615   -28.828 -37.130 1.00 193.18 ? 367 VAL A CB  1 
ATOM   2785 C CG1 . VAL A 1 367 ? 1.727   -27.781 -37.045 1.00 191.53 ? 367 VAL A CG1 1 
ATOM   2786 C CG2 . VAL A 1 367 ? -0.054  -29.011 -35.770 1.00 156.03 ? 367 VAL A CG2 1 
ATOM   2787 N N   . GLY A 1 368 ? 0.431   -27.155 -40.082 1.00 211.30 ? 368 GLY A N   1 
ATOM   2788 C CA  . GLY A 1 368 ? 0.587   -25.913 -40.829 1.00 210.92 ? 368 GLY A CA  1 
ATOM   2789 C C   . GLY A 1 368 ? 1.978   -25.288 -40.687 1.00 223.11 ? 368 GLY A C   1 
ATOM   2790 O O   . GLY A 1 368 ? 2.639   -25.449 -39.661 1.00 216.96 ? 368 GLY A O   1 
ATOM   2791 N N   . ALA A 1 369 ? 2.393   -24.545 -41.727 1.00 231.87 ? 369 ALA A N   1 
ATOM   2792 C CA  . ALA A 1 369 ? 3.711   -23.921 -41.827 1.00 221.16 ? 369 ALA A CA  1 
ATOM   2793 C C   . ALA A 1 369 ? 4.687   -24.606 -40.877 1.00 250.40 ? 369 ALA A C   1 
ATOM   2794 O O   . ALA A 1 369 ? 4.954   -25.796 -41.029 1.00 308.48 ? 369 ALA A O   1 
ATOM   2795 C CB  . ALA A 1 369 ? 3.642   -22.428 -41.577 1.00 177.27 ? 369 ALA A CB  1 
ATOM   2796 N N   . ASP A 1 370 ? 5.180   -23.871 -39.874 1.00 242.29 ? 370 ASP A N   1 
ATOM   2797 C CA  . ASP A 1 370 ? 5.954   -24.528 -38.837 1.00 253.40 ? 370 ASP A CA  1 
ATOM   2798 C C   . ASP A 1 370 ? 5.173   -24.450 -37.535 1.00 258.57 ? 370 ASP A C   1 
ATOM   2799 O O   . ASP A 1 370 ? 5.405   -25.232 -36.613 1.00 290.00 ? 370 ASP A O   1 
ATOM   2800 C CB  . ASP A 1 370 ? 7.382   -24.018 -38.770 1.00 254.92 ? 370 ASP A CB  1 
ATOM   2801 C CG  . ASP A 1 370 ? 8.372   -24.960 -38.101 1.00 255.52 ? 370 ASP A CG  1 
ATOM   2802 O OD1 . ASP A 1 370 ? 8.516   -26.116 -38.573 1.00 226.40 ? 370 ASP A OD1 1 
ATOM   2803 O OD2 . ASP A 1 370 ? 8.996   -24.528 -37.115 1.00 273.35 ? 370 ASP A OD2 1 
ATOM   2804 N N   . GLY A 1 371 ? 4.231   -23.501 -37.501 1.00 231.02 ? 371 GLY A N   1 
ATOM   2805 C CA  . GLY A 1 371 ? 3.359   -23.309 -36.354 1.00 212.39 ? 371 GLY A CA  1 
ATOM   2806 C C   . GLY A 1 371 ? 2.039   -22.658 -36.756 1.00 207.10 ? 371 GLY A C   1 
ATOM   2807 O O   . GLY A 1 371 ? 2.004   -21.874 -37.708 1.00 200.56 ? 371 GLY A O   1 
ATOM   2808 N N   . MET A 1 372 ? 0.970   -23.046 -36.042 1.00 200.66 ? 372 MET A N   1 
ATOM   2809 C CA  . MET A 1 372 ? -0.363  -22.471 -36.174 1.00 207.70 ? 372 MET A CA  1 
ATOM   2810 C C   . MET A 1 372 ? -1.115  -23.059 -37.375 1.00 226.77 ? 372 MET A C   1 
ATOM   2811 O O   . MET A 1 372 ? -0.809  -22.788 -38.539 1.00 266.70 ? 372 MET A O   1 
ATOM   2812 C CB  . MET A 1 372 ? -0.334  -20.940 -36.240 1.00 195.95 ? 372 MET A CB  1 
ATOM   2813 C CG  . MET A 1 372 ? -1.653  -20.285 -35.852 1.00 184.46 ? 372 MET A CG  1 
ATOM   2814 S SD  . MET A 1 372 ? -2.113  -18.892 -36.903 1.00 216.75 ? 372 MET A SD  1 
ATOM   2815 C CE  . MET A 1 372 ? -2.794  -19.498 -38.452 1.00 184.89 ? 372 MET A CE  1 
ATOM   2816 N N   . LEU A 1 373 ? -2.134  -23.860 -37.056 1.00 206.73 ? 373 LEU A N   1 
ATOM   2817 C CA  . LEU A 1 373 ? -3.010  -24.549 -37.987 1.00 192.17 ? 373 LEU A CA  1 
ATOM   2818 C C   . LEU A 1 373 ? -3.898  -23.542 -38.698 1.00 177.96 ? 373 LEU A C   1 
ATOM   2819 O O   . LEU A 1 373 ? -4.240  -22.523 -38.108 1.00 187.00 ? 373 LEU A O   1 
ATOM   2820 C CB  . LEU A 1 373 ? -3.856  -25.440 -37.078 1.00 213.60 ? 373 LEU A CB  1 
ATOM   2821 C CG  . LEU A 1 373 ? -4.730  -26.506 -37.748 1.00 218.23 ? 373 LEU A CG  1 
ATOM   2822 C CD1 . LEU A 1 373 ? -3.881  -27.295 -38.725 1.00 249.04 ? 373 LEU A CD1 1 
ATOM   2823 C CD2 . LEU A 1 373 ? -5.308  -27.442 -36.687 1.00 183.96 ? 373 LEU A CD2 1 
ATOM   2824 N N   . ARG A 1 374 ? -4.250  -23.846 -39.951 1.00 169.81 ? 374 ARG A N   1 
ATOM   2825 C CA  . ARG A 1 374 ? -5.110  -22.959 -40.720 1.00 201.44 ? 374 ARG A CA  1 
ATOM   2826 C C   . ARG A 1 374 ? -5.991  -23.802 -41.637 1.00 202.96 ? 374 ARG A C   1 
ATOM   2827 O O   . ARG A 1 374 ? -5.525  -24.801 -42.191 1.00 181.62 ? 374 ARG A O   1 
ATOM   2828 C CB  . ARG A 1 374 ? -4.309  -21.979 -41.587 1.00 233.79 ? 374 ARG A CB  1 
ATOM   2829 C CG  . ARG A 1 374 ? -2.910  -21.642 -41.096 1.00 256.26 ? 374 ARG A CG  1 
ATOM   2830 C CD  . ARG A 1 374 ? -2.117  -20.579 -41.861 1.00 225.31 ? 374 ARG A CD  1 
ATOM   2831 N NE  . ARG A 1 374 ? -0.676  -20.840 -41.736 1.00 201.52 ? 374 ARG A NE  1 
ATOM   2832 C CZ  . ARG A 1 374 ? 0.197   -20.159 -40.996 1.00 192.68 ? 374 ARG A CZ  1 
ATOM   2833 N NH1 . ARG A 1 374 ? -0.184  -19.072 -40.354 1.00 217.16 ? 374 ARG A NH1 1 
ATOM   2834 N NH2 . ARG A 1 374 ? 1.451   -20.560 -40.898 1.00 173.13 ? 374 ARG A NH2 1 
ATOM   2835 N N   . GLY A 1 375 ? -7.242  -23.357 -41.811 1.00 207.86 ? 375 GLY A N   1 
ATOM   2836 C CA  . GLY A 1 375 ? -8.224  -24.058 -42.623 1.00 194.08 ? 375 GLY A CA  1 
ATOM   2837 C C   . GLY A 1 375 ? -7.947  -23.930 -44.119 1.00 197.87 ? 375 GLY A C   1 
ATOM   2838 O O   . GLY A 1 375 ? -6.972  -23.307 -44.535 1.00 197.13 ? 375 GLY A O   1 
ATOM   2839 N N   . ALA A 1 376 ? -8.843  -24.523 -44.917 1.00 200.34 ? 376 ALA A N   1 
ATOM   2840 C CA  . ALA A 1 376 ? -8.776  -24.519 -46.370 1.00 201.61 ? 376 ALA A CA  1 
ATOM   2841 C C   . ALA A 1 376 ? -8.573  -23.102 -46.905 1.00 204.06 ? 376 ALA A C   1 
ATOM   2842 O O   . ALA A 1 376 ? -7.731  -22.871 -47.772 1.00 202.81 ? 376 ALA A O   1 
ATOM   2843 C CB  . ALA A 1 376 ? -10.041 -25.140 -46.924 1.00 188.76 ? 376 ALA A CB  1 
ATOM   2844 N N   . ASP A 1 377 ? -9.353  -22.166 -46.354 1.00 219.83 ? 377 ASP A N   1 
ATOM   2845 C CA  . ASP A 1 377 ? -9.394  -20.773 -46.771 1.00 225.39 ? 377 ASP A CA  1 
ATOM   2846 C C   . ASP A 1 377 ? -8.150  -20.028 -46.301 1.00 214.29 ? 377 ASP A C   1 
ATOM   2847 O O   . ASP A 1 377 ? -7.896  -18.919 -46.761 1.00 219.35 ? 377 ASP A O   1 
ATOM   2848 C CB  . ASP A 1 377 ? -10.640 -20.077 -46.247 1.00 231.73 ? 377 ASP A CB  1 
ATOM   2849 C CG  . ASP A 1 377 ? -10.904 -20.238 -44.757 1.00 230.87 ? 377 ASP A CG  1 
ATOM   2850 O OD1 . ASP A 1 377 ? -10.038 -20.822 -44.050 1.00 224.66 ? 377 ASP A OD1 1 
ATOM   2851 O OD2 . ASP A 1 377 ? -11.981 -19.788 -44.316 1.00 241.15 ? 377 ASP A OD2 1 
ATOM   2852 N N   . GLY A 1 378 ? -7.403  -20.634 -45.370 1.00 214.25 ? 378 GLY A N   1 
ATOM   2853 C CA  . GLY A 1 378 ? -6.156  -20.073 -44.868 1.00 214.46 ? 378 GLY A CA  1 
ATOM   2854 C C   . GLY A 1 378 ? -6.323  -19.470 -43.476 1.00 202.90 ? 378 GLY A C   1 
ATOM   2855 O O   . GLY A 1 378 ? -5.337  -19.292 -42.756 1.00 190.70 ? 378 GLY A O   1 
ATOM   2856 N N   . ARG A 1 379 ? -7.584  -19.158 -43.138 1.00 193.66 ? 379 ARG A N   1 
ATOM   2857 C CA  . ARG A 1 379 ? -8.000  -18.573 -41.876 1.00 195.07 ? 379 ARG A CA  1 
ATOM   2858 C C   . ARG A 1 379 ? -7.626  -19.483 -40.715 1.00 174.81 ? 379 ARG A C   1 
ATOM   2859 O O   . ARG A 1 379 ? -7.863  -20.699 -40.734 1.00 152.79 ? 379 ARG A O   1 
ATOM   2860 C CB  . ARG A 1 379 ? -9.490  -18.208 -41.883 1.00 197.21 ? 379 ARG A CB  1 
ATOM   2861 C CG  . ARG A 1 379 ? -9.906  -17.009 -42.726 1.00 210.44 ? 379 ARG A CG  1 
ATOM   2862 C CD  . ARG A 1 379 ? -9.422  -15.688 -42.159 1.00 228.84 ? 379 ARG A CD  1 
ATOM   2863 N NE  . ARG A 1 379 ? -9.524  -15.659 -40.695 1.00 237.39 ? 379 ARG A NE  1 
ATOM   2864 C CZ  . ARG A 1 379 ? -10.629 -15.792 -39.970 1.00 253.04 ? 379 ARG A CZ  1 
ATOM   2865 N NH1 . ARG A 1 379 ? -11.813 -15.840 -40.557 1.00 260.33 ? 379 ARG A NH1 1 
ATOM   2866 N NH2 . ARG A 1 379 ? -10.541 -15.868 -38.652 1.00 276.04 ? 379 ARG A NH2 1 
ATOM   2867 N N   . PRO A 1 380 ? -7.049  -18.858 -39.668 1.00 174.88 ? 380 PRO A N   1 
ATOM   2868 C CA  . PRO A 1 380 ? -6.610  -19.546 -38.465 1.00 172.80 ? 380 PRO A CA  1 
ATOM   2869 C C   . PRO A 1 380 ? -7.675  -20.377 -37.754 1.00 172.29 ? 380 PRO A C   1 
ATOM   2870 O O   . PRO A 1 380 ? -8.885  -20.130 -37.866 1.00 177.41 ? 380 PRO A O   1 
ATOM   2871 C CB  . PRO A 1 380 ? -6.097  -18.407 -37.561 1.00 170.15 ? 380 PRO A CB  1 
ATOM   2872 C CG  . PRO A 1 380 ? -5.716  -17.321 -38.534 1.00 173.91 ? 380 PRO A CG  1 
ATOM   2873 C CD  . PRO A 1 380 ? -6.818  -17.407 -39.570 1.00 178.68 ? 380 PRO A CD  1 
ATOM   2874 N N   . VAL A 1 381 ? -7.173  -21.360 -37.004 1.00 161.60 ? 381 VAL A N   1 
ATOM   2875 C CA  . VAL A 1 381 ? -7.995  -22.308 -36.271 1.00 146.31 ? 381 VAL A CA  1 
ATOM   2876 C C   . VAL A 1 381 ? -7.509  -22.402 -34.824 1.00 140.80 ? 381 VAL A C   1 
ATOM   2877 O O   . VAL A 1 381 ? -6.315  -22.521 -34.520 1.00 125.89 ? 381 VAL A O   1 
ATOM   2878 C CB  . VAL A 1 381 ? -8.050  -23.695 -36.926 1.00 149.64 ? 381 VAL A CB  1 
ATOM   2879 C CG1 . VAL A 1 381 ? -9.041  -24.595 -36.195 1.00 158.48 ? 381 VAL A CG1 1 
ATOM   2880 C CG2 . VAL A 1 381 ? -8.361  -23.614 -38.420 1.00 139.47 ? 381 VAL A CG2 1 
ATOM   2881 N N   . TYR A 1 382 ? -8.503  -22.337 -33.934 1.00 132.22 ? 382 TYR A N   1 
ATOM   2882 C CA  . TYR A 1 382 ? -8.318  -22.357 -32.492 1.00 140.46 ? 382 TYR A CA  1 
ATOM   2883 C C   . TYR A 1 382 ? -9.248  -23.407 -31.877 1.00 135.57 ? 382 TYR A C   1 
ATOM   2884 O O   . TYR A 1 382 ? -10.454 -23.468 -32.172 1.00 129.69 ? 382 TYR A O   1 
ATOM   2885 C CB  . TYR A 1 382 ? -8.624  -21.027 -31.792 1.00 133.51 ? 382 TYR A CB  1 
ATOM   2886 C CG  . TYR A 1 382 ? -7.897  -19.831 -32.378 1.00 142.61 ? 382 TYR A CG  1 
ATOM   2887 C CD1 . TYR A 1 382 ? -6.596  -19.536 -31.990 1.00 155.60 ? 382 TYR A CD1 1 
ATOM   2888 C CD2 . TYR A 1 382 ? -8.507  -19.012 -33.328 1.00 148.18 ? 382 TYR A CD2 1 
ATOM   2889 C CE1 . TYR A 1 382 ? -5.914  -18.460 -32.534 1.00 172.25 ? 382 TYR A CE1 1 
ATOM   2890 C CE2 . TYR A 1 382 ? -7.834  -17.939 -33.884 1.00 163.66 ? 382 TYR A CE2 1 
ATOM   2891 C CZ  . TYR A 1 382 ? -6.536  -17.664 -33.483 1.00 180.80 ? 382 TYR A CZ  1 
ATOM   2892 O OH  . TYR A 1 382 ? -5.864  -16.601 -34.016 1.00 213.08 ? 382 TYR A OH  1 
ATOM   2893 N N   . TYR A 1 383 ? -8.661  -24.186 -30.960 1.00 138.31 ? 383 TYR A N   1 
ATOM   2894 C CA  . TYR A 1 383 ? -9.358  -25.245 -30.259 1.00 122.73 ? 383 TYR A CA  1 
ATOM   2895 C C   . TYR A 1 383 ? -9.120  -25.169 -28.753 1.00 118.98 ? 383 TYR A C   1 
ATOM   2896 O O   . TYR A 1 383 ? -8.041  -24.846 -28.227 1.00 123.92 ? 383 TYR A O   1 
ATOM   2897 C CB  . TYR A 1 383 ? -9.183  -26.620 -30.904 1.00 138.59 ? 383 TYR A CB  1 
ATOM   2898 C CG  . TYR A 1 383 ? -7.853  -27.350 -30.759 1.00 152.48 ? 383 TYR A CG  1 
ATOM   2899 C CD1 . TYR A 1 383 ? -7.567  -28.103 -29.621 1.00 161.36 ? 383 TYR A CD1 1 
ATOM   2900 C CD2 . TYR A 1 383 ? -6.922  -27.363 -31.796 1.00 151.36 ? 383 TYR A CD2 1 
ATOM   2901 C CE1 . TYR A 1 383 ? -6.380  -28.814 -29.505 1.00 148.13 ? 383 TYR A CE1 1 
ATOM   2902 C CE2 . TYR A 1 383 ? -5.742  -28.089 -31.701 1.00 150.84 ? 383 TYR A CE2 1 
ATOM   2903 C CZ  . TYR A 1 383 ? -5.468  -28.805 -30.546 1.00 148.47 ? 383 TYR A CZ  1 
ATOM   2904 O OH  . TYR A 1 383 ? -4.306  -29.496 -30.411 1.00 149.83 ? 383 TYR A OH  1 
ATOM   2905 N N   . THR A 1 384 ? -10.180 -25.593 -28.051 1.00 111.84 ? 384 THR A N   1 
ATOM   2906 C CA  . THR A 1 384 ? -10.194 -25.802 -26.606 1.00 121.73 ? 384 THR A CA  1 
ATOM   2907 C C   . THR A 1 384 ? -10.619 -27.242 -26.283 1.00 135.35 ? 384 THR A C   1 
ATOM   2908 O O   . THR A 1 384 ? -11.655 -27.717 -26.772 1.00 160.92 ? 384 THR A O   1 
ATOM   2909 C CB  . THR A 1 384 ? -11.174 -24.834 -25.952 1.00 125.68 ? 384 THR A CB  1 
ATOM   2910 O OG1 . THR A 1 384 ? -10.766 -23.523 -26.327 1.00 161.66 ? 384 THR A OG1 1 
ATOM   2911 C CG2 . THR A 1 384 ? -11.176 -24.955 -24.439 1.00 119.47 ? 384 THR A CG2 1 
ATOM   2912 N N   . HIS A 1 385 ? -9.774  -27.897 -25.476 1.00 119.51 ? 385 HIS A N   1 
ATOM   2913 C CA  . HIS A 1 385 ? -9.939  -29.299 -25.147 1.00 123.68 ? 385 HIS A CA  1 
ATOM   2914 C C   . HIS A 1 385 ? -9.919  -29.513 -23.628 1.00 123.95 ? 385 HIS A C   1 
ATOM   2915 O O   . HIS A 1 385 ? -9.027  -29.030 -22.938 1.00 123.48 ? 385 HIS A O   1 
ATOM   2916 C CB  . HIS A 1 385 ? -8.840  -30.149 -25.780 1.00 136.16 ? 385 HIS A CB  1 
ATOM   2917 C CG  . HIS A 1 385 ? -8.754  -31.506 -25.155 1.00 146.54 ? 385 HIS A CG  1 
ATOM   2918 N ND1 . HIS A 1 385 ? -9.477  -32.597 -25.593 1.00 142.13 ? 385 HIS A ND1 1 
ATOM   2919 C CD2 . HIS A 1 385 ? -8.039  -31.925 -24.094 1.00 141.60 ? 385 HIS A CD2 1 
ATOM   2920 C CE1 . HIS A 1 385 ? -9.184  -33.634 -24.826 1.00 139.57 ? 385 HIS A CE1 1 
ATOM   2921 N NE2 . HIS A 1 385 ? -8.312  -33.247 -23.908 1.00 141.50 ? 385 HIS A NE2 1 
ATOM   2922 N N   . GLY A 1 386 ? -10.937 -30.222 -23.160 1.00 127.99 ? 386 GLY A N   1 
ATOM   2923 C CA  . GLY A 1 386 ? -11.190 -30.419 -21.752 1.00 119.94 ? 386 GLY A CA  1 
ATOM   2924 C C   . GLY A 1 386 ? -11.599 -31.860 -21.495 1.00 102.22 ? 386 GLY A C   1 
ATOM   2925 O O   . GLY A 1 386 ? -12.413 -32.464 -22.208 1.00 99.77  ? 386 GLY A O   1 
ATOM   2926 N N   . ARG A 1 387 ? -11.085 -32.382 -20.387 1.00 100.93 ? 387 ARG A N   1 
ATOM   2927 C CA  . ARG A 1 387 ? -11.681 -33.518 -19.673 1.00 110.50 ? 387 ARG A CA  1 
ATOM   2928 C C   . ARG A 1 387 ? -12.756 -33.005 -18.722 1.00 108.48 ? 387 ARG A C   1 
ATOM   2929 O O   . ARG A 1 387 ? -12.482 -32.122 -17.888 1.00 98.29  ? 387 ARG A O   1 
ATOM   2930 C CB  . ARG A 1 387 ? -10.628 -34.269 -18.844 1.00 126.01 ? 387 ARG A CB  1 
ATOM   2931 C CG  . ARG A 1 387 ? -9.286  -34.459 -19.533 1.00 128.71 ? 387 ARG A CG  1 
ATOM   2932 C CD  . ARG A 1 387 ? -8.285  -35.323 -18.804 1.00 97.61  ? 387 ARG A CD  1 
ATOM   2933 N NE  . ARG A 1 387 ? -7.260  -35.511 -19.836 1.00 102.11 ? 387 ARG A NE  1 
ATOM   2934 C CZ  . ARG A 1 387 ? -6.253  -36.350 -19.729 1.00 129.70 ? 387 ARG A CZ  1 
ATOM   2935 N NH1 . ARG A 1 387 ? -6.132  -37.074 -18.627 1.00 161.11 ? 387 ARG A NH1 1 
ATOM   2936 N NH2 . ARG A 1 387 ? -5.387  -36.457 -20.724 1.00 138.34 ? 387 ARG A NH2 1 
ATOM   2937 N N   . LEU A 1 388 ? -13.962 -33.590 -18.852 1.00 107.38 ? 388 LEU A N   1 
ATOM   2938 C CA  . LEU A 1 388 ? -15.055 -33.348 -17.914 1.00 112.97 ? 388 LEU A CA  1 
ATOM   2939 C C   . LEU A 1 388 ? -15.609 -34.667 -17.390 1.00 109.38 ? 388 LEU A C   1 
ATOM   2940 O O   . LEU A 1 388 ? -15.946 -35.559 -18.172 1.00 103.33 ? 388 LEU A O   1 
ATOM   2941 C CB  . LEU A 1 388 ? -16.213 -32.469 -18.394 1.00 100.42 ? 388 LEU A CB  1 
ATOM   2942 C CG  . LEU A 1 388 ? -16.554 -32.562 -19.885 1.00 107.50 ? 388 LEU A CG  1 
ATOM   2943 C CD1 . LEU A 1 388 ? -18.073 -32.523 -20.084 1.00 93.98  ? 388 LEU A CD1 1 
ATOM   2944 C CD2 . LEU A 1 388 ? -15.832 -31.437 -20.665 1.00 102.41 ? 388 LEU A CD2 1 
ATOM   2945 N N   . LEU A 1 389 ? -15.705 -34.755 -16.066 1.00 121.25 ? 389 LEU A N   1 
ATOM   2946 C CA  . LEU A 1 389 ? -16.268 -35.911 -15.376 1.00 124.01 ? 389 LEU A CA  1 
ATOM   2947 C C   . LEU A 1 389 ? -17.339 -35.465 -14.383 1.00 140.51 ? 389 LEU A C   1 
ATOM   2948 O O   . LEU A 1 389 ? -17.072 -34.621 -13.537 1.00 140.25 ? 389 LEU A O   1 
ATOM   2949 C CB  . LEU A 1 389 ? -15.096 -36.630 -14.710 1.00 129.35 ? 389 LEU A CB  1 
ATOM   2950 C CG  . LEU A 1 389 ? -15.443 -37.738 -13.714 1.00 127.77 ? 389 LEU A CG  1 
ATOM   2951 C CD1 . LEU A 1 389 ? -14.500 -38.892 -13.942 1.00 125.96 ? 389 LEU A CD1 1 
ATOM   2952 C CD2 . LEU A 1 389 ? -15.323 -37.265 -12.277 1.00 140.30 ? 389 LEU A CD2 1 
ATOM   2953 N N   . GLU A 1 390 ? -18.565 -35.978 -14.578 1.00 166.57 ? 390 GLU A N   1 
ATOM   2954 C CA  . GLU A 1 390 ? -19.710 -35.632 -13.767 1.00 175.14 ? 390 GLU A CA  1 
ATOM   2955 C C   . GLU A 1 390 ? -20.504 -36.915 -13.751 1.00 147.19 ? 390 GLU A C   1 
ATOM   2956 O O   . GLU A 1 390 ? -21.264 -37.112 -14.686 1.00 122.35 ? 390 GLU A O   1 
ATOM   2957 C CB  . GLU A 1 390 ? -20.568 -34.538 -14.405 1.00 196.87 ? 390 GLU A CB  1 
ATOM   2958 C CG  . GLU A 1 390 ? -20.085 -33.116 -14.126 1.00 255.30 ? 390 GLU A CG  1 
ATOM   2959 C CD  . GLU A 1 390 ? -20.515 -32.507 -12.804 1.00 275.41 ? 390 GLU A CD  1 
ATOM   2960 O OE1 . GLU A 1 390 ? -21.739 -32.405 -12.602 1.00 251.90 ? 390 GLU A OE1 1 
ATOM   2961 O OE2 . GLU A 1 390 ? -19.649 -32.113 -11.993 1.00 309.70 ? 390 GLU A OE2 1 
ATOM   2962 N N   . PRO A 1 391 ? -20.203 -37.861 -12.823 1.00 142.18 ? 391 PRO A N   1 
ATOM   2963 C CA  . PRO A 1 391 ? -20.949 -39.116 -12.720 1.00 135.47 ? 391 PRO A CA  1 
ATOM   2964 C C   . PRO A 1 391 ? -22.437 -38.792 -12.800 1.00 155.31 ? 391 PRO A C   1 
ATOM   2965 O O   . PRO A 1 391 ? -23.188 -39.384 -13.576 1.00 156.79 ? 391 PRO A O   1 
ATOM   2966 C CB  . PRO A 1 391 ? -20.553 -39.648 -11.325 1.00 129.28 ? 391 PRO A CB  1 
ATOM   2967 C CG  . PRO A 1 391 ? -19.175 -39.073 -11.074 1.00 155.45 ? 391 PRO A CG  1 
ATOM   2968 C CD  . PRO A 1 391 ? -19.106 -37.760 -11.839 1.00 150.36 ? 391 PRO A CD  1 
ATOM   2969 N N   . GLU A 1 392 ? -22.808 -37.780 -12.009 1.00 164.38 ? 392 GLU A N   1 
ATOM   2970 C CA  . GLU A 1 392 ? -24.155 -37.348 -11.702 1.00 171.71 ? 392 GLU A CA  1 
ATOM   2971 C C   . GLU A 1 392 ? -24.957 -37.200 -12.998 1.00 159.90 ? 392 GLU A C   1 
ATOM   2972 O O   . GLU A 1 392 ? -26.032 -37.779 -13.153 1.00 148.26 ? 392 GLU A O   1 
ATOM   2973 C CB  . GLU A 1 392 ? -24.065 -35.976 -11.022 1.00 188.67 ? 392 GLU A CB  1 
ATOM   2974 C CG  . GLU A 1 392 ? -22.748 -35.639 -10.315 1.00 182.60 ? 392 GLU A CG  1 
ATOM   2975 C CD  . GLU A 1 392 ? -22.543 -36.163 -8.909  1.00 203.42 ? 392 GLU A CD  1 
ATOM   2976 O OE1 . GLU A 1 392 ? -23.442 -35.926 -8.079  1.00 248.11 ? 392 GLU A OE1 1 
ATOM   2977 O OE2 . GLU A 1 392 ? -21.489 -36.767 -8.623  1.00 196.48 ? 392 GLU A OE2 1 
ATOM   2978 N N   . THR A 1 393 ? -24.413 -36.408 -13.929 1.00 170.71 ? 393 THR A N   1 
ATOM   2979 C CA  . THR A 1 393 ? -25.174 -35.918 -15.066 1.00 167.59 ? 393 THR A CA  1 
ATOM   2980 C C   . THR A 1 393 ? -24.783 -36.688 -16.319 1.00 152.57 ? 393 THR A C   1 
ATOM   2981 O O   . THR A 1 393 ? -25.599 -36.933 -17.199 1.00 147.51 ? 393 THR A O   1 
ATOM   2982 C CB  . THR A 1 393 ? -24.935 -34.420 -15.257 1.00 165.70 ? 393 THR A CB  1 
ATOM   2983 O OG1 . THR A 1 393 ? -23.578 -34.260 -15.652 1.00 164.52 ? 393 THR A OG1 1 
ATOM   2984 C CG2 . THR A 1 393 ? -25.154 -33.610 -13.996 1.00 169.56 ? 393 THR A CG2 1 
ATOM   2985 N N   . LEU A 1 394 ? -23.501 -37.019 -16.429 1.00 140.26 ? 394 LEU A N   1 
ATOM   2986 C CA  . LEU A 1 394 ? -23.056 -37.598 -17.676 1.00 133.90 ? 394 LEU A CA  1 
ATOM   2987 C C   . LEU A 1 394 ? -23.389 -39.084 -17.673 1.00 145.25 ? 394 LEU A C   1 
ATOM   2988 O O   . LEU A 1 394 ? -23.567 -39.661 -18.747 1.00 161.73 ? 394 LEU A O   1 
ATOM   2989 C CB  . LEU A 1 394 ? -21.571 -37.301 -17.855 1.00 130.07 ? 394 LEU A CB  1 
ATOM   2990 C CG  . LEU A 1 394 ? -21.245 -35.851 -18.224 1.00 133.01 ? 394 LEU A CG  1 
ATOM   2991 C CD1 . LEU A 1 394 ? -19.713 -35.694 -18.295 1.00 161.74 ? 394 LEU A CD1 1 
ATOM   2992 C CD2 . LEU A 1 394 ? -21.993 -35.444 -19.523 1.00 117.89 ? 394 LEU A CD2 1 
ATOM   2993 N N   . GLY A 1 395 ? -23.523 -39.662 -16.467 1.00 143.27 ? 395 GLY A N   1 
ATOM   2994 C CA  . GLY A 1 395 ? -23.718 -41.097 -16.292 1.00 153.82 ? 395 GLY A CA  1 
ATOM   2995 C C   . GLY A 1 395 ? -25.086 -41.551 -16.792 1.00 151.10 ? 395 GLY A C   1 
ATOM   2996 O O   . GLY A 1 395 ? -25.406 -42.746 -16.762 1.00 142.24 ? 395 GLY A O   1 
ATOM   2997 N N   . LYS A 1 396 ? -25.855 -40.556 -17.252 1.00 151.86 ? 396 LYS A N   1 
ATOM   2998 C CA  . LYS A 1 396 ? -27.196 -40.726 -17.779 1.00 150.46 ? 396 LYS A CA  1 
ATOM   2999 C C   . LYS A 1 396 ? -27.108 -40.967 -19.284 1.00 138.49 ? 396 LYS A C   1 
ATOM   3000 O O   . LYS A 1 396 ? -27.980 -41.613 -19.855 1.00 175.30 ? 396 LYS A O   1 
ATOM   3001 C CB  . LYS A 1 396 ? -28.002 -39.456 -17.463 1.00 168.26 ? 396 LYS A CB  1 
ATOM   3002 C CG  . LYS A 1 396 ? -28.755 -39.338 -16.126 1.00 173.44 ? 396 LYS A CG  1 
ATOM   3003 C CD  . LYS A 1 396 ? -28.800 -37.970 -15.430 1.00 189.38 ? 396 LYS A CD  1 
ATOM   3004 C CE  . LYS A 1 396 ? -29.254 -36.688 -16.119 1.00 181.52 ? 396 LYS A CE  1 
ATOM   3005 N NZ  . LYS A 1 396 ? -30.694 -36.489 -16.286 1.00 205.27 ? 396 LYS A NZ  1 
ATOM   3006 N N   . LEU A 1 397 ? -26.049 -40.460 -19.921 1.00 113.09 ? 397 LEU A N   1 
ATOM   3007 C CA  . LEU A 1 397 ? -25.940 -40.492 -21.370 1.00 119.37 ? 397 LEU A CA  1 
ATOM   3008 C C   . LEU A 1 397 ? -25.327 -41.801 -21.870 1.00 130.67 ? 397 LEU A C   1 
ATOM   3009 O O   . LEU A 1 397 ? -24.678 -42.529 -21.109 1.00 156.43 ? 397 LEU A O   1 
ATOM   3010 C CB  . LEU A 1 397 ? -25.032 -39.323 -21.720 1.00 117.86 ? 397 LEU A CB  1 
ATOM   3011 C CG  . LEU A 1 397 ? -25.678 -37.945 -21.659 1.00 116.05 ? 397 LEU A CG  1 
ATOM   3012 C CD1 . LEU A 1 397 ? -24.599 -36.900 -21.309 1.00 131.73 ? 397 LEU A CD1 1 
ATOM   3013 C CD2 . LEU A 1 397 ? -26.314 -37.722 -23.024 1.00 93.78  ? 397 LEU A CD2 1 
ATOM   3014 N N   . ASN A 1 398 ? -25.518 -42.057 -23.174 1.00 120.33 ? 398 ASN A N   1 
ATOM   3015 C CA  . ASN A 1 398 ? -24.701 -42.995 -23.926 1.00 121.88 ? 398 ASN A CA  1 
ATOM   3016 C C   . ASN A 1 398 ? -24.120 -42.262 -25.139 1.00 120.69 ? 398 ASN A C   1 
ATOM   3017 O O   . ASN A 1 398 ? -24.593 -41.174 -25.439 1.00 113.16 ? 398 ASN A O   1 
ATOM   3018 C CB  . ASN A 1 398 ? -25.519 -44.219 -24.298 1.00 128.19 ? 398 ASN A CB  1 
ATOM   3019 C CG  . ASN A 1 398 ? -26.317 -43.954 -25.549 1.00 155.84 ? 398 ASN A CG  1 
ATOM   3020 O OD1 . ASN A 1 398 ? -26.331 -42.819 -26.042 1.00 137.95 ? 398 ASN A OD1 1 
ATOM   3021 N ND2 . ASN A 1 398 ? -26.984 -44.976 -26.069 1.00 199.08 ? 398 ASN A ND2 1 
ATOM   3022 N N   . PRO A 1 399 ? -23.104 -42.807 -25.870 1.00 135.90 ? 399 PRO A N   1 
ATOM   3023 C CA  . PRO A 1 399 ? -22.378 -42.053 -26.901 1.00 138.39 ? 399 PRO A CA  1 
ATOM   3024 C C   . PRO A 1 399 ? -23.380 -41.399 -27.851 1.00 133.19 ? 399 PRO A C   1 
ATOM   3025 O O   . PRO A 1 399 ? -23.273 -40.210 -28.198 1.00 157.35 ? 399 PRO A O   1 
ATOM   3026 C CB  . PRO A 1 399 ? -21.587 -43.140 -27.641 1.00 119.71 ? 399 PRO A CB  1 
ATOM   3027 C CG  . PRO A 1 399 ? -21.305 -44.140 -26.557 1.00 134.64 ? 399 PRO A CG  1 
ATOM   3028 C CD  . PRO A 1 399 ? -22.541 -44.156 -25.679 1.00 141.98 ? 399 PRO A CD  1 
ATOM   3029 N N   . ARG A 1 400 ? -24.272 -42.278 -28.330 1.00 115.04 ? 400 ARG A N   1 
ATOM   3030 C CA  . ARG A 1 400 ? -25.206 -41.948 -29.392 1.00 129.91 ? 400 ARG A CA  1 
ATOM   3031 C C   . ARG A 1 400 ? -26.065 -40.753 -28.992 1.00 141.18 ? 400 ARG A C   1 
ATOM   3032 O O   . ARG A 1 400 ? -26.248 -39.804 -29.775 1.00 140.46 ? 400 ARG A O   1 
ATOM   3033 C CB  . ARG A 1 400 ? -26.193 -43.103 -29.600 1.00 135.01 ? 400 ARG A CB  1 
ATOM   3034 C CG  . ARG A 1 400 ? -27.326 -42.750 -30.552 1.00 158.03 ? 400 ARG A CG  1 
ATOM   3035 C CD  . ARG A 1 400 ? -28.706 -43.278 -30.127 1.00 177.24 ? 400 ARG A CD  1 
ATOM   3036 N NE  . ARG A 1 400 ? -29.006 -44.685 -30.415 1.00 157.21 ? 400 ARG A NE  1 
ATOM   3037 C CZ  . ARG A 1 400 ? -28.964 -45.191 -31.637 1.00 156.36 ? 400 ARG A CZ  1 
ATOM   3038 N NH1 . ARG A 1 400 ? -28.562 -44.453 -32.658 1.00 158.34 ? 400 ARG A NH1 1 
ATOM   3039 N NH2 . ARG A 1 400 ? -29.317 -46.446 -31.836 1.00 148.93 ? 400 ARG A NH2 1 
ATOM   3040 N N   . THR A 1 401 ? -26.579 -40.843 -27.757 1.00 147.39 ? 401 THR A N   1 
ATOM   3041 C CA  . THR A 1 401 ? -27.447 -39.828 -27.170 1.00 145.87 ? 401 THR A CA  1 
ATOM   3042 C C   . THR A 1 401 ? -26.746 -38.464 -27.191 1.00 132.68 ? 401 THR A C   1 
ATOM   3043 O O   . THR A 1 401 ? -27.311 -37.438 -27.609 1.00 126.02 ? 401 THR A O   1 
ATOM   3044 C CB  . THR A 1 401 ? -27.695 -40.231 -25.711 1.00 155.00 ? 401 THR A CB  1 
ATOM   3045 O OG1 . THR A 1 401 ? -28.511 -41.393 -25.725 1.00 159.07 ? 401 THR A OG1 1 
ATOM   3046 C CG2 . THR A 1 401 ? -28.417 -39.188 -24.874 1.00 163.17 ? 401 THR A CG2 1 
ATOM   3047 N N   . ALA A 1 402 ? -25.498 -38.509 -26.709 1.00 123.20 ? 402 ALA A N   1 
ATOM   3048 C CA  . ALA A 1 402 ? -24.675 -37.313 -26.582 1.00 111.21 ? 402 ALA A CA  1 
ATOM   3049 C C   . ALA A 1 402 ? -24.482 -36.672 -27.959 1.00 107.76 ? 402 ALA A C   1 
ATOM   3050 O O   . ALA A 1 402 ? -24.627 -35.436 -28.113 1.00 110.86 ? 402 ALA A O   1 
ATOM   3051 C CB  . ALA A 1 402 ? -23.381 -37.600 -25.853 1.00 115.38 ? 402 ALA A CB  1 
ATOM   3052 N N   . VAL A 1 403 ? -24.177 -37.544 -28.938 1.00 112.06 ? 403 VAL A N   1 
ATOM   3053 C CA  . VAL A 1 403 ? -23.904 -37.085 -30.295 1.00 113.78 ? 403 VAL A CA  1 
ATOM   3054 C C   . VAL A 1 403 ? -25.162 -36.405 -30.850 1.00 122.56 ? 403 VAL A C   1 
ATOM   3055 O O   . VAL A 1 403 ? -25.055 -35.332 -31.472 1.00 124.81 ? 403 VAL A O   1 
ATOM   3056 C CB  . VAL A 1 403 ? -23.220 -37.970 -31.359 1.00 119.56 ? 403 VAL A CB  1 
ATOM   3057 C CG1 . VAL A 1 403 ? -22.650 -37.158 -32.520 1.00 98.53  ? 403 VAL A CG1 1 
ATOM   3058 C CG2 . VAL A 1 403 ? -22.137 -38.867 -30.775 1.00 127.48 ? 403 VAL A CG2 1 
ATOM   3059 N N   . GLU A 1 404 ? -26.324 -37.021 -30.604 1.00 135.69 ? 404 GLU A N   1 
ATOM   3060 C CA  . GLU A 1 404 ? -27.542 -36.437 -31.159 1.00 150.03 ? 404 GLU A CA  1 
ATOM   3061 C C   . GLU A 1 404 ? -27.838 -35.101 -30.497 1.00 150.70 ? 404 GLU A C   1 
ATOM   3062 O O   . GLU A 1 404 ? -28.082 -34.072 -31.156 1.00 134.19 ? 404 GLU A O   1 
ATOM   3063 C CB  . GLU A 1 404 ? -28.745 -37.353 -31.290 1.00 187.72 ? 404 GLU A CB  1 
ATOM   3064 C CG  . GLU A 1 404 ? -28.414 -38.679 -31.967 1.00 236.11 ? 404 GLU A CG  1 
ATOM   3065 C CD  . GLU A 1 404 ? -29.531 -39.710 -31.845 1.00 292.72 ? 404 GLU A CD  1 
ATOM   3066 O OE1 . GLU A 1 404 ? -29.960 -40.269 -32.879 1.00 311.10 ? 404 GLU A OE1 1 
ATOM   3067 O OE2 . GLU A 1 404 ? -30.009 -39.924 -30.713 1.00 324.26 ? 404 GLU A OE2 1 
ATOM   3068 N N   . ARG A 1 405 ? -27.585 -35.015 -29.188 1.00 152.99 ? 405 ARG A N   1 
ATOM   3069 C CA  . ARG A 1 405 ? -27.768 -33.758 -28.454 1.00 132.35 ? 405 ARG A CA  1 
ATOM   3070 C C   . ARG A 1 405 ? -26.918 -32.660 -29.098 1.00 123.67 ? 405 ARG A C   1 
ATOM   3071 O O   . ARG A 1 405 ? -27.395 -31.541 -29.330 1.00 122.00 ? 405 ARG A O   1 
ATOM   3072 C CB  . ARG A 1 405 ? -27.268 -33.823 -27.010 1.00 135.64 ? 405 ARG A CB  1 
ATOM   3073 C CG  . ARG A 1 405 ? -28.217 -34.528 -26.055 1.00 132.44 ? 405 ARG A CG  1 
ATOM   3074 C CD  . ARG A 1 405 ? -28.738 -33.515 -25.092 1.00 133.32 ? 405 ARG A CD  1 
ATOM   3075 N NE  . ARG A 1 405 ? -29.367 -34.299 -24.023 1.00 145.52 ? 405 ARG A NE  1 
ATOM   3076 C CZ  . ARG A 1 405 ? -28.849 -34.404 -22.807 1.00 147.90 ? 405 ARG A CZ  1 
ATOM   3077 N NH1 . ARG A 1 405 ? -27.681 -33.834 -22.535 1.00 130.89 ? 405 ARG A NH1 1 
ATOM   3078 N NH2 . ARG A 1 405 ? -29.505 -35.107 -21.899 1.00 157.62 ? 405 ARG A NH2 1 
ATOM   3079 N N   . LEU A 1 406 ? -25.663 -33.026 -29.379 1.00 139.13 ? 406 LEU A N   1 
ATOM   3080 C CA  . LEU A 1 406 ? -24.738 -32.074 -29.971 1.00 127.85 ? 406 LEU A CA  1 
ATOM   3081 C C   . LEU A 1 406 ? -25.231 -31.625 -31.347 1.00 126.76 ? 406 LEU A C   1 
ATOM   3082 O O   . LEU A 1 406 ? -25.155 -30.434 -31.642 1.00 128.18 ? 406 LEU A O   1 
ATOM   3083 C CB  . LEU A 1 406 ? -23.233 -32.244 -29.751 1.00 124.33 ? 406 LEU A CB  1 
ATOM   3084 C CG  . LEU A 1 406 ? -22.824 -32.277 -28.270 1.00 118.35 ? 406 LEU A CG  1 
ATOM   3085 C CD1 . LEU A 1 406 ? -21.323 -32.322 -28.080 1.00 122.10 ? 406 LEU A CD1 1 
ATOM   3086 C CD2 . LEU A 1 406 ? -23.378 -31.113 -27.506 1.00 119.80 ? 406 LEU A CD2 1 
ATOM   3087 N N   . ARG A 1 407 ? -25.780 -32.580 -32.118 1.00 124.36 ? 407 ARG A N   1 
ATOM   3088 C CA  . ARG A 1 407 ? -26.249 -32.293 -33.455 1.00 122.89 ? 407 ARG A CA  1 
ATOM   3089 C C   . ARG A 1 407 ? -27.429 -31.324 -33.371 1.00 136.05 ? 407 ARG A C   1 
ATOM   3090 O O   . ARG A 1 407 ? -27.612 -30.513 -34.283 1.00 142.51 ? 407 ARG A O   1 
ATOM   3091 C CB  . ARG A 1 407 ? -26.551 -33.581 -34.235 1.00 111.32 ? 407 ARG A CB  1 
ATOM   3092 C CG  . ARG A 1 407 ? -26.522 -33.321 -35.734 1.00 117.51 ? 407 ARG A CG  1 
ATOM   3093 C CD  . ARG A 1 407 ? -26.641 -34.527 -36.644 1.00 125.72 ? 407 ARG A CD  1 
ATOM   3094 N NE  . ARG A 1 407 ? -25.569 -35.421 -36.215 1.00 140.59 ? 407 ARG A NE  1 
ATOM   3095 C CZ  . ARG A 1 407 ? -25.699 -36.665 -35.798 1.00 147.55 ? 407 ARG A CZ  1 
ATOM   3096 N NH1 . ARG A 1 407 ? -26.619 -37.490 -36.270 1.00 159.74 ? 407 ARG A NH1 1 
ATOM   3097 N NH2 . ARG A 1 407 ? -24.818 -37.068 -34.929 1.00 128.25 ? 407 ARG A NH2 1 
ATOM   3098 N N   . ALA A 1 408 ? -28.296 -31.533 -32.370 1.00 137.00 ? 408 ALA A N   1 
ATOM   3099 C CA  . ALA A 1 408 ? -29.593 -30.882 -32.322 1.00 146.84 ? 408 ALA A CA  1 
ATOM   3100 C C   . ALA A 1 408 ? -29.410 -29.380 -32.180 1.00 158.80 ? 408 ALA A C   1 
ATOM   3101 O O   . ALA A 1 408 ? -30.042 -28.591 -32.896 1.00 177.09 ? 408 ALA A O   1 
ATOM   3102 C CB  . ALA A 1 408 ? -30.395 -31.437 -31.172 1.00 152.00 ? 408 ALA A CB  1 
ATOM   3103 N N   . GLU A 1 409 ? -28.661 -28.999 -31.140 1.00 177.76 ? 409 GLU A N   1 
ATOM   3104 C CA  . GLU A 1 409 ? -28.498 -27.611 -30.748 1.00 181.28 ? 409 GLU A CA  1 
ATOM   3105 C C   . GLU A 1 409 ? -27.360 -26.985 -31.556 1.00 176.99 ? 409 GLU A C   1 
ATOM   3106 O O   . GLU A 1 409 ? -26.771 -25.986 -31.148 1.00 180.83 ? 409 GLU A O   1 
ATOM   3107 C CB  . GLU A 1 409 ? -28.364 -27.562 -29.225 1.00 183.51 ? 409 GLU A CB  1 
ATOM   3108 C CG  . GLU A 1 409 ? -29.414 -28.400 -28.497 1.00 203.82 ? 409 GLU A CG  1 
ATOM   3109 C CD  . GLU A 1 409 ? -30.885 -28.020 -28.628 1.00 257.71 ? 409 GLU A CD  1 
ATOM   3110 O OE1 . GLU A 1 409 ? -31.238 -26.880 -29.018 1.00 282.34 ? 409 GLU A OE1 1 
ATOM   3111 O OE2 . GLU A 1 409 ? -31.705 -28.911 -28.326 1.00 270.98 ? 409 GLU A OE2 1 
ATOM   3112 N N   . GLY A 1 410 ? -27.097 -27.583 -32.725 1.00 170.85 ? 410 GLY A N   1 
ATOM   3113 C CA  . GLY A 1 410 ? -26.112 -27.147 -33.695 1.00 162.98 ? 410 GLY A CA  1 
ATOM   3114 C C   . GLY A 1 410 ? -24.753 -26.936 -33.046 1.00 152.79 ? 410 GLY A C   1 
ATOM   3115 O O   . GLY A 1 410 ? -24.054 -25.999 -33.413 1.00 143.49 ? 410 GLY A O   1 
ATOM   3116 N N   . LEU A 1 411 ? -24.408 -27.813 -32.092 1.00 159.72 ? 411 LEU A N   1 
ATOM   3117 C CA  . LEU A 1 411 ? -23.172 -27.718 -31.329 1.00 174.03 ? 411 LEU A CA  1 
ATOM   3118 C C   . LEU A 1 411 ? -22.064 -28.560 -31.971 1.00 177.24 ? 411 LEU A C   1 
ATOM   3119 O O   . LEU A 1 411 ? -20.871 -28.226 -31.879 1.00 167.50 ? 411 LEU A O   1 
ATOM   3120 C CB  . LEU A 1 411 ? -23.428 -28.085 -29.866 1.00 158.48 ? 411 LEU A CB  1 
ATOM   3121 C CG  . LEU A 1 411 ? -23.860 -26.932 -28.954 1.00 141.40 ? 411 LEU A CG  1 
ATOM   3122 C CD1 . LEU A 1 411 ? -24.120 -27.378 -27.532 1.00 122.19 ? 411 LEU A CD1 1 
ATOM   3123 C CD2 . LEU A 1 411 ? -22.765 -25.872 -28.957 1.00 150.43 ? 411 LEU A CD2 1 
ATOM   3124 N N   . LEU A 1 412 ? -22.478 -29.632 -32.652 1.00 166.51 ? 412 LEU A N   1 
ATOM   3125 C CA  . LEU A 1 412 ? -21.527 -30.526 -33.285 1.00 166.97 ? 412 LEU A CA  1 
ATOM   3126 C C   . LEU A 1 412 ? -20.755 -29.781 -34.374 1.00 148.43 ? 412 LEU A C   1 
ATOM   3127 O O   . LEU A 1 412 ? -21.302 -28.922 -35.055 1.00 135.13 ? 412 LEU A O   1 
ATOM   3128 C CB  . LEU A 1 412 ? -22.315 -31.720 -33.818 1.00 158.31 ? 412 LEU A CB  1 
ATOM   3129 C CG  . LEU A 1 412 ? -21.603 -33.070 -33.708 1.00 138.03 ? 412 LEU A CG  1 
ATOM   3130 C CD1 . LEU A 1 412 ? -22.595 -34.182 -34.004 1.00 167.16 ? 412 LEU A CD1 1 
ATOM   3131 C CD2 . LEU A 1 412 ? -20.362 -33.178 -34.595 1.00 132.80 ? 412 LEU A CD2 1 
ATOM   3132 N N   . TYR A 1 413 ? -19.475 -30.130 -34.536 1.00 137.45 ? 413 TYR A N   1 
ATOM   3133 C CA  . TYR A 1 413 ? -18.631 -29.502 -35.529 1.00 130.32 ? 413 TYR A CA  1 
ATOM   3134 C C   . TYR A 1 413 ? -19.185 -29.832 -36.909 1.00 133.91 ? 413 TYR A C   1 
ATOM   3135 O O   . TYR A 1 413 ? -19.457 -30.997 -37.217 1.00 124.75 ? 413 TYR A O   1 
ATOM   3136 C CB  . TYR A 1 413 ? -17.190 -29.997 -35.380 1.00 136.85 ? 413 TYR A CB  1 
ATOM   3137 C CG  . TYR A 1 413 ? -16.277 -29.506 -36.494 1.00 157.56 ? 413 TYR A CG  1 
ATOM   3138 C CD1 . TYR A 1 413 ? -16.195 -30.197 -37.699 1.00 176.98 ? 413 TYR A CD1 1 
ATOM   3139 C CD2 . TYR A 1 413 ? -15.502 -28.362 -36.352 1.00 157.44 ? 413 TYR A CD2 1 
ATOM   3140 C CE1 . TYR A 1 413 ? -15.381 -29.767 -38.737 1.00 170.96 ? 413 TYR A CE1 1 
ATOM   3141 C CE2 . TYR A 1 413 ? -14.683 -27.916 -37.383 1.00 163.30 ? 413 TYR A CE2 1 
ATOM   3142 C CZ  . TYR A 1 413 ? -14.625 -28.616 -38.580 1.00 156.38 ? 413 TYR A CZ  1 
ATOM   3143 O OH  . TYR A 1 413 ? -13.822 -28.212 -39.613 1.00 140.07 ? 413 TYR A OH  1 
ATOM   3144 N N   . ARG A 1 414 ? -19.338 -28.787 -37.730 1.00 138.46 ? 414 ARG A N   1 
ATOM   3145 C CA  . ARG A 1 414 ? -19.693 -28.971 -39.126 1.00 159.15 ? 414 ARG A CA  1 
ATOM   3146 C C   . ARG A 1 414 ? -18.532 -28.498 -40.000 1.00 153.59 ? 414 ARG A C   1 
ATOM   3147 O O   . ARG A 1 414 ? -17.854 -27.536 -39.654 1.00 145.71 ? 414 ARG A O   1 
ATOM   3148 C CB  . ARG A 1 414 ? -21.028 -28.288 -39.437 1.00 169.48 ? 414 ARG A CB  1 
ATOM   3149 C CG  . ARG A 1 414 ? -22.247 -28.891 -38.746 1.00 195.78 ? 414 ARG A CG  1 
ATOM   3150 C CD  . ARG A 1 414 ? -23.473 -28.041 -39.024 1.00 206.23 ? 414 ARG A CD  1 
ATOM   3151 N NE  . ARG A 1 414 ? -23.201 -26.656 -38.614 1.00 243.09 ? 414 ARG A NE  1 
ATOM   3152 C CZ  . ARG A 1 414 ? -23.246 -26.169 -37.374 1.00 253.38 ? 414 ARG A CZ  1 
ATOM   3153 N NH1 . ARG A 1 414 ? -23.677 -26.922 -36.374 1.00 241.01 ? 414 ARG A NH1 1 
ATOM   3154 N NH2 . ARG A 1 414 ? -22.853 -24.927 -37.150 1.00 262.89 ? 414 ARG A NH2 1 
ATOM   3155 N N   . HIS A 1 415 ? -18.319 -29.193 -41.126 1.00 158.84 ? 415 HIS A N   1 
ATOM   3156 C CA  . HIS A 1 415 ? -17.152 -28.982 -41.967 1.00 162.58 ? 415 HIS A CA  1 
ATOM   3157 C C   . HIS A 1 415 ? -17.372 -27.792 -42.895 1.00 165.05 ? 415 HIS A C   1 
ATOM   3158 O O   . HIS A 1 415 ? -16.417 -27.225 -43.411 1.00 177.13 ? 415 HIS A O   1 
ATOM   3159 C CB  . HIS A 1 415 ? -16.817 -30.261 -42.747 1.00 191.08 ? 415 HIS A CB  1 
ATOM   3160 C CG  . HIS A 1 415 ? -16.372 -31.420 -41.901 1.00 211.77 ? 415 HIS A CG  1 
ATOM   3161 N ND1 . HIS A 1 415 ? -15.052 -31.641 -41.554 1.00 221.81 ? 415 HIS A ND1 1 
ATOM   3162 C CD2 . HIS A 1 415 ? -17.068 -32.422 -41.342 1.00 188.15 ? 415 HIS A CD2 1 
ATOM   3163 C CE1 . HIS A 1 415 ? -14.965 -32.727 -40.800 1.00 182.55 ? 415 HIS A CE1 1 
ATOM   3164 N NE2 . HIS A 1 415 ? -16.179 -33.228 -40.668 1.00 166.86 ? 415 HIS A NE2 1 
ATOM   3165 N N   . ASP A 1 416 ? -18.642 -27.438 -43.103 1.00 172.09 ? 416 ASP A N   1 
ATOM   3166 C CA  . ASP A 1 416 ? -19.051 -26.367 -43.998 1.00 197.79 ? 416 ASP A CA  1 
ATOM   3167 C C   . ASP A 1 416 ? -18.799 -25.001 -43.357 1.00 200.64 ? 416 ASP A C   1 
ATOM   3168 O O   . ASP A 1 416 ? -18.437 -24.050 -44.054 1.00 205.04 ? 416 ASP A O   1 
ATOM   3169 C CB  . ASP A 1 416 ? -20.489 -26.570 -44.451 1.00 208.32 ? 416 ASP A CB  1 
ATOM   3170 C CG  . ASP A 1 416 ? -21.476 -26.953 -43.354 1.00 204.71 ? 416 ASP A CG  1 
ATOM   3171 O OD1 . ASP A 1 416 ? -21.091 -26.898 -42.175 1.00 181.26 ? 416 ASP A OD1 1 
ATOM   3172 O OD2 . ASP A 1 416 ? -22.620 -27.327 -43.691 1.00 209.55 ? 416 ASP A OD2 1 
ATOM   3173 N N   . THR A 1 417 ? -19.005 -24.922 -42.034 1.00 184.57 ? 417 THR A N   1 
ATOM   3174 C CA  . THR A 1 417 ? -18.820 -23.701 -41.261 1.00 160.48 ? 417 THR A CA  1 
ATOM   3175 C C   . THR A 1 417 ? -17.376 -23.625 -40.783 1.00 146.37 ? 417 THR A C   1 
ATOM   3176 O O   . THR A 1 417 ? -16.767 -22.568 -40.828 1.00 154.21 ? 417 THR A O   1 
ATOM   3177 C CB  . THR A 1 417 ? -19.807 -23.614 -40.093 1.00 170.30 ? 417 THR A CB  1 
ATOM   3178 O OG1 . THR A 1 417 ? -19.653 -24.785 -39.298 1.00 179.15 ? 417 THR A OG1 1 
ATOM   3179 C CG2 . THR A 1 417 ? -21.255 -23.549 -40.549 1.00 182.42 ? 417 THR A CG2 1 
ATOM   3180 N N   . GLY A 1 418 ? -16.841 -24.759 -40.326 1.00 162.86 ? 418 GLY A N   1 
ATOM   3181 C CA  . GLY A 1 418 ? -15.441 -24.871 -39.955 1.00 162.94 ? 418 GLY A CA  1 
ATOM   3182 C C   . GLY A 1 418 ? -15.233 -24.672 -38.458 1.00 160.28 ? 418 GLY A C   1 
ATOM   3183 O O   . GLY A 1 418 ? -14.120 -24.382 -38.027 1.00 151.83 ? 418 GLY A O   1 
ATOM   3184 N N   . GLU A 1 419 ? -16.310 -24.845 -37.680 1.00 160.78 ? 419 GLU A N   1 
ATOM   3185 C CA  . GLU A 1 419 ? -16.265 -24.629 -36.243 1.00 161.06 ? 419 GLU A CA  1 
ATOM   3186 C C   . GLU A 1 419 ? -17.342 -25.456 -35.547 1.00 155.97 ? 419 GLU A C   1 
ATOM   3187 O O   . GLU A 1 419 ? -18.467 -25.559 -36.032 1.00 159.30 ? 419 GLU A O   1 
ATOM   3188 C CB  . GLU A 1 419 ? -16.449 -23.142 -35.948 1.00 176.05 ? 419 GLU A CB  1 
ATOM   3189 C CG  . GLU A 1 419 ? -17.591 -22.512 -36.745 1.00 175.98 ? 419 GLU A CG  1 
ATOM   3190 C CD  . GLU A 1 419 ? -18.111 -21.308 -36.002 1.00 192.55 ? 419 GLU A CD  1 
ATOM   3191 O OE1 . GLU A 1 419 ? -17.309 -20.379 -35.720 1.00 189.91 ? 419 GLU A OE1 1 
ATOM   3192 O OE2 . GLU A 1 419 ? -19.322 -21.347 -35.691 1.00 212.37 ? 419 GLU A OE2 1 
ATOM   3193 N N   . GLY A 1 420 ? -16.967 -26.039 -34.405 1.00 158.74 ? 420 GLY A N   1 
ATOM   3194 C CA  . GLY A 1 420 ? -17.868 -26.755 -33.522 1.00 148.73 ? 420 GLY A CA  1 
ATOM   3195 C C   . GLY A 1 420 ? -17.124 -27.694 -32.567 1.00 144.44 ? 420 GLY A C   1 
ATOM   3196 O O   . GLY A 1 420 ? -15.918 -27.573 -32.281 1.00 129.70 ? 420 GLY A O   1 
ATOM   3197 N N   . VAL A 1 421 ? -17.875 -28.715 -32.115 1.00 131.01 ? 421 VAL A N   1 
ATOM   3198 C CA  . VAL A 1 421 ? -17.493 -29.555 -30.986 1.00 133.69 ? 421 VAL A CA  1 
ATOM   3199 C C   . VAL A 1 421 ? -17.488 -31.028 -31.414 1.00 142.13 ? 421 VAL A C   1 
ATOM   3200 O O   . VAL A 1 421 ? -18.411 -31.548 -32.028 1.00 180.10 ? 421 VAL A O   1 
ATOM   3201 C CB  . VAL A 1 421 ? -18.293 -29.364 -29.671 1.00 129.68 ? 421 VAL A CB  1 
ATOM   3202 C CG1 . VAL A 1 421 ? -17.691 -30.138 -28.494 1.00 116.78 ? 421 VAL A CG1 1 
ATOM   3203 C CG2 . VAL A 1 421 ? -18.481 -27.900 -29.282 1.00 136.30 ? 421 VAL A CG2 1 
ATOM   3204 N N   . ALA A 1 422 ? -16.381 -31.684 -31.064 1.00 137.96 ? 422 ALA A N   1 
ATOM   3205 C CA  . ALA A 1 422 ? -16.185 -33.111 -31.222 1.00 120.02 ? 422 ALA A CA  1 
ATOM   3206 C C   . ALA A 1 422 ? -15.743 -33.715 -29.885 1.00 117.32 ? 422 ALA A C   1 
ATOM   3207 O O   . ALA A 1 422 ? -14.853 -33.212 -29.165 1.00 110.65 ? 422 ALA A O   1 
ATOM   3208 C CB  . ALA A 1 422 ? -15.222 -33.382 -32.355 1.00 116.13 ? 422 ALA A CB  1 
ATOM   3209 N N   . LEU A 1 423 ? -16.375 -34.854 -29.587 1.00 109.25 ? 423 LEU A N   1 
ATOM   3210 C CA  . LEU A 1 423 ? -16.095 -35.634 -28.388 1.00 118.09 ? 423 LEU A CA  1 
ATOM   3211 C C   . LEU A 1 423 ? -15.071 -36.757 -28.610 1.00 113.22 ? 423 LEU A C   1 
ATOM   3212 O O   . LEU A 1 423 ? -14.829 -37.259 -29.710 1.00 115.61 ? 423 LEU A O   1 
ATOM   3213 C CB  . LEU A 1 423 ? -17.348 -36.162 -27.704 1.00 128.66 ? 423 LEU A CB  1 
ATOM   3214 C CG  . LEU A 1 423 ? -18.409 -35.133 -27.329 1.00 116.99 ? 423 LEU A CG  1 
ATOM   3215 C CD1 . LEU A 1 423 ? -19.012 -34.862 -28.684 1.00 117.90 ? 423 LEU A CD1 1 
ATOM   3216 C CD2 . LEU A 1 423 ? -19.438 -35.751 -26.379 1.00 103.87 ? 423 LEU A CD2 1 
ATOM   3217 N N   . HIS A 1 424 ? -14.455 -37.125 -27.489 1.00 103.82 ? 424 HIS A N   1 
ATOM   3218 C CA  . HIS A 1 424 ? -13.557 -38.263 -27.393 1.00 121.93 ? 424 HIS A CA  1 
ATOM   3219 C C   . HIS A 1 424 ? -13.958 -39.167 -26.230 1.00 134.34 ? 424 HIS A C   1 
ATOM   3220 O O   . HIS A 1 424 ? -14.454 -38.738 -25.167 1.00 132.39 ? 424 HIS A O   1 
ATOM   3221 C CB  . HIS A 1 424 ? -12.094 -37.820 -27.335 1.00 107.75 ? 424 HIS A CB  1 
ATOM   3222 C CG  . HIS A 1 424 ? -11.805 -36.676 -28.227 1.00 99.36  ? 424 HIS A CG  1 
ATOM   3223 N ND1 . HIS A 1 424 ? -11.062 -35.610 -27.772 1.00 105.20 ? 424 HIS A ND1 1 
ATOM   3224 C CD2 . HIS A 1 424 ? -12.181 -36.382 -29.483 1.00 98.05  ? 424 HIS A CD2 1 
ATOM   3225 C CE1 . HIS A 1 424 ? -10.977 -34.707 -28.744 1.00 117.98 ? 424 HIS A CE1 1 
ATOM   3226 N NE2 . HIS A 1 424 ? -11.657 -35.154 -29.791 1.00 113.89 ? 424 HIS A NE2 1 
ATOM   3227 N N   . VAL A 1 425 ? -13.610 -40.450 -26.402 1.00 139.61 ? 425 VAL A N   1 
ATOM   3228 C CA  . VAL A 1 425 ? -13.675 -41.418 -25.305 1.00 145.49 ? 425 VAL A CA  1 
ATOM   3229 C C   . VAL A 1 425 ? -15.146 -41.526 -24.906 1.00 144.48 ? 425 VAL A C   1 
ATOM   3230 O O   . VAL A 1 425 ? -15.502 -41.360 -23.739 1.00 139.17 ? 425 VAL A O   1 
ATOM   3231 C CB  . VAL A 1 425 ? -12.840 -40.946 -24.087 1.00 130.95 ? 425 VAL A CB  1 
ATOM   3232 C CG1 . VAL A 1 425 ? -12.677 -42.045 -23.034 1.00 147.97 ? 425 VAL A CG1 1 
ATOM   3233 C CG2 . VAL A 1 425 ? -11.488 -40.364 -24.482 1.00 115.14 ? 425 VAL A CG2 1 
ATOM   3234 N N   . LEU A 1 426 ? -15.998 -41.775 -25.897 1.00 132.69 ? 426 LEU A N   1 
ATOM   3235 C CA  . LEU A 1 426 ? -17.428 -41.672 -25.662 1.00 123.64 ? 426 LEU A CA  1 
ATOM   3236 C C   . LEU A 1 426 ? -17.902 -42.812 -24.769 1.00 120.59 ? 426 LEU A C   1 
ATOM   3237 O O   . LEU A 1 426 ? -18.924 -42.690 -24.091 1.00 124.97 ? 426 LEU A O   1 
ATOM   3238 C CB  . LEU A 1 426 ? -18.134 -41.623 -27.013 1.00 118.95 ? 426 LEU A CB  1 
ATOM   3239 C CG  . LEU A 1 426 ? -17.932 -40.321 -27.793 1.00 114.18 ? 426 LEU A CG  1 
ATOM   3240 C CD1 . LEU A 1 426 ? -18.045 -40.465 -29.296 1.00 104.42 ? 426 LEU A CD1 1 
ATOM   3241 C CD2 . LEU A 1 426 ? -19.056 -39.455 -27.289 1.00 145.06 ? 426 LEU A CD2 1 
ATOM   3242 N N   . GLY A 1 427 ? -17.123 -43.899 -24.758 1.00 117.13 ? 427 GLY A N   1 
ATOM   3243 C CA  . GLY A 1 427 ? -17.504 -45.118 -24.058 1.00 132.25 ? 427 GLY A CA  1 
ATOM   3244 C C   . GLY A 1 427 ? -17.564 -44.910 -22.545 1.00 130.38 ? 427 GLY A C   1 
ATOM   3245 O O   . GLY A 1 427 ? -18.263 -45.641 -21.835 1.00 115.99 ? 427 GLY A O   1 
ATOM   3246 N N   . ALA A 1 428 ? -16.834 -43.888 -22.079 1.00 116.10 ? 428 ALA A N   1 
ATOM   3247 C CA  . ALA A 1 428 ? -16.743 -43.612 -20.659 1.00 124.35 ? 428 ALA A CA  1 
ATOM   3248 C C   . ALA A 1 428 ? -18.017 -42.942 -20.179 1.00 131.00 ? 428 ALA A C   1 
ATOM   3249 O O   . ALA A 1 428 ? -18.302 -42.977 -18.986 1.00 125.13 ? 428 ALA A O   1 
ATOM   3250 C CB  . ALA A 1 428 ? -15.550 -42.744 -20.392 1.00 140.79 ? 428 ALA A CB  1 
ATOM   3251 N N   . LEU A 1 429 ? -18.773 -42.360 -21.120 1.00 135.79 ? 429 LEU A N   1 
ATOM   3252 C CA  . LEU A 1 429 ? -20.008 -41.647 -20.836 1.00 122.43 ? 429 LEU A CA  1 
ATOM   3253 C C   . LEU A 1 429 ? -20.914 -42.470 -19.930 1.00 135.86 ? 429 LEU A C   1 
ATOM   3254 O O   . LEU A 1 429 ? -21.148 -42.068 -18.787 1.00 143.24 ? 429 LEU A O   1 
ATOM   3255 C CB  . LEU A 1 429 ? -20.732 -41.246 -22.117 1.00 117.13 ? 429 LEU A CB  1 
ATOM   3256 C CG  . LEU A 1 429 ? -20.252 -39.930 -22.731 1.00 121.50 ? 429 LEU A CG  1 
ATOM   3257 C CD1 . LEU A 1 429 ? -21.082 -39.565 -23.948 1.00 125.41 ? 429 LEU A CD1 1 
ATOM   3258 C CD2 . LEU A 1 429 ? -20.325 -38.842 -21.683 1.00 120.63 ? 429 LEU A CD2 1 
ATOM   3259 N N   . ASN A 1 430 ? -21.374 -43.627 -20.432 1.00 132.82 ? 430 ASN A N   1 
ATOM   3260 C CA  . ASN A 1 430 ? -22.395 -44.391 -19.736 1.00 150.64 ? 430 ASN A CA  1 
ATOM   3261 C C   . ASN A 1 430 ? -21.856 -44.944 -18.418 1.00 154.31 ? 430 ASN A C   1 
ATOM   3262 O O   . ASN A 1 430 ? -22.598 -45.101 -17.446 1.00 153.00 ? 430 ASN A O   1 
ATOM   3263 C CB  . ASN A 1 430 ? -22.980 -45.484 -20.619 1.00 157.93 ? 430 ASN A CB  1 
ATOM   3264 C CG  . ASN A 1 430 ? -24.354 -45.899 -20.145 1.00 178.60 ? 430 ASN A CG  1 
ATOM   3265 O OD1 . ASN A 1 430 ? -24.490 -46.472 -19.057 1.00 183.92 ? 430 ASN A OD1 1 
ATOM   3266 N ND2 . ASN A 1 430 ? -25.380 -45.652 -20.949 1.00 195.19 ? 430 ASN A ND2 1 
ATOM   3267 N N   . ALA A 1 431 ? -20.549 -45.205 -18.403 1.00 160.91 ? 431 ALA A N   1 
ATOM   3268 C CA  . ALA A 1 431 ? -19.945 -46.066 -17.404 1.00 164.82 ? 431 ALA A CA  1 
ATOM   3269 C C   . ALA A 1 431 ? -19.309 -45.271 -16.266 1.00 165.19 ? 431 ALA A C   1 
ATOM   3270 O O   . ALA A 1 431 ? -19.488 -45.625 -15.104 1.00 176.08 ? 431 ALA A O   1 
ATOM   3271 C CB  . ALA A 1 431 ? -18.956 -46.985 -18.068 1.00 183.58 ? 431 ALA A CB  1 
ATOM   3272 N N   . CYS A 1 432 ? -18.563 -44.213 -16.600 1.00 158.01 ? 432 CYS A N   1 
ATOM   3273 C CA  . CYS A 1 432 ? -17.875 -43.446 -15.578 1.00 144.01 ? 432 CYS A CA  1 
ATOM   3274 C C   . CYS A 1 432 ? -18.394 -42.014 -15.542 1.00 132.26 ? 432 CYS A C   1 
ATOM   3275 O O   . CYS A 1 432 ? -18.020 -41.250 -14.669 1.00 129.91 ? 432 CYS A O   1 
ATOM   3276 C CB  . CYS A 1 432 ? -16.367 -43.537 -15.758 1.00 154.65 ? 432 CYS A CB  1 
ATOM   3277 S SG  . CYS A 1 432 ? -15.672 -45.058 -15.056 1.00 183.60 ? 432 CYS A SG  1 
ATOM   3278 N N   . GLY A 1 433 ? -19.280 -41.673 -16.474 1.00 125.98 ? 433 GLY A N   1 
ATOM   3279 C CA  . GLY A 1 433 ? -19.722 -40.296 -16.615 1.00 134.94 ? 433 GLY A CA  1 
ATOM   3280 C C   . GLY A 1 433 ? -18.535 -39.382 -16.908 1.00 138.54 ? 433 GLY A C   1 
ATOM   3281 O O   . GLY A 1 433 ? -18.340 -38.365 -16.247 1.00 158.76 ? 433 GLY A O   1 
ATOM   3282 N N   . PHE A 1 434 ? -17.745 -39.795 -17.904 1.00 119.88 ? 434 PHE A N   1 
ATOM   3283 C CA  . PHE A 1 434 ? -16.546 -39.098 -18.325 1.00 107.76 ? 434 PHE A CA  1 
ATOM   3284 C C   . PHE A 1 434 ? -16.570 -38.850 -19.844 1.00 96.01  ? 434 PHE A C   1 
ATOM   3285 O O   . PHE A 1 434 ? -16.977 -39.685 -20.664 1.00 109.19 ? 434 PHE A O   1 
ATOM   3286 C CB  . PHE A 1 434 ? -15.269 -39.838 -17.903 1.00 104.19 ? 434 PHE A CB  1 
ATOM   3287 C CG  . PHE A 1 434 ? -14.001 -39.223 -18.483 1.00 102.33 ? 434 PHE A CG  1 
ATOM   3288 C CD1 . PHE A 1 434 ? -13.338 -38.207 -17.807 1.00 114.64 ? 434 PHE A CD1 1 
ATOM   3289 C CD2 . PHE A 1 434 ? -13.491 -39.629 -19.710 1.00 97.07  ? 434 PHE A CD2 1 
ATOM   3290 C CE1 . PHE A 1 434 ? -12.204 -37.616 -18.348 1.00 120.60 ? 434 PHE A CE1 1 
ATOM   3291 C CE2 . PHE A 1 434 ? -12.358 -39.039 -20.247 1.00 105.73 ? 434 PHE A CE2 1 
ATOM   3292 C CZ  . PHE A 1 434 ? -11.710 -38.037 -19.562 1.00 115.53 ? 434 PHE A CZ  1 
ATOM   3293 N N   . VAL A 1 435 ? -16.064 -37.701 -20.232 1.00 80.71  ? 435 VAL A N   1 
ATOM   3294 C CA  . VAL A 1 435 ? -15.870 -37.431 -21.643 1.00 80.11  ? 435 VAL A CA  1 
ATOM   3295 C C   . VAL A 1 435 ? -14.815 -36.345 -21.814 1.00 87.82  ? 435 VAL A C   1 
ATOM   3296 O O   . VAL A 1 435 ? -14.647 -35.406 -21.023 1.00 83.34  ? 435 VAL A O   1 
ATOM   3297 C CB  . VAL A 1 435 ? -17.190 -37.133 -22.378 1.00 77.17  ? 435 VAL A CB  1 
ATOM   3298 C CG1 . VAL A 1 435 ? -17.872 -35.902 -21.817 1.00 83.00  ? 435 VAL A CG1 1 
ATOM   3299 C CG2 . VAL A 1 435 ? -17.037 -37.020 -23.887 1.00 74.29  ? 435 VAL A CG2 1 
ATOM   3300 N N   . GLU A 1 436 ? -14.069 -36.484 -22.906 1.00 100.45 ? 436 GLU A N   1 
ATOM   3301 C CA  . GLU A 1 436 ? -13.303 -35.407 -23.523 1.00 114.56 ? 436 GLU A CA  1 
ATOM   3302 C C   . GLU A 1 436 ? -14.179 -34.666 -24.543 1.00 106.17 ? 436 GLU A C   1 
ATOM   3303 O O   . GLU A 1 436 ? -14.931 -35.250 -25.333 1.00 100.99 ? 436 GLU A O   1 
ATOM   3304 C CB  . GLU A 1 436 ? -11.993 -35.878 -24.162 1.00 133.82 ? 436 GLU A CB  1 
ATOM   3305 C CG  . GLU A 1 436 ? -11.114 -36.751 -23.264 1.00 139.21 ? 436 GLU A CG  1 
ATOM   3306 C CD  . GLU A 1 436 ? -9.649  -36.851 -23.692 1.00 134.44 ? 436 GLU A CD  1 
ATOM   3307 O OE1 . GLU A 1 436 ? -9.451  -36.932 -24.927 1.00 131.81 ? 436 GLU A OE1 1 
ATOM   3308 O OE2 . GLU A 1 436 ? -8.722  -36.816 -22.847 1.00 120.45 ? 436 GLU A OE2 1 
ATOM   3309 N N   . LEU A 1 437 ? -14.045 -33.341 -24.530 1.00 107.43 ? 437 LEU A N   1 
ATOM   3310 C CA  . LEU A 1 437 ? -14.606 -32.494 -25.571 1.00 118.75 ? 437 LEU A CA  1 
ATOM   3311 C C   . LEU A 1 437 ? -13.557 -31.506 -26.077 1.00 112.72 ? 437 LEU A C   1 
ATOM   3312 O O   . LEU A 1 437 ? -12.777 -30.888 -25.330 1.00 111.76 ? 437 LEU A O   1 
ATOM   3313 C CB  . LEU A 1 437 ? -15.971 -31.859 -25.297 1.00 139.59 ? 437 LEU A CB  1 
ATOM   3314 C CG  . LEU A 1 437 ? -16.010 -30.641 -24.367 1.00 135.16 ? 437 LEU A CG  1 
ATOM   3315 C CD1 . LEU A 1 437 ? -15.810 -29.334 -25.133 1.00 150.91 ? 437 LEU A CD1 1 
ATOM   3316 C CD2 . LEU A 1 437 ? -17.313 -30.624 -23.578 1.00 111.01 ? 437 LEU A CD2 1 
ATOM   3317 N N   . THR A 1 438 ? -13.609 -31.323 -27.397 1.00 107.25 ? 438 THR A N   1 
ATOM   3318 C CA  . THR A 1 438 ? -12.782 -30.375 -28.127 1.00 117.23 ? 438 THR A CA  1 
ATOM   3319 C C   . THR A 1 438 ? -13.661 -29.499 -29.020 1.00 115.68 ? 438 THR A C   1 
ATOM   3320 O O   . THR A 1 438 ? -14.515 -29.968 -29.766 1.00 126.65 ? 438 THR A O   1 
ATOM   3321 C CB  . THR A 1 438 ? -11.714 -31.097 -28.940 1.00 123.00 ? 438 THR A CB  1 
ATOM   3322 O OG1 . THR A 1 438 ? -10.819 -31.642 -27.974 1.00 122.00 ? 438 THR A OG1 1 
ATOM   3323 C CG2 . THR A 1 438 ? -10.987 -30.151 -29.876 1.00 123.83 ? 438 THR A CG2 1 
ATOM   3324 N N   . ALA A 1 439 ? -13.375 -28.199 -28.951 1.00 116.29 ? 439 ALA A N   1 
ATOM   3325 C CA  . ALA A 1 439 ? -14.144 -27.150 -29.592 1.00 116.06 ? 439 ALA A CA  1 
ATOM   3326 C C   . ALA A 1 439 ? -13.234 -26.269 -30.457 1.00 127.21 ? 439 ALA A C   1 
ATOM   3327 O O   . ALA A 1 439 ? -12.168 -25.809 -30.016 1.00 123.34 ? 439 ALA A O   1 
ATOM   3328 C CB  . ALA A 1 439 ? -14.846 -26.344 -28.514 1.00 129.09 ? 439 ALA A CB  1 
ATOM   3329 N N   . LEU A 1 440 ? -13.687 -26.087 -31.708 1.00 132.19 ? 440 LEU A N   1 
ATOM   3330 C CA  . LEU A 1 440 ? -12.932 -25.398 -32.742 1.00 141.65 ? 440 LEU A CA  1 
ATOM   3331 C C   . LEU A 1 440 ? -13.719 -24.220 -33.324 1.00 144.05 ? 440 LEU A C   1 
ATOM   3332 O O   . LEU A 1 440 ? -14.848 -24.393 -33.745 1.00 136.54 ? 440 LEU A O   1 
ATOM   3333 C CB  . LEU A 1 440 ? -12.634 -26.386 -33.866 1.00 131.28 ? 440 LEU A CB  1 
ATOM   3334 C CG  . LEU A 1 440 ? -11.595 -27.463 -33.565 1.00 128.85 ? 440 LEU A CG  1 
ATOM   3335 C CD1 . LEU A 1 440 ? -12.231 -28.645 -32.839 1.00 124.79 ? 440 LEU A CD1 1 
ATOM   3336 C CD2 . LEU A 1 440 ? -10.986 -27.848 -34.920 1.00 120.65 ? 440 LEU A CD2 1 
ATOM   3337 N N   . ALA A 1 441 ? -13.084 -23.046 -33.290 1.00 151.30 ? 441 ALA A N   1 
ATOM   3338 C CA  . ALA A 1 441 ? -13.651 -21.834 -33.856 1.00 157.81 ? 441 ALA A CA  1 
ATOM   3339 C C   . ALA A 1 441 ? -12.630 -20.935 -34.544 1.00 163.07 ? 441 ALA A C   1 
ATOM   3340 O O   . ALA A 1 441 ? -11.389 -21.092 -34.516 1.00 165.09 ? 441 ALA A O   1 
ATOM   3341 C CB  . ALA A 1 441 ? -14.426 -21.074 -32.805 1.00 176.94 ? 441 ALA A CB  1 
ATOM   3342 N N   . ARG A 1 442 ? -13.209 -19.875 -35.126 1.00 172.17 ? 442 ARG A N   1 
ATOM   3343 C CA  . ARG A 1 442 ? -12.505 -18.876 -35.910 1.00 178.63 ? 442 ARG A CA  1 
ATOM   3344 C C   . ARG A 1 442 ? -11.643 -17.997 -35.003 1.00 165.74 ? 442 ARG A C   1 
ATOM   3345 O O   . ARG A 1 442 ? -10.599 -17.506 -35.433 1.00 159.01 ? 442 ARG A O   1 
ATOM   3346 C CB  . ARG A 1 442 ? -13.524 -18.127 -36.782 1.00 188.53 ? 442 ARG A CB  1 
ATOM   3347 C CG  . ARG A 1 442 ? -14.174 -18.970 -37.877 1.00 194.29 ? 442 ARG A CG  1 
ATOM   3348 C CD  . ARG A 1 442 ? -13.423 -19.043 -39.207 1.00 205.49 ? 442 ARG A CD  1 
ATOM   3349 N NE  . ARG A 1 442 ? -12.084 -19.648 -39.170 1.00 246.78 ? 442 ARG A NE  1 
ATOM   3350 C CZ  . ARG A 1 442 ? -11.669 -20.628 -39.962 1.00 285.42 ? 442 ARG A CZ  1 
ATOM   3351 N NH1 . ARG A 1 442 ? -12.505 -21.156 -40.836 1.00 296.98 ? 442 ARG A NH1 1 
ATOM   3352 N NH2 . ARG A 1 442 ? -10.429 -21.082 -39.883 1.00 304.22 ? 442 ARG A NH2 1 
ATOM   3353 N N   . SER A 1 443 ? -12.093 -17.812 -33.753 1.00 163.01 ? 443 SER A N   1 
ATOM   3354 C CA  . SER A 1 443 ? -11.345 -17.077 -32.737 1.00 172.96 ? 443 SER A CA  1 
ATOM   3355 C C   . SER A 1 443 ? -11.280 -17.930 -31.473 1.00 159.81 ? 443 SER A C   1 
ATOM   3356 O O   . SER A 1 443 ? -12.190 -18.730 -31.265 1.00 148.80 ? 443 SER A O   1 
ATOM   3357 C CB  . SER A 1 443 ? -11.978 -15.739 -32.437 1.00 178.85 ? 443 SER A CB  1 
ATOM   3358 O OG  . SER A 1 443 ? -13.200 -15.914 -31.731 1.00 195.20 ? 443 SER A OG  1 
ATOM   3359 N N   . PRO A 1 444 ? -10.247 -17.792 -30.597 1.00 147.78 ? 444 PRO A N   1 
ATOM   3360 C CA  . PRO A 1 444 ? -10.110 -18.646 -29.419 1.00 153.72 ? 444 PRO A CA  1 
ATOM   3361 C C   . PRO A 1 444 ? -11.246 -18.439 -28.433 1.00 147.16 ? 444 PRO A C   1 
ATOM   3362 O O   . PRO A 1 444 ? -11.739 -19.412 -27.861 1.00 152.26 ? 444 PRO A O   1 
ATOM   3363 C CB  . PRO A 1 444 ? -8.734  -18.390 -28.800 1.00 143.13 ? 444 PRO A CB  1 
ATOM   3364 C CG  . PRO A 1 444 ? -8.137  -17.327 -29.687 1.00 146.50 ? 444 PRO A CG  1 
ATOM   3365 C CD  . PRO A 1 444 ? -9.188  -16.778 -30.645 1.00 143.47 ? 444 PRO A CD  1 
ATOM   3366 N N   . GLU A 1 445 ? -11.684 -17.185 -28.308 1.00 144.35 ? 445 GLU A N   1 
ATOM   3367 C CA  . GLU A 1 445 ? -12.814 -16.815 -27.464 1.00 165.46 ? 445 GLU A CA  1 
ATOM   3368 C C   . GLU A 1 445 ? -14.062 -17.588 -27.904 1.00 159.48 ? 445 GLU A C   1 
ATOM   3369 O O   . GLU A 1 445 ? -14.788 -18.152 -27.069 1.00 166.04 ? 445 GLU A O   1 
ATOM   3370 C CB  . GLU A 1 445 ? -12.890 -15.290 -27.563 1.00 181.43 ? 445 GLU A CB  1 
ATOM   3371 C CG  . GLU A 1 445 ? -11.548 -14.602 -27.307 1.00 210.02 ? 445 GLU A CG  1 
ATOM   3372 C CD  . GLU A 1 445 ? -11.137 -13.425 -28.187 1.00 249.95 ? 445 GLU A CD  1 
ATOM   3373 O OE1 . GLU A 1 445 ? -11.351 -13.480 -29.424 1.00 252.34 ? 445 GLU A OE1 1 
ATOM   3374 O OE2 . GLU A 1 445 ? -10.548 -12.473 -27.633 1.00 271.23 ? 445 GLU A OE2 1 
ATOM   3375 N N   . ALA A 1 446 ? -14.271 -17.594 -29.227 1.00 149.47 ? 446 ALA A N   1 
ATOM   3376 C CA  . ALA A 1 446 ? -15.422 -18.267 -29.825 1.00 145.84 ? 446 ALA A CA  1 
ATOM   3377 C C   . ALA A 1 446 ? -15.399 -19.754 -29.477 1.00 145.58 ? 446 ALA A C   1 
ATOM   3378 O O   . ALA A 1 446 ? -16.424 -20.330 -29.098 1.00 127.70 ? 446 ALA A O   1 
ATOM   3379 C CB  . ALA A 1 446 ? -15.493 -18.022 -31.321 1.00 141.18 ? 446 ALA A CB  1 
ATOM   3380 N N   . ALA A 1 447 ? -14.212 -20.340 -29.616 1.00 148.88 ? 447 ALA A N   1 
ATOM   3381 C CA  . ALA A 1 447 ? -13.983 -21.752 -29.331 1.00 146.71 ? 447 ALA A CA  1 
ATOM   3382 C C   . ALA A 1 447 ? -14.359 -22.062 -27.882 1.00 143.45 ? 447 ALA A C   1 
ATOM   3383 O O   . ALA A 1 447 ? -15.052 -23.053 -27.596 1.00 142.37 ? 447 ALA A O   1 
ATOM   3384 C CB  . ALA A 1 447 ? -12.541 -22.100 -29.624 1.00 152.21 ? 447 ALA A CB  1 
ATOM   3385 N N   . ASP A 1 448 ? -13.880 -21.188 -26.995 1.00 132.55 ? 448 ASP A N   1 
ATOM   3386 C CA  . ASP A 1 448 ? -14.117 -21.301 -25.559 1.00 134.62 ? 448 ASP A CA  1 
ATOM   3387 C C   . ASP A 1 448 ? -15.625 -21.311 -25.281 1.00 135.09 ? 448 ASP A C   1 
ATOM   3388 O O   . ASP A 1 448 ? -16.140 -22.141 -24.514 1.00 132.04 ? 448 ASP A O   1 
ATOM   3389 C CB  . ASP A 1 448 ? -13.435 -20.174 -24.789 1.00 137.26 ? 448 ASP A CB  1 
ATOM   3390 C CG  . ASP A 1 448 ? -11.926 -20.268 -24.596 1.00 146.37 ? 448 ASP A CG  1 
ATOM   3391 O OD1 . ASP A 1 448 ? -11.179 -19.967 -25.547 1.00 152.14 ? 448 ASP A OD1 1 
ATOM   3392 O OD2 . ASP A 1 448 ? -11.499 -20.643 -23.481 1.00 157.05 ? 448 ASP A OD2 1 
ATOM   3393 N N   . GLY A 1 449 ? -16.302 -20.360 -25.928 1.00 134.14 ? 449 GLY A N   1 
ATOM   3394 C CA  . GLY A 1 449 ? -17.743 -20.192 -25.799 1.00 141.23 ? 449 GLY A CA  1 
ATOM   3395 C C   . GLY A 1 449 ? -18.467 -21.465 -26.211 1.00 130.71 ? 449 GLY A C   1 
ATOM   3396 O O   . GLY A 1 449 ? -19.374 -21.931 -25.521 1.00 133.26 ? 449 GLY A O   1 
ATOM   3397 N N   . TYR A 1 450 ? -18.033 -22.005 -27.346 1.00 118.65 ? 450 TYR A N   1 
ATOM   3398 C CA  . TYR A 1 450 ? -18.588 -23.232 -27.912 1.00 118.90 ? 450 TYR A CA  1 
ATOM   3399 C C   . TYR A 1 450 ? -18.465 -24.375 -26.911 1.00 109.86 ? 450 TYR A C   1 
ATOM   3400 O O   . TYR A 1 450 ? -19.424 -25.122 -26.676 1.00 101.70 ? 450 TYR A O   1 
ATOM   3401 C CB  . TYR A 1 450 ? -17.820 -23.609 -29.175 1.00 125.10 ? 450 TYR A CB  1 
ATOM   3402 C CG  . TYR A 1 450 ? -18.632 -23.267 -30.410 1.00 151.06 ? 450 TYR A CG  1 
ATOM   3403 C CD1 . TYR A 1 450 ? -20.025 -23.269 -30.369 1.00 157.94 ? 450 TYR A CD1 1 
ATOM   3404 C CD2 . TYR A 1 450 ? -18.005 -22.939 -31.604 1.00 164.30 ? 450 TYR A CD2 1 
ATOM   3405 C CE1 . TYR A 1 450 ? -20.769 -22.939 -31.486 1.00 175.06 ? 450 TYR A CE1 1 
ATOM   3406 C CE2 . TYR A 1 450 ? -18.742 -22.629 -32.736 1.00 184.21 ? 450 TYR A CE2 1 
ATOM   3407 C CZ  . TYR A 1 450 ? -20.127 -22.624 -32.673 1.00 185.66 ? 450 TYR A CZ  1 
ATOM   3408 O OH  . TYR A 1 450 ? -20.862 -22.314 -33.781 1.00 183.87 ? 450 TYR A OH  1 
ATOM   3409 N N   . SER A 1 451 ? -17.265 -24.476 -26.339 1.00 105.09 ? 451 SER A N   1 
ATOM   3410 C CA  . SER A 1 451 ? -16.935 -25.497 -25.352 1.00 106.51 ? 451 SER A CA  1 
ATOM   3411 C C   . SER A 1 451 ? -17.902 -25.415 -24.163 1.00 101.72 ? 451 SER A C   1 
ATOM   3412 O O   . SER A 1 451 ? -18.468 -26.429 -23.702 1.00 96.26  ? 451 SER A O   1 
ATOM   3413 C CB  . SER A 1 451 ? -15.489 -25.293 -24.913 1.00 120.61 ? 451 SER A CB  1 
ATOM   3414 O OG  . SER A 1 451 ? -15.152 -25.950 -23.693 1.00 135.49 ? 451 SER A OG  1 
ATOM   3415 N N   . ARG A 1 452 ? -18.062 -24.174 -23.699 1.00 115.00 ? 452 ARG A N   1 
ATOM   3416 C CA  . ARG A 1 452 ? -18.923 -23.870 -22.559 1.00 125.01 ? 452 ARG A CA  1 
ATOM   3417 C C   . ARG A 1 452 ? -20.360 -24.322 -22.849 1.00 109.59 ? 452 ARG A C   1 
ATOM   3418 O O   . ARG A 1 452 ? -21.013 -24.952 -22.011 1.00 93.29  ? 452 ARG A O   1 
ATOM   3419 C CB  . ARG A 1 452 ? -18.609 -22.456 -22.041 1.00 138.45 ? 452 ARG A CB  1 
ATOM   3420 C CG  . ARG A 1 452 ? -18.731 -22.127 -20.556 1.00 147.77 ? 452 ARG A CG  1 
ATOM   3421 C CD  . ARG A 1 452 ? -17.631 -21.178 -20.054 1.00 173.49 ? 452 ARG A CD  1 
ATOM   3422 N NE  . ARG A 1 452 ? -17.373 -19.976 -20.863 1.00 189.76 ? 452 ARG A NE  1 
ATOM   3423 C CZ  . ARG A 1 452 ? -16.211 -19.601 -21.410 1.00 187.38 ? 452 ARG A CZ  1 
ATOM   3424 N NH1 . ARG A 1 452 ? -15.153 -20.393 -21.338 1.00 195.93 ? 452 ARG A NH1 1 
ATOM   3425 N NH2 . ARG A 1 452 ? -16.122 -18.457 -22.073 1.00 172.75 ? 452 ARG A NH2 1 
ATOM   3426 N N   . ALA A 1 453 ? -20.811 -23.988 -24.055 1.00 99.76  ? 453 ALA A N   1 
ATOM   3427 C CA  . ALA A 1 453 ? -22.144 -24.317 -24.540 1.00 108.15 ? 453 ALA A CA  1 
ATOM   3428 C C   . ALA A 1 453 ? -22.358 -25.824 -24.493 1.00 112.19 ? 453 ALA A C   1 
ATOM   3429 O O   . ALA A 1 453 ? -23.394 -26.311 -24.012 1.00 125.50 ? 453 ALA A O   1 
ATOM   3430 C CB  . ALA A 1 453 ? -22.242 -23.840 -25.977 1.00 106.18 ? 453 ALA A CB  1 
ATOM   3431 N N   . ALA A 1 454 ? -21.353 -26.531 -25.013 1.00 112.81 ? 454 ALA A N   1 
ATOM   3432 C CA  . ALA A 1 454 ? -21.369 -27.989 -25.080 1.00 117.05 ? 454 ALA A CA  1 
ATOM   3433 C C   . ALA A 1 454 ? -21.526 -28.574 -23.674 1.00 115.93 ? 454 ALA A C   1 
ATOM   3434 O O   . ALA A 1 454 ? -22.345 -29.484 -23.447 1.00 106.99 ? 454 ALA A O   1 
ATOM   3435 C CB  . ALA A 1 454 ? -20.136 -28.483 -25.811 1.00 134.25 ? 454 ALA A CB  1 
ATOM   3436 N N   . GLN A 1 455 ? -20.723 -28.015 -22.757 1.00 121.84 ? 455 GLN A N   1 
ATOM   3437 C CA  . GLN A 1 455 ? -20.717 -28.438 -21.360 1.00 126.05 ? 455 GLN A CA  1 
ATOM   3438 C C   . GLN A 1 455 ? -22.112 -28.282 -20.756 1.00 125.96 ? 455 GLN A C   1 
ATOM   3439 O O   . GLN A 1 455 ? -22.623 -29.180 -20.079 1.00 121.08 ? 455 GLN A O   1 
ATOM   3440 C CB  . GLN A 1 455 ? -19.675 -27.714 -20.501 1.00 121.22 ? 455 GLN A CB  1 
ATOM   3441 C CG  . GLN A 1 455 ? -18.248 -27.933 -20.992 1.00 139.77 ? 455 GLN A CG  1 
ATOM   3442 C CD  . GLN A 1 455 ? -17.238 -26.952 -20.442 1.00 155.79 ? 455 GLN A CD  1 
ATOM   3443 O OE1 . GLN A 1 455 ? -16.933 -26.968 -19.243 1.00 180.79 ? 455 GLN A OE1 1 
ATOM   3444 N NE2 . GLN A 1 455 ? -16.691 -26.115 -21.318 1.00 139.12 ? 455 GLN A NE2 1 
ATOM   3445 N N   . ALA A 1 456 ? -22.696 -27.115 -21.026 1.00 126.83 ? 456 ALA A N   1 
ATOM   3446 C CA  . ALA A 1 456 ? -24.022 -26.760 -20.533 1.00 133.45 ? 456 ALA A CA  1 
ATOM   3447 C C   . ALA A 1 456 ? -25.051 -27.782 -21.017 1.00 136.16 ? 456 ALA A C   1 
ATOM   3448 O O   . ALA A 1 456 ? -25.888 -28.267 -20.240 1.00 148.92 ? 456 ALA A O   1 
ATOM   3449 C CB  . ALA A 1 456 ? -24.376 -25.355 -20.954 1.00 146.27 ? 456 ALA A CB  1 
ATOM   3450 N N   . LEU A 1 457 ? -24.950 -28.093 -22.313 1.00 126.73 ? 457 LEU A N   1 
ATOM   3451 C CA  . LEU A 1 457 ? -25.863 -29.016 -22.971 1.00 116.81 ? 457 LEU A CA  1 
ATOM   3452 C C   . LEU A 1 457 ? -25.763 -30.391 -22.291 1.00 124.24 ? 457 LEU A C   1 
ATOM   3453 O O   . LEU A 1 457 ? -26.797 -31.021 -22.019 1.00 117.62 ? 457 LEU A O   1 
ATOM   3454 C CB  . LEU A 1 457 ? -25.602 -29.048 -24.472 1.00 102.61 ? 457 LEU A CB  1 
ATOM   3455 C CG  . LEU A 1 457 ? -26.510 -29.972 -25.289 1.00 100.79 ? 457 LEU A CG  1 
ATOM   3456 C CD1 . LEU A 1 457 ? -27.964 -29.884 -24.883 1.00 108.40 ? 457 LEU A CD1 1 
ATOM   3457 C CD2 . LEU A 1 457 ? -26.372 -29.638 -26.757 1.00 99.86  ? 457 LEU A CD2 1 
ATOM   3458 N N   . LEU A 1 458 ? -24.520 -30.815 -22.029 1.00 128.86 ? 458 LEU A N   1 
ATOM   3459 C CA  . LEU A 1 458 ? -24.317 -32.197 -21.647 1.00 128.69 ? 458 LEU A CA  1 
ATOM   3460 C C   . LEU A 1 458 ? -24.529 -32.373 -20.154 1.00 136.41 ? 458 LEU A C   1 
ATOM   3461 O O   . LEU A 1 458 ? -24.940 -33.446 -19.758 1.00 149.15 ? 458 LEU A O   1 
ATOM   3462 C CB  . LEU A 1 458 ? -23.061 -32.836 -22.230 1.00 130.53 ? 458 LEU A CB  1 
ATOM   3463 C CG  . LEU A 1 458 ? -22.989 -32.733 -23.759 1.00 130.01 ? 458 LEU A CG  1 
ATOM   3464 C CD1 . LEU A 1 458 ? -21.567 -32.873 -24.255 1.00 128.18 ? 458 LEU A CD1 1 
ATOM   3465 C CD2 . LEU A 1 458 ? -23.936 -33.687 -24.483 1.00 125.75 ? 458 LEU A CD2 1 
ATOM   3466 N N   . THR A 1 459 ? -24.269 -31.336 -19.343 1.00 143.94 ? 459 THR A N   1 
ATOM   3467 C CA  . THR A 1 459 ? -24.331 -31.461 -17.890 1.00 166.17 ? 459 THR A CA  1 
ATOM   3468 C C   . THR A 1 459 ? -25.602 -30.807 -17.358 1.00 181.15 ? 459 THR A C   1 
ATOM   3469 O O   . THR A 1 459 ? -25.573 -30.092 -16.359 1.00 215.02 ? 459 THR A O   1 
ATOM   3470 C CB  . THR A 1 459 ? -23.096 -30.862 -17.212 1.00 177.56 ? 459 THR A CB  1 
ATOM   3471 O OG1 . THR A 1 459 ? -23.010 -29.519 -17.679 1.00 180.70 ? 459 THR A OG1 1 
ATOM   3472 C CG2 . THR A 1 459 ? -21.814 -31.616 -17.514 1.00 196.83 ? 459 THR A CG2 1 
ATOM   3473 N N   . GLY A 1 460 ? -26.716 -31.047 -18.049 1.00 173.89 ? 460 GLY A N   1 
ATOM   3474 C CA  . GLY A 1 460 ? -28.035 -30.633 -17.599 1.00 197.40 ? 460 GLY A CA  1 
ATOM   3475 C C   . GLY A 1 460 ? -29.060 -31.694 -17.985 1.00 223.53 ? 460 GLY A C   1 
ATOM   3476 O O   . GLY A 1 460 ? -28.741 -32.591 -18.756 1.00 245.46 ? 460 GLY A O   1 
ATOM   3477 N N   . PRO A 1 461 ? -30.286 -31.695 -17.420 1.00 222.43 ? 461 PRO A N   1 
ATOM   3478 C CA  . PRO A 1 461 ? -31.366 -32.524 -17.958 1.00 210.69 ? 461 PRO A CA  1 
ATOM   3479 C C   . PRO A 1 461 ? -32.002 -31.896 -19.200 1.00 192.36 ? 461 PRO A C   1 
ATOM   3480 O O   . PRO A 1 461 ? -31.606 -30.806 -19.622 1.00 159.31 ? 461 PRO A O   1 
ATOM   3481 C CB  . PRO A 1 461 ? -32.314 -32.647 -16.758 1.00 212.18 ? 461 PRO A CB  1 
ATOM   3482 C CG  . PRO A 1 461 ? -31.460 -32.189 -15.588 1.00 212.24 ? 461 PRO A CG  1 
ATOM   3483 C CD  . PRO A 1 461 ? -30.657 -31.028 -16.166 1.00 216.94 ? 461 PRO A CD  1 
ATOM   3484 N N   . TYR A 1 462 ? -32.970 -32.615 -19.788 1.00 192.03 ? 462 TYR A N   1 
ATOM   3485 C CA  . TYR A 1 462 ? -33.438 -32.332 -21.136 1.00 188.89 ? 462 TYR A CA  1 
ATOM   3486 C C   . TYR A 1 462 ? -34.833 -32.971 -21.360 1.00 175.57 ? 462 TYR A C   1 
ATOM   3487 O O   . TYR A 1 462 ? -35.580 -32.620 -22.323 1.00 146.37 ? 462 TYR A O   1 
ATOM   3488 C CB  . TYR A 1 462 ? -32.332 -32.927 -22.014 1.00 176.56 ? 462 TYR A CB  1 
ATOM   3489 C CG  . TYR A 1 462 ? -32.347 -32.523 -23.483 1.00 177.89 ? 462 TYR A CG  1 
ATOM   3490 C CD1 . TYR A 1 462 ? -33.241 -33.102 -24.386 1.00 178.18 ? 462 TYR A CD1 1 
ATOM   3491 C CD2 . TYR A 1 462 ? -31.434 -31.590 -23.974 1.00 169.28 ? 462 TYR A CD2 1 
ATOM   3492 C CE1 . TYR A 1 462 ? -33.246 -32.744 -25.726 1.00 167.65 ? 462 TYR A CE1 1 
ATOM   3493 C CE2 . TYR A 1 462 ? -31.424 -31.233 -25.315 1.00 161.80 ? 462 TYR A CE2 1 
ATOM   3494 C CZ  . TYR A 1 462 ? -32.329 -31.813 -26.194 1.00 157.30 ? 462 TYR A CZ  1 
ATOM   3495 O OH  . TYR A 1 462 ? -32.280 -31.458 -27.514 1.00 133.67 ? 462 TYR A OH  1 
ATOM   3496 N N   . GLY B 1 5   ? -3.003  -48.201 50.447  1.00 179.07 ? 5   GLY B N   1 
ATOM   3497 C CA  . GLY B 1 5   ? -2.321  -48.935 49.372  1.00 176.59 ? 5   GLY B CA  1 
ATOM   3498 C C   . GLY B 1 5   ? -2.797  -48.448 48.013  1.00 184.36 ? 5   GLY B C   1 
ATOM   3499 O O   . GLY B 1 5   ? -3.983  -48.408 47.743  1.00 200.38 ? 5   GLY B O   1 
ATOM   3500 N N   . SER B 1 6   ? -1.832  -48.070 47.168  1.00 173.09 ? 6   SER B N   1 
ATOM   3501 C CA  . SER B 1 6   ? -2.054  -47.746 45.769  1.00 172.36 ? 6   SER B CA  1 
ATOM   3502 C C   . SER B 1 6   ? -1.125  -48.555 44.867  1.00 171.89 ? 6   SER B C   1 
ATOM   3503 O O   . SER B 1 6   ? 0.070   -48.758 45.149  1.00 190.24 ? 6   SER B O   1 
ATOM   3504 C CB  . SER B 1 6   ? -1.862  -46.271 45.486  1.00 172.80 ? 6   SER B CB  1 
ATOM   3505 O OG  . SER B 1 6   ? -2.374  -45.443 46.518  1.00 188.66 ? 6   SER B OG  1 
ATOM   3506 N N   . THR B 1 7   ? -1.669  -48.926 43.702  1.00 162.71 ? 7   THR B N   1 
ATOM   3507 C CA  . THR B 1 7   ? -0.899  -49.451 42.574  1.00 152.53 ? 7   THR B CA  1 
ATOM   3508 C C   . THR B 1 7   ? -1.188  -48.648 41.310  1.00 154.74 ? 7   THR B C   1 
ATOM   3509 O O   . THR B 1 7   ? -2.340  -48.466 40.936  1.00 209.45 ? 7   THR B O   1 
ATOM   3510 C CB  . THR B 1 7   ? -1.124  -50.952 42.373  1.00 140.67 ? 7   THR B CB  1 
ATOM   3511 O OG1 . THR B 1 7   ? -0.510  -51.516 43.528  1.00 123.62 ? 7   THR B OG1 1 
ATOM   3512 C CG2 . THR B 1 7   ? -0.453  -51.492 41.118  1.00 126.41 ? 7   THR B CG2 1 
ATOM   3513 N N   . LYS B 1 8   ? -0.103  -48.151 40.695  1.00 133.58 ? 8   LYS B N   1 
ATOM   3514 C CA  . LYS B 1 8   ? -0.163  -47.358 39.482  1.00 132.33 ? 8   LYS B CA  1 
ATOM   3515 C C   . LYS B 1 8   ? 0.751   -47.954 38.415  1.00 130.37 ? 8   LYS B C   1 
ATOM   3516 O O   . LYS B 1 8   ? 1.912   -48.273 38.654  1.00 158.46 ? 8   LYS B O   1 
ATOM   3517 C CB  . LYS B 1 8   ? 0.193   -45.878 39.669  1.00 139.29 ? 8   LYS B CB  1 
ATOM   3518 C CG  . LYS B 1 8   ? -0.506  -45.186 40.831  1.00 161.67 ? 8   LYS B CG  1 
ATOM   3519 C CD  . LYS B 1 8   ? -0.202  -43.715 41.096  1.00 163.77 ? 8   LYS B CD  1 
ATOM   3520 C CE  . LYS B 1 8   ? -0.703  -43.308 42.452  1.00 162.10 ? 8   LYS B CE  1 
ATOM   3521 N NZ  . LYS B 1 8   ? -2.025  -43.851 42.773  1.00 159.68 ? 8   LYS B NZ  1 
ATOM   3522 N N   . ILE B 1 9   ? 0.161   -48.097 37.225  1.00 134.04 ? 9   ILE B N   1 
ATOM   3523 C CA  . ILE B 1 9   ? 0.778   -48.724 36.066  1.00 140.80 ? 9   ILE B CA  1 
ATOM   3524 C C   . ILE B 1 9   ? 0.817   -47.716 34.908  1.00 160.09 ? 9   ILE B C   1 
ATOM   3525 O O   . ILE B 1 9   ? -0.211  -47.165 34.498  1.00 174.57 ? 9   ILE B O   1 
ATOM   3526 C CB  . ILE B 1 9   ? -0.021  -49.995 35.711  1.00 141.25 ? 9   ILE B CB  1 
ATOM   3527 C CG1 . ILE B 1 9   ? 0.050   -51.049 36.832  1.00 142.57 ? 9   ILE B CG1 1 
ATOM   3528 C CG2 . ILE B 1 9   ? 0.386   -50.566 34.354  1.00 137.79 ? 9   ILE B CG2 1 
ATOM   3529 C CD1 . ILE B 1 9   ? -0.957  -52.176 36.708  1.00 165.60 ? 9   ILE B CD1 1 
ATOM   3530 N N   . LEU B 1 10  ? 2.056   -47.472 34.408  1.00 182.31 ? 10  LEU B N   1 
ATOM   3531 C CA  . LEU B 1 10  ? 2.328   -46.340 33.536  1.00 176.66 ? 10  LEU B CA  1 
ATOM   3532 C C   . LEU B 1 10  ? 2.574   -46.829 32.111  1.00 184.03 ? 10  LEU B C   1 
ATOM   3533 O O   . LEU B 1 10  ? 3.576   -47.525 31.882  1.00 185.50 ? 10  LEU B O   1 
ATOM   3534 C CB  . LEU B 1 10  ? 3.544   -45.586 34.077  1.00 158.05 ? 10  LEU B CB  1 
ATOM   3535 C CG  . LEU B 1 10  ? 3.531   -45.223 35.567  1.00 152.57 ? 10  LEU B CG  1 
ATOM   3536 C CD1 . LEU B 1 10  ? 4.843   -44.587 35.975  1.00 169.56 ? 10  LEU B CD1 1 
ATOM   3537 C CD2 . LEU B 1 10  ? 2.383   -44.300 35.915  1.00 158.75 ? 10  LEU B CD2 1 
ATOM   3538 N N   . ILE B 1 11  ? 1.620   -46.507 31.216  1.00 155.69 ? 11  ILE B N   1 
ATOM   3539 C CA  . ILE B 1 11  ? 1.677   -46.937 29.837  1.00 162.30 ? 11  ILE B CA  1 
ATOM   3540 C C   . ILE B 1 11  ? 1.366   -45.673 29.050  1.00 150.17 ? 11  ILE B C   1 
ATOM   3541 O O   . ILE B 1 11  ? 0.206   -45.307 29.007  1.00 176.67 ? 11  ILE B O   1 
ATOM   3542 C CB  . ILE B 1 11  ? 0.627   -48.038 29.548  1.00 177.50 ? 11  ILE B CB  1 
ATOM   3543 C CG1 . ILE B 1 11  ? 0.469   -49.031 30.716  1.00 170.33 ? 11  ILE B CG1 1 
ATOM   3544 C CG2 . ILE B 1 11  ? 0.886   -48.741 28.205  1.00 192.29 ? 11  ILE B CG2 1 
ATOM   3545 C CD1 . ILE B 1 11  ? -0.656  -50.037 30.564  1.00 182.67 ? 11  ILE B CD1 1 
ATOM   3546 N N   . TYR B 1 12  ? 2.423   -44.962 28.634  1.00 124.74 ? 12  TYR B N   1 
ATOM   3547 C CA  . TYR B 1 12  ? 2.295   -43.642 28.047  1.00 118.22 ? 12  TYR B CA  1 
ATOM   3548 C C   . TYR B 1 12  ? 2.460   -43.800 26.544  1.00 129.00 ? 12  TYR B C   1 
ATOM   3549 O O   . TYR B 1 12  ? 3.145   -43.010 25.905  1.00 132.13 ? 12  TYR B O   1 
ATOM   3550 C CB  . TYR B 1 12  ? 3.339   -42.787 28.764  1.00 111.66 ? 12  TYR B CB  1 
ATOM   3551 C CG  . TYR B 1 12  ? 3.050   -41.305 28.966  1.00 119.28 ? 12  TYR B CG  1 
ATOM   3552 C CD1 . TYR B 1 12  ? 3.339   -40.384 27.961  1.00 136.09 ? 12  TYR B CD1 1 
ATOM   3553 C CD2 . TYR B 1 12  ? 2.564   -40.813 30.181  1.00 116.02 ? 12  TYR B CD2 1 
ATOM   3554 C CE1 . TYR B 1 12  ? 3.128   -39.025 28.140  1.00 150.79 ? 12  TYR B CE1 1 
ATOM   3555 C CE2 . TYR B 1 12  ? 2.336   -39.453 30.371  1.00 126.81 ? 12  TYR B CE2 1 
ATOM   3556 C CZ  . TYR B 1 12  ? 2.619   -38.557 29.341  1.00 145.26 ? 12  TYR B CZ  1 
ATOM   3557 O OH  . TYR B 1 12  ? 2.451   -37.197 29.419  1.00 124.47 ? 12  TYR B OH  1 
ATOM   3558 N N   . ALA B 1 13  ? 1.821   -44.847 26.012  1.00 154.35 ? 13  ALA B N   1 
ATOM   3559 C CA  . ALA B 1 13  ? 1.874   -45.191 24.600  1.00 162.14 ? 13  ALA B CA  1 
ATOM   3560 C C   . ALA B 1 13  ? 1.234   -44.113 23.721  1.00 163.52 ? 13  ALA B C   1 
ATOM   3561 O O   . ALA B 1 13  ? 0.182   -43.552 24.042  1.00 143.15 ? 13  ALA B O   1 
ATOM   3562 C CB  . ALA B 1 13  ? 1.214   -46.531 24.378  1.00 169.15 ? 13  ALA B CB  1 
ATOM   3563 N N   . PHE B 1 14  ? 1.903   -43.837 22.594  1.00 182.15 ? 14  PHE B N   1 
ATOM   3564 C CA  . PHE B 1 14  ? 1.382   -42.961 21.554  1.00 193.71 ? 14  PHE B CA  1 
ATOM   3565 C C   . PHE B 1 14  ? 0.600   -43.840 20.590  1.00 188.89 ? 14  PHE B C   1 
ATOM   3566 O O   . PHE B 1 14  ? 1.152   -44.376 19.634  1.00 208.48 ? 14  PHE B O   1 
ATOM   3567 C CB  . PHE B 1 14  ? 2.406   -42.083 20.812  1.00 193.30 ? 14  PHE B CB  1 
ATOM   3568 C CG  . PHE B 1 14  ? 3.010   -40.895 21.557  1.00 190.81 ? 14  PHE B CG  1 
ATOM   3569 C CD1 . PHE B 1 14  ? 3.164   -40.910 22.952  1.00 198.75 ? 14  PHE B CD1 1 
ATOM   3570 C CD2 . PHE B 1 14  ? 3.423   -39.761 20.861  1.00 169.26 ? 14  PHE B CD2 1 
ATOM   3571 C CE1 . PHE B 1 14  ? 3.704   -39.831 23.639  1.00 165.64 ? 14  PHE B CE1 1 
ATOM   3572 C CE2 . PHE B 1 14  ? 3.982   -38.689 21.551  1.00 197.29 ? 14  PHE B CE2 1 
ATOM   3573 C CZ  . PHE B 1 14  ? 4.106   -38.721 22.934  1.00 183.70 ? 14  PHE B CZ  1 
ATOM   3574 N N   . ASN B 1 15  ? -0.693  -43.976 20.889  1.00 181.31 ? 15  ASN B N   1 
ATOM   3575 C CA  . ASN B 1 15  ? -1.611  -44.856 20.190  1.00 188.06 ? 15  ASN B CA  1 
ATOM   3576 C C   . ASN B 1 15  ? -2.181  -44.133 18.971  1.00 216.82 ? 15  ASN B C   1 
ATOM   3577 O O   . ASN B 1 15  ? -2.391  -44.738 17.922  1.00 219.93 ? 15  ASN B O   1 
ATOM   3578 C CB  . ASN B 1 15  ? -2.632  -45.444 21.159  1.00 175.04 ? 15  ASN B CB  1 
ATOM   3579 C CG  . ASN B 1 15  ? -2.873  -44.591 22.391  1.00 173.27 ? 15  ASN B CG  1 
ATOM   3580 O OD1 . ASN B 1 15  ? -2.999  -43.367 22.290  1.00 185.82 ? 15  ASN B OD1 1 
ATOM   3581 N ND2 . ASN B 1 15  ? -2.933  -45.201 23.568  1.00 157.30 ? 15  ASN B ND2 1 
ATOM   3582 N N   . TYR B 1 16  ? -2.383  -42.818 19.120  1.00 242.23 ? 16  TYR B N   1 
ATOM   3583 C CA  . TYR B 1 16  ? -2.962  -41.961 18.098  1.00 240.70 ? 16  TYR B CA  1 
ATOM   3584 C C   . TYR B 1 16  ? -1.937  -41.722 16.984  1.00 257.57 ? 16  TYR B C   1 
ATOM   3585 O O   . TYR B 1 16  ? -2.243  -41.053 16.005  1.00 301.24 ? 16  TYR B O   1 
ATOM   3586 C CB  . TYR B 1 16  ? -3.497  -40.709 18.809  1.00 206.63 ? 16  TYR B CB  1 
ATOM   3587 C CG  . TYR B 1 16  ? -2.383  -39.836 19.368  1.00 189.27 ? 16  TYR B CG  1 
ATOM   3588 C CD1 . TYR B 1 16  ? -1.763  -40.137 20.576  1.00 174.68 ? 16  TYR B CD1 1 
ATOM   3589 C CD2 . TYR B 1 16  ? -1.927  -38.731 18.663  1.00 201.31 ? 16  TYR B CD2 1 
ATOM   3590 C CE1 . TYR B 1 16  ? -0.726  -39.361 21.065  1.00 193.40 ? 16  TYR B CE1 1 
ATOM   3591 C CE2 . TYR B 1 16  ? -0.902  -37.936 19.144  1.00 218.58 ? 16  TYR B CE2 1 
ATOM   3592 C CZ  . TYR B 1 16  ? -0.295  -38.259 20.344  1.00 238.01 ? 16  TYR B CZ  1 
ATOM   3593 O OH  . TYR B 1 16  ? 0.731   -37.489 20.816  1.00 317.79 ? 16  TYR B OH  1 
ATOM   3594 N N   . ALA B 1 17  ? -0.722  -42.266 17.135  1.00 242.57 ? 17  ALA B N   1 
ATOM   3595 C CA  . ALA B 1 17  ? 0.292   -42.254 16.088  1.00 223.67 ? 17  ALA B CA  1 
ATOM   3596 C C   . ALA B 1 17  ? 0.404   -43.649 15.473  1.00 230.89 ? 17  ALA B C   1 
ATOM   3597 O O   . ALA B 1 17  ? 1.180   -44.477 15.938  1.00 233.69 ? 17  ALA B O   1 
ATOM   3598 C CB  . ALA B 1 17  ? 1.628   -41.741 16.616  1.00 189.63 ? 17  ALA B CB  1 
ATOM   3599 N N   . ASP B 1 18  ? -0.406  -43.902 14.438  1.00 246.24 ? 18  ASP B N   1 
ATOM   3600 C CA  . ASP B 1 18  ? -0.446  -45.197 13.774  1.00 249.34 ? 18  ASP B CA  1 
ATOM   3601 C C   . ASP B 1 18  ? 0.640   -45.276 12.704  1.00 256.74 ? 18  ASP B C   1 
ATOM   3602 O O   . ASP B 1 18  ? 1.122   -46.363 12.405  1.00 246.27 ? 18  ASP B O   1 
ATOM   3603 C CB  . ASP B 1 18  ? -1.827  -45.530 13.226  1.00 256.43 ? 18  ASP B CB  1 
ATOM   3604 C CG  . ASP B 1 18  ? -2.626  -46.576 13.994  1.00 259.93 ? 18  ASP B CG  1 
ATOM   3605 O OD1 . ASP B 1 18  ? -2.062  -47.197 14.913  1.00 257.46 ? 18  ASP B OD1 1 
ATOM   3606 O OD2 . ASP B 1 18  ? -3.815  -46.771 13.667  1.00 255.11 ? 18  ASP B OD2 1 
ATOM   3607 N N   . ARG B 1 19  ? 1.006   -44.121 12.133  1.00 262.44 ? 19  ARG B N   1 
ATOM   3608 C CA  . ARG B 1 19  ? 2.020   -44.026 11.094  1.00 258.95 ? 19  ARG B CA  1 
ATOM   3609 C C   . ARG B 1 19  ? 3.349   -43.621 11.716  1.00 274.96 ? 19  ARG B C   1 
ATOM   3610 O O   . ARG B 1 19  ? 4.389   -44.241 11.469  1.00 279.59 ? 19  ARG B O   1 
ATOM   3611 C CB  . ARG B 1 19  ? 1.611   -42.912 10.118  1.00 250.19 ? 19  ARG B CB  1 
ATOM   3612 C CG  . ARG B 1 19  ? 2.540   -42.282 9.076   1.00 259.73 ? 19  ARG B CG  1 
ATOM   3613 C CD  . ARG B 1 19  ? 1.798   -41.880 7.804   1.00 232.11 ? 19  ARG B CD  1 
ATOM   3614 N NE  . ARG B 1 19  ? 0.398   -41.873 8.226   1.00 219.87 ? 19  ARG B NE  1 
ATOM   3615 C CZ  . ARG B 1 19  ? -0.502  -42.820 7.965   1.00 235.74 ? 19  ARG B CZ  1 
ATOM   3616 N NH1 . ARG B 1 19  ? -0.344  -43.651 6.946   1.00 252.28 ? 19  ARG B NH1 1 
ATOM   3617 N NH2 . ARG B 1 19  ? -1.573  -42.906 8.734   1.00 240.43 ? 19  ARG B NH2 1 
ATOM   3618 N N   . MET B 1 20  ? 3.282   -42.570 12.542  1.00 280.37 ? 20  MET B N   1 
ATOM   3619 C CA  . MET B 1 20  ? 4.472   -41.814 12.883  1.00 272.24 ? 20  MET B CA  1 
ATOM   3620 C C   . MET B 1 20  ? 5.482   -42.717 13.583  1.00 276.86 ? 20  MET B C   1 
ATOM   3621 O O   . MET B 1 20  ? 6.670   -42.629 13.290  1.00 307.42 ? 20  MET B O   1 
ATOM   3622 C CB  . MET B 1 20  ? 4.105   -40.484 13.547  1.00 248.72 ? 20  MET B CB  1 
ATOM   3623 C CG  . MET B 1 20  ? 3.321   -39.623 12.566  1.00 209.56 ? 20  MET B CG  1 
ATOM   3624 S SD  . MET B 1 20  ? 3.788   -37.903 12.292  1.00 232.56 ? 20  MET B SD  1 
ATOM   3625 C CE  . MET B 1 20  ? 5.560   -37.702 12.034  1.00 226.16 ? 20  MET B CE  1 
ATOM   3626 N N   . LEU B 1 21  ? 4.977   -43.649 14.406  1.00 242.15 ? 21  LEU B N   1 
ATOM   3627 C CA  . LEU B 1 21  ? 5.786   -44.645 15.096  1.00 211.81 ? 21  LEU B CA  1 
ATOM   3628 C C   . LEU B 1 21  ? 6.697   -45.366 14.096  1.00 241.39 ? 21  LEU B C   1 
ATOM   3629 O O   . LEU B 1 21  ? 7.870   -45.602 14.384  1.00 280.98 ? 21  LEU B O   1 
ATOM   3630 C CB  . LEU B 1 21  ? 4.829   -45.569 15.854  1.00 156.07 ? 21  LEU B CB  1 
ATOM   3631 C CG  . LEU B 1 21  ? 5.379   -46.492 16.950  1.00 159.81 ? 21  LEU B CG  1 
ATOM   3632 C CD1 . LEU B 1 21  ? 6.744   -46.166 17.511  1.00 172.13 ? 21  LEU B CD1 1 
ATOM   3633 C CD2 . LEU B 1 21  ? 4.393   -46.439 18.096  1.00 159.02 ? 21  LEU B CD2 1 
ATOM   3634 N N   . GLU B 1 22  ? 6.181   -45.638 12.891  1.00 232.21 ? 22  GLU B N   1 
ATOM   3635 C CA  . GLU B 1 22  ? 6.946   -46.329 11.862  1.00 228.80 ? 22  GLU B CA  1 
ATOM   3636 C C   . GLU B 1 22  ? 7.903   -45.388 11.124  1.00 222.26 ? 22  GLU B C   1 
ATOM   3637 O O   . GLU B 1 22  ? 8.672   -45.850 10.280  1.00 209.69 ? 22  GLU B O   1 
ATOM   3638 C CB  . GLU B 1 22  ? 6.021   -47.070 10.895  1.00 230.68 ? 22  GLU B CB  1 
ATOM   3639 C CG  . GLU B 1 22  ? 5.127   -48.081 11.605  1.00 236.26 ? 22  GLU B CG  1 
ATOM   3640 C CD  . GLU B 1 22  ? 4.665   -49.256 10.762  1.00 264.24 ? 22  GLU B CD  1 
ATOM   3641 O OE1 . GLU B 1 22  ? 3.873   -48.991 9.841   1.00 300.08 ? 22  GLU B OE1 1 
ATOM   3642 O OE2 . GLU B 1 22  ? 5.088   -50.412 10.999  1.00 262.16 ? 22  GLU B OE2 1 
ATOM   3643 N N   . GLU B 1 23  ? 7.868   -44.085 11.444  1.00 215.30 ? 23  GLU B N   1 
ATOM   3644 C CA  . GLU B 1 23  ? 8.727   -43.104 10.790  1.00 204.91 ? 23  GLU B CA  1 
ATOM   3645 C C   . GLU B 1 23  ? 9.689   -42.499 11.810  1.00 190.10 ? 23  GLU B C   1 
ATOM   3646 O O   . GLU B 1 23  ? 10.814  -42.968 11.944  1.00 180.73 ? 23  GLU B O   1 
ATOM   3647 C CB  . GLU B 1 23  ? 7.955   -42.015 10.036  1.00 218.68 ? 23  GLU B CB  1 
ATOM   3648 C CG  . GLU B 1 23  ? 6.877   -42.541 9.089   1.00 226.28 ? 23  GLU B CG  1 
ATOM   3649 C CD  . GLU B 1 23  ? 7.289   -43.638 8.123   1.00 233.39 ? 23  GLU B CD  1 
ATOM   3650 O OE1 . GLU B 1 23  ? 8.224   -43.436 7.316   1.00 230.97 ? 23  GLU B OE1 1 
ATOM   3651 O OE2 . GLU B 1 23  ? 6.647   -44.711 8.192   1.00 282.74 ? 23  GLU B OE2 1 
ATOM   3652 N N   . VAL B 1 24  ? 9.245   -41.447 12.511  1.00 193.10 ? 24  VAL B N   1 
ATOM   3653 C CA  . VAL B 1 24  ? 10.015  -40.891 13.610  1.00 173.05 ? 24  VAL B CA  1 
ATOM   3654 C C   . VAL B 1 24  ? 10.273  -42.035 14.585  1.00 151.35 ? 24  VAL B C   1 
ATOM   3655 O O   . VAL B 1 24  ? 9.339   -42.643 15.097  1.00 153.82 ? 24  VAL B O   1 
ATOM   3656 C CB  . VAL B 1 24  ? 9.339   -39.678 14.285  1.00 190.48 ? 24  VAL B CB  1 
ATOM   3657 C CG1 . VAL B 1 24  ? 9.442   -38.407 13.445  1.00 197.81 ? 24  VAL B CG1 1 
ATOM   3658 C CG2 . VAL B 1 24  ? 7.886   -39.945 14.679  1.00 195.83 ? 24  VAL B CG2 1 
ATOM   3659 N N   . PRO B 1 25  ? 11.542  -42.425 14.812  1.00 144.86 ? 25  PRO B N   1 
ATOM   3660 C CA  . PRO B 1 25  ? 11.834  -43.698 15.473  1.00 132.54 ? 25  PRO B CA  1 
ATOM   3661 C C   . PRO B 1 25  ? 11.974  -43.518 16.977  1.00 135.14 ? 25  PRO B C   1 
ATOM   3662 O O   . PRO B 1 25  ? 11.782  -44.468 17.719  1.00 132.73 ? 25  PRO B O   1 
ATOM   3663 C CB  . PRO B 1 25  ? 13.157  -44.118 14.810  1.00 129.17 ? 25  PRO B CB  1 
ATOM   3664 C CG  . PRO B 1 25  ? 13.800  -42.787 14.411  1.00 159.03 ? 25  PRO B CG  1 
ATOM   3665 C CD  . PRO B 1 25  ? 12.749  -41.667 14.445  1.00 156.65 ? 25  PRO B CD  1 
ATOM   3666 N N   . TYR B 1 26  ? 12.306  -42.290 17.400  1.00 148.30 ? 26  TYR B N   1 
ATOM   3667 C CA  . TYR B 1 26  ? 12.531  -41.969 18.798  1.00 154.98 ? 26  TYR B CA  1 
ATOM   3668 C C   . TYR B 1 26  ? 11.219  -42.150 19.557  1.00 156.67 ? 26  TYR B C   1 
ATOM   3669 O O   . TYR B 1 26  ? 11.164  -41.937 20.771  1.00 172.00 ? 26  TYR B O   1 
ATOM   3670 C CB  . TYR B 1 26  ? 13.141  -40.566 18.907  1.00 133.08 ? 26  TYR B CB  1 
ATOM   3671 C CG  . TYR B 1 26  ? 12.216  -39.450 18.460  1.00 130.58 ? 26  TYR B CG  1 
ATOM   3672 C CD1 . TYR B 1 26  ? 11.307  -38.881 19.350  1.00 161.21 ? 26  TYR B CD1 1 
ATOM   3673 C CD2 . TYR B 1 26  ? 12.256  -38.963 17.161  1.00 129.67 ? 26  TYR B CD2 1 
ATOM   3674 C CE1 . TYR B 1 26  ? 10.449  -37.864 18.960  1.00 197.69 ? 26  TYR B CE1 1 
ATOM   3675 C CE2 . TYR B 1 26  ? 11.393  -37.949 16.763  1.00 167.68 ? 26  TYR B CE2 1 
ATOM   3676 C CZ  . TYR B 1 26  ? 10.502  -37.383 17.662  1.00 190.38 ? 26  TYR B CZ  1 
ATOM   3677 O OH  . TYR B 1 26  ? 9.644   -36.377 17.298  1.00 180.45 ? 26  TYR B OH  1 
ATOM   3678 N N   . LEU B 1 27  ? 10.166  -42.525 18.818  1.00 135.18 ? 27  LEU B N   1 
ATOM   3679 C CA  . LEU B 1 27  ? 8.843   -42.634 19.406  1.00 144.39 ? 27  LEU B CA  1 
ATOM   3680 C C   . LEU B 1 27  ? 8.792   -43.867 20.298  1.00 144.34 ? 27  LEU B C   1 
ATOM   3681 O O   . LEU B 1 27  ? 8.101   -43.884 21.313  1.00 143.65 ? 27  LEU B O   1 
ATOM   3682 C CB  . LEU B 1 27  ? 7.704   -42.627 18.388  1.00 168.16 ? 27  LEU B CB  1 
ATOM   3683 C CG  . LEU B 1 27  ? 7.144   -41.261 17.968  1.00 188.53 ? 27  LEU B CG  1 
ATOM   3684 C CD1 . LEU B 1 27  ? 5.648   -41.386 17.686  1.00 200.50 ? 27  LEU B CD1 1 
ATOM   3685 C CD2 . LEU B 1 27  ? 7.395   -40.147 18.984  1.00 180.38 ? 27  LEU B CD2 1 
ATOM   3686 N N   . ARG B 1 28  ? 9.528   -44.908 19.917  1.00 145.03 ? 28  ARG B N   1 
ATOM   3687 C CA  . ARG B 1 28  ? 9.440   -46.111 20.724  1.00 158.24 ? 28  ARG B CA  1 
ATOM   3688 C C   . ARG B 1 28  ? 9.875   -45.781 22.159  1.00 149.06 ? 28  ARG B C   1 
ATOM   3689 O O   . ARG B 1 28  ? 9.370   -46.386 23.105  1.00 171.45 ? 28  ARG B O   1 
ATOM   3690 C CB  . ARG B 1 28  ? 10.010  -47.347 20.010  1.00 141.65 ? 28  ARG B CB  1 
ATOM   3691 C CG  . ARG B 1 28  ? 11.486  -47.203 19.678  1.00 163.18 ? 28  ARG B CG  1 
ATOM   3692 C CD  . ARG B 1 28  ? 12.093  -48.567 19.594  1.00 176.02 ? 28  ARG B CD  1 
ATOM   3693 N NE  . ARG B 1 28  ? 11.324  -49.457 18.716  1.00 176.14 ? 28  ARG B NE  1 
ATOM   3694 C CZ  . ARG B 1 28  ? 11.700  -50.714 18.490  1.00 200.85 ? 28  ARG B CZ  1 
ATOM   3695 N NH1 . ARG B 1 28  ? 12.692  -51.267 19.181  1.00 236.89 ? 28  ARG B NH1 1 
ATOM   3696 N NH2 . ARG B 1 28  ? 11.079  -51.424 17.575  1.00 176.31 ? 28  ARG B NH2 1 
ATOM   3697 N N   . TYR B 1 29  ? 10.732  -44.764 22.325  1.00 124.95 ? 29  TYR B N   1 
ATOM   3698 C CA  . TYR B 1 29  ? 11.263  -44.415 23.636  1.00 134.84 ? 29  TYR B CA  1 
ATOM   3699 C C   . TYR B 1 29  ? 10.334  -43.445 24.372  1.00 137.79 ? 29  TYR B C   1 
ATOM   3700 O O   . TYR B 1 29  ? 10.671  -43.010 25.466  1.00 127.44 ? 29  TYR B O   1 
ATOM   3701 C CB  . TYR B 1 29  ? 12.708  -43.911 23.511  1.00 143.86 ? 29  TYR B CB  1 
ATOM   3702 C CG  . TYR B 1 29  ? 13.700  -44.963 23.037  1.00 151.69 ? 29  TYR B CG  1 
ATOM   3703 C CD1 . TYR B 1 29  ? 13.922  -45.215 21.685  1.00 162.94 ? 29  TYR B CD1 1 
ATOM   3704 C CD2 . TYR B 1 29  ? 14.401  -45.738 23.952  1.00 164.20 ? 29  TYR B CD2 1 
ATOM   3705 C CE1 . TYR B 1 29  ? 14.820  -46.190 21.260  1.00 177.94 ? 29  TYR B CE1 1 
ATOM   3706 C CE2 . TYR B 1 29  ? 15.305  -46.710 23.542  1.00 189.87 ? 29  TYR B CE2 1 
ATOM   3707 C CZ  . TYR B 1 29  ? 15.522  -46.940 22.193  1.00 186.21 ? 29  TYR B CZ  1 
ATOM   3708 O OH  . TYR B 1 29  ? 16.417  -47.911 21.818  1.00 169.97 ? 29  TYR B OH  1 
ATOM   3709 N N   . SER B 1 30  ? 9.146   -43.172 23.804  1.00 141.91 ? 30  SER B N   1 
ATOM   3710 C CA  . SER B 1 30  ? 8.268   -42.108 24.286  1.00 136.60 ? 30  SER B CA  1 
ATOM   3711 C C   . SER B 1 30  ? 7.822   -42.340 25.722  1.00 116.74 ? 30  SER B C   1 
ATOM   3712 O O   . SER B 1 30  ? 7.780   -41.408 26.511  1.00 90.17  ? 30  SER B O   1 
ATOM   3713 C CB  . SER B 1 30  ? 7.085   -41.884 23.401  1.00 127.73 ? 30  SER B CB  1 
ATOM   3714 O OG  . SER B 1 30  ? 7.501   -41.280 22.184  1.00 133.23 ? 30  SER B OG  1 
ATOM   3715 N N   . ALA B 1 31  ? 7.487   -43.587 26.053  1.00 118.74 ? 31  ALA B N   1 
ATOM   3716 C CA  . ALA B 1 31  ? 6.930   -43.857 27.369  1.00 114.93 ? 31  ALA B CA  1 
ATOM   3717 C C   . ALA B 1 31  ? 7.861   -43.346 28.457  1.00 107.12 ? 31  ALA B C   1 
ATOM   3718 O O   . ALA B 1 31  ? 7.397   -42.991 29.534  1.00 104.18 ? 31  ALA B O   1 
ATOM   3719 C CB  . ALA B 1 31  ? 6.677   -45.320 27.553  1.00 122.65 ? 31  ALA B CB  1 
ATOM   3720 N N   . GLU B 1 32  ? 9.166   -43.304 28.169  1.00 103.33 ? 32  GLU B N   1 
ATOM   3721 C CA  . GLU B 1 32  ? 10.077  -42.834 29.192  1.00 114.97 ? 32  GLU B CA  1 
ATOM   3722 C C   . GLU B 1 32  ? 9.471   -41.596 29.852  1.00 117.87 ? 32  GLU B C   1 
ATOM   3723 O O   . GLU B 1 32  ? 9.712   -41.345 31.029  1.00 119.21 ? 32  GLU B O   1 
ATOM   3724 C CB  . GLU B 1 32  ? 11.503  -42.692 28.661  1.00 140.20 ? 32  GLU B CB  1 
ATOM   3725 C CG  . GLU B 1 32  ? 12.407  -43.886 28.958  1.00 171.37 ? 32  GLU B CG  1 
ATOM   3726 C CD  . GLU B 1 32  ? 13.903  -43.623 28.802  1.00 187.50 ? 32  GLU B CD  1 
ATOM   3727 O OE1 . GLU B 1 32  ? 14.446  -42.675 29.427  1.00 162.10 ? 32  GLU B OE1 1 
ATOM   3728 O OE2 . GLU B 1 32  ? 14.537  -44.399 28.058  1.00 205.99 ? 32  GLU B OE2 1 
ATOM   3729 N N   . ARG B 1 33  ? 8.618   -40.876 29.110  1.00 111.01 ? 33  ARG B N   1 
ATOM   3730 C CA  . ARG B 1 33  ? 8.001   -39.662 29.624  1.00 108.89 ? 33  ARG B CA  1 
ATOM   3731 C C   . ARG B 1 33  ? 7.397   -39.934 31.000  1.00 105.68 ? 33  ARG B C   1 
ATOM   3732 O O   . ARG B 1 33  ? 7.478   -39.100 31.896  1.00 109.62 ? 33  ARG B O   1 
ATOM   3733 C CB  . ARG B 1 33  ? 7.031   -38.977 28.651  1.00 96.30  ? 33  ARG B CB  1 
ATOM   3734 C CG  . ARG B 1 33  ? 7.702   -38.482 27.377  1.00 96.11  ? 33  ARG B CG  1 
ATOM   3735 C CD  . ARG B 1 33  ? 6.868   -37.757 26.334  1.00 95.07  ? 33  ARG B CD  1 
ATOM   3736 N NE  . ARG B 1 33  ? 7.720   -37.061 25.351  1.00 106.03 ? 33  ARG B NE  1 
ATOM   3737 C CZ  . ARG B 1 33  ? 7.904   -37.374 24.052  1.00 121.02 ? 33  ARG B CZ  1 
ATOM   3738 N NH1 . ARG B 1 33  ? 7.369   -38.457 23.538  1.00 130.73 ? 33  ARG B NH1 1 
ATOM   3739 N NH2 . ARG B 1 33  ? 8.642   -36.624 23.254  1.00 106.87 ? 33  ARG B NH2 1 
ATOM   3740 N N   . SER B 1 34  ? 6.863   -41.141 31.163  1.00 108.39 ? 34  SER B N   1 
ATOM   3741 C CA  . SER B 1 34  ? 6.137   -41.522 32.363  1.00 114.56 ? 34  SER B CA  1 
ATOM   3742 C C   . SER B 1 34  ? 7.002   -41.386 33.617  1.00 111.66 ? 34  SER B C   1 
ATOM   3743 O O   . SER B 1 34  ? 6.488   -41.426 34.736  1.00 98.34  ? 34  SER B O   1 
ATOM   3744 C CB  . SER B 1 34  ? 5.532   -42.917 32.227  1.00 122.74 ? 34  SER B CB  1 
ATOM   3745 O OG  . SER B 1 34  ? 6.425   -43.875 31.648  1.00 118.20 ? 34  SER B OG  1 
ATOM   3746 N N   . LEU B 1 35  ? 8.312   -41.204 33.414  1.00 109.91 ? 35  LEU B N   1 
ATOM   3747 C CA  . LEU B 1 35  ? 9.255   -41.280 34.515  1.00 121.51 ? 35  LEU B CA  1 
ATOM   3748 C C   . LEU B 1 35  ? 9.184   -40.016 35.355  1.00 132.47 ? 35  LEU B C   1 
ATOM   3749 O O   . LEU B 1 35  ? 9.954   -39.876 36.301  1.00 144.50 ? 35  LEU B O   1 
ATOM   3750 C CB  . LEU B 1 35  ? 10.667  -41.526 33.991  1.00 118.84 ? 35  LEU B CB  1 
ATOM   3751 C CG  . LEU B 1 35  ? 10.917  -42.955 33.524  1.00 116.43 ? 35  LEU B CG  1 
ATOM   3752 C CD1 . LEU B 1 35  ? 12.185  -42.938 32.695  1.00 149.68 ? 35  LEU B CD1 1 
ATOM   3753 C CD2 . LEU B 1 35  ? 11.091  -43.776 34.767  1.00 106.17 ? 35  LEU B CD2 1 
ATOM   3754 N N   . CYS B 1 36  ? 8.265   -39.117 34.994  1.00 138.54 ? 36  CYS B N   1 
ATOM   3755 C CA  . CYS B 1 36  ? 8.046   -37.888 35.738  1.00 142.68 ? 36  CYS B CA  1 
ATOM   3756 C C   . CYS B 1 36  ? 7.182   -38.210 36.950  1.00 150.76 ? 36  CYS B C   1 
ATOM   3757 O O   . CYS B 1 36  ? 7.080   -37.396 37.861  1.00 164.38 ? 36  CYS B O   1 
ATOM   3758 C CB  . CYS B 1 36  ? 7.287   -36.885 34.885  1.00 136.22 ? 36  CYS B CB  1 
ATOM   3759 S SG  . CYS B 1 36  ? 6.127   -37.747 33.797  1.00 163.53 ? 36  CYS B SG  1 
ATOM   3760 N N   . PHE B 1 37  ? 6.584   -39.407 36.949  1.00 150.69 ? 37  PHE B N   1 
ATOM   3761 C CA  . PHE B 1 37  ? 5.582   -39.774 37.935  1.00 146.52 ? 37  PHE B CA  1 
ATOM   3762 C C   . PHE B 1 37  ? 6.238   -40.462 39.130  1.00 140.85 ? 37  PHE B C   1 
ATOM   3763 O O   . PHE B 1 37  ? 5.592   -40.654 40.160  1.00 149.56 ? 37  PHE B O   1 
ATOM   3764 C CB  . PHE B 1 37  ? 4.497   -40.655 37.315  1.00 135.25 ? 37  PHE B CB  1 
ATOM   3765 C CG  . PHE B 1 37  ? 3.626   -39.954 36.286  1.00 122.57 ? 37  PHE B CG  1 
ATOM   3766 C CD1 . PHE B 1 37  ? 2.530   -39.198 36.668  1.00 123.08 ? 37  PHE B CD1 1 
ATOM   3767 C CD2 . PHE B 1 37  ? 3.905   -40.067 34.930  1.00 138.28 ? 37  PHE B CD2 1 
ATOM   3768 C CE1 . PHE B 1 37  ? 1.747   -38.561 35.712  1.00 153.52 ? 37  PHE B CE1 1 
ATOM   3769 C CE2 . PHE B 1 37  ? 3.119   -39.429 33.978  1.00 146.34 ? 37  PHE B CE2 1 
ATOM   3770 C CZ  . PHE B 1 37  ? 2.048   -38.667 34.369  1.00 152.67 ? 37  PHE B CZ  1 
ATOM   3771 N N   . LEU B 1 38  ? 7.521   -40.816 39.012  1.00 121.79 ? 38  LEU B N   1 
ATOM   3772 C CA  . LEU B 1 38  ? 8.233   -41.476 40.097  1.00 133.37 ? 38  LEU B CA  1 
ATOM   3773 C C   . LEU B 1 38  ? 8.100   -40.700 41.411  1.00 139.73 ? 38  LEU B C   1 
ATOM   3774 O O   . LEU B 1 38  ? 8.253   -41.263 42.491  1.00 141.64 ? 38  LEU B O   1 
ATOM   3775 C CB  . LEU B 1 38  ? 9.695   -41.746 39.741  1.00 130.26 ? 38  LEU B CB  1 
ATOM   3776 C CG  . LEU B 1 38  ? 9.948   -42.517 38.444  1.00 120.84 ? 38  LEU B CG  1 
ATOM   3777 C CD1 . LEU B 1 38  ? 11.422  -42.554 38.111  1.00 112.85 ? 38  LEU B CD1 1 
ATOM   3778 C CD2 . LEU B 1 38  ? 9.448   -43.942 38.561  1.00 100.22 ? 38  LEU B CD2 1 
ATOM   3779 N N   . GLY B 1 39  ? 7.813   -39.402 41.317  1.00 151.88 ? 39  GLY B N   1 
ATOM   3780 C CA  . GLY B 1 39  ? 7.591   -38.570 42.488  1.00 174.69 ? 39  GLY B CA  1 
ATOM   3781 C C   . GLY B 1 39  ? 6.545   -39.179 43.410  1.00 189.44 ? 39  GLY B C   1 
ATOM   3782 O O   . GLY B 1 39  ? 6.625   -39.003 44.620  1.00 186.09 ? 39  GLY B O   1 
ATOM   3783 N N   . ASP B 1 40  ? 5.584   -39.902 42.816  1.00 196.17 ? 40  ASP B N   1 
ATOM   3784 C CA  . ASP B 1 40  ? 4.482   -40.516 43.538  1.00 189.33 ? 40  ASP B CA  1 
ATOM   3785 C C   . ASP B 1 40  ? 5.029   -41.453 44.608  1.00 174.08 ? 40  ASP B C   1 
ATOM   3786 O O   . ASP B 1 40  ? 4.434   -41.560 45.672  1.00 188.07 ? 40  ASP B O   1 
ATOM   3787 C CB  . ASP B 1 40  ? 3.460   -41.161 42.610  1.00 212.81 ? 40  ASP B CB  1 
ATOM   3788 C CG  . ASP B 1 40  ? 2.724   -40.223 41.656  1.00 229.45 ? 40  ASP B CG  1 
ATOM   3789 O OD1 . ASP B 1 40  ? 3.088   -39.031 41.597  1.00 235.04 ? 40  ASP B OD1 1 
ATOM   3790 O OD2 . ASP B 1 40  ? 1.788   -40.686 40.970  1.00 215.58 ? 40  ASP B OD2 1 
ATOM   3791 N N   . LEU B 1 41  ? 6.180   -42.086 44.343  1.00 148.11 ? 41  LEU B N   1 
ATOM   3792 C CA  . LEU B 1 41  ? 6.764   -43.031 45.288  1.00 129.80 ? 41  LEU B CA  1 
ATOM   3793 C C   . LEU B 1 41  ? 7.080   -42.371 46.628  1.00 133.89 ? 41  LEU B C   1 
ATOM   3794 O O   . LEU B 1 41  ? 7.409   -43.071 47.577  1.00 119.35 ? 41  LEU B O   1 
ATOM   3795 C CB  . LEU B 1 41  ? 7.975   -43.762 44.717  1.00 114.57 ? 41  LEU B CB  1 
ATOM   3796 C CG  . LEU B 1 41  ? 7.649   -44.919 43.771  1.00 120.49 ? 41  LEU B CG  1 
ATOM   3797 C CD1 . LEU B 1 41  ? 8.891   -45.377 43.016  1.00 124.90 ? 41  LEU B CD1 1 
ATOM   3798 C CD2 . LEU B 1 41  ? 7.011   -46.087 44.534  1.00 139.05 ? 41  LEU B CD2 1 
ATOM   3799 N N   . ARG B 1 42  ? 6.931   -41.040 46.707  1.00 155.03 ? 42  ARG B N   1 
ATOM   3800 C CA  . ARG B 1 42  ? 7.072   -40.294 47.953  1.00 169.22 ? 42  ARG B CA  1 
ATOM   3801 C C   . ARG B 1 42  ? 6.018   -40.709 48.983  1.00 183.96 ? 42  ARG B C   1 
ATOM   3802 O O   . ARG B 1 42  ? 6.302   -40.666 50.181  1.00 173.48 ? 42  ARG B O   1 
ATOM   3803 C CB  . ARG B 1 42  ? 7.041   -38.770 47.777  1.00 185.20 ? 42  ARG B CB  1 
ATOM   3804 C CG  . ARG B 1 42  ? 8.284   -38.163 47.145  1.00 185.18 ? 42  ARG B CG  1 
ATOM   3805 C CD  . ARG B 1 42  ? 8.552   -36.717 47.546  1.00 169.74 ? 42  ARG B CD  1 
ATOM   3806 N NE  . ARG B 1 42  ? 9.955   -36.361 47.299  1.00 168.68 ? 42  ARG B NE  1 
ATOM   3807 C CZ  . ARG B 1 42  ? 11.043  -36.881 47.879  1.00 172.33 ? 42  ARG B CZ  1 
ATOM   3808 N NH1 . ARG B 1 42  ? 10.962  -37.759 48.863  1.00 189.72 ? 42  ARG B NH1 1 
ATOM   3809 N NH2 . ARG B 1 42  ? 12.239  -36.509 47.465  1.00 177.10 ? 42  ARG B NH2 1 
ATOM   3810 N N   . ASP B 1 43  ? 4.802   -41.066 48.522  1.00 212.58 ? 43  ASP B N   1 
ATOM   3811 C CA  . ASP B 1 43  ? 3.783   -41.667 49.376  1.00 201.01 ? 43  ASP B CA  1 
ATOM   3812 C C   . ASP B 1 43  ? 4.211   -43.092 49.704  1.00 179.52 ? 43  ASP B C   1 
ATOM   3813 O O   . ASP B 1 43  ? 4.407   -43.905 48.802  1.00 146.50 ? 43  ASP B O   1 
ATOM   3814 C CB  . ASP B 1 43  ? 2.379   -41.656 48.780  1.00 207.70 ? 43  ASP B CB  1 
ATOM   3815 C CG  . ASP B 1 43  ? 1.397   -42.641 49.409  1.00 209.18 ? 43  ASP B CG  1 
ATOM   3816 O OD1 . ASP B 1 43  ? 1.228   -42.606 50.645  1.00 199.46 ? 43  ASP B OD1 1 
ATOM   3817 O OD2 . ASP B 1 43  ? 0.812   -43.447 48.660  1.00 224.81 ? 43  ASP B OD2 1 
ATOM   3818 N N   . PRO B 1 44  ? 4.363   -43.424 51.010  1.00 178.37 ? 44  PRO B N   1 
ATOM   3819 C CA  . PRO B 1 44  ? 4.829   -44.749 51.428  1.00 167.56 ? 44  PRO B CA  1 
ATOM   3820 C C   . PRO B 1 44  ? 4.008   -45.888 50.838  1.00 148.61 ? 44  PRO B C   1 
ATOM   3821 O O   . PRO B 1 44  ? 4.494   -47.009 50.743  1.00 135.52 ? 44  PRO B O   1 
ATOM   3822 C CB  . PRO B 1 44  ? 4.721   -44.702 52.957  1.00 179.89 ? 44  PRO B CB  1 
ATOM   3823 C CG  . PRO B 1 44  ? 4.858   -43.228 53.279  1.00 179.89 ? 44  PRO B CG  1 
ATOM   3824 C CD  . PRO B 1 44  ? 4.112   -42.525 52.152  1.00 175.29 ? 44  PRO B CD  1 
ATOM   3825 N N   . GLY B 1 45  ? 2.774   -45.571 50.433  1.00 153.99 ? 45  GLY B N   1 
ATOM   3826 C CA  . GLY B 1 45  ? 1.800   -46.564 50.010  1.00 165.14 ? 45  GLY B CA  1 
ATOM   3827 C C   . GLY B 1 45  ? 1.921   -46.899 48.527  1.00 167.73 ? 45  GLY B C   1 
ATOM   3828 O O   . GLY B 1 45  ? 1.840   -48.072 48.143  1.00 159.58 ? 45  GLY B O   1 
ATOM   3829 N N   . THR B 1 46  ? 2.115   -45.850 47.718  1.00 177.24 ? 46  THR B N   1 
ATOM   3830 C CA  . THR B 1 46  ? 2.177   -45.965 46.277  1.00 182.92 ? 46  THR B CA  1 
ATOM   3831 C C   . THR B 1 46  ? 3.199   -47.035 45.889  1.00 153.51 ? 46  THR B C   1 
ATOM   3832 O O   . THR B 1 46  ? 4.321   -47.122 46.388  1.00 150.71 ? 46  THR B O   1 
ATOM   3833 C CB  . THR B 1 46  ? 2.396   -44.624 45.580  1.00 205.50 ? 46  THR B CB  1 
ATOM   3834 O OG1 . THR B 1 46  ? 1.375   -43.756 46.065  1.00 192.81 ? 46  THR B OG1 1 
ATOM   3835 C CG2 . THR B 1 46  ? 2.287   -44.738 44.071  1.00 229.44 ? 46  THR B CG2 1 
ATOM   3836 N N   . ARG B 1 47  ? 2.771   -47.856 44.932  1.00 133.40 ? 47  ARG B N   1 
ATOM   3837 C CA  . ARG B 1 47  ? 3.609   -48.817 44.226  1.00 136.75 ? 47  ARG B CA  1 
ATOM   3838 C C   . ARG B 1 47  ? 3.440   -48.612 42.722  1.00 138.92 ? 47  ARG B C   1 
ATOM   3839 O O   . ARG B 1 47  ? 2.335   -48.592 42.184  1.00 156.55 ? 47  ARG B O   1 
ATOM   3840 C CB  . ARG B 1 47  ? 3.239   -50.168 44.842  1.00 145.93 ? 47  ARG B CB  1 
ATOM   3841 C CG  . ARG B 1 47  ? 3.726   -51.467 44.223  1.00 181.61 ? 47  ARG B CG  1 
ATOM   3842 C CD  . ARG B 1 47  ? 2.976   -52.575 44.966  1.00 251.47 ? 47  ARG B CD  1 
ATOM   3843 N NE  . ARG B 1 47  ? 3.297   -53.966 44.625  1.00 292.91 ? 47  ARG B NE  1 
ATOM   3844 C CZ  . ARG B 1 47  ? 2.443   -54.983 44.458  1.00 282.70 ? 47  ARG B CZ  1 
ATOM   3845 N NH1 . ARG B 1 47  ? 1.139   -54.852 44.666  1.00 264.35 ? 47  ARG B NH1 1 
ATOM   3846 N NH2 . ARG B 1 47  ? 2.914   -56.163 44.093  1.00 279.99 ? 47  ARG B NH2 1 
ATOM   3847 N N   . LEU B 1 48  ? 4.584   -48.495 42.032  1.00 134.78 ? 48  LEU B N   1 
ATOM   3848 C CA  . LEU B 1 48  ? 4.666   -48.094 40.640  1.00 133.07 ? 48  LEU B CA  1 
ATOM   3849 C C   . LEU B 1 48  ? 5.167   -49.240 39.758  1.00 127.19 ? 48  LEU B C   1 
ATOM   3850 O O   . LEU B 1 48  ? 6.086   -49.990 40.094  1.00 123.41 ? 48  LEU B O   1 
ATOM   3851 C CB  . LEU B 1 48  ? 5.507   -46.846 40.374  1.00 122.13 ? 48  LEU B CB  1 
ATOM   3852 C CG  . LEU B 1 48  ? 4.998   -45.542 40.991  1.00 142.13 ? 48  LEU B CG  1 
ATOM   3853 C CD1 . LEU B 1 48  ? 5.943   -44.418 40.648  1.00 155.02 ? 48  LEU B CD1 1 
ATOM   3854 C CD2 . LEU B 1 48  ? 3.595   -45.176 40.559  1.00 161.00 ? 48  LEU B CD2 1 
ATOM   3855 N N   . VAL B 1 49  ? 4.532   -49.324 38.592  1.00 137.53 ? 49  VAL B N   1 
ATOM   3856 C CA  . VAL B 1 49  ? 4.977   -50.168 37.489  1.00 132.37 ? 49  VAL B CA  1 
ATOM   3857 C C   . VAL B 1 49  ? 5.152   -49.337 36.213  1.00 137.19 ? 49  VAL B C   1 
ATOM   3858 O O   . VAL B 1 49  ? 4.241   -48.617 35.796  1.00 177.64 ? 49  VAL B O   1 
ATOM   3859 C CB  . VAL B 1 49  ? 4.000   -51.333 37.312  1.00 120.38 ? 49  VAL B CB  1 
ATOM   3860 C CG1 . VAL B 1 49  ? 4.280   -52.084 36.026  1.00 128.33 ? 49  VAL B CG1 1 
ATOM   3861 C CG2 . VAL B 1 49  ? 4.078   -52.251 38.519  1.00 117.91 ? 49  VAL B CG2 1 
ATOM   3862 N N   . VAL B 1 50  ? 6.372   -49.408 35.675  1.00 115.81 ? 50  VAL B N   1 
ATOM   3863 C CA  . VAL B 1 50  ? 6.736   -48.734 34.447  1.00 129.06 ? 50  VAL B CA  1 
ATOM   3864 C C   . VAL B 1 50  ? 6.808   -49.756 33.317  1.00 132.63 ? 50  VAL B C   1 
ATOM   3865 O O   . VAL B 1 50  ? 7.446   -50.813 33.443  1.00 137.84 ? 50  VAL B O   1 
ATOM   3866 C CB  . VAL B 1 50  ? 8.045   -47.934 34.596  1.00 148.63 ? 50  VAL B CB  1 
ATOM   3867 C CG1 . VAL B 1 50  ? 8.559   -47.406 33.255  1.00 160.17 ? 50  VAL B CG1 1 
ATOM   3868 C CG2 . VAL B 1 50  ? 7.894   -46.806 35.619  1.00 151.14 ? 50  VAL B CG2 1 
ATOM   3869 N N   . ILE B 1 51  ? 6.166   -49.385 32.201  1.00 129.21 ? 51  ILE B N   1 
ATOM   3870 C CA  . ILE B 1 51  ? 6.178   -50.177 30.980  1.00 143.59 ? 51  ILE B CA  1 
ATOM   3871 C C   . ILE B 1 51  ? 6.613   -49.320 29.791  1.00 143.65 ? 51  ILE B C   1 
ATOM   3872 O O   . ILE B 1 51  ? 6.074   -48.248 29.561  1.00 179.38 ? 51  ILE B O   1 
ATOM   3873 C CB  . ILE B 1 51  ? 4.794   -50.807 30.763  1.00 155.01 ? 51  ILE B CB  1 
ATOM   3874 C CG1 . ILE B 1 51  ? 4.258   -51.414 32.059  1.00 150.77 ? 51  ILE B CG1 1 
ATOM   3875 C CG2 . ILE B 1 51  ? 4.837   -51.823 29.616  1.00 185.88 ? 51  ILE B CG2 1 
ATOM   3876 C CD1 . ILE B 1 51  ? 2.820   -51.886 31.982  1.00 145.70 ? 51  ILE B CD1 1 
ATOM   3877 N N   . THR B 1 52  ? 7.629   -49.816 29.075  1.00 127.42 ? 52  THR B N   1 
ATOM   3878 C CA  . THR B 1 52  ? 8.206   -49.150 27.929  1.00 126.95 ? 52  THR B CA  1 
ATOM   3879 C C   . THR B 1 52  ? 8.450   -50.236 26.898  1.00 120.50 ? 52  THR B C   1 
ATOM   3880 O O   . THR B 1 52  ? 8.628   -51.400 27.246  1.00 112.71 ? 52  THR B O   1 
ATOM   3881 C CB  . THR B 1 52  ? 9.472   -48.386 28.333  1.00 130.54 ? 52  THR B CB  1 
ATOM   3882 O OG1 . THR B 1 52  ? 10.367  -49.291 28.972  1.00 141.24 ? 52  THR B OG1 1 
ATOM   3883 C CG2 . THR B 1 52  ? 9.215   -47.290 29.351  1.00 137.44 ? 52  THR B CG2 1 
ATOM   3884 N N   . SER B 1 53  ? 8.422   -49.837 25.633  1.00 119.53 ? 53  SER B N   1 
ATOM   3885 C CA  . SER B 1 53  ? 8.683   -50.709 24.493  1.00 143.21 ? 53  SER B CA  1 
ATOM   3886 C C   . SER B 1 53  ? 10.143  -51.192 24.485  1.00 152.54 ? 53  SER B C   1 
ATOM   3887 O O   . SER B 1 53  ? 10.463  -52.254 23.940  1.00 154.28 ? 53  SER B O   1 
ATOM   3888 C CB  . SER B 1 53  ? 8.309   -49.973 23.216  1.00 148.17 ? 53  SER B CB  1 
ATOM   3889 O OG  . SER B 1 53  ? 8.165   -50.826 22.090  1.00 168.12 ? 53  SER B OG  1 
ATOM   3890 N N   . GLU B 1 54  ? 11.018  -50.386 25.104  1.00 151.85 ? 54  GLU B N   1 
ATOM   3891 C CA  . GLU B 1 54  ? 12.451  -50.598 25.226  1.00 139.24 ? 54  GLU B CA  1 
ATOM   3892 C C   . GLU B 1 54  ? 12.869  -50.342 26.675  1.00 124.69 ? 54  GLU B C   1 
ATOM   3893 O O   . GLU B 1 54  ? 12.357  -49.432 27.324  1.00 117.19 ? 54  GLU B O   1 
ATOM   3894 C CB  . GLU B 1 54  ? 13.157  -49.592 24.313  1.00 157.49 ? 54  GLU B CB  1 
ATOM   3895 C CG  . GLU B 1 54  ? 13.215  -50.026 22.853  1.00 178.70 ? 54  GLU B CG  1 
ATOM   3896 C CD  . GLU B 1 54  ? 14.037  -51.293 22.684  1.00 211.29 ? 54  GLU B CD  1 
ATOM   3897 O OE1 . GLU B 1 54  ? 15.217  -51.273 23.112  1.00 226.81 ? 54  GLU B OE1 1 
ATOM   3898 O OE2 . GLU B 1 54  ? 13.495  -52.289 22.146  1.00 212.82 ? 54  GLU B OE2 1 
ATOM   3899 N N   . ALA B 1 55  ? 13.856  -51.109 27.153  1.00 116.56 ? 55  ALA B N   1 
ATOM   3900 C CA  . ALA B 1 55  ? 14.189  -51.178 28.571  1.00 113.01 ? 55  ALA B CA  1 
ATOM   3901 C C   . ALA B 1 55  ? 14.769  -49.864 29.093  1.00 111.27 ? 55  ALA B C   1 
ATOM   3902 O O   . ALA B 1 55  ? 15.762  -49.371 28.565  1.00 130.36 ? 55  ALA B O   1 
ATOM   3903 C CB  . ALA B 1 55  ? 15.171  -52.306 28.788  1.00 117.40 ? 55  ALA B CB  1 
ATOM   3904 N N   . VAL B 1 56  ? 14.202  -49.342 30.186  1.00 103.36 ? 56  VAL B N   1 
ATOM   3905 C CA  . VAL B 1 56  ? 14.782  -48.196 30.878  1.00 110.01 ? 56  VAL B CA  1 
ATOM   3906 C C   . VAL B 1 56  ? 16.206  -48.514 31.332  1.00 123.11 ? 56  VAL B C   1 
ATOM   3907 O O   . VAL B 1 56  ? 16.436  -49.545 31.945  1.00 131.26 ? 56  VAL B O   1 
ATOM   3908 C CB  . VAL B 1 56  ? 13.886  -47.833 32.074  1.00 112.53 ? 56  VAL B CB  1 
ATOM   3909 C CG1 . VAL B 1 56  ? 14.574  -46.922 33.088  1.00 106.26 ? 56  VAL B CG1 1 
ATOM   3910 C CG2 . VAL B 1 56  ? 12.578  -47.227 31.571  1.00 130.03 ? 56  VAL B CG2 1 
ATOM   3911 N N   . ASP B 1 57  ? 17.146  -47.602 31.044  1.00 133.93 ? 57  ASP B N   1 
ATOM   3912 C CA  . ASP B 1 57  ? 18.570  -47.786 31.293  1.00 119.91 ? 57  ASP B CA  1 
ATOM   3913 C C   . ASP B 1 57  ? 18.927  -47.400 32.731  1.00 120.24 ? 57  ASP B C   1 
ATOM   3914 O O   . ASP B 1 57  ? 18.521  -46.341 33.238  1.00 110.24 ? 57  ASP B O   1 
ATOM   3915 C CB  . ASP B 1 57  ? 19.399  -46.976 30.316  1.00 122.36 ? 57  ASP B CB  1 
ATOM   3916 C CG  . ASP B 1 57  ? 20.892  -46.988 30.595  1.00 128.50 ? 57  ASP B CG  1 
ATOM   3917 O OD1 . ASP B 1 57  ? 21.282  -46.669 31.749  1.00 126.19 ? 57  ASP B OD1 1 
ATOM   3918 O OD2 . ASP B 1 57  ? 21.639  -47.324 29.651  1.00 130.72 ? 57  ASP B OD2 1 
ATOM   3919 N N   . PRO B 1 58  ? 19.765  -48.217 33.417  1.00 125.00 ? 58  PRO B N   1 
ATOM   3920 C CA  . PRO B 1 58  ? 20.009  -48.034 34.849  1.00 134.78 ? 58  PRO B CA  1 
ATOM   3921 C C   . PRO B 1 58  ? 20.364  -46.582 35.130  1.00 122.45 ? 58  PRO B C   1 
ATOM   3922 O O   . PRO B 1 58  ? 19.943  -46.052 36.153  1.00 115.41 ? 58  PRO B O   1 
ATOM   3923 C CB  . PRO B 1 58  ? 21.172  -48.984 35.181  1.00 128.53 ? 58  PRO B CB  1 
ATOM   3924 C CG  . PRO B 1 58  ? 21.783  -49.262 33.823  1.00 124.39 ? 58  PRO B CG  1 
ATOM   3925 C CD  . PRO B 1 58  ? 20.607  -49.286 32.850  1.00 116.99 ? 58  PRO B CD  1 
ATOM   3926 N N   . ALA B 1 59  ? 21.200  -46.010 34.256  1.00 113.66 ? 59  ALA B N   1 
ATOM   3927 C CA  . ALA B 1 59  ? 21.739  -44.674 34.423  1.00 116.24 ? 59  ALA B CA  1 
ATOM   3928 C C   . ALA B 1 59  ? 20.618  -43.657 34.565  1.00 115.75 ? 59  ALA B C   1 
ATOM   3929 O O   . ALA B 1 59  ? 20.626  -42.802 35.465  1.00 110.54 ? 59  ALA B O   1 
ATOM   3930 C CB  . ALA B 1 59  ? 22.519  -44.334 33.185  1.00 117.03 ? 59  ALA B CB  1 
ATOM   3931 N N   . THR B 1 60  ? 19.665  -43.782 33.637  1.00 112.61 ? 60  THR B N   1 
ATOM   3932 C CA  . THR B 1 60  ? 18.485  -42.925 33.554  1.00 101.82 ? 60  THR B CA  1 
ATOM   3933 C C   . THR B 1 60  ? 17.732  -42.946 34.889  1.00 92.29  ? 60  THR B C   1 
ATOM   3934 O O   . THR B 1 60  ? 17.362  -41.899 35.462  1.00 86.97  ? 60  THR B O   1 
ATOM   3935 C CB  . THR B 1 60  ? 17.596  -43.557 32.479  1.00 85.32  ? 60  THR B CB  1 
ATOM   3936 O OG1 . THR B 1 60  ? 18.382  -43.874 31.328  1.00 74.29  ? 60  THR B OG1 1 
ATOM   3937 C CG2 . THR B 1 60  ? 16.402  -42.681 32.131  1.00 86.04  ? 60  THR B CG2 1 
ATOM   3938 N N   . LEU B 1 61  ? 17.515  -44.191 35.337  1.00 79.97  ? 61  LEU B N   1 
ATOM   3939 C CA  . LEU B 1 61  ? 16.778  -44.450 36.568  1.00 88.70  ? 61  LEU B CA  1 
ATOM   3940 C C   . LEU B 1 61  ? 17.468  -43.775 37.748  1.00 95.08  ? 61  LEU B C   1 
ATOM   3941 O O   . LEU B 1 61  ? 16.813  -43.121 38.576  1.00 85.31  ? 61  LEU B O   1 
ATOM   3942 C CB  . LEU B 1 61  ? 16.557  -45.944 36.757  1.00 99.88  ? 61  LEU B CB  1 
ATOM   3943 C CG  . LEU B 1 61  ? 15.814  -46.369 38.032  1.00 104.86 ? 61  LEU B CG  1 
ATOM   3944 C CD1 . LEU B 1 61  ? 14.544  -45.627 38.387  1.00 87.34  ? 61  LEU B CD1 1 
ATOM   3945 C CD2 . LEU B 1 61  ? 15.516  -47.851 37.931  1.00 139.75 ? 61  LEU B CD2 1 
ATOM   3946 N N   . ASP B 1 62  ? 18.789  -43.943 37.788  1.00 109.88 ? 62  ASP B N   1 
ATOM   3947 C CA  . ASP B 1 62  ? 19.636  -43.382 38.836  1.00 133.60 ? 62  ASP B CA  1 
ATOM   3948 C C   . ASP B 1 62  ? 19.473  -41.868 38.881  1.00 127.32 ? 62  ASP B C   1 
ATOM   3949 O O   . ASP B 1 62  ? 19.297  -41.274 39.958  1.00 113.65 ? 62  ASP B O   1 
ATOM   3950 C CB  . ASP B 1 62  ? 21.101  -43.747 38.626  1.00 133.88 ? 62  ASP B CB  1 
ATOM   3951 C CG  . ASP B 1 62  ? 22.051  -43.391 39.771  1.00 146.34 ? 62  ASP B CG  1 
ATOM   3952 O OD1 . ASP B 1 62  ? 21.564  -43.089 40.887  1.00 155.31 ? 62  ASP B OD1 1 
ATOM   3953 O OD2 . ASP B 1 62  ? 23.281  -43.377 39.535  1.00 154.80 ? 62  ASP B OD2 1 
ATOM   3954 N N   . TYR B 1 63  ? 19.535  -41.275 37.684  1.00 112.76 ? 63  TYR B N   1 
ATOM   3955 C CA  . TYR B 1 63  ? 19.417  -39.831 37.505  1.00 116.01 ? 63  TYR B CA  1 
ATOM   3956 C C   . TYR B 1 63  ? 18.092  -39.345 38.086  1.00 115.27 ? 63  TYR B C   1 
ATOM   3957 O O   . TYR B 1 63  ? 18.042  -38.349 38.842  1.00 118.84 ? 63  TYR B O   1 
ATOM   3958 C CB  . TYR B 1 63  ? 19.442  -39.468 36.011  1.00 115.05 ? 63  TYR B CB  1 
ATOM   3959 C CG  . TYR B 1 63  ? 19.080  -38.023 35.652  1.00 136.21 ? 63  TYR B CG  1 
ATOM   3960 C CD1 . TYR B 1 63  ? 19.410  -36.949 36.490  1.00 123.15 ? 63  TYR B CD1 1 
ATOM   3961 C CD2 . TYR B 1 63  ? 18.379  -37.727 34.480  1.00 134.74 ? 63  TYR B CD2 1 
ATOM   3962 C CE1 . TYR B 1 63  ? 19.048  -35.646 36.185  1.00 117.67 ? 63  TYR B CE1 1 
ATOM   3963 C CE2 . TYR B 1 63  ? 18.044  -36.418 34.150  1.00 124.37 ? 63  TYR B CE2 1 
ATOM   3964 C CZ  . TYR B 1 63  ? 18.369  -35.376 35.008  1.00 122.14 ? 63  TYR B CZ  1 
ATOM   3965 O OH  . TYR B 1 63  ? 18.038  -34.082 34.711  1.00 118.13 ? 63  TYR B OH  1 
ATOM   3966 N N   . HIS B 1 64  ? 17.036  -40.080 37.708  1.00 105.29 ? 64  HIS B N   1 
ATOM   3967 C CA  . HIS B 1 64  ? 15.679  -39.743 38.120  1.00 108.89 ? 64  HIS B CA  1 
ATOM   3968 C C   . HIS B 1 64  ? 15.583  -39.773 39.651  1.00 119.89 ? 64  HIS B C   1 
ATOM   3969 O O   . HIS B 1 64  ? 15.016  -38.856 40.276  1.00 131.60 ? 64  HIS B O   1 
ATOM   3970 C CB  . HIS B 1 64  ? 14.643  -40.521 37.314  1.00 106.86 ? 64  HIS B CB  1 
ATOM   3971 C CG  . HIS B 1 64  ? 14.414  -40.115 35.885  1.00 109.67 ? 64  HIS B CG  1 
ATOM   3972 N ND1 . HIS B 1 64  ? 14.985  -40.789 34.819  1.00 116.24 ? 64  HIS B ND1 1 
ATOM   3973 C CD2 . HIS B 1 64  ? 13.588  -39.211 35.335  1.00 109.62 ? 64  HIS B CD2 1 
ATOM   3974 C CE1 . HIS B 1 64  ? 14.535  -40.286 33.671  1.00 108.18 ? 64  HIS B CE1 1 
ATOM   3975 N NE2 . HIS B 1 64  ? 13.702  -39.313 33.961  1.00 114.55 ? 64  HIS B NE2 1 
ATOM   3976 N N   . LEU B 1 65  ? 16.168  -40.826 40.226  1.00 110.63 ? 65  LEU B N   1 
ATOM   3977 C CA  . LEU B 1 65  ? 16.106  -41.074 41.650  1.00 122.08 ? 65  LEU B CA  1 
ATOM   3978 C C   . LEU B 1 65  ? 16.814  -39.941 42.374  1.00 126.11 ? 65  LEU B C   1 
ATOM   3979 O O   . LEU B 1 65  ? 16.268  -39.483 43.387  1.00 128.49 ? 65  LEU B O   1 
ATOM   3980 C CB  . LEU B 1 65  ? 16.565  -42.494 41.953  1.00 118.13 ? 65  LEU B CB  1 
ATOM   3981 C CG  . LEU B 1 65  ? 15.577  -43.534 41.401  1.00 106.98 ? 65  LEU B CG  1 
ATOM   3982 C CD1 . LEU B 1 65  ? 16.066  -44.961 41.567  1.00 108.39 ? 65  LEU B CD1 1 
ATOM   3983 C CD2 . LEU B 1 65  ? 14.173  -43.343 42.005  1.00 86.19  ? 65  LEU B CD2 1 
ATOM   3984 N N   . ARG B 1 66  ? 17.971  -39.491 41.836  1.00 125.33 ? 66  ARG B N   1 
ATOM   3985 C CA  . ARG B 1 66  ? 18.846  -38.702 42.708  1.00 143.50 ? 66  ARG B CA  1 
ATOM   3986 C C   . ARG B 1 66  ? 18.861  -37.236 42.291  1.00 144.12 ? 66  ARG B C   1 
ATOM   3987 O O   . ARG B 1 66  ? 18.730  -36.334 43.112  1.00 141.68 ? 66  ARG B O   1 
ATOM   3988 C CB  . ARG B 1 66  ? 20.226  -39.352 42.845  1.00 135.24 ? 66  ARG B CB  1 
ATOM   3989 C CG  . ARG B 1 66  ? 20.266  -40.788 43.342  1.00 121.88 ? 66  ARG B CG  1 
ATOM   3990 C CD  . ARG B 1 66  ? 21.690  -41.151 43.788  1.00 121.13 ? 66  ARG B CD  1 
ATOM   3991 N NE  . ARG B 1 66  ? 22.004  -42.558 43.505  1.00 133.31 ? 66  ARG B NE  1 
ATOM   3992 C CZ  . ARG B 1 66  ? 22.049  -43.539 44.405  1.00 133.15 ? 66  ARG B CZ  1 
ATOM   3993 N NH1 . ARG B 1 66  ? 21.903  -43.265 45.692  1.00 132.47 ? 66  ARG B NH1 1 
ATOM   3994 N NH2 . ARG B 1 66  ? 22.259  -44.785 44.002  1.00 122.88 ? 66  ARG B NH2 1 
ATOM   3995 N N   . ASP B 1 67  ? 18.984  -37.030 40.982  1.00 132.46 ? 67  ASP B N   1 
ATOM   3996 C CA  . ASP B 1 67  ? 19.294  -35.725 40.441  1.00 133.78 ? 67  ASP B CA  1 
ATOM   3997 C C   . ASP B 1 67  ? 17.997  -35.077 39.969  1.00 139.47 ? 67  ASP B C   1 
ATOM   3998 O O   . ASP B 1 67  ? 17.939  -33.874 39.731  1.00 153.14 ? 67  ASP B O   1 
ATOM   3999 C CB  . ASP B 1 67  ? 20.454  -35.852 39.467  1.00 140.68 ? 67  ASP B CB  1 
ATOM   4000 C CG  . ASP B 1 67  ? 21.649  -36.628 40.008  1.00 157.01 ? 67  ASP B CG  1 
ATOM   4001 O OD1 . ASP B 1 67  ? 22.287  -36.147 40.968  1.00 171.37 ? 67  ASP B OD1 1 
ATOM   4002 O OD2 . ASP B 1 67  ? 21.934  -37.720 39.482  1.00 165.68 ? 67  ASP B OD2 1 
ATOM   4003 N N   . VAL B 1 68  ? 16.949  -35.893 39.854  1.00 144.51 ? 68  VAL B N   1 
ATOM   4004 C CA  . VAL B 1 68  ? 15.636  -35.374 39.505  1.00 131.17 ? 68  VAL B CA  1 
ATOM   4005 C C   . VAL B 1 68  ? 14.825  -35.235 40.788  1.00 126.08 ? 68  VAL B C   1 
ATOM   4006 O O   . VAL B 1 68  ? 14.617  -34.127 41.263  1.00 126.34 ? 68  VAL B O   1 
ATOM   4007 C CB  . VAL B 1 68  ? 14.866  -36.153 38.421  1.00 127.55 ? 68  VAL B CB  1 
ATOM   4008 C CG1 . VAL B 1 68  ? 13.473  -35.587 38.213  1.00 122.59 ? 68  VAL B CG1 1 
ATOM   4009 C CG2 . VAL B 1 68  ? 15.628  -36.175 37.102  1.00 123.18 ? 68  VAL B CG2 1 
ATOM   4010 N N   . PHE B 1 69  ? 14.422  -36.369 41.370  1.00 119.58 ? 69  PHE B N   1 
ATOM   4011 C CA  . PHE B 1 69  ? 13.439  -36.349 42.437  1.00 124.28 ? 69  PHE B CA  1 
ATOM   4012 C C   . PHE B 1 69  ? 14.089  -36.153 43.800  1.00 132.64 ? 69  PHE B C   1 
ATOM   4013 O O   . PHE B 1 69  ? 13.368  -35.950 44.772  1.00 134.55 ? 69  PHE B O   1 
ATOM   4014 C CB  . PHE B 1 69  ? 12.591  -37.617 42.449  1.00 125.58 ? 69  PHE B CB  1 
ATOM   4015 C CG  . PHE B 1 69  ? 11.717  -37.750 41.217  1.00 130.57 ? 69  PHE B CG  1 
ATOM   4016 C CD1 . PHE B 1 69  ? 10.523  -37.047 41.122  1.00 140.73 ? 69  PHE B CD1 1 
ATOM   4017 C CD2 . PHE B 1 69  ? 12.110  -38.555 40.154  1.00 130.80 ? 69  PHE B CD2 1 
ATOM   4018 C CE1 . PHE B 1 69  ? 9.728   -37.176 40.000  1.00 150.96 ? 69  PHE B CE1 1 
ATOM   4019 C CE2 . PHE B 1 69  ? 11.307  -38.687 39.036  1.00 145.61 ? 69  PHE B CE2 1 
ATOM   4020 C CZ  . PHE B 1 69  ? 10.118  -37.998 38.963  1.00 153.12 ? 69  PHE B CZ  1 
ATOM   4021 N N   . ARG B 1 70  ? 15.426  -36.232 43.855  1.00 134.29 ? 70  ARG B N   1 
ATOM   4022 C CA  . ARG B 1 70  ? 16.221  -35.907 45.036  1.00 156.48 ? 70  ARG B CA  1 
ATOM   4023 C C   . ARG B 1 70  ? 15.836  -36.789 46.232  1.00 149.45 ? 70  ARG B C   1 
ATOM   4024 O O   . ARG B 1 70  ? 15.613  -36.302 47.337  1.00 154.86 ? 70  ARG B O   1 
ATOM   4025 C CB  . ARG B 1 70  ? 16.271  -34.388 45.302  1.00 199.05 ? 70  ARG B CB  1 
ATOM   4026 C CG  . ARG B 1 70  ? 15.026  -33.734 45.891  1.00 211.48 ? 70  ARG B CG  1 
ATOM   4027 C CD  . ARG B 1 70  ? 15.294  -32.427 46.617  1.00 193.69 ? 70  ARG B CD  1 
ATOM   4028 N NE  . ARG B 1 70  ? 14.196  -32.106 47.531  1.00 199.65 ? 70  ARG B NE  1 
ATOM   4029 C CZ  . ARG B 1 70  ? 13.173  -31.304 47.270  1.00 222.94 ? 70  ARG B CZ  1 
ATOM   4030 N NH1 . ARG B 1 70  ? 13.038  -30.729 46.091  1.00 213.65 ? 70  ARG B NH1 1 
ATOM   4031 N NH2 . ARG B 1 70  ? 12.263  -31.082 48.201  1.00 248.15 ? 70  ARG B NH2 1 
ATOM   4032 N N   . PHE B 1 71  ? 15.775  -38.105 46.021  1.00 137.33 ? 71  PHE B N   1 
ATOM   4033 C CA  . PHE B 1 71  ? 15.474  -39.000 47.125  1.00 138.93 ? 71  PHE B CA  1 
ATOM   4034 C C   . PHE B 1 71  ? 16.664  -39.055 48.065  1.00 155.89 ? 71  PHE B C   1 
ATOM   4035 O O   . PHE B 1 71  ? 17.786  -39.252 47.616  1.00 181.23 ? 71  PHE B O   1 
ATOM   4036 C CB  . PHE B 1 71  ? 15.207  -40.428 46.654  1.00 132.44 ? 71  PHE B CB  1 
ATOM   4037 C CG  . PHE B 1 71  ? 13.803  -40.557 46.094  1.00 151.23 ? 71  PHE B CG  1 
ATOM   4038 C CD1 . PHE B 1 71  ? 12.691  -40.399 46.926  1.00 147.76 ? 71  PHE B CD1 1 
ATOM   4039 C CD2 . PHE B 1 71  ? 13.603  -40.827 44.742  1.00 160.01 ? 71  PHE B CD2 1 
ATOM   4040 C CE1 . PHE B 1 71  ? 11.403  -40.521 46.418  1.00 146.06 ? 71  PHE B CE1 1 
ATOM   4041 C CE2 . PHE B 1 71  ? 12.309  -40.943 44.241  1.00 168.33 ? 71  PHE B CE2 1 
ATOM   4042 C CZ  . PHE B 1 71  ? 11.211  -40.789 45.077  1.00 153.53 ? 71  PHE B CZ  1 
ATOM   4043 N N   . ASP B 1 72  ? 16.395  -38.892 49.362  1.00 172.21 ? 72  ASP B N   1 
ATOM   4044 C CA  . ASP B 1 72  ? 17.407  -39.044 50.399  1.00 182.45 ? 72  ASP B CA  1 
ATOM   4045 C C   . ASP B 1 72  ? 17.900  -40.494 50.428  1.00 156.04 ? 72  ASP B C   1 
ATOM   4046 O O   . ASP B 1 72  ? 17.159  -41.414 50.091  1.00 146.42 ? 72  ASP B O   1 
ATOM   4047 C CB  . ASP B 1 72  ? 16.926  -38.467 51.725  1.00 226.69 ? 72  ASP B CB  1 
ATOM   4048 C CG  . ASP B 1 72  ? 15.663  -39.092 52.303  1.00 272.40 ? 72  ASP B CG  1 
ATOM   4049 O OD1 . ASP B 1 72  ? 15.711  -40.295 52.639  1.00 298.17 ? 72  ASP B OD1 1 
ATOM   4050 O OD2 . ASP B 1 72  ? 14.641  -38.372 52.415  1.00 279.69 ? 72  ASP B OD2 1 
ATOM   4051 N N   . GLU B 1 73  ? 19.165  -40.680 50.823  1.00 153.07 ? 73  GLU B N   1 
ATOM   4052 C CA  . GLU B 1 73  ? 19.858  -41.960 50.744  1.00 163.60 ? 73  GLU B CA  1 
ATOM   4053 C C   . GLU B 1 73  ? 19.190  -43.033 51.608  1.00 170.35 ? 73  GLU B C   1 
ATOM   4054 O O   . GLU B 1 73  ? 19.043  -44.174 51.167  1.00 144.46 ? 73  GLU B O   1 
ATOM   4055 C CB  . GLU B 1 73  ? 21.342  -41.845 51.096  1.00 164.34 ? 73  GLU B CB  1 
ATOM   4056 C CG  . GLU B 1 73  ? 22.210  -41.363 49.938  1.00 177.94 ? 73  GLU B CG  1 
ATOM   4057 C CD  . GLU B 1 73  ? 21.934  -41.998 48.582  1.00 174.79 ? 73  GLU B CD  1 
ATOM   4058 O OE1 . GLU B 1 73  ? 21.780  -43.240 48.485  1.00 182.37 ? 73  GLU B OE1 1 
ATOM   4059 O OE2 . GLU B 1 73  ? 21.885  -41.230 47.597  1.00 158.00 ? 73  GLU B OE2 1 
ATOM   4060 N N   . PRO B 1 74  ? 18.815  -42.733 52.874  1.00 194.22 ? 74  PRO B N   1 
ATOM   4061 C CA  . PRO B 1 74  ? 18.022  -43.668 53.676  1.00 194.55 ? 74  PRO B CA  1 
ATOM   4062 C C   . PRO B 1 74  ? 16.827  -44.299 52.959  1.00 201.94 ? 74  PRO B C   1 
ATOM   4063 O O   . PRO B 1 74  ? 16.768  -45.517 52.829  1.00 220.34 ? 74  PRO B O   1 
ATOM   4064 C CB  . PRO B 1 74  ? 17.616  -42.798 54.882  1.00 212.82 ? 74  PRO B CB  1 
ATOM   4065 C CG  . PRO B 1 74  ? 18.799  -41.869 55.058  1.00 221.53 ? 74  PRO B CG  1 
ATOM   4066 C CD  . PRO B 1 74  ? 19.191  -41.520 53.626  1.00 216.73 ? 74  PRO B CD  1 
ATOM   4067 N N   . ALA B 1 75  ? 15.895  -43.476 52.463  1.00 193.87 ? 75  ALA B N   1 
ATOM   4068 C CA  . ALA B 1 75  ? 14.619  -43.980 51.981  1.00 193.20 ? 75  ALA B CA  1 
ATOM   4069 C C   . ALA B 1 75  ? 14.755  -44.682 50.630  1.00 178.22 ? 75  ALA B C   1 
ATOM   4070 O O   . ALA B 1 75  ? 13.846  -45.415 50.234  1.00 189.77 ? 75  ALA B O   1 
ATOM   4071 C CB  . ALA B 1 75  ? 13.610  -42.853 51.929  1.00 218.18 ? 75  ALA B CB  1 
ATOM   4072 N N   . LEU B 1 76  ? 15.907  -44.499 49.964  1.00 164.24 ? 76  LEU B N   1 
ATOM   4073 C CA  . LEU B 1 76  ? 16.051  -44.802 48.546  1.00 162.02 ? 76  LEU B CA  1 
ATOM   4074 C C   . LEU B 1 76  ? 15.713  -46.264 48.290  1.00 148.79 ? 76  LEU B C   1 
ATOM   4075 O O   . LEU B 1 76  ? 15.050  -46.577 47.294  1.00 141.42 ? 76  LEU B O   1 
ATOM   4076 C CB  . LEU B 1 76  ? 17.414  -44.478 47.927  1.00 159.37 ? 76  LEU B CB  1 
ATOM   4077 C CG  . LEU B 1 76  ? 17.697  -45.099 46.546  1.00 138.02 ? 76  LEU B CG  1 
ATOM   4078 C CD1 . LEU B 1 76  ? 16.879  -44.522 45.399  1.00 139.14 ? 76  LEU B CD1 1 
ATOM   4079 C CD2 . LEU B 1 76  ? 19.165  -45.015 46.193  1.00 133.36 ? 76  LEU B CD2 1 
ATOM   4080 N N   . ALA B 1 77  ? 16.237  -47.135 49.161  1.00 128.14 ? 77  ALA B N   1 
ATOM   4081 C CA  . ALA B 1 77  ? 16.089  -48.570 49.029  1.00 124.25 ? 77  ALA B CA  1 
ATOM   4082 C C   . ALA B 1 77  ? 14.609  -48.950 48.998  1.00 133.66 ? 77  ALA B C   1 
ATOM   4083 O O   . ALA B 1 77  ? 14.170  -49.738 48.145  1.00 134.53 ? 77  ALA B O   1 
ATOM   4084 C CB  . ALA B 1 77  ? 16.789  -49.230 50.193  1.00 129.38 ? 77  ALA B CB  1 
ATOM   4085 N N   . ASP B 1 78  ? 13.873  -48.360 49.948  1.00 149.93 ? 78  ASP B N   1 
ATOM   4086 C CA  . ASP B 1 78  ? 12.442  -48.608 50.092  1.00 174.79 ? 78  ASP B CA  1 
ATOM   4087 C C   . ASP B 1 78  ? 11.712  -48.232 48.800  1.00 174.14 ? 78  ASP B C   1 
ATOM   4088 O O   . ASP B 1 78  ? 10.864  -48.987 48.303  1.00 183.82 ? 78  ASP B O   1 
ATOM   4089 C CB  . ASP B 1 78  ? 11.864  -47.891 51.301  1.00 198.92 ? 78  ASP B CB  1 
ATOM   4090 C CG  . ASP B 1 78  ? 10.345  -47.940 51.387  1.00 226.91 ? 78  ASP B CG  1 
ATOM   4091 O OD1 . ASP B 1 78  ? 9.808   -49.055 51.556  1.00 245.56 ? 78  ASP B OD1 1 
ATOM   4092 O OD2 . ASP B 1 78  ? 9.713   -46.871 51.248  1.00 235.91 ? 78  ASP B OD2 1 
ATOM   4093 N N   . VAL B 1 79  ? 12.075  -47.055 48.288  1.00 165.82 ? 79  VAL B N   1 
ATOM   4094 C CA  . VAL B 1 79  ? 11.495  -46.509 47.068  1.00 166.27 ? 79  VAL B CA  1 
ATOM   4095 C C   . VAL B 1 79  ? 11.715  -47.480 45.905  1.00 148.36 ? 79  VAL B C   1 
ATOM   4096 O O   . VAL B 1 79  ? 10.784  -47.782 45.132  1.00 132.55 ? 79  VAL B O   1 
ATOM   4097 C CB  . VAL B 1 79  ? 12.130  -45.129 46.815  1.00 190.25 ? 79  VAL B CB  1 
ATOM   4098 C CG1 . VAL B 1 79  ? 11.606  -44.504 45.529  1.00 225.69 ? 79  VAL B CG1 1 
ATOM   4099 C CG2 . VAL B 1 79  ? 11.903  -44.196 48.001  1.00 200.48 ? 79  VAL B CG2 1 
ATOM   4100 N N   . ARG B 1 80  ? 12.962  -47.954 45.819  1.00 134.13 ? 80  ARG B N   1 
ATOM   4101 C CA  . ARG B 1 80  ? 13.366  -48.880 44.764  1.00 121.79 ? 80  ARG B CA  1 
ATOM   4102 C C   . ARG B 1 80  ? 12.533  -50.148 44.832  1.00 121.69 ? 80  ARG B C   1 
ATOM   4103 O O   . ARG B 1 80  ? 12.079  -50.642 43.803  1.00 118.85 ? 80  ARG B O   1 
ATOM   4104 C CB  . ARG B 1 80  ? 14.814  -49.256 44.435  1.00 120.75 ? 80  ARG B CB  1 
ATOM   4105 C CG  . ARG B 1 80  ? 14.833  -50.295 43.309  1.00 116.58 ? 80  ARG B CG  1 
ATOM   4106 C CD  . ARG B 1 80  ? 14.238  -49.995 41.903  1.00 106.52 ? 80  ARG B CD  1 
ATOM   4107 N NE  . ARG B 1 80  ? 14.636  -50.799 40.732  1.00 124.28 ? 80  ARG B NE  1 
ATOM   4108 C CZ  . ARG B 1 80  ? 15.786  -50.845 39.972  1.00 145.75 ? 80  ARG B CZ  1 
ATOM   4109 N NH1 . ARG B 1 80  ? 16.898  -50.158 40.217  1.00 132.28 ? 80  ARG B NH1 1 
ATOM   4110 N NH2 . ARG B 1 80  ? 15.843  -51.628 38.912  1.00 152.55 ? 80  ARG B NH2 1 
ATOM   4111 N N   . ARG B 1 81  ? 12.363  -50.652 46.056  1.00 126.09 ? 81  ARG B N   1 
ATOM   4112 C CA  . ARG B 1 81  ? 11.570  -51.847 46.324  1.00 139.17 ? 81  ARG B CA  1 
ATOM   4113 C C   . ARG B 1 81  ? 10.153  -51.704 45.757  1.00 148.61 ? 81  ARG B C   1 
ATOM   4114 O O   . ARG B 1 81  ? 9.673   -52.649 45.127  1.00 144.60 ? 81  ARG B O   1 
ATOM   4115 C CB  . ARG B 1 81  ? 11.626  -52.135 47.828  1.00 147.56 ? 81  ARG B CB  1 
ATOM   4116 C CG  . ARG B 1 81  ? 10.598  -53.089 48.416  1.00 164.34 ? 81  ARG B CG  1 
ATOM   4117 C CD  . ARG B 1 81  ? 10.729  -53.266 49.929  1.00 195.81 ? 81  ARG B CD  1 
ATOM   4118 N NE  . ARG B 1 81  ? 11.839  -54.048 50.498  1.00 194.79 ? 81  ARG B NE  1 
ATOM   4119 C CZ  . ARG B 1 81  ? 11.895  -55.373 50.600  1.00 169.88 ? 81  ARG B CZ  1 
ATOM   4120 N NH1 . ARG B 1 81  ? 10.988  -56.123 50.010  1.00 170.35 ? 81  ARG B NH1 1 
ATOM   4121 N NH2 . ARG B 1 81  ? 12.860  -55.958 51.284  1.00 153.27 ? 81  ARG B NH2 1 
ATOM   4122 N N   . ARG B 1 82  ? 9.562   -50.500 45.807  1.00 157.51 ? 82  ARG B N   1 
ATOM   4123 C CA  . ARG B 1 82  ? 8.183   -50.301 45.368  1.00 142.81 ? 82  ARG B CA  1 
ATOM   4124 C C   . ARG B 1 82  ? 8.078   -49.926 43.892  1.00 149.46 ? 82  ARG B C   1 
ATOM   4125 O O   . ARG B 1 82  ? 7.085   -49.308 43.512  1.00 169.56 ? 82  ARG B O   1 
ATOM   4126 C CB  . ARG B 1 82  ? 7.488   -49.276 46.274  1.00 126.41 ? 82  ARG B CB  1 
ATOM   4127 C CG  . ARG B 1 82  ? 7.248   -49.823 47.673  1.00 129.42 ? 82  ARG B CG  1 
ATOM   4128 C CD  . ARG B 1 82  ? 6.597   -48.817 48.595  1.00 135.60 ? 82  ARG B CD  1 
ATOM   4129 N NE  . ARG B 1 82  ? 7.563   -47.790 48.992  1.00 136.02 ? 82  ARG B NE  1 
ATOM   4130 C CZ  . ARG B 1 82  ? 7.459   -46.504 48.670  1.00 150.02 ? 82  ARG B CZ  1 
ATOM   4131 N NH1 . ARG B 1 82  ? 6.458   -46.058 47.919  1.00 141.96 ? 82  ARG B NH1 1 
ATOM   4132 N NH2 . ARG B 1 82  ? 8.407   -45.674 49.069  1.00 173.37 ? 82  ARG B NH2 1 
ATOM   4133 N N   . LEU B 1 83  ? 9.077   -50.315 43.103  1.00 147.72 ? 83  LEU B N   1 
ATOM   4134 C CA  . LEU B 1 83  ? 9.157   -49.965 41.702  1.00 137.21 ? 83  LEU B CA  1 
ATOM   4135 C C   . LEU B 1 83  ? 9.510   -51.204 40.883  1.00 142.45 ? 83  LEU B C   1 
ATOM   4136 O O   . LEU B 1 83  ? 10.458  -51.938 41.190  1.00 151.35 ? 83  LEU B O   1 
ATOM   4137 C CB  . LEU B 1 83  ? 10.127  -48.810 41.468  1.00 127.09 ? 83  LEU B CB  1 
ATOM   4138 C CG  . LEU B 1 83  ? 10.368  -48.439 40.006  1.00 135.45 ? 83  LEU B CG  1 
ATOM   4139 C CD1 . LEU B 1 83  ? 9.075   -47.878 39.424  1.00 149.84 ? 83  LEU B CD1 1 
ATOM   4140 C CD2 . LEU B 1 83  ? 11.566  -47.507 39.861  1.00 149.49 ? 83  LEU B CD2 1 
ATOM   4141 N N   . THR B 1 84  ? 8.745   -51.391 39.803  1.00 135.32 ? 84  THR B N   1 
ATOM   4142 C CA  . THR B 1 84  ? 8.982   -52.434 38.821  1.00 145.27 ? 84  THR B CA  1 
ATOM   4143 C C   . THR B 1 84  ? 8.976   -51.841 37.418  1.00 136.01 ? 84  THR B C   1 
ATOM   4144 O O   . THR B 1 84  ? 8.105   -51.049 37.021  1.00 125.76 ? 84  THR B O   1 
ATOM   4145 C CB  . THR B 1 84  ? 7.998   -53.592 38.935  1.00 157.90 ? 84  THR B CB  1 
ATOM   4146 O OG1 . THR B 1 84  ? 7.933   -53.841 40.332  1.00 179.00 ? 84  THR B OG1 1 
