data_9BH1
# 
_entry.id   9BH1 
# 
_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   9BH1         pdb_00009bh1 10.2210/pdb9bh1/pdb 
WWPDB D_1000283053 ?            ?                   
EMDB  EMD-44529    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-12 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BH1 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Apo GltPh, intermediate outward-facing state' 
_pdbx_database_related.db_id          EMD-44529 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              olb2003@med.cornell.edu 
_pdbx_contact_author.name_first         Olga 
_pdbx_contact_author.name_last          Boudker 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6965-0851 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Reddy, K.D.' 1 ? 
'Boudker, O.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Evolutionary analysis reveals the origin of sodium coupling in glutamate transporters.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2023.12.03.569786 
_citation.pdbx_database_id_PubMed   38106174 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Reddy, K.D.'  1 0000-0002-0475-8375 
primary 'Rasool, B.'   2 ?                   
primary 'Akher, F.B.'  3 ?                   
primary 'Kutlesic, N.' 4 ?                   
primary 'Pant, S.'     5 ?                   
primary 'Boudker, O.'  6 ?                   
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'Glutamate transporter homolog' 
_entity.formula_weight             44641.945 
_entity.pdbx_number_of_molecules   1 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Glt(Ph),Sodium-aspartate symporter Glt(Ph),Sodium-dependent aspartate transporter' 
# 
_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       
;MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMPIVFASLVVGAASISPARLGR
VGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAII
LGIAITYLMNSENEKVRKSAETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYSFTLPLGATINMDGTALYQGV
CTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGAIMLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMV
NVTGDLTGTAIVAKTEGTLVPR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMPIVFASLVVGAASISPARLGR
VGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAII
LGIAITYLMNSENEKVRKSAETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYSFTLPLGATINMDGTALYQGV
CTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGAIMLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMV
NVTGDLTGTAIVAKTEGTLVPR
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
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   GLY n 
1 3   LEU n 
1 4   TYR n 
1 5   ARG n 
1 6   LYS n 
1 7   TYR n 
1 8   ILE n 
1 9   GLU n 
1 10  TYR n 
1 11  PRO n 
1 12  VAL n 
1 13  LEU n 
1 14  GLN n 
1 15  LYS n 
1 16  ILE n 
1 17  LEU n 
1 18  ILE n 
1 19  GLY n 
1 20  LEU n 
1 21  ILE n 
1 22  LEU n 
1 23  GLY n 
1 24  ALA n 
1 25  ILE n 
1 26  VAL n 
1 27  GLY n 
1 28  LEU n 
1 29  ILE n 
1 30  LEU n 
1 31  GLY n 
1 32  HIS n 
1 33  TYR n 
1 34  GLY n 
1 35  TYR n 
1 36  ALA n 
1 37  HIS n 
1 38  ALA n 
1 39  VAL n 
1 40  HIS n 
1 41  THR n 
1 42  TYR n 
1 43  VAL n 
1 44  LYS n 
1 45  PRO n 
1 46  PHE n 
1 47  GLY n 
1 48  ASP n 
1 49  LEU n 
1 50  PHE n 
1 51  VAL n 
1 52  ARG n 
1 53  LEU n 
1 54  LEU n 
1 55  LYS n 
1 56  MET n 
1 57  LEU n 
1 58  VAL n 
1 59  MET n 
1 60  PRO n 
1 61  ILE n 
1 62  VAL n 
1 63  PHE n 
1 64  ALA n 
1 65  SER n 
1 66  LEU n 
1 67  VAL n 
1 68  VAL n 
1 69  GLY n 
1 70  ALA n 
1 71  ALA n 
1 72  SER n 
1 73  ILE n 
1 74  SER n 
1 75  PRO n 
1 76  ALA n 
1 77  ARG n 
1 78  LEU n 
1 79  GLY n 
1 80  ARG n 
1 81  VAL n 
1 82  GLY n 
1 83  VAL n 
1 84  LYS n 
1 85  ILE n 
1 86  VAL n 
1 87  VAL n 
1 88  TYR n 
1 89  TYR n 
1 90  LEU n 
1 91  LEU n 
1 92  THR n 
1 93  SER n 
1 94  ALA n 
1 95  PHE n 
1 96  ALA n 
1 97  VAL n 
1 98  THR n 
1 99  LEU n 
1 100 GLY n 
1 101 ILE n 
1 102 ILE n 
1 103 MET n 
1 104 ALA n 
1 105 ARG n 
1 106 LEU n 
1 107 PHE n 
1 108 ASN n 
1 109 PRO n 
1 110 GLY n 
1 111 ALA n 
1 112 GLY n 
1 113 ILE n 
1 114 HIS n 
1 115 LEU n 
1 116 ALA n 
1 117 VAL n 
1 118 GLY n 
1 119 GLY n 
1 120 GLN n 
1 121 GLN n 
1 122 PHE n 
1 123 GLN n 
1 124 PRO n 
1 125 HIS n 
1 126 GLN n 
1 127 ALA n 
1 128 PRO n 
1 129 PRO n 
1 130 LEU n 
1 131 VAL n 
1 132 HIS n 
1 133 ILE n 
1 134 LEU n 
1 135 LEU n 
1 136 ASP n 
1 137 ILE n 
1 138 VAL n 
1 139 PRO n 
1 140 THR n 
1 141 ASN n 
1 142 PRO n 
1 143 PHE n 
1 144 GLY n 
1 145 ALA n 
1 146 LEU n 
1 147 ALA n 
1 148 ASN n 
1 149 GLY n 
1 150 GLN n 
1 151 VAL n 
1 152 LEU n 
1 153 PRO n 
1 154 THR n 
1 155 ILE n 
1 156 PHE n 
1 157 PHE n 
1 158 ALA n 
1 159 ILE n 
1 160 ILE n 
1 161 LEU n 
1 162 GLY n 
1 163 ILE n 
1 164 ALA n 
1 165 ILE n 
1 166 THR n 
1 167 TYR n 
1 168 LEU n 
1 169 MET n 
1 170 ASN n 
1 171 SER n 
1 172 GLU n 
1 173 ASN n 
1 174 GLU n 
1 175 LYS n 
1 176 VAL n 
1 177 ARG n 
1 178 LYS n 
1 179 SER n 
1 180 ALA n 
1 181 GLU n 
1 182 THR n 
1 183 LEU n 
1 184 LEU n 
1 185 ASP n 
1 186 ALA n 
1 187 ILE n 
1 188 ASN n 
1 189 GLY n 
1 190 LEU n 
1 191 ALA n 
1 192 GLU n 
1 193 ALA n 
1 194 MET n 
1 195 TYR n 
1 196 LYS n 
1 197 ILE n 
1 198 VAL n 
1 199 ASN n 
1 200 GLY n 
1 201 VAL n 
1 202 MET n 
1 203 GLN n 
1 204 TYR n 
1 205 ALA n 
1 206 PRO n 
1 207 ILE n 
1 208 GLY n 
1 209 VAL n 
1 210 PHE n 
1 211 ALA n 
1 212 LEU n 
1 213 ILE n 
1 214 ALA n 
1 215 TYR n 
1 216 VAL n 
1 217 MET n 
1 218 ALA n 
1 219 GLU n 
1 220 GLN n 
1 221 GLY n 
1 222 VAL n 
1 223 HIS n 
1 224 VAL n 
1 225 VAL n 
1 226 GLY n 
1 227 GLU n 
1 228 LEU n 
1 229 ALA n 
1 230 LYS n 
1 231 VAL n 
1 232 THR n 
1 233 ALA n 
1 234 ALA n 
1 235 VAL n 
1 236 TYR n 
1 237 VAL n 
1 238 GLY n 
1 239 LEU n 
1 240 THR n 
1 241 LEU n 
1 242 GLN n 
1 243 ILE n 
1 244 LEU n 
1 245 LEU n 
1 246 VAL n 
1 247 TYR n 
1 248 PHE n 
1 249 VAL n 
1 250 LEU n 
1 251 LEU n 
1 252 LYS n 
1 253 ILE n 
1 254 TYR n 
1 255 GLY n 
1 256 ILE n 
1 257 ASP n 
1 258 PRO n 
1 259 ILE n 
1 260 SER n 
1 261 PHE n 
1 262 ILE n 
1 263 LYS n 
1 264 HIS n 
1 265 ALA n 
1 266 LYS n 
1 267 ASP n 
1 268 ALA n 
1 269 MET n 
1 270 LEU n 
1 271 THR n 
1 272 ALA n 
1 273 PHE n 
1 274 VAL n 
1 275 THR n 
1 276 ARG n 
1 277 SER n 
1 278 SER n 
1 279 SER n 
1 280 GLY n 
1 281 THR n 
1 282 LEU n 
1 283 PRO n 
1 284 VAL n 
1 285 THR n 
1 286 MET n 
1 287 ARG n 
1 288 VAL n 
1 289 ALA n 
1 290 LYS n 
1 291 GLU n 
1 292 MET n 
1 293 GLY n 
1 294 ILE n 
1 295 SER n 
1 296 GLU n 
1 297 GLY n 
1 298 ILE n 
1 299 TYR n 
1 300 SER n 
1 301 PHE n 
1 302 THR n 
1 303 LEU n 
1 304 PRO n 
1 305 LEU n 
1 306 GLY n 
1 307 ALA n 
1 308 THR n 
1 309 ILE n 
1 310 ASN n 
1 311 MET n 
1 312 ASP n 
1 313 GLY n 
1 314 THR n 
1 315 ALA n 
1 316 LEU n 
1 317 TYR n 
1 318 GLN n 
1 319 GLY n 
1 320 VAL n 
1 321 CYS n 
1 322 THR n 
1 323 PHE n 
1 324 PHE n 
1 325 ILE n 
1 326 ALA n 
1 327 ASN n 
1 328 ALA n 
1 329 LEU n 
1 330 GLY n 
1 331 SER n 
1 332 HIS n 
1 333 LEU n 
1 334 THR n 
1 335 VAL n 
1 336 GLY n 
1 337 GLN n 
1 338 GLN n 
1 339 LEU n 
1 340 THR n 
1 341 ILE n 
1 342 VAL n 
1 343 LEU n 
1 344 THR n 
1 345 ALA n 
1 346 VAL n 
1 347 LEU n 
1 348 ALA n 
1 349 SER n 
1 350 ILE n 
1 351 GLY n 
1 352 THR n 
1 353 ALA n 
1 354 GLY n 
1 355 VAL n 
1 356 PRO n 
1 357 GLY n 
1 358 ALA n 
1 359 GLY n 
1 360 ALA n 
1 361 ILE n 
1 362 MET n 
1 363 LEU n 
1 364 ALA n 
1 365 MET n 
1 366 VAL n 
1 367 LEU n 
1 368 HIS n 
1 369 SER n 
1 370 VAL n 
1 371 GLY n 
1 372 LEU n 
1 373 PRO n 
1 374 LEU n 
1 375 THR n 
1 376 ASP n 
1 377 PRO n 
1 378 ASN n 
1 379 VAL n 
1 380 ALA n 
1 381 ALA n 
1 382 ALA n 
1 383 TYR n 
1 384 ALA n 
1 385 MET n 
1 386 ILE n 
1 387 LEU n 
1 388 GLY n 
1 389 ILE n 
1 390 ASP n 
1 391 ALA n 
1 392 ILE n 
1 393 LEU n 
1 394 ASP n 
1 395 MET n 
1 396 GLY n 
1 397 ARG n 
1 398 THR n 
1 399 MET n 
1 400 VAL n 
1 401 ASN n 
1 402 VAL n 
1 403 THR n 
1 404 GLY n 
1 405 ASP n 
1 406 LEU n 
1 407 THR n 
1 408 GLY n 
1 409 THR n 
1 410 ALA n 
1 411 ILE n 
1 412 VAL n 
1 413 ALA n 
1 414 LYS n 
1 415 THR n 
1 416 GLU n 
1 417 GLY n 
1 418 THR n 
1 419 LEU n 
1 420 VAL n 
1 421 PRO n 
1 422 ARG n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   422 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PH1295 
_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      'Pyrococcus horikoshii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     53953 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
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 
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   GLY 2   2   2   GLY GLY A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   TYR 4   4   4   TYR TYR A . n 
A 1 5   ARG 5   5   5   ARG ARG A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  TYR 10  10  10  TYR TYR A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  HIS 32  32  32  HIS HIS A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  TYR 35  35  35  TYR TYR A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  HIS 37  37  37  HIS HIS 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  HIS 40  40  40  HIS HIS A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  PHE 46  46  46  PHE PHE A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  MET 56  56  56  MET MET A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  MET 59  59  59  MET MET A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  PHE 63  63  63  PHE PHE A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  VAL 67  67  67  VAL VAL A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  ARG 77  77  77  ARG ARG A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  TYR 89  89  89  TYR TYR A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 MET 103 103 103 MET MET A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 PRO 109 109 109 PRO PRO A . n 
A 1 110 GLY 110 110 ?   ?   ?   A . n 
A 1 111 ALA 111 111 ?   ?   ?   A . n 
A 1 112 GLY 112 112 ?   ?   ?   A . n 
A 1 113 ILE 113 113 ?   ?   ?   A . n 
A 1 114 HIS 114 114 ?   ?   ?   A . n 
A 1 115 LEU 115 115 ?   ?   ?   A . n 
A 1 116 ALA 116 116 ?   ?   ?   A . n 
A 1 117 VAL 117 117 ?   ?   ?   A . n 
A 1 118 GLY 118 118 ?   ?   ?   A . n 
A 1 119 GLY 119 119 ?   ?   ?   A . n 
A 1 120 GLN 120 120 ?   ?   ?   A . n 
A 1 121 GLN 121 121 ?   ?   ?   A . n 
A 1 122 PHE 122 122 ?   ?   ?   A . n 
A 1 123 GLN 123 123 ?   ?   ?   A . n 
A 1 124 PRO 124 124 ?   ?   ?   A . n 
A 1 125 HIS 125 125 ?   ?   ?   A . n 
A 1 126 GLN 126 126 ?   ?   ?   A . n 
A 1 127 ALA 127 127 ?   ?   ?   A . n 
A 1 128 PRO 128 128 128 PRO PRO A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 HIS 132 132 132 HIS HIS A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 PRO 139 139 139 PRO PRO A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 ASN 141 141 141 ASN ASN A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 ASN 148 148 148 ASN ASN A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 MET 169 169 169 MET MET A . n 
A 1 170 ASN 170 170 170 ASN ASN A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 GLU 172 172 172 GLU GLU A . n 
A 1 173 ASN 173 173 173 ASN ASN A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 LYS 178 178 178 LYS LYS A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLU 192 192 192 GLU GLU A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 MET 194 194 194 MET MET A . n 
A 1 195 TYR 195 195 195 TYR TYR A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 ASN 199 199 199 ASN ASN 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 MET 202 202 202 MET MET A . n 
A 1 203 GLN 203 203 203 GLN GLN A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 PHE 210 210 210 PHE PHE A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 TYR 215 215 215 TYR TYR A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 MET 217 217 217 MET MET A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 VAL 235 235 235 VAL VAL A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 VAL 246 246 246 VAL VAL A . n 
A 1 247 TYR 247 247 247 TYR TYR A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 TYR 254 254 254 TYR TYR A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 PRO 258 258 258 PRO PRO A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 LYS 263 263 263 LYS LYS A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 ASP 267 267 267 ASP ASP A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 MET 269 269 269 MET MET A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 PHE 273 273 273 PHE PHE A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 THR 275 275 275 THR THR A . n 
A 1 276 ARG 276 276 276 ARG ARG A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 THR 281 281 281 THR THR A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 PRO 283 283 283 PRO PRO A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 MET 286 286 286 MET MET A . n 
A 1 287 ARG 287 287 287 ARG ARG A . n 
A 1 288 VAL 288 288 288 VAL VAL A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 GLU 291 291 291 GLU GLU A . n 
A 1 292 MET 292 292 292 MET MET A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 ILE 294 294 294 ILE ILE A . n 
A 1 295 SER 295 295 295 SER SER A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 GLY 297 297 297 GLY GLY A . n 
A 1 298 ILE 298 298 298 ILE ILE A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 PHE 301 301 301 PHE PHE A . n 
A 1 302 THR 302 302 302 THR THR A . n 
A 1 303 LEU 303 303 303 LEU LEU A . n 
A 1 304 PRO 304 304 304 PRO PRO A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 THR 308 308 308 THR THR A . n 
A 1 309 ILE 309 309 309 ILE ILE A . n 
A 1 310 ASN 310 310 310 ASN ASN A . n 
A 1 311 MET 311 311 311 MET MET A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 THR 314 314 314 THR THR A . n 
A 1 315 ALA 315 315 315 ALA ALA A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 TYR 317 317 317 TYR TYR A . n 
A 1 318 GLN 318 318 318 GLN GLN A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 VAL 320 320 320 VAL VAL A . n 
A 1 321 CYS 321 321 321 CYS CYS A . n 
A 1 322 THR 322 322 322 THR THR A . n 
