data_8Z29
# 
_entry.id   8Z29 
# 
_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   8Z29         pdb_00008z29 10.2210/pdb8z29/pdb 
WWPDB D_1300046885 ?            ?                   
# 
_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                        8Z29 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-12 
_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              pbhaumik@iitb.ac.in 
_pdbx_contact_author.name_first         Prasenjit 
_pdbx_contact_author.name_last          Bhaumik 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1257-9809 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Godsora, B.K.J.' 1 0000-0002-0732-998X 
'Bhaumik, P.'     2 0000-0003-1257-9809 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Protein Sci.' 
_citation.journal_id_ASTM           PRCIEI 
_citation.journal_id_CSD            0795 
_citation.journal_id_ISSN           1469-896X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            34 
_citation.language                  ? 
_citation.page_first                e70038 
_citation.page_last                 e70038 
_citation.title                     
'Conformational flexibility associated with remote residues regulates the kinetic properties of glutamate dehydrogenase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/pro.70038 
_citation.pdbx_database_id_PubMed   39981924 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Godsora, B.K.J.' 1 0000-0002-0732-998X 
primary 'Das, P.'         2 ?                   
primary 'Mishra, P.K.'    3 ?                   
primary 'Sairaman, A.'    4 ?                   
primary 'Kaledhonkar, S.' 5 ?                   
primary 'Punekar, N.S.'   6 ?                   
primary 'Bhaumik, P.'     7 0000-0003-1257-9809 
# 
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 'Glutamate dehydrogenase' 49075.258 2  ? ? ? ? 
2 non-polymer syn 'CHLORIDE ION'            35.453    5  ? ? ? ? 
3 water       nat water                     18.015    70 ? ? ? ? 
# 
_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       
;MSNLPVEPEFEQAYKELASTLENSTLFQKNPEYRKALAVVSVPERVIQFRVVWENDKGEVQVNRGFRVQFNSALGPYKGG
LRFHPSVNLSILKFLGFEQIFKNALTGLNMGGGKGGSDFDPKGKSDSEIRRFCVAFMTELCRHIGADTDVPAGDIGVTGR
EIGYLFGQYRKLRNSWEGVLTGKGGSWGGSLIRPEATGYGVVYYVEHMIAHATNGAESFAGKRVAISGSGNVAQYAALKV
IELGGRVVSLSDSQGSLIVKDKDSFTPAEIDAIAALKVDRKQIAELVTDAAFADKFTYLPGQRPWVHVGAVDVALPSATQ
NEVSGEEAQALIAAGCKFIAEGSNMGCTQAAIDAFEAHREANKGAAAIWYAPGKAANAGGVAVSGLEMAQNSARLSWTAE
EVDARLKDIMKSCFQNGLDTAKEYATPADGILPSLVTGSNIAGFTKVAAAMKDQGDWW
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSNLPVEPEFEQAYKELASTLENSTLFQKNPEYRKALAVVSVPERVIQFRVVWENDKGEVQVNRGFRVQFNSALGPYKGG
LRFHPSVNLSILKFLGFEQIFKNALTGLNMGGGKGGSDFDPKGKSDSEIRRFCVAFMTELCRHIGADTDVPAGDIGVTGR
EIGYLFGQYRKLRNSWEGVLTGKGGSWGGSLIRPEATGYGVVYYVEHMIAHATNGAESFAGKRVAISGSGNVAQYAALKV
IELGGRVVSLSDSQGSLIVKDKDSFTPAEIDAIAALKVDRKQIAELVTDAAFADKFTYLPGQRPWVHVGAVDVALPSATQ
NEVSGEEAQALIAAGCKFIAEGSNMGCTQAAIDAFEAHREANKGAAAIWYAPGKAANAGGVAVSGLEMAQNSARLSWTAE
EVDARLKDIMKSCFQNGLDTAKEYATPADGILPSLVTGSNIAGFTKVAAAMKDQGDWW
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CHLORIDE ION' CL  
3 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   ASN n 
1 4   LEU n 
1 5   PRO n 
1 6   VAL n 
1 7   GLU n 
1 8   PRO n 
1 9   GLU n 
1 10  PHE n 
1 11  GLU n 
1 12  GLN n 
1 13  ALA n 
1 14  TYR n 
1 15  LYS n 
1 16  GLU n 
1 17  LEU n 
1 18  ALA n 
1 19  SER n 
1 20  THR n 
1 21  LEU n 
1 22  GLU n 
1 23  ASN n 
1 24  SER n 
1 25  THR n 
1 26  LEU n 
1 27  PHE n 
1 28  GLN n 
1 29  LYS n 
1 30  ASN n 
1 31  PRO n 
1 32  GLU n 
1 33  TYR n 
1 34  ARG n 
1 35  LYS n 
1 36  ALA n 
1 37  LEU n 
1 38  ALA n 
1 39  VAL n 
1 40  VAL n 
1 41  SER n 
1 42  VAL n 
1 43  PRO n 
1 44  GLU n 
1 45  ARG n 
1 46  VAL n 
1 47  ILE n 
1 48  GLN n 
1 49  PHE n 
1 50  ARG n 
1 51  VAL n 
1 52  VAL n 
1 53  TRP n 
1 54  GLU n 
1 55  ASN n 
1 56  ASP n 
1 57  LYS n 
1 58  GLY n 
1 59  GLU n 
1 60  VAL n 
1 61  GLN n 
1 62  VAL n 
1 63  ASN n 
1 64  ARG n 
1 65  GLY n 
1 66  PHE n 
1 67  ARG n 
1 68  VAL n 
1 69  GLN n 
1 70  PHE n 
1 71  ASN n 
1 72  SER n 
1 73  ALA n 
1 74  LEU n 
1 75  GLY n 
1 76  PRO n 
1 77  TYR n 
1 78  LYS n 
1 79  GLY n 
1 80  GLY n 
1 81  LEU n 
1 82  ARG n 
1 83  PHE n 
1 84  HIS n 
1 85  PRO n 
1 86  SER n 
1 87  VAL n 
1 88  ASN n 
1 89  LEU n 
1 90  SER n 
1 91  ILE n 
1 92  LEU n 
1 93  LYS n 
1 94  PHE n 
1 95  LEU n 
1 96  GLY n 
1 97  PHE n 
1 98  GLU n 
1 99  GLN n 
1 100 ILE n 
1 101 PHE n 
1 102 LYS n 
1 103 ASN n 
1 104 ALA n 
1 105 LEU n 
1 106 THR n 
1 107 GLY n 
1 108 LEU n 
1 109 ASN n 
1 110 MET n 
1 111 GLY n 
1 112 GLY n 
1 113 GLY n 
1 114 LYS n 
1 115 GLY n 
1 116 GLY n 
1 117 SER n 
1 118 ASP n 
1 119 PHE n 
1 120 ASP n 
1 121 PRO n 
1 122 LYS n 
1 123 GLY n 
1 124 LYS n 
1 125 SER n 
1 126 ASP n 
1 127 SER n 
1 128 GLU n 
1 129 ILE n 
1 130 ARG n 
1 131 ARG n 
1 132 PHE n 
1 133 CYS n 
1 134 VAL n 
1 135 ALA n 
1 136 PHE n 
1 137 MET n 
1 138 THR n 
1 139 GLU n 
1 140 LEU n 
1 141 CYS n 
1 142 ARG n 
1 143 HIS n 
1 144 ILE n 
1 145 GLY n 
1 146 ALA n 
1 147 ASP n 
1 148 THR n 
1 149 ASP n 
1 150 VAL n 
1 151 PRO n 
1 152 ALA n 
1 153 GLY n 
1 154 ASP n 
1 155 ILE n 
1 156 GLY n 
1 157 VAL n 
1 158 THR n 
1 159 GLY n 
1 160 ARG n 
1 161 GLU n 
1 162 ILE n 
1 163 GLY n 
1 164 TYR n 
1 165 LEU n 
1 166 PHE n 
1 167 GLY n 
1 168 GLN n 
1 169 TYR n 
1 170 ARG n 
1 171 LYS n 
1 172 LEU n 
1 173 ARG n 
1 174 ASN n 
1 175 SER n 
1 176 TRP n 
1 177 GLU n 
1 178 GLY n 
1 179 VAL n 
1 180 LEU n 
1 181 THR n 
1 182 GLY n 
1 183 LYS n 
1 184 GLY n 
1 185 GLY n 
1 186 SER n 
1 187 TRP n 
1 188 GLY n 
1 189 GLY n 
1 190 SER n 
1 191 LEU n 
1 192 ILE n 
1 193 ARG n 
1 194 PRO n 
1 195 GLU n 
1 196 ALA n 
1 197 THR n 
1 198 GLY n 
1 199 TYR n 
1 200 GLY n 
1 201 VAL n 
1 202 VAL n 
1 203 TYR n 
1 204 TYR n 
1 205 VAL n 
1 206 GLU n 
1 207 HIS n 
1 208 MET n 
1 209 ILE n 
1 210 ALA n 
1 211 HIS n 
1 212 ALA n 
1 213 THR n 
1 214 ASN n 
1 215 GLY n 
1 216 ALA n 
1 217 GLU n 
1 218 SER n 
1 219 PHE n 
1 220 ALA n 
1 221 GLY n 
1 222 LYS n 
1 223 ARG n 
1 224 VAL n 
1 225 ALA n 
1 226 ILE n 
1 227 SER n 
1 228 GLY n 
1 229 SER n 
1 230 GLY n 
1 231 ASN n 
1 232 VAL n 
1 233 ALA n 
1 234 GLN n 
1 235 TYR n 
1 236 ALA n 
1 237 ALA n 
1 238 LEU n 
1 239 LYS n 
1 240 VAL n 
1 241 ILE n 
1 242 GLU n 
1 243 LEU n 
1 244 GLY n 
1 245 GLY n 
1 246 ARG n 
1 247 VAL n 
1 248 VAL n 
1 249 SER n 
1 250 LEU n 
1 251 SER n 
1 252 ASP n 
1 253 SER n 
1 254 GLN n 
1 255 GLY n 
1 256 SER n 
1 257 LEU n 
1 258 ILE n 
1 259 VAL n 
1 260 LYS n 
1 261 ASP n 
1 262 LYS n 
1 263 ASP n 
1 264 SER n 
1 265 PHE n 
1 266 THR n 
1 267 PRO n 
1 268 ALA n 
1 269 GLU n 
1 270 ILE n 
1 271 ASP n 
1 272 ALA n 
1 273 ILE n 
1 274 ALA n 
1 275 ALA n 
1 276 LEU n 
1 277 LYS n 
1 278 VAL n 
1 279 ASP n 
1 280 ARG n 
1 281 LYS n 
1 282 GLN n 
1 283 ILE n 
1 284 ALA n 
1 285 GLU n 
1 286 LEU n 
1 287 VAL n 
1 288 THR n 
1 289 ASP n 
1 290 ALA n 
1 291 ALA n 
1 292 PHE n 
1 293 ALA n 
1 294 ASP n 
1 295 LYS n 
1 296 PHE n 
1 297 THR n 
1 298 TYR n 
1 299 LEU n 
1 300 PRO n 
1 301 GLY n 
1 302 GLN n 
1 303 ARG n 
1 304 PRO n 
1 305 TRP n 
1 306 VAL n 
1 307 HIS n 
1 308 VAL n 
1 309 GLY n 
1 310 ALA n 
1 311 VAL n 
1 312 ASP n 
1 313 VAL n 
1 314 ALA n 
1 315 LEU n 
1 316 PRO n 
1 317 SER n 
1 318 ALA n 
1 319 THR n 
1 320 GLN n 
1 321 ASN n 
1 322 GLU n 
1 323 VAL n 
1 324 SER n 
1 325 GLY n 
1 326 GLU n 
1 327 GLU n 
1 328 ALA n 
1 329 GLN n 
1 330 ALA n 
1 331 LEU n 
1 332 ILE n 
1 333 ALA n 
1 334 ALA n 
1 335 GLY n 
1 336 CYS n 
1 337 LYS n 
1 338 PHE n 
1 339 ILE n 
1 340 ALA n 
1 341 GLU n 
1 342 GLY n 
1 343 SER n 
1 344 ASN n 
1 345 MET n 
1 346 GLY n 
1 347 CYS n 
1 348 THR n 
1 349 GLN n 
1 350 ALA n 
1 351 ALA n 
1 352 ILE n 
1 353 ASP n 
1 354 ALA n 
1 355 PHE n 
1 356 GLU n 
1 357 ALA n 
1 358 HIS n 
1 359 ARG n 
1 360 GLU n 
1 361 ALA n 
1 362 ASN n 
1 363 LYS n 
1 364 GLY n 
1 365 ALA n 
1 366 ALA n 
1 367 ALA n 
1 368 ILE n 
1 369 TRP n 
1 370 TYR n 
1 371 ALA n 
1 372 PRO n 
1 373 GLY n 
1 374 LYS n 
1 375 ALA n 
1 376 ALA n 
1 377 ASN n 
1 378 ALA n 
1 379 GLY n 
1 380 GLY n 
1 381 VAL n 
1 382 ALA n 
1 383 VAL n 
1 384 SER n 
1 385 GLY n 
1 386 LEU n 
1 387 GLU n 
1 388 MET n 
1 389 ALA n 
1 390 GLN n 
1 391 ASN n 
1 392 SER n 
1 393 ALA n 
1 394 ARG n 
1 395 LEU n 
1 396 SER n 
1 397 TRP n 
1 398 THR n 
1 399 ALA n 
1 400 GLU n 
1 401 GLU n 
1 402 VAL n 
1 403 ASP n 
1 404 ALA n 
1 405 ARG n 
1 406 LEU n 
1 407 LYS n 
1 408 ASP n 
1 409 ILE n 
1 410 MET n 
1 411 LYS n 
1 412 SER n 
1 413 CYS n 
1 414 PHE n 
1 415 GLN n 
1 416 ASN n 
1 417 GLY n 
1 418 LEU n 
1 419 ASP n 
1 420 THR n 
1 421 ALA n 
1 422 LYS n 
1 423 GLU n 
1 424 TYR n 
1 425 ALA n 
1 426 THR n 
1 427 PRO n 
1 428 ALA n 
1 429 ASP n 
1 430 GLY n 
1 431 ILE n 
1 432 LEU n 
1 433 PRO n 
1 434 SER n 
1 435 LEU n 
1 436 VAL n 
1 437 THR n 
1 438 GLY n 
1 439 SER n 
1 440 ASN n 
1 441 ILE n 
1 442 ALA n 
1 443 GLY n 
1 444 PHE n 
1 445 THR n 
1 446 LYS n 
1 447 VAL n 
1 448 ALA n 
1 449 ALA n 
1 450 ALA n 
1 451 MET n 
1 452 LYS n 
1 453 ASP n 
1 454 GLN n 
1 455 GLY n 
1 456 ASP n 
1 457 TRP n 
1 458 TRP 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                   458 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'gdhA, ATEIFO6365_0005079300' 
_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      'Aspergillus terreus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     33178 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'  ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   2   SER SER A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   PRO 5   5   5   PRO PRO A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  PHE 10  10  10  PHE PHE A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  TYR 14  14  14  TYR TYR A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  GLU 16  16  16  GLU GLU A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  THR 20  20  20  THR THR 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  ASN 23  23  23  ASN ASN A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  PRO 31  31  31  PRO PRO A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  TRP 53  53  53  TRP TRP A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  VAL 60  60  60  VAL VAL A . n 
A 1 61  GLN 61  61  61  GLN GLN A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  HIS 84  84  84  HIS HIS A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  PHE 97  97  97  PHE PHE A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 PHE 101 101 101 PHE PHE A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 MET 110 110 110 MET MET A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ASP 118 118 118 ASP ASP A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 ARG 130 130 130 ARG ARG A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 CYS 133 133 133 CYS CYS A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 PHE 136 136 136 PHE PHE A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 CYS 141 141 141 CYS CYS A . n 
A 1 142 ARG 142 142 142 ARG ARG A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 THR 148 148 148 THR THR A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 ARG 160 160 160 ARG ARG 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 GLY 163 163 163 GLY GLY A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 PHE 166 166 166 PHE PHE A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 GLN 168 168 168 GLN GLN A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ARG 173 173 173 ARG ARG A . n 
A 1 174 ASN 174 174 174 ASN ASN A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 TRP 176 176 176 TRP TRP A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 THR 181 181 181 THR THR A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 LYS 183 183 183 LYS LYS A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 TRP 187 187 187 TRP TRP A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 THR 197 197 197 THR THR A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 HIS 207 207 207 HIS HIS A . n 
A 1 208 MET 208 208 208 MET MET A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 HIS 211 211 211 HIS HIS A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 SER 227 227 227 SER SER A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 GLN 234 234 234 GLN GLN A . n 
A 1 235 TYR 235 235 235 TYR TYR A . n 
A 1 236 ALA 236 236 236 ALA ALA A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 LYS 239 239 239 LYS LYS A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 ARG 246 246 246 ARG ARG A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 VAL 248 248 248 VAL VAL A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 SER 251 251 251 SER SER A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 SER 253 253 253 SER SER A . n 
A 1 254 GLN 254 254 254 GLN GLN A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 LYS 262 262 262 LYS LYS A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 SER 264 264 264 SER SER A . n 
A 1 265 PHE 265 265 265 PHE PHE A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 PRO 267 267 267 PRO PRO A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 ASP 271 271 271 ASP ASP A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 ILE 273 273 273 ILE ILE A . n 
A 1 274 ALA 274 274 274 ALA ALA A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 VAL 278 278 278 VAL VAL A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 ARG 280 280 280 ARG ARG A . n 
A 1 281 LYS 281 281 281 LYS LYS A . n 
A 1 282 GLN 282 282 282 GLN GLN A . n 
A 1 283 ILE 283 283 283 ILE ILE A . n 
A 1 284 ALA 284 284 284 ALA ALA A . n 
A 1 285 GLU 285 285 285 GLU GLU A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 THR 288 288 288 THR THR A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 PHE 292 292 292 PHE PHE A . n 
A 1 293 ALA 293 293 293 ALA ALA A . n 
A 1 294 ASP 294 294 294 ASP ASP A . n 
A 1 295 LYS 295 295 295 LYS LYS A . n 
A 1 296 PHE 296 296 296 PHE PHE A . n 
A 1 297 THR 297 297 297 THR THR A . n 
A 1 298 TYR 298 298 298 TYR TYR A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 PRO 300 300 300 PRO PRO A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 GLN 302 302 302 GLN GLN A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 PRO 304 304 304 PRO PRO A . n 
A 1 305 TRP 305 305 305 TRP TRP A . n 
A 1 306 VAL 306 306 306 VAL VAL A . n 
A 1 307 HIS 307 307 307 HIS HIS A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 ALA 310 310 310 ALA ALA A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 VAL 313 313 313 VAL VAL A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 PRO 316 316 316 PRO PRO A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 ALA 318 318 318 ALA ALA A . n 
A 1 319 THR 319 319 319 THR THR A . n 
A 1 320 GLN 320 320 320 GLN GLN A . n 
A 1 321 ASN 321 321 321 ASN ASN A . n 
A 1 322 GLU 322 322 322 GLU GLU A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 SER 324 324 324 SER SER A . n 
A 1 325 GLY 325 325 325 GLY GLY A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 GLU 327 327 327 GLU GLU A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 GLN 329 329 329 GLN GLN A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 ILE 332 332 332 ILE ILE A . n 
A 1 333 ALA 333 333 333 ALA ALA A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 CYS 336 336 336 CYS CYS A . n 
A 1 337 LYS 337 337 337 LYS LYS A . n 
A 1 338 PHE 338 338 338 PHE PHE A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 ALA 340 340 340 ALA ALA A . n 
A 1 341 GLU 341 341 341 GLU GLU A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 ASN 344 344 344 ASN ASN A . n 
A 1 345 MET 345 345 345 MET MET A . n 
A 1 346 GLY 346 346 346 GLY GLY A . n 
A 1 347 CYS 347 347 347 CYS CYS A . n 
A 1 348 THR 348 348 348 THR THR A . n 
A 1 349 GLN 349 349 349 GLN GLN A . n 
A 1 350 ALA 350 350 350 ALA ALA A . n 
A 1 351 ALA 351 351 351 ALA ALA A . n 
A 1 352 ILE 352 352 352 ILE ILE A . n 
A 1 353 ASP 353 353 353 ASP ASP A . n 
A 1 354 ALA 354 354 354 ALA ALA A . n 
A 1 355 PHE 355 355 355 PHE PHE A . n 
A 1 356 GLU 356 356 356 GLU GLU A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 HIS 358 358 358 HIS HIS A . n 
A 1 359 ARG 359 359 359 ARG ARG 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 ASN 362 362 362 ASN ASN A . n 
A 1 363 LYS 363 363 363 LYS LYS 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 ALA 366 366 366 ALA ALA A . n 
A 1 367 ALA 367 367 367 ALA ALA A . n 
A 1 368 ILE 368 368 368 ILE ILE A . n 
A 1 369 TRP 369 369 369 TRP TRP A . n 
A 1 370 TYR 370 370 370 TYR TYR A . n 
A 1 371 ALA 371 371 371 ALA ALA A . n 
A 1 372 PRO 372 372 372 PRO PRO A . n 
A 1 373 GLY 373 373 373 GLY GLY A . n 
A 1 374 LYS 374 374 374 LYS LYS A . n 
A 1 375 ALA 375 375 375 ALA ALA A . n 
A 1 376 ALA 376 376 376 ALA ALA A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 ALA 378 378 378 ALA ALA A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 ALA 382 382 382 ALA ALA A . n 
A 1 383 VAL 383 383 383 VAL VAL A . n 
A 1 384 SER 384 384 384 SER SER A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 MET 388 388 388 MET MET A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 GLN 390 390 390 GLN GLN A . n 
A 1 391 ASN 391 391 391 ASN ASN A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 ALA 393 393 393 ALA ALA A . n 
A 1 394 ARG 394 394 394 ARG ARG A . n 
A 1 395 LEU 395 395 395 LEU LEU A . n 
A 1 396 SER 396 396 396 SER SER A . n 
A 1 397 TRP 397 397 397 TRP TRP A . n 
A 1 398 THR 398 398 398 THR THR A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 ASP 403 403 403 ASP ASP A . n 
A 1 404 ALA 404 404 404 ALA ALA 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 LYS 407 407 407 LYS LYS A . n 
A 1 408 ASP 408 408 408 ASP ASP A . n 
A 1 409 ILE 409 409 409 ILE ILE A . n 
A 1 410 MET 410 410 410 MET MET A . n 
A 1 411 LYS 411 411 411 LYS LYS A . n 
A 1 412 SER 412 412 412 SER SER A . n 
A 1 413 CYS 413 413 413 CYS CYS A . n 
A 1 414 PHE 414 414 414 PHE PHE A . n 
A 1 415 GLN 415 415 415 GLN GLN A . n 
A 1 416 ASN 416 416 416 ASN ASN A . n 
A 1 417 GLY 417 417 417 GLY GLY A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 ASP 419 419 419 ASP ASP A . n 
A 1 420 THR 420 420 420 THR THR A . n 
A 1 421 ALA 421 421 421 ALA ALA A . n 
A 1 422 LYS 422 422 422 LYS LYS A . n 
A 1 423 GLU 423 423 423 GLU GLU A . n 
A 1 424 TYR 424 424 424 TYR TYR A . n 
A 1 425 ALA 425 425 425 ALA ALA A . n 
A 1 426 THR 426 426 426 THR THR A . n 
A 1 427 PRO 427 427 427 PRO PRO A . n 
A 1 428 ALA 428 428 428 ALA ALA A . n 
A 1 429 ASP 429 429 429 ASP ASP A . n 
A 1 430 GLY 430 430 430 GLY GLY A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 LEU 432 432 432 LEU LEU A . n 
A 1 433 PRO 433 433 433 PRO PRO A . n 
A 1 434 SER 434 434 434 SER SER A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 VAL 436 436 436 VAL VAL A . n 
A 1 437 THR 437 437 437 THR THR A . n 
A 1 438 GLY 438 438 438 GLY GLY A . n 
A 1 439 SER 439 439 439 SER SER A . n 
A 1 440 ASN 440 440 440 ASN ASN A . n 
A 1 441 ILE 441 441 441 ILE ILE A . n 
A 1 442 ALA 442 442 442 ALA ALA A . n 
A 1 443 GLY 443 443 443 GLY GLY A . n 
A 1 444 PHE 444 444 444 PHE PHE A . n 
A 1 445 THR 445 445 445 THR THR A . n 
A 1 446 LYS 446 446 446 LYS LYS A . n 
A 1 447 VAL 447 447 447 VAL VAL A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 ALA 449 449 449 ALA ALA A . n 
A 1 450 ALA 450 450 450 ALA ALA A . n 
A 1 451 MET 451 451 451 MET MET A . n 
A 1 452 LYS 452 452 452 LYS LYS A . n 
A 1 453 ASP 453 453 453 ASP ASP A . n 
A 1 454 GLN 454 454 454 GLN GLN A . n 
A 1 455 GLY 455 455 455 GLY GLY A . n 
A 1 456 ASP 456 456 456 ASP ASP A . n 
A 1 457 TRP 457 457 457 TRP TRP A . n 
A 1 458 TRP 458 458 458 TRP TRP A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   ASN 3   3   3   ASN ASN B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   PRO 5   5   5   PRO PRO B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   GLU 7   7   7   GLU GLU B . n 
B 1 8   PRO 8   8   8   PRO PRO B . n 
B 1 9   GLU 9   9   9   GLU GLU B . n 
B 1 10  PHE 10  10  10  PHE PHE B . n 
B 1 11  GLU 11  11  11  GLU GLU B . n 
B 1 12  GLN 12  12  12  GLN GLN B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  TYR 14  14  14  TYR TYR B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  GLU 16  16  16  GLU GLU B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  ALA 18  18  18  ALA ALA B . n 
B 1 19  SER 19  19  19  SER SER B . n 
B 1 20  THR 20  20  20  THR THR 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  ASN 23  23  23  ASN ASN B . n 
B 1 24  SER 24  24  24  SER SER B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  ASN 30  30  30  ASN ASN B . n 
B 1 31  PRO 31  31  31  PRO PRO B . n 
B 1 32  GLU 32  32  32  GLU GLU B . n 
B 1 33  TYR 33  33  33  TYR TYR B . n 
B 1 34  ARG 34  34  34  ARG ARG B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  VAL 39  39  39  VAL VAL B . n 
B 1 40  VAL 40  40  40  VAL VAL B . n 
B 1 41  SER 41  41  41  SER SER B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  PRO 43  43  43  PRO PRO B . n 
B 1 44  GLU 44  44  44  GLU GLU B . n 
B 1 45  ARG 45  45  45  ARG ARG B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  GLN 48  48  48  GLN GLN B . n 
B 1 49  PHE 49  49  49  PHE PHE B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  VAL 52  52  52  VAL VAL B . n 
B 1 53  TRP 53  53  53  TRP TRP B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  ASN 55  55  55  ASN ASN B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLY 58  58  58  GLY GLY B . n 
B 1 59  GLU 59  59  59  GLU GLU B . n 
B 1 60  VAL 60  60  60  VAL VAL B . n 
B 1 61  GLN 61  61  61  GLN GLN B . n 
B 1 62  VAL 62  62  62  VAL VAL B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ARG 64  64  64  ARG ARG B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  ARG 67  67  67  ARG ARG B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  PRO 76  76  76  PRO PRO B . n 
B 1 77  TYR 77  77  77  TYR TYR B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  ARG 82  82  82  ARG ARG B . n 
B 1 83  PHE 83  83  83  PHE PHE B . n 
B 1 84  HIS 84  84  84  HIS HIS B . n 
B 1 85  PRO 85  85  85  PRO PRO B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  SER 90  90  90  SER SER B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  GLY 96  96  96  GLY GLY B . n 
B 1 97  PHE 97  97  97  PHE PHE B . n 
B 1 98  GLU 98  98  98  GLU GLU B . n 
B 1 99  GLN 99  99  99  GLN GLN B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 PHE 101 101 101 PHE PHE B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 ALA 104 104 104 ALA ALA B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 GLY 107 107 107 GLY GLY B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 MET 110 110 110 MET MET B . n 
B 1 111 GLY 111 111 111 GLY GLY B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 GLY 113 113 113 GLY GLY B . n 
B 1 114 LYS 114 114 114 LYS LYS B . n 
B 1 115 GLY 115 115 115 GLY GLY B . n 
B 1 116 GLY 116 116 116 GLY GLY B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 ASP 118 118 118 ASP ASP B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 PRO 121 121 121 PRO PRO B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 GLY 123 123 123 GLY GLY B . n 
B 1 124 LYS 124 124 124 LYS LYS B . n 
B 1 125 SER 125 125 125 SER SER B . n 
B 1 126 ASP 126 126 126 ASP ASP B . n 
B 1 127 SER 127 127 127 SER SER B . n 
B 1 128 GLU 128 128 128 GLU GLU B . n 
B 1 129 ILE 129 129 129 ILE ILE B . n 
B 1 130 ARG 130 130 130 ARG ARG B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 CYS 133 133 133 CYS CYS B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 PHE 136 136 136 PHE PHE B . n 
B 1 137 MET 137 137 137 MET MET B . n 
B 1 138 THR 138 138 138 THR THR B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 CYS 141 141 141 CYS CYS B . n 
B 1 142 ARG 142 142 142 ARG ARG B . n 
B 1 143 HIS 143 143 143 HIS HIS B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 GLY 145 145 145 GLY GLY B . n 
B 1 146 ALA 146 146 146 ALA ALA B . n 
B 1 147 ASP 147 147 147 ASP ASP B . n 
B 1 148 THR 148 148 148 THR THR B . n 
B 1 149 ASP 149 149 149 ASP ASP B . n 
B 1 150 VAL 150 150 150 VAL VAL B . n 
B 1 151 PRO 151 151 151 PRO PRO B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLY 153 153 153 GLY GLY B . n 
B 1 154 ASP 154 154 154 ASP ASP B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 ARG 160 160 160 ARG ARG 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 GLY 163 163 163 GLY GLY B . n 
B 1 164 TYR 164 164 164 TYR TYR B . n 
B 1 165 LEU 165 165 165 LEU LEU B . n 
B 1 166 PHE 166 166 166 PHE PHE B . n 
B 1 167 GLY 167 167 167 GLY GLY B . n 
B 1 168 GLN 168 168 168 GLN GLN B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 ARG 170 170 170 ARG ARG B . n 
B 1 171 LYS 171 171 171 LYS LYS B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 ARG 173 173 173 ARG ARG B . n 
B 1 174 ASN 174 174 174 ASN ASN B . n 
B 1 175 SER 175 175 175 SER SER B . n 
B 1 176 TRP 176 176 176 TRP TRP B . n 
B 1 177 GLU 177 177 177 GLU GLU B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 VAL 179 179 179 VAL VAL B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 THR 181 181 181 THR THR B . n 
B 1 182 GLY 182 182 182 GLY GLY B . n 
B 1 183 LYS 183 183 183 LYS LYS B . n 
B 1 184 GLY 184 184 184 GLY GLY B . n 
B 1 185 GLY 185 185 185 GLY GLY B . n 
B 1 186 SER 186 186 186 SER SER B . n 
B 1 187 TRP 187 187 187 TRP TRP B . n 
B 1 188 GLY 188 188 188 GLY GLY B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 ARG 193 193 193 ARG ARG B . n 
B 1 194 PRO 194 194 194 PRO PRO B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 THR 197 197 197 THR THR B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 TYR 199 199 199 TYR TYR B . n 
B 1 200 GLY 200 200 200 GLY GLY B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 TYR 203 203 203 TYR TYR B . n 
B 1 204 TYR 204 204 204 TYR TYR B . n 
B 1 205 VAL 205 205 205 VAL VAL B . n 
B 1 206 GLU 206 206 206 GLU GLU B . n 
B 1 207 HIS 207 207 207 HIS HIS B . n 
B 1 208 MET 208 208 208 MET MET B . n 
B 1 209 ILE 209 209 209 ILE ILE B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 HIS 211 211 211 HIS HIS B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ALA 216 216 216 ALA ALA B . n 
B 1 217 GLU 217 217 217 GLU GLU B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 ALA 220 220 220 ALA ALA B . n 
B 1 221 GLY 221 221 221 GLY GLY B . n 
B 1 222 LYS 222 222 222 LYS LYS B . n 
B 1 223 ARG 223 223 223 ARG ARG B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 ILE 226 226 226 ILE ILE B . n 
B 1 227 SER 227 227 227 SER SER B . n 
B 1 228 GLY 228 228 228 GLY GLY B . n 
B 1 229 SER 229 229 229 SER SER B . n 
B 1 230 GLY 230 230 230 GLY GLY B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 VAL 232 232 232 VAL VAL B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 GLN 234 234 234 GLN GLN B . n 
B 1 235 TYR 235 235 235 TYR TYR B . n 
B 1 236 ALA 236 236 236 ALA ALA B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 LYS 239 239 239 LYS LYS B . n 
B 1 240 VAL 240 240 240 VAL VAL B . n 
B 1 241 ILE 241 241 241 ILE ILE B . n 
B 1 242 GLU 242 242 242 GLU GLU B . n 
B 1 243 LEU 243 243 243 LEU LEU B . n 
B 1 244 GLY 244 244 244 GLY GLY B . n 
B 1 245 GLY 245 245 245 GLY GLY B . n 
B 1 246 ARG 246 246 246 ARG ARG B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 VAL 248 248 248 VAL VAL B . n 
B 1 249 SER 249 249 249 SER SER B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 SER 251 251 251 SER SER B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 SER 253 253 253 SER SER B . n 
B 1 254 GLN 254 254 254 GLN GLN B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 SER 256 256 256 SER SER B . n 
B 1 257 LEU 257 257 257 LEU LEU B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 VAL 259 259 259 VAL VAL B . n 
B 1 260 LYS 260 260 260 LYS LYS B . n 
B 1 261 ASP 261 261 261 ASP ASP B . n 
B 1 262 LYS 262 262 262 LYS LYS B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 SER 264 264 264 SER SER B . n 
B 1 265 PHE 265 265 265 PHE PHE B . n 
B 1 266 THR 266 266 266 THR THR B . n 
B 1 267 PRO 267 267 267 PRO PRO B . n 
B 1 268 ALA 268 268 268 ALA ALA B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 ILE 270 270 270 ILE ILE B . n 
B 1 271 ASP 271 271 271 ASP ASP B . n 
B 1 272 ALA 272 272 272 ALA ALA B . n 
B 1 273 ILE 273 273 273 ILE ILE B . n 
B 1 274 ALA 274 274 274 ALA ALA B . n 
B 1 275 ALA 275 275 275 ALA ALA B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 LYS 277 277 277 LYS LYS B . n 
B 1 278 VAL 278 278 278 VAL VAL B . n 
B 1 279 ASP 279 279 279 ASP ASP B . n 
B 1 280 ARG 280 280 280 ARG ARG B . n 
B 1 281 LYS 281 281 281 LYS LYS B . n 
B 1 282 GLN 282 282 282 GLN GLN B . n 
B 1 283 ILE 283 283 283 ILE ILE B . n 
B 1 284 ALA 284 284 284 ALA ALA B . n 
B 1 285 GLU 285 285 285 GLU GLU B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 VAL 287 287 287 VAL VAL B . n 
B 1 288 THR 288 288 288 THR THR B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 ALA 290 290 290 ALA ALA B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 PHE 292 292 292 PHE PHE B . n 
B 1 293 ALA 293 293 293 ALA ALA B . n 
B 1 294 ASP 294 294 294 ASP ASP B . n 
B 1 295 LYS 295 295 295 LYS LYS B . n 
B 1 296 PHE 296 296 296 PHE PHE B . n 
B 1 297 THR 297 297 297 THR THR B . n 
B 1 298 TYR 298 298 298 TYR TYR B . n 
B 1 299 LEU 299 299 299 LEU LEU B . n 
B 1 300 PRO 300 300 300 PRO PRO B . n 
B 1 301 GLY 301 301 301 GLY GLY B . n 
B 1 302 GLN 302 302 302 GLN GLN B . n 
B 1 303 ARG 303 303 303 ARG ARG B . n 
B 1 304 PRO 304 304 304 PRO PRO B . n 
B 1 305 TRP 305 305 305 TRP TRP B . n 
B 1 306 VAL 306 306 306 VAL VAL B . n 
B 1 307 HIS 307 307 307 HIS HIS B . n 
B 1 308 VAL 308 308 308 VAL VAL B . n 
B 1 309 GLY 309 309 309 GLY GLY B . n 
B 1 310 ALA 310 310 310 ALA ALA B . n 
B 1 311 VAL 311 311 311 VAL VAL B . n 
B 1 312 ASP 312 312 312 ASP ASP B . n 
B 1 313 VAL 313 313 313 VAL VAL B . n 
B 1 314 ALA 314 314 314 ALA ALA B . n 
B 1 315 LEU 315 315 315 LEU LEU B . n 
B 1 316 PRO 316 316 316 PRO PRO B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 ALA 318 318 318 ALA ALA B . n 
B 1 319 THR 319 319 319 THR THR B . n 
B 1 320 GLN 320 320 320 GLN GLN B . n 
B 1 321 ASN 321 321 321 ASN ASN B . n 
B 1 322 GLU 322 322 322 GLU GLU B . n 
B 1 323 VAL 323 323 323 VAL VAL B . n 
B 1 324 SER 324 324 324 SER SER B . n 
B 1 325 GLY 325 325 325 GLY GLY B . n 
B 1 326 GLU 326 326 326 GLU GLU B . n 
B 1 327 GLU 327 327 327 GLU GLU B . n 
B 1 328 ALA 328 328 328 ALA ALA B . n 
B 1 329 GLN 329 329 329 GLN GLN B . n 
B 1 330 ALA 330 330 330 ALA ALA B . n 
B 1 331 LEU 331 331 331 LEU LEU B . n 
B 1 332 ILE 332 332 332 ILE ILE B . n 
B 1 333 ALA 333 333 333 ALA ALA B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 GLY 335 335 335 GLY GLY B . n 
B 1 336 CYS 336 336 336 CYS CYS B . n 
B 1 337 LYS 337 337 337 LYS LYS B . n 
B 1 338 PHE 338 338 338 PHE PHE B . n 
B 1 339 ILE 339 339 339 ILE ILE B . n 
B 1 340 ALA 340 340 340 ALA ALA B . n 
B 1 341 GLU 341 341 341 GLU GLU B . n 
B 1 342 GLY 342 342 342 GLY GLY B . n 
B 1 343 SER 343 343 343 SER SER B . n 
B 1 344 ASN 344 344 344 ASN ASN B . n 
B 1 345 MET 345 345 345 MET MET B . n 
B 1 346 GLY 346 346 346 GLY GLY B . n 
B 1 347 CYS 347 347 347 CYS CYS B . n 
B 1 348 THR 348 348 348 THR THR B . n 
B 1 349 GLN 349 349 349 GLN GLN B . n 
B 1 350 ALA 350 350 350 ALA ALA B . n 
B 1 351 ALA 351 351 351 ALA ALA B . n 
B 1 352 ILE 352 352 352 ILE ILE B . n 
B 1 353 ASP 353 353 353 ASP ASP B . n 
B 1 354 ALA 354 354 354 ALA ALA B . n 
B 1 355 PHE 355 355 355 PHE PHE B . n 
B 1 356 GLU 356 356 356 GLU GLU B . n 
B 1 357 ALA 357 357 357 ALA ALA B . n 
B 1 358 HIS 358 358 358 HIS HIS B . n 
B 1 359 ARG 359 359 359 ARG ARG 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 ASN 362 362 362 ASN ASN B . n 
B 1 363 LYS 363 363 363 LYS LYS 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 ALA 366 366 366 ALA ALA B . n 
B 1 367 ALA 367 367 367 ALA ALA B . n 
B 1 368 ILE 368 368 368 ILE ILE B . n 
B 1 369 TRP 369 369 369 TRP TRP B . n 
B 1 370 TYR 370 370 370 TYR TYR B . n 
B 1 371 ALA 371 371 371 ALA ALA B . n 
B 1 372 PRO 372 372 372 PRO PRO B . n 
B 1 373 GLY 373 373 373 GLY GLY B . n 
B 1 374 LYS 374 374 374 LYS LYS B . n 
B 1 375 ALA 375 375 375 ALA ALA B . n 
B 1 376 ALA 376 376 376 ALA ALA B . n 
B 1 377 ASN 377 377 377 ASN ASN B . n 
B 1 378 ALA 378 378 378 ALA ALA B . n 
B 1 379 GLY 379 379 379 GLY GLY B . n 
B 1 380 GLY 380 380 380 GLY GLY B . n 
B 1 381 VAL 381 381 381 VAL VAL B . n 
B 1 382 ALA 382 382 382 ALA ALA B . n 
B 1 383 VAL 383 383 383 VAL VAL B . n 
B 1 384 SER 384 384 384 SER SER B . n 
B 1 385 GLY 385 385 385 GLY GLY B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 GLU 387 387 387 GLU GLU B . n 
B 1 388 MET 388 388 388 MET MET B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 GLN 390 390 390 GLN GLN B . n 
B 1 391 ASN 391 391 391 ASN ASN B . n 
B 1 392 SER 392 392 392 SER SER B . n 
B 1 393 ALA 393 393 393 ALA ALA B . n 
B 1 394 ARG 394 394 394 ARG ARG B . n 
B 1 395 LEU 395 395 395 LEU LEU B . n 
B 1 396 SER 396 396 396 SER SER B . n 
B 1 397 TRP 397 397 397 TRP TRP B . n 
B 1 398 THR 398 398 398 THR THR B . n 
B 1 399 ALA 399 399 399 ALA ALA B . n 
B 1 400 GLU 400 400 400 GLU GLU B . n 
B 1 401 GLU 401 401 401 GLU GLU B . n 
B 1 402 VAL 402 402 402 VAL VAL B . n 
B 1 403 ASP 403 403 403 ASP ASP B . n 
B 1 404 ALA 404 404 404 ALA ALA 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 LYS 407 407 407 LYS LYS B . n 
B 1 408 ASP 408 408 408 ASP ASP B . n 
B 1 409 ILE 409 409 409 ILE ILE B . n 
B 1 410 MET 410 410 410 MET MET B . n 
B 1 411 LYS 411 411 411 LYS LYS B . n 
B 1 412 SER 412 412 412 SER SER B . n 
B 1 413 CYS 413 413 413 CYS CYS B . n 
B 1 414 PHE 414 414 414 PHE PHE B . n 
B 1 415 GLN 415 415 415 GLN GLN B . n 
B 1 416 ASN 416 416 416 ASN ASN B . n 
B 1 417 GLY 417 417 417 GLY GLY B . n 
B 1 418 LEU 418 418 418 LEU LEU B . n 
B 1 419 ASP 419 419 419 ASP ASP B . n 
B 1 420 THR 420 420 420 THR THR B . n 
B 1 421 ALA 421 421 421 ALA ALA B . n 
B 1 422 LYS 422 422 422 LYS LYS B . n 
B 1 423 GLU 423 423 423 GLU GLU B . n 
B 1 424 TYR 424 424 424 TYR TYR B . n 
B 1 425 ALA 425 425 425 ALA ALA B . n 
B 1 426 THR 426 426 426 THR THR B . n 
B 1 427 PRO 427 427 427 PRO PRO B . n 
B 1 428 ALA 428 428 428 ALA ALA B . n 
B 1 429 ASP 429 429 429 ASP ASP B . n 
B 1 430 GLY 430 430 430 GLY GLY B . n 
B 1 431 ILE 431 431 431 ILE ILE B . n 
B 1 432 LEU 432 432 432 LEU LEU B . n 
B 1 433 PRO 433 433 433 PRO PRO B . n 
B 1 434 SER 434 434 434 SER SER B . n 
B 1 435 LEU 435 435 435 LEU LEU B . n 
B 1 436 VAL 436 436 436 VAL VAL B . n 
B 1 437 THR 437 437 437 THR THR B . n 
B 1 438 GLY 438 438 438 GLY GLY B . n 
B 1 439 SER 439 439 439 SER SER B . n 
B 1 440 ASN 440 440 440 ASN ASN B . n 
B 1 441 ILE 441 441 441 ILE ILE B . n 
B 1 442 ALA 442 442 442 ALA ALA B . n 
B 1 443 GLY 443 443 443 GLY GLY B . n 
B 1 444 PHE 444 444 444 PHE PHE B . n 
B 1 445 THR 445 445 445 THR THR B . n 
B 1 446 LYS 446 446 446 LYS LYS B . n 
B 1 447 VAL 447 447 447 VAL VAL B . n 
B 1 448 ALA 448 448 448 ALA ALA B . n 
B 1 449 ALA 449 449 449 ALA ALA B . n 
B 1 450 ALA 450 450 450 ALA ALA B . n 
B 1 451 MET 451 451 451 MET MET B . n 
B 1 452 LYS 452 452 452 LYS LYS B . n 
B 1 453 ASP 453 453 453 ASP ASP B . n 
B 1 454 GLN 454 454 454 GLN GLN B . n 
B 1 455 GLY 455 455 455 GLY GLY B . n 
B 1 456 ASP 456 456 456 ASP ASP B . n 
B 1 457 TRP 457 457 457 TRP TRP B . n 
B 1 458 TRP 458 458 458 TRP TRP B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CL 
_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 CL  1  501 4   CL  CL  A . 
D 2 CL  1  502 5   CL  CL  A . 
E 2 CL  1  501 3   CL  CL  B . 
F 2 CL  1  502 6   CL  CL  B . 
G 2 CL  1  503 7   CL  CL  B . 
H 3 HOH 1  601 221 HOH HOH A . 
H 3 HOH 2  602 10  HOH HOH A . 
H 3 HOH 3  603 276 HOH HOH A . 
H 3 HOH 4  604 261 HOH HOH A . 
H 3 HOH 5  605 311 HOH HOH A . 
H 3 HOH 6  606 265 HOH HOH A . 
H 3 HOH 7  607 118 HOH HOH A . 
H 3 HOH 8  608 290 HOH HOH A . 
H 3 HOH 9  609 63  HOH HOH A . 
H 3 HOH 10 610 129 HOH HOH A . 
H 3 HOH 11 611 297 HOH HOH A . 
H 3 HOH 12 612 302 HOH HOH A . 
H 3 HOH 13 613 299 HOH HOH A . 
H 3 HOH 14 614 262 HOH HOH A . 
H 3 HOH 15 615 308 HOH HOH A . 
H 3 HOH 16 616 310 HOH HOH A . 
H 3 HOH 17 617 294 HOH HOH A . 
H 3 HOH 18 618 174 HOH HOH A . 
H 3 HOH 19 619 288 HOH HOH A . 
H 3 HOH 20 620 268 HOH HOH A . 
H 3 HOH 21 621 260 HOH HOH A . 
H 3 HOH 22 622 278 HOH HOH A . 
H 3 HOH 23 623 266 HOH HOH A . 
H 3 HOH 24 624 246 HOH HOH A . 
H 3 HOH 25 625 292 HOH HOH A . 
H 3 HOH 26 626 64  HOH HOH A . 
H 3 HOH 27 627 305 HOH HOH A . 
H 3 HOH 28 628 316 HOH HOH A . 
H 3 HOH 29 629 314 HOH HOH A . 
H 3 HOH 30 630 209 HOH HOH A . 
H 3 HOH 31 631 71  HOH HOH A . 
H 3 HOH 32 632 254 HOH HOH A . 
H 3 HOH 33 633 264 HOH HOH A . 
H 3 HOH 34 634 313 HOH HOH A . 
H 3 HOH 35 635 317 HOH HOH A . 
H 3 HOH 36 636 312 HOH HOH A . 
H 3 HOH 37 637 315 HOH HOH A . 
I 3 HOH 1  601 242 HOH HOH B . 
I 3 HOH 2  602 277 HOH HOH B . 
I 3 HOH 3  603 301 HOH HOH B . 
I 3 HOH 4  604 281 HOH HOH B . 
I 3 HOH 5  605 267 HOH HOH B . 
I 3 HOH 6  606 14  HOH HOH B . 
I 3 HOH 7  607 274 HOH HOH B . 
I 3 HOH 8  608 131 HOH HOH B . 
I 3 HOH 9  609 304 HOH HOH B . 
I 3 HOH 10 610 188 HOH HOH B . 
I 3 HOH 11 611 51  HOH HOH B . 
I 3 HOH 12 612 19  HOH HOH B . 
I 3 HOH 13 613 285 HOH HOH B . 
I 3 HOH 14 614 245 HOH HOH B . 
I 3 HOH 15 615 286 HOH HOH B . 
I 3 HOH 16 616 45  HOH HOH B . 
I 3 HOH 17 617 7   HOH HOH B . 
I 3 HOH 18 618 298 HOH HOH B . 
I 3 HOH 19 619 283 HOH HOH B . 
I 3 HOH 20 620 309 HOH HOH B . 
I 3 HOH 21 621 34  HOH HOH B . 
I 3 HOH 22 622 279 HOH HOH B . 
I 3 HOH 23 623 280 HOH HOH B . 
I 3 HOH 24 624 247 HOH HOH B . 
I 3 HOH 25 625 303 HOH HOH B . 
I 3 HOH 26 626 272 HOH HOH B . 
I 3 HOH 27 627 41  HOH HOH B . 
I 3 HOH 28 628 296 HOH HOH B . 
I 3 HOH 29 629 282 HOH HOH B . 
I 3 HOH 30 630 248 HOH HOH B . 
I 3 HOH 31 631 5   HOH HOH B . 
I 3 HOH 32 632 271 HOH HOH B . 
I 3 HOH 33 633 275 HOH HOH 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       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? v1.20.1-4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .            2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BALBES ? ? ? .            4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z29 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     157.550 
_cell.length_a_esd                 ? 
_cell.length_b                     157.550 
_cell.length_b_esd                 ? 
_cell.length_c                     106.280 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Z29 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                173 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 63' 
_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                   8Z29 
_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             3.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          68.37 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '15% PEG3350, 0.1 M HEPES pH 7.0, 0.2 M NaCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_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                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         RIGAKU 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-02-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Z29 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.85 
_reflns.d_resolution_low                               30.0 
_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                                     35108 
_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                                10.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.98 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.85 
_reflns_shell.d_res_low                                     2.95 
_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                             3406 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.56 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Z29 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.85 
_refine.ls_d_res_low                             30.0 
_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                     33338 
_refine.ls_number_reflns_R_free                  1768 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.23 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5XVI 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.85 
_refine_hist.d_res_low                        30.0 
_refine_hist.number_atoms_solvent             70 
_refine_hist.number_atoms_total               6963 
_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        6888 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_struct.entry_id                     8Z29 
_struct.title                        
'Crystal structure of apo Aspergillus terreus glutamate dehydrogenase (AtGDH) deletion mutant (T262-A263)' 
_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        8Z29 
_struct_keywords.text            
'glutamate dehydrogenase, allostery, cooperativity, Aspergillus, cryo-EM, domain dynamics, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    T2D1F5_ASPTE 
_struct_ref.pdbx_db_accession          T2D1F5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSNLPVEPEFEQAYKELASTLENSTLFQKNPEYRKALAVVSVPERVIQFRVVWENDKGEVQVNRGFRVQFNSALGPYKGG
LRFHPSVNLSILKFLGFEQIFKNALTGLNMGGGKGGSDFDPKGKSDSEIRRFCVAFMTELCRHIGADTDVPAGDIGVTGR
EIGYLFGQYRKLRNSWEGVLTGKGGSWGGSLIRPEATGYGVVYYVEHMIAHATNGAESFAGKRVAISGSGNVAQYAALKV
IELGGRVVSLSDSQGSLIVKDTAKDSFTPAEIDAIAALKVDRKQIAELVTDAAFADKFTYLPGQRPWVHVGAVDVALPSA
TQNEVSGEEAQALIAAGCKFIAEGSNMGCTQAAIDAFEAHREANKGAAAIWYAPGKAANAGGVAVSGLEMAQNSARLSWT
AEEVDARLKDIMKSCFQNGLDTAKEYATPADGILPSLVTGSNIAGFTKVAAAMKDQGDWW
;
_struct_ref.pdbx_align_begin           1 
# 
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 8Z29 A 1 ? 458 ? T2D1F5 1 ? 460 ? 1 458 
2 1 8Z29 B 1 ? 458 ? T2D1F5 1 ? 460 ? 1 458 
# 
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 8Z29 ? A ? ? UNP T2D1F5 THR 262 deletion ? 1 
1 8Z29 ? A ? ? UNP T2D1F5 ALA 263 deletion ? 2 
2 8Z29 ? B ? ? UNP T2D1F5 THR 262 deletion ? 3 
2 8Z29 ? B ? ? UNP T2D1F5 ALA 263 deletion ? 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 25360 ? 
1 MORE         -145  ? 
1 'SSA (A^2)'  89760 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000  0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_545 -y,x-y-1,z  -0.5000000000 -0.8660254038 0.0000000000 78.7750000000  0.8660254038  
-0.5000000000 0.0000000000 -136.4423023662 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_655 -x+y+1,-x,z -0.5000000000 0.8660254038  0.0000000000 157.5500000000 -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 7   ? SER A 24  ? GLU A 7   SER A 24  1 ? 18 
HELX_P HELX_P2  AA2 THR A 25  ? ASN A 30  ? THR A 25  ASN A 30  1 ? 6  
HELX_P HELX_P3  AA3 TYR A 33  ? SER A 41  ? TYR A 33  SER A 41  1 ? 9  
HELX_P HELX_P4  AA4 ASN A 88  ? LEU A 105 ? ASN A 88  LEU A 105 1 ? 18 
HELX_P HELX_P5  AA5 SER A 125 ? CYS A 141 ? SER A 125 CYS A 141 1 ? 17 
HELX_P HELX_P6  AA6 ARG A 142 ? ILE A 144 ? ARG A 142 ILE A 144 5 ? 3  
HELX_P HELX_P7  AA7 THR A 158 ? ASN A 174 ? THR A 158 ASN A 174 1 ? 17 
HELX_P HELX_P8  AA8 GLU A 195 ? THR A 213 ? GLU A 195 THR A 213 1 ? 19 
HELX_P HELX_P9  AA9 GLY A 230 ? LEU A 243 ? GLY A 230 LEU A 243 1 ? 14 
HELX_P HELX_P10 AB1 THR A 266 ? VAL A 278 ? THR A 266 VAL A 278 1 ? 13 
HELX_P HELX_P11 AB2 ASP A 279 ? LYS A 281 ? ASP A 279 LYS A 281 5 ? 3  
HELX_P HELX_P12 AB3 ILE A 283 ? ASP A 289 ? ILE A 283 ASP A 289 1 ? 7  
HELX_P HELX_P13 AB4 ASP A 289 ? ASP A 294 ? ASP A 289 ASP A 294 1 ? 6  
HELX_P HELX_P14 AB5 ARG A 303 ? HIS A 307 ? ARG A 303 HIS A 307 5 ? 5  
HELX_P HELX_P15 AB6 SER A 324 ? ALA A 334 ? SER A 324 ALA A 334 1 ? 11 
HELX_P HELX_P16 AB7 THR A 348 ? ASN A 362 ? THR A 348 ASN A 362 1 ? 15 
HELX_P HELX_P17 AB8 LYS A 363 ? ALA A 367 ? LYS A 363 ALA A 367 5 ? 5  
HELX_P HELX_P18 AB9 PRO A 372 ? ASN A 377 ? PRO A 372 ASN A 377 1 ? 6  
HELX_P HELX_P19 AC1 ALA A 378 ? ARG A 394 ? ALA A 378 ARG A 394 1 ? 17 
HELX_P HELX_P20 AC2 THR A 398 ? ALA A 425 ? THR A 398 ALA A 425 1 ? 28 
HELX_P HELX_P21 AC3 SER A 434 ? GLN A 454 ? SER A 434 GLN A 454 1 ? 21 
HELX_P HELX_P22 AC4 GLU B 7   ? ASN B 23  ? GLU B 7   ASN B 23  1 ? 17 
HELX_P HELX_P23 AC5 THR B 25  ? ASN B 30  ? THR B 25  ASN B 30  1 ? 6  
HELX_P HELX_P24 AC6 TYR B 33  ? SER B 41  ? TYR B 33  SER B 41  1 ? 9  
HELX_P HELX_P25 AC7 ASN B 88  ? THR B 106 ? ASN B 88  THR B 106 1 ? 19 
HELX_P HELX_P26 AC8 SER B 125 ? CYS B 141 ? SER B 125 CYS B 141 1 ? 17 
HELX_P HELX_P27 AC9 ARG B 142 ? ILE B 144 ? ARG B 142 ILE B 144 5 ? 3  
HELX_P HELX_P28 AD1 THR B 158 ? ASN B 174 ? THR B 158 ASN B 174 1 ? 17 
HELX_P HELX_P29 AD2 GLY B 184 ? GLY B 188 ? GLY B 184 GLY B 188 5 ? 5  
HELX_P HELX_P30 AD3 GLU B 195 ? THR B 213 ? GLU B 195 THR B 213 1 ? 19 
HELX_P HELX_P31 AD4 GLY B 230 ? LEU B 243 ? GLY B 230 LEU B 243 1 ? 14 
HELX_P HELX_P32 AD5 THR B 266 ? LEU B 276 ? THR B 266 LEU B 276 1 ? 11 
HELX_P HELX_P33 AD6 GLN B 282 ? VAL B 287 ? GLN B 282 VAL B 287 1 ? 6  
HELX_P HELX_P34 AD7 ALA B 291 ? LYS B 295 ? ALA B 291 LYS B 295 1 ? 5  
HELX_P HELX_P35 AD8 ARG B 303 ? HIS B 307 ? ARG B 303 HIS B 307 5 ? 5  
HELX_P HELX_P36 AD9 SER B 324 ? ALA B 334 ? SER B 324 ALA B 334 1 ? 11 
HELX_P HELX_P37 AE1 THR B 348 ? ASN B 362 ? THR B 348 ASN B 362 1 ? 15 
HELX_P HELX_P38 AE2 LYS B 363 ? ALA B 367 ? LYS B 363 ALA B 367 5 ? 5  
HELX_P HELX_P39 AE3 PRO B 372 ? ASN B 377 ? PRO B 372 ASN B 377 1 ? 6  
HELX_P HELX_P40 AE4 ALA B 378 ? ARG B 394 ? ALA B 378 ARG B 394 1 ? 17 
HELX_P HELX_P41 AE5 THR B 398 ? ALA B 425 ? THR B 398 ALA B 425 1 ? 28 
HELX_P HELX_P42 AE6 SER B 434 ? GLN B 454 ? SER B 434 GLN B 454 1 ? 21 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 5 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
AA7 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA2 1 2 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 81  ? PHE A 83  ? LEU A 81  PHE A 83  
AA1 2 GLY A 112 ? SER A 117 ? GLY A 112 SER A 117 
AA1 3 VAL A 60  ? ASN A 71  ? VAL A 60  ASN A 71  
AA1 4 ARG A 45  ? GLU A 54  ? ARG A 45  GLU A 54  
AA1 5 ARG B 45  ? GLU B 54  ? ARG B 45  GLU B 54  
AA1 6 VAL B 60  ? ASN B 71  ? VAL B 60  ASN B 71  
AA1 7 GLY B 112 ? SER B 117 ? GLY B 112 SER B 117 
AA1 8 LEU B 81  ? PHE B 83  ? LEU B 81  PHE B 83  
AA2 1 TYR A 77  ? LYS A 78  ? TYR A 77  LYS A 78  
AA2 2 ASP A 149 ? VAL A 150 ? ASP A 149 VAL A 150 
AA3 1 ARG A 246 ? VAL A 247 ? ARG A 246 VAL A 247 
AA3 2 ARG A 223 ? SER A 227 ? ARG A 223 SER A 227 
AA3 3 VAL A 313 ? PRO A 316 ? VAL A 313 PRO A 316 
AA3 4 PHE A 338 ? ALA A 340 ? PHE A 338 ALA A 340 
AA3 5 TRP A 369 ? ALA A 371 ? TRP A 369 ALA A 371 
AA4 1 SER A 249 ? SER A 251 ? SER A 249 SER A 251 
AA4 2 SER A 256 ? VAL A 259 ? SER A 256 VAL A 259 
AA4 3 PHE A 296 ? LEU A 299 ? PHE A 296 LEU A 299 
AA5 1 TYR B 77  ? LYS B 78  ? TYR B 77  LYS B 78  
AA5 2 ASP B 149 ? VAL B 150 ? ASP B 149 VAL B 150 
AA6 1 ARG B 246 ? VAL B 247 ? ARG B 246 VAL B 247 
AA6 2 ARG B 223 ? ILE B 226 ? ARG B 223 ILE B 226 
AA6 3 VAL B 313 ? LEU B 315 ? VAL B 313 LEU B 315 
AA6 4 PHE B 338 ? ILE B 339 ? PHE B 338 ILE B 339 
AA6 5 TRP B 369 ? TYR B 370 ? TRP B 369 TYR B 370 
AA7 1 SER B 249 ? ASP B 252 ? SER B 249 ASP B 252 
AA7 2 GLY B 255 ? VAL B 259 ? GLY B 255 VAL B 259 
AA7 3 PHE B 296 ? PRO B 300 ? PHE B 296 PRO B 300 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 82  ? N ARG A 82  O SER A 117 ? O SER A 117 
AA1 2 3 O LYS A 114 ? O LYS A 114 N VAL A 68  ? N VAL A 68  
AA1 3 4 O ARG A 67  ? O ARG A 67  N ILE A 47  ? N ILE A 47  
AA1 4 5 N VAL A 46  ? N VAL A 46  O GLN B 48  ? O GLN B 48  
AA1 5 6 N ARG B 45  ? N ARG B 45  O GLN B 69  ? O GLN B 69  
AA1 6 7 N VAL B 68  ? N VAL B 68  O LYS B 114 ? O LYS B 114 
AA1 7 8 O SER B 117 ? O SER B 117 N ARG B 82  ? N ARG B 82  
AA2 1 2 N TYR A 77  ? N TYR A 77  O VAL A 150 ? O VAL A 150 
AA3 1 2 O ARG A 246 ? O ARG A 246 N VAL A 224 ? N VAL A 224 
AA3 2 3 N ALA A 225 ? N ALA A 225 O VAL A 313 ? O VAL A 313 
AA3 3 4 N ALA A 314 ? N ALA A 314 O PHE A 338 ? O PHE A 338 
AA3 4 5 N ILE A 339 ? N ILE A 339 O TRP A 369 ? O TRP A 369 
AA4 1 2 N LEU A 250 ? N LEU A 250 O LEU A 257 ? O LEU A 257 
AA4 2 3 N ILE A 258 ? N ILE A 258 O THR A 297 ? O THR A 297 
AA5 1 2 N TYR B 77  ? N TYR B 77  O VAL B 150 ? O VAL B 150 
AA6 1 2 O ARG B 246 ? O ARG B 246 N VAL B 224 ? N VAL B 224 
AA6 2 3 N ALA B 225 ? N ALA B 225 O VAL B 313 ? O VAL B 313 
AA6 3 4 N ALA B 314 ? N ALA B 314 O PHE B 338 ? O PHE B 338 
AA6 4 5 N ILE B 339 ? N ILE B 339 O TRP B 369 ? O TRP B 369 
AA7 1 2 N LEU B 250 ? N LEU B 250 O LEU B 257 ? O LEU B 257 
AA7 2 3 N ILE B 258 ? N ILE B 258 O THR B 297 ? O THR B 297 
# 
_pdbx_entry_details.entry_id                   8Z29 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 B GLU 44 ? ? OH B TYR 77 ? ? 1.99 
2 1 OE1 B GLU 9  ? ? OG B SER 90 ? ? 2.08 
3 1 OE2 A GLU 44 ? ? OH A TYR 77 ? ? 2.11 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              131 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              131 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              131 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.28 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.02 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                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 GLN A 12  ? ? -67.86  3.29    
2  1 ALA A 13  ? ? -134.98 -35.23  
3  1 SER A 24  ? ? -63.17  -173.86 
4  1 GLN A 28  ? ? -161.18 -43.81  
5  1 ALA A 152 ? ? -148.77 -157.28 
6  1 ASP A 154 ? ? 174.48  -159.21 
7  1 THR A 158 ? ? -123.80 -166.90 
8  1 ASN A 214 ? ? 22.97   62.68   
9  1 SER A 218 ? ? -110.76 -164.35 
10 1 SER A 229 ? ? -148.61 27.53   
11 1 ASP A 252 ? ? -127.05 -158.91 
12 1 GLN A 254 ? ? -103.89 74.33   
13 1 ASP A 261 ? ? 76.49   155.17  
14 1 ARG A 280 ? ? 48.31   19.10   
15 1 LYS A 295 ? ? 93.03   -13.35  
16 1 SER A 317 ? ? -145.70 23.45   
17 1 ALA A 318 ? ? -111.05 -71.80  
18 1 ALA A 425 ? ? -142.19 47.75   
19 1 ASN B 23  ? ? -63.25  50.19   
20 1 THR B 148 ? ? -120.70 -57.59  
21 1 ASP B 154 ? ? -167.97 -164.81 
22 1 SER B 218 ? ? -110.36 -157.49 
23 1 SER B 229 ? ? -140.62 12.17   
24 1 LYS B 260 ? ? -153.54 -12.33  
25 1 ARG B 280 ? ? 42.93   -131.93 
26 1 LYS B 281 ? ? 76.55   173.63  
27 1 THR B 288 ? ? 92.13   6.43    
28 1 ASP B 289 ? ? -127.11 -132.50 
29 1 ALA B 290 ? ? -67.30  77.15   
30 1 ALA B 291 ? ? 69.95   -2.32   
31 1 ALA B 318 ? ? -113.18 -74.36  
32 1 THR B 426 ? ? -39.65  111.82  
33 1 ASP B 429 ? ? -31.57  116.13  
# 
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 B MET 1 ? B MET 1 
3 1 Y 1 B SER 2 ? B SER 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Science and Engineering Research Board (SERB)' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           CRG/2021/002404 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5XVI 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Z29 
_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]   0.006347 
_atom_sites.fract_transf_matrix[1][2]   0.003665 
_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]   0.007329 
_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]   0.009409 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 2   ? 47.718 -68.929 0.979   1.00 58.90  ?  2   SER A N   1 
ATOM   2    C  CA  . SER A 1 2   ? 46.395 -68.741 1.646   1.00 60.45  ?  2   SER A CA  1 
ATOM   3    C  C   . SER A 1 2   ? 46.374 -67.436 2.430   1.00 59.86  ?  2   SER A C   1 
ATOM   4    O  O   . SER A 1 2   ? 45.349 -66.758 2.435   1.00 56.06  ?  2   SER A O   1 
ATOM   5    C  CB  . SER A 1 2   ? 46.045 -69.890 2.581   1.00 57.24  ?  2   SER A CB  1 
ATOM   6    O  OG  . SER A 1 2   ? 46.510 -71.137 2.071   1.00 49.54  ?  2   SER A OG  1 
ATOM   7    N  N   . ASN A 1 3   ? 47.503 -67.163 3.115   1.00 66.11  ?  3   ASN A N   1 
ATOM   8    C  CA  . ASN A 1 3   ? 47.730 -65.980 3.935   1.00 64.36  ?  3   ASN A CA  1 
ATOM   9    C  C   . ASN A 1 3   ? 47.871 -64.738 3.062   1.00 56.89  ?  3   ASN A C   1 
ATOM   10   O  O   . ASN A 1 3   ? 47.776 -63.623 3.564   1.00 47.48  ?  3   ASN A O   1 
ATOM   11   C  CB  . ASN A 1 3   ? 49.011 -66.095 4.761   1.00 71.80  ?  3   ASN A CB  1 
ATOM   12   C  CG  . ASN A 1 3   ? 50.269 -66.068 3.916   1.00 72.87  ?  3   ASN A CG  1 
ATOM   13   O  OD1 . ASN A 1 3   ? 50.985 -65.061 3.887   1.00 79.48  ?  3   ASN A OD1 1 
ATOM   14   N  ND2 . ASN A 1 3   ? 50.558 -67.150 3.211   1.00 73.07  ?  3   ASN A ND2 1 
ATOM   15   N  N   . LEU A 1 4   ? 48.139 -64.952 1.768   1.00 52.95  ?  4   LEU A N   1 
ATOM   16   C  CA  . LEU A 1 4   ? 48.485 -63.863 0.878   1.00 55.58  ?  4   LEU A CA  1 
ATOM   17   C  C   . LEU A 1 4   ? 47.283 -62.938 0.730   1.00 55.06  ?  4   LEU A C   1 
ATOM   18   O  O   . LEU A 1 4   ? 46.145 -63.399 0.793   1.00 52.52  ?  4   LEU A O   1 
ATOM   19   C  CB  . LEU A 1 4   ? 48.975 -64.416 -0.459  1.00 55.37  ?  4   LEU A CB  1 
ATOM   20   C  CG  . LEU A 1 4   ? 50.237 -65.288 -0.374  1.00 61.98  ?  4   LEU A CG  1 
ATOM   21   C  CD1 . LEU A 1 4   ? 50.668 -65.735 -1.765  1.00 59.10  ?  4   LEU A CD1 1 
ATOM   22   C  CD2 . LEU A 1 4   ? 51.407 -64.612 0.376   1.00 58.73  ?  4   LEU A CD2 1 
ATOM   23   N  N   . PRO A 1 5   ? 47.515 -61.607 0.598   1.00 55.47  ?  5   PRO A N   1 
ATOM   24   C  CA  . PRO A 1 5   ? 46.457 -60.649 0.255   1.00 50.54  ?  5   PRO A CA  1 
ATOM   25   C  C   . PRO A 1 5   ? 45.869 -60.984 -1.116  1.00 45.45  ?  5   PRO A C   1 
ATOM   26   O  O   . PRO A 1 5   ? 46.535 -61.599 -1.950  1.00 45.15  ?  5   PRO A O   1 
ATOM   27   C  CB  . PRO A 1 5   ? 47.198 -59.291 0.258   1.00 48.90  ?  5   PRO A CB  1 
ATOM   28   C  CG  . PRO A 1 5   ? 48.616 -59.684 -0.075  1.00 54.13  ?  5   PRO A CG  1 
ATOM   29   C  CD  . PRO A 1 5   ? 48.828 -60.953 0.742   1.00 56.22  ?  5   PRO A CD  1 
ATOM   30   N  N   . VAL A 1 6   ? 44.622 -60.568 -1.352  1.00 41.14  ?  6   VAL A N   1 
ATOM   31   C  CA  . VAL A 1 6   ? 44.025 -60.745 -2.664  1.00 44.74  ?  6   VAL A CA  1 
ATOM   32   C  C   . VAL A 1 6   ? 44.426 -59.527 -3.490  1.00 44.58  ?  6   VAL A C   1 
ATOM   33   O  O   . VAL A 1 6   ? 44.218 -58.391 -3.061  1.00 46.61  ?  6   VAL A O   1 
ATOM   34   C  CB  . VAL A 1 6   ? 42.496 -60.944 -2.743  1.00 47.85  ?  6   VAL A CB  1 
ATOM   35   C  CG1 . VAL A 1 6   ? 42.147 -61.778 -3.977  1.00 46.65  ?  6   VAL A CG1 1 
ATOM   36   C  CG2 . VAL A 1 6   ? 41.894 -61.577 -1.486  1.00 47.62  ?  6   VAL A CG2 1 
ATOM   37   N  N   . GLU A 1 7   ? 45.017 -59.789 -4.664  1.00 39.28  ?  7   GLU A N   1 
ATOM   38   C  CA  . GLU A 1 7   ? 45.493 -58.740 -5.546  1.00 34.28  ?  7   GLU A CA  1 
ATOM   39   C  C   . GLU A 1 7   ? 44.936 -59.027 -6.933  1.00 31.90  ?  7   GLU A C   1 
ATOM   40   O  O   . GLU A 1 7   ? 45.646 -59.555 -7.776  1.00 37.91  ?  7   GLU A O   1 
ATOM   41   C  CB  . GLU A 1 7   ? 47.023 -58.711 -5.534  1.00 31.35  ?  7   GLU A CB  1 
ATOM   42   C  CG  . GLU A 1 7   ? 47.623 -58.222 -4.219  1.00 31.33  ?  7   GLU A CG  1 
ATOM   43   C  CD  . GLU A 1 7   ? 49.126 -58.434 -4.066  1.00 33.57  ?  7   GLU A CD  1 
ATOM   44   O  OE1 . GLU A 1 7   ? 49.719 -59.198 -4.862  1.00 32.39  ?  7   GLU A OE1 1 
ATOM   45   O  OE2 . GLU A 1 7   ? 49.732 -57.832 -3.148  1.00 34.53  -1 7   GLU A OE2 1 
ATOM   46   N  N   . PRO A 1 8   ? 43.647 -58.734 -7.194  1.00 27.69  ?  8   PRO A N   1 
ATOM   47   C  CA  . PRO A 1 8   ? 42.968 -59.240 -8.390  1.00 27.80  ?  8   PRO A CA  1 
ATOM   48   C  C   . PRO A 1 8   ? 43.620 -58.915 -9.734  1.00 28.51  ?  8   PRO A C   1 
ATOM   49   O  O   . PRO A 1 8   ? 43.691 -59.771 -10.613 1.00 29.24  ?  8   PRO A O   1 
ATOM   50   C  CB  . PRO A 1 8   ? 41.536 -58.658 -8.280  1.00 27.29  ?  8   PRO A CB  1 
ATOM   51   C  CG  . PRO A 1 8   ? 41.619 -57.580 -7.231  1.00 27.74  ?  8   PRO A CG  1 
ATOM   52   C  CD  . PRO A 1 8   ? 42.759 -57.970 -6.308  1.00 27.94  ?  8   PRO A CD  1 
ATOM   53   N  N   . GLU A 1 9   ? 44.126 -57.688 -9.873  1.00 28.89  ?  9   GLU A N   1 
ATOM   54   C  CA  . GLU A 1 9   ? 44.806 -57.270 -11.088 1.00 30.63  ?  9   GLU A CA  1 
ATOM   55   C  C   . GLU A 1 9   ? 46.039 -58.152 -11.331 1.00 33.42  ?  9   GLU A C   1 
ATOM   56   O  O   . GLU A 1 9   ? 46.295 -58.599 -12.452 1.00 37.62  ?  9   GLU A O   1 
ATOM   57   C  CB  . GLU A 1 9   ? 45.153 -55.780 -11.012 1.00 29.42  ?  9   GLU A CB  1 
ATOM   58   C  CG  . GLU A 1 9   ? 43.934 -54.857 -11.016 1.00 29.38  ?  9   GLU A CG  1 
ATOM   59   C  CD  . GLU A 1 9   ? 43.388 -54.416 -9.664  1.00 31.72  ?  9   GLU A CD  1 
ATOM   60   O  OE1 . GLU A 1 9   ? 42.323 -53.739 -9.680  1.00 28.23  ?  9   GLU A OE1 1 
ATOM   61   O  OE2 . GLU A 1 9   ? 44.009 -54.719 -8.601  1.00 33.22  -1 9   GLU A OE2 1 
ATOM   62   N  N   . PHE A 1 10  ? 46.808 -58.415 -10.274 1.00 34.75  ?  10  PHE A N   1 
ATOM   63   C  CA  . PHE A 1 10  ? 48.054 -59.148 -10.419 1.00 35.02  ?  10  PHE A CA  1 
ATOM   64   C  C   . PHE A 1 10  ? 47.733 -60.573 -10.849 1.00 35.20  ?  10  PHE A C   1 
ATOM   65   O  O   . PHE A 1 10  ? 48.232 -61.022 -11.872 1.00 43.25  ?  10  PHE A O   1 
ATOM   66   C  CB  . PHE A 1 10  ? 48.944 -59.134 -9.171  1.00 33.84  ?  10  PHE A CB  1 
ATOM   67   C  CG  . PHE A 1 10  ? 50.163 -60.048 -9.288  1.00 34.50  ?  10  PHE A CG  1 
ATOM   68   C  CD1 . PHE A 1 10  ? 51.221 -59.719 -10.128 1.00 33.77  ?  10  PHE A CD1 1 
ATOM   69   C  CD2 . PHE A 1 10  ? 50.251 -61.240 -8.563  1.00 33.50  ?  10  PHE A CD2 1 
ATOM   70   C  CE1 . PHE A 1 10  ? 52.320 -60.556 -10.256 1.00 31.48  ?  10  PHE A CE1 1 
ATOM   71   C  CE2 . PHE A 1 10  ? 51.362 -62.065 -8.674  1.00 31.04  ?  10  PHE A CE2 1 
ATOM   72   C  CZ  . PHE A 1 10  ? 52.387 -61.727 -9.531  1.00 32.24  ?  10  PHE A CZ  1 
ATOM   73   N  N   . GLU A 1 11  ? 46.898 -61.280 -10.088 1.00 35.47  ?  11  GLU A N   1 
ATOM   74   C  CA  . GLU A 1 11  ? 46.699 -62.696 -10.358 1.00 36.89  ?  11  GLU A CA  1 
ATOM   75   C  C   . GLU A 1 11  ? 45.798 -62.898 -11.566 1.00 40.97  ?  11  GLU A C   1 
ATOM   76   O  O   . GLU A 1 11  ? 45.808 -63.990 -12.119 1.00 45.88  ?  11  GLU A O   1 
ATOM   77   C  CB  . GLU A 1 11  ? 46.222 -63.547 -9.184  1.00 39.75  ?  11  GLU A CB  1 
ATOM   78   C  CG  . GLU A 1 11  ? 45.070 -62.953 -8.380  1.00 43.67  ?  11  GLU A CG  1 
ATOM   79   C  CD  . GLU A 1 11  ? 45.406 -63.123 -6.907  1.00 44.42  ?  11  GLU A CD  1 
ATOM   80   O  OE1 . GLU A 1 11  ? 46.495 -62.612 -6.556  1.00 41.13  ?  11  GLU A OE1 1 
ATOM   81   O  OE2 . GLU A 1 11  ? 44.632 -63.756 -6.143  1.00 43.38  -1 11  GLU A OE2 1 
ATOM   82   N  N   . GLN A 1 12  ? 45.076 -61.855 -12.013 1.00 42.14  ?  12  GLN A N   1 
ATOM   83   C  CA  . GLN A 1 12  ? 44.364 -61.931 -13.282 1.00 40.24  ?  12  GLN A CA  1 
ATOM   84   C  C   . GLN A 1 12  ? 45.356 -61.992 -14.452 1.00 40.40  ?  12  GLN A C   1 
ATOM   85   O  O   . GLN A 1 12  ? 44.917 -61.998 -15.601 1.00 43.05  ?  12  GLN A O   1 
ATOM   86   C  CB  . GLN A 1 12  ? 43.391 -60.758 -13.445 1.00 43.93  ?  12  GLN A CB  1 
ATOM   87   C  CG  . GLN A 1 12  ? 42.457 -60.856 -14.654 1.00 51.79  ?  12  GLN A CG  1 
ATOM   88   C  CD  . GLN A 1 12  ? 41.125 -60.134 -14.476 1.00 63.64  ?  12  GLN A CD  1 
ATOM   89   O  OE1 . GLN A 1 12  ? 40.246 -60.530 -13.690 1.00 48.33  ?  12  GLN A OE1 1 
ATOM   90   N  NE2 . GLN A 1 12  ? 40.941 -59.057 -15.231 1.00 70.43  ?  12  GLN A NE2 1 
ATOM   91   N  N   . ALA A 1 13  ? 46.674 -62.037 -14.170 1.00 33.00  ?  13  ALA A N   1 
ATOM   92   C  CA  . ALA A 1 13  ? 47.713 -61.859 -15.179 1.00 31.99  ?  13  ALA A CA  1 
ATOM   93   C  C   . ALA A 1 13  ? 48.816 -62.909 -15.022 1.00 32.72  ?  13  ALA A C   1 
ATOM   94   O  O   . ALA A 1 13  ? 49.409 -63.348 -16.012 1.00 29.05  ?  13  ALA A O   1 
ATOM   95   C  CB  . ALA A 1 13  ? 48.284 -60.459 -15.099 1.00 30.81  ?  13  ALA A CB  1 
ATOM   96   N  N   . TYR A 1 14  ? 49.106 -63.276 -13.763 1.00 31.06  ?  14  TYR A N   1 
ATOM   97   C  CA  . TYR A 1 14  ? 49.786 -64.526 -13.446 1.00 28.50  ?  14  TYR A CA  1 
ATOM   98   C  C   . TYR A 1 14  ? 49.077 -65.698 -14.132 1.00 28.47  ?  14  TYR A C   1 
ATOM   99   O  O   . TYR A 1 14  ? 49.706 -66.492 -14.828 1.00 27.15  ?  14  TYR A O   1 
ATOM   100  C  CB  . TYR A 1 14  ? 49.834 -64.767 -11.936 1.00 23.47  ?  14  TYR A CB  1 
ATOM   101  C  CG  . TYR A 1 14  ? 50.447 -66.118 -11.624 1.00 24.44  ?  14  TYR A CG  1 
ATOM   102  C  CD1 . TYR A 1 14  ? 51.821 -66.325 -11.730 1.00 25.26  ?  14  TYR A CD1 1 
ATOM   103  C  CD2 . TYR A 1 14  ? 49.665 -67.190 -11.202 1.00 24.60  ?  14  TYR A CD2 1 
ATOM   104  C  CE1 . TYR A 1 14  ? 52.394 -67.549 -11.427 1.00 24.32  ?  14  TYR A CE1 1 
ATOM   105  C  CE2 . TYR A 1 14  ? 50.231 -68.418 -10.887 1.00 23.77  ?  14  TYR A CE2 1 
ATOM   106  C  CZ  . TYR A 1 14  ? 51.596 -68.602 -11.015 1.00 23.86  ?  14  TYR A CZ  1 
ATOM   107  O  OH  . TYR A 1 14  ? 52.160 -69.814 -10.741 1.00 23.72  ?  14  TYR A OH  1 
ATOM   108  N  N   . LYS A 1 15  ? 47.756 -65.761 -13.927 1.00 31.02  ?  15  LYS A N   1 
ATOM   109  C  CA  . LYS A 1 15  ? 46.885 -66.750 -14.538 1.00 37.24  ?  15  LYS A CA  1 
ATOM   110  C  C   . LYS A 1 15  ? 46.997 -66.686 -16.061 1.00 38.69  ?  15  LYS A C   1 
ATOM   111  O  O   . LYS A 1 15  ? 47.226 -67.724 -16.690 1.00 37.69  ?  15  LYS A O   1 
ATOM   112  C  CB  . LYS A 1 15  ? 45.428 -66.585 -14.078 1.00 39.00  ?  15  LYS A CB  1 
ATOM   113  C  CG  . LYS A 1 15  ? 44.992 -67.332 -12.808 1.00 38.88  ?  15  LYS A CG  1 
ATOM   114  C  CD  . LYS A 1 15  ? 45.948 -67.371 -11.614 1.00 40.38  ?  15  LYS A CD  1 
ATOM   115  C  CE  . LYS A 1 15  ? 46.504 -68.752 -11.293 1.00 44.27  ?  15  LYS A CE  1 
ATOM   116  N  NZ  . LYS A 1 15  ? 47.278 -69.388 -12.372 1.00 44.98  1  15  LYS A NZ  1 
ATOM   117  N  N   . GLU A 1 16  ? 46.855 -65.471 -16.626 1.00 36.73  ?  16  GLU A N   1 
ATOM   118  C  CA  . GLU A 1 16  ? 46.831 -65.280 -18.071 1.00 35.74  ?  16  GLU A CA  1 
ATOM   119  C  C   . GLU A 1 16  ? 48.095 -65.889 -18.675 1.00 36.56  ?  16  GLU A C   1 
ATOM   120  O  O   . GLU A 1 16  ? 48.003 -66.535 -19.717 1.00 38.21  ?  16  GLU A O   1 
ATOM   121  C  CB  . GLU A 1 16  ? 46.547 -63.829 -18.495 1.00 36.75  ?  16  GLU A CB  1 
ATOM   122  C  CG  . GLU A 1 16  ? 45.057 -63.478 -18.392 1.00 40.61  ?  16  GLU A CG  1 
ATOM   123  C  CD  . GLU A 1 16  ? 44.502 -62.065 -18.586 1.00 41.42  ?  16  GLU A CD  1 
ATOM   124  O  OE1 . GLU A 1 16  ? 43.665 -61.603 -17.761 1.00 43.32  ?  16  GLU A OE1 1 
ATOM   125  O  OE2 . GLU A 1 16  ? 44.859 -61.426 -19.585 1.00 42.38  -1 16  GLU A OE2 1 
ATOM   126  N  N   . LEU A 1 17  ? 49.247 -65.715 -17.994 1.00 34.10  ?  17  LEU A N   1 
ATOM   127  C  CA  . LEU A 1 17  ? 50.543 -66.143 -18.500 1.00 30.66  ?  17  LEU A CA  1 
ATOM   128  C  C   . LEU A 1 17  ? 50.668 -67.653 -18.341 1.00 31.67  ?  17  LEU A C   1 
ATOM   129  O  O   . LEU A 1 17  ? 50.996 -68.346 -19.309 1.00 35.60  ?  17  LEU A O   1 
ATOM   130  C  CB  . LEU A 1 17  ? 51.707 -65.423 -17.815 1.00 32.28  ?  17  LEU A CB  1 
ATOM   131  C  CG  . LEU A 1 17  ? 53.123 -65.817 -18.274 1.00 34.40  ?  17  LEU A CG  1 
ATOM   132  C  CD1 . LEU A 1 17  ? 53.508 -65.302 -19.668 1.00 31.93  ?  17  LEU A CD1 1 
ATOM   133  C  CD2 . LEU A 1 17  ? 54.151 -65.365 -17.241 1.00 35.58  ?  17  LEU A CD2 1 
ATOM   134  N  N   . ALA A 1 18  ? 50.435 -68.155 -17.118 1.00 27.88  ?  18  ALA A N   1 
ATOM   135  C  CA  . ALA A 1 18  ? 50.381 -69.597 -16.882 1.00 23.90  ?  18  ALA A CA  1 
ATOM   136  C  C   . ALA A 1 18  ? 49.551 -70.296 -17.970 1.00 19.99  ?  18  ALA A C   1 
ATOM   137  O  O   . ALA A 1 18  ? 50.022 -71.268 -18.539 1.00 16.89  ?  18  ALA A O   1 
ATOM   138  C  CB  . ALA A 1 18  ? 49.852 -69.902 -15.477 1.00 23.70  ?  18  ALA A CB  1 
ATOM   139  N  N   . SER A 1 19  ? 48.334 -69.794 -18.246 1.00 19.10  ?  19  SER A N   1 
ATOM   140  C  CA  . SER A 1 19  ? 47.438 -70.318 -19.274 1.00 20.68  ?  19  SER A CA  1 
ATOM   141  C  C   . SER A 1 19  ? 48.163 -70.550 -20.603 1.00 23.31  ?  19  SER A C   1 
ATOM   142  O  O   . SER A 1 19  ? 48.086 -71.664 -21.175 1.00 21.92  ?  19  SER A O   1 
ATOM   143  C  CB  . SER A 1 19  ? 46.284 -69.380 -19.531 1.00 21.67  ?  19  SER A CB  1 
ATOM   144  O  OG  . SER A 1 19  ? 45.575 -69.022 -18.353 1.00 23.36  ?  19  SER A OG  1 
ATOM   145  N  N   . THR A 1 20  ? 48.823 -69.461 -21.079 1.00 21.36  ?  20  THR A N   1 
ATOM   146  C  CA  . THR A 1 20  ? 49.528 -69.424 -22.357 1.00 20.52  ?  20  THR A CA  1 
ATOM   147  C  C   . THR A 1 20  ? 50.619 -70.494 -22.357 1.00 20.76  ?  20  THR A C   1 
ATOM   148  O  O   . THR A 1 20  ? 50.720 -71.269 -23.298 1.00 18.71  ?  20  THR A O   1 
ATOM   149  C  CB  . THR A 1 20  ? 50.156 -68.047 -22.629 1.00 20.42  ?  20  THR A CB  1 
ATOM   150  O  OG1 . THR A 1 20  ? 49.303 -66.936 -22.347 1.00 18.83  ?  20  THR A OG1 1 
ATOM   151  C  CG2 . THR A 1 20  ? 50.615 -67.919 -24.073 1.00 20.24  ?  20  THR A CG2 1 
ATOM   152  N  N   . LEU A 1 21  ? 51.418 -70.521 -21.275 1.00 24.60  ?  21  LEU A N   1 
ATOM   153  C  CA  . LEU A 1 21  ? 52.647 -71.305 -21.182 1.00 27.56  ?  21  LEU A CA  1 
ATOM   154  C  C   . LEU A 1 21  ? 52.338 -72.799 -21.171 1.00 26.93  ?  21  LEU A C   1 
ATOM   155  O  O   . LEU A 1 21  ? 53.020 -73.565 -21.850 1.00 26.37  ?  21  LEU A O   1 
ATOM   156  C  CB  . LEU A 1 21  ? 53.461 -70.898 -19.947 1.00 29.54  ?  21  LEU A CB  1 
ATOM   157  C  CG  . LEU A 1 21  ? 54.106 -69.504 -19.980 1.00 30.97  ?  21  LEU A CG  1 
ATOM   158  C  CD1 . LEU A 1 21  ? 55.037 -69.287 -18.799 1.00 29.56  ?  21  LEU A CD1 1 
ATOM   159  C  CD2 . LEU A 1 21  ? 54.879 -69.243 -21.274 1.00 33.61  ?  21  LEU A CD2 1 
ATOM   160  N  N   . GLU A 1 22  ? 51.336 -73.171 -20.355 1.00 28.87  ?  22  GLU A N   1 
ATOM   161  C  CA  . GLU A 1 22  ? 50.775 -74.511 -20.272 1.00 27.75  ?  22  GLU A CA  1 
ATOM   162  C  C   . GLU A 1 22  ? 50.346 -74.960 -21.657 1.00 30.04  ?  22  GLU A C   1 
ATOM   163  O  O   . GLU A 1 22  ? 50.845 -75.960 -22.140 1.00 30.97  ?  22  GLU A O   1 
ATOM   164  C  CB  . GLU A 1 22  ? 49.527 -74.525 -19.386 1.00 27.35  ?  22  GLU A CB  1 
ATOM   165  C  CG  . GLU A 1 22  ? 49.811 -74.404 -17.891 1.00 25.37  ?  22  GLU A CG  1 
ATOM   166  C  CD  . GLU A 1 22  ? 50.612 -75.553 -17.319 1.00 24.67  ?  22  GLU A CD  1 
ATOM   167  O  OE1 . GLU A 1 22  ? 51.252 -75.390 -16.278 1.00 25.94  ?  22  GLU A OE1 1 
ATOM   168  O  OE2 . GLU A 1 22  ? 50.622 -76.633 -17.903 1.00 25.44  -1 22  GLU A OE2 1 
ATOM   169  N  N   . ASN A 1 23  ? 49.436 -74.183 -22.275 1.00 33.67  ?  23  ASN A N   1 
ATOM   170  C  CA  . ASN A 1 23  ? 48.808 -74.509 -23.552 1.00 32.36  ?  23  ASN A CA  1 
ATOM   171  C  C   . ASN A 1 23  ? 49.870 -74.669 -24.642 1.00 34.00  ?  23  ASN A C   1 
ATOM   172  O  O   . ASN A 1 23  ? 49.726 -75.525 -25.519 1.00 35.55  ?  23  ASN A O   1 
ATOM   173  C  CB  . ASN A 1 23  ? 47.707 -73.497 -23.852 1.00 30.88  ?  23  ASN A CB  1 
ATOM   174  C  CG  . ASN A 1 23  ? 47.036 -73.695 -25.187 1.00 33.35  ?  23  ASN A CG  1 
ATOM   175  O  OD1 . ASN A 1 23  ? 46.770 -74.821 -25.630 1.00 30.85  ?  23  ASN A OD1 1 
ATOM   176  N  ND2 . ASN A 1 23  ? 46.739 -72.586 -25.839 1.00 37.86  ?  23  ASN A ND2 1 
ATOM   177  N  N   . SER A 1 24  ? 50.947 -73.865 -24.574 1.00 33.12  ?  24  SER A N   1 
ATOM   178  C  CA  . SER A 1 24  ? 52.080 -74.022 -25.480 1.00 31.74  ?  24  SER A CA  1 
ATOM   179  C  C   . SER A 1 24  ? 52.733 -75.396 -25.252 1.00 29.80  ?  24  SER A C   1 
ATOM   180  O  O   . SER A 1 24  ? 52.210 -76.218 -24.490 1.00 24.81  ?  24  SER A O   1 
ATOM   181  C  CB  . SER A 1 24  ? 53.076 -72.889 -25.323 1.00 31.20  ?  24  SER A CB  1 
ATOM   182  O  OG  . SER A 1 24  ? 54.155 -73.269 -24.475 1.00 32.80  ?  24  SER A OG  1 
ATOM   183  N  N   . THR A 1 25  ? 53.871 -75.651 -25.919 1.00 28.57  ?  25  THR A N   1 
ATOM   184  C  CA  . THR A 1 25  ? 54.577 -76.922 -25.771 1.00 32.38  ?  25  THR A CA  1 
ATOM   185  C  C   . THR A 1 25  ? 55.799 -76.760 -24.850 1.00 32.32  ?  25  THR A C   1 
ATOM   186  O  O   . THR A 1 25  ? 56.623 -77.668 -24.720 1.00 30.75  ?  25  THR A O   1 
ATOM   187  C  CB  . THR A 1 25  ? 54.923 -77.470 -27.162 1.00 34.35  ?  25  THR A CB  1 
ATOM   188  O  OG1 . THR A 1 25  ? 55.805 -76.592 -27.862 1.00 37.05  ?  25  THR A OG1 1 
ATOM   189  C  CG2 . THR A 1 25  ? 53.697 -77.628 -28.043 1.00 33.57  ?  25  THR A CG2 1 
ATOM   190  N  N   . LEU A 1 26  ? 55.863 -75.621 -24.146 1.00 31.02  ?  26  LEU A N   1 
ATOM   191  C  CA  . LEU A 1 26  ? 57.008 -75.259 -23.339 1.00 28.59  ?  26  LEU A CA  1 
ATOM   192  C  C   . LEU A 1 26  ? 57.190 -76.221 -22.170 1.00 27.57  ?  26  LEU A C   1 
ATOM   193  O  O   . LEU A 1 26  ? 58.320 -76.637 -21.927 1.00 27.06  ?  26  LEU A O   1 
ATOM   194  C  CB  . LEU A 1 26  ? 56.869 -73.827 -22.822 1.00 29.09  ?  26  LEU A CB  1 
ATOM   195  C  CG  . LEU A 1 26  ? 57.870 -73.416 -21.731 1.00 25.33  ?  26  LEU A CG  1 
ATOM   196  C  CD1 . LEU A 1 26  ? 59.259 -73.488 -22.349 1.00 24.63  ?  26  LEU A CD1 1 
ATOM   197  C  CD2 . LEU A 1 26  ? 57.568 -72.051 -21.158 1.00 23.79  ?  26  LEU A CD2 1 
ATOM   198  N  N   . PHE A 1 27  ? 56.127 -76.486 -21.397 1.00 27.99  ?  27  PHE A N   1 
ATOM   199  C  CA  . PHE A 1 27  ? 56.266 -77.246 -20.152 1.00 32.17  ?  27  PHE A CA  1 
ATOM   200  C  C   . PHE A 1 27  ? 56.188 -78.753 -20.451 1.00 39.45  ?  27  PHE A C   1 
ATOM   201  O  O   . PHE A 1 27  ? 55.419 -79.500 -19.848 1.00 53.63  ?  27  PHE A O   1 
ATOM   202  C  CB  . PHE A 1 27  ? 55.223 -76.783 -19.121 1.00 31.50  ?  27  PHE A CB  1 
ATOM   203  C  CG  . PHE A 1 27  ? 55.359 -75.386 -18.506 1.00 28.87  ?  27  PHE A CG  1 
ATOM   204  C  CD1 . PHE A 1 27  ? 54.239 -74.723 -18.019 1.00 27.79  ?  27  PHE A CD1 1 
ATOM   205  C  CD2 . PHE A 1 27  ? 56.589 -74.749 -18.385 1.00 29.23  ?  27  PHE A CD2 1 
ATOM   206  C  CE1 . PHE A 1 27  ? 54.339 -73.464 -17.453 1.00 28.58  ?  27  PHE A CE1 1 
ATOM   207  C  CE2 . PHE A 1 27  ? 56.688 -73.490 -17.807 1.00 29.94  ?  27  PHE A CE2 1 
ATOM   208  C  CZ  . PHE A 1 27  ? 55.562 -72.855 -17.334 1.00 29.33  ?  27  PHE A CZ  1 
ATOM   209  N  N   . GLN A 1 28  ? 57.024 -79.190 -21.397 1.00 38.54  ?  28  GLN A N   1 
ATOM   210  C  CA  . GLN A 1 28  ? 57.012 -80.512 -21.990 1.00 35.39  ?  28  GLN A CA  1 
ATOM   211  C  C   . GLN A 1 28  ? 58.372 -80.731 -22.640 1.00 31.16  ?  28  GLN A C   1 
ATOM   212  O  O   . GLN A 1 28  ? 58.917 -81.820 -22.579 1.00 35.02  ?  28  GLN A O   1 
ATOM   213  C  CB  . GLN A 1 28  ? 56.007 -80.660 -23.135 1.00 41.51  ?  28  GLN A CB  1 
ATOM   214  C  CG  . GLN A 1 28  ? 54.532 -80.587 -22.743 1.00 42.16  ?  28  GLN A CG  1 
ATOM   215  C  CD  . GLN A 1 28  ? 53.601 -80.953 -23.883 1.00 41.55  ?  28  GLN A CD  1 
ATOM   216  O  OE1 . GLN A 1 28  ? 52.452 -81.358 -23.669 1.00 36.01  ?  28  GLN A OE1 1 
ATOM   217  N  NE2 . GLN A 1 28  ? 54.087 -80.845 -25.114 1.00 44.25  ?  28  GLN A NE2 1 
ATOM   218  N  N   . LYS A 1 29  ? 58.863 -79.714 -23.344 1.00 27.91  ?  29  LYS A N   1 
ATOM   219  C  CA  . LYS A 1 29  ? 60.284 -79.589 -23.634 1.00 30.68  ?  29  LYS A CA  1 
ATOM   220  C  C   . LYS A 1 29  ? 61.025 -79.198 -22.351 1.00 31.62  ?  29  LYS A C   1 
ATOM   221  O  O   . LYS A 1 29  ? 62.102 -79.711 -22.049 1.00 27.61  ?  29  LYS A O   1 
ATOM   222  C  CB  . LYS A 1 29  ? 60.472 -78.580 -24.779 1.00 30.61  ?  29  LYS A CB  1 
ATOM   223  C  CG  . LYS A 1 29  ? 59.909 -79.086 -26.103 1.00 31.54  ?  29  LYS A CG  1 
ATOM   224  C  CD  . LYS A 1 29  ? 59.555 -78.072 -27.180 1.00 31.52  ?  29  LYS A CD  1 
ATOM   225  C  CE  . LYS A 1 29  ? 58.505 -78.692 -28.075 1.00 34.75  ?  29  LYS A CE  1 
ATOM   226  N  NZ  . LYS A 1 29  ? 58.564 -78.207 -29.459 1.00 36.21  1  29  LYS A NZ  1 
ATOM   227  N  N   . ASN A 1 30  ? 60.416 -78.281 -21.591 1.00 33.82  ?  30  ASN A N   1 
ATOM   228  C  CA  . ASN A 1 30  ? 61.061 -77.648 -20.458 1.00 35.82  ?  30  ASN A CA  1 
ATOM   229  C  C   . ASN A 1 30  ? 60.161 -77.669 -19.223 1.00 36.99  ?  30  ASN A C   1 
ATOM   230  O  O   . ASN A 1 30  ? 59.769 -76.606 -18.742 1.00 36.99  ?  30  ASN A O   1 
ATOM   231  C  CB  . ASN A 1 30  ? 61.431 -76.213 -20.809 1.00 37.77  ?  30  ASN A CB  1 
ATOM   232  C  CG  . ASN A 1 30  ? 62.448 -76.153 -21.915 1.00 38.68  ?  30  ASN A CG  1 
ATOM   233  O  OD1 . ASN A 1 30  ? 62.215 -75.496 -22.936 1.00 43.15  ?  30  ASN A OD1 1 
ATOM   234  N  ND2 . ASN A 1 30  ? 63.569 -76.832 -21.724 1.00 38.52  ?  30  ASN A ND2 1 
ATOM   235  N  N   . PRO A 1 31  ? 59.855 -78.860 -18.647 1.00 38.48  ?  31  PRO A N   1 
ATOM   236  C  CA  . PRO A 1 31  ? 59.063 -78.968 -17.413 1.00 33.64  ?  31  PRO A CA  1 
ATOM   237  C  C   . PRO A 1 31  ? 59.502 -77.983 -16.334 1.00 33.31  ?  31  PRO A C   1 
ATOM   238  O  O   . PRO A 1 31  ? 58.662 -77.342 -15.692 1.00 26.99  ?  31  PRO A O   1 
ATOM   239  C  CB  . PRO A 1 31  ? 59.264 -80.396 -16.919 1.00 34.80  ?  31  PRO A CB  1 
ATOM   240  C  CG  . PRO A 1 31  ? 59.946 -81.151 -18.059 1.00 38.75  ?  31  PRO A CG  1 
ATOM   241  C  CD  . PRO A 1 31  ? 60.271 -80.169 -19.174 1.00 40.13  ?  31  PRO A CD  1 
ATOM   242  N  N   . GLU A 1 32  ? 60.832 -77.837 -16.216 1.00 35.03  ?  32  GLU A N   1 
ATOM   243  C  CA  . GLU A 1 32  ? 61.478 -77.254 -15.046 1.00 39.68  ?  32  GLU A CA  1 
ATOM   244  C  C   . GLU A 1 32  ? 61.297 -75.736 -15.018 1.00 37.23  ?  32  GLU A C   1 
ATOM   245  O  O   . GLU A 1 32  ? 61.530 -75.113 -13.989 1.00 40.11  ?  32  GLU A O   1 
ATOM   246  C  CB  . GLU A 1 32  ? 62.938 -77.728 -14.936 1.00 43.64  ?  32  GLU A CB  1 
ATOM   247  C  CG  . GLU A 1 32  ? 63.849 -77.301 -16.088 1.00 49.36  ?  32  GLU A CG  1 
ATOM   248  C  CD  . GLU A 1 32  ? 63.557 -77.949 -17.439 1.00 53.09  ?  32  GLU A CD  1 
ATOM   249  O  OE1 . GLU A 1 32  ? 62.823 -77.334 -18.230 1.00 56.62  ?  32  GLU A OE1 1 
ATOM   250  O  OE2 . GLU A 1 32  ? 64.054 -79.053 -17.721 1.00 52.65  -1 32  GLU A OE2 1 
ATOM   251  N  N   . TYR A 1 33  ? 60.852 -75.149 -16.135 1.00 38.67  ?  33  TYR A N   1 
ATOM   252  C  CA  . TYR A 1 33  ? 60.543 -73.724 -16.233 1.00 37.08  ?  33  TYR A CA  1 
ATOM   253  C  C   . TYR A 1 33  ? 59.303 -73.342 -15.409 1.00 35.57  ?  33  TYR A C   1 
ATOM   254  O  O   . TYR A 1 33  ? 59.069 -72.157 -15.178 1.00 35.19  ?  33  TYR A O   1 
ATOM   255  C  CB  . TYR A 1 33  ? 60.386 -73.380 -17.723 1.00 40.88  ?  33  TYR A CB  1 
ATOM   256  C  CG  . TYR A 1 33  ? 61.656 -72.964 -18.457 1.00 42.20  ?  33  TYR A CG  1 
ATOM   257  C  CD1 . TYR A 1 33  ? 61.618 -71.954 -19.411 1.00 43.27  ?  33  TYR A CD1 1 
ATOM   258  C  CD2 . TYR A 1 33  ? 62.895 -73.538 -18.173 1.00 44.56  ?  33  TYR A CD2 1 
ATOM   259  C  CE1 . TYR A 1 33  ? 62.763 -71.539 -20.072 1.00 45.81  ?  33  TYR A CE1 1 
ATOM   260  C  CE2 . TYR A 1 33  ? 64.054 -73.120 -18.814 1.00 44.45  ?  33  TYR A CE2 1 
ATOM   261  C  CZ  . TYR A 1 33  ? 63.985 -72.123 -19.775 1.00 47.96  ?  33  TYR A CZ  1 
ATOM   262  O  OH  . TYR A 1 33  ? 65.102 -71.686 -20.432 1.00 45.01  ?  33  TYR A OH  1 
ATOM   263  N  N   . ARG A 1 34  ? 58.508 -74.329 -14.954 1.00 34.00  ?  34  ARG A N   1 
ATOM   264  C  CA  . ARG A 1 34  ? 57.474 -74.108 -13.944 1.00 31.10  ?  34  ARG A CA  1 
ATOM   265  C  C   . ARG A 1 34  ? 58.049 -73.513 -12.653 1.00 30.11  ?  34  ARG A C   1 
ATOM   266  O  O   . ARG A 1 34  ? 57.379 -72.732 -11.980 1.00 28.53  ?  34  ARG A O   1 
ATOM   267  C  CB  . ARG A 1 34  ? 56.795 -75.415 -13.519 1.00 30.58  ?  34  ARG A CB  1 
ATOM   268  C  CG  . ARG A 1 34  ? 55.815 -76.019 -14.518 1.00 32.01  ?  34  ARG A CG  1 
ATOM   269  C  CD  . ARG A 1 34  ? 54.755 -76.926 -13.864 1.00 30.24  ?  34  ARG A CD  1 
ATOM   270  N  NE  . ARG A 1 34  ? 53.603 -77.003 -14.764 1.00 27.80  ?  34  ARG A NE  1 
ATOM   271  C  CZ  . ARG A 1 34  ? 53.559 -77.703 -15.891 1.00 27.24  ?  34  ARG A CZ  1 
ATOM   272  N  NH1 . ARG A 1 34  ? 54.538 -78.557 -16.174 1.00 26.42  1  34  ARG A NH1 1 
ATOM   273  N  NH2 . ARG A 1 34  ? 52.523 -77.563 -16.716 1.00 23.65  ?  34  ARG A NH2 1 
ATOM   274  N  N   . LYS A 1 35  ? 59.270 -73.925 -12.285 1.00 28.24  ?  35  LYS A N   1 
ATOM   275  C  CA  . LYS A 1 35  ? 59.944 -73.411 -11.104 1.00 30.26  ?  35  LYS A CA  1 
ATOM   276  C  C   . LYS A 1 35  ? 60.264 -71.922 -11.286 1.00 33.55  ?  35  LYS A C   1 
ATOM   277  O  O   . LYS A 1 35  ? 60.366 -71.188 -10.295 1.00 33.78  ?  35  LYS A O   1 
ATOM   278  C  CB  . LYS A 1 35  ? 61.184 -74.261 -10.774 1.00 30.91  ?  35  LYS A CB  1 
ATOM   279  C  CG  . LYS A 1 35  ? 60.911 -75.643 -10.147 1.00 30.83  ?  35  LYS A CG  1 
ATOM   280  C  CD  . LYS A 1 35  ? 61.740 -76.796 -10.730 1.00 32.53  ?  35  LYS A CD  1 
ATOM   281  C  CE  . LYS A 1 35  ? 62.810 -77.389 -9.834  1.00 35.14  ?  35  LYS A CE  1 
ATOM   282  N  NZ  . LYS A 1 35  ? 63.979 -77.895 -10.580 1.00 35.21  1  35  LYS A NZ  1 
ATOM   283  N  N   . ALA A 1 36  ? 60.428 -71.478 -12.545 1.00 32.45  ?  36  ALA A N   1 
ATOM   284  C  CA  . ALA A 1 36  ? 60.780 -70.100 -12.847 1.00 30.88  ?  36  ALA A CA  1 
ATOM   285  C  C   . ALA A 1 36  ? 59.579 -69.183 -12.645 1.00 34.40  ?  36  ALA A C   1 
ATOM   286  O  O   . ALA A 1 36  ? 59.716 -68.076 -12.139 1.00 41.30  ?  36  ALA A O   1 
ATOM   287  C  CB  . ALA A 1 36  ? 61.274 -70.013 -14.262 1.00 30.79  ?  36  ALA A CB  1 
ATOM   288  N  N   . LEU A 1 37  ? 58.405 -69.645 -13.088 1.00 33.98  ?  37  LEU A N   1 
ATOM   289  C  CA  . LEU A 1 37  ? 57.146 -68.936 -12.927 1.00 29.85  ?  37  LEU A CA  1 
ATOM   290  C  C   . LEU A 1 37  ? 56.769 -68.796 -11.454 1.00 28.68  ?  37  LEU A C   1 
ATOM   291  O  O   . LEU A 1 37  ? 56.058 -67.874 -11.070 1.00 31.69  ?  37  LEU A O   1 
ATOM   292  C  CB  . LEU A 1 37  ? 56.093 -69.740 -13.686 1.00 29.07  ?  37  LEU A CB  1 
ATOM   293  C  CG  . LEU A 1 37  ? 54.743 -69.056 -13.895 1.00 27.65  ?  37  LEU A CG  1 
ATOM   294  C  CD1 . LEU A 1 37  ? 54.907 -67.651 -14.501 1.00 26.43  ?  37  LEU A CD1 1 
ATOM   295  C  CD2 . LEU A 1 37  ? 53.851 -69.938 -14.752 1.00 26.17  ?  37  LEU A CD2 1 
ATOM   296  N  N   . ALA A 1 38  ? 57.219 -69.736 -10.629 1.00 28.42  ?  38  ALA A N   1 
ATOM   297  C  CA  . ALA A 1 38  ? 57.031 -69.642 -9.193  1.00 30.68  ?  38  ALA A CA  1 
ATOM   298  C  C   . ALA A 1 38  ? 57.780 -68.425 -8.644  1.00 34.89  ?  38  ALA A C   1 
ATOM   299  O  O   . ALA A 1 38  ? 57.253 -67.715 -7.788  1.00 43.59  ?  38  ALA A O   1 
ATOM   300  C  CB  . ALA A 1 38  ? 57.473 -70.938 -8.520  1.00 27.38  ?  38  ALA A CB  1 
ATOM   301  N  N   . VAL A 1 39  ? 59.002 -68.180 -9.143  1.00 32.80  ?  39  VAL A N   1 
ATOM   302  C  CA  . VAL A 1 39  ? 59.926 -67.292 -8.463  1.00 32.65  ?  39  VAL A CA  1 
ATOM   303  C  C   . VAL A 1 39  ? 59.903 -65.930 -9.143  1.00 31.90  ?  39  VAL A C   1 
ATOM   304  O  O   . VAL A 1 39  ? 60.130 -64.937 -8.467  1.00 34.66  ?  39  VAL A O   1 
ATOM   305  C  CB  . VAL A 1 39  ? 61.372 -67.828 -8.313  1.00 35.69  ?  39  VAL A CB  1 
ATOM   306  C  CG1 . VAL A 1 39  ? 61.467 -69.345 -8.471  1.00 35.59  ?  39  VAL A CG1 1 
ATOM   307  C  CG2 . VAL A 1 39  ? 62.362 -67.127 -9.234  1.00 34.69  ?  39  VAL A CG2 1 
ATOM   308  N  N   . VAL A 1 40  ? 59.640 -65.887 -10.459 1.00 34.55  ?  40  VAL A N   1 
ATOM   309  C  CA  . VAL A 1 40  ? 59.546 -64.645 -11.226 1.00 33.27  ?  40  VAL A CA  1 
ATOM   310  C  C   . VAL A 1 40  ? 58.379 -63.816 -10.701 1.00 34.13  ?  40  VAL A C   1 
ATOM   311  O  O   . VAL A 1 40  ? 58.409 -62.583 -10.731 1.00 27.98  ?  40  VAL A O   1 
ATOM   312  C  CB  . VAL A 1 40  ? 59.358 -64.926 -12.728 1.00 32.81  ?  40  VAL A CB  1 
ATOM   313  C  CG1 . VAL A 1 40  ? 57.968 -65.434 -13.029 1.00 33.13  ?  40  VAL A CG1 1 
ATOM   314  C  CG2 . VAL A 1 40  ? 59.636 -63.711 -13.596 1.00 35.37  ?  40  VAL A CG2 1 
ATOM   315  N  N   . SER A 1 41  ? 57.371 -64.547 -10.201 1.00 39.92  ?  41  SER A N   1 
ATOM   316  C  CA  . SER A 1 41  ? 56.038 -64.033 -9.934  1.00 40.34  ?  41  SER A CA  1 
ATOM   317  C  C   . SER A 1 41  ? 55.932 -63.395 -8.552  1.00 31.33  ?  41  SER A C   1 
ATOM   318  O  O   . SER A 1 41  ? 54.877 -62.845 -8.251  1.00 29.37  ?  41  SER A O   1 
ATOM   319  C  CB  . SER A 1 41  ? 55.033 -65.136 -10.061 1.00 46.22  ?  41  SER A CB  1 
ATOM   320  O  OG  . SER A 1 41  ? 53.720 -64.607 -9.941  1.00 55.99  ?  41  SER A OG  1 
ATOM   321  N  N   . VAL A 1 42  ? 56.990 -63.519 -7.733  1.00 25.17  ?  42  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 42  ? 57.150 -62.755 -6.505  1.00 24.99  ?  42  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 42  ? 58.227 -61.693 -6.737  1.00 25.25  ?  42  VAL A C   1 
ATOM   324  O  O   . VAL A 1 42  ? 59.375 -62.042 -7.027  1.00 26.07  ?  42  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 42  ? 57.560 -63.656 -5.328  1.00 27.91  ?  42  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 42  ? 57.562 -62.899 -3.999  1.00 29.78  ?  42  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 42  ? 56.712 -64.920 -5.237  1.00 28.28  ?  42  VAL A CG2 1 
ATOM   328  N  N   . PRO A 1 43  ? 57.920 -60.376 -6.577  1.00 23.33  ?  43  PRO A N   1 
ATOM   329  C  CA  . PRO A 1 43  ? 58.901 -59.299 -6.827  1.00 19.91  ?  43  PRO A CA  1 
ATOM   330  C  C   . PRO A 1 43  ? 60.234 -59.400 -6.088  1.00 17.69  ?  43  PRO A C   1 
ATOM   331  O  O   . PRO A 1 43  ? 60.268 -59.693 -4.904  1.00 16.77  ?  43  PRO A O   1 
ATOM   332  C  CB  . PRO A 1 43  ? 58.169 -58.034 -6.353  1.00 20.75  ?  43  PRO A CB  1 
ATOM   333  C  CG  . PRO A 1 43  ? 56.682 -58.384 -6.414  1.00 22.70  ?  43  PRO A CG  1 
ATOM   334  C  CD  . PRO A 1 43  ? 56.604 -59.870 -6.142  1.00 22.90  ?  43  PRO A CD  1 
ATOM   335  N  N   . GLU A 1 44  ? 61.341 -59.079 -6.757  1.00 17.74  ?  44  GLU A N   1 
ATOM   336  C  CA  . GLU A 1 44  ? 62.641 -59.090 -6.100  1.00 17.10  ?  44  GLU A CA  1 
ATOM   337  C  C   . GLU A 1 44  ? 62.623 -58.135 -4.911  1.00 18.22  ?  44  GLU A C   1 
ATOM   338  O  O   . GLU A 1 44  ? 63.060 -58.449 -3.806  1.00 19.54  ?  44  GLU A O   1 
ATOM   339  C  CB  . GLU A 1 44  ? 63.714 -58.655 -7.084  1.00 16.18  ?  44  GLU A CB  1 
ATOM   340  C  CG  . GLU A 1 44  ? 64.119 -59.756 -8.056  1.00 15.11  ?  44  GLU A CG  1 
ATOM   341  C  CD  . GLU A 1 44  ? 65.190 -59.282 -9.022  1.00 14.05  ?  44  GLU A CD  1 
ATOM   342  O  OE1 . GLU A 1 44  ? 65.451 -60.113 -9.914  1.00 15.46  ?  44  GLU A OE1 1 
ATOM   343  O  OE2 . GLU A 1 44  ? 65.748 -58.162 -8.897  1.00 11.55  -1 44  GLU A OE2 1 
ATOM   344  N  N   . ARG A 1 45  ? 62.072 -56.954 -5.141  1.00 19.14  ?  45  ARG A N   1 
ATOM   345  C  CA  . ARG A 1 45  ? 61.933 -55.982 -4.080  1.00 20.82  ?  45  ARG A CA  1 
ATOM   346  C  C   . ARG A 1 45  ? 60.730 -55.128 -4.429  1.00 21.11  ?  45  ARG A C   1 
ATOM   347  O  O   . ARG A 1 45  ? 60.497 -54.897 -5.615  1.00 21.00  ?  45  ARG A O   1 
ATOM   348  C  CB  . ARG A 1 45  ? 63.214 -55.147 -4.005  1.00 22.96  ?  45  ARG A CB  1 
ATOM   349  C  CG  . ARG A 1 45  ? 63.416 -54.203 -2.829  1.00 23.35  ?  45  ARG A CG  1 
ATOM   350  C  CD  . ARG A 1 45  ? 64.910 -53.850 -2.765  1.00 24.84  ?  45  ARG A CD  1 
ATOM   351  N  NE  . ARG A 1 45  ? 65.538 -53.828 -4.095  1.00 26.71  ?  45  ARG A NE  1 
ATOM   352  C  CZ  . ARG A 1 45  ? 66.497 -54.646 -4.566  1.00 29.58  ?  45  ARG A CZ  1 
ATOM   353  N  NH1 . ARG A 1 45  ? 67.003 -55.625 -3.836  1.00 29.84  1  45  ARG A NH1 1 
ATOM   354  N  NH2 . ARG A 1 45  ? 66.972 -54.476 -5.790  1.00 29.65  ?  45  ARG A NH2 1 
ATOM   355  N  N   . VAL A 1 46  ? 59.979 -54.758 -3.381  1.00 20.42  ?  46  VAL A N   1 
ATOM   356  C  CA  . VAL A 1 46  ? 58.934 -53.747 -3.410  1.00 20.65  ?  46  VAL A CA  1 
ATOM   357  C  C   . VAL A 1 46  ? 59.250 -52.711 -2.318  1.00 22.02  ?  46  VAL A C   1 
ATOM   358  O  O   . VAL A 1 46  ? 59.561 -53.063 -1.180  1.00 20.61  ?  46  VAL A O   1 
ATOM   359  C  CB  . VAL A 1 46  ? 57.555 -54.406 -3.176  1.00 19.09  ?  46  VAL A CB  1 
ATOM   360  C  CG1 . VAL A 1 46  ? 56.430 -53.385 -3.047  1.00 18.96  ?  46  VAL A CG1 1 
ATOM   361  C  CG2 . VAL A 1 46  ? 57.214 -55.432 -4.240  1.00 17.71  ?  46  VAL A CG2 1 
ATOM   362  N  N   . ILE A 1 47  ? 59.188 -51.420 -2.662  1.00 22.17  ?  47  ILE A N   1 
ATOM   363  C  CA  . ILE A 1 47  ? 59.209 -50.382 -1.642  1.00 22.68  ?  47  ILE A CA  1 
ATOM   364  C  C   . ILE A 1 47  ? 57.869 -49.638 -1.705  1.00 21.98  ?  47  ILE A C   1 
ATOM   365  O  O   . ILE A 1 47  ? 57.407 -49.339 -2.806  1.00 19.53  ?  47  ILE A O   1 
ATOM   366  C  CB  . ILE A 1 47  ? 60.421 -49.435 -1.794  1.00 22.24  ?  47  ILE A CB  1 
ATOM   367  C  CG1 . ILE A 1 47  ? 61.743 -50.186 -2.015  1.00 20.34  ?  47  ILE A CG1 1 
ATOM   368  C  CG2 . ILE A 1 47  ? 60.513 -48.472 -0.607  1.00 23.45  ?  47  ILE A CG2 1 
ATOM   369  C  CD1 . ILE A 1 47  ? 62.124 -50.324 -3.479  1.00 20.52  ?  47  ILE A CD1 1 
ATOM   370  N  N   . GLN A 1 48  ? 57.256 -49.425 -0.518  1.00 20.14  ?  48  GLN A N   1 
ATOM   371  C  CA  . GLN A 1 48  ? 56.199 -48.461 -0.270  1.00 19.48  ?  48  GLN A CA  1 
ATOM   372  C  C   . GLN A 1 48  ? 56.597 -47.501 0.865   1.00 20.57  ?  48  GLN A C   1 
ATOM   373  O  O   . GLN A 1 48  ? 57.070 -47.920 1.914   1.00 23.10  ?  48  GLN A O   1 
ATOM   374  C  CB  . GLN A 1 48  ? 54.940 -49.177 0.200   1.00 20.00  ?  48  GLN A CB  1 
ATOM   375  C  CG  . GLN A 1 48  ? 54.828 -50.637 -0.219  1.00 20.30  ?  48  GLN A CG  1 
ATOM   376  C  CD  . GLN A 1 48  ? 53.439 -51.192 0.019   1.00 20.27  ?  48  GLN A CD  1 
ATOM   377  O  OE1 . GLN A 1 48  ? 53.074 -52.274 -0.459  1.00 20.54  ?  48  GLN A OE1 1 
ATOM   378  N  NE2 . GLN A 1 48  ? 52.633 -50.428 0.740   1.00 20.35  ?  48  GLN A NE2 1 
ATOM   379  N  N   . PHE A 1 49  ? 56.327 -46.198 0.698   1.00 20.39  ?  49  PHE A N   1 
ATOM   380  C  CA  . PHE A 1 49  ? 56.803 -45.176 1.617   1.00 18.71  ?  49  PHE A CA  1 
ATOM   381  C  C   . PHE A 1 49  ? 55.781 -44.047 1.752   1.00 18.71  ?  49  PHE A C   1 