ATOM   4147 C CG2 . THR B 1 84  ? 8.522   -54.840 38.246  1.00 149.74 ? 84  THR B CG2 1 
ATOM   4148 N N   . LEU B 1 85  ? 9.928   -52.359 36.623  1.00 129.21 ? 85  LEU B N   1 
ATOM   4149 C CA  . LEU B 1 85  ? 10.139  -51.942 35.239  1.00 127.34 ? 85  LEU B CA  1 
ATOM   4150 C C   . LEU B 1 85  ? 10.033  -53.144 34.292  1.00 122.52 ? 85  LEU B C   1 
ATOM   4151 O O   . LEU B 1 85  ? 10.721  -54.137 34.492  1.00 130.97 ? 85  LEU B O   1 
ATOM   4152 C CB  . LEU B 1 85  ? 11.514  -51.293 35.055  1.00 139.06 ? 85  LEU B CB  1 
ATOM   4153 C CG  . LEU B 1 85  ? 11.978  -50.199 36.026  1.00 140.61 ? 85  LEU B CG  1 
ATOM   4154 C CD1 . LEU B 1 85  ? 13.291  -49.648 35.487  1.00 151.14 ? 85  LEU B CD1 1 
ATOM   4155 C CD2 . LEU B 1 85  ? 11.023  -49.050 36.215  1.00 133.01 ? 85  LEU B CD2 1 
ATOM   4156 N N   . LEU B 1 86  ? 9.150   -53.015 33.299  1.00 118.62 ? 86  LEU B N   1 
ATOM   4157 C CA  . LEU B 1 86  ? 8.718   -54.131 32.481  1.00 128.34 ? 86  LEU B CA  1 
ATOM   4158 C C   . LEU B 1 86  ? 8.685   -53.716 31.014  1.00 126.32 ? 86  LEU B C   1 
ATOM   4159 O O   . LEU B 1 86  ? 8.254   -52.604 30.637  1.00 121.90 ? 86  LEU B O   1 
ATOM   4160 C CB  . LEU B 1 86  ? 7.357   -54.598 32.991  1.00 119.70 ? 86  LEU B CB  1 
ATOM   4161 C CG  . LEU B 1 86  ? 7.306   -54.874 34.497  1.00 108.21 ? 86  LEU B CG  1 
ATOM   4162 C CD1 . LEU B 1 86  ? 5.876   -54.732 35.023  1.00 89.45  ? 86  LEU B CD1 1 
ATOM   4163 C CD2 . LEU B 1 86  ? 7.944   -56.253 34.788  1.00 104.49 ? 86  LEU B CD2 1 
ATOM   4164 N N   . THR B 1 87  ? 9.075   -54.691 30.178  1.00 122.82 ? 87  THR B N   1 
ATOM   4165 C CA  . THR B 1 87  ? 9.039   -54.561 28.727  1.00 132.08 ? 87  THR B CA  1 
ATOM   4166 C C   . THR B 1 87  ? 8.249   -55.700 28.094  1.00 140.40 ? 87  THR B C   1 
ATOM   4167 O O   . THR B 1 87  ? 8.519   -56.861 28.367  1.00 141.24 ? 87  THR B O   1 
ATOM   4168 C CB  . THR B 1 87  ? 10.461  -54.481 28.190  1.00 137.55 ? 87  THR B CB  1 
ATOM   4169 O OG1 . THR B 1 87  ? 10.804  -53.177 28.632  1.00 159.62 ? 87  THR B OG1 1 
ATOM   4170 C CG2 . THR B 1 87  ? 10.514  -54.445 26.675  1.00 144.20 ? 87  THR B CG2 1 
ATOM   4171 N N   . PRO B 1 88  ? 7.203   -55.348 27.314  1.00 148.16 ? 88  PRO B N   1 
ATOM   4172 C CA  . PRO B 1 88  ? 6.557   -56.269 26.396  1.00 147.43 ? 88  PRO B CA  1 
ATOM   4173 C C   . PRO B 1 88  ? 7.542   -57.128 25.614  1.00 140.36 ? 88  PRO B C   1 
ATOM   4174 O O   . PRO B 1 88  ? 8.606   -56.665 25.181  1.00 139.96 ? 88  PRO B O   1 
ATOM   4175 C CB  . PRO B 1 88  ? 5.828   -55.293 25.436  1.00 155.86 ? 88  PRO B CB  1 
ATOM   4176 C CG  . PRO B 1 88  ? 5.383   -54.173 26.347  1.00 142.20 ? 88  PRO B CG  1 
ATOM   4177 C CD  . PRO B 1 88  ? 6.592   -54.008 27.259  1.00 148.38 ? 88  PRO B CD  1 
ATOM   4178 N N   . ALA B 1 89  ? 7.130   -58.380 25.414  1.00 137.97 ? 89  ALA B N   1 
ATOM   4179 C CA  . ALA B 1 89  ? 7.901   -59.365 24.659  1.00 160.62 ? 89  ALA B CA  1 
ATOM   4180 C C   . ALA B 1 89  ? 8.019   -58.962 23.187  1.00 168.44 ? 89  ALA B C   1 
ATOM   4181 O O   . ALA B 1 89  ? 8.917   -59.431 22.495  1.00 171.81 ? 89  ALA B O   1 
ATOM   4182 C CB  . ALA B 1 89  ? 7.287   -60.733 24.824  1.00 168.92 ? 89  ALA B CB  1 
ATOM   4183 N N   . SER B 1 90  ? 7.107   -58.095 22.730  1.00 177.41 ? 90  SER B N   1 
ATOM   4184 C CA  . SER B 1 90  ? 7.105   -57.570 21.375  1.00 186.58 ? 90  SER B CA  1 
ATOM   4185 C C   . SER B 1 90  ? 8.127   -56.445 21.236  1.00 183.81 ? 90  SER B C   1 
ATOM   4186 O O   . SER B 1 90  ? 8.203   -55.539 22.073  1.00 182.64 ? 90  SER B O   1 
ATOM   4187 C CB  . SER B 1 90  ? 5.727   -57.095 20.970  1.00 193.80 ? 90  SER B CB  1 
ATOM   4188 O OG  . SER B 1 90  ? 5.757   -56.575 19.649  1.00 198.84 ? 90  SER B OG  1 
ATOM   4189 N N   . ARG B 1 91  ? 8.895   -56.517 20.148  1.00 176.73 ? 91  ARG B N   1 
ATOM   4190 C CA  . ARG B 1 91  ? 9.822   -55.450 19.821  1.00 187.50 ? 91  ARG B CA  1 
ATOM   4191 C C   . ARG B 1 91  ? 9.418   -54.837 18.480  1.00 193.12 ? 91  ARG B C   1 
ATOM   4192 O O   . ARG B 1 91  ? 10.160  -54.042 17.908  1.00 200.78 ? 91  ARG B O   1 
ATOM   4193 C CB  . ARG B 1 91  ? 11.262  -55.966 19.951  1.00 184.96 ? 91  ARG B CB  1 
ATOM   4194 C CG  . ARG B 1 91  ? 12.283  -54.907 20.347  1.00 183.78 ? 91  ARG B CG  1 
ATOM   4195 C CD  . ARG B 1 91  ? 13.620  -55.492 20.759  1.00 204.17 ? 91  ARG B CD  1 
ATOM   4196 N NE  . ARG B 1 91  ? 14.621  -54.422 20.834  1.00 222.98 ? 91  ARG B NE  1 
ATOM   4197 C CZ  . ARG B 1 91  ? 15.790  -54.410 20.204  1.00 229.99 ? 91  ARG B CZ  1 
ATOM   4198 N NH1 . ARG B 1 91  ? 16.120  -55.387 19.378  1.00 232.82 ? 91  ARG B NH1 1 
ATOM   4199 N NH2 . ARG B 1 91  ? 16.630  -53.412 20.392  1.00 229.64 ? 91  ARG B NH2 1 
ATOM   4200 N N   . ALA B 1 92  ? 8.231   -55.208 17.987  1.00 186.64 ? 92  ALA B N   1 
ATOM   4201 C CA  . ALA B 1 92  ? 7.669   -54.597 16.789  1.00 184.94 ? 92  ALA B CA  1 
ATOM   4202 C C   . ALA B 1 92  ? 7.290   -53.151 17.088  1.00 185.06 ? 92  ALA B C   1 
ATOM   4203 O O   . ALA B 1 92  ? 6.912   -52.842 18.215  1.00 180.12 ? 92  ALA B O   1 
ATOM   4204 C CB  . ALA B 1 92  ? 6.464   -55.373 16.312  1.00 182.10 ? 92  ALA B CB  1 
ATOM   4205 N N   . ALA B 1 93  ? 7.399   -52.282 16.074  1.00 193.30 ? 93  ALA B N   1 
ATOM   4206 C CA  . ALA B 1 93  ? 7.175   -50.852 16.256  1.00 192.75 ? 93  ALA B CA  1 
ATOM   4207 C C   . ALA B 1 93  ? 5.687   -50.533 16.162  1.00 164.15 ? 93  ALA B C   1 
ATOM   4208 O O   . ALA B 1 93  ? 5.193   -50.148 15.109  1.00 144.15 ? 93  ALA B O   1 
ATOM   4209 C CB  . ALA B 1 93  ? 7.998   -50.027 15.281  1.00 195.58 ? 93  ALA B CB  1 
ATOM   4210 N N   . ARG B 1 94  ? 4.986   -50.709 17.285  1.00 151.45 ? 94  ARG B N   1 
ATOM   4211 C CA  . ARG B 1 94  ? 3.558   -50.466 17.356  1.00 148.39 ? 94  ARG B CA  1 
ATOM   4212 C C   . ARG B 1 94  ? 3.254   -49.744 18.662  1.00 156.35 ? 94  ARG B C   1 
ATOM   4213 O O   . ARG B 1 94  ? 4.095   -49.702 19.559  1.00 166.82 ? 94  ARG B O   1 
ATOM   4214 C CB  . ARG B 1 94  ? 2.818   -51.806 17.339  1.00 146.15 ? 94  ARG B CB  1 
ATOM   4215 C CG  . ARG B 1 94  ? 3.224   -52.700 16.178  1.00 166.00 ? 94  ARG B CG  1 
ATOM   4216 C CD  . ARG B 1 94  ? 2.534   -54.021 16.323  1.00 179.43 ? 94  ARG B CD  1 
ATOM   4217 N NE  . ARG B 1 94  ? 1.208   -53.744 16.882  1.00 191.19 ? 94  ARG B NE  1 
ATOM   4218 C CZ  . ARG B 1 94  ? 0.272   -54.665 17.009  1.00 224.00 ? 94  ARG B CZ  1 
ATOM   4219 N NH1 . ARG B 1 94  ? 0.484   -55.891 16.559  1.00 245.15 ? 94  ARG B NH1 1 
ATOM   4220 N NH2 . ARG B 1 94  ? -0.881  -54.357 17.567  1.00 236.32 ? 94  ARG B NH2 1 
ATOM   4221 N N   . PRO B 1 95  ? 2.063   -49.116 18.794  1.00 162.19 ? 95  PRO B N   1 
ATOM   4222 C CA  . PRO B 1 95  ? 1.660   -48.498 20.058  1.00 162.48 ? 95  PRO B CA  1 
ATOM   4223 C C   . PRO B 1 95  ? 1.922   -49.440 21.226  1.00 153.22 ? 95  PRO B C   1 
ATOM   4224 O O   . PRO B 1 95  ? 1.732   -50.653 21.102  1.00 148.37 ? 95  PRO B O   1 
ATOM   4225 C CB  . PRO B 1 95  ? 0.166   -48.245 19.818  1.00 170.15 ? 95  PRO B CB  1 
ATOM   4226 C CG  . PRO B 1 95  ? 0.109   -47.924 18.349  1.00 177.73 ? 95  PRO B CG  1 
ATOM   4227 C CD  . PRO B 1 95  ? 1.082   -48.902 17.717  1.00 172.80 ? 95  PRO B CD  1 
ATOM   4228 N N   . LEU B 1 96  ? 2.359   -48.854 22.349  1.00 140.65 ? 96  LEU B N   1 
ATOM   4229 C CA  . LEU B 1 96  ? 2.858   -49.615 23.476  1.00 146.49 ? 96  LEU B CA  1 
ATOM   4230 C C   . LEU B 1 96  ? 1.733   -50.442 24.091  1.00 182.96 ? 96  LEU B C   1 
ATOM   4231 O O   . LEU B 1 96  ? 1.975   -51.579 24.504  1.00 206.33 ? 96  LEU B O   1 
ATOM   4232 C CB  . LEU B 1 96  ? 3.532   -48.710 24.505  1.00 128.23 ? 96  LEU B CB  1 
ATOM   4233 C CG  . LEU B 1 96  ? 3.884   -49.400 25.830  1.00 140.81 ? 96  LEU B CG  1 
ATOM   4234 C CD1 . LEU B 1 96  ? 4.859   -50.573 25.661  1.00 160.93 ? 96  LEU B CD1 1 
ATOM   4235 C CD2 . LEU B 1 96  ? 4.430   -48.455 26.856  1.00 153.84 ? 96  LEU B CD2 1 
ATOM   4236 N N   . ASP B 1 97  ? 0.552   -49.820 24.211  1.00 197.91 ? 97  ASP B N   1 
ATOM   4237 C CA  . ASP B 1 97  ? -0.590  -50.428 24.867  1.00 177.10 ? 97  ASP B CA  1 
ATOM   4238 C C   . ASP B 1 97  ? -0.960  -51.743 24.174  1.00 166.52 ? 97  ASP B C   1 
ATOM   4239 O O   . ASP B 1 97  ? -1.195  -52.761 24.840  1.00 153.44 ? 97  ASP B O   1 
ATOM   4240 C CB  . ASP B 1 97  ? -1.722  -49.424 25.033  1.00 168.85 ? 97  ASP B CB  1 
ATOM   4241 C CG  . ASP B 1 97  ? -2.078  -48.644 23.775  1.00 182.36 ? 97  ASP B CG  1 
ATOM   4242 O OD1 . ASP B 1 97  ? -1.500  -48.943 22.712  1.00 180.68 ? 97  ASP B OD1 1 
ATOM   4243 O OD2 . ASP B 1 97  ? -2.917  -47.732 23.868  1.00 188.61 ? 97  ASP B OD2 1 
ATOM   4244 N N   . SER B 1 98  ? -0.992  -51.681 22.840  1.00 159.25 ? 98  SER B N   1 
ATOM   4245 C CA  . SER B 1 98  ? -1.325  -52.833 22.010  1.00 144.93 ? 98  SER B CA  1 
ATOM   4246 C C   . SER B 1 98  ? -0.353  -53.981 22.282  1.00 133.25 ? 98  SER B C   1 
ATOM   4247 O O   . SER B 1 98  ? -0.758  -55.139 22.456  1.00 146.11 ? 98  SER B O   1 
ATOM   4248 C CB  . SER B 1 98  ? -1.322  -52.473 20.553  1.00 159.99 ? 98  SER B CB  1 
ATOM   4249 O OG  . SER B 1 98  ? -2.360  -51.547 20.254  1.00 178.56 ? 98  SER B OG  1 
ATOM   4250 N N   . LEU B 1 99  ? 0.928   -53.614 22.314  1.00 126.87 ? 99  LEU B N   1 
ATOM   4251 C CA  . LEU B 1 99  ? 2.017   -54.556 22.558  1.00 133.49 ? 99  LEU B CA  1 
ATOM   4252 C C   . LEU B 1 99  ? 1.818   -55.248 23.904  1.00 150.95 ? 99  LEU B C   1 
ATOM   4253 O O   . LEU B 1 99  ? 1.945   -56.478 24.017  1.00 162.33 ? 99  LEU B O   1 
ATOM   4254 C CB  . LEU B 1 99  ? 3.372   -53.854 22.457  1.00 123.63 ? 99  LEU B CB  1 
ATOM   4255 C CG  . LEU B 1 99  ? 3.658   -53.213 21.095  1.00 133.35 ? 99  LEU B CG  1 
ATOM   4256 C CD1 . LEU B 1 99  ? 5.023   -52.542 21.042  1.00 152.96 ? 99  LEU B CD1 1 
ATOM   4257 C CD2 . LEU B 1 99  ? 3.528   -54.240 19.992  1.00 134.18 ? 99  LEU B CD2 1 
ATOM   4258 N N   . VAL B 1 100 ? 1.503   -54.425 24.905  1.00 150.75 ? 100 VAL B N   1 
ATOM   4259 C CA  . VAL B 1 100 ? 1.268   -54.878 26.274  1.00 166.85 ? 100 VAL B CA  1 
ATOM   4260 C C   . VAL B 1 100 ? 0.146   -55.918 26.291  1.00 183.52 ? 100 VAL B C   1 
ATOM   4261 O O   . VAL B 1 100 ? 0.261   -56.987 26.916  1.00 196.61 ? 100 VAL B O   1 
ATOM   4262 C CB  . VAL B 1 100 ? 0.849   -53.687 27.167  1.00 150.86 ? 100 VAL B CB  1 
ATOM   4263 C CG1 . VAL B 1 100 ? 0.225   -54.137 28.487  1.00 138.63 ? 100 VAL B CG1 1 
ATOM   4264 C CG2 . VAL B 1 100 ? 1.987   -52.710 27.431  1.00 174.08 ? 100 VAL B CG2 1 
ATOM   4265 N N   . LEU B 1 101 ? -0.933  -55.560 25.595  1.00 184.74 ? 101 LEU B N   1 
ATOM   4266 C CA  . LEU B 1 101 ? -2.124  -56.398 25.498  1.00 180.27 ? 101 LEU B CA  1 
ATOM   4267 C C   . LEU B 1 101 ? -1.762  -57.758 24.902  1.00 178.45 ? 101 LEU B C   1 
ATOM   4268 O O   . LEU B 1 101 ? -2.185  -58.805 25.418  1.00 192.38 ? 101 LEU B O   1 
ATOM   4269 C CB  . LEU B 1 101 ? -3.194  -55.661 24.698  1.00 169.02 ? 101 LEU B CB  1 
ATOM   4270 C CG  . LEU B 1 101 ? -4.642  -56.059 24.979  1.00 156.56 ? 101 LEU B CG  1 
ATOM   4271 C CD1 . LEU B 1 101 ? -4.979  -56.141 26.463  1.00 144.50 ? 101 LEU B CD1 1 
ATOM   4272 C CD2 . LEU B 1 101 ? -5.508  -55.025 24.285  1.00 147.96 ? 101 LEU B CD2 1 
ATOM   4273 N N   . GLU B 1 102 ? -0.975  -57.699 23.825  1.00 180.77 ? 102 GLU B N   1 
ATOM   4274 C CA  . GLU B 1 102 ? -0.503  -58.896 23.135  1.00 173.83 ? 102 GLU B CA  1 
ATOM   4275 C C   . GLU B 1 102 ? 0.232   -59.839 24.088  1.00 183.24 ? 102 GLU B C   1 
ATOM   4276 O O   . GLU B 1 102 ? -0.026  -61.041 24.031  1.00 197.23 ? 102 GLU B O   1 
ATOM   4277 C CB  . GLU B 1 102 ? 0.289   -58.690 21.850  1.00 169.00 ? 102 GLU B CB  1 
ATOM   4278 C CG  . GLU B 1 102 ? -0.612  -58.179 20.734  1.00 194.17 ? 102 GLU B CG  1 
ATOM   4279 C CD  . GLU B 1 102 ? 0.222   -57.709 19.571  1.00 217.51 ? 102 GLU B CD  1 
ATOM   4280 O OE1 . GLU B 1 102 ? 1.464   -57.831 19.627  1.00 227.51 ? 102 GLU B OE1 1 
ATOM   4281 O OE2 . GLU B 1 102 ? -0.390  -57.200 18.611  1.00 223.26 ? 102 GLU B OE2 1 
ATOM   4282 N N   . ASP B 1 103 ? 1.018   -59.316 25.038  1.00 187.56 ? 103 ASP B N   1 
ATOM   4283 C CA  . ASP B 1 103 ? 1.719   -60.161 26.004  1.00 219.83 ? 103 ASP B CA  1 
ATOM   4284 C C   . ASP B 1 103 ? 0.787   -60.598 27.145  1.00 202.44 ? 103 ASP B C   1 
ATOM   4285 O O   . ASP B 1 103 ? 0.655   -59.911 28.158  1.00 192.67 ? 103 ASP B O   1 
ATOM   4286 C CB  . ASP B 1 103 ? 3.031   -59.515 26.435  1.00 237.45 ? 103 ASP B CB  1 
ATOM   4287 C CG  . ASP B 1 103 ? 3.967   -60.319 27.338  1.00 226.28 ? 103 ASP B CG  1 
ATOM   4288 O OD1 . ASP B 1 103 ? 3.615   -61.474 27.714  1.00 217.54 ? 103 ASP B OD1 1 
ATOM   4289 O OD2 . ASP B 1 103 ? 5.051   -59.768 27.676  1.00 184.67 ? 103 ASP B OD2 1 
ATOM   4290 N N   . GLU B 1 104 ? 0.183   -61.785 26.995  1.00 177.53 ? 104 GLU B N   1 
ATOM   4291 C CA  . GLU B 1 104 ? -0.841  -62.273 27.900  1.00 173.91 ? 104 GLU B CA  1 
ATOM   4292 C C   . GLU B 1 104 ? -0.294  -62.331 29.326  1.00 164.85 ? 104 GLU B C   1 
ATOM   4293 O O   . GLU B 1 104 ? -0.979  -61.944 30.282  1.00 174.78 ? 104 GLU B O   1 
ATOM   4294 C CB  . GLU B 1 104 ? -1.239  -63.672 27.428  1.00 189.57 ? 104 GLU B CB  1 
ATOM   4295 C CG  . GLU B 1 104 ? -2.041  -63.662 26.129  1.00 186.22 ? 104 GLU B CG  1 
ATOM   4296 C CD  . GLU B 1 104 ? -3.445  -63.111 26.316  1.00 204.21 ? 104 GLU B CD  1 
ATOM   4297 O OE1 . GLU B 1 104 ? -3.607  -61.882 26.545  1.00 234.56 ? 104 GLU B OE1 1 
ATOM   4298 O OE2 . GLU B 1 104 ? -4.383  -63.937 26.220  1.00 200.03 ? 104 GLU B OE2 1 
ATOM   4299 N N   . ALA B 1 105 ? 0.913   -62.899 29.427  1.00 150.01 ? 105 ALA B N   1 
ATOM   4300 C CA  . ALA B 1 105 ? 1.560   -63.154 30.703  1.00 153.74 ? 105 ALA B CA  1 
ATOM   4301 C C   . ALA B 1 105 ? 1.715   -61.853 31.488  1.00 154.92 ? 105 ALA B C   1 
ATOM   4302 O O   . ALA B 1 105 ? 1.404   -61.776 32.691  1.00 140.51 ? 105 ALA B O   1 
ATOM   4303 C CB  . ALA B 1 105 ? 2.907   -63.804 30.456  1.00 157.17 ? 105 ALA B CB  1 
ATOM   4304 N N   . LEU B 1 106 ? 2.208   -60.842 30.759  1.00 177.54 ? 106 LEU B N   1 
ATOM   4305 C CA  . LEU B 1 106 ? 2.453   -59.515 31.326  1.00 195.49 ? 106 LEU B CA  1 
ATOM   4306 C C   . LEU B 1 106 ? 1.152   -58.943 31.885  1.00 186.99 ? 106 LEU B C   1 
ATOM   4307 O O   . LEU B 1 106 ? 1.128   -58.414 33.006  1.00 170.20 ? 106 LEU B O   1 
ATOM   4308 C CB  . LEU B 1 106 ? 3.119   -58.588 30.299  1.00 214.93 ? 106 LEU B CB  1 
ATOM   4309 C CG  . LEU B 1 106 ? 3.173   -57.078 30.603  1.00 203.79 ? 106 LEU B CG  1 
ATOM   4310 C CD1 . LEU B 1 106 ? 3.834   -56.706 31.927  1.00 224.03 ? 106 LEU B CD1 1 
ATOM   4311 C CD2 . LEU B 1 106 ? 3.857   -56.310 29.465  1.00 195.89 ? 106 LEU B CD2 1 
ATOM   4312 N N   . VAL B 1 107 ? 0.095   -59.074 31.075  1.00 173.86 ? 107 VAL B N   1 
ATOM   4313 C CA  . VAL B 1 107 ? -1.235  -58.582 31.426  1.00 170.45 ? 107 VAL B CA  1 
ATOM   4314 C C   . VAL B 1 107 ? -1.701  -59.229 32.731  1.00 168.76 ? 107 VAL B C   1 
ATOM   4315 O O   . VAL B 1 107 ? -2.204  -58.546 33.639  1.00 171.49 ? 107 VAL B O   1 
ATOM   4316 C CB  . VAL B 1 107 ? -2.340  -58.677 30.347  1.00 162.69 ? 107 VAL B CB  1 
ATOM   4317 C CG1 . VAL B 1 107 ? -3.625  -57.968 30.772  1.00 157.44 ? 107 VAL B CG1 1 
ATOM   4318 C CG2 . VAL B 1 107 ? -1.891  -58.128 28.995  1.00 172.22 ? 107 VAL B CG2 1 
ATOM   4319 N N   . GLU B 1 108 ? -1.519  -60.550 32.782  1.00 176.08 ? 108 GLU B N   1 
ATOM   4320 C CA  . GLU B 1 108 ? -1.904  -61.359 33.933  1.00 179.63 ? 108 GLU B CA  1 
ATOM   4321 C C   . GLU B 1 108 ? -1.204  -60.848 35.194  1.00 154.40 ? 108 GLU B C   1 
ATOM   4322 O O   . GLU B 1 108 ? -1.831  -60.665 36.256  1.00 142.60 ? 108 GLU B O   1 
ATOM   4323 C CB  . GLU B 1 108 ? -1.455  -62.796 33.664  1.00 197.89 ? 108 GLU B CB  1 
ATOM   4324 C CG  . GLU B 1 108 ? -2.506  -63.656 32.962  1.00 215.25 ? 108 GLU B CG  1 
ATOM   4325 C CD  . GLU B 1 108 ? -3.715  -63.946 33.845  1.00 226.23 ? 108 GLU B CD  1 
ATOM   4326 O OE1 . GLU B 1 108 ? -3.520  -64.170 35.061  1.00 226.05 ? 108 GLU B OE1 1 
ATOM   4327 O OE2 . GLU B 1 108 ? -4.852  -63.974 33.326  1.00 241.49 ? 108 GLU B OE2 1 
ATOM   4328 N N   . THR B 1 109 ? 0.106   -60.629 35.028  1.00 143.63 ? 109 THR B N   1 
ATOM   4329 C CA  . THR B 1 109 ? 0.955   -60.162 36.119  1.00 143.21 ? 109 THR B CA  1 
ATOM   4330 C C   . THR B 1 109 ? 0.449   -58.824 36.646  1.00 140.46 ? 109 THR B C   1 
ATOM   4331 O O   . THR B 1 109 ? 0.345   -58.623 37.868  1.00 121.98 ? 109 THR B O   1 
ATOM   4332 C CB  . THR B 1 109 ? 2.447   -60.167 35.828  1.00 137.70 ? 109 THR B CB  1 
ATOM   4333 O OG1 . THR B 1 109 ? 2.739   -61.374 35.135  1.00 153.24 ? 109 THR B OG1 1 
ATOM   4334 C CG2 . THR B 1 109 ? 3.212   -60.223 37.137  1.00 138.95 ? 109 THR B CG2 1 
ATOM   4335 N N   . LEU B 1 110 ? 0.137   -57.941 35.698  1.00 155.78 ? 110 LEU B N   1 
ATOM   4336 C CA  . LEU B 1 110 ? -0.362  -56.599 35.997  1.00 178.43 ? 110 LEU B CA  1 
ATOM   4337 C C   . LEU B 1 110 ? -1.639  -56.693 36.824  1.00 198.00 ? 110 LEU B C   1 
ATOM   4338 O O   . LEU B 1 110 ? -1.797  -55.989 37.836  1.00 220.14 ? 110 LEU B O   1 
ATOM   4339 C CB  . LEU B 1 110 ? -0.586  -55.733 34.750  1.00 158.76 ? 110 LEU B CB  1 
ATOM   4340 C CG  . LEU B 1 110 ? 0.640   -55.312 33.932  1.00 131.95 ? 110 LEU B CG  1 
ATOM   4341 C CD1 . LEU B 1 110 ? 0.264   -54.711 32.576  1.00 135.80 ? 110 LEU B CD1 1 
ATOM   4342 C CD2 . LEU B 1 110 ? 1.483   -54.330 34.697  1.00 140.65 ? 110 LEU B CD2 1 
ATOM   4343 N N   . ARG B 1 111 ? -2.531  -57.575 36.361  1.00 186.09 ? 111 ARG B N   1 
ATOM   4344 C CA  . ARG B 1 111 ? -3.821  -57.806 37.004  1.00 191.36 ? 111 ARG B CA  1 
ATOM   4345 C C   . ARG B 1 111 ? -3.609  -58.240 38.453  1.00 181.61 ? 111 ARG B C   1 
ATOM   4346 O O   . ARG B 1 111 ? -4.266  -57.728 39.375  1.00 185.70 ? 111 ARG B O   1 
ATOM   4347 C CB  . ARG B 1 111 ? -4.612  -58.876 36.239  1.00 218.80 ? 111 ARG B CB  1 
ATOM   4348 C CG  . ARG B 1 111 ? -5.951  -59.236 36.880  1.00 228.61 ? 111 ARG B CG  1 
ATOM   4349 C CD  . ARG B 1 111 ? -6.876  -60.238 36.172  1.00 192.42 ? 111 ARG B CD  1 
ATOM   4350 N NE  . ARG B 1 111 ? -6.279  -61.580 36.115  1.00 212.75 ? 111 ARG B NE  1 
ATOM   4351 C CZ  . ARG B 1 111 ? -5.935  -62.315 37.176  1.00 221.72 ? 111 ARG B CZ  1 
ATOM   4352 N NH1 . ARG B 1 111 ? -6.297  -61.952 38.398  1.00 206.18 ? 111 ARG B NH1 1 
ATOM   4353 N NH2 . ARG B 1 111 ? -5.220  -63.408 37.003  1.00 231.52 ? 111 ARG B NH2 1 
ATOM   4354 N N   . ARG B 1 112 ? -2.682  -59.186 38.613  1.00 157.79 ? 112 ARG B N   1 
ATOM   4355 C CA  . ARG B 1 112 ? -2.341  -59.742 39.919  1.00 163.35 ? 112 ARG B CA  1 
ATOM   4356 C C   . ARG B 1 112 ? -1.875  -58.634 40.859  1.00 158.27 ? 112 ARG B C   1 
ATOM   4357 O O   . ARG B 1 112 ? -2.314  -58.555 42.018  1.00 166.51 ? 112 ARG B O   1 
ATOM   4358 C CB  . ARG B 1 112 ? -1.284  -60.841 39.800  1.00 169.49 ? 112 ARG B CB  1 
ATOM   4359 C CG  . ARG B 1 112 ? -1.805  -61.922 38.869  1.00 184.85 ? 112 ARG B CG  1 
ATOM   4360 C CD  . ARG B 1 112 ? -0.787  -63.028 38.706  1.00 198.06 ? 112 ARG B CD  1 
ATOM   4361 N NE  . ARG B 1 112 ? -0.642  -63.662 40.023  1.00 207.82 ? 112 ARG B NE  1 
ATOM   4362 C CZ  . ARG B 1 112 ? -0.310  -64.925 40.261  1.00 222.59 ? 112 ARG B CZ  1 
ATOM   4363 N NH1 . ARG B 1 112 ? -0.044  -65.742 39.257  1.00 244.95 ? 112 ARG B NH1 1 
ATOM   4364 N NH2 . ARG B 1 112 ? -0.265  -65.361 41.507  1.00 206.27 ? 112 ARG B NH2 1 
ATOM   4365 N N   . ALA B 1 113 ? -0.991  -57.794 40.317  1.00 149.45 ? 113 ALA B N   1 
ATOM   4366 C CA  . ALA B 1 113 ? -0.418  -56.674 41.055  1.00 170.68 ? 113 ALA B CA  1 
ATOM   4367 C C   . ALA B 1 113 ? -1.526  -55.744 41.547  1.00 198.27 ? 113 ALA B C   1 
ATOM   4368 O O   . ALA B 1 113 ? -1.542  -55.328 42.720  1.00 218.89 ? 113 ALA B O   1 
ATOM   4369 C CB  . ALA B 1 113 ? 0.570   -55.935 40.200  1.00 178.00 ? 113 ALA B CB  1 
ATOM   4370 N N   . VAL B 1 114 ? -2.442  -55.449 40.620  1.00 214.46 ? 114 VAL B N   1 
ATOM   4371 C CA  . VAL B 1 114 ? -3.572  -54.563 40.889  1.00 204.28 ? 114 VAL B CA  1 
ATOM   4372 C C   . VAL B 1 114 ? -4.411  -55.124 42.035  1.00 196.31 ? 114 VAL B C   1 
ATOM   4373 O O   . VAL B 1 114 ? -4.791  -54.390 42.965  1.00 188.02 ? 114 VAL B O   1 
ATOM   4374 C CB  . VAL B 1 114 ? -4.450  -54.193 39.676  1.00 201.24 ? 114 VAL B CB  1 
ATOM   4375 C CG1 . VAL B 1 114 ? -5.589  -53.263 40.062  1.00 191.67 ? 114 VAL B CG1 1 
ATOM   4376 C CG2 . VAL B 1 114 ? -3.633  -53.566 38.557  1.00 207.91 ? 114 VAL B CG2 1 
ATOM   4377 N N   . ALA B 1 115 ? -4.673  -56.430 41.942  1.00 179.15 ? 115 ALA B N   1 
ATOM   4378 C CA  . ALA B 1 115 ? -5.468  -57.143 42.935  1.00 185.54 ? 115 ALA B CA  1 
ATOM   4379 C C   . ALA B 1 115 ? -4.821  -57.024 44.310  1.00 194.26 ? 115 ALA B C   1 
ATOM   4380 O O   . ALA B 1 115 ? -5.491  -56.736 45.312  1.00 233.61 ? 115 ALA B O   1 
ATOM   4381 C CB  . ALA B 1 115 ? -5.661  -58.584 42.522  1.00 198.03 ? 115 ALA B CB  1 
ATOM   4382 N N   . GLU B 1 116 ? -3.505  -57.235 44.321  1.00 186.90 ? 116 GLU B N   1 
ATOM   4383 C CA  . GLU B 1 116 ? -2.696  -57.182 45.533  1.00 196.45 ? 116 GLU B CA  1 
ATOM   4384 C C   . GLU B 1 116 ? -2.907  -55.846 46.249  1.00 186.80 ? 116 GLU B C   1 
ATOM   4385 O O   . GLU B 1 116 ? -3.016  -55.841 47.468  1.00 167.38 ? 116 GLU B O   1 
ATOM   4386 C CB  . GLU B 1 116 ? -1.283  -57.580 45.100  1.00 238.12 ? 116 GLU B CB  1 
ATOM   4387 C CG  . GLU B 1 116 ? -0.716  -58.777 45.861  1.00 266.20 ? 116 GLU B CG  1 
ATOM   4388 C CD  . GLU B 1 116 ? -0.186  -58.449 47.243  1.00 307.33 ? 116 GLU B CD  1 
ATOM   4389 O OE1 . GLU B 1 116 ? 0.727   -57.597 47.333  1.00 330.61 ? 116 GLU B OE1 1 
ATOM   4390 O OE2 . GLU B 1 116 ? -0.681  -59.048 48.221  1.00 322.92 ? 116 GLU B OE2 1 
ATOM   4391 N N   . ARG B 1 117 ? -3.246  -54.791 45.511  1.00 190.18 ? 117 ARG B N   1 
ATOM   4392 C CA  . ARG B 1 117 ? -3.430  -53.510 46.169  1.00 197.45 ? 117 ARG B CA  1 
ATOM   4393 C C   . ARG B 1 117 ? -4.894  -53.068 46.196  1.00 212.31 ? 117 ARG B C   1 
ATOM   4394 O O   . ARG B 1 117 ? -5.685  -53.387 45.303  1.00 194.24 ? 117 ARG B O   1 
ATOM   4395 C CB  . ARG B 1 117 ? -2.466  -52.457 45.618  1.00 198.99 ? 117 ARG B CB  1 
ATOM   4396 C CG  . ARG B 1 117 ? -1.036  -52.612 46.120  1.00 197.49 ? 117 ARG B CG  1 
ATOM   4397 C CD  . ARG B 1 117 ? -0.884  -52.490 47.621  1.00 213.37 ? 117 ARG B CD  1 
ATOM   4398 N NE  . ARG B 1 117 ? 0.519   -52.786 47.934  1.00 255.77 ? 117 ARG B NE  1 
ATOM   4399 C CZ  . ARG B 1 117 ? 1.428   -51.898 48.316  1.00 281.91 ? 117 ARG B CZ  1 
ATOM   4400 N NH1 . ARG B 1 117 ? 1.091   -50.642 48.464  1.00 293.16 ? 117 ARG B NH1 1 
ATOM   4401 N NH2 . ARG B 1 117 ? 2.676   -52.267 48.538  1.00 287.53 ? 117 ARG B NH2 1 
ATOM   4402 N N   . PRO B 1 118 ? -5.283  -52.325 47.263  1.00 226.35 ? 118 PRO B N   1 
ATOM   4403 C CA  . PRO B 1 118 ? -6.549  -51.588 47.295  1.00 216.47 ? 118 PRO B CA  1 
ATOM   4404 C C   . PRO B 1 118 ? -7.022  -50.929 46.000  1.00 211.81 ? 118 PRO B C   1 
ATOM   4405 O O   . PRO B 1 118 ? -8.183  -51.083 45.638  1.00 227.64 ? 118 PRO B O   1 
ATOM   4406 C CB  . PRO B 1 118 ? -6.272  -50.559 48.419  1.00 211.94 ? 118 PRO B CB  1 
ATOM   4407 C CG  . PRO B 1 118 ? -5.376  -51.292 49.394  1.00 207.36 ? 118 PRO B CG  1 
ATOM   4408 C CD  . PRO B 1 118 ? -4.534  -52.208 48.528  1.00 216.96 ? 118 PRO B CD  1 
ATOM   4409 N N   . ALA B 1 119 ? -6.109  -50.228 45.315  1.00 196.70 ? 119 ALA B N   1 
ATOM   4410 C CA  . ALA B 1 119 ? -6.449  -49.288 44.266  1.00 190.60 ? 119 ALA B CA  1 
ATOM   4411 C C   . ALA B 1 119 ? -5.597  -49.494 43.012  1.00 191.34 ? 119 ALA B C   1 
ATOM   4412 O O   . ALA B 1 119 ? -4.386  -49.765 43.081  1.00 196.59 ? 119 ALA B O   1 
ATOM   4413 C CB  . ALA B 1 119 ? -6.295  -47.873 44.781  1.00 174.89 ? 119 ALA B CB  1 
ATOM   4414 N N   . GLY B 1 120 ? -6.266  -49.323 41.867  1.00 194.77 ? 120 GLY B N   1 
ATOM   4415 C CA  . GLY B 1 120 ? -5.661  -49.491 40.554  1.00 184.66 ? 120 GLY B CA  1 
ATOM   4416 C C   . GLY B 1 120 ? -5.881  -48.267 39.676  1.00 170.88 ? 120 GLY B C   1 
ATOM   4417 O O   . GLY B 1 120 ? -6.985  -47.782 39.537  1.00 195.88 ? 120 GLY B O   1 
ATOM   4418 N N   . THR B 1 121 ? -4.780  -47.751 39.140  1.00 159.40 ? 121 THR B N   1 
ATOM   4419 C CA  . THR B 1 121 ? -4.758  -46.633 38.210  1.00 158.32 ? 121 THR B CA  1 
ATOM   4420 C C   . THR B 1 121 ? -3.836  -47.002 37.063  1.00 159.36 ? 121 THR B C   1 
ATOM   4421 O O   . THR B 1 121 ? -2.667  -47.339 37.284  1.00 191.27 ? 121 THR B O   1 
ATOM   4422 C CB  . THR B 1 121 ? -4.229  -45.352 38.864  1.00 155.57 ? 121 THR B CB  1 
ATOM   4423 O OG1 . THR B 1 121 ? -4.852  -45.222 40.138  1.00 190.22 ? 121 THR B OG1 1 
ATOM   4424 C CG2 . THR B 1 121 ? -4.448  -44.108 38.008  1.00 153.50 ? 121 THR B CG2 1 
ATOM   4425 N N   . ILE B 1 122 ? -4.329  -46.764 35.831  1.00 152.79 ? 122 ILE B N   1 
ATOM   4426 C CA  . ILE B 1 122 ? -3.505  -46.786 34.626  1.00 155.34 ? 122 ILE B CA  1 
ATOM   4427 C C   . ILE B 1 122 ? -3.253  -45.355 34.148  1.00 164.16 ? 122 ILE B C   1 
ATOM   4428 O O   . ILE B 1 122 ? -4.186  -44.591 33.886  1.00 207.05 ? 122 ILE B O   1 
ATOM   4429 C CB  . ILE B 1 122 ? -4.051  -47.728 33.524  1.00 144.45 ? 122 ILE B CB  1 
ATOM   4430 C CG1 . ILE B 1 122 ? -3.819  -49.210 33.861  1.00 137.45 ? 122 ILE B CG1 1 
ATOM   4431 C CG2 . ILE B 1 122 ? -3.439  -47.416 32.156  1.00 142.01 ? 122 ILE B CG2 1 
ATOM   4432 C CD1 . ILE B 1 122 ? -4.323  -50.172 32.795  1.00 152.07 ? 122 ILE B CD1 1 
ATOM   4433 N N   . VAL B 1 123 ? -1.947  -45.034 33.992  1.00 156.80 ? 123 VAL B N   1 
ATOM   4434 C CA  . VAL B 1 123 ? -1.512  -43.686 33.656  1.00 143.51 ? 123 VAL B CA  1 
ATOM   4435 C C   . VAL B 1 123 ? -1.085  -43.627 32.185  1.00 155.53 ? 123 VAL B C   1 
ATOM   4436 O O   . VAL B 1 123 ? -0.081  -44.252 31.819  1.00 185.44 ? 123 VAL B O   1 
ATOM   4437 C CB  . VAL B 1 123 ? -0.381  -43.249 34.606  1.00 134.91 ? 123 VAL B CB  1 
ATOM   4438 C CG1 . VAL B 1 123 ? 0.081   -41.838 34.296  1.00 127.53 ? 123 VAL B CG1 1 
ATOM   4439 C CG2 . VAL B 1 123 ? -0.774  -43.358 36.072  1.00 123.50 ? 123 VAL B CG2 1 
ATOM   4440 N N   . ASP B 1 124 ? -1.882  -42.904 31.375  1.00 132.07 ? 124 ASP B N   1 
ATOM   4441 C CA  . ASP B 1 124 ? -1.807  -43.015 29.926  1.00 145.75 ? 124 ASP B CA  1 
ATOM   4442 C C   . ASP B 1 124 ? -1.796  -41.661 29.226  1.00 146.06 ? 124 ASP B C   1 
ATOM   4443 O O   . ASP B 1 124 ? -2.191  -40.607 29.743  1.00 166.06 ? 124 ASP B O   1 
ATOM   4444 C CB  . ASP B 1 124 ? -2.946  -43.824 29.312  1.00 179.63 ? 124 ASP B CB  1 
ATOM   4445 C CG  . ASP B 1 124 ? -4.363  -43.480 29.761  1.00 206.87 ? 124 ASP B CG  1 
ATOM   4446 O OD1 . ASP B 1 124 ? -4.488  -42.789 30.790  1.00 207.36 ? 124 ASP B OD1 1 
ATOM   4447 O OD2 . ASP B 1 124 ? -5.336  -43.904 29.075  1.00 211.80 ? 124 ASP B OD2 1 
ATOM   4448 N N   . PHE B 1 125 ? -1.440  -41.702 27.942  1.00 149.45 ? 125 PHE B N   1 
ATOM   4449 C CA  . PHE B 1 125 ? -1.409  -40.438 27.224  1.00 167.13 ? 125 PHE B CA  1 
ATOM   4450 C C   . PHE B 1 125 ? -2.814  -40.057 26.750  1.00 170.43 ? 125 PHE B C   1 
ATOM   4451 O O   . PHE B 1 125 ? -3.418  -39.097 27.236  1.00 138.75 ? 125 PHE B O   1 
ATOM   4452 C CB  . PHE B 1 125 ? -0.324  -40.408 26.146  1.00 172.37 ? 125 PHE B CB  1 
ATOM   4453 C CG  . PHE B 1 125 ? -0.135  -38.996 25.620  1.00 148.99 ? 125 PHE B CG  1 
ATOM   4454 C CD1 . PHE B 1 125 ? 0.592   -38.053 26.346  1.00 155.83 ? 125 PHE B CD1 1 
ATOM   4455 C CD2 . PHE B 1 125 ? -0.702  -38.621 24.412  1.00 135.45 ? 125 PHE B CD2 1 
ATOM   4456 C CE1 . PHE B 1 125 ? 0.778   -36.767 25.862  1.00 155.27 ? 125 PHE B CE1 1 
ATOM   4457 C CE2 . PHE B 1 125 ? -0.506  -37.339 23.928  1.00 148.07 ? 125 PHE B CE2 1 
ATOM   4458 C CZ  . PHE B 1 125 ? 0.221   -36.414 24.654  1.00 151.28 ? 125 PHE B CZ  1 
ATOM   4459 N N   . SER B 1 126 ? -3.306  -40.812 25.766  1.00 189.98 ? 126 SER B N   1 
ATOM   4460 C CA  . SER B 1 126 ? -4.651  -40.664 25.247  1.00 177.49 ? 126 SER B CA  1 
ATOM   4461 C C   . SER B 1 126 ? -5.348  -41.998 25.432  1.00 171.65 ? 126 SER B C   1 
ATOM   4462 O O   . SER B 1 126 ? -4.713  -43.053 25.315  1.00 150.25 ? 126 SER B O   1 
ATOM   4463 C CB  . SER B 1 126 ? -4.661  -40.256 23.797  1.00 194.37 ? 126 SER B CB  1 
ATOM   4464 O OG  . SER B 1 126 ? -3.770  -41.057 23.034  1.00 252.47 ? 126 SER B OG  1 
ATOM   4465 N N   . ALA B 1 127 ? -6.640  -41.896 25.767  1.00 174.62 ? 127 ALA B N   1 
ATOM   4466 C CA  . ALA B 1 127 ? -7.530  -43.031 25.924  1.00 166.75 ? 127 ALA B CA  1 
ATOM   4467 C C   . ALA B 1 127 ? -7.639  -43.732 24.574  1.00 175.79 ? 127 ALA B C   1 
ATOM   4468 O O   . ALA B 1 127 ? -7.699  -43.063 23.541  1.00 179.67 ? 127 ALA B O   1 
ATOM   4469 C CB  . ALA B 1 127 ? -8.867  -42.521 26.379  1.00 162.42 ? 127 ALA B CB  1 
ATOM   4470 N N   . SER B 1 128 ? -7.609  -45.072 24.594  1.00 169.15 ? 128 SER B N   1 
ATOM   4471 C CA  . SER B 1 128 ? -7.533  -45.860 23.371  1.00 164.13 ? 128 SER B CA  1 
ATOM   4472 C C   . SER B 1 128 ? -8.211  -47.204 23.589  1.00 163.05 ? 128 SER B C   1 
ATOM   4473 O O   . SER B 1 128 ? -8.452  -47.588 24.732  1.00 160.18 ? 128 SER B O   1 
ATOM   4474 C CB  . SER B 1 128 ? -6.107  -46.059 22.898  1.00 167.19 ? 128 SER B CB  1 
ATOM   4475 O OG  . SER B 1 128 ? -5.500  -47.219 23.455  1.00 169.64 ? 128 SER B OG  1 
ATOM   4476 N N   . PRO B 1 129 ? -8.522  -47.959 22.511  1.00 169.34 ? 129 PRO B N   1 
ATOM   4477 C CA  . PRO B 1 129 ? -9.182  -49.251 22.689  1.00 176.71 ? 129 PRO B CA  1 
ATOM   4478 C C   . PRO B 1 129 ? -8.332  -50.088 23.650  1.00 165.17 ? 129 PRO B C   1 
ATOM   4479 O O   . PRO B 1 129 ? -8.859  -50.699 24.585  1.00 157.98 ? 129 PRO B O   1 
ATOM   4480 C CB  . PRO B 1 129 ? -9.179  -49.853 21.276  1.00 187.84 ? 129 PRO B CB  1 
ATOM   4481 C CG  . PRO B 1 129 ? -9.043  -48.675 20.329  1.00 172.28 ? 129 PRO B CG  1 
ATOM   4482 C CD  . PRO B 1 129 ? -8.344  -47.576 21.099  1.00 162.35 ? 129 PRO B CD  1 
ATOM   4483 N N   . ALA B 1 130 ? -7.041  -50.167 23.306  1.00 156.28 ? 130 ALA B N   1 
ATOM   4484 C CA  . ALA B 1 130 ? -6.111  -51.066 23.967  1.00 162.01 ? 130 ALA B CA  1 
ATOM   4485 C C   . ALA B 1 130 ? -6.032  -50.729 25.453  1.00 183.10 ? 130 ALA B C   1 
ATOM   4486 O O   . ALA B 1 130 ? -6.082  -51.637 26.303  1.00 169.66 ? 130 ALA B O   1 
ATOM   4487 C CB  . ALA B 1 130 ? -4.754  -51.015 23.293  1.00 167.78 ? 130 ALA B CB  1 
ATOM   4488 N N   . THR B 1 131 ? -5.918  -49.417 25.730  1.00 213.52 ? 131 THR B N   1 
ATOM   4489 C CA  . THR B 1 131 ? -5.805  -48.942 27.111  1.00 198.49 ? 131 THR B CA  1 
ATOM   4490 C C   . THR B 1 131 ? -7.043  -49.343 27.903  1.00 204.67 ? 131 THR B C   1 
ATOM   4491 O O   . THR B 1 131 ? -6.928  -49.823 29.041  1.00 208.35 ? 131 THR B O   1 
ATOM   4492 C CB  . THR B 1 131 ? -5.478  -47.461 27.320  1.00 190.69 ? 131 THR B CB  1 
ATOM   4493 O OG1 . THR B 1 131 ? -6.569  -46.668 26.861  1.00 195.84 ? 131 THR B OG1 1 
ATOM   4494 C CG2 . THR B 1 131 ? -4.135  -47.064 26.733  1.00 202.52 ? 131 THR B CG2 1 
ATOM   4495 N N   . ASP B 1 132 ? -8.206  -49.144 27.265  1.00 208.55 ? 132 ASP B N   1 
ATOM   4496 C CA  . ASP B 1 132 ? -9.493  -49.471 27.874  1.00 178.74 ? 132 ASP B CA  1 
ATOM   4497 C C   . ASP B 1 132 ? -9.540  -50.953 28.237  1.00 177.55 ? 132 ASP B C   1 
ATOM   4498 O O   . ASP B 1 132 ? -9.955  -51.324 29.346  1.00 155.94 ? 132 ASP B O   1 
ATOM   4499 C CB  . ASP B 1 132 ? -10.656 -48.891 27.087  1.00 167.90 ? 132 ASP B CB  1 
ATOM   4500 C CG  . ASP B 1 132 ? -10.931 -47.419 27.366  1.00 185.91 ? 132 ASP B CG  1 
ATOM   4501 O OD1 . ASP B 1 132 ? -10.374 -46.903 28.366  1.00 190.73 ? 132 ASP B OD1 1 
ATOM   4502 O OD2 . ASP B 1 132 ? -11.695 -46.795 26.588  1.00 200.75 ? 132 ASP B OD2 1 
ATOM   4503 N N   . GLU B 1 133 ? -9.101  -51.770 27.279  1.00 196.94 ? 133 GLU B N   1 
ATOM   4504 C CA  . GLU B 1 133 ? -9.068  -53.222 27.423  1.00 198.03 ? 133 GLU B CA  1 
ATOM   4505 C C   . GLU B 1 133 ? -8.213  -53.606 28.631  1.00 194.46 ? 133 GLU B C   1 
ATOM   4506 O O   . GLU B 1 133 ? -8.611  -54.440 29.454  1.00 176.22 ? 133 GLU B O   1 
ATOM   4507 C CB  . GLU B 1 133 ? -8.570  -53.841 26.113  1.00 198.93 ? 133 GLU B CB  1 
ATOM   4508 C CG  . GLU B 1 133 ? -8.369  -55.351 26.161  1.00 191.40 ? 133 GLU B CG  1 
ATOM   4509 C CD  . GLU B 1 133 ? -9.643  -56.139 26.293  1.00 223.21 ? 133 GLU B CD  1 
ATOM   4510 O OE1 . GLU B 1 133 ? -10.256 -56.102 27.376  1.00 251.39 ? 133 GLU B OE1 1 
ATOM   4511 O OE2 . GLU B 1 133 ? -10.004 -56.787 25.295  1.00 251.73 ? 133 GLU B OE2 1 
ATOM   4512 N N   . LEU B 1 134 ? -7.042  -52.975 28.698  1.00 194.16 ? 134 LEU B N   1 
ATOM   4513 C CA  . LEU B 1 134 ? -6.082  -53.220 29.769  1.00 196.23 ? 134 LEU B CA  1 
ATOM   4514 C C   . LEU B 1 134 ? -6.713  -52.904 31.122  1.00 181.66 ? 134 LEU B C   1 
ATOM   4515 O O   . LEU B 1 134 ? -6.588  -53.685 32.075  1.00 184.46 ? 134 LEU B O   1 
ATOM   4516 C CB  . LEU B 1 134 ? -4.721  -52.563 29.552  1.00 215.42 ? 134 LEU B CB  1 
ATOM   4517 C CG  . LEU B 1 134 ? -3.869  -53.189 28.446  1.00 216.95 ? 134 LEU B CG  1 
ATOM   4518 C CD1 . LEU B 1 134 ? -2.767  -52.220 28.051  1.00 259.72 ? 134 LEU B CD1 1 
ATOM   4519 C CD2 . LEU B 1 134 ? -3.303  -54.541 28.895  1.00 185.51 ? 134 LEU B CD2 1 
ATOM   4520 N N   . GLY B 1 135 ? -7.390  -51.757 31.165  1.00 171.87 ? 135 GLY B N   1 
ATOM   4521 C CA  . GLY B 1 135 ? -8.065  -51.286 32.368  1.00 180.00 ? 135 GLY B CA  1 
ATOM   4522 C C   . GLY B 1 135 ? -9.095  -52.314 32.832  1.00 196.50 ? 135 GLY B C   1 
ATOM   4523 O O   . GLY B 1 135 ? -9.169  -52.657 34.021  1.00 187.94 ? 135 GLY B O   1 
ATOM   4524 N N   . ARG B 1 136 ? -9.869  -52.794 31.857  1.00 210.99 ? 136 ARG B N   1 
ATOM   4525 C CA  . ARG B 1 136 ? -10.923 -53.771 32.102  1.00 216.51 ? 136 ARG B CA  1 
ATOM   4526 C C   . ARG B 1 136 ? -10.315 -55.049 32.682  1.00 226.65 ? 136 ARG B C   1 
ATOM   4527 O O   . ARG B 1 136 ? -10.803 -55.613 33.672  1.00 254.73 ? 136 ARG B O   1 
ATOM   4528 C CB  . ARG B 1 136 ? -11.871 -53.955 30.912  1.00 205.62 ? 136 ARG B CB  1 
ATOM   4529 C CG  . ARG B 1 136 ? -12.822 -52.785 30.702  1.00 200.80 ? 136 ARG B CG  1 
ATOM   4530 C CD  . ARG B 1 136 ? -13.808 -53.019 29.565  1.00 204.49 ? 136 ARG B CD  1 
ATOM   4531 N NE  . ARG B 1 136 ? -13.180 -53.152 28.244  1.00 221.27 ? 136 ARG B NE  1 
ATOM   4532 C CZ  . ARG B 1 136 ? -12.923 -54.299 27.614  1.00 233.59 ? 136 ARG B CZ  1 
ATOM   4533 N NH1 . ARG B 1 136 ? -13.159 -55.455 28.208  1.00 236.11 ? 136 ARG B NH1 1 
ATOM   4534 N NH2 . ARG B 1 136 ? -12.399 -54.291 26.399  1.00 247.93 ? 136 ARG B NH2 1 
ATOM   4535 N N   . ARG B 1 137 ? -9.273  -55.523 31.977  1.00 195.30 ? 137 ARG B N   1 
ATOM   4536 C CA  . ARG B 1 137 ? -8.717  -56.860 32.111  1.00 185.06 ? 137 ARG B CA  1 
ATOM   4537 C C   . ARG B 1 137 ? -7.703  -56.929 33.246  1.00 188.82 ? 137 ARG B C   1 
ATOM   4538 O O   . ARG B 1 137 ? -7.198  -58.011 33.538  1.00 204.13 ? 137 ARG B O   1 
ATOM   4539 C CB  . ARG B 1 137 ? -7.978  -57.308 30.844  1.00 170.42 ? 137 ARG B CB  1 
ATOM   4540 C CG  . ARG B 1 137 ? -8.837  -57.855 29.718  1.00 174.04 ? 137 ARG B CG  1 
ATOM   4541 C CD  . ARG B 1 137 ? -7.970  -58.376 28.585  1.00 174.22 ? 137 ARG B CD  1 
ATOM   4542 N NE  . ARG B 1 137 ? -7.212  -59.567 28.993  1.00 172.42 ? 137 ARG B NE  1 
ATOM   4543 C CZ  . ARG B 1 137 ? -6.414  -60.263 28.183  1.00 184.53 ? 137 ARG B CZ  1 
ATOM   4544 N NH1 . ARG B 1 137 ? -6.270  -59.901 26.919  1.00 180.30 ? 137 ARG B NH1 1 
ATOM   4545 N NH2 . ARG B 1 137 ? -5.757  -61.320 28.626  1.00 206.07 ? 137 ARG B NH2 1 
ATOM   4546 N N   . THR B 1 138 ? -7.388  -55.775 33.853  1.00 173.05 ? 138 THR B N   1 
ATOM   4547 C CA  . THR B 1 138 ? -6.430  -55.733 34.947  1.00 165.36 ? 138 THR B CA  1 
ATOM   4548 C C   . THR B 1 138 ? -7.078  -55.166 36.208  1.00 157.57 ? 138 THR B C   1 
ATOM   4549 O O   . THR B 1 138 ? -6.557  -55.337 37.307  1.00 153.91 ? 138 THR B O   1 
ATOM   4550 C CB  . THR B 1 138 ? -5.164  -54.966 34.563  1.00 189.82 ? 138 THR B CB  1 
ATOM   4551 O OG1 . THR B 1 138 ? -5.550  -53.616 34.303  1.00 216.94 ? 138 THR B OG1 1 
ATOM   4552 C CG2 . THR B 1 138 ? -4.436  -55.572 33.376  1.00 186.47 ? 138 THR B CG2 1 
ATOM   4553 N N   . GLY B 1 139 ? -8.198  -54.461 36.044  1.00 156.23 ? 139 GLY B N   1 
ATOM   4554 C CA  . GLY B 1 139 ? -8.890  -53.876 37.180  1.00 163.22 ? 139 GLY B CA  1 
ATOM   4555 C C   . GLY B 1 139 ? -8.283  -52.534 37.578  1.00 154.00 ? 139 GLY B C   1 
ATOM   4556 O O   . GLY B 1 139 ? -8.562  -52.009 38.657  1.00 150.75 ? 139 GLY B O   1 
ATOM   4557 N N   . ALA B 1 140 ? -7.428  -52.005 36.701  1.00 153.87 ? 140 ALA B N   1 
ATOM   4558 C CA  . ALA B 1 140 ? -6.948  -50.644 36.855  1.00 177.57 ? 140 ALA B CA  1 
ATOM   4559 C C   . ALA B 1 140 ? -7.724  -49.739 35.901  1.00 182.30 ? 140 ALA B C   1 
ATOM   4560 O O   . ALA B 1 140 ? -7.931  -50.087 34.741  1.00 154.62 ? 140 ALA B O   1 
ATOM   4561 C CB  . ALA B 1 140 ? -5.452  -50.581 36.646  1.00 176.60 ? 140 ALA B CB  1 
ATOM   4562 N N   . THR B 1 141 ? -8.179  -48.602 36.438  1.00 194.05 ? 141 THR B N   1 
ATOM   4563 C CA  . THR B 1 141 ? -9.037  -47.651 35.750  1.00 175.07 ? 141 THR B CA  1 
ATOM   4564 C C   . THR B 1 141 ? -8.146  -46.585 35.131  1.00 152.72 ? 141 THR B C   1 
ATOM   4565 O O   . THR B 1 141 ? -7.586  -45.787 35.895  1.00 137.56 ? 141 THR B O   1 
ATOM   4566 C CB  . THR B 1 141 ? -9.964  -47.022 36.793  1.00 192.56 ? 141 THR B CB  1 
ATOM   4567 O OG1 . THR B 1 141 ? -10.762 -48.063 37.353  1.00 204.72 ? 141 THR B OG1 1 
ATOM   4568 C CG2 . THR B 1 141 ? -10.811 -45.893 36.236  1.00 218.82 ? 141 THR B CG2 1 
ATOM   4569 N N   . PRO B 1 142 ? -7.953  -46.565 33.780  1.00 153.87 ? 142 PRO B N   1 
ATOM   4570 C CA  . PRO B 1 142 ? -7.157  -45.534 33.114  1.00 159.67 ? 142 PRO B CA  1 
ATOM   4571 C C   . PRO B 1 142 ? -7.496  -44.123 33.596  1.00 162.63 ? 142 PRO B C   1 
ATOM   4572 O O   . PRO B 1 142 ? -8.654  -43.745 33.684  1.00 159.83 ? 142 PRO B O   1 
ATOM   4573 C CB  . PRO B 1 142 ? -7.440  -45.753 31.600  1.00 144.06 ? 142 PRO B CB  1 
ATOM   4574 C CG  . PRO B 1 142 ? -7.636  -47.240 31.504  1.00 139.74 ? 142 PRO B CG  1 
ATOM   4575 C CD  . PRO B 1 142 ? -8.410  -47.562 32.797  1.00 154.02 ? 142 PRO B CD  1 
ATOM   4576 N N   . GLU B 1 143 ? -6.442  -43.378 33.944  1.00 187.70 ? 143 GLU B N   1 
ATOM   4577 C CA  . GLU B 1 143 ? -6.504  -42.055 34.542  1.00 179.19 ? 143 GLU B CA  1 
ATOM   4578 C C   . GLU B 1 143 ? -6.977  -41.063 33.480  1.00 156.59 ? 143 GLU B C   1 
ATOM   4579 O O   . GLU B 1 143 ? -7.384  -39.943 33.792  1.00 143.49 ? 143 GLU B O   1 
ATOM   4580 C CB  . GLU B 1 143 ? -5.076  -41.855 35.050  1.00 209.57 ? 143 GLU B CB  1 
ATOM   4581 C CG  . GLU B 1 143 ? -4.886  -40.700 36.029  1.00 218.52 ? 143 GLU B CG  1 
ATOM   4582 C CD  . GLU B 1 143 ? -3.397  -40.406 36.159  1.00 226.51 ? 143 GLU B CD  1 
ATOM   4583 O OE1 . GLU B 1 143 ? -2.763  -40.089 35.129  1.00 213.41 ? 143 GLU B OE1 1 
ATOM   4584 O OE2 . GLU B 1 143 ? -2.862  -40.523 37.281  1.00 238.21 ? 143 GLU B OE2 1 
ATOM   4585 N N   . GLU B 1 144 ? -6.933  -41.520 32.222  1.00 141.74 ? 144 GLU B N   1 
ATOM   4586 C CA  . GLU B 1 144 ? -7.239  -40.712 31.057  1.00 165.23 ? 144 GLU B CA  1 
ATOM   4587 C C   . GLU B 1 144 ? -7.737  -41.634 29.939  1.00 173.08 ? 144 GLU B C   1 
ATOM   4588 O O   . GLU B 1 144 ? -7.397  -41.440 28.775  1.00 190.22 ? 144 GLU B O   1 
ATOM   4589 C CB  . GLU B 1 144 ? -5.986  -39.897 30.719  1.00 187.53 ? 144 GLU B CB  1 
ATOM   4590 C CG  . GLU B 1 144 ? -6.232  -38.405 30.492  1.00 198.43 ? 144 GLU B CG  1 
ATOM   4591 C CD  . GLU B 1 144 ? -7.362  -38.046 29.540  1.00 222.91 ? 144 GLU B CD  1 
ATOM   4592 O OE1 . GLU B 1 144 ? -7.383  -38.521 28.377  1.00 227.15 ? 144 GLU B OE1 1 
ATOM   4593 O OE2 . GLU B 1 144 ? -8.222  -37.259 29.978  1.00 232.12 ? 144 GLU B OE2 1 
ATOM   4594 N N   . GLY B 1 145 ? -8.614  -42.587 30.296  1.00 179.11 ? 145 GLY B N   1 
ATOM   4595 C CA  . GLY B 1 145 ? -9.314  -43.447 29.342  1.00 204.31 ? 145 GLY B CA  1 
ATOM   4596 C C   . GLY B 1 145 ? -10.743 -42.977 29.002  1.00 227.49 ? 145 GLY B C   1 
ATOM   4597 O O   . GLY B 1 145 ? -11.146 -41.878 29.379  1.00 217.14 ? 145 GLY B O   1 
ATOM   4598 N N   . ASP B 1 146 ? -11.490 -43.800 28.234  1.00 227.87 ? 146 ASP B N   1 
ATOM   4599 C CA  . ASP B 1 146 ? -12.862 -43.590 27.756  1.00 203.40 ? 146 ASP B CA  1 
ATOM   4600 C C   . ASP B 1 146 ? -12.887 -43.434 26.231  1.00 190.29 ? 146 ASP B C   1 
ATOM   4601 O O   . ASP B 1 146 ? -12.964 -42.312 25.729  1.00 185.06 ? 146 ASP B O   1 
ATOM   4602 C CB  . ASP B 1 146 ? -13.587 -42.412 28.404  1.00 206.11 ? 146 ASP B CB  1 
ATOM   4603 C CG  . ASP B 1 146 ? -15.118 -42.421 28.322  1.00 215.58 ? 146 ASP B CG  1 
ATOM   4604 O OD1 . ASP B 1 146 ? -15.678 -42.785 27.256  1.00 195.60 ? 146 ASP B OD1 1 
ATOM   4605 O OD2 . ASP B 1 146 ? -15.773 -42.031 29.315  1.00 214.51 ? 146 ASP B OD2 1 
ATOM   4606 N N   . HIS B 1 147 ? -12.902 -44.562 25.511  1.00 175.74 ? 147 HIS B N   1 
ATOM   4607 C CA  . HIS B 1 147 ? -12.594 -44.600 24.096  1.00 166.01 ? 147 HIS B CA  1 
ATOM   4608 C C   . HIS B 1 147 ? -13.665 -43.865 23.284  1.00 168.17 ? 147 HIS B C   1 
ATOM   4609 O O   . HIS B 1 147 ? -13.338 -43.261 22.259  1.00 161.16 ? 147 HIS B O   1 
ATOM   4610 C CB  . HIS B 1 147 ? -12.471 -46.057 23.636  1.00 172.65 ? 147 HIS B CB  1 
ATOM   4611 C CG  . HIS B 1 147 ? -12.227 -46.171 22.169  1.00 178.00 ? 147 HIS B CG  1 
ATOM   4612 N ND1 . HIS B 1 147 ? -11.607 -45.189 21.425  1.00 161.59 ? 147 HIS B ND1 1 
ATOM   4613 C CD2 . HIS B 1 147 ? -12.553 -47.134 21.312  1.00 188.96 ? 147 HIS B CD2 1 
ATOM   4614 C CE1 . HIS B 1 147 ? -11.557 -45.566 20.159  1.00 173.03 ? 147 HIS B CE1 1 
ATOM   4615 N NE2 . HIS B 1 147 ? -12.111 -46.756 20.071  1.00 190.11 ? 147 HIS B NE2 1 
ATOM   4616 N N   . ALA B 1 148 ? -14.926 -44.065 23.700  1.00 170.77 ? 148 ALA B N   1 
ATOM   4617 C CA  . ALA B 1 148 ? -16.063 -43.605 22.931  1.00 159.92 ? 148 ALA B CA  1 
ATOM   4618 C C   . ALA B 1 148 ? -16.108 -42.084 23.033  1.00 144.78 ? 148 ALA B C   1 
ATOM   4619 O O   . ALA B 1 148 ? -16.273 -41.387 22.021  1.00 116.15 ? 148 ALA B O   1 
ATOM   4620 C CB  . ALA B 1 148 ? -17.312 -44.271 23.448  1.00 188.76 ? 148 ALA B CB  1 
ATOM   4621 N N   . PHE B 1 149 ? -16.078 -41.611 24.293  1.00 157.23 ? 149 PHE B N   1 
ATOM   4622 C CA  . PHE B 1 149 ? -16.259 -40.199 24.602  1.00 179.38 ? 149 PHE B CA  1 
ATOM   4623 C C   . PHE B 1 149 ? -15.189 -39.370 23.892  1.00 207.59 ? 149 PHE B C   1 
ATOM   4624 O O   . PHE B 1 149 ? -15.498 -38.331 23.289  1.00 210.41 ? 149 PHE B O   1 
ATOM   4625 C CB  . PHE B 1 149 ? -16.313 -39.949 26.118  1.00 175.43 ? 149 PHE B CB  1 
ATOM   4626 C CG  . PHE B 1 149 ? -16.654 -38.568 26.677  1.00 172.82 ? 149 PHE B CG  1 
ATOM   4627 C CD1 . PHE B 1 149 ? -16.330 -37.393 25.996  1.00 174.89 ? 149 PHE B CD1 1 
ATOM   4628 C CD2 . PHE B 1 149 ? -17.276 -38.446 27.920  1.00 170.33 ? 149 PHE B CD2 1 
ATOM   4629 C CE1 . PHE B 1 149 ? -16.640 -36.142 26.523  1.00 183.68 ? 149 PHE B CE1 1 
ATOM   4630 C CE2 . PHE B 1 149 ? -17.595 -37.192 28.440  1.00 180.15 ? 149 PHE B CE2 1 
ATOM   4631 C CZ  . PHE B 1 149 ? -17.287 -36.039 27.738  1.00 183.95 ? 149 PHE B CZ  1 
ATOM   4632 N N   . VAL B 1 150 ? -13.947 -39.858 23.984  1.00 212.17 ? 150 VAL B N   1 
ATOM   4633 C CA  . VAL B 1 150 ? -12.802 -39.187 23.379  1.00 184.75 ? 150 VAL B CA  1 
ATOM   4634 C C   . VAL B 1 150 ? -13.008 -39.058 21.867  1.00 175.58 ? 150 VAL B C   1 
ATOM   4635 O O   . VAL B 1 150 ? -12.779 -37.989 21.285  1.00 186.75 ? 150 VAL B O   1 
ATOM   4636 C CB  . VAL B 1 150 ? -11.445 -39.813 23.766  1.00 198.04 ? 150 VAL B CB  1 
ATOM   4637 C CG1 . VAL B 1 150 ? -10.298 -39.356 22.868  1.00 219.84 ? 150 VAL B CG1 1 
ATOM   4638 C CG2 . VAL B 1 150 ? -11.104 -39.552 25.227  1.00 203.46 ? 150 VAL B CG2 1 
ATOM   4639 N N   . ALA B 1 151 ? -13.452 -40.170 21.272  1.00 167.13 ? 151 ALA B N   1 
ATOM   4640 C CA  . ALA B 1 151 ? -13.711 -40.243 19.837  1.00 159.17 ? 151 ALA B CA  1 
ATOM   4641 C C   . ALA B 1 151 ? -14.745 -39.186 19.435  1.00 168.20 ? 151 ALA B C   1 
ATOM   4642 O O   . ALA B 1 151 ? -14.571 -38.458 18.445  1.00 167.02 ? 151 ALA B O   1 
ATOM   4643 C CB  . ALA B 1 151 ? -14.195 -41.619 19.445  1.00 161.04 ? 151 ALA B CB  1 
ATOM   4644 N N   . ARG B 1 152 ? -15.810 -39.135 20.237  1.00 174.05 ? 152 ARG B N   1 
ATOM   4645 C CA  . ARG B 1 152 ? -16.908 -38.201 20.023  1.00 165.46 ? 152 ARG B CA  1 
ATOM   4646 C C   . ARG B 1 152 ? -16.398 -36.756 20.042  1.00 164.71 ? 152 ARG B C   1 
ATOM   4647 O O   . ARG B 1 152 ? -16.767 -35.967 19.172  1.00 163.82 ? 152 ARG B O   1 
ATOM   4648 C CB  . ARG B 1 152 ? -18.127 -38.456 20.920  1.00 191.10 ? 152 ARG B CB  1 
ATOM   4649 C CG  . ARG B 1 152 ? -19.368 -37.713 20.454  1.00 218.65 ? 152 ARG B CG  1 
ATOM   4650 C CD  . ARG B 1 152 ? -20.573 -38.069 21.313  1.00 218.43 ? 152 ARG B CD  1 
ATOM   4651 N NE  . ARG B 1 152 ? -21.656 -37.112 21.060  1.00 235.38 ? 152 ARG B NE  1 
ATOM   4652 C CZ  . ARG B 1 152 ? -22.828 -37.430 20.525  1.00 264.87 ? 152 ARG B CZ  1 
ATOM   4653 N NH1 . ARG B 1 152 ? -23.043 -38.654 20.072  1.00 276.83 ? 152 ARG B NH1 1 
ATOM   4654 N NH2 . ARG B 1 152 ? -23.785 -36.522 20.434  1.00 288.66 ? 152 ARG B NH2 1 
ATOM   4655 N N   . TRP B 1 153 ? -15.588 -36.381 21.043  1.00 182.03 ? 153 TRP B N   1 
ATOM   4656 C CA  . TRP B 1 153 ? -15.478 -34.973 21.420  1.00 188.24 ? 153 TRP B CA  1 
ATOM   4657 C C   . TRP B 1 153 ? -14.089 -34.359 21.215  1.00 185.01 ? 153 TRP B C   1 
ATOM   4658 O O   . TRP B 1 153 ? -13.947 -33.129 21.224  1.00 173.72 ? 153 TRP B O   1 
ATOM   4659 C CB  . TRP B 1 153 ? -15.987 -34.753 22.852  1.00 188.80 ? 153 TRP B CB  1 
ATOM   4660 C CG  . TRP B 1 153 ? -17.484 -34.707 22.913  1.00 176.86 ? 153 TRP B CG  1 
ATOM   4661 C CD1 . TRP B 1 153 ? -18.323 -35.573 23.545  1.00 187.71 ? 153 TRP B CD1 1 
ATOM   4662 C CD2 . TRP B 1 153 ? -18.324 -33.753 22.235  1.00 171.01 ? 153 TRP B CD2 1 
ATOM   4663 N NE1 . TRP B 1 153 ? -19.627 -35.205 23.347  1.00 174.46 ? 153 TRP B NE1 1 
ATOM   4664 C CE2 . TRP B 1 153 ? -19.655 -34.103 22.534  1.00 176.85 ? 153 TRP B CE2 1 
ATOM   4665 C CE3 . TRP B 1 153 ? -18.080 -32.638 21.427  1.00 163.86 ? 153 TRP B CE3 1 
ATOM   4666 C CZ2 . TRP B 1 153 ? -20.727 -33.378 22.031  1.00 194.15 ? 153 TRP B CZ2 1 
ATOM   4667 C CZ3 . TRP B 1 153 ? -19.141 -31.919 20.933  1.00 154.50 ? 153 TRP B CZ3 1 
ATOM   4668 C CH2 . TRP B 1 153 ? -20.442 -32.293 21.229  1.00 177.97 ? 153 TRP B CH2 1 
ATOM   4669 N N   . GLY B 1 154 ? -13.075 -35.217 21.055  1.00 181.58 ? 154 GLY B N   1 
ATOM   4670 C CA  . GLY B 1 154 ? -11.709 -34.778 20.834  1.00 169.36 ? 154 GLY B CA  1 
ATOM   4671 C C   . GLY B 1 154 ? -11.466 -34.477 19.363  1.00 159.01 ? 154 GLY B C   1 
ATOM   4672 O O   . GLY B 1 154 ? -10.443 -33.874 19.036  1.00 173.30 ? 154 GLY B O   1 
ATOM   4673 N N   . SER B 1 155 ? -12.427 -34.895 18.517  1.00 148.96 ? 155 SER B N   1 
ATOM   4674 C CA  . SER B 1 155 ? -12.415 -34.661 17.078  1.00 168.47 ? 155 SER B CA  1 
ATOM   4675 C C   . SER B 1 155 ? -12.389 -33.156 16.798  1.00 178.81 ? 155 SER B C   1 
ATOM   4676 O O   . SER B 1 155 ? -12.659 -32.354 17.693  1.00 205.85 ? 155 SER B O   1 
ATOM   4677 C CB  . SER B 1 155 ? -13.597 -35.322 16.391  1.00 164.53 ? 155 SER B CB  1 
ATOM   4678 O OG  . SER B 1 155 ? -14.686 -34.412 16.261  1.00 192.90 ? 155 SER B OG  1 
ATOM   4679 N N   . LYS B 1 156 ? -12.071 -32.775 15.552  1.00 163.40 ? 156 LYS B N   1 
ATOM   4680 C CA  . LYS B 1 156 ? -11.861 -31.359 15.285  1.00 175.23 ? 156 LYS B CA  1 
ATOM   4681 C C   . LYS B 1 156 ? -13.190 -30.625 15.529  1.00 195.92 ? 156 LYS B C   1 
ATOM   4682 O O   . LYS B 1 156 ? -13.244 -29.598 16.222  1.00 211.06 ? 156 LYS B O   1 
ATOM   4683 C CB  . LYS B 1 156 ? -11.290 -31.130 13.876  1.00 164.78 ? 156 LYS B CB  1 
ATOM   4684 C CG  . LYS B 1 156 ? -10.000 -31.824 13.413  1.00 157.78 ? 156 LYS B CG  1 
ATOM   4685 C CD  . LYS B 1 156 ? -8.718  -31.504 14.177  1.00 166.61 ? 156 LYS B CD  1 
ATOM   4686 C CE  . LYS B 1 156 ? -7.532  -32.239 13.579  1.00 169.79 ? 156 LYS B CE  1 
ATOM   4687 N NZ  . LYS B 1 156 ? -6.435  -32.624 14.486  1.00 157.80 ? 156 LYS B NZ  1 
ATOM   4688 N N   . SER B 1 157 ? -14.225 -31.153 14.870  1.00 188.73 ? 157 SER B N   1 
ATOM   4689 C CA  . SER B 1 157 ? -15.550 -30.557 14.869  1.00 174.04 ? 157 SER B CA  1 
ATOM   4690 C C   . SER B 1 157 ? -16.077 -30.431 16.306  1.00 159.60 ? 157 SER B C   1 
ATOM   4691 O O   . SER B 1 157 ? -16.592 -29.380 16.723  1.00 162.45 ? 157 SER B O   1 
ATOM   4692 C CB  . SER B 1 157 ? -16.493 -31.371 14.008  1.00 182.83 ? 157 SER B CB  1 
ATOM   4693 O OG  . SER B 1 157 ? -16.631 -32.704 14.492  1.00 176.94 ? 157 SER B OG  1 
ATOM   4694 N N   . GLY B 1 158 ? -15.925 -31.545 17.030  1.00 143.69 ? 158 GLY B N   1 
ATOM   4695 C CA  . GLY B 1 158 ? -16.368 -31.643 18.417  1.00 136.12 ? 158 GLY B CA  1 
ATOM   4696 C C   . GLY B 1 158 ? -15.678 -30.576 19.267  1.00 135.46 ? 158 GLY B C   1 
ATOM   4697 O O   . GLY B 1 158 ? -16.322 -29.884 20.071  1.00 137.05 ? 158 GLY B O   1 
ATOM   4698 N N   . GLY B 1 159 ? -14.364 -30.474 19.057  1.00 152.35 ? 159 GLY B N   1 
ATOM   4699 C CA  . GLY B 1 159 ? -13.525 -29.515 19.769  1.00 188.19 ? 159 GLY B CA  1 
ATOM   4700 C C   . GLY B 1 159 ? -14.029 -28.093 19.534  1.00 183.66 ? 159 GLY B C   1 
ATOM   4701 O O   . GLY B 1 159 ? -14.158 -27.299 20.474  1.00 175.77 ? 159 GLY B O   1 
ATOM   4702 N N   . LYS B 1 160 ? -14.308 -27.813 18.260  1.00 177.44 ? 160 LYS B N   1 
ATOM   4703 C CA  . LYS B 1 160 ? -14.799 -26.510 17.823  1.00 170.85 ? 160 LYS B CA  1 
ATOM   4704 C C   . LYS B 1 160 ? -16.103 -26.172 18.553  1.00 176.16 ? 160 LYS B C   1 
ATOM   4705 O O   . LYS B 1 160 ? -16.279 -25.054 19.061  1.00 155.12 ? 160 LYS B O   1 
ATOM   4706 C CB  . LYS B 1 160 ? -14.835 -26.448 16.288  1.00 149.15 ? 160 LYS B CB  1 
ATOM   4707 C CG  . LYS B 1 160 ? -15.322 -25.133 15.694  1.00 127.71 ? 160 LYS B CG  1 
ATOM   4708 C CD  . LYS B 1 160 ? -14.727 -24.856 14.317  1.00 122.81 ? 160 LYS B CD  1 
ATOM   4709 C CE  . LYS B 1 160 ? -14.973 -23.418 13.985  1.00 134.24 ? 160 LYS B CE  1 
ATOM   4710 N NZ  . LYS B 1 160 ? -14.037 -22.930 12.976  1.00 146.56 ? 160 LYS B NZ  1 
ATOM   4711 N N   . GLU B 1 161 ? -16.989 -27.169 18.584  1.00 194.80 ? 161 GLU B N   1 
ATOM   4712 C CA  . GLU B 1 161 ? -18.293 -27.048 19.226  1.00 179.46 ? 161 GLU B CA  1 
ATOM   4713 C C   . GLU B 1 161 ? -18.121 -26.681 20.703  1.00 163.58 ? 161 GLU B C   1 
ATOM   4714 O O   . GLU B 1 161 ? -18.791 -25.770 21.227  1.00 162.20 ? 161 GLU B O   1 
ATOM   4715 C CB  . GLU B 1 161 ? -19.120 -28.323 19.068  1.00 171.46 ? 161 GLU B CB  1 
ATOM   4716 C CG  . GLU B 1 161 ? -19.445 -28.606 17.606  1.00 196.69 ? 161 GLU B CG  1 
ATOM   4717 C CD  . GLU B 1 161 ? -20.714 -29.378 17.319  1.00 209.70 ? 161 GLU B CD  1 
ATOM   4718 O OE1 . GLU B 1 161 ? -21.408 -29.758 18.283  1.00 220.99 ? 161 GLU B OE1 1 
ATOM   4719 O OE2 . GLU B 1 161 ? -21.007 -29.594 16.120  1.00 212.28 ? 161 GLU B OE2 1 
ATOM   4720 N N   . ILE B 1 162 ? -17.207 -27.417 21.339  1.00 161.97 ? 162 ILE B N   1 
ATOM   4721 C CA  . ILE B 1 162 ? -16.911 -27.225 22.757  1.00 161.52 ? 162 ILE B CA  1 
ATOM   4722 C C   . ILE B 1 162 ? -16.430 -25.797 23.007  1.00 162.76 ? 162 ILE B C   1 
ATOM   4723 O O   . ILE B 1 162 ? -16.867 -25.142 23.953  1.00 151.31 ? 162 ILE B O   1 
ATOM   4724 C CB  . ILE B 1 162 ? -16.020 -28.318 23.374  1.00 163.38 ? 162 ILE B CB  1 
ATOM   4725 C CG1 . ILE B 1 162 ? -16.685 -29.689 23.226  1.00 176.69 ? 162 ILE B CG1 1 
ATOM   4726 C CG2 . ILE B 1 162 ? -15.697 -27.995 24.838  1.00 152.07 ? 162 ILE B CG2 1 
ATOM   4727 C CD1 . ILE B 1 162 ? -15.718 -30.852 23.345  1.00 194.81 ? 162 ILE B CD1 1 
ATOM   4728 N N   . CYS B 1 163 ? -15.536 -25.345 22.131  1.00 185.53 ? 163 CYS B N   1 
ATOM   4729 C CA  . CYS B 1 163 ? -14.963 -24.004 22.194  1.00 206.59 ? 163 CYS B CA  1 
ATOM   4730 C C   . CYS B 1 163 ? -16.069 -22.958 22.125  1.00 190.38 ? 163 CYS B C   1 
ATOM   4731 O O   . CYS B 1 163 ? -16.088 -22.004 22.905  1.00 170.65 ? 163 CYS B O   1 
ATOM   4732 C CB  . CYS B 1 163 ? -14.060 -23.721 21.000  1.00 226.47 ? 163 CYS B CB  1 
ATOM   4733 S SG  . CYS B 1 163 ? -12.547 -24.717 20.956  1.00 212.58 ? 163 CYS B SG  1 
ATOM   4734 N N   . LEU B 1 164 ? -16.976 -23.175 21.173  1.00 190.83 ? 164 LEU B N   1 
ATOM   4735 C CA  . LEU B 1 164 ? -18.115 -22.287 20.944  1.00 185.96 ? 164 LEU B CA  1 
ATOM   4736 C C   . LEU B 1 164 ? -18.957 -22.182 22.219  1.00 168.25 ? 164 LEU B C   1 
ATOM   4737 O O   . LEU B 1 164 ? -19.340 -21.079 22.644  1.00 141.57 ? 164 LEU B O   1 
ATOM   4738 C CB  . LEU B 1 164 ? -18.959 -22.713 19.741  1.00 203.41 ? 164 LEU B CB  1 
ATOM   4739 C CG  . LEU B 1 164 ? -18.372 -22.427 18.351  1.00 212.74 ? 164 LEU B CG  1 
ATOM   4740 C CD1 . LEU B 1 164 ? -19.064 -23.266 17.268  1.00 216.73 ? 164 LEU B CD1 1 
ATOM   4741 C CD2 . LEU B 1 164 ? -18.400 -20.939 17.990  1.00 181.44 ? 164 LEU B CD2 1 
ATOM   4742 N N   . ARG B 1 165 ? -19.217 -23.355 22.801  1.00 178.60 ? 165 ARG B N   1 
ATOM   4743 C CA  . ARG B 1 165 ? -20.009 -23.464 24.022  1.00 162.42 ? 165 ARG B CA  1 
ATOM   4744 C C   . ARG B 1 165 ? -19.359 -22.654 25.147  1.00 164.61 ? 165 ARG B C   1 
ATOM   4745 O O   . ARG B 1 165 ? -20.028 -21.913 25.866  1.00 183.15 ? 165 ARG B O   1 
ATOM   4746 C CB  . ARG B 1 165 ? -20.470 -24.879 24.385  1.00 144.80 ? 165 ARG B CB  1 
ATOM   4747 C CG  . ARG B 1 165 ? -21.851 -25.046 23.785  1.00 139.21 ? 165 ARG B CG  1 
ATOM   4748 C CD  . ARG B 1 165 ? -22.219 -26.461 23.411  1.00 152.88 ? 165 ARG B CD  1 
ATOM   4749 N NE  . ARG B 1 165 ? -21.970 -26.694 21.982  1.00 169.07 ? 165 ARG B NE  1 
ATOM   4750 C CZ  . ARG B 1 165 ? -22.430 -27.729 21.280  1.00 180.53 ? 165 ARG B CZ  1 
ATOM   4751 N NH1 . ARG B 1 165 ? -23.237 -28.600 21.858  1.00 176.05 ? 165 ARG B NH1 1 
ATOM   4752 N NH2 . ARG B 1 165 ? -22.102 -27.878 20.006  1.00 200.40 ? 165 ARG B NH2 1 
ATOM   4753 N N   . ALA B 1 166 ? -18.044 -22.816 25.264  1.00 174.04 ? 166 ALA B N   1 
ATOM   4754 C CA  . ALA B 1 166 ? -17.247 -22.163 26.283  1.00 184.41 ? 166 ALA B CA  1 
ATOM   4755 C C   . ALA B 1 166 ? -17.317 -20.656 26.108  1.00 170.90 ? 166 ALA B C   1 
ATOM   4756 O O   . ALA B 1 166 ? -16.980 -19.941 27.050  1.00 157.66 ? 166 ALA B O   1 
ATOM   4757 C CB  . ALA B 1 166 ? -15.829 -22.705 26.289  1.00 210.54 ? 166 ALA B CB  1 
ATOM   4758 N N   . GLY B 1 167 ? -17.559 -20.196 24.872  1.00 163.85 ? 167 GLY B N   1 
ATOM   4759 C CA  . GLY B 1 167 ? -17.416 -18.790 24.521  1.00 178.20 ? 167 GLY B CA  1 
ATOM   4760 C C   . GLY B 1 167 ? -15.952 -18.418 24.335  1.00 169.54 ? 167 GLY B C   1 
ATOM   4761 O O   . GLY B 1 167 ? -15.543 -17.288 24.588  1.00 175.86 ? 167 GLY B O   1 
ATOM   4762 N N   . VAL B 1 168 ? -15.174 -19.395 23.879  1.00 164.40 ? 168 VAL B N   1 
ATOM   4763 C CA  . VAL B 1 168 ? -13.800 -19.135 23.495  1.00 161.24 ? 168 VAL B CA  1 
ATOM   4764 C C   . VAL B 1 168 ? -13.781 -18.872 21.987  1.00 157.94 ? 168 VAL B C   1 
ATOM   4765 O O   . VAL B 1 168 ? -14.410 -19.576 21.184  1.00 144.34 ? 168 VAL B O   1 
ATOM   4766 C CB  . VAL B 1 168 ? -12.795 -20.212 23.973  1.00 168.44 ? 168 VAL B CB  1 
ATOM   4767 C CG1 . VAL B 1 168 ? -12.948 -20.520 25.460  1.00 160.58 ? 168 VAL B CG1 1 
ATOM   4768 C CG2 . VAL B 1 168 ? -12.870 -21.512 23.178  1.00 175.81 ? 168 VAL B CG2 1 
ATOM   4769 N N   . ALA B 1 169 ? -13.076 -17.800 21.623  1.00 165.91 ? 169 ALA B N   1 
ATOM   4770 C CA  . ALA B 1 169 ? -12.907 -17.390 20.239  1.00 176.52 ? 169 ALA B CA  1 
ATOM   4771 C C   . ALA B 1 169 ? -12.316 -18.523 19.407  1.00 178.30 ? 169 ALA B C   1 
ATOM   4772 O O   . ALA B 1 169 ? -11.265 -19.057 19.744  1.00 183.95 ? 169 ALA B O   1 
ATOM   4773 C CB  . ALA B 1 169 ? -12.012 -16.178 20.199  1.00 189.24 ? 169 ALA B CB  1 
ATOM   4774 N N   . VAL B 1 170 ? -13.011 -18.882 18.324  1.00 174.29 ? 170 VAL B N   1 
ATOM   4775 C CA  . VAL B 1 170 ? -12.505 -19.860 17.372  1.00 166.30 ? 170 VAL B CA  1 
ATOM   4776 C C   . VAL B 1 170 ? -12.198 -19.135 16.064  1.00 175.64 ? 170 VAL B C   1 
ATOM   4777 O O   . VAL B 1 170 ? -12.621 -17.999 15.877  1.00 186.23 ? 170 VAL B O   1 
ATOM   4778 C CB  . VAL B 1 170 ? -13.440 -21.071 17.167  1.00 151.99 ? 170 VAL B CB  1 
ATOM   4779 C CG1 . VAL B 1 170 ? -13.800 -21.725 18.494  1.00 157.58 ? 170 VAL B CG1 1 
ATOM   4780 C CG2 . VAL B 1 170 ? -14.720 -20.730 16.412  1.00 160.31 ? 170 VAL B CG2 1 
ATOM   4781 N N   . PRO B 1 171 ? -11.431 -19.736 15.127  1.00 182.75 ? 171 PRO B N   1 
ATOM   4782 C CA  . PRO B 1 171 ? -11.305 -19.184 13.777  1.00 187.61 ? 171 PRO B CA  1 
ATOM   4783 C C   . PRO B 1 171 ? -12.632 -19.403 13.059  1.00 165.29 ? 171 PRO B C   1 
ATOM   4784 O O   . PRO B 1 171 ? -13.339 -20.366 13.338  1.00 156.33 ? 171 PRO B O   1 
ATOM   4785 C CB  . PRO B 1 171 ? -10.154 -19.972 13.130  1.00 192.78 ? 171 PRO B CB  1 
ATOM   4786 C CG  . PRO B 1 171 ? -9.516  -20.692 14.304  1.00 191.13 ? 171 PRO B CG  1 
ATOM   4787 C CD  . PRO B 1 171 ? -10.627 -20.948 15.314  1.00 189.68 ? 171 PRO B CD  1 
ATOM   4788 N N   . GLY B 1 172 ? -12.968 -18.478 12.159  1.00 150.02 ? 172 GLY B N   1 
ATOM   4789 C CA  . GLY B 1 172 ? -14.195 -18.572 11.390  1.00 148.71 ? 172 GLY B CA  1 
ATOM   4790 C C   . GLY B 1 172 ? -14.288 -19.923 10.697  1.00 142.15 ? 172 GLY B C   1 
ATOM   4791 O O   . GLY B 1 172 ? -13.374 -20.280 9.960   1.00 141.52 ? 172 GLY B O   1 
ATOM   4792 N N   . GLY B 1 173 ? -15.365 -20.671 10.988  1.00 150.92 ? 173 GLY B N   1 
ATOM   4793 C CA  . GLY B 1 173 ? -15.625 -21.954 10.344  1.00 160.19 ? 173 GLY B CA  1 
ATOM   4794 C C   . GLY B 1 173 ? -16.824 -22.705 10.928  1.00 155.84 ? 173 GLY B C   1 
ATOM   4795 O O   . GLY B 1 173 ? -17.366 -22.303 11.954  1.00 173.54 ? 173 GLY B O   1 
ATOM   4796 N N   . THR B 1 174 ? -17.237 -23.797 10.268  1.00 154.26 ? 174 THR B N   1 
ATOM   4797 C CA  . THR B 1 174 ? -18.351 -24.592 10.767  1.00 155.75 ? 174 THR B CA  1 
ATOM   4798 C C   . THR B 1 174 ? -17.816 -25.627 11.735  1.00 160.96 ? 174 THR B C   1 
ATOM   4799 O O   . THR B 1 174 ? -16.610 -25.899 11.750  1.00 166.03 ? 174 THR B O   1 
ATOM   4800 C CB  . THR B 1 174 ? -19.072 -25.373 9.674   1.00 156.49 ? 174 THR B CB  1 
ATOM   4801 O OG1 . THR B 1 174 ? -18.644 -24.868 8.414   1.00 189.96 ? 174 THR B OG1 1 
ATOM   4802 C CG2 . THR B 1 174 ? -20.564 -25.468 9.937   1.00 139.32 ? 174 THR B CG2 1 
ATOM   4803 N N   . SER B 1 175 ? -18.764 -26.243 12.447  1.00 152.59 ? 175 SER B N   1 
ATOM   4804 C CA  . SER B 1 175 ? -18.450 -27.372 13.302  1.00 170.24 ? 175 SER B CA  1 
ATOM   4805 C C   . SER B 1 175 ? -19.137 -28.624 12.760  1.00 164.93 ? 175 SER B C   1 
ATOM   4806 O O   . SER B 1 175 ? -19.729 -29.386 13.527  1.00 174.25 ? 175 SER B O   1 
ATOM   4807 C CB  . SER B 1 175 ? -18.801 -27.092 14.742  1.00 193.25 ? 175 SER B CB  1 
ATOM   4808 O OG  . SER B 1 175 ? -20.107 -26.550 14.878  1.00 192.24 ? 175 SER B OG  1 
ATOM   4809 N N   . GLU B 1 176 ? -19.030 -28.803 11.447  1.00 160.80 ? 176 GLU B N   1 
ATOM   4810 C CA  . GLU B 1 176 ? -19.758 -29.825 10.718  1.00 173.47 ? 176 GLU B CA  1 
ATOM   4811 C C   . GLU B 1 176 ? -18.811 -30.588 9.798   1.00 157.99 ? 176 GLU B C   1 
ATOM   4812 O O   . GLU B 1 176 ? -18.058 -30.003 9.026   1.00 153.60 ? 176 GLU B O   1 
ATOM   4813 C CB  . GLU B 1 176 ? -20.918 -29.209 9.930   1.00 202.76 ? 176 GLU B CB  1 
ATOM   4814 C CG  . GLU B 1 176 ? -21.927 -30.233 9.418   1.00 231.76 ? 176 GLU B CG  1 
ATOM   4815 C CD  . GLU B 1 176 ? -22.665 -31.075 10.452  1.00 251.83 ? 176 GLU B CD  1 
ATOM   4816 O OE1 . GLU B 1 176 ? -23.339 -30.491 11.328  1.00 262.90 ? 176 GLU B OE1 1 
ATOM   4817 O OE2 . GLU B 1 176 ? -22.566 -32.321 10.382  1.00 249.59 ? 176 GLU B OE2 1 
ATOM   4818 N N   . VAL B 1 177 ? -18.875 -31.916 9.906   1.00 155.22 ? 177 VAL B N   1 
ATOM   4819 C CA  . VAL B 1 177 ? -18.188 -32.848 9.035   1.00 162.61 ? 177 VAL B CA  1 
ATOM   4820 C C   . VAL B 1 177 ? -18.621 -32.671 7.581   1.00 158.09 ? 177 VAL B C   1 
ATOM   4821 O O   . VAL B 1 177 ? -19.794 -32.405 7.277   1.00 211.74 ? 177 VAL B O   1 
ATOM   4822 C CB  . VAL B 1 177 ? -18.519 -34.285 9.477   1.00 179.82 ? 177 VAL B CB  1 
ATOM   4823 C CG1 . VAL B 1 177 ? -17.413 -35.235 9.064   1.00 183.01 ? 177 VAL B CG1 1 
ATOM   4824 C CG2 . VAL B 1 177 ? -18.801 -34.395 10.970  1.00 199.25 ? 177 VAL B CG2 1 
ATOM   4825 N N   . LEU B 1 178 ? -17.653 -32.913 6.694   1.00 128.71 ? 178 LEU B N   1 
ATOM   4826 C CA  . LEU B 1 178 ? -17.829 -32.765 5.253   1.00 142.10 ? 178 LEU B CA  1 
ATOM   4827 C C   . LEU B 1 178 ? -17.446 -34.055 4.512   1.00 157.51 ? 178 LEU B C   1 
ATOM   4828 O O   . LEU B 1 178 ? -16.339 -34.172 3.993   1.00 178.22 ? 178 LEU B O   1 
ATOM   4829 C CB  . LEU B 1 178 ? -17.053 -31.567 4.706   1.00 134.92 ? 178 LEU B CB  1 
ATOM   4830 C CG  . LEU B 1 178 ? -17.241 -30.220 5.411   1.00 135.20 ? 178 LEU B CG  1 
ATOM   4831 C CD1 . LEU B 1 178 ? -16.030 -29.329 5.175   1.00 149.20 ? 178 LEU B CD1 1 
ATOM   4832 C CD2 . LEU B 1 178 ? -18.478 -29.544 4.882   1.00 157.80 ? 178 LEU B CD2 1 
ATOM   4833 N N   . ARG B 1 179 ? -18.426 -34.958 4.424   1.00 180.05 ? 179 ARG B N   1 
ATOM   4834 C CA  . ARG B 1 179 ? -18.210 -36.305 3.926   1.00 170.67 ? 179 ARG B CA  1 
ATOM   4835 C C   . ARG B 1 179 ? -17.949 -36.298 2.414   1.00 178.60 ? 179 ARG B C   1 
ATOM   4836 O O   . ARG B 1 179 ? -17.704 -37.357 1.866   1.00 182.29 ? 179 ARG B O   1 
ATOM   4837 C CB  . ARG B 1 179 ? -19.262 -37.277 4.483   1.00 163.59 ? 179 ARG B CB  1 
ATOM   4838 C CG  . ARG B 1 179 ? -19.059 -37.458 5.982   1.00 157.52 ? 179 ARG B CG  1 
ATOM   4839 C CD  . ARG B 1 179 ? -19.927 -38.557 6.589   1.00 176.03 ? 179 ARG B CD  1 
ATOM   4840 N NE  . ARG B 1 179 ? -20.024 -38.472 8.055   1.00 207.64 ? 179 ARG B NE  1 
ATOM   4841 C CZ  . ARG B 1 179 ? -20.551 -37.479 8.788   1.00 224.93 ? 179 ARG B CZ  1 
ATOM   4842 N NH1 . ARG B 1 179 ? -21.115 -36.436 8.209   1.00 241.99 ? 179 ARG B NH1 1 
ATOM   4843 N NH2 . ARG B 1 179 ? -20.544 -37.541 10.108  1.00 211.67 ? 179 ARG B NH2 1 
ATOM   4844 N N   . SER B 1 180 ? -17.930 -35.132 1.746   1.00 178.14 ? 180 SER B N   1 
ATOM   4845 C CA  . SER B 1 180 ? -17.681 -35.101 0.309   1.00 179.06 ? 180 SER B CA  1 
ATOM   4846 C C   . SER B 1 180 ? -16.890 -33.863 -0.083  1.00 176.87 ? 180 SER B C   1 
ATOM   4847 O O   . SER B 1 180 ? -16.949 -32.849 0.612   1.00 196.47 ? 180 SER B O   1 
ATOM   4848 C CB  . SER B 1 180 ? -18.963 -35.176 -0.514  1.00 201.77 ? 180 SER B CB  1 
ATOM   4849 O OG  . SER B 1 180 ? -19.639 -33.927 -0.577  1.00 154.52 ? 180 SER B OG  1 
ATOM   4850 N N   . GLU B 1 181 ? -16.234 -33.951 -1.249  1.00 169.65 ? 181 GLU B N   1 
ATOM   4851 C CA  . GLU B 1 181 ? -15.431 -32.860 -1.768  1.00 167.00 ? 181 GLU B CA  1 
ATOM   4852 C C   . GLU B 1 181 ? -16.301 -31.639 -2.035  1.00 172.14 ? 181 GLU B C   1 
ATOM   4853 O O   . GLU B 1 181 ? -15.851 -30.523 -1.758  1.00 181.62 ? 181 GLU B O   1 
ATOM   4854 C CB  . GLU B 1 181 ? -14.659 -33.190 -3.044  1.00 161.11 ? 181 GLU B CB  1 
ATOM   4855 C CG  . GLU B 1 181 ? -13.734 -34.397 -2.956  1.00 169.97 ? 181 GLU B CG  1 
ATOM   4856 C CD  . GLU B 1 181 ? -12.550 -34.307 -3.923  1.00 187.80 ? 181 GLU B CD  1 
ATOM   4857 O OE1 . GLU B 1 181 ? -12.631 -33.934 -5.122  1.00 196.13 ? 181 GLU B OE1 1 
ATOM   4858 O OE2 . GLU B 1 181 ? -11.467 -34.643 -3.431  1.00 189.74 ? 181 GLU B OE2 1 
ATOM   4859 N N   . ALA B 1 182 ? -17.506 -31.867 -2.569  1.00 157.16 ? 182 ALA B N   1 
ATOM   4860 C CA  . ALA B 1 182 ? -18.425 -30.795 -2.900  1.00 177.74 ? 182 ALA B CA  1 
ATOM   4861 C C   . ALA B 1 182 ? -18.750 -29.965 -1.653  1.00 194.64 ? 182 ALA B C   1 
ATOM   4862 O O   . ALA B 1 182 ? -18.721 -28.721 -1.685  1.00 246.69 ? 182 ALA B O   1 
ATOM   4863 C CB  . ALA B 1 182 ? -19.666 -31.367 -3.548  1.00 214.63 ? 182 ALA B CB  1 
ATOM   4864 N N   . GLU B 1 183 ? -19.041 -30.700 -0.573  1.00 173.78 ? 183 GLU B N   1 
ATOM   4865 C CA  . GLU B 1 183 ? -19.387 -30.098 0.711   1.00 183.75 ? 183 GLU B CA  1 
ATOM   4866 C C   . GLU B 1 183 ? -18.244 -29.202 1.193   1.00 194.51 ? 183 GLU B C   1 
ATOM   4867 O O   . GLU B 1 183 ? -18.457 -28.060 1.636   1.00 208.13 ? 183 GLU B O   1 
ATOM   4868 C CB  . GLU B 1 183 ? -19.708 -31.164 1.763   1.00 176.98 ? 183 GLU B CB  1 
ATOM   4869 C CG  . GLU B 1 183 ? -20.978 -31.960 1.472   1.00 194.28 ? 183 GLU B CG  1 
ATOM   4870 C CD  . GLU B 1 183 ? -21.215 -33.166 2.373   1.00 188.61 ? 183 GLU B CD  1 
ATOM   4871 O OE1 . GLU B 1 183 ? -20.271 -33.962 2.507   1.00 189.19 ? 183 GLU B OE1 1 
ATOM   4872 O OE2 . GLU B 1 183 ? -22.333 -33.345 2.902   1.00 189.41 ? 183 GLU B OE2 1 
ATOM   4873 N N   . VAL B 1 184 ? -17.034 -29.763 1.089   1.00 189.16 ? 184 VAL B N   1 
ATOM   4874 C CA  . VAL B 1 184 ? -15.807 -29.090 1.503   1.00 180.90 ? 184 VAL B CA  1 
ATOM   4875 C C   . VAL B 1 184 ? -15.657 -27.775 0.733   1.00 202.54 ? 184 VAL B C   1 
ATOM   4876 O O   . VAL B 1 184 ? -15.349 -26.732 1.307   1.00 252.45 ? 184 VAL B O   1 
ATOM   4877 C CB  . VAL B 1 184 ? -14.551 -29.964 1.296   1.00 159.76 ? 184 VAL B CB  1 
ATOM   4878 C CG1 . VAL B 1 184 ? -13.266 -29.206 1.593   1.00 151.92 ? 184 VAL B CG1 1 
ATOM   4879 C CG2 . VAL B 1 184 ? -14.584 -31.266 2.089   1.00 168.80 ? 184 VAL B CG2 1 
ATOM   4880 N N   . VAL B 1 185 ? -15.873 -27.869 -0.573  1.00 183.72 ? 185 VAL B N   1 
ATOM   4881 C CA  . VAL B 1 185 ? -15.743 -26.725 -1.463  1.00 169.37 ? 185 VAL B CA  1 
ATOM   4882 C C   . VAL B 1 185 ? -16.734 -25.634 -1.067  1.00 181.36 ? 185 VAL B C   1 
ATOM   4883 O O   . VAL B 1 185 ? -16.371 -24.453 -1.004  1.00 166.10 ? 185 VAL B O   1 
ATOM   4884 C CB  . VAL B 1 185 ? -15.644 -27.059 -2.957  1.00 154.42 ? 185 VAL B CB  1 
ATOM   4885 C CG1 . VAL B 1 185 ? -15.671 -25.806 -3.816  1.00 153.03 ? 185 VAL B CG1 1 
ATOM   4886 C CG2 . VAL B 1 185 ? -14.368 -27.846 -3.226  1.00 115.51 ? 185 VAL B CG2 1 
ATOM   4887 N N   . GLU B 1 186 ? -17.967 -26.062 -0.777  1.00 199.50 ? 186 GLU B N   1 
ATOM   4888 C CA  . GLU B 1 186 ? -19.039 -25.165 -0.345  1.00 197.73 ? 186 GLU B CA  1 
ATOM   4889 C C   . GLU B 1 186 ? -18.593 -24.409 0.912   1.00 213.04 ? 186 GLU B C   1 
ATOM   4890 O O   . GLU B 1 186 ? -18.511 -23.193 0.862   1.00 229.38 ? 186 GLU B O   1 
ATOM   4891 C CB  . GLU B 1 186 ? -20.412 -25.844 -0.251  1.00 191.10 ? 186 GLU B CB  1 
ATOM   4892 C CG  . GLU B 1 186 ? -21.261 -25.361 0.923   1.00 211.11 ? 186 GLU B CG  1 
ATOM   4893 C CD  . GLU B 1 186 ? -21.739 -26.458 1.863   1.00 228.59 ? 186 GLU B CD  1 
ATOM   4894 O OE1 . GLU B 1 186 ? -21.428 -27.637 1.604   1.00 220.87 ? 186 GLU B OE1 1 
ATOM   4895 O OE2 . GLU B 1 186 ? -22.435 -26.167 2.857   1.00 238.67 ? 186 GLU B OE2 1 
ATOM   4896 N N   . ALA B 1 187 ? -18.062 -25.181 1.860   1.00 199.60 ? 187 ALA B N   1 
ATOM   4897 C CA  . ALA B 1 187 ? -17.589 -24.656 3.132   1.00 192.88 ? 187 ALA B CA  1 
ATOM   4898 C C   . ALA B 1 187 ? -16.515 -23.586 2.914   1.00 188.71 ? 187 ALA B C   1 
ATOM   4899 O O   . ALA B 1 187 ? -16.530 -22.515 3.517   1.00 208.62 ? 187 ALA B O   1 
ATOM   4900 C CB  . ALA B 1 187 ? -17.063 -25.784 4.019   1.00 178.77 ? 187 ALA B CB  1 
ATOM   4901 N N   . ILE B 1 188 ? -15.590 -23.922 2.024   1.00 161.87 ? 188 ILE B N   1 
ATOM   4902 C CA  . ILE B 1 188 ? -14.456 -23.086 1.667   1.00 162.23 ? 188 ILE B CA  1 
ATOM   4903 C C   . ILE B 1 188 ? -14.974 -21.767 1.106   1.00 175.99 ? 188 ILE B C   1 
ATOM   4904 O O   . ILE B 1 188 ? -14.438 -20.711 1.413   1.00 168.99 ? 188 ILE B O   1 
ATOM   4905 C CB  . ILE B 1 188 ? -13.513 -23.828 0.691   1.00 150.39 ? 188 ILE B CB  1 
ATOM   4906 C CG1 . ILE B 1 188 ? -12.749 -24.976 1.379   1.00 126.63 ? 188 ILE B CG1 1 
ATOM   4907 C CG2 . ILE B 1 188 ? -12.539 -22.873 0.002   1.00 159.52 ? 188 ILE B CG2 1 
ATOM   4908 C CD1 . ILE B 1 188 ? -11.681 -25.629 0.522   1.00 119.88 ? 188 ILE B CD1 1 
ATOM   4909 N N   . HIS B 1 189 ? -15.986 -21.844 0.232   1.00 182.04 ? 189 HIS B N   1 
ATOM   4910 C CA  . HIS B 1 189 ? -16.478 -20.628 -0.398  1.00 176.64 ? 189 HIS B CA  1 
ATOM   4911 C C   . HIS B 1 189 ? -17.147 -19.753 0.674   1.00 160.92 ? 189 HIS B C   1 
ATOM   4912 O O   . HIS B 1 189 ? -16.954 -18.534 0.753   1.00 165.81 ? 189 HIS B O   1 
ATOM   4913 C CB  . HIS B 1 189 ? -17.132 -20.971 -1.737  1.00 187.97 ? 189 HIS B CB  1 
ATOM   4914 C CG  . HIS B 1 189 ? -16.123 -21.455 -2.737  1.00 187.25 ? 189 HIS B CG  1 
ATOM   4915 N ND1 . HIS B 1 189 ? -14.861 -21.907 -2.411  1.00 181.00 ? 189 HIS B ND1 1 
ATOM   4916 C CD2 . HIS B 1 189 ? -16.183 -21.491 -4.080  1.00 180.50 ? 189 HIS B CD2 1 
ATOM   4917 C CE1 . HIS B 1 189 ? -14.211 -22.224 -3.525  1.00 167.45 ? 189 HIS B CE1 1 
ATOM   4918 N NE2 . HIS B 1 189 ? -14.997 -21.990 -4.549  1.00 154.05 ? 189 HIS B NE2 1 
ATOM   4919 N N   . ARG B 1 190 ? -17.894 -20.431 1.559   1.00 138.40 ? 190 ARG B N   1 
ATOM   4920 C CA  . ARG B 1 190 ? -18.566 -19.787 2.675   1.00 144.80 ? 190 ARG B CA  1 
ATOM   4921 C C   . ARG B 1 190 ? -17.553 -19.387 3.747   1.00 148.48 ? 190 ARG B C   1 
ATOM   4922 O O   . ARG B 1 190 ? -17.558 -19.943 4.846   1.00 148.56 ? 190 ARG B O   1 
ATOM   4923 C CB  . ARG B 1 190 ? -19.653 -20.709 3.240   1.00 151.15 ? 190 ARG B CB  1 
ATOM   4924 C CG  . ARG B 1 190 ? -20.450 -20.138 4.409   1.00 174.62 ? 190 ARG B CG  1 
ATOM   4925 C CD  . ARG B 1 190 ? -21.766 -20.851 4.685   1.00 181.13 ? 190 ARG B CD  1 
ATOM   4926 N NE  . ARG B 1 190 ? -21.547 -22.256 5.037   1.00 188.15 ? 190 ARG B NE  1 
ATOM   4927 C CZ  . ARG B 1 190 ? -21.672 -23.290 4.205   1.00 188.17 ? 190 ARG B CZ  1 
ATOM   4928 N NH1 . ARG B 1 190 ? -22.009 -23.101 2.941   1.00 177.97 ? 190 ARG B NH1 1 
ATOM   4929 N NH2 . ARG B 1 190 ? -21.455 -24.514 4.653   1.00 188.26 ? 190 ARG B NH2 1 
ATOM   4930 N N   . LEU B 1 191 ? -16.698 -18.406 3.445   1.00 150.59 ? 191 LEU B N   1 
ATOM   4931 C CA  . LEU B 1 191 ? -15.646 -18.116 4.404   1.00 169.46 ? 191 LEU B CA  1 
ATOM   4932 C C   . LEU B 1 191 ? -15.440 -16.615 4.534   1.00 172.48 ? 191 LEU B C   1 
ATOM   4933 O O   . LEU B 1 191 ? -15.807 -15.857 3.636   1.00 166.16 ? 191 LEU B O   1 
ATOM   4934 C CB  . LEU B 1 191 ? -14.365 -18.861 4.046   1.00 174.11 ? 191 LEU B CB  1 
ATOM   4935 C CG  . LEU B 1 191 ? -13.659 -19.574 5.199   1.00 167.06 ? 191 LEU B CG  1 
ATOM   4936 C CD1 . LEU B 1 191 ? -14.659 -20.444 5.941   1.00 150.30 ? 191 LEU B CD1 1 
ATOM   4937 C CD2 . LEU B 1 191 ? -12.543 -20.409 4.625   1.00 158.45 ? 191 LEU B CD2 1 
ATOM   4938 N N   . SER B 1 192 ? -14.827 -16.228 5.662   1.00 187.98 ? 192 SER B N   1 
ATOM   4939 C CA  . SER B 1 192 ? -14.862 -14.874 6.194   1.00 213.27 ? 192 SER B CA  1 
ATOM   4940 C C   . SER B 1 192 ? -14.015 -13.935 5.340   1.00 200.91 ? 192 SER B C   1 
ATOM   4941 O O   . SER B 1 192 ? -14.077 -12.716 5.492   1.00 210.13 ? 192 SER B O   1 
ATOM   4942 C CB  . SER B 1 192 ? -14.402 -14.859 7.631   1.00 208.52 ? 192 SER B CB  1 
ATOM   4943 O OG  . SER B 1 192 ? -15.005 -15.899 8.391   1.00 200.69 ? 192 SER B OG  1 
ATOM   4944 N N   . CYS B 1 193 ? -13.240 -14.527 4.427   1.00 187.53 ? 193 CYS B N   1 
ATOM   4945 C CA  . CYS B 1 193 ? -12.194 -13.807 3.725   1.00 199.43 ? 193 CYS B CA  1 
ATOM   4946 C C   . CYS B 1 193 ? -11.494 -12.895 4.725   1.00 216.28 ? 193 CYS B C   1 
ATOM   4947 O O   . CYS B 1 193 ? -11.043 -13.344 5.785   1.00 222.30 ? 193 CYS B O   1 
ATOM   4948 C CB  . CYS B 1 193 ? -12.752 -13.067 2.514   1.00 161.51 ? 193 CYS B CB  1 
ATOM   4949 S SG  . CYS B 1 193 ? -13.194 -14.216 1.186   1.00 186.40 ? 193 CYS B SG  1 
ATOM   4950 N N   . GLY B 1 194 ? -11.461 -11.606 4.379   1.00 225.97 ? 194 GLY B N   1 
ATOM   4951 C CA  . GLY B 1 194 ? -10.660 -10.634 5.094   1.00 228.85 ? 194 GLY B CA  1 
ATOM   4952 C C   . GLY B 1 194 ? -9.356  -10.375 4.344   1.00 245.77 ? 194 GLY B C   1 
ATOM   4953 O O   . GLY B 1 194 ? -8.912  -11.195 3.533   1.00 251.03 ? 194 GLY B O   1 
ATOM   4954 N N   . THR B 1 195 ? -8.751  -9.227  4.641   1.00 249.23 ? 195 THR B N   1 
ATOM   4955 C CA  . THR B 1 195 ? -7.483  -8.859  4.037   1.00 244.11 ? 195 THR B CA  1 
ATOM   4956 C C   . THR B 1 195 ? -6.511  -10.023 4.211   1.00 228.18 ? 195 THR B C   1 
ATOM   4957 O O   . THR B 1 195 ? -6.284  -10.479 5.330   1.00 215.96 ? 195 THR B O   1 
ATOM   4958 C CB  . THR B 1 195 ? -6.965  -7.570  4.672   1.00 252.34 ? 195 THR B CB  1 
ATOM   4959 O OG1 . THR B 1 195 ? -6.713  -7.925  6.029   1.00 238.40 ? 195 THR B OG1 1 
ATOM   4960 C CG2 . THR B 1 195 ? -7.958  -6.423  4.571   1.00 250.11 ? 195 THR B CG2 1 
ATOM   4961 N N   . ALA B 1 196 ? -5.994  -10.524 3.082   1.00 225.54 ? 196 ALA B N   1 
ATOM   4962 C CA  . ALA B 1 196 ? -5.101  -11.669 3.060   1.00 234.41 ? 196 ALA B CA  1 
ATOM   4963 C C   . ALA B 1 196 ? -4.278  -11.642 1.775   1.00 257.85 ? 196 ALA B C   1 
ATOM   4964 O O   . ALA B 1 196 ? -4.817  -11.819 0.683   1.00 262.56 ? 196 ALA B O   1 
ATOM   4965 C CB  . ALA B 1 196 ? -5.892  -12.954 3.208   1.00 208.04 ? 196 ALA B CB  1 
ATOM   4966 N N   . ALA B 1 197 ? -2.970  -11.398 1.930   1.00 276.67 ? 197 ALA B N   1 
ATOM   4967 C CA  . ALA B 1 197 ? -2.038  -11.359 0.814   1.00 272.49 ? 197 ALA B CA  1 
ATOM   4968 C C   . ALA B 1 197 ? -2.344  -12.520 -0.126  1.00 255.49 ? 197 ALA B C   1 
ATOM   4969 O O   . ALA B 1 197 ? -2.554  -12.327 -1.320  1.00 259.29 ? 197 ALA B O   1 
ATOM   4970 C CB  . ALA B 1 197 ? -0.612  -11.415 1.324   1.00 272.48 ? 197 ALA B CB  1 
ATOM   4971 N N   . ALA B 1 198 ? -2.415  -13.722 0.453   1.00 229.96 ? 198 ALA B N   1 
ATOM   4972 C CA  . ALA B 1 198 ? -2.719  -14.932 -0.288  1.00 237.39 ? 198 ALA B CA  1 
ATOM   4973 C C   . ALA B 1 198 ? -3.838  -15.695 0.418   1.00 232.83 ? 198 ALA B C   1 
ATOM   4974 O O   . ALA B 1 198 ? -3.576  -16.686 1.101   1.00 281.87 ? 198 ALA B O   1 
ATOM   4975 C CB  . ALA B 1 198 ? -1.457  -15.761 -0.423  1.00 242.02 ? 198 ALA B CB  1 
ATOM   4976 N N   . ARG B 1 199 ? -5.075  -15.217 0.232   1.00 202.58 ? 199 ARG B N   1 
ATOM   4977 C CA  . ARG B 1 199 ? -6.266  -15.735 0.884   1.00 195.10 ? 199 ARG B CA  1 
ATOM   4978 C C   . ARG B 1 199 ? -6.303  -17.261 0.798   1.00 189.91 ? 199 ARG B C   1 
ATOM   4979 O O   . ARG B 1 199 ? -6.192  -17.826 -0.278  1.00 146.20 ? 199 ARG B O   1 
ATOM   4980 C CB  . ARG B 1 199 ? -7.480  -15.021 0.281   1.00 184.76 ? 199 ARG B CB  1 
ATOM   4981 C CG  . ARG B 1 199 ? -7.117  -14.443 -1.079  1.00 190.36 ? 199 ARG B CG  1 
ATOM   4982 C CD  . ARG B 1 199 ? -8.331  -13.946 -1.855  1.00 212.13 ? 199 ARG B CD  1 
ATOM   4983 N NE  . ARG B 1 199 ? -9.136  -15.101 -2.275  1.00 247.37 ? 199 ARG B NE  1 
ATOM   4984 C CZ  . ARG B 1 199 ? -9.587  -15.391 -3.490  1.00 261.07 ? 199 ARG B CZ  1 
ATOM   4985 N NH1 . ARG B 1 199 ? -10.110 -16.587 -3.720  1.00 246.26 ? 199 ARG B NH1 1 
ATOM   4986 N NH2 . ARG B 1 199 ? -9.464  -14.515 -4.471  1.00 288.73 ? 199 ARG B NH2 1 
ATOM   4987 N N   . ARG B 1 200 ? -6.450  -17.900 1.963   1.00 195.04 ? 200 ARG B N   1 
ATOM   4988 C CA  . ARG B 1 200 ? -6.296  -19.327 2.125   1.00 155.87 ? 200 ARG B CA  1 
ATOM   4989 C C   . ARG B 1 200 ? -7.398  -19.896 3.015   1.00 162.34 ? 200 ARG B C   1 
ATOM   4990 O O   . ARG B 1 200 ? -7.954  -19.293 3.951   1.00 164.19 ? 200 ARG B O   1 
ATOM   4991 C CB  . ARG B 1 200 ? -4.916  -19.771 2.625   1.00 152.79 ? 200 ARG B CB  1 
ATOM   4992 C CG  . ARG B 1 200 ? -3.875  -19.950 1.528   1.00 166.93 ? 200 ARG B CG  1 
ATOM   4993 C CD  . ARG B 1 200 ? -2.450  -20.272 1.971   1.00 180.67 ? 200 ARG B CD  1 
ATOM   4994 N NE  . ARG B 1 200 ? -1.699  -19.017 2.061   1.00 176.44 ? 200 ARG B NE  1 
ATOM   4995 C CZ  . ARG B 1 200 ? -0.500  -18.856 2.592   1.00 188.75 ? 200 ARG B CZ  1 
ATOM   4996 N NH1 . ARG B 1 200 ? 0.204   -19.906 2.979   1.00 194.16 ? 200 ARG B NH1 1 
ATOM   4997 N NH2 . ARG B 1 200 ? -0.008  -17.634 2.706   1.00 229.65 ? 200 ARG B NH2 1 
ATOM   4998 N N   . ALA B 1 201 ? -7.622  -21.187 2.775   1.00 161.43 ? 201 ALA B N   1 
ATOM   4999 C CA  . ALA B 1 201 ? -8.508  -22.051 3.540   1.00 143.64 ? 201 ALA B CA  1 
ATOM   5000 C C   . ALA B 1 201 ? -7.783  -23.334 3.959   1.00 133.68 ? 201 ALA B C   1 
ATOM   5001 O O   . ALA B 1 201 ? -6.893  -23.860 3.247   1.00 127.19 ? 201 ALA B O   1 
ATOM   5002 C CB  . ALA B 1 201 ? -9.750  -22.343 2.728   1.00 146.16 ? 201 ALA B CB  1 
ATOM   5003 N N   . MET B 1 202 ? -8.210  -23.841 5.121   1.00 126.50 ? 202 MET B N   1 
ATOM   5004 C CA  . MET B 1 202 ? -7.614  -25.016 5.736   1.00 125.12 ? 202 MET B CA  1 
ATOM   5005 C C   . MET B 1 202 ? -8.685  -26.015 6.137   1.00 130.39 ? 202 MET B C   1 
ATOM   5006 O O   . MET B 1 202 ? -9.650  -25.685 6.798   1.00 144.95 ? 202 MET B O   1 
ATOM   5007 C CB  . MET B 1 202 ? -6.801  -24.638 6.970   1.00 125.87 ? 202 MET B CB  1 
ATOM   5008 C CG  . MET B 1 202 ? -5.599  -25.531 7.187   1.00 144.84 ? 202 MET B CG  1 
ATOM   5009 S SD  . MET B 1 202 ? -5.474  -25.710 8.978   1.00 180.07 ? 202 MET B SD  1 
ATOM   5010 C CE  . MET B 1 202 ? -4.673  -24.151 9.383   1.00 162.99 ? 202 MET B CE  1 
ATOM   5011 N N   . VAL B 1 203 ? -8.457  -27.268 5.725   1.00 138.83 ? 203 VAL B N   1 
ATOM   5012 C CA  . VAL B 1 203 ? -9.400  -28.372 5.871   1.00 148.13 ? 203 VAL B CA  1 
ATOM   5013 C C   . VAL B 1 203 ? -8.816  -29.429 6.800   1.00 121.80 ? 203 VAL B C   1 
ATOM   5014 O O   . VAL B 1 203 ? -7.825  -30.021 6.414   1.00 120.51 ? 203 VAL B O   1 
ATOM   5015 C CB  . VAL B 1 203 ? -9.542  -29.035 4.477   1.00 156.74 ? 203 VAL B CB  1 
ATOM   5016 C CG1 . VAL B 1 203 ? -10.367 -30.322 4.513   1.00 153.28 ? 203 VAL B CG1 1 
ATOM   5017 C CG2 . VAL B 1 203 ? -10.031 -28.087 3.386   1.00 163.60 ? 203 VAL B CG2 1 
ATOM   5018 N N   . LYS B 1 204 ? -9.462  -29.689 7.952   1.00 116.90 ? 204 LYS B N   1 
ATOM   5019 C CA  . LYS B 1 204 ? -8.870  -30.503 8.999   1.00 126.59 ? 204 LYS B CA  1 
ATOM   5020 C C   . LYS B 1 204 ? -9.690  -31.771 9.198   1.00 130.24 ? 204 LYS B C   1 
ATOM   5021 O O   . LYS B 1 204 ? -10.831 -31.659 9.612   1.00 167.54 ? 204 LYS B O   1 
ATOM   5022 C CB  . LYS B 1 204 ? -8.879  -29.723 10.325  1.00 136.48 ? 204 LYS B CB  1 
ATOM   5023 C CG  . LYS B 1 204 ? -8.020  -28.468 10.482  1.00 121.07 ? 204 LYS B CG  1 
ATOM   5024 C CD  . LYS B 1 204 ? -7.948  -28.187 11.984  1.00 124.75 ? 204 LYS B CD  1 
ATOM   5025 C CE  . LYS B 1 204 ? -7.033  -27.081 12.358  1.00 129.86 ? 204 LYS B CE  1 
ATOM   5026 N NZ  . LYS B 1 204 ? -7.443  -25.836 11.702  1.00 137.13 ? 204 LYS B NZ  1 
ATOM   5027 N N   . LEU B 1 205 ? -9.101  -32.928 8.885   1.00 126.79 ? 205 LEU B N   1 
ATOM   5028 C CA  . LEU B 1 205 ? -9.789  -34.202 8.921   1.00 142.99 ? 205 LEU B CA  1 
ATOM   5029 C C   . LEU B 1 205 ? -10.263 -34.496 10.343  1.00 153.39 ? 205 LEU B C   1 
ATOM   5030 O O   . LEU B 1 205 ? -9.500  -34.422 11.305  1.00 151.51 ? 205 LEU B O   1 
ATOM   5031 C CB  . LEU B 1 205 ? -8.881  -35.293 8.361   1.00 137.64 ? 205 LEU B CB  1 
ATOM   5032 C CG  . LEU B 1 205 ? -8.453  -35.113 6.899   1.00 128.15 ? 205 LEU B CG  1 
ATOM   5033 C CD1 . LEU B 1 205 ? -7.379  -36.087 6.522   1.00 107.29 ? 205 LEU B CD1 1 
ATOM   5034 C CD2 . LEU B 1 205 ? -9.625  -35.271 5.945   1.00 135.99 ? 205 LEU B CD2 1 
ATOM   5035 N N   . ASP B 1 206 ? -11.546 -34.855 10.467  1.00 156.01 ? 206 ASP B N   1 
ATOM   5036 C CA  . ASP B 1 206 ? -12.290 -34.783 11.725  1.00 163.57 ? 206 ASP B CA  1 
ATOM   5037 C C   . ASP B 1 206 ? -11.795 -35.766 12.789  1.00 157.17 ? 206 ASP B C   1 
ATOM   5038 O O   . ASP B 1 206 ? -11.831 -35.462 13.985  1.00 152.58 ? 206 ASP B O   1 
ATOM   5039 C CB  . ASP B 1 206 ? -13.797 -34.904 11.523  1.00 184.98 ? 206 ASP B CB  1 
ATOM   5040 C CG  . ASP B 1 206 ? -14.643 -34.797 12.791  1.00 200.57 ? 206 ASP B CG  1 
ATOM   5041 O OD1 . ASP B 1 206 ? -14.503 -33.788 13.516  1.00 200.57 ? 206 ASP B OD1 1 
ATOM   5042 O OD2 . ASP B 1 206 ? -15.429 -35.733 13.058  1.00 208.47 ? 206 ASP B OD2 1 
ATOM   5043 N N   . ALA B 1 207 ? -11.351 -36.950 12.354  1.00 155.44 ? 207 ALA B N   1 
ATOM   5044 C CA  . ALA B 1 207 ? -10.918 -38.005 13.260  1.00 163.22 ? 207 ALA B CA  1 
ATOM   5045 C C   . ALA B 1 207 ? -9.814  -37.515 14.204  1.00 163.24 ? 207 ALA B C   1 
ATOM   5046 O O   . ALA B 1 207 ? -9.063  -36.603 13.859  1.00 143.80 ? 207 ALA B O   1 
ATOM   5047 C CB  . ALA B 1 207 ? -10.469 -39.205 12.460  1.00 163.20 ? 207 ALA B CB  1 
ATOM   5048 N N   . ILE B 1 208 ? -9.726  -38.135 15.395  1.00 179.73 ? 208 ILE B N   1 
ATOM   5049 C CA  . ILE B 1 208 ? -8.694  -37.823 16.381  1.00 176.51 ? 208 ILE B CA  1 
ATOM   5050 C C   . ILE B 1 208 ? -7.445  -38.657 16.093  1.00 183.83 ? 208 ILE B C   1 
ATOM   5051 O O   . ILE B 1 208 ? -6.358  -38.351 16.584  1.00 186.60 ? 208 ILE B O   1 
ATOM   5052 C CB  . ILE B 1 208 ? -9.190  -37.938 17.848  1.00 173.35 ? 208 ILE B CB  1 
ATOM   5053 C CG1 . ILE B 1 208 ? -8.466  -38.997 18.697  1.00 156.31 ? 208 ILE B CG1 1 
ATOM   5054 C CG2 . ILE B 1 208 ? -10.720 -38.027 17.950  1.00 188.54 ? 208 ILE B CG2 1 
ATOM   5055 C CD1 . ILE B 1 208 ? -8.125  -38.536 20.112  1.00 153.72 ? 208 ILE B CD1 1 
ATOM   5056 N N   . THR B 1 209 ? -7.628  -39.697 15.270  1.00 194.14 ? 209 THR B N   1 
ATOM   5057 C CA  . THR B 1 209 ? -6.565  -40.548 14.760  1.00 189.96 ? 209 THR B CA  1 
ATOM   5058 C C   . THR B 1 209 ? -5.569  -39.698 13.974  1.00 195.08 ? 209 THR B C   1 
ATOM   5059 O O   . THR B 1 209 ? -4.396  -40.047 13.888  1.00 222.26 ? 209 THR B O   1 
ATOM   5060 C CB  . THR B 1 209 ? -7.176  -41.624 13.862  1.00 191.29 ? 209 THR B CB  1 
ATOM   5061 O OG1 . THR B 1 209 ? -7.154  -41.073 12.545  1.00 203.71 ? 209 THR B OG1 1 
ATOM   5062 C CG2 . THR B 1 209 ? -8.561  -42.061 14.316  1.00 180.04 ? 209 THR B CG2 1 
ATOM   5063 N N   . TRP B 1 210 ? -6.051  -38.590 13.402  1.00 179.33 ? 210 TRP B N   1 
ATOM   5064 C CA  . TRP B 1 210 ? -5.279  -37.724 12.530  1.00 182.52 ? 210 TRP B CA  1 
ATOM   5065 C C   . TRP B 1 210 ? -4.671  -36.548 13.293  1.00 216.78 ? 210 TRP B C   1 
ATOM   5066 O O   . TRP B 1 210 ? -4.333  -35.535 12.680  1.00 240.29 ? 210 TRP B O   1 
ATOM   5067 C CB  . TRP B 1 210 ? -6.189  -37.216 11.406  1.00 197.26 ? 210 TRP B CB  1 
ATOM   5068 C CG  . TRP B 1 210 ? -6.171  -38.067 10.169  1.00 187.36 ? 210 TRP B CG  1 
ATOM   5069 C CD1 . TRP B 1 210 ? -7.182  -38.224 9.277   1.00 185.41 ? 210 TRP B CD1 1 
ATOM   5070 C CD2 . TRP B 1 210 ? -5.078  -38.868 9.677   1.00 188.81 ? 210 TRP B CD2 1 
ATOM   5071 N NE1 . TRP B 1 210 ? -6.786  -39.027 8.244   1.00 197.21 ? 210 TRP B NE1 1 
ATOM   5072 C CE2 . TRP B 1 210 ? -5.507  -39.450 8.464   1.00 187.98 ? 210 TRP B CE2 1 
ATOM   5073 C CE3 . TRP B 1 210 ? -3.784  -39.136 10.130  1.00 214.40 ? 210 TRP B CE3 1 
ATOM   5074 C CZ2 . TRP B 1 210 ? -4.701  -40.300 7.706   1.00 215.59 ? 210 TRP B CZ2 1 
ATOM   5075 C CZ3 . TRP B 1 210 ? -3.000  -39.995 9.397   1.00 247.29 ? 210 TRP B CZ3 1 
ATOM   5076 C CH2 . TRP B 1 210 ? -3.437  -40.541 8.189   1.00 248.98 ? 210 TRP B CH2 1 
ATOM   5077 N N   . ALA B 1 211 ? -4.526  -36.704 14.617  1.00 242.94 ? 211 ALA B N   1 
ATOM   5078 C CA  . ALA B 1 211 ? -4.149  -35.596 15.483  1.00 254.09 ? 211 ALA B CA  1 
ATOM   5079 C C   . ALA B 1 211 ? -2.919  -34.876 14.933  1.00 236.65 ? 211 ALA B C   1 
ATOM   5080 O O   . ALA B 1 211 ? -2.075  -35.479 14.260  1.00 181.27 ? 211 ALA B O   1 
ATOM   5081 C CB  . ALA B 1 211 ? -3.968  -36.047 16.916  1.00 240.50 ? 211 ALA B CB  1 
ATOM   5082 N N   . ALA B 1 212 ? -2.855  -33.567 15.213  1.00 230.74 ? 212 ALA B N   1 
ATOM   5083 C CA  . ALA B 1 212 ? -1.793  -32.717 14.697  1.00 198.63 ? 212 ALA B CA  1 
ATOM   5084 C C   . ALA B 1 212 ? -1.814  -32.745 13.171  1.00 179.87 ? 212 ALA B C   1 
ATOM   5085 O O   . ALA B 1 212 ? -2.877  -32.904 12.555  1.00 187.10 ? 212 ALA B O   1 
ATOM   5086 C CB  . ALA B 1 212 ? -0.437  -33.137 15.244  1.00 180.54 ? 212 ALA B CB  1 
ATOM   5087 N N   . SER B 1 213 ? -0.627  -32.593 12.573  1.00 161.45 ? 213 SER B N   1 
ATOM   5088 C CA  . SER B 1 213 ? -0.565  -32.189 11.177  1.00 189.78 ? 213 SER B CA  1 
ATOM   5089 C C   . SER B 1 213 ? -0.314  -33.358 10.230  1.00 188.65 ? 213 SER B C   1 
ATOM   5090 O O   . SER B 1 213 ? 0.739   -33.437 9.601   1.00 191.10 ? 213 SER B O   1 
ATOM   5091 C CB  . SER B 1 213 ? 0.448   -31.111 10.938  1.00 235.83 ? 213 SER B CB  1 
ATOM   5092 O OG  . SER B 1 213 ? 0.474   -30.836 9.545   1.00 278.64 ? 213 SER B OG  1 
ATOM   5093 N N   . ILE B 1 214 ? -1.286  -34.259 10.094  1.00 170.59 ? 214 ILE B N   1 
ATOM   5094 C CA  . ILE B 1 214 ? -1.301  -35.138 8.940   1.00 161.37 ? 214 ILE B CA  1 
ATOM   5095 C C   . ILE B 1 214 ? -2.642  -34.861 8.297   1.00 158.20 ? 214 ILE B C   1 
ATOM   5096 O O   . ILE B 1 214 ? -2.769  -34.894 7.072   1.00 150.34 ? 214 ILE B O   1 
ATOM   5097 C CB  . ILE B 1 214 ? -1.155  -36.615 9.353   1.00 165.13 ? 214 ILE B CB  1 
ATOM   5098 C CG1 . ILE B 1 214 ? -0.083  -36.778 10.442  1.00 172.52 ? 214 ILE B CG1 1 
ATOM   5099 C CG2 . ILE B 1 214 ? -0.893  -37.507 8.133   1.00 165.69 ? 214 ILE B CG2 1 
ATOM   5100 C CD1 . ILE B 1 214 ? 0.215   -38.206 10.882  1.00 173.86 ? 214 ILE B CD1 1 
ATOM   5101 N N   . GLY B 1 215 ? -3.595  -34.555 9.195   1.00 168.10 ? 215 GLY B N   1 
ATOM   5102 C CA  . GLY B 1 215 ? -4.987  -34.296 8.883   1.00 175.77 ? 215 GLY B CA  1 
ATOM   5103 C C   . GLY B 1 215 ? -5.143  -32.938 8.215   1.00 180.05 ? 215 GLY B C   1 
ATOM   5104 O O   . GLY B 1 215 ? -5.648  -32.853 7.092   1.00 205.63 ? 215 GLY B O   1 
ATOM   5105 N N   . ASN B 1 216 ? -4.678  -31.900 8.927   1.00 173.76 ? 216 ASN B N   1 
ATOM   5106 C CA  . ASN B 1 216 ? -4.786  -30.521 8.459   1.00 135.35 ? 216 ASN B CA  1 
ATOM   5107 C C   . ASN B 1 216 ? -4.203  -30.406 7.057   1.00 120.74 ? 216 ASN B C   1 
ATOM   5108 O O   . ASN B 1 216 ? -3.065  -30.770 6.824   1.00 128.20 ? 216 ASN B O   1 
ATOM   5109 C CB  . ASN B 1 216 ? -4.137  -29.544 9.438   1.00 123.24 ? 216 ASN B CB  1 
ATOM   5110 C CG  . ASN B 1 216 ? -4.574  -29.769 10.871  1.00 144.91 ? 216 ASN B CG  1 
ATOM   5111 O OD1 . ASN B 1 216 ? -5.394  -30.650 11.151  1.00 191.44 ? 216 ASN B OD1 1 
ATOM   5112 N ND2 . ASN B 1 216 ? -4.033  -29.003 11.806  1.00 123.33 ? 216 ASN B ND2 1 
ATOM   5113 N N   . VAL B 1 217 ? -5.015  -29.903 6.119   1.00 113.43 ? 217 VAL B N   1 
ATOM   5114 C CA  . VAL B 1 217 ? -4.656  -29.709 4.729   1.00 112.79 ? 217 VAL B CA  1 
ATOM   5115 C C   . VAL B 1 217 ? -5.156  -28.322 4.331   1.00 124.55 ? 217 VAL B C   1 
ATOM   5116 O O   . VAL B 1 217 ? -6.314  -27.932 4.555   1.00 153.37 ? 217 VAL B O   1 
ATOM   5117 C CB  . VAL B 1 217 ? -5.107  -30.782 3.705   1.00 117.48 ? 217 VAL B CB  1 
ATOM   5118 C CG1 . VAL B 1 217 ? -4.906  -30.362 2.249   1.00 108.47 ? 217 VAL B CG1 1 
ATOM   5119 C CG2 . VAL B 1 217 ? -4.451  -32.141 3.938   1.00 129.26 ? 217 VAL B CG2 1 
ATOM   5120 N N   . LEU B 1 218 ? -4.297  -27.619 3.579   1.00 126.33 ? 218 LEU B N   1 
ATOM   5121 C CA  . LEU B 1 218 ? -4.438  -26.202 3.288   1.00 148.92 ? 218 LEU B CA  1 
ATOM   5122 C C   . LEU B 1 218 ? -4.477  -25.940 1.775   1.00 158.97 ? 218 LEU B C   1 
ATOM   5123 O O   . LEU B 1 218 ? -3.685  -26.471 1.006   1.00 161.14 ? 218 LEU B O   1 
ATOM   5124 C CB  . LEU B 1 218 ? -3.229  -25.551 3.958   1.00 150.63 ? 218 LEU B CB  1 
ATOM   5125 C CG  . LEU B 1 218 ? -2.968  -24.085 3.597   1.00 171.58 ? 218 LEU B CG  1 
ATOM   5126 C CD1 . LEU B 1 218 ? -3.770  -23.154 4.528   1.00 196.98 ? 218 LEU B CD1 1 
ATOM   5127 C CD2 . LEU B 1 218 ? -1.465  -23.769 3.511   1.00 140.70 ? 218 LEU B CD2 1 
ATOM   5128 N N   . ILE B 1 219 ? -5.476  -25.155 1.387   1.00 148.25 ? 219 ILE B N   1 
ATOM   5129 C CA  . ILE B 1 219 ? -5.803  -24.860 0.002   1.00 135.86 ? 219 ILE B CA  1 
ATOM   5130 C C   . ILE B 1 219 ? -5.971  -23.351 -0.165  1.00 128.47 ? 219 ILE B C   1 
ATOM   5131 O O   . ILE B 1 219 ? -6.743  -22.725 0.583   1.00 149.51 ? 219 ILE B O   1 
ATOM   5132 C CB  . ILE B 1 219 ? -7.080  -25.624 -0.424  1.00 143.23 ? 219 ILE B CB  1 
ATOM   5133 C CG1 . ILE B 1 219 ? -6.806  -27.080 -0.777  1.00 151.00 ? 219 ILE B CG1 1 
ATOM   5134 C CG2 . ILE B 1 219 ? -7.840  -24.929 -1.552  1.00 162.01 ? 219 ILE B CG2 1 
ATOM   5135 C CD1 . ILE B 1 219 ? -7.236  -28.047 0.314   1.00 133.54 ? 219 ILE B CD1 1 
ATOM   5136 N N   . ASP B 1 220 ? -5.280  -22.817 -1.190  1.00 116.94 ? 220 ASP B N   1 
ATOM   5137 C CA  . ASP B 1 220 ? -5.476  -21.420 -1.583  1.00 143.17 ? 220 ASP B CA  1 
ATOM   5138 C C   . ASP B 1 220 ? -6.664  -21.308 -2.531  1.00 144.35 ? 220 ASP B C   1 
ATOM   5139 O O   . ASP B 1 220 ? -6.651  -21.928 -3.598  1.00 131.94 ? 220 ASP B O   1 
ATOM   5140 C CB  . ASP B 1 220 ? -4.206  -20.719 -2.050  1.00 147.58 ? 220 ASP B CB  1 
ATOM   5141 C CG  . ASP B 1 220 ? -3.816  -20.886 -3.513  1.00 141.57 ? 220 ASP B CG  1 
ATOM   5142 O OD1 . ASP B 1 220 ? -3.457  -22.013 -3.880  1.00 148.93 ? 220 ASP B OD1 1 
ATOM   5143 O OD2 . ASP B 1 220 ? -3.880  -19.885 -4.274  1.00 146.96 ? 220 ASP B OD2 1 
ATOM   5144 N N   . ARG B 1 221 ? -7.665  -20.493 -2.143  1.00 127.35 ? 221 ARG B N   1 
ATOM   5145 C CA  . ARG B 1 221 ? -8.962  -20.488 -2.784  1.00 155.24 ? 221 ARG B CA  1 
ATOM   5146 C C   . ARG B 1 221 ? -8.891  -20.065 -4.241  1.00 171.92 ? 221 ARG B C   1 
ATOM   5147 O O   . ARG B 1 221 ? -9.766  -20.469 -5.002  1.00 204.73 ? 221 ARG B O   1 
ATOM   5148 C CB  . ARG B 1 221 ? -9.954  -19.614 -2.018  1.00 168.87 ? 221 ARG B CB  1 
ATOM   5149 C CG  . ARG B 1 221 ? -9.976  -19.902 -0.529  1.00 150.28 ? 221 ARG B CG  1 
ATOM   5150 C CD  . ARG B 1 221 ? -11.273 -19.308 -0.021  1.00 156.78 ? 221 ARG B CD  1 
ATOM   5151 N NE  . ARG B 1 221 ? -10.994 -18.735 1.295   1.00 160.86 ? 221 ARG B NE  1 
ATOM   5152 C CZ  . ARG B 1 221 ? -11.854 -17.971 1.952   1.00 181.86 ? 221 ARG B CZ  1 
ATOM   5153 N NH1 . ARG B 1 221 ? -13.079 -17.798 1.483   1.00 192.78 ? 221 ARG B NH1 1 
ATOM   5154 N NH2 . ARG B 1 221 ? -11.478 -17.422 3.096   1.00 213.24 ? 221 ARG B NH2 1 
ATOM   5155 N N   . ASP B 1 222 ? -7.864  -19.293 -4.610  1.00 157.53 ? 222 ASP B N   1 
ATOM   5156 C CA  . ASP B 1 222 ? -7.663  -18.819 -5.966  1.00 170.68 ? 222 ASP B CA  1 
ATOM   5157 C C   . ASP B 1 222 ? -7.582  -20.016 -6.930  1.00 173.94 ? 222 ASP B C   1 
ATOM   5158 O O   . ASP B 1 222 ? -8.253  -20.061 -7.981  1.00 186.57 ? 222 ASP B O   1 
ATOM   5159 C CB  . ASP B 1 222 ? -6.407  -17.953 -6.007  1.00 184.91 ? 222 ASP B CB  1 
ATOM   5160 C CG  . ASP B 1 222 ? -6.463  -16.632 -5.241  1.00 213.42 ? 222 ASP B CG  1 
ATOM   5161 O OD1 . ASP B 1 222 ? -7.157  -15.701 -5.714  1.00 220.62 ? 222 ASP B OD1 1 
ATOM   5162 O OD2 . ASP B 1 222 ? -5.807  -16.532 -4.171  1.00 230.84 ? 222 ASP B OD2 1 
ATOM   5163 N N   . LYS B 1 223 ? -6.752  -20.977 -6.512  1.00 169.09 ? 223 LYS B N   1 
ATOM   5164 C CA  . LYS B 1 223 ? -6.513  -22.172 -7.314  1.00 184.38 ? 223 LYS B CA  1 
ATOM   5165 C C   . LYS B 1 223 ? -7.802  -22.962 -7.474  1.00 164.74 ? 223 LYS B C   1 
ATOM   5166 O O   . LYS B 1 223 ? -7.970  -23.652 -8.484  1.00 171.38 ? 223 LYS B O   1 
ATOM   5167 C CB  . LYS B 1 223 ? -5.292  -23.022 -6.940  1.00 196.37 ? 223 LYS B CB  1 
ATOM   5168 C CG  . LYS B 1 223 ? -3.917  -22.492 -7.353  1.00 205.41 ? 223 LYS B CG  1 
ATOM   5169 C CD  . LYS B 1 223 ? -3.827  -21.475 -8.488  1.00 219.30 ? 223 LYS B CD  1 
ATOM   5170 C CE  . LYS B 1 223 ? -4.290  -21.904 -9.848  1.00 239.12 ? 223 LYS B CE  1 
ATOM   5171 N NZ  . LYS B 1 223 ? -4.564  -20.734 -10.692 1.00 251.48 ? 223 LYS B NZ  1 
ATOM   5172 N N   . LEU B 1 224 ? -8.581  -23.047 -6.394  1.00 140.12 ? 224 LEU B N   1 
ATOM   5173 C CA  . LEU B 1 224 ? -9.836  -23.768 -6.365  1.00 130.70 ? 224 LEU B CA  1 
ATOM   5174 C C   . LEU B 1 224 ? -10.782 -23.137 -7.390  1.00 139.10 ? 224 LEU B C   1 
ATOM   5175 O O   . LEU B 1 224 ? -11.430 -23.878 -8.160  1.00 160.62 ? 224 LEU B O   1 
ATOM   5176 C CB  . LEU B 1 224 ? -10.378 -23.840 -4.936  1.00 112.27 ? 224 LEU B CB  1 
ATOM   5177 C CG  . LEU B 1 224 ? -11.448 -24.895 -4.647  1.00 126.48 ? 224 LEU B CG  1 
ATOM   5178 C CD1 . LEU B 1 224 ? -11.111 -26.285 -5.199  1.00 145.31 ? 224 LEU B CD1 1 
ATOM   5179 C CD2 . LEU B 1 224 ? -11.636 -24.942 -3.134  1.00 121.80 ? 224 LEU B CD2 1 
ATOM   5180 N N   . ARG B 1 225 ? -10.849 -21.790 -7.369  1.00 138.12 ? 225 ARG B N   1 
ATOM   5181 C CA  . ARG B 1 225 ? -11.914 -21.090 -8.066  1.00 156.44 ? 225 ARG B CA  1 
ATOM   5182 C C   . ARG B 1 225 ? -11.695 -21.278 -9.552  1.00 172.53 ? 225 ARG B C   1 
ATOM   5183 O O   . ARG B 1 225 ? -12.577 -20.958 -10.330 1.00 207.27 ? 225 ARG B O   1 
ATOM   5184 C CB  . ARG B 1 225 ? -12.036 -19.610 -7.701  1.00 151.47 ? 225 ARG B CB  1 
ATOM   5185 C CG  . ARG B 1 225 ? -12.217 -19.382 -6.207  1.00 154.19 ? 225 ARG B CG  1 
ATOM   5186 C CD  . ARG B 1 225 ? -12.968 -18.097 -5.986  1.00 173.12 ? 225 ARG B CD  1 
ATOM   5187 N NE  . ARG B 1 225 ? -14.369 -18.364 -6.319  1.00 189.14 ? 225 ARG B NE  1 
ATOM   5188 C CZ  . ARG B 1 225 ? -15.310 -18.442 -5.396  1.00 207.28 ? 225 ARG B CZ  1 
ATOM   5189 N NH1 . ARG B 1 225 ? -15.014 -18.172 -4.134  1.00 221.58 ? 225 ARG B NH1 1 
ATOM   5190 N NH2 . ARG B 1 225 ? -16.550 -18.765 -5.730  1.00 206.34 ? 225 ARG B NH2 1 
ATOM   5191 N N   . HIS B 1 226 ? -10.518 -21.803 -9.905  1.00 146.24 ? 226 HIS B N   1 
ATOM   5192 C CA  . HIS B 1 226 ? -10.141 -22.038 -11.287 1.00 158.89 ? 226 HIS B CA  1 
ATOM   5193 C C   . HIS B 1 226 ? -10.319 -23.521 -11.625 1.00 167.71 ? 226 HIS B C   1 
ATOM   5194 O O   . HIS B 1 226 ? -10.831 -23.852 -12.696 1.00 203.05 ? 226 HIS B O   1 
ATOM   5195 C CB  . HIS B 1 226 ? -8.732  -21.491 -11.534 1.00 161.47 ? 226 HIS B CB  1 
ATOM   5196 C CG  . HIS B 1 226 ? -8.224  -21.675 -12.926 1.00 187.83 ? 226 HIS B CG  1 
ATOM   5197 N ND1 . HIS B 1 226 ? -7.043  -22.343 -13.175 1.00 202.40 ? 226 HIS B ND1 1 
ATOM   5198 C CD2 . HIS B 1 226 ? -8.715  -21.339 -14.128 1.00 192.96 ? 226 HIS B CD2 1 
ATOM   5199 C CE1 . HIS B 1 226 ? -6.826  -22.388 -14.481 1.00 196.23 ? 226 HIS B CE1 1 
ATOM   5200 N NE2 . HIS B 1 226 ? -7.834  -21.792 -15.079 1.00 203.21 ? 226 HIS B NE2 1 
ATOM   5201 N N   . THR B 1 227 ? -9.903  -24.399 -10.701 1.00 155.98 ? 227 THR B N   1 
ATOM   5202 C CA  . THR B 1 227 ? -9.958  -25.845 -10.890 1.00 146.10 ? 227 THR B CA  1 
ATOM   5203 C C   . THR B 1 227 ? -10.668 -26.489 -9.700  1.00 144.66 ? 227 THR B C   1 
ATOM   5204 O O   . THR B 1 227 ? -10.191 -26.434 -8.572  1.00 153.67 ? 227 THR B O   1 
ATOM   5205 C CB  . THR B 1 227 ? -8.550  -26.413 -11.059 1.00 140.58 ? 227 THR B CB  1 
ATOM   5206 O OG1 . THR B 1 227 ? -7.926  -26.358 -9.776  1.00 182.94 ? 227 THR B OG1 1 
ATOM   5207 C CG2 . THR B 1 227 ? -7.760  -25.668 -12.116 1.00 108.12 ? 227 THR B CG2 1 
ATOM   5208 N N   . GLY B 1 228 ? -11.792 -27.149 -9.969  1.00 155.55 ? 228 GLY B N   1 
ATOM   5209 C CA  . GLY B 1 228 ? -12.751 -27.515 -8.941  1.00 179.29 ? 228 GLY B CA  1 
ATOM   5210 C C   . GLY B 1 228 ? -12.230 -28.468 -7.861  1.00 205.07 ? 228 GLY B C   1 
ATOM   5211 O O   . GLY B 1 228 ? -12.891 -28.607 -6.834  1.00 240.13 ? 228 GLY B O   1 
ATOM   5212 N N   . ASP B 1 229 ? -11.069 -29.116 -8.066  1.00 215.39 ? 229 ASP B N   1 
ATOM   5213 C CA  . ASP B 1 229 ? -10.646 -30.226 -7.209  1.00 209.63 ? 229 ASP B CA  1 
ATOM   5214 C C   . ASP B 1 229 ? -9.788  -29.765 -6.023  1.00 163.96 ? 229 ASP B C   1 
ATOM   5215 O O   . ASP B 1 229 ? -8.854  -28.973 -6.190  1.00 113.98 ? 229 ASP B O   1 
ATOM   5216 C CB  . ASP B 1 229 ? -10.014 -31.357 -8.007  1.00 204.00 ? 229 ASP B CB  1 
ATOM   5217 C CG  . ASP B 1 229 ? -8.860  -30.957 -8.917  1.00 199.10 ? 229 ASP B CG  1 
ATOM   5218 O OD1 . ASP B 1 229 ? -8.734  -29.734 -9.237  1.00 203.93 ? 229 ASP B OD1 1 
ATOM   5219 O OD2 . ASP B 1 229 ? -8.092  -31.871 -9.278  1.00 174.42 ? 229 ASP B OD2 1 
ATOM   5220 N N   . LEU B 1 230 ? -10.104 -30.324 -4.837  1.00 147.25 ? 230 LEU B N   1 
ATOM   5221 C CA  . LEU B 1 230 ? -9.462  -30.016 -3.564  1.00 144.44 ? 230 LEU B CA  1 
ATOM   5222 C C   . LEU B 1 230 ? -7.959  -30.238 -3.657  1.00 164.16 ? 230 LEU B C   1 
ATOM   5223 O O   . LEU B 1 230 ? -7.184  -29.434 -3.154  1.00 182.78 ? 230 LEU B O   1 
ATOM   5224 C CB  . LEU B 1 230 ? -9.978  -30.819 -2.368  1.00 144.31 ? 230 LEU B CB  1 
ATOM   5225 C CG  . LEU B 1 230 ? -11.003 -30.156 -1.443  1.00 173.32 ? 230 LEU B CG  1 
ATOM   5226 C CD1 . LEU B 1 230 ? -10.765 -28.662 -1.212  1.00 168.45 ? 230 LEU B CD1 1 
ATOM   5227 C CD2 . LEU B 1 230 ? -12.436 -30.446 -1.907  1.00 221.15 ? 230 LEU B CD2 1 
ATOM   5228 N N   . VAL B 1 231 ? -7.558  -31.373 -4.231  1.00 173.51 ? 231 VAL B N   1 
ATOM   5229 C CA  . VAL B 1 231 ? -6.172  -31.799 -4.134  1.00 151.48 ? 231 VAL B CA  1 
ATOM   5230 C C   . VAL B 1 231 ? -5.394  -31.211 -5.301  1.00 146.63 ? 231 VAL B C   1 
ATOM   5231 O O   . VAL B 1 231 ? -4.181  -31.368 -5.346  1.00 135.41 ? 231 VAL B O   1 
ATOM   5232 C CB  . VAL B 1 231 ? -6.072  -33.336 -4.086  1.00 154.71 ? 231 VAL B CB  1 
ATOM   5233 C CG1 . VAL B 1 231 ? -4.636  -33.839 -3.951  1.00 149.00 ? 231 VAL B CG1 1 
ATOM   5234 C CG2 . VAL B 1 231 ? -6.939  -33.909 -2.974  1.00 169.13 ? 231 VAL B CG2 1 
ATOM   5235 N N   . GLY B 1 232 ? -6.116  -30.499 -6.183  1.00 163.55 ? 232 GLY B N   1 
ATOM   5236 C CA  . GLY B 1 232 ? -5.534  -29.793 -7.310  1.00 177.03 ? 232 GLY B CA  1 
ATOM   5237 C C   . GLY B 1 232 ? -5.027  -28.416 -6.892  1.00 183.72 ? 232 GLY B C   1 
ATOM   5238 O O   . GLY B 1 232 ? -4.108  -27.878 -7.507  1.00 183.68 ? 232 GLY B O   1 
ATOM   5239 N N   . SER B 1 233 ? -5.607  -27.901 -5.800  1.00 187.76 ? 233 SER B N   1 
ATOM   5240 C CA  . SER B 1 233 ? -5.314  -26.578 -5.283  1.00 180.90 ? 233 SER B CA  1 
ATOM   5241 C C   . SER B 1 233 ? -4.636  -26.651 -3.912  1.00 169.55 ? 233 SER B C   1 
ATOM   5242 O O   . SER B 1 233 ? -4.548  -25.641 -3.210  1.00 150.76 ? 233 SER B O   1 
ATOM   5243 C CB  . SER B 1 233 ? -6.585  -25.763 -5.240  1.00 192.04 ? 233 SER B CB  1 
ATOM   5244 O OG  . SER B 1 233 ? -7.644  -26.482 -4.615  1.00 240.52 ? 233 SER B OG  1 
ATOM   5245 N N   . ALA B 1 234 ? -4.148  -27.844 -3.544  1.00 151.93 ? 234 ALA B N   1 
ATOM   5246 C CA  . ALA B 1 234 ? -3.520  -28.047 -2.247  1.00 137.15 ? 234 ALA B CA  1 
ATOM   5247 C C   . ALA B 1 234 ? -2.120  -27.436 -2.247  1.00 135.33 ? 234 ALA B C   1 
ATOM   5248 O O   . ALA B 1 234 ? -1.282  -27.794 -3.072  1.00 133.72 ? 234 ALA B O   1 
ATOM   5249 C CB  . ALA B 1 234 ? -3.525  -29.509 -1.861  1.00 113.78 ? 234 ALA B CB  1 
ATOM   5250 N N   . GLU B 1 235 ? -1.908  -26.475 -1.337  1.00 139.05 ? 235 GLU B N   1 
ATOM   5251 C CA  . GLU B 1 235 ? -0.623  -25.820 -1.112  1.00 141.02 ? 235 GLU B CA  1 
ATOM   5252 C C   . GLU B 1 235 ? 0.202   -26.665 -0.148  1.00 128.38 ? 235 GLU B C   1 
ATOM   5253 O O   . GLU B 1 235 ? 1.424   -26.661 -0.203  1.00 110.35 ? 235 GLU B O   1 
ATOM   5254 C CB  . GLU B 1 235 ? -0.676  -24.403 -0.523  1.00 142.59 ? 235 GLU B CB  1 
ATOM   5255 C CG  . GLU B 1 235 ? -0.934  -23.301 -1.550  1.00 186.93 ? 235 GLU B CG  1 
ATOM   5256 C CD  . GLU B 1 235 ? -0.687  -21.881 -1.055  1.00 195.74 ? 235 GLU B CD  1 
ATOM   5257 O OE1 . GLU B 1 235 ? -0.235  -21.779 0.114   1.00 168.53 ? 235 GLU B OE1 1 
ATOM   5258 O OE2 . GLU B 1 235 ? -0.906  -20.889 -1.799  1.00 194.67 ? 235 GLU B OE2 1 
ATOM   5259 N N   . VAL B 1 236 ? -0.474  -27.361 0.769   1.00 135.94 ? 236 VAL B N   1 
ATOM   5260 C CA  . VAL B 1 236 ? 0.178   -28.329 1.636   1.00 137.86 ? 236 VAL B CA  1 
ATOM   5261 C C   . VAL B 1 236 ? -0.766  -29.508 1.867   1.00 174.96 ? 236 VAL B C   1 
ATOM   5262 O O   . VAL B 1 236 ? -1.742  -29.373 2.597   1.00 199.45 ? 236 VAL B O   1 
ATOM   5263 C CB  . VAL B 1 236 ? 0.604   -27.683 2.969   1.00 115.17 ? 236 VAL B CB  1 
ATOM   5264 C CG1 . VAL B 1 236 ? 1.194   -28.699 3.957   1.00 117.29 ? 236 VAL B CG1 1 
ATOM   5265 C CG2 . VAL B 1 236 ? 1.537   -26.499 2.733   1.00 97.94  ? 236 VAL B CG2 1 
ATOM   5266 N N   . ILE B 1 237 ? -0.454  -30.658 1.253   1.00 178.92 ? 237 ILE B N   1 
ATOM   5267 C CA  . ILE B 1 237 ? -1.116  -31.915 1.569   1.00 162.93 ? 237 ILE B CA  1 
ATOM   5268 C C   . ILE B 1 237 ? -0.057  -32.938 1.973   1.00 153.90 ? 237 ILE B C   1 
ATOM   5269 O O   . ILE B 1 237 ? 0.922   -33.110 1.255   1.00 135.40 ? 237 ILE B O   1 
ATOM   5270 C CB  . ILE B 1 237 ? -2.016  -32.408 0.413   1.00 152.14 ? 237 ILE B CB  1 
ATOM   5271 C CG1 . ILE B 1 237 ? -2.796  -33.673 0.829   1.00 142.21 ? 237 ILE B CG1 1 
ATOM   5272 C CG2 . ILE B 1 237 ? -1.218  -32.589 -0.888  1.00 123.79 ? 237 ILE B CG2 1 
ATOM   5273 C CD1 . ILE B 1 237 ? -3.916  -34.088 -0.098  1.00 138.66 ? 237 ILE B CD1 1 
ATOM   5274 N N   . ARG B 1 238 ? -0.261  -33.607 3.119   1.00 159.26 ? 238 ARG B N   1 
ATOM   5275 C CA  . ARG B 1 238 ? 0.716   -34.562 3.623   1.00 154.47 ? 238 ARG B CA  1 
ATOM   5276 C C   . ARG B 1 238 ? 0.144   -35.978 3.575   1.00 140.94 ? 238 ARG B C   1 
ATOM   5277 O O   . ARG B 1 238 ? 0.773   -36.951 3.983   1.00 123.03 ? 238 ARG B O   1 
ATOM   5278 C CB  . ARG B 1 238 ? 1.229   -34.077 4.981   1.00 172.78 ? 238 ARG B CB  1 
ATOM   5279 C CG  . ARG B 1 238 ? 1.482   -32.577 4.867   1.00 205.31 ? 238 ARG B CG  1 
ATOM   5280 C CD  . ARG B 1 238 ? 2.908   -32.101 5.126   1.00 201.80 ? 238 ARG B CD  1 
ATOM   5281 N NE  . ARG B 1 238 ? 3.362   -32.390 6.490   1.00 208.88 ? 238 ARG B NE  1 
ATOM   5282 C CZ  . ARG B 1 238 ? 2.888   -31.854 7.612   1.00 219.52 ? 238 ARG B CZ  1 
ATOM   5283 N NH1 . ARG B 1 238 ? 1.964   -30.906 7.574   1.00 214.40 ? 238 ARG B NH1 1 
ATOM   5284 N NH2 . ARG B 1 238 ? 3.359   -32.280 8.769   1.00 227.75 ? 238 ARG B NH2 1 
ATOM   5285 N N   . LEU B 1 239 ? -1.077  -36.089 3.059   1.00 152.50 ? 239 LEU B N   1 
ATOM   5286 C CA  . LEU B 1 239 ? -1.710  -37.375 2.838   1.00 148.66 ? 239 LEU B CA  1 
ATOM   5287 C C   . LEU B 1 239 ? -1.576  -37.786 1.376   1.00 157.26 ? 239 LEU B C   1 
ATOM   5288 O O   . LEU B 1 239 ? -1.697  -36.961 0.464   1.00 149.45 ? 239 LEU B O   1 
ATOM   5289 C CB  . LEU B 1 239 ? -3.170  -37.307 3.279   1.00 154.08 ? 239 LEU B CB  1 
ATOM   5290 C CG  . LEU B 1 239 ? -3.380  -37.600 4.764   1.00 158.42 ? 239 LEU B CG  1 
ATOM   5291 C CD1 . LEU B 1 239 ? -4.834  -37.487 5.163   1.00 159.77 ? 239 LEU B CD1 1 
ATOM   5292 C CD2 . LEU B 1 239 ? -2.840  -39.006 4.979   1.00 145.70 ? 239 LEU B CD2 1 
ATOM   5293 N N   . PRO B 1 240 ? -1.324  -39.088 1.113   1.00 167.19 ? 240 PRO B N   1 
ATOM   5294 C CA  . PRO B 1 240 ? -1.565  -39.650 -0.217  1.00 186.74 ? 240 PRO B CA  1 
ATOM   5295 C C   . PRO B 1 240 ? -3.003  -39.287 -0.587  1.00 195.19 ? 240 PRO B C   1 
ATOM   5296 O O   . PRO B 1 240 ? -3.919  -39.467 0.214   1.00 184.09 ? 240 PRO B O   1 
ATOM   5297 C CB  . PRO B 1 240 ? -1.371  -41.156 -0.001  1.00 180.23 ? 240 PRO B CB  1 
ATOM   5298 C CG  . PRO B 1 240 ? -0.435  -41.238 1.183   1.00 164.01 ? 240 PRO B CG  1 
ATOM   5299 C CD  . PRO B 1 240 ? -0.797  -40.068 2.076   1.00 151.38 ? 240 PRO B CD  1 
ATOM   5300 N N   . ALA B 1 241 ? -3.174  -38.740 -1.794  1.00 175.51 ? 241 ALA B N   1 
ATOM   5301 C CA  . ALA B 1 241 ? -4.425  -38.119 -2.182  1.00 177.40 ? 241 ALA B CA  1 
ATOM   5302 C C   . ALA B 1 241 ? -5.590  -39.073 -1.913  1.00 185.00 ? 241 ALA B C   1 
ATOM   5303 O O   . ALA B 1 241 ? -6.641  -38.661 -1.397  1.00 212.38 ? 241 ALA B O   1 
ATOM   5304 C CB  . ALA B 1 241 ? -4.350  -37.734 -3.642  1.00 182.10 ? 241 ALA B CB  1 
ATOM   5305 N N   . GLU B 1 242 ? -5.380  -40.329 -2.335  1.00 174.50 ? 242 GLU B N   1 
ATOM   5306 C CA  . GLU B 1 242 ? -6.390  -41.370 -2.250  1.00 187.58 ? 242 GLU B CA  1 
ATOM   5307 C C   . GLU B 1 242 ? -6.847  -41.545 -0.801  1.00 182.64 ? 242 GLU B C   1 
ATOM   5308 O O   . GLU B 1 242 ? -8.060  -41.607 -0.507  1.00 188.22 ? 242 GLU B O   1 
ATOM   5309 C CB  . GLU B 1 242 ? -5.803  -42.717 -2.687  1.00 184.07 ? 242 GLU B CB  1 
ATOM   5310 C CG  . GLU B 1 242 ? -6.544  -43.926 -2.108  1.00 216.24 ? 242 GLU B CG  1 
ATOM   5311 C CD  . GLU B 1 242 ? -8.023  -44.170 -2.427  1.00 242.46 ? 242 GLU B CD  1 
ATOM   5312 O OE1 . GLU B 1 242 ? -8.590  -43.499 -3.318  1.00 274.01 ? 242 GLU B OE1 1 
ATOM   5313 O OE2 . GLU B 1 242 ? -8.640  -45.023 -1.759  1.00 218.45 ? 242 GLU B OE2 1 
ATOM   5314 N N   . GLU B 1 243 ? -5.832  -41.624 0.074   1.00 159.46 ? 243 GLU B N   1 
ATOM   5315 C CA  . GLU B 1 243 ? -6.075  -41.830 1.499   1.00 174.66 ? 243 GLU B CA  1 
ATOM   5316 C C   . GLU B 1 243 ? -6.913  -40.685 2.060   1.00 173.47 ? 243 GLU B C   1 
ATOM   5317 O O   . GLU B 1 243 ? -7.869  -40.920 2.809   1.00 169.71 ? 243 GLU B O   1 
ATOM   5318 C CB  . GLU B 1 243 ? -4.819  -42.168 2.295   1.00 179.59 ? 243 GLU B CB  1 
ATOM   5319 C CG  . GLU B 1 243 ? -5.171  -42.580 3.720   1.00 202.81 ? 243 GLU B CG  1 
ATOM   5320 C CD  . GLU B 1 243 ? -3.960  -42.809 4.586   1.00 225.37 ? 243 GLU B CD  1 
ATOM   5321 O OE1 . GLU B 1 243 ? -2.847  -42.775 4.016   1.00 235.23 ? 243 GLU B OE1 1 
ATOM   5322 O OE2 . GLU B 1 243 ? -4.153  -43.043 5.797   1.00 249.41 ? 243 GLU B OE2 1 
ATOM   5323 N N   . PHE B 1 244 ? -6.537  -39.466 1.664   1.00 178.03 ? 244 PHE B N   1 
ATOM   5324 C CA  . PHE B 1 244 ? -7.221  -38.250 2.095   1.00 179.71 ? 244 PHE B CA  1 
ATOM   5325 C C   . PHE B 1 244 ? -8.695  -38.308 1.693   1.00 173.02 ? 244 PHE B C   1 
ATOM   5326 O O   . PHE B 1 244 ? -9.587  -38.010 2.504   1.00 170.67 ? 244 PHE B O   1 
ATOM   5327 C CB  . PHE B 1 244 ? -6.551  -36.994 1.532   1.00 162.56 ? 244 PHE B CB  1 
ATOM   5328 C CG  . PHE B 1 244 ? -7.300  -35.686 1.715   1.00 137.49 ? 244 PHE B CG  1 
ATOM   5329 C CD1 . PHE B 1 244 ? -7.729  -35.264 2.972   1.00 127.69 ? 244 PHE B CD1 1 
ATOM   5330 C CD2 . PHE B 1 244 ? -7.570  -34.880 0.618   1.00 125.92 ? 244 PHE B CD2 1 
ATOM   5331 C CE1 . PHE B 1 244 ? -8.382  -34.042 3.119   1.00 125.64 ? 244 PHE B CE1 1 
ATOM   5332 C CE2 . PHE B 1 244 ? -8.213  -33.651 0.772   1.00 135.06 ? 244 PHE B CE2 1 
ATOM   5333 C CZ  . PHE B 1 244 ? -8.650  -33.246 2.020   1.00 133.94 ? 244 PHE B CZ  1 
ATOM   5334 N N   . ARG B 1 245 ? -8.905  -38.703 0.435   1.00 168.95 ? 245 ARG B N   1 
ATOM   5335 C CA  . ARG B 1 245 ? -10.243 -38.817 -0.140  1.00 155.55 ? 245 ARG B CA  1 
ATOM   5336 C C   . ARG B 1 245 ? -11.087 -39.794 0.684   1.00 146.91 ? 245 ARG B C   1 
ATOM   5337 O O   . ARG B 1 245 ? -12.248 -39.511 1.023   1.00 137.20 ? 245 ARG B O   1 
ATOM   5338 C CB  . ARG B 1 245 ? -10.234 -39.130 -1.642  1.00 160.32 ? 245 ARG B CB  1 
ATOM   5339 C CG  . ARG B 1 245 ? -9.816  -37.955 -2.523  1.00 167.16 ? 245 ARG B CG  1 
ATOM   5340 C CD  . ARG B 1 245 ? -10.053 -38.198 -4.011  1.00 173.02 ? 245 ARG B CD  1 
ATOM   5341 N NE  . ARG B 1 245 ? -9.782  -37.058 -4.896  1.00 165.91 ? 245 ARG B NE  1 
ATOM   5342 C CZ  . ARG B 1 245 ? -8.600  -36.686 -5.379  1.00 166.85 ? 245 ARG B CZ  1 
ATOM   5343 N NH1 . ARG B 1 245 ? -7.509  -37.381 -5.084  1.00 150.03 ? 245 ARG B NH1 1 
ATOM   5344 N NH2 . ARG B 1 245 ? -8.519  -35.618 -6.164  1.00 185.93 ? 245 ARG B NH2 1 
ATOM   5345 N N   . ARG B 1 246 ? -10.463 -40.934 0.983   1.00 141.19 ? 246 ARG B N   1 
ATOM   5346 C CA  . ARG B 1 246 ? -11.099 -42.000 1.752   1.00 149.13 ? 246 ARG B CA  1 
ATOM   5347 C C   . ARG B 1 246 ? -11.534 -41.473 3.120   1.00 165.18 ? 246 ARG B C   1 
ATOM   5348 O O   . ARG B 1 246 ? -12.659 -41.724 3.570   1.00 197.49 ? 246 ARG B O   1 
ATOM   5349 C CB  . ARG B 1 246 ? -10.299 -43.306 1.696   1.00 152.70 ? 246 ARG B CB  1 
ATOM   5350 C CG  . ARG B 1 246 ? -10.100 -43.983 3.045   1.00 202.69 ? 246 ARG B CG  1 
ATOM   5351 C CD  . ARG B 1 246 ? -9.692  -45.459 2.997   1.00 229.97 ? 246 ARG B CD  1 
ATOM   5352 N NE  . ARG B 1 246 ? -8.258  -45.596 2.724   1.00 234.94 ? 246 ARG B NE  1 
ATOM   5353 C CZ  . ARG B 1 246 ? -7.741  -46.000 1.575   1.00 218.09 ? 246 ARG B CZ  1 
ATOM   5354 N NH1 . ARG B 1 246 ? -8.532  -46.419 0.605   1.00 210.86 ? 246 ARG B NH1 1 
ATOM   5355 N NH2 . ARG B 1 246 ? -6.433  -45.971 1.397   1.00 226.42 ? 246 ARG B NH2 1 
ATOM   5356 N N   . GLU B 1 247 ? -10.613 -40.742 3.749   1.00 155.88 ? 247 GLU B N   1 
ATOM   5357 C CA  . GLU B 1 247 ? -10.834 -40.156 5.068   1.00 143.22 ? 247 GLU B CA  1 
ATOM   5358 C C   . GLU B 1 247 ? -12.040 -39.225 5.026   1.00 157.75 ? 247 GLU B C   1 
ATOM   5359 O O   . GLU B 1 247 ? -12.907 -39.268 5.908   1.00 155.03 ? 247 GLU B O   1 
ATOM   5360 C CB  . GLU B 1 247 ? -9.589  -39.618 5.774   1.00 137.90 ? 247 GLU B CB  1 
ATOM   5361 C CG  . GLU B 1 247 ? -9.858  -39.149 7.206   1.00 161.60 ? 247 GLU B CG  1 
ATOM   5362 C CD  . GLU B 1 247 ? -10.122 -40.193 8.294   1.00 170.52 ? 247 GLU B CD  1 
ATOM   5363 O OE1 . GLU B 1 247 ? -10.045 -41.411 8.007   1.00 169.57 ? 247 GLU B OE1 1 
ATOM   5364 O OE2 . GLU B 1 247 ? -10.375 -39.772 9.445   1.00 175.48 ? 247 GLU B OE2 1 
ATOM   5365 N N   . LEU B 1 248 ? -12.065 -38.393 3.983   1.00 176.30 ? 248 LEU B N   1 
ATOM   5366 C CA  . LEU B 1 248 ? -13.134 -37.423 3.762   1.00 190.83 ? 248 LEU B CA  1 
ATOM   5367 C C   . LEU B 1 248 ? -14.478 -38.147 3.671   1.00 202.15 ? 248 LEU B C   1 
ATOM   5368 O O   . LEU B 1 248 ? -15.464 -37.736 4.291   1.00 223.57 ? 248 LEU B O   1 
ATOM   5369 C CB  . LEU B 1 248 ? -12.810 -36.580 2.524   1.00 163.70 ? 248 LEU B CB  1 
ATOM   5370 C CG  . LEU B 1 248 ? -13.226 -35.101 2.546   1.00 157.98 ? 248 LEU B CG  1 
ATOM   5371 C CD1 . LEU B 1 248 ? -13.062 -34.474 3.917   1.00 136.96 ? 248 LEU B CD1 1 
ATOM   5372 C CD2 . LEU B 1 248 ? -12.384 -34.310 1.544   1.00 142.91 ? 248 LEU B CD2 1 
ATOM   5373 N N   . ALA B 1 249 ? -14.474 -39.231 2.887   1.00 180.50 ? 249 ALA B N   1 
ATOM   5374 C CA  . ALA B 1 249 ? -15.657 -40.042 2.649   1.00 165.95 ? 249 ALA B CA  1 
ATOM   5375 C C   . ALA B 1 249 ? -16.180 -40.589 3.982   1.00 170.90 ? 249 ALA B C   1 
ATOM   5376 O O   . ALA B 1 249 ? -17.390 -40.531 4.264   1.00 216.09 ? 249 ALA B O   1 
ATOM   5377 C CB  . ALA B 1 249 ? -15.362 -41.178 1.685   1.00 133.60 ? 249 ALA B CB  1 
ATOM   5378 N N   . GLU B 1 250 ? -15.243 -41.101 4.792   1.00 158.78 ? 250 GLU B N   1 
ATOM   5379 C CA  . GLU B 1 250 ? -15.609 -42.043 5.849   1.00 161.77 ? 250 GLU B CA  1 
ATOM   5380 C C   . GLU B 1 250 ? -15.715 -41.340 7.194   1.00 166.08 ? 250 GLU B C   1 
ATOM   5381 O O   . GLU B 1 250 ? -16.598 -41.663 7.969   1.00 171.96 ? 250 GLU B O   1 
ATOM   5382 C CB  . GLU B 1 250 ? -14.682 -43.258 5.853   1.00 175.92 ? 250 GLU B CB  1 
ATOM   5383 C CG  . GLU B 1 250 ? -14.908 -44.191 4.666   1.00 202.45 ? 250 GLU B CG  1 
ATOM   5384 C CD  . GLU B 1 250 ? -13.734 -45.119 4.390   1.00 223.65 ? 250 GLU B CD  1 
ATOM   5385 O OE1 . GLU B 1 250 ? -13.180 -45.708 5.345   1.00 221.68 ? 250 GLU B OE1 1 
ATOM   5386 O OE2 . GLU B 1 250 ? -13.360 -45.244 3.203   1.00 224.76 ? 250 GLU B OE2 1 
ATOM   5387 N N   . GLN B 1 251 ? -14.814 -40.385 7.447   1.00 158.66 ? 251 GLN B N   1 
ATOM   5388 C CA  . GLN B 1 251 ? -14.806 -39.642 8.693   1.00 154.66 ? 251 GLN B CA  1 
ATOM   5389 C C   . GLN B 1 251 ? -15.081 -38.176 8.413   1.00 178.06 ? 251 GLN B C   1 
ATOM   5390 O O   . GLN B 1 251 ? -15.751 -37.521 9.206   1.00 232.76 ? 251 GLN B O   1 
ATOM   5391 C CB  . GLN B 1 251 ? -13.444 -39.681 9.373   1.00 148.80 ? 251 GLN B CB  1 
ATOM   5392 C CG  . GLN B 1 251 ? -13.237 -40.932 10.212  1.00 164.28 ? 251 GLN B CG  1 
ATOM   5393 C CD  . GLN B 1 251 ? -14.067 -40.906 11.480  1.00 184.54 ? 251 GLN B CD  1 
ATOM   5394 O OE1 . GLN B 1 251 ? -14.668 -39.889 11.855  1.00 162.05 ? 251 GLN B OE1 1 
ATOM   5395 N NE2 . GLN B 1 251 ? -14.073 -42.024 12.196  1.00 223.67 ? 251 GLN B NE2 1 
ATOM   5396 N N   . GLY B 1 252 ? -14.529 -37.687 7.301   1.00 176.90 ? 252 GLY B N   1 
ATOM   5397 C CA  . GLY B 1 252 ? -14.663 -36.298 6.891   1.00 185.60 ? 252 GLY B CA  1 
ATOM   5398 C C   . GLY B 1 252 ? -13.720 -35.301 7.582   1.00 171.53 ? 252 GLY B C   1 
ATOM   5399 O O   . GLY B 1 252 ? -12.817 -35.644 8.364   1.00 154.71 ? 252 GLY B O   1 
ATOM   5400 N N   . ALA B 1 253 ? -13.960 -34.023 7.249   1.00 151.70 ? 253 ALA B N   1 
ATOM   5401 C CA  . ALA B 1 253 ? -13.149 -32.909 7.681   1.00 161.57 ? 253 ALA B CA  1 
ATOM   5402 C C   . ALA B 1 253 ? -14.083 -31.805 8.157   1.00 163.54 ? 253 ALA B C   1 
ATOM   5403 O O   . ALA B 1 253 ? -15.294 -31.926 8.212   1.00 173.52 ? 253 ALA B O   1 
ATOM   5404 C CB  . ALA B 1 253 ? -12.233 -32.443 6.562   1.00 147.32 ? 253 ALA B CB  1 
ATOM   5405 N N   . ILE B 1 254 ? -13.458 -30.697 8.531   1.00 147.78 ? 254 ILE B N   1 
ATOM   5406 C CA  . ILE B 1 254 ? -14.086 -29.470 8.987   1.00 135.40 ? 254 ILE B CA  1 
ATOM   5407 C C   . ILE B 1 254 ? -13.239 -28.358 8.385   1.00 134.08 ? 254 ILE B C   1 
ATOM   5408 O O   . ILE B 1 254 ? -11.999 -28.413 8.335   1.00 150.26 ? 254 ILE B O   1 
ATOM   5409 C CB  . ILE B 1 254 ? -14.172 -29.363 10.536  1.00 129.01 ? 254 ILE B CB  1 
ATOM   5410 C CG1 . ILE B 1 254 ? -13.127 -28.439 11.191  1.00 122.06 ? 254 ILE B CG1 1 
ATOM   5411 C CG2 . ILE B 1 254 ? -14.219 -30.724 11.241  1.00 122.77 ? 254 ILE B CG2 1 
ATOM   5412 C CD1 . ILE B 1 254 ? -13.355 -28.219 12.685  1.00 125.51 ? 254 ILE B CD1 1 
ATOM   5413 N N   . VAL B 1 255 ? -13.895 -27.231 8.073   1.00 132.75 ? 255 VAL B N   1 
ATOM   5414 C CA  . VAL B 1 255 ? -13.213 -26.142 7.377   1.00 117.58 ? 255 VAL B CA  1 
ATOM   5415 C C   . VAL B 1 255 ? -13.066 -24.890 8.255   1.00 118.46 ? 255 VAL B C   1 
ATOM   5416 O O   . VAL B 1 255 ? -14.020 -24.381 8.840   1.00 140.39 ? 255 VAL B O   1 
ATOM   5417 C CB  . VAL B 1 255 ? -13.667 -25.906 5.923   1.00 115.41 ? 255 VAL B CB  1 
ATOM   5418 C CG1 . VAL B 1 255 ? -12.830 -24.834 5.251   1.00 105.72 ? 255 VAL B CG1 1 
ATOM   5419 C CG2 . VAL B 1 255 ? -13.562 -27.196 5.130   1.00 107.31 ? 255 VAL B CG2 1 
ATOM   5420 N N   . GLU B 1 256 ? -11.803 -24.467 8.382   1.00 116.04 ? 256 GLU B N   1 
ATOM   5421 C CA  . GLU B 1 256 ? -11.423 -23.258 9.089   1.00 126.13 ? 256 GLU B CA  1 
ATOM   5422 C C   . GLU B 1 256 ? -10.543 -22.373 8.206   1.00 126.83 ? 256 GLU B C   1 
ATOM   5423 O O   . GLU B 1 256 ? -9.658  -22.800 7.440   1.00 119.74 ? 256 GLU B O   1 
ATOM   5424 C CB  . GLU B 1 256 ? -10.668 -23.417 10.405  1.00 128.35 ? 256 GLU B CB  1 
ATOM   5425 C CG  . GLU B 1 256 ? -11.494 -24.110 11.479  1.00 158.96 ? 256 GLU B CG  1 
ATOM   5426 C CD  . GLU B 1 256 ? -10.791 -24.220 12.816  1.00 206.76 ? 256 GLU B CD  1 
ATOM   5427 O OE1 . GLU B 1 256 ? -9.673  -24.784 12.889  1.00 230.79 ? 256 GLU B OE1 1 
ATOM   5428 O OE2 . GLU B 1 256 ? -11.386 -23.713 13.797  1.00 224.06 ? 256 GLU B OE2 1 
ATOM   5429 N N   . GLU B 1 257 ? -10.729 -21.076 8.426   1.00 135.10 ? 257 GLU B N   1 
ATOM   5430 C CA  . GLU B 1 257 ? -9.962  -20.006 7.810   1.00 146.88 ? 257 GLU B CA  1 
ATOM   5431 C C   . GLU B 1 257 ? -8.538  -20.019 8.355   1.00 136.08 ? 257 GLU B C   1 
ATOM   5432 O O   . GLU B 1 257 ? -8.303  -20.049 9.572   1.00 130.64 ? 257 GLU B O   1 
ATOM   5433 C CB  . GLU B 1 257 ? -10.610 -18.638 8.031   1.00 186.27 ? 257 GLU B CB  1 
ATOM   5434 C CG  . GLU B 1 257 ? -10.880 -18.299 9.497   1.00 194.10 ? 257 GLU B CG  1 
ATOM   5435 C CD  . GLU B 1 257 ? -11.108 -16.818 9.756   1.00 181.20 ? 257 GLU B CD  1 
ATOM   5436 O OE1 . GLU B 1 257 ? -10.724 -15.995 8.889   1.00 172.19 ? 257 GLU B OE1 1 
ATOM   5437 O OE2 . GLU B 1 257 ? -11.670 -16.501 10.821  1.00 189.12 ? 257 GLU B OE2 1 
ATOM   5438 N N   . PHE B 1 258 ? -7.597  -19.910 7.413   1.00 137.06 ? 258 PHE B N   1 
ATOM   5439 C CA  . PHE B 1 258 ? -6.172  -19.858 7.707   1.00 150.17 ? 258 PHE B CA  1 
ATOM   5440 C C   . PHE B 1 258 ? -5.752  -18.431 8.068   1.00 160.15 ? 258 PHE B C   1 
ATOM   5441 O O   . PHE B 1 258 ? -5.401  -17.648 7.177   1.00 172.00 ? 258 PHE B O   1 
ATOM   5442 C CB  . PHE B 1 258 ? -5.376  -20.495 6.568   1.00 155.61 ? 258 PHE B CB  1 
ATOM   5443 C CG  . PHE B 1 258 ? -3.884  -20.445 6.840   1.00 164.35 ? 258 PHE B CG  1 
ATOM   5444 C CD1 . PHE B 1 258 ? -3.305  -21.337 7.733   1.00 148.76 ? 258 PHE B CD1 1 
ATOM   5445 C CD2 . PHE B 1 258 ? -3.079  -19.481 6.233   1.00 188.74 ? 258 PHE B CD2 1 
ATOM   5446 C CE1 . PHE B 1 258 ? -1.949  -21.270 8.006   1.00 166.11 ? 258 PHE B CE1 1 
ATOM   5447 C CE2 . PHE B 1 258 ? -1.720  -19.430 6.493   1.00 180.84 ? 258 PHE B CE2 1 
ATOM   5448 C CZ  . PHE B 1 258 ? -1.157  -20.326 7.379   1.00 177.36 ? 258 PHE B CZ  1 
ATOM   5449 N N   . LEU B 1 259 ? -5.766  -18.135 9.382   1.00 156.64 ? 259 LEU B N   1 
ATOM   5450 C CA  . LEU B 1 259 ? -5.296  -16.880 9.956   1.00 154.47 ? 259 LEU B CA  1 
ATOM   5451 C C   . LEU B 1 259 ? -3.854  -16.650 9.519   1.00 171.34 ? 259 LEU B C   1 
ATOM   5452 O O   . LEU B 1 259 ? -3.008  -17.519 9.708   1.00 187.17 ? 259 LEU B O   1 
ATOM   5453 C CB  . LEU B 1 259 ? -5.404  -16.981 11.476  1.00 138.01 ? 259 LEU B CB  1 
ATOM   5454 C CG  . LEU B 1 259 ? -6.635  -17.733 11.994  1.00 143.33 ? 259 LEU B CG  1 
ATOM   5455 C CD1 . LEU B 1 259 ? -6.543  -18.081 13.463  1.00 136.87 ? 259 LEU B CD1 1 
ATOM   5456 C CD2 . LEU B 1 259 ? -7.930  -16.988 11.755  1.00 148.86 ? 259 LEU B CD2 1 
ATOM   5457 N N   . GLU B 1 260 ? -3.581  -15.477 8.938   1.00 174.52 ? 260 GLU B N   1 
ATOM   5458 C CA  . GLU B 1 260 ? -2.351  -15.281 8.189   1.00 180.87 ? 260 GLU B CA  1 
ATOM   5459 C C   . GLU B 1 260 ? -1.219  -14.874 9.118   1.00 177.81 ? 260 GLU B C   1 
ATOM   5460 O O   . GLU B 1 260 ? -0.151  -15.492 9.098   1.00 176.29 ? 260 GLU B O   1 
ATOM   5461 C CB  . GLU B 1 260 ? -2.545  -14.233 7.097   1.00 216.23 ? 260 GLU B CB  1 
ATOM   5462 C CG  . GLU B 1 260 ? -3.367  -14.758 5.925   1.00 241.82 ? 260 GLU B CG  1 
ATOM   5463 C CD  . GLU B 1 260 ? -2.693  -15.813 5.065   1.00 250.36 ? 260 GLU B CD  1 
ATOM   5464 O OE1 . GLU B 1 260 ? -1.475  -16.079 5.184   1.00 257.79 ? 260 GLU B OE1 1 
ATOM   5465 O OE2 . GLU B 1 260 ? -3.439  -16.379 4.253   1.00 256.04 ? 260 GLU B OE2 1 
ATOM   5466 N N   . GLU B 1 261 ? -1.479  -13.831 9.915   1.00 174.99 ? 261 GLU B N   1 
ATOM   5467 C CA  . GLU B 1 261 ? -0.477  -13.288 10.811  1.00 208.16 ? 261 GLU B CA  1 
ATOM   5468 C C   . GLU B 1 261 ? -0.647  -13.912 12.193  1.00 202.68 ? 261 GLU B C   1 
ATOM   5469 O O   . GLU B 1 261 ? -1.453  -13.435 12.983  1.00 173.11 ? 261 GLU B O   1 
ATOM   5470 C CB  . GLU B 1 261 ? -0.520  -11.757 10.782  1.00 225.01 ? 261 GLU B CB  1 
ATOM   5471 C CG  . GLU B 1 261 ? 0.031   -11.155 9.489   1.00 241.20 ? 261 GLU B CG  1 
ATOM   5472 C CD  . GLU B 1 261 ? 1.513   -11.377 9.208   1.00 263.26 ? 261 GLU B CD  1 
ATOM   5473 O OE1 . GLU B 1 261 ? 2.339   -10.864 9.997   1.00 258.39 ? 261 GLU B OE1 1 
ATOM   5474 O OE2 . GLU B 1 261 ? 1.851   -12.060 8.210   1.00 273.34 ? 261 GLU B OE2 1 
ATOM   5475 N N   . ILE B 1 262 ? 0.133   -14.974 12.458  1.00 203.29 ? 262 ILE B N   1 
ATOM   5476 C CA  . ILE B 1 262 ? 0.258   -15.590 13.771  1.00 187.08 ? 262 ILE B CA  1 
ATOM   5477 C C   . ILE B 1 262 ? 1.629   -15.218 14.342  1.00 189.21 ? 262 ILE B C   1 
ATOM   5478 O O   . ILE B 1 262 ? 2.657   -15.439 13.704  1.00 196.70 ? 262 ILE B O   1 
ATOM   5479 C CB  . ILE B 1 262 ? 0.017   -17.117 13.717  1.00 165.73 ? 262 ILE B CB  1 
ATOM   5480 C CG1 . ILE B 1 262 ? -1.346  -17.469 13.130  1.00 154.19 ? 262 ILE B CG1 1 
ATOM   5481 C CG2 . ILE B 1 262 ? 0.167   -17.745 15.101  1.00 161.46 ? 262 ILE B CG2 1 
ATOM   5482 C CD1 . ILE B 1 262 ? -1.487  -18.927 12.740  1.00 150.69 ? 262 ILE B CD1 1 
ATOM   5483 N N   . THR B 1 263 ? 1.630   -14.642 15.554  1.00 188.76 ? 263 THR B N   1 
ATOM   5484 C CA  . THR B 1 263 ? 2.846   -14.193 16.221  1.00 179.25 ? 263 THR B CA  1 
ATOM   5485 C C   . THR B 1 263 ? 3.274   -15.206 17.283  1.00 188.25 ? 263 THR B C   1 
ATOM   5486 O O   . THR B 1 263 ? 4.448   -15.568 17.337  1.00 211.42 ? 263 THR B O   1 
ATOM   5487 C CB  . THR B 1 263 ? 2.644   -12.793 16.801  1.00 186.19 ? 263 THR B CB  1 
ATOM   5488 O OG1 . THR B 1 263 ? 1.534   -12.930 17.687  1.00 199.28 ? 263 THR B OG1 1 
ATOM   5489 C CG2 . THR B 1 263 ? 2.388   -11.752 15.722  1.00 170.71 ? 263 THR B CG2 1 
ATOM   5490 N N   . ASP B 1 264 ? 2.314   -15.648 18.113  1.00 192.36 ? 264 ASP B N   1 
ATOM   5491 C CA  . ASP B 1 264 ? 2.511   -16.690 19.105  1.00 206.78 ? 264 ASP B CA  1 
ATOM   5492 C C   . ASP B 1 264 ? 1.424   -17.765 19.025  1.00 189.33 ? 264 ASP B C   1 
ATOM   5493 O O   . ASP B 1 264 ? 0.320   -17.546 18.509  1.00 173.75 ? 264 ASP B O   1 
ATOM   5494 C CB  . ASP B 1 264 ? 2.713   -16.114 20.498  1.00 230.97 ? 264 ASP B CB  1 
ATOM   5495 C CG  . ASP B 1 264 ? 4.013   -15.344 20.679  1.00 251.51 ? 264 ASP B CG  1 
ATOM   5496 O OD1 . ASP B 1 264 ? 5.083   -15.992 20.651  1.00 272.95 ? 264 ASP B OD1 1 
ATOM   5497 O OD2 . ASP B 1 264 ? 3.945   -14.100 20.814  1.00 228.82 ? 264 ASP B OD2 1 
ATOM   5498 N N   . SER B 1 265 ? 1.786   -18.940 19.544  1.00 181.71 ? 265 SER B N   1 
ATOM   5499 C CA  . SER B 1 265 ? 0.883   -20.081 19.624  1.00 191.43 ? 265 SER B CA  1 
ATOM   5500 C C   . SER B 1 265 ? 0.866   -20.671 21.022  1.00 177.11 ? 265 SER B C   1 
ATOM   5501 O O   . SER B 1 265 ? 1.372   -21.773 21.200  1.00 211.14 ? 265 SER B O   1 
ATOM   5502 C CB  . SER B 1 265 ? 1.221   -21.111 18.565  1.00 217.32 ? 265 SER B CB  1 
ATOM   5503 O OG  . SER B 1 265 ? 0.328   -22.217 18.604  1.00 236.43 ? 265 SER B OG  1 
ATOM   5504 N N   . PRO B 1 266 ? 0.236   -19.992 22.014  1.00 166.79 ? 266 PRO B N   1 
ATOM   5505 C CA  . PRO B 1 266 ? 0.128   -20.507 23.380  1.00 166.61 ? 266 PRO B CA  1 
ATOM   5506 C C   . PRO B 1 266 ? -0.788  -21.710 23.617  1.00 162.70 ? 266 PRO B C   1 
ATOM   5507 O O   . PRO B 1 266 ? -1.668  -22.000 22.814  1.00 152.94 ? 266 PRO B O   1 
ATOM   5508 C CB  . PRO B 1 266 ? -0.252  -19.270 24.230  1.00 159.60 ? 266 PRO B CB  1 
ATOM   5509 C CG  . PRO B 1 266 ? -0.904  -18.320 23.252  1.00 167.24 ? 266 PRO B CG  1 