A 1 323 PHE 323 323 323 PHE PHE A . n 
A 1 324 PHE 324 324 324 PHE PHE A . n 
A 1 325 ILE 325 325 325 ILE ILE A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 ASN 327 327 327 ASN ASN A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 GLY 330 330 330 GLY GLY A . n 
A 1 331 SER 331 331 331 SER SER A . n 
A 1 332 HIS 332 332 332 HIS HIS A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 THR 334 334 334 THR THR A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 GLY 336 336 336 GLY GLY A . n 
A 1 337 GLN 337 337 337 GLN GLN A . n 
A 1 338 GLN 338 338 338 GLN GLN A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 THR 340 340 340 THR THR A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 VAL 342 342 342 VAL VAL A . n 
A 1 343 LEU 343 343 343 LEU LEU A . n 
A 1 344 THR 344 344 344 THR THR A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 SER 349 349 349 SER SER A . n 
A 1 350 ILE 350 350 350 ILE ILE A . n 
A 1 351 GLY 351 351 351 GLY GLY A . n 
A 1 352 THR 352 352 352 THR THR A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 PRO 356 356 356 PRO PRO A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 ALA 358 358 358 ALA ALA A . n 
A 1 359 GLY 359 359 359 GLY GLY A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 ILE 361 361 361 ILE ILE A . n 
A 1 362 MET 362 362 362 MET MET A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 MET 365 365 365 MET MET A . n 
A 1 366 VAL 366 366 366 VAL VAL A . n 
A 1 367 LEU 367 367 367 LEU LEU A . n 
A 1 368 HIS 368 368 368 HIS HIS A . n 
A 1 369 SER 369 369 369 SER SER A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 GLY 371 371 371 GLY GLY A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 PRO 373 373 373 PRO PRO A . n 
A 1 374 LEU 374 374 374 LEU LEU A . n 
A 1 375 THR 375 375 375 THR THR A . n 
A 1 376 ASP 376 376 376 ASP ASP A . n 
A 1 377 PRO 377 377 377 PRO PRO A . n 
A 1 378 ASN 378 378 378 ASN ASN A . n 
A 1 379 VAL 379 379 379 VAL VAL A . n 
A 1 380 ALA 380 380 380 ALA ALA A . n 
A 1 381 ALA 381 381 381 ALA ALA A . n 
A 1 382 ALA 382 382 382 ALA ALA A . n 
A 1 383 TYR 383 383 383 TYR TYR A . n 
A 1 384 ALA 384 384 384 ALA ALA A . n 
A 1 385 MET 385 385 385 MET MET A . n 
A 1 386 ILE 386 386 386 ILE ILE A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 GLY 388 388 388 GLY GLY A . n 
A 1 389 ILE 389 389 389 ILE ILE A . n 
A 1 390 ASP 390 390 390 ASP ASP A . n 
A 1 391 ALA 391 391 391 ALA ALA A . n 
A 1 392 ILE 392 392 392 ILE ILE A . n 
A 1 393 LEU 393 393 393 LEU LEU A . n 
A 1 394 ASP 394 394 394 ASP ASP A . n 
A 1 395 MET 395 395 395 MET MET A . n 
A 1 396 GLY 396 396 396 GLY GLY A . n 
A 1 397 ARG 397 397 397 ARG ARG A . n 
A 1 398 THR 398 398 398 THR THR A . n 
A 1 399 MET 399 399 399 MET MET A . n 
A 1 400 VAL 400 400 400 VAL VAL A . n 
A 1 401 ASN 401 401 401 ASN ASN A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 THR 403 403 403 THR THR A . n 
A 1 404 GLY 404 404 404 GLY GLY A . n 
A 1 405 ASP 405 405 405 ASP ASP A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 THR 407 407 407 THR THR A . n 
A 1 408 GLY 408 408 408 GLY GLY A . n 
A 1 409 THR 409 409 409 THR THR A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 ILE 411 411 411 ILE ILE A . n 
A 1 412 VAL 412 412 412 VAL VAL A . n 
A 1 413 ALA 413 413 413 ALA ALA A . n 
A 1 414 LYS 414 414 414 LYS LYS A . n 
A 1 415 THR 415 415 ?   ?   ?   A . n 
A 1 416 GLU 416 416 ?   ?   ?   A . n 
A 1 417 GLY 417 417 ?   ?   ?   A . n 
A 1 418 THR 418 418 ?   ?   ?   A . n 
A 1 419 LEU 419 419 ?   ?   ?   A . n 
A 1 420 VAL 420 420 ?   ?   ?   A . n 
A 1 421 PRO 421 421 ?   ?   ?   A . n 
A 1 422 ARG 422 422 ?   ?   ?   A . n 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BH1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9BH1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_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                   9BH1 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BH1 
_struct.title                        'Apo GltPh, intermediate outward-facing state' 
_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        9BH1 
_struct_keywords.text            'Sodium-coupled aspartate transporter, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
# 
_struct_asym.id                            A 
_struct_asym.pdbx_blank_PDB_chainid_flag   N 
_struct_asym.pdbx_modified                 N 
_struct_asym.entity_id                     1 
_struct_asym.details                       ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    GLT_PYRHO 
_struct_ref.pdbx_db_accession          O59010 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYADAVKTYVKPFGDLFVRLLKMLVMPIVFASLVVGAASISPARLGR
VGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQFQPKQAPPLVKILLDIVPTNPFGALANGQVLPTIFFAII
LGIAITYLMNSENEKVRKSAETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVKVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKKAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYSFTLPLGATINMDGTALYQGV
CTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGAIMLAMVLESVGLPLTDPNVAAAYAMILGIDAILDMGRTMV
NVTGDLTGTAIVAKTEG
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BH1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 417 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O59010 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  417 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       417 
# 
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 9BH1 HIS A 37  ? UNP O59010 ASP 37  conflict         37  1  
1 9BH1 HIS A 40  ? UNP O59010 LYS 40  conflict         40  2  
1 9BH1 HIS A 125 ? UNP O59010 LYS 125 conflict         125 3  
1 9BH1 HIS A 132 ? UNP O59010 LYS 132 conflict         132 4  
1 9BH1 HIS A 223 ? UNP O59010 LYS 223 conflict         223 5  
1 9BH1 HIS A 264 ? UNP O59010 LYS 264 conflict         264 6  
1 9BH1 HIS A 368 ? UNP O59010 GLU 368 conflict         368 7  
1 9BH1 THR A 418 ? UNP O59010 ?   ?   'expression tag' 418 8  
1 9BH1 LEU A 419 ? UNP O59010 ?   ?   'expression tag' 419 9  
1 9BH1 VAL A 420 ? UNP O59010 ?   ?   'expression tag' 420 10 
1 9BH1 PRO A 421 ? UNP O59010 ?   ?   'expression tag' 421 11 
1 9BH1 ARG A 422 ? UNP O59010 ?   ?   'expression tag' 422 12 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 2   ? TYR A 10  ? GLY A 2   TYR A 10  1 ? 9  
HELX_P HELX_P2  AA2 PRO A 11  ? GLY A 34  ? PRO A 11  GLY A 34  1 ? 24 
HELX_P HELX_P3  AA3 TYR A 35  ? VAL A 43  ? TYR A 35  VAL A 43  1 ? 9  
HELX_P HELX_P4  AA4 VAL A 43  ? SER A 72  ? VAL A 43  SER A 72  1 ? 30 
HELX_P HELX_P5  AA5 SER A 74  ? ASN A 108 ? SER A 74  ASN A 108 1 ? 35 
HELX_P HELX_P6  AA6 PRO A 129 ? ASP A 136 ? PRO A 129 ASP A 136 1 ? 8  
HELX_P HELX_P7  AA7 ASN A 141 ? ASN A 148 ? ASN A 141 ASN A 148 1 ? 8  
HELX_P HELX_P8  AA8 GLN A 150 ? ASN A 170 ? GLN A 150 ASN A 170 1 ? 21 
HELX_P HELX_P9  AA9 ASN A 173 ? GLN A 220 ? ASN A 173 GLN A 220 1 ? 48 
HELX_P HELX_P10 AB1 GLY A 226 ? VAL A 246 ? GLY A 226 VAL A 246 1 ? 21 
HELX_P HELX_P11 AB2 VAL A 246 ? TYR A 254 ? VAL A 246 TYR A 254 1 ? 9  
HELX_P HELX_P12 AB3 ASP A 257 ? ALA A 265 ? ASP A 257 ALA A 265 1 ? 9  
HELX_P HELX_P13 AB4 ALA A 265 ? THR A 275 ? ALA A 265 THR A 275 1 ? 11 
HELX_P HELX_P14 AB5 THR A 281 ? MET A 292 ? THR A 281 MET A 292 1 ? 12 
HELX_P HELX_P15 AB6 ILE A 298 ? ASN A 310 ? ILE A 298 ASN A 310 1 ? 13 
HELX_P HELX_P16 AB7 MET A 311 ? LEU A 329 ? MET A 311 LEU A 329 1 ? 19 
HELX_P HELX_P17 AB8 THR A 334 ? SER A 349 ? THR A 334 SER A 349 1 ? 16 
HELX_P HELX_P18 AB9 GLY A 357 ? VAL A 370 ? GLY A 357 VAL A 370 1 ? 14 
HELX_P HELX_P19 AC1 ASP A 376 ? LYS A 414 ? ASP A 376 LYS A 414 1 ? 39 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9BH1 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    VAL 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     246 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -124.85 
_pdbx_validate_torsion.psi             -60.97 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BH1 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9BH1 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.1 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               157756 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '20 mM Hepes/Tris, pH 7.4, and 50 mM choline chloride' 
_em_buffer.pH            7.4 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Sodium-coupled aspartate transporter, apo conditions' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BH1 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             0900 
_em_imaging.nominal_defocus_max             2100 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9BH1 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9BH1 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A GLY 110 ? A GLY 110 
3  1 Y 1 A ALA 111 ? A ALA 111 
4  1 Y 1 A GLY 112 ? A GLY 112 
5  1 Y 1 A ILE 113 ? A ILE 113 
6  1 Y 1 A HIS 114 ? A HIS 114 
7  1 Y 1 A LEU 115 ? A LEU 115 
8  1 Y 1 A ALA 116 ? A ALA 116 
9  1 Y 1 A VAL 117 ? A VAL 117 
10 1 Y 1 A GLY 118 ? A GLY 118 
11 1 Y 1 A GLY 119 ? A GLY 119 
12 1 Y 1 A GLN 120 ? A GLN 120 
13 1 Y 1 A GLN 121 ? A GLN 121 
14 1 Y 1 A PHE 122 ? A PHE 122 
15 1 Y 1 A GLN 123 ? A GLN 123 
16 1 Y 1 A PRO 124 ? A PRO 124 
17 1 Y 1 A HIS 125 ? A HIS 125 
18 1 Y 1 A GLN 126 ? A GLN 126 
19 1 Y 1 A ALA 127 ? A ALA 127 
20 1 Y 1 A THR 415 ? A THR 415 
21 1 Y 1 A GLU 416 ? A GLU 416 
22 1 Y 1 A GLY 417 ? A GLY 417 
23 1 Y 1 A THR 418 ? A THR 418 
24 1 Y 1 A LEU 419 ? A LEU 419 
25 1 Y 1 A VAL 420 ? A VAL 420 
26 1 Y 1 A PRO 421 ? A PRO 421 
27 1 Y 1 A ARG 422 ? A ARG 422 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TYR N    N N N 318 
TYR CA   C N S 319 
TYR C    C N N 320 
TYR O    O N N 321 
TYR CB   C N N 322 
TYR CG   C Y N 323 
TYR CD1  C Y N 324 
TYR CD2  C Y N 325 
TYR CE1  C Y N 326 
TYR CE2  C Y N 327 
TYR CZ   C Y N 328 
TYR OH   O N N 329 
TYR OXT  O N N 330 
TYR H    H N N 331 
TYR H2   H N N 332 
TYR HA   H N N 333 
TYR HB2  H N N 334 
TYR HB3  H N N 335 
TYR HD1  H N N 336 
TYR HD2  H N N 337 
TYR HE1  H N N 338 
TYR HE2  H N N 339 
TYR HH   H N N 340 
TYR HXT  H N N 341 
VAL N    N N N 342 
VAL CA   C N S 343 
VAL C    C N N 344 
VAL O    O N N 345 
VAL CB   C N N 346 
VAL CG1  C N N 347 
VAL CG2  C N N 348 
VAL OXT  O N N 349 
VAL H    H N N 350 
VAL H2   H N N 351 
VAL HA   H N N 352 
VAL HB   H N N 353 
VAL HG11 H N N 354 
VAL HG12 H N N 355 
VAL HG13 H N N 356 
VAL HG21 H N N 357 
VAL HG22 H N N 358 
VAL HG23 H N N 359 
VAL HXT  H N N 360 
# 
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 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TYR N   CA   sing N N 304 
TYR N   H    sing N N 305 
TYR N   H2   sing N N 306 
TYR CA  C    sing N N 307 
TYR CA  CB   sing N N 308 
TYR CA  HA   sing N N 309 
TYR C   O    doub N N 310 
TYR C   OXT  sing N N 311 
TYR CB  CG   sing N N 312 
TYR CB  HB2  sing N N 313 
TYR CB  HB3  sing N N 314 
TYR CG  CD1  doub Y N 315 
TYR CG  CD2  sing Y N 316 
TYR CD1 CE1  sing Y N 317 
TYR CD1 HD1  sing N N 318 
TYR CD2 CE2  doub Y N 319 
TYR CD2 HD2  sing N N 320 
TYR CE1 CZ   doub Y N 321 
TYR CE1 HE1  sing N N 322 
TYR CE2 CZ   sing Y N 323 
TYR CE2 HE2  sing N N 324 
TYR CZ  OH   sing N N 325 
TYR OH  HH   sing N N 326 
TYR OXT HXT  sing N N 327 
VAL N   CA   sing N N 328 
VAL N   H    sing N N 329 
VAL N   H2   sing N N 330 
VAL CA  C    sing N N 331 
VAL CA  CB   sing N N 332 
VAL CA  HA   sing N N 333 
VAL C   O    doub N N 334 
VAL C   OXT  sing N N 335 
VAL CB  CG1  sing N N 336 
VAL CB  CG2  sing N N 337 
VAL CB  HB   sing N N 338 
VAL CG1 HG11 sing N N 339 
VAL CG1 HG12 sing N N 340 
VAL CG1 HG13 sing N N 341 
VAL CG2 HG21 sing N N 342 
VAL CG2 HG22 sing N N 343 
VAL CG2 HG23 sing N N 344 
VAL OXT HXT  sing N N 345 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-04-19 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BH1 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              'Apo GltPh, intermediate outward-facing state' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          53953 
_em_entity_assembly_naturalsource.organism             'Pyrococcus horikoshii' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         53.42 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 ? ? 
MASKING                    ? 3  ? ? ? ? ? 
'CTF CORRECTION'           ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ? ? 
'MODEL FITTING'            ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ? ? 
OTHER                      ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ? ? 
CLASSIFICATION             ? 12 1 ? ? ? ? 
RECONSTRUCTION             ? 13 1 ? ? ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)' 'United States' NS134865 1 
'Howard Hughes Medical Institute (HHMI)'                                                            'United States' ?        2 
# 
_atom_sites.entry_id                    9BH1 
_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]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_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]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . GLY A 1 2   ? 179.387 126.369 165.179 1.00 131.04 ? 2   GLY A N   1 
ATOM 2    C CA  . GLY A 1 2   ? 180.482 126.875 165.985 1.00 131.04 ? 2   GLY A CA  1 
ATOM 3    C C   . GLY A 1 2   ? 181.301 127.927 165.264 1.00 131.04 ? 2   GLY A C   1 
ATOM 4    O O   . GLY A 1 2   ? 181.658 128.953 165.841 1.00 131.04 ? 2   GLY A O   1 
ATOM 5    N N   . LEU A 1 3   ? 181.599 127.669 163.989 1.00 128.84 ? 3   LEU A N   1 
ATOM 6    C CA  . LEU A 1 3   ? 182.374 128.625 163.208 1.00 128.84 ? 3   LEU A CA  1 
ATOM 7    C C   . LEU A 1 3   ? 181.633 129.949 163.072 1.00 128.84 ? 3   LEU A C   1 
ATOM 8    O O   . LEU A 1 3   ? 182.241 131.022 163.166 1.00 128.84 ? 3   LEU A O   1 
ATOM 9    C CB  . LEU A 1 3   ? 182.687 128.043 161.830 1.00 128.84 ? 3   LEU A CB  1 
ATOM 10   C CG  . LEU A 1 3   ? 183.625 128.877 160.956 1.00 128.84 ? 3   LEU A CG  1 
ATOM 11   C CD1 . LEU A 1 3   ? 185.071 128.659 161.368 1.00 128.84 ? 3   LEU A CD1 1 