ATOM   382  O  O   . PHE A 1 49  ? 55.132 -43.675 0.780   1.00 19.49  ?  49  PHE A O   1 
ATOM   383  C  CB  . PHE A 1 49  ? 58.145 -44.670 1.084   1.00 18.51  ?  49  PHE A CB  1 
ATOM   384  C  CG  . PHE A 1 49  ? 58.167 -44.211 -0.367  1.00 18.18  ?  49  PHE A CG  1 
ATOM   385  C  CD1 . PHE A 1 49  ? 57.835 -42.906 -0.708  1.00 18.95  ?  49  PHE A CD1 1 
ATOM   386  C  CD2 . PHE A 1 49  ? 58.598 -45.062 -1.377  1.00 19.44  ?  49  PHE A CD2 1 
ATOM   387  C  CE1 . PHE A 1 49  ? 57.909 -42.469 -2.022  1.00 20.25  ?  49  PHE A CE1 1 
ATOM   388  C  CE2 . PHE A 1 49  ? 58.662 -44.630 -2.701  1.00 20.82  ?  49  PHE A CE2 1 
ATOM   389  C  CZ  . PHE A 1 49  ? 58.322 -43.336 -3.022  1.00 21.23  ?  49  PHE A CZ  1 
ATOM   390  N  N   . ARG A 1 50  ? 55.659 -43.498 2.968   1.00 18.37  ?  50  ARG A N   1 
ATOM   391  C  CA  . ARG A 1 50  ? 54.732 -42.419 3.256   1.00 18.54  ?  50  ARG A CA  1 
ATOM   392  C  C   . ARG A 1 50  ? 55.189 -41.173 2.511   1.00 19.63  ?  50  ARG A C   1 
ATOM   393  O  O   . ARG A 1 50  ? 56.395 -40.954 2.383   1.00 18.58  ?  50  ARG A O   1 
ATOM   394  C  CB  . ARG A 1 50  ? 54.709 -42.144 4.764   1.00 19.51  ?  50  ARG A CB  1 
ATOM   395  C  CG  . ARG A 1 50  ? 53.795 -40.993 5.176   1.00 20.55  ?  50  ARG A CG  1 
ATOM   396  C  CD  . ARG A 1 50  ? 53.565 -40.932 6.681   1.00 19.54  ?  50  ARG A CD  1 
ATOM   397  N  NE  . ARG A 1 50  ? 54.755 -40.445 7.386   1.00 19.32  ?  50  ARG A NE  1 
ATOM   398  C  CZ  . ARG A 1 50  ? 55.183 -40.861 8.580   1.00 18.99  ?  50  ARG A CZ  1 
ATOM   399  N  NH1 . ARG A 1 50  ? 54.493 -41.755 9.277   1.00 17.98  1  50  ARG A NH1 1 
ATOM   400  N  NH2 . ARG A 1 50  ? 56.302 -40.356 9.090   1.00 18.70  ?  50  ARG A NH2 1 
ATOM   401  N  N   . VAL A 1 51  ? 54.236 -40.353 2.034   1.00 22.25  ?  51  VAL A N   1 
ATOM   402  C  CA  . VAL A 1 51  ? 54.601 -39.176 1.252   1.00 25.25  ?  51  VAL A CA  1 
ATOM   403  C  C   . VAL A 1 51  ? 53.910 -37.957 1.830   1.00 24.70  ?  51  VAL A C   1 
ATOM   404  O  O   . VAL A 1 51  ? 52.734 -37.721 1.552   1.00 28.85  ?  51  VAL A O   1 
ATOM   405  C  CB  . VAL A 1 51  ? 54.304 -39.270 -0.252  1.00 28.96  ?  51  VAL A CB  1 
ATOM   406  C  CG1 . VAL A 1 51  ? 55.030 -38.160 -1.017  1.00 29.63  ?  51  VAL A CG1 1 
ATOM   407  C  CG2 . VAL A 1 51  ? 54.651 -40.660 -0.798  1.00 31.00  ?  51  VAL A CG2 1 
ATOM   408  N  N   . VAL A 1 52  ? 54.658 -37.199 2.635   1.00 23.31  ?  52  VAL A N   1 
ATOM   409  C  CA  . VAL A 1 52  ? 54.141 -35.959 3.185   1.00 23.34  ?  52  VAL A CA  1 
ATOM   410  C  C   . VAL A 1 52  ? 54.614 -34.794 2.313   1.00 23.19  ?  52  VAL A C   1 
ATOM   411  O  O   . VAL A 1 52  ? 55.809 -34.572 2.113   1.00 20.10  ?  52  VAL A O   1 
ATOM   412  C  CB  . VAL A 1 52  ? 54.503 -35.734 4.664   1.00 23.43  ?  52  VAL A CB  1 
ATOM   413  C  CG1 . VAL A 1 52  ? 54.251 -34.276 5.082   1.00 21.88  ?  52  VAL A CG1 1 
ATOM   414  C  CG2 . VAL A 1 52  ? 53.793 -36.752 5.568   1.00 22.84  ?  52  VAL A CG2 1 
ATOM   415  N  N   . TRP A 1 53  ? 53.622 -34.045 1.814   1.00 24.71  ?  53  TRP A N   1 
ATOM   416  C  CA  . TRP A 1 53  ? 53.830 -32.821 1.061   1.00 25.06  ?  53  TRP A CA  1 
ATOM   417  C  C   . TRP A 1 53  ? 52.834 -31.748 1.527   1.00 26.33  ?  53  TRP A C   1 
ATOM   418  O  O   . TRP A 1 53  ? 51.830 -32.066 2.168   1.00 25.71  ?  53  TRP A O   1 
ATOM   419  C  CB  . TRP A 1 53  ? 53.684 -33.170 -0.423  1.00 23.14  ?  53  TRP A CB  1 
ATOM   420  C  CG  . TRP A 1 53  ? 52.299 -33.626 -0.764  1.00 22.39  ?  53  TRP A CG  1 
ATOM   421  C  CD1 . TRP A 1 53  ? 51.708 -34.839 -0.542  1.00 22.38  ?  53  TRP A CD1 1 
ATOM   422  C  CD2 . TRP A 1 53  ? 51.308 -32.799 -1.393  1.00 20.63  ?  53  TRP A CD2 1 
ATOM   423  N  NE1 . TRP A 1 53  ? 50.423 -34.837 -1.021  1.00 21.82  ?  53  TRP A NE1 1 
ATOM   424  C  CE2 . TRP A 1 53  ? 50.153 -33.596 -1.546  1.00 21.06  ?  53  TRP A CE2 1 
ATOM   425  C  CE3 . TRP A 1 53  ? 51.307 -31.478 -1.839  1.00 19.21  ?  53  TRP A CE3 1 
ATOM   426  C  CZ2 . TRP A 1 53  ? 48.997 -33.098 -2.136  1.00 20.86  ?  53  TRP A CZ2 1 
ATOM   427  C  CZ3 . TRP A 1 53  ? 50.171 -30.992 -2.432  1.00 20.08  ?  53  TRP A CZ3 1 
ATOM   428  C  CH2 . TRP A 1 53  ? 49.036 -31.797 -2.582  1.00 21.48  ?  53  TRP A CH2 1 
ATOM   429  N  N   . GLU A 1 54  ? 53.119 -30.482 1.188   1.00 29.86  ?  54  GLU A N   1 
ATOM   430  C  CA  . GLU A 1 54  ? 52.332 -29.322 1.604   1.00 31.81  ?  54  GLU A CA  1 
ATOM   431  C  C   . GLU A 1 54  ? 51.562 -28.715 0.421   1.00 34.47  ?  54  GLU A C   1 
ATOM   432  O  O   . GLU A 1 54  ? 52.128 -28.526 -0.657  1.00 40.30  ?  54  GLU A O   1 
ATOM   433  C  CB  . GLU A 1 54  ? 53.332 -28.291 2.130   1.00 29.96  ?  54  GLU A CB  1 
ATOM   434  C  CG  . GLU A 1 54  ? 52.684 -27.116 2.852   1.00 32.26  ?  54  GLU A CG  1 
ATOM   435  C  CD  . GLU A 1 54  ? 53.674 -26.162 3.502   1.00 33.43  ?  54  GLU A CD  1 
ATOM   436  O  OE1 . GLU A 1 54  ? 54.900 -26.488 3.494   1.00 33.29  ?  54  GLU A OE1 1 
ATOM   437  O  OE2 . GLU A 1 54  ? 53.219 -25.094 3.996   1.00 25.92  -1 54  GLU A OE2 1 
ATOM   438  N  N   . ASN A 1 55  ? 50.293 -28.339 0.630   1.00 31.04  ?  55  ASN A N   1 
ATOM   439  C  CA  . ASN A 1 55  ? 49.498 -27.705 -0.419  1.00 31.63  ?  55  ASN A CA  1 
ATOM   440  C  C   . ASN A 1 55  ? 49.619 -26.179 -0.355  1.00 33.54  ?  55  ASN A C   1 
ATOM   441  O  O   . ASN A 1 55  ? 50.254 -25.634 0.538   1.00 38.02  ?  55  ASN A O   1 
ATOM   442  C  CB  . ASN A 1 55  ? 48.036 -28.106 -0.304  1.00 31.22  ?  55  ASN A CB  1 
ATOM   443  C  CG  . ASN A 1 55  ? 47.399 -27.487 0.914   1.00 28.54  ?  55  ASN A CG  1 
ATOM   444  O  OD1 . ASN A 1 55  ? 47.828 -26.404 1.338   1.00 24.40  ?  55  ASN A OD1 1 
ATOM   445  N  ND2 . ASN A 1 55  ? 46.396 -28.158 1.470   1.00 26.21  ?  55  ASN A ND2 1 
ATOM   446  N  N   . ASP A 1 56  ? 48.961 -25.481 -1.288  1.00 33.81  ?  56  ASP A N   1 
ATOM   447  C  CA  . ASP A 1 56  ? 49.086 -24.031 -1.417  1.00 33.24  ?  56  ASP A CA  1 
ATOM   448  C  C   . ASP A 1 56  ? 48.462 -23.292 -0.212  1.00 31.82  ?  56  ASP A C   1 
ATOM   449  O  O   . ASP A 1 56  ? 48.774 -22.131 0.020   1.00 30.50  ?  56  ASP A O   1 
ATOM   450  C  CB  . ASP A 1 56  ? 48.633 -23.597 -2.814  1.00 32.67  ?  56  ASP A CB  1 
ATOM   451  C  CG  . ASP A 1 56  ? 49.517 -24.043 -3.985  1.00 34.15  ?  56  ASP A CG  1 
ATOM   452  O  OD1 . ASP A 1 56  ? 48.986 -24.406 -5.039  1.00 34.08  ?  56  ASP A OD1 1 
ATOM   453  O  OD2 . ASP A 1 56  ? 50.753 -24.004 -3.872  1.00 35.70  -1 56  ASP A OD2 1 
ATOM   454  N  N   . LYS A 1 57  ? 47.592 -23.949 0.572   1.00 30.96  ?  57  LYS A N   1 
ATOM   455  C  CA  . LYS A 1 57  ? 47.044 -23.398 1.809   1.00 28.90  ?  57  LYS A CA  1 
ATOM   456  C  C   . LYS A 1 57  ? 47.990 -23.673 2.981   1.00 27.64  ?  57  LYS A C   1 
ATOM   457  O  O   . LYS A 1 57  ? 47.801 -23.180 4.086   1.00 25.10  ?  57  LYS A O   1 
ATOM   458  C  CB  . LYS A 1 57  ? 45.644 -23.973 2.077   1.00 30.56  ?  57  LYS A CB  1 
ATOM   459  C  CG  . LYS A 1 57  ? 44.585 -23.547 1.032   1.00 33.51  ?  57  LYS A CG  1 
ATOM   460  C  CD  . LYS A 1 57  ? 43.508 -24.559 0.644   1.00 33.27  ?  57  LYS A CD  1 
ATOM   461  C  CE  . LYS A 1 57  ? 42.266 -24.456 1.477   1.00 37.24  ?  57  LYS A CE  1 
ATOM   462  N  NZ  . LYS A 1 57  ? 41.542 -25.730 1.609   1.00 38.13  1  57  LYS A NZ  1 
ATOM   463  N  N   . GLY A 1 58  ? 49.030 -24.467 2.744   1.00 30.34  ?  58  GLY A N   1 
ATOM   464  C  CA  . GLY A 1 58  ? 50.053 -24.722 3.748   1.00 31.75  ?  58  GLY A CA  1 
ATOM   465  C  C   . GLY A 1 58  ? 49.710 -25.893 4.675   1.00 33.09  ?  58  GLY A C   1 
ATOM   466  O  O   . GLY A 1 58  ? 50.185 -25.928 5.811   1.00 33.89  ?  58  GLY A O   1 
ATOM   467  N  N   . GLU A 1 59  ? 48.887 -26.838 4.196   1.00 32.73  ?  59  GLU A N   1 
ATOM   468  C  CA  . GLU A 1 59  ? 48.392 -27.940 5.014   1.00 34.57  ?  59  GLU A CA  1 
ATOM   469  C  C   . GLU A 1 59  ? 49.158 -29.232 4.680   1.00 35.90  ?  59  GLU A C   1 
ATOM   470  O  O   . GLU A 1 59  ? 49.330 -29.583 3.508   1.00 37.69  ?  59  GLU A O   1 
ATOM   471  C  CB  . GLU A 1 59  ? 46.894 -28.211 4.809   1.00 33.64  ?  59  GLU A CB  1 
ATOM   472  C  CG  . GLU A 1 59  ? 45.946 -27.055 5.117   1.00 36.71  ?  59  GLU A CG  1 
ATOM   473  C  CD  . GLU A 1 59  ? 44.566 -27.109 4.444   1.00 40.08  ?  59  GLU A CD  1 
ATOM   474  O  OE1 . GLU A 1 59  ? 44.191 -28.145 3.863   1.00 32.48  ?  59  GLU A OE1 1 
ATOM   475  O  OE2 . GLU A 1 59  ? 43.848 -26.075 4.469   1.00 49.15  -1 59  GLU A OE2 1 
ATOM   476  N  N   . VAL A 1 60  ? 49.599 -29.950 5.731   1.00 32.53  ?  60  VAL A N   1 
ATOM   477  C  CA  . VAL A 1 60  ? 50.000 -31.353 5.657   1.00 29.12  ?  60  VAL A CA  1 
ATOM   478  C  C   . VAL A 1 60  ? 49.060 -32.164 4.778   1.00 31.74  ?  60  VAL A C   1 
ATOM   479  O  O   . VAL A 1 60  ? 47.861 -32.231 5.084   1.00 30.91  ?  60  VAL A O   1 
ATOM   480  C  CB  . VAL A 1 60  ? 50.025 -32.062 7.020   1.00 25.89  ?  60  VAL A CB  1 
ATOM   481  C  CG1 . VAL A 1 60  ? 51.435 -32.412 7.454   1.00 26.41  ?  60  VAL A CG1 1 
ATOM   482  C  CG2 . VAL A 1 60  ? 49.272 -31.286 8.084   1.00 25.67  ?  60  VAL A CG2 1 
ATOM   483  N  N   . GLN A 1 61  ? 49.654 -32.850 3.777   1.00 30.83  ?  61  GLN A N   1 
ATOM   484  C  CA  . GLN A 1 61  ? 48.966 -33.842 2.962   1.00 31.26  ?  61  GLN A CA  1 
ATOM   485  C  C   . GLN A 1 61  ? 49.751 -35.149 3.070   1.00 28.76  ?  61  GLN A C   1 
ATOM   486  O  O   . GLN A 1 61  ? 50.953 -35.126 3.308   1.00 28.11  ?  61  GLN A O   1 
ATOM   487  C  CB  . GLN A 1 61  ? 48.825 -33.416 1.492   1.00 34.40  ?  61  GLN A CB  1 
ATOM   488  C  CG  . GLN A 1 61  ? 48.237 -32.025 1.219   1.00 35.75  ?  61  GLN A CG  1 
ATOM   489  C  CD  . GLN A 1 61  ? 46.804 -31.818 1.665   1.00 39.70  ?  61  GLN A CD  1 
ATOM   490  O  OE1 . GLN A 1 61  ? 46.458 -30.748 2.177   1.00 39.56  ?  61  GLN A OE1 1 
ATOM   491  N  NE2 . GLN A 1 61  ? 45.944 -32.809 1.459   1.00 42.66  ?  61  GLN A NE2 1 
ATOM   492  N  N   . VAL A 1 62  ? 49.057 -36.278 2.869   1.00 26.13  ?  62  VAL A N   1 
ATOM   493  C  CA  . VAL A 1 62  ? 49.599 -37.622 3.043   1.00 24.36  ?  62  VAL A CA  1 
ATOM   494  C  C   . VAL A 1 62  ? 49.066 -38.533 1.930   1.00 25.48  ?  62  VAL A C   1 
ATOM   495  O  O   . VAL A 1 62  ? 47.854 -38.775 1.801   1.00 23.40  ?  62  VAL A O   1 
ATOM   496  C  CB  . VAL A 1 62  ? 49.224 -38.204 4.429   1.00 23.27  ?  62  VAL A CB  1 
ATOM   497  C  CG1 . VAL A 1 62  ? 49.934 -39.523 4.746   1.00 22.01  ?  62  VAL A CG1 1 
ATOM   498  C  CG2 . VAL A 1 62  ? 49.466 -37.204 5.552   1.00 22.75  ?  62  VAL A CG2 1 
ATOM   499  N  N   . ASN A 1 63  ? 49.996 -39.071 1.139   1.00 25.33  ?  63  ASN A N   1 
ATOM   500  C  CA  . ASN A 1 63  ? 49.693 -40.104 0.160   1.00 24.59  ?  63  ASN A CA  1 
ATOM   501  C  C   . ASN A 1 63  ? 50.680 -41.268 0.311   1.00 26.50  ?  63  ASN A C   1 
ATOM   502  O  O   . ASN A 1 63  ? 51.634 -41.187 1.071   1.00 28.68  ?  63  ASN A O   1 
ATOM   503  C  CB  . ASN A 1 63  ? 49.776 -39.500 -1.230  1.00 23.38  ?  63  ASN A CB  1 
ATOM   504  C  CG  . ASN A 1 63  ? 48.600 -38.626 -1.565  1.00 21.01  ?  63  ASN A CG  1 
ATOM   505  O  OD1 . ASN A 1 63  ? 48.651 -37.403 -1.354  1.00 19.37  ?  63  ASN A OD1 1 
ATOM   506  N  ND2 . ASN A 1 63  ? 47.579 -39.244 -2.140  1.00 20.01  ?  63  ASN A ND2 1 
ATOM   507  N  N   . ARG A 1 64  ? 50.480 -42.338 -0.451  1.00 28.66  ?  64  ARG A N   1 
ATOM   508  C  CA  . ARG A 1 64  ? 51.398 -43.461 -0.439  1.00 32.22  ?  64  ARG A CA  1 
ATOM   509  C  C   . ARG A 1 64  ? 52.176 -43.498 -1.755  1.00 28.71  ?  64  ARG A C   1 
ATOM   510  O  O   . ARG A 1 64  ? 51.582 -43.463 -2.829  1.00 25.59  ?  64  ARG A O   1 
ATOM   511  C  CB  . ARG A 1 64  ? 50.581 -44.733 -0.150  1.00 34.94  ?  64  ARG A CB  1 
ATOM   512  C  CG  . ARG A 1 64  ? 50.030 -44.686 1.268   1.00 38.13  ?  64  ARG A CG  1 
ATOM   513  C  CD  . ARG A 1 64  ? 48.868 -45.608 1.645   1.00 38.90  ?  64  ARG A CD  1 
ATOM   514  N  NE  . ARG A 1 64  ? 48.292 -45.010 2.858   1.00 41.62  ?  64  ARG A NE  1 
ATOM   515  C  CZ  . ARG A 1 64  ? 47.125 -45.284 3.420   1.00 44.17  ?  64  ARG A CZ  1 
ATOM   516  N  NH1 . ARG A 1 64  ? 46.429 -46.334 3.007   1.00 48.74  1  64  ARG A NH1 1 
ATOM   517  N  NH2 . ARG A 1 64  ? 46.681 -44.514 4.408   1.00 38.06  ?  64  ARG A NH2 1 
ATOM   518  N  N   . GLY A 1 65  ? 53.502 -43.623 -1.645  1.00 27.05  ?  65  GLY A N   1 
ATOM   519  C  CA  . GLY A 1 65  ? 54.380 -43.911 -2.772  1.00 25.67  ?  65  GLY A CA  1 
ATOM   520  C  C   . GLY A 1 65  ? 54.762 -45.393 -2.811  1.00 23.73  ?  65  GLY A C   1 
ATOM   521  O  O   . GLY A 1 65  ? 54.841 -46.050 -1.784  1.00 22.22  ?  65  GLY A O   1 
ATOM   522  N  N   . PHE A 1 66  ? 54.999 -45.909 -4.018  1.00 22.87  ?  66  PHE A N   1 
ATOM   523  C  CA  . PHE A 1 66  ? 55.283 -47.317 -4.245  1.00 22.23  ?  66  PHE A CA  1 
ATOM   524  C  C   . PHE A 1 66  ? 56.341 -47.390 -5.349  1.00 21.83  ?  66  PHE A C   1 
ATOM   525  O  O   . PHE A 1 66  ? 56.315 -46.554 -6.244  1.00 22.93  ?  66  PHE A O   1 
ATOM   526  C  CB  . PHE A 1 66  ? 54.059 -48.114 -4.721  1.00 21.54  ?  66  PHE A CB  1 
ATOM   527  C  CG  . PHE A 1 66  ? 52.724 -47.942 -4.000  1.00 22.73  ?  66  PHE A CG  1 
ATOM   528  C  CD1 . PHE A 1 66  ? 51.970 -46.773 -4.149  1.00 22.91  ?  66  PHE A CD1 1 
ATOM   529  C  CD2 . PHE A 1 66  ? 52.181 -48.982 -3.231  1.00 22.40  ?  66  PHE A CD2 1 
ATOM   530  C  CE1 . PHE A 1 66  ? 50.739 -46.640 -3.519  1.00 22.14  ?  66  PHE A CE1 1 
ATOM   531  C  CE2 . PHE A 1 66  ? 50.955 -48.843 -2.603  1.00 20.90  ?  66  PHE A CE2 1 
ATOM   532  C  CZ  . PHE A 1 66  ? 50.236 -47.677 -2.755  1.00 22.36  ?  66  PHE A CZ  1 
ATOM   533  N  N   . ARG A 1 67  ? 57.280 -48.345 -5.247  1.00 21.31  ?  67  ARG A N   1 
ATOM   534  C  CA  . ARG A 1 67  ? 58.174 -48.729 -6.336  1.00 22.24  ?  67  ARG A CA  1 
ATOM   535  C  C   . ARG A 1 67  ? 58.347 -50.261 -6.319  1.00 23.94  ?  67  ARG A C   1 
ATOM   536  O  O   . ARG A 1 67  ? 59.026 -50.825 -5.446  1.00 23.47  ?  67  ARG A O   1 
ATOM   537  C  CB  . ARG A 1 67  ? 59.521 -47.979 -6.290  1.00 20.35  ?  67  ARG A CB  1 
ATOM   538  C  CG  . ARG A 1 67  ? 60.336 -48.111 -7.577  1.00 19.47  ?  67  ARG A CG  1 
ATOM   539  C  CD  . ARG A 1 67  ? 59.667 -47.598 -8.868  1.00 17.33  ?  67  ARG A CD  1 
ATOM   540  N  NE  . ARG A 1 67  ? 60.428 -48.053 -10.041 1.00 16.36  ?  67  ARG A NE  1 
ATOM   541  C  CZ  . ARG A 1 67  ? 60.050 -47.960 -11.320 1.00 14.62  ?  67  ARG A CZ  1 
ATOM   542  N  NH1 . ARG A 1 67  ? 58.919 -47.371 -11.634 1.00 15.05  1  67  ARG A NH1 1 
ATOM   543  N  NH2 . ARG A 1 67  ? 60.805 -48.444 -12.284 1.00 13.30  ?  67  ARG A NH2 1 
ATOM   544  N  N   . VAL A 1 68  ? 57.664 -50.941 -7.256  1.00 22.42  ?  68  VAL A N   1 
ATOM   545  C  CA  . VAL A 1 68  ? 57.784 -52.378 -7.411  1.00 20.99  ?  68  VAL A CA  1 
ATOM   546  C  C   . VAL A 1 68  ? 58.979 -52.617 -8.306  1.00 20.93  ?  68  VAL A C   1 
ATOM   547  O  O   . VAL A 1 68  ? 58.973 -52.135 -9.435  1.00 26.10  ?  68  VAL A O   1 
ATOM   548  C  CB  . VAL A 1 68  ? 56.559 -53.050 -8.039  1.00 22.02  ?  68  VAL A CB  1 
ATOM   549  C  CG1 . VAL A 1 68  ? 56.773 -54.555 -8.156  1.00 22.25  ?  68  VAL A CG1 1 
ATOM   550  C  CG2 . VAL A 1 68  ? 55.272 -52.729 -7.278  1.00 23.53  ?  68  VAL A CG2 1 
ATOM   551  N  N   . GLN A 1 69  ? 59.975 -53.338 -7.782  1.00 18.92  ?  69  GLN A N   1 
ATOM   552  C  CA  . GLN A 1 69  ? 61.172 -53.689 -8.519  1.00 19.22  ?  69  GLN A CA  1 
ATOM   553  C  C   . GLN A 1 69  ? 61.152 -55.192 -8.797  1.00 20.65  ?  69  GLN A C   1 
ATOM   554  O  O   . GLN A 1 69  ? 61.653 -56.001 -8.001  1.00 20.55  ?  69  GLN A O   1 
ATOM   555  C  CB  . GLN A 1 69  ? 62.374 -53.231 -7.699  1.00 18.92  ?  69  GLN A CB  1 
ATOM   556  C  CG  . GLN A 1 69  ? 62.373 -51.747 -7.352  1.00 17.98  ?  69  GLN A CG  1 
ATOM   557  C  CD  . GLN A 1 69  ? 63.726 -51.277 -6.887  1.00 16.37  ?  69  GLN A CD  1 
ATOM   558  O  OE1 . GLN A 1 69  ? 64.459 -52.066 -6.279  1.00 17.81  ?  69  GLN A OE1 1 
ATOM   559  N  NE2 . GLN A 1 69  ? 64.078 -50.031 -7.195  1.00 14.81  ?  69  GLN A NE2 1 
ATOM   560  N  N   . PHE A 1 70  ? 60.590 -55.549 -9.958  1.00 19.99  ?  70  PHE A N   1 
ATOM   561  C  CA  . PHE A 1 70  ? 60.039 -56.877 -10.146 1.00 21.41  ?  70  PHE A CA  1 
ATOM   562  C  C   . PHE A 1 70  ? 61.120 -57.840 -10.620 1.00 22.31  ?  70  PHE A C   1 
ATOM   563  O  O   . PHE A 1 70  ? 61.273 -58.908 -10.035 1.00 21.10  ?  70  PHE A O   1 
ATOM   564  C  CB  . PHE A 1 70  ? 58.842 -56.835 -11.103 1.00 22.82  ?  70  PHE A CB  1 
ATOM   565  C  CG  . PHE A 1 70  ? 57.677 -57.737 -10.702 1.00 23.08  ?  70  PHE A CG  1 
ATOM   566  C  CD1 . PHE A 1 70  ? 56.403 -57.216 -10.530 1.00 22.69  ?  70  PHE A CD1 1 
ATOM   567  C  CD2 . PHE A 1 70  ? 57.857 -59.095 -10.487 1.00 24.42  ?  70  PHE A CD2 1 
ATOM   568  C  CE1 . PHE A 1 70  ? 55.344 -58.030 -10.178 1.00 24.31  ?  70  PHE A CE1 1 
ATOM   569  C  CE2 . PHE A 1 70  ? 56.790 -59.904 -10.137 1.00 25.41  ?  70  PHE A CE2 1 
ATOM   570  C  CZ  . PHE A 1 70  ? 55.536 -59.370 -9.981  1.00 24.59  ?  70  PHE A CZ  1 
ATOM   571  N  N   . ASN A 1 71  ? 61.839 -57.478 -11.690 1.00 24.48  ?  71  ASN A N   1 
ATOM   572  C  CA  . ASN A 1 71  ? 62.870 -58.347 -12.245 1.00 27.29  ?  71  ASN A CA  1 
ATOM   573  C  C   . ASN A 1 71  ? 64.045 -57.507 -12.730 1.00 29.93  ?  71  ASN A C   1 
ATOM   574  O  O   . ASN A 1 71  ? 63.810 -56.469 -13.364 1.00 33.21  ?  71  ASN A O   1 
ATOM   575  C  CB  . ASN A 1 71  ? 62.377 -59.141 -13.450 1.00 27.38  ?  71  ASN A CB  1 
ATOM   576  C  CG  . ASN A 1 71  ? 63.127 -60.438 -13.617 1.00 27.45  ?  71  ASN A CG  1 
ATOM   577  O  OD1 . ASN A 1 71  ? 64.029 -60.525 -14.456 1.00 28.32  ?  71  ASN A OD1 1 
ATOM   578  N  ND2 . ASN A 1 71  ? 62.790 -61.439 -12.815 1.00 26.95  ?  71  ASN A ND2 1 
ATOM   579  N  N   . SER A 1 72  ? 65.273 -58.008 -12.482 1.00 26.67  ?  72  SER A N   1 
ATOM   580  C  CA  . SER A 1 72  ? 66.501 -57.373 -12.952 1.00 24.60  ?  72  SER A CA  1 
ATOM   581  C  C   . SER A 1 72  ? 67.452 -58.361 -13.665 1.00 22.74  ?  72  SER A C   1 
ATOM   582  O  O   . SER A 1 72  ? 68.637 -58.064 -13.861 1.00 21.85  ?  72  SER A O   1 
ATOM   583  C  CB  . SER A 1 72  ? 67.179 -56.651 -11.798 1.00 23.78  ?  72  SER A CB  1 
ATOM   584  O  OG  . SER A 1 72  ? 67.631 -57.544 -10.786 1.00 23.20  ?  72  SER A OG  1 
ATOM   585  N  N   . ALA A 1 73  ? 66.929 -59.516 -14.097 1.00 19.93  ?  73  ALA A N   1 
ATOM   586  C  CA  . ALA A 1 73  ? 67.716 -60.556 -14.755 1.00 19.72  ?  73  ALA A CA  1 
ATOM   587  C  C   . ALA A 1 73  ? 68.388 -60.077 -16.048 1.00 20.21  ?  73  ALA A C   1 
ATOM   588  O  O   . ALA A 1 73  ? 69.550 -60.429 -16.292 1.00 18.89  ?  73  ALA A O   1 
ATOM   589  C  CB  . ALA A 1 73  ? 66.830 -61.754 -15.049 1.00 19.08  ?  73  ALA A CB  1 
ATOM   590  N  N   . LEU A 1 74  ? 67.643 -59.324 -16.885 1.00 19.84  ?  74  LEU A N   1 
ATOM   591  C  CA  . LEU A 1 74  ? 68.112 -58.864 -18.192 1.00 20.77  ?  74  LEU A CA  1 
ATOM   592  C  C   . LEU A 1 74  ? 68.577 -57.400 -18.166 1.00 19.61  ?  74  LEU A C   1 
ATOM   593  O  O   . LEU A 1 74  ? 69.012 -56.887 -19.192 1.00 17.67  ?  74  LEU A O   1 
ATOM   594  C  CB  . LEU A 1 74  ? 67.006 -58.996 -19.243 1.00 22.57  ?  74  LEU A CB  1 
ATOM   595  C  CG  . LEU A 1 74  ? 66.353 -60.367 -19.409 1.00 24.33  ?  74  LEU A CG  1 
ATOM   596  C  CD1 . LEU A 1 74  ? 65.048 -60.239 -20.177 1.00 25.86  ?  74  LEU A CD1 1 
ATOM   597  C  CD2 . LEU A 1 74  ? 67.279 -61.310 -20.147 1.00 25.95  ?  74  LEU A CD2 1 
ATOM   598  N  N   . GLY A 1 75  ? 68.396 -56.695 -17.043 1.00 20.31  ?  75  GLY A N   1 
ATOM   599  C  CA  . GLY A 1 75  ? 68.813 -55.302 -16.941 1.00 20.33  ?  75  GLY A CA  1 
ATOM   600  C  C   . GLY A 1 75  ? 68.250 -54.562 -15.718 1.00 20.51  ?  75  GLY A C   1 
ATOM   601  O  O   . GLY A 1 75  ? 67.432 -55.064 -14.930 1.00 16.99  ?  75  GLY A O   1 
ATOM   602  N  N   . PRO A 1 76  ? 68.612 -53.265 -15.567 1.00 22.32  ?  76  PRO A N   1 
ATOM   603  C  CA  . PRO A 1 76  ? 68.086 -52.459 -14.462 1.00 21.89  ?  76  PRO A CA  1 
ATOM   604  C  C   . PRO A 1 76  ? 66.556 -52.458 -14.459 1.00 22.10  ?  76  PRO A C   1 
ATOM   605  O  O   . PRO A 1 76  ? 65.902 -52.577 -15.497 1.00 21.52  ?  76  PRO A O   1 
ATOM   606  C  CB  . PRO A 1 76  ? 68.651 -51.063 -14.674 1.00 21.55  ?  76  PRO A CB  1 
ATOM   607  C  CG  . PRO A 1 76  ? 69.295 -51.086 -16.055 1.00 21.34  ?  76  PRO A CG  1 
ATOM   608  C  CD  . PRO A 1 76  ? 69.462 -52.508 -16.498 1.00 20.77  ?  76  PRO A CD  1 
ATOM   609  N  N   . TYR A 1 77  ? 65.977 -52.314 -13.269 1.00 23.18  ?  77  TYR A N   1 
ATOM   610  C  CA  . TYR A 1 77  ? 64.538 -52.178 -13.170 1.00 24.36  ?  77  TYR A CA  1 
ATOM   611  C  C   . TYR A 1 77  ? 64.156 -51.100 -14.180 1.00 25.93  ?  77  TYR A C   1 
ATOM   612  O  O   . TYR A 1 77  ? 64.870 -50.117 -14.332 1.00 27.32  ?  77  TYR A O   1 
ATOM   613  C  CB  . TYR A 1 77  ? 64.188 -51.921 -11.701 1.00 25.41  ?  77  TYR A CB  1 
ATOM   614  C  CG  . TYR A 1 77  ? 64.585 -53.049 -10.759 1.00 25.65  ?  77  TYR A CG  1 
ATOM   615  C  CD1 . TYR A 1 77  ? 65.656 -52.923 -9.906  1.00 27.30  ?  77  TYR A CD1 1 
ATOM   616  C  CD2 . TYR A 1 77  ? 63.883 -54.243 -10.728 1.00 29.10  ?  77  TYR A CD2 1 
ATOM   617  C  CE1 . TYR A 1 77  ? 66.035 -53.951 -9.056  1.00 31.68  ?  77  TYR A CE1 1 
ATOM   618  C  CE2 . TYR A 1 77  ? 64.241 -55.281 -9.885  1.00 31.24  ?  77  TYR A CE2 1 
ATOM   619  C  CZ  . TYR A 1 77  ? 65.325 -55.137 -9.037  1.00 33.15  ?  77  TYR A CZ  1 
ATOM   620  O  OH  . TYR A 1 77  ? 65.712 -56.164 -8.209  1.00 32.21  ?  77  TYR A OH  1 
ATOM   621  N  N   . LYS A 1 78  ? 63.075 -51.320 -14.925 1.00 27.19  ?  78  LYS A N   1 
ATOM   622  C  CA  . LYS A 1 78  ? 62.646 -50.377 -15.941 1.00 26.51  ?  78  LYS A CA  1 
ATOM   623  C  C   . LYS A 1 78  ? 61.132 -50.360 -15.924 1.00 25.04  ?  78  LYS A C   1 
ATOM   624  O  O   . LYS A 1 78  ? 60.518 -51.410 -15.848 1.00 24.35  ?  78  LYS A O   1 
ATOM   625  C  CB  . LYS A 1 78  ? 63.184 -50.798 -17.309 1.00 27.58  ?  78  LYS A CB  1 
ATOM   626  C  CG  . LYS A 1 78  ? 62.986 -49.771 -18.418 1.00 27.30  ?  78  LYS A CG  1 
ATOM   627  C  CD  . LYS A 1 78  ? 63.544 -48.392 -18.075 1.00 26.11  ?  78  LYS A CD  1 
ATOM   628  C  CE  . LYS A 1 78  ? 63.207 -47.355 -19.085 1.00 26.02  ?  78  LYS A CE  1 
ATOM   629  N  NZ  . LYS A 1 78  ? 62.839 -46.110 -18.411 1.00 25.62  1  78  LYS A NZ  1 
ATOM   630  N  N   . GLY A 1 79  ? 60.538 -49.169 -15.935 1.00 27.76  ?  79  GLY A N   1 
ATOM   631  C  CA  . GLY A 1 79  ? 59.137 -49.063 -15.552 1.00 29.94  ?  79  GLY A CA  1 
ATOM   632  C  C   . GLY A 1 79  ? 58.590 -47.665 -15.782 1.00 30.92  ?  79  GLY A C   1 
ATOM   633  O  O   . GLY A 1 79  ? 58.945 -47.002 -16.750 1.00 41.79  ?  79  GLY A O   1 
ATOM   634  N  N   . GLY A 1 80  ? 57.669 -47.258 -14.925 1.00 29.92  ?  80  GLY A N   1 
ATOM   635  C  CA  . GLY A 1 80  ? 57.051 -45.951 -15.042 1.00 29.51  ?  80  GLY A CA  1 
ATOM   636  C  C   . GLY A 1 80  ? 56.450 -45.545 -13.704 1.00 27.06  ?  80  GLY A C   1 
ATOM   637  O  O   . GLY A 1 80  ? 56.236 -46.387 -12.846 1.00 28.86  ?  80  GLY A O   1 
ATOM   638  N  N   . LEU A 1 81  ? 56.219 -44.250 -13.521 1.00 26.03  ?  81  LEU A N   1 
ATOM   639  C  CA  . LEU A 1 81  ? 55.508 -43.777 -12.357 1.00 25.66  ?  81  LEU A CA  1 
ATOM   640  C  C   . LEU A 1 81  ? 54.111 -43.377 -12.817 1.00 24.56  ?  81  LEU A C   1 
ATOM   641  O  O   . LEU A 1 81  ? 53.953 -42.810 -13.887 1.00 20.56  ?  81  LEU A O   1 
ATOM   642  C  CB  . LEU A 1 81  ? 56.330 -42.640 -11.759 1.00 26.73  ?  81  LEU A CB  1 
ATOM   643  C  CG  . LEU A 1 81  ? 57.793 -42.973 -11.453 1.00 27.41  ?  81  LEU A CG  1 
ATOM   644  C  CD1 . LEU A 1 81  ? 58.565 -41.751 -11.037 1.00 28.81  ?  81  LEU A CD1 1 
ATOM   645  C  CD2 . LEU A 1 81  ? 57.867 -44.002 -10.359 1.00 28.26  ?  81  LEU A CD2 1 
ATOM   646  N  N   . ARG A 1 82  ? 53.104 -43.757 -12.028 1.00 26.74  ?  82  ARG A N   1 
ATOM   647  C  CA  . ARG A 1 82  ? 51.724 -43.359 -12.255 1.00 28.63  ?  82  ARG A CA  1 
ATOM   648  C  C   . ARG A 1 82  ? 51.197 -42.645 -11.016 1.00 29.07  ?  82  ARG A C   1 
ATOM   649  O  O   . ARG A 1 82  ? 51.260 -43.178 -9.901  1.00 31.74  ?  82  ARG A O   1 
ATOM   650  C  CB  . ARG A 1 82  ? 50.849 -44.592 -12.522 1.00 30.36  ?  82  ARG A CB  1 
ATOM   651  C  CG  . ARG A 1 82  ? 49.348 -44.335 -12.547 1.00 30.66  ?  82  ARG A CG  1 
ATOM   652  C  CD  . ARG A 1 82  ? 48.557 -45.503 -13.142 1.00 31.27  ?  82  ARG A CD  1 
ATOM   653  N  NE  . ARG A 1 82  ? 48.977 -45.868 -14.501 1.00 34.07  ?  82  ARG A NE  1 
ATOM   654  C  CZ  . ARG A 1 82  ? 48.403 -46.841 -15.220 1.00 35.80  ?  82  ARG A CZ  1 
ATOM   655  N  NH1 . ARG A 1 82  ? 47.366 -47.491 -14.716 1.00 31.57  1  82  ARG A NH1 1 
ATOM   656  N  NH2 . ARG A 1 82  ? 48.861 -47.158 -16.430 1.00 34.56  ?  82  ARG A NH2 1 
ATOM   657  N  N   . PHE A 1 83  ? 50.667 -41.439 -11.217 1.00 27.08  ?  83  PHE A N   1 
ATOM   658  C  CA  . PHE A 1 83  ? 49.979 -40.741 -10.147 1.00 27.23  ?  83  PHE A CA  1 
ATOM   659  C  C   . PHE A 1 83  ? 48.491 -40.769 -10.463 1.00 27.76  ?  83  PHE A C   1 
ATOM   660  O  O   . PHE A 1 83  ? 48.015 -40.034 -11.311 1.00 29.24  ?  83  PHE A O   1 
ATOM   661  C  CB  . PHE A 1 83  ? 50.465 -39.300 -9.972  1.00 29.91  ?  83  PHE A CB  1 
ATOM   662  C  CG  . PHE A 1 83  ? 51.953 -39.111 -9.680  1.00 28.46  ?  83  PHE A CG  1 
ATOM   663  C  CD1 . PHE A 1 83  ? 52.527 -37.842 -9.758  1.00 27.55  ?  83  PHE A CD1 1 
ATOM   664  C  CD2 . PHE A 1 83  ? 52.778 -40.189 -9.365  1.00 25.76  ?  83  PHE A CD2 1 
ATOM   665  C  CE1 . PHE A 1 83  ? 53.879 -37.656 -9.500  1.00 27.84  ?  83  PHE A CE1 1 
ATOM   666  C  CE2 . PHE A 1 83  ? 54.129 -39.999 -9.132  1.00 27.27  ?  83  PHE A CE2 1 
ATOM   667  C  CZ  . PHE A 1 83  ? 54.675 -38.732 -9.189  1.00 28.23  ?  83  PHE A CZ  1 
ATOM   668  N  N   . HIS A 1 84  ? 47.771 -41.669 -9.796  1.00 30.12  ?  84  HIS A N   1 
ATOM   669  C  CA  . HIS A 1 84  ? 46.338 -41.818 -9.966  1.00 29.92  ?  84  HIS A CA  1 
ATOM   670  C  C   . HIS A 1 84  ? 45.793 -42.408 -8.668  1.00 29.94  ?  84  HIS A C   1 
ATOM   671  O  O   . HIS A 1 84  ? 46.425 -43.312 -8.104  1.00 24.98  ?  84  HIS A O   1 
ATOM   672  C  CB  . HIS A 1 84  ? 46.013 -42.711 -11.174 1.00 29.69  ?  84  HIS A CB  1 
ATOM   673  C  CG  . HIS A 1 84  ? 44.556 -42.719 -11.535 1.00 30.22  ?  84  HIS A CG  1 
ATOM   674  N  ND1 . HIS A 1 84  ? 43.647 -43.627 -11.038 1.00 26.45  ?  84  HIS A ND1 1 
ATOM   675  C  CD2 . HIS A 1 84  ? 43.853 -41.892 -12.344 1.00 29.25  ?  84  HIS A CD2 1 
ATOM   676  C  CE1 . HIS A 1 84  ? 42.451 -43.359 -11.539 1.00 26.51  ?  84  HIS A CE1 1 
ATOM   677  N  NE2 . HIS A 1 84  ? 42.554 -42.313 -12.332 1.00 27.34  ?  84  HIS A NE2 1 
ATOM   678  N  N   . PRO A 1 85  ? 44.606 -41.940 -8.190  1.00 28.95  ?  85  PRO A N   1 
ATOM   679  C  CA  . PRO A 1 85  ? 44.108 -42.277 -6.843  1.00 27.62  ?  85  PRO A CA  1 
ATOM   680  C  C   . PRO A 1 85  ? 43.545 -43.688 -6.729  1.00 30.51  ?  85  PRO A C   1 
ATOM   681  O  O   . PRO A 1 85  ? 43.145 -44.097 -5.642  1.00 29.24  ?  85  PRO A O   1 
ATOM   682  C  CB  . PRO A 1 85  ? 43.047 -41.226 -6.586  1.00 26.58  ?  85  PRO A CB  1 
ATOM   683  C  CG  . PRO A 1 85  ? 42.519 -40.958 -7.979  1.00 28.92  ?  85  PRO A CG  1 
ATOM   684  C  CD  . PRO A 1 85  ? 43.703 -41.041 -8.922  1.00 27.28  ?  85  PRO A CD  1 
ATOM   685  N  N   . SER A 1 86  ? 43.521 -44.390 -7.881  1.00 33.33  ?  86  SER A N   1 
ATOM   686  C  CA  . SER A 1 86  ? 43.208 -45.807 -8.011  1.00 29.90  ?  86  SER A CA  1 
ATOM   687  C  C   . SER A 1 86  ? 44.370 -46.678 -7.556  1.00 29.51  ?  86  SER A C   1 
ATOM   688  O  O   . SER A 1 86  ? 44.166 -47.863 -7.284  1.00 35.63  ?  86  SER A O   1 
ATOM   689  C  CB  . SER A 1 86  ? 42.916 -46.152 -9.447  1.00 31.61  ?  86  SER A CB  1 
ATOM   690  O  OG  . SER A 1 86  ? 44.107 -46.160 -10.239 1.00 32.76  ?  86  SER A OG  1 
ATOM   691  N  N   . VAL A 1 87  ? 45.580 -46.097 -7.548  1.00 25.83  ?  87  VAL A N   1 
ATOM   692  C  CA  . VAL A 1 87  ? 46.835 -46.845 -7.476  1.00 23.92  ?  87  VAL A CA  1 
ATOM   693  C  C   . VAL A 1 87  ? 46.984 -47.550 -6.125  1.00 21.60  ?  87  VAL A C   1 
ATOM   694  O  O   . VAL A 1 87  ? 46.723 -46.964 -5.079  1.00 21.06  ?  87  VAL A O   1 
ATOM   695  C  CB  . VAL A 1 87  ? 48.055 -45.932 -7.734  1.00 22.26  ?  87  VAL A CB  1 
ATOM   696  C  CG1 . VAL A 1 87  ? 49.323 -46.450 -7.065  1.00 22.11  ?  87  VAL A CG1 1 
ATOM   697  C  CG2 . VAL A 1 87  ? 48.291 -45.685 -9.220  1.00 21.73  ?  87  VAL A CG2 1 
ATOM   698  N  N   . ASN A 1 88  ? 47.461 -48.794 -6.196  1.00 20.10  ?  88  ASN A N   1 
ATOM   699  C  CA  . ASN A 1 88  ? 47.916 -49.586 -5.068  1.00 20.78  ?  88  ASN A CA  1 
ATOM   700  C  C   . ASN A 1 88  ? 48.952 -50.598 -5.586  1.00 25.13  ?  88  ASN A C   1 
ATOM   701  O  O   . ASN A 1 88  ? 49.417 -50.508 -6.737  1.00 23.30  ?  88  ASN A O   1 
ATOM   702  C  CB  . ASN A 1 88  ? 46.727 -50.208 -4.332  1.00 19.50  ?  88  ASN A CB  1 
ATOM   703  C  CG  . ASN A 1 88  ? 45.799 -51.012 -5.221  1.00 19.07  ?  88  ASN A CG  1 
ATOM   704  O  OD1 . ASN A 1 88  ? 46.191 -51.561 -6.258  1.00 18.92  ?  88  ASN A OD1 1 
ATOM   705  N  ND2 . ASN A 1 88  ? 44.564 -51.176 -4.785  1.00 18.20  ?  88  ASN A ND2 1 
ATOM   706  N  N   . LEU A 1 89  ? 49.309 -51.575 -4.729  1.00 27.52  ?  89  LEU A N   1 
ATOM   707  C  CA  . LEU A 1 89  ? 50.426 -52.466 -4.990  1.00 26.94  ?  89  LEU A CA  1 
ATOM   708  C  C   . LEU A 1 89  ? 50.006 -53.464 -6.063  1.00 31.73  ?  89  LEU A C   1 
ATOM   709  O  O   . LEU A 1 89  ? 50.775 -53.737 -6.992  1.00 31.72  ?  89  LEU A O   1 
ATOM   710  C  CB  . LEU A 1 89  ? 50.817 -53.153 -3.685  1.00 26.85  ?  89  LEU A CB  1 
ATOM   711  C  CG  . LEU A 1 89  ? 52.043 -54.067 -3.774  1.00 29.83  ?  89  LEU A CG  1 
ATOM   712  C  CD1 . LEU A 1 89  ? 53.279 -53.276 -4.210  1.00 32.49  ?  89  LEU A CD1 1 
ATOM   713  C  CD2 . LEU A 1 89  ? 52.322 -54.807 -2.481  1.00 28.08  ?  89  LEU A CD2 1 
ATOM   714  N  N   . SER A 1 90  ? 48.775 -53.989 -5.871  1.00 33.47  ?  90  SER A N   1 
ATOM   715  C  CA  . SER A 1 90  ? 48.061 -54.907 -6.752  1.00 27.62  ?  90  SER A CA  1 
ATOM   716  C  C   . SER A 1 90  ? 48.179 -54.466 -8.199  1.00 25.17  ?  90  SER A C   1 
ATOM   717  O  O   . SER A 1 90  ? 48.628 -55.264 -9.020  1.00 22.38  ?  90  SER A O   1 
ATOM   718  C  CB  . SER A 1 90  ? 46.617 -54.987 -6.345  1.00 27.49  ?  90  SER A CB  1 
ATOM   719  O  OG  . SER A 1 90  ? 45.842 -55.722 -7.276  1.00 29.74  ?  90  SER A OG  1 
ATOM   720  N  N   . ILE A 1 91  ? 47.807 -53.192 -8.456  1.00 25.69  ?  91  ILE A N   1 
ATOM   721  C  CA  . ILE A 1 91  ? 47.820 -52.579 -9.792  1.00 26.32  ?  91  ILE A CA  1 
ATOM   722  C  C   . ILE A 1 91  ? 49.252 -52.464 -10.322 1.00 28.82  ?  91  ILE A C   1 
ATOM   723  O  O   . ILE A 1 91  ? 49.491 -52.730 -11.502 1.00 28.22  ?  91  ILE A O   1 
ATOM   724  C  CB  . ILE A 1 91  ? 47.108 -51.206 -9.822  1.00 23.90  ?  91  ILE A CB  1 
ATOM   725  C  CG1 . ILE A 1 91  ? 45.721 -51.288 -9.172  1.00 24.26  ?  91  ILE A CG1 1 
ATOM   726  C  CG2 . ILE A 1 91  ? 47.040 -50.650 -11.241 1.00 24.49  ?  91  ILE A CG2 1 
ATOM   727  C  CD1 . ILE A 1 91  ? 44.614 -50.494 -9.834  1.00 24.51  ?  91  ILE A CD1 1 
ATOM   728  N  N   . LEU A 1 92  ? 50.189 -52.068 -9.441  1.00 28.63  ?  92  LEU A N   1 
ATOM   729  C  CA  . LEU A 1 92  ? 51.553 -51.775 -9.840  1.00 27.85  ?  92  LEU A CA  1 
ATOM   730  C  C   . LEU A 1 92  ? 52.372 -53.057 -9.934  1.00 30.01  ?  92  LEU A C   1 
ATOM   731  O  O   . LEU A 1 92  ? 53.472 -53.020 -10.492 1.00 36.70  ?  92  LEU A O   1 
ATOM   732  C  CB  . LEU A 1 92  ? 52.193 -50.787 -8.866  1.00 27.61  ?  92  LEU A CB  1 
ATOM   733  C  CG  . LEU A 1 92  ? 51.601 -49.374 -8.842  1.00 27.15  ?  92  LEU A CG  1 
ATOM   734  C  CD1 . LEU A 1 92  ? 52.023 -48.548 -7.626  1.00 26.58  ?  92  LEU A CD1 1 
ATOM   735  C  CD2 . LEU A 1 92  ? 51.991 -48.662 -10.118 1.00 26.97  ?  92  LEU A CD2 1 
ATOM   736  N  N   . LYS A 1 93  ? 51.875 -54.165 -9.362  1.00 27.66  ?  93  LYS A N   1 
ATOM   737  C  CA  . LYS A 1 93  ? 52.500 -55.463 -9.574  1.00 26.68  ?  93  LYS A CA  1 
ATOM   738  C  C   . LYS A 1 93  ? 51.940 -56.065 -10.859 1.00 28.35  ?  93  LYS A C   1 
ATOM   739  O  O   . LYS A 1 93  ? 52.657 -56.755 -11.581 1.00 27.42  ?  93  LYS A O   1 
ATOM   740  C  CB  . LYS A 1 93  ? 52.272 -56.417 -8.404  1.00 29.39  ?  93  LYS A CB  1 
ATOM   741  C  CG  . LYS A 1 93  ? 53.087 -56.134 -7.152  1.00 31.73  ?  93  LYS A CG  1 
ATOM   742  C  CD  . LYS A 1 93  ? 52.685 -57.016 -5.980  1.00 33.07  ?  93  LYS A CD  1 
ATOM   743  C  CE  . LYS A 1 93  ? 52.999 -58.467 -6.200  1.00 33.96  ?  93  LYS A CE  1 
ATOM   744  N  NZ  . LYS A 1 93  ? 51.880 -59.286 -5.718  1.00 35.87  1  93  LYS A NZ  1 
ATOM   745  N  N   . PHE A 1 94  ? 50.663 -55.759 -11.156 1.00 28.86  ?  94  PHE A N   1 
ATOM   746  C  CA  . PHE A 1 94  ? 50.076 -56.049 -12.462 1.00 29.05  ?  94  PHE A CA  1 
ATOM   747  C  C   . PHE A 1 94  ? 50.924 -55.385 -13.551 1.00 25.09  ?  94  PHE A C   1 
ATOM   748  O  O   . PHE A 1 94  ? 51.568 -56.045 -14.354 1.00 26.58  ?  94  PHE A O   1 
ATOM   749  C  CB  . PHE A 1 94  ? 48.590 -55.639 -12.544 1.00 29.58  ?  94  PHE A CB  1 
ATOM   750  C  CG  . PHE A 1 94  ? 48.056 -55.510 -13.969 1.00 30.57  ?  94  PHE A CG  1 
ATOM   751  C  CD1 . PHE A 1 94  ? 48.186 -56.558 -14.881 1.00 31.50  ?  94  PHE A CD1 1 
ATOM   752  C  CD2 . PHE A 1 94  ? 47.501 -54.312 -14.428 1.00 31.19  ?  94  PHE A CD2 1 
ATOM   753  C  CE1 . PHE A 1 94  ? 47.757 -56.426 -16.200 1.00 29.67  ?  94  PHE A CE1 1 
ATOM   754  C  CE2 . PHE A 1 94  ? 47.085 -54.185 -15.749 1.00 29.52  ?  94  PHE A CE2 1 
ATOM   755  C  CZ  . PHE A 1 94  ? 47.205 -55.246 -16.629 1.00 28.24  ?  94  PHE A CZ  1 
ATOM   756  N  N   . LEU A 1 95  ? 50.963 -54.064 -13.550 1.00 24.52  ?  95  LEU A N   1 
ATOM   757  C  CA  . LEU A 1 95  ? 51.682 -53.314 -14.569 1.00 26.80  ?  95  LEU A CA  1 
ATOM   758  C  C   . LEU A 1 95  ? 53.170 -53.703 -14.628 1.00 27.65  ?  95  LEU A C   1 
ATOM   759  O  O   . LEU A 1 95  ? 53.759 -53.804 -15.719 1.00 23.47  ?  95  LEU A O   1 
ATOM   760  C  CB  . LEU A 1 95  ? 51.449 -51.846 -14.199 1.00 26.37  ?  95  LEU A CB  1 
ATOM   761  C  CG  . LEU A 1 95  ? 49.995 -51.366 -14.288 1.00 25.82  ?  95  LEU A CG  1 
ATOM   762  C  CD1 . LEU A 1 95  ? 49.869 -49.903 -13.917 1.00 26.60  ?  95  LEU A CD1 1 
ATOM   763  C  CD2 . LEU A 1 95  ? 49.450 -51.603 -15.688 1.00 25.15  ?  95  LEU A CD2 1 
ATOM   764  N  N   . GLY A 1 96  ? 53.763 -53.911 -13.436 1.00 26.31  ?  96  GLY A N   1 
ATOM   765  C  CA  . GLY A 1 96  ? 55.172 -54.231 -13.290 1.00 27.12  ?  96  GLY A CA  1 
ATOM   766  C  C   . GLY A 1 96  ? 55.512 -55.604 -13.865 1.00 27.66  ?  96  GLY A C   1 
ATOM   767  O  O   . GLY A 1 96  ? 56.540 -55.744 -14.525 1.00 24.73  ?  96  GLY A O   1 
ATOM   768  N  N   . PHE A 1 97  ? 54.662 -56.607 -13.567 1.00 29.38  ?  97  PHE A N   1 
ATOM   769  C  CA  . PHE A 1 97  ? 54.799 -57.962 -14.094 1.00 30.17  ?  97  PHE A CA  1 
ATOM   770  C  C   . PHE A 1 97  ? 54.845 -57.903 -15.623 1.00 29.87  ?  97  PHE A C   1 
ATOM   771  O  O   . PHE A 1 97  ? 55.715 -58.499 -16.239 1.00 29.21  ?  97  PHE A O   1 
ATOM   772  C  CB  . PHE A 1 97  ? 53.661 -58.891 -13.639 1.00 29.72  ?  97  PHE A CB  1 
ATOM   773  C  CG  . PHE A 1 97  ? 53.882 -60.391 -13.820 1.00 29.76  ?  97  PHE A CG  1 
ATOM   774  C  CD1 . PHE A 1 97  ? 54.982 -61.042 -13.254 1.00 32.52  ?  97  PHE A CD1 1 
ATOM   775  C  CD2 . PHE A 1 97  ? 52.986 -61.171 -14.549 1.00 30.15  ?  97  PHE A CD2 1 
ATOM   776  C  CE1 . PHE A 1 97  ? 55.166 -62.433 -13.392 1.00 31.35  ?  97  PHE A CE1 1 
ATOM   777  C  CE2 . PHE A 1 97  ? 53.184 -62.555 -14.694 1.00 31.14  ?  97  PHE A CE2 1 
ATOM   778  C  CZ  . PHE A 1 97  ? 54.271 -63.185 -14.115 1.00 28.20  ?  97  PHE A CZ  1 
ATOM   779  N  N   . GLU A 1 98  ? 53.905 -57.182 -16.232 1.00 33.17  ?  98  GLU A N   1 
ATOM   780  C  CA  . GLU A 1 98  ? 53.839 -57.077 -17.683 1.00 38.55  ?  98  GLU A CA  1 
ATOM   781  C  C   . GLU A 1 98  ? 55.059 -56.361 -18.269 1.00 32.39  ?  98  GLU A C   1 
ATOM   782  O  O   . GLU A 1 98  ? 55.565 -56.809 -19.292 1.00 30.31  ?  98  GLU A O   1 
ATOM   783  C  CB  . GLU A 1 98  ? 52.538 -56.416 -18.139 1.00 49.76  ?  98  GLU A CB  1 
ATOM   784  C  CG  . GLU A 1 98  ? 51.299 -57.288 -17.923 1.00 56.98  ?  98  GLU A CG  1 
ATOM   785  C  CD  . GLU A 1 98  ? 50.077 -56.914 -18.769 1.00 66.84  ?  98  GLU A CD  1 
ATOM   786  O  OE1 . GLU A 1 98  ? 49.162 -57.775 -18.839 1.00 68.85  ?  98  GLU A OE1 1 
ATOM   787  O  OE2 . GLU A 1 98  ? 50.006 -55.791 -19.352 1.00 62.42  -1 98  GLU A OE2 1 
ATOM   788  N  N   . GLN A 1 99  ? 55.545 -55.277 -17.639 1.00 31.10  ?  99  GLN A N   1 
ATOM   789  C  CA  . GLN A 1 99  ? 56.736 -54.570 -18.124 1.00 30.00  ?  99  GLN A CA  1 
ATOM   790  C  C   . GLN A 1 99  ? 57.947 -55.498 -18.258 1.00 27.11  ?  99  GLN A C   1 
ATOM   791  O  O   . GLN A 1 99  ? 58.780 -55.287 -19.128 1.00 28.30  ?  99  GLN A O   1 
ATOM   792  C  CB  . GLN A 1 99  ? 57.163 -53.369 -17.275 1.00 28.45  ?  99  GLN A CB  1 
ATOM   793  C  CG  . GLN A 1 99  ? 56.322 -52.127 -17.535 1.00 29.33  ?  99  GLN A CG  1 
ATOM   794  C  CD  . GLN A 1 99  ? 56.363 -51.699 -18.987 1.00 29.58  ?  99  GLN A CD  1 
ATOM   795  O  OE1 . GLN A 1 99  ? 55.321 -51.532 -19.625 1.00 28.38  ?  99  GLN A OE1 1 
ATOM   796  N  NE2 . GLN A 1 99  ? 57.562 -51.558 -19.541 1.00 29.37  ?  99  GLN A NE2 1 
ATOM   797  N  N   . ILE A 1 100 ? 58.038 -56.524 -17.414 1.00 23.67  ?  100 ILE A N   1 
ATOM   798  C  CA  . ILE A 1 100 ? 59.142 -57.460 -17.494 1.00 24.47  ?  100 ILE A CA  1 
ATOM   799  C  C   . ILE A 1 100 ? 59.218 -58.066 -18.900 1.00 24.65  ?  100 ILE A C   1 
ATOM   800  O  O   . ILE A 1 100 ? 60.273 -58.006 -19.541 1.00 24.92  ?  100 ILE A O   1 
ATOM   801  C  CB  . ILE A 1 100 ? 59.013 -58.554 -16.418 1.00 23.00  ?  100 ILE A CB  1 
ATOM   802  C  CG1 . ILE A 1 100 ? 58.810 -57.976 -15.032 1.00 20.72  ?  100 ILE A CG1 1 
ATOM   803  C  CG2 . ILE A 1 100 ? 60.222 -59.499 -16.464 1.00 24.59  ?  100 ILE A CG2 1 
ATOM   804  C  CD1 . ILE A 1 100 ? 58.573 -59.023 -13.967 1.00 21.03  ?  100 ILE A CD1 1 
ATOM   805  N  N   . PHE A 1 101 ? 58.107 -58.673 -19.347 1.00 23.39  ?  101 PHE A N   1 
ATOM   806  C  CA  . PHE A 1 101 ? 58.096 -59.499 -20.552 1.00 26.14  ?  101 PHE A CA  1 
ATOM   807  C  C   . PHE A 1 101 ? 58.014 -58.609 -21.798 1.00 27.61  ?  101 PHE A C   1 
ATOM   808  O  O   . PHE A 1 101 ? 58.525 -58.979 -22.853 1.00 24.30  ?  101 PHE A O   1 
ATOM   809  C  CB  . PHE A 1 101 ? 56.993 -60.555 -20.388 1.00 25.08  ?  101 PHE A CB  1 
ATOM   810  C  CG  . PHE A 1 101 ? 57.062 -61.308 -19.060 1.00 25.04  ?  101 PHE A CG  1 
ATOM   811  C  CD1 . PHE A 1 101 ? 55.921 -61.516 -18.286 1.00 24.52  ?  101 PHE A CD1 1 
ATOM   812  C  CD2 . PHE A 1 101 ? 58.274 -61.793 -18.567 1.00 23.81  ?  101 PHE A CD2 1 
ATOM   813  C  CE1 . PHE A 1 101 ? 55.999 -62.205 -17.079 1.00 22.86  ?  101 PHE A CE1 1 
ATOM   814  C  CE2 . PHE A 1 101 ? 58.342 -62.448 -17.348 1.00 21.92  ?  101 PHE A CE2 1 
ATOM   815  C  CZ  . PHE A 1 101 ? 57.208 -62.654 -16.610 1.00 21.36  ?  101 PHE A CZ  1 
ATOM   816  N  N   . LYS A 1 102 ? 57.411 -57.420 -21.636 1.00 31.07  ?  102 LYS A N   1 
ATOM   817  C  CA  . LYS A 1 102 ? 57.291 -56.409 -22.679 1.00 33.11  ?  102 LYS A CA  1 
ATOM   818  C  C   . LYS A 1 102 ? 58.643 -55.771 -23.002 1.00 35.06  ?  102 LYS A C   1 
ATOM   819  O  O   . LYS A 1 102 ? 58.985 -55.591 -24.171 1.00 39.94  ?  102 LYS A O   1 
ATOM   820  C  CB  . LYS A 1 102 ? 56.324 -55.316 -22.211 1.00 33.07  ?  102 LYS A CB  1 
ATOM   821  C  CG  . LYS A 1 102 ? 55.939 -54.334 -23.311 1.00 34.09  ?  102 LYS A CG  1 
ATOM   822  C  CD  . LYS A 1 102 ? 54.488 -53.862 -23.264 1.00 33.14  ?  102 LYS A CD  1 
ATOM   823  C  CE  . LYS A 1 102 ? 54.147 -52.883 -24.358 1.00 30.81  ?  102 LYS A CE  1 
ATOM   824  N  NZ  . LYS A 1 102 ? 55.000 -51.703 -24.292 1.00 29.94  1  102 LYS A NZ  1 
ATOM   825  N  N   . ASN A 1 103 ? 59.376 -55.392 -21.947 1.00 32.39  ?  103 ASN A N   1 
ATOM   826  C  CA  . ASN A 1 103 ? 60.734 -54.873 -22.045 1.00 27.09  ?  103 ASN A CA  1 
ATOM   827  C  C   . ASN A 1 103 ? 61.642 -55.910 -22.708 1.00 25.41  ?  103 ASN A C   1 
ATOM   828  O  O   . ASN A 1 103 ? 62.447 -55.575 -23.562 1.00 24.75  ?  103 ASN A O   1 
ATOM   829  C  CB  . ASN A 1 103 ? 61.256 -54.438 -20.672 1.00 24.86  ?  103 ASN A CB  1 
ATOM   830  C  CG  . ASN A 1 103 ? 60.637 -53.141 -20.182 1.00 23.08  ?  103 ASN A CG  1 
ATOM   831  O  OD1 . ASN A 1 103 ? 59.856 -52.510 -20.904 1.00 21.67  ?  103 ASN A OD1 1 
ATOM   832  N  ND2 . ASN A 1 103 ? 60.967 -52.719 -18.967 1.00 21.95  ?  103 ASN A ND2 1 
ATOM   833  N  N   . ALA A 1 104 ? 61.486 -57.175 -22.319 1.00 26.70  ?  104 ALA A N   1 
ATOM   834  C  CA  . ALA A 1 104 ? 62.366 -58.258 -22.736 1.00 27.32  ?  104 ALA A CA  1 
ATOM   835  C  C   . ALA A 1 104 ? 62.318 -58.453 -24.247 1.00 27.39  ?  104 ALA A C   1 
ATOM   836  O  O   . ALA A 1 104 ? 63.338 -58.742 -24.860 1.00 32.77  ?  104 ALA A O   1 
ATOM   837  C  CB  . ALA A 1 104 ? 61.980 -59.538 -22.010 1.00 28.04  ?  104 ALA A CB  1 
ATOM   838  N  N   . LEU A 1 105 ? 61.120 -58.319 -24.826 1.00 28.04  ?  105 LEU A N   1 
ATOM   839  C  CA  . LEU A 1 105 ? 60.878 -58.505 -26.254 1.00 28.06  ?  105 LEU A CA  1 
ATOM   840  C  C   . LEU A 1 105 ? 61.790 -57.631 -27.112 1.00 29.17  ?  105 LEU A C   1 
ATOM   841  O  O   . LEU A 1 105 ? 62.122 -58.020 -28.231 1.00 26.78  ?  105 LEU A O   1 
ATOM   842  C  CB  . LEU A 1 105 ? 59.437 -58.116 -26.544 1.00 27.73  ?  105 LEU A CB  1 
ATOM   843  C  CG  . LEU A 1 105 ? 58.366 -59.136 -26.182 1.00 29.30  ?  105 LEU A CG  1 
ATOM   844  C  CD1 . LEU A 1 105 ? 57.034 -58.415 -26.060 1.00 29.13  ?  105 LEU A CD1 1 
ATOM   845  C  CD2 . LEU A 1 105 ? 58.325 -60.203 -27.241 1.00 32.26  ?  105 LEU A CD2 1 
ATOM   846  N  N   . THR A 1 106 ? 62.108 -56.432 -26.596 1.00 29.85  ?  106 THR A N   1 
ATOM   847  C  CA  . THR A 1 106 ? 62.886 -55.420 -27.295 1.00 30.82  ?  106 THR A CA  1 
ATOM   848  C  C   . THR A 1 106 ? 64.269 -55.965 -27.642 1.00 30.22  ?  106 THR A C   1 
ATOM   849  O  O   . THR A 1 106 ? 64.840 -55.565 -28.654 1.00 33.49  ?  106 THR A O   1 
ATOM   850  C  CB  . THR A 1 106 ? 63.031 -54.145 -26.452 1.00 34.07  ?  106 THR A CB  1 
ATOM   851  O  OG1 . THR A 1 106 ? 63.865 -54.427 -25.323 1.00 33.81  ?  106 THR A OG1 1 
ATOM   852  C  CG2 . THR A 1 106 ? 61.698 -53.551 -26.025 1.00 31.95  ?  106 THR A CG2 1 
ATOM   853  N  N   . GLY A 1 107 ? 64.821 -56.832 -26.781 1.00 26.18  ?  107 GLY A N   1 
ATOM   854  C  CA  . GLY A 1 107 ? 66.171 -57.338 -26.978 1.00 24.77  ?  107 GLY A CA  1 
ATOM   855  C  C   . GLY A 1 107 ? 67.222 -56.552 -26.188 1.00 24.70  ?  107 GLY A C   1 
ATOM   856  O  O   . GLY A 1 107 ? 68.361 -57.012 -26.057 1.00 22.00  ?  107 GLY A O   1 
ATOM   857  N  N   . LEU A 1 108 ? 66.829 -55.372 -25.663 1.00 25.51  ?  108 LEU A N   1 
ATOM   858  C  CA  . LEU A 1 108 ? 67.700 -54.502 -24.872 1.00 23.50  ?  108 LEU A CA  1 
ATOM   859  C  C   . LEU A 1 108 ? 67.768 -55.054 -23.458 1.00 22.85  ?  108 LEU A C   1 
ATOM   860  O  O   . LEU A 1 108 ? 66.910 -55.868 -23.101 1.00 21.24  ?  108 LEU A O   1 
ATOM   861  C  CB  . LEU A 1 108 ? 67.181 -53.068 -24.818 1.00 22.35  ?  108 LEU A CB  1 
ATOM   862  C  CG  . LEU A 1 108 ? 66.769 -52.453 -26.157 1.00 20.99  ?  108 LEU A CG  1 
ATOM   863  C  CD1 . LEU A 1 108 ? 65.579 -51.539 -25.919 1.00 21.79  ?  108 LEU A CD1 1 
ATOM   864  C  CD2 . LEU A 1 108 ? 67.919 -51.714 -26.786 1.00 18.80  ?  108 LEU A CD2 1 
ATOM   865  N  N   . ASN A 1 109 ? 68.746 -54.557 -22.683 1.00 22.77  ?  109 ASN A N   1 
ATOM   866  C  CA  . ASN A 1 109 ? 68.965 -55.001 -21.310 1.00 23.75  ?  109 ASN A CA  1 
ATOM   867  C  C   . ASN A 1 109 ? 68.143 -54.160 -20.333 1.00 21.49  ?  109 ASN A C   1 
ATOM   868  O  O   . ASN A 1 109 ? 68.635 -53.213 -19.751 1.00 18.27  ?  109 ASN A O   1 
ATOM   869  C  CB  . ASN A 1 109 ? 70.446 -54.975 -20.940 1.00 24.55  ?  109 ASN A CB  1 
ATOM   870  C  CG  . ASN A 1 109 ? 71.257 -55.969 -21.736 1.00 24.25  ?  109 ASN A CG  1 
ATOM   871  O  OD1 . ASN A 1 109 ? 72.178 -55.564 -22.442 1.00 23.98  ?  109 ASN A OD1 1 
ATOM   872  N  ND2 . ASN A 1 109 ? 70.986 -57.259 -21.599 1.00 24.24  ?  109 ASN A ND2 1 
ATOM   873  N  N   . MET A 1 110 ? 66.874 -54.524 -20.171 1.00 24.83  ?  110 MET A N   1 
ATOM   874  C  CA  . MET A 1 110 ? 65.960 -53.831 -19.276 1.00 28.08  ?  110 MET A CA  1 
ATOM   875  C  C   . MET A 1 110 ? 65.156 -54.844 -18.464 1.00 28.85  ?  110 MET A C   1 
ATOM   876  O  O   . MET A 1 110 ? 64.583 -55.772 -19.014 1.00 28.96  ?  110 MET A O   1 
ATOM   877  C  CB  . MET A 1 110 ? 65.016 -52.914 -20.055 1.00 28.41  ?  110 MET A CB  1 
ATOM   878  C  CG  . MET A 1 110 ? 65.756 -51.782 -20.736 1.00 31.03  ?  110 MET A CG  1 
ATOM   879  S  SD  . MET A 1 110 ? 64.678 -50.526 -21.440 1.00 33.11  ?  110 MET A SD  1 
ATOM   880  C  CE  . MET A 1 110 ? 63.507 -51.527 -22.368 1.00 31.20  ?  110 MET A CE  1 
ATOM   881  N  N   . GLY A 1 111 ? 65.166 -54.667 -17.141 1.00 31.27  ?  111 GLY A N   1 
ATOM   882  C  CA  . GLY A 1 111 ? 64.329 -55.437 -16.240 1.00 33.49  ?  111 GLY A CA  1 
ATOM   883  C  C   . GLY A 1 111 ? 62.900 -54.911 -16.283 1.00 33.25  ?  111 GLY A C   1 
ATOM   884  O  O   . GLY A 1 111 ? 62.499 -54.302 -17.270 1.00 34.82  ?  111 GLY A O   1 
ATOM   885  N  N   . GLY A 1 112 ? 62.145 -55.136 -15.208 1.00 32.17  ?  112 GLY A N   1 
ATOM   886  C  CA  . GLY A 1 112 ? 60.736 -54.782 -15.197 1.00 32.12  ?  112 GLY A CA  1 
ATOM   887  C  C   . GLY A 1 112 ? 60.320 -54.356 -13.800 1.00 34.49  ?  112 GLY A C   1 
ATOM   888  O  O   . GLY A 1 112 ? 60.663 -55.030 -12.827 1.00 43.77  ?  112 GLY A O   1 
ATOM   889  N  N   . GLY A 1 113 ? 59.640 -53.206 -13.727 1.00 32.54  ?  113 GLY A N   1 
ATOM   890  C  CA  . GLY A 1 113 ? 59.213 -52.607 -12.473 1.00 29.94  ?  113 GLY A CA  1 
ATOM   891  C  C   . GLY A 1 113 ? 58.163 -51.544 -12.766 1.00 28.90  ?  113 GLY A C   1 
ATOM   892  O  O   . GLY A 1 113 ? 57.862 -51.309 -13.933 1.00 27.02  ?  113 GLY A O   1 
ATOM   893  N  N   . LYS A 1 114 ? 57.606 -50.938 -11.709 1.00 28.51  ?  114 LYS A N   1 
ATOM   894  C  CA  . LYS A 1 114 ? 56.645 -49.854 -11.834 1.00 27.36  ?  114 LYS A CA  1 
ATOM   895  C  C   . LYS A 1 114 ? 56.445 -49.259 -10.454 1.00 25.61  ?  114 LYS A C   1 
ATOM   896  O  O   . LYS A 1 114 ? 56.681 -49.951 -9.468  1.00 24.73  ?  114 LYS A O   1 
ATOM   897  C  CB  . LYS A 1 114 ? 55.271 -50.316 -12.329 1.00 31.98  ?  114 LYS A CB  1 
ATOM   898  C  CG  . LYS A 1 114 ? 54.441 -49.271 -13.135 1.00 34.09  ?  114 LYS A CG  1 
ATOM   899  C  CD  . LYS A 1 114 ? 54.689 -49.260 -14.648 1.00 32.82  ?  114 LYS A CD  1 
ATOM   900  C  CE  . LYS A 1 114 ? 54.020 -48.130 -15.392 1.00 30.80  ?  114 LYS A CE  1 
ATOM   901  N  NZ  . LYS A 1 114 ? 52.801 -48.496 -16.127 1.00 28.71  1  114 LYS A NZ  1 
ATOM   902  N  N   . GLY A 1 115 ? 56.029 -47.983 -10.404 1.00 25.88  ?  115 GLY A N   1 
ATOM   903  C  CA  . GLY A 1 115 ? 55.815 -47.262 -9.153  1.00 25.15  ?  115 GLY A CA  1 
ATOM   904  C  C   . GLY A 1 115 ? 54.896 -46.059 -9.340  1.00 24.65  ?  115 GLY A C   1 
ATOM   905  O  O   . GLY A 1 115 ? 54.318 -45.903 -10.399 1.00 27.31  ?  115 GLY A O   1 
ATOM   906  N  N   . GLY A 1 116 ? 54.774 -45.194 -8.323  1.00 26.40  ?  116 GLY A N   1 
ATOM   907  C  CA  . GLY A 1 116 ? 53.820 -44.090 -8.377  1.00 25.52  ?  116 GLY A CA  1 
ATOM   908  C  C   . GLY A 1 116 ? 53.156 -43.879 -7.021  1.00 25.05  ?  116 GLY A C   1 
ATOM   909  O  O   . GLY A 1 116 ? 53.710 -44.339 -6.025  1.00 25.05  ?  116 GLY A O   1 
ATOM   910  N  N   . SER A 1 117 ? 51.969 -43.231 -7.026  1.00 23.00  ?  117 SER A N   1 
ATOM   911  C  CA  . SER A 1 117 ? 51.237 -42.822 -5.831  1.00 20.17  ?  117 SER A CA  1 
ATOM   912  C  C   . SER A 1 117 ? 49.741 -42.763 -6.152  1.00 20.47  ?  117 SER A C   1 
ATOM   913  O  O   . SER A 1 117 ? 49.360 -42.845 -7.319  1.00 20.95  ?  117 SER A O   1 
ATOM   914  C  CB  . SER A 1 117 ? 51.737 -41.480 -5.329  1.00 19.63  ?  117 SER A CB  1 
ATOM   915  O  OG  . SER A 1 117 ? 51.450 -41.246 -3.953  1.00 20.89  ?  117 SER A OG  1 
ATOM   916  N  N   . ASP A 1 118 ? 48.914 -42.626 -5.102  1.00 19.56  ?  118 ASP A N   1 
ATOM   917  C  CA  . ASP A 1 118 ? 47.489 -42.367 -5.195  1.00 20.22  ?  118 ASP A CA  1 
ATOM   918  C  C   . ASP A 1 118 ? 47.229 -40.860 -5.056  1.00 24.17  ?  118 ASP A C   1 
ATOM   919  O  O   . ASP A 1 118 ? 46.098 -40.412 -4.778  1.00 21.29  ?  118 ASP A O   1 
ATOM   920  C  CB  . ASP A 1 118 ? 46.763 -43.186 -4.140  1.00 20.18  ?  118 ASP A CB  1 
ATOM   921  C  CG  . ASP A 1 118 ? 47.160 -42.892 -2.698  1.00 20.54  ?  118 ASP A CG  1 
ATOM   922  O  OD1 . ASP A 1 118 ? 46.575 -43.523 -1.793  1.00 19.15  ?  118 ASP A OD1 1 
ATOM   923  O  OD2 . ASP A 1 118 ? 48.058 -42.037 -2.495  1.00 20.17  -1 118 ASP A OD2 1 
ATOM   924  N  N   . PHE A 1 119 ? 48.328 -40.089 -5.144  1.00 28.10  ?  119 PHE A N   1 
ATOM   925  C  CA  . PHE A 1 119 ? 48.269 -38.667 -5.445  1.00 30.01  ?  119 PHE A CA  1 
ATOM   926  C  C   . PHE A 1 119 ? 47.436 -38.499 -6.715  1.00 31.09  ?  119 PHE A C   1 
ATOM   927  O  O   . PHE A 1 119 ? 47.629 -39.234 -7.689  1.00 33.23  ?  119 PHE A O   1 
ATOM   928  C  CB  . PHE A 1 119 ? 49.695 -38.106 -5.567  1.00 29.44  ?  119 PHE A CB  1 
ATOM   929  C  CG  . PHE A 1 119 ? 49.804 -36.654 -6.027  1.00 27.86  ?  119 PHE A CG  1 
ATOM   930  C  CD1 . PHE A 1 119 ? 49.707 -35.610 -5.115  1.00 25.22  ?  119 PHE A CD1 1 
ATOM   931  C  CD2 . PHE A 1 119 ? 50.043 -36.336 -7.362  1.00 27.29  ?  119 PHE A CD2 1 
ATOM   932  C  CE1 . PHE A 1 119 ? 49.840 -34.299 -5.518  1.00 22.67  ?  119 PHE A CE1 1 
ATOM   933  C  CE2 . PHE A 1 119 ? 50.190 -35.018 -7.755  1.00 25.27  ?  119 PHE A CE2 1 
ATOM   934  C  CZ  . PHE A 1 119 ? 50.084 -34.009 -6.829  1.00 24.08  ?  119 PHE A CZ  1 
ATOM   935  N  N   . ASP A 1 120 ? 46.490 -37.551 -6.667  1.00 29.82  ?  120 ASP A N   1 
ATOM   936  C  CA  . ASP A 1 120 ? 45.610 -37.257 -7.791  1.00 28.59  ?  120 ASP A CA  1 
ATOM   937  C  C   . ASP A 1 120 ? 46.009 -35.902 -8.382  1.00 27.89  ?  120 ASP A C   1 
ATOM   938  O  O   . ASP A 1 120 ? 45.716 -34.847 -7.826  1.00 30.06  ?  120 ASP A O   1 
ATOM   939  C  CB  . ASP A 1 120 ? 44.151 -37.323 -7.363  1.00 29.01  ?  120 ASP A CB  1 
ATOM   940  C  CG  . ASP A 1 120 ? 43.097 -37.038 -8.429  1.00 30.85  ?  120 ASP A CG  1 
ATOM   941  O  OD1 . ASP A 1 120 ? 42.019 -36.545 -8.025  1.00 31.97  ?  120 ASP A OD1 1 
ATOM   942  O  OD2 . ASP A 1 120 ? 43.332 -37.353 -9.633  1.00 26.25  -1 120 ASP A OD2 1 
ATOM   943  N  N   . PRO A 1 121 ? 46.727 -35.881 -9.520  1.00 25.12  ?  121 PRO A N   1 
ATOM   944  C  CA  . PRO A 1 121 ? 46.989 -34.638 -10.250 1.00 25.01  ?  121 PRO A CA  1 
ATOM   945  C  C   . PRO A 1 121 ? 45.837 -33.664 -10.452 1.00 26.61  ?  121 PRO A C   1 
ATOM   946  O  O   . PRO A 1 121 ? 46.101 -32.467 -10.597 1.00 24.59  ?  121 PRO A O   1 
ATOM   947  C  CB  . PRO A 1 121 ? 47.440 -35.164 -11.619 1.00 26.58  ?  121 PRO A CB  1 
ATOM   948  C  CG  . PRO A 1 121 ? 48.118 -36.480 -11.306 1.00 26.66  ?  121 PRO A CG  1 
ATOM   949  C  CD  . PRO A 1 121 ? 47.362 -37.062 -10.122 1.00 25.27  ?  121 PRO A CD  1 
ATOM   950  N  N   . LYS A 1 122 ? 44.596 -34.202 -10.507 1.00 29.87  ?  122 LYS A N   1 
ATOM   951  C  CA  . LYS A 1 122 ? 43.382 -33.446 -10.792 1.00 31.66  ?  122 LYS A CA  1 
ATOM   952  C  C   . LYS A 1 122 ? 43.264 -32.223 -9.872  1.00 33.04  ?  122 LYS A C   1 
ATOM   953  O  O   . LYS A 1 122 ? 43.166 -32.355 -8.662  1.00 33.06  ?  122 LYS A O   1 
ATOM   954  C  CB  . LYS A 1 122 ? 42.115 -34.292 -10.616 1.00 33.16  ?  122 LYS A CB  1 
ATOM   955  C  CG  . LYS A 1 122 ? 41.935 -35.512 -11.503 1.00 37.53  ?  122 LYS A CG  1 
ATOM   956  C  CD  . LYS A 1 122 ? 41.932 -35.291 -13.015 1.00 41.09  ?  122 LYS A CD  1 
ATOM   957  C  CE  . LYS A 1 122 ? 43.169 -35.750 -13.731 1.00 39.61  ?  122 LYS A CE  1 
ATOM   958  N  NZ  . LYS A 1 122 ? 42.848 -36.319 -15.042 1.00 41.07  1  122 LYS A NZ  1 
ATOM   959  N  N   . GLY A 1 123 ? 43.252 -31.020 -10.457 1.00 36.13  ?  123 GLY A N   1 
ATOM   960  C  CA  . GLY A 1 123 ? 42.966 -29.806 -9.711  1.00 38.02  ?  123 GLY A CA  1 
ATOM   961  C  C   . GLY A 1 123 ? 44.078 -29.465 -8.719  1.00 40.38  ?  123 GLY A C   1 
ATOM   962  O  O   . GLY A 1 123 ? 43.841 -28.791 -7.708  1.00 43.05  ?  123 GLY A O   1 
ATOM   963  N  N   . LYS A 1 124 ? 45.290 -29.956 -8.991  1.00 34.34  ?  124 LYS A N   1 
ATOM   964  C  CA  . LYS A 1 124 ? 46.448 -29.490 -8.253  1.00 34.14  ?  124 LYS A CA  1 
ATOM   965  C  C   . LYS A 1 124 ? 47.183 -28.496 -9.144  1.00 33.22  ?  124 LYS A C   1 
ATOM   966  O  O   . LYS A 1 124 ? 47.219 -28.648 -10.363 1.00 31.45  ?  124 LYS A O   1 
ATOM   967  C  CB  . LYS A 1 124 ? 47.373 -30.643 -7.849  1.00 36.60  ?  124 LYS A CB  1 
ATOM   968  C  CG  . LYS A 1 124 ? 46.715 -31.914 -7.282  1.00 36.37  ?  124 LYS A CG  1 
ATOM   969  C  CD  . LYS A 1 124 ? 46.438 -31.943 -5.786  1.00 33.83  ?  124 LYS A CD  1 
ATOM   970  C  CE  . LYS A 1 124 ? 45.709 -33.189 -5.379  1.00 31.83  ?  124 LYS A CE  1 
ATOM   971  N  NZ  . LYS A 1 124 ? 44.368 -33.225 -5.967  1.00 30.89  1  124 LYS A NZ  1 
ATOM   972  N  N   . SER A 1 125 ? 47.726 -27.452 -8.518  1.00 34.19  ?  125 SER A N   1 
ATOM   973  C  CA  . SER A 1 125 ? 48.493 -26.430 -9.211  1.00 33.48  ?  125 SER A CA  1 
ATOM   974  C  C   . SER A 1 125 ? 49.903 -26.944 -9.440  1.00 35.40  ?  125 SER A C   1 
ATOM   975  O  O   . SER A 1 125 ? 50.265 -27.971 -8.887  1.00 40.53  ?  125 SER A O   1 
ATOM   976  C  CB  . SER A 1 125 ? 48.491 -25.185 -8.409  1.00 32.59  ?  125 SER A CB  1 
ATOM   977  O  OG  . SER A 1 125 ? 48.135 -25.530 -7.082  1.00 32.62  ?  125 SER A OG  1 
ATOM   978  N  N   . ASP A 1 126 ? 50.691 -26.236 -10.248 1.00 37.29  ?  126 ASP A N   1 
ATOM   979  C  CA  . ASP A 1 126 ? 52.021 -26.705 -10.595 1.00 37.71  ?  126 ASP A CA  1 
ATOM   980  C  C   . ASP A 1 126 ? 52.910 -26.731 -9.351  1.00 38.67  ?  126 ASP A C   1 
ATOM   981  O  O   . ASP A 1 126 ? 53.763 -27.610 -9.235  1.00 39.17  ?  126 ASP A O   1 
ATOM   982  C  CB  . ASP A 1 126 ? 52.639 -25.886 -11.714 1.00 43.52  ?  126 ASP A CB  1 
ATOM   983  C  CG  . ASP A 1 126 ? 54.031 -26.341 -12.133 1.00 53.33  ?  126 ASP A CG  1 
ATOM   984  O  OD1 . ASP A 1 126 ? 54.190 -27.577 -12.334 1.00 59.06  ?  126 ASP A OD1 1 
ATOM   985  O  OD2 . ASP A 1 126 ? 54.944 -25.468 -12.258 1.00 48.69  -1 126 ASP A OD2 1 
ATOM   986  N  N   . SER A 1 127 ? 52.708 -25.771 -8.429  1.00 37.25  ?  127 SER A N   1 
ATOM   987  C  CA  . SER A 1 127 ? 53.433 -25.737 -7.169  1.00 34.52  ?  127 SER A CA  1 
ATOM   988  C  C   . SER A 1 127 ? 53.172 -27.032 -6.410  1.00 37.31  ?  127 SER A C   1 
ATOM   989  O  O   . SER A 1 127 ? 54.084 -27.622 -5.841  1.00 37.22  ?  127 SER A O   1 
ATOM   990  C  CB  . SER A 1 127 ? 53.061 -24.543 -6.328  1.00 35.33  ?  127 SER A CB  1 
ATOM   991  O  OG  . SER A 1 127 ? 53.917 -23.431 -6.573  1.00 35.82  ?  127 SER A OG  1 
ATOM   992  N  N   . GLU A 1 128 ? 51.914 -27.485 -6.431  1.00 40.74  ?  128 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 128 ? 51.494 -28.624 -5.622  1.00 39.19  ?  128 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 128 ? 52.135 -29.908 -6.143  1.00 35.72  ?  128 GLU A C   1 
ATOM   995  O  O   . GLU A 1 128 ? 52.721 -30.648 -5.337  1.00 33.20  ?  128 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 128 ? 49.968 -28.700 -5.531  1.00 38.22  ?  128 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 128 ? 49.379 -27.546 -4.724  1.00 37.49  ?  128 GLU A CG  1 
ATOM   998  C  CD  . GLU A 1 128 ? 47.864 -27.520 -4.660  1.00 38.02  ?  128 GLU A CD  1 
ATOM   999  O  OE1 . GLU A 1 128 ? 47.276 -26.641 -3.961  1.00 35.03  ?  128 GLU A OE1 1 
ATOM   1000 O  OE2 . GLU A 1 128 ? 47.286 -28.411 -5.325  1.00 37.19  -1 128 GLU A OE2 1 
ATOM   1001 N  N   . ILE A 1 129 ? 51.995 -30.130 -7.473  1.00 30.38  ?  129 ILE A N   1 
ATOM   1002 C  CA  . ILE A 1 129 ? 52.704 -31.170 -8.224  1.00 26.41  ?  129 ILE A CA  1 
ATOM   1003 C  C   . ILE A 1 129 ? 54.193 -31.076 -7.861  1.00 26.16  ?  129 ILE A C   1 
ATOM   1004 O  O   . ILE A 1 129 ? 54.745 -32.035 -7.329  1.00 24.08  ?  129 ILE A O   1 
ATOM   1005 C  CB  . ILE A 1 129 ? 52.499 -31.052 -9.759  1.00 24.54  ?  129 ILE A CB  1 
ATOM   1006 C  CG1 . ILE A 1 129 ? 51.029 -31.140 -10.252 1.00 23.78  ?  129 ILE A CG1 1 
ATOM   1007 C  CG2 . ILE A 1 129 ? 53.380 -32.038 -10.524 1.00 23.60  ?  129 ILE A CG2 1 
ATOM   1008 C  CD1 . ILE A 1 129 ? 50.035 -31.671 -9.239  1.00 24.48  ?  129 ILE A CD1 1 
ATOM   1009 N  N   . ARG A 1 130 ? 54.815 -29.900 -8.098  1.00 26.17  ?  130 ARG A N   1 
ATOM   1010 C  CA  . ARG A 1 130 ? 56.234 -29.664 -7.828  1.00 27.53  ?  130 ARG A CA  1 
ATOM   1011 C  C   . ARG A 1 130 ? 56.614 -30.112 -6.414  1.00 26.75  ?  130 ARG A C   1 
ATOM   1012 O  O   . ARG A 1 130 ? 57.618 -30.801 -6.237  1.00 25.26  ?  130 ARG A O   1 
ATOM   1013 C  CB  . ARG A 1 130 ? 56.610 -28.185 -8.022  1.00 27.75  ?  130 ARG A CB  1 
ATOM   1014 C  CG  . ARG A 1 130 ? 57.863 -27.761 -7.273  1.00 28.20  ?  130 ARG A CG  1 
ATOM   1015 C  CD  . ARG A 1 130 ? 58.386 -26.405 -7.680  1.00 28.16  ?  130 ARG A CD  1 
ATOM   1016 N  NE  . ARG A 1 130 ? 57.461 -25.302 -7.410  1.00 29.65  ?  130 ARG A NE  1 
ATOM   1017 C  CZ  . ARG A 1 130 ? 57.127 -24.859 -6.198  1.00 32.22  ?  130 ARG A CZ  1 
ATOM   1018 N  NH1 . ARG A 1 130 ? 57.497 -25.510 -5.106  1.00 30.76  1  130 ARG A NH1 1 
ATOM   1019 N  NH2 . ARG A 1 130 ? 56.381 -23.774 -6.079  1.00 32.93  ?  130 ARG A NH2 1 
ATOM   1020 N  N   . ARG A 1 131 ? 55.806 -29.708 -5.421  1.00 26.18  ?  131 ARG A N   1 
ATOM   1021 C  CA  . ARG A 1 131 ? 56.072 -29.994 -4.016  1.00 24.84  ?  131 ARG A CA  1 
ATOM   1022 C  C   . ARG A 1 131 ? 55.850 -31.467 -3.706  1.00 27.12  ?  131 ARG A C   1 
ATOM   1023 O  O   . ARG A 1 131 ? 56.392 -31.936 -2.701  1.00 29.81  ?  131 ARG A O   1 
ATOM   1024 C  CB  . ARG A 1 131 ? 55.164 -29.241 -3.037  1.00 22.69  ?  131 ARG A CB  1 
ATOM   1025 C  CG  . ARG A 1 131 ? 55.517 -27.771 -2.861  1.00 21.24  ?  131 ARG A CG  1 
ATOM   1026 C  CD  . ARG A 1 131 ? 54.820 -27.178 -1.671  1.00 19.98  ?  131 ARG A CD  1 
ATOM   1027 N  NE  . ARG A 1 131 ? 54.422 -25.822 -2.035  1.00 20.77  ?  131 ARG A NE  1 
ATOM   1028 C  CZ  . ARG A 1 131 ? 53.197 -25.446 -2.423  1.00 21.57  ?  131 ARG A CZ  1 
ATOM   1029 N  NH1 . ARG A 1 131 ? 52.143 -26.272 -2.369  1.00 19.63  1  131 ARG A NH1 1 
ATOM   1030 N  NH2 . ARG A 1 131 ? 53.044 -24.190 -2.820  1.00 21.35  ?  131 ARG A NH2 1 
ATOM   1031 N  N   . PHE A 1 132 ? 55.001 -32.144 -4.509  1.00 25.89  ?  132 PHE A N   1 
ATOM   1032 C  CA  . PHE A 1 132 ? 54.744 -33.567 -4.332  1.00 24.70  ?  132 PHE A CA  1 
ATOM   1033 C  C   . PHE A 1 132 ? 55.867 -34.378 -4.999  1.00 24.59  ?  132 PHE A C   1 
ATOM   1034 O  O   . PHE A 1 132 ? 56.390 -35.308 -4.394  1.00 25.39  ?  132 PHE A O   1 
ATOM   1035 C  CB  . PHE A 1 132 ? 53.359 -34.007 -4.812  1.00 23.32  ?  132 PHE A CB  1 
ATOM   1036 C  CG  . PHE A 1 132 ? 53.281 -35.523 -4.784  1.00 24.97  ?  132 PHE A CG  1 
ATOM   1037 C  CD1 . PHE A 1 132 ? 53.028 -36.192 -3.595  1.00 26.46  ?  132 PHE A CD1 1 
ATOM   1038 C  CD2 . PHE A 1 132 ? 53.536 -36.279 -5.923  1.00 26.26  ?  132 PHE A CD2 1 
ATOM   1039 C  CE1 . PHE A 1 132 ? 53.000 -37.576 -3.559  1.00 28.41  ?  132 PHE A CE1 1 
ATOM   1040 C  CE2 . PHE A 1 132 ? 53.490 -37.666 -5.888  1.00 27.02  ?  132 PHE A CE2 1 
ATOM   1041 C  CZ  . PHE A 1 132 ? 53.224 -38.309 -4.706  1.00 29.72  ?  132 PHE A CZ  1 
ATOM   1042 N  N   . CYS A 1 133 ? 56.271 -34.024 -6.224  1.00 22.93  ?  133 CYS A N   1 
ATOM   1043 C  CA  . CYS A 1 133 ? 57.360 -34.716 -6.899  1.00 22.62  ?  133 CYS A CA  1 
ATOM   1044 C  C   . CYS A 1 133 ? 58.626 -34.698 -6.043  1.00 20.83  ?  133 CYS A C   1 
ATOM   1045 O  O   . CYS A 1 133 ? 59.364 -35.696 -5.968  1.00 17.97  ?  133 CYS A O   1 
ATOM   1046 C  CB  . CYS A 1 133 ? 57.584 -34.129 -8.286  1.00 23.84  ?  133 CYS A CB  1 
ATOM   1047 S  SG  . CYS A 1 133 ? 56.159 -34.433 -9.359  1.00 29.31  ?  133 CYS A SG  1 
ATOM   1048 N  N   . VAL A 1 134 ? 58.835 -33.540 -5.400  1.00 20.57  ?  134 VAL A N   1 
ATOM   1049 C  CA  . VAL A 1 134 ? 59.963 -33.285 -4.515  1.00 20.18  ?  134 VAL A CA  1 
ATOM   1050 C  C   . VAL A 1 134 ? 59.915 -34.182 -3.288  1.00 22.25  ?  134 VAL A C   1 
ATOM   1051 O  O   . VAL A 1 134 ? 60.939 -34.737 -2.900  1.00 22.15  ?  134 VAL A O   1 
ATOM   1052 C  CB  . VAL A 1 134 ? 59.961 -31.822 -4.062  1.00 17.70  ?  134 VAL A CB  1 
ATOM   1053 C  CG1 . VAL A 1 134 ? 60.807 -31.615 -2.813  1.00 17.25  ?  134 VAL A CG1 1 
ATOM   1054 C  CG2 . VAL A 1 134 ? 60.408 -30.921 -5.196  1.00 18.08  ?  134 VAL A CG2 1 
ATOM   1055 N  N   . ALA A 1 135 ? 58.735 -34.238 -2.660  1.00 24.88  ?  135 ALA A N   1 
ATOM   1056 C  CA  . ALA A 1 135 ? 58.518 -35.009 -1.448  1.00 27.00  ?  135 ALA A CA  1 
ATOM   1057 C  C   . ALA A 1 135 ? 58.646 -36.499 -1.738  1.00 27.73  ?  135 ALA A C   1 
ATOM   1058 O  O   . ALA A 1 135 ? 59.070 -37.230 -0.854  1.00 30.65  ?  135 ALA A O   1 
ATOM   1059 C  CB  . ALA A 1 135 ? 57.160 -34.684 -0.874  1.00 27.46  ?  135 ALA A CB  1 
ATOM   1060 N  N   . PHE A 1 136 ? 58.306 -36.900 -2.977  1.00 27.17  ?  136 PHE A N   1 
ATOM   1061 C  CA  . PHE A 1 136 ? 58.194 -38.291 -3.408  1.00 27.19  ?  136 PHE A CA  1 
ATOM   1062 C  C   . PHE A 1 136 ? 59.553 -38.864 -3.783  1.00 26.05  ?  136 PHE A C   1 
ATOM   1063 O  O   . PHE A 1 136 ? 59.820 -40.034 -3.554  1.00 25.94  ?  136 PHE A O   1 
ATOM   1064 C  CB  . PHE A 1 136 ? 57.332 -38.405 -4.672  1.00 28.88  ?  136 PHE A CB  1 
ATOM   1065 C  CG  . PHE A 1 136 ? 57.303 -39.769 -5.347  1.00 28.65  ?  136 PHE A CG  1 
ATOM   1066 C  CD1 . PHE A 1 136 ? 56.616 -40.836 -4.771  1.00 32.33  ?  136 PHE A CD1 1 
ATOM   1067 C  CD2 . PHE A 1 136 ? 57.917 -39.970 -6.568  1.00 27.87  ?  136 PHE A CD2 1 
ATOM   1068 C  CE1 . PHE A 1 136 ? 56.565 -42.071 -5.392  1.00 31.49  ?  136 PHE A CE1 1 
ATOM   1069 C  CE2 . PHE A 1 136 ? 57.874 -41.209 -7.179  1.00 30.42  ?  136 PHE A CE2 1 
ATOM   1070 C  CZ  . PHE A 1 136 ? 57.194 -42.256 -6.597  1.00 31.24  ?  136 PHE A CZ  1 
ATOM   1071 N  N   . MET A 1 137 ? 60.373 -38.034 -4.427  1.00 25.57  ?  137 MET A N   1 
ATOM   1072 C  CA  . MET A 1 137 ? 61.663 -38.455 -4.938  1.00 23.65  ?  137 MET A CA  1 
ATOM   1073 C  C   . MET A 1 137 ? 62.666 -38.527 -3.804  1.00 22.74  ?  137 MET A C   1 
ATOM   1074 O  O   . MET A 1 137 ? 63.673 -39.173 -4.004  1.00 24.67  ?  137 MET A O   1 
ATOM   1075 C  CB  . MET A 1 137 ? 62.196 -37.468 -5.985  1.00 24.11  ?  137 MET A CB  1 
ATOM   1076 C  CG  . MET A 1 137 ? 63.609 -37.757 -6.488  1.00 23.89  ?  137 MET A CG  1 
ATOM   1077 S  SD  . MET A 1 137 ? 63.830 -39.453 -7.060  1.00 23.01  ?  137 MET A SD  1 
ATOM   1078 C  CE  . MET A 1 137 ? 63.202 -39.255 -8.732  1.00 22.70  ?  137 MET A CE  1 
ATOM   1079 N  N   . THR A 1 138 ? 62.395 -37.859 -2.665  1.00 22.59  ?  138 THR A N   1 
ATOM   1080 C  CA  . THR A 1 138 ? 63.322 -37.785 -1.535  1.00 20.51  ?  138 THR A CA  1 
ATOM   1081 C  C   . THR A 1 138 ? 63.415 -39.157 -0.880  1.00 19.55  ?  138 THR A C   1 
ATOM   1082 O  O   . THR A 1 138 ? 64.439 -39.489 -0.304  1.00 16.55  ?  138 THR A O   1 
ATOM   1083 C  CB  . THR A 1 138 ? 62.917 -36.710 -0.518  1.00 19.81  ?  138 THR A CB  1 
ATOM   1084 O  OG1 . THR A 1 138 ? 63.184 -35.410 -1.031  1.00 19.33  ?  138 THR A OG1 1 
ATOM   1085 C  CG2 . THR A 1 138 ? 63.774 -36.712 0.728   1.00 19.88  ?  138 THR A CG2 1 
ATOM   1086 N  N   . GLU A 1 139 ? 62.350 -39.961 -0.979  1.00 22.05  ?  139 GLU A N   1 
ATOM   1087 C  CA  . GLU A 1 139 ? 62.412 -41.311 -0.447  1.00 23.61  ?  139 GLU A CA  1 
ATOM   1088 C  C   . GLU A 1 139 ? 62.815 -42.281 -1.551  1.00 25.30  ?  139 GLU A C   1 
ATOM   1089 O  O   . GLU A 1 139 ? 63.705 -43.096 -1.338  1.00 30.75  ?  139 GLU A O   1 
ATOM   1090 C  CB  . GLU A 1 139 ? 61.128 -41.695 0.276   1.00 24.74  ?  139 GLU A CB  1 
ATOM   1091 C  CG  . GLU A 1 139 ? 61.241 -43.056 0.954   1.00 29.20  ?  139 GLU A CG  1 
ATOM   1092 C  CD  . GLU A 1 139 ? 62.541 -43.446 1.647   1.00 29.93  ?  139 GLU A CD  1 
ATOM   1093 O  OE1 . GLU A 1 139 ? 63.146 -44.524 1.346   1.00 28.84  ?  139 GLU A OE1 1 
ATOM   1094 O  OE2 . GLU A 1 139 ? 62.926 -42.649 2.532   1.00 29.81  -1 139 GLU A OE2 1 
ATOM   1095 N  N   . LEU A 1 140 ? 62.181 -42.176 -2.724  1.00 25.08  ?  140 LEU A N   1 
ATOM   1096 C  CA  . LEU A 1 140 ? 62.538 -42.978 -3.886  1.00 25.72  ?  140 LEU A CA  1 
ATOM   1097 C  C   . LEU A 1 140 ? 64.030 -42.881 -4.180  1.00 25.57  ?  140 LEU A C   1 
ATOM   1098 O  O   . LEU A 1 140 ? 64.632 -43.830 -4.669  1.00 26.26  ?  140 LEU A O   1 
ATOM   1099 C  CB  . LEU A 1 140 ? 61.761 -42.541 -5.125  1.00 27.47  ?  140 LEU A CB  1 
ATOM   1100 C  CG  . LEU A 1 140 ? 61.906 -43.410 -6.378  1.00 27.71  ?  140 LEU A CG  1 
ATOM   1101 C  CD1 . LEU A 1 140 ? 61.654 -44.872 -6.037  1.00 31.61  ?  140 LEU A CD1 1 
ATOM   1102 C  CD2 . LEU A 1 140 ? 60.932 -42.986 -7.471  1.00 26.22  ?  140 LEU A CD2 1 
ATOM   1103 N  N   . CYS A 1 141 ? 64.622 -41.718 -3.922  1.00 25.76  ?  141 CYS A N   1 
ATOM   1104 C  CA  . CYS A 1 141 ? 65.944 -41.452 -4.454  1.00 27.94  ?  141 CYS A CA  1 
ATOM   1105 C  C   . CYS A 1 141 ? 66.864 -42.629 -4.149  1.00 28.15  ?  141 CYS A C   1 
ATOM   1106 O  O   . CYS A 1 141 ? 67.586 -43.086 -5.016  1.00 29.71  ?  141 CYS A O   1 
ATOM   1107 C  CB  . CYS A 1 141 ? 66.520 -40.154 -3.909  1.00 29.30  ?  141 CYS A CB  1 
ATOM   1108 S  SG  . CYS A 1 141 ? 68.291 -39.991 -4.232  1.00 35.10  ?  141 CYS A SG  1 
ATOM   1109 N  N   . ARG A 1 142 ? 66.794 -43.142 -2.920  1.00 29.06  ?  142 ARG A N   1 
ATOM   1110 C  CA  . ARG A 1 142 ? 67.799 -44.056 -2.401  1.00 27.91  ?  142 ARG A CA  1 
ATOM   1111 C  C   . ARG A 1 142 ? 67.690 -45.441 -3.034  1.00 26.77  ?  142 ARG A C   1 
ATOM   1112 O  O   . ARG A 1 142 ? 68.593 -46.247 -2.862  1.00 25.73  ?  142 ARG A O   1 
ATOM   1113 C  CB  . ARG A 1 142 ? 67.674 -44.202 -0.877  1.00 28.76  ?  142 ARG A CB  1 
ATOM   1114 C  CG  . ARG A 1 142 ? 66.539 -45.095 -0.390  1.00 29.06  ?  142 ARG A CG  1 
ATOM   1115 C  CD  . ARG A 1 142 ? 66.448 -45.119 1.130   1.00 29.03  ?  142 ARG A CD  1 
ATOM   1116 N  NE  . ARG A 1 142 ? 65.826 -43.893 1.649   1.00 26.93  ?  142 ARG A NE  1 
ATOM   1117 C  CZ  . ARG A 1 142 ? 66.467 -42.884 2.218   1.00 25.14  ?  142 ARG A CZ  1 
ATOM   1118 N  NH1 . ARG A 1 142 ? 67.794 -42.917 2.336   1.00 25.89  1  142 ARG A NH1 1 
ATOM   1119 N  NH2 . ARG A 1 142 ? 65.780 -41.832 2.625   1.00 21.57  ?  142 ARG A NH2 1 
ATOM   1120 N  N   . HIS A 1 143 ? 66.599 -45.724 -3.750  1.00 25.44  ?  143 HIS A N   1 
ATOM   1121 C  CA  . HIS A 1 143 ? 66.355 -47.069 -4.232  1.00 24.87  ?  143 HIS A CA  1 
ATOM   1122 C  C   . HIS A 1 143 ? 66.529 -47.170 -5.744  1.00 25.41  ?  143 HIS A C   1 
ATOM   1123 O  O   . HIS A 1 143 ? 66.338 -48.259 -6.272  1.00 32.50  ?  143 HIS A O   1 
ATOM   1124 C  CB  . HIS A 1 143 ? 64.932 -47.500 -3.881  1.00 25.94  ?  143 HIS A CB  1 
ATOM   1125 C  CG  . HIS A 1 143 ? 64.517 -47.184 -2.472  1.00 29.53  ?  143 HIS A CG  1 
ATOM   1126 N  ND1 . HIS A 1 143 ? 64.954 -47.915 -1.386  1.00 28.92  ?  143 HIS A ND1 1 
ATOM   1127 C  CD2 . HIS A 1 143 ? 63.695 -46.231 -1.975  1.00 29.97  ?  143 HIS A CD2 1 
ATOM   1128 C  CE1 . HIS A 1 143 ? 64.412 -47.422 -0.285  1.00 31.32  ?  143 HIS A CE1 1 
ATOM   1129 N  NE2 . HIS A 1 143 ? 63.648 -46.390 -0.614  1.00 31.40  ?  143 HIS A NE2 1 
ATOM   1130 N  N   . ILE A 1 144 ? 66.833 -46.060 -6.439  1.00 21.03  ?  144 ILE A N   1 
ATOM   1131 C  CA  . ILE A 1 144 ? 66.901 -46.046 -7.898  1.00 19.56  ?  144 ILE A CA  1 
ATOM   1132 C  C   . ILE A 1 144 ? 68.264 -45.497 -8.338  1.00 19.60  ?  144 ILE A C   1 
ATOM   1133 O  O   . ILE A 1 144 ? 69.006 -44.933 -7.523  1.00 16.65  ?  144 ILE A O   1 
ATOM   1134 C  CB  . ILE A 1 144 ? 65.756 -45.229 -8.532  1.00 19.24  ?  144 ILE A CB  1 
ATOM   1135 C  CG1 . ILE A 1 144 ? 65.873 -43.734 -8.209  1.00 21.09  ?  144 ILE A CG1 1 
ATOM   1136 C  CG2 . ILE A 1 144 ? 64.395 -45.773 -8.133  1.00 18.98  ?  144 ILE A CG2 1 
ATOM   1137 C  CD1 . ILE A 1 144 ? 64.883 -42.843 -8.929  1.00 21.32  ?  144 ILE A CD1 1 
ATOM   1138 N  N   . GLY A 1 145 ? 68.559 -45.646 -9.646  1.00 19.40  ?  145 GLY A N   1 
ATOM   1139 C  CA  . GLY A 1 145 ? 69.803 -45.174 -10.246 1.00 21.06  ?  145 GLY A CA  1 
ATOM   1140 C  C   . GLY A 1 145 ? 69.982 -45.683 -11.682 1.00 22.10  ?  145 GLY A C   1 
ATOM   1141 O  O   . GLY A 1 145 ? 69.273 -46.590 -12.132 1.00 20.73  ?  145 GLY A O   1 
ATOM   1142 N  N   . ALA A 1 146 ? 70.955 -45.099 -12.384 1.00 21.69  ?  146 ALA A N   1 
ATOM   1143 C  CA  . ALA A 1 146 ? 71.275 -45.463 -13.754 1.00 25.44  ?  146 ALA A CA  1 
ATOM   1144 C  C   . ALA A 1 146 ? 71.533 -46.961 -13.941 1.00 28.43  ?  146 ALA A C   1 
ATOM   1145 O  O   . ALA A 1 146 ? 71.374 -47.477 -15.053 1.00 32.82  ?  146 ALA A O   1 
ATOM   1146 C  CB  . ALA A 1 146 ? 72.474 -44.663 -14.198 1.00 26.96  ?  146 ALA A CB  1 
ATOM   1147 N  N   . ASP A 1 147 ? 71.959 -47.661 -12.883 1.00 26.78  ?  147 ASP A N   1 
ATOM   1148 C  CA  . ASP A 1 147 ? 72.352 -49.057 -13.023 1.00 27.25  ?  147 ASP A CA  1 
ATOM   1149 C  C   . ASP A 1 147 ? 71.500 -49.968 -12.138 1.00 27.81  ?  147 ASP A C   1 
ATOM   1150 O  O   . ASP A 1 147 ? 71.726 -51.177 -12.132 1.00 34.60  ?  147 ASP A O   1 
ATOM   1151 C  CB  . ASP A 1 147 ? 73.836 -49.252 -12.728 1.00 27.93  ?  147 ASP A CB  1 
ATOM   1152 C  CG  . ASP A 1 147 ? 74.837 -48.644 -13.712 1.00 28.46  ?  147 ASP A CG  1 
ATOM   1153 O  OD1 . ASP A 1 147 ? 74.473 -48.425 -14.912 1.00 30.06  ?  147 ASP A OD1 1 
ATOM   1154 O  OD2 . ASP A 1 147 ? 75.983 -48.384 -13.274 1.00 25.07  -1 147 ASP A OD2 1 
ATOM   1155 N  N   . THR A 1 148 ? 70.515 -49.384 -11.433 1.00 23.38  ?  148 THR A N   1 
ATOM   1156 C  CA  . THR A 1 148 ? 69.676 -50.046 -10.444 1.00 19.35  ?  148 THR A CA  1 
ATOM   1157 C  C   . THR A 1 148 ? 68.233 -49.995 -10.917 1.00 18.53  ?  148 THR A C   1 
ATOM   1158 O  O   . THR A 1 148 ? 67.602 -51.018 -10.989 1.00 18.52  ?  148 THR A O   1 
ATOM   1159 C  CB  . THR A 1 148 ? 69.800 -49.341 -9.090  1.00 18.29  ?  148 THR A CB  1 
ATOM   1160 O  OG1 . THR A 1 148 ? 71.038 -49.765 -8.550  1.00 21.22  ?  148 THR A OG1 1 
ATOM   1161 C  CG2 . THR A 1 148 ? 68.771 -49.762 -8.069  1.00 17.10  ?  148 THR A CG2 1 
ATOM   1162 N  N   . ASP A 1 149 ? 67.686 -48.791 -11.145 1.00 20.47  ?  149 ASP A N   1 
ATOM   1163 C  CA  . ASP A 1 149 ? 66.287 -48.601 -11.535 1.00 20.76  ?  149 ASP A CA  1 
ATOM   1164 C  C   . ASP A 1 149 ? 66.175 -47.273 -12.299 1.00 21.94  ?  149 ASP A C   1 
ATOM   1165 O  O   . ASP A 1 149 ? 66.588 -46.242 -11.779 1.00 23.17  ?  149 ASP A O   1 
ATOM   1166 C  CB  . ASP A 1 149 ? 65.333 -48.708 -10.344 1.00 19.59  ?  149 ASP A CB  1 
ATOM   1167 C  CG  . ASP A 1 149 ? 63.837 -48.798 -10.664 1.00 20.30  ?  149 ASP A CG  1 
ATOM   1168 O  OD1 . ASP A 1 149 ? 63.490 -48.746 -11.864 1.00 20.68  ?  149 ASP A OD1 1 
ATOM   1169 O  OD2 . ASP A 1 149 ? 62.999 -48.926 -9.716  1.00 19.64  -1 149 ASP A OD2 1 
ATOM   1170 N  N   . VAL A 1 150 ? 65.653 -47.301 -13.537 1.00 22.20  ?  150 VAL A N   1 
ATOM   1171 C  CA  . VAL A 1 150 ? 65.452 -46.086 -14.320 1.00 24.66  ?  150 VAL A CA  1 
ATOM   1172 C  C   . VAL A 1 150 ? 63.956 -45.884 -14.590 1.00 24.27  ?  150 VAL A C   1 
ATOM   1173 O  O   . VAL A 1 150 ? 63.430 -46.356 -15.591 1.00 22.66  ?  150 VAL A O   1 
ATOM   1174 C  CB  . VAL A 1 150 ? 66.263 -46.122 -15.630 1.00 25.00  ?  150 VAL A CB  1 
ATOM   1175 C  CG1 . VAL A 1 150 ? 66.047 -44.863 -16.454 1.00 24.32  ?  150 VAL A CG1 1 
ATOM   1176 C  CG2 . VAL A 1 150 ? 67.748 -46.326 -15.369 1.00 25.76  ?  150 VAL A CG2 1 
ATOM   1177 N  N   . PRO A 1 151 ? 63.211 -45.194 -13.698 1.00 25.99  ?  151 PRO A N   1 
ATOM   1178 C  CA  . PRO A 1 151 ? 61.780 -44.944 -13.893 1.00 25.55  ?  151 PRO A CA  1 
ATOM   1179 C  C   . PRO A 1 151 ? 61.457 -44.010 -15.056 1.00 22.81  ?  151 PRO A C   1 
ATOM   1180 O  O   . PRO A 1 151 ? 62.344 -43.421 -15.653 1.00 23.87  ?  151 PRO A O   1 
ATOM   1181 C  CB  . PRO A 1 151 ? 61.291 -44.343 -12.553 1.00 26.11  ?  151 PRO A CB  1 
ATOM   1182 C  CG  . PRO A 1 151 ? 62.389 -44.663 -11.578 1.00 28.72  ?  151 PRO A CG  1 
ATOM   1183 C  CD  . PRO A 1 151 ? 63.682 -44.688 -12.400 1.00 29.19  ?  151 PRO A CD  1 
ATOM   1184 N  N   . ALA A 1 152 ? 60.162 -43.885 -15.348 1.00 20.22  ?  152 ALA A N   1 
ATOM   1185 C  CA  . ALA A 1 152 ? 59.686 -43.002 -16.386 1.00 21.23  ?  152 ALA A CA  1 
ATOM   1186 C  C   . ALA A 1 152 ? 58.294 -42.452 -16.049 1.00 20.62  ?  152 ALA A C   1 
ATOM   1187 O  O   . ALA A 1 152 ? 57.910 -42.363 -14.877 1.00 19.02  ?  152 ALA A O   1 
ATOM   1188 C  CB  . ALA A 1 152 ? 59.702 -43.767 -17.680 1.00 22.64  ?  152 ALA A CB  1 
ATOM   1189 N  N   . GLY A 1 153 ? 57.575 -42.032 -17.103 1.00 20.39  ?  153 GLY A N   1 
ATOM   1190 C  CA  . GLY A 1 153 ? 56.254 -41.440 -16.992 1.00 19.89  ?  153 GLY A CA  1 
ATOM   1191 C  C   . GLY A 1 153 ? 55.193 -42.491 -17.235 1.00 19.87  ?  153 GLY A C   1 
ATOM   1192 O  O   . GLY A 1 153 ? 55.542 -43.633 -17.538 1.00 21.97  ?  153 GLY A O   1 
ATOM   1193 N  N   . ASP A 1 154 ? 53.931 -42.070 -17.079 1.00 20.95  ?  154 ASP A N   1 
ATOM   1194 C  CA  . ASP A 1 154 ? 52.741 -42.905 -17.210 1.00 23.18  ?  154 ASP A CA  1 
ATOM   1195 C  C   . ASP A 1 154 ? 51.550 -42.030 -16.810 1.00 20.49  ?  154 ASP A C   1 
ATOM   1196 O  O   . ASP A 1 154 ? 51.649 -40.816 -16.848 1.00 17.66  ?  154 ASP A O   1 
ATOM   1197 C  CB  . ASP A 1 154 ? 52.856 -44.208 -16.418 1.00 28.75  ?  154 ASP A CB  1 
ATOM   1198 C  CG  . ASP A 1 154 ? 51.791 -45.270 -16.695 1.00 36.01  ?  154 ASP A CG  1 
ATOM   1199 O  OD1 . ASP A 1 154 ? 51.151 -45.194 -17.769 1.00 45.12  ?  154 ASP A OD1 1 
ATOM   1200 O  OD2 . ASP A 1 154 ? 51.549 -46.141 -15.815 1.00 36.31  -1 154 ASP A OD2 1 
ATOM   1201 N  N   . ILE A 1 155 ? 50.416 -42.626 -16.435 1.00 20.79  ?  155 ILE A N   1 
ATOM   1202 C  CA  . ILE A 1 155 ? 49.249 -41.851 -16.051 1.00 21.69  ?  155 ILE A CA  1 
ATOM   1203 C  C   . ILE A 1 155 ? 49.679 -40.972 -14.875 1.00 21.34  ?  155 ILE A C   1 
ATOM   1204 O  O   . ILE A 1 155 ? 50.297 -41.463 -13.938 1.00 20.45  ?  155 ILE A O   1 
ATOM   1205 C  CB  . ILE A 1 155 ? 48.040 -42.794 -15.796 1.00 20.18  ?  155 ILE A CB  1 
ATOM   1206 C  CG1 . ILE A 1 155 ? 47.619 -43.473 -17.090 1.00 19.65  ?  155 ILE A CG1 1 
ATOM   1207 C  CG2 . ILE A 1 155 ? 46.839 -42.088 -15.153 1.00 20.12  ?  155 ILE A CG2 1 
ATOM   1208 C  CD1 . ILE A 1 155 ? 46.345 -44.307 -16.985 1.00 20.83  ?  155 ILE A CD1 1 
ATOM   1209 N  N   . GLY A 1 156 ? 49.449 -39.657 -14.993 1.00 24.90  ?  156 GLY A N   1 
ATOM   1210 C  CA  . GLY A 1 156 ? 49.716 -38.685 -13.929 1.00 28.88  ?  156 GLY A CA  1 
ATOM   1211 C  C   . GLY A 1 156 ? 51.171 -38.194 -13.860 1.00 31.53  ?  156 GLY A C   1 
ATOM   1212 O  O   . GLY A 1 156 ? 51.547 -37.422 -12.975 1.00 35.17  ?  156 GLY A O   1 
ATOM   1213 N  N   . VAL A 1 157 ? 52.016 -38.651 -14.785 1.00 30.61  ?  157 VAL A N   1 
ATOM   1214 C  CA  . VAL A 1 157 ? 53.441 -38.406 -14.688 1.00 29.32  ?  157 VAL A CA  1 
ATOM   1215 C  C   . VAL A 1 157 ? 53.952 -38.214 -16.098 1.00 27.51  ?  157 VAL A C   1 
ATOM   1216 O  O   . VAL A 1 157 ? 54.229 -39.208 -16.764 1.00 22.17  ?  157 VAL A O   1 
ATOM   1217 C  CB  . VAL A 1 157 ? 54.203 -39.562 -14.012 1.00 31.84  ?  157 VAL A CB  1 
ATOM   1218 C  CG1 . VAL A 1 157 ? 55.705 -39.302 -13.934 1.00 32.45  ?  157 VAL A CG1 1 
ATOM   1219 C  CG2 . VAL A 1 157 ? 53.649 -39.879 -12.629 1.00 33.49  ?  157 VAL A CG2 1 
ATOM   1220 N  N   . THR A 1 158 ? 54.061 -36.941 -16.509 1.00 29.60  ?  158 THR A N   1 
ATOM   1221 C  CA  . THR A 1 158 ? 54.529 -36.580 -17.837 1.00 30.42  ?  158 THR A CA  1 
ATOM   1222 C  C   . THR A 1 158 ? 55.732 -35.641 -17.726 1.00 30.34  ?  158 THR A C   1 
ATOM   1223 O  O   . THR A 1 158 ? 56.296 -35.485 -16.646 1.00 38.13  ?  158 THR A O   1 
ATOM   1224 C  CB  . THR A 1 158 ? 53.355 -35.953 -18.570 1.00 33.01  ?  158 THR A CB  1 
ATOM   1225 O  OG1 . THR A 1 158 ? 53.920 -35.787 -19.861 1.00 44.58  ?  158 THR A OG1 1 
ATOM   1226 C  CG2 . THR A 1 158 ? 52.904 -34.628 -17.986 1.00 32.67  ?  158 THR A CG2 1 
ATOM   1227 N  N   . GLY A 1 159 ? 56.117 -35.003 -18.835 1.00 27.27  ?  159 GLY A N   1 
ATOM   1228 C  CA  . GLY A 1 159 ? 57.358 -34.248 -18.927 1.00 27.00  ?  159 GLY A CA  1 
ATOM   1229 C  C   . GLY A 1 159 ? 57.568 -33.293 -17.753 1.00 28.23  ?  159 GLY A C   1 
ATOM   1230 O  O   . GLY A 1 159 ? 58.658 -33.248 -17.203 1.00 32.80  ?  159 GLY A O   1 
ATOM   1231 N  N   . ARG A 1 160 ? 56.528 -32.541 -17.375 1.00 30.97  ?  160 ARG A N   1 
ATOM   1232 C  CA  . ARG A 1 160 ? 56.556 -31.613 -16.244 1.00 33.78  ?  160 ARG A CA  1 
ATOM   1233 C  C   . ARG A 1 160 ? 57.027 -32.333 -14.970 1.00 33.22  ?  160 ARG A C   1 
ATOM   1234 O  O   . ARG A 1 160 ? 57.952 -31.862 -14.300 1.00 31.37  ?  160 ARG A O   1 
ATOM   1235 C  CB  . ARG A 1 160 ? 55.184 -30.905 -16.165 1.00 36.73  ?  160 ARG A CB  1 
ATOM   1236 C  CG  . ARG A 1 160 ? 54.720 -30.266 -14.855 1.00 40.98  ?  160 ARG A CG  1 
ATOM   1237 C  CD  . ARG A 1 160 ? 53.186 -30.043 -14.751 1.00 42.48  ?  160 ARG A CD  1 
ATOM   1238 N  NE  . ARG A 1 160 ? 52.460 -31.314 -14.941 1.00 50.30  ?  160 ARG A NE  1 
ATOM   1239 C  CZ  . ARG A 1 160 ? 51.223 -31.529 -15.417 1.00 49.04  ?  160 ARG A CZ  1 
ATOM   1240 N  NH1 . ARG A 1 160 ? 50.407 -30.512 -15.648 1.00 54.04  1  160 ARG A NH1 1 
ATOM   1241 N  NH2 . ARG A 1 160 ? 50.810 -32.767 -15.673 1.00 42.66  ?  160 ARG A NH2 1 
ATOM   1242 N  N   . GLU A 1 161 ? 56.413 -33.490 -14.654 1.00 33.00  ?  161 GLU A N   1 
ATOM   1243 C  CA  . GLU A 1 161 ? 56.723 -34.244 -13.441 1.00 32.31  ?  161 GLU A CA  1 
ATOM   1244 C  C   . GLU A 1 161 ? 58.129 -34.847 -13.496 1.00 33.63  ?  161 GLU A C   1 
ATOM   1245 O  O   . GLU A 1 161 ? 58.818 -34.831 -12.477 1.00 38.42  ?  161 GLU A O   1 
ATOM   1246 C  CB  . GLU A 1 161 ? 55.734 -35.365 -13.115 1.00 31.00  ?  161 GLU A CB  1 
ATOM   1247 C  CG  . GLU A 1 161 ? 54.338 -34.858 -12.746 1.00 32.39  ?  161 GLU A CG  1 
ATOM   1248 C  CD  . GLU A 1 161 ? 53.441 -34.432 -13.905 1.00 30.19  ?  161 GLU A CD  1 
ATOM   1249 O  OE1 . GLU A 1 161 ? 52.492 -33.702 -13.585 1.00 25.64  ?  161 GLU A OE1 1 
ATOM   1250 O  OE2 . GLU A 1 161 ? 53.656 -34.809 -15.090 1.00 27.62  -1 161 GLU A OE2 1 
ATOM   1251 N  N   . ILE A 1 162 ? 58.551 -35.384 -14.658 1.00 30.61  ?  162 ILE A N   1 
ATOM   1252 C  CA  . ILE A 1 162 ? 59.858 -36.031 -14.806 1.00 26.72  ?  162 ILE A CA  1 
ATOM   1253 C  C   . ILE A 1 162 ? 60.974 -34.997 -14.599 1.00 26.34  ?  162 ILE A C   1 
ATOM   1254 O  O   . ILE A 1 162 ? 62.033 -35.315 -14.052 1.00 22.31  ?  162 ILE A O   1 
ATOM   1255 C  CB  . ILE A 1 162 ? 59.948 -36.777 -16.156 1.00 23.62  ?  162 ILE A CB  1 
ATOM   1256 C  CG1 . ILE A 1 162 ? 59.262 -38.129 -16.075 1.00 24.22  ?  162 ILE A CG1 1 
ATOM   1257 C  CG2 . ILE A 1 162 ? 61.383 -36.957 -16.631 1.00 23.47  ?  162 ILE A CG2 1 
ATOM   1258 C  CD1 . ILE A 1 162 ? 58.212 -38.340 -17.155 1.00 23.96  ?  162 ILE A CD1 1 
ATOM   1259 N  N   . GLY A 1 163 ? 60.715 -33.749 -15.022 1.00 26.99  ?  163 GLY A N   1 
ATOM   1260 C  CA  . GLY A 1 163 ? 61.588 -32.625 -14.730 1.00 25.09  ?  163 GLY A CA  1 
ATOM   1261 C  C   . GLY A 1 163 ? 61.779 -32.459 -13.228 1.00 25.09  ?  163 GLY A C   1 
ATOM   1262 O  O   . GLY A 1 163 ? 62.911 -32.401 -12.739 1.00 20.99  ?  163 GLY A O   1 
ATOM   1263 N  N   . TYR A 1 164 ? 60.649 -32.388 -12.509 1.00 26.40  ?  164 TYR A N   1 
ATOM   1264 C  CA  . TYR A 1 164 ? 60.698 -32.127 -11.082 1.00 25.22  ?  164 TYR A CA  1 
ATOM   1265 C  C   . TYR A 1 164 ? 61.325 -33.292 -10.331 1.00 24.99  ?  164 TYR A C   1 
ATOM   1266 O  O   . TYR A 1 164 ? 61.982 -33.073 -9.331  1.00 29.96  ?  164 TYR A O   1 
ATOM   1267 C  CB  . TYR A 1 164 ? 59.308 -31.911 -10.524 1.00 24.68  ?  164 TYR A CB  1 
ATOM   1268 C  CG  . TYR A 1 164 ? 58.594 -30.665 -11.001 1.00 24.04  ?  164 TYR A CG  1 
ATOM   1269 C  CD1 . TYR A 1 164 ? 57.216 -30.707 -11.233 1.00 23.71  ?  164 TYR A CD1 1 
ATOM   1270 C  CD2 . TYR A 1 164 ? 59.252 -29.449 -11.125 1.00 23.84  ?  164 TYR A CD2 1 
ATOM   1271 C  CE1 . TYR A 1 164 ? 56.520 -29.591 -11.646 1.00 22.04  ?  164 TYR A CE1 1 
ATOM   1272 C  CE2 . TYR A 1 164 ? 58.553 -28.313 -11.517 1.00 24.09  ?  164 TYR A CE2 1 
ATOM   1273 C  CZ  . TYR A 1 164 ? 57.191 -28.395 -11.770 1.00 21.99  ?  164 TYR A CZ  1 
ATOM   1274 O  OH  . TYR A 1 164 ? 56.455 -27.327 -12.133 1.00 23.30  ?  164 TYR A OH  1 
ATOM   1275 N  N   . LEU A 1 165 ? 61.096 -34.519 -10.798 1.00 26.11  ?  165 LEU A N   1 
ATOM   1276 C  CA  . LEU A 1 165 ? 61.758 -35.695 -10.244 1.00 25.96  ?  165 LEU A CA  1 
ATOM   1277 C  C   . LEU A 1 165 ? 63.261 -35.595 -10.540 1.00 25.51  ?  165 LEU A C   1 
ATOM   1278 O  O   . LEU A 1 165 ? 64.088 -35.740 -9.659  1.00 27.04  ?  165 LEU A O   1 
ATOM   1279 C  CB  . LEU A 1 165 ? 61.107 -36.968 -10.796 1.00 25.27  ?  165 LEU A CB  1 
ATOM   1280 C  CG  . LEU A 1 165 ? 59.598 -37.107 -10.524 1.00 28.18  ?  165 LEU A CG  1 
ATOM   1281 C  CD1 . LEU A 1 165 ? 58.949 -38.149 -11.421 1.00 29.56  ?  165 LEU A CD1 1 
ATOM   1282 C  CD2 . LEU A 1 165 ? 59.277 -37.434 -9.071  1.00 29.08  ?  165 LEU A CD2 1 
ATOM   1283 N  N   . PHE A 1 166 ? 63.636 -35.240 -11.763 1.00 24.13  ?  166 PHE A N   1 
ATOM   1284 C  CA  . PHE A 1 166 ? 65.039 -35.249 -12.135 1.00 24.00  ?  166 PHE A CA  1 
ATOM   1285 C  C   . PHE A 1 166 ? 65.842 -34.229 -11.327 1.00 25.94  ?  166 PHE A C   1 
ATOM   1286 O  O   . PHE A 1 166 ? 66.972 -34.503 -10.900 1.00 23.82  ?  166 PHE A O   1 
ATOM   1287 C  CB  . PHE A 1 166 ? 65.221 -34.950 -13.622 1.00 21.88  ?  166 PHE A CB  1 
ATOM   1288 C  CG  . PHE A 1 166 ? 66.666 -35.175 -14.038 1.00 22.07  ?  166 PHE A CG  1 
ATOM   1289 C  CD1 . PHE A 1 166 ? 67.166 -36.460 -14.205 1.00 21.08  ?  166 PHE A CD1 1 
ATOM   1290 C  CD2 . PHE A 1 166 ? 67.531 -34.098 -14.203 1.00 22.98  ?  166 PHE A CD2 1 
ATOM   1291 C  CE1 . PHE A 1 166 ? 68.489 -36.652 -14.578 1.00 22.50  ?  166 PHE A CE1 1 
ATOM   1292 C  CE2 . PHE A 1 166 ? 68.855 -34.294 -14.551 1.00 21.85  ?  166 PHE A CE2 1 
ATOM   1293 C  CZ  . PHE A 1 166 ? 69.331 -35.571 -14.750 1.00 22.45  ?  166 PHE A CZ  1 
ATOM   1294 N  N   . GLY A 1 167 ? 65.252 -33.034 -11.187 1.00 28.51  ?  167 GLY A N   1 
ATOM   1295 C  CA  . GLY A 1 167 ? 65.794 -31.961 -10.370 1.00 27.18  ?  167 GLY A CA  1 
ATOM   1296 C  C   . GLY A 1 167 ? 66.050 -32.401 -8.932  1.00 25.74  ?  167 GLY A C   1 
ATOM   1297 O  O   . GLY A 1 167 ? 67.129 -32.161 -8.426  1.00 30.66  ?  167 GLY A O   1 
ATOM   1298 N  N   . GLN A 1 168 ? 65.095 -33.075 -8.286  1.00 24.18  ?  168 GLN A N   1 
ATOM   1299 C  CA  . GLN A 1 168 ? 65.260 -33.444 -6.882  1.00 26.49  ?  168 GLN A CA  1 
ATOM   1300 C  C   . GLN A 1 168 ? 66.316 -34.537 -6.679  1.00 28.83  ?  168 GLN A C   1 
ATOM   1301 O  O   . GLN A 1 168 ? 67.086 -34.454 -5.716  1.00 28.45  ?  168 GLN A O   1 
ATOM   1302 C  CB  . GLN A 1 168 ? 63.938 -33.862 -6.241  1.00 25.14  ?  168 GLN A CB  1 
ATOM   1303 C  CG  . GLN A 1 168 ? 64.018 -34.136 -4.738  1.00 23.87  ?  168 GLN A CG  1 
ATOM   1304 C  CD  . GLN A 1 168 ? 64.401 -32.943 -3.884  1.00 20.26  ?  168 GLN A CD  1 
ATOM   1305 O  OE1 . GLN A 1 168 ? 64.725 -31.865 -4.380  1.00 16.37  ?  168 GLN A OE1 1 
ATOM   1306 N  NE2 . GLN A 1 168 ? 64.361 -33.131 -2.571  1.00 19.58  ?  168 GLN A NE2 1 
ATOM   1307 N  N   . TYR A 1 169 ? 66.292 -35.563 -7.552  1.00 29.46  ?  169 TYR A N   1 
ATOM   1308 C  CA  . TYR A 1 169 ? 67.266 -36.642 -7.570  1.00 29.72  ?  169 TYR A CA  1 
ATOM   1309 C  C   . TYR A 1 169 ? 68.667 -36.047 -7.629  1.00 33.31  ?  169 TYR A C   1 
ATOM   1310 O  O   . TYR A 1 169 ? 69.478 -36.281 -6.725  1.00 31.95  ?  169 TYR A O   1 
ATOM   1311 C  CB  . TYR A 1 169 ? 67.066 -37.599 -8.751  1.00 27.95  ?  169 TYR A CB  1 
ATOM   1312 C  CG  . TYR A 1 169 ? 67.996 -38.808 -8.759  1.00 25.71  ?  169 TYR A CG  1 
ATOM   1313 C  CD1 . TYR A 1 169 ? 67.697 -39.939 -8.009  1.00 24.29  ?  169 TYR A CD1 1 
ATOM   1314 C  CD2 . TYR A 1 169 ? 69.172 -38.825 -9.508  1.00 25.50  ?  169 TYR A CD2 1 
ATOM   1315 C  CE1 . TYR A 1 169 ? 68.522 -41.052 -8.005  1.00 22.73  ?  169 TYR A CE1 1 
ATOM   1316 C  CE2 . TYR A 1 169 ? 70.001 -39.941 -9.535  1.00 24.37  ?  169 TYR A CE2 1 
ATOM   1317 C  CZ  . TYR A 1 169 ? 69.677 -41.055 -8.769  1.00 23.66  ?  169 TYR A CZ  1 
ATOM   1318 O  OH  . TYR A 1 169 ? 70.469 -42.168 -8.719  1.00 20.97  ?  169 TYR A OH  1 
ATOM   1319 N  N   . ARG A 1 170 ? 68.912 -35.261 -8.689  1.00 37.09  ?  170 ARG A N   1 
ATOM   1320 C  CA  . ARG A 1 170 ? 70.218 -34.655 -8.950  1.00 38.38  ?  170 ARG A CA  1 
ATOM   1321 C  C   . ARG A 1 170 ? 70.692 -33.899 -7.718  1.00 36.99  ?  170 ARG A C   1 
ATOM   1322 O  O   . ARG A 1 170 ? 71.838 -34.037 -7.296  1.00 39.04  ?  170 ARG A O   1 
ATOM   1323 C  CB  . ARG A 1 170 ? 70.138 -33.645 -10.102 1.00 39.09  ?  170 ARG A CB  1 
ATOM   1324 C  CG  . ARG A 1 170 ? 71.315 -32.701 -10.291 1.00 38.71  ?  170 ARG A CG  1 
ATOM   1325 C  CD  . ARG A 1 170 ? 71.148 -31.878 -11.569 1.00 38.90  ?  170 ARG A CD  1 
ATOM   1326 N  NE  . ARG A 1 170 ? 70.066 -30.892 -11.471 1.00 34.84  ?  170 ARG A NE  1 
ATOM   1327 C  CZ  . ARG A 1 170 ? 70.140 -29.730 -10.818 1.00 38.25  ?  170 ARG A CZ  1 
ATOM   1328 N  NH1 . ARG A 1 170 ? 71.258 -29.332 -10.210 1.00 32.22  1  170 ARG A NH1 1 
ATOM   1329 N  NH2 . ARG A 1 170 ? 69.080 -28.934 -10.814 1.00 41.47  ?  170 ARG A NH2 1 
ATOM   1330 N  N   . LYS A 1 171 ? 69.769 -33.103 -7.169  1.00 35.44  ?  171 LYS A N   1 
ATOM   1331 C  CA  . LYS A 1 171 ? 69.994 -32.298 -5.980  1.00 33.32  ?  171 LYS A CA  1 