ATOM   5510 C CD  . PRO B 1 266 ? -0.414  -18.680 21.863  1.00 171.69 ? 266 PRO B CD  1 
ATOM   5511 N N   . SER B 1 267 ? -0.543  -22.400 24.737  1.00 169.85 ? 267 SER B N   1 
ATOM   5512 C CA  . SER B 1 267 ? -1.297  -23.574 25.123  1.00 190.39 ? 267 SER B CA  1 
ATOM   5513 C C   . SER B 1 267 ? -1.767  -23.514 26.573  1.00 177.64 ? 267 SER B C   1 
ATOM   5514 O O   . SER B 1 267 ? -1.119  -22.983 27.490  1.00 182.39 ? 267 SER B O   1 
ATOM   5515 C CB  . SER B 1 267 ? -0.597  -24.874 24.828  1.00 216.75 ? 267 SER B CB  1 
ATOM   5516 O OG  . SER B 1 267 ? 0.516   -25.098 25.681  1.00 202.63 ? 267 SER B OG  1 
ATOM   5517 N N   . GLY B 1 268 ? -2.889  -24.202 26.784  1.00 147.13 ? 268 GLY B N   1 
ATOM   5518 C CA  . GLY B 1 268 ? -3.564  -24.316 28.061  1.00 134.61 ? 268 GLY B CA  1 
ATOM   5519 C C   . GLY B 1 268 ? -3.852  -25.774 28.398  1.00 122.38 ? 268 GLY B C   1 
ATOM   5520 O O   . GLY B 1 268 ? -4.329  -26.563 27.570  1.00 112.29 ? 268 GLY B O   1 
ATOM   5521 N N   . LEU B 1 269 ? -3.554  -26.096 29.664  1.00 126.35 ? 269 LEU B N   1 
ATOM   5522 C CA  . LEU B 1 269 ? -3.587  -27.456 30.185  1.00 138.02 ? 269 LEU B CA  1 
ATOM   5523 C C   . LEU B 1 269 ? -4.504  -27.552 31.410  1.00 136.42 ? 269 LEU B C   1 
ATOM   5524 O O   . LEU B 1 269 ? -4.368  -26.772 32.348  1.00 134.65 ? 269 LEU B O   1 
ATOM   5525 C CB  . LEU B 1 269 ? -2.200  -27.958 30.564  1.00 152.37 ? 269 LEU B CB  1 
ATOM   5526 C CG  . LEU B 1 269 ? -2.166  -29.468 30.832  1.00 191.35 ? 269 LEU B CG  1 
ATOM   5527 C CD1 . LEU B 1 269 ? -1.921  -30.286 29.553  1.00 246.26 ? 269 LEU B CD1 1 
ATOM   5528 C CD2 . LEU B 1 269 ? -1.261  -29.895 31.973  1.00 217.92 ? 269 LEU B CD2 1 
ATOM   5529 N N   . GLY B 1 270 ? -5.429  -28.504 31.345  1.00 138.90 ? 270 GLY B N   1 
ATOM   5530 C CA  . GLY B 1 270 ? -6.566  -28.565 32.242  1.00 159.63 ? 270 GLY B CA  1 
ATOM   5531 C C   . GLY B 1 270 ? -6.801  -29.987 32.728  1.00 161.41 ? 270 GLY B C   1 
ATOM   5532 O O   . GLY B 1 270 ? -6.706  -30.977 31.979  1.00 158.74 ? 270 GLY B O   1 
ATOM   5533 N N   . HIS B 1 271 ? -7.196  -30.051 34.003  1.00 171.05 ? 271 HIS B N   1 
ATOM   5534 C CA  . HIS B 1 271 ? -7.537  -31.297 34.683  1.00 185.96 ? 271 HIS B CA  1 
ATOM   5535 C C   . HIS B 1 271 ? -8.927  -31.193 35.322  1.00 173.78 ? 271 HIS B C   1 
ATOM   5536 O O   . HIS B 1 271 ? -9.231  -30.238 36.037  1.00 151.93 ? 271 HIS B O   1 
ATOM   5537 C CB  . HIS B 1 271 ? -6.410  -31.685 35.652  1.00 213.23 ? 271 HIS B CB  1 
ATOM   5538 C CG  . HIS B 1 271 ? -6.706  -32.769 36.639  1.00 231.46 ? 271 HIS B CG  1 
ATOM   5539 N ND1 . HIS B 1 271 ? -7.047  -32.488 37.945  1.00 259.56 ? 271 HIS B ND1 1 
ATOM   5540 C CD2 . HIS B 1 271 ? -6.668  -34.108 36.552  1.00 217.36 ? 271 HIS B CD2 1 
ATOM   5541 C CE1 . HIS B 1 271 ? -7.228  -33.621 38.613  1.00 245.82 ? 271 HIS B CE1 1 
ATOM   5542 N NE2 . HIS B 1 271 ? -7.004  -34.622 37.783  1.00 217.33 ? 271 HIS B NE2 1 
ATOM   5543 N N   . ILE B 1 272 ? -9.774  -32.168 34.970  1.00 190.28 ? 272 ILE B N   1 
ATOM   5544 C CA  . ILE B 1 272 ? -11.050 -32.390 35.635  1.00 203.32 ? 272 ILE B CA  1 
ATOM   5545 C C   . ILE B 1 272 ? -10.888 -33.528 36.642  1.00 209.24 ? 272 ILE B C   1 
ATOM   5546 O O   . ILE B 1 272 ? -10.505 -34.638 36.251  1.00 186.65 ? 272 ILE B O   1 
ATOM   5547 C CB  . ILE B 1 272 ? -12.120 -32.799 34.602  1.00 207.84 ? 272 ILE B CB  1 
ATOM   5548 C CG1 . ILE B 1 272 ? -11.835 -32.279 33.182  1.00 236.37 ? 272 ILE B CG1 1 
ATOM   5549 C CG2 . ILE B 1 272 ? -13.523 -32.448 35.090  1.00 192.32 ? 272 ILE B CG2 1 
ATOM   5550 C CD1 . ILE B 1 272 ? -12.764 -31.180 32.707  1.00 259.39 ? 272 ILE B CD1 1 
ATOM   5551 N N   . GLU B 1 273 ? -11.237 -33.254 37.913  1.00 231.02 ? 273 GLU B N   1 
ATOM   5552 C CA  . GLU B 1 273 ? -11.336 -34.275 38.930  1.00 227.91 ? 273 GLU B CA  1 
ATOM   5553 C C   . GLU B 1 273 ? -12.551 -35.104 38.542  1.00 206.23 ? 273 GLU B C   1 
ATOM   5554 O O   . GLU B 1 273 ? -13.257 -34.742 37.597  1.00 201.74 ? 273 GLU B O   1 
ATOM   5555 C CB  . GLU B 1 273 ? -11.331 -33.632 40.317  1.00 232.19 ? 273 GLU B CB  1 
ATOM   5556 C CG  . GLU B 1 273 ? -11.073 -34.642 41.431  1.00 240.03 ? 273 GLU B CG  1 
ATOM   5557 C CD  . GLU B 1 273 ? -11.146 -34.026 42.815  1.00 249.26 ? 273 GLU B CD  1 
ATOM   5558 O OE1 . GLU B 1 273 ? -11.217 -32.779 42.910  1.00 238.68 ? 273 GLU B OE1 1 
ATOM   5559 O OE2 . GLU B 1 273 ? -11.147 -34.805 43.795  1.00 268.78 ? 273 GLU B OE2 1 
ATOM   5560 N N   . ARG B 1 274 ? -12.749 -36.208 39.257  1.00 193.22 ? 274 ARG B N   1 
ATOM   5561 C CA  . ARG B 1 274 ? -13.896 -37.084 39.057  1.00 211.39 ? 274 ARG B CA  1 
ATOM   5562 C C   . ARG B 1 274 ? -15.173 -36.413 39.576  1.00 231.63 ? 274 ARG B C   1 
ATOM   5563 O O   . ARG B 1 274 ? -16.273 -36.745 39.140  1.00 217.92 ? 274 ARG B O   1 
ATOM   5564 C CB  . ARG B 1 274 ? -13.666 -38.476 39.652  1.00 208.23 ? 274 ARG B CB  1 
ATOM   5565 C CG  . ARG B 1 274 ? -13.495 -38.339 41.154  1.00 231.14 ? 274 ARG B CG  1 
ATOM   5566 C CD  . ARG B 1 274 ? -13.370 -39.610 41.968  1.00 234.38 ? 274 ARG B CD  1 
ATOM   5567 N NE  . ARG B 1 274 ? -13.503 -39.273 43.390  1.00 249.01 ? 274 ARG B NE  1 
ATOM   5568 C CZ  . ARG B 1 274 ? -12.711 -38.459 44.090  1.00 262.91 ? 274 ARG B CZ  1 
ATOM   5569 N NH1 . ARG B 1 274 ? -11.629 -37.931 43.541  1.00 287.21 ? 274 ARG B NH1 1 
ATOM   5570 N NH2 . ARG B 1 274 ? -13.006 -38.184 45.346  1.00 260.64 ? 274 ARG B NH2 1 
ATOM   5571 N N   . ASP B 1 275 ? -15.023 -35.463 40.510  1.00 230.83 ? 275 ASP B N   1 
ATOM   5572 C CA  . ASP B 1 275 ? -16.156 -34.728 41.047  1.00 202.86 ? 275 ASP B CA  1 
ATOM   5573 C C   . ASP B 1 275 ? -16.348 -33.420 40.280  1.00 195.11 ? 275 ASP B C   1 
ATOM   5574 O O   . ASP B 1 275 ? -16.933 -32.480 40.813  1.00 225.07 ? 275 ASP B O   1 
ATOM   5575 C CB  . ASP B 1 275 ? -16.066 -34.559 42.559  1.00 192.97 ? 275 ASP B CB  1 
ATOM   5576 C CG  . ASP B 1 275 ? -14.822 -33.861 43.092  1.00 191.80 ? 275 ASP B CG  1 
ATOM   5577 O OD1 . ASP B 1 275 ? -14.484 -32.768 42.573  1.00 206.51 ? 275 ASP B OD1 1 
ATOM   5578 O OD2 . ASP B 1 275 ? -14.213 -34.410 44.040  1.00 179.13 ? 275 ASP B OD2 1 
ATOM   5579 N N   . GLY B 1 276 ? -15.855 -33.370 39.037  1.00 170.36 ? 276 GLY B N   1 
ATOM   5580 C CA  . GLY B 1 276 ? -16.105 -32.256 38.138  1.00 180.88 ? 276 GLY B CA  1 
ATOM   5581 C C   . GLY B 1 276 ? -15.207 -31.043 38.364  1.00 197.90 ? 276 GLY B C   1 
ATOM   5582 O O   . GLY B 1 276 ? -15.269 -30.087 37.581  1.00 197.84 ? 276 GLY B O   1 
ATOM   5583 N N   . THR B 1 277 ? -14.385 -31.105 39.421  1.00 220.42 ? 277 THR B N   1 
ATOM   5584 C CA  . THR B 1 277 ? -13.522 -29.992 39.792  1.00 249.45 ? 277 THR B CA  1 
ATOM   5585 C C   . THR B 1 277 ? -12.511 -29.756 38.673  1.00 256.81 ? 277 THR B C   1 
ATOM   5586 O O   . THR B 1 277 ? -11.730 -30.654 38.368  1.00 288.98 ? 277 THR B O   1 
ATOM   5587 C CB  . THR B 1 277 ? -12.859 -30.243 41.150  1.00 272.88 ? 277 THR B CB  1 
ATOM   5588 O OG1 . THR B 1 277 ? -13.919 -30.118 42.096  1.00 263.28 ? 277 THR B OG1 1 
ATOM   5589 C CG2 . THR B 1 277 ? -11.775 -29.227 41.472  1.00 268.73 ? 277 THR B CG2 1 
ATOM   5590 N N   . VAL B 1 278 ? -12.586 -28.568 38.054  1.00 220.32 ? 278 VAL B N   1 
ATOM   5591 C CA  . VAL B 1 278 ? -11.686 -28.160 37.003  1.00 214.12 ? 278 VAL B CA  1 
ATOM   5592 C C   . VAL B 1 278 ? -10.524 -27.398 37.634  1.00 220.86 ? 278 VAL B C   1 
ATOM   5593 O O   . VAL B 1 278 ? -10.720 -26.548 38.515  1.00 233.79 ? 278 VAL B O   1 
ATOM   5594 C CB  . VAL B 1 278 ? -12.386 -27.281 35.947  1.00 205.55 ? 278 VAL B CB  1 
ATOM   5595 C CG1 . VAL B 1 278 ? -11.450 -26.976 34.780  1.00 241.05 ? 278 VAL B CG1 1 
ATOM   5596 C CG2 . VAL B 1 278 ? -13.656 -27.926 35.417  1.00 200.97 ? 278 VAL B CG2 1 
ATOM   5597 N N   . ARG B 1 279 ? -9.319  -27.708 37.141  1.00 204.75 ? 279 ARG B N   1 
ATOM   5598 C CA  . ARG B 1 279 ? -8.101  -27.017 37.531  1.00 179.89 ? 279 ARG B CA  1 
ATOM   5599 C C   . ARG B 1 279 ? -7.340  -26.535 36.289  1.00 168.77 ? 279 ARG B C   1 
ATOM   5600 O O   . ARG B 1 279 ? -7.121  -27.282 35.329  1.00 148.05 ? 279 ARG B O   1 
ATOM   5601 C CB  . ARG B 1 279 ? -7.335  -27.863 38.554  1.00 201.42 ? 279 ARG B CB  1 
ATOM   5602 C CG  . ARG B 1 279 ? -7.948  -27.778 39.947  1.00 215.93 ? 279 ARG B CG  1 
ATOM   5603 C CD  . ARG B 1 279 ? -7.423  -28.783 40.964  1.00 265.97 ? 279 ARG B CD  1 
ATOM   5604 N NE  . ARG B 1 279 ? -7.841  -30.186 40.818  1.00 297.00 ? 279 ARG B NE  1 
ATOM   5605 C CZ  . ARG B 1 279 ? -7.332  -31.193 41.524  1.00 319.64 ? 279 ARG B CZ  1 
ATOM   5606 N NH1 . ARG B 1 279 ? -6.298  -30.988 42.322  1.00 337.47 ? 279 ARG B NH1 1 
ATOM   5607 N NH2 . ARG B 1 279 ? -7.838  -32.408 41.445  1.00 311.94 ? 279 ARG B NH2 1 
ATOM   5608 N N   . VAL B 1 280 ? -6.999  -25.241 36.312  1.00 186.30 ? 280 VAL B N   1 
ATOM   5609 C CA  . VAL B 1 280 ? -6.046  -24.654 35.382  1.00 209.04 ? 280 VAL B CA  1 
ATOM   5610 C C   . VAL B 1 280 ? -4.701  -25.188 35.842  1.00 216.21 ? 280 VAL B C   1 
ATOM   5611 O O   . VAL B 1 280 ? -4.209  -24.770 36.886  1.00 222.06 ? 280 VAL B O   1 
ATOM   5612 C CB  . VAL B 1 280 ? -6.060  -23.110 35.413  1.00 199.77 ? 280 VAL B CB  1 
ATOM   5613 C CG1 . VAL B 1 280 ? -5.841  -22.568 36.822  1.00 189.24 ? 280 VAL B CG1 1 
ATOM   5614 C CG2 . VAL B 1 280 ? -5.042  -22.511 34.450  1.00 174.82 ? 280 VAL B CG2 1 
ATOM   5615 N N   . VAL B 1 281 ? -4.180  -26.186 35.127  1.00 193.50 ? 281 VAL B N   1 
ATOM   5616 C CA  . VAL B 1 281 ? -2.917  -26.758 35.549  1.00 167.44 ? 281 VAL B CA  1 
ATOM   5617 C C   . VAL B 1 281 ? -1.827  -25.756 35.197  1.00 177.48 ? 281 VAL B C   1 
ATOM   5618 O O   . VAL B 1 281 ? -1.160  -25.251 36.098  1.00 217.62 ? 281 VAL B O   1 
ATOM   5619 C CB  . VAL B 1 281 ? -2.601  -28.168 35.025  1.00 176.42 ? 281 VAL B CB  1 
ATOM   5620 C CG1 . VAL B 1 281 ? -1.334  -28.711 35.664  1.00 219.58 ? 281 VAL B CG1 1 
ATOM   5621 C CG2 . VAL B 1 281 ? -3.750  -29.134 35.281  1.00 183.09 ? 281 VAL B CG2 1 
ATOM   5622 N N   . ALA B 1 282 ? -1.692  -25.451 33.900  1.00 171.10 ? 282 ALA B N   1 
ATOM   5623 C CA  . ALA B 1 282 ? -0.655  -24.523 33.471  1.00 183.72 ? 282 ALA B CA  1 
ATOM   5624 C C   . ALA B 1 282 ? -0.940  -23.925 32.095  1.00 179.02 ? 282 ALA B C   1 
ATOM   5625 O O   . ALA B 1 282 ? -1.735  -24.442 31.307  1.00 186.47 ? 282 ALA B O   1 
ATOM   5626 C CB  . ALA B 1 282 ? 0.707   -25.198 33.506  1.00 208.61 ? 282 ALA B CB  1 
ATOM   5627 N N   . CYS B 1 283 ? -0.230  -22.825 31.825  1.00 156.37 ? 283 CYS B N   1 
ATOM   5628 C CA  . CYS B 1 283 ? -0.220  -22.176 30.527  1.00 155.73 ? 283 CYS B CA  1 
ATOM   5629 C C   . CYS B 1 283 ? 1.216   -21.970 30.051  1.00 154.56 ? 283 CYS B C   1 
ATOM   5630 O O   . CYS B 1 283 ? 2.073   -21.476 30.784  1.00 162.67 ? 283 CYS B O   1 
ATOM   5631 C CB  . CYS B 1 283 ? -0.952  -20.847 30.594  1.00 184.33 ? 283 CYS B CB  1 
ATOM   5632 S SG  . CYS B 1 283 ? -2.603  -21.052 31.305  1.00 233.74 ? 283 CYS B SG  1 
ATOM   5633 N N   . HIS B 1 284 ? 1.446   -22.367 28.798  1.00 144.30 ? 284 HIS B N   1 
ATOM   5634 C CA  . HIS B 1 284 ? 2.726   -22.237 28.122  1.00 149.69 ? 284 HIS B CA  1 
ATOM   5635 C C   . HIS B 1 284 ? 2.556   -21.530 26.776  1.00 151.96 ? 284 HIS B C   1 
ATOM   5636 O O   . HIS B 1 284 ? 1.451   -21.270 26.304  1.00 155.32 ? 284 HIS B O   1 
ATOM   5637 C CB  . HIS B 1 284 ? 3.305   -23.614 27.762  1.00 158.63 ? 284 HIS B CB  1 
ATOM   5638 C CG  . HIS B 1 284 ? 3.344   -24.648 28.846  1.00 160.00 ? 284 HIS B CG  1 
ATOM   5639 N ND1 . HIS B 1 284 ? 2.213   -25.264 29.336  1.00 170.27 ? 284 HIS B ND1 1 
ATOM   5640 C CD2 . HIS B 1 284 ? 4.372   -25.196 29.508  1.00 142.24 ? 284 HIS B CD2 1 
ATOM   5641 C CE1 . HIS B 1 284 ? 2.561   -26.138 30.271  1.00 147.51 ? 284 HIS B CE1 1 
ATOM   5642 N NE2 . HIS B 1 284 ? 3.866   -26.105 30.400  1.00 130.98 ? 284 HIS B NE2 1 
ATOM   5643 N N   . ASP B 1 285 ? 3.711   -21.290 26.148  1.00 149.66 ? 285 ASP B N   1 
ATOM   5644 C CA  . ASP B 1 285 ? 3.882   -20.724 24.822  1.00 155.00 ? 285 ASP B CA  1 
ATOM   5645 C C   . ASP B 1 285 ? 4.579   -21.745 23.928  1.00 162.01 ? 285 ASP B C   1 
ATOM   5646 O O   . ASP B 1 285 ? 5.793   -21.684 23.714  1.00 151.47 ? 285 ASP B O   1 
ATOM   5647 C CB  . ASP B 1 285 ? 4.607   -19.389 24.877  1.00 159.30 ? 285 ASP B CB  1 
ATOM   5648 C CG  . ASP B 1 285 ? 3.778   -18.151 24.581  1.00 176.19 ? 285 ASP B CG  1 
ATOM   5649 O OD1 . ASP B 1 285 ? 3.373   -17.995 23.398  1.00 220.44 ? 285 ASP B OD1 1 
ATOM   5650 O OD2 . ASP B 1 285 ? 3.567   -17.360 25.523  1.00 155.29 ? 285 ASP B OD2 1 
ATOM   5651 N N   . GLN B 1 286 ? 3.767   -22.689 23.439  1.00 179.38 ? 286 GLN B N   1 
ATOM   5652 C CA  . GLN B 1 286 ? 4.173   -23.675 22.455  1.00 174.40 ? 286 GLN B CA  1 
ATOM   5653 C C   . GLN B 1 286 ? 4.700   -22.961 21.220  1.00 183.13 ? 286 GLN B C   1 
ATOM   5654 O O   . GLN B 1 286 ? 4.370   -21.802 20.966  1.00 223.94 ? 286 GLN B O   1 
ATOM   5655 C CB  . GLN B 1 286 ? 3.013   -24.538 21.958  1.00 150.27 ? 286 GLN B CB  1 
ATOM   5656 C CG  . GLN B 1 286 ? 2.286   -25.325 23.040  1.00 164.58 ? 286 GLN B CG  1 
ATOM   5657 C CD  . GLN B 1 286 ? 1.251   -26.256 22.453  1.00 181.74 ? 286 GLN B CD  1 
ATOM   5658 O OE1 . GLN B 1 286 ? 1.130   -26.349 21.226  1.00 174.71 ? 286 GLN B OE1 1 
ATOM   5659 N NE2 . GLN B 1 286 ? 0.483   -26.934 23.299  1.00 189.22 ? 286 GLN B NE2 1 
ATOM   5660 N N   . VAL B 1 287 ? 5.501   -23.694 20.456  1.00 169.23 ? 287 VAL B N   1 
ATOM   5661 C CA  . VAL B 1 287 ? 5.923   -23.270 19.138  1.00 183.39 ? 287 VAL B CA  1 
ATOM   5662 C C   . VAL B 1 287 ? 5.699   -24.447 18.194  1.00 202.67 ? 287 VAL B C   1 
ATOM   5663 O O   . VAL B 1 287 ? 6.505   -25.366 18.172  1.00 228.15 ? 287 VAL B O   1 
ATOM   5664 C CB  . VAL B 1 287 ? 7.388   -22.785 19.200  1.00 164.69 ? 287 VAL B CB  1 
ATOM   5665 C CG1 . VAL B 1 287 ? 8.273   -23.624 20.121  1.00 117.87 ? 287 VAL B CG1 1 
ATOM   5666 C CG2 . VAL B 1 287 ? 8.009   -22.589 17.818  1.00 165.10 ? 287 VAL B CG2 1 
ATOM   5667 N N   . LEU B 1 288 ? 4.585   -24.432 17.450  1.00 222.05 ? 288 LEU B N   1 
ATOM   5668 C CA  . LEU B 1 288 ? 4.203   -25.548 16.589  1.00 244.80 ? 288 LEU B CA  1 
ATOM   5669 C C   . LEU B 1 288 ? 5.447   -26.097 15.897  1.00 280.92 ? 288 LEU B C   1 
ATOM   5670 O O   . LEU B 1 288 ? 5.695   -27.301 15.942  1.00 318.24 ? 288 LEU B O   1 
ATOM   5671 C CB  . LEU B 1 288 ? 3.105   -25.222 15.572  1.00 249.74 ? 288 LEU B CB  1 
ATOM   5672 C CG  . LEU B 1 288 ? 1.798   -24.637 16.116  1.00 240.20 ? 288 LEU B CG  1 
ATOM   5673 C CD1 . LEU B 1 288 ? 0.779   -24.290 15.029  1.00 192.79 ? 288 LEU B CD1 1 
ATOM   5674 C CD2 . LEU B 1 288 ? 1.199   -25.578 17.135  1.00 232.53 ? 288 LEU B CD2 1 
ATOM   5675 N N   . SER B 1 289 ? 6.237   -25.185 15.307  1.00 310.41 ? 289 SER B N   1 
ATOM   5676 C CA  . SER B 1 289 ? 7.518   -25.489 14.687  1.00 345.26 ? 289 SER B CA  1 
ATOM   5677 C C   . SER B 1 289 ? 7.393   -26.732 13.811  1.00 342.33 ? 289 SER B C   1 
ATOM   5678 O O   . SER B 1 289 ? 8.013   -27.761 14.097  1.00 408.51 ? 289 SER B O   1 
ATOM   5679 C CB  . SER B 1 289 ? 8.611   -25.644 15.717  1.00 391.22 ? 289 SER B CB  1 
ATOM   5680 O OG  . SER B 1 289 ? 8.311   -26.710 16.614  1.00 485.06 ? 289 SER B OG  1 
ATOM   5681 N N   . GLY B 1 290 ? 6.569   -26.615 12.759  1.00 294.23 ? 290 GLY B N   1 
ATOM   5682 C CA  . GLY B 1 290 ? 6.216   -27.729 11.894  1.00 278.88 ? 290 GLY B CA  1 
ATOM   5683 C C   . GLY B 1 290 ? 5.349   -28.758 12.620  1.00 250.87 ? 290 GLY B C   1 
ATOM   5684 O O   . GLY B 1 290 ? 5.247   -29.913 12.198  1.00 260.98 ? 290 GLY B O   1 
ATOM   5685 N N   . GLY B 1 291 ? 4.766   -28.333 13.746  1.00 217.07 ? 291 GLY B N   1 
ATOM   5686 C CA  . GLY B 1 291 ? 3.832   -29.152 14.499  1.00 208.47 ? 291 GLY B CA  1 
ATOM   5687 C C   . GLY B 1 291 ? 4.483   -30.308 15.270  1.00 253.50 ? 291 GLY B C   1 
ATOM   5688 O O   . GLY B 1 291 ? 3.790   -30.932 16.068  1.00 273.31 ? 291 GLY B O   1 
ATOM   5689 N N   . GLN B 1 292 ? 5.779   -30.608 15.039  1.00 282.86 ? 292 GLN B N   1 
ATOM   5690 C CA  . GLN B 1 292 ? 6.517   -31.619 15.802  1.00 261.40 ? 292 GLN B CA  1 
ATOM   5691 C C   . GLN B 1 292 ? 6.866   -31.080 17.200  1.00 245.46 ? 292 GLN B C   1 
ATOM   5692 O O   . GLN B 1 292 ? 7.639   -31.701 17.937  1.00 234.65 ? 292 GLN B O   1 
ATOM   5693 C CB  . GLN B 1 292 ? 7.830   -32.087 15.158  1.00 256.44 ? 292 GLN B CB  1 
ATOM   5694 C CG  . GLN B 1 292 ? 7.776   -32.331 13.652  1.00 242.35 ? 292 GLN B CG  1 
ATOM   5695 C CD  . GLN B 1 292 ? 7.074   -33.610 13.256  1.00 242.40 ? 292 GLN B CD  1 
ATOM   5696 O OE1 . GLN B 1 292 ? 6.034   -33.573 12.592  1.00 267.41 ? 292 GLN B OE1 1 
ATOM   5697 N NE2 . GLN B 1 292 ? 7.632   -34.753 13.631  1.00 210.70 ? 292 GLN B NE2 1 
ATOM   5698 N N   . TYR B 1 293 ? 6.310   -29.900 17.531  1.00 223.02 ? 293 TYR B N   1 
ATOM   5699 C CA  . TYR B 1 293 ? 6.420   -29.240 18.825  1.00 178.67 ? 293 TYR B CA  1 
ATOM   5700 C C   . TYR B 1 293 ? 7.832   -29.405 19.375  1.00 177.42 ? 293 TYR B C   1 
ATOM   5701 O O   . TYR B 1 293 ? 8.020   -29.872 20.493  1.00 178.82 ? 293 TYR B O   1 
ATOM   5702 C CB  . TYR B 1 293 ? 5.272   -29.779 19.685  1.00 147.07 ? 293 TYR B CB  1 
ATOM   5703 C CG  . TYR B 1 293 ? 5.335   -29.499 21.178  1.00 140.43 ? 293 TYR B CG  1 
ATOM   5704 C CD1 . TYR B 1 293 ? 5.974   -30.383 22.042  1.00 152.46 ? 293 TYR B CD1 1 
ATOM   5705 C CD2 . TYR B 1 293 ? 4.699   -28.394 21.730  1.00 129.64 ? 293 TYR B CD2 1 
ATOM   5706 C CE1 . TYR B 1 293 ? 6.007   -30.158 23.410  1.00 157.08 ? 293 TYR B CE1 1 
ATOM   5707 C CE2 . TYR B 1 293 ? 4.724   -28.159 23.093  1.00 126.59 ? 293 TYR B CE2 1 
ATOM   5708 C CZ  . TYR B 1 293 ? 5.381   -29.036 23.932  1.00 140.13 ? 293 TYR B CZ  1 
ATOM   5709 O OH  . TYR B 1 293 ? 5.411   -28.762 25.256  1.00 156.10 ? 293 TYR B OH  1 
ATOM   5710 N N   . TRP B 1 294 ? 8.827   -29.063 18.560  1.00 194.03 ? 294 TRP B N   1 
ATOM   5711 C CA  . TRP B 1 294 ? 10.180  -29.283 19.021  1.00 220.47 ? 294 TRP B CA  1 
ATOM   5712 C C   . TRP B 1 294 ? 10.387  -28.580 20.364  1.00 223.97 ? 294 TRP B C   1 
ATOM   5713 O O   . TRP B 1 294 ? 11.507  -28.575 20.875  1.00 251.23 ? 294 TRP B O   1 
ATOM   5714 C CB  . TRP B 1 294 ? 11.218  -28.920 17.945  1.00 204.70 ? 294 TRP B CB  1 
ATOM   5715 C CG  . TRP B 1 294 ? 11.043  -29.712 16.674  1.00 195.26 ? 294 TRP B CG  1 
ATOM   5716 C CD1 . TRP B 1 294 ? 10.462  -29.263 15.524  1.00 207.85 ? 294 TRP B CD1 1 
ATOM   5717 C CD2 . TRP B 1 294 ? 11.396  -31.090 16.430  1.00 181.11 ? 294 TRP B CD2 1 
ATOM   5718 N NE1 . TRP B 1 294 ? 10.445  -30.249 14.579  1.00 230.83 ? 294 TRP B NE1 1 
ATOM   5719 C CE2 . TRP B 1 294 ? 11.009  -31.383 15.103  1.00 210.17 ? 294 TRP B CE2 1 
ATOM   5720 C CE3 . TRP B 1 294 ? 12.014  -32.093 17.178  1.00 160.00 ? 294 TRP B CE3 1 
ATOM   5721 C CZ2 . TRP B 1 294 ? 11.209  -32.635 14.524  1.00 219.01 ? 294 TRP B CZ2 1 
ATOM   5722 C CZ3 . TRP B 1 294 ? 12.225  -33.325 16.604  1.00 210.37 ? 294 TRP B CZ3 1 
ATOM   5723 C CH2 . TRP B 1 294 ? 11.834  -33.588 15.291  1.00 225.97 ? 294 TRP B CH2 1 
ATOM   5724 N N   . GLY B 1 295 ? 9.293   -28.072 20.947  1.00 194.13 ? 295 GLY B N   1 
ATOM   5725 C CA  . GLY B 1 295 ? 9.253   -27.719 22.366  1.00 192.08 ? 295 GLY B CA  1 
ATOM   5726 C C   . GLY B 1 295 ? 8.228   -26.661 22.781  1.00 180.28 ? 295 GLY B C   1 
ATOM   5727 O O   . GLY B 1 295 ? 7.257   -26.422 22.073  1.00 154.50 ? 295 GLY B O   1 
ATOM   5728 N N   . CYS B 1 296 ? 8.438   -26.091 23.972  1.00 168.95 ? 296 CYS B N   1 
ATOM   5729 C CA  . CYS B 1 296 ? 7.619   -25.032 24.537  1.00 130.37 ? 296 CYS B CA  1 
ATOM   5730 C C   . CYS B 1 296 ? 8.248   -24.391 25.791  1.00 129.77 ? 296 CYS B C   1 
ATOM   5731 O O   . CYS B 1 296 ? 9.196   -24.918 26.397  1.00 104.06 ? 296 CYS B O   1 
ATOM   5732 C CB  . CYS B 1 296 ? 6.274   -25.612 24.933  1.00 122.97 ? 296 CYS B CB  1 
ATOM   5733 S SG  . CYS B 1 296 ? 6.297   -26.313 26.593  1.00 167.83 ? 296 CYS B SG  1 
ATOM   5734 N N   . ARG B 1 297 ? 7.654   -23.261 26.206  1.00 148.31 ? 297 ARG B N   1 
ATOM   5735 C CA  . ARG B 1 297 ? 8.135   -22.450 27.310  1.00 167.78 ? 297 ARG B CA  1 
ATOM   5736 C C   . ARG B 1 297 ? 7.039   -22.081 28.306  1.00 167.94 ? 297 ARG B C   1 
ATOM   5737 O O   . ARG B 1 297 ? 5.882   -21.849 27.960  1.00 160.81 ? 297 ARG B O   1 
ATOM   5738 C CB  . ARG B 1 297 ? 8.653   -21.049 26.962  1.00 156.19 ? 297 ARG B CB  1 
ATOM   5739 C CG  . ARG B 1 297 ? 10.050  -20.927 26.376  1.00 179.55 ? 297 ARG B CG  1 
ATOM   5740 C CD  . ARG B 1 297 ? 10.659  -19.513 26.555  1.00 160.24 ? 297 ARG B CD  1 
ATOM   5741 N NE  . ARG B 1 297 ? 11.218  -18.977 25.305  1.00 169.28 ? 297 ARG B NE  1 
ATOM   5742 C CZ  . ARG B 1 297 ? 11.520  -19.628 24.174  1.00 181.55 ? 297 ARG B CZ  1 
ATOM   5743 N NH1 . ARG B 1 297 ? 11.642  -18.966 23.036  1.00 185.56 ? 297 ARG B NH1 1 
ATOM   5744 N NH2 . ARG B 1 297 ? 11.631  -20.945 24.147  1.00 232.29 ? 297 ARG B NH2 1 
ATOM   5745 N N   . PHE B 1 298 ? 7.476   -21.894 29.550  1.00 172.94 ? 298 PHE B N   1 
ATOM   5746 C CA  . PHE B 1 298 ? 6.617   -21.497 30.664  1.00 182.18 ? 298 PHE B CA  1 
ATOM   5747 C C   . PHE B 1 298 ? 7.198   -20.337 31.479  1.00 184.23 ? 298 PHE B C   1 
ATOM   5748 O O   . PHE B 1 298 ? 8.407   -20.239 31.709  1.00 165.86 ? 298 PHE B O   1 
ATOM   5749 C CB  . PHE B 1 298 ? 6.267   -22.716 31.521  1.00 199.79 ? 298 PHE B CB  1 
ATOM   5750 C CG  . PHE B 1 298 ? 5.559   -22.404 32.830  1.00 181.41 ? 298 PHE B CG  1 
ATOM   5751 C CD1 . PHE B 1 298 ? 6.298   -22.110 33.967  1.00 178.08 ? 298 PHE B CD1 1 
ATOM   5752 C CD2 . PHE B 1 298 ? 4.171   -22.414 32.916  1.00 170.27 ? 298 PHE B CD2 1 
ATOM   5753 C CE1 . PHE B 1 298 ? 5.663   -21.843 35.162  1.00 169.53 ? 298 PHE B CE1 1 
ATOM   5754 C CE2 . PHE B 1 298 ? 3.538   -22.129 34.112  1.00 174.27 ? 298 PHE B CE2 1 
ATOM   5755 C CZ  . PHE B 1 298 ? 4.286   -21.857 35.232  1.00 169.22 ? 298 PHE B CZ  1 
ATOM   5756 N N   . PRO B 1 299 ? 6.341   -19.448 32.059  1.00 200.07 ? 299 PRO B N   1 
ATOM   5757 C CA  . PRO B 1 299 ? 4.891   -19.436 31.807  1.00 193.67 ? 299 PRO B CA  1 
ATOM   5758 C C   . PRO B 1 299 ? 4.544   -18.801 30.466  1.00 200.59 ? 299 PRO B C   1 
ATOM   5759 O O   . PRO B 1 299 ? 5.432   -18.428 29.701  1.00 244.36 ? 299 PRO B O   1 
ATOM   5760 C CB  . PRO B 1 299 ? 4.273   -18.640 32.959  1.00 169.13 ? 299 PRO B CB  1 
ATOM   5761 C CG  . PRO B 1 299 ? 5.416   -17.762 33.436  1.00 174.89 ? 299 PRO B CG  1 
ATOM   5762 C CD  . PRO B 1 299 ? 6.735   -18.439 33.059  1.00 177.79 ? 299 PRO B CD  1 
ATOM   5763 N N   . ALA B 1 300 ? 3.245   -18.692 30.182  1.00 181.67 ? 300 ALA B N   1 
ATOM   5764 C CA  . ALA B 1 300 ? 2.838   -18.045 28.949  1.00 189.91 ? 300 ALA B CA  1 
ATOM   5765 C C   . ALA B 1 300 ? 3.248   -16.579 29.019  1.00 202.30 ? 300 ALA B C   1 
ATOM   5766 O O   . ALA B 1 300 ? 3.616   -16.088 30.086  1.00 194.40 ? 300 ALA B O   1 
ATOM   5767 C CB  . ALA B 1 300 ? 1.352   -18.204 28.743  1.00 199.43 ? 300 ALA B CB  1 
ATOM   5768 N N   . ASP B 1 301 ? 3.189   -15.902 27.868  1.00 222.28 ? 301 ASP B N   1 
ATOM   5769 C CA  . ASP B 1 301 ? 3.490   -14.481 27.801  1.00 236.07 ? 301 ASP B CA  1 
ATOM   5770 C C   . ASP B 1 301 ? 2.532   -13.727 28.716  1.00 229.89 ? 301 ASP B C   1 
ATOM   5771 O O   . ASP B 1 301 ? 1.336   -14.012 28.736  1.00 241.54 ? 301 ASP B O   1 
ATOM   5772 C CB  . ASP B 1 301 ? 3.522   -13.991 26.363  1.00 248.98 ? 301 ASP B CB  1 
ATOM   5773 C CG  . ASP B 1 301 ? 3.862   -12.522 26.146  1.00 267.04 ? 301 ASP B CG  1 
ATOM   5774 O OD1 . ASP B 1 301 ? 3.784   -11.737 27.113  1.00 258.63 ? 301 ASP B OD1 1 
ATOM   5775 O OD2 . ASP B 1 301 ? 4.204   -12.175 24.994  1.00 293.75 ? 301 ASP B OD2 1 
ATOM   5776 N N   . GLU B 1 302 ? 3.098   -12.775 29.471  1.00 226.56 ? 302 GLU B N   1 
ATOM   5777 C CA  . GLU B 1 302 ? 2.424   -12.018 30.516  1.00 234.38 ? 302 GLU B CA  1 
ATOM   5778 C C   . GLU B 1 302 ? 1.093   -11.448 30.022  1.00 233.44 ? 302 GLU B C   1 
ATOM   5779 O O   . GLU B 1 302 ? 0.111   -11.470 30.762  1.00 246.53 ? 302 GLU B O   1 
ATOM   5780 C CB  . GLU B 1 302 ? 3.354   -10.942 31.079  1.00 229.98 ? 302 GLU B CB  1 
ATOM   5781 C CG  . GLU B 1 302 ? 3.997   -10.081 29.994  1.00 235.32 ? 302 GLU B CG  1 
ATOM   5782 C CD  . GLU B 1 302 ? 4.999   -9.059  30.475  1.00 247.44 ? 302 GLU B CD  1 
ATOM   5783 O OE1 . GLU B 1 302 ? 4.591   -8.082  31.143  1.00 254.11 ? 302 GLU B OE1 1 
ATOM   5784 O OE2 . GLU B 1 302 ? 6.191   -9.253  30.156  1.00 260.98 ? 302 GLU B OE2 1 
ATOM   5785 N N   . ARG B 1 303 ? 1.086   -10.934 28.782  1.00 215.45 ? 303 ARG B N   1 
ATOM   5786 C CA  . ARG B 1 303 ? -0.071  -10.269 28.199  1.00 191.53 ? 303 ARG B CA  1 
ATOM   5787 C C   . ARG B 1 303 ? -1.246  -11.234 28.079  1.00 194.18 ? 303 ARG B C   1 
ATOM   5788 O O   . ARG B 1 303 ? -2.316  -10.967 28.612  1.00 189.64 ? 303 ARG B O   1 
ATOM   5789 C CB  . ARG B 1 303 ? 0.268   -9.718  26.814  1.00 185.91 ? 303 ARG B CB  1 
ATOM   5790 C CG  . ARG B 1 303 ? 0.987   -8.382  26.815  1.00 212.02 ? 303 ARG B CG  1 
ATOM   5791 C CD  . ARG B 1 303 ? 2.063   -8.366  25.747  1.00 219.33 ? 303 ARG B CD  1 
ATOM   5792 N NE  . ARG B 1 303 ? 3.305   -8.977  26.238  1.00 248.26 ? 303 ARG B NE  1 
ATOM   5793 C CZ  . ARG B 1 303 ? 4.428   -9.071  25.530  1.00 245.27 ? 303 ARG B CZ  1 
ATOM   5794 N NH1 . ARG B 1 303 ? 4.458   -8.636  24.280  1.00 235.19 ? 303 ARG B NH1 1 
ATOM   5795 N NH2 . ARG B 1 303 ? 5.512   -9.606  26.074  1.00 239.14 ? 303 ARG B NH2 1 
ATOM   5796 N N   . TRP B 1 304 ? -1.036  -12.352 27.377  1.00 214.35 ? 304 TRP B N   1 
ATOM   5797 C CA  . TRP B 1 304 ? -2.117  -13.287 27.121  1.00 208.80 ? 304 TRP B CA  1 
ATOM   5798 C C   . TRP B 1 304 ? -2.087  -14.484 28.061  1.00 207.43 ? 304 TRP B C   1 
ATOM   5799 O O   . TRP B 1 304 ? -2.749  -15.471 27.770  1.00 203.11 ? 304 TRP B O   1 
ATOM   5800 C CB  . TRP B 1 304 ? -2.178  -13.747 25.655  1.00 201.43 ? 304 TRP B CB  1 
ATOM   5801 C CG  . TRP B 1 304 ? -0.852  -13.915 24.952  1.00 203.28 ? 304 TRP B CG  1 
ATOM   5802 C CD1 . TRP B 1 304 ? -0.016  -14.999 24.921  1.00 176.23 ? 304 TRP B CD1 1 
ATOM   5803 C CD2 . TRP B 1 304 ? -0.237  -12.910 24.119  1.00 226.46 ? 304 TRP B CD2 1 
ATOM   5804 N NE1 . TRP B 1 304 ? 1.077   -14.730 24.143  1.00 177.70 ? 304 TRP B NE1 1 
ATOM   5805 C CE2 . TRP B 1 304 ? 0.969   -13.459 23.632  1.00 221.73 ? 304 TRP B CE2 1 
ATOM   5806 C CE3 . TRP B 1 304 ? -0.596  -11.608 23.740  1.00 246.67 ? 304 TRP B CE3 1 
ATOM   5807 C CZ2 . TRP B 1 304 ? 1.812   -12.730 22.789  1.00 245.90 ? 304 TRP B CZ2 1 
ATOM   5808 C CZ3 . TRP B 1 304 ? 0.239   -10.895 22.906  1.00 245.25 ? 304 TRP B CZ3 1 
ATOM   5809 C CH2 . TRP B 1 304 ? 1.431   -11.450 22.445  1.00 247.37 ? 304 TRP B CH2 1 
ATOM   5810 N N   . ARG B 1 305 ? -1.363  -14.407 29.184  1.00 209.77 ? 305 ARG B N   1 
ATOM   5811 C CA  . ARG B 1 305 ? -1.381  -15.554 30.076  1.00 224.15 ? 305 ARG B CA  1 
ATOM   5812 C C   . ARG B 1 305 ? -2.729  -15.527 30.769  1.00 250.73 ? 305 ARG B C   1 
ATOM   5813 O O   . ARG B 1 305 ? -3.523  -16.436 30.558  1.00 270.85 ? 305 ARG B O   1 
ATOM   5814 C CB  . ARG B 1 305 ? -0.223  -15.634 31.079  1.00 209.90 ? 305 ARG B CB  1 
ATOM   5815 C CG  . ARG B 1 305 ? -0.240  -16.872 31.964  1.00 187.33 ? 305 ARG B CG  1 
ATOM   5816 C CD  . ARG B 1 305 ? -0.554  -16.635 33.432  1.00 179.95 ? 305 ARG B CD  1 
ATOM   5817 N NE  . ARG B 1 305 ? -0.755  -17.936 34.082  1.00 199.18 ? 305 ARG B NE  1 
ATOM   5818 C CZ  . ARG B 1 305 ? -1.822  -18.295 34.798  1.00 212.44 ? 305 ARG B CZ  1 
ATOM   5819 N NH1 . ARG B 1 305 ? -1.972  -19.545 35.201  1.00 232.20 ? 305 ARG B NH1 1 
ATOM   5820 N NH2 . ARG B 1 305 ? -2.762  -17.411 35.068  1.00 206.53 ? 305 ARG B NH2 1 
ATOM   5821 N N   . PRO B 1 306 ? -3.017  -14.384 31.428  1.00 237.38 ? 306 PRO B N   1 
ATOM   5822 C CA  . PRO B 1 306 ? -4.232  -14.229 32.217  1.00 221.08 ? 306 PRO B CA  1 
ATOM   5823 C C   . PRO B 1 306 ? -5.477  -14.473 31.377  1.00 219.12 ? 306 PRO B C   1 
ATOM   5824 O O   . PRO B 1 306 ? -6.387  -15.177 31.820  1.00 225.32 ? 306 PRO B O   1 
ATOM   5825 C CB  . PRO B 1 306 ? -4.157  -12.776 32.734  1.00 197.63 ? 306 PRO B CB  1 
ATOM   5826 C CG  . PRO B 1 306 ? -2.677  -12.453 32.742  1.00 204.47 ? 306 PRO B CG  1 
ATOM   5827 C CD  . PRO B 1 306 ? -2.105  -13.235 31.572  1.00 212.68 ? 306 PRO B CD  1 
ATOM   5828 N N   . GLU B 1 307 ? -5.457  -13.922 30.161  1.00 213.58 ? 307 GLU B N   1 
ATOM   5829 C CA  . GLU B 1 307 ? -6.541  -14.074 29.206  1.00 218.08 ? 307 GLU B CA  1 
ATOM   5830 C C   . GLU B 1 307 ? -6.784  -15.556 28.913  1.00 205.49 ? 307 GLU B C   1 
ATOM   5831 O O   . GLU B 1 307 ? -7.933  -16.045 28.923  1.00 199.32 ? 307 GLU B O   1 
ATOM   5832 C CB  . GLU B 1 307 ? -6.182  -13.292 27.943  1.00 217.16 ? 307 GLU B CB  1 
ATOM   5833 C CG  . GLU B 1 307 ? -5.983  -11.795 28.189  1.00 218.41 ? 307 GLU B CG  1 
ATOM   5834 C CD  . GLU B 1 307 ? -6.047  -10.869 26.982  1.00 240.18 ? 307 GLU B CD  1 
ATOM   5835 O OE1 . GLU B 1 307 ? -5.327  -11.125 25.985  1.00 248.79 ? 307 GLU B OE1 1 
ATOM   5836 O OE2 . GLU B 1 307 ? -6.806  -9.875  27.055  1.00 249.36 ? 307 GLU B OE2 1 
ATOM   5837 N N   . ILE B 1 308 ? -5.667  -16.250 28.668  1.00 198.06 ? 308 ILE B N   1 
ATOM   5838 C CA  . ILE B 1 308 ? -5.691  -17.670 28.329  1.00 198.39 ? 308 ILE B CA  1 
ATOM   5839 C C   . ILE B 1 308 ? -6.306  -18.444 29.481  1.00 187.17 ? 308 ILE B C   1 
ATOM   5840 O O   . ILE B 1 308 ? -7.054  -19.349 29.201  1.00 185.15 ? 308 ILE B O   1 
ATOM   5841 C CB  . ILE B 1 308 ? -4.332  -18.277 27.938  1.00 191.93 ? 308 ILE B CB  1 
ATOM   5842 C CG1 . ILE B 1 308 ? -3.847  -17.743 26.613  1.00 204.55 ? 308 ILE B CG1 1 
ATOM   5843 C CG2 . ILE B 1 308 ? -4.429  -19.806 27.921  1.00 153.95 ? 308 ILE B CG2 1 
ATOM   5844 C CD1 . ILE B 1 308 ? -2.588  -18.417 26.109  1.00 219.02 ? 308 ILE B CD1 1 
ATOM   5845 N N   . THR B 1 309 ? -5.903  -18.100 30.713  1.00 163.39 ? 309 THR B N   1 
ATOM   5846 C CA  . THR B 1 309 ? -6.236  -18.841 31.904  1.00 171.82 ? 309 THR B CA  1 
ATOM   5847 C C   . THR B 1 309 ? -7.756  -18.981 32.039  1.00 186.86 ? 309 THR B C   1 
ATOM   5848 O O   . THR B 1 309 ? -8.303  -20.076 32.259  1.00 176.64 ? 309 THR B O   1 
ATOM   5849 C CB  . THR B 1 309 ? -5.675  -18.148 33.149  1.00 169.11 ? 309 THR B CB  1 
ATOM   5850 O OG1 . THR B 1 309 ? -4.292  -18.474 33.205  1.00 184.71 ? 309 THR B OG1 1 
ATOM   5851 C CG2 . THR B 1 309 ? -6.311  -18.632 34.442  1.00 164.13 ? 309 THR B CG2 1 
ATOM   5852 N N   . ASP B 1 310 ? -8.395  -17.812 31.923  1.00 200.44 ? 310 ASP B N   1 
ATOM   5853 C CA  . ASP B 1 310 ? -9.844  -17.700 32.065  1.00 202.39 ? 310 ASP B CA  1 
ATOM   5854 C C   . ASP B 1 310 ? -10.546 -18.586 31.035  1.00 181.36 ? 310 ASP B C   1 
ATOM   5855 O O   . ASP B 1 310 ? -11.490 -19.329 31.361  1.00 194.52 ? 310 ASP B O   1 
ATOM   5856 C CB  . ASP B 1 310 ? -10.317 -16.256 32.016  1.00 243.94 ? 310 ASP B CB  1 
ATOM   5857 C CG  . ASP B 1 310 ? -10.358 -15.548 33.360  1.00 279.27 ? 310 ASP B CG  1 
ATOM   5858 O OD1 . ASP B 1 310 ? -10.963 -16.115 34.295  1.00 306.78 ? 310 ASP B OD1 1 
ATOM   5859 O OD2 . ASP B 1 310 ? -9.806  -14.433 33.449  1.00 293.04 ? 310 ASP B OD2 1 
ATOM   5860 N N   . ALA B 1 311 ? -10.041 -18.479 29.798  1.00 151.15 ? 311 ALA B N   1 
ATOM   5861 C CA  . ALA B 1 311 ? -10.574 -19.226 28.667  1.00 149.66 ? 311 ALA B CA  1 
ATOM   5862 C C   . ALA B 1 311 ? -10.501 -20.730 28.954  1.00 152.84 ? 311 ALA B C   1 
ATOM   5863 O O   . ALA B 1 311 ? -11.473 -21.478 28.740  1.00 149.65 ? 311 ALA B O   1 
ATOM   5864 C CB  . ALA B 1 311 ? -9.782  -18.835 27.443  1.00 140.46 ? 311 ALA B CB  1 
ATOM   5865 N N   . VAL B 1 312 ? -9.328  -21.137 29.445  1.00 148.30 ? 312 VAL B N   1 
ATOM   5866 C CA  . VAL B 1 312 ? -9.046  -22.530 29.764  1.00 157.68 ? 312 VAL B CA  1 
ATOM   5867 C C   . VAL B 1 312 ? -10.030 -23.027 30.807  1.00 172.13 ? 312 VAL B C   1 
ATOM   5868 O O   . VAL B 1 312 ? -10.574 -24.119 30.670  1.00 162.17 ? 312 VAL B O   1 
ATOM   5869 C CB  . VAL B 1 312 ? -7.590  -22.906 30.102  1.00 172.01 ? 312 VAL B CB  1 
ATOM   5870 C CG1 . VAL B 1 312 ? -7.497  -24.087 31.070  1.00 202.10 ? 312 VAL B CG1 1 
ATOM   5871 C CG2 . VAL B 1 312 ? -6.804  -23.216 28.834  1.00 188.42 ? 312 VAL B CG2 1 
ATOM   5872 N N   . ARG B 1 313 ? -10.238 -22.202 31.834  1.00 187.15 ? 313 ARG B N   1 
ATOM   5873 C CA  . ARG B 1 313 ? -11.144 -22.508 32.938  1.00 199.47 ? 313 ARG B CA  1 
ATOM   5874 C C   . ARG B 1 313 ? -12.550 -22.751 32.397  1.00 192.47 ? 313 ARG B C   1 
ATOM   5875 O O   . ARG B 1 313 ? -13.206 -23.746 32.777  1.00 201.89 ? 313 ARG B O   1 
ATOM   5876 C CB  . ARG B 1 313 ? -11.093 -21.425 34.030  1.00 187.93 ? 313 ARG B CB  1 
ATOM   5877 C CG  . ARG B 1 313 ? -12.073 -21.569 35.186  1.00 191.00 ? 313 ARG B CG  1 
ATOM   5878 C CD  . ARG B 1 313 ? -12.611 -20.205 35.631  1.00 225.80 ? 313 ARG B CD  1 
ATOM   5879 N NE  . ARG B 1 313 ? -13.187 -19.415 34.530  1.00 257.40 ? 313 ARG B NE  1 
ATOM   5880 C CZ  . ARG B 1 313 ? -13.851 -18.256 34.602  1.00 263.08 ? 313 ARG B CZ  1 
ATOM   5881 N NH1 . ARG B 1 313 ? -14.199 -17.754 35.774  1.00 270.55 ? 313 ARG B NH1 1 
ATOM   5882 N NH2 . ARG B 1 313 ? -14.191 -17.614 33.494  1.00 242.94 ? 313 ARG B NH2 1 
ATOM   5883 N N   . ARG B 1 314 ? -12.968 -21.839 31.509  1.00 173.52 ? 314 ARG B N   1 
ATOM   5884 C CA  . ARG B 1 314 ? -14.295 -21.918 30.901  1.00 186.66 ? 314 ARG B CA  1 
ATOM   5885 C C   . ARG B 1 314 ? -14.466 -23.255 30.157  1.00 186.77 ? 314 ARG B C   1 
ATOM   5886 O O   . ARG B 1 314 ? -15.482 -23.987 30.296  1.00 190.54 ? 314 ARG B O   1 
ATOM   5887 C CB  . ARG B 1 314 ? -14.701 -20.688 30.081  1.00 190.95 ? 314 ARG B CB  1 
ATOM   5888 C CG  . ARG B 1 314 ? -14.926 -19.485 30.989  1.00 194.77 ? 314 ARG B CG  1 
ATOM   5889 C CD  . ARG B 1 314 ? -15.301 -18.219 30.236  1.00 175.90 ? 314 ARG B CD  1 
ATOM   5890 N NE  . ARG B 1 314 ? -14.174 -17.607 29.518  1.00 164.46 ? 314 ARG B NE  1 
ATOM   5891 C CZ  . ARG B 1 314 ? -14.099 -17.501 28.184  1.00 168.60 ? 314 ARG B CZ  1 
ATOM   5892 N NH1 . ARG B 1 314 ? -15.009 -18.070 27.398  1.00 159.84 ? 314 ARG B NH1 1 
ATOM   5893 N NH2 . ARG B 1 314 ? -13.087 -16.850 27.641  1.00 183.31 ? 314 ARG B NH2 1 
ATOM   5894 N N   . THR B 1 315 ? -13.420 -23.545 29.374  1.00 174.10 ? 315 THR B N   1 
ATOM   5895 C CA  . THR B 1 315 ? -13.378 -24.755 28.555  1.00 160.77 ? 315 THR B CA  1 
ATOM   5896 C C   . THR B 1 315 ? -13.469 -25.981 29.443  1.00 158.00 ? 315 THR B C   1 
ATOM   5897 O O   . THR B 1 315 ? -14.202 -26.911 29.134  1.00 136.71 ? 315 THR B O   1 
ATOM   5898 C CB  . THR B 1 315 ? -12.151 -24.772 27.660  1.00 160.85 ? 315 THR B CB  1 
ATOM   5899 O OG1 . THR B 1 315 ? -12.002 -23.426 27.210  1.00 169.69 ? 315 THR B OG1 1 
ATOM   5900 C CG2 . THR B 1 315 ? -12.375 -25.724 26.499  1.00 155.47 ? 315 THR B CG2 1 
ATOM   5901 N N   . GLY B 1 316 ? -12.716 -25.959 30.539  1.00 167.31 ? 316 GLY B N   1 
ATOM   5902 C CA  . GLY B 1 316 ? -12.668 -27.032 31.520  1.00 197.67 ? 316 GLY B CA  1 
ATOM   5903 C C   . GLY B 1 316 ? -14.056 -27.290 32.070  1.00 209.75 ? 316 GLY B C   1 
ATOM   5904 O O   . GLY B 1 316 ? -14.480 -28.442 32.153  1.00 240.25 ? 316 GLY B O   1 
ATOM   5905 N N   . GLU B 1 317 ? -14.734 -26.196 32.427  1.00 202.49 ? 317 GLU B N   1 
ATOM   5906 C CA  . GLU B 1 317 ? -16.083 -26.251 32.987  1.00 217.94 ? 317 GLU B CA  1 
ATOM   5907 C C   . GLU B 1 317 ? -17.026 -26.957 31.997  1.00 210.08 ? 317 GLU B C   1 
ATOM   5908 O O   . GLU B 1 317 ? -17.807 -27.867 32.373  1.00 225.00 ? 317 GLU B O   1 
ATOM   5909 C CB  . GLU B 1 317 ? -16.554 -24.899 33.529  1.00 221.51 ? 317 GLU B CB  1 
ATOM   5910 C CG  . GLU B 1 317 ? -15.854 -24.496 34.825  1.00 233.05 ? 317 GLU B CG  1 
ATOM   5911 C CD  . GLU B 1 317 ? -15.880 -23.022 35.199  1.00 240.42 ? 317 GLU B CD  1 
ATOM   5912 O OE1 . GLU B 1 317 ? -16.503 -22.231 34.465  1.00 219.43 ? 317 GLU B OE1 1 
ATOM   5913 O OE2 . GLU B 1 317 ? -15.262 -22.652 36.221  1.00 269.00 ? 317 GLU B OE2 1 
ATOM   5914 N N   . VAL B 1 318 ? -16.909 -26.510 30.740  1.00 184.35 ? 318 VAL B N   1 
ATOM   5915 C CA  . VAL B 1 318 ? -17.736 -27.032 29.660  1.00 186.02 ? 318 VAL B CA  1 
ATOM   5916 C C   . VAL B 1 318 ? -17.511 -28.547 29.514  1.00 197.68 ? 318 VAL B C   1 
ATOM   5917 O O   . VAL B 1 318 ? -18.459 -29.330 29.382  1.00 188.84 ? 318 VAL B O   1 
ATOM   5918 C CB  . VAL B 1 318 ? -17.552 -26.268 28.341  1.00 181.38 ? 318 VAL B CB  1 
ATOM   5919 C CG1 . VAL B 1 318 ? -18.272 -26.958 27.186  1.00 173.71 ? 318 VAL B CG1 1 
ATOM   5920 C CG2 . VAL B 1 318 ? -18.040 -24.839 28.513  1.00 168.94 ? 318 VAL B CG2 1 
ATOM   5921 N N   . LEU B 1 319 ? -16.236 -28.922 29.543  1.00 175.38 ? 319 LEU B N   1 
ATOM   5922 C CA  . LEU B 1 319 ? -15.865 -30.317 29.385  1.00 155.28 ? 319 LEU B CA  1 
ATOM   5923 C C   . LEU B 1 319 ? -16.420 -31.152 30.521  1.00 162.72 ? 319 LEU B C   1 
ATOM   5924 O O   . LEU B 1 319 ? -16.922 -32.239 30.274  1.00 155.25 ? 319 LEU B O   1 
ATOM   5925 C CB  . LEU B 1 319 ? -14.430 -30.589 28.972  1.00 164.09 ? 319 LEU B CB  1 
ATOM   5926 C CG  . LEU B 1 319 ? -14.268 -30.681 27.456  1.00 175.55 ? 319 LEU B CG  1 
ATOM   5927 C CD1 . LEU B 1 319 ? -12.799 -30.859 27.101  1.00 235.11 ? 319 LEU B CD1 1 
ATOM   5928 C CD2 . LEU B 1 319 ? -15.124 -31.829 26.920  1.00 161.80 ? 319 LEU B CD2 1 
ATOM   5929 N N   . SER B 1 320 ? -16.357 -30.612 31.737  1.00 164.01 ? 320 SER B N   1 
ATOM   5930 C CA  . SER B 1 320 ? -16.893 -31.272 32.923  1.00 176.91 ? 320 SER B CA  1 
ATOM   5931 C C   . SER B 1 320 ? -18.383 -31.527 32.744  1.00 195.38 ? 320 SER B C   1 
ATOM   5932 O O   . SER B 1 320 ? -18.866 -32.626 33.037  1.00 206.52 ? 320 SER B O   1 
ATOM   5933 C CB  . SER B 1 320 ? -16.603 -30.528 34.190  1.00 176.94 ? 320 SER B CB  1 
ATOM   5934 O OG  . SER B 1 320 ? -17.031 -31.312 35.295  1.00 199.97 ? 320 SER B OG  1 
ATOM   5935 N N   . GLY B 1 321 ? -19.077 -30.493 32.259  1.00 203.67 ? 321 GLY B N   1 
ATOM   5936 C CA  . GLY B 1 321 ? -20.512 -30.560 32.007  1.00 224.94 ? 321 GLY B CA  1 
ATOM   5937 C C   . GLY B 1 321 ? -20.827 -31.690 31.026  1.00 231.13 ? 321 GLY B C   1 
ATOM   5938 O O   . GLY B 1 321 ? -21.733 -32.510 31.231  1.00 285.84 ? 321 GLY B O   1 
ATOM   5939 N N   . LEU B 1 322 ? -20.034 -31.712 29.956  1.00 194.52 ? 322 LEU B N   1 
ATOM   5940 C CA  . LEU B 1 322 ? -20.157 -32.706 28.888  1.00 181.36 ? 322 LEU B CA  1 
ATOM   5941 C C   . LEU B 1 322 ? -19.946 -34.097 29.490  1.00 173.42 ? 322 LEU B C   1 
ATOM   5942 O O   . LEU B 1 322 ? -20.670 -35.052 29.225  1.00 159.77 ? 322 LEU B O   1 
ATOM   5943 C CB  . LEU B 1 322 ? -19.207 -32.446 27.718  1.00 178.15 ? 322 LEU B CB  1 
ATOM   5944 C CG  . LEU B 1 322 ? -19.773 -31.617 26.557  1.00 177.39 ? 322 LEU B CG  1 
ATOM   5945 C CD1 . LEU B 1 322 ? -19.931 -30.119 26.856  1.00 153.24 ? 322 LEU B CD1 1 
ATOM   5946 C CD2 . LEU B 1 322 ? -18.983 -31.863 25.265  1.00 184.91 ? 322 LEU B CD2 1 
ATOM   5947 N N   . GLY B 1 323 ? -19.007 -34.089 30.447  1.00 167.77 ? 323 GLY B N   1 
ATOM   5948 C CA  . GLY B 1 323 ? -18.786 -35.179 31.377  1.00 191.31 ? 323 GLY B CA  1 
ATOM   5949 C C   . GLY B 1 323 ? -17.414 -35.816 31.176  1.00 201.15 ? 323 GLY B C   1 
ATOM   5950 O O   . GLY B 1 323 ? -17.247 -37.022 31.373  1.00 186.46 ? 323 GLY B O   1 
ATOM   5951 N N   . HIS B 1 324 ? -16.434 -35.010 30.754  1.00 217.75 ? 324 HIS B N   1 
ATOM   5952 C CA  . HIS B 1 324 ? -15.094 -35.548 30.595  1.00 257.53 ? 324 HIS B CA  1 
ATOM   5953 C C   . HIS B 1 324 ? -14.340 -35.421 31.911  1.00 276.97 ? 324 HIS B C   1 
ATOM   5954 O O   . HIS B 1 324 ? -14.287 -34.345 32.502  1.00 284.85 ? 324 HIS B O   1 
ATOM   5955 C CB  . HIS B 1 324 ? -14.312 -34.881 29.457  1.00 263.49 ? 324 HIS B CB  1 
ATOM   5956 C CG  . HIS B 1 324 ? -13.093 -35.671 29.107  1.00 250.13 ? 324 HIS B CG  1 
ATOM   5957 N ND1 . HIS B 1 324 ? -11.825 -35.141 29.006  1.00 231.44 ? 324 HIS B ND1 1 
ATOM   5958 C CD2 . HIS B 1 324 ? -12.970 -36.986 28.881  1.00 240.54 ? 324 HIS B CD2 1 
ATOM   5959 C CE1 . HIS B 1 324 ? -10.975 -36.112 28.708  1.00 244.98 ? 324 HIS B CE1 1 
ATOM   5960 N NE2 . HIS B 1 324 ? -11.652 -37.237 28.622  1.00 256.77 ? 324 HIS B NE2 1 
ATOM   5961 N N   . ARG B 1 325 ? -13.774 -36.544 32.353  1.00 277.16 ? 325 ARG B N   1 
ATOM   5962 C CA  . ARG B 1 325 ? -12.943 -36.588 33.543  1.00 251.51 ? 325 ARG B CA  1 
ATOM   5963 C C   . ARG B 1 325 ? -11.532 -36.965 33.106  1.00 221.81 ? 325 ARG B C   1 
ATOM   5964 O O   . ARG B 1 325 ? -11.361 -37.732 32.156  1.00 224.28 ? 325 ARG B O   1 
ATOM   5965 C CB  . ARG B 1 325 ? -13.647 -37.466 34.585  1.00 277.13 ? 325 ARG B CB  1 
ATOM   5966 C CG  . ARG B 1 325 ? -14.859 -36.732 35.150  1.00 287.45 ? 325 ARG B CG  1 
ATOM   5967 C CD  . ARG B 1 325 ? -15.983 -37.575 35.732  1.00 269.79 ? 325 ARG B CD  1 
ATOM   5968 N NE  . ARG B 1 325 ? -16.924 -38.164 34.775  1.00 241.28 ? 325 ARG B NE  1 
ATOM   5969 C CZ  . ARG B 1 325 ? -18.066 -38.760 35.093  1.00 219.36 ? 325 ARG B CZ  1 
ATOM   5970 N NH1 . ARG B 1 325 ? -18.482 -38.793 36.347  1.00 209.60 ? 325 ARG B NH1 1 
ATOM   5971 N NH2 . ARG B 1 325 ? -18.799 -39.320 34.148  1.00 213.69 ? 325 ARG B NH2 1 
ATOM   5972 N N   . GLY B 1 326 ? -10.535 -36.351 33.755  1.00 197.83 ? 326 GLY B N   1 
ATOM   5973 C CA  . GLY B 1 326 ? -9.154  -36.484 33.324  1.00 200.26 ? 326 GLY B CA  1 
ATOM   5974 C C   . GLY B 1 326 ? -8.583  -35.123 32.906  1.00 172.96 ? 326 GLY B C   1 
ATOM   5975 O O   . GLY B 1 326 ? -8.640  -34.175 33.690  1.00 164.42 ? 326 GLY B O   1 
ATOM   5976 N N   . ALA B 1 327 ? -8.052  -35.063 31.686  1.00 145.74 ? 327 ALA B N   1 
ATOM   5977 C CA  . ALA B 1 327 ? -7.215  -33.971 31.248  1.00 142.69 ? 327 ALA B CA  1 
ATOM   5978 C C   . ALA B 1 327 ? -7.605  -33.546 29.835  1.00 149.02 ? 327 ALA B C   1 
ATOM   5979 O O   . ALA B 1 327 ? -7.865  -34.344 28.932  1.00 153.86 ? 327 ALA B O   1 
ATOM   5980 C CB  . ALA B 1 327 ? -5.758  -34.363 31.352  1.00 166.91 ? 327 ALA B CB  1 
ATOM   5981 N N   . PHE B 1 328 ? -7.553  -32.233 29.651  1.00 150.23 ? 328 PHE B N   1 
ATOM   5982 C CA  . PHE B 1 328 ? -7.815  -31.574 28.382  1.00 151.95 ? 328 PHE B CA  1 
ATOM   5983 C C   . PHE B 1 328 ? -6.713  -30.554 28.068  1.00 139.62 ? 328 PHE B C   1 
ATOM   5984 O O   . PHE B 1 328 ? -6.060  -29.903 28.923  1.00 126.51 ? 328 PHE B O   1 
ATOM   5985 C CB  . PHE B 1 328 ? -9.242  -31.017 28.351  1.00 182.18 ? 328 PHE B CB  1 
ATOM   5986 C CG  . PHE B 1 328 ? -9.383  -29.835 29.300  1.00 211.16 ? 328 PHE B CG  1 
ATOM   5987 C CD1 . PHE B 1 328 ? -9.012  -28.555 28.891  1.00 235.50 ? 328 PHE B CD1 1 
ATOM   5988 C CD2 . PHE B 1 328 ? -9.814  -30.008 30.615  1.00 203.34 ? 328 PHE B CD2 1 
ATOM   5989 C CE1 . PHE B 1 328 ? -9.082  -27.474 29.763  1.00 243.63 ? 328 PHE B CE1 1 
ATOM   5990 C CE2 . PHE B 1 328 ? -9.899  -28.923 31.483  1.00 213.41 ? 328 PHE B CE2 1 
ATOM   5991 C CZ  . PHE B 1 328 ? -9.530  -27.656 31.055  1.00 226.29 ? 328 PHE B CZ  1 
ATOM   5992 N N   . GLY B 1 329 ? -6.582  -30.347 26.758  1.00 140.56 ? 329 GLY B N   1 
ATOM   5993 C CA  . GLY B 1 329 ? -5.660  -29.400 26.153  1.00 143.18 ? 329 GLY B CA  1 
ATOM   5994 C C   . GLY B 1 329 ? -6.369  -28.492 25.154  1.00 136.37 ? 329 GLY B C   1 
ATOM   5995 O O   . GLY B 1 329 ? -7.158  -28.947 24.315  1.00 119.61 ? 329 GLY B O   1 
ATOM   5996 N N   . VAL B 1 330 ? -6.030  -27.197 25.257  1.00 148.35 ? 330 VAL B N   1 
ATOM   5997 C CA  . VAL B 1 330 ? -6.454  -26.188 24.286  1.00 159.79 ? 330 VAL B CA  1 
ATOM   5998 C C   . VAL B 1 330 ? -5.251  -25.472 23.658  1.00 169.30 ? 330 VAL B C   1 
ATOM   5999 O O   . VAL B 1 330 ? -4.423  -24.946 24.380  1.00 140.16 ? 330 VAL B O   1 
ATOM   6000 C CB  . VAL B 1 330 ? -7.396  -25.139 24.907  1.00 147.78 ? 330 VAL B CB  1 
ATOM   6001 C CG1 . VAL B 1 330 ? -8.141  -24.371 23.822  1.00 131.07 ? 330 VAL B CG1 1 
ATOM   6002 C CG2 . VAL B 1 330 ? -8.356  -25.747 25.921  1.00 142.39 ? 330 VAL B CG2 1 
ATOM   6003 N N   . ASP B 1 331 ? -5.157  -25.553 22.328  1.00 172.70 ? 331 ASP B N   1 
ATOM   6004 C CA  . ASP B 1 331 ? -4.156  -24.861 21.553  1.00 151.41 ? 331 ASP B CA  1 
ATOM   6005 C C   . ASP B 1 331 ? -4.791  -23.598 20.964  1.00 141.98 ? 331 ASP B C   1 
ATOM   6006 O O   . ASP B 1 331 ? -5.925  -23.588 20.464  1.00 128.67 ? 331 ASP B O   1 
ATOM   6007 C CB  . ASP B 1 331 ? -3.477  -25.776 20.539  1.00 164.88 ? 331 ASP B CB  1 
ATOM   6008 C CG  . ASP B 1 331 ? -2.207  -25.238 19.889  1.00 157.49 ? 331 ASP B CG  1 
ATOM   6009 O OD1 . ASP B 1 331 ? -1.606  -24.317 20.475  1.00 156.39 ? 331 ASP B OD1 1 
ATOM   6010 O OD2 . ASP B 1 331 ? -1.852  -25.714 18.787  1.00 139.96 ? 331 ASP B OD2 1 
ATOM   6011 N N   . PHE B 1 332 ? -3.990  -22.533 21.019  1.00 148.40 ? 332 PHE B N   1 
ATOM   6012 C CA  . PHE B 1 332 ? -4.370  -21.196 20.598  1.00 161.27 ? 332 PHE B CA  1 
ATOM   6013 C C   . PHE B 1 332 ? -3.379  -20.587 19.593  1.00 169.43 ? 332 PHE B C   1 
ATOM   6014 O O   . PHE B 1 332 ? -2.188  -20.908 19.483  1.00 171.13 ? 332 PHE B O   1 
ATOM   6015 C CB  . PHE B 1 332 ? -4.377  -20.260 21.811  1.00 147.61 ? 332 PHE B CB  1 
ATOM   6016 C CG  . PHE B 1 332 ? -5.275  -20.642 22.981  1.00 162.92 ? 332 PHE B CG  1 
ATOM   6017 C CD1 . PHE B 1 332 ? -6.655  -20.462 22.912  1.00 156.32 ? 332 PHE B CD1 1 
ATOM   6018 C CD2 . PHE B 1 332 ? -4.735  -21.151 24.162  1.00 186.80 ? 332 PHE B CD2 1 
ATOM   6019 C CE1 . PHE B 1 332 ? -7.470  -20.795 23.988  1.00 149.33 ? 332 PHE B CE1 1 
ATOM   6020 C CE2 . PHE B 1 332 ? -5.561  -21.480 25.234  1.00 185.51 ? 332 PHE B CE2 1 
ATOM   6021 C CZ  . PHE B 1 332 ? -6.925  -21.294 25.151  1.00 152.50 ? 332 PHE B CZ  1 
ATOM   6022 N N   . VAL B 1 333 ? -3.916  -19.597 18.874  1.00 152.44 ? 333 VAL B N   1 
ATOM   6023 C CA  . VAL B 1 333 ? -3.164  -18.678 18.027  1.00 145.77 ? 333 VAL B CA  1 
ATOM   6024 C C   . VAL B 1 333 ? -3.480  -17.230 18.395  1.00 164.73 ? 333 VAL B C   1 
ATOM   6025 O O   . VAL B 1 333 ? -4.605  -16.833 18.743  1.00 171.89 ? 333 VAL B O   1 
ATOM   6026 C CB  . VAL B 1 333 ? -3.261  -18.915 16.506  1.00 131.62 ? 333 VAL B CB  1 
ATOM   6027 C CG1 . VAL B 1 333 ? -2.670  -20.259 16.124  1.00 164.50 ? 333 VAL B CG1 1 
ATOM   6028 C CG2 . VAL B 1 333 ? -4.689  -18.849 16.000  1.00 143.54 ? 333 VAL B CG2 1 
ATOM   6029 N N   . VAL B 1 334 ? -2.445  -16.396 18.181  1.00 181.64 ? 334 VAL B N   1 
ATOM   6030 C CA  . VAL B 1 334 ? -2.528  -14.940 18.329  1.00 171.61 ? 334 VAL B CA  1 
ATOM   6031 C C   . VAL B 1 334 ? -2.443  -14.254 16.956  1.00 177.82 ? 334 VAL B C   1 
ATOM   6032 O O   . VAL B 1 334 ? -1.430  -14.369 16.277  1.00 168.07 ? 334 VAL B O   1 
ATOM   6033 C CB  . VAL B 1 334 ? -1.466  -14.391 19.310  1.00 146.29 ? 334 VAL B CB  1 
ATOM   6034 C CG1 . VAL B 1 334 ? -1.339  -12.876 19.281  1.00 125.00 ? 334 VAL B CG1 1 
ATOM   6035 C CG2 . VAL B 1 334 ? -1.726  -14.855 20.736  1.00 148.19 ? 334 VAL B CG2 1 
ATOM   6036 N N   . ALA B 1 335 ? -3.514  -13.530 16.565  1.00 192.31 ? 335 ALA B N   1 
ATOM   6037 C CA  . ALA B 1 335 ? -3.808  -13.282 15.158  1.00 216.27 ? 335 ALA B CA  1 
ATOM   6038 C C   . ALA B 1 335 ? -3.793  -11.787 14.841  1.00 238.54 ? 335 ALA B C   1 
ATOM   6039 O O   . ALA B 1 335 ? -4.843  -11.162 14.671  1.00 252.37 ? 335 ALA B O   1 
ATOM   6040 C CB  . ALA B 1 335 ? -5.136  -13.912 14.776  1.00 206.39 ? 335 ALA B CB  1 
ATOM   6041 N N   . GLY B 1 336 ? -2.573  -11.239 14.781  1.00 236.18 ? 336 GLY B N   1 
ATOM   6042 C CA  . GLY B 1 336 ? -2.373  -9.812  14.596  1.00 243.34 ? 336 GLY B CA  1 
ATOM   6043 C C   . GLY B 1 336 ? -3.148  -9.030  15.652  1.00 253.76 ? 336 GLY B C   1 
ATOM   6044 O O   . GLY B 1 336 ? -2.966  -9.236  16.852  1.00 278.77 ? 336 GLY B O   1 
ATOM   6045 N N   . GLU B 1 337 ? -4.039  -8.149  15.187  1.00 254.88 ? 337 GLU B N   1 
ATOM   6046 C CA  . GLU B 1 337 ? -4.817  -7.310  16.085  1.00 263.65 ? 337 GLU B CA  1 
ATOM   6047 C C   . GLU B 1 337 ? -6.158  -7.975  16.394  1.00 252.10 ? 337 GLU B C   1 
ATOM   6048 O O   . GLU B 1 337 ? -6.910  -7.490  17.237  1.00 259.79 ? 337 GLU B O   1 
ATOM   6049 C CB  . GLU B 1 337 ? -4.977  -5.882  15.560  1.00 276.23 ? 337 GLU B CB  1 
ATOM   6050 C CG  . GLU B 1 337 ? -3.653  -5.128  15.482  1.00 293.13 ? 337 GLU B CG  1 
ATOM   6051 C CD  . GLU B 1 337 ? -3.770  -3.621  15.474  1.00 297.66 ? 337 GLU B CD  1 
ATOM   6052 O OE1 . GLU B 1 337 ? -4.456  -3.060  14.593  1.00 284.94 ? 337 GLU B OE1 1 
ATOM   6053 O OE2 . GLU B 1 337 ? -3.153  -3.020  16.375  1.00 303.69 ? 337 GLU B OE2 1 
ATOM   6054 N N   . ARG B 1 338 ? -6.433  -9.099  15.724  1.00 221.72 ? 338 ARG B N   1 
ATOM   6055 C CA  . ARG B 1 338 ? -7.709  -9.791  15.839  1.00 188.27 ? 338 ARG B CA  1 
ATOM   6056 C C   . ARG B 1 338 ? -7.853  -10.472 17.201  1.00 182.30 ? 338 ARG B C   1 
ATOM   6057 O O   . ARG B 1 338 ? -8.971  -10.800 17.608  1.00 160.43 ? 338 ARG B O   1 
ATOM   6058 C CB  . ARG B 1 338 ? -7.862  -10.800 14.699  1.00 169.15 ? 338 ARG B CB  1 
ATOM   6059 C CG  . ARG B 1 338 ? -9.189  -11.535 14.803  1.00 161.11 ? 338 ARG B CG  1 
ATOM   6060 C CD  . ARG B 1 338 ? -9.249  -12.461 13.623  1.00 168.40 ? 338 ARG B CD  1 
ATOM   6061 N NE  . ARG B 1 338 ? -10.402 -13.357 13.729  1.00 175.55 ? 338 ARG B NE  1 
ATOM   6062 C CZ  . ARG B 1 338 ? -10.704 -14.279 12.816  1.00 187.27 ? 338 ARG B CZ  1 
ATOM   6063 N NH1 . ARG B 1 338 ? -9.971  -14.429 11.725  1.00 197.42 ? 338 ARG B NH1 1 
ATOM   6064 N NH2 . ARG B 1 338 ? -11.769 -15.041 12.990  1.00 183.23 ? 338 ARG B NH2 1 
ATOM   6065 N N   . GLY B 1 339 ? -6.714  -10.681 17.877  1.00 188.49 ? 339 GLY B N   1 
ATOM   6066 C CA  . GLY B 1 339 ? -6.643  -11.208 19.230  1.00 201.50 ? 339 GLY B CA  1 
ATOM   6067 C C   . GLY B 1 339 ? -6.286  -12.691 19.270  1.00 211.16 ? 339 GLY B C   1 
ATOM   6068 O O   . GLY B 1 339 ? -5.511  -13.216 18.466  1.00 196.19 ? 339 GLY B O   1 
ATOM   6069 N N   . LEU B 1 340 ? -6.949  -13.401 20.203  1.00 215.66 ? 340 LEU B N   1 
ATOM   6070 C CA  . LEU B 1 340 ? -6.570  -14.754 20.606  1.00 203.02 ? 340 LEU B CA  1 
ATOM   6071 C C   . LEU B 1 340 ? -7.700  -15.752 20.331  1.00 206.17 ? 340 LEU B C   1 
ATOM   6072 O O   . LEU B 1 340 ? -8.833  -15.530 20.760  1.00 204.04 ? 340 LEU B O   1 
ATOM   6073 C CB  . LEU B 1 340 ? -6.112  -14.796 22.067  1.00 181.55 ? 340 LEU B CB  1 
ATOM   6074 C CG  . LEU B 1 340 ? -5.558  -16.134 22.571  1.00 178.56 ? 340 LEU B CG  1 
ATOM   6075 C CD1 . LEU B 1 340 ? -4.323  -15.891 23.418  1.00 167.76 ? 340 LEU B CD1 1 
ATOM   6076 C CD2 . LEU B 1 340 ? -6.594  -16.938 23.347  1.00 179.09 ? 340 LEU B CD2 1 
ATOM   6077 N N   . LEU B 1 341 ? -7.366  -16.797 19.573  1.00 200.97 ? 341 LEU B N   1 
ATOM   6078 C CA  . LEU B 1 341 ? -8.336  -17.728 19.026  1.00 184.24 ? 341 LEU B CA  1 
ATOM   6079 C C   . LEU B 1 341 ? -7.906  -19.167 19.319  1.00 179.49 ? 341 LEU B C   1 
ATOM   6080 O O   . LEU B 1 341 ? -6.765  -19.561 19.079  1.00 150.34 ? 341 LEU B O   1 
ATOM   6081 C CB  . LEU B 1 341 ? -8.503  -17.503 17.521  1.00 191.45 ? 341 LEU B CB  1 
ATOM   6082 C CG  . LEU B 1 341 ? -8.522  -16.054 17.021  1.00 199.45 ? 341 LEU B CG  1 
ATOM   6083 C CD1 . LEU B 1 341 ? -8.361  -16.014 15.504  1.00 181.66 ? 341 LEU B CD1 1 
ATOM   6084 C CD2 . LEU B 1 341 ? -9.787  -15.315 17.408  1.00 224.10 ? 341 LEU B CD2 1 
ATOM   6085 N N   . ALA B 1 342 ? -8.866  -19.928 19.853  1.00 174.25 ? 342 ALA B N   1 
ATOM   6086 C CA  . ALA B 1 342 ? -8.708  -21.338 20.159  1.00 161.58 ? 342 ALA B CA  1 
ATOM   6087 C C   . ALA B 1 342 ? -8.923  -22.166 18.900  1.00 157.66 ? 342 ALA B C   1 
ATOM   6088 O O   . ALA B 1 342 ? -9.961  -22.058 18.253  1.00 146.18 ? 342 ALA B O   1 
ATOM   6089 C CB  . ALA B 1 342 ? -9.708  -21.716 21.233  1.00 132.31 ? 342 ALA B CB  1 
ATOM   6090 N N   . VAL B 1 343 ? -7.951  -23.044 18.597  1.00 155.82 ? 343 VAL B N   1 
ATOM   6091 C CA  . VAL B 1 343 ? -7.850  -23.709 17.304  1.00 144.04 ? 343 VAL B CA  1 
ATOM   6092 C C   . VAL B 1 343 ? -8.002  -25.229 17.445  1.00 159.42 ? 343 VAL B C   1 
ATOM   6093 O O   . VAL B 1 343 ? -8.603  -25.879 16.585  1.00 185.61 ? 343 VAL B O   1 
ATOM   6094 C CB  . VAL B 1 343 ? -6.504  -23.363 16.638  1.00 109.79 ? 343 VAL B CB  1 
ATOM   6095 C CG1 . VAL B 1 343 ? -6.230  -21.862 16.609  1.00 102.41 ? 343 VAL B CG1 1 
ATOM   6096 C CG2 . VAL B 1 343 ? -5.369  -24.044 17.373  1.00 113.74 ? 343 VAL B CG2 1 
ATOM   6097 N N   . GLU B 1 344 ? -7.480  -25.747 18.565  1.00 145.25 ? 344 GLU B N   1 
ATOM   6098 C CA  . GLU B 1 344 ? -7.503  -27.162 18.855  1.00 151.39 ? 344 GLU B CA  1 
ATOM   6099 C C   . GLU B 1 344 ? -8.000  -27.430 20.277  1.00 141.56 ? 344 GLU B C   1 
ATOM   6100 O O   . GLU B 1 344 ? -7.744  -26.719 21.256  1.00 119.97 ? 344 GLU B O   1 
ATOM   6101 C CB  . GLU B 1 344 ? -6.235  -27.924 18.454  1.00 184.20 ? 344 GLU B CB  1 
ATOM   6102 C CG  . GLU B 1 344 ? -6.266  -28.471 17.026  1.00 221.79 ? 344 GLU B CG  1 
ATOM   6103 C CD  . GLU B 1 344 ? -5.546  -29.812 16.847  1.00 258.43 ? 344 GLU B CD  1 
ATOM   6104 O OE1 . GLU B 1 344 ? -6.122  -30.827 17.302  1.00 266.87 ? 344 GLU B OE1 1 
ATOM   6105 O OE2 . GLU B 1 344 ? -4.410  -29.874 16.303  1.00 283.22 ? 344 GLU B OE2 1 
ATOM   6106 N N   . ILE B 1 345 ? -8.666  -28.587 20.390  1.00 145.77 ? 345 ILE B N   1 
ATOM   6107 C CA  . ILE B 1 345 ? -9.018  -29.233 21.649  1.00 143.73 ? 345 ILE B CA  1 
ATOM   6108 C C   . ILE B 1 345 ? -8.518  -30.675 21.643  1.00 149.96 ? 345 ILE B C   1 
ATOM   6109 O O   . ILE B 1 345 ? -8.755  -31.445 20.696  1.00 151.77 ? 345 ILE B O   1 
ATOM   6110 C CB  . ILE B 1 345 ? -10.533 -29.259 21.887  1.00 151.82 ? 345 ILE B CB  1 
ATOM   6111 C CG1 . ILE B 1 345 ? -10.842 -29.066 23.364  1.00 160.15 ? 345 ILE B CG1 1 
ATOM   6112 C CG2 . ILE B 1 345 ? -11.148 -30.552 21.339  1.00 162.90 ? 345 ILE B CG2 1 
ATOM   6113 C CD1 . ILE B 1 345 ? -10.639 -27.644 23.848  1.00 161.10 ? 345 ILE B CD1 1 
ATOM   6114 N N   . ASN B 1 346 ? -7.880  -31.033 22.764  1.00 145.34 ? 346 ASN B N   1 
ATOM   6115 C CA  . ASN B 1 346 ? -7.294  -32.356 22.960  1.00 131.97 ? 346 ASN B CA  1 
ATOM   6116 C C   . ASN B 1 346 ? -7.854  -33.036 24.218  1.00 130.83 ? 346 ASN B C   1 
ATOM   6117 O O   . ASN B 1 346 ? -7.795  -32.430 25.291  1.00 115.45 ? 346 ASN B O   1 
ATOM   6118 C CB  . ASN B 1 346 ? -5.775  -32.233 23.051  1.00 147.88 ? 346 ASN B CB  1 
ATOM   6119 C CG  . ASN B 1 346 ? -5.134  -31.636 21.815  1.00 178.82 ? 346 ASN B CG  1 
ATOM   6120 O OD1 . ASN B 1 346 ? -5.092  -32.283 20.761  1.00 236.55 ? 346 ASN B OD1 1 
ATOM   6121 N ND2 . ASN B 1 346 ? -4.618  -30.416 21.922  1.00 166.29 ? 346 ASN B ND2 1 
ATOM   6122 N N   . LEU B 1 347 ? -8.497  -34.196 24.009  1.00 139.35 ? 347 LEU B N   1 
ATOM   6123 C CA  . LEU B 1 347 ? -9.056  -34.965 25.098  1.00 163.51 ? 347 LEU B CA  1 
ATOM   6124 C C   . LEU B 1 347 ? -8.026  -36.023 25.433  1.00 166.98 ? 347 LEU B C   1 
ATOM   6125 O O   . LEU B 1 347 ? -8.110  -37.133 24.944  1.00 177.07 ? 347 LEU B O   1 
ATOM   6126 C CB  . LEU B 1 347 ? -10.396 -35.581 24.702  1.00 198.45 ? 347 LEU B CB  1 
ATOM   6127 C CG  . LEU B 1 347 ? -11.557 -34.607 24.466  1.00 218.14 ? 347 LEU B CG  1 
ATOM   6128 C CD1 . LEU B 1 347 ? -12.845 -35.417 24.439  1.00 229.70 ? 347 LEU B CD1 1 
ATOM   6129 C CD2 . LEU B 1 347 ? -11.630 -33.501 25.513  1.00 212.40 ? 347 LEU B CD2 1 
ATOM   6130 N N   . ARG B 1 348 ? -7.002  -35.602 26.175  1.00 176.06 ? 348 ARG B N   1 
ATOM   6131 C CA  . ARG B 1 348 ? -5.802  -36.385 26.438  1.00 178.81 ? 348 ARG B CA  1 
ATOM   6132 C C   . ARG B 1 348 ? -4.806  -35.476 27.153  1.00 193.28 ? 348 ARG B C   1 
ATOM   6133 O O   . ARG B 1 348 ? -5.012  -34.267 27.241  1.00 204.50 ? 348 ARG B O   1 
ATOM   6134 C CB  . ARG B 1 348 ? -5.181  -37.008 25.177  1.00 158.32 ? 348 ARG B CB  1 
ATOM   6135 C CG  . ARG B 1 348 ? -4.751  -36.042 24.080  1.00 164.03 ? 348 ARG B CG  1 
ATOM   6136 C CD  . ARG B 1 348 ? -4.146  -36.700 22.848  1.00 159.34 ? 348 ARG B CD  1 
ATOM   6137 N NE  . ARG B 1 348 ? -3.753  -35.764 21.784  1.00 162.47 ? 348 ARG B NE  1 
ATOM   6138 C CZ  . ARG B 1 348 ? -2.890  -34.745 21.869  1.00 149.77 ? 348 ARG B CZ  1 
ATOM   6139 N NH1 . ARG B 1 348 ? -2.283  -34.445 23.012  1.00 128.33 ? 348 ARG B NH1 1 
ATOM   6140 N NH2 . ARG B 1 348 ? -2.630  -34.036 20.782  1.00 148.23 ? 348 ARG B NH2 1 
ATOM   6141 N N   . LYS B 1 349 ? -3.730  -36.067 27.681  1.00 200.45 ? 349 LYS B N   1 
ATOM   6142 C CA  . LYS B 1 349 ? -2.618  -35.280 28.188  1.00 164.34 ? 349 LYS B CA  1 
ATOM   6143 C C   . LYS B 1 349 ? -1.959  -34.600 26.989  1.00 154.70 ? 349 LYS B C   1 
ATOM   6144 O O   . LYS B 1 349 ? -2.147  -35.004 25.841  1.00 145.27 ? 349 LYS B O   1 
ATOM   6145 C CB  . LYS B 1 349 ? -1.707  -36.192 29.014  1.00 160.13 ? 349 LYS B CB  1 
ATOM   6146 C CG  . LYS B 1 349 ? -2.398  -36.945 30.147  1.00 155.12 ? 349 LYS B CG  1 
ATOM   6147 C CD  . LYS B 1 349 ? -1.485  -37.933 30.866  1.00 172.11 ? 349 LYS B CD  1 
ATOM   6148 C CE  . LYS B 1 349 ? -2.162  -38.799 31.888  1.00 172.97 ? 349 LYS B CE  1 
ATOM   6149 N NZ  . LYS B 1 349 ? -3.043  -38.057 32.795  1.00 169.03 ? 349 LYS B NZ  1 
ATOM   6150 N N   . VAL B 1 350 ? -1.266  -33.495 27.242  1.00 147.86 ? 350 VAL B N   1 
ATOM   6151 C CA  . VAL B 1 350 ? -0.681  -32.786 26.122  1.00 143.38 ? 350 VAL B CA  1 
ATOM   6152 C C   . VAL B 1 350 ? 0.805   -32.700 26.403  1.00 131.93 ? 350 VAL B C   1 
ATOM   6153 O O   . VAL B 1 350 ? 1.223   -32.831 27.550  1.00 127.21 ? 350 VAL B O   1 
ATOM   6154 C CB  . VAL B 1 350 ? -1.308  -31.394 25.946  1.00 172.59 ? 350 VAL B CB  1 
ATOM   6155 C CG1 . VAL B 1 350 ? -1.037  -30.831 24.553  1.00 183.90 ? 350 VAL B CG1 1 
ATOM   6156 C CG2 . VAL B 1 350 ? -2.811  -31.449 26.183  1.00 218.35 ? 350 VAL B CG2 1 
ATOM   6157 N N   . GLY B 1 351 ? 1.587   -32.519 25.340  1.00 129.05 ? 351 GLY B N   1 
ATOM   6158 C CA  . GLY B 1 351 ? 3.031   -32.477 25.483  1.00 143.78 ? 351 GLY B CA  1 
ATOM   6159 C C   . GLY B 1 351 ? 3.443   -31.919 26.846  1.00 155.05 ? 351 GLY B C   1 
ATOM   6160 O O   . GLY B 1 351 ? 3.953   -32.650 27.693  1.00 176.41 ? 351 GLY B O   1 
ATOM   6161 N N   . PRO B 1 352 ? 3.203   -30.622 27.111  1.00 139.78 ? 352 PRO B N   1 
ATOM   6162 C CA  . PRO B 1 352 ? 3.753   -29.966 28.277  1.00 137.62 ? 352 PRO B CA  1 
ATOM   6163 C C   . PRO B 1 352 ? 3.384   -30.568 29.611  1.00 134.09 ? 352 PRO B C   1 
ATOM   6164 O O   . PRO B 1 352 ? 4.041   -30.198 30.558  1.00 128.08 ? 352 PRO B O   1 
ATOM   6165 C CB  . PRO B 1 352 ? 3.226   -28.548 28.099  1.00 135.96 ? 352 PRO B CB  1 
ATOM   6166 C CG  . PRO B 1 352 ? 2.000   -28.722 27.250  1.00 144.93 ? 352 PRO B CG  1 
ATOM   6167 C CD  . PRO B 1 352 ? 2.522   -29.684 26.206  1.00 130.03 ? 352 PRO B CD  1 
ATOM   6168 N N   . SER B 1 353 ? 2.378   -31.436 29.670  1.00 128.22 ? 353 SER B N   1 
ATOM   6169 C CA  . SER B 1 353 ? 1.882   -31.938 30.943  1.00 133.42 ? 353 SER B CA  1 
ATOM   6170 C C   . SER B 1 353 ? 3.005   -32.664 31.710  1.00 130.12 ? 353 SER B C   1 
ATOM   6171 O O   . SER B 1 353 ? 3.305   -32.422 32.898  1.00 114.88 ? 353 SER B O   1 
ATOM   6172 C CB  . SER B 1 353 ? 0.710   -32.858 30.725  1.00 151.32 ? 353 SER B CB  1 
ATOM   6173 O OG  . SER B 1 353 ? 1.106   -33.979 29.948  1.00 160.41 ? 353 SER B OG  1 
ATOM   6174 N N   . HIS B 1 354 ? 3.627   -33.560 30.944  1.00 136.67 ? 354 HIS B N   1 
ATOM   6175 C CA  . HIS B 1 354 ? 4.723   -34.383 31.480  1.00 119.73 ? 354 HIS B CA  1 
ATOM   6176 C C   . HIS B 1 354 ? 5.877   -33.487 31.897  1.00 109.96 ? 354 HIS B C   1 
ATOM   6177 O O   . HIS B 1 354 ? 6.450   -33.694 32.970  1.00 101.30 ? 354 HIS B O   1 
ATOM   6178 C CB  . HIS B 1 354 ? 5.081   -35.574 30.589  1.00 119.21 ? 354 HIS B CB  1 
ATOM   6179 C CG  . HIS B 1 354 ? 6.210   -35.352 29.650  1.00 116.02 ? 354 HIS B CG  1 
ATOM   6180 N ND1 . HIS B 1 354 ? 6.053   -34.775 28.411  1.00 127.80 ? 354 HIS B ND1 1 
ATOM   6181 C CD2 . HIS B 1 354 ? 7.496   -35.636 29.760  1.00 118.98 ? 354 HIS B CD2 1 
ATOM   6182 C CE1 . HIS B 1 354 ? 7.226   -34.705 27.801  1.00 134.30 ? 354 HIS B CE1 1 
ATOM   6183 N NE2 . HIS B 1 354 ? 8.118   -35.227 28.602  1.00 141.71 ? 354 HIS B NE2 1 
ATOM   6184 N N   . VAL B 1 355 ? 6.171   -32.490 31.051  1.00 108.84 ? 355 VAL B N   1 
ATOM   6185 C CA  . VAL B 1 355 ? 7.240   -31.529 31.306  1.00 129.51 ? 355 VAL B CA  1 
ATOM   6186 C C   . VAL B 1 355 ? 6.978   -30.807 32.627  1.00 116.17 ? 355 VAL B C   1 
ATOM   6187 O O   . VAL B 1 355 ? 7.863   -30.639 33.465  1.00 112.79 ? 355 VAL B O   1 
ATOM   6188 C CB  . VAL B 1 355 ? 7.343   -30.564 30.096  1.00 127.69 ? 355 VAL B CB  1 
ATOM   6189 C CG1 . VAL B 1 355 ? 8.280   -29.369 30.315  1.00 111.70 ? 355 VAL B CG1 1 
ATOM   6190 C CG2 . VAL B 1 355 ? 7.678   -31.322 28.813  1.00 122.18 ? 355 VAL B CG2 1 
ATOM   6191 N N   . VAL B 1 356 ? 5.729   -30.375 32.786  1.00 109.30 ? 356 VAL B N   1 
ATOM   6192 C CA  . VAL B 1 356 ? 5.248   -29.630 33.933  1.00 132.19 ? 356 VAL B CA  1 
ATOM   6193 C C   . VAL B 1 356 ? 5.453   -30.468 35.169  1.00 129.17 ? 356 VAL B C   1 
ATOM   6194 O O   . VAL B 1 356 ? 5.899   -29.883 36.146  1.00 124.60 ? 356 VAL B O   1 
ATOM   6195 C CB  . VAL B 1 356 ? 3.765   -29.215 33.847  1.00 154.81 ? 356 VAL B CB  1 
ATOM   6196 C CG1 . VAL B 1 356 ? 3.218   -28.814 35.218  1.00 137.29 ? 356 VAL B CG1 1 
ATOM   6197 C CG2 . VAL B 1 356 ? 3.535   -28.095 32.833  1.00 166.56 ? 356 VAL B CG2 1 
ATOM   6198 N N   . ARG B 1 357 ? 5.134   -31.775 35.109  1.00 129.11 ? 357 ARG B N   1 
ATOM   6199 C CA  . ARG B 1 357 ? 5.301   -32.657 36.254  1.00 120.23 ? 357 ARG B CA  1 
ATOM   6200 C C   . ARG B 1 357 ? 6.750   -32.639 36.762  1.00 110.00 ? 357 ARG B C   1 
ATOM   6201 O O   . ARG B 1 357 ? 7.041   -32.488 37.965  1.00 92.28  ? 357 ARG B O   1 
ATOM   6202 C CB  . ARG B 1 357 ? 4.916   -34.109 35.981  1.00 121.58 ? 357 ARG B CB  1 
ATOM   6203 C CG  . ARG B 1 357 ? 3.402   -34.161 36.072  1.00 140.28 ? 357 ARG B CG  1 
ATOM   6204 C CD  . ARG B 1 357 ? 2.918   -35.565 36.381  1.00 198.15 ? 357 ARG B CD  1 
ATOM   6205 N NE  . ARG B 1 357 ? 2.563   -35.803 37.785  1.00 239.20 ? 357 ARG B NE  1 
ATOM   6206 C CZ  . ARG B 1 357 ? 3.251   -36.501 38.690  1.00 272.61 ? 357 ARG B CZ  1 
ATOM   6207 N NH1 . ARG B 1 357 ? 4.511   -36.845 38.481  1.00 295.42 ? 357 ARG B NH1 1 
ATOM   6208 N NH2 . ARG B 1 357 ? 2.678   -36.822 39.837  1.00 276.20 ? 357 ARG B NH2 1 
ATOM   6209 N N   . TYR B 1 358 ? 7.636   -32.790 35.766  1.00 108.99 ? 358 TYR B N   1 
ATOM   6210 C CA  . TYR B 1 358 ? 9.081   -32.823 36.006  1.00 119.04 ? 358 TYR B CA  1 
ATOM   6211 C C   . TYR B 1 358 ? 9.523   -31.531 36.683  1.00 123.26 ? 358 TYR B C   1 
ATOM   6212 O O   . TYR B 1 358 ? 10.284  -31.546 37.665  1.00 106.89 ? 358 TYR B O   1 
ATOM   6213 C CB  . TYR B 1 358 ? 10.075  -32.989 34.841  1.00 120.91 ? 358 TYR B CB  1 
ATOM   6214 C CG  . TYR B 1 358 ? 10.392  -34.368 34.274  1.00 136.09 ? 358 TYR B CG  1 
ATOM   6215 C CD1 . TYR B 1 358 ? 9.677   -34.871 33.196  1.00 137.61 ? 358 TYR B CD1 1 
ATOM   6216 C CD2 . TYR B 1 358 ? 11.446  -35.144 34.764  1.00 138.55 ? 358 TYR B CD2 1 
ATOM   6217 C CE1 . TYR B 1 358 ? 9.964   -36.120 32.657  1.00 146.76 ? 358 TYR B CE1 1 
ATOM   6218 C CE2 . TYR B 1 358 ? 11.742  -36.393 34.228  1.00 133.16 ? 358 TYR B CE2 1 
ATOM   6219 C CZ  . TYR B 1 358 ? 10.995  -36.893 33.169  1.00 136.54 ? 358 TYR B CZ  1 
ATOM   6220 O OH  . TYR B 1 358 ? 11.249  -38.121 32.592  1.00 129.64 ? 358 TYR B OH  1 
ATOM   6221 N N   . ALA B 1 359 ? 9.031   -30.423 36.124  1.00 137.50 ? 359 ALA B N   1 
ATOM   6222 C CA  . ALA B 1 359 ? 9.342   -29.079 36.602  1.00 133.29 ? 359 ALA B CA  1 
ATOM   6223 C C   . ALA B 1 359 ? 8.935   -28.945 38.063  1.00 128.60 ? 359 ALA B C   1 
ATOM   6224 O O   . ALA B 1 359 ? 9.698   -28.437 38.888  1.00 123.44 ? 359 ALA B O   1 
ATOM   6225 C CB  . ALA B 1 359 ? 8.642   -28.051 35.720  1.00 155.61 ? 359 ALA B CB  1 
ATOM   6226 N N   . GLU B 1 360 ? 7.719   -29.410 38.346  1.00 126.02 ? 360 GLU B N   1 
ATOM   6227 C CA  . GLU B 1 360 ? 7.128   -29.363 39.679  1.00 135.77 ? 360 GLU B CA  1 
ATOM   6228 C C   . GLU B 1 360 ? 8.025   -30.110 40.662  1.00 126.82 ? 360 GLU B C   1 
ATOM   6229 O O   . GLU B 1 360 ? 8.325   -29.608 41.761  1.00 111.65 ? 360 GLU B O   1 
ATOM   6230 C CB  . GLU B 1 360 ? 5.699   -29.919 39.656  1.00 165.78 ? 360 GLU B CB  1 
ATOM   6231 C CG  . GLU B 1 360 ? 4.600   -28.908 39.316  1.00 196.10 ? 360 GLU B CG  1 
ATOM   6232 C CD  . GLU B 1 360 ? 3.170   -29.422 39.461  1.00 209.85 ? 360 GLU B CD  1 
ATOM   6233 O OE1 . GLU B 1 360 ? 3.028   -30.660 39.479  1.00 231.53 ? 360 GLU B OE1 1 
ATOM   6234 O OE2 . GLU B 1 360 ? 2.198   -28.640 39.540  1.00 201.16 ? 360 GLU B OE2 1 
ATOM   6235 N N   . ALA B 1 361 ? 8.436   -31.307 40.231  1.00 125.03 ? 361 ALA B N   1 
ATOM   6236 C CA  . ALA B 1 361 ? 9.286   -32.179 41.031  1.00 128.61 ? 361 ALA B CA  1 
ATOM   6237 C C   . ALA B 1 361 ? 10.594  -31.461 41.377  1.00 132.79 ? 361 ALA B C   1 
ATOM   6238 O O   . ALA B 1 361 ? 11.044  -31.468 42.539  1.00 137.44 ? 361 ALA B O   1 
ATOM   6239 C CB  . ALA B 1 361 ? 9.495   -33.485 40.299  1.00 130.53 ? 361 ALA B CB  1 
ATOM   6240 N N   . LEU B 1 362 ? 11.168  -30.839 40.346  1.00 127.74 ? 362 LEU B N   1 
ATOM   6241 C CA  . LEU B 1 362 ? 12.432  -30.125 40.464  1.00 128.09 ? 362 LEU B CA  1 
ATOM   6242 C C   . LEU B 1 362 ? 12.295  -29.001 41.492  1.00 145.26 ? 362 LEU B C   1 
ATOM   6243 O O   . LEU B 1 362 ? 13.158  -28.822 42.369  1.00 148.77 ? 362 LEU B O   1 
ATOM   6244 C CB  . LEU B 1 362 ? 12.915  -29.653 39.093  1.00 120.64 ? 362 LEU B CB  1 
ATOM   6245 C CG  . LEU B 1 362 ? 13.395  -30.759 38.147  1.00 121.30 ? 362 LEU B CG  1 
ATOM   6246 C CD1 . LEU B 1 362 ? 13.750  -30.234 36.783  1.00 119.17 ? 362 LEU B CD1 1 
ATOM   6247 C CD2 . LEU B 1 362 ? 14.608  -31.447 38.720  1.00 142.30 ? 362 LEU B CD2 1 
ATOM   6248 N N   . VAL B 1 363 ? 11.181  -28.270 41.381  1.00 151.72 ? 363 VAL B N   1 
ATOM   6249 C CA  . VAL B 1 363 ? 10.949  -27.108 42.224  1.00 155.94 ? 363 VAL B CA  1 
ATOM   6250 C C   . VAL B 1 363 ? 10.783  -27.594 43.659  1.00 173.36 ? 363 VAL B C   1 
ATOM   6251 O O   . VAL B 1 363 ? 11.344  -27.024 44.607  1.00 195.28 ? 363 VAL B O   1 
ATOM   6252 C CB  . VAL B 1 363 ? 9.803   -26.206 41.742  1.00 185.62 ? 363 VAL B CB  1 
ATOM   6253 C CG1 . VAL B 1 363 ? 9.679   -24.956 42.607  1.00 235.10 ? 363 VAL B CG1 1 
ATOM   6254 C CG2 . VAL B 1 363 ? 9.997   -25.810 40.281  1.00 197.29 ? 363 VAL B CG2 1 
ATOM   6255 N N   . GLY B 1 364 ? 9.916   -28.605 43.787  1.00 169.83 ? 364 GLY B N   1 
ATOM   6256 C CA  . GLY B 1 364 ? 9.472   -29.117 45.070  1.00 163.69 ? 364 GLY B CA  1 
ATOM   6257 C C   . GLY B 1 364 ? 8.039   -28.681 45.360  1.00 156.27 ? 364 GLY B C   1 
ATOM   6258 O O   . GLY B 1 364 ? 7.462   -29.096 46.359  1.00 167.38 ? 364 GLY B O   1 
ATOM   6259 N N   . ALA B 1 365 ? 7.481   -27.849 44.472  1.00 162.75 ? 365 ALA B N   1 
ATOM   6260 C CA  . ALA B 1 365 ? 6.162   -27.264 44.660  1.00 192.39 ? 365 ALA B CA  1 
ATOM   6261 C C   . ALA B 1 365 ? 5.284   -27.500 43.435  1.00 205.47 ? 365 ALA B C   1 
ATOM   6262 O O   . ALA B 1 365 ? 5.781   -27.793 42.350  1.00 230.19 ? 365 ALA B O   1 
ATOM   6263 C CB  . ALA B 1 365 ? 6.278   -25.791 44.973  1.00 187.36 ? 365 ALA B CB  1 
ATOM   6264 N N   . ARG B 1 366 ? 3.966   -27.386 43.648  1.00 195.88 ? 366 ARG B N   1 
ATOM   6265 C CA  . ARG B 1 366 ? 2.980   -27.529 42.592  1.00 204.63 ? 366 ARG B CA  1 
ATOM   6266 C C   . ARG B 1 366 ? 2.926   -26.229 41.806  1.00 213.92 ? 366 ARG B C   1 
ATOM   6267 O O   . ARG B 1 366 ? 3.640   -25.288 42.151  1.00 214.15 ? 366 ARG B O   1 
ATOM   6268 C CB  . ARG B 1 366 ? 1.632   -27.867 43.233  1.00 220.03 ? 366 ARG B CB  1 
ATOM   6269 C CG  . ARG B 1 366 ? 1.828   -28.982 44.250  1.00 205.42 ? 366 ARG B CG  1 
ATOM   6270 C CD  . ARG B 1 366 ? 0.603   -29.869 44.398  1.00 217.69 ? 366 ARG B CD  1 
ATOM   6271 N NE  . ARG B 1 366 ? 0.179   -30.340 43.074  1.00 210.31 ? 366 ARG B NE  1 
ATOM   6272 C CZ  . ARG B 1 366 ? 0.051   -31.608 42.715  1.00 203.43 ? 366 ARG B CZ  1 
ATOM   6273 N NH1 . ARG B 1 366 ? 0.294   -32.579 43.585  1.00 210.70 ? 366 ARG B NH1 1 
ATOM   6274 N NH2 . ARG B 1 366 ? -0.346  -31.897 41.488  1.00 187.65 ? 366 ARG B NH2 1 
ATOM   6275 N N   . VAL B 1 367 ? 2.058   -26.188 40.782  1.00 219.48 ? 367 VAL B N   1 
ATOM   6276 C CA  . VAL B 1 367 ? 2.020   -25.120 39.788  1.00 223.74 ? 367 VAL B CA  1 
ATOM   6277 C C   . VAL B 1 367 ? 2.058   -23.731 40.428  1.00 227.37 ? 367 VAL B C   1 
ATOM   6278 O O   . VAL B 1 367 ? 2.677   -22.826 39.872  1.00 226.03 ? 367 VAL B O   1 
ATOM   6279 C CB  . VAL B 1 367 ? 0.971   -25.258 38.662  1.00 228.10 ? 367 VAL B CB  1 
ATOM   6280 C CG1 . VAL B 1 367 ? 0.021   -24.069 38.545  1.00 240.10 ? 367 VAL B CG1 1 
ATOM   6281 C CG2 . VAL B 1 367 ? 1.649   -25.572 37.331  1.00 236.66 ? 367 VAL B CG2 1 
ATOM   6282 N N   . GLY B 1 368 ? 1.399   -23.564 41.583  1.00 224.93 ? 368 GLY B N   1 
ATOM   6283 C CA  . GLY B 1 368 ? 1.440   -22.320 42.333  1.00 231.70 ? 368 GLY B CA  1 
ATOM   6284 C C   . GLY B 1 368 ? 0.209   -21.468 42.044  1.00 244.65 ? 368 GLY B C   1 
ATOM   6285 O O   . GLY B 1 368 ? -0.142  -21.272 40.887  1.00 233.55 ? 368 GLY B O   1 
ATOM   6286 N N   . ALA B 1 369 ? -0.454  -21.001 43.110  1.00 251.52 ? 369 ALA B N   1 
ATOM   6287 C CA  . ALA B 1 369 ? -1.620  -20.131 43.028  1.00 240.09 ? 369 ALA B CA  1 
ATOM   6288 C C   . ALA B 1 369 ? -2.571  -20.534 41.896  1.00 230.54 ? 369 ALA B C   1 
ATOM   6289 O O   . ALA B 1 369 ? -2.735  -21.709 41.562  1.00 232.32 ? 369 ALA B O   1 
ATOM   6290 C CB  . ALA B 1 369 ? -1.172  -18.689 42.894  1.00 231.86 ? 369 ALA B CB  1 
ATOM   6291 N N   . ASP B 1 370 ? -3.251  -19.527 41.340  1.00 212.76 ? 370 ASP B N   1 
ATOM   6292 C CA  . ASP B 1 370 ? -4.067  -19.725 40.157  1.00 228.97 ? 370 ASP B CA  1 
ATOM   6293 C C   . ASP B 1 370 ? -3.127  -19.758 38.955  1.00 242.70 ? 370 ASP B C   1 
ATOM   6294 O O   . ASP B 1 370 ? -3.503  -20.188 37.863  1.00 266.14 ? 370 ASP B O   1 
ATOM   6295 C CB  . ASP B 1 370 ? -5.129  -18.641 40.051  1.00 252.97 ? 370 ASP B CB  1 
ATOM   6296 C CG  . ASP B 1 370 ? -6.319  -18.976 39.163  1.00 281.48 ? 370 ASP B CG  1 
ATOM   6297 O OD1 . ASP B 1 370 ? -7.001  -19.978 39.461  1.00 294.78 ? 370 ASP B OD1 1 
ATOM   6298 O OD2 . ASP B 1 370 ? -6.565  -18.229 38.189  1.00 282.09 ? 370 ASP B OD2 1 
ATOM   6299 N N   . GLY B 1 371 ? -1.891  -19.303 39.193  1.00 235.45 ? 371 GLY B N   1 
ATOM   6300 C CA  . GLY B 1 371 ? -0.891  -19.227 38.143  1.00 221.97 ? 371 GLY B CA  1 
ATOM   6301 C C   . GLY B 1 371 ? 0.441   -18.697 38.664  1.00 214.08 ? 371 GLY B C   1 
ATOM   6302 O O   . GLY B 1 371 ? 0.484   -17.947 39.643  1.00 194.13 ? 371 GLY B O   1 
ATOM   6303 N N   . MET B 1 372 ? 1.520   -19.150 38.007  1.00 223.37 ? 372 MET B N   1 
ATOM   6304 C CA  . MET B 1 372 ? 2.862   -18.582 38.057  1.00 261.30 ? 372 MET B CA  1 
ATOM   6305 C C   . MET B 1 372 ? 3.945   -19.638 38.285  1.00 267.22 ? 372 MET B C   1 
ATOM   6306 O O   . MET B 1 372 ? 4.879   -19.699 37.494  1.00 294.89 ? 372 MET B O   1 
ATOM   6307 C CB  . MET B 1 372 ? 3.034   -17.389 39.008  1.00 274.29 ? 372 MET B CB  1 
ATOM   6308 C CG  . MET B 1 372 ? 4.386   -16.708 38.886  1.00 266.25 ? 372 MET B CG  1 
ATOM   6309 S SD  . MET B 1 372 ? 4.722   -16.024 37.253  1.00 255.46 ? 372 MET B SD  1 
ATOM   6310 C CE  . MET B 1 372 ? 6.430   -16.541 37.054  1.00 230.83 ? 372 MET B CE  1 
ATOM   6311 N N   . LEU B 1 373 ? 3.870   -20.415 39.374  1.00 236.66 ? 373 LEU B N   1 
ATOM   6312 C CA  . LEU B 1 373 ? 4.931   -21.340 39.771  1.00 206.13 ? 373 LEU B CA  1 
ATOM   6313 C C   . LEU B 1 373 ? 6.124   -20.586 40.345  1.00 181.65 ? 373 LEU B C   1 
ATOM   6314 O O   . LEU B 1 373 ? 6.773   -19.798 39.672  1.00 166.57 ? 373 LEU B O   1 
ATOM   6315 C CB  . LEU B 1 373 ? 5.392   -22.366 38.735  1.00 204.40 ? 373 LEU B CB  1 
ATOM   6316 C CG  . LEU B 1 373 ? 6.650   -23.156 39.114  1.00 171.67 ? 373 LEU B CG  1 
ATOM   6317 C CD1 . LEU B 1 373 ? 6.415   -23.908 40.409  1.00 153.77 ? 373 LEU B CD1 1 
ATOM   6318 C CD2 . LEU B 1 373 ? 7.099   -24.098 38.013  1.00 159.71 ? 373 LEU B CD2 1 
ATOM   6319 N N   . ARG B 1 374 ? 6.418   -20.886 41.610  1.00 174.60 ? 374 ARG B N   1 
ATOM   6320 C CA  . ARG B 1 374 ? 7.412   -20.151 42.363  1.00 179.23 ? 374 ARG B CA  1 
ATOM   6321 C C   . ARG B 1 374 ? 8.064   -21.101 43.363  1.00 174.34 ? 374 ARG B C   1 
ATOM   6322 O O   . ARG B 1 374 ? 7.425   -22.019 43.872  1.00 167.93 ? 374 ARG B O   1 
ATOM   6323 C CB  . ARG B 1 374 ? 6.784   -18.957 43.098  1.00 182.59 ? 374 ARG B CB  1 
ATOM   6324 C CG  . ARG B 1 374 ? 5.510   -18.352 42.520  1.00 177.19 ? 374 ARG B CG  1 
ATOM   6325 C CD  . ARG B 1 374 ? 5.042   -17.136 43.302  1.00 185.18 ? 374 ARG B CD  1 
ATOM   6326 N NE  . ARG B 1 374 ? 3.607   -16.892 43.106  1.00 201.30 ? 374 ARG B NE  1 
ATOM   6327 C CZ  . ARG B 1 374 ? 3.066   -15.839 42.509  1.00 195.26 ? 374 ARG B CZ  1 
ATOM   6328 N NH1 . ARG B 1 374 ? 3.839   -14.895 42.002  1.00 191.55 ? 374 ARG B NH1 1 
ATOM   6329 N NH2 . ARG B 1 374 ? 1.751   -15.749 42.398  1.00 184.25 ? 374 ARG B NH2 1 
ATOM   6330 N N   . GLY B 1 375 ? 9.350   -20.846 43.640  1.00 173.33 ? 375 GLY B N   1 
ATOM   6331 C CA  . GLY B 1 375 ? 10.148  -21.648 44.553  1.00 169.25 ? 375 GLY B CA  1 
ATOM   6332 C C   . GLY B 1 375 ? 9.743   -21.433 46.010  1.00 192.40 ? 375 GLY B C   1 
ATOM   6333 O O   . GLY B 1 375 ? 8.845   -20.647 46.315  1.00 211.60 ? 375 GLY B O   1 
ATOM   6334 N N   . ALA B 1 376 ? 10.445  -22.137 46.904  1.00 204.94 ? 376 ALA B N   1 
ATOM   6335 C CA  . ALA B 1 376 ? 10.205  -22.084 48.338  1.00 224.01 ? 376 ALA B CA  1 
ATOM   6336 C C   . ALA B 1 376 ? 10.211  -20.639 48.835  1.00 242.06 ? 376 ALA B C   1 
ATOM   6337 O O   . ALA B 1 376 ? 9.342   -20.255 49.619  1.00 245.40 ? 376 ALA B O   1 
ATOM   6338 C CB  . ALA B 1 376 ? 11.248  -22.916 49.053  1.00 216.05 ? 376 ALA B CB  1 
ATOM   6339 N N   . ASP B 1 377 ? 11.188  -19.858 48.345  1.00 244.05 ? 377 ASP B N   1 
ATOM   6340 C CA  . ASP B 1 377 ? 11.425  -18.479 48.743  1.00 224.69 ? 377 ASP B CA  1 
ATOM   6341 C C   . ASP B 1 377 ? 10.345  -17.557 48.185  1.00 223.14 ? 377 ASP B C   1 
ATOM   6342 O O   . ASP B 1 377 ? 10.235  -16.416 48.627  1.00 239.73 ? 377 ASP B O   1 
ATOM   6343 C CB  . ASP B 1 377 ? 12.799  -18.007 48.296  1.00 219.93 ? 377 ASP B CB  1 
ATOM   6344 C CG  . ASP B 1 377 ? 13.122  -18.212 46.821  1.00 231.47 ? 377 ASP B CG  1 
ATOM   6345 O OD1 . ASP B 1 377 ? 12.227  -18.655 46.067  1.00 236.31 ? 377 ASP B OD1 1 
ATOM   6346 O OD2 . ASP B 1 377 ? 14.277  -17.953 46.433  1.00 245.11 ? 377 ASP B OD2 1 
ATOM   6347 N N   . GLY B 1 378 ? 9.576   -18.054 47.204  1.00 222.50 ? 378 GLY B N   1 
ATOM   6348 C CA  . GLY B 1 378 ? 8.460   -17.322 46.627  1.00 222.14 ? 378 GLY B CA  1 
ATOM   6349 C C   . GLY B 1 378 ? 8.811   -16.734 45.262  1.00 226.02 ? 378 GLY B C   1 
ATOM   6350 O O   . GLY B 1 378 ? 7.918   -16.362 44.505  1.00 211.21 ? 378 GLY B O   1 
ATOM   6351 N N   . ARG B 1 379 ? 10.119  -16.644 44.984  1.00 231.55 ? 379 ARG B N   1 
ATOM   6352 C CA  . ARG B 1 379 ? 10.683  -16.163 43.734  1.00 240.85 ? 379 ARG B CA  1 
ATOM   6353 C C   . ARG B 1 379 ? 10.227  -17.031 42.571  1.00 237.54 ? 379 ARG B C   1 
ATOM   6354 O O   . ARG B 1 379 ? 10.282  -18.266 42.621  1.00 260.47 ? 379 ARG B O   1 
ATOM   6355 C CB  . ARG B 1 379 ? 12.212  -16.054 43.812  1.00 245.18 ? 379 ARG B CB  1 
ATOM   6356 C CG  . ARG B 1 379 ? 12.773  -14.914 44.654  1.00 265.39 ? 379 ARG B CG  1 
ATOM   6357 C CD  . ARG B 1 379 ? 12.523  -13.541 44.047  1.00 304.35 ? 379 ARG B CD  1 
ATOM   6358 N NE  . ARG B 1 379 ? 12.698  -13.556 42.590  1.00 301.44 ? 379 ARG B NE  1 
ATOM   6359 C CZ  . ARG B 1 379 ? 13.803  -13.876 41.927  1.00 280.41 ? 379 ARG B CZ  1 
ATOM   6360 N NH1 . ARG B 1 379 ? 14.939  -14.119 42.560  1.00 247.19 ? 379 ARG B NH1 1 
ATOM   6361 N NH2 . ARG B 1 379 ? 13.759  -13.941 40.614  1.00 290.82 ? 379 ARG B NH2 1 
ATOM   6362 N N   . PRO B 1 380 ? 9.803   -16.352 41.483  1.00 207.07 ? 380 PRO B N   1 
ATOM   6363 C CA  . PRO B 1 380 ? 9.314   -17.000 40.277  1.00 193.29 ? 380 PRO B CA  1 
ATOM   6364 C C   . PRO B 1 380 ? 10.286  -17.984 39.622  1.00 213.87 ? 380 PRO B C   1 
ATOM   6365 O O   . PRO B 1 380 ? 11.508  -17.939 39.801  1.00 203.47 ? 380 PRO B O   1 
ATOM   6366 C CB  . PRO B 1 380 ? 8.993   -15.824 39.362  1.00 169.29 ? 380 PRO B CB  1 
ATOM   6367 C CG  . PRO B 1 380 ? 8.704   -14.699 40.309  1.00 186.53 ? 380 PRO B CG  1 
ATOM   6368 C CD  . PRO B 1 380 ? 9.808   -14.887 41.339  1.00 206.91 ? 380 PRO B CD  1 
ATOM   6369 N N   . VAL B 1 381 ? 9.682   -18.888 38.855  1.00 225.35 ? 381 VAL B N   1 
ATOM   6370 C CA  . VAL B 1 381 ? 10.370  -19.961 38.154  1.00 190.38 ? 381 VAL B CA  1 
ATOM   6371 C C   . VAL B 1 381 ? 9.947   -19.974 36.682  1.00 187.06 ? 381 VAL B C   1 
ATOM   6372 O O   . VAL B 1 381 ? 8.764   -19.920 36.330  1.00 185.91 ? 381 VAL B O   1 
ATOM   6373 C CB  . VAL B 1 381 ? 10.122  -21.331 38.801  1.00 186.07 ? 381 VAL B CB  1 
ATOM   6374 C CG1 . VAL B 1 381 ? 10.937  -22.417 38.114  1.00 194.13 ? 381 VAL B CG1 1 
ATOM   6375 C CG2 . VAL B 1 381 ? 10.414  -21.305 40.292  1.00 192.95 ? 381 VAL B CG2 1 
ATOM   6376 N N   . TYR B 1 382 ? 10.973  -20.038 35.835  1.00 174.14 ? 382 TYR B N   1 
ATOM   6377 C CA  . TYR B 1 382 ? 10.840  -20.001 34.388  1.00 184.05 ? 382 TYR B CA  1 
ATOM   6378 C C   . TYR B 1 382 ? 11.628  -21.154 33.766  1.00 190.24 ? 382 TYR B C   1 
ATOM   6379 O O   . TYR B 1 382 ? 12.807  -21.366 34.082  1.00 207.95 ? 382 TYR B O   1 
ATOM   6380 C CB  . TYR B 1 382 ? 11.381  -18.726 33.742  1.00 176.31 ? 382 TYR B CB  1 
ATOM   6381 C CG  . TYR B 1 382 ? 10.809  -17.444 34.314  1.00 173.76 ? 382 TYR B CG  1 
ATOM   6382 C CD1 . TYR B 1 382 ? 9.584   -16.960 33.877  1.00 188.81 ? 382 TYR B CD1 1 
ATOM   6383 C CD2 . TYR B 1 382 ? 11.494  -16.727 35.288  1.00 161.36 ? 382 TYR B CD2 1 
ATOM   6384 C CE1 . TYR B 1 382 ? 9.052   -15.792 34.397  1.00 210.80 ? 382 TYR B CE1 1 
ATOM   6385 C CE2 . TYR B 1 382 ? 10.973  -15.559 35.815  1.00 180.45 ? 382 TYR B CE2 1 
ATOM   6386 C CZ  . TYR B 1 382 ? 9.753   -15.086 35.362  1.00 205.68 ? 382 TYR B CZ  1 
ATOM   6387 O OH  . TYR B 1 382 ? 9.243   -13.930 35.880  1.00 222.30 ? 382 TYR B OH  1 
ATOM   6388 N N   . TYR B 1 383 ? 10.938  -21.859 32.859  1.00 179.08 ? 383 TYR B N   1 
ATOM   6389 C CA  . TYR B 1 383 ? 11.481  -23.034 32.208  1.00 160.46 ? 383 TYR B CA  1 
ATOM   6390 C C   . TYR B 1 383 ? 11.306  -22.985 30.695  1.00 144.68 ? 383 TYR B C   1 
ATOM   6391 O O   . TYR B 1 383 ? 10.315  -22.540 30.134  1.00 145.60 ? 383 TYR B O   1 
ATOM   6392 C CB  . TYR B 1 383 ? 11.105  -24.353 32.880  1.00 172.06 ? 383 TYR B CB  1 
ATOM   6393 C CG  . TYR B 1 383 ? 9.688   -24.875 32.713  1.00 172.35 ? 383 TYR B CG  1 
ATOM   6394 C CD1 . TYR B 1 383 ? 9.322   -25.609 31.580  1.00 167.77 ? 383 TYR B CD1 1 
ATOM   6395 C CD2 . TYR B 1 383 ? 8.759   -24.733 33.740  1.00 160.59 ? 383 TYR B CD2 1 
ATOM   6396 C CE1 . TYR B 1 383 ? 8.050   -26.141 31.446  1.00 152.17 ? 383 TYR B CE1 1 
ATOM   6397 C CE2 . TYR B 1 383 ? 7.486   -25.271 33.622  1.00 163.69 ? 383 TYR B CE2 1 
ATOM   6398 C CZ  . TYR B 1 383 ? 7.142   -25.985 32.483  1.00 158.66 ? 383 TYR B CZ  1 
ATOM   6399 O OH  . TYR B 1 383 ? 5.872   -26.476 32.360  1.00 140.44 ? 383 TYR B OH  1 
ATOM   6400 N N   . THR B 1 384 ? 12.315  -23.559 30.037  1.00 157.54 ? 384 THR B N   1 
ATOM   6401 C CA  . THR B 1 384 ? 12.369  -23.771 28.591  1.00 156.64 ? 384 THR B CA  1 
ATOM   6402 C C   . THR B 1 384 ? 12.599  -25.256 28.282  1.00 161.08 ? 384 THR B C   1 
ATOM   6403 O O   . THR B 1 384 ? 13.540  -25.864 28.810  1.00 146.05 ? 384 THR B O   1 
ATOM   6404 C CB  . THR B 1 384 ? 13.505  -22.938 27.987  1.00 147.73 ? 384 THR B CB  1 
ATOM   6405 O OG1 . THR B 1 384 ? 13.346  -21.579 28.380  1.00 132.61 ? 384 THR B OG1 1 
ATOM   6406 C CG2 . THR B 1 384 ? 13.550  -23.040 26.476  1.00 143.92 ? 384 THR B CG2 1 
ATOM   6407 N N   . HIS B 1 385 ? 11.690  -25.799 27.462  1.00 149.51 ? 385 HIS B N   1 
ATOM   6408 C CA  . HIS B 1 385 ? 11.655  -27.219 27.165  1.00 149.67 ? 385 HIS B CA  1 
ATOM   6409 C C   . HIS B 1 385 ? 11.648  -27.459 25.652  1.00 149.85 ? 385 HIS B C   1 
ATOM   6410 O O   . HIS B 1 385 ? 10.840  -26.892 24.941  1.00 139.58 ? 385 HIS B O   1 
ATOM   6411 C CB  . HIS B 1 385 ? 10.423  -27.891 27.773  1.00 138.64 ? 385 HIS B CB  1 
ATOM   6412 C CG  . HIS B 1 385 ? 10.166  -29.229 27.167  1.00 128.96 ? 385 HIS B CG  1 
ATOM   6413 N ND1 . HIS B 1 385 ? 10.729  -30.404 27.619  1.00 132.87 ? 385 HIS B ND1 1 
ATOM   6414 C CD2 . HIS B 1 385 ? 9.420   -29.553 26.103  1.00 127.03 ? 385 HIS B CD2 1 
ATOM   6415 C CE1 . HIS B 1 385 ? 10.324  -31.402 26.839  1.00 153.83 ? 385 HIS B CE1 1 
ATOM   6416 N NE2 . HIS B 1 385 ? 9.516   -30.908 25.915  1.00 143.02 ? 385 HIS B NE2 1 
ATOM   6417 N N   . GLY B 1 386 ? 12.571  -28.296 25.208  1.00 168.61 ? 386 GLY B N   1 
ATOM   6418 C CA  . GLY B 1 386 ? 12.873  -28.503 23.809  1.00 161.40 ? 386 GLY B CA  1 
ATOM   6419 C C   . GLY B 1 386 ? 13.091  -29.988 23.565  1.00 138.06 ? 386 GLY B C   1 
ATOM   6420 O O   . GLY B 1 386 ? 13.811  -30.682 24.294  1.00 122.68 ? 386 GLY B O   1 
ATOM   6421 N N   . ARG B 1 387 ? 12.501  -30.474 22.472  1.00 123.37 ? 387 ARG B N   1 
ATOM   6422 C CA  . ARG B 1 387 ? 12.969  -31.667 21.766  1.00 120.63 ? 387 ARG B CA  1 
ATOM   6423 C C   . ARG B 1 387 ? 14.100  -31.289 20.813  1.00 139.25 ? 387 ARG B C   1 
ATOM   6424 O O   . ARG B 1 387 ? 13.962  -30.381 19.995  1.00 157.12 ? 387 ARG B O   1 
ATOM   6425 C CB  . ARG B 1 387 ? 11.835  -32.309 20.967  1.00 92.94  ? 387 ARG B CB  1 
ATOM   6426 C CG  . ARG B 1 387 ? 10.524  -32.345 21.727  1.00 97.77  ? 387 ARG B CG  1 
ATOM   6427 C CD  . ARG B 1 387 ? 9.507   -33.117 20.930  1.00 130.40 ? 387 ARG B CD  1 
ATOM   6428 N NE  . ARG B 1 387 ? 8.332   -33.195 21.801  1.00 166.46 ? 387 ARG B NE  1 
ATOM   6429 C CZ  . ARG B 1 387 ? 7.281   -33.965 21.578  1.00 189.39 ? 387 ARG B CZ  1 
ATOM   6430 N NH1 . ARG B 1 387 ? 7.208   -34.729 20.495  1.00 182.46 ? 387 ARG B NH1 1 
ATOM   6431 N NH2 . ARG B 1 387 ? 6.313   -33.978 22.471  1.00 208.69 ? 387 ARG B NH2 1 
ATOM   6432 N N   . LEU B 1 388 ? 15.229  -32.004 20.950  1.00 138.94 ? 388 LEU B N   1 
ATOM   6433 C CA  . LEU B 1 388 ? 16.358  -31.903 20.040  1.00 119.44 ? 388 LEU B CA  1 
ATOM   6434 C C   . LEU B 1 388 ? 16.740  -33.279 19.505  1.00 125.82 ? 388 LEU B C   1 
ATOM   6435 O O   . LEU B 1 388 ? 16.937  -34.216 20.283  1.00 149.73 ? 388 LEU B O   1 
ATOM   6436 C CB  . LEU B 1 388 ? 17.589  -31.193 20.598  1.00 116.40 ? 388 LEU B CB  1 
ATOM   6437 C CG  . LEU B 1 388 ? 17.866  -31.340 22.095  1.00 129.07 ? 388 LEU B CG  1 
ATOM   6438 C CD1 . LEU B 1 388 ? 19.363  -31.446 22.324  1.00 168.19 ? 388 LEU B CD1 1 
ATOM   6439 C CD2 . LEU B 1 388 ? 17.332  -30.128 22.840  1.00 136.41 ? 388 LEU B CD2 1 
ATOM   6440 N N   . LEU B 1 389 ? 16.836  -33.351 18.170  1.00 127.93 ? 389 LEU B N   1 
ATOM   6441 C CA  . LEU B 1 389 ? 17.288  -34.550 17.482  1.00 137.99 ? 389 LEU B CA  1 
ATOM   6442 C C   . LEU B 1 389 ? 18.459  -34.243 16.540  1.00 163.31 ? 389 LEU B C   1 
ATOM   6443 O O   . LEU B 1 389 ? 18.362  -33.334 15.722  1.00 196.91 ? 389 LEU B O   1 
ATOM   6444 C CB  . LEU B 1 389 ? 16.020  -35.007 16.769  1.00 106.30 ? 389 LEU B CB  1 
ATOM   6445 C CG  . LEU B 1 389 ? 16.215  -36.099 15.720  1.00 123.87 ? 389 LEU B CG  1 
ATOM   6446 C CD1 . LEU B 1 389 ? 15.036  -37.013 15.903  1.00 137.64 ? 389 LEU B CD1 1 
ATOM   6447 C CD2 . LEU B 1 389 ? 16.227  -35.534 14.301  1.00 123.82 ? 389 LEU B CD2 1 
ATOM   6448 N N   . GLU B 1 390 ? 19.576  -34.952 16.748  1.00 157.12 ? 390 GLU B N   1 
ATOM   6449 C CA  . GLU B 1 390 ? 20.780  -34.779 15.971  1.00 172.59 ? 390 GLU B CA  1 
ATOM   6450 C C   . GLU B 1 390 ? 21.409  -36.147 15.938  1.00 157.92 ? 390 GLU B C   1 
ATOM   6451 O O   . GLU B 1 390 ? 22.153  -36.453 16.856  1.00 140.52 ? 390 GLU B O   1 
ATOM   6452 C CB  . GLU B 1 390 ? 21.786  -33.800 16.587  1.00 216.24 ? 390 GLU B CB  1 
ATOM   6453 C CG  . GLU B 1 390 ? 21.582  -32.345 16.168  1.00 243.55 ? 390 GLU B CG  1 
ATOM   6454 C CD  . GLU B 1 390 ? 22.151  -31.974 14.804  1.00 240.10 ? 390 GLU B CD  1 
ATOM   6455 O OE1 . GLU B 1 390 ? 23.365  -32.179 14.560  1.00 198.97 ? 390 GLU B OE1 1 
ATOM   6456 O OE2 . GLU B 1 390 ? 21.361  -31.461 13.977  1.00 274.38 ? 390 GLU B OE2 1 
ATOM   6457 N N   . PRO B 1 391 ? 21.014  -37.019 14.984  1.00 155.83 ? 391 PRO B N   1 
ATOM   6458 C CA  . PRO B 1 391 ? 21.620  -38.347 14.857  1.00 155.99 ? 391 PRO B CA  1 
ATOM   6459 C C   . PRO B 1 391 ? 23.137  -38.251 15.010  1.00 152.71 ? 391 PRO B C   1 
ATOM   6460 O O   . PRO B 1 391 ? 23.750  -38.953 15.817  1.00 143.06 ? 391 PRO B O   1 
ATOM   6461 C CB  . PRO B 1 391 ? 21.188  -38.822 13.454  1.00 143.27 ? 391 PRO B CB  1 
ATOM   6462 C CG  . PRO B 1 391 ? 19.978  -37.977 13.082  1.00 135.82 ? 391 PRO B CG  1 
ATOM   6463 C CD  . PRO B 1 391 ? 19.924  -36.779 14.022  1.00 141.02 ? 391 PRO B CD  1 
ATOM   6464 N N   . GLU B 1 392 ? 23.699  -37.303 14.259  1.00 156.43 ? 392 GLU B N   1 
ATOM   6465 C CA  . GLU B 1 392 ? 25.126  -37.185 14.021  1.00 166.43 ? 392 GLU B CA  1 
ATOM   6466 C C   . GLU B 1 392 ? 25.880  -37.055 15.331  1.00 167.98 ? 392 GLU B C   1 
ATOM   6467 O O   . GLU B 1 392 ? 26.869  -37.751 15.549  1.00 203.26 ? 392 GLU B O   1 
ATOM   6468 C CB  . GLU B 1 392 ? 25.344  -35.922 13.192  1.00 196.18 ? 392 GLU B CB  1 
ATOM   6469 C CG  . GLU B 1 392 ? 24.315  -35.737 12.078  1.00 219.26 ? 392 GLU B CG  1 
ATOM   6470 C CD  . GLU B 1 392 ? 24.316  -36.689 10.886  1.00 228.31 ? 392 GLU B CD  1 
ATOM   6471 O OE1 . GLU B 1 392 ? 25.390  -37.001 10.319  1.00 247.20 ? 392 GLU B OE1 1 
ATOM   6472 O OE2 . GLU B 1 392 ? 23.203  -37.101 10.502  1.00 211.02 ? 392 GLU B OE2 1 
ATOM   6473 N N   . THR B 1 393 ? 25.397  -36.158 16.197  1.00 157.61 ? 393 THR B N   1 
ATOM   6474 C CA  . THR B 1 393 ? 26.158  -35.759 17.370  1.00 160.28 ? 393 THR B CA  1 
ATOM   6475 C C   . THR B 1 393 ? 25.614  -36.445 18.623  1.00 168.21 ? 393 THR B C   1 
ATOM   6476 O O   . THR B 1 393 ? 26.355  -36.779 19.545  1.00 192.33 ? 393 THR B O   1 
ATOM   6477 C CB  . THR B 1 393 ? 26.136  -34.241 17.510  1.00 164.70 ? 393 THR B CB  1 
ATOM   6478 O OG1 . THR B 1 393 ? 24.798  -33.912 17.873  1.00 194.33 ? 393 THR B OG1 1 
ATOM   6479 C CG2 . THR B 1 393 ? 26.557  -33.543 16.231  1.00 171.05 ? 393 THR B CG2 1 
ATOM   6480 N N   . LEU B 1 394 ? 24.300  -36.623 18.676  1.00 139.92 ? 394 LEU B N   1 
ATOM   6481 C CA  . LEU B 1 394 ? 23.732  -37.147 19.895  1.00 134.27 ? 394 LEU B CA  1 
ATOM   6482 C C   . LEU B 1 394 ? 23.886  -38.664 19.899  1.00 151.54 ? 394 LEU B C   1 
ATOM   6483 O O   . LEU B 1 394 ? 23.948  -39.271 20.959  1.00 169.64 ? 394 LEU B O   1 
ATOM   6484 C CB  . LEU B 1 394 ? 22.283  -36.679 20.032  1.00 125.04 ? 394 LEU B CB  1 
ATOM   6485 C CG  . LEU B 1 394 ? 22.084  -35.199 20.377  1.00 115.11 ? 394 LEU B CG  1 
ATOM   6486 C CD1 . LEU B 1 394 ? 20.609  -34.854 20.473  1.00 93.60  ? 394 LEU B CD1 1 
ATOM   6487 C CD2 . LEU B 1 394 ? 22.783  -34.803 21.666  1.00 117.71 ? 394 LEU B CD2 1 
ATOM   6488 N N   . GLY B 1 395 ? 23.974  -39.262 18.703  1.00 156.91 ? 395 GLY B N   1 
ATOM   6489 C CA  . GLY B 1 395 ? 24.010  -40.710 18.545  1.00 164.23 ? 395 GLY B CA  1 
ATOM   6490 C C   . GLY B 1 395 ? 25.334  -41.290 19.040  1.00 161.05 ? 395 GLY B C   1 
ATOM   6491 O O   . GLY B 1 395 ? 25.553  -42.502 18.981  1.00 167.22 ? 395 GLY B O   1 
ATOM   6492 N N   . LYS B 1 396 ? 26.190  -40.393 19.544  1.00 139.50 ? 396 LYS B N   1 
ATOM   6493 C CA  . LYS B 1 396 ? 27.472  -40.724 20.134  1.00 154.32 ? 396 LYS B CA  1 
ATOM   6494 C C   . LYS B 1 396 ? 27.295  -40.949 21.636  1.00 161.83 ? 396 LYS B C   1 
ATOM   6495 O O   . LYS B 1 396 ? 28.080  -41.662 22.256  1.00 190.14 ? 396 LYS B O   1 
ATOM   6496 C CB  . LYS B 1 396 ? 28.418  -39.550 19.857  1.00 164.67 ? 396 LYS B CB  1 
ATOM   6497 C CG  . LYS B 1 396 ? 29.256  -39.506 18.566  1.00 168.17 ? 396 LYS B CG  1 
ATOM   6498 C CD  . LYS B 1 396 ? 29.542  -38.140 17.925  1.00 168.17 ? 396 LYS B CD  1 
ATOM   6499 C CE  . LYS B 1 396 ? 30.112  -36.940 18.687  1.00 149.24 ? 396 LYS B CE  1 
ATOM   6500 N NZ  . LYS B 1 396 ? 31.540  -36.950 19.021  1.00 152.11 ? 396 LYS B NZ  1 
ATOM   6501 N N   . LEU B 1 397 ? 26.260  -40.337 22.221  1.00 138.52 ? 397 LEU B N   1 
ATOM   6502 C CA  . LEU B 1 397 ? 26.089  -40.317 23.664  1.00 136.52 ? 397 LEU B CA  1 
ATOM   6503 C C   . LEU B 1 397 ? 25.337  -41.543 24.166  1.00 123.85 ? 397 LEU B C   1 
ATOM   6504 O O   . LEU B 1 397 ? 24.664  -42.218 23.394  1.00 112.15 ? 397 LEU B O   1 
ATOM   6505 C CB  . LEU B 1 397 ? 25.280  -39.055 23.945  1.00 128.16 ? 397 LEU B CB  1 
ATOM   6506 C CG  . LEU B 1 397 ? 26.065  -37.750 23.911  1.00 119.11 ? 397 LEU B CG  1 
ATOM   6507 C CD1 . LEU B 1 397 ? 25.147  -36.626 23.549  1.00 119.38 ? 397 LEU B CD1 1 
ATOM   6508 C CD2 . LEU B 1 397 ? 26.526  -37.593 25.331  1.00 118.80 ? 397 LEU B CD2 1 
ATOM   6509 N N   . ASN B 1 398 ? 25.449  -41.774 25.476  1.00 124.19 ? 398 ASN B N   1 
ATOM   6510 C CA  . ASN B 1 398 ? 24.500  -42.580 26.218  1.00 133.53 ? 398 ASN B CA  1 
ATOM   6511 C C   . ASN B 1 398 ? 23.986  -41.748 27.399  1.00 129.50 ? 398 ASN B C   1 
ATOM   6512 O O   . ASN B 1 398 ? 24.588  -40.725 27.717  1.00 117.73 ? 398 ASN B O   1 
ATOM   6513 C CB  . ASN B 1 398 ? 25.153  -43.889 26.635  1.00 144.10 ? 398 ASN B CB  1 
ATOM   6514 C CG  . ASN B 1 398 ? 25.978  -43.696 27.876  1.00 161.55 ? 398 ASN B CG  1 
ATOM   6515 O OD1 . ASN B 1 398 ? 26.113  -42.563 28.352  1.00 126.61 ? 398 ASN B OD1 1 
ATOM   6516 N ND2 . ASN B 1 398 ? 26.551  -44.770 28.398  1.00 217.81 ? 398 ASN B ND2 1 
ATOM   6517 N N   . PRO B 1 399 ? 22.891  -42.154 28.095  1.00 132.28 ? 399 PRO B N   1 
ATOM   6518 C CA  . PRO B 1 399 ? 22.243  -41.336 29.124  1.00 142.85 ? 399 PRO B CA  1 
ATOM   6519 C C   . PRO B 1 399 ? 23.299  -40.817 30.097  1.00 139.32 ? 399 PRO B C   1 
ATOM   6520 O O   . PRO B 1 399 ? 23.323  -39.635 30.475  1.00 140.77 ? 399 PRO B O   1 
ATOM   6521 C CB  . PRO B 1 399 ? 21.325  -42.363 29.839  1.00 134.52 ? 399 PRO B CB  1 
ATOM   6522 C CG  . PRO B 1 399 ? 20.959  -43.344 28.764  1.00 131.53 ? 399 PRO B CG  1 
ATOM   6523 C CD  . PRO B 1 399 ? 22.159  -43.407 27.846  1.00 124.68 ? 399 PRO B CD  1 
ATOM   6524 N N   . ARG B 1 400 ? 24.066  -41.799 30.588  1.00 135.01 ? 400 ARG B N   1 
ATOM   6525 C CA  . ARG B 1 400 ? 25.019  -41.604 31.672  1.00 138.56 ? 400 ARG B CA  1 
ATOM   6526 C C   . ARG B 1 400 ? 26.017  -40.522 31.301  1.00 139.15 ? 400 ARG B C   1 
ATOM   6527 O O   . ARG B 1 400 ? 26.296  -39.613 32.099  1.00 174.33 ? 400 ARG B O   1 
ATOM   6528 C CB  . ARG B 1 400 ? 25.906  -42.837 31.908  1.00 143.39 ? 400 ARG B CB  1 
ATOM   6529 C CG  . ARG B 1 400 ? 27.021  -42.608 32.917  1.00 144.50 ? 400 ARG B CG  1 
ATOM   6530 C CD  . ARG B 1 400 ? 28.376  -43.231 32.568  1.00 155.79 ? 400 ARG B CD  1 
ATOM   6531 N NE  . ARG B 1 400 ? 28.543  -44.662 32.837  1.00 151.24 ? 400 ARG B NE  1 
ATOM   6532 C CZ  . ARG B 1 400 ? 28.343  -45.198 34.030  1.00 162.81 ? 400 ARG B CZ  1 
ATOM   6533 N NH1 . ARG B 1 400 ? 27.944  -44.447 35.046  1.00 166.43 ? 400 ARG B NH1 1 
ATOM   6534 N NH2 . ARG B 1 400 ? 28.532  -46.492 34.199  1.00 166.34 ? 400 ARG B NH2 1 
ATOM   6535 N N   . THR B 1 401 ? 26.542  -40.659 30.076  1.00 119.65 ? 401 THR B N   1 
ATOM   6536 C CA  . THR B 1 401 ? 27.534  -39.747 29.511  1.00 128.79 ? 401 THR B CA  1 
ATOM   6537 C C   . THR B 1 401 ? 26.993  -38.314 29.541  1.00 130.91 ? 401 THR B C   1 
ATOM   6538 O O   . THR B 1 401 ? 27.673  -37.371 29.979  1.00 127.76 ? 401 THR B O   1 
ATOM   6539 C CB  . THR B 1 401 ? 27.737  -40.160 28.049  1.00 121.73 ? 401 THR B CB  1 
ATOM   6540 O OG1 . THR B 1 401 ? 28.433  -41.392 28.076  1.00 131.39 ? 401 THR B OG1 1 
ATOM   6541 C CG2 . THR B 1 401 ? 28.567  -39.213 27.204  1.00 118.81 ? 401 THR B CG2 1 
ATOM   6542 N N   . ALA B 1 402 ? 25.754  -38.204 29.042  1.00 111.73 ? 402 ALA B N   1 
ATOM   6543 C CA  . ALA B 1 402 ? 25.079  -36.919 28.926  1.00 102.35 ? 402 ALA B CA  1 
ATOM   6544 C C   . ALA B 1 402 ? 24.949  -36.271 30.309  1.00 104.73 ? 402 ALA B C   1 
ATOM   6545 O O   . ALA B 1 402 ? 25.240  -35.066 30.479  1.00 110.42 ? 402 ALA B O   1 
ATOM   6546 C CB  . ALA B 1 402 ? 23.772  -37.057 28.188  1.00 95.91  ? 402 ALA B CB  1 
ATOM   6547 N N   . VAL B 1 403 ? 24.526  -37.108 31.271  1.00 109.81 ? 403 VAL B N   1 
ATOM   6548 C CA  . VAL B 1 403 ? 24.317  -36.642 32.638  1.00 115.39 ? 403 VAL B CA  1 
ATOM   6549 C C   . VAL B 1 403 ? 25.636  -36.113 33.210  1.00 136.16 ? 403 VAL B C   1 
ATOM   6550 O O   . VAL B 1 403 ? 25.663  -35.043 33.838  1.00 144.54 ? 403 VAL B O   1 
ATOM   6551 C CB  . VAL B 1 403 ? 23.527  -37.440 33.696  1.00 123.41 ? 403 VAL B CB  1 
ATOM   6552 C CG1 . VAL B 1 403 ? 22.974  -36.522 34.784  1.00 123.03 ? 403 VAL B CG1 1 
ATOM   6553 C CG2 . VAL B 1 403 ? 22.379  -38.233 33.096  1.00 128.64 ? 403 VAL B CG2 1 
ATOM   6554 N N   . GLU B 1 404 ? 26.705  -36.870 32.961  1.00 143.73 ? 404 GLU B N   1 
ATOM   6555 C CA  . GLU B 1 404 ? 28.037  -36.529 33.430  1.00 154.10 ? 404 GLU B CA  1 
ATOM   6556 C C   . GLU B 1 404 ? 28.462  -35.183 32.877  1.00 143.41 ? 404 GLU B C   1 
ATOM   6557 O O   . GLU B 1 404 ? 28.978  -34.339 33.611  1.00 144.01 ? 404 GLU B O   1 
ATOM   6558 C CB  . GLU B 1 404 ? 28.935  -37.706 33.072  1.00 188.01 ? 404 GLU B CB  1 
ATOM   6559 C CG  . GLU B 1 404 ? 28.751  -38.805 34.111  1.00 224.98 ? 404 GLU B CG  1 
ATOM   6560 C CD  . GLU B 1 404 ? 28.577  -38.090 35.442  1.00 225.34 ? 404 GLU B CD  1 
ATOM   6561 O OE1 . GLU B 1 404 ? 29.347  -37.115 35.654  1.00 255.40 ? 404 GLU B OE1 1 
ATOM   6562 O OE2 . GLU B 1 404 ? 27.677  -38.482 36.231  1.00 175.01 ? 404 GLU B OE2 1 
ATOM   6563 N N   . ARG B 1 405 ? 28.220  -35.012 31.575  1.00 130.26 ? 405 ARG B N   1 
ATOM   6564 C CA  . ARG B 1 405 ? 28.561  -33.781 30.859  1.00 127.16 ? 405 ARG B CA  1 
ATOM   6565 C C   . ARG B 1 405 ? 27.841  -32.600 31.506  1.00 114.50 ? 405 ARG B C   1 
ATOM   6566 O O   . ARG B 1 405 ? 28.439  -31.547 31.750  1.00 104.92 ? 405 ARG B O   1 
ATOM   6567 C CB  . ARG B 1 405 ? 28.058  -33.774 29.412  1.00 121.59 ? 405 ARG B CB  1 
ATOM   6568 C CG  . ARG B 1 405 ? 28.780  -34.615 28.380  1.00 131.74 ? 405 ARG B CG  1 
ATOM   6569 C CD  . ARG B 1 405 ? 29.655  -33.788 27.483  1.00 142.02 ? 405 ARG B CD  1 
ATOM   6570 N NE  . ARG B 1 405 ? 30.257  -34.624 26.440  1.00 159.64 ? 405 ARG B NE  1 
ATOM   6571 C CZ  . ARG B 1 405 ? 29.811  -34.730 25.186  1.00 144.04 ? 405 ARG B CZ  1 
ATOM   6572 N NH1 . ARG B 1 405 ? 28.693  -34.124 24.800  1.00 109.53 ? 405 ARG B NH1 1 
ATOM   6573 N NH2 . ARG B 1 405 ? 30.468  -35.481 24.321  1.00 152.46 ? 405 ARG B NH2 1 
ATOM   6574 N N   . LEU B 1 406 ? 26.554  -32.809 31.771  1.00 129.37 ? 406 LEU B N   1 
ATOM   6575 C CA  . LEU B 1 406 ? 25.745  -31.749 32.352  1.00 136.95 ? 406 LEU B CA  1 
ATOM   6576 C C   . LEU B 1 406 ? 26.268  -31.375 33.743  1.00 137.69 ? 406 LEU B C   1 
ATOM   6577 O O   . LEU B 1 406 ? 26.351  -30.193 34.064  1.00 147.17 ? 406 LEU B O   1 
ATOM   6578 C CB  . LEU B 1 406 ? 24.232  -31.756 32.100  1.00 141.54 ? 406 LEU B CB  1 
ATOM   6579 C CG  . LEU B 1 406 ? 23.860  -31.772 30.606  1.00 113.59 ? 406 LEU B CG  1 
ATOM   6580 C CD1 . LEU B 1 406 ? 22.408  -31.688 30.336  1.00 113.35 ? 406 LEU B CD1 1 
ATOM   6581 C CD2 . LEU B 1 406 ? 24.541  -30.733 29.766  1.00 103.72 ? 406 LEU B CD2 1 
ATOM   6582 N N   . ARG B 1 407 ? 26.671  -32.390 34.512  1.00 128.82 ? 407 ARG B N   1 
ATOM   6583 C CA  . ARG B 1 407 ? 27.183  -32.201 35.847  1.00 143.52 ? 407 ARG B CA  1 
ATOM   6584 C C   . ARG B 1 407 ? 28.487  -31.415 35.800  1.00 160.29 ? 407 ARG B C   1 
ATOM   6585 O O   . ARG B 1 407 ? 28.815  -30.775 36.793  1.00 186.16 ? 407 ARG B O   1 
ATOM   6586 C CB  . ARG B 1 407 ? 27.137  -33.605 36.447  1.00 130.71 ? 407 ARG B CB  1 
ATOM   6587 C CG  . ARG B 1 407 ? 28.387  -34.045 37.182  1.00 157.86 ? 407 ARG B CG  1 
ATOM   6588 C CD  . ARG B 1 407 ? 28.035  -34.929 38.356  1.00 177.44 ? 407 ARG B CD  1 
ATOM   6589 N NE  . ARG B 1 407 ? 26.637  -34.822 38.783  1.00 167.82 ? 407 ARG B NE  1 
ATOM   6590 C CZ  . ARG B 1 407 ? 25.738  -35.775 38.570  1.00 161.65 ? 407 ARG B CZ  1 
ATOM   6591 N NH1 . ARG B 1 407 ? 25.780  -36.562 37.512  1.00 152.96 ? 407 ARG B NH1 1 
ATOM   6592 N NH2 . ARG B 1 407 ? 24.743  -35.891 39.406  1.00 158.03 ? 407 ARG B NH2 1 
ATOM   6593 N N   . ALA B 1 408 ? 29.313  -31.698 34.794  1.00 156.79 ? 408 ALA B N   1 
ATOM   6594 C CA  . ALA B 1 408 ? 30.669  -31.185 34.713  1.00 148.89 ? 408 ALA B CA  1 
ATOM   6595 C C   . ALA B 1 408 ? 30.672  -29.674 34.591  1.00 155.73 ? 408 ALA B C   1 
ATOM   6596 O O   . ALA B 1 408 ? 31.396  -28.988 35.316  1.00 170.73 ? 408 ALA B O   1 
ATOM   6597 C CB  . ALA B 1 408 ? 31.421  -31.826 33.581  1.00 132.47 ? 408 ALA B CB  1 
ATOM   6598 N N   . GLU B 1 409 ? 29.973  -29.191 33.559  1.00 164.98 ? 409 GLU B N   1 
ATOM   6599 C CA  . GLU B 1 409 ? 29.972  -27.789 33.186  1.00 184.83 ? 409 GLU B CA  1 
ATOM   6600 C C   . GLU B 1 409 ? 28.936  -27.028 34.014  1.00 176.05 ? 409 GLU B C   1 
ATOM   6601 O O   . GLU B 1 409 ? 28.502  -25.944 33.638  1.00 184.59 ? 409 GLU B O   1 
ATOM   6602 C CB  . GLU B 1 409 ? 29.834  -27.724 31.665  1.00 198.04 ? 409 GLU B CB  1 
ATOM   6603 C CG  . GLU B 1 409 ? 30.809  -28.653 30.940  1.00 211.89 ? 409 GLU B CG  1 
ATOM   6604 C CD  . GLU B 1 409 ? 32.310  -28.424 31.068  1.00 219.48 ? 409 GLU B CD  1 
ATOM   6605 O OE1 . GLU B 1 409 ? 32.750  -27.304 31.416  1.00 236.83 ? 409 GLU B OE1 1 
ATOM   6606 O OE2 . GLU B 1 409 ? 33.052  -29.392 30.804  1.00 194.09 ? 409 GLU B OE2 1 
ATOM   6607 N N   . GLY B 1 410 ? 28.598  -27.598 35.176  1.00 168.09 ? 410 GLY B N   1 
ATOM   6608 C CA  . GLY B 1 410 ? 27.683  -27.026 36.150  1.00 156.73 ? 410 GLY B CA  1 
ATOM   6609 C C   . GLY B 1 410 ? 26.353  -26.676 35.503  1.00 172.92 ? 410 GLY B C   1 
ATOM   6610 O O   . GLY B 1 410 ? 25.756  -25.667 35.861  1.00 201.91 ? 410 GLY B O   1 
ATOM   6611 N N   . LEU B 1 411 ? 25.921  -27.513 34.550  1.00 171.29 ? 411 LEU B N   1 
ATOM   6612 C CA  . LEU B 1 411 ? 24.729  -27.265 33.747  1.00 167.04 ? 411 LEU B CA  1 
ATOM   6613 C C   . LEU B 1 411 ? 23.514  -27.967 34.359  1.00 179.76 ? 411 LEU B C   1 
ATOM   6614 O O   . LEU B 1 411 ? 22.385  -27.493 34.245  1.00 196.34 ? 411 LEU B O   1 
ATOM   6615 C CB  . LEU B 1 411 ? 24.961  -27.679 32.290  1.00 145.38 ? 411 LEU B CB  1 
ATOM   6616 C CG  . LEU B 1 411 ? 25.677  -26.672 31.391  1.00 119.57 ? 411 LEU B CG  1 
ATOM   6617 C CD1 . LEU B 1 411 ? 25.853  -27.183 29.973  1.00 117.34 ? 411 LEU B CD1 1 
ATOM   6618 C CD2 . LEU B 1 411 ? 24.802  -25.454 31.366  1.00 127.67 ? 411 LEU B CD2 1 
ATOM   6619 N N   . LEU B 1 412 ? 23.757  -29.095 35.033  1.00 154.07 ? 412 LEU B N   1 
ATOM   6620 C CA  . LEU B 1 412 ? 22.676  -29.866 35.616  1.00 144.76 ? 412 LEU B CA  1 
ATOM   6621 C C   . LEU B 1 412 ? 21.975  -29.054 36.709  1.00 150.36 ? 412 LEU B C   1 
ATOM   6622 O O   . LEU B 1 412 ? 22.591  -28.250 37.406  1.00 156.14 ? 412 LEU B O   1 
ATOM   6623 C CB  . LEU B 1 412 ? 23.290  -31.159 36.139  1.00 143.18 ? 412 LEU B CB  1 
ATOM   6624 C CG  . LEU B 1 412 ? 22.420  -32.411 35.997  1.00 142.62 ? 412 LEU B CG  1 
ATOM   6625 C CD1 . LEU B 1 412 ? 23.277  -33.620 36.298  1.00 152.49 ? 412 LEU B CD1 1 
ATOM   6626 C CD2 . LEU B 1 412 ? 21.179  -32.368 36.890  1.00 141.90 ? 412 LEU B CD2 1 
ATOM   6627 N N   . TYR B 1 413 ? 20.663  -29.259 36.840  1.00 141.75 ? 413 TYR B N   1 
ATOM   6628 C CA  . TYR B 1 413 ? 19.870  -28.526 37.807  1.00 152.10 ? 413 TYR B CA  1 
ATOM   6629 C C   . TYR B 1 413 ? 20.329  -28.895 39.209  1.00 164.92 ? 413 TYR B C   1 
ATOM   6630 O O   . TYR B 1 413 ? 20.444  -30.079 39.525  1.00 193.13 ? 413 TYR B O   1 
ATOM   6631 C CB  . TYR B 1 413 ? 18.383  -28.835 37.617  1.00 167.69 ? 413 TYR B CB  1 
ATOM   6632 C CG  . TYR B 1 413 ? 17.503  -28.218 38.697  1.00 173.72 ? 413 TYR B CG  1 
ATOM   6633 C CD1 . TYR B 1 413 ? 17.300  -28.880 39.905  1.00 159.45 ? 413 TYR B CD1 1 
ATOM   6634 C CD2 . TYR B 1 413 ? 16.891  -26.973 38.520  1.00 162.20 ? 413 TYR B CD2 1 
ATOM   6635 C CE1 . TYR B 1 413 ? 16.518  -28.327 40.903  1.00 163.18 ? 413 TYR B CE1 1 
ATOM   6636 C CE2 . TYR B 1 413 ? 16.106  -26.411 39.517  1.00 158.91 ? 413 TYR B CE2 1 
ATOM   6637 C CZ  . TYR B 1 413 ? 15.920  -27.092 40.711  1.00 169.83 ? 413 TYR B CZ  1 
ATOM   6638 O OH  . TYR B 1 413 ? 15.146  -26.573 41.713  1.00 190.83 ? 413 TYR B OH  1 
ATOM   6639 N N   . ARG B 1 414 ? 20.583  -27.866 40.027  1.00 153.01 ? 414 ARG B N   1 
ATOM   6640 C CA  . ARG B 1 414 ? 20.866  -28.064 41.439  1.00 170.28 ? 414 ARG B CA  1 
ATOM   6641 C C   . ARG B 1 414 ? 19.753  -27.433 42.271  1.00 154.66 ? 414 ARG B C   1 
ATOM   6642 O O   . ARG B 1 414 ? 19.222  -26.400 41.899  1.00 151.15 ? 414 ARG B O   1 
ATOM   6643 C CB  . ARG B 1 414 ? 22.266  -27.548 41.785  1.00 192.95 ? 414 ARG B CB  1 
ATOM   6644 C CG  . ARG B 1 414 ? 23.427  -28.278 41.125  1.00 200.29 ? 414 ARG B CG  1 
ATOM   6645 C CD  . ARG B 1 414 ? 24.720  -27.550 41.453  1.00 232.13 ? 414 ARG B CD  1 
ATOM   6646 N NE  . ARG B 1 414 ? 24.645  -26.145 41.031  1.00 252.89 ? 414 ARG B NE  1 
ATOM   6647 C CZ  . ARG B 1 414 ? 24.784  -25.673 39.792  1.00 241.58 ? 414 ARG B CZ  1 
ATOM   6648 N NH1 . ARG B 1 414 ? 25.137  -26.468 38.791  1.00 265.35 ? 414 ARG B NH1 1 
ATOM   6649 N NH2 . ARG B 1 414 ? 24.597  -24.384 39.576  1.00 222.59 ? 414 ARG B NH2 1 
ATOM   6650 N N   . HIS B 1 415 ? 19.408  -28.067 43.396  1.00 171.04 ? 415 HIS B N   1 
ATOM   6651 C CA  . HIS B 1 415 ? 18.238  -27.701 44.180  1.00 185.33 ? 415 HIS B CA  1 
ATOM   6652 C C   . HIS B 1 415 ? 18.569  -26.557 45.128  1.00 193.41 ? 415 HIS B C   1 
ATOM   6653 O O   . HIS B 1 415 ? 17.660  -25.879 45.604  1.00 194.79 ? 415 HIS B O   1 
ATOM   6654 C CB  . HIS B 1 415 ? 17.680  -28.906 44.946  1.00 218.07 ? 415 HIS B CB  1 
ATOM   6655 C CG  . HIS B 1 415 ? 17.191  -30.035 44.091  1.00 230.81 ? 415 HIS B CG  1 
ATOM   6656 N ND1 . HIS B 1 415 ? 15.873  -30.126 43.706  1.00 225.03 ? 415 HIS B ND1 1 
ATOM   6657 C CD2 . HIS B 1 415 ? 17.804  -31.111 43.559  1.00 210.92 ? 415 HIS B CD2 1 
ATOM   6658 C CE1 . HIS B 1 415 ? 15.706  -31.216 42.968  1.00 212.11 ? 415 HIS B CE1 1 
ATOM   6659 N NE2 . HIS B 1 415 ? 16.864  -31.828 42.866  1.00 193.95 ? 415 HIS B NE2 1 
ATOM   6660 N N   . ASP B 1 416 ? 19.870  -26.363 45.388  1.00 207.11 ? 416 ASP B N   1 
ATOM   6661 C CA  . ASP B 1 416 ? 20.360  -25.339 46.300  1.00 217.25 ? 416 ASP B CA  1 
ATOM   6662 C C   . ASP B 1 416 ? 20.304  -23.960 45.644  1.00 202.95 ? 416 ASP B C   1 
ATOM   6663 O O   . ASP B 1 416 ? 20.030  -22.966 46.324  1.00 213.30 ? 416 ASP B O   1 
ATOM   6664 C CB  . ASP B 1 416 ? 21.741  -25.695 46.829  1.00 195.90 ? 416 ASP B CB  1 
ATOM   6665 C CG  . ASP B 1 416 ? 22.749  -26.134 45.778  1.00 197.01 ? 416 ASP B CG  1 
ATOM   6666 O OD1 . ASP B 1 416 ? 22.400  -26.144 44.567  1.00 219.42 ? 416 ASP B OD1 1 
ATOM   6667 O OD2 . ASP B 1 416 ? 23.872  -26.469 46.179  1.00 198.91 ? 416 ASP B OD2 1 
ATOM   6668 N N   . THR B 1 417 ? 20.569  -23.927 44.328  1.00 176.36 ? 417 THR B N   1 
ATOM   6669 C CA  . THR B 1 417 ? 20.569  -22.704 43.541  1.00 179.74 ? 417 THR B CA  1 
ATOM   6670 C C   . THR B 1 417 ? 19.161  -22.453 43.011  1.00 184.96 ? 417 THR B C   1 
ATOM   6671 O O   . THR B 1 417 ? 18.682  -21.322 43.031  1.00 219.67 ? 417 THR B O   1 
ATOM   6672 C CB  . THR B 1 417 ? 21.612  -22.747 42.420  1.00 167.91 ? 417 THR B CB  1 
ATOM   6673 O OG1 . THR B 1 417 ? 21.341  -23.899 41.632  1.00 162.59 ? 417 THR B OG1 1 
ATOM   6674 C CG2 . THR B 1 417 ? 23.039  -22.852 42.929  1.00 161.49 ? 417 THR B CG2 1 
ATOM   6675 N N   . GLY B 1 418 ? 18.509  -23.520 42.541  1.00 178.29 ? 418 GLY B N   1 
ATOM   6676 C CA  . GLY B 1 418 ? 17.122  -23.463 42.113  1.00 164.17 ? 418 GLY B CA  1 
ATOM   6677 C C   . GLY B 1 418 ? 17.013  -23.248 40.608  1.00 159.82 ? 418 GLY B C   1 
ATOM   6678 O O   . GLY B 1 418 ? 15.969  -22.817 40.135  1.00 163.74 ? 418 GLY B O   1 
ATOM   6679 N N   . GLU B 1 419 ? 18.091  -23.565 39.879  1.00 159.17 ? 419 GLU B N   1 
ATOM   6680 C CA  . GLU B 1 419 ? 18.153  -23.351 38.447  1.00 165.25 ? 419 GLU B CA  1 
ATOM   6681 C C   . GLU B 1 419 ? 19.130  -24.325 37.794  1.00 174.70 ? 419 GLU B C   1 
ATOM   6682 O O   . GLU B 1 419 ? 20.218  -24.570 38.312  1.00 205.43 ? 419 GLU B O   1 
ATOM   6683 C CB  . GLU B 1 419 ? 18.553  -21.906 38.159  1.00 181.83 ? 419 GLU B CB  1 
ATOM   6684 C CG  . GLU B 1 419 ? 19.731  -21.415 38.991  1.00 188.20 ? 419 GLU B CG  1 
ATOM   6685 C CD  . GLU B 1 419 ? 20.491  -20.319 38.269  1.00 201.51 ? 419 GLU B CD  1 
ATOM   6686 O OE1 . GLU B 1 419 ? 19.897  -19.267 37.956  1.00 221.16 ? 419 GLU B OE1 1 
ATOM   6687 O OE2 . GLU B 1 419 ? 21.685  -20.534 37.990  1.00 178.95 ? 419 GLU B OE2 1 
ATOM   6688 N N   . GLY B 1 420 ? 18.712  -24.871 36.647  1.00 164.44 ? 420 GLY B N   1 
ATOM   6689 C CA  . GLY B 1 420 ? 19.547  -25.696 35.795  1.00 165.70 ? 420 GLY B CA  1 
ATOM   6690 C C   . GLY B 1 420 ? 18.731  -26.524 34.801  1.00 144.86 ? 420 GLY B C   1 
ATOM   6691 O O   . GLY B 1 420 ? 17.571  -26.240 34.474  1.00 127.31 ? 420 GLY B O   1 
ATOM   6692 N N   . VAL B 1 421 ? 19.357  -27.632 34.367  1.00 134.08 ? 421 VAL B N   1 
ATOM   6693 C CA  . VAL B 1 421 ? 18.912  -28.418 33.225  1.00 130.10 ? 421 VAL B CA  1 
ATOM   6694 C C   . VAL B 1 421 ? 18.690  -29.877 33.648  1.00 147.06 ? 421 VAL B C   1 
ATOM   6695 O O   . VAL B 1 421 ? 19.518  -30.516 34.284  1.00 155.49 ? 421 VAL B O   1 
ATOM   6696 C CB  . VAL B 1 421 ? 19.792  -28.356 31.952  1.00 122.46 ? 421 VAL B CB  1 
ATOM   6697 C CG1 . VAL B 1 421 ? 19.118  -29.032 30.750  1.00 123.74 ? 421 VAL B CG1 1 
ATOM   6698 C CG2 . VAL B 1 421 ? 20.219  -26.937 31.573  1.00 119.81 ? 421 VAL B CG2 1 
ATOM   6699 N N   . ALA B 1 422 ? 17.503  -30.369 33.273  1.00 140.20 ? 422 ALA B N   1 
ATOM   6700 C CA  . ALA B 1 422 ? 17.105  -31.753 33.436  1.00 134.17 ? 422 ALA B CA  1 
ATOM   6701 C C   . ALA B 1 422 ? 16.616  -32.315 32.100  1.00 131.80 ? 422 ALA B C   1 
ATOM   6702 O O   . ALA B 1 422 ? 15.838  -31.705 31.349  1.00 144.21 ? 422 ALA B O   1 
ATOM   6703 C CB  . ALA B 1 422 ? 16.088  -31.886 34.545  1.00 129.98 ? 422 ALA B CB  1 
ATOM   6704 N N   . LEU B 1 423 ? 17.106  -33.523 31.813  1.00 120.58 ? 423 LEU B N   1 
ATOM   6705 C CA  . LEU B 1 423 ? 16.784  -34.264 30.601  1.00 122.28 ? 423 LEU B CA  1 
ATOM   6706 C C   . LEU B 1 423 ? 15.641  -35.271 30.779  1.00 117.52 ? 423 LEU B C   1 
ATOM   6707 O O   . LEU B 1 423 ? 15.319  -35.749 31.862  1.00 136.21 ? 423 LEU B O   1 
ATOM   6708 C CB  . LEU B 1 423 ? 17.987  -34.923 29.938  1.00 133.02 ? 423 LEU B CB  1 
ATOM   6709 C CG  . LEU B 1 423 ? 19.117  -33.977 29.547  1.00 129.33 ? 423 LEU B CG  1 
ATOM   6710 C CD1 . LEU B 1 423 ? 19.747  -33.704 30.882  1.00 145.90 ? 423 LEU B CD1 1 
ATOM   6711 C CD2 . LEU B 1 423 ? 20.082  -34.700 28.636  1.00 139.25 ? 423 LEU B CD2 1 
ATOM   6712 N N   . HIS B 1 424 ? 15.019  -35.567 29.643  1.00 104.38 ? 424 HIS B N   1 
ATOM   6713 C CA  . HIS B 1 424 ? 13.986  -36.584 29.524  1.00 115.47 ? 424 HIS B CA  1 
ATOM   6714 C C   . HIS B 1 424 ? 14.289  -37.505 28.347  1.00 112.92 ? 424 HIS B C   1 
ATOM   6715 O O   . HIS B 1 424 ? 14.861  -37.131 27.300  1.00 99.07  ? 424 HIS B O   1 
ATOM   6716 C CB  . HIS B 1 424 ? 12.584  -35.971 29.435  1.00 115.63 ? 424 HIS B CB  1 
ATOM   6717 C CG  . HIS B 1 424 ? 12.422  -34.785 30.305  1.00 129.48 ? 424 HIS B CG  1 
ATOM   6718 N ND1 . HIS B 1 424 ? 11.860  -33.624 29.822  1.00 149.63 ? 424 HIS B ND1 1 
ATOM   6719 C CD2 . HIS B 1 424 ? 12.797  -34.529 31.561  1.00 135.26 ? 424 HIS B CD2 1 
ATOM   6720 C CE1 . HIS B 1 424 ? 11.863  -32.710 30.784  1.00 163.09 ? 424 HIS B CE1 1 
ATOM   6721 N NE2 . HIS B 1 424 ? 12.435  -33.238 31.848  1.00 158.94 ? 424 HIS B NE2 1 
ATOM   6722 N N   . VAL B 1 425 ? 13.778  -38.731 28.483  1.00 114.58 ? 425 VAL B N   1 
ATOM   6723 C CA  . VAL B 1 425 ? 13.757  -39.676 27.365  1.00 119.46 ? 425 VAL B CA  1 
ATOM   6724 C C   . VAL B 1 425 ? 15.215  -39.949 27.001  1.00 118.36 ? 425 VAL B C   1 
ATOM   6725 O O   . VAL B 1 425 ? 15.594  -39.850 25.835  1.00 107.34 ? 425 VAL B O   1 
ATOM   6726 C CB  . VAL B 1 425 ? 12.995  -39.109 26.136  1.00 101.59 ? 425 VAL B CB  1 
ATOM   6727 C CG1 . VAL B 1 425 ? 12.675  -40.190 25.087  1.00 100.23 ? 425 VAL B CG1 1 
ATOM   6728 C CG2 . VAL B 1 425 ? 11.721  -38.369 26.527  1.00 89.86  ? 425 VAL B CG2 1 
ATOM   6729 N N   . LEU B 1 426 ? 16.031  -40.260 28.016  1.00 115.70 ? 426 LEU B N   1 
ATOM   6730 C CA  . LEU B 1 426 ? 17.467  -40.365 27.832  1.00 108.40 ? 426 LEU B CA  1 
ATOM   6731 C C   . LEU B 1 426 ? 17.783  -41.563 26.940  1.00 107.43 ? 426 LEU B C   1 
ATOM   6732 O O   . LEU B 1 426 ? 18.821  -41.595 26.282  1.00 105.77 ? 426 LEU B O   1 
ATOM   6733 C CB  . LEU B 1 426 ? 18.100  -40.462 29.219  1.00 102.95 ? 426 LEU B CB  1 
ATOM   6734 C CG  . LEU B 1 426 ? 18.117  -39.151 30.010  1.00 104.48 ? 426 LEU B CG  1 
ATOM   6735 C CD1 . LEU B 1 426 ? 18.163  -39.326 31.527  1.00 100.42 ? 426 LEU B CD1 1 
ATOM   6736 C CD2 . LEU B 1 426 ? 19.332  -38.381 29.524  1.00 115.49 ? 426 LEU B CD2 1 
ATOM   6737 N N   . GLY B 1 427 ? 16.858  -42.532 26.916  1.00 115.04 ? 427 GLY B N   1 
ATOM   6738 C CA  . GLY B 1 427 ? 17.080  -43.800 26.243  1.00 134.14 ? 427 GLY B CA  1 
ATOM   6739 C C   . GLY B 1 427 ? 17.231  -43.628 24.733  1.00 128.58 ? 427 GLY B C   1 
ATOM   6740 O O   . GLY B 1 427 ? 17.864  -44.450 24.055  1.00 129.04 ? 427 GLY B O   1 
ATOM   6741 N N   . ALA B 1 428 ? 16.644  -42.540 24.226  1.00 105.99 ? 428 ALA B N   1 
ATOM   6742 C CA  . ALA B 1 428 ? 16.634  -42.290 22.799  1.00 111.24 ? 428 ALA B CA  1 
ATOM   6743 C C   . ALA B 1 428 ? 18.010  -41.806 22.337  1.00 124.83 ? 428 ALA B C   1 
ATOM   6744 O O   . ALA B 1 428 ? 18.329  -41.878 21.150  1.00 131.08 ? 428 ALA B O   1 
ATOM   6745 C CB  . ALA B 1 428 ? 15.558  -41.290 22.499  1.00 106.27 ? 428 ALA B CB  1 
ATOM   6746 N N   . LEU B 1 429 ? 18.813  -41.333 23.301  1.00 135.61 ? 429 LEU B N   1 
ATOM   6747 C CA  . LEU B 1 429 ? 20.135  -40.775 23.053  1.00 139.48 ? 429 LEU B CA  1 
ATOM   6748 C C   . LEU B 1 429 ? 20.958  -41.682 22.146  1.00 140.24 ? 429 LEU B C   1 
ATOM   6749 O O   . LEU B 1 429 ? 21.269  -41.299 21.011  1.00 115.59 ? 429 LEU B O   1 
ATOM   6750 C CB  . LEU B 1 429 ? 20.880  -40.462 24.351  1.00 137.89 ? 429 LEU B CB  1 
ATOM   6751 C CG  . LEU B 1 429 ? 20.549  -39.085 24.936  1.00 132.27 ? 429 LEU B CG  1 
ATOM   6752 C CD1 . LEU B 1 429 ? 21.311  -38.749 26.195  1.00 147.46 ? 429 LEU B CD1 1 
ATOM   6753 C CD2 . LEU B 1 429 ? 20.783  -38.027 23.878  1.00 110.91 ? 429 LEU B CD2 1 
ATOM   6754 N N   . ASN B 1 430 ? 21.271  -42.883 22.650  1.00 145.45 ? 430 ASN B N   1 
ATOM   6755 C CA  . ASN B 1 430 ? 22.237  -43.739 21.980  1.00 160.81 ? 430 ASN B CA  1 
ATOM   6756 C C   . ASN B 1 430 ? 21.689  -44.202 20.637  1.00 146.18 ? 430 ASN B C   1 
ATOM   6757 O O   . ASN B 1 430 ? 22.445  -44.392 19.678  1.00 125.60 ? 430 ASN B O   1 
ATOM   6758 C CB  . ASN B 1 430 ? 22.638  -44.923 22.850  1.00 193.68 ? 430 ASN B CB  1 
ATOM   6759 C CG  . ASN B 1 430 ? 23.981  -45.481 22.445  1.00 218.05 ? 430 ASN B CG  1 
ATOM   6760 O OD1 . ASN B 1 430 ? 24.142  -45.988 21.329  1.00 236.55 ? 430 ASN B OD1 1 
ATOM   6761 N ND2 . ASN B 1 430 ? 24.955  -45.406 23.341  1.00 222.11 ? 430 ASN B ND2 1 
ATOM   6762 N N   . ALA B 1 431 ? 20.358  -44.333 20.599  1.00 164.60 ? 431 ALA B N   1 
ATOM   6763 C CA  . ALA B 1 431 ? 19.658  -45.132 19.611  1.00 174.82 ? 431 ALA B CA  1 
ATOM   6764 C C   . ALA B 1 431 ? 19.189  -44.265 18.443  1.00 173.98 ? 431 ALA B C   1 
ATOM   6765 O O   . ALA B 1 431 ? 19.358  -44.644 17.285  1.00 165.34 ? 431 ALA B O   1 
ATOM   6766 C CB  . ALA B 1 431 ? 18.507  -45.872 20.283  1.00 161.48 ? 431 ALA B CB  1 
ATOM   6767 N N   . CYS B 1 432 ? 18.567  -43.119 18.746  1.00 168.34 ? 432 CYS B N   1 
ATOM   6768 C CA  . CYS B 1 432 ? 17.996  -42.293 17.696  1.00 145.49 ? 432 CYS B CA  1 
ATOM   6769 C C   . CYS B 1 432 ? 18.675  -40.932 17.673  1.00 126.53 ? 432 CYS B C   1 
ATOM   6770 O O   . CYS B 1 432 ? 18.429  -40.135 16.777  1.00 100.13 ? 432 CYS B O   1 
ATOM   6771 C CB  . CYS B 1 432 ? 16.489  -42.161 17.865  1.00 158.02 ? 432 CYS B CB  1 
ATOM   6772 S SG  . CYS B 1 432 ? 15.621  -43.732 17.655  1.00 208.67 ? 432 CYS B SG  1 
ATOM   6773 N N   . GLY B 1 433 ? 19.560  -40.691 18.641  1.00 132.25 ? 433 GLY B N   1 
ATOM   6774 C CA  . GLY B 1 433 ? 20.131  -39.367 18.800  1.00 146.98 ? 433 GLY B CA  1 
ATOM   6775 C C   . GLY B 1 433 ? 19.032  -38.330 19.042  1.00 142.48 ? 433 GLY B C   1 
ATOM   6776 O O   . GLY B 1 433 ? 18.962  -37.300 18.359  1.00 156.24 ? 433 GLY B O   1 
ATOM   6777 N N   . PHE B 1 434 ? 18.188  -38.633 20.033  1.00 124.49 ? 434 PHE B N   1 
ATOM   6778 C CA  . PHE B 1 434 ? 17.106  -37.762 20.451  1.00 115.70 ? 434 PHE B CA  1 
ATOM   6779 C C   . PHE B 1 434 ? 17.123  -37.535 21.964  1.00 115.06 ? 434 PHE B C   1 
ATOM   6780 O O   . PHE B 1 434 ? 17.382  -38.433 22.782  1.00 159.30 ? 434 PHE B O   1 
ATOM   6781 C CB  . PHE B 1 434 ? 15.753  -38.330 20.022  1.00 123.37 ? 434 PHE B CB  1 
ATOM   6782 C CG  . PHE B 1 434 ? 14.569  -37.537 20.561  1.00 120.78 ? 434 PHE B CG  1 
ATOM   6783 C CD1 . PHE B 1 434 ? 14.055  -36.467 19.850  1.00 121.74 ? 434 PHE B CD1 1 
ATOM   6784 C CD2 . PHE B 1 434 ? 13.983  -37.852 21.785  1.00 123.74 ? 434 PHE B CD2 1 
ATOM   6785 C CE1 . PHE B 1 434 ? 12.985  -35.748 20.365  1.00 124.29 ? 434 PHE B CE1 1 
ATOM   6786 C CE2 . PHE B 1 434 ? 12.913  -37.125 22.289  1.00 117.42 ? 434 PHE B CE2 1 
ATOM   6787 C CZ  . PHE B 1 434 ? 12.418  -36.074 21.578  1.00 111.60 ? 434 PHE B CZ  1 
ATOM   6788 N N   . VAL B 1 435 ? 16.722  -36.340 22.372  1.00 95.70  ? 435 VAL B N   1 
ATOM   6789 C CA  . VAL B 1 435 ? 16.546  -36.056 23.789  1.00 105.21 ? 435 VAL B CA  1 
ATOM   6790 C C   . VAL B 1 435 ? 15.649  -34.839 23.953  1.00 114.25 ? 435 VAL B C   1 
ATOM   6791 O O   . VAL B 1 435 ? 15.645  -33.891 23.163  1.00 135.38 ? 435 VAL B O   1 
ATOM   6792 C CB  . VAL B 1 435 ? 17.871  -35.946 24.574  1.00 110.45 ? 435 VAL B CB  1 
ATOM   6793 C CG1 . VAL B 1 435 ? 18.744  -34.824 24.021  1.00 124.46 ? 435 VAL B CG1 1 
ATOM   6794 C CG2 . VAL B 1 435 ? 17.677  -35.809 26.088  1.00 106.36 ? 435 VAL B CG2 1 
ATOM   6795 N N   . GLU B 1 436 ? 14.855  -34.871 25.026  1.00 112.98 ? 436 GLU B N   1 
ATOM   6796 C CA  . GLU B 1 436 ? 14.218  -33.696 25.613  1.00 110.45 ? 436 GLU B CA  1 
ATOM   6797 C C   . GLU B 1 436 ? 15.126  -33.079 26.681  1.00 116.50 ? 436 GLU B C   1 
ATOM   6798 O O   . GLU B 1 436 ? 15.733  -33.762 27.511  1.00 110.56 ? 436 GLU B O   1 
ATOM   6799 C CB  . GLU B 1 436 ? 12.846  -33.997 26.226  1.00 111.68 ? 436 GLU B CB  1 
ATOM   6800 C CG  . GLU B 1 436 ? 11.892  -34.747 25.298  1.00 124.71 ? 436 GLU B CG  1 
ATOM   6801 C CD  . GLU B 1 436 ? 10.438  -34.663 25.737  1.00 146.65 ? 436 GLU B CD  1 
ATOM   6802 O OE1 . GLU B 1 436 ? 10.200  -34.742 26.956  1.00 156.62 ? 436 GLU B OE1 1 
ATOM   6803 O OE2 . GLU B 1 436 ? 9.533   -34.541 24.876  1.00 151.87 ? 436 GLU B OE2 1 
ATOM   6804 N N   . LEU B 1 437 ? 15.190  -31.745 26.652  1.00 131.08 ? 437 LEU B N   1 
ATOM   6805 C CA  . LEU B 1 437 ? 15.839  -30.967 27.702  1.00 153.06 ? 437 LEU B CA  1 
ATOM   6806 C C   . LEU B 1 437 ? 14.922  -29.847 28.187  1.00 136.88 ? 437 LEU B C   1 
ATOM   6807 O O   . LEU B 1 437 ? 14.246  -29.143 27.424  1.00 115.41 ? 437 LEU B O   1 
ATOM   6808 C CB  . LEU B 1 437 ? 17.290  -30.531 27.483  1.00 150.96 ? 437 LEU B CB  1 
ATOM   6809 C CG  . LEU B 1 437 ? 17.524  -29.325 26.565  1.00 137.43 ? 437 LEU B CG  1 
ATOM   6810 C CD1 . LEU B 1 437 ? 17.466  -27.988 27.313  1.00 153.21 ? 437 LEU B CD1 1 
ATOM   6811 C CD2 . LEU B 1 437 ? 18.837  -29.461 25.801  1.00 124.57 ? 437 LEU B CD2 1 
ATOM   6812 N N   . THR B 1 438 ? 14.957  -29.667 29.507  1.00 135.92 ? 438 THR B N   1 
ATOM   6813 C CA  . THR B 1 438 ? 14.231  -28.626 30.218  1.00 132.13 ? 438 THR B CA  1 
ATOM   6814 C C   . THR B 1 438 ? 15.189  -27.870 31.136  1.00 147.60 ? 438 THR B C   1 
ATOM   6815 O O   . THR B 1 438 ? 15.955  -28.445 31.910  1.00 140.79 ? 438 THR B O   1 
ATOM   6816 C CB  . THR B 1 438 ? 13.056  -29.193 31.009  1.00 123.87 ? 438 THR B CB  1 
ATOM   6817 O OG1 . THR B 1 438 ? 12.151  -29.664 30.013  1.00 120.52 ? 438 THR B OG1 1 
ATOM   6818 C CG2 . THR B 1 438 ? 12.438  -28.133 31.911  1.00 116.88 ? 438 THR B CG2 1 
ATOM   6819 N N   . ALA B 1 439 ? 15.071  -26.541 31.045  1.00 148.93 ? 439 ALA B N   1 
ATOM   6820 C CA  . ALA B 1 439 ? 15.954  -25.593 31.710  1.00 154.88 ? 439 ALA B CA  1 
ATOM   6821 C C   . ALA B 1 439 ? 15.144  -24.608 32.554  1.00 136.27 ? 439 ALA B C   1 
ATOM   6822 O O   . ALA B 1 439 ? 14.167  -24.021 32.083  1.00 139.47 ? 439 ALA B O   1 
ATOM   6823 C CB  . ALA B 1 439 ? 16.827  -24.881 30.674  1.00 152.36 ? 439 ALA B CB  1 
ATOM   6824 N N   . LEU B 1 440 ? 15.568  -24.489 33.820  1.00 138.05 ? 440 LEU B N   1 
ATOM   6825 C CA  . LEU B 1 440 ? 14.880  -23.691 34.824  1.00 156.82 ? 440 LEU B CA  1 
ATOM   6826 C C   . LEU B 1 440 ? 15.812  -22.642 35.438  1.00 188.46 ? 440 LEU B C   1 
ATOM   6827 O O   . LEU B 1 440 ? 16.881  -22.983 35.907  1.00 201.47 ? 440 LEU B O   1 
ATOM   6828 C CB  . LEU B 1 440 ? 14.360  -24.602 35.930  1.00 140.72 ? 440 LEU B CB  1 
ATOM   6829 C CG  . LEU B 1 440 ? 13.218  -25.539 35.545  1.00 139.62 ? 440 LEU B CG  1 
ATOM   6830 C CD1 . LEU B 1 440 ? 13.755  -26.816 34.907  1.00 148.42 ? 440 LEU B CD1 1 
ATOM   6831 C CD2 . LEU B 1 440 ? 12.364  -25.811 36.757  1.00 145.00 ? 440 LEU B CD2 1 
ATOM   6832 N N   . ALA B 1 441 ? 15.378  -21.382 35.373  1.00 194.38 ? 441 ALA B N   1 
ATOM   6833 C CA  . ALA B 1 441 ? 16.100  -20.275 35.974  1.00 181.15 ? 441 ALA B CA  1 
ATOM   6834 C C   . ALA B 1 441 ? 15.202  -19.252 36.653  1.00 182.77 ? 441 ALA B C   1 
ATOM   6835 O O   . ALA B 1 441 ? 13.959  -19.221 36.574  1.00 202.74 ? 441 ALA B O   1 
ATOM   6836 C CB  . ALA B 1 441 ? 17.042  -19.633 34.984  1.00 181.18 ? 441 ALA B CB  1 
ATOM   6837 N N   . ARG B 1 442 ? 15.906  -18.309 37.286  1.00 169.13 ? 442 ARG B N   1 
ATOM   6838 C CA  . ARG B 1 442 ? 15.311  -17.228 38.052  1.00 189.40 ? 442 ARG B CA  1 
ATOM   6839 C C   . ARG B 1 442 ? 14.651  -16.211 37.116  1.00 181.78 ? 442 ARG B C   1 
ATOM   6840 O O   . ARG B 1 442 ? 13.676  -15.566 37.495  1.00 173.14 ? 442 ARG B O   1 
ATOM   6841 C CB  . ARG B 1 442 ? 16.396  -16.675 38.985  1.00 209.77 ? 442 ARG B CB  1 
ATOM   6842 C CG  . ARG B 1 442 ? 16.857  -17.618 40.091  1.00 209.58 ? 442 ARG B CG  1 
ATOM   6843 C CD  . ARG B 1 442 ? 16.049  -17.577 41.380  1.00 241.63 ? 442 ARG B CD  1 
ATOM   6844 N NE  . ARG B 1 442 ? 14.638  -17.973 41.274  1.00 268.07 ? 442 ARG B NE  1 
ATOM   6845 C CZ  . ARG B 1 442 ? 14.041  -18.876 42.049  1.00 264.42 ? 442 ARG B CZ  1 
ATOM   6846 N NH1 . ARG B 1 442 ? 14.731  -19.518 42.976  1.00 275.86 ? 442 ARG B NH1 1 
ATOM   6847 N NH2 . ARG B 1 442 ? 12.748  -19.120 41.918  1.00 245.84 ? 442 ARG B NH2 1 
ATOM   6848 N N   . SER B 1 443 ? 15.179  -16.089 35.889  1.00 171.76 ? 443 SER B N   1 
ATOM   6849 C CA  . SER B 1 443 ? 14.608  -15.247 34.846  1.00 171.77 ? 443 SER B CA  1 
ATOM   6850 C C   . SER B 1 443 ? 14.470  -16.064 33.567  1.00 162.70 ? 443 SER B C   1 
ATOM   6851 O O   . SER B 1 443 ? 15.259  -16.987 33.386  1.00 197.08 ? 443 SER B O   1 
ATOM   6852 C CB  . SER B 1 443 ? 15.476  -14.043 34.606  1.00 194.45 ? 443 SER B CB  1 
ATOM   6853 O OG  . SER B 1 443 ? 16.691  -14.399 33.960  1.00 199.77 ? 443 SER B OG  1 
ATOM   6854 N N   . PRO B 1 444 ? 13.510  -15.774 32.648  1.00 148.45 ? 444 PRO B N   1 
ATOM   6855 C CA  . PRO B 1 444 ? 13.301  -16.600 31.457  1.00 170.22 ? 444 PRO B CA  1 
ATOM   6856 C C   . PRO B 1 444 ? 14.492  -16.537 30.522  1.00 194.16 ? 444 PRO B C   1 
ATOM   6857 O O   . PRO B 1 444 ? 14.853  -17.570 29.965  1.00 207.59 ? 444 PRO B O   1 
ATOM   6858 C CB  . PRO B 1 444 ? 11.996  -16.204 30.769  1.00 143.85 ? 444 PRO B CB  1 
ATOM   6859 C CG  . PRO B 1 444 ? 11.525  -15.053 31.630  1.00 163.82 ? 444 PRO B CG  1 
ATOM   6860 C CD  . PRO B 1 444 ? 12.610  -14.621 32.647  1.00 152.32 ? 444 PRO B CD  1 
ATOM   6861 N N   . GLU B 1 445 ? 15.118  -15.358 30.430  1.00 206.96 ? 445 GLU B N   1 
ATOM   6862 C CA  . GLU B 1 445 ? 16.319  -15.161 29.631  1.00 236.32 ? 445 GLU B CA  1 
ATOM   6863 C C   . GLU B 1 445 ? 17.421  -16.115 30.102  1.00 228.07 ? 445 GLU B C   1 
ATOM   6864 O O   . GLU B 1 445 ? 18.082  -16.779 29.286  1.00 232.75 ? 445 GLU B O   1 
ATOM   6865 C CB  . GLU B 1 445 ? 16.685  -13.683 29.815  1.00 275.74 ? 445 GLU B CB  1 
ATOM   6866 C CG  . GLU B 1 445 ? 15.512  -12.737 29.557  1.00 324.10 ? 445 GLU B CG  1 
ATOM   6867 C CD  . GLU B 1 445 ? 15.396  -11.492 30.425  1.00 316.30 ? 445 GLU B CD  1 
ATOM   6868 O OE1 . GLU B 1 445 ? 15.386  -11.670 31.654  1.00 317.80 ? 445 GLU B OE1 1 
ATOM   6869 O OE2 . GLU B 1 445 ? 15.270  -10.354 29.914  1.00 295.94 ? 445 GLU B OE2 1 
ATOM   6870 N N   . ALA B 1 446 ? 17.582  -16.155 31.432  1.00 216.42 ? 446 ALA B N   1 
ATOM   6871 C CA  . ALA B 1 446 ? 18.597  -16.994 32.062  1.00 191.99 ? 446 ALA B CA  1 
ATOM   6872 C C   . ALA B 1 446 ? 18.363  -18.461 31.702  1.00 178.56 ? 446 ALA B C   1 