ATOM 12   C CD2 . LEU A 1 3   ? 183.427 128.540 159.488 1.00 128.84 ? 3   LEU A CD2 1 
ATOM 13   N N   . TYR A 1 4   ? 180.319 129.893 162.849 1.00 120.80 ? 4   TYR A N   1 
ATOM 14   C CA  . TYR A 1 4   ? 179.538 131.117 162.717 1.00 120.80 ? 4   TYR A CA  1 
ATOM 15   C C   . TYR A 1 4   ? 179.727 132.021 163.926 1.00 120.80 ? 4   TYR A C   1 
ATOM 16   O O   . TYR A 1 4   ? 179.813 133.247 163.788 1.00 120.80 ? 4   TYR A O   1 
ATOM 17   C CB  . TYR A 1 4   ? 178.060 130.773 162.530 1.00 120.80 ? 4   TYR A CB  1 
ATOM 18   C CG  . TYR A 1 4   ? 177.134 131.965 162.598 1.00 120.80 ? 4   TYR A CG  1 
ATOM 19   C CD1 . TYR A 1 4   ? 176.608 132.393 163.808 1.00 120.80 ? 4   TYR A CD1 1 
ATOM 20   C CD2 . TYR A 1 4   ? 176.783 132.661 161.452 1.00 120.80 ? 4   TYR A CD2 1 
ATOM 21   C CE1 . TYR A 1 4   ? 175.762 133.479 163.875 1.00 120.80 ? 4   TYR A CE1 1 
ATOM 22   C CE2 . TYR A 1 4   ? 175.938 133.748 161.508 1.00 120.80 ? 4   TYR A CE2 1 
ATOM 23   C CZ  . TYR A 1 4   ? 175.430 134.153 162.722 1.00 120.80 ? 4   TYR A CZ  1 
ATOM 24   O OH  . TYR A 1 4   ? 174.587 135.236 162.784 1.00 120.80 ? 4   TYR A OH  1 
ATOM 25   N N   . ARG A 1 5   ? 179.799 131.435 165.121 1.00 121.70 ? 5   ARG A N   1 
ATOM 26   C CA  . ARG A 1 5   ? 180.017 132.238 166.318 1.00 121.70 ? 5   ARG A CA  1 
ATOM 27   C C   . ARG A 1 5   ? 181.345 132.977 166.239 1.00 121.70 ? 5   ARG A C   1 
ATOM 28   O O   . ARG A 1 5   ? 181.431 134.158 166.594 1.00 121.70 ? 5   ARG A O   1 
ATOM 29   C CB  . ARG A 1 5   ? 179.967 131.352 167.562 1.00 121.70 ? 5   ARG A CB  1 
ATOM 30   C CG  . ARG A 1 5   ? 178.559 130.972 167.998 1.00 121.70 ? 5   ARG A CG  1 
ATOM 31   C CD  . ARG A 1 5   ? 178.127 129.643 167.396 1.00 121.70 ? 5   ARG A CD  1 
ATOM 32   N NE  . ARG A 1 5   ? 176.686 129.443 167.485 1.00 121.70 ? 5   ARG A NE  1 
ATOM 33   C CZ  . ARG A 1 5   ? 175.992 128.616 166.713 1.00 121.70 ? 5   ARG A CZ  1 
ATOM 34   N NH1 . ARG A 1 5   ? 176.578 127.888 165.776 1.00 121.70 ? 5   ARG A NH1 1 
ATOM 35   N NH2 . ARG A 1 5   ? 174.677 128.518 166.886 1.00 121.70 ? 5   ARG A NH2 1 
ATOM 36   N N   . LYS A 1 6   ? 182.395 132.298 165.773 1.00 123.43 ? 6   LYS A N   1 
ATOM 37   C CA  . LYS A 1 6   ? 183.679 132.964 165.592 1.00 123.43 ? 6   LYS A CA  1 
ATOM 38   C C   . LYS A 1 6   ? 183.579 134.070 164.550 1.00 123.43 ? 6   LYS A C   1 
ATOM 39   O O   . LYS A 1 6   ? 184.155 135.150 164.721 1.00 123.43 ? 6   LYS A O   1 
ATOM 40   C CB  . LYS A 1 6   ? 184.744 131.943 165.192 1.00 123.43 ? 6   LYS A CB  1 
ATOM 41   C CG  . LYS A 1 6   ? 186.065 132.556 164.746 1.00 123.43 ? 6   LYS A CG  1 
ATOM 42   C CD  . LYS A 1 6   ? 186.167 132.636 163.229 1.00 123.43 ? 6   LYS A CD  1 
ATOM 43   C CE  . LYS A 1 6   ? 187.594 132.901 162.779 1.00 123.43 ? 6   LYS A CE  1 
ATOM 44   N NZ  . LYS A 1 6   ? 187.715 132.921 161.295 1.00 123.43 ? 6   LYS A NZ  1 
ATOM 45   N N   . TYR A 1 7   ? 182.851 133.817 163.461 1.00 101.56 ? 7   TYR A N   1 
ATOM 46   C CA  . TYR A 1 7   ? 182.733 134.813 162.401 1.00 101.56 ? 7   TYR A CA  1 
ATOM 47   C C   . TYR A 1 7   ? 182.086 136.091 162.919 1.00 101.56 ? 7   TYR A C   1 
ATOM 48   O O   . TYR A 1 7   ? 182.567 137.198 162.650 1.00 101.56 ? 7   TYR A O   1 
ATOM 49   C CB  . TYR A 1 7   ? 181.930 134.233 161.237 1.00 101.56 ? 7   TYR A CB  1 
ATOM 50   C CG  . TYR A 1 7   ? 181.493 135.252 160.209 1.00 101.56 ? 7   TYR A CG  1 
ATOM 51   C CD1 . TYR A 1 7   ? 180.287 135.924 160.339 1.00 101.56 ? 7   TYR A CD1 1 
ATOM 52   C CD2 . TYR A 1 7   ? 182.281 135.533 159.104 1.00 101.56 ? 7   TYR A CD2 1 
ATOM 53   C CE1 . TYR A 1 7   ? 179.883 136.851 159.403 1.00 101.56 ? 7   TYR A CE1 1 
ATOM 54   C CE2 . TYR A 1 7   ? 181.884 136.458 158.163 1.00 101.56 ? 7   TYR A CE2 1 
ATOM 55   C CZ  . TYR A 1 7   ? 180.684 137.114 158.318 1.00 101.56 ? 7   TYR A CZ  1 
ATOM 56   O OH  . TYR A 1 7   ? 180.280 138.039 157.384 1.00 101.56 ? 7   TYR A OH  1 
ATOM 57   N N   . ILE A 1 8   ? 180.991 135.959 163.667 1.00 101.15 ? 8   ILE A N   1 
ATOM 58   C CA  . ILE A 1 8   ? 180.314 137.139 164.193 1.00 101.15 ? 8   ILE A CA  1 
ATOM 59   C C   . ILE A 1 8   ? 181.179 137.831 165.237 1.00 101.15 ? 8   ILE A C   1 
ATOM 60   O O   . ILE A 1 8   ? 181.267 139.064 165.272 1.00 101.15 ? 8   ILE A O   1 
ATOM 61   C CB  . ILE A 1 8   ? 178.940 136.752 164.767 1.00 101.15 ? 8   ILE A CB  1 
ATOM 62   C CG1 . ILE A 1 8   ? 177.982 136.350 163.642 1.00 101.15 ? 8   ILE A CG1 1 
ATOM 63   C CG2 . ILE A 1 8   ? 178.363 137.899 165.583 1.00 101.15 ? 8   ILE A CG2 1 
ATOM 64   C CD1 . ILE A 1 8   ? 177.554 137.494 162.743 1.00 101.15 ? 8   ILE A CD1 1 
ATOM 65   N N   . GLU A 1 9   ? 181.830 137.055 166.105 1.00 119.19 ? 9   GLU A N   1 
ATOM 66   C CA  . GLU A 1 9   ? 182.632 137.651 167.167 1.00 119.19 ? 9   GLU A CA  1 
ATOM 67   C C   . GLU A 1 9   ? 183.763 138.502 166.607 1.00 119.19 ? 9   GLU A C   1 
ATOM 68   O O   . GLU A 1 9   ? 184.224 139.437 167.271 1.00 119.19 ? 9   GLU A O   1 
ATOM 69   C CB  . GLU A 1 9   ? 183.190 136.557 168.075 1.00 119.19 ? 9   GLU A CB  1 
ATOM 70   C CG  . GLU A 1 9   ? 182.174 135.996 169.055 1.00 119.19 ? 9   GLU A CG  1 
ATOM 71   C CD  . GLU A 1 9   ? 182.738 134.873 169.902 1.00 119.19 ? 9   GLU A CD  1 
ATOM 72   O OE1 . GLU A 1 9   ? 183.885 134.452 169.644 1.00 119.19 ? 9   GLU A OE1 1 
ATOM 73   O OE2 . GLU A 1 9   ? 182.034 134.410 170.824 1.00 119.19 ? 9   GLU A OE2 1 
ATOM 74   N N   . TYR A 1 10  ? 184.220 138.200 165.398 1.00 107.25 ? 10  TYR A N   1 
ATOM 75   C CA  . TYR A 1 10  ? 185.267 139.001 164.786 1.00 107.25 ? 10  TYR A CA  1 
ATOM 76   C C   . TYR A 1 10  ? 184.779 140.440 164.625 1.00 107.25 ? 10  TYR A C   1 
ATOM 77   O O   . TYR A 1 10  ? 183.617 140.660 164.264 1.00 107.25 ? 10  TYR A O   1 
ATOM 78   C CB  . TYR A 1 10  ? 185.651 138.419 163.426 1.00 107.25 ? 10  TYR A CB  1 
ATOM 79   C CG  . TYR A 1 10  ? 187.096 138.631 163.042 1.00 107.25 ? 10  TYR A CG  1 
ATOM 80   C CD1 . TYR A 1 10  ? 187.489 139.762 162.342 1.00 107.25 ? 10  TYR A CD1 1 
ATOM 81   C CD2 . TYR A 1 10  ? 188.066 137.696 163.373 1.00 107.25 ? 10  TYR A CD2 1 
ATOM 82   C CE1 . TYR A 1 10  ? 188.807 139.958 161.987 1.00 107.25 ? 10  TYR A CE1 1 
ATOM 83   C CE2 . TYR A 1 10  ? 189.387 137.884 163.022 1.00 107.25 ? 10  TYR A CE2 1 
ATOM 84   C CZ  . TYR A 1 10  ? 189.752 139.017 162.329 1.00 107.25 ? 10  TYR A CZ  1 
ATOM 85   O OH  . TYR A 1 10  ? 191.067 139.212 161.975 1.00 107.25 ? 10  TYR A OH  1 
ATOM 86   N N   . PRO A 1 11  ? 185.622 141.439 164.887 1.00 98.15  ? 11  PRO A N   1 
ATOM 87   C CA  . PRO A 1 11  ? 185.162 142.827 164.761 1.00 98.15  ? 11  PRO A CA  1 
ATOM 88   C C   . PRO A 1 11  ? 184.616 143.095 163.368 1.00 98.15  ? 11  PRO A C   1 
ATOM 89   O O   . PRO A 1 11  ? 185.190 142.671 162.363 1.00 98.15  ? 11  PRO A O   1 
ATOM 90   C CB  . PRO A 1 11  ? 186.421 143.655 165.047 1.00 98.15  ? 11  PRO A CB  1 
ATOM 91   C CG  . PRO A 1 11  ? 187.563 142.693 164.989 1.00 98.15  ? 11  PRO A CG  1 
ATOM 92   C CD  . PRO A 1 11  ? 187.011 141.366 165.367 1.00 98.15  ? 11  PRO A CD  1 
ATOM 93   N N   . VAL A 1 12  ? 183.492 143.811 163.318 1.00 86.87  ? 12  VAL A N   1 
ATOM 94   C CA  . VAL A 1 12  ? 182.774 143.974 162.056 1.00 86.87  ? 12  VAL A CA  1 
ATOM 95   C C   . VAL A 1 12  ? 183.639 144.708 161.040 1.00 86.87  ? 12  VAL A C   1 
ATOM 96   O O   . VAL A 1 12  ? 183.758 144.288 159.884 1.00 86.87  ? 12  VAL A O   1 
ATOM 97   C CB  . VAL A 1 12  ? 181.438 144.701 162.287 1.00 86.87  ? 12  VAL A CB  1 
ATOM 98   C CG1 . VAL A 1 12  ? 181.665 146.094 162.859 1.00 86.87  ? 12  VAL A CG1 1 
ATOM 99   C CG2 . VAL A 1 12  ? 180.655 144.779 160.991 1.00 86.87  ? 12  VAL A CG2 1 
ATOM 100  N N   . LEU A 1 13  ? 184.271 145.805 161.458 1.00 94.63  ? 13  LEU A N   1 
ATOM 101  C CA  . LEU A 1 13  ? 185.016 146.621 160.506 1.00 94.63  ? 13  LEU A CA  1 
ATOM 102  C C   . LEU A 1 13  ? 186.162 145.835 159.885 1.00 94.63  ? 13  LEU A C   1 
ATOM 103  O O   . LEU A 1 13  ? 186.416 145.943 158.680 1.00 94.63  ? 13  LEU A O   1 
ATOM 104  C CB  . LEU A 1 13  ? 185.537 147.883 161.191 1.00 94.63  ? 13  LEU A CB  1 
ATOM 105  C CG  . LEU A 1 13  ? 186.423 148.781 160.327 1.00 94.63  ? 13  LEU A CG  1 
ATOM 106  C CD1 . LEU A 1 13  ? 185.765 149.070 158.991 1.00 94.63  ? 13  LEU A CD1 1 
ATOM 107  C CD2 . LEU A 1 13  ? 186.732 150.074 161.058 1.00 94.63  ? 13  LEU A CD2 1 
ATOM 108  N N   . GLN A 1 14  ? 186.865 145.036 160.688 1.00 96.89  ? 14  GLN A N   1 
ATOM 109  C CA  . GLN A 1 14  ? 187.940 144.218 160.137 1.00 96.89  ? 14  GLN A CA  1 
ATOM 110  C C   . GLN A 1 14  ? 187.401 143.239 159.103 1.00 96.89  ? 14  GLN A C   1 
ATOM 111  O O   . GLN A 1 14  ? 188.018 143.032 158.052 1.00 96.89  ? 14  GLN A O   1 
ATOM 112  C CB  . GLN A 1 14  ? 188.661 143.473 161.258 1.00 96.89  ? 14  GLN A CB  1 
ATOM 113  C CG  . GLN A 1 14  ? 189.779 144.271 161.901 1.00 96.89  ? 14  GLN A CG  1 
ATOM 114  C CD  . GLN A 1 14  ? 189.326 145.645 162.346 1.00 96.89  ? 14  GLN A CD  1 
ATOM 115  O OE1 . GLN A 1 14  ? 188.158 145.847 162.678 1.00 96.89  ? 14  GLN A OE1 1 
ATOM 116  N NE2 . GLN A 1 14  ? 190.247 146.601 162.352 1.00 96.89  ? 14  GLN A NE2 1 
ATOM 117  N N   . LYS A 1 15  ? 186.247 142.629 159.379 1.00 95.88  ? 15  LYS A N   1 
ATOM 118  C CA  . LYS A 1 15  ? 185.615 141.776 158.379 1.00 95.88  ? 15  LYS A CA  1 
ATOM 119  C C   . LYS A 1 15  ? 185.276 142.572 157.128 1.00 95.88  ? 15  LYS A C   1 
ATOM 120  O O   . LYS A 1 15  ? 185.453 142.088 156.005 1.00 95.88  ? 15  LYS A O   1 
ATOM 121  C CB  . LYS A 1 15  ? 184.352 141.136 158.950 1.00 95.88  ? 15  LYS A CB  1 
ATOM 122  C CG  . LYS A 1 15  ? 184.585 140.228 160.138 1.00 95.88  ? 15  LYS A CG  1 
ATOM 123  C CD  . LYS A 1 15  ? 183.464 139.213 160.281 1.00 95.88  ? 15  LYS A CD  1 
ATOM 124  C CE  . LYS A 1 15  ? 182.152 139.869 160.687 1.00 95.88  ? 15  LYS A CE  1 
ATOM 125  N NZ  . LYS A 1 15  ? 182.053 140.052 162.159 1.00 95.88  ? 15  LYS A NZ  1 
ATOM 126  N N   . ILE A 1 16  ? 184.786 143.799 157.305 1.00 90.54  ? 16  ILE A N   1 
ATOM 127  C CA  . ILE A 1 16  ? 184.415 144.626 156.161 1.00 90.54  ? 16  ILE A CA  1 
ATOM 128  C C   . ILE A 1 16  ? 185.610 144.808 155.234 1.00 90.54  ? 16  ILE A C   1 
ATOM 129  O O   . ILE A 1 16  ? 185.519 144.587 154.021 1.00 90.54  ? 16  ILE A O   1 
ATOM 130  C CB  . ILE A 1 16  ? 183.865 145.980 156.643 1.00 90.54  ? 16  ILE A CB  1 
ATOM 131  C CG1 . ILE A 1 16  ? 182.551 145.794 157.404 1.00 90.54  ? 16  ILE A CG1 1 
ATOM 132  C CG2 . ILE A 1 16  ? 183.646 146.903 155.478 1.00 90.54  ? 16  ILE A CG2 1 
ATOM 133  C CD1 . ILE A 1 16  ? 181.364 145.498 156.528 1.00 90.54  ? 16  ILE A CD1 1 
ATOM 134  N N   . LEU A 1 17  ? 186.753 145.207 155.794 1.00 97.02  ? 17  LEU A N   1 
ATOM 135  C CA  . LEU A 1 17  ? 187.945 145.407 154.978 1.00 97.02  ? 17  LEU A CA  1 
ATOM 136  C C   . LEU A 1 17  ? 188.425 144.093 154.377 1.00 97.02  ? 17  LEU A C   1 
ATOM 137  O O   . LEU A 1 17  ? 188.816 144.039 153.206 1.00 97.02  ? 17  LEU A O   1 
ATOM 138  C CB  . LEU A 1 17  ? 189.051 146.047 155.816 1.00 97.02  ? 17  LEU A CB  1 
ATOM 139  C CG  . LEU A 1 17  ? 188.698 147.349 156.533 1.00 97.02  ? 17  LEU A CG  1 
ATOM 140  C CD1 . LEU A 1 17  ? 189.964 148.058 156.980 1.00 97.02  ? 17  LEU A CD1 1 
ATOM 141  C CD2 . LEU A 1 17  ? 187.864 148.256 155.644 1.00 97.02  ? 17  LEU A CD2 1 
ATOM 142  N N   . ILE A 1 18  ? 188.402 143.018 155.166 1.00 92.89  ? 18  ILE A N   1 
ATOM 143  C CA  . ILE A 1 18  ? 188.905 141.736 154.682 1.00 92.89  ? 18  ILE A CA  1 
ATOM 144  C C   . ILE A 1 18  ? 188.123 141.296 153.453 1.00 92.89  ? 18  ILE A C   1 
ATOM 145  O O   . ILE A 1 18  ? 188.698 140.849 152.454 1.00 92.89  ? 18  ILE A O   1 
ATOM 146  C CB  . ILE A 1 18  ? 188.843 140.678 155.798 1.00 92.89  ? 18  ILE A CB  1 
ATOM 147  C CG1 . ILE A 1 18  ? 189.930 140.937 156.844 1.00 92.89  ? 18  ILE A CG1 1 
ATOM 148  C CG2 . ILE A 1 18  ? 188.984 139.280 155.214 1.00 92.89  ? 18  ILE A CG2 1 
ATOM 149  C CD1 . ILE A 1 18  ? 191.340 140.619 156.378 1.00 92.89  ? 18  ILE A CD1 1 
ATOM 150  N N   . GLY A 1 19  ? 186.797 141.418 153.507 1.00 93.98  ? 19  GLY A N   1 
ATOM 151  C CA  . GLY A 1 19  ? 185.993 141.083 152.346 1.00 93.98  ? 19  GLY A CA  1 
ATOM 152  C C   . GLY A 1 19  ? 186.333 141.942 151.145 1.00 93.98  ? 19  GLY A C   1 
ATOM 153  O O   . GLY A 1 19  ? 186.390 141.453 150.014 1.00 93.98  ? 19  GLY A O   1 
ATOM 154  N N   . LEU A 1 20  ? 186.565 143.235 151.373 1.00 88.75  ? 20  LEU A N   1 
ATOM 155  C CA  . LEU A 1 20  ? 186.903 144.131 150.274 1.00 88.75  ? 20  LEU A CA  1 
ATOM 156  C C   . LEU A 1 20  ? 188.189 143.690 149.587 1.00 88.75  ? 20  LEU A C   1 
ATOM 157  O O   . LEU A 1 20  ? 188.239 143.565 148.359 1.00 88.75  ? 20  LEU A O   1 
ATOM 158  C CB  . LEU A 1 20  ? 187.041 145.560 150.796 1.00 88.75  ? 20  LEU A CB  1 
ATOM 159  C CG  . LEU A 1 20  ? 187.357 146.629 149.751 1.00 88.75  ? 20  LEU A CG  1 
ATOM 160  C CD1 . LEU A 1 20  ? 186.089 147.057 149.037 1.00 88.75  ? 20  LEU A CD1 1 
ATOM 161  C CD2 . LEU A 1 20  ? 188.053 147.815 150.393 1.00 88.75  ? 20  LEU A CD2 1 
ATOM 162  N N   . ILE A 1 21  ? 189.241 143.446 150.368 1.00 94.05  ? 21  ILE A N   1 
ATOM 163  C CA  . ILE A 1 21  ? 190.541 143.126 149.784 1.00 94.05  ? 21  ILE A CA  1 
ATOM 164  C C   . ILE A 1 21  ? 190.464 141.824 148.998 1.00 94.05  ? 21  ILE A C   1 
ATOM 165  O O   . ILE A 1 21  ? 190.942 141.735 147.862 1.00 94.05  ? 21  ILE A O   1 
ATOM 166  C CB  . ILE A 1 21  ? 191.617 143.062 150.882 1.00 94.05  ? 21  ILE A CB  1 
ATOM 167  C CG1 . ILE A 1 21  ? 191.892 144.462 151.432 1.00 94.05  ? 21  ILE A CG1 1 
ATOM 168  C CG2 . ILE A 1 21  ? 192.896 142.449 150.339 1.00 94.05  ? 21  ILE A CG2 1 
ATOM 169  C CD1 . ILE A 1 21  ? 192.339 144.472 152.874 1.00 94.05  ? 21  ILE A CD1 1 
ATOM 170  N N   . LEU A 1 22  ? 189.860 140.793 149.590 1.00 102.91 ? 22  LEU A N   1 
ATOM 171  C CA  . LEU A 1 22  ? 189.753 139.514 148.896 1.00 102.91 ? 22  LEU A CA  1 
ATOM 172  C C   . LEU A 1 22  ? 188.914 139.645 147.633 1.00 102.91 ? 22  LEU A C   1 