ATOM   1332 C  C   . LYS A 1 171 ? 70.527 -33.198 -4.863  1.00 32.02  ?  171 LYS A C   1 
ATOM   1333 O  O   . LYS A 1 171 ? 71.618 -32.959 -4.361  1.00 31.51  ?  171 LYS A O   1 
ATOM   1334 C  CB  . LYS A 1 171 ? 68.668 -31.584 -5.688  1.00 32.29  ?  171 LYS A CB  1 
ATOM   1335 C  CG  . LYS A 1 171 ? 68.758 -30.263 -4.959  1.00 35.40  ?  171 LYS A CG  1 
ATOM   1336 C  CD  . LYS A 1 171 ? 67.612 -29.292 -5.244  1.00 36.58  ?  171 LYS A CD  1 
ATOM   1337 C  CE  . LYS A 1 171 ? 67.873 -27.958 -4.581  1.00 40.64  ?  171 LYS A CE  1 
ATOM   1338 N  NZ  . LYS A 1 171 ? 67.456 -26.787 -5.365  1.00 41.18  1  171 LYS A NZ  1 
ATOM   1339 N  N   . LEU A 1 172 ? 69.790 -34.274 -4.548  1.00 29.50  ?  172 LEU A N   1 
ATOM   1340 C  CA  . LEU A 1 172 ? 70.070 -35.119 -3.399  1.00 28.72  ?  172 LEU A CA  1 
ATOM   1341 C  C   . LEU A 1 172 ? 71.320 -35.957 -3.666  1.00 28.99  ?  172 LEU A C   1 
ATOM   1342 O  O   . LEU A 1 172 ? 72.264 -35.965 -2.893  1.00 28.27  ?  172 LEU A O   1 
ATOM   1343 C  CB  . LEU A 1 172 ? 68.849 -36.007 -3.125  1.00 30.51  ?  172 LEU A CB  1 
ATOM   1344 C  CG  . LEU A 1 172 ? 67.527 -35.304 -2.781  1.00 29.65  ?  172 LEU A CG  1 
ATOM   1345 C  CD1 . LEU A 1 172 ? 66.393 -36.295 -2.698  1.00 31.57  ?  172 LEU A CD1 1 
ATOM   1346 C  CD2 . LEU A 1 172 ? 67.605 -34.563 -1.481  1.00 29.39  ?  172 LEU A CD2 1 
ATOM   1347 N  N   . ARG A 1 173 ? 71.318 -36.686 -4.774  1.00 30.03  ?  173 ARG A N   1 
ATOM   1348 C  CA  . ARG A 1 173 ? 72.373 -37.634 -5.079  1.00 30.68  ?  173 ARG A CA  1 
ATOM   1349 C  C   . ARG A 1 173 ? 73.674 -36.911 -5.415  1.00 31.08  ?  173 ARG A C   1 
ATOM   1350 O  O   . ARG A 1 173 ? 74.739 -37.492 -5.300  1.00 30.94  ?  173 ARG A O   1 
ATOM   1351 C  CB  . ARG A 1 173 ? 71.861 -38.454 -6.270  1.00 34.75  ?  173 ARG A CB  1 
ATOM   1352 C  CG  . ARG A 1 173 ? 72.756 -39.551 -6.827  1.00 38.54  ?  173 ARG A CG  1 
ATOM   1353 C  CD  . ARG A 1 173 ? 72.866 -40.757 -5.904  1.00 41.21  ?  173 ARG A CD  1 
ATOM   1354 N  NE  . ARG A 1 173 ? 71.603 -41.477 -5.679  1.00 43.85  ?  173 ARG A NE  1 
ATOM   1355 C  CZ  . ARG A 1 173 ? 71.426 -42.809 -5.674  1.00 45.46  ?  173 ARG A CZ  1 
ATOM   1356 N  NH1 . ARG A 1 173 ? 72.436 -43.664 -5.853  1.00 48.08  1  173 ARG A NH1 1 
ATOM   1357 N  NH2 . ARG A 1 173 ? 70.213 -43.290 -5.468  1.00 42.93  ?  173 ARG A NH2 1 
ATOM   1358 N  N   . ASN A 1 174 ? 73.590 -35.654 -5.871  1.00 34.99  ?  174 ASN A N   1 
ATOM   1359 C  CA  . ASN A 1 174 ? 74.733 -34.921 -6.408  1.00 34.12  ?  174 ASN A CA  1 
ATOM   1360 C  C   . ASN A 1 174 ? 75.369 -35.698 -7.560  1.00 32.36  ?  174 ASN A C   1 
ATOM   1361 O  O   . ASN A 1 174 ? 76.592 -35.886 -7.554  1.00 32.28  ?  174 ASN A O   1 
ATOM   1362 C  CB  . ASN A 1 174 ? 75.794 -34.637 -5.348  1.00 37.15  ?  174 ASN A CB  1 
ATOM   1363 C  CG  . ASN A 1 174 ? 76.867 -33.664 -5.797  1.00 40.97  ?  174 ASN A CG  1 
ATOM   1364 O  OD1 . ASN A 1 174 ? 76.823 -33.121 -6.914  1.00 38.83  ?  174 ASN A OD1 1 
ATOM   1365 N  ND2 . ASN A 1 174 ? 77.833 -33.417 -4.920  1.00 41.44  ?  174 ASN A ND2 1 
ATOM   1366 N  N   A SER A 1 175 ? 74.537 -36.126 -8.524  0.50 29.31  ?  175 SER A N   1 
ATOM   1367 N  N   B SER A 1 175 ? 74.543 -36.156 -8.521  0.50 29.18  ?  175 SER A N   1 
ATOM   1368 C  CA  A SER A 1 175 ? 75.025 -36.802 -9.715  0.50 25.98  ?  175 SER A CA  1 
ATOM   1369 C  CA  B SER A 1 175 ? 75.031 -36.851 -9.708  0.50 25.78  ?  175 SER A CA  1 
ATOM   1370 C  C   A SER A 1 175 ? 74.118 -36.513 -10.910 0.50 23.27  ?  175 SER A C   1 
ATOM   1371 C  C   B SER A 1 175 ? 74.122 -36.559 -10.906 0.50 23.18  ?  175 SER A C   1 
ATOM   1372 O  O   A SER A 1 175 ? 72.919 -36.327 -10.754 0.50 22.56  ?  175 SER A O   1 
ATOM   1373 O  O   B SER A 1 175 ? 72.922 -36.387 -10.747 0.50 22.44  ?  175 SER A O   1 
ATOM   1374 C  CB  A SER A 1 175 ? 75.162 -38.281 -9.488  0.50 24.61  ?  175 SER A CB  1 
ATOM   1375 C  CB  B SER A 1 175 ? 75.182 -38.346 -9.456  0.50 24.26  ?  175 SER A CB  1 
ATOM   1376 O  OG  A SER A 1 175 ? 76.207 -38.775 -10.311 0.50 23.39  ?  175 SER A OG  1 
ATOM   1377 O  OG  B SER A 1 175 ? 73.966 -39.061 -9.617  0.50 22.88  ?  175 SER A OG  1 
ATOM   1378 N  N   . TRP A 1 176 ? 74.717 -36.480 -12.103 1.00 22.29  ?  176 TRP A N   1 
ATOM   1379 C  CA  . TRP A 1 176 ? 73.988 -36.308 -13.350 1.00 22.24  ?  176 TRP A CA  1 
ATOM   1380 C  C   . TRP A 1 176 ? 74.104 -37.583 -14.188 1.00 21.57  ?  176 TRP A C   1 
ATOM   1381 O  O   . TRP A 1 176 ? 75.134 -37.816 -14.830 1.00 19.94  ?  176 TRP A O   1 
ATOM   1382 C  CB  . TRP A 1 176 ? 74.543 -35.098 -14.111 1.00 23.85  ?  176 TRP A CB  1 
ATOM   1383 C  CG  . TRP A 1 176 ? 73.540 -34.425 -15.012 1.00 25.29  ?  176 TRP A CG  1 
ATOM   1384 C  CD1 . TRP A 1 176 ? 72.861 -33.264 -14.770 1.00 24.81  ?  176 TRP A CD1 1 
ATOM   1385 C  CD2 . TRP A 1 176 ? 73.098 -34.891 -16.311 1.00 27.16  ?  176 TRP A CD2 1 
ATOM   1386 N  NE1 . TRP A 1 176 ? 72.030 -32.968 -15.822 1.00 25.76  ?  176 TRP A NE1 1 
ATOM   1387 C  CE2 . TRP A 1 176 ? 72.146 -33.942 -16.779 1.00 25.71  ?  176 TRP A CE2 1 
ATOM   1388 C  CE3 . TRP A 1 176 ? 73.419 -36.002 -17.110 1.00 23.37  ?  176 TRP A CE3 1 
ATOM   1389 C  CZ2 . TRP A 1 176 ? 71.503 -34.081 -18.005 1.00 23.70  ?  176 TRP A CZ2 1 
ATOM   1390 C  CZ3 . TRP A 1 176 ? 72.784 -36.137 -18.320 1.00 23.65  ?  176 TRP A CZ3 1 
ATOM   1391 C  CH2 . TRP A 1 176 ? 71.841 -35.188 -18.757 1.00 25.86  ?  176 TRP A CH2 1 
ATOM   1392 N  N   . GLU A 1 177 ? 73.038 -38.400 -14.162 1.00 20.24  ?  177 GLU A N   1 
ATOM   1393 C  CA  . GLU A 1 177 ? 73.018 -39.697 -14.815 1.00 21.68  ?  177 GLU A CA  1 
ATOM   1394 C  C   . GLU A 1 177 ? 71.636 -39.977 -15.396 1.00 23.08  ?  177 GLU A C   1 
ATOM   1395 O  O   . GLU A 1 177 ? 70.667 -39.341 -15.008 1.00 22.53  ?  177 GLU A O   1 
ATOM   1396 C  CB  . GLU A 1 177 ? 73.390 -40.788 -13.806 1.00 23.30  ?  177 GLU A CB  1 
ATOM   1397 C  CG  . GLU A 1 177 ? 72.403 -40.935 -12.651 1.00 22.45  ?  177 GLU A CG  1 
ATOM   1398 C  CD  . GLU A 1 177 ? 72.891 -41.774 -11.481 1.00 20.94  ?  177 GLU A CD  1 
ATOM   1399 O  OE1 . GLU A 1 177 ? 73.719 -41.307 -10.678 1.00 18.64  ?  177 GLU A OE1 1 
ATOM   1400 O  OE2 . GLU A 1 177 ? 72.374 -42.898 -11.357 1.00 22.12  -1 177 GLU A OE2 1 
ATOM   1401 N  N   . GLY A 1 178 ? 71.537 -40.990 -16.274 1.00 25.06  ?  178 GLY A N   1 
ATOM   1402 C  CA  . GLY A 1 178 ? 70.264 -41.355 -16.883 1.00 23.27  ?  178 GLY A CA  1 
ATOM   1403 C  C   . GLY A 1 178 ? 69.319 -42.079 -15.923 1.00 22.56  ?  178 GLY A C   1 
ATOM   1404 O  O   . GLY A 1 178 ? 68.827 -43.157 -16.254 1.00 22.74  ?  178 GLY A O   1 
ATOM   1405 N  N   . VAL A 1 179 ? 69.012 -41.453 -14.773 1.00 24.02  ?  179 VAL A N   1 
ATOM   1406 C  CA  . VAL A 1 179 ? 68.134 -42.041 -13.760 1.00 25.00  ?  179 VAL A CA  1 
ATOM   1407 C  C   . VAL A 1 179 ? 66.645 -41.956 -14.145 1.00 24.08  ?  179 VAL A C   1 
ATOM   1408 O  O   . VAL A 1 179 ? 65.845 -42.715 -13.593 1.00 24.22  ?  179 VAL A O   1 
ATOM   1409 C  CB  . VAL A 1 179 ? 68.345 -41.453 -12.354 1.00 25.49  ?  179 VAL A CB  1 
ATOM   1410 C  CG1 . VAL A 1 179 ? 67.864 -40.008 -12.272 1.00 26.32  ?  179 VAL A CG1 1 
ATOM   1411 C  CG2 . VAL A 1 179 ? 67.654 -42.315 -11.298 1.00 27.00  ?  179 VAL A CG2 1 
ATOM   1412 N  N   . LEU A 1 180 ? 66.269 -41.064 -15.079 1.00 22.91  ?  180 LEU A N   1 
ATOM   1413 C  CA  . LEU A 1 180 ? 64.932 -41.080 -15.675 1.00 22.95  ?  180 LEU A CA  1 
ATOM   1414 C  C   . LEU A 1 180 ? 64.988 -41.070 -17.214 1.00 22.64  ?  180 LEU A C   1 
ATOM   1415 O  O   . LEU A 1 180 ? 65.930 -40.601 -17.843 1.00 22.63  ?  180 LEU A O   1 
ATOM   1416 C  CB  . LEU A 1 180 ? 64.139 -39.896 -15.114 1.00 22.60  ?  180 LEU A CB  1 
ATOM   1417 C  CG  . LEU A 1 180 ? 63.887 -39.922 -13.604 1.00 23.35  ?  180 LEU A CG  1 
ATOM   1418 C  CD1 . LEU A 1 180 ? 63.403 -38.591 -13.077 1.00 24.18  ?  180 LEU A CD1 1 
ATOM   1419 C  CD2 . LEU A 1 180 ? 62.869 -40.987 -13.254 1.00 24.37  ?  180 LEU A CD2 1 
ATOM   1420 N  N   . THR A 1 181 ? 63.943 -41.605 -17.839 1.00 22.28  ?  181 THR A N   1 
ATOM   1421 C  CA  . THR A 1 181 ? 63.704 -41.417 -19.260 1.00 23.75  ?  181 THR A CA  1 
ATOM   1422 C  C   . THR A 1 181 ? 62.435 -40.564 -19.376 1.00 23.53  ?  181 THR A C   1 
ATOM   1423 O  O   . THR A 1 181 ? 61.674 -40.503 -18.407 1.00 21.66  ?  181 THR A O   1 
ATOM   1424 C  CB  . THR A 1 181 ? 63.580 -42.791 -19.933 1.00 25.62  ?  181 THR A CB  1 
ATOM   1425 O  OG1 . THR A 1 181 ? 62.486 -43.484 -19.324 1.00 25.17  ?  181 THR A OG1 1 
ATOM   1426 C  CG2 . THR A 1 181 ? 64.852 -43.617 -19.795 1.00 25.19  ?  181 THR A CG2 1 
ATOM   1427 N  N   . GLY A 1 182 ? 62.225 -39.912 -20.539 1.00 22.28  ?  182 GLY A N   1 
ATOM   1428 C  CA  . GLY A 1 182 ? 61.174 -38.924 -20.729 1.00 21.33  ?  182 GLY A CA  1 
ATOM   1429 C  C   . GLY A 1 182 ? 61.673 -37.503 -20.467 1.00 23.50  ?  182 GLY A C   1 
ATOM   1430 O  O   . GLY A 1 182 ? 60.878 -36.611 -20.161 1.00 27.35  ?  182 GLY A O   1 
ATOM   1431 N  N   . LYS A 1 183 ? 62.985 -37.278 -20.601 1.00 23.90  ?  183 LYS A N   1 
ATOM   1432 C  CA  . LYS A 1 183 ? 63.598 -36.013 -20.199 1.00 25.23  ?  183 LYS A CA  1 
ATOM   1433 C  C   . LYS A 1 183 ? 63.493 -34.980 -21.322 1.00 23.00  ?  183 LYS A C   1 
ATOM   1434 O  O   . LYS A 1 183 ? 63.194 -35.314 -22.472 1.00 17.74  ?  183 LYS A O   1 
ATOM   1435 C  CB  . LYS A 1 183 ? 65.082 -36.179 -19.822 1.00 28.30  ?  183 LYS A CB  1 
ATOM   1436 C  CG  . LYS A 1 183 ? 65.325 -37.154 -18.660 1.00 32.99  ?  183 LYS A CG  1 
ATOM   1437 C  CD  . LYS A 1 183 ? 66.669 -37.107 -17.927 1.00 32.40  ?  183 LYS A CD  1 
ATOM   1438 C  CE  . LYS A 1 183 ? 67.798 -37.784 -18.641 1.00 31.09  ?  183 LYS A CE  1 
ATOM   1439 N  NZ  . LYS A 1 183 ? 67.374 -39.083 -19.176 1.00 30.65  1  183 LYS A NZ  1 
ATOM   1440 N  N   . GLY A 1 184 ? 63.817 -33.729 -20.954 1.00 23.12  ?  184 GLY A N   1 
ATOM   1441 C  CA  . GLY A 1 184 ? 63.841 -32.596 -21.866 1.00 22.50  ?  184 GLY A CA  1 
ATOM   1442 C  C   . GLY A 1 184 ? 64.836 -32.809 -23.002 1.00 21.49  ?  184 GLY A C   1 
ATOM   1443 O  O   . GLY A 1 184 ? 65.678 -33.705 -22.952 1.00 21.37  ?  184 GLY A O   1 
ATOM   1444 N  N   . GLY A 1 185 ? 64.725 -31.980 -24.040 1.00 21.20  ?  185 GLY A N   1 
ATOM   1445 C  CA  . GLY A 1 185 ? 65.697 -32.004 -25.121 1.00 21.34  ?  185 GLY A CA  1 
ATOM   1446 C  C   . GLY A 1 185 ? 67.107 -31.684 -24.618 1.00 21.24  ?  185 GLY A C   1 
ATOM   1447 O  O   . GLY A 1 185 ? 68.058 -32.361 -24.982 1.00 20.58  ?  185 GLY A O   1 
ATOM   1448 N  N   . SER A 1 186 ? 67.236 -30.669 -23.754 1.00 20.93  ?  186 SER A N   1 
ATOM   1449 C  CA  . SER A 1 186 ? 68.537 -30.111 -23.445 1.00 21.41  ?  186 SER A CA  1 
ATOM   1450 C  C   . SER A 1 186 ? 69.116 -30.662 -22.137 1.00 25.61  ?  186 SER A C   1 
ATOM   1451 O  O   . SER A 1 186 ? 70.221 -30.278 -21.743 1.00 29.39  ?  186 SER A O   1 
ATOM   1452 C  CB  . SER A 1 186 ? 68.458 -28.630 -23.443 1.00 19.08  ?  186 SER A CB  1 
ATOM   1453 O  OG  . SER A 1 186 ? 67.862 -28.196 -22.242 1.00 19.46  ?  186 SER A OG  1 
ATOM   1454 N  N   . TRP A 1 187 ? 68.401 -31.583 -21.478 1.00 26.48  ?  187 TRP A N   1 
ATOM   1455 C  CA  . TRP A 1 187 ? 68.930 -32.274 -20.309 1.00 28.26  ?  187 TRP A CA  1 
ATOM   1456 C  C   . TRP A 1 187 ? 68.702 -33.793 -20.409 1.00 28.61  ?  187 TRP A C   1 
ATOM   1457 O  O   . TRP A 1 187 ? 68.265 -34.462 -19.463 1.00 24.59  ?  187 TRP A O   1 
ATOM   1458 C  CB  . TRP A 1 187 ? 68.387 -31.660 -19.008 1.00 29.95  ?  187 TRP A CB  1 
ATOM   1459 C  CG  . TRP A 1 187 ? 66.908 -31.369 -18.971 1.00 31.46  ?  187 TRP A CG  1 
ATOM   1460 C  CD1 . TRP A 1 187 ? 66.290 -30.262 -19.479 1.00 32.92  ?  187 TRP A CD1 1 
ATOM   1461 C  CD2 . TRP A 1 187 ? 65.875 -32.157 -18.336 1.00 30.78  ?  187 TRP A CD2 1 
ATOM   1462 N  NE1 . TRP A 1 187 ? 64.944 -30.320 -19.238 1.00 34.96  ?  187 TRP A NE1 1 
ATOM   1463 C  CE2 . TRP A 1 187 ? 64.657 -31.465 -18.533 1.00 32.10  ?  187 TRP A CE2 1 
ATOM   1464 C  CE3 . TRP A 1 187 ? 65.856 -33.367 -17.633 1.00 29.98  ?  187 TRP A CE3 1 
ATOM   1465 C  CZ2 . TRP A 1 187 ? 63.440 -31.950 -18.061 1.00 27.68  ?  187 TRP A CZ2 1 
ATOM   1466 C  CZ3 . TRP A 1 187 ? 64.650 -33.842 -17.164 1.00 29.39  ?  187 TRP A CZ3 1 
ATOM   1467 C  CH2 . TRP A 1 187 ? 63.465 -33.136 -17.367 1.00 28.55  ?  187 TRP A CH2 1 
ATOM   1468 N  N   . GLY A 1 188 ? 69.076 -34.336 -21.578 1.00 27.74  ?  188 GLY A N   1 
ATOM   1469 C  CA  . GLY A 1 188 ? 69.374 -35.745 -21.735 1.00 24.98  ?  188 GLY A CA  1 
ATOM   1470 C  C   . GLY A 1 188 ? 68.231 -36.486 -22.413 1.00 24.46  ?  188 GLY A C   1 
ATOM   1471 O  O   . GLY A 1 188 ? 68.241 -37.719 -22.451 1.00 24.25  ?  188 GLY A O   1 
ATOM   1472 N  N   . GLY A 1 189 ? 67.256 -35.752 -22.954 1.00 22.62  ?  189 GLY A N   1 
ATOM   1473 C  CA  . GLY A 1 189 ? 66.224 -36.405 -23.743 1.00 23.75  ?  189 GLY A CA  1 
ATOM   1474 C  C   . GLY A 1 189 ? 66.773 -36.933 -25.073 1.00 25.42  ?  189 GLY A C   1 
ATOM   1475 O  O   . GLY A 1 189 ? 67.840 -36.509 -25.541 1.00 23.20  ?  189 GLY A O   1 
ATOM   1476 N  N   . SER A 1 190 ? 66.023 -37.874 -25.665 1.00 28.12  ?  190 SER A N   1 
ATOM   1477 C  CA  . SER A 1 190 ? 66.246 -38.336 -27.035 1.00 31.03  ?  190 SER A CA  1 
ATOM   1478 C  C   . SER A 1 190 ? 65.171 -37.799 -27.984 1.00 31.20  ?  190 SER A C   1 
ATOM   1479 O  O   . SER A 1 190 ? 63.998 -37.682 -27.631 1.00 36.76  ?  190 SER A O   1 
ATOM   1480 C  CB  . SER A 1 190 ? 66.272 -39.851 -27.121 1.00 29.42  ?  190 SER A CB  1 
ATOM   1481 O  OG  . SER A 1 190 ? 66.395 -40.257 -28.479 1.00 27.92  ?  190 SER A OG  1 
ATOM   1482 N  N   . LEU A 1 191 ? 65.561 -37.532 -29.226 1.00 30.14  ?  191 LEU A N   1 
ATOM   1483 C  CA  . LEU A 1 191 ? 64.583 -37.206 -30.252 1.00 30.85  ?  191 LEU A CA  1 
ATOM   1484 C  C   . LEU A 1 191 ? 63.937 -38.524 -30.661 1.00 31.78  ?  191 LEU A C   1 
ATOM   1485 O  O   . LEU A 1 191 ? 64.499 -39.579 -30.385 1.00 28.88  ?  191 LEU A O   1 
ATOM   1486 C  CB  . LEU A 1 191 ? 65.220 -36.485 -31.441 1.00 28.24  ?  191 LEU A CB  1 
ATOM   1487 C  CG  . LEU A 1 191 ? 66.207 -35.369 -31.088 1.00 26.10  ?  191 LEU A CG  1 
ATOM   1488 C  CD1 . LEU A 1 191 ? 67.468 -35.509 -31.925 1.00 26.17  ?  191 LEU A CD1 1 
ATOM   1489 C  CD2 . LEU A 1 191 ? 65.588 -33.985 -31.244 1.00 24.95  ?  191 LEU A CD2 1 
ATOM   1490 N  N   . ILE A 1 192 ? 62.755 -38.425 -31.287 1.00 34.63  ?  192 ILE A N   1 
ATOM   1491 C  CA  . ILE A 1 192 ? 61.877 -39.543 -31.623 1.00 34.60  ?  192 ILE A CA  1 
ATOM   1492 C  C   . ILE A 1 192 ? 61.174 -40.103 -30.383 1.00 33.42  ?  192 ILE A C   1 
ATOM   1493 O  O   . ILE A 1 192 ? 60.463 -41.091 -30.507 1.00 40.81  ?  192 ILE A O   1 
ATOM   1494 C  CB  . ILE A 1 192 ? 62.584 -40.637 -32.454 1.00 34.66  ?  192 ILE A CB  1 
ATOM   1495 C  CG1 . ILE A 1 192 ? 63.273 -40.048 -33.706 1.00 35.53  ?  192 ILE A CG1 1 
ATOM   1496 C  CG2 . ILE A 1 192 ? 61.621 -41.763 -32.858 1.00 34.18  ?  192 ILE A CG2 1 
ATOM   1497 C  CD1 . ILE A 1 192 ? 62.325 -39.384 -34.689 1.00 34.38  ?  192 ILE A CD1 1 
ATOM   1498 N  N   . ARG A 1 193 ? 61.274 -39.456 -29.213 1.00 32.25  ?  193 ARG A N   1 
ATOM   1499 C  CA  . ARG A 1 193 ? 60.463 -39.862 -28.069 1.00 28.76  ?  193 ARG A CA  1 
ATOM   1500 C  C   . ARG A 1 193 ? 58.989 -39.636 -28.410 1.00 27.06  ?  193 ARG A C   1 
ATOM   1501 O  O   . ARG A 1 193 ? 58.183 -40.567 -28.372 1.00 22.17  ?  193 ARG A O   1 
ATOM   1502 C  CB  . ARG A 1 193 ? 60.823 -39.138 -26.762 1.00 28.30  ?  193 ARG A CB  1 
ATOM   1503 C  CG  . ARG A 1 193 ? 60.100 -39.690 -25.537 1.00 27.78  ?  193 ARG A CG  1 
ATOM   1504 C  CD  . ARG A 1 193 ? 60.085 -38.775 -24.328 1.00 28.89  ?  193 ARG A CD  1 
ATOM   1505 N  NE  . ARG A 1 193 ? 59.549 -37.419 -24.526 1.00 30.45  ?  193 ARG A NE  1 
ATOM   1506 C  CZ  . ARG A 1 193 ? 58.283 -37.091 -24.843 1.00 29.33  ?  193 ARG A CZ  1 
ATOM   1507 N  NH1 . ARG A 1 193 ? 57.362 -38.041 -24.998 1.00 30.09  1  193 ARG A NH1 1 
ATOM   1508 N  NH2 . ARG A 1 193 ? 57.951 -35.815 -24.999 1.00 24.00  ?  193 ARG A NH2 1 
ATOM   1509 N  N   . PRO A 1 194 ? 58.585 -38.410 -28.823 1.00 31.31  ?  194 PRO A N   1 
ATOM   1510 C  CA  . PRO A 1 194 ? 57.195 -38.180 -29.213 1.00 30.43  ?  194 PRO A CA  1 
ATOM   1511 C  C   . PRO A 1 194 ? 56.753 -39.196 -30.267 1.00 29.61  ?  194 PRO A C   1 
ATOM   1512 O  O   . PRO A 1 194 ? 55.660 -39.749 -30.175 1.00 31.01  ?  194 PRO A O   1 
ATOM   1513 C  CB  . PRO A 1 194 ? 57.199 -36.719 -29.708 1.00 29.31  ?  194 PRO A CB  1 
ATOM   1514 C  CG  . PRO A 1 194 ? 58.387 -36.085 -29.022 1.00 28.12  ?  194 PRO A CG  1 
ATOM   1515 C  CD  . PRO A 1 194 ? 59.418 -37.195 -28.987 1.00 31.83  ?  194 PRO A CD  1 
ATOM   1516 N  N   . GLU A 1 195 ? 57.643 -39.500 -31.216 1.00 30.83  ?  195 GLU A N   1 
ATOM   1517 C  CA  . GLU A 1 195 ? 57.298 -40.291 -32.389 1.00 31.47  ?  195 GLU A CA  1 
ATOM   1518 C  C   . GLU A 1 195 ? 57.567 -41.782 -32.189 1.00 28.92  ?  195 GLU A C   1 
ATOM   1519 O  O   . GLU A 1 195 ? 57.384 -42.551 -33.121 1.00 27.90  ?  195 GLU A O   1 
ATOM   1520 C  CB  . GLU A 1 195 ? 58.093 -39.827 -33.609 1.00 31.87  ?  195 GLU A CB  1 
ATOM   1521 C  CG  . GLU A 1 195 ? 57.906 -38.346 -33.908 1.00 34.04  ?  195 GLU A CG  1 
ATOM   1522 C  CD  . GLU A 1 195 ? 58.950 -37.424 -33.313 1.00 36.22  ?  195 GLU A CD  1 
ATOM   1523 O  OE1 . GLU A 1 195 ? 59.248 -36.448 -34.009 1.00 33.15  ?  195 GLU A OE1 1 
ATOM   1524 O  OE2 . GLU A 1 195 ? 59.462 -37.652 -32.192 1.00 43.96  -1 195 GLU A OE2 1 
ATOM   1525 N  N   . ALA A 1 196 ? 57.916 -42.193 -30.971 1.00 28.51  ?  196 ALA A N   1 
ATOM   1526 C  CA  . ALA A 1 196 ? 58.458 -43.522 -30.719 1.00 30.44  ?  196 ALA A CA  1 
ATOM   1527 C  C   . ALA A 1 196 ? 57.440 -44.649 -30.914 1.00 28.13  ?  196 ALA A C   1 
ATOM   1528 O  O   . ALA A 1 196 ? 57.754 -45.631 -31.592 1.00 29.57  ?  196 ALA A O   1 
ATOM   1529 C  CB  . ALA A 1 196 ? 59.023 -43.579 -29.324 1.00 32.84  ?  196 ALA A CB  1 
ATOM   1530 N  N   . THR A 1 197 ? 56.260 -44.532 -30.293 1.00 25.58  ?  197 THR A N   1 
ATOM   1531 C  CA  . THR A 1 197 ? 55.263 -45.597 -30.304 1.00 24.85  ?  197 THR A CA  1 
ATOM   1532 C  C   . THR A 1 197 ? 54.705 -45.816 -31.714 1.00 27.99  ?  197 THR A C   1 
ATOM   1533 O  O   . THR A 1 197 ? 54.608 -46.972 -32.150 1.00 28.68  ?  197 THR A O   1 
ATOM   1534 C  CB  . THR A 1 197 ? 54.152 -45.294 -29.301 1.00 22.81  ?  197 THR A CB  1 
ATOM   1535 O  OG1 . THR A 1 197 ? 54.713 -45.257 -27.982 1.00 22.35  ?  197 THR A OG1 1 
ATOM   1536 C  CG2 . THR A 1 197 ? 53.069 -46.354 -29.316 1.00 22.75  ?  197 THR A CG2 1 
ATOM   1537 N  N   . GLY A 1 198 ? 54.360 -44.712 -32.412 1.00 28.75  ?  198 GLY A N   1 
ATOM   1538 C  CA  . GLY A 1 198 ? 53.713 -44.741 -33.722 1.00 27.42  ?  198 GLY A CA  1 
ATOM   1539 C  C   . GLY A 1 198 ? 54.648 -45.235 -34.825 1.00 30.01  ?  198 GLY A C   1 
ATOM   1540 O  O   . GLY A 1 198 ? 54.260 -46.073 -35.629 1.00 29.12  ?  198 GLY A O   1 
ATOM   1541 N  N   . TYR A 1 199 ? 55.876 -44.696 -34.872 1.00 36.11  ?  199 TYR A N   1 
ATOM   1542 C  CA  . TYR A 1 199 ? 56.924 -45.203 -35.749 1.00 38.27  ?  199 TYR A CA  1 
ATOM   1543 C  C   . TYR A 1 199 ? 57.188 -46.677 -35.431 1.00 40.98  ?  199 TYR A C   1 
ATOM   1544 O  O   . TYR A 1 199 ? 57.403 -47.480 -36.334 1.00 45.79  ?  199 TYR A O   1 
ATOM   1545 C  CB  . TYR A 1 199 ? 58.222 -44.406 -35.588 1.00 38.32  ?  199 TYR A CB  1 
ATOM   1546 C  CG  . TYR A 1 199 ? 58.249 -42.976 -36.116 1.00 40.70  ?  199 TYR A CG  1 
ATOM   1547 C  CD1 . TYR A 1 199 ? 57.125 -42.360 -36.648 1.00 43.64  ?  199 TYR A CD1 1 
ATOM   1548 C  CD2 . TYR A 1 199 ? 59.422 -42.227 -36.066 1.00 42.83  ?  199 TYR A CD2 1 
ATOM   1549 C  CE1 . TYR A 1 199 ? 57.175 -41.061 -37.138 1.00 46.00  ?  199 TYR A CE1 1 
ATOM   1550 C  CE2 . TYR A 1 199 ? 59.479 -40.924 -36.533 1.00 42.92  ?  199 TYR A CE2 1 
ATOM   1551 C  CZ  . TYR A 1 199 ? 58.353 -40.333 -37.076 1.00 44.62  ?  199 TYR A CZ  1 
ATOM   1552 O  OH  . TYR A 1 199 ? 58.434 -39.036 -37.531 1.00 40.35  ?  199 TYR A OH  1 
ATOM   1553 N  N   . GLY A 1 200 ? 57.137 -47.045 -34.146 1.00 38.52  ?  200 GLY A N   1 
ATOM   1554 C  CA  . GLY A 1 200 ? 57.317 -48.433 -33.740 1.00 41.69  ?  200 GLY A CA  1 
ATOM   1555 C  C   . GLY A 1 200 ? 56.296 -49.377 -34.381 1.00 43.01  ?  200 GLY A C   1 
ATOM   1556 O  O   . GLY A 1 200 ? 56.658 -50.449 -34.882 1.00 42.33  ?  200 GLY A O   1 
ATOM   1557 N  N   . VAL A 1 201 ? 55.021 -48.961 -34.365 1.00 41.79  ?  201 VAL A N   1 
ATOM   1558 C  CA  . VAL A 1 201 ? 53.924 -49.775 -34.873 1.00 40.88  ?  201 VAL A CA  1 
ATOM   1559 C  C   . VAL A 1 201 ? 54.144 -50.049 -36.361 1.00 37.18  ?  201 VAL A C   1 
ATOM   1560 O  O   . VAL A 1 201 ? 54.051 -51.191 -36.823 1.00 30.74  ?  201 VAL A O   1 
ATOM   1561 C  CB  . VAL A 1 201 ? 52.563 -49.100 -34.613 1.00 40.37  ?  201 VAL A CB  1 
ATOM   1562 C  CG1 . VAL A 1 201 ? 51.412 -49.896 -35.210 1.00 40.24  ?  201 VAL A CG1 1 
ATOM   1563 C  CG2 . VAL A 1 201 ? 52.312 -48.885 -33.125 1.00 43.22  ?  201 VAL A CG2 1 
ATOM   1564 N  N   . VAL A 1 202 ? 54.466 -48.974 -37.079 1.00 34.20  ?  202 VAL A N   1 
ATOM   1565 C  CA  . VAL A 1 202 ? 54.746 -49.041 -38.498 1.00 33.63  ?  202 VAL A CA  1 
ATOM   1566 C  C   . VAL A 1 202 ? 55.940 -49.961 -38.752 1.00 32.78  ?  202 VAL A C   1 
ATOM   1567 O  O   . VAL A 1 202 ? 55.938 -50.719 -39.716 1.00 30.80  ?  202 VAL A O   1 
ATOM   1568 C  CB  . VAL A 1 202 ? 54.990 -47.639 -39.081 1.00 35.34  ?  202 VAL A CB  1 
ATOM   1569 C  CG1 . VAL A 1 202 ? 55.226 -47.719 -40.579 1.00 37.94  ?  202 VAL A CG1 1 
ATOM   1570 C  CG2 . VAL A 1 202 ? 53.823 -46.694 -38.817 1.00 37.93  ?  202 VAL A CG2 1 
ATOM   1571 N  N   . TYR A 1 203 ? 56.971 -49.880 -37.905 1.00 33.77  ?  203 TYR A N   1 
ATOM   1572 C  CA  . TYR A 1 203 ? 58.211 -50.607 -38.149 1.00 33.81  ?  203 TYR A CA  1 
ATOM   1573 C  C   . TYR A 1 203 ? 57.969 -52.102 -37.937 1.00 30.12  ?  203 TYR A C   1 
ATOM   1574 O  O   . TYR A 1 203 ? 58.637 -52.939 -38.544 1.00 26.32  ?  203 TYR A O   1 
ATOM   1575 C  CB  . TYR A 1 203 ? 59.368 -50.107 -37.268 1.00 34.35  ?  203 TYR A CB  1 
ATOM   1576 C  CG  . TYR A 1 203 ? 60.035 -48.814 -37.720 1.00 35.05  ?  203 TYR A CG  1 
ATOM   1577 C  CD1 . TYR A 1 203 ? 60.165 -47.732 -36.855 1.00 36.10  ?  203 TYR A CD1 1 
ATOM   1578 C  CD2 . TYR A 1 203 ? 60.571 -48.678 -38.994 1.00 35.80  ?  203 TYR A CD2 1 
ATOM   1579 C  CE1 . TYR A 1 203 ? 60.776 -46.551 -37.249 1.00 33.65  ?  203 TYR A CE1 1 
ATOM   1580 C  CE2 . TYR A 1 203 ? 61.187 -47.502 -39.397 1.00 35.66  ?  203 TYR A CE2 1 
ATOM   1581 C  CZ  . TYR A 1 203 ? 61.282 -46.429 -38.527 1.00 32.55  ?  203 TYR A CZ  1 
ATOM   1582 O  OH  . TYR A 1 203 ? 61.875 -45.264 -38.917 1.00 29.00  ?  203 TYR A OH  1 
ATOM   1583 N  N   . TYR A 1 204 ? 57.035 -52.424 -37.038 1.00 29.58  ?  204 TYR A N   1 
ATOM   1584 C  CA  . TYR A 1 204 ? 56.677 -53.806 -36.760 1.00 29.06  ?  204 TYR A CA  1 
ATOM   1585 C  C   . TYR A 1 204 ? 56.030 -54.392 -38.015 1.00 31.05  ?  204 TYR A C   1 
ATOM   1586 O  O   . TYR A 1 204 ? 56.494 -55.377 -38.574 1.00 39.31  ?  204 TYR A O   1 
ATOM   1587 C  CB  . TYR A 1 204 ? 55.788 -53.858 -35.512 1.00 28.56  ?  204 TYR A CB  1 
ATOM   1588 C  CG  . TYR A 1 204 ? 55.607 -55.261 -34.957 1.00 29.09  ?  204 TYR A CG  1 
ATOM   1589 C  CD1 . TYR A 1 204 ? 56.427 -55.752 -33.949 1.00 29.89  ?  204 TYR A CD1 1 
ATOM   1590 C  CD2 . TYR A 1 204 ? 54.646 -56.118 -35.479 1.00 29.03  ?  204 TYR A CD2 1 
ATOM   1591 C  CE1 . TYR A 1 204 ? 56.289 -57.047 -33.468 1.00 28.58  ?  204 TYR A CE1 1 
ATOM   1592 C  CE2 . TYR A 1 204 ? 54.495 -57.412 -35.004 1.00 27.11  ?  204 TYR A CE2 1 
ATOM   1593 C  CZ  . TYR A 1 204 ? 55.321 -57.884 -33.997 1.00 27.52  ?  204 TYR A CZ  1 
ATOM   1594 O  OH  . TYR A 1 204 ? 55.200 -59.164 -33.508 1.00 25.69  ?  204 TYR A OH  1 
ATOM   1595 N  N   . VAL A 1 205 ? 54.994 -53.724 -38.514 1.00 33.16  ?  205 VAL A N   1 
ATOM   1596 C  CA  . VAL A 1 205 ? 54.266 -54.186 -39.684 1.00 32.32  ?  205 VAL A CA  1 
ATOM   1597 C  C   . VAL A 1 205 ? 55.212 -54.359 -40.867 1.00 34.64  ?  205 VAL A C   1 
ATOM   1598 O  O   . VAL A 1 205 ? 55.067 -55.307 -41.644 1.00 31.35  ?  205 VAL A O   1 
ATOM   1599 C  CB  . VAL A 1 205 ? 53.108 -53.238 -40.040 1.00 29.89  ?  205 VAL A CB  1 
ATOM   1600 C  CG1 . VAL A 1 205 ? 52.424 -53.686 -41.329 1.00 30.97  ?  205 VAL A CG1 1 
ATOM   1601 C  CG2 . VAL A 1 205 ? 52.092 -53.143 -38.904 1.00 27.77  ?  205 VAL A CG2 1 
ATOM   1602 N  N   . GLU A 1 206 ? 56.166 -53.426 -40.999 1.00 40.37  ?  206 GLU A N   1 
ATOM   1603 C  CA  . GLU A 1 206 ? 57.100 -53.439 -42.114 1.00 41.61  ?  206 GLU A CA  1 
ATOM   1604 C  C   . GLU A 1 206 ? 57.826 -54.773 -42.099 1.00 45.28  ?  206 GLU A C   1 
ATOM   1605 O  O   . GLU A 1 206 ? 57.961 -55.426 -43.140 1.00 56.22  ?  206 GLU A O   1 
ATOM   1606 C  CB  . GLU A 1 206 ? 58.120 -52.303 -42.110 1.00 41.88  ?  206 GLU A CB  1 
ATOM   1607 C  CG  . GLU A 1 206 ? 58.675 -52.062 -43.510 1.00 45.70  ?  206 GLU A CG  1 
ATOM   1608 C  CD  . GLU A 1 206 ? 59.713 -50.965 -43.702 1.00 46.70  ?  206 GLU A CD  1 
ATOM   1609 O  OE1 . GLU A 1 206 ? 60.083 -50.800 -44.891 1.00 39.54  ?  206 GLU A OE1 1 
ATOM   1610 O  OE2 . GLU A 1 206 ? 60.137 -50.300 -42.717 1.00 44.91  -1 206 GLU A OE2 1 
ATOM   1611 N  N   . HIS A 1 207 ? 58.240 -55.178 -40.895 1.00 40.91  ?  207 HIS A N   1 
ATOM   1612 C  CA  . HIS A 1 207 ? 58.899 -56.460 -40.721 1.00 42.07  ?  207 HIS A CA  1 
ATOM   1613 C  C   . HIS A 1 207 ? 57.917 -57.582 -41.047 1.00 39.15  ?  207 HIS A C   1 
ATOM   1614 O  O   . HIS A 1 207 ? 58.290 -58.545 -41.711 1.00 37.44  ?  207 HIS A O   1 
ATOM   1615 C  CB  . HIS A 1 207 ? 59.547 -56.550 -39.333 1.00 41.13  ?  207 HIS A CB  1 
ATOM   1616 C  CG  . HIS A 1 207 ? 60.688 -55.598 -39.164 1.00 40.46  ?  207 HIS A CG  1 
ATOM   1617 N  ND1 . HIS A 1 207 ? 60.784 -54.751 -38.080 1.00 37.19  ?  207 HIS A ND1 1 
ATOM   1618 C  CD2 . HIS A 1 207 ? 61.741 -55.302 -39.963 1.00 40.01  ?  207 HIS A CD2 1 
ATOM   1619 C  CE1 . HIS A 1 207 ? 61.876 -53.999 -38.210 1.00 36.50  ?  207 HIS A CE1 1 
ATOM   1620 N  NE2 . HIS A 1 207 ? 62.472 -54.314 -39.338 1.00 35.07  ?  207 HIS A NE2 1 
ATOM   1621 N  N   . MET A 1 208 ? 56.667 -57.455 -40.586 1.00 36.31  ?  208 MET A N   1 
ATOM   1622 C  CA  . MET A 1 208 ? 55.671 -58.480 -40.850 1.00 35.63  ?  208 MET A CA  1 
ATOM   1623 C  C   . MET A 1 208 ? 55.573 -58.710 -42.351 1.00 34.61  ?  208 MET A C   1 
ATOM   1624 O  O   . MET A 1 208 ? 55.624 -59.861 -42.788 1.00 34.97  ?  208 MET A O   1 
ATOM   1625 C  CB  . MET A 1 208 ? 54.290 -58.112 -40.301 1.00 35.58  ?  208 MET A CB  1 
ATOM   1626 C  CG  . MET A 1 208 ? 54.246 -58.083 -38.807 1.00 34.19  ?  208 MET A CG  1 
ATOM   1627 S  SD  . MET A 1 208 ? 52.731 -57.279 -38.268 1.00 32.95  ?  208 MET A SD  1 
ATOM   1628 C  CE  . MET A 1 208 ? 51.544 -58.622 -38.412 1.00 30.91  ?  208 MET A CE  1 
ATOM   1629 N  N   . ILE A 1 209 ? 55.448 -57.609 -43.113 1.00 34.59  ?  209 ILE A N   1 
ATOM   1630 C  CA  . ILE A 1 209 ? 55.266 -57.666 -44.561 1.00 33.81  ?  209 ILE A CA  1 
ATOM   1631 C  C   . ILE A 1 209 ? 56.469 -58.373 -45.179 1.00 34.09  ?  209 ILE A C   1 
ATOM   1632 O  O   . ILE A 1 209 ? 56.306 -59.340 -45.911 1.00 35.17  ?  209 ILE A O   1 
ATOM   1633 C  CB  . ILE A 1 209 ? 55.062 -56.261 -45.164 1.00 33.20  ?  209 ILE A CB  1 
ATOM   1634 C  CG1 . ILE A 1 209 ? 53.822 -55.571 -44.608 1.00 32.82  ?  209 ILE A CG1 1 
ATOM   1635 C  CG2 . ILE A 1 209 ? 55.022 -56.323 -46.693 1.00 33.51  ?  209 ILE A CG2 1 
ATOM   1636 C  CD1 . ILE A 1 209 ? 53.843 -54.066 -44.737 1.00 32.87  ?  209 ILE A CD1 1 
ATOM   1637 N  N   . ALA A 1 210 ? 57.672 -57.903 -44.839 1.00 35.91  ?  210 ALA A N   1 
ATOM   1638 C  CA  . ALA A 1 210 ? 58.910 -58.505 -45.318 1.00 40.34  ?  210 ALA A CA  1 
ATOM   1639 C  C   . ALA A 1 210 ? 58.901 -60.024 -45.174 1.00 37.75  ?  210 ALA A C   1 
ATOM   1640 O  O   . ALA A 1 210 ? 59.268 -60.710 -46.119 1.00 39.56  ?  210 ALA A O   1 
ATOM   1641 C  CB  . ALA A 1 210 ? 60.109 -57.911 -44.599 1.00 41.51  ?  210 ALA A CB  1 
ATOM   1642 N  N   . HIS A 1 211 ? 58.528 -60.533 -43.990 1.00 41.12  ?  211 HIS A N   1 
ATOM   1643 C  CA  . HIS A 1 211 ? 58.549 -61.965 -43.714 1.00 42.93  ?  211 HIS A CA  1 
ATOM   1644 C  C   . HIS A 1 211 ? 57.516 -62.646 -44.600 1.00 38.47  ?  211 HIS A C   1 
ATOM   1645 O  O   . HIS A 1 211 ? 57.852 -63.433 -45.469 1.00 42.72  ?  211 HIS A O   1 
ATOM   1646 C  CB  . HIS A 1 211 ? 58.265 -62.286 -42.239 1.00 41.40  ?  211 HIS A CB  1 
ATOM   1647 C  CG  . HIS A 1 211 ? 58.581 -63.702 -41.859 1.00 44.71  ?  211 HIS A CG  1 
ATOM   1648 N  ND1 . HIS A 1 211 ? 57.667 -64.735 -41.900 1.00 43.30  ?  211 HIS A ND1 1 
ATOM   1649 C  CD2 . HIS A 1 211 ? 59.732 -64.249 -41.403 1.00 46.18  ?  211 HIS A CD2 1 
ATOM   1650 C  CE1 . HIS A 1 211 ? 58.246 -65.851 -41.464 1.00 42.61  ?  211 HIS A CE1 1 
ATOM   1651 N  NE2 . HIS A 1 211 ? 59.495 -65.581 -41.161 1.00 42.40  ?  211 HIS A NE2 1 
ATOM   1652 N  N   . ALA A 1 212 ? 56.264 -62.277 -44.394 1.00 34.89  ?  212 ALA A N   1 
ATOM   1653 C  CA  . ALA A 1 212 ? 55.157 -62.902 -45.079 1.00 39.16  ?  212 ALA A CA  1 
ATOM   1654 C  C   . ALA A 1 212 ? 55.379 -62.928 -46.592 1.00 38.73  ?  212 ALA A C   1 
ATOM   1655 O  O   . ALA A 1 212 ? 55.066 -63.944 -47.209 1.00 42.52  ?  212 ALA A O   1 
ATOM   1656 C  CB  . ALA A 1 212 ? 53.879 -62.181 -44.698 1.00 42.50  ?  212 ALA A CB  1 
ATOM   1657 N  N   . THR A 1 213 ? 55.897 -61.830 -47.187 1.00 37.36  ?  213 THR A N   1 
ATOM   1658 C  CA  . THR A 1 213 ? 56.045 -61.721 -48.641 1.00 35.42  ?  213 THR A CA  1 
ATOM   1659 C  C   . THR A 1 213 ? 57.477 -62.069 -49.063 1.00 37.52  ?  213 THR A C   1 
ATOM   1660 O  O   . THR A 1 213 ? 57.954 -61.626 -50.111 1.00 38.79  ?  213 THR A O   1 
ATOM   1661 C  CB  . THR A 1 213 ? 55.632 -60.338 -49.167 1.00 31.80  ?  213 THR A CB  1 
ATOM   1662 O  OG1 . THR A 1 213 ? 56.621 -59.390 -48.807 1.00 35.15  ?  213 THR A OG1 1 
ATOM   1663 C  CG2 . THR A 1 213 ? 54.304 -59.834 -48.641 1.00 29.93  ?  213 THR A CG2 1 
ATOM   1664 N  N   . ASN A 1 214 ? 58.145 -62.911 -48.266 1.00 41.76  ?  214 ASN A N   1 
ATOM   1665 C  CA  . ASN A 1 214 ? 59.574 -63.159 -48.378 1.00 43.32  ?  214 ASN A CA  1 
ATOM   1666 C  C   . ASN A 1 214 ? 60.262 -61.980 -49.073 1.00 45.41  ?  214 ASN A C   1 
ATOM   1667 O  O   . ASN A 1 214 ? 60.811 -62.131 -50.163 1.00 51.95  ?  214 ASN A O   1 
ATOM   1668 C  CB  . ASN A 1 214 ? 59.845 -64.510 -49.037 1.00 43.17  ?  214 ASN A CB  1 
ATOM   1669 C  CG  . ASN A 1 214 ? 61.285 -64.936 -48.880 1.00 44.75  ?  214 ASN A CG  1 
ATOM   1670 O  OD1 . ASN A 1 214 ? 61.881 -65.444 -49.835 1.00 51.93  ?  214 ASN A OD1 1 
ATOM   1671 N  ND2 . ASN A 1 214 ? 61.853 -64.768 -47.691 1.00 40.12  ?  214 ASN A ND2 1 
ATOM   1672 N  N   . GLY A 1 215 ? 60.198 -60.799 -48.442 1.00 41.08  ?  215 GLY A N   1 
ATOM   1673 C  CA  . GLY A 1 215 ? 60.967 -59.638 -48.863 1.00 41.27  ?  215 GLY A CA  1 
ATOM   1674 C  C   . GLY A 1 215 ? 60.612 -59.141 -50.265 1.00 39.00  ?  215 GLY A C   1 
ATOM   1675 O  O   . GLY A 1 215 ? 61.398 -58.425 -50.866 1.00 40.64  ?  215 GLY A O   1 
ATOM   1676 N  N   . ALA A 1 216 ? 59.414 -59.473 -50.753 1.00 40.72  ?  216 ALA A N   1 
ATOM   1677 C  CA  . ALA A 1 216 ? 58.974 -59.085 -52.080 1.00 44.26  ?  216 ALA A CA  1 
ATOM   1678 C  C   . ALA A 1 216 ? 57.976 -57.930 -52.026 1.00 46.83  ?  216 ALA A C   1 
ATOM   1679 O  O   . ALA A 1 216 ? 57.395 -57.607 -53.063 1.00 55.50  ?  216 ALA A O   1 
ATOM   1680 C  CB  . ALA A 1 216 ? 58.351 -60.282 -52.771 1.00 47.74  ?  216 ALA A CB  1 
ATOM   1681 N  N   . GLU A 1 217 ? 57.732 -57.340 -50.840 1.00 43.79  ?  217 GLU A N   1 
ATOM   1682 C  CA  . GLU A 1 217 ? 56.838 -56.187 -50.728 1.00 44.97  ?  217 GLU A CA  1 
ATOM   1683 C  C   . GLU A 1 217 ? 57.358 -55.191 -49.688 1.00 42.46  ?  217 GLU A C   1 
ATOM   1684 O  O   . GLU A 1 217 ? 58.114 -55.555 -48.790 1.00 42.36  ?  217 GLU A O   1 
ATOM   1685 C  CB  . GLU A 1 217 ? 55.378 -56.579 -50.460 1.00 47.88  ?  217 GLU A CB  1 
ATOM   1686 C  CG  . GLU A 1 217 ? 54.773 -57.473 -51.549 1.00 47.28  ?  217 GLU A CG  1 
ATOM   1687 C  CD  . GLU A 1 217 ? 53.259 -57.660 -51.589 1.00 41.81  ?  217 GLU A CD  1 
ATOM   1688 O  OE1 . GLU A 1 217 ? 52.560 -56.685 -51.945 1.00 37.74  ?  217 GLU A OE1 1 
ATOM   1689 O  OE2 . GLU A 1 217 ? 52.779 -58.784 -51.297 1.00 37.75  -1 217 GLU A OE2 1 
ATOM   1690 N  N   . SER A 1 218 ? 56.961 -53.918 -49.861 1.00 41.69  ?  218 SER A N   1 
ATOM   1691 C  CA  . SER A 1 218 ? 57.281 -52.808 -48.964 1.00 39.64  ?  218 SER A CA  1 
ATOM   1692 C  C   . SER A 1 218 ? 55.999 -52.378 -48.259 1.00 35.90  ?  218 SER A C   1 
ATOM   1693 O  O   . SER A 1 218 ? 55.036 -53.125 -48.243 1.00 31.96  ?  218 SER A O   1 
ATOM   1694 C  CB  . SER A 1 218 ? 57.909 -51.603 -49.700 1.00 37.57  ?  218 SER A CB  1 
ATOM   1695 O  OG  . SER A 1 218 ? 59.314 -51.722 -49.875 1.00 38.37  ?  218 SER A OG  1 
ATOM   1696 N  N   . PHE A 1 219 ? 56.017 -51.187 -47.651 1.00 35.34  ?  219 PHE A N   1 
ATOM   1697 C  CA  . PHE A 1 219 ? 54.799 -50.462 -47.351 1.00 37.25  ?  219 PHE A CA  1 
ATOM   1698 C  C   . PHE A 1 219 ? 54.318 -49.711 -48.592 1.00 41.23  ?  219 PHE A C   1 
ATOM   1699 O  O   . PHE A 1 219 ? 53.186 -49.215 -48.621 1.00 40.81  ?  219 PHE A O   1 
ATOM   1700 C  CB  . PHE A 1 219 ? 55.020 -49.463 -46.219 1.00 37.82  ?  219 PHE A CB  1 
ATOM   1701 C  CG  . PHE A 1 219 ? 54.315 -49.830 -44.924 1.00 43.74  ?  219 PHE A CG  1 
ATOM   1702 C  CD1 . PHE A 1 219 ? 53.024 -49.373 -44.660 1.00 44.69  ?  219 PHE A CD1 1 
ATOM   1703 C  CD2 . PHE A 1 219 ? 54.957 -50.607 -43.965 1.00 45.57  ?  219 PHE A CD2 1 
ATOM   1704 C  CE1 . PHE A 1 219 ? 52.402 -49.675 -43.456 1.00 48.89  ?  219 PHE A CE1 1 
ATOM   1705 C  CE2 . PHE A 1 219 ? 54.329 -50.913 -42.767 1.00 48.95  ?  219 PHE A CE2 1 
ATOM   1706 C  CZ  . PHE A 1 219 ? 53.054 -50.447 -42.511 1.00 49.52  ?  219 PHE A CZ  1 
ATOM   1707 N  N   . ALA A 1 220 ? 55.206 -49.606 -49.595 1.00 43.20  ?  220 ALA A N   1 
ATOM   1708 C  CA  . ALA A 1 220 ? 54.995 -48.734 -50.741 1.00 41.44  ?  220 ALA A CA  1 
ATOM   1709 C  C   . ALA A 1 220 ? 53.670 -49.099 -51.415 1.00 36.23  ?  220 ALA A C   1 
ATOM   1710 O  O   . ALA A 1 220 ? 53.391 -50.273 -51.674 1.00 28.68  ?  220 ALA A O   1 
ATOM   1711 C  CB  . ALA A 1 220 ? 56.195 -48.793 -51.680 1.00 39.06  ?  220 ALA A CB  1 
ATOM   1712 N  N   . GLY A 1 221 ? 52.821 -48.079 -51.585 1.00 34.66  ?  221 GLY A N   1 
ATOM   1713 C  CA  . GLY A 1 221 ? 51.484 -48.255 -52.126 1.00 37.29  ?  221 GLY A CA  1 
ATOM   1714 C  C   . GLY A 1 221 ? 50.428 -48.528 -51.054 1.00 38.00  ?  221 GLY A C   1 
ATOM   1715 O  O   . GLY A 1 221 ? 49.322 -47.993 -51.154 1.00 40.59  ?  221 GLY A O   1 
ATOM   1716 N  N   . LYS A 1 222 ? 50.784 -49.335 -50.036 1.00 39.53  ?  222 LYS A N   1 
ATOM   1717 C  CA  . LYS A 1 222 ? 49.835 -50.015 -49.154 1.00 41.72  ?  222 LYS A CA  1 
ATOM   1718 C  C   . LYS A 1 222 ? 48.811 -49.051 -48.538 1.00 41.03  ?  222 LYS A C   1 
ATOM   1719 O  O   . LYS A 1 222 ? 49.152 -47.965 -48.066 1.00 37.33  ?  222 LYS A O   1 
ATOM   1720 C  CB  . LYS A 1 222 ? 50.552 -50.744 -48.010 1.00 42.17  ?  222 LYS A CB  1 
ATOM   1721 C  CG  . LYS A 1 222 ? 51.504 -51.857 -48.417 1.00 41.72  ?  222 LYS A CG  1 
ATOM   1722 C  CD  . LYS A 1 222 ? 50.959 -53.269 -48.276 1.00 41.83  ?  222 LYS A CD  1 
ATOM   1723 C  CE  . LYS A 1 222 ? 51.822 -54.242 -49.001 1.00 42.34  ?  222 LYS A CE  1 
ATOM   1724 N  NZ  . LYS A 1 222 ? 51.775 -53.963 -50.444 1.00 43.92  1  222 LYS A NZ  1 
ATOM   1725 N  N   . ARG A 1 223 ? 47.547 -49.495 -48.522 1.00 38.01  ?  223 ARG A N   1 
ATOM   1726 C  CA  . ARG A 1 223 ? 46.435 -48.690 -48.053 1.00 36.52  ?  223 ARG A CA  1 
ATOM   1727 C  C   . ARG A 1 223 ? 46.217 -49.035 -46.592 1.00 30.54  ?  223 ARG A C   1 
ATOM   1728 O  O   . ARG A 1 223 ? 46.006 -50.203 -46.280 1.00 29.78  ?  223 ARG A O   1 
ATOM   1729 C  CB  . ARG A 1 223 ? 45.205 -48.974 -48.925 1.00 41.45  ?  223 ARG A CB  1 
ATOM   1730 C  CG  . ARG A 1 223 ? 45.391 -48.562 -50.379 1.00 45.33  ?  223 ARG A CG  1 
ATOM   1731 C  CD  . ARG A 1 223 ? 45.738 -49.710 -51.307 1.00 49.67  ?  223 ARG A CD  1 
ATOM   1732 N  NE  . ARG A 1 223 ? 44.547 -50.229 -51.991 1.00 54.00  ?  223 ARG A NE  1 
ATOM   1733 C  CZ  . ARG A 1 223 ? 44.076 -51.475 -52.010 1.00 53.43  ?  223 ARG A CZ  1 
ATOM   1734 N  NH1 . ARG A 1 223 ? 44.708 -52.477 -51.428 1.00 47.61  1  223 ARG A NH1 1 
ATOM   1735 N  NH2 . ARG A 1 223 ? 42.936 -51.711 -52.634 1.00 58.01  ?  223 ARG A NH2 1 
ATOM   1736 N  N   . VAL A 1 224 ? 46.299 -48.028 -45.716 1.00 28.40  ?  224 VAL A N   1 
ATOM   1737 C  CA  . VAL A 1 224 ? 46.416 -48.261 -44.280 1.00 30.20  ?  224 VAL A CA  1 
ATOM   1738 C  C   . VAL A 1 224 ? 45.272 -47.580 -43.526 1.00 34.05  ?  224 VAL A C   1 
ATOM   1739 O  O   . VAL A 1 224 ? 45.119 -46.359 -43.579 1.00 39.74  ?  224 VAL A O   1 
ATOM   1740 C  CB  . VAL A 1 224 ? 47.771 -47.786 -43.723 1.00 29.41  ?  224 VAL A CB  1 
ATOM   1741 C  CG1 . VAL A 1 224 ? 47.858 -48.019 -42.221 1.00 30.63  ?  224 VAL A CG1 1 
ATOM   1742 C  CG2 . VAL A 1 224 ? 48.960 -48.431 -44.435 1.00 28.80  ?  224 VAL A CG2 1 
ATOM   1743 N  N   . ALA A 1 225 ? 44.499 -48.375 -42.777 1.00 35.02  ?  225 ALA A N   1 
ATOM   1744 C  CA  . ALA A 1 225 ? 43.374 -47.877 -41.999 1.00 37.97  ?  225 ALA A CA  1 
ATOM   1745 C  C   . ALA A 1 225 ? 43.800 -47.607 -40.556 1.00 39.78  ?  225 ALA A C   1 
ATOM   1746 O  O   . ALA A 1 225 ? 43.894 -48.542 -39.760 1.00 52.44  ?  225 ALA A O   1 
ATOM   1747 C  CB  . ALA A 1 225 ? 42.250 -48.907 -42.023 1.00 39.00  ?  225 ALA A CB  1 
ATOM   1748 N  N   . ILE A 1 226 ? 44.034 -46.345 -40.196 1.00 35.78  ?  226 ILE A N   1 
ATOM   1749 C  CA  . ILE A 1 226 ? 44.377 -46.035 -38.813 1.00 36.24  ?  226 ILE A CA  1 
ATOM   1750 C  C   . ILE A 1 226 ? 43.097 -45.577 -38.118 1.00 33.52  ?  226 ILE A C   1 
ATOM   1751 O  O   . ILE A 1 226 ? 42.206 -45.041 -38.772 1.00 31.88  ?  226 ILE A O   1 
ATOM   1752 C  CB  . ILE A 1 226 ? 45.535 -45.012 -38.705 1.00 35.30  ?  226 ILE A CB  1 
ATOM   1753 C  CG1 . ILE A 1 226 ? 46.821 -45.534 -39.363 1.00 38.39  ?  226 ILE A CG1 1 
ATOM   1754 C  CG2 . ILE A 1 226 ? 45.818 -44.624 -37.256 1.00 33.32  ?  226 ILE A CG2 1 
ATOM   1755 C  CD1 . ILE A 1 226 ? 47.208 -44.849 -40.661 1.00 38.71  ?  226 ILE A CD1 1 
ATOM   1756 N  N   . SER A 1 227 ? 42.995 -45.856 -36.812 1.00 32.64  ?  227 SER A N   1 
ATOM   1757 C  CA  . SER A 1 227 ? 41.997 -45.216 -35.970 1.00 34.88  ?  227 SER A CA  1 
ATOM   1758 C  C   . SER A 1 227 ? 42.706 -44.519 -34.815 1.00 32.83  ?  227 SER A C   1 
ATOM   1759 O  O   . SER A 1 227 ? 43.712 -45.023 -34.321 1.00 26.84  ?  227 SER A O   1 
ATOM   1760 C  CB  . SER A 1 227 ? 40.966 -46.191 -35.467 1.00 34.33  ?  227 SER A CB  1 
ATOM   1761 O  OG  . SER A 1 227 ? 41.435 -46.827 -34.292 1.00 35.52  ?  227 SER A OG  1 
ATOM   1762 N  N   . GLY A 1 228 ? 42.147 -43.371 -34.404 1.00 36.97  ?  228 GLY A N   1 
ATOM   1763 C  CA  . GLY A 1 228 ? 42.722 -42.508 -33.382 1.00 36.42  ?  228 GLY A CA  1 
ATOM   1764 C  C   . GLY A 1 228 ? 43.289 -41.263 -34.040 1.00 34.76  ?  228 GLY A C   1 
ATOM   1765 O  O   . GLY A 1 228 ? 43.458 -41.259 -35.253 1.00 30.63  ?  228 GLY A O   1 
ATOM   1766 N  N   . SER A 1 229 ? 43.574 -40.236 -33.232 1.00 37.65  ?  229 SER A N   1 
ATOM   1767 C  CA  . SER A 1 229 ? 43.998 -38.939 -33.734 1.00 40.93  ?  229 SER A CA  1 
ATOM   1768 C  C   . SER A 1 229 ? 44.948 -38.254 -32.752 1.00 45.36  ?  229 SER A C   1 
ATOM   1769 O  O   . SER A 1 229 ? 45.020 -37.020 -32.716 1.00 47.48  ?  229 SER A O   1 
ATOM   1770 C  CB  . SER A 1 229 ? 42.787 -38.090 -34.010 1.00 43.82  ?  229 SER A CB  1 
ATOM   1771 O  OG  . SER A 1 229 ? 41.839 -38.230 -32.963 1.00 43.20  ?  229 SER A OG  1 
ATOM   1772 N  N   . GLY A 1 230 ? 45.674 -39.065 -31.963 1.00 43.30  ?  230 GLY A N   1 
ATOM   1773 C  CA  . GLY A 1 230 ? 46.629 -38.575 -30.981 1.00 40.48  ?  230 GLY A CA  1 
ATOM   1774 C  C   . GLY A 1 230 ? 48.041 -39.052 -31.312 1.00 42.74  ?  230 GLY A C   1 
ATOM   1775 O  O   . GLY A 1 230 ? 48.301 -39.429 -32.447 1.00 52.45  ?  230 GLY A O   1 
ATOM   1776 N  N   . ASN A 1 231 ? 48.927 -39.045 -30.306 1.00 44.11  ?  231 ASN A N   1 
ATOM   1777 C  CA  . ASN A 1 231 ? 50.348 -39.325 -30.450 1.00 43.41  ?  231 ASN A CA  1 
ATOM   1778 C  C   . ASN A 1 231 ? 50.519 -40.438 -31.490 1.00 42.77  ?  231 ASN A C   1 
ATOM   1779 O  O   . ASN A 1 231 ? 51.226 -40.271 -32.493 1.00 40.58  ?  231 ASN A O   1 
ATOM   1780 C  CB  . ASN A 1 231 ? 50.943 -39.628 -29.067 1.00 48.10  ?  231 ASN A CB  1 
ATOM   1781 C  CG  . ASN A 1 231 ? 52.460 -39.616 -28.990 1.00 53.06  ?  231 ASN A CG  1 
ATOM   1782 O  OD1 . ASN A 1 231 ? 53.081 -40.628 -28.630 1.00 55.40  ?  231 ASN A OD1 1 
ATOM   1783 N  ND2 . ASN A 1 231 ? 53.082 -38.475 -29.253 1.00 52.16  ?  231 ASN A ND2 1 
ATOM   1784 N  N   . VAL A 1 232 ? 49.812 -41.556 -31.257 1.00 36.52  ?  232 VAL A N   1 
ATOM   1785 C  CA  . VAL A 1 232 ? 50.117 -42.833 -31.885 1.00 32.04  ?  232 VAL A CA  1 
ATOM   1786 C  C   . VAL A 1 232 ? 49.617 -42.813 -33.326 1.00 32.10  ?  232 VAL A C   1 
ATOM   1787 O  O   . VAL A 1 232 ? 50.307 -43.253 -34.244 1.00 34.21  ?  232 VAL A O   1 
ATOM   1788 C  CB  . VAL A 1 232 ? 49.499 -44.026 -31.122 1.00 30.39  ?  232 VAL A CB  1 
ATOM   1789 C  CG1 . VAL A 1 232 ? 50.076 -45.351 -31.576 1.00 29.26  ?  232 VAL A CG1 1 
ATOM   1790 C  CG2 . VAL A 1 232 ? 49.672 -43.935 -29.615 1.00 32.24  ?  232 VAL A CG2 1 
ATOM   1791 N  N   . ALA A 1 233 ? 48.382 -42.348 -33.508 1.00 33.51  ?  233 ALA A N   1 
ATOM   1792 C  CA  . ALA A 1 233 ? 47.757 -42.285 -34.819 1.00 35.92  ?  233 ALA A CA  1 
ATOM   1793 C  C   . ALA A 1 233 ? 48.524 -41.319 -35.724 1.00 38.61  ?  233 ALA A C   1 
ATOM   1794 O  O   . ALA A 1 233 ? 48.734 -41.586 -36.915 1.00 40.94  ?  233 ALA A O   1 
ATOM   1795 C  CB  . ALA A 1 233 ? 46.314 -41.862 -34.668 1.00 34.20  ?  233 ALA A CB  1 
ATOM   1796 N  N   . GLN A 1 234 ? 48.948 -40.206 -35.120 1.00 34.72  ?  234 GLN A N   1 
ATOM   1797 C  CA  . GLN A 1 234 ? 49.576 -39.103 -35.822 1.00 34.05  ?  234 GLN A CA  1 
ATOM   1798 C  C   . GLN A 1 234 ? 50.901 -39.560 -36.405 1.00 31.04  ?  234 GLN A C   1 
ATOM   1799 O  O   . GLN A 1 234 ? 51.107 -39.488 -37.614 1.00 32.17  ?  234 GLN A O   1 
ATOM   1800 C  CB  . GLN A 1 234 ? 49.727 -37.969 -34.805 1.00 36.31  ?  234 GLN A CB  1 
ATOM   1801 C  CG  . GLN A 1 234 ? 50.395 -36.701 -35.318 1.00 39.72  ?  234 GLN A CG  1 
ATOM   1802 C  CD  . GLN A 1 234 ? 50.259 -35.564 -34.325 1.00 45.63  ?  234 GLN A CD  1 
ATOM   1803 O  OE1 . GLN A 1 234 ? 49.142 -35.202 -33.925 1.00 49.09  ?  234 GLN A OE1 1 
ATOM   1804 N  NE2 . GLN A 1 234 ? 51.389 -35.022 -33.882 1.00 42.84  ?  234 GLN A NE2 1 
ATOM   1805 N  N   . TYR A 1 235 ? 51.780 -40.057 -35.539 1.00 27.92  ?  235 TYR A N   1 
ATOM   1806 C  CA  . TYR A 1 235 ? 53.136 -40.368 -35.964 1.00 27.76  ?  235 TYR A CA  1 
ATOM   1807 C  C   . TYR A 1 235 ? 53.126 -41.636 -36.817 1.00 25.93  ?  235 TYR A C   1 
ATOM   1808 O  O   . TYR A 1 235 ? 53.893 -41.751 -37.769 1.00 22.58  ?  235 TYR A O   1 
ATOM   1809 C  CB  . TYR A 1 235 ? 53.990 -40.336 -34.690 1.00 29.38  ?  235 TYR A CB  1 
ATOM   1810 C  CG  . TYR A 1 235 ? 54.209 -38.908 -34.202 1.00 27.83  ?  235 TYR A CG  1 
ATOM   1811 C  CD1 . TYR A 1 235 ? 54.747 -37.956 -35.062 1.00 26.88  ?  235 TYR A CD1 1 
ATOM   1812 C  CD2 . TYR A 1 235 ? 53.803 -38.493 -32.935 1.00 25.48  ?  235 TYR A CD2 1 
ATOM   1813 C  CE1 . TYR A 1 235 ? 54.937 -36.644 -34.660 1.00 27.27  ?  235 TYR A CE1 1 
ATOM   1814 C  CE2 . TYR A 1 235 ? 53.977 -37.182 -32.520 1.00 25.91  ?  235 TYR A CE2 1 
ATOM   1815 C  CZ  . TYR A 1 235 ? 54.560 -36.260 -33.381 1.00 28.51  ?  235 TYR A CZ  1 
ATOM   1816 O  OH  . TYR A 1 235 ? 54.773 -34.959 -33.009 1.00 26.97  ?  235 TYR A OH  1 
ATOM   1817 N  N   . ALA A 1 236 ? 52.243 -42.577 -36.475 1.00 27.05  ?  236 ALA A N   1 
ATOM   1818 C  CA  . ALA A 1 236 ? 52.054 -43.765 -37.284 1.00 29.11  ?  236 ALA A CA  1 
ATOM   1819 C  C   . ALA A 1 236 ? 51.772 -43.357 -38.731 1.00 30.89  ?  236 ALA A C   1 
ATOM   1820 O  O   . ALA A 1 236 ? 52.436 -43.805 -39.657 1.00 29.84  ?  236 ALA A O   1 
ATOM   1821 C  CB  . ALA A 1 236 ? 50.929 -44.594 -36.693 1.00 29.11  ?  236 ALA A CB  1 
ATOM   1822 N  N   . ALA A 1 237 ? 50.763 -42.503 -38.919 1.00 34.83  ?  237 ALA A N   1 
ATOM   1823 C  CA  . ALA A 1 237 ? 50.397 -42.015 -40.240 1.00 37.04  ?  237 ALA A CA  1 
ATOM   1824 C  C   . ALA A 1 237 ? 51.626 -41.458 -40.964 1.00 39.51  ?  237 ALA A C   1 
ATOM   1825 O  O   . ALA A 1 237 ? 51.961 -41.910 -42.064 1.00 42.27  ?  237 ALA A O   1 
ATOM   1826 C  CB  . ALA A 1 237 ? 49.311 -40.968 -40.111 1.00 35.59  ?  237 ALA A CB  1 
ATOM   1827 N  N   . LEU A 1 238 ? 52.305 -40.497 -40.316 1.00 35.69  ?  238 LEU A N   1 
ATOM   1828 C  CA  . LEU A 1 238 ? 53.497 -39.855 -40.861 1.00 32.36  ?  238 LEU A CA  1 
ATOM   1829 C  C   . LEU A 1 238 ? 54.528 -40.884 -41.337 1.00 30.05  ?  238 LEU A C   1 
ATOM   1830 O  O   . LEU A 1 238 ? 55.139 -40.701 -42.389 1.00 30.40  ?  238 LEU A O   1 
ATOM   1831 C  CB  . LEU A 1 238 ? 54.076 -38.891 -39.826 1.00 29.85  ?  238 LEU A CB  1 
ATOM   1832 C  CG  . LEU A 1 238 ? 53.196 -37.676 -39.499 1.00 28.10  ?  238 LEU A CG  1 
ATOM   1833 C  CD1 . LEU A 1 238 ? 53.753 -36.875 -38.353 1.00 25.37  ?  238 LEU A CD1 1 
ATOM   1834 C  CD2 . LEU A 1 238 ? 53.000 -36.782 -40.728 1.00 29.27  ?  238 LEU A CD2 1 
ATOM   1835 N  N   . LYS A 1 239 ? 54.702 -41.971 -40.584 1.00 27.86  ?  239 LYS A N   1 
ATOM   1836 C  CA  . LYS A 1 239 ? 55.729 -42.950 -40.900 1.00 29.59  ?  239 LYS A CA  1 
ATOM   1837 C  C   . LYS A 1 239 ? 55.314 -43.753 -42.134 1.00 35.78  ?  239 LYS A C   1 
ATOM   1838 O  O   . LYS A 1 239 ? 56.144 -44.117 -42.979 1.00 34.79  ?  239 LYS A O   1 
ATOM   1839 C  CB  . LYS A 1 239 ? 56.005 -43.776 -39.644 1.00 27.98  ?  239 LYS A CB  1 
ATOM   1840 C  CG  . LYS A 1 239 ? 57.103 -44.794 -39.747 1.00 29.70  ?  239 LYS A CG  1 
ATOM   1841 C  CD  . LYS A 1 239 ? 58.437 -44.249 -40.247 1.00 34.55  ?  239 LYS A CD  1 
ATOM   1842 C  CE  . LYS A 1 239 ? 59.024 -43.169 -39.381 1.00 35.54  ?  239 LYS A CE  1 
ATOM   1843 N  NZ  . LYS A 1 239 ? 60.377 -42.811 -39.812 1.00 33.10  1  239 LYS A NZ  1 
ATOM   1844 N  N   . VAL A 1 240 ? 54.003 -44.005 -42.240 1.00 40.83  ?  240 VAL A N   1 
ATOM   1845 C  CA  . VAL A 1 240 ? 53.431 -44.689 -43.391 1.00 39.19  ?  240 VAL A CA  1 
ATOM   1846 C  C   . VAL A 1 240 ? 53.630 -43.819 -44.633 1.00 37.03  ?  240 VAL A C   1 
ATOM   1847 O  O   . VAL A 1 240 ? 53.896 -44.341 -45.719 1.00 36.72  ?  240 VAL A O   1 
ATOM   1848 C  CB  . VAL A 1 240 ? 51.949 -45.043 -43.132 1.00 39.37  ?  240 VAL A CB  1 
ATOM   1849 C  CG1 . VAL A 1 240 ? 51.181 -45.371 -44.408 1.00 38.61  ?  240 VAL A CG1 1 
ATOM   1850 C  CG2 . VAL A 1 240 ? 51.807 -46.186 -42.119 1.00 39.66  ?  240 VAL A CG2 1 
ATOM   1851 N  N   . ILE A 1 241 ? 53.560 -42.493 -44.450 1.00 34.05  ?  241 ILE A N   1 
ATOM   1852 C  CA  . ILE A 1 241 ? 53.659 -41.574 -45.572 1.00 35.09  ?  241 ILE A CA  1 
ATOM   1853 C  C   . ILE A 1 241 ? 55.107 -41.544 -46.079 1.00 32.02  ?  241 ILE A C   1 
ATOM   1854 O  O   . ILE A 1 241 ? 55.323 -41.715 -47.282 1.00 27.32  ?  241 ILE A O   1 
ATOM   1855 C  CB  . ILE A 1 241 ? 53.077 -40.194 -45.203 1.00 35.47  ?  241 ILE A CB  1 
ATOM   1856 C  CG1 . ILE A 1 241 ? 51.650 -40.332 -44.704 1.00 38.31  ?  241 ILE A CG1 1 
ATOM   1857 C  CG2 . ILE A 1 241 ? 53.117 -39.235 -46.393 1.00 35.72  ?  241 ILE A CG2 1 
ATOM   1858 C  CD1 . ILE A 1 241 ? 51.236 -39.275 -43.704 1.00 40.20  ?  241 ILE A CD1 1 
ATOM   1859 N  N   . GLU A 1 242 ? 56.074 -41.368 -45.158 1.00 32.43  ?  242 GLU A N   1 
ATOM   1860 C  CA  . GLU A 1 242 ? 57.512 -41.397 -45.440 1.00 32.74  ?  242 GLU A CA  1 
ATOM   1861 C  C   . GLU A 1 242 ? 57.902 -42.642 -46.229 1.00 32.64  ?  242 GLU A C   1 
ATOM   1862 O  O   . GLU A 1 242 ? 58.771 -42.549 -47.092 1.00 33.08  ?  242 GLU A O   1 
ATOM   1863 C  CB  . GLU A 1 242 ? 58.426 -41.471 -44.211 1.00 33.12  ?  242 GLU A CB  1 
ATOM   1864 C  CG  . GLU A 1 242 ? 58.569 -40.164 -43.434 1.00 35.66  ?  242 GLU A CG  1 
ATOM   1865 C  CD  . GLU A 1 242 ? 59.013 -40.344 -41.986 1.00 38.57  ?  242 GLU A CD  1 
ATOM   1866 O  OE1 . GLU A 1 242 ? 59.930 -41.176 -41.794 1.00 42.99  ?  242 GLU A OE1 1 
ATOM   1867 O  OE2 . GLU A 1 242 ? 58.494 -39.674 -41.059 1.00 34.00  -1 242 GLU A OE2 1 
ATOM   1868 N  N   . LEU A 1 243 ? 57.260 -43.783 -45.922 1.00 34.03  ?  243 LEU A N   1 
ATOM   1869 C  CA  . LEU A 1 243 ? 57.608 -45.078 -46.496 1.00 35.86  ?  243 LEU A CA  1 
ATOM   1870 C  C   . LEU A 1 243 ? 56.850 -45.356 -47.793 1.00 34.41  ?  243 LEU A C   1 
ATOM   1871 O  O   . LEU A 1 243 ? 56.970 -46.438 -48.361 1.00 33.35  ?  243 LEU A O   1 
ATOM   1872 C  CB  . LEU A 1 243 ? 57.309 -46.136 -45.433 1.00 39.23  ?  243 LEU A CB  1 
ATOM   1873 C  CG  . LEU A 1 243 ? 58.178 -46.103 -44.166 1.00 38.53  ?  243 LEU A CG  1 
ATOM   1874 C  CD1 . LEU A 1 243 ? 57.493 -46.753 -42.969 1.00 35.57  ?  243 LEU A CD1 1 
ATOM   1875 C  CD2 . LEU A 1 243 ? 59.518 -46.778 -44.441 1.00 40.38  ?  243 LEU A CD2 1 
ATOM   1876 N  N   . GLY A 1 244 ? 56.067 -44.376 -48.252 1.00 39.51  ?  244 GLY A N   1 
ATOM   1877 C  CA  . GLY A 1 244 ? 55.357 -44.451 -49.522 1.00 40.72  ?  244 GLY A CA  1 
ATOM   1878 C  C   . GLY A 1 244 ? 54.011 -45.153 -49.361 1.00 39.18  ?  244 GLY A C   1 
ATOM   1879 O  O   . GLY A 1 244 ? 53.584 -45.889 -50.246 1.00 36.03  ?  244 GLY A O   1 
ATOM   1880 N  N   . GLY A 1 245 ? 53.374 -44.934 -48.205 1.00 38.70  ?  245 GLY A N   1 
ATOM   1881 C  CA  . GLY A 1 245 ? 52.105 -45.562 -47.884 1.00 38.41  ?  245 GLY A CA  1 
ATOM   1882 C  C   . GLY A 1 245 ? 50.967 -44.543 -47.927 1.00 41.47  ?  245 GLY A C   1 
ATOM   1883 O  O   . GLY A 1 245 ? 51.180 -43.343 -47.763 1.00 41.44  ?  245 GLY A O   1 
ATOM   1884 N  N   . ARG A 1 246 ? 49.752 -45.053 -48.149 1.00 44.67  ?  246 ARG A N   1 
ATOM   1885 C  CA  . ARG A 1 246 ? 48.546 -44.249 -48.192 1.00 43.84  ?  246 ARG A CA  1 
ATOM   1886 C  C   . ARG A 1 246 ? 47.776 -44.421 -46.888 1.00 44.51  ?  246 ARG A C   1 
ATOM   1887 O  O   . ARG A 1 246 ? 47.165 -45.465 -46.681 1.00 47.17  ?  246 ARG A O   1 
ATOM   1888 C  CB  . ARG A 1 246 ? 47.652 -44.710 -49.349 1.00 40.30  ?  246 ARG A CB  1 
ATOM   1889 C  CG  . ARG A 1 246 ? 48.072 -44.212 -50.722 1.00 41.38  ?  246 ARG A CG  1 
ATOM   1890 C  CD  . ARG A 1 246 ? 49.425 -44.701 -51.245 1.00 40.11  ?  246 ARG A CD  1 
ATOM   1891 N  NE  . ARG A 1 246 ? 49.615 -44.107 -52.572 1.00 41.29  ?  246 ARG A NE  1 
ATOM   1892 C  CZ  . ARG A 1 246 ? 50.686 -44.136 -53.351 1.00 41.45  ?  246 ARG A CZ  1 
ATOM   1893 N  NH1 . ARG A 1 246 ? 51.786 -44.769 -53.001 1.00 42.06  1  246 ARG A NH1 1 
ATOM   1894 N  NH2 . ARG A 1 246 ? 50.638 -43.525 -54.516 1.00 42.89  ?  246 ARG A NH2 1 
ATOM   1895 N  N   . VAL A 1 247 ? 47.791 -43.391 -46.037 1.00 45.55  ?  247 VAL A N   1 
ATOM   1896 C  CA  . VAL A 1 247 ? 47.004 -43.386 -44.808 1.00 47.38  ?  247 VAL A CA  1 
ATOM   1897 C  C   . VAL A 1 247 ? 45.616 -42.905 -45.201 1.00 46.27  ?  247 VAL A C   1 
ATOM   1898 O  O   . VAL A 1 247 ? 45.485 -41.774 -45.655 1.00 48.07  ?  247 VAL A O   1 
ATOM   1899 C  CB  . VAL A 1 247 ? 47.609 -42.579 -43.627 1.00 43.64  ?  247 VAL A CB  1 
ATOM   1900 C  CG1 . VAL A 1 247 ? 48.958 -41.947 -43.970 1.00 42.48  ?  247 VAL A CG1 1 
ATOM   1901 C  CG2 . VAL A 1 247 ? 46.655 -41.535 -43.040 1.00 39.89  ?  247 VAL A CG2 1 
ATOM   1902 N  N   . VAL A 1 248 ? 44.615 -43.780 -45.019 1.00 52.83  ?  248 VAL A N   1 
ATOM   1903 C  CA  . VAL A 1 248 ? 43.296 -43.643 -45.634 1.00 56.37  ?  248 VAL A CA  1 
ATOM   1904 C  C   . VAL A 1 248 ? 42.218 -43.226 -44.613 1.00 56.37  ?  248 VAL A C   1 
ATOM   1905 O  O   . VAL A 1 248 ? 41.106 -42.861 -45.001 1.00 52.28  ?  248 VAL A O   1 
ATOM   1906 C  CB  . VAL A 1 248 ? 42.986 -44.986 -46.339 1.00 52.29  ?  248 VAL A CB  1 
ATOM   1907 C  CG1 . VAL A 1 248 ? 42.533 -46.070 -45.365 1.00 50.53  ?  248 VAL A CG1 1 
ATOM   1908 C  CG2 . VAL A 1 248 ? 41.971 -44.840 -47.463 1.00 56.80  ?  248 VAL A CG2 1 
ATOM   1909 N  N   . SER A 1 249 ? 42.534 -43.247 -43.305 1.00 56.45  ?  249 SER A N   1 
ATOM   1910 C  CA  . SER A 1 249 ? 41.531 -43.006 -42.271 1.00 55.92  ?  249 SER A CA  1 
ATOM   1911 C  C   . SER A 1 249 ? 42.163 -42.507 -40.969 1.00 51.70  ?  249 SER A C   1 
ATOM   1912 O  O   . SER A 1 249 ? 43.290 -42.862 -40.642 1.00 55.47  ?  249 SER A O   1 
ATOM   1913 C  CB  . SER A 1 249 ? 40.712 -44.263 -42.010 1.00 54.14  ?  249 SER A CB  1 
ATOM   1914 O  OG  . SER A 1 249 ? 41.525 -45.327 -41.526 1.00 50.52  ?  249 SER A OG  1 
ATOM   1915 N  N   . LEU A 1 250 ? 41.403 -41.691 -40.230 1.00 46.06  ?  250 LEU A N   1 
ATOM   1916 C  CA  . LEU A 1 250 ? 41.664 -41.350 -38.835 1.00 44.31  ?  250 LEU A CA  1 
ATOM   1917 C  C   . LEU A 1 250 ? 40.337 -41.516 -38.103 1.00 46.36  ?  250 LEU A C   1 
ATOM   1918 O  O   . LEU A 1 250 ? 39.367 -41.905 -38.748 1.00 57.25  ?  250 LEU A O   1 
ATOM   1919 C  CB  . LEU A 1 250 ? 42.204 -39.927 -38.695 1.00 40.54  ?  250 LEU A CB  1 
ATOM   1920 C  CG  . LEU A 1 250 ? 43.694 -39.771 -38.387 1.00 40.92  ?  250 LEU A CG  1 
ATOM   1921 C  CD1 . LEU A 1 250 ? 44.589 -40.496 -39.357 1.00 42.55  ?  250 LEU A CD1 1 
ATOM   1922 C  CD2 . LEU A 1 250 ? 44.062 -38.294 -38.363 1.00 41.09  ?  250 LEU A CD2 1 
ATOM   1923 N  N   . SER A 1 251 ? 40.287 -41.251 -36.787 1.00 43.88  ?  251 SER A N   1 
ATOM   1924 C  CA  . SER A 1 251 ? 39.050 -41.409 -36.032 1.00 44.04  ?  251 SER A CA  1 
ATOM   1925 C  C   . SER A 1 251 ? 39.151 -40.751 -34.654 1.00 46.80  ?  251 SER A C   1 
ATOM   1926 O  O   . SER A 1 251 ? 40.248 -40.618 -34.103 1.00 42.70  ?  251 SER A O   1 
ATOM   1927 C  CB  . SER A 1 251 ? 38.665 -42.866 -35.906 1.00 43.55  ?  251 SER A CB  1 
ATOM   1928 O  OG  . SER A 1 251 ? 39.445 -43.517 -34.914 1.00 46.87  ?  251 SER A OG  1 
ATOM   1929 N  N   . ASP A 1 252 ? 37.974 -40.403 -34.101 1.00 48.77  ?  252 ASP A N   1 
ATOM   1930 C  CA  . ASP A 1 252 ? 37.835 -39.594 -32.896 1.00 49.15  ?  252 ASP A CA  1 
ATOM   1931 C  C   . ASP A 1 252 ? 36.941 -40.332 -31.900 1.00 49.93  ?  252 ASP A C   1 
ATOM   1932 O  O   . ASP A 1 252 ? 36.816 -41.547 -31.991 1.00 50.51  ?  252 ASP A O   1 
ATOM   1933 C  CB  . ASP A 1 252 ? 37.282 -38.216 -33.246 1.00 49.02  ?  252 ASP A CB  1 
ATOM   1934 C  CG  . ASP A 1 252 ? 37.904 -37.056 -32.481 1.00 46.77  ?  252 ASP A CG  1 
ATOM   1935 O  OD1 . ASP A 1 252 ? 38.783 -37.321 -31.625 1.00 47.71  ?  252 ASP A OD1 1 
ATOM   1936 O  OD2 . ASP A 1 252 ? 37.524 -35.899 -32.755 1.00 41.66  -1 252 ASP A OD2 1 
ATOM   1937 N  N   . SER A 1 253 ? 36.345 -39.606 -30.942 1.00 53.95  ?  253 SER A N   1 
ATOM   1938 C  CA  . SER A 1 253 ? 35.432 -40.193 -29.977 1.00 57.16  ?  253 SER A CA  1 
ATOM   1939 C  C   . SER A 1 253 ? 34.014 -40.134 -30.524 1.00 62.74  ?  253 SER A C   1 
ATOM   1940 O  O   . SER A 1 253 ? 33.353 -41.166 -30.670 1.00 63.67  ?  253 SER A O   1 
ATOM   1941 C  CB  . SER A 1 253 ? 35.534 -39.515 -28.648 1.00 60.46  ?  253 SER A CB  1 
ATOM   1942 O  OG  . SER A 1 253 ? 36.854 -39.656 -28.144 1.00 63.61  ?  253 SER A OG  1 
ATOM   1943 N  N   . GLN A 1 254 ? 33.544 -38.919 -30.822 1.00 65.02  ?  254 GLN A N   1 
ATOM   1944 C  CA  . GLN A 1 254 ? 32.288 -38.779 -31.544 1.00 65.72  ?  254 GLN A CA  1 
ATOM   1945 C  C   . GLN A 1 254 ? 32.621 -38.416 -32.990 1.00 62.32  ?  254 GLN A C   1 
ATOM   1946 O  O   . GLN A 1 254 ? 32.488 -37.259 -33.374 1.00 60.53  ?  254 GLN A O   1 
ATOM   1947 C  CB  . GLN A 1 254 ? 31.293 -37.852 -30.833 1.00 63.88  ?  254 GLN A CB  1 
ATOM   1948 C  CG  . GLN A 1 254 ? 30.036 -37.494 -31.634 1.00 67.66  ?  254 GLN A CG  1 
ATOM   1949 C  CD  . GLN A 1 254 ? 29.420 -38.624 -32.445 1.00 68.04  ?  254 GLN A CD  1 
ATOM   1950 O  OE1 . GLN A 1 254 ? 29.464 -39.807 -32.088 1.00 70.04  ?  254 GLN A OE1 1 
ATOM   1951 N  NE2 . GLN A 1 254 ? 28.783 -38.265 -33.549 1.00 61.89  ?  254 GLN A NE2 1 
ATOM   1952 N  N   . GLY A 1 255 ? 33.101 -39.413 -33.755 1.00 57.79  ?  255 GLY A N   1 
ATOM   1953 C  CA  . GLY A 1 255 ? 33.200 -39.319 -35.203 1.00 53.46  ?  255 GLY A CA  1 
ATOM   1954 C  C   . GLY A 1 255 ? 34.505 -39.893 -35.747 1.00 52.41  ?  255 GLY A C   1 
ATOM   1955 O  O   . GLY A 1 255 ? 35.476 -39.983 -35.006 1.00 55.33  ?  255 GLY A O   1 
ATOM   1956 N  N   . SER A 1 256 ? 34.495 -40.242 -37.049 1.00 54.27  ?  256 SER A N   1 
ATOM   1957 C  CA  . SER A 1 256 ? 35.646 -40.724 -37.811 1.00 59.66  ?  256 SER A CA  1 
ATOM   1958 C  C   . SER A 1 256 ? 35.826 -39.997 -39.150 1.00 65.86  ?  256 SER A C   1 
ATOM   1959 O  O   . SER A 1 256 ? 34.878 -39.446 -39.705 1.00 65.30  ?  256 SER A O   1 
ATOM   1960 C  CB  . SER A 1 256 ? 35.535 -42.193 -38.099 1.00 63.93  ?  256 SER A CB  1 
ATOM   1961 O  OG  . SER A 1 256 ? 36.303 -42.528 -39.250 1.00 67.35  ?  256 SER A OG  1 
ATOM   1962 N  N   . LEU A 1 257 ? 37.049 -40.102 -39.708 1.00 71.06  ?  257 LEU A N   1 
ATOM   1963 C  CA  . LEU A 1 257 ? 37.436 -39.471 -40.963 1.00 71.81  ?  257 LEU A CA  1 
ATOM   1964 C  C   . LEU A 1 257 ? 37.921 -40.532 -41.958 1.00 69.71  ?  257 LEU A C   1 
ATOM   1965 O  O   . LEU A 1 257 ? 38.774 -41.345 -41.610 1.00 78.39  ?  257 LEU A O   1 
ATOM   1966 C  CB  . LEU A 1 257 ? 38.531 -38.452 -40.647 1.00 73.90  ?  257 LEU A CB  1 
ATOM   1967 C  CG  . LEU A 1 257 ? 38.725 -37.319 -41.665 1.00 87.39  ?  257 LEU A CG  1 
ATOM   1968 C  CD1 . LEU A 1 257 ? 39.865 -36.379 -41.296 1.00 91.68  ?  257 LEU A CD1 1 
ATOM   1969 C  CD2 . LEU A 1 257 ? 38.971 -37.847 -43.062 1.00 90.08  ?  257 LEU A CD2 1 
ATOM   1970 N  N   . ILE A 1 258 ? 37.388 -40.499 -43.195 1.00 63.56  ?  258 ILE A N   1 
ATOM   1971 C  CA  . ILE A 1 258 ? 37.781 -41.391 -44.284 1.00 65.61  ?  258 ILE A CA  1 
ATOM   1972 C  C   . ILE A 1 258 ? 38.220 -40.558 -45.497 1.00 65.42  ?  258 ILE A C   1 
ATOM   1973 O  O   . ILE A 1 258 ? 37.619 -39.521 -45.773 1.00 64.16  ?  258 ILE A O   1 
ATOM   1974 C  CB  . ILE A 1 258 ? 36.607 -42.321 -44.668 1.00 67.13  ?  258 ILE A CB  1 
ATOM   1975 C  CG1 . ILE A 1 258 ? 35.836 -42.847 -43.446 1.00 65.73  ?  258 ILE A CG1 1 
ATOM   1976 C  CG2 . ILE A 1 258 ? 37.060 -43.464 -45.579 1.00 65.11  ?  258 ILE A CG2 1 
ATOM   1977 C  CD1 . ILE A 1 258 ? 36.641 -43.721 -42.506 1.00 62.01  ?  258 ILE A CD1 1 
ATOM   1978 N  N   . VAL A 1 259 ? 39.214 -41.047 -46.265 1.00 60.18  ?  259 VAL A N   1 
ATOM   1979 C  CA  . VAL A 1 259 ? 39.754 -40.335 -47.423 1.00 54.49  ?  259 VAL A CA  1 
ATOM   1980 C  C   . VAL A 1 259 ? 38.747 -40.377 -48.582 1.00 53.60  ?  259 VAL A C   1 
ATOM   1981 O  O   . VAL A 1 259 ? 37.752 -41.090 -48.518 1.00 46.44  ?  259 VAL A O   1 
ATOM   1982 C  CB  . VAL A 1 259 ? 41.139 -40.893 -47.833 1.00 48.70  ?  259 VAL A CB  1 
ATOM   1983 C  CG1 . VAL A 1 259 ? 41.043 -42.041 -48.828 1.00 45.31  ?  259 VAL A CG1 1 
ATOM   1984 C  CG2 . VAL A 1 259 ? 42.081 -39.810 -48.366 1.00 47.15  ?  259 VAL A CG2 1 
ATOM   1985 N  N   . LYS A 1 260 ? 39.020 -39.586 -49.634 1.00 58.46  ?  260 LYS A N   1 
ATOM   1986 C  CA  . LYS A 1 260 ? 38.196 -39.473 -50.834 1.00 60.98  ?  260 LYS A CA  1 
ATOM   1987 C  C   . LYS A 1 260 ? 38.259 -40.732 -51.710 1.00 62.61  ?  260 LYS A C   1 
ATOM   1988 O  O   . LYS A 1 260 ? 37.585 -40.796 -52.739 1.00 58.55  ?  260 LYS A O   1 
ATOM   1989 C  CB  . LYS A 1 260 ? 38.611 -38.241 -51.662 1.00 63.74  ?  260 LYS A CB  1 
ATOM   1990 C  CG  . LYS A 1 260 ? 40.109 -38.044 -51.934 1.00 64.41  ?  260 LYS A CG  1 
ATOM   1991 C  CD  . LYS A 1 260 ? 40.469 -37.190 -53.149 1.00 65.83  ?  260 LYS A CD  1 
ATOM   1992 C  CE  . LYS A 1 260 ? 40.208 -37.826 -54.489 1.00 66.98  ?  260 LYS A CE  1 
ATOM   1993 N  NZ  . LYS A 1 260 ? 40.910 -39.097 -54.694 1.00 66.81  1  260 LYS A NZ  1 
ATOM   1994 N  N   . ASP A 1 261 ? 39.009 -41.750 -51.261 1.00 62.55  ?  261 ASP A N   1 
ATOM   1995 C  CA  . ASP A 1 261 ? 39.370 -42.930 -52.036 1.00 60.68  ?  261 ASP A CA  1 
ATOM   1996 C  C   . ASP A 1 261 ? 40.479 -42.557 -53.018 1.00 66.04  ?  261 ASP A C   1 
ATOM   1997 O  O   . ASP A 1 261 ? 40.629 -41.387 -53.374 1.00 63.17  ?  261 ASP A O   1 
ATOM   1998 C  CB  . ASP A 1 261 ? 38.174 -43.583 -52.713 1.00 60.56  ?  261 ASP A CB  1 
ATOM   1999 C  CG  . ASP A 1 261 ? 38.027 -45.077 -52.456 1.00 67.59  ?  261 ASP A CG  1 
ATOM   2000 O  OD1 . ASP A 1 261 ? 38.138 -45.861 -53.436 1.00 56.45  ?  261 ASP A OD1 1 
ATOM   2001 O  OD2 . ASP A 1 261 ? 37.781 -45.442 -51.269 1.00 69.88  -1 261 ASP A OD2 1 
ATOM   2002 N  N   . LYS A 1 262 ? 41.265 -43.569 -53.419 1.00 68.31  ?  262 LYS A N   1 
ATOM   2003 C  CA  . LYS A 1 262 ? 42.396 -43.396 -54.319 1.00 65.61  ?  262 LYS A CA  1 
ATOM   2004 C  C   . LYS A 1 262 ? 43.219 -42.175 -53.894 1.00 67.96  ?  262 LYS A C   1 
ATOM   2005 O  O   . LYS A 1 262 ? 43.453 -41.291 -54.714 1.00 78.13  ?  262 LYS A O   1 
ATOM   2006 C  CB  . LYS A 1 262 ? 41.822 -43.302 -55.739 1.00 68.46  ?  262 LYS A CB  1 
ATOM   2007 C  CG  . LYS A 1 262 ? 42.685 -43.872 -56.855 1.00 72.99  ?  262 LYS A CG  1 
ATOM   2008 C  CD  . LYS A 1 262 ? 42.899 -45.376 -56.749 1.00 68.92  ?  262 LYS A CD  1 
ATOM   2009 C  CE  . LYS A 1 262 ? 43.303 -45.969 -58.057 1.00 67.63  ?  262 LYS A CE  1 
ATOM   2010 N  NZ  . LYS A 1 262 ? 43.069 -47.411 -58.014 1.00 67.95  1  262 LYS A NZ  1 
ATOM   2011 N  N   . ASP A 1 263 ? 43.657 -42.130 -52.617 1.00 65.08  ?  263 ASP A N   1 
ATOM   2012 C  CA  . ASP A 1 263 ? 44.339 -40.968 -52.044 1.00 62.03  ?  263 ASP A CA  1 
ATOM   2013 C  C   . ASP A 1 263 ? 44.821 -41.242 -50.606 1.00 59.19  ?  263 ASP A C   1 
ATOM   2014 O  O   . ASP A 1 263 ? 44.527 -42.279 -50.021 1.00 55.73  ?  263 ASP A O   1 
ATOM   2015 C  CB  . ASP A 1 263 ? 43.435 -39.737 -52.084 1.00 60.33  ?  263 ASP A CB  1 
ATOM   2016 C  CG  . ASP A 1 263 ? 44.135 -38.386 -52.187 1.00 55.65  ?  263 ASP A CG  1 
ATOM   2017 O  OD1 . ASP A 1 263 ? 45.383 -38.366 -52.286 1.00 48.28  ?  263 ASP A OD1 1 
ATOM   2018 O  OD2 . ASP A 1 263 ? 43.429 -37.359 -52.160 1.00 53.08  -1 263 ASP A OD2 1 
ATOM   2019 N  N   . SER A 1 264 ? 45.560 -40.280 -50.025 1.00 53.72  ?  264 SER A N   1 
ATOM   2020 C  CA  . SER A 1 264 ? 46.041 -40.340 -48.650 1.00 45.51  ?  264 SER A CA  1 
ATOM   2021 C  C   . SER A 1 264 ? 46.004 -38.957 -48.002 1.00 40.55  ?  264 SER A C   1 
ATOM   2022 O  O   . SER A 1 264 ? 45.842 -37.960 -48.692 1.00 39.59  ?  264 SER A O   1 
ATOM   2023 C  CB  . SER A 1 264 ? 47.435 -40.880 -48.595 1.00 43.62  ?  264 SER A CB  1 
ATOM   2024 O  OG  . SER A 1 264 ? 48.148 -40.244 -47.544 1.00 42.87  ?  264 SER A OG  1 
ATOM   2025 N  N   . PHE A 1 265 ? 46.185 -38.905 -46.676 1.00 38.22  ?  265 PHE A N   1 
ATOM   2026 C  CA  . PHE A 1 265 ? 46.391 -37.646 -45.972 1.00 37.29  ?  265 PHE A CA  1 
ATOM   2027 C  C   . PHE A 1 265 ? 47.798 -37.145 -46.284 1.00 40.45  ?  265 PHE A C   1 
ATOM   2028 O  O   . PHE A 1 265 ? 48.716 -37.937 -46.522 1.00 39.04  ?  265 PHE A O   1 
ATOM   2029 C  CB  . PHE A 1 265 ? 46.318 -37.745 -44.444 1.00 37.69  ?  265 PHE A CB  1 
ATOM   2030 C  CG  . PHE A 1 265 ? 44.964 -38.064 -43.825 1.00 34.71  ?  265 PHE A CG  1 
ATOM   2031 C  CD1 . PHE A 1 265 ? 44.549 -37.415 -42.676 1.00 33.06  ?  265 PHE A CD1 1 
ATOM   2032 C  CD2 . PHE A 1 265 ? 44.128 -39.017 -44.379 1.00 37.82  ?  265 PHE A CD2 1 
ATOM   2033 C  CE1 . PHE A 1 265 ? 43.330 -37.708 -42.105 1.00 38.16  ?  265 PHE A CE1 1 
ATOM   2034 C  CE2 . PHE A 1 265 ? 42.908 -39.304 -43.802 1.00 40.74  ?  265 PHE A CE2 1 
ATOM   2035 C  CZ  . PHE A 1 265 ? 42.513 -38.650 -42.666 1.00 39.54  ?  265 PHE A CZ  1 
ATOM   2036 N  N   . THR A 1 266 ? 47.961 -35.821 -46.242 1.00 46.98  ?  266 THR A N   1 
ATOM   2037 C  CA  . THR A 1 266 ? 49.263 -35.195 -46.416 1.00 51.18  ?  266 THR A CA  1 
ATOM   2038 C  C   . THR A 1 266 ? 49.772 -34.755 -45.046 1.00 56.25  ?  266 THR A C   1 
ATOM   2039 O  O   . THR A 1 266 ? 48.968 -34.441 -44.164 1.00 58.84  ?  266 THR A O   1 
ATOM   2040 C  CB  . THR A 1 266 ? 49.133 -34.015 -47.371 1.00 53.58  ?  266 THR A CB  1 
ATOM   2041 O  OG1 . THR A 1 266 ? 48.330 -33.076 -46.653 1.00 56.32  ?  266 THR A OG1 1 
ATOM   2042 C  CG2 . THR A 1 266 ? 48.545 -34.440 -48.706 1.00 53.33  ?  266 THR A CG2 1 
ATOM   2043 N  N   . PRO A 1 267 ? 51.106 -34.742 -44.809 1.00 54.17  ?  267 PRO A N   1 
ATOM   2044 C  CA  . PRO A 1 267 ? 51.639 -34.315 -43.515 1.00 50.07  ?  267 PRO A CA  1 
ATOM   2045 C  C   . PRO A 1 267 ? 50.990 -33.058 -42.948 1.00 42.50  ?  267 PRO A C   1 
ATOM   2046 O  O   . PRO A 1 267 ? 50.795 -32.985 -41.745 1.00 41.38  ?  267 PRO A O   1 
ATOM   2047 C  CB  . PRO A 1 267 ? 53.142 -34.154 -43.799 1.00 51.79  ?  267 PRO A CB  1 
ATOM   2048 C  CG  . PRO A 1 267 ? 53.406 -35.245 -44.823 1.00 53.84  ?  267 PRO A CG  1 
ATOM   2049 C  CD  . PRO A 1 267 ? 52.163 -35.223 -45.719 1.00 54.18  ?  267 PRO A CD  1 
ATOM   2050 N  N   . ALA A 1 268 ? 50.612 -32.107 -43.807 1.00 40.00  ?  268 ALA A N   1 
ATOM   2051 C  CA  . ALA A 1 268 ? 50.005 -30.865 -43.346 1.00 41.72  ?  268 ALA A CA  1 
ATOM   2052 C  C   . ALA A 1 268 ? 48.574 -31.098 -42.835 1.00 42.79  ?  268 ALA A C   1 
ATOM   2053 O  O   . ALA A 1 268 ? 48.113 -30.405 -41.925 1.00 44.06  ?  268 ALA A O   1 
ATOM   2054 C  CB  . ALA A 1 268 ? 50.059 -29.821 -44.448 1.00 40.48  ?  268 ALA A CB  1 
ATOM   2055 N  N   . GLU A 1 269 ? 47.860 -32.063 -43.429 1.00 38.73  ?  269 GLU A N   1 
ATOM   2056 C  CA  . GLU A 1 269 ? 46.516 -32.396 -42.986 1.00 36.89  ?  269 GLU A CA  1 
ATOM   2057 C  C   . GLU A 1 269 ? 46.600 -33.083 -41.628 1.00 38.51  ?  269 GLU A C   1 
ATOM   2058 O  O   . GLU A 1 269 ? 45.759 -32.826 -40.764 1.00 35.57  ?  269 GLU A O   1 
ATOM   2059 C  CB  . GLU A 1 269 ? 45.813 -33.254 -44.036 1.00 37.39  ?  269 GLU A CB  1 
ATOM   2060 C  CG  . GLU A 1 269 ? 45.633 -32.489 -45.338 1.00 37.39  ?  269 GLU A CG  1 
ATOM   2061 C  CD  . GLU A 1 269 ? 45.461 -33.315 -46.578 1.00 38.82  ?  269 GLU A CD  1 
ATOM   2062 O  OE1 . GLU A 1 269 ? 45.426 -34.542 -46.414 1.00 42.44  ?  269 GLU A OE1 1 
ATOM   2063 O  OE2 . GLU A 1 269 ? 45.402 -32.739 -47.688 1.00 42.72  -1 269 GLU A OE2 1 
ATOM   2064 N  N   . ILE A 1 270 ? 47.629 -33.934 -41.460 1.00 38.79  ?  270 ILE A N   1 
ATOM   2065 C  CA  . ILE A 1 270 ? 47.953 -34.544 -40.177 1.00 39.79  ?  270 ILE A CA  1 
ATOM   2066 C  C   . ILE A 1 270 ? 48.343 -33.430 -39.203 1.00 44.90  ?  270 ILE A C   1 
ATOM   2067 O  O   . ILE A 1 270 ? 47.802 -33.358 -38.103 1.00 52.08  ?  270 ILE A O   1 
ATOM   2068 C  CB  . ILE A 1 270 ? 49.066 -35.607 -40.314 1.00 38.60  ?  270 ILE A CB  1 
ATOM   2069 C  CG1 . ILE A 1 270 ? 48.726 -36.698 -41.318 1.00 38.27  ?  270 ILE A CG1 1 
ATOM   2070 C  CG2 . ILE A 1 270 ? 49.431 -36.227 -38.967 1.00 38.26  ?  270 ILE A CG2 1 
ATOM   2071 C  CD1 . ILE A 1 270 ? 47.617 -37.626 -40.872 1.00 38.43  ?  270 ILE A CD1 1 
ATOM   2072 N  N   . ASP A 1 271 ? 49.273 -32.558 -39.626 1.00 48.49  ?  271 ASP A N   1 
ATOM   2073 C  CA  . ASP A 1 271 ? 49.754 -31.440 -38.823 1.00 50.22  ?  271 ASP A CA  1 
ATOM   2074 C  C   . ASP A 1 271 ? 48.583 -30.545 -38.412 1.00 52.11  ?  271 ASP A C   1 
ATOM   2075 O  O   . ASP A 1 271 ? 48.701 -29.762 -37.468 1.00 56.99  ?  271 ASP A O   1 
ATOM   2076 C  CB  . ASP A 1 271 ? 50.817 -30.621 -39.548 1.00 51.83  ?  271 ASP A CB  1 
ATOM   2077 C  CG  . ASP A 1 271 ? 52.204 -31.249 -39.652 1.00 59.08  ?  271 ASP A CG  1 
ATOM   2078 O  OD1 . ASP A 1 271 ? 52.364 -32.371 -39.119 1.00 64.14  ?  271 ASP A OD1 1 
ATOM   2079 O  OD2 . ASP A 1 271 ? 53.120 -30.620 -40.268 1.00 56.98  -1 271 ASP A OD2 1 
ATOM   2080 N  N   . ALA A 1 272 ? 47.465 -30.657 -39.136 1.00 47.00  ?  272 ALA A N   1 
ATOM   2081 C  CA  . ALA A 1 272 ? 46.282 -29.863 -38.860 1.00 49.09  ?  272 ALA A CA  1 
ATOM   2082 C  C   . ALA A 1 272 ? 45.374 -30.589 -37.873 1.00 50.48  ?  272 ALA A C   1 
ATOM   2083 O  O   . ALA A 1 272 ? 44.658 -29.933 -37.124 1.00 60.50  ?  272 ALA A O   1 
ATOM   2084 C  CB  . ALA A 1 272 ? 45.563 -29.543 -40.156 1.00 50.49  ?  272 ALA A CB  1 
ATOM   2085 N  N   . ILE A 1 273 ? 45.395 -31.932 -37.879 1.00 47.63  ?  273 ILE A N   1 
ATOM   2086 C  CA  . ILE A 1 273 ? 44.705 -32.721 -36.860 1.00 40.74  ?  273 ILE A CA  1 
ATOM   2087 C  C   . ILE A 1 273 ? 45.393 -32.552 -35.501 1.00 38.08  ?  273 ILE A C   1 
ATOM   2088 O  O   . ILE A 1 273 ? 44.747 -32.708 -34.472 1.00 33.51  ?  273 ILE A O   1 
ATOM   2089 C  CB  . ILE A 1 273 ? 44.596 -34.207 -37.255 1.00 37.16  ?  273 ILE A CB  1 
ATOM   2090 C  CG1 . ILE A 1 273 ? 43.364 -34.514 -38.104 1.00 37.11  ?  273 ILE A CG1 1 
ATOM   2091 C  CG2 . ILE A 1 273 ? 44.575 -35.097 -36.017 1.00 38.80  ?  273 ILE A CG2 1 
ATOM   2092 C  CD1 . ILE A 1 273 ? 43.467 -34.161 -39.573 1.00 36.95  ?  273 ILE A CD1 1 
ATOM   2093 N  N   . ALA A 1 274 ? 46.697 -32.239 -35.498 1.00 39.80  ?  274 ALA A N   1 
ATOM   2094 C  CA  . ALA A 1 274 ? 47.439 -32.027 -34.264 1.00 44.12  ?  274 ALA A CA  1 
ATOM   2095 C  C   . ALA A 1 274 ? 46.997 -30.722 -33.612 1.00 47.49  ?  274 ALA A C   1 
ATOM   2096 O  O   . ALA A 1 274 ? 46.820 -30.653 -32.399 1.00 54.96  ?  274 ALA A O   1 
ATOM   2097 C  CB  . ALA A 1 274 ? 48.925 -32.038 -34.536 1.00 43.53  ?  274 ALA A CB  1 
ATOM   2098 N  N   . ALA A 1 275 ? 46.786 -29.697 -34.440 1.00 53.20  ?  275 ALA A N   1 
ATOM   2099 C  CA  . ALA A 1 275 ? 46.291 -28.408 -33.975 1.00 58.31  ?  275 ALA A CA  1 
ATOM   2100 C  C   . ALA A 1 275 ? 44.856 -28.536 -33.473 1.00 61.92  ?  275 ALA A C   1 
ATOM   2101 O  O   . ALA A 1 275 ? 44.420 -27.715 -32.667 1.00 69.28  ?  275 ALA A O   1 
ATOM   2102 C  CB  . ALA A 1 275 ? 46.374 -27.365 -35.072 1.00 56.52  ?  275 ALA A CB  1 
ATOM   2103 N  N   . LEU A 1 276 ? 44.123 -29.540 -33.977 1.00 58.24  ?  276 LEU A N   1 
ATOM   2104 C  CA  . LEU A 1 276 ? 42.719 -29.707 -33.632 1.00 61.45  ?  276 LEU A CA  1 
ATOM   2105 C  C   . LEU A 1 276 ? 42.570 -30.361 -32.251 1.00 66.27  ?  276 LEU A C   1 
ATOM   2106 O  O   . LEU A 1 276 ? 41.721 -29.945 -31.462 1.00 65.29  ?  276 LEU A O   1 
ATOM   2107 C  CB  . LEU A 1 276 ? 42.011 -30.446 -34.771 1.00 55.83  ?  276 LEU A CB  1 
ATOM   2108 C  CG  . LEU A 1 276 ? 41.717 -29.579 -36.007 1.00 58.54  ?  276 LEU A CG  1 
ATOM   2109 C  CD1 . LEU A 1 276 ? 41.101 -30.363 -37.161 1.00 58.88  ?  276 LEU A CD1 1 
ATOM   2110 C  CD2 . LEU A 1 276 ? 40.832 -28.369 -35.677 1.00 53.61  ?  276 LEU A CD2 1 
ATOM   2111 N  N   . LYS A 1 277 ? 43.432 -31.336 -31.932 1.00 66.40  ?  277 LYS A N   1 
ATOM   2112 C  CA  . LYS A 1 277 ? 43.416 -31.979 -30.624 1.00 63.09  ?  277 LYS A CA  1 
ATOM   2113 C  C   . LYS A 1 277 ? 43.892 -30.985 -29.563 1.00 59.46  ?  277 LYS A C   1 
ATOM   2114 O  O   . LYS A 1 277 ? 43.265 -30.828 -28.522 1.00 45.24  ?  277 LYS A O   1 
ATOM   2115 C  CB  . LYS A 1 277 ? 44.285 -33.245 -30.602 1.00 64.21  ?  277 LYS A CB  1 
ATOM   2116 C  CG  . LYS A 1 277 ? 44.123 -34.227 -31.758 1.00 59.93  ?  277 LYS A CG  1 
ATOM   2117 C  CD  . LYS A 1 277 ? 42.708 -34.411 -32.299 1.00 56.43  ?  277 LYS A CD  1 
ATOM   2118 C  CE  . LYS A 1 277 ? 41.805 -35.208 -31.417 1.00 52.51  ?  277 LYS A CE  1 
ATOM   2119 N  NZ  . LYS A 1 277 ? 40.435 -35.152 -31.931 1.00 50.68  1  277 LYS A NZ  1 
ATOM   2120 N  N   . VAL A 1 278 ? 45.021 -30.319 -29.835 1.00 67.60  ?  278 VAL A N   1 
ATOM   2121 C  CA  . VAL A 1 278 ? 45.384 -29.105 -29.117 1.00 72.42  ?  278 VAL A CA  1 
ATOM   2122 C  C   . VAL A 1 278 ? 44.288 -28.078 -29.439 1.00 82.25  ?  278 VAL A C   1 
ATOM   2123 O  O   . VAL A 1 278 ? 43.712 -28.119 -30.526 1.00 85.87  ?  278 VAL A O   1 
ATOM   2124 C  CB  . VAL A 1 278 ? 46.821 -28.662 -29.490 1.00 59.05  ?  278 VAL A CB  1 
ATOM   2125 C  CG1 . VAL A 1 278 ? 46.851 -27.540 -30.520 1.00 61.90  ?  278 VAL A CG1 1 
ATOM   2126 C  CG2 . VAL A 1 278 ? 47.635 -28.261 -28.267 1.00 53.81  ?  278 VAL A CG2 1 
ATOM   2127 N  N   . ASP A 1 279 ? 43.941 -27.211 -28.478 1.00 84.62  ?  279 ASP A N   1 
ATOM   2128 C  CA  . ASP A 1 279 ? 42.693 -26.447 -28.523 1.00 87.49  ?  279 ASP A CA  1 
ATOM   2129 C  C   . ASP A 1 279 ? 41.473 -27.384 -28.468 1.00 81.93  ?  279 ASP A C   1 
ATOM   2130 O  O   . ASP A 1 279 ? 40.384 -26.997 -28.884 1.00 83.51  ?  279 ASP A O   1 
ATOM   2131 C  CB  . ASP A 1 279 ? 42.607 -25.495 -29.719 1.00 81.41  ?  279 ASP A CB  1 
ATOM   2132 C  CG  . ASP A 1 279 ? 43.618 -24.353 -29.801 1.00 75.49  ?  279 ASP A CG  1 
ATOM   2133 O  OD1 . ASP A 1 279 ? 43.179 -23.185 -29.897 1.00 67.85  ?  279 ASP A OD1 1 
ATOM   2134 O  OD2 . ASP A 1 279 ? 44.838 -24.628 -29.799 1.00 71.29  -1 279 ASP A OD2 1 
ATOM   2135 N  N   . ARG A 1 280 ? 41.659 -28.617 -27.964 1.00 77.88  ?  280 ARG A N   1 
ATOM   2136 C  CA  . ARG A 1 280 ? 40.598 -29.551 -27.581 1.00 74.55  ?  280 ARG A CA  1 
ATOM   2137 C  C   . ARG A 1 280 ? 39.483 -29.746 -28.618 1.00 67.45  ?  280 ARG A C   1 
ATOM   2138 O  O   . ARG A 1 280 ? 38.434 -30.265 -28.252 1.00 70.02  ?  280 ARG A O   1 
ATOM   2139 C  CB  . ARG A 1 280 ? 39.937 -29.181 -26.245 1.00 75.54  ?  280 ARG A CB  1 
ATOM   2140 C  CG  . ARG A 1 280 ? 39.081 -27.918 -26.206 1.00 79.43  ?  280 ARG A CG  1 
ATOM   2141 C  CD  . ARG A 1 280 ? 39.804 -26.643 -25.759 1.00 75.93  ?  280 ARG A CD  1 
ATOM   2142 N  NE  . ARG A 1 280 ? 40.372 -26.805 -24.417 1.00 76.75  ?  280 ARG A NE  1 
ATOM   2143 C  CZ  . ARG A 1 280 ? 41.620 -27.155 -24.116 1.00 80.47  ?  280 ARG A CZ  1 
ATOM   2144 N  NH1 . ARG A 1 280 ? 42.528 -27.350 -25.058 1.00 79.79  1  280 ARG A NH1 1 
ATOM   2145 N  NH2 . ARG A 1 280 ? 41.958 -27.328 -22.851 1.00 86.13  ?  280 ARG A NH2 1 
ATOM   2146 N  N   . LYS A 1 281 ? 39.710 -29.402 -29.897 1.00 60.13  ?  281 LYS A N   1 
ATOM   2147 C  CA  . LYS A 1 281 ? 38.697 -29.496 -30.944 1.00 57.24  ?  281 LYS A CA  1 
ATOM   2148 C  C   . LYS A 1 281 ? 38.712 -30.889 -31.589 1.00 60.15  ?  281 LYS A C   1 
ATOM   2149 O  O   . LYS A 1 281 ? 39.484 -31.749 -31.175 1.00 53.74  ?  281 LYS A O   1 
ATOM   2150 C  CB  . LYS A 1 281 ? 38.958 -28.373 -31.955 1.00 60.73  ?  281 LYS A CB  1 
ATOM   2151 C  CG  . LYS A 1 281 ? 38.361 -27.005 -31.633 1.00 63.39  ?  281 LYS A CG  1 
ATOM   2152 C  CD  . LYS A 1 281 ? 36.966 -26.773 -32.215 1.00 64.30  ?  281 LYS A CD  1 
ATOM   2153 C  CE  . LYS A 1 281 ? 36.424 -25.397 -31.984 1.00 66.41  ?  281 LYS A CE  1 
ATOM   2154 N  NZ  . LYS A 1 281 ? 37.283 -24.396 -32.628 1.00 70.09  1  281 LYS A NZ  1 
ATOM   2155 N  N   . GLN A 1 282 ? 37.850 -31.101 -32.607 1.00 67.65  ?  282 GLN A N   1 
ATOM   2156 C  CA  . GLN A 1 282 ? 37.542 -32.416 -33.179 1.00 69.02  ?  282 GLN A CA  1 
ATOM   2157 C  C   . GLN A 1 282 ? 38.002 -32.509 -34.641 1.00 65.51  ?  282 GLN A C   1 
ATOM   2158 O  O   . GLN A 1 282 ? 38.618 -31.577 -35.156 1.00 68.45  ?  282 GLN A O   1 
ATOM   2159 C  CB  . GLN A 1 282 ? 36.036 -32.680 -33.039 1.00 68.16  ?  282 GLN A CB  1 
ATOM   2160 C  CG  . GLN A 1 282 ? 35.607 -33.204 -31.669 1.00 64.56  ?  282 GLN A CG  1 
ATOM   2161 C  CD  . GLN A 1 282 ? 35.893 -32.225 -30.548 1.00 67.48  ?  282 GLN A CD  1 
ATOM   2162 O  OE1 . GLN A 1 282 ? 35.625 -31.025 -30.673 1.00 79.17  ?  282 GLN A OE1 1 
ATOM   2163 N  NE2 . GLN A 1 282 ? 36.475 -32.704 -29.456 1.00 61.51  ?  282 GLN A NE2 1 
ATOM   2164 N  N   . ILE A 1 283 ? 37.706 -33.631 -35.319 1.00 57.90  ?  283 ILE A N   1 
ATOM   2165 C  CA  . ILE A 1 283 ? 38.256 -33.885 -36.648 1.00 61.39  ?  283 ILE A CA  1 
ATOM   2166 C  C   . ILE A 1 283 ? 37.337 -33.308 -37.730 1.00 54.46  ?  283 ILE A C   1 
ATOM   2167 O  O   . ILE A 1 283 ? 37.810 -32.883 -38.782 1.00 46.11  ?  283 ILE A O   1 
ATOM   2168 C  CB  . ILE A 1 283 ? 38.531 -35.382 -36.899 1.00 64.92  ?  283 ILE A CB  1 
ATOM   2169 C  CG1 . ILE A 1 283 ? 39.230 -36.072 -35.736 1.00 66.33  ?  283 ILE A CG1 1 
ATOM   2170 C  CG2 . ILE A 1 283 ? 39.333 -35.557 -38.190 1.00 67.60  ?  283 ILE A CG2 1 
ATOM   2171 C  CD1 . ILE A 1 283 ? 39.353 -37.577 -35.906 1.00 70.62  ?  283 ILE A CD1 1 
ATOM   2172 N  N   . ALA A 1 284 ? 36.022 -33.338 -37.488 1.00 59.68  ?  284 ALA A N   1 
ATOM   2173 C  CA  . ALA A 1 284 ? 35.049 -32.631 -38.314 1.00 61.62  ?  284 ALA A CA  1 
ATOM   2174 C  C   . ALA A 1 284 ? 35.545 -31.224 -38.662 1.00 64.13  ?  284 ALA A C   1 
ATOM   2175 O  O   . ALA A 1 284 ? 35.408 -30.796 -39.806 1.00 68.89  ?  284 ALA A O   1 
ATOM   2176 C  CB  . ALA A 1 284 ? 33.707 -32.585 -37.605 1.00 57.04  ?  284 ALA A CB  1 
ATOM   2177 N  N   . GLU A 1 285 ? 36.155 -30.534 -37.683 1.00 65.48  ?  285 GLU A N   1 
ATOM   2178 C  CA  . GLU A 1 285 ? 36.616 -29.152 -37.812 1.00 68.83  ?  285 GLU A CA  1 
ATOM   2179 C  C   . GLU A 1 285 ? 37.482 -28.933 -39.063 1.00 64.67  ?  285 GLU A C   1 
ATOM   2180 O  O   . GLU A 1 285 ? 37.655 -27.794 -39.490 1.00 59.15  ?  285 GLU A O   1 
ATOM   2181 C  CB  . GLU A 1 285 ? 37.433 -28.687 -36.599 1.00 72.66  ?  285 GLU A CB  1 
ATOM   2182 C  CG  . GLU A 1 285 ? 36.917 -29.155 -35.240 1.00 81.06  ?  285 GLU A CG  1 
ATOM   2183 C  CD  . GLU A 1 285 ? 35.554 -28.678 -34.770 1.00 90.97  ?  285 GLU A CD  1 
ATOM   2184 O  OE1 . GLU A 1 285 ? 34.955 -29.436 -33.964 1.00 89.54  ?  285 GLU A OE1 1 
ATOM   2185 O  OE2 . GLU A 1 285 ? 35.120 -27.564 -35.151 1.00 89.65  -1 285 GLU A OE2 1 
ATOM   2186 N  N   . LEU A 1 286 ? 38.063 -30.007 -39.620 1.00 68.88  ?  286 LEU A N   1 
ATOM   2187 C  CA  . LEU A 1 286 ? 38.882 -29.947 -40.826 1.00 72.26  ?  286 LEU A CA  1 
ATOM   2188 C  C   . LEU A 1 286 ? 37.999 -29.869 -42.080 1.00 81.33  ?  286 LEU A C   1 
ATOM   2189 O  O   . LEU A 1 286 ? 38.236 -29.037 -42.962 1.00 71.66  ?  286 LEU A O   1 
ATOM   2190 C  CB  . LEU A 1 286 ? 39.818 -31.163 -40.818 1.00 70.68  ?  286 LEU A CB  1 
ATOM   2191 C  CG  . LEU A 1 286 ? 40.616 -31.456 -42.099 1.00 68.59  ?  286 LEU A CG  1 
ATOM   2192 C  CD1 . LEU A 1 286 ? 42.111 -31.644 -41.849 1.00 60.58  ?  286 LEU A CD1 1 
ATOM   2193 C  CD2 . LEU A 1 286 ? 40.061 -32.693 -42.797 1.00 64.48  ?  286 LEU A CD2 1 
ATOM   2194 N  N   . VAL A 1 287 ? 36.970 -30.734 -42.132 1.00 87.63  ?  287 VAL A N   1 
ATOM   2195 C  CA  . VAL A 1 287 ? 36.027 -30.821 -43.242 1.00 84.41  ?  287 VAL A CA  1 
ATOM   2196 C  C   . VAL A 1 287 ? 35.174 -29.552 -43.275 1.00 81.60  ?  287 VAL A C   1 
ATOM   2197 O  O   . VAL A 1 287 ? 34.571 -29.242 -44.299 1.00 77.49  ?  287 VAL A O   1 
ATOM   2198 C  CB  . VAL A 1 287 ? 35.130 -32.078 -43.161 1.00 89.85  ?  287 VAL A CB  1 
ATOM   2199 C  CG1 . VAL A 1 287 ? 34.292 -32.279 -44.421 1.00 93.64  ?  287 VAL A CG1 1 
ATOM   2200 C  CG2 . VAL A 1 287 ? 35.910 -33.361 -42.876 1.00 88.57  ?  287 VAL A CG2 1 
ATOM   2201 N  N   . THR A 1 288 ? 35.094 -28.847 -42.138 1.00 85.52  ?  288 THR A N   1 
ATOM   2202 C  CA  . THR A 1 288 ? 34.538 -27.500 -42.082 1.00 87.46  ?  288 THR A CA  1 
ATOM   2203 C  C   . THR A 1 288 ? 35.301 -26.598 -43.057 1.00 85.68  ?  288 THR A C   1 
ATOM   2204 O  O   . THR A 1 288 ? 34.693 -26.014 -43.950 1.00 91.39  ?  288 THR A O   1 
ATOM   2205 C  CB  . THR A 1 288 ? 34.567 -26.985 -40.639 1.00 82.25  ?  288 THR A CB  1 
ATOM   2206 O  OG1 . THR A 1 288 ? 33.423 -27.552 -40.009 1.00 74.83  ?  288 THR A OG1 1 
ATOM   2207 C  CG2 . THR A 1 288 ? 34.461 -25.476 -40.512 1.00 82.57  ?  288 THR A CG2 1 
ATOM   2208 N  N   . ASP A 1 289 ? 36.627 -26.499 -42.896 1.00 79.02  ?  289 ASP A N   1 
ATOM   2209 C  CA  . ASP A 1 289 ? 37.464 -25.795 -43.859 1.00 84.49  ?  289 ASP A CA  1 
ATOM   2210 C  C   . ASP A 1 289 ? 37.211 -26.361 -45.257 1.00 82.41  ?  289 ASP A C   1 
ATOM   2211 O  O   . ASP A 1 289 ? 36.998 -27.562 -45.401 1.00 92.84  ?  289 ASP A O   1 
ATOM   2212 C  CB  . ASP A 1 289 ? 38.931 -25.835 -43.452 1.00 87.99  ?  289 ASP A CB  1 
ATOM   2213 C  CG  . ASP A 1 289 ? 39.935 -25.716 -44.590 1.00 93.99  ?  289 ASP A CG  1 
ATOM   2214 O  OD1 . ASP A 1 289 ? 40.562 -24.641 -44.712 1.00 104.30 ?  289 ASP A OD1 1 
ATOM   2215 O  OD2 . ASP A 1 289 ? 40.093 -26.708 -45.332 1.00 103.96 -1 289 ASP A OD2 1 
ATOM   2216 N  N   . ALA A 1 290 ? 37.264 -25.485 -46.274 1.00 75.95  ?  290 ALA A N   1 
ATOM   2217 C  CA  . ALA A 1 290 ? 36.902 -25.809 -47.648 1.00 72.07  ?  290 ALA A CA  1 
ATOM   2218 C  C   . ALA A 1 290 ? 37.950 -26.697 -48.322 1.00 68.42  ?  290 ALA A C   1 
ATOM   2219 O  O   . ALA A 1 290 ? 37.601 -27.682 -48.966 1.00 64.05  ?  290 ALA A O   1 
ATOM   2220 C  CB  . ALA A 1 290 ? 36.700 -24.528 -48.431 1.00 72.96  ?  290 ALA A CB  1 
ATOM   2221 N  N   . ALA A 1 291 ? 39.231 -26.335 -48.174 1.00 73.20  ?  291 ALA A N   1 
ATOM   2222 C  CA  . ALA A 1 291 ? 40.347 -27.032 -48.805 1.00 76.51  ?  291 ALA A CA  1 
ATOM   2223 C  C   . ALA A 1 291 ? 40.414 -28.512 -48.405 1.00 75.72  ?  291 ALA A C   1 
ATOM   2224 O  O   . ALA A 1 291 ? 41.111 -29.290 -49.062 1.00 70.93  ?  291 ALA A O   1 
ATOM   2225 C  CB  . ALA A 1 291 ? 41.645 -26.312 -48.469 1.00 76.19  ?  291 ALA A CB  1 
ATOM   2226 N  N   . PHE A 1 292 ? 39.719 -28.886 -47.315 1.00 73.32  ?  292 PHE A N   1 
ATOM   2227 C  CA  . PHE A 1 292 ? 39.626 -30.269 -46.868 1.00 71.82  ?  292 PHE A CA  1 
ATOM   2228 C  C   . PHE A 1 292 ? 38.166 -30.739 -46.841 1.00 76.66  ?  292 PHE A C   1 
ATOM   2229 O  O   . PHE A 1 292 ? 37.922 -31.941 -46.711 1.00 77.21  ?  292 PHE A O   1 
ATOM   2230 C  CB  . PHE A 1 292 ? 40.335 -30.383 -45.513 1.00 72.05  ?  292 PHE A CB  1 
ATOM   2231 C  CG  . PHE A 1 292 ? 41.823 -30.042 -45.522 1.00 76.34  ?  292 PHE A CG  1 
ATOM   2232 C  CD1 . PHE A 1 292 ? 42.618 -30.306 -46.638 1.00 80.45  ?  292 PHE A CD1 1 
ATOM   2233 C  CD2 . PHE A 1 292 ? 42.429 -29.447 -44.416 1.00 75.58  ?  292 PHE A CD2 1 
ATOM   2234 C  CE1 . PHE A 1 292 ? 43.966 -29.974 -46.654 1.00 79.59  ?  292 PHE A CE1 1 
ATOM   2235 C  CE2 . PHE A 1 292 ? 43.780 -29.121 -44.435 1.00 77.73  ?  292 PHE A CE2 1 
ATOM   2236 C  CZ  . PHE A 1 292 ? 44.545 -29.384 -45.552 1.00 79.30  ?  292 PHE A CZ  1 
ATOM   2237 N  N   . ALA A 1 293 ? 37.202 -29.805 -46.982 1.00 74.23  ?  293 ALA A N   1 
ATOM   2238 C  CA  . ALA A 1 293 ? 35.780 -30.125 -47.090 1.00 68.72  ?  293 ALA A CA  1 
ATOM   2239 C  C   . ALA A 1 293 ? 35.557 -31.208 -48.144 1.00 64.32  ?  293 ALA A C   1 
ATOM   2240 O  O   . ALA A 1 293 ? 34.844 -32.179 -47.898 1.00 58.51  ?  293 ALA A O   1 
ATOM   2241 C  CB  . ALA A 1 293 ? 34.977 -28.883 -47.417 1.00 66.40  ?  293 ALA A CB  1 
ATOM   2242 N  N   . ASP A 1 294 ? 36.154 -30.989 -49.322 1.00 63.83  ?  294 ASP A N   1 
ATOM   2243 C  CA  . ASP A 1 294 ? 36.459 -32.057 -50.260 1.00 62.90  ?  294 ASP A CA  1 
ATOM   2244 C  C   . ASP A 1 294 ? 37.850 -32.607 -49.930 1.00 59.36  ?  294 ASP A C   1 
ATOM   2245 O  O   . ASP A 1 294 ? 38.685 -31.932 -49.320 1.00 49.26  ?  294 ASP A O   1 
ATOM   2246 C  CB  . ASP A 1 294 ? 36.310 -31.604 -51.708 1.00 63.52  ?  294 ASP A CB  1 
ATOM   2247 C  CG  . ASP A 1 294 ? 34.938 -31.065 -52.105 1.00 61.89  ?  294 ASP A CG  1 
ATOM   2248 O  OD1 . ASP A 1 294 ? 34.203 -30.586 -51.197 1.00 56.56  ?  294 ASP A OD1 1 
ATOM   2249 O  OD2 . ASP A 1 294 ? 34.608 -31.148 -53.317 1.00 49.98  -1 294 ASP A OD2 1 
ATOM   2250 N  N   . LYS A 1 295 ? 38.069 -33.858 -50.350 1.00 56.65  ?  295 LYS A N   1 
ATOM   2251 C  CA  . LYS A 1 295 ? 39.248 -34.648 -50.022 1.00 52.87  ?  295 LYS A CA  1 
ATOM   2252 C  C   . LYS A 1 295 ? 38.991 -35.505 -48.776 1.00 53.92  ?  295 LYS A C   1 
ATOM   2253 O  O   . LYS A 1 295 ? 39.765 -36.423 -48.527 1.00 51.46  ?  295 LYS A O   1 
ATOM   2254 C  CB  . LYS A 1 295 ? 40.551 -33.845 -49.880 1.00 49.99  ?  295 LYS A CB  1 
ATOM   2255 C  CG  . LYS A 1 295 ? 41.791 -34.609 -50.339 1.00 48.32  ?  295 LYS A CG  1 
ATOM   2256 C  CD  . LYS A 1 295 ? 43.044 -34.436 -49.490 1.00 50.44  ?  295 LYS A CD  1 
ATOM   2257 C  CE  . LYS A 1 295 ? 43.855 -35.718 -49.458 1.00 54.46  ?  295 LYS A CE  1 
ATOM   2258 N  NZ  . LYS A 1 295 ? 45.260 -35.548 -49.058 1.00 53.46  1  295 LYS A NZ  1 
ATOM   2259 N  N   . PHE A 1 296 ? 37.905 -35.239 -48.015 1.00 58.05  ?  296 PHE A N   1 
ATOM   2260 C  CA  . PHE A 1 296 ? 37.625 -35.970 -46.779 1.00 55.48  ?  296 PHE A CA  1 
ATOM   2261 C  C   . PHE A 1 296 ? 36.125 -36.034 -46.453 1.00 50.95  ?  296 PHE A C   1 
ATOM   2262 O  O   . PHE A 1 296 ? 35.418 -35.050 -46.638 1.00 51.29  ?  296 PHE A O   1 
ATOM   2263 C  CB  . PHE A 1 296 ? 38.401 -35.333 -45.620 1.00 55.02  ?  296 PHE A CB  1 
ATOM   2264 C  CG  . PHE A 1 296 ? 39.912 -35.416 -45.793 1.00 54.19  ?  296 PHE A CG  1 
ATOM   2265 C  CD1 . PHE A 1 296 ? 40.554 -36.646 -45.855 1.00 62.53  ?  296 PHE A CD1 1 
ATOM   2266 C  CD2 . PHE A 1 296 ? 40.680 -34.268 -45.902 1.00 56.77  ?  296 PHE A CD2 1 
ATOM   2267 C  CE1 . PHE A 1 296 ? 41.924 -36.723 -46.034 1.00 69.89  ?  296 PHE A CE1 1 
ATOM   2268 C  CE2 . PHE A 1 296 ? 42.051 -34.345 -46.060 1.00 65.83  ?  296 PHE A CE2 1 
ATOM   2269 C  CZ  . PHE A 1 296 ? 42.670 -35.573 -46.130 1.00 71.61  ?  296 PHE A CZ  1 
ATOM   2270 N  N   A THR A 1 297 ? 35.685 -37.202 -45.948 0.50 49.42  ?  297 THR A N   1 
ATOM   2271 N  N   B THR A 1 297 ? 35.685 -37.202 -45.948 0.50 49.42  ?  297 THR A N   1 
ATOM   2272 C  CA  A THR A 1 297 ? 34.317 -37.459 -45.516 0.50 46.72  ?  297 THR A CA  1 
ATOM   2273 C  CA  B THR A 1 297 ? 34.317 -37.459 -45.516 0.50 46.72  ?  297 THR A CA  1 
ATOM   2274 C  C   A THR A 1 297 ? 34.297 -37.696 -44.005 0.50 46.21  ?  297 THR A C   1 
ATOM   2275 C  C   B THR A 1 297 ? 34.297 -37.696 -44.005 0.50 46.21  ?  297 THR A C   1 
ATOM   2276 O  O   A THR A 1 297 ? 35.026 -38.546 -43.504 0.50 43.03  ?  297 THR A O   1 
ATOM   2277 O  O   B THR A 1 297 ? 35.026 -38.546 -43.504 0.50 43.03  ?  297 THR A O   1 
ATOM   2278 C  CB  A THR A 1 297 ? 33.765 -38.695 -46.229 0.50 45.51  ?  297 THR A CB  1 
ATOM   2279 C  CB  B THR A 1 297 ? 33.765 -38.695 -46.229 0.50 45.51  ?  297 THR A CB  1 
ATOM   2280 O  OG1 A THR A 1 297 ? 34.151 -38.601 -47.595 0.50 45.61  ?  297 THR A OG1 1 
ATOM   2281 O  OG1 B THR A 1 297 ? 34.151 -38.601 -47.595 0.50 45.61  ?  297 THR A OG1 1 
ATOM   2282 C  CG2 A THR A 1 297 ? 32.257 -38.821 -46.097 0.50 44.02  ?  297 THR A CG2 1 