ATOM   6873 O O   . ALA B 1 446 ? 19.302  -19.183 31.349  1.00 178.89 ? 446 ALA B O   1 
ATOM   6874 C CB  . ALA B 1 446 ? 18.641  -16.774 33.561  1.00 178.90 ? 446 ALA B CB  1 
ATOM   6875 N N   . ALA B 1 447 ? 17.097  -18.862 31.797  1.00 163.48 ? 447 ALA B N   1 
ATOM   6876 C CA  . ALA B 1 447 ? 16.665  -20.222 31.493  1.00 154.95 ? 447 ALA B CA  1 
ATOM   6877 C C   . ALA B 1 447 ? 17.042  -20.583 30.060  1.00 149.57 ? 447 ALA B C   1 
ATOM   6878 O O   . ALA B 1 447 ? 17.590  -21.665 29.789  1.00 147.76 ? 447 ALA B O   1 
ATOM   6879 C CB  . ALA B 1 447 ? 15.167  -20.341 31.695  1.00 146.17 ? 447 ALA B CB  1 
ATOM   6880 N N   . ASP B 1 448 ? 16.730  -19.649 29.164  1.00 150.10 ? 448 ASP B N   1 
ATOM   6881 C CA  . ASP B 1 448 ? 16.994  -19.796 27.735  1.00 176.95 ? 448 ASP B CA  1 
ATOM   6882 C C   . ASP B 1 448 ? 18.487  -20.018 27.505  1.00 162.34 ? 448 ASP B C   1 
ATOM   6883 O O   . ASP B 1 448 ? 18.890  -20.906 26.747  1.00 152.36 ? 448 ASP B O   1 
ATOM   6884 C CB  . ASP B 1 448 ? 16.476  -18.590 26.961  1.00 223.79 ? 448 ASP B CB  1 
ATOM   6885 C CG  . ASP B 1 448 ? 14.963  -18.497 26.770  1.00 224.97 ? 448 ASP B CG  1 
ATOM   6886 O OD1 . ASP B 1 448 ? 14.224  -18.142 27.725  1.00 194.66 ? 448 ASP B OD1 1 
ATOM   6887 O OD2 . ASP B 1 448 ? 14.526  -18.769 25.654  1.00 226.33 ? 448 ASP B OD2 1 
ATOM   6888 N N   . GLY B 1 449 ? 19.280  -19.185 28.176  1.00 159.51 ? 449 GLY B N   1 
ATOM   6889 C CA  . GLY B 1 449 ? 20.736  -19.229 28.091  1.00 174.46 ? 449 GLY B CA  1 
ATOM   6890 C C   . GLY B 1 449 ? 21.245  -20.598 28.513  1.00 171.71 ? 449 GLY B C   1 
ATOM   6891 O O   . GLY B 1 449 ? 22.092  -21.190 27.842  1.00 172.55 ? 449 GLY B O   1 
ATOM   6892 N N   . TYR B 1 450 ? 20.702  -21.073 29.634  1.00 163.68 ? 450 TYR B N   1 
ATOM   6893 C CA  . TYR B 1 450 ? 21.050  -22.370 30.207  1.00 142.95 ? 450 TYR B CA  1 
ATOM   6894 C C   . TYR B 1 450 ? 20.792  -23.475 29.186  1.00 138.05 ? 450 TYR B C   1 
ATOM   6895 O O   . TYR B 1 450 ? 21.640  -24.357 28.963  1.00 148.13 ? 450 TYR B O   1 
ATOM   6896 C CB  . TYR B 1 450 ? 20.163  -22.664 31.419  1.00 135.86 ? 450 TYR B CB  1 
ATOM   6897 C CG  . TYR B 1 450 ? 20.918  -22.453 32.714  1.00 153.33 ? 450 TYR B CG  1 
ATOM   6898 C CD1 . TYR B 1 450 ? 22.285  -22.685 32.761  1.00 160.35 ? 450 TYR B CD1 1 
ATOM   6899 C CD2 . TYR B 1 450 ? 20.280  -22.023 33.870  1.00 163.56 ? 450 TYR B CD2 1 
ATOM   6900 C CE1 . TYR B 1 450 ? 23.001  -22.502 33.929  1.00 181.51 ? 450 TYR B CE1 1 
ATOM   6901 C CE2 . TYR B 1 450 ? 20.991  -21.811 35.043  1.00 184.76 ? 450 TYR B CE2 1 
ATOM   6902 C CZ  . TYR B 1 450 ? 22.351  -22.067 35.070  1.00 191.58 ? 450 TYR B CZ  1 
ATOM   6903 O OH  . TYR B 1 450 ? 23.069  -21.880 36.211  1.00 226.69 ? 450 TYR B OH  1 
ATOM   6904 N N   . SER B 1 451 ? 19.601  -23.395 28.586  1.00 122.73 ? 451 SER B N   1 
ATOM   6905 C CA  . SER B 1 451 ? 19.146  -24.350 27.585  1.00 116.80 ? 451 SER B CA  1 
ATOM   6906 C C   . SER B 1 451 ? 20.141  -24.402 26.418  1.00 127.44 ? 451 SER B C   1 
ATOM   6907 O O   . SER B 1 451 ? 20.553  -25.483 25.958  1.00 129.28 ? 451 SER B O   1 
ATOM   6908 C CB  . SER B 1 451 ? 17.750  -23.931 27.134  1.00 105.75 ? 451 SER B CB  1 
ATOM   6909 O OG  . SER B 1 451 ? 17.357  -24.509 25.894  1.00 105.91 ? 451 SER B OG  1 
ATOM   6910 N N   . ARG B 1 452 ? 20.501  -23.202 25.968  1.00 145.19 ? 452 ARG B N   1 
ATOM   6911 C CA  . ARG B 1 452 ? 21.418  -23.017 24.845  1.00 158.05 ? 452 ARG B CA  1 
ATOM   6912 C C   . ARG B 1 452 ? 22.759  -23.682 25.160  1.00 143.51 ? 452 ARG B C   1 
ATOM   6913 O O   . ARG B 1 452 ? 23.324  -24.400 24.325  1.00 131.97 ? 452 ARG B O   1 
ATOM   6914 C CB  . ARG B 1 452 ? 21.345  -21.555 24.363  1.00 197.23 ? 452 ARG B CB  1 
ATOM   6915 C CG  . ARG B 1 452 ? 21.466  -21.206 22.884  1.00 200.33 ? 452 ARG B CG  1 
ATOM   6916 C CD  . ARG B 1 452 ? 20.655  -19.951 22.467  1.00 166.52 ? 452 ARG B CD  1 
ATOM   6917 N NE  . ARG B 1 452 ? 21.172  -18.618 22.809  1.00 154.38 ? 452 ARG B NE  1 
ATOM   6918 C CZ  . ARG B 1 452 ? 20.628  -17.720 23.641  1.00 163.61 ? 452 ARG B CZ  1 
ATOM   6919 N NH1 . ARG B 1 452 ? 19.468  -17.967 24.238  1.00 158.07 ? 452 ARG B NH1 1 
ATOM   6920 N NH2 . ARG B 1 452 ? 21.252  -16.563 23.870  1.00 156.82 ? 452 ARG B NH2 1 
ATOM   6921 N N   . ALA B 1 453 ? 23.235  -23.427 26.377  1.00 142.97 ? 453 ALA B N   1 
ATOM   6922 C CA  . ALA B 1 453 ? 24.497  -23.957 26.873  1.00 148.73 ? 453 ALA B CA  1 
ATOM   6923 C C   . ALA B 1 453 ? 24.474  -25.482 26.822  1.00 144.16 ? 453 ALA B C   1 
ATOM   6924 O O   . ALA B 1 453 ? 25.428  -26.119 26.354  1.00 157.76 ? 453 ALA B O   1 
ATOM   6925 C CB  . ALA B 1 453 ? 24.657  -23.473 28.297  1.00 180.11 ? 453 ALA B CB  1 
ATOM   6926 N N   . ALA B 1 454 ? 23.363  -26.030 27.320  1.00 134.12 ? 454 ALA B N   1 
ATOM   6927 C CA  . ALA B 1 454 ? 23.155  -27.473 27.377  1.00 127.91 ? 454 ALA B CA  1 
ATOM   6928 C C   . ALA B 1 454 ? 23.235  -28.067 25.966  1.00 134.84 ? 454 ALA B C   1 
ATOM   6929 O O   . ALA B 1 454 ? 23.902  -29.087 25.745  1.00 140.67 ? 454 ALA B O   1 
ATOM   6930 C CB  . ALA B 1 454 ? 21.871  -27.768 28.118  1.00 117.84 ? 454 ALA B CB  1 
ATOM   6931 N N   . GLN B 1 455 ? 22.550  -27.390 25.042  1.00 128.73 ? 455 GLN B N   1 
ATOM   6932 C CA  . GLN B 1 455 ? 22.502  -27.800 23.642  1.00 124.89 ? 455 GLN B CA  1 
ATOM   6933 C C   . GLN B 1 455 ? 23.913  -27.850 23.059  1.00 124.69 ? 455 GLN B C   1 
ATOM   6934 O O   . GLN B 1 455 ? 24.291  -28.809 22.381  1.00 136.32 ? 455 GLN B O   1 
ATOM   6935 C CB  . GLN B 1 455 ? 21.596  -26.933 22.773  1.00 135.07 ? 455 GLN B CB  1 
ATOM   6936 C CG  . GLN B 1 455 ? 20.143  -26.927 23.236  1.00 158.80 ? 455 GLN B CG  1 
ATOM   6937 C CD  . GLN B 1 455 ? 19.319  -25.782 22.681  1.00 175.39 ? 455 GLN B CD  1 
ATOM   6938 O OE1 . GLN B 1 455 ? 19.032  -25.728 21.482  1.00 223.96 ? 455 GLN B OE1 1 
ATOM   6939 N NE2 . GLN B 1 455 ? 18.896  -24.863 23.542  1.00 140.98 ? 455 GLN B NE2 1 
ATOM   6940 N N   . ALA B 1 456 ? 24.664  -26.792 23.347  1.00 131.82 ? 456 ALA B N   1 
ATOM   6941 C CA  . ALA B 1 456 ? 26.040  -26.644 22.882  1.00 156.41 ? 456 ALA B CA  1 
ATOM   6942 C C   . ALA B 1 456 ? 26.887  -27.814 23.376  1.00 158.04 ? 456 ALA B C   1 
ATOM   6943 O O   . ALA B 1 456 ? 27.655  -28.419 22.615  1.00 163.46 ? 456 ALA B O   1 
ATOM   6944 C CB  . ALA B 1 456 ? 26.600  -25.310 23.323  1.00 201.54 ? 456 ALA B CB  1 
ATOM   6945 N N   . LEU B 1 457 ? 26.714  -28.114 24.665  1.00 153.72 ? 457 LEU B N   1 
ATOM   6946 C CA  . LEU B 1 457 ? 27.445  -29.174 25.341  1.00 151.20 ? 457 LEU B CA  1 
ATOM   6947 C C   . LEU B 1 457 ? 27.158  -30.505 24.650  1.00 149.88 ? 457 LEU B C   1 
ATOM   6948 O O   . LEU B 1 457 ? 28.099  -31.273 24.405  1.00 170.41 ? 457 LEU B O   1 
ATOM   6949 C CB  . LEU B 1 457 ? 27.089  -29.182 26.828  1.00 159.26 ? 457 LEU B CB  1 
ATOM   6950 C CG  . LEU B 1 457 ? 27.900  -30.144 27.694  1.00 191.17 ? 457 LEU B CG  1 
ATOM   6951 C CD1 . LEU B 1 457 ? 29.367  -30.125 27.311  1.00 189.42 ? 457 LEU B CD1 1 
ATOM   6952 C CD2 . LEU B 1 457 ? 27.743  -29.705 29.133  1.00 209.47 ? 457 LEU B CD2 1 
ATOM   6953 N N   . LEU B 1 458 ? 25.870  -30.733 24.355  1.00 150.17 ? 458 LEU B N   1 
ATOM   6954 C CA  . LEU B 1 458 ? 25.445  -32.063 23.946  1.00 143.84 ? 458 LEU B CA  1 
ATOM   6955 C C   . LEU B 1 458 ? 25.692  -32.252 22.455  1.00 141.21 ? 458 LEU B C   1 
ATOM   6956 O O   . LEU B 1 458 ? 25.981  -33.360 22.050  1.00 145.94 ? 458 LEU B O   1 
ATOM   6957 C CB  . LEU B 1 458 ? 24.053  -32.447 24.448  1.00 122.22 ? 458 LEU B CB  1 
ATOM   6958 C CG  . LEU B 1 458 ? 23.918  -32.329 25.975  1.00 125.35 ? 458 LEU B CG  1 
ATOM   6959 C CD1 . LEU B 1 458 ? 22.501  -32.165 26.452  1.00 126.15 ? 458 LEU B CD1 1 
ATOM   6960 C CD2 . LEU B 1 458 ? 24.613  -33.423 26.760  1.00 126.08 ? 458 LEU B CD2 1 
ATOM   6961 N N   . THR B 1 459 ? 25.598  -31.190 21.644  1.00 148.68 ? 459 THR B N   1 
ATOM   6962 C CA  . THR B 1 459 ? 25.673  -31.313 20.193  1.00 154.51 ? 459 THR B CA  1 
ATOM   6963 C C   . THR B 1 459 ? 27.036  -30.867 19.672  1.00 179.40 ? 459 THR B C   1 
ATOM   6964 O O   . THR B 1 459 ? 27.116  -30.170 18.659  1.00 180.56 ? 459 THR B O   1 
ATOM   6965 C CB  . THR B 1 459 ? 24.563  -30.530 19.495  1.00 168.80 ? 459 THR B CB  1 
ATOM   6966 O OG1 . THR B 1 459 ? 24.669  -29.194 19.982  1.00 198.55 ? 459 THR B OG1 1 
ATOM   6967 C CG2 . THR B 1 459 ? 23.187  -31.116 19.740  1.00 167.56 ? 459 THR B CG2 1 
ATOM   6968 N N   . GLY B 1 460 ? 28.097  -31.285 20.364  1.00 209.73 ? 460 GLY B N   1 
ATOM   6969 C CA  . GLY B 1 460 ? 29.439  -31.126 19.836  1.00 215.61 ? 460 GLY B CA  1 
ATOM   6970 C C   . GLY B 1 460 ? 30.326  -32.297 20.251  1.00 205.42 ? 460 GLY B C   1 
ATOM   6971 O O   . GLY B 1 460 ? 29.869  -33.248 20.885  1.00 214.87 ? 460 GLY B O   1 
ATOM   6972 N N   . PRO B 1 461 ? 31.621  -32.275 19.872  1.00 176.66 ? 461 PRO B N   1 
ATOM   6973 C CA  . PRO B 1 461 ? 32.617  -33.167 20.472  1.00 166.50 ? 461 PRO B CA  1 
ATOM   6974 C C   . PRO B 1 461 ? 33.087  -32.667 21.838  1.00 152.61 ? 461 PRO B C   1 
ATOM   6975 O O   . PRO B 1 461 ? 32.563  -31.675 22.343  1.00 159.91 ? 461 PRO B O   1 
ATOM   6976 C CB  . PRO B 1 461 ? 33.713  -33.102 19.390  1.00 175.50 ? 461 PRO B CB  1 
ATOM   6977 C CG  . PRO B 1 461 ? 33.005  -32.542 18.171  1.00 170.33 ? 461 PRO B CG  1 
ATOM   6978 C CD  . PRO B 1 461 ? 32.163  -31.452 18.781  1.00 166.76 ? 461 PRO B CD  1 
ATOM   6979 N N   . TYR B 1 462 ? 34.102  -33.331 22.415  1.00 156.97 ? 462 TYR B N   1 
ATOM   6980 C CA  . TYR B 1 462 ? 34.559  -33.013 23.759  1.00 157.84 ? 462 TYR B CA  1 
ATOM   6981 C C   . TYR B 1 462 ? 35.986  -33.566 24.012  1.00 152.10 ? 462 TYR B C   1 
ATOM   6982 O O   . TYR B 1 462 ? 36.683  -33.115 24.968  1.00 132.50 ? 462 TYR B O   1 
ATOM   6983 C CB  . TYR B 1 462 ? 33.444  -33.594 24.632  1.00 138.23 ? 462 TYR B CB  1 
ATOM   6984 C CG  . TYR B 1 462 ? 33.428  -33.166 26.088  1.00 139.17 ? 462 TYR B CG  1 
ATOM   6985 C CD1 . TYR B 1 462 ? 34.275  -33.776 27.010  1.00 154.29 ? 462 TYR B CD1 1 
ATOM   6986 C CD2 . TYR B 1 462 ? 32.569  -32.165 26.535  1.00 128.12 ? 462 TYR B CD2 1 
ATOM   6987 C CE1 . TYR B 1 462 ? 34.275  -33.397 28.345  1.00 160.65 ? 462 TYR B CE1 1 
ATOM   6988 C CE2 . TYR B 1 462 ? 32.547  -31.791 27.870  1.00 147.87 ? 462 TYR B CE2 1 
ATOM   6989 C CZ  . TYR B 1 462 ? 33.394  -32.413 28.774  1.00 165.97 ? 462 TYR B CZ  1 
ATOM   6990 O OH  . TYR B 1 462 ? 33.374  -32.020 30.081  1.00 183.63 ? 462 TYR B OH  1 
HETATM 6991 N N9  . ADE C 2 .   ? 7.098   -28.160 -11.597 1.00 166.24 ? 501 ADE A N9  1 
HETATM 6992 C C8  . ADE C 2 .   ? 8.192   -28.747 -12.149 1.00 163.27 ? 501 ADE A C8  1 
HETATM 6993 N N7  . ADE C 2 .   ? 9.319   -28.161 -11.836 1.00 169.13 ? 501 ADE A N7  1 
HETATM 6994 C C5  . ADE C 2 .   ? 8.921   -27.107 -11.023 1.00 182.78 ? 501 ADE A C5  1 
HETATM 6995 C C6  . ADE C 2 .   ? 9.638   -26.098 -10.354 1.00 238.92 ? 501 ADE A C6  1 
HETATM 6996 N N6  . ADE C 2 .   ? 10.962  -25.986 -10.399 1.00 291.48 ? 501 ADE A N6  1 
HETATM 6997 N N1  . ADE C 2 .   ? 8.931   -25.200 -9.626  1.00 240.22 ? 501 ADE A N1  1 
HETATM 6998 C C2  . ADE C 2 .   ? 7.599   -25.316 -9.584  1.00 195.23 ? 501 ADE A C2  1 
HETATM 6999 N N3  . ADE C 2 .   ? 6.822   -26.225 -10.159 1.00 160.76 ? 501 ADE A N3  1 
HETATM 7000 C C4  . ADE C 2 .   ? 7.548   -27.100 -10.875 1.00 151.30 ? 501 ADE A C4  1 
HETATM 7001 N N9  . ADE D 2 .   ? -3.949  -23.473 13.232  1.00 168.00 ? 501 ADE B N9  1 
HETATM 7002 C C8  . ADE D 2 .   ? -5.147  -23.994 13.612  1.00 173.84 ? 501 ADE B C8  1 
HETATM 7003 N N7  . ADE D 2 .   ? -6.167  -23.525 12.935  1.00 175.63 ? 501 ADE B N7  1 
HETATM 7004 C C5  . ADE D 2 .   ? -5.581  -22.629 12.044  1.00 182.82 ? 501 ADE B C5  1 
HETATM 7005 C C6  . ADE D 2 .   ? -6.111  -21.795 11.040  1.00 209.94 ? 501 ADE B C6  1 
HETATM 7006 N N6  . ADE D 2 .   ? -7.410  -21.741 10.752  1.00 243.78 ? 501 ADE B N6  1 
HETATM 7007 N N1  . ADE D 2 .   ? -5.246  -21.022 10.331  1.00 166.25 ? 501 ADE B N1  1 
HETATM 7008 C C2  . ADE D 2 .   ? -3.943  -21.079 10.626  1.00 133.47 ? 501 ADE B C2  1 
HETATM 7009 N N3  . ADE D 2 .   ? -3.332  -21.827 11.539  1.00 139.68 ? 501 ADE B N3  1 
HETATM 7010 C C4  . ADE D 2 .   ? -4.210  -22.588 12.225  1.00 150.21 ? 501 ADE B C4  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY A 5   ? 2.2586 2.0492 3.0018 -0.1535 0.0630  -0.4493 5   GLY A N   
2    C CA  . GLY A 5   ? 2.2466 2.0431 3.0191 -0.1369 0.0379  -0.4314 5   GLY A CA  
3    C C   . GLY A 5   ? 2.2168 2.0470 3.0295 -0.1299 0.0382  -0.4294 5   GLY A C   
4    O O   . GLY A 5   ? 2.4427 2.3006 3.2839 -0.1277 0.0501  -0.4488 5   GLY A O   
5    N N   . SER A 6   ? 2.0914 1.9188 2.9053 -0.1264 0.0246  -0.4063 6   SER A N   
6    C CA  . SER A 6   ? 1.8860 1.7408 2.7344 -0.1190 0.0213  -0.4005 6   SER A CA  
7    C C   . SER A 6   ? 1.8381 1.6932 2.7060 -0.1059 -0.0030 -0.3809 6   SER A C   
8    O O   . SER A 6   ? 2.3411 2.1749 3.1891 -0.1060 -0.0163 -0.3639 6   SER A O   
9    C CB  . SER A 6   ? 1.7400 1.5951 2.5709 -0.1295 0.0324  -0.3930 6   SER A CB  
10   O OG  . SER A 6   ? 1.6890 1.5327 2.4873 -0.1459 0.0532  -0.4060 6   SER A OG  
11   N N   . THR A 7   ? 1.6447 1.5255 2.5522 -0.0953 -0.0086 -0.3831 7   THR A N   
12   C CA  . THR A 7   ? 1.7859 1.6716 2.7134 -0.0850 -0.0289 -0.3644 7   THR A CA  
13   C C   . THR A 7   ? 1.8464 1.7550 2.7945 -0.0829 -0.0253 -0.3601 7   THR A C   
14   O O   . THR A 7   ? 2.2893 2.2187 3.2594 -0.0812 -0.0154 -0.3764 7   THR A O   
15   C CB  . THR A 7   ? 1.7927 1.6797 2.7442 -0.0734 -0.0444 -0.3699 7   THR A CB  
16   O OG1 . THR A 7   ? 2.0122 1.8730 2.9374 -0.0769 -0.0504 -0.3664 7   THR A OG1 
17   C CG2 . THR A 7   ? 1.5759 1.4708 2.5517 -0.0637 -0.0637 -0.3541 7   THR A CG2 
18   N N   . LYS A 8   ? 1.7260 1.6305 2.6659 -0.0830 -0.0335 -0.3388 8   LYS A N   
19   C CA  . LYS A 8   ? 1.4528 1.3749 2.4070 -0.0811 -0.0320 -0.3314 8   LYS A CA  
20   C C   . LYS A 8   ? 1.4591 1.3841 2.4276 -0.0726 -0.0512 -0.3121 8   LYS A C   
21   O O   . LYS A 8   ? 1.4186 1.3296 2.3728 -0.0731 -0.0620 -0.2972 8   LYS A O   
22   C CB  . LYS A 8   ? 1.2602 1.1753 2.1867 -0.0910 -0.0201 -0.3255 8   LYS A CB  
23   C CG  . LYS A 8   ? 1.4060 1.3117 2.3080 -0.1033 -0.0011 -0.3414 8   LYS A CG  
24   C CD  . LYS A 8   ? 1.5040 1.3988 2.3750 -0.1147 0.0106  -0.3372 8   LYS A CD  
25   C CE  . LYS A 8   ? 1.6175 1.4967 2.4589 -0.1285 0.0272  -0.3521 8   LYS A CE  
26   N NZ  . LYS A 8   ? 1.7121 1.6091 2.5755 -0.1290 0.0385  -0.3750 8   LYS A NZ  
27   N N   . ILE A 9   ? 1.4768 1.4211 2.4740 -0.0654 -0.0551 -0.3134 9   ILE A N   
28   C CA  . ILE A 9   ? 1.3774 1.3260 2.3909 -0.0579 -0.0727 -0.2981 9   ILE A CA  
29   C C   . ILE A 9   ? 1.5091 1.4717 2.5287 -0.0571 -0.0702 -0.2887 9   ILE A C   
30   O O   . ILE A 9   ? 1.6084 1.5851 2.6419 -0.0560 -0.0617 -0.3000 9   ILE A O   
31   C CB  . ILE A 9   ? 1.1158 1.0694 2.1560 -0.0490 -0.0832 -0.3090 9   ILE A CB  
32   C CG1 . ILE A 9   ? 1.0157 0.9531 2.0487 -0.0488 -0.0879 -0.3175 9   ILE A CG1 
33   C CG2 . ILE A 9   ? 0.9493 0.9076 2.0069 -0.0422 -0.1004 -0.2955 9   ILE A CG2 
34   C CD1 . ILE A 9   ? 1.0631 1.0025 2.1204 -0.0388 -0.0996 -0.3299 9   ILE A CD1 
35   N N   . LEU A 10  ? 1.4872 1.4466 2.4969 -0.0576 -0.0775 -0.2691 10  LEU A N   
36   C CA  . LEU A 10  ? 1.3992 1.3679 2.4057 -0.0581 -0.0726 -0.2602 10  LEU A CA  
37   C C   . LEU A 10  ? 1.3757 1.3552 2.4009 -0.0519 -0.0849 -0.2486 10  LEU A C   
38   O O   . LEU A 10  ? 1.2456 1.2211 2.2689 -0.0514 -0.0965 -0.2349 10  LEU A O   
39   C CB  . LEU A 10  ? 1.4003 1.3581 2.3796 -0.0630 -0.0703 -0.2487 10  LEU A CB  
40   C CG  . LEU A 10  ? 1.4486 1.3882 2.4022 -0.0701 -0.0622 -0.2564 10  LEU A CG  
41   C CD1 . LEU A 10  ? 1.5796 1.5065 2.5078 -0.0727 -0.0653 -0.2434 10  LEU A CD1 
42   C CD2 . LEU A 10  ? 1.2738 1.2145 2.2211 -0.0759 -0.0453 -0.2725 10  LEU A CD2 
43   N N   . ILE A 11  ? 1.2941 1.2866 2.3364 -0.0482 -0.0824 -0.2550 11  ILE A N   
44   C CA  . ILE A 11  ? 1.3318 1.3323 2.3898 -0.0427 -0.0937 -0.2458 11  ILE A CA  
45   C C   . ILE A 11  ? 1.4691 1.4807 2.5272 -0.0427 -0.0846 -0.2459 11  ILE A C   
46   O O   . ILE A 11  ? 1.6740 1.6931 2.7436 -0.0418 -0.0778 -0.2605 11  ILE A O   
47   C CB  . ILE A 11  ? 1.1842 1.1859 2.2649 -0.0366 -0.1033 -0.2572 11  ILE A CB  
48   C CG1 . ILE A 11  ? 1.2442 1.2343 2.3242 -0.0367 -0.1070 -0.2664 11  ILE A CG1 
49   C CG2 . ILE A 11  ? 1.1494 1.1517 2.2404 -0.0322 -0.1191 -0.2451 11  ILE A CG2 
50   C CD1 . ILE A 11  ? 1.2252 1.2168 2.3279 -0.0290 -0.1151 -0.2821 11  ILE A CD1 
51   N N   . TYR A 12  ? 1.3615 1.3736 2.4053 -0.0442 -0.0835 -0.2315 12  TYR A N   
52   C CA  . TYR A 12  ? 1.3456 1.3644 2.3836 -0.0446 -0.0747 -0.2307 12  TYR A CA  
53   C C   . TYR A 12  ? 1.3618 1.3893 2.4109 -0.0396 -0.0835 -0.2206 12  TYR A C   
54   O O   . TYR A 12  ? 1.7529 1.7838 2.7922 -0.0391 -0.0818 -0.2104 12  TYR A O   
55   C CB  . TYR A 12  ? 1.4378 1.4482 2.4502 -0.0486 -0.0687 -0.2234 12  TYR A CB  
56   C CG  . TYR A 12  ? 1.2321 1.2396 2.2280 -0.0524 -0.0561 -0.2285 12  TYR A CG  
57   C CD1 . TYR A 12  ? 1.1688 1.1817 2.1604 -0.0497 -0.0552 -0.2211 12  TYR A CD1 
58   C CD2 . TYR A 12  ? 1.1241 1.1213 2.1056 -0.0595 -0.0453 -0.2403 12  TYR A CD2 
59   C CE1 . TYR A 12  ? 1.3594 1.3665 2.3335 -0.0536 -0.0450 -0.2254 12  TYR A CE1 
60   C CE2 . TYR A 12  ? 1.0881 1.0795 2.0510 -0.0649 -0.0344 -0.2443 12  TYR A CE2 
61   C CZ  . TYR A 12  ? 1.3501 1.3456 2.3091 -0.0618 -0.0349 -0.2366 12  TYR A CZ  
62   O OH  . TYR A 12  ? 1.4358 1.4228 2.3744 -0.0674 -0.0256 -0.2399 12  TYR A OH  
63   N N   . ALA A 13  ? 1.2288 1.2579 2.2967 -0.0358 -0.0937 -0.2239 13  ALA A N   
64   C CA  . ALA A 13  ? 1.2477 1.2811 2.3247 -0.0318 -0.1039 -0.2154 13  ALA A CA  
65   C C   . ALA A 13  ? 1.3200 1.3620 2.4006 -0.0297 -0.0977 -0.2199 13  ALA A C   
66   O O   . ALA A 13  ? 1.4064 1.4528 2.4948 -0.0299 -0.0900 -0.2349 13  ALA A O   
67   C CB  . ALA A 13  ? 1.4220 1.4503 2.5154 -0.0282 -0.1175 -0.2204 13  ALA A CB  
68   N N   . PHE A 14  ? 1.4407 1.4856 2.5154 -0.0284 -0.1011 -0.2069 14  PHE A N   
69   C CA  . PHE A 14  ? 1.5639 1.6149 2.6409 -0.0259 -0.0981 -0.2091 14  PHE A CA  
70   C C   . PHE A 14  ? 1.4897 1.5397 2.5832 -0.0213 -0.1116 -0.2111 14  PHE A C   
71   O O   . PHE A 14  ? 1.4533 1.4999 2.5428 -0.0205 -0.1213 -0.1984 14  PHE A O   
72   C CB  . PHE A 14  ? 2.0543 2.1080 3.1143 -0.0261 -0.0939 -0.1962 14  PHE A CB  
73   C CG  . PHE A 14  ? 2.3081 2.3606 3.3501 -0.0289 -0.0817 -0.1962 14  PHE A CG  
74   C CD1 . PHE A 14  ? 2.2069 2.2536 3.2422 -0.0327 -0.0763 -0.2012 14  PHE A CD1 
75   C CD2 . PHE A 14  ? 2.3915 2.4459 3.4205 -0.0273 -0.0768 -0.1911 14  PHE A CD2 
76   C CE1 . PHE A 14  ? 1.7874 1.8286 2.8024 -0.0353 -0.0674 -0.2007 14  PHE A CE1 
77   C CE2 . PHE A 14  ? 2.2758 2.3253 3.2858 -0.0291 -0.0679 -0.1913 14  PHE A CE2 
78   C CZ  . PHE A 14  ? 1.8829 1.9250 2.8853 -0.0333 -0.0637 -0.1958 14  PHE A CZ  
79   N N   . ASN A 15  ? 1.6059 1.6586 2.7176 -0.0187 -0.1123 -0.2279 15  ASN A N   
80   C CA  . ASN A 15  ? 1.6397 1.6897 2.7698 -0.0127 -0.1272 -0.2341 15  ASN A CA  
81   C C   . ASN A 15  ? 1.6186 1.6732 2.7535 -0.0094 -0.1296 -0.2351 15  ASN A C   
82   O O   . ASN A 15  ? 1.6449 1.6925 2.7835 -0.0054 -0.1444 -0.2302 15  ASN A O   
83   C CB  . ASN A 15  ? 1.4804 1.5322 2.6293 -0.0100 -0.1282 -0.2527 15  ASN A CB  
84   C CG  . ASN A 15  ? 1.5166 1.5767 2.6633 -0.0152 -0.1098 -0.2645 15  ASN A CG  
85   O OD1 . ASN A 15  ? 1.5693 1.6369 2.7103 -0.0187 -0.0979 -0.2665 15  ASN A OD1 
86   N ND2 . ASN A 15  ? 1.4242 1.4810 2.5723 -0.0166 -0.1074 -0.2720 15  ASN A ND2 
87   N N   . TYR A 16  ? 1.7641 1.8280 2.8959 -0.0121 -0.1157 -0.2405 16  TYR A N   
88   C CA  . TYR A 16  ? 1.9639 2.0328 3.0999 -0.0099 -0.1162 -0.2433 16  TYR A CA  
89   C C   . TYR A 16  ? 2.2187 2.2810 3.3354 -0.0097 -0.1203 -0.2247 16  TYR A C   
90   O O   . TYR A 16  ? 2.3195 2.3830 3.4355 -0.0077 -0.1224 -0.2242 16  TYR A O   
91   C CB  . TYR A 16  ? 1.9080 1.9869 3.0442 -0.0149 -0.0993 -0.2554 16  TYR A CB  
92   C CG  . TYR A 16  ? 2.0794 2.1542 3.1891 -0.0209 -0.0866 -0.2449 16  TYR A CG  
93   C CD1 . TYR A 16  ? 2.1309 2.2015 3.2310 -0.0248 -0.0805 -0.2436 16  TYR A CD1 
94   C CD2 . TYR A 16  ? 2.0406 2.1139 3.1340 -0.0217 -0.0824 -0.2367 16  TYR A CD2 
95   C CE1 . TYR A 16  ? 2.1611 2.2261 3.2368 -0.0290 -0.0716 -0.2344 16  TYR A CE1 
96   C CE2 . TYR A 16  ? 1.9592 2.0271 3.0283 -0.0253 -0.0733 -0.2279 16  TYR A CE2 
97   C CZ  . TYR A 16  ? 2.2114 2.2752 3.2720 -0.0288 -0.0682 -0.2269 16  TYR A CZ  
98   O OH  . TYR A 16  ? 2.5229 2.5800 3.5597 -0.0312 -0.0612 -0.2192 16  TYR A OH  
99   N N   . ALA A 17  ? 2.5999 2.6565 3.7013 -0.0122 -0.1212 -0.2101 17  ALA A N   
100  C CA  . ALA A 17  ? 2.6461 2.6990 3.7303 -0.0127 -0.1245 -0.1932 17  ALA A CA  
101  C C   . ALA A 17  ? 2.5935 2.6362 3.6790 -0.0123 -0.1405 -0.1850 17  ALA A C   
102  O O   . ALA A 17  ? 2.4272 2.4667 3.5074 -0.0159 -0.1424 -0.1772 17  ALA A O   
103  C CB  . ALA A 17  ? 2.3921 2.4485 3.4583 -0.0164 -0.1132 -0.1837 17  ALA A CB  
104  N N   . ASP A 18  ? 2.6070 2.6430 3.6989 -0.0085 -0.1530 -0.1872 18  ASP A N   
105  C CA  . ASP A 18  ? 2.7683 2.7895 3.8584 -0.0084 -0.1705 -0.1802 18  ASP A CA  
106  C C   . ASP A 18  ? 2.6587 2.6750 3.7262 -0.0134 -0.1718 -0.1617 18  ASP A C   
107  O O   . ASP A 18  ? 2.6646 2.6699 3.7234 -0.0180 -0.1815 -0.1514 18  ASP A O   
108  C CB  . ASP A 18  ? 2.8579 2.8711 3.9640 -0.0015 -0.1858 -0.1918 18  ASP A CB  
109  C CG  . ASP A 18  ? 2.6299 2.6362 3.7537 0.0024  -0.1976 -0.2032 18  ASP A CG  
110  O OD1 . ASP A 18  ? 2.4260 2.4329 3.5488 -0.0009 -0.1933 -0.2019 18  ASP A OD1 
111  O OD2 . ASP A 18  ? 2.4021 2.4013 3.5398 0.0094  -0.2126 -0.2133 18  ASP A OD2 
112  N N   . ARG A 19  ? 2.5099 2.5340 3.5673 -0.0130 -0.1619 -0.1582 19  ARG A N   
113  C CA  . ARG A 19  ? 2.7497 2.7723 3.7859 -0.0169 -0.1608 -0.1430 19  ARG A CA  
114  C C   . ARG A 19  ? 2.9667 3.0030 3.9936 -0.0207 -0.1461 -0.1357 19  ARG A C   
115  O O   . ARG A 19  ? 2.8098 2.8472 3.8260 -0.0266 -0.1467 -0.1236 19  ARG A O   
116  C CB  . ARG A 19  ? 2.9562 2.9756 3.9858 -0.0130 -0.1626 -0.1438 19  ARG A CB  
117  C CG  . ARG A 19  ? 2.7607 2.7855 3.7696 -0.0146 -0.1534 -0.1335 19  ARG A CG  
118  C CD  . ARG A 19  ? 2.4757 2.4963 3.4810 -0.0096 -0.1552 -0.1381 19  ARG A CD  
119  N NE  . ARG A 19  ? 2.4234 2.4415 3.4510 -0.0050 -0.1623 -0.1532 19  ARG A NE  
120  C CZ  . ARG A 19  ? 2.4193 2.4239 3.4539 -0.0024 -0.1791 -0.1570 19  ARG A CZ  
121  N NH1 . ARG A 19  ? 2.2760 2.2663 3.2939 -0.0030 -0.1893 -0.1485 19  ARG A NH1 
122  N NH2 . ARG A 19  ? 2.4085 2.4136 3.4668 0.0014  -0.1861 -0.1709 19  ARG A NH2 
123  N N   . MET A 20  ? 3.2215 3.2679 4.2530 -0.0177 -0.1339 -0.1438 20  MET A N   
124  C CA  . MET A 20  ? 3.1058 3.1636 4.1262 -0.0189 -0.1213 -0.1381 20  MET A CA  
125  C C   . MET A 20  ? 3.6865 3.7479 4.7068 -0.0242 -0.1218 -0.1308 20  MET A C   
126  O O   . MET A 20  ? 4.3471 4.4175 5.3572 -0.0267 -0.1170 -0.1211 20  MET A O   
127  C CB  . MET A 20  ? 2.5655 2.6279 3.5869 -0.0153 -0.1102 -0.1483 20  MET A CB  
128  C CG  . MET A 20  ? 2.3410 2.4007 3.3592 -0.0115 -0.1099 -0.1526 20  MET A CG  
129  S SD  . MET A 20  ? 2.8133 2.8773 3.8154 -0.0085 -0.0966 -0.1539 20  MET A SD  
130  C CE  . MET A 20  ? 2.5996 2.6713 3.5836 -0.0073 -0.0929 -0.1398 20  MET A CE  
131  N N   . LEU A 21  ? 3.5708 3.6253 4.6029 -0.0260 -0.1287 -0.1357 21  LEU A N   
132  C CA  . LEU A 21  ? 3.1477 3.2023 4.1802 -0.0317 -0.1319 -0.1293 21  LEU A CA  
133  C C   . LEU A 21  ? 3.2249 3.2801 4.2462 -0.0383 -0.1368 -0.1146 21  LEU A C   
134  O O   . LEU A 21  ? 3.2121 3.2771 4.2291 -0.0435 -0.1329 -0.1065 21  LEU A O   
135  C CB  . LEU A 21  ? 2.1546 2.1977 3.2006 -0.0313 -0.1413 -0.1381 21  LEU A CB  
136  C CG  . LEU A 21  ? 1.5631 1.6042 2.6118 -0.0360 -0.1436 -0.1363 21  LEU A CG  
137  C CD1 . LEU A 21  ? 1.6430 1.6961 2.6837 -0.0401 -0.1349 -0.1281 21  LEU A CD1 
138  C CD2 . LEU A 21  ? 1.0250 1.0623 2.0861 -0.0319 -0.1421 -0.1519 21  LEU A CD2 
139  N N   . GLU A 22  ? 3.0990 3.1444 4.1148 -0.0385 -0.1449 -0.1115 22  GLU A N   
140  C CA  . GLU A 22  ? 2.9243 2.9672 3.9258 -0.0466 -0.1495 -0.0978 22  GLU A CA  
141  C C   . GLU A 22  ? 3.1967 3.2557 4.1864 -0.0465 -0.1373 -0.0917 22  GLU A C   
142  O O   . GLU A 22  ? 3.4503 3.5114 4.4271 -0.0540 -0.1378 -0.0809 22  GLU A O   
143  C CB  . GLU A 22  ? 2.6507 2.6721 3.6472 -0.0475 -0.1650 -0.0966 22  GLU A CB  
144  C CG  . GLU A 22  ? 2.7583 2.7631 3.7675 -0.0453 -0.1790 -0.1047 22  GLU A CG  
145  C CD  . GLU A 22  ? 2.8939 2.8753 3.8971 -0.0448 -0.1968 -0.1042 22  GLU A CD  
146  O OE1 . GLU A 22  ? 2.8486 2.8276 3.8478 -0.0400 -0.1975 -0.1064 22  GLU A OE1 
147  O OE2 . GLU A 22  ? 3.2350 3.1985 4.2368 -0.0487 -0.2114 -0.1019 22  GLU A OE2 
148  N N   . GLU A 23  ? 3.2518 3.3212 4.2441 -0.0383 -0.1265 -0.0990 23  GLU A N   
149  C CA  . GLU A 23  ? 2.9576 3.0409 3.9388 -0.0357 -0.1158 -0.0954 23  GLU A CA  
150  C C   . GLU A 23  ? 2.4508 2.5509 3.4355 -0.0332 -0.1054 -0.0971 23  GLU A C   
151  O O   . GLU A 23  ? 2.2560 2.3693 3.2398 -0.0384 -0.1027 -0.0900 23  GLU A O   
152  C CB  . GLU A 23  ? 3.1891 3.2664 4.1653 -0.0280 -0.1142 -0.1016 23  GLU A CB  
153  C CG  . GLU A 23  ? 3.3112 3.3705 4.2854 -0.0289 -0.1264 -0.1018 23  GLU A CG  
154  C CD  . GLU A 23  ? 3.5785 3.6298 4.5400 -0.0377 -0.1345 -0.0901 23  GLU A CD  
155  O OE1 . GLU A 23  ? 3.5397 3.5995 4.4863 -0.0408 -0.1280 -0.0822 23  GLU A OE1 
156  O OE2 . GLU A 23  ? 3.8125 3.8480 4.7776 -0.0417 -0.1476 -0.0893 23  GLU A OE2 
157  N N   . VAL A 24  ? 2.2388 2.3378 3.2266 -0.0257 -0.1002 -0.1067 24  VAL A N   
158  C CA  . VAL A 24  ? 1.8682 1.9770 2.8574 -0.0229 -0.0931 -0.1094 24  VAL A CA  
159  C C   . VAL A 24  ? 1.8294 1.9388 2.8281 -0.0295 -0.0979 -0.1070 24  VAL A C   
160  O O   . VAL A 24  ? 1.7203 1.8172 2.7268 -0.0317 -0.1043 -0.1112 24  VAL A O   
161  C CB  . VAL A 24  ? 1.8330 1.9346 2.8203 -0.0163 -0.0881 -0.1202 24  VAL A CB  
162  C CG1 . VAL A 24  ? 1.8664 1.9699 2.8411 -0.0097 -0.0825 -0.1212 24  VAL A CG1 
163  C CG2 . VAL A 24  ? 1.7040 1.7919 2.7006 -0.0175 -0.0926 -0.1286 24  VAL A CG2 
164  N N   . PRO A 25  ? 1.9331 2.0577 2.9321 -0.0330 -0.0957 -0.1002 25  PRO A N   
165  C CA  . PRO A 25  ? 1.8973 2.0225 2.9040 -0.0415 -0.1018 -0.0955 25  PRO A CA  
166  C C   . PRO A 25  ? 1.6442 1.7681 2.6563 -0.0394 -0.1010 -0.1013 25  PRO A C   
167  O O   . PRO A 25  ? 1.4981 1.6145 2.5165 -0.0449 -0.1074 -0.1010 25  PRO A O   
168  C CB  . PRO A 25  ? 1.5877 1.7326 2.5920 -0.0474 -0.0990 -0.0857 25  PRO A CB  
169  C CG  . PRO A 25  ? 1.7975 1.9561 2.7958 -0.0379 -0.0894 -0.0888 25  PRO A CG  
170  C CD  . PRO A 25  ? 1.6593 1.8023 2.6522 -0.0288 -0.0879 -0.0976 25  PRO A CD  
171  N N   . TYR A 26  ? 1.4105 1.5388 2.4175 -0.0315 -0.0940 -0.1067 26  TYR A N   
172  C CA  . TYR A 26  ? 1.3429 1.4672 2.3502 -0.0293 -0.0934 -0.1122 26  TYR A CA  
173  C C   . TYR A 26  ? 1.3343 1.4392 2.3433 -0.0302 -0.0955 -0.1205 26  TYR A C   
174  O O   . TYR A 26  ? 1.3000 1.3970 2.3064 -0.0294 -0.0945 -0.1263 26  TYR A O   
175  C CB  . TYR A 26  ? 1.4407 1.5700 2.4382 -0.0203 -0.0870 -0.1160 26  TYR A CB  
176  C CG  . TYR A 26  ? 1.3920 1.5102 2.3796 -0.0146 -0.0824 -0.1223 26  TYR A CG  
177  C CD1 . TYR A 26  ? 1.3726 1.4734 2.3545 -0.0137 -0.0807 -0.1311 26  TYR A CD1 
178  C CD2 . TYR A 26  ? 1.4683 1.5933 2.4515 -0.0112 -0.0797 -0.1195 26  TYR A CD2 
179  C CE1 . TYR A 26  ? 1.7625 1.8540 2.7358 -0.0103 -0.0764 -0.1369 26  TYR A CE1 
180  C CE2 . TYR A 26  ? 1.8748 1.9890 2.8488 -0.0066 -0.0764 -0.1250 26  TYR A CE2 
181  C CZ  . TYR A 26  ? 2.0638 2.1617 3.0334 -0.0064 -0.0749 -0.1337 26  TYR A CZ  
182  O OH  . TYR A 26  ? 2.6149 2.7030 3.5757 -0.0035 -0.0715 -0.1393 26  TYR A OH  
183  N N   . LEU A 27  ? 1.4173 1.5147 2.4301 -0.0315 -0.0985 -0.1217 27  LEU A N   
184  C CA  . LEU A 27  ? 1.4683 1.5511 2.4861 -0.0314 -0.1002 -0.1316 27  LEU A CA  
185  C C   . LEU A 27  ? 1.3777 1.4541 2.4030 -0.0366 -0.1071 -0.1318 27  LEU A C   
186  O O   . LEU A 27  ? 1.3757 1.4425 2.4031 -0.0362 -0.1060 -0.1413 27  LEU A O   
187  C CB  . LEU A 27  ? 1.3965 1.4737 2.4186 -0.0299 -0.1033 -0.1346 27  LEU A CB  
188  C CG  . LEU A 27  ? 1.6429 1.7191 2.6593 -0.0246 -0.0961 -0.1414 27  LEU A CG  
189  C CD1 . LEU A 27  ? 1.9493 2.0171 2.9761 -0.0237 -0.0995 -0.1515 27  LEU A CD1 
190  C CD2 . LEU A 27  ? 1.9634 2.0389 2.9692 -0.0220 -0.0870 -0.1464 27  LEU A CD2 
191  N N   . ARG A 28  ? 1.3192 1.4006 2.3473 -0.0422 -0.1138 -0.1217 28  ARG A N   
192  C CA  . ARG A 28  ? 1.4630 1.5359 2.4966 -0.0474 -0.1216 -0.1218 28  ARG A CA  
193  C C   . ARG A 28  ? 1.4716 1.5431 2.5020 -0.0463 -0.1174 -0.1269 28  ARG A C   
194  O O   . ARG A 28  ? 1.4831 1.5428 2.5162 -0.0480 -0.1212 -0.1327 28  ARG A O   
195  C CB  . ARG A 28  ? 1.4053 1.4805 2.4405 -0.0556 -0.1305 -0.1100 28  ARG A CB  
196  C CG  . ARG A 28  ? 1.5700 1.6645 2.6022 -0.0596 -0.1266 -0.0999 28  ARG A CG  
197  C CD  . ARG A 28  ? 1.8117 1.9049 2.8462 -0.0707 -0.1360 -0.0908 28  ARG A CD  
198  N NE  . ARG A 28  ? 2.0772 2.1560 3.1093 -0.0755 -0.1452 -0.0870 28  ARG A NE  
199  C CZ  . ARG A 28  ? 2.3451 2.4158 3.3755 -0.0863 -0.1556 -0.0790 28  ARG A CZ  
200  N NH1 . ARG A 28  ? 2.3872 2.4647 3.4201 -0.0937 -0.1575 -0.0742 28  ARG A NH1 
201  N NH2 . ARG A 28  ? 2.2863 2.3402 3.3111 -0.0897 -0.1652 -0.0759 28  ARG A NH2 
202  N N   . TYR A 29  ? 1.3311 1.4124 2.3541 -0.0428 -0.1103 -0.1256 29  TYR A N   
203  C CA  . TYR A 29  ? 1.1394 1.2168 2.1558 -0.0417 -0.1080 -0.1295 29  TYR A CA  
204  C C   . TYR A 29  ? 1.0217 1.0860 2.0289 -0.0378 -0.1009 -0.1411 29  TYR A C   
205  O O   . TYR A 29  ? 0.7916 0.8479 1.7887 -0.0374 -0.0989 -0.1451 29  TYR A O   
206  C CB  . TYR A 29  ? 0.9604 1.0535 1.9738 -0.0398 -0.1069 -0.1229 29  TYR A CB  
207  C CG  . TYR A 29  ? 1.2627 1.3697 2.2860 -0.0467 -0.1134 -0.1127 29  TYR A CG  
208  C CD1 . TYR A 29  ? 1.4314 1.5522 2.4593 -0.0497 -0.1132 -0.1049 29  TYR A CD1 
209  C CD2 . TYR A 29  ? 1.4864 1.5919 2.5129 -0.0516 -0.1197 -0.1110 29  TYR A CD2 
210  C CE1 . TYR A 29  ? 1.6717 1.8051 2.7067 -0.0585 -0.1182 -0.0956 29  TYR A CE1 
211  C CE2 . TYR A 29  ? 1.9131 2.0320 2.9485 -0.0597 -0.1255 -0.1017 29  TYR A CE2 
212  C CZ  . TYR A 29  ? 1.8865 2.0199 2.9261 -0.0639 -0.1243 -0.0940 29  TYR A CZ  
213  O OH  . TYR A 29  ? 1.6470 1.7935 2.6939 -0.0744 -0.1291 -0.0848 29  TYR A OH  
214  N N   . SER A 30  ? 1.0080 1.0690 2.0182 -0.0361 -0.0977 -0.1467 30  SER A N   
215  C CA  . SER A 30  ? 1.0806 1.1319 2.0831 -0.0343 -0.0897 -0.1579 30  SER A CA  
216  C C   . SER A 30  ? 1.1070 1.1450 2.1058 -0.0379 -0.0885 -0.1668 30  SER A C   
217  O O   . SER A 30  ? 1.0376 1.0663 2.0215 -0.0384 -0.0816 -0.1730 30  SER A O   
218  C CB  . SER A 30  ? 1.1796 1.2316 2.1910 -0.0330 -0.0885 -0.1633 30  SER A CB  
219  O OG  . SER A 30  ? 1.5045 1.5653 2.5133 -0.0295 -0.0875 -0.1567 30  SER A OG  
220  N N   . ALA A 31  ? 1.0882 1.1233 2.0984 -0.0407 -0.0953 -0.1678 31  ALA A N   
221  C CA  . ALA A 31  ? 1.1361 1.1586 2.1439 -0.0436 -0.0937 -0.1782 31  ALA A CA  
222  C C   . ALA A 31  ? 1.2757 1.2894 2.2649 -0.0455 -0.0908 -0.1776 31  ALA A C   
223  O O   . ALA A 31  ? 1.5497 1.5509 2.5288 -0.0483 -0.0850 -0.1876 31  ALA A O   
224  C CB  . ALA A 31  ? 0.9995 1.0189 2.0200 -0.0454 -0.1038 -0.1776 31  ALA A CB  
225  N N   . GLU A 32  ? 1.1345 1.1549 2.1192 -0.0439 -0.0950 -0.1666 32  GLU A N   
226  C CA  . GLU A 32  ? 1.1948 1.2061 2.1628 -0.0445 -0.0955 -0.1658 32  GLU A CA  
227  C C   . GLU A 32  ? 1.1614 1.1578 2.1088 -0.0449 -0.0861 -0.1750 32  GLU A C   
228  O O   . GLU A 32  ? 0.9643 0.9444 1.8933 -0.0474 -0.0857 -0.1784 32  GLU A O   
229  C CB  . GLU A 32  ? 1.3255 1.3510 2.2957 -0.0412 -0.1012 -0.1544 32  GLU A CB  
230  C CG  . GLU A 32  ? 1.7145 1.7454 2.6944 -0.0448 -0.1111 -0.1474 32  GLU A CG  
231  C CD  . GLU A 32  ? 2.3300 2.3745 3.3102 -0.0421 -0.1159 -0.1394 32  GLU A CD  
232  O OE1 . GLU A 32  ? 2.2230 2.2606 3.1885 -0.0379 -0.1154 -0.1420 32  GLU A OE1 
233  O OE2 . GLU A 32  ? 2.7738 2.8360 3.7691 -0.0447 -0.1207 -0.1310 32  GLU A OE2 
234  N N   . ARG A 33  ? 1.0107 1.0109 1.9598 -0.0436 -0.0789 -0.1791 33  ARG A N   
235  C CA  . ARG A 33  ? 0.9277 0.9140 1.8568 -0.0460 -0.0695 -0.1875 33  ARG A CA  
236  C C   . ARG A 33  ? 0.8788 0.8484 1.7974 -0.0531 -0.0653 -0.1977 33  ARG A C   
237  O O   . ARG A 33  ? 0.8475 0.7990 1.7406 -0.0570 -0.0607 -0.2018 33  ARG A O   
238  C CB  . ARG A 33  ? 0.8442 0.8378 1.7800 -0.0452 -0.0626 -0.1920 33  ARG A CB  
239  C CG  . ARG A 33  ? 0.8456 0.8515 1.7844 -0.0383 -0.0657 -0.1825 33  ARG A CG  
240  C CD  . ARG A 33  ? 1.0023 1.0137 1.9458 -0.0373 -0.0603 -0.1861 33  ARG A CD  
241  N NE  . ARG A 33  ? 1.1436 1.1621 2.0822 -0.0307 -0.0622 -0.1779 33  ARG A NE  
242  C CZ  . ARG A 33  ? 1.2534 1.2870 2.2063 -0.0264 -0.0656 -0.1716 33  ARG A CZ  
243  N NH1 . ARG A 33  ? 1.3276 1.3693 2.3005 -0.0280 -0.0690 -0.1718 33  ARG A NH1 
244  N NH2 . ARG A 33  ? 1.4477 1.4868 2.3932 -0.0204 -0.0663 -0.1654 33  ARG A NH2 
245  N N   . SER A 34  ? 0.8672 0.8414 1.8035 -0.0547 -0.0678 -0.2016 34  SER A N   
246  C CA  . SER A 34  ? 0.9946 0.9561 1.9246 -0.0608 -0.0627 -0.2135 34  SER A CA  
247  C C   . SER A 34  ? 1.0970 1.0390 2.0022 -0.0642 -0.0652 -0.2117 34  SER A C   
248  O O   . SER A 34  ? 1.2322 1.1591 2.1233 -0.0706 -0.0593 -0.2216 34  SER A O   
249  C CB  . SER A 34  ? 1.1173 1.0866 2.0713 -0.0599 -0.0670 -0.2184 34  SER A CB  
250  O OG  . SER A 34  ? 1.2754 1.2532 2.2440 -0.0558 -0.0796 -0.2067 34  SER A OG  
251  N N   . LEU A 35  ? 1.0269 0.9694 1.9260 -0.0599 -0.0739 -0.1998 35  LEU A N   
252  C CA  . LEU A 35  ? 1.1756 1.1007 2.0546 -0.0617 -0.0800 -0.1973 35  LEU A CA  
253  C C   . LEU A 35  ? 1.2111 1.1125 2.0560 -0.0660 -0.0734 -0.2027 35  LEU A C   
254  O O   . LEU A 35  ? 1.3242 1.2064 2.1466 -0.0673 -0.0791 -0.2011 35  LEU A O   
255  C CB  . LEU A 35  ? 1.2545 1.1920 2.1423 -0.0552 -0.0917 -0.1844 35  LEU A CB  
256  C CG  . LEU A 35  ? 1.1213 1.0745 2.0347 -0.0546 -0.1003 -0.1784 35  LEU A CG  
257  C CD1 . LEU A 35  ? 1.3218 1.2939 2.2467 -0.0494 -0.1081 -0.1665 35  LEU A CD1 
258  C CD2 . LEU A 35  ? 0.9721 0.9081 1.8751 -0.0590 -0.1060 -0.1809 35  LEU A CD2 
259  N N   . CYS A 36  ? 1.0001 0.9015 1.8402 -0.0689 -0.0623 -0.2092 36  CYS A N   
260  C CA  . CYS A 36  ? 1.0188 0.8957 1.8242 -0.0755 -0.0552 -0.2147 36  CYS A CA  
261  C C   . CYS A 36  ? 1.1095 0.9705 1.9012 -0.0864 -0.0462 -0.2267 36  CYS A C   
262  O O   . CYS A 36  ? 1.1801 1.0153 1.9373 -0.0948 -0.0408 -0.2315 36  CYS A O   
263  C CB  . CYS A 36  ? 1.0739 0.9580 1.8809 -0.0763 -0.0462 -0.2176 36  CYS A CB  
264  S SG  . CYS A 36  ? 1.0283 0.9437 1.8777 -0.0739 -0.0416 -0.2221 36  CYS A SG  
265  N N   . PHE A 37  ? 1.3017 1.1767 2.1186 -0.0863 -0.0454 -0.2318 37  PHE A N   
266  C CA  . PHE A 37  ? 1.6115 1.4776 2.4219 -0.0955 -0.0352 -0.2458 37  PHE A CA  
267  C C   . PHE A 37  ? 1.6991 1.5435 2.4894 -0.0986 -0.0414 -0.2456 37  PHE A C   
268  O O   . PHE A 37  ? 1.8890 1.7196 2.6640 -0.1074 -0.0326 -0.2572 37  PHE A O   
269  C CB  . PHE A 37  ? 1.6253 1.5162 2.4726 -0.0925 -0.0319 -0.2536 37  PHE A CB  
270  C CG  . PHE A 37  ? 1.5671 1.4759 2.4302 -0.0921 -0.0236 -0.2579 37  PHE A CG  
271  C CD1 . PHE A 37  ? 1.7501 1.6570 2.6047 -0.1018 -0.0080 -0.2720 37  PHE A CD1 
272  C CD2 . PHE A 37  ? 1.4690 1.3966 2.3552 -0.0829 -0.0312 -0.2484 37  PHE A CD2 
273  C CE1 . PHE A 37  ? 1.8309 1.7549 2.7016 -0.1017 -0.0015 -0.2763 37  PHE A CE1 
274  C CE2 . PHE A 37  ? 1.4747 1.4170 2.3745 -0.0823 -0.0248 -0.2524 37  PHE A CE2 
275  C CZ  . PHE A 37  ? 1.5220 1.4629 2.4151 -0.0913 -0.0105 -0.2663 37  PHE A CZ  
276  N N   . LEU A 38  ? 1.5866 1.4287 2.3769 -0.0916 -0.0564 -0.2328 38  LEU A N   
277  C CA  . LEU A 38  ? 1.5819 1.4049 2.3564 -0.0933 -0.0653 -0.2311 38  LEU A CA  
278  C C   . LEU A 38  ? 1.5052 1.2945 2.2358 -0.1038 -0.0584 -0.2384 38  LEU A C   
279  O O   . LEU A 38  ? 1.4196 1.1899 2.1337 -0.1082 -0.0614 -0.2418 38  LEU A O   
280  C CB  . LEU A 38  ? 1.5687 1.3969 2.3502 -0.0846 -0.0822 -0.2167 38  LEU A CB  
281  C CG  . LEU A 38  ? 1.3376 1.1976 2.1584 -0.0765 -0.0887 -0.2085 38  LEU A CG  
282  C CD1 . LEU A 38  ? 1.1098 0.9769 1.9360 -0.0699 -0.1031 -0.1957 38  LEU A CD1 
283  C CD2 . LEU A 38  ? 1.5959 1.4657 2.4402 -0.0772 -0.0902 -0.2122 38  LEU A CD2 
284  N N   . GLY A 39  ? 1.6075 1.3873 2.3170 -0.1086 -0.0496 -0.2406 39  GLY A N   
285  C CA  . GLY A 39  ? 1.7824 1.5280 2.4465 -0.1210 -0.0420 -0.2475 39  GLY A CA  
286  C C   . GLY A 39  ? 1.8987 1.6382 2.5574 -0.1315 -0.0298 -0.2616 39  GLY A C   
287  O O   . GLY A 39  ? 1.7574 1.4658 2.3787 -0.1409 -0.0281 -0.2660 39  GLY A O   
288  N N   . ASP A 40  ? 2.0615 1.8307 2.7578 -0.1290 -0.0222 -0.2693 40  ASP A N   
289  C CA  . ASP A 40  ? 2.0646 1.8355 2.7639 -0.1367 -0.0096 -0.2854 40  ASP A CA  
290  C C   . ASP A 40  ? 2.0199 1.7710 2.7048 -0.1370 -0.0184 -0.2853 40  ASP A C   
291  O O   . ASP A 40  ? 2.4458 2.1810 3.1092 -0.1472 -0.0081 -0.2977 40  ASP A O   
292  C CB  . ASP A 40  ? 2.1240 1.9307 2.8695 -0.1307 -0.0043 -0.2932 40  ASP A CB  
293  C CG  . ASP A 40  ? 2.1014 1.9268 2.8599 -0.1325 0.0063  -0.2967 40  ASP A CG  
294  O OD1 . ASP A 40  ? 2.1513 1.9625 2.8838 -0.1374 0.0083  -0.2908 40  ASP A OD1 
295  O OD2 . ASP A 40  ? 1.9016 1.7542 2.6953 -0.1288 0.0115  -0.3059 40  ASP A OD2 
296  N N   . LEU A 41  ? 1.8353 1.5874 2.5309 -0.1267 -0.0371 -0.2717 41  LEU A N   
297  C CA  . LEU A 41  ? 1.7729 1.5077 2.4580 -0.1264 -0.0476 -0.2707 41  LEU A CA  
298  C C   . LEU A 41  ? 1.8539 1.5485 2.4871 -0.1372 -0.0459 -0.2731 41  LEU A C   
299  O O   . LEU A 41  ? 1.9317 1.6070 2.5496 -0.1390 -0.0528 -0.2744 41  LEU A O   
300  C CB  . LEU A 41  ? 1.6838 1.4291 2.3910 -0.1150 -0.0678 -0.2556 41  LEU A CB  
301  C CG  . LEU A 41  ? 1.6543 1.4306 2.4070 -0.1066 -0.0721 -0.2543 41  LEU A CG  
302  C CD1 . LEU A 41  ? 1.5023 1.2914 2.2746 -0.0979 -0.0899 -0.2380 41  LEU A CD1 
303  C CD2 . LEU A 41  ? 1.6988 1.4697 2.4560 -0.1085 -0.0715 -0.2650 41  LEU A CD2 
304  N N   . ARG A 42  ? 1.7688 1.4486 2.3729 -0.1451 -0.0371 -0.2740 42  ARG A N   
305  C CA  . ARG A 42  ? 1.7979 1.4359 2.3475 -0.1578 -0.0337 -0.2775 42  ARG A CA  
306  C C   . ARG A 42  ? 2.0923 1.7202 2.6264 -0.1703 -0.0178 -0.2941 42  ARG A C   
307  O O   . ARG A 42  ? 2.0200 1.6122 2.5122 -0.1789 -0.0196 -0.2963 42  ARG A O   
308  C CB  . ARG A 42  ? 1.9336 1.5558 2.4535 -0.1647 -0.0280 -0.2751 42  ARG A CB  
309  C CG  . ARG A 42  ? 2.4695 2.0862 2.9867 -0.1534 -0.0470 -0.2594 42  ARG A CG  
310  C CD  . ARG A 42  ? 2.7023 2.2835 3.1711 -0.1611 -0.0475 -0.2568 42  ARG A CD  
311  N NE  . ARG A 42  ? 2.9713 2.5439 3.4358 -0.1481 -0.0689 -0.2434 42  ARG A NE  
312  C CZ  . ARG A 42  ? 3.0882 2.6464 3.5455 -0.1405 -0.0883 -0.2364 42  ARG A CZ  
313  N NH1 . ARG A 42  ? 3.1581 2.7020 3.6049 -0.1454 -0.0904 -0.2404 42  ARG A NH1 
314  N NH2 . ARG A 42  ? 3.0205 2.5788 3.4813 -0.1276 -0.1062 -0.2262 42  ARG A NH2 
315  N N   . ASP A 43  ? 2.4433 2.1019 3.0097 -0.1712 -0.0023 -0.3068 43  ASP A N   
316  C CA  . ASP A 43  ? 2.2575 1.9152 2.8203 -0.1795 0.0118  -0.3244 43  ASP A CA  
317  C C   . ASP A 43  ? 2.0270 1.6846 2.6055 -0.1697 -0.0025 -0.3226 43  ASP A C   
318  O O   . ASP A 43  ? 1.8568 1.5410 2.4776 -0.1562 -0.0133 -0.3165 43  ASP A O   
319  C CB  . ASP A 43  ? 2.1034 1.7960 2.6996 -0.1815 0.0307  -0.3401 43  ASP A CB  
320  C CG  . ASP A 43  ? 2.1065 1.8094 2.7163 -0.1831 0.0409  -0.3589 43  ASP A CG  
321  O OD1 . ASP A 43  ? 2.1306 1.8071 2.7030 -0.1950 0.0493  -0.3681 43  ASP A OD1 
322  O OD2 . ASP A 43  ? 1.9767 1.7125 2.6333 -0.1719 0.0397  -0.3647 43  ASP A OD2 
323  N N   . PRO A 44  ? 2.0103 1.6364 2.5530 -0.1773 -0.0030 -0.3278 44  PRO A N   
324  C CA  . PRO A 44  ? 1.9384 1.5595 2.4908 -0.1694 -0.0175 -0.3262 44  PRO A CA  
325  C C   . PRO A 44  ? 2.0389 1.6947 2.6409 -0.1594 -0.0157 -0.3351 44  PRO A C   
326  O O   . PRO A 44  ? 2.1343 1.7931 2.7555 -0.1496 -0.0320 -0.3292 44  PRO A O   
327  C CB  . PRO A 44  ? 1.9374 1.5208 2.4410 -0.1825 -0.0106 -0.3365 44  PRO A CB  
328  C CG  . PRO A 44  ? 2.0589 1.6219 2.5203 -0.1986 0.0051  -0.3403 44  PRO A CG  
329  C CD  . PRO A 44  ? 2.0746 1.6658 2.5626 -0.1952 0.0102  -0.3355 44  PRO A CD  
330  N N   . GLY A 45  ? 1.8979 1.5783 2.5189 -0.1626 0.0032  -0.3499 45  GLY A N   
331  C CA  . GLY A 45  ? 1.6797 1.3899 2.3435 -0.1539 0.0065  -0.3629 45  GLY A CA  
332  C C   . GLY A 45  ? 1.4376 1.1791 2.1480 -0.1401 -0.0046 -0.3526 45  GLY A C   
333  O O   . GLY A 45  ? 1.4027 1.1566 2.1434 -0.1291 -0.0162 -0.3529 45  GLY A O   
334  N N   . THR A 46  ? 1.3437 1.0952 2.0566 -0.1416 -0.0013 -0.3440 46  THR A N   
335  C CA  . THR A 46  ? 1.3597 1.1404 2.1128 -0.1304 -0.0090 -0.3353 46  THR A CA  
336  C C   . THR A 46  ? 1.4245 1.2048 2.1941 -0.1192 -0.0317 -0.3200 46  THR A C   
337  O O   . THR A 46  ? 1.6576 1.4169 2.4057 -0.1199 -0.0440 -0.3076 46  THR A O   
338  C CB  . THR A 46  ? 1.4680 1.2537 2.2145 -0.1338 -0.0039 -0.3266 46  THR A CB  
339  O OG1 . THR A 46  ? 1.6622 1.4455 2.3905 -0.1468 0.0175  -0.3422 46  THR A OG1 
340  C CG2 . THR A 46  ? 1.2768 1.0938 2.0649 -0.1228 -0.0097 -0.3200 46  THR A CG2 
341  N N   . ARG A 47  ? 1.4620 1.2671 2.2717 -0.1091 -0.0379 -0.3210 47  ARG A N   
342  C CA  . ARG A 47  ? 1.5178 1.3288 2.3491 -0.0994 -0.0582 -0.3060 47  ARG A CA  
343  C C   . ARG A 47  ? 1.4772 1.3156 2.3403 -0.0926 -0.0599 -0.2998 47  ARG A C   
344  O O   . ARG A 47  ? 1.7887 1.6456 2.6740 -0.0899 -0.0515 -0.3120 47  ARG A O   
345  C CB  . ARG A 47  ? 1.5975 1.4012 2.4360 -0.0959 -0.0652 -0.3155 47  ARG A CB  
346  C CG  . ARG A 47  ? 1.7932 1.6023 2.6569 -0.0869 -0.0852 -0.3060 47  ARG A CG  
347  C CD  . ARG A 47  ? 1.9805 1.7788 2.8457 -0.0843 -0.0883 -0.3206 47  ARG A CD  
348  N NE  . ARG A 47  ? 2.5022 2.3001 3.3873 -0.0768 -0.1085 -0.3132 47  ARG A NE  
349  C CZ  . ARG A 47  ? 2.7890 2.5889 3.6929 -0.0694 -0.1141 -0.3254 47  ARG A CZ  
350  N NH1 . ARG A 47  ? 2.4585 2.2659 3.3688 -0.0672 -0.1001 -0.3477 47  ARG A NH1 
351  N NH2 . ARG A 47  ? 3.0619 2.8559 3.9777 -0.0645 -0.1343 -0.3159 47  ARG A NH2 
352  N N   . LEU A 48  ? 1.3295 1.1710 2.1957 -0.0894 -0.0719 -0.2808 48  LEU A N   
353  C CA  . LEU A 48  ? 1.3476 1.2115 2.2369 -0.0841 -0.0738 -0.2722 48  LEU A CA  
354  C C   . LEU A 48  ? 1.4655 1.3387 2.3794 -0.0770 -0.0913 -0.2609 48  LEU A C   
355  O O   . LEU A 48  ? 1.6078 1.4705 2.5159 -0.0774 -0.1043 -0.2511 48  LEU A O   
356  C CB  . LEU A 48  ? 1.4187 1.2820 2.2923 -0.0863 -0.0713 -0.2607 48  LEU A CB  
357  C CG  . LEU A 48  ? 1.6666 1.5173 2.5115 -0.0948 -0.0553 -0.2694 48  LEU A CG  
358  C CD1 . LEU A 48  ? 1.7728 1.6190 2.6009 -0.0950 -0.0577 -0.2565 48  LEU A CD1 
359  C CD2 . LEU A 48  ? 1.9289 1.7963 2.7895 -0.0963 -0.0405 -0.2840 48  LEU A CD2 
360  N N   . VAL A 49  ? 1.5073 1.4001 2.4479 -0.0715 -0.0915 -0.2622 49  VAL A N   
361  C CA  . VAL A 49  ? 1.5884 1.4907 2.5501 -0.0663 -0.1068 -0.2498 49  VAL A CA  
362  C C   . VAL A 49  ? 1.7629 1.6835 2.7357 -0.0638 -0.1048 -0.2405 49  VAL A C   
363  O O   . VAL A 49  ? 1.8792 1.8103 2.8602 -0.0623 -0.0948 -0.2494 49  VAL A O   
364  C CB  . VAL A 49  ? 1.4047 1.3075 2.3862 -0.0611 -0.1139 -0.2601 49  VAL A CB  
365  C CG1 . VAL A 49  ? 1.2996 1.2103 2.3004 -0.0570 -0.1292 -0.2475 49  VAL A CG1 
366  C CG2 . VAL A 49  ? 1.5226 1.4056 2.4917 -0.0629 -0.1185 -0.2672 49  VAL A CG2 
367  N N   . VAL A 50  ? 1.7341 1.6583 2.7057 -0.0642 -0.1138 -0.2233 50  VAL A N   
368  C CA  . VAL A 50  ? 1.5999 1.5407 2.5796 -0.0619 -0.1128 -0.2132 50  VAL A CA  
369  C C   . VAL A 50  ? 1.3903 1.3401 2.3899 -0.0594 -0.1255 -0.2040 50  VAL A C   
370  O O   . VAL A 50  ? 1.1468 1.0908 2.1481 -0.0616 -0.1377 -0.1966 50  VAL A O   
371  C CB  . VAL A 50  ? 1.6126 1.5533 2.5759 -0.0637 -0.1120 -0.2022 50  VAL A CB  
372  C CG1 . VAL A 50  ? 1.6901 1.6492 2.6633 -0.0605 -0.1127 -0.1911 50  VAL A CG1 
373  C CG2 . VAL A 50  ? 1.4610 1.3887 2.4004 -0.0667 -0.1002 -0.2109 50  VAL A CG2 
374  N N   . ILE A 51  ? 1.3157 1.2782 2.3285 -0.0557 -0.1226 -0.2048 51  ILE A N   
375  C CA  . ILE A 51  ? 1.2098 1.1792 2.2383 -0.0538 -0.1336 -0.1965 51  ILE A CA  
376  C C   . ILE A 51  ? 1.1394 1.1241 2.1696 -0.0527 -0.1295 -0.1869 51  ILE A C   
377  O O   . ILE A 51  ? 1.3552 1.3461 2.3840 -0.0503 -0.1187 -0.1930 51  ILE A O   
378  C CB  . ILE A 51  ? 1.2339 1.1997 2.2772 -0.0491 -0.1370 -0.2099 51  ILE A CB  
379  C CG1 . ILE A 51  ? 1.0901 1.0416 2.1298 -0.0493 -0.1380 -0.2225 51  ILE A CG1 
380  C CG2 . ILE A 51  ? 1.1182 1.0844 2.1737 -0.0475 -0.1515 -0.2015 51  ILE A CG2 
381  C CD1 . ILE A 51  ? 1.3406 1.2915 2.3959 -0.0430 -0.1385 -0.2403 51  ILE A CD1 
382  N N   . THR A 52  ? 0.9878 0.9785 2.0200 -0.0554 -0.1381 -0.1719 52  THR A N   
383  C CA  . THR A 52  ? 1.1373 1.1431 2.1704 -0.0547 -0.1351 -0.1619 52  THR A CA  
384  C C   . THR A 52  ? 1.2608 1.2682 2.3023 -0.0578 -0.1471 -0.1516 52  THR A C   
385  O O   . THR A 52  ? 1.2604 1.2574 2.3033 -0.0618 -0.1579 -0.1492 52  THR A O   
386  C CB  . THR A 52  ? 1.1845 1.1973 2.2066 -0.0562 -0.1306 -0.1548 52  THR A CB  
387  O OG1 . THR A 52  ? 1.2467 1.2553 2.2672 -0.0612 -0.1395 -0.1485 52  THR A OG1 
388  C CG2 . THR A 52  ? 1.1965 1.2017 2.2050 -0.0542 -0.1205 -0.1646 52  THR A CG2 
389  N N   . SER A 53  ? 1.3304 1.3483 2.3750 -0.0566 -0.1455 -0.1458 53  SER A N   
390  C CA  . SER A 53  ? 1.5485 1.5671 2.5965 -0.0609 -0.1558 -0.1348 53  SER A CA  
391  C C   . SER A 53  ? 1.5911 1.6175 2.6354 -0.0694 -0.1597 -0.1213 53  SER A C   
392  O O   . SER A 53  ? 1.8104 1.8323 2.8550 -0.0767 -0.1702 -0.1124 53  SER A O   
393  C CB  . SER A 53  ? 1.6985 1.7258 2.7477 -0.0576 -0.1516 -0.1328 53  SER A CB  
394  O OG  . SER A 53  ? 1.9235 1.9432 2.9744 -0.0607 -0.1631 -0.1266 53  SER A OG  
395  N N   . GLU A 54  ? 1.5551 1.5926 2.5954 -0.0686 -0.1518 -0.1203 54  GLU A N   
396  C CA  . GLU A 54  ? 1.3288 1.3784 2.3686 -0.0750 -0.1540 -0.1103 54  GLU A CA  
397  C C   . GLU A 54  ? 1.2533 1.2978 2.2882 -0.0733 -0.1525 -0.1160 54  GLU A C   
398  O O   . GLU A 54  ? 1.1732 1.2123 2.2018 -0.0666 -0.1447 -0.1254 54  GLU A O   
399  C CB  . GLU A 54  ? 1.5504 1.6219 2.5900 -0.0730 -0.1456 -0.1046 54  GLU A CB  
400  C CG  . GLU A 54  ? 1.5376 1.6168 2.5793 -0.0782 -0.1479 -0.0955 54  GLU A CG  
401  C CD  . GLU A 54  ? 1.6040 1.6851 2.6480 -0.0907 -0.1572 -0.0850 54  GLU A CD  
402  O OE1 . GLU A 54  ? 1.7217 1.8175 2.7689 -0.0949 -0.1566 -0.0808 54  GLU A OE1 
403  O OE2 . GLU A 54  ? 1.6935 1.7603 2.7354 -0.0964 -0.1661 -0.0815 54  GLU A OE2 
404  N N   . ALA A 55  ? 1.0812 1.1269 2.1173 -0.0802 -0.1602 -0.1099 55  ALA A N   
405  C CA  . ALA A 55  ? 1.1926 1.2276 2.2225 -0.0797 -0.1623 -0.1151 55  ALA A CA  
406  C C   . ALA A 55  ? 1.3399 1.3828 2.3629 -0.0734 -0.1545 -0.1183 55  ALA A C   
407  O O   . ALA A 55  ? 1.8776 1.9406 2.9050 -0.0731 -0.1530 -0.1118 55  ALA A O   
408  C CB  . ALA A 55  ? 1.1660 1.2024 2.2001 -0.0893 -0.1736 -0.1066 55  ALA A CB  
409  N N   . VAL A 56  ? 1.1966 1.2226 2.2076 -0.0688 -0.1502 -0.1286 56  VAL A N   
410  C CA  . VAL A 56  ? 1.1104 1.1363 2.1095 -0.0637 -0.1456 -0.1317 56  VAL A CA  
411  C C   . VAL A 56  ? 1.3837 1.4173 2.3849 -0.0664 -0.1543 -0.1254 56  VAL A C   
412  O O   . VAL A 56  ? 1.3969 1.4216 2.3995 -0.0724 -0.1631 -0.1240 56  VAL A O   
413  C CB  . VAL A 56  ? 1.0898 1.0912 2.0723 -0.0620 -0.1411 -0.1435 56  VAL A CB  
414  C CG1 . VAL A 56  ? 0.8993 0.8918 1.8637 -0.0590 -0.1401 -0.1462 56  VAL A CG1 
415  C CG2 . VAL A 56  ? 1.2268 1.2244 2.2090 -0.0593 -0.1313 -0.1515 56  VAL A CG2 
416  N N   . ASP A 57  ? 1.5360 1.5857 2.5377 -0.0614 -0.1526 -0.1227 57  ASP A N   
417  C CA  . ASP A 57  ? 1.3598 1.4238 2.3684 -0.0626 -0.1610 -0.1176 57  ASP A CA  
418  C C   . ASP A 57  ? 1.2109 1.2546 2.2032 -0.0600 -0.1667 -0.1233 57  ASP A C   
419  O O   . ASP A 57  ? 0.9909 1.0185 1.9648 -0.0537 -0.1620 -0.1301 57  ASP A O   
420  C CB  . ASP A 57  ? 1.2388 1.3307 2.2570 -0.0571 -0.1575 -0.1141 57  ASP A CB  
421  C CG  . ASP A 57  ? 1.3459 1.4567 2.3742 -0.0566 -0.1658 -0.1113 57  ASP A CG  
422  O OD1 . ASP A 57  ? 1.1219 1.2180 2.1397 -0.0535 -0.1728 -0.1155 57  ASP A OD1 
423  O OD2 . ASP A 57  ? 1.7798 1.9203 2.8264 -0.0599 -0.1652 -0.1053 57  ASP A OD2 
424  N N   . PRO A 58  ? 1.1648 1.2078 2.1615 -0.0653 -0.1779 -0.1203 58  PRO A N   
425  C CA  . PRO A 58  ? 1.0331 1.0519 2.0116 -0.0639 -0.1849 -0.1257 58  PRO A CA  
426  C C   . PRO A 58  ? 0.9230 0.9385 1.8876 -0.0538 -0.1837 -0.1301 58  PRO A C   
427  O O   . PRO A 58  ? 0.7380 0.7245 1.6777 -0.0518 -0.1837 -0.1367 58  PRO A O   
428  C CB  . PRO A 58  ? 0.9561 0.9844 1.9477 -0.0706 -0.1980 -0.1199 58  PRO A CB  
429  C CG  . PRO A 58  ? 1.0787 1.1436 2.0959 -0.0736 -0.1963 -0.1119 58  PRO A CG  
430  C CD  . PRO A 58  ? 1.2145 1.2797 2.2325 -0.0738 -0.1849 -0.1115 58  PRO A CD  
431  N N   . ALA A 59  ? 0.9466 0.9905 1.9261 -0.0482 -0.1833 -0.1267 59  ALA A N   
432  C CA  . ALA A 59  ? 1.0325 1.0754 2.0010 -0.0371 -0.1847 -0.1309 59  ALA A CA  
433  C C   . ALA A 59  ? 0.9908 1.0084 1.9340 -0.0330 -0.1749 -0.1370 59  ALA A C   
434  O O   . ALA A 59  ? 0.9463 0.9381 1.8639 -0.0284 -0.1781 -0.1425 59  ALA A O   
435  C CB  . ALA A 59  ? 1.1271 1.2081 2.1187 -0.0318 -0.1826 -0.1272 59  ALA A CB  
436  N N   . THR A 60  ? 0.9389 0.9641 1.8894 -0.0356 -0.1636 -0.1359 60  THR A N   
437  C CA  . THR A 60  ? 0.8938 0.9011 1.8260 -0.0336 -0.1527 -0.1415 60  THR A CA  
438  C C   . THR A 60  ? 0.8406 0.8126 1.7475 -0.0386 -0.1521 -0.1484 60  THR A C   
439  O O   . THR A 60  ? 0.7599 0.7085 1.6405 -0.0363 -0.1486 -0.1543 60  THR A O   
440  C CB  . THR A 60  ? 0.9297 0.9511 1.8788 -0.0381 -0.1441 -0.1388 60  THR A CB  
441  O OG1 . THR A 60  ? 1.0781 1.1313 2.0501 -0.0369 -0.1455 -0.1314 60  THR A OG1 
442  C CG2 . THR A 60  ? 1.1387 1.1497 2.0761 -0.0362 -0.1325 -0.1443 60  THR A CG2 
443  N N   . LEU A 61  ? 0.8342 0.8022 1.7484 -0.0461 -0.1555 -0.1476 61  LEU A N   
444  C CA  . LEU A 61  ? 0.9833 0.9206 1.8763 -0.0518 -0.1544 -0.1547 61  LEU A CA  
445  C C   . LEU A 61  ? 0.8975 0.8107 1.7637 -0.0496 -0.1622 -0.1575 61  LEU A C   
446  O O   . LEU A 61  ? 0.7217 0.6063 1.5589 -0.0518 -0.1570 -0.1647 61  LEU A O   
447  C CB  . LEU A 61  ? 0.9996 0.9384 1.9069 -0.0588 -0.1587 -0.1530 61  LEU A CB  
448  C CG  . LEU A 61  ? 1.0403 0.9494 1.9281 -0.0644 -0.1585 -0.1610 61  LEU A CG  
449  C CD1 . LEU A 61  ? 1.0318 0.9219 1.8991 -0.0658 -0.1452 -0.1714 61  LEU A CD1 
450  C CD2 . LEU A 61  ? 1.2420 1.1594 2.1503 -0.0691 -0.1615 -0.1589 61  LEU A CD2 
451  N N   . ASP A 62  ? 0.8997 0.8251 1.7758 -0.0458 -0.1750 -0.1521 62  ASP A N   
452  C CA  . ASP A 62  ? 1.0956 1.0003 1.9496 -0.0421 -0.1865 -0.1542 62  ASP A CA  
453  C C   . ASP A 62  ? 1.0479 0.9362 1.8766 -0.0356 -0.1827 -0.1584 62  ASP A C   
454  O O   . ASP A 62  ? 0.9962 0.8490 1.7904 -0.0371 -0.1852 -0.1635 62  ASP A O   
455  C CB  . ASP A 62  ? 1.3622 1.2918 2.2392 -0.0379 -0.2005 -0.1483 62  ASP A CB  
456  C CG  . ASP A 62  ? 1.7305 1.6395 2.5888 -0.0339 -0.2162 -0.1506 62  ASP A CG  
457  O OD1 . ASP A 62  ? 1.7340 1.6045 2.5583 -0.0371 -0.2169 -0.1558 62  ASP A OD1 
458  O OD2 . ASP A 62  ? 1.8814 1.8129 2.7585 -0.0279 -0.2278 -0.1479 62  ASP A OD2 
459  N N   . TYR A 63  ? 0.9909 0.9036 1.8352 -0.0291 -0.1770 -0.1561 63  TYR A N   
460  C CA  . TYR A 63  ? 0.9992 0.8996 1.8225 -0.0222 -0.1737 -0.1595 63  TYR A CA  
461  C C   . TYR A 63  ? 1.0797 0.9479 1.8725 -0.0300 -0.1622 -0.1658 63  TYR A C   
462  O O   . TYR A 63  ? 1.1301 0.9657 1.8874 -0.0296 -0.1644 -0.1701 63  TYR A O   
463  C CB  . TYR A 63  ? 0.9740 0.9063 1.8202 -0.0159 -0.1662 -0.1564 63  TYR A CB  
464  C CG  . TYR A 63  ? 1.0725 0.9920 1.8977 -0.0099 -0.1607 -0.1600 63  TYR A CG  
465  C CD1 . TYR A 63  ? 1.1688 1.0561 1.9599 -0.0053 -0.1687 -0.1641 63  TYR A CD1 
466  C CD2 . TYR A 63  ? 1.0470 0.9834 1.8839 -0.0093 -0.1487 -0.1591 63  TYR A CD2 
467  C CE1 . TYR A 63  ? 1.2859 1.1575 2.0545 -0.0009 -0.1646 -0.1672 63  TYR A CE1 
468  C CE2 . TYR A 63  ? 1.2661 1.1892 2.0827 -0.0044 -0.1443 -0.1623 63  TYR A CE2 
469  C CZ  . TYR A 63  ? 1.2607 1.1510 2.0427 -0.0005 -0.1521 -0.1663 63  TYR A CZ  
470  O OH  . TYR A 63  ? 0.9436 0.8167 1.7021 0.0033  -0.1491 -0.1693 63  TYR A OH  
471  N N   . HIS A 64  ? 1.0395 0.9174 1.8468 -0.0375 -0.1504 -0.1667 64  HIS A N   
472  C CA  . HIS A 64  ? 1.0201 0.8763 1.8068 -0.0456 -0.1372 -0.1742 64  HIS A CA  
473  C C   . HIS A 64  ? 1.0961 0.9152 1.8491 -0.0527 -0.1405 -0.1796 64  HIS A C   
474  O O   . HIS A 64  ? 1.1322 0.9222 1.8512 -0.0576 -0.1345 -0.1854 64  HIS A O   
475  C CB  . HIS A 64  ? 0.9875 0.8647 1.8007 -0.0500 -0.1263 -0.1751 64  HIS A CB  
476  C CG  . HIS A 64  ? 1.0711 0.9740 1.9048 -0.0451 -0.1199 -0.1721 64  HIS A CG  
477  N ND1 . HIS A 64  ? 1.1004 1.0345 1.9653 -0.0406 -0.1241 -0.1644 64  HIS A ND1 
478  C CD2 . HIS A 64  ? 1.0424 0.9437 1.8695 -0.0453 -0.1091 -0.1759 64  HIS A CD2 
479  C CE1 . HIS A 64  ? 1.0642 1.0136 1.9392 -0.0375 -0.1164 -0.1635 64  HIS A CE1 
480  N NE2 . HIS A 64  ? 1.0328 0.9630 1.8862 -0.0398 -0.1078 -0.1705 64  HIS A NE2 
481  N N   . LEU A 65  ? 1.0930 0.9124 1.8541 -0.0541 -0.1504 -0.1772 65  LEU A N   
482  C CA  . LEU A 65  ? 1.1474 0.9332 1.8791 -0.0611 -0.1544 -0.1820 65  LEU A CA  
483  C C   . LEU A 65  ? 1.2805 1.0362 1.9760 -0.0578 -0.1641 -0.1825 65  LEU A C   
484  O O   . LEU A 65  ? 1.2534 0.9728 1.9103 -0.0658 -0.1599 -0.1887 65  LEU A O   
485  C CB  . LEU A 65  ? 1.1236 0.9192 1.8754 -0.0626 -0.1639 -0.1787 65  LEU A CB  
486  C CG  . LEU A 65  ? 1.2351 1.0498 2.0133 -0.0672 -0.1540 -0.1803 65  LEU A CG  
487  C CD1 . LEU A 65  ? 1.4940 1.3174 2.2918 -0.0692 -0.1645 -0.1763 65  LEU A CD1 
488  C CD2 . LEU A 65  ? 1.2243 1.0200 1.9833 -0.0752 -0.1385 -0.1912 65  LEU A CD2 
489  N N   . ARG A 66  ? 1.3448 1.1153 2.0519 -0.0464 -0.1764 -0.1768 66  ARG A N   
490  C CA  . ARG A 66  ? 1.5218 1.2614 2.1964 -0.0419 -0.1915 -0.1776 66  ARG A CA  
491  C C   . ARG A 66  ? 1.6532 1.3814 2.3074 -0.0356 -0.1904 -0.1789 66  ARG A C   
492  O O   . ARG A 66  ? 1.6680 1.3553 2.2785 -0.0387 -0.1935 -0.1825 66  ARG A O   
493  C CB  . ARG A 66  ? 1.4987 1.2539 2.1943 -0.0342 -0.2104 -0.1729 66  ARG A CB  
494  C CG  . ARG A 66  ? 1.4113 1.1736 2.1235 -0.0414 -0.2131 -0.1713 66  ARG A CG  
495  C CD  . ARG A 66  ? 1.4508 1.2190 2.1739 -0.0353 -0.2339 -0.1680 66  ARG A CD  
496  N NE  . ARG A 66  ? 1.3238 1.1185 2.0806 -0.0403 -0.2352 -0.1638 66  ARG A NE  
497  C CZ  . ARG A 66  ? 1.3144 1.0928 2.0643 -0.0475 -0.2422 -0.1642 66  ARG A CZ  
498  N NH1 . ARG A 66  ? 1.3413 1.0758 2.0500 -0.0517 -0.2467 -0.1691 66  ARG A NH1 
499  N NH2 . ARG A 66  ? 1.3096 1.1138 2.0915 -0.0514 -0.2445 -0.1597 66  ARG A NH2 
500  N N   . ASP A 67  ? 1.5932 1.3569 2.2784 -0.0276 -0.1860 -0.1756 67  ASP A N   
501  C CA  . ASP A 67  ? 1.5531 1.3124 2.2260 -0.0180 -0.1888 -0.1761 67  ASP A CA  
502  C C   . ASP A 67  ? 1.5678 1.3205 2.2287 -0.0254 -0.1706 -0.1790 67  ASP A C   
503  O O   . ASP A 67  ? 1.5283 1.2651 2.1671 -0.0215 -0.1707 -0.1806 67  ASP A O   
504  C CB  . ASP A 67  ? 1.5670 1.3659 2.2770 -0.0037 -0.1983 -0.1719 67  ASP A CB  
505  C CG  . ASP A 67  ? 1.6785 1.4868 2.4037 0.0007  -0.2153 -0.1699 67  ASP A CG  
506  O OD1 . ASP A 67  ? 1.5618 1.3398 2.2598 0.0047  -0.2309 -0.1725 67  ASP A OD1 
507  O OD2 . ASP A 67  ? 1.9906 1.8350 2.7539 -0.0005 -0.2137 -0.1658 67  ASP A OD2 
508  N N   . VAL A 68  ? 1.5249 1.2890 2.2004 -0.0360 -0.1559 -0.1805 68  VAL A N   
509  C CA  . VAL A 68  ? 1.4064 1.1658 2.0730 -0.0442 -0.1386 -0.1848 68  VAL A CA  
510  C C   . VAL A 68  ? 1.3722 1.0927 1.9999 -0.0585 -0.1320 -0.1917 68  VAL A C   
511  O O   . VAL A 68  ? 1.4407 1.1282 2.0291 -0.0627 -0.1313 -0.1947 68  VAL A O   
512  C CB  . VAL A 68  ? 1.2755 1.0723 1.9819 -0.0457 -0.1258 -0.1840 68  VAL A CB  
513  C CG1 . VAL A 68  ? 1.2090 0.9977 1.9035 -0.0549 -0.1091 -0.1904 68  VAL A CG1 
514  C CG2 . VAL A 68  ? 1.1855 1.0185 1.9252 -0.0333 -0.1306 -0.1772 68  VAL A CG2 
515  N N   . PHE A 69  ? 1.4104 1.1333 2.0470 -0.0662 -0.1279 -0.1944 69  PHE A N   
516  C CA  . PHE A 69  ? 1.4534 1.1469 2.0589 -0.0810 -0.1170 -0.2027 69  PHE A CA  
517  C C   . PHE A 69  ? 1.5413 1.1929 2.1045 -0.0845 -0.1291 -0.2033 69  PHE A C   
518  O O   . PHE A 69  ? 1.4691 1.0897 1.9971 -0.0978 -0.1206 -0.2102 69  PHE A O   
519  C CB  . PHE A 69  ? 1.4417 1.1555 2.0747 -0.0869 -0.1069 -0.2071 69  PHE A CB  
520  C CG  . PHE A 69  ? 1.3896 1.1379 2.0580 -0.0855 -0.0943 -0.2085 69  PHE A CG  
521  C CD1 . PHE A 69  ? 1.5164 1.2600 2.1742 -0.0948 -0.0776 -0.2170 69  PHE A CD1 
522  C CD2 . PHE A 69  ? 1.2969 1.0815 2.0079 -0.0759 -0.0994 -0.2017 69  PHE A CD2 
523  C CE1 . PHE A 69  ? 1.5663 1.3406 2.2568 -0.0930 -0.0677 -0.2189 69  PHE A CE1 
524  C CE2 . PHE A 69  ? 1.2077 1.0200 1.9479 -0.0746 -0.0896 -0.2029 69  PHE A CE2 
525  C CZ  . PHE A 69  ? 1.4312 1.2383 2.1618 -0.0825 -0.0743 -0.2117 69  PHE A CZ  
526  N N   . ARG A 70  ? 1.7476 1.3993 2.3151 -0.0730 -0.1487 -0.1968 70  ARG A N   
527  C CA  . ARG A 70  ? 2.1745 1.7860 2.7028 -0.0734 -0.1647 -0.1967 70  ARG A CA  
528  C C   . ARG A 70  ? 2.0120 1.6019 2.5224 -0.0856 -0.1614 -0.2015 70  ARG A C   
529  O O   . ARG A 70  ? 1.9934 1.5396 2.4555 -0.0960 -0.1609 -0.2060 70  ARG A O   
530  C CB  . ARG A 70  ? 2.4783 2.0514 2.9603 -0.0738 -0.1692 -0.1978 70  ARG A CB  
531  C CG  . ARG A 70  ? 2.7272 2.2683 3.1683 -0.0914 -0.1522 -0.2048 70  ARG A CG  
532  C CD  . ARG A 70  ? 2.8441 2.3317 3.2252 -0.0963 -0.1605 -0.2058 70  ARG A CD  
533  N NE  . ARG A 70  ? 3.0524 2.5127 3.3979 -0.1176 -0.1422 -0.2133 70  ARG A NE  
534  C CZ  . ARG A 70  ? 2.9443 2.4013 3.2769 -0.1292 -0.1243 -0.2178 70  ARG A CZ  
535  N NH1 . ARG A 70  ? 2.7053 2.1773 3.0508 -0.1213 -0.1243 -0.2147 70  ARG A NH1 
536  N NH2 . ARG A 70  ? 2.8645 2.3044 3.1719 -0.1490 -0.1064 -0.2259 70  ARG A NH2 
537  N N   . PHE A 71  ? 1.8474 1.4664 2.3951 -0.0846 -0.1602 -0.2005 71  PHE A N   
538  C CA  . PHE A 71  ? 2.0406 1.6404 2.5736 -0.0941 -0.1591 -0.2052 71  PHE A CA  
539  C C   . PHE A 71  ? 2.5264 2.0951 3.0322 -0.0911 -0.1805 -0.2022 71  PHE A C   
540  O O   . PHE A 71  ? 3.1711 2.7566 3.6989 -0.0789 -0.1974 -0.1954 71  PHE A O   
541  C CB  . PHE A 71  ? 1.7881 1.4240 2.3669 -0.0924 -0.1562 -0.2042 71  PHE A CB  
542  C CG  . PHE A 71  ? 1.6205 1.2765 2.2172 -0.0984 -0.1349 -0.2108 71  PHE A CG  
543  C CD1 . PHE A 71  ? 1.6236 1.2569 2.1922 -0.1113 -0.1195 -0.2215 71  PHE A CD1 
544  C CD2 . PHE A 71  ? 1.4540 1.1511 2.0946 -0.0913 -0.1306 -0.2069 71  PHE A CD2 
545  C CE1 . PHE A 71  ? 1.7331 1.3873 2.3209 -0.1160 -0.1006 -0.2292 71  PHE A CE1 
546  C CE2 . PHE A 71  ? 1.5209 1.2348 2.1777 -0.0958 -0.1132 -0.2136 71  PHE A CE2 
547  C CZ  . PHE A 71  ? 1.7416 1.4354 2.3738 -0.1076 -0.0985 -0.2251 71  PHE A CZ  
548  N N   . ASP A 72  ? 2.6953 2.2200 3.1541 -0.1026 -0.1795 -0.2078 72  ASP A N   
549  C CA  . ASP A 72  ? 2.7392 2.2312 3.1707 -0.1009 -0.2003 -0.2057 72  ASP A CA  
550  C C   . ASP A 72  ? 2.3577 1.8748 2.8263 -0.0966 -0.2095 -0.2026 72  ASP A C   
551  O O   . ASP A 72  ? 2.1559 1.6982 2.6529 -0.1004 -0.1966 -0.2051 72  ASP A O   
552  C CB  . ASP A 72  ? 3.0485 2.4849 3.4169 -0.1154 -0.1967 -0.2122 72  ASP A CB  
553  C CG  . ASP A 72  ? 3.3398 2.7714 3.6996 -0.1304 -0.1761 -0.2212 72  ASP A CG  
554  O OD1 . ASP A 72  ? 3.1294 2.5707 3.5076 -0.1301 -0.1795 -0.2221 72  ASP A OD1 
555  O OD2 . ASP A 72  ? 3.5836 3.0025 3.9189 -0.1424 -0.1569 -0.2280 72  ASP A OD2 
556  N N   . GLU A 73  ? 2.0790 1.5882 2.5469 -0.0884 -0.2330 -0.1976 73  GLU A N   
557  C CA  . GLU A 73  ? 1.8783 1.4154 2.3854 -0.0834 -0.2445 -0.1931 73  GLU A CA  
558  C C   . GLU A 73  ? 1.8002 1.3223 2.2976 -0.0942 -0.2393 -0.1978 73  GLU A C   
559  O O   . GLU A 73  ? 1.7213 1.2739 2.2565 -0.0940 -0.2364 -0.1962 73  GLU A O   
560  C CB  . GLU A 73  ? 1.9425 1.4748 2.4506 -0.0726 -0.2712 -0.1881 73  GLU A CB  
561  C CG  . GLU A 73  ? 2.1235 1.6949 2.6684 -0.0588 -0.2764 -0.1832 73  GLU A CG  
562  C CD  . GLU A 73  ? 2.1565 1.7815 2.7547 -0.0573 -0.2627 -0.1796 73  GLU A CD  
563  O OE1 . GLU A 73  ? 2.1298 1.7732 2.7539 -0.0615 -0.2627 -0.1777 73  GLU A OE1 
564  O OE2 . GLU A 73  ? 1.9715 1.6179 2.5839 -0.0519 -0.2534 -0.1787 73  GLU A OE2 
565  N N   . PRO A 74  ? 1.9205 1.3936 2.3653 -0.1040 -0.2390 -0.2037 74  PRO A N   
566  C CA  . PRO A 74  ? 2.0742 1.5326 2.5069 -0.1148 -0.2301 -0.2104 74  PRO A CA  
567  C C   . PRO A 74  ? 2.1382 1.6291 2.6031 -0.1185 -0.2079 -0.2154 74  PRO A C   
568  O O   . PRO A 74  ? 2.3600 1.8706 2.8546 -0.1174 -0.2100 -0.2149 74  PRO A O   
569  C CB  . PRO A 74  ? 2.1737 1.5762 2.5404 -0.1259 -0.2267 -0.2170 74  PRO A CB  
570  C CG  . PRO A 74  ? 2.0126 1.3931 2.3577 -0.1178 -0.2487 -0.2107 74  PRO A CG  
571  C CD  . PRO A 74  ? 1.9171 1.3442 2.3095 -0.1052 -0.2486 -0.2046 74  PRO A CD  
572  N N   . ALA A 75  ? 1.9906 1.4873 2.4506 -0.1226 -0.1881 -0.2202 75  ALA A N   
573  C CA  . ALA A 75  ? 2.0593 1.5805 2.5432 -0.1271 -0.1670 -0.2278 75  ALA A CA  
574  C C   . ALA A 75  ? 2.0312 1.6024 2.5740 -0.1171 -0.1682 -0.2215 75  ALA A C   
575  O O   . ALA A 75  ? 2.0333 1.6261 2.6022 -0.1185 -0.1567 -0.2267 75  ALA A O   
576  C CB  . ALA A 75  ? 2.0560 1.5668 2.5150 -0.1357 -0.1465 -0.2355 75  ALA A CB  
577  N N   . LEU A 76  ? 1.9113 1.4997 2.4739 -0.1071 -0.1831 -0.2108 76  LEU A N   
578  C CA  . LEU A 76  ? 1.9260 1.5598 2.5371 -0.0990 -0.1814 -0.2045 76  LEU A CA  
579  C C   . LEU A 76  ? 2.0178 1.6742 2.6636 -0.0990 -0.1828 -0.2038 76  LEU A C   
580  O O   . LEU A 76  ? 1.9942 1.6803 2.6716 -0.0972 -0.1728 -0.2040 76  LEU A O   
581  C CB  . LEU A 76  ? 1.8017 1.4514 2.4276 -0.0885 -0.1965 -0.1945 76  LEU A CB  
582  C CG  . LEU A 76  ? 1.7417 1.4392 2.4187 -0.0814 -0.1964 -0.1874 76  LEU A CG  
583  C CD1 . LEU A 76  ? 1.5520 1.2693 2.2420 -0.0805 -0.1789 -0.1895 76  LEU A CD1 
584  C CD2 . LEU A 76  ? 2.0072 1.7233 2.7033 -0.0722 -0.2139 -0.1786 76  LEU A CD2 
585  N N   . ALA A 77  ? 2.0444 1.6847 2.6826 -0.1010 -0.1966 -0.2026 77  ALA A N   
586  C CA  . ALA A 77  ? 2.2500 1.9058 2.9163 -0.1016 -0.2013 -0.2013 77  ALA A CA  
587  C C   . ALA A 77  ? 2.3963 2.0536 3.0661 -0.1060 -0.1837 -0.2121 77  ALA A C   
588  O O   . ALA A 77  ? 2.5526 2.2366 3.2569 -0.1035 -0.1812 -0.2110 77  ALA A O   
589  C CB  . ALA A 77  ? 2.4104 2.0413 3.0596 -0.1042 -0.2187 -0.1998 77  ALA A CB  
590  N N   . ASP A 78  ? 2.2879 1.9157 2.9205 -0.1127 -0.1722 -0.2231 78  ASP A N   
591  C CA  . ASP A 78  ? 2.2491 1.8772 2.8817 -0.1174 -0.1542 -0.2365 78  ASP A CA  
592  C C   . ASP A 78  ? 1.7749 1.4366 2.4385 -0.1136 -0.1408 -0.2374 78  ASP A C   
593  O O   . ASP A 78  ? 1.6674 1.3480 2.3580 -0.1117 -0.1348 -0.2430 78  ASP A O   
594  C CB  . ASP A 78  ? 2.4918 2.0840 3.0768 -0.1270 -0.1427 -0.2479 78  ASP A CB  
595  C CG  . ASP A 78  ? 2.6899 2.2875 3.2760 -0.1323 -0.1208 -0.2639 78  ASP A CG  
596  O OD1 . ASP A 78  ? 2.7228 2.3261 3.3249 -0.1310 -0.1204 -0.2710 78  ASP A OD1 
597  O OD2 . ASP A 78  ? 2.6744 2.2718 3.2472 -0.1374 -0.1048 -0.2695 78  ASP A OD2 
598  N N   . VAL A 79  ? 1.4687 1.1349 2.1263 -0.1120 -0.1379 -0.2323 79  VAL A N   
599  C CA  . VAL A 79  ? 1.4722 1.1670 2.1543 -0.1087 -0.1262 -0.2323 79  VAL A CA  
600  C C   . VAL A 79  ? 1.4063 1.1351 2.1339 -0.1010 -0.1342 -0.2241 79  VAL A C   
601  O O   . VAL A 79  ? 1.4888 1.2387 2.2416 -0.0992 -0.1251 -0.2287 79  VAL A O   
602  C CB  . VAL A 79  ? 1.6209 1.3090 2.2840 -0.1076 -0.1264 -0.2264 79  VAL A CB  
603  C CG1 . VAL A 79  ? 1.6358 1.3527 2.3233 -0.1036 -0.1161 -0.2251 79  VAL A CG1 
604  C CG2 . VAL A 79  ? 1.6247 1.2736 2.2373 -0.1171 -0.1198 -0.2339 79  VAL A CG2 
605  N N   . ARG A 80  ? 1.3894 1.1219 2.1255 -0.0972 -0.1517 -0.2124 80  ARG A N   
606  C CA  . ARG A 80  ? 1.4448 1.2070 2.2197 -0.0923 -0.1606 -0.2031 80  ARG A CA  
607  C C   . ARG A 80  ? 1.3994 1.1633 2.1896 -0.0940 -0.1604 -0.2089 80  ARG A C   
608  O O   . ARG A 80  ? 1.2349 1.0216 2.0539 -0.0910 -0.1585 -0.2073 80  ARG A O   
609  C CB  . ARG A 80  ? 1.4367 1.2130 2.2272 -0.0887 -0.1776 -0.1895 80  ARG A CB  
610  C CG  . ARG A 80  ? 1.2066 1.0115 2.0346 -0.0873 -0.1822 -0.1825 80  ARG A CG  
611  C CD  . ARG A 80  ? 1.2125 1.0448 2.0648 -0.0838 -0.1721 -0.1809 80  ARG A CD  
612  N NE  . ARG A 80  ? 1.4815 1.3396 2.3654 -0.0833 -0.1788 -0.1715 80  ARG A NE  
613  C CZ  . ARG A 80  ? 1.8655 1.7473 2.7683 -0.0823 -0.1865 -0.1597 80  ARG A CZ  
614  N NH1 . ARG A 80  ? 1.8767 1.7641 2.7751 -0.0797 -0.1917 -0.1548 80  ARG A NH1 
615  N NH2 . ARG A 80  ? 1.8124 1.7131 2.7393 -0.0841 -0.1895 -0.1533 80  ARG A NH2 
616  N N   . ARG A 81  ? 1.5545 1.2918 2.3228 -0.0983 -0.1634 -0.2159 81  ARG A N   
617  C CA  . ARG A 81  ? 1.6912 1.4242 2.4685 -0.0992 -0.1642 -0.2237 81  ARG A CA  
618  C C   . ARG A 81  ? 1.6593 1.4061 2.4509 -0.0973 -0.1480 -0.2354 81  ARG A C   
619  O O   . ARG A 81  ? 1.6278 1.3877 2.4451 -0.0939 -0.1518 -0.2364 81  ARG A O   
620  C CB  . ARG A 81  ? 1.9084 1.6074 2.6531 -0.1044 -0.1679 -0.2309 81  ARG A CB  
621  C CG  . ARG A 81  ? 2.1153 1.8019 2.8567 -0.1057 -0.1633 -0.2450 81  ARG A CG  
622  C CD  . ARG A 81  ? 2.2564 1.9068 2.9571 -0.1119 -0.1633 -0.2527 81  ARG A CD  
623  N NE  . ARG A 81  ? 2.3279 1.9602 3.0211 -0.1130 -0.1827 -0.2464 81  ARG A NE  
624  C CZ  . ARG A 81  ? 2.4773 2.1019 3.1770 -0.1122 -0.1900 -0.2514 81  ARG A CZ  
625  N NH1 . ARG A 81  ? 2.4687 2.1027 3.1838 -0.1090 -0.1801 -0.2637 81  ARG A NH1 
626  N NH2 . ARG A 81  ? 2.4113 2.0184 3.1025 -0.1142 -0.2083 -0.2448 81  ARG A NH2 
627  N N   . ARG A 82  ? 1.7250 1.4715 2.5032 -0.0993 -0.1317 -0.2427 82  ARG A N   
628  C CA  . ARG A 82  ? 1.5777 1.3381 2.3693 -0.0983 -0.1158 -0.2556 82  ARG A CA  
629  C C   . ARG A 82  ? 1.4464 1.2361 2.2667 -0.0930 -0.1135 -0.2488 82  ARG A C   
630  O O   . ARG A 82  ? 1.3258 1.1265 2.1520 -0.0932 -0.0991 -0.2582 82  ARG A O   
631  C CB  . ARG A 82  ? 1.3915 1.1351 2.1520 -0.1058 -0.0982 -0.2690 82  ARG A CB  
632  C CG  . ARG A 82  ? 1.4067 1.1230 2.1413 -0.1112 -0.0976 -0.2797 82  ARG A CG  
633  C CD  . ARG A 82  ? 1.4880 1.1866 2.1880 -0.1209 -0.0795 -0.2920 82  ARG A CD  
634  N NE  . ARG A 82  ? 1.4931 1.1702 2.1595 -0.1258 -0.0836 -0.2819 82  ARG A NE  
635  C CZ  . ARG A 82  ? 1.5926 1.2700 2.2458 -0.1298 -0.0736 -0.2808 82  ARG A CZ  
636  N NH1 . ARG A 82  ? 1.5027 1.2028 2.1747 -0.1302 -0.0584 -0.2885 82  ARG A NH1 
637  N NH2 . ARG A 82  ? 1.8801 1.5332 2.4999 -0.1334 -0.0797 -0.2727 82  ARG A NH2 
638  N N   . LEU A 83  ? 1.3804 1.1828 2.2178 -0.0892 -0.1274 -0.2334 83  LEU A N   
639  C CA  . LEU A 83  ? 1.3668 1.1953 2.2284 -0.0846 -0.1266 -0.2253 83  LEU A CA  
640  C C   . LEU A 83  ? 1.4325 1.2741 2.3207 -0.0816 -0.1407 -0.2161 83  LEU A C   
641  O O   . LEU A 83  ? 1.6245 1.4600 2.5112 -0.0835 -0.1543 -0.2073 83  LEU A O   
642  C CB  . LEU A 83  ? 1.4344 1.2662 2.2849 -0.0843 -0.1263 -0.2155 83  LEU A CB  
643  C CG  . LEU A 83  ? 1.3727 1.2314 2.2464 -0.0793 -0.1257 -0.2066 83  LEU A CG  
644  C CD1 . LEU A 83  ? 1.6693 1.5379 2.5521 -0.0782 -0.1116 -0.2166 83  LEU A CD1 
645  C CD2 . LEU A 83  ? 1.1672 1.0279 2.0297 -0.0775 -0.1279 -0.1976 83  LEU A CD2 
646  N N   . THR A 84  ? 1.3543 1.2135 2.2660 -0.0778 -0.1378 -0.2180 84  THR A N   
647  C CA  . THR A 84  ? 1.4039 1.2741 2.3386 -0.0759 -0.1505 -0.2091 84  THR A CA  
648  C C   . THR A 84  ? 1.3187 1.2117 2.2707 -0.0727 -0.1473 -0.2019 84  THR A C   
649  O O   . THR A 84  ? 1.1615 1.0624 2.1171 -0.0699 -0.1354 -0.2098 84  THR A O   
650  C CB  . THR A 84  ? 1.4390 1.3008 2.3831 -0.0737 -0.1549 -0.2198 84  THR A CB  
651  O OG1 . THR A 84  ? 1.6693 1.5096 2.5930 -0.0764 -0.1537 -0.2290 84  THR A OG1 
652  C CG2 . THR A 84  ? 1.3576 1.2205 2.3162 -0.0742 -0.1722 -0.2089 84  THR A CG2 
653  N N   . LEU A 85  ? 1.2504 1.1542 2.2139 -0.0741 -0.1585 -0.1872 85  LEU A N   
654  C CA  . LEU A 85  ? 1.3672 1.2921 2.3452 -0.0722 -0.1570 -0.1782 85  LEU A CA  
655  C C   . LEU A 85  ? 1.3142 1.2429 2.3088 -0.0734 -0.1688 -0.1717 85  LEU A C   
656  O O   . LEU A 85  ? 1.5167 1.4397 2.5115 -0.0784 -0.1808 -0.1641 85  LEU A O   
657  C CB  . LEU A 85  ? 1.4290 1.3663 2.4033 -0.0736 -0.1578 -0.1662 85  LEU A CB  
658  C CG  . LEU A 85  ? 1.4739 1.4034 2.4280 -0.0727 -0.1513 -0.1695 85  LEU A CG  
659  C CD1 . LEU A 85  ? 1.3722 1.3191 2.3300 -0.0717 -0.1546 -0.1577 85  LEU A CD1 
660  C CD2 . LEU A 85  ? 1.3087 1.2318 2.2505 -0.0701 -0.1368 -0.1810 85  LEU A CD2 
661  N N   . LEU A 86  ? 1.2580 1.1942 2.2645 -0.0694 -0.1658 -0.1750 86  LEU A N   
662  C CA  . LEU A 86  ? 1.1506 1.0836 2.1692 -0.0696 -0.1775 -0.1723 86  LEU A CA  
663  C C   . LEU A 86  ? 1.2359 1.1846 2.2646 -0.0680 -0.1756 -0.1655 86  LEU A C   
664  O O   . LEU A 86  ? 1.1401 1.0998 2.1704 -0.0636 -0.1638 -0.1700 86  LEU A O   
665  C CB  . LEU A 86  ? 1.1118 1.0306 2.1332 -0.0642 -0.1779 -0.1891 86  LEU A CB  
666  C CG  . LEU A 86  ? 1.2103 1.1128 2.2190 -0.0654 -0.1770 -0.1984 86  LEU A CG  
667  C CD1 . LEU A 86  ? 1.5024 1.3991 2.5147 -0.0591 -0.1700 -0.2185 86  LEU A CD1 
668  C CD2 . LEU A 86  ? 1.4569 1.3445 2.4624 -0.0703 -0.1938 -0.1908 86  LEU A CD2 
669  N N   . THR A 87  ? 1.2670 1.2144 2.3009 -0.0725 -0.1882 -0.1547 87  THR A N   
670  C CA  . THR A 87  ? 1.4593 1.4178 2.4998 -0.0728 -0.1891 -0.1466 87  THR A CA  
671  C C   . THR A 87  ? 1.4211 1.3643 2.4665 -0.0721 -0.2031 -0.1479 87  THR A C   
672  O O   . THR A 87  ? 1.6830 1.6110 2.7249 -0.0773 -0.2165 -0.1439 87  THR A O   
673  C CB  . THR A 87  ? 1.5462 1.5200 2.5844 -0.0810 -0.1895 -0.1302 87  THR A CB  
674  O OG1 . THR A 87  ? 2.1778 2.1645 3.2126 -0.0770 -0.1760 -0.1334 87  THR A OG1 
675  C CG2 . THR A 87  ? 1.6009 1.5848 2.6428 -0.0831 -0.1906 -0.1210 87  THR A CG2 
676  N N   . PRO A 88  ? 1.2817 1.2269 2.3345 -0.0651 -0.2012 -0.1548 88  PRO A N   
677  C CA  . PRO A 88  ? 1.1995 1.1313 2.2559 -0.0639 -0.2159 -0.1538 88  PRO A CA  
678  C C   . PRO A 88  ? 1.3595 1.2864 2.4076 -0.0754 -0.2274 -0.1355 88  PRO A C   
679  O O   . PRO A 88  ? 1.5636 1.5070 2.6079 -0.0825 -0.2205 -0.1232 88  PRO A O   
680  C CB  . PRO A 88  ? 1.0994 1.0422 2.1632 -0.0570 -0.2087 -0.1587 88  PRO A CB  
681  C CG  . PRO A 88  ? 1.3439 1.2994 2.4110 -0.0517 -0.1914 -0.1708 88  PRO A CG  
682  C CD  . PRO A 88  ? 1.3064 1.2657 2.3634 -0.0582 -0.1856 -0.1639 88  PRO A CD  
683  N N   . ALA A 89  ? 1.3159 1.2195 2.3609 -0.0770 -0.2454 -0.1350 89  ALA A N   
684  C CA  . ALA A 89  ? 1.4303 1.3230 2.4643 -0.0897 -0.2587 -0.1184 89  ALA A CA  
685  C C   . ALA A 89  ? 1.6080 1.5090 2.6390 -0.0929 -0.2570 -0.1089 89  ALA A C   
686  O O   . ALA A 89  ? 1.8569 1.7582 2.8777 -0.1062 -0.2612 -0.0932 89  ALA A O   
687  C CB  . ALA A 89  ? 1.6155 1.4766 2.6445 -0.0892 -0.2796 -0.1221 89  ALA A CB  
688  N N   . SER A 90  ? 1.6932 1.6011 2.7324 -0.0817 -0.2504 -0.1185 90  SER A N   
689  C CA  . SER A 90  ? 1.7302 1.6458 2.7655 -0.0836 -0.2478 -0.1104 90  SER A CA  
690  C C   . SER A 90  ? 1.7025 1.6476 2.7385 -0.0868 -0.2287 -0.1039 90  SER A C   
691  O O   . SER A 90  ? 1.6599 1.6197 2.7034 -0.0802 -0.2154 -0.1124 90  SER A O   
692  C CB  . SER A 90  ? 1.8940 1.8035 2.9373 -0.0710 -0.2510 -0.1228 90  SER A CB  
693  O OG  . SER A 90  ? 2.1919 2.1083 3.2295 -0.0732 -0.2481 -0.1145 90  SER A OG  
694  N N   . ARG A 91  ? 1.6681 1.6204 2.6946 -0.0973 -0.2281 -0.0891 91  ARG A N   
695  C CA  . ARG A 91  ? 1.8563 1.8369 2.8837 -0.0993 -0.2114 -0.0835 91  ARG A CA  
696  C C   . ARG A 91  ? 1.8663 1.8510 2.8889 -0.0973 -0.2082 -0.0804 91  ARG A C   
697  O O   . ARG A 91  ? 1.8135 1.8198 2.8342 -0.0993 -0.1960 -0.0747 91  ARG A O   
698  C CB  . ARG A 91  ? 1.9731 1.9644 2.9962 -0.1133 -0.2109 -0.0711 91  ARG A CB  
699  C CG  . ARG A 91  ? 2.0090 2.0302 3.0383 -0.1121 -0.1949 -0.0703 91  ARG A CG  
700  C CD  . ARG A 91  ? 2.3020 2.3353 3.3307 -0.1257 -0.1963 -0.0597 91  ARG A CD  
701  N NE  . ARG A 91  ? 2.5554 2.6197 3.5906 -0.1240 -0.1823 -0.0586 91  ARG A NE  
702  C CZ  . ARG A 91  ? 2.6269 2.7143 3.6621 -0.1331 -0.1764 -0.0493 91  ARG A CZ  
703  N NH1 . ARG A 91  ? 2.9397 3.0222 3.9664 -0.1472 -0.1824 -0.0387 91  ARG A NH1 
704  N NH2 . ARG A 91  ? 2.4813 2.5962 3.5242 -0.1283 -0.1649 -0.0511 91  ARG A NH2 
705  N N   . ALA A 92  ? 1.7485 1.7119 2.7692 -0.0922 -0.2200 -0.0852 92  ALA A N   
706  C CA  . ALA A 92  ? 1.6780 1.6425 2.6951 -0.0878 -0.2181 -0.0852 92  ALA A CA  
707  C C   . ALA A 92  ? 1.9527 1.9360 2.9816 -0.0756 -0.2027 -0.0966 92  ALA A C   
708  O O   . ALA A 92  ? 1.9461 1.9314 2.9862 -0.0684 -0.1988 -0.1083 92  ALA A O   
709  C CB  . ALA A 92  ? 1.4327 1.3688 2.4467 -0.0839 -0.2367 -0.0894 92  ALA A CB  
710  N N   . ALA A 93  ? 2.1908 2.1862 3.2150 -0.0742 -0.1940 -0.0930 93  ALA A N   
711  C CA  . ALA A 93  ? 2.0523 2.0644 3.0839 -0.0644 -0.1795 -0.1019 93  ALA A CA  
712  C C   . ALA A 93  ? 1.7370 1.7384 2.7775 -0.0540 -0.1846 -0.1152 93  ALA A C   
713  O O   . ALA A 93  ? 1.4943 1.4924 2.5309 -0.0514 -0.1871 -0.1145 93  ALA A O   
714  C CB  . ALA A 93  ? 2.0833 2.1125 3.1057 -0.0668 -0.1687 -0.0932 93  ALA A CB  
715  N N   . ARG A 94  ? 1.7152 1.7118 2.7681 -0.0484 -0.1862 -0.1282 94  ARG A N   
716  C CA  . ARG A 94  ? 1.5851 1.5760 2.6511 -0.0385 -0.1900 -0.1437 94  ARG A CA  
717  C C   . ARG A 94  ? 1.6477 1.6496 2.7242 -0.0338 -0.1771 -0.1573 94  ARG A C   
718  O O   . ARG A 94  ? 2.0443 2.0518 3.1164 -0.0380 -0.1696 -0.1540 94  ARG A O   
719  C CB  . ARG A 94  ? 1.6300 1.5987 2.6998 -0.0373 -0.2096 -0.1473 94  ARG A CB  
720  C CG  . ARG A 94  ? 1.7864 1.7382 2.8402 -0.0448 -0.2242 -0.1325 94  ARG A CG  
721  C CD  . ARG A 94  ? 1.6959 1.6216 2.7510 -0.0432 -0.2454 -0.1366 94  ARG A CD  
722  N NE  . ARG A 94  ? 1.8446 1.7723 2.9207 -0.0299 -0.2466 -0.1571 94  ARG A NE  
723  C CZ  . ARG A 94  ? 1.8707 1.7803 2.9555 -0.0226 -0.2637 -0.1681 94  ARG A CZ  
724  N NH1 . ARG A 94  ? 1.9232 1.8064 2.9943 -0.0274 -0.2834 -0.1594 94  ARG A NH1 
725  N NH2 . ARG A 94  ? 2.0254 1.9437 3.1320 -0.0110 -0.2610 -0.1883 94  ARG A NH2 
726  N N   . PRO A 95  ? 1.4941 1.4994 2.5838 -0.0260 -0.1739 -0.1729 95  PRO A N   
727  C CA  . PRO A 95  ? 1.4912 1.5049 2.5886 -0.0236 -0.1613 -0.1867 95  PRO A CA  
728  C C   . PRO A 95  ? 1.2862 1.2918 2.3844 -0.0259 -0.1651 -0.1892 95  PRO A C   
729  O O   . PRO A 95  ? 1.0217 1.0133 2.1225 -0.0256 -0.1803 -0.1881 95  PRO A O   
730  C CB  . PRO A 95  ? 1.6160 1.6324 2.7306 -0.0161 -0.1627 -0.2035 95  PRO A CB  
731  C CG  . PRO A 95  ? 1.8081 1.8236 2.9180 -0.0149 -0.1684 -0.1951 95  PRO A CG  
732  C CD  . PRO A 95  ? 1.6237 1.6258 2.7202 -0.0202 -0.1812 -0.1781 95  PRO A CD  
733  N N   . LEU A 96  ? 1.4627 1.4746 2.5557 -0.0286 -0.1521 -0.1919 96  LEU A N   
734  C CA  . LEU A 96  ? 1.2534 1.2576 2.3424 -0.0321 -0.1545 -0.1913 96  LEU A CA  
735  C C   . LEU A 96  ? 1.1807 1.1759 2.2828 -0.0271 -0.1614 -0.2075 96  LEU A C   
736  O O   . LEU A 96  ? 1.0029 0.9853 2.1034 -0.0286 -0.1724 -0.2052 96  LEU A O   
737  C CB  . LEU A 96  ? 1.3456 1.3566 2.4237 -0.0357 -0.1397 -0.1911 96  LEU A CB  
738  C CG  . LEU A 96  ? 1.3484 1.3503 2.4216 -0.0388 -0.1409 -0.1937 96  LEU A CG  
739  C CD1 . LEU A 96  ? 1.2410 1.2359 2.3097 -0.0437 -0.1537 -0.1793 96  LEU A CD1 
740  C CD2 . LEU A 96  ? 1.6938 1.6992 2.7539 -0.0417 -0.1273 -0.1946 96  LEU A CD2 
741  N N   . ASP A 97  ? 1.1869 1.1900 2.3018 -0.0216 -0.1542 -0.2243 97  ASP A N   
742  C CA  . ASP A 97  ? 1.1518 1.1514 2.2822 -0.0158 -0.1581 -0.2432 97  ASP A CA  
743  C C   . ASP A 97  ? 1.1619 1.1470 2.3004 -0.0104 -0.1799 -0.2425 97  ASP A C   
744  O O   . ASP A 97  ? 1.0475 1.0207 2.1894 -0.0079 -0.1891 -0.2493 97  ASP A O   
745  C CB  . ASP A 97  ? 1.1093 1.1242 2.2529 -0.0125 -0.1449 -0.2612 97  ASP A CB  
746  C CG  . ASP A 97  ? 1.4057 1.4298 2.5549 -0.0102 -0.1447 -0.2586 97  ASP A CG  
747  O OD1 . ASP A 97  ? 1.2287 1.2463 2.3711 -0.0104 -0.1554 -0.2432 97  ASP A OD1 
748  O OD2 . ASP A 97  ? 1.7719 1.8094 2.9315 -0.0091 -0.1337 -0.2723 97  ASP A OD2 
749  N N   . SER A 98  ? 1.2469 1.2309 2.3858 -0.0090 -0.1884 -0.2340 98  SER A N   
750  C CA  . SER A 98  ? 1.2300 1.1963 2.3719 -0.0047 -0.2107 -0.2314 98  SER A CA  
751  C C   . SER A 98  ? 1.3608 1.3087 2.4874 -0.0113 -0.2220 -0.2178 98  SER A C   
752  O O   . SER A 98  ? 1.5181 1.4479 2.6478 -0.0074 -0.2387 -0.2230 98  SER A O   
753  C CB  . SER A 98  ? 1.2025 1.1685 2.3401 -0.0048 -0.2163 -0.2211 98  SER A CB  
754  O OG  . SER A 98  ? 1.5833 1.5645 2.7362 0.0014  -0.2088 -0.2344 98  SER A OG  
755  N N   . LEU A 99  ? 1.5132 1.4665 2.6238 -0.0213 -0.2130 -0.2009 99  LEU A N   
756  C CA  . LEU A 99  ? 1.3923 1.3328 2.4884 -0.0302 -0.2212 -0.1863 99  LEU A CA  
757  C C   . LEU A 99  ? 1.3124 1.2439 2.4115 -0.0285 -0.2237 -0.1967 99  LEU A C   
758  O O   . LEU A 99  ? 1.3858 1.2971 2.4798 -0.0303 -0.2401 -0.1934 99  LEU A O   
759  C CB  . LEU A 99  ? 1.3921 1.3465 2.4753 -0.0397 -0.2087 -0.1701 99  LEU A CB  
760  C CG  . LEU A 99  ? 1.4766 1.4400 2.5544 -0.0418 -0.2055 -0.1593 99  LEU A CG  
761  C CD1 . LEU A 99  ? 1.2847 1.2640 2.3518 -0.0495 -0.1929 -0.1458 99  LEU A CD1 
762  C CD2 . LEU A 99  ? 1.7320 1.6766 2.8031 -0.0448 -0.2243 -0.1506 99  LEU A CD2 
763  N N   . VAL A 100 ? 1.1329 1.0777 2.2380 -0.0256 -0.2074 -0.2093 100 VAL A N   
764  C CA  . VAL A 100 ? 1.0764 1.0146 2.1828 -0.0241 -0.2060 -0.2211 100 VAL A CA  
765  C C   . VAL A 100 ? 1.3084 1.2320 2.4273 -0.0147 -0.2219 -0.2359 100 VAL A C   
766  O O   . VAL A 100 ? 1.6468 1.5528 2.7612 -0.0149 -0.2334 -0.2373 100 VAL A O   
767  C CB  . VAL A 100 ? 1.0296 0.9843 2.1397 -0.0226 -0.1850 -0.2346 100 VAL A CB  
768  C CG1 . VAL A 100 ? 0.9464 0.8944 2.0603 -0.0192 -0.1833 -0.2519 100 VAL A CG1 
769  C CG2 . VAL A 100 ? 1.1053 1.0701 2.2004 -0.0307 -0.1706 -0.2220 100 VAL A CG2 
770  N N   . LEU A 101 ? 1.4290 1.3602 2.5639 -0.0061 -0.2231 -0.2475 101 LEU A N   
771  C CA  . LEU A 101 ? 1.3087 1.2295 2.4596 0.0054  -0.2387 -0.2645 101 LEU A CA  
772  C C   . LEU A 101 ? 1.4310 1.3236 2.5710 0.0044  -0.2639 -0.2527 101 LEU A C   
773  O O   . LEU A 101 ? 1.5005 1.3752 2.6429 0.0102  -0.2781 -0.2622 101 LEU A O   
774  C CB  . LEU A 101 ? 1.2406 1.1764 2.4105 0.0138  -0.2365 -0.2764 101 LEU A CB  
775  C CG  . LEU A 101 ? 1.3886 1.3265 2.5830 0.0275  -0.2436 -0.3027 101 LEU A CG  
776  C CD1 . LEU A 101 ? 1.4134 1.3581 2.6132 0.0287  -0.2313 -0.3198 101 LEU A CD1 
777  C CD2 . LEU A 101 ? 1.6194 1.5788 2.8326 0.0327  -0.2361 -0.3132 101 LEU A CD2 
778  N N   . GLU A 102 ? 1.5318 1.4199 2.6581 -0.0035 -0.2686 -0.2323 102 GLU A N   
779  C CA  . GLU A 102 ? 1.5533 1.4137 2.6641 -0.0084 -0.2911 -0.2179 102 GLU A CA  
780  C C   . GLU A 102 ? 1.5714 1.4159 2.6696 -0.0154 -0.2970 -0.2121 102 GLU A C   
781  O O   . GLU A 102 ? 1.7671 1.5844 2.8599 -0.0131 -0.3184 -0.2134 102 GLU A O   
782  C CB  . GLU A 102 ? 1.7058 1.5646 2.8015 -0.0181 -0.2935 -0.1970 102 GLU A CB  
783  C CG  . GLU A 102 ? 2.0498 1.9130 3.1552 -0.0099 -0.2969 -0.2029 102 GLU A CG  
784  C CD  . GLU A 102 ? 2.5244 2.3908 3.6132 -0.0205 -0.2934 -0.1825 102 GLU A CD  
785  O OE1 . GLU A 102 ? 2.4413 2.3074 3.5133 -0.0338 -0.2892 -0.1651 102 GLU A OE1 
786  O OE2 . GLU A 102 ? 2.8290 2.6996 3.9225 -0.0153 -0.2945 -0.1850 102 GLU A OE2 
787  N N   . ASP A 103 ? 1.5713 1.4303 2.6651 -0.0225 -0.2796 -0.2083 103 ASP A N   
788  C CA  . ASP A 103 ? 1.7591 1.6040 2.8412 -0.0293 -0.2847 -0.2033 103 ASP A CA  
789  C C   . ASP A 103 ? 1.8547 1.6925 2.9468 -0.0186 -0.2867 -0.2251 103 ASP A C   
790  O O   . ASP A 103 ? 1.6087 1.4622 2.7063 -0.0166 -0.2691 -0.2361 103 ASP A O   
791  C CB  . ASP A 103 ? 1.8790 1.7406 2.9513 -0.0412 -0.2684 -0.1892 103 ASP A CB  
792  C CG  . ASP A 103 ? 1.8617 1.7118 2.9217 -0.0501 -0.2728 -0.1817 103 ASP A CG  
793  O OD1 . ASP A 103 ? 1.9809 1.8068 3.0372 -0.0483 -0.2896 -0.1862 103 ASP A OD1 
794  O OD2 . ASP A 103 ? 1.8035 1.6686 2.8576 -0.0584 -0.2603 -0.1720 103 ASP A OD2 
795  N N   . GLU A 104 ? 2.0002 1.8120 3.0922 -0.0122 -0.3091 -0.2313 104 GLU A N   
796  C CA  . GLU A 104 ? 1.9872 1.7913 3.0905 0.0003  -0.3138 -0.2544 104 GLU A CA  
797  C C   . GLU A 104 ? 1.9007 1.7060 2.9958 -0.0049 -0.3027 -0.2564 104 GLU A C   
798  O O   . GLU A 104 ? 1.6391 1.4556 2.7446 0.0024  -0.2901 -0.2758 104 GLU A O   
799  C CB  . GLU A 104 ? 1.9548 1.7246 3.0525 0.0057  -0.3435 -0.2554 104 GLU A CB  
800  C CG  . GLU A 104 ? 2.1425 1.9074 3.2489 0.0140  -0.3571 -0.2581 104 GLU A CG  
801  C CD  . GLU A 104 ? 2.3263 2.1109 3.4610 0.0311  -0.3504 -0.2844 104 GLU A CD  
802  O OE1 . GLU A 104 ? 2.2410 2.0575 3.3882 0.0306  -0.3269 -0.2894 104 GLU A OE1 
803  O OE2 . GLU A 104 ? 2.7218 2.4896 3.8663 0.0451  -0.3696 -0.3011 104 GLU A OE2 
804  N N   . ALA A 105 ? 1.9763 1.7682 3.0520 -0.0181 -0.3091 -0.2367 105 ALA A N   
805  C CA  . ALA A 105 ? 2.0754 1.8624 3.1401 -0.0242 -0.3038 -0.2358 105 ALA A CA  
806  C C   . ALA A 105 ? 1.8665 1.6805 2.9350 -0.0255 -0.2773 -0.2413 105 ALA A C   
807  O O   . ALA A 105 ? 1.7391 1.5526 2.8066 -0.0223 -0.2689 -0.2552 105 ALA A O   
808  C CB  . ALA A 105 ? 2.2985 2.0723 3.3447 -0.0398 -0.3143 -0.2120 105 ALA A CB  
809  N N   . LEU A 106 ? 1.7083 1.5431 2.7785 -0.0306 -0.2652 -0.2301 106 LEU A N   
810  C CA  . LEU A 106 ? 1.6225 1.4805 2.6930 -0.0328 -0.2416 -0.2327 106 LEU A CA  
811  C C   . LEU A 106 ? 1.5463 1.4141 2.6303 -0.0222 -0.2296 -0.2572 106 LEU A C   
812  O O   . LEU A 106 ? 1.5109 1.3838 2.5895 -0.0236 -0.2147 -0.2663 106 LEU A O   
813  C CB  . LEU A 106 ? 1.6752 1.5521 2.7458 -0.0383 -0.2330 -0.2177 106 LEU A CB  
814  C CG  . LEU A 106 ? 1.6064 1.5057 2.6776 -0.0387 -0.2101 -0.2215 106 LEU A CG  
815  C CD1 . LEU A 106 ? 1.5390 1.4380 2.5970 -0.0440 -0.1993 -0.2222 106 LEU A CD1 
816  C CD2 . LEU A 106 ? 1.4331 1.3478 2.5032 -0.0432 -0.2051 -0.2062 106 LEU A CD2 
817  N N   . VAL A 107 ? 1.4233 1.2930 2.5240 -0.0124 -0.2368 -0.2677 107 VAL A N   
818  C CA  . VAL A 107 ? 1.3580 1.2410 2.4766 -0.0020 -0.2265 -0.2925 107 VAL A CA  
819  C C   . VAL A 107 ? 1.4211 1.2929 2.5380 0.0021  -0.2269 -0.3097 107 VAL A C   
820  O O   . VAL A 107 ? 1.1406 1.0254 2.2604 0.0029  -0.2086 -0.3257 107 VAL A O   
821  C CB  . VAL A 107 ? 1.2475 1.1356 2.3874 0.0092  -0.2362 -0.3031 107 VAL A CB  
822  C CG1 . VAL A 107 ? 1.2945 1.2049 2.4545 0.0169  -0.2199 -0.3282 107 VAL A CG1 
823  C CG2 . VAL A 107 ? 1.1667 1.0612 2.3055 0.0051  -0.2386 -0.2856 107 VAL A CG2 
824  N N   . GLU A 108 ? 1.5243 1.3706 2.6345 0.0040  -0.2481 -0.3059 108 GLU A N   
825  C CA  . GLU A 108 ? 1.5955 1.4263 2.7019 0.0087  -0.2527 -0.3209 108 GLU A CA  
826  C C   . GLU A 108 ? 1.5984 1.4314 2.6871 -0.0009 -0.2355 -0.3186 108 GLU A C   
827  O O   . GLU A 108 ? 1.5811 1.4174 2.6704 0.0025  -0.2237 -0.3379 108 GLU A O   
828  C CB  . GLU A 108 ? 1.7107 1.5102 2.8060 0.0082  -0.2797 -0.3096 108 GLU A CB  
829  C CG  . GLU A 108 ? 2.3030 2.0894 3.4129 0.0221  -0.3008 -0.3219 108 GLU A CG  
830  C CD  . GLU A 108 ? 2.6797 2.4665 3.8037 0.0366  -0.2999 -0.3517 108 GLU A CD  
831  O OE1 . GLU A 108 ? 3.0683 2.8474 4.1807 0.0340  -0.2940 -0.3576 108 GLU A OE1 
832  O OE2 . GLU A 108 ? 2.3798 2.1746 3.5263 0.0504  -0.3055 -0.3695 108 GLU A OE2 
833  N N   . THR A 109 ? 1.4329 1.2641 2.5056 -0.0131 -0.2348 -0.2952 109 THR A N   
834  C CA  . THR A 109 ? 1.3482 1.1790 2.4021 -0.0227 -0.2220 -0.2896 109 THR A CA  
835  C C   . THR A 109 ? 1.3617 1.2128 2.4177 -0.0226 -0.1972 -0.3029 109 THR A C   
836  O O   . THR A 109 ? 1.3237 1.1702 2.3676 -0.0249 -0.1863 -0.3135 109 THR A O   
837  C CB  . THR A 109 ? 1.3714 1.2005 2.4115 -0.0346 -0.2261 -0.2637 109 THR A CB  
838  O OG1 . THR A 109 ? 1.7172 1.5295 2.7569 -0.0360 -0.2484 -0.2520 109 THR A OG1 
839  C CG2 . THR A 109 ? 1.3633 1.1831 2.3835 -0.0423 -0.2210 -0.2603 109 THR A CG2 
840  N N   . LEU A 110 ? 1.4446 1.3161 2.5139 -0.0210 -0.1891 -0.3018 110 LEU A N   
841  C CA  . LEU A 110 ? 1.4537 1.3451 2.5254 -0.0223 -0.1662 -0.3130 110 LEU A CA  
842  C C   . LEU A 110 ? 1.3750 1.2694 2.4557 -0.0159 -0.1577 -0.3403 110 LEU A C   
843  O O   . LEU A 110 ? 1.0621 0.9600 2.1310 -0.0212 -0.1395 -0.3503 110 LEU A O   
844  C CB  . LEU A 110 ? 1.3938 1.3051 2.4800 -0.0207 -0.1617 -0.3083 110 LEU A CB  
845  C CG  . LEU A 110 ? 1.3379 1.2521 2.4143 -0.0279 -0.1639 -0.2836 110 LEU A CG  
846  C CD1 . LEU A 110 ? 1.1374 1.0676 2.2285 -0.0247 -0.1632 -0.2799 110 LEU A CD1 
847  C CD2 . LEU A 110 ? 1.2967 1.2128 2.3525 -0.0369 -0.1488 -0.2770 110 LEU A CD2 
848  N N   . ARG A 111 ? 1.5501 1.4423 2.6508 -0.0045 -0.1717 -0.3523 111 ARG A N   
849  C CA  . ARG A 111 ? 1.6751 1.5729 2.7902 0.0043  -0.1663 -0.3806 111 ARG A CA  
850  C C   . ARG A 111 ? 1.6417 1.5229 2.7363 0.0005  -0.1618 -0.3878 111 ARG A C   
851  O O   . ARG A 111 ? 1.5349 1.4255 2.6278 -0.0010 -0.1432 -0.4070 111 ARG A O   
852  C CB  . ARG A 111 ? 1.6480 1.5397 2.7851 0.0186  -0.1885 -0.3897 111 ARG A CB  
853  C CG  . ARG A 111 ? 1.8646 1.7630 3.0197 0.0303  -0.1855 -0.4210 111 ARG A CG  
854  C CD  . ARG A 111 ? 1.8582 1.7504 3.0367 0.0470  -0.2089 -0.4332 111 ARG A CD  
855  N NE  . ARG A 111 ? 2.0425 1.9009 3.2069 0.0498  -0.2348 -0.4218 111 ARG A NE  
856  C CZ  . ARG A 111 ? 2.2227 2.0594 3.3687 0.0482  -0.2391 -0.4234 111 ARG A CZ  
857  N NH1 . ARG A 111 ? 2.3623 2.2064 3.5016 0.0451  -0.2195 -0.4386 111 ARG A NH1 
858  N NH2 . ARG A 111 ? 2.1311 1.9367 3.2637 0.0488  -0.2639 -0.4097 111 ARG A NH2 
859  N N   . ARG A 112 ? 1.6992 1.5554 2.7776 -0.0019 -0.1792 -0.3718 112 ARG A N   
860  C CA  . ARG A 112 ? 1.9235 1.7590 2.9802 -0.0055 -0.1795 -0.3754 112 ARG A CA  
861  C C   . ARG A 112 ? 1.9378 1.7778 2.9727 -0.0175 -0.1573 -0.3736 112 ARG A C   
862  O O   . ARG A 112 ? 2.0590 1.8942 3.0823 -0.0191 -0.1454 -0.3901 112 ARG A O   
863  C CB  . ARG A 112 ? 2.1122 1.9214 3.1565 -0.0077 -0.2034 -0.3561 112 ARG A CB  
864  C CG  . ARG A 112 ? 1.9802 1.7813 3.0432 0.0040  -0.2256 -0.3606 112 ARG A CG  
865  C CD  . ARG A 112 ? 1.8866 1.6601 2.9368 0.0006  -0.2504 -0.3420 112 ARG A CD  
866  N NE  . ARG A 112 ? 2.1996 1.9500 3.2320 -0.0002 -0.2552 -0.3483 112 ARG A NE  
867  C CZ  . ARG A 112 ? 2.6149 2.3410 3.6287 -0.0078 -0.2713 -0.3317 112 ARG A CZ  
868  N NH1 . ARG A 112 ? 2.6490 2.3733 3.6593 -0.0169 -0.2816 -0.3071 112 ARG A NH1 
869  N NH2 . ARG A 112 ? 2.9712 2.6758 3.9696 -0.0072 -0.2761 -0.3402 112 ARG A NH2 
870  N N   . ALA A 113 ? 1.7769 1.6247 2.8050 -0.0257 -0.1526 -0.3540 113 ALA A N   
871  C CA  . ALA A 113 ? 1.8505 1.6996 2.8558 -0.0369 -0.1347 -0.3492 113 ALA A CA  
872  C C   . ALA A 113 ? 1.7175 1.5824 2.7259 -0.0379 -0.1116 -0.3715 113 ALA A C   
873  O O   . ALA A 113 ? 1.6716 1.5277 2.6571 -0.0454 -0.0978 -0.3796 113 ALA A O   
874  C CB  . ALA A 113 ? 2.3820 2.2400 3.3850 -0.0424 -0.1350 -0.3270 113 ALA A CB  
875  N N   . VAL A 114 ? 1.4814 1.3688 2.5174 -0.0311 -0.1083 -0.3812 114 VAL A N   
876  C CA  . VAL A 114 ? 1.4163 1.3242 2.4613 -0.0325 -0.0867 -0.4030 114 VAL A CA  
877  C C   . VAL A 114 ? 1.8193 1.7219 2.8620 -0.0299 -0.0803 -0.4274 114 VAL A C   
878  O O   . VAL A 114 ? 1.8618 1.7677 2.8893 -0.0388 -0.0592 -0.4406 114 VAL A O   
879  C CB  . VAL A 114 ? 1.3348 1.2691 2.4129 -0.0251 -0.0858 -0.4106 114 VAL A CB  
880  C CG1 . VAL A 114 ? 1.4231 1.3802 2.5103 -0.0287 -0.0620 -0.4344 114 VAL A CG1 
881  C CG2 . VAL A 114 ? 1.1183 1.0570 2.1968 -0.0276 -0.0916 -0.3871 114 VAL A CG2 
882  N N   . ALA A 115 ? 1.9668 1.8595 3.0226 -0.0182 -0.0991 -0.4330 115 ALA A N   
883  C CA  . ALA A 115 ? 1.8971 1.7836 2.9531 -0.0127 -0.0968 -0.4568 115 ALA A CA  
884  C C   . ALA A 115 ? 1.8713 1.7356 2.8893 -0.0243 -0.0876 -0.4540 115 ALA A C   
885  O O   . ALA A 115 ? 2.2995 2.1667 3.3082 -0.0282 -0.0697 -0.4745 115 ALA A O   
886  C CB  . ALA A 115 ? 1.9333 1.8071 3.0055 0.0018  -0.1226 -0.4592 115 ALA A CB  
887  N N   . GLU A 116 ? 1.9293 1.7719 2.9255 -0.0301 -0.1002 -0.4285 116 GLU A N   
888  C CA  . GLU A 116 ? 2.4566 2.2742 3.4155 -0.0406 -0.0968 -0.4216 116 GLU A CA  
889  C C   . GLU A 116 ? 2.2568 2.0810 3.1952 -0.0531 -0.0703 -0.4297 116 GLU A C   
890  O O   . GLU A 116 ? 2.1218 1.9303 3.0346 -0.0593 -0.0607 -0.4403 116 GLU A O   
891  C CB  . GLU A 116 ? 2.9893 2.7908 3.9381 -0.0435 -0.1163 -0.3925 116 GLU A CB  
892  C CG  . GLU A 116 ? 3.1265 2.8984 4.0581 -0.0428 -0.1340 -0.3875 116 GLU A CG  
893  C CD  . GLU A 116 ? 3.2372 2.9879 4.1318 -0.0533 -0.1254 -0.3873 116 GLU A CD  
894  O OE1 . GLU A 116 ? 3.5207 3.2692 4.3975 -0.0629 -0.1205 -0.3716 116 GLU A OE1 
895  O OE2 . GLU A 116 ? 3.3510 3.0859 4.2335 -0.0515 -0.1246 -0.4031 116 GLU A OE2 
896  N N   . ARG A 117 ? 2.2606 2.1088 3.2125 -0.0560 -0.0575 -0.4297 117 ARG A N   
897  C CA  . ARG A 117 ? 2.1274 1.9788 3.0567 -0.0696 -0.0331 -0.4364 117 ARG A CA  
898  C C   . ARG A 117 ? 1.8164 1.6952 2.7664 -0.0693 -0.0128 -0.4639 117 ARG A C   
899  O O   . ARG A 117 ? 1.3429 1.2454 2.3307 -0.0579 -0.0175 -0.4738 117 ARG A O   
900  C CB  . ARG A 117 ? 2.2326 2.0834 3.1492 -0.0774 -0.0324 -0.4135 117 ARG A CB  
901  C CG  . ARG A 117 ? 2.2105 2.0327 3.0961 -0.0825 -0.0449 -0.3917 117 ARG A CG  
902  C CD  . ARG A 117 ? 2.2571 2.0527 3.1033 -0.0925 -0.0366 -0.3985 117 ARG A CD  
903  N NE  . ARG A 117 ? 2.5726 2.3433 3.3959 -0.0948 -0.0531 -0.3767 117 ARG A NE  
904  C CZ  . ARG A 117 ? 2.7924 2.5481 3.5849 -0.1045 -0.0498 -0.3643 117 ARG A CZ  
905  N NH1 . ARG A 117 ? 3.0260 2.7851 3.8027 -0.1140 -0.0301 -0.3715 117 ARG A NH1 
906  N NH2 . ARG A 117 ? 2.6674 2.4047 3.4450 -0.1049 -0.0666 -0.3454 117 ARG A NH2 
907  N N   . PRO A 118 ? 1.8196 1.6952 2.7436 -0.0828 0.0100  -0.4774 118 PRO A N   
908  C CA  . PRO A 118 ? 1.8315 1.7359 2.7714 -0.0877 0.0335  -0.5014 118 PRO A CA  
909  C C   . PRO A 118 ? 1.8286 1.7647 2.8036 -0.0835 0.0353  -0.5010 118 PRO A C   
910  O O   . PRO A 118 ? 2.1320 2.0964 3.1423 -0.0758 0.0405  -0.5228 118 PRO A O   
911  C CB  . PRO A 118 ? 1.7425 1.6294 2.6359 -0.1083 0.0546  -0.5014 118 PRO A CB  
912  C CG  . PRO A 118 ? 1.7836 1.6329 2.6417 -0.1097 0.0429  -0.4911 118 PRO A CG  
913  C CD  . PRO A 118 ? 1.7733 1.6160 2.6497 -0.0952 0.0142  -0.4705 118 PRO A CD  
914  N N   . ALA A 119 ? 1.7312 1.6619 2.6966 -0.0879 0.0300  -0.4770 119 ALA A N   
915  C CA  . ALA A 119 ? 1.7415 1.6973 2.7278 -0.0893 0.0366  -0.4755 119 ALA A CA  
916  C C   . ALA A 119 ? 1.9677 1.9214 2.9655 -0.0806 0.0158  -0.4502 119 ALA A C   
917  O O   . ALA A 119 ? 2.8057 2.7357 3.7808 -0.0815 0.0032  -0.4284 119 ALA A O   
918  C CB  . ALA A 119 ? 1.5708 1.5228 2.5257 -0.1086 0.0589  -0.4754 119 ALA A CB  
919  N N   . GLY A 120 ? 1.8164 1.7962 2.8494 -0.0729 0.0132  -0.4543 120 GLY A N   
920  C CA  . GLY A 120 ? 1.7936 1.7752 2.8414 -0.0642 -0.0051 -0.4338 120 GLY A CA  
921  C C   . GLY A 120 ? 1.9494 1.9496 3.0054 -0.0691 0.0043  -0.4303 120 GLY A C   
922  O O   . GLY A 120 ? 2.3321 2.3559 3.4083 -0.0706 0.0172  -0.4492 120 GLY A O   
923  N N   . THR A 121 ? 1.7973 1.7863 2.8364 -0.0721 -0.0020 -0.4063 121 THR A N   
924  C CA  . THR A 121 ? 1.5446 1.5459 2.5875 -0.0754 0.0028  -0.3983 121 THR A CA  
925  C C   . THR A 121 ? 1.3258 1.3220 2.3741 -0.0669 -0.0169 -0.3750 121 THR A C   
926  O O   . THR A 121 ? 1.4561 1.4328 2.4839 -0.0675 -0.0264 -0.3578 121 THR A O   
927  C CB  . THR A 121 ? 1.5169 1.5053 2.5224 -0.0912 0.0188  -0.3927 121 THR A CB  
928  O OG1 . THR A 121 ? 1.7905 1.7761 2.7816 -0.1016 0.0364  -0.4118 121 THR A OG1 
929  C CG2 . THR A 121 ? 1.1651 1.1667 2.1739 -0.0961 0.0269  -0.3896 121 THR A CG2 
930  N N   . ILE A 122 ? 1.1164 1.1307 2.1895 -0.0608 -0.0212 -0.3739 122 ILE A N   
931  C CA  . ILE A 122 ? 1.2483 1.2602 2.3248 -0.0548 -0.0367 -0.3524 122 ILE A CA  
932  C C   . ILE A 122 ? 1.4931 1.5090 2.5568 -0.0615 -0.0276 -0.3427 122 ILE A C   
933  O O   . ILE A 122 ? 1.5174 1.5487 2.5915 -0.0646 -0.0163 -0.3544 122 ILE A O   
934  C CB  . ILE A 122 ? 1.3063 1.3289 2.4159 -0.0417 -0.0532 -0.3554 122 ILE A CB  
935  C CG1 . ILE A 122 ? 1.5109 1.5209 2.6257 -0.0344 -0.0686 -0.3568 122 ILE A CG1 
936  C CG2 . ILE A 122 ? 1.1888 1.2136 2.3020 -0.0381 -0.0640 -0.3363 122 ILE A CG2 
937  C CD1 . ILE A 122 ? 1.6331 1.6473 2.7753 -0.0219 -0.0878 -0.3581 122 ILE A CD1 
938  N N   . VAL A 123 ? 1.6749 1.6769 2.7166 -0.0633 -0.0334 -0.3218 123 VAL A N   
939  C CA  . VAL A 123 ? 1.4428 1.4433 2.4664 -0.0689 -0.0263 -0.3114 123 VAL A CA  
940  C C   . VAL A 123 ? 1.4753 1.4845 2.5122 -0.0613 -0.0378 -0.2969 123 VAL A C   
941  O O   . VAL A 123 ? 1.4346 1.4377 2.4696 -0.0569 -0.0508 -0.2817 123 VAL A O   
942  C CB  . VAL A 123 ? 1.2498 1.2287 2.2381 -0.0757 -0.0245 -0.3002 123 VAL A CB  
943  C CG1 . VAL A 123 ? 1.3715 1.3459 2.3387 -0.0806 -0.0183 -0.2910 123 VAL A CG1 
944  C CG2 . VAL A 123 ? 1.2447 1.2109 2.2156 -0.0837 -0.0145 -0.3135 123 VAL A CG2 
945  N N   . ASP A 124 ? 1.5030 1.5267 2.5532 -0.0608 -0.0325 -0.3027 124 ASP A N   
946  C CA  . ASP A 124 ? 1.5422 1.5754 2.6091 -0.0530 -0.0434 -0.2935 124 ASP A CA  
947  C C   . ASP A 124 ? 1.5638 1.6016 2.6221 -0.0562 -0.0360 -0.2890 124 ASP A C   
948  O O   . ASP A 124 ? 1.6679 1.7050 2.7134 -0.0647 -0.0219 -0.2969 124 ASP A O   
949  C CB  . ASP A 124 ? 1.4534 1.5004 2.5532 -0.0453 -0.0507 -0.3063 124 ASP A CB  
950  C CG  . ASP A 124 ? 1.5777 1.6386 2.6930 -0.0484 -0.0382 -0.3300 124 ASP A CG  
951  O OD1 . ASP A 124 ? 1.7741 1.8317 2.8722 -0.0585 -0.0224 -0.3377 124 ASP A OD1 
952  O OD2 . ASP A 124 ? 1.5296 1.6045 2.6739 -0.0411 -0.0445 -0.3415 124 ASP A OD2 
953  N N   . PHE A 125 ? 1.5128 1.5551 2.5785 -0.0497 -0.0462 -0.2768 125 PHE A N   
954  C CA  . PHE A 125 ? 1.5517 1.5974 2.6092 -0.0516 -0.0406 -0.2725 125 PHE A CA  
955  C C   . PHE A 125 ? 1.6169 1.6775 2.6956 -0.0520 -0.0356 -0.2884 125 PHE A C   
956  O O   . PHE A 125 ? 1.3531 1.4159 2.4246 -0.0605 -0.0219 -0.2988 125 PHE A O   
957  C CB  . PHE A 125 ? 1.3354 1.3789 2.3863 -0.0461 -0.0507 -0.2532 125 PHE A CB  
958  C CG  . PHE A 125 ? 1.3668 1.4099 2.4028 -0.0482 -0.0440 -0.2489 125 PHE A CG  
959  C CD1 . PHE A 125 ? 1.5201 1.5509 2.5280 -0.0538 -0.0360 -0.2451 125 PHE A CD1 
960  C CD2 . PHE A 125 ? 1.2745 1.3269 2.3231 -0.0447 -0.0467 -0.2499 125 PHE A CD2 
961  C CE1 . PHE A 125 ? 1.5668 1.5942 2.5589 -0.0555 -0.0309 -0.2421 125 PHE A CE1 
962  C CE2 . PHE A 125 ? 1.4892 1.5395 2.5229 -0.0469 -0.0406 -0.2470 125 PHE A CE2 
963  C CZ  . PHE A 125 ? 1.6408 1.6783 2.6461 -0.0522 -0.0329 -0.2429 125 PHE A CZ  
964  N N   . SER A 126 ? 1.5686 1.6384 2.6727 -0.0434 -0.0477 -0.2900 126 SER A N   
965  C CA  . SER A 126 ? 1.5928 1.6784 2.7225 -0.0417 -0.0465 -0.3064 126 SER A CA  
966  C C   . SER A 126 ? 1.6501 1.7413 2.8057 -0.0345 -0.0558 -0.3187 126 SER A C   
967  O O   . SER A 126 ? 1.4516 1.5328 2.6063 -0.0289 -0.0688 -0.3090 126 SER A O   
968  C CB  . SER A 126 ? 1.8658 1.9555 3.0014 -0.0367 -0.0544 -0.2987 126 SER A CB  
969  O OG  . SER A 126 ? 2.0466 2.1276 3.1787 -0.0297 -0.0694 -0.2820 126 SER A OG  
970  N N   . ALA A 127 ? 1.7370 1.8441 2.9145 -0.0356 -0.0487 -0.3406 127 ALA A N   
971  C CA  . ALA A 127 ? 1.4828 1.5982 2.6888 -0.0274 -0.0572 -0.3570 127 ALA A CA  
972  C C   . ALA A 127 ? 1.3908 1.5047 2.6140 -0.0154 -0.0784 -0.3512 127 ALA A C   
973  O O   . ALA A 127 ? 0.9670 1.0845 2.1915 -0.0146 -0.0812 -0.3453 127 ALA A O   
974  C CB  . ALA A 127 ? 1.3273 1.4643 2.5542 -0.0316 -0.0437 -0.3820 127 ALA A CB  
975  N N   . SER A 128 ? 1.5015 1.6068 2.7339 -0.0067 -0.0939 -0.3517 128 SER A N   
976  C CA  . SER A 128 ? 1.6608 1.7567 2.9006 0.0029  -0.1161 -0.3422 128 SER A CA  
977  C C   . SER A 128 ? 1.5398 1.6322 2.8003 0.0133  -0.1314 -0.3556 128 SER A C   
978  O O   . SER A 128 ? 1.6550 1.7497 2.9192 0.0126  -0.1246 -0.3681 128 SER A O   
979  C CB  . SER A 128 ? 1.9276 2.0047 3.1398 0.0001  -0.1228 -0.3156 128 SER A CB  
980  O OG  . SER A 128 ? 1.3632 1.4252 2.5676 0.0012  -0.1317 -0.3093 128 SER A OG  
981  N N   . PRO A 129 ? 1.3521 1.4362 2.6242 0.0234  -0.1535 -0.3535 129 PRO A N   
982  C CA  . PRO A 129 ? 1.2768 1.3540 2.5672 0.0347  -0.1710 -0.3668 129 PRO A CA  
983  C C   . PRO A 129 ? 1.4501 1.5105 2.7219 0.0313  -0.1714 -0.3586 129 PRO A C   
984  O O   . PRO A 129 ? 1.5481 1.6105 2.8317 0.0357  -0.1713 -0.3754 129 PRO A O   
985  C CB  . PRO A 129 ? 1.2319 1.2928 2.5218 0.0421  -0.1953 -0.3554 129 PRO A CB  
986  C CG  . PRO A 129 ? 1.1909 1.2627 2.4783 0.0377  -0.1874 -0.3490 129 PRO A CG  
987  C CD  . PRO A 129 ? 1.2827 1.3619 2.5495 0.0247  -0.1631 -0.3398 129 PRO A CD  
988  N N   . ALA A 130 ? 1.5019 1.5457 2.7461 0.0243  -0.1740 -0.3333 130 ALA A N   
989  C CA  . ALA A 130 ? 1.6471 1.6723 2.8731 0.0209  -0.1792 -0.3221 130 ALA A CA  
990  C C   . ALA A 130 ? 1.7635 1.7964 2.9851 0.0151  -0.1603 -0.3319 130 ALA A C   
991  O O   . ALA A 130 ? 1.8970 1.9203 3.1192 0.0178  -0.1653 -0.3391 130 ALA A O   
992  C CB  . ALA A 130 ? 1.9123 1.9251 3.1126 0.0132  -0.1823 -0.2947 130 ALA A CB  
993  N N   . THR A 131 ? 1.5773 1.6248 2.7920 0.0070  -0.1394 -0.3320 131 THR A N   
994  C CA  . THR A 131 ? 1.4192 1.4713 2.6240 -0.0006 -0.1204 -0.3399 131 THR A CA  
995  C C   . THR A 131 ? 1.7206 1.7837 2.9483 0.0049  -0.1170 -0.3672 131 THR A C   
996  O O   . THR A 131 ? 1.9900 2.0466 3.2106 0.0030  -0.1125 -0.3738 131 THR A O   
997  C CB  . THR A 131 ? 1.4673 1.5287 2.6568 -0.0110 -0.1002 -0.3352 131 THR A CB  
998  O OG1 . THR A 131 ? 1.7402 1.8210 2.9490 -0.0099 -0.0929 -0.3498 131 THR A OG1 
999  C CG2 . THR A 131 ? 1.6431 1.6943 2.8092 -0.0156 -0.1027 -0.3097 131 THR A CG2 
1000 N N   . ASP A 132 ? 1.8559 1.9359 3.1111 0.0120  -0.1197 -0.3831 132 ASP A N   
1001 C CA  . ASP A 132 ? 1.4575 1.5536 2.7404 0.0187  -0.1168 -0.4118 132 ASP A CA  
1002 C C   . ASP A 132 ? 1.5174 1.5973 2.8054 0.0290  -0.1348 -0.4170 132 ASP A C   
1003 O O   . ASP A 132 ? 1.4428 1.5265 2.7359 0.0300  -0.1275 -0.4344 132 ASP A O   
1004 C CB  . ASP A 132 ? 1.4516 1.5710 2.7647 0.0243  -0.1171 -0.4277 132 ASP A CB  
1005 C CG  . ASP A 132 ? 1.8193 1.9595 3.1306 0.0119  -0.0925 -0.4337 132 ASP A CG  
1006 O OD1 . ASP A 132 ? 1.9494 2.0858 3.2367 -0.0003 -0.0744 -0.4295 132 ASP A OD1 
1007 O OD2 . ASP A 132 ? 2.1735 2.3315 3.5058 0.0142  -0.0928 -0.4424 132 ASP A OD2 
1008 N N   . GLU A 133 ? 1.8203 1.8806 3.1045 0.0357  -0.1581 -0.4016 133 GLU A N   
1009 C CA  . GLU A 133 ? 2.0084 2.0474 3.2935 0.0450  -0.1795 -0.4030 133 GLU A CA  
1010 C C   . GLU A 133 ? 1.8043 1.8292 3.0658 0.0374  -0.1722 -0.3966 133 GLU A C   
1011 O O   . GLU A 133 ? 1.6448 1.6638 2.9124 0.0435  -0.1767 -0.4115 133 GLU A O   
1012 C CB  . GLU A 133 ? 2.1845 2.2021 3.4617 0.0489  -0.2037 -0.3833 133 GLU A CB  
1013 C CG  . GLU A 133 ? 2.4432 2.4328 3.7152 0.0564  -0.2281 -0.3811 133 GLU A CG  
1014 C CD  . GLU A 133 ? 2.6852 2.6769 3.9856 0.0728  -0.2422 -0.4081 133 GLU A CD  
1015 O OE1 . GLU A 133 ? 2.9072 2.9142 4.2210 0.0756  -0.2292 -0.4298 133 GLU A OE1 
1016 O OE2 . GLU A 133 ? 2.6900 2.6675 3.9982 0.0830  -0.2666 -0.4079 133 GLU A OE2 
1017 N N   . LEU A 134 ? 1.6553 1.6748 2.8904 0.0248  -0.1618 -0.3748 134 LEU A N   
1018 C CA  . LEU A 134 ? 1.6057 1.6113 2.8160 0.0164  -0.1554 -0.3658 134 LEU A CA  
1019 C C   . LEU A 134 ? 1.7893 1.8063 3.0032 0.0142  -0.1368 -0.3879 134 LEU A C   
1020 O O   . LEU A 134 ? 2.0618 2.0660 3.2682 0.0152  -0.1394 -0.3936 134 LEU A O   
1021 C CB  . LEU A 134 ? 1.3651 1.3648 2.5488 0.0046  -0.1488 -0.3401 134 LEU A CB  
1022 C CG  . LEU A 134 ? 1.2868 1.2720 2.4622 0.0048  -0.1674 -0.3173 134 LEU A CG  
1023 C CD1 . LEU A 134 ? 1.2367 1.2255 2.3937 -0.0047 -0.1586 -0.2961 134 LEU A CD1 
1024 C CD2 . LEU A 134 ? 1.2970 1.2589 2.4620 0.0052  -0.1840 -0.3099 134 LEU A CD2 
1025 N N   . GLY A 135 ? 1.8791 1.9193 3.1030 0.0104  -0.1181 -0.4000 135 GLY A N   
1026 C CA  . GLY A 135 ? 1.8123 1.8664 3.0388 0.0056  -0.0972 -0.4218 135 GLY A CA  
1027 C C   . GLY A 135 ? 1.7167 1.7748 2.9670 0.0178  -0.1050 -0.4468 135 GLY A C   
1028 O O   . GLY A 135 ? 1.6908 1.7444 2.9329 0.0157  -0.0970 -0.4585 135 GLY A O   
1029 N N   . ARG A 136 ? 1.7041 1.7693 2.9827 0.0310  -0.1219 -0.4550 136 ARG A N   
1030 C CA  . ARG A 136 ? 1.8335 1.9035 3.1391 0.0459  -0.1333 -0.4801 136 ARG A CA  
1031 C C   . ARG A 136 ? 1.7779 1.8182 3.0665 0.0501  -0.1486 -0.4741 136 ARG A C   
1032 O O   . ARG A 136 ? 1.8362 1.8768 3.1299 0.0549  -0.1456 -0.4939 136 ARG A O   
1033 C CB  . ARG A 136 ? 2.0529 2.1349 3.3916 0.0599  -0.1501 -0.4903 136 ARG A CB  
1034 C CG  . ARG A 136 ? 2.4424 2.5600 3.8050 0.0566  -0.1315 -0.5075 136 ARG A CG  
1035 C CD  . ARG A 136 ? 2.4958 2.6265 3.8937 0.0715  -0.1493 -0.5202 136 ARG A CD  
1036 N NE  . ARG A 136 ? 2.5753 2.6864 3.9624 0.0734  -0.1691 -0.4951 136 ARG A NE  
1037 C CZ  . ARG A 136 ? 2.6014 2.6853 3.9849 0.0844  -0.1976 -0.4858 136 ARG A CZ  
1038 N NH1 . ARG A 136 ? 2.1865 2.2573 3.5754 0.0953  -0.2112 -0.4984 136 ARG A NH1 
1039 N NH2 . ARG A 136 ? 2.7899 2.8579 4.1614 0.0836  -0.2123 -0.4636 136 ARG A NH2 
1040 N N   . ARG A 137 ? 1.7132 1.7284 2.9827 0.0485  -0.1663 -0.4471 137 ARG A N   
1041 C CA  . ARG A 137 ? 1.7159 1.7003 2.9720 0.0533  -0.1880 -0.4381 137 ARG A CA  
1042 C C   . ARG A 137 ? 1.7105 1.6799 2.9360 0.0415  -0.1778 -0.4270 137 ARG A C   
1043 O O   . ARG A 137 ? 1.6598 1.6037 2.8722 0.0436  -0.1938 -0.4201 137 ARG A O   
1044 C CB  . ARG A 137 ? 1.5737 1.5380 2.8206 0.0539  -0.2104 -0.4132 137 ARG A CB  
1045 C CG  . ARG A 137 ? 1.5378 1.5004 2.8084 0.0686  -0.2327 -0.4222 137 ARG A CG  
1046 C CD  . ARG A 137 ? 1.5720 1.5097 2.8265 0.0664  -0.2545 -0.3962 137 ARG A CD  
1047 N NE  . ARG A 137 ? 1.6781 1.5849 2.9067 0.0610  -0.2679 -0.3790 137 ARG A NE  
1048 C CZ  . ARG A 137 ? 1.9063 1.7892 3.1169 0.0561  -0.2863 -0.3558 137 ARG A CZ  
1049 N NH1 . ARG A 137 ? 1.7299 1.6128 2.9440 0.0574  -0.2955 -0.3470 137 ARG A NH1 
1050 N NH2 . ARG A 137 ? 2.2439 2.1020 3.4319 0.0492  -0.2956 -0.3419 137 ARG A NH2 
1051 N N   . THR A 138 ? 1.7459 1.7291 2.9588 0.0289  -0.1527 -0.4251 138 THR A N   
1052 C CA  . THR A 138 ? 1.8555 1.8240 3.0381 0.0175  -0.1430 -0.4151 138 THR A CA  
1053 C C   . THR A 138 ? 1.7556 1.7373 2.9368 0.0130  -0.1196 -0.4376 138 THR A C   
1054 O O   . THR A 138 ? 1.8493 1.8163 3.0071 0.0063  -0.1135 -0.4363 138 THR A O   
1055 C CB  . THR A 138 ? 1.9078 1.8719 3.0675 0.0051  -0.1380 -0.3876 138 THR A CB  
1056 O OG1 . THR A 138 ? 1.7673 1.7542 2.9322 -0.0003 -0.1187 -0.3918 138 THR A OG1 
1057 C CG2 . THR A 138 ? 1.8512 1.8025 3.0095 0.0073  -0.1595 -0.3651 138 THR A CG2 
1058 N N   . GLY A 139 ? 1.6253 1.6348 2.8306 0.0157  -0.1063 -0.4582 139 GLY A N   
1059 C CA  . GLY A 139 ? 1.6650 1.6901 2.8700 0.0096  -0.0822 -0.4812 139 GLY A CA  
1060 C C   . GLY A 139 ? 1.6205 1.6486 2.7993 -0.0082 -0.0596 -0.4703 139 GLY A C   
1061 O O   . GLY A 139 ? 1.4852 1.5183 2.6516 -0.0178 -0.0388 -0.4840 139 GLY A O   
1062 N N   . ALA A 140 ? 1.6632 1.6862 2.8318 -0.0127 -0.0647 -0.4457 140 ALA A N   
1063 C CA  . ALA A 140 ? 1.5752 1.6020 2.7225 -0.0273 -0.0460 -0.4360 140 ALA A CA  
1064 C C   . ALA A 140 ? 1.7208 1.7736 2.8917 -0.0267 -0.0393 -0.4427 140 ALA A C   
1065 O O   . ALA A 140 ? 1.7785 1.8372 2.9714 -0.0164 -0.0551 -0.4381 140 ALA A O   
1066 C CB  . ALA A 140 ? 1.4202 1.4257 2.5400 -0.0326 -0.0546 -0.4065 140 ALA A CB  
1067 N N   . THR A 141 ? 1.7879 1.8544 2.9520 -0.0387 -0.0159 -0.4538 141 THR A N   
1068 C CA  . THR A 141 ? 1.6390 1.7310 2.8232 -0.0412 -0.0062 -0.4625 141 THR A CA  
1069 C C   . THR A 141 ? 1.4284 1.5114 2.5895 -0.0498 -0.0042 -0.4384 141 THR A C   
1070 O O   . THR A 141 ? 1.3283 1.3994 2.4571 -0.0634 0.0098  -0.4321 141 THR A O   
1071 C CB  . THR A 141 ? 1.8852 1.9951 3.0711 -0.0520 0.0186  -0.4878 141 THR A CB  
1072 O OG1 . THR A 141 ? 2.0803 2.2013 3.2932 -0.0404 0.0139  -0.5110 141 THR A OG1 
1073 C CG2 . THR A 141 ? 2.1785 2.3143 3.3801 -0.0590 0.0322  -0.4966 141 THR A CG2 
1074 N N   . PRO A 142 ? 1.4173 1.5037 2.5921 -0.0419 -0.0188 -0.4250 142 PRO A N   
1075 C CA  . PRO A 142 ? 1.6431 1.7229 2.7980 -0.0486 -0.0171 -0.4037 142 PRO A CA  
1076 C C   . PRO A 142 ? 1.8461 1.9325 2.9847 -0.0638 0.0054  -0.4097 142 PRO A C   
1077 O O   . PRO A 142 ? 1.8253 1.9335 2.9833 -0.0672 0.0175  -0.4302 142 PRO A O   
1078 C CB  . PRO A 142 ? 1.3826 1.4723 2.5630 -0.0374 -0.0333 -0.3979 142 PRO A CB  
1079 C CG  . PRO A 142 ? 1.1952 1.2832 2.3982 -0.0237 -0.0510 -0.4061 142 PRO A CG  
1080 C CD  . PRO A 142 ? 1.2297 1.3241 2.4377 -0.0260 -0.0387 -0.4297 142 PRO A CD  
1081 N N   . GLU A 143 ? 1.9963 2.0629 3.0985 -0.0731 0.0102  -0.3922 143 GLU A N   
1082 C CA  . GLU A 143 ? 1.8242 1.8868 2.8999 -0.0890 0.0293  -0.3943 143 GLU A CA  
1083 C C   . GLU A 143 ? 1.6473 1.7255 2.7352 -0.0906 0.0324  -0.3937 143 GLU A C   
1084 O O   . GLU A 143 ? 1.4608 1.5425 2.5361 -0.1039 0.0490  -0.4010 143 GLU A O   
1085 C CB  . GLU A 143 ? 1.6801 1.7140 2.7170 -0.0930 0.0252  -0.3729 143 GLU A CB  
1086 C CG  . GLU A 143 ? 1.9073 1.9248 2.9052 -0.1095 0.0416  -0.3727 143 GLU A CG  
1087 C CD  . GLU A 143 ? 1.9911 1.9824 2.9570 -0.1089 0.0318  -0.3500 143 GLU A CD  
1088 O OE1 . GLU A 143 ? 1.7635 1.7561 2.7323 -0.1026 0.0222  -0.3347 143 GLU A OE1 
1089 O OE2 . GLU A 143 ? 2.2924 2.2626 3.2305 -0.1146 0.0337  -0.3483 143 GLU A OE2 
1090 N N   . GLU A 144 ? 1.6350 1.7207 2.7458 -0.0775 0.0157  -0.3850 144 GLU A N   
1091 C CA  . GLU A 144 ? 1.8928 1.9895 3.0134 -0.0768 0.0145  -0.3809 144 GLU A CA  
1092 C C   . GLU A 144 ? 1.9115 2.0220 3.0683 -0.0615 -0.0029 -0.3831 144 GLU A C   
1093 O O   . GLU A 144 ? 2.1430 2.2537 3.3036 -0.0561 -0.0129 -0.3707 144 GLU A O   
1094 C CB  . GLU A 144 ? 1.8880 1.9650 2.9756 -0.0805 0.0125  -0.3576 144 GLU A CB  
1095 C CG  . GLU A 144 ? 1.8946 1.9727 2.9672 -0.0915 0.0250  -0.3580 144 GLU A CG  
1096 C CD  . GLU A 144 ? 2.5345 2.6362 3.6370 -0.0901 0.0263  -0.3699 144 GLU A CD  
1097 O OE1 . GLU A 144 ? 2.4171 2.5266 3.5414 -0.0779 0.0115  -0.3641 144 GLU A OE1 
1098 O OE2 . GLU A 144 ? 3.2210 3.3330 4.3240 -0.1024 0.0425  -0.3857 144 GLU A OE2 
1099 N N   . GLY A 145 ? 1.7385 1.8578 2.9195 -0.0541 -0.0078 -0.3990 145 GLY A N   
1100 C CA  . GLY A 145 ? 1.8560 1.9886 3.0731 -0.0399 -0.0238 -0.4074 145 GLY A CA  
1101 C C   . GLY A 145 ? 2.0446 2.2059 3.2928 -0.0412 -0.0136 -0.4341 145 GLY A C   
1102 O O   . GLY A 145 ? 2.0963 2.2671 3.3387 -0.0534 0.0067  -0.4482 145 GLY A O   
1103 N N   . ASP A 146 ? 1.8148 1.9894 3.0956 -0.0288 -0.0284 -0.4412 146 ASP A N   
1104 C CA  . ASP A 146 ? 1.7240 1.9286 3.0405 -0.0273 -0.0231 -0.4663 146 ASP A CA  
1105 C C   . ASP A 146 ? 1.5940 1.8020 2.9268 -0.0183 -0.0399 -0.4590 146 ASP A C   
1106 O O   . ASP A 146 ? 1.8719 2.0889 3.2028 -0.0263 -0.0317 -0.4572 146 ASP A O   
1107 C CB  . ASP A 146 ? 2.1570 2.3758 3.4639 -0.0456 0.0027  -0.4757 146 ASP A CB  
1108 C CG  . ASP A 146 ? 2.6809 2.9341 4.0232 -0.0481 0.0150  -0.5076 146 ASP A CG  
1109 O OD1 . ASP A 146 ? 2.7288 3.0004 4.1099 -0.0344 0.0012  -0.5216 146 ASP A OD1 
1110 O OD2 . ASP A 146 ? 3.0715 3.3323 4.4014 -0.0641 0.0382  -0.5187 146 ASP A OD2 
1111 N N   . HIS A 147 ? 1.4145 1.6124 2.7602 -0.0026 -0.0640 -0.4543 147 HIS A N   
1112 C CA  . HIS A 147 ? 1.5983 1.7847 2.9401 0.0034  -0.0813 -0.4360 147 HIS A CA  
1113 C C   . HIS A 147 ? 1.4950 1.7043 2.8654 0.0056  -0.0823 -0.4504 147 HIS A C   
1114 O O   . HIS A 147 ? 1.4624 1.6689 2.8215 0.0010  -0.0818 -0.4376 147 HIS A O   
1115 C CB  . HIS A 147 ? 1.9422 2.1099 3.2888 0.0182  -0.1077 -0.4284 147 HIS A CB  
1116 C CG  . HIS A 147 ? 2.0065 2.1634 3.3517 0.0246  -0.1263 -0.4135 147 HIS A CG  
1117 N ND1 . HIS A 147 ? 1.6311 1.7821 2.9537 0.0166  -0.1206 -0.3944 147 HIS A ND1 
1118 C CD2 . HIS A 147 ? 2.0038 2.1528 3.3652 0.0381  -0.1510 -0.4151 147 HIS A CD2 
1119 C CE1 . HIS A 147 ? 1.5020 1.6426 2.8265 0.0245  -0.1400 -0.3847 147 HIS A CE1 
1120 N NE2 . HIS A 147 ? 1.9446 2.0830 3.2918 0.0371  -0.1589 -0.3968 147 HIS A NE2 
1121 N N   . ALA A 148 ? 1.3486 1.5800 2.7568 0.0138  -0.0857 -0.4773 148 ALA A N   
1122 C CA  . ALA A 148 ? 1.1929 1.4486 2.6356 0.0186  -0.0906 -0.4945 148 ALA A CA  
1123 C C   . ALA A 148 ? 1.2490 1.5218 2.6856 0.0015  -0.0676 -0.4971 148 ALA A C   
1124 O O   . ALA A 148 ? 1.1907 1.4679 2.6320 0.0006  -0.0723 -0.4928 148 ALA A O   
1125 C CB  . ALA A 148 ? 1.2648 1.5439 2.7494 0.0300  -0.0957 -0.5253 148 ALA A CB  
1126 N N   . PHE A 149 ? 1.3386 1.6184 2.7621 -0.0125 -0.0435 -0.5039 149 PHE A N   
1127 C CA  . PHE A 149 ? 1.2115 1.5041 2.6236 -0.0317 -0.0197 -0.5071 149 PHE A CA  
1128 C C   . PHE A 149 ? 1.2332 1.5020 2.6096 -0.0378 -0.0217 -0.4791 149 PHE A C   
1129 O O   . PHE A 149 ? 1.3921 1.6700 2.7702 -0.0453 -0.0167 -0.4796 149 PHE A O   
1130 C CB  . PHE A 149 ? 1.1394 1.4340 2.5329 -0.0468 0.0048  -0.5151 149 PHE A CB  
1131 C CG  . PHE A 149 ? 1.2536 1.5629 2.6369 -0.0688 0.0309  -0.5240 149 PHE A CG  
1132 C CD1 . PHE A 149 ? 1.3427 1.6463 2.7091 -0.0787 0.0343  -0.5113 149 PHE A CD1 
1133 C CD2 . PHE A 149 ? 1.4045 1.7316 2.7928 -0.0806 0.0524  -0.5456 149 PHE A CD2 
1134 C CE1 . PHE A 149 ? 1.3417 1.6552 2.6955 -0.1002 0.0572  -0.5190 149 PHE A CE1 
1135 C CE2 . PHE A 149 ? 1.6249 1.9637 3.0012 -0.1030 0.0765  -0.5539 149 PHE A CE2 
1136 C CZ  . PHE A 149 ? 1.5983 1.9291 2.9566 -0.1131 0.0785  -0.5402 149 PHE A CZ  
1137 N N   . VAL A 150 ? 1.0955 1.3351 2.4409 -0.0344 -0.0291 -0.4559 150 VAL A N   
1138 C CA  . VAL A 150 ? 1.1024 1.3192 2.4130 -0.0385 -0.0313 -0.4293 150 VAL A CA  
1139 C C   . VAL A 150 ? 1.1585 1.3767 2.4828 -0.0296 -0.0482 -0.4238 150 VAL A C   
1140 O O   . VAL A 150 ? 1.2991 1.5140 2.6085 -0.0366 -0.0438 -0.4148 150 VAL A O   
1141 C CB  . VAL A 150 ? 1.2415 1.4313 2.5217 -0.0359 -0.0364 -0.4085 150 VAL A CB  
1142 C CG1 . VAL A 150 ? 1.5900 1.7593 2.8424 -0.0351 -0.0442 -0.3823 150 VAL A CG1 
1143 C CG2 . VAL A 150 ? 1.4340 1.6188 2.6914 -0.0486 -0.0169 -0.4113 150 VAL A CG2 
1144 N N   . ALA A 151 ? 1.1813 1.4018 2.5318 -0.0141 -0.0685 -0.4298 151 ALA A N   
1145 C CA  . ALA A 151 ? 1.2001 1.4189 2.5640 -0.0041 -0.0881 -0.4259 151 ALA A CA  
1146 C C   . ALA A 151 ? 1.2878 1.5308 2.6734 -0.0099 -0.0807 -0.4419 151 ALA A C   
1147 O O   . ALA A 151 ? 1.3391 1.5766 2.7159 -0.0113 -0.0855 -0.4317 151 ALA A O   
1148 C CB  . ALA A 151 ? 1.3613 1.5777 2.7501 0.0126  -0.1110 -0.4336 151 ALA A CB  
1149 N N   . ARG A 152 ? 1.5398 1.8103 2.9538 -0.0138 -0.0686 -0.4678 152 ARG A N   
1150 C CA  . ARG A 152 ? 1.5958 1.8949 3.0356 -0.0213 -0.0595 -0.4872 152 ARG A CA  
1151 C C   . ARG A 152 ? 1.5273 1.8190 2.9345 -0.0392 -0.0422 -0.4742 152 ARG A C   
1152 O O   . ARG A 152 ? 1.3720 1.6697 2.7852 -0.0419 -0.0453 -0.4745 152 ARG A O   
1153 C CB  . ARG A 152 ? 1.8181 2.1512 3.2963 -0.0225 -0.0489 -0.5190 152 ARG A CB  
1154 C CG  . ARG A 152 ? 1.7183 2.0830 3.2317 -0.0261 -0.0470 -0.5394 152 ARG A CG  
1155 C CD  . ARG A 152 ? 1.6592 2.0651 3.2185 -0.0269 -0.0374 -0.5742 152 ARG A CD  
1156 N NE  . ARG A 152 ? 1.9383 2.3651 3.5157 -0.0351 -0.0347 -0.5828 152 ARG A NE  
1157 C CZ  . ARG A 152 ? 2.3564 2.8033 3.9749 -0.0231 -0.0525 -0.5982 152 ARG A CZ  
1158 N NH1 . ARG A 152 ? 2.8170 3.2719 4.4695 -0.0024 -0.0724 -0.6129 152 ARG A NH1 
1159 N NH2 . ARG A 152 ? 2.3325 2.7904 3.9575 -0.0319 -0.0511 -0.5996 152 ARG A NH2 
1160 N N   . TRP A 153 ? 1.6232 1.9009 2.9957 -0.0514 -0.0248 -0.4641 153 TRP A N   
1161 C CA  . TRP A 153 ? 1.5550 1.8322 2.9032 -0.0711 -0.0043 -0.4619 153 TRP A CA  
1162 C C   . TRP A 153 ? 1.4749 1.7191 2.7747 -0.0754 -0.0038 -0.4337 153 TRP A C   
1163 O O   . TRP A 153 ? 1.3396 1.5782 2.6172 -0.0891 0.0074  -0.4292 153 TRP A O   
1164 C CB  . TRP A 153 ? 1.6109 1.9039 2.9609 -0.0859 0.0188  -0.4803 153 TRP A CB  
1165 C CG  . TRP A 153 ? 1.9425 2.2747 3.3393 -0.0881 0.0242  -0.5107 153 TRP A CG  
1166 C CD1 . TRP A 153 ? 1.8298 2.1867 3.2616 -0.0819 0.0260  -0.5343 153 TRP A CD1 
1167 C CD2 . TRP A 153 ? 2.0604 2.4132 3.4762 -0.0961 0.0270  -0.5214 153 TRP A CD2 
1168 N NE1 . TRP A 153 ? 1.5966 1.9905 3.0693 -0.0858 0.0310  -0.5600 153 TRP A NE1 
1169 C CE2 . TRP A 153 ? 1.5661 1.9584 3.0303 -0.0950 0.0315  -0.5523 153 TRP A CE2 
1170 C CE3 . TRP A 153 ? 2.2429 2.5847 3.6397 -0.1040 0.0260  -0.5084 153 TRP A CE3 
1171 C CZ2 . TRP A 153 ? 1.3892 1.8115 2.8844 -0.1021 0.0347  -0.5702 153 TRP A CZ2 
1172 C CZ3 . TRP A 153 ? 1.9979 2.3666 3.4232 -0.1113 0.0286  -0.5252 153 TRP A CZ3 
1173 C CH2 . TRP A 153 ? 1.7020 2.1113 3.1771 -0.1104 0.0327  -0.5557 153 TRP A CH2 
1174 N N   . GLY A 154 ? 1.4507 1.6736 2.7349 -0.0638 -0.0164 -0.4158 154 GLY A N   
1175 C CA  . GLY A 154 ? 1.5588 1.7536 2.8016 -0.0652 -0.0176 -0.3903 154 GLY A CA  
1176 C C   . GLY A 154 ? 1.6842 1.8716 2.9259 -0.0568 -0.0331 -0.3778 154 GLY A C   
1177 O O   . GLY A 154 ? 2.0460 2.2130 3.2555 -0.0576 -0.0341 -0.3582 154 GLY A O   
1178 N N   . SER A 155 ? 1.4279 1.6317 2.7046 -0.0483 -0.0458 -0.3901 155 SER A N   
1179 C CA  . SER A 155 ? 1.5915 1.7890 2.8698 -0.0405 -0.0617 -0.3812 155 SER A CA  
1180 C C   . SER A 155 ? 1.6684 1.8628 2.9271 -0.0523 -0.0515 -0.3774 155 SER A C   
1181 O O   . SER A 155 ? 1.5428 1.7439 2.7941 -0.0669 -0.0331 -0.3858 155 SER A O   
1182 C CB  . SER A 155 ? 1.6980 1.9136 3.0182 -0.0300 -0.0772 -0.3982 155 SER A CB  
1183 O OG  . SER A 155 ? 1.7924 2.0301 3.1338 -0.0381 -0.0700 -0.4158 155 SER A OG  
1184 N N   . LYS A 156 ? 1.6111 1.7936 2.8596 -0.0467 -0.0637 -0.3651 156 LYS A N   
1185 C CA  . LYS A 156 ? 1.6192 1.7934 2.8432 -0.0569 -0.0554 -0.3590 156 LYS A CA  
1186 C C   . LYS A 156 ? 1.6547 1.8527 2.9035 -0.0686 -0.0458 -0.3809 156 LYS A C   
1187 O O   . LYS A 156 ? 1.8401 2.0374 3.0715 -0.0844 -0.0287 -0.3841 156 LYS A O   
1188 C CB  . LYS A 156 ? 1.4856 1.6439 2.6956 -0.0483 -0.0706 -0.3437 156 LYS A CB  
1189 C CG  . LYS A 156 ? 1.4494 1.5866 2.6361 -0.0375 -0.0808 -0.3223 156 LYS A CG  
1190 C CD  . LYS A 156 ? 1.2560 1.3770 2.4067 -0.0418 -0.0694 -0.3074 156 LYS A CD  
1191 C CE  . LYS A 156 ? 1.3636 1.4699 2.4987 -0.0313 -0.0803 -0.2889 156 LYS A CE  
1192 N NZ  . LYS A 156 ? 1.5353 1.6340 2.6514 -0.0330 -0.0720 -0.2798 156 LYS A NZ  
1193 N N   . SER A 157 ? 1.6362 1.8535 2.9243 -0.0605 -0.0585 -0.3955 157 SER A N   
1194 C CA  . SER A 157 ? 1.5444 1.7885 2.8631 -0.0696 -0.0528 -0.4176 157 SER A CA  
1195 C C   . SER A 157 ? 1.3784 1.6420 2.7067 -0.0835 -0.0315 -0.4347 157 SER A C   
1196 O O   . SER A 157 ? 1.3976 1.6713 2.7227 -0.1011 -0.0156 -0.4441 157 SER A O   
1197 C CB  . SER A 157 ? 1.6271 1.8888 2.9889 -0.0556 -0.0726 -0.4313 157 SER A CB  
1198 O OG  . SER A 157 ? 1.8030 2.0726 3.1872 -0.0442 -0.0791 -0.4392 157 SER A OG  
1199 N N   . GLY A 158 ? 1.2657 1.5326 2.6037 -0.0760 -0.0316 -0.4382 158 GLY A N   
1200 C CA  . GLY A 158 ? 1.2791 1.5631 2.6258 -0.0871 -0.0124 -0.4546 158 GLY A CA  
1201 C C   . GLY A 158 ? 1.3185 1.5848 2.6211 -0.1060 0.0078  -0.4445 158 GLY A C   
1202 O O   . GLY A 158 ? 1.3849 1.6659 2.6892 -0.1242 0.0269  -0.4593 158 GLY A O   
1203 N N   . GLY A 159 ? 1.4576 1.6918 2.7208 -0.1015 0.0026  -0.4197 159 GLY A N   
1204 C CA  . GLY A 159 ? 1.7686 1.9795 2.9857 -0.1158 0.0172  -0.4073 159 GLY A CA  
1205 C C   . GLY A 159 ? 1.8634 2.0751 3.0695 -0.1323 0.0263  -0.4116 159 GLY A C   
1206 O O   . GLY A 159 ? 1.8895 2.0978 3.0750 -0.1513 0.0443  -0.4169 159 GLY A O   
1207 N N   . LYS A 160 ? 1.9536 2.1679 3.1717 -0.1253 0.0128  -0.4090 160 LYS A N   
1208 C CA  . LYS A 160 ? 1.8171 2.0310 3.0265 -0.1390 0.0175  -0.4120 160 LYS A CA  
1209 C C   . LYS A 160 ? 1.7174 1.9619 2.9537 -0.1568 0.0336  -0.4372 160 LYS A C   
1210 O O   . LYS A 160 ? 1.4279 1.6664 2.6411 -0.1776 0.0486  -0.4398 160 LYS A O   
1211 C CB  . LYS A 160 ? 1.8388 2.0486 3.0570 -0.1257 -0.0023 -0.4042 160 LYS A CB  
1212 C CG  . LYS A 160 ? 1.7861 1.9943 2.9962 -0.1384 -0.0003 -0.4068 160 LYS A CG  
1213 C CD  . LYS A 160 ? 1.4418 1.6327 2.6410 -0.1265 -0.0184 -0.3925 160 LYS A CD  
1214 C CE  . LYS A 160 ? 1.3696 1.5506 2.5476 -0.1421 -0.0132 -0.3921 160 LYS A CE  
1215 N NZ  . LYS A 160 ? 1.5602 1.7115 2.7055 -0.1327 -0.0257 -0.3724 160 LYS A NZ  
1216 N N   . GLU A 161 ? 1.7430 2.0193 3.0274 -0.1483 0.0297  -0.4559 161 GLU A N   
1217 C CA  . GLU A 161 ? 1.7492 2.0621 3.0684 -0.1624 0.0442  -0.4833 161 GLU A CA  
1218 C C   . GLU A 161 ? 1.5257 1.8336 2.8178 -0.1824 0.0684  -0.4872 161 GLU A C   
1219 O O   . GLU A 161 ? 1.6537 1.9730 2.9420 -0.2056 0.0862  -0.4997 161 GLU A O   
1220 C CB  . GLU A 161 ? 2.0518 2.3971 3.4257 -0.1458 0.0339  -0.5024 161 GLU A CB  
1221 C CG  . GLU A 161 ? 2.3646 2.7141 3.7654 -0.1274 0.0088  -0.5008 161 GLU A CG  
1222 C CD  . GLU A 161 ? 2.6315 3.0194 4.0925 -0.1163 -0.0009 -0.5267 161 GLU A CD  
1223 O OE1 . GLU A 161 ? 2.4208 2.8375 3.9083 -0.1223 0.0129  -0.5488 161 GLU A OE1 
1224 O OE2 . GLU A 161 ? 3.0854 3.4737 4.5658 -0.1017 -0.0229 -0.5254 161 GLU A OE2 
1225 N N   . ILE A 162 ? 1.3463 1.6354 2.6182 -0.1739 0.0681  -0.4759 162 ILE A N   
1226 C CA  . ILE A 162 ? 1.3596 1.6391 2.6027 -0.1902 0.0885  -0.4780 162 ILE A CA  
1227 C C   . ILE A 162 ? 1.5597 1.8100 2.7518 -0.2107 0.0992  -0.4657 162 ILE A C   
1228 O O   . ILE A 162 ? 1.4350 1.6884 2.6124 -0.2341 0.1193  -0.4765 162 ILE A O   
1229 C CB  . ILE A 162 ? 1.3676 1.6321 2.5994 -0.1770 0.0846  -0.4687 162 ILE A CB  
1230 C CG1 . ILE A 162 ? 1.4052 1.6980 2.6869 -0.1588 0.0744  -0.4837 162 ILE A CG1 
1231 C CG2 . ILE A 162 ? 1.1997 1.4514 2.3977 -0.1955 0.1054  -0.4709 162 ILE A CG2 
1232 C CD1 . ILE A 162 ? 1.5130 1.7862 2.7847 -0.1406 0.0618  -0.4688 162 ILE A CD1 
1233 N N   . CYS A 163 ? 1.8187 2.0401 2.9835 -0.2017 0.0851  -0.4437 163 CYS A N   
1234 C CA  . CYS A 163 ? 1.7025 1.8909 2.8169 -0.2166 0.0903  -0.4300 163 CYS A CA  
1235 C C   . CYS A 163 ? 1.8650 2.0689 2.9866 -0.2389 0.1015  -0.4449 163 CYS A C   
1236 O O   . CYS A 163 ? 2.5236 2.7112 3.6097 -0.2621 0.1168  -0.4456 163 CYS A O   
1237 C CB  . CYS A 163 ? 1.6445 1.8087 2.7410 -0.2008 0.0713  -0.4087 163 CYS A CB  
1238 S SG  . CYS A 163 ? 1.7427 1.8840 2.8225 -0.1767 0.0572  -0.3870 163 CYS A SG  
1239 N N   . LEU A 164 ? 1.6484 1.8827 2.8156 -0.2317 0.0926  -0.4566 164 LEU A N   
1240 C CA  . LEU A 164 ? 1.5560 1.8112 2.7395 -0.2508 0.1006  -0.4723 164 LEU A CA  
1241 C C   . LEU A 164 ? 1.4104 1.6888 2.6021 -0.2747 0.1251  -0.4938 164 LEU A C   
1242 O O   . LEU A 164 ? 1.1103 1.3827 2.2780 -0.3015 0.1402  -0.4984 164 LEU A O   
1243 C CB  . LEU A 164 ? 1.4624 1.7493 2.6995 -0.2358 0.0847  -0.4832 164 LEU A CB  
1244 C CG  . LEU A 164 ? 1.3979 1.6630 2.6248 -0.2190 0.0623  -0.4647 164 LEU A CG  
1245 C CD1 . LEU A 164 ? 1.2159 1.5089 2.4953 -0.1993 0.0438  -0.4745 164 LEU A CD1 
1246 C CD2 . LEU A 164 ? 1.3684 1.6147 2.5648 -0.2362 0.0646  -0.4586 164 LEU A CD2 
1247 N N   . ARG A 165 ? 1.5243 1.8275 2.7481 -0.2649 0.1286  -0.5068 165 ARG A N   
1248 C CA  . ARG A 165 ? 1.6192 1.9487 2.8557 -0.2847 0.1520  -0.5294 165 ARG A CA  
1249 C C   . ARG A 165 ? 1.8331 2.1265 3.0081 -0.3076 0.1694  -0.5193 165 ARG A C   
1250 O O   . ARG A 165 ? 1.8718 2.1741 3.0367 -0.3357 0.1901  -0.5328 165 ARG A O   
1251 C CB  . ARG A 165 ? 1.6499 2.0233 2.9459 -0.2702 0.1510  -0.5521 165 ARG A CB  
1252 C CG  . ARG A 165 ? 1.7061 2.1184 3.0519 -0.2714 0.1459  -0.5705 165 ARG A CG  
1253 C CD  . ARG A 165 ? 2.2149 2.6638 3.6235 -0.2463 0.1303  -0.5870 165 ARG A CD  
1254 N NE  . ARG A 165 ? 2.3093 2.7412 3.7245 -0.2186 0.1016  -0.5700 165 ARG A NE  
1255 C CZ  . ARG A 165 ? 2.4523 2.9066 3.9147 -0.1947 0.0841  -0.5808 165 ARG A CZ  
1256 N NH1 . ARG A 165 ? 2.7694 3.2603 4.2736 -0.1916 0.0913  -0.6064 165 ARG A NH1 
1257 N NH2 . ARG A 165 ? 2.2063 2.6447 3.6722 -0.1735 0.0586  -0.5661 165 ARG A NH2 
1258 N N   . ALA A 166 ? 2.0079 2.2605 3.1420 -0.2953 0.1600  -0.4958 166 ALA A N   
1259 C CA  . ALA A 166 ? 1.8375 2.0498 2.9104 -0.3122 0.1715  -0.4838 166 ALA A CA  
1260 C C   . ALA A 166 ? 1.7249 1.9127 2.7583 -0.3352 0.1764  -0.4774 166 ALA A C   
1261 O O   . ALA A 166 ? 1.4964 1.6533 2.4793 -0.3560 0.1889  -0.4725 166 ALA A O   
1262 C CB  . ALA A 166 ? 1.7793 1.9570 2.8239 -0.2910 0.1569  -0.4609 166 ALA A CB  
1263 N N   . GLY A 167 ? 1.5318 1.7246 2.5803 -0.3291 0.1634  -0.4737 167 GLY A N   
1264 C CA  . GLY A 167 ? 1.4355 1.5967 2.4415 -0.3454 0.1625  -0.4628 167 GLY A CA  
1265 C C   . GLY A 167 ? 1.4706 1.5800 2.4239 -0.3323 0.1481  -0.4356 167 GLY A C   
1266 O O   . GLY A 167 ? 1.6210 1.6913 2.5212 -0.3481 0.1505  -0.4251 167 GLY A O   
1267 N N   . VAL A 168 ? 1.3639 1.4732 2.3323 -0.3032 0.1326  -0.4248 168 VAL A N   
1268 C CA  . VAL A 168 ? 1.3058 1.3738 2.2341 -0.2874 0.1172  -0.4005 168 VAL A CA  
1269 C C   . VAL A 168 ? 1.3547 1.4248 2.2978 -0.2723 0.0996  -0.3929 168 VAL A C   
1270 O O   . VAL A 168 ? 1.4521 1.5557 2.4445 -0.2593 0.0922  -0.4012 168 VAL A O   
1271 C CB  . VAL A 168 ? 1.2775 1.3383 2.2040 -0.2677 0.1115  -0.3911 168 VAL A CB  
1272 C CG1 . VAL A 168 ? 1.1224 1.1845 2.0387 -0.2826 0.1289  -0.4011 168 VAL A CG1 
1273 C CG2 . VAL A 168 ? 1.2951 1.3860 2.2724 -0.2419 0.0984  -0.3925 168 VAL A CG2 
1274 N N   . ALA A 169 ? 1.3403 1.3722 2.2380 -0.2747 0.0924  -0.3778 169 ALA A N   
1275 C CA  . ALA A 169 ? 1.4781 1.5063 2.3811 -0.2629 0.0767  -0.3701 169 ALA A CA  
1276 C C   . ALA A 169 ? 1.3992 1.4401 2.3315 -0.2327 0.0606  -0.3620 169 ALA A C   
1277 O O   . ALA A 169 ? 1.9591 1.9846 2.8756 -0.2184 0.0558  -0.3497 169 ALA A O   
1278 C CB  . ALA A 169 ? 1.8621 1.8421 2.7057 -0.2674 0.0712  -0.3542 169 ALA A CB  
1279 N N   . VAL A 170 ? 1.2061 1.2741 2.1799 -0.2239 0.0517  -0.3689 170 VAL A N   
1280 C CA  . VAL A 170 ? 1.1947 1.2705 2.1916 -0.1971 0.0350  -0.3604 170 VAL A CA  
1281 C C   . VAL A 170 ? 1.1249 1.1839 2.1077 -0.1893 0.0207  -0.3499 170 VAL A C   
1282 O O   . VAL A 170 ? 1.1153 1.1635 2.0804 -0.2047 0.0237  -0.3526 170 VAL A O   