ATOM 173  O O   . LEU A 1 22  ? 189.255 139.076 146.590 1.00 102.91 ? 22  LEU A O   1 
ATOM 174  C CB  . LEU A 1 22  ? 189.154 138.457 149.824 1.00 102.91 ? 22  LEU A CB  1 
ATOM 175  C CG  . LEU A 1 22  ? 189.995 137.988 151.015 1.00 102.91 ? 22  LEU A CG  1 
ATOM 176  C CD1 . LEU A 1 22  ? 189.545 136.604 151.453 1.00 102.91 ? 22  LEU A CD1 1 
ATOM 177  C CD2 . LEU A 1 22  ? 191.486 137.988 150.705 1.00 102.91 ? 22  LEU A CD2 1 
ATOM 178  N N   . GLY A 1 23  ? 187.812 140.391 147.705 1.00 101.82 ? 23  GLY A N   1 
ATOM 179  C CA  . GLY A 1 23  ? 186.973 140.552 146.530 1.00 101.82 ? 23  GLY A CA  1 
ATOM 180  C C   . GLY A 1 23  ? 187.708 141.216 145.384 1.00 101.82 ? 23  GLY A C   1 
ATOM 181  O O   . GLY A 1 23  ? 187.650 140.757 144.241 1.00 101.82 ? 23  GLY A O   1 
ATOM 182  N N   . ALA A 1 24  ? 188.420 142.305 145.675 1.00 108.40 ? 24  ALA A N   1 
ATOM 183  C CA  . ALA A 1 24  ? 189.169 142.993 144.630 1.00 108.40 ? 24  ALA A CA  1 
ATOM 184  C C   . ALA A 1 24  ? 190.243 142.085 144.048 1.00 108.40 ? 24  ALA A C   1 
ATOM 185  O O   . ALA A 1 24  ? 190.435 142.031 142.828 1.00 108.40 ? 24  ALA A O   1 
ATOM 186  C CB  . ALA A 1 24  ? 189.787 144.275 145.184 1.00 108.40 ? 24  ALA A CB  1 
ATOM 187  N N   . ILE A 1 25  ? 190.957 141.361 144.910 1.00 110.30 ? 25  ILE A N   1 
ATOM 188  C CA  . ILE A 1 25  ? 191.964 140.420 144.430 1.00 110.30 ? 25  ILE A CA  1 
ATOM 189  C C   . ILE A 1 25  ? 191.304 139.325 143.603 1.00 110.30 ? 25  ILE A C   1 
ATOM 190  O O   . ILE A 1 25  ? 191.783 138.963 142.523 1.00 110.30 ? 25  ILE A O   1 
ATOM 191  C CB  . ILE A 1 25  ? 192.756 139.833 145.612 1.00 110.30 ? 25  ILE A CB  1 
ATOM 192  C CG1 . ILE A 1 25  ? 193.658 140.901 146.239 1.00 110.30 ? 25  ILE A CG1 1 
ATOM 193  C CG2 . ILE A 1 25  ? 193.568 138.627 145.163 1.00 110.30 ? 25  ILE A CG2 1 
ATOM 194  C CD1 . ILE A 1 25  ? 194.759 141.415 145.326 1.00 110.30 ? 25  ILE A CD1 1 
ATOM 195  N N   . VAL A 1 26  ? 190.189 138.784 144.098 1.00 108.64 ? 26  VAL A N   1 
ATOM 196  C CA  . VAL A 1 26  ? 189.495 137.731 143.363 1.00 108.64 ? 26  VAL A CA  1 
ATOM 197  C C   . VAL A 1 26  ? 188.994 138.258 142.027 1.00 108.64 ? 26  VAL A C   1 
ATOM 198  O O   . VAL A 1 26  ? 189.170 137.616 140.986 1.00 108.64 ? 26  VAL A O   1 
ATOM 199  C CB  . VAL A 1 26  ? 188.346 137.155 144.210 1.00 108.64 ? 26  VAL A CB  1 
ATOM 200  C CG1 . VAL A 1 26  ? 187.365 136.394 143.330 1.00 108.64 ? 26  VAL A CG1 1 
ATOM 201  C CG2 . VAL A 1 26  ? 188.896 136.252 145.299 1.00 108.64 ? 26  VAL A CG2 1 
ATOM 202  N N   . GLY A 1 27  ? 188.372 139.437 142.029 1.00 114.75 ? 27  GLY A N   1 
ATOM 203  C CA  . GLY A 1 27  ? 187.846 139.973 140.785 1.00 114.75 ? 27  GLY A CA  1 
ATOM 204  C C   . GLY A 1 27  ? 188.928 140.172 139.743 1.00 114.75 ? 27  GLY A C   1 
ATOM 205  O O   . GLY A 1 27  ? 188.799 139.728 138.601 1.00 114.75 ? 27  GLY A O   1 
ATOM 206  N N   . LEU A 1 28  ? 190.031 140.813 140.135 1.00 119.75 ? 28  LEU A N   1 
ATOM 207  C CA  . LEU A 1 28  ? 191.108 141.061 139.184 1.00 119.75 ? 28  LEU A CA  1 
ATOM 208  C C   . LEU A 1 28  ? 191.668 139.760 138.628 1.00 119.75 ? 28  LEU A C   1 
ATOM 209  O O   . LEU A 1 28  ? 192.133 139.725 137.483 1.00 119.75 ? 28  LEU A O   1 
ATOM 210  C CB  . LEU A 1 28  ? 192.217 141.877 139.850 1.00 119.75 ? 28  LEU A CB  1 
ATOM 211  C CG  . LEU A 1 28  ? 192.006 143.388 140.013 1.00 119.75 ? 28  LEU A CG  1 
ATOM 212  C CD1 . LEU A 1 28  ? 193.320 144.054 140.390 1.00 119.75 ? 28  LEU A CD1 1 
ATOM 213  C CD2 . LEU A 1 28  ? 191.428 144.038 138.762 1.00 119.75 ? 28  LEU A CD2 1 
ATOM 214  N N   . ILE A 1 29  ? 191.634 138.682 139.414 1.00 125.52 ? 29  ILE A N   1 
ATOM 215  C CA  . ILE A 1 29  ? 192.099 137.391 138.916 1.00 125.52 ? 29  ILE A CA  1 
ATOM 216  C C   . ILE A 1 29  ? 191.255 136.954 137.726 1.00 125.52 ? 29  ILE A C   1 
ATOM 217  O O   . ILE A 1 29  ? 191.779 136.526 136.691 1.00 125.52 ? 29  ILE A O   1 
ATOM 218  C CB  . ILE A 1 29  ? 192.075 136.340 140.041 1.00 125.52 ? 29  ILE A CB  1 
ATOM 219  C CG1 . ILE A 1 29  ? 193.240 136.571 141.006 1.00 125.52 ? 29  ILE A CG1 1 
ATOM 220  C CG2 . ILE A 1 29  ? 192.139 134.934 139.463 1.00 125.52 ? 29  ILE A CG2 1 
ATOM 221  C CD1 . ILE A 1 29  ? 193.093 135.851 142.330 1.00 125.52 ? 29  ILE A CD1 1 
ATOM 222  N N   . LEU A 1 30  ? 189.931 137.063 137.853 1.00 124.54 ? 30  LEU A N   1 
ATOM 223  C CA  . LEU A 1 30  ? 189.053 136.706 136.744 1.00 124.54 ? 30  LEU A CA  1 
ATOM 224  C C   . LEU A 1 30  ? 189.200 137.674 135.579 1.00 124.54 ? 30  LEU A C   1 
ATOM 225  O O   . LEU A 1 30  ? 188.889 137.319 134.437 1.00 124.54 ? 30  LEU A O   1 
ATOM 226  C CB  . LEU A 1 30  ? 187.601 136.653 137.216 1.00 124.54 ? 30  LEU A CB  1 
ATOM 227  C CG  . LEU A 1 30  ? 187.181 135.478 138.108 1.00 124.54 ? 30  LEU A CG  1 
ATOM 228  C CD1 . LEU A 1 30  ? 188.231 135.093 139.136 1.00 124.54 ? 30  LEU A CD1 1 
ATOM 229  C CD2 . LEU A 1 30  ? 185.874 135.815 138.799 1.00 124.54 ? 30  LEU A CD2 1 
ATOM 230  N N   . GLY A 1 31  ? 189.674 138.891 135.838 1.00 127.64 ? 31  GLY A N   1 
ATOM 231  C CA  . GLY A 1 31  ? 189.927 139.814 134.747 1.00 127.64 ? 31  GLY A CA  1 
ATOM 232  C C   . GLY A 1 31  ? 190.925 139.267 133.748 1.00 127.64 ? 31  GLY A C   1 
ATOM 233  O O   . GLY A 1 31  ? 190.788 139.486 132.541 1.00 127.64 ? 31  GLY A O   1 
ATOM 234  N N   . HIS A 1 32  ? 191.937 138.548 134.231 1.00 141.83 ? 32  HIS A N   1 
ATOM 235  C CA  . HIS A 1 32  ? 192.913 137.891 133.374 1.00 141.83 ? 32  HIS A CA  1 
ATOM 236  C C   . HIS A 1 32  ? 192.534 136.458 133.035 1.00 141.83 ? 32  HIS A C   1 
ATOM 237  O O   . HIS A 1 32  ? 192.834 135.996 131.929 1.00 141.83 ? 32  HIS A O   1 
ATOM 238  C CB  . HIS A 1 32  ? 194.292 137.903 134.045 1.00 141.83 ? 32  HIS A CB  1 
ATOM 239  C CG  . HIS A 1 32  ? 195.174 136.763 133.640 1.00 141.83 ? 32  HIS A CG  1 
ATOM 240  N ND1 . HIS A 1 32  ? 195.421 136.443 132.322 1.00 141.83 ? 32  HIS A ND1 1 
ATOM 241  C CD2 . HIS A 1 32  ? 195.867 135.867 134.381 1.00 141.83 ? 32  HIS A CD2 1 
ATOM 242  C CE1 . HIS A 1 32  ? 196.229 135.399 132.269 1.00 141.83 ? 32  HIS A CE1 1 
ATOM 243  N NE2 . HIS A 1 32  ? 196.515 135.030 133.505 1.00 141.83 ? 32  HIS A NE2 1 
ATOM 244  N N   . TYR A 1 33  ? 191.882 135.746 133.954 1.00 134.93 ? 33  TYR A N   1 
ATOM 245  C CA  . TYR A 1 33  ? 191.455 134.376 133.704 1.00 134.93 ? 33  TYR A CA  1 
ATOM 246  C C   . TYR A 1 33  ? 190.130 134.291 132.962 1.00 134.93 ? 33  TYR A C   1 
ATOM 247  O O   . TYR A 1 33  ? 189.715 133.185 132.599 1.00 134.93 ? 33  TYR A O   1 
ATOM 248  C CB  . TYR A 1 33  ? 191.331 133.612 135.024 1.00 134.93 ? 33  TYR A CB  1 
ATOM 249  C CG  . TYR A 1 33  ? 192.615 132.975 135.495 1.00 134.93 ? 33  TYR A CG  1 
ATOM 250  C CD1 . TYR A 1 33  ? 193.704 133.750 135.867 1.00 134.93 ? 33  TYR A CD1 1 
ATOM 251  C CD2 . TYR A 1 33  ? 192.737 131.595 135.572 1.00 134.93 ? 33  TYR A CD2 1 
ATOM 252  C CE1 . TYR A 1 33  ? 194.879 133.169 136.300 1.00 134.93 ? 33  TYR A CE1 1 
ATOM 253  C CE2 . TYR A 1 33  ? 193.908 131.004 136.003 1.00 134.93 ? 33  TYR A CE2 1 
ATOM 254  C CZ  . TYR A 1 33  ? 194.976 131.796 136.366 1.00 134.93 ? 33  TYR A CZ  1 
ATOM 255  O OH  . TYR A 1 33  ? 196.144 131.212 136.797 1.00 134.93 ? 33  TYR A OH  1 
ATOM 256  N N   . GLY A 1 34  ? 189.458 135.415 132.730 1.00 139.03 ? 34  GLY A N   1 
ATOM 257  C CA  . GLY A 1 34  ? 188.130 135.369 132.152 1.00 139.03 ? 34  GLY A CA  1 
ATOM 258  C C   . GLY A 1 34  ? 187.081 135.051 133.206 1.00 139.03 ? 34  GLY A C   1 
ATOM 259  O O   . GLY A 1 34  ? 187.203 135.420 134.374 1.00 139.03 ? 34  GLY A O   1 
ATOM 260  N N   . TYR A 1 35  ? 186.035 134.348 132.779 1.00 125.77 ? 35  TYR A N   1 
ATOM 261  C CA  . TYR A 1 35  ? 184.925 133.981 133.652 1.00 125.77 ? 35  TYR A CA  1 
ATOM 262  C C   . TYR A 1 35  ? 184.207 135.201 134.215 1.00 125.77 ? 35  TYR A C   1 
ATOM 263  O O   . TYR A 1 35  ? 183.523 135.104 135.239 1.00 125.77 ? 35  TYR A O   1 
ATOM 264  C CB  . TYR A 1 35  ? 185.395 133.082 134.802 1.00 125.77 ? 35  TYR A CB  1 
ATOM 265  C CG  . TYR A 1 35  ? 186.297 131.949 134.374 1.00 125.77 ? 35  TYR A CG  1 
ATOM 266  C CD1 . TYR A 1 35  ? 185.815 130.915 133.583 1.00 125.77 ? 35  TYR A CD1 1 
ATOM 267  C CD2 . TYR A 1 35  ? 187.627 131.907 134.767 1.00 125.77 ? 35  TYR A CD2 1 
ATOM 268  C CE1 . TYR A 1 35  ? 186.633 129.874 133.191 1.00 125.77 ? 35  TYR A CE1 1 
ATOM 269  C CE2 . TYR A 1 35  ? 188.453 130.869 134.380 1.00 125.77 ? 35  TYR A CE2 1 
ATOM 270  C CZ  . TYR A 1 35  ? 187.951 129.856 133.592 1.00 125.77 ? 35  TYR A CZ  1 
ATOM 271  O OH  . TYR A 1 35  ? 188.768 128.820 133.202 1.00 125.77 ? 35  TYR A OH  1 
ATOM 272  N N   . ALA A 1 36  ? 184.348 136.359 133.567 1.00 121.86 ? 36  ALA A N   1 
ATOM 273  C CA  . ALA A 1 36  ? 183.625 137.541 134.021 1.00 121.86 ? 36  ALA A CA  1 
ATOM 274  C C   . ALA A 1 36  ? 182.123 137.305 134.012 1.00 121.86 ? 36  ALA A C   1 
ATOM 275  O O   . ALA A 1 36  ? 181.398 137.878 134.833 1.00 121.86 ? 36  ALA A O   1 
ATOM 276  C CB  . ALA A 1 36  ? 183.978 138.743 133.145 1.00 121.86 ? 36  ALA A CB  1 
ATOM 277  N N   . HIS A 1 37  ? 181.636 136.475 133.088 1.00 124.32 ? 37  HIS A N   1 
ATOM 278  C CA  . HIS A 1 37  ? 180.224 136.113 133.095 1.00 124.32 ? 37  HIS A CA  1 
ATOM 279  C C   . HIS A 1 37  ? 179.879 135.275 134.319 1.00 124.32 ? 37  HIS A C   1 
ATOM 280  O O   . HIS A 1 37  ? 178.826 135.472 134.937 1.00 124.32 ? 37  HIS A O   1 
ATOM 281  C CB  . HIS A 1 37  ? 179.874 135.358 131.814 1.00 124.32 ? 37  HIS A CB  1 
ATOM 282  C CG  . HIS A 1 37  ? 178.405 135.159 131.613 1.00 124.32 ? 37  HIS A CG  1 
ATOM 283  N ND1 . HIS A 1 37  ? 177.893 134.384 130.594 1.00 124.32 ? 37  HIS A ND1 1 
ATOM 284  C CD2 . HIS A 1 37  ? 177.337 135.634 132.297 1.00 124.32 ? 37  HIS A CD2 1 
ATOM 285  C CE1 . HIS A 1 37  ? 176.573 134.389 130.661 1.00 124.32 ? 37  HIS A CE1 1 
ATOM 286  N NE2 . HIS A 1 37  ? 176.211 135.140 131.685 1.00 124.32 ? 37  HIS A NE2 1 
ATOM 287  N N   . ALA A 1 38  ? 180.754 134.337 134.688 1.00 121.31 ? 38  ALA A N   1 
ATOM 288  C CA  . ALA A 1 38  ? 180.456 133.448 135.806 1.00 121.31 ? 38  ALA A CA  1 
ATOM 289  C C   . ALA A 1 38  ? 180.303 134.224 137.107 1.00 121.31 ? 38  ALA A C   1 
ATOM 290  O O   . ALA A 1 38  ? 179.362 133.983 137.872 1.00 121.31 ? 38  ALA A O   1 
ATOM 291  C CB  . ALA A 1 38  ? 181.551 132.392 135.941 1.00 121.31 ? 38  ALA A CB  1 
ATOM 292  N N   . VAL A 1 39  ? 181.215 135.159 137.377 1.00 115.92 ? 39  VAL A N   1 
ATOM 293  C CA  . VAL A 1 39  ? 181.109 135.961 138.591 1.00 115.92 ? 39  VAL A CA  1 
ATOM 294  C C   . VAL A 1 39  ? 179.852 136.819 138.551 1.00 115.92 ? 39  VAL A C   1 
ATOM 295  O O   . VAL A 1 39  ? 179.146 136.957 139.557 1.00 115.92 ? 39  VAL A O   1 
ATOM 296  C CB  . VAL A 1 39  ? 182.377 136.815 138.779 1.00 115.92 ? 39  VAL A CB  1 
ATOM 297  C CG1 . VAL A 1 39  ? 182.561 137.770 137.618 1.00 115.92 ? 39  VAL A CG1 1 
ATOM 298  C CG2 . VAL A 1 39  ? 182.331 137.573 140.097 1.00 115.92 ? 39  VAL A CG2 1 
ATOM 299  N N   . HIS A 1 40  ? 179.546 137.404 137.392 1.00 116.49 ? 40  HIS A N   1 
ATOM 300  C CA  . HIS A 1 40  ? 178.331 138.200 137.273 1.00 116.49 ? 40  HIS A CA  1 
ATOM 301  C C   . HIS A 1 40  ? 177.086 137.359 137.515 1.00 116.49 ? 40  HIS A C   1 
ATOM 302  O O   . HIS A 1 40  ? 176.029 137.900 137.855 1.00 116.49 ? 40  HIS A O   1 
ATOM 303  C CB  . HIS A 1 40  ? 178.263 138.850 135.893 1.00 116.49 ? 40  HIS A CB  1 
ATOM 304  C CG  . HIS A 1 40  ? 176.903 139.363 135.539 1.00 116.49 ? 40  HIS A CG  1 
ATOM 305  N ND1 . HIS A 1 40  ? 175.988 138.615 134.830 1.00 116.49 ? 40  HIS A ND1 1 
ATOM 306  C CD2 . HIS A 1 40  ? 176.298 140.544 135.805 1.00 116.49 ? 40  HIS A CD2 1 
ATOM 307  C CE1 . HIS A 1 40  ? 174.880 139.316 134.670 1.00 116.49 ? 40  HIS A CE1 1 
ATOM 308  N NE2 . HIS A 1 40  ? 175.042 140.490 135.252 1.00 116.49 ? 40  HIS A NE2 1 
ATOM 309  N N   . THR A 1 41  ? 177.188 136.042 137.346 1.00 112.37 ? 41  THR A N   1 
ATOM 310  C CA  . THR A 1 41  ? 176.040 135.156 137.500 1.00 112.37 ? 41  THR A CA  1 
ATOM 311  C C   . THR A 1 41  ? 175.948 134.591 138.915 1.00 112.37 ? 41  THR A C   1 
ATOM 312  O O   . THR A 1 41  ? 174.934 134.767 139.596 1.00 112.37 ? 41  THR A O   1 
ATOM 313  C CB  . THR A 1 41  ? 176.121 134.018 136.476 1.00 112.37 ? 41  THR A CB  1 
ATOM 314  O OG1 . THR A 1 41  ? 175.815 134.525 135.171 1.00 112.37 ? 41  THR A OG1 1 
ATOM 315  C CG2 . THR A 1 41  ? 175.148 132.902 136.826 1.00 112.37 ? 41  THR A CG2 1 
ATOM 316  N N   . TYR A 1 42  ? 177.000 133.911 139.368 1.00 118.61 ? 42  TYR A N   1 
ATOM 317  C CA  . TYR A 1 42  ? 176.948 133.176 140.624 1.00 118.61 ? 42  TYR A CA  1 
ATOM 318  C C   . TYR A 1 42  ? 177.444 133.973 141.823 1.00 118.61 ? 42  TYR A C   1 
ATOM 319  O O   . TYR A 1 42  ? 177.204 133.556 142.961 1.00 118.61 ? 42  TYR A O   1 
ATOM 320  C CB  . TYR A 1 42  ? 177.772 131.891 140.509 1.00 118.61 ? 42  TYR A CB  1 
ATOM 321  C CG  . TYR A 1 42  ? 177.308 130.975 139.402 1.00 118.61 ? 42  TYR A CG  1 
ATOM 322  C CD1 . TYR A 1 42  ? 176.154 130.219 139.541 1.00 118.61 ? 42  TYR A CD1 1 
ATOM 323  C CD2 . TYR A 1 42  ? 178.021 130.871 138.218 1.00 118.61 ? 42  TYR A CD2 1 
ATOM 324  C CE1 . TYR A 1 42  ? 175.725 129.381 138.532 1.00 118.61 ? 42  TYR A CE1 1 
ATOM 325  C CE2 . TYR A 1 42  ? 177.600 130.037 137.203 1.00 118.61 ? 42  TYR A CE2 1 
ATOM 326  C CZ  . TYR A 1 42  ? 176.451 129.294 137.365 1.00 118.61 ? 42  TYR A CZ  1 
ATOM 327  O OH  . TYR A 1 42  ? 176.026 128.460 136.356 1.00 118.61 ? 42  TYR A OH  1 
ATOM 328  N N   . VAL A 1 43  ? 178.124 135.094 141.608 1.00 99.21  ? 43  VAL A N   1 
ATOM 329  C CA  . VAL A 1 43  ? 178.703 135.887 142.685 1.00 99.21  ? 43  VAL A CA  1 
ATOM 330  C C   . VAL A 1 43  ? 177.962 137.205 142.867 1.00 99.21  ? 43  VAL A C   1 
ATOM 331  O O   . VAL A 1 43  ? 177.645 137.598 143.989 1.00 99.21  ? 43  VAL A O   1 
ATOM 332  C CB  . VAL A 1 43  ? 180.209 136.131 142.441 1.00 99.21  ? 43  VAL A CB  1 