ATOM   2283 C  CG2 B THR A 1 297 ? 32.257 -38.821 -46.097 0.50 44.02  ?  297 THR A CG2 1 
ATOM   2284 N  N   . TYR A 1 298 ? 33.418 -36.975 -43.298 1.00 48.73  ?  298 TYR A N   1 
ATOM   2285 C  CA  . TYR A 1 298 ? 33.165 -37.211 -41.882 1.00 52.58  ?  298 TYR A CA  1 
ATOM   2286 C  C   . TYR A 1 298 ? 31.905 -38.054 -41.684 1.00 56.13  ?  298 TYR A C   1 
ATOM   2287 O  O   . TYR A 1 298 ? 30.840 -37.712 -42.186 1.00 69.66  ?  298 TYR A O   1 
ATOM   2288 C  CB  . TYR A 1 298 ? 32.951 -35.900 -41.128 1.00 52.10  ?  298 TYR A CB  1 
ATOM   2289 C  CG  . TYR A 1 298 ? 32.767 -36.043 -39.623 1.00 54.11  ?  298 TYR A CG  1 
ATOM   2290 C  CD1 . TYR A 1 298 ? 33.721 -36.661 -38.821 1.00 52.63  ?  298 TYR A CD1 1 
ATOM   2291 C  CD2 . TYR A 1 298 ? 31.623 -35.550 -39.003 1.00 61.03  ?  298 TYR A CD2 1 
ATOM   2292 C  CE1 . TYR A 1 298 ? 33.545 -36.763 -37.448 1.00 56.52  ?  298 TYR A CE1 1 
ATOM   2293 C  CE2 . TYR A 1 298 ? 31.435 -35.645 -37.634 1.00 59.46  ?  298 TYR A CE2 1 
ATOM   2294 C  CZ  . TYR A 1 298 ? 32.397 -36.256 -36.857 1.00 59.80  ?  298 TYR A CZ  1 
ATOM   2295 O  OH  . TYR A 1 298 ? 32.137 -36.313 -35.523 1.00 62.15  ?  298 TYR A OH  1 
ATOM   2296 N  N   . LEU A 1 299 ? 32.043 -39.130 -40.903 1.00 55.17  ?  299 LEU A N   1 
ATOM   2297 C  CA  . LEU A 1 299 ? 30.961 -40.029 -40.548 1.00 50.27  ?  299 LEU A CA  1 
ATOM   2298 C  C   . LEU A 1 299 ? 30.844 -40.007 -39.026 1.00 49.09  ?  299 LEU A C   1 
ATOM   2299 O  O   . LEU A 1 299 ? 31.606 -40.684 -38.346 1.00 42.88  ?  299 LEU A O   1 
ATOM   2300 C  CB  . LEU A 1 299 ? 31.279 -41.438 -41.052 1.00 50.58  ?  299 LEU A CB  1 
ATOM   2301 C  CG  . LEU A 1 299 ? 31.983 -41.545 -42.410 1.00 52.08  ?  299 LEU A CG  1 
ATOM   2302 C  CD1 . LEU A 1 299 ? 32.369 -42.986 -42.713 1.00 49.81  ?  299 LEU A CD1 1 
ATOM   2303 C  CD2 . LEU A 1 299 ? 31.130 -40.982 -43.535 1.00 54.02  ?  299 LEU A CD2 1 
ATOM   2304 N  N   . PRO A 1 300 ? 29.915 -39.223 -38.430 1.00 48.06  ?  300 PRO A N   1 
ATOM   2305 C  CA  . PRO A 1 300 ? 29.791 -39.182 -36.967 1.00 42.49  ?  300 PRO A CA  1 
ATOM   2306 C  C   . PRO A 1 300 ? 29.461 -40.552 -36.369 1.00 39.23  ?  300 PRO A C   1 
ATOM   2307 O  O   . PRO A 1 300 ? 28.780 -41.346 -37.003 1.00 39.69  ?  300 PRO A O   1 
ATOM   2308 C  CB  . PRO A 1 300 ? 28.668 -38.149 -36.756 1.00 44.50  ?  300 PRO A CB  1 
ATOM   2309 C  CG  . PRO A 1 300 ? 27.888 -38.150 -38.061 1.00 45.03  ?  300 PRO A CG  1 
ATOM   2310 C  CD  . PRO A 1 300 ? 28.936 -38.370 -39.131 1.00 45.46  ?  300 PRO A CD  1 
ATOM   2311 N  N   . GLY A 1 301 ? 29.978 -40.839 -35.166 1.00 37.18  ?  301 GLY A N   1 
ATOM   2312 C  CA  . GLY A 1 301 ? 29.646 -42.051 -34.427 1.00 37.20  ?  301 GLY A CA  1 
ATOM   2313 C  C   . GLY A 1 301 ? 30.240 -43.348 -34.992 1.00 38.31  ?  301 GLY A C   1 
ATOM   2314 O  O   . GLY A 1 301 ? 29.885 -44.436 -34.522 1.00 34.44  ?  301 GLY A O   1 
ATOM   2315 N  N   . GLN A 1 302 ? 31.175 -43.243 -35.949 1.00 37.80  ?  302 GLN A N   1 
ATOM   2316 C  CA  . GLN A 1 302 ? 31.625 -44.396 -36.719 1.00 36.76  ?  302 GLN A CA  1 
ATOM   2317 C  C   . GLN A 1 302 ? 33.121 -44.685 -36.555 1.00 41.30  ?  302 GLN A C   1 
ATOM   2318 O  O   . GLN A 1 302 ? 33.934 -43.789 -36.277 1.00 39.00  ?  302 GLN A O   1 
ATOM   2319 C  CB  . GLN A 1 302 ? 31.404 -44.193 -38.215 1.00 35.39  ?  302 GLN A CB  1 
ATOM   2320 C  CG  . GLN A 1 302 ? 29.948 -44.273 -38.633 1.00 35.92  ?  302 GLN A CG  1 
ATOM   2321 C  CD  . GLN A 1 302 ? 29.238 -45.449 -38.002 1.00 32.56  ?  302 GLN A CD  1 
ATOM   2322 O  OE1 . GLN A 1 302 ? 28.591 -45.299 -36.962 1.00 32.87  ?  302 GLN A OE1 1 
ATOM   2323 N  NE2 . GLN A 1 302 ? 29.375 -46.621 -38.601 1.00 28.07  ?  302 GLN A NE2 1 
ATOM   2324 N  N   . ARG A 1 303 ? 33.443 -45.970 -36.792 1.00 38.09  ?  303 ARG A N   1 
ATOM   2325 C  CA  . ARG A 1 303 ? 34.788 -46.514 -36.746 1.00 37.65  ?  303 ARG A CA  1 
ATOM   2326 C  C   . ARG A 1 303 ? 35.175 -46.974 -38.150 1.00 36.05  ?  303 ARG A C   1 
ATOM   2327 O  O   . ARG A 1 303 ? 34.438 -47.719 -38.791 1.00 39.01  ?  303 ARG A O   1 
ATOM   2328 C  CB  . ARG A 1 303 ? 34.782 -47.673 -35.737 1.00 36.30  ?  303 ARG A CB  1 
ATOM   2329 C  CG  . ARG A 1 303 ? 34.613 -47.194 -34.305 1.00 34.00  ?  303 ARG A CG  1 
ATOM   2330 C  CD  . ARG A 1 303 ? 33.569 -47.961 -33.554 1.00 33.27  ?  303 ARG A CD  1 
ATOM   2331 N  NE  . ARG A 1 303 ? 33.981 -49.348 -33.323 1.00 33.17  ?  303 ARG A NE  1 
ATOM   2332 C  CZ  . ARG A 1 303 ? 34.214 -49.922 -32.143 1.00 30.19  ?  303 ARG A CZ  1 
ATOM   2333 N  NH1 . ARG A 1 303 ? 34.510 -51.209 -32.086 1.00 31.93  1  303 ARG A NH1 1 
ATOM   2334 N  NH2 . ARG A 1 303 ? 34.154 -49.225 -31.030 1.00 27.00  ?  303 ARG A NH2 1 
ATOM   2335 N  N   . PRO A 1 304 ? 36.379 -46.629 -38.642 1.00 35.15  ?  304 PRO A N   1 
ATOM   2336 C  CA  . PRO A 1 304 ? 36.666 -46.715 -40.081 1.00 37.17  ?  304 PRO A CA  1 
ATOM   2337 C  C   . PRO A 1 304 ? 36.616 -48.102 -40.743 1.00 36.71  ?  304 PRO A C   1 
ATOM   2338 O  O   . PRO A 1 304 ? 36.609 -48.214 -41.972 1.00 26.56  ?  304 PRO A O   1 
ATOM   2339 C  CB  . PRO A 1 304 ? 38.092 -46.094 -40.166 1.00 38.44  ?  304 PRO A CB  1 
ATOM   2340 C  CG  . PRO A 1 304 ? 38.706 -46.327 -38.796 1.00 39.07  ?  304 PRO A CG  1 
ATOM   2341 C  CD  . PRO A 1 304 ? 37.536 -46.227 -37.828 1.00 38.37  ?  304 PRO A CD  1 
ATOM   2342 N  N   . TRP A 1 305 ? 36.563 -49.161 -39.917 1.00 42.67  ?  305 TRP A N   1 
ATOM   2343 C  CA  . TRP A 1 305 ? 36.992 -50.487 -40.342 1.00 41.41  ?  305 TRP A CA  1 
ATOM   2344 C  C   . TRP A 1 305 ? 36.283 -50.867 -41.636 1.00 39.81  ?  305 TRP A C   1 
ATOM   2345 O  O   . TRP A 1 305 ? 36.945 -51.374 -42.541 1.00 37.92  ?  305 TRP A O   1 
ATOM   2346 C  CB  . TRP A 1 305 ? 36.816 -51.523 -39.215 1.00 39.67  ?  305 TRP A CB  1 
ATOM   2347 C  CG  . TRP A 1 305 ? 37.552 -51.154 -37.949 1.00 40.01  ?  305 TRP A CG  1 
ATOM   2348 C  CD1 . TRP A 1 305 ? 37.127 -51.302 -36.655 1.00 39.66  ?  305 TRP A CD1 1 
ATOM   2349 C  CD2 . TRP A 1 305 ? 38.857 -50.536 -37.871 1.00 39.48  ?  305 TRP A CD2 1 
ATOM   2350 N  NE1 . TRP A 1 305 ? 38.064 -50.821 -35.777 1.00 38.36  ?  305 TRP A NE1 1 
ATOM   2351 C  CE2 . TRP A 1 305 ? 39.137 -50.351 -36.496 1.00 40.48  ?  305 TRP A CE2 1 
ATOM   2352 C  CE3 . TRP A 1 305 ? 39.811 -50.141 -38.819 1.00 40.94  ?  305 TRP A CE3 1 
ATOM   2353 C  CZ2 . TRP A 1 305 ? 40.329 -49.775 -36.063 1.00 41.23  ?  305 TRP A CZ2 1 
ATOM   2354 C  CZ3 . TRP A 1 305 ? 41.003 -49.602 -38.388 1.00 42.72  ?  305 TRP A CZ3 1 
ATOM   2355 C  CH2 . TRP A 1 305 ? 41.248 -49.408 -37.028 1.00 44.43  ?  305 TRP A CH2 1 
ATOM   2356 N  N   . VAL A 1 306 ? 34.985 -50.518 -41.735 1.00 39.99  ?  306 VAL A N   1 
ATOM   2357 C  CA  . VAL A 1 306 ? 34.137 -50.905 -42.859 1.00 37.28  ?  306 VAL A CA  1 
ATOM   2358 C  C   . VAL A 1 306 ? 33.878 -49.757 -43.846 1.00 35.26  ?  306 VAL A C   1 
ATOM   2359 O  O   . VAL A 1 306 ? 33.375 -50.012 -44.935 1.00 37.97  ?  306 VAL A O   1 
ATOM   2360 C  CB  . VAL A 1 306 ? 32.820 -51.481 -42.301 1.00 39.06  ?  306 VAL A CB  1 
ATOM   2361 C  CG1 . VAL A 1 306 ? 33.088 -52.541 -41.238 1.00 36.38  ?  306 VAL A CG1 1 
ATOM   2362 C  CG2 . VAL A 1 306 ? 31.879 -50.397 -41.761 1.00 43.48  ?  306 VAL A CG2 1 
ATOM   2363 N  N   . HIS A 1 307 ? 34.217 -48.502 -43.515 1.00 34.63  ?  307 HIS A N   1 
ATOM   2364 C  CA  . HIS A 1 307 ? 33.866 -47.375 -44.379 1.00 37.17  ?  307 HIS A CA  1 
ATOM   2365 C  C   . HIS A 1 307 ? 34.957 -47.053 -45.410 1.00 37.90  ?  307 HIS A C   1 
ATOM   2366 O  O   . HIS A 1 307 ? 34.792 -46.138 -46.221 1.00 33.35  ?  307 HIS A O   1 
ATOM   2367 C  CB  . HIS A 1 307 ? 33.463 -46.149 -43.546 1.00 36.24  ?  307 HIS A CB  1 
ATOM   2368 C  CG  . HIS A 1 307 ? 32.373 -46.478 -42.597 1.00 41.58  ?  307 HIS A CG  1 
ATOM   2369 N  ND1 . HIS A 1 307 ? 31.196 -47.034 -43.054 1.00 47.11  ?  307 HIS A ND1 1 
ATOM   2370 C  CD2 . HIS A 1 307 ? 32.295 -46.473 -41.263 1.00 44.49  ?  307 HIS A CD2 1 
ATOM   2371 C  CE1 . HIS A 1 307 ? 30.411 -47.306 -42.025 1.00 47.37  ?  307 HIS A CE1 1 
ATOM   2372 N  NE2 . HIS A 1 307 ? 31.058 -46.969 -40.929 1.00 50.23  ?  307 HIS A NE2 1 
ATOM   2373 N  N   A VAL A 1 308 ? 36.048 -47.834 -45.398 0.50 39.94  ?  308 VAL A N   1 
ATOM   2374 N  N   B VAL A 1 308 ? 36.039 -47.847 -45.401 0.50 38.25  ?  308 VAL A N   1 
ATOM   2375 C  CA  A VAL A 1 308 ? 37.298 -47.444 -46.040 0.50 38.91  ?  308 VAL A CA  1 
ATOM   2376 C  CA  B VAL A 1 308 ? 37.304 -47.465 -46.018 0.50 36.21  ?  308 VAL A CA  1 
ATOM   2377 C  C   A VAL A 1 308 ? 37.405 -48.042 -47.441 0.50 36.29  ?  308 VAL A C   1 
ATOM   2378 C  C   B VAL A 1 308 ? 37.439 -48.064 -47.417 0.50 34.89  ?  308 VAL A C   1 
ATOM   2379 O  O   A VAL A 1 308 ? 38.011 -47.442 -48.323 0.50 37.23  ?  308 VAL A O   1 
ATOM   2380 O  O   B VAL A 1 308 ? 38.092 -47.481 -48.277 0.50 36.00  ?  308 VAL A O   1 
ATOM   2381 C  CB  A VAL A 1 308 ? 38.504 -47.853 -45.171 0.50 37.75  ?  308 VAL A CB  1 
ATOM   2382 C  CB  B VAL A 1 308 ? 38.478 -47.876 -45.106 0.50 33.08  ?  308 VAL A CB  1 
ATOM   2383 C  CG1 A VAL A 1 308 ? 38.262 -49.174 -44.456 0.50 37.76  ?  308 VAL A CG1 1 
ATOM   2384 C  CG1 B VAL A 1 308 ? 39.731 -48.211 -45.907 0.50 33.15  ?  308 VAL A CG1 1 
ATOM   2385 C  CG2 A VAL A 1 308 ? 39.791 -47.906 -45.986 0.50 38.07  ?  308 VAL A CG2 1 
ATOM   2386 C  CG2 B VAL A 1 308 ? 38.764 -46.813 -44.050 0.50 31.12  ?  308 VAL A CG2 1 
ATOM   2387 N  N   . GLY A 1 309 ? 36.828 -49.230 -47.639 1.00 36.33  ?  309 GLY A N   1 
ATOM   2388 C  CA  . GLY A 1 309 ? 36.886 -49.905 -48.921 1.00 33.71  ?  309 GLY A CA  1 
ATOM   2389 C  C   . GLY A 1 309 ? 37.946 -50.986 -48.849 1.00 34.25  ?  309 GLY A C   1 
ATOM   2390 O  O   . GLY A 1 309 ? 37.989 -51.714 -47.862 1.00 31.45  ?  309 GLY A O   1 
ATOM   2391 N  N   . ALA A 1 310 ? 38.819 -51.000 -49.863 1.00 38.96  ?  310 ALA A N   1 
ATOM   2392 C  CA  . ALA A 1 310 ? 39.816 -52.037 -50.063 1.00 42.25  ?  310 ALA A CA  1 
ATOM   2393 C  C   . ALA A 1 310 ? 41.111 -51.675 -49.332 1.00 41.92  ?  310 ALA A C   1 
ATOM   2394 O  O   . ALA A 1 310 ? 41.807 -50.762 -49.759 1.00 42.15  ?  310 ALA A O   1 
ATOM   2395 C  CB  . ALA A 1 310 ? 40.045 -52.185 -51.557 1.00 44.66  ?  310 ALA A CB  1 
ATOM   2396 N  N   . VAL A 1 311 ? 41.458 -52.411 -48.260 1.00 38.33  ?  311 VAL A N   1 
ATOM   2397 C  CA  . VAL A 1 311 ? 42.562 -52.012 -47.400 1.00 33.59  ?  311 VAL A CA  1 
ATOM   2398 C  C   . VAL A 1 311 ? 43.514 -53.179 -47.107 1.00 34.05  ?  311 VAL A C   1 
ATOM   2399 O  O   . VAL A 1 311 ? 43.132 -54.348 -47.099 1.00 31.24  ?  311 VAL A O   1 
ATOM   2400 C  CB  . VAL A 1 311 ? 41.961 -51.393 -46.122 1.00 33.62  ?  311 VAL A CB  1 
ATOM   2401 C  CG1 . VAL A 1 311 ? 41.589 -52.446 -45.084 1.00 33.96  ?  311 VAL A CG1 1 
ATOM   2402 C  CG2 . VAL A 1 311 ? 42.875 -50.329 -45.518 1.00 32.44  ?  311 VAL A CG2 1 
ATOM   2403 N  N   . ASP A 1 312 ? 44.788 -52.831 -46.869 1.00 36.39  ?  312 ASP A N   1 
ATOM   2404 C  CA  . ASP A 1 312 ? 45.859 -53.792 -46.663 1.00 38.44  ?  312 ASP A CA  1 
ATOM   2405 C  C   . ASP A 1 312 ? 46.315 -53.790 -45.202 1.00 38.46  ?  312 ASP A C   1 
ATOM   2406 O  O   . ASP A 1 312 ? 46.585 -54.848 -44.646 1.00 38.93  ?  312 ASP A O   1 
ATOM   2407 C  CB  . ASP A 1 312 ? 47.055 -53.497 -47.556 1.00 44.92  ?  312 ASP A CB  1 
ATOM   2408 C  CG  . ASP A 1 312 ? 46.787 -53.385 -49.051 1.00 48.31  ?  312 ASP A CG  1 
ATOM   2409 O  OD1 . ASP A 1 312 ? 46.231 -54.359 -49.610 1.00 45.26  ?  312 ASP A OD1 1 
ATOM   2410 O  OD2 . ASP A 1 312 ? 47.173 -52.335 -49.645 1.00 46.99  -1 312 ASP A OD2 1 
ATOM   2411 N  N   . VAL A 1 313 ? 46.449 -52.607 -44.584 1.00 39.32  ?  313 VAL A N   1 
ATOM   2412 C  CA  . VAL A 1 313 ? 46.985 -52.526 -43.232 1.00 39.76  ?  313 VAL A CA  1 
ATOM   2413 C  C   . VAL A 1 313 ? 46.049 -51.716 -42.337 1.00 42.15  ?  313 VAL A C   1 
ATOM   2414 O  O   . VAL A 1 313 ? 45.564 -50.655 -42.727 1.00 43.57  ?  313 VAL A O   1 
ATOM   2415 C  CB  . VAL A 1 313 ? 48.402 -51.933 -43.180 1.00 39.30  ?  313 VAL A CB  1 
ATOM   2416 C  CG1 . VAL A 1 313 ? 48.996 -52.086 -41.791 1.00 39.27  ?  313 VAL A CG1 1 
ATOM   2417 C  CG2 . VAL A 1 313 ? 49.327 -52.551 -44.225 1.00 41.13  ?  313 VAL A CG2 1 
ATOM   2418 N  N   . ALA A 1 314 ? 45.857 -52.227 -41.113 1.00 40.69  ?  314 ALA A N   1 
ATOM   2419 C  CA  . ALA A 1 314 ? 44.953 -51.672 -40.118 1.00 35.95  ?  314 ALA A CA  1 
ATOM   2420 C  C   . ALA A 1 314 ? 45.731 -51.425 -38.829 1.00 34.69  ?  314 ALA A C   1 
ATOM   2421 O  O   . ALA A 1 314 ? 46.341 -52.341 -38.283 1.00 35.03  ?  314 ALA A O   1 
ATOM   2422 C  CB  . ALA A 1 314 ? 43.814 -52.647 -39.891 1.00 36.38  ?  314 ALA A CB  1 
ATOM   2423 N  N   . LEU A 1 315 ? 45.715 -50.190 -38.328 1.00 33.13  ?  315 LEU A N   1 
ATOM   2424 C  CA  . LEU A 1 315 ? 46.482 -49.877 -37.136 1.00 32.98  ?  315 LEU A CA  1 
ATOM   2425 C  C   . LEU A 1 315 ? 45.591 -49.229 -36.074 1.00 36.63  ?  315 LEU A C   1 
ATOM   2426 O  O   . LEU A 1 315 ? 45.629 -48.013 -35.886 1.00 43.74  ?  315 LEU A O   1 
ATOM   2427 C  CB  . LEU A 1 315 ? 47.632 -48.977 -37.589 1.00 30.16  ?  315 LEU A CB  1 
ATOM   2428 C  CG  . LEU A 1 315 ? 48.512 -49.542 -38.708 1.00 26.55  ?  315 LEU A CG  1 
ATOM   2429 C  CD1 . LEU A 1 315 ? 49.486 -48.521 -39.257 1.00 27.38  ?  315 LEU A CD1 1 
ATOM   2430 C  CD2 . LEU A 1 315 ? 49.286 -50.736 -38.210 1.00 25.87  ?  315 LEU A CD2 1 
ATOM   2431 N  N   . PRO A 1 316 ? 44.781 -50.008 -35.320 1.00 32.61  ?  316 PRO A N   1 
ATOM   2432 C  CA  . PRO A 1 316 ? 43.945 -49.439 -34.255 1.00 33.17  ?  316 PRO A CA  1 
ATOM   2433 C  C   . PRO A 1 316 ? 44.809 -48.708 -33.229 1.00 35.08  ?  316 PRO A C   1 
ATOM   2434 O  O   . PRO A 1 316 ? 45.733 -49.305 -32.681 1.00 35.03  ?  316 PRO A O   1 
ATOM   2435 C  CB  . PRO A 1 316 ? 43.268 -50.679 -33.652 1.00 32.20  ?  316 PRO A CB  1 
ATOM   2436 C  CG  . PRO A 1 316 ? 44.214 -51.806 -33.995 1.00 31.90  ?  316 PRO A CG  1 
ATOM   2437 C  CD  . PRO A 1 316 ? 44.698 -51.468 -35.390 1.00 31.46  ?  316 PRO A CD  1 
ATOM   2438 N  N   . SER A 1 317 ? 44.528 -47.422 -32.978 1.00 35.02  ?  317 SER A N   1 
ATOM   2439 C  CA  . SER A 1 317 ? 45.450 -46.605 -32.199 1.00 32.56  ?  317 SER A CA  1 
ATOM   2440 C  C   . SER A 1 317 ? 44.747 -45.571 -31.325 1.00 33.24  ?  317 SER A C   1 
ATOM   2441 O  O   . SER A 1 317 ? 45.410 -44.631 -30.909 1.00 34.11  ?  317 SER A O   1 
ATOM   2442 C  CB  . SER A 1 317 ? 46.440 -45.958 -33.111 1.00 32.33  ?  317 SER A CB  1 
ATOM   2443 O  OG  . SER A 1 317 ? 47.055 -46.969 -33.903 1.00 33.44  ?  317 SER A OG  1 
ATOM   2444 N  N   . ALA A 1 318 ? 43.463 -45.810 -30.977 1.00 36.38  ?  318 ALA A N   1 
ATOM   2445 C  CA  . ALA A 1 318 ? 42.583 -44.853 -30.310 1.00 35.91  ?  318 ALA A CA  1 
ATOM   2446 C  C   . ALA A 1 318 ? 42.268 -45.279 -28.870 1.00 38.87  ?  318 ALA A C   1 
ATOM   2447 O  O   . ALA A 1 318 ? 42.746 -44.663 -27.929 1.00 40.38  ?  318 ALA A O   1 
ATOM   2448 C  CB  . ALA A 1 318 ? 41.308 -44.722 -31.113 1.00 37.59  ?  318 ALA A CB  1 
ATOM   2449 N  N   . THR A 1 319 ? 41.450 -46.327 -28.698 1.00 40.36  ?  319 THR A N   1 
ATOM   2450 C  CA  . THR A 1 319 ? 41.126 -46.890 -27.391 1.00 38.84  ?  319 THR A CA  1 
ATOM   2451 C  C   . THR A 1 319 ? 41.267 -48.416 -27.434 1.00 38.81  ?  319 THR A C   1 
ATOM   2452 O  O   . THR A 1 319 ? 41.682 -48.987 -28.442 1.00 35.13  ?  319 THR A O   1 
ATOM   2453 C  CB  . THR A 1 319 ? 39.685 -46.528 -27.012 1.00 36.16  ?  319 THR A CB  1 
ATOM   2454 O  OG1 . THR A 1 319 ? 39.305 -45.577 -28.000 1.00 34.85  ?  319 THR A OG1 1 
ATOM   2455 C  CG2 . THR A 1 319 ? 39.518 -46.047 -25.577 1.00 32.46  ?  319 THR A CG2 1 
ATOM   2456 N  N   . GLN A 1 320 ? 40.858 -49.049 -26.321 1.00 39.26  ?  320 GLN A N   1 
ATOM   2457 C  CA  . GLN A 1 320 ? 40.736 -50.491 -26.183 1.00 40.91  ?  320 GLN A CA  1 
ATOM   2458 C  C   . GLN A 1 320 ? 39.377 -50.914 -26.727 1.00 37.70  ?  320 GLN A C   1 
ATOM   2459 O  O   . GLN A 1 320 ? 38.445 -50.119 -26.759 1.00 34.53  ?  320 GLN A O   1 
ATOM   2460 C  CB  . GLN A 1 320 ? 40.867 -50.990 -24.739 1.00 46.40  ?  320 GLN A CB  1 
ATOM   2461 C  CG  . GLN A 1 320 ? 40.364 -50.029 -23.663 1.00 50.98  ?  320 GLN A CG  1 
ATOM   2462 C  CD  . GLN A 1 320 ? 41.318 -48.890 -23.365 1.00 59.02  ?  320 GLN A CD  1 
ATOM   2463 O  OE1 . GLN A 1 320 ? 40.914 -47.833 -22.863 1.00 57.93  ?  320 GLN A OE1 1 
ATOM   2464 N  NE2 . GLN A 1 320 ? 42.590 -49.064 -23.712 1.00 66.24  ?  320 GLN A NE2 1 
ATOM   2465 N  N   . ASN A 1 321 ? 39.296 -52.168 -27.180 1.00 37.55  ?  321 ASN A N   1 
ATOM   2466 C  CA  . ASN A 1 321 ? 38.042 -52.780 -27.593 1.00 39.77  ?  321 ASN A CA  1 
ATOM   2467 C  C   . ASN A 1 321 ? 37.389 -51.953 -28.712 1.00 38.99  ?  321 ASN A C   1 
ATOM   2468 O  O   . ASN A 1 321 ? 36.164 -51.840 -28.785 1.00 40.83  ?  321 ASN A O   1 
ATOM   2469 C  CB  . ASN A 1 321 ? 37.180 -53.051 -26.359 1.00 39.70  ?  321 ASN A CB  1 
ATOM   2470 C  CG  . ASN A 1 321 ? 37.930 -53.857 -25.312 1.00 40.17  ?  321 ASN A CG  1 
ATOM   2471 O  OD1 . ASN A 1 321 ? 38.432 -54.946 -25.604 1.00 34.19  ?  321 ASN A OD1 1 
ATOM   2472 N  ND2 . ASN A 1 321 ? 38.029 -53.352 -24.089 1.00 39.78  ?  321 ASN A ND2 1 
ATOM   2473 N  N   . GLU A 1 322 ? 38.211 -51.442 -29.637 1.00 39.02  ?  322 GLU A N   1 
ATOM   2474 C  CA  . GLU A 1 322 ? 37.736 -50.606 -30.730 1.00 44.38  ?  322 GLU A CA  1 
ATOM   2475 C  C   . GLU A 1 322 ? 37.568 -51.412 -32.015 1.00 45.42  ?  322 GLU A C   1 
ATOM   2476 O  O   . GLU A 1 322 ? 37.314 -50.810 -33.056 1.00 42.31  ?  322 GLU A O   1 
ATOM   2477 C  CB  . GLU A 1 322 ? 38.689 -49.434 -30.997 1.00 50.63  ?  322 GLU A CB  1 
ATOM   2478 C  CG  . GLU A 1 322 ? 40.095 -49.811 -31.479 1.00 51.80  ?  322 GLU A CG  1 
ATOM   2479 C  CD  . GLU A 1 322 ? 40.969 -48.591 -31.768 1.00 52.18  ?  322 GLU A CD  1 
ATOM   2480 O  OE1 . GLU A 1 322 ? 42.144 -48.452 -31.321 1.00 48.27  ?  322 GLU A OE1 1 
ATOM   2481 O  OE2 . GLU A 1 322 ? 40.413 -47.732 -32.479 1.00 45.23  -1 322 GLU A OE2 1 
ATOM   2482 N  N   . VAL A 1 323 ? 37.738 -52.750 -31.941 1.00 52.20  ?  323 VAL A N   1 
ATOM   2483 C  CA  . VAL A 1 323 ? 37.579 -53.654 -33.084 1.00 52.15  ?  323 VAL A CA  1 
ATOM   2484 C  C   . VAL A 1 323 ? 36.761 -54.893 -32.685 1.00 54.51  ?  323 VAL A C   1 
ATOM   2485 O  O   . VAL A 1 323 ? 37.246 -55.747 -31.930 1.00 52.68  ?  323 VAL A O   1 
ATOM   2486 C  CB  . VAL A 1 323 ? 38.922 -54.101 -33.692 1.00 45.04  ?  323 VAL A CB  1 
ATOM   2487 C  CG1 . VAL A 1 323 ? 38.712 -54.877 -34.982 1.00 44.65  ?  323 VAL A CG1 1 
ATOM   2488 C  CG2 . VAL A 1 323 ? 39.869 -52.932 -33.925 1.00 46.60  ?  323 VAL A CG2 1 
ATOM   2489 N  N   . SER A 1 324 ? 35.539 -55.006 -33.240 1.00 48.26  ?  324 SER A N   1 
ATOM   2490 C  CA  . SER A 1 324 ? 34.669 -56.139 -32.965 1.00 47.74  ?  324 SER A CA  1 
ATOM   2491 C  C   . SER A 1 324 ? 35.003 -57.289 -33.910 1.00 48.35  ?  324 SER A C   1 
ATOM   2492 O  O   . SER A 1 324 ? 35.760 -57.098 -34.858 1.00 54.39  ?  324 SER A O   1 
ATOM   2493 C  CB  . SER A 1 324 ? 33.212 -55.759 -33.053 1.00 46.01  ?  324 SER A CB  1 
ATOM   2494 O  OG  . SER A 1 324 ? 32.745 -55.777 -34.391 1.00 43.62  ?  324 SER A OG  1 
ATOM   2495 N  N   . GLY A 1 325 ? 34.425 -58.467 -33.634 1.00 46.46  ?  325 GLY A N   1 
ATOM   2496 C  CA  . GLY A 1 325 ? 34.560 -59.636 -34.489 1.00 49.99  ?  325 GLY A CA  1 
ATOM   2497 C  C   . GLY A 1 325 ? 33.913 -59.427 -35.860 1.00 58.97  ?  325 GLY A C   1 
ATOM   2498 O  O   . GLY A 1 325 ? 34.321 -60.064 -36.834 1.00 67.29  ?  325 GLY A O   1 
ATOM   2499 N  N   . GLU A 1 326 ? 32.891 -58.553 -35.919 1.00 58.20  ?  326 GLU A N   1 
ATOM   2500 C  CA  . GLU A 1 326 ? 32.256 -58.150 -37.169 1.00 51.91  ?  326 GLU A CA  1 
ATOM   2501 C  C   . GLU A 1 326 ? 33.259 -57.363 -38.015 1.00 50.83  ?  326 GLU A C   1 
ATOM   2502 O  O   . GLU A 1 326 ? 33.425 -57.653 -39.200 1.00 58.37  ?  326 GLU A O   1 
ATOM   2503 C  CB  . GLU A 1 326 ? 30.950 -57.406 -36.855 1.00 51.78  ?  326 GLU A CB  1 
ATOM   2504 C  CG  . GLU A 1 326 ? 30.616 -56.247 -37.801 1.00 56.52  ?  326 GLU A CG  1 
ATOM   2505 C  CD  . GLU A 1 326 ? 29.999 -54.993 -37.161 1.00 59.59  ?  326 GLU A CD  1 
ATOM   2506 O  OE1 . GLU A 1 326 ? 29.047 -54.414 -37.748 1.00 54.25  ?  326 GLU A OE1 1 
ATOM   2507 O  OE2 . GLU A 1 326 ? 30.469 -54.570 -36.069 1.00 58.05  -1 326 GLU A OE2 1 
ATOM   2508 N  N   . GLU A 1 327 ? 33.939 -56.387 -37.388 1.00 48.75  ?  327 GLU A N   1 
ATOM   2509 C  CA  . GLU A 1 327 ? 34.765 -55.400 -38.081 1.00 41.88  ?  327 GLU A CA  1 
ATOM   2510 C  C   . GLU A 1 327 ? 36.034 -56.100 -38.568 1.00 37.76  ?  327 GLU A C   1 
ATOM   2511 O  O   . GLU A 1 327 ? 36.579 -55.783 -39.617 1.00 35.05  ?  327 GLU A O   1 
ATOM   2512 C  CB  . GLU A 1 327 ? 35.056 -54.211 -37.156 1.00 38.66  ?  327 GLU A CB  1 
ATOM   2513 C  CG  . GLU A 1 327 ? 33.804 -53.566 -36.561 1.00 38.54  ?  327 GLU A CG  1 
ATOM   2514 C  CD  . GLU A 1 327 ? 33.940 -52.393 -35.588 1.00 38.34  ?  327 GLU A CD  1 
ATOM   2515 O  OE1 . GLU A 1 327 ? 34.561 -52.572 -34.520 1.00 34.89  ?  327 GLU A OE1 1 
ATOM   2516 O  OE2 . GLU A 1 327 ? 33.367 -51.305 -35.868 1.00 38.83  -1 327 GLU A OE2 1 
ATOM   2517 N  N   . ALA A 1 328 ? 36.462 -57.095 -37.799 1.00 36.55  ?  328 ALA A N   1 
ATOM   2518 C  CA  . ALA A 1 328 ? 37.542 -57.979 -38.195 1.00 42.50  ?  328 ALA A CA  1 
ATOM   2519 C  C   . ALA A 1 328 ? 37.247 -58.683 -39.523 1.00 43.91  ?  328 ALA A C   1 
ATOM   2520 O  O   . ALA A 1 328 ? 38.143 -58.881 -40.331 1.00 44.36  ?  328 ALA A O   1 
ATOM   2521 C  CB  . ALA A 1 328 ? 37.773 -58.983 -37.083 1.00 41.72  ?  328 ALA A CB  1 
ATOM   2522 N  N   . GLN A 1 329 ? 36.003 -59.123 -39.713 1.00 49.07  ?  329 GLN A N   1 
ATOM   2523 C  CA  . GLN A 1 329 ? 35.647 -59.940 -40.866 1.00 51.58  ?  329 GLN A CA  1 
ATOM   2524 C  C   . GLN A 1 329 ? 35.590 -59.043 -42.107 1.00 44.91  ?  329 GLN A C   1 
ATOM   2525 O  O   . GLN A 1 329 ? 35.948 -59.477 -43.199 1.00 33.97  ?  329 GLN A O   1 
ATOM   2526 C  CB  . GLN A 1 329 ? 34.362 -60.737 -40.587 1.00 51.29  ?  329 GLN A CB  1 
ATOM   2527 C  CG  . GLN A 1 329 ? 34.574 -62.110 -39.942 1.00 50.21  ?  329 GLN A CG  1 
ATOM   2528 C  CD  . GLN A 1 329 ? 35.178 -63.176 -40.849 1.00 50.15  ?  329 GLN A CD  1 
ATOM   2529 O  OE1 . GLN A 1 329 ? 35.778 -64.147 -40.370 1.00 47.72  ?  329 GLN A OE1 1 
ATOM   2530 N  NE2 . GLN A 1 329 ? 35.064 -63.031 -42.166 1.00 46.02  ?  329 GLN A NE2 1 
ATOM   2531 N  N   . ALA A 1 330 ? 35.148 -57.791 -41.917 1.00 41.06  ?  330 ALA A N   1 
ATOM   2532 C  CA  . ALA A 1 330 ? 35.057 -56.827 -43.004 1.00 40.42  ?  330 ALA A CA  1 
ATOM   2533 C  C   . ALA A 1 330 ? 36.439 -56.596 -43.602 1.00 35.75  ?  330 ALA A C   1 
ATOM   2534 O  O   . ALA A 1 330 ? 36.589 -56.554 -44.821 1.00 28.82  ?  330 ALA A O   1 
ATOM   2535 C  CB  . ALA A 1 330 ? 34.463 -55.523 -42.500 1.00 41.40  ?  330 ALA A CB  1 
ATOM   2536 N  N   . LEU A 1 331 ? 37.410 -56.438 -42.688 1.00 38.99  ?  331 LEU A N   1 
ATOM   2537 C  CA  . LEU A 1 331 ? 38.825 -56.215 -42.976 1.00 38.35  ?  331 LEU A CA  1 
ATOM   2538 C  C   . LEU A 1 331 ? 39.405 -57.365 -43.788 1.00 34.86  ?  331 LEU A C   1 
ATOM   2539 O  O   . LEU A 1 331 ? 40.084 -57.148 -44.797 1.00 31.38  ?  331 LEU A O   1 
ATOM   2540 C  CB  . LEU A 1 331 ? 39.583 -56.079 -41.655 1.00 35.02  ?  331 LEU A CB  1 
ATOM   2541 C  CG  . LEU A 1 331 ? 39.183 -54.890 -40.777 1.00 35.76  ?  331 LEU A CG  1 
ATOM   2542 C  CD1 . LEU A 1 331 ? 40.051 -54.898 -39.523 1.00 39.17  ?  331 LEU A CD1 1 
ATOM   2543 C  CD2 . LEU A 1 331 ? 39.301 -53.557 -41.505 1.00 35.91  ?  331 LEU A CD2 1 
ATOM   2544 N  N   . ILE A 1 332 ? 39.134 -58.576 -43.297 1.00 33.97  ?  332 ILE A N   1 
ATOM   2545 C  CA  . ILE A 1 332 ? 39.546 -59.805 -43.951 1.00 37.27  ?  332 ILE A CA  1 
ATOM   2546 C  C   . ILE A 1 332 ? 39.032 -59.827 -45.396 1.00 40.26  ?  332 ILE A C   1 
ATOM   2547 O  O   . ILE A 1 332 ? 39.841 -60.008 -46.317 1.00 36.25  ?  332 ILE A O   1 
ATOM   2548 C  CB  . ILE A 1 332 ? 39.094 -61.014 -43.115 1.00 35.36  ?  332 ILE A CB  1 
ATOM   2549 C  CG1 . ILE A 1 332 ? 39.924 -61.109 -41.824 1.00 36.57  ?  332 ILE A CG1 1 
ATOM   2550 C  CG2 . ILE A 1 332 ? 39.163 -62.297 -43.935 1.00 36.74  ?  332 ILE A CG2 1 
ATOM   2551 C  CD1 . ILE A 1 332 ? 39.571 -62.267 -40.902 1.00 37.91  ?  332 ILE A CD1 1 
ATOM   2552 N  N   . ALA A 1 333 ? 37.710 -59.591 -45.566 1.00 40.97  ?  333 ALA A N   1 
ATOM   2553 C  CA  . ALA A 1 333 ? 37.012 -59.612 -46.852 1.00 39.77  ?  333 ALA A CA  1 
ATOM   2554 C  C   . ALA A 1 333 ? 37.413 -58.440 -47.754 1.00 41.99  ?  333 ALA A C   1 
ATOM   2555 O  O   . ALA A 1 333 ? 37.315 -58.554 -48.972 1.00 44.88  ?  333 ALA A O   1 
ATOM   2556 C  CB  . ALA A 1 333 ? 35.516 -59.609 -46.639 1.00 38.78  ?  333 ALA A CB  1 
ATOM   2557 N  N   . ALA A 1 334 ? 37.857 -57.323 -47.155 1.00 40.92  ?  334 ALA A N   1 
ATOM   2558 C  CA  . ALA A 1 334 ? 38.452 -56.195 -47.867 1.00 34.56  ?  334 ALA A CA  1 
ATOM   2559 C  C   . ALA A 1 334 ? 39.897 -56.466 -48.297 1.00 30.76  ?  334 ALA A C   1 
ATOM   2560 O  O   . ALA A 1 334 ? 40.534 -55.578 -48.840 1.00 29.36  ?  334 ALA A O   1 
ATOM   2561 C  CB  . ALA A 1 334 ? 38.404 -54.975 -46.966 1.00 34.10  ?  334 ALA A CB  1 
ATOM   2562 N  N   . GLY A 1 335 ? 40.431 -57.663 -48.024 1.00 31.61  ?  335 GLY A N   1 
ATOM   2563 C  CA  . GLY A 1 335 ? 41.792 -58.032 -48.397 1.00 34.33  ?  335 GLY A CA  1 
ATOM   2564 C  C   . GLY A 1 335 ? 42.894 -57.530 -47.447 1.00 33.51  ?  335 GLY A C   1 
ATOM   2565 O  O   . GLY A 1 335 ? 44.057 -57.561 -47.846 1.00 29.09  ?  335 GLY A O   1 
ATOM   2566 N  N   . CYS A 1 336 ? 42.544 -57.089 -46.219 1.00 32.52  ?  336 CYS A N   1 
ATOM   2567 C  CA  . CYS A 1 336 ? 43.516 -56.703 -45.200 1.00 35.97  ?  336 CYS A CA  1 
ATOM   2568 C  C   . CYS A 1 336 ? 44.352 -57.913 -44.798 1.00 38.24  ?  336 CYS A C   1 
ATOM   2569 O  O   . CYS A 1 336 ? 43.777 -58.992 -44.600 1.00 32.84  ?  336 CYS A O   1 
ATOM   2570 C  CB  . CYS A 1 336 ? 42.839 -56.183 -43.933 1.00 39.99  ?  336 CYS A CB  1 
ATOM   2571 S  SG  . CYS A 1 336 ? 43.940 -55.269 -42.816 1.00 44.00  ?  336 CYS A SG  1 
ATOM   2572 N  N   . LYS A 1 337 ? 45.688 -57.721 -44.710 1.00 41.47  ?  337 LYS A N   1 
ATOM   2573 C  CA  . LYS A 1 337 ? 46.638 -58.821 -44.515 1.00 46.89  ?  337 LYS A CA  1 
ATOM   2574 C  C   . LYS A 1 337 ? 47.584 -58.585 -43.318 1.00 40.88  ?  337 LYS A C   1 
ATOM   2575 O  O   . LYS A 1 337 ? 48.365 -59.485 -42.981 1.00 30.10  ?  337 LYS A O   1 
ATOM   2576 C  CB  . LYS A 1 337 ? 47.448 -59.103 -45.795 1.00 47.52  ?  337 LYS A CB  1 
ATOM   2577 C  CG  . LYS A 1 337 ? 46.678 -59.119 -47.112 1.00 52.35  ?  337 LYS A CG  1 
ATOM   2578 C  CD  . LYS A 1 337 ? 47.494 -58.660 -48.328 1.00 60.57  ?  337 LYS A CD  1 
ATOM   2579 C  CE  . LYS A 1 337 ? 46.689 -58.112 -49.493 1.00 61.52  ?  337 LYS A CE  1 
ATOM   2580 N  NZ  . LYS A 1 337 ? 46.130 -56.777 -49.229 1.00 59.48  1  337 LYS A NZ  1 
ATOM   2581 N  N   . PHE A 1 338 ? 47.488 -57.397 -42.677 1.00 38.26  ?  338 PHE A N   1 
ATOM   2582 C  CA  . PHE A 1 338 ? 48.395 -56.950 -41.621 1.00 35.19  ?  338 PHE A CA  1 
ATOM   2583 C  C   . PHE A 1 338 ? 47.698 -55.944 -40.696 1.00 31.53  ?  338 PHE A C   1 
ATOM   2584 O  O   . PHE A 1 338 ? 47.273 -54.885 -41.137 1.00 27.85  ?  338 PHE A O   1 
ATOM   2585 C  CB  . PHE A 1 338 ? 49.631 -56.293 -42.241 1.00 37.84  ?  338 PHE A CB  1 
ATOM   2586 C  CG  . PHE A 1 338 ? 50.551 -57.254 -42.985 1.00 36.37  ?  338 PHE A CG  1 
ATOM   2587 C  CD1 . PHE A 1 338 ? 50.510 -57.355 -44.376 1.00 38.44  ?  338 PHE A CD1 1 
ATOM   2588 C  CD2 . PHE A 1 338 ? 51.453 -58.040 -42.291 1.00 33.65  ?  338 PHE A CD2 1 
ATOM   2589 C  CE1 . PHE A 1 338 ? 51.335 -58.235 -45.050 1.00 38.05  ?  338 PHE A CE1 1 
ATOM   2590 C  CE2 . PHE A 1 338 ? 52.271 -58.920 -42.968 1.00 37.39  ?  338 PHE A CE2 1 
ATOM   2591 C  CZ  . PHE A 1 338 ? 52.210 -59.018 -44.343 1.00 38.96  ?  338 PHE A CZ  1 
ATOM   2592 N  N   . ILE A 1 339 ? 47.600 -56.281 -39.402 1.00 32.28  ?  339 ILE A N   1 
ATOM   2593 C  CA  . ILE A 1 339 ? 46.886 -55.479 -38.412 1.00 33.96  ?  339 ILE A CA  1 
ATOM   2594 C  C   . ILE A 1 339 ? 47.615 -55.563 -37.069 1.00 33.14  ?  339 ILE A C   1 
ATOM   2595 O  O   . ILE A 1 339 ? 47.623 -56.626 -36.459 1.00 33.96  ?  339 ILE A O   1 
ATOM   2596 C  CB  . ILE A 1 339 ? 45.402 -55.897 -38.229 1.00 33.31  ?  339 ILE A CB  1 
ATOM   2597 C  CG1 . ILE A 1 339 ? 44.803 -55.271 -36.936 1.00 33.12  ?  339 ILE A CG1 1 
ATOM   2598 C  CG2 . ILE A 1 339 ? 45.228 -57.418 -38.215 1.00 32.24  ?  339 ILE A CG2 1 
ATOM   2599 C  CD1 . ILE A 1 339 ? 43.302 -55.046 -36.951 1.00 32.12  ?  339 ILE A CD1 1 
ATOM   2600 N  N   . ALA A 1 340 ? 48.125 -54.421 -36.577 1.00 31.88  ?  340 ALA A N   1 
ATOM   2601 C  CA  . ALA A 1 340 ? 48.782 -54.348 -35.277 1.00 34.83  ?  340 ALA A CA  1 
ATOM   2602 C  C   . ALA A 1 340 ? 48.133 -53.280 -34.394 1.00 36.93  ?  340 ALA A C   1 
ATOM   2603 O  O   . ALA A 1 340 ? 47.572 -52.311 -34.904 1.00 45.67  ?  340 ALA A O   1 
ATOM   2604 C  CB  . ALA A 1 340 ? 50.252 -54.067 -35.474 1.00 36.14  ?  340 ALA A CB  1 
ATOM   2605 N  N   . GLU A 1 341 ? 48.236 -53.444 -33.069 1.00 34.67  ?  341 GLU A N   1 
ATOM   2606 C  CA  . GLU A 1 341 ? 47.646 -52.504 -32.126 1.00 38.61  ?  341 GLU A CA  1 
ATOM   2607 C  C   . GLU A 1 341 ? 48.658 -51.426 -31.743 1.00 40.18  ?  341 GLU A C   1 
ATOM   2608 O  O   . GLU A 1 341 ? 49.704 -51.737 -31.186 1.00 44.33  ?  341 GLU A O   1 
ATOM   2609 C  CB  . GLU A 1 341 ? 47.212 -53.181 -30.823 1.00 41.91  ?  341 GLU A CB  1 
ATOM   2610 C  CG  . GLU A 1 341 ? 46.334 -54.415 -31.022 1.00 42.94  ?  341 GLU A CG  1 
ATOM   2611 C  CD  . GLU A 1 341 ? 46.050 -55.263 -29.790 1.00 42.59  ?  341 GLU A CD  1 
ATOM   2612 O  OE1 . GLU A 1 341 ? 44.995 -55.932 -29.883 1.00 45.02  ?  341 GLU A OE1 1 
ATOM   2613 O  OE2 . GLU A 1 341 ? 46.830 -55.317 -28.799 1.00 36.77  -1 341 GLU A OE2 1 
ATOM   2614 N  N   . GLY A 1 342 ? 48.330 -50.164 -32.048 1.00 41.47  ?  342 GLY A N   1 
ATOM   2615 C  CA  . GLY A 1 342 ? 48.875 -49.020 -31.338 1.00 41.60  ?  342 GLY A CA  1 
ATOM   2616 C  C   . GLY A 1 342 ? 48.280 -48.888 -29.934 1.00 45.81  ?  342 GLY A C   1 
ATOM   2617 O  O   . GLY A 1 342 ? 48.993 -48.508 -29.019 1.00 51.95  ?  342 GLY A O   1 
ATOM   2618 N  N   . SER A 1 343 ? 46.971 -49.177 -29.790 1.00 55.99  ?  343 SER A N   1 
ATOM   2619 C  CA  . SER A 1 343 ? 46.244 -49.203 -28.521 1.00 51.76  ?  343 SER A CA  1 
ATOM   2620 C  C   . SER A 1 343 ? 46.418 -50.565 -27.850 1.00 52.87  ?  343 SER A C   1 
ATOM   2621 O  O   . SER A 1 343 ? 46.668 -51.557 -28.534 1.00 63.71  ?  343 SER A O   1 
ATOM   2622 C  CB  . SER A 1 343 ? 44.765 -48.933 -28.748 1.00 52.89  ?  343 SER A CB  1 
ATOM   2623 O  OG  . SER A 1 343 ? 44.218 -49.877 -29.667 1.00 53.30  ?  343 SER A OG  1 
ATOM   2624 N  N   . ASN A 1 344 ? 46.243 -50.617 -26.524 1.00 47.58  ?  344 ASN A N   1 
ATOM   2625 C  CA  . ASN A 1 344 ? 46.274 -51.870 -25.778 1.00 47.79  ?  344 ASN A CA  1 
ATOM   2626 C  C   . ASN A 1 344 ? 44.899 -52.553 -25.815 1.00 50.06  ?  344 ASN A C   1 
ATOM   2627 O  O   . ASN A 1 344 ? 43.896 -51.940 -25.440 1.00 53.91  ?  344 ASN A O   1 
ATOM   2628 C  CB  . ASN A 1 344 ? 46.773 -51.650 -24.349 1.00 47.45  ?  344 ASN A CB  1 
ATOM   2629 C  CG  . ASN A 1 344 ? 48.272 -51.829 -24.233 1.00 46.45  ?  344 ASN A CG  1 
ATOM   2630 O  OD1 . ASN A 1 344 ? 48.820 -52.821 -24.733 1.00 44.64  ?  344 ASN A OD1 1 
ATOM   2631 N  ND2 . ASN A 1 344 ? 48.952 -50.886 -23.596 1.00 40.27  ?  344 ASN A ND2 1 
ATOM   2632 N  N   A MET A 1 345 ? 44.886 -53.819 -26.265 0.50 49.95  ?  345 MET A N   1 
ATOM   2633 N  N   B MET A 1 345 ? 44.872 -53.826 -26.247 0.50 48.25  ?  345 MET A N   1 
ATOM   2634 C  CA  A MET A 1 345 ? 43.679 -54.628 -26.411 0.50 50.20  ?  345 MET A CA  1 
ATOM   2635 C  CA  B MET A 1 345 ? 43.652 -54.619 -26.408 0.50 47.28  ?  345 MET A CA  1 
ATOM   2636 C  C   A MET A 1 345 ? 42.656 -53.917 -27.299 0.50 49.15  ?  345 MET A C   1 
ATOM   2637 C  C   B MET A 1 345 ? 42.644 -53.923 -27.317 0.50 47.56  ?  345 MET A C   1 
ATOM   2638 O  O   A MET A 1 345 ? 41.458 -53.994 -27.038 0.50 47.53  ?  345 MET A O   1 
ATOM   2639 O  O   B MET A 1 345 ? 41.442 -54.013 -27.081 0.50 46.12  ?  345 MET A O   1 
ATOM   2640 C  CB  A MET A 1 345 ? 43.051 -54.964 -25.048 0.50 50.18  ?  345 MET A CB  1 
ATOM   2641 C  CB  B MET A 1 345 ? 42.919 -54.874 -25.085 0.50 45.04  ?  345 MET A CB  1 
ATOM   2642 C  CG  A MET A 1 345 ? 43.994 -55.676 -24.073 0.50 49.59  ?  345 MET A CG  1 
ATOM   2643 C  CG  B MET A 1 345 ? 43.789 -55.422 -23.979 0.50 43.30  ?  345 MET A CG  1 
ATOM   2644 S  SD  A MET A 1 345 ? 44.039 -57.472 -24.251 0.50 45.04  ?  345 MET A SD  1 
ATOM   2645 S  SD  B MET A 1 345 ? 43.215 -54.811 -22.386 0.50 36.64  ?  345 MET A SD  1 
ATOM   2646 C  CE  A MET A 1 345 ? 45.730 -57.888 -23.801 0.50 42.89  ?  345 MET A CE  1 
ATOM   2647 C  CE  B MET A 1 345 ? 44.794 -54.886 -21.530 0.50 36.56  ?  345 MET A CE  1 
ATOM   2648 N  N   . GLY A 1 346 ? 43.141 -53.243 -28.355 1.00 49.57  ?  346 GLY A N   1 
ATOM   2649 C  CA  . GLY A 1 346 ? 42.291 -52.513 -29.280 1.00 46.60  ?  346 GLY A CA  1 
ATOM   2650 C  C   . GLY A 1 346 ? 41.311 -53.465 -29.946 1.00 43.19  ?  346 GLY A C   1 
ATOM   2651 O  O   . GLY A 1 346 ? 40.163 -53.109 -30.214 1.00 49.69  ?  346 GLY A O   1 
ATOM   2652 N  N   . CYS A 1 347 ? 41.806 -54.678 -30.195 1.00 38.98  ?  347 CYS A N   1 
ATOM   2653 C  CA  . CYS A 1 347 ? 41.013 -55.753 -30.767 1.00 38.69  ?  347 CYS A CA  1 
ATOM   2654 C  C   . CYS A 1 347 ? 40.413 -56.587 -29.636 1.00 35.94  ?  347 CYS A C   1 
ATOM   2655 O  O   . CYS A 1 347 ? 41.040 -56.850 -28.614 1.00 30.62  ?  347 CYS A O   1 
ATOM   2656 C  CB  . CYS A 1 347 ? 41.848 -56.628 -31.700 1.00 42.18  ?  347 CYS A CB  1 
ATOM   2657 S  SG  . CYS A 1 347 ? 42.721 -55.720 -33.013 1.00 47.76  ?  347 CYS A SG  1 
ATOM   2658 N  N   . THR A 1 348 ? 39.158 -56.978 -29.830 1.00 36.79  ?  348 THR A N   1 
ATOM   2659 C  CA  . THR A 1 348 ? 38.451 -57.804 -28.873 1.00 36.60  ?  348 THR A CA  1 
ATOM   2660 C  C   . THR A 1 348 ? 38.860 -59.253 -29.122 1.00 31.63  ?  348 THR A C   1 
ATOM   2661 O  O   . THR A 1 348 ? 39.403 -59.561 -30.170 1.00 27.36  ?  348 THR A O   1 
ATOM   2662 C  CB  . THR A 1 348 ? 36.958 -57.538 -29.071 1.00 38.94  ?  348 THR A CB  1 
ATOM   2663 O  OG1 . THR A 1 348 ? 36.734 -57.777 -30.457 1.00 41.81  ?  348 THR A OG1 1 
ATOM   2664 C  CG2 . THR A 1 348 ? 36.573 -56.094 -28.792 1.00 38.08  ?  348 THR A CG2 1 
ATOM   2665 N  N   . GLN A 1 349 ? 38.598 -60.144 -28.164 1.00 33.84  ?  349 GLN A N   1 
ATOM   2666 C  CA  . GLN A 1 349 ? 39.002 -61.536 -28.298 1.00 34.67  ?  349 GLN A CA  1 
ATOM   2667 C  C   . GLN A 1 349 ? 38.422 -62.157 -29.577 1.00 37.03  ?  349 GLN A C   1 
ATOM   2668 O  O   . GLN A 1 349 ? 39.148 -62.853 -30.294 1.00 38.45  ?  349 GLN A O   1 
ATOM   2669 C  CB  . GLN A 1 349 ? 38.640 -62.332 -27.047 1.00 32.47  ?  349 GLN A CB  1 
ATOM   2670 C  CG  . GLN A 1 349 ? 39.197 -63.752 -27.075 1.00 34.19  ?  349 GLN A CG  1 
ATOM   2671 C  CD  . GLN A 1 349 ? 40.666 -63.839 -27.437 1.00 30.72  ?  349 GLN A CD  1 
ATOM   2672 O  OE1 . GLN A 1 349 ? 41.054 -64.541 -28.374 1.00 33.42  ?  349 GLN A OE1 1 
ATOM   2673 N  NE2 . GLN A 1 349 ? 41.505 -63.165 -26.670 1.00 27.74  ?  349 GLN A NE2 1 
ATOM   2674 N  N   . ALA A 1 350 ? 37.122 -61.909 -29.829 1.00 33.52  ?  350 ALA A N   1 
ATOM   2675 C  CA  . ALA A 1 350 ? 36.447 -62.221 -31.080 1.00 32.90  ?  350 ALA A CA  1 
ATOM   2676 C  C   . ALA A 1 350 ? 37.294 -61.874 -32.308 1.00 39.39  ?  350 ALA A C   1 
ATOM   2677 O  O   . ALA A 1 350 ? 37.536 -62.734 -33.153 1.00 49.77  ?  350 ALA A O   1 
ATOM   2678 C  CB  . ALA A 1 350 ? 35.171 -61.444 -31.122 1.00 33.28  ?  350 ALA A CB  1 
ATOM   2679 N  N   . ALA A 1 351 ? 37.713 -60.602 -32.412 1.00 36.69  ?  351 ALA A N   1 
ATOM   2680 C  CA  . ALA A 1 351 ? 38.559 -60.094 -33.486 1.00 36.61  ?  351 ALA A CA  1 
ATOM   2681 C  C   . ALA A 1 351 ? 39.841 -60.910 -33.647 1.00 35.72  ?  351 ALA A C   1 
ATOM   2682 O  O   . ALA A 1 351 ? 40.246 -61.227 -34.764 1.00 35.12  ?  351 ALA A O   1 
ATOM   2683 C  CB  . ALA A 1 351 ? 38.908 -58.633 -33.224 1.00 35.99  ?  351 ALA A CB  1 
ATOM   2684 N  N   . ILE A 1 352 ? 40.489 -61.202 -32.518 1.00 36.31  ?  352 ILE A N   1 
ATOM   2685 C  CA  . ILE A 1 352 ? 41.745 -61.930 -32.502 1.00 35.86  ?  352 ILE A CA  1 
ATOM   2686 C  C   . ILE A 1 352 ? 41.514 -63.314 -33.088 1.00 34.38  ?  352 ILE A C   1 
ATOM   2687 O  O   . ILE A 1 352 ? 42.301 -63.787 -33.897 1.00 35.74  ?  352 ILE A O   1 
ATOM   2688 C  CB  . ILE A 1 352 ? 42.324 -61.995 -31.077 1.00 36.04  ?  352 ILE A CB  1 
ATOM   2689 C  CG1 . ILE A 1 352 ? 42.649 -60.576 -30.531 1.00 31.35  ?  352 ILE A CG1 1 
ATOM   2690 C  CG2 . ILE A 1 352 ? 43.547 -62.918 -31.035 1.00 37.62  ?  352 ILE A CG2 1 
ATOM   2691 C  CD1 . ILE A 1 352 ? 42.641 -60.469 -29.021 1.00 28.85  ?  352 ILE A CD1 1 
ATOM   2692 N  N   . ASP A 1 353 ? 40.416 -63.942 -32.677 1.00 35.06  ?  353 ASP A N   1 
ATOM   2693 C  CA  . ASP A 1 353 ? 40.158 -65.330 -33.027 1.00 36.09  ?  353 ASP A CA  1 
ATOM   2694 C  C   . ASP A 1 353 ? 39.866 -65.399 -34.522 1.00 36.85  ?  353 ASP A C   1 
ATOM   2695 O  O   . ASP A 1 353 ? 40.143 -66.427 -35.135 1.00 39.10  ?  353 ASP A O   1 
ATOM   2696 C  CB  . ASP A 1 353 ? 39.114 -65.935 -32.092 1.00 33.02  ?  353 ASP A CB  1 
ATOM   2697 C  CG  . ASP A 1 353 ? 39.547 -65.956 -30.626 1.00 34.08  ?  353 ASP A CG  1 
ATOM   2698 O  OD1 . ASP A 1 353 ? 38.649 -65.930 -29.752 1.00 34.10  ?  353 ASP A OD1 1 
ATOM   2699 O  OD2 . ASP A 1 353 ? 40.789 -66.000 -30.354 1.00 25.69  -1 353 ASP A OD2 1 
ATOM   2700 N  N   . ALA A 1 354 ? 39.320 -64.295 -35.070 1.00 34.00  ?  354 ALA A N   1 
ATOM   2701 C  CA  . ALA A 1 354 ? 38.903 -64.193 -36.462 1.00 32.80  ?  354 ALA A CA  1 
ATOM   2702 C  C   . ALA A 1 354 ? 40.127 -64.120 -37.369 1.00 34.22  ?  354 ALA A C   1 
ATOM   2703 O  O   . ALA A 1 354 ? 40.163 -64.772 -38.417 1.00 36.90  ?  354 ALA A O   1 
ATOM   2704 C  CB  . ALA A 1 354 ? 38.022 -62.969 -36.660 1.00 30.21  ?  354 ALA A CB  1 
ATOM   2705 N  N   . PHE A 1 355 ? 41.092 -63.284 -36.958 1.00 33.14  ?  355 PHE A N   1 
ATOM   2706 C  CA  . PHE A 1 355 ? 42.350 -63.112 -37.668 1.00 38.41  ?  355 PHE A CA  1 
ATOM   2707 C  C   . PHE A 1 355 ? 43.168 -64.409 -37.624 1.00 46.60  ?  355 PHE A C   1 
ATOM   2708 O  O   . PHE A 1 355 ? 43.781 -64.804 -38.628 1.00 47.60  ?  355 PHE A O   1 
ATOM   2709 C  CB  . PHE A 1 355 ? 43.170 -61.958 -37.069 1.00 35.15  ?  355 PHE A CB  1 
ATOM   2710 C  CG  . PHE A 1 355 ? 42.487 -60.597 -37.057 1.00 33.97  ?  355 PHE A CG  1 
ATOM   2711 C  CD1 . PHE A 1 355 ? 41.805 -60.121 -38.181 1.00 33.08  ?  355 PHE A CD1 1 
ATOM   2712 C  CD2 . PHE A 1 355 ? 42.485 -59.814 -35.908 1.00 32.11  ?  355 PHE A CD2 1 
ATOM   2713 C  CE1 . PHE A 1 355 ? 41.136 -58.906 -38.155 1.00 29.54  ?  355 PHE A CE1 1 
ATOM   2714 C  CE2 . PHE A 1 355 ? 41.811 -58.603 -35.886 1.00 31.67  ?  355 PHE A CE2 1 
ATOM   2715 C  CZ  . PHE A 1 355 ? 41.140 -58.153 -37.007 1.00 30.88  ?  355 PHE A CZ  1 
ATOM   2716 N  N   . GLU A 1 356 ? 43.204 -65.020 -36.426 1.00 47.33  ?  356 GLU A N   1 
ATOM   2717 C  CA  . GLU A 1 356 ? 44.021 -66.186 -36.119 1.00 39.95  ?  356 GLU A CA  1 
ATOM   2718 C  C   . GLU A 1 356 ? 43.355 -67.411 -36.722 1.00 39.03  ?  356 GLU A C   1 
ATOM   2719 O  O   . GLU A 1 356 ? 44.010 -68.412 -36.973 1.00 38.06  ?  356 GLU A O   1 
ATOM   2720 C  CB  . GLU A 1 356 ? 44.152 -66.363 -34.604 1.00 37.69  ?  356 GLU A CB  1 
ATOM   2721 C  CG  . GLU A 1 356 ? 45.092 -65.350 -33.967 1.00 36.55  ?  356 GLU A CG  1 
ATOM   2722 C  CD  . GLU A 1 356 ? 46.531 -65.735 -34.204 1.00 35.99  ?  356 GLU A CD  1 
ATOM   2723 O  OE1 . GLU A 1 356 ? 47.219 -65.039 -34.963 1.00 42.85  ?  356 GLU A OE1 1 
ATOM   2724 O  OE2 . GLU A 1 356 ? 46.962 -66.751 -33.638 1.00 34.97  -1 356 GLU A OE2 1 
ATOM   2725 N  N   . ALA A 1 357 ? 42.036 -67.333 -36.906 1.00 39.95  ?  357 ALA A N   1 
ATOM   2726 C  CA  . ALA A 1 357 ? 41.321 -68.405 -37.569 1.00 45.15  ?  357 ALA A CA  1 
ATOM   2727 C  C   . ALA A 1 357 ? 41.699 -68.370 -39.044 1.00 45.31  ?  357 ALA A C   1 
ATOM   2728 O  O   . ALA A 1 357 ? 42.137 -69.381 -39.588 1.00 49.63  ?  357 ALA A O   1 
ATOM   2729 C  CB  . ALA A 1 357 ? 39.824 -68.285 -37.358 1.00 45.65  ?  357 ALA A CB  1 
ATOM   2730 N  N   . HIS A 1 358 ? 41.559 -67.184 -39.651 1.00 40.99  ?  358 HIS A N   1 
ATOM   2731 C  CA  . HIS A 1 358 ? 41.833 -66.984 -41.063 1.00 42.01  ?  358 HIS A CA  1 
ATOM   2732 C  C   . HIS A 1 358 ? 43.308 -67.264 -41.347 1.00 38.70  ?  358 HIS A C   1 
ATOM   2733 O  O   . HIS A 1 358 ? 43.672 -67.704 -42.432 1.00 34.72  ?  358 HIS A O   1 
ATOM   2734 C  CB  . HIS A 1 358 ? 41.415 -65.563 -41.455 1.00 47.28  ?  358 HIS A CB  1 
ATOM   2735 C  CG  . HIS A 1 358 ? 41.708 -65.160 -42.859 1.00 44.13  ?  358 HIS A CG  1 
ATOM   2736 N  ND1 . HIS A 1 358 ? 42.985 -64.914 -43.311 1.00 46.29  ?  358 HIS A ND1 1 
ATOM   2737 C  CD2 . HIS A 1 358 ? 40.895 -64.943 -43.885 1.00 40.21  ?  358 HIS A CD2 1 
ATOM   2738 C  CE1 . HIS A 1 358 ? 42.923 -64.545 -44.578 1.00 47.93  ?  358 HIS A CE1 1 
ATOM   2739 N  NE2 . HIS A 1 358 ? 41.660 -64.557 -44.946 1.00 43.66  ?  358 HIS A NE2 1 
ATOM   2740 N  N   . ARG A 1 359 ? 44.156 -66.997 -40.356 1.00 40.37  ?  359 ARG A N   1 
ATOM   2741 C  CA  . ARG A 1 359 ? 45.570 -67.313 -40.442 1.00 39.14  ?  359 ARG A CA  1 
ATOM   2742 C  C   . ARG A 1 359 ? 45.769 -68.826 -40.561 1.00 36.75  ?  359 ARG A C   1 
ATOM   2743 O  O   . ARG A 1 359 ? 46.587 -69.288 -41.356 1.00 34.98  ?  359 ARG A O   1 
ATOM   2744 C  CB  . ARG A 1 359 ? 46.308 -66.763 -39.216 1.00 38.15  ?  359 ARG A CB  1 
ATOM   2745 C  CG  . ARG A 1 359 ? 47.807 -66.712 -39.467 1.00 42.53  ?  359 ARG A CG  1 
ATOM   2746 C  CD  . ARG A 1 359 ? 48.620 -66.649 -38.198 1.00 43.10  ?  359 ARG A CD  1 
ATOM   2747 N  NE  . ARG A 1 359 ? 49.031 -67.997 -37.792 1.00 41.81  ?  359 ARG A NE  1 
ATOM   2748 C  CZ  . ARG A 1 359 ? 48.741 -68.618 -36.650 1.00 42.52  ?  359 ARG A CZ  1 
ATOM   2749 N  NH1 . ARG A 1 359 ? 47.956 -68.068 -35.747 1.00 40.78  1  359 ARG A NH1 1 
ATOM   2750 N  NH2 . ARG A 1 359 ? 49.242 -69.818 -36.419 1.00 47.03  ?  359 ARG A NH2 1 
ATOM   2751 N  N   . GLU A 1 360 ? 45.022 -69.587 -39.752 1.00 34.76  ?  360 GLU A N   1 
ATOM   2752 C  CA  . GLU A 1 360 ? 45.230 -71.021 -39.616 1.00 34.29  ?  360 GLU A CA  1 
ATOM   2753 C  C   . GLU A 1 360 ? 44.680 -71.751 -40.847 1.00 37.18  ?  360 GLU A C   1 
ATOM   2754 O  O   . GLU A 1 360 ? 45.100 -72.868 -41.144 1.00 38.95  ?  360 GLU A O   1 
ATOM   2755 C  CB  . GLU A 1 360 ? 44.629 -71.493 -38.286 1.00 31.94  ?  360 GLU A CB  1 
ATOM   2756 C  CG  . GLU A 1 360 ? 45.582 -71.376 -37.098 1.00 32.69  ?  360 GLU A CG  1 
ATOM   2757 C  CD  . GLU A 1 360 ? 44.930 -71.402 -35.722 1.00 35.01  ?  360 GLU A CD  1 
ATOM   2758 O  OE1 . GLU A 1 360 ? 43.831 -70.826 -35.659 1.00 37.92  ?  360 GLU A OE1 1 
ATOM   2759 O  OE2 . GLU A 1 360 ? 45.486 -71.910 -34.712 1.00 34.11  -1 360 GLU A OE2 1 
ATOM   2760 N  N   . ALA A 1 361 ? 43.757 -71.100 -41.574 1.00 41.61  ?  361 ALA A N   1 
ATOM   2761 C  CA  . ALA A 1 361 ? 42.992 -71.719 -42.650 1.00 41.85  ?  361 ALA A CA  1 
ATOM   2762 C  C   . ALA A 1 361 ? 43.315 -71.110 -44.019 1.00 42.94  ?  361 ALA A C   1 
ATOM   2763 O  O   . ALA A 1 361 ? 42.705 -71.525 -45.007 1.00 37.56  ?  361 ALA A O   1 
ATOM   2764 C  CB  . ALA A 1 361 ? 41.515 -71.591 -42.338 1.00 42.98  ?  361 ALA A CB  1 
ATOM   2765 N  N   . ASN A 1 362 ? 44.241 -70.127 -44.053 1.00 42.31  ?  362 ASN A N   1 
ATOM   2766 C  CA  . ASN A 1 362 ? 44.837 -69.589 -45.269 1.00 39.28  ?  362 ASN A CA  1 
ATOM   2767 C  C   . ASN A 1 362 ? 46.361 -69.617 -45.108 1.00 42.08  ?  362 ASN A C   1 
ATOM   2768 O  O   . ASN A 1 362 ? 46.860 -69.154 -44.091 1.00 46.49  ?  362 ASN A O   1 
ATOM   2769 C  CB  . ASN A 1 362 ? 44.379 -68.158 -45.538 1.00 40.01  ?  362 ASN A CB  1 
ATOM   2770 C  CG  . ASN A 1 362 ? 42.874 -67.981 -45.535 1.00 38.40  ?  362 ASN A CG  1 
ATOM   2771 O  OD1 . ASN A 1 362 ? 42.330 -67.138 -44.806 1.00 31.94  ?  362 ASN A OD1 1 
ATOM   2772 N  ND2 . ASN A 1 362 ? 42.181 -68.716 -46.387 1.00 40.23  ?  362 ASN A ND2 1 
ATOM   2773 N  N   . LYS A 1 363 ? 47.092 -70.134 -46.113 1.00 45.73  ?  363 LYS A N   1 
ATOM   2774 C  CA  . LYS A 1 363 ? 48.540 -70.346 -46.065 1.00 45.59  ?  363 LYS A CA  1 
ATOM   2775 C  C   . LYS A 1 363 ? 49.338 -69.113 -46.512 1.00 45.35  ?  363 LYS A C   1 
ATOM   2776 O  O   . LYS A 1 363 ? 48.999 -68.468 -47.506 1.00 41.17  ?  363 LYS A O   1 
ATOM   2777 C  CB  . LYS A 1 363 ? 48.973 -71.475 -47.011 1.00 48.80  ?  363 LYS A CB  1 
ATOM   2778 C  CG  . LYS A 1 363 ? 48.691 -72.910 -46.550 1.00 53.40  ?  363 LYS A CG  1 
ATOM   2779 C  CD  . LYS A 1 363 ? 49.235 -74.016 -47.460 1.00 54.10  ?  363 LYS A CD  1 
ATOM   2780 C  CE  . LYS A 1 363 ? 50.680 -73.810 -47.851 1.00 54.72  ?  363 LYS A CE  1 
ATOM   2781 N  NZ  . LYS A 1 363 ? 51.471 -75.044 -47.894 1.00 53.47  1  363 LYS A NZ  1 
ATOM   2782 N  N   . GLY A 1 364 ? 50.441 -68.828 -45.792 1.00 44.24  ?  364 GLY A N   1 
ATOM   2783 C  CA  . GLY A 1 364 ? 51.393 -67.796 -46.180 1.00 41.29  ?  364 GLY A CA  1 
ATOM   2784 C  C   . GLY A 1 364 ? 50.759 -66.407 -46.139 1.00 41.58  ?  364 GLY A C   1 
ATOM   2785 O  O   . GLY A 1 364 ? 49.907 -66.152 -45.297 1.00 39.98  ?  364 GLY A O   1 
ATOM   2786 N  N   . ALA A 1 365 ? 51.152 -65.528 -47.076 1.00 44.27  ?  365 ALA A N   1 
ATOM   2787 C  CA  . ALA A 1 365 ? 50.796 -64.114 -47.013 1.00 44.70  ?  365 ALA A CA  1 
ATOM   2788 C  C   . ALA A 1 365 ? 49.407 -63.865 -47.601 1.00 41.24  ?  365 ALA A C   1 
ATOM   2789 O  O   . ALA A 1 365 ? 49.053 -62.716 -47.831 1.00 36.56  ?  365 ALA A O   1 
ATOM   2790 C  CB  . ALA A 1 365 ? 51.850 -63.278 -47.718 1.00 45.23  ?  365 ALA A CB  1 
ATOM   2791 N  N   . ALA A 1 366 ? 48.655 -64.948 -47.861 1.00 43.29  ?  366 ALA A N   1 
ATOM   2792 C  CA  . ALA A 1 366 ? 47.233 -64.895 -48.169 1.00 43.01  ?  366 ALA A CA  1 
ATOM   2793 C  C   . ALA A 1 366 ? 46.421 -64.773 -46.883 1.00 45.94  ?  366 ALA A C   1 
ATOM   2794 O  O   . ALA A 1 366 ? 45.213 -64.544 -46.944 1.00 44.93  ?  366 ALA A O   1 
ATOM   2795 C  CB  . ALA A 1 366 ? 46.834 -66.150 -48.918 1.00 41.96  ?  366 ALA A CB  1 
ATOM   2796 N  N   . ALA A 1 367 ? 47.096 -65.043 -45.752 1.00 44.54  ?  367 ALA A N   1 
ATOM   2797 C  CA  . ALA A 1 367 ? 46.554 -64.933 -44.409 1.00 43.57  ?  367 ALA A CA  1 
ATOM   2798 C  C   . ALA A 1 367 ? 46.585 -63.477 -43.989 1.00 35.94  ?  367 ALA A C   1 
ATOM   2799 O  O   . ALA A 1 367 ? 47.433 -62.772 -44.511 1.00 29.22  ?  367 ALA A O   1 
ATOM   2800 C  CB  . ALA A 1 367 ? 47.394 -65.748 -43.451 1.00 45.76  ?  367 ALA A CB  1 
ATOM   2801 N  N   . ILE A 1 368 ? 45.666 -63.064 -43.089 1.00 33.87  ?  368 ILE A N   1 
ATOM   2802 C  CA  . ILE A 1 368 ? 45.759 -61.774 -42.409 1.00 34.87  ?  368 ILE A CA  1 
ATOM   2803 C  C   . ILE A 1 368 ? 46.552 -62.031 -41.136 1.00 37.42  ?  368 ILE A C   1 
ATOM   2804 O  O   . ILE A 1 368 ? 46.289 -63.010 -40.442 1.00 48.39  ?  368 ILE A O   1 
ATOM   2805 C  CB  . ILE A 1 368 ? 44.397 -61.095 -42.100 1.00 32.07  ?  368 ILE A CB  1 
ATOM   2806 C  CG1 . ILE A 1 368 ? 44.584 -59.637 -41.664 1.00 32.47  ?  368 ILE A CG1 1 
ATOM   2807 C  CG2 . ILE A 1 368 ? 43.579 -61.857 -41.050 1.00 31.67  ?  368 ILE A CG2 1 
ATOM   2808 C  CD1 . ILE A 1 368 ? 43.295 -58.882 -41.377 1.00 33.63  ?  368 ILE A CD1 1 
ATOM   2809 N  N   . TRP A 1 369 ? 47.496 -61.140 -40.825 1.00 36.07  ?  369 TRP A N   1 
ATOM   2810 C  CA  . TRP A 1 369 ? 48.384 -61.352 -39.702 1.00 36.35  ?  369 TRP A CA  1 
ATOM   2811 C  C   . TRP A 1 369 ? 48.120 -60.270 -38.658 1.00 39.60  ?  369 TRP A C   1 
ATOM   2812 O  O   . TRP A 1 369 ? 48.121 -59.086 -38.998 1.00 32.58  ?  369 TRP A O   1 
ATOM   2813 C  CB  . TRP A 1 369 ? 49.841 -61.364 -40.196 1.00 37.07  ?  369 TRP A CB  1 
ATOM   2814 C  CG  . TRP A 1 369 ? 50.794 -62.225 -39.405 1.00 34.25  ?  369 TRP A CG  1 
ATOM   2815 C  CD1 . TRP A 1 369 ? 50.517 -62.923 -38.268 1.00 32.38  ?  369 TRP A CD1 1 
ATOM   2816 C  CD2 . TRP A 1 369 ? 52.202 -62.434 -39.677 1.00 32.85  ?  369 TRP A CD2 1 
ATOM   2817 N  NE1 . TRP A 1 369 ? 51.640 -63.578 -37.836 1.00 34.79  ?  369 TRP A NE1 1 
ATOM   2818 C  CE2 . TRP A 1 369 ? 52.692 -63.293 -38.668 1.00 33.38  ?  369 TRP A CE2 1 
ATOM   2819 C  CE3 . TRP A 1 369 ? 53.090 -61.993 -40.663 1.00 31.43  ?  369 TRP A CE3 1 
ATOM   2820 C  CZ2 . TRP A 1 369 ? 54.021 -63.716 -38.623 1.00 30.94  ?  369 TRP A CZ2 1 
ATOM   2821 C  CZ3 . TRP A 1 369 ? 54.398 -62.428 -40.626 1.00 29.92  ?  369 TRP A CZ3 1 
ATOM   2822 C  CH2 . TRP A 1 369 ? 54.855 -63.276 -39.624 1.00 29.02  ?  369 TRP A CH2 1 
ATOM   2823 N  N   . TYR A 1 370 ? 47.891 -60.727 -37.408 1.00 46.91  ?  370 TYR A N   1 
ATOM   2824 C  CA  . TYR A 1 370 ? 47.600 -59.889 -36.250 1.00 44.41  ?  370 TYR A CA  1 
ATOM   2825 C  C   . TYR A 1 370 ? 48.735 -59.986 -35.243 1.00 45.40  ?  370 TYR A C   1 
ATOM   2826 O  O   . TYR A 1 370 ? 49.088 -61.080 -34.803 1.00 51.63  ?  370 TYR A O   1 
ATOM   2827 C  CB  . TYR A 1 370 ? 46.318 -60.283 -35.513 1.00 43.34  ?  370 TYR A CB  1 
ATOM   2828 C  CG  . TYR A 1 370 ? 46.178 -59.801 -34.071 1.00 44.31  ?  370 TYR A CG  1 
ATOM   2829 C  CD1 . TYR A 1 370 ? 45.813 -58.492 -33.774 1.00 46.90  ?  370 TYR A CD1 1 
ATOM   2830 C  CD2 . TYR A 1 370 ? 46.343 -60.672 -32.999 1.00 43.95  ?  370 TYR A CD2 1 
ATOM   2831 C  CE1 . TYR A 1 370 ? 45.644 -58.060 -32.465 1.00 42.94  ?  370 TYR A CE1 1 
ATOM   2832 C  CE2 . TYR A 1 370 ? 46.178 -60.254 -31.686 1.00 41.69  ?  370 TYR A CE2 1 
ATOM   2833 C  CZ  . TYR A 1 370 ? 45.833 -58.943 -31.419 1.00 40.31  ?  370 TYR A CZ  1 
ATOM   2834 O  OH  . TYR A 1 370 ? 45.676 -58.510 -30.138 1.00 38.52  ?  370 TYR A OH  1 
ATOM   2835 N  N   . ALA A 1 371 ? 49.265 -58.808 -34.890 1.00 48.57  ?  371 ALA A N   1 
ATOM   2836 C  CA  . ALA A 1 371 ? 50.286 -58.631 -33.871 1.00 44.66  ?  371 ALA A CA  1 
ATOM   2837 C  C   . ALA A 1 371 ? 49.707 -57.870 -32.680 1.00 41.92  ?  371 ALA A C   1 
ATOM   2838 O  O   . ALA A 1 371 ? 49.007 -56.872 -32.862 1.00 35.15  ?  371 ALA A O   1 
ATOM   2839 C  CB  . ALA A 1 371 ? 51.452 -57.881 -34.465 1.00 44.34  ?  371 ALA A CB  1 
ATOM   2840 N  N   . PRO A 1 372 ? 50.009 -58.301 -31.432 1.00 41.96  ?  372 PRO A N   1 
ATOM   2841 C  CA  . PRO A 1 372 ? 49.508 -57.637 -30.229 1.00 38.90  ?  372 PRO A CA  1 
ATOM   2842 C  C   . PRO A 1 372 ? 50.294 -56.380 -29.873 1.00 37.73  ?  372 PRO A C   1 
ATOM   2843 O  O   . PRO A 1 372 ? 51.483 -56.264 -30.183 1.00 35.33  ?  372 PRO A O   1 
ATOM   2844 C  CB  . PRO A 1 372 ? 49.697 -58.722 -29.171 1.00 39.77  ?  372 PRO A CB  1 
ATOM   2845 C  CG  . PRO A 1 372 ? 50.983 -59.381 -29.592 1.00 43.90  ?  372 PRO A CG  1 
ATOM   2846 C  CD  . PRO A 1 372 ? 50.883 -59.442 -31.112 1.00 45.18  ?  372 PRO A CD  1 
ATOM   2847 N  N   . GLY A 1 373 ? 49.606 -55.475 -29.173 1.00 35.20  ?  373 GLY A N   1 
ATOM   2848 C  CA  . GLY A 1 373 ? 50.169 -54.207 -28.760 1.00 35.81  ?  373 GLY A CA  1 
ATOM   2849 C  C   . GLY A 1 373 ? 51.404 -54.405 -27.891 1.00 36.55  ?  373 GLY A C   1 
ATOM   2850 O  O   . GLY A 1 373 ? 52.307 -53.575 -27.910 1.00 41.14  ?  373 GLY A O   1 
ATOM   2851 N  N   . LYS A 1 374 ? 51.431 -55.511 -27.144 1.00 37.42  ?  374 LYS A N   1 
ATOM   2852 C  CA  . LYS A 1 374 ? 52.559 -55.847 -26.283 1.00 36.35  ?  374 LYS A CA  1 
ATOM   2853 C  C   . LYS A 1 374 ? 53.854 -55.716 -27.080 1.00 31.86  ?  374 LYS A C   1 
ATOM   2854 O  O   . LYS A 1 374 ? 54.850 -55.289 -26.520 1.00 33.76  ?  374 LYS A O   1 
ATOM   2855 C  CB  . LYS A 1 374 ? 52.386 -57.254 -25.690 1.00 38.67  ?  374 LYS A CB  1 
ATOM   2856 C  CG  . LYS A 1 374 ? 52.982 -57.486 -24.321 1.00 42.32  ?  374 LYS A CG  1 
ATOM   2857 C  CD  . LYS A 1 374 ? 52.999 -58.948 -23.875 1.00 46.75  ?  374 LYS A CD  1 
ATOM   2858 C  CE  . LYS A 1 374 ? 51.697 -59.468 -23.331 1.00 47.84  ?  374 LYS A CE  1 
ATOM   2859 N  NZ  . LYS A 1 374 ? 51.929 -60.717 -22.596 1.00 47.48  1  374 LYS A NZ  1 
ATOM   2860 N  N   . ALA A 1 375 ? 53.815 -56.024 -28.387 1.00 29.60  ?  375 ALA A N   1 
ATOM   2861 C  CA  . ALA A 1 375 ? 54.995 -55.959 -29.246 1.00 31.95  ?  375 ALA A CA  1 
ATOM   2862 C  C   . ALA A 1 375 ? 54.951 -54.783 -30.224 1.00 31.75  ?  375 ALA A C   1 
ATOM   2863 O  O   . ALA A 1 375 ? 55.907 -54.021 -30.336 1.00 31.92  ?  375 ALA A O   1 
ATOM   2864 C  CB  . ALA A 1 375 ? 55.163 -57.257 -30.017 1.00 31.48  ?  375 ALA A CB  1 
ATOM   2865 N  N   . ALA A 1 376 ? 53.879 -54.696 -31.008 1.00 31.01  ?  376 ALA A N   1 
ATOM   2866 C  CA  . ALA A 1 376 ? 53.769 -53.671 -32.030 1.00 29.97  ?  376 ALA A CA  1 
ATOM   2867 C  C   . ALA A 1 376 ? 53.851 -52.254 -31.428 1.00 30.29  ?  376 ALA A C   1 
ATOM   2868 O  O   . ALA A 1 376 ? 54.185 -51.324 -32.160 1.00 31.00  ?  376 ALA A O   1 
ATOM   2869 C  CB  . ALA A 1 376 ? 52.489 -53.887 -32.843 1.00 27.32  ?  376 ALA A CB  1 
ATOM   2870 N  N   . ASN A 1 377 ? 53.582 -52.056 -30.119 1.00 29.11  ?  377 ASN A N   1 
ATOM   2871 C  CA  . ASN A 1 377 ? 53.560 -50.699 -29.559 1.00 30.45  ?  377 ASN A CA  1 
ATOM   2872 C  C   . ASN A 1 377 ? 54.757 -50.370 -28.653 1.00 25.86  ?  377 ASN A C   1 
ATOM   2873 O  O   . ASN A 1 377 ? 54.674 -49.428 -27.867 1.00 20.48  ?  377 ASN A O   1 
ATOM   2874 C  CB  . ASN A 1 377 ? 52.236 -50.369 -28.864 1.00 33.07  ?  377 ASN A CB  1 
ATOM   2875 C  CG  . ASN A 1 377 ? 52.025 -50.977 -27.490 1.00 35.35  ?  377 ASN A CG  1 
ATOM   2876 O  OD1 . ASN A 1 377 ? 52.925 -51.007 -26.637 1.00 34.27  ?  377 ASN A OD1 1 
ATOM   2877 N  ND2 . ASN A 1 377 ? 50.796 -51.408 -27.232 1.00 38.34  ?  377 ASN A ND2 1 
ATOM   2878 N  N   . ALA A 1 378 ? 55.887 -51.069 -28.838 1.00 25.42  ?  378 ALA A N   1 
ATOM   2879 C  CA  . ALA A 1 378 ? 56.978 -51.093 -27.871 1.00 26.49  ?  378 ALA A CA  1 
ATOM   2880 C  C   . ALA A 1 378 ? 58.061 -50.068 -28.214 1.00 26.42  ?  378 ALA A C   1 
ATOM   2881 O  O   . ALA A 1 378 ? 59.166 -50.125 -27.670 1.00 27.69  ?  378 ALA A O   1 
ATOM   2882 C  CB  . ALA A 1 378 ? 57.564 -52.497 -27.779 1.00 26.62  ?  378 ALA A CB  1 
ATOM   2883 N  N   . GLY A 1 379 ? 57.734 -49.106 -29.083 1.00 26.11  ?  379 GLY A N   1 
ATOM   2884 C  CA  . GLY A 1 379 ? 58.678 -48.071 -29.469 1.00 26.32  ?  379 GLY A CA  1 
ATOM   2885 C  C   . GLY A 1 379 ? 59.029 -47.151 -28.298 1.00 27.42  ?  379 GLY A C   1 
ATOM   2886 O  O   . GLY A 1 379 ? 60.176 -46.743 -28.113 1.00 27.47  ?  379 GLY A O   1 
ATOM   2887 N  N   . GLY A 1 380 ? 58.025 -46.778 -27.514 1.00 25.90  ?  380 GLY A N   1 
ATOM   2888 C  CA  . GLY A 1 380 ? 58.269 -45.806 -26.472 1.00 26.25  ?  380 GLY A CA  1 
ATOM   2889 C  C   . GLY A 1 380 ? 59.331 -46.319 -25.520 1.00 24.26  ?  380 GLY A C   1 
ATOM   2890 O  O   . GLY A 1 380 ? 60.176 -45.548 -25.072 1.00 24.88  ?  380 GLY A O   1 
ATOM   2891 N  N   . VAL A 1 381 ? 59.249 -47.624 -25.245 1.00 22.88  ?  381 VAL A N   1 
ATOM   2892 C  CA  . VAL A 1 381 ? 60.108 -48.294 -24.288 1.00 23.89  ?  381 VAL A CA  1 
ATOM   2893 C  C   . VAL A 1 381 ? 61.476 -48.552 -24.915 1.00 25.53  ?  381 VAL A C   1 
ATOM   2894 O  O   . VAL A 1 381 ? 62.492 -48.595 -24.221 1.00 25.40  ?  381 VAL A O   1 
ATOM   2895 C  CB  . VAL A 1 381 ? 59.365 -49.579 -23.871 1.00 24.50  ?  381 VAL A CB  1 
ATOM   2896 C  CG1 . VAL A 1 381 ? 60.275 -50.667 -23.294 1.00 23.72  ?  381 VAL A CG1 1 
ATOM   2897 C  CG2 . VAL A 1 381 ? 58.235 -49.217 -22.912 1.00 24.41  ?  381 VAL A CG2 1 
ATOM   2898 N  N   . ALA A 1 382 ? 61.470 -48.725 -26.241 1.00 25.55  ?  382 ALA A N   1 
ATOM   2899 C  CA  . ALA A 1 382 ? 62.674 -48.863 -27.038 1.00 24.88  ?  382 ALA A CA  1 
ATOM   2900 C  C   . ALA A 1 382 ? 63.512 -47.590 -27.005 1.00 24.78  ?  382 ALA A C   1 
ATOM   2901 O  O   . ALA A 1 382 ? 64.740 -47.665 -27.016 1.00 28.15  ?  382 ALA A O   1 
ATOM   2902 C  CB  . ALA A 1 382 ? 62.266 -49.184 -28.450 1.00 26.50  ?  382 ALA A CB  1 
ATOM   2903 N  N   . VAL A 1 383 ? 62.837 -46.433 -27.028 1.00 25.22  ?  383 VAL A N   1 
ATOM   2904 C  CA  . VAL A 1 383 ? 63.495 -45.136 -27.093 1.00 25.67  ?  383 VAL A CA  1 
ATOM   2905 C  C   . VAL A 1 383 ? 63.928 -44.750 -25.677 1.00 28.43  ?  383 VAL A C   1 
ATOM   2906 O  O   . VAL A 1 383 ? 65.056 -44.270 -25.513 1.00 31.06  ?  383 VAL A O   1 
ATOM   2907 C  CB  . VAL A 1 383 ? 62.621 -44.065 -27.778 1.00 23.99  ?  383 VAL A CB  1 
ATOM   2908 C  CG1 . VAL A 1 383 ? 63.210 -42.658 -27.659 1.00 23.38  ?  383 VAL A CG1 1 
ATOM   2909 C  CG2 . VAL A 1 383 ? 62.376 -44.407 -29.249 1.00 23.79  ?  383 VAL A CG2 1 
ATOM   2910 N  N   . SER A 1 384 ? 63.084 -45.039 -24.665 1.00 24.88  ?  384 SER A N   1 
ATOM   2911 C  CA  . SER A 1 384 ? 63.548 -45.047 -23.290 1.00 25.73  ?  384 SER A CA  1 
ATOM   2912 C  C   . SER A 1 384 ? 64.933 -45.681 -23.234 1.00 25.23  ?  384 SER A C   1 
ATOM   2913 O  O   . SER A 1 384 ? 65.860 -45.107 -22.665 1.00 27.93  ?  384 SER A O   1 
ATOM   2914 C  CB  . SER A 1 384 ? 62.626 -45.791 -22.368 1.00 30.71  ?  384 SER A CB  1 
ATOM   2915 O  OG  . SER A 1 384 ? 61.453 -45.047 -22.076 1.00 36.42  ?  384 SER A OG  1 
ATOM   2916 N  N   . GLY A 1 385 ? 65.036 -46.883 -23.821 1.00 23.22  ?  385 GLY A N   1 
ATOM   2917 C  CA  . GLY A 1 385 ? 66.251 -47.675 -23.859 1.00 21.33  ?  385 GLY A CA  1 
ATOM   2918 C  C   . GLY A 1 385 ? 67.407 -46.896 -24.464 1.00 23.16  ?  385 GLY A C   1 
ATOM   2919 O  O   . GLY A 1 385 ? 68.529 -46.980 -23.977 1.00 22.91  ?  385 GLY A O   1 
ATOM   2920 N  N   . LEU A 1 386 ? 67.113 -46.166 -25.547 1.00 26.08  ?  386 LEU A N   1 
ATOM   2921 C  CA  . LEU A 1 386 ? 68.131 -45.458 -26.318 1.00 26.45  ?  386 LEU A CA  1 
ATOM   2922 C  C   . LEU A 1 386 ? 68.435 -44.115 -25.658 1.00 25.41  ?  386 LEU A C   1 
ATOM   2923 O  O   . LEU A 1 386 ? 69.503 -43.544 -25.880 1.00 25.19  ?  386 LEU A O   1 
ATOM   2924 C  CB  . LEU A 1 386 ? 67.668 -45.262 -27.766 1.00 24.39  ?  386 LEU A CB  1 
ATOM   2925 C  CG  . LEU A 1 386 ? 67.333 -46.538 -28.548 1.00 22.56  ?  386 LEU A CG  1 
ATOM   2926 C  CD1 . LEU A 1 386 ? 66.928 -46.197 -29.991 1.00 21.07  ?  386 LEU A CD1 1 
ATOM   2927 C  CD2 . LEU A 1 386 ? 68.484 -47.561 -28.498 1.00 21.10  ?  386 LEU A CD2 1 
ATOM   2928 N  N   . GLU A 1 387 ? 67.452 -43.596 -24.912 1.00 22.44  ?  387 GLU A N   1 
ATOM   2929 C  CA  . GLU A 1 387 ? 67.642 -42.390 -24.123 1.00 20.71  ?  387 GLU A CA  1 
ATOM   2930 C  C   . GLU A 1 387 ? 68.666 -42.689 -23.031 1.00 20.07  ?  387 GLU A C   1 
ATOM   2931 O  O   . GLU A 1 387 ? 69.541 -41.862 -22.779 1.00 16.91  ?  387 GLU A O   1 
ATOM   2932 C  CB  . GLU A 1 387 ? 66.282 -41.897 -23.615 1.00 19.27  ?  387 GLU A CB  1 
ATOM   2933 C  CG  . GLU A 1 387 ? 66.377 -40.836 -22.531 1.00 18.61  ?  387 GLU A CG  1 
ATOM   2934 C  CD  . GLU A 1 387 ? 65.151 -39.986 -22.275 1.00 19.60  ?  387 GLU A CD  1 
ATOM   2935 O  OE1 . GLU A 1 387 ? 64.007 -40.248 -22.774 1.00 16.13  ?  387 GLU A OE1 1 
ATOM   2936 O  OE2 . GLU A 1 387 ? 65.423 -38.991 -21.520 1.00 23.03  -1 387 GLU A OE2 1 
ATOM   2937 N  N   . MET A 1 388 ? 68.519 -43.881 -22.418 1.00 20.96  ?  388 MET A N   1 
ATOM   2938 C  CA  . MET A 1 388 ? 69.497 -44.478 -21.519 1.00 22.15  ?  388 MET A CA  1 
ATOM   2939 C  C   . MET A 1 388 ? 70.878 -44.580 -22.181 1.00 23.45  ?  388 MET A C   1 
ATOM   2940 O  O   . MET A 1 388 ? 71.866 -44.058 -21.657 1.00 24.29  ?  388 MET A O   1 
ATOM   2941 C  CB  . MET A 1 388 ? 69.042 -45.880 -21.084 1.00 22.43  ?  388 MET A CB  1 
ATOM   2942 C  CG  . MET A 1 388 ? 68.304 -45.926 -19.759 1.00 23.03  ?  388 MET A CG  1 
ATOM   2943 S  SD  . MET A 1 388 ? 67.787 -47.601 -19.319 1.00 20.55  ?  388 MET A SD  1 
ATOM   2944 C  CE  . MET A 1 388 ? 66.256 -47.552 -20.242 1.00 23.80  ?  388 MET A CE  1 
ATOM   2945 N  N   . ALA A 1 389 ? 70.944 -45.267 -23.328 1.00 24.51  ?  389 ALA A N   1 
ATOM   2946 C  CA  . ALA A 1 389 ? 72.197 -45.516 -24.030 1.00 26.44  ?  389 ALA A CA  1 
ATOM   2947 C  C   . ALA A 1 389 ? 72.921 -44.214 -24.374 1.00 29.52  ?  389 ALA A C   1 
ATOM   2948 O  O   . ALA A 1 389 ? 74.153 -44.154 -24.282 1.00 34.16  ?  389 ALA A O   1 
ATOM   2949 C  CB  . ALA A 1 389 ? 71.923 -46.303 -25.291 1.00 27.37  ?  389 ALA A CB  1 
ATOM   2950 N  N   . GLN A 1 390 ? 72.146 -43.204 -24.807 1.00 27.76  ?  390 GLN A N   1 
ATOM   2951 C  CA  . GLN A 1 390 ? 72.665 -41.895 -25.168 1.00 27.84  ?  390 GLN A CA  1 
ATOM   2952 C  C   . GLN A 1 390 ? 73.255 -41.188 -23.957 1.00 27.91  ?  390 GLN A C   1 
ATOM   2953 O  O   . GLN A 1 390 ? 74.384 -40.718 -24.036 1.00 31.09  ?  390 GLN A O   1 
ATOM   2954 C  CB  . GLN A 1 390 ? 71.581 -41.070 -25.855 1.00 30.05  ?  390 GLN A CB  1 
ATOM   2955 C  CG  . GLN A 1 390 ? 71.405 -41.477 -27.310 1.00 32.33  ?  390 GLN A CG  1 
ATOM   2956 C  CD  . GLN A 1 390 ? 70.361 -40.663 -28.023 1.00 33.70  ?  390 GLN A CD  1 
ATOM   2957 O  OE1 . GLN A 1 390 ? 70.688 -39.691 -28.703 1.00 38.62  ?  390 GLN A OE1 1 
ATOM   2958 N  NE2 . GLN A 1 390 ? 69.103 -41.049 -27.881 1.00 35.55  ?  390 GLN A NE2 1 
ATOM   2959 N  N   . ASN A 1 391 ? 72.505 -41.138 -22.844 1.00 28.91  ?  391 ASN A N   1 
ATOM   2960 C  CA  . ASN A 1 391 ? 72.972 -40.530 -21.599 1.00 27.07  ?  391 ASN A CA  1 
ATOM   2961 C  C   . ASN A 1 391 ? 74.303 -41.123 -21.114 1.00 26.52  ?  391 ASN A C   1 
ATOM   2962 O  O   . ASN A 1 391 ? 75.038 -40.451 -20.411 1.00 25.43  ?  391 ASN A O   1 
ATOM   2963 C  CB  . ASN A 1 391 ? 71.965 -40.699 -20.471 1.00 25.70  ?  391 ASN A CB  1 
ATOM   2964 C  CG  . ASN A 1 391 ? 70.657 -39.982 -20.702 1.00 28.46  ?  391 ASN A CG  1 
ATOM   2965 O  OD1 . ASN A 1 391 ? 69.676 -40.262 -19.991 1.00 29.89  ?  391 ASN A OD1 1 
ATOM   2966 N  ND2 . ASN A 1 391 ? 70.593 -39.085 -21.680 1.00 27.66  ?  391 ASN A ND2 1 
ATOM   2967 N  N   . SER A 1 392 ? 74.573 -42.401 -21.415 1.00 27.92  ?  392 SER A N   1 
ATOM   2968 C  CA  . SER A 1 392 ? 75.774 -43.099 -20.966 1.00 28.73  ?  392 SER A CA  1 
ATOM   2969 C  C   . SER A 1 392 ? 76.933 -42.801 -21.927 1.00 29.31  ?  392 SER A C   1 
ATOM   2970 O  O   . SER A 1 392 ? 78.046 -42.441 -21.519 1.00 25.14  ?  392 SER A O   1 
ATOM   2971 C  CB  . SER A 1 392 ? 75.491 -44.595 -20.845 1.00 27.66  ?  392 SER A CB  1 
ATOM   2972 O  OG  . SER A 1 392 ? 74.382 -44.857 -19.988 1.00 25.97  ?  392 SER A OG  1 
ATOM   2973 N  N   . ALA A 1 393 ? 76.616 -42.896 -23.225 1.00 29.54  ?  393 ALA A N   1 
ATOM   2974 C  CA  . ALA A 1 393 ? 77.459 -42.400 -24.302 1.00 30.51  ?  393 ALA A CA  1 
ATOM   2975 C  C   . ALA A 1 393 ? 77.874 -40.932 -24.121 1.00 31.03  ?  393 ALA A C   1 
ATOM   2976 O  O   . ALA A 1 393 ? 78.856 -40.510 -24.735 1.00 32.43  ?  393 ALA A O   1 
ATOM   2977 C  CB  . ALA A 1 393 ? 76.711 -42.594 -25.607 1.00 29.59  ?  393 ALA A CB  1 
ATOM   2978 N  N   . ARG A 1 394 ? 77.112 -40.160 -23.320 1.00 30.69  ?  394 ARG A N   1 
ATOM   2979 C  CA  . ARG A 1 394 ? 77.279 -38.714 -23.173 1.00 31.00  ?  394 ARG A CA  1 
ATOM   2980 C  C   . ARG A 1 394 ? 77.086 -38.054 -24.543 1.00 34.37  ?  394 ARG A C   1 
ATOM   2981 O  O   . ARG A 1 394 ? 78.003 -37.425 -25.065 1.00 42.16  ?  394 ARG A O   1 
ATOM   2982 C  CB  . ARG A 1 394 ? 78.618 -38.294 -22.538 1.00 26.55  ?  394 ARG A CB  1 
ATOM   2983 C  CG  . ARG A 1 394 ? 79.128 -39.230 -21.449 1.00 27.35  ?  394 ARG A CG  1 
ATOM   2984 C  CD  . ARG A 1 394 ? 80.206 -38.681 -20.486 1.00 25.21  ?  394 ARG A CD  1 
ATOM   2985 N  NE  . ARG A 1 394 ? 79.614 -38.083 -19.281 1.00 24.02  ?  394 ARG A NE  1 
ATOM   2986 C  CZ  . ARG A 1 394 ? 79.504 -38.641 -18.072 1.00 23.46  ?  394 ARG A CZ  1 
ATOM   2987 N  NH1 . ARG A 1 394 ? 80.082 -39.805 -17.801 1.00 21.26  1  394 ARG A NH1 1 
ATOM   2988 N  NH2 . ARG A 1 394 ? 78.822 -38.007 -17.120 1.00 24.37  ?  394 ARG A NH2 1 
ATOM   2989 N  N   . LEU A 1 395 ? 75.894 -38.195 -25.135 1.00 31.49  ?  395 LEU A N   1 
ATOM   2990 C  CA  . LEU A 1 395 ? 75.732 -37.841 -26.533 1.00 32.87  ?  395 LEU A CA  1 
ATOM   2991 C  C   . LEU A 1 395 ? 74.264 -37.681 -26.874 1.00 28.75  ?  395 LEU A C   1 
ATOM   2992 O  O   . LEU A 1 395 ? 73.432 -38.393 -26.332 1.00 32.88  ?  395 LEU A O   1 
ATOM   2993 C  CB  . LEU A 1 395 ? 76.329 -38.981 -27.364 1.00 39.93  ?  395 LEU A CB  1 
ATOM   2994 C  CG  . LEU A 1 395 ? 77.305 -38.605 -28.487 1.00 40.44  ?  395 LEU A CG  1 
ATOM   2995 C  CD1 . LEU A 1 395 ? 78.164 -37.385 -28.163 1.00 39.74  ?  395 LEU A CD1 1 
ATOM   2996 C  CD2 . LEU A 1 395 ? 78.184 -39.836 -28.743 1.00 38.85  ?  395 LEU A CD2 1 
ATOM   2997 N  N   . SER A 1 396 ? 73.989 -36.783 -27.816 1.00 24.79  ?  396 SER A N   1 
ATOM   2998 C  CA  . SER A 1 396 ? 72.720 -36.744 -28.512 1.00 24.34  ?  396 SER A CA  1 
ATOM   2999 C  C   . SER A 1 396 ? 72.913 -37.196 -29.958 1.00 25.56  ?  396 SER A C   1 
ATOM   3000 O  O   . SER A 1 396 ? 73.427 -36.456 -30.785 1.00 23.67  ?  396 SER A O   1 
ATOM   3001 C  CB  . SER A 1 396 ? 72.116 -35.364 -28.480 1.00 23.24  ?  396 SER A CB  1 
ATOM   3002 O  OG  . SER A 1 396 ? 71.852 -34.933 -27.159 1.00 21.27  ?  396 SER A OG  1 
ATOM   3003 N  N   . TRP A 1 397 ? 72.433 -38.397 -30.267 1.00 28.86  ?  397 TRP A N   1 
ATOM   3004 C  CA  . TRP A 1 397 ? 72.354 -38.877 -31.634 1.00 33.92  ?  397 TRP A CA  1 
ATOM   3005 C  C   . TRP A 1 397 ? 71.413 -37.975 -32.437 1.00 36.31  ?  397 TRP A C   1 
ATOM   3006 O  O   . TRP A 1 397 ? 70.695 -37.165 -31.852 1.00 38.75  ?  397 TRP A O   1 
ATOM   3007 C  CB  . TRP A 1 397 ? 71.892 -40.345 -31.648 1.00 37.04  ?  397 TRP A CB  1 
ATOM   3008 C  CG  . TRP A 1 397 ? 72.719 -41.290 -30.811 1.00 38.48  ?  397 TRP A CG  1 
ATOM   3009 C  CD1 . TRP A 1 397 ? 73.952 -41.047 -30.275 1.00 43.26  ?  397 TRP A CD1 1 
ATOM   3010 C  CD2 . TRP A 1 397 ? 72.382 -42.646 -30.434 1.00 38.55  ?  397 TRP A CD2 1 
ATOM   3011 N  NE1 . TRP A 1 397 ? 74.388 -42.134 -29.565 1.00 45.33  ?  397 TRP A NE1 1 
ATOM   3012 C  CE2 . TRP A 1 397 ? 73.453 -43.135 -29.659 1.00 41.24  ?  397 TRP A CE2 1 
ATOM   3013 C  CE3 . TRP A 1 397 ? 71.297 -43.494 -30.678 1.00 40.25  ?  397 TRP A CE3 1 
ATOM   3014 C  CZ2 . TRP A 1 397 ? 73.457 -44.424 -29.135 1.00 39.14  ?  397 TRP A CZ2 1 
ATOM   3015 C  CZ3 . TRP A 1 397 ? 71.307 -44.772 -30.167 1.00 36.76  ?  397 TRP A CZ3 1 
ATOM   3016 C  CH2 . TRP A 1 397 ? 72.369 -45.223 -29.395 1.00 37.52  ?  397 TRP A CH2 1 
ATOM   3017 N  N   . THR A 1 398 ? 71.476 -38.088 -33.778 1.00 37.30  ?  398 THR A N   1 
ATOM   3018 C  CA  . THR A 1 398 ? 70.609 -37.365 -34.705 1.00 33.48  ?  398 THR A CA  1 
ATOM   3019 C  C   . THR A 1 398 ? 69.260 -38.079 -34.734 1.00 34.74  ?  398 THR A C   1 
ATOM   3020 O  O   . THR A 1 398 ? 69.167 -39.226 -34.296 1.00 37.76  ?  398 THR A O   1 
ATOM   3021 C  CB  . THR A 1 398 ? 71.217 -37.341 -36.112 1.00 32.26  ?  398 THR A CB  1 
ATOM   3022 O  OG1 . THR A 1 398 ? 71.093 -38.665 -36.617 1.00 32.27  ?  398 THR A OG1 1 
ATOM   3023 C  CG2 . THR A 1 398 ? 72.689 -36.970 -36.173 1.00 32.10  ?  398 THR A CG2 1 
ATOM   3024 N  N   . ALA A 1 399 ? 68.234 -37.432 -35.306 1.00 33.69  ?  399 ALA A N   1 
ATOM   3025 C  CA  . ALA A 1 399 ? 66.915 -38.037 -35.425 1.00 32.56  ?  399 ALA A CA  1 
ATOM   3026 C  C   . ALA A 1 399 ? 66.984 -39.361 -36.189 1.00 34.01  ?  399 ALA A C   1 
ATOM   3027 O  O   . ALA A 1 399 ? 66.375 -40.341 -35.764 1.00 35.57  ?  399 ALA A O   1 
ATOM   3028 C  CB  . ALA A 1 399 ? 65.977 -37.067 -36.087 1.00 32.35  ?  399 ALA A CB  1 
ATOM   3029 N  N   . GLU A 1 400 ? 67.725 -39.347 -37.312 1.00 37.03  ?  400 GLU A N   1 
ATOM   3030 C  CA  . GLU A 1 400 ? 67.948 -40.478 -38.203 1.00 37.06  ?  400 GLU A CA  1 
ATOM   3031 C  C   . GLU A 1 400 ? 68.551 -41.662 -37.451 1.00 38.77  ?  400 GLU A C   1 
ATOM   3032 O  O   . GLU A 1 400 ? 68.084 -42.790 -37.615 1.00 38.62  ?  400 GLU A O   1 
ATOM   3033 C  CB  . GLU A 1 400 ? 68.932 -40.095 -39.309 1.00 39.36  ?  400 GLU A CB  1 
ATOM   3034 C  CG  . GLU A 1 400 ? 68.357 -39.131 -40.343 1.00 45.15  ?  400 GLU A CG  1 
ATOM   3035 C  CD  . GLU A 1 400 ? 68.194 -37.664 -39.967 1.00 49.25  ?  400 GLU A CD  1 
ATOM   3036 O  OE1 . GLU A 1 400 ? 68.399 -37.294 -38.791 1.00 46.77  ?  400 GLU A OE1 1 
ATOM   3037 O  OE2 . GLU A 1 400 ? 67.871 -36.881 -40.896 1.00 53.11  -1 400 GLU A OE2 1 
ATOM   3038 N  N   . GLU A 1 401 ? 69.606 -41.392 -36.660 1.00 37.70  ?  401 GLU A N   1 
ATOM   3039 C  CA  . GLU A 1 401 ? 70.261 -42.407 -35.842 1.00 40.49  ?  401 GLU A CA  1 
ATOM   3040 C  C   . GLU A 1 401 ? 69.237 -43.096 -34.925 1.00 34.37  ?  401 GLU A C   1 
ATOM   3041 O  O   . GLU A 1 401 ? 69.171 -44.324 -34.893 1.00 27.03  ?  401 GLU A O   1 
ATOM   3042 C  CB  . GLU A 1 401 ? 71.430 -41.796 -35.058 1.00 45.26  ?  401 GLU A CB  1 
ATOM   3043 C  CG  . GLU A 1 401 ? 72.749 -41.687 -35.829 1.00 49.96  ?  401 GLU A CG  1 
ATOM   3044 C  CD  . GLU A 1 401 ? 73.678 -40.588 -35.300 1.00 53.98  ?  401 GLU A CD  1 
ATOM   3045 O  OE1 . GLU A 1 401 ? 74.193 -39.752 -36.089 1.00 51.81  ?  401 GLU A OE1 1 
ATOM   3046 O  OE2 . GLU A 1 401 ? 73.844 -40.527 -34.063 1.00 51.74  -1 401 GLU A OE2 1 
ATOM   3047 N  N   . VAL A 1 402 ? 68.437 -42.297 -34.202 1.00 31.52  ?  402 VAL A N   1 
ATOM   3048 C  CA  . VAL A 1 402 ? 67.482 -42.802 -33.219 1.00 33.07  ?  402 VAL A CA  1 
ATOM   3049 C  C   . VAL A 1 402 ? 66.423 -43.653 -33.935 1.00 33.21  ?  402 VAL A C   1 
ATOM   3050 O  O   . VAL A 1 402 ? 66.145 -44.776 -33.500 1.00 30.73  ?  402 VAL A O   1 
ATOM   3051 C  CB  . VAL A 1 402 ? 66.831 -41.688 -32.353 1.00 29.89  ?  402 VAL A CB  1 
ATOM   3052 C  CG1 . VAL A 1 402 ? 65.927 -42.238 -31.263 1.00 27.79  ?  402 VAL A CG1 1 
ATOM   3053 C  CG2 . VAL A 1 402 ? 67.861 -40.792 -31.677 1.00 29.71  ?  402 VAL A CG2 1 
ATOM   3054 N  N   . ASP A 1 403 ? 65.848 -43.116 -35.029 1.00 32.78  ?  403 ASP A N   1 
ATOM   3055 C  CA  . ASP A 1 403 ? 64.808 -43.786 -35.812 1.00 32.80  ?  403 ASP A CA  1 
ATOM   3056 C  C   . ASP A 1 403 ? 65.272 -45.140 -36.370 1.00 30.25  ?  403 ASP A C   1 
ATOM   3057 O  O   . ASP A 1 403 ? 64.514 -46.111 -36.457 1.00 29.52  ?  403 ASP A O   1 
ATOM   3058 C  CB  . ASP A 1 403 ? 64.350 -42.889 -36.950 1.00 33.42  ?  403 ASP A CB  1 
ATOM   3059 C  CG  . ASP A 1 403 ? 62.875 -42.987 -37.312 1.00 36.65  ?  403 ASP A CG  1 
ATOM   3060 O  OD1 . ASP A 1 403 ? 62.178 -43.876 -36.756 1.00 33.36  ?  403 ASP A OD1 1 
ATOM   3061 O  OD2 . ASP A 1 403 ? 62.423 -42.130 -38.110 1.00 38.66  -1 403 ASP A OD2 1 
ATOM   3062 N  N   . ALA A 1 404 ? 66.540 -45.176 -36.771 1.00 27.64  ?  404 ALA A N   1 
ATOM   3063 C  CA  . ALA A 1 404 ? 67.171 -46.357 -37.329 1.00 26.17  ?  404 ALA A CA  1 
ATOM   3064 C  C   . ALA A 1 404 ? 67.323 -47.444 -36.268 1.00 23.45  ?  404 ALA A C   1 
ATOM   3065 O  O   . ALA A 1 404 ? 67.220 -48.620 -36.587 1.00 21.48  ?  404 ALA A O   1 
ATOM   3066 C  CB  . ALA A 1 404 ? 68.523 -45.953 -37.915 1.00 26.60  ?  404 ALA A CB  1 
ATOM   3067 N  N   . ARG A 1 405 ? 67.663 -47.037 -35.035 1.00 25.19  ?  405 ARG A N   1 
ATOM   3068 C  CA  . ARG A 1 405 ? 67.850 -47.959 -33.926 1.00 25.96  ?  405 ARG A CA  1 
ATOM   3069 C  C   . ARG A 1 405 ? 66.487 -48.389 -33.407 1.00 27.21  ?  405 ARG A C   1 
ATOM   3070 O  O   . ARG A 1 405 ? 66.301 -49.540 -33.041 1.00 28.10  ?  405 ARG A O   1 
ATOM   3071 C  CB  . ARG A 1 405 ? 68.726 -47.401 -32.805 1.00 25.07  ?  405 ARG A CB  1 
ATOM   3072 C  CG  . ARG A 1 405 ? 70.191 -47.408 -33.202 1.00 27.42  ?  405 ARG A CG  1 
ATOM   3073 C  CD  . ARG A 1 405 ? 71.158 -47.681 -32.044 1.00 30.83  ?  405 ARG A CD  1 
ATOM   3074 N  NE  . ARG A 1 405 ? 72.504 -48.100 -32.467 1.00 31.45  ?  405 ARG A NE  1 
ATOM   3075 C  CZ  . ARG A 1 405 ? 72.789 -49.297 -32.993 1.00 40.24  ?  405 ARG A CZ  1 
ATOM   3076 N  NH1 . ARG A 1 405 ? 71.826 -50.211 -33.183 1.00 43.62  1  405 ARG A NH1 1 
ATOM   3077 N  NH2 . ARG A 1 405 ? 74.044 -49.574 -33.336 1.00 39.68  ?  405 ARG A NH2 1 
ATOM   3078 N  N   . LEU A 1 406 ? 65.525 -47.471 -33.458 1.00 31.31  ?  406 LEU A N   1 
ATOM   3079 C  CA  . LEU A 1 406 ? 64.149 -47.806 -33.142 1.00 34.54  ?  406 LEU A CA  1 
ATOM   3080 C  C   . LEU A 1 406 ? 63.710 -48.926 -34.089 1.00 41.84  ?  406 LEU A C   1 
ATOM   3081 O  O   . LEU A 1 406 ? 63.119 -49.918 -33.655 1.00 45.71  ?  406 LEU A O   1 
ATOM   3082 C  CB  . LEU A 1 406 ? 63.266 -46.555 -33.212 1.00 32.13  ?  406 LEU A CB  1 
ATOM   3083 C  CG  . LEU A 1 406 ? 61.751 -46.799 -33.156 1.00 34.78  ?  406 LEU A CG  1 
ATOM   3084 C  CD1 . LEU A 1 406 ? 61.303 -47.435 -31.847 1.00 36.28  ?  406 LEU A CD1 1 
ATOM   3085 C  CD2 . LEU A 1 406 ? 60.967 -45.522 -33.391 1.00 37.35  ?  406 LEU A CD2 1 
ATOM   3086 N  N   . LYS A 1 407 ? 64.030 -48.776 -35.383 1.00 44.64  ?  407 LYS A N   1 
ATOM   3087 C  CA  . LYS A 1 407 ? 63.635 -49.762 -36.372 1.00 46.97  ?  407 LYS A CA  1 
ATOM   3088 C  C   . LYS A 1 407 ? 64.291 -51.096 -36.020 1.00 40.65  ?  407 LYS A C   1 
ATOM   3089 O  O   . LYS A 1 407 ? 63.654 -52.138 -36.128 1.00 43.11  ?  407 LYS A O   1 
ATOM   3090 C  CB  . LYS A 1 407 ? 63.930 -49.265 -37.796 1.00 57.88  ?  407 LYS A CB  1 
ATOM   3091 C  CG  . LYS A 1 407 ? 63.570 -50.219 -38.958 1.00 63.10  ?  407 LYS A CG  1 
ATOM   3092 C  CD  . LYS A 1 407 ? 64.318 -49.954 -40.262 1.00 70.96  ?  407 LYS A CD  1 
ATOM   3093 C  CE  . LYS A 1 407 ? 65.825 -49.949 -40.088 1.00 79.53  ?  407 LYS A CE  1 
ATOM   3094 N  NZ  . LYS A 1 407 ? 66.574 -49.872 -41.348 1.00 83.56  1  407 LYS A NZ  1 
ATOM   3095 N  N   . ASP A 1 408 ? 65.546 -51.088 -35.569 1.00 38.72  ?  408 ASP A N   1 
ATOM   3096 C  CA  . ASP A 1 408 ? 66.196 -52.365 -35.322 1.00 42.46  ?  408 ASP A CA  1 
ATOM   3097 C  C   . ASP A 1 408 ? 65.601 -53.034 -34.091 1.00 37.54  ?  408 ASP A C   1 
ATOM   3098 O  O   . ASP A 1 408 ? 65.539 -54.263 -34.050 1.00 35.55  ?  408 ASP A O   1 
ATOM   3099 C  CB  . ASP A 1 408 ? 67.710 -52.322 -35.201 1.00 48.01  ?  408 ASP A CB  1 
ATOM   3100 C  CG  . ASP A 1 408 ? 68.362 -53.675 -35.467 1.00 49.82  ?  408 ASP A CG  1 
ATOM   3101 O  OD1 . ASP A 1 408 ? 69.349 -54.025 -34.781 1.00 55.90  ?  408 ASP A OD1 1 
ATOM   3102 O  OD2 . ASP A 1 408 ? 67.851 -54.391 -36.350 1.00 50.30  -1 408 ASP A OD2 1 
ATOM   3103 N  N   . ILE A 1 409 ? 65.170 -52.232 -33.105 1.00 33.34  ?  409 ILE A N   1 
ATOM   3104 C  CA  . ILE A 1 409 ? 64.594 -52.802 -31.892 1.00 31.29  ?  409 ILE A CA  1 
ATOM   3105 C  C   . ILE A 1 409 ? 63.233 -53.432 -32.222 1.00 34.46  ?  409 ILE A C   1 
ATOM   3106 O  O   . ILE A 1 409 ? 62.891 -54.470 -31.646 1.00 31.78  ?  409 ILE A O   1 
ATOM   3107 C  CB  . ILE A 1 409 ? 64.569 -51.823 -30.693 1.00 25.67  ?  409 ILE A CB  1 
ATOM   3108 C  CG1 . ILE A 1 409 ? 65.920 -51.741 -29.982 1.00 26.07  ?  409 ILE A CG1 1 
ATOM   3109 C  CG2 . ILE A 1 409 ? 63.531 -52.247 -29.664 1.00 24.58  ?  409 ILE A CG2 1 
ATOM   3110 C  CD1 . ILE A 1 409 ? 66.929 -50.790 -30.587 1.00 27.02  ?  409 ILE A CD1 1 
ATOM   3111 N  N   . MET A 1 410 ? 62.493 -52.864 -33.193 1.00 39.12  ?  410 MET A N   1 
ATOM   3112 C  CA  . MET A 1 410 ? 61.209 -53.433 -33.594 1.00 43.85  ?  410 MET A CA  1 
ATOM   3113 C  C   . MET A 1 410 ? 61.388 -54.758 -34.345 1.00 41.50  ?  410 MET A C   1 
ATOM   3114 O  O   . MET A 1 410 ? 60.558 -55.660 -34.204 1.00 40.78  ?  410 MET A O   1 
ATOM   3115 C  CB  . MET A 1 410 ? 60.368 -52.464 -34.431 1.00 47.13  ?  410 MET A CB  1 
ATOM   3116 C  CG  . MET A 1 410 ? 60.111 -51.119 -33.746 1.00 52.72  ?  410 MET A CG  1 
ATOM   3117 S  SD  . MET A 1 410 ? 59.586 -51.172 -32.018 1.00 46.12  ?  410 MET A SD  1 
ATOM   3118 C  CE  . MET A 1 410 ? 57.897 -51.766 -32.177 1.00 47.40  ?  410 MET A CE  1 
ATOM   3119 N  N   . LYS A 1 411 ? 62.479 -54.930 -35.098 1.00 37.75  ?  411 LYS A N   1 
ATOM   3120 C  CA  . LYS A 1 411 ? 62.704 -56.246 -35.682 1.00 37.77  ?  411 LYS A CA  1 
ATOM   3121 C  C   . LYS A 1 411 ? 62.958 -57.251 -34.558 1.00 32.03  ?  411 LYS A C   1 
ATOM   3122 O  O   . LYS A 1 411 ? 62.466 -58.370 -34.595 1.00 31.28  ?  411 LYS A O   1 
ATOM   3123 C  CB  . LYS A 1 411 ? 63.801 -56.348 -36.751 1.00 41.07  ?  411 LYS A CB  1 
ATOM   3124 C  CG  . LYS A 1 411 ? 63.533 -57.445 -37.799 1.00 41.97  ?  411 LYS A CG  1 
ATOM   3125 C  CD  . LYS A 1 411 ? 64.754 -57.979 -38.546 1.00 44.07  ?  411 LYS A CD  1 
ATOM   3126 C  CE  . LYS A 1 411 ? 64.388 -58.813 -39.738 1.00 44.37  ?  411 LYS A CE  1 
ATOM   3127 N  NZ  . LYS A 1 411 ? 65.553 -59.303 -40.485 1.00 46.00  1  411 LYS A NZ  1 
ATOM   3128 N  N   . SER A 1 412 ? 63.711 -56.849 -33.539 1.00 28.95  ?  412 SER A N   1 
ATOM   3129 C  CA  . SER A 1 412 ? 64.052 -57.771 -32.474 1.00 28.14  ?  412 SER A CA  1 
ATOM   3130 C  C   . SER A 1 412 ? 62.792 -58.240 -31.757 1.00 29.12  ?  412 SER A C   1 
ATOM   3131 O  O   . SER A 1 412 ? 62.700 -59.419 -31.414 1.00 32.81  ?  412 SER A O   1 
ATOM   3132 C  CB  . SER A 1 412 ? 65.024 -57.163 -31.517 1.00 28.58  ?  412 SER A CB  1 
ATOM   3133 O  OG  . SER A 1 412 ? 66.222 -56.832 -32.203 1.00 30.30  ?  412 SER A OG  1 
ATOM   3134 N  N   A CYS A 1 413 ? 61.855 -57.308 -31.518 0.49 28.67  ?  413 CYS A N   1 
ATOM   3135 N  N   B CYS A 1 413 ? 61.842 -57.318 -31.539 0.51 28.27  ?  413 CYS A N   1 
ATOM   3136 C  CA  A CYS A 1 413 ? 60.535 -57.626 -30.985 0.49 27.67  ?  413 CYS A CA  1 
ATOM   3137 C  CA  B CYS A 1 413 ? 60.539 -57.649 -30.973 0.51 26.98  ?  413 CYS A CA  1 
ATOM   3138 C  C   A CYS A 1 413 ? 59.845 -58.694 -31.832 0.49 26.72  ?  413 CYS A C   1 
ATOM   3139 C  C   B CYS A 1 413 ? 59.831 -58.698 -31.829 0.51 26.31  ?  413 CYS A C   1 
ATOM   3140 O  O   A CYS A 1 413 ? 59.521 -59.776 -31.344 0.49 24.60  ?  413 CYS A O   1 
ATOM   3141 O  O   B CYS A 1 413 ? 59.489 -59.778 -31.348 0.51 24.19  ?  413 CYS A O   1 
ATOM   3142 C  CB  A CYS A 1 413 ? 59.642 -56.392 -30.964 0.49 27.47  ?  413 CYS A CB  1 
ATOM   3143 C  CB  B CYS A 1 413 ? 59.660 -56.409 -30.877 0.51 26.29  ?  413 CYS A CB  1 
ATOM   3144 S  SG  A CYS A 1 413 ? 59.836 -55.390 -29.471 0.49 28.38  ?  413 CYS A SG  1 
ATOM   3145 S  SG  B CYS A 1 413 ? 60.490 -55.022 -30.068 0.51 26.26  ?  413 CYS A SG  1 
ATOM   3146 N  N   . PHE A 1 414 ? 59.617 -58.351 -33.106 1.00 27.65  ?  414 PHE A N   1 
ATOM   3147 C  CA  . PHE A 1 414 ? 59.022 -59.246 -34.086 1.00 26.38  ?  414 PHE A CA  1 
ATOM   3148 C  C   . PHE A 1 414 ? 59.679 -60.617 -34.013 1.00 24.74  ?  414 PHE A C   1 
ATOM   3149 O  O   . PHE A 1 414 ? 58.994 -61.601 -33.759 1.00 23.27  ?  414 PHE A O   1 
ATOM   3150 C  CB  . PHE A 1 414 ? 59.159 -58.658 -35.493 1.00 26.04  ?  414 PHE A CB  1 
ATOM   3151 C  CG  . PHE A 1 414 ? 58.791 -59.673 -36.557 1.00 27.30  ?  414 PHE A CG  1 
ATOM   3152 C  CD1 . PHE A 1 414 ? 57.461 -59.963 -36.842 1.00 29.84  ?  414 PHE A CD1 1 
ATOM   3153 C  CD2 . PHE A 1 414 ? 59.771 -60.363 -37.248 1.00 28.29  ?  414 PHE A CD2 1 
ATOM   3154 C  CE1 . PHE A 1 414 ? 57.125 -60.901 -37.804 1.00 27.97  ?  414 PHE A CE1 1 
ATOM   3155 C  CE2 . PHE A 1 414 ? 59.421 -61.311 -38.195 1.00 29.52  ?  414 PHE A CE2 1 
ATOM   3156 C  CZ  . PHE A 1 414 ? 58.100 -61.571 -38.473 1.00 26.97  ?  414 PHE A CZ  1 
ATOM   3157 N  N   A GLN A 1 415 ? 61.006 -60.655 -34.216 0.50 25.24  ?  415 GLN A N   1 
ATOM   3158 N  N   B GLN A 1 415 ? 61.004 -60.642 -34.198 0.50 24.68  ?  415 GLN A N   1 
ATOM   3159 C  CA  A GLN A 1 415 ? 61.737 -61.906 -34.372 0.50 26.02  ?  415 GLN A CA  1 
ATOM   3160 C  CA  B GLN A 1 415 ? 61.748 -61.880 -34.359 0.50 25.01  ?  415 GLN A CA  1 
ATOM   3161 C  C   A GLN A 1 415 ? 61.552 -62.782 -33.141 0.50 26.01  ?  415 GLN A C   1 
ATOM   3162 C  C   B GLN A 1 415 ? 61.560 -62.774 -33.144 0.50 25.44  ?  415 GLN A C   1 
ATOM   3163 O  O   A GLN A 1 415 ? 61.322 -63.980 -33.281 0.50 28.35  ?  415 GLN A O   1 
ATOM   3164 O  O   B GLN A 1 415 ? 61.330 -63.971 -33.298 0.50 27.71  ?  415 GLN A O   1 
ATOM   3165 C  CB  A GLN A 1 415 ? 63.230 -61.721 -34.654 0.50 27.20  ?  415 GLN A CB  1 
ATOM   3166 C  CB  B GLN A 1 415 ? 63.222 -61.578 -34.616 0.50 25.40  ?  415 GLN A CB  1 
ATOM   3167 C  CG  A GLN A 1 415 ? 63.618 -61.875 -36.125 0.50 27.21  ?  415 GLN A CG  1 
ATOM   3168 C  CG  B GLN A 1 415 ? 63.531 -61.261 -36.077 0.50 24.84  ?  415 GLN A CG  1 
ATOM   3169 C  CD  A GLN A 1 415 ? 65.048 -61.467 -36.417 0.50 26.74  ?  415 GLN A CD  1 
ATOM   3170 C  CD  B GLN A 1 415 ? 63.556 -62.498 -36.943 0.50 23.40  ?  415 GLN A CD  1 
ATOM   3171 O  OE1 A GLN A 1 415 ? 65.847 -61.181 -35.511 0.50 23.34  ?  415 GLN A OE1 1 
ATOM   3172 O  OE1 B GLN A 1 415 ? 63.259 -63.611 -36.491 0.50 22.22  ?  415 GLN A OE1 1 
ATOM   3173 N  NE2 A GLN A 1 415 ? 65.375 -61.431 -37.702 0.50 26.93  ?  415 GLN A NE2 1 
ATOM   3174 N  NE2 B GLN A 1 415 ? 63.933 -62.305 -38.194 0.50 23.06  ?  415 GLN A NE2 1 
ATOM   3175 N  N   . ASN A 1 416 ? 61.643 -62.165 -31.956 1.00 25.83  ?  416 ASN A N   1 
ATOM   3176 C  CA  . ASN A 1 416 ? 61.496 -62.855 -30.681 1.00 26.10  ?  416 ASN A CA  1 
ATOM   3177 C  C   . ASN A 1 416 ? 60.174 -63.607 -30.606 1.00 25.08  ?  416 ASN A C   1 
ATOM   3178 O  O   . ASN A 1 416 ? 60.111 -64.726 -30.114 1.00 23.62  ?  416 ASN A O   1 
ATOM   3179 C  CB  . ASN A 1 416 ? 61.602 -61.882 -29.505 1.00 27.13  ?  416 ASN A CB  1 
ATOM   3180 C  CG  . ASN A 1 416 ? 63.032 -61.600 -29.098 1.00 30.00  ?  416 ASN A CG  1 
ATOM   3181 O  OD1 . ASN A 1 416 ? 63.909 -62.457 -29.251 1.00 34.46  ?  416 ASN A OD1 1 
ATOM   3182 N  ND2 . ASN A 1 416 ? 63.291 -60.435 -28.524 1.00 30.67  ?  416 ASN A ND2 1 
ATOM   3183 N  N   . GLY A 1 417 ? 59.108 -62.968 -31.066 1.00 29.17  ?  417 GLY A N   1 
ATOM   3184 C  CA  . GLY A 1 417 ? 57.805 -63.608 -31.066 1.00 35.23  ?  417 GLY A CA  1 
ATOM   3185 C  C   . GLY A 1 417 ? 57.768 -64.744 -32.082 1.00 36.56  ?  417 GLY A C   1 
ATOM   3186 O  O   . GLY A 1 417 ? 57.422 -65.881 -31.734 1.00 40.43  ?  417 GLY A O   1 
ATOM   3187 N  N   . LEU A 1 418 ? 58.149 -64.395 -33.320 1.00 34.25  ?  418 LEU A N   1 
ATOM   3188 C  CA  . LEU A 1 418 ? 58.218 -65.338 -34.420 1.00 33.55  ?  418 LEU A CA  1 
ATOM   3189 C  C   . LEU A 1 418 ? 58.895 -66.623 -33.952 1.00 31.94  ?  418 LEU A C   1 
ATOM   3190 O  O   . LEU A 1 418 ? 58.256 -67.675 -33.899 1.00 29.62  ?  418 LEU A O   1 
ATOM   3191 C  CB  . LEU A 1 418 ? 58.951 -64.753 -35.628 1.00 32.90  ?  418 LEU A CB  1 
ATOM   3192 C  CG  . LEU A 1 418 ? 58.710 -65.530 -36.928 1.00 31.73  ?  418 LEU A CG  1 
ATOM   3193 C  CD1 . LEU A 1 418 ? 57.453 -64.993 -37.598 1.00 30.78  ?  418 LEU A CD1 1 
ATOM   3194 C  CD2 . LEU A 1 418 ? 59.912 -65.501 -37.852 1.00 31.69  ?  418 LEU A CD2 1 
ATOM   3195 N  N   . ASP A 1 419 ? 60.187 -66.509 -33.615 1.00 30.71  ?  419 ASP A N   1 
ATOM   3196 C  CA  . ASP A 1 419 ? 61.008 -67.658 -33.274 1.00 33.33  ?  419 ASP A CA  1 
ATOM   3197 C  C   . ASP A 1 419 ? 60.292 -68.477 -32.190 1.00 37.35  ?  419 ASP A C   1 
ATOM   3198 O  O   . ASP A 1 419 ? 60.213 -69.708 -32.295 1.00 45.18  ?  419 ASP A O   1 
ATOM   3199 C  CB  . ASP A 1 419 ? 62.428 -67.217 -32.941 1.00 33.94  ?  419 ASP A CB  1 
ATOM   3200 C  CG  . ASP A 1 419 ? 63.252 -66.610 -34.080 1.00 36.84  ?  419 ASP A CG  1 
ATOM   3201 O  OD1 . ASP A 1 419 ? 64.336 -66.044 -33.783 1.00 37.55  ?  419 ASP A OD1 1 
ATOM   3202 O  OD2 . ASP A 1 419 ? 62.839 -66.727 -35.264 1.00 34.42  -1 419 ASP A OD2 1 
ATOM   3203 N  N   . THR A 1 420 ? 59.719 -67.793 -31.181 1.00 33.37  ?  420 THR A N   1 
ATOM   3204 C  CA  . THR A 1 420 ? 59.133 -68.452 -30.022 1.00 32.18  ?  420 THR A CA  1 
ATOM   3205 C  C   . THR A 1 420 ? 57.959 -69.333 -30.449 1.00 32.87  ?  420 THR A C   1 
ATOM   3206 O  O   . THR A 1 420 ? 57.931 -70.538 -30.174 1.00 31.23  ?  420 THR A O   1 
ATOM   3207 C  CB  . THR A 1 420 ? 58.703 -67.422 -28.981 1.00 31.88  ?  420 THR A CB  1 
ATOM   3208 O  OG1 . THR A 1 420 ? 59.878 -66.769 -28.516 1.00 31.74  ?  420 THR A OG1 1 
ATOM   3209 C  CG2 . THR A 1 420 ? 58.044 -68.074 -27.780 1.00 32.63  ?  420 THR A CG2 1 
ATOM   3210 N  N   . ALA A 1 421 ? 57.002 -68.705 -31.133 1.00 33.49  ?  421 ALA A N   1 
ATOM   3211 C  CA  . ALA A 1 421 ? 55.870 -69.394 -31.729 1.00 35.59  ?  421 ALA A CA  1 
ATOM   3212 C  C   . ALA A 1 421 ? 56.298 -70.589 -32.591 1.00 35.09  ?  421 ALA A C   1 
ATOM   3213 O  O   . ALA A 1 421 ? 55.657 -71.636 -32.526 1.00 33.01  ?  421 ALA A O   1 
ATOM   3214 C  CB  . ALA A 1 421 ? 55.063 -68.383 -32.519 1.00 38.09  ?  421 ALA A CB  1 
ATOM   3215 N  N   . LYS A 1 422 ? 57.385 -70.444 -33.379 1.00 37.95  ?  422 LYS A N   1 
ATOM   3216 C  CA  . LYS A 1 422 ? 57.925 -71.513 -34.224 1.00 37.40  ?  422 LYS A CA  1 
ATOM   3217 C  C   . LYS A 1 422 ? 58.471 -72.685 -33.408 1.00 39.79  ?  422 LYS A C   1 
ATOM   3218 O  O   . LYS A 1 422 ? 58.522 -73.813 -33.915 1.00 35.71  ?  422 LYS A O   1 
ATOM   3219 C  CB  . LYS A 1 422 ? 59.105 -71.051 -35.090 1.00 37.82  ?  422 LYS A CB  1 
ATOM   3220 C  CG  . LYS A 1 422 ? 58.710 -70.277 -36.336 1.00 40.22  ?  422 LYS A CG  1 
ATOM   3221 C  CD  . LYS A 1 422 ? 59.547 -70.543 -37.583 1.00 40.74  ?  422 LYS A CD  1 
ATOM   3222 C  CE  . LYS A 1 422 ? 60.929 -69.996 -37.502 1.00 42.07  ?  422 LYS A CE  1 
ATOM   3223 N  NZ  . LYS A 1 422 ? 61.298 -69.423 -38.798 1.00 41.99  1  422 LYS A NZ  1 
ATOM   3224 N  N   A GLU A 1 423 ? 58.881 -72.394 -32.164 0.50 40.15  ?  423 GLU A N   1 
ATOM   3225 N  N   B GLU A 1 423 ? 58.906 -72.387 -32.170 0.50 40.55  ?  423 GLU A N   1 
ATOM   3226 C  CA  A GLU A 1 423 ? 59.420 -73.392 -31.256 0.50 38.35  ?  423 GLU A CA  1 
ATOM   3227 C  CA  B GLU A 1 423 ? 59.442 -73.363 -31.232 0.50 39.10  ?  423 GLU A CA  1 
ATOM   3228 C  C   A GLU A 1 423 ? 58.290 -74.027 -30.445 0.50 34.92  ?  423 GLU A C   1 
ATOM   3229 C  C   B GLU A 1 423 ? 58.295 -74.015 -30.456 0.50 35.22  ?  423 GLU A C   1 
ATOM   3230 O  O   A GLU A 1 423 ? 58.193 -75.248 -30.390 0.50 33.39  ?  423 GLU A O   1 
ATOM   3231 O  O   B GLU A 1 423 ? 58.173 -75.235 -30.458 0.50 33.51  ?  423 GLU A O   1 
ATOM   3232 C  CB  A GLU A 1 423 ? 60.490 -72.750 -30.368 0.50 38.78  ?  423 GLU A CB  1 