1283 C CB  . VAL A 170 ? 1.2938 1.4110 2.3490 -0.1887 0.0327  -0.3759 170 VAL A CB  
1284 C CG1 . VAL A 170 ? 1.2290 1.3621 2.2965 -0.1964 0.0475  -0.3875 170 VAL A CG1 
1285 C CG2 . VAL A 170 ? 1.3976 1.5410 2.4876 -0.1963 0.0307  -0.3918 170 VAL A CG2 
1286 N N   . PRO A 171 ? 1.2814 1.3360 2.2688 -0.1664 0.0050  -0.3375 171 PRO A N   
1287 C CA  . PRO A 171 ? 1.3329 1.3762 2.3129 -0.1585 -0.0087 -0.3302 171 PRO A CA  
1288 C C   . PRO A 171 ? 1.3461 1.4200 2.3710 -0.1617 -0.0131 -0.3461 171 PRO A C   
1289 O O   . PRO A 171 ? 1.3419 1.4463 2.4081 -0.1599 -0.0109 -0.3591 171 PRO A O   
1290 C CB  . PRO A 171 ? 1.5368 1.5722 2.5136 -0.1345 -0.0217 -0.3149 171 PRO A CB  
1291 C CG  . PRO A 171 ? 1.6836 1.7193 2.6562 -0.1321 -0.0138 -0.3118 171 PRO A CG  
1292 C CD  . PRO A 171 ? 1.4043 1.4635 2.4022 -0.1483 0.0000  -0.3300 171 PRO A CD  
1293 N N   . GLY A 172 ? 1.4115 1.4763 2.4278 -0.1659 -0.0201 -0.3456 172 GLY A N   
1294 C CA  . GLY A 172 ? 1.5585 1.6505 2.6164 -0.1681 -0.0268 -0.3602 172 GLY A CA  
1295 C C   . GLY A 172 ? 1.4317 1.5436 2.5281 -0.1470 -0.0406 -0.3617 172 GLY A C   
1296 O O   . GLY A 172 ? 1.3113 1.4062 2.3931 -0.1293 -0.0529 -0.3465 172 GLY A O   
1297 N N   . GLY A 173 ? 1.3371 1.4845 2.4811 -0.1497 -0.0380 -0.3806 173 GLY A N   
1298 C CA  . GLY A 173 ? 1.4599 1.6258 2.6426 -0.1308 -0.0529 -0.3849 173 GLY A CA  
1299 C C   . GLY A 173 ? 1.5747 1.7802 2.8082 -0.1354 -0.0471 -0.4085 173 GLY A C   
1300 O O   . GLY A 173 ? 1.5772 1.7971 2.8146 -0.1533 -0.0286 -0.4207 173 GLY A O   
1301 N N   . THR A 174 ? 1.6342 1.8568 2.9062 -0.1189 -0.0636 -0.4157 174 THR A N   
1302 C CA  . THR A 174 ? 1.5725 1.8327 2.8945 -0.1189 -0.0604 -0.4388 174 THR A CA  
1303 C C   . THR A 174 ? 1.7630 2.0203 3.0823 -0.1095 -0.0565 -0.4339 174 THR A C   
1304 O O   . THR A 174 ? 1.8265 2.0553 3.1112 -0.1008 -0.0600 -0.4129 174 THR A O   
1305 C CB  . THR A 174 ? 1.5687 1.8474 2.9348 -0.1040 -0.0824 -0.4508 174 THR A CB  
1306 O OG1 . THR A 174 ? 1.7519 2.0095 3.0984 -0.1012 -0.0963 -0.4392 174 THR A OG1 
1307 C CG2 . THR A 174 ? 1.3873 1.7104 2.8071 -0.1115 -0.0768 -0.4806 174 THR A CG2 
1308 N N   . SER A 175 ? 1.4950 1.7843 2.8542 -0.1108 -0.0503 -0.4550 175 SER A N   
1309 C CA  . SER A 175 ? 1.3770 1.6683 2.7422 -0.1012 -0.0484 -0.4550 175 SER A CA  
1310 C C   . SER A 175 ? 1.3455 1.6561 2.7569 -0.0823 -0.0681 -0.4682 175 SER A C   
1311 O O   . SER A 175 ? 1.3523 1.6861 2.7939 -0.0797 -0.0635 -0.4851 175 SER A O   
1312 C CB  . SER A 175 ? 1.2655 1.5727 2.6311 -0.1186 -0.0236 -0.4677 175 SER A CB  
1313 O OG  . SER A 175 ? 1.5144 1.8557 2.9138 -0.1329 -0.0140 -0.4921 175 SER A OG  
1314 N N   . GLU A 176 ? 1.4091 1.7075 2.8227 -0.0693 -0.0906 -0.4604 176 GLU A N   
1315 C CA  . GLU A 176 ? 1.7892 2.1023 3.2448 -0.0521 -0.1130 -0.4736 176 GLU A CA  
1316 C C   . GLU A 176 ? 1.7142 1.9950 3.1484 -0.0339 -0.1351 -0.4526 176 GLU A C   
1317 O O   . GLU A 176 ? 1.7666 2.0203 3.1653 -0.0339 -0.1401 -0.4327 176 GLU A O   
1318 C CB  . GLU A 176 ? 2.0961 2.4288 3.5801 -0.0564 -0.1206 -0.4890 176 GLU A CB  
1319 C CG  . GLU A 176 ? 2.4093 2.7619 3.9430 -0.0393 -0.1444 -0.5078 176 GLU A CG  
1320 C CD  . GLU A 176 ? 2.8462 3.2356 4.4264 -0.0367 -0.1382 -0.5344 176 GLU A CD  
1321 O OE1 . GLU A 176 ? 3.0358 3.4569 4.6358 -0.0534 -0.1175 -0.5528 176 GLU A OE1 
1322 O OE2 . GLU A 176 ? 3.1436 3.5301 4.7395 -0.0187 -0.1539 -0.5375 176 GLU A OE2 
1323 N N   . VAL A 177 ? 1.5138 1.7979 2.9692 -0.0192 -0.1475 -0.4583 177 VAL A N   
1324 C CA  . VAL A 177 ? 1.5693 1.8244 3.0083 -0.0028 -0.1696 -0.4413 177 VAL A CA  
1325 C C   . VAL A 177 ? 1.5387 1.7840 2.9832 0.0057  -0.1934 -0.4400 177 VAL A C   
1326 O O   . VAL A 177 ? 2.0767 2.3453 3.5581 0.0064  -0.2007 -0.4603 177 VAL A O   
1327 C CB  . VAL A 177 ? 1.6772 1.9396 3.1423 0.0101  -0.1795 -0.4519 177 VAL A CB  
1328 C CG1 . VAL A 177 ? 1.9918 2.2195 3.4238 0.0199  -0.1917 -0.4283 177 VAL A CG1 
1329 C CG2 . VAL A 177 ? 1.5921 1.8812 3.0751 0.0011  -0.1569 -0.4683 177 VAL A CG2 
1330 N N   . LEU A 178 ? 1.4249 1.6356 2.8329 0.0126  -0.2059 -0.4165 178 LEU A N   
1331 C CA  . LEU A 178 ? 1.4764 1.6693 2.8778 0.0202  -0.2284 -0.4104 178 LEU A CA  
1332 C C   . LEU A 178 ? 1.6800 1.8463 3.0712 0.0357  -0.2525 -0.3994 178 LEU A C   
1333 O O   . LEU A 178 ? 1.9928 2.1296 3.3427 0.0363  -0.2540 -0.3761 178 LEU A O   
1334 C CB  . LEU A 178 ? 1.5914 1.7643 2.9507 0.0110  -0.2197 -0.3916 178 LEU A CB  
1335 C CG  . LEU A 178 ? 1.8906 2.0809 3.2486 -0.0060 -0.1964 -0.3983 178 LEU A CG  
1336 C CD1 . LEU A 178 ? 2.0747 2.2381 3.3814 -0.0126 -0.1861 -0.3751 178 LEU A CD1 
1337 C CD2 . LEU A 178 ? 1.8394 2.0490 3.2285 -0.0092 -0.2042 -0.4167 178 LEU A CD2 
1338 N N   . ARG A 179 ? 1.5771 1.7547 3.0067 0.0475  -0.2713 -0.4177 179 ARG A N   
1339 C CA  . ARG A 179 ? 1.6984 1.8514 3.1216 0.0616  -0.2946 -0.4106 179 ARG A CA  
1340 C C   . ARG A 179 ? 1.8151 1.9341 3.2105 0.0676  -0.3177 -0.3952 179 ARG A C   
1341 O O   . ARG A 179 ? 1.9256 2.0185 3.3085 0.0773  -0.3382 -0.3868 179 ARG A O   
1342 C CB  . ARG A 179 ? 1.5394 1.7139 3.0096 0.0724  -0.3057 -0.4354 179 ARG A CB  
1343 C CG  . ARG A 179 ? 1.6924 1.8883 3.1709 0.0651  -0.2803 -0.4414 179 ARG A CG  
1344 C CD  . ARG A 179 ? 1.9904 2.2016 3.5067 0.0768  -0.2900 -0.4623 179 ARG A CD  
1345 N NE  . ARG A 179 ? 2.1185 2.3566 3.6477 0.0680  -0.2631 -0.4729 179 ARG A NE  
1346 C CZ  . ARG A 179 ? 2.1877 2.4609 3.7397 0.0562  -0.2407 -0.4900 179 ARG A CZ  
1347 N NH1 . ARG A 179 ? 2.3635 2.6516 3.9293 0.0507  -0.2406 -0.4981 179 ARG A NH1 
1348 N NH2 . ARG A 179 ? 2.0605 2.3529 3.6196 0.0486  -0.2182 -0.4986 179 ARG A NH2 
1349 N N   . SER A 180 ? 1.7292 1.8454 3.1104 0.0608  -0.3142 -0.3901 180 SER A N   
1350 C CA  . SER A 180 ? 1.7737 1.8563 3.1252 0.0659  -0.3351 -0.3754 180 SER A CA  
1351 C C   . SER A 180 ? 2.0055 2.0774 3.3190 0.0549  -0.3192 -0.3586 180 SER A C   
1352 O O   . SER A 180 ? 2.2566 2.3498 3.5757 0.0439  -0.2970 -0.3638 180 SER A O   
1353 C CB  . SER A 180 ? 1.9773 2.0636 3.3605 0.0757  -0.3619 -0.3932 180 SER A CB  
1354 O OG  . SER A 180 ? 1.9129 2.0222 3.3145 0.0680  -0.3535 -0.4053 180 SER A OG  
1355 N N   . GLU A 181 ? 2.1358 2.1731 3.4105 0.0580  -0.3327 -0.3399 181 GLU A N   
1356 C CA  . GLU A 181 ? 2.2622 2.2849 3.4975 0.0501  -0.3211 -0.3236 181 GLU A CA  
1357 C C   . GLU A 181 ? 2.3880 2.4256 3.6403 0.0454  -0.3205 -0.3366 181 GLU A C   
1358 O O   . GLU A 181 ? 2.0510 2.0928 3.2857 0.0353  -0.3008 -0.3312 181 GLU A O   
1359 C CB  . GLU A 181 ? 2.1632 2.1469 3.3550 0.0545  -0.3366 -0.3032 181 GLU A CB  
1360 C CG  . GLU A 181 ? 2.3514 2.3185 3.5260 0.0579  -0.3401 -0.2904 181 GLU A CG  
1361 C CD  . GLU A 181 ? 2.4954 2.4264 3.6203 0.0577  -0.3476 -0.2680 181 GLU A CD  
1362 O OE1 . GLU A 181 ? 2.6435 2.5513 3.7560 0.0622  -0.3693 -0.2663 181 GLU A OE1 
1363 O OE2 . GLU A 181 ? 2.2855 2.2124 3.3839 0.0524  -0.3310 -0.2526 181 GLU A OE2 
1364 N N   . ALA A 182 ? 2.2503 2.2941 3.5354 0.0528  -0.3430 -0.3534 182 ALA A N   
1365 C CA  . ALA A 182 ? 1.7646 1.8236 3.0701 0.0485  -0.3458 -0.3674 182 ALA A CA  
1366 C C   . ALA A 182 ? 1.8936 1.9892 3.2236 0.0357  -0.3188 -0.3807 182 ALA A C   
1367 O O   . ALA A 182 ? 2.4556 2.5550 3.7744 0.0247  -0.3065 -0.3797 182 ALA A O   
1368 C CB  . ALA A 182 ? 1.5130 1.5758 2.8552 0.0602  -0.3756 -0.3852 182 ALA A CB  
1369 N N   . GLU A 183 ? 1.6857 1.8054 3.0463 0.0369  -0.3107 -0.3928 183 GLU A N   
1370 C CA  . GLU A 183 ? 1.9279 2.0823 3.3121 0.0243  -0.2849 -0.4067 183 GLU A CA  
1371 C C   . GLU A 183 ? 2.2333 2.3762 3.5745 0.0115  -0.2596 -0.3886 183 GLU A C   
1372 O O   . GLU A 183 ? 2.3292 2.4861 3.6710 -0.0021 -0.2428 -0.3942 183 GLU A O   
1373 C CB  . GLU A 183 ? 1.9992 2.1760 3.4165 0.0290  -0.2809 -0.4204 183 GLU A CB  
1374 C CG  . GLU A 183 ? 2.2752 2.4698 3.7421 0.0417  -0.3046 -0.4437 183 GLU A CG  
1375 C CD  . GLU A 183 ? 2.4361 2.6467 3.9312 0.0495  -0.3042 -0.4559 183 GLU A CD  
1376 O OE1 . GLU A 183 ? 2.7345 2.9206 4.2017 0.0547  -0.3058 -0.4390 183 GLU A OE1 
1377 O OE2 . GLU A 183 ? 2.2237 2.4713 3.7681 0.0503  -0.3022 -0.4825 183 GLU A OE2 
1378 N N   . VAL A 184 ? 2.1897 2.3065 3.4939 0.0161  -0.2582 -0.3674 184 VAL A N   
1379 C CA  . VAL A 184 ? 2.0175 2.1209 3.2797 0.0073  -0.2371 -0.3493 184 VAL A CA  
1380 C C   . VAL A 184 ? 2.1766 2.2660 3.4126 0.0012  -0.2364 -0.3425 184 VAL A C   
1381 O O   . VAL A 184 ? 2.3142 2.4068 3.5347 -0.0105 -0.2174 -0.3407 184 VAL A O   
1382 C CB  . VAL A 184 ? 1.9580 2.0366 3.1872 0.0146  -0.2394 -0.3284 184 VAL A CB  
1383 C CG1 . VAL A 184 ? 1.7621 1.8269 2.9484 0.0074  -0.2201 -0.3105 184 VAL A CG1 
1384 C CG2 . VAL A 184 ? 2.0173 2.1071 3.2690 0.0197  -0.2399 -0.3342 184 VAL A CG2 
1385 N N   . VAL A 185 ? 2.1302 2.2010 3.3591 0.0095  -0.2586 -0.3387 185 VAL A N   
1386 C CA  . VAL A 185 ? 2.1041 2.1577 3.3068 0.0057  -0.2620 -0.3321 185 VAL A CA  
1387 C C   . VAL A 185 ? 2.2167 2.2941 3.4446 -0.0063 -0.2538 -0.3495 185 VAL A C   
1388 O O   . VAL A 185 ? 2.0978 2.1674 3.3002 -0.0163 -0.2416 -0.3439 185 VAL A O   
1389 C CB  . VAL A 185 ? 2.0141 2.0406 3.2013 0.0166  -0.2880 -0.3244 185 VAL A CB  
1390 C CG1 . VAL A 185 ? 2.1856 2.1979 3.3528 0.0125  -0.2931 -0.3221 185 VAL A CG1 
1391 C CG2 . VAL A 185 ? 1.9507 1.9505 3.1005 0.0237  -0.2901 -0.3036 185 VAL A CG2 
1392 N N   . GLU A 186 ? 2.4416 2.5476 3.7193 -0.0054 -0.2612 -0.3712 186 GLU A N   
1393 C CA  . GLU A 186 ? 2.5094 2.6440 3.8186 -0.0179 -0.2537 -0.3909 186 GLU A CA  
1394 C C   . GLU A 186 ? 2.3291 2.4744 3.6257 -0.0341 -0.2241 -0.3900 186 GLU A C   
1395 O O   . GLU A 186 ? 2.3097 2.4562 3.5958 -0.0482 -0.2139 -0.3922 186 GLU A O   
1396 C CB  . GLU A 186 ? 2.7015 2.8657 4.0682 -0.0121 -0.2698 -0.4156 186 GLU A CB  
1397 C CG  . GLU A 186 ? 2.7887 2.9847 4.1936 -0.0117 -0.2593 -0.4313 186 GLU A CG  
1398 C CD  . GLU A 186 ? 2.9765 3.2053 4.4013 -0.0303 -0.2340 -0.4466 186 GLU A CD  
1399 O OE1 . GLU A 186 ? 3.1709 3.4204 4.6232 -0.0382 -0.2373 -0.4631 186 GLU A OE1 
1400 O OE2 . GLU A 186 ? 2.7162 2.9489 4.1280 -0.0379 -0.2118 -0.4422 186 GLU A OE2 
1401 N N   . ALA A 187 ? 2.0292 2.1796 3.3251 -0.0322 -0.2120 -0.3866 187 ALA A N   
1402 C CA  . ALA A 187 ? 1.9780 2.1356 3.2600 -0.0461 -0.1853 -0.3851 187 ALA A CA  
1403 C C   . ALA A 187 ? 2.1438 2.2713 3.3728 -0.0523 -0.1766 -0.3658 187 ALA A C   
1404 O O   . ALA A 187 ? 1.9623 2.0917 3.1785 -0.0679 -0.1607 -0.3682 187 ALA A O   
1405 C CB  . ALA A 187 ? 1.7442 1.9069 3.0310 -0.0400 -0.1783 -0.3825 187 ALA A CB  
1406 N N   . ILE A 188 ? 2.2180 2.3171 3.4158 -0.0399 -0.1879 -0.3472 188 ILE A N   
1407 C CA  . ILE A 188 ? 1.9412 2.0106 3.0884 -0.0414 -0.1825 -0.3286 188 ILE A CA  
1408 C C   . ILE A 188 ? 2.0267 2.0901 3.1659 -0.0507 -0.1852 -0.3332 188 ILE A C   
1409 O O   . ILE A 188 ? 1.9345 1.9845 3.0420 -0.0602 -0.1726 -0.3267 188 ILE A O   
1410 C CB  . ILE A 188 ? 1.6152 1.6596 2.7367 -0.0259 -0.1961 -0.3109 188 ILE A CB  
1411 C CG1 . ILE A 188 ? 1.5000 1.5465 2.6208 -0.0194 -0.1906 -0.3033 188 ILE A CG1 
1412 C CG2 . ILE A 188 ? 1.7560 1.7711 2.8297 -0.0254 -0.1953 -0.2950 188 ILE A CG2 
1413 C CD1 . ILE A 188 ? 1.5338 1.5560 2.6256 -0.0074 -0.2012 -0.2852 188 ILE A CD1 
1414 N N   . HIS A 189 ? 1.8207 1.8908 2.9856 -0.0469 -0.2038 -0.3433 189 HIS A N   
1415 C CA  . HIS A 189 ? 1.5919 1.6569 2.7526 -0.0553 -0.2095 -0.3485 189 HIS A CA  
1416 C C   . HIS A 189 ? 1.6291 1.7284 2.8312 -0.0706 -0.2009 -0.3708 189 HIS A C   
1417 O O   . HIS A 189 ? 2.0869 2.2057 3.3283 -0.0686 -0.2150 -0.3864 189 HIS A O   
1418 C CB  . HIS A 189 ? 1.4712 1.5275 2.6423 -0.0436 -0.2358 -0.3501 189 HIS A CB  
1419 C CG  . HIS A 189 ? 1.7283 1.7537 2.8662 -0.0283 -0.2488 -0.3316 189 HIS A CG  
1420 N ND1 . HIS A 189 ? 1.6844 1.6997 2.8304 -0.0172 -0.2737 -0.3327 189 HIS A ND1 
1421 C CD2 . HIS A 189 ? 2.1451 2.1481 3.2422 -0.0229 -0.2413 -0.3127 189 HIS A CD2 
1422 C CE1 . HIS A 189 ? 1.8655 1.8517 2.9738 -0.0070 -0.2799 -0.3144 189 HIS A CE1 
1423 N NE2 . HIS A 189 ? 2.3310 2.3114 3.4109 -0.0101 -0.2599 -0.3025 189 HIS A NE2 
1424 N N   . ARG A 190 ? 1.7417 1.8480 2.9342 -0.0860 -0.1783 -0.3727 190 ARG A N   
1425 C CA  . ARG A 190 ? 1.7912 1.9304 3.0183 -0.1037 -0.1657 -0.3933 190 ARG A CA  
1426 C C   . ARG A 190 ? 1.7094 1.8433 2.9090 -0.1174 -0.1411 -0.3880 190 ARG A C   
1427 O O   . ARG A 190 ? 1.6686 1.8289 2.8920 -0.1301 -0.1256 -0.4021 190 ARG A O   
1428 C CB  . ARG A 190 ? 1.9270 2.1026 3.2098 -0.0969 -0.1702 -0.4117 190 ARG A CB  
1429 C CG  . ARG A 190 ? 2.0836 2.2947 3.4167 -0.1061 -0.1748 -0.4367 190 ARG A CG  
1430 C CD  . ARG A 190 ? 2.0326 2.2724 3.4189 -0.0915 -0.1888 -0.4533 190 ARG A CD  
1431 N NE  . ARG A 190 ? 2.3459 2.6077 3.7489 -0.0944 -0.1707 -0.4611 190 ARG A NE  
1432 C CZ  . ARG A 190 ? 2.5256 2.8156 3.9751 -0.0837 -0.1777 -0.4778 190 ARG A CZ  
1433 N NH1 . ARG A 190 ? 2.7692 3.0784 4.2614 -0.0749 -0.1984 -0.4946 190 ARG A NH1 
1434 N NH2 . ARG A 190 ? 2.3593 2.6584 3.8132 -0.0817 -0.1646 -0.4791 190 ARG A NH2 
1435 N N   . LEU A 191 ? 1.6886 1.7872 2.8367 -0.1141 -0.1382 -0.3677 191 LEU A N   
1436 C CA  . LEU A 191 ? 1.7412 1.8291 2.8591 -0.1223 -0.1187 -0.3599 191 LEU A CA  
1437 C C   . LEU A 191 ? 1.8722 1.9396 2.9536 -0.1400 -0.1096 -0.3569 191 LEU A C   
1438 O O   . LEU A 191 ? 2.2537 2.3245 3.3434 -0.1499 -0.1152 -0.3653 191 LEU A O   
1439 C CB  . LEU A 191 ? 1.8304 1.8943 2.9183 -0.1041 -0.1231 -0.3401 191 LEU A CB  
1440 C CG  . LEU A 191 ? 1.9114 1.9871 3.0093 -0.0990 -0.1134 -0.3388 191 LEU A CG  
1441 C CD1 . LEU A 191 ? 1.7034 1.8161 2.8498 -0.1065 -0.1067 -0.3593 191 LEU A CD1 
1442 C CD2 . LEU A 191 ? 1.8345 1.9000 2.9284 -0.0781 -0.1272 -0.3260 191 LEU A CD2 
1443 N N   . SER A 192 ? 1.8548 1.9001 2.8961 -0.1439 -0.0967 -0.3453 192 SER A N   
1444 C CA  . SER A 192 ? 1.9846 2.0094 2.9897 -0.1631 -0.0859 -0.3439 192 SER A CA  
1445 C C   . SER A 192 ? 2.1284 2.1131 3.0850 -0.1553 -0.0957 -0.3276 192 SER A C   
1446 O O   . SER A 192 ? 2.5535 2.5161 3.4780 -0.1696 -0.0922 -0.3263 192 SER A O   
1447 C CB  . SER A 192 ? 1.9286 1.9512 2.9176 -0.1732 -0.0673 -0.3431 192 SER A CB  
1448 O OG  . SER A 192 ? 2.0556 2.1155 3.0893 -0.1780 -0.0583 -0.3583 192 SER A OG  
1449 N N   . CYS A 193 ? 1.9954 1.9705 2.9460 -0.1330 -0.1080 -0.3158 193 CYS A N   
1450 C CA  . CYS A 193 ? 2.2956 2.2342 3.1987 -0.1225 -0.1149 -0.2998 193 CYS A CA  
1451 C C   . CYS A 193 ? 2.6600 2.5739 3.5208 -0.1327 -0.1024 -0.2941 193 CYS A C   
1452 O O   . CYS A 193 ? 3.2323 3.1521 4.0928 -0.1344 -0.0907 -0.2931 193 CYS A O   
1453 C CB  . CYS A 193 ? 1.9745 1.8999 2.8702 -0.1227 -0.1294 -0.3006 193 CYS A CB  
1454 S SG  . CYS A 193 ? 1.9621 1.9052 2.8952 -0.1054 -0.1483 -0.3029 193 CYS A SG  
1455 N N   . GLY A 194 ? 2.3458 2.2306 3.1705 -0.1400 -0.1062 -0.2909 194 GLY A N   
1456 C CA  . GLY A 194 ? 2.1436 1.9959 2.9198 -0.1457 -0.0993 -0.2833 194 GLY A CA  
1457 C C   . GLY A 194 ? 2.2658 2.0882 3.0042 -0.1252 -0.1095 -0.2689 194 GLY A C   
1458 O O   . GLY A 194 ? 2.3096 2.1418 3.0606 -0.1062 -0.1155 -0.2630 194 GLY A O   
1459 N N   . THR A 195 ? 2.5672 2.3530 3.2590 -0.1298 -0.1118 -0.2642 195 THR A N   
1460 C CA  . THR A 195 ? 2.6200 2.3771 3.2745 -0.1105 -0.1213 -0.2526 195 THR A CA  
1461 C C   . THR A 195 ? 2.7469 2.5128 3.4037 -0.0921 -0.1172 -0.2446 195 THR A C   
1462 O O   . THR A 195 ? 2.8319 2.5998 3.4856 -0.0967 -0.1071 -0.2444 195 THR A O   
1463 C CB  . THR A 195 ? 2.6082 2.3235 3.2111 -0.1190 -0.1230 -0.2500 195 THR A CB  
1464 O OG1 . THR A 195 ? 2.7412 2.4523 3.3327 -0.1263 -0.1116 -0.2495 195 THR A OG1 
1465 C CG2 . THR A 195 ? 2.3888 2.0957 2.9893 -0.1406 -0.1262 -0.2581 195 THR A CG2 
1466 N N   . ALA A 196 ? 2.9291 2.7005 3.5916 -0.0726 -0.1251 -0.2383 196 ALA A N   
1467 C CA  . ALA A 196 ? 2.8321 2.6157 3.5008 -0.0558 -0.1220 -0.2309 196 ALA A CA  
1468 C C   . ALA A 196 ? 2.7436 2.5168 3.3956 -0.0365 -0.1318 -0.2230 196 ALA A C   
1469 O O   . ALA A 196 ? 2.8268 2.6062 3.4930 -0.0342 -0.1405 -0.2242 196 ALA A O   
1470 C CB  . ALA A 196 ? 2.7039 2.5238 3.4205 -0.0585 -0.1173 -0.2356 196 ALA A CB  
1471 N N   . ALA A 197 ? 2.5835 2.3403 3.2043 -0.0231 -0.1308 -0.2157 197 ALA A N   
1472 C CA  . ALA A 197 ? 2.8156 2.5668 3.4209 -0.0040 -0.1370 -0.2087 197 ALA A CA  
1473 C C   . ALA A 197 ? 3.3600 3.1361 3.9980 0.0003  -0.1403 -0.2073 197 ALA A C   
1474 O O   . ALA A 197 ? 3.6577 3.4265 4.2898 0.0053  -0.1497 -0.2062 197 ALA A O   
1475 C CB  . ALA A 197 ? 2.6837 2.4315 3.2704 0.0095  -0.1317 -0.2029 197 ALA A CB  
1476 N N   . ALA A 198 ? 3.5603 3.3630 4.2308 -0.0019 -0.1337 -0.2076 198 ALA A N   
1477 C CA  . ALA A 198 ? 3.2816 3.1057 3.9825 0.0016  -0.1380 -0.2065 198 ALA A CA  
1478 C C   . ALA A 198 ? 3.0809 2.9279 3.8220 -0.0111 -0.1349 -0.2146 198 ALA A C   
1479 O O   . ALA A 198 ? 3.3682 3.2338 4.1296 -0.0103 -0.1285 -0.2136 198 ALA A O   
1480 C CB  . ALA A 198 ? 3.0911 2.9243 3.7887 0.0154  -0.1346 -0.1975 198 ALA A CB  
1481 N N   . ARG A 199 ? 2.7557 2.6020 3.5089 -0.0226 -0.1399 -0.2234 199 ARG A N   
1482 C CA  . ARG A 199 ? 2.5123 2.3814 3.3043 -0.0356 -0.1371 -0.2343 199 ARG A CA  
1483 C C   . ARG A 199 ? 2.3624 2.2553 3.1883 -0.0288 -0.1396 -0.2338 199 ARG A C   
1484 O O   . ARG A 199 ? 2.0291 1.9205 2.8571 -0.0191 -0.1503 -0.2293 199 ARG A O   
1485 C CB  . ARG A 199 ? 2.6510 2.5153 3.4490 -0.0456 -0.1455 -0.2430 199 ARG A CB  
1486 C CG  . ARG A 199 ? 2.9041 2.7455 3.6746 -0.0354 -0.1580 -0.2363 199 ARG A CG  
1487 C CD  . ARG A 199 ? 3.0755 2.9149 3.8578 -0.0431 -0.1698 -0.2447 199 ARG A CD  
1488 N NE  . ARG A 199 ? 3.0788 2.9408 3.9012 -0.0401 -0.1785 -0.2498 199 ARG A NE  
1489 C CZ  . ARG A 199 ? 2.7363 2.5934 3.5637 -0.0338 -0.1945 -0.2499 199 ARG A CZ  
1490 N NH1 . ARG A 199 ? 2.3604 2.2360 3.2221 -0.0295 -0.2027 -0.2538 199 ARG A NH1 
1491 N NH2 . ARG A 199 ? 2.6976 2.5288 3.4935 -0.0310 -0.2033 -0.2459 199 ARG A NH2 
1492 N N   . ARG A 200 ? 2.3108 2.2228 3.1596 -0.0344 -0.1299 -0.2382 200 ARG A N   
1493 C CA  . ARG A 200 ? 1.9781 1.9091 2.8530 -0.0276 -0.1307 -0.2364 200 ARG A CA  
1494 C C   . ARG A 200 ? 2.1189 2.0749 3.0344 -0.0375 -0.1268 -0.2495 200 ARG A C   
1495 O O   . ARG A 200 ? 2.3808 2.3422 3.3014 -0.0508 -0.1170 -0.2585 200 ARG A O   
1496 C CB  . ARG A 200 ? 2.0137 1.9421 2.8710 -0.0192 -0.1229 -0.2254 200 ARG A CB  
1497 C CG  . ARG A 200 ? 2.2355 2.1518 3.0692 -0.0054 -0.1292 -0.2132 200 ARG A CG  
1498 C CD  . ARG A 200 ? 2.0018 1.9177 2.8185 0.0026  -0.1214 -0.2033 200 ARG A CD  
1499 N NE  . ARG A 200 ? 2.0655 1.9625 2.8471 0.0049  -0.1170 -0.2004 200 ARG A NE  
1500 C CZ  . ARG A 200 ? 2.5446 2.4379 3.3069 0.0116  -0.1103 -0.1943 200 ARG A CZ  
1501 N NH1 . ARG A 200 ? 2.6140 2.5227 3.3883 0.0163  -0.1064 -0.1892 200 ARG A NH1 
1502 N NH2 . ARG A 200 ? 2.9353 2.8088 3.6664 0.0137  -0.1087 -0.1939 200 ARG A NH2 
1503 N N   . ALA A 201 ? 2.1826 2.1535 3.1256 -0.0306 -0.1339 -0.2504 201 ALA A N   
1504 C CA  . ALA A 201 ? 1.9367 1.9326 2.9203 -0.0355 -0.1319 -0.2625 201 ALA A CA  
1505 C C   . ALA A 201 ? 1.6725 1.6759 2.6645 -0.0273 -0.1308 -0.2561 201 ALA A C   
1506 O O   . ALA A 201 ? 1.6733 1.6665 2.6504 -0.0167 -0.1377 -0.2438 201 ALA A O   
1507 C CB  . ALA A 201 ? 2.2694 2.2756 3.2833 -0.0353 -0.1461 -0.2736 201 ALA A CB  
1508 N N   . MET A 202 ? 1.5440 1.5657 2.5600 -0.0335 -0.1219 -0.2652 202 MET A N   
1509 C CA  . MET A 202 ? 1.6181 1.6469 2.6419 -0.0281 -0.1190 -0.2605 202 MET A CA  
1510 C C   . MET A 202 ? 1.4835 1.5346 2.5498 -0.0290 -0.1230 -0.2746 202 MET A C   
1511 O O   . MET A 202 ? 1.4998 1.5665 2.5877 -0.0386 -0.1166 -0.2897 202 MET A O   
1512 C CB  . MET A 202 ? 1.7307 1.7560 2.7347 -0.0336 -0.1029 -0.2563 202 MET A CB  
1513 C CG  . MET A 202 ? 1.5498 1.5723 2.5439 -0.0251 -0.1018 -0.2439 202 MET A CG  
1514 S SD  . MET A 202 ? 1.9059 1.9354 2.9003 -0.0331 -0.0856 -0.2474 202 MET A SD  
1515 C CE  . MET A 202 ? 1.5225 1.5317 2.4765 -0.0397 -0.0755 -0.2432 202 MET A CE  
1516 N N   . VAL A 203 ? 1.4779 1.5295 2.5546 -0.0189 -0.1340 -0.2697 203 VAL A N   
1517 C CA  . VAL A 203 ? 1.4106 1.4793 2.5256 -0.0160 -0.1420 -0.2820 203 VAL A CA  
1518 C C   . VAL A 203 ? 1.4053 1.4780 2.5226 -0.0139 -0.1359 -0.2776 203 VAL A C   
1519 O O   . VAL A 203 ? 1.5810 1.6405 2.6795 -0.0072 -0.1408 -0.2628 203 VAL A O   
1520 C CB  . VAL A 203 ? 1.5477 1.6055 2.6654 -0.0052 -0.1634 -0.2771 203 VAL A CB  
1521 C CG1 . VAL A 203 ? 1.5807 1.6493 2.7326 0.0012  -0.1765 -0.2869 203 VAL A CG1 
1522 C CG2 . VAL A 203 ? 1.9160 1.9663 3.0289 -0.0055 -0.1728 -0.2796 203 VAL A CG2 
1523 N N   . LYS A 204 ? 1.2667 1.3576 2.4074 -0.0199 -0.1261 -0.2912 204 LYS A N   
1524 C CA  . LYS A 204 ? 1.2730 1.3663 2.4124 -0.0195 -0.1184 -0.2875 204 LYS A CA  
1525 C C   . LYS A 204 ? 1.2406 1.3475 2.4153 -0.0138 -0.1280 -0.2992 204 LYS A C   
1526 O O   . LYS A 204 ? 1.3176 1.4436 2.5219 -0.0177 -0.1254 -0.3179 204 LYS A O   
1527 C CB  . LYS A 204 ? 1.3310 1.4310 2.4637 -0.0316 -0.0984 -0.2935 204 LYS A CB  
1528 C CG  . LYS A 204 ? 1.4157 1.4994 2.5101 -0.0374 -0.0877 -0.2824 204 LYS A CG  
1529 C CD  . LYS A 204 ? 1.4694 1.5564 2.5569 -0.0478 -0.0706 -0.2871 204 LYS A CD  
1530 C CE  . LYS A 204 ? 1.4618 1.5302 2.5104 -0.0531 -0.0611 -0.2770 204 LYS A CE  
1531 N NZ  . LYS A 204 ? 1.7893 1.8508 2.8267 -0.0589 -0.0613 -0.2796 204 LYS A NZ  
1532 N N   . LEU A 205 ? 1.2572 1.3535 2.4273 -0.0050 -0.1394 -0.2885 205 LEU A N   
1533 C CA  . LEU A 205 ? 1.2263 1.3292 2.4252 0.0022  -0.1526 -0.2977 205 LEU A CA  
1534 C C   . LEU A 205 ? 1.3230 1.4439 2.5423 -0.0024 -0.1399 -0.3117 205 LEU A C   
1535 O O   . LEU A 205 ? 1.4108 1.5294 2.6130 -0.0078 -0.1258 -0.3049 205 LEU A O   
1536 C CB  . LEU A 205 ? 1.0269 1.1108 2.2089 0.0095  -0.1653 -0.2811 205 LEU A CB  
1537 C CG  . LEU A 205 ? 1.0393 1.1043 2.2002 0.0140  -0.1787 -0.2681 205 LEU A CG  
1538 C CD1 . LEU A 205 ? 1.1180 1.1652 2.2564 0.0171  -0.1858 -0.2502 205 LEU A CD1 
1539 C CD2 . LEU A 205 ? 0.9877 1.0531 2.1714 0.0202  -0.1978 -0.2799 205 LEU A CD2 
1540 N N   . ASP A 206 ? 1.2769 1.4162 2.5337 0.0001  -0.1457 -0.3324 206 ASP A N   
1541 C CA  . ASP A 206 ? 1.3154 1.4771 2.5946 -0.0067 -0.1307 -0.3508 206 ASP A CA  
1542 C C   . ASP A 206 ? 1.5734 1.7329 2.8498 -0.0054 -0.1257 -0.3482 206 ASP A C   
1543 O O   . ASP A 206 ? 1.5686 1.7379 2.8437 -0.0145 -0.1077 -0.3549 206 ASP A O   
1544 C CB  . ASP A 206 ? 1.5305 1.7154 2.8527 -0.0034 -0.1386 -0.3749 206 ASP A CB  
1545 C CG  . ASP A 206 ? 2.1008 2.3127 3.4488 -0.0112 -0.1220 -0.3965 206 ASP A CG  
1546 O OD1 . ASP A 206 ? 2.0479 2.2645 3.3807 -0.0255 -0.1013 -0.3967 206 ASP A OD1 
1547 O OD2 . ASP A 206 ? 2.8230 3.0496 4.2043 -0.0031 -0.1302 -0.4131 206 ASP A OD2 
1548 N N   . ALA A 207 ? 1.6527 1.7978 2.9268 0.0048  -0.1423 -0.3390 207 ALA A N   
1549 C CA  . ALA A 207 ? 1.4254 1.5672 2.6992 0.0070  -0.1412 -0.3373 207 ALA A CA  
1550 C C   . ALA A 207 ? 1.6364 1.7721 2.8804 -0.0026 -0.1221 -0.3250 207 ALA A C   
1551 O O   . ALA A 207 ? 1.7670 1.8939 2.9845 -0.0077 -0.1150 -0.3117 207 ALA A O   
1552 C CB  . ALA A 207 ? 1.3569 1.4790 2.6248 0.0173  -0.1627 -0.3254 207 ALA A CB  
1553 N N   . ILE A 208 ? 1.6994 1.8391 2.9481 -0.0042 -0.1150 -0.3303 208 ILE A N   
1554 C CA  . ILE A 208 ? 1.9363 2.0687 3.1579 -0.0123 -0.0995 -0.3196 208 ILE A CA  
1555 C C   . ILE A 208 ? 2.0605 2.1740 3.2610 -0.0075 -0.1091 -0.2989 208 ILE A C   
1556 O O   . ILE A 208 ? 2.1277 2.2329 3.3027 -0.0125 -0.0997 -0.2861 208 ILE A O   
1557 C CB  . ILE A 208 ? 1.7632 1.9077 2.9954 -0.0184 -0.0853 -0.3351 208 ILE A CB  
1558 C CG1 . ILE A 208 ? 1.5354 1.6704 2.7619 -0.0152 -0.0885 -0.3294 208 ILE A CG1 
1559 C CG2 . ILE A 208 ? 1.6370 1.8045 2.9062 -0.0175 -0.0850 -0.3603 208 ILE A CG2 
1560 C CD1 . ILE A 208 ? 1.4958 1.6300 2.7058 -0.0252 -0.0703 -0.3309 208 ILE A CD1 
1561 N N   . THR A 209 ? 1.9092 2.0156 3.1201 0.0016  -0.1285 -0.2963 209 THR A N   
1562 C CA  . THR A 209 ? 1.7995 1.8878 2.9909 0.0047  -0.1392 -0.2769 209 THR A CA  
1563 C C   . THR A 209 ? 2.3268 2.4072 3.4902 0.0015  -0.1348 -0.2594 209 THR A C   
1564 O O   . THR A 209 ? 2.6134 2.6838 3.7553 0.0001  -0.1347 -0.2428 209 THR A O   
1565 C CB  . THR A 209 ? 1.5867 1.6665 2.7928 0.0139  -0.1621 -0.2792 209 THR A CB  
1566 O OG1 . THR A 209 ? 1.2929 1.3663 2.4901 0.0157  -0.1695 -0.2719 209 THR A OG1 
1567 C CG2 . THR A 209 ? 1.6550 1.7477 2.8961 0.0198  -0.1681 -0.3028 209 THR A CG2 
1568 N N   . TRP A 210 ? 2.5347 2.6206 3.6995 0.0003  -0.1312 -0.2645 210 TRP A N   
1569 C CA  . TRP A 210 ? 2.1048 2.1830 3.2451 -0.0011 -0.1286 -0.2510 210 TRP A CA  
1570 C C   . TRP A 210 ? 2.0951 2.1764 3.2176 -0.0085 -0.1098 -0.2494 210 TRP A C   
1571 O O   . TRP A 210 ? 2.1499 2.2271 3.2557 -0.0099 -0.1061 -0.2439 210 TRP A O   
1572 C CB  . TRP A 210 ? 1.8636 1.9428 3.0145 0.0023  -0.1382 -0.2579 210 TRP A CB  
1573 C CG  . TRP A 210 ? 1.7529 1.8184 2.9021 0.0094  -0.1582 -0.2500 210 TRP A CG  
1574 C CD1 . TRP A 210 ? 1.5151 1.5789 2.6813 0.0152  -0.1742 -0.2586 210 TRP A CD1 
1575 C CD2 . TRP A 210 ? 1.9533 2.0036 3.0802 0.0103  -0.1648 -0.2315 210 TRP A CD2 
1576 N NE1 . TRP A 210 ? 1.4791 1.5242 2.6321 0.0196  -0.1910 -0.2463 210 TRP A NE1 
1577 C CE2 . TRP A 210 ? 1.8257 1.8628 2.9544 0.0158  -0.1847 -0.2295 210 TRP A CE2 
1578 C CE3 . TRP A 210 ? 2.3162 2.3631 3.4221 0.0064  -0.1560 -0.2172 210 TRP A CE3 
1579 C CZ2 . TRP A 210 ? 2.1994 2.2189 3.3070 0.0158  -0.1949 -0.2131 210 TRP A CZ2 
1580 C CZ3 . TRP A 210 ? 2.6434 2.6769 3.7325 0.0067  -0.1655 -0.2019 210 TRP A CZ3 
1581 C CH2 . TRP A 210 ? 2.5869 2.6064 3.6755 0.0106  -0.1840 -0.1996 210 TRP A CH2 
1582 N N   . ALA A 211 ? 2.1480 2.2337 3.2717 -0.0131 -0.0993 -0.2540 211 ALA A N   
1583 C CA  . ALA A 211 ? 2.3615 2.4472 3.4679 -0.0209 -0.0827 -0.2548 211 ALA A CA  
1584 C C   . ALA A 211 ? 2.5615 2.6363 3.6380 -0.0202 -0.0806 -0.2384 211 ALA A C   
1585 O O   . ALA A 211 ? 2.3354 2.4045 3.4031 -0.0150 -0.0885 -0.2250 211 ALA A O   
1586 C CB  . ALA A 211 ? 2.1435 2.2306 3.2501 -0.0250 -0.0747 -0.2584 211 ALA A CB  
1587 N N   . ALA A 212 ? 2.5095 2.5812 3.5697 -0.0259 -0.0697 -0.2405 212 ALA A N   
1588 C CA  . ALA A 212 ? 2.4415 2.5026 3.4736 -0.0242 -0.0677 -0.2280 212 ALA A CA  
1589 C C   . ALA A 212 ? 2.4075 2.4665 3.4397 -0.0177 -0.0785 -0.2217 212 ALA A C   
1590 O O   . ALA A 212 ? 2.3170 2.3810 3.3685 -0.0166 -0.0858 -0.2297 212 ALA A O   
1591 C CB  . ALA A 212 ? 2.1152 2.1712 3.1307 -0.0220 -0.0656 -0.2160 212 ALA A CB  
1592 N N   . SER A 213 ? 2.1482 2.2000 3.1586 -0.0131 -0.0798 -0.2078 213 SER A N   
1593 C CA  . SER A 213 ? 1.8287 1.8748 2.8282 -0.0089 -0.0854 -0.2026 213 SER A CA  
1594 C C   . SER A 213 ? 1.6696 1.7153 2.6741 -0.0035 -0.0974 -0.1941 213 SER A C   
1595 O O   . SER A 213 ? 1.7608 1.8018 2.7469 0.0002  -0.0989 -0.1829 213 SER A O   
1596 C CB  . SER A 213 ? 1.8959 1.9336 2.8664 -0.0071 -0.0789 -0.1948 213 SER A CB  
1597 O OG  . SER A 213 ? 1.8229 1.8579 2.7845 -0.0121 -0.0689 -0.1988 213 SER A OG  
1598 N N   . ILE A 214 ? 1.5943 1.6439 2.6220 -0.0033 -0.1062 -0.2002 214 ILE A N   
1599 C CA  . ILE A 214 ? 1.6217 1.6658 2.6514 0.0007  -0.1200 -0.1931 214 ILE A CA  
1600 C C   . ILE A 214 ? 1.7024 1.7453 2.7485 0.0025  -0.1303 -0.2037 214 ILE A C   
1601 O O   . ILE A 214 ? 1.5995 1.6332 2.6385 0.0059  -0.1413 -0.1984 214 ILE A O   
1602 C CB  . ILE A 214 ? 1.7487 1.7942 2.7896 0.0004  -0.1257 -0.1904 214 ILE A CB  
1603 C CG1 . ILE A 214 ? 1.9865 2.0378 3.0231 -0.0028 -0.1142 -0.1878 214 ILE A CG1 
1604 C CG2 . ILE A 214 ? 1.5197 1.5553 2.5495 0.0024  -0.1375 -0.1777 214 ILE A CG2 
1605 C CD1 . ILE A 214 ? 2.1267 2.1791 3.1772 -0.0037 -0.1198 -0.1883 214 ILE A CD1 
1606 N N   . GLY A 215 ? 1.8452 1.8981 2.9130 -0.0002 -0.1262 -0.2192 215 GLY A N   
1607 C CA  . GLY A 215 ? 2.1315 2.1890 3.2221 0.0010  -0.1348 -0.2331 215 GLY A CA  
1608 C C   . GLY A 215 ? 1.8614 1.9156 2.9403 -0.0005 -0.1322 -0.2342 215 GLY A C   
1609 O O   . GLY A 215 ? 2.2629 2.3111 3.3440 0.0032  -0.1446 -0.2347 215 GLY A O   
1610 N N   . ASN A 216 ? 1.4037 1.4592 2.4678 -0.0063 -0.1170 -0.2342 216 ASN A N   
1611 C CA  . ASN A 216 ? 1.3171 1.3669 2.3659 -0.0090 -0.1132 -0.2349 216 ASN A CA  
1612 C C   . ASN A 216 ? 1.3633 1.3996 2.3925 -0.0025 -0.1233 -0.2229 216 ASN A C   
1613 O O   . ASN A 216 ? 1.2492 1.2787 2.2591 0.0010  -0.1229 -0.2095 216 ASN A O   
1614 C CB  . ASN A 216 ? 1.3076 1.3540 2.3343 -0.0149 -0.0976 -0.2323 216 ASN A CB  
1615 C CG  . ASN A 216 ? 1.6086 1.6653 2.6490 -0.0220 -0.0872 -0.2422 216 ASN A CG  
1616 O OD1 . ASN A 216 ? 1.7500 1.8189 2.8189 -0.0221 -0.0908 -0.2522 216 ASN A OD1 
1617 N ND2 . ASN A 216 ? 1.8054 1.8558 2.8245 -0.0275 -0.0750 -0.2399 216 ASN A ND2 
1618 N N   . VAL A 217 ? 1.5777 1.6108 2.6124 -0.0017 -0.1323 -0.2286 217 VAL A N   
1619 C CA  . VAL A 217 ? 1.5319 1.5503 2.5469 0.0036  -0.1423 -0.2192 217 VAL A CA  
1620 C C   . VAL A 217 ? 1.8804 1.8942 2.8870 0.0003  -0.1406 -0.2248 217 VAL A C   
1621 O O   . VAL A 217 ? 2.4630 2.4860 3.4913 -0.0045 -0.1414 -0.2387 217 VAL A O   
1622 C CB  . VAL A 217 ? 1.4131 1.4257 2.4388 0.0094  -0.1610 -0.2177 217 VAL A CB  
1623 C CG1 . VAL A 217 ? 1.2924 1.2877 2.2941 0.0133  -0.1704 -0.2093 217 VAL A CG1 
1624 C CG2 . VAL A 217 ? 1.8017 1.8134 2.8277 0.0118  -0.1639 -0.2092 217 VAL A CG2 
1625 N N   . LEU A 218 ? 1.9746 1.9737 2.9493 0.0034  -0.1397 -0.2140 218 LEU A N   
1626 C CA  . LEU A 218 ? 1.8388 1.8290 2.7960 0.0005  -0.1361 -0.2163 218 LEU A CA  
1627 C C   . LEU A 218 ? 1.9022 1.8771 2.8429 0.0061  -0.1486 -0.2108 218 LEU A C   
1628 O O   . LEU A 218 ? 1.8912 1.8574 2.8147 0.0124  -0.1531 -0.1995 218 LEU A O   
1629 C CB  . LEU A 218 ? 1.6939 1.6790 2.6246 0.0000  -0.1223 -0.2091 218 LEU A CB  
1630 C CG  . LEU A 218 ? 1.6069 1.5766 2.5089 -0.0006 -0.1192 -0.2079 218 LEU A CG  
1631 C CD1 . LEU A 218 ? 1.5569 1.5286 2.4651 -0.0114 -0.1120 -0.2191 218 LEU A CD1 
1632 C CD2 . LEU A 218 ? 1.5236 1.4844 2.3949 0.0054  -0.1122 -0.1972 218 LEU A CD2 
1633 N N   . ILE A 219 ? 1.9084 1.8808 2.8560 0.0025  -0.1543 -0.2201 219 ILE A N   
1634 C CA  . ILE A 219 ? 2.0787 2.0363 3.0144 0.0065  -0.1679 -0.2179 219 ILE A CA  
1635 C C   . ILE A 219 ? 2.3662 2.3137 3.2838 0.0020  -0.1641 -0.2213 219 ILE A C   
1636 O O   . ILE A 219 ? 2.3720 2.3285 3.3045 -0.0070 -0.1583 -0.2324 219 ILE A O   
1637 C CB  . ILE A 219 ? 2.1024 2.0668 3.0706 0.0073  -0.1840 -0.2278 219 ILE A CB  
1638 C CG1 . ILE A 219 ? 1.7695 1.7317 2.7425 0.0138  -0.1939 -0.2209 219 ILE A CG1 
1639 C CG2 . ILE A 219 ? 2.5905 2.5432 3.5544 0.0076  -0.1972 -0.2321 219 ILE A CG2 
1640 C CD1 . ILE A 219 ? 2.0191 1.9998 3.0242 0.0124  -0.1915 -0.2282 219 ILE A CD1 
1641 N N   . ASP A 220 ? 2.8063 2.7343 3.6903 0.0078  -0.1675 -0.2118 220 ASP A N   
1642 C CA  . ASP A 220 ? 3.0039 2.9173 3.8666 0.0050  -0.1675 -0.2141 220 ASP A CA  
1643 C C   . ASP A 220 ? 2.9130 2.8220 3.7886 0.0035  -0.1834 -0.2214 220 ASP A C   
1644 O O   . ASP A 220 ? 2.7737 2.6741 3.6451 0.0104  -0.1962 -0.2165 220 ASP A O   
1645 C CB  . ASP A 220 ? 3.0870 2.9822 3.9079 0.0119  -0.1626 -0.2031 220 ASP A CB  
1646 C CG  . ASP A 220 ? 2.8420 2.7212 3.6404 0.0206  -0.1732 -0.1949 220 ASP A CG  
1647 O OD1 . ASP A 220 ? 3.1142 2.9976 3.9171 0.0250  -0.1769 -0.1886 220 ASP A OD1 
1648 O OD2 . ASP A 220 ? 2.3186 2.1798 3.0930 0.0221  -0.1777 -0.1947 220 ASP A OD2 
1649 N N   . ARG A 221 ? 2.7136 2.6277 3.6034 -0.0061 -0.1827 -0.2331 221 ARG A N   
1650 C CA  . ARG A 221 ? 2.4717 2.3893 3.3847 -0.0091 -0.1972 -0.2436 221 ARG A CA  
1651 C C   . ARG A 221 ? 2.4356 2.3292 3.3225 -0.0027 -0.2115 -0.2376 221 ARG A C   
1652 O O   . ARG A 221 ? 2.6745 2.5684 3.5793 -0.0009 -0.2279 -0.2432 221 ARG A O   
1653 C CB  . ARG A 221 ? 2.2718 2.2008 3.2020 -0.0231 -0.1907 -0.2573 221 ARG A CB  
1654 C CG  . ARG A 221 ? 2.0499 2.0009 3.0021 -0.0306 -0.1752 -0.2636 221 ARG A CG  
1655 C CD  . ARG A 221 ? 1.8124 1.7810 2.7933 -0.0450 -0.1725 -0.2805 221 ARG A CD  
1656 N NE  . ARG A 221 ? 1.7835 1.7555 2.7548 -0.0560 -0.1534 -0.2818 221 ARG A NE  
1657 C CZ  . ARG A 221 ? 1.9005 1.8847 2.8860 -0.0722 -0.1449 -0.2946 221 ARG A CZ  
1658 N NH1 . ARG A 221 ? 1.7541 1.7531 2.7692 -0.0790 -0.1530 -0.3083 221 ARG A NH1 
1659 N NH2 . ARG A 221 ? 2.1979 2.1796 3.1677 -0.0822 -0.1285 -0.2940 221 ARG A NH2 
1660 N N   . ASP A 222 ? 2.3242 2.1971 3.1694 0.0012  -0.2061 -0.2272 222 ASP A N   
1661 C CA  . ASP A 222 ? 2.4415 2.2896 3.2560 0.0075  -0.2177 -0.2210 222 ASP A CA  
1662 C C   . ASP A 222 ? 2.2679 2.1116 3.0845 0.0160  -0.2310 -0.2151 222 ASP A C   
1663 O O   . ASP A 222 ? 2.2762 2.1079 3.0928 0.0180  -0.2482 -0.2173 222 ASP A O   
1664 C CB  . ASP A 222 ? 2.9573 2.7880 3.7289 0.0122  -0.2070 -0.2115 222 ASP A CB  
1665 C CG  . ASP A 222 ? 3.2732 3.0985 4.0327 0.0043  -0.1974 -0.2161 222 ASP A CG  
1666 O OD1 . ASP A 222 ? 2.9222 2.7342 3.6734 -0.0008 -0.2050 -0.2213 222 ASP A OD1 
1667 O OD2 . ASP A 222 ? 3.8473 3.6798 4.6039 0.0027  -0.1832 -0.2145 222 ASP A OD2 
1668 N N   . LYS A 223 ? 2.2093 2.0618 3.0269 0.0201  -0.2232 -0.2077 223 LYS A N   
1669 C CA  . LYS A 223 ? 2.1269 1.9732 2.9414 0.0265  -0.2338 -0.2003 223 LYS A CA  
1670 C C   . LYS A 223 ? 2.2207 2.0746 3.0715 0.0251  -0.2506 -0.2101 223 LYS A C   
1671 O O   . LYS A 223 ? 2.4082 2.2474 3.2518 0.0297  -0.2667 -0.2062 223 LYS A O   
1672 C CB  . LYS A 223 ? 1.9843 1.8368 2.7894 0.0300  -0.2225 -0.1897 223 LYS A CB  
1673 C CG  . LYS A 223 ? 2.0537 1.8946 2.8181 0.0350  -0.2121 -0.1785 223 LYS A CG  
1674 C CD  . LYS A 223 ? 2.4104 2.2267 3.1411 0.0388  -0.2200 -0.1759 223 LYS A CD  
1675 C CE  . LYS A 223 ? 2.1937 1.9917 2.9140 0.0410  -0.2380 -0.1725 223 LYS A CE  
1676 N NZ  . LYS A 223 ? 2.4053 2.1803 3.0873 0.0450  -0.2406 -0.1692 223 LYS A NZ  
1677 N N   . LEU A 224 ? 2.2428 2.1202 3.1317 0.0192  -0.2460 -0.2221 224 LEU A N   
1678 C CA  . LEU A 224 ? 2.3796 2.2698 3.3091 0.0187  -0.2606 -0.2345 224 LEU A CA  
1679 C C   . LEU A 224 ? 2.3469 2.2247 3.2768 0.0186  -0.2783 -0.2413 224 LEU A C   
1680 O O   . LEU A 224 ? 2.0032 1.8741 2.9452 0.0238  -0.2989 -0.2443 224 LEU A O   
1681 C CB  . LEU A 224 ? 2.3703 2.2903 3.3383 0.0118  -0.2488 -0.2470 224 LEU A CB  
1682 C CG  . LEU A 224 ? 2.2079 2.1459 3.2210 0.0137  -0.2612 -0.2599 224 LEU A CG  
1683 C CD1 . LEU A 224 ? 2.4400 2.3667 3.4491 0.0228  -0.2744 -0.2517 224 LEU A CD1 
1684 C CD2 . LEU A 224 ? 1.7845 1.7518 2.8298 0.0068  -0.2454 -0.2711 224 LEU A CD2 
1685 N N   . ARG A 225 ? 2.4927 2.3662 3.4087 0.0127  -0.2715 -0.2438 225 ARG A N   
1686 C CA  . ARG A 225 ? 2.5819 2.4500 3.5070 0.0097  -0.2865 -0.2535 225 ARG A CA  
1687 C C   . ARG A 225 ? 2.7253 2.5635 3.6210 0.0182  -0.3053 -0.2447 225 ARG A C   
1688 O O   . ARG A 225 ? 2.8820 2.7124 3.7855 0.0184  -0.3234 -0.2518 225 ARG A O   
1689 C CB  . ARG A 225 ? 2.5858 2.4512 3.4973 0.0004  -0.2762 -0.2570 225 ARG A CB  
1690 C CG  . ARG A 225 ? 2.4328 2.3222 3.3639 -0.0102 -0.2563 -0.2645 225 ARG A CG  
1691 C CD  . ARG A 225 ? 2.0304 1.9219 2.9661 -0.0227 -0.2547 -0.2749 225 ARG A CD  
1692 N NE  . ARG A 225 ? 2.0004 1.9100 2.9795 -0.0255 -0.2700 -0.2905 225 ARG A NE  
1693 C CZ  . ARG A 225 ? 2.0122 1.9538 3.0353 -0.0347 -0.2641 -0.3063 225 ARG A CZ  
1694 N NH1 . ARG A 225 ? 2.2687 2.2241 3.2936 -0.0443 -0.2428 -0.3080 225 ARG A NH1 
1695 N NH2 . ARG A 225 ? 1.8649 1.8243 2.9292 -0.0343 -0.2798 -0.3210 225 ARG A NH2 
1696 N N   . HIS A 226 ? 2.9155 2.7383 3.7781 0.0246  -0.3007 -0.2296 226 HIS A N   
1697 C CA  . HIS A 226 ? 3.0229 2.8152 3.8493 0.0313  -0.3147 -0.2192 226 HIS A CA  
1698 C C   . HIS A 226 ? 3.2437 3.0324 4.0802 0.0365  -0.3288 -0.2162 226 HIS A C   
1699 O O   . HIS A 226 ? 3.6513 3.4185 4.4778 0.0404  -0.3501 -0.2153 226 HIS A O   
1700 C CB  . HIS A 226 ? 2.9902 2.7681 3.7703 0.0335  -0.2988 -0.2057 226 HIS A CB  
1701 C CG  . HIS A 226 ? 3.0323 2.7797 3.7701 0.0393  -0.3089 -0.1949 226 HIS A CG  
1702 N ND1 . HIS A 226 ? 3.1345 2.8752 3.8440 0.0429  -0.2997 -0.1820 226 HIS A ND1 
1703 C CD2 . HIS A 226 ? 3.0697 2.7921 3.7880 0.0414  -0.3265 -0.1951 226 HIS A CD2 
1704 C CE1 . HIS A 226 ? 3.0960 2.8085 3.7680 0.0464  -0.3100 -0.1747 226 HIS A CE1 
1705 N NE2 . HIS A 226 ? 3.1031 2.8026 3.7788 0.0460  -0.3269 -0.1822 226 HIS A NE2 
1706 N N   . THR A 227 ? 3.1441 2.9515 3.9985 0.0361  -0.3179 -0.2147 227 THR A N   
1707 C CA  . THR A 227 ? 2.9873 2.7903 3.8493 0.0402  -0.3298 -0.2112 227 THR A CA  
1708 C C   . THR A 227 ? 2.6205 2.4531 3.5328 0.0388  -0.3284 -0.2241 227 THR A C   
1709 O O   . THR A 227 ? 3.1529 3.0065 4.0763 0.0351  -0.3084 -0.2245 227 THR A O   
1710 C CB  . THR A 227 ? 3.5096 3.3035 4.3366 0.0409  -0.3166 -0.1945 227 THR A CB  
1711 O OG1 . THR A 227 ? 3.6590 3.4787 4.5022 0.0378  -0.2950 -0.1950 227 THR A OG1 
1712 C CG2 . THR A 227 ? 3.5570 3.3315 4.3372 0.0415  -0.3088 -0.1840 227 THR A CG2 
1713 N N   . GLY A 228 ? 2.0799 1.9129 3.0214 0.0424  -0.3506 -0.2351 228 GLY A N   
1714 C CA  . GLY A 228 ? 2.0764 1.9399 3.0701 0.0417  -0.3509 -0.2520 228 GLY A CA  
1715 C C   . GLY A 228 ? 2.2505 2.1301 3.2579 0.0416  -0.3383 -0.2496 228 GLY A C   
1716 O O   . GLY A 228 ? 2.0993 2.0071 3.1472 0.0398  -0.3326 -0.2637 228 GLY A O   
1717 N N   . ASP A 229 ? 2.6185 2.4814 3.5930 0.0429  -0.3336 -0.2328 229 ASP A N   
1718 C CA  . ASP A 229 ? 2.6025 2.4755 3.5889 0.0435  -0.3277 -0.2301 229 ASP A CA  
1719 C C   . ASP A 229 ? 2.4650 2.3586 3.4500 0.0377  -0.2992 -0.2263 229 ASP A C   
1720 O O   . ASP A 229 ? 2.8775 2.7645 3.8306 0.0350  -0.2850 -0.2158 229 ASP A O   
1721 C CB  . ASP A 229 ? 2.7678 2.6126 3.7240 0.0466  -0.3406 -0.2155 229 ASP A CB  
1722 C CG  . ASP A 229 ? 3.0816 2.9026 3.9861 0.0444  -0.3346 -0.1979 229 ASP A CG  
1723 O OD1 . ASP A 229 ? 3.4905 3.3110 4.3807 0.0428  -0.3262 -0.1979 229 ASP A OD1 
1724 O OD2 . ASP A 229 ? 3.1480 2.9511 4.0262 0.0437  -0.3379 -0.1848 229 ASP A OD2 
1725 N N   . LEU A 230 ? 1.9308 1.8479 2.9495 0.0367  -0.2924 -0.2354 230 LEU A N   
1726 C CA  . LEU A 230 ? 1.7613 1.6975 2.7823 0.0313  -0.2677 -0.2336 230 LEU A CA  
1727 C C   . LEU A 230 ? 1.8780 1.8019 2.8613 0.0307  -0.2567 -0.2147 230 LEU A C   
1728 O O   . LEU A 230 ? 1.9815 1.9114 2.9492 0.0271  -0.2378 -0.2098 230 LEU A O   
1729 C CB  . LEU A 230 ? 1.6196 1.5788 2.6786 0.0309  -0.2641 -0.2450 230 LEU A CB  
1730 C CG  . LEU A 230 ? 1.6986 1.6854 2.7921 0.0255  -0.2535 -0.2631 230 LEU A CG  
1731 C CD1 . LEU A 230 ? 1.5751 1.5647 2.6536 0.0179  -0.2383 -0.2632 230 LEU A CD1 
1732 C CD2 . LEU A 230 ? 1.9774 1.9717 3.1072 0.0301  -0.2736 -0.2801 230 LEU A CD2 
1733 N N   . VAL A 231 ? 1.7912 1.6988 2.7617 0.0338  -0.2687 -0.2052 231 VAL A N   
1734 C CA  . VAL A 231 ? 1.6879 1.5898 2.6298 0.0318  -0.2573 -0.1892 231 VAL A CA  
1735 C C   . VAL A 231 ? 1.8045 1.6846 2.7043 0.0321  -0.2584 -0.1767 231 VAL A C   
1736 O O   . VAL A 231 ? 1.7814 1.6544 2.6532 0.0303  -0.2510 -0.1632 231 VAL A O   
1737 C CB  . VAL A 231 ? 1.6301 1.5275 2.5788 0.0323  -0.2663 -0.1850 231 VAL A CB  
1738 C CG1 . VAL A 231 ? 1.6117 1.5090 2.5355 0.0283  -0.2518 -0.1697 231 VAL A CG1 
1739 C CG2 . VAL A 231 ? 1.6701 1.5878 2.6615 0.0335  -0.2674 -0.1997 231 VAL A CG2 
1740 N N   . GLY A 232 ? 2.0322 1.9022 2.9279 0.0341  -0.2680 -0.1823 232 GLY A N   
1741 C CA  . GLY A 232 ? 2.1512 2.0016 3.0078 0.0348  -0.2678 -0.1730 232 GLY A CA  
1742 C C   . GLY A 232 ? 2.1742 2.0353 3.0215 0.0335  -0.2486 -0.1740 232 GLY A C   
1743 O O   . GLY A 232 ? 2.3886 2.2382 3.2012 0.0346  -0.2419 -0.1651 232 GLY A O   
1744 N N   . SER A 233 ? 1.9471 1.8291 2.8242 0.0312  -0.2402 -0.1855 233 SER A N   
1745 C CA  . SER A 233 ? 2.1118 2.0008 2.9813 0.0289  -0.2246 -0.1882 233 SER A CA  
1746 C C   . SER A 233 ? 1.9697 1.8779 2.8481 0.0262  -0.2056 -0.1876 233 SER A C   
1747 O O   . SER A 233 ? 1.9790 1.8941 2.8564 0.0232  -0.1933 -0.1920 233 SER A O   
1748 C CB  . SER A 233 ? 2.0514 1.9443 2.9418 0.0261  -0.2312 -0.2022 233 SER A CB  
1749 O OG  . SER A 233 ? 1.7833 1.6928 2.7151 0.0244  -0.2382 -0.2142 233 SER A OG  
1750 N N   . ALA A 234 ? 1.6736 1.5881 2.5584 0.0267  -0.2042 -0.1819 234 ALA A N   
1751 C CA  . ALA A 234 ? 1.6398 1.5717 2.5340 0.0242  -0.1882 -0.1813 234 ALA A CA  
1752 C C   . ALA A 234 ? 1.7977 1.7267 2.6602 0.0261  -0.1740 -0.1712 234 ALA A C   
1753 O O   . ALA A 234 ? 1.8309 1.7506 2.6694 0.0289  -0.1753 -0.1605 234 ALA A O   
1754 C CB  . ALA A 234 ? 1.6774 1.6157 2.5888 0.0239  -0.1927 -0.1790 234 ALA A CB  
1755 N N   . GLU A 235 ? 1.7129 1.6493 2.5748 0.0244  -0.1611 -0.1755 235 GLU A N   
1756 C CA  . GLU A 235 ? 1.5581 1.4937 2.3942 0.0276  -0.1482 -0.1684 235 GLU A CA  
1757 C C   . GLU A 235 ? 1.6459 1.5967 2.4913 0.0268  -0.1387 -0.1643 235 GLU A C   
1758 O O   . GLU A 235 ? 2.0445 1.9974 2.8717 0.0304  -0.1310 -0.1564 235 GLU A O   
1759 C CB  . GLU A 235 ? 1.6493 1.5812 2.4765 0.0262  -0.1408 -0.1747 235 GLU A CB  
1760 C CG  . GLU A 235 ? 1.6979 1.6113 2.4990 0.0296  -0.1459 -0.1743 235 GLU A CG  
1761 C CD  . GLU A 235 ? 2.1018 2.0088 2.8889 0.0281  -0.1380 -0.1790 235 GLU A CD  
1762 O OE1 . GLU A 235 ? 1.9622 1.8786 2.7576 0.0248  -0.1283 -0.1813 235 GLU A OE1 
1763 O OE2 . GLU A 235 ? 2.5691 2.4595 3.3356 0.0296  -0.1424 -0.1804 235 GLU A OE2 
1764 N N   . VAL A 236 ? 1.6701 1.6323 2.5446 0.0221  -0.1390 -0.1708 236 VAL A N   
1765 C CA  . VAL A 236 ? 1.7535 1.7285 2.6381 0.0208  -0.1322 -0.1671 236 VAL A CA  
1766 C C   . VAL A 236 ? 1.9960 1.9771 2.9096 0.0178  -0.1411 -0.1718 236 VAL A C   
1767 O O   . VAL A 236 ? 2.1257 2.1140 3.0624 0.0143  -0.1410 -0.1830 236 VAL A O   
1768 C CB  . VAL A 236 ? 1.3965 1.3792 2.2806 0.0190  -0.1186 -0.1704 236 VAL A CB  
1769 C CG1 . VAL A 236 ? 1.3413 1.3354 2.2310 0.0189  -0.1127 -0.1644 236 VAL A CG1 
1770 C CG2 . VAL A 236 ? 1.6794 1.6528 2.5348 0.0232  -0.1124 -0.1679 236 VAL A CG2 
1771 N N   . ILE A 237 ? 1.9331 1.9105 2.8442 0.0189  -0.1491 -0.1636 237 ILE A N   
1772 C CA  . ILE A 237 ? 1.7392 1.7202 2.6743 0.0171  -0.1581 -0.1667 237 ILE A CA  
1773 C C   . ILE A 237 ? 1.6389 1.6247 2.5682 0.0155  -0.1532 -0.1563 237 ILE A C   
1774 O O   . ILE A 237 ? 1.7268 1.7073 2.6331 0.0157  -0.1521 -0.1450 237 ILE A O   
1775 C CB  . ILE A 237 ? 1.8757 1.8427 2.8142 0.0189  -0.1771 -0.1682 237 ILE A CB  
1776 C CG1 . ILE A 237 ? 2.0579 2.0272 3.0225 0.0186  -0.1883 -0.1735 237 ILE A CG1 
1777 C CG2 . ILE A 237 ? 1.8669 1.8177 2.7736 0.0201  -0.1821 -0.1551 237 ILE A CG2 
1778 C CD1 . ILE A 237 ? 2.3763 2.3332 3.3518 0.0218  -0.2089 -0.1801 237 ILE A CD1 
1779 N N   . ARG A 238 ? 1.4691 1.4661 2.4193 0.0131  -0.1497 -0.1608 238 ARG A N   
1780 C CA  . ARG A 238 ? 1.5685 1.5712 2.5152 0.0107  -0.1450 -0.1518 238 ARG A CA  
1781 C C   . ARG A 238 ? 1.7848 1.7824 2.7467 0.0090  -0.1584 -0.1519 238 ARG A C   
1782 O O   . ARG A 238 ? 1.6811 1.6806 2.6408 0.0058  -0.1576 -0.1444 238 ARG A O   
1783 C CB  . ARG A 238 ? 1.4748 1.4909 2.4253 0.0097  -0.1299 -0.1545 238 ARG A CB  
1784 C CG  . ARG A 238 ? 1.5812 1.5956 2.5163 0.0123  -0.1218 -0.1569 238 ARG A CG  
1785 C CD  . ARG A 238 ? 1.9084 1.9282 2.8246 0.0143  -0.1099 -0.1500 238 ARG A CD  
1786 N NE  . ARG A 238 ? 2.2934 2.3227 3.2190 0.0122  -0.1017 -0.1527 238 ARG A NE  
1787 C CZ  . ARG A 238 ? 2.4833 2.5136 3.4174 0.0099  -0.0965 -0.1622 238 ARG A CZ  
1788 N NH1 . ARG A 238 ? 2.0419 2.0666 2.9800 0.0083  -0.0979 -0.1713 238 ARG A NH1 
1789 N NH2 . ARG A 238 ? 2.9333 2.9699 3.8710 0.0080  -0.0896 -0.1626 238 ARG A NH2 
1790 N N   . LEU A 239 ? 1.9245 1.9143 2.9004 0.0114  -0.1720 -0.1607 239 LEU A N   
1791 C CA  . LEU A 239 ? 1.6612 1.6412 2.6490 0.0117  -0.1889 -0.1619 239 LEU A CA  
1792 C C   . LEU A 239 ? 1.8205 1.7793 2.7858 0.0117  -0.2030 -0.1523 239 LEU A C   
1793 O O   . LEU A 239 ? 1.8479 1.7997 2.7997 0.0138  -0.2047 -0.1518 239 LEU A O   
1794 C CB  . LEU A 239 ? 1.4859 1.4716 2.5051 0.0153  -0.1962 -0.1794 239 LEU A CB  
1795 C CG  . LEU A 239 ? 1.5175 1.5194 2.5603 0.0140  -0.1875 -0.1886 239 LEU A CG  
1796 C CD1 . LEU A 239 ? 1.8646 1.8752 2.9397 0.0172  -0.1937 -0.2076 239 LEU A CD1 
1797 C CD2 . LEU A 239 ? 1.5191 1.5136 2.5589 0.0124  -0.1944 -0.1801 239 LEU A CD2 
1798 N N   . PRO A 240 ? 1.9072 1.8530 2.8652 0.0086  -0.2141 -0.1441 240 PRO A N   
1799 C CA  . PRO A 240 ? 1.7955 1.7157 2.7343 0.0082  -0.2325 -0.1377 240 PRO A CA  
1800 C C   . PRO A 240 ? 1.6416 1.5562 2.5996 0.0155  -0.2473 -0.1518 240 PRO A C   
1801 O O   . PRO A 240 ? 1.4184 1.3437 2.4081 0.0196  -0.2508 -0.1657 240 PRO A O   
1802 C CB  . PRO A 240 ? 1.7087 1.6168 2.6455 0.0036  -0.2434 -0.1312 240 PRO A CB  
1803 C CG  . PRO A 240 ? 1.9077 1.8369 2.8508 -0.0005 -0.2249 -0.1279 240 PRO A CG  
1804 C CD  . PRO A 240 ? 1.9621 1.9143 2.9267 0.0044  -0.2102 -0.1401 240 PRO A CD  
1805 N N   . ALA A 241 ? 1.6536 1.5530 2.5923 0.0169  -0.2550 -0.1489 241 ALA A N   
1806 C CA  . ALA A 241 ? 1.6891 1.5864 2.6451 0.0235  -0.2665 -0.1623 241 ALA A CA  
1807 C C   . ALA A 241 ? 1.7245 1.6175 2.7096 0.0287  -0.2862 -0.1744 241 ALA A C   
1808 O O   . ALA A 241 ? 1.5879 1.4964 2.6058 0.0338  -0.2879 -0.1912 241 ALA A O   
1809 C CB  . ALA A 241 ? 1.8479 1.7222 2.7736 0.0237  -0.2767 -0.1549 241 ALA A CB  
1810 N N   . GLU A 242 ? 1.9401 1.8106 2.9109 0.0271  -0.3018 -0.1660 242 GLU A N   
1811 C CA  . GLU A 242 ? 1.9474 1.8063 2.9390 0.0330  -0.3248 -0.1758 242 GLU A CA  
1812 C C   . GLU A 242 ? 1.9202 1.8058 2.9500 0.0360  -0.3157 -0.1896 242 GLU A C   
1813 O O   . GLU A 242 ? 2.0772 1.9708 3.1405 0.0440  -0.3268 -0.2075 242 GLU A O   
1814 C CB  . GLU A 242 ? 2.2540 2.0843 3.2151 0.0270  -0.3366 -0.1601 242 GLU A CB  
1815 C CG  . GLU A 242 ? 2.5311 2.3583 3.5098 0.0286  -0.3467 -0.1646 242 GLU A CG  
1816 C CD  . GLU A 242 ? 2.9243 2.7362 3.9248 0.0394  -0.3751 -0.1793 242 GLU A CD  
1817 O OE1 . GLU A 242 ? 2.9289 2.7078 3.9052 0.0399  -0.3971 -0.1733 242 GLU A OE1 
1818 O OE2 . GLU A 242 ? 3.4066 3.2381 4.4461 0.0471  -0.3760 -0.1967 242 GLU A OE2 
1819 N N   . GLU A 243 ? 1.9010 1.8002 2.9247 0.0294  -0.2955 -0.1815 243 GLU A N   
1820 C CA  . GLU A 243 ? 1.6666 1.5886 2.7206 0.0306  -0.2853 -0.1926 243 GLU A CA  
1821 C C   . GLU A 243 ? 1.7740 1.7215 2.8566 0.0341  -0.2744 -0.2096 243 GLU A C   
1822 O O   . GLU A 243 ? 2.0028 1.9641 3.1190 0.0390  -0.2777 -0.2267 243 GLU A O   
1823 C CB  . GLU A 243 ? 1.5128 1.4420 2.5541 0.0229  -0.2684 -0.1807 243 GLU A CB  
1824 C CG  . GLU A 243 ? 1.4063 1.3537 2.4765 0.0245  -0.2614 -0.1923 243 GLU A CG  
1825 C CD  . GLU A 243 ? 1.8840 1.8385 2.9406 0.0168  -0.2449 -0.1802 243 GLU A CD  
1826 O OE1 . GLU A 243 ? 2.2101 2.1563 3.2374 0.0106  -0.2406 -0.1637 243 GLU A OE1 
1827 O OE2 . GLU A 243 ? 2.2375 2.2066 3.3117 0.0165  -0.2358 -0.1873 243 GLU A OE2 
1828 N N   . PHE A 244 ? 1.6670 1.6197 2.7348 0.0312  -0.2618 -0.2052 244 PHE A N   
1829 C CA  . PHE A 244 ? 1.7592 1.7328 2.8475 0.0318  -0.2507 -0.2192 244 PHE A CA  
1830 C C   . PHE A 244 ? 1.8231 1.7978 2.9405 0.0390  -0.2694 -0.2367 244 PHE A C   
1831 O O   . PHE A 244 ? 1.8207 1.8177 2.9715 0.0404  -0.2643 -0.2546 244 PHE A O   
1832 C CB  . PHE A 244 ? 1.7598 1.7328 2.8229 0.0281  -0.2379 -0.2108 244 PHE A CB  
1833 C CG  . PHE A 244 ? 1.7046 1.6917 2.7850 0.0282  -0.2327 -0.2249 244 PHE A CG  
1834 C CD1 . PHE A 244 ? 1.5024 1.5129 2.6106 0.0257  -0.2204 -0.2396 244 PHE A CD1 
1835 C CD2 . PHE A 244 ? 1.7204 1.6964 2.7890 0.0299  -0.2412 -0.2243 244 PHE A CD2 
1836 C CE1 . PHE A 244 ? 1.5857 1.6091 2.7096 0.0236  -0.2158 -0.2529 244 PHE A CE1 
1837 C CE2 . PHE A 244 ? 1.5651 1.5537 2.6506 0.0288  -0.2379 -0.2377 244 PHE A CE2 
1838 C CZ  . PHE A 244 ? 1.5866 1.5994 2.6997 0.0250  -0.2247 -0.2518 244 PHE A CZ  
1839 N N   . ARG A 245 ? 1.9076 1.8580 3.0109 0.0431  -0.2908 -0.2315 245 ARG A N   
1840 C CA  . ARG A 245 ? 1.9136 1.8607 3.0413 0.0513  -0.3129 -0.2470 245 ARG A CA  
1841 C C   . ARG A 245 ? 1.8846 1.8423 3.0484 0.0577  -0.3225 -0.2630 245 ARG A C   
1842 O O   . ARG A 245 ? 1.8407 1.8186 3.0421 0.0627  -0.3261 -0.2838 245 ARG A O   
1843 C CB  . ARG A 245 ? 1.9565 1.8699 3.0568 0.0544  -0.3362 -0.2368 245 ARG A CB  
1844 C CG  . ARG A 245 ? 1.8906 1.7946 2.9616 0.0505  -0.3309 -0.2269 245 ARG A CG  
1845 C CD  . ARG A 245 ? 1.9214 1.7906 2.9669 0.0538  -0.3562 -0.2195 245 ARG A CD  
1846 N NE  . ARG A 245 ? 1.9563 1.8169 2.9783 0.0518  -0.3539 -0.2140 245 ARG A NE  
1847 C CZ  . ARG A 245 ? 2.2733 2.1242 3.2561 0.0454  -0.3403 -0.1971 245 ARG A CZ  
1848 N NH1 . ARG A 245 ? 2.5410 2.3896 3.5031 0.0396  -0.3282 -0.1832 245 ARG A NH1 
1849 N NH2 . ARG A 245 ? 2.3529 2.1966 3.3177 0.0449  -0.3393 -0.1949 245 ARG A NH2 
1850 N N   . ARG A 246 ? 1.9003 1.8445 3.0518 0.0570  -0.3261 -0.2534 246 ARG A N   
1851 C CA  . ARG A 246 ? 1.8493 1.7983 3.0290 0.0634  -0.3362 -0.2664 246 ARG A CA  
1852 C C   . ARG A 246 ? 1.7734 1.7589 2.9871 0.0620  -0.3153 -0.2832 246 ARG A C   
1853 O O   . ARG A 246 ? 1.9024 1.9039 3.1540 0.0695  -0.3231 -0.3046 246 ARG A O   
1854 C CB  . ARG A 246 ? 2.1541 2.0780 3.3088 0.0612  -0.3445 -0.2510 246 ARG A CB  
1855 C CG  . ARG A 246 ? 2.2049 2.1432 3.3752 0.0600  -0.3335 -0.2555 246 ARG A CG  
1856 C CD  . ARG A 246 ? 2.0481 1.9607 3.2022 0.0598  -0.3483 -0.2456 246 ARG A CD  
1857 N NE  . ARG A 246 ? 2.0189 1.9170 3.1322 0.0483  -0.3383 -0.2213 246 ARG A NE  
1858 C CZ  . ARG A 246 ? 2.2480 2.1147 3.3272 0.0446  -0.3531 -0.2054 246 ARG A CZ  
1859 N NH1 . ARG A 246 ? 2.1279 1.9695 3.2059 0.0520  -0.3808 -0.2101 246 ARG A NH1 
1860 N NH2 . ARG A 246 ? 2.5918 2.4520 3.6375 0.0333  -0.3403 -0.1853 246 ARG A NH2 
1861 N N   . GLU A 247 ? 1.7023 1.6998 2.9004 0.0524  -0.2893 -0.2736 247 GLU A N   
1862 C CA  . GLU A 247 ? 1.6742 1.7018 2.8950 0.0482  -0.2671 -0.2862 247 GLU A CA  
1863 C C   . GLU A 247 ? 1.5713 1.6207 2.8225 0.0498  -0.2659 -0.3063 247 GLU A C   
1864 O O   . GLU A 247 ? 1.3788 1.4520 2.6647 0.0513  -0.2610 -0.3263 247 GLU A O   
1865 C CB  . GLU A 247 ? 1.7587 1.7910 2.9548 0.0382  -0.2423 -0.2720 247 GLU A CB  
1866 C CG  . GLU A 247 ? 1.8904 1.9486 3.1078 0.0338  -0.2223 -0.2856 247 GLU A CG  
1867 C CD  . GLU A 247 ? 1.8135 1.8781 3.0503 0.0366  -0.2235 -0.2946 247 GLU A CD  
1868 O OE1 . GLU A 247 ? 1.8499 1.8975 3.0849 0.0428  -0.2416 -0.2905 247 GLU A OE1 
1869 O OE2 . GLU A 247 ? 1.7123 1.7974 2.9636 0.0319  -0.2060 -0.3059 247 GLU A OE2 
1870 N N   . LEU A 248 ? 1.5684 1.6094 2.8055 0.0488  -0.2703 -0.3009 248 LEU A N   
1871 C CA  . LEU A 248 ? 1.3243 1.3834 2.5864 0.0489  -0.2704 -0.3178 248 LEU A CA  
1872 C C   . LEU A 248 ? 1.7037 1.7721 3.0067 0.0596  -0.2913 -0.3394 248 LEU A C   
1873 O O   . LEU A 248 ? 2.1045 2.2024 3.4446 0.0590  -0.2847 -0.3611 248 LEU A O   
1874 C CB  . LEU A 248 ? 1.1646 1.2064 2.3997 0.0473  -0.2759 -0.3060 248 LEU A CB  
1875 C CG  . LEU A 248 ? 1.1676 1.2278 2.4135 0.0410  -0.2643 -0.3161 248 LEU A CG  
1876 C CD1 . LEU A 248 ? 0.9830 1.0662 2.2339 0.0306  -0.2363 -0.3208 248 LEU A CD1 
1877 C CD2 . LEU A 248 ? 1.4307 1.4680 2.6388 0.0391  -0.2673 -0.2993 248 LEU A CD2 
1878 N N   . ALA A 249 ? 2.0962 2.1383 3.3907 0.0689  -0.3167 -0.3335 249 ALA A N   
1879 C CA  . ALA A 249 ? 2.1004 2.1439 3.4290 0.0817  -0.3420 -0.3525 249 ALA A CA  
1880 C C   . ALA A 249 ? 1.9372 2.0070 3.3014 0.0844  -0.3335 -0.3711 249 ALA A C   
1881 O O   . ALA A 249 ? 1.7029 1.7985 3.1107 0.0907  -0.3387 -0.3963 249 ALA A O   
1882 C CB  . ALA A 249 ? 2.1421 2.1460 3.4457 0.0894  -0.3699 -0.3394 249 ALA A CB  
1883 N N   . GLU A 250 ? 1.8951 1.9593 3.2403 0.0794  -0.3200 -0.3590 250 GLU A N   
1884 C CA  . GLU A 250 ? 1.7665 1.8420 3.1365 0.0848  -0.3204 -0.3727 250 GLU A CA  
1885 C C   . GLU A 250 ? 1.7502 1.8603 3.1385 0.0758  -0.2906 -0.3844 250 GLU A C   
1886 O O   . GLU A 250 ? 1.9512 2.0847 3.3762 0.0807  -0.2895 -0.4071 250 GLU A O   
1887 C CB  . GLU A 250 ? 1.7422 1.7869 3.0828 0.0862  -0.3299 -0.3546 250 GLU A CB  
1888 C CG  . GLU A 250 ? 1.8610 1.8712 3.1901 0.0963  -0.3637 -0.3493 250 GLU A CG  
1889 C CD  . GLU A 250 ? 2.1422 2.1176 3.4296 0.0921  -0.3699 -0.3249 250 GLU A CD  
1890 O OE1 . GLU A 250 ? 1.9036 1.8818 3.1876 0.0884  -0.3588 -0.3213 250 GLU A OE1 
1891 O OE2 . GLU A 250 ? 2.4573 2.4023 3.7140 0.0913  -0.3855 -0.3092 250 GLU A OE2 
1892 N N   . GLN A 251 ? 1.8323 1.9438 3.1933 0.0628  -0.2673 -0.3694 251 GLN A N   
1893 C CA  . GLN A 251 ? 1.9968 2.1346 3.3661 0.0522  -0.2391 -0.3774 251 GLN A CA  
1894 C C   . GLN A 251 ? 1.9527 2.1054 3.3229 0.0431  -0.2258 -0.3811 251 GLN A C   
1895 O O   . GLN A 251 ? 1.8204 2.0011 3.2135 0.0361  -0.2092 -0.3984 251 GLN A O   
1896 C CB  . GLN A 251 ? 2.1272 2.2530 3.4619 0.0439  -0.2222 -0.3576 251 GLN A CB  
1897 C CG  . GLN A 251 ? 2.2875 2.4067 3.6254 0.0488  -0.2270 -0.3579 251 GLN A CG  
1898 C CD  . GLN A 251 ? 2.2483 2.3939 3.6224 0.0506  -0.2194 -0.3828 251 GLN A CD  
1899 O OE1 . GLN A 251 ? 1.9060 2.0784 3.3064 0.0475  -0.2095 -0.4018 251 GLN A OE1 
1900 N NE2 . GLN A 251 ? 2.4402 2.5782 3.8151 0.0551  -0.2239 -0.3830 251 GLN A NE2 
1901 N N   . GLY A 252 ? 1.8046 1.9367 3.1470 0.0424  -0.2332 -0.3643 252 GLY A N   
1902 C CA  . GLY A 252 ? 1.5318 1.6712 2.8687 0.0343  -0.2238 -0.3647 252 GLY A CA  
1903 C C   . GLY A 252 ? 1.4949 1.6348 2.8024 0.0210  -0.1975 -0.3528 252 GLY A C   
1904 O O   . GLY A 252 ? 1.5302 1.6642 2.8192 0.0177  -0.1859 -0.3423 252 GLY A O   
1905 N N   . ALA A 253 ? 1.4171 1.5628 2.7203 0.0133  -0.1899 -0.3550 253 ALA A N   
1906 C CA  . ALA A 253 ? 1.5266 1.6679 2.7990 0.0015  -0.1691 -0.3439 253 ALA A CA  
1907 C C   . ALA A 253 ? 1.5068 1.6711 2.7983 -0.0096 -0.1559 -0.3615 253 ALA A C   
1908 O O   . ALA A 253 ? 1.7871 1.9736 3.1169 -0.0086 -0.1613 -0.3821 253 ALA A O   
1909 C CB  . ALA A 253 ? 1.5570 1.6722 2.7924 0.0037  -0.1760 -0.3234 253 ALA A CB  
1910 N N   . ILE A 254 ? 1.2600 1.4179 2.5224 -0.0212 -0.1384 -0.3529 254 ILE A N   
1911 C CA  . ILE A 254 ? 1.0272 1.1997 2.2946 -0.0356 -0.1234 -0.3648 254 ILE A CA  
1912 C C   . ILE A 254 ? 1.0211 1.1704 2.2477 -0.0402 -0.1204 -0.3481 254 ILE A C   
1913 O O   . ILE A 254 ? 1.2545 1.3822 2.4462 -0.0368 -0.1183 -0.3290 254 ILE A O   
1914 C CB  . ILE A 254 ? 1.0234 1.2108 2.2948 -0.0474 -0.1016 -0.3741 254 ILE A CB  
1915 C CG1 . ILE A 254 ? 1.0405 1.2101 2.2687 -0.0590 -0.0840 -0.3603 254 ILE A CG1 
1916 C CG2 . ILE A 254 ? 1.1209 1.3158 2.4103 -0.0391 -0.1038 -0.3784 254 ILE A CG2 
1917 C CD1 . ILE A 254 ? 1.0226 1.2029 2.2503 -0.0720 -0.0633 -0.3694 254 ILE A CD1 
1918 N N   . VAL A 255 ? 0.9715 1.1269 2.2019 -0.0498 -0.1177 -0.3567 255 VAL A N   
1919 C CA  . VAL A 255 ? 1.0422 1.1743 2.2360 -0.0525 -0.1187 -0.3427 255 VAL A CA  
1920 C C   . VAL A 255 ? 1.1571 1.2844 2.3258 -0.0693 -0.0993 -0.3425 255 VAL A C   
1921 O O   . VAL A 255 ? 1.1715 1.3174 2.3584 -0.0830 -0.0888 -0.3585 255 VAL A O   
1922 C CB  . VAL A 255 ? 0.8358 0.9620 2.0367 -0.0451 -0.1386 -0.3431 255 VAL A CB  
1923 C CG1 . VAL A 255 ? 0.6666 0.7666 1.8258 -0.0472 -0.1389 -0.3282 255 VAL A CG1 
1924 C CG2 . VAL A 255 ? 0.7146 0.8353 1.9268 -0.0283 -0.1581 -0.3382 255 VAL A CG2 
1925 N N   . GLU A 256 ? 1.2748 1.3769 2.4011 -0.0678 -0.0944 -0.3243 256 GLU A N   
1926 C CA  . GLU A 256 ? 1.3122 1.4011 2.4058 -0.0809 -0.0787 -0.3204 256 GLU A CA  
1927 C C   . GLU A 256 ? 1.3519 1.4122 2.4052 -0.0769 -0.0841 -0.3047 256 GLU A C   
1928 O O   . GLU A 256 ? 1.2955 1.3422 2.3340 -0.0629 -0.0942 -0.2910 256 GLU A O   
1929 C CB  . GLU A 256 ? 1.3802 1.4644 2.4576 -0.0829 -0.0656 -0.3146 256 GLU A CB  
1930 C CG  . GLU A 256 ? 1.9490 2.0586 3.0584 -0.0904 -0.0557 -0.3309 256 GLU A CG  
1931 C CD  . GLU A 256 ? 2.3767 2.4786 3.4646 -0.0968 -0.0409 -0.3268 256 GLU A CD  
1932 O OE1 . GLU A 256 ? 2.3406 2.4299 3.4118 -0.0864 -0.0436 -0.3129 256 GLU A OE1 
1933 O OE2 . GLU A 256 ? 3.0051 3.1137 4.0926 -0.1132 -0.0264 -0.3379 256 GLU A OE2 
1934 N N   . GLU A 257 ? 1.3786 1.4279 2.4095 -0.0906 -0.0756 -0.3067 257 GLU A N   
1935 C CA  . GLU A 257 ? 1.5601 1.5805 2.5499 -0.0884 -0.0793 -0.2940 257 GLU A CA  
1936 C C   . GLU A 257 ? 1.6045 1.6054 2.5593 -0.0818 -0.0738 -0.2793 257 GLU A C   
1937 O O   . GLU A 257 ? 1.5563 1.5581 2.5052 -0.0888 -0.0618 -0.2807 257 GLU A O   
1938 C CB  . GLU A 257 ? 1.7303 1.7430 2.7063 -0.1063 -0.0730 -0.3015 257 GLU A CB  
1939 C CG  . GLU A 257 ? 1.7384 1.7549 2.7092 -0.1240 -0.0555 -0.3092 257 GLU A CG  
1940 C CD  . GLU A 257 ? 1.7966 1.7932 2.7364 -0.1418 -0.0495 -0.3110 257 GLU A CD  
1941 O OE1 . GLU A 257 ? 1.6570 1.6310 2.5710 -0.1380 -0.0587 -0.3032 257 GLU A OE1 
1942 O OE2 . GLU A 257 ? 1.7582 1.7607 2.6979 -0.1603 -0.0354 -0.3204 257 GLU A OE2 
1943 N N   . PHE A 258 ? 1.6088 1.5916 2.5394 -0.0686 -0.0828 -0.2659 258 PHE A N   
1944 C CA  . PHE A 258 ? 1.6044 1.5704 2.5034 -0.0600 -0.0796 -0.2524 258 PHE A CA  
1945 C C   . PHE A 258 ? 1.5085 1.4487 2.3673 -0.0672 -0.0743 -0.2496 258 PHE A C   
1946 O O   . PHE A 258 ? 1.6309 1.5522 2.4649 -0.0621 -0.0811 -0.2439 258 PHE A O   
1947 C CB  . PHE A 258 ? 1.5416 1.5037 2.4359 -0.0431 -0.0908 -0.2411 258 PHE A CB  
1948 C CG  . PHE A 258 ? 1.3933 1.3430 2.2591 -0.0336 -0.0873 -0.2286 258 PHE A CG  
1949 C CD1 . PHE A 258 ? 1.4897 1.4502 2.3650 -0.0309 -0.0818 -0.2256 258 PHE A CD1 
1950 C CD2 . PHE A 258 ? 1.4914 1.4194 2.3220 -0.0274 -0.0900 -0.2210 258 PHE A CD2 
1951 C CE1 . PHE A 258 ? 2.0953 2.0470 2.9472 -0.0223 -0.0791 -0.2153 258 PHE A CE1 
1952 C CE2 . PHE A 258 ? 2.1633 2.0831 2.9710 -0.0179 -0.0871 -0.2116 258 PHE A CE2 
1953 C CZ  . PHE A 258 ? 2.3556 2.2882 3.1750 -0.0155 -0.0817 -0.2088 258 PHE A CZ  
1954 N N   . LEU A 259 ? 1.2978 1.2352 2.1482 -0.0787 -0.0627 -0.2535 259 LEU A N   
1955 C CA  . LEU A 259 ? 1.3408 1.2498 2.1494 -0.0859 -0.0580 -0.2503 259 LEU A CA  
1956 C C   . LEU A 259 ? 1.4549 1.3446 2.2329 -0.0688 -0.0640 -0.2369 259 LEU A C   
1957 O O   . LEU A 259 ? 1.6405 1.5396 2.4258 -0.0574 -0.0637 -0.2307 259 LEU A O   
1958 C CB  . LEU A 259 ? 1.3071 1.2187 2.1152 -0.0985 -0.0455 -0.2555 259 LEU A CB  
1959 C CG  . LEU A 259 ? 1.4666 1.4085 2.3163 -0.1098 -0.0383 -0.2691 259 LEU A CG  
1960 C CD1 . LEU A 259 ? 1.5892 1.5334 2.4365 -0.1186 -0.0262 -0.2725 259 LEU A CD1 
1961 C CD2 . LEU A 259 ? 1.7023 1.6498 2.5622 -0.1264 -0.0364 -0.2812 259 LEU A CD2 
1962 N N   . GLU A 260 ? 1.4701 1.3338 2.2146 -0.0671 -0.0695 -0.2333 260 GLU A N   
1963 C CA  . GLU A 260 ? 1.4527 1.3030 2.1742 -0.0486 -0.0768 -0.2228 260 GLU A CA  
1964 C C   . GLU A 260 ? 1.6300 1.4625 2.3218 -0.0439 -0.0737 -0.2176 260 GLU A C   
1965 O O   . GLU A 260 ? 1.7207 1.5610 2.4146 -0.0298 -0.0744 -0.2110 260 GLU A O   
1966 C CB  . GLU A 260 ? 1.5398 1.3695 2.2386 -0.0475 -0.0853 -0.2223 260 GLU A CB  
1967 C CG  . GLU A 260 ? 1.7016 1.5475 2.4277 -0.0465 -0.0921 -0.2253 260 GLU A CG  
1968 C CD  . GLU A 260 ? 1.7740 1.6343 2.5141 -0.0295 -0.0976 -0.2181 260 GLU A CD  
1969 O OE1 . GLU A 260 ? 1.5783 1.4369 2.3056 -0.0171 -0.0961 -0.2102 260 GLU A OE1 
1970 O OE2 . GLU A 260 ? 1.9436 1.8171 2.7081 -0.0295 -0.1039 -0.2209 260 GLU A OE2 
1971 N N   . GLU A 261 ? 1.7097 1.5170 2.3726 -0.0563 -0.0711 -0.2209 261 GLU A N   
1972 C CA  . GLU A 261 ? 1.8244 1.6061 2.4511 -0.0509 -0.0720 -0.2163 261 GLU A CA  
1973 C C   . GLU A 261 ? 1.6405 1.4275 2.2735 -0.0614 -0.0628 -0.2191 261 GLU A C   
1974 O O   . GLU A 261 ? 1.7248 1.5017 2.3496 -0.0810 -0.0567 -0.2256 261 GLU A O   
1975 C CB  . GLU A 261 ? 2.3278 2.0712 2.9112 -0.0556 -0.0781 -0.2168 261 GLU A CB  
1976 C CG  . GLU A 261 ? 2.6071 2.3416 3.1777 -0.0398 -0.0884 -0.2127 261 GLU A CG  
1977 C CD  . GLU A 261 ? 2.5993 2.3367 3.1632 -0.0160 -0.0930 -0.2057 261 GLU A CD  
1978 O OE1 . GLU A 261 ? 2.3304 2.0474 2.8664 -0.0091 -0.0955 -0.2038 261 GLU A OE1 
1979 O OE2 . GLU A 261 ? 2.4257 2.1854 3.0115 -0.0046 -0.0946 -0.2027 261 GLU A OE2 
1980 N N   . ILE A 262 ? 1.4203 1.2243 2.0687 -0.0492 -0.0616 -0.2146 262 ILE A N   
1981 C CA  . ILE A 262 ? 1.5150 1.3257 2.1714 -0.0568 -0.0538 -0.2166 262 ILE A CA  
1982 C C   . ILE A 262 ? 1.5905 1.3778 2.2141 -0.0475 -0.0578 -0.2112 262 ILE A C   
1983 O O   . ILE A 262 ? 1.7538 1.5442 2.3749 -0.0289 -0.0642 -0.2051 262 ILE A O   
1984 C CB  . ILE A 262 ? 1.3360 1.1836 2.0371 -0.0529 -0.0498 -0.2169 262 ILE A CB  
1985 C CG1 . ILE A 262 ? 1.1678 1.0369 1.9013 -0.0594 -0.0491 -0.2230 262 ILE A CG1 
1986 C CG2 . ILE A 262 ? 1.3433 1.1960 2.0510 -0.0615 -0.0418 -0.2199 262 ILE A CG2 
1987 C CD1 . ILE A 262 ? 1.0513 0.9527 1.8266 -0.0547 -0.0479 -0.2238 262 ILE A CD1 
1988 N N   . THR A 263 ? 1.6162 1.3800 2.2142 -0.0608 -0.0543 -0.2142 263 THR A N   
1989 C CA  . THR A 263 ? 1.7323 1.4679 2.2948 -0.0532 -0.0603 -0.2102 263 THR A CA  
1990 C C   . THR A 263 ? 1.8118 1.5602 2.3880 -0.0526 -0.0558 -0.2094 263 THR A C   
1991 O O   . THR A 263 ? 2.1016 1.8513 2.6751 -0.0361 -0.0618 -0.2044 263 THR A O   
1992 C CB  . THR A 263 ? 1.7105 1.4031 2.2268 -0.0678 -0.0626 -0.2130 263 THR A CB  
1993 O OG1 . THR A 263 ? 1.6985 1.3955 2.2225 -0.0911 -0.0508 -0.2194 263 THR A OG1 
1994 C CG2 . THR A 263 ? 1.6916 1.3697 2.1932 -0.0701 -0.0676 -0.2140 263 THR A CG2 
1995 N N   . ASP A 264 ? 1.7753 1.5342 2.3669 -0.0705 -0.0451 -0.2151 264 ASP A N   
1996 C CA  . ASP A 264 ? 1.9072 1.6805 2.5155 -0.0719 -0.0397 -0.2156 264 ASP A CA  
1997 C C   . ASP A 264 ? 1.5604 1.3700 2.2138 -0.0798 -0.0302 -0.2212 264 ASP A C   
1998 O O   . ASP A 264 ? 1.7153 1.5354 2.3836 -0.0893 -0.0261 -0.2270 264 ASP A O   
1999 C CB  . ASP A 264 ? 2.2967 2.0370 2.8676 -0.0846 -0.0381 -0.2175 264 ASP A CB  
2000 C CG  . ASP A 264 ? 2.6556 2.3616 3.1858 -0.0721 -0.0506 -0.2118 264 ASP A CG  
2001 O OD1 . ASP A 264 ? 2.6194 2.3358 3.1590 -0.0543 -0.0569 -0.2068 264 ASP A OD1 
2002 O OD2 . ASP A 264 ? 2.9964 2.6656 3.4860 -0.0802 -0.0547 -0.2128 264 ASP A OD2 
2003 N N   . SER A 265 ? 1.2443 1.0724 1.9193 -0.0751 -0.0279 -0.2200 265 SER A N   
2004 C CA  . SER A 265 ? 1.3118 1.1715 2.0276 -0.0808 -0.0204 -0.2258 265 SER A CA  
2005 C C   . SER A 265 ? 1.2930 1.1505 2.0069 -0.0900 -0.0134 -0.2295 265 SER A C   
2006 O O   . SER A 265 ? 1.4070 1.2806 2.1405 -0.0810 -0.0151 -0.2261 265 SER A O   
2007 C CB  . SER A 265 ? 1.3881 1.2762 2.1377 -0.0643 -0.0260 -0.2203 265 SER A CB  
2008 O OG  . SER A 265 ? 1.3662 1.2818 2.1539 -0.0682 -0.0212 -0.2259 265 SER A OG  
2009 N N   . PRO A 266 ? 1.2847 1.1232 1.9757 -0.1093 -0.0051 -0.2368 266 PRO A N   
2010 C CA  . PRO A 266 ? 1.2851 1.1196 1.9711 -0.1199 0.0025  -0.2413 266 PRO A CA  
2011 C C   . PRO A 266 ? 1.2662 1.1345 1.9948 -0.1242 0.0111  -0.2499 266 PRO A C   
2012 O O   . PRO A 266 ? 1.1853 1.0793 1.9472 -0.1241 0.0130  -0.2554 266 PRO A O   
2013 C CB  . PRO A 266 ? 1.3100 1.1114 1.9540 -0.1405 0.0088  -0.2463 266 PRO A CB  
2014 C CG  . PRO A 266 ? 1.2941 1.0940 1.9362 -0.1451 0.0081  -0.2484 266 PRO A CG  
2015 C CD  . PRO A 266 ? 1.2264 1.0453 1.8932 -0.1233 -0.0024 -0.2412 266 PRO A CD  
2016 N N   . SER A 267 ? 1.4539 1.3198 2.1798 -0.1273 0.0149  -0.2513 267 SER A N   
2017 C CA  . SER A 267 ? 1.7807 1.6742 2.5423 -0.1308 0.0223  -0.2600 267 SER A CA  
2018 C C   . SER A 267 ? 1.8515 1.7323 2.5943 -0.1494 0.0344  -0.2691 267 SER A C   
2019 O O   . SER A 267 ? 1.9110 1.7598 2.6128 -0.1553 0.0340  -0.2651 267 SER A O   
2020 C CB  . SER A 267 ? 1.9510 1.8634 2.7399 -0.1134 0.0142  -0.2532 267 SER A CB  
2021 O OG  . SER A 267 ? 1.8527 1.7469 2.6188 -0.1091 0.0099  -0.2461 267 SER A OG  
2022 N N   . GLY A 268 ? 1.7436 1.6508 2.5183 -0.1578 0.0448  -0.2822 268 GLY A N   
2023 C CA  . GLY A 268 ? 1.6663 1.5701 2.4316 -0.1764 0.0591  -0.2943 268 GLY A CA  
2024 C C   . GLY A 268 ? 1.4882 1.4194 2.2910 -0.1707 0.0618  -0.3017 268 GLY A C   
2025 O O   . GLY A 268 ? 1.3076 1.2695 2.1533 -0.1612 0.0588  -0.3062 268 GLY A O   
2026 N N   . LEU A 269 ? 1.4139 1.3302 2.1966 -0.1771 0.0667  -0.3032 269 LEU A N   
2027 C CA  . LEU A 269 ? 1.5028 1.4365 2.3117 -0.1703 0.0668  -0.3076 269 LEU A CA  
2028 C C   . LEU A 269 ? 1.4418 1.3767 2.2447 -0.1890 0.0837  -0.3237 269 LEU A C   
2029 O O   . LEU A 269 ? 1.5035 1.4095 2.2638 -0.2045 0.0910  -0.3240 269 LEU A O   
2030 C CB  . LEU A 269 ? 1.5992 1.5150 2.3917 -0.1573 0.0545  -0.2932 269 LEU A CB  
2031 C CG  . LEU A 269 ? 1.4494 1.3837 2.2721 -0.1472 0.0508  -0.2950 269 LEU A CG  
2032 C CD1 . LEU A 269 ? 1.2756 1.2332 2.1351 -0.1284 0.0379  -0.2876 269 LEU A CD1 
2033 C CD2 . LEU A 269 ? 1.4319 1.3417 2.2261 -0.1458 0.0460  -0.2874 269 LEU A CD2 
2034 N N   . GLY A 270 ? 1.4027 1.3704 2.2481 -0.1868 0.0889  -0.3374 270 GLY A N   
2035 C CA  . GLY A 270 ? 1.5516 1.5310 2.4025 -0.2035 0.1065  -0.3566 270 GLY A CA  
2036 C C   . GLY A 270 ? 1.5319 1.5296 2.4122 -0.1939 0.1054  -0.3643 270 GLY A C   
2037 O O   . GLY A 270 ? 1.2761 1.2925 2.1917 -0.1754 0.0929  -0.3611 270 GLY A O   
2038 N N   . HIS A 271 ? 1.7348 1.7258 2.5982 -0.2085 0.1195  -0.3758 271 HIS A N   
2039 C CA  . HIS A 271 ? 1.9177 1.9233 2.8031 -0.2036 0.1222  -0.3870 271 HIS A CA  
2040 C C   . HIS A 271 ? 2.0718 2.0996 2.9705 -0.2208 0.1433  -0.4118 271 HIS A C   
2041 O O   . HIS A 271 ? 1.8435 1.8568 2.7088 -0.2428 0.1589  -0.4175 271 HIS A O   
2042 C CB  . HIS A 271 ? 1.8948 1.8674 2.7434 -0.2018 0.1163  -0.3749 271 HIS A CB  
2043 C CG  . HIS A 271 ? 2.1347 2.1126 2.9915 -0.2016 0.1212  -0.3863 271 HIS A CG  
2044 N ND1 . HIS A 271 ? 2.3388 2.3012 3.1641 -0.2204 0.1373  -0.3969 271 HIS A ND1 
2045 C CD2 . HIS A 271 ? 2.4270 2.4203 3.3157 -0.1856 0.1118  -0.3884 271 HIS A CD2 
2046 C CE1 . HIS A 271 ? 2.5776 2.5479 3.4174 -0.2149 0.1380  -0.4059 271 HIS A CE1 
2047 N NE2 . HIS A 271 ? 2.7124 2.7010 3.5908 -0.1937 0.1221  -0.4009 271 HIS A NE2 
2048 N N   . ILE A 272 ? 2.2312 2.2948 3.1800 -0.2104 0.1427  -0.4270 272 ILE A N   
2049 C CA  . ILE A 272 ? 2.0990 2.1890 3.0683 -0.2221 0.1613  -0.4532 272 ILE A CA  
2050 C C   . ILE A 272 ? 2.1135 2.1984 3.0810 -0.2169 0.1619  -0.4589 272 ILE A C   
2051 O O   . ILE A 272 ? 1.8883 1.9781 2.8797 -0.1963 0.1453  -0.4533 272 ILE A O   
2052 C CB  . ILE A 272 ? 1.7960 1.9296 2.8244 -0.2117 0.1585  -0.4688 272 ILE A CB  
2053 C CG1 . ILE A 272 ? 1.4951 1.6309 2.5352 -0.2021 0.1439  -0.4549 272 ILE A CG1 
2054 C CG2 . ILE A 272 ? 1.7907 1.9547 2.8376 -0.2296 0.1811  -0.4967 272 ILE A CG2 
2055 C CD1 . ILE A 272 ? 1.4920 1.6468 2.5425 -0.2169 0.1555  -0.4664 272 ILE A CD1 
2056 N N   . GLU A 273 ? 2.1182 2.1929 3.0565 -0.2366 0.1810  -0.4706 273 GLU A N   
2057 C CA  . GLU A 273 ? 2.2375 2.3111 3.1756 -0.2344 0.1851  -0.4810 273 GLU A CA  
2058 C C   . GLU A 273 ? 2.6887 2.8088 3.6852 -0.2256 0.1894  -0.5058 273 GLU A C   
2059 O O   . GLU A 273 ? 2.7727 2.9211 3.8026 -0.2242 0.1899  -0.5133 273 GLU A O   
2060 C CB  . GLU A 273 ? 2.0483 2.0954 2.9345 -0.2592 0.2043  -0.4857 273 GLU A CB  
2061 C CG  . GLU A 273 ? 2.2567 2.2914 3.1311 -0.2559 0.2052  -0.4910 273 GLU A CG  
2062 C CD  . GLU A 273 ? 2.6439 2.6516 3.4653 -0.2816 0.2248  -0.4972 273 GLU A CD  
2063 O OE1 . GLU A 273 ? 3.1111 3.1037 3.8996 -0.3018 0.2353  -0.4937 273 GLU A OE1 
2064 O OE2 . GLU A 273 ? 2.3336 2.3332 3.1446 -0.2818 0.2290  -0.5053 273 GLU A OE2 
2065 N N   . ARG A 274 ? 2.7900 2.9156 3.7981 -0.2182 0.1900  -0.5177 274 ARG A N   
2066 C CA  . ARG A 274 ? 2.5917 2.7584 3.6536 -0.2075 0.1923  -0.5431 274 ARG A CA  
2067 C C   . ARG A 274 ? 2.7821 2.9769 3.8519 -0.2288 0.2198  -0.5702 274 ARG A C   
2068 O O   . ARG A 274 ? 2.9433 3.1796 4.0632 -0.2223 0.2231  -0.5927 274 ARG A O   
2069 C CB  . ARG A 274 ? 2.4347 2.5926 3.4993 -0.1938 0.1839  -0.5463 274 ARG A CB  
2070 C CG  . ARG A 274 ? 2.7396 2.8719 3.7565 -0.2122 0.2009  -0.5498 274 ARG A CG  
2071 C CD  . ARG A 274 ? 3.4626 3.5864 4.4812 -0.1999 0.1939  -0.5552 274 ARG A CD  
2072 N NE  . ARG A 274 ? 3.7889 3.8925 4.7639 -0.2196 0.2134  -0.5634 274 ARG A NE  
2073 C CZ  . ARG A 274 ? 3.7478 3.8110 4.6654 -0.2354 0.2172  -0.5463 274 ARG A CZ  
2074 N NH1 . ARG A 274 ? 3.5324 3.5715 4.4296 -0.2327 0.2024  -0.5198 274 ARG A NH1 
2075 N NH2 . ARG A 274 ? 3.7873 3.8333 4.6665 -0.2538 0.2352  -0.5564 274 ARG A NH2 
2076 N N   . ASP A 275 ? 2.7578 2.9302 3.7782 -0.2548 0.2389  -0.5686 275 ASP A N   
2077 C CA  . ASP A 275 ? 2.1910 2.3881 3.2134 -0.2792 0.2669  -0.5931 275 ASP A CA  
2078 C C   . ASP A 275 ? 2.0295 2.2317 3.0483 -0.2933 0.2714  -0.5873 275 ASP A C   
2079 O O   . ASP A 275 ? 1.9539 2.1589 2.9510 -0.3205 0.2942  -0.5981 275 ASP A O   
2080 C CB  . ASP A 275 ? 2.0870 2.2586 3.0583 -0.3015 0.2870  -0.5988 275 ASP A CB  
2081 C CG  . ASP A 275 ? 2.3299 2.4442 3.2324 -0.3126 0.2818  -0.5714 275 ASP A CG  
2082 O OD1 . ASP A 275 ? 2.3223 2.4210 3.2035 -0.3219 0.2792  -0.5563 275 ASP A OD1 
2083 O OD2 . ASP A 275 ? 2.6719 2.7567 3.5420 -0.3116 0.2796  -0.5661 275 ASP A OD2 
2084 N N   . GLY A 276 ? 2.0666 2.2678 3.1041 -0.2756 0.2496  -0.5699 276 GLY A N   
2085 C CA  . GLY A 276 ? 2.1274 2.3369 3.1696 -0.2844 0.2504  -0.5653 276 GLY A CA  
2086 C C   . GLY A 276 ? 2.2650 2.4284 3.2447 -0.3014 0.2513  -0.5421 276 GLY A C   
2087 O O   . GLY A 276 ? 2.2667 2.4305 3.2448 -0.3077 0.2493  -0.5352 276 GLY A O   
2088 N N   . THR A 277 ? 2.3129 2.4362 3.2422 -0.3075 0.2526  -0.5309 277 THR A N   
2089 C CA  . THR A 277 ? 2.4239 2.4997 3.2896 -0.3240 0.2531  -0.5110 277 THR A CA  
2090 C C   . THR A 277 ? 2.5693 2.6278 3.4338 -0.3055 0.2287  -0.4857 277 THR A C   
2091 O O   . THR A 277 ? 2.4063 2.4589 3.2827 -0.2823 0.2098  -0.4734 277 THR A O   
2092 C CB  . THR A 277 ? 2.2803 2.3174 3.0953 -0.3322 0.2573  -0.5059 277 THR A CB  
2093 O OG1 . THR A 277 ? 2.3237 2.3761 3.1329 -0.3561 0.2841  -0.5300 277 THR A OG1 
2094 C CG2 . THR A 277 ? 2.4403 2.4232 3.1894 -0.3437 0.2513  -0.4830 277 THR A CG2 
2095 N N   . VAL A 278 ? 2.6560 2.7084 3.5074 -0.3166 0.2299  -0.4793 278 VAL A N   
2096 C CA  . VAL A 278 ? 2.3363 2.3714 3.1819 -0.3020 0.2093  -0.4568 278 VAL A CA  
2097 C C   . VAL A 278 ? 2.2542 2.2348 3.0330 -0.3107 0.2045  -0.4368 278 VAL A C   
2098 O O   . VAL A 278 ? 2.5149 2.4717 3.2491 -0.3363 0.2196  -0.4408 278 VAL A O   
2099 C CB  . VAL A 278 ? 2.2534 2.3101 3.1208 -0.3080 0.2115  -0.4612 278 VAL A CB  
2100 C CG1 . VAL A 278 ? 2.1283 2.1688 2.9923 -0.2903 0.1895  -0.4386 278 VAL A CG1 
2101 C CG2 . VAL A 278 ? 2.0183 2.1296 2.9505 -0.3026 0.2179  -0.4846 278 VAL A CG2 
2102 N N   . ARG A 279 ? 1.9488 1.9100 2.7217 -0.2893 0.1828  -0.4161 279 ARG A N   
2103 C CA  . ARG A 279 ? 1.9183 1.8297 2.6341 -0.2916 0.1732  -0.3963 279 ARG A CA  
2104 C C   . ARG A 279 ? 1.8114 1.7145 2.5286 -0.2761 0.1546  -0.3780 279 ARG A C   
2105 O O   . ARG A 279 ? 1.7007 1.6267 2.4581 -0.2539 0.1413  -0.3729 279 ARG A O   
2106 C CB  . ARG A 279 ? 2.0000 1.8918 2.6979 -0.2851 0.1683  -0.3920 279 ARG A CB  
2107 C CG  . ARG A 279 ? 2.2409 2.1230 2.9111 -0.3086 0.1888  -0.4075 279 ARG A CG  
2108 C CD  . ARG A 279 ? 2.8705 2.7344 3.5247 -0.3024 0.1845  -0.4052 279 ARG A CD  
2109 N NE  . ARG A 279 ? 3.2392 3.1395 3.9445 -0.2867 0.1837  -0.4164 279 ARG A NE  
2110 C CZ  . ARG A 279 ? 3.2891 3.1793 3.9908 -0.2768 0.1767  -0.4141 279 ARG A CZ  
2111 N NH1 . ARG A 279 ? 3.4290 3.2752 4.0800 -0.2807 0.1697  -0.4010 279 ARG A NH1 
2112 N NH2 . ARG A 279 ? 3.0423 2.9642 3.7893 -0.2633 0.1757  -0.4253 279 ARG A NH2 
2113 N N   . VAL A 280 ? 1.8185 1.6887 2.4905 -0.2895 0.1547  -0.3697 280 VAL A N   
2114 C CA  . VAL A 280 ? 1.9154 1.7681 2.5759 -0.2758 0.1369  -0.3517 280 VAL A CA  
2115 C C   . VAL A 280 ? 2.1070 1.9328 2.7455 -0.2604 0.1213  -0.3366 280 VAL A C   
2116 O O   . VAL A 280 ? 2.2305 2.0175 2.8194 -0.2716 0.1221  -0.3327 280 VAL A O   
2117 C CB  . VAL A 280 ? 2.0688 1.8899 2.6833 -0.2952 0.1407  -0.3483 280 VAL A CB  
2118 C CG1 . VAL A 280 ? 2.1934 1.9718 2.7479 -0.3172 0.1492  -0.3491 280 VAL A CG1 
2119 C CG2 . VAL A 280 ? 2.3913 2.1925 2.9924 -0.2788 0.1211  -0.3303 280 VAL A CG2 
2120 N N   . VAL A 281 ? 2.0099 1.8574 2.6865 -0.2361 0.1077  -0.3296 281 VAL A N   
2121 C CA  . VAL A 281 ? 1.8726 1.7001 2.5341 -0.2216 0.0931  -0.3164 281 VAL A CA  
2122 C C   . VAL A 281 ? 1.9835 1.7776 2.6077 -0.2165 0.0796  -0.3006 281 VAL A C   
2123 O O   . VAL A 281 ? 2.3112 2.0662 2.8879 -0.2232 0.0760  -0.2951 281 VAL A O   
2124 C CB  . VAL A 281 ? 1.8353 1.6924 2.5436 -0.1992 0.0823  -0.3127 281 VAL A CB  
2125 C CG1 . VAL A 281 ? 1.8740 1.7093 2.5634 -0.1883 0.0690  -0.3005 281 VAL A CG1 
2126 C CG2 . VAL A 281 ? 2.2899 2.1804 3.0378 -0.2020 0.0936  -0.3296 281 VAL A CG2 
2127 N N   . ALA A 282 ? 1.8473 1.6557 2.4918 -0.2048 0.0717  -0.2944 282 ALA A N   
2128 C CA  . ALA A 282 ? 1.7703 1.5515 2.3855 -0.1956 0.0573  -0.2801 282 ALA A CA  
2129 C C   . ALA A 282 ? 1.7315 1.5278 2.3643 -0.1906 0.0549  -0.2784 282 ALA A C   
2130 O O   . ALA A 282 ? 1.6604 1.4926 2.3367 -0.1873 0.0594  -0.2849 282 ALA A O   
2131 C CB  . ALA A 282 ? 1.7504 1.5301 2.3719 -0.1749 0.0414  -0.2683 282 ALA A CB  
2132 N N   . CYS A 283 ? 1.6951 1.4607 2.2918 -0.1882 0.0453  -0.2689 283 CYS A N   
2133 C CA  . CYS A 283 ? 1.6400 1.4120 2.2452 -0.1797 0.0387  -0.2640 283 CYS A CA  
2134 C C   . CYS A 283 ? 1.5048 1.2617 2.0969 -0.1588 0.0206  -0.2500 283 CYS A C   
2135 O O   . CYS A 283 ? 1.4468 1.1686 1.9986 -0.1584 0.0128  -0.2444 283 CYS A O   
2136 C CB  . CYS A 283 ? 1.7492 1.4989 2.3222 -0.1997 0.0462  -0.2690 283 CYS A CB  
2137 S SG  . CYS A 283 ? 2.7902 2.5604 3.3786 -0.2263 0.0694  -0.2875 283 CYS A SG  
2138 N N   . HIS A 284 ? 1.4168 1.2013 2.0438 -0.1415 0.0139  -0.2452 284 HIS A N   
2139 C CA  . HIS A 284 ? 1.3158 1.0948 1.9380 -0.1212 -0.0012 -0.2337 284 HIS A CA  
2140 C C   . HIS A 284 ? 1.4729 1.2589 2.1021 -0.1152 -0.0045 -0.2315 284 HIS A C   
2141 O O   . HIS A 284 ? 1.4876 1.2856 2.1300 -0.1256 0.0037  -0.2384 284 HIS A O   
2142 C CB  . HIS A 284 ? 1.4013 1.2118 2.0632 -0.1042 -0.0067 -0.2288 284 HIS A CB  
2143 C CG  . HIS A 284 ? 1.5736 1.3885 2.2434 -0.1068 -0.0042 -0.2309 284 HIS A CG  
2144 N ND1 . HIS A 284 ? 1.6548 1.4828 2.3410 -0.1202 0.0081  -0.2412 284 HIS A ND1 
2145 C CD2 . HIS A 284 ? 1.5020 1.3118 2.1678 -0.0972 -0.0129 -0.2247 284 HIS A CD2 
2146 C CE1 . HIS A 284 ? 1.5232 1.3511 2.2122 -0.1187 0.0068  -0.2408 284 HIS A CE1 
2147 N NE2 . HIS A 284 ? 1.3790 1.1963 2.0565 -0.1050 -0.0061 -0.2304 284 HIS A NE2 
2148 N N   . ASP A 285 ? 1.5853 1.3648 2.2065 -0.0971 -0.0176 -0.2222 285 ASP A N   
2149 C CA  . ASP A 285 ? 1.6594 1.4449 2.2858 -0.0861 -0.0236 -0.2183 285 ASP A CA  
2150 C C   . ASP A 285 ? 1.4932 1.3101 2.1550 -0.0664 -0.0300 -0.2117 285 ASP A C   
2151 O O   . ASP A 285 ? 1.4599 1.2719 2.1130 -0.0513 -0.0400 -0.2050 285 ASP A O   
2152 C CB  . ASP A 285 ? 1.9175 1.6642 2.4978 -0.0833 -0.0329 -0.2147 285 ASP A CB  
2153 C CG  . ASP A 285 ? 2.0471 1.7740 2.6042 -0.0975 -0.0290 -0.2190 285 ASP A CG  
2154 O OD1 . ASP A 285 ? 1.9444 1.6889 2.5212 -0.0933 -0.0287 -0.2192 285 ASP A OD1 
2155 O OD2 . ASP A 285 ? 2.0540 1.7463 2.5717 -0.1133 -0.0269 -0.2220 285 ASP A OD2 
2156 N N   . GLN A 286 ? 1.5700 1.4188 2.2713 -0.0683 -0.0238 -0.2149 286 GLN A N   
2157 C CA  . GLN A 286 ? 1.5699 1.4487 2.3055 -0.0537 -0.0284 -0.2094 286 GLN A CA  
2158 C C   . GLN A 286 ? 1.5301 1.4068 2.2581 -0.0421 -0.0353 -0.2042 286 GLN A C   
2159 O O   . GLN A 286 ? 1.6449 1.5023 2.3499 -0.0473 -0.0351 -0.2066 286 GLN A O   
2160 C CB  . GLN A 286 ? 1.7280 1.6344 2.5013 -0.0592 -0.0222 -0.2151 286 GLN A CB  
2161 C CG  . GLN A 286 ? 1.8910 1.8043 2.6777 -0.0703 -0.0144 -0.2227 286 GLN A CG  
2162 C CD  . GLN A 286 ? 1.9997 1.9414 2.8263 -0.0716 -0.0112 -0.2288 286 GLN A CD  
2163 O OE1 . GLN A 286 ? 1.7869 1.7423 2.6308 -0.0642 -0.0159 -0.2262 286 GLN A OE1 
2164 N NE2 . GLN A 286 ? 2.3564 2.3060 3.1970 -0.0805 -0.0043 -0.2374 286 GLN A NE2 
2165 N N   . VAL A 287 ? 1.6337 1.5298 2.3798 -0.0272 -0.0412 -0.1972 287 VAL A N   
2166 C CA  . VAL A 287 ? 1.9302 1.8293 2.6733 -0.0154 -0.0467 -0.1927 287 VAL A CA  
2167 C C   . VAL A 287 ? 1.7914 1.7217 2.5700 -0.0096 -0.0470 -0.1891 287 VAL A C   
2168 O O   . VAL A 287 ? 1.7283 1.6737 2.5201 -0.0017 -0.0498 -0.1837 287 VAL A O   
2169 C CB  . VAL A 287 ? 2.2692 2.1539 2.9875 -0.0021 -0.0549 -0.1880 287 VAL A CB  
2170 C CG1 . VAL A 287 ? 2.2322 2.1222 2.9554 0.0020  -0.0575 -0.1854 287 VAL A CG1 
2171 C CG2 . VAL A 287 ? 2.4189 2.3143 3.1401 0.0125  -0.0599 -0.1836 287 VAL A CG2 
2172 N N   . LEU A 288 ? 1.8715 1.8100 2.6648 -0.0147 -0.0446 -0.1924 288 LEU A N   
2173 C CA  . LEU A 288 ? 2.1556 2.1190 2.9807 -0.0115 -0.0459 -0.1901 288 LEU A CA  
2174 C C   . LEU A 288 ? 2.2463 2.2216 3.0743 0.0017  -0.0511 -0.1808 288 LEU A C   
2175 O O   . LEU A 288 ? 1.9680 1.9603 2.8164 0.0031  -0.0520 -0.1772 288 LEU A O   
2176 C CB  . LEU A 288 ? 2.5201 2.4871 3.3550 -0.0150 -0.0461 -0.1941 288 LEU A CB  
2177 C CG  . LEU A 288 ? 2.7678 2.7284 3.6046 -0.0295 -0.0401 -0.2049 288 LEU A CG  
2178 C CD1 . LEU A 288 ? 2.3131 2.2784 3.1609 -0.0321 -0.0419 -0.2093 288 LEU A CD1 
2179 C CD2 . LEU A 288 ? 2.8729 2.8446 3.7305 -0.0376 -0.0349 -0.2109 288 LEU A CD2 
2180 N N   . SER A 289 ? 2.9680 2.9339 3.7745 0.0109  -0.0543 -0.1777 289 SER A N   
2181 C CA  . SER A 289 ? 3.6233 3.6012 4.4298 0.0237  -0.0578 -0.1708 289 SER A CA  
2182 C C   . SER A 289 ? 3.4680 3.4698 4.3007 0.0246  -0.0583 -0.1657 289 SER A C   
2183 O O   . SER A 289 ? 4.1475 4.1643 4.9945 0.0255  -0.0586 -0.1616 289 SER A O   
2184 C CB  . SER A 289 ? 4.0250 4.0009 4.8246 0.0276  -0.0592 -0.1697 289 SER A CB  
2185 O OG  . SER A 289 ? 4.5473 4.5323 5.3655 0.0199  -0.0570 -0.1698 289 SER A OG  
2186 N N   . GLY A 290 ? 2.8945 2.8972 3.7314 0.0234  -0.0593 -0.1660 290 GLY A N   
2187 C CA  . GLY A 290 ? 2.8991 2.9181 3.7570 0.0225  -0.0615 -0.1617 290 GLY A CA  
2188 C C   . GLY A 290 ? 3.1095 3.1342 3.9901 0.0133  -0.0612 -0.1650 290 GLY A C   
2189 O O   . GLY A 290 ? 3.2652 3.3018 4.1632 0.0123  -0.0643 -0.1610 290 GLY A O   
2190 N N   . GLY A 291 ? 3.0283 3.0431 3.9068 0.0063  -0.0576 -0.1725 291 GLY A N   
2191 C CA  . GLY A 291 ? 2.9728 2.9926 3.8722 -0.0021 -0.0563 -0.1783 291 GLY A CA  
2192 C C   . GLY A 291 ? 3.0813 3.1100 3.9916 -0.0025 -0.0566 -0.1748 291 GLY A C   
2193 O O   . GLY A 291 ? 3.4015 3.4320 4.3257 -0.0091 -0.0550 -0.1807 291 GLY A O   
2194 N N   . GLN A 292 ? 3.0461 3.0815 3.9511 0.0042  -0.0585 -0.1662 292 GLN A N   
2195 C CA  . GLN A 292 ? 2.7986 2.8425 3.7127 0.0035  -0.0593 -0.1624 292 GLN A CA  
2196 C C   . GLN A 292 ? 2.7498 2.7822 3.6502 0.0017  -0.0561 -0.1664 292 GLN A C   
2197 O O   . GLN A 292 ? 2.4070 2.4440 3.3107 0.0020  -0.0573 -0.1634 292 GLN A O   
2198 C CB  . GLN A 292 ? 2.4043 2.4620 3.3189 0.0100  -0.0619 -0.1528 292 GLN A CB  
2199 C CG  . GLN A 292 ? 2.6858 2.7514 3.6040 0.0124  -0.0646 -0.1475 292 GLN A CG  
2200 C CD  . GLN A 292 ? 2.8019 2.8720 3.7388 0.0067  -0.0693 -0.1458 292 GLN A CD  
2201 O OE1 . GLN A 292 ? 2.9328 2.9976 3.8738 0.0052  -0.0722 -0.1488 292 GLN A OE1 
2202 N NE2 . GLN A 292 ? 2.9330 3.0116 3.8808 0.0035  -0.0715 -0.1412 292 GLN A NE2 
2203 N N   . TYR A 293 ? 2.4211 2.4369 3.3043 -0.0010 -0.0526 -0.1729 293 TYR A N   
2204 C CA  . TYR A 293 ? 1.6750 1.6733 2.5394 -0.0052 -0.0497 -0.1776 293 TYR A CA  
2205 C C   . TYR A 293 ? 1.2089 1.2082 2.0656 0.0015  -0.0534 -0.1722 293 TYR A C   
2206 O O   . TYR A 293 ? 1.1718 1.1675 2.0290 -0.0025 -0.0533 -0.1735 293 TYR A O   
2207 C CB  . TYR A 293 ? 1.3643 1.3611 2.2405 -0.0166 -0.0450 -0.1857 293 TYR A CB  
2208 C CG  . TYR A 293 ? 1.1715 1.1523 2.0317 -0.0236 -0.0413 -0.1905 293 TYR A CG  
2209 C CD1 . TYR A 293 ? 1.1974 1.1813 2.0625 -0.0230 -0.0435 -0.1878 293 TYR A CD1 
2210 C CD2 . TYR A 293 ? 1.1891 1.1506 2.0283 -0.0323 -0.0357 -0.1978 293 TYR A CD2 
2211 C CE1 . TYR A 293 ? 1.3359 1.3027 2.1839 -0.0297 -0.0408 -0.1921 293 TYR A CE1 
2212 C CE2 . TYR A 293 ? 1.3378 1.2820 2.1588 -0.0404 -0.0322 -0.2020 293 TYR A CE2 
2213 C CZ  . TYR A 293 ? 1.4464 1.3928 2.2714 -0.0386 -0.0349 -0.1993 293 TYR A CZ  
2214 O OH  . TYR A 293 ? 1.6729 1.6003 2.4780 -0.0468 -0.0320 -0.2034 293 TYR A OH  
2215 N N   . TRP A 294 ? 1.0322 1.0381 1.8835 0.0121  -0.0570 -0.1667 294 TRP A N   
2216 C CA  . TRP A 294 ? 1.5043 1.5166 2.3540 0.0192  -0.0610 -0.1626 294 TRP A CA  
2217 C C   . TRP A 294 ? 1.6771 1.6664 2.5049 0.0171  -0.0624 -0.1670 294 TRP A C   
2218 O O   . TRP A 294 ? 2.4426 2.4331 3.2662 0.0235  -0.0675 -0.1651 294 TRP A O   
2219 C CB  . TRP A 294 ? 1.5857 1.6102 2.4326 0.0314  -0.0637 -0.1584 294 TRP A CB  
2220 C CG  . TRP A 294 ? 1.5814 1.6267 2.4473 0.0312  -0.0622 -0.1534 294 TRP A CG  
2221 C CD1 . TRP A 294 ? 1.3395 1.3835 2.2017 0.0327  -0.0609 -0.1533 294 TRP A CD1 
2222 C CD2 . TRP A 294 ? 2.0357 2.1024 2.9242 0.0280  -0.0628 -0.1475 294 TRP A CD2 
2223 N NE1 . TRP A 294 ? 1.6017 1.6640 2.4811 0.0311  -0.0609 -0.1477 294 TRP A NE1 
2224 C CE2 . TRP A 294 ? 2.2616 2.3375 3.1569 0.0276  -0.0619 -0.1440 294 TRP A CE2 
2225 C CE3 . TRP A 294 ? 2.0197 2.0967 2.9216 0.0247  -0.0646 -0.1448 294 TRP A CE3 
2226 C CZ2 . TRP A 294 ? 2.7956 2.8886 3.7082 0.0235  -0.0630 -0.1375 294 TRP A CZ2 
2227 C CZ3 . TRP A 294 ? 2.1625 2.2577 3.0831 0.0204  -0.0654 -0.1385 294 TRP A CZ3 
2228 C CH2 . TRP A 294 ? 2.5320 2.6343 3.4570 0.0195  -0.0646 -0.1348 294 TRP A CH2 
2229 N N   . GLY A 295 ? 1.1504 1.1196 1.9650 0.0073  -0.0582 -0.1732 295 GLY A N   
2230 C CA  . GLY A 295 ? 1.2591 1.2048 2.0529 0.0008  -0.0580 -0.1776 295 GLY A CA  
2231 C C   . GLY A 295 ? 1.1960 1.1165 1.9665 -0.0097 -0.0529 -0.1845 295 GLY A C   
2232 O O   . GLY A 295 ? 1.0239 0.9486 1.8015 -0.0146 -0.0480 -0.1874 295 GLY A O   
2233 N N   . CYS A 296 ? 1.2023 1.0955 1.9435 -0.0139 -0.0547 -0.1872 296 CYS A N   
2234 C CA  . CYS A 296 ? 0.9772 0.8431 1.6916 -0.0273 -0.0493 -0.1936 296 CYS A CA  
2235 C C   . CYS A 296 ? 1.1465 0.9791 1.8239 -0.0293 -0.0548 -0.1943 296 CYS A C   
2236 O O   . CYS A 296 ? 1.3083 1.1410 1.9854 -0.0218 -0.0621 -0.1911 296 CYS A O   
2237 C CB  . CYS A 296 ? 0.9522 0.8275 1.6843 -0.0419 -0.0390 -0.2000 296 CYS A CB  
2238 S SG  . CYS A 296 ? 1.3105 1.1796 2.0406 -0.0483 -0.0382 -0.2018 296 CYS A SG  
2239 N N   . ARG A 297 ? 1.1030 0.9053 1.7475 -0.0409 -0.0516 -0.1990 297 ARG A N   
2240 C CA  . ARG A 297 ? 1.2182 0.9808 1.8193 -0.0456 -0.0573 -0.2000 297 ARG A CA  
2241 C C   . ARG A 297 ? 1.2905 1.0324 1.8710 -0.0681 -0.0464 -0.2070 297 ARG A C   
2242 O O   . ARG A 297 ? 1.3778 1.1268 1.9659 -0.0803 -0.0356 -0.2122 297 ARG A O   
2243 C CB  . ARG A 297 ? 1.5799 1.3115 2.1440 -0.0394 -0.0667 -0.1987 297 ARG A CB  
2244 C CG  . ARG A 297 ? 1.9817 1.7205 2.5499 -0.0165 -0.0804 -0.1937 297 ARG A CG  
2245 C CD  . ARG A 297 ? 1.9952 1.6962 2.5209 -0.0089 -0.0929 -0.1938 297 ARG A CD  
2246 N NE  . ARG A 297 ? 2.2436 1.9602 2.7805 0.0087  -0.0985 -0.1918 297 ARG A NE  
2247 C CZ  . ARG A 297 ? 2.5445 2.3026 3.1213 0.0196  -0.0954 -0.1891 297 ARG A CZ  
2248 N NH1 . ARG A 297 ? 2.9337 2.6990 3.5127 0.0301  -0.0974 -0.1885 297 ARG A NH1 
2249 N NH2 . ARG A 297 ? 2.9495 2.7403 3.5621 0.0187  -0.0898 -0.1869 297 ARG A NH2 
2250 N N   . PHE A 298 ? 1.2943 1.0063 1.8433 -0.0737 -0.0504 -0.2076 298 PHE A N   
2251 C CA  . PHE A 298 ? 1.4227 1.1069 1.9410 -0.0961 -0.0410 -0.2141 298 PHE A CA  
2252 C C   . PHE A 298 ? 1.6621 1.2940 2.1224 -0.1001 -0.0511 -0.2127 298 PHE A C   
2253 O O   . PHE A 298 ? 1.9742 1.5907 2.4200 -0.0853 -0.0666 -0.2077 298 PHE A O   
2254 C CB  . PHE A 298 ? 1.5284 1.2285 2.0667 -0.1036 -0.0328 -0.2178 298 PHE A CB  
2255 C CG  . PHE A 298 ? 1.6021 1.2719 2.1051 -0.1259 -0.0237 -0.2246 298 PHE A CG  
2256 C CD1 . PHE A 298 ? 1.5866 1.2172 2.0473 -0.1279 -0.0329 -0.2223 298 PHE A CD1 
2257 C CD2 . PHE A 298 ? 1.7566 1.4372 2.2679 -0.1450 -0.0062 -0.2340 298 PHE A CD2 
2258 C CE1 . PHE A 298 ? 1.7272 1.3276 2.1515 -0.1496 -0.0242 -0.2282 298 PHE A CE1 
2259 C CE2 . PHE A 298 ? 1.9624 1.6162 2.4398 -0.1668 0.0036  -0.2409 298 PHE A CE2 
2260 C CZ  . PHE A 298 ? 1.8518 1.4648 2.2845 -0.1695 -0.0050 -0.2376 298 PHE A CZ  
2261 N N   . PRO A 299 ? 1.8068 1.4072 2.2297 -0.1219 -0.0431 -0.2177 299 PRO A N   
2262 C CA  . PRO A 299 ? 1.8095 1.4279 2.2483 -0.1407 -0.0247 -0.2253 299 PRO A CA  
2263 C C   . PRO A 299 ? 1.8620 1.4944 2.3150 -0.1361 -0.0244 -0.2246 299 PRO A C   
2264 O O   . PRO A 299 ? 2.0210 1.6507 2.4726 -0.1177 -0.0375 -0.2183 299 PRO A O   
2265 C CB  . PRO A 299 ? 1.7249 1.3013 2.1130 -0.1667 -0.0172 -0.2306 299 PRO A CB  
2266 C CG  . PRO A 299 ? 1.9699 1.4972 2.3069 -0.1595 -0.0356 -0.2240 299 PRO A CG  
2267 C CD  . PRO A 299 ? 1.9363 1.4805 2.2977 -0.1308 -0.0518 -0.2169 299 PRO A CD  
2268 N N   . ALA A 300 ? 1.9379 1.5853 2.4044 -0.1532 -0.0094 -0.2322 300 ALA A N   
2269 C CA  . ALA A 300 ? 2.0624 1.7195 2.5388 -0.1513 -0.0093 -0.2322 300 ALA A CA  
2270 C C   . ALA A 300 ? 2.1115 1.7201 2.5330 -0.1554 -0.0189 -0.2288 300 ALA A C   
2271 O O   . ALA A 300 ? 2.2465 1.8145 2.6225 -0.1647 -0.0227 -0.2281 300 ALA A O   
2272 C CB  . ALA A 300 ? 2.4693 2.1510 2.9701 -0.1701 0.0079  -0.2424 300 ALA A CB  
2273 N N   . ASP A 301 ? 2.1373 1.7484 2.5618 -0.1489 -0.0235 -0.2269 301 ASP A N   
2274 C CA  . ASP A 301 ? 2.4058 1.9710 2.7794 -0.1533 -0.0328 -0.2244 301 ASP A CA  
2275 C C   . ASP A 301 ? 2.5828 2.1175 2.9183 -0.1845 -0.0218 -0.2306 301 ASP A C   
2276 O O   . ASP A 301 ? 2.8185 2.3783 3.1775 -0.2025 -0.0050 -0.2385 301 ASP A O   
2277 C CB  . ASP A 301 ? 2.3822 1.9594 2.7698 -0.1414 -0.0384 -0.2222 301 ASP A CB  
2278 C CG  . ASP A 301 ? 2.4466 1.9760 2.7825 -0.1428 -0.0503 -0.2195 301 ASP A CG  
2279 O OD1 . ASP A 301 ? 2.5900 2.0741 2.8757 -0.1586 -0.0526 -0.2201 301 ASP A OD1 
2280 O OD2 . ASP A 301 ? 2.4798 2.0151 2.8233 -0.1280 -0.0582 -0.2167 301 ASP A OD2 
2281 N N   . GLU A 302 ? 2.6834 2.1633 2.9593 -0.1903 -0.0323 -0.2273 302 GLU A N   
2282 C CA  . GLU A 302 ? 2.6574 2.0976 2.8846 -0.2205 -0.0243 -0.2316 302 GLU A CA  
2283 C C   . GLU A 302 ? 2.3282 1.7786 2.5607 -0.2436 -0.0098 -0.2383 302 GLU A C   
2284 O O   . GLU A 302 ? 2.0471 1.4987 2.2731 -0.2706 0.0071  -0.2461 302 GLU A O   
2285 C CB  . GLU A 302 ? 3.0516 2.4264 3.2109 -0.2192 -0.0431 -0.2256 302 GLU A CB  
2286 C CG  . GLU A 302 ? 3.3262 2.6850 3.4740 -0.1985 -0.0614 -0.2200 302 GLU A CG  
2287 C CD  . GLU A 302 ? 3.5764 2.8820 3.6731 -0.1840 -0.0850 -0.2142 302 GLU A CD  
2288 O OE1 . GLU A 302 ? 3.8943 3.1432 3.9292 -0.2028 -0.0902 -0.2139 302 GLU A OE1 
2289 O OE2 . GLU A 302 ? 3.3300 2.6500 3.4474 -0.1545 -0.0987 -0.2105 302 GLU A OE2 
2290 N N   . ARG A 303 ? 2.2101 1.6686 2.4545 -0.2328 -0.0166 -0.2360 303 ARG A N   
2291 C CA  . ARG A 303 ? 2.3901 1.8560 2.6387 -0.2519 -0.0066 -0.2416 303 ARG A CA  
2292 C C   . ARG A 303 ? 2.3890 1.9104 2.6939 -0.2629 0.0137  -0.2516 303 ARG A C   
2293 O O   . ARG A 303 ? 2.6901 2.2113 2.9869 -0.2914 0.0293  -0.2602 303 ARG A O   
2294 C CB  . ARG A 303 ? 2.4505 1.9179 2.7063 -0.2328 -0.0200 -0.2365 303 ARG A CB  
2295 C CG  . ARG A 303 ? 2.7720 2.1771 2.9626 -0.2331 -0.0371 -0.2306 303 ARG A CG  
2296 C CD  . ARG A 303 ? 2.9012 2.3045 3.0967 -0.2001 -0.0563 -0.2236 303 ARG A CD  
2297 N NE  . ARG A 303 ? 3.3290 2.7322 3.5276 -0.1771 -0.0666 -0.2190 303 ARG A NE  
2298 C CZ  . ARG A 303 ? 3.5368 2.9457 3.7456 -0.1468 -0.0818 -0.2141 303 ARG A CZ  
2299 N NH1 . ARG A 303 ? 3.6853 3.1002 3.9017 -0.1351 -0.0879 -0.2129 303 ARG A NH1 
2300 N NH2 . ARG A 303 ? 3.5742 2.9842 3.7863 -0.1286 -0.0906 -0.2111 303 ARG A NH2 
2301 N N   . TRP A 304 ? 2.2643 1.8326 2.6254 -0.2404 0.0129  -0.2509 304 TRP A N   
2302 C CA  . TRP A 304 ? 2.2329 1.8537 2.6500 -0.2469 0.0289  -0.2607 304 TRP A CA  
2303 C C   . TRP A 304 ? 2.0133 1.6536 2.4507 -0.2467 0.0375  -0.2646 304 TRP A C   
2304 O O   . TRP A 304 ? 1.6785 1.3643 2.1672 -0.2441 0.0466  -0.2716 304 TRP A O   
2305 C CB  . TRP A 304 ? 2.3355 1.9961 2.8028 -0.2266 0.0238  -0.2594 304 TRP A CB  
2306 C CG  . TRP A 304 ? 2.6678 2.3236 3.1357 -0.1967 0.0061  -0.2479 304 TRP A CG  
2307 C CD1 . TRP A 304 ? 2.5680 2.2442 3.0619 -0.1750 0.0006  -0.2428 304 TRP A CD1 
2308 C CD2 . TRP A 304 ? 3.0623 2.6923 3.5038 -0.1861 -0.0077 -0.2410 304 TRP A CD2 
2309 N NE1 . TRP A 304 ? 3.0143 2.6807 3.4998 -0.1525 -0.0147 -0.2337 304 TRP A NE1 
2310 C CE2 . TRP A 304 ? 3.3610 2.9992 3.8148 -0.1576 -0.0203 -0.2327 304 TRP A CE2 
2311 C CE3 . TRP A 304 ? 3.3415 2.9419 3.7493 -0.1983 -0.0109 -0.2415 304 TRP A CE3 
2312 C CZ2 . TRP A 304 ? 3.8266 3.4461 4.2613 -0.1403 -0.0350 -0.2260 304 TRP A CZ2 
2313 C CZ3 . TRP A 304 ? 3.8978 3.4769 4.2853 -0.1806 -0.0267 -0.2342 304 TRP A CZ3 
2314 C CH2 . TRP A 304 ? 3.9307 3.5200 4.3320 -0.1514 -0.0383 -0.2270 304 TRP A CH2 
2315 N N   . ARG A 305 ? 2.2814 1.8864 2.6781 -0.2496 0.0337  -0.2605 305 ARG A N   
2316 C CA  . ARG A 305 ? 2.2536 1.8767 2.6692 -0.2499 0.0418  -0.2646 305 ARG A CA  
2317 C C   . ARG A 305 ? 2.0022 1.6364 2.4204 -0.2796 0.0633  -0.2783 305 ARG A C   
2318 O O   . ARG A 305 ? 1.6176 1.2944 2.0821 -0.2802 0.0751  -0.2876 305 ARG A O   
2319 C CB  . ARG A 305 ? 2.5904 2.1743 2.9648 -0.2430 0.0303  -0.2566 305 ARG A CB  
2320 C CG  . ARG A 305 ? 2.2954 1.8826 2.6707 -0.2507 0.0392  -0.2613 305 ARG A CG  
2321 C CD  . ARG A 305 ? 2.2486 1.7794 2.5594 -0.2613 0.0330  -0.2573 305 ARG A CD  
2322 N NE  . ARG A 305 ? 2.3889 1.8861 2.6697 -0.2431 0.0110  -0.2461 305 ARG A NE  
2323 C CZ  . ARG A 305 ? 2.3863 1.8338 2.6152 -0.2409 -0.0032 -0.2399 305 ARG A CZ  
2324 N NH1 . ARG A 305 ? 2.5975 2.0208 2.7965 -0.2557 0.0014  -0.2424 305 ARG A NH1 
2325 N NH2 . ARG A 305 ? 2.1991 1.6215 2.4072 -0.2226 -0.0231 -0.2317 305 ARG A NH2 
2326 N N   . PRO A 306 ? 2.2051 1.7974 2.5690 -0.3047 0.0676  -0.2798 306 PRO A N   
2327 C CA  . PRO A 306 ? 2.1383 1.7353 2.4947 -0.3367 0.0890  -0.2931 306 PRO A CA  
2328 C C   . PRO A 306 ? 1.9819 1.6319 2.3947 -0.3422 0.1022  -0.3052 306 PRO A C   
2329 O O   . PRO A 306 ? 1.5911 1.2758 2.0357 -0.3535 0.1194  -0.3186 306 PRO A O   
2330 C CB  . PRO A 306 ? 2.2772 1.8155 2.5624 -0.3597 0.0864  -0.2893 306 PRO A CB  
2331 C CG  . PRO A 306 ? 2.1962 1.6905 2.4432 -0.3378 0.0624  -0.2742 306 PRO A CG  
2332 C CD  . PRO A 306 ? 2.2911 1.8256 2.5935 -0.3039 0.0514  -0.2691 306 PRO A CD  
2333 N N   . GLU A 307 ? 1.9159 1.5706 2.3396 -0.3330 0.0927  -0.3007 307 GLU A N   
2334 C CA  . GLU A 307 ? 1.8443 1.5449 2.3190 -0.3359 0.1008  -0.3109 307 GLU A CA  
2335 C C   . GLU A 307 ? 1.6905 1.4442 2.2304 -0.3173 0.1038  -0.3169 307 GLU A C   
2336 O O   . GLU A 307 ? 1.3841 1.1781 1.9648 -0.3276 0.1183  -0.3320 307 GLU A O   
2337 C CB  . GLU A 307 ? 1.9891 1.6802 2.4612 -0.3223 0.0852  -0.3019 307 GLU A CB  
2338 C CG  . GLU A 307 ? 2.4019 2.0379 2.8092 -0.3382 0.0790  -0.2954 307 GLU A CG  
2339 C CD  . GLU A 307 ? 2.8033 2.4333 3.2091 -0.3333 0.0683  -0.2912 307 GLU A CD  
2340 O OE1 . GLU A 307 ? 3.1617 2.8056 3.5927 -0.3054 0.0545  -0.2839 307 GLU A OE1 
2341 O OE2 . GLU A 307 ? 2.9116 2.5205 3.2877 -0.3584 0.0734  -0.2950 307 GLU A OE2 
2342 N N   . ILE A 308 ? 1.9422 1.6938 2.4897 -0.2897 0.0890  -0.3053 308 ILE A N   
2343 C CA  . ILE A 308 ? 1.9323 1.7266 2.5352 -0.2697 0.0878  -0.3078 308 ILE A CA  
2344 C C   . ILE A 308 ? 1.8097 1.6201 2.4245 -0.2824 0.1035  -0.3200 308 ILE A C   
2345 O O   . ILE A 308 ? 1.6139 1.4673 2.2798 -0.2780 0.1098  -0.3306 308 ILE A O   
2346 C CB  . ILE A 308 ? 1.8514 1.6405 2.4583 -0.2402 0.0698  -0.2930 308 ILE A CB  
2347 C CG1 . ILE A 308 ? 2.0402 1.8262 2.6492 -0.2250 0.0559  -0.2839 308 ILE A CG1 
2348 C CG2 . ILE A 308 ? 1.8142 1.6434 2.4725 -0.2255 0.0709  -0.2968 308 ILE A CG2 
2349 C CD1 . ILE A 308 ? 2.2544 2.0427 2.8735 -0.1965 0.0402  -0.2711 308 ILE A CD1 
2350 N N   . THR A 309 ? 1.8260 1.6000 2.3927 -0.2959 0.1076  -0.3180 309 THR A N   
2351 C CA  . THR A 309 ? 1.8238 1.6062 2.3939 -0.3061 0.1209  -0.3277 309 THR A CA  
2352 C C   . THR A 309 ? 1.9121 1.7312 2.5137 -0.3265 0.1416  -0.3477 309 THR A C   
2353 O O   . THR A 309 ? 1.7995 1.6557 2.4438 -0.3221 0.1496  -0.3592 309 THR A O   
2354 C CB  . THR A 309 ? 2.1454 1.8749 2.6485 -0.3224 0.1220  -0.3225 309 THR A CB  
2355 O OG1 . THR A 309 ? 2.4169 2.1243 2.9053 -0.2994 0.1035  -0.3075 309 THR A OG1 
2356 C CG2 . THR A 309 ? 2.1544 1.8870 2.6492 -0.3435 0.1409  -0.3356 309 THR A CG2 
2357 N N   . ASP A 310 ? 2.1143 1.9207 2.6922 -0.3491 0.1493  -0.3519 310 ASP A N   
2358 C CA  . ASP A 310 ? 2.2105 2.0499 2.8135 -0.3726 0.1699  -0.3717 310 ASP A CA  
2359 C C   . ASP A 310 ? 2.0896 1.9855 2.7653 -0.3555 0.1683  -0.3813 310 ASP A C   
2360 O O   . ASP A 310 ? 2.1199 2.0556 2.8358 -0.3610 0.1822  -0.3992 310 ASP A O   
2361 C CB  . ASP A 310 ? 2.4372 2.2498 2.9981 -0.4014 0.1773  -0.3733 310 ASP A CB  
2362 C CG  . ASP A 310 ? 2.6605 2.4324 3.1602 -0.4299 0.1900  -0.3750 310 ASP A CG  
2363 O OD1 . ASP A 310 ? 2.5153 2.3064 3.0260 -0.4417 0.2071  -0.3886 310 ASP A OD1 
2364 O OD2 . ASP A 310 ? 2.9556 2.6755 3.3954 -0.4403 0.1822  -0.3632 310 ASP A OD2 
2365 N N   . ALA A 311 ? 1.8697 1.7662 2.5594 -0.3344 0.1504  -0.3695 311 ALA A N   
2366 C CA  . ALA A 311 ? 1.5500 1.4920 2.3022 -0.3161 0.1443  -0.3754 311 ALA A CA  
2367 C C   . ALA A 311 ? 1.3351 1.3054 2.1267 -0.2987 0.1436  -0.3804 311 ALA A C   
2368 O O   . ALA A 311 ? 1.2094 1.2227 2.0521 -0.2965 0.1497  -0.3964 311 ALA A O   
2369 C CB  . ALA A 311 ? 1.5234 1.4507 2.2709 -0.2956 0.1240  -0.3585 311 ALA A CB  
2370 N N   . VAL A 312 ? 1.4439 1.3879 2.2101 -0.2861 0.1349  -0.3667 312 VAL A N   
2371 C CA  . VAL A 312 ? 1.5474 1.5097 2.3423 -0.2691 0.1318  -0.3681 312 VAL A CA  
2372 C C   . VAL A 312 ? 1.4841 1.4682 2.2941 -0.2854 0.1510  -0.3881 312 VAL A C   
2373 O O   . VAL A 312 ? 1.4329 1.4531 2.2907 -0.2747 0.1519  -0.3994 312 VAL A O   
2374 C CB  . VAL A 312 ? 1.8792 1.8118 2.6468 -0.2529 0.1185  -0.3504 312 VAL A CB  
2375 C CG1 . VAL A 312 ? 1.6512 1.5917 2.4289 -0.2496 0.1231  -0.3560 312 VAL A CG1 
2376 C CG2 . VAL A 312 ? 2.2151 2.1523 3.0010 -0.2272 0.0990  -0.3359 312 VAL A CG2 
2377 N N   . ARG A 313 ? 1.6443 1.6041 2.4109 -0.3113 0.1657  -0.3926 313 ARG A N   
2378 C CA  . ARG A 313 ? 1.7160 1.6923 2.4878 -0.3308 0.1868  -0.4121 313 ARG A CA  
2379 C C   . ARG A 313 ? 1.7610 1.7892 2.5893 -0.3354 0.1972  -0.4335 313 ARG A C   
2380 O O   . ARG A 313 ? 1.6662 1.7286 2.5333 -0.3318 0.2053  -0.4501 313 ARG A O   
2381 C CB  . ARG A 313 ? 1.7465 1.6823 2.4546 -0.3601 0.2000  -0.4114 313 ARG A CB  
2382 C CG  . ARG A 313 ? 1.8572 1.8083 2.5645 -0.3846 0.2246  -0.4323 313 ARG A CG  
2383 C CD  . ARG A 313 ? 2.2933 2.2237 2.9571 -0.4200 0.2409  -0.4378 313 ARG A CD  
2384 N NE  . ARG A 313 ? 2.3685 2.3149 3.0513 -0.4247 0.2389  -0.4394 313 ARG A NE  
2385 C CZ  . ARG A 313 ? 2.1689 2.1058 2.8260 -0.4536 0.2508  -0.4448 313 ARG A CZ  
2386 N NH1 . ARG A 313 ? 2.2792 2.1977 2.8950 -0.4847 0.2705  -0.4532 313 ARG A NH1 
2387 N NH2 . ARG A 313 ? 1.9966 1.9422 2.6689 -0.4523 0.2432  -0.4420 313 ARG A NH2 
2388 N N   . ARG A 314 ? 1.8078 1.8402 2.6397 -0.3424 0.1954  -0.4330 314 ARG A N   
2389 C CA  . ARG A 314 ? 1.4780 1.5586 2.3628 -0.3475 0.2034  -0.4530 314 ARG A CA  
2390 C C   . ARG A 314 ? 1.3278 1.4462 2.2742 -0.3185 0.1907  -0.4581 314 ARG A C   
2391 O O   . ARG A 314 ? 1.2870 1.4482 2.2812 -0.3180 0.1995  -0.4798 314 ARG A O   
2392 C CB  . ARG A 314 ? 1.5609 1.6376 2.4376 -0.3605 0.2023  -0.4512 314 ARG A CB  
2393 C CG  . ARG A 314 ? 1.7775 1.8246 2.5997 -0.3950 0.2194  -0.4532 314 ARG A CG  
2394 C CD  . ARG A 314 ? 1.8404 1.8783 2.6489 -0.4094 0.2174  -0.4502 314 ARG A CD  
2395 N NE  . ARG A 314 ? 1.7874 1.7824 2.5592 -0.3954 0.1967  -0.4261 314 ARG A NE  
2396 C CZ  . ARG A 314 ? 1.8280 1.8310 2.6230 -0.3771 0.1799  -0.4185 314 ARG A CZ  
2397 N NH1 . ARG A 314 ? 1.8163 1.8673 2.6734 -0.3664 0.1779  -0.4313 314 ARG A NH1 
2398 N NH2 . ARG A 314 ? 1.6281 1.5898 2.3831 -0.3688 0.1640  -0.3986 314 ARG A NH2 
2399 N N   . THR A 315 ? 1.3213 1.4213 2.2632 -0.2944 0.1693  -0.4376 315 THR A N   
2400 C CA  . THR A 315 ? 1.2112 1.3371 2.2018 -0.2665 0.1536  -0.4374 315 THR A CA  
2401 C C   . THR A 315 ? 1.1994 1.3394 2.2082 -0.2599 0.1585  -0.4474 315 THR A C   
2402 O O   . THR A 315 ? 1.1562 1.3320 2.2151 -0.2483 0.1560  -0.4618 315 THR A O   
2403 C CB  . THR A 315 ? 1.2343 1.3338 2.2080 -0.2456 0.1323  -0.4128 315 THR A CB  
2404 O OG1 . THR A 315 ? 1.4409 1.5176 2.3824 -0.2564 0.1311  -0.4038 315 THR A OG1 
2405 C CG2 . THR A 315 ? 1.2450 1.3707 2.2673 -0.2211 0.1156  -0.4126 315 THR A CG2 
2406 N N   . GLY A 316 ? 1.3616 1.4710 2.3278 -0.2668 0.1641  -0.4396 316 GLY A N   
2407 C CA  . GLY A 316 ? 1.5231 1.6377 2.4962 -0.2622 0.1688  -0.4469 316 GLY A CA  
2408 C C   . GLY A 316 ? 1.3822 1.5347 2.3880 -0.2757 0.1878  -0.4750 316 GLY A C   
2409 O O   . GLY A 316 ? 1.2868 1.4660 2.3321 -0.2621 0.1856  -0.4872 316 GLY A O   
2410 N N   . GLU A 317 ? 1.4884 1.6424 2.4768 -0.3025 0.2060  -0.4852 317 GLU A N   
2411 C CA  . GLU A 317 ? 1.5183 1.7106 2.5357 -0.3194 0.2273  -0.5137 317 GLU A CA  
2412 C C   . GLU A 317 ? 1.4225 1.6643 2.5101 -0.3021 0.2194  -0.5299 317 GLU A C   
2413 O O   . GLU A 317 ? 1.5578 1.8342 2.6858 -0.2965 0.2258  -0.5514 317 GLU A O   
2414 C CB  . GLU A 317 ? 1.7851 1.9664 2.7655 -0.3539 0.2482  -0.5198 317 GLU A CB  
2415 C CG  . GLU A 317 ? 2.1160 2.2526 3.0313 -0.3715 0.2585  -0.5108 317 GLU A CG  
2416 C CD  . GLU A 317 ? 2.8779 2.9823 3.7378 -0.4027 0.2705  -0.5057 317 GLU A CD  
2417 O OE1 . GLU A 317 ? 3.4055 3.5239 4.2772 -0.4135 0.2729  -0.5099 317 GLU A OE1 
2418 O OE2 . GLU A 317 ? 3.4233 3.4858 4.2257 -0.4166 0.2763  -0.4972 317 GLU A OE2 
2419 N N   . VAL A 318 ? 1.3498 1.5916 2.4487 -0.2930 0.2042  -0.5192 318 VAL A N   
2420 C CA  . VAL A 318 ? 1.3284 1.6108 2.4887 -0.2765 0.1931  -0.5318 318 VAL A CA  
2421 C C   . VAL A 318 ? 1.5713 1.8639 2.7638 -0.2482 0.1776  -0.5324 318 VAL A C   
2422 O O   . VAL A 318 ? 1.6140 1.9454 2.8581 -0.2386 0.1769  -0.5539 318 VAL A O   
2423 C CB  . VAL A 318 ? 1.4828 1.7565 2.6429 -0.2705 0.1774  -0.5173 318 VAL A CB  
2424 C CG1 . VAL A 318 ? 1.2343 1.5443 2.4552 -0.2497 0.1615  -0.5279 318 VAL A CG1 
2425 C CG2 . VAL A 318 ? 1.8951 2.1618 3.0282 -0.2989 0.1919  -0.5196 318 VAL A CG2 
2426 N N   . LEU A 319 ? 1.8358 2.0922 2.9965 -0.2352 0.1643  -0.5086 319 LEU A N   
2427 C CA  . LEU A 319 ? 1.8080 2.0667 2.9911 -0.2099 0.1479  -0.5049 319 LEU A CA  
2428 C C   . LEU A 319 ? 1.6847 1.9607 2.8826 -0.2123 0.1606  -0.5250 319 LEU A C   
2429 O O   . LEU A 319 ? 1.7539 2.0540 2.9946 -0.1947 0.1513  -0.5373 319 LEU A O   
2430 C CB  . LEU A 319 ? 2.0184 2.2408 3.1721 -0.1942 0.1294  -0.4761 319 LEU A CB  
2431 C CG  . LEU A 319 ? 2.1746 2.3999 3.3488 -0.1765 0.1083  -0.4647 319 LEU A CG  
2432 C CD1 . LEU A 319 ? 2.3223 2.5127 3.4638 -0.1642 0.0930  -0.4367 319 LEU A CD1 
2433 C CD2 . LEU A 319 ? 1.7764 2.0346 3.0065 -0.1588 0.0970  -0.4808 319 LEU A CD2 
2434 N N   . SER A 320 ? 1.7093 1.9714 2.8703 -0.2342 0.1811  -0.5287 320 SER A N   
2435 C CA  . SER A 320 ? 1.7477 2.0240 2.9162 -0.2398 0.1962  -0.5486 320 SER A CA  
2436 C C   . SER A 320 ? 1.8602 2.1886 3.0859 -0.2406 0.2052  -0.5800 320 SER A C   
2437 O O   . SER A 320 ? 1.8006 2.1512 3.0603 -0.2271 0.2031  -0.5966 320 SER A O   
2438 C CB  . SER A 320 ? 1.7724 2.0217 2.8867 -0.2655 0.2167  -0.5465 320 SER A CB  
2439 O OG  . SER A 320 ? 1.6875 1.9484 2.8083 -0.2679 0.2292  -0.5645 320 SER A OG  
2440 N N   . GLY A 321 ? 1.9523 2.2991 3.1879 -0.2561 0.2141  -0.5881 321 GLY A N   
2441 C CA  . GLY A 321 ? 1.9078 2.3072 3.1997 -0.2585 0.2226  -0.6186 321 GLY A CA  
2442 C C   . GLY A 321 ? 1.8775 2.3001 3.2245 -0.2271 0.1985  -0.6245 321 GLY A C   
2443 O O   . GLY A 321 ? 2.2638 2.7226 3.6569 -0.2174 0.2002  -0.6501 321 GLY A O   
2444 N N   . LEU A 322 ? 1.6790 2.0779 3.0180 -0.2112 0.1753  -0.6002 322 LEU A N   
2445 C CA  . LEU A 322 ? 1.5257 1.9363 2.9068 -0.1823 0.1490  -0.6000 322 LEU A CA  
2446 C C   . LEU A 322 ? 1.5298 1.9369 2.9197 -0.1649 0.1418  -0.6040 322 LEU A C   
2447 O O   . LEU A 322 ? 1.5029 1.9360 2.9389 -0.1471 0.1311  -0.6220 322 LEU A O   
2448 C CB  . LEU A 322 ? 1.4729 1.8533 2.8339 -0.1713 0.1276  -0.5708 322 LEU A CB  
2449 C CG  . LEU A 322 ? 1.5443 1.9398 2.9253 -0.1736 0.1212  -0.5725 322 LEU A CG  
2450 C CD1 . LEU A 322 ? 1.5314 1.9237 2.8840 -0.2021 0.1415  -0.5725 322 LEU A CD1 
2451 C CD2 . LEU A 322 ? 1.6440 2.0147 3.0171 -0.1547 0.0953  -0.5478 322 LEU A CD2 
2452 N N   . GLY A 323 ? 1.7165 2.0909 3.0587 -0.1734 0.1505  -0.5895 323 GLY A N   
2453 C CA  . GLY A 323 ? 1.6907 2.0578 3.0293 -0.1648 0.1505  -0.5939 323 GLY A CA  
2454 C C   . GLY A 323 ? 1.7139 2.0403 3.0220 -0.1501 0.1309  -0.5645 323 GLY A C   
2455 O O   . GLY A 323 ? 1.5831 1.9056 2.9029 -0.1332 0.1187  -0.5655 323 GLY A O   
2456 N N   . HIS A 324 ? 1.9633 2.2597 3.2331 -0.1561 0.1270  -0.5387 324 HIS A N   
2457 C CA  . HIS A 324 ? 1.9925 2.2535 3.2340 -0.1436 0.1101  -0.5117 324 HIS A CA  
2458 C C   . HIS A 324 ? 2.1580 2.3913 3.3531 -0.1567 0.1231  -0.5042 324 HIS A C   
2459 O O   . HIS A 324 ? 2.4319 2.6545 3.5943 -0.1777 0.1403  -0.5034 324 HIS A O   
2460 C CB  . HIS A 324 ? 2.0243 2.2666 3.2485 -0.1403 0.0973  -0.4877 324 HIS A CB  
2461 C CG  . HIS A 324 ? 1.9306 2.1458 3.1384 -0.1245 0.0780  -0.4638 324 HIS A CG  
2462 N ND1 . HIS A 324 ? 1.8467 2.0300 3.0123 -0.1273 0.0745  -0.4388 324 HIS A ND1 
2463 C CD2 . HIS A 324 ? 2.0707 2.2874 3.3000 -0.1060 0.0613  -0.4629 324 HIS A CD2 
2464 C CE1 . HIS A 324 ? 2.1183 2.2878 3.2828 -0.1115 0.0573  -0.4238 324 HIS A CE1 
2465 N NE2 . HIS A 324 ? 2.3875 2.5755 3.5891 -0.0990 0.0488  -0.4374 324 HIS A NE2 
2466 N N   . ARG A 325 ? 2.0553 2.2750 3.2467 -0.1443 0.1133  -0.4988 325 ARG A N   
2467 C CA  . ARG A 325 ? 1.8503 2.0403 2.9979 -0.1532 0.1208  -0.4895 325 ARG A CA  
2468 C C   . ARG A 325 ? 1.8248 1.9847 2.9507 -0.1404 0.1009  -0.4610 325 ARG A C   
2469 O O   . ARG A 325 ? 1.7047 1.8701 2.8560 -0.1222 0.0817  -0.4544 325 ARG A O   
2470 C CB  . ARG A 325 ? 1.9314 2.1350 3.0920 -0.1545 0.1316  -0.5122 325 ARG A CB  
2471 C CG  . ARG A 325 ? 2.1009 2.3295 3.2681 -0.1748 0.1570  -0.5367 325 ARG A CG  
2472 C CD  . ARG A 325 ? 2.3641 2.6275 3.5677 -0.1747 0.1692  -0.5688 325 ARG A CD  
2473 N NE  . ARG A 325 ? 2.7342 3.0333 3.9966 -0.1560 0.1566  -0.5847 325 ARG A NE  
2474 C CZ  . ARG A 325 ? 3.2241 3.5590 4.5271 -0.1520 0.1641  -0.6151 325 ARG A CZ  
2475 N NH1 . ARG A 325 ? 3.6497 3.9953 4.9430 -0.1689 0.1886  -0.6347 325 ARG A NH1 
2476 N NH2 . ARG A 325 ? 3.3774 3.7379 4.7309 -0.1313 0.1471  -0.6268 325 ARG A NH2 
2477 N N   . GLY A 326 ? 2.1945 2.3226 3.2727 -0.1508 0.1052  -0.4446 326 GLY A N   
2478 C CA  . GLY A 326 ? 2.3340 2.4357 3.3902 -0.1408 0.0883  -0.4183 326 GLY A CA  
2479 C C   . GLY A 326 ? 2.1464 2.2305 3.1711 -0.1498 0.0904  -0.4031 326 GLY A C   
2480 O O   . GLY A 326 ? 2.1335 2.2038 3.1258 -0.1678 0.1054  -0.4061 326 GLY A O   
2481 N N   . ALA A 327 ? 1.9231 2.0064 2.9560 -0.1375 0.0750  -0.3877 327 ALA A N   
2482 C CA  . ALA A 327 ? 1.6897 1.7526 2.6914 -0.1412 0.0724  -0.3702 327 ALA A CA  
2483 C C   . ALA A 327 ? 1.4832 1.5620 2.5079 -0.1349 0.0655  -0.3682 327 ALA A C   
2484 O O   . ALA A 327 ? 1.5146 1.6109 2.5736 -0.1207 0.0534  -0.3690 327 ALA A O   
2485 C CB  . ALA A 327 ? 1.8571 1.8960 2.8358 -0.1318 0.0594  -0.3497 327 ALA A CB  
2486 N N   . PHE A 328 ? 1.2530 1.3213 2.2538 -0.1460 0.0721  -0.3644 328 PHE A N   
2487 C CA  . PHE A 328 ? 1.1508 1.2294 2.1651 -0.1431 0.0672  -0.3622 328 PHE A CA  
2488 C C   . PHE A 328 ? 1.0056 1.0564 1.9805 -0.1448 0.0631  -0.3437 328 PHE A C   
2489 O O   . PHE A 328 ? 1.0556 1.0798 1.9896 -0.1550 0.0690  -0.3378 328 PHE A O   
2490 C CB  . PHE A 328 ? 1.4016 1.5045 2.4382 -0.1557 0.0803  -0.3833 328 PHE A CB  
2491 C CG  . PHE A 328 ? 1.5238 1.6109 2.5234 -0.1788 0.0984  -0.3883 328 PHE A CG  
2492 C CD1 . PHE A 328 ? 1.5583 1.6262 2.5277 -0.1875 0.0991  -0.3786 328 PHE A CD1 
2493 C CD2 . PHE A 328 ? 1.5348 1.6218 2.5250 -0.1921 0.1137  -0.4015 328 PHE A CD2 
2494 C CE1 . PHE A 328 ? 1.6852 1.7330 2.6153 -0.2095 0.1138  -0.3817 328 PHE A CE1 
2495 C CE2 . PHE A 328 ? 1.3618 1.4301 2.3128 -0.2149 0.1298  -0.4049 328 PHE A CE2 
2496 C CZ  . PHE A 328 ? 1.5216 1.5695 2.4421 -0.2239 0.1294  -0.3947 328 PHE A CZ  
2497 N N   . GLY A 329 ? 0.8698 0.9266 1.8572 -0.1350 0.0524  -0.3360 329 GLY A N   
2498 C CA  . GLY A 329 ? 0.8890 0.9241 1.8465 -0.1325 0.0459  -0.3195 329 GLY A CA  
2499 C C   . GLY A 329 ? 0.9444 0.9881 1.9105 -0.1359 0.0460  -0.3231 329 GLY A C   
2500 O O   . GLY A 329 ? 0.8780 0.9460 1.8812 -0.1294 0.0412  -0.3307 329 GLY A O   
2501 N N   . VAL A 330 ? 1.1567 1.1774 2.0858 -0.1459 0.0501  -0.3175 330 VAL A N   
2502 C CA  . VAL A 330 ? 1.2202 1.2415 2.1484 -0.1490 0.0483  -0.3175 330 VAL A CA  
2503 C C   . VAL A 330 ? 1.3313 1.3271 2.2279 -0.1399 0.0376  -0.2993 330 VAL A C   
2504 O O   . VAL A 330 ? 1.3240 1.2924 2.1822 -0.1437 0.0388  -0.2916 330 VAL A O   
2505 C CB  . VAL A 330 ? 1.1790 1.1962 2.0917 -0.1720 0.0635  -0.3300 330 VAL A CB  
2506 C CG1 . VAL A 330 ? 1.2831 1.3113 2.2097 -0.1747 0.0612  -0.3341 330 VAL A CG1 
2507 C CG2 . VAL A 330 ? 1.3756 1.4132 2.3089 -0.1838 0.0777  -0.3485 330 VAL A CG2 
2508 N N   . ASP A 331 ? 1.4062 1.4121 2.3210 -0.1266 0.0263  -0.2933 331 ASP A N   
2509 C CA  . ASP A 331 ? 1.7133 1.7003 2.6034 -0.1167 0.0165  -0.2783 331 ASP A CA  
2510 C C   . ASP A 331 ? 1.6516 1.6314 2.5301 -0.1257 0.0181  -0.2817 331 ASP A C   
2511 O O   . ASP A 331 ? 1.6687 1.6682 2.5742 -0.1310 0.0202  -0.2926 331 ASP A O   
2512 C CB  . ASP A 331 ? 2.1354 2.1336 3.0453 -0.0973 0.0035  -0.2680 331 ASP A CB  
2513 C CG  . ASP A 331 ? 2.8417 2.8212 3.7241 -0.0858 -0.0051 -0.2522 331 ASP A CG  
2514 O OD1 . ASP A 331 ? 3.0902 3.0451 3.9363 -0.0907 -0.0026 -0.2484 331 ASP A OD1 
2515 O OD2 . ASP A 331 ? 3.0484 3.0373 3.9446 -0.0722 -0.0146 -0.2443 331 ASP A OD2 
2516 N N   . PHE A 332 ? 1.4555 1.4057 2.2931 -0.1266 0.0156  -0.2723 332 PHE A N   
2517 C CA  . PHE A 332 ? 1.1950 1.1293 2.0104 -0.1360 0.0162  -0.2736 332 PHE A CA  
2518 C C   . PHE A 332 ? 1.0736 0.9907 1.8683 -0.1211 0.0037  -0.2602 332 PHE A C   
2519 O O   . PHE A 332 ? 1.4060 1.3149 2.1896 -0.1065 -0.0035 -0.2492 332 PHE A O   
2520 C CB  . PHE A 332 ? 1.3014 1.2073 2.0760 -0.1545 0.0254  -0.2763 332 PHE A CB  
2521 C CG  . PHE A 332 ? 1.4633 1.3804 2.2475 -0.1727 0.0404  -0.2900 332 PHE A CG  
2522 C CD1 . PHE A 332 ? 1.4158 1.3537 2.2226 -0.1884 0.0503  -0.3049 332 PHE A CD1 
2523 C CD2 . PHE A 332 ? 1.6851 1.5915 2.4541 -0.1750 0.0448  -0.2888 332 PHE A CD2 
2524 C CE1 . PHE A 332 ? 1.4689 1.4186 2.2840 -0.2054 0.0654  -0.3188 332 PHE A CE1 
2525 C CE2 . PHE A 332 ? 1.6538 1.5691 2.4285 -0.1922 0.0593  -0.3020 332 PHE A CE2 
2526 C CZ  . PHE A 332 ? 1.5440 1.4816 2.3418 -0.2075 0.0703  -0.3173 332 PHE A CZ  
2527 N N   . VAL A 333 ? 1.0868 0.9976 1.8743 -0.1263 0.0018  -0.2623 333 VAL A N   
2528 C CA  . VAL A 333 ? 1.2409 1.1290 1.9998 -0.1171 -0.0080 -0.2525 333 VAL A CA  
2529 C C   . VAL A 333 ? 1.4930 1.3515 2.2139 -0.1340 -0.0047 -0.2556 333 VAL A C   
2530 O O   . VAL A 333 ? 1.8190 1.6823 2.5451 -0.1534 0.0041  -0.2663 333 VAL A O   
2531 C CB  . VAL A 333 ? 1.1507 1.0554 1.9336 -0.1032 -0.0175 -0.2493 333 VAL A CB  
2532 C CG1 . VAL A 333 ? 1.0136 0.9396 1.8237 -0.0863 -0.0226 -0.2434 333 VAL A CG1 
2533 C CG2 . VAL A 333 ? 1.0529 0.9764 1.8635 -0.1140 -0.0148 -0.2607 333 VAL A CG2 
2534 N N   . VAL A 334 ? 1.5251 1.3522 2.2068 -0.1257 -0.0132 -0.2460 334 VAL A N   
2535 C CA  . VAL A 334 ? 1.3912 1.1828 2.0298 -0.1382 -0.0145 -0.2463 334 VAL A CA  
2536 C C   . VAL A 334 ? 1.7729 1.5575 2.4054 -0.1278 -0.0251 -0.2420 334 VAL A C   
2537 O O   . VAL A 334 ? 2.1228 1.9032 2.7492 -0.1074 -0.0348 -0.2333 334 VAL A O   
2538 C CB  . VAL A 334 ? 1.1754 0.9290 1.7668 -0.1389 -0.0172 -0.2407 334 VAL A CB  
2539 C CG1 . VAL A 334 ? 1.3979 1.1097 1.9407 -0.1494 -0.0218 -0.2397 334 VAL A CG1 
2540 C CG2 . VAL A 334 ? 1.1896 0.9428 1.7783 -0.1539 -0.0062 -0.2460 334 VAL A CG2 
2541 N N   . ALA A 335 ? 2.1259 1.9095 2.7594 -0.1425 -0.0230 -0.2486 335 ALA A N   
2542 C CA  . ALA A 335 ? 2.1894 1.9783 2.8325 -0.1336 -0.0318 -0.2470 335 ALA A CA  
2543 C C   . ALA A 335 ? 2.5771 2.3273 3.1753 -0.1406 -0.0381 -0.2450 335 ALA A C   
2544 O O   . ALA A 335 ? 3.0171 2.7653 3.6150 -0.1581 -0.0354 -0.2519 335 ALA A O   
2545 C CB  . ALA A 335 ? 1.7867 1.6119 2.4766 -0.1416 -0.0269 -0.2570 335 ALA A CB  
2546 N N   . GLY A 336 ? 2.6880 2.4076 3.2487 -0.1267 -0.0472 -0.2362 336 GLY A N   
2547 C CA  . GLY A 336 ? 2.8920 2.5688 3.4042 -0.1310 -0.0553 -0.2338 336 GLY A CA  
2548 C C   . GLY A 336 ? 2.9933 2.6475 3.4793 -0.1598 -0.0473 -0.2400 336 GLY A C   
2549 O O   . GLY A 336 ? 2.9869 2.6347 3.4628 -0.1686 -0.0403 -0.2410 336 GLY A O   
2550 N N   . GLU A 337 ? 2.8128 2.4556 3.2882 -0.1756 -0.0482 -0.2442 337 GLU A N   
2551 C CA  . GLU A 337 ? 2.9056 2.5260 3.3536 -0.2058 -0.0402 -0.2503 337 GLU A CA  
2552 C C   . GLU A 337 ? 2.6540 2.3163 3.1475 -0.2255 -0.0246 -0.2620 337 GLU A C   
2553 O O   . GLU A 337 ? 2.9942 2.6479 3.4735 -0.2530 -0.0139 -0.2691 337 GLU A O   
2554 C CB  . GLU A 337 ? 3.2185 2.7993 3.6246 -0.2147 -0.0498 -0.2487 337 GLU A CB  
2555 C CG  . GLU A 337 ? 3.4062 2.9375 3.7578 -0.1995 -0.0646 -0.2393 337 GLU A CG  
2556 C CD  . GLU A 337 ? 3.6175 3.0965 3.9124 -0.2187 -0.0712 -0.2391 337 GLU A CD  
2557 O OE1 . GLU A 337 ? 3.4884 2.9644 3.7830 -0.2260 -0.0751 -0.2413 337 GLU A OE1 
2558 O OE2 . GLU A 337 ? 3.9503 3.3895 4.1995 -0.2270 -0.0732 -0.2365 337 GLU A OE2 
2559 N N   . ARG A 338 ? 2.2999 2.0067 2.8470 -0.2112 -0.0237 -0.2645 338 ARG A N   
2560 C CA  . ARG A 338 ? 2.2815 2.0313 2.8777 -0.2252 -0.0118 -0.2771 338 ARG A CA  
2561 C C   . ARG A 338 ? 2.2058 1.9696 2.8120 -0.2363 0.0026  -0.2829 338 ARG A C   
2562 O O   . ARG A 338 ? 2.1279 1.9219 2.7661 -0.2532 0.0151  -0.2956 338 ARG A O   
2563 C CB  . ARG A 338 ? 1.9389 1.7251 2.5835 -0.2041 -0.0188 -0.2770 338 ARG A CB  
2564 C CG  . ARG A 338 ? 1.5812 1.4133 2.2801 -0.2143 -0.0089 -0.2909 338 ARG A CG  
2565 C CD  . ARG A 338 ? 1.5775 1.4382 2.3177 -0.1926 -0.0185 -0.2896 338 ARG A CD  
2566 N NE  . ARG A 338 ? 1.6732 1.5763 2.4649 -0.2014 -0.0102 -0.3043 338 ARG A NE  
2567 C CZ  . ARG A 338 ? 1.6012 1.5352 2.4374 -0.1878 -0.0170 -0.3080 338 ARG A CZ  
2568 N NH1 . ARG A 338 ? 1.4471 1.3736 2.2807 -0.1677 -0.0315 -0.2979 338 ARG A NH1 
2569 N NH2 . ARG A 338 ? 1.5666 1.5376 2.4483 -0.1945 -0.0098 -0.3224 338 ARG A NH2 
2570 N N   . GLY A 339 ? 2.1555 1.8986 2.7359 -0.2256 0.0005  -0.2743 339 GLY A N   
2571 C CA  . GLY A 339 ? 2.0350 1.7818 2.6142 -0.2353 0.0124  -0.2780 339 GLY A CA  
2572 C C   . GLY A 339 ? 1.8463 1.6289 2.4690 -0.2162 0.0136  -0.2776 339 GLY A C   
2573 O O   . GLY A 339 ? 1.9457 1.7393 2.5859 -0.1920 0.0031  -0.2701 339 GLY A O   
2574 N N   . LEU A 340 ? 1.6858 1.4891 2.3281 -0.2293 0.0275  -0.2871 340 LEU A N   
2575 C CA  . LEU A 340 ? 1.5116 1.3393 2.1835 -0.2153 0.0297  -0.2866 340 LEU A CA  
2576 C C   . LEU A 340 ? 1.4973 1.3731 2.2271 -0.2181 0.0378  -0.3000 340 LEU A C   
2577 O O   . LEU A 340 ? 1.6995 1.5885 2.4395 -0.2400 0.0504  -0.3135 340 LEU A O   
2578 C CB  . LEU A 340 ? 1.4753 1.2796 2.1144 -0.2243 0.0365  -0.2851 340 LEU A CB  
2579 C CG  . LEU A 340 ? 1.5093 1.3331 2.1725 -0.2108 0.0380  -0.2839 340 LEU A CG  
2580 C CD1 . LEU A 340 ? 1.9710 1.7564 2.5874 -0.2094 0.0343  -0.2749 340 LEU A CD1 
2581 C CD2 . LEU A 340 ? 1.5554 1.4087 2.2490 -0.2258 0.0538  -0.2984 340 LEU A CD2 
2582 N N   . LEU A 341 ? 1.4438 1.3442 2.2096 -0.1959 0.0295  -0.2964 341 LEU A N   
2583 C CA  . LEU A 341 ? 1.4154 1.3580 2.2362 -0.1928 0.0310  -0.3075 341 LEU A CA  
2584 C C   . LEU A 341 ? 1.6168 1.5788 2.4646 -0.1767 0.0293  -0.3056 341 LEU A C   
2585 O O   . LEU A 341 ? 1.6775 1.6288 2.5152 -0.1587 0.0199  -0.2924 341 LEU A O   
2586 C CB  . LEU A 341 ? 1.1627 1.1122 1.9988 -0.1821 0.0186  -0.3049 341 LEU A CB  
2587 C CG  . LEU A 341 ? 1.1439 1.0634 1.9424 -0.1906 0.0144  -0.3003 341 LEU A CG  
2588 C CD1 . LEU A 341 ? 1.1957 1.1158 2.0024 -0.1735 -0.0005 -0.2933 341 LEU A CD1 
2589 C CD2 . LEU A 341 ? 1.2180 1.1428 2.0178 -0.2175 0.0258  -0.3143 341 LEU A CD2 
2590 N N   . ALA A 342 ? 1.9753 1.9668 2.8582 -0.1844 0.0390  -0.3201 342 ALA A N   
2591 C CA  . ALA A 342 ? 1.6242 1.6364 2.5369 -0.1718 0.0379  -0.3216 342 ALA A CA  
2592 C C   . ALA A 342 ? 1.5789 1.6143 2.5310 -0.1537 0.0248  -0.3210 342 ALA A C   
2593 O O   . ALA A 342 ? 1.4436 1.4994 2.4242 -0.1574 0.0236  -0.3320 342 ALA A O   
2594 C CB  . ALA A 342 ? 1.5357 1.5687 2.4681 -0.1875 0.0533  -0.3391 342 ALA A CB  
2595 N N   . VAL A 343 ? 1.6299 1.6628 2.5844 -0.1349 0.0148  -0.3089 343 VAL A N   
2596 C CA  . VAL A 343 ? 1.6288 1.6731 2.6072 -0.1173 0.0002  -0.3035 343 VAL A CA  
2597 C C   . VAL A 343 ? 1.6648 1.7309 2.6784 -0.1074 -0.0031 -0.3078 343 VAL A C   
2598 O O   . VAL A 343 ? 2.0112 2.0953 3.0574 -0.0990 -0.0125 -0.3127 343 VAL A O   
2599 C CB  . VAL A 343 ? 1.4131 1.4337 2.3604 -0.1042 -0.0092 -0.2846 343 VAL A CB  
2600 C CG1 . VAL A 343 ? 1.4213 1.4158 2.3294 -0.1125 -0.0071 -0.2803 343 VAL A CG1 
2601 C CG2 . VAL A 343 ? 1.5976 1.6100 2.5317 -0.0970 -0.0086 -0.2752 343 VAL A CG2 
2602 N N   . GLU A 344 ? 1.5218 1.5836 2.5263 -0.1093 0.0038  -0.3066 344 GLU A N   
2603 C CA  . GLU A 344 ? 1.6201 1.6977 2.6517 -0.1008 0.0007  -0.3097 344 GLU A CA  
2604 C C   . GLU A 344 ? 1.2686 1.3532 2.3039 -0.1135 0.0151  -0.3229 344 GLU A C   
2605 O O   . GLU A 344 ? 0.9523 1.0207 1.9570 -0.1264 0.0264  -0.3226 344 GLU A O   
2606 C CB  . GLU A 344 ? 2.3918 2.4596 3.4148 -0.0851 -0.0102 -0.2927 344 GLU A CB  
2607 C CG  . GLU A 344 ? 2.8885 2.9638 3.9307 -0.0714 -0.0253 -0.2874 344 GLU A CG  
2608 C CD  . GLU A 344 ? 3.2919 3.3664 4.3388 -0.0582 -0.0355 -0.2758 344 GLU A CD  
2609 O OE1 . GLU A 344 ? 3.3285 3.4142 4.3976 -0.0559 -0.0371 -0.2819 344 GLU A OE1 
2610 O OE2 . GLU A 344 ? 3.5174 3.5802 4.5454 -0.0505 -0.0420 -0.2610 344 GLU A OE2 
2611 N N   . ILE A 345 ? 1.1163 1.2237 2.1886 -0.1082 0.0130  -0.3341 345 ILE A N   
2612 C CA  . ILE A 345 ? 1.2007 1.3166 2.2812 -0.1146 0.0235  -0.3456 345 ILE A CA  
2613 C C   . ILE A 345 ? 1.4081 1.5270 2.5040 -0.0993 0.0128  -0.3401 345 ILE A C   
2614 O O   . ILE A 345 ? 1.7626 1.8927 2.8856 -0.0864 -0.0009 -0.3400 345 ILE A O   
2615 C CB  . ILE A 345 ? 1.3297 1.4741 2.4448 -0.1237 0.0323  -0.3694 345 ILE A CB  
2616 C CG1 . ILE A 345 ? 1.4658 1.6106 2.5685 -0.1406 0.0512  -0.3810 345 ILE A CG1 
2617 C CG2 . ILE A 345 ? 1.2575 1.4250 2.4174 -0.1085 0.0200  -0.3784 345 ILE A CG2 
2618 C CD1 . ILE A 345 ? 1.5773 1.7015 2.6394 -0.1595 0.0636  -0.3775 345 ILE A CD1 
2619 N N   . ASN A 346 ? 1.3084 1.4153 2.3850 -0.1024 0.0189  -0.3363 346 ASN A N   
2620 C CA  . ASN A 346 ? 1.2684 1.3745 2.3538 -0.0904 0.0099  -0.3301 346 ASN A CA  
2621 C C   . ASN A 346 ? 1.3331 1.4477 2.4290 -0.0963 0.0195  -0.3449 346 ASN A C   
2622 O O   . ASN A 346 ? 1.1580 1.2629 2.2300 -0.1097 0.0334  -0.3486 346 ASN A O   
2623 C CB  . ASN A 346 ? 1.3555 1.4378 2.4071 -0.0860 0.0051  -0.3094 346 ASN A CB  
2624 C CG  . ASN A 346 ? 1.4395 1.5142 2.4803 -0.0789 -0.0040 -0.2954 346 ASN A CG  
2625 O OD1 . ASN A 346 ? 1.5173 1.5995 2.5769 -0.0675 -0.0166 -0.2905 346 ASN A OD1 
2626 N ND2 . ASN A 346 ? 1.4657 1.5232 2.4742 -0.0853 0.0012  -0.2887 346 ASN A ND2 
2627 N N   . LEU A 347 ? 1.3835 1.5160 2.5151 -0.0867 0.0117  -0.3550 347 LEU A N   
2628 C CA  . LEU A 347 ? 1.4717 1.6134 2.6167 -0.0891 0.0185  -0.3699 347 LEU A CA  
2629 C C   . LEU A 347 ? 1.4696 1.5958 2.6042 -0.0794 0.0081  -0.3558 347 LEU A C   
2630 O O   . LEU A 347 ? 1.4998 1.6314 2.6569 -0.0666 -0.0062 -0.3551 347 LEU A O   
2631 C CB  . LEU A 347 ? 1.5882 1.7580 2.7785 -0.0835 0.0148  -0.3908 347 LEU A CB  
2632 C CG  . LEU A 347 ? 1.4632 1.6538 2.6702 -0.0937 0.0253  -0.4077 347 LEU A CG  
2633 C CD1 . LEU A 347 ? 1.3665 1.5868 2.6205 -0.0870 0.0223  -0.4316 347 LEU A CD1 
2634 C CD2 . LEU A 347 ? 1.5994 1.7845 2.7784 -0.1145 0.0471  -0.4127 347 LEU A CD2 
2635 N N   . ARG A 348 ? 1.5366 1.6416 2.6348 -0.0857 0.0138  -0.3433 348 ARG A N   
2636 C CA  . ARG A 348 ? 1.4891 1.5780 2.5726 -0.0784 0.0045  -0.3277 348 ARG A CA  
2637 C C   . ARG A 348 ? 1.3561 1.4225 2.3982 -0.0870 0.0120  -0.3163 348 ARG A C   
2638 O O   . ARG A 348 ? 1.4101 1.4711 2.4340 -0.0974 0.0221  -0.3187 348 ARG A O   
2639 C CB  . ARG A 348 ? 1.2575 1.3461 2.3513 -0.0647 -0.0133 -0.3129 348 ARG A CB  
2640 C CG  . ARG A 348 ? 1.1187 1.2032 2.2004 -0.0636 -0.0160 -0.3014 348 ARG A CG  
2641 C CD  . ARG A 348 ? 1.2386 1.3226 2.3284 -0.0514 -0.0324 -0.2874 348 ARG A CD  
2642 N NE  . ARG A 348 ? 1.2464 1.3264 2.3237 -0.0499 -0.0347 -0.2772 348 ARG A NE  
2643 C CZ  . ARG A 348 ? 1.4999 1.5673 2.5476 -0.0538 -0.0290 -0.2675 348 ARG A CZ  
2644 N NH1 . ARG A 348 ? 1.4270 1.4824 2.4519 -0.0601 -0.0209 -0.2659 348 ARG A NH1 
2645 N NH2 . ARG A 348 ? 2.1367 2.2015 3.1763 -0.0507 -0.0325 -0.2598 348 ARG A NH2 
2646 N N   . LYS A 349 ? 1.1381 1.1904 2.1652 -0.0830 0.0061  -0.3049 349 LYS A N   
2647 C CA  . LYS A 349 ? 1.1859 1.2160 2.1753 -0.0876 0.0085  -0.2924 349 LYS A CA  
2648 C C   . LYS A 349 ? 1.3697 1.3971 2.3519 -0.0810 0.0008  -0.2781 349 LYS A C   
2649 O O   . LYS A 349 ? 1.3497 1.3906 2.3548 -0.0727 -0.0073 -0.2759 349 LYS A O   
2650 C CB  . LYS A 349 ? 0.9917 1.0110 1.9726 -0.0839 0.0024  -0.2852 349 LYS A CB  
2651 C CG  . LYS A 349 ? 1.0713 1.0929 2.0598 -0.0890 0.0089  -0.2997 349 LYS A CG  
2652 C CD  . LYS A 349 ? 1.1744 1.1844 2.1552 -0.0848 0.0008  -0.2918 349 LYS A CD  
2653 C CE  . LYS A 349 ? 1.2097 1.2214 2.1991 -0.0880 0.0054  -0.3063 349 LYS A CE  
2654 N NZ  . LYS A 349 ? 1.4226 1.4322 2.3991 -0.1015 0.0230  -0.3222 349 LYS A NZ  
2655 N N   . VAL A 350 ? 1.3670 1.3754 2.3160 -0.0844 0.0029  -0.2690 350 VAL A N   
2656 C CA  . VAL A 350 ? 1.2971 1.3041 2.2405 -0.0766 -0.0046 -0.2565 350 VAL A CA  
2657 C C   . VAL A 350 ? 1.4309 1.4217 2.3490 -0.0719 -0.0104 -0.2428 350 VAL A C   
2658 O O   . VAL A 350 ? 1.5511 1.5299 2.4547 -0.0762 -0.0084 -0.2437 350 VAL A O   
2659 C CB  . VAL A 350 ? 1.3152 1.3186 2.2473 -0.0827 0.0014  -0.2602 350 VAL A CB  
2660 C CG1 . VAL A 350 ? 1.2596 1.2739 2.2066 -0.0724 -0.0076 -0.2529 350 VAL A CG1 
2661 C CG2 . VAL A 350 ? 1.2678 1.2793 2.2099 -0.0954 0.0136  -0.2780 350 VAL A CG2 
2662 N N   . GLY A 351 ? 1.4419 1.4336 2.3563 -0.0629 -0.0180 -0.2311 351 GLY A N   
2663 C CA  . GLY A 351 ? 1.5577 1.5391 2.4535 -0.0565 -0.0247 -0.2191 351 GLY A CA  
2664 C C   . GLY A 351 ? 1.4102 1.3675 2.2733 -0.0640 -0.0202 -0.2215 351 GLY A C   
2665 O O   . GLY A 351 ? 1.4285 1.3790 2.2855 -0.0643 -0.0227 -0.2197 351 GLY A O   
2666 N N   . PRO A 352 ? 1.2046 1.1457 2.0434 -0.0713 -0.0141 -0.2257 352 PRO A N   
2667 C CA  . PRO A 352 ? 1.2327 1.1455 2.0344 -0.0796 -0.0110 -0.2274 352 PRO A CA  
2668 C C   . PRO A 352 ? 1.3272 1.2344 2.1266 -0.0878 -0.0063 -0.2338 352 PRO A C   
2669 O O   . PRO A 352 ? 1.2777 1.1612 2.0473 -0.0904 -0.0087 -0.2312 352 PRO A O   
2670 C CB  . PRO A 352 ? 1.1199 1.0232 1.9067 -0.0900 -0.0026 -0.2344 352 PRO A CB  
2671 C CG  . PRO A 352 ? 1.2918 1.2230 2.1150 -0.0877 -0.0005 -0.2388 352 PRO A CG  
2672 C CD  . PRO A 352 ? 1.0875 1.0335 1.9293 -0.0716 -0.0119 -0.2275 352 PRO A CD  
2673 N N   . SER A 353 ? 1.5014 1.4280 2.3295 -0.0913 -0.0007 -0.2425 353 SER A N   
2674 C CA  . SER A 353 ? 1.6947 1.6152 2.5185 -0.1011 0.0064  -0.2520 353 SER A CA  
2675 C C   . SER A 353 ? 1.4635 1.3724 2.2765 -0.0956 -0.0025 -0.2439 353 SER A C   
2676 O O   . SER A 353 ? 1.5438 1.4287 2.3269 -0.1031 -0.0005 -0.2456 353 SER A O   
2677 C CB  . SER A 353 ? 1.8353 1.7821 2.6978 -0.1006 0.0101  -0.2619 353 SER A CB  
2678 O OG  . SER A 353 ? 1.8016 1.7638 2.6897 -0.0870 -0.0019 -0.2529 353 SER A OG  
2679 N N   . HIS A 354 ? 1.2372 1.1637 2.0755 -0.0828 -0.0130 -0.2351 354 HIS A N   
2680 C CA  . HIS A 354 ? 1.4300 1.3520 2.2662 -0.0769 -0.0228 -0.2272 354 HIS A CA  
2681 C C   . HIS A 354 ? 1.3367 1.2353 2.1387 -0.0749 -0.0287 -0.2197 354 HIS A C   
2682 O O   . HIS A 354 ? 1.0685 0.9496 1.8519 -0.0773 -0.0323 -0.2189 354 HIS A O   
2683 C CB  . HIS A 354 ? 1.5274 1.4735 2.3974 -0.0666 -0.0319 -0.2201 354 HIS A CB  
2684 C CG  . HIS A 354 ? 1.2309 1.1832 2.1015 -0.0561 -0.0414 -0.2071 354 HIS A CG  
2685 N ND1 . HIS A 354 ? 1.2288 1.1919 2.1069 -0.0513 -0.0411 -0.2041 354 HIS A ND1 
2686 C CD2 . HIS A 354 ? 0.9455 0.8966 1.8116 -0.0499 -0.0507 -0.1978 354 HIS A CD2 
2687 C CE1 . HIS A 354 ? 0.9849 0.9536 1.8623 -0.0422 -0.0491 -0.1936 354 HIS A CE1 
2688 N NE2 . HIS A 354 ? 0.9857 0.9488 1.8574 -0.0413 -0.0549 -0.1900 354 HIS A NE2 
2689 N N   . VAL A 355 ? 1.2001 1.0976 1.9940 -0.0702 -0.0304 -0.2151 355 VAL A N   
2690 C CA  . VAL A 355 ? 1.1305 1.0058 1.8930 -0.0659 -0.0378 -0.2089 355 VAL A CA  
2691 C C   . VAL A 355 ? 1.0441 0.8853 1.7670 -0.0783 -0.0332 -0.2151 355 VAL A C   
2692 O O   . VAL A 355 ? 0.9189 0.7379 1.6167 -0.0769 -0.0412 -0.2118 355 VAL A O   
2693 C CB  . VAL A 355 ? 1.2171 1.0974 1.9787 -0.0586 -0.0396 -0.2048 355 VAL A CB  
2694 C CG1 . VAL A 355 ? 1.4855 1.3406 2.2129 -0.0533 -0.0479 -0.2004 355 VAL A CG1 
2695 C CG2 . VAL A 355 ? 1.2579 1.1696 2.0546 -0.0471 -0.0445 -0.1980 355 VAL A CG2 
2696 N N   . VAL A 356 ? 1.1377 0.9752 1.8552 -0.0915 -0.0202 -0.2247 356 VAL A N   
2697 C CA  . VAL A 356 ? 1.2259 1.0328 1.9056 -0.1074 -0.0122 -0.2321 356 VAL A CA  
2698 C C   . VAL A 356 ? 1.2505 1.0467 1.9222 -0.1116 -0.0131 -0.2345 356 VAL A C   
2699 O O   . VAL A 356 ? 1.0836 0.8459 1.7148 -0.1179 -0.0160 -0.2339 356 VAL A O   
2700 C CB  . VAL A 356 ? 1.0886 0.9030 1.7736 -0.1220 0.0039  -0.2439 356 VAL A CB  
2701 C CG1 . VAL A 356 ? 1.1366 0.9247 1.7876 -0.1409 0.0147  -0.2533 356 VAL A CG1 
2702 C CG2 . VAL A 356 ? 1.0466 0.8625 1.7288 -0.1213 0.0049  -0.2424 356 VAL A CG2 
2703 N N   . ARG A 357 ? 1.4977 1.3194 2.2046 -0.1083 -0.0118 -0.2370 357 ARG A N   
2704 C CA  . ARG A 357 ? 1.7224 1.5349 2.4236 -0.1118 -0.0130 -0.2396 357 ARG A CA  
2705 C C   . ARG A 357 ? 1.8104 1.6020 2.4894 -0.1041 -0.0283 -0.2295 357 ARG A C   
2706 O O   . ARG A 357 ? 2.2568 2.0183 2.9017 -0.1113 -0.0300 -0.2313 357 ARG A O   
2707 C CB  . ARG A 357 ? 1.6019 1.4438 2.3450 -0.1062 -0.0135 -0.2419 357 ARG A CB  
2708 C CG  . ARG A 357 ? 1.9397 1.7970 2.7002 -0.1155 0.0015  -0.2559 357 ARG A CG  
2709 C CD  . ARG A 357 ? 1.7875 1.6603 2.5745 -0.1146 0.0030  -0.2632 357 ARG A CD  