ATOM 333  C CG1 . VAL A 1 43  ? 180.782 137.031 143.521 1.00 99.21  ? 43  VAL A CG1 1 
ATOM 334  C CG2 . VAL A 1 43  ? 180.956 134.810 142.388 1.00 99.21  ? 43  VAL A CG2 1 
ATOM 335  N N   . LYS A 1 44  ? 177.677 137.902 141.770 1.00 99.98  ? 44  LYS A N   1 
ATOM 336  C CA  . LYS A 1 44  ? 177.011 139.199 141.857 1.00 99.98  ? 44  LYS A CA  1 
ATOM 337  C C   . LYS A 1 44  ? 175.716 139.155 142.656 1.00 99.98  ? 44  LYS A C   1 
ATOM 338  O O   . LYS A 1 44  ? 175.468 140.090 143.433 1.00 99.98  ? 44  LYS A O   1 
ATOM 339  C CB  . LYS A 1 44  ? 176.751 139.735 140.444 1.00 99.98  ? 44  LYS A CB  1 
ATOM 340  C CG  . LYS A 1 44  ? 176.076 141.095 140.422 1.00 99.98  ? 44  LYS A CG  1 
ATOM 341  C CD  . LYS A 1 44  ? 175.889 141.598 139.004 1.00 99.98  ? 44  LYS A CD  1 
ATOM 342  C CE  . LYS A 1 44  ? 174.906 142.753 138.954 1.00 99.98  ? 44  LYS A CE  1 
ATOM 343  N NZ  . LYS A 1 44  ? 175.259 143.822 139.927 1.00 99.98  ? 44  LYS A NZ  1 
ATOM 344  N N   . PRO A 1 45  ? 174.859 138.139 142.522 1.00 92.60  ? 45  PRO A N   1 
ATOM 345  C CA  . PRO A 1 45  ? 173.596 138.158 143.280 1.00 92.60  ? 45  PRO A CA  1 
ATOM 346  C C   . PRO A 1 45  ? 173.791 138.361 144.771 1.00 92.60  ? 45  PRO A C   1 
ATOM 347  O O   . PRO A 1 45  ? 172.980 139.044 145.407 1.00 92.60  ? 45  PRO A O   1 
ATOM 348  C CB  . PRO A 1 45  ? 172.984 136.788 142.966 1.00 92.60  ? 45  PRO A CB  1 
ATOM 349  C CG  . PRO A 1 45  ? 173.561 136.403 141.661 1.00 92.60  ? 45  PRO A CG  1 
ATOM 350  C CD  . PRO A 1 45  ? 174.937 136.987 141.609 1.00 92.60  ? 45  PRO A CD  1 
ATOM 351  N N   . PHE A 1 46  ? 174.848 137.791 145.351 1.00 81.37  ? 46  PHE A N   1 
ATOM 352  C CA  . PHE A 1 46  ? 175.141 138.052 146.756 1.00 81.37  ? 46  PHE A CA  1 
ATOM 353  C C   . PHE A 1 46  ? 175.388 139.535 146.986 1.00 81.37  ? 46  PHE A C   1 
ATOM 354  O O   . PHE A 1 46  ? 174.905 140.114 147.965 1.00 81.37  ? 46  PHE A O   1 
ATOM 355  C CB  . PHE A 1 46  ? 176.348 137.231 147.202 1.00 81.37  ? 46  PHE A CB  1 
ATOM 356  C CG  . PHE A 1 46  ? 176.079 135.760 147.289 1.00 81.37  ? 46  PHE A CG  1 
ATOM 357  C CD1 . PHE A 1 46  ? 175.121 135.269 148.156 1.00 81.37  ? 46  PHE A CD1 1 
ATOM 358  C CD2 . PHE A 1 46  ? 176.784 134.867 146.504 1.00 81.37  ? 46  PHE A CD2 1 
ATOM 359  C CE1 . PHE A 1 46  ? 174.872 133.918 148.239 1.00 81.37  ? 46  PHE A CE1 1 
ATOM 360  C CE2 . PHE A 1 46  ? 176.538 133.514 146.582 1.00 81.37  ? 46  PHE A CE2 1 
ATOM 361  C CZ  . PHE A 1 46  ? 175.581 133.038 147.451 1.00 81.37  ? 46  PHE A CZ  1 
ATOM 362  N N   . GLY A 1 47  ? 176.141 140.169 146.088 1.00 90.84  ? 47  GLY A N   1 
ATOM 363  C CA  . GLY A 1 47  ? 176.317 141.608 146.178 1.00 90.84  ? 47  GLY A CA  1 
ATOM 364  C C   . GLY A 1 47  ? 175.012 142.356 145.997 1.00 90.84  ? 47  GLY A C   1 
ATOM 365  O O   . GLY A 1 47  ? 174.751 143.346 146.685 1.00 90.84  ? 47  GLY A O   1 
ATOM 366  N N   . ASP A 1 48  ? 174.170 141.892 145.073 1.00 96.39  ? 48  ASP A N   1 
ATOM 367  C CA  . ASP A 1 48  ? 172.872 142.526 144.871 1.00 96.39  ? 48  ASP A CA  1 
ATOM 368  C C   . ASP A 1 48  ? 172.031 142.448 146.137 1.00 96.39  ? 48  ASP A C   1 
ATOM 369  O O   . ASP A 1 48  ? 171.352 143.411 146.507 1.00 96.39  ? 48  ASP A O   1 
ATOM 370  C CB  . ASP A 1 48  ? 172.144 141.865 143.700 1.00 96.39  ? 48  ASP A CB  1 
ATOM 371  C CG  . ASP A 1 48  ? 172.581 142.412 142.357 1.00 96.39  ? 48  ASP A CG  1 
ATOM 372  O OD1 . ASP A 1 48  ? 173.550 143.199 142.318 1.00 96.39  ? 48  ASP A OD1 1 
ATOM 373  O OD2 . ASP A 1 48  ? 171.955 142.054 141.338 1.00 96.39  ? 48  ASP A OD2 1 
ATOM 374  N N   . LEU A 1 49  ? 172.068 141.302 146.818 1.00 83.24  ? 49  LEU A N   1 
ATOM 375  C CA  . LEU A 1 49  ? 171.325 141.168 148.065 1.00 83.24  ? 49  LEU A CA  1 
ATOM 376  C C   . LEU A 1 49  ? 171.796 142.188 149.090 1.00 83.24  ? 49  LEU A C   1 
ATOM 377  O O   . LEU A 1 49  ? 170.980 142.811 149.778 1.00 83.24  ? 49  LEU A O   1 
ATOM 378  C CB  . LEU A 1 49  ? 171.478 139.750 148.611 1.00 83.24  ? 49  LEU A CB  1 
ATOM 379  C CG  . LEU A 1 49  ? 170.883 139.495 149.995 1.00 83.24  ? 49  LEU A CG  1 
ATOM 380  C CD1 . LEU A 1 49  ? 169.404 139.831 150.013 1.00 83.24  ? 49  LEU A CD1 1 
ATOM 381  C CD2 . LEU A 1 49  ? 171.110 138.054 150.405 1.00 83.24  ? 49  LEU A CD2 1 
ATOM 382  N N   . PHE A 1 50  ? 173.112 142.375 149.206 1.00 82.88  ? 50  PHE A N   1 
ATOM 383  C CA  . PHE A 1 50  ? 173.632 143.379 150.126 1.00 82.88  ? 50  PHE A CA  1 
ATOM 384  C C   . PHE A 1 50  ? 173.153 144.770 149.740 1.00 82.88  ? 50  PHE A C   1 
ATOM 385  O O   . PHE A 1 50  ? 172.764 145.564 150.603 1.00 82.88  ? 50  PHE A O   1 
ATOM 386  C CB  . PHE A 1 50  ? 175.156 143.326 150.148 1.00 82.88  ? 50  PHE A CB  1 
ATOM 387  C CG  . PHE A 1 50  ? 175.784 144.347 151.047 1.00 82.88  ? 50  PHE A CG  1 
ATOM 388  C CD1 . PHE A 1 50  ? 175.390 144.462 152.367 1.00 82.88  ? 50  PHE A CD1 1 
ATOM 389  C CD2 . PHE A 1 50  ? 176.769 145.194 150.573 1.00 82.88  ? 50  PHE A CD2 1 
ATOM 390  C CE1 . PHE A 1 50  ? 175.967 145.399 153.195 1.00 82.88  ? 50  PHE A CE1 1 
ATOM 391  C CE2 . PHE A 1 50  ? 177.348 146.133 151.398 1.00 82.88  ? 50  PHE A CE2 1 
ATOM 392  C CZ  . PHE A 1 50  ? 176.946 146.235 152.710 1.00 82.88  ? 50  PHE A CZ  1 
ATOM 393  N N   . VAL A 1 51  ? 173.173 145.084 148.444 1.00 84.09  ? 51  VAL A N   1 
ATOM 394  C CA  . VAL A 1 51  ? 172.657 146.369 147.989 1.00 84.09  ? 51  VAL A CA  1 
ATOM 395  C C   . VAL A 1 51  ? 171.177 146.490 148.324 1.00 84.09  ? 51  VAL A C   1 
ATOM 396  O O   . VAL A 1 51  ? 170.714 147.537 148.790 1.00 84.09  ? 51  VAL A O   1 
ATOM 397  C CB  . VAL A 1 51  ? 172.913 146.540 146.481 1.00 84.09  ? 51  VAL A CB  1 
ATOM 398  C CG1 . VAL A 1 51  ? 172.022 147.627 145.906 1.00 84.09  ? 51  VAL A CG1 1 
ATOM 399  C CG2 . VAL A 1 51  ? 174.377 146.854 146.230 1.00 84.09  ? 51  VAL A CG2 1 
ATOM 400  N N   . ARG A 1 52  ? 170.413 145.421 148.096 1.00 82.43  ? 52  ARG A N   1 
ATOM 401  C CA  . ARG A 1 52  ? 168.993 145.451 148.427 1.00 82.43  ? 52  ARG A CA  1 
ATOM 402  C C   . ARG A 1 52  ? 168.786 145.692 149.914 1.00 82.43  ? 52  ARG A C   1 
ATOM 403  O O   . ARG A 1 52  ? 167.916 146.477 150.308 1.00 82.43  ? 52  ARG A O   1 
ATOM 404  C CB  . ARG A 1 52  ? 168.328 144.143 148.002 1.00 82.43  ? 52  ARG A CB  1 
ATOM 405  C CG  . ARG A 1 52  ? 168.281 143.932 146.501 1.00 82.43  ? 52  ARG A CG  1 
ATOM 406  C CD  . ARG A 1 52  ? 166.979 144.438 145.916 1.00 82.43  ? 52  ARG A CD  1 
ATOM 407  N NE  . ARG A 1 52  ? 165.870 143.535 146.192 1.00 82.43  ? 52  ARG A NE  1 
ATOM 408  C CZ  . ARG A 1 52  ? 164.698 143.576 145.574 1.00 82.43  ? 52  ARG A CZ  1 
ATOM 409  N NH1 . ARG A 1 52  ? 164.443 144.470 144.633 1.00 82.43  ? 52  ARG A NH1 1 
ATOM 410  N NH2 . ARG A 1 52  ? 163.756 142.699 145.908 1.00 82.43  ? 52  ARG A NH2 1 
ATOM 411  N N   . LEU A 1 53  ? 169.578 145.029 150.758 1.00 80.48  ? 53  LEU A N   1 
ATOM 412  C CA  . LEU A 1 53  ? 169.444 145.227 152.195 1.00 80.48  ? 53  LEU A CA  1 
ATOM 413  C C   . LEU A 1 53  ? 169.719 146.674 152.576 1.00 80.48  ? 53  LEU A C   1 
ATOM 414  O O   . LEU A 1 53  ? 168.994 147.259 153.389 1.00 80.48  ? 53  LEU A O   1 
ATOM 415  C CB  . LEU A 1 53  ? 170.390 144.290 152.943 1.00 80.48  ? 53  LEU A CB  1 
ATOM 416  C CG  . LEU A 1 53  ? 169.968 142.822 152.984 1.00 80.48  ? 53  LEU A CG  1 
ATOM 417  C CD1 . LEU A 1 53  ? 171.146 141.941 153.347 1.00 80.48  ? 53  LEU A CD1 1 
ATOM 418  C CD2 . LEU A 1 53  ? 168.832 142.626 153.967 1.00 80.48  ? 53  LEU A CD2 1 
ATOM 419  N N   . LEU A 1 54  ? 170.761 147.272 151.998 1.00 85.07  ? 54  LEU A N   1 
ATOM 420  C CA  . LEU A 1 54  ? 171.080 148.659 152.316 1.00 85.07  ? 54  LEU A CA  1 
ATOM 421  C C   . LEU A 1 54  ? 169.974 149.599 151.855 1.00 85.07  ? 54  LEU A C   1 
ATOM 422  O O   . LEU A 1 54  ? 169.640 150.561 152.555 1.00 85.07  ? 54  LEU A O   1 
ATOM 423  C CB  . LEU A 1 54  ? 172.413 149.046 151.682 1.00 85.07  ? 54  LEU A CB  1 
ATOM 424  C CG  . LEU A 1 54  ? 173.650 148.380 152.286 1.00 85.07  ? 54  LEU A CG  1 
ATOM 425  C CD1 . LEU A 1 54  ? 174.890 148.778 151.504 1.00 85.07  ? 54  LEU A CD1 1 
ATOM 426  C CD2 . LEU A 1 54  ? 173.797 148.732 153.758 1.00 85.07  ? 54  LEU A CD2 1 
ATOM 427  N N   . LYS A 1 55  ? 169.397 149.342 150.681 1.00 79.49  ? 55  LYS A N   1 
ATOM 428  C CA  . LYS A 1 55  ? 168.291 150.170 150.213 1.00 79.49  ? 55  LYS A CA  1 
ATOM 429  C C   . LYS A 1 55  ? 167.100 150.070 151.155 1.00 79.49  ? 55  LYS A C   1 
ATOM 430  O O   . LYS A 1 55  ? 166.389 151.056 151.379 1.00 79.49  ? 55  LYS A O   1 
ATOM 431  C CB  . LYS A 1 55  ? 167.888 149.757 148.799 1.00 79.49  ? 55  LYS A CB  1 
ATOM 432  C CG  . LYS A 1 55  ? 168.818 150.271 147.716 1.00 79.49  ? 55  LYS A CG  1 
ATOM 433  C CD  . LYS A 1 55  ? 168.534 149.605 146.383 1.00 79.49  ? 55  LYS A CD  1 
ATOM 434  C CE  . LYS A 1 55  ? 169.304 150.269 145.258 1.00 79.49  ? 55  LYS A CE  1 
ATOM 435  N NZ  . LYS A 1 55  ? 168.510 151.342 144.604 1.00 79.49  ? 55  LYS A NZ  1 
ATOM 436  N N   . MET A 1 56  ? 166.865 148.883 151.715 1.00 82.55  ? 56  MET A N   1 
ATOM 437  C CA  . MET A 1 56  ? 165.734 148.699 152.617 1.00 82.55  ? 56  MET A CA  1 
ATOM 438  C C   . MET A 1 56  ? 165.852 149.601 153.837 1.00 82.55  ? 56  MET A C   1 
ATOM 439  O O   . MET A 1 56  ? 164.858 150.178 154.291 1.00 82.55  ? 56  MET A O   1 
ATOM 440  C CB  . MET A 1 56  ? 165.647 147.231 153.038 1.00 82.55  ? 56  MET A CB  1 
ATOM 441  C CG  . MET A 1 56  ? 164.790 146.957 154.267 1.00 82.55  ? 56  MET A CG  1 
ATOM 442  S SD  . MET A 1 56  ? 164.916 145.245 154.808 1.00 82.55  ? 56  MET A SD  1 
ATOM 443  C CE  . MET A 1 56  ? 166.507 145.269 155.626 1.00 82.55  ? 56  MET A CE  1 
ATOM 444  N N   . LEU A 1 57  ? 167.060 149.733 154.384 1.00 82.30  ? 57  LEU A N   1 
ATOM 445  C CA  . LEU A 1 57  ? 167.232 150.453 155.641 1.00 82.30  ? 57  LEU A CA  1 
ATOM 446  C C   . LEU A 1 57  ? 166.848 151.921 155.519 1.00 82.30  ? 57  LEU A C   1 
ATOM 447  O O   . LEU A 1 57  ? 166.422 152.531 156.505 1.00 82.30  ? 57  LEU A O   1 
ATOM 448  C CB  . LEU A 1 57  ? 168.681 150.340 156.108 1.00 82.30  ? 57  LEU A CB  1 
ATOM 449  C CG  . LEU A 1 57  ? 169.151 148.930 156.451 1.00 82.30  ? 57  LEU A CG  1 
ATOM 450  C CD1 . LEU A 1 57  ? 170.666 148.882 156.515 1.00 82.30  ? 57  LEU A CD1 1 
ATOM 451  C CD2 . LEU A 1 57  ? 168.536 148.468 157.757 1.00 82.30  ? 57  LEU A CD2 1 
ATOM 452  N N   . VAL A 1 58  ? 166.989 152.504 154.329 1.00 88.20  ? 58  VAL A N   1 
ATOM 453  C CA  . VAL A 1 58  ? 166.938 153.959 154.208 1.00 88.20  ? 58  VAL A CA  1 
ATOM 454  C C   . VAL A 1 58  ? 165.579 154.491 154.645 1.00 88.20  ? 58  VAL A C   1 
ATOM 455  O O   . VAL A 1 58  ? 165.490 155.406 155.471 1.00 88.20  ? 58  VAL A O   1 
ATOM 456  C CB  . VAL A 1 58  ? 167.271 154.389 152.769 1.00 88.20  ? 58  VAL A CB  1 
ATOM 457  C CG1 . VAL A 1 58  ? 167.151 155.895 152.628 1.00 88.20  ? 58  VAL A CG1 1 
ATOM 458  C CG2 . VAL A 1 58  ? 168.672 153.934 152.389 1.00 88.20  ? 58  VAL A CG2 1 
ATOM 459  N N   . MET A 1 59  ? 164.501 153.929 154.104 1.00 84.50  ? 59  MET A N   1 
ATOM 460  C CA  . MET A 1 59  ? 163.182 154.499 154.369 1.00 84.50  ? 59  MET A CA  1 
ATOM 461  C C   . MET A 1 59  ? 162.783 154.392 155.833 1.00 84.50  ? 59  MET A C   1 
ATOM 462  O O   . MET A 1 59  ? 162.427 155.424 156.429 1.00 84.50  ? 59  MET A O   1 
ATOM 463  C CB  . MET A 1 59  ? 162.144 153.838 153.456 1.00 84.50  ? 59  MET A CB  1 
ATOM 464  C CG  . MET A 1 59  ? 162.123 154.370 152.027 1.00 84.50  ? 59  MET A CG  1 
ATOM 465  S SD  . MET A 1 59  ? 162.084 156.168 151.891 1.00 84.50  ? 59  MET A SD  1 
ATOM 466  C CE  . MET A 1 59  ? 160.772 156.564 153.039 1.00 84.50  ? 59  MET A CE  1 
ATOM 467  N N   . PRO A 1 60  ? 162.808 153.220 156.473 1.00 87.11  ? 60  PRO A N   1 
ATOM 468  C CA  . PRO A 1 60  ? 162.437 153.177 157.897 1.00 87.11  ? 60  PRO A CA  1 
ATOM 469  C C   . PRO A 1 60  ? 163.323 154.043 158.773 1.00 87.11  ? 60  PRO A C   1 
ATOM 470  O O   . PRO A 1 60  ? 162.829 154.673 159.715 1.00 87.11  ? 60  PRO A O   1 
ATOM 471  C CB  . PRO A 1 60  ? 162.569 151.689 158.250 1.00 87.11  ? 60  PRO A CB  1 
ATOM 472  C CG  . PRO A 1 60  ? 162.535 150.970 156.955 1.00 87.11  ? 60  PRO A CG  1 
ATOM 473  C CD  . PRO A 1 60  ? 163.156 151.886 155.959 1.00 87.11  ? 60  PRO A CD  1 
ATOM 474  N N   . ILE A 1 61  ? 164.625 154.090 158.491 1.00 83.30  ? 61  ILE A N   1 
ATOM 475  C CA  . ILE A 1 61  ? 165.537 154.863 159.329 1.00 83.30  ? 61  ILE A CA  1 
ATOM 476  C C   . ILE A 1 61  ? 165.277 156.353 159.164 1.00 83.30  ? 61  ILE A C   1 
ATOM 477  O O   . ILE A 1 61  ? 165.168 157.094 160.146 1.00 83.30  ? 61  ILE A O   1 
ATOM 478  C CB  . ILE A 1 61  ? 166.997 154.506 158.998 1.00 83.30  ? 61  ILE A CB  1 
ATOM 479  C CG1 . ILE A 1 61  ? 167.451 153.330 159.858 1.00 83.30  ? 61  ILE A CG1 1 
ATOM 480  C CG2 . ILE A 1 61  ? 167.914 155.706 159.214 1.00 83.30  ? 61  ILE A CG2 1 
ATOM 481  C CD1 . ILE A 1 61  ? 168.806 152.791 159.486 1.00 83.30  ? 61  ILE A CD1 1 
ATOM 482  N N   . VAL A 1 62  ? 165.169 156.813 157.917 1.00 85.04  ? 62  VAL A N   1 
ATOM 483  C CA  . VAL A 1 62  ? 165.029 158.244 157.671 1.00 85.04  ? 62  VAL A CA  1 
ATOM 484  C C   . VAL A 1 62  ? 163.749 158.774 158.296 1.00 85.04  ? 62  VAL A C   1 
ATOM 485  O O   . VAL A 1 62  ? 163.690 159.935 158.715 1.00 85.04  ? 62  VAL A O   1 
ATOM 486  C CB  . VAL A 1 62  ? 165.078 158.531 156.159 1.00 85.04  ? 62  VAL A CB  1 
ATOM 487  C CG1 . VAL A 1 62  ? 164.727 159.982 155.884 1.00 85.04  ? 62  VAL A CG1 1 
ATOM 488  C CG2 . VAL A 1 62  ? 166.454 158.195 155.605 1.00 85.04  ? 62  VAL A CG2 1 
ATOM 489  N N   . PHE A 1 63  ? 162.707 157.948 158.366 1.00 81.31  ? 63  PHE A N   1 
ATOM 490  C CA  . PHE A 1 63  ? 161.462 158.383 158.987 1.00 81.31  ? 63  PHE A CA  1 
ATOM 491  C C   . PHE A 1 63  ? 161.522 158.245 160.503 1.00 81.31  ? 63  PHE A C   1 
ATOM 492  O O   . PHE A 1 63  ? 161.399 159.232 161.234 1.00 81.31  ? 63  PHE A O   1 
ATOM 493  C CB  . PHE A 1 63  ? 160.287 157.582 158.426 1.00 81.31  ? 63  PHE A CB  1 