ATOM   3233 C  CB  B GLU A 1 423 ? 60.470 -72.655 -30.335 0.50 40.08  ?  423 GLU A CB  1 
ATOM   3234 C  CG  A GLU A 1 423 ? 61.528 -73.764 -29.896 0.50 38.71  ?  423 GLU A CG  1 
ATOM   3235 C  CG  B GLU A 1 423 ? 61.423 -73.587 -29.584 0.50 40.81  ?  423 GLU A CG  1 
ATOM   3236 C  CD  A GLU A 1 423 ? 61.943 -74.684 -31.030 0.50 38.51  ?  423 GLU A CD  1 
ATOM   3237 C  CD  B GLU A 1 423 ? 62.706 -72.937 -29.071 0.50 41.58  ?  423 GLU A CD  1 
ATOM   3238 O  OE1 A GLU A 1 423 ? 61.894 -74.211 -32.180 0.50 39.71  ?  423 GLU A OE1 1 
ATOM   3239 O  OE1 B GLU A 1 423 ? 63.689 -73.660 -28.807 0.50 39.44  ?  423 GLU A OE1 1 
ATOM   3240 O  OE2 A GLU A 1 423 ? 62.257 -75.866 -30.794 0.50 38.13  -1 423 GLU A OE2 1 
ATOM   3241 O  OE2 B GLU A 1 423 ? 62.726 -71.699 -28.906 0.50 42.83  -1 423 GLU A OE2 1 
ATOM   3242 N  N   . TYR A 1 424 ? 57.449 -73.199 -29.807 1.00 32.86  ?  424 TYR A N   1 
ATOM   3243 C  CA  . TYR A 1 424 ? 56.586 -73.673 -28.724 1.00 30.38  ?  424 TYR A CA  1 
ATOM   3244 C  C   . TYR A 1 424 ? 55.109 -73.624 -29.089 1.00 28.15  ?  424 TYR A C   1 
ATOM   3245 O  O   . TYR A 1 424 ? 54.283 -74.006 -28.277 1.00 28.95  ?  424 TYR A O   1 
ATOM   3246 C  CB  . TYR A 1 424 ? 56.768 -72.883 -27.424 1.00 29.81  ?  424 TYR A CB  1 
ATOM   3247 C  CG  . TYR A 1 424 ? 58.176 -73.037 -26.877 1.00 31.70  ?  424 TYR A CG  1 
ATOM   3248 C  CD1 . TYR A 1 424 ? 59.097 -71.996 -26.942 1.00 32.76  ?  424 TYR A CD1 1 
ATOM   3249 C  CD2 . TYR A 1 424 ? 58.613 -74.260 -26.383 1.00 32.96  ?  424 TYR A CD2 1 
ATOM   3250 C  CE1 . TYR A 1 424 ? 60.394 -72.153 -26.478 1.00 32.48  ?  424 TYR A CE1 1 
ATOM   3251 C  CE2 . TYR A 1 424 ? 59.915 -74.438 -25.937 1.00 31.73  ?  424 TYR A CE2 1 
ATOM   3252 C  CZ  . TYR A 1 424 ? 60.804 -73.379 -25.984 1.00 31.17  ?  424 TYR A CZ  1 
ATOM   3253 O  OH  . TYR A 1 424 ? 62.078 -73.537 -25.538 1.00 29.99  ?  424 TYR A OH  1 
ATOM   3254 N  N   . ALA A 1 425 ? 54.791 -73.143 -30.289 1.00 28.38  ?  425 ALA A N   1 
ATOM   3255 C  CA  . ALA A 1 425 ? 53.454 -73.237 -30.846 1.00 30.06  ?  425 ALA A CA  1 
ATOM   3256 C  C   . ALA A 1 425 ? 53.598 -73.510 -32.348 1.00 30.85  ?  425 ALA A C   1 
ATOM   3257 O  O   . ALA A 1 425 ? 52.967 -72.850 -33.183 1.00 30.12  ?  425 ALA A O   1 
ATOM   3258 C  CB  . ALA A 1 425 ? 52.686 -71.969 -30.531 1.00 30.11  ?  425 ALA A CB  1 
ATOM   3259 N  N   . THR A 1 426 ? 54.465 -74.491 -32.655 1.00 30.67  ?  426 THR A N   1 
ATOM   3260 C  CA  . THR A 1 426 ? 54.925 -74.782 -34.007 1.00 33.14  ?  426 THR A CA  1 
ATOM   3261 C  C   . THR A 1 426 ? 53.714 -74.945 -34.926 1.00 35.03  ?  426 THR A C   1 
ATOM   3262 O  O   . THR A 1 426 ? 52.909 -75.852 -34.692 1.00 34.15  ?  426 THR A O   1 
ATOM   3263 C  CB  . THR A 1 426 ? 55.796 -76.040 -33.991 1.00 31.63  ?  426 THR A CB  1 
ATOM   3264 O  OG1 . THR A 1 426 ? 56.840 -75.854 -33.040 1.00 28.31  ?  426 THR A OG1 1 
ATOM   3265 C  CG2 . THR A 1 426 ? 56.422 -76.328 -35.342 1.00 31.01  ?  426 THR A CG2 1 
ATOM   3266 N  N   . PRO A 1 427 ? 53.528 -74.034 -35.925 1.00 36.53  ?  427 PRO A N   1 
ATOM   3267 C  CA  . PRO A 1 427 ? 52.372 -74.054 -36.832 1.00 36.84  ?  427 PRO A CA  1 
ATOM   3268 C  C   . PRO A 1 427 ? 52.414 -75.154 -37.883 1.00 38.32  ?  427 PRO A C   1 
ATOM   3269 O  O   . PRO A 1 427 ? 53.465 -75.739 -38.144 1.00 41.86  ?  427 PRO A O   1 
ATOM   3270 C  CB  . PRO A 1 427 ? 52.452 -72.678 -37.522 1.00 40.24  ?  427 PRO A CB  1 
ATOM   3271 C  CG  . PRO A 1 427 ? 53.934 -72.341 -37.542 1.00 37.33  ?  427 PRO A CG  1 
ATOM   3272 C  CD  . PRO A 1 427 ? 54.421 -72.894 -36.209 1.00 37.33  ?  427 PRO A CD  1 
ATOM   3273 N  N   . ALA A 1 428 ? 51.252 -75.420 -38.479 1.00 40.35  ?  428 ALA A N   1 
ATOM   3274 C  CA  . ALA A 1 428 ? 51.156 -76.324 -39.614 1.00 41.43  ?  428 ALA A CA  1 
ATOM   3275 C  C   . ALA A 1 428 ? 52.001 -75.754 -40.751 1.00 40.92  ?  428 ALA A C   1 
ATOM   3276 O  O   . ALA A 1 428 ? 52.296 -74.555 -40.760 1.00 35.72  ?  428 ALA A O   1 
ATOM   3277 C  CB  . ALA A 1 428 ? 49.705 -76.515 -40.036 1.00 38.58  ?  428 ALA A CB  1 
ATOM   3278 N  N   . ASP A 1 429 ? 52.380 -76.642 -41.675 1.00 38.49  ?  429 ASP A N   1 
ATOM   3279 C  CA  . ASP A 1 429 ? 53.276 -76.323 -42.770 1.00 42.33  ?  429 ASP A CA  1 
ATOM   3280 C  C   . ASP A 1 429 ? 52.670 -75.261 -43.695 1.00 41.66  ?  429 ASP A C   1 
ATOM   3281 O  O   . ASP A 1 429 ? 51.581 -75.444 -44.244 1.00 38.51  ?  429 ASP A O   1 
ATOM   3282 C  CB  . ASP A 1 429 ? 53.616 -77.595 -43.528 1.00 46.49  ?  429 ASP A CB  1 
ATOM   3283 C  CG  . ASP A 1 429 ? 54.671 -77.412 -44.601 1.00 47.92  ?  429 ASP A CG  1 
ATOM   3284 O  OD1 . ASP A 1 429 ? 54.790 -78.324 -45.445 1.00 48.78  ?  429 ASP A OD1 1 
ATOM   3285 O  OD2 . ASP A 1 429 ? 55.335 -76.346 -44.580 1.00 42.61  -1 429 ASP A OD2 1 
ATOM   3286 N  N   . GLY A 1 430 ? 53.399 -74.145 -43.866 1.00 41.75  ?  430 GLY A N   1 
ATOM   3287 C  CA  . GLY A 1 430 ? 52.974 -73.041 -44.718 1.00 40.72  ?  430 GLY A CA  1 
ATOM   3288 C  C   . GLY A 1 430 ? 52.274 -71.905 -43.967 1.00 39.79  ?  430 GLY A C   1 
ATOM   3289 O  O   . GLY A 1 430 ? 52.195 -70.793 -44.503 1.00 41.67  ?  430 GLY A O   1 
ATOM   3290 N  N   . ILE A 1 431 ? 51.786 -72.186 -42.742 1.00 37.95  ?  431 ILE A N   1 
ATOM   3291 C  CA  . ILE A 1 431 ? 51.008 -71.244 -41.936 1.00 36.00  ?  431 ILE A CA  1 
ATOM   3292 C  C   . ILE A 1 431 ? 51.953 -70.325 -41.159 1.00 36.08  ?  431 ILE A C   1 
ATOM   3293 O  O   . ILE A 1 431 ? 52.901 -70.780 -40.517 1.00 34.90  ?  431 ILE A O   1 
ATOM   3294 C  CB  . ILE A 1 431 ? 50.061 -71.959 -40.946 1.00 35.33  ?  431 ILE A CB  1 
ATOM   3295 C  CG1 . ILE A 1 431 ? 49.220 -73.102 -41.571 1.00 33.08  ?  431 ILE A CG1 1 
ATOM   3296 C  CG2 . ILE A 1 431 ? 49.175 -70.938 -40.235 1.00 36.71  ?  431 ILE A CG2 1 
ATOM   3297 C  CD1 . ILE A 1 431 ? 48.263 -72.665 -42.661 1.00 32.05  ?  431 ILE A CD1 1 
ATOM   3298 N  N   . LEU A 1 432 ? 51.647 -69.024 -41.205 1.00 37.49  ?  432 LEU A N   1 
ATOM   3299 C  CA  . LEU A 1 432 ? 52.296 -67.999 -40.398 1.00 37.80  ?  432 LEU A CA  1 
ATOM   3300 C  C   . LEU A 1 432 ? 52.245 -68.335 -38.905 1.00 36.86  ?  432 LEU A C   1 
ATOM   3301 O  O   . LEU A 1 432 ? 51.149 -68.479 -38.367 1.00 41.58  ?  432 LEU A O   1 
ATOM   3302 C  CB  . LEU A 1 432 ? 51.517 -66.708 -40.649 1.00 36.03  ?  432 LEU A CB  1 
ATOM   3303 C  CG  . LEU A 1 432 ? 51.567 -66.136 -42.066 1.00 34.24  ?  432 LEU A CG  1 
ATOM   3304 C  CD1 . LEU A 1 432 ? 50.786 -64.832 -42.125 1.00 33.96  ?  432 LEU A CD1 1 
ATOM   3305 C  CD2 . LEU A 1 432 ? 52.999 -65.907 -42.497 1.00 36.10  ?  432 LEU A CD2 1 
ATOM   3306 N  N   . PRO A 1 433 ? 53.380 -68.380 -38.157 1.00 30.75  ?  433 PRO A N   1 
ATOM   3307 C  CA  . PRO A 1 433 ? 53.315 -68.529 -36.699 1.00 27.00  ?  433 PRO A CA  1 
ATOM   3308 C  C   . PRO A 1 433 ? 52.447 -67.438 -36.053 1.00 24.87  ?  433 PRO A C   1 
ATOM   3309 O  O   . PRO A 1 433 ? 52.172 -66.375 -36.633 1.00 20.96  ?  433 PRO A O   1 
ATOM   3310 C  CB  . PRO A 1 433 ? 54.785 -68.497 -36.203 1.00 25.21  ?  433 PRO A CB  1 
ATOM   3311 C  CG  . PRO A 1 433 ? 55.624 -68.694 -37.456 1.00 26.65  ?  433 PRO A CG  1 
ATOM   3312 C  CD  . PRO A 1 433 ? 54.766 -68.254 -38.642 1.00 28.90  ?  433 PRO A CD  1 
ATOM   3313 N  N   . SER A 1 434 ? 52.008 -67.740 -34.829 1.00 24.66  ?  434 SER A N   1 
ATOM   3314 C  CA  . SER A 1 434 ? 51.187 -66.838 -34.037 1.00 23.86  ?  434 SER A CA  1 
ATOM   3315 C  C   . SER A 1 434 ? 52.074 -65.867 -33.260 1.00 24.18  ?  434 SER A C   1 
ATOM   3316 O  O   . SER A 1 434 ? 52.951 -66.264 -32.488 1.00 21.82  ?  434 SER A O   1 
ATOM   3317 C  CB  . SER A 1 434 ? 50.281 -67.598 -33.129 1.00 21.50  ?  434 SER A CB  1 
ATOM   3318 O  OG  . SER A 1 434 ? 49.386 -66.683 -32.535 1.00 20.02  ?  434 SER A OG  1 
ATOM   3319 N  N   . LEU A 1 435 ? 51.858 -64.584 -33.538 1.00 25.85  ?  435 LEU A N   1 
ATOM   3320 C  CA  . LEU A 1 435 ? 52.614 -63.508 -32.928 1.00 26.41  ?  435 LEU A CA  1 
ATOM   3321 C  C   . LEU A 1 435 ? 51.909 -63.044 -31.650 1.00 29.00  ?  435 LEU A C   1 
ATOM   3322 O  O   . LEU A 1 435 ? 52.549 -62.420 -30.811 1.00 31.33  ?  435 LEU A O   1 
ATOM   3323 C  CB  . LEU A 1 435 ? 52.759 -62.387 -33.964 1.00 25.78  ?  435 LEU A CB  1 
ATOM   3324 C  CG  . LEU A 1 435 ? 53.679 -62.684 -35.153 1.00 24.69  ?  435 LEU A CG  1 
ATOM   3325 C  CD1 . LEU A 1 435 ? 53.803 -61.491 -36.058 1.00 23.64  ?  435 LEU A CD1 1 
ATOM   3326 C  CD2 . LEU A 1 435 ? 55.065 -63.104 -34.681 1.00 26.14  ?  435 LEU A CD2 1 
ATOM   3327 N  N   . VAL A 1 436 ? 50.594 -63.300 -31.525 1.00 27.84  ?  436 VAL A N   1 
ATOM   3328 C  CA  . VAL A 1 436 ? 49.904 -63.180 -30.246 1.00 28.14  ?  436 VAL A CA  1 
ATOM   3329 C  C   . VAL A 1 436 ? 50.624 -64.093 -29.256 1.00 27.90  ?  436 VAL A C   1 
ATOM   3330 O  O   . VAL A 1 436 ? 51.238 -63.618 -28.300 1.00 30.23  ?  436 VAL A O   1 
ATOM   3331 C  CB  . VAL A 1 436 ? 48.381 -63.478 -30.253 1.00 28.58  ?  436 VAL A CB  1 
ATOM   3332 C  CG1 . VAL A 1 436 ? 47.982 -64.574 -31.231 1.00 29.51  ?  436 VAL A CG1 1 
ATOM   3333 C  CG2 . VAL A 1 436 ? 47.810 -63.812 -28.874 1.00 25.88  ?  436 VAL A CG2 1 
ATOM   3334 N  N   . THR A 1 437 ? 50.555 -65.397 -29.520 1.00 24.80  ?  437 THR A N   1 
ATOM   3335 C  CA  . THR A 1 437 ? 51.149 -66.398 -28.658 1.00 25.94  ?  437 THR A CA  1 
ATOM   3336 C  C   . THR A 1 437 ? 52.658 -66.175 -28.577 1.00 28.46  ?  437 THR A C   1 
ATOM   3337 O  O   . THR A 1 437 ? 53.230 -66.076 -27.497 1.00 31.68  ?  437 THR A O   1 
ATOM   3338 C  CB  . THR A 1 437 ? 50.825 -67.791 -29.192 1.00 24.61  ?  437 THR A CB  1 
ATOM   3339 O  OG1 . THR A 1 437 ? 49.429 -67.800 -29.462 1.00 24.00  ?  437 THR A OG1 1 
ATOM   3340 C  CG2 . THR A 1 437 ? 51.086 -68.880 -28.169 1.00 26.67  ?  437 THR A CG2 1 
ATOM   3341 N  N   . GLY A 1 438 ? 53.316 -66.111 -29.730 1.00 31.68  ?  438 GLY A N   1 
ATOM   3342 C  CA  . GLY A 1 438 ? 54.754 -65.908 -29.768 1.00 32.29  ?  438 GLY A CA  1 
ATOM   3343 C  C   . GLY A 1 438 ? 55.169 -64.783 -28.821 1.00 32.43  ?  438 GLY A C   1 
ATOM   3344 O  O   . GLY A 1 438 ? 56.080 -64.970 -28.013 1.00 31.81  ?  438 GLY A O   1 
ATOM   3345 N  N   . SER A 1 439 ? 54.467 -63.637 -28.919 1.00 29.45  ?  439 SER A N   1 
ATOM   3346 C  CA  . SER A 1 439 ? 54.820 -62.428 -28.185 1.00 27.89  ?  439 SER A CA  1 
ATOM   3347 C  C   . SER A 1 439 ? 54.367 -62.493 -26.734 1.00 26.29  ?  439 SER A C   1 
ATOM   3348 O  O   . SER A 1 439 ? 54.780 -61.673 -25.927 1.00 29.89  ?  439 SER A O   1 
ATOM   3349 C  CB  . SER A 1 439 ? 54.238 -61.189 -28.818 1.00 27.23  ?  439 SER A CB  1 
ATOM   3350 O  OG  . SER A 1 439 ? 54.695 -61.046 -30.152 1.00 31.32  ?  439 SER A OG  1 
ATOM   3351 N  N   . ASN A 1 440 ? 53.430 -63.383 -26.428 1.00 26.12  ?  440 ASN A N   1 
ATOM   3352 C  CA  . ASN A 1 440 ? 52.964 -63.572 -25.062 1.00 25.22  ?  440 ASN A CA  1 
ATOM   3353 C  C   . ASN A 1 440 ? 53.883 -64.492 -24.276 1.00 23.79  ?  440 ASN A C   1 
ATOM   3354 O  O   . ASN A 1 440 ? 53.732 -64.546 -23.068 1.00 23.51  ?  440 ASN A O   1 
ATOM   3355 C  CB  . ASN A 1 440 ? 51.584 -64.216 -25.009 1.00 24.41  ?  440 ASN A CB  1 
ATOM   3356 C  CG  . ASN A 1 440 ? 50.505 -63.248 -25.400 1.00 24.38  ?  440 ASN A CG  1 
ATOM   3357 O  OD1 . ASN A 1 440 ? 50.720 -62.030 -25.388 1.00 23.78  ?  440 ASN A OD1 1 
ATOM   3358 N  ND2 . ASN A 1 440 ? 49.344 -63.780 -25.742 1.00 26.36  ?  440 ASN A ND2 1 
ATOM   3359 N  N   . ILE A 1 441 ? 54.756 -65.233 -24.979 1.00 25.30  ?  441 ILE A N   1 
ATOM   3360 C  CA  . ILE A 1 441 ? 55.597 -66.292 -24.428 1.00 26.24  ?  441 ILE A CA  1 
ATOM   3361 C  C   . ILE A 1 441 ? 57.040 -65.789 -24.316 1.00 28.41  ?  441 ILE A C   1 
ATOM   3362 O  O   . ILE A 1 441 ? 57.709 -66.081 -23.331 1.00 40.34  ?  441 ILE A O   1 
ATOM   3363 C  CB  . ILE A 1 441 ? 55.490 -67.578 -25.295 1.00 24.17  ?  441 ILE A CB  1 
ATOM   3364 C  CG1 . ILE A 1 441 ? 54.074 -68.229 -25.160 1.00 25.91  ?  441 ILE A CG1 1 
ATOM   3365 C  CG2 . ILE A 1 441 ? 56.601 -68.588 -24.990 1.00 21.52  ?  441 ILE A CG2 1 
ATOM   3366 C  CD1 . ILE A 1 441 ? 53.901 -69.609 -25.791 1.00 24.85  ?  441 ILE A CD1 1 
ATOM   3367 N  N   . ALA A 1 442 ? 57.521 -65.048 -25.322 1.00 24.46  ?  442 ALA A N   1 
ATOM   3368 C  CA  . ALA A 1 442 ? 58.947 -64.857 -25.561 1.00 23.59  ?  442 ALA A CA  1 
ATOM   3369 C  C   . ALA A 1 442 ? 59.643 -64.113 -24.427 1.00 23.06  ?  442 ALA A C   1 
ATOM   3370 O  O   . ALA A 1 442 ? 60.817 -64.350 -24.174 1.00 22.90  ?  442 ALA A O   1 
ATOM   3371 C  CB  . ALA A 1 442 ? 59.157 -64.083 -26.840 1.00 25.05  ?  442 ALA A CB  1 
ATOM   3372 N  N   . GLY A 1 443 ? 58.958 -63.143 -23.825 1.00 23.61  ?  443 GLY A N   1 
ATOM   3373 C  CA  . GLY A 1 443 ? 59.508 -62.411 -22.702 1.00 23.97  ?  443 GLY A CA  1 
ATOM   3374 C  C   . GLY A 1 443 ? 59.862 -63.393 -21.596 1.00 25.20  ?  443 GLY A C   1 
ATOM   3375 O  O   . GLY A 1 443 ? 60.980 -63.392 -21.094 1.00 31.70  ?  443 GLY A O   1 
ATOM   3376 N  N   . PHE A 1 444 ? 58.919 -64.275 -21.268 1.00 23.83  ?  444 PHE A N   1 
ATOM   3377 C  CA  . PHE A 1 444 ? 59.131 -65.217 -20.184 1.00 23.82  ?  444 PHE A CA  1 
ATOM   3378 C  C   . PHE A 1 444 ? 60.386 -66.043 -20.438 1.00 23.41  ?  444 PHE A C   1 
ATOM   3379 O  O   . PHE A 1 444 ? 61.218 -66.199 -19.550 1.00 26.44  ?  444 PHE A O   1 
ATOM   3380 C  CB  . PHE A 1 444 ? 57.963 -66.186 -20.006 1.00 23.21  ?  444 PHE A CB  1 
ATOM   3381 C  CG  . PHE A 1 444 ? 58.144 -67.146 -18.841 1.00 21.51  ?  444 PHE A CG  1 
ATOM   3382 C  CD1 . PHE A 1 444 ? 57.913 -66.731 -17.528 1.00 19.94  ?  444 PHE A CD1 1 
ATOM   3383 C  CD2 . PHE A 1 444 ? 58.524 -68.462 -19.063 1.00 20.76  ?  444 PHE A CD2 1 
ATOM   3384 C  CE1 . PHE A 1 444 ? 58.026 -67.625 -16.470 1.00 19.18  ?  444 PHE A CE1 1 
ATOM   3385 C  CE2 . PHE A 1 444 ? 58.669 -69.346 -17.996 1.00 20.47  ?  444 PHE A CE2 1 
ATOM   3386 C  CZ  . PHE A 1 444 ? 58.401 -68.930 -16.704 1.00 18.91  ?  444 PHE A CZ  1 
ATOM   3387 N  N   . THR A 1 445 ? 60.494 -66.586 -21.647 1.00 21.81  ?  445 THR A N   1 
ATOM   3388 C  CA  . THR A 1 445 ? 61.512 -67.580 -21.944 1.00 22.50  ?  445 THR A CA  1 
ATOM   3389 C  C   . THR A 1 445 ? 62.901 -66.947 -21.872 1.00 23.91  ?  445 THR A C   1 
ATOM   3390 O  O   . THR A 1 445 ? 63.848 -67.557 -21.366 1.00 22.61  ?  445 THR A O   1 
ATOM   3391 C  CB  . THR A 1 445 ? 61.197 -68.177 -23.311 1.00 21.83  ?  445 THR A CB  1 
ATOM   3392 O  OG1 . THR A 1 445 ? 61.228 -67.111 -24.255 1.00 19.68  ?  445 THR A OG1 1 
ATOM   3393 C  CG2 . THR A 1 445 ? 59.828 -68.831 -23.316 1.00 22.21  ?  445 THR A CG2 1 
ATOM   3394 N  N   . LYS A 1 446 ? 62.990 -65.698 -22.347 1.00 24.58  ?  446 LYS A N   1 
ATOM   3395 C  CA  . LYS A 1 446 ? 64.246 -64.976 -22.346 1.00 25.19  ?  446 LYS A CA  1 
ATOM   3396 C  C   . LYS A 1 446 ? 64.637 -64.738 -20.895 1.00 25.57  ?  446 LYS A C   1 
ATOM   3397 O  O   . LYS A 1 446 ? 65.795 -64.916 -20.535 1.00 26.47  ?  446 LYS A O   1 
ATOM   3398 C  CB  . LYS A 1 446 ? 64.136 -63.696 -23.192 1.00 25.08  ?  446 LYS A CB  1 
ATOM   3399 C  CG  . LYS A 1 446 ? 65.417 -62.855 -23.358 1.00 24.27  ?  446 LYS A CG  1 
ATOM   3400 C  CD  . LYS A 1 446 ? 65.226 -61.526 -24.082 1.00 24.99  ?  446 LYS A CD  1 
ATOM   3401 C  CE  . LYS A 1 446 ? 64.600 -61.696 -25.439 1.00 27.68  ?  446 LYS A CE  1 
ATOM   3402 N  NZ  . LYS A 1 446 ? 65.213 -62.772 -26.235 1.00 28.61  1  446 LYS A NZ  1 
ATOM   3403 N  N   . VAL A 1 447 ? 63.646 -64.363 -20.080 1.00 27.03  ?  447 VAL A N   1 
ATOM   3404 C  CA  . VAL A 1 447 ? 63.887 -63.943 -18.710 1.00 27.60  ?  447 VAL A CA  1 
ATOM   3405 C  C   . VAL A 1 447 ? 64.167 -65.163 -17.845 1.00 29.66  ?  447 VAL A C   1 
ATOM   3406 O  O   . VAL A 1 447 ? 65.083 -65.168 -17.028 1.00 34.02  ?  447 VAL A O   1 
ATOM   3407 C  CB  . VAL A 1 447 ? 62.694 -63.149 -18.148 1.00 26.17  ?  447 VAL A CB  1 
ATOM   3408 C  CG1 . VAL A 1 447 ? 62.836 -62.932 -16.643 1.00 27.25  ?  447 VAL A CG1 1 
ATOM   3409 C  CG2 . VAL A 1 447 ? 62.532 -61.821 -18.877 1.00 24.57  ?  447 VAL A CG2 1 
ATOM   3410 N  N   . ALA A 1 448 ? 63.325 -66.179 -18.003 1.00 30.00  ?  448 ALA A N   1 
ATOM   3411 C  CA  . ALA A 1 448 ? 63.434 -67.391 -17.215 1.00 29.80  ?  448 ALA A CA  1 
ATOM   3412 C  C   . ALA A 1 448 ? 64.788 -68.045 -17.466 1.00 27.78  ?  448 ALA A C   1 
ATOM   3413 O  O   . ALA A 1 448 ? 65.347 -68.678 -16.570 1.00 25.75  ?  448 ALA A O   1 
ATOM   3414 C  CB  . ALA A 1 448 ? 62.285 -68.329 -17.563 1.00 32.18  ?  448 ALA A CB  1 
ATOM   3415 N  N   . ALA A 1 449 ? 65.278 -67.941 -18.708 1.00 26.81  ?  449 ALA A N   1 
ATOM   3416 C  CA  . ALA A 1 449 ? 66.506 -68.630 -19.068 1.00 27.76  ?  449 ALA A CA  1 
ATOM   3417 C  C   . ALA A 1 449 ? 67.678 -67.929 -18.388 1.00 28.26  ?  449 ALA A C   1 
ATOM   3418 O  O   . ALA A 1 449 ? 68.530 -68.585 -17.792 1.00 33.27  ?  449 ALA A O   1 
ATOM   3419 C  CB  . ALA A 1 449 ? 66.660 -68.688 -20.559 1.00 26.92  ?  449 ALA A CB  1 
ATOM   3420 N  N   . ALA A 1 450 ? 67.659 -66.597 -18.465 1.00 24.08  ?  450 ALA A N   1 
ATOM   3421 C  CA  . ALA A 1 450 ? 68.661 -65.735 -17.881 1.00 24.08  ?  450 ALA A CA  1 
ATOM   3422 C  C   . ALA A 1 450 ? 68.712 -65.898 -16.364 1.00 25.47  ?  450 ALA A C   1 
ATOM   3423 O  O   . ALA A 1 450 ? 69.776 -65.780 -15.759 1.00 30.44  ?  450 ALA A O   1 
ATOM   3424 C  CB  . ALA A 1 450 ? 68.341 -64.302 -18.264 1.00 24.18  ?  450 ALA A CB  1 
ATOM   3425 N  N   . MET A 1 451 ? 67.551 -66.093 -15.735 1.00 24.78  ?  451 MET A N   1 
ATOM   3426 C  CA  . MET A 1 451 ? 67.491 -66.281 -14.295 1.00 25.17  ?  451 MET A CA  1 
ATOM   3427 C  C   . MET A 1 451 ? 68.092 -67.640 -13.947 1.00 23.17  ?  451 MET A C   1 
ATOM   3428 O  O   . MET A 1 451 ? 68.715 -67.772 -12.905 1.00 23.72  ?  451 MET A O   1 
ATOM   3429 C  CB  . MET A 1 451 ? 66.056 -66.240 -13.752 1.00 27.23  ?  451 MET A CB  1 
ATOM   3430 C  CG  . MET A 1 451 ? 65.399 -64.881 -13.739 1.00 28.49  ?  451 MET A CG  1 
ATOM   3431 S  SD  . MET A 1 451 ? 63.607 -64.964 -13.495 1.00 31.50  ?  451 MET A SD  1 
ATOM   3432 C  CE  . MET A 1 451 ? 63.568 -65.390 -11.752 1.00 28.57  ?  451 MET A CE  1 
ATOM   3433 N  N   . LYS A 1 452 ? 67.918 -68.641 -14.817 1.00 23.16  ?  452 LYS A N   1 
ATOM   3434 C  CA  . LYS A 1 452 ? 68.602 -69.914 -14.634 1.00 24.86  ?  452 LYS A CA  1 
ATOM   3435 C  C   . LYS A 1 452 ? 70.100 -69.688 -14.778 1.00 23.00  ?  452 LYS A C   1 
ATOM   3436 O  O   . LYS A 1 452 ? 70.850 -70.054 -13.886 1.00 23.21  ?  452 LYS A O   1 
ATOM   3437 C  CB  . LYS A 1 452 ? 68.178 -71.083 -15.533 1.00 25.55  ?  452 LYS A CB  1 
ATOM   3438 C  CG  . LYS A 1 452 ? 68.727 -72.425 -15.022 1.00 27.18  ?  452 LYS A CG  1 
ATOM   3439 C  CD  . LYS A 1 452 ? 67.924 -73.712 -15.262 1.00 27.18  ?  452 LYS A CD  1 
ATOM   3440 C  CE  . LYS A 1 452 ? 68.070 -74.348 -16.619 1.00 26.42  ?  452 LYS A CE  1 
ATOM   3441 N  NZ  . LYS A 1 452 ? 67.169 -75.497 -16.836 1.00 25.99  1  452 LYS A NZ  1 
ATOM   3442 N  N   . ASP A 1 453 ? 70.502 -69.037 -15.875 1.00 23.76  ?  453 ASP A N   1 
ATOM   3443 C  CA  . ASP A 1 453 ? 71.903 -68.761 -16.168 1.00 24.18  ?  453 ASP A CA  1 
ATOM   3444 C  C   . ASP A 1 453 ? 72.563 -68.166 -14.924 1.00 24.81  ?  453 ASP A C   1 
ATOM   3445 O  O   . ASP A 1 453 ? 73.595 -68.671 -14.479 1.00 27.82  ?  453 ASP A O   1 
ATOM   3446 C  CB  . ASP A 1 453 ? 72.058 -67.952 -17.453 1.00 25.19  ?  453 ASP A CB  1 
ATOM   3447 C  CG  . ASP A 1 453 ? 71.990 -68.696 -18.793 1.00 26.44  ?  453 ASP A CG  1 
ATOM   3448 O  OD1 . ASP A 1 453 ? 71.596 -69.884 -18.820 1.00 26.15  ?  453 ASP A OD1 1 
ATOM   3449 O  OD2 . ASP A 1 453 ? 72.353 -68.087 -19.834 1.00 27.41  -1 453 ASP A OD2 1 
ATOM   3450 N  N   . GLN A 1 454 ? 71.905 -67.159 -14.329 1.00 24.64  ?  454 GLN A N   1 
ATOM   3451 C  CA  . GLN A 1 454 ? 72.373 -66.436 -13.150 1.00 23.12  ?  454 GLN A CA  1 
ATOM   3452 C  C   . GLN A 1 454 ? 72.050 -67.098 -11.804 1.00 26.06  ?  454 GLN A C   1 
ATOM   3453 O  O   . GLN A 1 454 ? 72.471 -66.580 -10.778 1.00 28.01  ?  454 GLN A O   1 
ATOM   3454 C  CB  . GLN A 1 454 ? 71.691 -65.076 -13.200 1.00 20.69  ?  454 GLN A CB  1 
ATOM   3455 C  CG  . GLN A 1 454 ? 72.137 -64.284 -14.421 1.00 19.87  ?  454 GLN A CG  1 
ATOM   3456 C  CD  . GLN A 1 454 ? 71.482 -62.934 -14.535 1.00 17.79  ?  454 GLN A CD  1 
ATOM   3457 O  OE1 . GLN A 1 454 ? 71.189 -62.274 -13.526 1.00 16.28  ?  454 GLN A OE1 1 
ATOM   3458 N  NE2 . GLN A 1 454 ? 71.205 -62.556 -15.776 1.00 16.97  ?  454 GLN A NE2 1 
ATOM   3459 N  N   . GLY A 1 455 ? 71.275 -68.196 -11.778 1.00 27.36  ?  455 GLY A N   1 
ATOM   3460 C  CA  . GLY A 1 455 ? 71.082 -68.991 -10.569 1.00 28.24  ?  455 GLY A CA  1 
ATOM   3461 C  C   . GLY A 1 455 ? 70.006 -68.476 -9.600  1.00 27.49  ?  455 GLY A C   1 
ATOM   3462 O  O   . GLY A 1 455 ? 70.081 -68.775 -8.407  1.00 24.90  ?  455 GLY A O   1 
ATOM   3463 N  N   . ASP A 1 456 ? 68.993 -67.754 -10.107 1.00 28.22  ?  456 ASP A N   1 
ATOM   3464 C  CA  . ASP A 1 456 ? 67.822 -67.368 -9.324  1.00 30.27  ?  456 ASP A CA  1 
ATOM   3465 C  C   . ASP A 1 456 ? 66.839 -68.530 -9.196  1.00 29.05  ?  456 ASP A C   1 
ATOM   3466 O  O   . ASP A 1 456 ? 65.940 -68.492 -8.379  1.00 33.03  ?  456 ASP A O   1 
ATOM   3467 C  CB  . ASP A 1 456 ? 67.099 -66.183 -9.939  1.00 31.99  ?  456 ASP A CB  1 
ATOM   3468 C  CG  . ASP A 1 456 ? 67.943 -64.928 -10.062 1.00 34.70  ?  456 ASP A CG  1 
ATOM   3469 O  OD1 . ASP A 1 456 ? 69.015 -64.888 -9.414  1.00 37.75  ?  456 ASP A OD1 1 
ATOM   3470 O  OD2 . ASP A 1 456 ? 67.551 -64.032 -10.845 1.00 34.02  -1 456 ASP A OD2 1 
ATOM   3471 N  N   . TRP A 1 457 ? 66.979 -69.536 -10.055 1.00 29.85  ?  457 TRP A N   1 
ATOM   3472 C  CA  . TRP A 1 457 ? 66.353 -70.830 -9.860  1.00 29.12  ?  457 TRP A CA  1 
ATOM   3473 C  C   . TRP A 1 457 ? 67.272 -71.902 -10.450 1.00 29.35  ?  457 TRP A C   1 
ATOM   3474 O  O   . TRP A 1 457 ? 68.159 -71.622 -11.253 1.00 27.46  ?  457 TRP A O   1 
ATOM   3475 C  CB  . TRP A 1 457 ? 64.943 -70.834 -10.467 1.00 29.11  ?  457 TRP A CB  1 
ATOM   3476 C  CG  . TRP A 1 457 ? 64.910 -70.735 -11.966 1.00 29.41  ?  457 TRP A CG  1 
ATOM   3477 C  CD1 . TRP A 1 457 ? 65.023 -69.617 -12.749 1.00 28.96  ?  457 TRP A CD1 1 
ATOM   3478 C  CD2 . TRP A 1 457 ? 64.767 -71.849 -12.868 1.00 30.91  ?  457 TRP A CD2 1 
ATOM   3479 N  NE1 . TRP A 1 457 ? 64.945 -69.953 -14.075 1.00 28.17  ?  457 TRP A NE1 1 
ATOM   3480 C  CE2 . TRP A 1 457 ? 64.802 -71.315 -14.176 1.00 29.78  ?  457 TRP A CE2 1 
ATOM   3481 C  CE3 . TRP A 1 457 ? 64.620 -73.232 -12.692 1.00 32.20  ?  457 TRP A CE3 1 
ATOM   3482 C  CZ2 . TRP A 1 457 ? 64.706 -72.131 -15.295 1.00 31.20  ?  457 TRP A CZ2 1 
ATOM   3483 C  CZ3 . TRP A 1 457 ? 64.526 -74.034 -13.806 1.00 32.19  ?  457 TRP A CZ3 1 
ATOM   3484 C  CH2 . TRP A 1 457 ? 64.568 -73.486 -15.087 1.00 31.65  ?  457 TRP A CH2 1 
ATOM   3485 N  N   . TRP A 1 458 ? 67.103 -73.133 -9.975  1.00 31.22  ?  458 TRP A N   1 
ATOM   3486 C  CA  . TRP A 1 458 ? 67.878 -74.276 -10.430 1.00 28.75  ?  458 TRP A CA  1 
ATOM   3487 C  C   . TRP A 1 458 ? 66.937 -75.476 -10.438 1.00 28.02  ?  458 TRP A C   1 
ATOM   3488 O  O   . TRP A 1 458 ? 65.953 -75.403 -9.686  1.00 24.57  ?  458 TRP A O   1 
ATOM   3489 C  CB  . TRP A 1 458 ? 69.089 -74.513 -9.513  1.00 27.76  ?  458 TRP A CB  1 
ATOM   3490 C  CG  . TRP A 1 458 ? 68.714 -74.713 -8.066  1.00 26.43  ?  458 TRP A CG  1 
ATOM   3491 C  CD1 . TRP A 1 458 ? 68.398 -75.889 -7.456  1.00 26.41  ?  458 TRP A CD1 1 
ATOM   3492 C  CD2 . TRP A 1 458 ? 68.540 -73.684 -7.063  1.00 25.73  ?  458 TRP A CD2 1 
ATOM   3493 N  NE1 . TRP A 1 458 ? 68.081 -75.669 -6.140  1.00 27.41  ?  458 TRP A NE1 1 
ATOM   3494 C  CE2 . TRP A 1 458 ? 68.152 -74.330 -5.873  1.00 25.07  ?  458 TRP A CE2 1 
ATOM   3495 C  CE3 . TRP A 1 458 ? 68.672 -72.289 -7.053  1.00 25.41  ?  458 TRP A CE3 1 
ATOM   3496 C  CZ2 . TRP A 1 458 ? 67.906 -73.629 -4.699  1.00 23.78  ?  458 TRP A CZ2 1 
ATOM   3497 C  CZ3 . TRP A 1 458 ? 68.417 -71.596 -5.891  1.00 22.73  ?  458 TRP A CZ3 1 
ATOM   3498 C  CH2 . TRP A 1 458 ? 68.040 -72.260 -4.736  1.00 22.64  ?  458 TRP A CH2 1 
ATOM   3499 O  OXT . TRP A 1 458 ? 67.203 -76.422 -11.199 1.00 34.74  -1 458 TRP A OXT 1 
ATOM   3500 N  N   . ASN B 1 3   ? 40.482 -47.333 -2.907  1.00 45.85  ?  3   ASN B N   1 
ATOM   3501 C  CA  . ASN B 1 3   ? 41.871 -47.472 -3.434  1.00 48.10  ?  3   ASN B CA  1 
ATOM   3502 C  C   . ASN B 1 3   ? 42.675 -48.374 -2.494  1.00 49.67  ?  3   ASN B C   1 
ATOM   3503 O  O   . ASN B 1 3   ? 43.063 -49.469 -2.883  1.00 53.59  ?  3   ASN B O   1 
ATOM   3504 C  CB  . ASN B 1 3   ? 42.497 -46.105 -3.736  1.00 50.75  ?  3   ASN B CB  1 
ATOM   3505 C  CG  . ASN B 1 3   ? 43.316 -45.485 -2.617  1.00 54.13  ?  3   ASN B CG  1 
ATOM   3506 O  OD1 . ASN B 1 3   ? 42.863 -44.559 -1.929  1.00 49.97  ?  3   ASN B OD1 1 
ATOM   3507 N  ND2 . ASN B 1 3   ? 44.546 -45.947 -2.436  1.00 57.57  ?  3   ASN B ND2 1 
ATOM   3508 N  N   . LEU B 1 4   ? 42.871 -47.932 -1.243  1.00 50.44  ?  4   LEU B N   1 
ATOM   3509 C  CA  . LEU B 1 4   ? 43.766 -48.587 -0.305  1.00 50.96  ?  4   LEU B CA  1 
ATOM   3510 C  C   . LEU B 1 4   ? 43.230 -49.987 0.007   1.00 46.78  ?  4   LEU B C   1 
ATOM   3511 O  O   . LEU B 1 4   ? 42.022 -50.171 0.131   1.00 48.21  ?  4   LEU B O   1 
ATOM   3512 C  CB  . LEU B 1 4   ? 43.943 -47.698 0.936   1.00 58.67  ?  4   LEU B CB  1 
ATOM   3513 C  CG  . LEU B 1 4   ? 42.736 -47.470 1.864   1.00 64.64  ?  4   LEU B CG  1 
ATOM   3514 C  CD1 . LEU B 1 4   ? 42.696 -48.469 3.016   1.00 66.78  ?  4   LEU B CD1 1 
ATOM   3515 C  CD2 . LEU B 1 4   ? 42.681 -46.053 2.444   1.00 62.87  ?  4   LEU B CD2 1 
ATOM   3516 N  N   . PRO B 1 5   ? 44.094 -51.028 0.122   1.00 45.21  ?  5   PRO B N   1 
ATOM   3517 C  CA  . PRO B 1 5   ? 43.630 -52.383 0.453   1.00 42.71  ?  5   PRO B CA  1 
ATOM   3518 C  C   . PRO B 1 5   ? 42.994 -52.482 1.840   1.00 38.93  ?  5   PRO B C   1 
ATOM   3519 O  O   . PRO B 1 5   ? 43.053 -51.537 2.628   1.00 33.59  ?  5   PRO B O   1 
ATOM   3520 C  CB  . PRO B 1 5   ? 44.924 -53.223 0.371   1.00 43.09  ?  5   PRO B CB  1 
ATOM   3521 C  CG  . PRO B 1 5   ? 46.008 -52.224 0.744   1.00 44.03  ?  5   PRO B CG  1 
ATOM   3522 C  CD  . PRO B 1 5   ? 45.563 -50.954 0.010   1.00 44.63  ?  5   PRO B CD  1 
ATOM   3523 N  N   . VAL B 1 6   ? 42.408 -53.653 2.117   1.00 39.99  ?  6   VAL B N   1 
ATOM   3524 C  CA  . VAL B 1 6   ? 41.793 -53.965 3.399   1.00 41.42  ?  6   VAL B CA  1 
ATOM   3525 C  C   . VAL B 1 6   ? 42.818 -54.744 4.225   1.00 45.02  ?  6   VAL B C   1 
ATOM   3526 O  O   . VAL B 1 6   ? 43.399 -55.738 3.760   1.00 41.24  ?  6   VAL B O   1 
ATOM   3527 C  CB  . VAL B 1 6   ? 40.476 -54.732 3.133   1.00 42.13  ?  6   VAL B CB  1 
ATOM   3528 C  CG1 . VAL B 1 6   ? 40.052 -55.653 4.273   1.00 42.47  ?  6   VAL B CG1 1 
ATOM   3529 C  CG2 . VAL B 1 6   ? 39.338 -53.785 2.760   1.00 42.10  ?  6   VAL B CG2 1 
ATOM   3530 N  N   . GLU B 1 7   ? 43.079 -54.248 5.441   1.00 45.53  ?  7   GLU B N   1 
ATOM   3531 C  CA  . GLU B 1 7   ? 44.070 -54.852 6.325   1.00 43.80  ?  7   GLU B CA  1 
ATOM   3532 C  C   . GLU B 1 7   ? 43.478 -54.969 7.732   1.00 41.89  ?  7   GLU B C   1 
ATOM   3533 O  O   . GLU B 1 7   ? 43.823 -54.218 8.638   1.00 40.66  ?  7   GLU B O   1 
ATOM   3534 C  CB  . GLU B 1 7   ? 45.340 -54.006 6.230   1.00 42.16  ?  7   GLU B CB  1 
ATOM   3535 C  CG  . GLU B 1 7   ? 46.082 -54.188 4.910   1.00 40.15  ?  7   GLU B CG  1 
ATOM   3536 C  CD  . GLU B 1 7   ? 47.260 -53.252 4.696   1.00 39.00  ?  7   GLU B CD  1 
ATOM   3537 O  OE1 . GLU B 1 7   ? 47.307 -52.143 5.290   1.00 36.56  ?  7   GLU B OE1 1 
ATOM   3538 O  OE2 . GLU B 1 7   ? 48.151 -53.667 3.920   1.00 35.52  -1 7   GLU B OE2 1 
ATOM   3539 N  N   . PRO B 1 8   ? 42.534 -55.904 7.960   1.00 43.89  ?  8   PRO B N   1 
ATOM   3540 C  CA  . PRO B 1 8   ? 41.698 -55.875 9.167   1.00 42.06  ?  8   PRO B CA  1 
ATOM   3541 C  C   . PRO B 1 8   ? 42.396 -55.760 10.525  1.00 35.78  ?  8   PRO B C   1 
ATOM   3542 O  O   . PRO B 1 8   ? 41.956 -54.998 11.371  1.00 30.06  ?  8   PRO B O   1 
ATOM   3543 C  CB  . PRO B 1 8   ? 40.868 -57.175 9.040   1.00 42.77  ?  8   PRO B CB  1 
ATOM   3544 C  CG  . PRO B 1 8   ? 41.631 -58.027 8.053   1.00 44.70  ?  8   PRO B CG  1 
ATOM   3545 C  CD  . PRO B 1 8   ? 42.208 -57.024 7.065   1.00 45.18  ?  8   PRO B CD  1 
ATOM   3546 N  N   . GLU B 1 9   ? 43.492 -56.494 10.724  1.00 38.08  ?  9   GLU B N   1 
ATOM   3547 C  CA  . GLU B 1 9   ? 44.149 -56.558 12.023  1.00 38.05  ?  9   GLU B CA  1 
ATOM   3548 C  C   . GLU B 1 9   ? 44.854 -55.234 12.305  1.00 37.53  ?  9   GLU B C   1 
ATOM   3549 O  O   . GLU B 1 9   ? 44.959 -54.842 13.458  1.00 40.70  ?  9   GLU B O   1 
ATOM   3550 C  CB  . GLU B 1 9   ? 45.169 -57.688 12.192  1.00 41.41  ?  9   GLU B CB  1 
ATOM   3551 C  CG  . GLU B 1 9   ? 44.927 -58.901 11.298  1.00 46.40  ?  9   GLU B CG  1 
ATOM   3552 C  CD  . GLU B 1 9   ? 45.074 -58.536 9.824   1.00 53.17  ?  9   GLU B CD  1 
ATOM   3553 O  OE1 . GLU B 1 9   ? 45.433 -57.351 9.554   1.00 49.83  ?  9   GLU B OE1 1 
ATOM   3554 O  OE2 . GLU B 1 9   ? 44.800 -59.390 8.948   1.00 54.19  -1 9   GLU B OE2 1 
ATOM   3555 N  N   . PHE B 1 10  ? 45.353 -54.553 11.264  1.00 38.79  ?  10  PHE B N   1 
ATOM   3556 C  CA  . PHE B 1 10  ? 45.990 -53.250 11.439  1.00 35.35  ?  10  PHE B CA  1 
ATOM   3557 C  C   . PHE B 1 10  ? 44.916 -52.208 11.735  1.00 38.63  ?  10  PHE B C   1 
ATOM   3558 O  O   . PHE B 1 10  ? 45.039 -51.467 12.708  1.00 44.66  ?  10  PHE B O   1 
ATOM   3559 C  CB  . PHE B 1 10  ? 46.846 -52.828 10.233  1.00 33.05  ?  10  PHE B CB  1 
ATOM   3560 C  CG  . PHE B 1 10  ? 47.239 -51.355 10.258  1.00 31.08  ?  10  PHE B CG  1 
ATOM   3561 C  CD1 . PHE B 1 10  ? 48.209 -50.895 11.135  1.00 29.42  ?  10  PHE B CD1 1 
ATOM   3562 C  CD2 . PHE B 1 10  ? 46.623 -50.429 9.420   1.00 29.16  ?  10  PHE B CD2 1 
ATOM   3563 C  CE1 . PHE B 1 10  ? 48.555 -49.556 11.164  1.00 27.86  ?  10  PHE B CE1 1 
ATOM   3564 C  CE2 . PHE B 1 10  ? 46.967 -49.095 9.464   1.00 27.36  ?  10  PHE B CE2 1 
ATOM   3565 C  CZ  . PHE B 1 10  ? 47.936 -48.666 10.329  1.00 27.98  ?  10  PHE B CZ  1 
ATOM   3566 N  N   . GLU B 1 11  ? 43.888 -52.163 10.872  1.00 39.82  ?  11  GLU B N   1 
ATOM   3567 C  CA  . GLU B 1 11  ? 42.762 -51.245 10.968  1.00 44.92  ?  11  GLU B CA  1 
ATOM   3568 C  C   . GLU B 1 11  ? 42.038 -51.371 12.310  1.00 48.95  ?  11  GLU B C   1 
ATOM   3569 O  O   . GLU B 1 11  ? 41.601 -50.371 12.882  1.00 48.05  ?  11  GLU B O   1 
ATOM   3570 C  CB  . GLU B 1 11  ? 41.820 -51.528 9.796   1.00 48.67  ?  11  GLU B CB  1 
ATOM   3571 C  CG  . GLU B 1 11  ? 42.391 -51.100 8.443   1.00 52.29  ?  11  GLU B CG  1 
ATOM   3572 C  CD  . GLU B 1 11  ? 41.488 -51.385 7.255   1.00 51.41  ?  11  GLU B CD  1 
ATOM   3573 O  OE1 . GLU B 1 11  ? 41.878 -51.136 6.088   1.00 50.35  ?  11  GLU B OE1 1 
ATOM   3574 O  OE2 . GLU B 1 11  ? 40.373 -51.872 7.521   1.00 46.65  -1 11  GLU B OE2 1 
ATOM   3575 N  N   . GLN B 1 12  ? 41.899 -52.614 12.787  1.00 55.95  ?  12  GLN B N   1 
ATOM   3576 C  CA  . GLN B 1 12  ? 41.352 -52.916 14.102  1.00 60.03  ?  12  GLN B CA  1 
ATOM   3577 C  C   . GLN B 1 12  ? 42.048 -52.088 15.181  1.00 59.75  ?  12  GLN B C   1 
ATOM   3578 O  O   . GLN B 1 12  ? 41.398 -51.553 16.079  1.00 64.80  ?  12  GLN B O   1 
ATOM   3579 C  CB  . GLN B 1 12  ? 41.541 -54.401 14.429  1.00 62.75  ?  12  GLN B CB  1 
ATOM   3580 C  CG  . GLN B 1 12  ? 40.372 -55.297 14.026  1.00 68.63  ?  12  GLN B CG  1 
ATOM   3581 C  CD  . GLN B 1 12  ? 39.140 -55.132 14.892  1.00 68.29  ?  12  GLN B CD  1 
ATOM   3582 O  OE1 . GLN B 1 12  ? 38.036 -54.887 14.393  1.00 69.95  ?  12  GLN B OE1 1 
ATOM   3583 N  NE2 . GLN B 1 12  ? 39.305 -55.295 16.198  1.00 65.71  ?  12  GLN B NE2 1 
ATOM   3584 N  N   . ALA B 1 13  ? 43.380 -52.026 15.090  1.00 54.15  ?  13  ALA B N   1 
ATOM   3585 C  CA  . ALA B 1 13  ? 44.224 -51.480 16.139  1.00 49.83  ?  13  ALA B CA  1 
ATOM   3586 C  C   . ALA B 1 13  ? 44.330 -49.961 16.000  1.00 50.03  ?  13  ALA B C   1 
ATOM   3587 O  O   . ALA B 1 13  ? 44.577 -49.269 16.987  1.00 52.41  ?  13  ALA B O   1 
ATOM   3588 C  CB  . ALA B 1 13  ? 45.576 -52.148 16.075  1.00 45.40  ?  13  ALA B CB  1 
ATOM   3589 N  N   . TYR B 1 14  ? 44.169 -49.456 14.768  1.00 45.79  ?  14  TYR B N   1 
ATOM   3590 C  CA  . TYR B 1 14  ? 44.186 -48.024 14.518  1.00 41.57  ?  14  TYR B CA  1 
ATOM   3591 C  C   . TYR B 1 14  ? 42.977 -47.433 15.233  1.00 39.93  ?  14  TYR B C   1 
ATOM   3592 O  O   . TYR B 1 14  ? 43.130 -46.514 16.034  1.00 38.76  ?  14  TYR B O   1 
ATOM   3593 C  CB  . TYR B 1 14  ? 44.187 -47.651 13.024  1.00 37.86  ?  14  TYR B CB  1 
ATOM   3594 C  CG  . TYR B 1 14  ? 43.933 -46.166 12.818  1.00 37.15  ?  14  TYR B CG  1 
ATOM   3595 C  CD1 . TYR B 1 14  ? 44.926 -45.242 13.095  1.00 43.78  ?  14  TYR B CD1 1 
ATOM   3596 C  CD2 . TYR B 1 14  ? 42.693 -45.674 12.438  1.00 38.54  ?  14  TYR B CD2 1 
ATOM   3597 C  CE1 . TYR B 1 14  ? 44.714 -43.877 12.965  1.00 46.27  ?  14  TYR B CE1 1 
ATOM   3598 C  CE2 . TYR B 1 14  ? 42.456 -44.312 12.317  1.00 41.32  ?  14  TYR B CE2 1 
ATOM   3599 C  CZ  . TYR B 1 14  ? 43.471 -43.403 12.580  1.00 47.97  ?  14  TYR B CZ  1 
ATOM   3600 O  OH  . TYR B 1 14  ? 43.308 -42.040 12.471  1.00 46.69  ?  14  TYR B OH  1 
ATOM   3601 N  N   . LYS B 1 15  ? 41.792 -47.998 14.936  1.00 40.38  ?  15  LYS B N   1 
ATOM   3602 C  CA  . LYS B 1 15  ? 40.518 -47.445 15.373  1.00 40.81  ?  15  LYS B CA  1 
ATOM   3603 C  C   . LYS B 1 15  ? 40.342 -47.676 16.880  1.00 40.81  ?  15  LYS B C   1 
ATOM   3604 O  O   . LYS B 1 15  ? 39.835 -46.802 17.589  1.00 38.53  ?  15  LYS B O   1 
ATOM   3605 C  CB  . LYS B 1 15  ? 39.400 -47.927 14.433  1.00 40.56  ?  15  LYS B CB  1 
ATOM   3606 C  CG  . LYS B 1 15  ? 38.882 -49.356 14.585  1.00 44.40  ?  15  LYS B CG  1 
ATOM   3607 C  CD  . LYS B 1 15  ? 38.269 -49.951 13.315  1.00 44.18  ?  15  LYS B CD  1 
ATOM   3608 C  CE  . LYS B 1 15  ? 37.188 -49.129 12.654  1.00 43.04  ?  15  LYS B CE  1 
ATOM   3609 N  NZ  . LYS B 1 15  ? 35.876 -49.302 13.293  1.00 41.82  1  15  LYS B NZ  1 
ATOM   3610 N  N   . GLU B 1 16  ? 40.856 -48.803 17.393  1.00 42.60  ?  16  GLU B N   1 
ATOM   3611 C  CA  . GLU B 1 16  ? 40.839 -49.034 18.832  1.00 47.13  ?  16  GLU B CA  1 
ATOM   3612 C  C   . GLU B 1 16  ? 41.807 -48.094 19.560  1.00 46.50  ?  16  GLU B C   1 
ATOM   3613 O  O   . GLU B 1 16  ? 41.626 -47.852 20.749  1.00 57.87  ?  16  GLU B O   1 
ATOM   3614 C  CB  . GLU B 1 16  ? 41.089 -50.481 19.260  1.00 46.58  ?  16  GLU B CB  1 
ATOM   3615 C  CG  . GLU B 1 16  ? 39.983 -51.001 20.181  1.00 49.19  ?  16  GLU B CG  1 
ATOM   3616 C  CD  . GLU B 1 16  ? 39.704 -50.195 21.449  1.00 52.37  ?  16  GLU B CD  1 
ATOM   3617 O  OE1 . GLU B 1 16  ? 38.810 -49.317 21.407  1.00 51.55  ?  16  GLU B OE1 1 
ATOM   3618 O  OE2 . GLU B 1 16  ? 40.335 -50.461 22.500  1.00 53.94  -1 16  GLU B OE2 1 
ATOM   3619 N  N   . LEU B 1 17  ? 42.819 -47.550 18.875  1.00 40.96  ?  17  LEU B N   1 
ATOM   3620 C  CA  . LEU B 1 17  ? 43.675 -46.561 19.503  1.00 39.13  ?  17  LEU B CA  1 
ATOM   3621 C  C   . LEU B 1 17  ? 42.963 -45.218 19.466  1.00 40.76  ?  17  LEU B C   1 
ATOM   3622 O  O   . LEU B 1 17  ? 42.845 -44.548 20.492  1.00 40.00  ?  17  LEU B O   1 
ATOM   3623 C  CB  . LEU B 1 17  ? 45.050 -46.439 18.855  1.00 40.69  ?  17  LEU B CB  1 
ATOM   3624 C  CG  . LEU B 1 17  ? 45.999 -45.430 19.522  1.00 40.51  ?  17  LEU B CG  1 
ATOM   3625 C  CD1 . LEU B 1 17  ? 46.699 -46.042 20.740  1.00 35.41  ?  17  LEU B CD1 1 
ATOM   3626 C  CD2 . LEU B 1 17  ? 46.998 -44.839 18.534  1.00 40.62  ?  17  LEU B CD2 1 
ATOM   3627 N  N   . ALA B 1 18  ? 42.531 -44.837 18.258  1.00 42.38  ?  18  ALA B N   1 
ATOM   3628 C  CA  . ALA B 1 18  ? 41.809 -43.595 18.020  1.00 42.61  ?  18  ALA B CA  1 
ATOM   3629 C  C   . ALA B 1 18  ? 40.670 -43.409 19.028  1.00 44.03  ?  18  ALA B C   1 
ATOM   3630 O  O   . ALA B 1 18  ? 40.604 -42.368 19.677  1.00 39.36  ?  18  ALA B O   1 
ATOM   3631 C  CB  . ALA B 1 18  ? 41.307 -43.585 16.590  1.00 43.31  ?  18  ALA B CB  1 
ATOM   3632 N  N   . SER B 1 19  ? 39.797 -44.424 19.175  1.00 44.56  ?  19  SER B N   1 
ATOM   3633 C  CA  . SER B 1 19  ? 38.668 -44.357 20.097  1.00 48.98  ?  19  SER B CA  1 
ATOM   3634 C  C   . SER B 1 19  ? 39.097 -43.850 21.477  1.00 51.04  ?  19  SER B C   1 
ATOM   3635 O  O   . SER B 1 19  ? 38.369 -43.070 22.091  1.00 52.76  ?  19  SER B O   1 
ATOM   3636 C  CB  . SER B 1 19  ? 37.937 -45.695 20.230  1.00 50.03  ?  19  SER B CB  1 
ATOM   3637 O  OG  . SER B 1 19  ? 36.716 -45.692 19.502  1.00 46.92  ?  19  SER B OG  1 
ATOM   3638 N  N   . THR B 1 20  ? 40.253 -44.325 21.968  1.00 45.37  ?  20  THR B N   1 
ATOM   3639 C  CA  . THR B 1 20  ? 40.710 -44.021 23.313  1.00 41.61  ?  20  THR B CA  1 
ATOM   3640 C  C   . THR B 1 20  ? 41.112 -42.558 23.418  1.00 40.29  ?  20  THR B C   1 
ATOM   3641 O  O   . THR B 1 20  ? 41.105 -42.045 24.525  1.00 48.24  ?  20  THR B O   1 
ATOM   3642 C  CB  . THR B 1 20  ? 41.885 -44.910 23.715  1.00 51.70  ?  20  THR B CB  1 
ATOM   3643 O  OG1 . THR B 1 20  ? 42.935 -44.597 22.806  1.00 58.34  ?  20  THR B OG1 1 
ATOM   3644 C  CG2 . THR B 1 20  ? 41.582 -46.397 23.636  1.00 54.89  ?  20  THR B CG2 1 
ATOM   3645 N  N   . LEU B 1 21  ? 41.513 -41.919 22.302  1.00 41.15  ?  21  LEU B N   1 
ATOM   3646 C  CA  . LEU B 1 21  ? 42.006 -40.538 22.297  1.00 41.84  ?  21  LEU B CA  1 
ATOM   3647 C  C   . LEU B 1 21  ? 40.822 -39.560 22.226  1.00 38.04  ?  21  LEU B C   1 
ATOM   3648 O  O   . LEU B 1 21  ? 40.892 -38.428 22.708  1.00 32.62  ?  21  LEU B O   1 
ATOM   3649 C  CB  . LEU B 1 21  ? 42.986 -40.255 21.141  1.00 43.67  ?  21  LEU B CB  1 
ATOM   3650 C  CG  . LEU B 1 21  ? 44.460 -40.710 21.205  1.00 42.33  ?  21  LEU B CG  1 
ATOM   3651 C  CD1 . LEU B 1 21  ? 45.094 -40.801 22.586  1.00 39.40  ?  21  LEU B CD1 1 
ATOM   3652 C  CD2 . LEU B 1 21  ? 44.706 -41.997 20.448  1.00 43.26  ?  21  LEU B CD2 1 
ATOM   3653 N  N   . GLU B 1 22  ? 39.765 -39.980 21.523  1.00 40.75  ?  22  GLU B N   1 
ATOM   3654 C  CA  . GLU B 1 22  ? 38.484 -39.292 21.511  1.00 41.89  ?  22  GLU B CA  1 
ATOM   3655 C  C   . GLU B 1 22  ? 37.903 -39.342 22.926  1.00 41.74  ?  22  GLU B C   1 
ATOM   3656 O  O   . GLU B 1 22  ? 37.628 -38.308 23.526  1.00 40.50  ?  22  GLU B O   1 
ATOM   3657 C  CB  . GLU B 1 22  ? 37.530 -39.957 20.512  1.00 43.70  ?  22  GLU B CB  1 
ATOM   3658 C  CG  . GLU B 1 22  ? 38.016 -40.001 19.061  1.00 45.49  ?  22  GLU B CG  1 
ATOM   3659 C  CD  . GLU B 1 22  ? 38.313 -38.666 18.394  1.00 48.90  ?  22  GLU B CD  1 
ATOM   3660 O  OE1 . GLU B 1 22  ? 37.505 -37.728 18.532  1.00 49.00  ?  22  GLU B OE1 1 
ATOM   3661 O  OE2 . GLU B 1 22  ? 39.357 -38.570 17.711  1.00 55.42  -1 22  GLU B OE2 1 
ATOM   3662 N  N   . ASN B 1 23  ? 37.780 -40.562 23.468  1.00 43.98  ?  23  ASN B N   1 
ATOM   3663 C  CA  . ASN B 1 23  ? 37.393 -40.807 24.850  1.00 44.20  ?  23  ASN B CA  1 
ATOM   3664 C  C   . ASN B 1 23  ? 38.446 -40.224 25.786  1.00 43.13  ?  23  ASN B C   1 
ATOM   3665 O  O   . ASN B 1 23  ? 38.927 -40.906 26.687  1.00 55.28  ?  23  ASN B O   1 
ATOM   3666 C  CB  . ASN B 1 23  ? 37.221 -42.300 25.139  1.00 46.39  ?  23  ASN B CB  1 
ATOM   3667 C  CG  . ASN B 1 23  ? 35.948 -42.906 24.591  1.00 56.76  ?  23  ASN B CG  1 
ATOM   3668 O  OD1 . ASN B 1 23  ? 35.654 -44.068 24.896  1.00 70.21  ?  23  ASN B OD1 1 
ATOM   3669 N  ND2 . ASN B 1 23  ? 35.171 -42.177 23.798  1.00 59.01  ?  23  ASN B ND2 1 
ATOM   3670 N  N   . SER B 1 24  ? 38.810 -38.962 25.568  1.00 37.09  ?  24  SER B N   1 
ATOM   3671 C  CA  . SER B 1 24  ? 39.776 -38.275 26.409  1.00 35.59  ?  24  SER B CA  1 
ATOM   3672 C  C   . SER B 1 24  ? 39.620 -36.776 26.163  1.00 34.75  ?  24  SER B C   1 
ATOM   3673 O  O   . SER B 1 24  ? 38.752 -36.383 25.381  1.00 34.98  ?  24  SER B O   1 
ATOM   3674 C  CB  . SER B 1 24  ? 41.176 -38.726 26.128  1.00 35.05  ?  24  SER B CB  1 
ATOM   3675 O  OG  . SER B 1 24  ? 41.849 -37.782 25.305  1.00 36.42  ?  24  SER B OG  1 
ATOM   3676 N  N   . THR B 1 25  ? 40.441 -35.942 26.813  1.00 29.42  ?  25  THR B N   1 
ATOM   3677 C  CA  . THR B 1 25  ? 40.321 -34.509 26.598  1.00 31.77  ?  25  THR B CA  1 
ATOM   3678 C  C   . THR B 1 25  ? 41.473 -34.006 25.721  1.00 33.08  ?  25  THR B C   1 
ATOM   3679 O  O   . THR B 1 25  ? 41.647 -32.792 25.585  1.00 33.66  ?  25  THR B O   1 
ATOM   3680 C  CB  . THR B 1 25  ? 40.251 -33.779 27.942  1.00 34.35  ?  25  THR B CB  1 
ATOM   3681 O  OG1 . THR B 1 25  ? 41.464 -34.071 28.634  1.00 37.85  ?  25  THR B OG1 1 
ATOM   3682 C  CG2 . THR B 1 25  ? 39.038 -34.170 28.771  1.00 33.28  ?  25  THR B CG2 1 
ATOM   3683 N  N   . LEU B 1 26  ? 42.220 -34.934 25.093  1.00 30.09  ?  26  LEU B N   1 
ATOM   3684 C  CA  . LEU B 1 26  ? 43.470 -34.617 24.422  1.00 30.01  ?  26  LEU B CA  1 
ATOM   3685 C  C   . LEU B 1 26  ? 43.221 -33.751 23.195  1.00 33.96  ?  26  LEU B C   1 
ATOM   3686 O  O   . LEU B 1 26  ? 43.971 -32.815 22.949  1.00 37.95  ?  26  LEU B O   1 
ATOM   3687 C  CB  . LEU B 1 26  ? 44.229 -35.878 24.021  1.00 33.78  ?  26  LEU B CB  1 
ATOM   3688 C  CG  . LEU B 1 26  ? 45.494 -35.672 23.170  1.00 35.83  ?  26  LEU B CG  1 
ATOM   3689 C  CD1 . LEU B 1 26  ? 46.557 -34.808 23.838  1.00 35.98  ?  26  LEU B CD1 1 
ATOM   3690 C  CD2 . LEU B 1 26  ? 46.097 -37.015 22.778  1.00 35.92  ?  26  LEU B CD2 1 
ATOM   3691 N  N   . PHE B 1 27  ? 42.184 -34.058 22.408  1.00 39.01  ?  27  PHE B N   1 
ATOM   3692 C  CA  . PHE B 1 27  ? 41.936 -33.296 21.187  1.00 41.22  ?  27  PHE B CA  1 
ATOM   3693 C  C   . PHE B 1 27  ? 41.208 -31.973 21.464  1.00 42.24  ?  27  PHE B C   1 
ATOM   3694 O  O   . PHE B 1 27  ? 40.745 -31.353 20.507  1.00 37.52  ?  27  PHE B O   1 
ATOM   3695 C  CB  . PHE B 1 27  ? 41.151 -34.184 20.217  1.00 41.88  ?  27  PHE B CB  1 
ATOM   3696 C  CG  . PHE B 1 27  ? 41.925 -35.375 19.667  1.00 39.34  ?  27  PHE B CG  1 
ATOM   3697 C  CD1 . PHE B 1 27  ? 43.152 -35.203 19.045  1.00 39.25  ?  27  PHE B CD1 1 
ATOM   3698 C  CD2 . PHE B 1 27  ? 41.427 -36.670 19.782  1.00 41.71  ?  27  PHE B CD2 1 
ATOM   3699 C  CE1 . PHE B 1 27  ? 43.862 -36.298 18.565  1.00 40.95  ?  27  PHE B CE1 1 
ATOM   3700 C  CE2 . PHE B 1 27  ? 42.132 -37.757 19.290  1.00 40.58  ?  27  PHE B CE2 1 
ATOM   3701 C  CZ  . PHE B 1 27  ? 43.350 -37.571 18.689  1.00 40.83  ?  27  PHE B CZ  1 
ATOM   3702 N  N   . GLN B 1 28  ? 41.095 -31.571 22.752  1.00 44.67  ?  28  GLN B N   1 
ATOM   3703 C  CA  . GLN B 1 28  ? 40.517 -30.298 23.185  1.00 47.15  ?  28  GLN B CA  1 
ATOM   3704 C  C   . GLN B 1 28  ? 41.602 -29.348 23.704  1.00 47.63  ?  28  GLN B C   1 
ATOM   3705 O  O   . GLN B 1 28  ? 41.544 -28.133 23.513  1.00 45.12  ?  28  GLN B O   1 
ATOM   3706 C  CB  . GLN B 1 28  ? 39.604 -30.414 24.408  1.00 45.37  ?  28  GLN B CB  1 
ATOM   3707 C  CG  . GLN B 1 28  ? 38.325 -31.225 24.222  1.00 42.19  ?  28  GLN B CG  1 
ATOM   3708 C  CD  . GLN B 1 28  ? 37.473 -31.190 25.476  1.00 37.62  ?  28  GLN B CD  1 
ATOM   3709 O  OE1 . GLN B 1 28  ? 37.832 -30.540 26.468  1.00 30.16  ?  28  GLN B OE1 1 
ATOM   3710 N  NE2 . GLN B 1 28  ? 36.352 -31.902 25.457  1.00 37.60  ?  28  GLN B NE2 1 
ATOM   3711 N  N   . LYS B 1 29  ? 42.550 -29.914 24.454  1.00 48.38  ?  29  LYS B N   1 
ATOM   3712 C  CA  . LYS B 1 29  ? 43.774 -29.211 24.788  1.00 47.67  ?  29  LYS B CA  1 
ATOM   3713 C  C   . LYS B 1 29  ? 44.669 -29.176 23.550  1.00 43.22  ?  29  LYS B C   1 
ATOM   3714 O  O   . LYS B 1 29  ? 45.346 -28.181 23.313  1.00 39.49  ?  29  LYS B O   1 
ATOM   3715 C  CB  . LYS B 1 29  ? 44.475 -29.879 25.977  1.00 49.90  ?  29  LYS B CB  1 
ATOM   3716 C  CG  . LYS B 1 29  ? 43.688 -29.933 27.296  1.00 52.24  ?  29  LYS B CG  1 
ATOM   3717 C  CD  . LYS B 1 29  ? 44.499 -29.637 28.565  1.00 55.53  ?  29  LYS B CD  1 
ATOM   3718 C  CE  . LYS B 1 29  ? 44.440 -30.647 29.698  1.00 54.81  ?  29  LYS B CE  1 
ATOM   3719 N  NZ  . LYS B 1 29  ? 43.088 -31.096 30.057  1.00 56.77  1  29  LYS B NZ  1 
ATOM   3720 N  N   . ASN B 1 30  ? 44.634 -30.252 22.745  1.00 40.58  ?  30  ASN B N   1 
ATOM   3721 C  CA  . ASN B 1 30  ? 45.524 -30.405 21.602  1.00 38.09  ?  30  ASN B CA  1 
ATOM   3722 C  C   . ASN B 1 30  ? 44.759 -30.926 20.381  1.00 37.63  ?  30  ASN B C   1 
ATOM   3723 O  O   . ASN B 1 30  ? 44.930 -32.069 19.985  1.00 43.73  ?  30  ASN B O   1 
ATOM   3724 C  CB  . ASN B 1 30  ? 46.720 -31.267 21.997  1.00 35.12  ?  30  ASN B CB  1 
ATOM   3725 C  CG  . ASN B 1 30  ? 47.456 -30.693 23.187  1.00 30.69  ?  30  ASN B CG  1 
ATOM   3726 O  OD1 . ASN B 1 30  ? 47.639 -31.360 24.211  1.00 27.90  ?  30  ASN B OD1 1 
ATOM   3727 N  ND2 . ASN B 1 30  ? 47.898 -29.454 23.072  1.00 30.61  ?  30  ASN B ND2 1 
ATOM   3728 N  N   . PRO B 1 31  ? 43.899 -30.104 19.736  1.00 36.23  ?  31  PRO B N   1 
ATOM   3729 C  CA  . PRO B 1 31  ? 43.199 -30.482 18.499  1.00 34.75  ?  31  PRO B CA  1 
ATOM   3730 C  C   . PRO B 1 31  ? 44.027 -30.884 17.281  1.00 34.66  ?  31  PRO B C   1 
ATOM   3731 O  O   . PRO B 1 31  ? 43.609 -31.751 16.503  1.00 31.02  ?  31  PRO B O   1 
ATOM   3732 C  CB  . PRO B 1 31  ? 42.378 -29.235 18.134  1.00 33.35  ?  31  PRO B CB  1 
ATOM   3733 C  CG  . PRO B 1 31  ? 42.247 -28.466 19.412  1.00 34.92  ?  31  PRO B CG  1 
ATOM   3734 C  CD  . PRO B 1 31  ? 43.483 -28.787 20.234  1.00 36.23  ?  31  PRO B CD  1 
ATOM   3735 N  N   . GLU B 1 32  ? 45.165 -30.192 17.113  1.00 36.50  ?  32  GLU B N   1 
ATOM   3736 C  CA  . GLU B 1 32  ? 46.045 -30.311 15.952  1.00 35.56  ?  32  GLU B CA  1 
ATOM   3737 C  C   . GLU B 1 32  ? 46.711 -31.695 15.898  1.00 34.14  ?  32  GLU B C   1 
ATOM   3738 O  O   . GLU B 1 32  ? 47.232 -32.098 14.856  1.00 32.46  ?  32  GLU B O   1 
ATOM   3739 C  CB  . GLU B 1 32  ? 47.013 -29.121 15.962  1.00 37.89  ?  32  GLU B CB  1 
ATOM   3740 C  CG  . GLU B 1 32  ? 47.971 -29.064 17.155  1.00 42.53  ?  32  GLU B CG  1 
ATOM   3741 C  CD  . GLU B 1 32  ? 47.438 -28.691 18.543  1.00 46.75  ?  32  GLU B CD  1 
ATOM   3742 O  OE1 . GLU B 1 32  ? 46.299 -28.180 18.681  1.00 44.53  ?  32  GLU B OE1 1 
ATOM   3743 O  OE2 . GLU B 1 32  ? 48.180 -28.941 19.524  1.00 47.98  -1 32  GLU B OE2 1 
ATOM   3744 N  N   . TYR B 1 33  ? 46.630 -32.445 17.005  1.00 33.21  ?  33  TYR B N   1 
ATOM   3745 C  CA  . TYR B 1 33  ? 47.160 -33.796 17.104  1.00 36.70  ?  33  TYR B CA  1 
ATOM   3746 C  C   . TYR B 1 33  ? 46.372 -34.766 16.216  1.00 40.97  ?  33  TYR B C   1 
ATOM   3747 O  O   . TYR B 1 33  ? 46.862 -35.856 15.913  1.00 45.33  ?  33  TYR B O   1 
ATOM   3748 C  CB  . TYR B 1 33  ? 47.155 -34.226 18.581  1.00 38.79  ?  33  TYR B CB  1 
ATOM   3749 C  CG  . TYR B 1 33  ? 48.374 -33.833 19.413  1.00 42.28  ?  33  TYR B CG  1 
ATOM   3750 C  CD1 . TYR B 1 33  ? 48.792 -34.629 20.469  1.00 44.00  ?  33  TYR B CD1 1 
ATOM   3751 C  CD2 . TYR B 1 33  ? 49.118 -32.683 19.151  1.00 43.67  ?  33  TYR B CD2 1 
ATOM   3752 C  CE1 . TYR B 1 33  ? 49.913 -34.313 21.218  1.00 43.36  ?  33  TYR B CE1 1 
ATOM   3753 C  CE2 . TYR B 1 33  ? 50.241 -32.355 19.895  1.00 42.07  ?  33  TYR B CE2 1 
ATOM   3754 C  CZ  . TYR B 1 33  ? 50.639 -33.175 20.936  1.00 41.53  ?  33  TYR B CZ  1 
ATOM   3755 O  OH  . TYR B 1 33  ? 51.726 -32.900 21.713  1.00 41.21  ?  33  TYR B OH  1 
ATOM   3756 N  N   . ARG B 1 34  ? 45.145 -34.403 15.807  1.00 39.56  ?  34  ARG B N   1 
ATOM   3757 C  CA  . ARG B 1 34  ? 44.372 -35.248 14.903  1.00 39.81  ?  34  ARG B CA  1 
ATOM   3758 C  C   . ARG B 1 34  ? 45.128 -35.382 13.584  1.00 40.08  ?  34  ARG B C   1 
ATOM   3759 O  O   . ARG B 1 34  ? 45.065 -36.437 12.940  1.00 40.37  ?  34  ARG B O   1 
ATOM   3760 C  CB  . ARG B 1 34  ? 42.986 -34.715 14.520  1.00 43.18  ?  34  ARG B CB  1 
ATOM   3761 C  CG  . ARG B 1 34  ? 41.916 -34.586 15.597  1.00 48.61  ?  34  ARG B CG  1 
ATOM   3762 C  CD  . ARG B 1 34  ? 40.630 -33.969 15.015  1.00 49.73  ?  34  ARG B CD  1 
ATOM   3763 N  NE  . ARG B 1 34  ? 39.884 -33.175 15.996  1.00 49.51  ?  34  ARG B NE  1 
ATOM   3764 C  CZ  . ARG B 1 34  ? 39.175 -33.670 17.010  1.00 58.01  ?  34  ARG B CZ  1 
ATOM   3765 N  NH1 . ARG B 1 34  ? 39.019 -34.980 17.162  1.00 60.15  1  34  ARG B NH1 1 
ATOM   3766 N  NH2 . ARG B 1 34  ? 38.597 -32.846 17.869  1.00 59.50  ?  34  ARG B NH2 1 
ATOM   3767 N  N   . LYS B 1 35  ? 45.818 -34.292 13.199  1.00 34.66  ?  35  LYS B N   1 
ATOM   3768 C  CA  . LYS B 1 35  ? 46.655 -34.286 12.014  1.00 34.82  ?  35  LYS B CA  1 
ATOM   3769 C  C   . LYS B 1 35  ? 47.797 -35.285 12.169  1.00 29.47  ?  35  LYS B C   1 
ATOM   3770 O  O   . LYS B 1 35  ? 48.226 -35.837 11.177  1.00 32.34  ?  35  LYS B O   1 
ATOM   3771 C  CB  . LYS B 1 35  ? 47.211 -32.895 11.673  1.00 38.36  ?  35  LYS B CB  1 
ATOM   3772 C  CG  . LYS B 1 35  ? 46.187 -31.919 11.099  1.00 38.59  ?  35  LYS B CG  1 
ATOM   3773 C  CD  . LYS B 1 35  ? 46.653 -30.483 10.917  1.00 37.93  ?  35  LYS B CD  1 
ATOM   3774 C  CE  . LYS B 1 35  ? 46.981 -29.816 12.215  1.00 38.91  ?  35  LYS B CE  1 
ATOM   3775 N  NZ  . LYS B 1 35  ? 47.680 -28.555 11.985  1.00 36.63  1  35  LYS B NZ  1 
ATOM   3776 N  N   . ALA B 1 36  ? 48.289 -35.509 13.391  1.00 26.79  ?  36  ALA B N   1 
ATOM   3777 C  CA  . ALA B 1 36  ? 49.415 -36.409 13.605  1.00 30.07  ?  36  ALA B CA  1 
ATOM   3778 C  C   . ALA B 1 36  ? 49.006 -37.865 13.363  1.00 36.10  ?  36  ALA B C   1 
ATOM   3779 O  O   . ALA B 1 36  ? 49.688 -38.589 12.636  1.00 34.23  ?  36  ALA B O   1 
ATOM   3780 C  CB  . ALA B 1 36  ? 49.981 -36.223 14.993  1.00 28.54  ?  36  ALA B CB  1 
ATOM   3781 N  N   . LEU B 1 37  ? 47.870 -38.260 13.963  1.00 39.88  ?  37  LEU B N   1 
ATOM   3782 C  CA  . LEU B 1 37  ? 47.272 -39.576 13.818  1.00 37.22  ?  37  LEU B CA  1 
ATOM   3783 C  C   . LEU B 1 37  ? 47.053 -39.946 12.358  1.00 35.03  ?  37  LEU B C   1 
ATOM   3784 O  O   . LEU B 1 37  ? 46.978 -41.122 12.046  1.00 37.27  ?  37  LEU B O   1 
ATOM   3785 C  CB  . LEU B 1 37  ? 45.937 -39.538 14.549  1.00 42.76  ?  37  LEU B CB  1 
ATOM   3786 C  CG  . LEU B 1 37  ? 45.213 -40.878 14.704  1.00 47.74  ?  37  LEU B CG  1 
ATOM   3787 C  CD1 . LEU B 1 37  ? 46.102 -41.924 15.395  1.00 51.69  ?  37  LEU B CD1 1 
ATOM   3788 C  CD2 . LEU B 1 37  ? 43.922 -40.654 15.477  1.00 42.06  ?  37  LEU B CD2 1 
ATOM   3789 N  N   . ALA B 1 38  ? 46.886 -38.949 11.483  1.00 33.40  ?  38  ALA B N   1 
ATOM   3790 C  CA  . ALA B 1 38  ? 46.764 -39.201 10.055  1.00 33.68  ?  38  ALA B CA  1 
ATOM   3791 C  C   . ALA B 1 38  ? 48.096 -39.712 9.515   1.00 32.00  ?  38  ALA B C   1 
ATOM   3792 O  O   . ALA B 1 38  ? 48.125 -40.605 8.681   1.00 34.60  ?  38  ALA B O   1 
ATOM   3793 C  CB  . ALA B 1 38  ? 46.327 -37.934 9.333   1.00 33.01  ?  38  ALA B CB  1 
ATOM   3794 N  N   . VAL B 1 39  ? 49.187 -39.142 10.039  1.00 30.05  ?  39  VAL B N   1 
ATOM   3795 C  CA  . VAL B 1 39  ? 50.525 -39.256 9.477   1.00 27.29  ?  39  VAL B CA  1 
ATOM   3796 C  C   . VAL B 1 39  ? 51.282 -40.435 10.110  1.00 28.93  ?  39  VAL B C   1 
ATOM   3797 O  O   . VAL B 1 39  ? 52.022 -41.101 9.394   1.00 29.56  ?  39  VAL B O   1 
ATOM   3798 C  CB  . VAL B 1 39  ? 51.257 -37.901 9.652   1.00 23.25  ?  39  VAL B CB  1 
ATOM   3799 C  CG1 . VAL B 1 39  ? 52.611 -37.844 8.951   1.00 23.12  ?  39  VAL B CG1 1 
ATOM   3800 C  CG2 . VAL B 1 39  ? 50.431 -36.722 9.155   1.00 22.31  ?  39  VAL B CG2 1 
ATOM   3801 N  N   . VAL B 1 40  ? 51.066 -40.719 11.418  1.00 28.69  ?  40  VAL B N   1 
ATOM   3802 C  CA  . VAL B 1 40  ? 51.787 -41.762 12.146  1.00 27.82  ?  40  VAL B CA  1 
ATOM   3803 C  C   . VAL B 1 40  ? 51.335 -43.112 11.598  1.00 29.77  ?  40  VAL B C   1 
ATOM   3804 O  O   . VAL B 1 40  ? 52.073 -44.091 11.698  1.00 28.49  ?  40  VAL B O   1 
ATOM   3805 C  CB  . VAL B 1 40  ? 51.657 -41.824 13.691  1.00 26.63  ?  40  VAL B CB  1 
ATOM   3806 C  CG1 . VAL B 1 40  ? 52.904 -42.406 14.341  1.00 26.23  ?  40  VAL B CG1 1 
ATOM   3807 C  CG2 . VAL B 1 40  ? 51.352 -40.496 14.353  1.00 26.04  ?  40  VAL B CG2 1 
ATOM   3808 N  N   . SER B 1 41  ? 50.107 -43.142 11.051  1.00 33.46  ?  41  SER B N   1 
ATOM   3809 C  CA  . SER B 1 41  ? 49.358 -44.368 10.791  1.00 33.39  ?  41  SER B CA  1 
ATOM   3810 C  C   . SER B 1 41  ? 49.722 -45.007 9.452   1.00 28.42  ?  41  SER B C   1 
ATOM   3811 O  O   . SER B 1 41  ? 49.375 -46.160 9.182   1.00 26.08  ?  41  SER B O   1 
ATOM   3812 C  CB  . SER B 1 41  ? 47.904 -44.057 10.877  1.00 34.86  ?  41  SER B CB  1 
ATOM   3813 O  OG  . SER B 1 41  ? 47.696 -43.385 12.114  1.00 39.74  ?  41  SER B OG  1 
ATOM   3814 N  N   . VAL B 1 42  ? 50.439 -44.246 8.622   1.00 25.88  ?  42  VAL B N   1 
ATOM   3815 C  CA  . VAL B 1 42  ? 50.948 -44.758 7.359   1.00 24.91  ?  42  VAL B CA  1 
ATOM   3816 C  C   . VAL B 1 42  ? 52.458 -44.948 7.538   1.00 26.12  ?  42  VAL B C   1 
ATOM   3817 O  O   . VAL B 1 42  ? 53.169 -44.001 7.913   1.00 29.61  ?  42  VAL B O   1 
ATOM   3818 C  CB  . VAL B 1 42  ? 50.547 -43.855 6.172   1.00 22.68  ?  42  VAL B CB  1 
ATOM   3819 C  CG1 . VAL B 1 42  ? 50.081 -42.482 6.637   1.00 23.03  ?  42  VAL B CG1 1 
ATOM   3820 C  CG2 . VAL B 1 42  ? 51.625 -43.738 5.096   1.00 22.16  ?  42  VAL B CG2 1 
ATOM   3821 N  N   . PRO B 1 43  ? 52.987 -46.189 7.363   1.00 22.19  ?  43  PRO B N   1 
ATOM   3822 C  CA  . PRO B 1 43  ? 54.399 -46.472 7.640   1.00 21.34  ?  43  PRO B CA  1 
ATOM   3823 C  C   . PRO B 1 43  ? 55.365 -45.533 6.924   1.00 18.83  ?  43  PRO B C   1 
ATOM   3824 O  O   . PRO B 1 43  ? 55.159 -45.206 5.764   1.00 19.61  ?  43  PRO B O   1 
ATOM   3825 C  CB  . PRO B 1 43  ? 54.543 -47.932 7.131   1.00 21.88  ?  43  PRO B CB  1 
ATOM   3826 C  CG  . PRO B 1 43  ? 53.171 -48.525 7.295   1.00 20.62  ?  43  PRO B CG  1 
ATOM   3827 C  CD  . PRO B 1 43  ? 52.249 -47.386 6.935   1.00 21.34  ?  43  PRO B CD  1 
ATOM   3828 N  N   . GLU B 1 44  ? 56.459 -45.162 7.580   1.00 17.81  ?  44  GLU B N   1 
ATOM   3829 C  CA  . GLU B 1 44  ? 57.473 -44.349 6.920   1.00 18.00  ?  44  GLU B CA  1 
ATOM   3830 C  C   . GLU B 1 44  ? 57.963 -45.068 5.659   1.00 19.35  ?  44  GLU B C   1 
ATOM   3831 O  O   . GLU B 1 44  ? 57.943 -44.482 4.577   1.00 18.09  ?  44  GLU B O   1 
ATOM   3832 C  CB  . GLU B 1 44  ? 58.650 -44.025 7.839   1.00 16.14  ?  44  GLU B CB  1 
ATOM   3833 C  CG  . GLU B 1 44  ? 58.394 -42.887 8.818   1.00 15.05  ?  44  GLU B CG  1 
ATOM   3834 C  CD  . GLU B 1 44  ? 59.547 -42.667 9.796   1.00 15.52  ?  44  GLU B CD  1 
ATOM   3835 O  OE1 . GLU B 1 44  ? 59.339 -41.905 10.758  1.00 17.10  ?  44  GLU B OE1 1 
ATOM   3836 O  OE2 . GLU B 1 44  ? 60.662 -43.207 9.624   1.00 13.90  -1 44  GLU B OE2 1 
ATOM   3837 N  N   . ARG B 1 45  ? 58.366 -46.342 5.834   1.00 21.37  ?  45  ARG B N   1 
ATOM   3838 C  CA  . ARG B 1 45  ? 58.846 -47.204 4.765   1.00 23.90  ?  45  ARG B CA  1 
ATOM   3839 C  C   . ARG B 1 45  ? 58.455 -48.653 5.058   1.00 24.62  ?  45  ARG B C   1 
ATOM   3840 O  O   . ARG B 1 45  ? 58.389 -49.046 6.219   1.00 29.47  ?  45  ARG B O   1 
ATOM   3841 C  CB  . ARG B 1 45  ? 60.367 -47.054 4.704   1.00 27.16  ?  45  ARG B CB  1 
ATOM   3842 C  CG  . ARG B 1 45  ? 61.034 -47.699 3.495   1.00 30.50  ?  45  ARG B CG  1 
ATOM   3843 C  CD  . ARG B 1 45  ? 62.453 -47.153 3.350   1.00 32.23  ?  45  ARG B CD  1 
ATOM   3844 N  NE  . ARG B 1 45  ? 62.993 -46.848 4.681   1.00 35.15  ?  45  ARG B NE  1 
ATOM   3845 C  CZ  . ARG B 1 45  ? 63.422 -45.666 5.133   1.00 37.20  ?  45  ARG B CZ  1 
ATOM   3846 N  NH1 . ARG B 1 45  ? 63.415 -44.598 4.349   1.00 35.85  1  45  ARG B NH1 1 
ATOM   3847 N  NH2 . ARG B 1 45  ? 63.879 -45.570 6.377   1.00 35.57  ?  45  ARG B NH2 1 
ATOM   3848 N  N   . VAL B 1 46  ? 58.193 -49.422 3.997   1.00 23.66  ?  46  VAL B N   1 
ATOM   3849 C  CA  . VAL B 1 46  ? 57.939 -50.855 4.047   1.00 26.18  ?  46  VAL B CA  1 
ATOM   3850 C  C   . VAL B 1 46  ? 58.751 -51.532 2.928   1.00 26.86  ?  46  VAL B C   1 
ATOM   3851 O  O   . VAL B 1 46  ? 58.781 -51.071 1.783   1.00 23.15  ?  46  VAL B O   1 
ATOM   3852 C  CB  . VAL B 1 46  ? 56.428 -51.175 3.886   1.00 28.86  ?  46  VAL B CB  1 
ATOM   3853 C  CG1 . VAL B 1 46  ? 56.172 -52.662 3.609   1.00 29.99  ?  46  VAL B CG1 1 
ATOM   3854 C  CG2 . VAL B 1 46  ? 55.564 -50.711 5.061   1.00 27.44  ?  46  VAL B CG2 1 
ATOM   3855 N  N   . ILE B 1 47  ? 59.401 -52.659 3.242   1.00 27.59  ?  47  ILE B N   1 
ATOM   3856 C  CA  . ILE B 1 47  ? 60.098 -53.427 2.219   1.00 27.58  ?  47  ILE B CA  1 
ATOM   3857 C  C   . ILE B 1 47  ? 59.501 -54.832 2.175   1.00 26.83  ?  47  ILE B C   1 
ATOM   3858 O  O   . ILE B 1 47  ? 59.362 -55.484 3.208   1.00 27.86  ?  47  ILE B O   1 
ATOM   3859 C  CB  . ILE B 1 47  ? 61.629 -53.455 2.421   1.00 28.11  ?  47  ILE B CB  1 
ATOM   3860 C  CG1 . ILE B 1 47  ? 62.222 -52.083 2.777   1.00 29.15  ?  47  ILE B CG1 1 
ATOM   3861 C  CG2 . ILE B 1 47  ? 62.321 -54.026 1.184   1.00 28.58  ?  47  ILE B CG2 1 
ATOM   3862 C  CD1 . ILE B 1 47  ? 62.431 -51.864 4.266   1.00 29.67  ?  47  ILE B CD1 1 
ATOM   3863 N  N   . GLN B 1 48  ? 59.149 -55.266 0.956   1.00 25.82  ?  48  GLN B N   1 
ATOM   3864 C  CA  . GLN B 1 48  ? 58.752 -56.632 0.670   1.00 26.29  ?  48  GLN B CA  1 
ATOM   3865 C  C   . GLN B 1 48  ? 59.664 -57.172 -0.424  1.00 27.08  ?  48  GLN B C   1 
ATOM   3866 O  O   . GLN B 1 48  ? 59.768 -56.562 -1.488  1.00 27.14  ?  48  GLN B O   1 
ATOM   3867 C  CB  . GLN B 1 48  ? 57.337 -56.751 0.114   1.00 28.94  ?  48  GLN B CB  1 
ATOM   3868 C  CG  . GLN B 1 48  ? 56.305 -55.843 0.771   1.00 30.93  ?  48  GLN B CG  1 
ATOM   3869 C  CD  . GLN B 1 48  ? 54.912 -56.397 0.611   1.00 31.33  ?  48  GLN B CD  1 
ATOM   3870 O  OE1 . GLN B 1 48  ? 54.742 -57.531 0.162   1.00 30.47  ?  48  GLN B OE1 1 
ATOM   3871 N  NE2 . GLN B 1 48  ? 53.907 -55.623 0.990   1.00 34.31  ?  48  GLN B NE2 1 
ATOM   3872 N  N   . PHE B 1 49  ? 60.293 -58.323 -0.159  1.00 25.79  ?  49  PHE B N   1 
ATOM   3873 C  CA  . PHE B 1 49  ? 61.338 -58.848 -1.015  1.00 25.50  ?  49  PHE B CA  1 
ATOM   3874 C  C   . PHE B 1 49  ? 61.216 -60.371 -1.089  1.00 28.85  ?  49  PHE B C   1 
ATOM   3875 O  O   . PHE B 1 49  ? 60.792 -61.031 -0.129  1.00 28.11  ?  49  PHE B O   1 
ATOM   3876 C  CB  . PHE B 1 49  ? 62.686 -58.382 -0.454  1.00 24.27  ?  49  PHE B CB  1 
ATOM   3877 C  CG  . PHE B 1 49  ? 62.975 -58.787 0.991   1.00 22.85  ?  49  PHE B CG  1 
ATOM   3878 C  CD1 . PHE B 1 49  ? 63.547 -60.025 1.294   1.00 22.03  ?  49  PHE B CD1 1 
ATOM   3879 C  CD2 . PHE B 1 49  ? 62.678 -57.931 2.039   1.00 21.76  ?  49  PHE B CD2 1 
ATOM   3880 C  CE1 . PHE B 1 49  ? 63.778 -60.410 2.605   1.00 21.39  ?  49  PHE B CE1 1 
ATOM   3881 C  CE2 . PHE B 1 49  ? 62.938 -58.306 3.344   1.00 22.80  ?  49  PHE B CE2 1 
ATOM   3882 C  CZ  . PHE B 1 49  ? 63.481 -59.548 3.625   1.00 22.90  ?  49  PHE B CZ  1 
ATOM   3883 N  N   . ARG B 1 50  ? 61.629 -60.932 -2.233  1.00 28.67  ?  50  ARG B N   1 
ATOM   3884 C  CA  . ARG B 1 50  ? 61.576 -62.371 -2.439  1.00 28.80  ?  50  ARG B CA  1 
ATOM   3885 C  C   . ARG B 1 50  ? 62.712 -63.024 -1.654  1.00 28.69  ?  50  ARG B C   1 
ATOM   3886 O  O   . ARG B 1 50  ? 63.799 -62.436 -1.556  1.00 24.97  ?  50  ARG B O   1 
ATOM   3887 C  CB  . ARG B 1 50  ? 61.700 -62.564 -3.949  1.00 29.41  ?  50  ARG B CB  1 
ATOM   3888 C  CG  . ARG B 1 50  ? 61.372 -63.944 -4.482  1.00 30.83  ?  50  ARG B CG  1 
ATOM   3889 C  CD  . ARG B 1 50  ? 61.501 -63.888 -5.999  1.00 29.17  ?  50  ARG B CD  1 
ATOM   3890 N  NE  . ARG B 1 50  ? 62.902 -63.888 -6.429  1.00 28.37  ?  50  ARG B NE  1 
ATOM   3891 C  CZ  . ARG B 1 50  ? 63.279 -63.660 -7.678  1.00 30.08  ?  50  ARG B CZ  1 
ATOM   3892 N  NH1 . ARG B 1 50  ? 62.375 -63.310 -8.589  1.00 27.80  1  50  ARG B NH1 1 
ATOM   3893 N  NH2 . ARG B 1 50  ? 64.556 -63.795 -8.016  1.00 30.09  ?  50  ARG B NH2 1 
ATOM   3894 N  N   . VAL B 1 51  ? 62.450 -64.218 -1.088  1.00 27.25  ?  51  VAL B N   1 
ATOM   3895 C  CA  . VAL B 1 51  ? 63.484 -64.996 -0.406  1.00 24.98  ?  51  VAL B CA  1 
ATOM   3896 C  C   . VAL B 1 51  ? 63.558 -66.367 -1.059  1.00 24.22  ?  51  VAL B C   1 
ATOM   3897 O  O   . VAL B 1 51  ? 62.699 -67.214 -0.774  1.00 27.10  ?  51  VAL B O   1 
ATOM   3898 C  CB  . VAL B 1 51  ? 63.250 -65.155 1.110   1.00 24.40  ?  51  VAL B CB  1 
ATOM   3899 C  CG1 . VAL B 1 51  ? 64.346 -65.962 1.790   1.00 23.59  ?  51  VAL B CG1 1 
ATOM   3900 C  CG2 . VAL B 1 51  ? 63.089 -63.816 1.818   1.00 25.27  ?  51  VAL B CG2 1 
ATOM   3901 N  N   . VAL B 1 52  ? 64.571 -66.548 -1.923  1.00 20.92  ?  52  VAL B N   1 
ATOM   3902 C  CA  . VAL B 1 52  ? 64.854 -67.822 -2.570  1.00 21.19  ?  52  VAL B CA  1 
ATOM   3903 C  C   . VAL B 1 52  ? 65.963 -68.524 -1.772  1.00 22.22  ?  52  VAL B C   1 
ATOM   3904 O  O   . VAL B 1 52  ? 67.039 -67.972 -1.549  1.00 19.24  ?  52  VAL B O   1 
ATOM   3905 C  CB  . VAL B 1 52  ? 65.209 -67.702 -4.075  1.00 21.46  ?  52  VAL B CB  1 
ATOM   3906 C  CG1 . VAL B 1 52  ? 65.753 -69.008 -4.657  1.00 22.29  ?  52  VAL B CG1 1 
ATOM   3907 C  CG2 . VAL B 1 52  ? 64.043 -67.217 -4.929  1.00 20.67  ?  52  VAL B CG2 1 
ATOM   3908 N  N   . TRP B 1 53  ? 65.659 -69.752 -1.329  1.00 24.45  ?  53  TRP B N   1 
ATOM   3909 C  CA  . TRP B 1 53  ? 66.559 -70.579 -0.541  1.00 26.68  ?  53  TRP B CA  1 
ATOM   3910 C  C   . TRP B 1 53  ? 66.378 -72.040 -0.958  1.00 26.86  ?  53  TRP B C   1 
ATOM   3911 O  O   . TRP B 1 53  ? 65.368 -72.347 -1.584  1.00 29.55  ?  53  TRP B O   1 
ATOM   3912 C  CB  . TRP B 1 53  ? 66.238 -70.375 0.947   1.00 28.05  ?  53  TRP B CB  1 
ATOM   3913 C  CG  . TRP B 1 53  ? 64.856 -70.832 1.343   1.00 27.84  ?  53  TRP B CG  1 
ATOM   3914 C  CD1 . TRP B 1 53  ? 63.666 -70.195 1.138   1.00 30.18  ?  53  TRP B CD1 1 
ATOM   3915 C  CD2 . TRP B 1 53  ? 64.527 -72.053 2.029   1.00 27.19  ?  53  TRP B CD2 1 
ATOM   3916 N  NE1 . TRP B 1 53  ? 62.623 -70.924 1.656   1.00 28.83  ?  53  TRP B NE1 1 
ATOM   3917 C  CE2 . TRP B 1 53  ? 63.123 -72.075 2.205   1.00 28.53  ?  53  TRP B CE2 1 
ATOM   3918 C  CE3 . TRP B 1 53  ? 65.282 -73.126 2.502   1.00 27.63  ?  53  TRP B CE3 1 
ATOM   3919 C  CZ2 . TRP B 1 53  ? 62.467 -73.133 2.832   1.00 27.62  ?  53  TRP B CZ2 1 
ATOM   3920 C  CZ3 . TRP B 1 53  ? 64.632 -74.168 3.125   1.00 26.36  ?  53  TRP B CZ3 1 
ATOM   3921 C  CH2 . TRP B 1 53  ? 63.246 -74.175 3.273   1.00 26.25  ?  53  TRP B CH2 1 
ATOM   3922 N  N   . GLU B 1 54  ? 67.314 -72.922 -0.565  1.00 25.79  ?  54  GLU B N   1 
ATOM   3923 C  CA  . GLU B 1 54  ? 67.331 -74.343 -0.921  1.00 26.43  ?  54  GLU B CA  1 
ATOM   3924 C  C   . GLU B 1 54  ? 67.041 -75.258 0.280   1.00 26.61  ?  54  GLU B C   1 
ATOM   3925 O  O   . GLU B 1 54  ? 67.525 -75.017 1.391   1.00 27.99  ?  54  GLU B O   1 
ATOM   3926 C  CB  . GLU B 1 54  ? 68.749 -74.626 -1.416  1.00 28.81  ?  54  GLU B CB  1 
ATOM   3927 C  CG  . GLU B 1 54  ? 68.935 -75.988 -2.076  1.00 31.45  ?  54  GLU B CG  1 
ATOM   3928 C  CD  . GLU B 1 54  ? 70.304 -76.152 -2.724  1.00 34.02  ?  54  GLU B CD  1 
ATOM   3929 O  OE1 . GLU B 1 54  ? 71.094 -75.163 -2.717  1.00 31.51  ?  54  GLU B OE1 1 
ATOM   3930 O  OE2 . GLU B 1 54  ? 70.567 -77.268 -3.245  1.00 31.93  -1 54  GLU B OE2 1 
ATOM   3931 N  N   . ASN B 1 55  ? 66.266 -76.337 0.068   1.00 24.78  ?  55  ASN B N   1 
ATOM   3932 C  CA  . ASN B 1 55  ? 65.989 -77.304 1.121   1.00 23.68  ?  55  ASN B CA  1 
ATOM   3933 C  C   . ASN B 1 55  ? 67.036 -78.417 1.064   1.00 26.90  ?  55  ASN B C   1 
ATOM   3934 O  O   . ASN B 1 55  ? 67.809 -78.511 0.114   1.00 25.55  ?  55  ASN B O   1 
ATOM   3935 C  CB  . ASN B 1 55  ? 64.578 -77.872 0.995   1.00 24.29  ?  55  ASN B CB  1 
ATOM   3936 C  CG  . ASN B 1 55  ? 64.421 -78.747 -0.227  1.00 24.03  ?  55  ASN B CG  1 
ATOM   3937 O  OD1 . ASN B 1 55  ? 65.419 -79.286 -0.718  1.00 27.80  ?  55  ASN B OD1 1 
ATOM   3938 N  ND2 . ASN B 1 55  ? 63.209 -78.905 -0.742  1.00 20.51  ?  55  ASN B ND2 1 
ATOM   3939 N  N   . ASP B 1 56  ? 67.010 -79.322 2.050   1.00 30.06  ?  56  ASP B N   1 
ATOM   3940 C  CA  . ASP B 1 56  ? 68.013 -80.372 2.154   1.00 30.29  ?  56  ASP B CA  1 
ATOM   3941 C  C   . ASP B 1 56  ? 67.923 -81.359 0.983   1.00 31.93  ?  56  ASP B C   1 
ATOM   3942 O  O   . ASP B 1 56  ? 68.880 -82.102 0.759   1.00 31.83  ?  56  ASP B O   1 
ATOM   3943 C  CB  . ASP B 1 56  ? 67.963 -81.075 3.503   1.00 30.95  ?  56  ASP B CB  1 
ATOM   3944 C  CG  . ASP B 1 56  ? 67.742 -80.180 4.715   1.00 30.31  ?  56  ASP B CG  1 
ATOM   3945 O  OD1 . ASP B 1 56  ? 67.043 -80.602 5.651   1.00 34.53  ?  56  ASP B OD1 1 
ATOM   3946 O  OD2 . ASP B 1 56  ? 68.252 -79.066 4.711   1.00 29.60  -1 56  ASP B OD2 1 
ATOM   3947 N  N   . LYS B 1 57  ? 66.791 -81.381 0.254   1.00 32.16  ?  57  LYS B N   1 
ATOM   3948 C  CA  . LYS B 1 57  ? 66.632 -82.244 -0.913  1.00 34.31  ?  57  LYS B CA  1 
ATOM   3949 C  C   . LYS B 1 57  ? 67.206 -81.555 -2.155  1.00 36.62  ?  57  LYS B C   1 
ATOM   3950 O  O   . LYS B 1 57  ? 67.406 -82.204 -3.183  1.00 34.00  ?  57  LYS B O   1 
ATOM   3951 C  CB  . LYS B 1 57  ? 65.172 -82.676 -1.137  1.00 35.89  ?  57  LYS B CB  1 
ATOM   3952 C  CG  . LYS B 1 57  ? 64.598 -83.667 -0.115  1.00 39.25  ?  57  LYS B CG  1 
ATOM   3953 C  CD  . LYS B 1 57  ? 63.621 -84.712 -0.655  1.00 41.99  ?  57  LYS B CD  1 
ATOM   3954 C  CE  . LYS B 1 57  ? 62.170 -84.309 -0.682  1.00 42.36  ?  57  LYS B CE  1 
ATOM   3955 N  NZ  . LYS B 1 57  ? 61.443 -85.009 -1.755  1.00 42.03  1  57  LYS B NZ  1 
ATOM   3956 N  N   . GLY B 1 58  ? 67.461 -80.240 -2.040  1.00 38.05  ?  58  GLY B N   1 
ATOM   3957 C  CA  . GLY B 1 58  ? 68.179 -79.470 -3.046  1.00 34.43  ?  58  GLY B CA  1 
ATOM   3958 C  C   . GLY B 1 58  ? 67.223 -78.725 -3.969  1.00 36.50  ?  58  GLY B C   1 
ATOM   3959 O  O   . GLY B 1 58  ? 67.638 -78.262 -5.024  1.00 37.19  ?  58  GLY B O   1 
ATOM   3960 N  N   . GLU B 1 59  ? 65.958 -78.576 -3.547  1.00 37.70  ?  59  GLU B N   1 
ATOM   3961 C  CA  . GLU B 1 59  ? 64.934 -77.927 -4.354  1.00 38.15  ?  59  GLU B CA  1 
ATOM   3962 C  C   . GLU B 1 59  ? 64.813 -76.438 -4.022  1.00 39.31  ?  59  GLU B C   1 
ATOM   3963 O  O   . GLU B 1 59  ? 64.834 -76.050 -2.849  1.00 35.58  ?  59  GLU B O   1 
ATOM   3964 C  CB  . GLU B 1 59  ? 63.581 -78.588 -4.100  1.00 40.73  ?  59  GLU B CB  1 
ATOM   3965 C  CG  . GLU B 1 59  ? 63.554 -80.072 -4.451  1.00 43.85  ?  59  GLU B CG  1 
ATOM   3966 C  CD  . GLU B 1 59  ? 62.494 -80.863 -3.706  1.00 47.92  ?  59  GLU B CD  1 
ATOM   3967 O  OE1 . GLU B 1 59  ? 61.684 -80.232 -2.987  1.00 46.20  ?  59  GLU B OE1 1 
ATOM   3968 O  OE2 . GLU B 1 59  ? 62.502 -82.111 -3.819  1.00 47.29  -1 59  GLU B OE2 1 
ATOM   3969 N  N   . VAL B 1 60  ? 64.659 -75.624 -5.082  1.00 40.96  ?  60  VAL B N   1 
ATOM   3970 C  CA  . VAL B 1 60  ? 64.369 -74.202 -4.977  1.00 38.60  ?  60  VAL B CA  1 
ATOM   3971 C  C   . VAL B 1 60  ? 63.108 -74.037 -4.142  1.00 37.47  ?  60  VAL B C   1 
ATOM   3972 O  O   . VAL B 1 60  ? 62.159 -74.767 -4.357  1.00 38.28  ?  60  VAL B O   1 
ATOM   3973 C  CB  . VAL B 1 60  ? 64.187 -73.539 -6.356  1.00 41.34  ?  60  VAL B CB  1 
ATOM   3974 C  CG1 . VAL B 1 60  ? 63.032 -74.108 -7.163  1.00 39.60  ?  60  VAL B CG1 1 
ATOM   3975 C  CG2 . VAL B 1 60  ? 63.994 -72.041 -6.222  1.00 49.90  ?  60  VAL B CG2 1 
ATOM   3976 N  N   . GLN B 1 61  ? 63.142 -73.113 -3.173  1.00 37.47  ?  61  GLN B N   1 
ATOM   3977 C  CA  . GLN B 1 61  ? 61.990 -72.707 -2.380  1.00 33.49  ?  61  GLN B CA  1 
ATOM   3978 C  C   . GLN B 1 61  ? 61.864 -71.179 -2.448  1.00 33.28  ?  61  GLN B C   1 
ATOM   3979 O  O   . GLN B 1 61  ? 62.854 -70.489 -2.687  1.00 34.50  ?  61  GLN B O   1 
ATOM   3980 C  CB  . GLN B 1 61  ? 62.200 -73.128 -0.925  1.00 32.53  ?  61  GLN B CB  1 
ATOM   3981 C  CG  . GLN B 1 61  ? 62.422 -74.625 -0.717  1.00 35.05  ?  61  GLN B CG  1 
ATOM   3982 C  CD  . GLN B 1 61  ? 61.264 -75.489 -1.169  1.00 32.28  ?  61  GLN B CD  1 
ATOM   3983 O  OE1 . GLN B 1 61  ? 61.443 -76.451 -1.911  1.00 36.20  ?  61  GLN B OE1 1 
ATOM   3984 N  NE2 . GLN B 1 61  ? 60.062 -75.172 -0.725  1.00 30.32  ?  61  GLN B NE2 1 
ATOM   3985 N  N   . VAL B 1 62  ? 60.663 -70.638 -2.201  1.00 27.48  ?  62  VAL B N   1 
ATOM   3986 C  CA  . VAL B 1 62  ? 60.490 -69.200 -2.224  1.00 27.11  ?  62  VAL B CA  1 
ATOM   3987 C  C   . VAL B 1 62  ? 59.426 -68.773 -1.206  1.00 28.11  ?  62  VAL B C   1 
ATOM   3988 O  O   . VAL B 1 62  ? 58.299 -69.267 -1.197  1.00 25.27  ?  62  VAL B O   1 
ATOM   3989 C  CB  . VAL B 1 62  ? 60.178 -68.707 -3.654  1.00 26.65  ?  62  VAL B CB  1 
ATOM   3990 C  CG1 . VAL B 1 62  ? 59.070 -69.511 -4.309  1.00 27.41  ?  62  VAL B CG1 1 
ATOM   3991 C  CG2 . VAL B 1 62  ? 59.864 -67.209 -3.713  1.00 25.92  ?  62  VAL B CG2 1 
ATOM   3992 N  N   . ASN B 1 63  ? 59.798 -67.795 -0.368  1.00 27.22  ?  63  ASN B N   1 
ATOM   3993 C  CA  . ASN B 1 63  ? 58.886 -67.174 0.575   1.00 24.03  ?  63  ASN B CA  1 
ATOM   3994 C  C   . ASN B 1 63  ? 58.900 -65.679 0.323   1.00 25.61  ?  63  ASN B C   1 
ATOM   3995 O  O   . ASN B 1 63  ? 59.729 -65.234 -0.454  1.00 28.66  ?  63  ASN B O   1 
ATOM   3996 C  CB  . ASN B 1 63  ? 59.307 -67.485 1.999   1.00 20.98  ?  63  ASN B CB  1 
ATOM   3997 C  CG  . ASN B 1 63  ? 58.962 -68.910 2.321   1.00 20.36  ?  63  ASN B CG  1 
ATOM   3998 O  OD1 . ASN B 1 63  ? 59.764 -69.821 2.067   1.00 18.02  ?  63  ASN B OD1 1 
ATOM   3999 N  ND2 . ASN B 1 63  ? 57.739 -69.111 2.796   1.00 20.92  ?  63  ASN B ND2 1 
ATOM   4000 N  N   . ARG B 1 64  ? 58.037 -64.929 1.023   1.00 28.83  ?  64  ARG B N   1 
ATOM   4001 C  CA  . ARG B 1 64  ? 58.086 -63.471 1.033   1.00 29.68  ?  64  ARG B CA  1 
ATOM   4002 C  C   . ARG B 1 64  ? 58.750 -62.986 2.323   1.00 28.89  ?  64  ARG B C   1 
ATOM   4003 O  O   . ARG B 1 64  ? 58.568 -63.553 3.399   1.00 30.43  ?  64  ARG B O   1 
ATOM   4004 C  CB  . ARG B 1 64  ? 56.684 -62.894 0.799   1.00 31.72  ?  64  ARG B CB  1 
ATOM   4005 C  CG  . ARG B 1 64  ? 55.969 -63.596 -0.351  1.00 33.96  ?  64  ARG B CG  1 
ATOM   4006 C  CD  . ARG B 1 64  ? 55.184 -62.643 -1.246  1.00 34.36  ?  64  ARG B CD  1 
ATOM   4007 N  NE  . ARG B 1 64  ? 54.350 -63.209 -2.317  1.00 33.73  ?  64  ARG B NE  1 
ATOM   4008 C  CZ  . ARG B 1 64  ? 54.270 -64.449 -2.791  1.00 35.08  ?  64  ARG B CZ  1 
ATOM   4009 N  NH1 . ARG B 1 64  ? 55.060 -65.425 -2.374  1.00 34.58  1  64  ARG B NH1 1 
ATOM   4010 N  NH2 . ARG B 1 64  ? 53.380 -64.707 -3.734  1.00 36.97  ?  64  ARG B NH2 1 
ATOM   4011 N  N   . GLY B 1 65  ? 59.577 -61.953 2.179   1.00 28.17  ?  65  GLY B N   1 
ATOM   4012 C  CA  . GLY B 1 65  ? 60.106 -61.209 3.307   1.00 27.28  ?  65  GLY B CA  1 
ATOM   4013 C  C   . GLY B 1 65  ? 59.447 -59.841 3.360   1.00 27.32  ?  65  GLY B C   1 
ATOM   4014 O  O   . GLY B 1 65  ? 58.994 -59.344 2.334   1.00 30.64  ?  65  GLY B O   1 
ATOM   4015 N  N   . PHE B 1 66  ? 59.359 -59.292 4.571   1.00 27.08  ?  66  PHE B N   1 
ATOM   4016 C  CA  . PHE B 1 66  ? 58.760 -57.995 4.835   1.00 28.64  ?  66  PHE B CA  1 
ATOM   4017 C  C   . PHE B 1 66  ? 59.575 -57.336 5.953   1.00 32.04  ?  66  PHE B C   1 
ATOM   4018 O  O   . PHE B 1 66  ? 60.005 -58.035 6.884   1.00 35.70  ?  66  PHE B O   1 
ATOM   4019 C  CB  . PHE B 1 66  ? 57.303 -58.115 5.321   1.00 27.23  ?  66  PHE B CB  1 
ATOM   4020 C  CG  . PHE B 1 66  ? 56.333 -58.977 4.521   1.00 25.01  ?  66  PHE B CG  1 
ATOM   4021 C  CD1 . PHE B 1 66  ? 56.443 -60.365 4.522   1.00 23.56  ?  66  PHE B CD1 1 
ATOM   4022 C  CD2 . PHE B 1 66  ? 55.282 -58.400 3.808   1.00 25.92  ?  66  PHE B CD2 1 
ATOM   4023 C  CE1 . PHE B 1 66  ? 55.558 -61.154 3.803   1.00 23.21  ?  66  PHE B CE1 1 
ATOM   4024 C  CE2 . PHE B 1 66  ? 54.402 -59.189 3.075   1.00 24.47  ?  66  PHE B CE2 1 
ATOM   4025 C  CZ  . PHE B 1 66  ? 54.546 -60.562 3.070   1.00 24.08  ?  66  PHE B CZ  1 
ATOM   4026 N  N   . ARG B 1 67  ? 59.779 -56.007 5.871   1.00 29.75  ?  67  ARG B N   1 
ATOM   4027 C  CA  . ARG B 1 67  ? 60.229 -55.221 7.013   1.00 28.22  ?  67  ARG B CA  1 
ATOM   4028 C  C   . ARG B 1 67  ? 59.473 -53.902 7.016   1.00 28.77  ?  67  ARG B C   1 
ATOM   4029 O  O   . ARG B 1 67  ? 59.706 -53.067 6.142   1.00 31.34  ?  67  ARG B O   1 
ATOM   4030 C  CB  . ARG B 1 67  ? 61.728 -54.909 7.021   1.00 31.94  ?  67  ARG B CB  1 
ATOM   4031 C  CG  . ARG B 1 67  ? 62.252 -54.200 8.270   1.00 33.72  ?  67  ARG B CG  1 
ATOM   4032 C  CD  . ARG B 1 67  ? 61.990 -54.958 9.575   1.00 33.87  ?  67  ARG B CD  1 
ATOM   4033 N  NE  . ARG B 1 67  ? 62.439 -54.223 10.764  1.00 33.77  ?  67  ARG B NE  1 
ATOM   4034 C  CZ  . ARG B 1 67  ? 62.236 -54.604 12.032  1.00 36.93  ?  67  ARG B CZ  1 
ATOM   4035 N  NH1 . ARG B 1 67  ? 61.535 -55.692 12.309  1.00 36.93  1  67  ARG B NH1 1 
ATOM   4036 N  NH2 . ARG B 1 67  ? 62.731 -53.892 13.035  1.00 37.17  ?  67  ARG B NH2 1 
ATOM   4037 N  N   . VAL B 1 68  ? 58.517 -53.771 7.955   1.00 26.51  ?  68  VAL B N   1 
ATOM   4038 C  CA  . VAL B 1 68  ? 57.773 -52.542 8.149   1.00 24.14  ?  68  VAL B CA  1 
ATOM   4039 C  C   . VAL B 1 68  ? 58.628 -51.657 9.045   1.00 25.64  ?  68  VAL B C   1 
ATOM   4040 O  O   . VAL B 1 68  ? 58.907 -52.063 10.172  1.00 25.36  ?  68  VAL B O   1 
ATOM   4041 C  CB  . VAL B 1 68  ? 56.385 -52.771 8.766   1.00 22.79  ?  68  VAL B CB  1 
ATOM   4042 C  CG1 . VAL B 1 68  ? 55.639 -51.470 9.011   1.00 20.90  ?  68  VAL B CG1 1 
ATOM   4043 C  CG2 . VAL B 1 68  ? 55.543 -53.693 7.898   1.00 25.31  ?  68  VAL B CG2 1 
ATOM   4044 N  N   . GLN B 1 69  ? 59.039 -50.489 8.511   1.00 22.48  ?  69  GLN B N   1 
ATOM   4045 C  CA  . GLN B 1 69  ? 59.770 -49.478 9.247   1.00 20.85  ?  69  GLN B CA  1 
ATOM   4046 C  C   . GLN B 1 69  ? 58.829 -48.297 9.466   1.00 22.47  ?  69  GLN B C   1 
ATOM   4047 O  O   . GLN B 1 69  ? 58.777 -47.392 8.628   1.00 22.60  ?  69  GLN B O   1 
ATOM   4048 C  CB  . GLN B 1 69  ? 61.015 -49.095 8.446   1.00 20.13  ?  69  GLN B CB  1 
ATOM   4049 C  CG  . GLN B 1 69  ? 61.911 -50.277 8.095   1.00 18.86  ?  69  GLN B CG  1 
ATOM   4050 C  CD  . GLN B 1 69  ? 63.202 -49.890 7.396   1.00 18.30  ?  69  GLN B CD  1 
ATOM   4051 O  OE1 . GLN B 1 69  ? 63.214 -49.096 6.452   1.00 17.77  ?  69  GLN B OE1 1 
ATOM   4052 N  NE2 . GLN B 1 69  ? 64.313 -50.479 7.822   1.00 18.44  ?  69  GLN B NE2 1 
ATOM   4053 N  N   . PHE B 1 70  ? 58.115 -48.324 10.608  1.00 22.97  ?  70  PHE B N   1 
ATOM   4054 C  CA  . PHE B 1 70  ? 56.907 -47.539 10.829  1.00 23.17  ?  70  PHE B CA  1 
ATOM   4055 C  C   . PHE B 1 70  ? 57.260 -46.104 11.229  1.00 25.49  ?  70  PHE B C   1 
ATOM   4056 O  O   . PHE B 1 70  ? 56.806 -45.155 10.593  1.00 24.72  ?  70  PHE B O   1 
ATOM   4057 C  CB  . PHE B 1 70  ? 56.026 -48.263 11.861  1.00 23.85  ?  70  PHE B CB  1 
ATOM   4058 C  CG  . PHE B 1 70  ? 54.538 -48.288 11.512  1.00 25.23  ?  70  PHE B CG  1 
ATOM   4059 C  CD1 . PHE B 1 70  ? 53.857 -49.491 11.386  1.00 25.58  ?  70  PHE B CD1 1 
ATOM   4060 C  CD2 . PHE B 1 70  ? 53.824 -47.113 11.284  1.00 24.99  ?  70  PHE B CD2 1 
ATOM   4061 C  CE1 . PHE B 1 70  ? 52.513 -49.503 11.038  1.00 26.87  ?  70  PHE B CE1 1 
ATOM   4062 C  CE2 . PHE B 1 70  ? 52.477 -47.131 10.956  1.00 24.14  ?  70  PHE B CE2 1 
ATOM   4063 C  CZ  . PHE B 1 70  ? 51.826 -48.320 10.830  1.00 25.82  ?  70  PHE B CZ  1 
ATOM   4064 N  N   . ASN B 1 71  ? 58.029 -45.938 12.316  1.00 28.80  ?  71  ASN B N   1 
ATOM   4065 C  CA  . ASN B 1 71  ? 58.261 -44.619 12.903  1.00 29.91  ?  71  ASN B CA  1 
ATOM   4066 C  C   . ASN B 1 71  ? 59.661 -44.578 13.484  1.00 28.68  ?  71  ASN B C   1 
ATOM   4067 O  O   . ASN B 1 71  ? 60.019 -45.534 14.171  1.00 30.08  ?  71  ASN B O   1 
ATOM   4068 C  CB  . ASN B 1 71  ? 57.335 -44.260 14.069  1.00 28.49  ?  71  ASN B CB  1 
ATOM   4069 C  CG  . ASN B 1 71  ? 57.149 -42.759 14.171  1.00 30.64  ?  71  ASN B CG  1 
ATOM   4070 O  OD1 . ASN B 1 71  ? 57.841 -42.057 14.917  1.00 27.88  ?  71  ASN B OD1 1 
ATOM   4071 N  ND2 . ASN B 1 71  ? 56.240 -42.227 13.372  1.00 35.86  ?  71  ASN B ND2 1 
ATOM   4072 N  N   . SER B 1 72  ? 60.386 -43.473 13.222  1.00 26.72  ?  72  SER B N   1 
ATOM   4073 C  CA  . SER B 1 72  ? 61.767 -43.302 13.644  1.00 27.47  ?  72  SER B CA  1 
ATOM   4074 C  C   . SER B 1 72  ? 61.992 -41.924 14.280  1.00 25.66  ?  72  SER B C   1 
ATOM   4075 O  O   . SER B 1 72  ? 63.128 -41.475 14.460  1.00 27.98  ?  72  SER B O   1 
ATOM   4076 C  CB  . SER B 1 72  ? 62.704 -43.556 12.475  1.00 31.46  ?  72  SER B CB  1 
ATOM   4077 O  OG  . SER B 1 72  ? 62.553 -42.590 11.439  1.00 36.67  ?  72  SER B OG  1 
ATOM   4078 N  N   . ALA B 1 73  ? 60.899 -41.286 14.688  1.00 22.83  ?  73  ALA B N   1 
ATOM   4079 C  CA  . ALA B 1 73  ? 60.934 -39.988 15.322  1.00 22.39  ?  73  ALA B CA  1 
ATOM   4080 C  C   . ALA B 1 73  ? 61.687 -40.023 16.663  1.00 25.10  ?  73  ALA B C   1 
ATOM   4081 O  O   . ALA B 1 73  ? 62.408 -39.071 16.985  1.00 24.71  ?  73  ALA B O   1 
ATOM   4082 C  CB  . ALA B 1 73  ? 59.503 -39.521 15.463  1.00 22.18  ?  73  ALA B CB  1 
ATOM   4083 N  N   . LEU B 1 74  ? 61.520 -41.101 17.455  1.00 25.41  ?  74  LEU B N   1 
ATOM   4084 C  CA  . LEU B 1 74  ? 62.161 -41.203 18.770  1.00 25.22  ?  74  LEU B CA  1 
ATOM   4085 C  C   . LEU B 1 74  ? 63.482 -41.980 18.746  1.00 24.55  ?  74  LEU B C   1 
ATOM   4086 O  O   . LEU B 1 74  ? 64.190 -41.952 19.753  1.00 21.96  ?  74  LEU B O   1 
ATOM   4087 C  CB  . LEU B 1 74  ? 61.195 -41.821 19.784  1.00 24.68  ?  74  LEU B CB  1 
ATOM   4088 C  CG  . LEU B 1 74  ? 59.977 -40.957 20.139  1.00 26.09  ?  74  LEU B CG  1 
ATOM   4089 C  CD1 . LEU B 1 74  ? 58.994 -41.666 21.040  1.00 24.55  ?  74  LEU B CD1 1 
ATOM   4090 C  CD2 . LEU B 1 74  ? 60.385 -39.655 20.815  1.00 26.78  ?  74  LEU B CD2 1 
ATOM   4091 N  N   . GLY B 1 75  ? 63.784 -42.693 17.640  1.00 24.50  ?  75  GLY B N   1 
ATOM   4092 C  CA  . GLY B 1 75  ? 64.982 -43.521 17.529  1.00 24.30  ?  75  GLY B CA  1 
ATOM   4093 C  C   . GLY B 1 75  ? 65.049 -44.363 16.244  1.00 24.33  ?  75  GLY B C   1 
ATOM   4094 O  O   . GLY B 1 75  ? 64.145 -44.342 15.400  1.00 23.17  ?  75  GLY B O   1 
ATOM   4095 N  N   . PRO B 1 76  ? 66.117 -45.184 16.055  1.00 22.22  ?  76  PRO B N   1 
ATOM   4096 C  CA  . PRO B 1 76  ? 66.115 -46.172 14.978  1.00 20.93  ?  76  PRO B CA  1 
ATOM   4097 C  C   . PRO B 1 76  ? 64.901 -47.088 15.129  1.00 20.48  ?  76  PRO B C   1 
ATOM   4098 O  O   . PRO B 1 76  ? 64.483 -47.390 16.233  1.00 17.03  ?  76  PRO B O   1 
ATOM   4099 C  CB  . PRO B 1 76  ? 67.438 -46.944 15.090  1.00 19.83  ?  76  PRO B CB  1 
ATOM   4100 C  CG  . PRO B 1 76  ? 68.053 -46.487 16.412  1.00 20.39  ?  76  PRO B CG  1 
ATOM   4101 C  CD  . PRO B 1 76  ? 67.334 -45.236 16.881  1.00 20.53  ?  76  PRO B CD  1 
ATOM   4102 N  N   . TYR B 1 77  ? 64.369 -47.532 13.984  1.00 24.17  ?  77  TYR B N   1 
ATOM   4103 C  CA  . TYR B 1 77  ? 63.358 -48.575 13.903  1.00 24.76  ?  77  TYR B CA  1 
ATOM   4104 C  C   . TYR B 1 77  ? 63.750 -49.706 14.848  1.00 25.14  ?  77  TYR B C   1 
ATOM   4105 O  O   . TYR B 1 77  ? 64.908 -50.096 14.888  1.00 24.01  ?  77  TYR B O   1 
ATOM   4106 C  CB  . TYR B 1 77  ? 63.208 -49.047 12.451  1.00 24.24  ?  77  TYR B CB  1 
ATOM   4107 C  CG  . TYR B 1 77  ? 62.831 -47.916 11.506  1.00 24.08  ?  77  TYR B CG  1 
ATOM   4108 C  CD1 . TYR B 1 77  ? 63.785 -47.317 10.686  1.00 24.86  ?  77  TYR B CD1 1 
ATOM   4109 C  CD2 . TYR B 1 77  ? 61.536 -47.418 11.477  1.00 22.39  ?  77  TYR B CD2 1 
ATOM   4110 C  CE1 . TYR B 1 77  ? 63.459 -46.256 9.852   1.00 26.55  ?  77  TYR B CE1 1 
ATOM   4111 C  CE2 . TYR B 1 77  ? 61.198 -46.362 10.646  1.00 24.53  ?  77  TYR B CE2 1 
ATOM   4112 C  CZ  . TYR B 1 77  ? 62.161 -45.766 9.838   1.00 25.89  ?  77  TYR B CZ  1 
ATOM   4113 O  OH  . TYR B 1 77  ? 61.812 -44.714 9.020   1.00 20.92  ?  77  TYR B OH  1 
ATOM   4114 N  N   . LYS B 1 78  ? 62.778 -50.161 15.645  1.00 27.49  ?  78  LYS B N   1 
ATOM   4115 C  CA  . LYS B 1 78  ? 62.968 -51.242 16.595  1.00 29.58  ?  78  LYS B CA  1 
ATOM   4116 C  C   . LYS B 1 78  ? 61.672 -52.040 16.573  1.00 28.12  ?  78  LYS B C   1 
ATOM   4117 O  O   . LYS B 1 78  ? 60.610 -51.439 16.506  1.00 34.72  ?  78  LYS B O   1 
ATOM   4118 C  CB  . LYS B 1 78  ? 63.244 -50.668 17.996  1.00 31.41  ?  78  LYS B CB  1 
ATOM   4119 C  CG  . LYS B 1 78  ? 64.388 -51.257 18.838  1.00 30.27  ?  78  LYS B CG  1 
ATOM   4120 C  CD  . LYS B 1 78  ? 64.959 -52.566 18.311  1.00 31.41  ?  78  LYS B CD  1 
ATOM   4121 C  CE  . LYS B 1 78  ? 65.693 -53.388 19.314  1.00 32.28  ?  78  LYS B CE  1 
ATOM   4122 N  NZ  . LYS B 1 78  ? 65.288 -54.785 19.197  1.00 32.99  1  78  LYS B NZ  1 
ATOM   4123 N  N   . GLY B 1 79  ? 61.775 -53.365 16.601  1.00 25.07  ?  79  GLY B N   1 
ATOM   4124 C  CA  . GLY B 1 79  ? 60.688 -54.254 16.245  1.00 25.67  ?  79  GLY B CA  1 
ATOM   4125 C  C   . GLY B 1 79  ? 61.198 -55.682 16.349  1.00 28.93  ?  79  GLY B C   1 
ATOM   4126 O  O   . GLY B 1 79  ? 62.086 -55.922 17.150  1.00 43.13  ?  79  GLY B O   1 
ATOM   4127 N  N   . GLY B 1 80  ? 60.681 -56.608 15.542  1.00 28.28  ?  80  GLY B N   1 
ATOM   4128 C  CA  . GLY B 1 80  ? 61.012 -58.020 15.676  1.00 28.43  ?  80  GLY B CA  1 
ATOM   4129 C  C   . GLY B 1 80  ? 60.802 -58.758 14.359  1.00 28.41  ?  80  GLY B C   1 
ATOM   4130 O  O   . GLY B 1 80  ? 60.119 -58.266 13.467  1.00 31.19  ?  80  GLY B O   1 
ATOM   4131 N  N   . LEU B 1 81  ? 61.400 -59.938 14.222  1.00 27.90  ?  81  LEU B N   1 
ATOM   4132 C  CA  . LEU B 1 81  ? 61.172 -60.737 13.030  1.00 27.41  ?  81  LEU B CA  1 
ATOM   4133 C  C   . LEU B 1 81  ? 60.318 -61.944 13.426  1.00 28.68  ?  81  LEU B C   1 
ATOM   4134 O  O   . LEU B 1 81  ? 60.619 -62.596 14.415  1.00 28.80  ?  81  LEU B O   1 
ATOM   4135 C  CB  . LEU B 1 81  ? 62.521 -61.098 12.401  1.00 25.20  ?  81  LEU B CB  1 
ATOM   4136 C  CG  . LEU B 1 81  ? 63.436 -59.906 12.078  1.00 22.70  ?  81  LEU B CG  1 
ATOM   4137 C  CD1 . LEU B 1 81  ? 64.767 -60.351 11.519  1.00 20.49  ?  81  LEU B CD1 1 
ATOM   4138 C  CD2 . LEU B 1 81  ? 62.754 -58.914 11.127  1.00 22.89  ?  81  LEU B CD2 1 
ATOM   4139 N  N   . ARG B 1 82  ? 59.198 -62.152 12.711  1.00 29.97  ?  82  ARG B N   1 
ATOM   4140 C  CA  . ARG B 1 82  ? 58.305 -63.273 12.930  1.00 30.80  ?  82  ARG B CA  1 
ATOM   4141 C  C   . ARG B 1 82  ? 58.323 -64.211 11.727  1.00 29.11  ?  82  ARG B C   1 
ATOM   4142 O  O   . ARG B 1 82  ? 57.911 -63.810 10.641  1.00 31.15  ?  82  ARG B O   1 
ATOM   4143 C  CB  . ARG B 1 82  ? 56.869 -62.765 13.095  1.00 34.25  ?  82  ARG B CB  1 
ATOM   4144 C  CG  . ARG B 1 82  ? 55.868 -63.912 13.136  1.00 39.82  ?  82  ARG B CG  1 
ATOM   4145 C  CD  . ARG B 1 82  ? 54.559 -63.622 13.835  1.00 41.42  ?  82  ARG B CD  1 
ATOM   4146 N  NE  . ARG B 1 82  ? 54.783 -63.096 15.183  1.00 46.36  ?  82  ARG B NE  1 
ATOM   4147 C  CZ  . ARG B 1 82  ? 53.804 -62.632 15.938  1.00 53.34  ?  82  ARG B CZ  1 
ATOM   4148 N  NH1 . ARG B 1 82  ? 52.555 -62.790 15.532  1.00 52.20  1  82  ARG B NH1 1 
ATOM   4149 N  NH2 . ARG B 1 82  ? 54.070 -62.051 17.103  1.00 54.92  ?  82  ARG B NH2 1 
ATOM   4150 N  N   . PHE B 1 83  ? 58.769 -65.456 11.928  1.00 26.87  ?  83  PHE B N   1 
ATOM   4151 C  CA  . PHE B 1 83  ? 58.665 -66.473 10.894  1.00 28.26  ?  83  PHE B CA  1 
ATOM   4152 C  C   . PHE B 1 83  ? 57.454 -67.343 11.200  1.00 29.12  ?  83  PHE B C   1 
ATOM   4153 O  O   . PHE B 1 83  ? 57.537 -68.233 12.044  1.00 31.18  ?  83  PHE B O   1 
ATOM   4154 C  CB  . PHE B 1 83  ? 59.930 -67.337 10.781  1.00 27.31  ?  83  PHE B CB  1 
ATOM   4155 C  CG  . PHE B 1 83  ? 61.198 -66.576 10.414  1.00 23.57  ?  83  PHE B CG  1 
ATOM   4156 C  CD1 . PHE B 1 83  ? 62.445 -67.195 10.493  1.00 21.48  ?  83  PHE B CD1 1 
ATOM   4157 C  CD2 . PHE B 1 83  ? 61.143 -65.236 10.034  1.00 21.06  ?  83  PHE B CD2 1 
ATOM   4158 C  CE1 . PHE B 1 83  ? 63.596 -66.506 10.171  1.00 20.71  ?  83  PHE B CE1 1 
ATOM   4159 C  CE2 . PHE B 1 83  ? 62.300 -64.551 9.718   1.00 20.91  ?  83  PHE B CE2 1 
ATOM   4160 C  CZ  . PHE B 1 83  ? 63.523 -65.185 9.788   1.00 20.73  ?  83  PHE B CZ  1 
ATOM   4161 N  N   . HIS B 1 84  ? 56.348 -67.082 10.492  1.00 31.06  ?  84  HIS B N   1 
ATOM   4162 C  CA  . HIS B 1 84  ? 55.111 -67.824 10.669  1.00 33.58  ?  84  HIS B CA  1 
ATOM   4163 C  C   . HIS B 1 84  ? 54.305 -67.744 9.382   1.00 35.32  ?  84  HIS B C   1 
ATOM   4164 O  O   . HIS B 1 84  ? 54.149 -66.654 8.843   1.00 35.53  ?  84  HIS B O   1 
ATOM   4165 C  CB  . HIS B 1 84  ? 54.275 -67.274 11.831  1.00 36.13  ?  84  HIS B CB  1 
ATOM   4166 C  CG  . HIS B 1 84  ? 53.193 -68.226 12.244  1.00 43.07  ?  84  HIS B CG  1 
ATOM   4167 N  ND1 . HIS B 1 84  ? 51.884 -68.082 11.838  1.00 45.30  ?  84  HIS B ND1 1 
ATOM   4168 C  CD2 . HIS B 1 84  ? 53.231 -69.348 12.987  1.00 44.52  ?  84  HIS B CD2 1 
ATOM   4169 C  CE1 . HIS B 1 84  ? 51.162 -69.074 12.330  1.00 48.01  ?  84  HIS B CE1 1 
ATOM   4170 N  NE2 . HIS B 1 84  ? 51.961 -69.859 13.025  1.00 50.36  ?  84  HIS B NE2 1 
ATOM   4171 N  N   . PRO B 1 85  ? 53.689 -68.864 8.921   1.00 37.73  ?  85  PRO B N   1 
ATOM   4172 C  CA  . PRO B 1 85  ? 53.027 -68.913 7.611   1.00 34.29  ?  85  PRO B CA  1 
ATOM   4173 C  C   . PRO B 1 85  ? 51.750 -68.086 7.512   1.00 30.31  ?  85  PRO B C   1 
ATOM   4174 O  O   . PRO B 1 85  ? 51.217 -67.896 6.418   1.00 32.17  ?  85  PRO B O   1 
ATOM   4175 C  CB  . PRO B 1 85  ? 52.742 -70.418 7.449   1.00 35.11  ?  85  PRO B CB  1 
ATOM   4176 C  CG  . PRO B 1 85  ? 52.509 -70.883 8.860   1.00 34.98  ?  85  PRO B CG  1 
ATOM   4177 C  CD  . PRO B 1 85  ? 53.534 -70.124 9.677   1.00 36.37  ?  85  PRO B CD  1 
ATOM   4178 N  N   . SER B 1 86  ? 51.293 -67.598 8.669   1.00 26.75  ?  86  SER B N   1 
ATOM   4179 C  CA  . SER B 1 86  ? 50.187 -66.660 8.775   1.00 27.17  ?  86  SER B CA  1 
ATOM   4180 C  C   . SER B 1 86  ? 50.544 -65.262 8.258   1.00 27.59  ?  86  SER B C   1 
ATOM   4181 O  O   . SER B 1 86  ? 49.624 -64.506 7.934   1.00 26.55  ?  86  SER B O   1 
ATOM   4182 C  CB  . SER B 1 86  ? 49.720 -66.571 10.228  1.00 28.36  ?  86  SER B CB  1 
ATOM   4183 O  OG  . SER B 1 86  ? 50.560 -65.757 11.052  1.00 25.33  ?  86  SER B OG  1 