2710 N NE  . ARG A 357 ? 1.8103 1.6653 2.5754 -0.1268 0.0119  -0.2739 357 ARG A NE  
2711 C CZ  . ARG A 357 ? 2.0252 1.8644 2.7768 -0.1265 0.0055  -0.2717 357 ARG A CZ  
2712 N NH1 . ARG A 357 ? 2.0599 1.8939 2.8102 -0.1163 -0.0100 -0.2582 357 ARG A NH1 
2713 N NH2 . ARG A 357 ? 2.1482 1.9759 2.8853 -0.1372 0.0151  -0.2835 357 ARG A NH2 
2714 N N   . TYR A 358 ? 1.6686 1.4783 2.3686 -0.0892 -0.0394 -0.2196 358 TYR A N   
2715 C CA  . TYR A 358 ? 1.5627 1.3620 2.2517 -0.0789 -0.0551 -0.2105 358 TYR A CA  
2716 C C   . TYR A 358 ? 1.4956 1.2565 2.1373 -0.0823 -0.0594 -0.2103 358 TYR A C   
2717 O O   . TYR A 358 ? 1.2987 1.0347 1.9152 -0.0820 -0.0691 -0.2085 358 TYR A O   
2718 C CB  . TYR A 358 ? 1.3763 1.2000 2.0909 -0.0629 -0.0662 -0.2006 358 TYR A CB  
2719 C CG  . TYR A 358 ? 1.1552 1.0111 1.9103 -0.0564 -0.0702 -0.1960 358 TYR A CG  
2720 C CD1 . TYR A 358 ? 1.2529 1.1367 2.0402 -0.0551 -0.0640 -0.1963 358 TYR A CD1 
2721 C CD2 . TYR A 358 ? 1.1208 0.9783 1.8810 -0.0514 -0.0817 -0.1909 358 TYR A CD2 
2722 C CE1 . TYR A 358 ? 1.4967 1.4060 2.3168 -0.0502 -0.0689 -0.1913 358 TYR A CE1 
2723 C CE2 . TYR A 358 ? 1.2273 1.1126 2.0223 -0.0473 -0.0858 -0.1860 358 TYR A CE2 
2724 C CZ  . TYR A 358 ? 1.3650 1.2752 2.1888 -0.0470 -0.0794 -0.1859 358 TYR A CZ  
2725 O OH  . TYR A 358 ? 1.1256 1.0596 1.9801 -0.0442 -0.0841 -0.1806 358 TYR A OH  
2726 N N   . ALA A 359 ? 1.4165 1.1711 2.0455 -0.0855 -0.0534 -0.2121 359 ALA A N   
2727 C CA  . ALA A 359 ? 1.4164 1.1321 1.9983 -0.0893 -0.0578 -0.2119 359 ALA A CA  
2728 C C   . ALA A 359 ? 1.3961 1.0758 1.9384 -0.1057 -0.0531 -0.2180 359 ALA A C   
2729 O O   . ALA A 359 ? 1.5581 1.2018 2.0618 -0.1055 -0.0645 -0.2155 359 ALA A O   
2730 C CB  . ALA A 359 ? 1.4422 1.1597 2.0204 -0.0933 -0.0494 -0.2142 359 ALA A CB  
2731 N N   . GLU A 360 ? 1.2685 0.9588 1.8213 -0.1196 -0.0366 -0.2267 360 GLU A N   
2732 C CA  . GLU A 360 ? 1.4544 1.1156 1.9727 -0.1376 -0.0278 -0.2346 360 GLU A CA  
2733 C C   . GLU A 360 ? 1.5858 1.2314 2.0930 -0.1332 -0.0399 -0.2313 360 GLU A C   
2734 O O   . GLU A 360 ? 1.7182 1.3220 2.1782 -0.1418 -0.0443 -0.2319 360 GLU A O   
2735 C CB  . GLU A 360 ? 1.5664 1.2526 2.1097 -0.1497 -0.0082 -0.2461 360 GLU A CB  
2736 C CG  . GLU A 360 ? 1.9094 1.5929 2.4408 -0.1645 0.0070  -0.2537 360 GLU A CG  
2737 C CD  . GLU A 360 ? 2.3342 2.0411 2.8881 -0.1777 0.0266  -0.2678 360 GLU A CD  
2738 O OE1 . GLU A 360 ? 2.6853 2.4158 3.2719 -0.1713 0.0269  -0.2709 360 GLU A OE1 
2739 O OE2 . GLU A 360 ? 2.5377 2.2396 3.0769 -0.1944 0.0413  -0.2766 360 GLU A OE2 
2740 N N   . ALA A 361 ? 1.7269 1.4047 2.2766 -0.1206 -0.0457 -0.2276 361 ALA A N   
2741 C CA  . ALA A 361 ? 2.1196 1.7893 2.6672 -0.1155 -0.0578 -0.2242 361 ALA A CA  
2742 C C   . ALA A 361 ? 1.9379 1.5777 2.4538 -0.1071 -0.0766 -0.2167 361 ALA A C   
2743 O O   . ALA A 361 ? 2.0506 1.6569 2.5326 -0.1116 -0.0846 -0.2170 361 ALA A O   
2744 C CB  . ALA A 361 ? 2.6548 2.3658 3.2545 -0.1038 -0.0614 -0.2205 361 ALA A CB  
2745 N N   . LEU A 362 ? 1.5530 1.2049 2.0802 -0.0945 -0.0839 -0.2108 362 LEU A N   
2746 C CA  . LEU A 362 ? 1.5124 1.1417 2.0161 -0.0829 -0.1029 -0.2048 362 LEU A CA  
2747 C C   . LEU A 362 ? 1.6897 1.2646 2.1320 -0.0949 -0.1051 -0.2080 362 LEU A C   
2748 O O   . LEU A 362 ? 1.9065 1.4488 2.3178 -0.0918 -0.1210 -0.2059 362 LEU A O   
2749 C CB  . LEU A 362 ? 1.4711 1.1268 2.0003 -0.0677 -0.1074 -0.1999 362 LEU A CB  
2750 C CG  . LEU A 362 ? 1.5260 1.2301 2.1096 -0.0551 -0.1099 -0.1951 362 LEU A CG  
2751 C CD1 . LEU A 362 ? 1.6202 1.3536 2.2302 -0.0427 -0.1102 -0.1913 362 LEU A CD1 
2752 C CD2 . LEU A 362 ? 1.7243 1.4262 2.3108 -0.0458 -0.1271 -0.1913 362 LEU A CD2 
2753 N N   . VAL A 363 ? 1.7825 1.3474 2.2072 -0.1095 -0.0893 -0.2132 363 VAL A N   
2754 C CA  . VAL A 363 ? 1.8129 1.3256 2.1768 -0.1242 -0.0892 -0.2160 363 VAL A CA  
2755 C C   . VAL A 363 ? 1.8408 1.3245 2.1745 -0.1377 -0.0876 -0.2200 363 VAL A C   
2756 O O   . VAL A 363 ? 2.0156 1.4512 2.2990 -0.1414 -0.1003 -0.2186 363 VAL A O   
2757 C CB  . VAL A 363 ? 1.9298 1.4409 2.2833 -0.1387 -0.0718 -0.2209 363 VAL A CB  
2758 C CG1 . VAL A 363 ? 2.2854 1.7383 2.5712 -0.1549 -0.0736 -0.2227 363 VAL A CG1 
2759 C CG2 . VAL A 363 ? 1.8474 1.3879 2.2323 -0.1240 -0.0744 -0.2167 363 VAL A CG2 
2760 N N   . GLY A 364 ? 1.6631 1.1747 2.0259 -0.1457 -0.0716 -0.2259 364 GLY A N   
2761 C CA  . GLY A 364 ? 1.9142 1.4037 2.2520 -0.1607 -0.0650 -0.2320 364 GLY A CA  
2762 C C   . GLY A 364 ? 2.1192 1.6036 2.4402 -0.1838 -0.0408 -0.2427 364 GLY A C   
2763 O O   . GLY A 364 ? 2.2429 1.7163 2.5485 -0.1978 -0.0304 -0.2503 364 GLY A O   
2764 N N   . ALA A 365 ? 2.1064 1.6009 2.4322 -0.1875 -0.0318 -0.2438 365 ALA A N   
2765 C CA  . ALA A 365 ? 2.2350 1.7263 2.5454 -0.2103 -0.0090 -0.2543 365 ALA A CA  
2766 C C   . ALA A 365 ? 2.1561 1.6979 2.5197 -0.2068 0.0042  -0.2586 365 ALA A C   
2767 O O   . ALA A 365 ? 1.9524 1.5231 2.3544 -0.1878 -0.0052 -0.2516 365 ALA A O   
2768 C CB  . ALA A 365 ? 2.4316 1.8718 2.6792 -0.2248 -0.0112 -0.2529 365 ALA A CB  
2769 N N   . ARG A 366 ? 2.2172 1.7686 2.5813 -0.2261 0.0264  -0.2708 366 ARG A N   
2770 C CA  . ARG A 366 ? 2.1398 1.7356 2.5498 -0.2264 0.0405  -0.2777 366 ARG A CA  
2771 C C   . ARG A 366 ? 2.0703 1.6541 2.4626 -0.2297 0.0391  -0.2734 366 ARG A C   
2772 O O   . ARG A 366 ? 2.0319 1.5710 2.3737 -0.2337 0.0288  -0.2668 366 ARG A O   
2773 C CB  . ARG A 366 ? 2.3321 1.9370 2.7414 -0.2479 0.0642  -0.2941 366 ARG A CB  
2774 C CG  . ARG A 366 ? 2.3827 1.9652 2.7659 -0.2561 0.0664  -0.2988 366 ARG A CG  
2775 C CD  . ARG A 366 ? 2.3205 1.9289 2.7235 -0.2703 0.0893  -0.3165 366 ARG A CD  
2776 N NE  . ARG A 366 ? 2.3307 1.9918 2.8015 -0.2527 0.0889  -0.3193 366 ARG A NE  
2777 C CZ  . ARG A 366 ? 2.3773 2.0639 2.8819 -0.2462 0.0923  -0.3273 366 ARG A CZ  
2778 N NH1 . ARG A 366 ? 2.4174 2.0854 2.8965 -0.2572 0.0994  -0.3354 366 ARG A NH1 
2779 N NH2 . ARG A 366 ? 2.4713 2.1995 3.0325 -0.2292 0.0879  -0.3275 366 ARG A NH2 
2780 N N   . VAL A 367 ? 2.2072 1.8282 2.6385 -0.2290 0.0491  -0.2783 367 VAL A N   
2781 C CA  . VAL A 367 ? 2.4811 2.0991 2.9072 -0.2278 0.0461  -0.2736 367 VAL A CA  
2782 C C   . VAL A 367 ? 2.8897 2.4563 3.2505 -0.2470 0.0470  -0.2728 367 VAL A C   
2783 O O   . VAL A 367 ? 3.4424 2.9875 3.7822 -0.2396 0.0337  -0.2638 367 VAL A O   
2784 C CB  . VAL A 367 ? 2.4000 2.0639 2.8757 -0.2265 0.0573  -0.2803 367 VAL A CB  
2785 C CG1 . VAL A 367 ? 2.3897 2.0438 2.8437 -0.2474 0.0705  -0.2872 367 VAL A CG1 
2786 C CG2 . VAL A 367 ? 1.9084 1.5979 2.4221 -0.2016 0.0427  -0.2701 367 VAL A CG2 
2787 N N   . GLY A 368 ? 2.7181 2.2644 3.0459 -0.2716 0.0623  -0.2825 368 GLY A N   
2788 C CA  . GLY A 368 ? 2.7539 2.2463 3.0136 -0.2929 0.0633  -0.2816 368 GLY A CA  
2789 C C   . GLY A 368 ? 2.9082 2.4073 3.1617 -0.3176 0.0838  -0.2918 368 GLY A C   
2790 O O   . GLY A 368 ? 2.8007 2.3417 3.1008 -0.3125 0.0905  -0.2957 368 GLY A O   
2791 N N   . ALA A 369 ? 3.0538 2.5091 3.2469 -0.3452 0.0927  -0.2957 369 ALA A N   
2792 C CA  . ALA A 369 ? 2.9226 2.3792 3.1012 -0.3742 0.1139  -0.3064 369 ALA A CA  
2793 C C   . ALA A 369 ? 3.2472 2.7697 3.4970 -0.3696 0.1285  -0.3170 369 ALA A C   
2794 O O   . ALA A 369 ? 3.9551 3.5169 4.2486 -0.3639 0.1381  -0.3263 369 ALA A O   
2795 C CB  . ALA A 369 ? 2.3992 1.8099 2.5262 -0.3837 0.1042  -0.2979 369 ALA A CB  
2796 N N   . ASP A 370 ? 3.1371 2.6702 3.3986 -0.3703 0.1280  -0.3155 370 ASP A N   
2797 C CA  . ASP A 370 ? 3.2342 2.8283 3.5653 -0.3609 0.1365  -0.3238 370 ASP A CA  
2798 C C   . ASP A 370 ? 3.2864 2.8919 3.6458 -0.3312 0.1155  -0.3106 370 ASP A C   
2799 O O   . ASP A 370 ? 3.6487 3.3019 4.0679 -0.3147 0.1155  -0.3134 370 ASP A O   
2800 C CB  . ASP A 370 ? 3.2474 2.8573 3.5811 -0.3879 0.1576  -0.3373 370 ASP A CB  
2801 C CG  . ASP A 370 ? 3.2087 2.8845 3.6151 -0.3829 0.1709  -0.3518 370 ASP A CG  
2802 O OD1 . ASP A 370 ? 2.8202 2.5241 3.2575 -0.3786 0.1794  -0.3617 370 ASP A OD1 
2803 O OD2 . ASP A 370 ? 3.4195 3.1163 3.8501 -0.3828 0.1716  -0.3535 370 ASP A OD2 
2804 N N   . GLY A 371 ? 2.9683 2.5275 3.2819 -0.3247 0.0971  -0.2967 371 GLY A N   
2805 C CA  . GLY A 371 ? 2.7242 2.2888 3.0568 -0.2968 0.0767  -0.2841 371 GLY A CA  
2806 C C   . GLY A 371 ? 2.6906 2.2045 2.9738 -0.2861 0.0553  -0.2711 371 GLY A C   
2807 O O   . GLY A 371 ? 2.6445 2.1085 2.8672 -0.3045 0.0548  -0.2704 371 GLY A O   
2808 N N   . MET A 372 ? 2.5949 2.1233 2.9057 -0.2569 0.0379  -0.2617 372 MET A N   
2809 C CA  . MET A 372 ? 2.7083 2.1984 2.9847 -0.2409 0.0151  -0.2501 372 MET A CA  
2810 C C   . MET A 372 ? 2.9633 2.4331 3.2197 -0.2405 0.0102  -0.2491 372 MET A C   
2811 O O   . MET A 372 ? 3.4963 2.9302 3.7067 -0.2622 0.0169  -0.2532 372 MET A O   
2812 C CB  . MET A 372 ? 2.5968 2.0346 2.8136 -0.2513 0.0067  -0.2461 372 MET A CB  
2813 C CG  . MET A 372 ? 2.4669 1.8777 2.6641 -0.2271 -0.0191 -0.2351 372 MET A CG  
2814 S SD  . MET A 372 ? 2.9335 2.2612 3.0405 -0.2398 -0.0348 -0.2307 372 MET A SD  
2815 C CE  . MET A 372 ? 2.5498 1.8484 2.6265 -0.2449 -0.0391 -0.2309 372 MET A CE  
2816 N N   . LEU A 373 ? 2.6906 2.1830 2.9809 -0.2161 -0.0021 -0.2434 373 LEU A N   
2817 C CA  . LEU A 373 ? 2.5129 1.9935 2.7950 -0.2103 -0.0101 -0.2413 373 LEU A CA  
2818 C C   . LEU A 373 ? 2.3735 1.7945 2.5936 -0.2096 -0.0289 -0.2348 373 LEU A C   
2819 O O   . LEU A 373 ? 2.5008 1.9021 2.7020 -0.2012 -0.0417 -0.2293 373 LEU A O   
2820 C CB  . LEU A 373 ? 2.7513 2.2750 3.0893 -0.1829 -0.0202 -0.2357 373 LEU A CB  
2821 C CG  . LEU A 373 ? 2.8035 2.3336 3.1547 -0.1736 -0.0273 -0.2338 373 LEU A CG  
2822 C CD1 . LEU A 373 ? 3.1928 2.7266 3.5430 -0.1932 -0.0093 -0.2437 373 LEU A CD1 
2823 C CD2 . LEU A 373 ? 2.3328 1.9123 2.7445 -0.1509 -0.0330 -0.2293 373 LEU A CD2 
2824 N N   . ARG A 374 ? 2.2905 1.6824 2.4791 -0.2179 -0.0313 -0.2359 374 ARG A N   
2825 C CA  . ARG A 374 ? 2.7315 2.0632 2.8589 -0.2171 -0.0513 -0.2302 374 ARG A CA  
2826 C C   . ARG A 374 ? 2.7538 2.0782 2.8795 -0.2101 -0.0606 -0.2289 374 ARG A C   
2827 O O   . ARG A 374 ? 2.4711 1.8153 2.6143 -0.2204 -0.0455 -0.2350 374 ARG A O   
2828 C CB  . ARG A 374 ? 3.1815 2.4598 3.2416 -0.2468 -0.0433 -0.2339 374 ARG A CB  
2829 C CG  . ARG A 374 ? 3.4573 2.7537 3.5256 -0.2670 -0.0209 -0.2407 374 ARG A CG  
2830 C CD  . ARG A 374 ? 3.1055 2.3492 3.1057 -0.2984 -0.0128 -0.2439 374 ARG A CD  
2831 N NE  . ARG A 374 ? 2.7859 2.0626 2.8082 -0.3216 0.0157  -0.2546 374 ARG A NE  
2832 C CZ  . ARG A 374 ? 2.6694 1.9555 2.6960 -0.3321 0.0248  -0.2571 374 ARG A CZ  
2833 N NH1 . ARG A 374 ? 2.9967 2.2550 2.9994 -0.3234 0.0079  -0.2492 374 ARG A NH1 
2834 N NH2 . ARG A 374 ? 2.3997 1.7231 2.4552 -0.3508 0.0502  -0.2683 374 ARG A NH2 
2835 N N   . GLY A 375 ? 2.8333 2.1279 2.9364 -0.1928 -0.0863 -0.2218 375 GLY A N   
2836 C CA  . GLY A 375 ? 2.6626 1.9481 2.7634 -0.1837 -0.0994 -0.2198 375 GLY A CA  
2837 C C   . GLY A 375 ? 2.7485 1.9813 2.7881 -0.2071 -0.0964 -0.2233 375 GLY A C   
2838 O O   . GLY A 375 ? 2.7623 1.9668 2.7610 -0.2319 -0.0825 -0.2275 375 GLY A O   
2839 N N   . ALA A 376 ? 2.7864 2.0061 2.8192 -0.1995 -0.1099 -0.2215 376 ALA A N   
2840 C CA  . ALA A 376 ? 2.8388 2.0075 2.8138 -0.2188 -0.1102 -0.2241 376 ALA A CA  
2841 C C   . ALA A 376 ? 2.9185 2.0185 2.8161 -0.2348 -0.1181 -0.2226 376 ALA A C   
2842 O O   . ALA A 376 ? 2.9296 1.9961 2.7798 -0.2631 -0.1032 -0.2275 376 ALA A O   
2843 C CB  . ALA A 376 ? 2.6769 1.8386 2.6566 -0.2016 -0.1317 -0.2203 376 ALA A CB  
2844 N N   . ASP A 377 ? 3.1290 2.2088 3.0143 -0.2164 -0.1417 -0.2164 377 ASP A N   
2845 C CA  . ASP A 377 ? 3.2474 2.2574 3.0586 -0.2259 -0.1565 -0.2138 377 ASP A CA  
2846 C C   . ASP A 377 ? 3.1128 2.1203 2.9090 -0.2470 -0.1367 -0.2165 377 ASP A C   
2847 O O   . ASP A 377 ? 3.2197 2.1665 2.9481 -0.2633 -0.1431 -0.2152 377 ASP A O   
2848 C CB  . ASP A 377 ? 3.3331 2.3282 3.1433 -0.1962 -0.1888 -0.2079 377 ASP A CB  
2849 C CG  . ASP A 377 ? 3.2781 2.3355 3.1582 -0.1711 -0.1887 -0.2064 377 ASP A CG  
2850 O OD1 . ASP A 377 ? 3.1661 2.2761 3.0938 -0.1775 -0.1638 -0.2092 377 ASP A OD1 
2851 O OD2 . ASP A 377 ? 3.4078 2.4606 3.2941 -0.1451 -0.2139 -0.2032 377 ASP A OD2 
2852 N N   . GLY A 378 ? 3.0699 2.1419 2.9286 -0.2464 -0.1143 -0.2201 378 GLY A N   
2853 C CA  . GLY A 378 ? 3.0715 2.1508 2.9261 -0.2663 -0.0936 -0.2239 378 GLY A CA  
2854 C C   . GLY A 378 ? 2.9068 2.0098 2.7925 -0.2464 -0.1021 -0.2199 378 GLY A C   
2855 O O   . GLY A 378 ? 2.7365 1.8663 2.6428 -0.2566 -0.0842 -0.2232 378 GLY A O   
2856 N N   . ARG A 379 ? 2.7924 1.8851 2.6805 -0.2181 -0.1298 -0.2137 379 ARG A N   
2857 C CA  . ARG A 379 ? 2.7954 1.9067 2.7096 -0.1948 -0.1422 -0.2100 379 ARG A CA  
2858 C C   . ARG A 379 ? 2.4865 1.6749 2.4803 -0.1843 -0.1249 -0.2118 379 ARG A C   
2859 O O   . ARG A 379 ? 2.1772 1.4091 2.2188 -0.1767 -0.1182 -0.2130 379 ARG A O   
2860 C CB  . ARG A 379 ? 2.8334 1.9222 2.7376 -0.1662 -0.1747 -0.2053 379 ARG A CB  
2861 C CG  . ARG A 379 ? 3.0552 2.0623 2.8781 -0.1713 -0.1981 -0.2031 379 ARG A CG  
2862 C CD  . ARG A 379 ? 3.3114 2.2856 3.0978 -0.1768 -0.2024 -0.2020 379 ARG A CD  
2863 N NE  . ARG A 379 ? 3.3833 2.4098 3.2267 -0.1548 -0.2010 -0.2015 379 ARG A NE  
2864 C CZ  . ARG A 379 ? 3.5586 2.6140 3.4417 -0.1218 -0.2185 -0.2002 379 ARG A CZ  
2865 N NH1 . ARG A 379 ? 3.6621 2.6963 3.5329 -0.1044 -0.2425 -0.1993 379 ARG A NH1 
2866 N NH2 . ARG A 379 ? 3.8159 2.9216 3.7505 -0.1068 -0.2119 -0.2002 379 ARG A NH2 
2867 N N   . PRO A 380 ? 2.4786 1.6813 2.4844 -0.1836 -0.1192 -0.2118 380 PRO A N   
2868 C CA  . PRO A 380 ? 2.4071 1.6766 2.4819 -0.1746 -0.1043 -0.2133 380 PRO A CA  
2869 C C   . PRO A 380 ? 2.3658 1.6821 2.4982 -0.1445 -0.1146 -0.2099 380 PRO A C   
2870 O O   . PRO A 380 ? 2.4395 1.7392 2.5621 -0.1247 -0.1371 -0.2061 380 PRO A O   
2871 C CB  . PRO A 380 ? 2.3821 1.6402 2.4425 -0.1760 -0.1054 -0.2124 380 PRO A CB  
2872 C CG  . PRO A 380 ? 2.4791 1.6672 2.4614 -0.1995 -0.1094 -0.2128 380 PRO A CG  
2873 C CD  . PRO A 380 ? 2.5628 1.7134 2.5127 -0.1912 -0.1290 -0.2100 380 PRO A CD  
2874 N N   . VAL A 381 ? 2.1907 1.5660 2.3834 -0.1424 -0.0978 -0.2119 381 VAL A N   
2875 C CA  . VAL A 381 ? 1.9608 1.3862 2.2120 -0.1187 -0.1029 -0.2090 381 VAL A CA  
2876 C C   . VAL A 381 ? 1.8606 1.3314 2.1577 -0.1107 -0.0937 -0.2087 381 VAL A C   
2877 O O   . VAL A 381 ? 1.6623 1.1493 1.9715 -0.1261 -0.0755 -0.2130 381 VAL A O   
2878 C CB  . VAL A 381 ? 1.9851 1.4357 2.2646 -0.1226 -0.0944 -0.2110 381 VAL A CB  
2879 C CG1 . VAL A 381 ? 2.0636 1.5601 2.3976 -0.0987 -0.1026 -0.2069 381 VAL A CG1 
2880 C CG2 . VAL A 381 ? 1.8887 1.2916 2.1188 -0.1341 -0.1012 -0.2120 381 VAL A CG2 
2881 N N   . TYR A 382 ? 1.7367 1.2279 2.0591 -0.0857 -0.1076 -0.2042 382 TYR A N   
2882 C CA  . TYR A 382 ? 1.8145 1.3453 2.1768 -0.0740 -0.1033 -0.2029 382 TYR A CA  
2883 C C   . TYR A 382 ? 1.7192 1.2975 2.1343 -0.0541 -0.1075 -0.1995 382 TYR A C   
2884 O O   . TYR A 382 ? 1.6467 1.2205 2.0604 -0.0393 -0.1232 -0.1970 382 TYR A O   
2885 C CB  . TYR A 382 ? 1.7427 1.2503 2.0796 -0.0625 -0.1163 -0.2010 382 TYR A CB  
2886 C CG  . TYR A 382 ? 1.8959 1.3491 2.1733 -0.0808 -0.1167 -0.2032 382 TYR A CG  
2887 C CD1 . TYR A 382 ? 2.0602 1.5162 2.3356 -0.0988 -0.1007 -0.2061 382 TYR A CD1 
2888 C CD2 . TYR A 382 ? 2.0032 1.4011 2.2257 -0.0811 -0.1337 -0.2024 382 TYR A CD2 
2889 C CE1 . TYR A 382 ? 2.3060 1.7124 2.5261 -0.1183 -0.1002 -0.2080 382 TYR A CE1 
2890 C CE2 . TYR A 382 ? 2.2366 1.5811 2.4005 -0.1002 -0.1343 -0.2037 382 TYR A CE2 
2891 C CZ  . TYR A 382 ? 2.4524 1.8018 2.6151 -0.1196 -0.1168 -0.2064 382 TYR A CZ  
2892 O OH  . TYR A 382 ? 2.8982 2.1952 3.0024 -0.1406 -0.1168 -0.2076 382 TYR A OH  
2893 N N   . TYR A 383 ? 1.7235 1.3468 2.1846 -0.0543 -0.0941 -0.1998 383 TYR A N   
2894 C CA  . TYR A 383 ? 1.4940 1.1635 2.0054 -0.0393 -0.0954 -0.1963 383 TYR A CA  
2895 C C   . TYR A 383 ? 1.4254 1.1275 1.9675 -0.0299 -0.0913 -0.1946 383 TYR A C   
2896 O O   . TYR A 383 ? 1.4875 1.1912 2.0294 -0.0392 -0.0810 -0.1970 383 TYR A O   
2897 C CB  . TYR A 383 ? 1.6800 1.3694 2.2163 -0.0478 -0.0870 -0.1976 383 TYR A CB  
2898 C CG  . TYR A 383 ? 1.8415 1.5518 2.4003 -0.0631 -0.0684 -0.2023 383 TYR A CG  
2899 C CD1 . TYR A 383 ? 1.9246 1.6771 2.5289 -0.0571 -0.0623 -0.2010 383 TYR A CD1 
2900 C CD2 . TYR A 383 ? 1.8424 1.5307 2.3776 -0.0834 -0.0576 -0.2088 383 TYR A CD2 
2901 C CE1 . TYR A 383 ? 1.7432 1.5149 2.3701 -0.0691 -0.0477 -0.2065 383 TYR A CE1 
2902 C CE2 . TYR A 383 ? 1.8200 1.5311 2.3798 -0.0958 -0.0412 -0.2151 383 TYR A CE2 
2903 C CZ  . TYR A 383 ? 1.7606 1.5132 2.3670 -0.0878 -0.0372 -0.2142 383 TYR A CZ  
2904 O OH  . TYR A 383 ? 1.7620 1.5367 2.3938 -0.0981 -0.0232 -0.2214 383 TYR A OH  
2905 N N   . THR A 384 ? 1.3152 1.0468 1.8872 -0.0116 -0.0992 -0.1904 384 THR A N   
2906 C CA  . THR A 384 ? 1.4167 1.1851 2.0232 -0.0012 -0.0958 -0.1878 384 THR A CA  
2907 C C   . THR A 384 ? 1.5601 1.3704 2.2120 0.0023  -0.0925 -0.1846 384 THR A C   
2908 O O   . THR A 384 ? 1.8796 1.6958 2.5388 0.0092  -0.1007 -0.1826 384 THR A O   
2909 C CB  . THR A 384 ? 1.4717 1.2356 2.0679 0.0177  -0.1089 -0.1864 384 THR A CB  
2910 O OG1 . THR A 384 ? 1.9573 1.6773 2.5076 0.0134  -0.1137 -0.1893 384 THR A OG1 
2911 C CG2 . THR A 384 ? 1.3712 1.1702 1.9979 0.0277  -0.1048 -0.1841 384 THR A CG2 
2912 N N   . HIS A 385 ? 1.3415 1.1778 2.0215 -0.0029 -0.0813 -0.1843 385 HIS A N   
2913 C CA  . HIS A 385 ? 1.3694 1.2407 2.0890 -0.0025 -0.0776 -0.1814 385 HIS A CA  
2914 C C   . HIS A 385 ? 1.3534 1.2555 2.1005 0.0054  -0.0752 -0.1778 385 HIS A C   
2915 O O   . HIS A 385 ? 1.3492 1.2492 2.0933 0.0024  -0.0698 -0.1796 385 HIS A O   
2916 C CB  . HIS A 385 ? 1.5247 1.3960 2.2525 -0.0185 -0.0672 -0.1857 385 HIS A CB  
2917 C CG  . HIS A 385 ? 1.6313 1.5369 2.3994 -0.0178 -0.0637 -0.1831 385 HIS A CG  
2918 N ND1 . HIS A 385 ? 1.5652 1.4838 2.3509 -0.0165 -0.0676 -0.1802 385 HIS A ND1 
2919 C CD2 . HIS A 385 ? 1.5537 1.4806 2.3458 -0.0184 -0.0581 -0.1829 385 HIS A CD2 
2920 C CE1 . HIS A 385 ? 1.5134 1.4586 2.3309 -0.0169 -0.0644 -0.1781 385 HIS A CE1 
2921 N NE2 . HIS A 385 ? 1.5349 1.4851 2.3564 -0.0176 -0.0590 -0.1797 385 HIS A NE2 
2922 N N   . GLY A 386 ? 1.3873 1.3164 2.1591 0.0146  -0.0797 -0.1728 386 GLY A N   
2923 C CA  . GLY A 386 ? 1.2685 1.2258 2.0627 0.0227  -0.0786 -0.1687 386 GLY A CA  
2924 C C   . GLY A 386 ? 1.0232 1.0101 1.8504 0.0208  -0.0776 -0.1640 386 GLY A C   
2925 O O   . GLY A 386 ? 0.9884 0.9800 1.8222 0.0211  -0.0824 -0.1623 386 GLY A O   
2926 N N   . ARG A 387 ? 0.9943 1.0000 1.8406 0.0193  -0.0727 -0.1613 387 ARG A N   
2927 C CA  . ARG A 387 ? 1.0963 1.1313 1.9705 0.0203  -0.0733 -0.1551 387 ARG A CA  
2928 C C   . ARG A 387 ? 1.0640 1.1169 1.9408 0.0321  -0.0760 -0.1518 387 ARG A C   
2929 O O   . ARG A 387 ? 0.9393 0.9893 1.8059 0.0379  -0.0743 -0.1530 387 ARG A O   
2930 C CB  . ARG A 387 ? 1.2846 1.3283 2.1748 0.0135  -0.0683 -0.1540 387 ARG A CB  
2931 C CG  . ARG A 387 ? 1.3253 1.3524 2.2124 0.0036  -0.0640 -0.1604 387 ARG A CG  
2932 C CD  . ARG A 387 ? 0.9219 0.9585 1.8282 -0.0016 -0.0616 -0.1607 387 ARG A CD  
2933 N NE  . ARG A 387 ? 0.9843 1.0069 1.8884 -0.0105 -0.0577 -0.1690 387 ARG A NE  
2934 C CZ  . ARG A 387 ? 1.3266 1.3537 2.2477 -0.0163 -0.0559 -0.1731 387 ARG A CZ  
2935 N NH1 . ARG A 387 ? 1.7136 1.7550 2.6526 -0.0142 -0.0593 -0.1688 387 ARG A NH1 
2936 N NH2 . ARG A 387 ? 1.4402 1.4568 2.3592 -0.0241 -0.0512 -0.1822 387 ARG A NH2 
2937 N N   . LEU A 388 ? 1.0387 1.1111 1.9299 0.0351  -0.0801 -0.1484 388 LEU A N   
2938 C CA  . LEU A 388 ? 1.0983 1.1957 1.9984 0.0448  -0.0811 -0.1459 388 LEU A CA  
2939 C C   . LEU A 388 ? 1.0345 1.1605 1.9606 0.0386  -0.0797 -0.1393 388 LEU A C   
2940 O O   . LEU A 388 ? 0.9534 1.0823 1.8899 0.0323  -0.0828 -0.1374 388 LEU A O   
2941 C CB  . LEU A 388 ? 0.9419 1.0397 1.8335 0.0572  -0.0882 -0.1499 388 LEU A CB  
2942 C CG  . LEU A 388 ? 1.0397 1.1206 1.9239 0.0555  -0.0954 -0.1524 388 LEU A CG  
2943 C CD1 . LEU A 388 ? 0.8578 0.9593 1.7536 0.0652  -0.1031 -0.1535 388 LEU A CD1 
2944 C CD2 . LEU A 388 ? 0.9991 1.0412 1.8507 0.0567  -0.0981 -0.1580 388 LEU A CD2 
2945 N N   . LEU A 389 ? 1.1762 1.3209 2.1098 0.0399  -0.0752 -0.1358 389 LEU A N   
2946 C CA  . LEU A 389 ? 1.1957 1.3665 2.1495 0.0328  -0.0734 -0.1289 389 LEU A CA  
2947 C C   . LEU A 389 ? 1.3937 1.5919 2.3527 0.0407  -0.0705 -0.1286 389 LEU A C   
2948 O O   . LEU A 389 ? 1.3948 1.5912 2.3429 0.0478  -0.0672 -0.1308 389 LEU A O   
2949 C CB  . LEU A 389 ? 1.2655 1.4282 2.2210 0.0234  -0.0705 -0.1250 389 LEU A CB  
2950 C CG  . LEU A 389 ? 1.2342 1.4169 2.2035 0.0150  -0.0689 -0.1171 389 LEU A CG  
2951 C CD1 . LEU A 389 ? 1.2139 1.3830 2.1889 0.0040  -0.0718 -0.1142 389 LEU A CD1 
2952 C CD2 . LEU A 389 ? 1.3924 1.5830 2.3552 0.0183  -0.0640 -0.1154 389 LEU A CD2 
2953 N N   . GLU A 390 ? 1.7099 1.9333 2.6854 0.0397  -0.0721 -0.1271 390 GLU A N   
2954 C CA  . GLU A 390 ? 1.8050 2.0599 2.7895 0.0465  -0.0687 -0.1286 390 GLU A CA  
2955 C C   . GLU A 390 ? 1.4356 1.7157 2.4413 0.0343  -0.0682 -0.1225 390 GLU A C   
2956 O O   . GLU A 390 ? 1.1151 1.4025 2.1311 0.0351  -0.0738 -0.1245 390 GLU A O   
2957 C CB  . GLU A 390 ? 2.0800 2.3383 3.0617 0.0622  -0.0742 -0.1375 390 GLU A CB  
2958 C CG  . GLU A 390 ? 2.8339 3.0728 3.7935 0.0760  -0.0746 -0.1440 390 GLU A CG  
2959 C CD  . GLU A 390 ? 3.0813 3.3418 4.0409 0.0846  -0.0683 -0.1466 390 GLU A CD  
2960 O OE1 . GLU A 390 ? 2.7681 3.0599 3.7429 0.0915  -0.0679 -0.1508 390 GLU A OE1 
2961 O OE2 . GLU A 390 ? 3.5250 3.7720 4.4700 0.0847  -0.0639 -0.1454 390 GLU A OE2 
2962 N N   . PRO A 391 ? 1.3684 1.6556 2.3781 0.0214  -0.0632 -0.1146 391 PRO A N   
2963 C CA  . PRO A 391 ? 1.2704 1.5794 2.2973 0.0074  -0.0628 -0.1079 391 PRO A CA  
2964 C C   . PRO A 391 ? 1.5045 1.8489 2.5476 0.0131  -0.0617 -0.1126 391 PRO A C   
2965 O O   . PRO A 391 ? 1.5143 1.8705 2.5723 0.0082  -0.0665 -0.1121 391 PRO A O   
2966 C CB  . PRO A 391 ? 1.1924 1.5054 2.2140 -0.0025 -0.0563 -0.1008 391 PRO A CB  
2967 C CG  . PRO A 391 ? 1.5402 1.8224 2.5435 0.0030  -0.0568 -0.1023 391 PRO A CG  
2968 C CD  . PRO A 391 ? 1.4818 1.7534 2.4776 0.0192  -0.0591 -0.1117 391 PRO A CD  
2969 N N   . GLU A 392 ? 1.6152 1.9754 2.6549 0.0248  -0.0559 -0.1185 392 GLU A N   
2970 C CA  . GLU A 392 ? 1.6898 2.0889 2.7453 0.0320  -0.0523 -0.1250 392 GLU A CA  
2971 C C   . GLU A 392 ? 1.5338 1.9388 2.6028 0.0391  -0.0620 -0.1311 392 GLU A C   
2972 O O   . GLU A 392 ? 1.3685 1.8049 2.4595 0.0332  -0.0621 -0.1314 392 GLU A O   
2973 C CB  . GLU A 392 ? 1.9089 2.3080 2.9516 0.0494  -0.0486 -0.1333 392 GLU A CB  
2974 C CG  . GLU A 392 ? 1.8500 2.2189 2.8688 0.0493  -0.0454 -0.1298 392 GLU A CG  
2975 C CD  . GLU A 392 ? 2.1115 2.4911 3.1260 0.0380  -0.0356 -0.1231 392 GLU A CD  
2976 O OE1 . GLU A 392 ? 2.6643 3.0766 3.6859 0.0404  -0.0276 -0.1267 392 GLU A OE1 
2977 O OE2 . GLU A 392 ? 2.0356 2.3908 3.0388 0.0275  -0.0362 -0.1153 392 GLU A OE2 
2978 N N   . THR A 393 ? 1.6861 2.0595 2.7404 0.0511  -0.0704 -0.1360 393 THR A N   
2979 C CA  . THR A 393 ? 1.6440 2.0186 2.7048 0.0624  -0.0809 -0.1438 393 THR A CA  
2980 C C   . THR A 393 ? 1.4629 1.8124 2.5215 0.0529  -0.0892 -0.1391 393 THR A C   
2981 O O   . THR A 393 ? 1.3916 1.7501 2.4630 0.0537  -0.0973 -0.1416 393 THR A O   
2982 C CB  . THR A 393 ? 1.6335 1.9873 2.6748 0.0823  -0.0858 -0.1531 393 THR A CB  
2983 O OG1 . THR A 393 ? 1.6414 1.9516 2.6579 0.0790  -0.0873 -0.1494 393 THR A OG1 
2984 C CG2 . THR A 393 ? 1.6767 2.0497 2.7160 0.0926  -0.0778 -0.1582 393 THR A CG2 
2985 N N   . LEU A 394 ? 1.3235 1.6402 2.3653 0.0449  -0.0877 -0.1333 394 LEU A N   
2986 C CA  . LEU A 394 ? 1.2534 1.5437 2.2903 0.0381  -0.0952 -0.1310 394 LEU A CA  
2987 C C   . LEU A 394 ? 1.3860 1.6919 2.4409 0.0210  -0.0948 -0.1230 394 LEU A C   
2988 O O   . LEU A 394 ? 1.5967 1.8930 2.6551 0.0162  -0.1025 -0.1222 394 LEU A O   
2989 C CB  . LEU A 394 ? 1.2256 1.4773 2.2391 0.0370  -0.0937 -0.1303 394 LEU A CB  
2990 C CG  . LEU A 394 ? 1.2780 1.5062 2.2695 0.0518  -0.0969 -0.1383 394 LEU A CG  
2991 C CD1 . LEU A 394 ? 1.6598 1.8542 2.6311 0.0470  -0.0934 -0.1372 394 LEU A CD1 
2992 C CD2 . LEU A 394 ? 1.0905 1.3097 2.0788 0.0595  -0.1083 -0.1440 394 LEU A CD2 
2993 N N   . GLY A 395 ? 1.3502 1.6789 2.4144 0.0119  -0.0865 -0.1172 395 GLY A N   
2994 C CA  . GLY A 395 ? 1.4763 1.8153 2.5528 -0.0062 -0.0861 -0.1084 395 GLY A CA  
2995 C C   . GLY A 395 ? 1.4248 1.7931 2.5232 -0.0100 -0.0906 -0.1093 395 GLY A C   
2996 O O   . GLY A 395 ? 1.3059 1.6835 2.4151 -0.0261 -0.0916 -0.1021 395 GLY A O   
2997 N N   . LYS A 396 ? 1.4285 1.8091 2.5324 0.0053  -0.0945 -0.1187 396 LYS A N   
2998 C CA  . LYS A 396 ? 1.3933 1.8035 2.5197 0.0060  -0.1004 -0.1227 396 LYS A CA  
2999 C C   . LYS A 396 ? 1.2523 1.6356 2.3740 0.0066  -0.1133 -0.1236 396 LYS A C   
3000 O O   . LYS A 396 ? 1.7074 2.1068 2.8463 0.0003  -0.1199 -0.1231 396 LYS A O   
3001 C CB  . LYS A 396 ? 1.6081 2.0431 2.7417 0.0247  -0.0996 -0.1341 396 LYS A CB  
3002 C CG  . LYS A 396 ? 1.6533 2.1332 2.8034 0.0237  -0.0877 -0.1362 396 LYS A CG  
3003 C CD  . LYS A 396 ? 1.8549 2.3424 2.9979 0.0429  -0.0831 -0.1459 396 LYS A CD  
3004 C CE  . LYS A 396 ? 1.7574 2.2406 2.8986 0.0665  -0.0935 -0.1589 396 LYS A CE  
3005 N NZ  . LYS A 396 ? 2.0346 2.5603 3.2045 0.0749  -0.0980 -0.1691 396 LYS A NZ  
3006 N N   . LEU A 397 ? 0.9524 1.2945 2.0498 0.0132  -0.1166 -0.1251 397 LEU A N   
3007 C CA  . LEU A 397 ? 1.0446 1.3583 2.1324 0.0153  -0.1281 -0.1275 397 LEU A CA  
3008 C C   . LEU A 397 ? 1.1950 1.4894 2.2804 -0.0011 -0.1298 -0.1196 397 LEU A C   
3009 O O   . LEU A 397 ? 1.5215 1.8152 2.6068 -0.0121 -0.1226 -0.1127 397 LEU A O   
3010 C CB  . LEU A 397 ? 1.0463 1.3251 2.1067 0.0279  -0.1288 -0.1329 397 LEU A CB  
3011 C CG  . LEU A 397 ? 1.0219 1.3084 2.0791 0.0468  -0.1329 -0.1424 397 LEU A CG  
3012 C CD1 . LEU A 397 ? 1.2385 1.4971 2.2692 0.0549  -0.1279 -0.1450 397 LEU A CD1 
3013 C CD2 . LEU A 397 ? 0.7456 1.0182 1.7993 0.0532  -0.1477 -0.1477 397 LEU A CD2 
3014 N N   . ASN A 398 ? 1.0714 1.3475 2.1529 -0.0017 -0.1405 -0.1214 398 ASN A N   
3015 C CA  . ASN A 398 ? 1.1045 1.3507 2.1755 -0.0127 -0.1434 -0.1171 398 ASN A CA  
3016 C C   . ASN A 398 ? 1.1105 1.3185 2.1565 -0.0043 -0.1491 -0.1235 398 ASN A C   
3017 O O   . ASN A 398 ? 1.0177 1.2246 2.0572 0.0086  -0.1537 -0.1300 398 ASN A O   
3018 C CB  . ASN A 398 ? 1.1737 1.4344 2.2626 -0.0252 -0.1502 -0.1121 398 ASN A CB  
3019 C CG  . ASN A 398 ? 1.5257 1.7806 2.6147 -0.0191 -0.1630 -0.1175 398 ASN A CG  
3020 O OD1 . ASN A 398 ? 1.3081 1.5496 2.3836 -0.0051 -0.1667 -0.1249 398 ASN A OD1 
3021 N ND2 . ASN A 398 ? 2.0665 2.3289 3.1686 -0.0296 -0.1709 -0.1140 398 ASN A ND2 
3022 N N   . PRO A 399 ? 1.3192 1.4947 2.3496 -0.0115 -0.1493 -0.1225 399 PRO A N   
3023 C CA  . PRO A 399 ? 1.3724 1.5105 2.3753 -0.0058 -0.1515 -0.1288 399 PRO A CA  
3024 C C   . PRO A 399 ? 1.3100 1.4433 2.3071 0.0030  -0.1636 -0.1338 399 PRO A C   
3025 O O   . PRO A 399 ? 1.6288 1.7439 2.6057 0.0136  -0.1660 -0.1397 399 PRO A O   
3026 C CB  . PRO A 399 ? 1.1456 1.2606 2.1422 -0.0174 -0.1520 -0.1271 399 PRO A CB  
3027 C CG  . PRO A 399 ? 1.3223 1.4563 2.3371 -0.0266 -0.1460 -0.1203 399 PRO A CG  
3028 C CD  . PRO A 399 ? 1.3951 1.5674 2.4322 -0.0256 -0.1470 -0.1162 399 PRO A CD  
3029 N N   . ARG A 400 ? 1.0707 1.2164 2.0837 -0.0027 -0.1723 -0.1313 400 ARG A N   
3030 C CA  . ARG A 400 ? 1.2629 1.4014 2.2717 0.0034  -0.1865 -0.1357 400 ARG A CA  
3031 C C   . ARG A 400 ? 1.3975 1.5547 2.4118 0.0190  -0.1907 -0.1414 400 ARG A C   
3032 O O   . ARG A 400 ? 1.4029 1.5368 2.3969 0.0297  -0.2002 -0.1477 400 ARG A O   
3033 C CB  . ARG A 400 ? 1.3117 1.4728 2.3452 -0.0055 -0.1943 -0.1314 400 ARG A CB  
3034 C CG  . ARG A 400 ? 1.6029 1.7637 2.6379 0.0019  -0.2105 -0.1365 400 ARG A CG  
3035 C CD  . ARG A 400 ? 1.8189 2.0252 2.8901 -0.0003 -0.2162 -0.1351 400 ARG A CD  
3036 N NE  . ARG A 400 ? 1.5583 1.7713 2.6437 -0.0161 -0.2201 -0.1287 400 ARG A NE  
3037 C CZ  . ARG A 400 ? 1.5619 1.7455 2.6334 -0.0207 -0.2309 -0.1287 400 ARG A CZ  
3038 N NH1 . ARG A 400 ? 1.6100 1.7547 2.6515 -0.0123 -0.2374 -0.1343 400 ARG A NH1 
3039 N NH2 . ARG A 400 ? 1.4607 1.6519 2.5460 -0.0347 -0.2354 -0.1231 400 ARG A NH2 
3040 N N   . THR A 401 ? 1.4538 1.6521 2.4943 0.0197  -0.1838 -0.1393 401 THR A N   
3041 C CA  . THR A 401 ? 1.4219 1.6466 2.4737 0.0346  -0.1860 -0.1455 401 THR A CA  
3042 C C   . THR A 401 ? 1.2743 1.4700 2.2969 0.0476  -0.1847 -0.1512 401 THR A C   
3043 O O   . THR A 401 ? 1.1954 1.3835 2.2089 0.0624  -0.1955 -0.1588 401 THR A O   
3044 C CB  . THR A 401 ? 1.5145 1.7821 2.5925 0.0295  -0.1735 -0.1415 401 THR A CB  
3045 O OG1 . THR A 401 ? 1.5481 1.8433 2.6522 0.0172  -0.1762 -0.1369 401 THR A OG1 
3046 C CG2 . THR A 401 ? 1.6041 1.9017 2.6938 0.0446  -0.1717 -0.1486 401 THR A CG2 
3047 N N   . ALA A 402 ? 1.1645 1.3437 2.1729 0.0412  -0.1723 -0.1473 402 ALA A N   
3048 C CA  . ALA A 402 ? 1.0306 1.1831 2.0116 0.0501  -0.1688 -0.1514 402 ALA A CA  
3049 C C   . ALA A 402 ? 1.0121 1.1208 1.9612 0.0543  -0.1801 -0.1563 402 ALA A C   
3050 O O   . ALA A 402 ? 1.0635 1.1554 1.9931 0.0675  -0.1866 -0.1625 402 ALA A O   
3051 C CB  . ALA A 402 ? 1.0879 1.2331 2.0628 0.0410  -0.1543 -0.1467 402 ALA A CB  
3052 N N   . VAL A 403 ? 1.0754 1.1644 2.0178 0.0427  -0.1828 -0.1535 403 VAL A N   
3053 C CA  . VAL A 403 ? 1.1232 1.1676 2.0320 0.0432  -0.1920 -0.1574 403 VAL A CA  
3054 C C   . VAL A 403 ? 1.2348 1.2795 2.1424 0.0569  -0.2098 -0.1631 403 VAL A C   
3055 O O   . VAL A 403 ? 1.2855 1.2954 2.1611 0.0652  -0.2183 -0.1683 403 VAL A O   
3056 C CB  . VAL A 403 ? 1.2107 1.2268 2.1049 0.0291  -0.1913 -0.1553 403 VAL A CB  
3057 C CG1 . VAL A 403 ? 0.9756 0.9416 1.8265 0.0293  -0.1961 -0.1602 403 VAL A CG1 
3058 C CG2 . VAL A 403 ? 1.3055 1.3285 2.2094 0.0166  -0.1760 -0.1507 403 VAL A CG2 
3059 N N   . GLU A 404 ? 1.3769 1.4598 2.3186 0.0588  -0.2159 -0.1624 404 GLU A N   
3060 C CA  . GLU A 404 ? 1.5567 1.6426 2.5012 0.0725  -0.2343 -0.1691 404 GLU A CA  
3061 C C   . GLU A 404 ? 1.5644 1.6565 2.5048 0.0905  -0.2369 -0.1761 404 GLU A C   
3062 O O   . GLU A 404 ? 1.3738 1.4359 2.2885 0.1031  -0.2513 -0.1827 404 GLU A O   
3063 C CB  . GLU A 404 ? 2.0102 2.1320 2.9901 0.0700  -0.2428 -0.1684 404 GLU A CB  
3064 C CG  . GLU A 404 ? 2.6264 2.7375 3.6070 0.0522  -0.2414 -0.1615 404 GLU A CG  
3065 C CD  . GLU A 404 ? 3.3169 3.4689 4.3361 0.0464  -0.2468 -0.1592 404 GLU A CD  
3066 O OE1 . GLU A 404 ? 3.5551 3.6936 4.5717 0.0417  -0.2595 -0.1590 404 GLU A OE1 
3067 O OE2 . GLU A 404 ? 3.6905 3.8881 4.7415 0.0461  -0.2387 -0.1580 404 GLU A OE2 
3068 N N   . ARG A 405 ? 1.5778 1.6997 2.5352 0.0914  -0.2224 -0.1744 405 ARG A N   
3069 C CA  . ARG A 405 ? 1.3162 1.4438 2.2687 0.1084  -0.2232 -0.1812 405 ARG A CA  
3070 C C   . ARG A 405 ? 1.2406 1.3125 2.1457 0.1130  -0.2281 -0.1839 405 ARG A C   
3071 O O   . ARG A 405 ? 1.2302 1.2861 2.1191 0.1295  -0.2418 -0.1918 405 ARG A O   
3072 C CB  . ARG A 405 ? 1.3435 1.4994 2.3109 0.1055  -0.2046 -0.1777 405 ARG A CB  
3073 C CG  . ARG A 405 ? 1.2688 1.4830 2.2801 0.1042  -0.1988 -0.1770 405 ARG A CG  
3074 C CD  . ARG A 405 ? 1.2690 1.5076 2.2889 0.1214  -0.1977 -0.1849 405 ARG A CD  
3075 N NE  . ARG A 405 ? 1.3923 1.6859 2.4508 0.1150  -0.1863 -0.1826 405 ARG A NE  
3076 C CZ  . ARG A 405 ? 1.4154 1.7256 2.4783 0.1098  -0.1700 -0.1784 405 ARG A CZ  
3077 N NH1 . ARG A 405 ? 1.2203 1.4981 2.2547 0.1103  -0.1636 -0.1761 405 ARG A NH1 
3078 N NH2 . ARG A 405 ? 1.5118 1.8701 2.6068 0.1029  -0.1606 -0.1766 405 ARG A NH2 
3079 N N   . LEU A 406 ? 1.4532 1.4963 2.3367 0.0978  -0.2172 -0.1779 406 LEU A N   
3080 C CA  . LEU A 406 ? 1.3428 1.3340 2.1807 0.0977  -0.2189 -0.1799 406 LEU A CA  
3081 C C   . LEU A 406 ? 1.3514 1.3039 2.1608 0.1026  -0.2385 -0.1844 406 LEU A C   
3082 O O   . LEU A 406 ? 1.3920 1.3100 2.1682 0.1123  -0.2482 -0.1894 406 LEU A O   
3083 C CB  . LEU A 406 ? 1.3101 1.2824 2.1312 0.0832  -0.2017 -0.1753 406 LEU A CB  
3084 C CG  . LEU A 406 ? 1.2164 1.2212 2.0591 0.0837  -0.1865 -0.1727 406 LEU A CG  
3085 C CD1 . LEU A 406 ? 1.2764 1.2608 2.1019 0.0710  -0.1718 -0.1696 406 LEU A CD1 
3086 C CD2 . LEU A 406 ? 1.2319 1.2462 2.0735 0.1016  -0.1916 -0.1783 406 LEU A CD2 
3087 N N   . ARG A 407 ? 1.3147 1.2731 2.1372 0.0962  -0.2454 -0.1825 407 ARG A N   
3088 C CA  . ARG A 407 ? 1.3176 1.2384 2.1130 0.0994  -0.2647 -0.1862 407 ARG A CA  
3089 C C   . ARG A 407 ? 1.4806 1.4083 2.2802 0.1213  -0.2841 -0.1946 407 ARG A C   
3090 O O   . ARG A 407 ? 1.5892 1.4730 2.3526 0.1286  -0.3016 -0.1992 407 ARG A O   
3091 C CB  . ARG A 407 ? 1.1644 1.0912 1.9741 0.0873  -0.2675 -0.1822 407 ARG A CB  
3092 C CG  . ARG A 407 ? 1.2746 1.1477 2.0423 0.0846  -0.2827 -0.1844 407 ARG A CG  
3093 C CD  . ARG A 407 ? 1.3785 1.2471 2.1510 0.0715  -0.2854 -0.1808 407 ARG A CD  
3094 N NE  . ARG A 407 ? 1.5599 1.4395 2.3421 0.0554  -0.2635 -0.1749 407 ARG A NE  
3095 C CZ  . ARG A 407 ? 1.6241 1.5397 2.4424 0.0469  -0.2557 -0.1699 407 ARG A CZ  
3096 N NH1 . ARG A 407 ? 1.7669 1.6971 2.6052 0.0454  -0.2671 -0.1689 407 ARG A NH1 
3097 N NH2 . ARG A 407 ? 1.3697 1.3025 2.2007 0.0391  -0.2369 -0.1660 407 ARG A NH2 
3098 N N   . ALA A 408 ? 1.4592 1.4421 2.3038 0.1309  -0.2822 -0.1969 408 ALA A N   
3099 C CA  . ALA A 408 ? 1.5726 1.5736 2.4328 0.1518  -0.3011 -0.2065 408 ALA A CA  
3100 C C   . ALA A 408 ? 1.7459 1.7148 2.5729 0.1680  -0.3097 -0.2134 408 ALA A C   
3101 O O   . ALA A 408 ? 1.9934 1.9347 2.8002 0.1826  -0.3323 -0.2210 408 ALA A O   
3102 C CB  . ALA A 408 ? 1.5970 1.6666 2.5118 0.1556  -0.2924 -0.2078 408 ALA A CB  
3103 N N   . GLU A 409 ? 1.9838 1.9609 2.8092 0.1672  -0.2928 -0.2114 409 GLU A N   
3104 C CA  . GLU A 409 ? 2.0448 1.9989 2.8439 0.1828  -0.2988 -0.2178 409 GLU A CA  
3105 C C   . GLU A 409 ? 2.0323 1.9188 2.7734 0.1730  -0.3001 -0.2144 409 GLU A C   
3106 O O   . GLU A 409 ? 2.0984 1.9604 2.8120 0.1779  -0.2982 -0.2162 409 GLU A O   
3107 C CB  . GLU A 409 ? 2.0485 2.0473 2.8764 0.1865  -0.2810 -0.2178 409 GLU A CB  
3108 C CG  . GLU A 409 ? 2.2643 2.3310 3.1489 0.1898  -0.2762 -0.2197 409 GLU A CG  
3109 C CD  . GLU A 409 ? 2.9301 3.0230 3.8387 0.2107  -0.2957 -0.2317 409 GLU A CD  
3110 O OE1 . GLU A 409 ? 3.2597 3.3233 4.1444 0.2295  -0.3150 -0.2411 409 GLU A OE1 
3111 O OE2 . GLU A 409 ? 3.0659 3.2106 4.0192 0.2078  -0.2920 -0.2322 409 GLU A OE2 
3112 N N   . GLY A 410 ? 1.9709 1.8276 2.6930 0.1588  -0.3037 -0.2101 410 GLY A N   
3113 C CA  . GLY A 410 ? 1.9107 1.7040 2.5776 0.1464  -0.3051 -0.2073 410 GLY A CA  
3114 C C   . GLY A 410 ? 1.7895 1.5739 2.4417 0.1340  -0.2835 -0.2026 410 GLY A C   
3115 O O   . GLY A 410 ? 1.7037 1.4390 2.3091 0.1310  -0.2862 -0.2035 410 GLY A O   
3116 N N   . LEU A 411 ? 1.8487 1.6797 2.5401 0.1263  -0.2633 -0.1977 411 LEU A N   
3117 C CA  . LEU A 411 ? 2.0318 1.8627 2.7175 0.1157  -0.2431 -0.1938 411 LEU A CA  
3118 C C   . LEU A 411 ? 2.0822 1.8956 2.7563 0.0928  -0.2291 -0.1881 411 LEU A C   
3119 O O   . LEU A 411 ? 1.9742 1.7650 2.6248 0.0817  -0.2169 -0.1868 411 LEU A O   
3120 C CB  . LEU A 411 ? 1.8009 1.6885 2.5320 0.1220  -0.2310 -0.1926 411 LEU A CB  
3121 C CG  . LEU A 411 ? 1.5821 1.4778 2.3124 0.1414  -0.2367 -0.1988 411 LEU A CG  
3122 C CD1 . LEU A 411 ? 1.3055 1.2576 2.0792 0.1456  -0.2233 -0.1976 411 LEU A CD1 
3123 C CD2 . LEU A 411 ? 1.7268 1.5764 2.4123 0.1378  -0.2338 -0.1991 411 LEU A CD2 
3124 N N   . LEU A 412 ? 1.9375 1.7612 2.6279 0.0860  -0.2316 -0.1859 412 LEU A N   
3125 C CA  . LEU A 412 ? 1.9502 1.7607 2.6330 0.0659  -0.2193 -0.1819 412 LEU A CA  
3126 C C   . LEU A 412 ? 1.7539 1.5045 2.3813 0.0566  -0.2221 -0.1842 412 LEU A C   
3127 O O   . LEU A 412 ? 1.6074 1.3236 2.2031 0.0648  -0.2397 -0.1877 412 LEU A O   
3128 C CB  . LEU A 412 ? 1.8249 1.6560 2.5340 0.0632  -0.2253 -0.1798 412 LEU A CB  
3129 C CG  . LEU A 412 ? 1.5540 1.4049 2.2856 0.0470  -0.2091 -0.1748 412 LEU A CG  
3130 C CD1 . LEU A 412 ? 1.9040 1.7810 2.6662 0.0469  -0.2171 -0.1725 412 LEU A CD1 
3131 C CD2 . LEU A 412 ? 1.5124 1.3236 2.2097 0.0304  -0.1998 -0.1754 412 LEU A CD2 
3132 N N   . TYR A 413 ? 1.6227 1.3613 2.2384 0.0390  -0.2048 -0.1827 413 TYR A N   
3133 C CA  . TYR A 413 ? 1.5673 1.2528 2.1315 0.0264  -0.2036 -0.1851 413 TYR A CA  
3134 C C   . TYR A 413 ? 1.6300 1.2859 2.1718 0.0227  -0.2170 -0.1860 413 TYR A C   
3135 O O   . TYR A 413 ? 1.4988 1.1752 2.0657 0.0184  -0.2154 -0.1841 413 TYR A O   
3136 C CB  . TYR A 413 ? 1.6482 1.3371 2.2142 0.0081  -0.1809 -0.1847 413 TYR A CB  
3137 C CG  . TYR A 413 ? 1.9447 1.5824 2.4593 -0.0085 -0.1766 -0.1881 413 TYR A CG  
3138 C CD1 . TYR A 413 ? 2.2025 1.8202 2.7016 -0.0203 -0.1768 -0.1893 413 TYR A CD1 
3139 C CD2 . TYR A 413 ? 1.9645 1.5731 2.4444 -0.0138 -0.1721 -0.1902 413 TYR A CD2 
3140 C CE1 . TYR A 413 ? 2.1581 1.7292 2.6083 -0.0371 -0.1716 -0.1928 413 TYR A CE1 
3141 C CE2 . TYR A 413 ? 2.0704 1.6323 2.5016 -0.0315 -0.1672 -0.1933 413 TYR A CE2 
3142 C CZ  . TYR A 413 ? 1.9942 1.5375 2.4099 -0.0434 -0.1665 -0.1948 413 TYR A CZ  
3143 O OH  . TYR A 413 ? 1.8192 1.3172 2.1855 -0.0625 -0.1602 -0.1984 413 TYR A OH  
3144 N N   . ARG A 414 ? 1.7214 1.3261 2.2132 0.0240  -0.2311 -0.1888 414 ARG A N   
3145 C CA  . ARG A 414 ? 2.0070 1.5732 2.4666 0.0180  -0.2437 -0.1899 414 ARG A CA  
3146 C C   . ARG A 414 ? 1.9721 1.4865 2.3771 -0.0020 -0.2343 -0.1916 414 ARG A C   
3147 O O   . ARG A 414 ? 1.8871 1.3821 2.2669 -0.0054 -0.2287 -0.1927 414 ARG A O   
3148 C CB  . ARG A 414 ? 2.1469 1.6970 2.5954 0.0370  -0.2715 -0.1921 414 ARG A CB  
3149 C CG  . ARG A 414 ? 2.4434 2.0474 2.9479 0.0546  -0.2804 -0.1917 414 ARG A CG  
3150 C CD  . ARG A 414 ? 2.5856 2.1725 3.0775 0.0746  -0.3083 -0.1963 414 ARG A CD  
3151 N NE  . ARG A 414 ? 3.0721 2.6315 3.5327 0.0827  -0.3130 -0.1992 414 ARG A NE  
3152 C CZ  . ARG A 414 ? 3.1838 2.7745 3.6689 0.0949  -0.3078 -0.2005 414 ARG A CZ  
3153 N NH1 . ARG A 414 ? 2.9869 2.6403 3.5300 0.1017  -0.2987 -0.1993 414 ARG A NH1 
3154 N NH2 . ARG A 414 ? 3.3276 2.8846 3.7764 0.0991  -0.3118 -0.2029 414 ARG A NH2 
3155 N N   . HIS A 415 ? 2.0516 1.5448 2.4385 -0.0160 -0.2322 -0.1922 415 HIS A N   
3156 C CA  . HIS A 415 ? 2.1282 1.5802 2.4688 -0.0382 -0.2188 -0.1948 415 HIS A CA  
3157 C C   . HIS A 415 ? 2.2035 1.5896 2.4777 -0.0404 -0.2360 -0.1962 415 HIS A C   
3158 O O   . HIS A 415 ? 2.3849 1.7319 2.6131 -0.0584 -0.2260 -0.1982 415 HIS A O   
3159 C CB  . HIS A 415 ? 2.4840 1.9424 2.8335 -0.0519 -0.2085 -0.1958 415 HIS A CB  
3160 C CG  . HIS A 415 ? 2.7080 2.2230 3.1150 -0.0529 -0.1906 -0.1950 415 HIS A CG  
3161 N ND1 . HIS A 415 ? 2.8286 2.3564 3.2427 -0.0667 -0.1669 -0.1980 415 HIS A ND1 
3162 C CD2 . HIS A 415 ? 2.3765 1.9370 2.8351 -0.0423 -0.1939 -0.1918 415 HIS A CD2 
3163 C CE1 . HIS A 415 ? 2.2973 1.8742 2.7644 -0.0631 -0.1579 -0.1966 415 HIS A CE1 
3164 N NE2 . HIS A 415 ? 2.0834 1.6798 2.5766 -0.0493 -0.1737 -0.1923 415 HIS A NE2 
3165 N N   . ASP A 416 ? 2.2982 1.6725 2.5679 -0.0224 -0.2624 -0.1956 416 ASP A N   
3166 C CA  . ASP A 416 ? 2.6658 1.9756 2.8734 -0.0211 -0.2844 -0.1970 416 ASP A CA  
3167 C C   . ASP A 416 ? 2.7173 2.0062 2.8998 -0.0153 -0.2884 -0.1977 416 ASP A C   
3168 O O   . ASP A 416 ? 2.8145 2.0423 2.9335 -0.0256 -0.2953 -0.1986 416 ASP A O   
3169 C CB  . ASP A 416 ? 2.7969 2.1047 3.0134 -0.0030 -0.3122 -0.1973 416 ASP A CB  
3170 C CG  . ASP A 416 ? 2.7081 2.0786 2.9913 0.0201  -0.3189 -0.1970 416 ASP A CG  
3171 O OD1 . ASP A 416 ? 2.3862 1.7969 2.7037 0.0241  -0.3039 -0.1962 416 ASP A OD1 
3172 O OD2 . ASP A 416 ? 2.7606 2.1401 3.0611 0.0331  -0.3386 -0.1979 416 ASP A OD2 
3173 N N   . THR A 417 ? 2.4815 1.8194 2.7119 0.0003  -0.2845 -0.1972 417 THR A N   
3174 C CA  . THR A 417 ? 2.1858 1.5114 2.4002 0.0084  -0.2881 -0.1982 417 THR A CA  
3175 C C   . THR A 417 ? 2.0060 1.3380 2.2171 -0.0109 -0.2606 -0.1974 417 THR A C   
3176 O O   . THR A 417 ? 2.1339 1.4253 2.2999 -0.0190 -0.2605 -0.1981 417 THR A O   
3177 C CB  . THR A 417 ? 2.2770 1.6510 2.5423 0.0356  -0.2983 -0.1992 417 THR A CB  
3178 O OG1 . THR A 417 ? 2.3465 1.7859 2.6745 0.0347  -0.2789 -0.1969 417 THR A OG1 
3179 C CG2 . THR A 417 ? 2.4313 1.7994 2.7001 0.0559  -0.3273 -0.2019 417 THR A CG2 
3180 N N   . GLY A 418 ? 2.1821 1.5646 2.4411 -0.0183 -0.2385 -0.1963 418 GLY A N   
3181 C CA  . GLY A 418 ? 2.1788 1.5716 2.4402 -0.0372 -0.2122 -0.1969 418 GLY A CA  
3182 C C   . GLY A 418 ? 2.1172 1.5536 2.4191 -0.0262 -0.2037 -0.1959 418 GLY A C   
3183 O O   . GLY A 418 ? 2.0115 1.4490 2.3083 -0.0390 -0.1866 -0.1969 418 GLY A O   
3184 N N   . GLU A 419 ? 2.0979 1.5707 2.4401 -0.0033 -0.2155 -0.1945 419 GLU A N   
3185 C CA  . GLU A 419 ? 2.0760 1.5889 2.4545 0.0088  -0.2095 -0.1937 419 GLU A CA  
3186 C C   . GLU A 419 ? 1.9744 1.5416 2.4098 0.0272  -0.2148 -0.1922 419 GLU A C   
3187 O O   . GLU A 419 ? 2.0169 1.5811 2.4544 0.0392  -0.2329 -0.1929 419 GLU A O   
3188 C CB  . GLU A 419 ? 2.2897 1.7677 2.6315 0.0191  -0.2236 -0.1955 419 GLU A CB  
3189 C CG  . GLU A 419 ? 2.3125 1.7520 2.6221 0.0328  -0.2514 -0.1975 419 GLU A CG  
3190 C CD  . GLU A 419 ? 2.5292 1.9586 2.8282 0.0528  -0.2670 -0.2001 419 GLU A CD  
3191 O OE1 . GLU A 419 ? 2.5162 1.9170 2.7824 0.0455  -0.2626 -0.2003 419 GLU A OE1 
3192 O OE2 . GLU A 419 ? 2.7633 2.2163 3.0894 0.0756  -0.2832 -0.2025 419 GLU A OE2 
3193 N N   . GLY A 420 ? 1.9784 1.5942 2.4587 0.0281  -0.1989 -0.1903 420 GLY A N   
3194 C CA  . GLY A 420 ? 1.8158 1.4855 2.3495 0.0432  -0.2008 -0.1884 420 GLY A CA  
3195 C C   . GLY A 420 ? 1.7328 1.4471 2.3081 0.0356  -0.1800 -0.1854 420 GLY A C   
3196 O O   . GLY A 420 ? 1.5506 1.2593 2.1180 0.0231  -0.1648 -0.1856 420 GLY A O   
3197 N N   . VAL A 421 ? 1.5327 1.2915 2.1533 0.0423  -0.1802 -0.1828 421 VAL A N   
3198 C CA  . VAL A 421 ? 1.5375 1.3418 2.2004 0.0400  -0.1652 -0.1794 421 VAL A CA  
3199 C C   . VAL A 421 ? 1.6292 1.4531 2.3179 0.0299  -0.1599 -0.1766 421 VAL A C   
3200 O O   . VAL A 421 ? 2.1061 1.9341 2.8028 0.0333  -0.1706 -0.1760 421 VAL A O   
3201 C CB  . VAL A 421 ? 1.4629 1.3067 2.1574 0.0566  -0.1678 -0.1784 421 VAL A CB  
3202 C CG1 . VAL A 421 ? 1.2753 1.1573 2.0044 0.0514  -0.1517 -0.1746 421 VAL A CG1 
3203 C CG2 . VAL A 421 ? 1.5618 1.3858 2.2310 0.0697  -0.1762 -0.1823 421 VAL A CG2 
3204 N N   . ALA A 422 ? 1.5686 1.4035 2.2698 0.0176  -0.1438 -0.1756 422 ALA A N   
3205 C CA  . ALA A 422 ? 1.3254 1.1810 2.0536 0.0085  -0.1372 -0.1733 422 ALA A CA  
3206 C C   . ALA A 422 ? 1.2669 1.1601 2.0305 0.0084  -0.1261 -0.1701 422 ALA A C   
3207 O O   . ALA A 422 ? 1.1836 1.0767 1.9437 0.0066  -0.1168 -0.1713 422 ALA A O   
3208 C CB  . ALA A 422 ? 1.2946 1.1196 1.9981 -0.0069 -0.1305 -0.1771 422 ALA A CB  
3209 N N   . LEU A 423 ? 1.1436 1.0674 1.9401 0.0092  -0.1279 -0.1658 423 LEU A N   
3210 C CA  . LEU A 423 ? 1.2332 1.1910 2.0626 0.0078  -0.1196 -0.1617 423 LEU A CA  
3211 C C   . LEU A 423 ? 1.1682 1.1260 2.0076 -0.0049 -0.1109 -0.1622 423 LEU A C   
3212 O O   . LEU A 423 ? 1.2079 1.1476 2.0371 -0.0126 -0.1116 -0.1650 423 LEU A O   
3213 C CB  . LEU A 423 ? 1.3455 1.3384 2.2045 0.0153  -0.1259 -0.1565 423 LEU A CB  
3214 C CG  . LEU A 423 ? 1.1958 1.1969 2.0522 0.0299  -0.1342 -0.1576 423 LEU A CG  
3215 C CD1 . LEU A 423 ? 1.2227 1.1981 2.0587 0.0318  -0.1465 -0.1608 423 LEU A CD1 
3216 C CD2 . LEU A 423 ? 1.0038 1.0478 1.8949 0.0346  -0.1355 -0.1531 423 LEU A CD2 
3217 N N   . HIS A 424 ? 1.0357 1.0139 1.8949 -0.0062 -0.1030 -0.1602 424 HIS A N   
3218 C CA  . HIS A 424 ? 1.2576 1.2421 2.1331 -0.0154 -0.0966 -0.1607 424 HIS A CA  
3219 C C   . HIS A 424 ? 1.3941 1.4099 2.3001 -0.0139 -0.0975 -0.1537 424 HIS A C   
3220 O O   . HIS A 424 ? 1.3605 1.3947 2.2748 -0.0070 -0.0977 -0.1496 424 HIS A O   
3221 C CB  . HIS A 424 ? 1.0863 1.0569 1.9507 -0.0211 -0.0861 -0.1673 424 HIS A CB  
3222 C CG  . HIS A 424 ? 1.0013 0.9418 1.8318 -0.0230 -0.0847 -0.1730 424 HIS A CG  
3223 N ND1 . HIS A 424 ? 1.0833 1.0145 1.8992 -0.0229 -0.0787 -0.1762 424 HIS A ND1 
3224 C CD2 . HIS A 424 ? 1.0013 0.9167 1.8071 -0.0255 -0.0895 -0.1756 424 HIS A CD2 
3225 C CE1 . HIS A 424 ? 1.2667 1.1671 2.0488 -0.0262 -0.0795 -0.1805 424 HIS A CE1 
3226 N NE2 . HIS A 424 ? 1.2209 1.1107 1.9957 -0.0277 -0.0862 -0.1801 424 HIS A NE2 
3227 N N   . VAL A 425 ? 1.4546 1.4743 2.3756 -0.0212 -0.0975 -0.1529 425 VAL A N   
3228 C CA  . VAL A 425 ? 1.5131 1.5559 2.4589 -0.0228 -0.0980 -0.1467 425 VAL A CA  
3229 C C   . VAL A 425 ? 1.4895 1.5535 2.4463 -0.0189 -0.1047 -0.1392 425 VAL A C   
3230 O O   . VAL A 425 ? 1.4121 1.4964 2.3792 -0.0155 -0.1030 -0.1345 425 VAL A O   
3231 C CB  . VAL A 425 ? 1.3254 1.3753 2.2746 -0.0204 -0.0912 -0.1470 425 VAL A CB  
3232 C CG1 . VAL A 425 ? 1.5285 1.5950 2.4988 -0.0239 -0.0925 -0.1414 425 VAL A CG1 
3233 C CG2 . VAL A 425 ? 1.1362 1.1668 2.0717 -0.0229 -0.0839 -0.1560 425 VAL A CG2 
3234 N N   . LEU A 426 ? 1.3425 1.4021 2.2968 -0.0196 -0.1120 -0.1389 426 LEU A N   
3235 C CA  . LEU A 426 ? 1.2175 1.2980 2.1820 -0.0150 -0.1184 -0.1342 426 LEU A CA  
3236 C C   . LEU A 426 ? 1.1623 1.2686 2.1509 -0.0211 -0.1195 -0.1264 426 LEU A C   
3237 O O   . LEU A 426 ? 1.2051 1.3369 2.2063 -0.0183 -0.1209 -0.1223 426 LEU A O   
3238 C CB  . LEU A 426 ? 1.1663 1.2326 2.1206 -0.0143 -0.1273 -0.1368 426 LEU A CB  
3239 C CG  . LEU A 426 ? 1.1238 1.1643 2.0503 -0.0077 -0.1281 -0.1436 426 LEU A CG  
3240 C CD1 . LEU A 426 ? 1.0151 1.0286 1.9235 -0.0112 -0.1349 -0.1473 426 LEU A CD1 
3241 C CD2 . LEU A 426 ? 1.5074 1.5658 2.4383 0.0035  -0.1331 -0.1428 426 LEU A CD2 
3242 N N   . GLY A 427 ? 1.1192 1.2180 2.1132 -0.0297 -0.1189 -0.1250 427 GLY A N   
3243 C CA  . GLY A 427 ? 1.2990 1.4145 2.3111 -0.0378 -0.1220 -0.1172 427 GLY A CA  
3244 C C   . GLY A 427 ? 1.2658 1.4021 2.2860 -0.0368 -0.1166 -0.1121 427 GLY A C   
3245 O O   . GLY A 427 ? 1.0728 1.2283 2.1059 -0.0433 -0.1186 -0.1047 427 GLY A O   
3246 N N   . ALA A 428 ? 1.0899 1.2210 2.1003 -0.0296 -0.1097 -0.1163 428 ALA A N   
3247 C CA  . ALA A 428 ? 1.1879 1.3345 2.2023 -0.0281 -0.1044 -0.1125 428 ALA A CA  
3248 C C   . ALA A 428 ? 1.2618 1.4339 2.2815 -0.0225 -0.1034 -0.1105 428 ALA A C   
3249 O O   . ALA A 428 ? 1.1791 1.3701 2.2050 -0.0238 -0.0994 -0.1059 428 ALA A O   
3250 C CB  . ALA A 428 ? 1.4051 1.5368 2.4073 -0.0224 -0.0985 -0.1183 428 ALA A CB  
3251 N N   . LEU A 429 ? 1.3235 1.4954 2.3402 -0.0164 -0.1074 -0.1146 429 LEU A N   
3252 C CA  . LEU A 429 ? 1.1441 1.3402 2.1674 -0.0087 -0.1080 -0.1154 429 LEU A CA  
3253 C C   . LEU A 429 ? 1.2969 1.5251 2.3400 -0.0166 -0.1068 -0.1083 429 LEU A C   
3254 O O   . LEU A 429 ? 1.3826 1.6305 2.4292 -0.0140 -0.1004 -0.1071 429 LEU A O   
3255 C CB  . LEU A 429 ? 1.0806 1.2697 2.1000 -0.0030 -0.1163 -0.1203 429 LEU A CB  
3256 C CG  . LEU A 429 ? 1.1519 1.3159 2.1485 0.0080  -0.1169 -0.1280 429 LEU A CG  
3257 C CD1 . LEU A 429 ? 1.2062 1.3617 2.1971 0.0136  -0.1272 -0.1324 429 LEU A CD1 
3258 C CD2 . LEU A 429 ? 1.1379 1.3139 2.1313 0.0184  -0.1116 -0.1302 429 LEU A CD2 
3259 N N   . ASN A 430 ? 1.2535 1.4853 2.3074 -0.0275 -0.1127 -0.1039 430 ASN A N   
3260 C CA  . ASN A 430 ? 1.4630 1.7257 2.5349 -0.0371 -0.1122 -0.0975 430 ASN A CA  
3261 C C   . ASN A 430 ? 1.5085 1.7751 2.5794 -0.0459 -0.1058 -0.0906 430 ASN A C   
3262 O O   . ASN A 430 ? 1.4795 1.7739 2.5599 -0.0514 -0.1009 -0.0866 430 ASN A O   
3263 C CB  . ASN A 430 ? 1.5522 1.8144 2.6337 -0.0474 -0.1211 -0.0942 430 ASN A CB  
3264 C CG  . ASN A 430 ? 1.7947 2.0945 2.8966 -0.0549 -0.1211 -0.0905 430 ASN A CG  
3265 O OD1 . ASN A 430 ? 1.8550 2.1710 2.9622 -0.0657 -0.1156 -0.0839 430 ASN A OD1 
3266 N ND2 . ASN A 430 ? 1.9965 2.3102 3.1094 -0.0506 -0.1276 -0.0948 430 ASN A ND2 
3267 N N   . ALA A 431 ? 1.6055 1.8439 2.6642 -0.0472 -0.1059 -0.0902 431 ALA A N   
3268 C CA  . ALA A 431 ? 1.6574 1.8909 2.7140 -0.0576 -0.1046 -0.0832 431 ALA A CA  
3269 C C   . ALA A 431 ? 1.6650 1.8990 2.7125 -0.0513 -0.0968 -0.0842 431 ALA A C   
3270 O O   . ALA A 431 ? 1.7988 2.0448 2.8466 -0.0585 -0.0934 -0.0780 431 ALA A O   
3271 C CB  . ALA A 431 ? 1.9065 2.1104 2.9582 -0.0628 -0.1116 -0.0831 431 ALA A CB  
3272 N N   . CYS A 432 ? 1.5822 1.8015 2.6199 -0.0390 -0.0944 -0.0917 432 CYS A N   
3273 C CA  . CYS A 432 ? 1.4089 1.6256 2.4369 -0.0330 -0.0882 -0.0931 432 CYS A CA  
3274 C C   . CYS A 432 ? 1.2576 1.4860 2.2816 -0.0196 -0.0834 -0.0993 432 CYS A C   
3275 O O   . CYS A 432 ? 1.2304 1.4595 2.2460 -0.0135 -0.0781 -0.1007 432 CYS A O   
3276 C CB  . CYS A 432 ? 1.5563 1.7442 2.5755 -0.0322 -0.0899 -0.0963 432 CYS A CB  
3277 S SG  . CYS A 432 ? 1.9259 2.1025 2.9474 -0.0453 -0.0956 -0.0889 432 CYS A SG  
3278 N N   . GLY A 433 ? 1.1736 1.4102 2.2029 -0.0145 -0.0865 -0.1031 433 GLY A N   
3279 C CA  . GLY A 433 ? 1.2872 1.5292 2.3108 0.0000  -0.0850 -0.1103 433 GLY A CA  
3280 C C   . GLY A 433 ? 1.3490 1.5613 2.3533 0.0075  -0.0842 -0.1159 433 GLY A C   
3281 O O   . GLY A 433 ? 1.6083 1.8206 2.6030 0.0164  -0.0801 -0.1191 433 GLY A O   
3282 N N   . PHE A 434 ? 1.1228 1.3103 2.1217 0.0029  -0.0878 -0.1173 434 PHE A N   
3283 C CA  . PHE A 434 ? 0.9842 1.1438 1.9661 0.0063  -0.0863 -0.1230 434 PHE A CA  
3284 C C   . PHE A 434 ? 0.8453 0.9850 1.8176 0.0077  -0.0913 -0.1283 434 PHE A C   
3285 O O   . PHE A 434 ? 1.0098 1.1491 1.9895 0.0019  -0.0962 -0.1268 434 PHE A O   
3286 C CB  . PHE A 434 ? 0.9426 1.0903 1.9257 -0.0017 -0.0841 -0.1212 434 PHE A CB  
3287 C CG  . PHE A 434 ? 0.9326 1.0540 1.9014 -0.0003 -0.0821 -0.1285 434 PHE A CG  
3288 C CD1 . PHE A 434 ? 1.0944 1.2094 2.0518 0.0051  -0.0777 -0.1315 434 PHE A CD1 
3289 C CD2 . PHE A 434 ? 0.8728 0.9765 1.8388 -0.0052 -0.0841 -0.1327 434 PHE A CD2 
3290 C CE1 . PHE A 434 ? 1.1816 1.2743 2.1261 0.0046  -0.0752 -0.1385 434 PHE A CE1 
3291 C CE2 . PHE A 434 ? 0.9940 1.0762 1.9468 -0.0056 -0.0805 -0.1402 434 PHE A CE2 
3292 C CZ  . PHE A 434 ? 1.1232 1.2005 2.0658 -0.0012 -0.0760 -0.1430 434 PHE A CZ  
3293 N N   . VAL A 435 ? 0.6647 0.7843 1.6176 0.0143  -0.0903 -0.1345 435 VAL A N   
3294 C CA  . VAL A 435 ? 0.6704 0.7651 1.6082 0.0135  -0.0941 -0.1396 435 VAL A CA  
3295 C C   . VAL A 435 ? 0.7843 0.8534 1.6990 0.0156  -0.0901 -0.1456 435 VAL A C   
3296 O O   . VAL A 435 ? 0.7301 0.7997 1.6365 0.0223  -0.0874 -0.1467 435 VAL A O   
3297 C CB  . VAL A 435 ? 0.6319 0.7313 1.5688 0.0201  -0.1024 -0.1406 435 VAL A CB  
3298 C CG1 . VAL A 435 ? 0.7052 0.8127 1.6356 0.0335  -0.1040 -0.1433 435 VAL A CG1 
3299 C CG2 . VAL A 435 ? 0.6108 0.6817 1.5301 0.0175  -0.1076 -0.1450 435 VAL A CG2 
3300 N N   . GLU A 436 ? 0.9562 1.0015 1.8588 0.0086  -0.0894 -0.1499 436 GLU A N   
3301 C CA  . GLU A 436 ? 1.1535 1.1700 2.0289 0.0083  -0.0871 -0.1564 436 GLU A CA  
3302 C C   . GLU A 436 ? 1.0600 1.0592 1.9148 0.0138  -0.0953 -0.1587 436 GLU A C   
3303 O O   . GLU A 436 ? 0.9925 0.9927 1.8517 0.0129  -0.1017 -0.1575 436 GLU A O   
3304 C CB  . GLU A 436 ? 1.4042 1.4046 2.2757 -0.0032 -0.0807 -0.1613 436 GLU A CB  
3305 C CG  . GLU A 436 ? 1.4598 1.4759 2.3535 -0.0079 -0.0753 -0.1602 436 GLU A CG  
3306 C CD  . GLU A 436 ? 1.4054 1.4074 2.2950 -0.0168 -0.0681 -0.1681 436 GLU A CD  
3307 O OE1 . GLU A 436 ? 1.3820 1.3668 2.2592 -0.0228 -0.0670 -0.1732 436 GLU A OE1 
3308 O OE2 . GLU A 436 ? 1.2236 1.2315 2.1215 -0.0180 -0.0635 -0.1699 436 GLU A OE2 
3309 N N   . LEU A 437 ? 1.0905 1.0708 1.9206 0.0196  -0.0964 -0.1622 437 LEU A N   
3310 C CA  . LEU A 437 ? 1.2518 1.2056 2.0544 0.0239  -0.1052 -0.1656 437 LEU A CA  
3311 C C   . LEU A 437 ? 1.1988 1.1167 1.9672 0.0177  -0.1014 -0.1707 437 LEU A C   
3312 O O   . LEU A 437 ? 1.1895 1.1048 1.9521 0.0171  -0.0952 -0.1720 437 LEU A O   
3313 C CB  . LEU A 437 ? 1.5120 1.4760 2.3157 0.0394  -0.1160 -0.1651 437 LEU A CB  
3314 C CG  . LEU A 437 ? 1.4599 1.4228 2.2527 0.0507  -0.1166 -0.1670 437 LEU A CG  
3315 C CD1 . LEU A 437 ? 1.6870 1.6079 2.4388 0.0534  -0.1236 -0.1720 437 LEU A CD1 
3316 C CD2 . LEU A 437 ? 1.1357 1.1315 1.9507 0.0648  -0.1222 -0.1659 437 LEU A CD2 
3317 N N   . THR A 438 ? 1.1479 1.0361 1.8910 0.0124  -0.1060 -0.1737 438 THR A N   
3318 C CA  . THR A 438 ? 1.3002 1.1493 2.0046 0.0042  -0.1037 -0.1787 438 THR A CA  
3319 C C   . THR A 438 ? 1.3021 1.1197 1.9733 0.0108  -0.1179 -0.1800 438 THR A C   
3320 O O   . THR A 438 ? 1.4407 1.2571 2.1140 0.0135  -0.1268 -0.1791 438 THR A O   
3321 C CB  . THR A 438 ? 1.3774 1.2168 2.0790 -0.0128 -0.0932 -0.1822 438 THR A CB  
3322 O OG1 . THR A 438 ? 1.3472 1.2121 2.0761 -0.0166 -0.0821 -0.1823 438 THR A OG1 
3323 C CG2 . THR A 438 ? 1.4165 1.2138 2.0744 -0.0239 -0.0907 -0.1876 438 THR A CG2 
3324 N N   . ALA A 439 ? 1.3302 1.1194 1.9687 0.0127  -0.1207 -0.1825 439 ALA A N   
3325 C CA  . ALA A 439 ? 1.3505 1.1057 1.9535 0.0212  -0.1364 -0.1842 439 ALA A CA  
3326 C C   . ALA A 439 ? 1.5245 1.2303 2.0783 0.0070  -0.1344 -0.1877 439 ALA A C   
3327 O O   . ALA A 439 ? 1.4809 1.1802 2.0254 -0.0019 -0.1237 -0.1893 439 ALA A O   
3328 C CB  . ALA A 439 ? 1.5089 1.2772 2.1186 0.0399  -0.1444 -0.1840 439 ALA A CB  
3329 N N   . LEU A 440 ? 1.6097 1.2808 2.1320 0.0041  -0.1450 -0.1891 440 LEU A N   
3330 C CA  . LEU A 440 ? 1.7632 1.3840 2.2346 -0.0121 -0.1435 -0.1921 440 LEU A CA  
3331 C C   . LEU A 440 ? 1.8241 1.3991 2.2500 -0.0030 -0.1641 -0.1929 440 LEU A C   
3332 O O   . LEU A 440 ? 1.7282 1.3023 2.1572 0.0093  -0.1797 -0.1924 440 LEU A O   
3333 C CB  . LEU A 440 ? 1.6341 1.2496 2.1040 -0.0273 -0.1367 -0.1933 440 LEU A CB  
3334 C CG  . LEU A 440 ? 1.5811 1.2297 2.0849 -0.0400 -0.1163 -0.1947 440 LEU A CG  
3335 C CD1 . LEU A 440 ? 1.4951 1.1933 2.0529 -0.0283 -0.1165 -0.1910 440 LEU A CD1 
3336 C CD2 . LEU A 440 ? 1.4952 1.1165 1.9724 -0.0593 -0.1090 -0.1989 440 LEU A CD2 
3337 N N   . ALA A 441 ? 1.9416 1.4799 2.3269 -0.0094 -0.1644 -0.1946 441 ALA A N   
3338 C CA  . ALA A 441 ? 2.0584 1.5447 2.3927 -0.0029 -0.1846 -0.1957 441 ALA A CA  
3339 C C   . ALA A 441 ? 2.1626 1.5945 2.4388 -0.0243 -0.1804 -0.1973 441 ALA A C   
3340 O O   . ALA A 441 ? 2.1877 1.6226 2.4621 -0.0449 -0.1605 -0.1985 441 ALA A O   
3341 C CB  . ALA A 441 ? 2.2933 1.7912 2.6384 0.0209  -0.1979 -0.1961 441 ALA A CB  
3342 N N   . ARG A 442 ? 2.3121 1.6915 2.5379 -0.0184 -0.2013 -0.1980 442 ARG A N   
3343 C CA  . ARG A 442 ? 2.4370 1.7534 2.5965 -0.0376 -0.2033 -0.1989 442 ARG A CA  
3344 C C   . ARG A 442 ? 2.2787 1.5905 2.4282 -0.0428 -0.1954 -0.1993 442 ARG A C   
3345 O O   . ARG A 442 ? 2.2174 1.4959 2.3280 -0.0668 -0.1852 -0.2001 442 ARG A O   
3346 C CB  . ARG A 442 ? 2.5965 1.8587 2.7077 -0.0271 -0.2314 -0.1992 442 ARG A CB  
3347 C CG  . ARG A 442 ? 2.6708 1.9287 2.7826 -0.0280 -0.2381 -0.1991 442 ARG A CG  
3348 C CD  . ARG A 442 ? 2.8446 2.0565 2.9063 -0.0568 -0.2301 -0.1993 442 ARG A CD  
3349 N NE  . ARG A 442 ? 3.3553 2.5899 3.4312 -0.0817 -0.2000 -0.2004 442 ARG A NE  
3350 C CZ  . ARG A 442 ? 3.8396 3.0830 3.9219 -0.0982 -0.1855 -0.2019 442 ARG A CZ  
3351 N NH1 . ARG A 442 ? 3.9919 3.2236 4.0682 -0.0928 -0.1982 -0.2013 442 ARG A NH1 
3352 N NH2 . ARG A 442 ? 4.0664 3.3307 4.1619 -0.1193 -0.1591 -0.2047 442 ARG A NH2 
3353 N N   . SER A 443 ? 2.2211 1.5668 2.4056 -0.0209 -0.1999 -0.1990 443 SER A N   
3354 C CA  . SER A 443 ? 2.3469 1.6951 2.5294 -0.0229 -0.1929 -0.1992 443 SER A CA  
3355 C C   . SER A 443 ? 2.1352 1.5518 2.3848 -0.0122 -0.1791 -0.1984 443 SER A C   
3356 O O   . SER A 443 ? 1.9700 1.4239 2.2598 0.0041  -0.1831 -0.1977 443 SER A O   
3357 C CB  . SER A 443 ? 2.4469 1.7560 2.5925 -0.0058 -0.2159 -0.2002 443 SER A CB  
3358 O OG  . SER A 443 ? 2.6301 1.9734 2.8133 0.0244  -0.2290 -0.2013 443 SER A OG  
3359 N N   . PRO A 444 ? 1.9728 1.4067 2.2354 -0.0213 -0.1637 -0.1986 444 PRO A N   
3360 C CA  . PRO A 444 ? 2.0075 1.5027 2.3304 -0.0131 -0.1509 -0.1976 444 PRO A CA  
3361 C C   . PRO A 444 ? 1.9085 1.4276 2.2552 0.0155  -0.1642 -0.1970 444 PRO A C   
3362 O O   . PRO A 444 ? 1.9403 1.5086 2.3363 0.0262  -0.1595 -0.1955 444 PRO A O   
3363 C CB  . PRO A 444 ? 1.8716 1.3714 2.1952 -0.0297 -0.1346 -0.1987 444 PRO A CB  
3364 C CG  . PRO A 444 ? 1.9552 1.3947 2.2162 -0.0485 -0.1380 -0.2003 444 PRO A CG  
3365 C CD  . PRO A 444 ? 1.9457 1.3403 2.1649 -0.0398 -0.1593 -0.1998 444 PRO A CD  
3366 N N   . GLU A 445 ? 1.8976 1.3796 2.2071 0.0273  -0.1813 -0.1986 445 GLU A N   
3367 C CA  . GLU A 445 ? 2.1538 1.6532 2.4798 0.0557  -0.1957 -0.2002 445 GLU A CA  
3368 C C   . GLU A 445 ? 2.0612 1.5843 2.4139 0.0703  -0.2048 -0.2006 445 GLU A C   
3369 O O   . GLU A 445 ? 2.1128 1.6845 2.5111 0.0870  -0.2036 -0.2008 445 GLU A O   
3370 C CB  . GLU A 445 ? 2.3933 1.8362 2.6638 0.0615  -0.2135 -0.2028 445 GLU A CB  
3371 C CG  . GLU A 445 ? 2.7741 2.1904 3.0153 0.0415  -0.2033 -0.2019 445 GLU A CG  
3372 C CD  . GLU A 445 ? 3.3270 2.6715 3.4984 0.0278  -0.2148 -0.2026 445 GLU A CD  
3373 O OE1 . GLU A 445 ? 3.3784 2.6895 3.5197 0.0187  -0.2217 -0.2024 445 GLU A OE1 
3374 O OE2 . GLU A 445 ? 3.6132 2.9335 3.7584 0.0242  -0.2163 -0.2031 445 GLU A OE2 
3375 N N   . ALA A 446 ? 1.9567 1.4437 2.2786 0.0623  -0.2136 -0.2008 446 ALA A N   
3376 C CA  . ALA A 446 ? 1.8993 1.4013 2.2403 0.0740  -0.2244 -0.2015 446 ALA A CA  
3377 C C   . ALA A 446 ? 1.8571 1.4184 2.2559 0.0699  -0.2072 -0.1984 446 ALA A C   
3378 O O   . ALA A 446 ? 1.6046 1.2052 2.0422 0.0865  -0.2122 -0.1990 446 ALA A O   
3379 C CB  . ALA A 446 ? 1.8742 1.3225 2.1675 0.0631  -0.2360 -0.2018 446 ALA A CB  
3380 N N   . ALA A 447 ? 1.8957 1.4620 2.2987 0.0474  -0.1876 -0.1959 447 ALA A N   
3381 C CA  . ALA A 447 ? 1.8352 1.4511 2.2878 0.0410  -0.1713 -0.1932 447 ALA A CA  
3382 C C   . ALA A 447 ? 1.7617 1.4284 2.2602 0.0564  -0.1669 -0.1921 447 ALA A C   
3383 O O   . ALA A 447 ? 1.7203 1.4286 2.2602 0.0637  -0.1653 -0.1903 447 ALA A O   
3384 C CB  . ALA A 447 ? 1.9095 1.5185 2.3551 0.0160  -0.1524 -0.1929 447 ALA A CB  
3385 N N   . ASP A 448 ? 1.6295 1.2896 2.1169 0.0598  -0.1651 -0.1930 448 ASP A N   
3386 C CA  . ASP A 448 ? 1.6301 1.3318 2.1528 0.0732  -0.1606 -0.1923 448 ASP A CA  
3387 C C   . ASP A 448 ? 1.6218 1.3465 2.1644 0.0966  -0.1742 -0.1943 448 ASP A C   
3388 O O   . ASP A 448 ? 1.5526 1.3255 2.1388 0.1037  -0.1683 -0.1927 448 ASP A O   
3389 C CB  . ASP A 448 ? 1.6783 1.3598 2.1770 0.0742  -0.1599 -0.1939 448 ASP A CB  
3390 C CG  . ASP A 448 ? 1.7968 1.4732 2.2912 0.0531  -0.1436 -0.1925 448 ASP A CG  
3391 O OD1 . ASP A 448 ? 1.8930 1.5330 2.3544 0.0355  -0.1415 -0.1935 448 ASP A OD1 
3392 O OD2 . ASP A 448 ? 1.9113 1.6206 2.4353 0.0539  -0.1332 -0.1910 448 ASP A OD2 
3393 N N   . GLY A 449 ? 1.6333 1.3214 2.1419 0.1075  -0.1929 -0.1985 449 GLY A N   
3394 C CA  . GLY A 449 ? 1.7126 1.4174 2.2360 0.1310  -0.2088 -0.2028 449 GLY A CA  
3395 C C   . GLY A 449 ? 1.5547 1.2956 2.1160 0.1302  -0.2069 -0.2008 449 GLY A C   
3396 O O   . GLY A 449 ? 1.5588 1.3451 2.1593 0.1436  -0.2072 -0.2022 449 GLY A O   
3397 N N   . TYR A 450 ? 1.4138 1.1331 1.9611 0.1131  -0.2047 -0.1979 450 TYR A N   
3398 C CA  . TYR A 450 ? 1.3984 1.1438 1.9752 0.1093  -0.2035 -0.1956 450 TYR A CA  
3399 C C   . TYR A 450 ? 1.2486 1.0497 1.8757 0.1057  -0.1866 -0.1914 450 TYR A C   
3400 O O   . TYR A 450 ? 1.1202 0.9602 1.7836 0.1136  -0.1888 -0.1910 450 TYR A O   
3401 C CB  . TYR A 450 ? 1.4974 1.2081 2.0474 0.0883  -0.1996 -0.1933 450 TYR A CB  
3402 C CG  . TYR A 450 ? 1.8477 1.5228 2.3689 0.0937  -0.2197 -0.1962 450 TYR A CG  
3403 C CD1 . TYR A 450 ? 1.9217 1.6163 2.4628 0.1139  -0.2362 -0.1996 450 TYR A CD1 
3404 C CD2 . TYR A 450 ? 2.0486 1.6711 2.5226 0.0781  -0.2223 -0.1961 450 TYR A CD2 
3405 C CE1 . TYR A 450 ? 2.1586 1.8193 2.6734 0.1198  -0.2568 -0.2028 450 TYR A CE1 
3406 C CE2 . TYR A 450 ? 2.3229 1.9091 2.7671 0.0826  -0.2420 -0.1984 450 TYR A CE2 
3407 C CZ  . TYR A 450 ? 2.3282 1.9328 2.7930 0.1042  -0.2602 -0.2017 450 TYR A CZ  
3408 O OH  . TYR A 450 ? 2.3275 1.8952 2.7633 0.1097  -0.2817 -0.2046 450 TYR A OH  
3409 N N   . SER A 451 ? 1.1878 0.9904 1.8148 0.0930  -0.1707 -0.1885 451 SER A N   
3410 C CA  . SER A 451 ? 1.1770 1.0247 1.8451 0.0879  -0.1552 -0.1842 451 SER A CA  
3411 C C   . SER A 451 ? 1.0935 0.9808 1.7906 0.1057  -0.1575 -0.1853 451 SER A C   
3412 O O   . SER A 451 ? 0.9976 0.9269 1.7329 0.1066  -0.1527 -0.1825 451 SER A O   
3413 C CB  . SER A 451 ? 1.3635 1.1991 2.0200 0.0744  -0.1416 -0.1830 451 SER A CB  
3414 O OG  . SER A 451 ? 1.5279 1.4019 2.2181 0.0733  -0.1295 -0.1797 451 SER A OG  
3415 N N   . ARG A 452 ? 1.2741 1.1453 1.9500 0.1191  -0.1649 -0.1898 452 ARG A N   
3416 C CA  . ARG A 452 ? 1.3825 1.2870 2.0800 0.1373  -0.1670 -0.1930 452 ARG A CA  
3417 C C   . ARG A 452 ? 1.1690 1.1023 1.8926 0.1494  -0.1768 -0.1959 452 ARG A C   
3418 O O   . ARG A 452 ? 0.9344 0.9147 1.6951 0.1543  -0.1708 -0.1954 452 ARG A O   
3419 C CB  . ARG A 452 ? 1.5726 1.4491 2.2386 0.1476  -0.1724 -0.1975 452 ARG A CB  
3420 C CG  . ARG A 452 ? 1.6760 1.5810 2.3576 0.1589  -0.1663 -0.1992 452 ARG A CG  
3421 C CD  . ARG A 452 ? 2.0225 1.8960 2.6730 0.1552  -0.1631 -0.1992 452 ARG A CD  
3422 N NE  . ARG A 452 ? 2.2628 2.0813 2.8658 0.1571  -0.1767 -0.2031 452 ARG A NE  
3423 C CZ  . ARG A 452 ? 2.2572 2.0350 2.8272 0.1404  -0.1739 -0.2006 452 ARG A CZ  
3424 N NH1 . ARG A 452 ? 2.3582 2.1456 2.9405 0.1207  -0.1580 -0.1952 452 ARG A NH1 
3425 N NH2 . ARG A 452 ? 2.1040 1.8311 2.6284 0.1428  -0.1875 -0.2042 452 ARG A NH2 
3426 N N   . ALA A 453 ? 1.0616 0.9647 1.7639 0.1527  -0.1920 -0.1992 453 ALA A N   
3427 C CA  . ALA A 453 ? 1.1543 1.0777 1.8770 0.1640  -0.2046 -0.2031 453 ALA A CA  
3428 C C   . ALA A 453 ? 1.1784 1.1429 1.9413 0.1521  -0.1939 -0.1971 453 ALA A C   
3429 O O   . ALA A 453 ? 1.3201 1.3290 2.1191 0.1604  -0.1947 -0.1991 453 ALA A O   
3430 C CB  . ALA A 453 ? 1.1580 1.0320 1.8440 0.1634  -0.2214 -0.2055 453 ALA A CB  
3431 N N   . ALA A 454 ? 1.1943 1.1425 1.9492 0.1321  -0.1843 -0.1905 454 ALA A N   
3432 C CA  . ALA A 454 ? 1.2275 1.2055 2.0142 0.1188  -0.1750 -0.1843 454 ALA A CA  
3433 C C   . ALA A 454 ? 1.1850 1.2116 2.0080 0.1196  -0.1623 -0.1813 454 ALA A C   
3434 O O   . ALA A 454 ? 1.0477 1.1127 1.9045 0.1189  -0.1612 -0.1795 454 ALA A O   
3435 C CB  . ALA A 454 ? 1.4611 1.4101 2.2295 0.0992  -0.1668 -0.1798 454 ALA A CB  
3436 N N   . GLN A 455 ? 1.2647 1.2866 2.0778 0.1198  -0.1535 -0.1809 455 GLN A N   
3437 C CA  . GLN A 455 ? 1.2963 1.3569 2.1360 0.1198  -0.1414 -0.1779 455 GLN A CA  
3438 C C   . GLN A 455 ? 1.2741 1.3732 2.1383 0.1356  -0.1462 -0.1829 455 GLN A C   
3439 O O   . GLN A 455 ? 1.1879 1.3283 2.0841 0.1316  -0.1387 -0.1797 455 GLN A O   
3440 C CB  . GLN A 455 ? 1.2461 1.2918 2.0677 0.1194  -0.1335 -0.1777 455 GLN A CB  
3441 C CG  . GLN A 455 ? 1.4975 1.5123 2.3007 0.1026  -0.1269 -0.1739 455 GLN A CG  
3442 C CD  . GLN A 455 ? 1.7169 1.7075 2.4950 0.1028  -0.1230 -0.1754 455 GLN A CD  
3443 O OE1 . GLN A 455 ? 2.0237 2.0328 2.8126 0.1039  -0.1150 -0.1737 455 GLN A OE1 
3444 N NE2 . GLN A 455 ? 1.5316 1.4794 2.2746 0.1001  -0.1287 -0.1785 455 GLN A NE2 
3445 N N   . ALA A 456 ? 1.2961 1.3796 2.1430 0.1530  -0.1592 -0.1914 456 ALA A N   
3446 C CA  . ALA A 456 ? 1.3614 1.4792 2.2296 0.1712  -0.1656 -0.1994 456 ALA A CA  
3447 C C   . ALA A 456 ? 1.3738 1.5247 2.2747 0.1680  -0.1690 -0.1988 456 ALA A C   
3448 O O   . ALA A 456 ? 1.5081 1.7072 2.4428 0.1707  -0.1633 -0.2004 456 ALA A O   
3449 C CB  . ALA A 456 ? 1.5434 1.6304 2.3836 0.1905  -0.1823 -0.2091 456 ALA A CB  
3450 N N   . LEU A 457 ? 1.2678 1.3909 2.1564 0.1609  -0.1781 -0.1968 457 LEU A N   
3451 C CA  . LEU A 457 ? 1.1259 1.2718 2.0403 0.1572  -0.1841 -0.1962 457 LEU A CA  
3452 C C   . LEU A 457 ? 1.1967 1.3809 2.1429 0.1405  -0.1684 -0.1876 457 LEU A C   
3453 O O   . LEU A 457 ? 1.0874 1.3143 2.0672 0.1411  -0.1683 -0.1888 457 LEU A O   
3454 C CB  . LEU A 457 ? 0.9694 1.0714 1.8579 0.1516  -0.1962 -0.1951 457 LEU A CB  
3455 C CG  . LEU A 457 ? 0.9330 1.0523 1.8441 0.1477  -0.2047 -0.1946 457 LEU A CG  
3456 C CD1 . LEU A 457 ? 1.0029 1.1676 1.9480 0.1628  -0.2124 -0.2027 457 LEU A CD1 
3457 C CD2 . LEU A 457 ? 0.9488 1.0185 1.8267 0.1473  -0.2201 -0.1962 457 LEU A CD2 
3458 N N   . LEU A 458 ? 1.2647 1.4321 2.1992 0.1257  -0.1563 -0.1796 458 LEU A N   
3459 C CA  . LEU A 458 ? 1.2464 1.4383 2.2046 0.1085  -0.1451 -0.1708 458 LEU A CA  
3460 C C   . LEU A 458 ? 1.3243 1.5552 2.3034 0.1089  -0.1329 -0.1693 458 LEU A C   
3461 O O   . LEU A 458 ? 1.4665 1.7290 2.4713 0.0983  -0.1269 -0.1642 458 LEU A O   
3462 C CB  . LEU A 458 ? 1.2857 1.4458 2.2279 0.0920  -0.1402 -0.1639 458 LEU A CB  
3463 C CG  . LEU A 458 ? 1.2982 1.4220 2.2195 0.0905  -0.1517 -0.1660 458 LEU A CG  
3464 C CD1 . LEU A 458 ? 1.2953 1.3823 2.1924 0.0779  -0.1456 -0.1628 458 LEU A CD1 
3465 C CD2 . LEU A 458 ? 1.2314 1.3723 2.1739 0.0862  -0.1594 -0.1647 458 LEU A CD2 
3466 N N   . THR A 459 ? 1.4252 1.6524 2.3913 0.1201  -0.1296 -0.1736 459 THR A N   
3467 C CA  . THR A 459 ? 1.6913 1.9505 2.6717 0.1195  -0.1171 -0.1720 459 THR A CA  
3468 C C   . THR A 459 ? 1.8640 2.1580 2.8608 0.1365  -0.1200 -0.1818 459 THR A C   
3469 O O   . THR A 459 ? 2.2915 2.5945 3.2837 0.1459  -0.1144 -0.1859 459 THR A O   
3470 C CB  . THR A 459 ? 1.8522 2.0859 2.8084 0.1189  -0.1100 -0.1700 459 THR A CB  
3471 O OG1 . THR A 459 ? 1.9107 2.1141 2.8408 0.1340  -0.1198 -0.1778 459 THR A OG1 
3472 C CG2 . THR A 459 ? 2.1080 2.3161 3.0544 0.1015  -0.1050 -0.1615 459 THR A CG2 
3473 N N   . GLY A 460 ? 1.7589 2.0727 2.7753 0.1410  -0.1292 -0.1866 460 GLY A N   
3474 C CA  . GLY A 460 ? 2.0349 2.3903 3.0751 0.1558  -0.1318 -0.1971 460 GLY A CA  
3475 C C   . GLY A 460 ? 2.3422 2.7344 3.4162 0.1471  -0.1335 -0.1962 460 GLY A C   
3476 O O   . GLY A 460 ? 2.6252 3.0024 3.6987 0.1323  -0.1359 -0.1880 460 GLY A O   
3477 N N   . PRO A 461 ? 2.3009 2.7440 3.4061 0.1542  -0.1313 -0.2045 461 PRO A N   
3478 C CA  . PRO A 461 ? 2.1303 2.6071 3.2677 0.1481  -0.1365 -0.2060 461 PRO A CA  
3479 C C   . PRO A 461 ? 1.9039 2.3651 3.0396 0.1646  -0.1577 -0.2158 461 PRO A C   
3480 O O   . PRO A 461 ? 1.5076 1.9302 2.6149 0.1804  -0.1683 -0.2212 461 PRO A O   
3481 C CB  . PRO A 461 ? 2.1185 2.6557 3.2875 0.1490  -0.1240 -0.2123 461 PRO A CB  
3482 C CG  . PRO A 461 ? 2.1293 2.6568 3.2780 0.1494  -0.1102 -0.2093 461 PRO A CG  
3483 C CD  . PRO A 461 ? 2.2186 2.6926 3.3314 0.1655  -0.1218 -0.2125 461 PRO A CD  
3484 N N   . TYR A 462 ? 1.8810 2.3699 3.0453 0.1597  -0.1646 -0.2176 462 TYR A N   
3485 C CA  . TYR A 462 ? 1.8497 2.3168 3.0100 0.1699  -0.1860 -0.2235 462 TYR A CA  
3486 C C   . TYR A 462 ? 1.6495 2.1678 2.8532 0.1685  -0.1917 -0.2299 462 TYR A C   
3487 O O   . TYR A 462 ? 1.2791 1.7932 2.4890 0.1816  -0.2115 -0.2391 462 TYR A O   
3488 C CB  . TYR A 462 ? 1.7206 2.1364 2.8516 0.1536  -0.1877 -0.2103 462 TYR A CB  
3489 C CG  . TYR A 462 ? 1.7595 2.1313 2.8682 0.1616  -0.2086 -0.2134 462 TYR A CG  
3490 C CD1 . TYR A 462 ? 1.7526 2.1364 2.8808 0.1595  -0.2219 -0.2156 462 TYR A CD1 
3491 C CD2 . TYR A 462 ? 1.6833 1.9993 2.7491 0.1692  -0.2150 -0.2135 462 TYR A CD2 
3492 C CE1 . TYR A 462 ? 1.6416 1.9821 2.7461 0.1661  -0.2417 -0.2182 462 TYR A CE1 
3493 C CE2 . TYR A 462 ? 1.6115 1.8837 2.6522 0.1743  -0.2337 -0.2158 462 TYR A CE2 
3494 C CZ  . TYR A 462 ? 1.5446 1.8282 2.6039 0.1731  -0.2473 -0.2181 462 TYR A CZ  
3495 O OH  . TYR A 462 ? 1.2706 1.5070 2.3010 0.1775  -0.2661 -0.2199 462 TYR A OH  
3496 N N   . GLY B 5   ? 1.6915 2.6650 2.4472 0.1183  -0.0234 0.4481  5   GLY B N   
3497 C CA  . GLY B 5   ? 1.6664 2.5891 2.4539 0.0848  -0.0343 0.4423  5   GLY B CA  
3498 C C   . GLY B 5   ? 1.7624 2.6827 2.5596 0.0878  -0.0286 0.4326  5   GLY B C   
3499 O O   . GLY B 5   ? 1.9434 2.9237 2.7461 0.0908  -0.0206 0.4491  5   GLY B O   
3500 N N   . SER B 6   ? 1.6420 2.4928 2.4416 0.0868  -0.0332 0.4065  6   SER B N   
3501 C CA  . SER B 6   ? 1.6343 2.4691 2.4453 0.0842  -0.0304 0.3957  6   SER B CA  
3502 C C   . SER B 6   ? 1.6392 2.4160 2.4755 0.0540  -0.0411 0.3887  6   SER B C   
3503 O O   . SER B 6   ? 1.8884 2.6139 2.7258 0.0481  -0.0489 0.3770  6   SER B O   
3504 C CB  . SER B 6   ? 1.6578 2.4658 2.4418 0.1185  -0.0237 0.3690  6   SER B CB  
3505 O OG  . SER B 6   ? 1.8576 2.7010 2.6094 0.1520  -0.0164 0.3695  6   SER B OG  
3506 N N   . THR B 7   ? 1.5147 2.2978 2.3697 0.0376  -0.0411 0.3940  7   THR B N   
3507 C CA  . THR B 7   ? 1.3987 2.1248 2.2719 0.0164  -0.0487 0.3830  7   THR B CA  
3508 C C   . THR B 7   ? 1.4320 2.1448 2.3025 0.0272  -0.0418 0.3675  7   THR B C   
3509 O O   . THR B 7   ? 2.1095 2.8678 2.9807 0.0304  -0.0363 0.3786  7   THR B O   
3510 C CB  . THR B 7   ? 1.2380 1.9718 2.1350 -0.0195 -0.0605 0.4055  7   THR B CB  
3511 O OG1 . THR B 7   ? 1.0240 1.7527 1.9202 -0.0261 -0.0675 0.4126  7   THR B OG1 
3512 C CG2 . THR B 7   ? 1.0718 1.7481 1.9831 -0.0380 -0.0679 0.3940  7   THR B CG2 
3513 N N   . LYS B 8   ? 1.1855 1.8367 2.0532 0.0329  -0.0423 0.3428  8   LYS B N   
3514 C CA  . LYS B 8   ? 1.1784 1.8072 2.0422 0.0426  -0.0366 0.3259  8   LYS B CA  
3515 C C   . LYS B 8   ? 1.1668 1.7395 2.0471 0.0231  -0.0422 0.3159  8   LYS B C   
3516 O O   . LYS B 8   ? 1.5343 2.0661 2.4201 0.0171  -0.0476 0.3080  8   LYS B O   
3517 C CB  . LYS B 8   ? 1.2811 1.8913 2.1199 0.0743  -0.0303 0.3042  8   LYS B CB  
3518 C CG  . LYS B 8   ? 1.5572 2.2127 2.3724 0.1000  -0.0253 0.3098  8   LYS B CG  
3519 C CD  . LYS B 8   ? 1.6017 2.2348 2.3858 0.1332  -0.0224 0.2885  8   LYS B CD  
3520 C CE  . LYS B 8   ? 1.5760 2.2479 2.3350 0.1568  -0.0199 0.2954  8   LYS B CE  
3521 N NZ  . LYS B 8   ? 1.5185 2.2643 2.2843 0.1546  -0.0133 0.3201  8   LYS B NZ  
3522 N N   . ILE B 9   ? 1.2107 1.7844 2.0976 0.0144  -0.0409 0.3172  9   ILE B N   
3523 C CA  . ILE B 9   ? 1.3079 1.8345 2.2073 -0.0031 -0.0456 0.3099  9   ILE B CA  
3524 C C   . ILE B 9   ? 1.5629 2.0659 2.4536 0.0106  -0.0377 0.2911  9   ILE B C   
3525 O O   . ILE B 9   ? 1.7386 2.2720 2.6221 0.0190  -0.0327 0.2940  9   ILE B O   
3526 C CB  . ILE B 9   ? 1.3022 1.8492 2.2152 -0.0299 -0.0548 0.3318  9   ILE B CB  
3527 C CG1 . ILE B 9   ? 1.3102 1.8747 2.2319 -0.0462 -0.0647 0.3510  9   ILE B CG1 
3528 C CG2 . ILE B 9   ? 1.2721 1.7714 2.1915 -0.0446 -0.0598 0.3239  9   ILE B CG2 
3529 C CD1 . ILE B 9   ? 1.5875 2.1841 2.5201 -0.0722 -0.0756 0.3776  9   ILE B CD1 
3530 N N   . LEU B 10  ? 1.8619 2.3113 2.7538 0.0131  -0.0369 0.2727  10  LEU B N   
3531 C CA  . LEU B 10  ? 1.8022 2.2262 2.6837 0.0287  -0.0296 0.2537  10  LEU B CA  
3532 C C   . LEU B 10  ? 1.9042 2.2944 2.7937 0.0154  -0.0297 0.2484  10  LEU B C   
3533 O O   . LEU B 10  ? 1.9311 2.2854 2.8314 0.0048  -0.0332 0.2447  10  LEU B O   
3534 C CB  . LEU B 10  ? 1.5788 1.9713 2.4550 0.0422  -0.0289 0.2389  10  LEU B CB  
3535 C CG  . LEU B 10  ? 1.5054 1.9204 2.3710 0.0547  -0.0313 0.2429  10  LEU B CG  
3536 C CD1 . LEU B 10  ? 1.7349 2.1105 2.5968 0.0638  -0.0340 0.2289  10  LEU B CD1 
3537 C CD2 . LEU B 10  ? 1.5772 2.0322 2.4220 0.0751  -0.0264 0.2447  10  LEU B CD2 
3538 N N   . ILE B 11  ? 1.5428 1.9467 2.4259 0.0169  -0.0264 0.2491  11  ILE B N   
3539 C CA  . ILE B 11  ? 1.6355 2.0095 2.5215 0.0055  -0.0269 0.2448  11  ILE B CA  
3540 C C   . ILE B 11  ? 1.4878 1.8580 2.3599 0.0221  -0.0187 0.2316  11  ILE B C   
3541 O O   . ILE B 11  ? 1.8136 2.2199 2.6791 0.0272  -0.0176 0.2386  11  ILE B O   
3542 C CB  . ILE B 11  ? 1.8183 2.2154 2.7103 -0.0145 -0.0355 0.2638  11  ILE B CB  
3543 C CG1 . ILE B 11  ? 1.7152 2.1386 2.6177 -0.0280 -0.0444 0.2826  11  ILE B CG1 
3544 C CG2 . ILE B 11  ? 2.0196 2.3745 2.9119 -0.0282 -0.0395 0.2593  11  ILE B CG2 
3545 C CD1 . ILE B 11  ? 1.8598 2.3122 2.7684 -0.0493 -0.0551 0.3052  11  ILE B CD1 
3546 N N   . TYR B 12  ? 1.1800 1.5113 2.0481 0.0316  -0.0137 0.2144  12  TYR B N   
3547 C CA  . TYR B 12  ? 1.1051 1.4285 1.9582 0.0483  -0.0075 0.2012  12  TYR B CA  
3548 C C   . TYR B 12  ? 1.2525 1.5439 2.1051 0.0407  -0.0046 0.1942  12  TYR B C   
3549 O O   . TYR B 12  ? 1.3039 1.5657 2.1505 0.0487  0.0003  0.1808  12  TYR B O   
3550 C CB  . TYR B 12  ? 1.0296 1.3343 1.8784 0.0618  -0.0067 0.1904  12  TYR B CB  
3551 C CG  . TYR B 12  ? 1.1315 1.4408 1.9596 0.0839  -0.0050 0.1807  12  TYR B CG  
3552 C CD1 . TYR B 12  ? 1.3574 1.6378 2.1755 0.0906  -0.0018 0.1678  12  TYR B CD1 
3553 C CD2 . TYR B 12  ? 1.0845 1.4231 1.9003 0.0989  -0.0075 0.1841  12  TYR B CD2 
3554 C CE1 . TYR B 12  ? 1.5515 1.8297 2.3479 0.1106  -0.0029 0.1585  12  TYR B CE1 
3555 C CE2 . TYR B 12  ? 1.2298 1.5664 2.0219 0.1215  -0.0079 0.1740  12  TYR B CE2 
3556 C CZ  . TYR B 12  ? 1.4773 1.7821 2.2596 0.1268  -0.0065 0.1610  12  TYR B CZ  
3557 O OH  . TYR B 12  ? 1.2258 1.5209 1.9826 0.1481  -0.0093 0.1502  12  TYR B OH  
3558 N N   . ALA B 13  ? 1.5698 1.8672 2.4275 0.0247  -0.0090 0.2047  13  ALA B N   
3559 C CA  . ALA B 13  ? 1.6801 1.9463 2.5341 0.0165  -0.0082 0.1997  13  ALA B CA  
3560 C C   . ALA B 13  ? 1.7021 1.9697 2.5413 0.0273  -0.0030 0.1918  13  ALA B C   
3561 O O   . ALA B 13  ? 1.4339 1.7378 2.2671 0.0350  -0.0036 0.1970  13  ALA B O   
3562 C CB  . ALA B 13  ? 1.7650 2.0377 2.6241 -0.0030 -0.0179 0.2144  13  ALA B CB  
3563 N N   . PHE B 14  ? 1.9532 2.1814 2.7862 0.0287  0.0021  0.1794  14  PHE B N   
3564 C CA  . PHE B 14  ? 2.1069 2.3280 2.9249 0.0360  0.0060  0.1716  14  PHE B CA  
3565 C C   . PHE B 14  ? 2.0486 2.2651 2.8629 0.0218  0.0007  0.1787  14  PHE B C   
3566 O O   . PHE B 14  ? 2.3105 2.4898 3.1209 0.0150  0.0017  0.1736  14  PHE B O   
3567 C CB  . PHE B 14  ? 2.1165 2.3006 2.9274 0.0449  0.0140  0.1562  14  PHE B CB  
3568 C CG  . PHE B 14  ? 2.0853 2.2703 2.8940 0.0597  0.0164  0.1487  14  PHE B CG  
3569 C CD1 . PHE B 14  ? 2.1764 2.3827 2.9924 0.0638  0.0127  0.1535  14  PHE B CD1 
3570 C CD2 . PHE B 14  ? 1.8240 1.9860 2.6209 0.0688  0.0207  0.1373  14  PHE B CD2 
3571 C CE1 . PHE B 14  ? 1.7605 1.9625 2.5705 0.0774  0.0121  0.1465  14  PHE B CE1 
3572 C CE2 . PHE B 14  ? 2.1818 2.3399 2.9743 0.0809  0.0193  0.1314  14  PHE B CE2 
3573 C CZ  . PHE B 14  ? 2.0015 2.1784 2.7996 0.0855  0.0145  0.1356  14  PHE B CZ  
3574 N N   . ASN B 15  ? 1.9394 2.1952 2.7542 0.0182  -0.0054 0.1915  15  ASN B N   
3575 C CA  . ASN B 15  ? 2.0244 2.2835 2.8375 0.0021  -0.0145 0.2028  15  ASN B CA  
3576 C C   . ASN B 15  ? 2.3975 2.6452 3.1951 0.0073  -0.0122 0.1955  15  ASN B C   
3577 O O   . ASN B 15  ? 2.4483 2.6701 3.2377 -0.0040 -0.0175 0.1964  15  ASN B O   
3578 C CB  . ASN B 15  ? 1.8386 2.1485 2.6636 -0.0067 -0.0232 0.2234  15  ASN B CB  
3579 C CG  . ASN B 15  ? 1.8002 2.1537 2.6295 0.0096  -0.0176 0.2254  15  ASN B CG  
3580 O OD1 . ASN B 15  ? 1.9608 2.3196 2.7797 0.0284  -0.0105 0.2148  15  ASN B OD1 
3581 N ND2 . ASN B 15  ? 1.5839 1.9669 2.4257 0.0041  -0.0216 0.2386  15  ASN B ND2 
3582 N N   . TYR B 16  ? 2.7165 2.9795 3.5074 0.0254  -0.0053 0.1875  16  TYR B N   
3583 C CA  . TYR B 16  ? 2.7046 2.9606 3.4803 0.0328  -0.0033 0.1804  16  TYR B CA  
3584 C C   . TYR B 16  ? 2.9402 3.1420 3.7042 0.0337  0.0029  0.1647  16  TYR B C   
3585 O O   . TYR B 16  ? 3.5031 3.6901 4.2524 0.0385  0.0047  0.1575  16  TYR B O   
3586 C CB  . TYR B 16  ? 2.2628 2.5538 3.0342 0.0532  0.0000  0.1780  16  TYR B CB  
3587 C CG  . TYR B 16  ? 2.0507 2.3226 2.8180 0.0680  0.0067  0.1643  16  TYR B CG  
3588 C CD1 . TYR B 16  ? 1.8587 2.1409 2.6373 0.0690  0.0069  0.1674  16  TYR B CD1 
3589 C CD2 . TYR B 16  ? 2.2185 2.4597 2.9704 0.0791  0.0110  0.1493  16  TYR B CD2 
3590 C CE1 . TYR B 16  ? 2.1037 2.3658 2.8785 0.0806  0.0106  0.1561  16  TYR B CE1 
3591 C CE2 . TYR B 16  ? 2.4449 2.6668 3.1931 0.0901  0.0143  0.1388  16  TYR B CE2 
3592 C CZ  . TYR B 16  ? 2.6838 2.9157 3.4437 0.0906  0.0138  0.1422  16  TYR B CZ  
3593 O OH  . TYR B 16  ? 3.7024 3.9133 4.4587 0.0998  0.0148  0.1331  16  TYR B OH  
3594 N N   . ALA B 17  ? 2.7574 2.9314 3.5278 0.0297  0.0064  0.1603  17  ALA B N   
3595 C CA  . ALA B 17  ? 2.5365 2.6635 3.2982 0.0297  0.0131  0.1485  17  ALA B CA  
3596 C C   . ALA B 17  ? 2.6371 2.7387 3.3969 0.0149  0.0075  0.1532  17  ALA B C   
3597 O O   . ALA B 17  ? 2.6727 2.7639 3.4426 0.0102  0.0069  0.1552  17  ALA B O   
3598 C CB  . ALA B 17  ? 2.1070 2.2212 2.8766 0.0385  0.0213  0.1402  17  ALA B CB  
3599 N N   . ASP B 18  ? 2.8402 2.9302 3.5852 0.0082  0.0018  0.1551  18  ASP B N   
3600 C CA  . ASP B 18  ? 2.8921 2.9529 3.6288 -0.0053 -0.0070 0.1595  18  ASP B CA  
3601 C C   . ASP B 18  ? 3.0072 3.0185 3.7290 0.0002  0.0019  0.1461  18  ASP B C   
3602 O O   . ASP B 18  ? 2.8864 2.8679 3.6025 -0.0054 -0.0022 0.1465  18  ASP B O   
3603 C CB  . ASP B 18  ? 2.9818 3.0523 3.7090 -0.0167 -0.0202 0.1699  18  ASP B CB  
3604 C CG  . ASP B 18  ? 3.0129 3.1108 3.7523 -0.0332 -0.0359 0.1889  18  ASP B CG  
3605 O OD1 . ASP B 18  ? 2.9752 3.0789 3.7283 -0.0366 -0.0371 0.1933  18  ASP B OD1 
3606 O OD2 . ASP B 18  ? 2.9475 3.0619 3.6834 -0.0436 -0.0477 0.2005  18  ASP B OD2 
3607 N N   . ARG B 19  ? 3.0847 3.0878 3.7989 0.0121  0.0136  0.1351  19  ARG B N   
3608 C CA  . ARG B 19  ? 3.0584 3.0213 3.7591 0.0189  0.0244  0.1238  19  ARG B CA  
3609 C C   . ARG B 19  ? 3.2549 3.2200 3.9724 0.0277  0.0362  0.1190  19  ARG B C   
3610 O O   . ARG B 19  ? 3.3209 3.2624 4.0396 0.0300  0.0421  0.1159  19  ARG B O   
3611 C CB  . ARG B 19  ? 2.9556 2.9112 3.6391 0.0249  0.0292  0.1168  19  ARG B CB  
3612 C CG  . ARG B 19  ? 3.0912 3.0162 3.7612 0.0339  0.0427  0.1059  19  ARG B CG  
3613 C CD  . ARG B 19  ? 2.7563 2.6622 3.4004 0.0336  0.0408  0.1019  19  ARG B CD  
3614 N NE  . ARG B 19  ? 2.5911 2.5249 3.2378 0.0267  0.0273  0.1100  19  ARG B NE  
3615 C CZ  . ARG B 19  ? 2.7961 2.7260 3.4349 0.0155  0.0139  0.1176  19  ARG B CZ  
3616 N NH1 . ARG B 19  ? 3.0264 2.9154 3.6435 0.0113  0.0109  0.1149  19  ARG B NH1 
3617 N NH2 . ARG B 19  ? 2.8388 2.8062 3.4901 0.0089  0.0028  0.1286  19  ARG B NH2 
3618 N N   . MET B 20  ? 3.3097 3.3036 4.0393 0.0334  0.0383  0.1191  20  MET B N   
3619 C CA  . MET B 20  ? 3.2036 3.1956 3.9443 0.0419  0.0484  0.1138  20  MET B CA  
3620 C C   . MET B 20  ? 3.2571 3.2465 4.0159 0.0400  0.0500  0.1169  20  MET B C   
3621 O O   . MET B 20  ? 3.6477 3.6211 4.4118 0.0450  0.0596  0.1130  20  MET B O   
3622 C CB  . MET B 20  ? 2.8969 2.9131 3.6401 0.0490  0.0470  0.1125  20  MET B CB  
3623 C CG  . MET B 20  ? 2.4102 2.4194 3.1326 0.0524  0.0468  0.1078  20  MET B CG  
3624 S SD  . MET B 20  ? 2.7071 2.7080 3.4210 0.0630  0.0517  0.0996  20  MET B SD  
3625 C CE  . MET B 20  ? 2.6302 2.6083 3.3543 0.0639  0.0630  0.0970  20  MET B CE  
3626 N N   . LEU B 21  ? 2.8096 2.8142 3.5768 0.0323  0.0400  0.1250  21  LEU B N   
3627 C CA  . LEU B 21  ? 2.4213 2.4224 3.2039 0.0293  0.0386  0.1287  21  LEU B CA  
3628 C C   . LEU B 21  ? 2.8110 2.7753 3.5854 0.0321  0.0453  0.1235  21  LEU B C   
3629 O O   . LEU B 21  ? 3.3099 3.2679 4.0980 0.0369  0.0517  0.1223  21  LEU B O   
3630 C CB  . LEU B 21  ? 1.7078 1.7277 2.4942 0.0180  0.0246  0.1396  21  LEU B CB  
3631 C CG  . LEU B 21  ? 1.7471 1.7736 2.5512 0.0132  0.0193  0.1462  21  LEU B CG  
3632 C CD1 . LEU B 21  ? 1.8983 1.9225 2.7194 0.0214  0.0280  0.1419  21  LEU B CD1 
3633 C CD2 . LEU B 21  ? 1.7208 1.7872 2.5337 0.0071  0.0100  0.1570  21  LEU B CD2 
3634 N N   . GLU B 22  ? 2.7105 2.6507 3.4614 0.0309  0.0443  0.1202  22  GLU B N   
3635 C CA  . GLU B 22  ? 2.6845 2.5876 3.4212 0.0364  0.0505  0.1145  22  GLU B CA  
3636 C C   . GLU B 22  ? 2.6047 2.4998 3.3403 0.0479  0.0676  0.1073  22  GLU B C   
3637 O O   . GLU B 22  ? 2.4577 2.3267 3.1827 0.0558  0.0760  0.1028  22  GLU B O   
3638 C CB  . GLU B 22  ? 2.7266 2.6029 3.4350 0.0305  0.0403  0.1143  22  GLU B CB  
3639 C CG  . GLU B 22  ? 2.7940 2.6779 3.5046 0.0164  0.0214  0.1245  22  GLU B CG  
3640 C CD  . GLU B 22  ? 3.1704 3.0156 3.8537 0.0103  0.0082  0.1253  22  GLU B CD  
3641 O OE1 . GLU B 22  ? 3.6353 3.4684 4.2976 0.0076  0.0046  0.1237  22  GLU B OE1 
3642 O OE2 . GLU B 22  ? 3.1519 2.9761 3.8328 0.0084  0.0001  0.1274  22  GLU B OE2 
3643 N N   . GLU B 23  ? 2.5060 2.4232 3.2512 0.0496  0.0719  0.1068  23  GLU B N   
3644 C CA  . GLU B 23  ? 2.3762 2.2879 3.1213 0.0576  0.0857  0.1025  23  GLU B CA  
3645 C C   . GLU B 23  ? 2.1724 2.1051 2.9452 0.0596  0.0893  0.1059  23  GLU B C   
3646 O O   . GLU B 23  ? 2.0499 1.9796 2.8373 0.0636  0.0962  0.1077  23  GLU B O   
3647 C CB  . GLU B 23  ? 2.5573 2.4671 3.2841 0.0576  0.0861  0.0988  23  GLU B CB  
3648 C CG  . GLU B 23  ? 2.6692 2.5596 3.3688 0.0540  0.0798  0.0964  23  GLU B CG  
3649 C CD  . GLU B 23  ? 2.7763 2.6332 3.4580 0.0573  0.0837  0.0934  23  GLU B CD  
3650 O OE1 . GLU B 23  ? 2.7529 2.5944 3.4285 0.0662  0.0974  0.0896  23  GLU B OE1 
3651 O OE2 . GLU B 23  ? 3.4080 3.2542 4.0806 0.0512  0.0718  0.0957  23  GLU B OE2 
3652 N N   . VAL B 24  ? 2.2020 2.1547 2.9802 0.0579  0.0837  0.1069  24  VAL B N   
3653 C CA  . VAL B 24  ? 1.9347 1.9046 2.7357 0.0588  0.0827  0.1105  24  VAL B CA  
3654 C C   . VAL B 24  ? 1.6515 1.6295 2.4693 0.0559  0.0778  0.1151  24  VAL B C   
3655 O O   . VAL B 24  ? 1.6812 1.6678 2.4952 0.0510  0.0682  0.1173  24  VAL B O   
3656 C CB  . VAL B 24  ? 2.1512 2.1371 2.9488 0.0595  0.0744  0.1098  24  VAL B CB  
3657 C CG1 . VAL B 24  ? 2.2520 2.2272 3.0366 0.0626  0.0784  0.1060  24  VAL B CG1 
3658 C CG2 . VAL B 24  ? 2.2179 2.2179 3.0046 0.0572  0.0644  0.1103  24  VAL B CG2 
3659 N N   . PRO B 25  ? 1.5637 1.5395 2.4006 0.0584  0.0839  0.1178  25  PRO B N   
3660 C CA  . PRO B 25  ? 1.4036 1.3798 2.2525 0.0565  0.0797  0.1213  25  PRO B CA  
3661 C C   . PRO B 25  ? 1.4227 1.4206 2.2914 0.0531  0.0709  0.1264  25  PRO B C   
3662 O O   . PRO B 25  ? 1.3885 1.3910 2.2634 0.0489  0.0633  0.1301  25  PRO B O   
3663 C CB  . PRO B 25  ? 1.3623 1.3253 2.2201 0.0638  0.0921  0.1213  25  PRO B CB  
3664 C CG  . PRO B 25  ? 1.7367 1.7056 2.6001 0.0667  0.1008  0.1218  25  PRO B CG  
3665 C CD  . PRO B 25  ? 1.7097 1.6839 2.5582 0.0628  0.0941  0.1190  25  PRO B CD  
3666 N N   . TYR B 26  ? 1.5834 1.5918 2.4593 0.0547  0.0708  0.1269  26  TYR B N   
3667 C CA  . TYR B 26  ? 1.6575 1.6824 2.5485 0.0532  0.0620  0.1310  26  TYR B CA  
3668 C C   . TYR B 26  ? 1.6775 1.7176 2.5576 0.0504  0.0516  0.1318  26  TYR B C   
3669 O O   . TYR B 26  ? 1.8641 1.9194 2.7514 0.0503  0.0435  0.1350  26  TYR B O   
3670 C CB  . TYR B 26  ? 1.3786 1.4042 2.2735 0.0557  0.0620  0.1310  26  TYR B CB  
3671 C CG  . TYR B 26  ? 1.3552 1.3788 2.2272 0.0582  0.0595  0.1259  26  TYR B CG  
3672 C CD1 . TYR B 26  ? 1.7428 1.7786 2.6039 0.0607  0.0487  0.1245  26  TYR B CD1 
3673 C CD2 . TYR B 26  ? 1.3522 1.3621 2.2123 0.0595  0.0678  0.1226  26  TYR B CD2 
3674 C CE1 . TYR B 26  ? 2.2128 2.2466 3.0519 0.0654  0.0457  0.1194  26  TYR B CE1 
3675 C CE2 . TYR B 26  ? 1.8419 1.8485 2.6804 0.0621  0.0642  0.1177  26  TYR B CE2 
3676 C CZ  . TYR B 26  ? 2.1291 2.1472 2.9572 0.0655  0.0529  0.1159  26  TYR B CZ  
3677 O OH  . TYR B 26  ? 2.0118 2.0267 2.8177 0.0704  0.0487  0.1108  26  TYR B OH  
3678 N N   . LEU B 27  ? 1.4122 1.4491 2.2747 0.0484  0.0515  0.1298  27  LEU B N   
3679 C CA  . LEU B 27  ? 1.5254 1.5820 2.3785 0.0455  0.0425  0.1328  27  LEU B CA  
3680 C C   . LEU B 27  ? 1.5177 1.5837 2.3825 0.0384  0.0353  0.1403  27  LEU B C   
3681 O O   . LEU B 27  ? 1.5006 1.5905 2.3667 0.0366  0.0275  0.1458  27  LEU B O   
3682 C CB  . LEU B 27  ? 1.8345 1.8874 2.6671 0.0439  0.0426  0.1306  27  LEU B CB  
3683 C CG  . LEU B 27  ? 2.0965 2.1527 2.9140 0.0508  0.0439  0.1251  27  LEU B CG  
3684 C CD1 . LEU B 27  ? 2.2484 2.3185 3.0510 0.0484  0.0383  0.1274  27  LEU B CD1 
3685 C CD2 . LEU B 27  ? 1.9877 2.0569 2.8089 0.0583  0.0403  0.1241  27  LEU B CD2 
3686 N N   . ARG B 28  ? 1.5305 1.5776 2.4023 0.0354  0.0378  0.1409  28  ARG B N   
3687 C CA  . ARG B 28  ? 1.6931 1.7455 2.5736 0.0279  0.0289  0.1483  28  ARG B CA  
3688 C C   . ARG B 28  ? 1.5647 1.6370 2.4617 0.0289  0.0245  0.1525  28  ARG B C   
3689 O O   . ARG B 28  ? 1.8415 1.9304 2.7423 0.0225  0.0154  0.1601  28  ARG B O   
3690 C CB  . ARG B 28  ? 1.4928 1.5172 2.3721 0.0260  0.0298  0.1475  28  ARG B CB  
3691 C CG  . ARG B 28  ? 1.7662 1.7756 2.6582 0.0350  0.0405  0.1429  28  ARG B CG  
3692 C CD  . ARG B 28  ? 1.9343 1.9237 2.8298 0.0348  0.0377  0.1443  28  ARG B CD  
3693 N NE  . ARG B 28  ? 1.9510 1.9182 2.8232 0.0311  0.0323  0.1431  28  ARG B NE  
3694 C CZ  . ARG B 28  ? 2.2742 2.2161 3.1411 0.0318  0.0271  0.1432  28  ARG B CZ  
3695 N NH1 . ARG B 28  ? 2.7250 2.6656 3.6099 0.0351  0.0262  0.1454  28  ARG B NH1 
3696 N NH2 . ARG B 28  ? 1.9806 1.8960 2.8222 0.0296  0.0213  0.1412  28  ARG B NH2 
3697 N N   . TYR B 29  ? 1.2571 1.3282 2.1620 0.0362  0.0297  0.1484  29  TYR B N   
3698 C CA  . TYR B 29  ? 1.3737 1.4575 2.2920 0.0376  0.0242  0.1518  29  TYR B CA  
3699 C C   . TYR B 29  ? 1.4082 1.5132 2.3138 0.0419  0.0187  0.1519  29  TYR B C   
3700 O O   . TYR B 29  ? 1.2726 1.3861 2.1833 0.0449  0.0130  0.1537  29  TYR B O   
3701 C CB  . TYR B 29  ? 1.4870 1.5579 2.4211 0.0417  0.0296  0.1498  29  TYR B CB  
3702 C CG  . TYR B 29  ? 1.5861 1.6420 2.5352 0.0405  0.0350  0.1512  29  TYR B CG  
3703 C CD1 . TYR B 29  ? 1.7363 1.7752 2.6792 0.0436  0.0452  0.1470  29  TYR B CD1 
3704 C CD2 . TYR B 29  ? 1.7377 1.7958 2.7050 0.0379  0.0295  0.1565  29  TYR B CD2 
3705 C CE1 . TYR B 29  ? 1.9275 1.9526 2.8808 0.0463  0.0503  0.1477  29  TYR B CE1 
3706 C CE2 . TYR B 29  ? 2.0633 2.1078 3.0431 0.0395  0.0338  0.1575  29  TYR B CE2 
3707 C CZ  . TYR B 29  ? 2.0248 2.0529 2.9971 0.0447  0.0446  0.1529  29  TYR B CZ  
3708 O OH  . TYR B 29  ? 1.8205 1.8351 2.8024 0.0497  0.0489  0.1533  29  TYR B OH  
3709 N N   . SER B 30  ? 1.4635 1.5768 2.3514 0.0430  0.0194  0.1503  30  SER B N   
3710 C CA  . SER B 30  ? 1.3950 1.5272 2.2679 0.0512  0.0159  0.1488  30  SER B CA  
3711 C C   . SER B 30  ? 1.1341 1.2927 2.0088 0.0521  0.0080  0.1560  30  SER B C   
3712 O O   . SER B 30  ? 0.7976 0.9642 1.6640 0.0622  0.0042  0.1538  30  SER B O   
3713 C CB  . SER B 30  ? 1.2860 1.4247 2.1422 0.0523  0.0180  0.1470  30  SER B CB  
3714 O OG  . SER B 30  ? 1.3660 1.4804 2.2157 0.0549  0.0250  0.1390  30  SER B OG  
3715 N N   . ALA B 31  ? 1.1526 1.3229 2.0358 0.0417  0.0045  0.1650  31  ALA B N   
3716 C CA  . ALA B 31  ? 1.0944 1.2942 1.9782 0.0415  -0.0023 0.1740  31  ALA B CA  
3717 C C   . ALA B 31  ? 0.9953 1.1905 1.8841 0.0482  -0.0058 0.1719  31  ALA B C   
3718 O O   . ALA B 31  ? 0.9533 1.1707 1.8340 0.0552  -0.0105 0.1754  31  ALA B O   
3719 C CB  . ALA B 31  ? 1.1863 1.3933 2.0805 0.0266  -0.0073 0.1851  31  ALA B CB  
3720 N N   . GLU B 32  ? 0.9524 1.1197 1.8537 0.0467  -0.0039 0.1670  32  GLU B N   
3721 C CA  . GLU B 32  ? 1.0999 1.2613 2.0069 0.0513  -0.0094 0.1663  32  GLU B CA  
3722 C C   . GLU B 32  ? 1.1402 1.3130 2.0254 0.0652  -0.0138 0.1627  32  GLU B C   
3723 O O   . GLU B 32  ? 1.1567 1.3341 2.0385 0.0702  -0.0213 0.1646  32  GLU B O   
3724 C CB  . GLU B 32  ? 1.4233 1.5569 2.3465 0.0491  -0.0064 0.1624  32  GLU B CB  
3725 C CG  . GLU B 32  ? 1.8126 1.9396 2.7588 0.0401  -0.0078 0.1681  32  GLU B CG  
3726 C CD  . GLU B 32  ? 2.0171 2.1246 2.9821 0.0403  -0.0064 0.1669  32  GLU B CD  
3727 O OE1 . GLU B 32  ? 1.6969 1.8003 2.6618 0.0446  -0.0125 0.1661  32  GLU B OE1 
3728 O OE2 . GLU B 32  ? 2.2500 2.3467 3.2297 0.0364  -0.0001 0.1675  32  GLU B OE2 
3729 N N   . ARG B 33  ? 1.0576 1.2347 1.9256 0.0724  -0.0099 0.1575  33  ARG B N   
3730 C CA  . ARG B 33  ? 1.0361 1.2213 1.8797 0.0887  -0.0143 0.1527  33  ARG B CA  
3731 C C   . ARG B 33  ? 0.9881 1.2023 1.8247 0.0945  -0.0197 0.1598  33  ARG B C   
3732 O O   . ARG B 33  ? 1.0444 1.2565 1.8641 0.1081  -0.0266 0.1563  33  ARG B O   
3733 C CB  . ARG B 33  ? 0.8810 1.0706 1.7072 0.0961  -0.0096 0.1473  33  ARG B CB  
3734 C CG  . ARG B 33  ? 0.8882 1.0467 1.7169 0.0926  -0.0052 0.1398  33  ARG B CG  
3735 C CD  . ARG B 33  ? 0.8812 1.0384 1.6924 0.0991  -0.0015 0.1337  33  ARG B CD  
3736 N NE  . ARG B 33  ? 1.0309 1.1557 1.8421 0.0970  0.0006  0.1270  33  ARG B NE  
3737 C CZ  . ARG B 33  ? 1.2228 1.3345 2.0406 0.0885  0.0090  0.1256  33  ARG B CZ  
3738 N NH1 . ARG B 33  ? 1.3397 1.4626 2.1647 0.0802  0.0148  0.1298  33  ARG B NH1 
3739 N NH2 . ARG B 33  ? 1.0528 1.1390 1.8688 0.0880  0.0108  0.1209  33  ARG B NH2 
3740 N N   . SER B 34  ? 1.0102 1.2488 1.8590 0.0834  -0.0176 0.1704  34  SER B N   
3741 C CA  . SER B 34  ? 1.0787 1.3518 1.9222 0.0867  -0.0212 0.1802  34  SER B CA  
3742 C C   . SER B 34  ? 1.0454 1.3086 1.8883 0.0908  -0.0289 0.1802  34  SER B C   
3743 O O   . SER B 34  ? 0.8717 1.1605 1.7040 0.0982  -0.0324 0.1865  34  SER B O   
3744 C CB  . SER B 34  ? 1.1692 1.4659 2.0283 0.0696  -0.0199 0.1937  34  SER B CB  
3745 O OG  . SER B 34  ? 1.1136 1.3838 1.9934 0.0530  -0.0200 0.1943  34  SER B OG  
3746 N N   . LEU B 35  ? 1.0315 1.2588 1.8855 0.0863  -0.0318 0.1741  35  LEU B N   
3747 C CA  . LEU B 35  ? 1.1808 1.3961 2.0399 0.0858  -0.0404 0.1758  35  LEU B CA  
3748 C C   . LEU B 35  ? 1.3311 1.5402 2.1619 0.1049  -0.0484 0.1694  35  LEU B C   
3749 O O   . LEU B 35  ? 1.4886 1.6835 2.3181 0.1066  -0.0578 0.1697  35  LEU B O   
3750 C CB  . LEU B 35  ? 1.1497 1.3328 2.0325 0.0745  -0.0410 0.1734  35  LEU B CB  
3751 C CG  . LEU B 35  ? 1.1100 1.2955 2.0182 0.0579  -0.0363 0.1804  35  LEU B CG  
3752 C CD1 . LEU B 35  ? 1.5343 1.6906 2.4620 0.0523  -0.0335 0.1761  35  LEU B CD1 
3753 C CD2 . LEU B 35  ? 0.9739 1.1706 1.8892 0.0525  -0.0438 0.1895  35  LEU B CD2 
3754 N N   . CYS B 36  ? 1.4130 1.6307 2.2200 0.1199  -0.0457 0.1634  36  CYS B N   
3755 C CA  . CYS B 36  ? 1.4791 1.6893 2.2527 0.1417  -0.0542 0.1561  36  CYS B CA  
3756 C C   . CYS B 36  ? 1.5742 1.8208 2.3329 0.1525  -0.0547 0.1636  36  CYS B C   
3757 O O   . CYS B 36  ? 1.7584 1.9996 2.4876 0.1719  -0.0628 0.1590  36  CYS B O   
3758 C CB  . CYS B 36  ? 1.4048 1.6132 2.1574 0.1553  -0.0510 0.1473  36  CYS B CB  
3759 S SG  . CYS B 36  ? 1.7331 1.9784 2.5015 0.1454  -0.0362 0.1542  36  CYS B SG  
3760 N N   . PHE B 37  ? 1.5551 1.8373 2.3329 0.1397  -0.0471 0.1760  37  PHE B N   
3761 C CA  . PHE B 37  ? 1.4914 1.8179 2.2577 0.1481  -0.0453 0.1865  37  PHE B CA  
3762 C C   . PHE B 37  ? 1.4176 1.7430 2.1909 0.1409  -0.0522 0.1941  37  PHE B C   
3763 O O   . PHE B 37  ? 1.5215 1.8795 2.2815 0.1497  -0.0524 0.2026  37  PHE B O   
3764 C CB  . PHE B 37  ? 1.3297 1.6974 2.1117 0.1367  -0.0357 0.1985  37  PHE B CB  
3765 C CG  . PHE B 37  ? 1.1697 1.5462 1.9411 0.1465  -0.0292 0.1927  37  PHE B CG  
3766 C CD1 . PHE B 37  ? 1.1741 1.5827 1.9195 0.1701  -0.0266 0.1927  37  PHE B CD1 
3767 C CD2 . PHE B 37  ? 1.3713 1.7247 2.1580 0.1334  -0.0257 0.1874  37  PHE B CD2 
3768 C CE1 . PHE B 37  ? 1.5602 1.9762 2.2967 0.1793  -0.0216 0.1874  37  PHE B CE1 
3769 C CE2 . PHE B 37  ? 1.4747 1.8343 2.2511 0.1418  -0.0207 0.1822  37  PHE B CE2 
3770 C CZ  . PHE B 37  ? 1.5527 1.9430 2.3048 0.1644  -0.0191 0.1821  37  PHE B CZ  
3771 N N   . LEU B 38  ? 1.1813 1.4710 1.9751 0.1258  -0.0578 0.1917  38  LEU B N   
3772 C CA  . LEU B 38  ? 1.3267 1.6116 2.1288 0.1179  -0.0656 0.1985  38  LEU B CA  
3773 C C   . LEU B 38  ? 1.4181 1.7043 2.1867 0.1392  -0.0738 0.1961  38  LEU B C   
3774 O O   . LEU B 38  ? 1.4391 1.7353 2.2071 0.1365  -0.0787 0.2044  38  LEU B O   
3775 C CB  . LEU B 38  ? 1.2924 1.5371 2.1197 0.1027  -0.0711 0.1949  38  LEU B CB  
3776 C CG  . LEU B 38  ? 1.1651 1.4040 2.0221 0.0847  -0.0632 0.1961  38  LEU B CG  
3777 C CD1 . LEU B 38  ? 1.0690 1.2707 1.9477 0.0753  -0.0677 0.1919  38  LEU B CD1 
3778 C CD2 . LEU B 38  ? 0.8894 1.1553 1.7633 0.0691  -0.0602 0.2095  38  LEU B CD2 
3779 N N   . GLY B 39  ? 1.5864 1.8599 2.3243 0.1611  -0.0761 0.1845  39  GLY B N   
3780 C CA  . GLY B 39  ? 1.8892 2.1603 2.5879 0.1857  -0.0845 0.1803  39  GLY B CA  
3781 C C   . GLY B 39  ? 2.0620 2.3850 2.7508 0.1932  -0.0781 0.1931  39  GLY B C   
3782 O O   . GLY B 39  ? 2.0275 2.3504 2.6926 0.2062  -0.0852 0.1944  39  GLY B O   
3783 N N   . ASP B 40  ? 2.1264 2.4933 2.8336 0.1840  -0.0653 0.2037  40  ASP B N   
3784 C CA  . ASP B 40  ? 2.0221 2.4466 2.7247 0.1882  -0.0581 0.2195  40  ASP B CA  
3785 C C   . ASP B 40  ? 1.8246 2.2521 2.5374 0.1747  -0.0642 0.2308  40  ASP B C   
3786 O O   . ASP B 40  ? 1.9966 2.4580 2.6908 0.1867  -0.0631 0.2403  40  ASP B O   
3787 C CB  . ASP B 40  ? 2.2982 2.7647 3.0228 0.1758  -0.0465 0.2306  40  ASP B CB  
3788 C CG  . ASP B 40  ? 2.5117 2.9830 3.2231 0.1919  -0.0401 0.2211  40  ASP B CG  
3789 O OD1 . ASP B 40  ? 2.6030 3.0390 3.2884 0.2118  -0.0453 0.2043  40  ASP B OD1 
3790 O OD2 . ASP B 40  ? 2.3185 2.8273 3.0449 0.1837  -0.0315 0.2311  40  ASP B OD2 
3791 N N   . LEU B 41  ? 1.4983 1.8901 2.2389 0.1515  -0.0708 0.2298  41  LEU B N   
3792 C CA  . LEU B 41  ? 1.2626 1.6538 2.0152 0.1370  -0.0778 0.2404  41  LEU B CA  
3793 C C   . LEU B 41  ? 1.3300 1.7082 2.0490 0.1570  -0.0872 0.2362  41  LEU B C   
3794 O O   . LEU B 41  ? 1.1432 1.5258 1.8657 0.1486  -0.0930 0.2459  41  LEU B O   
3795 C CB  . LEU B 41  ? 1.0705 1.4246 1.8579 0.1119  -0.0832 0.2388  41  LEU B CB  
3796 C CG  . LEU B 41  ? 1.1291 1.5003 1.9487 0.0883  -0.0766 0.2488  41  LEU B CG  
3797 C CD1 . LEU B 41  ? 1.1892 1.5184 2.0378 0.0709  -0.0806 0.2428  41  LEU B CD1 
3798 C CD2 . LEU B 41  ? 1.3484 1.7597 2.1751 0.0754  -0.0771 0.2689  41  LEU B CD2 
3799 N N   . ARG B 42  ? 1.6151 1.9763 2.2989 0.1839  -0.0898 0.2222  42  ARG B N   
3800 C CA  . ARG B 42  ? 1.8132 2.1602 2.4559 0.2078  -0.0996 0.2170  42  ARG B CA  
3801 C C   . ARG B 42  ? 1.9877 2.3899 2.6118 0.2200  -0.0924 0.2313  42  ARG B C   
3802 O O   . ARG B 42  ? 1.8652 2.2600 2.4659 0.2296  -0.1006 0.2331  42  ARG B O   
3803 C CB  . ARG B 42  ? 2.0393 2.3540 2.6432 0.2358  -0.1057 0.1989  42  ARG B CB  
3804 C CG  . ARG B 42  ? 2.0567 2.3096 2.6694 0.2267  -0.1184 0.1856  42  ARG B CG  
3805 C CD  . ARG B 42  ? 1.8918 2.1000 2.4573 0.2533  -0.1336 0.1700  42  ARG B CD  
3806 N NE  . ARG B 42  ? 1.8935 2.0439 2.4714 0.2387  -0.1500 0.1632  42  ARG B NE  
3807 C CZ  . ARG B 42  ? 1.9414 2.0689 2.5371 0.2216  -0.1612 0.1683  42  ARG B CZ  
3808 N NH1 . ARG B 42  ? 2.1530 2.3038 2.7517 0.2174  -0.1601 0.1790  42  ARG B NH1 
3809 N NH2 . ARG B 42  ? 2.0120 2.0936 2.6234 0.2080  -0.1744 0.1637  42  ARG B NH2 
3810 N N   . ASP B 43  ? 2.3286 2.7864 2.9618 0.2202  -0.0775 0.2423  43  ASP B N   
3811 C CA  . ASP B 43  ? 2.1637 2.6837 2.7897 0.2254  -0.0691 0.2613  43  ASP B CA  
3812 C C   . ASP B 43  ? 1.8772 2.4065 2.5373 0.1927  -0.0723 0.2782  43  ASP B C   
3813 O O   . ASP B 43  ? 1.4472 1.9736 2.1454 0.1650  -0.0710 0.2833  43  ASP B O   
3814 C CB  . ASP B 43  ? 2.2275 2.8071 2.8570 0.2329  -0.0539 0.2708  43  ASP B CB  
3815 C CG  . ASP B 43  ? 2.2191 2.8696 2.8589 0.2249  -0.0451 0.2971  43  ASP B CG  
3816 O OD1 . ASP B 43  ? 2.0979 2.7686 2.7119 0.2405  -0.0457 0.3040  43  ASP B OD1 
3817 O OD2 . ASP B 43  ? 2.3948 3.0794 3.0676 0.2023  -0.0387 0.3116  43  ASP B OD2 
3818 N N   . PRO B 44  ? 1.8649 2.4031 2.5092 0.1963  -0.0776 0.2871  44  PRO B N   
3819 C CA  . PRO B 44  ? 1.7170 2.2593 2.3901 0.1661  -0.0832 0.3029  44  PRO B CA  
3820 C C   . PRO B 44  ? 1.4493 2.0406 2.1565 0.1410  -0.0748 0.3236  44  PRO B C   
3821 O O   . PRO B 44  ? 1.2765 1.8588 2.0138 0.1115  -0.0811 0.3335  44  PRO B O   
3822 C CB  . PRO B 44  ? 1.8787 2.4368 2.5192 0.1821  -0.0869 0.3105  44  PRO B CB  
3823 C CG  . PRO B 44  ? 1.9044 2.4314 2.4989 0.2185  -0.0904 0.2899  44  PRO B CG  
3824 C CD  . PRO B 44  ? 1.8414 2.3826 2.4360 0.2308  -0.0797 0.2817  44  PRO B CD  
3825 N N   . GLY B 45  ? 1.5030 2.1437 2.2041 0.1533  -0.0622 0.3299  45  GLY B N   
3826 C CA  . GLY B 45  ? 1.6169 2.3124 2.3452 0.1318  -0.0554 0.3530  45  GLY B CA  
3827 C C   . GLY B 45  ? 1.6460 2.3208 2.4061 0.1105  -0.0552 0.3481  45  GLY B C   
3828 O O   . GLY B 45  ? 1.5297 2.2139 2.3197 0.0802  -0.0589 0.3633  45  GLY B O   
3829 N N   . THR B 46  ? 1.7801 2.4241 2.5302 0.1274  -0.0521 0.3267  46  THR B N   
3830 C CA  . THR B 46  ? 1.8506 2.4748 2.6244 0.1127  -0.0503 0.3199  46  THR B CA  
3831 C C   . THR B 46  ? 1.4813 2.0654 2.2858 0.0817  -0.0598 0.3209  46  THR B C   
3832 O O   . THR B 46  ? 1.4591 2.0028 2.2641 0.0785  -0.0686 0.3133  46  THR B O   
3833 C CB  . THR B 46  ? 2.1538 2.7446 2.9095 0.1357  -0.0473 0.2962  46  THR B CB  
3834 O OG1 . THR B 46  ? 1.9897 2.6212 2.7147 0.1659  -0.0395 0.2973  46  THR B OG1 
3835 C CG2 . THR B 46  ? 2.4538 3.0318 3.2317 0.1218  -0.0438 0.2912  46  THR B CG2 
3836 N N   . ARG B 47  ? 1.2144 1.8099 2.0441 0.0593  -0.0588 0.3307  47  ARG B N   
3837 C CA  . ARG B 47  ? 1.2611 1.8166 2.1179 0.0328  -0.0666 0.3294  47  ARG B CA  
3838 C C   . ARG B 47  ? 1.2905 1.8299 2.1576 0.0291  -0.0617 0.3198  47  ARG B C   
3839 O O   . ARG B 47  ? 1.5016 2.0771 2.3692 0.0285  -0.0559 0.3284  47  ARG B O   
3840 C CB  . ARG B 47  ? 1.3630 1.9477 2.2337 0.0088  -0.0740 0.3541  47  ARG B CB  
3841 C CG  . ARG B 47  ? 1.8157 2.3722 2.7122 -0.0211 -0.0843 0.3603  47  ARG B CG  
3842 C CD  . ARG B 47  ? 2.6841 3.2835 3.5868 -0.0412 -0.0914 0.3886  47  ARG B CD  
3843 N NE  . ARG B 47  ? 3.2099 3.7864 4.1327 -0.0713 -0.1052 0.3994  47  ARG B NE  
3844 C CZ  . ARG B 47  ? 3.0677 3.6726 4.0008 -0.0953 -0.1131 0.4228  47  ARG B CZ  
3845 N NH1 . ARG B 47  ? 2.8158 3.4828 3.7453 -0.0951 -0.1077 0.4421  47  ARG B NH1 
3846 N NH2 . ARG B 47  ? 3.0405 3.6106 3.9873 -0.1197 -0.1279 0.4280  47  ARG B NH2 
3847 N N   . LEU B 48  ? 1.2532 1.7381 2.1296 0.0260  -0.0644 0.3028  48  LEU B N   
3848 C CA  . LEU B 48  ? 1.2377 1.6986 2.1195 0.0268  -0.0592 0.2897  48  LEU B CA  
3849 C C   . LEU B 48  ? 1.1649 1.5974 2.0702 0.0027  -0.0645 0.2921  48  LEU B C   
3850 O O   . LEU B 48  ? 1.1217 1.5281 2.0392 -0.0088 -0.0725 0.2933  48  LEU B O   
3851 C CB  . LEU B 48  ? 1.1156 1.5386 1.9860 0.0458  -0.0565 0.2678  48  LEU B CB  
3852 C CG  . LEU B 48  ? 1.3729 1.8134 2.2138 0.0733  -0.0526 0.2613  48  LEU B CG  
3853 C CD1 . LEU B 48  ? 1.5547 1.9495 2.3859 0.0871  -0.0541 0.2410  48  LEU B CD1 
3854 C CD2 . LEU B 48  ? 1.6009 2.0846 2.4316 0.0826  -0.0440 0.2668  48  LEU B CD2 
3855 N N   . VAL B 49  ? 1.2934 1.7295 2.2024 -0.0027 -0.0604 0.2921  49  VAL B N   
3856 C CA  . VAL B 49  ? 1.2344 1.6364 2.1587 -0.0198 -0.0641 0.2897  49  VAL B CA  
3857 C C   . VAL B 49  ? 1.3049 1.6822 2.2255 -0.0097 -0.0556 0.2724  49  VAL B C   
3858 O O   . VAL B 49  ? 1.8131 2.2134 2.7228 -0.0002 -0.0489 0.2713  49  VAL B O   
3859 C CB  . VAL B 49  ? 1.0717 1.4990 2.0029 -0.0413 -0.0715 0.3101  49  VAL B CB  
3860 C CG1 . VAL B 49  ? 1.1821 1.5719 2.1217 -0.0555 -0.0757 0.3060  49  VAL B CG1 
3861 C CG2 . VAL B 49  ? 1.0335 1.4760 1.9703 -0.0541 -0.0817 0.3268  49  VAL B CG2 
3862 N N   . VAL B 50  ? 1.0462 1.3783 1.9757 -0.0105 -0.0557 0.2597  50  VAL B N   
3863 C CA  . VAL B 50  ? 1.2237 1.5284 2.1516 -0.0030 -0.0480 0.2443  50  VAL B CA  
3864 C C   . VAL B 50  ? 1.2737 1.5552 2.2104 -0.0179 -0.0502 0.2456  50  VAL B C   
3865 O O   . VAL B 50  ? 1.3426 1.6041 2.2903 -0.0295 -0.0577 0.2497  50  VAL B O   
3866 C CB  . VAL B 50  ? 1.4809 1.7549 2.4114 0.0086  -0.0456 0.2301  50  VAL B CB  
3867 C CG1 . VAL B 50  ? 1.6363 1.8808 2.5684 0.0131  -0.0380 0.2166  50  VAL B CG1 
3868 C CG2 . VAL B 50  ? 1.5122 1.8030 2.4271 0.0253  -0.0455 0.2272  50  VAL B CG2 
3869 N N   . ILE B 51  ? 1.2330 1.5143 2.1619 -0.0158 -0.0445 0.2412  51  ILE B N   
3870 C CA  . ILE B 51  ? 1.4233 1.6782 2.3542 -0.0267 -0.0463 0.2400  51  ILE B CA  
3871 C C   . ILE B 51  ? 1.4344 1.6636 2.3600 -0.0154 -0.0357 0.2236  51  ILE B C   
3872 O O   . ILE B 51  ? 1.8854 2.1293 2.8009 -0.0046 -0.0290 0.2185  51  ILE B O   
3873 C CB  . ILE B 51  ? 1.5606 1.8424 2.4864 -0.0402 -0.0530 0.2552  51  ILE B CB  
3874 C CG1 . ILE B 51  ? 1.4935 1.8110 2.4240 -0.0500 -0.0620 0.2737  51  ILE B CG1 
3875 C CG2 . ILE B 51  ? 1.9634 2.2112 2.8879 -0.0534 -0.0595 0.2554  51  ILE B CG2 
3876 C CD1 . ILE B 51  ? 1.4176 1.7725 2.3455 -0.0633 -0.0685 0.2924  51  ILE B CD1 
3877 N N   . THR B 52  ? 1.2393 1.4304 2.1714 -0.0171 -0.0345 0.2161  52  THR B N   
3878 C CA  . THR B 52  ? 1.2430 1.4084 2.1718 -0.0077 -0.0243 0.2023  52  THR B CA  
3879 C C   . THR B 52  ? 1.1723 1.3063 2.0997 -0.0153 -0.0267 0.2013  52  THR B C   
3880 O O   . THR B 52  ? 1.0751 1.1997 2.0074 -0.0252 -0.0365 0.2085  52  THR B O   
3881 C CB  . THR B 52  ? 1.2888 1.4429 2.2279 0.0031  -0.0188 0.1939  52  THR B CB  
3882 O OG1 . THR B 52  ? 1.4233 1.5659 2.3772 -0.0021 -0.0249 0.1980  52  THR B OG1 
3883 C CG2 . THR B 52  ? 1.3696 1.5481 2.3041 0.0119  -0.0191 0.1939  52  THR B CG2 
3884 N N   . SER B 53  ? 1.1693 1.2854 2.0868 -0.0100 -0.0188 0.1922  53  SER B N   
3885 C CA  . SER B 53  ? 1.4831 1.5647 2.3932 -0.0130 -0.0196 0.1886  53  SER B CA  
3886 C C   . SER B 53  ? 1.6061 1.6613 2.5284 -0.0070 -0.0165 0.1832  53  SER B C   
3887 O O   . SER B 53  ? 1.6394 1.6660 2.5565 -0.0092 -0.0211 0.1826  53  SER B O   
3888 C CB  . SER B 53  ? 1.5540 1.6261 2.4494 -0.0067 -0.0105 0.1800  53  SER B CB  
3889 O OG  . SER B 53  ? 1.8219 1.8630 2.7027 -0.0105 -0.0137 0.1780  53  SER B OG  
3890 N N   . GLU B 54  ? 1.5891 1.6538 2.5266 0.0013  -0.0097 0.1799  54  GLU B N   
3891 C CA  . GLU B 54  ? 1.4292 1.4780 2.3833 0.0080  -0.0056 0.1765  54  GLU B CA  
3892 C C   . GLU B 54  ? 1.2330 1.3011 2.2035 0.0066  -0.0110 0.1819  54  GLU B C   
3893 O O   . GLU B 54  ? 1.1312 1.2221 2.0991 0.0074  -0.0116 0.1833  54  GLU B O   
3894 C CB  . GLU B 54  ? 1.6623 1.7031 2.6182 0.0195  0.0088  0.1673  54  GLU B CB  
3895 C CG  . GLU B 54  ? 1.9442 1.9590 2.8863 0.0240  0.0158  0.1611  54  GLU B CG  
3896 C CD  . GLU B 54  ? 2.3636 2.3543 3.3101 0.0268  0.0131  0.1613  54  GLU B CD  
3897 O OE1 . GLU B 54  ? 2.5527 2.5450 3.5200 0.0331  0.0169  0.1618  54  GLU B OE1 
3898 O OE2 . GLU B 54  ? 2.3960 2.3656 3.3246 0.0230  0.0058  0.1613  54  GLU B OE2 
3899 N N   . ALA B 55  ? 1.1286 1.1855 2.1145 0.0065  -0.0152 0.1843  55  ALA B N   
3900 C CA  . ALA B 55  ? 1.0745 1.1455 2.0739 0.0028  -0.0237 0.1910  55  ALA B CA  
3901 C C   . ALA B 55  ? 1.0451 1.1284 2.0540 0.0101  -0.0189 0.1882  55  ALA B C   
3902 O O   . ALA B 55  ? 1.2864 1.3598 2.3066 0.0176  -0.0108 0.1834  55  ALA B O   
3903 C CB  . ALA B 55  ? 1.1318 1.1840 2.1449 0.0023  -0.0291 0.1933  55  ALA B CB  
3904 N N   . VAL B 56  ? 0.9395 1.0440 1.9436 0.0080  -0.0253 0.1925  56  VAL B N   
3905 C CA  . VAL B 56  ? 1.0199 1.1305 2.0294 0.0144  -0.0256 0.1906  56  VAL B CA  
3906 C C   . VAL B 56  ? 1.1818 1.2806 2.2149 0.0148  -0.0286 0.1927  56  VAL B C   
3907 O O   . VAL B 56  ? 1.2830 1.3797 2.3246 0.0091  -0.0362 0.1984  56  VAL B O   
3908 C CB  . VAL B 56  ? 1.0486 1.1821 2.0448 0.0136  -0.0335 0.1954  56  VAL B CB  
3909 C CG1 . VAL B 56  ? 0.9680 1.1019 1.9674 0.0195  -0.0391 0.1947  56  VAL B CG1 
3910 C CG2 . VAL B 56  ? 1.2723 1.4210 2.2472 0.0168  -0.0289 0.1929  56  VAL B CG2 
3911 N N   . ASP B 57  ? 1.3175 1.4097 2.3614 0.0208  -0.0239 0.1892  57  ASP B N   
3912 C CA  . ASP B 57  ? 1.1340 1.2181 2.2038 0.0217  -0.0255 0.1925  57  ASP B CA  
3913 C C   . ASP B 57  ? 1.1348 1.2242 2.2095 0.0196  -0.0384 0.1974  57  ASP B C   
3914 O O   . ASP B 57  ? 1.0114 1.1057 2.0714 0.0220  -0.0429 0.1957  57  ASP B O   
3915 C CB  . ASP B 57  ? 1.1634 1.2417 2.2439 0.0273  -0.0155 0.1896  57  ASP B CB  
3916 C CG  . ASP B 57  ? 1.2320 1.3080 2.3422 0.0281  -0.0173 0.1954  57  ASP B CG  
3917 O OD1 . ASP B 57  ? 1.1994 1.2781 2.3169 0.0249  -0.0294 0.2002  57  ASP B OD1 
3918 O OD2 . ASP B 57  ? 1.2563 1.3289 2.3815 0.0326  -0.0068 0.1957  57  ASP B OD2 
3919 N N   . PRO B 58  ? 1.1897 1.2755 2.2840 0.0163  -0.0454 0.2032  58  PRO B N   
3920 C CA  . PRO B 58  ? 1.3119 1.4009 2.4080 0.0133  -0.0592 0.2084  58  PRO B CA  
3921 C C   . PRO B 58  ? 1.1577 1.2446 2.2501 0.0171  -0.0632 0.2069  58  PRO B C   
3922 O O   . PRO B 58  ? 1.0732 1.1628 2.1488 0.0179  -0.0733 0.2074  58  PRO B O   
3923 C CB  . PRO B 58  ? 1.2259 1.3079 2.3495 0.0107  -0.0639 0.2143  58  PRO B CB  
3924 C CG  . PRO B 58  ? 1.1705 1.2466 2.3090 0.0158  -0.0506 0.2115  58  PRO B CG  
3925 C CD  . PRO B 58  ? 1.0846 1.1611 2.1994 0.0171  -0.0411 0.2049  58  PRO B CD  
3926 N N   . ALA B 59  ? 1.0431 1.1243 2.1510 0.0194  -0.0564 0.2061  59  ALA B N   
3927 C CA  . ALA B 59  ? 1.0777 1.1530 2.1857 0.0205  -0.0626 0.2069  59  ALA B CA  
3928 C C   . ALA B 59  ? 1.0832 1.1578 2.1568 0.0252  -0.0654 0.2002  59  ALA B C   
3929 O O   . ALA B 59  ? 1.0244 1.0919 2.0838 0.0272  -0.0786 0.2003  59  ALA B O   
3930 C CB  . ALA B 59  ? 1.0819 1.1560 2.2086 0.0215  -0.0515 0.2079  59  ALA B CB  
3931 N N   . THR B 60  ? 1.0462 1.1267 2.1055 0.0281  -0.0533 0.1942  60  THR B N   
3932 C CA  . THR B 60  ? 0.9192 1.0026 1.9467 0.0343  -0.0531 0.1875  60  THR B CA  
3933 C C   . THR B 60  ? 0.8027 0.8941 1.8095 0.0373  -0.0637 0.1883  60  THR B C   
3934 O O   . THR B 60  ? 0.7447 0.8318 1.7276 0.0449  -0.0721 0.1849  60  THR B O   
3935 C CB  . THR B 60  ? 0.7095 0.8012 1.7308 0.0343  -0.0393 0.1838  60  THR B CB  
3936 O OG1 . THR B 60  ? 0.5655 0.6502 1.6070 0.0323  -0.0287 0.1840  60  THR B OG1 
3937 C CG2 . THR B 60  ? 0.7269 0.8234 1.7189 0.0412  -0.0368 0.1771  60  THR B CG2 
3938 N N   . LEU B 61  ? 0.6404 0.7427 1.6553 0.0319  -0.0635 0.1933  61  LEU B N   
3939 C CA  . LEU B 61  ? 0.7522 0.8675 1.7502 0.0332  -0.0718 0.1966  61  LEU B CA  
3940 C C   . LEU B 61  ? 0.8384 0.9421 1.8321 0.0364  -0.0863 0.1982  61  LEU B C   
3941 O O   . LEU B 61  ? 0.7225 0.8302 1.6885 0.0450  -0.0933 0.1962  61  LEU B O   
3942 C CB  . LEU B 61  ? 0.8863 1.0123 1.8962 0.0240  -0.0706 0.2035  61  LEU B CB  
3943 C CG  . LEU B 61  ? 0.9485 1.0918 1.9437 0.0230  -0.0787 0.2100  61  LEU B CG  
3944 C CD1 . LEU B 61  ? 0.7303 0.8932 1.6948 0.0326  -0.0776 0.2082  61  LEU B CD1 
3945 C CD2 . LEU B 61  ? 1.3839 1.5355 2.3904 0.0115  -0.0778 0.2174  61  LEU B CD2 
3946 N N   . ASP B 62  ? 1.0217 1.1111 2.0420 0.0303  -0.0912 0.2020  62  ASP B N   
3947 C CA  . ASP B 62  ? 1.3268 1.4014 2.3477 0.0306  -0.1072 0.2051  62  ASP B CA  
3948 C C   . ASP B 62  ? 1.2607 1.3211 2.2557 0.0395  -0.1145 0.1991  62  ASP B C   
3949 O O   . ASP B 62  ? 1.0986 1.1504 2.0690 0.0461  -0.1281 0.1981  62  ASP B O   
3950 C CB  . ASP B 62  ? 1.3211 1.3861 2.3793 0.0223  -0.1097 0.2114  62  ASP B CB  
3951 C CG  . ASP B 62  ? 1.4819 1.5325 2.5458 0.0196  -0.1283 0.2172  62  ASP B CG  
3952 O OD1 . ASP B 62  ? 1.6058 1.6524 2.6429 0.0242  -0.1398 0.2161  62  ASP B OD1 
3953 O OD2 . ASP B 62  ? 1.5812 1.6250 2.6753 0.0136  -0.1316 0.2234  62  ASP B OD2 
3954 N N   . TYR B 63  ? 1.0766 1.1326 2.0753 0.0401  -0.1059 0.1951  63  TYR B N   
3955 C CA  . TYR B 63  ? 1.1312 1.1702 2.1061 0.0474  -0.1131 0.1895  63  TYR B CA  
3956 C C   . TYR B 63  ? 1.1339 1.1784 2.0672 0.0612  -0.1157 0.1823  63  TYR B C   
3957 O O   . TYR B 63  ? 1.1947 1.2212 2.0995 0.0705  -0.1308 0.1789  63  TYR B O   
3958 C CB  . TYR B 63  ? 1.1162 1.1550 2.0999 0.0456  -0.1002 0.1866  63  TYR B CB  
3959 C CG  . TYR B 63  ? 1.3994 1.4214 2.3546 0.0534  -0.1063 0.1799  63  TYR B CG  
3960 C CD1 . TYR B 63  ? 1.2491 1.2466 2.1832 0.0577  -0.1268 0.1793  63  TYR B CD1 
3961 C CD2 . TYR B 63  ? 1.3820 1.4091 2.3283 0.0569  -0.0933 0.1739  63  TYR B CD2 
3962 C CE1 . TYR B 63  ? 1.1963 1.1741 2.1004 0.0658  -0.1348 0.1728  63  TYR B CE1 
3963 C CE2 . TYR B 63  ? 1.2654 1.2753 2.1846 0.0642  -0.1001 0.1677  63  TYR B CE2 
3964 C CZ  . TYR B 63  ? 1.2528 1.2374 2.1502 0.0690  -0.1211 0.1670  63  TYR B CZ  
3965 O OH  . TYR B 63  ? 1.2194 1.1822 2.0864 0.0770  -0.1305 0.1606  63  TYR B OH  
3966 N N   . HIS B 64  ? 1.0004 1.0698 1.9302 0.0630  -0.1014 0.1809  64  HIS B N   
3967 C CA  . HIS B 64  ? 1.0526 1.1370 1.9475 0.0765  -0.1002 0.1762  64  HIS B CA  
3968 C C   . HIS B 64  ? 1.1978 1.2833 2.0741 0.0830  -0.1129 0.1789  64  HIS B C   
3969 O O   . HIS B 64  ? 1.3599 1.4400 2.2000 0.0990  -0.1209 0.1735  64  HIS B O   
3970 C CB  . HIS B 64  ? 1.0164 1.1281 1.9155 0.0742  -0.0838 0.1766  64  HIS B CB  
3971 C CG  . HIS B 64  ? 1.0525 1.1606 1.9538 0.0740  -0.0731 0.1710  64  HIS B CG  
3972 N ND1 . HIS B 64  ? 1.1272 1.2324 2.0568 0.0624  -0.0633 0.1730  64  HIS B ND1 
3973 C CD2 . HIS B 64  ? 1.0596 1.1686 1.9368 0.0848  -0.0700 0.1638  64  HIS B CD2 
3974 C CE1 . HIS B 64  ? 1.0282 1.1315 1.9505 0.0653  -0.0546 0.1674  64  HIS B CE1 
3975 N NE2 . HIS B 64  ? 1.1185 1.2236 2.0101 0.0781  -0.0590 0.1618  64  HIS B NE2 
3976 N N   . LEU B 65  ? 1.0710 1.1616 1.9706 0.0718  -0.1152 0.1871  65  LEU B N   
3977 C CA  . LEU B 65  ? 1.2198 1.3136 2.1051 0.0755  -0.1260 0.1914  65  LEU B CA  
3978 C C   . LEU B 65  ? 1.2881 1.3494 2.1538 0.0832  -0.1445 0.1877  65  LEU B C   
3979 O O   . LEU B 65  ? 1.3303 1.3907 2.1609 0.0973  -0.1530 0.1853  65  LEU B O   
3980 C CB  . LEU B 65  ? 1.1559 1.2606 2.0717 0.0604  -0.1244 0.2011  65  LEU B CB  
3981 C CG  . LEU B 65  ? 1.0020 1.1373 1.9252 0.0548  -0.1099 0.2051  65  LEU B CG  
3982 C CD1 . LEU B 65  ? 1.0087 1.1488 1.9607 0.0394  -0.1101 0.2142  65  LEU B CD1 
3983 C CD2 . LEU B 65  ? 0.7404 0.9033 1.6312 0.0666  -0.1072 0.2060  65  LEU B CD2 
3984 N N   . ARG B 66  ? 1.2798 1.3156 2.1662 0.0747  -0.1510 0.1879  66  ARG B N   
3985 C CA  . ARG B 66  ? 1.5247 1.5282 2.3992 0.0764  -0.1729 0.1886  66  ARG B CA  
3986 C C   . ARG B 66  ? 1.5503 1.5262 2.3991 0.0852  -0.1825 0.1811  66  ARG B C   
3987 O O   . ARG B 66  ? 1.5400 1.4920 2.3508 0.0979  -0.1997 0.1764  66  ARG B O   
3988 C CB  . ARG B 66  ? 1.4090 1.4046 2.3246 0.0593  -0.1793 0.1983  66  ARG B CB  
3989 C CG  . ARG B 66  ? 1.2254 1.2424 2.1631 0.0512  -0.1733 0.2056  66  ARG B CG  
3990 C CD  . ARG B 66  ? 1.2102 1.2125 2.1797 0.0386  -0.1860 0.2145  66  ARG B CD  
3991 N NE  . ARG B 66  ? 1.3457 1.3675 2.3519 0.0277  -0.1750 0.2211  66  ARG B NE  
3992 C CZ  . ARG B 66  ? 1.3395 1.3684 2.3510 0.0235  -0.1793 0.2268  66  ARG B CZ  
3993 N NH1 . ARG B 66  ? 1.3430 1.3621 2.3278 0.0285  -0.1943 0.2276  66  ARG B NH1 
3994 N NH2 . ARG B 66  ? 1.1947 1.2380 2.2361 0.0148  -0.1697 0.2316  66  ARG B NH2 
3995 N N   . ASP B 67  ? 1.3957 1.3739 2.2631 0.0791  -0.1717 0.1799  67  ASP B N   
3996 C CA  . ASP B 67  ? 1.4268 1.3764 2.2797 0.0816  -0.1822 0.1758  67  ASP B CA  
3997 C C   . ASP B 67  ? 1.5089 1.4640 2.3262 0.0982  -0.1744 0.1649  67  ASP B C   
3998 O O   . ASP B 67  ? 1.6998 1.6283 2.4903 0.1059  -0.1858 0.1590  67  ASP B O   
3999 C CB  . ASP B 67  ? 1.5004 1.4475 2.3970 0.0636  -0.1786 0.1840  67  ASP B CB  
4000 C CG  . ASP B 67  ? 1.6945 1.6429 2.6281 0.0495  -0.1848 0.1955  67  ASP B CG  
4001 O OD1 . ASP B 67  ? 1.8878 1.8118 2.8118 0.0482  -0.2069 0.1992  67  ASP B OD1 
4002 O OD2 . ASP B 67  ? 1.7843 1.7565 2.7543 0.0408  -0.1687 0.2006  67  ASP B OD2 
4003 N N   . VAL B 68  ? 1.5614 1.5511 2.3781 0.1034  -0.1563 0.1632  68  VAL B N   
4004 C CA  . VAL B 68  ? 1.3993 1.4006 2.1838 0.1202  -0.1485 0.1544  68  VAL B CA  
4005 C C   . VAL B 68  ? 1.3453 1.3536 2.0914 0.1391  -0.1554 0.1513  68  VAL B C   
4006 O O   . VAL B 68  ? 1.3703 1.3536 2.0760 0.1562  -0.1699 0.1438  68  VAL B O   
4007 C CB  . VAL B 68  ? 1.3358 1.3707 2.1396 0.1152  -0.1255 0.1549  68  VAL B CB  
4008 C CG1 . VAL B 68  ? 1.2796 1.3290 2.0492 0.1338  -0.1195 0.1470  68  VAL B CG1 
4009 C CG2 . VAL B 68  ? 1.2731 1.2989 2.1082 0.1003  -0.1182 0.1566  68  VAL B CG2 
4010 N N   . PHE B 69  ? 1.2484 1.2890 2.0060 0.1360  -0.1462 0.1579  69  PHE B N   
4011 C CA  . PHE B 69  ? 1.3133 1.3724 2.0361 0.1547  -0.1473 0.1569  69  PHE B CA  
4012 C C   . PHE B 69  ? 1.4332 1.4685 2.1378 0.1594  -0.1664 0.1583  69  PHE B C   
4013 O O   . PHE B 69  ? 1.4663 1.5109 2.1349 0.1784  -0.1697 0.1565  69  PHE B O   
4014 C CB  . PHE B 69  ? 1.3077 1.4152 2.0484 0.1488  -0.1298 0.1654  69  PHE B CB  
4015 C CG  . PHE B 69  ? 1.3596 1.4917 2.1095 0.1475  -0.1129 0.1639  69  PHE B CG  
4016 C CD1 . PHE B 69  ? 1.4935 1.6423 2.2111 0.1682  -0.1082 0.1581  69  PHE B CD1 
4017 C CD2 . PHE B 69  ? 1.3480 1.4847 2.1369 0.1271  -0.1025 0.1680  69  PHE B CD2 
4018 C CE1 . PHE B 69  ? 1.6127 1.7835 2.3394 0.1661  -0.0940 0.1575  69  PHE B CE1 
4019 C CE2 . PHE B 69  ? 1.5272 1.6831 2.3219 0.1258  -0.0886 0.1666  69  PHE B CE2 
4020 C CZ  . PHE B 69  ? 1.6266 1.7998 2.3913 0.1442  -0.0847 0.1618  69  PHE B CZ  
4021 N N   . ARG B 70  ? 1.4554 1.4620 2.1848 0.1428  -0.1784 0.1624  70  ARG B N   
4022 C CA  . ARG B 70  ? 1.7524 1.7275 2.4656 0.1448  -0.2004 0.1638  70  ARG B CA  
4023 C C   . ARG B 70  ? 1.6578 1.6567 2.3637 0.1485  -0.1987 0.1698  70  ARG B C   
4024 O O   . ARG B 70  ? 1.7445 1.7296 2.4097 0.1655  -0.2116 0.1667  70  ARG B O   
4025 C CB  . ARG B 70  ? 2.3216 2.2532 2.9881 0.1624  -0.2209 0.1538  70  ARG B CB  
4026 C CG  . ARG B 70  ? 2.4957 2.4327 3.1066 0.1927  -0.2212 0.1444  70  ARG B CG  
4027 C CD  . ARG B 70  ? 2.3051 2.1900 2.8641 0.2111  -0.2483 0.1356  70  ARG B CD  
4028 N NE  . ARG B 70  ? 2.3949 2.2900 2.9008 0.2421  -0.2481 0.1287  70  ARG B NE  
4029 C CZ  . ARG B 70  ? 2.7018 2.6000 3.1687 0.2677  -0.2443 0.1184  70  ARG B CZ  
4030 N NH1 . ARG B 70  ? 2.5842 2.4751 3.0582 0.2651  -0.2405 0.1132  70  ARG B NH1 
4031 N NH2 . ARG B 70  ? 3.0326 2.9431 3.4525 0.2972  -0.2440 0.1137  70  ARG B NH2 
4032 N N   . PHE B 71  ? 1.4806 1.5132 2.2239 0.1326  -0.1838 0.1790  71  PHE B N   
4033 C CA  . PHE B 71  ? 1.4948 1.5496 2.2341 0.1326  -0.1832 0.1868  71  PHE B CA  
4034 C C   . PHE B 71  ? 1.7188 1.7418 2.4624 0.1249  -0.2031 0.1908  71  PHE B C   
4035 O O   . PHE B 71  ? 2.0338 2.0389 2.8129 0.1075  -0.2083 0.1942  71  PHE B O   
4036 C CB  . PHE B 71  ? 1.3871 1.4795 2.1654 0.1150  -0.1662 0.1966  71  PHE B CB  
4037 C CG  . PHE B 71  ? 1.6154 1.7468 2.3838 0.1233  -0.1484 0.1962  71  PHE B CG  
4038 C CD1 . PHE B 71  ? 1.5743 1.7326 2.3072 0.1416  -0.1457 0.1977  71  PHE B CD1 
4039 C CD2 . PHE B 71  ? 1.7143 1.8567 2.5083 0.1135  -0.1347 0.1952  71  PHE B CD2 
4040 C CE1 . PHE B 71  ? 1.5414 1.7399 2.2682 0.1486  -0.1299 0.1995  71  PHE B CE1 
4041 C CE2 . PHE B 71  ? 1.8108 1.9888 2.5961 0.1201  -0.1202 0.1960  71  PHE B CE2 
4042 C CZ  . PHE B 71  ? 1.6242 1.8316 2.3777 0.1371  -0.1180 0.1988  71  PHE B CZ  
4043 N N   . ASP B 72  ? 1.9391 1.9576 2.6464 0.1387  -0.2138 0.1910  72  ASP B N   
4044 C CA  . ASP B 72  ? 2.0780 2.0685 2.7857 0.1319  -0.2333 0.1957  72  ASP B CA  
4045 C C   . ASP B 72  ? 1.7208 1.7326 2.4753 0.1091  -0.2267 0.2078  72  ASP B C   
4046 O O   . ASP B 72  ? 1.5806 1.6314 2.3509 0.1038  -0.2089 0.2130  72  ASP B O   
4047 C CB  . ASP B 72  ? 2.6609 2.6395 3.3126 0.1549  -0.2459 0.1919  72  ASP B CB  
4048 C CG  . ASP B 72  ? 3.2307 3.2562 3.8631 0.1670  -0.2303 0.1964  72  ASP B CG  
4049 O OD1 . ASP B 72  ? 3.5394 3.5910 4.1984 0.1516  -0.2240 0.2079  72  ASP B OD1 
4050 O OD2 . ASP B 72  ? 3.3332 3.3696 3.9240 0.1918  -0.2252 0.1894  72  ASP B OD2 
4051 N N   . GLU B 73  ? 1.6852 1.6695 2.4611 0.0955  -0.2427 0.2127  73  GLU B N   
4052 C CA  . GLU B 73  ? 1.7988 1.7955 2.6217 0.0743  -0.2392 0.2231  73  GLU B CA  
4053 C C   . GLU B 73  ? 1.8767 1.9026 2.6931 0.0732  -0.2338 0.2310  73  GLU B C   
4054 O O   . GLU B 73  ? 1.5297 1.5814 2.3776 0.0597  -0.2214 0.2379  73  GLU B O   
4055 C CB  . GLU B 73  ? 1.8123 1.7746 2.6571 0.0622  -0.2594 0.2276  73  GLU B CB  
4056 C CG  . GLU B 73  ? 1.9785 1.9266 2.8558 0.0528  -0.2593 0.2266  73  GLU B CG  
4057 C CD  . GLU B 73  ? 1.9175 1.8944 2.8290 0.0453  -0.2359 0.2267  73  GLU B CD  
4058 O OE1 . GLU B 73  ? 1.9974 1.9987 2.9329 0.0367  -0.2245 0.2324  73  GLU B OE1 
4059 O OE2 . GLU B 73  ? 1.7063 1.6781 2.6186 0.0481  -0.2304 0.2212  73  GLU B OE2 
4060 N N   . PRO B 74  ? 2.1947 2.2153 2.9694 0.0868  -0.2442 0.2311  74  PRO B N   
4061 C CA  . PRO B 74  ? 2.1912 2.2451 2.9556 0.0870  -0.2374 0.2399  74  PRO B CA  
4062 C C   . PRO B 74  ? 2.2661 2.3671 3.0395 0.0855  -0.2148 0.2438  74  PRO B C   
4063 O O   . PRO B 74  ? 2.4820 2.6051 3.2847 0.0686  -0.2082 0.2539  74  PRO B O   
4064 C CB  . PRO B 74  ? 2.4462 2.4865 3.1535 0.1100  -0.2492 0.2355  74  PRO B CB  
4065 C CG  . PRO B 74  ? 2.5765 2.5629 3.2777 0.1107  -0.2717 0.2287  74  PRO B CG  
4066 C CD  . PRO B 74  ? 2.5066 2.4868 3.2411 0.1018  -0.2648 0.2238  74  PRO B CD  
4067 N N   . ALA B 75  ? 2.1678 2.2819 2.9163 0.1026  -0.2045 0.2360  75  ALA B N   
4068 C CA  . ALA B 75  ? 2.1429 2.3048 2.8929 0.1038  -0.1851 0.2412  75  ALA B CA  
4069 C C   . ALA B 75  ? 1.9353 2.1063 2.7298 0.0847  -0.1736 0.2430  75  ALA B C   
4070 O O   . ALA B 75  ? 2.0659 2.2743 2.8699 0.0785  -0.1604 0.2507  75  ALA B O   
4071 C CB  . ALA B 75  ? 2.4696 2.6422 3.1779 0.1301  -0.1790 0.2325  75  ALA B CB  
4072 N N   . LEU B 76  ? 1.7605 1.8979 2.5818 0.0751  -0.1795 0.2374  76  LEU B N   
4073 C CA  . LEU B 76  ? 1.7203 1.8605 2.5750 0.0638  -0.1681 0.2352  76  LEU B CA  
4074 C C   . LEU B 76  ? 1.5350 1.7019 2.4164 0.0466  -0.1596 0.2463  76  LEU B C   
4075 O O   . LEU B 76  ? 1.4318 1.6178 2.3234 0.0427  -0.1465 0.2465  76  LEU B O   
4076 C CB  . LEU B 76  ? 1.6894 1.7942 2.5714 0.0558  -0.1752 0.2304  76  LEU B CB  
4077 C CG  . LEU B 76  ? 1.4048 1.5143 2.3250 0.0427  -0.1628 0.2306  76  LEU B CG  
4078 C CD1 . LEU B 76  ? 1.4178 1.5388 2.3298 0.0500  -0.1487 0.2232  76  LEU B CD1 
4079 C CD2 . LEU B 76  ? 1.3447 1.4261 2.2960 0.0339  -0.1705 0.2302  76  LEU B CD2 
4080 N N   . ALA B 77  ? 1.2711 1.4343 2.1630 0.0359  -0.1694 0.2554  77  ALA B N   
4081 C CA  . ALA B 77  ? 1.2082 1.3882 2.1243 0.0181  -0.1664 0.2665  77  ALA B CA  
4082 C C   . ALA B 77  ? 1.3185 1.5404 2.2194 0.0187  -0.1557 0.2745  77  ALA B C   
4083 O O   . ALA B 77  ? 1.3188 1.5549 2.2376 0.0069  -0.1479 0.2792  77  ALA B O   
4084 C CB  . ALA B 77  ? 1.2754 1.4441 2.1960 0.0100  -0.1809 0.2747  77  ALA B CB  
4085 N N   . ASP B 78  ? 1.5298 1.7705 2.3962 0.0333  -0.1563 0.2765  78  ASP B N   
4086 C CA  . ASP B 78  ? 1.8345 2.1219 2.6847 0.0364  -0.1463 0.2865  78  ASP B CA  
4087 C C   . ASP B 78  ? 1.8202 2.1218 2.6744 0.0401  -0.1326 0.2808  78  ASP B C   
4088 O O   . ASP B 78  ? 1.9292 2.2612 2.7940 0.0290  -0.1253 0.2910  78  ASP B O   
4089 C CB  . ASP B 78  ? 2.1479 2.4522 2.9579 0.0566  -0.1482 0.2880  78  ASP B CB  
4090 C CG  . ASP B 78  ? 2.4901 2.8487 3.2825 0.0642  -0.1357 0.2984  78  ASP B CG  
4091 O OD1 . ASP B 78  ? 2.7111 3.1015 3.5173 0.0472  -0.1340 0.3157  78  ASP B OD1 
4092 O OD2 . ASP B 78  ? 2.6094 2.9785 3.3756 0.0868  -0.1286 0.2900  78  ASP B OD2 
4093 N N   . VAL B 79  ? 1.7261 2.0032 2.5710 0.0547  -0.1313 0.2653  79  VAL B N   
4094 C CA  . VAL B 79  ? 1.7292 2.0134 2.5747 0.0604  -0.1196 0.2576  79  VAL B CA  
4095 C C   . VAL B 79  ? 1.4920 1.7722 2.3727 0.0399  -0.1148 0.2605  79  VAL B C   
4096 O O   . VAL B 79  ? 1.2823 1.5875 2.1665 0.0358  -0.1052 0.2645  79  VAL B O   
4097 C CB  . VAL B 79  ? 2.0495 2.2985 2.8804 0.0765  -0.1235 0.2411  79  VAL B CB  
4098 C CG1 . VAL B 79  ? 2.4973 2.7497 3.3282 0.0824  -0.1124 0.2326  79  VAL B CG1 
4099 C CG2 . VAL B 79  ? 2.1934 2.4404 2.9835 0.0984  -0.1310 0.2376  79  VAL B CG2 
4100 N N   . ARG B 80  ? 1.3145 1.5623 2.2192 0.0285  -0.1224 0.2586  80  ARG B N   
4101 C CA  . ARG B 80  ? 1.1517 1.3886 2.0871 0.0122  -0.1192 0.2597  80  ARG B CA  
4102 C C   . ARG B 80  ? 1.1395 1.4034 2.0808 -0.0028 -0.1188 0.2744  80  ARG B C   
4103 O O   . ARG B 80  ? 1.0984 1.3676 2.0497 -0.0109 -0.1126 0.2757  80  ARG B O   
4104 C CB  . ARG B 80  ? 1.1409 1.3424 2.1044 0.0040  -0.1251 0.2557  80  ARG B CB  
4105 C CG  . ARG B 80  ? 1.0817 1.2796 2.0679 -0.0089 -0.1197 0.2577  80  ARG B CG  
4106 C CD  . ARG B 80  ? 0.9532 1.1552 1.9388 -0.0063 -0.1069 0.2511  80  ARG B CD  
4107 N NE  . ARG B 80  ? 1.1767 1.3622 2.1828 -0.0150 -0.1029 0.2492  80  ARG B NE  
4108 C CZ  . ARG B 80  ? 1.4508 1.6094 2.4774 -0.0142 -0.1007 0.2421  80  ARG B CZ  
4109 N NH1 . ARG B 80  ? 1.2823 1.4245 2.3191 -0.0079 -0.1033 0.2371  80  ARG B NH1 
4110 N NH2 . ARG B 80  ? 1.5369 1.6850 2.5741 -0.0196 -0.0962 0.2410  80  ARG B NH2 
4111 N N   . ARG B 81  ? 1.1929 1.4715 2.1263 -0.0070 -0.1268 0.2860  81  ARG B N   
4112 C CA  . ARG B 81  ? 1.3482 1.6542 2.2854 -0.0232 -0.1295 0.3033  81  ARG B CA  
4113 C C   . ARG B 81  ? 1.4584 1.8027 2.3853 -0.0216 -0.1191 0.3091  81  ARG B C   
4114 O O   . ARG B 81  ? 1.4007 1.7534 2.3400 -0.0381 -0.1198 0.3185  81  ARG B O   
4115 C CB  . ARG B 81  ? 1.4545 1.7717 2.3802 -0.0244 -0.1391 0.3142  81  ARG B CB  
4116 C CG  . ARG B 81  ? 1.6554 2.0119 2.5766 -0.0380 -0.1417 0.3352  81  ARG B CG  
4117 C CD  . ARG B 81  ? 2.0555 2.4216 2.9628 -0.0373 -0.1505 0.3452  81  ARG B CD  
4118 N NE  . ARG B 81  ? 2.0485 2.3824 2.9700 -0.0496 -0.1649 0.3474  81  ARG B NE  
4119 C CZ  . ARG B 81  ? 1.7286 2.0605 2.6654 -0.0714 -0.1748 0.3611  81  ARG B CZ  
4120 N NH1 . ARG B 81  ? 1.7249 2.0797 2.6678 -0.0861 -0.1732 0.3734  81  ARG B NH1 
4121 N NH2 . ARG B 81  ? 1.5243 1.8294 2.4696 -0.0792 -0.1882 0.3631  81  ARG B NH2 
4122 N N   . ARG B 82  ? 1.5726 1.9343 2.4777 -0.0016 -0.1104 0.3022  82  ARG B N   
4123 C CA  . ARG B 82  ? 1.3759 1.7789 2.2711 0.0020  -0.1006 0.3088  82  ARG B CA  
4124 C C   . ARG B 82  ? 1.4621 1.8513 2.3653 0.0034  -0.0925 0.2974  82  ARG B C   
4125 O O   . ARG B 82  ? 1.7116 2.1286 2.6022 0.0138  -0.0837 0.2972  82  ARG B O   
4126 C CB  . ARG B 82  ? 1.1683 1.6017 2.0328 0.0252  -0.0957 0.3088  82  ARG B CB  
4127 C CG  . ARG B 82  ? 1.2009 1.6607 2.0558 0.0221  -0.1017 0.3250  82  ARG B CG  
4128 C CD  . ARG B 82  ? 1.2811 1.7695 2.1016 0.0486  -0.0965 0.3244  82  ARG B CD  
4129 N NE  . ARG B 82  ? 1.3067 1.7523 2.1092 0.0671  -0.1019 0.3057  82  ARG B NE  
4130 C CZ  . ARG B 82  ? 1.4950 1.9291 2.2758 0.0905  -0.0975 0.2899  82  ARG B CZ  
4131 N NH1 . ARG B 82  ? 1.3855 1.8476 2.1608 0.0998  -0.0862 0.2890  82  ARG B NH1 
4132 N NH2 . ARG B 82  ? 1.8103 2.2012 2.5755 0.1033  -0.1063 0.2753  82  ARG B NH2 
4133 N N   . LEU B 83  ? 1.4467 1.7958 2.3699 -0.0060 -0.0953 0.2889  83  LEU B N   
4134 C CA  . LEU B 83  ? 1.3175 1.6482 2.2476 -0.0043 -0.0878 0.2773  83  LEU B CA  
4135 C C   . LEU B 83  ? 1.3834 1.6938 2.3350 -0.0238 -0.0919 0.2811  83  LEU B C   
4136 O O   . LEU B 83  ? 1.4997 1.7857 2.4652 -0.0325 -0.1001 0.2823  83  LEU B O   