ATOM 494  C CG  . PHE A 1 63  ? 159.010 157.781 159.184 1.00 81.31  ? 63  PHE A CG  1 
ATOM 495  C CD1 . PHE A 1 63  ? 158.338 158.987 159.124 1.00 81.31  ? 63  PHE A CD1 1 
ATOM 496  C CD2 . PHE A 1 63  ? 158.485 156.764 159.959 1.00 81.31  ? 63  PHE A CD2 1 
ATOM 497  C CE1 . PHE A 1 63  ? 157.165 159.175 159.822 1.00 81.31  ? 63  PHE A CE1 1 
ATOM 498  C CE2 . PHE A 1 63  ? 157.312 156.947 160.659 1.00 81.31  ? 63  PHE A CE2 1 
ATOM 499  C CZ  . PHE A 1 63  ? 156.651 158.154 160.590 1.00 81.31  ? 63  PHE A CZ  1 
ATOM 500  N N   . ALA A 1 64  ? 161.718 157.020 160.994 1.00 80.49  ? 64  ALA A N   1 
ATOM 501  C CA  . ALA A 1 64  ? 161.668 156.787 162.432 1.00 80.49  ? 64  ALA A CA  1 
ATOM 502  C C   . ALA A 1 64  ? 162.759 157.559 163.160 1.00 80.49  ? 64  ALA A C   1 
ATOM 503  O O   . ALA A 1 64  ? 162.503 158.175 164.201 1.00 80.49  ? 64  ALA A O   1 
ATOM 504  C CB  . ALA A 1 64  ? 161.789 155.292 162.723 1.00 80.49  ? 64  ALA A CB  1 
ATOM 505  N N   . SER A 1 65  ? 163.984 157.539 162.634 1.00 83.08  ? 65  SER A N   1 
ATOM 506  C CA  . SER A 1 65  ? 165.085 158.204 163.321 1.00 83.08  ? 65  SER A CA  1 
ATOM 507  C C   . SER A 1 65  ? 164.856 159.706 163.410 1.00 83.08  ? 65  SER A C   1 
ATOM 508  O O   . SER A 1 65  ? 165.077 160.313 164.463 1.00 83.08  ? 65  SER A O   1 
ATOM 509  C CB  . SER A 1 65  ? 166.402 157.910 162.608 1.00 83.08  ? 65  SER A CB  1 
ATOM 510  O OG  . SER A 1 65  ? 166.498 158.650 161.405 1.00 83.08  ? 65  SER A OG  1 
ATOM 511  N N   . LEU A 1 66  ? 164.415 160.324 162.314 1.00 78.61  ? 66  LEU A N   1 
ATOM 512  C CA  . LEU A 1 66  ? 164.239 161.772 162.310 1.00 78.61  ? 66  LEU A CA  1 
ATOM 513  C C   . LEU A 1 66  ? 163.086 162.193 163.211 1.00 78.61  ? 66  LEU A C   1 
ATOM 514  O O   . LEU A 1 66  ? 163.176 163.211 163.907 1.00 78.61  ? 66  LEU A O   1 
ATOM 515  C CB  . LEU A 1 66  ? 164.014 162.266 160.884 1.00 78.61  ? 66  LEU A CB  1 
ATOM 516  C CG  . LEU A 1 66  ? 164.831 163.483 160.457 1.00 78.61  ? 66  LEU A CG  1 
ATOM 517  C CD1 . LEU A 1 66  ? 166.316 163.185 160.522 1.00 78.61  ? 66  LEU A CD1 1 
ATOM 518  C CD2 . LEU A 1 66  ? 164.438 163.905 159.060 1.00 78.61  ? 66  LEU A CD2 1 
ATOM 519  N N   . VAL A 1 67  ? 161.994 161.426 163.213 1.00 75.49  ? 67  VAL A N   1 
ATOM 520  C CA  . VAL A 1 67  ? 160.875 161.744 164.095 1.00 75.49  ? 67  VAL A CA  1 
ATOM 521  C C   . VAL A 1 67  ? 161.335 161.745 165.544 1.00 75.49  ? 67  VAL A C   1 
ATOM 522  O O   . VAL A 1 67  ? 160.971 162.630 166.327 1.00 75.49  ? 67  VAL A O   1 
ATOM 523  C CB  . VAL A 1 67  ? 159.721 160.750 163.873 1.00 75.49  ? 67  VAL A CB  1 
ATOM 524  C CG1 . VAL A 1 67  ? 158.720 160.837 165.014 1.00 75.49  ? 67  VAL A CG1 1 
ATOM 525  C CG2 . VAL A 1 67  ? 159.047 161.013 162.537 1.00 75.49  ? 67  VAL A CG2 1 
ATOM 526  N N   . VAL A 1 68  ? 162.135 160.752 165.926 1.00 77.72  ? 68  VAL A N   1 
ATOM 527  C CA  . VAL A 1 68  ? 162.687 160.721 167.275 1.00 77.72  ? 68  VAL A CA  1 
ATOM 528  C C   . VAL A 1 68  ? 163.633 161.896 167.484 1.00 77.72  ? 68  VAL A C   1 
ATOM 529  O O   . VAL A 1 68  ? 163.579 162.583 168.509 1.00 77.72  ? 68  VAL A O   1 
ATOM 530  C CB  . VAL A 1 68  ? 163.397 159.381 167.529 1.00 77.72  ? 68  VAL A CB  1 
ATOM 531  C CG1 . VAL A 1 68  ? 164.046 159.381 168.901 1.00 77.72  ? 68  VAL A CG1 1 
ATOM 532  C CG2 . VAL A 1 68  ? 162.423 158.230 167.396 1.00 77.72  ? 68  VAL A CG2 1 
ATOM 533  N N   . GLY A 1 69  ? 164.514 162.143 166.515 1.00 83.14  ? 69  GLY A N   1 
ATOM 534  C CA  . GLY A 1 69  ? 165.471 163.227 166.665 1.00 83.14  ? 69  GLY A CA  1 
ATOM 535  C C   . GLY A 1 69  ? 164.799 164.582 166.745 1.00 83.14  ? 69  GLY A C   1 
ATOM 536  O O   . GLY A 1 69  ? 165.121 165.401 167.609 1.00 83.14  ? 69  GLY A O   1 
ATOM 537  N N   . ALA A 1 70  ? 163.852 164.839 165.842 1.00 81.30  ? 70  ALA A N   1 
ATOM 538  C CA  . ALA A 1 70  ? 163.142 166.111 165.867 1.00 81.30  ? 70  ALA A CA  1 
ATOM 539  C C   . ALA A 1 70  ? 162.309 166.252 167.133 1.00 81.30  ? 70  ALA A C   1 
ATOM 540  O O   . ALA A 1 70  ? 162.245 167.335 167.724 1.00 81.30  ? 70  ALA A O   1 
ATOM 541  C CB  . ALA A 1 70  ? 162.259 166.243 164.629 1.00 81.30  ? 70  ALA A CB  1 
ATOM 542  N N   . ALA A 1 71  ? 161.665 165.169 167.565 1.00 82.21  ? 71  ALA A N   1 
ATOM 543  C CA  . ALA A 1 71  ? 160.790 165.218 168.728 1.00 82.21  ? 71  ALA A CA  1 
ATOM 544  C C   . ALA A 1 71  ? 161.543 165.149 170.048 1.00 82.21  ? 71  ALA A C   1 
ATOM 545  O O   . ALA A 1 71  ? 160.925 165.341 171.100 1.00 82.21  ? 71  ALA A O   1 
ATOM 546  C CB  . ALA A 1 71  ? 159.776 164.075 168.666 1.00 82.21  ? 71  ALA A CB  1 
ATOM 547  N N   . SER A 1 72  ? 162.844 164.878 170.026 1.00 90.47  ? 72  SER A N   1 
ATOM 548  C CA  . SER A 1 72  ? 163.631 164.756 171.245 1.00 90.47  ? 72  SER A CA  1 
ATOM 549  C C   . SER A 1 72  ? 164.259 166.071 171.686 1.00 90.47  ? 72  SER A C   1 
ATOM 550  O O   . SER A 1 72  ? 164.884 166.112 172.750 1.00 90.47  ? 72  SER A O   1 
ATOM 551  C CB  . SER A 1 72  ? 164.730 163.708 171.056 1.00 90.47  ? 72  SER A CB  1 
ATOM 552  O OG  . SER A 1 72  ? 165.645 164.109 170.053 1.00 90.47  ? 72  SER A OG  1 
ATOM 553  N N   . ILE A 1 73  ? 164.116 167.140 170.903 1.00 84.90  ? 73  ILE A N   1 
ATOM 554  C CA  . ILE A 1 73  ? 164.677 168.437 171.247 1.00 84.90  ? 73  ILE A CA  1 
ATOM 555  C C   . ILE A 1 73  ? 163.614 169.504 171.035 1.00 84.90  ? 73  ILE A C   1 
ATOM 556  O O   . ILE A 1 73  ? 162.627 169.304 170.324 1.00 84.90  ? 73  ILE A O   1 
ATOM 557  C CB  . ILE A 1 73  ? 165.941 168.763 170.426 1.00 84.90  ? 73  ILE A CB  1 
ATOM 558  C CG1 . ILE A 1 73  ? 165.624 168.782 168.930 1.00 84.90  ? 73  ILE A CG1 1 
ATOM 559  C CG2 . ILE A 1 73  ? 167.027 167.745 170.717 1.00 84.90  ? 73  ILE A CG2 1 
ATOM 560  C CD1 . ILE A 1 73  ? 166.804 169.159 168.066 1.00 84.90  ? 73  ILE A CD1 1 
ATOM 561  N N   . SER A 1 74  ? 163.830 170.653 171.668 1.00 84.78  ? 74  SER A N   1 
ATOM 562  C CA  . SER A 1 74  ? 162.870 171.737 171.576 1.00 84.78  ? 74  SER A CA  1 
ATOM 563  C C   . SER A 1 74  ? 162.787 172.242 170.136 1.00 84.78  ? 74  SER A C   1 
ATOM 564  O O   . SER A 1 74  ? 163.787 172.245 169.413 1.00 84.78  ? 74  SER A O   1 
ATOM 565  C CB  . SER A 1 74  ? 163.267 172.881 172.505 1.00 84.78  ? 74  SER A CB  1 
ATOM 566  O OG  . SER A 1 74  ? 164.447 173.515 172.047 1.00 84.78  ? 74  SER A OG  1 
ATOM 567  N N   . PRO A 1 75  ? 161.607 172.679 169.693 1.00 82.98  ? 75  PRO A N   1 
ATOM 568  C CA  . PRO A 1 75  ? 161.496 173.181 168.316 1.00 82.98  ? 75  PRO A CA  1 
ATOM 569  C C   . PRO A 1 75  ? 162.403 174.364 168.038 1.00 82.98  ? 75  PRO A C   1 
ATOM 570  O O   . PRO A 1 75  ? 162.884 174.513 166.908 1.00 82.98  ? 75  PRO A O   1 
ATOM 571  C CB  . PRO A 1 75  ? 160.014 173.561 168.199 1.00 82.98  ? 75  PRO A CB  1 
ATOM 572  C CG  . PRO A 1 75  ? 159.567 173.793 169.597 1.00 82.98  ? 75  PRO A CG  1 
ATOM 573  C CD  . PRO A 1 75  ? 160.352 172.845 170.445 1.00 82.98  ? 75  PRO A CD  1 
ATOM 574  N N   . ALA A 1 76  ? 162.649 175.216 169.034 1.00 97.86  ? 76  ALA A N   1 
ATOM 575  C CA  . ALA A 1 76  ? 163.542 176.350 168.827 1.00 97.86  ? 76  ALA A CA  1 
ATOM 576  C C   . ALA A 1 76  ? 164.947 175.878 168.484 1.00 97.86  ? 76  ALA A C   1 
ATOM 577  O O   . ALA A 1 76  ? 165.561 176.360 167.526 1.00 97.86  ? 76  ALA A O   1 
ATOM 578  C CB  . ALA A 1 76  ? 163.559 177.235 170.073 1.00 97.86  ? 76  ALA A CB  1 
ATOM 579  N N   . ARG A 1 77  ? 165.472 174.923 169.254 1.00 97.86  ? 77  ARG A N   1 
ATOM 580  C CA  . ARG A 1 77  ? 166.798 174.393 168.958 1.00 97.86  ? 77  ARG A CA  1 
ATOM 581  C C   . ARG A 1 77  ? 166.814 173.698 167.606 1.00 97.86  ? 77  ARG A C   1 
ATOM 582  O O   . ARG A 1 77  ? 167.789 173.807 166.853 1.00 97.86  ? 77  ARG A O   1 
ATOM 583  C CB  . ARG A 1 77  ? 167.240 173.431 170.059 1.00 97.86  ? 77  ARG A CB  1 
ATOM 584  C CG  . ARG A 1 77  ? 168.640 172.872 169.852 1.00 97.86  ? 77  ARG A CG  1 
ATOM 585  C CD  . ARG A 1 77  ? 169.439 172.841 171.143 1.00 97.86  ? 77  ARG A CD  1 
ATOM 586  N NE  . ARG A 1 77  ? 169.168 171.638 171.922 1.00 97.86  ? 77  ARG A NE  1 
ATOM 587  C CZ  . ARG A 1 77  ? 169.960 170.575 171.980 1.00 97.86  ? 77  ARG A CZ  1 
ATOM 588  N NH1 . ARG A 1 77  ? 171.094 170.514 171.300 1.00 97.86  ? 77  ARG A NH1 1 
ATOM 589  N NH2 . ARG A 1 77  ? 169.604 169.543 172.740 1.00 97.86  ? 77  ARG A NH2 1 
ATOM 590  N N   . LEU A 1 78  ? 165.741 172.978 167.279 1.00 97.86  ? 78  LEU A N   1 
ATOM 591  C CA  . LEU A 1 78  ? 165.675 172.300 165.991 1.00 97.86  ? 78  LEU A CA  1 
ATOM 592  C C   . LEU A 1 78  ? 165.798 173.293 164.845 1.00 97.86  ? 78  LEU A C   1 
ATOM 593  O O   . LEU A 1 78  ? 166.514 173.041 163.870 1.00 97.86  ? 78  LEU A O   1 
ATOM 594  C CB  . LEU A 1 78  ? 164.369 171.516 165.885 1.00 97.86  ? 78  LEU A CB  1 
ATOM 595  C CG  . LEU A 1 78  ? 164.165 170.716 164.601 1.00 97.86  ? 78  LEU A CG  1 
ATOM 596  C CD1 . LEU A 1 78  ? 165.234 169.653 164.456 1.00 97.86  ? 78  LEU A CD1 1 
ATOM 597  C CD2 . LEU A 1 78  ? 162.785 170.092 164.597 1.00 97.86  ? 78  LEU A CD2 1 
ATOM 598  N N   . GLY A 1 79  ? 165.110 174.430 164.944 1.00 97.86  ? 79  GLY A N   1 
ATOM 599  C CA  . GLY A 1 79  ? 165.238 175.446 163.913 1.00 97.86  ? 79  GLY A CA  1 
ATOM 600  C C   . GLY A 1 79  ? 166.657 175.961 163.786 1.00 97.86  ? 79  GLY A C   1 
ATOM 601  O O   . GLY A 1 79  ? 167.181 176.103 162.679 1.00 97.86  ? 79  GLY A O   1 
ATOM 602  N N   . ARG A 1 80  ? 167.303 176.243 164.919 1.00 97.86  ? 80  ARG A N   1 
ATOM 603  C CA  . ARG A 1 80  ? 168.696 176.671 164.883 1.00 97.86  ? 80  ARG A CA  1 
ATOM 604  C C   . ARG A 1 80  ? 169.567 175.615 164.219 1.00 97.86  ? 80  ARG A C   1 
ATOM 605  O O   . ARG A 1 80  ? 170.328 175.912 163.292 1.00 97.86  ? 80  ARG A O   1 
ATOM 606  C CB  . ARG A 1 80  ? 169.192 176.955 166.300 1.00 97.86  ? 80  ARG A CB  1 
ATOM 607  C CG  . ARG A 1 80  ? 169.173 178.419 166.690 1.00 97.86  ? 80  ARG A CG  1 
ATOM 608  C CD  . ARG A 1 80  ? 170.165 178.692 167.804 1.00 97.86  ? 80  ARG A CD  1 
ATOM 609  N NE  . ARG A 1 80  ? 170.078 177.695 168.863 1.00 97.86  ? 80  ARG A NE  1 
ATOM 610  C CZ  . ARG A 1 80  ? 169.075 177.602 169.725 1.00 97.86  ? 80  ARG A CZ  1 
ATOM 611  N NH1 . ARG A 1 80  ? 168.048 178.434 169.683 1.00 97.86  ? 80  ARG A NH1 1 
ATOM 612  N NH2 . ARG A 1 80  ? 169.105 176.650 170.653 1.00 97.86  ? 80  ARG A NH2 1 
ATOM 613  N N   . VAL A 1 81  ? 169.462 174.368 164.679 1.00 97.86  ? 81  VAL A N   1 
ATOM 614  C CA  . VAL A 1 81  ? 170.258 173.296 164.093 1.00 97.86  ? 81  VAL A CA  1 
ATOM 615  C C   . VAL A 1 81  ? 169.842 173.050 162.650 1.00 97.86  ? 81  VAL A C   1 
ATOM 616  O O   . VAL A 1 81  ? 170.690 172.921 161.761 1.00 97.86  ? 81  VAL A O   1 
ATOM 617  C CB  . VAL A 1 81  ? 170.136 172.018 164.940 1.00 97.86  ? 81  VAL A CB  1 
ATOM 618  C CG1 . VAL A 1 81  ? 170.673 170.821 164.175 1.00 97.86  ? 81  VAL A CG1 1 
ATOM 619  C CG2 . VAL A 1 81  ? 170.869 172.191 166.258 1.00 97.86  ? 81  VAL A CG2 1 
ATOM 620  N N   . GLY A 1 82  ? 168.535 172.992 162.392 1.00 97.86  ? 82  GLY A N   1 
ATOM 621  C CA  . GLY A 1 82  ? 168.072 172.672 161.051 1.00 97.86  ? 82  GLY A CA  1 
ATOM 622  C C   . GLY A 1 82  ? 168.545 173.674 160.017 1.00 97.86  ? 82  GLY A C   1 
ATOM 623  O O   . GLY A 1 82  ? 169.009 173.302 158.937 1.00 97.86  ? 82  GLY A O   1 
ATOM 624  N N   . VAL A 1 83  ? 168.432 174.964 160.332 1.00 97.86  ? 83  VAL A N   1 
ATOM 625  C CA  . VAL A 1 83  ? 168.906 175.986 159.406 1.00 97.86  ? 83  VAL A CA  1 
ATOM 626  C C   . VAL A 1 83  ? 170.415 175.890 159.240 1.00 97.86  ? 83  VAL A C   1 
ATOM 627  O O   . VAL A 1 83  ? 170.942 176.029 158.131 1.00 97.86  ? 83  VAL A O   1 
ATOM 628  C CB  . VAL A 1 83  ? 168.477 177.382 159.889 1.00 97.86  ? 83  VAL A CB  1 
ATOM 629  C CG1 . VAL A 1 83  ? 169.320 178.460 159.223 1.00 97.86  ? 83  VAL A CG1 1 
ATOM 630  C CG2 . VAL A 1 83  ? 167.002 177.605 159.611 1.00 97.86  ? 83  VAL A CG2 1 
ATOM 631  N N   . LYS A 1 84  ? 171.136 175.658 160.337 1.00 97.86  ? 84  LYS A N   1 
ATOM 632  C CA  . LYS A 1 84  ? 172.588 175.567 160.256 1.00 97.86  ? 84  LYS A CA  1 
ATOM 633  C C   . LYS A 1 84  ? 173.016 174.400 159.377 1.00 97.86  ? 84  LYS A C   1 
ATOM 634  O O   . LYS A 1 84  ? 173.908 174.539 158.533 1.00 97.86  ? 84  LYS A O   1 
ATOM 635  C CB  . LYS A 1 84  ? 173.181 175.425 161.657 1.00 97.86  ? 84  LYS A CB  1 
ATOM 636  C CG  . LYS A 1 84  ? 173.249 176.723 162.435 1.00 97.86  ? 84  LYS A CG  1 
ATOM 637  C CD  . LYS A 1 84  ? 173.688 176.482 163.866 1.00 97.86  ? 84  LYS A CD  1 
ATOM 638  C CE  . LYS A 1 84  ? 173.736 177.775 164.656 1.00 97.86  ? 84  LYS A CE  1 
ATOM 639  N NZ  . LYS A 1 84  ? 174.279 177.569 166.024 1.00 97.86  ? 84  LYS A NZ  1 
ATOM 640  N N   . ILE A 1 85  ? 172.389 173.237 159.558 1.00 97.86  ? 85  ILE A N   1 
ATOM 641  C CA  . ILE A 1 85  ? 172.872 172.040 158.876 1.00 97.86  ? 85  ILE A CA  1 
ATOM 642  C C   . ILE A 1 85  ? 172.590 172.133 157.382 1.00 97.86  ? 85  ILE A C   1 
ATOM 643  O O   . ILE A 1 85  ? 173.458 171.835 156.554 1.00 97.86  ? 85  ILE A O   1 
ATOM 644  C CB  . ILE A 1 85  ? 172.248 170.771 159.486 1.00 97.86  ? 85  ILE A CB  1 
ATOM 645  C CG1 . ILE A 1 85  ? 172.631 169.539 158.668 1.00 97.86  ? 85  ILE A CG1 1 
ATOM 646  C CG2 . ILE A 1 85  ? 170.730 170.846 159.486 1.00 97.86  ? 85  ILE A CG2 1 
ATOM 647  C CD1 . ILE A 1 85  ? 174.119 169.418 158.431 1.00 97.86  ? 85  ILE A CD1 1 
ATOM 648  N N   . VAL A 1 86  ? 171.378 172.551 157.010 1.00 97.86  ? 86  VAL A N   1 
ATOM 649  C CA  . VAL A 1 86  ? 171.037 172.653 155.594 1.00 97.86  ? 86  VAL A CA  1 
ATOM 650  C C   . VAL A 1 86  ? 171.918 173.690 154.912 1.00 97.86  ? 86  VAL A C   1 
ATOM 651  O O   . VAL A 1 86  ? 172.390 173.483 153.788 1.00 97.86  ? 86  VAL A O   1 
ATOM 652  C CB  . VAL A 1 86  ? 169.542 172.978 155.417 1.00 97.86  ? 86  VAL A CB  1 
ATOM 653  C CG1 . VAL A 1 86  ? 168.686 171.886 156.041 1.00 97.86  ? 86  VAL A CG1 1 
ATOM 654  C CG2 . VAL A 1 86  ? 169.210 174.339 156.008 1.00 97.86  ? 86  VAL A CG2 1 