ATOM   4184 N  N   . VAL B 1 87  ? 51.861 -64.935 8.241   1.00 27.14  ?  87  VAL B N   1 
ATOM   4185 C  CA  . VAL B 1 87  ? 52.420 -63.581 8.194   1.00 24.57  ?  87  VAL B CA  1 
ATOM   4186 C  C   . VAL B 1 87  ? 52.092 -62.883 6.877   1.00 22.75  ?  87  VAL B C   1 
ATOM   4187 O  O   . VAL B 1 87  ? 52.143 -63.490 5.817   1.00 22.97  ?  87  VAL B O   1 
ATOM   4188 C  CB  . VAL B 1 87  ? 53.956 -63.578 8.403   1.00 25.37  ?  87  VAL B CB  1 
ATOM   4189 C  CG1 . VAL B 1 87  ? 54.635 -62.403 7.706   1.00 24.17  ?  87  VAL B CG1 1 
ATOM   4190 C  CG2 . VAL B 1 87  ? 54.360 -63.593 9.884   1.00 24.96  ?  87  VAL B CG2 1 
ATOM   4191 N  N   . ASN B 1 88  ? 51.791 -61.585 6.971   1.00 21.80  ?  88  ASN B N   1 
ATOM   4192 C  CA  . ASN B 1 88  ? 51.672 -60.703 5.818   1.00 22.35  ?  88  ASN B CA  1 
ATOM   4193 C  C   . ASN B 1 88  ? 51.923 -59.260 6.269   1.00 24.86  ?  88  ASN B C   1 
ATOM   4194 O  O   . ASN B 1 88  ? 52.400 -59.033 7.386   1.00 30.58  ?  88  ASN B O   1 
ATOM   4195 C  CB  . ASN B 1 88  ? 50.351 -60.928 5.091   1.00 22.80  ?  88  ASN B CB  1 
ATOM   4196 C  CG  . ASN B 1 88  ? 49.120 -60.760 5.952   1.00 22.07  ?  88  ASN B CG  1 
ATOM   4197 O  OD1 . ASN B 1 88  ? 49.106 -59.984 6.917   1.00 24.89  ?  88  ASN B OD1 1 
ATOM   4198 N  ND2 . ASN B 1 88  ? 48.054 -61.449 5.585   1.00 20.52  ?  88  ASN B ND2 1 
ATOM   4199 N  N   . LEU B 1 89  ? 51.602 -58.285 5.408   1.00 23.61  ?  89  LEU B N   1 
ATOM   4200 C  CA  . LEU B 1 89  ? 51.891 -56.885 5.667   1.00 22.65  ?  89  LEU B CA  1 
ATOM   4201 C  C   . LEU B 1 89  ? 50.959 -56.364 6.749   1.00 23.80  ?  89  LEU B C   1 
ATOM   4202 O  O   . LEU B 1 89  ? 51.408 -55.713 7.700   1.00 20.70  ?  89  LEU B O   1 
ATOM   4203 C  CB  . LEU B 1 89  ? 51.713 -56.126 4.353   1.00 23.63  ?  89  LEU B CB  1 
ATOM   4204 C  CG  . LEU B 1 89  ? 51.880 -54.602 4.397   1.00 24.53  ?  89  LEU B CG  1 
ATOM   4205 C  CD1 . LEU B 1 89  ? 53.151 -54.137 5.123   1.00 24.11  ?  89  LEU B CD1 1 
ATOM   4206 C  CD2 . LEU B 1 89  ? 51.836 -54.095 2.962   1.00 24.38  ?  89  LEU B CD2 1 
ATOM   4207 N  N   . SER B 1 90  ? 49.661 -56.668 6.560   1.00 26.54  ?  90  SER B N   1 
ATOM   4208 C  CA  . SER B 1 90  ? 48.591 -56.282 7.467   1.00 27.14  ?  90  SER B CA  1 
ATOM   4209 C  C   . SER B 1 90  ? 48.961 -56.621 8.909   1.00 31.45  ?  90  SER B C   1 
ATOM   4210 O  O   . SER B 1 90  ? 48.821 -55.787 9.814   1.00 32.22  ?  90  SER B O   1 
ATOM   4211 C  CB  . SER B 1 90  ? 47.320 -56.956 7.087   1.00 28.21  ?  90  SER B CB  1 
ATOM   4212 O  OG  . SER B 1 90  ? 46.226 -56.455 7.848   1.00 31.48  ?  90  SER B OG  1 
ATOM   4213 N  N   . ILE B 1 91  ? 49.422 -57.864 9.110   1.00 30.41  ?  91  ILE B N   1 
ATOM   4214 C  CA  . ILE B 1 91  ? 49.719 -58.363 10.443  1.00 28.93  ?  91  ILE B CA  1 
ATOM   4215 C  C   . ILE B 1 91  ? 50.960 -57.650 10.962  1.00 27.32  ?  91  ILE B C   1 
ATOM   4216 O  O   . ILE B 1 91  ? 50.992 -57.271 12.132  1.00 27.99  ?  91  ILE B O   1 
ATOM   4217 C  CB  . ILE B 1 91  ? 49.866 -59.898 10.410  1.00 30.65  ?  91  ILE B CB  1 
ATOM   4218 C  CG1 . ILE B 1 91  ? 48.550 -60.536 9.928   1.00 30.45  ?  91  ILE B CG1 1 
ATOM   4219 C  CG2 . ILE B 1 91  ? 50.328 -60.473 11.756  1.00 29.89  ?  91  ILE B CG2 1 
ATOM   4220 C  CD1 . ILE B 1 91  ? 48.408 -62.029 10.182  1.00 30.20  ?  91  ILE B CD1 1 
ATOM   4221 N  N   . LEU B 1 92  ? 51.965 -57.506 10.078  1.00 25.03  ?  92  LEU B N   1 
ATOM   4222 C  CA  . LEU B 1 92  ? 53.254 -56.883 10.379  1.00 22.42  ?  92  LEU B CA  1 
ATOM   4223 C  C   . LEU B 1 92  ? 53.161 -55.357 10.548  1.00 22.09  ?  92  LEU B C   1 
ATOM   4224 O  O   . LEU B 1 92  ? 54.051 -54.752 11.137  1.00 23.78  ?  92  LEU B O   1 
ATOM   4225 C  CB  . LEU B 1 92  ? 54.199 -57.239 9.230   1.00 20.92  ?  92  LEU B CB  1 
ATOM   4226 C  CG  . LEU B 1 92  ? 55.266 -58.318 9.447   1.00 19.91  ?  92  LEU B CG  1 
ATOM   4227 C  CD1 . LEU B 1 92  ? 55.022 -59.245 10.636  1.00 19.40  ?  92  LEU B CD1 1 
ATOM   4228 C  CD2 . LEU B 1 92  ? 55.405 -59.097 8.151   1.00 18.49  ?  92  LEU B CD2 1 
ATOM   4229 N  N   . LYS B 1 93  ? 52.142 -54.715 9.977   1.00 21.48  ?  93  LYS B N   1 
ATOM   4230 C  CA  . LYS B 1 93  ? 51.852 -53.315 10.259  1.00 23.87  ?  93  LYS B CA  1 
ATOM   4231 C  C   . LYS B 1 93  ? 51.125 -53.188 11.594  1.00 26.80  ?  93  LYS B C   1 
ATOM   4232 O  O   . LYS B 1 93  ? 51.353 -52.232 12.327  1.00 25.14  ?  93  LYS B O   1 
ATOM   4233 C  CB  . LYS B 1 93  ? 50.961 -52.668 9.189   1.00 24.02  ?  93  LYS B CB  1 
ATOM   4234 C  CG  . LYS B 1 93  ? 51.699 -52.343 7.905   1.00 24.01  ?  93  LYS B CG  1 
ATOM   4235 C  CD  . LYS B 1 93  ? 50.804 -51.960 6.744   1.00 23.10  ?  93  LYS B CD  1 
ATOM   4236 C  CE  . LYS B 1 93  ? 50.102 -50.678 6.975   1.00 22.39  ?  93  LYS B CE  1 
ATOM   4237 N  NZ  . LYS B 1 93  ? 49.706 -50.118 5.679   1.00 22.34  1  93  LYS B NZ  1 
ATOM   4238 N  N   . PHE B 1 94  ? 50.211 -54.134 11.869  1.00 31.26  ?  94  PHE B N   1 
ATOM   4239 C  CA  . PHE B 1 94  ? 49.534 -54.222 13.155  1.00 31.80  ?  94  PHE B CA  1 
ATOM   4240 C  C   . PHE B 1 94  ? 50.590 -54.327 14.261  1.00 33.16  ?  94  PHE B C   1 
ATOM   4241 O  O   . PHE B 1 94  ? 50.636 -53.477 15.139  1.00 39.88  ?  94  PHE B O   1 
ATOM   4242 C  CB  . PHE B 1 94  ? 48.518 -55.376 13.145  1.00 30.87  ?  94  PHE B CB  1 
ATOM   4243 C  CG  . PHE B 1 94  ? 48.051 -55.854 14.517  1.00 31.57  ?  94  PHE B CG  1 
ATOM   4244 C  CD1 . PHE B 1 94  ? 47.762 -54.940 15.532  1.00 33.44  ?  94  PHE B CD1 1 
ATOM   4245 C  CD2 . PHE B 1 94  ? 47.966 -57.216 14.806  1.00 29.50  ?  94  PHE B CD2 1 
ATOM   4246 C  CE1 . PHE B 1 94  ? 47.357 -55.374 16.785  1.00 33.65  ?  94  PHE B CE1 1 
ATOM   4247 C  CE2 . PHE B 1 94  ? 47.568 -57.640 16.059  1.00 31.22  ?  94  PHE B CE2 1 
ATOM   4248 C  CZ  . PHE B 1 94  ? 47.254 -56.720 17.044  1.00 31.70  ?  94  PHE B CZ  1 
ATOM   4249 N  N   . LEU B 1 95  ? 51.442 -55.357 14.216  1.00 30.48  ?  95  LEU B N   1 
ATOM   4250 C  CA  . LEU B 1 95  ? 52.406 -55.586 15.277  1.00 30.22  ?  95  LEU B CA  1 
ATOM   4251 C  C   . LEU B 1 95  ? 53.408 -54.435 15.320  1.00 29.35  ?  95  LEU B C   1 
ATOM   4252 O  O   . LEU B 1 95  ? 53.825 -54.009 16.397  1.00 28.09  ?  95  LEU B O   1 
ATOM   4253 C  CB  . LEU B 1 95  ? 53.074 -56.946 15.065  1.00 30.14  ?  95  LEU B CB  1 
ATOM   4254 C  CG  . LEU B 1 95  ? 52.166 -58.163 15.293  1.00 29.28  ?  95  LEU B CG  1 
ATOM   4255 C  CD1 . LEU B 1 95  ? 52.849 -59.468 14.889  1.00 29.07  ?  95  LEU B CD1 1 
ATOM   4256 C  CD2 . LEU B 1 95  ? 51.708 -58.239 16.746  1.00 27.93  ?  95  LEU B CD2 1 
ATOM   4257 N  N   . GLY B 1 96  ? 53.756 -53.928 14.134  1.00 28.99  ?  96  GLY B N   1 
ATOM   4258 C  CA  . GLY B 1 96  ? 54.635 -52.774 14.000  1.00 29.52  ?  96  GLY B CA  1 
ATOM   4259 C  C   . GLY B 1 96  ? 54.068 -51.532 14.681  1.00 28.63  ?  96  GLY B C   1 
ATOM   4260 O  O   . GLY B 1 96  ? 54.764 -50.910 15.477  1.00 27.47  ?  96  GLY B O   1 
ATOM   4261 N  N   . PHE B 1 97  ? 52.800 -51.212 14.354  1.00 29.92  ?  97  PHE B N   1 
ATOM   4262 C  CA  . PHE B 1 97  ? 52.066 -50.059 14.870  1.00 28.60  ?  97  PHE B CA  1 
ATOM   4263 C  C   . PHE B 1 97  ? 52.151 -50.031 16.393  1.00 29.03  ?  97  PHE B C   1 
ATOM   4264 O  O   . PHE B 1 97  ? 52.425 -48.974 16.959  1.00 26.61  ?  97  PHE B O   1 
ATOM   4265 C  CB  . PHE B 1 97  ? 50.598 -50.047 14.410  1.00 28.30  ?  97  PHE B CB  1 
ATOM   4266 C  CG  . PHE B 1 97  ? 49.851 -48.730 14.612  1.00 29.61  ?  97  PHE B CG  1 
ATOM   4267 C  CD1 . PHE B 1 97  ? 50.328 -47.540 14.072  1.00 30.60  ?  97  PHE B CD1 1 
ATOM   4268 C  CD2 . PHE B 1 97  ? 48.680 -48.679 15.365  1.00 31.71  ?  97  PHE B CD2 1 
ATOM   4269 C  CE1 . PHE B 1 97  ? 49.652 -46.341 14.271  1.00 31.38  ?  97  PHE B CE1 1 
ATOM   4270 C  CE2 . PHE B 1 97  ? 48.014 -47.476 15.573  1.00 31.39  ?  97  PHE B CE2 1 
ATOM   4271 C  CZ  . PHE B 1 97  ? 48.503 -46.313 15.032  1.00 31.79  ?  97  PHE B CZ  1 
ATOM   4272 N  N   . GLU B 1 98  ? 51.929 -51.185 17.054  1.00 30.91  ?  98  GLU B N   1 
ATOM   4273 C  CA  . GLU B 1 98  ? 52.016 -51.231 18.512  1.00 32.17  ?  98  GLU B CA  1 
ATOM   4274 C  C   . GLU B 1 98  ? 53.429 -50.847 18.981  1.00 30.25  ?  98  GLU B C   1 
ATOM   4275 O  O   . GLU B 1 98  ? 53.571 -49.989 19.857  1.00 28.86  ?  98  GLU B O   1 
ATOM   4276 C  CB  . GLU B 1 98  ? 51.542 -52.538 19.151  1.00 30.92  ?  98  GLU B CB  1 
ATOM   4277 C  CG  . GLU B 1 98  ? 50.566 -52.282 20.300  1.00 32.63  ?  98  GLU B CG  1 
ATOM   4278 C  CD  . GLU B 1 98  ? 49.304 -51.570 19.809  1.00 35.48  ?  98  GLU B CD  1 
ATOM   4279 O  OE1 . GLU B 1 98  ? 48.860 -50.501 20.371  1.00 29.03  ?  98  GLU B OE1 1 
ATOM   4280 O  OE2 . GLU B 1 98  ? 48.798 -52.110 18.775  1.00 35.34  -1 98  GLU B OE2 1 
ATOM   4281 N  N   . GLN B 1 99  ? 54.453 -51.437 18.351  1.00 27.25  ?  99  GLN B N   1 
ATOM   4282 C  CA  . GLN B 1 99  ? 55.834 -51.315 18.789  1.00 27.57  ?  99  GLN B CA  1 
ATOM   4283 C  C   . GLN B 1 99  ? 56.283 -49.862 18.899  1.00 26.83  ?  99  GLN B C   1 
ATOM   4284 O  O   . GLN B 1 99  ? 57.162 -49.542 19.698  1.00 29.59  ?  99  GLN B O   1 
ATOM   4285 C  CB  . GLN B 1 99  ? 56.696 -52.123 17.825  1.00 27.09  ?  99  GLN B CB  1 
ATOM   4286 C  CG  . GLN B 1 99  ? 56.522 -53.622 18.044  1.00 24.93  ?  99  GLN B CG  1 
ATOM   4287 C  CD  . GLN B 1 99  ? 57.362 -54.098 19.197  1.00 22.04  ?  99  GLN B CD  1 
ATOM   4288 O  OE1 . GLN B 1 99  ? 58.309 -53.424 19.613  1.00 19.81  ?  99  GLN B OE1 1 
ATOM   4289 N  NE2 . GLN B 1 99  ? 57.031 -55.268 19.707  1.00 22.31  ?  99  GLN B NE2 1 
ATOM   4290 N  N   . ILE B 1 100 ? 55.654 -48.986 18.125  1.00 24.86  ?  100 ILE B N   1 
ATOM   4291 C  CA  . ILE B 1 100 ? 55.968 -47.567 18.168  1.00 25.66  ?  100 ILE B CA  1 
ATOM   4292 C  C   . ILE B 1 100 ? 55.817 -47.023 19.596  1.00 26.81  ?  100 ILE B C   1 
ATOM   4293 O  O   . ILE B 1 100 ? 56.776 -46.476 20.164  1.00 31.70  ?  100 ILE B O   1 
ATOM   4294 C  CB  . ILE B 1 100 ? 55.079 -46.806 17.170  1.00 24.07  ?  100 ILE B CB  1 
ATOM   4295 C  CG1 . ILE B 1 100 ? 55.098 -47.437 15.784  1.00 23.46  ?  100 ILE B CG1 1 
ATOM   4296 C  CG2 . ILE B 1 100 ? 55.492 -45.343 17.120  1.00 25.70  ?  100 ILE B CG2 1 
ATOM   4297 C  CD1 . ILE B 1 100 ? 54.037 -46.885 14.863  1.00 24.00  ?  100 ILE B CD1 1 
ATOM   4298 N  N   . PHE B 1 101 ? 54.615 -47.216 20.156  1.00 24.95  ?  101 PHE B N   1 
ATOM   4299 C  CA  . PHE B 1 101 ? 54.149 -46.590 21.385  1.00 26.99  ?  101 PHE B CA  1 
ATOM   4300 C  C   . PHE B 1 101 ? 54.692 -47.326 22.614  1.00 26.22  ?  101 PHE B C   1 
ATOM   4301 O  O   . PHE B 1 101 ? 55.085 -46.712 23.620  1.00 23.49  ?  101 PHE B O   1 
ATOM   4302 C  CB  . PHE B 1 101 ? 52.614 -46.592 21.317  1.00 29.53  ?  101 PHE B CB  1 
ATOM   4303 C  CG  . PHE B 1 101 ? 52.052 -46.083 19.987  1.00 30.91  ?  101 PHE B CG  1 
ATOM   4304 C  CD1 . PHE B 1 101 ? 51.429 -46.949 19.091  1.00 30.50  ?  101 PHE B CD1 1 
ATOM   4305 C  CD2 . PHE B 1 101 ? 52.203 -44.748 19.610  1.00 32.62  ?  101 PHE B CD2 1 
ATOM   4306 C  CE1 . PHE B 1 101 ? 50.945 -46.484 17.877  1.00 32.11  ?  101 PHE B CE1 1 
ATOM   4307 C  CE2 . PHE B 1 101 ? 51.730 -44.288 18.391  1.00 31.88  ?  101 PHE B CE2 1 
ATOM   4308 C  CZ  . PHE B 1 101 ? 51.102 -45.156 17.527  1.00 32.62  ?  101 PHE B CZ  1 
ATOM   4309 N  N   . LYS B 1 102 ? 54.647 -48.660 22.530  1.00 23.35  ?  102 LYS B N   1 
ATOM   4310 C  CA  . LYS B 1 102 ? 55.348 -49.521 23.462  1.00 21.24  ?  102 LYS B CA  1 
ATOM   4311 C  C   . LYS B 1 102 ? 56.774 -48.985 23.644  1.00 22.59  ?  102 LYS B C   1 
ATOM   4312 O  O   . LYS B 1 102 ? 57.172 -48.653 24.760  1.00 24.09  ?  102 LYS B O   1 
ATOM   4313 C  CB  . LYS B 1 102 ? 55.240 -50.939 22.876  1.00 20.68  ?  102 LYS B CB  1 
ATOM   4314 C  CG  . LYS B 1 102 ? 55.762 -52.111 23.715  1.00 19.90  ?  102 LYS B CG  1 
ATOM   4315 C  CD  . LYS B 1 102 ? 55.486 -53.490 23.135  1.00 18.93  ?  102 LYS B CD  1 
ATOM   4316 C  CE  . LYS B 1 102 ? 55.727 -54.565 24.156  1.00 20.68  ?  102 LYS B CE  1 
ATOM   4317 N  NZ  . LYS B 1 102 ? 55.036 -55.841 23.909  1.00 21.11  1  102 LYS B NZ  1 
ATOM   4318 N  N   . ASN B 1 103 ? 57.540 -48.905 22.537  1.00 22.76  ?  103 ASN B N   1 
ATOM   4319 C  CA  . ASN B 1 103 ? 58.956 -48.544 22.560  1.00 22.88  ?  103 ASN B CA  1 
ATOM   4320 C  C   . ASN B 1 103 ? 59.113 -47.140 23.153  1.00 20.70  ?  103 ASN B C   1 
ATOM   4321 O  O   . ASN B 1 103 ? 60.064 -46.874 23.878  1.00 18.58  ?  103 ASN B O   1 
ATOM   4322 C  CB  . ASN B 1 103 ? 59.617 -48.701 21.180  1.00 23.42  ?  103 ASN B CB  1 
ATOM   4323 C  CG  . ASN B 1 103 ? 59.839 -50.143 20.735  1.00 24.41  ?  103 ASN B CG  1 
ATOM   4324 O  OD1 . ASN B 1 103 ? 59.694 -51.095 21.519  1.00 25.99  ?  103 ASN B OD1 1 
ATOM   4325 N  ND2 . ASN B 1 103 ? 60.201 -50.337 19.474  1.00 22.01  ?  103 ASN B ND2 1 
ATOM   4326 N  N   . ALA B 1 104 ? 58.156 -46.259 22.843  1.00 21.48  ?  104 ALA B N   1 
ATOM   4327 C  CA  . ALA B 1 104 ? 58.148 -44.866 23.277  1.00 21.22  ?  104 ALA B CA  1 
ATOM   4328 C  C   . ALA B 1 104 ? 57.912 -44.731 24.789  1.00 21.34  ?  104 ALA B C   1 
ATOM   4329 O  O   . ALA B 1 104 ? 58.465 -43.833 25.416  1.00 19.55  ?  104 ALA B O   1 
ATOM   4330 C  CB  . ALA B 1 104 ? 57.091 -44.121 22.469  1.00 20.08  ?  104 ALA B CB  1 
ATOM   4331 N  N   . LEU B 1 105 ? 57.066 -45.609 25.355  1.00 23.41  ?  105 LEU B N   1 
ATOM   4332 C  CA  . LEU B 1 105 ? 56.800 -45.691 26.792  1.00 25.93  ?  105 LEU B CA  1 
ATOM   4333 C  C   . LEU B 1 105 ? 58.027 -46.134 27.608  1.00 29.61  ?  105 LEU B C   1 
ATOM   4334 O  O   . LEU B 1 105 ? 58.008 -45.900 28.831  1.00 30.34  ?  105 LEU B O   1 
ATOM   4335 C  CB  . LEU B 1 105 ? 55.624 -46.633 27.067  1.00 25.75  ?  105 LEU B CB  1 
ATOM   4336 C  CG  . LEU B 1 105 ? 54.224 -46.064 26.785  1.00 26.98  ?  105 LEU B CG  1 
ATOM   4337 C  CD1 . LEU B 1 105 ? 53.148 -47.099 26.471  1.00 25.56  ?  105 LEU B CD1 1 
ATOM   4338 C  CD2 . LEU B 1 105 ? 53.770 -45.260 27.985  1.00 27.21  ?  105 LEU B CD2 1 
ATOM   4339 N  N   . THR B 1 106 ? 59.048 -46.769 26.959  1.00 25.46  ?  106 THR B N   1 
ATOM   4340 C  CA  . THR B 1 106 ? 60.301 -47.159 27.605  1.00 23.68  ?  106 THR B CA  1 
ATOM   4341 C  C   . THR B 1 106 ? 61.079 -45.926 28.052  1.00 26.45  ?  106 THR B C   1 
ATOM   4342 O  O   . THR B 1 106 ? 61.855 -46.032 29.016  1.00 29.35  ?  106 THR B O   1 
ATOM   4343 C  CB  . THR B 1 106 ? 61.242 -48.000 26.732  1.00 22.81  ?  106 THR B CB  1 
ATOM   4344 O  OG1 . THR B 1 106 ? 61.779 -47.222 25.660  1.00 18.68  ?  106 THR B OG1 1 
ATOM   4345 C  CG2 . THR B 1 106 ? 60.594 -49.269 26.209  1.00 24.09  ?  106 THR B CG2 1 
ATOM   4346 N  N   . GLY B 1 107 ? 60.938 -44.804 27.309  1.00 24.41  ?  107 GLY B N   1 
ATOM   4347 C  CA  . GLY B 1 107 ? 61.730 -43.600 27.563  1.00 24.39  ?  107 GLY B CA  1 
ATOM   4348 C  C   . GLY B 1 107 ? 63.061 -43.554 26.790  1.00 25.05  ?  107 GLY B C   1 
ATOM   4349 O  O   . GLY B 1 107 ? 63.587 -42.464 26.542  1.00 25.72  ?  107 GLY B O   1 
ATOM   4350 N  N   . LEU B 1 108 ? 63.609 -44.730 26.418  1.00 24.97  ?  108 LEU B N   1 
ATOM   4351 C  CA  . LEU B 1 108 ? 64.766 -44.854 25.526  1.00 25.20  ?  108 LEU B CA  1 
ATOM   4352 C  C   . LEU B 1 108 ? 64.409 -44.458 24.089  1.00 23.19  ?  108 LEU B C   1 
ATOM   4353 O  O   . LEU B 1 108 ? 63.238 -44.487 23.700  1.00 21.23  ?  108 LEU B O   1 
ATOM   4354 C  CB  . LEU B 1 108 ? 65.304 -46.288 25.560  1.00 25.61  ?  108 LEU B CB  1 
ATOM   4355 C  CG  . LEU B 1 108 ? 65.669 -46.832 26.950  1.00 25.89  ?  108 LEU B CG  1 
ATOM   4356 C  CD1 . LEU B 1 108 ? 65.647 -48.348 26.985  1.00 24.13  ?  108 LEU B CD1 1 
ATOM   4357 C  CD2 . LEU B 1 108 ? 67.037 -46.310 27.408  1.00 27.11  ?  108 LEU B CD2 1 
ATOM   4358 N  N   . ASN B 1 109 ? 65.448 -44.126 23.305  1.00 21.49  ?  109 ASN B N   1 
ATOM   4359 C  CA  . ASN B 1 109 ? 65.277 -43.615 21.954  1.00 22.25  ?  109 ASN B CA  1 
ATOM   4360 C  C   . ASN B 1 109 ? 65.240 -44.779 20.967  1.00 21.07  ?  109 ASN B C   1 
ATOM   4361 O  O   . ASN B 1 109 ? 66.279 -45.183 20.449  1.00 18.58  ?  109 ASN B O   1 
ATOM   4362 C  CB  . ASN B 1 109 ? 66.349 -42.592 21.585  1.00 22.68  ?  109 ASN B CB  1 
ATOM   4363 C  CG  . ASN B 1 109 ? 66.258 -41.331 22.412  1.00 22.27  ?  109 ASN B CG  1 
ATOM   4364 O  OD1 . ASN B 1 109 ? 65.467 -40.421 22.117  1.00 20.69  ?  109 ASN B OD1 1 
ATOM   4365 N  ND2 . ASN B 1 109 ? 67.104 -41.245 23.425  1.00 22.54  ?  109 ASN B ND2 1 
ATOM   4366 N  N   . MET B 1 110 ? 64.023 -45.293 20.746  1.00 21.80  ?  110 MET B N   1 
ATOM   4367 C  CA  . MET B 1 110 ? 63.749 -46.394 19.838  1.00 25.35  ?  110 MET B CA  1 
ATOM   4368 C  C   . MET B 1 110 ? 62.426 -46.131 19.120  1.00 27.74  ?  110 MET B C   1 
ATOM   4369 O  O   . MET B 1 110 ? 61.412 -45.869 19.751  1.00 32.64  ?  110 MET B O   1 
ATOM   4370 C  CB  . MET B 1 110 ? 63.597 -47.705 20.612  1.00 25.45  ?  110 MET B CB  1 
ATOM   4371 C  CG  . MET B 1 110 ? 64.817 -48.079 21.424  1.00 27.11  ?  110 MET B CG  1 
ATOM   4372 S  SD  . MET B 1 110 ? 64.646 -49.695 22.204  1.00 32.57  ?  110 MET B SD  1 
ATOM   4373 C  CE  . MET B 1 110 ? 63.161 -49.468 23.195  1.00 33.41  ?  110 MET B CE  1 
ATOM   4374 N  N   . GLY B 1 111 ? 62.437 -46.155 17.792  1.00 29.21  ?  111 GLY B N   1 
ATOM   4375 C  CA  . GLY B 1 111 ? 61.217 -46.026 17.021  1.00 29.98  ?  111 GLY B CA  1 
ATOM   4376 C  C   . GLY B 1 111 ? 60.488 -47.363 16.960  1.00 32.65  ?  111 GLY B C   1 
ATOM   4377 O  O   . GLY B 1 111 ? 60.662 -48.220 17.826  1.00 33.60  ?  111 GLY B O   1 
ATOM   4378 N  N   . GLY B 1 112 ? 59.696 -47.563 15.906  1.00 35.15  ?  112 GLY B N   1 
ATOM   4379 C  CA  . GLY B 1 112 ? 58.846 -48.739 15.857  1.00 37.04  ?  112 GLY B CA  1 
ATOM   4380 C  C   . GLY B 1 112 ? 58.744 -49.310 14.452  1.00 34.67  ?  112 GLY B C   1 
ATOM   4381 O  O   . GLY B 1 112 ? 58.387 -48.581 13.537  1.00 36.22  ?  112 GLY B O   1 
ATOM   4382 N  N   . GLY B 1 113 ? 59.027 -50.616 14.329  1.00 33.82  ?  113 GLY B N   1 
ATOM   4383 C  CA  . GLY B 1 113 ? 58.766 -51.374 13.111  1.00 35.36  ?  113 GLY B CA  1 
ATOM   4384 C  C   . GLY B 1 113 ? 58.475 -52.852 13.385  1.00 31.81  ?  113 GLY B C   1 
ATOM   4385 O  O   . GLY B 1 113 ? 58.224 -53.236 14.524  1.00 29.50  ?  113 GLY B O   1 
ATOM   4386 N  N   . LYS B 1 114 ? 58.498 -53.665 12.318  1.00 32.29  ?  114 LYS B N   1 
ATOM   4387 C  CA  . LYS B 1 114 ? 58.339 -55.109 12.418  1.00 36.08  ?  114 LYS B CA  1 
ATOM   4388 C  C   . LYS B 1 114 ? 58.591 -55.734 11.051  1.00 31.77  ?  114 LYS B C   1 
ATOM   4389 O  O   . LYS B 1 114 ? 58.345 -55.091 10.033  1.00 32.84  ?  114 LYS B O   1 
ATOM   4390 C  CB  . LYS B 1 114 ? 56.907 -55.502 12.817  1.00 42.56  ?  114 LYS B CB  1 
ATOM   4391 C  CG  . LYS B 1 114 ? 56.788 -56.625 13.844  1.00 44.15  ?  114 LYS B CG  1 
ATOM   4392 C  CD  . LYS B 1 114 ? 57.111 -56.168 15.266  1.00 45.22  ?  114 LYS B CD  1 
ATOM   4393 C  CE  . LYS B 1 114 ? 56.898 -57.237 16.318  1.00 48.55  ?  114 LYS B CE  1 
ATOM   4394 N  NZ  . LYS B 1 114 ? 57.356 -58.579 15.946  1.00 46.16  1  114 LYS B NZ  1 
ATOM   4395 N  N   . GLY B 1 115 ? 59.003 -57.005 11.040  1.00 28.90  ?  115 GLY B N   1 
ATOM   4396 C  CA  . GLY B 1 115 ? 59.301 -57.722 9.808   1.00 26.78  ?  115 GLY B CA  1 
ATOM   4397 C  C   . GLY B 1 115 ? 59.190 -59.231 10.009  1.00 25.75  ?  115 GLY B C   1 
ATOM   4398 O  O   . GLY B 1 115 ? 58.755 -59.677 11.072  1.00 20.91  ?  115 GLY B O   1 
ATOM   4399 N  N   . GLY B 1 116 ? 59.589 -60.000 8.977   1.00 27.92  ?  116 GLY B N   1 
ATOM   4400 C  CA  . GLY B 1 116 ? 59.483 -61.452 9.013   1.00 27.55  ?  116 GLY B CA  1 
ATOM   4401 C  C   . GLY B 1 116 ? 59.088 -62.054 7.667   1.00 27.74  ?  116 GLY B C   1 
ATOM   4402 O  O   . GLY B 1 116 ? 59.263 -61.420 6.626   1.00 26.56  ?  116 GLY B O   1 
ATOM   4403 N  N   . SER B 1 117 ? 58.587 -63.300 7.732   1.00 26.48  ?  117 SER B N   1 
ATOM   4404 C  CA  . SER B 1 117 ? 58.354 -64.158 6.578   1.00 26.66  ?  117 SER B CA  1 
ATOM   4405 C  C   . SER B 1 117 ? 57.206 -65.129 6.862   1.00 28.76  ?  117 SER B C   1 
ATOM   4406 O  O   . SER B 1 117 ? 56.878 -65.368 8.023   1.00 31.73  ?  117 SER B O   1 
ATOM   4407 C  CB  . SER B 1 117 ? 59.583 -64.942 6.219   1.00 25.53  ?  117 SER B CB  1 
ATOM   4408 O  OG  . SER B 1 117 ? 59.241 -66.039 5.381   1.00 24.58  ?  117 SER B OG  1 
ATOM   4409 N  N   . ASP B 1 118 ? 56.630 -65.699 5.788   1.00 26.45  ?  118 ASP B N   1 
ATOM   4410 C  CA  . ASP B 1 118 ? 55.666 -66.791 5.863   1.00 24.69  ?  118 ASP B CA  1 
ATOM   4411 C  C   . ASP B 1 118 ? 56.410 -68.115 5.732   1.00 26.57  ?  118 ASP B C   1 
ATOM   4412 O  O   . ASP B 1 118 ? 55.798 -69.154 5.459   1.00 28.93  ?  118 ASP B O   1 
ATOM   4413 C  CB  . ASP B 1 118 ? 54.580 -66.657 4.805   1.00 22.58  ?  118 ASP B CB  1 
ATOM   4414 C  CG  . ASP B 1 118 ? 55.045 -66.389 3.375   1.00 21.54  ?  118 ASP B CG  1 
ATOM   4415 O  OD1 . ASP B 1 118 ? 54.198 -65.961 2.572   1.00 20.84  ?  118 ASP B OD1 1 
ATOM   4416 O  OD2 . ASP B 1 118 ? 56.240 -66.619 3.070   1.00 19.81  -1 118 ASP B OD2 1 
ATOM   4417 N  N   . PHE B 1 119 ? 57.744 -68.036 5.839   1.00 26.07  ?  119 PHE B N   1 
ATOM   4418 C  CA  . PHE B 1 119 ? 58.581 -69.200 6.072   1.00 28.39  ?  119 PHE B CA  1 
ATOM   4419 C  C   . PHE B 1 119 ? 58.114 -69.843 7.380   1.00 31.39  ?  119 PHE B C   1 
ATOM   4420 O  O   . PHE B 1 119 ? 58.055 -69.160 8.405   1.00 35.29  ?  119 PHE B O   1 
ATOM   4421 C  CB  . PHE B 1 119 ? 60.068 -68.795 6.068   1.00 28.45  ?  119 PHE B CB  1 
ATOM   4422 C  CG  . PHE B 1 119 ? 61.029 -69.845 6.611   1.00 26.41  ?  119 PHE B CG  1 
ATOM   4423 C  CD1 . PHE B 1 119 ? 61.533 -70.823 5.772   1.00 27.24  ?  119 PHE B CD1 1 
ATOM   4424 C  CD2 . PHE B 1 119 ? 61.369 -69.890 7.962   1.00 25.58  ?  119 PHE B CD2 1 
ATOM   4425 C  CE1 . PHE B 1 119 ? 62.357 -71.818 6.270   1.00 29.14  ?  119 PHE B CE1 1 
ATOM   4426 C  CE2 . PHE B 1 119 ? 62.188 -70.891 8.464   1.00 25.20  ?  119 PHE B CE2 1 
ATOM   4427 C  CZ  . PHE B 1 119 ? 62.684 -71.851 7.618   1.00 27.90  ?  119 PHE B CZ  1 
ATOM   4428 N  N   . ASP B 1 120 ? 57.753 -71.138 7.300   1.00 33.54  ?  120 ASP B N   1 
ATOM   4429 C  CA  . ASP B 1 120 ? 57.213 -71.924 8.400   1.00 33.97  ?  120 ASP B CA  1 
ATOM   4430 C  C   . ASP B 1 120 ? 58.322 -72.806 8.955   1.00 32.08  ?  120 ASP B C   1 
ATOM   4431 O  O   . ASP B 1 120 ? 58.646 -73.823 8.340   1.00 27.91  ?  120 ASP B O   1 
ATOM   4432 C  CB  . ASP B 1 120 ? 56.074 -72.831 7.954   1.00 35.52  ?  120 ASP B CB  1 
ATOM   4433 C  CG  . ASP B 1 120 ? 55.344 -73.579 9.063   1.00 40.35  ?  120 ASP B CG  1 
ATOM   4434 O  OD1 . ASP B 1 120 ? 54.576 -74.506 8.730   1.00 51.74  ?  120 ASP B OD1 1 
ATOM   4435 O  OD2 . ASP B 1 120 ? 55.497 -73.208 10.245  1.00 36.82  -1 120 ASP B OD2 1 
ATOM   4436 N  N   . PRO B 1 121 ? 58.950 -72.408 10.094  1.00 31.57  ?  121 PRO B N   1 
ATOM   4437 C  CA  . PRO B 1 121 ? 59.917 -73.267 10.796  1.00 29.51  ?  121 PRO B CA  1 
ATOM   4438 C  C   . PRO B 1 121 ? 59.501 -74.733 10.948  1.00 31.29  ?  121 PRO B C   1 
ATOM   4439 O  O   . PRO B 1 121 ? 60.329 -75.652 10.795  1.00 32.02  ?  121 PRO B O   1 
ATOM   4440 C  CB  . PRO B 1 121 ? 60.082 -72.594 12.171  1.00 28.99  ?  121 PRO B CB  1 
ATOM   4441 C  CG  . PRO B 1 121 ? 59.628 -71.145 11.977  1.00 29.62  ?  121 PRO B CG  1 
ATOM   4442 C  CD  . PRO B 1 121 ? 58.794 -71.073 10.712  1.00 28.55  ?  121 PRO B CD  1 
ATOM   4443 N  N   . LYS B 1 122 ? 58.215 -74.954 11.273  1.00 31.14  ?  122 LYS B N   1 
ATOM   4444 C  CA  . LYS B 1 122 ? 57.751 -76.292 11.637  1.00 33.50  ?  122 LYS B CA  1 
ATOM   4445 C  C   . LYS B 1 122 ? 58.059 -77.277 10.498  1.00 31.20  ?  122 LYS B C   1 
ATOM   4446 O  O   . LYS B 1 122 ? 57.814 -77.005 9.323   1.00 28.79  ?  122 LYS B O   1 
ATOM   4447 C  CB  . LYS B 1 122 ? 56.288 -76.261 12.096  1.00 33.82  ?  122 LYS B CB  1 
ATOM   4448 C  CG  . LYS B 1 122 ? 55.592 -77.605 12.120  1.00 38.37  ?  122 LYS B CG  1 
ATOM   4449 C  CD  . LYS B 1 122 ? 56.284 -78.668 12.974  1.00 46.55  ?  122 LYS B CD  1 
ATOM   4450 C  CE  . LYS B 1 122 ? 56.234 -80.053 12.331  1.00 49.27  ?  122 LYS B CE  1 
ATOM   4451 N  NZ  . LYS B 1 122 ? 56.435 -81.180 13.248  1.00 44.82  1  122 LYS B NZ  1 
ATOM   4452 N  N   . GLY B 1 123 ? 58.669 -78.409 10.856  1.00 30.32  ?  123 GLY B N   1 
ATOM   4453 C  CA  . GLY B 1 123 ? 59.085 -79.410 9.884   1.00 31.18  ?  123 GLY B CA  1 
ATOM   4454 C  C   . GLY B 1 123 ? 60.528 -79.210 9.416   1.00 31.86  ?  123 GLY B C   1 
ATOM   4455 O  O   . GLY B 1 123 ? 61.191 -80.181 9.082   1.00 31.27  ?  123 GLY B O   1 
ATOM   4456 N  N   . LYS B 1 124 ? 61.015 -77.958 9.402   1.00 30.45  ?  124 LYS B N   1 
ATOM   4457 C  CA  . LYS B 1 124 ? 62.261 -77.631 8.736   1.00 28.64  ?  124 LYS B CA  1 
ATOM   4458 C  C   . LYS B 1 124 ? 63.416 -77.997 9.650   1.00 28.06  ?  124 LYS B C   1 
ATOM   4459 O  O   . LYS B 1 124 ? 63.279 -77.839 10.855  1.00 30.49  ?  124 LYS B O   1 
ATOM   4460 C  CB  . LYS B 1 124 ? 62.359 -76.123 8.460   1.00 30.68  ?  124 LYS B CB  1 
ATOM   4461 C  CG  . LYS B 1 124 ? 61.207 -75.475 7.682   1.00 28.33  ?  124 LYS B CG  1 
ATOM   4462 C  CD  . LYS B 1 124 ? 61.258 -75.695 6.176   1.00 25.91  ?  124 LYS B CD  1 
ATOM   4463 C  CE  . LYS B 1 124 ? 59.980 -75.319 5.508   1.00 26.35  ?  124 LYS B CE  1 
ATOM   4464 N  NZ  . LYS B 1 124 ? 58.799 -76.015 6.028   1.00 26.39  1  124 LYS B NZ  1 
ATOM   4465 N  N   . SER B 1 125 ? 64.540 -78.426 9.058   1.00 26.58  ?  125 SER B N   1 
ATOM   4466 C  CA  . SER B 1 125 ? 65.755 -78.790 9.776   1.00 26.93  ?  125 SER B CA  1 
ATOM   4467 C  C   . SER B 1 125 ? 66.535 -77.539 10.159  1.00 28.46  ?  125 SER B C   1 
ATOM   4468 O  O   . SER B 1 125 ? 66.215 -76.471 9.661   1.00 29.64  ?  125 SER B O   1 
ATOM   4469 C  CB  . SER B 1 125 ? 66.589 -79.654 8.896   1.00 26.60  ?  125 SER B CB  1 
ATOM   4470 O  OG  . SER B 1 125 ? 66.522 -79.130 7.578   1.00 22.98  ?  125 SER B OG  1 
ATOM   4471 N  N   . ASP B 1 126 ? 67.588 -77.683 10.981  1.00 31.38  ?  126 ASP B N   1 
ATOM   4472 C  CA  . ASP B 1 126 ? 68.435 -76.554 11.352  1.00 31.23  ?  126 ASP B CA  1 
ATOM   4473 C  C   . ASP B 1 126 ? 69.186 -76.025 10.128  1.00 27.45  ?  126 ASP B C   1 
ATOM   4474 O  O   . ASP B 1 126 ? 69.419 -74.830 10.025  1.00 26.94  ?  126 ASP B O   1 
ATOM   4475 C  CB  . ASP B 1 126 ? 69.383 -76.858 12.510  1.00 33.63  ?  126 ASP B CB  1 
ATOM   4476 C  CG  . ASP B 1 126 ? 69.607 -75.677 13.456  1.00 41.32  ?  126 ASP B CG  1 
ATOM   4477 O  OD1 . ASP B 1 126 ? 69.735 -74.534 12.939  1.00 47.61  ?  126 ASP B OD1 1 
ATOM   4478 O  OD2 . ASP B 1 126 ? 69.632 -75.877 14.704  1.00 41.93  -1 126 ASP B OD2 1 
ATOM   4479 N  N   . SER B 1 127 ? 69.574 -76.907 9.204   1.00 27.81  ?  127 SER B N   1 
ATOM   4480 C  CA  . SER B 1 127 ? 70.271 -76.495 7.990   1.00 29.23  ?  127 SER B CA  1 
ATOM   4481 C  C   . SER B 1 127 ? 69.348 -75.664 7.091   1.00 29.45  ?  127 SER B C   1 
ATOM   4482 O  O   . SER B 1 127 ? 69.786 -74.687 6.475   1.00 26.24  ?  127 SER B O   1 
ATOM   4483 C  CB  . SER B 1 127 ? 70.817 -77.689 7.249   1.00 26.41  ?  127 SER B CB  1 
ATOM   4484 O  OG  . SER B 1 127 ? 69.744 -78.554 6.907   1.00 26.00  ?  127 SER B OG  1 
ATOM   4485 N  N   . GLU B 1 128 ? 68.073 -76.068 7.023   1.00 28.88  ?  128 GLU B N   1 
ATOM   4486 C  CA  . GLU B 1 128 ? 67.078 -75.340 6.251   1.00 31.84  ?  128 GLU B CA  1 
ATOM   4487 C  C   . GLU B 1 128 ? 66.922 -73.932 6.816   1.00 35.21  ?  128 GLU B C   1 
ATOM   4488 O  O   . GLU B 1 128 ? 67.021 -72.959 6.072   1.00 42.27  ?  128 GLU B O   1 
ATOM   4489 C  CB  . GLU B 1 128 ? 65.752 -76.097 6.182   1.00 33.02  ?  128 GLU B CB  1 
ATOM   4490 C  CG  . GLU B 1 128 ? 65.736 -77.128 5.052   1.00 33.68  ?  128 GLU B CG  1 
ATOM   4491 C  CD  . GLU B 1 128 ? 64.760 -78.275 5.171   1.00 33.91  ?  128 GLU B CD  1 
ATOM   4492 O  OE1 . GLU B 1 128 ? 64.110 -78.421 6.235   1.00 37.44  ?  128 GLU B OE1 1 
ATOM   4493 O  OE2 . GLU B 1 128 ? 64.676 -79.031 4.184   1.00 31.83  -1 128 GLU B OE2 1 
ATOM   4494 N  N   . ILE B 1 129 ? 66.709 -73.838 8.136   1.00 35.57  ?  129 ILE B N   1 
ATOM   4495 C  CA  . ILE B 1 129 ? 66.586 -72.571 8.850   1.00 32.52  ?  129 ILE B CA  1 
ATOM   4496 C  C   . ILE B 1 129 ? 67.818 -71.713 8.551   1.00 31.61  ?  129 ILE B C   1 
ATOM   4497 O  O   . ILE B 1 129 ? 67.680 -70.589 8.070   1.00 34.43  ?  129 ILE B O   1 
ATOM   4498 C  CB  . ILE B 1 129 ? 66.338 -72.824 10.356  1.00 31.47  ?  129 ILE B CB  1 
ATOM   4499 C  CG1 . ILE B 1 129 ? 64.923 -73.387 10.573  1.00 33.13  ?  129 ILE B CG1 1 
ATOM   4500 C  CG2 . ILE B 1 129 ? 66.563 -71.570 11.201  1.00 32.11  ?  129 ILE B CG2 1 
ATOM   4501 C  CD1 . ILE B 1 129 ? 64.668 -74.050 11.911  1.00 32.19  ?  129 ILE B CD1 1 
ATOM   4502 N  N   . ARG B 1 130 ? 69.010 -72.274 8.787   1.00 30.83  ?  130 ARG B N   1 
ATOM   4503 C  CA  . ARG B 1 130 ? 70.279 -71.616 8.513   1.00 31.81  ?  130 ARG B CA  1 
ATOM   4504 C  C   . ARG B 1 130 ? 70.325 -71.063 7.078   1.00 35.54  ?  130 ARG B C   1 
ATOM   4505 O  O   . ARG B 1 130 ? 70.799 -69.953 6.865   1.00 32.60  ?  130 ARG B O   1 
ATOM   4506 C  CB  . ARG B 1 130 ? 71.445 -72.581 8.793   1.00 31.65  ?  130 ARG B CB  1 
ATOM   4507 C  CG  . ARG B 1 130 ? 72.768 -72.081 8.214   1.00 32.88  ?  130 ARG B CG  1 
ATOM   4508 C  CD  . ARG B 1 130 ? 74.048 -72.852 8.520   1.00 30.19  ?  130 ARG B CD  1 
ATOM   4509 N  NE  . ARG B 1 130 ? 73.982 -74.284 8.199   1.00 30.26  ?  130 ARG B NE  1 
ATOM   4510 C  CZ  . ARG B 1 130 ? 73.841 -74.850 6.997   1.00 29.35  ?  130 ARG B CZ  1 
ATOM   4511 N  NH1 . ARG B 1 130 ? 73.762 -74.118 5.891   1.00 27.86  1  130 ARG B NH1 1 
ATOM   4512 N  NH2 . ARG B 1 130 ? 73.752 -76.168 6.918   1.00 27.87  ?  130 ARG B NH2 1 
ATOM   4513 N  N   . ARG B 1 131 ? 69.853 -71.834 6.082   1.00 38.08  ?  131 ARG B N   1 
ATOM   4514 C  CA  . ARG B 1 131 ? 69.926 -71.424 4.685   1.00 35.83  ?  131 ARG B CA  1 
ATOM   4515 C  C   . ARG B 1 131 ? 68.793 -70.456 4.329   1.00 41.02  ?  131 ARG B C   1 
ATOM   4516 O  O   . ARG B 1 131 ? 68.908 -69.710 3.351   1.00 48.62  ?  131 ARG B O   1 
ATOM   4517 C  CB  . ARG B 1 131 ? 69.888 -72.615 3.721   1.00 35.47  ?  131 ARG B CB  1 
ATOM   4518 C  CG  . ARG B 1 131 ? 71.181 -73.412 3.648   1.00 35.69  ?  131 ARG B CG  1 
ATOM   4519 C  CD  . ARG B 1 131 ? 71.203 -74.446 2.534   1.00 33.04  ?  131 ARG B CD  1 
ATOM   4520 N  NE  . ARG B 1 131 ? 70.069 -75.350 2.716   1.00 34.12  ?  131 ARG B NE  1 
ATOM   4521 C  CZ  . ARG B 1 131 ? 70.072 -76.601 3.199   1.00 34.48  ?  131 ARG B CZ  1 
ATOM   4522 N  NH1 . ARG B 1 131 ? 71.185 -77.228 3.555   1.00 29.96  1  131 ARG B NH1 1 
ATOM   4523 N  NH2 . ARG B 1 131 ? 68.916 -77.237 3.299   1.00 36.83  ?  131 ARG B NH2 1 
ATOM   4524 N  N   . PHE B 1 132 ? 67.688 -70.468 5.093   1.00 35.80  ?  132 PHE B N   1 
ATOM   4525 C  CA  . PHE B 1 132 ? 66.661 -69.444 4.947   1.00 33.75  ?  132 PHE B CA  1 
ATOM   4526 C  C   . PHE B 1 132 ? 67.081 -68.113 5.607   1.00 37.11  ?  132 PHE B C   1 
ATOM   4527 O  O   . PHE B 1 132 ? 66.875 -67.041 5.012   1.00 37.97  ?  132 PHE B O   1 
ATOM   4528 C  CB  . PHE B 1 132 ? 65.316 -69.922 5.501   1.00 31.57  ?  132 PHE B CB  1 
ATOM   4529 C  CG  . PHE B 1 132 ? 64.271 -68.815 5.479   1.00 32.10  ?  132 PHE B CG  1 
ATOM   4530 C  CD1 . PHE B 1 132 ? 63.555 -68.546 4.320   1.00 30.80  ?  132 PHE B CD1 1 
ATOM   4531 C  CD2 . PHE B 1 132 ? 64.058 -68.006 6.592   1.00 33.46  ?  132 PHE B CD2 1 
ATOM   4532 C  CE1 . PHE B 1 132 ? 62.637 -67.519 4.283   1.00 31.44  ?  132 PHE B CE1 1 
ATOM   4533 C  CE2 . PHE B 1 132 ? 63.134 -66.973 6.553   1.00 33.11  ?  132 PHE B CE2 1 
ATOM   4534 C  CZ  . PHE B 1 132 ? 62.420 -66.739 5.404   1.00 32.58  ?  132 PHE B CZ  1 
ATOM   4535 N  N   . CYS B 1 133 ? 67.637 -68.154 6.838   1.00 30.32  ?  133 CYS B N   1 
ATOM   4536 C  CA  . CYS B 1 133 ? 68.017 -66.934 7.541   1.00 29.75  ?  133 CYS B CA  1 
ATOM   4537 C  C   . CYS B 1 133 ? 69.035 -66.139 6.715   1.00 28.87  ?  133 CYS B C   1 
ATOM   4538 O  O   . CYS B 1 133 ? 69.011 -64.900 6.675   1.00 26.57  ?  133 CYS B O   1 
ATOM   4539 C  CB  . CYS B 1 133 ? 68.516 -67.263 8.945   1.00 31.05  ?  133 CYS B CB  1 
ATOM   4540 S  SG  . CYS B 1 133 ? 67.201 -67.898 10.023  1.00 35.18  ?  133 CYS B SG  1 
ATOM   4541 N  N   . VAL B 1 134 ? 69.929 -66.894 6.058   1.00 27.10  ?  134 VAL B N   1 
ATOM   4542 C  CA  . VAL B 1 134 ? 70.993 -66.375 5.210   1.00 24.48  ?  134 VAL B CA  1 
ATOM   4543 C  C   . VAL B 1 134 ? 70.405 -65.724 3.956   1.00 25.05  ?  134 VAL B C   1 
ATOM   4544 O  O   . VAL B 1 134 ? 70.888 -64.678 3.531   1.00 26.08  ?  134 VAL B O   1 
ATOM   4545 C  CB  . VAL B 1 134 ? 71.958 -67.527 4.851   1.00 22.20  ?  134 VAL B CB  1 
ATOM   4546 C  CG1 . VAL B 1 134 ? 72.835 -67.227 3.637   1.00 22.05  ?  134 VAL B CG1 1 
ATOM   4547 C  CG2 . VAL B 1 134 ? 72.825 -67.936 6.031   1.00 21.66  ?  134 VAL B CG2 1 
ATOM   4548 N  N   . ALA B 1 135 ? 69.418 -66.382 3.330   1.00 25.39  ?  135 ALA B N   1 
ATOM   4549 C  CA  . ALA B 1 135 ? 68.802 -65.886 2.107   1.00 26.28  ?  135 ALA B CA  1 
ATOM   4550 C  C   . ALA B 1 135 ? 67.999 -64.617 2.412   1.00 27.31  ?  135 ALA B C   1 
ATOM   4551 O  O   . ALA B 1 135 ? 67.906 -63.725 1.576   1.00 24.52  ?  135 ALA B O   1 
ATOM   4552 C  CB  . ALA B 1 135 ? 67.920 -66.964 1.491   1.00 26.94  ?  135 ALA B CB  1 
ATOM   4553 N  N   . PHE B 1 136 ? 67.438 -64.549 3.630   1.00 28.87  ?  136 PHE B N   1 
ATOM   4554 C  CA  . PHE B 1 136 ? 66.545 -63.482 4.070   1.00 26.62  ?  136 PHE B CA  1 
ATOM   4555 C  C   . PHE B 1 136 ? 67.315 -62.173 4.230   1.00 25.78  ?  136 PHE B C   1 
ATOM   4556 O  O   . PHE B 1 136 ? 66.919 -61.143 3.674   1.00 24.00  ?  136 PHE B O   1 
ATOM   4557 C  CB  . PHE B 1 136 ? 65.923 -63.957 5.391   1.00 25.96  ?  136 PHE B CB  1 
ATOM   4558 C  CG  . PHE B 1 136 ? 64.981 -62.961 6.045   1.00 25.72  ?  136 PHE B CG  1 
ATOM   4559 C  CD1 . PHE B 1 136 ? 63.710 -62.730 5.509   1.00 27.50  ?  136 PHE B CD1 1 
ATOM   4560 C  CD2 . PHE B 1 136 ? 65.356 -62.274 7.189   1.00 24.69  ?  136 PHE B CD2 1 
ATOM   4561 C  CE1 . PHE B 1 136 ? 62.844 -61.811 6.077   1.00 26.59  ?  136 PHE B CE1 1 
ATOM   4562 C  CE2 . PHE B 1 136 ? 64.493 -61.348 7.757   1.00 25.84  ?  136 PHE B CE2 1 
ATOM   4563 C  CZ  . PHE B 1 136 ? 63.243 -61.113 7.193   1.00 28.55  ?  136 PHE B CZ  1 
ATOM   4564 N  N   . MET B 1 137 ? 68.409 -62.259 5.008   1.00 26.86  ?  137 MET B N   1 
ATOM   4565 C  CA  . MET B 1 137 ? 69.242 -61.139 5.444   1.00 26.74  ?  137 MET B CA  1 
ATOM   4566 C  C   . MET B 1 137 ? 70.086 -60.615 4.292   1.00 26.74  ?  137 MET B C   1 
ATOM   4567 O  O   . MET B 1 137 ? 70.639 -59.526 4.392   1.00 25.56  ?  137 MET B O   1 
ATOM   4568 C  CB  . MET B 1 137 ? 70.240 -61.585 6.526   1.00 27.86  ?  137 MET B CB  1 
ATOM   4569 C  CG  . MET B 1 137 ? 71.211 -60.515 7.008   1.00 25.32  ?  137 MET B CG  1 
ATOM   4570 S  SD  . MET B 1 137 ? 70.361 -59.108 7.733   1.00 20.41  ?  137 MET B SD  1 
ATOM   4571 C  CE  . MET B 1 137 ? 70.231 -59.755 9.402   1.00 21.47  ?  137 MET B CE  1 
ATOM   4572 N  N   . THR B 1 138 ? 70.215 -61.415 3.223   1.00 27.67  ?  138 THR B N   1 
ATOM   4573 C  CA  . THR B 1 138 ? 70.955 -60.964 2.059   1.00 28.00  ?  138 THR B CA  1 
ATOM   4574 C  C   . THR B 1 138 ? 70.231 -59.772 1.450   1.00 26.90  ?  138 THR B C   1 
ATOM   4575 O  O   . THR B 1 138 ? 70.876 -58.838 1.045   1.00 26.66  ?  138 THR B O   1 
ATOM   4576 C  CB  . THR B 1 138 ? 71.187 -62.074 1.033   1.00 30.17  ?  138 THR B CB  1 
ATOM   4577 O  OG1 . THR B 1 138 ? 71.776 -63.208 1.681   1.00 27.36  ?  138 THR B OG1 1 
ATOM   4578 C  CG2 . THR B 1 138 ? 72.091 -61.578 -0.089  1.00 29.89  ?  138 THR B CG2 1 
ATOM   4579 N  N   . GLU B 1 139 ? 68.900 -59.767 1.424   1.00 33.00  ?  139 GLU B N   1 
ATOM   4580 C  CA  . GLU B 1 139 ? 68.177 -58.595 0.962   1.00 37.48  ?  139 GLU B CA  1 
ATOM   4581 C  C   . GLU B 1 139 ? 68.011 -57.590 2.105   1.00 37.62  ?  139 GLU B C   1 
ATOM   4582 O  O   . GLU B 1 139 ? 68.326 -56.411 1.929   1.00 46.09  ?  139 GLU B O   1 
ATOM   4583 C  CB  . GLU B 1 139 ? 66.850 -58.971 0.298   1.00 40.68  ?  139 GLU B CB  1 
ATOM   4584 C  CG  . GLU B 1 139 ? 66.074 -57.771 -0.265  1.00 40.91  ?  139 GLU B CG  1 
ATOM   4585 C  CD  . GLU B 1 139 ? 66.858 -56.663 -0.971  1.00 39.70  ?  139 GLU B CD  1 
ATOM   4586 O  OE1 . GLU B 1 139 ? 66.503 -55.483 -0.760  1.00 36.55  ?  139 GLU B OE1 1 
ATOM   4587 O  OE2 . GLU B 1 139 ? 67.820 -56.944 -1.739  1.00 39.89  -1 139 GLU B OE2 1 
ATOM   4588 N  N   . LEU B 1 140 ? 67.506 -58.044 3.261   1.00 33.05  ?  140 LEU B N   1 
ATOM   4589 C  CA  . LEU B 1 140 ? 67.212 -57.147 4.379   1.00 31.14  ?  140 LEU B CA  1 
ATOM   4590 C  C   . LEU B 1 140 ? 68.415 -56.262 4.687   1.00 26.14  ?  140 LEU B C   1 
ATOM   4591 O  O   . LEU B 1 140 ? 68.223 -55.093 4.982   1.00 27.78  ?  140 LEU B O   1 
ATOM   4592 C  CB  . LEU B 1 140 ? 66.801 -57.914 5.640   1.00 31.57  ?  140 LEU B CB  1 
ATOM   4593 C  CG  . LEU B 1 140 ? 66.512 -57.066 6.886   1.00 32.33  ?  140 LEU B CG  1 
ATOM   4594 C  CD1 . LEU B 1 140 ? 65.214 -56.265 6.759   1.00 32.52  ?  140 LEU B CD1 1 
ATOM   4595 C  CD2 . LEU B 1 140 ? 66.455 -57.944 8.115   1.00 32.39  ?  140 LEU B CD2 1 
ATOM   4596 N  N   . CYS B 1 141 ? 69.626 -56.840 4.635   1.00 23.30  ?  141 CYS B N   1 
ATOM   4597 C  CA  . CYS B 1 141 ? 70.845 -56.246 5.170   1.00 24.07  ?  141 CYS B CA  1 
ATOM   4598 C  C   . CYS B 1 141 ? 70.956 -54.757 4.830   1.00 24.10  ?  141 CYS B C   1 
ATOM   4599 O  O   . CYS B 1 141 ? 71.226 -53.935 5.701   1.00 24.03  ?  141 CYS B O   1 
ATOM   4600 C  CB  . CYS B 1 141 ? 72.072 -56.996 4.667   1.00 25.48  ?  141 CYS B CB  1 
ATOM   4601 S  SG  . CYS B 1 141 ? 73.570 -55.982 4.662   1.00 31.96  ?  141 CYS B SG  1 
ATOM   4602 N  N   . ARG B 1 142 ? 70.684 -54.417 3.565   1.00 23.68  ?  142 ARG B N   1 
ATOM   4603 C  CA  . ARG B 1 142 ? 70.857 -53.074 3.038   1.00 22.16  ?  142 ARG B CA  1 
ATOM   4604 C  C   . ARG B 1 142 ? 69.913 -52.061 3.699   1.00 19.11  ?  142 ARG B C   1 
ATOM   4605 O  O   . ARG B 1 142 ? 70.103 -50.876 3.525   1.00 19.16  ?  142 ARG B O   1 
ATOM   4606 C  CB  . ARG B 1 142 ? 70.650 -53.095 1.507   1.00 22.81  ?  142 ARG B CB  1 
ATOM   4607 C  CG  . ARG B 1 142 ? 69.214 -53.163 0.990   1.00 21.01  ?  142 ARG B CG  1 
ATOM   4608 C  CD  . ARG B 1 142 ? 69.138 -53.133 -0.528  1.00 20.22  ?  142 ARG B CD  1 
ATOM   4609 N  NE  . ARG B 1 142 ? 69.491 -54.430 -1.114  1.00 19.72  ?  142 ARG B NE  1 
ATOM   4610 C  CZ  . ARG B 1 142 ? 70.664 -54.784 -1.649  1.00 17.27  ?  142 ARG B CZ  1 
ATOM   4611 N  NH1 . ARG B 1 142 ? 71.643 -53.908 -1.735  1.00 18.35  1  142 ARG B NH1 1 
ATOM   4612 N  NH2 . ARG B 1 142 ? 70.850 -56.000 -2.121  1.00 14.83  ?  142 ARG B NH2 1 
ATOM   4613 N  N   . HIS B 1 143 ? 68.859 -52.487 4.387   1.00 18.30  ?  143 HIS B N   1 
ATOM   4614 C  CA  . HIS B 1 143 ? 67.795 -51.555 4.744   1.00 18.74  ?  143 HIS B CA  1 
ATOM   4615 C  C   . HIS B 1 143 ? 67.815 -51.242 6.230   1.00 21.96  ?  143 HIS B C   1 
ATOM   4616 O  O   . HIS B 1 143 ? 67.026 -50.395 6.647   1.00 21.38  ?  143 HIS B O   1 
ATOM   4617 C  CB  . HIS B 1 143 ? 66.393 -52.095 4.445   1.00 15.93  ?  143 HIS B CB  1 
ATOM   4618 C  CG  . HIS B 1 143 ? 66.203 -52.521 3.028   1.00 14.59  ?  143 HIS B CG  1 
ATOM   4619 N  ND1 . HIS B 1 143 ? 66.033 -51.634 1.995   1.00 13.13  ?  143 HIS B ND1 1 
ATOM   4620 C  CD2 . HIS B 1 143 ? 66.194 -53.728 2.467   1.00 14.19  ?  143 HIS B CD2 1 
ATOM   4621 C  CE1 . HIS B 1 143 ? 65.897 -52.301 0.864   1.00 12.74  ?  143 HIS B CE1 1 
ATOM   4622 N  NE2 . HIS B 1 143 ? 65.989 -53.564 1.128   1.00 13.22  ?  143 HIS B NE2 1 
ATOM   4623 N  N   . ILE B 1 144 ? 68.713 -51.933 6.965   1.00 25.31  ?  144 ILE B N   1 
ATOM   4624 C  CA  . ILE B 1 144 ? 68.768 -51.932 8.423   1.00 26.75  ?  144 ILE B CA  1 
ATOM   4625 C  C   . ILE B 1 144 ? 70.184 -51.592 8.873   1.00 26.08  ?  144 ILE B C   1 
ATOM   4626 O  O   . ILE B 1 144 ? 71.103 -51.505 8.051   1.00 28.13  ?  144 ILE B O   1 
ATOM   4627 C  CB  . ILE B 1 144 ? 68.343 -53.304 8.979   1.00 29.89  ?  144 ILE B CB  1 
ATOM   4628 C  CG1 . ILE B 1 144 ? 69.358 -54.417 8.611   1.00 33.80  ?  144 ILE B CG1 1 
ATOM   4629 C  CG2 . ILE B 1 144 ? 66.925 -53.647 8.525   1.00 29.77  ?  144 ILE B CG2 1 
ATOM   4630 C  CD1 . ILE B 1 144 ? 69.046 -55.792 9.189   1.00 34.77  ?  144 ILE B CD1 1 
ATOM   4631 N  N   . GLY B 1 145 ? 70.354 -51.442 10.191  1.00 24.81  ?  145 GLY B N   1 
ATOM   4632 C  CA  . GLY B 1 145 ? 71.672 -51.184 10.763  1.00 26.23  ?  145 GLY B CA  1 
ATOM   4633 C  C   . GLY B 1 145 ? 71.608 -50.726 12.223  1.00 25.69  ?  145 GLY B C   1 
ATOM   4634 O  O   . GLY B 1 145 ? 70.538 -50.392 12.738  1.00 24.15  ?  145 GLY B O   1 
ATOM   4635 N  N   . ALA B 1 146 ? 72.783 -50.709 12.873  1.00 23.96  ?  146 ALA B N   1 
ATOM   4636 C  CA  . ALA B 1 146 ? 72.921 -50.296 14.262  1.00 22.43  ?  146 ALA B CA  1 
ATOM   4637 C  C   . ALA B 1 146 ? 72.231 -48.958 14.556  1.00 22.78  ?  146 ALA B C   1 
ATOM   4638 O  O   . ALA B 1 146 ? 71.787 -48.779 15.681  1.00 23.89  ?  146 ALA B O   1 
ATOM   4639 C  CB  . ALA B 1 146 ? 74.374 -50.253 14.618  1.00 21.08  ?  146 ALA B CB  1 
ATOM   4640 N  N   . ASP B 1 147 ? 72.138 -48.033 13.579  1.00 22.78  ?  147 ASP B N   1 
ATOM   4641 C  CA  . ASP B 1 147 ? 71.635 -46.686 13.830  1.00 23.72  ?  147 ASP B CA  1 
ATOM   4642 C  C   . ASP B 1 147 ? 70.391 -46.325 13.021  1.00 24.01  ?  147 ASP B C   1 
ATOM   4643 O  O   . ASP B 1 147 ? 69.942 -45.178 13.121  1.00 22.06  ?  147 ASP B O   1 
ATOM   4644 C  CB  . ASP B 1 147 ? 72.654 -45.645 13.439  1.00 24.46  ?  147 ASP B CB  1 
ATOM   4645 C  CG  . ASP B 1 147 ? 73.872 -45.654 14.324  1.00 27.90  ?  147 ASP B CG  1 
ATOM   4646 O  OD1 . ASP B 1 147 ? 73.779 -46.242 15.410  1.00 28.99  ?  147 ASP B OD1 1 
ATOM   4647 O  OD2 . ASP B 1 147 ? 74.885 -45.074 13.900  1.00 37.72  -1 147 ASP B OD2 1 
ATOM   4648 N  N   . THR B 1 148 ? 69.875 -47.310 12.255  1.00 23.99  ?  148 THR B N   1 
ATOM   4649 C  CA  . THR B 1 148 ? 68.827 -47.155 11.266  1.00 22.26  ?  148 THR B CA  1 
ATOM   4650 C  C   . THR B 1 148 ? 67.645 -48.038 11.623  1.00 23.47  ?  148 THR B C   1 
ATOM   4651 O  O   . THR B 1 148 ? 66.529 -47.517 11.716  1.00 24.81  ?  148 THR B O   1 
ATOM   4652 C  CB  . THR B 1 148 ? 69.344 -47.549 9.890   1.00 24.92  ?  148 THR B CB  1 
ATOM   4653 O  OG1 . THR B 1 148 ? 70.208 -46.483 9.505   1.00 24.76  ?  148 THR B OG1 1 
ATOM   4654 C  CG2 . THR B 1 148 ? 68.204 -47.723 8.896   1.00 26.89  ?  148 THR B CG2 1 
ATOM   4655 N  N   . ASP B 1 149 ? 67.900 -49.359 11.742  1.00 24.45  ?  149 ASP B N   1 
ATOM   4656 C  CA  . ASP B 1 149 ? 66.902 -50.331 12.179  1.00 26.78  ?  149 ASP B CA  1 
ATOM   4657 C  C   . ASP B 1 149 ? 67.563 -51.512 12.882  1.00 28.59  ?  149 ASP B C   1 
ATOM   4658 O  O   . ASP B 1 149 ? 68.374 -52.219 12.286  1.00 36.27  ?  149 ASP B O   1 
ATOM   4659 C  CB  . ASP B 1 149 ? 66.088 -50.856 11.006  1.00 29.31  ?  149 ASP B CB  1 
ATOM   4660 C  CG  . ASP B 1 149 ? 64.879 -51.700 11.373  1.00 32.75  ?  149 ASP B CG  1 
ATOM   4661 O  OD1 . ASP B 1 149 ? 64.689 -51.931 12.574  1.00 38.67  ?  149 ASP B OD1 1 
ATOM   4662 O  OD2 . ASP B 1 149 ? 64.124 -52.110 10.459  1.00 38.73  -1 149 ASP B OD2 1 
ATOM   4663 N  N   . VAL B 1 150 ? 67.179 -51.759 14.138  1.00 29.42  ?  150 VAL B N   1 
ATOM   4664 C  CA  . VAL B 1 150 ? 67.681 -52.896 14.902  1.00 28.90  ?  150 VAL B CA  1 
ATOM   4665 C  C   . VAL B 1 150 ? 66.568 -53.933 15.127  1.00 29.70  ?  150 VAL B C   1 
ATOM   4666 O  O   . VAL B 1 150 ? 65.808 -53.839 16.095  1.00 26.73  ?  150 VAL B O   1 
ATOM   4667 C  CB  . VAL B 1 150 ? 68.267 -52.377 16.226  1.00 29.03  ?  150 VAL B CB  1 
ATOM   4668 C  CG1 . VAL B 1 150 ? 68.769 -53.514 17.098  1.00 29.80  ?  150 VAL B CG1 1 
ATOM   4669 C  CG2 . VAL B 1 150 ? 69.374 -51.342 16.011  1.00 29.29  ?  150 VAL B CG2 1 
ATOM   4670 N  N   . PRO B 1 151 ? 66.427 -54.957 14.239  1.00 30.04  ?  151 PRO B N   1 
ATOM   4671 C  CA  . PRO B 1 151 ? 65.432 -56.019 14.419  1.00 27.89  ?  151 PRO B CA  1 
ATOM   4672 C  C   . PRO B 1 151 ? 65.679 -56.870 15.660  1.00 25.56  ?  151 PRO B C   1 
ATOM   4673 O  O   . PRO B 1 151 ? 66.696 -56.691 16.327  1.00 24.18  ?  151 PRO B O   1 
ATOM   4674 C  CB  . PRO B 1 151 ? 65.556 -56.859 13.115  1.00 28.12  ?  151 PRO B CB  1 
ATOM   4675 C  CG  . PRO B 1 151 ? 66.190 -55.930 12.119  1.00 30.16  ?  151 PRO B CG  1 
ATOM   4676 C  CD  . PRO B 1 151 ? 67.157 -55.106 12.966  1.00 30.83  ?  151 PRO B CD  1 
ATOM   4677 N  N   . ALA B 1 152 ? 64.759 -57.814 15.926  1.00 23.96  ?  152 ALA B N   1 
ATOM   4678 C  CA  . ALA B 1 152 ? 64.902 -58.743 17.037  1.00 25.61  ?  152 ALA B CA  1 
ATOM   4679 C  C   . ALA B 1 152 ? 64.162 -60.050 16.773  1.00 28.88  ?  152 ALA B C   1 
ATOM   4680 O  O   . ALA B 1 152 ? 63.738 -60.329 15.636  1.00 28.73  ?  152 ALA B O   1 
ATOM   4681 C  CB  . ALA B 1 152 ? 64.401 -58.119 18.320  1.00 25.20  ?  152 ALA B CB  1 
ATOM   4682 N  N   . GLY B 1 153 ? 64.059 -60.837 17.864  1.00 29.54  ?  153 GLY B N   1 
ATOM   4683 C  CA  . GLY B 1 153 ? 63.318 -62.092 17.919  1.00 29.21  ?  153 GLY B CA  1 
ATOM   4684 C  C   . GLY B 1 153 ? 61.820 -61.894 18.148  1.00 30.46  ?  153 GLY B C   1 
ATOM   4685 O  O   . GLY B 1 153 ? 61.391 -60.849 18.652  1.00 31.13  ?  153 GLY B O   1 
ATOM   4686 N  N   . ASP B 1 154 ? 61.056 -62.919 17.726  1.00 32.04  ?  154 ASP B N   1 
ATOM   4687 C  CA  . ASP B 1 154 ? 59.605 -62.993 17.826  1.00 33.48  ?  154 ASP B CA  1 
ATOM   4688 C  C   . ASP B 1 154 ? 59.199 -64.444 17.507  1.00 34.15  ?  154 ASP B C   1 
ATOM   4689 O  O   . ASP B 1 154 ? 60.049 -65.333 17.538  1.00 30.94  ?  154 ASP B O   1 
ATOM   4690 C  CB  . ASP B 1 154 ? 58.987 -61.876 17.000  1.00 40.28  ?  154 ASP B CB  1 
ATOM   4691 C  CG  . ASP B 1 154 ? 57.472 -61.696 17.068  1.00 51.86  ?  154 ASP B CG  1 
ATOM   4692 O  OD1 . ASP B 1 154 ? 56.862 -62.001 18.116  1.00 51.62  ?  154 ASP B OD1 1 
ATOM   4693 O  OD2 . ASP B 1 154 ? 56.889 -61.284 16.040  1.00 64.28  -1 154 ASP B OD2 1 
ATOM   4694 N  N   . ILE B 1 155 ? 57.908 -64.716 17.227  1.00 36.13  ?  155 ILE B N   1 
ATOM   4695 C  CA  . ILE B 1 155 ? 57.446 -66.068 16.912  1.00 33.21  ?  155 ILE B CA  1 
ATOM   4696 C  C   . ILE B 1 155 ? 58.153 -66.512 15.635  1.00 29.08  ?  155 ILE B C   1 
ATOM   4697 O  O   . ILE B 1 155 ? 58.089 -65.815 14.631  1.00 25.87  ?  155 ILE B O   1 
ATOM   4698 C  CB  . ILE B 1 155 ? 55.907 -66.163 16.766  1.00 35.82  ?  155 ILE B CB  1 
ATOM   4699 C  CG1 . ILE B 1 155 ? 55.146 -65.625 17.990  1.00 38.83  ?  155 ILE B CG1 1 
ATOM   4700 C  CG2 . ILE B 1 155 ? 55.448 -67.586 16.452  1.00 32.11  ?  155 ILE B CG2 1 
ATOM   4701 C  CD1 . ILE B 1 155 ? 53.633 -65.573 17.801  1.00 38.82  ?  155 ILE B CD1 1 
ATOM   4702 N  N   . GLY B 1 156 ? 58.862 -67.646 15.717  1.00 28.34  ?  156 GLY B N   1 
ATOM   4703 C  CA  . GLY B 1 156 ? 59.527 -68.262 14.583  1.00 27.62  ?  156 GLY B CA  1 
ATOM   4704 C  C   . GLY B 1 156 ? 61.033 -68.038 14.600  1.00 29.18  ?  156 GLY B C   1 
ATOM   4705 O  O   . GLY B 1 156 ? 61.783 -68.796 13.976  1.00 33.69  ?  156 GLY B O   1 
ATOM   4706 N  N   . VAL B 1 157 ? 61.489 -67.015 15.335  1.00 30.41  ?  157 VAL B N   1 
ATOM   4707 C  CA  . VAL B 1 157 ? 62.894 -66.628 15.288  1.00 31.83  ?  157 VAL B CA  1 
ATOM   4708 C  C   . VAL B 1 157 ? 63.447 -66.393 16.704  1.00 34.92  ?  157 VAL B C   1 
ATOM   4709 O  O   . VAL B 1 157 ? 62.942 -65.573 17.476  1.00 38.16  ?  157 VAL B O   1 
ATOM   4710 C  CB  . VAL B 1 157 ? 63.037 -65.411 14.348  1.00 30.62  ?  157 VAL B CB  1 
ATOM   4711 C  CG1 . VAL B 1 157 ? 61.837 -65.229 13.433  1.00 31.14  ?  157 VAL B CG1 1 
ATOM   4712 C  CG2 . VAL B 1 157 ? 63.296 -64.106 15.071  1.00 34.23  ?  157 VAL B CG2 1 
ATOM   4713 N  N   . THR B 1 158 ? 64.507 -67.129 17.053  1.00 35.43  ?  158 THR B N   1 
ATOM   4714 C  CA  . THR B 1 158 ? 65.018 -67.156 18.420  1.00 36.03  ?  158 THR B CA  1 
ATOM   4715 C  C   . THR B 1 158 ? 66.526 -66.916 18.400  1.00 33.96  ?  158 THR B C   1 
ATOM   4716 O  O   . THR B 1 158 ? 67.115 -66.596 17.374  1.00 34.27  ?  158 THR B O   1 
ATOM   4717 C  CB  . THR B 1 158 ? 64.644 -68.495 19.064  1.00 36.53  ?  158 THR B CB  1 
ATOM   4718 O  OG1 . THR B 1 158 ? 65.187 -69.569 18.301  1.00 39.97  ?  158 THR B OG1 1 
ATOM   4719 C  CG2 . THR B 1 158 ? 63.144 -68.721 19.097  1.00 35.42  ?  158 THR B CG2 1 
ATOM   4720 N  N   . GLY B 1 159 ? 67.167 -67.063 19.548  1.00 35.42  ?  159 GLY B N   1 
ATOM   4721 C  CA  . GLY B 1 159 ? 68.619 -67.015 19.596  1.00 40.47  ?  159 GLY B CA  1 
ATOM   4722 C  C   . GLY B 1 159 ? 69.271 -67.731 18.411  1.00 38.28  ?  159 GLY B C   1 
ATOM   4723 O  O   . GLY B 1 159 ? 70.271 -67.249 17.889  1.00 41.91  ?  159 GLY B O   1 
ATOM   4724 N  N   . ARG B 1 160 ? 68.699 -68.875 18.013  1.00 34.45  ?  160 ARG B N   1 
ATOM   4725 C  CA  . ARG B 1 160 ? 69.202 -69.684 16.909  1.00 33.74  ?  160 ARG B CA  1 
ATOM   4726 C  C   . ARG B 1 160 ? 69.268 -68.860 15.627  1.00 29.70  ?  160 ARG B C   1 
ATOM   4727 O  O   . ARG B 1 160 ? 70.315 -68.793 14.990  1.00 28.11  ?  160 ARG B O   1 
ATOM   4728 C  CB  . ARG B 1 160 ? 68.333 -70.945 16.731  1.00 35.11  ?  160 ARG B CB  1 
ATOM   4729 C  CG  . ARG B 1 160 ? 68.688 -71.793 15.516  1.00 37.11  ?  160 ARG B CG  1 
ATOM   4730 C  CD  . ARG B 1 160 ? 68.157 -73.221 15.506  1.00 39.19  ?  160 ARG B CD  1 
ATOM   4731 N  NE  . ARG B 1 160 ? 66.759 -73.360 15.078  1.00 41.76  ?  160 ARG B NE  1 
ATOM   4732 C  CZ  . ARG B 1 160 ? 65.665 -73.226 15.836  1.00 44.83  ?  160 ARG B CZ  1 
ATOM   4733 N  NH1 . ARG B 1 160 ? 65.733 -72.849 17.105  1.00 51.78  1  160 ARG B NH1 1 
ATOM   4734 N  NH2 . ARG B 1 160 ? 64.481 -73.480 15.318  1.00 42.62  ?  160 ARG B NH2 1 
ATOM   4735 N  N   . GLU B 1 161 ? 68.124 -68.270 15.268  1.00 30.16  ?  161 GLU B N   1 
ATOM   4736 C  CA  . GLU B 1 161 ? 67.919 -67.605 13.993  1.00 30.88  ?  161 GLU B CA  1 
ATOM   4737 C  C   . GLU B 1 161 ? 68.668 -66.276 14.010  1.00 31.72  ?  161 GLU B C   1 
ATOM   4738 O  O   . GLU B 1 161 ? 69.268 -65.922 12.992  1.00 32.57  ?  161 GLU B O   1 
ATOM   4739 C  CB  . GLU B 1 161 ? 66.436 -67.370 13.680  1.00 32.12  ?  161 GLU B CB  1 
ATOM   4740 C  CG  . GLU B 1 161 ? 65.618 -68.629 13.373  1.00 33.04  ?  161 GLU B CG  1 
ATOM   4741 C  CD  . GLU B 1 161 ? 65.215 -69.530 14.543  1.00 38.19  ?  161 GLU B CD  1 
ATOM   4742 O  OE1 . GLU B 1 161 ? 65.229 -69.072 15.713  1.00 38.28  ?  161 GLU B OE1 1 
ATOM   4743 O  OE2 . GLU B 1 161 ? 64.905 -70.727 14.304  1.00 40.27  -1 161 GLU B OE2 1 
ATOM   4744 N  N   . ILE B 1 162 ? 68.627 -65.579 15.170  1.00 31.23  ?  162 ILE B N   1 
ATOM   4745 C  CA  . ILE B 1 162 ? 69.300 -64.295 15.399  1.00 29.24  ?  162 ILE B CA  1 
ATOM   4746 C  C   . ILE B 1 162 ? 70.798 -64.477 15.153  1.00 30.35  ?  162 ILE B C   1 
ATOM   4747 O  O   . ILE B 1 162 ? 71.457 -63.575 14.626  1.00 31.59  ?  162 ILE B O   1 
ATOM   4748 C  CB  . ILE B 1 162 ? 69.018 -63.742 16.825  1.00 27.54  ?  162 ILE B CB  1 
ATOM   4749 C  CG1 . ILE B 1 162 ? 67.598 -63.208 16.965  1.00 24.83  ?  162 ILE B CG1 1 
ATOM   4750 C  CG2 . ILE B 1 162 ? 70.031 -62.682 17.302  1.00 25.66  ?  162 ILE B CG2 1 
ATOM   4751 C  CD1 . ILE B 1 162 ? 67.314 -62.004 16.097  1.00 25.28  ?  162 ILE B CD1 1 
ATOM   4752 N  N   . GLY B 1 163 ? 71.320 -65.650 15.543  1.00 27.68  ?  163 GLY B N   1 
ATOM   4753 C  CA  . GLY B 1 163 ? 72.703 -66.016 15.280  1.00 27.62  ?  163 GLY B CA  1 
ATOM   4754 C  C   . GLY B 1 163 ? 73.003 -66.017 13.786  1.00 27.18  ?  163 GLY B C   1 
ATOM   4755 O  O   . GLY B 1 163 ? 73.894 -65.301 13.302  1.00 28.80  ?  163 GLY B O   1 
ATOM   4756 N  N   . TYR B 1 164 ? 72.217 -66.810 13.064  1.00 24.84  ?  164 TYR B N   1 
ATOM   4757 C  CA  . TYR B 1 164 ? 72.417 -66.970 11.636  1.00 24.38  ?  164 TYR B CA  1 
ATOM   4758 C  C   . TYR B 1 164 ? 72.206 -65.628 10.926  1.00 24.70  ?  164 TYR B C   1 
ATOM   4759 O  O   . TYR B 1 164 ? 72.942 -65.294 9.991   1.00 24.47  ?  164 TYR B O   1 
ATOM   4760 C  CB  . TYR B 1 164 ? 71.449 -68.030 11.107  1.00 23.21  ?  164 TYR B CB  1 
ATOM   4761 C  CG  . TYR B 1 164 ? 71.558 -69.430 11.689  1.00 21.78  ?  164 TYR B CG  1 
ATOM   4762 C  CD1 . TYR B 1 164 ? 72.786 -70.018 11.952  1.00 21.87  ?  164 TYR B CD1 1 
ATOM   4763 C  CD2 . TYR B 1 164 ? 70.411 -70.192 11.910  1.00 22.30  ?  164 TYR B CD2 1 
ATOM   4764 C  CE1 . TYR B 1 164 ? 72.871 -71.321 12.418  1.00 22.48  ?  164 TYR B CE1 1 
ATOM   4765 C  CE2 . TYR B 1 164 ? 70.477 -71.492 12.382  1.00 21.83  ?  164 TYR B CE2 1 
ATOM   4766 C  CZ  . TYR B 1 164 ? 71.712 -72.054 12.651  1.00 22.55  ?  164 TYR B CZ  1 
ATOM   4767 O  OH  . TYR B 1 164 ? 71.784 -73.333 13.130  1.00 20.74  ?  164 TYR B OH  1 
ATOM   4768 N  N   . LEU B 1 165 ? 71.185 -64.871 11.349  1.00 23.42  ?  165 LEU B N   1 
ATOM   4769 C  CA  . LEU B 1 165 ? 70.967 -63.541 10.804  1.00 25.16  ?  165 LEU B CA  1 
ATOM   4770 C  C   . LEU B 1 165 ? 72.220 -62.681 11.018  1.00 25.62  ?  165 LEU B C   1 
ATOM   4771 O  O   . LEU B 1 165 ? 72.747 -62.106 10.077  1.00 27.68  ?  165 LEU B O   1 
ATOM   4772 C  CB  . LEU B 1 165 ? 69.725 -62.907 11.433  1.00 25.95  ?  165 LEU B CB  1 
ATOM   4773 C  CG  . LEU B 1 165 ? 68.374 -63.575 11.128  1.00 24.97  ?  165 LEU B CG  1 
ATOM   4774 C  CD1 . LEU B 1 165 ? 67.315 -62.908 11.969  1.00 22.90  ?  165 LEU B CD1 1 
ATOM   4775 C  CD2 . LEU B 1 165 ? 67.961 -63.550 9.657   1.00 25.74  ?  165 LEU B CD2 1 
ATOM   4776 N  N   . PHE B 1 166 ? 72.739 -62.640 12.247  1.00 24.37  ?  166 PHE B N   1 
ATOM   4777 C  CA  . PHE B 1 166 ? 73.819 -61.729 12.584  1.00 22.74  ?  166 PHE B CA  1 
ATOM   4778 C  C   . PHE B 1 166 ? 75.090 -62.119 11.832  1.00 22.84  ?  166 PHE B C   1 
ATOM   4779 O  O   . PHE B 1 166 ? 75.889 -61.242 11.509  1.00 23.73  ?  166 PHE B O   1 
ATOM   4780 C  CB  . PHE B 1 166 ? 74.068 -61.698 14.098  1.00 21.48  ?  166 PHE B CB  1 
ATOM   4781 C  CG  . PHE B 1 166 ? 75.272 -60.874 14.532  1.00 19.32  ?  166 PHE B CG  1 
ATOM   4782 C  CD1 . PHE B 1 166 ? 75.162 -59.511 14.726  1.00 18.71  ?  166 PHE B CD1 1 
ATOM   4783 C  CD2 . PHE B 1 166 ? 76.508 -61.472 14.777  1.00 19.93  ?  166 PHE B CD2 1 
ATOM   4784 C  CE1 . PHE B 1 166 ? 76.259 -58.761 15.142  1.00 19.50  ?  166 PHE B CE1 1 
ATOM   4785 C  CE2 . PHE B 1 166 ? 77.603 -60.723 15.200  1.00 19.08  ?  166 PHE B CE2 1 
ATOM   4786 C  CZ  . PHE B 1 166 ? 77.482 -59.368 15.375  1.00 18.93  ?  166 PHE B CZ  1 
ATOM   4787 N  N   . GLY B 1 167 ? 75.317 -63.426 11.628  1.00 21.91  ?  167 GLY B N   1 
ATOM   4788 C  CA  . GLY B 1 167 ? 76.498 -63.885 10.906  1.00 20.89  ?  167 GLY B CA  1 
ATOM   4789 C  C   . GLY B 1 167 ? 76.505 -63.388 9.459   1.00 20.31  ?  167 GLY B C   1 
ATOM   4790 O  O   . GLY B 1 167 ? 77.548 -62.986 8.957   1.00 19.54  ?  167 GLY B O   1 
ATOM   4791 N  N   . GLN B 1 168 ? 75.335 -63.412 8.802   1.00 19.48  ?  168 GLN B N   1 
ATOM   4792 C  CA  . GLN B 1 168 ? 75.234 -63.071 7.392   1.00 20.32  ?  168 GLN B CA  1 
ATOM   4793 C  C   . GLN B 1 168 ? 75.322 -61.552 7.202   1.00 21.59  ?  168 GLN B C   1 
ATOM   4794 O  O   . GLN B 1 168 ? 75.987 -61.080 6.279   1.00 23.79  ?  168 GLN B O   1 
ATOM   4795 C  CB  . GLN B 1 168 ? 73.951 -63.691 6.830   1.00 20.65  ?  168 GLN B CB  1 
ATOM   4796 C  CG  . GLN B 1 168 ? 73.673 -63.394 5.356   1.00 21.59  ?  168 GLN B CG  1 
ATOM   4797 C  CD  . GLN B 1 168 ? 74.722 -63.893 4.384   1.00 20.58  ?  168 GLN B CD  1 
ATOM   4798 O  OE1 . GLN B 1 168 ? 75.749 -64.454 4.757   1.00 20.06  ?  168 GLN B OE1 1 
ATOM   4799 N  NE2 . GLN B 1 168 ? 74.477 -63.681 3.102   1.00 22.15  ?  168 GLN B NE2 1 
ATOM   4800 N  N   . TYR B 1 169 ? 74.638 -60.796 8.064   1.00 21.26  ?  169 TYR B N   1 
ATOM   4801 C  CA  . TYR B 1 169 ? 74.827 -59.357 8.166   1.00 24.44  ?  169 TYR B CA  1 
ATOM   4802 C  C   . TYR B 1 169 ? 76.316 -59.019 8.275   1.00 24.22  ?  169 TYR B C   1 
ATOM   4803 O  O   . TYR B 1 169 ? 76.841 -58.306 7.427   1.00 24.17  ?  169 TYR B O   1 
ATOM   4804 C  CB  . TYR B 1 169 ? 74.085 -58.750 9.368   1.00 25.81  ?  169 TYR B CB  1 
ATOM   4805 C  CG  . TYR B 1 169 ? 74.142 -57.233 9.389   1.00 25.19  ?  169 TYR B CG  1 
ATOM   4806 C  CD1 . TYR B 1 169 ? 73.243 -56.483 8.645   1.00 25.72  ?  169 TYR B CD1 1 
ATOM   4807 C  CD2 . TYR B 1 169 ? 75.135 -56.555 10.092  1.00 25.97  ?  169 TYR B CD2 1 
ATOM   4808 C  CE1 . TYR B 1 169 ? 73.300 -55.098 8.642   1.00 28.35  ?  169 TYR B CE1 1 
ATOM   4809 C  CE2 . TYR B 1 169 ? 75.215 -55.169 10.088  1.00 26.03  ?  169 TYR B CE2 1 
ATOM   4810 C  CZ  . TYR B 1 169 ? 74.293 -54.432 9.359   1.00 28.76  ?  169 TYR B CZ  1 
ATOM   4811 O  OH  . TYR B 1 169 ? 74.366 -53.055 9.363   1.00 28.09  ?  169 TYR B OH  1 
ATOM   4812 N  N   . ARG B 1 170 ? 76.980 -59.529 9.320   1.00 25.44  ?  170 ARG B N   1 
ATOM   4813 C  CA  . ARG B 1 170 ? 78.396 -59.264 9.582   1.00 28.04  ?  170 ARG B CA  1 
ATOM   4814 C  C   . ARG B 1 170 ? 79.238 -59.448 8.326   1.00 30.64  ?  170 ARG B C   1 
ATOM   4815 O  O   . ARG B 1 170 ? 80.096 -58.615 8.038   1.00 31.98  ?  170 ARG B O   1 
ATOM   4816 C  CB  . ARG B 1 170 ? 78.950 -60.166 10.691  1.00 27.73  ?  170 ARG B CB  1 
ATOM   4817 C  CG  . ARG B 1 170 ? 80.465 -60.178 10.846  1.00 28.82  ?  170 ARG B CG  1 
ATOM   4818 C  CD  . ARG B 1 170 ? 80.932 -60.818 12.162  1.00 27.58  ?  170 ARG B CD  1 
ATOM   4819 N  NE  . ARG B 1 170 ? 80.530 -62.226 12.303  1.00 26.76  ?  170 ARG B NE  1 
ATOM   4820 C  CZ  . ARG B 1 170 ? 81.142 -63.309 11.798  1.00 24.59  ?  170 ARG B CZ  1 
ATOM   4821 N  NH1 . ARG B 1 170 ? 82.297 -63.201 11.178  1.00 24.25  1  170 ARG B NH1 1 
ATOM   4822 N  NH2 . ARG B 1 170 ? 80.632 -64.515 11.980  1.00 22.75  ?  170 ARG B NH2 1 
ATOM   4823 N  N   . LYS B 1 171 ? 78.955 -60.531 7.595   1.00 33.56  ?  171 LYS B N   1 
ATOM   4824 C  CA  . LYS B 1 171 ? 79.747 -60.956 6.454   1.00 36.42  ?  171 LYS B CA  1 
ATOM   4825 C  C   . LYS B 1 171 ? 79.415 -60.106 5.232   1.00 31.60  ?  171 LYS B C   1 
ATOM   4826 O  O   . LYS B 1 171 ? 80.242 -59.986 4.345   1.00 32.38  ?  171 LYS B O   1 
ATOM   4827 C  CB  . LYS B 1 171 ? 79.476 -62.446 6.196   1.00 45.74  ?  171 LYS B CB  1 
ATOM   4828 C  CG  . LYS B 1 171 ? 80.484 -63.175 5.313   1.00 55.24  ?  171 LYS B CG  1 
ATOM   4829 C  CD  . LYS B 1 171 ? 80.164 -64.651 5.072   1.00 63.78  ?  171 LYS B CD  1 
ATOM   4830 C  CE  . LYS B 1 171 ? 80.966 -65.275 3.953   1.00 66.89  ?  171 LYS B CE  1 
ATOM   4831 N  NZ  . LYS B 1 171 ? 80.217 -66.371 3.327   1.00 68.39  1  171 LYS B NZ  1 
ATOM   4832 N  N   . LEU B 1 172 ? 78.200 -59.554 5.156   1.00 28.81  ?  172 LEU B N   1 
ATOM   4833 C  CA  . LEU B 1 172 ? 77.834 -58.678 4.048   1.00 28.81  ?  172 LEU B CA  1 
ATOM   4834 C  C   . LEU B 1 172 ? 78.371 -57.273 4.288   1.00 30.32  ?  172 LEU B C   1 
ATOM   4835 O  O   . LEU B 1 172 ? 79.041 -56.681 3.439   1.00 29.74  ?  172 LEU B O   1 
ATOM   4836 C  CB  . LEU B 1 172 ? 76.318 -58.660 3.880   1.00 26.96  ?  172 LEU B CB  1 
ATOM   4837 C  CG  . LEU B 1 172 ? 75.738 -59.676 2.890   1.00 26.70  ?  172 LEU B CG  1 
ATOM   4838 C  CD1 . LEU B 1 172 ? 76.702 -60.807 2.652   1.00 27.44  ?  172 LEU B CD1 1 
ATOM   4839 C  CD2 . LEU B 1 172 ? 74.406 -60.233 3.365   1.00 26.35  ?  172 LEU B CD2 1 
ATOM   4840 N  N   . ARG B 1 173 ? 78.059 -56.768 5.477   1.00 33.56  ?  173 ARG B N   1 
ATOM   4841 C  CA  . ARG B 1 173 ? 78.383 -55.414 5.881   1.00 34.58  ?  173 ARG B CA  1 
ATOM   4842 C  C   . ARG B 1 173 ? 79.862 -55.293 6.247   1.00 29.63  ?  173 ARG B C   1 
ATOM   4843 O  O   . ARG B 1 173 ? 80.419 -54.209 6.165   1.00 25.29  ?  173 ARG B O   1 
ATOM   4844 C  CB  . ARG B 1 173 ? 77.428 -55.070 7.029   1.00 39.92  ?  173 ARG B CB  1 
ATOM   4845 C  CG  . ARG B 1 173 ? 77.457 -53.620 7.489   1.00 46.78  ?  173 ARG B CG  1 
ATOM   4846 C  CD  . ARG B 1 173 ? 76.816 -52.661 6.506   1.00 47.10  ?  173 ARG B CD  1 
ATOM   4847 N  NE  . ARG B 1 173 ? 75.359 -52.831 6.431   1.00 47.67  ?  173 ARG B NE  1 
ATOM   4848 C  CZ  . ARG B 1 173 ? 74.459 -51.839 6.425   1.00 46.34  ?  173 ARG B CZ  1 
ATOM   4849 N  NH1 . ARG B 1 173 ? 74.834 -50.580 6.562   1.00 48.30  1  173 ARG B NH1 1 
ATOM   4850 N  NH2 . ARG B 1 173 ? 73.171 -52.097 6.290   1.00 42.59  ?  173 ARG B NH2 1 
ATOM   4851 N  N   . ASN B 1 174 ? 80.515 -56.401 6.605   1.00 29.10  ?  174 ASN B N   1 
ATOM   4852 C  CA  . ASN B 1 174 ? 81.889 -56.366 7.112   1.00 30.60  ?  174 ASN B CA  1 
ATOM   4853 C  C   . ASN B 1 174 ? 81.958 -55.465 8.345   1.00 29.47  ?  174 ASN B C   1 
ATOM   4854 O  O   . ASN B 1 174 ? 82.856 -54.626 8.445   1.00 30.21  ?  174 ASN B O   1 
ATOM   4855 C  CB  . ASN B 1 174 ? 82.951 -55.918 6.094   1.00 29.23  ?  174 ASN B CB  1 
ATOM   4856 C  CG  . ASN B 1 174 ? 84.387 -56.235 6.496   1.00 25.86  ?  174 ASN B CG  1 
ATOM   4857 O  OD1 . ASN B 1 174 ? 84.648 -57.042 7.398   1.00 21.89  ?  174 ASN B OD1 1 
ATOM   4858 N  ND2 . ASN B 1 174 ? 85.350 -55.652 5.794   1.00 24.17  ?  174 ASN B ND2 1 
ATOM   4859 N  N   . SER B 1 175 ? 81.044 -55.696 9.298   1.00 26.84  ?  175 SER B N   1 
ATOM   4860 C  CA  . SER B 1 175 ? 80.912 -54.825 10.453  1.00 24.79  ?  175 SER B CA  1 
ATOM   4861 C  C   . SER B 1 175 ? 80.388 -55.610 11.653  1.00 22.72  ?  175 SER B C   1 
ATOM   4862 O  O   . SER B 1 175 ? 79.426 -56.355 11.510  1.00 20.94  ?  175 SER B O   1 
ATOM   4863 C  CB  . SER B 1 175 ? 80.002 -53.667 10.127  1.00 24.23  ?  175 SER B CB  1 
ATOM   4864 O  OG  . SER B 1 175 ? 79.939 -52.773 11.226  1.00 24.65  ?  175 SER B OG  1 
ATOM   4865 N  N   . TRP B 1 176 ? 81.004 -55.402 12.831  1.00 21.75  ?  176 TRP B N   1 
ATOM   4866 C  CA  . TRP B 1 176 ? 80.456 -55.878 14.094  1.00 22.67  ?  176 TRP B CA  1 
ATOM   4867 C  C   . TRP B 1 176 ? 79.749 -54.730 14.837  1.00 24.39  ?  176 TRP B C   1 
ATOM   4868 O  O   . TRP B 1 176 ? 80.389 -53.882 15.462  1.00 23.17  ?  176 TRP B O   1 
ATOM   4869 C  CB  . TRP B 1 176 ? 81.575 -56.505 14.933  1.00 23.33  ?  176 TRP B CB  1 
ATOM   4870 C  CG  . TRP B 1 176 ? 81.116 -57.588 15.880  1.00 23.57  ?  176 TRP B CG  1 
ATOM   4871 C  CD1 . TRP B 1 176 ? 81.125 -58.944 15.689  1.00 24.33  ?  176 TRP B CD1 1 
ATOM   4872 C  CD2 . TRP B 1 176 ? 80.567 -57.382 17.194  1.00 22.63  ?  176 TRP B CD2 1 
ATOM   4873 N  NE1 . TRP B 1 176 ? 80.634 -59.596 16.793  1.00 23.45  ?  176 TRP B NE1 1 
ATOM   4874 C  CE2 . TRP B 1 176 ? 80.269 -58.660 17.726  1.00 23.74  ?  176 TRP B CE2 1 
ATOM   4875 C  CE3 . TRP B 1 176 ? 80.295 -56.246 17.959  1.00 21.96  ?  176 TRP B CE3 1 
ATOM   4876 C  CZ2 . TRP B 1 176 ? 79.700 -58.820 18.990  1.00 23.45  ?  176 TRP B CZ2 1 
ATOM   4877 C  CZ3 . TRP B 1 176 ? 79.737 -56.409 19.207  1.00 23.00  ?  176 TRP B CZ3 1 
ATOM   4878 C  CH2 . TRP B 1 176 ? 79.438 -57.679 19.714  1.00 23.03  ?  176 TRP B CH2 1 
ATOM   4879 N  N   . GLU B 1 177 ? 78.408 -54.724 14.777  1.00 24.95  ?  177 GLU B N   1 
ATOM   4880 C  CA  . GLU B 1 177 ? 77.588 -53.645 15.310  1.00 26.73  ?  177 GLU B CA  1 
ATOM   4881 C  C   . GLU B 1 177 ? 76.275 -54.210 15.848  1.00 27.02  ?  177 GLU B C   1 
ATOM   4882 O  O   . GLU B 1 177 ? 75.843 -55.282 15.420  1.00 25.08  ?  177 GLU B O   1 
ATOM   4883 C  CB  . GLU B 1 177 ? 77.249 -52.656 14.196  1.00 27.74  ?  177 GLU B CB  1 
ATOM   4884 C  CG  . GLU B 1 177 ? 76.486 -53.305 13.042  1.00 27.86  ?  177 GLU B CG  1 
ATOM   4885 C  CD  . GLU B 1 177 ? 75.992 -52.328 11.992  1.00 28.83  ?  177 GLU B CD  1 
ATOM   4886 O  OE1 . GLU B 1 177 ? 76.806 -51.537 11.509  1.00 24.03  ?  177 GLU B OE1 1 
ATOM   4887 O  OE2 . GLU B 1 177 ? 74.783 -52.371 11.648  1.00 39.52  -1 177 GLU B OE2 1 
ATOM   4888 N  N   . GLY B 1 178 ? 75.623 -53.456 16.747  1.00 27.79  ?  178 GLY B N   1 
ATOM   4889 C  CA  . GLY B 1 178 ? 74.393 -53.914 17.387  1.00 27.15  ?  178 GLY B CA  1 
ATOM   4890 C  C   . GLY B 1 178 ? 73.189 -53.823 16.451  1.00 25.09  ?  178 GLY B C   1 
ATOM   4891 O  O   . GLY B 1 178 ? 72.237 -53.117 16.776  1.00 23.74  ?  178 GLY B O   1 
ATOM   4892 N  N   . VAL B 1 179 ? 73.260 -54.532 15.304  1.00 24.58  ?  179 VAL B N   1 
ATOM   4893 C  CA  . VAL B 1 179 ? 72.208 -54.530 14.284  1.00 23.35  ?  179 VAL B CA  1 
ATOM   4894 C  C   . VAL B 1 179 ? 71.004 -55.366 14.723  1.00 22.58  ?  179 VAL B C   1 
ATOM   4895 O  O   . VAL B 1 179 ? 69.919 -55.138 14.219  1.00 27.05  ?  179 VAL B O   1 
ATOM   4896 C  CB  . VAL B 1 179 ? 72.697 -55.015 12.907  1.00 20.71  ?  179 VAL B CB  1 
ATOM   4897 C  CG1 . VAL B 1 179 ? 73.262 -56.423 12.992  1.00 20.57  ?  179 VAL B CG1 1 
ATOM   4898 C  CG2 . VAL B 1 179 ? 71.615 -54.929 11.831  1.00 19.54  ?  179 VAL B CG2 1 
ATOM   4899 N  N   . LEU B 1 180 ? 71.205 -56.348 15.609  1.00 21.15  ?  180 LEU B N   1 
ATOM   4900 C  CA  . LEU B 1 180 ? 70.158 -57.243 16.087  1.00 19.73  ?  180 LEU B CA  1 
ATOM   4901 C  C   . LEU B 1 180 ? 70.281 -57.355 17.609  1.00 19.57  ?  180 LEU B C   1 
ATOM   4902 O  O   . LEU B 1 180 ? 71.392 -57.431 18.128  1.00 20.01  ?  180 LEU B O   1 
ATOM   4903 C  CB  . LEU B 1 180 ? 70.324 -58.626 15.455  1.00 18.78  ?  180 LEU B CB  1 
ATOM   4904 C  CG  . LEU B 1 180 ? 70.184 -58.713 13.937  1.00 19.07  ?  180 LEU B CG  1 
ATOM   4905 C  CD1 . LEU B 1 180 ? 70.792 -59.994 13.379  1.00 19.24  ?  180 LEU B CD1 1 
ATOM   4906 C  CD2 . LEU B 1 180 ? 68.726 -58.612 13.561  1.00 19.35  ?  180 LEU B CD2 1 
ATOM   4907 N  N   . THR B 1 181 ? 69.146 -57.422 18.314  1.00 18.17  ?  181 THR B N   1 
ATOM   4908 C  CA  . THR B 1 181 ? 69.140 -57.740 19.733  1.00 18.32  ?  181 THR B CA  1 
ATOM   4909 C  C   . THR B 1 181 ? 68.717 -59.212 19.910  1.00 18.18  ?  181 THR B C   1 
ATOM   4910 O  O   . THR B 1 181 ? 68.365 -59.880 18.935  1.00 16.84  ?  181 THR B O   1 
ATOM   4911 C  CB  . THR B 1 181 ? 68.227 -56.717 20.406  1.00 19.08  ?  181 THR B CB  1 
ATOM   4912 O  OG1 . THR B 1 181 ? 66.984 -56.823 19.718  1.00 17.86  ?  181 THR B OG1 1 
ATOM   4913 C  CG2 . THR B 1 181 ? 68.739 -55.289 20.255  1.00 20.08  ?  181 THR B CG2 1 
ATOM   4914 N  N   . GLY B 1 182 ? 68.801 -59.748 21.138  1.00 17.73  ?  182 GLY B N   1 
ATOM   4915 C  CA  . GLY B 1 182 ? 68.550 -61.162 21.382  1.00 17.94  ?  182 GLY B CA  1 
ATOM   4916 C  C   . GLY B 1 182 ? 69.807 -62.009 21.176  1.00 18.79  ?  182 GLY B C   1 
ATOM   4917 O  O   . GLY B 1 182 ? 69.738 -63.211 20.919  1.00 18.51  ?  182 GLY B O   1 
ATOM   4918 N  N   . LYS B 1 183 ? 70.978 -61.384 21.309  1.00 19.62  ?  183 LYS B N   1 
ATOM   4919 C  CA  . LYS B 1 183 ? 72.214 -62.013 20.856  1.00 20.64  ?  183 LYS B CA  1 
ATOM   4920 C  C   . LYS B 1 183 ? 72.751 -62.909 21.964  1.00 20.91  ?  183 LYS B C   1 
ATOM   4921 O  O   . LYS B 1 183 ? 72.343 -62.761 23.108  1.00 20.03  ?  183 LYS B O   1 
ATOM   4922 C  CB  . LYS B 1 183 ? 73.245 -60.987 20.367  1.00 19.80  ?  183 LYS B CB  1 
ATOM   4923 C  CG  . LYS B 1 183 ? 72.721 -60.140 19.203  1.00 21.01  ?  183 LYS B CG  1 
ATOM   4924 C  CD  . LYS B 1 183 ? 73.765 -59.397 18.362  1.00 22.04  ?  183 LYS B CD  1 
ATOM   4925 C  CE  . LYS B 1 183 ? 74.123 -58.021 18.851  1.00 21.31  ?  183 LYS B CE  1 
ATOM   4926 N  NZ  . LYS B 1 183 ? 73.835 -57.801 20.274  1.00 20.08  1  183 LYS B NZ  1 
ATOM   4927 N  N   . GLY B 1 184 ? 73.643 -63.841 21.581  1.00 22.24  ?  184 GLY B N   1 
ATOM   4928 C  CA  . GLY B 1 184 ? 74.328 -64.736 22.501  1.00 21.67  ?  184 GLY B CA  1 
ATOM   4929 C  C   . GLY B 1 184 ? 75.278 -63.977 23.426  1.00 22.23  ?  184 GLY B C   1 
ATOM   4930 O  O   . GLY B 1 184 ? 75.701 -62.870 23.093  1.00 23.57  ?  184 GLY B O   1 
ATOM   4931 N  N   . GLY B 1 185 ? 75.598 -64.600 24.574  1.00 21.84  ?  185 GLY B N   1 
ATOM   4932 C  CA  . GLY B 1 185 ? 76.471 -64.041 25.597  1.00 21.48  ?  185 GLY B CA  1 
ATOM   4933 C  C   . GLY B 1 185 ? 77.811 -63.563 25.039  1.00 21.03  ?  185 GLY B C   1 
ATOM   4934 O  O   . GLY B 1 185 ? 78.259 -62.483 25.375  1.00 19.02  ?  185 GLY B O   1 
ATOM   4935 N  N   . SER B 1 186 ? 78.413 -64.345 24.142  1.00 23.34  ?  186 SER B N   1 
ATOM   4936 C  CA  . SER B 1 186 ? 79.790 -64.143 23.706  1.00 25.16  ?  186 SER B CA  1 
ATOM   4937 C  C   . SER B 1 186 ? 79.928 -63.115 22.577  1.00 24.73  ?  186 SER B C   1 
ATOM   4938 O  O   . SER B 1 186 ? 81.050 -62.721 22.260  1.00 21.89  ?  186 SER B O   1 
ATOM   4939 C  CB  . SER B 1 186 ? 80.355 -65.478 23.286  1.00 28.12  ?  186 SER B CB  1 
ATOM   4940 O  OG  . SER B 1 186 ? 79.413 -66.172 22.473  1.00 33.33  ?  186 SER B OG  1 
ATOM   4941 N  N   . TRP B 1 187 ? 78.797 -62.722 21.958  1.00 26.69  ?  187 TRP B N   1 
ATOM   4942 C  CA  . TRP B 1 187 ? 78.778 -61.840 20.792  1.00 27.51  ?  187 TRP B CA  1 
ATOM   4943 C  C   . TRP B 1 187 ? 77.718 -60.737 20.931  1.00 29.08  ?  187 TRP B C   1 
ATOM   4944 O  O   . TRP B 1 187 ? 76.986 -60.418 19.976  1.00 29.46  ?  187 TRP B O   1 
ATOM   4945 C  CB  . TRP B 1 187 ? 78.611 -62.631 19.476  1.00 26.05  ?  187 TRP B CB  1 
ATOM   4946 C  CG  . TRP B 1 187 ? 77.605 -63.754 19.490  1.00 23.14  ?  187 TRP B CG  1 
ATOM   4947 C  CD1 . TRP B 1 187 ? 77.782 -64.998 20.016  1.00 22.24  ?  187 TRP B CD1 1 
ATOM   4948 C  CD2 . TRP B 1 187 ? 76.286 -63.752 18.905  1.00 21.99  ?  187 TRP B CD2 1 
ATOM   4949 N  NE1 . TRP B 1 187 ? 76.659 -65.756 19.831  1.00 21.43  ?  187 TRP B NE1 1 
ATOM   4950 C  CE2 . TRP B 1 187 ? 75.722 -65.019 19.158  1.00 20.77  ?  187 TRP B CE2 1 
ATOM   4951 C  CE3 . TRP B 1 187 ? 75.517 -62.804 18.219  1.00 22.58  ?  187 TRP B CE3 1 
ATOM   4952 C  CZ2 . TRP B 1 187 ? 74.437 -65.353 18.743  1.00 19.48  ?  187 TRP B CZ2 1 
ATOM   4953 C  CZ3 . TRP B 1 187 ? 74.248 -63.141 17.798  1.00 20.74  ?  187 TRP B CZ3 1 
ATOM   4954 C  CH2 . TRP B 1 187 ? 73.723 -64.401 18.054  1.00 19.87  ?  187 TRP B CH2 1 
ATOM   4955 N  N   . GLY B 1 188 ? 77.699 -60.108 22.119  1.00 26.58  ?  188 GLY B N   1 
ATOM   4956 C  CA  . GLY B 1 188 ? 76.974 -58.867 22.334  1.00 22.79  ?  188 GLY B CA  1 
ATOM   4957 C  C   . GLY B 1 188 ? 75.580 -59.065 22.915  1.00 21.82  ?  188 GLY B C   1 
ATOM   4958 O  O   . GLY B 1 188 ? 74.777 -58.168 22.767  1.00 22.91  ?  188 GLY B O   1 
ATOM   4959 N  N   . GLY B 1 189 ? 75.291 -60.192 23.587  1.00 22.43  ?  189 GLY B N   1 
ATOM   4960 C  CA  . GLY B 1 189 ? 74.057 -60.352 24.348  1.00 22.86  ?  189 GLY B CA  1 
ATOM   4961 C  C   . GLY B 1 189 ? 74.034 -59.505 25.636  1.00 26.09  ?  189 GLY B C   1 
ATOM   4962 O  O   . GLY B 1 189 ? 75.064 -58.995 26.097  1.00 26.68  ?  189 GLY B O   1 
ATOM   4963 N  N   . SER B 1 190 ? 72.840 -59.331 26.224  1.00 25.75  ?  190 SER B N   1 
ATOM   4964 C  CA  . SER B 1 190 ? 72.721 -58.720 27.541  1.00 27.43  ?  190 SER B CA  1 
ATOM   4965 C  C   . SER B 1 190 ? 72.200 -59.739 28.557  1.00 28.51  ?  190 SER B C   1 
ATOM   4966 O  O   . SER B 1 190 ? 71.356 -60.556 28.224  1.00 28.11  ?  190 SER B O   1 
ATOM   4967 C  CB  . SER B 1 190 ? 71.833 -57.485 27.538  1.00 26.42  ?  190 SER B CB  1 
ATOM   4968 O  OG  . SER B 1 190 ? 71.496 -57.095 28.871  1.00 24.16  ?  190 SER B OG  1 
ATOM   4969 N  N   . LEU B 1 191 ? 72.684 -59.636 29.807  1.00 29.45  ?  191 LEU B N   1 
ATOM   4970 C  CA  . LEU B 1 191 ? 72.113 -60.338 30.948  1.00 29.60  ?  191 LEU B CA  1 
ATOM   4971 C  C   . LEU B 1 191 ? 70.755 -59.710 31.225  1.00 28.12  ?  191 LEU B C   1 
ATOM   4972 O  O   . LEU B 1 191 ? 70.530 -58.589 30.795  1.00 32.21  ?  191 LEU B O   1 
ATOM   4973 C  CB  . LEU B 1 191 ? 73.025 -60.306 32.180  1.00 29.04  ?  191 LEU B CB  1 
ATOM   4974 C  CG  . LEU B 1 191 ? 74.366 -61.017 31.975  1.00 29.56  ?  191 LEU B CG  1 
ATOM   4975 C  CD1 . LEU B 1 191 ? 75.327 -60.733 33.083  1.00 29.45  ?  191 LEU B CD1 1 
ATOM   4976 C  CD2 . LEU B 1 191 ? 74.179 -62.524 31.794  1.00 30.08  ?  191 LEU B CD2 1 
ATOM   4977 N  N   . ILE B 1 192 ? 69.863 -60.489 31.851  1.00 25.89  ?  192 ILE B N   1 
ATOM   4978 C  CA  . ILE B 1 192 ? 68.466 -60.153 32.087  1.00 25.92  ?  192 ILE B CA  1 
ATOM   4979 C  C   . ILE B 1 192 ? 67.608 -60.189 30.811  1.00 26.87  ?  192 ILE B C   1 
ATOM   4980 O  O   . ILE B 1 192 ? 66.413 -59.949 30.906  1.00 29.84  ?  192 ILE B O   1 
ATOM   4981 C  CB  . ILE B 1 192 ? 68.327 -58.841 32.888  1.00 25.70  ?  192 ILE B CB  1 
ATOM   4982 C  CG1 . ILE B 1 192 ? 69.072 -58.950 34.247  1.00 25.80  ?  192 ILE B CG1 1 
ATOM   4983 C  CG2 . ILE B 1 192 ? 66.863 -58.432 33.102  1.00 25.26  ?  192 ILE B CG2 1 
ATOM   4984 C  CD1 . ILE B 1 192 ? 68.495 -59.984 35.209  1.00 24.13  ?  192 ILE B CD1 1 
ATOM   4985 N  N   A ARG B 1 193 ? 68.177 -60.545 29.653  0.50 26.74  ?  193 ARG B N   1 
ATOM   4986 N  N   B ARG B 1 193 ? 68.176 -60.549 29.651  0.50 25.98  ?  193 ARG B N   1 
ATOM   4987 C  CA  A ARG B 1 193 ? 67.377 -60.702 28.446  0.50 29.17  ?  193 ARG B CA  1 
ATOM   4988 C  CA  B ARG B 1 193 ? 67.378 -60.700 28.441  0.50 27.73  ?  193 ARG B CA  1 
ATOM   4989 C  C   A ARG B 1 193 ? 66.335 -61.823 28.614  0.50 28.48  ?  193 ARG B C   1 
ATOM   4990 C  C   B ARG B 1 193 ? 66.340 -61.827 28.594  0.50 27.67  ?  193 ARG B C   1 
ATOM   4991 O  O   A ARG B 1 193 ? 65.137 -61.608 28.377  0.50 26.82  ?  193 ARG B O   1 
ATOM   4992 O  O   B ARG B 1 193 ? 65.148 -61.624 28.317  0.50 26.10  ?  193 ARG B O   1 
ATOM   4993 C  CB  A ARG B 1 193 ? 68.294 -60.907 27.233  0.50 30.41  ?  193 ARG B CB  1 
ATOM   4994 C  CB  B ARG B 1 193 ? 68.272 -60.913 27.211  0.50 27.79  ?  193 ARG B CB  1 
ATOM   4995 C  CG  A ARG B 1 193 ? 67.601 -61.592 26.065  0.50 31.21  ?  193 ARG B CG  1 
ATOM   4996 C  CG  B ARG B 1 193 ? 67.497 -61.417 26.002  0.50 27.45  ?  193 ARG B CG  1 
ATOM   4997 C  CD  A ARG B 1 193 ? 68.508 -61.710 24.854  0.50 33.44  ?  193 ARG B CD  1 
ATOM   4998 C  CD  B ARG B 1 193 ? 68.279 -62.451 25.203  0.50 28.36  ?  193 ARG B CD  1 
ATOM   4999 N  NE  A ARG B 1 193 ? 69.760 -62.449 25.071  0.50 34.77  ?  193 ARG B NE  1 
ATOM   5000 N  NE  B ARG B 1 193 ? 68.280 -63.780 25.824  0.50 28.26  ?  193 ARG B NE  1 
ATOM   5001 C  CZ  A ARG B 1 193 ? 69.824 -63.758 25.309  0.50 36.85  ?  193 ARG B CZ  1 
ATOM   5002 C  CZ  B ARG B 1 193 ? 69.123 -64.765 25.510  0.50 29.49  ?  193 ARG B CZ  1 
ATOM   5003 N  NH1 A ARG B 1 193 ? 68.705 -64.457 25.404  0.50 36.86  1  193 ARG B NH1 1 
ATOM   5004 N  NH1 B ARG B 1 193 ? 70.048 -64.605 24.573  0.50 29.20  1  193 ARG B NH1 1 
ATOM   5005 N  NH2 A ARG B 1 193 ? 70.996 -64.360 25.452  0.50 37.21  ?  193 ARG B NH2 1 
ATOM   5006 N  NH2 B ARG B 1 193 ? 69.045 -65.917 26.152  0.50 29.96  ?  193 ARG B NH2 1 
ATOM   5007 N  N   . PRO B 1 194 ? 66.735 -63.054 29.026  1.00 26.30  ?  194 PRO B N   1 
ATOM   5008 C  CA  . PRO B 1 194 ? 65.775 -64.135 29.219  1.00 23.83  ?  194 PRO B CA  1 
ATOM   5009 C  C   . PRO B 1 194 ? 64.713 -63.734 30.233  1.00 24.16  ?  194 PRO B C   1 
ATOM   5010 O  O   . PRO B 1 194 ? 63.553 -64.100 30.071  1.00 26.08  ?  194 PRO B O   1 
ATOM   5011 C  CB  . PRO B 1 194 ? 66.575 -65.347 29.694  1.00 23.24  ?  194 PRO B CB  1 
ATOM   5012 C  CG  . PRO B 1 194 ? 68.028 -64.943 29.651  1.00 22.96  ?  194 PRO B CG  1 
ATOM   5013 C  CD  . PRO B 1 194 ? 68.113 -63.469 29.330  1.00 25.31  ?  194 PRO B CD  1 
ATOM   5014 N  N   . GLU B 1 195 ? 65.099 -62.966 31.262  1.00 22.76  ?  195 GLU B N   1 
ATOM   5015 C  CA  . GLU B 1 195 ? 64.181 -62.710 32.360  1.00 23.16  ?  195 GLU B CA  1 
ATOM   5016 C  C   . GLU B 1 195 ? 63.601 -61.309 32.272  1.00 22.40  ?  195 GLU B C   1 
ATOM   5017 O  O   . GLU B 1 195 ? 62.947 -60.890 33.204  1.00 26.67  ?  195 GLU B O   1 
ATOM   5018 C  CB  . GLU B 1 195 ? 64.789 -62.965 33.745  1.00 24.94  ?  195 GLU B CB  1 
ATOM   5019 C  CG  . GLU B 1 195 ? 66.191 -62.404 33.955  1.00 25.96  ?  195 GLU B CG  1 
ATOM   5020 C  CD  . GLU B 1 195 ? 67.329 -63.300 33.489  1.00 24.77  ?  195 GLU B CD  1 
ATOM   5021 O  OE1 . GLU B 1 195 ? 67.875 -64.061 34.296  1.00 21.84  ?  195 GLU B OE1 1 
ATOM   5022 O  OE2 . GLU B 1 195 ? 67.689 -63.206 32.307  1.00 27.98  -1 195 GLU B OE2 1 
ATOM   5023 N  N   . ALA B 1 196 ? 63.769 -60.614 31.147  1.00 22.53  ?  196 ALA B N   1 
ATOM   5024 C  CA  . ALA B 1 196 ? 63.416 -59.203 31.057  1.00 21.63  ?  196 ALA B CA  1 
ATOM   5025 C  C   . ALA B 1 196 ? 61.903 -58.964 31.136  1.00 21.72  ?  196 ALA B C   1 
ATOM   5026 O  O   . ALA B 1 196 ? 61.478 -58.101 31.890  1.00 20.42  ?  196 ALA B O   1 
ATOM   5027 C  CB  . ALA B 1 196 ? 63.972 -58.621 29.785  1.00 21.35  ?  196 ALA B CB  1 
ATOM   5028 N  N   . THR B 1 197 ? 61.102 -59.671 30.321  1.00 22.63  ?  197 THR B N   1 
ATOM   5029 C  CA  . THR B 1 197 ? 59.692 -59.332 30.136  1.00 23.24  ?  197 THR B CA  1 
ATOM   5030 C  C   . THR B 1 197 ? 58.908 -59.724 31.384  1.00 24.10  ?  197 THR B C   1 
ATOM   5031 O  O   . THR B 1 197 ? 58.043 -58.956 31.826  1.00 23.24  ?  197 THR B O   1 
ATOM   5032 C  CB  . THR B 1 197 ? 59.098 -60.020 28.904  1.00 22.94  ?  197 THR B CB  1 
ATOM   5033 O  OG1 . THR B 1 197 ? 59.829 -59.558 27.768  1.00 21.98  ?  197 THR B OG1 1 
ATOM   5034 C  CG2 . THR B 1 197 ? 57.616 -59.719 28.753  1.00 23.12  ?  197 THR B CG2 1 
ATOM   5035 N  N   . GLY B 1 198 ? 59.256 -60.915 31.910  1.00 25.22  ?  198 GLY B N   1 
ATOM   5036 C  CA  . GLY B 1 198 ? 58.711 -61.487 33.137  1.00 25.78  ?  198 GLY B CA  1 
ATOM   5037 C  C   . GLY B 1 198 ? 58.925 -60.569 34.336  1.00 25.53  ?  198 GLY B C   1 
ATOM   5038 O  O   . GLY B 1 198 ? 57.970 -60.190 35.004  1.00 25.92  ?  198 GLY B O   1 
ATOM   5039 N  N   . TYR B 1 199 ? 60.189 -60.205 34.579  1.00 24.79  ?  199 TYR B N   1 
ATOM   5040 C  CA  . TYR B 1 199 ? 60.547 -59.285 35.635  1.00 25.09  ?  199 TYR B CA  1 
ATOM   5041 C  C   . TYR B 1 199 ? 59.819 -57.961 35.452  1.00 27.99  ?  199 TYR B C   1 
ATOM   5042 O  O   . TYR B 1 199 ? 59.424 -57.334 36.440  1.00 31.88  ?  199 TYR B O   1 
ATOM   5043 C  CB  . TYR B 1 199 ? 62.050 -59.043 35.588  1.00 26.54  ?  199 TYR B CB  1 
ATOM   5044 C  CG  . TYR B 1 199 ? 62.919 -60.068 36.302  1.00 28.32  ?  199 TYR B CG  1 
ATOM   5045 C  CD1 . TYR B 1 199 ? 62.432 -61.291 36.742  1.00 28.98  ?  199 TYR B CD1 1 
ATOM   5046 C  CD2 . TYR B 1 199 ? 64.267 -59.797 36.512  1.00 29.13  ?  199 TYR B CD2 1 
ATOM   5047 C  CE1 . TYR B 1 199 ? 63.268 -62.194 37.387  1.00 30.55  ?  199 TYR B CE1 1 
ATOM   5048 C  CE2 . TYR B 1 199 ? 65.111 -60.695 37.134  1.00 26.98  ?  199 TYR B CE2 1 
ATOM   5049 C  CZ  . TYR B 1 199 ? 64.605 -61.890 37.584  1.00 27.75  ?  199 TYR B CZ  1 
ATOM   5050 O  OH  . TYR B 1 199 ? 65.474 -62.738 38.196  1.00 28.90  ?  199 TYR B OH  1 
ATOM   5051 N  N   . GLY B 1 200 ? 59.694 -57.540 34.185  1.00 28.66  ?  200 GLY B N   1 
ATOM   5052 C  CA  . GLY B 1 200 ? 59.130 -56.247 33.818  1.00 27.99  ?  200 GLY B CA  1 
ATOM   5053 C  C   . GLY B 1 200 ? 57.639 -56.160 34.138  1.00 29.20  ?  200 GLY B C   1 
ATOM   5054 O  O   . GLY B 1 200 ? 57.184 -55.087 34.547  1.00 26.90  ?  200 GLY B O   1 
ATOM   5055 N  N   . VAL B 1 201 ? 56.908 -57.288 33.958  1.00 28.75  ?  201 VAL B N   1 
ATOM   5056 C  CA  . VAL B 1 201 ? 55.473 -57.358 34.235  1.00 26.85  ?  201 VAL B CA  1 
ATOM   5057 C  C   . VAL B 1 201 ? 55.263 -57.276 35.750  1.00 27.51  ?  201 VAL B C   1 
ATOM   5058 O  O   . VAL B 1 201 ? 54.499 -56.427 36.215  1.00 26.45  ?  201 VAL B O   1 
ATOM   5059 C  CB  . VAL B 1 201 ? 54.755 -58.585 33.625  1.00 24.60  ?  201 VAL B CB  1 
ATOM   5060 C  CG1 . VAL B 1 201 ? 54.927 -59.847 34.450  1.00 26.38  ?  201 VAL B CG1 1 
ATOM   5061 C  CG2 . VAL B 1 201 ? 53.260 -58.370 33.443  1.00 23.90  ?  201 VAL B CG2 1 
ATOM   5062 N  N   . VAL B 1 202 ? 56.001 -58.107 36.501  1.00 27.50  ?  202 VAL B N   1 
ATOM   5063 C  CA  . VAL B 1 202 ? 55.925 -58.151 37.955  1.00 31.25  ?  202 VAL B CA  1 
ATOM   5064 C  C   . VAL B 1 202 ? 56.270 -56.779 38.540  1.00 30.83  ?  202 VAL B C   1 
ATOM   5065 O  O   . VAL B 1 202 ? 55.580 -56.272 39.422  1.00 33.60  ?  202 VAL B O   1 
ATOM   5066 C  CB  . VAL B 1 202 ? 56.863 -59.239 38.524  1.00 33.18  ?  202 VAL B CB  1 
ATOM   5067 C  CG1 . VAL B 1 202 ? 56.899 -59.196 40.047  1.00 34.65  ?  202 VAL B CG1 1 
ATOM   5068 C  CG2 . VAL B 1 202 ? 56.495 -60.645 38.047  1.00 31.65  ?  202 VAL B CG2 1 
ATOM   5069 N  N   . TYR B 1 203 ? 57.350 -56.174 38.053  1.00 29.03  ?  203 TYR B N   1 
ATOM   5070 C  CA  . TYR B 1 203 ? 57.767 -54.870 38.544  1.00 32.06  ?  203 TYR B CA  1 
ATOM   5071 C  C   . TYR B 1 203 ? 56.693 -53.812 38.281  1.00 29.17  ?  203 TYR B C   1 
ATOM   5072 O  O   . TYR B 1 203 ? 56.569 -52.856 39.026  1.00 26.07  ?  203 TYR B O   1 
ATOM   5073 C  CB  . TYR B 1 203 ? 59.061 -54.451 37.845  1.00 35.75  ?  203 TYR B CB  1 
ATOM   5074 C  CG  . TYR B 1 203 ? 60.355 -55.140 38.259  1.00 38.86  ?  203 TYR B CG  1 
ATOM   5075 C  CD1 . TYR B 1 203 ? 61.318 -55.436 37.308  1.00 39.31  ?  203 TYR B CD1 1 
ATOM   5076 C  CD2 . TYR B 1 203 ? 60.649 -55.429 39.587  1.00 44.05  ?  203 TYR B CD2 1 
ATOM   5077 C  CE1 . TYR B 1 203 ? 62.521 -56.020 37.653  1.00 43.58  ?  203 TYR B CE1 1 
ATOM   5078 C  CE2 . TYR B 1 203 ? 61.851 -56.015 39.949  1.00 45.69  ?  203 TYR B CE2 1 
ATOM   5079 C  CZ  . TYR B 1 203 ? 62.791 -56.308 38.976  1.00 45.60  ?  203 TYR B CZ  1 
ATOM   5080 O  OH  . TYR B 1 203 ? 63.995 -56.867 39.286  1.00 46.19  ?  203 TYR B OH  1 
ATOM   5081 N  N   . TYR B 1 204 ? 55.950 -53.955 37.183  1.00 31.00  ?  204 TYR B N   1 
ATOM   5082 C  CA  . TYR B 1 204 ? 54.967 -52.962 36.782  1.00 31.20  ?  204 TYR B CA  1 
ATOM   5083 C  C   . TYR B 1 204 ? 53.781 -53.017 37.741  1.00 34.13  ?  204 TYR B C   1 
ATOM   5084 O  O   . TYR B 1 204 ? 53.263 -51.970 38.147  1.00 30.77  ?  204 TYR B O   1 
ATOM   5085 C  CB  . TYR B 1 204 ? 54.525 -53.205 35.334  1.00 29.18  ?  204 TYR B CB  1 
ATOM   5086 C  CG  . TYR B 1 204 ? 53.581 -52.139 34.802  1.00 27.92  ?  204 TYR B CG  1 
ATOM   5087 C  CD1 . TYR B 1 204 ? 54.060 -51.053 34.084  1.00 29.03  ?  204 TYR B CD1 1 
ATOM   5088 C  CD2 . TYR B 1 204 ? 52.209 -52.223 35.015  1.00 28.31  ?  204 TYR B CD2 1 
ATOM   5089 C  CE1 . TYR B 1 204 ? 53.203 -50.064 33.618  1.00 30.76  ?  204 TYR B CE1 1 
ATOM   5090 C  CE2 . TYR B 1 204 ? 51.340 -51.249 34.546  1.00 28.40  ?  204 TYR B CE2 1 
ATOM   5091 C  CZ  . TYR B 1 204 ? 51.837 -50.162 33.849  1.00 28.33  ?  204 TYR B CZ  1 
ATOM   5092 O  OH  . TYR B 1 204 ? 51.001 -49.191 33.396  1.00 23.90  ?  204 TYR B OH  1 
ATOM   5093 N  N   . VAL B 1 205 ? 53.364 -54.257 38.057  1.00 34.91  ?  205 VAL B N   1 
ATOM   5094 C  CA  . VAL B 1 205 ? 52.200 -54.533 38.893  1.00 36.42  ?  205 VAL B CA  1 
ATOM   5095 C  C   . VAL B 1 205 ? 52.482 -54.095 40.333  1.00 34.96  ?  205 VAL B C   1 
ATOM   5096 O  O   . VAL B 1 205 ? 51.580 -53.616 41.021  1.00 29.98  ?  205 VAL B O   1 
ATOM   5097 C  CB  . VAL B 1 205 ? 51.826 -56.030 38.802  1.00 34.32  ?  205 VAL B CB  1 
ATOM   5098 C  CG1 . VAL B 1 205 ? 50.876 -56.488 39.907  1.00 31.63  ?  205 VAL B CG1 1 
ATOM   5099 C  CG2 . VAL B 1 205 ? 51.272 -56.364 37.423  1.00 34.48  ?  205 VAL B CG2 1 
ATOM   5100 N  N   . GLU B 1 206 ? 53.739 -54.286 40.773  1.00 33.69  ?  206 GLU B N   1 
ATOM   5101 C  CA  . GLU B 1 206 ? 54.187 -53.846 42.088  1.00 31.27  ?  206 GLU B CA  1 
ATOM   5102 C  C   . GLU B 1 206 ? 53.681 -52.421 42.295  1.00 31.86  ?  206 GLU B C   1 
ATOM   5103 O  O   . GLU B 1 206 ? 53.082 -52.123 43.323  1.00 40.24  ?  206 GLU B O   1 
ATOM   5104 C  CB  . GLU B 1 206 ? 55.714 -53.944 42.151  1.00 28.41  ?  206 GLU B CB  1 
ATOM   5105 C  CG  . GLU B 1 206 ? 56.317 -54.316 43.502  1.00 25.97  ?  206 GLU B CG  1 
ATOM   5106 C  CD  . GLU B 1 206 ? 57.833 -54.368 43.389  1.00 25.25  ?  206 GLU B CD  1 
ATOM   5107 O  OE1 . GLU B 1 206 ? 58.330 -54.985 42.434  1.00 25.77  ?  206 GLU B OE1 1 
ATOM   5108 O  OE2 . GLU B 1 206 ? 58.544 -53.795 44.233  1.00 24.75  -1 206 GLU B OE2 1 
ATOM   5109 N  N   . HIS B 1 207 ? 53.879 -51.574 41.276  1.00 29.87  ?  207 HIS B N   1 
ATOM   5110 C  CA  . HIS B 1 207 ? 53.438 -50.186 41.297  1.00 30.88  ?  207 HIS B CA  1 
ATOM   5111 C  C   . HIS B 1 207 ? 51.913 -50.072 41.288  1.00 29.07  ?  207 HIS B C   1 
ATOM   5112 O  O   . HIS B 1 207 ? 51.366 -49.256 42.027  1.00 30.52  ?  207 HIS B O   1 
ATOM   5113 C  CB  . HIS B 1 207 ? 54.055 -49.388 40.140  1.00 30.78  ?  207 HIS B CB  1 
ATOM   5114 C  CG  . HIS B 1 207 ? 55.537 -49.322 40.202  1.00 27.73  ?  207 HIS B CG  1 
ATOM   5115 N  ND1 . HIS B 1 207 ? 56.179 -48.578 41.167  1.00 26.21  ?  207 HIS B ND1 1 
ATOM   5116 C  CD2 . HIS B 1 207 ? 56.486 -49.917 39.467  1.00 26.94  ?  207 HIS B CD2 1 
ATOM   5117 C  CE1 . HIS B 1 207 ? 57.491 -48.734 41.019  1.00 29.37  ?  207 HIS B CE1 1 
ATOM   5118 N  NE2 . HIS B 1 207 ? 57.699 -49.539 39.985  1.00 29.25  ?  207 HIS B NE2 1 
ATOM   5119 N  N   . MET B 1 208 ? 51.240 -50.871 40.446  1.00 27.64  ?  208 MET B N   1 
ATOM   5120 C  CA  . MET B 1 208 ? 49.781 -50.943 40.433  1.00 25.51  ?  208 MET B CA  1 
ATOM   5121 C  C   . MET B 1 208 ? 49.266 -51.143 41.858  1.00 25.79  ?  208 MET B C   1 
ATOM   5122 O  O   . MET B 1 208 ? 48.502 -50.326 42.366  1.00 25.29  ?  208 MET B O   1 
ATOM   5123 C  CB  . MET B 1 208 ? 49.270 -52.040 39.490  1.00 22.77  ?  208 MET B CB  1 
ATOM   5124 C  CG  . MET B 1 208 ? 49.560 -51.713 38.034  1.00 22.84  ?  208 MET B CG  1 
ATOM   5125 S  SD  . MET B 1 208 ? 49.185 -52.963 36.788  1.00 22.95  ?  208 MET B SD  1 
ATOM   5126 C  CE  . MET B 1 208 ? 47.391 -52.867 36.885  1.00 22.96  ?  208 MET B CE  1 
ATOM   5127 N  N   . ILE B 1 209 ? 49.768 -52.184 42.521  1.00 28.19  ?  209 ILE B N   1 
ATOM   5128 C  CA  . ILE B 1 209 ? 49.325 -52.537 43.857  1.00 29.89  ?  209 ILE B CA  1 
ATOM   5129 C  C   . ILE B 1 209 ? 49.545 -51.356 44.798  1.00 28.20  ?  209 ILE B C   1 
ATOM   5130 O  O   . ILE B 1 209 ? 48.620 -50.976 45.525  1.00 26.06  ?  209 ILE B O   1 
ATOM   5131 C  CB  . ILE B 1 209 ? 50.024 -53.808 44.371  1.00 32.85  ?  209 ILE B CB  1 
ATOM   5132 C  CG1 . ILE B 1 209 ? 49.817 -55.002 43.415  1.00 38.56  ?  209 ILE B CG1 1 
ATOM   5133 C  CG2 . ILE B 1 209 ? 49.534 -54.132 45.781  1.00 34.91  ?  209 ILE B CG2 1 