4137 C CB  . LEU B 83  ? 1.2011 1.4997 2.1280 0.0109  -0.0855 0.2596  83  LEU B CB  
4138 C CG  . LEU B 83  ? 1.3113 1.5885 2.2464 0.0122  -0.0777 0.2479  83  LEU B CG  
4139 C CD1 . LEU B 83  ? 1.4896 1.7945 2.4089 0.0198  -0.0689 0.2477  83  LEU B CD1 
4140 C CD2 . LEU B 83  ? 1.4995 1.7428 2.4375 0.0220  -0.0785 0.2342  83  LEU B CD2 
4141 N N   . THR B 84  ? 1.2905 1.6086 2.2425 -0.0289 -0.0866 0.2822  84  THR B N   
4142 C CA  . THR B 84  ? 1.4199 1.7138 2.3856 -0.0439 -0.0903 0.2833  84  THR B CA  
4143 C C   . THR B 84  ? 1.3086 1.5858 2.2731 -0.0367 -0.0803 0.2700  84  THR B C   
4144 O O   . THR B 84  ? 1.1756 1.4740 2.1283 -0.0285 -0.0725 0.2678  84  THR B O   
4145 C CB  . THR B 84  ? 1.5724 1.8886 2.5384 -0.0632 -0.0990 0.3025  84  THR B CB  
4146 O OG1 . THR B 84  ? 1.8330 2.1713 2.7968 -0.0663 -0.1058 0.3146  84  THR B OG1 
4147 C CG2 . THR B 84  ? 1.4773 1.7575 2.4544 -0.0786 -0.1086 0.3037  84  THR B CG2 
4148 N N   . LEU B 85  ? 1.2311 1.4703 2.2079 -0.0404 -0.0813 0.2622  85  LEU B N   
4149 C CA  . LEU B 85  ? 1.2146 1.4323 2.1914 -0.0342 -0.0720 0.2496  85  LEU B CA  
4150 C C   . LEU B 85  ? 1.1597 1.3560 2.1392 -0.0469 -0.0771 0.2527  85  LEU B C   
4151 O O   . LEU B 85  ? 1.2710 1.4457 2.2595 -0.0543 -0.0858 0.2557  85  LEU B O   
4152 C CB  . LEU B 85  ? 1.3687 1.5591 2.3559 -0.0228 -0.0667 0.2363  85  LEU B CB  
4153 C CG  . LEU B 85  ? 1.3866 1.5843 2.3716 -0.0113 -0.0663 0.2324  85  LEU B CG  
4154 C CD1 . LEU B 85  ? 1.5251 1.6944 2.5230 -0.0038 -0.0617 0.2213  85  LEU B CD1 
4155 C CD2 . LEU B 85  ? 1.2886 1.5113 2.2539 -0.0005 -0.0613 0.2303  85  LEU B CD2 
4156 N N   . LEU B 86  ? 1.1121 1.3132 2.0814 -0.0485 -0.0729 0.2519  86  LEU B N   
4157 C CA  . LEU B 86  ? 1.2422 1.4265 2.2075 -0.0619 -0.0809 0.2575  86  LEU B CA  
4158 C C   . LEU B 86  ? 1.2260 1.3897 2.1836 -0.0548 -0.0716 0.2453  86  LEU B C   
4159 O O   . LEU B 86  ? 1.1671 1.3462 2.1184 -0.0450 -0.0609 0.2390  86  LEU B O   
4160 C CB  . LEU B 86  ? 1.1231 1.3428 2.0821 -0.0767 -0.0903 0.2761  86  LEU B CB  
4161 C CG  . LEU B 86  ? 0.9668 1.2131 1.9314 -0.0825 -0.0978 0.2893  86  LEU B CG  
4162 C CD1 . LEU B 86  ? 0.7143 1.0118 1.6726 -0.0894 -0.0996 0.3064  86  LEU B CD1 
4163 C CD2 . LEU B 86  ? 0.9271 1.1445 1.8983 -0.0965 -0.1132 0.2960  86  LEU B CD2 
4164 N N   . THR B 87  ? 1.1949 1.3219 2.1499 -0.0598 -0.0772 0.2428  87  THR B N   
4165 C CA  . THR B 87  ? 1.3241 1.4262 2.2682 -0.0545 -0.0705 0.2325  87  THR B CA  
4166 C C   . THR B 87  ? 1.4399 1.5248 2.3698 -0.0695 -0.0848 0.2409  87  THR B C   
4167 O O   . THR B 87  ? 1.4575 1.5216 2.3872 -0.0789 -0.0989 0.2472  87  THR B O   
4168 C CB  . THR B 87  ? 1.4018 1.4711 2.3532 -0.0408 -0.0616 0.2186  87  THR B CB  
4169 O OG1 . THR B 87  ? 1.6711 1.7619 2.6316 -0.0298 -0.0499 0.2131  87  THR B OG1 
4170 C CG2 . THR B 87  ? 1.4999 1.5412 2.4380 -0.0340 -0.0543 0.2082  87  THR B CG2 
4171 N N   . PRO B 88  ? 1.5390 1.6337 2.4564 -0.0727 -0.0832 0.2423  88  PRO B N   
4172 C CA  . PRO B 88  ? 1.5439 1.6133 2.4445 -0.0847 -0.0961 0.2471  88  PRO B CA  
4173 C C   . PRO B 88  ? 1.4758 1.4902 2.3671 -0.0793 -0.1000 0.2368  88  PRO B C   
4174 O O   . PRO B 88  ? 1.4754 1.4720 2.3705 -0.0618 -0.0856 0.2219  88  PRO B O   
4175 C CB  . PRO B 88  ? 1.6503 1.7306 2.5409 -0.0785 -0.0853 0.2410  88  PRO B CB  
4176 C CG  . PRO B 88  ? 1.4566 1.5876 2.3587 -0.0733 -0.0757 0.2447  88  PRO B CG  
4177 C CD  . PRO B 88  ? 1.5308 1.6591 2.4477 -0.0640 -0.0702 0.2390  88  PRO B CD  
4178 N N   . ALA B 89  ? 1.4587 1.4471 2.3363 -0.0942 -0.1204 0.2461  89  ALA B N   
4179 C CA  . ALA B 89  ? 1.7697 1.7014 2.6317 -0.0889 -0.1284 0.2375  89  ALA B CA  
4180 C C   . ALA B 89  ? 1.8843 1.7876 2.7279 -0.0751 -0.1173 0.2225  89  ALA B C   
4181 O O   . ALA B 89  ? 1.9450 1.8057 2.7771 -0.0616 -0.1153 0.2107  89  ALA B O   
4182 C CB  . ALA B 89  ? 1.8870 1.7963 2.7347 -0.1098 -0.1564 0.2524  89  ALA B CB  
4183 N N   . SER B 90  ? 1.9908 1.9188 2.8310 -0.0774 -0.1100 0.2234  90  SER B N   
4184 C CA  . SER B 90  ? 2.1199 2.0263 2.9428 -0.0655 -0.0987 0.2103  90  SER B CA  
4185 C C   . SER B 90  ? 2.0768 1.9933 2.9136 -0.0444 -0.0737 0.1957  90  SER B C   
4186 O O   . SER B 90  ? 2.0419 1.9977 2.8995 -0.0421 -0.0637 0.1974  90  SER B O   
4187 C CB  . SER B 90  ? 2.2065 2.1356 3.0211 -0.0769 -0.1023 0.2179  90  SER B CB  
4188 O OG  . SER B 90  ? 2.2841 2.1901 3.0808 -0.0652 -0.0917 0.2048  90  SER B OG  
4189 N N   . ARG B 91  ? 2.0042 1.8836 2.8270 -0.0289 -0.0648 0.1821  91  ARG B N   
4190 C CA  . ARG B 91  ? 2.1339 2.0220 2.9683 -0.0106 -0.0417 0.1702  91  ARG B CA  
4191 C C   . ARG B 91  ? 2.2162 2.0914 3.0301 -0.0041 -0.0324 0.1618  91  ARG B C   
4192 O O   . ARG B 91  ? 2.3122 2.1870 3.1296 0.0108  -0.0141 0.1520  91  ARG B O   
4193 C CB  . ARG B 91  ? 2.1053 1.9729 2.9492 0.0033  -0.0365 0.1641  91  ARG B CB  
4194 C CG  . ARG B 91  ? 2.0729 1.9666 2.9434 0.0155  -0.0176 0.1596  91  ARG B CG  
4195 C CD  . ARG B 91  ? 2.3296 2.2120 3.2156 0.0261  -0.0156 0.1579  91  ARG B CD  
4196 N NE  . ARG B 91  ? 2.5529 2.4569 3.4621 0.0379  0.0028  0.1540  91  ARG B NE  
4197 C CZ  . ARG B 91  ? 2.6437 2.5362 3.5585 0.0549  0.0160  0.1479  91  ARG B CZ  
4198 N NH1 . ARG B 91  ? 2.6976 2.5550 3.5932 0.0658  0.0148  0.1426  91  ARG B NH1 
4199 N NH2 . ARG B 91  ? 2.6233 2.5397 3.5621 0.0616  0.0299  0.1479  91  ARG B NH2 
4200 N N   . ALA B 92  ? 2.1442 2.0099 2.9372 -0.0167 -0.0460 0.1671  92  ALA B N   
4201 C CA  . ALA B 92  ? 2.1326 1.9886 2.9057 -0.0131 -0.0395 0.1607  92  ALA B CA  
4202 C C   . ALA B 92  ? 2.1140 2.0139 2.9033 -0.0118 -0.0262 0.1607  92  ALA B C   
4203 O O   . ALA B 92  ? 2.0324 1.9701 2.8410 -0.0194 -0.0293 0.1696  92  ALA B O   
4204 C CB  . ALA B 92  ? 2.1108 1.9480 2.8599 -0.0291 -0.0603 0.1687  92  ALA B CB  
4205 N N   . ALA B 93  ? 2.2243 2.1169 3.0031 -0.0011 -0.0121 0.1508  93  ALA B N   
4206 C CA  . ALA B 93  ? 2.2020 2.1288 2.9926 0.0027  0.0000  0.1489  93  ALA B CA  
4207 C C   . ALA B 93  ? 1.8361 1.7830 2.6178 -0.0084 -0.0089 0.1559  93  ALA B C   
4208 O O   . ALA B 93  ? 1.5933 1.5272 2.3565 -0.0066 -0.0065 0.1512  93  ALA B O   
4209 C CB  . ALA B 93  ? 2.2446 2.1568 3.0296 0.0181  0.0183  0.1369  93  ALA B CB  
4210 N N   . ARG B 94  ? 1.6594 1.6399 2.4549 -0.0196 -0.0193 0.1682  94  ARG B N   
4211 C CA  . ARG B 94  ? 1.6125 1.6212 2.4042 -0.0301 -0.0282 0.1781  94  ARG B CA  
4212 C C   . ARG B 94  ? 1.6899 1.7483 2.5021 -0.0291 -0.0255 0.1850  94  ARG B C   
4213 O O   . ARG B 94  ? 1.8150 1.8806 2.6426 -0.0243 -0.0211 0.1839  94  ARG B O   
4214 C CB  . ARG B 94  ? 1.5910 1.5880 2.3739 -0.0483 -0.0492 0.1912  94  ARG B CB  
4215 C CG  . ARG B 94  ? 1.8696 1.8097 2.6278 -0.0479 -0.0552 0.1840  94  ARG B CG  
4216 C CD  . ARG B 94  ? 2.0471 1.9736 2.7964 -0.0672 -0.0795 0.1983  94  ARG B CD  
4217 N NE  . ARG B 94  ? 2.1765 2.1507 2.9369 -0.0819 -0.0883 0.2148  94  ARG B NE  
4218 C CZ  . ARG B 94  ? 2.5928 2.5693 3.3487 -0.1027 -0.1107 0.2322  94  ARG B CZ  
4219 N NH1 . ARG B 94  ? 2.8837 2.8107 3.6201 -0.1114 -0.1283 0.2337  94  ARG B NH1 
4220 N NH2 . ARG B 94  ? 2.7272 2.7550 3.4969 -0.1144 -0.1162 0.2488  94  ARG B NH2 
4221 N N   . PRO B 95  ? 1.7524 1.8462 2.5639 -0.0317 -0.0277 0.1920  95  PRO B N   
4222 C CA  . PRO B 95  ? 1.7348 1.8770 2.5614 -0.0286 -0.0261 0.1994  95  PRO B CA  
4223 C C   . PRO B 95  ? 1.6089 1.7628 2.4499 -0.0380 -0.0347 0.2106  95  PRO B C   
4224 O O   . PRO B 95  ? 1.5533 1.6919 2.3918 -0.0531 -0.0481 0.2199  95  PRO B O   
4225 C CB  . PRO B 95  ? 1.8233 1.9970 2.6443 -0.0344 -0.0324 0.2098  95  PRO B CB  
4226 C CG  . PRO B 95  ? 1.9368 2.0768 2.7393 -0.0311 -0.0289 0.1989  95  PRO B CG  
4227 C CD  . PRO B 95  ? 1.8939 1.9829 2.6887 -0.0352 -0.0312 0.1925  95  PRO B CD  
4228 N N   . LEU B 96  ? 1.4373 1.6154 2.2910 -0.0291 -0.0285 0.2098  96  LEU B N   
4229 C CA  . LEU B 96  ? 1.5047 1.6893 2.3719 -0.0354 -0.0346 0.2177  96  LEU B CA  
4230 C C   . LEU B 96  ? 1.9544 2.1717 2.8255 -0.0522 -0.0487 0.2383  96  LEU B C   
4231 O O   . LEU B 96  ? 2.2521 2.4588 3.1284 -0.0654 -0.0599 0.2473  96  LEU B O   
4232 C CB  . LEU B 96  ? 1.2646 1.4660 2.1413 -0.0215 -0.0258 0.2119  96  LEU B CB  
4233 C CG  . LEU B 96  ? 1.4149 1.6303 2.3050 -0.0278 -0.0328 0.2218  96  LEU B CG  
4234 C CD1 . LEU B 96  ? 1.6805 1.8579 2.5760 -0.0362 -0.0388 0.2209  96  LEU B CD1 
4235 C CD2 . LEU B 96  ? 1.5726 1.8040 2.4683 -0.0140 -0.0262 0.2168  96  LEU B CD2 
4236 N N   . ASP B 97  ? 2.1304 2.3894 2.9999 -0.0508 -0.0479 0.2463  97  ASP B N   
4237 C CA  . ASP B 97  ? 1.8502 2.1523 2.7263 -0.0656 -0.0594 0.2688  97  ASP B CA  
4238 C C   . ASP B 97  ? 1.7259 2.0033 2.5976 -0.0881 -0.0766 0.2800  97  ASP B C   
4239 O O   . ASP B 97  ? 1.5542 1.8425 2.4332 -0.1053 -0.0903 0.2972  97  ASP B O   
4240 C CB  . ASP B 97  ? 1.7293 2.0817 2.6044 -0.0558 -0.0535 0.2742  97  ASP B CB  
4241 C CG  . ASP B 97  ? 1.9096 2.2471 2.7718 -0.0475 -0.0477 0.2627  97  ASP B CG  
4242 O OD1 . ASP B 97  ? 1.9079 2.1959 2.7609 -0.0508 -0.0485 0.2515  97  ASP B OD1 
4243 O OD2 . ASP B 97  ? 1.9771 2.3520 2.8370 -0.0363 -0.0423 0.2647  97  ASP B OD2 
4244 N N   . SER B 98  ? 1.6507 1.8922 2.5079 -0.0875 -0.0766 0.2700  98  SER B N   
4245 C CA  . SER B 98  ? 1.4841 1.6923 2.3303 -0.1065 -0.0941 0.2777  98  SER B CA  
4246 C C   . SER B 98  ? 1.3498 1.5179 2.1953 -0.1140 -0.1035 0.2768  98  SER B C   
4247 O O   . SER B 98  ? 1.5152 1.6768 2.3593 -0.1344 -0.1235 0.2931  98  SER B O   
4248 C CB  . SER B 98  ? 1.6937 1.8643 2.5209 -0.1002 -0.0903 0.2636  98  SER B CB  
4249 O OG  . SER B 98  ? 1.9170 2.1236 2.7438 -0.0960 -0.0854 0.2669  98  SER B OG  
4250 N N   . LEU B 99  ? 1.2772 1.4193 2.1239 -0.0972 -0.0898 0.2585  99  LEU B N   
4251 C CA  . LEU B 99  ? 1.3735 1.4777 2.2206 -0.0989 -0.0955 0.2545  99  LEU B CA  
4252 C C   . LEU B 99  ? 1.5801 1.7131 2.4421 -0.1127 -0.1073 0.2725  99  LEU B C   
4253 O O   . LEU B 99  ? 1.7342 1.8415 2.5919 -0.1272 -0.1249 0.2811  99  LEU B O   
4254 C CB  . LEU B 99  ? 1.2540 1.3382 2.1051 -0.0776 -0.0769 0.2343  99  LEU B CB  
4255 C CG  . LEU B 99  ? 1.3920 1.4467 2.2280 -0.0646 -0.0650 0.2176  99  LEU B CG  
4256 C CD1 . LEU B 99  ? 1.6429 1.6827 2.4860 -0.0457 -0.0474 0.2013  99  LEU B CD1 
4257 C CD2 . LEU B 99  ? 1.4257 1.4331 2.2394 -0.0724 -0.0778 0.2169  99  LEU B CD2 
4258 N N   . VAL B 100 ? 1.5554 1.7400 2.4321 -0.1069 -0.0979 0.2778  100 VAL B N   
4259 C CA  . VAL B 100 ? 1.7428 1.9633 2.6335 -0.1172 -0.1058 0.2951  100 VAL B CA  
4260 C C   . VAL B 100 ? 1.9499 2.1844 2.8387 -0.1429 -0.1272 0.3192  100 VAL B C   
4261 O O   . VAL B 100 ? 2.1165 2.3445 3.0090 -0.1590 -0.1430 0.3325  100 VAL B O   
4262 C CB  . VAL B 100 ? 1.5184 1.7948 2.4187 -0.1041 -0.0919 0.2970  100 VAL B CB  
4263 C CG1 . VAL B 100 ? 1.3438 1.6680 2.2555 -0.1161 -0.1004 0.3195  100 VAL B CG1 
4264 C CG2 . VAL B 100 ? 1.8157 2.0798 2.7187 -0.0819 -0.0752 0.2769  100 VAL B CG2 
4265 N N   . LEU B 101 ? 1.9605 2.2145 2.8440 -0.1469 -0.1283 0.3254  101 LEU B N   
4266 C CA  . LEU B 101 ? 1.8979 2.1704 2.7809 -0.1722 -0.1490 0.3504  101 LEU B CA  
4267 C C   . LEU B 101 ? 1.8999 2.1116 2.7684 -0.1895 -0.1711 0.3524  101 LEU B C   
4268 O O   . LEU B 101 ? 2.0735 2.2909 2.9450 -0.2126 -0.1922 0.3741  101 LEU B O   
4269 C CB  . LEU B 101 ? 1.7484 2.0461 2.6274 -0.1701 -0.1449 0.3529  101 LEU B CB  
4270 C CG  . LEU B 101 ? 1.5700 1.9202 2.4584 -0.1919 -0.1600 0.3834  101 LEU B CG  
4271 C CD1 . LEU B 101 ? 1.3903 1.8018 2.2980 -0.1968 -0.1592 0.4036  101 LEU B CD1 
4272 C CD2 . LEU B 101 ? 1.4520 1.8311 2.3387 -0.1815 -0.1498 0.3808  101 LEU B CD2 
4273 N N   . GLU B 102 ? 1.9544 2.1082 2.8056 -0.1769 -0.1660 0.3299  102 GLU B N   
4274 C CA  . GLU B 102 ? 1.8953 1.9829 2.7264 -0.1863 -0.1849 0.3267  102 GLU B CA  
4275 C C   . GLU B 102 ? 2.0174 2.0903 2.8545 -0.1932 -0.1958 0.3323  102 GLU B C   
4276 O O   . GLU B 102 ? 2.2077 2.2522 3.0337 -0.2136 -0.2216 0.3458  102 GLU B O   
4277 C CB  . GLU B 102 ? 1.8607 1.8902 2.6704 -0.1683 -0.1758 0.3016  102 GLU B CB  
4278 C CG  . GLU B 102 ? 2.1836 2.2135 2.9801 -0.1694 -0.1755 0.3006  102 GLU B CG  
4279 C CD  . GLU B 102 ? 2.5011 2.4841 3.2790 -0.1477 -0.1604 0.2749  102 GLU B CD  
4280 O OE1 . GLU B 102 ? 2.6383 2.5912 3.4149 -0.1327 -0.1510 0.2597  102 GLU B OE1 
4281 O OE2 . GLU B 102 ? 2.5792 2.5588 3.3447 -0.1460 -0.1580 0.2713  102 GLU B OE2 
4282 N N   . ASP B 103 ? 2.0589 2.1540 2.9135 -0.1791 -0.1792 0.3250  103 ASP B N   
4283 C CA  . ASP B 103 ? 2.4690 2.5527 3.3305 -0.1852 -0.1892 0.3305  103 ASP B CA  
4284 C C   . ASP B 103 ? 2.2273 2.3616 3.1027 -0.2080 -0.2033 0.3591  103 ASP B C   
4285 O O   . ASP B 103 ? 2.0800 2.2672 2.9732 -0.2024 -0.1904 0.3645  103 ASP B O   
4286 C CB  . ASP B 103 ? 2.6904 2.7687 3.5627 -0.1615 -0.1684 0.3107  103 ASP B CB  
4287 C CG  . ASP B 103 ? 2.5527 2.6127 3.4320 -0.1636 -0.1767 0.3123  103 ASP B CG  
4288 O OD1 . ASP B 103 ? 2.4472 2.4964 3.3218 -0.1847 -0.2005 0.3295  103 ASP B OD1 
4289 O OD2 . ASP B 103 ? 2.0233 2.0801 2.9130 -0.1448 -0.1604 0.2973  103 ASP B OD2 
4290 N N   . GLU B 104 ? 1.9215 2.0370 2.7868 -0.2337 -0.2313 0.3781  104 GLU B N   
4291 C CA  . GLU B 104 ? 1.8552 2.0198 2.7327 -0.2593 -0.2474 0.4093  104 GLU B CA  
4292 C C   . GLU B 104 ? 1.7257 1.9178 2.6201 -0.2575 -0.2425 0.4147  104 GLU B C   
4293 O O   . GLU B 104 ? 1.8240 2.0816 2.7351 -0.2628 -0.2370 0.4326  104 GLU B O   
4294 C CB  . GLU B 104 ? 2.0743 2.1943 2.9340 -0.2867 -0.2819 0.4254  104 GLU B CB  
4295 C CG  . GLU B 104 ? 2.0440 2.1446 2.8867 -0.2937 -0.2912 0.4264  104 GLU B CG  
4296 C CD  . GLU B 104 ? 2.2421 2.4156 3.1014 -0.3069 -0.2896 0.4498  104 GLU B CD  
4297 O OE1 . GLU B 104 ? 2.6044 2.8288 3.4787 -0.2878 -0.2625 0.4423  104 GLU B OE1 
4298 O OE2 . GLU B 104 ? 2.1887 2.3668 3.0448 -0.3364 -0.3171 0.4765  104 GLU B OE2 
4299 N N   . ALA B 105 ? 1.5572 1.6973 2.4453 -0.2503 -0.2463 0.4005  105 ALA B N   
4300 C CA  . ALA B 105 ? 1.5958 1.7485 2.4968 -0.2503 -0.2463 0.4049  105 ALA B CA  
4301 C C   . ALA B 105 ? 1.5872 1.7934 2.5056 -0.2301 -0.2187 0.3977  105 ALA B C   
4302 O O   . ALA B 105 ? 1.3844 1.6386 2.3156 -0.2362 -0.2179 0.4137  105 ALA B O   
4303 C CB  . ALA B 105 ? 1.6652 1.7504 2.5560 -0.2400 -0.2515 0.3862  105 ALA B CB  
4304 N N   . LEU B 106 ? 1.8785 2.0727 2.7945 -0.2057 -0.1973 0.3734  106 LEU B N   
4305 C CA  . LEU B 106 ? 2.0890 2.3220 3.0165 -0.1840 -0.1725 0.3627  106 LEU B CA  
4306 C C   . LEU B 106 ? 1.9558 2.2584 2.8903 -0.1895 -0.1683 0.3817  106 LEU B C   
4307 O O   . LEU B 106 ? 1.7260 2.0710 2.6699 -0.1822 -0.1591 0.3867  106 LEU B O   
4308 C CB  . LEU B 106 ? 2.3466 2.5513 3.2682 -0.1604 -0.1538 0.3359  106 LEU B CB  
4309 C CG  . LEU B 106 ? 2.1913 2.4320 3.1197 -0.1386 -0.1304 0.3246  106 LEU B CG  
4310 C CD1 . LEU B 106 ? 2.4371 2.6979 3.3769 -0.1295 -0.1238 0.3237  106 LEU B CD1 
4311 C CD2 . LEU B 106 ? 2.1048 2.3114 3.0265 -0.1194 -0.1155 0.3004  106 LEU B CD2 
4312 N N   . VAL B 107 ? 1.7880 2.1006 2.7169 -0.2015 -0.1757 0.3922  107 VAL B N   
4313 C CA  . VAL B 107 ? 1.7197 2.1005 2.6559 -0.2067 -0.1724 0.4120  107 VAL B CA  
4314 C C   . VAL B 107 ? 1.6798 2.1049 2.6271 -0.2245 -0.1836 0.4395  107 VAL B C   
4315 O O   . VAL B 107 ? 1.6913 2.1773 2.6472 -0.2159 -0.1715 0.4489  107 VAL B O   
4316 C CB  . VAL B 107 ? 1.6215 2.0081 2.5518 -0.2191 -0.1809 0.4219  107 VAL B CB  
4317 C CG1 . VAL B 107 ? 1.5253 1.9901 2.4664 -0.2184 -0.1730 0.4405  107 VAL B CG1 
4318 C CG2 . VAL B 107 ? 1.7626 2.1016 2.6793 -0.2032 -0.1714 0.3957  107 VAL B CG2 
4319 N N   . GLU B 108 ? 1.7846 2.1763 2.7291 -0.2482 -0.2073 0.4519  108 GLU B N   
4320 C CA  . GLU B 108 ? 1.8155 2.2405 2.7689 -0.2698 -0.2223 0.4799  108 GLU B CA  
4321 C C   . GLU B 108 ? 1.4861 1.9333 2.4469 -0.2529 -0.2073 0.4734  108 GLU B C   
4322 O O   . GLU B 108 ? 1.3131 1.8223 2.2828 -0.2560 -0.2037 0.4933  108 GLU B O   
4323 C CB  . GLU B 108 ? 2.0703 2.4342 3.0144 -0.2926 -0.2504 0.4856  108 GLU B CB  
4324 C CG  . GLU B 108 ? 2.2935 2.6533 3.2316 -0.3221 -0.2759 0.5089  108 GLU B CG  
4325 C CD  . GLU B 108 ? 2.4031 2.8363 3.3561 -0.3461 -0.2859 0.5471  108 GLU B CD  
4326 O OE1 . GLU B 108 ? 2.3884 2.8498 3.3505 -0.3503 -0.2860 0.5593  108 GLU B OE1 
4327 O OE2 . GLU B 108 ? 2.5852 3.0488 3.5412 -0.3614 -0.2942 0.5662  108 GLU B OE2 
4328 N N   . THR B 109 ? 1.3685 1.7640 2.3246 -0.2347 -0.1993 0.4460  109 THR B N   
4329 C CA  . THR B 109 ? 1.3588 1.7625 2.3201 -0.2184 -0.1874 0.4367  109 THR B CA  
4330 C C   . THR B 109 ? 1.3036 1.7653 2.2676 -0.1976 -0.1654 0.4346  109 THR B C   
4331 O O   . THR B 109 ? 1.0550 1.5568 2.0226 -0.1941 -0.1613 0.4450  109 THR B O   
4332 C CB  . THR B 109 ? 1.3106 1.6520 2.2692 -0.2037 -0.1836 0.4100  109 THR B CB  
4333 O OG1 . THR B 109 ? 1.5277 1.8153 2.4794 -0.2201 -0.2039 0.4115  109 THR B OG1 
4334 C CG2 . THR B 109 ? 1.3223 1.6696 2.2874 -0.1992 -0.1828 0.4108  109 THR B CG2 
4335 N N   . LEU B 110 ? 1.4988 1.9616 2.4583 -0.1832 -0.1525 0.4210  110 LEU B N   
4336 C CA  . LEU B 110 ? 1.7704 2.2807 2.7283 -0.1604 -0.1326 0.4160  110 LEU B CA  
4337 C C   . LEU B 110 ? 1.9920 2.5758 2.9553 -0.1698 -0.1347 0.4453  110 LEU B C   
4338 O O   . LEU B 110 ? 2.2586 2.8853 3.2203 -0.1535 -0.1229 0.4478  110 LEU B O   
4339 C CB  . LEU B 110 ? 1.5275 2.0255 2.4790 -0.1464 -0.1214 0.3988  110 LEU B CB  
4340 C CG  . LEU B 110 ? 1.2105 1.6467 2.1564 -0.1312 -0.1138 0.3691  110 LEU B CG  
4341 C CD1 . LEU B 110 ? 1.2661 1.6890 2.2046 -0.1240 -0.1068 0.3571  110 LEU B CD1 
4342 C CD2 . LEU B 110 ? 1.3209 1.7575 2.2656 -0.1077 -0.0998 0.3529  110 LEU B CD2 
4343 N N   . ARG B 111 ? 1.8351 2.4317 2.8035 -0.1959 -0.1505 0.4679  111 ARG B N   
4344 C CA  . ARG B 111 ? 1.8747 2.5445 2.8516 -0.2096 -0.1548 0.5007  111 ARG B CA  
4345 C C   . ARG B 111 ? 1.7410 2.4376 2.7218 -0.2151 -0.1582 0.5163  111 ARG B C   
4346 O O   . ARG B 111 ? 1.7700 2.5325 2.7529 -0.2050 -0.1475 0.5304  111 ARG B O   
4347 C CB  . ARG B 111 ? 2.2219 2.8876 3.2040 -0.2422 -0.1772 0.5233  111 ARG B CB  
4348 C CG  . ARG B 111 ? 2.3156 3.0602 3.3104 -0.2612 -0.1843 0.5622  111 ARG B CG  
4349 C CD  . ARG B 111 ? 1.8539 2.6021 2.8551 -0.2961 -0.2089 0.5895  111 ARG B CD  
4350 N NE  . ARG B 111 ? 2.1325 2.8215 3.1292 -0.3234 -0.2353 0.5953  111 ARG B NE  
4351 C CZ  . ARG B 111 ? 2.2437 2.9368 3.2436 -0.3369 -0.2456 0.6098  111 ARG B CZ  
4352 N NH1 . ARG B 111 ? 2.0210 2.7825 3.0300 -0.3302 -0.2336 0.6259  111 ARG B NH1 
4353 N NH2 . ARG B 111 ? 2.3926 3.0194 3.3845 -0.3555 -0.2682 0.6076  111 ARG B NH2 
4354 N N   . ARG B 112 ? 1.4570 2.1007 2.4372 -0.2296 -0.1733 0.5130  112 ARG B N   
4355 C CA  . ARG B 112 ? 1.5222 2.1793 2.5051 -0.2377 -0.1799 0.5267  112 ARG B CA  
4356 C C   . ARG B 112 ? 1.4526 2.1310 2.4296 -0.2069 -0.1589 0.5116  112 ARG B C   
4357 O O   . ARG B 112 ? 1.5391 2.2709 2.5164 -0.2052 -0.1552 0.5296  112 ARG B O   
4358 C CB  . ARG B 112 ? 1.6238 2.2107 2.6051 -0.2538 -0.1990 0.5202  112 ARG B CB  
4359 C CG  . ARG B 112 ? 1.8266 2.3886 2.8082 -0.2832 -0.2222 0.5352  112 ARG B CG  
4360 C CD  . ARG B 112 ? 2.0200 2.5091 2.9959 -0.2965 -0.2425 0.5280  112 ARG B CD  
4361 N NE  . ARG B 112 ? 2.1357 2.6442 3.1161 -0.3097 -0.2526 0.5470  112 ARG B NE  
4362 C CZ  . ARG B 112 ? 2.3358 2.8077 3.3136 -0.3337 -0.2781 0.5593  112 ARG B CZ  
4363 N NH1 . ARG B 112 ? 2.6431 3.0521 3.6117 -0.3460 -0.2974 0.5533  112 ARG B NH1 
4364 N NH2 . ARG B 112 ? 2.1193 2.6166 3.1013 -0.3445 -0.2850 0.5776  112 ARG B NH2 
4365 N N   . ALA B 113 ? 1.3579 1.9926 2.3279 -0.1830 -0.1465 0.4794  113 ALA B N   
4366 C CA  . ALA B 113 ? 1.6276 2.2685 2.5888 -0.1531 -0.1293 0.4614  113 ALA B CA  
4367 C C   . ALA B 113 ? 1.9552 2.6674 2.9106 -0.1358 -0.1146 0.4717  113 ALA B C   
4368 O O   . ALA B 113 ? 2.2081 2.9530 3.1557 -0.1218 -0.1076 0.4761  113 ALA B O   
4369 C CB  . ALA B 113 ? 1.7405 2.3256 2.6969 -0.1342 -0.1205 0.4287  113 ALA B CB  
4370 N N   . VAL B 114 ? 2.1520 2.8863 3.1099 -0.1362 -0.1108 0.4755  114 VAL B N   
4371 C CA  . VAL B 114 ? 2.0019 2.8047 2.9551 -0.1182 -0.0968 0.4851  114 VAL B CA  
4372 C C   . VAL B 114 ? 1.8763 2.7475 2.8350 -0.1300 -0.1005 0.5188  114 VAL B C   
4373 O O   . VAL B 114 ? 1.7583 2.6787 2.7068 -0.1072 -0.0872 0.5227  114 VAL B O   
4374 C CB  . VAL B 114 ? 1.9576 2.7742 2.9143 -0.1178 -0.0933 0.4852  114 VAL B CB  
4375 C CG1 . VAL B 114 ? 1.8132 2.7040 2.7650 -0.0960 -0.0785 0.4955  114 VAL B CG1 
4376 C CG2 . VAL B 114 ? 2.0662 2.8179 3.0155 -0.1047 -0.0882 0.4525  114 VAL B CG2 
4377 N N   . ALA B 115 ? 1.6542 2.5255 2.6271 -0.1653 -0.1194 0.5429  115 ALA B N   
4378 C CA  . ALA B 115 ? 1.7112 2.6460 2.6924 -0.1837 -0.1264 0.5793  115 ALA B CA  
4379 C C   . ALA B 115 ? 1.8235 2.7631 2.7943 -0.1710 -0.1215 0.5771  115 ALA B C   
4380 O O   . ALA B 115 ? 2.3008 3.3075 3.2678 -0.1607 -0.1123 0.5955  115 ALA B O   
4381 C CB  . ALA B 115 ? 1.8706 2.7876 2.8659 -0.2254 -0.1518 0.6023  115 ALA B CB  
4382 N N   . GLU B 116 ? 1.7557 2.6238 2.7216 -0.1707 -0.1276 0.5543  116 GLU B N   
4383 C CA  . GLU B 116 ? 1.8835 2.7412 2.8394 -0.1607 -0.1262 0.5489  116 GLU B CA  
4384 C C   . GLU B 116 ? 1.7547 2.6504 2.6923 -0.1230 -0.1052 0.5385  116 GLU B C   
4385 O O   . GLU B 116 ? 1.4999 2.4310 2.4286 -0.1166 -0.1024 0.5512  116 GLU B O   
4386 C CB  . GLU B 116 ? 2.4394 3.2113 3.3965 -0.1664 -0.1364 0.5247  116 GLU B CB  
4387 C CG  . GLU B 116 ? 2.8004 3.5514 3.7624 -0.1906 -0.1548 0.5387  116 GLU B CG  
4388 C CD  . GLU B 116 ? 3.3217 4.0829 4.2723 -0.1756 -0.1497 0.5368  116 GLU B CD  
4389 O OE1 . GLU B 116 ? 3.6318 4.3575 4.5724 -0.1507 -0.1404 0.5091  116 GLU B OE1 
4390 O OE2 . GLU B 116 ? 3.5049 4.3086 4.4559 -0.1896 -0.1560 0.5639  116 GLU B OE2 
4391 N N   . ARG B 117 ? 1.7979 2.6988 2.7290 -0.0999 -0.0915 0.5219  117 ARG B N   
4392 C CA  . ARG B 117 ? 1.8874 2.8178 2.7967 -0.0621 -0.0739 0.5106  117 ARG B CA  
4393 C C   . ARG B 117 ? 2.0487 3.0607 2.9573 -0.0509 -0.0622 0.5306  117 ARG B C   
4394 O O   . ARG B 117 ? 1.8071 2.8409 2.7321 -0.0668 -0.0651 0.5435  117 ARG B O   
4395 C CB  . ARG B 117 ? 1.9323 2.8006 2.8278 -0.0373 -0.0672 0.4729  117 ARG B CB  
4396 C CG  . ARG B 117 ? 1.9355 2.7418 2.8262 -0.0378 -0.0748 0.4557  117 ARG B CG  
4397 C CD  . ARG B 117 ? 2.1347 2.9635 3.0086 -0.0255 -0.0735 0.4628  117 ARG B CD  
4398 N NE  . ARG B 117 ? 2.6929 3.4577 3.5674 -0.0315 -0.0837 0.4476  117 ARG B NE  
4399 C CZ  . ARG B 117 ? 3.0427 3.7691 3.8995 -0.0083 -0.0811 0.4242  117 ARG B CZ  
4400 N NH1 . ARG B 117 ? 3.1881 3.9291 4.0212 0.0234  -0.0694 0.4119  117 ARG B NH1 
4401 N NH2 . ARG B 117 ? 3.1301 3.8021 3.9925 -0.0169 -0.0916 0.4136  117 ARG B NH2 
4402 N N   . PRO B 118 ? 2.2174 3.2772 3.1055 -0.0219 -0.0492 0.5342  118 PRO B N   
4403 C CA  . PRO B 118 ? 2.0698 3.2036 2.9515 0.0008  -0.0343 0.5460  118 PRO B CA  
4404 C C   . PRO B 118 ? 2.0109 3.1397 2.8972 0.0097  -0.0287 0.5332  118 PRO B C   
4405 O O   . PRO B 118 ? 2.1863 3.3759 3.0869 0.0030  -0.0258 0.5559  118 PRO B O   
4406 C CB  . PRO B 118 ? 2.0216 3.1620 2.8689 0.0413  -0.0222 0.5314  118 PRO B CB  
4407 C CG  . PRO B 118 ? 1.9740 3.0858 2.8187 0.0263  -0.0326 0.5350  118 PRO B CG  
4408 C CD  . PRO B 118 ? 2.1097 3.1553 2.9783 -0.0090 -0.0492 0.5284  118 PRO B CD  
4409 N N   . ALA B 119 ? 1.8470 2.9043 2.7224 0.0231  -0.0281 0.4986  119 ALA B N   
4410 C CA  . ALA B 119 ? 1.7742 2.8230 2.6445 0.0413  -0.0203 0.4810  119 ALA B CA  
4411 C C   . ALA B 119 ? 1.8054 2.7778 2.6867 0.0238  -0.0291 0.4601  119 ALA B C   
4412 O O   . ALA B 119 ? 1.8931 2.8030 2.7735 0.0158  -0.0365 0.4444  119 ALA B O   
4413 C CB  . ALA B 119 ? 1.5877 2.6327 2.4244 0.0859  -0.0078 0.4583  119 ALA B CB  
4414 N N   . GLY B 120 ? 1.8428 2.8237 2.7336 0.0199  -0.0276 0.4605  120 GLY B N   
4415 C CA  . GLY B 120 ? 1.7332 2.6499 2.6328 0.0049  -0.0344 0.4430  120 GLY B CA  
4416 C C   . GLY B 120 ? 1.5670 2.4720 2.4536 0.0303  -0.0245 0.4215  120 GLY B C   
4417 O O   . GLY B 120 ? 1.8664 2.8249 2.7512 0.0432  -0.0171 0.4315  120 GLY B O   
4418 N N   . THR B 121 ? 1.4479 2.2833 2.3253 0.0380  -0.0247 0.3925  121 THR B N   
4419 C CA  . THR B 121 ? 1.4470 2.2565 2.3116 0.0583  -0.0178 0.3698  121 THR B CA  
4420 C C   . THR B 121 ? 1.4799 2.2208 2.3542 0.0398  -0.0244 0.3542  121 THR B C   
4421 O O   . THR B 121 ? 1.8991 2.5927 2.7754 0.0325  -0.0294 0.3440  121 THR B O   
4422 C CB  . THR B 121 ? 1.4276 2.2194 2.2640 0.0934  -0.0107 0.3480  121 THR B CB  
4423 O OG1 . THR B 121 ? 1.8512 2.6999 2.6762 0.1097  -0.0059 0.3627  121 THR B OG1 
4424 C CG2 . THR B 121 ? 1.4119 2.1880 2.2320 0.1169  -0.0043 0.3282  121 THR B CG2 
4425 N N   . ILE B 122 ? 1.3977 2.1327 2.2749 0.0373  -0.0231 0.3499  122 ILE B N   
4426 C CA  . ILE B 122 ? 1.4507 2.1210 2.3302 0.0284  -0.0259 0.3311  122 ILE B CA  
4427 C C   . ILE B 122 ? 1.5770 2.2231 2.4372 0.0559  -0.0173 0.3067  122 ILE B C   
4428 O O   . ILE B 122 ? 2.1126 2.7906 2.9636 0.0722  -0.0115 0.3072  122 ILE B O   
4429 C CB  . ILE B 122 ? 1.3085 1.9762 2.2035 0.0013  -0.0340 0.3434  122 ILE B CB  
4430 C CG1 . ILE B 122 ? 1.2163 1.8787 2.1273 -0.0286 -0.0470 0.3614  122 ILE B CG1 
4431 C CG2 . ILE B 122 ? 1.2988 1.9076 2.1894 0.0009  -0.0332 0.3221  122 ILE B CG2 
4432 C CD1 . ILE B 122 ? 1.4015 2.0536 2.3230 -0.0556 -0.0587 0.3735  122 ILE B CD1 
4433 N N   . VAL B 123 ? 1.5049 2.0924 2.3602 0.0595  -0.0177 0.2861  123 VAL B N   
4434 C CA  . VAL B 123 ? 1.3529 1.9106 2.1891 0.0833  -0.0122 0.2635  123 VAL B CA  
4435 C C   . VAL B 123 ? 1.5188 2.0311 2.3593 0.0740  -0.0120 0.2507  123 VAL B C   
4436 O O   . VAL B 123 ? 1.9077 2.3786 2.7594 0.0587  -0.0153 0.2457  123 VAL B O   
4437 C CB  . VAL B 123 ? 1.2569 1.7856 2.0833 0.0949  -0.0139 0.2518  123 VAL B CB  
4438 C CG1 . VAL B 123 ? 1.1817 1.6769 1.9868 0.1178  -0.0116 0.2302  123 VAL B CG1 
4439 C CG2 . VAL B 123 ? 1.1007 1.6716 1.9199 0.1044  -0.0145 0.2644  123 VAL B CG2 
4440 N N   . ASP B 124 ? 1.2213 1.7443 2.0523 0.0843  -0.0078 0.2465  124 ASP B N   
4441 C CA  . ASP B 124 ? 1.4038 1.8950 2.2389 0.0730  -0.0078 0.2396  124 ASP B CA  
4442 C C   . ASP B 124 ? 1.4208 1.8914 2.2372 0.0931  -0.0029 0.2215  124 ASP B C   
4443 O O   . ASP B 124 ? 1.6742 2.1626 2.4727 0.1171  -0.0004 0.2162  124 ASP B O   
4444 C CB  . ASP B 124 ? 1.8187 2.3414 2.6649 0.0559  -0.0112 0.2571  124 ASP B CB  
4445 C CG  . ASP B 124 ? 2.1432 2.7307 2.9862 0.0672  -0.0090 0.2719  124 ASP B CG  
4446 O OD1 . ASP B 124 ? 2.1444 2.7581 2.9762 0.0888  -0.0047 0.2707  124 ASP B OD1 
4447 O OD2 . ASP B 124 ? 2.1948 2.8067 3.0458 0.0550  -0.0121 0.2850  124 ASP B OD2 
4448 N N   . PHE B 125 ? 1.4759 1.9084 2.2942 0.0836  -0.0024 0.2126  125 PHE B N   
4449 C CA  . PHE B 125 ? 1.7130 2.1237 2.5134 0.1005  0.0011  0.1964  125 PHE B CA  
4450 C C   . PHE B 125 ? 1.7450 2.1922 2.5381 0.1081  0.0023  0.2024  125 PHE B C   
4451 O O   . PHE B 125 ? 1.3408 1.8129 2.1181 0.1311  0.0040  0.1998  125 PHE B O   
4452 C CB  . PHE B 125 ? 1.7973 2.1522 2.5996 0.0914  0.0025  0.1832  125 PHE B CB  
4453 C CG  . PHE B 125 ? 1.5158 1.8466 2.2984 0.1092  0.0047  0.1670  125 PHE B CG  
4454 C CD1 . PHE B 125 ? 1.6121 1.9260 2.3826 0.1249  0.0029  0.1570  125 PHE B CD1 
4455 C CD2 . PHE B 125 ? 1.3495 1.6725 2.1241 0.1095  0.0066  0.1628  125 PHE B CD2 
4456 C CE1 . PHE B 125 ? 1.6202 1.9081 2.3709 0.1395  0.0020  0.1433  125 PHE B CE1 
4457 C CE2 . PHE B 125 ? 1.5239 1.8224 2.2795 0.1245  0.0071  0.1487  125 PHE B CE2 
4458 C CZ  . PHE B 125 ? 1.5744 1.8554 2.3180 0.1392  0.0044  0.1393  125 PHE B CZ  
4459 N N   . SER B 126 ? 1.9892 2.4367 2.7925 0.0896  0.0004  0.2103  126 SER B N   
4460 C CA  . SER B 126 ? 1.8196 2.3031 2.6209 0.0917  -0.0002 0.2194  126 SER B CA  
4461 C C   . SER B 126 ? 1.7274 2.2460 2.5483 0.0691  -0.0063 0.2425  126 SER B C   
4462 O O   . SER B 126 ? 1.4612 1.9543 2.2933 0.0481  -0.0110 0.2463  126 SER B O   
4463 C CB  . SER B 126 ? 2.0480 2.4964 2.8406 0.0895  0.0002  0.2081  126 SER B CB  
4464 O OG  . SER B 126 ? 2.7971 3.1990 3.5965 0.0696  -0.0013 0.2040  126 SER B OG  
4465 N N   . ALA B 127 ? 1.7444 2.3219 2.5683 0.0749  -0.0067 0.2584  127 ALA B N   
4466 C CA  . ALA B 127 ? 1.6242 2.2446 2.4668 0.0533  -0.0141 0.2843  127 ALA B CA  
4467 C C   . ALA B 127 ? 1.7483 2.3356 2.5950 0.0299  -0.0222 0.2862  127 ALA B C   
4468 O O   . ALA B 127 ? 1.8101 2.3713 2.6450 0.0369  -0.0200 0.2728  127 ALA B O   
4469 C CB  . ALA B 127 ? 1.5457 2.2359 2.3893 0.0687  -0.0112 0.2990  127 ALA B CB  
4470 N N   . SER B 128 ? 1.6608 2.2446 2.5215 0.0026  -0.0326 0.3019  128 SER B N   
4471 C CA  . SER B 128 ? 1.6118 2.1527 2.4716 -0.0196 -0.0426 0.3021  128 SER B CA  
4472 C C   . SER B 128 ? 1.5844 2.1509 2.4597 -0.0479 -0.0580 0.3295  128 SER B C   
4473 O O   . SER B 128 ? 1.5294 2.1394 2.4173 -0.0514 -0.0594 0.3462  128 SER B O   
4474 C CB  . SER B 128 ? 1.6767 2.1477 2.5280 -0.0215 -0.0404 0.2815  128 SER B CB  
4475 O OG  . SER B 128 ? 1.7092 2.1663 2.5700 -0.0387 -0.0480 0.2896  128 SER B OG  
4476 N N   . PRO B 129 ? 1.6743 2.2125 2.5472 -0.0693 -0.0713 0.3355  129 PRO B N   
4477 C CA  . PRO B 129 ? 1.7567 2.3148 2.6425 -0.0986 -0.0897 0.3631  129 PRO B CA  
4478 C C   . PRO B 129 ? 1.6125 2.1583 2.5048 -0.1076 -0.0931 0.3665  129 PRO B C   
4479 O O   . PRO B 129 ? 1.5008 2.0932 2.4084 -0.1204 -0.1004 0.3906  129 PRO B O   
4480 C CB  . PRO B 129 ? 1.9209 2.4225 2.7936 -0.1158 -0.1033 0.3591  129 PRO B CB  
4481 C CG  . PRO B 129 ? 1.7369 2.2148 2.5939 -0.0945 -0.0905 0.3357  129 PRO B CG  
4482 C CD  . PRO B 129 ? 1.6081 2.0964 2.4641 -0.0664 -0.0706 0.3179  129 PRO B CD  
4483 N N   . ALA B 130 ? 1.5251 2.0067 2.4059 -0.1024 -0.0889 0.3437  130 ALA B N   
4484 C CA  . ALA B 130 ? 1.6049 2.0607 2.4897 -0.1121 -0.0943 0.3443  130 ALA B CA  
4485 C C   . ALA B 130 ? 1.8519 2.3561 2.7488 -0.1014 -0.0855 0.3509  130 ALA B C   
4486 O O   . ALA B 130 ? 1.6722 2.1942 2.5798 -0.1174 -0.0955 0.3690  130 ALA B O   
4487 C CB  . ALA B 130 ? 1.7060 2.0913 2.5772 -0.1034 -0.0883 0.3179  130 ALA B CB  
4488 N N   . THR B 131 ? 2.2327 2.7548 3.1250 -0.0741 -0.0683 0.3362  131 THR B N   
4489 C CA  . THR B 131 ? 2.0269 2.5898 2.9248 -0.0590 -0.0593 0.3391  131 THR B CA  
4490 C C   . THR B 131 ? 2.0766 2.7117 2.9880 -0.0688 -0.0652 0.3691  131 THR B C   
4491 O O   . THR B 131 ? 2.1118 2.7727 3.0317 -0.0737 -0.0673 0.3820  131 THR B O   
4492 C CB  . THR B 131 ? 1.9313 2.4965 2.8174 -0.0273 -0.0429 0.3183  131 THR B CB  
4493 O OG1 . THR B 131 ? 1.9863 2.5867 2.8680 -0.0160 -0.0388 0.3213  131 THR B OG1 
4494 C CG2 . THR B 131 ? 2.1065 2.6057 2.9824 -0.0188 -0.0371 0.2917  131 THR B CG2 
4495 N N   . ASP B 132 ? 2.1141 2.7818 3.0279 -0.0720 -0.0680 0.3808  132 ASP B N   
4496 C CA  . ASP B 132 ? 1.7062 2.4497 2.6353 -0.0815 -0.0733 0.4122  132 ASP B CA  
4497 C C   . ASP B 132 ? 1.6864 2.4307 2.6287 -0.1149 -0.0916 0.4364  132 ASP B C   
4498 O O   . ASP B 132 ? 1.3908 2.1888 2.3454 -0.1206 -0.0932 0.4588  132 ASP B O   
4499 C CB  . ASP B 132 ? 1.5574 2.3345 2.4874 -0.0766 -0.0725 0.4190  132 ASP B CB  
4500 C CG  . ASP B 132 ? 1.7780 2.5872 2.6985 -0.0401 -0.0543 0.4053  132 ASP B CG  
4501 O OD1 . ASP B 132 ? 1.8388 2.6551 2.7528 -0.0197 -0.0434 0.3956  132 ASP B OD1 
4502 O OD2 . ASP B 132 ? 1.9620 2.7859 2.8795 -0.0319 -0.0526 0.4042  132 ASP B OD2 
4503 N N   . GLU B 133 ? 1.9546 2.6369 2.8914 -0.1356 -0.1059 0.4313  133 GLU B N   
4504 C CA  . GLU B 133 ? 1.9712 2.6378 2.9149 -0.1682 -0.1273 0.4513  133 GLU B CA  
4505 C C   . GLU B 133 ? 1.9257 2.5896 2.8732 -0.1670 -0.1250 0.4509  133 GLU B C   
4506 O O   . GLU B 133 ? 1.6789 2.3775 2.6388 -0.1866 -0.1365 0.4773  133 GLU B O   
4507 C CB  . GLU B 133 ? 2.0135 2.6020 2.9426 -0.1820 -0.1407 0.4382  133 GLU B CB  
4508 C CG  . GLU B 133 ? 1.9292 2.4844 2.8586 -0.2132 -0.1653 0.4541  133 GLU B CG  
4509 C CD  . GLU B 133 ? 2.3120 2.9140 3.2547 -0.2428 -0.1862 0.4913  133 GLU B CD  
4510 O OE1 . GLU B 133 ? 2.6394 3.3121 3.6002 -0.2455 -0.1832 0.5143  133 GLU B OE1 
4511 O OE2 . GLU B 133 ? 2.6880 3.2546 3.6218 -0.2629 -0.2060 0.4976  133 GLU B OE2 
4512 N N   . LEU B 134 ? 1.9393 2.5616 2.8762 -0.1447 -0.1108 0.4217  134 LEU B N   
4513 C CA  . LEU B 134 ? 1.9684 2.5802 2.9072 -0.1407 -0.1078 0.4169  134 LEU B CA  
4514 C C   . LEU B 134 ? 1.7558 2.4419 2.7044 -0.1331 -0.1008 0.4355  134 LEU B C   
4515 O O   . LEU B 134 ? 1.7835 2.4848 2.7400 -0.1468 -0.1088 0.4518  134 LEU B O   
4516 C CB  . LEU B 134 ? 2.2338 2.7897 3.1613 -0.1192 -0.0951 0.3841  134 LEU B CB  
4517 C CG  . LEU B 134 ? 2.2811 2.7621 3.1998 -0.1287 -0.1032 0.3688  134 LEU B CG  
4518 C CD1 . LEU B 134 ? 2.8393 3.2800 3.7487 -0.1041 -0.0869 0.3383  134 LEU B CD1 
4519 C CD2 . LEU B 134 ? 1.8907 2.3440 2.8136 -0.1498 -0.1197 0.3788  134 LEU B CD2 
4520 N N   . GLY B 135 ? 1.6179 2.3483 2.5638 -0.1100 -0.0862 0.4325  135 GLY B N   
4521 C CA  . GLY B 135 ? 1.6948 2.4988 2.6455 -0.0960 -0.0767 0.4480  135 GLY B CA  
4522 C C   . GLY B 135 ? 1.8786 2.7399 2.8473 -0.1235 -0.0904 0.4864  135 GLY B C   
4523 O O   . GLY B 135 ? 1.7550 2.6556 2.7300 -0.1263 -0.0904 0.5034  135 GLY B O   
4524 N N   . ARG B 136 ? 2.0589 2.9226 3.0349 -0.1445 -0.1032 0.5004  136 ARG B N   
4525 C CA  . ARG B 136 ? 2.1053 3.0214 3.0995 -0.1746 -0.1196 0.5394  136 ARG B CA  
4526 C C   . ARG B 136 ? 2.2417 3.1300 3.2400 -0.2018 -0.1367 0.5515  136 ARG B C   
4527 O O   . ARG B 136 ? 2.5751 3.5170 3.5862 -0.2158 -0.1424 0.5806  136 ARG B O   
4528 C CB  . ARG B 136 ? 1.9638 2.8851 2.9636 -0.1913 -0.1316 0.5516  136 ARG B CB  
4529 C CG  . ARG B 136 ? 1.8827 2.8620 2.8848 -0.1665 -0.1158 0.5521  136 ARG B CG  
4530 C CD  . ARG B 136 ? 1.9240 2.9120 2.9337 -0.1853 -0.1296 0.5672  136 ARG B CD  
4531 N NE  . ARG B 136 ? 2.1707 3.0721 3.1641 -0.1917 -0.1381 0.5428  136 ARG B NE  
4532 C CZ  . ARG B 136 ? 2.3462 3.1927 3.3362 -0.2229 -0.1613 0.5486  136 ARG B CZ  
4533 N NH1 . ARG B 136 ? 2.3685 3.2318 3.3706 -0.2529 -0.1802 0.5775  136 ARG B NH1 
4534 N NH2 . ARG B 136 ? 2.5586 3.3307 3.5307 -0.2232 -0.1661 0.5252  136 ARG B NH2 
4535 N N   . ARG B 137 ? 1.8770 2.6800 2.8635 -0.2094 -0.1457 0.5297  137 ARG B N   
4536 C CA  . ARG B 137 ? 1.7619 2.5207 2.7487 -0.2379 -0.1673 0.5388  137 ARG B CA  
4537 C C   . ARG B 137 ? 1.8140 2.5613 2.7988 -0.2280 -0.1604 0.5296  137 ARG B C   
4538 O O   . ARG B 137 ? 2.0187 2.7332 3.0038 -0.2494 -0.1776 0.5374  137 ARG B O   
4539 C CB  . ARG B 137 ? 1.6111 2.2811 2.5827 -0.2453 -0.1787 0.5172  137 ARG B CB  
4540 C CG  . ARG B 137 ? 1.6611 2.3202 2.6313 -0.2686 -0.1982 0.5316  137 ARG B CG  
4541 C CD  . ARG B 137 ? 1.7011 2.2670 2.6513 -0.2731 -0.2095 0.5089  137 ARG B CD  
4542 N NE  . ARG B 137 ? 1.6951 2.2154 2.6406 -0.2910 -0.2277 0.5128  137 ARG B NE  
4543 C CZ  . ARG B 137 ? 1.8819 2.3206 2.8086 -0.2963 -0.2411 0.4966  137 ARG B CZ  
4544 N NH1 . ARG B 137 ? 1.8483 2.2430 2.7591 -0.2861 -0.2376 0.4762  137 ARG B NH1 
4545 N NH2 . ARG B 137 ? 2.1690 2.5695 3.0911 -0.3105 -0.2579 0.5007  137 ARG B NH2 
4546 N N   . THR B 138 ? 1.6082 2.3779 2.5889 -0.1956 -0.1371 0.5124  138 THR B N   
4547 C CA  . THR B 138 ? 1.5155 2.2745 2.4929 -0.1845 -0.1306 0.5029  138 THR B CA  
4548 C C   . THR B 138 ? 1.3891 2.2268 2.3707 -0.1697 -0.1178 0.5190  138 THR B C   
4549 O O   . THR B 138 ? 1.3413 2.1847 2.3217 -0.1666 -0.1162 0.5212  138 THR B O   
4550 C CB  . THR B 138 ? 1.8504 2.5474 2.8145 -0.1596 -0.1178 0.4649  138 THR B CB  
4551 O OG1 . THR B 138 ? 2.1878 2.9099 3.1450 -0.1314 -0.0993 0.4512  138 THR B OG1 
4552 C CG2 . THR B 138 ? 1.8354 2.4558 2.7938 -0.1716 -0.1289 0.4492  138 THR B CG2 
4553 N N   . GLY B 139 ? 1.3511 2.2488 2.3360 -0.1584 -0.1082 0.5294  139 GLY B N   
4554 C CA  . GLY B 139 ? 1.4129 2.3892 2.3993 -0.1402 -0.0946 0.5448  139 GLY B CA  
4555 C C   . GLY B 139 ? 1.3059 2.2717 2.2733 -0.0993 -0.0739 0.5147  139 GLY B C   
4556 O O   . GLY B 139 ? 1.2502 2.2662 2.2114 -0.0788 -0.0624 0.5210  139 GLY B O   
4557 N N   . ALA B 140 ? 1.3306 2.2285 2.2871 -0.0880 -0.0706 0.4826  140 ALA B N   
4558 C CA  . ALA B 140 ? 1.6415 2.5258 2.5792 -0.0510 -0.0538 0.4546  140 ALA B CA  
4559 C C   . ALA B 140 ? 1.6976 2.5978 2.6308 -0.0354 -0.0457 0.4474  140 ALA B C   
4560 O O   . ALA B 140 ? 1.3529 2.2290 2.2930 -0.0522 -0.0534 0.4473  140 ALA B O   
4561 C CB  . ALA B 140 ? 1.6587 2.4632 2.5880 -0.0479 -0.0551 0.4261  140 ALA B CB  
4562 N N   . THR B 141 ? 1.8375 2.7784 2.7570 -0.0024 -0.0312 0.4423  141 THR B N   
4563 C CA  . THR B 141 ? 1.5903 2.5575 2.5039 0.0172  -0.0228 0.4376  141 THR B CA  
4564 C C   . THR B 141 ? 1.3355 2.2382 2.2289 0.0397  -0.0165 0.4015  141 THR B C   
4565 O O   . THR B 141 ? 1.1533 2.0453 2.0277 0.0657  -0.0089 0.3856  141 THR B O   
4566 C CB  . THR B 141 ? 1.7878 2.8342 2.6943 0.0438  -0.0111 0.4521  141 THR B CB  
4567 O OG1 . THR B 141 ? 1.9137 3.0229 2.8416 0.0199  -0.0174 0.4886  141 THR B OG1 
4568 C CG2 . THR B 141 ? 2.1141 3.1892 3.0106 0.0715  -0.0012 0.4450  141 THR B CG2 
4569 N N   . PRO B 142 ? 1.3647 2.2211 2.2603 0.0294  -0.0206 0.3887  142 PRO B N   
4570 C CA  . PRO B 142 ? 1.4635 2.2620 2.3410 0.0491  -0.0148 0.3568  142 PRO B CA  
4571 C C   . PRO B 142 ? 1.5003 2.3231 2.3556 0.0877  -0.0033 0.3450  142 PRO B C   
4572 O O   . PRO B 142 ? 1.4457 2.3267 2.3002 0.1006  0.0014  0.3576  142 PRO B O   
4573 C CB  . PRO B 142 ? 1.2724 2.0445 2.1566 0.0328  -0.0201 0.3542  142 PRO B CB  
4574 C CG  . PRO B 142 ? 1.2090 1.9867 2.1136 -0.0029 -0.0334 0.3772  142 PRO B CG  
4575 C CD  . PRO B 142 ? 1.3624 2.2137 2.2758 -0.0026 -0.0326 0.4038  142 PRO B CD  
4576 N N   . GLU B 143 ? 1.8395 2.6160 2.6761 0.1059  -0.0004 0.3214  143 GLU B N   
4577 C CA  . GLU B 143 ? 1.7384 2.5223 2.5477 0.1431  0.0069  0.3070  143 GLU B CA  
4578 C C   . GLU B 143 ? 1.4595 2.2334 2.2569 0.1589  0.0102  0.2935  143 GLU B C   
4579 O O   . GLU B 143 ? 1.2963 2.0854 2.0701 0.1913  0.0153  0.2846  143 GLU B O   
4580 C CB  . GLU B 143 ? 2.1461 2.8717 2.9446 0.1463  0.0039  0.2886  143 GLU B CB  
4581 C CG  . GLU B 143 ? 2.2702 2.9948 3.0376 0.1815  0.0071  0.2754  143 GLU B CG  
4582 C CD  . GLU B 143 ? 2.3974 3.0527 3.1563 0.1807  0.0014  0.2552  143 GLU B CD  
4583 O OE1 . GLU B 143 ? 2.2474 2.8529 3.0082 0.1742  -0.0005 0.2398  143 GLU B OE1 
4584 O OE2 . GLU B 143 ? 2.5489 3.2014 3.3005 0.1854  -0.0011 0.2562  143 GLU B OE2 
4585 N N   . GLU B 144 ? 1.2755 2.0223 2.0876 0.1361  0.0062  0.2926  144 GLU B N   
4586 C CA  . GLU B 144 ? 1.5826 2.3100 2.3853 0.1454  0.0077  0.2793  144 GLU B CA  
4587 C C   . GLU B 144 ? 1.6740 2.4037 2.4982 0.1158  0.0024  0.2922  144 GLU B C   
4588 O O   . GLU B 144 ? 1.9073 2.5914 2.7286 0.1093  0.0007  0.2787  144 GLU B O   
4589 C CB  . GLU B 144 ? 1.8946 2.5508 2.6796 0.1552  0.0074  0.2515  144 GLU B CB  
4590 C CG  . GLU B 144 ? 2.0451 2.6918 2.8023 0.1872  0.0104  0.2340  144 GLU B CG  
4591 C CD  . GLU B 144 ? 2.3468 3.0191 3.1036 0.1921  0.0121  0.2377  144 GLU B CD  
4592 O OE1 . GLU B 144 ? 2.4029 3.0547 3.1731 0.1703  0.0096  0.2387  144 GLU B OE1 
4593 O OE2 . GLU B 144 ? 2.4554 3.1674 3.1964 0.2200  0.0157  0.2391  144 GLU B OE2 
4594 N N   . GLY B 145 ? 1.7255 2.5105 2.5693 0.0989  -0.0009 0.3196  145 GLY B N   
4595 C CA  . GLY B 145 ? 2.0349 2.8306 2.8972 0.0715  -0.0088 0.3362  145 GLY B CA  
4596 C C   . GLY B 145 ? 2.3079 3.1627 3.1728 0.0821  -0.0066 0.3496  145 GLY B C   
4597 O O   . GLY B 145 ? 2.1731 3.0544 3.0225 0.1142  0.0022  0.3422  145 GLY B O   
4598 N N   . ASP B 146 ? 2.3012 3.1724 3.1842 0.0556  -0.0160 0.3689  146 ASP B N   
4599 C CA  . ASP B 146 ? 1.9701 2.8966 2.8616 0.0577  -0.0173 0.3860  146 ASP B CA  
4600 C C   . ASP B 146 ? 1.8216 2.7005 2.7079 0.0482  -0.0232 0.3738  146 ASP B C   
4601 O O   . ASP B 146 ? 1.7654 2.6308 2.6350 0.0723  -0.0165 0.3553  146 ASP B O   
4602 C CB  . ASP B 146 ? 1.9894 2.9720 2.8697 0.0960  -0.0048 0.3849  146 ASP B CB  
4603 C CG  . ASP B 146 ? 2.0766 3.1410 2.9732 0.0976  -0.0054 0.4123  146 ASP B CG  
4604 O OD1 . ASP B 146 ? 1.8206 2.8820 2.7290 0.0771  -0.0148 0.4214  146 ASP B OD1 
4605 O OD2 . ASP B 146 ? 2.0403 3.1730 2.9369 0.1209  0.0035  0.4249  146 ASP B OD2 
4606 N N   . HIS B 147 ? 1.6410 2.4963 2.5399 0.0137  -0.0370 0.3856  147 HIS B N   
4607 C CA  . HIS B 147 ? 1.5417 2.3344 2.4313 0.0022  -0.0435 0.3708  147 HIS B CA  
4608 C C   . HIS B 147 ? 1.5609 2.3804 2.4482 0.0126  -0.0433 0.3734  147 HIS B C   
4609 O O   . HIS B 147 ? 1.4942 2.2640 2.3651 0.0196  -0.0418 0.3521  147 HIS B O   
4610 C CB  . HIS B 147 ? 1.6314 2.3963 2.5320 -0.0358 -0.0607 0.3857  147 HIS B CB  
4611 C CG  . HIS B 147 ? 1.7244 2.4261 2.6125 -0.0470 -0.0682 0.3721  147 HIS B CG  
4612 N ND1 . HIS B 147 ? 1.5393 2.1931 2.4073 -0.0274 -0.0583 0.3432  147 HIS B ND1 
4613 C CD2 . HIS B 147 ? 1.8699 2.5486 2.7607 -0.0755 -0.0854 0.3842  147 HIS B CD2 
4614 C CE1 . HIS B 147 ? 1.7030 2.3087 2.5623 -0.0429 -0.0677 0.3382  147 HIS B CE1 
4615 N NE2 . HIS B 147 ? 1.9115 2.5286 2.7829 -0.0716 -0.0847 0.3620  147 HIS B NE2 
4616 N N   . ALA B 148 ? 1.5617 2.4591 2.4675 0.0095  -0.0466 0.4021  148 ALA B N   
4617 C CA  . ALA B 148 ? 1.4121 2.3424 2.3215 0.0137  -0.0496 0.4110  148 ALA B CA  
4618 C C   . ALA B 148 ? 1.2243 2.1619 2.1145 0.0550  -0.0345 0.3892  148 ALA B C   
4619 O O   . ALA B 148 ? 0.8751 1.7852 1.7526 0.0638  -0.0349 0.3747  148 ALA B O   
4620 C CB  . ALA B 148 ? 1.7397 2.7554 2.6768 -0.0011 -0.0570 0.4498  148 ALA B CB  
4621 N N   . PHE B 149 ? 1.3688 2.3484 2.2567 0.0800  -0.0228 0.3898  149 PHE B N   
4622 C CA  . PHE B 149 ? 1.6509 2.6462 2.5185 0.1220  -0.0103 0.3729  149 PHE B CA  
4623 C C   . PHE B 149 ? 2.0455 2.9560 2.8857 0.1340  -0.0077 0.3371  149 PHE B C   
4624 O O   . PHE B 149 ? 2.0898 2.9908 2.9136 0.1556  -0.0052 0.3229  149 PHE B O   
4625 C CB  . PHE B 149 ? 1.5840 2.6316 2.4496 0.1459  0.0001  0.3794  149 PHE B CB  
4626 C CG  . PHE B 149 ? 1.5496 2.6246 2.3920 0.1930  0.0118  0.3662  149 PHE B CG  
4627 C CD1 . PHE B 149 ? 1.6019 2.6261 2.4169 0.2164  0.0136  0.3374  149 PHE B CD1 
4628 C CD2 . PHE B 149 ? 1.4922 2.6423 2.3372 0.2150  0.0204  0.3829  149 PHE B CD2 
4629 C CE1 . PHE B 149 ? 1.7149 2.7590 2.5047 0.2603  0.0216  0.3249  149 PHE B CE1 
4630 C CE2 . PHE B 149 ? 1.6177 2.7899 2.4369 0.2612  0.0301  0.3699  149 PHE B CE2 
4631 C CZ  . PHE B 149 ? 1.6936 2.8111 2.4844 0.2840  0.0298  0.3406  149 PHE B CZ  
4632 N N   . VAL B 150 ? 2.1244 2.9763 2.9606 0.1193  -0.0089 0.3245  150 VAL B N   
4633 C CA  . VAL B 150 ? 1.8108 2.5841 2.6244 0.1271  -0.0065 0.2937  150 VAL B CA  
4634 C C   . VAL B 150 ? 1.7087 2.4449 2.5174 0.1161  -0.0124 0.2865  150 VAL B C   
4635 O O   . VAL B 150 ? 1.8686 2.5707 2.6563 0.1349  -0.0092 0.2655  150 VAL B O   
4636 C CB  . VAL B 150 ? 1.9955 2.7192 2.8097 0.1125  -0.0066 0.2846  150 VAL B CB  
4637 C CG1 . VAL B 150 ? 2.3038 2.9478 3.1009 0.1122  -0.0058 0.2580  150 VAL B CG1 
4638 C CG2 . VAL B 150 ? 2.0573 2.8058 2.8672 0.1314  0.0000  0.2843  150 VAL B CG2 
4639 N N   . ALA B 151 ? 1.5939 2.3359 2.4205 0.0851  -0.0226 0.3050  151 ALA B N   
4640 C CA  . ALA B 151 ? 1.5062 2.2134 2.3281 0.0710  -0.0304 0.3014  151 ALA B CA  
4641 C C   . ALA B 151 ? 1.6118 2.3524 2.4267 0.0932  -0.0285 0.3007  151 ALA B C   
4642 O O   . ALA B 151 ? 1.6173 2.3146 2.4140 0.1009  -0.0284 0.2824  151 ALA B O   
4643 C CB  . ALA B 151 ? 1.5205 2.2369 2.3615 0.0356  -0.0445 0.3252  151 ALA B CB  
4644 N N   . ARG B 152 ? 1.6545 2.4742 2.4843 0.1038  -0.0269 0.3220  152 ARG B N   
4645 C CA  . ARG B 152 ? 1.5318 2.3965 2.3582 0.1275  -0.0249 0.3253  152 ARG B CA  
4646 C C   . ARG B 152 ? 1.5437 2.3746 2.3398 0.1633  -0.0159 0.2957  152 ARG B C   
4647 O O   . ARG B 152 ? 1.5421 2.3573 2.3247 0.1749  -0.0179 0.2852  152 ARG B O   
4648 C CB  . ARG B 152 ? 1.8163 2.7783 2.6660 0.1334  -0.0237 0.3558  152 ARG B CB  
4649 C CG  . ARG B 152 ? 2.1487 3.1587 3.0001 0.1517  -0.0244 0.3636  152 ARG B CG  
4650 C CD  . ARG B 152 ? 2.1027 3.2154 2.9811 0.1553  -0.0229 0.3977  152 ARG B CD  
4651 N NE  . ARG B 152 ? 2.3018 3.4634 3.1779 0.1840  -0.0200 0.4009  152 ARG B NE  
4652 C CZ  . ARG B 152 ? 2.6498 3.8644 3.5494 0.1711  -0.0286 0.4267  152 ARG B CZ  
4653 N NH1 . ARG B 152 ? 2.7928 4.0087 3.7166 0.1281  -0.0429 0.4499  152 ARG B NH1 
4654 N NH2 . ARG B 152 ? 2.9351 4.1995 3.8329 0.2014  -0.0246 0.4297  152 ARG B NH2 
4655 N N   . TRP B 153 ? 1.7709 2.5904 2.5549 0.1810  -0.0078 0.2829  153 TRP B N   
4656 C CA  . TRP B 153 ? 1.8612 2.6736 2.6174 0.2205  -0.0013 0.2626  153 TRP B CA  
4657 C C   . TRP B 153 ? 1.8558 2.5866 2.5870 0.2256  -0.0001 0.2335  153 TRP B C   
4658 O O   . TRP B 153 ? 1.7292 2.4380 2.4333 0.2545  0.0011  0.2145  153 TRP B O   
4659 C CB  . TRP B 153 ? 1.8455 2.7253 2.6027 0.2468  0.0060  0.2738  153 TRP B CB  
4660 C CG  . TRP B 153 ? 1.6619 2.6239 2.4339 0.2579  0.0066  0.2967  153 TRP B CG  
4661 C CD1 . TRP B 153 ? 1.7638 2.8033 2.5647 0.2468  0.0076  0.3280  153 TRP B CD1 
4662 C CD2 . TRP B 153 ? 1.5874 2.5625 2.3478 0.2805  0.0053  0.2915  153 TRP B CD2 
4663 N NE1 . TRP B 153 ? 1.5715 2.6760 2.3810 0.2622  0.0080  0.3435  153 TRP B NE1 
4664 C CE2 . TRP B 153 ? 1.6230 2.6885 2.4080 0.2833  0.0065  0.3210  153 TRP B CE2 
4665 C CE3 . TRP B 153 ? 1.5244 2.4451 2.2563 0.2985  0.0027  0.2660  153 TRP B CE3 
4666 C CZ2 . TRP B 153 ? 1.8306 2.9329 2.6132 0.3045  0.0054  0.3247  153 TRP B CZ2 
4667 C CZ3 . TRP B 153 ? 1.3965 2.3499 2.1239 0.3193  0.0009  0.2687  153 TRP B CZ3 
4668 C CH2 . TRP B 153 ? 1.6553 2.6984 2.4081 0.3227  0.0025  0.2974  153 TRP B CH2 
4669 N N   . GLY B 154 ? 1.8239 2.5112 2.5640 0.1980  -0.0016 0.2312  154 GLY B N   
4670 C CA  . GLY B 154 ? 1.6994 2.3140 2.4215 0.1986  -0.0005 0.2075  154 GLY B CA  
4671 C C   . GLY B 154 ? 1.5896 2.1505 2.3015 0.1884  -0.0042 0.1947  154 GLY B C   
4672 O O   . GLY B 154 ? 1.7954 2.2988 2.4900 0.1923  -0.0033 0.1750  154 GLY B O   
4673 N N   . SER B 155 ? 1.4517 2.0339 2.1743 0.1753  -0.0090 0.2075  155 SER B N   
4674 C CA  . SER B 155 ? 1.7170 2.2550 2.4291 0.1658  -0.0134 0.1981  155 SER B CA  
4675 C C   . SER B 155 ? 1.8649 2.3798 2.5491 0.1942  -0.0125 0.1785  155 SER B C   
4676 O O   . SER B 155 ? 2.2017 2.7440 2.8756 0.2224  -0.0100 0.1752  155 SER B O   
4677 C CB  . SER B 155 ? 1.6504 2.2228 2.3781 0.1493  -0.0207 0.2176  155 SER B CB  
4678 O OG  . SER B 155 ? 1.9995 2.6092 2.7204 0.1719  -0.0219 0.2196  155 SER B OG  
4679 N N   . LYS B 156 ? 1.6919 2.1548 2.3616 0.1874  -0.0153 0.1658  156 LYS B N   
4680 C CA  . LYS B 156 ? 1.8617 2.2931 2.5031 0.2116  -0.0162 0.1465  156 LYS B CA  
4681 C C   . LYS B 156 ? 2.1086 2.5912 2.7442 0.2377  -0.0190 0.1520  156 LYS B C   
4682 O O   . LYS B 156 ? 2.3046 2.7934 2.9210 0.2680  -0.0188 0.1423  156 LYS B O   
4683 C CB  . LYS B 156 ? 1.7548 2.1235 2.3822 0.1978  -0.0185 0.1340  156 LYS B CB  
4684 C CG  . LYS B 156 ? 1.6820 1.9995 2.3134 0.1738  -0.0148 0.1286  156 LYS B CG  
4685 C CD  . LYS B 156 ? 1.8046 2.0944 2.4312 0.1795  -0.0103 0.1178  156 LYS B CD  
4686 C CE  . LYS B 156 ? 1.8579 2.1024 2.4906 0.1563  -0.0061 0.1144  156 LYS B CE  
4687 N NZ  . LYS B 156 ? 1.7053 1.9418 2.3485 0.1526  -0.0016 0.1133  156 LYS B NZ  
4688 N N   . SER B 157 ? 2.0020 2.5164 2.6524 0.2256  -0.0229 0.1672  157 SER B N   
4689 C CA  . SER B 157 ? 1.7996 2.3646 2.4485 0.2471  -0.0260 0.1748  157 SER B CA  
4690 C C   . SER B 157 ? 1.5926 2.2231 2.2483 0.2717  -0.0209 0.1848  157 SER B C   
4691 O O   . SER B 157 ? 1.6278 2.2791 2.2653 0.3062  -0.0206 0.1781  157 SER B O   
4692 C CB  . SER B 157 ? 1.8954 2.4864 2.5647 0.2240  -0.0323 0.1936  157 SER B CB  
4693 O OG  . SER B 157 ? 1.7992 2.4259 2.4977 0.1998  -0.0320 0.2150  157 SER B OG  
4694 N N   . GLY B 158 ? 1.3730 2.0333 2.0533 0.2535  -0.0172 0.2008  158 GLY B N   
4695 C CA  . GLY B 158 ? 1.2524 1.9774 1.9421 0.2718  -0.0114 0.2135  158 GLY B CA  
4696 C C   . GLY B 158 ? 1.2623 1.9622 1.9223 0.3041  -0.0076 0.1928  158 GLY B C   
4697 O O   . GLY B 158 ? 1.2719 2.0150 1.9202 0.3380  -0.0049 0.1938  158 GLY B O   
4698 N N   . GLY B 159 ? 1.5040 2.1334 2.1512 0.2932  -0.0084 0.1749  159 GLY B N   
4699 C CA  . GLY B 159 ? 1.9797 2.5725 2.5982 0.3176  -0.0082 0.1551  159 GLY B CA  
4700 C C   . GLY B 159 ? 1.9364 2.5192 2.5225 0.3522  -0.0133 0.1406  159 GLY B C   
4701 O O   . GLY B 159 ? 1.8399 2.4352 2.4033 0.3859  -0.0136 0.1336  159 GLY B O   
4702 N N   . LYS B 160 ? 1.8673 2.4249 2.4497 0.3436  -0.0183 0.1362  160 LYS B N   
4703 C CA  . LYS B 160 ? 1.7991 2.3412 2.3512 0.3726  -0.0251 0.1226  160 LYS B CA  
4704 C C   . LYS B 160 ? 1.8422 2.4578 2.3931 0.4061  -0.0229 0.1331  160 LYS B C   
4705 O O   . LYS B 160 ? 1.5879 2.1988 2.1068 0.4438  -0.0266 0.1202  160 LYS B O   
4706 C CB  . LYS B 160 ? 1.5374 2.0403 2.0891 0.3523  -0.0304 0.1183  160 LYS B CB  
4707 C CG  . LYS B 160 ? 1.2835 1.7647 1.8041 0.3786  -0.0390 0.1044  160 LYS B CG  
4708 C CD  . LYS B 160 ? 1.2478 1.6613 1.7570 0.3581  -0.0449 0.0927  160 LYS B CD  
4709 C CE  . LYS B 160 ? 1.4150 1.7978 1.8874 0.3870  -0.0551 0.0763  160 LYS B CE  
4710 N NZ  . LYS B 160 ? 1.6026 1.9096 2.0563 0.3711  -0.0612 0.0618  160 LYS B NZ  
4711 N N   . GLU B 161 ? 2.0444 2.7269 2.6299 0.3914  -0.0179 0.1575  161 GLU B N   
4712 C CA  . GLU B 161 ? 1.8200 2.5855 2.4131 0.4185  -0.0141 0.1735  161 GLU B CA  
4713 C C   . GLU B 161 ? 1.6164 2.4058 2.1929 0.4504  -0.0084 0.1701  161 GLU B C   
4714 O O   . GLU B 161 ? 1.5970 2.4154 2.1504 0.4924  -0.0082 0.1657  161 GLU B O   
4715 C CB  . GLU B 161 ? 1.6820 2.5138 2.3189 0.3903  -0.0109 0.2037  161 GLU B CB  
4716 C CG  . GLU B 161 ? 2.0049 2.8149 2.6535 0.3632  -0.0186 0.2073  161 GLU B CG  
4717 C CD  . GLU B 161 ? 2.1337 3.0170 2.8169 0.3489  -0.0203 0.2367  161 GLU B CD  
4718 O OE1 . GLU B 161 ? 2.2444 3.2052 2.9470 0.3588  -0.0143 0.2576  161 GLU B OE1 
4719 O OE2 . GLU B 161 ? 2.1708 3.0338 2.8609 0.3273  -0.0283 0.2396  161 GLU B OE2 
4720 N N   . ILE B 162 ? 1.5975 2.3719 2.1844 0.4304  -0.0044 0.1721  162 ILE B N   
4721 C CA  . ILE B 162 ? 1.5911 2.3826 2.1633 0.4551  0.0003  0.1697  162 ILE B CA  
4722 C C   . ILE B 162 ? 1.6418 2.3777 2.1647 0.4917  -0.0069 0.1424  162 ILE B C   
4723 O O   . ILE B 162 ? 1.4951 2.2600 1.9937 0.5318  -0.0053 0.1395  162 ILE B O   
4724 C CB  . ILE B 162 ? 1.6097 2.3946 2.2031 0.4252  0.0047  0.1776  162 ILE B CB  
4725 C CG1 . ILE B 162 ? 1.7429 2.5891 2.3814 0.3932  0.0094  0.2069  162 ILE B CG1 
4726 C CG2 . ILE B 162 ? 1.4695 2.2664 2.0421 0.4535  0.0084  0.1732  162 ILE B CG2 
4727 C CD1 . ILE B 162 ? 1.9736 2.7939 2.6343 0.3545  0.0100  0.2126  162 ILE B CD1 
4728 N N   . CYS B 163 ? 1.9619 2.6178 2.4696 0.4771  -0.0156 0.1238  163 CYS B N   
4729 C CA  . CYS B 163 ? 2.2657 2.8569 2.7269 0.5044  -0.0264 0.0984  163 CYS B CA  
4730 C C   . CYS B 163 ? 2.0611 2.6768 2.4954 0.5464  -0.0308 0.0933  163 CYS B C   
4731 O O   . CYS B 163 ? 1.8283 2.4323 2.2233 0.5860  -0.0363 0.0802  163 CYS B O   
4732 C CB  . CYS B 163 ? 2.5458 3.0582 3.0008 0.4786  -0.0349 0.0843  163 CYS B CB  
4733 S SG  . CYS B 163 ? 2.3767 2.8446 2.8556 0.4338  -0.0316 0.0853  163 CYS B SG  
4734 N N   . LEU B 164 ? 2.0494 2.6971 2.5042 0.5373  -0.0293 0.1040  164 LEU B N   
4735 C CA  . LEU B 164 ? 1.9843 2.6612 2.4201 0.5740  -0.0331 0.1018  164 LEU B CA  
4736 C C   . LEU B 164 ? 1.7371 2.4888 2.1668 0.6140  -0.0250 0.1117  164 LEU B C   
4737 O O   . LEU B 164 ? 1.4137 2.1617 1.8033 0.6602  -0.0305 0.0985  164 LEU B O   
4738 C CB  . LEU B 164 ? 2.1859 2.8913 2.6511 0.5528  -0.0326 0.1154  164 LEU B CB  
4739 C CG  . LEU B 164 ? 2.3318 2.9617 2.7896 0.5269  -0.0424 0.1019  164 LEU B CG  
4740 C CD1 . LEU B 164 ? 2.3598 3.0205 2.8544 0.4953  -0.0404 0.1199  164 LEU B CD1 
4741 C CD2 . LEU B 164 ? 1.9683 2.5465 2.3790 0.5598  -0.0556 0.0792  164 LEU B CD2 
4742 N N   . ARG B 165 ? 1.8334 2.6506 2.3018 0.5954  -0.0127 0.1354  165 ARG B N   
4743 C CA  . ARG B 165 ? 1.6009 2.4995 2.0707 0.6277  -0.0024 0.1500  165 ARG B CA  
4744 C C   . ARG B 165 ? 1.6566 2.5183 2.0795 0.6639  -0.0057 0.1302  165 ARG B C   
4745 O O   . ARG B 165 ? 1.8901 2.7850 2.2836 0.7124  -0.0043 0.1269  165 ARG B O   
4746 C CB  . ARG B 165 ? 1.3340 2.3123 1.8552 0.5985  0.0098  0.1819  165 ARG B CB  
4747 C CG  . ARG B 165 ? 1.2296 2.2818 1.7779 0.6015  0.0126  0.2030  165 ARG B CG  
4748 C CD  . ARG B 165 ? 1.3678 2.4703 1.9707 0.5546  0.0168  0.2331  165 ARG B CD  
4749 N NE  . ARG B 165 ? 1.5863 2.6359 2.2015 0.5180  0.0073  0.2284  165 ARG B NE  
4750 C CZ  . ARG B 165 ? 1.7078 2.7877 2.3638 0.4788  0.0057  0.2514  165 ARG B CZ  
4751 N NH1 . ARG B 165 ? 1.6099 2.7779 2.3013 0.4705  0.0122  0.2828  165 ARG B NH1 
4752 N NH2 . ARG B 165 ? 1.9774 2.9999 2.6370 0.4487  -0.0032 0.2439  165 ARG B NH2 
4753 N N   . ALA B 166 ? 1.8017 2.5936 2.2173 0.6399  -0.0109 0.1176  166 ALA B N   
4754 C CA  . ALA B 166 ? 1.9623 2.7086 2.3356 0.6654  -0.0168 0.0997  166 ALA B CA  
4755 C C   . ALA B 166 ? 1.8273 2.5204 2.1454 0.7067  -0.0316 0.0749  166 ALA B C   
4756 O O   . ALA B 166 ? 1.6834 2.3490 1.9579 0.7406  -0.0383 0.0606  166 ALA B O   
4757 C CB  . ALA B 166 ? 2.3105 2.9950 2.6940 0.6260  -0.0203 0.0939  166 ALA B CB  
4758 N N   . GLY B 167 ? 1.7478 2.4123 2.0652 0.6992  -0.0394 0.0682  167 GLY B N   
4759 C CA  . GLY B 167 ? 1.9696 2.5660 2.2349 0.7293  -0.0571 0.0434  167 GLY B CA  
4760 C C   . GLY B 167 ? 1.9001 2.3975 2.1438 0.7073  -0.0715 0.0249  167 GLY B C   
4761 O O   . GLY B 167 ? 2.0182 2.4529 2.2107 0.7348  -0.0884 0.0043  167 GLY B O   
4762 N N   . VAL B 168 ? 1.8260 2.3108 2.1096 0.6574  -0.0656 0.0336  168 VAL B N   
4763 C CA  . VAL B 168 ? 1.8187 2.2167 2.0910 0.6310  -0.0776 0.0197  168 VAL B CA  
4764 C C   . VAL B 168 ? 1.7870 2.1479 2.0659 0.6085  -0.0837 0.0154  168 VAL B C   
4765 O O   . VAL B 168 ? 1.5891 1.9910 1.9041 0.5877  -0.0737 0.0291  168 VAL B O   
4766 C CB  . VAL B 168 ? 1.9000 2.2960 2.2038 0.5950  -0.0693 0.0288  168 VAL B CB  
4767 C CG1 . VAL B 168 ? 1.7877 2.2275 2.0859 0.6178  -0.0624 0.0350  168 VAL B CG1 
4768 C CG2 . VAL B 168 ? 1.9633 2.3940 2.3225 0.5506  -0.0555 0.0470  168 VAL B CG2 
4769 N N   . ALA B 169 ? 1.9275 2.2083 2.1677 0.6141  -0.1020 -0.0034 169 ALA B N   
4770 C CA  . ALA B 169 ? 2.0779 2.3124 2.3164 0.5943  -0.1103 -0.0095 169 ALA B CA  
4771 C C   . ALA B 169 ? 2.0843 2.3199 2.3703 0.5429  -0.0986 0.0023  169 ALA B C   
4772 O O   . ALA B 169 ? 2.1581 2.3727 2.4583 0.5188  -0.0957 0.0042  169 ALA B O   
4773 C CB  . ALA B 169 ? 2.2840 2.4307 2.4755 0.6033  -0.1326 -0.0290 169 ALA B CB  
4774 N N   . VAL B 170 ? 2.0180 2.2774 2.3266 0.5280  -0.0927 0.0103  170 VAL B N   
4775 C CA  . VAL B 170 ? 1.9068 2.1588 2.2527 0.4823  -0.0840 0.0195  170 VAL B CA  
4776 C C   . VAL B 170 ? 2.0512 2.2427 2.3795 0.4707  -0.0949 0.0091  170 VAL B C   
4777 O O   . VAL B 170 ? 2.2051 2.3729 2.4978 0.4978  -0.1082 -0.0024 170 VAL B O   
4778 C CB  . VAL B 170 ? 1.6867 2.0123 2.0756 0.4673  -0.0690 0.0399  170 VAL B CB  
4779 C CG1 . VAL B 170 ? 1.7313 2.1201 2.1359 0.4800  -0.0590 0.0519  170 VAL B CG1 
4780 C CG2 . VAL B 170 ? 1.7826 2.1387 2.1695 0.4815  -0.0713 0.0434  170 VAL B CG2 
4781 N N   . PRO B 171 ? 2.1438 2.3062 2.4937 0.4316  -0.0902 0.0125  171 PRO B N   
4782 C CA  . PRO B 171 ? 2.2252 2.3407 2.5621 0.4190  -0.0980 0.0058  171 PRO B CA  
4783 C C   . PRO B 171 ? 1.9247 2.0830 2.2725 0.4236  -0.0946 0.0135  171 PRO B C   
4784 O O   . PRO B 171 ? 1.7805 2.0004 2.1588 0.4193  -0.0833 0.0280  171 PRO B O   
4785 C CB  . PRO B 171 ? 2.2929 2.3783 2.6535 0.3780  -0.0902 0.0102  171 PRO B CB  
4786 C CG  . PRO B 171 ? 2.2592 2.3644 2.6382 0.3734  -0.0823 0.0156  171 PRO B CG  
4787 C CD  . PRO B 171 ? 2.2169 2.3883 2.6017 0.3995  -0.0777 0.0225  171 PRO B CD  
4788 N N   . GLY B 172 ? 1.7509 1.8759 2.0730 0.4322  -0.1062 0.0045  172 GLY B N   
4789 C CA  . GLY B 172 ? 1.7203 1.8798 2.0502 0.4365  -0.1056 0.0111  172 GLY B CA  
4790 C C   . GLY B 172 ? 1.6149 1.8011 1.9851 0.4003  -0.0927 0.0265  172 GLY B C   
4791 O O   . GLY B 172 ? 1.6191 1.7630 1.9948 0.3702  -0.0902 0.0252  172 GLY B O   
4792 N N   . GLY B 173 ? 1.6936 1.9500 2.0905 0.4042  -0.0854 0.0419  173 GLY B N   
4793 C CA  . GLY B 173 ? 1.7903 2.0732 2.2227 0.3713  -0.0770 0.0581  173 GLY B CA  
4794 C C   . GLY B 173 ? 1.6976 2.0641 2.1593 0.3782  -0.0711 0.0776  173 GLY B C   
4795 O O   . GLY B 173 ? 1.9093 2.3183 2.3661 0.4094  -0.0704 0.0790  173 GLY B O   
4796 N N   . THR B 174 ? 1.6600 2.0500 2.1509 0.3492  -0.0678 0.0936  174 THR B N   
4797 C CA  . THR B 174 ? 1.6417 2.1121 2.1639 0.3501  -0.0640 0.1158  174 THR B CA  
4798 C C   . THR B 174 ? 1.6914 2.1864 2.2377 0.3353  -0.0544 0.1262  174 THR B C   
4799 O O   . THR B 174 ? 1.7731 2.2195 2.3155 0.3182  -0.0510 0.1173  174 THR B O   
4800 C CB  . THR B 174 ? 1.6394 2.1240 2.1825 0.3231  -0.0680 0.1310  174 THR B CB  
4801 O OG1 . THR B 174 ? 2.0936 2.5103 2.6135 0.3128  -0.0747 0.1165  174 THR B OG1 
4802 C CG2 . THR B 174 ? 1.3884 1.9535 1.9513 0.3380  -0.0702 0.1505  174 THR B CG2 
4803 N N   . SER B 175 ? 1.5508 2.1232 2.1236 0.3401  -0.0506 0.1470  175 SER B N   
4804 C CA  . SER B 175 ? 1.7549 2.3587 2.3545 0.3225  -0.0429 0.1615  175 SER B CA  
4805 C C   . SER B 175 ? 1.6645 2.3043 2.2977 0.2901  -0.0455 0.1856  175 SER B C   
4806 O O   . SER B 175 ? 1.7515 2.4571 2.4119 0.2860  -0.0422 0.2073  175 SER B O   
4807 C CB  . SER B 175 ? 2.0273 2.6877 2.6275 0.3535  -0.0366 0.1664  175 SER B CB  
4808 O OG  . SER B 175 ? 1.9941 2.7151 2.5950 0.3818  -0.0383 0.1756  175 SER B OG  
4809 N N   . GLU B 176 ? 1.6290 2.2229 2.2577 0.2673  -0.0523 0.1819  176 GLU B N   
4810 C CA  . GLU B 176 ? 1.7737 2.3904 2.4267 0.2380  -0.0593 0.2027  176 GLU B CA  
4811 C C   . GLU B 176 ? 1.6019 2.1503 2.2506 0.2037  -0.0617 0.1963  176 GLU B C   
4812 O O   . GLU B 176 ? 1.5768 2.0592 2.1998 0.2039  -0.0619 0.1761  176 GLU B O   
4813 C CB  . GLU B 176 ? 2.1389 2.7767 2.7881 0.2493  -0.0681 0.2072  176 GLU B CB  
4814 C CG  . GLU B 176 ? 2.4822 3.1627 3.1607 0.2227  -0.0773 0.2344  176 GLU B CG  
4815 C CD  . GLU B 176 ? 2.6962 3.4618 3.4103 0.2183  -0.0752 0.2631  176 GLU B CD  
4816 O OE1 . GLU B 176 ? 2.8133 3.6424 3.5332 0.2491  -0.0695 0.2695  176 GLU B OE1 
4817 O OE2 . GLU B 176 ? 2.6601 3.4282 3.3948 0.1844  -0.0798 0.2797  176 GLU B OE2 
4818 N N   . VAL B 177 ? 1.5525 2.1191 2.2258 0.1749  -0.0640 0.2150  177 VAL B N   
4819 C CA  . VAL B 177 ? 1.6656 2.1762 2.3366 0.1422  -0.0682 0.2134  177 VAL B CA  
4820 C C   . VAL B 177 ? 1.6249 2.1003 2.2813 0.1321  -0.0785 0.2104  177 VAL B C   
4821 O O   . VAL B 177 ? 2.2891 2.8035 2.9523 0.1376  -0.0867 0.2222  177 VAL B O   
4822 C CB  . VAL B 177 ? 1.8614 2.4093 2.5617 0.1157  -0.0732 0.2384  177 VAL B CB  
4823 C CG1 . VAL B 177 ? 1.9240 2.4107 2.6186 0.0895  -0.0735 0.2321  177 VAL B CG1 
4824 C CG2 . VAL B 177 ? 2.0773 2.6940 2.7991 0.1291  -0.0661 0.2517  177 VAL B CG2 
4825 N N   . LEU B 178 ? 1.2833 1.6863 1.9207 0.1161  -0.0782 0.1961  178 LEU B N   
4826 C CA  . LEU B 178 ? 1.4751 1.8316 2.0925 0.1056  -0.0869 0.1901  178 LEU B CA  
4827 C C   . LEU B 178 ? 1.6841 2.0000 2.3005 0.0734  -0.0934 0.1960  178 LEU B C   
4828 O O   . LEU B 178 ? 1.9731 2.2279 2.5704 0.0668  -0.0877 0.1806  178 LEU B O   
4829 C CB  . LEU B 178 ? 1.4127 1.7144 1.9992 0.1224  -0.0806 0.1648  178 LEU B CB  
4830 C CG  . LEU B 178 ? 1.4106 1.7365 1.9897 0.1560  -0.0760 0.1550  178 LEU B CG  
4831 C CD1 . LEU B 178 ? 1.6175 1.8823 2.1691 0.1658  -0.0692 0.1314  178 LEU B CD1 
4832 C CD2 . LEU B 178 ? 1.6897 2.0413 2.2647 0.1685  -0.0858 0.1598  178 LEU B CD2 
4833 N N   . ARG B 179 ? 1.9516 2.3024 2.5868 0.0547  -0.1068 0.2191  179 ARG B N   
4834 C CA  . ARG B 179 ? 1.8433 2.1625 2.4787 0.0242  -0.1167 0.2285  179 ARG B CA  
4835 C C   . ARG B 179 ? 1.9781 2.2259 2.5818 0.0138  -0.1235 0.2162  179 ARG B C   
4836 O O   . ARG B 179 ? 2.0400 2.2503 2.6358 -0.0087 -0.1325 0.2207  179 ARG B O   
4837 C CB  . ARG B 179 ? 1.7228 2.1035 2.3893 0.0066  -0.1302 0.2590  179 ARG B CB  
4838 C CG  . ARG B 179 ? 1.6198 2.0535 2.3114 0.0149  -0.1197 0.2669  179 ARG B CG  
4839 C CD  . ARG B 179 ? 1.8245 2.3163 2.5472 -0.0061 -0.1325 0.2987  179 ARG B CD  
4840 N NE  . ARG B 179 ? 2.1943 2.7529 2.9421 0.0073  -0.1219 0.3087  179 ARG B NE  
4841 C CZ  . ARG B 179 ? 2.3907 3.0076 3.1478 0.0361  -0.1118 0.3093  179 ARG B CZ  
4842 N NH1 . ARG B 179 ? 2.6091 3.2303 3.3551 0.0551  -0.1119 0.3014  179 ARG B NH1 
4843 N NH2 . ARG B 179 ? 2.1984 2.8694 2.9745 0.0470  -0.1025 0.3183  179 ARG B NH2 
4844 N N   . SER B 180 ? 1.9871 2.2117 2.5696 0.0308  -0.1195 0.2001  180 SER B N   
4845 C CA  . SER B 180 ? 2.0317 2.1894 2.5823 0.0215  -0.1252 0.1889  180 SER B CA  
4846 C C   . SER B 180 ? 2.0251 2.1440 2.5508 0.0414  -0.1123 0.1649  180 SER B C   
4847 O O   . SER B 180 ? 2.2613 2.4104 2.7931 0.0637  -0.1046 0.1591  180 SER B O   
4848 C CB  . SER B 180 ? 2.3158 2.4852 2.8652 0.0116  -0.1441 0.2029  180 SER B CB  
4849 O OG  . SER B 180 ? 1.7086 1.9052 2.2571 0.0330  -0.1435 0.1989  180 SER B OG  
4850 N N   . GLU B 181 ? 1.9662 2.0180 2.4617 0.0330  -0.1119 0.1525  181 GLU B N   
4851 C CA  . GLU B 181 ? 1.9550 1.9650 2.4251 0.0474  -0.1010 0.1319  181 GLU B CA  
4852 C C   . GLU B 181 ? 2.0163 2.0440 2.4799 0.0636  -0.1070 0.1295  181 GLU B C   
4853 O O   . GLU B 181 ? 2.1405 2.1639 2.5961 0.0827  -0.0985 0.1164  181 GLU B O   
4854 C CB  . GLU B 181 ? 1.9148 1.8538 2.3526 0.0358  -0.0994 0.1213  181 GLU B CB  
4855 C CG  . GLU B 181 ? 2.0360 1.9484 2.4737 0.0221  -0.0939 0.1217  181 GLU B CG  
4856 C CD  . GLU B 181 ? 2.2939 2.1415 2.7000 0.0220  -0.0831 0.1058  181 GLU B CD  
4857 O OE1 . GLU B 181 ? 2.4227 2.2299 2.7992 0.0209  -0.0864 0.0991  181 GLU B OE1 
4858 O OE2 . GLU B 181 ? 2.3193 2.1584 2.7313 0.0234  -0.0702 0.1008  181 GLU B OE2 
4859 N N   . ALA B 182 ? 1.8199 1.8651 2.2862 0.0557  -0.1229 0.1424  182 ALA B N   
4860 C CA  . ALA B 182 ? 2.0766 2.1394 2.5372 0.0707  -0.1305 0.1414  182 ALA B CA  
4861 C C   . ALA B 182 ? 2.2645 2.3856 2.7451 0.0960  -0.1244 0.1422  182 ALA B C   
4862 O O   . ALA B 182 ? 2.9309 3.0453 3.3967 0.1175  -0.1221 0.1294  182 ALA B O   
4863 C CB  . ALA B 182 ? 2.5365 2.6155 3.0028 0.0555  -0.1494 0.1589  182 ALA B CB  
4864 N N   . GLU B 183 ? 1.9717 2.1472 2.4836 0.0929  -0.1230 0.1574  183 GLU B N   
4865 C CA  . GLU B 183 ? 2.0712 2.3074 2.6028 0.1170  -0.1169 0.1606  183 GLU B CA  
4866 C C   . GLU B 183 ? 2.2228 2.4295 2.7381 0.1357  -0.1034 0.1396  183 GLU B C   
4867 O O   . GLU B 183 ? 2.3923 2.6151 2.9004 0.1624  -0.1020 0.1314  183 GLU B O   
4868 C CB  . GLU B 183 ? 1.9550 2.2484 2.5209 0.1071  -0.1163 0.1809  183 GLU B CB  
4869 C CG  . GLU B 183 ? 2.1531 2.4885 2.7399 0.0896  -0.1321 0.2061  183 GLU B CG  
4870 C CD  . GLU B 183 ? 2.0544 2.4382 2.6735 0.0730  -0.1339 0.2284  183 GLU B CD  
4871 O OE1 . GLU B 183 ? 2.0742 2.4236 2.6905 0.0576  -0.1292 0.2244  183 GLU B OE1 
4872 O OE2 . GLU B 183 ? 2.0316 2.4868 2.6783 0.0745  -0.1406 0.2508  183 GLU B OE2 
4873 N N   . VAL B 184 ? 2.1719 2.3345 2.6806 0.1214  -0.0949 0.1318  184 VAL B N   
4874 C CA  . VAL B 184 ? 2.0819 2.2133 2.5778 0.1332  -0.0829 0.1145  184 VAL B CA  
4875 C C   . VAL B 184 ? 2.3796 2.4707 2.8451 0.1470  -0.0854 0.0985  184 VAL B C   
4876 O O   . VAL B 184 ? 3.0148 3.1055 3.4713 0.1683  -0.0826 0.0880  184 VAL B O   
4877 C CB  . VAL B 184 ? 1.8292 1.9180 2.3228 0.1138  -0.0741 0.1102  184 VAL B CB  
4878 C CG1 . VAL B 184 ? 1.7452 1.8007 2.2260 0.1243  -0.0630 0.0940  184 VAL B CG1 
4879 C CG2 . VAL B 184 ? 1.9235 2.0455 2.4446 0.0999  -0.0728 0.1250  184 VAL B CG2 
4880 N N   . VAL B 185 ? 2.1594 2.2139 2.6072 0.1340  -0.0921 0.0973  185 VAL B N   
4881 C CA  . VAL B 185 ? 2.0021 2.0138 2.4192 0.1429  -0.0958 0.0837  185 VAL B CA  
4882 C C   . VAL B 185 ? 2.1429 2.1894 2.5586 0.1686  -0.1042 0.0830  185 VAL B C   
4883 O O   . VAL B 185 ? 1.9639 1.9878 2.3592 0.1863  -0.1047 0.0696  185 VAL B O   
4884 C CB  . VAL B 185 ? 1.8373 1.7977 2.2322 0.1238  -0.1000 0.0817  185 VAL B CB  
4885 C CG1 . VAL B 185 ? 1.8424 1.7653 2.2066 0.1341  -0.1055 0.0696  185 VAL B CG1 
4886 C CG2 . VAL B 185 ? 1.3595 1.2797 1.7494 0.1069  -0.0885 0.0775  185 VAL B CG2 
4887 N N   . GLU B 186 ? 2.3468 2.4489 2.7841 0.1705  -0.1116 0.0986  186 GLU B N   
4888 C CA  . GLU B 186 ? 2.3088 2.4550 2.7487 0.1969  -0.1190 0.1009  186 GLU B CA  
4889 C C   . GLU B 186 ? 2.4972 2.6609 2.9365 0.2232  -0.1118 0.0920  186 GLU B C   
4890 O O   . GLU B 186 ? 2.7196 2.8612 3.1346 0.2446  -0.1159 0.0784  186 GLU B O   
4891 C CB  . GLU B 186 ? 2.1948 2.4039 2.6621 0.1926  -0.1275 0.1225  186 GLU B CB  
4892 C CG  . GLU B 186 ? 2.4181 2.6992 2.9036 0.2214  -0.1270 0.1301  186 GLU B CG  
4893 C CD  . GLU B 186 ? 2.6043 2.9530 3.1278 0.2128  -0.1235 0.1520  186 GLU B CD  
4894 O OE1 . GLU B 186 ? 2.5063 2.8434 3.0421 0.1829  -0.1234 0.1614  186 GLU B OE1 
4895 O OE2 . GLU B 186 ? 2.7049 3.1184 3.2448 0.2360  -0.1215 0.1605  186 GLU B OE2 
4896 N N   . ALA B 187 ? 2.3126 2.4984 2.7728 0.2168  -0.1019 0.0976  187 ALA B N   
4897 C CA  . ALA B 187 ? 2.2216 2.4243 2.6826 0.2388  -0.0951 0.0909  187 ALA B CA  
4898 C C   . ALA B 187 ? 2.2003 2.3403 2.6294 0.2476  -0.0947 0.0704  187 ALA B C   
4899 O O   . ALA B 187 ? 2.4577 2.5981 2.8707 0.2746  -0.0982 0.0606  187 ALA B O   
4900 C CB  . ALA B 187 ? 2.0260 2.2530 2.5133 0.2247  -0.0850 0.1003  187 ALA B CB  
4901 N N   . ILE B 188 ? 1.8814 1.9676 2.3010 0.2239  -0.0912 0.0652  188 ILE B N   
4902 C CA  . ILE B 188 ? 1.9149 1.9409 2.3080 0.2245  -0.0902 0.0496  188 ILE B CA  
4903 C C   . ILE B 188 ? 2.1063 2.1103 2.4703 0.2430  -0.1027 0.0400  188 ILE B C   
4904 O O   . ILE B 188 ? 2.0341 2.0101 2.3766 0.2583  -0.1069 0.0282  188 ILE B O   
4905 C CB  . ILE B 188 ? 1.7810 1.7616 2.1714 0.1954  -0.0830 0.0491  188 ILE B CB  
4906 C CG1 . ILE B 188 ? 1.4674 1.4613 1.8823 0.1809  -0.0710 0.0555  188 ILE B CG1 
4907 C CG2 . ILE B 188 ? 1.9265 1.8465 2.2877 0.1943  -0.0839 0.0360  188 ILE B CG2 
4908 C CD1 . ILE B 188 ? 1.3989 1.3472 1.8085 0.1575  -0.0627 0.0534  188 ILE B CD1 
4909 N N   . HIS B 189 ? 2.1808 2.1931 2.5426 0.2398  -0.1104 0.0455  189 HIS B N   
4910 C CA  . HIS B 189 ? 2.1301 2.1181 2.4633 0.2561  -0.1232 0.0365  189 HIS B CA  
4911 C C   . HIS B 189 ? 1.9198 1.9448 2.2497 0.2916  -0.1295 0.0332  189 HIS B C   
4912 O O   . HIS B 189 ? 2.0016 1.9959 2.3026 0.3117  -0.1385 0.0203  189 HIS B O   
4913 C CB  . HIS B 189 ? 2.2795 2.2542 2.6080 0.2394  -0.1294 0.0419  189 HIS B CB  
4914 C CG  . HIS B 189 ? 2.2923 2.2124 2.6097 0.2115  -0.1231 0.0389  189 HIS B CG  
4915 N ND1 . HIS B 189 ? 2.2181 2.1181 2.5407 0.1990  -0.1106 0.0363  189 HIS B ND1 
4916 C CD2 . HIS B 189 ? 2.2262 2.1068 2.5250 0.1960  -0.1277 0.0378  189 HIS B CD2 
4917 C CE1 . HIS B 189 ? 2.0667 1.9203 2.3751 0.1780  -0.1068 0.0342  189 HIS B CE1 
4918 N NE2 . HIS B 189 ? 1.9067 1.7468 2.1995 0.1757  -0.1170 0.0349  189 HIS B NE2 
4919 N N   . ARG B 190 ? 1.6025 1.6943 1.9616 0.2993  -0.1249 0.0460  190 ARG B N   
4920 C CA  . ARG B 190 ? 1.6685 1.8056 2.0274 0.3346  -0.1280 0.0452  190 ARG B CA  
4921 C C   . ARG B 190 ? 1.7240 1.8442 2.0731 0.3467  -0.1234 0.0350  190 ARG B C   
4922 O O   . ARG B 190 ? 1.7033 1.8678 2.0735 0.3523  -0.1149 0.0422  190 ARG B O   
4923 C CB  . ARG B 190 ? 1.7100 1.9275 2.1053 0.3362  -0.1235 0.0651  190 ARG B CB  
4924 C CG  . ARG B 190 ? 1.9873 2.2625 2.3846 0.3747  -0.1245 0.0671  190 ARG B CG  
4925 C CD  . ARG B 190 ? 2.0307 2.3891 2.4621 0.3777  -0.1230 0.0893  190 ARG B CD  
4926 N NE  . ARG B 190 ? 2.0978 2.4867 2.5640 0.3489  -0.1131 0.1059  190 ARG B NE  
4927 C CZ  . ARG B 190 ? 2.0930 2.4786 2.5780 0.3141  -0.1144 0.1186  190 ARG B CZ  
4928 N NH1 . ARG B 190 ? 1.9785 2.3320 2.4515 0.3028  -0.1242 0.1167  190 ARG B NH1 
4929 N NH2 . ARG B 190 ? 2.0759 2.4876 2.5894 0.2912  -0.1071 0.1330  190 ARG B NH2 
4930 N N   . LEU B 191 ? 1.7828 1.8393 2.0994 0.3502  -0.1303 0.0192  191 LEU B N   
4931 C CA  . LEU B 191 ? 2.0312 2.0675 2.3397 0.3565  -0.1275 0.0112  191 LEU B CA  
4932 C C   . LEU B 191 ? 2.0982 2.0898 2.3654 0.3824  -0.1430 -0.0048 191 LEU B C   
4933 O O   . LEU B 191 ? 2.0361 1.9973 2.2799 0.3870  -0.1548 -0.0108 191 LEU B O   
4934 C CB  . LEU B 191 ? 2.0978 2.0996 2.4178 0.3224  -0.1173 0.0126  191 LEU B CB  
4935 C CG  . LEU B 191 ? 1.9939 2.0178 2.3355 0.3181  -0.1061 0.0169  191 LEU B CG  
4936 C CD1 . LEU B 191 ? 1.7473 1.8446 2.1187 0.3253  -0.0992 0.0306  191 LEU B CD1 
4937 C CD2 . LEU B 191 ? 1.8907 1.8842 2.2454 0.2841  -0.0958 0.0198  191 LEU B CD2 
4938 N N   . SER B 192 ? 2.2998 2.2850 2.5573 0.3982  -0.1443 -0.0112 192 SER B N   
4939 C CA  . SER B 192 ? 2.6428 2.5994 2.8609 0.4316  -0.1609 -0.0251 192 SER B CA  
4940 C C   . SER B 192 ? 2.5234 2.4015 2.7087 0.4200  -0.1749 -0.0359 192 SER B C   
4941 O O   . SER B 192 ? 2.6650 2.5067 2.8119 0.4444  -0.1932 -0.0478 192 SER B O   
4942 C CB  . SER B 192 ? 2.5785 2.5486 2.7956 0.4484  -0.1587 -0.0277 192 SER B CB  
4943 O OG  . SER B 192 ? 2.4435 2.4862 2.6954 0.4516  -0.1434 -0.0149 192 SER B OG  
4944 N N   . CYS B 193 ? 2.3575 2.2102 2.5573 0.3830  -0.1665 -0.0308 193 CYS B N   
4945 C CA  . CYS B 193 ? 2.5395 2.3230 2.7148 0.3664  -0.1761 -0.0373 193 CYS B CA  
4946 C C   . CYS B 193 ? 2.7722 2.5236 2.9217 0.3840  -0.1896 -0.0464 193 CYS B C   
4947 O O   . CYS B 193 ? 2.8365 2.6087 3.0011 0.3865  -0.1823 -0.0442 193 CYS B O   
4948 C CB  . CYS B 193 ? 2.0782 1.8302 2.2283 0.3675  -0.1888 -0.0416 193 CYS B CB  
4949 S SG  . CYS B 193 ? 2.3772 2.1500 2.5549 0.3372  -0.1737 -0.0302 193 CYS B SG  
4950 N N   . GLY B 194 ? 2.9261 2.6249 3.0345 0.3966  -0.2113 -0.0565 194 GLY B N   
4951 C CA  . GLY B 194 ? 2.9888 2.6402 3.0662 0.4075  -0.2292 -0.0648 194 GLY B CA  
4952 C C   . GLY B 194 ? 3.2236 2.8188 3.2956 0.3738  -0.2335 -0.0617 194 GLY B C   
4953 O O   . GLY B 194 ? 3.2787 2.8813 3.3779 0.3424  -0.2167 -0.0525 194 GLY B O   
4954 N N   . THR B 195 ? 3.2984 2.8375 3.3338 0.3813  -0.2571 -0.0688 195 THR B N   
4955 C CA  . THR B 195 ? 3.2530 2.7398 3.2820 0.3503  -0.2641 -0.0637 195 THR B CA  
4956 C C   . THR B 195 ? 3.0279 2.5416 3.1004 0.3213  -0.2405 -0.0521 195 THR B C   
4957 O O   . THR B 195 ? 2.8594 2.3988 2.9473 0.3293  -0.2344 -0.0516 195 THR B O   
4958 C CB  . THR B 195 ? 3.3909 2.8196 3.3771 0.3643  -0.2945 -0.0712 195 THR B CB  
4959 O OG1 . THR B 195 ? 3.2031 2.6551 3.1997 0.3777  -0.2908 -0.0725 195 THR B OG1 
4960 C CG2 . THR B 195 ? 3.3876 2.7879 3.3273 0.3973  -0.3193 -0.0841 195 THR B CG2 
4961 N N   . ALA B 196 ? 2.9899 2.4987 3.0807 0.2895  -0.2270 -0.0430 196 ALA B N   
4962 C CA  . ALA B 196 ? 3.0807 2.6141 3.2114 0.2626  -0.2036 -0.0320 196 ALA B CA  
4963 C C   . ALA B 196 ? 3.3870 2.8907 3.5193 0.2311  -0.1988 -0.0235 196 ALA B C   
4964 O O   . ALA B 196 ? 3.4473 2.9517 3.5769 0.2245  -0.1926 -0.0229 196 ALA B O   
4965 C CB  . ALA B 196 ? 2.7157 2.3094 2.8793 0.2663  -0.1809 -0.0296 196 ALA B CB  
4966 N N   . ALA B 197 ? 3.6326 3.1109 3.7685 0.2123  -0.2023 -0.0161 197 ALA B N   
4967 C CA  . ALA B 197 ? 3.5864 3.0409 3.7259 0.1824  -0.1966 -0.0054 197 ALA B CA  
4968 C C   . ALA B 197 ? 3.3528 2.8387 3.5159 0.1700  -0.1702 -0.0013 197 ALA B C   
4969 O O   . ALA B 197 ? 3.4115 2.8795 3.5608 0.1604  -0.1694 0.0001  197 ALA B O   
4970 C CB  . ALA B 197 ? 3.5831 3.0300 3.7399 0.1639  -0.1955 0.0051  197 ALA B CB  
4971 N N   . ALA B 198 ? 3.0036 2.5340 3.1995 0.1712  -0.1504 0.0001  198 ALA B N   
4972 C CA  . ALA B 198 ? 3.0809 2.6402 3.2985 0.1609  -0.1273 0.0037  198 ALA B CA  
4973 C C   . ALA B 198 ? 3.0035 2.6070 3.2359 0.1791  -0.1214 -0.0013 198 ALA B C   
4974 O O   . ALA B 198 ? 3.6041 3.2402 3.8655 0.1763  -0.1072 0.0024  198 ALA B O   
4975 C CB  . ALA B 198 ? 3.1276 2.6950 3.3729 0.1384  -0.1082 0.0145  198 ALA B CB  
4976 N N   . ARG B 199 ? 2.6263 2.2315 2.8389 0.1972  -0.1327 -0.0086 199 ARG B N   
4977 C CA  . ARG B 199 ? 2.5133 2.1626 2.7369 0.2169  -0.1304 -0.0119 199 ARG B CA  
4978 C C   . ARG B 199 ? 2.4231 2.1112 2.6813 0.2030  -0.1084 -0.0043 199 ARG B C   
4979 O O   . ARG B 199 ? 1.8710 1.5511 2.1326 0.1852  -0.0984 -0.0001 199 ARG B O   
4980 C CB  . ARG B 199 ? 2.3935 2.0350 2.5912 0.2328  -0.1441 -0.0182 199 ARG B CB  
4981 C CG  . ARG B 199 ? 2.4874 2.0826 2.6625 0.2163  -0.1494 -0.0177 199 ARG B CG  
4982 C CD  . ARG B 199 ? 2.7726 2.3616 2.9255 0.2281  -0.1606 -0.0227 199 ARG B CD  
4983 N NE  . ARG B 199 ? 3.1987 2.8261 3.3738 0.2229  -0.1464 -0.0179 199 ARG B NE  
4984 C CZ  . ARG B 199 ? 3.3772 2.9957 3.5463 0.2111  -0.1436 -0.0156 199 ARG B CZ  
4985 N NH1 . ARG B 199 ? 3.1710 2.8228 3.3629 0.2031  -0.1309 -0.0096 199 ARG B NH1 
4986 N NH2 . ARG B 199 ? 3.7524 3.3261 3.8916 0.2059  -0.1545 -0.0185 199 ARG B NH2 
4987 N N   . ARG B 200 ? 2.4675 2.1947 2.7483 0.2120  -0.1025 -0.0026 200 ARG B N   
4988 C CA  . ARG B 200 ? 1.9493 1.7099 2.2628 0.1986  -0.0842 0.0051  200 ARG B CA  
4989 C C   . ARG B 200 ? 2.0086 1.8210 2.3383 0.2146  -0.0831 0.0070  200 ARG B C   
4990 O O   . ARG B 200 ? 2.0290 1.8584 2.3510 0.2382  -0.0928 0.0027  200 ARG B O   
4991 C CB  . ARG B 200 ? 1.9062 1.6611 2.2381 0.1845  -0.0743 0.0094  200 ARG B CB  
4992 C CG  . ARG B 200 ? 2.0960 1.8193 2.4271 0.1613  -0.0651 0.0136  200 ARG B CG  
4993 C CD  . ARG B 200 ? 2.2656 1.9838 2.6151 0.1484  -0.0560 0.0192  200 ARG B CD  
4994 N NE  . ARG B 200 ? 2.2298 1.9132 2.5608 0.1485  -0.0697 0.0179  200 ARG B NE  
4995 C CZ  . ARG B 200 ? 2.3853 2.0595 2.7268 0.1403  -0.0695 0.0228  200 ARG B CZ  
4996 N NH1 . ARG B 200 ? 2.4364 2.1328 2.8077 0.1307  -0.0537 0.0290  200 ARG B NH1 
4997 N NH2 . ARG B 200 ? 2.9210 2.5622 3.2422 0.1412  -0.0868 0.0222  200 ARG B NH2 
4998 N N   . ALA B 201 ? 1.9801 1.8194 2.3340 0.2006  -0.0702 0.0149  201 ALA B N   
4999 C CA  . ALA B 201 ? 1.7293 1.6218 2.1063 0.2075  -0.0662 0.0215  201 ALA B CA  
5000 C C   . ALA B 201 ? 1.5885 1.4965 1.9941 0.1903  -0.0521 0.0290  201 ALA B C   
5001 O O   . ALA B 201 ? 1.5140 1.3956 1.9230 0.1706  -0.0432 0.0305  201 ALA B O   
5002 C CB  . ALA B 201 ? 1.7562 1.6654 2.1317 0.2068  -0.0694 0.0255  201 ALA B CB  
5003 N N   . MET B 202 ? 1.4762 1.4289 1.9013 0.1995  -0.0502 0.0341  202 MET B N   
5004 C CA  . MET B 202 ? 1.4434 1.4148 1.8955 0.1864  -0.0392 0.0414  202 MET B CA  
5005 C C   . MET B 202 ? 1.4859 1.5086 1.9595 0.1857  -0.0376 0.0525  202 MET B C   
5006 O O   . MET B 202 ? 1.6576 1.7176 2.1321 0.2038  -0.0432 0.0549  202 MET B O   
5007 C CB  . MET B 202 ? 1.4514 1.4239 1.9071 0.1960  -0.0392 0.0382  202 MET B CB  
5008 C CG  . MET B 202 ? 1.6878 1.6519 2.1635 0.1778  -0.0281 0.0422  202 MET B CG  
5009 S SD  . MET B 202 ? 2.1166 2.1168 2.6084 0.1911  -0.0283 0.0448  202 MET B SD  
5010 C CE  . MET B 202 ? 1.9221 1.8831 2.3877 0.2057  -0.0397 0.0337  202 MET B CE  
5011 N N   . VAL B 203 ? 1.5871 1.6104 2.0772 0.1642  -0.0302 0.0602  203 VAL B N   
5012 C CA  . VAL B 203 ? 1.6846 1.7488 2.1947 0.1563  -0.0307 0.0732  203 VAL B CA  
5013 C C   . VAL B 203 ? 1.3367 1.4200 1.8710 0.1470  -0.0234 0.0804  203 VAL B C   
5014 O O   . VAL B 203 ? 1.3297 1.3825 1.8663 0.1319  -0.0167 0.0786  203 VAL B O   
5015 C CB  . VAL B 203 ? 1.8050 1.8418 2.3084 0.1367  -0.0312 0.0757  203 VAL B CB  
5016 C CG1 . VAL B 203 ? 1.7439 1.8133 2.2666 0.1228  -0.0343 0.0907  203 VAL B CG1 
5017 C CG2 . VAL B 203 ? 1.9090 1.9200 2.3869 0.1422  -0.0384 0.0688  203 VAL B CG2 
5018 N N   . LYS B 204 ? 1.2519 1.3862 1.8034 0.1561  -0.0248 0.0892  204 LYS B N   
5019 C CA  . LYS B 204 ? 1.3617 1.5142 1.9340 0.1504  -0.0189 0.0950  204 LYS B CA  
5020 C C   . LYS B 204 ? 1.3870 1.5797 1.9816 0.1366  -0.0210 0.1121  204 LYS B C   
5021 O O   . LYS B 204 ? 1.8415 2.0810 2.4430 0.1461  -0.0259 0.1214  204 LYS B O   
5022 C CB  . LYS B 204 ? 1.4784 1.6572 2.0501 0.1735  -0.0194 0.0919  204 LYS B CB  
5023 C CG  . LYS B 204 ? 1.3028 1.4443 1.8529 0.1882  -0.0207 0.0768  204 LYS B CG  
5024 C CD  . LYS B 204 ? 1.3387 1.5087 1.8926 0.2063  -0.0211 0.0771  204 LYS B CD  
5025 C CE  . LYS B 204 ? 1.4223 1.5556 1.9561 0.2191  -0.0251 0.0641  204 LYS B CE  
5026 N NZ  . LYS B 204 ? 1.5318 1.6413 2.0372 0.2341  -0.0340 0.0542  204 LYS B NZ  
5027 N N   . LEU B 205 ? 1.3465 1.5202 1.9507 0.1150  -0.0181 0.1166  205 LEU B N   
5028 C CA  . LEU B 205 ? 1.5368 1.7375 2.1586 0.0977  -0.0233 0.1332  205 LEU B CA  
5029 C C   . LEU B 205 ? 1.6418 1.9006 2.2856 0.1041  -0.0234 0.1457  205 LEU B C   
5030 O O   . LEU B 205 ? 1.6150 1.8768 2.2647 0.1108  -0.0172 0.1419  205 LEU B O   
5031 C CB  . LEU B 205 ? 1.4825 1.6423 2.1048 0.0770  -0.0208 0.1325  205 LEU B CB  
5032 C CG  . LEU B 205 ? 1.3886 1.4930 1.9874 0.0709  -0.0198 0.1218  205 LEU B CG  
5033 C CD1 . LEU B 205 ? 1.1378 1.2032 1.7352 0.0568  -0.0147 0.1192  205 LEU B CD1 
5034 C CD2 . LEU B 205 ? 1.4900 1.5969 2.0800 0.0634  -0.0308 0.1288  205 LEU B CD2 
5035 N N   . ASP B 206 ? 1.6549 1.9617 2.3110 0.1013  -0.0310 0.1622  206 ASP B N   
5036 C CA  . ASP B 206 ? 1.7231 2.0953 2.3962 0.1141  -0.0308 0.1748  206 ASP B CA  
5037 C C   . ASP B 206 ? 1.6293 2.0201 2.3222 0.1037  -0.0278 0.1845  206 ASP B C   
5038 O O   . ASP B 206 ? 1.5565 1.9841 2.2564 0.1193  -0.0233 0.1870  206 ASP B O   
5039 C CB  . ASP B 206 ? 1.9737 2.3972 2.6573 0.1132  -0.0395 0.1926  206 ASP B CB  
5040 C CG  . ASP B 206 ? 2.1401 2.6390 2.8415 0.1287  -0.0380 0.2077  206 ASP B CG  
5041 O OD1 . ASP B 206 ? 2.1397 2.6501 2.8307 0.1565  -0.0315 0.1971  206 ASP B OD1 
5042 O OD2 . ASP B 206 ? 2.2171 2.7622 2.9413 0.1131  -0.0440 0.2308  206 ASP B OD2 
5043 N N   . ALA B 207 ? 1.6142 1.9779 2.3136 0.0782  -0.0313 0.1899  207 ALA B N   
5044 C CA  . ALA B 207 ? 1.7021 2.0795 2.4198 0.0654  -0.0309 0.2003  207 ALA B CA  
5045 C C   . ALA B 207 ? 1.7066 2.0733 2.4225 0.0802  -0.0205 0.1875  207 ALA B C   
5046 O O   . ALA B 207 ? 1.4787 1.8074 2.1775 0.0926  -0.0147 0.1690  207 ALA B O   
5047 C CB  . ALA B 207 ? 1.7164 2.0512 2.4333 0.0393  -0.0372 0.2032  207 ALA B CB  
5048 N N   . ILE B 208 ? 1.8985 2.2985 2.6319 0.0773  -0.0196 0.1986  208 ILE B N   
5049 C CA  . ILE B 208 ? 1.8607 2.2519 2.5939 0.0887  -0.0118 0.1889  208 ILE B CA  
5050 C C   . ILE B 208 ? 1.9689 2.3108 2.7046 0.0714  -0.0102 0.1831  208 ILE B C   
5051 O O   . ILE B 208 ? 2.0122 2.3317 2.7458 0.0785  -0.0040 0.1720  208 ILE B O   
5052 C CB  . ILE B 208 ? 1.7960 2.2471 2.5433 0.0981  -0.0107 0.2024  208 ILE B CB  
5053 C CG1 . ILE B 208 ? 1.5749 2.0259 2.3380 0.0835  -0.0106 0.2100  208 ILE B CG1 
5054 C CG2 . ILE B 208 ? 1.9642 2.4778 2.7215 0.0998  -0.0158 0.2218  208 ILE B CG2 
5055 C CD1 . ILE B 208 ? 1.5337 2.0094 2.2975 0.1019  -0.0050 0.2081  208 ILE B CD1 
5056 N N   . THR B 209 ? 2.1044 2.4289 2.8431 0.0495  -0.0171 0.1908  209 THR B N   
5057 C CA  . THR B 209 ? 2.0687 2.3431 2.8055 0.0345  -0.0167 0.1851  209 THR B CA  
5058 C C   . THR B 209 ? 2.1559 2.3809 2.8752 0.0446  -0.0078 0.1646  209 THR B C   
5059 O O   . THR B 209 ? 2.5118 2.7018 3.2312 0.0409  -0.0027 0.1569  209 THR B O   
5060 C CB  . THR B 209 ? 2.0901 2.3523 2.8254 0.0129  -0.0283 0.1963  209 THR B CB  
5061 O OG1 . THR B 209 ? 2.2670 2.4912 2.9818 0.0159  -0.0270 0.1841  209 THR B OG1 
5062 C CG2 . THR B 209 ? 1.9241 2.2425 2.6739 0.0042  -0.0392 0.2187  209 THR B CG2 
5063 N N   . TRP B 210 ? 1.9613 2.1857 2.6663 0.0573  -0.0065 0.1570  210 TRP B N   
5064 C CA  . TRP B 210 ? 2.0227 2.2025 2.7095 0.0651  -0.0001 0.1401  210 TRP B CA  
5065 C C   . TRP B 210 ? 2.4570 2.6389 3.1406 0.0840  0.0056  0.1298  210 TRP B C   
5066 O O   . TRP B 210 ? 2.7692 2.9241 3.4364 0.0931  0.0083  0.1179  210 TRP B O   
5067 C CB  . TRP B 210 ? 2.2168 2.3904 2.8875 0.0664  -0.0047 0.1385  210 TRP B CB  
5068 C CG  . TRP B 210 ? 2.1065 2.2442 2.7679 0.0494  -0.0084 0.1395  210 TRP B CG  
5069 C CD1 . TRP B 210 ? 2.0849 2.2226 2.7371 0.0422  -0.0172 0.1451  210 TRP B CD1 
5070 C CD2 . TRP B 210 ? 2.1406 2.2350 2.7982 0.0391  -0.0042 0.1345  210 TRP B CD2 
5071 N NE1 . TRP B 210 ? 2.2534 2.3466 2.8930 0.0285  -0.0194 0.1428  210 TRP B NE1 
5072 C CE2 . TRP B 210 ? 2.1444 2.2112 2.7866 0.0274  -0.0110 0.1362  210 TRP B CE2 
5073 C CE3 . TRP B 210 ? 2.4682 2.5448 3.1331 0.0399  0.0042  0.1290  210 TRP B CE3 
5074 C CZ2 . TRP B 210 ? 2.5131 2.5342 3.1441 0.0186  -0.0092 0.1318  210 TRP B CZ2 
5075 C CZ3 . TRP B 210 ? 2.9007 2.9368 3.5582 0.0309  0.0066  0.1257  210 TRP B CZ3 
5076 C CH2 . TRP B 210 ? 2.9377 2.9453 3.5768 0.0217  0.0005  0.1262  210 TRP B CH2 
5077 N N   . ALA B 211 ? 2.7740 2.9852 3.4714 0.0890  0.0061  0.1350  211 ALA B N   
5078 C CA  . ALA B 211 ? 2.9154 3.1320 3.6068 0.1084  0.0082  0.1269  211 ALA B CA  
5079 C C   . ALA B 211 ? 2.7145 2.8824 3.3946 0.1108  0.0126  0.1127  211 ALA B C   
5080 O O   . ALA B 211 ? 2.0222 2.1588 2.7062 0.0974  0.0170  0.1108  211 ALA B O   
5081 C CB  . ALA B 211 ? 2.7281 2.9749 3.4348 0.1106  0.0083  0.1344  211 ALA B CB  
5082 N N   . ALA B 212 ? 2.6466 2.8091 3.3112 0.1286  0.0104  0.1037  212 ALA B N   
5083 C CA  . ALA B 212 ? 2.2583 2.3774 2.9111 0.1306  0.0120  0.0924  212 ALA B CA  
5084 C C   . ALA B 212 ? 2.0336 2.1236 2.6767 0.1208  0.0148  0.0890  212 ALA B C   
5085 O O   . ALA B 212 ? 2.1231 2.2253 2.7604 0.1196  0.0121  0.0921  212 ALA B O   
5086 C CB  . ALA B 212 ? 2.0296 2.1330 2.6970 0.1229  0.0162  0.0924  212 ALA B CB  
5087 N N   . SER B 213 ? 1.8132 1.8662 2.4547 0.1139  0.0199  0.0837  213 SER B N   
5088 C CA  . SER B 213 ? 2.1876 2.2097 2.8131 0.1097  0.0221  0.0785  213 SER B CA  
5089 C C   . SER B 213 ? 2.1766 2.1838 2.8072 0.0943  0.0292  0.0818  213 SER B C   
5090 O O   . SER B 213 ? 2.2171 2.1962 2.8474 0.0883  0.0367  0.0792  213 SER B O   
5091 C CB  . SER B 213 ? 2.7845 2.7757 3.4001 0.1131  0.0224  0.0716  213 SER B CB  
5092 O OG  . SER B 213 ? 3.3410 3.3047 3.9412 0.1077  0.0254  0.0682  213 SER B OG  
5093 N N   . ILE B 214 ? 1.9408 1.9662 2.5747 0.0882  0.0261  0.0883  214 ILE B N   
5094 C CA  . ILE B 214 ? 1.8335 1.8363 2.4612 0.0760  0.0288  0.0896  214 ILE B CA  
5095 C C   . ILE B 214 ? 1.7954 1.8065 2.4089 0.0772  0.0209  0.0910  214 ILE B C   
5096 O O   . ILE B 214 ? 1.7106 1.6944 2.3072 0.0722  0.0214  0.0879  214 ILE B O   
5097 C CB  . ILE B 214 ? 1.8731 1.8840 2.5170 0.0648  0.0288  0.0977  214 ILE B CB  
5098 C CG1 . ILE B 214 ? 1.9580 1.9757 2.6209 0.0667  0.0337  0.0982  214 ILE B CG1 
5099 C CG2 . ILE B 214 ? 1.8956 1.8720 2.5277 0.0545  0.0315  0.0967  214 ILE B CG2 
5100 C CD1 . ILE B 214 ? 1.9687 1.9902 2.6469 0.0563  0.0334  0.1055  214 ILE B CD1 
5101 N N   . GLY B 215 ? 1.9053 1.9558 2.5257 0.0853  0.0141  0.0960  215 GLY B N   
5102 C CA  . GLY B 215 ? 1.9977 2.0701 2.6107 0.0886  0.0057  0.1003  215 GLY B CA  
5103 C C   . GLY B 215 ? 2.0653 2.1191 2.6566 0.1005  0.0043  0.0902  215 GLY B C   
5104 O O   . GLY B 215 ? 2.4001 2.4364 2.9765 0.0962  0.0012  0.0888  215 GLY B O   
5105 N N   . ASN B 216 ? 1.9866 2.0410 2.5745 0.1150  0.0049  0.0834  216 ASN B N   
5106 C CA  . ASN B 216 ? 1.5139 1.5491 2.0796 0.1277  0.0009  0.0739  216 ASN B CA  
5107 C C   . ASN B 216 ? 1.3489 1.3392 1.8993 0.1173  0.0048  0.0684  216 ASN B C   
5108 O O   . ASN B 216 ? 1.4499 1.4163 2.0047 0.1081  0.0128  0.0671  216 ASN B O   
5109 C CB  . ASN B 216 ? 1.3625 1.3952 1.9248 0.1420  -0.0008 0.0676  216 ASN B CB  
5110 C CG  . ASN B 216 ? 1.6181 1.6936 2.1941 0.1527  -0.0030 0.0731  216 ASN B CG  
5111 O OD1 . ASN B 216 ? 2.1906 2.3021 2.7811 0.1485  -0.0029 0.0831  216 ASN B OD1 
5112 N ND2 . ASN B 216 ? 1.3476 1.4197 1.9186 0.1658  -0.0060 0.0679  216 ASN B ND2 
5113 N N   . VAL B 217 ? 1.2656 1.2465 1.7977 0.1197  -0.0007 0.0659  217 VAL B N   
5114 C CA  . VAL B 217 ? 1.2775 1.2173 1.7907 0.1114  0.0018  0.0611  217 VAL B CA  
5115 C C   . VAL B 217 ? 1.4378 1.3659 1.9284 0.1240  -0.0065 0.0541  217 VAL B C   
5116 O O   . VAL B 217 ? 1.7960 1.7486 2.2827 0.1351  -0.0154 0.0551  217 VAL B O   
5117 C CB  . VAL B 217 ? 1.3411 1.2713 1.8510 0.0971  0.0027  0.0658  217 VAL B CB  
5118 C CG1 . VAL B 217 ? 1.2496 1.1378 1.7339 0.0925  0.0041  0.0599  217 VAL B CG1 
5119 C CG2 . VAL B 217 ? 1.4849 1.4148 2.0113 0.0848  0.0099  0.0712  217 VAL B CG2 
5120 N N   . LEU B 218 ? 1.4788 1.3678 1.9531 0.1210  -0.0039 0.0480  218 LEU B N   
5121 C CA  . LEU B 218 ? 1.7792 1.6484 2.2306 0.1318  -0.0129 0.0409  218 LEU B CA  
5122 C C   . LEU B 218 ? 1.9256 1.7598 2.3547 0.1235  -0.0126 0.0383  218 LEU B C   
5123 O O   . LEU B 218 ? 1.9609 1.7725 2.3889 0.1103  -0.0026 0.0398  218 LEU B O   
5124 C CB  . LEU B 218 ? 1.8047 1.6598 2.2586 0.1341  -0.0120 0.0384  218 LEU B CB  
5125 C CG  . LEU B 218 ? 2.0892 1.9119 2.5178 0.1405  -0.0221 0.0321  218 LEU B CG  
5126 C CD1 . LEU B 218 ? 2.4099 2.2467 2.8275 0.1622  -0.0367 0.0270  218 LEU B CD1 
5127 C CD2 . LEU B 218 ? 1.7063 1.5021 2.1374 0.1300  -0.0174 0.0339  218 LEU B CD2 
5128 N N   . ILE B 219 ? 1.7966 1.6289 2.2072 0.1330  -0.0238 0.0348  219 ILE B N   
5129 C CA  . ILE B 219 ? 1.6572 1.4600 2.0446 0.1272  -0.0265 0.0325  219 ILE B CA  
5130 C C   . ILE B 219 ? 1.5787 1.3606 1.9418 0.1392  -0.0388 0.0255  219 ILE B C   
5131 O O   . ILE B 219 ? 1.8392 1.6414 2.2000 0.1566  -0.0496 0.0228  219 ILE B O   
5132 C CB  . ILE B 219 ? 1.7431 1.5659 2.1327 0.1248  -0.0305 0.0370  219 ILE B CB  
5133 C CG1 . ILE B 219 ? 1.8377 1.6602 2.2394 0.1085  -0.0209 0.0431  219 ILE B CG1 
5134 C CG2 . ILE B 219 ? 1.9972 1.7979 2.3605 0.1267  -0.0400 0.0335  219 ILE B CG2 
5135 C CD1 . ILE B 219 ? 1.5929 1.4587 2.0224 0.1086  -0.0206 0.0509  219 ILE B CD1 
5136 N N   . ASP B 220 ? 1.4528 1.1942 1.7962 0.1302  -0.0373 0.0233  220 ASP B N   
5137 C CA  . ASP B 220 ? 1.8031 1.5174 2.1192 0.1384  -0.0510 0.0175  220 ASP B CA  
5138 C C   . ASP B 220 ? 1.8255 1.5351 2.1239 0.1408  -0.0587 0.0157  220 ASP B C   
5139 O O   . ASP B 220 ? 1.6754 1.3699 1.9678 0.1274  -0.0517 0.0182  220 ASP B O   
5140 C CB  . ASP B 220 ? 1.8755 1.5523 2.1795 0.1284  -0.0492 0.0179  220 ASP B CB  
5141 C CG  . ASP B 220 ? 1.8145 1.4614 2.1031 0.1129  -0.0412 0.0204  220 ASP B CG  
5142 O OD1 . ASP B 220 ? 1.9015 1.5545 2.2023 0.1024  -0.0261 0.0246  220 ASP B OD1 
5143 O OD2 . ASP B 220 ? 1.9018 1.5179 2.1640 0.1124  -0.0508 0.0181  220 ASP B OD2 
5144 N N   . ARG B 221 ? 1.6099 1.3306 1.8980 0.1592  -0.0735 0.0113  221 ARG B N   
5145 C CA  . ARG B 221 ? 1.9636 1.6925 2.2420 0.1644  -0.0817 0.0111  221 ARG B CA  
5146 C C   . ARG B 221 ? 2.1984 1.8842 2.4494 0.1537  -0.0849 0.0090  221 ARG B C   
5147 O O   . ARG B 221 ? 2.6146 2.3035 2.8607 0.1502  -0.0876 0.0111  221 ARG B O   
5148 C CB  . ARG B 221 ? 2.1310 1.8819 2.4032 0.1897  -0.0965 0.0067  221 ARG B CB  
5149 C CG  . ARG B 221 ? 1.8742 1.6663 2.1691 0.2027  -0.0935 0.0085  221 ARG B CG  
5150 C CD  . ARG B 221 ? 1.9483 1.7709 2.2375 0.2285  -0.1060 0.0063  221 ARG B CD  
5151 N NE  . ARG B 221 ? 1.9964 1.8304 2.2850 0.2484  -0.1099 0.0018  221 ARG B NE  
5152 C CZ  . ARG B 221 ? 2.2596 2.1134 2.5368 0.2769  -0.1213 -0.0026 221 ARG B CZ  
5153 N NH1 . ARG B 221 ? 2.3932 2.2663 2.6653 0.2881  -0.1282 -0.0013 221 ARG B NH1 
5154 N NH2 . ARG B 221 ? 2.6587 2.5138 2.9295 0.2950  -0.1257 -0.0079 221 ARG B NH2 
5155 N N   . ASP B 222 ? 2.0347 1.6820 2.2687 0.1477  -0.0851 0.0064  222 ASP B N   
5156 C CA  . ASP B 222 ? 2.2243 1.8297 2.4310 0.1369  -0.0874 0.0055  222 ASP B CA  
5157 C C   . ASP B 222 ? 2.2658 1.8672 2.4757 0.1201  -0.0735 0.0103  222 ASP B C   
5158 O O   . ASP B 222 ? 2.4375 2.0225 2.6288 0.1161  -0.0781 0.0098  222 ASP B O   
5159 C CB  . ASP B 222 ? 2.4193 1.9921 2.6144 0.1306  -0.0879 0.0055  222 ASP B CB  
5160 C CG  . ASP B 222 ? 2.7882 2.3506 2.9701 0.1463  -0.1065 0.0001  222 ASP B CG  
5161 O OD1 . ASP B 222 ? 2.8952 2.4365 3.0506 0.1551  -0.1227 -0.0048 222 ASP B OD1 
5162 O OD2 . ASP B 222 ? 3.0007 2.5734 3.1966 0.1503  -0.1059 0.0007  222 ASP B OD2 
5163 N N   . LYS B 223 ? 2.1925 1.8074 2.4246 0.1116  -0.0578 0.0147  223 LYS B N   
5164 C CA  . LYS B 223 ? 2.3881 1.9960 2.6214 0.0977  -0.0445 0.0187  223 LYS B CA  
5165 C C   . LYS B 223 ? 2.1316 1.7587 2.3688 0.0988  -0.0507 0.0202  223 LYS B C   
5166 O O   . LYS B 223 ? 2.2264 1.8348 2.4504 0.0887  -0.0476 0.0219  223 LYS B O   
5167 C CB  . LYS B 223 ? 2.5314 2.1454 2.7843 0.0894  -0.0268 0.0228  223 LYS B CB  
5168 C CG  . LYS B 223 ? 2.6571 2.2455 2.9019 0.0818  -0.0174 0.0249  223 LYS B CG  
5169 C CD  . LYS B 223 ? 2.8561 2.4075 3.0688 0.0777  -0.0231 0.0239  223 LYS B CD  
5170 C CE  . LYS B 223 ? 3.1233 2.6510 3.3110 0.0715  -0.0208 0.0233  223 LYS B CE  
5171 N NZ  . LYS B 223 ? 3.3001 2.7972 3.4575 0.0709  -0.0325 0.0212  223 LYS B NZ  
5172 N N   . LEU B 224 ? 1.7995 1.4666 2.0578 0.1099  -0.0577 0.0214  224 LEU B N   
5173 C CA  . LEU B 224 ? 1.6677 1.3625 1.9357 0.1106  -0.0650 0.0262  224 LEU B CA  
5174 C C   . LEU B 224 ? 1.7889 1.4646 2.0315 0.1127  -0.0785 0.0240  224 LEU B C   
5175 O O   . LEU B 224 ? 2.0650 1.7357 2.3020 0.1032  -0.0820 0.0283  224 LEU B O   
5176 C CB  . LEU B 224 ? 1.4082 1.1535 1.7039 0.1237  -0.0684 0.0293  224 LEU B CB  
5177 C CG  . LEU B 224 ? 1.5681 1.3531 1.8845 0.1206  -0.0725 0.0388  224 LEU B CG  
5178 C CD1 . LEU B 224 ? 1.8097 1.5815 2.1298 0.1010  -0.0650 0.0444  224 LEU B CD1 
5179 C CD2 . LEU B 224 ? 1.4831 1.3174 1.8271 0.1334  -0.0715 0.0423  224 LEU B CD2 
5180 N N   . ARG B 225 ? 1.7861 1.4491 2.0125 0.1249  -0.0876 0.0177  225 ARG B N   
5181 C CA  . ARG B 225 ? 2.0279 1.6817 2.2342 0.1317  -0.1030 0.0156  225 ARG B CA  
5182 C C   . ARG B 225 ? 2.2556 1.8646 2.4351 0.1159  -0.1014 0.0152  225 ARG B C   
5183 O O   . ARG B 225 ? 2.7052 2.3027 2.8672 0.1170  -0.1135 0.0147  225 ARG B O   
5184 C CB  . ARG B 225 ? 1.9725 1.6186 2.1640 0.1498  -0.1151 0.0082  225 ARG B CB  
5185 C CG  . ARG B 225 ? 1.9862 1.6733 2.1989 0.1685  -0.1169 0.0076  225 ARG B CG  
5186 C CD  . ARG B 225 ? 2.2320 1.9186 2.4272 0.1912  -0.1342 0.0011  225 ARG B CD  
5187 N NE  . ARG B 225 ? 2.4240 2.1386 2.6237 0.1972  -0.1427 0.0056  225 ARG B NE  
5188 C CZ  . ARG B 225 ? 2.6301 2.3963 2.8490 0.2156  -0.1469 0.0092  225 ARG B CZ  
5189 N NH1 . ARG B 225 ? 2.8001 2.5893 3.0295 0.2318  -0.1444 0.0066  225 ARG B NH1 
5190 N NH2 . ARG B 225 ? 2.6057 2.4015 2.8326 0.2184  -0.1542 0.0163  225 ARG B NH2 
5191 N N   . HIS B 226 ? 1.9314 1.5172 2.1078 0.1027  -0.0861 0.0157  226 HIS B N   
5192 C CA  . HIS B 226 ? 2.1151 1.6580 2.2639 0.0893  -0.0814 0.0154  226 HIS B CA  
5193 C C   . HIS B 226 ? 2.2237 1.7698 2.3785 0.0782  -0.0753 0.0204  226 HIS B C   
5194 O O   . HIS B 226 ? 2.6869 2.2083 2.8195 0.0709  -0.0810 0.0211  226 HIS B O   
5195 C CB  . HIS B 226 ? 2.1611 1.6757 2.2984 0.0843  -0.0696 0.0136  226 HIS B CB  
5196 C CG  . HIS B 226 ? 2.5186 1.9916 2.6263 0.0724  -0.0622 0.0142  226 HIS B CG  
5197 N ND1 . HIS B 226 ? 2.7063 2.1690 2.8149 0.0641  -0.0433 0.0169  226 HIS B ND1 
5198 C CD2 . HIS B 226 ? 2.6051 2.0457 2.6809 0.0685  -0.0701 0.0126  226 HIS B CD2 
5199 C CE1 . HIS B 226 ? 2.6509 2.0769 2.7279 0.0567  -0.0391 0.0170  226 HIS B CE1 
5200 N NE2 . HIS B 226 ? 2.7512 2.1621 2.8075 0.0584  -0.0556 0.0143  226 HIS B NE2 
5201 N N   . THR B 227 ? 2.0567 1.6305 2.2394 0.0770  -0.0656 0.0239  227 THR B N   
5202 C CA  . THR B 227 ? 1.9292 1.5039 2.1177 0.0667  -0.0610 0.0288  227 THR B CA  
5203 C C   . THR B 227 ? 1.8830 1.5072 2.1060 0.0697  -0.0664 0.0352  227 THR B C   
5204 O O   . THR B 227 ? 1.9796 1.6319 2.2272 0.0758  -0.0595 0.0356  227 THR B O   
5205 C CB  . THR B 227 ? 1.8671 1.4215 2.0527 0.0608  -0.0420 0.0276  227 THR B CB  
5206 O OG1 . THR B 227 ? 2.3828 1.9690 2.5990 0.0663  -0.0342 0.0286  227 THR B OG1 
5207 C CG2 . THR B 227 ? 1.4798 0.9933 1.6347 0.0588  -0.0348 0.0235  227 THR B CG2 
5208 N N   . GLY B 228 ? 2.0171 1.6516 2.2415 0.0641  -0.0791 0.0417  228 GLY B N   
5209 C CA  . GLY B 228 ? 2.2897 1.9769 2.5456 0.0676  -0.0880 0.0504  228 GLY B CA  
5210 C C   . GLY B 228 ? 2.5971 2.3124 2.8821 0.0645  -0.0786 0.0555  228 GLY B C   
5211 O O   . GLY B 228 ? 3.0156 2.7796 3.3285 0.0697  -0.0836 0.0628  228 GLY B O   
5212 N N   . ASP B 229 ? 2.7392 2.4266 3.0178 0.0574  -0.0651 0.0522  229 ASP B N   
5213 C CA  . ASP B 229 ? 2.6513 2.3592 2.9542 0.0521  -0.0586 0.0577  229 ASP B CA  
5214 C C   . ASP B 229 ? 2.0573 1.7898 2.3827 0.0620  -0.0465 0.0547  229 ASP B C   
5215 O O   . ASP B 229 ? 1.4345 1.1462 1.7496 0.0673  -0.0368 0.0469  229 ASP B O   
5216 C CB  . ASP B 229 ? 2.5996 2.2670 2.8841 0.0404  -0.0533 0.0572  229 ASP B CB  
5217 C CG  . ASP B 229 ? 2.5620 2.1839 2.8187 0.0424  -0.0393 0.0476  229 ASP B CG  
5218 O OD1 . ASP B 229 ? 2.6299 2.2434 2.8751 0.0492  -0.0376 0.0420  229 ASP B OD1 
5219 O OD2 . ASP B 229 ? 2.2614 1.8577 2.5079 0.0376  -0.0305 0.0465  229 ASP B OD2 
5220 N N   . LEU B 230 ? 1.8207 1.5971 2.1768 0.0629  -0.0481 0.0622  230 LEU B N   
5221 C CA  . LEU B 230 ? 1.7680 1.5725 2.1474 0.0721  -0.0394 0.0610  230 LEU B CA  
5222 C C   . LEU B 230 ? 2.0286 1.8043 2.4044 0.0689  -0.0238 0.0553  230 LEU B C   
5223 O O   . LEU B 230 ? 2.2626 2.0393 2.6427 0.0770  -0.0168 0.0503  230 LEU B O   
5224 C CB  . LEU B 230 ? 1.7398 1.5928 2.1505 0.0710  -0.0428 0.0715  230 LEU B CB  
5225 C CG  . LEU B 230 ? 2.0848 1.9883 2.5122 0.0845  -0.0510 0.0762  230 LEU B CG  
5226 C CD1 . LEU B 230 ? 2.0279 1.9275 2.4448 0.1028  -0.0497 0.0658  230 LEU B CD1 
5227 C CD2 . LEU B 230 ? 2.6838 2.6072 3.1116 0.0796  -0.0658 0.0864  230 LEU B CD2 
5228 N N   . VAL B 231 ? 2.1573 1.9092 2.5261 0.0576  -0.0195 0.0572  231 VAL B N   
5229 C CA  . VAL B 231 ? 1.8831 1.6178 2.2547 0.0561  -0.0040 0.0541  231 VAL B CA  
5230 C C   . VAL B 231 ? 1.8451 1.5376 2.1884 0.0567  0.0047  0.0470  231 VAL B C   
5231 O O   . VAL B 231 ? 1.7071 1.3863 2.0513 0.0570  0.0189  0.0450  231 VAL B O   
5232 C CB  . VAL B 231 ? 1.9238 1.6539 2.3006 0.0465  -0.0040 0.0594  231 VAL B CB  
5233 C CG1 . VAL B 231 ? 1.8551 1.5701 2.2360 0.0472  0.0121  0.0564  231 VAL B CG1 
5234 C CG2 . VAL B 231 ? 2.0824 1.8565 2.4870 0.0435  -0.0144 0.0690  231 VAL B CG2 
5235 N N   . GLY B 232 ? 2.0727 1.7485 2.3929 0.0573  -0.0039 0.0444  232 GLY B N   
5236 C CA  . GLY B 232 ? 2.2656 1.9035 2.5572 0.0577  0.0024  0.0389  232 GLY B CA  
5237 C C   . GLY B 232 ? 2.3465 1.9911 2.6429 0.0650  0.0048  0.0359  232 GLY B C   
5238 O O   . GLY B 232 ? 2.3589 1.9791 2.6409 0.0641  0.0141  0.0338  232 GLY B O   
5239 N N   . SER B 233 ? 2.3796 2.0582 2.6960 0.0725  -0.0040 0.0367  233 SER B N   
5240 C CA  . SER B 233 ? 2.2906 1.9738 2.6086 0.0812  -0.0069 0.0335  233 SER B CA  
5241 C C   . SER B 233 ? 2.1282 1.8391 2.4748 0.0856  -0.0016 0.0352  233 SER B C   
5242 O O   . SER B 233 ? 1.8863 1.6055 2.2362 0.0946  -0.0075 0.0329  233 SER B O   
5243 C CB  . SER B 233 ? 2.4309 2.1248 2.7408 0.0901  -0.0233 0.0314  233 SER B CB  
5244 O OG  . SER B 233 ? 3.0269 2.7568 3.3548 0.0924  -0.0303 0.0363  233 SER B OG  
5245 N N   . ALA B 234 ? 1.8954 1.6170 2.2600 0.0797  0.0080  0.0391  234 ALA B N   
5246 C CA  . ALA B 234 ? 1.6903 1.4380 2.0825 0.0829  0.0128  0.0414  234 ALA B CA  
5247 C C   . ALA B 234 ? 1.6727 1.4038 2.0655 0.0816  0.0222  0.0407  234 ALA B C   
5248 O O   . ALA B 234 ? 1.6623 1.3713 2.0472 0.0747  0.0339  0.0419  234 ALA B O   
5249 C CB  . ALA B 234 ? 1.3831 1.1466 1.7932 0.0768  0.0178  0.0464  234 ALA B CB  
5250 N N   . GLU B 235 ? 1.7136 1.4555 2.1141 0.0891  0.0159  0.0395  235 GLU B N   
5251 C CA  . GLU B 235 ? 1.7408 1.4713 2.1458 0.0868  0.0208  0.0412  235 GLU B CA  
5252 C C   . GLU B 235 ? 1.5641 1.3155 1.9981 0.0846  0.0301  0.0455  235 GLU B C   
5253 O O   . GLU B 235 ? 1.3355 1.0793 1.7779 0.0789  0.0396  0.0495  235 GLU B O   
5254 C CB  . GLU B 235 ? 1.7648 1.4910 2.1620 0.0952  0.0066  0.0382  235 GLU B CB  
5255 C CG  . GLU B 235 ? 2.3467 2.0420 2.7138 0.0949  -0.0019 0.0353  235 GLU B CG  
5256 C CD  . GLU B 235 ? 2.4666 2.1479 2.8227 0.1011  -0.0169 0.0333  235 GLU B CD  
5257 O OE1 . GLU B 235 ? 2.1119 1.8072 2.4842 0.1056  -0.0199 0.0343  235 GLU B OE1 
5258 O OE2 . GLU B 235 ? 2.4707 2.1248 2.8009 0.1012  -0.0269 0.0310  235 GLU B OE2 
5259 N N   . VAL B 236 ? 1.6450 1.4250 2.0951 0.0892  0.0268  0.0458  236 VAL B N   
5260 C CA  . VAL B 236 ? 1.6540 1.4533 2.1306 0.0864  0.0350  0.0500  236 VAL B CA  
5261 C C   . VAL B 236 ? 2.1141 1.9344 2.5991 0.0853  0.0336  0.0521  236 VAL B C   
5262 O O   . VAL B 236 ? 2.4142 2.2597 2.9040 0.0923  0.0238  0.0524  236 VAL B O   
5263 C CB  . VAL B 236 ? 1.3563 1.1715 1.8478 0.0932  0.0292  0.0505  236 VAL B CB  
5264 C CG1 . VAL B 236 ? 1.3666 1.2037 1.8860 0.0906  0.0362  0.0550  236 VAL B CG1 
5265 C CG2 . VAL B 236 ? 1.1491 0.9407 1.6314 0.0917  0.0270  0.0504  236 VAL B CG2 
5266 N N   . ILE B 237 ? 2.1674 1.9773 2.6532 0.0771  0.0426  0.0544  237 ILE B N   
5267 C CA  . ILE B 237 ? 1.9560 1.7826 2.4519 0.0731  0.0400  0.0583  237 ILE B CA  
5268 C C   . ILE B 237 ? 1.8356 1.6627 2.3491 0.0688  0.0504  0.0614  237 ILE B C   
5269 O O   . ILE B 237 ? 1.6113 1.4150 2.1181 0.0667  0.0616  0.0602  237 ILE B O   
5270 C CB  . ILE B 237 ? 1.8325 1.6413 2.3068 0.0678  0.0352  0.0581  237 ILE B CB  
5271 C CG1 . ILE B 237 ? 1.6968 1.5241 2.1823 0.0616  0.0282  0.0646  237 ILE B CG1 
5272 C CG2 . ILE B 237 ? 1.4936 1.2632 1.9466 0.0640  0.0456  0.0548  237 ILE B CG2 
5273 C CD1 . ILE B 237 ? 1.6620 1.4775 2.1287 0.0554  0.0179  0.0666  237 ILE B CD1 
5274 N N   . ARG B 238 ? 1.8867 1.7419 2.4224 0.0684  0.0469  0.0660  238 ARG B N   
5275 C CA  . ARG B 238 ? 1.8195 1.6765 2.3730 0.0651  0.0551  0.0689  238 ARG B CA  
5276 C C   . ARG B 238 ? 1.6473 1.5056 2.2020 0.0578  0.0504  0.0734  238 ARG B C   
5277 O O   . ARG B 238 ? 1.4164 1.2746 1.9835 0.0548  0.0544  0.0761  238 ARG B O   
5278 C CB  . ARG B 238 ? 2.0355 1.9173 2.6119 0.0699  0.0548  0.0706  238 ARG B CB  
5279 C CG  . ARG B 238 ? 2.4530 2.3274 3.0202 0.0762  0.0535  0.0664  238 ARG B CG  
5280 C CD  . ARG B 238 ? 2.4076 2.2740 2.9856 0.0762  0.0611  0.0672  238 ARG B CD  
5281 N NE  . ARG B 238 ? 2.4817 2.3705 3.0841 0.0777  0.0598  0.0706  238 ARG B NE  
5282 C CZ  . ARG B 238 ? 2.6078 2.5169 3.2158 0.0844  0.0498  0.0703  238 ARG B CZ  
5283 N NH1 . ARG B 238 ? 2.5479 2.4589 3.1391 0.0921  0.0400  0.0664  238 ARG B NH1 
5284 N NH2 . ARG B 238 ? 2.6993 2.6261 3.3281 0.0848  0.0497  0.0739  238 ARG B NH2 
5285 N N   . LEU B 239 ? 1.7985 1.6565 2.3391 0.0543  0.0401  0.0749  239 LEU B N   
5286 C CA  . LEU B 239 ? 1.7527 1.6061 2.2897 0.0450  0.0319  0.0804  239 LEU B CA  
5287 C C   . LEU B 239 ? 1.8861 1.6955 2.3934 0.0420  0.0339  0.0759  239 LEU B C   
5288 O O   . LEU B 239 ? 1.7997 1.5914 2.2871 0.0453  0.0360  0.0707  239 LEU B O   
5289 C CB  . LEU B 239 ? 1.8085 1.6940 2.3515 0.0418  0.0174  0.0878  239 LEU B CB  
5290 C CG  . LEU B 239 ? 1.8397 1.7682 2.4112 0.0418  0.0138  0.0959  239 LEU B CG  
5291 C CD1 . LEU B 239 ? 1.8421 1.8082 2.4202 0.0403  0.0011  0.1051  239 LEU B CD1 
5292 C CD2 . LEU B 239 ? 1.6799 1.5972 2.2587 0.0325  0.0137  0.1004  239 LEU B CD2 
5293 N N   . PRO B 240 ? 2.0212 1.8093 2.5219 0.0364  0.0322  0.0778  240 PRO B N   
5294 C CA  . PRO B 240 ? 2.2938 2.0398 2.7614 0.0332  0.0282  0.0748  240 PRO B CA  
5295 C C   . PRO B 240 ? 2.4016 2.1552 2.8595 0.0269  0.0129  0.0787  240 PRO B C   
5296 O O   . PRO B 240 ? 2.2436 2.0310 2.7200 0.0206  0.0008  0.0877  240 PRO B O   
5297 C CB  . PRO B 240 ? 2.2165 1.9478 2.6836 0.0274  0.0220  0.0788  240 PRO B CB  
5298 C CG  . PRO B 240 ? 1.9923 1.7492 2.4900 0.0316  0.0318  0.0801  240 PRO B CG  
5299 C CD  . PRO B 240 ? 1.8100 1.6099 2.3315 0.0338  0.0326  0.0824  240 PRO B CD  
5300 N N   . ALA B 241 ? 2.1714 1.8960 2.6010 0.0292  0.0139  0.0728  241 ALA B N   
5301 C CA  . ALA B 241 ? 2.1952 1.9284 2.6165 0.0258  0.0014  0.0753  241 ALA B CA  
5302 C C   . ALA B 241 ? 2.2854 2.0316 2.7122 0.0131  -0.0183 0.0867  241 ALA B C   
5303 O O   . ALA B 241 ? 2.6141 2.3981 3.0569 0.0105  -0.0284 0.0944  241 ALA B O   
5304 C CB  . ALA B 241 ? 2.2812 1.9714 2.6663 0.0281  0.0040  0.0678  241 ALA B CB  
5305 N N   . GLU B 242 ? 2.1688 1.8815 2.5797 0.0059  -0.0242 0.0881  242 GLU B N   
5306 C CA  . GLU B 242 ? 2.3340 2.0483 2.7446 -0.0090 -0.0458 0.1001  242 GLU B CA  
5307 C C   . GLU B 242 ? 2.2396 2.0101 2.6895 -0.0143 -0.0511 0.1125  242 GLU B C   
5308 O O   . GLU B 242 ? 2.2957 2.0978 2.7578 -0.0239 -0.0667 0.1253  242 GLU B O   
5309 C CB  . GLU B 242 ? 2.3127 1.9798 2.7011 -0.0132 -0.0504 0.0984  242 GLU B CB  
5310 C CG  . GLU B 242 ? 2.7138 2.3900 3.1123 -0.0299 -0.0723 0.1131  242 GLU B CG  
5311 C CD  . GLU B 242 ? 3.0450 2.7282 3.4390 -0.0463 -0.0973 0.1267  242 GLU B CD  
5312 O OE1 . GLU B 242 ? 3.4544 3.1261 3.8304 -0.0452 -0.1004 0.1237  242 GLU B OE1 
5313 O OE2 . GLU B 242 ? 2.7288 2.4319 3.1392 -0.0613 -0.1147 0.1420  242 GLU B OE2 
5314 N N   . GLU B 243 ? 1.9355 1.7186 2.4045 -0.0075 -0.0374 0.1091  243 GLU B N   
5315 C CA  . GLU B 243 ? 2.0996 1.9328 2.6037 -0.0109 -0.0402 0.1198  243 GLU B CA  
5316 C C   . GLU B 243 ? 2.0619 1.9448 2.5844 -0.0052 -0.0402 0.1238  243 GLU B C   
5317 O O   . GLU B 243 ? 1.9933 1.9190 2.5359 -0.0122 -0.0514 0.1378  243 GLU B O   
5318 C CB  . GLU B 243 ? 2.1568 1.9906 2.6759 -0.0050 -0.0270 0.1154  243 GLU B CB  
5319 C CG  . GLU B 243 ? 2.4243 2.3057 2.9759 -0.0110 -0.0330 0.1281  243 GLU B CG  
5320 C CD  . GLU B 243 ? 2.7033 2.5882 3.2715 -0.0048 -0.0206 0.1240  243 GLU B CD  
5321 O OE1 . GLU B 243 ? 2.8443 2.6938 3.3992 0.0032  -0.0081 0.1126  243 GLU B OE1 
5322 O OE2 . GLU B 243 ? 2.9862 2.9100 3.5802 -0.0081 -0.0238 0.1334  243 GLU B OE2 
5323 N N   . PHE B 244 ? 2.1250 2.0007 2.6385 0.0079  -0.0282 0.1121  244 PHE B N   
5324 C CA  . PHE B 244 ? 2.1299 2.0441 2.6542 0.0175  -0.0280 0.1127  244 PHE B CA  
5325 C C   . PHE B 244 ? 2.0405 1.9720 2.5615 0.0099  -0.0448 0.1232  244 PHE B C   
5326 O O   . PHE B 244 ? 1.9868 1.9691 2.5284 0.0125  -0.0505 0.1332  244 PHE B O   
5327 C CB  . PHE B 244 ? 1.9253 1.8173 2.4340 0.0307  -0.0158 0.0985  244 PHE B CB  
5328 C CG  . PHE B 244 ? 1.5982 1.5171 2.1084 0.0419  -0.0185 0.0970  244 PHE B CG  
5329 C CD1 . PHE B 244 ? 1.4500 1.4181 1.9832 0.0504  -0.0198 0.1023  244 PHE B CD1 
5330 C CD2 . PHE B 244 ? 1.4684 1.3616 1.9542 0.0455  -0.0201 0.0900  244 PHE B CD2 
5331 C CE1 . PHE B 244 ? 1.4181 1.4071 1.9483 0.0642  -0.0227 0.0995  244 PHE B CE1 
5332 C CE2 . PHE B 244 ? 1.5777 1.4916 2.0623 0.0576  -0.0236 0.0876  244 PHE B CE2 
5333 C CZ  . PHE B 244 ? 1.5403 1.5021 2.0466 0.0677  -0.0253 0.0922  244 PHE B CZ  
5334 N N   . ARG B 245 ? 2.0119 1.9010 2.5062 0.0015  -0.0523 0.1214  245 ARG B N   
5335 C CA  . ARG B 245 ? 1.8417 1.7387 2.3295 -0.0078 -0.0702 0.1316  245 ARG B CA  
5336 C C   . ARG B 245 ? 1.7107 1.6479 2.2231 -0.0220 -0.0850 0.1514  245 ARG B C   
5337 O O   . ARG B 245 ? 1.5668 1.5504 2.0956 -0.0236 -0.0949 0.1642  245 ARG B O   
5338 C CB  . ARG B 245 ? 1.9342 1.7720 2.3851 -0.0146 -0.0768 0.1257  245 ARG B CB  
5339 C CG  . ARG B 245 ? 2.0378 1.8476 2.4656 -0.0018 -0.0656 0.1105  245 ARG B CG  
5340 C CD  . ARG B 245 ? 2.1422 1.8990 2.5324 -0.0084 -0.0743 0.1066  245 ARG B CD  
5341 N NE  . ARG B 245 ? 2.0682 1.8001 2.4354 0.0020  -0.0654 0.0941  245 ARG B NE  
5342 C CZ  . ARG B 245 ? 2.0971 1.7956 2.4469 0.0107  -0.0485 0.0814  245 ARG B CZ  
5343 N NH1 . ARG B 245 ? 1.8876 1.5726 2.2402 0.0118  -0.0371 0.0782  245 ARG B NH1 
5344 N NH2 . ARG B 245 ? 2.3514 2.0316 2.6815 0.0179  -0.0434 0.0731  245 ARG B NH2 
5345 N N   . ARG B 246 ? 1.6436 1.5629 2.1580 -0.0316 -0.0865 0.1542  246 ARG B N   
5346 C CA  . ARG B 246 ? 1.7267 1.6771 2.2623 -0.0478 -0.1016 0.1737  246 ARG B CA  
5347 C C   . ARG B 246 ? 1.8943 1.9161 2.4655 -0.0404 -0.0962 0.1833  246 ARG B C   
5348 O O   . ARG B 246 ? 2.2814 2.3503 2.8719 -0.0496 -0.1094 0.2025  246 ARG B O   
5349 C CB  . ARG B 246 ? 1.7896 1.6977 2.3146 -0.0584 -0.1057 0.1731  246 ARG B CB  
5350 C CG  . ARG B 246 ? 2.4007 2.3452 2.9551 -0.0639 -0.1060 0.1842  246 ARG B CG  
5351 C CD  . ARG B 246 ? 2.7624 2.6688 3.3066 -0.0790 -0.1188 0.1894  246 ARG B CD  
5352 N NE  . ARG B 246 ? 2.8467 2.7059 3.3740 -0.0670 -0.1031 0.1708  246 ARG B NE  
5353 C CZ  . ARG B 246 ? 2.6663 2.4621 3.1578 -0.0654 -0.1046 0.1595  246 ARG B CZ  
5354 N NH1 . ARG B 246 ? 2.5934 2.3586 3.0597 -0.0770 -0.1237 0.1647  246 ARG B NH1 
5355 N NH2 . ARG B 246 ? 2.7860 2.5502 3.2665 -0.0514 -0.0870 0.1438  246 ARG B NH2 
5356 N N   . GLU B 247 ? 1.7719 1.8004 2.3501 -0.0232 -0.0773 0.1704  247 GLU B N   
5357 C CA  . GLU B 247 ? 1.5824 1.6709 2.1882 -0.0119 -0.0704 0.1757  247 GLU B CA  
5358 C C   . GLU B 247 ? 1.7509 1.8810 2.3617 -0.0032 -0.0751 0.1817  247 GLU B C   
5359 O O   . GLU B 247 ? 1.6888 1.8784 2.3232 -0.0029 -0.0800 0.1977  247 GLU B O   
5360 C CB  . GLU B 247 ? 1.5154 1.5983 2.1258 0.0032  -0.0523 0.1616  247 GLU B CB  
5361 C CG  . GLU B 247 ? 1.7874 1.9296 2.4231 0.0145  -0.0477 0.1682  247 GLU B CG  
5362 C CD  . GLU B 247 ? 1.8793 2.0598 2.5396 0.0029  -0.0538 0.1858  247 GLU B CD  
5363 O OE1 . GLU B 247 ? 1.8749 2.0337 2.5342 -0.0162 -0.0635 0.1938  247 GLU B OE1 
5364 O OE2 . GLU B 247 ? 1.9196 2.1496 2.5980 0.0139  -0.0494 0.1913  247 GLU B OE2 
5365 N N   . LEU B 248 ? 2.0040 2.1028 2.5918 0.0044  -0.0733 0.1693  248 LEU B N   
5366 C CA  . LEU B 248 ? 2.1780 2.3071 2.7655 0.0148  -0.0780 0.1720  248 LEU B CA  
5367 C C   . LEU B 248 ? 2.3050 2.4695 2.9060 -0.0012 -0.0964 0.1946  248 LEU B C   
5368 O O   . LEU B 248 ? 2.5497 2.7745 3.1703 0.0062  -0.0997 0.2071  248 LEU B O   
5369 C CB  . LEU B 248 ? 1.8615 1.9399 2.4184 0.0220  -0.0746 0.1549  248 LEU B CB  
5370 C CG  . LEU B 248 ? 1.7845 1.8816 2.3364 0.0434  -0.0709 0.1469  248 LEU B CG  
5371 C CD1 . LEU B 248 ? 1.4973 1.6386 2.0678 0.0617  -0.0619 0.1459  248 LEU B CD1 
5372 C CD2 . LEU B 248 ? 1.6229 1.6621 2.1450 0.0499  -0.0633 0.1276  248 LEU B CD2 
5373 N N   . ALA B 249 ? 2.0480 2.1733 2.6369 -0.0229 -0.1089 0.2002  249 ALA B N   
5374 C CA  . ALA B 249 ? 1.8533 2.0006 2.4514 -0.0433 -0.1303 0.2228  249 ALA B CA  
5375 C C   . ALA B 249 ? 1.8813 2.0966 2.5153 -0.0492 -0.1337 0.2444  249 ALA B C   
5376 O O   . ALA B 249 ? 2.4276 2.7004 3.0821 -0.0528 -0.1440 0.2646  249 ALA B O   
5377 C CB  . ALA B 249 ? 1.4726 1.5567 2.0469 -0.0646 -0.1440 0.2231  249 ALA B CB  
5378 N N   . GLU B 250 ? 1.7272 1.9369 2.3686 -0.0496 -0.1247 0.2408  250 GLU B N   
5379 C CA  . GLU B 250 ? 1.7404 1.9964 2.4098 -0.0637 -0.1325 0.2631  250 GLU B CA  
5380 C C   . GLU B 250 ? 1.7644 2.0867 2.4591 -0.0444 -0.1182 0.2662  250 GLU B C   
5381 O O   . GLU B 250 ? 1.8090 2.1947 2.5298 -0.0506 -0.1251 0.2892  250 GLU B O   
5382 C CB  . GLU B 250 ? 1.9385 2.1462 2.5992 -0.0800 -0.1368 0.2611  250 GLU B CB  
5383 C CG  . GLU B 250 ? 2.3009 2.4532 2.9378 -0.1020 -0.1576 0.2656  250 GLU B CG  
5384 C CD  . GLU B 250 ? 2.5987 2.6845 3.2144 -0.1088 -0.1577 0.2539  250 GLU B CD  
5385 O OE1 . GLU B 250 ? 2.5647 2.6625 3.1956 -0.1116 -0.1541 0.2578  250 GLU B OE1 
5386 O OE2 . GLU B 250 ? 2.6453 2.6667 3.2278 -0.1097 -0.1611 0.2405  250 GLU B OE2 
5387 N N   . GLN B 251 ? 1.6788 1.9852 2.3640 -0.0212 -0.0994 0.2439  251 GLN B N   
5388 C CA  . GLN B 251 ? 1.6051 1.9639 2.3071 0.0000  -0.0864 0.2434  251 GLN B CA  
5389 C C   . GLN B 251 ? 1.9033 2.2688 2.5932 0.0256  -0.0787 0.2296  251 GLN B C   
5390 O O   . GLN B 251 ? 2.5726 2.9956 3.2754 0.0434  -0.0751 0.2362  251 GLN B O   
5391 C CB  . GLN B 251 ? 1.5402 1.8732 2.2401 0.0070  -0.0728 0.2287  251 GLN B CB  
5392 C CG  . GLN B 251 ? 1.7247 2.0735 2.4434 -0.0105 -0.0776 0.2441  251 GLN B CG  
5393 C CD  . GLN B 251 ? 1.9461 2.3737 2.6916 -0.0052 -0.0776 0.2637  251 GLN B CD  
5394 O OE1 . GLN B 251 ? 1.6459 2.1162 2.3948 0.0161  -0.0714 0.2633  251 GLN B OE1 
5395 N NE2 . GLN B 251 ? 2.4292 2.8767 3.1923 -0.0232 -0.0844 0.2812  251 GLN B NE2 
5396 N N   . GLY B 252 ? 1.9176 2.2228 2.5809 0.0282  -0.0765 0.2107  252 GLY B N   
5397 C CA  . GLY B 252 ? 2.0354 2.3340 2.6823 0.0506  -0.0710 0.1959  252 GLY B CA  
5398 C C   . GLY B 252 ? 1.8627 2.1522 2.5023 0.0737  -0.0563 0.1776  252 GLY B C   
5399 O O   . GLY B 252 ? 1.6489 1.9334 2.2959 0.0732  -0.0485 0.1744  252 GLY B O   
5400 N N   . ALA B 253 ? 1.6185 1.9033 2.2420 0.0940  -0.0546 0.1659  253 ALA B N   
5401 C CA  . ALA B 253 ? 1.7540 2.0208 2.3640 0.1157  -0.0450 0.1478  253 ALA B CA  
5402 C C   . ALA B 253 ? 1.7656 2.0748 2.3731 0.1422  -0.0472 0.1481  253 ALA B C   
5403 O O   . ALA B 253 ? 1.8720 2.2292 2.4915 0.1443  -0.0539 0.1627  253 ALA B O   
5404 C CB  . ALA B 253 ? 1.6049 1.8033 2.1891 0.1123  -0.0420 0.1302  253 ALA B CB  
5405 N N   . ILE B 254 ? 1.5781 1.8680 2.1689 0.1634  -0.0421 0.1317  254 ILE B N   
5406 C CA  . ILE B 254 ? 1.4168 1.7316 1.9960 0.1936  -0.0444 0.1263  254 ILE B CA  
5407 C C   . ILE B 254 ? 1.4306 1.6840 1.9799 0.2025  -0.0445 0.1054  254 ILE B C   
5408 O O   . ILE B 254 ? 1.6519 1.8618 2.1953 0.1935  -0.0392 0.0961  254 ILE B O   
5409 C CB  . ILE B 254 ? 1.3161 1.6791 1.9064 0.2129  -0.0396 0.1309  254 ILE B CB  
5410 C CG1 . ILE B 254 ? 1.2458 1.5755 1.8165 0.2311  -0.0360 0.1131  254 ILE B CG1 
5411 C CG2 . ILE B 254 ? 1.2144 1.6157 1.8347 0.1942  -0.0362 0.1490  254 ILE B CG2 
5412 C CD1 . ILE B 254 ? 1.2723 1.6487 1.8478 0.2544  -0.0330 0.1168  254 ILE B CD1 
5413 N N   . VAL B 255 ? 1.4202 1.6735 1.9501 0.2235  -0.0512 0.0985  255 VAL B N   
5414 C CA  . VAL B 255 ? 1.2579 1.4517 1.7576 0.2300  -0.0544 0.0806  255 VAL B CA  
5415 C C   . VAL B 255 ? 1.2764 1.4683 1.7562 0.2608  -0.0578 0.0689  255 VAL B C   
5416 O O   . VAL B 255 ? 1.5415 1.7741 2.0184 0.2860  -0.0620 0.0712  255 VAL B O   
5417 C CB  . VAL B 255 ? 1.2449 1.4099 1.7300 0.2210  -0.0611 0.0784  255 VAL B CB  
5418 C CG1 . VAL B 255 ? 1.1531 1.2558 1.6078 0.2248  -0.0639 0.0616  255 VAL B CG1 
5419 C CG2 . VAL B 255 ? 1.1407 1.2961 1.6403 0.1901  -0.0583 0.0881  255 VAL B CG2 
5420 N N   . GLU B 256 ? 1.2659 1.4104 1.7326 0.2582  -0.0562 0.0573  256 GLU B N   
5421 C CA  . GLU B 256 ? 1.4082 1.5335 1.8505 0.2831  -0.0626 0.0448  256 GLU B CA  
5422 C C   . GLU B 256 ? 1.4483 1.5063 1.8643 0.2770  -0.0688 0.0321  256 GLU B C   
5423 O O   . GLU B 256 ? 1.3684 1.3919 1.7891 0.2521  -0.0633 0.0321  256 GLU B O   
5424 C CB  . GLU B 256 ? 1.4311 1.5649 1.8805 0.2890  -0.0584 0.0442  256 GLU B CB  
5425 C CG  . GLU B 256 ? 1.7890 1.9903 2.2602 0.2994  -0.0532 0.0566  256 GLU B CG  
5426 C CD  . GLU B 256 ? 2.3906 2.5996 2.8656 0.3071  -0.0498 0.0556  256 GLU B CD  
5427 O OE1 . GLU B 256 ? 2.6994 2.8834 3.1860 0.2863  -0.0445 0.0557  256 GLU B OE1 
5428 O OE2 . GLU B 256 ? 2.6025 2.8433 3.0672 0.3360  -0.0528 0.0548  256 GLU B OE2 
5429 N N   . GLU B 257 ? 1.5693 1.6085 1.9554 0.3021  -0.0809 0.0212  257 GLU B N   
5430 C CA  . GLU B 257 ? 1.7491 1.7257 2.1057 0.3011  -0.0909 0.0096  257 GLU B CA  
5431 C C   . GLU B 257 ? 1.6215 1.5682 1.9805 0.2899  -0.0886 0.0072  257 GLU B C   
5432 O O   . GLU B 257 ? 1.5458 1.5092 1.9086 0.3021  -0.0886 0.0070  257 GLU B O   
5433 C CB  . GLU B 257 ? 2.2636 2.2284 2.5853 0.3333  -0.1074 -0.0008 257 GLU B CB  
5434 C CG  . GLU B 257 ? 2.3559 2.3485 2.6705 0.3635  -0.1112 -0.0037 257 GLU B CG  
5435 C CD  . GLU B 257 ? 2.2177 2.1779 2.4890 0.3953  -0.1303 -0.0173 257 GLU B CD  
5436 O OE1 . GLU B 257 ? 2.1300 2.0356 2.3766 0.3891  -0.1421 -0.0249 257 GLU B OE1 
5437 O OE2 . GLU B 257 ? 2.3121 2.3009 2.5727 0.4265  -0.1340 -0.0200 257 GLU B OE2 
5438 N N   . PHE B 258 ? 1.6506 1.5518 2.0051 0.2677  -0.0877 0.0057  258 PHE B N   
5439 C CA  . PHE B 258 ? 1.8259 1.6960 2.1837 0.2540  -0.0862 0.0053  258 PHE B CA  
5440 C C   . PHE B 258 ? 1.9773 1.8056 2.3018 0.2695  -0.1049 -0.0041 258 PHE B C   
5441 O O   . PHE B 258 ? 2.1489 1.9337 2.4525 0.2623  -0.1137 -0.0076 258 PHE B O   
5442 C CB  . PHE B 258 ? 1.8977 1.7461 2.2685 0.2242  -0.0749 0.0105  258 PHE B CB  
5443 C CG  . PHE B 258 ? 2.0152 1.8367 2.3926 0.2100  -0.0727 0.0121  258 PHE B CG  
5444 C CD1 . PHE B 258 ? 1.8009 1.6461 2.2051 0.2040  -0.0628 0.0176  258 PHE B CD1 
5445 C CD2 . PHE B 258 ? 2.3464 2.1208 2.7038 0.2026  -0.0817 0.0096  258 PHE B CD2 
5446 C CE1 . PHE B 258 ? 2.0254 1.8486 2.4374 0.1917  -0.0616 0.0202  258 PHE B CE1 
5447 C CE2 . PHE B 258 ? 2.2500 2.0045 2.6165 0.1887  -0.0803 0.0137  258 PHE B CE2 
5448 C CZ  . PHE B 258 ? 2.1883 1.9678 2.5827 0.1837  -0.0701 0.0188  258 PHE B CZ  
5449 N N   . LEU B 259 ? 1.9310 1.7710 2.2493 0.2899  -0.1117 -0.0075 259 LEU B N   
5450 C CA  . LEU B 259 ? 1.9284 1.7268 2.2137 0.3055  -0.1316 -0.0162 259 LEU B CA  
5451 C C   . LEU B 259 ? 2.1568 1.9095 2.4436 0.2796  -0.1346 -0.0131 259 LEU B C   
5452 O O   . LEU B 259 ? 2.3436 2.1078 2.6599 0.2598  -0.1214 -0.0053 259 LEU B O   
5453 C CB  . LEU B 259 ? 1.7113 1.5354 1.9968 0.3268  -0.1336 -0.0178 259 LEU B CB  
5454 C CG  . LEU B 259 ? 1.7518 1.6402 2.0537 0.3437  -0.1219 -0.0140 259 LEU B CG  
5455 C CD1 . LEU B 259 ? 1.6581 1.5755 1.9668 0.3581  -0.1194 -0.0125 259 LEU B CD1 
5456 C CD2 . LEU B 259 ? 1.8271 1.7256 2.1034 0.3719  -0.1312 -0.0203 259 LEU B CD2 
5457 N N   . GLU B 260 ? 2.2244 1.9267 2.4797 0.2799  -0.1525 -0.0182 260 GLU B N   
5458 C CA  . GLU B 260 ? 2.3162 1.9805 2.5753 0.2517  -0.1535 -0.0120 260 GLU B CA  
5459 C C   . GLU B 260 ? 2.2866 1.9262 2.5428 0.2481  -0.1653 -0.0100 260 GLU B C   
5460 O O   . GLU B 260 ? 2.2570 1.9000 2.5410 0.2249  -0.1544 -0.0005 260 GLU B O   
5461 C CB  . GLU B 260 ? 2.7888 2.4105 3.0165 0.2502  -0.1682 -0.0158 260 GLU B CB  
5462 C CG  . GLU B 260 ? 3.1039 2.7446 3.3394 0.2442  -0.1546 -0.0147 260 GLU B CG  
5463 C CD  . GLU B 260 ? 3.1979 2.8501 3.4645 0.2145  -0.1326 -0.0044 260 GLU B CD  
5464 O OE1 . GLU B 260 ? 3.2893 2.9328 3.5727 0.1958  -0.1268 0.0030  260 GLU B OE1 
5465 O OE2 . GLU B 260 ? 3.2618 2.9320 3.5346 0.2115  -0.1218 -0.0038 260 GLU B OE2 
5466 N N   . GLU B 261 ? 2.2714 1.8850 2.4922 0.2723  -0.1887 -0.0190 261 GLU B N   
5467 C CA  . GLU B 261 ? 2.7055 2.2875 2.9159 0.2707  -0.2056 -0.0179 261 GLU B CA  
5468 C C   . GLU B 261 ? 2.6204 2.2375 2.8429 0.2873  -0.1994 -0.0198 261 GLU B C   
5469 O O   . GLU B 261 ? 2.2541 1.8738 2.4491 0.3187  -0.2107 -0.0298 261 GLU B O   
5470 C CB  . GLU B 261 ? 2.9554 2.4781 3.1156 0.2843  -0.2380 -0.0259 261 GLU B CB  
5471 C CG  . GLU B 261 ? 3.1763 2.6595 3.3286 0.2597  -0.2456 -0.0197 261 GLU B CG  
5472 C CD  . GLU B 261 ? 3.4514 2.9215 3.6295 0.2246  -0.2420 -0.0045 261 GLU B CD  
5473 O OE1 . GLU B 261 ? 3.4025 2.8439 3.5711 0.2217  -0.2608 -0.0015 261 GLU B OE1 
5474 O OE2 . GLU B 261 ? 3.5633 3.0522 3.7703 0.2009  -0.2209 0.0047  261 GLU B OE2 
5475 N N   . ILE B 262 ? 2.6058 2.2497 2.8684 0.2667  -0.1815 -0.0099 262 ILE B N   
5476 C CA  . ILE B 262 ? 2.3865 2.0584 2.6633 0.2761  -0.1765 -0.0093 262 ILE B CA  
5477 C C   . ILE B 262 ? 2.4251 2.0617 2.7020 0.2617  -0.1907 -0.0038 262 ILE B C   
5478 O O   . ILE B 262 ? 2.5161 2.1418 2.8157 0.2329  -0.1853 0.0065  262 ILE B O   
5479 C CB  . ILE B 262 ? 2.0820 1.8116 2.4031 0.2652  -0.1475 -0.0020 262 ILE B CB  
5480 C CG1 . ILE B 262 ? 1.9243 1.6881 2.2458 0.2769  -0.1363 -0.0051 262 ILE B CG1 
5481 C CG2 . ILE B 262 ? 2.0140 1.7716 2.3490 0.2739  -0.1434 -0.0004 262 ILE B CG2 
5482 C CD1 . ILE B 262 ? 1.8513 1.6602 2.2139 0.2593  -0.1110 0.0037  262 ILE B CD1 
5483 N N   . THR B 263 ? 2.4341 2.0533 2.6843 0.2829  -0.2095 -0.0103 263 THR B N   
5484 C CA  . THR B 263 ? 2.3279 1.9097 2.5729 0.2719  -0.2280 -0.0055 263 THR B CA  
5485 C C   . THR B 263 ? 2.4202 2.0368 2.6956 0.2691  -0.2150 -0.0004 263 THR B C   
5486 O O   . THR B 263 ? 2.7061 2.3179 3.0088 0.2440  -0.2127 0.0106  263 THR B O   
5487 C CB  . THR B 263 ? 2.4526 1.9805 2.6412 0.2963  -0.2621 -0.0164 263 THR B CB  
5488 O OG1 . THR B 263 ? 2.6151 2.1709 2.7856 0.3319  -0.2589 -0.0276 263 THR B OG1 
5489 C CG2 . THR B 263 ? 2.2804 1.7670 2.4388 0.2951  -0.2780 -0.0200 263 THR B CG2 
5490 N N   . ASP B 264 ? 2.4616 2.1147 2.7323 0.2951  -0.2068 -0.0074 264 ASP B N   
5491 C CA  . ASP B 264 ? 2.6219 2.3140 2.9207 0.2944  -0.1927 -0.0026 264 ASP B CA  
5492 C C   . ASP B 264 ? 2.3723 2.1268 2.6945 0.3025  -0.1670 -0.0020 264 ASP B C   
5493 O O   . ASP B 264 ? 2.1749 1.9435 2.4831 0.3181  -0.1638 -0.0077 264 ASP B O   
5494 C CB  . ASP B 264 ? 2.9466 2.6150 3.2143 0.3154  -0.2137 -0.0085 264 ASP B CB  
5495 C CG  . ASP B 264 ? 3.2298 2.8410 3.4854 0.2992  -0.2385 -0.0044 264 ASP B CG  
5496 O OD1 . ASP B 264 ? 3.4863 3.1047 3.7798 0.2710  -0.2304 0.0077  264 ASP B OD1 
5497 O OD2 . ASP B 264 ? 2.9753 2.5350 3.1838 0.3144  -0.2666 -0.0125 264 ASP B OD2 
5498 N N   . SER B 265 ? 2.2514 2.0423 2.6104 0.2901  -0.1502 0.0062  265 SER B N   
5499 C CA  . SER B 265 ? 2.3462 2.1965 2.7306 0.2938  -0.1278 0.0098  265 SER B CA  
5500 C C   . SER B 265 ? 2.1530 2.0320 2.5443 0.3048  -0.1249 0.0120  265 SER B C   
5501 O O   . SER B 265 ? 2.5636 2.4673 2.9915 0.2856  -0.1107 0.0212  265 SER B O   
5502 C CB  . SER B 265 ? 2.6545 2.5232 3.0793 0.2641  -0.1077 0.0192  265 SER B CB  
5503 O OG  . SER B 265 ? 2.8713 2.7932 3.3188 0.2655  -0.0894 0.0238  265 SER B OG  
5504 N N   . PRO B 266 ? 2.0347 1.9124 2.3901 0.3371  -0.1376 0.0037  266 PRO B N   
5505 C CA  . PRO B 266 ? 2.0220 1.9287 2.3794 0.3506  -0.1347 0.0058  266 PRO B CA  
5506 C C   . PRO B 266 ? 1.9400 1.9154 2.3263 0.3524  -0.1125 0.0141  266 PRO B C   
5507 O O   . PRO B 266 ? 1.8032 1.8077 2.2000 0.3517  -0.1013 0.0164  266 PRO B O   
5508 C CB  . PRO B 266 ? 1.9614 1.8385 2.2642 0.3870  -0.1568 -0.0065 266 PRO B CB  
5509 C CG  . PRO B 266 ? 2.0745 1.9293 2.3503 0.3987  -0.1652 -0.0148 266 PRO B CG  
5510 C CD  . PRO B 266 ? 2.1228 1.9699 2.4307 0.3641  -0.1557 -0.0082 266 PRO B CD  
5511 N N   . SER B 267 ? 2.0185 2.0177 2.4172 0.3532  -0.1079 0.0196  267 SER B N   
5512 C CA  . SER B 267 ? 2.2481 2.3112 2.6744 0.3525  -0.0894 0.0299  267 SER B CA  
5513 C C   . SER B 267 ? 2.0849 2.1736 2.4908 0.3807  -0.0923 0.0293  267 SER B C   
5514 O O   . SER B 267 ? 2.1638 2.2204 2.5456 0.3916  -0.1063 0.0235  267 SER B O   
5515 C CB  . SER B 267 ? 2.5614 2.6397 3.0343 0.3182  -0.0753 0.0415  267 SER B CB  
5516 O OG  . SER B 267 ? 2.3867 2.4458 2.8665 0.3090  -0.0808 0.0435  267 SER B OG  
5517 N N   . GLY B 268 ? 1.6732 1.8245 2.0925 0.3897  -0.0778 0.0377  268 GLY B N   
5518 C CA  . GLY B 268 ? 1.5057 1.6979 1.9108 0.4166  -0.0755 0.0407  268 GLY B CA  
5519 C C   . GLY B 268 ? 1.3168 1.5691 1.7639 0.3981  -0.0579 0.0581  268 GLY B C   
5520 O O   . GLY B 268 ? 1.1679 1.4518 1.6468 0.3785  -0.0460 0.0681  268 GLY B O   
5521 N N   . LEU B 269 ? 1.3643 1.6285 1.8076 0.4053  -0.0586 0.0618  269 LEU B N   
5522 C CA  . LEU B 269 ? 1.4842 1.7957 1.9640 0.3863  -0.0457 0.0782  269 LEU B CA  
5523 C C   . LEU B 269 ? 1.4508 1.8168 1.9156 0.4148  -0.0409 0.0852  269 LEU B C   
5524 O O   . LEU B 269 ? 1.4473 1.7945 1.8741 0.4430  -0.0506 0.0759  269 LEU B O   
5525 C CB  . LEU B 269 ? 1.6723 1.9485 2.1684 0.3619  -0.0499 0.0789  269 LEU B CB  
5526 C CG  . LEU B 269 ? 2.1379 2.4565 2.6760 0.3363  -0.0372 0.0961  269 LEU B CG  
5527 C CD1 . LEU B 269 ? 2.8223 3.1371 3.3974 0.3026  -0.0294 0.1019  269 LEU B CD1 
5528 C CD2 . LEU B 269 ? 2.4769 2.7848 3.0182 0.3307  -0.0415 0.0988  269 LEU B CD2 
5529 N N   . GLY B 270 ? 1.4505 1.8826 1.9444 0.4066  -0.0267 0.1022  270 GLY B N   
5530 C CA  . GLY B 270 ? 1.6948 2.1920 2.1783 0.4342  -0.0194 0.1122  270 GLY B CA  
5531 C C   . GLY B 270 ? 1.6855 2.2396 2.2076 0.4114  -0.0079 0.1344  270 GLY B C   
5532 O O   . GLY B 270 ? 1.6358 2.1989 2.1966 0.3766  -0.0026 0.1454  270 GLY B O   
5533 N N   . HIS B 271 ? 1.7992 2.3931 2.3068 0.4338  -0.0046 0.1415  271 HIS B N   
5534 C CA  . HIS B 271 ? 1.9578 2.6119 2.4959 0.4175  0.0052  0.1644  271 HIS B CA  
5535 C C   . HIS B 271 ? 1.7803 2.5136 2.3089 0.4478  0.0148  0.1782  271 HIS B C   
5536 O O   . HIS B 271 ? 1.5166 2.2519 2.0040 0.4886  0.0128  0.1685  271 HIS B O   
5537 C CB  . HIS B 271 ? 2.3142 2.9374 2.8501 0.4075  0.0000  0.1624  271 HIS B CB  
5538 C CG  . HIS B 271 ? 2.5194 3.1995 3.0752 0.3983  0.0078  0.1839  271 HIS B CG  
5539 N ND1 . HIS B 271 ? 2.8745 3.5850 3.4024 0.4287  0.0097  0.1869  271 HIS B ND1 
5540 C CD2 . HIS B 271 ? 2.3177 3.0260 2.9147 0.3630  0.0127  0.2030  271 HIS B CD2 
5541 C CE1 . HIS B 271 ? 2.6758 3.4348 3.2295 0.4111  0.0165  0.2084  271 HIS B CE1 
5542 N NE2 . HIS B 271 ? 2.3013 3.0587 2.8973 0.3704  0.0175  0.2186  271 HIS B NE2 
5543 N N   . ILE B 272 ? 1.9554 2.7523 2.5221 0.4272  0.0243  0.2015  272 ILE B N   
5544 C CA  . ILE B 272 ? 2.0898 2.9751 2.6600 0.4469  0.0350  0.2224  272 ILE B CA  
5545 C C   . ILE B 272 ? 2.1452 3.0683 2.7365 0.4282  0.0395  0.2430  272 ILE B C   
5546 O O   . ILE B 272 ? 1.8483 2.7667 2.4765 0.3867  0.0382  0.2548  272 ILE B O   
5547 C CB  . ILE B 272 ? 2.1200 3.0549 2.7220 0.4320  0.0403  0.2390  272 ILE B CB  
5548 C CG1 . ILE B 272 ? 2.5009 3.3777 3.1021 0.4216  0.0332  0.2216  272 ILE B CG1 
5549 C CG2 . ILE B 272 ? 1.8981 2.9172 2.4919 0.4666  0.0499  0.2539  272 ILE B CG2 
5550 C CD1 . ILE B 272 ? 2.7948 3.6875 3.3730 0.4560  0.0339  0.2136  272 ILE B CD1 
5551 N N   . GLU B 273 ? 2.4166 3.3781 2.9828 0.4602  0.0445  0.2477  273 GLU B N   
5552 C CA  . GLU B 273 ? 2.3543 3.3664 2.9385 0.4472  0.0503  0.2708  273 GLU B CA  
5553 C C   . GLU B 273 ? 2.0383 3.1351 2.6621 0.4299  0.0592  0.3013  273 GLU B C   
5554 O O   . GLU B 273 ? 1.9742 3.0857 2.6050 0.4340  0.0605  0.3012  273 GLU B O   
5555 C CB  . GLU B 273 ? 2.4194 3.4421 2.9603 0.4888  0.0526  0.2649  273 GLU B CB  
5556 C CG  . GLU B 273 ? 2.5041 3.5575 3.0583 0.4727  0.0558  0.2839  273 GLU B CG  
5557 C CD  . GLU B 273 ? 2.6314 3.6990 3.1400 0.5157  0.0587  0.2794  273 GLU B CD  
5558 O OE1 . GLU B 273 ? 2.5223 3.5612 2.9850 0.5577  0.0555  0.2576  273 GLU B OE1 
5559 O OE2 . GLU B 273 ? 2.8631 3.9691 3.3800 0.5075  0.0632  0.2979  273 GLU B OE2 
5560 N N   . ARG B 274 ? 1.8478 2.9964 2.4969 0.4090  0.0633  0.3276  274 ARG B N   
5561 C CA  . ARG B 274 ? 2.0366 3.2708 2.7241 0.3899  0.0697  0.3615  274 ARG B CA  
5562 C C   . ARG B 274 ? 2.2709 3.5874 2.9423 0.4329  0.0818  0.3734  274 ARG B C   
5563 O O   . ARG B 274 ? 2.0648 3.4510 2.7639 0.4258  0.0868  0.3973  274 ARG B O   