ATOM 655  N N   . VAL A 1 87  ? 172.156 174.820 155.579 1.00 97.86  ? 87  VAL A N   1 
ATOM 656  C CA  . VAL A 1 87  ? 173.057 175.824 155.025 1.00 97.86  ? 87  VAL A CA  1 
ATOM 657  C C   . VAL A 1 87  ? 174.439 175.226 154.812 1.00 97.86  ? 87  VAL A C   1 
ATOM 658  O O   . VAL A 1 87  ? 175.107 175.508 153.810 1.00 97.86  ? 87  VAL A O   1 
ATOM 659  C CB  . VAL A 1 87  ? 173.113 177.058 155.942 1.00 97.86  ? 87  VAL A CB  1 
ATOM 660  C CG1 . VAL A 1 87  ? 174.366 177.877 155.664 1.00 97.86  ? 87  VAL A CG1 1 
ATOM 661  C CG2 . VAL A 1 87  ? 171.865 177.907 155.764 1.00 97.86  ? 87  VAL A CG2 1 
ATOM 662  N N   . TYR A 1 88  ? 174.892 174.392 155.749 1.00 97.86  ? 88  TYR A N   1 
ATOM 663  C CA  . TYR A 1 88  ? 176.217 173.797 155.625 1.00 97.86  ? 88  TYR A CA  1 
ATOM 664  C C   . TYR A 1 88  ? 176.317 172.939 154.371 1.00 97.86  ? 88  TYR A C   1 
ATOM 665  O O   . TYR A 1 88  ? 177.292 173.031 153.618 1.00 97.86  ? 88  TYR A O   1 
ATOM 666  C CB  . TYR A 1 88  ? 176.539 172.969 156.866 1.00 97.86  ? 88  TYR A CB  1 
ATOM 667  C CG  . TYR A 1 88  ? 177.623 171.951 156.631 1.00 97.86  ? 88  TYR A CG  1 
ATOM 668  C CD1 . TYR A 1 88  ? 178.954 172.329 156.584 1.00 97.86  ? 88  TYR A CD1 1 
ATOM 669  C CD2 . TYR A 1 88  ? 177.316 170.612 156.448 1.00 97.86  ? 88  TYR A CD2 1 
ATOM 670  C CE1 . TYR A 1 88  ? 179.949 171.403 156.366 1.00 97.86  ? 88  TYR A CE1 1 
ATOM 671  C CE2 . TYR A 1 88  ? 178.304 169.679 156.228 1.00 97.86  ? 88  TYR A CE2 1 
ATOM 672  C CZ  . TYR A 1 88  ? 179.619 170.079 156.188 1.00 97.86  ? 88  TYR A CZ  1 
ATOM 673  O OH  . TYR A 1 88  ? 180.608 169.152 155.970 1.00 97.86  ? 88  TYR A OH  1 
ATOM 674  N N   . TYR A 1 89  ? 175.313 172.092 154.128 1.00 97.86  ? 89  TYR A N   1 
ATOM 675  C CA  . TYR A 1 89  ? 175.349 171.246 152.940 1.00 97.86  ? 89  TYR A CA  1 
ATOM 676  C C   . TYR A 1 89  ? 175.317 172.081 151.670 1.00 97.86  ? 89  TYR A C   1 
ATOM 677  O O   . TYR A 1 89  ? 176.063 171.811 150.722 1.00 97.86  ? 89  TYR A O   1 
ATOM 678  C CB  . TYR A 1 89  ? 174.185 170.258 152.954 1.00 97.86  ? 89  TYR A CB  1 
ATOM 679  C CG  . TYR A 1 89  ? 174.321 169.175 153.993 1.00 97.86  ? 89  TYR A CG  1 
ATOM 680  C CD1 . TYR A 1 89  ? 175.502 168.464 154.130 1.00 97.86  ? 89  TYR A CD1 1 
ATOM 681  C CD2 . TYR A 1 89  ? 173.266 168.859 154.832 1.00 97.86  ? 89  TYR A CD2 1 
ATOM 682  C CE1 . TYR A 1 89  ? 175.631 167.475 155.076 1.00 97.86  ? 89  TYR A CE1 1 
ATOM 683  C CE2 . TYR A 1 89  ? 173.385 167.869 155.779 1.00 97.86  ? 89  TYR A CE2 1 
ATOM 684  C CZ  . TYR A 1 89  ? 174.570 167.181 155.898 1.00 97.86  ? 89  TYR A CZ  1 
ATOM 685  O OH  . TYR A 1 89  ? 174.695 166.194 156.844 1.00 97.86  ? 89  TYR A OH  1 
ATOM 686  N N   . LEU A 1 90  ? 174.469 173.109 151.633 1.00 97.86  ? 90  LEU A N   1 
ATOM 687  C CA  . LEU A 1 90  ? 174.399 173.951 150.446 1.00 97.86  ? 90  LEU A CA  1 
ATOM 688  C C   . LEU A 1 90  ? 175.756 174.564 150.138 1.00 97.86  ? 90  LEU A C   1 
ATOM 689  O O   . LEU A 1 90  ? 176.183 174.596 148.978 1.00 97.86  ? 90  LEU A O   1 
ATOM 690  C CB  . LEU A 1 90  ? 173.349 175.043 150.639 1.00 97.86  ? 90  LEU A CB  1 
ATOM 691  C CG  . LEU A 1 90  ? 171.897 174.570 150.584 1.00 97.86  ? 90  LEU A CG  1 
ATOM 692  C CD1 . LEU A 1 90  ? 170.968 175.647 151.113 1.00 97.86  ? 90  LEU A CD1 1 
ATOM 693  C CD2 . LEU A 1 90  ? 171.513 174.180 149.167 1.00 97.86  ? 90  LEU A CD2 1 
ATOM 694  N N   . LEU A 1 91  ? 176.455 175.047 151.164 1.00 97.86  ? 91  LEU A N   1 
ATOM 695  C CA  . LEU A 1 91  ? 177.787 175.599 150.949 1.00 97.86  ? 91  LEU A CA  1 
ATOM 696  C C   . LEU A 1 91  ? 178.741 174.530 150.433 1.00 97.86  ? 91  LEU A C   1 
ATOM 697  O O   . LEU A 1 91  ? 179.410 174.720 149.411 1.00 97.86  ? 91  LEU A O   1 
ATOM 698  C CB  . LEU A 1 91  ? 178.318 176.208 152.244 1.00 97.86  ? 91  LEU A CB  1 
ATOM 699  C CG  . LEU A 1 91  ? 179.716 176.813 152.132 1.00 97.86  ? 91  LEU A CG  1 
ATOM 700  C CD1 . LEU A 1 91  ? 179.764 178.169 152.811 1.00 97.86  ? 91  LEU A CD1 1 
ATOM 701  C CD2 . LEU A 1 91  ? 180.752 175.879 152.727 1.00 97.86  ? 91  LEU A CD2 1 
ATOM 702  N N   . THR A 1 92  ? 178.816 173.394 151.127 1.00 101.62 ? 92  THR A N   1 
ATOM 703  C CA  . THR A 1 92  ? 179.735 172.342 150.707 1.00 101.62 ? 92  THR A CA  1 
ATOM 704  C C   . THR A 1 92  ? 179.353 171.793 149.339 1.00 101.62 ? 92  THR A C   1 
ATOM 705  O O   . THR A 1 92  ? 180.222 171.574 148.486 1.00 101.62 ? 92  THR A O   1 
ATOM 706  C CB  . THR A 1 92  ? 179.763 171.221 151.741 1.00 101.62 ? 92  THR A CB  1 
ATOM 707  O OG1 . THR A 1 92  ? 178.432 170.745 151.970 1.00 101.62 ? 92  THR A OG1 1 
ATOM 708  C CG2 . THR A 1 92  ? 180.353 171.720 153.047 1.00 101.62 ? 92  THR A CG2 1 
ATOM 709  N N   . SER A 1 93  ? 178.059 171.570 149.105 1.00 105.45 ? 93  SER A N   1 
ATOM 710  C CA  . SER A 1 93  ? 177.628 171.106 147.791 1.00 105.45 ? 93  SER A CA  1 
ATOM 711  C C   . SER A 1 93  ? 178.003 172.113 146.714 1.00 105.45 ? 93  SER A C   1 
ATOM 712  O O   . SER A 1 93  ? 178.484 171.737 145.640 1.00 105.45 ? 93  SER A O   1 
ATOM 713  C CB  . SER A 1 93  ? 176.122 170.855 147.784 1.00 105.45 ? 93  SER A CB  1 
ATOM 714  O OG  . SER A 1 93  ? 175.423 171.997 147.322 1.00 105.45 ? 93  SER A OG  1 
ATOM 715  N N   . ALA A 1 94  ? 177.796 173.403 146.987 1.00 107.79 ? 94  ALA A N   1 
ATOM 716  C CA  . ALA A 1 94  ? 178.255 174.427 146.059 1.00 107.79 ? 94  ALA A CA  1 
ATOM 717  C C   . ALA A 1 94  ? 179.756 174.330 145.837 1.00 107.79 ? 94  ALA A C   1 
ATOM 718  O O   . ALA A 1 94  ? 180.255 174.733 144.781 1.00 107.79 ? 94  ALA A O   1 
ATOM 719  C CB  . ALA A 1 94  ? 177.883 175.814 146.579 1.00 107.79 ? 94  ALA A CB  1 
ATOM 720  N N   . PHE A 1 95  ? 180.491 173.806 146.818 1.00 100.98 ? 95  PHE A N   1 
ATOM 721  C CA  . PHE A 1 95  ? 181.912 173.554 146.622 1.00 100.98 ? 95  PHE A CA  1 
ATOM 722  C C   . PHE A 1 95  ? 182.141 172.259 145.854 1.00 100.98 ? 95  PHE A C   1 
ATOM 723  O O   . PHE A 1 95  ? 182.963 172.218 144.932 1.00 100.98 ? 95  PHE A O   1 
ATOM 724  C CB  . PHE A 1 95  ? 182.627 173.502 147.970 1.00 100.98 ? 95  PHE A CB  1 
ATOM 725  C CG  . PHE A 1 95  ? 183.336 174.771 148.325 1.00 100.98 ? 95  PHE A CG  1 
ATOM 726  C CD1 . PHE A 1 95  ? 184.464 175.167 147.629 1.00 100.98 ? 95  PHE A CD1 1 
ATOM 727  C CD2 . PHE A 1 95  ? 182.876 175.570 149.356 1.00 100.98 ? 95  PHE A CD2 1 
ATOM 728  C CE1 . PHE A 1 95  ? 185.119 176.336 147.954 1.00 100.98 ? 95  PHE A CE1 1 
ATOM 729  C CE2 . PHE A 1 95  ? 183.528 176.740 149.687 1.00 100.98 ? 95  PHE A CE2 1 
ATOM 730  C CZ  . PHE A 1 95  ? 184.651 177.124 148.985 1.00 100.98 ? 95  PHE A CZ  1 
ATOM 731  N N   . ALA A 1 96  ? 181.423 171.195 146.218 1.00 109.54 ? 96  ALA A N   1 
ATOM 732  C CA  . ALA A 1 96  ? 181.595 169.922 145.527 1.00 109.54 ? 96  ALA A CA  1 
ATOM 733  C C   . ALA A 1 96  ? 181.197 170.032 144.062 1.00 109.54 ? 96  ALA A C   1 
ATOM 734  O O   . ALA A 1 96  ? 181.879 169.491 143.184 1.00 109.54 ? 96  ALA A O   1 
ATOM 735  C CB  . ALA A 1 96  ? 180.782 168.834 146.225 1.00 109.54 ? 96  ALA A CB  1 
ATOM 736  N N   . VAL A 1 97  ? 180.096 170.729 143.774 1.00 111.58 ? 97  VAL A N   1 
ATOM 737  C CA  . VAL A 1 97  ? 179.654 170.863 142.390 1.00 111.58 ? 97  VAL A CA  1 
ATOM 738  C C   . VAL A 1 97  ? 180.716 171.574 141.562 1.00 111.58 ? 97  VAL A C   1 
ATOM 739  O O   . VAL A 1 97  ? 181.039 171.151 140.446 1.00 111.58 ? 97  VAL A O   1 
ATOM 740  C CB  . VAL A 1 97  ? 178.297 171.591 142.326 1.00 111.58 ? 97  VAL A CB  1 
ATOM 741  C CG1 . VAL A 1 97  ? 178.440 173.046 142.741 1.00 111.58 ? 97  VAL A CG1 1 
ATOM 742  C CG2 . VAL A 1 97  ? 177.707 171.488 140.930 1.00 111.58 ? 97  VAL A CG2 1 
ATOM 743  N N   . THR A 1 98  ? 181.278 172.661 142.093 1.00 114.96 ? 98  THR A N   1 
ATOM 744  C CA  . THR A 1 98  ? 182.357 173.344 141.391 1.00 114.96 ? 98  THR A CA  1 
ATOM 745  C C   . THR A 1 98  ? 183.615 172.491 141.365 1.00 114.96 ? 98  THR A C   1 
ATOM 746  O O   . THR A 1 98  ? 184.323 172.447 140.353 1.00 114.96 ? 98  THR A O   1 
ATOM 747  C CB  . THR A 1 98  ? 182.648 174.691 142.048 1.00 114.96 ? 98  THR A CB  1 
ATOM 748  O OG1 . THR A 1 98  ? 183.002 174.486 143.421 1.00 114.96 ? 98  THR A OG1 1 
ATOM 749  C CG2 . THR A 1 98  ? 181.432 175.600 141.967 1.00 114.96 ? 98  THR A CG2 1 
ATOM 750  N N   . LEU A 1 99  ? 183.907 171.803 142.469 1.00 108.77 ? 99  LEU A N   1 
ATOM 751  C CA  . LEU A 1 99  ? 185.115 170.990 142.531 1.00 108.77 ? 99  LEU A CA  1 
ATOM 752  C C   . LEU A 1 99  ? 185.074 169.870 141.499 1.00 108.77 ? 99  LEU A C   1 
ATOM 753  O O   . LEU A 1 99  ? 186.086 169.574 140.853 1.00 108.77 ? 99  LEU A O   1 
ATOM 754  C CB  . LEU A 1 99  ? 185.284 170.424 143.940 1.00 108.77 ? 99  LEU A CB  1 
ATOM 755  C CG  . LEU A 1 99  ? 186.586 169.683 144.240 1.00 108.77 ? 99  LEU A CG  1 
ATOM 756  C CD1 . LEU A 1 99  ? 187.795 170.521 143.862 1.00 108.77 ? 99  LEU A CD1 1 
ATOM 757  C CD2 . LEU A 1 99  ? 186.636 169.307 145.708 1.00 108.77 ? 99  LEU A CD2 1 
ATOM 758  N N   . GLY A 1 100 ? 183.915 169.233 141.331 1.00 107.83 ? 100 GLY A N   1 
ATOM 759  C CA  . GLY A 1 100 ? 183.798 168.193 140.324 1.00 107.83 ? 100 GLY A CA  1 
ATOM 760  C C   . GLY A 1 100 ? 183.960 168.726 138.914 1.00 107.83 ? 100 GLY A C   1 
ATOM 761  O O   . GLY A 1 100 ? 184.621 168.105 138.078 1.00 107.83 ? 100 GLY A O   1 
ATOM 762  N N   . ILE A 1 101 ? 183.363 169.884 138.629 1.00 106.27 ? 101 ILE A N   1 
ATOM 763  C CA  . ILE A 1 101 ? 183.499 170.479 137.303 1.00 106.27 ? 101 ILE A CA  1 
ATOM 764  C C   . ILE A 1 101 ? 184.962 170.781 137.013 1.00 106.27 ? 101 ILE A C   1 
ATOM 765  O O   . ILE A 1 101 ? 185.472 170.493 135.924 1.00 106.27 ? 101 ILE A O   1 
ATOM 766  C CB  . ILE A 1 101 ? 182.634 171.746 137.192 1.00 106.27 ? 101 ILE A CB  1 
ATOM 767  C CG1 . ILE A 1 101 ? 181.151 171.381 137.206 1.00 106.27 ? 101 ILE A CG1 1 
ATOM 768  C CG2 . ILE A 1 101 ? 182.979 172.511 135.926 1.00 106.27 ? 101 ILE A CG2 1 
ATOM 769  C CD1 . ILE A 1 101 ? 180.246 172.543 137.547 1.00 106.27 ? 101 ILE A CD1 1 
ATOM 770  N N   . ILE A 1 102 ? 185.661 171.363 137.988 1.00 110.48 ? 102 ILE A N   1 
ATOM 771  C CA  . ILE A 1 102 ? 187.068 171.701 137.792 1.00 110.48 ? 102 ILE A CA  1 
ATOM 772  C C   . ILE A 1 102 ? 187.878 170.441 137.521 1.00 110.48 ? 102 ILE A C   1 
ATOM 773  O O   . ILE A 1 102 ? 188.711 170.401 136.609 1.00 110.48 ? 102 ILE A O   1 
ATOM 774  C CB  . ILE A 1 102 ? 187.610 172.465 139.012 1.00 110.48 ? 102 ILE A CB  1 
ATOM 775  C CG1 . ILE A 1 102 ? 186.969 173.854 139.104 1.00 110.48 ? 102 ILE A CG1 1 
ATOM 776  C CG2 . ILE A 1 102 ? 189.126 172.566 138.943 1.00 110.48 ? 102 ILE A CG2 1 
ATOM 777  C CD1 . ILE A 1 102 ? 187.309 174.786 137.954 1.00 110.48 ? 102 ILE A CD1 1 
ATOM 778  N N   . MET A 1 103 ? 187.645 169.392 138.310 1.00 111.95 ? 103 MET A N   1 
ATOM 779  C CA  . MET A 1 103 ? 188.379 168.150 138.103 1.00 111.95 ? 103 MET A CA  1 
ATOM 780  C C   . MET A 1 103 ? 187.935 167.444 136.831 1.00 111.95 ? 103 MET A C   1 
ATOM 781  O O   . MET A 1 103 ? 188.732 166.732 136.210 1.00 111.95 ? 103 MET A O   1 
ATOM 782  C CB  . MET A 1 103 ? 188.203 167.229 139.307 1.00 111.95 ? 103 MET A CB  1 
ATOM 783  C CG  . MET A 1 103 ? 188.886 167.737 140.558 1.00 111.95 ? 103 MET A CG  1 
ATOM 784  S SD  . MET A 1 103 ? 190.672 167.526 140.476 1.00 111.95 ? 103 MET A SD  1 
ATOM 785  C CE  . MET A 1 103 ? 190.892 166.086 141.512 1.00 111.95 ? 103 MET A CE  1 
ATOM 786  N N   . ALA A 1 104 ? 186.677 167.623 136.430 1.00 110.89 ? 104 ALA A N   1 
ATOM 787  C CA  . ALA A 1 104 ? 186.204 167.005 135.198 1.00 110.89 ? 104 ALA A CA  1 
ATOM 788  C C   . ALA A 1 104 ? 187.003 167.502 134.001 1.00 110.89 ? 104 ALA A C   1 
ATOM 789  O O   . ALA A 1 104 ? 187.448 166.711 133.162 1.00 110.89 ? 104 ALA A O   1 
ATOM 790  C CB  . ALA A 1 104 ? 184.717 167.297 135.009 1.00 110.89 ? 104 ALA A CB  1 
ATOM 791  N N   . ARG A 1 105 ? 187.195 168.817 133.906 1.00 106.98 ? 105 ARG A N   1 
ATOM 792  C CA  . ARG A 1 105 ? 187.948 169.381 132.794 1.00 106.98 ? 105 ARG A CA  1 
ATOM 793  C C   . ARG A 1 105 ? 189.449 169.203 132.970 1.00 106.98 ? 105 ARG A C   1 
ATOM 794  O O   . ARG A 1 105 ? 190.170 169.052 131.978 1.00 106.98 ? 105 ARG A O   1 
ATOM 795  C CB  . ARG A 1 105 ? 187.606 170.860 132.635 1.00 106.98 ? 105 ARG A CB  1 
ATOM 796  C CG  . ARG A 1 105 ? 186.340 171.091 131.840 1.00 106.98 ? 105 ARG A CG  1 
ATOM 797  C CD  . ARG A 1 105 ? 185.906 172.539 131.875 1.00 106.98 ? 105 ARG A CD  1 
ATOM 798  N NE  . ARG A 1 105 ? 184.891 172.812 130.863 1.00 106.98 ? 105 ARG A NE  1 
ATOM 799  C CZ  . ARG A 1 105 ? 183.584 172.829 131.086 1.00 106.98 ? 105 ARG A CZ  1 
ATOM 800  N NH1 . ARG A 1 105 ? 183.080 172.583 132.285 1.00 106.98 ? 105 ARG A NH1 1 
ATOM 801  N NH2 . ARG A 1 105 ? 182.759 173.092 130.077 1.00 106.98 ? 105 ARG A NH2 1 
ATOM 802  N N   . LEU A 1 106 ? 189.939 169.218 134.211 1.00 112.52 ? 106 LEU A N   1 
ATOM 803  C CA  . LEU A 1 106 ? 191.372 169.067 134.435 1.00 112.52 ? 106 LEU A CA  1 
ATOM 804  C C   . LEU A 1 106 ? 191.870 167.727 133.911 1.00 112.52 ? 106 LEU A C   1 
ATOM 805  O O   . LEU A 1 106 ? 192.928 167.654 133.276 1.00 112.52 ? 106 LEU A O   1 
ATOM 806  C CB  . LEU A 1 106 ? 191.687 169.211 135.923 1.00 112.52 ? 106 LEU A CB  1 
ATOM 807  C CG  . LEU A 1 106 ? 193.171 169.279 136.284 1.00 112.52 ? 106 LEU A CG  1 
ATOM 808  C CD1 . LEU A 1 106 ? 193.398 170.282 137.400 1.00 112.52 ? 106 LEU A CD1 1 
ATOM 809  C CD2 . LEU A 1 106 ? 193.697 167.908 136.682 1.00 112.52 ? 106 LEU A CD2 1 
ATOM 810  N N   . PHE A 1 107 ? 191.123 166.655 134.167 1.00 110.59 ? 107 PHE A N   1 
ATOM 811  C CA  . PHE A 1 107 ? 191.491 165.338 133.663 1.00 110.59 ? 107 PHE A CA  1 
ATOM 812  C C   . PHE A 1 107 ? 190.999 165.100 132.244 1.00 110.59 ? 107 PHE A C   1 
ATOM 813  O O   . PHE A 1 107 ? 191.676 164.415 131.469 1.00 110.59 ? 107 PHE A O   1 
ATOM 814  C CB  . PHE A 1 107 ? 190.942 164.252 134.589 1.00 110.59 ? 107 PHE A CB  1 
ATOM 815  C CG  . PHE A 1 107 ? 191.760 164.050 135.830 1.00 110.59 ? 107 PHE A CG  1 