ATOM   5134 C  CD1 . ILE B 1 209 ? 50.411 -56.324 43.896  1.00 40.71  ?  209 ILE B CD1 1 
ATOM   5135 N  N   . ALA B 1 210 ? 50.771 -50.809 44.782  1.00 25.70  ?  210 ALA B N   1 
ATOM   5136 C  CA  . ALA B 1 210 ? 51.117 -49.669 45.621  1.00 26.99  ?  210 ALA B CA  1 
ATOM   5137 C  C   . ALA B 1 210 ? 50.089 -48.534 45.490  1.00 27.99  ?  210 ALA B C   1 
ATOM   5138 O  O   . ALA B 1 210 ? 49.620 -48.013 46.503  1.00 25.41  ?  210 ALA B O   1 
ATOM   5139 C  CB  . ALA B 1 210 ? 52.505 -49.190 45.293  1.00 25.12  ?  210 ALA B CB  1 
ATOM   5140 N  N   . HIS B 1 211 ? 49.750 -48.142 44.247  1.00 29.10  ?  211 HIS B N   1 
ATOM   5141 C  CA  . HIS B 1 211 ? 48.899 -46.982 44.020  1.00 29.38  ?  211 HIS B CA  1 
ATOM   5142 C  C   . HIS B 1 211 ? 47.500 -47.281 44.554  1.00 29.97  ?  211 HIS B C   1 
ATOM   5143 O  O   . HIS B 1 211 ? 47.033 -46.642 45.494  1.00 27.99  ?  211 HIS B O   1 
ATOM   5144 C  CB  . HIS B 1 211 ? 48.863 -46.567 42.548  1.00 28.85  ?  211 HIS B CB  1 
ATOM   5145 C  CG  . HIS B 1 211 ? 48.208 -45.233 42.394  1.00 35.56  ?  211 HIS B CG  1 
ATOM   5146 N  ND1 . HIS B 1 211 ? 46.859 -45.076 42.129  1.00 39.64  ?  211 HIS B ND1 1 
ATOM   5147 C  CD2 . HIS B 1 211 ? 48.710 -43.986 42.517  1.00 36.18  ?  211 HIS B CD2 1 
ATOM   5148 C  CE1 . HIS B 1 211 ? 46.571 -43.779 42.067  1.00 37.38  ?  211 HIS B CE1 1 
ATOM   5149 N  NE2 . HIS B 1 211 ? 47.676 -43.100 42.305  1.00 35.91  ?  211 HIS B NE2 1 
ATOM   5150 N  N   . ALA B 1 212 ? 46.878 -48.301 43.956  1.00 28.52  ?  212 ALA B N   1 
ATOM   5151 C  CA  . ALA B 1 212 ? 45.566 -48.780 44.329  1.00 27.93  ?  212 ALA B CA  1 
ATOM   5152 C  C   . ALA B 1 212 ? 45.379 -48.891 45.848  1.00 30.83  ?  212 ALA B C   1 
ATOM   5153 O  O   . ALA B 1 212 ? 44.343 -48.469 46.350  1.00 32.06  ?  212 ALA B O   1 
ATOM   5154 C  CB  . ALA B 1 212 ? 45.370 -50.109 43.658  1.00 28.41  ?  212 ALA B CB  1 
ATOM   5155 N  N   . THR B 1 213 ? 46.357 -49.471 46.573  1.00 31.85  ?  213 THR B N   1 
ATOM   5156 C  CA  . THR B 1 213 ? 46.203 -49.769 47.992  1.00 31.25  ?  213 THR B CA  1 
ATOM   5157 C  C   . THR B 1 213 ? 46.884 -48.708 48.865  1.00 34.77  ?  213 THR B C   1 
ATOM   5158 O  O   . THR B 1 213 ? 46.948 -48.868 50.080  1.00 37.35  ?  213 THR B O   1 
ATOM   5159 C  CB  . THR B 1 213 ? 46.714 -51.180 48.303  1.00 29.62  ?  213 THR B CB  1 
ATOM   5160 O  OG1 . THR B 1 213 ? 48.127 -51.309 48.207  1.00 26.17  ?  213 THR B OG1 1 
ATOM   5161 C  CG2 . THR B 1 213 ? 46.100 -52.216 47.384  1.00 30.60  ?  213 THR B CG2 1 
ATOM   5162 N  N   . ASN B 1 214 ? 47.376 -47.621 48.249  1.00 35.91  ?  214 ASN B N   1 
ATOM   5163 C  CA  . ASN B 1 214 ? 48.091 -46.543 48.927  1.00 31.46  ?  214 ASN B CA  1 
ATOM   5164 C  C   . ASN B 1 214 ? 49.268 -47.092 49.736  1.00 33.71  ?  214 ASN B C   1 
ATOM   5165 O  O   . ASN B 1 214 ? 49.631 -46.512 50.752  1.00 41.94  ?  214 ASN B O   1 
ATOM   5166 C  CB  . ASN B 1 214 ? 47.120 -45.709 49.757  1.00 28.73  ?  214 ASN B CB  1 
ATOM   5167 C  CG  . ASN B 1 214 ? 47.667 -44.373 50.231  1.00 28.06  ?  214 ASN B CG  1 
ATOM   5168 O  OD1 . ASN B 1 214 ? 48.719 -43.902 49.789  1.00 22.09  ?  214 ASN B OD1 1 
ATOM   5169 N  ND2 . ASN B 1 214 ? 46.953 -43.735 51.151  1.00 29.11  ?  214 ASN B ND2 1 
ATOM   5170 N  N   . GLY B 1 215 ? 49.884 -48.194 49.285  1.00 33.90  ?  215 GLY B N   1 
ATOM   5171 C  CA  . GLY B 1 215 ? 50.998 -48.807 49.998  1.00 35.22  ?  215 GLY B CA  1 
ATOM   5172 C  C   . GLY B 1 215 ? 50.572 -49.929 50.950  1.00 38.86  ?  215 GLY B C   1 
ATOM   5173 O  O   . GLY B 1 215 ? 51.413 -50.687 51.434  1.00 38.54  ?  215 GLY B O   1 
ATOM   5174 N  N   . ALA B 1 216 ? 49.267 -50.068 51.212  1.00 39.88  ?  216 ALA B N   1 
ATOM   5175 C  CA  . ALA B 1 216 ? 48.778 -51.038 52.189  1.00 43.05  ?  216 ALA B CA  1 
ATOM   5176 C  C   . ALA B 1 216 ? 49.113 -52.489 51.818  1.00 42.19  ?  216 ALA B C   1 
ATOM   5177 O  O   . ALA B 1 216 ? 48.944 -53.381 52.646  1.00 37.11  ?  216 ALA B O   1 
ATOM   5178 C  CB  . ALA B 1 216 ? 47.277 -50.877 52.340  1.00 44.62  ?  216 ALA B CB  1 
ATOM   5179 N  N   . GLU B 1 217 ? 49.523 -52.733 50.565  1.00 43.36  ?  217 GLU B N   1 
ATOM   5180 C  CA  . GLU B 1 217 ? 49.694 -54.085 50.051  1.00 40.88  ?  217 GLU B CA  1 
ATOM   5181 C  C   . GLU B 1 217 ? 50.833 -54.095 49.037  1.00 36.35  ?  217 GLU B C   1 
ATOM   5182 O  O   . GLU B 1 217 ? 50.975 -53.153 48.262  1.00 41.45  ?  217 GLU B O   1 
ATOM   5183 C  CB  . GLU B 1 217 ? 48.432 -54.583 49.342  1.00 43.27  ?  217 GLU B CB  1 
ATOM   5184 C  CG  . GLU B 1 217 ? 47.146 -54.468 50.165  1.00 43.68  ?  217 GLU B CG  1 
ATOM   5185 C  CD  . GLU B 1 217 ? 45.935 -55.220 49.618  1.00 37.96  ?  217 GLU B CD  1 
ATOM   5186 O  OE1 . GLU B 1 217 ? 45.183 -55.767 50.462  1.00 35.03  ?  217 GLU B OE1 1 
ATOM   5187 O  OE2 . GLU B 1 217 ? 45.756 -55.299 48.374  1.00 30.35  -1 217 GLU B OE2 1 
ATOM   5188 N  N   . SER B 1 218 ? 51.652 -55.146 49.101  1.00 30.23  ?  218 SER B N   1 
ATOM   5189 C  CA  . SER B 1 218 ? 52.671 -55.450 48.112  1.00 30.69  ?  218 SER B CA  1 
ATOM   5190 C  C   . SER B 1 218 ? 52.238 -56.702 47.354  1.00 33.92  ?  218 SER B C   1 
ATOM   5191 O  O   . SER B 1 218 ? 51.046 -56.991 47.307  1.00 37.69  ?  218 SER B O   1 
ATOM   5192 C  CB  . SER B 1 218 ? 54.024 -55.621 48.782  1.00 30.62  ?  218 SER B CB  1 
ATOM   5193 O  OG  . SER B 1 218 ? 53.915 -56.391 49.971  1.00 29.01  ?  218 SER B OG  1 
ATOM   5194 N  N   . PHE B 1 219 ? 53.197 -57.417 46.741  1.00 33.79  ?  219 PHE B N   1 
ATOM   5195 C  CA  . PHE B 1 219 ? 52.984 -58.763 46.233  1.00 32.65  ?  219 PHE B CA  1 
ATOM   5196 C  C   . PHE B 1 219 ? 52.982 -59.806 47.348  1.00 37.39  ?  219 PHE B C   1 
ATOM   5197 O  O   . PHE B 1 219 ? 52.512 -60.921 47.125  1.00 40.15  ?  219 PHE B O   1 
ATOM   5198 C  CB  . PHE B 1 219 ? 54.093 -59.207 45.278  1.00 30.84  ?  219 PHE B CB  1 
ATOM   5199 C  CG  . PHE B 1 219 ? 53.757 -59.075 43.800  1.00 31.35  ?  219 PHE B CG  1 
ATOM   5200 C  CD1 . PHE B 1 219 ? 54.135 -57.948 43.083  1.00 29.77  ?  219 PHE B CD1 1 
ATOM   5201 C  CD2 . PHE B 1 219 ? 53.053 -60.076 43.136  1.00 28.91  ?  219 PHE B CD2 1 
ATOM   5202 C  CE1 . PHE B 1 219 ? 53.825 -57.832 41.746  1.00 29.79  ?  219 PHE B CE1 1 
ATOM   5203 C  CE2 . PHE B 1 219 ? 52.750 -59.952 41.798  1.00 27.92  ?  219 PHE B CE2 1 
ATOM   5204 C  CZ  . PHE B 1 219 ? 53.140 -58.836 41.104  1.00 29.11  ?  219 PHE B CZ  1 
ATOM   5205 N  N   . ALA B 1 220 ? 53.577 -59.478 48.506  1.00 40.08  ?  220 ALA B N   1 
ATOM   5206 C  CA  . ALA B 1 220 ? 53.701 -60.426 49.608  1.00 40.64  ?  220 ALA B CA  1 
ATOM   5207 C  C   . ALA B 1 220 ? 52.323 -60.955 50.021  1.00 40.34  ?  220 ALA B C   1 
ATOM   5208 O  O   . ALA B 1 220 ? 51.407 -60.168 50.241  1.00 40.17  ?  220 ALA B O   1 
ATOM   5209 C  CB  . ALA B 1 220 ? 54.414 -59.772 50.779  1.00 39.17  ?  220 ALA B CB  1 
ATOM   5210 N  N   . GLY B 1 221 ? 52.177 -62.286 50.102  1.00 41.05  ?  221 GLY B N   1 
ATOM   5211 C  CA  . GLY B 1 221 ? 50.958 -62.915 50.600  1.00 48.42  ?  221 GLY B CA  1 
ATOM   5212 C  C   . GLY B 1 221 ? 49.776 -62.806 49.628  1.00 53.37  ?  221 GLY B C   1 
ATOM   5213 O  O   . GLY B 1 221 ? 48.620 -62.995 50.022  1.00 57.78  ?  221 GLY B O   1 
ATOM   5214 N  N   . LYS B 1 222 ? 50.074 -62.496 48.359  1.00 48.48  ?  222 LYS B N   1 
ATOM   5215 C  CA  . LYS B 1 222 ? 49.067 -62.390 47.319  1.00 43.09  ?  222 LYS B CA  1 
ATOM   5216 C  C   . LYS B 1 222 ? 49.088 -63.692 46.543  1.00 37.12  ?  222 LYS B C   1 
ATOM   5217 O  O   . LYS B 1 222 ? 50.149 -64.298 46.407  1.00 35.37  ?  222 LYS B O   1 
ATOM   5218 C  CB  . LYS B 1 222 ? 49.369 -61.242 46.345  1.00 42.49  ?  222 LYS B CB  1 
ATOM   5219 C  CG  . LYS B 1 222 ? 49.101 -59.829 46.827  1.00 39.62  ?  222 LYS B CG  1 
ATOM   5220 C  CD  . LYS B 1 222 ? 48.099 -59.068 45.975  1.00 39.91  ?  222 LYS B CD  1 
ATOM   5221 C  CE  . LYS B 1 222 ? 47.776 -57.723 46.546  1.00 41.94  ?  222 LYS B CE  1 
ATOM   5222 N  NZ  . LYS B 1 222 ? 46.766 -57.845 47.611  1.00 46.55  1  222 LYS B NZ  1 
ATOM   5223 N  N   . ARG B 1 223 ? 47.911 -64.096 46.059  1.00 34.76  ?  223 ARG B N   1 
ATOM   5224 C  CA  . ARG B 1 223 ? 47.793 -65.258 45.199  1.00 38.69  ?  223 ARG B CA  1 
ATOM   5225 C  C   . ARG B 1 223 ? 47.836 -64.767 43.755  1.00 39.19  ?  223 ARG B C   1 
ATOM   5226 O  O   . ARG B 1 223 ? 46.995 -63.964 43.353  1.00 42.88  ?  223 ARG B O   1 
ATOM   5227 C  CB  . ARG B 1 223 ? 46.512 -66.030 45.533  1.00 40.39  ?  223 ARG B CB  1 
ATOM   5228 C  CG  . ARG B 1 223 ? 46.377 -66.490 46.980  1.00 40.01  ?  223 ARG B CG  1 
ATOM   5229 C  CD  . ARG B 1 223 ? 44.919 -66.785 47.369  1.00 43.33  ?  223 ARG B CD  1 
ATOM   5230 N  NE  . ARG B 1 223 ? 44.029 -65.613 47.347  1.00 44.88  ?  223 ARG B NE  1 
ATOM   5231 C  CZ  . ARG B 1 223 ? 44.012 -64.602 48.220  1.00 46.10  ?  223 ARG B CZ  1 
ATOM   5232 N  NH1 . ARG B 1 223 ? 44.754 -64.625 49.324  1.00 43.08  1  223 ARG B NH1 1 
ATOM   5233 N  NH2 . ARG B 1 223 ? 43.233 -63.558 47.971  1.00 48.46  ?  223 ARG B NH2 1 
ATOM   5234 N  N   . VAL B 1 224 ? 48.833 -65.240 42.991  1.00 38.76  ?  224 VAL B N   1 
ATOM   5235 C  CA  . VAL B 1 224 ? 49.051 -64.759 41.637  1.00 38.22  ?  224 VAL B CA  1 
ATOM   5236 C  C   . VAL B 1 224 ? 48.935 -65.920 40.653  1.00 35.56  ?  224 VAL B C   1 
ATOM   5237 O  O   . VAL B 1 224 ? 49.688 -66.890 40.776  1.00 32.90  ?  224 VAL B O   1 
ATOM   5238 C  CB  . VAL B 1 224 ? 50.414 -64.067 41.515  1.00 39.92  ?  224 VAL B CB  1 
ATOM   5239 C  CG1 . VAL B 1 224 ? 51.551 -65.026 41.838  1.00 43.31  ?  224 VAL B CG1 1 
ATOM   5240 C  CG2 . VAL B 1 224 ? 50.605 -63.462 40.132  1.00 40.22  ?  224 VAL B CG2 1 
ATOM   5241 N  N   . ALA B 1 225 ? 48.003 -65.781 39.686  1.00 31.44  ?  225 ALA B N   1 
ATOM   5242 C  CA  . ALA B 1 225 ? 47.764 -66.781 38.651  1.00 33.42  ?  225 ALA B CA  1 
ATOM   5243 C  C   . ALA B 1 225 ? 48.604 -66.525 37.385  1.00 32.81  ?  225 ALA B C   1 
ATOM   5244 O  O   . ALA B 1 225 ? 48.396 -65.544 36.662  1.00 31.30  ?  225 ALA B O   1 
ATOM   5245 C  CB  . ALA B 1 225 ? 46.289 -66.805 38.327  1.00 32.56  ?  225 ALA B CB  1 
ATOM   5246 N  N   . ILE B 1 226 ? 49.556 -67.430 37.109  1.00 29.13  ?  226 ILE B N   1 
ATOM   5247 C  CA  . ILE B 1 226 ? 50.352 -67.363 35.896  1.00 29.10  ?  226 ILE B CA  1 
ATOM   5248 C  C   . ILE B 1 226 ? 49.921 -68.495 34.950  1.00 28.74  ?  226 ILE B C   1 
ATOM   5249 O  O   . ILE B 1 226 ? 49.372 -69.518 35.371  1.00 23.20  ?  226 ILE B O   1 
ATOM   5250 C  CB  . ILE B 1 226 ? 51.863 -67.385 36.223  1.00 29.54  ?  226 ILE B CB  1 
ATOM   5251 C  CG1 . ILE B 1 226 ? 52.257 -66.259 37.178  1.00 30.57  ?  226 ILE B CG1 1 
ATOM   5252 C  CG2 . ILE B 1 226 ? 52.710 -67.335 34.948  1.00 31.56  ?  226 ILE B CG2 1 
ATOM   5253 C  CD1 . ILE B 1 226 ? 53.701 -66.313 37.664  1.00 31.82  ?  226 ILE B CD1 1 
ATOM   5254 N  N   . SER B 1 227 ? 50.124 -68.250 33.645  1.00 32.19  ?  227 SER B N   1 
ATOM   5255 C  CA  . SER B 1 227 ? 50.073 -69.268 32.600  1.00 33.11  ?  227 SER B CA  1 
ATOM   5256 C  C   . SER B 1 227 ? 51.381 -69.221 31.814  1.00 30.64  ?  227 SER B C   1 
ATOM   5257 O  O   . SER B 1 227 ? 52.034 -68.182 31.813  1.00 30.46  ?  227 SER B O   1 
ATOM   5258 C  CB  . SER B 1 227 ? 48.882 -69.062 31.696  1.00 32.02  ?  227 SER B CB  1 
ATOM   5259 O  OG  . SER B 1 227 ? 49.065 -67.960 30.812  1.00 30.04  ?  227 SER B OG  1 
ATOM   5260 N  N   . GLY B 1 228 ? 51.742 -70.332 31.159  1.00 30.19  ?  228 GLY B N   1 
ATOM   5261 C  CA  . GLY B 1 228 ? 52.958 -70.420 30.356  1.00 32.76  ?  228 GLY B CA  1 
ATOM   5262 C  C   . GLY B 1 228 ? 54.100 -70.997 31.187  1.00 36.38  ?  228 GLY B C   1 
ATOM   5263 O  O   . GLY B 1 228 ? 54.012 -70.969 32.416  1.00 37.34  ?  228 GLY B O   1 
ATOM   5264 N  N   . SER B 1 229 ? 55.132 -71.558 30.522  1.00 37.96  ?  229 SER B N   1 
ATOM   5265 C  CA  . SER B 1 229 ? 56.271 -72.163 31.217  1.00 35.25  ?  229 SER B CA  1 
ATOM   5266 C  C   . SER B 1 229 ? 57.596 -71.861 30.517  1.00 33.33  ?  229 SER B C   1 
ATOM   5267 O  O   . SER B 1 229 ? 58.607 -72.501 30.827  1.00 30.65  ?  229 SER B O   1 
ATOM   5268 C  CB  . SER B 1 229 ? 56.116 -73.637 31.346  1.00 33.13  ?  229 SER B CB  1 
ATOM   5269 O  OG  . SER B 1 229 ? 54.760 -74.006 31.226  1.00 38.91  ?  229 SER B OG  1 
ATOM   5270 N  N   . GLY B 1 230 ? 57.571 -70.919 29.566  1.00 31.09  ?  230 GLY B N   1 
ATOM   5271 C  CA  . GLY B 1 230 ? 58.785 -70.365 29.002  1.00 35.65  ?  230 GLY B CA  1 
ATOM   5272 C  C   . GLY B 1 230 ? 59.413 -69.383 29.983  1.00 39.65  ?  230 GLY B C   1 
ATOM   5273 O  O   . GLY B 1 230 ? 58.875 -69.173 31.066  1.00 45.30  ?  230 GLY B O   1 
ATOM   5274 N  N   . ASN B 1 231 ? 60.515 -68.753 29.560  1.00 46.23  ?  231 ASN B N   1 
ATOM   5275 C  CA  . ASN B 1 231 ? 61.340 -67.907 30.415  1.00 45.74  ?  231 ASN B CA  1 
ATOM   5276 C  C   . ASN B 1 231 ? 60.530 -66.723 30.939  1.00 38.25  ?  231 ASN B C   1 
ATOM   5277 O  O   . ASN B 1 231 ? 60.945 -66.103 31.913  1.00 37.82  ?  231 ASN B O   1 
ATOM   5278 C  CB  . ASN B 1 231 ? 62.635 -67.483 29.715  1.00 47.99  ?  231 ASN B CB  1 
ATOM   5279 C  CG  . ASN B 1 231 ? 63.534 -68.665 29.425  1.00 49.09  ?  231 ASN B CG  1 
ATOM   5280 O  OD1 . ASN B 1 231 ? 64.436 -68.971 30.211  1.00 57.46  ?  231 ASN B OD1 1 
ATOM   5281 N  ND2 . ASN B 1 231 ? 63.274 -69.385 28.345  1.00 48.50  ?  231 ASN B ND2 1 
ATOM   5282 N  N   . VAL B 1 232 ? 59.372 -66.435 30.321  1.00 35.06  ?  232 VAL B N   1 
ATOM   5283 C  CA  . VAL B 1 232 ? 58.526 -65.326 30.751  1.00 34.04  ?  232 VAL B CA  1 
ATOM   5284 C  C   . VAL B 1 232 ? 57.775 -65.721 32.025  1.00 35.66  ?  232 VAL B C   1 
ATOM   5285 O  O   . VAL B 1 232 ? 57.825 -65.011 33.027  1.00 38.97  ?  232 VAL B O   1 
ATOM   5286 C  CB  . VAL B 1 232 ? 57.547 -64.822 29.669  1.00 28.82  ?  232 VAL B CB  1 
ATOM   5287 C  CG1 . VAL B 1 232 ? 56.656 -63.700 30.204  1.00 29.35  ?  232 VAL B CG1 1 
ATOM   5288 C  CG2 . VAL B 1 232 ? 58.274 -64.347 28.417  1.00 27.01  ?  232 VAL B CG2 1 
ATOM   5289 N  N   . ALA B 1 233 ? 57.059 -66.843 31.959  1.00 33.70  ?  233 ALA B N   1 
ATOM   5290 C  CA  . ALA B 1 233 ? 56.272 -67.323 33.076  1.00 34.06  ?  233 ALA B CA  1 
ATOM   5291 C  C   . ALA B 1 233 ? 57.200 -67.741 34.205  1.00 34.32  ?  233 ALA B C   1 
ATOM   5292 O  O   . ALA B 1 233 ? 56.814 -67.647 35.372  1.00 33.03  ?  233 ALA B O   1 
ATOM   5293 C  CB  . ALA B 1 233 ? 55.414 -68.487 32.637  1.00 35.54  ?  233 ALA B CB  1 
ATOM   5294 N  N   . GLN B 1 234 ? 58.393 -68.238 33.837  1.00 34.06  ?  234 GLN B N   1 
ATOM   5295 C  CA  . GLN B 1 234 ? 59.349 -68.744 34.814  1.00 40.49  ?  234 GLN B CA  1 
ATOM   5296 C  C   . GLN B 1 234 ? 59.897 -67.603 35.674  1.00 41.34  ?  234 GLN B C   1 
ATOM   5297 O  O   . GLN B 1 234 ? 59.890 -67.674 36.908  1.00 39.07  ?  234 GLN B O   1 
ATOM   5298 C  CB  . GLN B 1 234 ? 60.492 -69.515 34.154  1.00 42.13  ?  234 GLN B CB  1 
ATOM   5299 C  CG  . GLN B 1 234 ? 60.037 -70.818 33.506  1.00 47.76  ?  234 GLN B CG  1 
ATOM   5300 C  CD  . GLN B 1 234 ? 61.171 -71.669 32.976  1.00 46.47  ?  234 GLN B CD  1 
ATOM   5301 O  OE1 . GLN B 1 234 ? 61.934 -72.243 33.753  1.00 48.08  ?  234 GLN B OE1 1 
ATOM   5302 N  NE2 . GLN B 1 234 ? 61.278 -71.790 31.658  1.00 45.87  ?  234 GLN B NE2 1 
ATOM   5303 N  N   . TYR B 1 235 ? 60.365 -66.543 35.012  1.00 36.94  ?  235 TYR B N   1 
ATOM   5304 C  CA  . TYR B 1 235 ? 61.038 -65.475 35.729  1.00 36.09  ?  235 TYR B CA  1 
ATOM   5305 C  C   . TYR B 1 235 ? 59.980 -64.656 36.465  1.00 33.52  ?  235 TYR B C   1 
ATOM   5306 O  O   . TYR B 1 235 ? 60.165 -64.294 37.624  1.00 34.75  ?  235 TYR B O   1 
ATOM   5307 C  CB  . TYR B 1 235 ? 62.006 -64.799 34.746  1.00 34.46  ?  235 TYR B CB  1 
ATOM   5308 C  CG  . TYR B 1 235 ? 63.204 -65.692 34.457  1.00 32.25  ?  235 TYR B CG  1 
ATOM   5309 C  CD1 . TYR B 1 235 ? 63.476 -66.168 33.181  1.00 34.86  ?  235 TYR B CD1 1 
ATOM   5310 C  CD2 . TYR B 1 235 ? 64.022 -66.122 35.495  1.00 32.85  ?  235 TYR B CD2 1 
ATOM   5311 C  CE1 . TYR B 1 235 ? 64.561 -66.999 32.934  1.00 37.31  ?  235 TYR B CE1 1 
ATOM   5312 C  CE2 . TYR B 1 235 ? 65.102 -66.958 35.268  1.00 34.90  ?  235 TYR B CE2 1 
ATOM   5313 C  CZ  . TYR B 1 235 ? 65.374 -67.396 33.983  1.00 38.83  ?  235 TYR B CZ  1 
ATOM   5314 O  OH  . TYR B 1 235 ? 66.445 -68.213 33.757  1.00 43.61  ?  235 TYR B OH  1 
ATOM   5315 N  N   . ALA B 1 236 ? 58.848 -64.406 35.811  1.00 32.94  ?  236 ALA B N   1 
ATOM   5316 C  CA  . ALA B 1 236 ? 57.734 -63.722 36.453  1.00 30.66  ?  236 ALA B CA  1 
ATOM   5317 C  C   . ALA B 1 236 ? 57.440 -64.360 37.816  1.00 32.59  ?  236 ALA B C   1 
ATOM   5318 O  O   . ALA B 1 236 ? 57.381 -63.670 38.834  1.00 30.66  ?  236 ALA B O   1 
ATOM   5319 C  CB  . ALA B 1 236 ? 56.527 -63.773 35.545  1.00 26.97  ?  236 ALA B CB  1 
ATOM   5320 N  N   . ALA B 1 237 ? 57.288 -65.694 37.802  1.00 33.34  ?  237 ALA B N   1 
ATOM   5321 C  CA  . ALA B 1 237 ? 56.960 -66.509 38.959  1.00 30.61  ?  237 ALA B CA  1 
ATOM   5322 C  C   . ALA B 1 237 ? 58.012 -66.360 40.048  1.00 31.21  ?  237 ALA B C   1 
ATOM   5323 O  O   . ALA B 1 237 ? 57.677 -66.037 41.182  1.00 32.56  ?  237 ALA B O   1 
ATOM   5324 C  CB  . ALA B 1 237 ? 56.868 -67.943 38.524  1.00 30.74  ?  237 ALA B CB  1 
ATOM   5325 N  N   . LEU B 1 238 ? 59.277 -66.598 39.679  1.00 33.07  ?  238 LEU B N   1 
ATOM   5326 C  CA  . LEU B 1 238 ? 60.413 -66.463 40.585  1.00 33.13  ?  238 LEU B CA  1 
ATOM   5327 C  C   . LEU B 1 238 ? 60.394 -65.104 41.283  1.00 35.30  ?  238 LEU B C   1 
ATOM   5328 O  O   . LEU B 1 238 ? 60.578 -65.038 42.503  1.00 34.60  ?  238 LEU B O   1 
ATOM   5329 C  CB  . LEU B 1 238 ? 61.730 -66.700 39.840  1.00 30.13  ?  238 LEU B CB  1 
ATOM   5330 C  CG  . LEU B 1 238 ? 62.086 -68.173 39.595  1.00 29.34  ?  238 LEU B CG  1 
ATOM   5331 C  CD1 . LEU B 1 238 ? 63.224 -68.378 38.616  1.00 29.05  ?  238 LEU B CD1 1 
ATOM   5332 C  CD2 . LEU B 1 238 ? 62.433 -68.859 40.900  1.00 28.73  ?  238 LEU B CD2 1 
ATOM   5333 N  N   . LYS B 1 239 ? 60.141 -64.040 40.505  1.00 37.95  ?  239 LYS B N   1 
ATOM   5334 C  CA  . LYS B 1 239 ? 60.155 -62.680 41.022  1.00 41.63  ?  239 LYS B CA  1 
ATOM   5335 C  C   . LYS B 1 239 ? 58.999 -62.482 42.002  1.00 41.23  ?  239 LYS B C   1 
ATOM   5336 O  O   . LYS B 1 239 ? 59.162 -61.786 42.994  1.00 44.10  ?  239 LYS B O   1 
ATOM   5337 C  CB  . LYS B 1 239 ? 60.165 -61.676 39.862  1.00 45.54  ?  239 LYS B CB  1 
ATOM   5338 C  CG  . LYS B 1 239 ? 60.642 -60.282 40.250  1.00 48.34  ?  239 LYS B CG  1 
ATOM   5339 C  CD  . LYS B 1 239 ? 62.093 -60.167 40.723  1.00 47.61  ?  239 LYS B CD  1 
ATOM   5340 C  CE  . LYS B 1 239 ? 62.173 -59.373 41.996  1.00 48.51  ?  239 LYS B CE  1 
ATOM   5341 N  NZ  . LYS B 1 239 ? 63.448 -58.710 42.250  1.00 45.16  1  239 LYS B NZ  1 
ATOM   5342 N  N   . VAL B 1 240 ? 57.849 -63.121 41.748  1.00 40.43  ?  240 VAL B N   1 
ATOM   5343 C  CA  . VAL B 1 240 ? 56.741 -63.075 42.689  1.00 41.61  ?  240 VAL B CA  1 
ATOM   5344 C  C   . VAL B 1 240 ? 57.146 -63.732 44.014  1.00 46.01  ?  240 VAL B C   1 
ATOM   5345 O  O   . VAL B 1 240 ? 56.768 -63.261 45.094  1.00 50.11  ?  240 VAL B O   1 
ATOM   5346 C  CB  . VAL B 1 240 ? 55.447 -63.693 42.135  1.00 37.34  ?  240 VAL B CB  1 
ATOM   5347 C  CG1 . VAL B 1 240 ? 54.367 -63.764 43.206  1.00 38.08  ?  240 VAL B CG1 1 
ATOM   5348 C  CG2 . VAL B 1 240 ? 54.914 -62.926 40.937  1.00 38.12  ?  240 VAL B CG2 1 
ATOM   5349 N  N   . ILE B 1 241 ? 57.909 -64.825 43.931  1.00 45.12  ?  241 ILE B N   1 
ATOM   5350 C  CA  . ILE B 1 241 ? 58.287 -65.585 45.114  1.00 43.58  ?  241 ILE B CA  1 
ATOM   5351 C  C   . ILE B 1 241 ? 59.217 -64.727 45.974  1.00 40.92  ?  241 ILE B C   1 
ATOM   5352 O  O   . ILE B 1 241 ? 58.957 -64.558 47.162  1.00 35.51  ?  241 ILE B O   1 
ATOM   5353 C  CB  . ILE B 1 241 ? 58.896 -66.939 44.702  1.00 43.74  ?  241 ILE B CB  1 
ATOM   5354 C  CG1 . ILE B 1 241 ? 57.873 -67.769 43.933  1.00 42.08  ?  241 ILE B CG1 1 
ATOM   5355 C  CG2 . ILE B 1 241 ? 59.450 -67.704 45.903  1.00 45.24  ?  241 ILE B CG2 1 
ATOM   5356 C  CD1 . ILE B 1 241 ? 58.451 -68.958 43.193  1.00 42.11  ?  241 ILE B CD1 1 
ATOM   5357 N  N   . GLU B 1 242 ? 60.241 -64.129 45.341  1.00 44.08  ?  242 GLU B N   1 
ATOM   5358 C  CA  . GLU B 1 242 ? 61.212 -63.267 46.003  1.00 41.19  ?  242 GLU B CA  1 
ATOM   5359 C  C   . GLU B 1 242 ? 60.503 -62.185 46.811  1.00 42.58  ?  242 GLU B C   1 
ATOM   5360 O  O   . GLU B 1 242 ? 60.841 -61.963 47.958  1.00 48.72  ?  242 GLU B O   1 
ATOM   5361 C  CB  . GLU B 1 242 ? 62.144 -62.626 44.974  1.00 41.64  ?  242 GLU B CB  1 
ATOM   5362 C  CG  . GLU B 1 242 ? 63.256 -61.784 45.596  1.00 43.55  ?  242 GLU B CG  1 
ATOM   5363 C  CD  . GLU B 1 242 ? 64.210 -61.104 44.623  1.00 44.02  ?  242 GLU B CD  1 
ATOM   5364 O  OE1 . GLU B 1 242 ? 64.323 -61.469 43.420  1.00 39.19  ?  242 GLU B OE1 1 
ATOM   5365 O  OE2 . GLU B 1 242 ? 64.837 -60.143 45.120  1.00 46.69  -1 242 GLU B OE2 1 
ATOM   5366 N  N   . LEU B 1 243 ? 59.482 -61.550 46.224  1.00 49.08  ?  243 LEU B N   1 
ATOM   5367 C  CA  . LEU B 1 243 ? 58.761 -60.437 46.836  1.00 42.80  ?  243 LEU B CA  1 
ATOM   5368 C  C   . LEU B 1 243 ? 57.720 -60.912 47.855  1.00 37.55  ?  243 LEU B C   1 
ATOM   5369 O  O   . LEU B 1 243 ? 56.904 -60.120 48.321  1.00 32.00  ?  243 LEU B O   1 
ATOM   5370 C  CB  . LEU B 1 243 ? 58.086 -59.650 45.708  1.00 41.20  ?  243 LEU B CB  1 
ATOM   5371 C  CG  . LEU B 1 243 ? 59.009 -59.023 44.658  1.00 41.69  ?  243 LEU B CG  1 
ATOM   5372 C  CD1 . LEU B 1 243 ? 58.217 -58.024 43.827  1.00 45.24  ?  243 LEU B CD1 1 
ATOM   5373 C  CD2 . LEU B 1 243 ? 60.229 -58.363 45.268  1.00 41.58  ?  243 LEU B CD2 1 
ATOM   5374 N  N   . GLY B 1 244 ? 57.693 -62.216 48.139  1.00 38.54  ?  244 GLY B N   1 
ATOM   5375 C  CA  . GLY B 1 244 ? 56.869 -62.760 49.207  1.00 42.84  ?  244 GLY B CA  1 
ATOM   5376 C  C   . GLY B 1 244 ? 55.470 -63.177 48.745  1.00 43.90  ?  244 GLY B C   1 
ATOM   5377 O  O   . GLY B 1 244 ? 54.586 -63.317 49.598  1.00 39.55  ?  244 GLY B O   1 
ATOM   5378 N  N   . GLY B 1 245 ? 55.297 -63.408 47.424  1.00 38.40  ?  245 GLY B N   1 
ATOM   5379 C  CA  . GLY B 1 245 ? 54.012 -63.768 46.849  1.00 35.63  ?  245 GLY B CA  1 
ATOM   5380 C  C   . GLY B 1 245 ? 53.920 -65.266 46.597  1.00 36.06  ?  245 GLY B C   1 
ATOM   5381 O  O   . GLY B 1 245 ? 54.955 -65.920 46.584  1.00 34.04  ?  245 GLY B O   1 
ATOM   5382 N  N   . ARG B 1 246 ? 52.688 -65.777 46.370  1.00 43.25  ?  246 ARG B N   1 
ATOM   5383 C  CA  . ARG B 1 246 ? 52.418 -67.203 46.169  1.00 46.14  ?  246 ARG B CA  1 
ATOM   5384 C  C   . ARG B 1 246 ? 51.922 -67.440 44.741  1.00 45.37  ?  246 ARG B C   1 
ATOM   5385 O  O   . ARG B 1 246 ? 50.897 -66.880 44.361  1.00 46.72  ?  246 ARG B O   1 
ATOM   5386 C  CB  . ARG B 1 246 ? 51.364 -67.737 47.158  1.00 47.65  ?  246 ARG B CB  1 
ATOM   5387 C  CG  . ARG B 1 246 ? 51.494 -67.217 48.585  1.00 46.00  ?  246 ARG B CG  1 
ATOM   5388 C  CD  . ARG B 1 246 ? 51.090 -68.195 49.668  1.00 45.07  ?  246 ARG B CD  1 
ATOM   5389 N  NE  . ARG B 1 246 ? 50.824 -67.465 50.914  1.00 48.95  ?  246 ARG B NE  1 
ATOM   5390 C  CZ  . ARG B 1 246 ? 49.736 -66.729 51.159  1.00 54.02  ?  246 ARG B CZ  1 
ATOM   5391 N  NH1 . ARG B 1 246 ? 48.703 -66.737 50.331  1.00 50.01  1  246 ARG B NH1 1 
ATOM   5392 N  NH2 . ARG B 1 246 ? 49.660 -66.005 52.263  1.00 59.53  ?  246 ARG B NH2 1 
ATOM   5393 N  N   . VAL B 1 247 ? 52.646 -68.275 43.970  1.00 42.71  ?  247 VAL B N   1 
ATOM   5394 C  CA  . VAL B 1 247 ? 52.317 -68.602 42.582  1.00 39.48  ?  247 VAL B CA  1 
ATOM   5395 C  C   . VAL B 1 247 ? 51.512 -69.900 42.552  1.00 39.88  ?  247 VAL B C   1 
ATOM   5396 O  O   . VAL B 1 247 ? 52.041 -70.958 42.893  1.00 43.13  ?  247 VAL B O   1 
ATOM   5397 C  CB  . VAL B 1 247 ? 53.570 -68.768 41.695  1.00 39.76  ?  247 VAL B CB  1 
ATOM   5398 C  CG1 . VAL B 1 247 ? 53.218 -68.866 40.208  1.00 37.18  ?  247 VAL B CG1 1 
ATOM   5399 C  CG2 . VAL B 1 247 ? 54.618 -67.682 41.945  1.00 36.32  ?  247 VAL B CG2 1 
ATOM   5400 N  N   . VAL B 1 248 ? 50.259 -69.813 42.087  1.00 38.36  ?  248 VAL B N   1 
ATOM   5401 C  CA  . VAL B 1 248 ? 49.281 -70.883 42.221  1.00 37.12  ?  248 VAL B CA  1 
ATOM   5402 C  C   . VAL B 1 248 ? 49.259 -71.730 40.942  1.00 38.86  ?  248 VAL B C   1 
ATOM   5403 O  O   . VAL B 1 248 ? 48.882 -72.898 41.000  1.00 44.88  ?  248 VAL B O   1 
ATOM   5404 C  CB  . VAL B 1 248 ? 47.854 -70.392 42.604  1.00 39.13  ?  248 VAL B CB  1 
ATOM   5405 C  CG1 . VAL B 1 248 ? 47.651 -70.230 44.107  1.00 39.29  ?  248 VAL B CG1 1 
ATOM   5406 C  CG2 . VAL B 1 248 ? 47.451 -69.084 41.932  1.00 41.19  ?  248 VAL B CG2 1 
ATOM   5407 N  N   . SER B 1 249 ? 49.658 -71.177 39.781  1.00 39.22  ?  249 SER B N   1 
ATOM   5408 C  CA  . SER B 1 249 ? 49.358 -71.811 38.497  1.00 37.96  ?  249 SER B CA  1 
ATOM   5409 C  C   . SER B 1 249 ? 50.520 -71.695 37.517  1.00 37.74  ?  249 SER B C   1 
ATOM   5410 O  O   . SER B 1 249 ? 51.129 -70.639 37.456  1.00 40.63  ?  249 SER B O   1 
ATOM   5411 C  CB  . SER B 1 249 ? 48.185 -71.146 37.876  1.00 39.04  ?  249 SER B CB  1 
ATOM   5412 O  OG  . SER B 1 249 ? 48.564 -69.818 37.536  1.00 37.29  ?  249 SER B OG  1 
ATOM   5413 N  N   . LEU B 1 250 ? 50.782 -72.753 36.729  1.00 37.13  ?  250 LEU B N   1 
ATOM   5414 C  CA  . LEU B 1 250 ? 51.515 -72.642 35.466  1.00 35.20  ?  250 LEU B CA  1 
ATOM   5415 C  C   . LEU B 1 250 ? 50.775 -73.447 34.399  1.00 33.64  ?  250 LEU B C   1 
ATOM   5416 O  O   . LEU B 1 250 ? 49.910 -74.230 34.742  1.00 30.78  ?  250 LEU B O   1 
ATOM   5417 C  CB  . LEU B 1 250 ? 52.966 -73.107 35.574  1.00 33.27  ?  250 LEU B CB  1 
ATOM   5418 C  CG  . LEU B 1 250 ? 53.885 -72.216 36.411  1.00 37.14  ?  250 LEU B CG  1 
ATOM   5419 C  CD1 . LEU B 1 250 ? 55.315 -72.725 36.345  1.00 40.48  ?  250 LEU B CD1 1 
ATOM   5420 C  CD2 . LEU B 1 250 ? 53.818 -70.760 35.992  1.00 35.38  ?  250 LEU B CD2 1 
ATOM   5421 N  N   . SER B 1 251 ? 51.142 -73.278 33.117  1.00 37.46  ?  251 SER B N   1 
ATOM   5422 C  CA  . SER B 1 251 ? 50.473 -73.965 32.019  1.00 39.29  ?  251 SER B CA  1 
ATOM   5423 C  C   . SER B 1 251 ? 51.442 -74.244 30.875  1.00 42.56  ?  251 SER B C   1 
ATOM   5424 O  O   . SER B 1 251 ? 52.474 -73.597 30.775  1.00 41.70  ?  251 SER B O   1 
ATOM   5425 C  CB  . SER B 1 251 ? 49.303 -73.182 31.513  1.00 41.23  ?  251 SER B CB  1 
ATOM   5426 O  OG  . SER B 1 251 ? 49.719 -72.157 30.624  1.00 44.01  ?  251 SER B OG  1 
ATOM   5427 N  N   . ASP B 1 252 ? 51.081 -75.232 30.040  1.00 48.48  ?  252 ASP B N   1 
ATOM   5428 C  CA  . ASP B 1 252 ? 51.682 -75.505 28.741  1.00 44.61  ?  252 ASP B CA  1 
ATOM   5429 C  C   . ASP B 1 252 ? 50.534 -75.605 27.732  1.00 45.05  ?  252 ASP B C   1 
ATOM   5430 O  O   . ASP B 1 252 ? 49.356 -75.461 28.095  1.00 38.42  ?  252 ASP B O   1 
ATOM   5431 C  CB  . ASP B 1 252 ? 52.584 -76.737 28.772  1.00 45.40  ?  252 ASP B CB  1 
ATOM   5432 C  CG  . ASP B 1 252 ? 51.918 -78.115 28.767  1.00 52.50  ?  252 ASP B CG  1 
ATOM   5433 O  OD1 . ASP B 1 252 ? 50.656 -78.196 28.666  1.00 47.54  ?  252 ASP B OD1 1 
ATOM   5434 O  OD2 . ASP B 1 252 ? 52.671 -79.118 28.883  1.00 53.85  -1 252 ASP B OD2 1 
ATOM   5435 N  N   . SER B 1 253 ? 50.885 -75.892 26.469  1.00 45.79  ?  253 SER B N   1 
ATOM   5436 C  CA  . SER B 1 253 ? 49.913 -75.962 25.386  1.00 44.38  ?  253 SER B CA  1 
ATOM   5437 C  C   . SER B 1 253 ? 48.952 -77.148 25.551  1.00 42.45  ?  253 SER B C   1 
ATOM   5438 O  O   . SER B 1 253 ? 47.920 -77.176 24.882  1.00 38.47  ?  253 SER B O   1 
ATOM   5439 C  CB  . SER B 1 253 ? 50.609 -76.016 24.052  1.00 42.27  ?  253 SER B CB  1 
ATOM   5440 O  OG  . SER B 1 253 ? 51.379 -77.203 23.956  1.00 42.38  ?  253 SER B OG  1 
ATOM   5441 N  N   . GLN B 1 254 ? 49.276 -78.112 26.433  1.00 41.84  ?  254 GLN B N   1 
ATOM   5442 C  CA  . GLN B 1 254 ? 48.463 -79.313 26.598  1.00 44.79  ?  254 GLN B CA  1 
ATOM   5443 C  C   . GLN B 1 254 ? 47.593 -79.265 27.863  1.00 43.75  ?  254 GLN B C   1 
ATOM   5444 O  O   . GLN B 1 254 ? 46.945 -80.258 28.183  1.00 45.06  ?  254 GLN B O   1 
ATOM   5445 C  CB  . GLN B 1 254 ? 49.341 -80.575 26.564  1.00 45.80  ?  254 GLN B CB  1 
ATOM   5446 C  CG  . GLN B 1 254 ? 49.919 -80.919 25.191  1.00 45.84  ?  254 GLN B CG  1 
ATOM   5447 C  CD  . GLN B 1 254 ? 50.937 -79.913 24.694  1.00 49.84  ?  254 GLN B CD  1 
ATOM   5448 O  OE1 . GLN B 1 254 ? 51.566 -79.188 25.479  1.00 57.32  ?  254 GLN B OE1 1 
ATOM   5449 N  NE2 . GLN B 1 254 ? 51.112 -79.853 23.380  1.00 45.37  ?  254 GLN B NE2 1 
ATOM   5450 N  N   . GLY B 1 255 ? 47.534 -78.122 28.565  1.00 42.64  ?  255 GLY B N   1 
ATOM   5451 C  CA  . GLY B 1 255 ? 46.781 -78.015 29.815  1.00 40.51  ?  255 GLY B CA  1 
ATOM   5452 C  C   . GLY B 1 255 ? 47.606 -77.356 30.922  1.00 38.89  ?  255 GLY B C   1 
ATOM   5453 O  O   . GLY B 1 255 ? 48.769 -77.029 30.695  1.00 36.88  ?  255 GLY B O   1 
ATOM   5454 N  N   . SER B 1 256 ? 47.010 -77.163 32.111  1.00 36.92  ?  256 SER B N   1 
ATOM   5455 C  CA  . SER B 1 256 ? 47.646 -76.378 33.163  1.00 40.99  ?  256 SER B CA  1 
ATOM   5456 C  C   . SER B 1 256 ? 47.830 -77.178 34.450  1.00 43.98  ?  256 SER B C   1 
ATOM   5457 O  O   . SER B 1 256 ? 47.208 -78.216 34.627  1.00 51.95  ?  256 SER B O   1 
ATOM   5458 C  CB  . SER B 1 256 ? 46.877 -75.133 33.446  1.00 42.39  ?  256 SER B CB  1 
ATOM   5459 O  OG  . SER B 1 256 ? 45.572 -75.496 33.856  1.00 56.96  ?  256 SER B OG  1 
ATOM   5460 N  N   . LEU B 1 257 ? 48.692 -76.656 35.339  1.00 47.62  ?  257 LEU B N   1 
ATOM   5461 C  CA  . LEU B 1 257 ? 48.989 -77.223 36.648  1.00 49.89  ?  257 LEU B CA  1 
ATOM   5462 C  C   . LEU B 1 257 ? 48.600 -76.216 37.728  1.00 54.94  ?  257 LEU B C   1 
ATOM   5463 O  O   . LEU B 1 257 ? 49.126 -75.100 37.744  1.00 56.11  ?  257 LEU B O   1 
ATOM   5464 C  CB  . LEU B 1 257 ? 50.481 -77.537 36.768  1.00 51.26  ?  257 LEU B CB  1 
ATOM   5465 C  CG  . LEU B 1 257 ? 50.955 -78.932 36.359  1.00 51.81  ?  257 LEU B CG  1 
ATOM   5466 C  CD1 . LEU B 1 257 ? 52.458 -78.972 36.443  1.00 56.07  ?  257 LEU B CD1 1 
ATOM   5467 C  CD2 . LEU B 1 257 ? 50.388 -80.013 37.233  1.00 56.71  ?  257 LEU B CD2 1 
ATOM   5468 N  N   . ILE B 1 258 ? 47.734 -76.643 38.659  1.00 58.00  ?  258 ILE B N   1 
ATOM   5469 C  CA  . ILE B 1 258 ? 47.240 -75.775 39.720  1.00 64.37  ?  258 ILE B CA  1 
ATOM   5470 C  C   . ILE B 1 258 ? 47.691 -76.326 41.080  1.00 72.07  ?  258 ILE B C   1 
ATOM   5471 O  O   . ILE B 1 258 ? 47.634 -77.535 41.309  1.00 72.19  ?  258 ILE B O   1 
ATOM   5472 C  CB  . ILE B 1 258 ? 45.707 -75.646 39.620  1.00 60.16  ?  258 ILE B CB  1 
ATOM   5473 C  CG1 . ILE B 1 258 ? 45.238 -75.620 38.158  1.00 57.83  ?  258 ILE B CG1 1 
ATOM   5474 C  CG2 . ILE B 1 258 ? 45.182 -74.455 40.431  1.00 51.87  ?  258 ILE B CG2 1 
ATOM   5475 C  CD1 . ILE B 1 258 ? 45.735 -74.441 37.349  1.00 57.94  ?  258 ILE B CD1 1 
ATOM   5476 N  N   . VAL B 1 259 ? 48.144 -75.421 41.966  1.00 72.71  ?  259 VAL B N   1 
ATOM   5477 C  CA  . VAL B 1 259 ? 48.543 -75.738 43.330  1.00 72.89  ?  259 VAL B CA  1 
ATOM   5478 C  C   . VAL B 1 259 ? 47.297 -75.859 44.204  1.00 76.88  ?  259 VAL B C   1 
ATOM   5479 O  O   . VAL B 1 259 ? 46.435 -74.986 44.131  1.00 76.77  ?  259 VAL B O   1 
ATOM   5480 C  CB  . VAL B 1 259 ? 49.465 -74.613 43.841  1.00 77.15  ?  259 VAL B CB  1 
ATOM   5481 C  CG1 . VAL B 1 259 ? 49.678 -74.659 45.351  1.00 83.34  ?  259 VAL B CG1 1 
ATOM   5482 C  CG2 . VAL B 1 259 ? 50.805 -74.612 43.121  1.00 78.26  ?  259 VAL B CG2 1 
ATOM   5483 N  N   . LYS B 1 260 ? 47.219 -76.910 45.044  1.00 81.36  ?  260 LYS B N   1 
ATOM   5484 C  CA  . LYS B 1 260 ? 46.076 -77.070 45.941  1.00 87.18  ?  260 LYS B CA  1 
ATOM   5485 C  C   . LYS B 1 260 ? 46.381 -77.868 47.219  1.00 86.03  ?  260 LYS B C   1 
ATOM   5486 O  O   . LYS B 1 260 ? 45.548 -77.853 48.124  1.00 84.28  ?  260 LYS B O   1 
ATOM   5487 C  CB  . LYS B 1 260 ? 44.874 -77.650 45.176  1.00 90.90  ?  260 LYS B CB  1 
ATOM   5488 C  CG  . LYS B 1 260 ? 43.469 -77.351 45.736  1.00 84.82  ?  260 LYS B CG  1 
ATOM   5489 C  CD  . LYS B 1 260 ? 42.752 -78.519 46.414  1.00 79.10  ?  260 LYS B CD  1 
ATOM   5490 C  CE  . LYS B 1 260 ? 41.254 -78.390 46.416  1.00 75.00  ?  260 LYS B CE  1 
ATOM   5491 N  NZ  . LYS B 1 260 ? 40.687 -78.377 45.061  1.00 71.43  1  260 LYS B NZ  1 
ATOM   5492 N  N   . ASP B 1 261 ? 47.527 -78.564 47.339  1.00 86.10  ?  261 ASP B N   1 
ATOM   5493 C  CA  . ASP B 1 261 ? 47.888 -79.147 48.629  1.00 86.43  ?  261 ASP B CA  1 
ATOM   5494 C  C   . ASP B 1 261 ? 48.631 -78.130 49.483  1.00 83.86  ?  261 ASP B C   1 
ATOM   5495 O  O   . ASP B 1 261 ? 48.257 -77.897 50.632  1.00 75.69  ?  261 ASP B O   1 
ATOM   5496 C  CB  . ASP B 1 261 ? 48.824 -80.343 48.585  1.00 90.88  ?  261 ASP B CB  1 
ATOM   5497 C  CG  . ASP B 1 261 ? 49.329 -80.785 49.960  1.00 87.35  ?  261 ASP B CG  1 
ATOM   5498 O  OD1 . ASP B 1 261 ? 48.480 -81.196 50.782  1.00 78.49  ?  261 ASP B OD1 1 
ATOM   5499 O  OD2 . ASP B 1 261 ? 50.559 -80.686 50.220  1.00 80.91  -1 261 ASP B OD2 1 
ATOM   5500 N  N   . LYS B 1 262 ? 49.719 -77.598 48.911  1.00 84.55  ?  262 LYS B N   1 
ATOM   5501 C  CA  . LYS B 1 262 ? 50.530 -76.570 49.542  1.00 86.86  ?  262 LYS B CA  1 
ATOM   5502 C  C   . LYS B 1 262 ? 50.121 -75.214 48.962  1.00 80.21  ?  262 LYS B C   1 
ATOM   5503 O  O   . LYS B 1 262 ? 49.229 -75.139 48.119  1.00 85.82  ?  262 LYS B O   1 
ATOM   5504 C  CB  . LYS B 1 262 ? 52.023 -76.894 49.364  1.00 96.71  ?  262 LYS B CB  1 
ATOM   5505 C  CG  . LYS B 1 262 ? 52.559 -78.174 50.022  1.00 92.34  ?  262 LYS B CG  1 
ATOM   5506 C  CD  . LYS B 1 262 ? 52.268 -78.351 51.512  1.00 92.45  ?  262 LYS B CD  1 
ATOM   5507 C  CE  . LYS B 1 262 ? 52.775 -77.263 52.424  1.00 83.73  ?  262 LYS B CE  1 
ATOM   5508 N  NZ  . LYS B 1 262 ? 51.850 -76.141 52.631  1.00 77.08  1  262 LYS B NZ  1 
ATOM   5509 N  N   . ASP B 1 263 ? 50.784 -74.148 49.428  1.00 70.94  ?  263 ASP B N   1 
ATOM   5510 C  CA  . ASP B 1 263 ? 50.369 -72.776 49.177  1.00 62.61  ?  263 ASP B CA  1 
ATOM   5511 C  C   . ASP B 1 263 ? 50.824 -72.309 47.794  1.00 58.45  ?  263 ASP B C   1 
ATOM   5512 O  O   . ASP B 1 263 ? 50.048 -71.653 47.094  1.00 65.60  ?  263 ASP B O   1 
ATOM   5513 C  CB  . ASP B 1 263 ? 50.882 -71.842 50.267  1.00 66.73  ?  263 ASP B CB  1 
ATOM   5514 C  CG  . ASP B 1 263 ? 49.855 -71.330 51.270  1.00 67.35  ?  263 ASP B CG  1 
ATOM   5515 O  OD1 . ASP B 1 263 ? 48.800 -70.842 50.823  1.00 71.38  ?  263 ASP B OD1 1 
ATOM   5516 O  OD2 . ASP B 1 263 ? 50.138 -71.377 52.486  1.00 65.26  -1 263 ASP B OD2 1 
ATOM   5517 N  N   . SER B 1 264 ? 52.084 -72.620 47.428  1.00 46.95  ?  264 SER B N   1 
ATOM   5518 C  CA  . SER B 1 264 ? 52.723 -72.090 46.227  1.00 44.41  ?  264 SER B CA  1 
ATOM   5519 C  C   . SER B 1 264 ? 53.704 -73.083 45.595  1.00 46.24  ?  264 SER B C   1 
ATOM   5520 O  O   . SER B 1 264 ? 54.175 -74.019 46.247  1.00 40.67  ?  264 SER B O   1 
ATOM   5521 C  CB  . SER B 1 264 ? 53.439 -70.788 46.525  1.00 43.24  ?  264 SER B CB  1 
ATOM   5522 O  OG  . SER B 1 264 ? 54.657 -70.679 45.791  1.00 39.33  ?  264 SER B OG  1 
ATOM   5523 N  N   . PHE B 1 265 ? 54.033 -72.844 44.310  1.00 48.50  ?  265 PHE B N   1 
ATOM   5524 C  CA  . PHE B 1 265 ? 55.175 -73.483 43.652  1.00 41.85  ?  265 PHE B CA  1 
ATOM   5525 C  C   . PHE B 1 265 ? 56.457 -73.019 44.349  1.00 36.75  ?  265 PHE B C   1 
ATOM   5526 O  O   . PHE B 1 265 ? 56.549 -71.876 44.812  1.00 31.84  ?  265 PHE B O   1 
ATOM   5527 C  CB  . PHE B 1 265 ? 55.377 -73.153 42.164  1.00 37.54  ?  265 PHE B CB  1 
ATOM   5528 C  CG  . PHE B 1 265 ? 54.350 -73.682 41.163  1.00 37.49  ?  265 PHE B CG  1 
ATOM   5529 C  CD1 . PHE B 1 265 ? 53.090 -73.094 41.031  1.00 35.34  ?  265 PHE B CD1 1 
ATOM   5530 C  CD2 . PHE B 1 265 ? 54.675 -74.705 40.279  1.00 35.07  ?  265 PHE B CD2 1 
ATOM   5531 C  CE1 . PHE B 1 265 ? 52.178 -73.550 40.091  1.00 31.37  ?  265 PHE B CE1 1 
ATOM   5532 C  CE2 . PHE B 1 265 ? 53.748 -75.162 39.353  1.00 34.46  ?  265 PHE B CE2 1 
ATOM   5533 C  CZ  . PHE B 1 265 ? 52.500 -74.581 39.261  1.00 31.04  ?  265 PHE B CZ  1 
ATOM   5534 N  N   . THR B 1 266 ? 57.438 -73.921 44.415  1.00 32.31  ?  266 THR B N   1 
ATOM   5535 C  CA  . THR B 1 266 ? 58.729 -73.596 44.985  1.00 33.92  ?  266 THR B CA  1 
ATOM   5536 C  C   . THR B 1 266 ? 59.650 -73.343 43.800  1.00 36.85  ?  266 THR B C   1 
ATOM   5537 O  O   . THR B 1 266 ? 59.419 -73.904 42.728  1.00 42.69  ?  266 THR B O   1 
ATOM   5538 C  CB  . THR B 1 266 ? 59.217 -74.737 45.881  1.00 34.91  ?  266 THR B CB  1 
ATOM   5539 O  OG1 . THR B 1 266 ? 58.193 -75.059 46.827  1.00 30.53  ?  266 THR B OG1 1 
ATOM   5540 C  CG2 . THR B 1 266 ? 60.515 -74.403 46.605  1.00 35.21  ?  266 THR B CG2 1 
ATOM   5541 N  N   . PRO B 1 267 ? 60.681 -72.476 43.922  1.00 35.55  ?  267 PRO B N   1 
ATOM   5542 C  CA  . PRO B 1 267 ? 61.655 -72.307 42.840  1.00 36.69  ?  267 PRO B CA  1 
ATOM   5543 C  C   . PRO B 1 267 ? 62.068 -73.621 42.163  1.00 39.61  ?  267 PRO B C   1 
ATOM   5544 O  O   . PRO B 1 267 ? 62.149 -73.679 40.940  1.00 36.63  ?  267 PRO B O   1 
ATOM   5545 C  CB  . PRO B 1 267 ? 62.831 -71.586 43.546  1.00 33.58  ?  267 PRO B CB  1 
ATOM   5546 C  CG  . PRO B 1 267 ? 62.147 -70.772 44.628  1.00 34.51  ?  267 PRO B CG  1 
ATOM   5547 C  CD  . PRO B 1 267 ? 60.940 -71.586 45.068  1.00 34.35  ?  267 PRO B CD  1 
ATOM   5548 N  N   . ALA B 1 268 ? 62.294 -74.692 42.948  1.00 42.10  ?  268 ALA B N   1 
ATOM   5549 C  CA  . ALA B 1 268 ? 62.800 -75.953 42.411  1.00 41.39  ?  268 ALA B CA  1 
ATOM   5550 C  C   . ALA B 1 268 ? 61.737 -76.651 41.557  1.00 39.56  ?  268 ALA B C   1 
ATOM   5551 O  O   . ALA B 1 268 ? 62.059 -77.328 40.587  1.00 37.72  ?  268 ALA B O   1 
ATOM   5552 C  CB  . ALA B 1 268 ? 63.312 -76.831 43.537  1.00 40.61  ?  268 ALA B CB  1 
ATOM   5553 N  N   . GLU B 1 269 ? 60.465 -76.446 41.903  1.00 41.66  ?  269 GLU B N   1 
ATOM   5554 C  CA  . GLU B 1 269 ? 59.360 -76.945 41.106  1.00 46.55  ?  269 GLU B CA  1 
ATOM   5555 C  C   . GLU B 1 269 ? 59.260 -76.168 39.795  1.00 51.70  ?  269 GLU B C   1 
ATOM   5556 O  O   . GLU B 1 269 ? 58.964 -76.765 38.761  1.00 53.12  ?  269 GLU B O   1 
ATOM   5557 C  CB  . GLU B 1 269 ? 58.078 -76.882 41.931  1.00 48.92  ?  269 GLU B CB  1 
ATOM   5558 C  CG  . GLU B 1 269 ? 58.160 -77.786 43.156  1.00 52.27  ?  269 GLU B CG  1 
ATOM   5559 C  CD  . GLU B 1 269 ? 57.068 -77.606 44.182  1.00 54.36  ?  269 GLU B CD  1 
ATOM   5560 O  OE1 . GLU B 1 269 ? 56.258 -76.664 44.049  1.00 53.55  ?  269 GLU B OE1 1 
ATOM   5561 O  OE2 . GLU B 1 269 ? 57.063 -78.421 45.126  1.00 59.05  -1 269 GLU B OE2 1 
ATOM   5562 N  N   . ILE B 1 270 ? 59.509 -74.848 39.849  1.00 52.26  ?  270 ILE B N   1 
ATOM   5563 C  CA  . ILE B 1 270 ? 59.670 -74.034 38.646  1.00 53.52  ?  270 ILE B CA  1 
ATOM   5564 C  C   . ILE B 1 270 ? 60.920 -74.491 37.884  1.00 58.07  ?  270 ILE B C   1 
ATOM   5565 O  O   . ILE B 1 270 ? 60.902 -74.659 36.666  1.00 65.33  ?  270 ILE B O   1 
ATOM   5566 C  CB  . ILE B 1 270 ? 59.771 -72.529 38.973  1.00 50.09  ?  270 ILE B CB  1 
ATOM   5567 C  CG1 . ILE B 1 270 ? 58.621 -72.008 39.859  1.00 53.41  ?  270 ILE B CG1 1 
ATOM   5568 C  CG2 . ILE B 1 270 ? 59.917 -71.702 37.694  1.00 45.63  ?  270 ILE B CG2 1 
ATOM   5569 C  CD1 . ILE B 1 270 ? 57.263 -71.927 39.182  1.00 54.37  ?  270 ILE B CD1 1 
ATOM   5570 N  N   . ASP B 1 271 ? 62.016 -74.674 38.622  1.00 56.99  ?  271 ASP B N   1 
ATOM   5571 C  CA  . ASP B 1 271 ? 63.300 -75.037 38.052  1.00 63.32  ?  271 ASP B CA  1 
ATOM   5572 C  C   . ASP B 1 271 ? 63.204 -76.389 37.342  1.00 62.79  ?  271 ASP B C   1 
ATOM   5573 O  O   . ASP B 1 271 ? 64.004 -76.680 36.452  1.00 59.71  ?  271 ASP B O   1 
ATOM   5574 C  CB  . ASP B 1 271 ? 64.364 -75.106 39.137  1.00 67.61  ?  271 ASP B CB  1 
ATOM   5575 C  CG  . ASP B 1 271 ? 65.716 -74.522 38.767  1.00 75.77  ?  271 ASP B CG  1 
ATOM   5576 O  OD1 . ASP B 1 271 ? 66.306 -73.857 39.643  1.00 80.83  ?  271 ASP B OD1 1 
ATOM   5577 O  OD2 . ASP B 1 271 ? 66.145 -74.709 37.602  1.00 82.16  -1 271 ASP B OD2 1 
ATOM   5578 N  N   . ALA B 1 272 ? 62.244 -77.223 37.763  1.00 57.82  ?  272 ALA B N   1 
ATOM   5579 C  CA  . ALA B 1 272 ? 62.118 -78.567 37.225  1.00 56.97  ?  272 ALA B CA  1 
ATOM   5580 C  C   . ALA B 1 272 ? 61.258 -78.556 35.961  1.00 54.10  ?  272 ALA B C   1 
ATOM   5581 O  O   . ALA B 1 272 ? 61.401 -79.449 35.134  1.00 49.44  ?  272 ALA B O   1 
ATOM   5582 C  CB  . ALA B 1 272 ? 61.567 -79.504 38.280  1.00 54.20  ?  272 ALA B CB  1 
ATOM   5583 N  N   . ILE B 1 273 ? 60.379 -77.548 35.823  1.00 50.72  ?  273 ILE B N   1 
ATOM   5584 C  CA  . ILE B 1 273 ? 59.577 -77.369 34.619  1.00 50.62  ?  273 ILE B CA  1 
ATOM   5585 C  C   . ILE B 1 273 ? 60.436 -76.730 33.525  1.00 48.35  ?  273 ILE B C   1 
ATOM   5586 O  O   . ILE B 1 273 ? 60.124 -76.838 32.342  1.00 47.79  ?  273 ILE B O   1 
ATOM   5587 C  CB  . ILE B 1 273 ? 58.289 -76.573 34.922  1.00 50.17  ?  273 ILE B CB  1 
ATOM   5588 C  CG1 . ILE B 1 273 ? 57.415 -77.307 35.936  1.00 51.01  ?  273 ILE B CG1 1 
ATOM   5589 C  CG2 . ILE B 1 273 ? 57.495 -76.275 33.648  1.00 51.09  ?  273 ILE B CG2 1 
ATOM   5590 C  CD1 . ILE B 1 273 ? 56.365 -76.436 36.598  1.00 55.18  ?  273 ILE B CD1 1 
ATOM   5591 N  N   . ALA B 1 274 ? 61.538 -76.084 33.918  1.00 46.82  ?  274 ALA B N   1 
ATOM   5592 C  CA  . ALA B 1 274 ? 62.487 -75.540 32.960  1.00 46.21  ?  274 ALA B CA  1 
ATOM   5593 C  C   . ALA B 1 274 ? 63.227 -76.673 32.260  1.00 49.68  ?  274 ALA B C   1 
ATOM   5594 O  O   . ALA B 1 274 ? 63.473 -76.604 31.059  1.00 54.45  ?  274 ALA B O   1 
ATOM   5595 C  CB  . ALA B 1 274 ? 63.457 -74.628 33.663  1.00 46.40  ?  274 ALA B CB  1 
ATOM   5596 N  N   . ALA B 1 275 ? 63.596 -77.699 33.039  1.00 51.94  ?  275 ALA B N   1 
ATOM   5597 C  CA  . ALA B 1 275 ? 64.172 -78.929 32.515  1.00 52.83  ?  275 ALA B CA  1 
ATOM   5598 C  C   . ALA B 1 275 ? 63.176 -79.672 31.620  1.00 59.00  ?  275 ALA B C   1 
ATOM   5599 O  O   . ALA B 1 275 ? 63.576 -80.384 30.694  1.00 60.83  ?  275 ALA B O   1 
ATOM   5600 C  CB  . ALA B 1 275 ? 64.609 -79.801 33.665  1.00 52.85  ?  275 ALA B CB  1 
ATOM   5601 N  N   . LEU B 1 276 ? 61.877 -79.505 31.912  1.00 56.99  ?  276 LEU B N   1 
ATOM   5602 C  CA  . LEU B 1 276 ? 60.817 -80.126 31.137  1.00 53.28  ?  276 LEU B CA  1 
ATOM   5603 C  C   . LEU B 1 276 ? 60.605 -79.383 29.819  1.00 55.08  ?  276 LEU B C   1 
ATOM   5604 O  O   . LEU B 1 276 ? 59.870 -79.877 28.979  1.00 62.72  ?  276 LEU B O   1 
ATOM   5605 C  CB  . LEU B 1 276 ? 59.531 -80.175 31.966  1.00 52.04  ?  276 LEU B CB  1 
ATOM   5606 C  CG  . LEU B 1 276 ? 59.565 -81.047 33.230  1.00 50.53  ?  276 LEU B CG  1 
ATOM   5607 C  CD1 . LEU B 1 276 ? 58.303 -80.861 34.051  1.00 52.71  ?  276 LEU B CD1 1 
ATOM   5608 C  CD2 . LEU B 1 276 ? 59.754 -82.524 32.934  1.00 45.78  ?  276 LEU B CD2 1 
ATOM   5609 N  N   . LYS B 1 277 ? 61.205 -78.199 29.643  1.00 57.56  ?  277 LYS B N   1 
ATOM   5610 C  CA  . LYS B 1 277 ? 61.052 -77.433 28.413  1.00 65.25  ?  277 LYS B CA  1 
ATOM   5611 C  C   . LYS B 1 277 ? 62.236 -77.664 27.478  1.00 67.67  ?  277 LYS B C   1 
ATOM   5612 O  O   . LYS B 1 277 ? 62.065 -77.790 26.267  1.00 75.99  ?  277 LYS B O   1 
ATOM   5613 C  CB  . LYS B 1 277 ? 60.909 -75.932 28.677  1.00 74.59  ?  277 LYS B CB  1 
ATOM   5614 C  CG  . LYS B 1 277 ? 59.497 -75.375 28.594  1.00 79.93  ?  277 LYS B CG  1 
ATOM   5615 C  CD  . LYS B 1 277 ? 58.515 -75.982 29.582  1.00 81.11  ?  277 LYS B CD  1 
ATOM   5616 C  CE  . LYS B 1 277 ? 57.742 -77.126 29.025  1.00 83.70  ?  277 LYS B CE  1 
ATOM   5617 N  NZ  . LYS B 1 277 ? 57.001 -77.769 30.110  1.00 95.63  1  277 LYS B NZ  1 
ATOM   5618 N  N   . VAL B 1 278 ? 63.445 -77.668 28.032  1.00 63.75  ?  278 VAL B N   1 
ATOM   5619 C  CA  . VAL B 1 278 ? 64.598 -78.107 27.268  1.00 64.03  ?  278 VAL B CA  1 
ATOM   5620 C  C   . VAL B 1 278 ? 64.383 -79.589 26.995  1.00 60.38  ?  278 VAL B C   1 
ATOM   5621 O  O   . VAL B 1 278 ? 63.644 -80.232 27.736  1.00 60.83  ?  278 VAL B O   1 
ATOM   5622 C  CB  . VAL B 1 278 ? 65.919 -77.834 28.016  1.00 69.84  ?  278 VAL B CB  1 
ATOM   5623 C  CG1 . VAL B 1 278 ? 66.086 -76.354 28.342  1.00 68.05  ?  278 VAL B CG1 1 
ATOM   5624 C  CG2 . VAL B 1 278 ? 66.051 -78.664 29.292  1.00 76.00  ?  278 VAL B CG2 1 
ATOM   5625 N  N   . ASP B 1 279 ? 65.017 -80.115 25.942  1.00 64.82  ?  279 ASP B N   1 
ATOM   5626 C  CA  . ASP B 1 279 ? 64.891 -81.521 25.568  1.00 75.36  ?  279 ASP B CA  1 
ATOM   5627 C  C   . ASP B 1 279 ? 63.410 -81.922 25.511  1.00 77.98  ?  279 ASP B C   1 
ATOM   5628 O  O   . ASP B 1 279 ? 63.020 -82.940 26.088  1.00 68.54  ?  279 ASP B O   1 
ATOM   5629 C  CB  . ASP B 1 279 ? 65.768 -82.432 26.431  1.00 76.10  ?  279 ASP B CB  1 
ATOM   5630 C  CG  . ASP B 1 279 ? 65.598 -82.396 27.953  1.00 78.35  ?  279 ASP B CG  1 
ATOM   5631 O  OD1 . ASP B 1 279 ? 64.439 -82.395 28.441  1.00 78.35  ?  279 ASP B OD1 1 
ATOM   5632 O  OD2 . ASP B 1 279 ? 66.632 -82.427 28.662  1.00 70.60  -1 279 ASP B OD2 1 
ATOM   5633 N  N   . ARG B 1 280 ? 62.602 -81.122 24.789  1.00 75.14  ?  280 ARG B N   1 
ATOM   5634 C  CA  . ARG B 1 280 ? 61.146 -81.242 24.743  1.00 72.74  ?  280 ARG B CA  1 
ATOM   5635 C  C   . ARG B 1 280 ? 60.613 -81.491 26.160  1.00 75.34  ?  280 ARG B C   1 
ATOM   5636 O  O   . ARG B 1 280 ? 61.026 -80.788 27.079  1.00 81.96  ?  280 ARG B O   1 
ATOM   5637 C  CB  . ARG B 1 280 ? 60.727 -82.272 23.685  1.00 81.68  ?  280 ARG B CB  1 
ATOM   5638 C  CG  . ARG B 1 280 ? 59.377 -82.046 23.010  1.00 86.78  ?  280 ARG B CG  1 
ATOM   5639 C  CD  . ARG B 1 280 ? 58.278 -81.380 23.847  1.00 85.96  ?  280 ARG B CD  1 
ATOM   5640 N  NE  . ARG B 1 280 ? 57.023 -81.350 23.087  1.00 89.29  ?  280 ARG B NE  1 
ATOM   5641 C  CZ  . ARG B 1 280 ? 55.849 -80.896 23.512  1.00 87.29  ?  280 ARG B CZ  1 
ATOM   5642 N  NH1 . ARG B 1 280 ? 54.776 -81.044 22.749  1.00 88.49  1  280 ARG B NH1 1 
ATOM   5643 N  NH2 . ARG B 1 280 ? 55.741 -80.326 24.698  1.00 82.60  ?  280 ARG B NH2 1 
ATOM   5644 N  N   . LYS B 1 281 ? 59.725 -82.493 26.335  1.00 67.14  ?  281 LYS B N   1 
ATOM   5645 C  CA  . LYS B 1 281 ? 59.054 -82.806 27.594  1.00 61.22  ?  281 LYS B CA  1 
ATOM   5646 C  C   . LYS B 1 281 ? 57.929 -81.796 27.850  1.00 54.27  ?  281 LYS B C   1 
ATOM   5647 O  O   . LYS B 1 281 ? 57.777 -80.839 27.102  1.00 48.88  ?  281 LYS B O   1 
ATOM   5648 C  CB  . LYS B 1 281 ? 60.005 -82.967 28.793  1.00 70.71  ?  281 LYS B CB  1 
ATOM   5649 C  CG  . LYS B 1 281 ? 60.988 -84.145 28.793  1.00 74.01  ?  281 LYS B CG  1 
ATOM   5650 C  CD  . LYS B 1 281 ? 61.924 -84.122 30.005  1.00 79.39  ?  281 LYS B CD  1 
ATOM   5651 C  CE  . LYS B 1 281 ? 63.016 -85.164 30.029  1.00 76.32  ?  281 LYS B CE  1 
ATOM   5652 N  NZ  . LYS B 1 281 ? 62.507 -86.535 30.152  1.00 70.90  1  281 LYS B NZ  1 
ATOM   5653 N  N   . GLN B 1 282 ? 57.136 -82.035 28.907  1.00 53.65  ?  282 GLN B N   1 
ATOM   5654 C  CA  . GLN B 1 282 ? 55.864 -81.367 29.136  1.00 56.03  ?  282 GLN B CA  1 
ATOM   5655 C  C   . GLN B 1 282 ? 55.645 -81.083 30.625  1.00 62.56  ?  282 GLN B C   1 
ATOM   5656 O  O   . GLN B 1 282 ? 56.208 -81.744 31.484  1.00 68.76  ?  282 GLN B O   1 
ATOM   5657 C  CB  . GLN B 1 282 ? 54.714 -82.228 28.613  1.00 56.08  ?  282 GLN B CB  1 
ATOM   5658 C  CG  . GLN B 1 282 ? 54.586 -82.213 27.093  1.00 57.75  ?  282 GLN B CG  1 
ATOM   5659 C  CD  . GLN B 1 282 ? 53.161 -82.126 26.580  1.00 61.31  ?  282 GLN B CD  1 
ATOM   5660 O  OE1 . GLN B 1 282 ? 52.201 -81.870 27.318  1.00 58.78  ?  282 GLN B OE1 1 
ATOM   5661 N  NE2 . GLN B 1 282 ? 53.016 -82.320 25.278  1.00 64.83  ?  282 GLN B NE2 1 
ATOM   5662 N  N   . ILE B 1 283 ? 54.802 -80.095 30.938  1.00 61.58  ?  283 ILE B N   1 
ATOM   5663 C  CA  . ILE B 1 283 ? 54.571 -79.719 32.319  1.00 60.10  ?  283 ILE B CA  1 
ATOM   5664 C  C   . ILE B 1 283 ? 54.012 -80.935 33.060  1.00 60.23  ?  283 ILE B C   1 
ATOM   5665 O  O   . ILE B 1 283 ? 54.353 -81.173 34.218  1.00 67.17  ?  283 ILE B O   1 
ATOM   5666 C  CB  . ILE B 1 283 ? 53.664 -78.473 32.385  1.00 63.41  ?  283 ILE B CB  1 
ATOM   5667 C  CG1 . ILE B 1 283 ? 53.889 -77.656 33.659  1.00 66.63  ?  283 ILE B CG1 1 
ATOM   5668 C  CG2 . ILE B 1 283 ? 52.193 -78.841 32.183  1.00 61.86  ?  283 ILE B CG2 1 
ATOM   5669 C  CD1 . ILE B 1 283 ? 52.947 -76.471 33.824  1.00 70.96  ?  283 ILE B CD1 1 
ATOM   5670 N  N   . ALA B 1 284 ? 53.200 -81.735 32.359  1.00 59.03  ?  284 ALA B N   1 
ATOM   5671 C  CA  . ALA B 1 284 ? 52.525 -82.898 32.925  1.00 63.44  ?  284 ALA B CA  1 
ATOM   5672 C  C   . ALA B 1 284 ? 53.506 -83.834 33.632  1.00 70.39  ?  284 ALA B C   1 
ATOM   5673 O  O   . ALA B 1 284 ? 53.310 -84.171 34.799  1.00 69.05  ?  284 ALA B O   1 
ATOM   5674 C  CB  . ALA B 1 284 ? 51.770 -83.632 31.832  1.00 60.14  ?  284 ALA B CB  1 
ATOM   5675 N  N   . GLU B 1 285 ? 54.551 -84.244 32.897  1.00 79.48  ?  285 GLU B N   1 
ATOM   5676 C  CA  . GLU B 1 285 ? 55.653 -85.067 33.393  1.00 75.37  ?  285 GLU B CA  1 
ATOM   5677 C  C   . GLU B 1 285 ? 55.938 -84.809 34.875  1.00 75.75  ?  285 GLU B C   1 
ATOM   5678 O  O   . GLU B 1 285 ? 56.105 -85.771 35.618  1.00 74.49  ?  285 GLU B O   1 
ATOM   5679 C  CB  . GLU B 1 285 ? 56.984 -84.823 32.672  1.00 70.50  ?  285 GLU B CB  1 
ATOM   5680 C  CG  . GLU B 1 285 ? 56.887 -84.680 31.153  1.00 72.11  ?  285 GLU B CG  1 
ATOM   5681 C  CD  . GLU B 1 285 ? 56.699 -85.954 30.360  1.00 70.25  ?  285 GLU B CD  1 
ATOM   5682 O  OE1 . GLU B 1 285 ? 57.118 -86.999 30.892  1.00 66.88  ?  285 GLU B OE1 1 
ATOM   5683 O  OE2 . GLU B 1 285 ? 56.139 -85.909 29.239  1.00 67.74  -1 285 GLU B OE2 1 
ATOM   5684 N  N   . LEU B 1 286 ? 56.019 -83.526 35.281  1.00 78.84  ?  286 LEU B N   1 
ATOM   5685 C  CA  . LEU B 1 286 ? 56.390 -83.134 36.638  1.00 82.61  ?  286 LEU B CA  1 
ATOM   5686 C  C   . LEU B 1 286 ? 55.543 -83.905 37.655  1.00 88.42  ?  286 LEU B C   1 
ATOM   5687 O  O   . LEU B 1 286 ? 56.076 -84.480 38.604  1.00 83.85  ?  286 LEU B O   1 
ATOM   5688 C  CB  . LEU B 1 286 ? 56.244 -81.621 36.834  1.00 86.64  ?  286 LEU B CB  1 
ATOM   5689 C  CG  . LEU B 1 286 ? 56.719 -81.048 38.178  1.00 91.02  ?  286 LEU B CG  1 
ATOM   5690 C  CD1 . LEU B 1 286 ? 58.235 -80.940 38.213  1.00 91.27  ?  286 LEU B CD1 1 
ATOM   5691 C  CD2 . LEU B 1 286 ? 56.094 -79.687 38.481  1.00 94.04  ?  286 LEU B CD2 1 
ATOM   5692 N  N   . VAL B 1 287 ? 54.216 -83.897 37.458  1.00 94.83  ?  287 VAL B N   1 
ATOM   5693 C  CA  . VAL B 1 287 ? 53.292 -84.588 38.348  1.00 92.92  ?  287 VAL B CA  1 
ATOM   5694 C  C   . VAL B 1 287 ? 53.337 -86.074 38.016  1.00 97.17  ?  287 VAL B C   1 
ATOM   5695 O  O   . VAL B 1 287 ? 53.649 -86.434 36.885  1.00 100.65 ?  287 VAL B O   1 
ATOM   5696 C  CB  . VAL B 1 287 ? 51.843 -84.062 38.286  1.00 86.19  ?  287 VAL B CB  1 
ATOM   5697 C  CG1 . VAL B 1 287 ? 51.723 -82.681 38.906  1.00 91.21  ?  287 VAL B CG1 1 
ATOM   5698 C  CG2 . VAL B 1 287 ? 51.280 -84.047 36.871  1.00 84.80  ?  287 VAL B CG2 1 
ATOM   5699 N  N   . THR B 1 288 ? 52.987 -86.901 39.011  1.00 101.92 ?  288 THR B N   1 
ATOM   5700 C  CA  . THR B 1 288 ? 53.074 -88.356 38.953  1.00 111.46 ?  288 THR B CA  1 
ATOM   5701 C  C   . THR B 1 288 ? 54.427 -88.824 39.503  1.00 120.43 ?  288 THR B C   1 
ATOM   5702 O  O   . THR B 1 288 ? 54.710 -90.020 39.456  1.00 136.40 ?  288 THR B O   1 
ATOM   5703 C  CB  . THR B 1 288 ? 52.800 -88.908 37.544  1.00 115.00 ?  288 THR B CB  1 
ATOM   5704 O  OG1 . THR B 1 288 ? 52.248 -90.207 37.734  1.00 119.78 ?  288 THR B OG1 1 
ATOM   5705 C  CG2 . THR B 1 288 ? 54.024 -89.057 36.651  1.00 110.98 ?  288 THR B CG2 1 
ATOM   5706 N  N   . ASP B 1 289 ? 55.243 -87.907 40.058  1.00 110.19 ?  289 ASP B N   1 
ATOM   5707 C  CA  . ASP B 1 289 ? 56.639 -88.202 40.367  1.00 94.21  ?  289 ASP B CA  1 
ATOM   5708 C  C   . ASP B 1 289 ? 56.932 -87.860 41.833  1.00 90.71  ?  289 ASP B C   1 
ATOM   5709 O  O   . ASP B 1 289 ? 56.173 -88.264 42.711  1.00 88.06  ?  289 ASP B O   1 
ATOM   5710 C  CB  . ASP B 1 289 ? 57.542 -87.620 39.286  1.00 84.16  ?  289 ASP B CB  1 
ATOM   5711 C  CG  . ASP B 1 289 ? 57.325 -88.182 37.882  1.00 83.27  ?  289 ASP B CG  1 
ATOM   5712 O  OD1 . ASP B 1 289 ? 56.843 -89.325 37.766  1.00 72.74  ?  289 ASP B OD1 1 
ATOM   5713 O  OD2 . ASP B 1 289 ? 57.620 -87.472 36.899  1.00 85.19  -1 289 ASP B OD2 1 
ATOM   5714 N  N   . ALA B 1 290 ? 58.035 -87.144 42.106  1.00 88.52  ?  290 ALA B N   1 
ATOM   5715 C  CA  . ALA B 1 290 ? 58.562 -86.990 43.460  1.00 84.28  ?  290 ALA B CA  1 
ATOM   5716 C  C   . ALA B 1 290 ? 57.615 -86.168 44.335  1.00 89.83  ?  290 ALA B C   1 
ATOM   5717 O  O   . ALA B 1 290 ? 57.873 -84.996 44.600  1.00 94.69  ?  290 ALA B O   1 
ATOM   5718 C  CB  . ALA B 1 290 ? 59.952 -86.368 43.427  1.00 73.35  ?  290 ALA B CB  1 
ATOM   5719 N  N   . ALA B 1 291 ? 56.529 -86.808 44.793  1.00 94.71  ?  291 ALA B N   1 
ATOM   5720 C  CA  . ALA B 1 291 ? 55.565 -86.225 45.721  1.00 97.58  ?  291 ALA B CA  1 
ATOM   5721 C  C   . ALA B 1 291 ? 54.734 -85.117 45.069  1.00 94.54  ?  291 ALA B C   1 
ATOM   5722 O  O   . ALA B 1 291 ? 53.840 -84.562 45.714  1.00 92.60  ?  291 ALA B O   1 
ATOM   5723 C  CB  . ALA B 1 291 ? 56.261 -85.729 46.979  1.00 94.63  ?  291 ALA B CB  1 
ATOM   5724 N  N   . PHE B 1 292 ? 55.022 -84.804 43.795  1.00 94.27  ?  292 PHE B N   1 
ATOM   5725 C  CA  . PHE B 1 292 ? 54.318 -83.755 43.067  1.00 98.47  ?  292 PHE B CA  1 
ATOM   5726 C  C   . PHE B 1 292 ? 52.872 -84.189 42.807  1.00 92.82  ?  292 PHE B C   1 
ATOM   5727 O  O   . PHE B 1 292 ? 52.009 -83.346 42.556  1.00 89.10  ?  292 PHE B O   1 
ATOM   5728 C  CB  . PHE B 1 292 ? 55.024 -83.395 41.752  1.00 103.82 ?  292 PHE B CB  1 
ATOM   5729 C  CG  . PHE B 1 292 ? 56.532 -83.164 41.823  1.00 106.56 ?  292 PHE B CG  1 
ATOM   5730 C  CD1 . PHE B 1 292 ? 57.417 -83.998 41.145  1.00 108.64 ?  292 PHE B CD1 1 
ATOM   5731 C  CD2 . PHE B 1 292 ? 57.067 -82.124 42.579  1.00 108.99 ?  292 PHE B CD2 1 
ATOM   5732 C  CE1 . PHE B 1 292 ? 58.787 -83.786 41.208  1.00 107.49 ?  292 PHE B CE1 1 
ATOM   5733 C  CE2 . PHE B 1 292 ? 58.440 -81.924 42.649  1.00 102.74 ?  292 PHE B CE2 1 
ATOM   5734 C  CZ  . PHE B 1 292 ? 59.296 -82.754 41.964  1.00 104.35 ?  292 PHE B CZ  1 
ATOM   5735 N  N   . ALA B 1 293 ? 52.628 -85.507 42.866  1.00 84.37  ?  293 ALA B N   1 
ATOM   5736 C  CA  . ALA B 1 293 ? 51.303 -86.090 42.720  1.00 76.61  ?  293 ALA B CA  1 
ATOM   5737 C  C   . ALA B 1 293 ? 50.303 -85.418 43.658  1.00 76.90  ?  293 ALA B C   1 
ATOM   5738 O  O   . ALA B 1 293 ? 49.205 -85.072 43.225  1.00 79.09  ?  293 ALA B O   1 
ATOM   5739 C  CB  . ALA B 1 293 ? 51.381 -87.576 42.981  1.00 80.10  ?  293 ALA B CB  1 
ATOM   5740 N  N   . ASP B 1 294 ? 50.686 -85.244 44.935  1.00 75.93  ?  294 ASP B N   1 
ATOM   5741 C  CA  . ASP B 1 294 ? 49.793 -84.697 45.950  1.00 68.85  ?  294 ASP B CA  1 
ATOM   5742 C  C   . ASP B 1 294 ? 49.637 -83.189 45.770  1.00 66.52  ?  294 ASP B C   1 
ATOM   5743 O  O   . ASP B 1 294 ? 48.523 -82.679 45.811  1.00 63.08  ?  294 ASP B O   1 
ATOM   5744 C  CB  . ASP B 1 294 ? 50.264 -84.977 47.371  1.00 66.21  ?  294 ASP B CB  1 
ATOM   5745 C  CG  . ASP B 1 294 ? 49.544 -84.165 48.446  1.00 62.38  ?  294 ASP B CG  1 
ATOM   5746 O  OD1 . ASP B 1 294 ? 48.420 -83.702 48.159  1.00 53.24  ?  294 ASP B OD1 1 
ATOM   5747 O  OD2 . ASP B 1 294 ? 50.120 -83.965 49.550  1.00 53.15  -1 294 ASP B OD2 1 
ATOM   5748 N  N   . LYS B 1 295 ? 50.760 -82.482 45.592  1.00 66.74  ?  295 LYS B N   1 
ATOM   5749 C  CA  . LYS B 1 295 ? 50.774 -81.028 45.637  1.00 62.51  ?  295 LYS B CA  1 
ATOM   5750 C  C   . LYS B 1 295 ? 49.843 -80.441 44.577  1.00 61.03  ?  295 LYS B C   1 
ATOM   5751 O  O   . LYS B 1 295 ? 49.062 -79.543 44.880  1.00 52.38  ?  295 LYS B O   1 
ATOM   5752 C  CB  . LYS B 1 295 ? 52.211 -80.505 45.521  1.00 63.35  ?  295 LYS B CB  1 
ATOM   5753 C  CG  . LYS B 1 295 ? 52.311 -78.983 45.550  1.00 67.38  ?  295 LYS B CG  1 
ATOM   5754 C  CD  . LYS B 1 295 ? 53.649 -78.399 45.988  1.00 66.82  ?  295 LYS B CD  1 
ATOM   5755 C  CE  . LYS B 1 295 ? 53.614 -76.905 45.916  1.00 67.85  ?  295 LYS B CE  1 
ATOM   5756 N  NZ  . LYS B 1 295 ? 54.839 -76.283 46.416  1.00 71.79  1  295 LYS B NZ  1 
ATOM   5757 N  N   . PHE B 1 296 ? 49.911 -80.995 43.354  1.00 72.11  ?  296 PHE B N   1 
ATOM   5758 C  CA  . PHE B 1 296 ? 49.409 -80.348 42.146  1.00 67.66  ?  296 PHE B CA  1 
ATOM   5759 C  C   . PHE B 1 296 ? 48.283 -81.138 41.481  1.00 63.84  ?  296 PHE B C   1 
ATOM   5760 O  O   . PHE B 1 296 ? 48.338 -82.368 41.409  1.00 58.07  ?  296 PHE B O   1 
ATOM   5761 C  CB  . PHE B 1 296 ? 50.533 -80.245 41.113  1.00 64.04  ?  296 PHE B CB  1 
ATOM   5762 C  CG  . PHE B 1 296 ? 51.740 -79.442 41.557  1.00 59.55  ?  296 PHE B CG  1 
ATOM   5763 C  CD1 . PHE B 1 296 ? 51.722 -78.059 41.501  1.00 53.58  ?  296 PHE B CD1 1 
ATOM   5764 C  CD2 . PHE B 1 296 ? 52.887 -80.076 42.013  1.00 60.34  ?  296 PHE B CD2 1 
ATOM   5765 C  CE1 . PHE B 1 296 ? 52.822 -77.329 41.895  1.00 53.95  ?  296 PHE B CE1 1 
ATOM   5766 C  CE2 . PHE B 1 296 ? 53.984 -79.335 42.406  1.00 58.95  ?  296 PHE B CE2 1 
ATOM   5767 C  CZ  . PHE B 1 296 ? 53.944 -77.966 42.349  1.00 57.35  ?  296 PHE B CZ  1 
ATOM   5768 N  N   . THR B 1 297 ? 47.309 -80.383 40.946  1.00 61.75  ?  297 THR B N   1 
ATOM   5769 C  CA  . THR B 1 297 ? 46.223 -80.887 40.118  1.00 65.74  ?  297 THR B CA  1 
ATOM   5770 C  C   . THR B 1 297 ? 46.485 -80.495 38.666  1.00 70.87  ?  297 THR B C   1 
ATOM   5771 O  O   . THR B 1 297 ? 46.650 -79.309 38.379  1.00 80.22  ?  297 THR B O   1 
ATOM   5772 C  CB  . THR B 1 297 ? 44.895 -80.296 40.589  1.00 59.00  ?  297 THR B CB  1 
ATOM   5773 O  OG1 . THR B 1 297 ? 44.799 -80.668 41.959  1.00 66.01  ?  297 THR B OG1 1 
ATOM   5774 C  CG2 . THR B 1 297 ? 43.696 -80.838 39.835  1.00 53.97  ?  297 THR B CG2 1 
ATOM   5775 N  N   . TYR B 1 298 ? 46.480 -81.496 37.769  1.00 66.67  ?  298 TYR B N   1 
ATOM   5776 C  CA  . TYR B 1 298 ? 46.619 -81.284 36.335  1.00 52.94  ?  298 TYR B CA  1 
ATOM   5777 C  C   . TYR B 1 298 ? 45.249 -81.399 35.670  1.00 50.23  ?  298 TYR B C   1 
ATOM   5778 O  O   . TYR B 1 298 ? 44.499 -82.339 35.921  1.00 51.12  ?  298 TYR B O   1 
ATOM   5779 C  CB  . TYR B 1 298 ? 47.589 -82.297 35.725  1.00 46.10  ?  298 TYR B CB  1 
ATOM   5780 C  CG  . TYR B 1 298 ? 47.903 -82.036 34.261  1.00 44.55  ?  298 TYR B CG  1 
ATOM   5781 C  CD1 . TYR B 1 298 ? 47.551 -82.945 33.270  1.00 42.17  ?  298 TYR B CD1 1 
ATOM   5782 C  CD2 . TYR B 1 298 ? 48.532 -80.864 33.867  1.00 40.52  ?  298 TYR B CD2 1 
ATOM   5783 C  CE1 . TYR B 1 298 ? 47.843 -82.705 31.938  1.00 38.45  ?  298 TYR B CE1 1 
ATOM   5784 C  CE2 . TYR B 1 298 ? 48.810 -80.608 32.536  1.00 37.38  ?  298 TYR B CE2 1 
ATOM   5785 C  CZ  . TYR B 1 298 ? 48.472 -81.532 31.571  1.00 35.79  ?  298 TYR B CZ  1 
ATOM   5786 O  OH  . TYR B 1 298 ? 48.760 -81.277 30.264  1.00 38.51  ?  298 TYR B OH  1 
ATOM   5787 N  N   . LEU B 1 299 ? 44.945 -80.425 34.814  1.00 45.43  ?  299 LEU B N   1 
ATOM   5788 C  CA  . LEU B 1 299 ? 43.732 -80.424 34.019  1.00 45.56  ?  299 LEU B CA  1 
ATOM   5789 C  C   . LEU B 1 299 ? 44.137 -80.265 32.553  1.00 38.24  ?  299 LEU B C   1 
ATOM   5790 O  O   . LEU B 1 299 ? 44.376 -79.170 32.059  1.00 37.47  ?  299 LEU B O   1 
ATOM   5791 C  CB  . LEU B 1 299 ? 42.756 -79.344 34.501  1.00 50.39  ?  299 LEU B CB  1 
ATOM   5792 C  CG  . LEU B 1 299 ? 43.252 -78.412 35.612  1.00 55.75  ?  299 LEU B CG  1 
ATOM   5793 C  CD1 . LEU B 1 299 ? 42.796 -76.971 35.461  1.00 59.06  ?  299 LEU B CD1 1 
ATOM   5794 C  CD2 . LEU B 1 299 ? 42.784 -78.940 36.943  1.00 53.94  ?  299 LEU B CD2 1 
ATOM   5795 N  N   . PRO B 1 300 ? 44.249 -81.364 31.790  1.00 36.20  ?  300 PRO B N   1 
ATOM   5796 C  CA  . PRO B 1 300 ? 44.659 -81.262 30.390  1.00 37.52  ?  300 PRO B CA  1 
ATOM   5797 C  C   . PRO B 1 300 ? 43.585 -80.505 29.611  1.00 36.50  ?  300 PRO B C   1 
ATOM   5798 O  O   . PRO B 1 300 ? 42.428 -80.481 30.034  1.00 36.71  ?  300 PRO B O   1 
ATOM   5799 C  CB  . PRO B 1 300 ? 44.804 -82.740 29.964  1.00 34.58  ?  300 PRO B CB  1 
ATOM   5800 C  CG  . PRO B 1 300 ? 43.835 -83.475 30.865  1.00 33.51  ?  300 PRO B CG  1 
ATOM   5801 C  CD  . PRO B 1 300 ? 43.931 -82.742 32.196  1.00 35.51  ?  300 PRO B CD  1 
ATOM   5802 N  N   . GLY B 1 301 ? 43.984 -79.863 28.507  1.00 34.33  ?  301 GLY B N   1 
ATOM   5803 C  CA  . GLY B 1 301 ? 43.042 -79.218 27.599  1.00 34.90  ?  301 GLY B CA  1 
ATOM   5804 C  C   . GLY B 1 301 ? 42.544 -77.835 28.036  1.00 32.55  ?  301 GLY B C   1 
ATOM   5805 O  O   . GLY B 1 301 ? 41.918 -77.166 27.225  1.00 35.88  ?  301 GLY B O   1 
ATOM   5806 N  N   . GLN B 1 302 ? 42.829 -77.401 29.275  1.00 30.91  ?  302 GLN B N   1 
ATOM   5807 C  CA  . GLN B 1 302 ? 42.188 -76.242 29.895  1.00 35.19  ?  302 GLN B CA  1 
ATOM   5808 C  C   . GLN B 1 302 ? 43.211 -75.134 30.204  1.00 40.56  ?  302 GLN B C   1 
ATOM   5809 O  O   . GLN B 1 302 ? 44.423 -75.357 30.123  1.00 43.27  ?  302 GLN B O   1 
ATOM   5810 C  CB  . GLN B 1 302 ? 41.451 -76.703 31.162  1.00 33.52  ?  302 GLN B CB  1 
ATOM   5811 C  CG  . GLN B 1 302 ? 40.070 -77.311 30.917  1.00 34.38  ?  302 GLN B CG  1 
ATOM   5812 C  CD  . GLN B 1 302 ? 38.984 -76.285 30.634  1.00 35.23  ?  302 GLN B CD  1 
ATOM   5813 O  OE1 . GLN B 1 302 ? 38.568 -75.527 31.515  1.00 31.64  ?  302 GLN B OE1 1 
ATOM   5814 N  NE2 . GLN B 1 302 ? 38.489 -76.242 29.403  1.00 36.02  ?  302 GLN B NE2 1 
ATOM   5815 N  N   . ARG B 1 303 ? 42.721 -73.941 30.602  1.00 39.61  ?  303 ARG B N   1 
ATOM   5816 C  CA  . ARG B 1 303 ? 43.584 -72.833 31.012  1.00 38.78  ?  303 ARG B CA  1 
ATOM   5817 C  C   . ARG B 1 303 ? 43.226 -72.363 32.424  1.00 41.08  ?  303 ARG B C   1 
ATOM   5818 O  O   . ARG B 1 303 ? 42.042 -72.306 32.764  1.00 45.26  ?  303 ARG B O   1 
ATOM   5819 C  CB  . ARG B 1 303 ? 43.509 -71.656 30.031  1.00 33.19  ?  303 ARG B CB  1 
ATOM   5820 C  CG  . ARG B 1 303 ? 43.953 -72.049 28.631  1.00 31.02  ?  303 ARG B CG  1 
ATOM   5821 C  CD  . ARG B 1 303 ? 44.065 -70.818 27.788  1.00 31.76  ?  303 ARG B CD  1 
ATOM   5822 N  NE  . ARG B 1 303 ? 42.806 -70.064 27.777  1.00 31.47  ?  303 ARG B NE  1 
ATOM   5823 C  CZ  . ARG B 1 303 ? 41.973 -69.971 26.747  1.00 30.08  ?  303 ARG B CZ  1 
ATOM   5824 N  NH1 . ARG B 1 303 ? 42.189 -70.645 25.618  1.00 29.48  1  303 ARG B NH1 1 
ATOM   5825 N  NH2 . ARG B 1 303 ? 40.922 -69.187 26.869  1.00 28.56  ?  303 ARG B NH2 1 
ATOM   5826 N  N   . PRO B 1 304 ? 44.220 -71.919 33.244  1.00 37.75  ?  304 PRO B N   1 
ATOM   5827 C  CA  . PRO B 1 304 ? 44.030 -71.779 34.696  1.00 35.33  ?  304 PRO B CA  1 
ATOM   5828 C  C   . PRO B 1 304 ? 43.023 -70.750 35.206  1.00 35.74  ?  304 PRO B C   1 
ATOM   5829 O  O   . PRO B 1 304 ? 42.689 -70.747 36.389  1.00 33.33  ?  304 PRO B O   1 
ATOM   5830 C  CB  . PRO B 1 304 ? 45.443 -71.423 35.183  1.00 32.42  ?  304 PRO B CB  1 
ATOM   5831 C  CG  . PRO B 1 304 ? 46.063 -70.729 33.999  1.00 33.70  ?  304 PRO B CG  1 
ATOM   5832 C  CD  . PRO B 1 304 ? 45.562 -71.494 32.802  1.00 34.23  ?  304 PRO B CD  1 
ATOM   5833 N  N   . TRP B 1 305 ? 42.534 -69.883 34.317  1.00 37.17  ?  305 TRP B N   1 
ATOM   5834 C  CA  . TRP B 1 305 ? 41.877 -68.664 34.760  1.00 40.65  ?  305 TRP B CA  1 
ATOM   5835 C  C   . TRP B 1 305 ? 40.728 -68.974 35.720  1.00 40.17  ?  305 TRP B C   1 
ATOM   5836 O  O   . TRP B 1 305 ? 40.606 -68.298 36.740  1.00 34.10  ?  305 TRP B O   1 
ATOM   5837 C  CB  . TRP B 1 305 ? 41.493 -67.800 33.546  1.00 41.97  ?  305 TRP B CB  1 
ATOM   5838 C  CG  . TRP B 1 305 ? 42.699 -67.534 32.679  1.00 41.90  ?  305 TRP B CG  1 
ATOM   5839 C  CD1 . TRP B 1 305 ? 42.790 -67.640 31.321  1.00 43.58  ?  305 TRP B CD1 1 
ATOM   5840 C  CD2 . TRP B 1 305 ? 44.030 -67.204 33.146  1.00 42.08  ?  305 TRP B CD2 1 
ATOM   5841 N  NE1 . TRP B 1 305 ? 44.071 -67.381 30.907  1.00 45.29  ?  305 TRP B NE1 1 
ATOM   5842 C  CE2 . TRP B 1 305 ? 44.854 -67.113 32.002  1.00 43.48  ?  305 TRP B CE2 1 
ATOM   5843 C  CE3 . TRP B 1 305 ? 44.600 -66.961 34.404  1.00 39.34  ?  305 TRP B CE3 1 
ATOM   5844 C  CZ2 . TRP B 1 305 ? 46.210 -66.800 32.090  1.00 40.37  ?  305 TRP B CZ2 1 
ATOM   5845 C  CZ3 . TRP B 1 305 ? 45.941 -66.660 34.487  1.00 38.06  ?  305 TRP B CZ3 1 
ATOM   5846 C  CH2 . TRP B 1 305 ? 46.738 -66.606 33.347  1.00 38.31  ?  305 TRP B CH2 1 
ATOM   5847 N  N   . VAL B 1 306 ? 39.993 -70.067 35.460  1.00 45.87  ?  306 VAL B N   1 
ATOM   5848 C  CA  . VAL B 1 306 ? 38.866 -70.490 36.288  1.00 50.56  ?  306 VAL B CA  1 
ATOM   5849 C  C   . VAL B 1 306 ? 39.285 -71.503 37.367  1.00 47.54  ?  306 VAL B C   1 
ATOM   5850 O  O   . VAL B 1 306 ? 38.568 -71.689 38.346  1.00 49.61  ?  306 VAL B O   1 
ATOM   5851 C  CB  . VAL B 1 306 ? 37.763 -71.106 35.404  1.00 57.49  ?  306 VAL B CB  1 
ATOM   5852 C  CG1 . VAL B 1 306 ? 36.451 -71.217 36.169  1.00 62.44  ?  306 VAL B CG1 1 
ATOM   5853 C  CG2 . VAL B 1 306 ? 37.543 -70.345 34.097  1.00 59.32  ?  306 VAL B CG2 1 
ATOM   5854 N  N   . HIS B 1 307 ? 40.415 -72.197 37.178  1.00 39.47  ?  307 HIS B N   1 
ATOM   5855 C  CA  . HIS B 1 307 ? 40.710 -73.382 37.957  1.00 38.22  ?  307 HIS B CA  1 
ATOM   5856 C  C   . HIS B 1 307 ? 41.706 -73.074 39.070  1.00 46.40  ?  307 HIS B C   1 
ATOM   5857 O  O   . HIS B 1 307 ? 42.455 -73.964 39.493  1.00 45.64  ?  307 HIS B O   1 
ATOM   5858 C  CB  . HIS B 1 307 ? 41.258 -74.471 37.040  1.00 35.66  ?  307 HIS B CB  1 
ATOM   5859 C  CG  . HIS B 1 307 ? 40.337 -74.841 35.936  1.00 35.50  ?  307 HIS B CG  1 
ATOM   5860 N  ND1 . HIS B 1 307 ? 39.475 -75.913 35.998  1.00 35.51  ?  307 HIS B ND1 1 
ATOM   5861 C  CD2 . HIS B 1 307 ? 40.177 -74.304 34.723  1.00 34.50  ?  307 HIS B CD2 1 
ATOM   5862 C  CE1 . HIS B 1 307 ? 38.805 -75.991 34.860  1.00 35.04  ?  307 HIS B CE1 1 
ATOM   5863 N  NE2 . HIS B 1 307 ? 39.222 -75.025 34.071  1.00 33.83  ?  307 HIS B NE2 1 
ATOM   5864 N  N   . VAL B 1 308 ? 41.693 -71.817 39.547  1.00 47.47  ?  308 VAL B N   1 
ATOM   5865 C  CA  . VAL B 1 308 ? 42.712 -71.334 40.469  1.00 43.51  ?  308 VAL B CA  1 
ATOM   5866 C  C   . VAL B 1 308 ? 42.091 -71.003 41.832  1.00 46.78  ?  308 VAL B C   1 
ATOM   5867 O  O   . VAL B 1 308 ? 42.795 -70.985 42.852  1.00 40.73  ?  308 VAL B O   1 
ATOM   5868 C  CB  . VAL B 1 308 ? 43.509 -70.148 39.888  1.00 37.99  ?  308 VAL B CB  1 
ATOM   5869 C  CG1 . VAL B 1 308 ? 44.651 -70.630 39.013  1.00 41.21  ?  308 VAL B CG1 1 
ATOM   5870 C  CG2 . VAL B 1 308 ? 42.658 -69.138 39.137  1.00 36.37  ?  308 VAL B CG2 1 
ATOM   5871 N  N   . GLY B 1 309 ? 40.774 -70.754 41.840  1.00 46.78  ?  309 GLY B N   1 
ATOM   5872 C  CA  . GLY B 1 309 ? 40.063 -70.444 43.067  1.00 52.85  ?  309 GLY B CA  1 
ATOM   5873 C  C   . GLY B 1 309 ? 39.943 -68.936 43.246  1.00 63.49  ?  309 GLY B C   1 
ATOM   5874 O  O   . GLY B 1 309 ? 39.600 -68.226 42.294  1.00 68.40  ?  309 GLY B O   1 
ATOM   5875 N  N   . ALA B 1 310 ? 40.224 -68.458 44.468  1.00 61.07  ?  310 ALA B N   1 
ATOM   5876 C  CA  . ALA B 1 310 ? 40.251 -67.025 44.726  1.00 54.47  ?  310 ALA B CA  1 
ATOM   5877 C  C   . ALA B 1 310 ? 41.682 -66.501 44.559  1.00 50.25  ?  310 ALA B C   1 
ATOM   5878 O  O   . ALA B 1 310 ? 42.538 -66.793 45.390  1.00 50.00  ?  310 ALA B O   1 
ATOM   5879 C  CB  . ALA B 1 310 ? 39.691 -66.737 46.103  1.00 53.81  ?  310 ALA B CB  1 
ATOM   5880 N  N   . VAL B 1 311 ? 41.935 -65.718 43.494  1.00 43.62  ?  311 VAL B N   1 
ATOM   5881 C  CA  . VAL B 1 311 ? 43.261 -65.174 43.227  1.00 43.35  ?  311 VAL B CA  1 
ATOM   5882 C  C   . VAL B 1 311 ? 43.247 -63.643 43.300  1.00 42.38  ?  311 VAL B C   1 
ATOM   5883 O  O   . VAL B 1 311 ? 42.191 -63.018 43.326  1.00 42.99  ?  311 VAL B O   1 
ATOM   5884 C  CB  . VAL B 1 311 ? 43.815 -65.656 41.873  1.00 47.78  ?  311 VAL B CB  1 
ATOM   5885 C  CG1 . VAL B 1 311 ? 43.998 -67.168 41.850  1.00 53.59  ?  311 VAL B CG1 1 
ATOM   5886 C  CG2 . VAL B 1 311 ? 42.967 -65.200 40.688  1.00 45.64  ?  311 VAL B CG2 1 
ATOM   5887 N  N   . ASP B 1 312 ? 44.452 -63.056 43.325  1.00 37.59  ?  312 ASP B N   1 
ATOM   5888 C  CA  . ASP B 1 312 ? 44.638 -61.630 43.495  1.00 36.85  ?  312 ASP B CA  1 
ATOM   5889 C  C   . ASP B 1 312 ? 45.288 -61.032 42.254  1.00 37.31  ?  312 ASP B C   1 
ATOM   5890 O  O   . ASP B 1 312 ? 44.942 -59.917 41.859  1.00 39.48  ?  312 ASP B O   1 
ATOM   5891 C  CB  . ASP B 1 312 ? 45.470 -61.321 44.732  1.00 39.25  ?  312 ASP B CB  1 
ATOM   5892 C  CG  . ASP B 1 312 ? 44.862 -61.743 46.067  1.00 38.60  ?  312 ASP B CG  1 
ATOM   5893 O  OD1 . ASP B 1 312 ? 45.463 -62.611 46.732  1.00 33.86  ?  312 ASP B OD1 1 
ATOM   5894 O  OD2 . ASP B 1 312 ? 43.785 -61.202 46.427  1.00 38.65  -1 312 ASP B OD2 1 
ATOM   5895 N  N   . VAL B 1 313 ? 46.261 -61.738 41.667  1.00 34.96  ?  313 VAL B N   1 
ATOM   5896 C  CA  . VAL B 1 313 ? 46.974 -61.199 40.516  1.00 36.28  ?  313 VAL B CA  1 
ATOM   5897 C  C   . VAL B 1 313 ? 47.028 -62.263 39.418  1.00 36.11  ?  313 VAL B C   1 
ATOM   5898 O  O   . VAL B 1 313 ? 47.228 -63.447 39.693  1.00 39.58  ?  313 VAL B O   1 
ATOM   5899 C  CB  . VAL B 1 313 ? 48.392 -60.691 40.871  1.00 36.94  ?  313 VAL B CB  1 
ATOM   5900 C  CG1 . VAL B 1 313 ? 49.083 -60.020 39.690  1.00 36.33  ?  313 VAL B CG1 1 
ATOM   5901 C  CG2 . VAL B 1 313 ? 48.407 -59.737 42.062  1.00 36.42  ?  313 VAL B CG2 1 
ATOM   5902 N  N   . ALA B 1 314 ? 46.888 -61.813 38.167  1.00 32.07  ?  314 ALA B N   1 
ATOM   5903 C  CA  . ALA B 1 314 ? 46.840 -62.680 37.003  1.00 29.00  ?  314 ALA B CA  1 
ATOM   5904 C  C   . ALA B 1 314 ? 47.898 -62.253 35.986  1.00 29.94  ?  314 ALA B C   1 
ATOM   5905 O  O   . ALA B 1 314 ? 47.901 -61.093 35.555  1.00 29.51  ?  314 ALA B O   1 
ATOM   5906 C  CB  . ALA B 1 314 ? 45.466 -62.573 36.409  1.00 29.82  ?  314 ALA B CB  1 
ATOM   5907 N  N   . LEU B 1 315 ? 48.768 -63.190 35.571  1.00 27.47  ?  315 LEU B N   1 
ATOM   5908 C  CA  . LEU B 1 315 ? 49.860 -62.852 34.672  1.00 26.48  ?  315 LEU B CA  1 
ATOM   5909 C  C   . LEU B 1 315 ? 49.862 -63.822 33.486  1.00 27.29  ?  315 LEU B C   1 
ATOM   5910 O  O   . LEU B 1 315 ? 50.641 -64.776 33.428  1.00 26.35  ?  315 LEU B O   1 
ATOM   5911 C  CB  . LEU B 1 315 ? 51.172 -62.848 35.452  1.00 26.96  ?  315 LEU B CB  1 
ATOM   5912 C  CG  . LEU B 1 315 ? 51.182 -62.018 36.742  1.00 28.87  ?  315 LEU B CG  1 
ATOM   5913 C  CD1 . LEU B 1 315 ? 52.372 -62.302 37.643  1.00 28.81  ?  315 LEU B CD1 1 
ATOM   5914 C  CD2 . LEU B 1 315 ? 51.139 -60.537 36.428  1.00 30.57  ?  315 LEU B CD2 1 
ATOM   5915 N  N   . PRO B 1 316 ? 49.022 -63.576 32.454  1.00 25.66  ?  316 PRO B N   1 
ATOM   5916 C  CA  . PRO B 1 316 ? 48.995 -64.426 31.264  1.00 25.49  ?  316 PRO B CA  1 
ATOM   5917 C  C   . PRO B 1 316 ? 50.363 -64.350 30.608  1.00 24.61  ?  316 PRO B C   1 
ATOM   5918 O  O   . PRO B 1 316 ? 50.807 -63.261 30.266  1.00 26.21  ?  316 PRO B O   1 
ATOM   5919 C  CB  . PRO B 1 316 ? 47.904 -63.845 30.354  1.00 26.83  ?  316 PRO B CB  1 
ATOM   5920 C  CG  . PRO B 1 316 ? 47.208 -62.788 31.208  1.00 27.31  ?  316 PRO B CG  1 
ATOM   5921 C  CD  . PRO B 1 316 ? 48.132 -62.419 32.347  1.00 26.02  ?  316 PRO B CD  1 
ATOM   5922 N  N   . SER B 1 317 ? 51.046 -65.481 30.452  1.00 23.84  ?  317 SER B N   1 
ATOM   5923 C  CA  . SER B 1 317 ? 52.413 -65.404 29.973  1.00 24.86  ?  317 SER B CA  1 
ATOM   5924 C  C   . SER B 1 317 ? 52.700 -66.455 28.902  1.00 28.44  ?  317 SER B C   1 
ATOM   5925 O  O   . SER B 1 317 ? 53.875 -66.741 28.639  1.00 27.57  ?  317 SER B O   1 
ATOM   5926 C  CB  . SER B 1 317 ? 53.358 -65.446 31.135  1.00 23.30  ?  317 SER B CB  1 
ATOM   5927 O  OG  . SER B 1 317 ? 53.047 -64.365 32.008  1.00 22.49  ?  317 SER B OG  1 
ATOM   5928 N  N   . ALA B 1 318 ? 51.628 -66.879 28.193  1.00 29.30  ?  318 ALA B N   1 
ATOM   5929 C  CA  . ALA B 1 318 ? 51.661 -68.000 27.261  1.00 30.00  ?  318 ALA B CA  1 
ATOM   5930 C  C   . ALA B 1 318 ? 51.452 -67.572 25.801  1.00 28.65  ?  318 ALA B C   1 
ATOM   5931 O  O   . ALA B 1 318 ? 52.384 -67.609 25.015  1.00 27.86  ?  318 ALA B O   1 
ATOM   5932 C  CB  . ALA B 1 318 ? 50.635 -69.022 27.706  1.00 32.26  ?  318 ALA B CB  1 
ATOM   5933 N  N   . THR B 1 319 ? 50.224 -67.224 25.400  1.00 30.27  ?  319 THR B N   1 
ATOM   5934 C  CA  . THR B 1 319 ? 49.924 -66.950 23.998  1.00 31.13  ?  319 THR B CA  1 
ATOM   5935 C  C   . THR B 1 319 ? 49.121 -65.662 23.891  1.00 30.88  ?  319 THR B C   1 
ATOM   5936 O  O   . THR B 1 319 ? 48.791 -65.028 24.884  1.00 31.71  ?  319 THR B O   1 
ATOM   5937 C  CB  . THR B 1 319 ? 49.153 -68.077 23.281  1.00 33.78  ?  319 THR B CB  1 
ATOM   5938 O  OG1 . THR B 1 319 ? 47.903 -68.405 23.890  1.00 30.49  ?  319 THR B OG1 1 
ATOM   5939 C  CG2 . THR B 1 319 ? 49.949 -69.362 23.158  1.00 35.08  ?  319 THR B CG2 1 
ATOM   5940 N  N   . GLN B 1 320 ? 48.861 -65.290 22.638  1.00 35.03  ?  320 GLN B N   1 
ATOM   5941 C  CA  . GLN B 1 320 ? 47.882 -64.292 22.268  1.00 38.80  ?  320 GLN B CA  1 
ATOM   5942 C  C   . GLN B 1 320 ? 46.507 -64.772 22.714  1.00 37.21  ?  320 GLN B C   1 
ATOM   5943 O  O   . GLN B 1 320 ? 46.260 -65.975 22.801  1.00 36.94  ?  320 GLN B O   1 
ATOM   5944 C  CB  . GLN B 1 320 ? 47.842 -64.110 20.746  1.00 42.06  ?  320 GLN B CB  1 
ATOM   5945 C  CG  . GLN B 1 320 ? 49.098 -63.502 20.131  1.00 47.04  ?  320 GLN B CG  1 
ATOM   5946 C  CD  . GLN B 1 320 ? 48.846 -62.952 18.742  1.00 54.10  ?  320 GLN B CD  1 
ATOM   5947 O  OE1 . GLN B 1 320 ? 47.690 -62.866 18.307  1.00 54.40  ?  320 GLN B OE1 1 
ATOM   5948 N  NE2 . GLN B 1 320 ? 49.911 -62.558 18.045  1.00 50.62  ?  320 GLN B NE2 1 
ATOM   5949 N  N   . ASN B 1 321 ? 45.622 -63.808 22.982  1.00 35.17  ?  321 ASN B N   1 
ATOM   5950 C  CA  . ASN B 1 321 ? 44.200 -64.076 23.105  1.00 33.23  ?  321 ASN B CA  1 
ATOM   5951 C  C   . ASN B 1 321 ? 43.967 -65.280 24.017  1.00 30.00  ?  321 ASN B C   1 
ATOM   5952 O  O   . ASN B 1 321 ? 43.105 -66.087 23.723  1.00 29.71  ?  321 ASN B O   1 
ATOM   5953 C  CB  . ASN B 1 321 ? 43.546 -64.308 21.744  1.00 32.83  ?  321 ASN B CB  1 
ATOM   5954 C  CG  . ASN B 1 321 ? 43.814 -63.226 20.716  1.00 32.82  ?  321 ASN B CG  1 
ATOM   5955 O  OD1 . ASN B 1 321 ? 43.636 -62.028 20.989  1.00 35.01  ?  321 ASN B OD1 1 
ATOM   5956 N  ND2 . ASN B 1 321 ? 44.192 -63.639 19.513  1.00 27.62  ?  321 ASN B ND2 1 
ATOM   5957 N  N   . GLU B 1 322 ? 44.705 -65.365 25.131  1.00 29.70  ?  322 GLU B N   1 
ATOM   5958 C  CA  . GLU B 1 322 ? 44.575 -66.449 26.095  1.00 31.75  ?  322 GLU B CA  1 
ATOM   5959 C  C   . GLU B 1 322 ? 43.692 -66.051 27.286  1.00 30.41  ?  322 GLU B C   1 
ATOM   5960 O  O   . GLU B 1 322 ? 43.641 -66.809 28.256  1.00 29.26  ?  322 GLU B O   1 
ATOM   5961 C  CB  . GLU B 1 322 ? 45.953 -66.912 26.587  1.00 33.09  ?  322 GLU B CB  1 
ATOM   5962 C  CG  . GLU B 1 322 ? 46.676 -65.931 27.515  1.00 34.34  ?  322 GLU B CG  1 
ATOM   5963 C  CD  . GLU B 1 322 ? 47.942 -66.464 28.170  1.00 37.75  ?  322 GLU B CD  1 
ATOM   5964 O  OE1 . GLU B 1 322 ? 49.011 -65.824 28.009  1.00 44.47  ?  322 GLU B OE1 1 
ATOM   5965 O  OE2 . GLU B 1 322 ? 47.882 -67.526 28.834  1.00 35.17  -1 322 GLU B OE2 1 
ATOM   5966 N  N   . VAL B 1 323 ? 43.037 -64.872 27.225  1.00 27.19  ?  323 VAL B N   1 
ATOM   5967 C  CA  . VAL B 1 323 ? 42.077 -64.439 28.234  1.00 29.31  ?  323 VAL B CA  1 
ATOM   5968 C  C   . VAL B 1 323 ? 40.853 -63.861 27.519  1.00 28.03  ?  323 VAL B C   1 
ATOM   5969 O  O   . VAL B 1 323 ? 40.893 -62.741 27.013  1.00 23.83  ?  323 VAL B O   1 
ATOM   5970 C  CB  . VAL B 1 323 ? 42.603 -63.395 29.256  1.00 33.45  ?  323 VAL B CB  1 
ATOM   5971 C  CG1 . VAL B 1 323 ? 41.700 -63.242 30.490  1.00 30.77  ?  323 VAL B CG1 1 
ATOM   5972 C  CG2 . VAL B 1 323 ? 44.033 -63.683 29.694  1.00 34.48  ?  323 VAL B CG2 1 
ATOM   5973 N  N   . SER B 1 324 ? 39.748 -64.616 27.569  1.00 30.06  ?  324 SER B N   1 
ATOM   5974 C  CA  . SER B 1 324 ? 38.463 -64.234 26.993  1.00 30.14  ?  324 SER B CA  1 
ATOM   5975 C  C   . SER B 1 324 ? 37.616 -63.439 27.990  1.00 28.77  ?  324 SER B C   1 
ATOM   5976 O  O   . SER B 1 324 ? 37.972 -63.265 29.153  1.00 27.34  ?  324 SER B O   1 
ATOM   5977 C  CB  . SER B 1 324 ? 37.723 -65.472 26.557  1.00 29.79  ?  324 SER B CB  1 
ATOM   5978 O  OG  . SER B 1 324 ? 37.384 -66.215 27.718  1.00 28.77  ?  324 SER B OG  1 
ATOM   5979 N  N   . GLY B 1 325 ? 36.466 -62.970 27.511  1.00 32.44  ?  325 GLY B N   1 
ATOM   5980 C  CA  . GLY B 1 325 ? 35.503 -62.248 28.331  1.00 36.39  ?  325 GLY B CA  1 
ATOM   5981 C  C   . GLY B 1 325 ? 34.985 -63.079 29.506  1.00 36.88  ?  325 GLY B C   1 
ATOM   5982 O  O   . GLY B 1 325 ? 34.676 -62.522 30.552  1.00 35.26  ?  325 GLY B O   1 
ATOM   5983 N  N   . GLU B 1 326 ? 34.872 -64.401 29.323  1.00 36.76  ?  326 GLU B N   1 
ATOM   5984 C  CA  . GLU B 1 326 ? 34.463 -65.296 30.398  1.00 36.35  ?  326 GLU B CA  1 
ATOM   5985 C  C   . GLU B 1 326 ? 35.560 -65.351 31.462  1.00 34.37  ?  326 GLU B C   1 
ATOM   5986 O  O   . GLU B 1 326 ? 35.298 -65.207 32.644  1.00 36.61  ?  326 GLU B O   1 
ATOM   5987 C  CB  . GLU B 1 326 ? 34.125 -66.681 29.850  1.00 37.89  ?  326 GLU B CB  1 
ATOM   5988 C  CG  . GLU B 1 326 ? 33.072 -66.638 28.739  1.00 40.43  ?  326 GLU B CG  1 
ATOM   5989 C  CD  . GLU B 1 326 ? 33.560 -66.352 27.324  1.00 43.82  ?  326 GLU B CD  1 
ATOM   5990 O  OE1 . GLU B 1 326 ? 34.786 -66.269 27.108  1.00 49.63  ?  326 GLU B OE1 1 
ATOM   5991 O  OE2 . GLU B 1 326 ? 32.715 -66.200 26.415  1.00 46.06  -1 326 GLU B OE2 1 
ATOM   5992 N  N   . GLU B 1 327 ? 36.813 -65.492 31.030  1.00 33.45  ?  327 GLU B N   1 
ATOM   5993 C  CA  . GLU B 1 327 ? 37.917 -65.688 31.946  1.00 29.68  ?  327 GLU B CA  1 
ATOM   5994 C  C   . GLU B 1 327 ? 38.169 -64.413 32.737  1.00 31.35  ?  327 GLU B C   1 
ATOM   5995 O  O   . GLU B 1 327 ? 38.669 -64.469 33.854  1.00 39.30  ?  327 GLU B O   1 
ATOM   5996 C  CB  . GLU B 1 327 ? 39.100 -66.236 31.154  1.00 27.55  ?  327 GLU B CB  1 
ATOM   5997 C  CG  . GLU B 1 327 ? 38.965 -67.733 30.879  1.00 28.06  ?  327 GLU B CG  1 
ATOM   5998 C  CD  . GLU B 1 327 ? 39.693 -68.210 29.631  1.00 31.30  ?  327 GLU B CD  1 
ATOM   5999 O  OE1 . GLU B 1 327 ? 40.422 -69.248 29.595  1.00 25.27  ?  327 GLU B OE1 1 
ATOM   6000 O  OE2 . GLU B 1 327 ? 39.510 -67.450 28.640  1.00 38.24  -1 327 GLU B OE2 1 
ATOM   6001 N  N   . ALA B 1 328 ? 37.819 -63.268 32.158  1.00 30.40  ?  328 ALA B N   1 
ATOM   6002 C  CA  . ALA B 1 328 ? 37.922 -61.997 32.853  1.00 30.04  ?  328 ALA B CA  1 
ATOM   6003 C  C   . ALA B 1 328 ? 36.814 -61.865 33.905  1.00 29.91  ?  328 ALA B C   1 
ATOM   6004 O  O   . ALA B 1 328 ? 36.968 -61.182 34.913  1.00 30.30  ?  328 ALA B O   1 
ATOM   6005 C  CB  . ALA B 1 328 ? 37.848 -60.886 31.816  1.00 31.45  ?  328 ALA B CB  1 
ATOM   6006 N  N   . GLN B 1 329 ? 35.656 -62.471 33.630  1.00 30.44  ?  329 GLN B N   1 
ATOM   6007 C  CA  . GLN B 1 329 ? 34.503 -62.377 34.506  1.00 30.17  ?  329 GLN B CA  1 
ATOM   6008 C  C   . GLN B 1 329 ? 34.686 -63.390 35.632  1.00 29.13  ?  329 GLN B C   1 
ATOM   6009 O  O   . GLN B 1 329 ? 34.302 -63.141 36.776  1.00 31.17  ?  329 GLN B O   1 
ATOM   6010 C  CB  . GLN B 1 329 ? 33.227 -62.614 33.697  1.00 31.17  ?  329 GLN B CB  1 
ATOM   6011 C  CG  . GLN B 1 329 ? 32.844 -61.467 32.769  1.00 31.49  ?  329 GLN B CG  1 
ATOM   6012 C  CD  . GLN B 1 329 ? 32.281 -60.284 33.512  1.00 37.49  ?  329 GLN B CD  1 
ATOM   6013 O  OE1 . GLN B 1 329 ? 31.899 -60.399 34.678  1.00 46.03  ?  329 GLN B OE1 1 
ATOM   6014 N  NE2 . GLN B 1 329 ? 32.221 -59.130 32.859  1.00 42.26  ?  329 GLN B NE2 1 
ATOM   6015 N  N   . ALA B 1 330 ? 35.285 -64.530 35.277  1.00 28.10  ?  330 ALA B N   1 
ATOM   6016 C  CA  . ALA B 1 330 ? 35.704 -65.540 36.238  1.00 30.87  ?  330 ALA B CA  1 
ATOM   6017 C  C   . ALA B 1 330 ? 36.618 -64.904 37.284  1.00 32.63  ?  330 ALA B C   1 
ATOM   6018 O  O   . ALA B 1 330 ? 36.382 -65.055 38.483  1.00 34.48  ?  330 ALA B O   1 
ATOM   6019 C  CB  . ALA B 1 330 ? 36.405 -66.684 35.514  1.00 28.88  ?  330 ALA B CB  1 
ATOM   6020 N  N   . LEU B 1 331 ? 37.647 -64.203 36.777  1.00 30.54  ?  331 LEU B N   1 
ATOM   6021 C  CA  . LEU B 1 331 ? 38.696 -63.593 37.571  1.00 30.55  ?  331 LEU B CA  1 
ATOM   6022 C  C   . LEU B 1 331 ? 38.099 -62.523 38.475  1.00 31.25  ?  331 LEU B C   1 
ATOM   6023 O  O   . LEU B 1 331 ? 38.393 -62.480 39.667  1.00 35.45  ?  331 LEU B O   1 
ATOM   6024 C  CB  . LEU B 1 331 ? 39.766 -63.027 36.633  1.00 31.46  ?  331 LEU B CB  1 
ATOM   6025 C  CG  . LEU B 1 331 ? 40.814 -64.028 36.127  1.00 30.49  ?  331 LEU B CG  1 
ATOM   6026 C  CD1 . LEU B 1 331 ? 41.524 -63.571 34.872  1.00 32.01  ?  331 LEU B CD1 1 
ATOM   6027 C  CD2 . LEU B 1 331 ? 41.841 -64.272 37.191  1.00 29.96  ?  331 LEU B CD2 1 
ATOM   6028 N  N   . ILE B 1 332 ? 37.272 -61.655 37.900  1.00 31.85  ?  332 ILE B N   1 
ATOM   6029 C  CA  . ILE B 1 332 ? 36.619 -60.617 38.675  1.00 35.00  ?  332 ILE B CA  1 
ATOM   6030 C  C   . ILE B 1 332 ? 35.926 -61.264 39.871  1.00 36.49  ?  332 ILE B C   1 
ATOM   6031 O  O   . ILE B 1 332 ? 36.210 -60.888 41.007  1.00 34.01  ?  332 ILE B O   1 
ATOM   6032 C  CB  . ILE B 1 332 ? 35.650 -59.820 37.788  1.00 37.18  ?  332 ILE B CB  1 
ATOM   6033 C  CG1 . ILE B 1 332 ? 36.429 -58.945 36.812  1.00 39.30  ?  332 ILE B CG1 1 
ATOM   6034 C  CG2 . ILE B 1 332 ? 34.660 -59.015 38.638  1.00 37.86  ?  332 ILE B CG2 1 
ATOM   6035 C  CD1 . ILE B 1 332 ? 35.567 -58.005 35.975  1.00 44.08  ?  332 ILE B CD1 1 
ATOM   6036 N  N   . ALA B 1 333 ? 35.062 -62.258 39.580  1.00 39.38  ?  333 ALA B N   1 
ATOM   6037 C  CA  . ALA B 1 333 ? 34.279 -63.006 40.564  1.00 39.64  ?  333 ALA B CA  1 
ATOM   6038 C  C   . ALA B 1 333 ? 35.174 -63.764 41.544  1.00 33.86  ?  333 ALA B C   1 
ATOM   6039 O  O   . ALA B 1 333 ? 34.759 -64.008 42.667  1.00 32.83  ?  333 ALA B O   1 
ATOM   6040 C  CB  . ALA B 1 333 ? 33.327 -63.981 39.871  1.00 39.66  ?  333 ALA B CB  1 
ATOM   6041 N  N   . ALA B 1 334 ? 36.380 -64.131 41.098  1.00 30.66  ?  334 ALA B N   1 
ATOM   6042 C  CA  . ALA B 1 334 ? 37.362 -64.825 41.913  1.00 33.83  ?  334 ALA B CA  1 
ATOM   6043 C  C   . ALA B 1 334 ? 38.161 -63.857 42.798  1.00 34.37  ?  334 ALA B C   1 
ATOM   6044 O  O   . ALA B 1 334 ? 39.115 -64.261 43.454  1.00 36.96  ?  334 ALA B O   1 
ATOM   6045 C  CB  . ALA B 1 334 ? 38.279 -65.639 41.010  1.00 32.54  ?  334 ALA B CB  1 
ATOM   6046 N  N   . GLY B 1 335 ? 37.800 -62.575 42.812  1.00 33.85  ?  335 GLY B N   1 
ATOM   6047 C  CA  . GLY B 1 335 ? 38.464 -61.615 43.678  1.00 35.52  ?  335 GLY B CA  1 
ATOM   6048 C  C   . GLY B 1 335 ? 39.759 -61.028 43.101  1.00 37.78  ?  335 GLY B C   1 
ATOM   6049 O  O   . GLY B 1 335 ? 40.465 -60.351 43.842  1.00 37.56  ?  335 GLY B O   1 
ATOM   6050 N  N   . CYS B 1 336 ? 40.060 -61.259 41.803  1.00 39.25  ?  336 CYS B N   1 
ATOM   6051 C  CA  . CYS B 1 336 ? 41.252 -60.721 41.143  1.00 38.07  ?  336 CYS B CA  1 
ATOM   6052 C  C   . CYS B 1 336 ? 41.143 -59.200 41.076  1.00 36.84  ?  336 CYS B C   1 
ATOM   6053 O  O   . CYS B 1 336 ? 40.070 -58.667 40.821  1.00 39.34  ?  336 CYS B O   1 
ATOM   6054 C  CB  . CYS B 1 336 ? 41.416 -61.306 39.739  1.00 39.14  ?  336 CYS B CB  1 
ATOM   6055 S  SG  . CYS B 1 336 ? 43.107 -61.294 39.072  1.00 41.49  ?  336 CYS B SG  1 
ATOM   6056 N  N   . LYS B 1 337 ? 42.241 -58.494 41.337  1.00 35.48  ?  337 LYS B N   1 
ATOM   6057 C  CA  . LYS B 1 337 ? 42.195 -57.039 41.377  1.00 35.53  ?  337 LYS B CA  1 
ATOM   6058 C  C   . LYS B 1 337 ? 43.290 -56.412 40.502  1.00 33.06  ?  337 LYS B C   1 
ATOM   6059 O  O   . LYS B 1 337 ? 43.304 -55.188 40.357  1.00 32.92  ?  337 LYS B O   1 
ATOM   6060 C  CB  . LYS B 1 337 ? 42.282 -56.556 42.833  1.00 36.18  ?  337 LYS B CB  1 
ATOM   6061 C  CG  . LYS B 1 337 ? 41.366 -57.247 43.836  1.00 35.92  ?  337 LYS B CG  1 
ATOM   6062 C  CD  . LYS B 1 337 ? 39.991 -56.611 43.958  1.00 37.99  ?  337 LYS B CD  1 
ATOM   6063 C  CE  . LYS B 1 337 ? 39.000 -57.456 44.685  1.00 38.33  ?  337 LYS B CE  1 
ATOM   6064 N  NZ  . LYS B 1 337 ? 37.730 -56.737 44.825  1.00 40.46  1  337 LYS B NZ  1 
ATOM   6065 N  N   . PHE B 1 338 ? 44.157 -57.243 39.889  1.00 30.49  ?  338 PHE B N   1 
ATOM   6066 C  CA  . PHE B 1 338 ? 45.382 -56.808 39.213  1.00 30.08  ?  338 PHE B CA  1 
ATOM   6067 C  C   . PHE B 1 338 ? 45.719 -57.801 38.086  1.00 28.98  ?  338 PHE B C   1 
ATOM   6068 O  O   . PHE B 1 338 ? 45.982 -58.981 38.332  1.00 26.23  ?  338 PHE B O   1 
ATOM   6069 C  CB  . PHE B 1 338 ? 46.583 -56.654 40.175  1.00 28.06  ?  338 PHE B CB  1 
ATOM   6070 C  CG  . PHE B 1 338 ? 46.369 -55.694 41.345  1.00 27.29  ?  338 PHE B CG  1 
ATOM   6071 C  CD1 . PHE B 1 338 ? 46.383 -54.309 41.154  1.00 27.34  ?  338 PHE B CD1 1 
ATOM   6072 C  CD2 . PHE B 1 338 ? 46.102 -56.171 42.630  1.00 27.09  ?  338 PHE B CD2 1 
ATOM   6073 C  CE1 . PHE B 1 338 ? 46.139 -53.440 42.217  1.00 28.26  ?  338 PHE B CE1 1 
ATOM   6074 C  CE2 . PHE B 1 338 ? 45.865 -55.299 43.696  1.00 27.05  ?  338 PHE B CE2 1 
ATOM   6075 C  CZ  . PHE B 1 338 ? 45.883 -53.935 43.487  1.00 28.19  ?  338 PHE B CZ  1 
ATOM   6076 N  N   . ILE B 1 339 ? 45.713 -57.328 36.834  1.00 28.41  ?  339 ILE B N   1 
ATOM   6077 C  CA  . ILE B 1 339 ? 46.116 -58.173 35.721  1.00 30.57  ?  339 ILE B CA  1 
ATOM   6078 C  C   . ILE B 1 339 ? 46.919 -57.347 34.724  1.00 30.89  ?  339 ILE B C   1 
ATOM   6079 O  O   . ILE B 1 339 ? 46.483 -56.268 34.337  1.00 29.88  ?  339 ILE B O   1 
ATOM   6080 C  CB  . ILE B 1 339 ? 44.914 -58.870 35.051  1.00 33.94  ?  339 ILE B CB  1 
ATOM   6081 C  CG1 . ILE B 1 339 ? 45.348 -59.720 33.851  1.00 34.85  ?  339 ILE B CG1 1 
ATOM   6082 C  CG2 . ILE B 1 339 ? 43.815 -57.874 34.663  1.00 34.28  ?  339 ILE B CG2 1 
ATOM   6083 C  CD1 . ILE B 1 339 ? 44.376 -60.835 33.502  1.00 37.26  ?  339 ILE B CD1 1 
ATOM   6084 N  N   . ALA B 1 340 ? 48.102 -57.876 34.357  1.00 32.62  ?  340 ALA B N   1 