5564 C CB  . ARG B 274 ? 1.9779 3.2375 2.6962 0.3521  0.0679  0.3868  274 ARG B CB  
5565 C CG  . ARG B 274 ? 2.2692 3.5514 2.9614 0.3776  0.0736  0.3895  274 ARG B CG  
5566 C CD  . ARG B 274 ? 2.2905 3.6071 3.0074 0.3471  0.0729  0.4162  274 ARG B CD  
5567 N NE  . ARG B 274 ? 2.4737 3.8269 3.1603 0.3811  0.0812  0.4203  274 ARG B NE  
5568 C CZ  . ARG B 274 ? 2.6821 3.9820 3.3253 0.4114  0.0794  0.3942  274 ARG B CZ  
5569 N NH1 . ARG B 274 ? 3.0261 4.2324 3.6540 0.4089  0.0689  0.3629  274 ARG B NH1 
5570 N NH2 . ARG B 274 ? 2.6490 3.9903 3.2635 0.4440  0.0875  0.4007  274 ARG B NH2 
5571 N N   . ASP B 275 ? 2.2790 3.5870 2.9045 0.4784  0.0858  0.3570  275 ASP B N   
5572 C CA  . ASP B 275 ? 1.9081 3.2886 2.5111 0.5263  0.0977  0.3647  275 ASP B CA  
5573 C C   . ASP B 275 ? 1.8327 3.1754 2.4051 0.5602  0.0947  0.3380  275 ASP B C   
5574 O O   . ASP B 275 ? 2.2154 3.5857 2.7505 0.6108  0.1011  0.3313  275 ASP B O   
5575 C CB  . ASP B 275 ? 1.7858 3.1908 2.3554 0.5583  0.1044  0.3670  275 ASP B CB  
5576 C CG  . ASP B 275 ? 1.8177 3.1290 2.3406 0.5759  0.0944  0.3339  275 ASP B CG  
5577 O OD1 . ASP B 275 ? 2.0365 3.2832 2.5267 0.5991  0.0866  0.3043  275 ASP B OD1 
5578 O OD2 . ASP B 275 ? 1.6610 2.9648 2.1802 0.5658  0.0933  0.3391  275 ASP B OD2 
5579 N N   . GLY B 276 ? 1.5357 2.8147 2.1222 0.5332  0.0846  0.3231  276 GLY B N   
5580 C CA  . GLY B 276 ? 1.6872 2.9334 2.2518 0.5576  0.0806  0.3016  276 GLY B CA  
5581 C C   . GLY B 276 ? 1.9503 3.1087 2.4603 0.5895  0.0710  0.2652  276 GLY B C   
5582 O O   . GLY B 276 ? 1.9699 3.0880 2.4589 0.6071  0.0647  0.2451  276 GLY B O   
5583 N N   . THR B 277 ? 2.2530 3.3814 2.7404 0.5950  0.0682  0.2581  277 THR B N   
5584 C CA  . THR B 277 ? 2.6662 3.7123 3.0994 0.6247  0.0566  0.2263  277 THR B CA  
5585 C C   . THR B 277 ? 2.7878 3.7428 3.2270 0.5959  0.0427  0.2052  277 THR B C   
5586 O O   . THR B 277 ? 3.1925 4.1216 3.6656 0.5515  0.0397  0.2105  277 THR B O   
5587 C CB  . THR B 277 ? 2.9732 4.0092 3.3855 0.6316  0.0556  0.2264  277 THR B CB  
5588 O OG1 . THR B 277 ? 2.8302 3.9484 3.2249 0.6707  0.0688  0.2418  277 THR B OG1 
5589 C CG2 . THR B 277 ? 2.9701 3.9094 3.3309 0.6522  0.0392  0.1946  277 THR B CG2 
5590 N N   . VAL B 278 ? 2.3510 3.2622 2.7576 0.6221  0.0346  0.1831  278 VAL B N   
5591 C CA  . VAL B 278 ? 2.3010 3.1274 2.7071 0.6006  0.0213  0.1628  278 VAL B CA  
5592 C C   . VAL B 278 ? 2.4287 3.1724 2.7904 0.6149  0.0061  0.1391  278 VAL B C   
5593 O O   . VAL B 278 ? 2.6108 3.3489 2.9229 0.6593  0.0020  0.1284  278 VAL B O   
5594 C CB  . VAL B 278 ? 2.1980 3.0191 2.5927 0.6185  0.0188  0.1529  278 VAL B CB  
5595 C CG1 . VAL B 278 ? 2.6740 3.4117 3.0732 0.5908  0.0062  0.1353  278 VAL B CG1 
5596 C CG2 . VAL B 278 ? 2.0978 3.0059 2.5321 0.6100  0.0325  0.1775  278 VAL B CG2 
5597 N N   . ARG B 279 ? 2.2402 2.9194 2.6197 0.5773  -0.0030 0.1316  279 ARG B N   
5598 C CA  . ARG B 279 ? 1.9650 2.5600 2.3099 0.5823  -0.0201 0.1107  279 ARG B CA  
5599 C C   . ARG B 279 ? 1.8463 2.3700 2.1960 0.5603  -0.0319 0.0955  279 ARG B C   
5600 O O   . ARG B 279 ? 1.5684 2.0944 1.9622 0.5217  -0.0266 0.1035  279 ARG B O   
5601 C CB  . ARG B 279 ? 2.2335 2.8291 2.5904 0.5644  -0.0195 0.1195  279 ARG B CB  
5602 C CG  . ARG B 279 ? 2.4119 3.0544 2.7380 0.6015  -0.0139 0.1259  279 ARG B CG  
5603 C CD  . ARG B 279 ? 3.0341 3.6941 3.3774 0.5826  -0.0102 0.1396  279 ARG B CD  
5604 N NE  . ARG B 279 ? 3.3860 4.1135 3.7850 0.5479  0.0047  0.1662  279 ARG B NE  
5605 C CZ  . ARG B 279 ? 3.6613 4.4009 4.0824 0.5236  0.0069  0.1795  279 ARG B CZ  
5606 N NH1 . ARG B 279 ? 3.9130 4.5990 4.3100 0.5264  -0.0046 0.1682  279 ARG B NH1 
5607 N NH2 . ARG B 279 ? 3.5277 4.3305 3.9939 0.4957  0.0187  0.2046  279 ARG B NH2 
5608 N N   . VAL B 280 ? 2.1057 2.5666 2.4062 0.5876  -0.0487 0.0739  280 VAL B N   
5609 C CA  . VAL B 280 ? 2.4209 2.8038 2.7177 0.5684  -0.0637 0.0589  280 VAL B CA  
5610 C C   . VAL B 280 ? 2.5200 2.8629 2.8318 0.5391  -0.0705 0.0599  280 VAL B C   
5611 O O   . VAL B 280 ? 2.6155 2.9286 2.8929 0.5573  -0.0821 0.0525  280 VAL B O   
5612 C CB  . VAL B 280 ? 2.3430 2.6682 2.5788 0.6065  -0.0830 0.0371  280 VAL B CB  
5613 C CG1 . VAL B 280 ? 2.2335 2.5377 2.4189 0.6410  -0.0944 0.0287  280 VAL B CG1 
5614 C CG2 . VAL B 280 ? 2.0542 2.3001 2.2879 0.5834  -0.0997 0.0244  280 VAL B CG2 
5615 N N   . VAL B 281 ? 2.2137 2.5614 2.5767 0.4955  -0.0626 0.0702  281 VAL B N   
5616 C CA  . VAL B 281 ? 1.8888 2.2037 2.2695 0.4681  -0.0679 0.0724  281 VAL B CA  
5617 C C   . VAL B 281 ? 2.0516 2.2835 2.4082 0.4653  -0.0883 0.0557  281 VAL B C   
5618 O O   . VAL B 281 ? 2.5836 2.7756 2.9093 0.4777  -0.1035 0.0481  281 VAL B O   
5619 C CB  . VAL B 281 ? 1.9739 2.3160 2.4130 0.4250  -0.0547 0.0883  281 VAL B CB  
5620 C CG1 . VAL B 281 ? 2.5262 2.8377 2.9789 0.4033  -0.0610 0.0904  281 VAL B CG1 
5621 C CG2 . VAL B 281 ? 2.0232 2.4469 2.4863 0.4251  -0.0373 0.1071  281 VAL B CG2 
5622 N N   . ALA B 282 ? 1.9751 2.1820 2.3439 0.4496  -0.0897 0.0511  282 ALA B N   
5623 C CA  . ALA B 282 ? 2.1664 2.2979 2.5162 0.4430  -0.1091 0.0383  282 ALA B CA  
5624 C C   . ALA B 282 ? 2.1132 2.2262 2.4625 0.4388  -0.1102 0.0321  282 ALA B C   
5625 O O   . ALA B 282 ? 2.1848 2.3404 2.5594 0.4313  -0.0946 0.0390  282 ALA B O   
5626 C CB  . ALA B 282 ? 2.4794 2.5845 2.8623 0.4072  -0.1115 0.0443  282 ALA B CB  
5627 N N   . CYS B 283 ? 1.8587 1.9044 2.1782 0.4419  -0.1309 0.0199  283 CYS B N   
5628 C CA  . CYS B 283 ? 1.8614 1.8766 2.1788 0.4335  -0.1358 0.0139  283 CYS B CA  
5629 C C   . CYS B 283 ? 1.8615 1.8195 2.1914 0.4032  -0.1483 0.0137  283 CYS B C   
5630 O O   . CYS B 283 ? 1.9859 1.9001 2.2947 0.4053  -0.1669 0.0099  283 CYS B O   
5631 C CB  . CYS B 283 ? 2.2506 2.2408 2.5123 0.4720  -0.1512 -0.0002 283 CYS B CB  
5632 S SG  . CYS B 283 ? 2.8571 2.9208 3.1032 0.5124  -0.1362 0.0017  283 CYS B SG  
5633 N N   . HIS B 284 ? 1.7191 1.6799 2.0836 0.3750  -0.1379 0.0189  284 HIS B N   
5634 C CA  . HIS B 284 ? 1.7962 1.7128 2.1785 0.3449  -0.1455 0.0213  284 HIS B CA  
5635 C C   . HIS B 284 ? 1.8356 1.7276 2.2104 0.3396  -0.1487 0.0166  284 HIS B C   
5636 O O   . HIS B 284 ? 1.8764 1.7877 2.2373 0.3565  -0.1435 0.0119  284 HIS B O   
5637 C CB  . HIS B 284 ? 1.8808 1.8279 2.3186 0.3116  -0.1260 0.0343  284 HIS B CB  
5638 C CG  . HIS B 284 ? 1.8794 1.8631 2.3365 0.3104  -0.1169 0.0420  284 HIS B CG  
5639 N ND1 . HIS B 284 ? 1.9908 2.0286 2.4497 0.3257  -0.1037 0.0455  284 HIS B ND1 
5640 C CD2 . HIS B 284 ? 1.6505 1.6264 2.1273 0.2946  -0.1193 0.0483  284 HIS B CD2 
5641 C CE1 . HIS B 284 ? 1.6893 1.7486 2.1666 0.3188  -0.0988 0.0534  284 HIS B CE1 
5642 N NE2 . HIS B 284 ? 1.4893 1.5104 1.9768 0.3007  -0.1084 0.0544  284 HIS B NE2 
5643 N N   . ASP B 285 ? 1.8154 1.6677 2.2032 0.3138  -0.1565 0.0198  285 ASP B N   
5644 C CA  . ASP B 285 ? 1.8921 1.7174 2.2795 0.3005  -0.1594 0.0186  285 ASP B CA  
5645 C C   . ASP B 285 ? 1.9581 1.8013 2.3959 0.2663  -0.1404 0.0301  285 ASP B C   
5646 O O   . ASP B 285 ? 1.8282 1.6448 2.2821 0.2442  -0.1461 0.0364  285 ASP B O   
5647 C CB  . ASP B 285 ? 1.9802 1.7402 2.3320 0.3028  -0.1883 0.0133  285 ASP B CB  
5648 C CG  . ASP B 285 ? 2.2205 1.9509 2.5230 0.3287  -0.2048 0.0009  285 ASP B CG  
5649 O OD1 . ASP B 285 ? 2.7786 2.5111 3.0857 0.3221  -0.1979 0.0003  285 ASP B OD1 
5650 O OD2 . ASP B 285 ? 1.9794 1.6829 2.2379 0.3556  -0.2251 -0.0081 285 ASP B OD2 
5651 N N   . GLN B 286 ? 2.1549 2.0446 2.6160 0.2637  -0.1185 0.0332  286 GLN B N   
5652 C CA  . GLN B 286 ? 2.0724 1.9794 2.5744 0.2363  -0.0998 0.0421  286 GLN B CA  
5653 C C   . GLN B 286 ? 2.1967 2.0669 2.6943 0.2224  -0.1050 0.0414  286 GLN B C   
5654 O O   . GLN B 286 ? 2.7352 2.5752 3.1982 0.2355  -0.1203 0.0337  286 GLN B O   
5655 C CB  . GLN B 286 ? 1.7466 1.6997 2.2629 0.2385  -0.0811 0.0440  286 GLN B CB  
5656 C CG  . GLN B 286 ? 1.9105 1.9092 2.4334 0.2509  -0.0739 0.0473  286 GLN B CG  
5657 C CD  . GLN B 286 ? 2.1066 2.1501 2.6485 0.2469  -0.0571 0.0528  286 GLN B CD  
5658 O OE1 . GLN B 286 ? 2.0171 2.0543 2.5666 0.2347  -0.0508 0.0531  286 GLN B OE1 
5659 N NE2 . GLN B 286 ? 2.1841 2.2726 2.7325 0.2567  -0.0508 0.0582  286 GLN B NE2 
5660 N N   . VAL B 287 ? 2.0080 1.8821 2.5398 0.1969  -0.0918 0.0501  287 VAL B N   
5661 C CA  . VAL B 287 ? 2.1948 2.0450 2.7280 0.1819  -0.0906 0.0519  287 VAL B CA  
5662 C C   . VAL B 287 ? 2.4192 2.2993 2.9819 0.1680  -0.0672 0.0568  287 VAL B C   
5663 O O   . VAL B 287 ? 2.7276 2.6192 3.3217 0.1518  -0.0557 0.0648  287 VAL B O   
5664 C CB  . VAL B 287 ? 1.9663 1.7834 2.5075 0.1651  -0.1022 0.0591  287 VAL B CB  
5665 C CG1 . VAL B 287 ? 1.3586 1.1907 1.9292 0.1557  -0.0982 0.0670  287 VAL B CG1 
5666 C CG2 . VAL B 287 ? 1.9731 1.7746 2.5250 0.1453  -0.0964 0.0652  287 VAL B CG2 
5667 N N   . LEU B 288 ? 2.6648 2.5562 3.2156 0.1755  -0.0613 0.0520  288 LEU B N   
5668 C CA  . LEU B 288 ? 2.9372 2.8542 3.5099 0.1643  -0.0420 0.0559  288 LEU B CA  
5669 C C   . LEU B 288 ? 3.3894 3.2958 3.9882 0.1418  -0.0317 0.0637  288 LEU B C   
5670 O O   . LEU B 288 ? 3.8461 3.7739 4.4714 0.1322  -0.0182 0.0693  288 LEU B O   
5671 C CB  . LEU B 288 ? 3.0054 2.9232 3.5601 0.1706  -0.0402 0.0508  288 LEU B CB  
5672 C CG  . LEU B 288 ? 2.8886 2.8206 3.4174 0.1954  -0.0494 0.0437  288 LEU B CG  
5673 C CD1 . LEU B 288 ? 2.2935 2.2252 2.8063 0.2004  -0.0484 0.0396  288 LEU B CD1 
5674 C CD2 . LEU B 288 ? 2.7718 2.7476 3.3156 0.2026  -0.0427 0.0476  288 LEU B CD2 
5675 N N   . SER B 289 ? 3.7769 3.6503 4.3669 0.1342  -0.0392 0.0649  289 SER B N   
5676 C CA  . SER B 289 ? 4.2136 4.0778 4.8268 0.1147  -0.0308 0.0740  289 SER B CA  
5677 C C   . SER B 289 ? 4.1633 4.0474 4.7962 0.1058  -0.0095 0.0768  289 SER B C   
5678 O O   . SER B 289 ? 4.9872 4.8873 5.6469 0.0982  0.0009  0.0826  289 SER B O   
5679 C CB  . SER B 289 ? 4.7890 4.6536 5.4216 0.1091  -0.0360 0.0807  289 SER B CB  
5680 O OG  . SER B 289 ? 5.9625 5.8563 6.6113 0.1137  -0.0289 0.0807  289 SER B OG  
5681 N N   . GLY B 290 ? 3.5607 3.4408 4.1775 0.1077  -0.0051 0.0723  290 GLY B N   
5682 C CA  . GLY B 290 ? 3.3584 3.2522 3.9853 0.1016  0.0114  0.0734  290 GLY B CA  
5683 C C   . GLY B 290 ? 2.9905 2.9148 3.6266 0.1075  0.0148  0.0724  290 GLY B C   
5684 O O   . GLY B 290 ? 3.1103 3.0462 3.7595 0.1006  0.0266  0.0752  290 GLY B O   
5685 N N   . GLY B 291 ? 2.5612 2.4972 3.1890 0.1205  0.0035  0.0693  291 GLY B N   
5686 C CA  . GLY B 291 ? 2.4392 2.4082 3.0736 0.1271  0.0052  0.0701  291 GLY B CA  
5687 C C   . GLY B 291 ? 2.9946 2.9806 3.6567 0.1190  0.0118  0.0768  291 GLY B C   
5688 O O   . GLY B 291 ? 3.2342 3.2482 3.9021 0.1238  0.0113  0.0791  291 GLY B O   
5689 N N   . GLN B 292 ? 3.3654 3.3370 4.0448 0.1072  0.0178  0.0810  292 GLN B N   
5690 C CA  . GLN B 292 ? 3.0807 3.0653 3.7860 0.1006  0.0226  0.0871  292 GLN B CA  
5691 C C   . GLN B 292 ? 2.8775 2.8652 3.5835 0.1078  0.0109  0.0874  292 GLN B C   
5692 O O   . GLN B 292 ? 2.7315 2.7259 3.4580 0.1026  0.0122  0.0926  292 GLN B O   
5693 C CB  . GLN B 292 ? 3.0160 2.9872 3.7404 0.0883  0.0328  0.0921  292 GLN B CB  
5694 C CG  . GLN B 292 ? 2.8438 2.8023 3.5618 0.0827  0.0438  0.0911  292 GLN B CG  
5695 C CD  . GLN B 292 ? 2.8400 2.8096 3.5605 0.0800  0.0513  0.0912  292 GLN B CD  
5696 O OE1 . GLN B 292 ? 3.1626 3.1316 3.8660 0.0820  0.0506  0.0877  292 GLN B OE1 
5697 N NE2 . GLN B 292 ? 2.4291 2.4066 3.1697 0.0750  0.0570  0.0958  292 GLN B NE2 
5698 N N   . TYR B 293 ? 2.6044 2.5840 3.2852 0.1207  -0.0015 0.0816  293 TYR B N   
5699 C CA  . TYR B 293 ? 2.0465 2.0243 2.7175 0.1319  -0.0154 0.0798  293 TYR B CA  
5700 C C   . TYR B 293 ? 2.0274 1.9944 2.7191 0.1215  -0.0176 0.0860  293 TYR B C   
5701 O O   . TYR B 293 ? 2.0374 2.0177 2.7390 0.1236  -0.0204 0.0887  293 TYR B O   
5702 C CB  . TYR B 293 ? 1.6362 1.6478 2.3037 0.1438  -0.0149 0.0793  293 TYR B CB  
5703 C CG  . TYR B 293 ? 1.5523 1.5706 2.2128 0.1560  -0.0257 0.0789  293 TYR B CG  
5704 C CD1 . TYR B 293 ? 1.6928 1.7236 2.3760 0.1485  -0.0231 0.0854  293 TYR B CD1 
5705 C CD2 . TYR B 293 ? 1.4284 1.4401 2.0571 0.1767  -0.0387 0.0717  293 TYR B CD2 
5706 C CE1 . TYR B 293 ? 1.7524 1.7887 2.4270 0.1599  -0.0330 0.0851  293 TYR B CE1 
5707 C CE2 . TYR B 293 ? 1.3919 1.4081 2.0097 0.1900  -0.0486 0.0707  293 TYR B CE2 
5708 C CZ  . TYR B 293 ? 1.5517 1.5802 2.1925 0.1811  -0.0456 0.0776  293 TYR B CZ  
5709 O OH  . TYR B 293 ? 1.7579 1.7881 2.3849 0.1947  -0.0560 0.0764  293 TYR B OH  
5710 N N   . TRP B 294 ? 2.2424 2.1877 2.9420 0.1096  -0.0158 0.0895  294 TRP B N   
5711 C CA  . TRP B 294 ? 2.5711 2.5112 3.2945 0.0989  -0.0170 0.0976  294 TRP B CA  
5712 C C   . TRP B 294 ? 2.6225 2.5527 3.3344 0.1070  -0.0358 0.0966  294 TRP B C   
5713 O O   . TRP B 294 ? 2.9646 2.8873 3.6935 0.0985  -0.0414 0.1037  294 TRP B O   
5714 C CB  . TRP B 294 ? 2.3737 2.2963 3.1076 0.0855  -0.0126 0.1039  294 TRP B CB  
5715 C CG  . TRP B 294 ? 2.2484 2.1796 2.9908 0.0797  0.0063  0.1044  294 TRP B CG  
5716 C CD1 . TRP B 294 ? 2.4176 2.3382 3.1413 0.0806  0.0101  0.1002  294 TRP B CD1 
5717 C CD2 . TRP B 294 ? 2.0551 2.0038 2.8225 0.0737  0.0226  0.1086  294 TRP B CD2 
5718 N NE1 . TRP B 294 ? 2.7022 2.6316 3.4365 0.0755  0.0274  0.1015  294 TRP B NE1 
5719 C CE2 . TRP B 294 ? 2.4266 2.3722 3.1867 0.0718  0.0351  0.1063  294 TRP B CE2 
5720 C CE3 . TRP B 294 ? 1.7741 1.7379 2.5672 0.0703  0.0268  0.1138  294 TRP B CE3 
5721 C CZ2 . TRP B 294 ? 2.5307 2.4852 3.3053 0.0678  0.0506  0.1084  294 TRP B CZ2 
5722 C CZ3 . TRP B 294 ? 2.4035 2.3770 3.2126 0.0662  0.0421  0.1161  294 TRP B CZ3 
5723 C CH2 . TRP B 294 ? 2.6063 2.5741 3.4052 0.0654  0.0536  0.1132  294 TRP B CH2 
5724 N N   . GLY B 295 ? 2.2534 2.1857 2.9368 0.1243  -0.0449 0.0883  295 GLY B N   
5725 C CA  . GLY B 295 ? 2.2327 2.1625 2.9027 0.1364  -0.0599 0.0861  295 GLY B CA  
5726 C C   . GLY B 295 ? 2.1005 2.0198 2.7292 0.1587  -0.0739 0.0760  295 GLY B C   
5727 O O   . GLY B 295 ? 1.7772 1.7022 2.3906 0.1667  -0.0694 0.0705  295 GLY B O   
5728 N N   . CYS B 296 ? 1.9681 1.8727 2.5784 0.1699  -0.0910 0.0737  296 CYS B N   
5729 C CA  . CYS B 296 ? 1.4991 1.3885 2.0658 0.1946  -0.1072 0.0636  296 CYS B CA  
5730 C C   . CYS B 296 ? 1.5075 1.3686 2.0543 0.2027  -0.1290 0.0624  296 CYS B C   
5731 O O   . CYS B 296 ? 1.1741 1.0357 1.7440 0.1899  -0.1302 0.0700  296 CYS B O   
5732 C CB  . CYS B 296 ? 1.3936 1.3245 1.9541 0.2122  -0.0959 0.0600  296 CYS B CB  
5733 S SG  . CYS B 296 ? 1.9522 1.9075 2.5170 0.2211  -0.0971 0.0634  296 CYS B SG  
5734 N N   . ARG B 297 ? 1.7660 1.6019 2.2670 0.2262  -0.1472 0.0522  297 ARG B N   
5735 C CA  . ARG B 297 ? 2.0352 1.8341 2.5056 0.2375  -0.1723 0.0489  297 ARG B CA  
5736 C C   . ARG B 297 ? 2.0486 1.8547 2.4775 0.2720  -0.1790 0.0382  297 ARG B C   
5737 O O   . ARG B 297 ? 1.9589 1.7821 2.3687 0.2911  -0.1726 0.0310  297 ARG B O   
5738 C CB  . ARG B 297 ? 1.9183 1.6589 2.3572 0.2368  -0.1986 0.0455  297 ARG B CB  
5739 C CG  . ARG B 297 ? 2.2133 1.9292 2.6797 0.2057  -0.2052 0.0576  297 ARG B CG  
5740 C CD  . ARG B 297 ? 2.0018 1.6551 2.4312 0.2062  -0.2396 0.0564  297 ARG B CD  
5741 N NE  . ARG B 297 ? 2.1199 1.7524 2.5594 0.1847  -0.2430 0.0637  297 ARG B NE  
5742 C CZ  . ARG B 297 ? 2.2525 1.9128 2.7328 0.1633  -0.2202 0.0726  297 ARG B CZ  
5743 N NH1 . ARG B 297 ? 2.3115 1.9521 2.7868 0.1524  -0.2238 0.0754  297 ARG B NH1 
5744 N NH2 . ARG B 297 ? 2.8655 2.5721 3.3881 0.1544  -0.1938 0.0780  297 ARG B NH2 
5745 N N   . PHE B 298 ? 2.1238 1.9119 2.5350 0.2810  -0.1947 0.0374  298 PHE B N   
5746 C CA  . PHE B 298 ? 2.2547 2.0449 2.6220 0.3158  -0.2034 0.0277  298 PHE B CA  
5747 C C   . PHE B 298 ? 2.3171 2.0451 2.6376 0.3289  -0.2366 0.0211  298 PHE B C   
5748 O O   . PHE B 298 ? 2.0915 1.7870 2.4233 0.3082  -0.2513 0.0279  298 PHE B O   
5749 C CB  . PHE B 298 ? 2.4523 2.2958 2.8427 0.3186  -0.1848 0.0336  298 PHE B CB  
5750 C CG  . PHE B 298 ? 2.2321 2.0807 2.5797 0.3533  -0.1929 0.0262  298 PHE B CG  
5751 C CD1 . PHE B 298 ? 2.2085 2.0232 2.5345 0.3584  -0.2127 0.0252  298 PHE B CD1 
5752 C CD2 . PHE B 298 ? 2.0840 1.9725 2.4130 0.3812  -0.1809 0.0214  298 PHE B CD2 
5753 C CE1 . PHE B 298 ? 2.1128 1.9316 2.3966 0.3919  -0.2194 0.0183  298 PHE B CE1 
5754 C CE2 . PHE B 298 ? 2.1452 2.0419 2.4342 0.4152  -0.1869 0.0155  298 PHE B CE2 
5755 C CZ  . PHE B 298 ? 2.1010 1.9622 2.3664 0.4209  -0.2056 0.0135  298 PHE B CZ  
5756 N N   . PRO B 299 ? 2.5427 2.2525 2.8065 0.3658  -0.2508 0.0079  299 PRO B N   
5757 C CA  . PRO B 299 ? 2.4541 2.2026 2.7019 0.3932  -0.2354 0.0005  299 PRO B CA  
5758 C C   . PRO B 299 ? 2.5479 2.2816 2.7917 0.3893  -0.2360 -0.0034 299 PRO B C   
5759 O O   . PRO B 299 ? 3.1107 2.8073 3.3662 0.3639  -0.2463 0.0004  299 PRO B O   
5760 C CB  . PRO B 299 ? 2.1706 1.8991 2.3563 0.4356  -0.2530 -0.0118 299 PRO B CB  
5761 C CG  . PRO B 299 ? 2.2784 1.9322 2.4341 0.4298  -0.2868 -0.0146 299 PRO B CG  
5762 C CD  . PRO B 299 ? 2.2979 1.9488 2.5083 0.3848  -0.2833 0.0000  299 PRO B CD  
5763 N N   . ALA B 300 ? 2.3028 2.0684 2.5312 0.4142  -0.2246 -0.0100 300 ALA B N   
5764 C CA  . ALA B 300 ? 2.4149 2.1652 2.6354 0.4132  -0.2265 -0.0146 300 ALA B CA  
5765 C C   . ALA B 300 ? 2.6151 2.2894 2.7820 0.4258  -0.2610 -0.0250 300 ALA B C   
5766 O O   . ALA B 300 ? 2.5385 2.1775 2.6700 0.4414  -0.2820 -0.0300 300 ALA B O   
5767 C CB  . ALA B 300 ? 2.5211 2.3217 2.7346 0.4393  -0.2095 -0.0188 300 ALA B CB  
5768 N N   . ASP B 301 ? 2.8794 2.5266 3.0394 0.4180  -0.2678 -0.0277 301 ASP B N   
5769 C CA  . ASP B 301 ? 3.0962 2.6694 3.2039 0.4287  -0.3021 -0.0368 301 ASP B CA  
5770 C C   . ASP B 301 ? 3.0430 2.6030 3.0887 0.4778  -0.3166 -0.0523 301 ASP B C   
5771 O O   . ASP B 301 ? 3.1749 2.7843 3.2180 0.5034  -0.2981 -0.0569 301 ASP B O   
5772 C CB  . ASP B 301 ? 3.2642 2.8174 3.3785 0.4107  -0.3042 -0.0355 301 ASP B CB  
5773 C CG  . ASP B 301 ? 3.5365 3.0108 3.5988 0.4168  -0.3413 -0.0429 301 ASP B CG  
5774 O OD1 . ASP B 301 ? 3.4618 2.8939 3.4708 0.4450  -0.3673 -0.0532 301 ASP B OD1 
5775 O OD2 . ASP B 301 ? 3.8778 3.3317 3.9515 0.3933  -0.3447 -0.0379 301 ASP B OD2 
5776 N N   . GLU B 302 ? 3.0397 2.5327 3.0358 0.4903  -0.3505 -0.0593 302 GLU B N   
5777 C CA  . GLU B 302 ? 3.1691 2.6373 3.0990 0.5382  -0.3691 -0.0745 302 GLU B CA  
5778 C C   . GLU B 302 ? 3.1634 2.6445 3.0615 0.5735  -0.3653 -0.0866 302 GLU B C   
5779 O O   . GLU B 302 ? 3.3280 2.8403 3.1985 0.6142  -0.3576 -0.0948 302 GLU B O   
5780 C CB  . GLU B 302 ? 3.1601 2.5386 3.0394 0.5395  -0.4120 -0.0796 302 GLU B CB  
5781 C CG  . GLU B 302 ? 3.2490 2.5687 3.1232 0.5132  -0.4352 -0.0768 302 GLU B CG  
5782 C CD  . GLU B 302 ? 3.4472 2.6777 3.2767 0.5073  -0.4801 -0.0779 302 GLU B CD  
5783 O OE1 . GLU B 302 ? 3.5732 2.7506 3.3311 0.5455  -0.5090 -0.0933 302 GLU B OE1 
5784 O OE2 . GLU B 302 ? 3.6115 2.8263 3.4782 0.4644  -0.4865 -0.0626 302 GLU B OE2 
5785 N N   . ARG B 303 ? 2.9419 2.4001 2.8439 0.5579  -0.3708 -0.0867 303 ARG B N   
5786 C CA  . ARG B 303 ? 2.6487 2.1092 2.5190 0.5886  -0.3718 -0.0980 303 ARG B CA  
5787 C C   . ARG B 303 ? 2.6404 2.1920 2.5455 0.6019  -0.3341 -0.0946 303 ARG B C   
5788 O O   . ARG B 303 ? 2.5866 2.1611 2.4576 0.6458  -0.3317 -0.1042 303 ARG B O   
5789 C CB  . ARG B 303 ? 2.5872 2.0110 2.4655 0.5609  -0.3818 -0.0954 303 ARG B CB  
5790 C CG  . ARG B 303 ? 2.9677 2.2957 2.7921 0.5608  -0.4256 -0.1019 303 ARG B CG  
5791 C CD  . ARG B 303 ? 3.0568 2.3589 2.9177 0.5099  -0.4305 -0.0880 303 ARG B CD  
5792 N NE  . ARG B 303 ? 3.4115 2.7129 3.3082 0.4767  -0.4300 -0.0743 303 ARG B NE  
5793 C CZ  . ARG B 303 ? 3.3674 2.6515 3.3001 0.4317  -0.4336 -0.0593 303 ARG B CZ  
5794 N NH1 . ARG B 303 ? 3.2432 2.5112 3.1818 0.4134  -0.4363 -0.0557 303 ARG B NH1 
5795 N NH2 . ARG B 303 ? 3.2791 2.5646 3.2422 0.4059  -0.4341 -0.0471 303 ARG B NH2 
5796 N N   . TRP B 304 ? 2.8563 2.4594 2.8284 0.5642  -0.3059 -0.0802 304 TRP B N   
5797 C CA  . TRP B 304 ? 2.7464 2.4325 2.7545 0.5706  -0.2729 -0.0745 304 TRP B CA  
5798 C C   . TRP B 304 ? 2.6981 2.4429 2.7403 0.5664  -0.2510 -0.0646 304 TRP B C   
5799 O O   . TRP B 304 ? 2.6063 2.4203 2.6904 0.5590  -0.2232 -0.0552 304 TRP B O   
5800 C CB  . TRP B 304 ? 2.6307 2.3383 2.6844 0.5372  -0.2559 -0.0661 304 TRP B CB  
5801 C CG  . TRP B 304 ? 2.6557 2.3275 2.7403 0.4909  -0.2603 -0.0573 304 TRP B CG  
5802 C CD1 . TRP B 304 ? 2.2875 1.9838 2.4244 0.4550  -0.2435 -0.0439 304 TRP B CD1 
5803 C CD2 . TRP B 304 ? 2.9787 2.5838 3.0417 0.4768  -0.2836 -0.0606 304 TRP B CD2 
5804 N NE1 . TRP B 304 ? 2.3163 1.9691 2.4663 0.4215  -0.2536 -0.0384 304 TRP B NE1 
5805 C CE2 . TRP B 304 ? 2.9069 2.5043 3.0133 0.4325  -0.2781 -0.0476 304 TRP B CE2 
5806 C CE3 . TRP B 304 ? 3.2697 2.8219 3.2808 0.4976  -0.3091 -0.0725 304 TRP B CE3 
5807 C CZ2 . TRP B 304 ? 3.2335 2.7758 3.3338 0.4082  -0.2965 -0.0447 304 TRP B CZ2 
5808 C CZ3 . TRP B 304 ? 3.2736 2.7671 3.2777 0.4719  -0.3288 -0.0701 304 TRP B CZ3 
5809 C CH2 . TRP B 304 ? 3.2864 2.7770 3.3354 0.4272  -0.3221 -0.0555 304 TRP B CH2 
5810 N N   . ARG B 305 ? 2.7432 2.4603 2.7665 0.5711  -0.2646 -0.0661 305 ARG B N   
5811 C CA  . ARG B 305 ? 2.8960 2.6698 2.9508 0.5675  -0.2439 -0.0563 305 ARG B CA  
5812 C C   . ARG B 305 ? 3.2245 3.0487 3.2532 0.6131  -0.2335 -0.0610 305 ARG B C   
5813 O O   . ARG B 305 ? 3.4421 3.3398 3.5089 0.6101  -0.2065 -0.0510 305 ARG B O   
5814 C CB  . ARG B 305 ? 2.7298 2.4669 2.7782 0.5566  -0.2586 -0.0544 305 ARG B CB  
5815 C CG  . ARG B 305 ? 2.4128 2.2093 2.4956 0.5510  -0.2368 -0.0434 305 ARG B CG  
5816 C CD  . ARG B 305 ? 2.3339 2.1312 2.3719 0.5894  -0.2451 -0.0499 305 ARG B CD  
5817 N NE  . ARG B 305 ? 2.5410 2.4077 2.6192 0.5812  -0.2196 -0.0368 305 ARG B NE  
5818 C CZ  . ARG B 305 ? 2.6918 2.6186 2.7610 0.6119  -0.2037 -0.0348 305 ARG B CZ  
5819 N NH1 . ARG B 305 ? 2.9062 2.8971 3.0190 0.5969  -0.1805 -0.0201 305 ARG B NH1 
5820 N NH2 . ARG B 305 ? 2.6350 2.5599 2.6522 0.6577  -0.2109 -0.0465 305 ARG B NH2 
5821 N N   . PRO B 306 ? 3.0924 2.8729 3.0538 0.6554  -0.2570 -0.0762 306 PRO B N   
5822 C CA  . PRO B 306 ? 2.8827 2.7066 2.8107 0.7053  -0.2494 -0.0817 306 PRO B CA  
5823 C C   . PRO B 306 ? 2.8290 2.7165 2.7798 0.7143  -0.2279 -0.0775 306 PRO B C   
5824 O O   . PRO B 306 ? 2.8756 2.8406 2.8448 0.7304  -0.2047 -0.0687 306 PRO B O   
5825 C CB  . PRO B 306 ? 2.6388 2.3840 2.4860 0.7451  -0.2842 -0.1011 306 PRO B CB  
5826 C CG  . PRO B 306 ? 2.7533 2.4195 2.5960 0.7119  -0.3098 -0.1019 306 PRO B CG  
5827 C CD  . PRO B 306 ? 2.8274 2.5132 2.7400 0.6574  -0.2934 -0.0877 306 PRO B CD  
5828 N N   . GLU B 307 ? 2.7695 2.6240 2.7214 0.7008  -0.2363 -0.0819 307 GLU B N   
5829 C CA  . GLU B 307 ? 2.8027 2.7071 2.7761 0.7050  -0.2196 -0.0782 307 GLU B CA  
5830 C C   . GLU B 307 ? 2.5930 2.5774 2.6370 0.6727  -0.1875 -0.0586 307 GLU B C   
5831 O O   . GLU B 307 ? 2.4845 2.5427 2.5459 0.6886  -0.1677 -0.0506 307 GLU B O   
5832 C CB  . GLU B 307 ? 2.8141 2.6581 2.7789 0.6870  -0.2364 -0.0851 307 GLU B CB  
5833 C CG  . GLU B 307 ? 2.8819 2.6424 2.7740 0.7182  -0.2715 -0.1038 307 GLU B CG  
5834 C CD  . GLU B 307 ? 3.1808 2.8910 3.0539 0.7135  -0.2886 -0.1117 307 GLU B CD  
5835 O OE1 . GLU B 307 ? 3.2840 2.9757 3.1932 0.6688  -0.2868 -0.1042 307 GLU B OE1 
5836 O OE2 . GLU B 307 ? 3.3219 3.0104 3.1421 0.7560  -0.3041 -0.1254 307 GLU B OE2 
5837 N N   . ILE B 308 ? 2.4917 2.4589 2.5747 0.6274  -0.1844 -0.0503 308 ILE B N   
5838 C CA  . ILE B 308 ? 2.4537 2.4824 2.6015 0.5922  -0.1579 -0.0326 308 ILE B CA  
5839 C C   . ILE B 308 ? 2.2859 2.3825 2.4431 0.6101  -0.1417 -0.0232 308 ILE B C   
5840 O O   . ILE B 308 ? 2.2245 2.3893 2.4208 0.6008  -0.1205 -0.0096 308 ILE B O   
5841 C CB  . ILE B 308 ? 2.3700 2.3673 2.5550 0.5443  -0.1578 -0.0259 308 ILE B CB  
5842 C CG1 . ILE B 308 ? 2.5452 2.4934 2.7330 0.5213  -0.1673 -0.0301 308 ILE B CG1 
5843 C CG2 . ILE B 308 ? 1.8475 1.9105 2.0913 0.5162  -0.1319 -0.0084 308 ILE B CG2 
5844 C CD1 . ILE B 308 ? 2.7215 2.6496 2.9505 0.4750  -0.1633 -0.0214 308 ILE B CD1 
5845 N N   . THR B 309 ? 2.0042 2.0775 2.1262 0.6320  -0.1534 -0.0295 309 THR B N   
5846 C CA  . THR B 309 ? 2.0901 2.2190 2.2192 0.6453  -0.1399 -0.0202 309 THR B CA  
5847 C C   . THR B 309 ? 2.2548 2.4618 2.3832 0.6777  -0.1230 -0.0138 309 THR B C   
5848 O O   . THR B 309 ? 2.0866 2.3689 2.2559 0.6670  -0.1011 0.0038  309 THR B O   
5849 C CB  . THR B 309 ? 2.0894 2.1700 2.1657 0.6724  -0.1597 -0.0318 309 THR B CB  
5850 O OG1 . THR B 309 ? 2.2960 2.3301 2.3917 0.6349  -0.1686 -0.0297 309 THR B OG1 
5851 C CG2 . THR B 309 ? 2.0095 2.1496 2.0769 0.7010  -0.1469 -0.0249 309 THR B CG2 
5852 N N   . ASP B 310 ? 2.4505 2.6356 2.5297 0.7178  -0.1357 -0.0281 310 ASP B N   
5853 C CA  . ASP B 310 ? 2.4554 2.7092 2.5253 0.7564  -0.1229 -0.0241 310 ASP B CA  
5854 C C   . ASP B 310 ? 2.1478 2.4664 2.2766 0.7280  -0.1021 -0.0070 310 ASP B C   
5855 O O   . ASP B 310 ? 2.2772 2.6809 2.4326 0.7355  -0.0822 0.0096  310 ASP B O   
5856 C CB  . ASP B 310 ? 3.0175 3.2280 3.0230 0.8036  -0.1424 -0.0438 310 ASP B CB  
5857 C CG  . ASP B 310 ? 3.4929 3.6825 3.4355 0.8527  -0.1549 -0.0559 310 ASP B CG  
5858 O OD1 . ASP B 310 ? 3.8166 4.0750 3.7644 0.8733  -0.1377 -0.0452 310 ASP B OD1 
5859 O OD2 . ASP B 310 ? 3.7141 3.8186 3.6014 0.8702  -0.1824 -0.0752 310 ASP B OD2 
5860 N N   . ALA B 311 ? 1.7738 2.0484 1.9205 0.6950  -0.1085 -0.0107 311 ALA B N   
5861 C CA  . ALA B 311 ? 1.7235 2.0422 1.9205 0.6654  -0.0931 0.0028  311 ALA B CA  
5862 C C   . ALA B 311 ? 1.7254 2.1038 1.9778 0.6323  -0.0731 0.0242  311 ALA B C   
5863 O O   . ALA B 311 ? 1.6490 2.1015 1.9353 0.6279  -0.0566 0.0411  311 ALA B O   
5864 C CB  . ALA B 311 ? 1.6289 1.8785 1.8293 0.6353  -0.1052 -0.0061 311 ALA B CB  
5865 N N   . VAL B 312 ? 1.6772 2.0204 1.9371 0.6090  -0.0768 0.0236  312 VAL B N   
5866 C CA  . VAL B 312 ? 1.7658 2.1513 2.0739 0.5760  -0.0615 0.0417  312 VAL B CA  
5867 C C   . VAL B 312 ? 1.9208 2.3868 2.2325 0.6002  -0.0478 0.0558  312 VAL B C   
5868 O O   . VAL B 312 ? 1.7586 2.2888 2.1141 0.5796  -0.0321 0.0758  312 VAL B O   
5869 C CB  . VAL B 312 ? 1.9610 2.2960 2.2786 0.5468  -0.0679 0.0393  312 VAL B CB  
5870 C CG1 . VAL B 312 ? 2.3162 2.7002 2.6625 0.5343  -0.0552 0.0555  312 VAL B CG1 
5871 C CG2 . VAL B 312 ? 2.1718 2.4674 2.5197 0.5049  -0.0689 0.0391  312 VAL B CG2 
5872 N N   . ARG B 313 ? 2.1292 2.5891 2.3925 0.6441  -0.0551 0.0457  313 ARG B N   
5873 C CA  . ARG B 313 ? 2.2623 2.7966 2.5200 0.6744  -0.0427 0.0578  313 ARG B CA  
5874 C C   . ARG B 313 ? 2.1396 2.7527 2.4205 0.6840  -0.0283 0.0725  313 ARG B C   
5875 O O   . ARG B 313 ? 2.2205 2.9136 2.5369 0.6754  -0.0117 0.0954  313 ARG B O   
5876 C CB  . ARG B 313 ? 2.1483 2.6513 2.3408 0.7245  -0.0553 0.0410  313 ARG B CB  
5877 C CG  . ARG B 313 ? 2.1668 2.7457 2.3444 0.7642  -0.0424 0.0516  313 ARG B CG  
5878 C CD  . ARG B 313 ? 2.6372 3.1949 2.7470 0.8248  -0.0539 0.0330  313 ARG B CD  
5879 N NE  . ARG B 313 ? 3.0458 3.5885 3.1455 0.8369  -0.0602 0.0236  313 ARG B NE  
5880 C CZ  . ARG B 313 ? 3.1394 3.6698 3.1865 0.8880  -0.0695 0.0087  313 ARG B CZ  
5881 N NH1 . ARG B 313 ? 3.2466 3.7889 3.2442 0.9383  -0.0710 0.0027  313 ARG B NH1 
5882 N NH2 . ARG B 313 ? 2.8937 3.4004 2.9365 0.8900  -0.0774 0.0001  313 ARG B NH2 
5883 N N   . ARG B 314 ? 1.9147 2.5026 2.1755 0.6999  -0.0366 0.0603  314 ARG B N   
5884 C CA  . ARG B 314 ? 2.0520 2.7081 2.3318 0.7110  -0.0259 0.0726  314 ARG B CA  
5885 C C   . ARG B 314 ? 2.0165 2.7183 2.3614 0.6612  -0.0128 0.0954  314 ARG B C   
5886 O O   . ARG B 314 ? 2.0246 2.8133 2.4015 0.6605  0.0015  0.1185  314 ARG B O   
5887 C CB  . ARG B 314 ? 2.1307 2.7487 2.3758 0.7374  -0.0384 0.0550  314 ARG B CB  
5888 C CG  . ARG B 314 ? 2.2078 2.8047 2.3876 0.7958  -0.0491 0.0374  314 ARG B CG  
5889 C CD  . ARG B 314 ? 1.9968 2.5497 2.1369 0.8244  -0.0643 0.0187  314 ARG B CD  
5890 N NE  . ARG B 314 ? 1.8919 2.3431 2.0136 0.8017  -0.0847 0.0000  314 ARG B NE  
5891 C CZ  . ARG B 314 ? 1.9476 2.3706 2.0878 0.7744  -0.0892 -0.0022 314 ARG B CZ  
5892 N NH1 . ARG B 314 ? 1.8024 2.2873 1.9833 0.7614  -0.0753 0.0132  314 ARG B NH1 
5893 N NH2 . ARG B 314 ? 2.1711 2.5040 2.2895 0.7583  -0.1083 -0.0185 314 ARG B NH2 
5894 N N   . THR B 315 ? 1.8711 2.5106 2.2331 0.6201  -0.0195 0.0890  315 THR B N   
5895 C CA  . THR B 315 ? 1.6766 2.3388 2.0932 0.5717  -0.0109 0.1063  315 THR B CA  
5896 C C   . THR B 315 ? 1.6105 2.3329 2.0596 0.5556  0.0013  0.1283  315 THR B C   
5897 O O   . THR B 315 ? 1.3071 2.0912 1.7959 0.5354  0.0111  0.1504  315 THR B O   
5898 C CB  . THR B 315 ? 1.7024 2.2842 2.1250 0.5362  -0.0200 0.0939  315 THR B CB  
5899 O OG1 . THR B 315 ? 1.8480 2.3710 2.2282 0.5601  -0.0340 0.0722  315 THR B OG1 
5900 C CG2 . THR B 315 ? 1.6130 2.2130 2.0808 0.4959  -0.0134 0.1078  315 THR B CG2 
5901 N N   . GLY B 316 ? 1.7415 2.4430 2.1722 0.5638  -0.0009 0.1227  316 GLY B N   
5902 C CA  . GLY B 316 ? 2.1018 2.8519 2.5569 0.5509  0.0088  0.1415  316 GLY B CA  
5903 C C   . GLY B 316 ? 2.2194 3.0665 2.6836 0.5742  0.0215  0.1624  316 GLY B C   
5904 O O   . GLY B 316 ? 2.5716 3.4790 3.0776 0.5483  0.0312  0.1873  316 GLY B O   
5905 N N   . GLU B 317 ? 2.1366 2.9965 2.5604 0.6235  0.0201  0.1525  317 GLU B N   
5906 C CA  . GLU B 317 ? 2.2996 3.2544 2.7264 0.6543  0.0327  0.1713  317 GLU B CA  
5907 C C   . GLU B 317 ? 2.1640 3.1786 2.6392 0.6282  0.0398  0.1937  317 GLU B C   
5908 O O   . GLU B 317 ? 2.3128 3.4130 2.8230 0.6182  0.0515  0.2226  317 GLU B O   
5909 C CB  . GLU B 317 ? 2.3657 3.3155 2.7352 0.7153  0.0288  0.1539  317 GLU B CB  
5910 C CG  . GLU B 317 ? 2.5376 3.4537 2.8632 0.7420  0.0241  0.1408  317 GLU B CG  
5911 C CD  . GLU B 317 ? 2.6696 3.5383 2.9269 0.7971  0.0120  0.1145  317 GLU B CD  
5912 O OE1 . GLU B 317 ? 2.4104 3.2746 2.6523 0.8189  0.0076  0.1057  317 GLU B OE1 
5913 O OE2 . GLU B 317 ? 3.0573 3.8892 3.2742 0.8185  0.0052  0.1024  317 GLU B OE2 
5914 N N   . VAL B 318 ? 1.8546 2.8200 2.3296 0.6164  0.0311  0.1806  318 VAL B N   
5915 C CA  . VAL B 318 ? 1.8488 2.8556 2.3632 0.5924  0.0342  0.1978  318 VAL B CA  
5916 C C   . VAL B 318 ? 1.9712 3.0026 2.5368 0.5400  0.0387  0.2212  318 VAL B C   
5917 O O   . VAL B 318 ? 1.8219 2.9288 2.4243 0.5257  0.0453  0.2487  318 VAL B O   
5918 C CB  . VAL B 318 ? 1.8162 2.7579 2.3172 0.5884  0.0231  0.1781  318 VAL B CB  
5919 C CG1 . VAL B 318 ? 1.6935 2.6697 2.2368 0.5566  0.0248  0.1963  318 VAL B CG1 
5920 C CG2 . VAL B 318 ? 1.6782 2.6100 2.1306 0.6425  0.0181  0.1597  318 VAL B CG2 
5921 N N   . LEU B 319 ? 1.7107 2.6758 2.2768 0.5126  0.0335  0.2102  319 LEU B N   
5922 C CA  . LEU B 319 ? 1.4391 2.4130 2.0478 0.4643  0.0354  0.2283  319 LEU B CA  
5923 C C   . LEU B 319 ? 1.4998 2.5545 2.1284 0.4647  0.0450  0.2550  319 LEU B C   
5924 O O   . LEU B 319 ? 1.3757 2.4785 2.0445 0.4332  0.0474  0.2808  319 LEU B O   
5925 C CB  . LEU B 319 ? 1.5791 2.4673 2.1882 0.4332  0.0281  0.2122  319 LEU B CB  
5926 C CG  . LEU B 319 ? 1.7341 2.5790 2.3568 0.4055  0.0222  0.2062  319 LEU B CG  
5927 C CD1 . LEU B 319 ? 2.5166 3.2793 3.1372 0.3798  0.0163  0.1898  319 LEU B CD1 
5928 C CD2 . LEU B 319 ? 1.5269 2.4287 2.1920 0.3749  0.0250  0.2337  319 LEU B CD2 
5929 N N   . SER B 320 ? 1.5216 2.5899 2.1199 0.5009  0.0491  0.2492  320 SER B N   
5930 C CA  . SER B 320 ? 1.6544 2.8016 2.2655 0.5073  0.0592  0.2739  320 SER B CA  
5931 C C   . SER B 320 ? 1.8472 3.0919 2.4844 0.5140  0.0673  0.3019  320 SER B C   
5932 O O   . SER B 320 ? 1.9539 3.2639 2.6287 0.4885  0.0723  0.3325  320 SER B O   
5933 C CB  . SER B 320 ? 1.6716 2.8122 2.2391 0.5496  0.0617  0.2607  320 SER B CB  
5934 O OG  . SER B 320 ? 1.9330 3.1484 2.5162 0.5497  0.0719  0.2865  320 SER B OG  
5935 N N   . GLY B 321 ? 1.9565 3.2086 2.5731 0.5479  0.0671  0.2916  321 GLY B N   
5936 C CA  . GLY B 321 ? 2.1880 3.5313 2.8273 0.5590  0.0740  0.3163  321 GLY B CA  
5937 C C   . GLY B 321 ? 2.2425 3.6059 2.9334 0.5063  0.0698  0.3397  321 GLY B C   
5938 O O   . GLY B 321 ? 2.8944 4.3441 3.6220 0.4918  0.0750  0.3739  321 GLY B O   
5939 N N   . LEU B 322 ? 1.8067 3.0862 2.4979 0.4779  0.0591  0.3211  322 LEU B N   
5940 C CA  . LEU B 322 ? 1.6279 2.9040 2.3590 0.4285  0.0520  0.3369  322 LEU B CA  
5941 C C   . LEU B 322 ? 1.5061 2.8128 2.2701 0.3913  0.0530  0.3623  322 LEU B C   
5942 O O   . LEU B 322 ? 1.3023 2.6640 2.1042 0.3618  0.0508  0.3926  322 LEU B O   
5943 C CB  . LEU B 322 ? 1.6246 2.8001 2.3439 0.4084  0.0417  0.3101  322 LEU B CB  
5944 C CG  . LEU B 322 ? 1.6234 2.7834 2.3331 0.4207  0.0366  0.2993  322 LEU B CG  
5945 C CD1 . LEU B 322 ? 1.3363 2.4839 2.0019 0.4741  0.0385  0.2762  322 LEU B CD1 
5946 C CD2 . LEU B 322 ? 1.7449 2.8224 2.4584 0.3850  0.0267  0.2848  322 LEU B CD2 
5947 N N   . GLY B 323 ? 1.4517 2.7264 2.1964 0.3985  0.0558  0.3501  323 GLY B N   
5948 C CA  . GLY B 323 ? 1.7319 3.0394 2.4974 0.3762  0.0585  0.3713  323 GLY B CA  
5949 C C   . GLY B 323 ? 1.8833 3.1080 2.6512 0.3414  0.0506  0.3574  323 GLY B C   
5950 O O   . GLY B 323 ? 1.6834 2.9218 2.4795 0.3054  0.0473  0.3773  323 GLY B O   
5951 N N   . HIS B 324 ? 2.1319 3.2709 2.8704 0.3518  0.0465  0.3240  324 HIS B N   
5952 C CA  . HIS B 324 ? 2.6601 3.7239 3.4007 0.3224  0.0401  0.3108  324 HIS B CA  
5953 C C   . HIS B 324 ? 2.9166 3.9693 3.6374 0.3386  0.0434  0.3033  324 HIS B C   
5954 O O   . HIS B 324 ? 3.0308 4.0758 3.7164 0.3783  0.0463  0.2869  324 HIS B O   
5955 C CB  . HIS B 324 ? 2.7698 3.7477 3.4936 0.3192  0.0334  0.2822  324 HIS B CB  
5956 C CG  . HIS B 324 ? 2.6179 3.5319 3.3537 0.2833  0.0276  0.2754  324 HIS B CG  
5957 N ND1 . HIS B 324 ? 2.4141 3.2506 3.1288 0.2864  0.0243  0.2494  324 HIS B ND1 
5958 C CD2 . HIS B 324 ? 2.4843 3.4038 3.2511 0.2444  0.0240  0.2931  324 HIS B CD2 
5959 C CE1 . HIS B 324 ? 2.5911 3.3914 3.3253 0.2517  0.0205  0.2513  324 HIS B CE1 
5960 N NE2 . HIS B 324 ? 2.7151 3.5620 3.4790 0.2266  0.0198  0.2766  324 HIS B NE2 
5961 N N   . ARG B 325 ? 2.9130 3.9627 3.6550 0.3076  0.0414  0.3156  325 ARG B N   
5962 C CA  . ARG B 325 ? 2.5988 3.6316 3.3256 0.3160  0.0427  0.3095  325 ARG B CA  
5963 C C   . ARG B 325 ? 2.2496 3.1983 2.9798 0.2883  0.0347  0.2926  325 ARG B C   
5964 O O   . ARG B 325 ? 2.2798 3.2073 3.0346 0.2542  0.0296  0.2976  325 ARG B O   
5965 C CB  . ARG B 325 ? 2.8895 4.0040 3.6358 0.3104  0.0483  0.3409  325 ARG B CB  
5966 C CG  . ARG B 325 ? 2.9997 4.1903 3.7316 0.3508  0.0583  0.3509  325 ARG B CG  
5967 C CD  . ARG B 325 ? 2.7328 4.0242 3.4936 0.3423  0.0647  0.3892  325 ARG B CD  
5968 N NE  . ARG B 325 ? 2.3456 3.6799 3.1418 0.3163  0.0616  0.4121  325 ARG B NE  
5969 C CZ  . ARG B 325 ? 2.0278 3.4556 2.8511 0.3096  0.0658  0.4477  325 ARG B CZ  
5970 N NH1 . ARG B 325 ? 1.8837 3.3783 2.7018 0.3306  0.0758  0.4646  325 ARG B NH1 
5971 N NH2 . ARG B 325 ? 1.9362 3.3915 2.7915 0.2816  0.0594  0.4675  325 ARG B NH2 
5972 N N   . GLY B 326 ? 1.9713 2.8709 2.6742 0.3054  0.0329  0.2720  326 GLY B N   
5973 C CA  . GLY B 326 ? 2.0285 2.8482 2.7321 0.2849  0.0257  0.2541  326 GLY B CA  
5974 C C   . GLY B 326 ? 1.7142 2.4727 2.3844 0.3091  0.0216  0.2253  326 GLY B C   
5975 O O   . GLY B 326 ? 1.6171 2.3756 2.2542 0.3438  0.0215  0.2150  326 GLY B O   
5976 N N   . ALA B 327 ? 1.3844 2.0912 2.0619 0.2906  0.0174  0.2138  327 ALA B N   
5977 C CA  . ALA B 327 ? 1.3772 2.0159 2.0285 0.3033  0.0114  0.1884  327 ALA B CA  
5978 C C   . ALA B 327 ? 1.4626 2.0844 2.1150 0.2994  0.0105  0.1816  327 ALA B C   
5979 O O   . ALA B 327 ? 1.5124 2.1422 2.1911 0.2727  0.0121  0.1917  327 ALA B O   
5980 C CB  . ALA B 327 ? 1.7002 2.2824 2.3591 0.2820  0.0064  0.1803  327 ALA B CB  
5981 N N   . PHE B 328 ? 1.4994 2.0895 2.1188 0.3265  0.0060  0.1631  328 PHE B N   
5982 C CA  . PHE B 328 ? 1.5322 2.0968 2.1443 0.3278  0.0035  0.1529  328 PHE B CA  
5983 C C   . PHE B 328 ? 1.4100 1.8988 1.9960 0.3342  -0.0056 0.1301  328 PHE B C   
5984 O O   . PHE B 328 ? 1.2619 1.7220 1.8227 0.3516  -0.0122 0.1193  328 PHE B O   
5985 C CB  . PHE B 328 ? 1.9013 2.5190 2.5017 0.3554  0.0066  0.1584  328 PHE B CB  
5986 C CG  . PHE B 328 ? 2.2830 2.8983 2.8418 0.3984  0.0030  0.1459  328 PHE B CG  
5987 C CD1 . PHE B 328 ? 2.6220 3.1801 3.1456 0.4182  -0.0067 0.1239  328 PHE B CD1 
5988 C CD2 . PHE B 328 ? 2.1696 2.8347 2.7216 0.4186  0.0078  0.1560  328 PHE B CD2 
5989 C CE1 . PHE B 328 ? 2.7431 3.2900 3.2235 0.4580  -0.0131 0.1113  328 PHE B CE1 
5990 C CE2 . PHE B 328 ? 2.3144 2.9712 2.8229 0.4603  0.0035  0.1431  328 PHE B CE2 
5991 C CZ  . PHE B 328 ? 2.5104 3.1057 2.9819 0.4803  -0.0078 0.1202  328 PHE B CZ  
5992 N N   . GLY B 329 ? 1.4314 1.8876 2.0216 0.3205  -0.0073 0.1234  329 GLY B N   
5993 C CA  . GLY B 329 ? 1.4943 1.8821 2.0637 0.3218  -0.0160 0.1049  329 GLY B CA  
5994 C C   . GLY B 329 ? 1.4172 1.7957 1.9684 0.3353  -0.0193 0.0967  329 GLY B C   
5995 O O   . GLY B 329 ? 1.1901 1.5959 1.7584 0.3246  -0.0138 0.1053  329 GLY B O   
5996 N N   . VAL B 330 ? 1.5956 1.9305 2.1102 0.3579  -0.0303 0.0801  330 VAL B N   
5997 C CA  . VAL B 330 ? 1.7563 2.0664 2.2485 0.3700  -0.0367 0.0694  330 VAL B CA  
5998 C C   . VAL B 330 ? 1.9060 2.1424 2.3842 0.3588  -0.0473 0.0558  330 VAL B C   
5999 O O   . VAL B 330 ? 1.5548 1.7562 2.0142 0.3664  -0.0569 0.0481  330 VAL B O   
6000 C CB  . VAL B 330 ? 1.6105 1.9388 2.0655 0.4128  -0.0428 0.0626  330 VAL B CB  
6001 C CG1 . VAL B 330 ? 1.4067 1.7265 1.8468 0.4233  -0.0469 0.0560  330 VAL B CG1 
6002 C CG2 . VAL B 330 ? 1.5144 1.9164 1.9792 0.4287  -0.0329 0.0767  330 VAL B CG2 
6003 N N   . ASP B 331 ? 1.9518 2.1681 2.4415 0.3386  -0.0451 0.0551  331 ASP B N   
6004 C CA  . ASP B 331 ? 1.7072 1.8604 2.1852 0.3271  -0.0539 0.0449  331 ASP B CA  
6005 C C   . ASP B 331 ? 1.6066 1.7379 2.0498 0.3490  -0.0646 0.0338  331 ASP B C   
6006 O O   . ASP B 331 ? 1.4278 1.5904 1.8705 0.3585  -0.0607 0.0362  331 ASP B O   
6007 C CB  . ASP B 331 ? 1.8709 2.0123 2.3813 0.2914  -0.0445 0.0513  331 ASP B CB  
6008 C CG  . ASP B 331 ? 1.7989 1.8810 2.3039 0.2760  -0.0511 0.0444  331 ASP B CG  
6009 O OD1 . ASP B 331 ? 1.8041 1.8523 2.2854 0.2878  -0.0643 0.0366  331 ASP B OD1 
6010 O OD2 . ASP B 331 ? 1.5750 1.6449 2.0977 0.2529  -0.0438 0.0474  331 ASP B OD2 
6011 N N   . PHE B 332 ? 1.7164 1.7911 2.1309 0.3554  -0.0800 0.0224  332 PHE B N   
6012 C CA  . PHE B 332 ? 1.9040 1.9444 2.2789 0.3770  -0.0951 0.0102  332 PHE B CA  
6013 C C   . PHE B 332 ? 2.0300 2.0092 2.3983 0.3564  -0.1047 0.0051  332 PHE B C   
6014 O O   . PHE B 332 ? 2.0541 2.0081 2.4399 0.3313  -0.1038 0.0089  332 PHE B O   
6015 C CB  . PHE B 332 ? 1.7504 1.7731 2.0850 0.4101  -0.1110 0.0006  332 PHE B CB  
6016 C CG  . PHE B 332 ? 1.9261 2.0054 2.2584 0.4367  -0.1036 0.0046  332 PHE B CG  
6017 C CD1 . PHE B 332 ? 1.8311 1.9544 2.1537 0.4628  -0.0990 0.0052  332 PHE B CD1 
6018 C CD2 . PHE B 332 ? 2.2227 2.3128 2.5620 0.4363  -0.1016 0.0088  332 PHE B CD2 
6019 C CE1 . PHE B 332 ? 1.7242 1.9043 2.0453 0.4879  -0.0914 0.0109  332 PHE B CE1 
6020 C CE2 . PHE B 332 ? 2.1897 2.3333 2.5253 0.4611  -0.0945 0.0136  332 PHE B CE2 
6021 C CZ  . PHE B 332 ? 1.7593 1.9492 2.0858 0.4872  -0.0890 0.0151  332 PHE B CZ  
6022 N N   . VAL B 333 ? 1.8324 1.7875 2.1718 0.3700  -0.1153 -0.0032 333 VAL B N   
6023 C CA  . VAL B 333 ? 1.7747 1.6685 2.0952 0.3586  -0.1296 -0.0092 333 VAL B CA  
6024 C C   . VAL B 333 ? 2.0453 1.8999 2.3136 0.3901  -0.1534 -0.0224 333 VAL B C   
6025 O O   . VAL B 333 ? 2.1364 2.0130 2.3816 0.4224  -0.1564 -0.0283 333 VAL B O   
6026 C CB  . VAL B 333 ? 1.5917 1.4809 1.9282 0.3357  -0.1209 -0.0056 333 VAL B CB  
6027 C CG1 . VAL B 333 ? 1.9854 1.8976 2.3671 0.3038  -0.1012 0.0059  333 VAL B CG1 
6028 C CG2 . VAL B 333 ? 1.7344 1.6554 2.0638 0.3530  -0.1169 -0.0074 333 VAL B CG2 
6029 N N   . VAL B 334 ? 2.2866 2.0793 2.5356 0.3792  -0.1717 -0.0261 334 VAL B N   
6030 C CA  . VAL B 334 ? 2.1951 1.9340 2.3912 0.4029  -0.1992 -0.0383 334 VAL B CA  
6031 C C   . VAL B 334 ? 2.2902 1.9905 2.4754 0.3888  -0.2077 -0.0400 334 VAL B C   
6032 O O   . VAL B 334 ? 2.1687 1.8444 2.3724 0.3566  -0.2068 -0.0327 334 VAL B O   
6033 C CB  . VAL B 334 ? 1.8968 1.5898 2.0717 0.4038  -0.2198 -0.0407 334 VAL B CB  
6034 C CG1 . VAL B 334 ? 1.6685 1.2926 1.7881 0.4206  -0.2525 -0.0517 334 VAL B CG1 
6035 C CG2 . VAL B 334 ? 1.9103 1.6365 2.0837 0.4258  -0.2151 -0.0417 334 VAL B CG2 
6036 N N   . ALA B 335 ? 2.4854 2.1818 2.6398 0.4141  -0.2158 -0.0490 335 ALA B N   
6037 C CA  . ALA B 335 ? 2.7925 2.4766 2.9479 0.4009  -0.2145 -0.0485 335 ALA B CA  
6038 C C   . ALA B 335 ? 3.1136 2.7323 3.2174 0.4151  -0.2444 -0.0591 335 ALA B C   
6039 O O   . ALA B 335 ? 3.2985 2.9172 3.3729 0.4434  -0.2525 -0.0682 335 ALA B O   
6040 C CB  . ALA B 335 ? 2.6423 2.3850 2.8145 0.4129  -0.1959 -0.0472 335 ALA B CB  
6041 N N   . GLY B 336 ? 3.1052 2.6691 3.1991 0.3945  -0.2615 -0.0564 336 GLY B N   
6042 C CA  . GLY B 336 ? 3.2361 2.7302 3.2795 0.4040  -0.2943 -0.0645 336 GLY B CA  
6043 C C   . GLY B 336 ? 3.3890 2.8695 3.3832 0.4502  -0.3137 -0.0792 336 GLY B C   
6044 O O   . GLY B 336 ? 3.7039 3.1939 3.6939 0.4646  -0.3152 -0.0810 336 GLY B O   
6045 N N   . GLU B 337 ? 3.4229 2.8824 3.3789 0.4750  -0.3281 -0.0897 337 GLU B N   
6046 C CA  . GLU B 337 ? 3.5571 2.9998 3.4605 0.5232  -0.3478 -0.1049 337 GLU B CA  
6047 C C   . GLU B 337 ? 3.3806 2.8988 3.2990 0.5531  -0.3239 -0.1073 337 GLU B C   
6048 O O   . GLU B 337 ? 3.4889 3.0114 3.3704 0.5969  -0.3333 -0.1183 337 GLU B O   
6049 C CB  . GLU B 337 ? 3.7591 3.1303 3.6061 0.5376  -0.3815 -0.1156 337 GLU B CB  
6050 C CG  . GLU B 337 ? 4.0058 3.2998 3.8320 0.5111  -0.4105 -0.1119 337 GLU B CG  
6051 C CD  . GLU B 337 ? 4.1128 3.3267 3.8699 0.5342  -0.4520 -0.1245 337 GLU B CD  
6052 O OE1 . GLU B 337 ? 3.9630 3.1626 3.7005 0.5430  -0.4590 -0.1300 337 GLU B OE1 
6053 O OE2 . GLU B 337 ? 4.2181 3.3811 3.9393 0.5430  -0.4790 -0.1286 337 GLU B OE2 
6054 N N   . ARG B 338 ? 2.9580 2.5360 2.9301 0.5294  -0.2937 -0.0959 338 ARG B N   
6055 C CA  . ARG B 338 ? 2.5027 2.1555 2.4952 0.5507  -0.2713 -0.0942 338 ARG B CA  
6056 C C   . ARG B 338 ? 2.4070 2.1079 2.4113 0.5686  -0.2586 -0.0918 338 ARG B C   
6057 O O   . ARG B 338 ? 2.1088 1.8687 2.1178 0.5967  -0.2458 -0.0914 338 ARG B O   
6058 C CB  . ARG B 338 ? 2.2297 1.9234 2.2735 0.5162  -0.2465 -0.0817 338 ARG B CB  
6059 C CG  . ARG B 338 ? 2.0942 1.8660 2.1612 0.5349  -0.2257 -0.0772 338 ARG B CG  
6060 C CD  . ARG B 338 ? 2.1626 1.9617 2.2740 0.4989  -0.2062 -0.0655 338 ARG B CD  
6061 N NE  . ARG B 338 ? 2.2172 2.0940 2.3588 0.5085  -0.1861 -0.0570 338 ARG B NE  
6062 C CZ  . ARG B 338 ? 2.3419 2.2519 2.5216 0.4819  -0.1691 -0.0460 338 ARG B CZ  
6063 N NH1 . ARG B 338 ? 2.4789 2.3527 2.6693 0.4472  -0.1679 -0.0434 338 ARG B NH1 
6064 N NH2 . ARG B 338 ? 2.2589 2.2385 2.4642 0.4909  -0.1543 -0.0368 338 ARG B NH2 
6065 N N   . GLY B 339 ? 2.4915 2.1686 2.5016 0.5512  -0.2625 -0.0887 339 GLY B N   
6066 C CA  . GLY B 339 ? 2.6439 2.3531 2.6590 0.5663  -0.2551 -0.0872 339 GLY B CA  
6067 C C   . GLY B 339 ? 2.7271 2.4922 2.8038 0.5333  -0.2264 -0.0716 339 GLY B C   
6068 O O   . GLY B 339 ? 2.5290 2.2853 2.6397 0.4932  -0.2182 -0.0629 339 GLY B O   
6069 N N   . LEU B 340 ? 2.7587 2.5862 2.8492 0.5527  -0.2103 -0.0675 340 LEU B N   
6070 C CA  . LEU B 340 ? 2.5658 2.4417 2.7061 0.5276  -0.1877 -0.0538 340 LEU B CA  
6071 C C   . LEU B 340 ? 2.5666 2.5225 2.7442 0.5279  -0.1629 -0.0429 340 LEU B C   
6072 O O   . LEU B 340 ? 2.5319 2.5270 2.6934 0.5630  -0.1608 -0.0450 340 LEU B O   
6073 C CB  . LEU B 340 ? 2.2996 2.1731 2.4251 0.5432  -0.1930 -0.0557 340 LEU B CB  
6074 C CG  . LEU B 340 ? 2.2321 2.1464 2.4057 0.5162  -0.1732 -0.0421 340 LEU B CG  
6075 C CD1 . LEU B 340 ? 2.1159 1.9827 2.2754 0.5093  -0.1880 -0.0449 340 LEU B CD1 
6076 C CD2 . LEU B 340 ? 2.2073 2.1999 2.3973 0.5362  -0.1541 -0.0344 340 LEU B CD2 
6077 N N   . LEU B 341 ? 2.4781 2.4545 2.7030 0.4890  -0.1460 -0.0309 341 LEU B N   
6078 C CA  . LEU B 341 ? 2.2331 2.2732 2.4937 0.4809  -0.1264 -0.0194 341 LEU B CA  
6079 C C   . LEU B 341 ? 2.1442 2.2232 2.4523 0.4515  -0.1075 -0.0049 341 LEU B C   
6080 O O   . LEU B 341 ? 1.7793 1.8278 2.1048 0.4213  -0.1061 -0.0026 341 LEU B O   
6081 C CB  . LEU B 341 ? 2.3307 2.3485 2.5950 0.4632  -0.1278 -0.0204 341 LEU B CB  
6082 C CG  . LEU B 341 ? 2.4672 2.4258 2.6849 0.4812  -0.1499 -0.0349 341 LEU B CG  
6083 C CD1 . LEU B 341 ? 2.2477 2.1793 2.4751 0.4536  -0.1495 -0.0335 341 LEU B CD1 
6084 C CD2 . LEU B 341 ? 2.7823 2.7642 2.9682 0.5259  -0.1571 -0.0420 341 LEU B CD2 
6085 N N   . ALA B 342 ? 2.0479 2.1966 2.3761 0.4619  -0.0939 0.0056  342 ALA B N   
6086 C CA  . ALA B 342 ? 1.8579 2.0511 2.2301 0.4369  -0.0771 0.0210  342 ALA B CA  
6087 C C   . ALA B 342 ? 1.7929 1.9990 2.1985 0.4052  -0.0669 0.0306  342 ALA B C   
6088 O O   . ALA B 342 ? 1.6387 1.8706 2.0448 0.4128  -0.0656 0.0334  342 ALA B O   
6089 C CB  . ALA B 342 ? 1.4628 1.7250 1.8394 0.4619  -0.0690 0.0299  342 ALA B CB  
6090 N N   . VAL B 343 ? 1.7656 1.9558 2.1990 0.3707  -0.0599 0.0361  343 VAL B N   
6091 C CA  . VAL B 343 ? 1.6112 1.7935 2.0680 0.3399  -0.0531 0.0417  343 VAL B CA  
6092 C C   . VAL B 343 ? 1.7775 2.0051 2.2743 0.3169  -0.0394 0.0580  343 VAL B C   
6093 O O   . VAL B 343 ? 2.0969 2.3438 2.6114 0.3015  -0.0341 0.0664  343 VAL B O   
6094 C CB  . VAL B 343 ? 1.2012 1.3183 1.6519 0.3196  -0.0578 0.0338  343 VAL B CB  
6095 C CG1 . VAL B 343 ? 1.1379 1.2052 1.5480 0.3394  -0.0747 0.0193  343 VAL B CG1 
6096 C CG2 . VAL B 343 ? 1.2471 1.3575 1.7168 0.3036  -0.0531 0.0377  343 VAL B CG2 
6097 N N   . GLU B 344 ? 1.5897 1.8315 2.0975 0.3159  -0.0358 0.0623  344 GLU B N   
6098 C CA  . GLU B 344 ? 1.6431 1.9227 2.1860 0.2946  -0.0252 0.0774  344 GLU B CA  
6099 C C   . GLU B 344 ? 1.5005 1.8311 2.0470 0.3125  -0.0226 0.0855  344 GLU B C   
6100 O O   . GLU B 344 ? 1.2369 1.5598 1.7612 0.3356  -0.0279 0.0778  344 GLU B O   
6101 C CB  . GLU B 344 ? 2.0642 2.3082 2.6264 0.2637  -0.0209 0.0782  344 GLU B CB  
6102 C CG  . GLU B 344 ? 2.5413 2.7696 3.1158 0.2395  -0.0170 0.0810  344 GLU B CG  
6103 C CD  . GLU B 344 ? 2.9972 3.2220 3.5999 0.2106  -0.0093 0.0895  344 GLU B CD  
6104 O OE1 . GLU B 344 ? 3.0830 3.3504 3.7062 0.2034  -0.0056 0.1028  344 GLU B OE1 
6105 O OE2 . GLU B 344 ? 3.3250 3.5065 3.9295 0.1958  -0.0074 0.0839  344 GLU B OE2 
6106 N N   . ILE B 345 ? 1.5267 1.9094 2.1025 0.2987  -0.0147 0.1029  345 ILE B N   
6107 C CA  . ILE B 345 ? 1.4788 1.9143 2.0679 0.3050  -0.0099 0.1158  345 ILE B CA  
6108 C C   . ILE B 345 ? 1.5441 1.9865 2.1668 0.2712  -0.0043 0.1288  345 ILE B C   
6109 O O   . ILE B 345 ? 1.5603 2.0043 2.2019 0.2472  -0.0027 0.1369  345 ILE B O   
6110 C CB  . ILE B 345 ? 1.5569 2.0615 2.1501 0.3226  -0.0071 0.1291  345 ILE B CB  
6111 C CG1 . ILE B 345 ? 1.6516 2.1980 2.2351 0.3497  -0.0048 0.1332  345 ILE B CG1 
6112 C CG2 . ILE B 345 ? 1.6725 2.2158 2.3012 0.2933  -0.0028 0.1495  345 ILE B CG2 
6113 C CD1 . ILE B 345 ? 1.6882 2.2034 2.2294 0.3863  -0.0120 0.1140  345 ILE B CD1 
6114 N N   . ASN B 346 ? 1.4827 1.9295 2.1100 0.2714  -0.0027 0.1310  346 ASN B N   
6115 C CA  . ASN B 346 ? 1.3027 1.7527 1.9586 0.2426  0.0010  0.1422  346 ASN B CA  
6116 C C   . ASN B 346 ? 1.2640 1.7737 1.9329 0.2471  0.0044  0.1588  346 ASN B C   
6117 O O   . ASN B 346 ? 1.0718 1.5914 1.7232 0.2713  0.0038  0.1544  346 ASN B O   
6118 C CB  . ASN B 346 ? 1.5247 1.9171 2.1768 0.2337  -0.0008 0.1298  346 ASN B CB  
6119 C CG  . ASN B 346 ? 1.9387 2.2750 2.5805 0.2265  -0.0034 0.1161  346 ASN B CG  
6120 O OD1 . ASN B 346 ? 2.6691 2.9936 3.3249 0.2049  -0.0006 0.1196  346 ASN B OD1 
6121 N ND2 . ASN B 346 ? 1.8011 2.1006 2.4165 0.2440  -0.0096 0.1013  346 ASN B ND2 
6122 N N   . LEU B 347 ? 1.3499 1.8986 2.0459 0.2255  0.0066  0.1781  347 LEU B N   
6123 C CA  . LEU B 347 ? 1.6308 2.2390 2.3429 0.2245  0.0093  0.1976  347 LEU B CA  
6124 C C   . LEU B 347 ? 1.6767 2.2614 2.4064 0.1988  0.0088  0.2013  347 LEU B C   
6125 O O   . LEU B 347 ? 1.7957 2.3844 2.5476 0.1710  0.0070  0.2139  347 LEU B O   
6126 C CB  . LEU B 347 ? 2.0475 2.7136 2.7789 0.2149  0.0094  0.2190  347 LEU B CB  
6127 C CG  . LEU B 347 ? 2.2897 2.9913 3.0072 0.2421  0.0103  0.2188  347 LEU B CG  
6128 C CD1 . LEU B 347 ? 2.4036 3.1769 3.1470 0.2304  0.0103  0.2465  347 LEU B CD1 
6129 C CD2 . LEU B 347 ? 2.2217 2.9369 2.9117 0.2817  0.0133  0.2086  347 LEU B CD2 
6130 N N   . ARG B 348 ? 1.8064 2.3596 2.5234 0.2088  0.0086  0.1888  348 ARG B N   
6131 C CA  . ARG B 348 ? 1.8479 2.3676 2.5782 0.1880  0.0075  0.1878  348 ARG B CA  
6132 C C   . ARG B 348 ? 2.0504 2.5336 2.7597 0.2064  0.0054  0.1712  348 ARG B C   
6133 O O   . ARG B 348 ? 2.2040 2.6790 2.8868 0.2324  0.0035  0.1593  348 ARG B O   
6134 C CB  . ARG B 348 ? 1.5986 2.0745 2.3421 0.1612  0.0064  0.1842  348 ARG B CB  
6135 C CG  . ARG B 348 ? 1.6929 2.1198 2.4194 0.1674  0.0060  0.1659  348 ARG B CG  
6136 C CD  . ARG B 348 ? 1.6433 2.0299 2.3808 0.1428  0.0063  0.1633  348 ARG B CD  
6137 N NE  . ARG B 348 ? 1.7030 2.0459 2.4241 0.1483  0.0066  0.1475  348 ARG B NE  
6138 C CZ  . ARG B 348 ? 1.5596 1.8662 2.2648 0.1606  0.0055  0.1328  348 ARG B CZ  
6139 N NH1 . ARG B 348 ? 1.2898 1.5948 1.9910 0.1708  0.0035  0.1300  348 ARG B NH1 
6140 N NH2 . ARG B 348 ? 1.5565 1.8266 2.2489 0.1613  0.0052  0.1218  348 ARG B NH2 
6141 N N   . LYS B 349 ? 2.1454 2.6054 2.8654 0.1928  0.0042  0.1710  349 LYS B N   
6142 C CA  . LYS B 349 ? 1.7080 2.1248 2.4112 0.2042  0.0000  0.1560  349 LYS B CA  
6143 C C   . LYS B 349 ? 1.6060 1.9697 2.3019 0.2003  -0.0019 0.1411  349 LYS B C   
6144 O O   . LYS B 349 ? 1.4850 1.8420 2.1925 0.1846  0.0011  0.1429  349 LYS B O   
6145 C CB  . LYS B 349 ? 1.6510 2.0617 2.3714 0.1888  -0.0011 0.1622  349 LYS B CB  
6146 C CG  . LYS B 349 ? 1.5667 2.0318 2.2952 0.1899  0.0006  0.1792  349 LYS B CG  
6147 C CD  . LYS B 349 ? 1.7789 2.2347 2.5256 0.1718  -0.0014 0.1857  349 LYS B CD  
6148 C CE  . LYS B 349 ? 1.7686 2.2779 2.5255 0.1683  -0.0001 0.2049  349 LYS B CE  
6149 N NZ  . LYS B 349 ? 1.7123 2.2631 2.4470 0.1969  0.0018  0.2075  349 LYS B NZ  
6150 N N   . VAL B 350 ? 1.5393 1.8658 2.2127 0.2157  -0.0081 0.1271  350 VAL B N   
6151 C CA  . VAL B 350 ? 1.5008 1.7803 2.1665 0.2117  -0.0106 0.1150  350 VAL B CA  
6152 C C   . VAL B 350 ? 1.3685 1.6052 2.0389 0.2025  -0.0153 0.1096  350 VAL B C   
6153 O O   . VAL B 350 ? 1.3076 1.5483 1.9773 0.2070  -0.0192 0.1117  350 VAL B O   
6154 C CB  . VAL B 350 ? 1.8846 2.1559 2.5169 0.2379  -0.0165 0.1041  350 VAL B CB  
6155 C CG1 . VAL B 350 ? 2.0423 2.2752 2.6697 0.2303  -0.0175 0.0953  350 VAL B CG1 
6156 C CG2 . VAL B 350 ? 2.4478 2.7739 3.0746 0.2540  -0.0125 0.1117  350 VAL B CG2 
6157 N N   . GLY B 351 ? 1.3427 1.5413 2.0190 0.1891  -0.0147 0.1039  351 GLY B N   
6158 C CA  . GLY B 351 ? 1.5385 1.7004 2.2239 0.1783  -0.0185 0.1013  351 GLY B CA  
6159 C C   . GLY B 351 ? 1.6887 1.8437 2.3588 0.1926  -0.0291 0.0987  351 GLY B C   
6160 O O   . GLY B 351 ? 1.9510 2.1148 2.6366 0.1855  -0.0290 0.1050  351 GLY B O   
6161 N N   . PRO B 352 ? 1.5123 1.6495 2.1490 0.2140  -0.0399 0.0892  352 PRO B N   
6162 C CA  . PRO B 352 ? 1.4982 1.6156 2.1149 0.2273  -0.0532 0.0850  352 PRO B CA  
6163 C C   . PRO B 352 ? 1.4423 1.5936 2.0589 0.2363  -0.0521 0.0914  352 PRO B C   
6164 O O   . PRO B 352 ? 1.3772 1.5078 1.9811 0.2430  -0.0632 0.0889  352 PRO B O   
6165 C CB  . PRO B 352 ? 1.4979 1.5934 2.0746 0.2508  -0.0642 0.0736  352 PRO B CB  
6166 C CG  . PRO B 352 ? 1.6005 1.7276 2.1785 0.2550  -0.0533 0.0746  352 PRO B CG  
6167 C CD  . PRO B 352 ? 1.3997 1.5262 2.0143 0.2254  -0.0419 0.0813  352 PRO B CD  
6168 N N   . SER B 353 ? 1.3473 1.5477 1.9768 0.2358  -0.0405 0.1002  353 SER B N   
6169 C CA  . SER B 353 ? 1.4014 1.6397 2.0282 0.2461  -0.0391 0.1079  353 SER B CA  
6170 C C   . SER B 353 ? 1.3573 1.5833 2.0034 0.2302  -0.0421 0.1132  353 SER B C   
6171 O O   . SER B 353 ? 1.1712 1.3923 1.8014 0.2421  -0.0503 0.1122  353 SER B O   
6172 C CB  . SER B 353 ? 1.6038 1.8974 2.2480 0.2415  -0.0268 0.1201  353 SER B CB  
6173 O OG  . SER B 353 ? 1.7074 2.0008 2.3865 0.2120  -0.0197 0.1277  353 SER B OG  
6174 N N   . HIS B 354 ? 1.4313 1.6505 2.1109 0.2036  -0.0356 0.1184  354 HIS B N   
6175 C CA  . HIS B 354 ? 1.2123 1.4209 1.9157 0.1861  -0.0372 0.1242  354 HIS B CA  
6176 C C   . HIS B 354 ? 1.1080 1.2713 1.7985 0.1903  -0.0505 0.1163  354 HIS B C   
6177 O O   . HIS B 354 ? 0.9996 1.1587 1.6905 0.1906  -0.0574 0.1192  354 HIS B O   
6178 C CB  . HIS B 354 ? 1.1930 1.4048 1.9317 0.1602  -0.0276 0.1314  354 HIS B CB  
6179 C CG  . HIS B 354 ? 1.1616 1.3337 1.9127 0.1475  -0.0279 0.1261  354 HIS B CG  
6180 N ND1 . HIS B 354 ? 1.3180 1.4743 2.0632 0.1471  -0.0245 0.1199  354 HIS B ND1 
6181 C CD2 . HIS B 354 ? 1.2008 1.3491 1.9705 0.1350  -0.0307 0.1275  354 HIS B CD2 
6182 C CE1 . HIS B 354 ? 1.4060 1.5311 2.1655 0.1349  -0.0246 0.1181  354 HIS B CE1 
6183 N NE2 . HIS B 354 ? 1.4957 1.6169 2.2714 0.1276  -0.0282 0.1230  354 HIS B NE2 
6184 N N   . VAL B 355 ? 1.1091 1.2391 1.7872 0.1929  -0.0554 0.1074  355 VAL B N   
6185 C CA  . VAL B 355 ? 1.3905 1.4748 2.0553 0.1949  -0.0707 0.1013  355 VAL B CA  
6186 C C   . VAL B 355 ? 1.2357 1.3138 1.8644 0.2184  -0.0846 0.0966  355 VAL B C   
6187 O O   . VAL B 355 ? 1.2019 1.2563 1.8270 0.2170  -0.0971 0.0972  355 VAL B O   
6188 C CB  . VAL B 355 ? 1.3808 1.4354 2.0351 0.1943  -0.0735 0.0940  355 VAL B CB  
6189 C CG1 . VAL B 355 ? 1.2014 1.2071 1.8356 0.1975  -0.0931 0.0886  355 VAL B CG1 
6190 C CG2 . VAL B 355 ? 1.2982 1.3576 1.9862 0.1721  -0.0593 0.0988  355 VAL B CG2 
6191 N N   . VAL B 356 ? 1.1506 1.2509 1.7514 0.2414  -0.0825 0.0923  356 VAL B N   
6192 C CA  . VAL B 356 ? 1.4549 1.5531 2.0145 0.2702  -0.0937 0.0865  356 VAL B CA  
6193 C C   . VAL B 356 ? 1.4066 1.5262 1.9751 0.2683  -0.0927 0.0947  356 VAL B C   
6194 O O   . VAL B 356 ? 1.3666 1.4593 1.9081 0.2813  -0.1079 0.0902  356 VAL B O   
6195 C CB  . VAL B 356 ? 1.7392 1.8700 2.2727 0.2963  -0.0874 0.0828  356 VAL B CB  
6196 C CG1 . VAL B 356 ? 1.5259 1.6688 2.0217 0.3268  -0.0943 0.0801  356 VAL B CG1 
6197 C CG2 . VAL B 356 ? 1.9052 2.0061 2.4171 0.3052  -0.0936 0.0719  356 VAL B CG2 
6198 N N   . ARG B 357 ? 1.3798 1.5430 1.9826 0.2523  -0.0772 0.1066  357 ARG B N   
6199 C CA  . ARG B 357 ? 1.2566 1.4420 1.8695 0.2483  -0.0762 0.1160  357 ARG B CA  
6200 C C   . ARG B 357 ? 1.1383 1.2819 1.7592 0.2356  -0.0893 0.1153  357 ARG B C   
6201 O O   . ARG B 357 ? 0.9231 1.0578 1.5252 0.2459  -0.0999 0.1152  357 ARG B O   
6202 C CB  . ARG B 357 ? 1.2461 1.4758 1.8973 0.2275  -0.0608 0.1298  357 ARG B CB  
6203 C CG  . ARG B 357 ? 1.4703 1.7511 2.1087 0.2442  -0.0512 0.1346  357 ARG B CG  
6204 C CD  . ARG B 357 ? 2.1774 2.5069 2.8442 0.2283  -0.0410 0.1515  357 ARG B CD  
6205 N NE  . ARG B 357 ? 2.6921 3.0514 3.3448 0.2413  -0.0423 0.1592  357 ARG B NE  
6206 C CZ  . ARG B 357 ? 3.1128 3.4689 3.7761 0.2304  -0.0465 0.1659  357 ARG B CZ  
6207 N NH1 . ARG B 357 ? 3.4077 3.7246 4.0921 0.2100  -0.0524 0.1635  357 ARG B NH1 
6208 N NH2 . ARG B 357 ? 3.1495 3.5433 3.8013 0.2415  -0.0450 0.1756  357 ARG B NH2 
6209 N N   . TYR B 358 ? 1.1241 1.2436 1.7733 0.2134  -0.0882 0.1154  358 TYR B N   
6210 C CA  . TYR B 358 ? 1.2579 1.3416 1.9232 0.1977  -0.0991 0.1171  358 TYR B CA  
6211 C C   . TYR B 358 ? 1.3385 1.3791 1.9657 0.2139  -0.1206 0.1085  358 TYR B C   
6212 O O   . TYR B 358 ? 1.1386 1.1605 1.7621 0.2125  -0.1335 0.1108  358 TYR B O   
6213 C CB  . TYR B 358 ? 1.2775 1.3403 1.9760 0.1745  -0.0959 0.1189  358 TYR B CB  
6214 C CG  . TYR B 358 ? 1.4478 1.5329 2.1900 0.1520  -0.0809 0.1282  358 TYR B CG  
6215 C CD1 . TYR B 358 ? 1.4556 1.5626 2.2101 0.1464  -0.0656 0.1291  358 TYR B CD1 
6216 C CD2 . TYR B 358 ? 1.4715 1.5515 2.2412 0.1368  -0.0836 0.1356  358 TYR B CD2 
6217 C CE1 . TYR B 358 ? 1.5553 1.6765 2.3444 0.1276  -0.0542 0.1365  358 TYR B CE1 
6218 C CE2 . TYR B 358 ? 1.3858 1.4820 2.1916 0.1188  -0.0713 0.1430  358 TYR B CE2 
6219 C CZ  . TYR B 358 ? 1.4194 1.5348 2.2336 0.1145  -0.0569 0.1431  358 TYR B CZ  
6220 O OH  . TYR B 358 ? 1.3183 1.4444 2.1627 0.0984  -0.0465 0.1494  358 TYR B OH  
6221 N N   . ALA B 359 ? 1.5347 1.5571 2.1323 0.2291  -0.1258 0.0989  359 ALA B N   
6222 C CA  . ALA B 359 ? 1.5114 1.4864 2.0664 0.2460  -0.1487 0.0895  359 ALA B CA  
6223 C C   . ALA B 359 ? 1.4625 1.4415 1.9820 0.2695  -0.1577 0.0871  359 ALA B C   
6224 O O   . ALA B 359 ? 1.4168 1.3570 1.9160 0.2730  -0.1780 0.0850  359 ALA B O   
6225 C CB  . ALA B 359 ? 1.8075 1.7693 2.3356 0.2604  -0.1505 0.0797  359 ALA B CB  
6226 N N   . GLU B 360 ? 1.4162 1.4433 1.9285 0.2853  -0.1425 0.0885  360 GLU B N   
6227 C CA  . GLU B 360 ? 1.5459 1.5886 2.0241 0.3107  -0.1462 0.0876  360 GLU B CA  
6228 C C   . GLU B 360 ? 1.4285 1.4667 1.9234 0.2963  -0.1519 0.0957  360 GLU B C   
6229 O O   . GLU B 360 ? 1.2570 1.2679 1.7172 0.3119  -0.1688 0.0917  360 GLU B O   
6230 C CB  . GLU B 360 ? 1.9042 2.0106 2.3839 0.3241  -0.1256 0.0924  360 GLU B CB  
6231 C CG  . GLU B 360 ? 2.2996 2.4107 2.7406 0.3547  -0.1254 0.0823  360 GLU B CG  
6232 C CD  . GLU B 360 ? 2.4507 2.6302 2.8922 0.3704  -0.1064 0.0896  360 GLU B CD  
6233 O OE1 . GLU B 360 ? 2.6977 2.9208 3.1783 0.3497  -0.0918 0.1037  360 GLU B OE1 
6234 O OE2 . GLU B 360 ? 2.3490 2.5401 2.7538 0.4021  -0.1063 0.0826  360 GLU B OE2 
6235 N N   . ALA B 361 ? 1.3804 1.4432 1.9267 0.2673  -0.1385 0.1069  361 ALA B N   
6236 C CA  . ALA B 361 ? 1.4181 1.4808 1.9874 0.2506  -0.1419 0.1160  361 ALA B CA  
6237 C C   . ALA B 361 ? 1.4936 1.4981 2.0537 0.2449  -0.1653 0.1121  361 ALA B C   
6238 O O   . ALA B 361 ? 1.5630 1.5518 2.1071 0.2499  -0.1786 0.1135  361 ALA B O   
6239 C CB  . ALA B 361 ? 1.4145 1.5073 2.0377 0.2221  -0.1249 0.1269  361 ALA B CB  
6240 N N   . LEU B 362 ? 1.4366 1.4105 2.0064 0.2341  -0.1706 0.1084  362 LEU B N   
6241 C CA  . LEU B 362 ? 1.4599 1.3805 2.0265 0.2244  -0.1933 0.1076  362 LEU B CA  
6242 C C   . LEU B 362 ? 1.7101 1.5915 2.2176 0.2506  -0.2172 0.0982  362 LEU B C   
6243 O O   . LEU B 362 ? 1.7686 1.6172 2.2667 0.2473  -0.2371 0.1003  362 LEU B O   
6244 C CB  . LEU B 362 ? 1.3649 1.2669 1.9516 0.2089  -0.1926 0.1070  362 LEU B CB  
6245 C CG  . LEU B 362 ? 1.3447 1.2748 1.9893 0.1817  -0.1729 0.1168  362 LEU B CG  
6246 C CD1 . LEU B 362 ? 1.3182 1.2328 1.9769 0.1700  -0.1706 0.1161  362 LEU B CD1 
6247 C CD2 . LEU B 362 ? 1.6021 1.5259 2.2786 0.1626  -0.1792 0.1270  362 LEU B CD2 
6248 N N   . VAL B 363 ? 1.8044 1.6894 2.2709 0.2779  -0.2155 0.0878  363 VAL B N   
6249 C CA  . VAL B 363 ? 1.8924 1.7365 2.2959 0.3075  -0.2384 0.0766  363 VAL B CA  
6250 C C   . VAL B 363 ? 2.1149 1.9727 2.4991 0.3215  -0.2405 0.0790  363 VAL B C   
6251 O O   . VAL B 363 ? 2.4191 2.2321 2.7683 0.3308  -0.2648 0.0754  363 VAL B O   
6252 C CB  . VAL B 363 ? 2.2816 2.1263 2.6448 0.3359  -0.2362 0.0646  363 VAL B CB  
6253 C CG1 . VAL B 363 ? 2.9488 2.7417 3.2421 0.3681  -0.2634 0.0520  363 VAL B CG1 
6254 C CG2 . VAL B 363 ? 2.4261 2.2586 2.8114 0.3191  -0.2333 0.0636  363 VAL B CG2 
6255 N N   . GLY B 364 ? 2.0430 1.9631 2.4466 0.3242  -0.2154 0.0853  364 GLY B N   
6256 C CA  . GLY B 364 ? 1.9629 1.9091 2.3472 0.3401  -0.2122 0.0888  364 GLY B CA  
6257 C C   . GLY B 364 ? 1.8732 1.8501 2.2141 0.3775  -0.2030 0.0821  364 GLY B C   
6258 O O   . GLY B 364 ? 2.0089 2.0182 2.3323 0.3943  -0.1964 0.0862  364 GLY B O   
6259 N N   . ALA B 365 ? 1.9635 1.9319 2.2880 0.3904  -0.2022 0.0728  365 ALA B N   
6260 C CA  . ALA B 365 ? 2.3455 2.3382 2.6260 0.4289  -0.1957 0.0652  365 ALA B CA  
6261 C C   . ALA B 365 ? 2.4868 2.5240 2.7961 0.4238  -0.1742 0.0677  365 ALA B C   
6262 O O   . ALA B 365 ? 2.7878 2.8192 3.1391 0.3940  -0.1695 0.0711  365 ALA B O   
6263 C CB  . ALA B 365 ? 2.3249 2.2530 2.5408 0.4586  -0.2223 0.0487  365 ALA B CB  
6264 N N   . ARG B 366 ? 2.3579 2.4412 2.6433 0.4540  -0.1610 0.0670  366 ARG B N   
6265 C CA  . ARG B 366 ? 2.4469 2.5748 2.7531 0.4540  -0.1422 0.0696  366 ARG B CA  
6266 C C   . ARG B 366 ? 2.5910 2.6714 2.8654 0.4692  -0.1559 0.0540  366 ARG B C   
6267 O O   . ARG B 366 ? 2.6282 2.6433 2.8649 0.4789  -0.1802 0.0426  366 ARG B O   
6268 C CB  . ARG B 366 ? 2.6234 2.8210 2.9157 0.4816  -0.1248 0.0768  366 ARG B CB  
6269 C CG  . ARG B 366 ? 2.4202 2.6523 2.7323 0.4693  -0.1174 0.0914  366 ARG B CG  
6270 C CD  . ARG B 366 ? 2.5399 2.8584 2.8728 0.4734  -0.0936 0.1080  366 ARG B CD  
6271 N NE  . ARG B 366 ? 2.4220 2.7696 2.7991 0.4501  -0.0797 0.1145  366 ARG B NE  
6272 C CZ  . ARG B 366 ? 2.3030 2.6947 2.7315 0.4183  -0.0655 0.1316  366 ARG B CZ  
6273 N NH1 . ARG B 366 ? 2.3816 2.7972 2.8266 0.4048  -0.0622 0.1450  366 ARG B NH1 
6274 N NH2 . ARG B 366 ? 2.0865 2.4963 2.5469 0.4008  -0.0558 0.1353  366 ARG B NH2 
6275 N N   . VAL B 367 ? 2.6461 2.7586 2.9343 0.4710  -0.1417 0.0544  367 VAL B N   
6276 C CA  . VAL B 367 ? 2.7200 2.7916 2.9893 0.4777  -0.1522 0.0418  367 VAL B CA  
6277 C C   . VAL B 367 ? 2.8082 2.8226 3.0082 0.5146  -0.1772 0.0251  367 VAL B C   
6278 O O   . VAL B 367 ? 2.8176 2.7700 3.0002 0.5102  -0.1969 0.0152  367 VAL B O   
6279 C CB  . VAL B 367 ? 2.7534 2.8698 3.0434 0.4777  -0.1339 0.0446  367 VAL B CB  
6280 C CG1 . VAL B 367 ? 2.9251 3.0335 3.1641 0.5186  -0.1406 0.0315  367 VAL B CG1 
6281 C CG2 . VAL B 367 ? 2.8530 2.9512 3.1876 0.4389  -0.1309 0.0476  367 VAL B CG2 
6282 N N   . GLY B 368 ? 2.7843 2.8186 2.9431 0.5510  -0.1772 0.0227  368 GLY B N   
6283 C CA  . GLY B 368 ? 2.9131 2.8905 3.0000 0.5893  -0.2022 0.0064  368 GLY B CA  
6284 C C   . GLY B 368 ? 3.0857 3.0778 3.1319 0.6308  -0.1995 -0.0038 368 GLY B C   
6285 O O   . GLY B 368 ? 2.9366 2.9353 3.0017 0.6220  -0.1935 -0.0050 368 GLY B O   
6286 N N   . ALA B 369 ? 3.1890 3.1883 3.1792 0.6769  -0.2032 -0.0106 369 ALA B N   
6287 C CA  . ALA B 369 ? 3.0556 3.0677 2.9988 0.7241  -0.2022 -0.0213 369 ALA B CA  
6288 C C   . ALA B 369 ? 2.8983 2.9752 2.8857 0.7150  -0.1778 -0.0129 369 ALA B C   
6289 O O   . ALA B 369 ? 2.8797 3.0188 2.9283 0.6839  -0.1545 0.0045  369 ALA B O   
6290 C CB  . ALA B 369 ? 3.0031 2.9215 2.8848 0.7445  -0.2360 -0.0419 369 ALA B CB  
6291 N N   . ASP B 370 ? 2.6905 2.7511 2.6421 0.7450  -0.1849 -0.0255 370 ASP B N   
6292 C CA  . ASP B 370 ? 2.8678 2.9756 2.8561 0.7360  -0.1671 -0.0198 370 ASP B CA  
6293 C C   . ASP B 370 ? 3.0447 3.1058 3.0707 0.6892  -0.1753 -0.0202 370 ASP B C   
6294 O O   . ASP B 370 ? 3.3156 3.4109 3.3854 0.6668  -0.1600 -0.0126 370 ASP B O   
6295 C CB  . ASP B 370 ? 3.1895 3.2975 3.1247 0.7868  -0.1721 -0.0330 370 ASP B CB  
6296 C CG  . ASP B 370 ? 3.5142 3.6965 3.4842 0.7887  -0.1486 -0.0234 370 ASP B CG  
6297 O OD1 . ASP B 370 ? 3.6418 3.9093 3.6489 0.7848  -0.1234 -0.0053 370 ASP B OD1 
6298 O OD2 . ASP B 370 ? 3.5349 3.6890 3.4941 0.7936  -0.1570 -0.0332 370 ASP B OD2 
6299 N N   . GLY B 371 ? 2.9850 2.9682 2.9925 0.6749  -0.2001 -0.0280 371 GLY B N   
6300 C CA  . GLY B 371 ? 2.8201 2.7553 2.8583 0.6329  -0.2102 -0.0279 371 GLY B CA  
6301 C C   . GLY B 371 ? 2.7556 2.6096 2.7687 0.6217  -0.2396 -0.0342 371 GLY B C   
6302 O O   . GLY B 371 ? 2.5364 2.3498 2.4898 0.6546  -0.2601 -0.0452 371 GLY B O   
6303 N N   . MET B 372 ? 2.8641 2.6982 2.9246 0.5750  -0.2410 -0.0260 372 MET B N   
6304 C CA  . MET B 372 ? 3.3741 3.1307 3.4233 0.5544  -0.2695 -0.0290 372 MET B CA  
6305 C C   . MET B 372 ? 3.4277 3.1950 3.5301 0.5138  -0.2628 -0.0147 372 MET B C   
6306 O O   . MET B 372 ? 3.7755 3.5171 3.9117 0.4780  -0.2679 -0.0091 372 MET B O   
6307 C CB  . MET B 372 ? 3.5872 3.2745 3.5600 0.5892  -0.3030 -0.0437 372 MET B CB  
6308 C CG  . MET B 372 ? 3.5165 3.1211 3.4787 0.5645  -0.3359 -0.0450 372 MET B CG  
6309 S SD  . MET B 372 ? 3.3862 2.9546 3.3654 0.5378  -0.3450 -0.0454 372 MET B SD  
6310 C CE  . MET B 372 ? 3.0647 2.6077 3.0978 0.4825  -0.3535 -0.0294 372 MET B CE  
6311 N N   . LEU B 373 ? 3.0275 2.8295 3.1350 0.5202  -0.2531 -0.0087 373 LEU B N   
6312 C CA  . LEU B 373 ? 2.6255 2.4307 2.7755 0.4862  -0.2509 0.0034  373 LEU B CA  
6313 C C   . LEU B 373 ? 2.3516 2.0790 2.4713 0.4810  -0.2848 -0.0009 373 LEU B C   
6314 O O   . LEU B 373 ? 2.1808 1.8542 2.2937 0.4676  -0.3047 -0.0042 373 LEU B O   
6315 C CB  . LEU B 373 ? 2.5684 2.4068 2.7910 0.4425  -0.2305 0.0169  373 LEU B CB  
6316 C CG  . LEU B 373 ? 2.1436 1.9734 2.4055 0.4089  -0.2332 0.0282  373 LEU B CG  
6317 C CD1 . LEU B 373 ? 1.9071 1.7705 2.1648 0.4206  -0.2259 0.0331  373 LEU B CD1 
6318 C CD2 . LEU B 373 ? 1.9604 1.8189 2.2888 0.3699  -0.2138 0.0399  373 LEU B CD2 
6319 N N   . ARG B 374 ? 2.2690 1.9927 2.3723 0.4897  -0.2916 0.0007  374 ARG B N   
6320 C CA  . ARG B 374 ? 2.3649 2.0147 2.4302 0.4906  -0.3263 -0.0038 374 ARG B CA  
6321 C C   . ARG B 374 ? 2.2897 1.9557 2.3787 0.4756  -0.3231 0.0066  374 ARG B C   
6322 O O   . ARG B 374 ? 2.1829 1.9098 2.2875 0.4835  -0.2991 0.0122  374 ARG B O   
6323 C CB  . ARG B 374 ? 2.4504 2.0558 2.4311 0.5390  -0.3491 -0.0209 374 ARG B CB  
6324 C CG  . ARG B 374 ? 2.3856 2.0098 2.3366 0.5722  -0.3397 -0.0319 374 ARG B CG  
6325 C CD  . ARG B 374 ? 2.5341 2.1049 2.3969 0.6215  -0.3661 -0.0496 374 ARG B CD  
6326 N NE  . ARG B 374 ? 2.7320 2.3467 2.5696 0.6614  -0.3482 -0.0578 374 ARG B NE  
6327 C CZ  . ARG B 374 ? 2.6797 2.2622 2.4768 0.6855  -0.3608 -0.0708 374 ARG B CZ  
6328 N NH1 . ARG B 374 ? 2.6663 2.1694 2.4422 0.6721  -0.3926 -0.0769 374 ARG B NH1 
6329 N NH2 . ARG B 374 ? 2.5293 2.1617 2.3095 0.7217  -0.3418 -0.0761 374 ARG B NH2 
6330 N N   . GLY B 375 ? 2.2948 1.9049 2.3858 0.4531  -0.3492 0.0103  375 GLY B N   
6331 C CA  . GLY B 375 ? 2.2341 1.8489 2.3474 0.4360  -0.3513 0.0204  375 GLY B CA  
6332 C C   . GLY B 375 ? 2.5516 2.1536 2.6051 0.4723  -0.3626 0.0127  375 GLY B C   
6333 O O   . GLY B 375 ? 2.8190 2.4086 2.8122 0.5129  -0.3685 -0.0007 375 GLY B O   
6334 N N   . ALA B 376 ? 2.7044 2.3084 2.7739 0.4580  -0.3660 0.0216  376 ALA B N   
6335 C CA  . ALA B 376 ? 2.9668 2.5600 2.9846 0.4880  -0.3759 0.0166  376 ALA B CA  
6336 C C   . ALA B 376 ? 3.2498 2.7629 3.1843 0.5208  -0.4126 0.0004  376 ALA B C   
6337 O O   . ALA B 376 ? 3.3120 2.8257 3.1861 0.5644  -0.4134 -0.0104 376 ALA B O   
6338 C CB  . ALA B 376 ? 2.8557 2.4465 2.9064 0.4599  -0.3813 0.0292  376 ALA B CB  
6339 N N   . ASP B 377 ? 3.2983 2.7441 3.2304 0.4997  -0.4428 0.0000  377 ASP B N   
6340 C CA  . ASP B 377 ? 3.1079 2.4651 2.9642 0.5224  -0.4846 -0.0132 377 ASP B CA  
6341 C C   . ASP B 377 ? 3.1065 2.4557 2.9159 0.5580  -0.4838 -0.0287 377 ASP B C   
6342 O O   . ASP B 377 ? 3.3650 2.6452 3.0985 0.5887  -0.5158 -0.0429 377 ASP B O   
6343 C CB  . ASP B 377 ? 3.0615 2.3567 2.9381 0.4835  -0.5163 -0.0049 377 ASP B CB  
6344 C CG  . ASP B 377 ? 3.1765 2.4979 3.1203 0.4465  -0.5009 0.0051  377 ASP B CG  
6345 O OD1 . ASP B 377 ? 3.2084 2.5908 3.1795 0.4519  -0.4671 0.0037  377 ASP B OD1 
6346 O OD2 . ASP B 377 ? 3.3536 2.6362 3.3232 0.4119  -0.5228 0.0154  377 ASP B OD2 
6347 N N   . GLY B 378 ? 3.0612 2.4779 2.9149 0.5533  -0.4489 -0.0257 378 GLY B N   
6348 C CA  . GLY B 378 ? 3.0669 2.4888 2.8844 0.5865  -0.4431 -0.0389 378 GLY B CA  
6349 C C   . GLY B 378 ? 3.1178 2.5119 2.9580 0.5614  -0.4519 -0.0381 378 GLY B C   
6350 O O   . GLY B 378 ? 2.9269 2.3396 2.7582 0.5787  -0.4401 -0.0455 378 GLY B O   
6351 N N   . ARG B 379 ? 3.1928 2.5434 3.0617 0.5211  -0.4733 -0.0282 379 ARG B N   
6352 C CA  . ARG B 379 ? 3.3099 2.6343 3.2069 0.4903  -0.4830 -0.0232 379 ARG B CA  
6353 C C   . ARG B 379 ? 3.2195 2.6204 3.1854 0.4702  -0.4423 -0.0152 379 ARG B C   
6354 O O   . ARG B 379 ? 3.4701 2.9340 3.4924 0.4518  -0.4130 -0.0040 379 ARG B O   
6355 C CB  . ARG B 379 ? 3.3736 2.6480 3.2938 0.4503  -0.5113 -0.0102 379 ARG B CB  
6356 C CG  . ARG B 379 ? 3.6848 2.8650 3.5335 0.4640  -0.5611 -0.0174 379 ARG B CG  
6357 C CD  . ARG B 379 ? 4.2178 3.3334 4.0125 0.4787  -0.5900 -0.0286 379 ARG B CD  
6358 N NE  . ARG B 379 ? 4.1558 3.2936 4.0040 0.4471  -0.5764 -0.0195 379 ARG B NE  
6359 C CZ  . ARG B 379 ? 3.8672 3.0095 3.7775 0.3992  -0.5774 -0.0008 379 ARG B CZ  
6360 N NH1 . ARG B 379 ? 3.4478 2.5678 3.3763 0.3741  -0.5961 0.0118  379 ARG B NH1 
6361 N NH2 . ARG B 379 ? 3.9752 3.1455 3.9289 0.3776  -0.5598 0.0053  379 ARG B NH2 
6362 N N   . PRO B 380 ? 2.8395 2.2296 2.7984 0.4726  -0.4430 -0.0207 380 PRO B N   
6363 C CA  . PRO B 380 ? 2.6254 2.0781 2.6404 0.4560  -0.4085 -0.0149 380 PRO B CA  
6364 C C   . PRO B 380 ? 2.8490 2.3331 2.9439 0.4071  -0.3919 0.0032  380 PRO B C   
6365 O O   . PRO B 380 ? 2.7234 2.1725 2.8350 0.3797  -0.4113 0.0129  380 PRO B O   
6366 C CB  . PRO B 380 ? 2.3470 1.7567 2.3282 0.4655  -0.4252 -0.0243 380 PRO B CB  
6367 C CG  . PRO B 380 ? 2.6155 1.9607 2.5109 0.5060  -0.4588 -0.0402 380 PRO B CG  
6368 C CD  . PRO B 380 ? 2.8856 2.1965 2.7793 0.4908  -0.4802 -0.0329 380 PRO B CD  
6369 N N   . VAL B 381 ? 2.9556 2.5080 3.0986 0.3983  -0.3557 0.0081  381 VAL B N   
6370 C CA  . VAL B 381 ? 2.4746 2.0668 2.6921 0.3579  -0.3338 0.0237  381 VAL B CA  
6371 C C   . VAL B 381 ? 2.4153 2.0313 2.6606 0.3463  -0.3153 0.0246  381 VAL B C   
6372 O O   . VAL B 381 ? 2.3958 2.0412 2.6265 0.3685  -0.2999 0.0166  381 VAL B O   
6373 C CB  . VAL B 381 ? 2.3876 2.0423 2.6400 0.3557  -0.3071 0.0308  381 VAL B CB  
6374 C CG1 . VAL B 381 ? 2.4546 2.1419 2.7796 0.3153  -0.2883 0.0461  381 VAL B CG1 
6375 C CG2 . VAL B 381 ? 2.4929 2.1257 2.7125 0.3707  -0.3245 0.0290  381 VAL B CG2 
6376 N N   . TYR B 382 ? 2.2426 1.8454 2.5283 0.3109  -0.3177 0.0355  382 TYR B N   
6377 C CA  . TYR B 382 ? 2.3545 1.9709 2.6674 0.2948  -0.3036 0.0382  382 TYR B CA  
6378 C C   . TYR B 382 ? 2.3968 2.0516 2.7797 0.2589  -0.2812 0.0536  382 TYR B C   
6379 O O   . TYR B 382 ? 2.6180 2.2579 3.0253 0.2366  -0.2913 0.0645  382 TYR B O   
6380 C CB  . TYR B 382 ? 2.2852 1.8402 2.5734 0.2867  -0.3316 0.0372  382 TYR B CB  
6381 C CG  . TYR B 382 ? 2.2955 1.7970 2.5094 0.3205  -0.3610 0.0220  382 TYR B CG  
6382 C CD1 . TYR B 382 ? 2.4948 2.0033 2.6758 0.3484  -0.3547 0.0089  382 TYR B CD1 
6383 C CD2 . TYR B 382 ? 2.1710 1.6135 2.3462 0.3254  -0.3962 0.0208  382 TYR B CD2 
6384 C CE1 . TYR B 382 ? 2.8135 2.2719 2.9238 0.3827  -0.3818 -0.0057 382 TYR B CE1 
6385 C CE2 . TYR B 382 ? 2.4553 1.8436 2.5573 0.3587  -0.4248 0.0058  382 TYR B CE2 
6386 C CZ  . TYR B 382 ? 2.7831 2.1794 2.8522 0.3883  -0.4173 -0.0078 382 TYR B CZ  
6387 O OH  . TYR B 382 ? 3.0370 2.3781 3.0312 0.4241  -0.4461 -0.0234 382 TYR B OH  
6388 N N   . TYR B 383 ? 2.2297 1.9324 2.6418 0.2552  -0.2518 0.0543  383 TYR B N   
6389 C CA  . TYR B 383 ? 1.9605 1.7024 2.4338 0.2267  -0.2278 0.0666  383 TYR B CA  
6390 C C   . TYR B 383 ? 1.7508 1.5023 2.2438 0.2138  -0.2135 0.0681  383 TYR B C   
6391 O O   . TYR B 383 ? 1.7692 1.5240 2.2387 0.2294  -0.2092 0.0593  383 TYR B O   
6392 C CB  . TYR B 383 ? 2.0821 1.8750 2.5803 0.2289  -0.2066 0.0700  383 TYR B CB  
6393 C CG  . TYR B 383 ? 2.0717 1.9114 2.5653 0.2468  -0.1847 0.0645  383 TYR B CG  
6394 C CD1 . TYR B 383 ? 1.9906 1.8654 2.5185 0.2332  -0.1609 0.0685  383 TYR B CD1 
6395 C CD2 . TYR B 383 ? 1.9307 1.7827 2.3880 0.2762  -0.1875 0.0573  383 TYR B CD2 
6396 C CE1 . TYR B 383 ? 1.7787 1.6977 2.3054 0.2465  -0.1427 0.0661  383 TYR B CE1 
6397 C CE2 . TYR B 383 ? 1.9532 1.8549 2.4113 0.2906  -0.1672 0.0557  383 TYR B CE2 
6398 C CZ  . TYR B 383 ? 1.8664 1.8014 2.3606 0.2743  -0.1457 0.0607  383 TYR B CZ  
6399 O OH  . TYR B 383 ? 1.6193 1.6024 2.1141 0.2871  -0.1284 0.0608  383 TYR B OH  
6400 N N   . THR B 384 ? 1.8953 1.6553 2.4349 0.1847  -0.2043 0.0806  384 THR B N   
6401 C CA  . THR B 384 ? 1.8703 1.6443 2.4371 0.1683  -0.1871 0.0849  384 THR B CA  
6402 C C   . THR B 384 ? 1.8943 1.7145 2.5116 0.1526  -0.1597 0.0933  384 THR B C   
6403 O O   . THR B 384 ? 1.6926 1.5182 2.3383 0.1391  -0.1601 0.1025  384 THR B O   
6404 C CB  . THR B 384 ? 1.7681 1.5041 2.3405 0.1483  -0.2040 0.0936  384 THR B CB  
6405 O OG1 . THR B 384 ? 1.6098 1.2965 2.1322 0.1622  -0.2338 0.0862  384 THR B OG1 
6406 C CG2 . THR B 384 ? 1.7085 1.4563 2.3033 0.1334  -0.1871 0.0979  384 THR B CG2 
6407 N N   . HIS B 385 ? 1.7352 1.5857 2.3598 0.1559  -0.1383 0.0896  385 HIS B N   
6408 C CA  . HIS B 385 ? 1.7105 1.6021 2.3742 0.1450  -0.1139 0.0954  385 HIS B CA  
6409 C C   . HIS B 385 ? 1.7039 1.6033 2.3863 0.1323  -0.0973 0.0977  385 HIS B C   
6410 O O   . HIS B 385 ? 1.5829 1.4772 2.2433 0.1408  -0.0962 0.0908  385 HIS B O   
6411 C CB  . HIS B 385 ? 1.5624 1.4886 2.2166 0.1615  -0.1038 0.0903  385 HIS B CB  
6412 C CG  . HIS B 385 ? 1.4164 1.3795 2.1041 0.1500  -0.0806 0.0955  385 HIS B CG  
6413 N ND1 . HIS B 385 ? 1.4488 1.4312 2.1685 0.1381  -0.0724 0.1036  385 HIS B ND1 
6414 C CD2 . HIS B 385 ? 1.3851 1.3647 2.0768 0.1485  -0.0660 0.0937  385 HIS B CD2 
6415 C CE1 . HIS B 385 ? 1.6990 1.7066 2.4392 0.1301  -0.0543 0.1062  385 HIS B CE1 
6416 N NE2 . HIS B 385 ? 1.5679 1.5745 2.2915 0.1360  -0.0502 0.1005  385 HIS B NE2 
6417 N N   . GLY B 386 ? 1.9247 1.8355 2.6458 0.1136  -0.0852 0.1074  386 GLY B N   
6418 C CA  . GLY B 386 ? 1.8264 1.7401 2.5659 0.1006  -0.0707 0.1113  386 GLY B CA  
6419 C C   . GLY B 386 ? 1.5091 1.4527 2.2835 0.0915  -0.0502 0.1168  386 GLY B C   
6420 O O   . GLY B 386 ? 1.3036 1.2564 2.1012 0.0855  -0.0501 0.1232  386 GLY B O   
6421 N N   . ARG B 387 ? 1.3182 1.2740 2.0952 0.0902  -0.0339 0.1143  387 ARG B N   
6422 C CA  . ARG B 387 ? 1.2681 1.2401 2.0751 0.0793  -0.0155 0.1200  387 ARG B CA  
6423 C C   . ARG B 387 ? 1.5031 1.4620 2.3254 0.0676  -0.0115 0.1273  387 ARG B C   
6424 O O   . ARG B 387 ? 1.7402 1.6832 2.5461 0.0672  -0.0140 0.1255  387 ARG B O   
6425 C CB  . ARG B 387 ? 0.9154 0.9015 1.7142 0.0830  -0.0021 0.1144  387 ARG B CB  
6426 C CG  . ARG B 387 ? 0.9784 0.9794 1.7570 0.0956  -0.0074 0.1083  387 ARG B CG  
6427 C CD  . ARG B 387 ? 1.3870 1.4042 2.1632 0.0956  0.0047  0.1062  387 ARG B CD  
6428 N NE  . ARG B 387 ? 1.8414 1.8799 2.6033 0.1069  -0.0004 0.1038  387 ARG B NE  
6429 C CZ  . ARG B 387 ? 2.1245 2.1857 2.8857 0.1074  0.0060  0.1046  387 ARG B CZ  
6430 N NH1 . ARG B 387 ? 2.0340 2.0943 2.8042 0.0977  0.0166  0.1062  387 ARG B NH1 
6431 N NH2 . ARG B 387 ? 2.3644 2.4496 3.1150 0.1179  0.0012  0.1049  387 ARG B NH2 
6432 N N   . LEU B 388 ? 1.4856 1.4533 2.3399 0.0584  -0.0055 0.1367  388 LEU B N   
6433 C CA  . LEU B 388 ? 1.2324 1.1980 2.1078 0.0479  0.0024  0.1465  388 LEU B CA  
6434 C C   . LEU B 388 ? 1.2986 1.2828 2.1989 0.0458  0.0223  0.1497  388 LEU B C   
6435 O O   . LEU B 388 ? 1.5919 1.5883 2.5085 0.0465  0.0235  0.1511  388 LEU B O   
6436 C CB  . LEU B 388 ? 1.1915 1.1484 2.0826 0.0389  -0.0116 0.1579  388 LEU B CB  
6437 C CG  . LEU B 388 ? 1.3497 1.3069 2.2472 0.0402  -0.0263 0.1596  388 LEU B CG  
6438 C CD1 . LEU B 388 ? 1.8317 1.7944 2.7641 0.0282  -0.0291 0.1749  388 LEU B CD1 
6439 C CD2 . LEU B 388 ? 1.4620 1.3948 2.3259 0.0465  -0.0493 0.1535  388 LEU B CD2 
6440 N N   . LEU B 389 ? 1.3257 1.3092 2.2255 0.0441  0.0367  0.1505  389 LEU B N   
6441 C CA  . LEU B 389 ? 1.4429 1.4387 2.3613 0.0443  0.0555  0.1533  389 LEU B CA  
6442 C C   . LEU B 389 ? 1.7567 1.7557 2.6925 0.0387  0.0656  0.1645  389 LEU B C   
6443 O O   . LEU B 389 ? 2.1903 2.1794 3.1119 0.0359  0.0656  0.1655  389 LEU B O   
6444 C CB  . LEU B 389 ? 1.0511 1.0429 1.9448 0.0505  0.0631  0.1422  389 LEU B CB  
6445 C CG  . LEU B 389 ? 1.2709 1.2655 2.1698 0.0528  0.0815  0.1420  389 LEU B CG  
6446 C CD1 . LEU B 389 ? 1.4502 1.4451 2.3343 0.0569  0.0808  0.1333  389 LEU B CD1 
6447 C CD2 . LEU B 389 ? 1.2783 1.2630 2.1630 0.0526  0.0913  0.1418  389 LEU B CD2 
6448 N N   . GLU B 390 ? 1.6626 1.6771 2.6299 0.0371  0.0726  0.1742  390 GLU B N   
6449 C CA  . GLU B 390 ? 1.8475 1.8732 2.8367 0.0330  0.0835  0.1876  390 GLU B CA  
6450 C C   . GLU B 390 ? 1.6487 1.6906 2.6608 0.0397  0.0980  0.1902  390 GLU B C   
6451 O O   . GLU B 390 ? 1.4160 1.4691 2.4538 0.0373  0.0920  0.1975  390 GLU B O   
6452 C CB  . GLU B 390 ? 2.3922 2.4218 3.4019 0.0217  0.0690  0.2024  390 GLU B CB  
6453 C CG  . GLU B 390 ? 2.7502 2.7633 3.7403 0.0138  0.0574  0.2051  390 GLU B CG  
6454 C CD  . GLU B 390 ? 2.7023 2.7231 3.6971 0.0097  0.0716  0.2154  390 GLU B CD  
6455 O OE1 . GLU B 390 ? 2.1631 2.2066 3.1901 0.0053  0.0805  0.2317  390 GLU B OE1 
6456 O OE2 . GLU B 390 ? 3.1512 3.1566 4.1171 0.0112  0.0736  0.2077  390 GLU B OE2 
6457 N N   . PRO B 391 ? 1.6273 1.6667 2.6266 0.0490  0.1145  0.1827  391 PRO B N   
6458 C CA  . PRO B 391 ? 1.6203 1.6702 2.6364 0.0581  0.1277  0.1842  391 PRO B CA  
6459 C C   . PRO B 391 ? 1.5583 1.6317 2.6122 0.0560  0.1324  0.2011  391 PRO B C   
6460 O O   . PRO B 391 ? 1.4244 1.5089 2.5022 0.0579  0.1299  0.2054  391 PRO B O   
6461 C CB  . PRO B 391 ? 1.4705 1.5104 2.4627 0.0676  0.1445  0.1769  391 PRO B CB  
6462 C CG  . PRO B 391 ? 1.3929 1.4147 2.3528 0.0629  0.1372  0.1679  391 PRO B CG  
6463 C CD  . PRO B 391 ? 1.4567 1.4793 2.4218 0.0520  0.1189  0.1719  391 PRO B CD  
6464 N N   . GLU B 392 ? 1.6008 1.6825 2.6600 0.0507  0.1375  0.2120  392 GLU B N   
6465 C CA  . GLU B 392 ? 1.7066 1.8160 2.8007 0.0493  0.1464  0.2310  392 GLU B CA  
6466 C C   . GLU B 392 ? 1.7115 1.8332 2.8376 0.0405  0.1308  0.2417  392 GLU B C   
6467 O O   . GLU B 392 ? 2.1406 2.2846 3.2977 0.0455  0.1380  0.2515  392 GLU B O   
6468 C CB  . GLU B 392 ? 2.0841 2.1963 3.1736 0.0396  0.1474  0.2416  392 GLU B CB  
6469 C CG  . GLU B 392 ? 2.3963 2.4878 3.4467 0.0445  0.1557  0.2287  392 GLU B CG  
6470 C CD  . GLU B 392 ? 2.5141 2.6081 3.5523 0.0607  0.1797  0.2235  392 GLU B CD  
6471 O OE1 . GLU B 392 ? 2.7376 2.8570 3.7976 0.0675  0.1965  0.2365  392 GLU B OE1 
6472 O OE2 . GLU B 392 ? 2.3142 2.3842 3.3191 0.0673  0.1809  0.2066  392 GLU B OE2 
6473 N N   . THR B 393 ? 1.5889 1.6945 2.7051 0.0288  0.1086  0.2395  393 THR B N   
6474 C CA  . THR B 393 ? 1.6113 1.7245 2.7541 0.0181  0.0906  0.2516  393 THR B CA  
6475 C C   . THR B 393 ? 1.7172 1.8191 2.8549 0.0216  0.0787  0.2400  393 THR B C   
6476 O O   . THR B 393 ? 2.0102 2.1229 3.1746 0.0188  0.0708  0.2481  393 THR B O   
6477 C CB  . THR B 393 ? 1.6748 1.7748 2.8083 0.0032  0.0716  0.2589  393 THR B CB  
6478 O OG1 . THR B 393 ? 2.0726 2.1435 3.1675 0.0056  0.0599  0.2406  393 THR B OG1 
6479 C CG2 . THR B 393 ? 1.7515 1.8612 2.8864 -0.0016 0.0825  0.2706  393 THR B CG2 
6480 N N   . LEU B 394 ? 1.3770 1.4585 2.4805 0.0269  0.0765  0.2222  394 LEU B N   
6481 C CA  . LEU B 394 ? 1.3103 1.3835 2.4077 0.0287  0.0641  0.2134  394 LEU B CA  
6482 C C   . LEU B 394 ? 1.5217 1.6045 2.6312 0.0384  0.0767  0.2100  394 LEU B C   
6483 O O   . LEU B 394 ? 1.7474 1.8314 2.8665 0.0384  0.0679  0.2092  394 LEU B O   
6484 C CB  . LEU B 394 ? 1.2132 1.2658 2.2717 0.0303  0.0555  0.1985  394 LEU B CB  
6485 C CG  . LEU B 394 ? 1.0978 1.1354 2.1404 0.0229  0.0371  0.2001  394 LEU B CG  
6486 C CD1 . LEU B 394 ? 0.8437 0.8646 1.8478 0.0285  0.0309  0.1848  394 LEU B CD1 
6487 C CD2 . LEU B 394 ? 1.1259 1.1621 2.1843 0.0158  0.0174  0.2087  394 LEU B CD2 
6488 N N   . GLY B 395 ? 1.5892 1.6764 2.6961 0.0471  0.0964  0.2082  395 GLY B N   
6489 C CA  . GLY B 395 ? 1.6804 1.7693 2.7903 0.0585  0.1074  0.2029  395 GLY B CA  
6490 C C   . GLY B 395 ? 1.6207 1.7297 2.7689 0.0610  0.1095  0.2152  395 GLY B C   
6491 O O   . GLY B 395 ? 1.6966 1.8068 2.8501 0.0716  0.1171  0.2122  395 GLY B O   
6492 N N   . LYS B 396 ? 1.3347 1.4574 2.5080 0.0507  0.1004  0.2294  396 LYS B N   
6493 C CA  . LYS B 396 ? 1.5019 1.6464 2.7150 0.0501  0.0987  0.2438  396 LYS B CA  
6494 C C   . LYS B 396 ? 1.5985 1.7344 2.8157 0.0439  0.0787  0.2414  396 LYS B C   
6495 O O   . LYS B 396 ? 1.9442 2.0921 3.1882 0.0464  0.0768  0.2481  396 LYS B O   
6496 C CB  . LYS B 396 ? 1.6191 1.7819 2.8554 0.0393  0.0967  0.2624  396 LYS B CB  
6497 C CG  . LYS B 396 ? 1.6497 1.8375 2.9024 0.0457  0.1182  0.2746  396 LYS B CG  
6498 C CD  . LYS B 396 ? 1.6465 1.8417 2.9012 0.0330  0.1166  0.2877  396 LYS B CD  
6499 C CE  . LYS B 396 ? 1.3996 1.5979 2.6729 0.0129  0.0940  0.3041  396 LYS B CE  
6500 N NZ  . LYS B 396 ? 1.4090 1.6406 2.7299 0.0071  0.0923  0.3276  396 LYS B NZ  
6501 N N   . LEU B 397 ? 1.3192 1.4350 2.5088 0.0371  0.0640  0.2320  397 LEU B N   
6502 C CA  . LEU B 397 ? 1.2964 1.4043 2.4864 0.0310  0.0441  0.2309  397 LEU B CA  
6503 C C   . LEU B 397 ? 1.1427 1.2430 2.3199 0.0378  0.0444  0.2193  397 LEU B C   
6504 O O   . LEU B 397 ? 1.0024 1.0971 2.1617 0.0455  0.0567  0.2098  397 LEU B O   
6505 C CB  . LEU B 397 ? 1.2057 1.2961 2.3676 0.0239  0.0297  0.2259  397 LEU B CB  
6506 C CG  . LEU B 397 ? 1.0867 1.1782 2.2605 0.0130  0.0191  0.2393  397 LEU B CG  
6507 C CD1 . LEU B 397 ? 1.1081 1.1802 2.2472 0.0108  0.0126  0.2316  397 LEU B CD1 
6508 C CD2 . LEU B 397 ? 1.0803 1.1675 2.2659 0.0062  -0.0021 0.2453  397 LEU B CD2 
6509 N N   . ASN B 398 ? 1.1452 1.2436 2.3298 0.0336  0.0289  0.2211  398 ASN B N   
6510 C CA  . ASN B 398 ? 1.2728 1.3618 2.4387 0.0356  0.0229  0.2112  398 ASN B CA  
6511 C C   . ASN B 398 ? 1.2300 1.3101 2.3801 0.0291  0.0035  0.2097  398 ASN B C   
6512 O O   . ASN B 398 ? 1.0790 1.1573 2.2369 0.0231  -0.0069 0.2171  398 ASN B O   
6513 C CB  . ASN B 398 ? 1.3971 1.4924 2.5854 0.0395  0.0245  0.2148  398 ASN B CB  
6514 C CG  . ASN B 398 ? 1.6089 1.7090 2.8201 0.0328  0.0086  0.2245  398 ASN B CG  
6515 O OD1 . ASN B 398 ? 1.1680 1.2651 2.3775 0.0253  -0.0035 0.2289  398 ASN B OD1 
6516 N ND2 . ASN B 398 ? 2.3134 2.4180 3.5442 0.0355  0.0070  0.2281  398 ASN B ND2 
6517 N N   . PRO B 399 ? 1.2751 1.3492 2.4017 0.0305  -0.0027 0.2012  399 PRO B N   
6518 C CA  . PRO B 399 ? 1.4189 1.4851 2.5234 0.0284  -0.0190 0.1981  399 PRO B CA  
6519 C C   . PRO B 399 ? 1.3691 1.4323 2.4920 0.0226  -0.0348 0.2078  399 PRO B C   
6520 O O   . PRO B 399 ? 1.3954 1.4473 2.5056 0.0202  -0.0481 0.2088  399 PRO B O   
6521 C CB  . PRO B 399 ? 1.3167 1.3861 2.4081 0.0304  -0.0211 0.1930  399 PRO B CB  
6522 C CG  . PRO B 399 ? 1.2779 1.3504 2.3692 0.0334  -0.0053 0.1891  399 PRO B CG  
6523 C CD  . PRO B 399 ? 1.1817 1.2565 2.2990 0.0347  0.0053  0.1947  399 PRO B CD  
6524 N N   . ARG B 400 ? 1.3032 1.3741 2.4524 0.0210  -0.0355 0.2142  400 ARG B N   
6525 C CA  . ARG B 400 ? 1.3424 1.4114 2.5106 0.0151  -0.0518 0.2238  400 ARG B CA  
6526 C C   . ARG B 400 ? 1.3444 1.4127 2.5299 0.0089  -0.0569 0.2342  400 ARG B C   
6527 O O   . ARG B 400 ? 1.7961 1.8516 2.9757 0.0032  -0.0761 0.2386  400 ARG B O   
6528 C CB  . ARG B 400 ? 1.3890 1.4692 2.5900 0.0150  -0.0483 0.2309  400 ARG B CB  
6529 C CG  . ARG B 400 ? 1.3950 1.4748 2.6203 0.0081  -0.0651 0.2427  400 ARG B CG  
6530 C CD  . ARG B 400 ? 1.5178 1.6145 2.7868 0.0078  -0.0586 0.2549  400 ARG B CD  
6531 N NE  . ARG B 400 ? 1.4539 1.5561 2.7362 0.0129  -0.0539 0.2539  400 ARG B NE  
6532 C CZ  . ARG B 400 ? 1.6050 1.6993 2.8815 0.0104  -0.0674 0.2528  400 ARG B CZ  
6533 N NH1 . ARG B 400 ? 1.6619 1.7435 2.9181 0.0047  -0.0847 0.2517  400 ARG B NH1 
6534 N NH2 . ARG B 400 ? 1.6448 1.7422 2.9332 0.0146  -0.0641 0.2527  400 ARG B NH2 
6535 N N   . THR B 401 ? 1.0865 1.1678 2.2916 0.0102  -0.0401 0.2386  401 THR B N   
6536 C CA  . THR B 401 ? 1.1933 1.2807 2.4194 0.0033  -0.0414 0.2515  401 THR B CA  
6537 C C   . THR B 401 ? 1.2365 1.3043 2.4331 -0.0013 -0.0547 0.2484  401 THR B C   
6538 O O   . THR B 401 ? 1.1970 1.2565 2.4006 -0.0108 -0.0726 0.2590  401 THR B O   
6539 C CB  . THR B 401 ? 1.0943 1.1983 2.3326 0.0093  -0.0172 0.2524  401 THR B CB  
6540 O OG1 . THR B 401 ? 1.2019 1.3218 2.4685 0.0150  -0.0078 0.2569  401 THR B OG1 
6541 C CG2 . THR B 401 ? 1.0478 1.1623 2.3040 0.0028  -0.0140 0.2658  401 THR B CG2 
6542 N N   . ALA B 402 ? 1.0077 1.0670 2.1704 0.0057  -0.0466 0.2342  402 ALA B N   
6543 C CA  . ALA B 402 ? 0.9062 0.9461 2.0363 0.0048  -0.0568 0.2287  402 ALA B CA  
6544 C C   . ALA B 402 ? 0.9496 0.9690 2.0606 0.0031  -0.0823 0.2277  402 ALA B C   
6545 O O   . ALA B 402 ? 1.0314 1.0321 2.1316 -0.0026 -0.1001 0.2324  402 ALA B O   
6546 C CB  . ALA B 402 ? 0.8353 0.8733 1.9355 0.0138  -0.0432 0.2142  402 ALA B CB  
6547 N N   . VAL B 403 ? 1.0150 1.0368 2.1204 0.0082  -0.0847 0.2220  403 VAL B N   
6548 C CA  . VAL B 403 ? 1.0992 1.1025 2.1826 0.0094  -0.1070 0.2198  403 VAL B CA  
6549 C C   . VAL B 403 ? 1.3577 1.3517 2.4638 -0.0018 -0.1264 0.2344  403 VAL B C   
6550 O O   . VAL B 403 ? 1.4802 1.4484 2.5632 -0.0036 -0.1489 0.2349  403 VAL B O   
6551 C CB  . VAL B 403 ? 1.2053 1.2114 2.2720 0.0169  -0.1089 0.2120  403 VAL B CB  
6552 C CG1 . VAL B 403 ? 1.2212 1.2043 2.2490 0.0231  -0.1300 0.2062  403 VAL B CG1 
6553 C CG2 . VAL B 403 ? 1.2704 1.2920 2.3252 0.0246  -0.0894 0.2020  403 VAL B CG2 
6554 N N   . GLU B 404 ? 1.4323 1.4467 2.5820 -0.0086 -0.1183 0.2465  404 GLU B N   
6555 C CA  . GLU B 404 ? 1.5541 1.5671 2.7336 -0.0206 -0.1348 0.2634  404 GLU B CA  
6556 C C   . GLU B 404 ? 1.4241 1.4243 2.6005 -0.0298 -0.1463 0.2721  404 GLU B C   
6557 O O   . GLU B 404 ? 1.4405 1.4192 2.6118 -0.0385 -0.1723 0.2802  404 GLU B O   
6558 C CB  . GLU B 404 ? 1.9581 2.0013 3.1841 -0.0220 -0.1186 0.2731  404 GLU B CB  
6559 C CG  . GLU B 404 ? 2.4255 2.4702 3.6525 -0.0172 -0.1210 0.2682  404 GLU B CG  
6560 C CD  . GLU B 404 ? 2.4478 2.4654 3.6483 -0.0201 -0.1482 0.2668  404 GLU B CD  
6561 O OE1 . GLU B 404 ? 2.8307 2.8355 4.0378 -0.0301 -0.1672 0.2781  404 GLU B OE1 
6562 O OE2 . GLU B 404 ? 1.8227 1.8318 2.9950 -0.0125 -0.1509 0.2554  404 GLU B OE2 
6563 N N   . ARG B 405 ? 1.2534 1.2648 2.4309 -0.0283 -0.1278 0.2706  405 ARG B N   
6564 C CA  . ARG B 405 ? 1.2183 1.2200 2.3929 -0.0377 -0.1359 0.2794  405 ARG B CA  
6565 C C   . ARG B 405 ? 1.0874 1.0492 2.2140 -0.0361 -0.1609 0.2704  405 ARG B C   
6566 O O   . ARG B 405 ? 0.9742 0.9148 2.0976 -0.0476 -0.1851 0.2814  405 ARG B O   
6567 C CB  . ARG B 405 ? 1.1451 1.1596 2.3149 -0.0329 -0.1119 0.2741  405 ARG B CB  
6568 C CG  . ARG B 405 ? 1.2482 1.2987 2.4586 -0.0331 -0.0862 0.2838  405 ARG B CG  
6569 C CD  . ARG B 405 ? 1.3677 1.4289 2.5994 -0.0452 -0.0863 0.3019  405 ARG B CD  
6570 N NE  . ARG B 405 ? 1.5673 1.6650 2.8332 -0.0411 -0.0587 0.3098  405 ARG B NE  
6571 C CZ  . ARG B 405 ? 1.3699 1.4764 2.6264 -0.0341 -0.0365 0.3040  405 ARG B CZ  
6572 N NH1 . ARG B 405 ? 0.9543 1.0373 2.1699 -0.0307 -0.0374 0.2894  405 ARG B NH1 
6573 N NH2 . ARG B 405 ? 1.4559 1.5945 2.7424 -0.0287 -0.0130 0.3122  405 ARG B NH2 
6574 N N   . LEU B 406 ? 1.2913 1.2436 2.3805 -0.0213 -0.1554 0.2510  406 LEU B N   
6575 C CA  . LEU B 406 ? 1.4159 1.3323 2.4552 -0.0144 -0.1764 0.2401  406 LEU B CA  
6576 C C   . LEU B 406 ? 1.4365 1.3278 2.4672 -0.0182 -0.2059 0.2452  406 LEU B C   
6577 O O   . LEU B 406 ? 1.5774 1.4338 2.5805 -0.0211 -0.2317 0.2467  406 LEU B O   
6578 C CB  . LEU B 406 ? 1.4883 1.4017 2.4877 0.0024  -0.1645 0.2205  406 LEU B CB  
6579 C CG  . LEU B 406 ? 1.1275 1.0563 2.1320 0.0028  -0.1419 0.2180  406 LEU B CG  
6580 C CD1 . LEU B 406 ? 1.1381 1.0637 2.1048 0.0180  -0.1328 0.2006  406 LEU B CD1 
6581 C CD2 . LEU B 406 ? 1.0040 0.9217 2.0151 -0.0093 -0.1497 0.2291  406 LEU B CD2 
6582 N N   . ARG B 407 ? 1.3111 1.2183 2.3652 -0.0188 -0.2032 0.2487  407 ARG B N   
6583 C CA  . ARG B 407 ? 1.5066 1.3920 2.5545 -0.0222 -0.2296 0.2537  407 ARG B CA  
6584 C C   . ARG B 407 ? 1.7150 1.5882 2.7868 -0.0412 -0.2515 0.2737  407 ARG B C   
6585 O O   . ARG B 407 ? 2.0598 1.9005 3.1127 -0.0450 -0.2814 0.2772  407 ARG B O   
6586 C CB  . ARG B 407 ? 1.3294 1.2397 2.3972 -0.0175 -0.2158 0.2514  407 ARG B CB  
6587 C CG  . ARG B 407 ? 1.6594 1.5744 2.7639 -0.0296 -0.2286 0.2671  407 ARG B CG  
6588 C CD  . ARG B 407 ? 1.9103 1.8262 3.0054 -0.0217 -0.2306 0.2603  407 ARG B CD  
6589 N NE  . ARG B 407 ? 1.8089 1.7132 2.8542 -0.0051 -0.2284 0.2423  407 ARG B NE  
6590 C CZ  . ARG B 407 ? 1.7239 1.6518 2.7662 0.0043  -0.2057 0.2326  407 ARG B CZ  
6591 N NH1 . ARG B 407 ? 1.5944 1.5507 2.6667 0.0019  -0.1812 0.2341  407 ARG B NH1 
6592 N NH2 . ARG B 407 ? 1.6923 1.6142 2.6978 0.0169  -0.2086 0.2217  407 ARG B NH2 
6593 N N   . ALA B 408 ? 1.6451 1.5487 2.7632 -0.0528 -0.2362 0.2883  408 ALA B N   
6594 C CA  . ALA B 408 ? 1.5329 1.4381 2.6861 -0.0727 -0.2532 0.3120  408 ALA B CA  
6595 C C   . ALA B 408 ? 1.6425 1.5093 2.7649 -0.0813 -0.2802 0.3161  408 ALA B C   
6596 O O   . ALA B 408 ? 1.8418 1.6823 2.9627 -0.0940 -0.3121 0.3288  408 ALA B O   
6597 C CB  . ALA B 408 ? 1.2920 1.2431 2.4979 -0.0794 -0.2271 0.3259  408 ALA B CB  
6598 N N   . GLU B 409 ? 1.7668 1.6321 2.8694 -0.0763 -0.2674 0.3080  409 GLU B N   
6599 C CA  . GLU B 409 ? 2.0384 1.8699 3.1141 -0.0850 -0.2899 0.3127  409 GLU B CA  
6600 C C   . GLU B 409 ? 1.9658 1.7471 2.9758 -0.0699 -0.3123 0.2929  409 GLU B C   
6601 O O   . GLU B 409 ? 2.0967 1.8462 3.0705 -0.0690 -0.3264 0.2884  409 GLU B O   
6602 C CB  . GLU B 409 ? 2.1922 2.0495 3.2828 -0.0874 -0.2646 0.3154  409 GLU B CB  
6603 C CG  . GLU B 409 ? 2.3291 2.2395 3.4821 -0.0964 -0.2391 0.3330  409 GLU B CG  
6604 C CD  . GLU B 409 ? 2.4049 2.3299 3.6044 -0.1187 -0.2551 0.3625  409 GLU B CD  
6605 O OE1 . GLU B 409 ? 2.6394 2.5323 3.8265 -0.1340 -0.2884 0.3749  409 GLU B OE1 
6606 O OE2 . GLU B 409 ? 2.0521 2.0215 3.3009 -0.1204 -0.2345 0.3740  409 GLU B OE2 
6607 N N   . GLY B 410 ? 1.8726 1.6468 2.8672 -0.0578 -0.3166 0.2822  410 GLY B N   
6608 C CA  . GLY B 410 ? 1.7634 1.4947 2.6967 -0.0403 -0.3367 0.2642  410 GLY B CA  
6609 C C   . GLY B 410 ? 1.9835 1.7097 2.8768 -0.0220 -0.3224 0.2447  410 GLY B C   
6610 O O   . GLY B 410 ? 2.3827 2.0660 3.2229 -0.0111 -0.3443 0.2342  410 GLY B O   
6611 N N   . LEU B 411 ? 1.9404 1.7090 2.8586 -0.0183 -0.2868 0.2405  411 LEU B N   
6612 C CA  . LEU B 411 ? 1.8959 1.6661 2.7846 -0.0038 -0.2705 0.2247  411 LEU B CA  
6613 C C   . LEU B 411 ? 2.0618 1.8435 2.9245 0.0185  -0.2564 0.2060  411 LEU B C   
6614 O O   . LEU B 411 ? 2.2897 2.0594 3.1106 0.0357  -0.2550 0.1908  411 LEU B O   
6615 C CB  . LEU B 411 ? 1.5970 1.4027 2.5240 -0.0135 -0.2427 0.2320  411 LEU B CB  
6616 C CG  . LEU B 411 ? 1.2714 1.0640 2.2075 -0.0308 -0.2542 0.2466  411 LEU B CG  
6617 C CD1 . LEU B 411 ? 1.2185 1.0495 2.1902 -0.0373 -0.2236 0.2530  411 LEU B CD1 
6618 C CD2 . LEU B 411 ? 1.4073 1.1571 2.2864 -0.0202 -0.2731 0.2338  411 LEU B CD2 
6619 N N   . LEU B 412 ? 1.7200 1.5260 2.6079 0.0181  -0.2468 0.2085  412 LEU B N   
6620 C CA  . LEU B 412 ? 1.6030 1.4253 2.4718 0.0361  -0.2329 0.1945  412 LEU B CA  
6621 C C   . LEU B 412 ? 1.7046 1.4917 2.5164 0.0541  -0.2559 0.1828  412 LEU B C   
6622 O O   . LEU B 412 ? 1.7963 1.5457 2.5903 0.0505  -0.2853 0.1873  412 LEU B O   
6623 C CB  . LEU B 412 ? 1.5603 1.4105 2.4693 0.0286  -0.2230 0.2026  412 LEU B CB  
6624 C CG  . LEU B 412 ? 1.5383 1.4248 2.4555 0.0375  -0.1955 0.1948  412 LEU B CG  
6625 C CD1 . LEU B 412 ? 1.6406 1.5504 2.6027 0.0266  -0.1877 0.2053  412 LEU B CD1 
6626 C CD2 . LEU B 412 ? 1.5456 1.4278 2.4179 0.0572  -0.1985 0.1812  412 LEU B CD2 
6627 N N   . TYR B 413 ? 1.6017 1.4010 2.3831 0.0743  -0.2430 0.1683  413 TYR B N   
6628 C CA  . TYR B 413 ? 1.7610 1.5324 2.4854 0.0962  -0.2608 0.1562  413 TYR B CA  
6629 C C   . TYR B 413 ? 1.9279 1.6900 2.6481 0.0973  -0.2759 0.1597  413 TYR B C   
6630 O O   . TYR B 413 ? 2.2640 2.0588 3.0150 0.0920  -0.2605 0.1644  413 TYR B O   
6631 C CB  . TYR B 413 ? 1.9571 1.7556 2.6584 0.1169  -0.2399 0.1429  413 TYR B CB  
6632 C CG  . TYR B 413 ? 2.0595 1.8380 2.7027 0.1437  -0.2545 0.1308  413 TYR B CG  
6633 C CD1 . TYR B 413 ? 1.8772 1.6685 2.5125 0.1526  -0.2548 0.1305  413 TYR B CD1 
6634 C CD2 . TYR B 413 ? 1.9407 1.6870 2.5351 0.1614  -0.2686 0.1200  413 TYR B CD2 
6635 C CE1 . TYR B 413 ? 1.9481 1.7232 2.5286 0.1793  -0.2670 0.1201  413 TYR B CE1 
6636 C CE2 . TYR B 413 ? 1.9237 1.6516 2.4622 0.1894  -0.2818 0.1085  413 TYR B CE2 
6637 C CZ  . TYR B 413 ? 2.0592 1.8028 2.5907 0.1989  -0.2802 0.1087  413 TYR B CZ  
6638 O OH  . TYR B 413 ? 2.3489 2.0776 2.8240 0.2287  -0.2915 0.0980  413 TYR B OH  
6639 N N   . ARG B 414 ? 1.8065 1.5208 2.4861 0.1043  -0.3074 0.1573  414 ARG B N   
6640 C CA  . ARG B 414 ? 2.0361 1.7346 2.6990 0.1096  -0.3247 0.1583  414 ARG B CA  
6641 C C   . ARG B 414 ? 1.8677 1.5449 2.4638 0.1407  -0.3347 0.1423  414 ARG B C   
6642 O O   . ARG B 414 ? 1.8450 1.4957 2.4020 0.1542  -0.3442 0.1330  414 ARG B O   
6643 C CB  . ARG B 414 ? 2.3314 1.9924 3.0072 0.0897  -0.3547 0.1716  414 ARG B CB  
6644 C CG  . ARG B 414 ? 2.3921 2.0810 3.1367 0.0613  -0.3440 0.1894  414 ARG B CG  
6645 C CD  . ARG B 414 ? 2.8059 2.4561 3.5580 0.0426  -0.3774 0.2039  414 ARG B CD  
6646 N NE  . ARG B 414 ? 3.0957 2.7018 3.8109 0.0441  -0.4002 0.2013  414 ARG B NE  
6647 C CZ  . ARG B 414 ? 2.9453 2.5562 3.6772 0.0330  -0.3938 0.2064  414 ARG B CZ  
6648 N NH1 . ARG B 414 ? 3.2118 2.8700 4.0000 0.0185  -0.3653 0.2158  414 ARG B NH1 
6649 N NH2 . ARG B 414 ? 2.7342 2.2995 3.4236 0.0370  -0.4178 0.2023  414 ARG B NH2 
6650 N N   . HIS B 415 ? 2.0755 1.7653 2.6579 0.1528  -0.3324 0.1397  415 HIS B N   
6651 C CA  . HIS B 415 ? 2.2779 1.9623 2.8013 0.1851  -0.3345 0.1257  415 HIS B CA  
6652 C C   . HIS B 415 ? 2.4204 2.0410 2.8872 0.1984  -0.3720 0.1204  415 HIS B C   
6653 O O   . HIS B 415 ? 2.4635 2.0662 2.8712 0.2287  -0.3792 0.1069  415 HIS B O   
6654 C CB  . HIS B 415 ? 2.6743 2.4039 3.2072 0.1921  -0.3146 0.1270  415 HIS B CB  
6655 C CG  . HIS B 415 ? 2.8005 2.5891 3.3802 0.1819  -0.2803 0.1313  415 HIS B CG  
6656 N ND1 . HIS B 415 ? 2.7215 2.5432 3.2851 0.1997  -0.2599 0.1235  415 HIS B ND1 
6657 C CD2 . HIS B 415 ? 2.5189 2.3375 3.1575 0.1572  -0.2643 0.1424  415 HIS B CD2 
6658 C CE1 . HIS B 415 ? 2.5272 2.3943 3.1376 0.1844  -0.2342 0.1301  415 HIS B CE1 
6659 N NE2 . HIS B 415 ? 2.2833 2.1477 2.9379 0.1597  -0.2363 0.1407  415 HIS B NE2 
6660 N N   . ASP B 416 ? 2.5992 2.1860 3.0840 0.1763  -0.3963 0.1315  416 ASP B N   
6661 C CA  . ASP B 416 ? 2.7665 2.2871 3.2009 0.1839  -0.4363 0.1291  416 ASP B CA  
6662 C C   . ASP B 416 ? 2.6133 2.0859 3.0120 0.1886  -0.4579 0.1232  416 ASP B C   
6663 O O   . ASP B 416 ? 2.7843 2.2030 3.1168 0.2108  -0.4861 0.1126  416 ASP B O   
6664 C CB  . ASP B 416 ? 2.4895 1.9950 2.9588 0.1571  -0.4550 0.1451  416 ASP B CB  
6665 C CG  . ASP B 416 ? 2.4708 2.0016 3.0130 0.1225  -0.4449 0.1621  416 ASP B CG  
6666 O OD1 . ASP B 416 ? 2.7381 2.2958 3.3031 0.1182  -0.4233 0.1612  416 ASP B OD1 
6667 O OD2 . ASP B 416 ? 2.4860 2.0106 3.0610 0.1012  -0.4585 0.1764  416 ASP B OD2 
6668 N N   . THR B 417 ? 2.2562 1.7473 2.6973 0.1684  -0.4451 0.1302  417 THR B N   
6669 C CA  . THR B 417 ? 2.3209 1.7716 2.7367 0.1679  -0.4633 0.1272  417 THR B CA  
6670 C C   . THR B 417 ? 2.3917 1.8602 2.7754 0.1956  -0.4431 0.1105  417 THR B C   
6671 O O   . THR B 417 ? 2.8656 2.2887 3.1920 0.2156  -0.4639 0.0990  417 THR B O   
6672 C CB  . THR B 417 ? 2.1474 1.6089 2.6235 0.1320  -0.4610 0.1450  417 THR B CB  
6673 O OG1 . THR B 417 ? 2.0392 1.5679 2.5702 0.1239  -0.4197 0.1482  417 THR B OG1 
6674 C CG2 . THR B 417 ? 2.0621 1.5046 2.5689 0.1049  -0.4846 0.1634  417 THR B CG2 
6675 N N   . GLY B 418 ? 2.2732 1.8069 2.6939 0.1966  -0.4041 0.1098  418 GLY B N   
6676 C CA  . GLY B 418 ? 2.0936 1.6540 2.4899 0.2222  -0.3823 0.0960  418 GLY B CA  
6677 C C   . GLY B 418 ? 2.0249 1.5992 2.4481 0.2090  -0.3681 0.0979  418 GLY B C   
6678 O O   . GLY B 418 ? 2.0822 1.6620 2.4769 0.2295  -0.3593 0.0862  418 GLY B O   
6679 N N   . GLU B 419 ? 1.9960 1.5778 2.4739 0.1759  -0.3654 0.1131  419 GLU B N   
6680 C CA  . GLU B 419 ? 2.0605 1.6530 2.5651 0.1610  -0.3533 0.1170  419 GLU B CA  
6681 C C   . GLU B 419 ? 2.1441 1.7735 2.7202 0.1296  -0.3350 0.1339  419 GLU B C   
6682 O O   . GLU B 419 ? 2.5277 2.1487 3.1287 0.1120  -0.3478 0.1463  419 GLU B O   
6683 C CB  . GLU B 419 ? 2.3025 1.8339 2.7720 0.1582  -0.3868 0.1168  419 GLU B CB  
6684 C CG  . GLU B 419 ? 2.4016 1.8852 2.8638 0.1442  -0.4230 0.1272  419 GLU B CG  
6685 C CD  . GLU B 419 ? 2.5858 2.0255 3.0449 0.1244  -0.4496 0.1369  419 GLU B CD  
6686 O OE1 . GLU B 419 ? 2.8634 2.2654 3.2740 0.1393  -0.4651 0.1264  419 GLU B OE1 
6687 O OE2 . GLU B 419 ? 2.2821 1.7279 2.7891 0.0936  -0.4546 0.1564  419 GLU B OE2 
6688 N N   . GLY B 420 ? 1.9904 1.6602 2.5973 0.1242  -0.3052 0.1340  420 GLY B N   
6689 C CA  . GLY B 420 ? 1.9743 1.6775 2.6438 0.0982  -0.2860 0.1484  420 GLY B CA  
6690 C C   . GLY B 420 ? 1.6875 1.4374 2.3790 0.1010  -0.2507 0.1438  420 GLY B C   
6691 O O   . GLY B 420 ? 1.4739 1.2281 2.1352 0.1191  -0.2424 0.1313  420 GLY B O   
6692 N N   . VAL B 421 ? 1.5212 1.3069 2.2662 0.0836  -0.2304 0.1545  421 VAL B N   
6693 C CA  . VAL B 421 ? 1.4491 1.2729 2.2213 0.0801  -0.1998 0.1537  421 VAL B CA  
6694 C C   . VAL B 421 ? 1.6421 1.5049 2.4403 0.0808  -0.1797 0.1545  421 VAL B C   
6695 O O   . VAL B 421 ? 1.7381 1.6070 2.5627 0.0711  -0.1829 0.1633  421 VAL B O   
6696 C CB  . VAL B 421 ? 1.3381 1.1676 2.1471 0.0599  -0.1914 0.1653  421 VAL B CB  
6697 C CG1 . VAL B 421 ? 1.3388 1.2002 2.1625 0.0611  -0.1617 0.1610  421 VAL B CG1 
6698 C CG2 . VAL B 421 ? 1.3245 1.1146 2.1131 0.0538  -0.2146 0.1689  421 VAL B CG2 
6699 N N   . ALA B 422 ? 1.5500 1.4382 2.3385 0.0925  -0.1603 0.1456  422 ALA B N   
6700 C CA  . ALA B 422 ? 1.4539 1.3795 2.2645 0.0920  -0.1404 0.1466  422 ALA B CA  
6701 C C   . ALA B 422 ? 1.4100 1.3596 2.2380 0.0880  -0.1166 0.1453  422 ALA B C   
6702 O O   . ALA B 422 ? 1.5755 1.5215 2.3820 0.0956  -0.1126 0.1380  422 ALA B O   
6703 C CB  . ALA B 422 ? 1.4084 1.3426 2.1874 0.1102  -0.1438 0.1393  422 ALA B CB  
6704 N N   . LEU B 423 ? 1.2478 1.2198 2.1138 0.0762  -0.1017 0.1524  423 LEU B N   
6705 C CA  . LEU B 423 ? 1.2566 1.2489 2.1406 0.0715  -0.0799 0.1521  423 LEU B CA  
6706 C C   . LEU B 423 ? 1.1890 1.2082 2.0678 0.0778  -0.0676 0.1482  423 LEU B C   
6707 O O   . LEU B 423 ? 1.4240 1.4538 2.2973 0.0822  -0.0722 0.1490  423 LEU B O   
6708 C CB  . LEU B 423 ? 1.3770 1.3749 2.3022 0.0568  -0.0706 0.1619  423 LEU B CB  
6709 C CG  . LEU B 423 ? 1.3332 1.3117 2.2691 0.0478  -0.0803 0.1693  423 LEU B CG  
6710 C CD1 . LEU B 423 ? 1.5477 1.5127 2.4829 0.0463  -0.1010 0.1741  423 LEU B CD1 
6711 C CD2 . LEU B 423 ? 1.4407 1.4337 2.4162 0.0369  -0.0650 0.1786  423 LEU B CD2 
6712 N N   . HIS B 424 ? 1.0187 1.0487 1.8985 0.0772  -0.0525 0.1451  424 HIS B N   
6713 C CA  . HIS B 424 ? 1.1510 1.2062 2.0301 0.0791  -0.0406 0.1438  424 HIS B CA  
6714 C C   . HIS B 424 ? 1.1088 1.1694 2.0120 0.0690  -0.0250 0.1465  424 HIS B C   
6715 O O   . HIS B 424 ? 0.9349 0.9834 1.8458 0.0648  -0.0192 0.1464  424 HIS B O   
6716 C CB  . HIS B 424 ? 1.1612 1.2245 2.0077 0.0924  -0.0406 0.1364  424 HIS B CB  
6717 C CG  . HIS B 424 ? 1.3511 1.4001 2.1683 0.1057  -0.0564 0.1316  424 HIS B CG  
6718 N ND1 . HIS B 424 ? 1.6202 1.6556 2.4092 0.1166  -0.0608 0.1239  424 HIS B ND1 
6719 C CD2 . HIS B 424 ? 1.4299 1.4708 2.2385 0.1107  -0.0702 0.1329  424 HIS B CD2 
6720 C CE1 . HIS B 424 ? 1.8052 1.8240 2.5675 0.1291  -0.0773 0.1201  424 HIS B CE1 
6721 N NE2 . HIS B 424 ? 1.7480 1.7695 2.5213 0.1256  -0.0832 0.1255  424 HIS B NE2 
6722 N N   . VAL B 425 ? 1.1211 1.2001 2.0322 0.0659  -0.0183 0.1491  425 VAL B N   
6723 C CA  . VAL B 425 ? 1.1775 1.2593 2.1020 0.0592  -0.0050 0.1499  425 VAL B CA  
6724 C C   . VAL B 425 ? 1.1583 1.2284 2.1101 0.0527  -0.0013 0.1544  425 VAL B C   
6725 O O   . VAL B 425 ? 1.0197 1.0818 1.9769 0.0511  0.0082  0.1534  425 VAL B O   
6726 C CB  . VAL B 425 ? 0.9583 1.0363 1.8651 0.0627  0.0024  0.1436  425 VAL B CB  
6727 C CG1 . VAL B 425 ? 0.9384 1.0188 1.8511 0.0573  0.0140  0.1439  425 VAL B CG1 
6728 C CG2 . VAL B 425 ? 0.8157 0.9039 1.6944 0.0727  -0.0032 0.1390  425 VAL B CG2 
6729 N N   . LEU B 426 ? 1.1189 1.1896 2.0874 0.0496  -0.0092 0.1601  426 LEU B N   
6730 C CA  . LEU B 426 ? 1.0197 1.0831 2.0159 0.0445  -0.0077 0.1662  426 LEU B CA  
6731 C C   . LEU B 426 ? 1.0008 1.0670 2.0138 0.0421  0.0058  0.1676  426 LEU B C   
6732 O O   . LEU B 426 ? 0.9743 1.0372 2.0072 0.0409  0.0129  0.1715  426 LEU B O   
6733 C CB  . LEU B 426 ? 0.9467 1.0107 1.9541 0.0423  -0.0211 0.1718  426 LEU B CB  
6734 C CG  . LEU B 426 ? 0.9754 1.0286 1.9656 0.0456  -0.0366 0.1708  426 LEU B CG  
6735 C CD1 . LEU B 426 ? 0.9247 0.9791 1.9114 0.0466  -0.0507 0.1735  426 LEU B CD1 
6736 C CD2 . LEU B 426 ? 1.1132 1.1542 2.1205 0.0403  -0.0392 0.1765  426 LEU B CD2 
6737 N N   . GLY B 427 ? 1.0984 1.1707 2.1018 0.0420  0.0085  0.1652  427 GLY B N   
6738 C CA  . GLY B 427 ? 1.3377 1.4072 2.3515 0.0405  0.0173  0.1660  427 GLY B CA  
6739 C C   . GLY B 427 ? 1.2714 1.3320 2.2818 0.0438  0.0308  0.1623  427 GLY B C   
6740 O O   . GLY B 427 ? 1.2755 1.3301 2.2972 0.0458  0.0393  0.1633  427 GLY B O   
6741 N N   . ALA B 428 ? 0.9919 1.0508 1.9844 0.0457  0.0322  0.1578  428 ALA B N   
6742 C CA  . ALA B 428 ? 1.0639 1.1140 2.0485 0.0484  0.0443  0.1541  428 ALA B CA  
6743 C C   . ALA B 428 ? 1.2297 1.2780 2.2352 0.0492  0.0509  0.1594  428 ALA B C   
6744 O O   . ALA B 428 ? 1.3106 1.3538 2.3157 0.0523  0.0634  0.1587  428 ALA B O   
6745 C CB  . ALA B 428 ? 1.0097 1.0589 1.9689 0.0500  0.0420  0.1484  428 ALA B CB  
6746 N N   . LEU B 429 ? 1.3586 1.4120 2.3818 0.0461  0.0416  0.1659  429 LEU B N   
6747 C CA  . LEU B 429 ? 1.3990 1.4550 2.4455 0.0443  0.0444  0.1744  429 LEU B CA  
6748 C C   . LEU B 429 ? 1.4013 1.4614 2.4657 0.0488  0.0600  0.1778  429 LEU B C   
6749 O O   . LEU B 429 ? 1.0893 1.1493 2.1530 0.0512  0.0718  0.1791  429 LEU B O   
6750 C CB  . LEU B 429 ? 1.3714 1.4315 2.4362 0.0394  0.0298  0.1820  429 LEU B CB  
6751 C CG  . LEU B 429 ? 1.3086 1.3603 2.3566 0.0364  0.0147  0.1811  429 LEU B CG  
6752 C CD1 . LEU B 429 ? 1.4966 1.5473 2.5590 0.0317  -0.0017 0.1886  429 LEU B CD1 
6753 C CD2 . LEU B 429 ? 1.0416 1.0875 2.0847 0.0347  0.0192  0.1829  429 LEU B CD2 
6754 N N   . ASN B 430 ? 1.4617 1.5248 2.5396 0.0511  0.0596  0.1791  430 ASN B N   
6755 C CA  . ASN B 430 ? 1.6486 1.7159 2.7455 0.0583  0.0725  0.1832  430 ASN B CA  
6756 C C   . ASN B 430 ? 1.4743 1.5306 2.5491 0.0660  0.0864  0.1754  430 ASN B C   
6757 O O   . ASN B 430 ? 1.2099 1.2694 2.2928 0.0741  0.1007  0.1783  430 ASN B O   
6758 C CB  . ASN B 430 ? 2.0592 2.1279 3.1717 0.0599  0.0667  0.1855  430 ASN B CB  
6759 C CG  . ASN B 430 ? 2.3553 2.4339 3.4958 0.0682  0.0772  0.1931  430 ASN B CG  
6760 O OD1 . ASN B 430 ? 2.5928 2.6677 3.7271 0.0788  0.0918  0.1902  430 ASN B OD1 
6761 N ND2 . ASN B 430 ? 2.3924 2.4839 3.5627 0.0648  0.0697  0.2030  430 ASN B ND2 
6762 N N   . ALA B 431 ? 1.7210 1.7656 2.7672 0.0636  0.0814  0.1664  431 ALA B N   
6763 C CA  . ALA B 431 ? 1.8635 1.8927 2.8860 0.0692  0.0887  0.1586  431 ALA B CA  
6764 C C   . ALA B 431 ? 1.8614 1.8850 2.8639 0.0705  0.0975  0.1544  431 ALA B C   
6765 O O   . ALA B 431 ? 1.7585 1.7725 2.7509 0.0786  0.1099  0.1516  431 ALA B O   
6766 C CB  . ALA B 431 ? 1.7023 1.7246 2.7084 0.0639  0.0764  0.1543  431 ALA B CB  
6767 N N   . CYS B 432 ? 1.7917 1.8191 2.7853 0.0638  0.0903  0.1535  432 CYS B N   
6768 C CA  . CYS B 432 ? 1.5119 1.5321 2.4841 0.0643  0.0963  0.1490  432 CYS B CA  
6769 C C   . CYS B 432 ? 1.2654 1.2933 2.2486 0.0608  0.0961  0.1553  432 CYS B C   
6770 O O   . CYS B 432 ? 0.9378 0.9600 1.9064 0.0608  0.1011  0.1535  432 CYS B O   
6771 C CB  . CYS B 432 ? 1.6810 1.6958 2.6270 0.0609  0.0873  0.1417  432 CYS B CB  
6772 S SG  . CYS B 432 ? 2.3317 2.3349 3.2619 0.0618  0.0857  0.1368  432 CYS B SG  
6773 N N   . GLY B 433 ? 1.3256 1.3648 2.3344 0.0570  0.0890  0.1636  433 GLY B N   
6774 C CA  . GLY B 433 ? 1.5079 1.5512 2.5254 0.0510  0.0831  0.1708  433 GLY B CA  
6775 C C   . GLY B 433 ? 1.4633 1.4963 2.4537 0.0481  0.0712  0.1639  433 GLY B C   
6776 O O   . GLY B 433 ? 1.6437 1.6701 2.6226 0.0461  0.0717  0.1644  433 GLY B O   
6777 N N   . PHE B 434 ? 1.2390 1.2717 2.2192 0.0487  0.0605  0.1583  434 PHE B N   
6778 C CA  . PHE B 434 ? 1.1383 1.1649 2.0928 0.0494  0.0489  0.1517  434 PHE B CA  
6779 C C   . PHE B 434 ? 1.1278 1.1579 2.0857 0.0485  0.0327  0.1535  434 PHE B C   
6780 O O   . PHE B 434 ? 1.6804 1.7188 2.6533 0.0476  0.0306  0.1563  434 PHE B O   
6781 C CB  . PHE B 434 ? 1.2434 1.2692 2.1749 0.0533  0.0530  0.1428  434 PHE B CB  
6782 C CG  . PHE B 434 ? 1.2189 1.2447 2.1255 0.0566  0.0416  0.1368  434 PHE B CG  
6783 C CD1 . PHE B 434 ? 1.2414 1.2572 2.1267 0.0591  0.0406  0.1322  434 PHE B CD1 
6784 C CD2 . PHE B 434 ? 1.2537 1.2902 2.1573 0.0586  0.0319  0.1363  434 PHE B CD2 
6785 C CE1 . PHE B 434 ? 1.2812 1.2979 2.1431 0.0651  0.0301  0.1265  434 PHE B CE1 
6786 C CE2 . PHE B 434 ? 1.1803 1.2203 2.0605 0.0648  0.0228  0.1313  434 PHE B CE2 
6787 C CZ  . PHE B 434 ? 1.1170 1.1469 1.9762 0.0689  0.0219  0.1260  434 PHE B CZ  
6788 N N   . VAL B 435 ? 0.8918 0.9132 1.8309 0.0500  0.0201  0.1508  435 VAL B N   
6789 C CA  . VAL B 435 ? 1.0142 1.0357 1.9475 0.0522  0.0041  0.1505  435 VAL B CA  
6790 C C   . VAL B 435 ? 1.1435 1.1535 2.0438 0.0593  -0.0071 0.1433  435 VAL B C   
6791 O O   . VAL B 435 ? 1.4197 1.4162 2.3077 0.0590  -0.0081 0.1417  435 VAL B O   
6792 C CB  . VAL B 435 ? 1.0729 1.0925 2.0309 0.0459  -0.0049 0.1603  435 VAL B CB  
6793 C CG1 . VAL B 435 ? 1.2529 1.2598 2.2159 0.0398  -0.0098 0.1669  435 VAL B CG1 
6794 C CG2 . VAL B 435 ? 1.0245 1.0424 1.9741 0.0490  -0.0215 0.1595  435 VAL B CG2 
6795 N N   . GLU B 436 ? 1.1308 1.1467 2.0151 0.0669  -0.0161 0.1390  436 GLU B N   
6796 C CA  . GLU B 436 ? 1.1132 1.1171 1.9661 0.0770  -0.0310 0.1330  436 GLU B CA  
6797 C C   . GLU B 436 ? 1.1944 1.1826 2.0492 0.0756  -0.0488 0.1375  436 GLU B C   
6798 O O   . GLU B 436 ? 1.1104 1.1058 1.9844 0.0712  -0.0513 0.1432  436 GLU B O   
6799 C CB  . GLU B 436 ? 1.1299 1.1513 1.9619 0.0887  -0.0311 0.1270  436 GLU B CB  
6800 C CG  . GLU B 436 ? 1.2891 1.3281 2.1209 0.0882  -0.0160 0.1246  436 GLU B CG  
6801 C CD  . GLU B 436 ? 1.5690 1.6263 2.3767 0.1006  -0.0179 0.1199  436 GLU B CD  
6802 O OE1 . GLU B 436 ? 1.6937 1.7619 2.4951 0.1074  -0.0255 0.1212  436 GLU B OE1 
6803 O OE2 . GLU B 436 ? 1.6374 1.7001 2.4327 0.1039  -0.0117 0.1160  436 GLU B OE2 
6804 N N   . LEU B 437 ? 1.3951 1.3584 2.2269 0.0793  -0.0634 0.1348  437 LEU B N   
6805 C CA  . LEU B 437 ? 1.6839 1.6251 2.5065 0.0800  -0.0853 0.1376  437 LEU B CA  
6806 C C   . LEU B 437 ? 1.5008 1.4223 2.2776 0.0969  -0.1012 0.1272  437 LEU B C   
6807 O O   . LEU B 437 ? 1.2394 1.1519 1.9938 0.1035  -0.1005 0.1206  437 LEU B O   
6808 C CB  . LEU B 437 ? 1.6550 1.5800 2.5007 0.0644  -0.0941 0.1493  437 LEU B CB  
6809 C CG  . LEU B 437 ? 1.4959 1.3970 2.3287 0.0596  -0.1018 0.1508  437 LEU B CG  
6810 C CD1 . LEU B 437 ? 1.7201 1.5846 2.5165 0.0662  -0.1303 0.1473  437 LEU B CD1 
6811 C CD2 . LEU B 437 ? 1.3186 1.2252 2.1893 0.0413  -0.0957 0.1656  437 LEU B CD2 
6812 N N   . THR B 438 ? 1.4967 1.4094 2.2581 0.1051  -0.1168 0.1260  438 THR B N   
6813 C CA  . THR B 438 ? 1.4715 1.3624 2.1863 0.1246  -0.1347 0.1163  438 THR B CA  
6814 C C   . THR B 438 ? 1.6831 1.5382 2.3867 0.1220  -0.1609 0.1202  438 THR B C   
6815 O O   . THR B 438 ? 1.5885 1.4476 2.3131 0.1137  -0.1648 0.1277  438 THR B O   
6816 C CB  . THR B 438 ? 1.3634 1.2816 2.0614 0.1424  -0.1274 0.1098  438 THR B CB  
6817 O OG1 . THR B 438 ? 1.3099 1.2548 2.0144 0.1434  -0.1074 0.1071  438 THR B OG1 
6818 C CG2 . THR B 438 ? 1.2991 1.1945 1.9472 0.1659  -0.1468 0.1003  438 THR B CG2 
6819 N N   . ALA B 439 ? 1.7247 1.5422 2.3915 0.1301  -0.1809 0.1146  439 ALA B N   
6820 C CA  . ALA B 439 ? 1.8204 1.5941 2.4701 0.1264  -0.2107 0.1185  439 ALA B CA  
6821 C C   . ALA B 439 ? 1.6151 1.3574 2.2052 0.1528  -0.2317 0.1053  439 ALA B C   
6822 O O   . ALA B 439 ? 1.6674 1.4050 2.2266 0.1691  -0.2300 0.0947  439 ALA B O   
6823 C CB  . ALA B 439 ? 1.7913 1.5426 2.4549 0.1067  -0.2186 0.1276  439 ALA B CB  
6824 N N   . LEU B 440 ? 1.6496 1.3715 2.2240 0.1578  -0.2511 0.1061  440 LEU B N   
6825 C CA  . LEU B 440 ? 1.9167 1.6090 2.4325 0.1857  -0.2713 0.0937  440 LEU B CA  
6826 C C   . LEU B 440 ? 2.3465 1.9787 2.8354 0.1813  -0.3086 0.0967  440 LEU B C   
6827 O O   . LEU B 440 ? 2.5042 2.1308 3.0198 0.1628  -0.3175 0.1084  440 LEU B O   
6828 C CB  . LEU B 440 ? 1.7027 1.4269 2.2168 0.2000  -0.2602 0.0910  440 LEU B CB  
6829 C CG  . LEU B 440 ? 1.6650 1.4456 2.1941 0.2088  -0.2285 0.0875  440 LEU B CG  
6830 C CD1 . LEU B 440 ? 1.7431 1.5625 2.3334 0.1826  -0.2051 0.0993  440 LEU B CD1 
6831 C CD2 . LEU B 440 ? 1.7372 1.5355 2.2365 0.2342  -0.2272 0.0813  440 LEU B CD2 
6832 N N   . ALA B 441 ? 2.4539 2.0412 2.8902 0.1982  -0.3307 0.0867  441 ALA B N   
6833 C CA  . ALA B 441 ? 2.3204 1.8426 2.7198 0.1972  -0.3707 0.0879  441 ALA B CA  
6834 C C   . ALA B 441 ? 2.3801 1.8600 2.7044 0.2332  -0.3927 0.0703  441 ALA B C   
6835 O O   . ALA B 441 ? 2.6353 2.1352 2.9326 0.2611  -0.3780 0.0566  441 ALA B O   
6836 C CB  . ALA B 441 ? 2.3227 1.8187 2.7426 0.1688  -0.3846 0.1005  441 ALA B CB  
6837 N N   . ARG B 442 ? 2.2408 1.6564 2.5289 0.2319  -0.4319 0.0716  442 ARG B N   
6838 C CA  . ARG B 442 ? 2.5421 1.9021 2.7521 0.2654  -0.4613 0.0557  442 ARG B CA  
6839 C C   . ARG B 442 ? 2.4656 1.7994 2.6417 0.2774  -0.4687 0.0461  442 ARG B C   
6840 O O   . ARG B 442 ? 2.3835 1.6953 2.4994 0.3141  -0.4776 0.0290  442 ARG B O   
6841 C CB  . ARG B 442 ? 2.8278 2.1268 3.0155 0.2552  -0.5018 0.0626  442 ARG B CB  
6842 C CG  . ARG B 442 ? 2.8110 2.1321 3.0199 0.2513  -0.4964 0.0686  442 ARG B CG  
6843 C CD  . ARG B 442 ? 3.2398 2.5503 3.3906 0.2908  -0.5018 0.0528  442 ARG B CD  
6844 N NE  . ARG B 442 ? 3.5623 2.9225 3.7006 0.3219  -0.4698 0.0393  442 ARG B NE  
6845 C CZ  . ARG B 442 ? 3.4991 2.9063 3.6412 0.3389  -0.4470 0.0362  442 ARG B CZ  
6846 N NH1 . ARG B 442 ? 3.6375 3.0478 3.7958 0.3280  -0.4513 0.0443  442 ARG B NH1 
6847 N NH2 . ARG B 442 ? 3.2535 2.7047 3.3825 0.3666  -0.4212 0.0259  442 ARG B NH2 
6848 N N   . SER B 443 ? 2.3244 1.6624 2.5389 0.2475  -0.4644 0.0576  443 SER B N   
6849 C CA  . SER B 443 ? 2.3384 1.6578 2.5300 0.2536  -0.4679 0.0509  443 SER B CA  
6850 C C   . SER B 443 ? 2.1827 1.5637 2.4352 0.2335  -0.4295 0.0586  443 SER B C   
6851 O O   . SER B 443 ? 2.5862 2.0040 2.8979 0.2060  -0.4122 0.0735  443 SER B O   
6852 C CB  . SER B 443 ? 2.6576 1.9058 2.8248 0.2360  -0.5096 0.0585  443 SER B CB  
6853 O OG  . SER B 443 ? 2.6993 1.9627 2.9280 0.1929  -0.5064 0.0810  443 SER B OG  
6854 N N   . PRO B 444 ? 2.0026 1.3954 2.2424 0.2466  -0.4159 0.0491  444 PRO B N   
6855 C CA  . PRO B 444 ? 2.2413 1.6913 2.5347 0.2297  -0.3793 0.0553  444 PRO B CA  
6856 C C   . PRO B 444 ? 2.5323 1.9758 2.8687 0.1904  -0.3825 0.0739  444 PRO B C   
6857 O O   . PRO B 444 ? 2.6668 2.1600 3.0604 0.1700  -0.3536 0.0845  444 PRO B O   
6858 C CB  . PRO B 444 ? 1.9144 1.3725 2.1787 0.2540  -0.3686 0.0409  444 PRO B CB  
6859 C CG  . PRO B 444 ? 2.2110 1.6118 2.4014 0.2867  -0.4020 0.0261  444 PRO B CG  
6860 C CD  . PRO B 444 ? 2.0885 1.4376 2.2612 0.2778  -0.4363 0.0324  444 PRO B CD  
6861 N N   . GLU B 445 ? 2.7244 2.1069 3.0322 0.1807  -0.4186 0.0787  445 GLU B N   
6862 C CA  . GLU B 445 ? 3.0864 2.4604 3.4320 0.1427  -0.4263 0.0994  445 GLU B CA  
6863 C C   . GLU B 445 ? 2.9537 2.3582 3.3538 0.1190  -0.4173 0.1162  445 GLU B C   
6864 O O   . GLU B 445 ? 2.9808 2.4248 3.4378 0.0931  -0.3954 0.1316  445 GLU B O   
6865 C CB  . GLU B 445 ? 3.6292 2.9250 3.9227 0.1414  -0.4738 0.1004  445 GLU B CB  
6866 C CG  . GLU B 445 ? 4.2741 3.5349 4.5053 0.1716  -0.4855 0.0807  445 GLU B CG  
6867 C CD  . GLU B 445 ? 4.2264 3.4082 4.3832 0.1925  -0.5322 0.0702  445 GLU B CD  
6868 O OE1 . GLU B 445 ? 4.2562 3.4271 4.3914 0.2097  -0.5421 0.0637  445 GLU B OE1 
6869 O OE2 . GLU B 445 ? 3.9996 3.1288 4.1160 0.1938  -0.5593 0.0676  445 GLU B OE2 
6870 N N   . ALA B 446 ? 2.8198 2.2045 3.1986 0.1307  -0.4350 0.1124  446 ALA B N   
6871 C CA  . ALA B 446 ? 2.4878 1.8952 2.9116 0.1114  -0.4313 0.1270  446 ALA B CA  
6872 C C   . ALA B 446 ? 2.2750 1.7560 2.7533 0.1084  -0.3860 0.1283  446 ALA B C   
6873 O O   . ALA B 446 ? 2.2498 1.7627 2.7846 0.0826  -0.3721 0.1452  446 ALA B O   
6874 C CB  . ALA B 446 ? 2.3472 1.7188 2.7314 0.1284  -0.4576 0.1201  446 ALA B CB  
6875 N N   . ALA B 447 ? 2.0821 1.5883 2.5408 0.1357  -0.3649 0.1110  447 ALA B N   
6876 C CA  . ALA B 447 ? 1.9383 1.5095 2.4394 0.1359  -0.3247 0.1103  447 ALA B CA  
6877 C C   . ALA B 447 ? 1.8452 1.4453 2.3923 0.1126  -0.3025 0.1212  447 ALA B C   
6878 O O   . ALA B 447 ? 1.7911 1.4327 2.3901 0.0962  -0.2795 0.1317  447 ALA B O   
6879 C CB  . ALA B 447 ? 1.8328 1.4213 2.2997 0.1682  -0.3107 0.0917  447 ALA B CB  
6880 N N   . ASP B 448 ? 1.8679 1.4433 2.3916 0.1131  -0.3107 0.1182  448 ASP B N   
6881 C CA  . ASP B 448 ? 2.1899 1.7863 2.7471 0.0936  -0.2920 0.1273  448 ASP B CA  
6882 C C   . ASP B 448 ? 1.9867 1.5896 2.5916 0.0621  -0.2950 0.1497  448 ASP B C   
6883 O O   . ASP B 448 ? 1.8304 1.4754 2.4830 0.0475  -0.2677 0.1592  448 ASP B O   
6884 C CB  . ASP B 448 ? 2.8085 2.3682 3.3260 0.0993  -0.3071 0.1210  448 ASP B CB  
6885 C CG  . ASP B 448 ? 2.8330 2.3998 3.3148 0.1283  -0.2957 0.1011  448 ASP B CG  
6886 O OD1 . ASP B 448 ? 2.4698 2.0182 2.9082 0.1552  -0.3090 0.0871  448 ASP B OD1 
6887 O OD2 . ASP B 448 ? 2.8370 2.4285 3.3339 0.1247  -0.2736 0.1002  448 ASP B OD2 
6888 N N   . GLY B 449 ? 1.9706 1.5302 2.5596 0.0531  -0.3298 0.1582  449 GLY B N   
6889 C CA  . GLY B 449 ? 2.1449 1.7073 2.7763 0.0229  -0.3390 0.1819  449 GLY B CA  
6890 C C   . GLY B 449 ? 2.0774 1.6879 2.7588 0.0172  -0.3153 0.1886  449 GLY B C   
6891 O O   . GLY B 449 ? 2.0595 1.7044 2.7922 -0.0030 -0.2980 0.2051  449 GLY B O   
6892 N N   . TYR B 450 ? 1.9812 1.5931 2.6448 0.0366  -0.3153 0.1757  450 TYR B N   
6893 C CA  . TYR B 450 ? 1.6919 1.3442 2.3951 0.0343  -0.2960 0.1797  450 TYR B CA  
6894 C C   . TYR B 450 ? 1.5988 1.3043 2.3418 0.0314  -0.2561 0.1800  450 TYR B C   
6895 O O   . TYR B 450 ? 1.6988 1.4375 2.4916 0.0162  -0.2402 0.1932  450 TYR B O   
6896 C CB  . TYR B 450 ? 1.6151 1.2628 2.2841 0.0598  -0.2987 0.1628  450 TYR B CB  
6897 C CG  . TYR B 450 ? 1.8487 1.4678 2.5094 0.0564  -0.3272 0.1689  450 TYR B CG  
6898 C CD1 . TYR B 450 ? 1.9209 1.5456 2.6258 0.0305  -0.3346 0.1894  450 TYR B CD1 
6899 C CD2 . TYR B 450 ? 2.0063 1.5935 2.6147 0.0797  -0.3467 0.1549  450 TYR B CD2 
6900 C CE1 . TYR B 450 ? 2.2001 1.7978 2.8986 0.0257  -0.3621 0.1961  450 TYR B CE1 
6901 C CE2 . TYR B 450 ? 2.2886 1.8453 2.8861 0.0764  -0.3745 0.1605  450 TYR B CE2 
6902 C CZ  . TYR B 450 ? 2.3579 1.9196 3.0015 0.0484  -0.3825 0.1811  450 TYR B CZ  
6903 O OH  . TYR B 450 ? 2.8157 2.3472 3.4502 0.0437  -0.4110 0.1876  450 TYR B OH  
6904 N N   . SER B 451 ? 1.4116 1.1223 2.1292 0.0476  -0.2419 0.1650  451 SER B N   
6905 C CA  . SER B 451 ? 1.3133 1.0669 2.0577 0.0477  -0.2069 0.1625  451 SER B CA  
6906 C C   . SER B 451 ? 1.4302 1.1978 2.2142 0.0249  -0.1966 0.1794  451 SER B C   
6907 O O   . SER B 451 ? 1.4269 1.2324 2.2525 0.0173  -0.1717 0.1863  451 SER B O   
6908 C CB  . SER B 451 ? 1.1888 0.9360 1.8932 0.0674  -0.2016 0.1455  451 SER B CB  
6909 O OG  . SER B 451 ? 1.1745 0.9514 1.8982 0.0643  -0.1737 0.1445  451 SER B OG  
6910 N N   . ARG B 452 ? 1.6712 1.4064 2.4389 0.0152  -0.2172 0.1861  452 ARG B N   
6911 C CA  . ARG B 452 ? 1.8198 1.5659 2.6194 -0.0065 -0.2108 0.2041  452 ARG B CA  
6912 C C   . ARG B 452 ? 1.6103 1.3814 2.4607 -0.0240 -0.2078 0.2236  452 ARG B C   
6913 O O   . ARG B 452 ? 1.4383 1.2463 2.3296 -0.0337 -0.1834 0.2344  452 ARG B O   
6914 C CB  . ARG B 452 ? 2.3417 2.0451 3.1067 -0.0119 -0.2359 0.2062  452 ARG B CB  
6915 C CG  . ARG B 452 ? 2.3754 2.0865 3.1496 -0.0239 -0.2238 0.2144  452 ARG B CG  
6916 C CD  . ARG B 452 ? 1.9787 1.6468 2.7015 -0.0166 -0.2430 0.2042  452 ARG B CD  
6917 N NE  . ARG B 452 ? 1.8503 1.4683 2.5469 -0.0278 -0.2828 0.2135  452 ARG B NE  
6918 C CZ  . ARG B 452 ? 2.0010 1.5693 2.6460 -0.0136 -0.3141 0.2010  452 ARG B CZ  
6919 N NH1 . ARG B 452 ? 1.9425 1.5079 2.5553 0.0147  -0.3086 0.1781  452 ARG B NH1 
6920 N NH2 . ARG B 452 ? 1.9377 1.4587 2.5620 -0.0274 -0.3519 0.2124  452 ARG B NH2 
6921 N N   . ALA B 453 ? 1.6125 1.3623 2.4574 -0.0263 -0.2333 0.2275  453 ALA B N   
6922 C CA  . ALA B 453 ? 1.6641 1.4330 2.5539 -0.0422 -0.2361 0.2461  453 ALA B CA  
6923 C C   . ALA B 453 ? 1.5784 1.3946 2.5044 -0.0359 -0.2030 0.2431  453 ALA B C   
6924 O O   . ALA B 453 ? 1.7235 1.5734 2.6969 -0.0484 -0.1877 0.2592  453 ALA B O   
6925 C CB  . ALA B 453 ? 2.0821 1.8142 2.9470 -0.0396 -0.2693 0.2444  453 ALA B CB  
6926 N N   . ALA B 454 ? 1.4588 1.2767 2.3602 -0.0157 -0.1935 0.2231  454 ALA B N   
6927 C CA  . ALA B 454 ? 1.3588 1.2149 2.2861 -0.0084 -0.1659 0.2182  454 ALA B CA  
6928 C C   . ALA B 454 ? 1.4272 1.3149 2.3812 -0.0124 -0.1361 0.2220  454 ALA B C   
6929 O O   . ALA B 454 ? 1.4771 1.3965 2.4711 -0.0171 -0.1178 0.2305  454 ALA B O   
6930 C CB  . ALA B 454 ? 1.2450 1.0955 2.1368 0.0122  -0.1645 0.1982  454 ALA B CB  
6931 N N   . GLN B 455 ? 1.3623 1.2380 2.2906 -0.0091 -0.1328 0.2152  455 GLN B N   
6932 C CA  . GLN B 455 ? 1.3006 1.1996 2.2449 -0.0113 -0.1064 0.2172  455 GLN B CA  
6933 C C   . GLN B 455 ? 1.2771 1.1960 2.2646 -0.0289 -0.1013 0.2397  455 GLN B C   
6934 O O   . GLN B 455 ? 1.4035 1.3547 2.4214 -0.0289 -0.0760 0.2445  455 GLN B O   
6935 C CB  . GLN B 455 ? 1.4482 1.3275 2.3563 -0.0063 -0.1073 0.2077  455 GLN B CB  
6936 C CG  . GLN B 455 ? 1.7663 1.6332 2.6341 0.0131  -0.1092 0.1865  455 GLN B CG  
6937 C CD  . GLN B 455 ? 1.9995 1.8382 2.8263 0.0190  -0.1198 0.1777  455 GLN B CD  
6938 O OE1 . GLN B 455 ? 2.6130 2.4578 3.4384 0.0173  -0.1052 0.1768  455 GLN B OE1 
6939 N NE2 . GLN B 455 ? 1.5869 1.3926 2.3769 0.0276  -0.1457 0.1703  455 GLN B NE2 
6940 N N   . ALA B 456 ? 1.3741 1.2726 2.3618 -0.0432 -0.1269 0.2538  456 ALA B N   
6941 C CA  . ALA B 456 ? 1.6652 1.5835 2.6942 -0.0623 -0.1268 0.2790  456 ALA B CA  
6942 C C   . ALA B 456 ? 1.6594 1.6119 2.7331 -0.0632 -0.1146 0.2881  456 ALA B C   
6943 O O   . ALA B 456 ? 1.7034 1.6920 2.8152 -0.0677 -0.0933 0.3014  456 ALA B O   
6944 C CB  . ALA B 456 ? 2.2514 2.1369 3.2691 -0.0783 -0.1624 0.2925  456 ALA B CB  
6945 N N   . LEU B 457 ? 1.6115 1.5515 2.6775 -0.0573 -0.1284 0.2803  457 LEU B N   
6946 C CA  . LEU B 457 ? 1.5586 1.5243 2.6618 -0.0576 -0.1219 0.2872  457 LEU B CA  
6947 C C   . LEU B 457 ? 1.5252 1.5240 2.6452 -0.0455 -0.0874 0.2793  457 LEU B C   
6948 O O   . LEU B 457 ? 1.7607 1.7917 2.9224 -0.0487 -0.0731 0.2924  457 LEU B O   
6949 C CB  . LEU B 457 ? 1.6760 1.6171 2.7579 -0.0517 -0.1436 0.2773  457 LEU B CB  
6950 C CG  . LEU B 457 ? 2.0614 2.0228 3.1792 -0.0540 -0.1431 0.2857  457 LEU B CG  
6951 C CD1 . LEU B 457 ? 2.0140 2.0014 3.1815 -0.0709 -0.1429 0.3118  457 LEU B CD1 
6952 C CD2 . LEU B 457 ? 2.3127 2.2411 3.4050 -0.0529 -0.1729 0.2808  457 LEU B CD2 
6953 N N   . LEU B 458 ? 1.5433 1.5327 2.6296 -0.0314 -0.0764 0.2587  458 LEU B N   
6954 C CA  . LEU B 458 ? 1.4526 1.4650 2.5476 -0.0193 -0.0494 0.2490  458 LEU B CA  
6955 C C   . LEU B 458 ? 1.4083 1.4403 2.5164 -0.0196 -0.0256 0.2543  458 LEU B C   
6956 O O   . LEU B 458 ? 1.4531 1.5089 2.5830 -0.0133 -0.0047 0.2551  458 LEU B O   
6957 C CB  . LEU B 458 ? 1.1948 1.1942 2.2547 -0.0054 -0.0488 0.2279  458 LEU B CB  
6958 C CG  . LEU B 458 ? 1.2435 1.2272 2.2918 -0.0038 -0.0710 0.2243  458 LEU B CG  
6959 C CD1 . LEU B 458 ? 1.2732 1.2408 2.2790 0.0091  -0.0760 0.2061  458 LEU B CD1 
6960 C CD2 . LEU B 458 ? 1.2362 1.2380 2.3162 -0.0048 -0.0684 0.2304  458 LEU B CD2 
6961 N N   . THR B 459 ? 1.5118 1.5324 2.6047 -0.0260 -0.0293 0.2582  459 THR B N   
6962 C CA  . THR B 459 ? 1.5787 1.6151 2.6766 -0.0248 -0.0065 0.2615  459 THR B CA  
6963 C C   . THR B 459 ? 1.8752 1.9329 3.0083 -0.0389 -0.0055 0.2866  459 THR B C   
6964 O O   . THR B 459 ? 1.8917 1.9497 3.0189 -0.0449 -0.0010 0.2937  459 THR B O   
6965 C CB  . THR B 459 ? 1.7816 1.7940 2.8381 -0.0215 -0.0080 0.2488  459 THR B CB  
6966 O OG1 . THR B 459 ? 2.1721 2.1585 3.2132 -0.0323 -0.0358 0.2545  459 THR B OG1 
6967 C CG2 . THR B 459 ? 1.7797 1.7811 2.8058 -0.0066 -0.0029 0.2262  459 THR B CG2 
6968 N N   . GLY B 460 ? 2.2402 2.3177 3.4108 -0.0443 -0.0098 0.3010  460 GLY B N   
6969 C CA  . GLY B 460 ? 2.2904 2.3996 3.5021 -0.0555 -0.0040 0.3269  460 GLY B CA  
6970 C C   . GLY B 460 ? 2.1366 2.2785 3.3896 -0.0498 0.0077  0.3351  460 GLY B C   
6971 O O   . GLY B 460 ? 2.2598 2.3969 3.5073 -0.0378 0.0115  0.3199  460 GLY B O   
6972 N N   . PRO B 461 ? 1.7459 1.9240 3.0420 -0.0580 0.0142  0.3604  461 PRO B N   
6973 C CA  . PRO B 461 ? 1.5930 1.8012 2.9318 -0.0551 0.0182  0.3720  461 PRO B CA  
6974 C C   . PRO B 461 ? 1.4177 1.6122 2.7686 -0.0701 -0.0136 0.3816  461 PRO B C   
6975 O O   . PRO B 461 ? 1.5321 1.6901 2.8534 -0.0804 -0.0388 0.3767  461 PRO B O   
6976 C CB  . PRO B 461 ? 1.6797 1.9330 3.0553 -0.0583 0.0370  0.3969  461 PRO B CB  
6977 C CG  . PRO B 461 ? 1.6285 1.8709 2.9722 -0.0566 0.0491  0.3900  461 PRO B CG  
6978 C CD  . PRO B 461 ? 1.6114 1.8069 2.9176 -0.0690 0.0199  0.3798  461 PRO B CD  
6979 N N   . TYR B 462 ? 1.4495 1.6720 2.8425 -0.0707 -0.0136 0.3957  462 TYR B N   
6980 C CA  . TYR B 462 ? 1.4612 1.6699 2.8658 -0.0835 -0.0437 0.4040  462 TYR B CA  
6981 C C   . TYR B 462 ? 1.3546 1.6072 2.8172 -0.0875 -0.0406 0.4288  462 TYR B C   
6982 O O   . TYR B 462 ? 1.1012 1.3497 2.5834 -0.1035 -0.0676 0.4446  462 TYR B O   
6983 C CB  . TYR B 462 ? 1.2363 1.4112 2.6045 -0.0706 -0.0486 0.3757  462 TYR B CB  
6984 C CG  . TYR B 462 ? 1.2618 1.4063 2.6196 -0.0800 -0.0814 0.3747  462 TYR B CG  
6985 C CD1 . TYR B 462 ? 1.4373 1.5963 2.8286 -0.0825 -0.0898 0.3852  462 TYR B CD1 
6986 C CD2 . TYR B 462 ? 1.1516 1.2520 2.4640 -0.0845 -0.1041 0.3630  462 TYR B CD2 
6987 C CE1 . TYR B 462 ? 1.5318 1.6610 2.9112 -0.0906 -0.1203 0.3843  462 TYR B CE1 
6988 C CE2 . TYR B 462 ? 1.4166 1.4869 2.7149 -0.0903 -0.1340 0.3611  462 TYR B CE2 
6989 C CZ  . TYR B 462 ? 1.6303 1.7143 2.9614 -0.0937 -0.1421 0.3717  462 TYR B CZ  
6990 O OH  . TYR B 462 ? 1.8704 1.9221 3.1843 -0.0992 -0.1724 0.3699  462 TYR B OH  
# 