ATOM   6085 C  CA  . ALA B 1 340 ? 48.845 -57.459 33.178  1.00 34.30  ?  340 ALA B CA  1 
ATOM   6086 C  C   . ALA B 1 340 ? 49.389 -58.680 32.444  1.00 31.88  ?  340 ALA B C   1 
ATOM   6087 O  O   . ALA B 1 340 ? 49.480 -59.761 33.020  1.00 30.44  ?  340 ALA B O   1 
ATOM   6088 C  CB  . ALA B 1 340 ? 49.973 -56.527 33.566  1.00 38.84  ?  340 ALA B CB  1 
ATOM   6089 N  N   . GLU B 1 341 ? 49.792 -58.466 31.182  1.00 31.95  ?  341 GLU B N   1 
ATOM   6090 C  CA  . GLU B 1 341 ? 50.242 -59.526 30.290  1.00 31.24  ?  341 GLU B CA  1 
ATOM   6091 C  C   . GLU B 1 341 ? 51.763 -59.666 30.330  1.00 28.90  ?  341 GLU B C   1 
ATOM   6092 O  O   . GLU B 1 341 ? 52.472 -58.678 30.188  1.00 24.87  ?  341 GLU B O   1 
ATOM   6093 C  CB  . GLU B 1 341 ? 49.811 -59.184 28.866  1.00 31.43  ?  341 GLU B CB  1 
ATOM   6094 C  CG  . GLU B 1 341 ? 48.333 -58.820 28.778  1.00 33.03  ?  341 GLU B CG  1 
ATOM   6095 C  CD  . GLU B 1 341 ? 47.987 -58.069 27.515  1.00 33.93  ?  341 GLU B CD  1 
ATOM   6096 O  OE1 . GLU B 1 341 ? 46.798 -57.699 27.375  1.00 32.52  ?  341 GLU B OE1 1 
ATOM   6097 O  OE2 . GLU B 1 341 ? 48.911 -57.852 26.693  1.00 36.40  -1 341 GLU B OE2 1 
ATOM   6098 N  N   . GLY B 1 342 ? 52.238 -60.906 30.533  1.00 30.45  ?  342 GLY B N   1 
ATOM   6099 C  CA  . GLY B 1 342 ? 53.610 -61.302 30.245  1.00 31.75  ?  342 GLY B CA  1 
ATOM   6100 C  C   . GLY B 1 342 ? 53.767 -61.758 28.796  1.00 34.06  ?  342 GLY B C   1 
ATOM   6101 O  O   . GLY B 1 342 ? 54.857 -61.658 28.238  1.00 36.15  ?  342 GLY B O   1 
ATOM   6102 N  N   . SER B 1 343 ? 52.663 -62.266 28.220  1.00 35.58  ?  343 SER B N   1 
ATOM   6103 C  CA  . SER B 1 343 ? 52.524 -62.619 26.813  1.00 35.29  ?  343 SER B CA  1 
ATOM   6104 C  C   . SER B 1 343 ? 52.027 -61.415 26.007  1.00 37.08  ?  343 SER B C   1 
ATOM   6105 O  O   . SER B 1 343 ? 51.384 -60.530 26.572  1.00 34.93  ?  343 SER B O   1 
ATOM   6106 C  CB  . SER B 1 343 ? 51.564 -63.794 26.666  1.00 36.40  ?  343 SER B CB  1 
ATOM   6107 O  OG  . SER B 1 343 ? 50.211 -63.447 26.968  1.00 34.52  ?  343 SER B OG  1 
ATOM   6108 N  N   . ASN B 1 344 ? 52.283 -61.419 24.681  1.00 39.17  ?  344 ASN B N   1 
ATOM   6109 C  CA  . ASN B 1 344 ? 51.950 -60.306 23.797  1.00 36.48  ?  344 ASN B CA  1 
ATOM   6110 C  C   . ASN B 1 344 ? 50.481 -60.426 23.407  1.00 40.18  ?  344 ASN B C   1 
ATOM   6111 O  O   . ASN B 1 344 ? 50.105 -61.413 22.783  1.00 45.46  ?  344 ASN B O   1 
ATOM   6112 C  CB  . ASN B 1 344 ? 52.863 -60.240 22.571  1.00 34.64  ?  344 ASN B CB  1 
ATOM   6113 C  CG  . ASN B 1 344 ? 52.828 -58.893 21.865  1.00 37.30  ?  344 ASN B CG  1 
ATOM   6114 O  OD1 . ASN B 1 344 ? 51.892 -58.567 21.124  1.00 34.01  ?  344 ASN B OD1 1 
ATOM   6115 N  ND2 . ASN B 1 344 ? 53.852 -58.075 22.058  1.00 39.30  ?  344 ASN B ND2 1 
ATOM   6116 N  N   . MET B 1 345 ? 49.675 -59.421 23.796  1.00 43.55  ?  345 MET B N   1 
ATOM   6117 C  CA  . MET B 1 345 ? 48.234 -59.380 23.569  1.00 45.83  ?  345 MET B CA  1 
ATOM   6118 C  C   . MET B 1 345 ? 47.535 -60.645 24.080  1.00 42.35  ?  345 MET B C   1 
ATOM   6119 O  O   . MET B 1 345 ? 46.603 -61.151 23.452  1.00 44.96  ?  345 MET B O   1 
ATOM   6120 C  CB  . MET B 1 345 ? 47.935 -59.194 22.078  1.00 49.85  ?  345 MET B CB  1 
ATOM   6121 C  CG  . MET B 1 345 ? 48.628 -58.005 21.467  1.00 50.35  ?  345 MET B CG  1 
ATOM   6122 S  SD  . MET B 1 345 ? 48.319 -58.001 19.693  1.00 62.15  ?  345 MET B SD  1 
ATOM   6123 C  CE  . MET B 1 345 ? 49.141 -59.493 19.108  1.00 61.84  ?  345 MET B CE  1 
ATOM   6124 N  N   . GLY B 1 346 ? 47.990 -61.157 25.227  1.00 40.49  ?  346 GLY B N   1 
ATOM   6125 C  CA  . GLY B 1 346 ? 47.370 -62.316 25.846  1.00 36.92  ?  346 GLY B CA  1 
ATOM   6126 C  C   . GLY B 1 346 ? 45.877 -62.070 26.046  1.00 34.31  ?  346 GLY B C   1 
ATOM   6127 O  O   . GLY B 1 346 ? 45.064 -62.938 25.740  1.00 31.87  ?  346 GLY B O   1 
ATOM   6128 N  N   . CYS B 1 347 ? 45.534 -60.874 26.543  1.00 30.38  ?  347 CYS B N   1 
ATOM   6129 C  CA  . CYS B 1 347 ? 44.151 -60.531 26.818  1.00 31.76  ?  347 CYS B CA  1 
ATOM   6130 C  C   . CYS B 1 347 ? 43.462 -60.007 25.566  1.00 29.31  ?  347 CYS B C   1 
ATOM   6131 O  O   . CYS B 1 347 ? 44.019 -59.171 24.855  1.00 29.72  ?  347 CYS B O   1 
ATOM   6132 C  CB  . CYS B 1 347 ? 44.038 -59.500 27.933  1.00 34.06  ?  347 CYS B CB  1 
ATOM   6133 S  SG  . CYS B 1 347 ? 44.507 -60.178 29.541  1.00 37.48  ?  347 CYS B SG  1 
ATOM   6134 N  N   . THR B 1 348 ? 42.222 -60.478 25.374  1.00 27.42  ?  348 THR B N   1 
ATOM   6135 C  CA  . THR B 1 348 ? 41.394 -60.144 24.232  1.00 26.01  ?  348 THR B CA  1 
ATOM   6136 C  C   . THR B 1 348 ? 40.761 -58.791 24.507  1.00 26.31  ?  348 THR B C   1 
ATOM   6137 O  O   . THR B 1 348 ? 40.736 -58.350 25.651  1.00 26.81  ?  348 THR B O   1 
ATOM   6138 C  CB  . THR B 1 348 ? 40.338 -61.237 24.028  1.00 25.78  ?  348 THR B CB  1 
ATOM   6139 O  OG1 . THR B 1 348 ? 39.584 -61.301 25.223  1.00 25.34  ?  348 THR B OG1 1 
ATOM   6140 C  CG2 . THR B 1 348 ? 40.905 -62.631 23.828  1.00 26.30  ?  348 THR B CG2 1 
ATOM   6141 N  N   . GLN B 1 349 ? 40.239 -58.147 23.460  1.00 29.30  ?  349 GLN B N   1 
ATOM   6142 C  CA  . GLN B 1 349 ? 39.500 -56.903 23.630  1.00 30.70  ?  349 GLN B CA  1 
ATOM   6143 C  C   . GLN B 1 349 ? 38.360 -57.102 24.634  1.00 30.32  ?  349 GLN B C   1 
ATOM   6144 O  O   . GLN B 1 349 ? 38.165 -56.295 25.547  1.00 32.37  ?  349 GLN B O   1 
ATOM   6145 C  CB  . GLN B 1 349 ? 38.930 -56.373 22.310  1.00 29.91  ?  349 GLN B CB  1 
ATOM   6146 C  CG  . GLN B 1 349 ? 38.365 -54.962 22.451  1.00 28.22  ?  349 GLN B CG  1 
ATOM   6147 C  CD  . GLN B 1 349 ? 39.448 -54.015 22.921  1.00 26.16  ?  349 GLN B CD  1 
ATOM   6148 O  OE1 . GLN B 1 349 ? 40.539 -54.016 22.350  1.00 28.71  ?  349 GLN B OE1 1 
ATOM   6149 N  NE2 . GLN B 1 349 ? 39.202 -53.243 23.966  1.00 23.52  ?  349 GLN B NE2 1 
ATOM   6150 N  N   . ALA B 1 350 ? 37.589 -58.172 24.432  1.00 28.94  ?  350 ALA B N   1 
ATOM   6151 C  CA  . ALA B 1 350 ? 36.455 -58.479 25.286  1.00 28.81  ?  350 ALA B CA  1 
ATOM   6152 C  C   . ALA B 1 350 ? 36.856 -58.330 26.757  1.00 32.89  ?  350 ALA B C   1 
ATOM   6153 O  O   . ALA B 1 350 ? 36.153 -57.639 27.514  1.00 33.45  ?  350 ALA B O   1 
ATOM   6154 C  CB  . ALA B 1 350 ? 35.945 -59.864 24.966  1.00 25.74  ?  350 ALA B CB  1 
ATOM   6155 N  N   . ALA B 1 351 ? 38.001 -58.952 27.124  1.00 30.62  ?  351 ALA B N   1 
ATOM   6156 C  CA  . ALA B 1 351 ? 38.519 -58.963 28.489  1.00 30.35  ?  351 ALA B CA  1 
ATOM   6157 C  C   . ALA B 1 351 ? 38.868 -57.560 28.971  1.00 30.64  ?  351 ALA B C   1 
ATOM   6158 O  O   . ALA B 1 351 ? 38.502 -57.191 30.078  1.00 31.19  ?  351 ALA B O   1 
ATOM   6159 C  CB  . ALA B 1 351 ? 39.736 -59.841 28.573  1.00 32.46  ?  351 ALA B CB  1 
ATOM   6160 N  N   . ILE B 1 352 ? 39.586 -56.795 28.141  1.00 30.56  ?  352 ILE B N   1 
ATOM   6161 C  CA  . ILE B 1 352 ? 39.939 -55.419 28.459  1.00 32.56  ?  352 ILE B CA  1 
ATOM   6162 C  C   . ILE B 1 352 ? 38.675 -54.615 28.760  1.00 34.30  ?  352 ILE B C   1 
ATOM   6163 O  O   . ILE B 1 352 ? 38.667 -53.785 29.672  1.00 36.29  ?  352 ILE B O   1 
ATOM   6164 C  CB  . ILE B 1 352 ? 40.706 -54.764 27.298  1.00 35.05  ?  352 ILE B CB  1 
ATOM   6165 C  CG1 . ILE B 1 352 ? 41.971 -55.540 26.929  1.00 37.45  ?  352 ILE B CG1 1 
ATOM   6166 C  CG2 . ILE B 1 352 ? 41.008 -53.294 27.597  1.00 33.77  ?  352 ILE B CG2 1 
ATOM   6167 C  CD1 . ILE B 1 352 ? 42.452 -55.293 25.505  1.00 37.28  ?  352 ILE B CD1 1 
ATOM   6168 N  N   . ASP B 1 353 ? 37.629 -54.840 27.947  1.00 34.19  ?  353 ASP B N   1 
ATOM   6169 C  CA  . ASP B 1 353 ? 36.389 -54.075 28.027  1.00 31.78  ?  353 ASP B CA  1 
ATOM   6170 C  C   . ASP B 1 353 ? 35.699 -54.352 29.366  1.00 30.63  ?  353 ASP B C   1 
ATOM   6171 O  O   . ASP B 1 353 ? 35.098 -53.457 29.959  1.00 30.67  ?  353 ASP B O   1 
ATOM   6172 C  CB  . ASP B 1 353 ? 35.538 -54.350 26.793  1.00 29.11  ?  353 ASP B CB  1 
ATOM   6173 C  CG  . ASP B 1 353 ? 36.122 -53.838 25.479  1.00 28.50  ?  353 ASP B CG  1 
ATOM   6174 O  OD1 . ASP B 1 353 ? 37.082 -53.028 25.531  1.00 22.47  ?  353 ASP B OD1 1 
ATOM   6175 O  OD2 . ASP B 1 353 ? 35.603 -54.243 24.408  1.00 29.91  -1 353 ASP B OD2 1 
ATOM   6176 N  N   . ALA B 1 354 ? 35.819 -55.607 29.821  1.00 26.69  ?  354 ALA B N   1 
ATOM   6177 C  CA  . ALA B 1 354 ? 35.152 -56.100 31.005  1.00 25.78  ?  354 ALA B CA  1 
ATOM   6178 C  C   . ALA B 1 354 ? 35.795 -55.518 32.271  1.00 27.89  ?  354 ALA B C   1 
ATOM   6179 O  O   . ALA B 1 354 ? 35.095 -55.099 33.204  1.00 25.10  ?  354 ALA B O   1 
ATOM   6180 C  CB  . ALA B 1 354 ? 35.210 -57.614 30.964  1.00 25.64  ?  354 ALA B CB  1 
ATOM   6181 N  N   . PHE B 1 355 ? 37.138 -55.502 32.282  1.00 28.96  ?  355 PHE B N   1 
ATOM   6182 C  CA  . PHE B 1 355 ? 37.940 -54.949 33.361  1.00 29.39  ?  355 PHE B CA  1 
ATOM   6183 C  C   . PHE B 1 355 ? 37.764 -53.435 33.422  1.00 30.86  ?  355 PHE B C   1 
ATOM   6184 O  O   . PHE B 1 355 ? 37.680 -52.850 34.510  1.00 34.24  ?  355 PHE B O   1 
ATOM   6185 C  CB  . PHE B 1 355 ? 39.427 -55.232 33.125  1.00 31.63  ?  355 PHE B CB  1 
ATOM   6186 C  CG  . PHE B 1 355 ? 39.863 -56.694 33.031  1.00 29.74  ?  355 PHE B CG  1 
ATOM   6187 C  CD1 . PHE B 1 355 ? 40.829 -57.089 32.101  1.00 28.46  ?  355 PHE B CD1 1 
ATOM   6188 C  CD2 . PHE B 1 355 ? 39.335 -57.649 33.897  1.00 27.51  ?  355 PHE B CD2 1 
ATOM   6189 C  CE1 . PHE B 1 355 ? 41.223 -58.416 32.013  1.00 31.55  ?  355 PHE B CE1 1 
ATOM   6190 C  CE2 . PHE B 1 355 ? 39.745 -58.962 33.826  1.00 30.40  ?  355 PHE B CE2 1 
ATOM   6191 C  CZ  . PHE B 1 355 ? 40.695 -59.348 32.884  1.00 33.50  ?  355 PHE B CZ  1 
ATOM   6192 N  N   . GLU B 1 356 ? 37.743 -52.800 32.245  1.00 29.26  ?  356 GLU B N   1 
ATOM   6193 C  CA  . GLU B 1 356 ? 37.676 -51.342 32.168  1.00 30.48  ?  356 GLU B CA  1 
ATOM   6194 C  C   . GLU B 1 356 ? 36.281 -50.853 32.573  1.00 34.55  ?  356 GLU B C   1 
ATOM   6195 O  O   . GLU B 1 356 ? 36.151 -49.728 33.070  1.00 40.76  ?  356 GLU B O   1 
ATOM   6196 C  CB  . GLU B 1 356 ? 38.091 -50.826 30.787  1.00 26.59  ?  356 GLU B CB  1 
ATOM   6197 C  CG  . GLU B 1 356 ? 39.600 -50.844 30.561  1.00 25.74  ?  356 GLU B CG  1 
ATOM   6198 C  CD  . GLU B 1 356 ? 40.336 -49.696 31.231  1.00 26.03  ?  356 GLU B CD  1 
ATOM   6199 O  OE1 . GLU B 1 356 ? 40.065 -48.536 30.866  1.00 26.88  ?  356 GLU B OE1 1 
ATOM   6200 O  OE2 . GLU B 1 356 ? 41.172 -49.923 32.122  1.00 24.98  -1 356 GLU B OE2 1 
ATOM   6201 N  N   . ALA B 1 357 ? 35.248 -51.694 32.336  1.00 31.75  ?  357 ALA B N   1 
ATOM   6202 C  CA  . ALA B 1 357 ? 33.900 -51.455 32.831  1.00 26.31  ?  357 ALA B CA  1 
ATOM   6203 C  C   . ALA B 1 357 ? 33.883 -51.633 34.349  1.00 25.87  ?  357 ALA B C   1 
ATOM   6204 O  O   . ALA B 1 357 ? 33.483 -50.722 35.072  1.00 22.82  ?  357 ALA B O   1 
ATOM   6205 C  CB  . ALA B 1 357 ? 32.927 -52.385 32.153  1.00 25.23  ?  357 ALA B CB  1 
ATOM   6206 N  N   . HIS B 1 358 ? 34.383 -52.794 34.814  1.00 27.08  ?  358 HIS B N   1 
ATOM   6207 C  CA  . HIS B 1 358 ? 34.489 -53.120 36.233  1.00 27.56  ?  358 HIS B CA  1 
ATOM   6208 C  C   . HIS B 1 358 ? 35.221 -52.027 37.000  1.00 29.08  ?  358 HIS B C   1 
ATOM   6209 O  O   . HIS B 1 358 ? 34.837 -51.714 38.118  1.00 26.89  ?  358 HIS B O   1 
ATOM   6210 C  CB  . HIS B 1 358 ? 35.206 -54.460 36.461  1.00 27.12  ?  358 HIS B CB  1 
ATOM   6211 C  CG  . HIS B 1 358 ? 35.242 -54.881 37.902  1.00 29.07  ?  358 HIS B CG  1 
ATOM   6212 N  ND1 . HIS B 1 358 ? 36.073 -54.314 38.846  1.00 28.12  ?  358 HIS B ND1 1 
ATOM   6213 C  CD2 . HIS B 1 358 ? 34.520 -55.797 38.572  1.00 28.92  ?  358 HIS B CD2 1 
ATOM   6214 C  CE1 . HIS B 1 358 ? 35.856 -54.883 40.025  1.00 26.46  ?  358 HIS B CE1 1 
ATOM   6215 N  NE2 . HIS B 1 358 ? 34.937 -55.794 39.875  1.00 26.44  ?  358 HIS B NE2 1 
ATOM   6216 N  N   . ARG B 1 359 ? 36.276 -51.465 36.384  1.00 36.25  ?  359 ARG B N   1 
ATOM   6217 C  CA  . ARG B 1 359 ? 37.053 -50.376 36.966  1.00 36.73  ?  359 ARG B CA  1 
ATOM   6218 C  C   . ARG B 1 359 ? 36.204 -49.111 37.143  1.00 35.70  ?  359 ARG B C   1 
ATOM   6219 O  O   . ARG B 1 359 ? 36.352 -48.434 38.162  1.00 33.51  ?  359 ARG B O   1 
ATOM   6220 C  CB  . ARG B 1 359 ? 38.291 -50.080 36.110  1.00 36.38  ?  359 ARG B CB  1 
ATOM   6221 C  CG  . ARG B 1 359 ? 39.215 -49.056 36.760  1.00 35.16  ?  359 ARG B CG  1 
ATOM   6222 C  CD  . ARG B 1 359 ? 40.272 -48.535 35.810  1.00 34.63  ?  359 ARG B CD  1 
ATOM   6223 N  NE  . ARG B 1 359 ? 39.723 -48.233 34.481  1.00 33.14  ?  359 ARG B NE  1 
ATOM   6224 C  CZ  . ARG B 1 359 ? 39.315 -47.049 34.031  1.00 28.01  ?  359 ARG B CZ  1 
ATOM   6225 N  NH1 . ARG B 1 359 ? 38.981 -46.928 32.757  1.00 24.93  1  359 ARG B NH1 1 
ATOM   6226 N  NH2 . ARG B 1 359 ? 39.274 -45.997 34.832  1.00 27.25  ?  359 ARG B NH2 1 
ATOM   6227 N  N   . GLU B 1 360 ? 35.350 -48.793 36.146  1.00 35.29  ?  360 GLU B N   1 
ATOM   6228 C  CA  . GLU B 1 360 ? 34.590 -47.543 36.127  1.00 39.22  ?  360 GLU B CA  1 
ATOM   6229 C  C   . GLU B 1 360 ? 33.486 -47.582 37.188  1.00 37.96  ?  360 GLU B C   1 
ATOM   6230 O  O   . GLU B 1 360 ? 33.069 -46.535 37.713  1.00 36.36  ?  360 GLU B O   1 
ATOM   6231 C  CB  . GLU B 1 360 ? 33.972 -47.218 34.759  1.00 39.57  ?  360 GLU B CB  1 
ATOM   6232 C  CG  . GLU B 1 360 ? 34.744 -46.229 33.881  1.00 36.24  ?  360 GLU B CG  1 
ATOM   6233 C  CD  . GLU B 1 360 ? 34.289 -46.296 32.429  1.00 37.78  ?  360 GLU B CD  1 
ATOM   6234 O  OE1 . GLU B 1 360 ? 33.980 -47.415 31.940  1.00 36.55  ?  360 GLU B OE1 1 
ATOM   6235 O  OE2 . GLU B 1 360 ? 34.242 -45.237 31.768  1.00 37.85  -1 360 GLU B OE2 1 
ATOM   6236 N  N   . ALA B 1 361 ? 33.052 -48.808 37.506  1.00 35.74  ?  361 ALA B N   1 
ATOM   6237 C  CA  . ALA B 1 361 ? 31.877 -49.056 38.325  1.00 37.84  ?  361 ALA B CA  1 
ATOM   6238 C  C   . ALA B 1 361 ? 32.252 -49.349 39.785  1.00 39.08  ?  361 ALA B C   1 
ATOM   6239 O  O   . ALA B 1 361 ? 31.428 -49.224 40.690  1.00 37.13  ?  361 ALA B O   1 
ATOM   6240 C  CB  . ALA B 1 361 ? 31.118 -50.203 37.700  1.00 37.90  ?  361 ALA B CB  1 
ATOM   6241 N  N   . ASN B 1 362 ? 33.502 -49.757 40.019  1.00 36.39  ?  362 ASN B N   1 
ATOM   6242 C  CA  . ASN B 1 362 ? 33.942 -50.107 41.353  1.00 34.15  ?  362 ASN B CA  1 
ATOM   6243 C  C   . ASN B 1 362 ? 35.010 -49.112 41.789  1.00 34.87  ?  362 ASN B C   1 
ATOM   6244 O  O   . ASN B 1 362 ? 35.999 -48.920 41.075  1.00 36.73  ?  362 ASN B O   1 
ATOM   6245 C  CB  . ASN B 1 362 ? 34.382 -51.562 41.396  1.00 34.58  ?  362 ASN B CB  1 
ATOM   6246 C  CG  . ASN B 1 362 ? 33.190 -52.465 41.216  1.00 38.13  ?  362 ASN B CG  1 
ATOM   6247 O  OD1 . ASN B 1 362 ? 32.374 -52.594 42.141  1.00 37.49  ?  362 ASN B OD1 1 
ATOM   6248 N  ND2 . ASN B 1 362 ? 33.057 -53.066 40.036  1.00 39.47  ?  362 ASN B ND2 1 
ATOM   6249 N  N   . LYS B 1 363 ? 34.786 -48.512 42.972  1.00 32.76  ?  363 LYS B N   1 
ATOM   6250 C  CA  . LYS B 1 363 ? 35.598 -47.431 43.504  1.00 35.67  ?  363 LYS B CA  1 
ATOM   6251 C  C   . LYS B 1 363 ? 36.787 -47.974 44.295  1.00 37.00  ?  363 LYS B C   1 
ATOM   6252 O  O   . LYS B 1 363 ? 36.626 -48.904 45.079  1.00 44.62  ?  363 LYS B O   1 
ATOM   6253 C  CB  . LYS B 1 363 ? 34.747 -46.553 44.425  1.00 41.04  ?  363 LYS B CB  1 
ATOM   6254 C  CG  . LYS B 1 363 ? 33.789 -45.570 43.730  1.00 46.78  ?  363 LYS B CG  1 
ATOM   6255 C  CD  . LYS B 1 363 ? 33.143 -44.529 44.649  1.00 47.91  ?  363 LYS B CD  1 
ATOM   6256 C  CE  . LYS B 1 363 ? 34.101 -43.895 45.627  1.00 47.28  ?  363 LYS B CE  1 
ATOM   6257 N  NZ  . LYS B 1 363 ? 33.487 -42.868 46.470  1.00 47.34  1  363 LYS B NZ  1 
ATOM   6258 N  N   . GLY B 1 364 ? 37.969 -47.371 44.081  1.00 37.45  ?  364 GLY B N   1 
ATOM   6259 C  CA  . GLY B 1 364 ? 39.183 -47.649 44.836  1.00 35.92  ?  364 GLY B CA  1 
ATOM   6260 C  C   . GLY B 1 364 ? 39.671 -49.071 44.600  1.00 37.42  ?  364 GLY B C   1 
ATOM   6261 O  O   . GLY B 1 364 ? 39.565 -49.573 43.487  1.00 43.59  ?  364 GLY B O   1 
ATOM   6262 N  N   . ALA B 1 365 ? 40.118 -49.727 45.681  1.00 40.72  ?  365 ALA B N   1 
ATOM   6263 C  CA  . ALA B 1 365 ? 40.797 -51.020 45.634  1.00 42.04  ?  365 ALA B CA  1 
ATOM   6264 C  C   . ALA B 1 365 ? 39.870 -52.158 45.203  1.00 38.69  ?  365 ALA B C   1 
ATOM   6265 O  O   . ALA B 1 365 ? 40.341 -53.279 44.980  1.00 37.50  ?  365 ALA B O   1 
ATOM   6266 C  CB  . ALA B 1 365 ? 41.397 -51.325 47.001  1.00 43.25  ?  365 ALA B CB  1 
ATOM   6267 N  N   . ALA B 1 366 ? 38.561 -51.872 45.154  1.00 35.25  ?  366 ALA B N   1 
ATOM   6268 C  CA  . ALA B 1 366 ? 37.548 -52.874 44.876  1.00 35.53  ?  366 ALA B CA  1 
ATOM   6269 C  C   . ALA B 1 366 ? 37.511 -53.208 43.378  1.00 38.00  ?  366 ALA B C   1 
ATOM   6270 O  O   . ALA B 1 366 ? 36.889 -54.193 42.972  1.00 37.19  ?  366 ALA B O   1 
ATOM   6271 C  CB  . ALA B 1 366 ? 36.215 -52.370 45.384  1.00 33.18  ?  366 ALA B CB  1 
ATOM   6272 N  N   . ALA B 1 367 ? 38.162 -52.370 42.556  1.00 35.06  ?  367 ALA B N   1 
ATOM   6273 C  CA  . ALA B 1 367 ? 38.188 -52.556 41.112  1.00 36.47  ?  367 ALA B CA  1 
ATOM   6274 C  C   . ALA B 1 367 ? 39.256 -53.577 40.748  1.00 34.26  ?  367 ALA B C   1 
ATOM   6275 O  O   . ALA B 1 367 ? 40.248 -53.650 41.458  1.00 38.26  ?  367 ALA B O   1 
ATOM   6276 C  CB  . ALA B 1 367 ? 38.478 -51.235 40.428  1.00 38.13  ?  367 ALA B CB  1 
ATOM   6277 N  N   . ILE B 1 368 ? 39.079 -54.309 39.629  1.00 31.75  ?  368 ILE B N   1 
ATOM   6278 C  CA  . ILE B 1 368 ? 40.201 -54.967 38.959  1.00 29.63  ?  368 ILE B CA  1 
ATOM   6279 C  C   . ILE B 1 368 ? 40.863 -53.964 38.025  1.00 27.24  ?  368 ILE B C   1 
ATOM   6280 O  O   . ILE B 1 368 ? 40.174 -53.243 37.304  1.00 27.81  ?  368 ILE B O   1 
ATOM   6281 C  CB  . ILE B 1 368 ? 39.835 -56.238 38.171  1.00 29.91  ?  368 ILE B CB  1 
ATOM   6282 C  CG1 . ILE B 1 368 ? 41.096 -56.924 37.658  1.00 29.31  ?  368 ILE B CG1 1 
ATOM   6283 C  CG2 . ILE B 1 368 ? 38.874 -55.922 37.023  1.00 32.02  ?  368 ILE B CG2 1 
ATOM   6284 C  CD1 . ILE B 1 368 ? 40.990 -58.429 37.535  1.00 29.82  ?  368 ILE B CD1 1 
ATOM   6285 N  N   . TRP B 1 369 ? 42.201 -53.932 38.071  1.00 26.41  ?  369 TRP B N   1 
ATOM   6286 C  CA  . TRP B 1 369 ? 43.002 -52.986 37.311  1.00 25.26  ?  369 TRP B CA  1 
ATOM   6287 C  C   . TRP B 1 369 ? 43.806 -53.768 36.288  1.00 25.64  ?  369 TRP B C   1 
ATOM   6288 O  O   . TRP B 1 369 ? 44.574 -54.662 36.659  1.00 25.09  ?  369 TRP B O   1 
ATOM   6289 C  CB  . TRP B 1 369 ? 43.942 -52.195 38.230  1.00 25.69  ?  369 TRP B CB  1 
ATOM   6290 C  CG  . TRP B 1 369 ? 44.289 -50.803 37.761  1.00 26.17  ?  369 TRP B CG  1 
ATOM   6291 C  CD1 . TRP B 1 369 ? 43.936 -50.181 36.594  1.00 25.72  ?  369 TRP B CD1 1 
ATOM   6292 C  CD2 . TRP B 1 369 ? 45.125 -49.859 38.477  1.00 25.83  ?  369 TRP B CD2 1 
ATOM   6293 N  NE1 . TRP B 1 369 ? 44.459 -48.913 36.541  1.00 24.08  ?  369 TRP B NE1 1 
ATOM   6294 C  CE2 . TRP B 1 369 ? 45.203 -48.691 37.672  1.00 24.94  ?  369 TRP B CE2 1 
ATOM   6295 C  CE3 . TRP B 1 369 ? 45.816 -49.896 39.705  1.00 23.18  ?  369 TRP B CE3 1 
ATOM   6296 C  CZ2 . TRP B 1 369 ? 45.933 -47.568 38.075  1.00 25.13  ?  369 TRP B CZ2 1 
ATOM   6297 C  CZ3 . TRP B 1 369 ? 46.546 -48.793 40.095  1.00 23.52  ?  369 TRP B CZ3 1 
ATOM   6298 C  CH2 . TRP B 1 369 ? 46.585 -47.637 39.296  1.00 25.25  ?  369 TRP B CH2 1 
ATOM   6299 N  N   . TYR B 1 370 ? 43.563 -53.443 35.010  1.00 27.71  ?  370 TYR B N   1 
ATOM   6300 C  CA  . TYR B 1 370 ? 44.318 -53.968 33.881  1.00 26.23  ?  370 TYR B CA  1 
ATOM   6301 C  C   . TYR B 1 370 ? 45.281 -52.909 33.367  1.00 25.67  ?  370 TYR B C   1 
ATOM   6302 O  O   . TYR B 1 370 ? 44.877 -51.760 33.178  1.00 25.05  ?  370 TYR B O   1 
ATOM   6303 C  CB  . TYR B 1 370 ? 43.341 -54.346 32.771  1.00 26.76  ?  370 TYR B CB  1 
ATOM   6304 C  CG  . TYR B 1 370 ? 43.986 -54.729 31.448  1.00 26.99  ?  370 TYR B CG  1 
ATOM   6305 C  CD1 . TYR B 1 370 ? 44.640 -55.938 31.287  1.00 25.51  ?  370 TYR B CD1 1 
ATOM   6306 C  CD2 . TYR B 1 370 ? 43.907 -53.882 30.349  1.00 28.16  ?  370 TYR B CD2 1 
ATOM   6307 C  CE1 . TYR B 1 370 ? 45.199 -56.290 30.072  1.00 25.67  ?  370 TYR B CE1 1 
ATOM   6308 C  CE2 . TYR B 1 370 ? 44.480 -54.217 29.134  1.00 27.16  ?  370 TYR B CE2 1 
ATOM   6309 C  CZ  . TYR B 1 370 ? 45.123 -55.429 28.993  1.00 25.69  ?  370 TYR B CZ  1 
ATOM   6310 O  OH  . TYR B 1 370 ? 45.656 -55.751 27.779  1.00 25.22  ?  370 TYR B OH  1 
ATOM   6311 N  N   . ALA B 1 371 ? 46.537 -53.322 33.165  1.00 25.95  ?  371 ALA B N   1 
ATOM   6312 C  CA  . ALA B 1 371 ? 47.525 -52.557 32.419  1.00 27.49  ?  371 ALA B CA  1 
ATOM   6313 C  C   . ALA B 1 371 ? 47.685 -53.134 31.019  1.00 30.78  ?  371 ALA B C   1 
ATOM   6314 O  O   . ALA B 1 371 ? 47.664 -54.353 30.854  1.00 37.09  ?  371 ALA B O   1 
ATOM   6315 C  CB  . ALA B 1 371 ? 48.841 -52.608 33.133  1.00 28.18  ?  371 ALA B CB  1 
ATOM   6316 N  N   . PRO B 1 372 ? 47.903 -52.289 29.987  1.00 30.12  ?  372 PRO B N   1 
ATOM   6317 C  CA  . PRO B 1 372 ? 48.166 -52.770 28.632  1.00 28.89  ?  372 PRO B CA  1 
ATOM   6318 C  C   . PRO B 1 372 ? 49.590 -53.263 28.388  1.00 31.89  ?  372 PRO B C   1 
ATOM   6319 O  O   . PRO B 1 372 ? 50.532 -52.880 29.100  1.00 29.75  ?  372 PRO B O   1 
ATOM   6320 C  CB  . PRO B 1 372 ? 47.866 -51.517 27.808  1.00 30.89  ?  372 PRO B CB  1 
ATOM   6321 C  CG  . PRO B 1 372 ? 48.305 -50.374 28.681  1.00 31.14  ?  372 PRO B CG  1 
ATOM   6322 C  CD  . PRO B 1 372 ? 47.913 -50.819 30.081  1.00 32.15  ?  372 PRO B CD  1 
ATOM   6323 N  N   . GLY B 1 373 ? 49.730 -54.097 27.340  1.00 30.78  ?  373 GLY B N   1 
ATOM   6324 C  CA  . GLY B 1 373 ? 51.017 -54.640 26.951  1.00 28.38  ?  373 GLY B CA  1 
ATOM   6325 C  C   . GLY B 1 373 ? 51.999 -53.532 26.592  1.00 28.55  ?  373 GLY B C   1 
ATOM   6326 O  O   . GLY B 1 373 ? 53.201 -53.677 26.775  1.00 29.38  ?  373 GLY B O   1 
ATOM   6327 N  N   . LYS B 1 374 ? 51.490 -52.416 26.070  1.00 30.40  ?  374 LYS B N   1 
ATOM   6328 C  CA  . LYS B 1 374 ? 52.376 -51.360 25.604  1.00 33.84  ?  374 LYS B CA  1 
ATOM   6329 C  C   . LYS B 1 374 ? 53.053 -50.685 26.800  1.00 35.29  ?  374 LYS B C   1 
ATOM   6330 O  O   . LYS B 1 374 ? 53.976 -49.891 26.599  1.00 32.41  ?  374 LYS B O   1 
ATOM   6331 C  CB  . LYS B 1 374 ? 51.682 -50.374 24.651  1.00 36.36  ?  374 LYS B CB  1 
ATOM   6332 C  CG  . LYS B 1 374 ? 50.635 -49.425 25.239  1.00 38.61  ?  374 LYS B CG  1 
ATOM   6333 C  CD  . LYS B 1 374 ? 49.711 -48.820 24.185  1.00 41.73  ?  374 LYS B CD  1 
ATOM   6334 C  CE  . LYS B 1 374 ? 48.942 -49.878 23.427  1.00 44.91  ?  374 LYS B CE  1 
ATOM   6335 N  NZ  . LYS B 1 374 ? 47.744 -49.386 22.738  1.00 45.74  1  374 LYS B NZ  1 
ATOM   6336 N  N   . ALA B 1 375 ? 52.599 -51.010 28.029  1.00 35.84  ?  375 ALA B N   1 
ATOM   6337 C  CA  . ALA B 1 375 ? 53.233 -50.531 29.252  1.00 31.80  ?  375 ALA B CA  1 
ATOM   6338 C  C   . ALA B 1 375 ? 53.723 -51.694 30.120  1.00 34.54  ?  375 ALA B C   1 
ATOM   6339 O  O   . ALA B 1 375 ? 54.853 -51.667 30.580  1.00 41.60  ?  375 ALA B O   1 
ATOM   6340 C  CB  . ALA B 1 375 ? 52.293 -49.611 30.001  1.00 27.81  ?  375 ALA B CB  1 
ATOM   6341 N  N   . ALA B 1 376 ? 52.911 -52.724 30.366  1.00 35.62  ?  376 ALA B N   1 
ATOM   6342 C  CA  . ALA B 1 376 ? 53.315 -53.728 31.346  1.00 39.29  ?  376 ALA B CA  1 
ATOM   6343 C  C   . ALA B 1 376 ? 54.343 -54.730 30.799  1.00 37.03  ?  376 ALA B C   1 
ATOM   6344 O  O   . ALA B 1 376 ? 55.194 -55.171 31.569  1.00 37.84  ?  376 ALA B O   1 
ATOM   6345 C  CB  . ALA B 1 376 ? 52.105 -54.433 31.932  1.00 40.83  ?  376 ALA B CB  1 
ATOM   6346 N  N   . ASN B 1 377 ? 54.293 -55.119 29.510  1.00 36.50  ?  377 ASN B N   1 
ATOM   6347 C  CA  . ASN B 1 377 ? 55.226 -56.140 29.024  1.00 39.66  ?  377 ASN B CA  1 
ATOM   6348 C  C   . ASN B 1 377 ? 56.340 -55.528 28.161  1.00 38.44  ?  377 ASN B C   1 
ATOM   6349 O  O   . ASN B 1 377 ? 56.941 -56.213 27.333  1.00 39.26  ?  377 ASN B O   1 
ATOM   6350 C  CB  . ASN B 1 377 ? 54.497 -57.339 28.413  1.00 38.62  ?  377 ASN B CB  1 
ATOM   6351 C  CG  . ASN B 1 377 ? 54.286 -57.246 26.925  1.00 37.31  ?  377 ASN B CG  1 
ATOM   6352 O  OD1 . ASN B 1 377 ? 54.108 -56.136 26.396  1.00 35.33  ?  377 ASN B OD1 1 
ATOM   6353 N  ND2 . ASN B 1 377 ? 54.325 -58.396 26.254  1.00 34.36  ?  377 ASN B ND2 1 
ATOM   6354 N  N   . ALA B 1 378 ? 56.695 -54.268 28.449  1.00 36.49  ?  378 ALA B N   1 
ATOM   6355 C  CA  . ALA B 1 378 ? 57.811 -53.585 27.809  1.00 33.59  ?  378 ALA B CA  1 
ATOM   6356 C  C   . ALA B 1 378 ? 59.173 -54.096 28.284  1.00 33.25  ?  378 ALA B C   1 
ATOM   6357 O  O   . ALA B 1 378 ? 60.188 -53.716 27.718  1.00 41.07  ?  378 ALA B O   1 
ATOM   6358 C  CB  . ALA B 1 378 ? 57.700 -52.093 28.064  1.00 31.13  ?  378 ALA B CB  1 
ATOM   6359 N  N   . GLY B 1 379 ? 59.225 -54.921 29.332  1.00 32.30  ?  379 GLY B N   1 
ATOM   6360 C  CA  . GLY B 1 379 ? 60.488 -55.306 29.948  1.00 29.15  ?  379 GLY B CA  1 
ATOM   6361 C  C   . GLY B 1 379 ? 61.495 -55.865 28.947  1.00 28.30  ?  379 GLY B C   1 
ATOM   6362 O  O   . GLY B 1 379 ? 62.686 -55.614 29.081  1.00 30.37  ?  379 GLY B O   1 
ATOM   6363 N  N   . GLY B 1 380 ? 61.020 -56.625 27.950  1.00 27.02  ?  380 GLY B N   1 
ATOM   6364 C  CA  . GLY B 1 380 ? 61.907 -57.246 26.982  1.00 24.59  ?  380 GLY B CA  1 
ATOM   6365 C  C   . GLY B 1 380 ? 62.412 -56.256 25.942  1.00 24.35  ?  380 GLY B C   1 
ATOM   6366 O  O   . GLY B 1 380 ? 63.520 -56.397 25.457  1.00 30.09  ?  380 GLY B O   1 
ATOM   6367 N  N   . VAL B 1 381 ? 61.582 -55.291 25.554  1.00 23.78  ?  381 VAL B N   1 
ATOM   6368 C  CA  . VAL B 1 381 ? 61.966 -54.334 24.533  1.00 24.63  ?  381 VAL B CA  1 
ATOM   6369 C  C   . VAL B 1 381 ? 62.896 -53.320 25.193  1.00 24.43  ?  381 VAL B C   1 
ATOM   6370 O  O   . VAL B 1 381 ? 63.772 -52.764 24.529  1.00 25.54  ?  381 VAL B O   1 
ATOM   6371 C  CB  . VAL B 1 381 ? 60.754 -53.677 23.832  1.00 27.03  ?  381 VAL B CB  1 
ATOM   6372 C  CG1 . VAL B 1 381 ? 59.784 -54.719 23.258  1.00 26.88  ?  381 VAL B CG1 1 
ATOM   6373 C  CG2 . VAL B 1 381 ? 59.996 -52.701 24.726  1.00 26.82  ?  381 VAL B CG2 1 
ATOM   6374 N  N   . ALA B 1 382 ? 62.714 -53.128 26.508  1.00 23.07  ?  382 ALA B N   1 
ATOM   6375 C  CA  . ALA B 1 382 ? 63.567 -52.276 27.331  1.00 23.42  ?  382 ALA B CA  1 
ATOM   6376 C  C   . ALA B 1 382 ? 65.007 -52.790 27.335  1.00 25.88  ?  382 ALA B C   1 
ATOM   6377 O  O   . ALA B 1 382 ? 65.991 -52.024 27.277  1.00 23.29  ?  382 ALA B O   1 
ATOM   6378 C  CB  . ALA B 1 382 ? 63.025 -52.242 28.741  1.00 22.91  ?  382 ALA B CB  1 
ATOM   6379 N  N   . VAL B 1 383 ? 65.104 -54.121 27.436  1.00 27.78  ?  383 VAL B N   1 
ATOM   6380 C  CA  . VAL B 1 383 ? 66.391 -54.763 27.601  1.00 27.22  ?  383 VAL B CA  1 
ATOM   6381 C  C   . VAL B 1 383 ? 67.028 -54.852 26.222  1.00 25.41  ?  383 VAL B C   1 
ATOM   6382 O  O   . VAL B 1 383 ? 68.246 -54.716 26.105  1.00 24.90  ?  383 VAL B O   1 
ATOM   6383 C  CB  . VAL B 1 383 ? 66.264 -56.099 28.356  1.00 28.22  ?  383 VAL B CB  1 
ATOM   6384 C  CG1 . VAL B 1 383 ? 67.532 -56.936 28.274  1.00 29.59  ?  383 VAL B CG1 1 
ATOM   6385 C  CG2 . VAL B 1 383 ? 65.911 -55.853 29.826  1.00 27.93  ?  383 VAL B CG2 1 
ATOM   6386 N  N   . SER B 1 384 ? 66.185 -54.970 25.186  1.00 24.15  ?  384 SER B N   1 
ATOM   6387 C  CA  . SER B 1 384 ? 66.661 -54.847 23.817  1.00 23.78  ?  384 SER B CA  1 
ATOM   6388 C  C   . SER B 1 384 ? 67.387 -53.518 23.707  1.00 21.71  ?  384 SER B C   1 
ATOM   6389 O  O   . SER B 1 384 ? 68.492 -53.466 23.159  1.00 20.89  ?  384 SER B O   1 
ATOM   6390 C  CB  . SER B 1 384 ? 65.558 -54.928 22.794  1.00 24.42  ?  384 SER B CB  1 
ATOM   6391 O  OG  . SER B 1 384 ? 64.895 -53.673 22.683  1.00 25.29  ?  384 SER B OG  1 
ATOM   6392 N  N   . GLY B 1 385 ? 66.738 -52.482 24.267  1.00 20.49  ?  385 GLY B N   1 
ATOM   6393 C  CA  . GLY B 1 385 ? 67.262 -51.122 24.323  1.00 20.89  ?  385 GLY B CA  1 
ATOM   6394 C  C   . GLY B 1 385 ? 68.647 -51.045 24.974  1.00 22.69  ?  385 GLY B C   1 
ATOM   6395 O  O   . GLY B 1 385 ? 69.543 -50.381 24.424  1.00 18.92  ?  385 GLY B O   1 
ATOM   6396 N  N   . LEU B 1 386 ? 68.798 -51.770 26.112  1.00 23.39  ?  386 LEU B N   1 
ATOM   6397 C  CA  . LEU B 1 386 ? 70.028 -51.838 26.901  1.00 23.71  ?  386 LEU B CA  1 
ATOM   6398 C  C   . LEU B 1 386 ? 71.069 -52.782 26.292  1.00 23.67  ?  386 LEU B C   1 
ATOM   6399 O  O   . LEU B 1 386 ? 72.268 -52.674 26.573  1.00 22.87  ?  386 LEU B O   1 
ATOM   6400 C  CB  . LEU B 1 386 ? 69.706 -52.291 28.323  1.00 26.74  ?  386 LEU B CB  1 
ATOM   6401 C  CG  . LEU B 1 386 ? 68.612 -51.514 29.069  1.00 28.78  ?  386 LEU B CG  1 
ATOM   6402 C  CD1 . LEU B 1 386 ? 68.369 -52.141 30.417  1.00 28.98  ?  386 LEU B CD1 1 
ATOM   6403 C  CD2 . LEU B 1 386 ? 68.932 -50.044 29.236  1.00 29.16  ?  386 LEU B CD2 1 
ATOM   6404 N  N   . GLU B 1 387 ? 70.629 -53.745 25.475  1.00 24.13  ?  387 GLU B N   1 
ATOM   6405 C  CA  . GLU B 1 387 ? 71.571 -54.533 24.694  1.00 22.53  ?  387 GLU B CA  1 
ATOM   6406 C  C   . GLU B 1 387 ? 72.204 -53.619 23.636  1.00 23.90  ?  387 GLU B C   1 
ATOM   6407 O  O   . GLU B 1 387 ? 73.430 -53.619 23.424  1.00 23.53  ?  387 GLU B O   1 
ATOM   6408 C  CB  . GLU B 1 387 ? 70.842 -55.743 24.123  1.00 22.17  ?  387 GLU B CB  1 
ATOM   6409 C  CG  . GLU B 1 387 ? 71.798 -56.748 23.491  1.00 23.52  ?  387 GLU B CG  1 
ATOM   6410 C  CD  . GLU B 1 387 ? 71.150 -57.978 22.884  1.00 25.04  ?  387 GLU B CD  1 
ATOM   6411 O  OE1 . GLU B 1 387 ? 69.991 -58.343 23.199  1.00 26.80  ?  387 GLU B OE1 1 
ATOM   6412 O  OE2 . GLU B 1 387 ? 71.829 -58.549 22.021  1.00 27.44  -1 387 GLU B OE2 1 
ATOM   6413 N  N   . MET B 1 388 ? 71.351 -52.802 22.996  1.00 22.72  ?  388 MET B N   1 
ATOM   6414 C  CA  . MET B 1 388 ? 71.817 -51.747 22.104  1.00 22.40  ?  388 MET B CA  1 
ATOM   6415 C  C   . MET B 1 388 ? 72.843 -50.857 22.815  1.00 19.91  ?  388 MET B C   1 
ATOM   6416 O  O   . MET B 1 388 ? 73.926 -50.638 22.280  1.00 17.48  ?  388 MET B O   1 
ATOM   6417 C  CB  . MET B 1 388 ? 70.644 -50.875 21.631  1.00 22.10  ?  388 MET B CB  1 
ATOM   6418 C  CG  . MET B 1 388 ? 70.028 -51.303 20.324  1.00 21.76  ?  388 MET B CG  1 
ATOM   6419 S  SD  . MET B 1 388 ? 68.787 -50.102 19.814  1.00 20.48  ?  388 MET B SD  1 
ATOM   6420 C  CE  . MET B 1 388 ? 67.311 -50.840 20.511  1.00 22.09  ?  388 MET B CE  1 
ATOM   6421 N  N   . ALA B 1 389 ? 72.462 -50.333 23.994  1.00 18.12  ?  389 ALA B N   1 
ATOM   6422 C  CA  . ALA B 1 389 ? 73.301 -49.435 24.770  1.00 18.90  ?  389 ALA B CA  1 
ATOM   6423 C  C   . ALA B 1 389 ? 74.638 -50.089 25.125  1.00 20.35  ?  389 ALA B C   1 
ATOM   6424 O  O   . ALA B 1 389 ? 75.680 -49.438 25.133  1.00 19.15  ?  389 ALA B O   1 
ATOM   6425 C  CB  . ALA B 1 389 ? 72.567 -49.006 26.017  1.00 18.97  ?  389 ALA B CB  1 
ATOM   6426 N  N   . GLN B 1 390 ? 74.606 -51.388 25.429  1.00 22.37  ?  390 GLN B N   1 
ATOM   6427 C  CA  . GLN B 1 390 ? 75.824 -52.093 25.799  1.00 24.39  ?  390 GLN B CA  1 
ATOM   6428 C  C   . GLN B 1 390 ? 76.745 -52.238 24.594  1.00 24.80  ?  390 GLN B C   1 
ATOM   6429 O  O   . GLN B 1 390 ? 77.941 -52.005 24.732  1.00 27.39  ?  390 GLN B O   1 
ATOM   6430 C  CB  . GLN B 1 390 ? 75.503 -53.441 26.442  1.00 24.27  ?  390 GLN B CB  1 
ATOM   6431 C  CG  . GLN B 1 390 ? 75.054 -53.254 27.879  1.00 25.96  ?  390 GLN B CG  1 
ATOM   6432 C  CD  . GLN B 1 390 ? 74.583 -54.512 28.553  1.00 26.11  ?  390 GLN B CD  1 
ATOM   6433 O  OE1 . GLN B 1 390 ? 75.336 -55.467 28.732  1.00 30.50  ?  390 GLN B OE1 1 
ATOM   6434 N  NE2 . GLN B 1 390 ? 73.360 -54.475 29.041  1.00 26.59  ?  390 GLN B NE2 1 
ATOM   6435 N  N   . ASN B 1 391 ? 76.189 -52.669 23.451  1.00 22.97  ?  391 ASN B N   1 
ATOM   6436 C  CA  . ASN B 1 391 ? 76.965 -52.835 22.236  1.00 22.22  ?  391 ASN B CA  1 
ATOM   6437 C  C   . ASN B 1 391 ? 77.735 -51.549 21.951  1.00 22.28  ?  391 ASN B C   1 
ATOM   6438 O  O   . ASN B 1 391 ? 78.923 -51.571 21.673  1.00 19.58  ?  391 ASN B O   1 
ATOM   6439 C  CB  . ASN B 1 391 ? 76.083 -53.193 21.047  1.00 23.28  ?  391 ASN B CB  1 
ATOM   6440 C  CG  . ASN B 1 391 ? 75.394 -54.542 21.132  1.00 23.42  ?  391 ASN B CG  1 
ATOM   6441 O  OD1 . ASN B 1 391 ? 74.467 -54.805 20.351  1.00 24.74  ?  391 ASN B OD1 1 
ATOM   6442 N  ND2 . ASN B 1 391 ? 75.803 -55.413 22.040  1.00 22.57  ?  391 ASN B ND2 1 
ATOM   6443 N  N   . SER B 1 392 ? 77.046 -50.418 22.093  1.00 25.97  ?  392 SER B N   1 
ATOM   6444 C  CA  . SER B 1 392 ? 77.573 -49.119 21.716  1.00 28.22  ?  392 SER B CA  1 
ATOM   6445 C  C   . SER B 1 392 ? 78.708 -48.706 22.669  1.00 29.11  ?  392 SER B C   1 
ATOM   6446 O  O   . SER B 1 392 ? 79.797 -48.387 22.197  1.00 32.42  ?  392 SER B O   1 
ATOM   6447 C  CB  . SER B 1 392 ? 76.417 -48.141 21.670  1.00 28.62  ?  392 SER B CB  1 
ATOM   6448 O  OG  . SER B 1 392 ? 76.819 -46.860 21.214  1.00 34.43  ?  392 SER B OG  1 
ATOM   6449 N  N   . ALA B 1 393 ? 78.449 -48.749 23.994  1.00 25.15  ?  393 ALA B N   1 
ATOM   6450 C  CA  . ALA B 1 393 ? 79.437 -48.657 25.066  1.00 23.83  ?  393 ALA B CA  1 
ATOM   6451 C  C   . ALA B 1 393 ? 80.672 -49.554 24.862  1.00 24.67  ?  393 ALA B C   1 
ATOM   6452 O  O   . ALA B 1 393 ? 81.760 -49.265 25.369  1.00 24.96  ?  393 ALA B O   1 
ATOM   6453 C  CB  . ALA B 1 393 ? 78.750 -49.052 26.365  1.00 24.56  ?  393 ALA B CB  1 
ATOM   6454 N  N   . ARG B 1 394 ? 80.484 -50.676 24.161  1.00 24.39  ?  394 ARG B N   1 
ATOM   6455 C  CA  . ARG B 1 394 ? 81.480 -51.720 24.010  1.00 24.75  ?  394 ARG B CA  1 
ATOM   6456 C  C   . ARG B 1 394 ? 81.706 -52.376 25.370  1.00 26.82  ?  394 ARG B C   1 
ATOM   6457 O  O   . ARG B 1 394 ? 82.860 -52.511 25.765  1.00 32.01  ?  394 ARG B O   1 
ATOM   6458 C  CB  . ARG B 1 394 ? 82.779 -51.200 23.375  1.00 22.94  ?  394 ARG B CB  1 
ATOM   6459 C  CG  . ARG B 1 394 ? 82.511 -50.308 22.176  1.00 22.42  ?  394 ARG B CG  1 
ATOM   6460 C  CD  . ARG B 1 394 ? 83.725 -50.089 21.303  1.00 23.55  ?  394 ARG B CD  1 
ATOM   6461 N  NE  . ARG B 1 394 ? 83.422 -49.475 19.998  1.00 23.81  ?  394 ARG B NE  1 
ATOM   6462 C  CZ  . ARG B 1 394 ? 83.022 -50.132 18.918  1.00 24.28  ?  394 ARG B CZ  1 
ATOM   6463 N  NH1 . ARG B 1 394 ? 82.878 -49.480 17.786  1.00 25.25  1  394 ARG B NH1 1 
ATOM   6464 N  NH2 . ARG B 1 394 ? 82.800 -51.436 18.953  1.00 24.46  ?  394 ARG B NH2 1 
ATOM   6465 N  N   . LEU B 1 395 ? 80.626 -52.797 26.063  1.00 23.55  ?  395 LEU B N   1 
ATOM   6466 C  CA  . LEU B 1 395 ? 80.754 -53.331 27.414  1.00 25.14  ?  395 LEU B CA  1 
ATOM   6467 C  C   . LEU B 1 395 ? 79.619 -54.296 27.705  1.00 28.07  ?  395 LEU B C   1 
ATOM   6468 O  O   . LEU B 1 395 ? 78.510 -54.079 27.236  1.00 32.08  ?  395 LEU B O   1 
ATOM   6469 C  CB  . LEU B 1 395 ? 80.722 -52.236 28.482  1.00 25.77  ?  395 LEU B CB  1 
ATOM   6470 C  CG  . LEU B 1 395 ? 81.890 -51.254 28.495  1.00 29.01  ?  395 LEU B CG  1 
ATOM   6471 C  CD1 . LEU B 1 395 ? 81.644 -50.184 29.539  1.00 29.31  ?  395 LEU B CD1 1 
ATOM   6472 C  CD2 . LEU B 1 395 ? 83.197 -51.983 28.750  1.00 30.80  ?  395 LEU B CD2 1 
ATOM   6473 N  N   . SER B 1 396 ? 79.880 -55.286 28.570  1.00 29.50  ?  396 SER B N   1 
ATOM   6474 C  CA  . SER B 1 396 ? 78.817 -56.076 29.161  1.00 31.99  ?  396 SER B CA  1 
ATOM   6475 C  C   . SER B 1 396 ? 78.636 -55.672 30.620  1.00 30.02  ?  396 SER B C   1 
ATOM   6476 O  O   . SER B 1 396 ? 79.498 -55.940 31.446  1.00 31.82  ?  396 SER B O   1 
ATOM   6477 C  CB  . SER B 1 396 ? 79.073 -57.563 29.039  1.00 33.79  ?  396 SER B CB  1 
ATOM   6478 O  OG  . SER B 1 396 ? 79.241 -57.917 27.677  1.00 36.15  ?  396 SER B OG  1 
ATOM   6479 N  N   . TRP B 1 397 ? 77.489 -55.051 30.900  1.00 28.93  ?  397 TRP B N   1 
ATOM   6480 C  CA  . TRP B 1 397 ? 77.028 -54.739 32.243  1.00 31.43  ?  397 TRP B CA  1 
ATOM   6481 C  C   . TRP B 1 397 ? 76.667 -56.003 33.040  1.00 32.92  ?  397 TRP B C   1 
ATOM   6482 O  O   . TRP B 1 397 ? 76.175 -56.990 32.482  1.00 31.30  ?  397 TRP B O   1 
ATOM   6483 C  CB  . TRP B 1 397 ? 75.786 -53.833 32.170  1.00 31.57  ?  397 TRP B CB  1 
ATOM   6484 C  CG  . TRP B 1 397 ? 75.933 -52.578 31.353  1.00 27.47  ?  397 TRP B CG  1 
ATOM   6485 C  CD1 . TRP B 1 397 ? 77.091 -51.993 30.954  1.00 25.05  ?  397 TRP B CD1 1 
ATOM   6486 C  CD2 . TRP B 1 397 ? 74.861 -51.741 30.869  1.00 28.65  ?  397 TRP B CD2 1 
ATOM   6487 N  NE1 . TRP B 1 397 ? 76.818 -50.859 30.245  1.00 26.87  ?  397 TRP B NE1 1 
ATOM   6488 C  CE2 . TRP B 1 397 ? 75.464 -50.666 30.183  1.00 27.43  ?  397 TRP B CE2 1 
ATOM   6489 C  CE3 . TRP B 1 397 ? 73.460 -51.783 30.957  1.00 30.18  ?  397 TRP B CE3 1 
ATOM   6490 C  CZ2 . TRP B 1 397 ? 74.721 -49.647 29.590  1.00 26.27  ?  397 TRP B CZ2 1 
ATOM   6491 C  CZ3 . TRP B 1 397 ? 72.724 -50.775 30.361  1.00 29.64  ?  397 TRP B CZ3 1 
ATOM   6492 C  CH2 . TRP B 1 397 ? 73.349 -49.722 29.688  1.00 27.56  ?  397 TRP B CH2 1 
ATOM   6493 N  N   . THR B 1 398 ? 76.808 -55.904 34.375  1.00 28.94  ?  398 THR B N   1 
ATOM   6494 C  CA  . THR B 1 398 ? 76.389 -56.943 35.297  1.00 27.87  ?  398 THR B CA  1 
ATOM   6495 C  C   . THR B 1 398 ? 74.869 -57.076 35.299  1.00 27.30  ?  398 THR B C   1 
ATOM   6496 O  O   . THR B 1 398 ? 74.167 -56.166 34.865  1.00 28.06  ?  398 THR B O   1 
ATOM   6497 C  CB  . THR B 1 398 ? 76.872 -56.574 36.693  1.00 29.02  ?  398 THR B CB  1 
ATOM   6498 O  OG1 . THR B 1 398 ? 76.178 -55.367 36.998  1.00 33.05  ?  398 THR B OG1 1 
ATOM   6499 C  CG2 . THR B 1 398 ? 78.379 -56.418 36.775  1.00 27.88  ?  398 THR B CG2 1 
ATOM   6500 N  N   . ALA B 1 399 ? 74.374 -58.190 35.860  1.00 27.33  ?  399 ALA B N   1 
ATOM   6501 C  CA  . ALA B 1 399 ? 72.943 -58.434 35.972  1.00 27.54  ?  399 ALA B CA  1 
ATOM   6502 C  C   . ALA B 1 399 ? 72.316 -57.350 36.835  1.00 27.78  ?  399 ALA B C   1 
ATOM   6503 O  O   . ALA B 1 399 ? 71.184 -56.956 36.601  1.00 29.08  ?  399 ALA B O   1 
ATOM   6504 C  CB  . ALA B 1 399 ? 72.647 -59.815 36.531  1.00 26.45  ?  399 ALA B CB  1 
ATOM   6505 N  N   . GLU B 1 400 ? 73.059 -56.891 37.846  1.00 30.10  ?  400 GLU B N   1 
ATOM   6506 C  CA  . GLU B 1 400 ? 72.583 -55.861 38.761  1.00 31.04  ?  400 GLU B CA  1 
ATOM   6507 C  C   . GLU B 1 400 ? 72.262 -54.597 37.967  1.00 28.50  ?  400 GLU B C   1 
ATOM   6508 O  O   . GLU B 1 400 ? 71.172 -54.055 38.093  1.00 22.23  ?  400 GLU B O   1 
ATOM   6509 C  CB  . GLU B 1 400 ? 73.627 -55.596 39.852  1.00 37.17  ?  400 GLU B CB  1 
ATOM   6510 C  CG  . GLU B 1 400 ? 73.752 -56.730 40.871  1.00 43.64  ?  400 GLU B CG  1 
ATOM   6511 C  CD  . GLU B 1 400 ? 74.432 -58.015 40.384  1.00 49.94  ?  400 GLU B CD  1 
ATOM   6512 O  OE1 . GLU B 1 400 ? 74.077 -59.081 40.934  1.00 49.35  ?  400 GLU B OE1 1 
ATOM   6513 O  OE2 . GLU B 1 400 ? 75.326 -57.975 39.492  1.00 47.65  -1 400 GLU B OE2 1 
ATOM   6514 N  N   . GLU B 1 401 ? 73.258 -54.158 37.175  1.00 34.09  ?  401 GLU B N   1 
ATOM   6515 C  CA  . GLU B 1 401 ? 73.207 -53.001 36.287  1.00 35.86  ?  401 GLU B CA  1 
ATOM   6516 C  C   . GLU B 1 401 ? 71.923 -53.004 35.454  1.00 34.34  ?  401 GLU B C   1 
ATOM   6517 O  O   . GLU B 1 401 ? 71.163 -52.043 35.474  1.00 39.02  ?  401 GLU B O   1 
ATOM   6518 C  CB  . GLU B 1 401 ? 74.472 -52.967 35.414  1.00 37.44  ?  401 GLU B CB  1 
ATOM   6519 C  CG  . GLU B 1 401 ? 75.522 -51.929 35.819  1.00 40.32  ?  401 GLU B CG  1 
ATOM   6520 C  CD  . GLU B 1 401 ? 77.005 -52.289 35.677  1.00 41.18  ?  401 GLU B CD  1 
ATOM   6521 O  OE1 . GLU B 1 401 ? 77.391 -53.148 34.857  1.00 41.60  ?  401 GLU B OE1 1 
ATOM   6522 O  OE2 . GLU B 1 401 ? 77.809 -51.701 36.431  1.00 37.09  -1 401 GLU B OE2 1 
ATOM   6523 N  N   . VAL B 1 402 ? 71.670 -54.097 34.737  1.00 31.78  ?  402 VAL B N   1 
ATOM   6524 C  CA  . VAL B 1 402 ? 70.592 -54.130 33.758  1.00 31.16  ?  402 VAL B CA  1 
ATOM   6525 C  C   . VAL B 1 402 ? 69.232 -54.119 34.459  1.00 30.62  ?  402 VAL B C   1 
ATOM   6526 O  O   . VAL B 1 402 ? 68.341 -53.402 34.006  1.00 30.05  ?  402 VAL B O   1 
ATOM   6527 C  CB  . VAL B 1 402 ? 70.699 -55.355 32.828  1.00 29.95  ?  402 VAL B CB  1 
ATOM   6528 C  CG1 . VAL B 1 402 ? 69.741 -55.229 31.650  1.00 31.07  ?  402 VAL B CG1 1 
ATOM   6529 C  CG2 . VAL B 1 402 ? 72.114 -55.569 32.327  1.00 28.95  ?  402 VAL B CG2 1 
ATOM   6530 N  N   . ASP B 1 403 ? 69.078 -54.967 35.506  1.00 29.43  ?  403 ASP B N   1 
ATOM   6531 C  CA  . ASP B 1 403 ? 67.862 -55.127 36.300  1.00 27.39  ?  403 ASP B CA  1 
ATOM   6532 C  C   . ASP B 1 403 ? 67.508 -53.814 36.992  1.00 27.95  ?  403 ASP B C   1 
ATOM   6533 O  O   . ASP B 1 403 ? 66.332 -53.487 37.150  1.00 27.65  ?  403 ASP B O   1 
ATOM   6534 C  CB  . ASP B 1 403 ? 68.011 -56.202 37.373  1.00 27.67  ?  403 ASP B CB  1 
ATOM   6535 C  CG  . ASP B 1 403 ? 66.723 -56.705 38.032  1.00 27.63  ?  403 ASP B CG  1 
ATOM   6536 O  OD1 . ASP B 1 403 ? 66.698 -56.861 39.284  1.00 24.53  ?  403 ASP B OD1 1 
ATOM   6537 O  OD2 . ASP B 1 403 ? 65.747 -56.968 37.288  1.00 26.43  -1 403 ASP B OD2 1 
ATOM   6538 N  N   . ALA B 1 404 ? 68.544 -53.085 37.416  1.00 27.34  ?  404 ALA B N   1 
ATOM   6539 C  CA  . ALA B 1 404 ? 68.399 -51.783 38.043  1.00 28.14  ?  404 ALA B CA  1 
ATOM   6540 C  C   . ALA B 1 404 ? 67.762 -50.799 37.077  1.00 26.89  ?  404 ALA B C   1 
ATOM   6541 O  O   . ALA B 1 404 ? 66.816 -50.096 37.429  1.00 32.34  ?  404 ALA B O   1 
ATOM   6542 C  CB  . ALA B 1 404 ? 69.761 -51.272 38.485  1.00 30.63  ?  404 ALA B CB  1 
ATOM   6543 N  N   . ARG B 1 405 ? 68.327 -50.730 35.874  1.00 23.96  ?  405 ARG B N   1 
ATOM   6544 C  CA  . ARG B 1 405 ? 67.813 -49.841 34.850  1.00 23.88  ?  405 ARG B CA  1 
ATOM   6545 C  C   . ARG B 1 405 ? 66.418 -50.263 34.413  1.00 24.88  ?  405 ARG B C   1 
ATOM   6546 O  O   . ARG B 1 405 ? 65.566 -49.399 34.198  1.00 27.54  ?  405 ARG B O   1 
ATOM   6547 C  CB  . ARG B 1 405 ? 68.737 -49.806 33.636  1.00 22.71  ?  405 ARG B CB  1 
ATOM   6548 C  CG  . ARG B 1 405 ? 69.950 -48.940 33.911  1.00 21.71  ?  405 ARG B CG  1 
ATOM   6549 C  CD  . ARG B 1 405 ? 70.898 -49.066 32.777  1.00 21.50  ?  405 ARG B CD  1 
ATOM   6550 N  NE  . ARG B 1 405 ? 72.029 -48.171 33.022  1.00 22.87  ?  405 ARG B NE  1 
ATOM   6551 C  CZ  . ARG B 1 405 ? 72.030 -46.859 32.853  1.00 23.88  ?  405 ARG B CZ  1 
ATOM   6552 N  NH1 . ARG B 1 405 ? 70.908 -46.230 32.510  1.00 24.05  1  405 ARG B NH1 1 
ATOM   6553 N  NH2 . ARG B 1 405 ? 73.170 -46.197 33.031  1.00 23.77  ?  405 ARG B NH2 1 
ATOM   6554 N  N   . LEU B 1 406 ? 66.209 -51.577 34.268  1.00 24.79  ?  406 LEU B N   1 
ATOM   6555 C  CA  . LEU B 1 406 ? 64.884 -52.100 33.972  1.00 29.54  ?  406 LEU B CA  1 
ATOM   6556 C  C   . LEU B 1 406 ? 63.878 -51.613 35.018  1.00 28.67  ?  406 LEU B C   1 
ATOM   6557 O  O   . LEU B 1 406 ? 62.796 -51.191 34.641  1.00 26.52  ?  406 LEU B O   1 
ATOM   6558 C  CB  . LEU B 1 406 ? 64.863 -53.631 33.875  1.00 33.48  ?  406 LEU B CB  1 
ATOM   6559 C  CG  . LEU B 1 406 ? 63.473 -54.276 33.702  1.00 31.80  ?  406 LEU B CG  1 
ATOM   6560 C  CD1 . LEU B 1 406 ? 62.838 -53.876 32.391  1.00 28.98  ?  406 LEU B CD1 1 
ATOM   6561 C  CD2 . LEU B 1 406 ? 63.498 -55.795 33.815  1.00 32.69  ?  406 LEU B CD2 1 
ATOM   6562 N  N   . LYS B 1 407 ? 64.240 -51.709 36.312  1.00 30.15  ?  407 LYS B N   1 
ATOM   6563 C  CA  . LYS B 1 407 ? 63.419 -51.272 37.439  1.00 29.11  ?  407 LYS B CA  1 
ATOM   6564 C  C   . LYS B 1 407 ? 63.061 -49.792 37.327  1.00 29.33  ?  407 LYS B C   1 
ATOM   6565 O  O   . LYS B 1 407 ? 61.909 -49.432 37.520  1.00 31.73  ?  407 LYS B O   1 
ATOM   6566 C  CB  . LYS B 1 407 ? 64.102 -51.487 38.797  1.00 28.58  ?  407 LYS B CB  1 
ATOM   6567 C  CG  . LYS B 1 407 ? 63.541 -52.629 39.617  1.00 30.58  ?  407 LYS B CG  1 
ATOM   6568 C  CD  . LYS B 1 407 ? 64.314 -52.962 40.886  1.00 31.95  ?  407 LYS B CD  1 
ATOM   6569 C  CE  . LYS B 1 407 ? 65.440 -53.916 40.620  1.00 34.26  ?  407 LYS B CE  1 
ATOM   6570 N  NZ  . LYS B 1 407 ? 65.895 -54.611 41.833  1.00 35.49  1  407 LYS B NZ  1 
ATOM   6571 N  N   A ASP B 1 408 ? 64.038 -48.930 37.038  0.50 31.58  ?  408 ASP B N   1 
ATOM   6572 N  N   B ASP B 1 408 ? 64.082 -48.968 37.053  0.50 27.82  ?  408 ASP B N   1 
ATOM   6573 C  CA  A ASP B 1 408 ? 63.732 -47.518 36.890  0.50 34.07  ?  408 ASP B CA  1 
ATOM   6574 C  CA  B ASP B 1 408 ? 63.946 -47.537 36.822  0.50 27.34  ?  408 ASP B CA  1 
ATOM   6575 C  C   A ASP B 1 408 ? 62.821 -47.318 35.683  0.50 33.51  ?  408 ASP B C   1 
ATOM   6576 C  C   B ASP B 1 408 ? 62.966 -47.274 35.674  0.50 29.70  ?  408 ASP B C   1 
ATOM   6577 O  O   A ASP B 1 408 ? 61.911 -46.494 35.741  0.50 34.38  ?  408 ASP B O   1 
ATOM   6578 O  O   B ASP B 1 408 ? 62.157 -46.354 35.761  0.50 30.58  ?  408 ASP B O   1 
ATOM   6579 C  CB  A ASP B 1 408 ? 64.965 -46.638 36.773  0.50 37.76  ?  408 ASP B CB  1 
ATOM   6580 C  CB  B ASP B 1 408 ? 65.310 -46.896 36.569  0.50 25.20  ?  408 ASP B CB  1 
ATOM   6581 C  CG  A ASP B 1 408 ? 64.673 -45.143 36.858  0.50 41.32  ?  408 ASP B CG  1 
ATOM   6582 C  CG  B ASP B 1 408 ? 66.053 -46.315 37.774  0.50 23.06  ?  408 ASP B CG  1 
ATOM   6583 O  OD1 A ASP B 1 408 ? 64.327 -44.665 37.971  0.50 37.96  ?  408 ASP B OD1 1 
ATOM   6584 O  OD1 B ASP B 1 408 ? 65.670 -46.613 38.917  0.50 22.46  ?  408 ASP B OD1 1 
ATOM   6585 O  OD2 A ASP B 1 408 ? 64.767 -44.467 35.803  0.50 43.89  -1 408 ASP B OD2 1 
ATOM   6586 O  OD2 B ASP B 1 408 ? 67.000 -45.524 37.568  0.50 20.39  -1 408 ASP B OD2 1 
ATOM   6587 N  N   . ILE B 1 409 ? 63.055 -48.090 34.610  1.00 32.47  ?  409 ILE B N   1 
ATOM   6588 C  CA  . ILE B 1 409 ? 62.308 -47.920 33.366  1.00 32.49  ?  409 ILE B CA  1 
ATOM   6589 C  C   . ILE B 1 409 ? 60.838 -48.298 33.522  1.00 32.13  ?  409 ILE B C   1 
ATOM   6590 O  O   . ILE B 1 409 ? 59.998 -47.633 32.930  1.00 35.63  ?  409 ILE B O   1 
ATOM   6591 C  CB  . ILE B 1 409 ? 62.967 -48.689 32.199  1.00 31.96  ?  409 ILE B CB  1 
ATOM   6592 C  CG1 . ILE B 1 409 ? 64.255 -47.982 31.739  1.00 30.13  ?  409 ILE B CG1 1 
ATOM   6593 C  CG2 . ILE B 1 409 ? 61.988 -48.886 31.032  1.00 31.86  ?  409 ILE B CG2 1 
ATOM   6594 C  CD1 . ILE B 1 409 ? 64.859 -48.536 30.462  1.00 30.12  ?  409 ILE B CD1 1 
ATOM   6595 N  N   . MET B 1 410 ? 60.539 -49.338 34.310  1.00 34.46  ?  410 MET B N   1 
ATOM   6596 C  CA  . MET B 1 410 ? 59.169 -49.809 34.503  1.00 37.26  ?  410 MET B CA  1 
ATOM   6597 C  C   . MET B 1 410 ? 58.396 -48.896 35.470  1.00 36.78  ?  410 MET B C   1 
ATOM   6598 O  O   . MET B 1 410 ? 57.193 -48.743 35.326  1.00 38.42  ?  410 MET B O   1 
ATOM   6599 C  CB  . MET B 1 410 ? 59.115 -51.279 34.974  1.00 36.55  ?  410 MET B CB  1 
ATOM   6600 C  CG  . MET B 1 410 ? 59.598 -52.364 33.962  1.00 35.32  ?  410 MET B CG  1 
ATOM   6601 S  SD  . MET B 1 410 ? 58.760 -52.549 32.359  1.00 34.18  ?  410 MET B SD  1 
ATOM   6602 C  CE  . MET B 1 410 ? 59.654 -51.273 31.470  1.00 38.31  ?  410 MET B CE  1 
ATOM   6603 N  N   . LYS B 1 411 ? 59.064 -48.281 36.453  1.00 36.83  ?  411 LYS B N   1 
ATOM   6604 C  CA  . LYS B 1 411 ? 58.403 -47.394 37.405  1.00 34.49  ?  411 LYS B CA  1 
ATOM   6605 C  C   . LYS B 1 411 ? 57.940 -46.153 36.645  1.00 37.24  ?  411 LYS B C   1 
ATOM   6606 O  O   . LYS B 1 411 ? 56.822 -45.662 36.817  1.00 37.75  ?  411 LYS B O   1 
ATOM   6607 C  CB  . LYS B 1 411 ? 59.357 -47.117 38.580  1.00 32.34  ?  411 LYS B CB  1 
ATOM   6608 C  CG  . LYS B 1 411 ? 59.062 -45.903 39.439  1.00 36.37  ?  411 LYS B CG  1 
ATOM   6609 C  CD  . LYS B 1 411 ? 59.657 -44.603 38.882  1.00 42.76  ?  411 LYS B CD  1 
ATOM   6610 C  CE  . LYS B 1 411 ? 59.107 -43.318 39.455  1.00 43.86  ?  411 LYS B CE  1 
ATOM   6611 N  NZ  . LYS B 1 411 ? 57.718 -43.046 39.078  1.00 42.82  1  411 LYS B NZ  1 
ATOM   6612 N  N   . SER B 1 412 ? 58.826 -45.660 35.777  1.00 39.81  ?  412 SER B N   1 
ATOM   6613 C  CA  . SER B 1 412 ? 58.602 -44.423 35.046  1.00 40.03  ?  412 SER B CA  1 
ATOM   6614 C  C   . SER B 1 412 ? 57.511 -44.630 34.012  1.00 35.00  ?  412 SER B C   1 
ATOM   6615 O  O   . SER B 1 412 ? 56.786 -43.703 33.678  1.00 34.99  ?  412 SER B O   1 
ATOM   6616 C  CB  . SER B 1 412 ? 59.871 -43.978 34.401  1.00 45.28  ?  412 SER B CB  1 
ATOM   6617 O  OG  . SER B 1 412 ? 60.924 -44.048 35.359  1.00 53.78  ?  412 SER B OG  1 
ATOM   6618 N  N   . CYS B 1 413 ? 57.419 -45.862 33.508  1.00 31.68  ?  413 CYS B N   1 
ATOM   6619 C  CA  . CYS B 1 413 ? 56.338 -46.210 32.611  1.00 28.58  ?  413 CYS B CA  1 
ATOM   6620 C  C   . CYS B 1 413 ? 55.009 -46.040 33.343  1.00 27.69  ?  413 CYS B C   1 
ATOM   6621 O  O   . CYS B 1 413 ? 54.225 -45.153 33.027  1.00 27.76  ?  413 CYS B O   1 
ATOM   6622 C  CB  . CYS B 1 413 ? 56.516 -47.619 32.085  1.00 26.80  ?  413 CYS B CB  1 
ATOM   6623 S  SG  . CYS B 1 413 ? 55.201 -48.022 30.921  1.00 25.56  ?  413 CYS B SG  1 
ATOM   6624 N  N   . PHE B 1 414 ? 54.801 -46.873 34.364  1.00 27.96  ?  414 PHE B N   1 
ATOM   6625 C  CA  . PHE B 1 414 ? 53.609 -46.833 35.192  1.00 27.81  ?  414 PHE B CA  1 
ATOM   6626 C  C   . PHE B 1 414 ? 53.218 -45.379 35.467  1.00 31.41  ?  414 PHE B C   1 
ATOM   6627 O  O   . PHE B 1 414 ? 52.079 -44.989 35.193  1.00 31.13  ?  414 PHE B O   1 
ATOM   6628 C  CB  . PHE B 1 414 ? 53.835 -47.615 36.490  1.00 24.12  ?  414 PHE B CB  1 
ATOM   6629 C  CG  . PHE B 1 414 ? 52.655 -47.520 37.439  1.00 22.36  ?  414 PHE B CG  1 
ATOM   6630 C  CD1 . PHE B 1 414 ? 51.615 -48.449 37.364  1.00 21.96  ?  414 PHE B CD1 1 
ATOM   6631 C  CD2 . PHE B 1 414 ? 52.589 -46.514 38.409  1.00 20.94  ?  414 PHE B CD2 1 
ATOM   6632 C  CE1 . PHE B 1 414 ? 50.539 -48.373 38.250  1.00 20.97  ?  414 PHE B CE1 1 
ATOM   6633 C  CE2 . PHE B 1 414 ? 51.506 -46.441 39.287  1.00 19.68  ?  414 PHE B CE2 1 
ATOM   6634 C  CZ  . PHE B 1 414 ? 50.482 -47.356 39.195  1.00 19.93  ?  414 PHE B CZ  1 
ATOM   6635 N  N   . GLN B 1 415 ? 54.162 -44.584 36.009  1.00 32.60  ?  415 GLN B N   1 
ATOM   6636 C  CA  . GLN B 1 415 ? 53.856 -43.225 36.436  1.00 32.17  ?  415 GLN B CA  1 
ATOM   6637 C  C   . GLN B 1 415 ? 53.324 -42.421 35.240  1.00 29.81  ?  415 GLN B C   1 
ATOM   6638 O  O   . GLN B 1 415 ? 52.363 -41.674 35.395  1.00 27.48  ?  415 GLN B O   1 
ATOM   6639 C  CB  . GLN B 1 415 ? 55.045 -42.603 37.170  1.00 31.38  ?  415 GLN B CB  1 
ATOM   6640 C  CG  . GLN B 1 415 ? 54.774 -41.231 37.787  1.00 35.79  ?  415 GLN B CG  1 
ATOM   6641 C  CD  . GLN B 1 415 ? 54.014 -41.245 39.107  1.00 45.21  ?  415 GLN B CD  1 
ATOM   6642 O  OE1 . GLN B 1 415 ? 52.969 -40.589 39.281  1.00 41.63  ?  415 GLN B OE1 1 
ATOM   6643 N  NE2 . GLN B 1 415 ? 54.563 -41.965 40.083  1.00 46.96  ?  415 GLN B NE2 1 
ATOM   6644 N  N   . ASN B 1 416 ? 53.907 -42.617 34.051  1.00 30.28  ?  416 ASN B N   1 
ATOM   6645 C  CA  . ASN B 1 416 ? 53.574 -41.827 32.869  1.00 35.68  ?  416 ASN B CA  1 
ATOM   6646 C  C   . ASN B 1 416 ? 52.142 -42.085 32.419  1.00 34.96  ?  416 ASN B C   1 
ATOM   6647 O  O   . ASN B 1 416 ? 51.480 -41.190 31.913  1.00 34.05  ?  416 ASN B O   1 
ATOM   6648 C  CB  . ASN B 1 416 ? 54.491 -42.128 31.685  1.00 40.25  ?  416 ASN B CB  1 
ATOM   6649 C  CG  . ASN B 1 416 ? 54.361 -41.141 30.541  1.00 41.31  ?  416 ASN B CG  1 
ATOM   6650 O  OD1 . ASN B 1 416 ? 53.772 -40.064 30.700  1.00 37.64  ?  416 ASN B OD1 1 
ATOM   6651 N  ND2 . ASN B 1 416 ? 54.911 -41.485 29.382  1.00 39.29  ?  416 ASN B ND2 1 
ATOM   6652 N  N   . GLY B 1 417 ? 51.679 -43.320 32.580  1.00 35.81  ?  417 GLY B N   1 
ATOM   6653 C  CA  . GLY B 1 417 ? 50.310 -43.661 32.241  1.00 35.85  ?  417 GLY B CA  1 
ATOM   6654 C  C   . GLY B 1 417 ? 49.329 -43.129 33.278  1.00 35.83  ?  417 GLY B C   1 
ATOM   6655 O  O   . GLY B 1 417 ? 48.285 -42.585 32.917  1.00 46.26  ?  417 GLY B O   1 
ATOM   6656 N  N   . LEU B 1 418 ? 49.667 -43.325 34.561  1.00 33.28  ?  418 LEU B N   1 
ATOM   6657 C  CA  . LEU B 1 418 ? 48.901 -42.795 35.687  1.00 30.65  ?  418 LEU B CA  1 
ATOM   6658 C  C   . LEU B 1 418 ? 48.622 -41.305 35.457  1.00 31.74  ?  418 LEU B C   1 
ATOM   6659 O  O   . LEU B 1 418 ? 47.499 -40.932 35.134  1.00 28.25  ?  418 LEU B O   1 
ATOM   6660 C  CB  . LEU B 1 418 ? 49.721 -43.049 36.961  1.00 29.61  ?  418 LEU B CB  1 
ATOM   6661 C  CG  . LEU B 1 418 ? 48.974 -43.324 38.272  1.00 30.46  ?  418 LEU B CG  1 
ATOM   6662 C  CD1 . LEU B 1 418 ? 49.146 -42.242 39.317  1.00 29.20  ?  418 LEU B CD1 1 
ATOM   6663 C  CD2 . LEU B 1 418 ? 47.498 -43.621 38.062  1.00 33.99  ?  418 LEU B CD2 1 
ATOM   6664 N  N   . ASP B 1 419 ? 49.690 -40.484 35.518  1.00 35.18  ?  419 ASP B N   1 
ATOM   6665 C  CA  . ASP B 1 419 ? 49.640 -39.026 35.511  1.00 35.87  ?  419 ASP B CA  1 
ATOM   6666 C  C   . ASP B 1 419 ? 48.994 -38.479 34.230  1.00 41.14  ?  419 ASP B C   1 
ATOM   6667 O  O   . ASP B 1 419 ? 48.332 -37.427 34.269  1.00 44.51  ?  419 ASP B O   1 
ATOM   6668 C  CB  . ASP B 1 419 ? 51.036 -38.448 35.699  1.00 34.24  ?  419 ASP B CB  1 
ATOM   6669 C  CG  . ASP B 1 419 ? 51.761 -38.844 36.980  1.00 33.80  ?  419 ASP B CG  1 
ATOM   6670 O  OD1 . ASP B 1 419 ? 51.126 -39.468 37.864  1.00 30.39  ?  419 ASP B OD1 1 
ATOM   6671 O  OD2 . ASP B 1 419 ? 52.964 -38.524 37.084  1.00 34.26  -1 419 ASP B OD2 1 
ATOM   6672 N  N   . THR B 1 420 ? 49.205 -39.169 33.092  1.00 37.08  ?  420 THR B N   1 
ATOM   6673 C  CA  . THR B 1 420 ? 48.577 -38.763 31.839  1.00 36.32  ?  420 THR B CA  1 
ATOM   6674 C  C   . THR B 1 420 ? 47.067 -38.957 31.968  1.00 36.10  ?  420 THR B C   1 
ATOM   6675 O  O   . THR B 1 420 ? 46.306 -37.991 31.844  1.00 36.83  ?  420 THR B O   1 
ATOM   6676 C  CB  . THR B 1 420 ? 49.150 -39.487 30.616  1.00 30.08  ?  420 THR B CB  1 
ATOM   6677 O  OG1 . THR B 1 420 ? 50.487 -39.012 30.488  1.00 29.05  ?  420 THR B OG1 1 
ATOM   6678 C  CG2 . THR B 1 420 ? 48.435 -39.123 29.328  1.00 26.94  ?  420 THR B CG2 1 
ATOM   6679 N  N   . ALA B 1 421 ? 46.663 -40.194 32.267  1.00 32.51  ?  421 ALA B N   1 
ATOM   6680 C  CA  . ALA B 1 421 ? 45.262 -40.509 32.464  1.00 35.25  ?  421 ALA B CA  1 
ATOM   6681 C  C   . ALA B 1 421 ? 44.600 -39.524 33.429  1.00 37.40  ?  421 ALA B C   1 
ATOM   6682 O  O   . ALA B 1 421 ? 43.439 -39.177 33.235  1.00 39.08  ?  421 ALA B O   1 
ATOM   6683 C  CB  . ALA B 1 421 ? 45.149 -41.921 32.965  1.00 36.75  ?  421 ALA B CB  1 
ATOM   6684 N  N   . LYS B 1 422 ? 45.336 -39.088 34.466  1.00 39.21  ?  422 LYS B N   1 
ATOM   6685 C  CA  . LYS B 1 422 ? 44.821 -38.142 35.445  1.00 40.54  ?  422 LYS B CA  1 
ATOM   6686 C  C   . LYS B 1 422 ? 44.687 -36.748 34.837  1.00 42.49  ?  422 LYS B C   1 
ATOM   6687 O  O   . LYS B 1 422 ? 44.018 -35.899 35.426  1.00 54.02  ?  422 LYS B O   1 
ATOM   6688 C  CB  . LYS B 1 422 ? 45.690 -38.029 36.701  1.00 38.86  ?  422 LYS B CB  1 
ATOM   6689 C  CG  . LYS B 1 422 ? 45.545 -39.178 37.683  1.00 39.75  ?  422 LYS B CG  1 
ATOM   6690 C  CD  . LYS B 1 422 ? 46.169 -38.936 39.050  1.00 39.57  ?  422 LYS B CD  1 
ATOM   6691 C  CE  . LYS B 1 422 ? 47.457 -38.190 38.937  1.00 43.74  ?  422 LYS B CE  1 
ATOM   6692 N  NZ  . LYS B 1 422 ? 48.278 -38.284 40.143  1.00 48.06  1  422 LYS B NZ  1 
ATOM   6693 N  N   . GLU B 1 423 ? 45.345 -36.507 33.694  1.00 39.46  ?  423 GLU B N   1 
ATOM   6694 C  CA  . GLU B 1 423 ? 45.240 -35.227 33.012  1.00 39.76  ?  423 GLU B CA  1 
ATOM   6695 C  C   . GLU B 1 423 ? 44.116 -35.266 31.982  1.00 37.75  ?  423 GLU B C   1 
ATOM   6696 O  O   . GLU B 1 423 ? 43.307 -34.349 31.931  1.00 41.67  ?  423 GLU B O   1 
ATOM   6697 C  CB  . GLU B 1 423 ? 46.554 -34.843 32.335  1.00 40.95  ?  423 GLU B CB  1 
ATOM   6698 C  CG  . GLU B 1 423 ? 46.617 -33.371 31.928  1.00 41.73  ?  423 GLU B CG  1 
ATOM   6699 C  CD  . GLU B 1 423 ? 47.016 -32.395 33.028  1.00 43.96  ?  423 GLU B CD  1 
ATOM   6700 O  OE1 . GLU B 1 423 ? 46.193 -31.568 33.516  1.00 42.52  ?  423 GLU B OE1 1 
ATOM   6701 O  OE2 . GLU B 1 423 ? 48.214 -32.454 33.379  1.00 44.37  -1 423 GLU B OE2 1 
ATOM   6702 N  N   . TYR B 1 424 ? 44.059 -36.336 31.186  1.00 35.99  ?  424 TYR B N   1 
ATOM   6703 C  CA  . TYR B 1 424 ? 43.241 -36.368 29.980  1.00 36.51  ?  424 TYR B CA  1 
ATOM   6704 C  C   . TYR B 1 424 ? 42.002 -37.270 30.105  1.00 35.92  ?  424 TYR B C   1 
ATOM   6705 O  O   . TYR B 1 424 ? 40.981 -36.968 29.474  1.00 36.54  ?  424 TYR B O   1 
ATOM   6706 C  CB  . TYR B 1 424 ? 44.142 -36.789 28.816  1.00 35.93  ?  424 TYR B CB  1 
ATOM   6707 C  CG  . TYR B 1 424 ? 45.183 -35.744 28.443  1.00 37.82  ?  424 TYR B CG  1 
ATOM   6708 C  CD1 . TYR B 1 424 ? 46.497 -35.866 28.873  1.00 40.97  ?  424 TYR B CD1 1 
ATOM   6709 C  CD2 . TYR B 1 424 ? 44.857 -34.637 27.663  1.00 38.20  ?  424 TYR B CD2 1 
ATOM   6710 C  CE1 . TYR B 1 424 ? 47.454 -34.917 28.548  1.00 40.76  ?  424 TYR B CE1 1 
ATOM   6711 C  CE2 . TYR B 1 424 ? 45.811 -33.696 27.313  1.00 38.65  ?  424 TYR B CE2 1 
ATOM   6712 C  CZ  . TYR B 1 424 ? 47.113 -33.830 27.767  1.00 38.50  ?  424 TYR B CZ  1 
ATOM   6713 O  OH  . TYR B 1 424 ? 48.093 -32.927 27.471  1.00 40.15  ?  424 TYR B OH  1 
ATOM   6714 N  N   . ALA B 1 425 ? 42.104 -38.378 30.870  1.00 33.87  ?  425 ALA B N   1 
ATOM   6715 C  CA  . ALA B 1 425 ? 40.987 -39.269 31.190  1.00 32.00  ?  425 ALA B CA  1 
ATOM   6716 C  C   . ALA B 1 425 ? 40.659 -39.211 32.685  1.00 34.46  ?  425 ALA B C   1 
ATOM   6717 O  O   . ALA B 1 425 ? 40.330 -40.242 33.280  1.00 36.15  ?  425 ALA B O   1 
ATOM   6718 C  CB  . ALA B 1 425 ? 41.327 -40.688 30.782  1.00 31.15  ?  425 ALA B CB  1 
ATOM   6719 N  N   . THR B 1 426 ? 40.759 -37.993 33.259  1.00 35.52  ?  426 THR B N   1 
ATOM   6720 C  CA  . THR B 1 426 ? 40.546 -37.689 34.665  1.00 36.04  ?  426 THR B CA  1 
ATOM   6721 C  C   . THR B 1 426 ? 39.360 -38.498 35.192  1.00 42.65  ?  426 THR B C   1 
ATOM   6722 O  O   . THR B 1 426 ? 38.217 -38.230 34.809  1.00 36.84  ?  426 THR B O   1 
ATOM   6723 C  CB  . THR B 1 426 ? 40.270 -36.193 34.851  1.00 35.96  ?  426 THR B CB  1 
ATOM   6724 O  OG1 . THR B 1 426 ? 41.205 -35.343 34.198  1.00 34.99  ?  426 THR B OG1 1 
ATOM   6725 C  CG2 . THR B 1 426 ? 40.310 -35.796 36.314  1.00 38.71  ?  426 THR B CG2 1 
ATOM   6726 N  N   . PRO B 1 427 ? 39.595 -39.484 36.100  1.00 45.90  ?  427 PRO B N   1 
ATOM   6727 C  CA  . PRO B 1 427 ? 38.517 -40.307 36.661  1.00 43.49  ?  427 PRO B CA  1 
ATOM   6728 C  C   . PRO B 1 427 ? 37.643 -39.597 37.699  1.00 45.90  ?  427 PRO B C   1 
ATOM   6729 O  O   . PRO B 1 427 ? 37.926 -38.482 38.118  1.00 51.72  ?  427 PRO B O   1 
ATOM   6730 C  CB  . PRO B 1 427 ? 39.303 -41.474 37.268  1.00 43.60  ?  427 PRO B CB  1 
ATOM   6731 C  CG  . PRO B 1 427 ? 40.589 -40.841 37.734  1.00 45.36  ?  427 PRO B CG  1 
ATOM   6732 C  CD  . PRO B 1 427 ? 40.920 -39.836 36.641  1.00 46.00  ?  427 PRO B CD  1 
ATOM   6733 N  N   . ALA B 1 428 ? 36.549 -40.254 38.083  1.00 48.92  ?  428 ALA B N   1 
ATOM   6734 C  CA  . ALA B 1 428 ? 35.648 -39.767 39.114  1.00 46.83  ?  428 ALA B CA  1 
ATOM   6735 C  C   . ALA B 1 428 ? 36.208 -40.094 40.501  1.00 52.26  ?  428 ALA B C   1 
ATOM   6736 O  O   . ALA B 1 428 ? 36.989 -41.034 40.642  1.00 50.68  ?  428 ALA B O   1 
ATOM   6737 C  CB  . ALA B 1 428 ? 34.286 -40.390 38.911  1.00 41.26  ?  428 ALA B CB  1 
ATOM   6738 N  N   . ASP B 1 429 ? 35.779 -39.314 41.511  1.00 50.93  ?  429 ASP B N   1 
ATOM   6739 C  CA  . ASP B 1 429 ? 36.145 -39.495 42.911  1.00 50.24  ?  429 ASP B CA  1 
ATOM   6740 C  C   . ASP B 1 429 ? 36.369 -40.976 43.207  1.00 45.11  ?  429 ASP B C   1 
ATOM   6741 O  O   . ASP B 1 429 ? 35.450 -41.778 43.069  1.00 45.53  ?  429 ASP B O   1 
ATOM   6742 C  CB  . ASP B 1 429 ? 35.083 -38.900 43.834  1.00 52.95  ?  429 ASP B CB  1 
ATOM   6743 C  CG  . ASP B 1 429 ? 35.397 -38.888 45.330  1.00 56.22  ?  429 ASP B CG  1 
ATOM   6744 O  OD1 . ASP B 1 429 ? 36.127 -37.969 45.771  1.00 57.56  ?  429 ASP B OD1 1 
ATOM   6745 O  OD2 . ASP B 1 429 ? 34.907 -39.792 46.055  1.00 54.02  -1 429 ASP B OD2 1 
ATOM   6746 N  N   . GLY B 1 430 ? 37.613 -41.321 43.566  1.00 45.20  ?  430 GLY B N   1 
ATOM   6747 C  CA  . GLY B 1 430 ? 37.987 -42.640 44.068  1.00 44.35  ?  430 GLY B CA  1 
ATOM   6748 C  C   . GLY B 1 430 ? 38.091 -43.724 42.993  1.00 43.98  ?  430 GLY B C   1 
ATOM   6749 O  O   . GLY B 1 430 ? 38.442 -44.851 43.326  1.00 46.50  ?  430 GLY B O   1 
ATOM   6750 N  N   . ILE B 1 431 ? 37.790 -43.393 41.725  1.00 42.64  ?  431 ILE B N   1 
ATOM   6751 C  CA  . ILE B 1 431 ? 38.030 -44.276 40.586  1.00 40.17  ?  431 ILE B CA  1 
ATOM   6752 C  C   . ILE B 1 431 ? 39.532 -44.290 40.256  1.00 36.09  ?  431 ILE B C   1 
ATOM   6753 O  O   . ILE B 1 431 ? 40.180 -43.238 40.228  1.00 30.44  ?  431 ILE B O   1 
ATOM   6754 C  CB  . ILE B 1 431 ? 37.171 -43.858 39.365  1.00 41.28  ?  431 ILE B CB  1 
ATOM   6755 C  CG1 . ILE B 1 431 ? 35.672 -43.804 39.672  1.00 40.26  ?  431 ILE B CG1 1 
ATOM   6756 C  CG2 . ILE B 1 431 ? 37.426 -44.777 38.169  1.00 44.63  ?  431 ILE B CG2 1 
ATOM   6757 C  CD1 . ILE B 1 431 ? 35.066 -45.140 40.103  1.00 38.27  ?  431 ILE B CD1 1 
ATOM   6758 N  N   . LEU B 1 432 ? 40.064 -45.510 40.031  1.00 34.77  ?  432 LEU B N   1 
ATOM   6759 C  CA  . LEU B 1 432 ? 41.420 -45.781 39.562  1.00 31.34  ?  432 LEU B CA  1 
ATOM   6760 C  C   . LEU B 1 432 ? 41.605 -45.321 38.115  1.00 31.30  ?  432 LEU B C   1 
ATOM   6761 O  O   . LEU B 1 432 ? 40.906 -45.788 37.214  1.00 27.14  ?  432 LEU B O   1 
ATOM   6762 C  CB  . LEU B 1 432 ? 41.639 -47.290 39.621  1.00 32.48  ?  432 LEU B CB  1 
ATOM   6763 C  CG  . LEU B 1 432 ? 41.706 -47.936 41.003  1.00 32.44  ?  432 LEU B CG  1 
ATOM   6764 C  CD1 . LEU B 1 432 ? 42.008 -49.405 40.840  1.00 35.27  ?  432 LEU B CD1 1 
ATOM   6765 C  CD2 . LEU B 1 432 ? 42.762 -47.282 41.858  1.00 31.98  ?  432 LEU B CD2 1 
ATOM   6766 N  N   . PRO B 1 433 ? 42.573 -44.424 37.830  1.00 32.44  ?  433 PRO B N   1 
ATOM   6767 C  CA  . PRO B 1 433 ? 42.761 -43.911 36.474  1.00 32.85  ?  433 PRO B CA  1 
ATOM   6768 C  C   . PRO B 1 433 ? 43.017 -45.022 35.463  1.00 34.92  ?  433 PRO B C   1 
ATOM   6769 O  O   . PRO B 1 433 ? 43.475 -46.100 35.840  1.00 39.30  ?  433 PRO B O   1 
ATOM   6770 C  CB  . PRO B 1 433 ? 43.975 -42.990 36.619  1.00 34.45  ?  433 PRO B CB  1 
ATOM   6771 C  CG  . PRO B 1 433 ? 43.993 -42.601 38.074  1.00 35.20  ?  433 PRO B CG  1 
ATOM   6772 C  CD  . PRO B 1 433 ? 43.503 -43.833 38.804  1.00 34.99  ?  433 PRO B CD  1 
ATOM   6773 N  N   . SER B 1 434 ? 42.744 -44.745 34.178  1.00 33.74  ?  434 SER B N   1 
ATOM   6774 C  CA  . SER B 1 434 ? 42.925 -45.739 33.127  1.00 32.25  ?  434 SER B CA  1 
ATOM   6775 C  C   . SER B 1 434 ? 44.382 -45.814 32.700  1.00 31.15  ?  434 SER B C   1 
ATOM   6776 O  O   . SER B 1 434 ? 44.861 -44.855 32.113  1.00 32.80  ?  434 SER B O   1 
ATOM   6777 C  CB  . SER B 1 434 ? 42.101 -45.436 31.924  1.00 30.00  ?  434 SER B CB  1 
ATOM   6778 O  OG  . SER B 1 434 ? 42.253 -46.479 30.974  1.00 29.37  ?  434 SER B OG  1 
ATOM   6779 N  N   . LEU B 1 435 ? 45.023 -46.973 32.930  1.00 29.93  ?  435 LEU B N   1 
ATOM   6780 C  CA  . LEU B 1 435 ? 46.367 -47.263 32.447  1.00 29.07  ?  435 LEU B CA  1 
ATOM   6781 C  C   . LEU B 1 435 ? 46.319 -47.695 30.980  1.00 32.28  ?  435 LEU B C   1 
ATOM   6782 O  O   . LEU B 1 435 ? 47.343 -47.632 30.296  1.00 42.44  ?  435 LEU B O   1 
ATOM   6783 C  CB  . LEU B 1 435 ? 47.074 -48.310 33.313  1.00 26.95  ?  435 LEU B CB  1 
ATOM   6784 C  CG  . LEU B 1 435 ? 47.417 -47.891 34.754  1.00 26.94  ?  435 LEU B CG  1 
ATOM   6785 C  CD1 . LEU B 1 435 ? 47.988 -49.010 35.596  1.00 26.51  ?  435 LEU B CD1 1 
ATOM   6786 C  CD2 . LEU B 1 435 ? 48.382 -46.724 34.841  1.00 26.31  ?  435 LEU B CD2 1 
ATOM   6787 N  N   . VAL B 1 436 ? 45.154 -48.148 30.492  1.00 28.99  ?  436 VAL B N   1 
ATOM   6788 C  CA  . VAL B 1 436 ? 44.949 -48.297 29.055  1.00 28.56  ?  436 VAL B CA  1 
ATOM   6789 C  C   . VAL B 1 436 ? 45.016 -46.909 28.397  1.00 29.50  ?  436 VAL B C   1 
ATOM   6790 O  O   . VAL B 1 436 ? 45.946 -46.620 27.657  1.00 33.38  ?  436 VAL B O   1 
ATOM   6791 C  CB  . VAL B 1 436 ? 43.663 -49.062 28.666  1.00 24.82  ?  436 VAL B CB  1 
ATOM   6792 C  CG1 . VAL B 1 436 ? 43.365 -48.973 27.171  1.00 22.22  ?  436 VAL B CG1 1 
ATOM   6793 C  CG2 . VAL B 1 436 ? 43.736 -50.526 29.099  1.00 24.11  ?  436 VAL B CG2 1 
ATOM   6794 N  N   . THR B 1 437 ? 44.056 -46.024 28.674  1.00 30.26  ?  437 THR B N   1 
ATOM   6795 C  CA  . THR B 1 437 ? 44.020 -44.719 28.024  1.00 30.15  ?  437 THR B CA  1 
ATOM   6796 C  C   . THR B 1 437 ? 45.283 -43.933 28.359  1.00 29.60  ?  437 THR B C   1 
ATOM   6797 O  O   . THR B 1 437 ? 45.945 -43.438 27.457  1.00 28.53  ?  437 THR B O   1 
ATOM   6798 C  CB  . THR B 1 437 ? 42.780 -43.935 28.439  1.00 33.37  ?  437 THR B CB  1 
ATOM   6799 O  OG1 . THR B 1 437 ? 41.649 -44.792 28.300  1.00 32.63  ?  437 THR B OG1 1 
ATOM   6800 C  CG2 . THR B 1 437 ? 42.576 -42.705 27.576  1.00 36.31  ?  437 THR B CG2 1 
ATOM   6801 N  N   . GLY B 1 438 ? 45.593 -43.818 29.661  1.00 30.75  ?  438 GLY B N   1 
ATOM   6802 C  CA  . GLY B 1 438 ? 46.812 -43.175 30.147  1.00 27.71  ?  438 GLY B CA  1 
ATOM   6803 C  C   . GLY B 1 438 ? 48.040 -43.539 29.315  1.00 25.88  ?  438 GLY B C   1 
ATOM   6804 O  O   . GLY B 1 438 ? 48.794 -42.661 28.917  1.00 24.34  ?  438 GLY B O   1 
ATOM   6805 N  N   . SER B 1 439 ? 48.220 -44.837 29.051  1.00 26.42  ?  439 SER B N   1 
ATOM   6806 C  CA  . SER B 1 439 ? 49.392 -45.321 28.347  1.00 29.48  ?  439 SER B CA  1 
ATOM   6807 C  C   . SER B 1 439 ? 49.270 -45.016 26.849  1.00 35.37  ?  439 SER B C   1 
ATOM   6808 O  O   . SER B 1 439 ? 50.187 -44.477 26.217  1.00 33.66  ?  439 SER B O   1 
ATOM   6809 C  CB  . SER B 1 439 ? 49.594 -46.784 28.639  1.00 29.54  ?  439 SER B CB  1 
ATOM   6810 O  OG  . SER B 1 439 ? 49.921 -46.995 30.013  1.00 30.19  ?  439 SER B OG  1 
ATOM   6811 N  N   . ASN B 1 440 ? 48.089 -45.298 26.290  1.00 39.90  ?  440 ASN B N   1 
ATOM   6812 C  CA  . ASN B 1 440 ? 47.801 -44.976 24.902  1.00 40.87  ?  440 ASN B CA  1 
ATOM   6813 C  C   . ASN B 1 440 ? 48.182 -43.515 24.632  1.00 42.65  ?  440 ASN B C   1 
ATOM   6814 O  O   . ASN B 1 440 ? 49.084 -43.245 23.833  1.00 48.44  ?  440 ASN B O   1 
ATOM   6815 C  CB  . ASN B 1 440 ? 46.353 -45.309 24.549  1.00 39.79  ?  440 ASN B CB  1 
ATOM   6816 C  CG  . ASN B 1 440 ? 46.098 -46.797 24.468  1.00 38.99  ?  440 ASN B CG  1 
ATOM   6817 O  OD1 . ASN B 1 440 ? 46.936 -47.608 24.870  1.00 33.90  ?  440 ASN B OD1 1 
ATOM   6818 N  ND2 . ASN B 1 440 ? 44.942 -47.182 23.948  1.00 46.67  ?  440 ASN B ND2 1 
ATOM   6819 N  N   . ILE B 1 441 ? 47.536 -42.586 25.351  1.00 38.50  ?  441 ILE B N   1 
ATOM   6820 C  CA  . ILE B 1 441 ? 47.793 -41.160 25.191  1.00 34.39  ?  441 ILE B CA  1 
ATOM   6821 C  C   . ILE B 1 441 ? 49.294 -40.918 25.280  1.00 31.78  ?  441 ILE B C   1 
ATOM   6822 O  O   . ILE B 1 441 ? 49.818 -40.194 24.452  1.00 31.48  ?  441 ILE B O   1 
ATOM   6823 C  CB  . ILE B 1 441 ? 47.046 -40.282 26.218  1.00 33.60  ?  441 ILE B CB  1 
ATOM   6824 C  CG1 . ILE B 1 441 ? 45.541 -40.386 26.109  1.00 33.90  ?  441 ILE B CG1 1 
ATOM   6825 C  CG2 . ILE B 1 441 ? 47.473 -38.823 26.084  1.00 36.97  ?  441 ILE B CG2 1 
ATOM   6826 C  CD1 . ILE B 1 441 ? 44.802 -39.597 27.169  1.00 35.49  ?  441 ILE B CD1 1 
ATOM   6827 N  N   . ALA B 1 442 ? 49.966 -41.511 26.278  1.00 31.46  ?  442 ALA B N   1 
ATOM   6828 C  CA  . ALA B 1 442 ? 51.350 -41.163 26.585  1.00 31.95  ?  442 ALA B CA  1 
ATOM   6829 C  C   . ALA B 1 442 ? 52.283 -41.531 25.423  1.00 29.06  ?  442 ALA B C   1 
ATOM   6830 O  O   . ALA B 1 442 ? 53.223 -40.793 25.131  1.00 26.56  ?  442 ALA B O   1 
ATOM   6831 C  CB  . ALA B 1 442 ? 51.787 -41.793 27.901  1.00 29.60  ?  442 ALA B CB  1 
ATOM   6832 N  N   . GLY B 1 443 ? 52.014 -42.649 24.748  1.00 26.34  ?  443 GLY B N   1 
ATOM   6833 C  CA  . GLY B 1 443 ? 52.843 -43.074 23.625  1.00 29.50  ?  443 GLY B CA  1 
ATOM   6834 C  C   . GLY B 1 443 ? 52.563 -42.250 22.364  1.00 30.23  ?  443 GLY B C   1 
ATOM   6835 O  O   . GLY B 1 443 ? 53.454 -41.812 21.635  1.00 29.04  ?  443 GLY B O   1 
ATOM   6836 N  N   . PHE B 1 444 ? 51.286 -42.005 22.120  1.00 31.43  ?  444 PHE B N   1 
ATOM   6837 C  CA  . PHE B 1 444 ? 50.910 -41.100 21.057  1.00 30.78  ?  444 PHE B CA  1 
ATOM   6838 C  C   . PHE B 1 444 ? 51.497 -39.705 21.268  1.00 26.51  ?  444 PHE B C   1 
ATOM   6839 O  O   . PHE B 1 444 ? 51.986 -39.088 20.338  1.00 28.92  ?  444 PHE B O   1 
ATOM   6840 C  CB  . PHE B 1 444 ? 49.391 -41.051 20.969  1.00 32.45  ?  444 PHE B CB  1 
ATOM   6841 C  CG  . PHE B 1 444 ? 48.967 -40.082 19.888  1.00 35.97  ?  444 PHE B CG  1 
ATOM   6842 C  CD1 . PHE B 1 444 ? 49.096 -40.430 18.549  1.00 37.75  ?  444 PHE B CD1 1 
ATOM   6843 C  CD2 . PHE B 1 444 ? 48.495 -38.817 20.218  1.00 38.27  ?  444 PHE B CD2 1 
ATOM   6844 C  CE1 . PHE B 1 444 ? 48.736 -39.534 17.560  1.00 39.87  ?  444 PHE B CE1 1 
ATOM   6845 C  CE2 . PHE B 1 444 ? 48.148 -37.924 19.223  1.00 40.82  ?  444 PHE B CE2 1 
ATOM   6846 C  CZ  . PHE B 1 444 ? 48.254 -38.291 17.898  1.00 41.28  ?  444 PHE B CZ  1 
ATOM   6847 N  N   . THR B 1 445 ? 51.451 -39.160 22.469  1.00 26.11  ?  445 THR B N   1 
ATOM   6848 C  CA  . THR B 1 445 ? 51.851 -37.765 22.626  1.00 27.24  ?  445 THR B CA  1 
ATOM   6849 C  C   . THR B 1 445 ? 53.382 -37.606 22.564  1.00 28.68  ?  445 THR B C   1 
ATOM   6850 O  O   . THR B 1 445 ? 53.888 -36.599 22.068  1.00 27.12  ?  445 THR B O   1 
ATOM   6851 C  CB  . THR B 1 445 ? 51.243 -37.201 23.906  1.00 25.53  ?  445 THR B CB  1 
ATOM   6852 O  OG1 . THR B 1 445 ? 51.643 -38.073 24.963  1.00 27.80  ?  445 THR B OG1 1 
ATOM   6853 C  CG2 . THR B 1 445 ? 49.731 -37.136 23.803  1.00 24.45  ?  445 THR B CG2 1 
ATOM   6854 N  N   . LYS B 1 446 ? 54.152 -38.592 23.035  1.00 27.72  ?  446 LYS B N   1 
ATOM   6855 C  CA  . LYS B 1 446 ? 55.597 -38.441 22.997  1.00 28.10  ?  446 LYS B CA  1 
ATOM   6856 C  C   . LYS B 1 446 ? 56.041 -38.499 21.535  1.00 27.53  ?  446 LYS B C   1 
ATOM   6857 O  O   . LYS B 1 446 ? 56.910 -37.728 21.122  1.00 27.26  ?  446 LYS B O   1 
ATOM   6858 C  CB  . LYS B 1 446 ? 56.276 -39.360 24.030  1.00 29.48  ?  446 LYS B CB  1 
ATOM   6859 C  CG  . LYS B 1 446 ? 57.635 -39.984 23.672  1.00 31.18  ?  446 LYS B CG  1 
ATOM   6860 C  CD  . LYS B 1 446 ? 58.670 -39.999 24.795  1.00 31.33  ?  446 LYS B CD  1 
ATOM   6861 C  CE  . LYS B 1 446 ? 58.214 -40.640 26.057  1.00 32.85  ?  446 LYS B CE  1 
ATOM   6862 N  NZ  . LYS B 1 446 ? 58.507 -39.744 27.185  1.00 35.48  1  446 LYS B NZ  1 
ATOM   6863 N  N   . VAL B 1 447 ? 55.431 -39.410 20.764  1.00 29.39  ?  447 VAL B N   1 
ATOM   6864 C  CA  . VAL B 1 447 ? 55.850 -39.667 19.393  1.00 30.03  ?  447 VAL B CA  1 
ATOM   6865 C  C   . VAL B 1 447 ? 55.365 -38.524 18.516  1.00 33.48  ?  447 VAL B C   1 
ATOM   6866 O  O   . VAL B 1 447 ? 56.150 -37.966 17.737  1.00 34.36  ?  447 VAL B O   1 
ATOM   6867 C  CB  . VAL B 1 447 ? 55.374 -41.021 18.841  1.00 29.26  ?  447 VAL B CB  1 
ATOM   6868 C  CG1 . VAL B 1 447 ? 55.518 -41.119 17.321  1.00 31.61  ?  447 VAL B CG1 1 
ATOM   6869 C  CG2 . VAL B 1 447 ? 56.106 -42.180 19.494  1.00 26.92  ?  447 VAL B CG2 1 
ATOM   6870 N  N   . ALA B 1 448 ? 54.070 -38.200 18.663  1.00 35.25  ?  448 ALA B N   1 
ATOM   6871 C  CA  . ALA B 1 448 ? 53.442 -37.119 17.913  1.00 35.38  ?  448 ALA B CA  1 
ATOM   6872 C  C   . ALA B 1 448 ? 54.183 -35.807 18.118  1.00 31.15  ?  448 ALA B C   1 
ATOM   6873 O  O   . ALA B 1 448 ? 54.277 -35.045 17.174  1.00 35.86  ?  448 ALA B O   1 
ATOM   6874 C  CB  . ALA B 1 448 ? 51.987 -36.956 18.277  1.00 36.34  ?  448 ALA B CB  1 
ATOM   6875 N  N   . ALA B 1 449 ? 54.716 -35.564 19.322  1.00 30.65  ?  449 ALA B N   1 
ATOM   6876 C  CA  . ALA B 1 449 ? 55.355 -34.290 19.640  1.00 30.02  ?  449 ALA B CA  1 
ATOM   6877 C  C   . ALA B 1 449 ? 56.690 -34.208 18.910  1.00 31.24  ?  449 ALA B C   1 
ATOM   6878 O  O   . ALA B 1 449 ? 56.945 -33.257 18.182  1.00 32.71  ?  449 ALA B O   1 
ATOM   6879 C  CB  . ALA B 1 449 ? 55.529 -34.121 21.135  1.00 28.12  ?  449 ALA B CB  1 
ATOM   6880 N  N   . ALA B 1 450 ? 57.501 -35.251 19.078  1.00 32.58  ?  450 ALA B N   1 
ATOM   6881 C  CA  . ALA B 1 450 ? 58.795 -35.367 18.430  1.00 34.44  ?  450 ALA B CA  1 
ATOM   6882 C  C   . ALA B 1 450 ? 58.674 -35.234 16.906  1.00 36.12  ?  450 ALA B C   1 
ATOM   6883 O  O   . ALA B 1 450 ? 59.570 -34.670 16.266  1.00 39.25  ?  450 ALA B O   1 
ATOM   6884 C  CB  . ALA B 1 450 ? 59.406 -36.695 18.833  1.00 35.17  ?  450 ALA B CB  1 
ATOM   6885 N  N   . MET B 1 451 ? 57.582 -35.781 16.338  1.00 33.26  ?  451 MET B N   1 
ATOM   6886 C  CA  . MET B 1 451 ? 57.294 -35.690 14.911  1.00 31.38  ?  451 MET B CA  1 
ATOM   6887 C  C   . MET B 1 451 ? 57.074 -34.227 14.523  1.00 29.16  ?  451 MET B C   1 
ATOM   6888 O  O   . MET B 1 451 ? 57.569 -33.797 13.482  1.00 26.89  ?  451 MET B O   1 
ATOM   6889 C  CB  . MET B 1 451 ? 56.051 -36.509 14.524  1.00 30.07  ?  451 MET B CB  1 
ATOM   6890 C  CG  . MET B 1 451 ? 56.262 -38.025 14.462  1.00 27.69  ?  451 MET B CG  1 
ATOM   6891 S  SD  . MET B 1 451 ? 54.720 -38.934 14.214  1.00 25.90  ?  451 MET B SD  1 
ATOM   6892 C  CE  . MET B 1 451 ? 54.297 -38.583 12.502  1.00 23.26  ?  451 MET B CE  1 
ATOM   6893 N  N   . LYS B 1 452 ? 56.321 -33.486 15.357  1.00 25.99  ?  452 LYS B N   1 
ATOM   6894 C  CA  . LYS B 1 452 ? 56.127 -32.052 15.181  1.00 23.52  ?  452 LYS B CA  1 
ATOM   6895 C  C   . LYS B 1 452 ? 57.472 -31.350 15.313  1.00 21.82  ?  452 LYS B C   1 
ATOM   6896 O  O   . LYS B 1 452 ? 57.860 -30.570 14.470  1.00 23.76  ?  452 LYS B O   1 
ATOM   6897 C  CB  . LYS B 1 452 ? 55.162 -31.460 16.212  1.00 23.69  ?  452 LYS B CB  1 
ATOM   6898 C  CG  . LYS B 1 452 ? 54.726 -30.008 15.981  1.00 24.96  ?  452 LYS B CG  1 
ATOM   6899 C  CD  . LYS B 1 452 ? 53.537 -29.592 16.855  1.00 25.60  ?  452 LYS B CD  1 
ATOM   6900 C  CE  . LYS B 1 452 ? 52.830 -28.331 16.448  1.00 26.13  ?  452 LYS B CE  1 
ATOM   6901 N  NZ  . LYS B 1 452 ? 53.597 -27.118 16.760  1.00 25.10  1  452 LYS B NZ  1 
ATOM   6902 N  N   . ASP B 1 453 ? 58.214 -31.659 16.362  1.00 21.57  ?  453 ASP B N   1 
ATOM   6903 C  CA  . ASP B 1 453 ? 59.504 -31.038 16.586  1.00 21.57  ?  453 ASP B CA  1 
ATOM   6904 C  C   . ASP B 1 453 ? 60.378 -31.180 15.340  1.00 25.25  ?  453 ASP B C   1 
ATOM   6905 O  O   . ASP B 1 453 ? 61.036 -30.208 14.929  1.00 25.18  ?  453 ASP B O   1 
ATOM   6906 C  CB  . ASP B 1 453 ? 60.131 -31.588 17.856  1.00 18.97  ?  453 ASP B CB  1 
ATOM   6907 C  CG  . ASP B 1 453 ? 59.399 -31.203 19.127  1.00 16.81  ?  453 ASP B CG  1 
ATOM   6908 O  OD1 . ASP B 1 453 ? 58.612 -30.264 19.065  1.00 15.10  ?  453 ASP B OD1 1 
ATOM   6909 O  OD2 . ASP B 1 453 ? 59.586 -31.886 20.152  1.00 17.64  -1 453 ASP B OD2 1 
ATOM   6910 N  N   . GLN B 1 454 ? 60.342 -32.390 14.740  1.00 27.72  ?  454 GLN B N   1 
ATOM   6911 C  CA  . GLN B 1 454 ? 61.158 -32.734 13.575  1.00 27.16  ?  454 GLN B CA  1 
ATOM   6912 C  C   . GLN B 1 454 ? 60.494 -32.447 12.218  1.00 28.10  ?  454 GLN B C   1 
ATOM   6913 O  O   . GLN B 1 454 ? 61.124 -32.671 11.184  1.00 31.04  ?  454 GLN B O   1 
ATOM   6914 C  CB  . GLN B 1 454 ? 61.532 -34.204 13.715  1.00 24.19  ?  454 GLN B CB  1 
ATOM   6915 C  CG  . GLN B 1 454 ? 62.451 -34.462 14.900  1.00 22.24  ?  454 GLN B CG  1 
ATOM   6916 C  CD  . GLN B 1 454 ? 62.738 -35.930 15.072  1.00 20.30  ?  454 GLN B CD  1 
ATOM   6917 O  OE1 . GLN B 1 454 ? 62.802 -36.674 14.091  1.00 17.31  ?  454 GLN B OE1 1 
ATOM   6918 N  NE2 . GLN B 1 454 ? 62.803 -36.373 16.319  1.00 21.03  ?  454 GLN B NE2 1 
ATOM   6919 N  N   . GLY B 1 455 ? 59.233 -31.983 12.221  1.00 27.45  ?  455 GLY B N   1 
ATOM   6920 C  CA  . GLY B 1 455 ? 58.550 -31.464 11.042  1.00 28.18  ?  455 GLY B CA  1 
ATOM   6921 C  C   . GLY B 1 455 ? 57.990 -32.552 10.123  1.00 30.77  ?  455 GLY B C   1 
ATOM   6922 O  O   . GLY B 1 455 ? 58.008 -32.390 8.902   1.00 38.30  ?  455 GLY B O   1 
ATOM   6923 N  N   . ASP B 1 456 ? 57.474 -33.643 10.711  1.00 28.86  ?  456 ASP B N   1 
ATOM   6924 C  CA  . ASP B 1 456 ? 56.885 -34.743 9.964   1.00 26.86  ?  456 ASP B CA  1 
ATOM   6925 C  C   . ASP B 1 456 ? 55.429 -34.411 9.668   1.00 27.92  ?  456 ASP B C   1 
ATOM   6926 O  O   . ASP B 1 456 ? 54.866 -34.919 8.701   1.00 27.27  ?  456 ASP B O   1 
ATOM   6927 C  CB  . ASP B 1 456 ? 57.050 -36.056 10.718  1.00 26.51  ?  456 ASP B CB  1 
ATOM   6928 C  CG  . ASP B 1 456 ? 58.489 -36.520 10.895  1.00 25.08  ?  456 ASP B CG  1 
ATOM   6929 O  OD1 . ASP B 1 456 ? 59.379 -35.890 10.274  1.00 24.77  ?  456 ASP B OD1 1 
ATOM   6930 O  OD2 . ASP B 1 456 ? 58.720 -37.480 11.676  1.00 22.80  -1 456 ASP B OD2 1 
ATOM   6931 N  N   . TRP B 1 457 ? 54.832 -33.603 10.560  1.00 30.26  ?  457 TRP B N   1 
ATOM   6932 C  CA  . TRP B 1 457 ? 53.564 -32.917 10.331  1.00 29.57  ?  457 TRP B CA  1 
ATOM   6933 C  C   . TRP B 1 457 ? 53.673 -31.478 10.828  1.00 32.15  ?  457 TRP B C   1 
ATOM   6934 O  O   . TRP B 1 457 ? 54.645 -31.107 11.495  1.00 35.24  ?  457 TRP B O   1 
ATOM   6935 C  CB  . TRP B 1 457 ? 52.391 -33.632 11.015  1.00 29.72  ?  457 TRP B CB  1 
ATOM   6936 C  CG  . TRP B 1 457 ? 52.459 -33.600 12.523  1.00 30.79  ?  457 TRP B CG  1 
ATOM   6937 C  CD1 . TRP B 1 457 ? 53.264 -34.354 13.331  1.00 31.30  ?  457 TRP B CD1 1 
ATOM   6938 C  CD2 . TRP B 1 457 ? 51.678 -32.774 13.406  1.00 26.96  ?  457 TRP B CD2 1 
ATOM   6939 N  NE1 . TRP B 1 457 ? 53.047 -34.044 14.643  1.00 30.16  ?  457 TRP B NE1 1 
ATOM   6940 C  CE2 . TRP B 1 457 ? 52.076 -33.083 14.720  1.00 27.60  ?  457 TRP B CE2 1 
ATOM   6941 C  CE3 . TRP B 1 457 ? 50.695 -31.806 13.212  1.00 28.56  ?  457 TRP B CE3 1 
ATOM   6942 C  CZ2 . TRP B 1 457 ? 51.522 -32.459 15.831  1.00 27.67  ?  457 TRP B CZ2 1 
ATOM   6943 C  CZ3 . TRP B 1 457 ? 50.157 -31.176 14.312  1.00 29.28  ?  457 TRP B CZ3 1 
ATOM   6944 C  CH2 . TRP B 1 457 ? 50.563 -31.500 15.601  1.00 28.01  ?  457 TRP B CH2 1 
ATOM   6945 N  N   . TRP B 1 458 ? 52.695 -30.666 10.409  1.00 36.71  ?  458 TRP B N   1 
ATOM   6946 C  CA  . TRP B 1 458 ? 52.496 -29.304 10.894  1.00 40.69  ?  458 TRP B CA  1 
ATOM   6947 C  C   . TRP B 1 458 ? 50.992 -28.982 10.848  1.00 40.22  ?  458 TRP B C   1 
ATOM   6948 O  O   . TRP B 1 458 ? 50.253 -29.772 10.245  1.00 39.41  ?  458 TRP B O   1 
ATOM   6949 C  CB  . TRP B 1 458 ? 53.321 -28.297 10.075  1.00 38.04  ?  458 TRP B CB  1 
ATOM   6950 C  CG  . TRP B 1 458 ? 53.101 -28.401 8.586   1.00 38.64  ?  458 TRP B CG  1 
ATOM   6951 C  CD1 . TRP B 1 458 ? 52.289 -27.617 7.823   1.00 37.56  ?  458 TRP B CD1 1 
ATOM   6952 C  CD2 . TRP B 1 458 ? 53.671 -29.382 7.688   1.00 37.70  ?  458 TRP B CD2 1 
ATOM   6953 N  NE1 . TRP B 1 458 ? 52.338 -28.013 6.514   1.00 37.19  ?  458 TRP B NE1 1 
ATOM   6954 C  CE2 . TRP B 1 458 ? 53.169 -29.097 6.400   1.00 37.85  ?  458 TRP B CE2 1 
ATOM   6955 C  CE3 . TRP B 1 458 ? 54.557 -30.457 7.838   1.00 37.28  ?  458 TRP B CE3 1 
ATOM   6956 C  CZ2 . TRP B 1 458 ? 53.515 -29.860 5.285   1.00 35.78  ?  458 TRP B CZ2 1 
ATOM   6957 C  CZ3 . TRP B 1 458 ? 54.877 -31.223 6.740   1.00 35.02  ?  458 TRP B CZ3 1 
ATOM   6958 C  CH2 . TRP B 1 458 ? 54.353 -30.931 5.483   1.00 34.59  ?  458 TRP B CH2 1 
ATOM   6959 O  OXT . TRP B 1 458 ? 50.606 -27.969 11.421  1.00 42.74  -1 458 TRP B OXT 1 
HETATM 6960 CL CL  . CL  C 2 .   ? 64.857 -45.508 -40.862 1.00 50.41  ?  501 CL  A CL  1 
HETATM 6961 CL CL  . CL  D 2 .   ? 55.832 -46.848 -18.754 1.00 38.74  ?  502 CL  A CL  1 
HETATM 6962 CL CL  . CL  E 2 .   ? 44.606 -47.327 6.559   1.00 52.18  ?  501 CL  B CL  1 
HETATM 6963 CL CL  . CL  F 2 .   ? 63.042 -61.166 25.705  1.00 48.72  ?  502 CL  B CL  1 
HETATM 6964 CL CL  . CL  G 2 .   ? 68.995 -48.969 0.149   1.00 46.52  ?  503 CL  B CL  1 
HETATM 6965 O  O   . HOH H 3 .   ? 42.369 -39.981 -31.197 1.00 25.26  ?  601 HOH A O   1 
HETATM 6966 O  O   . HOH H 3 .   ? 58.940 -29.859 -15.138 1.00 12.69  ?  602 HOH A O   1 
HETATM 6967 O  O   . HOH H 3 .   ? 55.525 -49.437 -31.268 1.00 22.50  ?  603 HOH A O   1 
HETATM 6968 O  O   . HOH H 3 .   ? 63.581 -70.087 -30.641 1.00 37.19  ?  604 HOH A O   1 
HETATM 6969 O  O   . HOH H 3 .   ? 47.672 -24.588 6.200   1.00 24.79  ?  605 HOH A O   1 
HETATM 6970 O  O   . HOH H 3 .   ? 63.468 -37.974 -23.809 1.00 19.50  ?  606 HOH A O   1 
HETATM 6971 O  O   . HOH H 3 .   ? 61.694 -48.288 -42.423 1.00 21.11  ?  607 HOH A O   1 
HETATM 6972 O  O   . HOH H 3 .   ? 60.456 -42.542 -20.655 1.00 9.12   ?  608 HOH A O   1 
HETATM 6973 O  O   . HOH H 3 .   ? 70.706 -72.126 -11.529 1.00 5.25   ?  609 HOH A O   1 
HETATM 6974 O  O   . HOH H 3 .   ? 69.802 -71.376 -20.131 1.00 17.99  ?  610 HOH A O   1 
HETATM 6975 O  O   . HOH H 3 .   ? 65.076 -29.436 -22.744 1.00 4.22   ?  611 HOH A O   1 
HETATM 6976 O  O   . HOH H 3 .   ? 55.710 -51.631 -51.919 1.00 38.60  ?  612 HOH A O   1 
HETATM 6977 O  O   . HOH H 3 .   ? 66.066 -41.676 -0.234  1.00 17.75  ?  613 HOH A O   1 
HETATM 6978 O  O   . HOH H 3 .   ? 55.516 -76.062 -30.659 1.00 23.03  ?  614 HOH A O   1 
HETATM 6979 O  O   . HOH H 3 .   ? 48.654 -67.790 -42.494 1.00 46.91  ?  615 HOH A O   1 
HETATM 6980 O  O   . HOH H 3 .   ? 38.268 -47.159 -23.293 1.00 23.82  ?  616 HOH A O   1 
HETATM 6981 O  O   . HOH H 3 .   ? 62.834 -64.964 -25.993 1.00 22.62  ?  617 HOH A O   1 
HETATM 6982 O  O   . HOH H 3 .   ? 55.385 -42.529 -27.836 1.00 28.55  ?  618 HOH A O   1 
HETATM 6983 O  O   . HOH H 3 .   ? 70.294 -43.923 1.402   1.00 6.93   ?  619 HOH A O   1 
HETATM 6984 O  O   . HOH H 3 .   ? 54.250 -42.054 -31.269 1.00 24.93  ?  620 HOH A O   1 
HETATM 6985 O  O   . HOH H 3 .   ? 76.670 -39.357 -6.415  1.00 26.55  ?  621 HOH A O   1 
HETATM 6986 O  O   . HOH H 3 .   ? 64.462 -59.104 -16.993 1.00 26.44  ?  622 HOH A O   1 
HETATM 6987 O  O   . HOH H 3 .   ? 43.668 -38.430 -12.357 1.00 11.61  ?  623 HOH A O   1 
HETATM 6988 O  O   . HOH H 3 .   ? 50.502 -56.309 -22.224 1.00 20.91  ?  624 HOH A O   1 
HETATM 6989 O  O   . HOH H 3 .   ? 66.460 -43.893 -40.080 1.00 11.11  ?  625 HOH A O   1 
HETATM 6990 O  O   . HOH H 3 .   ? 68.083 -34.217 -38.165 1.00 24.55  ?  626 HOH A O   1 
HETATM 6991 O  O   . HOH H 3 .   ? 64.994 -79.082 -13.344 1.00 43.47  ?  627 HOH A O   1 
HETATM 6992 O  O   . HOH H 3 .   ? 57.035 -35.389 -21.921 1.00 17.62  ?  628 HOH A O   1 
HETATM 6993 O  O   . HOH H 3 .   ? 47.102 -44.089 -28.142 1.00 19.28  ?  629 HOH A O   1 
HETATM 6994 O  O   . HOH H 3 .   ? 57.936 -41.046 -20.293 1.00 18.50  ?  630 HOH A O   1 
HETATM 6995 O  O   . HOH H 3 .   ? 44.690 -73.747 -28.338 1.00 21.00  ?  631 HOH A O   1 
HETATM 6996 O  O   . HOH H 3 .   ? 69.615 -51.554 -37.604 1.00 29.92  ?  632 HOH A O   1 
HETATM 6997 O  O   . HOH H 3 .   ? 55.927 -67.823 -41.389 1.00 25.33  ?  633 HOH A O   1 
HETATM 6998 O  O   . HOH H 3 .   ? 44.669 -46.189 -24.289 1.00 28.33  ?  634 HOH A O   1 
HETATM 6999 O  O   . HOH H 3 .   ? 47.520 -35.792 -14.892 1.00 28.09  ?  635 HOH A O   1 
HETATM 7000 O  O   . HOH H 3 .   ? 43.330 -45.269 -15.583 1.00 21.01  ?  636 HOH A O   1 
HETATM 7001 O  O   . HOH H 3 .   ? 50.174 -39.363 -24.929 1.00 34.08  ?  637 HOH A O   1 
HETATM 7002 O  O   . HOH I 3 .   ? 46.197 -50.023 21.098  1.00 11.35  ?  601 HOH B O   1 
HETATM 7003 O  O   . HOH I 3 .   ? 43.645 -49.682 33.430  1.00 19.70  ?  602 HOH B O   1 
HETATM 7004 O  O   . HOH I 3 .   ? 36.242 -36.753 37.817  1.00 34.25  ?  603 HOH B O   1 
HETATM 7005 O  O   . HOH I 3 .   ? 70.868 -60.305 24.722  1.00 38.66  ?  604 HOH B O   1 
HETATM 7006 O  O   . HOH I 3 .   ? 42.740 -53.445 42.002  1.00 18.33  ?  605 HOH B O   1 
HETATM 7007 O  O   . HOH I 3 .   ? 61.188 -61.993 -10.338 1.00 6.00   ?  606 HOH B O   1 
HETATM 7008 O  O   . HOH I 3 .   ? 58.425 -56.151 25.314  1.00 33.15  ?  607 HOH B O   1 
HETATM 7009 O  O   . HOH I 3 .   ? 54.359 -38.771 26.192  1.00 22.65  ?  608 HOH B O   1 
HETATM 7010 O  O   . HOH I 3 .   ? 69.644 -72.106 0.171   1.00 17.55  ?  609 HOH B O   1 
HETATM 7011 O  O   . HOH I 3 .   ? 77.555 -57.965 25.723  1.00 17.99  ?  610 HOH B O   1 
HETATM 7012 O  O   . HOH I 3 .   ? 71.249 -69.895 2.217   1.00 14.08  ?  611 HOH B O   1 
HETATM 7013 O  O   . HOH I 3 .   ? 54.525 -43.208 11.483  1.00 11.37  ?  612 HOH B O   1 
HETATM 7014 O  O   . HOH I 3 .   ? 67.330 -77.142 14.335  1.00 16.05  ?  613 HOH B O   1 
HETATM 7015 O  O   . HOH I 3 .   ? 74.093 -50.766 19.621  1.00 29.67  ?  614 HOH B O   1 
HETATM 7016 O  O   . HOH I 3 .   ? 51.656 -52.684 53.285  1.00 37.87  ?  615 HOH B O   1 
HETATM 7017 O  O   . HOH I 3 .   ? 46.318 -57.275 24.703  1.00 25.01  ?  616 HOH B O   1 
HETATM 7018 O  O   . HOH I 3 .   ? 54.995 -71.425 27.741  1.00 27.43  ?  617 HOH B O   1 
HETATM 7019 O  O   . HOH I 3 .   ? 53.449 -75.714 54.898  1.00 28.91  ?  618 HOH B O   1 
HETATM 7020 O  O   . HOH I 3 .   ? 49.699 -56.038 29.763  1.00 17.06  ?  619 HOH B O   1 
HETATM 7021 O  O   . HOH I 3 .   ? 49.095 -58.335 4.120   1.00 13.82  ?  620 HOH B O   1 
HETATM 7022 O  O   . HOH I 3 .   ? 76.815 -51.217 18.028  1.00 19.30  ?  621 HOH B O   1 
HETATM 7023 O  O   . HOH I 3 .   ? 43.205 -59.115 20.868  1.00 21.89  ?  622 HOH B O   1 
HETATM 7024 O  O   . HOH I 3 .   ? 40.537 -51.902 34.502  1.00 42.60  ?  623 HOH B O   1 
HETATM 7025 O  O   . HOH I 3 .   ? 65.103 -60.845 20.830  1.00 6.88   ?  624 HOH B O   1 
HETATM 7026 O  O   . HOH I 3 .   ? 40.664 -55.731 46.983  1.00 21.23  ?  625 HOH B O   1 
HETATM 7027 O  O   . HOH I 3 .   ? 61.547 -54.457 42.793  1.00 30.44  ?  626 HOH B O   1 
HETATM 7028 O  O   . HOH I 3 .   ? 67.215 -58.314 24.963  1.00 30.66  ?  627 HOH B O   1 
HETATM 7029 O  O   . HOH I 3 .   ? 60.373 -86.274 39.890  1.00 29.50  ?  628 HOH B O   1 
HETATM 7030 O  O   . HOH I 3 .   ? 32.176 -65.576 37.631  1.00 19.78  ?  629 HOH B O   1 
HETATM 7031 O  O   . HOH I 3 .   ? 71.736 -48.379 6.891   1.00 5.34   ?  630 HOH B O   1 
HETATM 7032 O  O   . HOH I 3 .   ? 55.144 -58.024 -3.376  1.00 4.92   ?  631 HOH B O   1 
HETATM 7033 O  O   . HOH I 3 .   ? 54.479 -30.556 19.968  1.00 21.64  ?  632 HOH B O   1 
HETATM 7034 O  O   . HOH I 3 .   ? 46.340 -70.015 46.816  1.00 6.76   ?  633 HOH B O   1 
# 