ATOM 816  C CD1 . PHE A 1 107 ? 191.625 164.904 136.909 1.00 110.59 ? 107 PHE A CD1 1 
ATOM 817  C CD2 . PHE A 1 107 ? 192.667 163.010 135.916 1.00 110.59 ? 107 PHE A CD2 1 
ATOM 818  C CE1 . PHE A 1 107 ? 192.377 164.723 138.049 1.00 110.59 ? 107 PHE A CE1 1 
ATOM 819  C CE2 . PHE A 1 107 ? 193.421 162.824 137.055 1.00 110.59 ? 107 PHE A CE2 1 
ATOM 820  C CZ  . PHE A 1 107 ? 193.277 163.682 138.122 1.00 110.59 ? 107 PHE A CZ  1 
ATOM 821  N N   . ASN A 1 108 ? 189.843 165.648 131.888 1.00 120.43 ? 108 ASN A N   1 
ATOM 822  C CA  . ASN A 1 108 ? 189.320 165.579 130.530 1.00 120.43 ? 108 ASN A CA  1 
ATOM 823  C C   . ASN A 1 108 ? 189.231 164.133 130.035 1.00 120.43 ? 108 ASN A C   1 
ATOM 824  O O   . ASN A 1 108 ? 189.927 163.750 129.091 1.00 120.43 ? 108 ASN A O   1 
ATOM 825  C CB  . ASN A 1 108 ? 190.174 166.417 129.587 1.00 120.43 ? 108 ASN A CB  1 
ATOM 826  C CG  . ASN A 1 108 ? 189.543 166.584 128.220 1.00 120.43 ? 108 ASN A CG  1 
ATOM 827  O OD1 . ASN A 1 108 ? 188.325 166.708 128.095 1.00 120.43 ? 108 ASN A OD1 1 
ATOM 828  N ND2 . ASN A 1 108 ? 190.373 166.592 127.183 1.00 120.43 ? 108 ASN A ND2 1 
ATOM 829  N N   . PRO A 1 109 ? 188.383 163.303 130.659 1.00 101.22 ? 109 PRO A N   1 
ATOM 830  C CA  . PRO A 1 109 ? 188.186 161.922 130.210 1.00 101.22 ? 109 PRO A CA  1 
ATOM 831  C C   . PRO A 1 109 ? 187.335 161.830 128.948 1.00 101.22 ? 109 PRO A C   1 
ATOM 832  O O   . PRO A 1 109 ? 186.124 162.021 129.037 1.00 101.22 ? 109 PRO A O   1 
ATOM 833  C CB  . PRO A 1 109 ? 187.475 161.269 131.395 1.00 101.22 ? 109 PRO A CB  1 
ATOM 834  C CG  . PRO A 1 109 ? 186.754 162.381 132.053 1.00 101.22 ? 109 PRO A CG  1 
ATOM 835  C CD  . PRO A 1 109 ? 187.602 163.605 131.870 1.00 101.22 ? 109 PRO A CD  1 
ATOM 836  N N   . PRO A 1 128 ? 161.805 169.166 134.375 1.00 123.74 ? 128 PRO A N   1 
ATOM 837  C CA  . PRO A 1 128 ? 161.008 170.000 135.252 1.00 123.74 ? 128 PRO A CA  1 
ATOM 838  C C   . PRO A 1 128 ? 161.714 171.254 135.759 1.00 123.74 ? 128 PRO A C   1 
ATOM 839  O O   . PRO A 1 128 ? 162.928 171.228 135.956 1.00 123.74 ? 128 PRO A O   1 
ATOM 840  C CB  . PRO A 1 128 ? 160.722 169.038 136.406 1.00 123.74 ? 128 PRO A CB  1 
ATOM 841  C CG  . PRO A 1 128 ? 160.843 167.599 135.719 1.00 123.74 ? 128 PRO A CG  1 
ATOM 842  C CD  . PRO A 1 128 ? 161.039 167.912 134.249 1.00 123.74 ? 128 PRO A CD  1 
ATOM 843  N N   . PRO A 1 129 ? 160.959 172.330 135.984 1.00 124.24 ? 129 PRO A N   1 
ATOM 844  C CA  . PRO A 1 129 ? 161.569 173.552 136.522 1.00 124.24 ? 129 PRO A CA  1 
ATOM 845  C C   . PRO A 1 129 ? 161.905 173.423 137.999 1.00 124.24 ? 129 PRO A C   1 
ATOM 846  O O   . PRO A 1 129 ? 161.605 172.405 138.630 1.00 124.24 ? 129 PRO A O   1 
ATOM 847  C CB  . PRO A 1 129 ? 160.493 174.613 136.277 1.00 124.24 ? 129 PRO A CB  1 
ATOM 848  C CG  . PRO A 1 129 ? 159.211 173.856 136.312 1.00 124.24 ? 129 PRO A CG  1 
ATOM 849  C CD  . PRO A 1 129 ? 159.505 172.475 135.791 1.00 124.24 ? 129 PRO A CD  1 
ATOM 850  N N   . LEU A 1 130 ? 162.522 174.463 138.561 1.00 118.28 ? 130 LEU A N   1 
ATOM 851  C CA  . LEU A 1 130 ? 162.973 174.397 139.947 1.00 118.28 ? 130 LEU A CA  1 
ATOM 852  C C   . LEU A 1 130 ? 161.803 174.240 140.912 1.00 118.28 ? 130 LEU A C   1 
ATOM 853  O O   . LEU A 1 130 ? 161.887 173.474 141.879 1.00 118.28 ? 130 LEU A O   1 
ATOM 854  C CB  . LEU A 1 130 ? 163.782 175.651 140.283 1.00 118.28 ? 130 LEU A CB  1 
ATOM 855  C CG  . LEU A 1 130 ? 164.022 175.975 141.758 1.00 118.28 ? 130 LEU A CG  1 
ATOM 856  C CD1 . LEU A 1 130 ? 164.751 174.832 142.445 1.00 118.28 ? 130 LEU A CD1 1 
ATOM 857  C CD2 . LEU A 1 130 ? 164.809 177.269 141.870 1.00 118.28 ? 130 LEU A CD2 1 
ATOM 858  N N   . VAL A 1 131 ? 160.701 174.951 140.668 1.00 110.95 ? 131 VAL A N   1 
ATOM 859  C CA  . VAL A 1 131 ? 159.659 175.063 141.687 1.00 110.95 ? 131 VAL A CA  1 
ATOM 860  C C   . VAL A 1 131 ? 159.054 173.701 142.008 1.00 110.95 ? 131 VAL A C   1 
ATOM 861  O O   . VAL A 1 131 ? 158.888 173.346 143.181 1.00 110.95 ? 131 VAL A O   1 
ATOM 862  C CB  . VAL A 1 131 ? 158.588 176.080 141.248 1.00 110.95 ? 131 VAL A CB  1 
ATOM 863  C CG1 . VAL A 1 131 ? 157.639 175.478 140.220 1.00 110.95 ? 131 VAL A CG1 1 
ATOM 864  C CG2 . VAL A 1 131 ? 157.822 176.583 142.459 1.00 110.95 ? 131 VAL A CG2 1 
ATOM 865  N N   . HIS A 1 132 ? 158.721 172.909 140.985 1.00 118.91 ? 132 HIS A N   1 
ATOM 866  C CA  . HIS A 1 132 ? 158.117 171.608 141.259 1.00 118.91 ? 132 HIS A CA  1 
ATOM 867  C C   . HIS A 1 132 ? 159.089 170.679 141.972 1.00 118.91 ? 132 HIS A C   1 
ATOM 868  O O   . HIS A 1 132 ? 158.661 169.785 142.709 1.00 118.91 ? 132 HIS A O   1 
ATOM 869  C CB  . HIS A 1 132 ? 157.600 170.960 139.974 1.00 118.91 ? 132 HIS A CB  1 
ATOM 870  C CG  . HIS A 1 132 ? 156.779 171.876 139.122 1.00 118.91 ? 132 HIS A CG  1 
ATOM 871  N ND1 . HIS A 1 132 ? 157.050 172.098 137.789 1.00 118.91 ? 132 HIS A ND1 1 
ATOM 872  C CD2 . HIS A 1 132 ? 155.685 172.620 139.412 1.00 118.91 ? 132 HIS A CD2 1 
ATOM 873  C CE1 . HIS A 1 132 ? 156.161 172.942 137.296 1.00 118.91 ? 132 HIS A CE1 1 
ATOM 874  N NE2 . HIS A 1 132 ? 155.322 173.274 138.260 1.00 118.91 ? 132 HIS A NE2 1 
ATOM 875  N N   . ILE A 1 133 ? 160.393 170.864 141.767 1.00 105.37 ? 133 ILE A N   1 
ATOM 876  C CA  . ILE A 1 133 ? 161.361 170.135 142.580 1.00 105.37 ? 133 ILE A CA  1 
ATOM 877  C C   . ILE A 1 133 ? 161.220 170.539 144.040 1.00 105.37 ? 133 ILE A C   1 
ATOM 878  O O   . ILE A 1 133 ? 161.244 169.692 144.940 1.00 105.37 ? 133 ILE A O   1 
ATOM 879  C CB  . ILE A 1 133 ? 162.793 170.376 142.067 1.00 105.37 ? 133 ILE A CB  1 
ATOM 880  C CG1 . ILE A 1 133 ? 162.926 170.044 140.574 1.00 105.37 ? 133 ILE A CG1 1 
ATOM 881  C CG2 . ILE A 1 133 ? 163.786 169.556 142.877 1.00 105.37 ? 133 ILE A CG2 1 
ATOM 882  C CD1 . ILE A 1 133 ? 161.981 168.971 140.055 1.00 105.37 ? 133 ILE A CD1 1 
ATOM 883  N N   . LEU A 1 134 ? 161.074 171.839 144.297 1.00 99.59  ? 134 LEU A N   1 
ATOM 884  C CA  . LEU A 1 134 ? 160.915 172.308 145.669 1.00 99.59  ? 134 LEU A CA  1 
ATOM 885  C C   . LEU A 1 134 ? 159.563 171.899 146.239 1.00 99.59  ? 134 LEU A C   1 
ATOM 886  O O   . LEU A 1 134 ? 159.478 171.460 147.391 1.00 99.59  ? 134 LEU A O   1 
ATOM 887  C CB  . LEU A 1 134 ? 161.085 173.826 145.719 1.00 99.59  ? 134 LEU A CB  1 
ATOM 888  C CG  . LEU A 1 134 ? 161.332 174.446 147.095 1.00 99.59  ? 134 LEU A CG  1 
ATOM 889  C CD1 . LEU A 1 134 ? 161.956 175.821 146.940 1.00 99.59  ? 134 LEU A CD1 1 
ATOM 890  C CD2 . LEU A 1 134 ? 160.047 174.535 147.903 1.00 99.59  ? 134 LEU A CD2 1 
ATOM 891  N N   . LEU A 1 135 ? 158.496 172.030 145.448 1.00 94.74  ? 135 LEU A N   1 
ATOM 892  C CA  . LEU A 1 135 ? 157.166 171.702 145.950 1.00 94.74  ? 135 LEU A CA  1 
ATOM 893  C C   . LEU A 1 135 ? 157.055 170.233 146.329 1.00 94.74  ? 135 LEU A C   1 
ATOM 894  O O   . LEU A 1 135 ? 156.251 169.876 147.196 1.00 94.74  ? 135 LEU A O   1 
ATOM 895  C CB  . LEU A 1 135 ? 156.108 172.052 144.906 1.00 94.74  ? 135 LEU A CB  1 
ATOM 896  C CG  . LEU A 1 135 ? 155.747 173.531 144.785 1.00 94.74  ? 135 LEU A CG  1 
ATOM 897  C CD1 . LEU A 1 135 ? 154.842 173.752 143.588 1.00 94.74  ? 135 LEU A CD1 1 
ATOM 898  C CD2 . LEU A 1 135 ? 155.087 174.036 146.056 1.00 94.74  ? 135 LEU A CD2 1 
ATOM 899  N N   . ASP A 1 136 ? 157.848 169.368 145.698 1.00 100.00 ? 136 ASP A N   1 
ATOM 900  C CA  . ASP A 1 136 ? 157.796 167.947 146.013 1.00 100.00 ? 136 ASP A CA  1 
ATOM 901  C C   . ASP A 1 136 ? 158.293 167.642 147.418 1.00 100.00 ? 136 ASP A C   1 
ATOM 902  O O   . ASP A 1 136 ? 158.108 166.515 147.888 1.00 100.00 ? 136 ASP A O   1 
ATOM 903  C CB  . ASP A 1 136 ? 158.617 167.153 144.997 1.00 100.00 ? 136 ASP A CB  1 
ATOM 904  C CG  . ASP A 1 136 ? 157.779 166.649 143.838 1.00 100.00 ? 136 ASP A CG  1 
ATOM 905  O OD1 . ASP A 1 136 ? 156.628 166.225 144.072 1.00 100.00 ? 136 ASP A OD1 1 
ATOM 906  O OD2 . ASP A 1 136 ? 158.271 166.678 142.691 1.00 100.00 ? 136 ASP A OD2 1 
ATOM 907  N N   . ILE A 1 137 ? 158.921 168.607 148.092 1.00 88.41  ? 137 ILE A N   1 
ATOM 908  C CA  . ILE A 1 137 ? 159.343 168.401 149.470 1.00 88.41  ? 137 ILE A CA  1 
ATOM 909  C C   . ILE A 1 137 ? 158.148 168.172 150.380 1.00 88.41  ? 137 ILE A C   1 
ATOM 910  O O   . ILE A 1 137 ? 158.293 167.578 151.453 1.00 88.41  ? 137 ILE A O   1 
ATOM 911  C CB  . ILE A 1 137 ? 160.180 169.600 149.958 1.00 88.41  ? 137 ILE A CB  1 
ATOM 912  C CG1 . ILE A 1 137 ? 161.456 169.727 149.126 1.00 88.41  ? 137 ILE A CG1 1 
ATOM 913  C CG2 . ILE A 1 137 ? 160.524 169.442 151.429 1.00 88.41  ? 137 ILE A CG2 1 
ATOM 914  C CD1 . ILE A 1 137 ? 162.182 171.038 149.319 1.00 88.41  ? 137 ILE A CD1 1 
ATOM 915  N N   . VAL A 1 138 ? 156.965 168.630 149.981 1.00 75.42  ? 138 VAL A N   1 
ATOM 916  C CA  . VAL A 1 138 ? 155.742 168.446 150.756 1.00 75.42  ? 138 VAL A CA  1 
ATOM 917  C C   . VAL A 1 138 ? 154.967 167.293 150.123 1.00 75.42  ? 138 VAL A C   1 
ATOM 918  O O   . VAL A 1 138 ? 154.414 167.466 149.025 1.00 75.42  ? 138 VAL A O   1 
ATOM 919  C CB  . VAL A 1 138 ? 154.900 169.727 150.788 1.00 75.42  ? 138 VAL A CB  1 
ATOM 920  C CG1 . VAL A 1 138 ? 153.645 169.518 151.617 1.00 75.42  ? 138 VAL A CG1 1 
ATOM 921  C CG2 . VAL A 1 138 ? 155.717 170.884 151.335 1.00 75.42  ? 138 VAL A CG2 1 
ATOM 922  N N   . PRO A 1 139 ? 154.894 166.124 150.759 1.00 81.25  ? 139 PRO A N   1 
ATOM 923  C CA  . PRO A 1 139 ? 154.187 164.998 150.136 1.00 81.25  ? 139 PRO A CA  1 
ATOM 924  C C   . PRO A 1 139 ? 152.684 165.223 150.141 1.00 81.25  ? 139 PRO A C   1 
ATOM 925  O O   . PRO A 1 139 ? 152.104 165.624 151.152 1.00 81.25  ? 139 PRO A O   1 
ATOM 926  C CB  . PRO A 1 139 ? 154.578 163.801 151.008 1.00 81.25  ? 139 PRO A CB  1 
ATOM 927  C CG  . PRO A 1 139 ? 154.936 164.383 152.320 1.00 81.25  ? 139 PRO A CG  1 
ATOM 928  C CD  . PRO A 1 139 ? 155.460 165.765 152.071 1.00 81.25  ? 139 PRO A CD  1 
ATOM 929  N N   . THR A 1 140 ? 152.053 164.960 148.997 1.00 86.69  ? 140 THR A N   1 
ATOM 930  C CA  . THR A 1 140 ? 150.599 165.007 148.933 1.00 86.69  ? 140 THR A CA  1 
ATOM 931  C C   . THR A 1 140 ? 149.961 163.866 149.711 1.00 86.69  ? 140 THR A C   1 
ATOM 932  O O   . THR A 1 140 ? 148.761 163.921 149.997 1.00 86.69  ? 140 THR A O   1 
ATOM 933  C CB  . THR A 1 140 ? 150.132 164.972 147.478 1.00 86.69  ? 140 THR A CB  1 
ATOM 934  O OG1 . THR A 1 140 ? 148.710 165.136 147.425 1.00 86.69  ? 140 THR A OG1 1 
ATOM 935  C CG2 . THR A 1 140 ? 150.514 163.656 146.818 1.00 86.69  ? 140 THR A CG2 1 
ATOM 936  N N   . ASN A 1 141 ? 150.734 162.840 150.057 1.00 91.01  ? 141 ASN A N   1 
ATOM 937  C CA  . ASN A 1 141 ? 150.235 161.711 150.841 1.00 91.01  ? 141 ASN A CA  1 
ATOM 938  C C   . ASN A 1 141 ? 151.415 161.134 151.610 1.00 91.01  ? 141 ASN A C   1 
ATOM 939  O O   . ASN A 1 141 ? 152.253 160.423 151.033 1.00 91.01  ? 141 ASN A O   1 
ATOM 940  C CB  . ASN A 1 141 ? 149.590 160.650 149.954 1.00 91.01  ? 141 ASN A CB  1 
ATOM 941  C CG  . ASN A 1 141 ? 148.889 159.573 150.753 1.00 91.01  ? 141 ASN A CG  1 
ATOM 942  O OD1 . ASN A 1 141 ? 149.237 159.311 151.902 1.00 91.01  ? 141 ASN A OD1 1 
ATOM 943  N ND2 . ASN A 1 141 ? 147.893 158.941 150.145 1.00 91.01  ? 141 ASN A ND2 1 
ATOM 944  N N   . PRO A 1 142 ? 151.524 161.415 152.913 1.00 78.30  ? 142 PRO A N   1 
ATOM 945  C CA  . PRO A 1 142 ? 152.708 160.939 153.647 1.00 78.30  ? 142 PRO A CA  1 
ATOM 946  C C   . PRO A 1 142 ? 152.894 159.436 153.573 1.00 78.30  ? 142 PRO A C   1 
ATOM 947  O O   . PRO A 1 142 ? 154.031 158.962 153.458 1.00 78.30  ? 142 PRO A O   1 
ATOM 948  C CB  . PRO A 1 142 ? 152.445 161.415 155.082 1.00 78.30  ? 142 PRO A CB  1 
ATOM 949  C CG  . PRO A 1 142 ? 150.982 161.620 155.160 1.00 78.30  ? 142 PRO A CG  1 
ATOM 950  C CD  . PRO A 1 142 ? 150.560 162.078 153.805 1.00 78.30  ? 142 PRO A CD  1 
ATOM 951  N N   . PHE A 1 143 ? 151.806 158.667 153.632 1.00 84.61  ? 143 PHE A N   1 
ATOM 952  C CA  . PHE A 1 143 ? 151.925 157.224 153.460 1.00 84.61  ? 143 PHE A CA  1 
ATOM 953  C C   . PHE A 1 143 ? 152.405 156.881 152.058 1.00 84.61  ? 143 PHE A C   1 
ATOM 954  O O   . PHE A 1 143 ? 153.236 155.984 151.881 1.00 84.61  ? 143 PHE A O   1 
ATOM 955  C CB  . PHE A 1 143 ? 150.588 156.547 153.751 1.00 84.61  ? 143 PHE A CB  1 
ATOM 956  C CG  . PHE A 1 143 ? 150.085 156.781 155.143 1.00 84.61  ? 143 PHE A CG  1 
ATOM 957  C CD1 . PHE A 1 143 ? 150.800 156.328 156.236 1.00 84.61  ? 143 PHE A CD1 1 
ATOM 958  C CD2 . PHE A 1 143 ? 148.897 157.454 155.360 1.00 84.61  ? 143 PHE A CD2 1 
ATOM 959  C CE1 . PHE A 1 143 ? 150.342 156.542 157.517 1.00 84.61  ? 143 PHE A CE1 1 
ATOM 960  C CE2 . PHE A 1 143 ? 148.433 157.670 156.640 1.00 84.61  ? 143 PHE A CE2 1 
ATOM 961  C CZ  . PHE A 1 143 ? 149.157 157.213 157.720 1.00 84.61  ? 143 PHE A CZ  1 
ATOM 962  N N   . GLY A 1 144 ? 151.894 157.585 151.048 1.00 95.20  ? 144 GLY A N   1 
ATOM 963  C CA  . GLY A 1 144 ? 152.363 157.354 149.693 1.00 95.20  ? 144 GLY A CA  1 
ATOM 964  C C   . GLY A 1 144 ? 153.846 157.627 149.543 1.00 95.20  ? 144 GLY A C   1 
ATOM 965  O O   . GLY A 1 144 ? 154.554 156.902 148.841 1.00 95.20  ? 144 GLY A O   1 
ATOM 966  N N   . ALA A 1 145 ? 154.337 158.680 150.200 1.00 88.29  ? 145 ALA A N   1 
ATOM 967  C CA  . ALA A 1 145 ? 155.767 158.962 150.169 1.00 88.29  ? 145 ALA A CA  1 
ATOM 968  C C   . ALA A 1 145 ? 156.560 157.817 150.783 1.00 88.29  ? 145 ALA A C   1 
ATOM 969  O O   . ALA A 1 145 ? 157.595 157.410 150.244 1.00 88.29  ? 145 ALA A O   1 
ATOM 970  C CB  . ALA A 1 145 ? 156.058 160.269 150.903 1.00 88.29  ? 145 ALA A CB  1 
ATOM 971  N N   . LEU A 1 146 ? 156.092 157.287 151.913 1.00 88.30  ? 146 LEU A N   1 
ATOM 972  C CA  . LEU A 1 146 ? 156.764 156.147 152.524 1.00 88.30  ? 146 LEU A CA  1 
ATOM 973  C C   . LEU A 1 146 ? 156.690 154.918 151.628 1.00 88.30  ? 146 LEU A C   1 
ATOM 974  O O   . LEU A 1 146 ? 157.675 154.184 151.490 1.00 88.30  ? 146 LEU A O   1 
ATOM 975  C CB  . LEU A 1 146 ? 156.150 155.849 153.890 1.00 88.30  ? 146 LEU A CB  1 
ATOM 976  C CG  . LEU A 1 146 ? 156.509 156.840 154.996 1.00 88.30  ? 146 LEU A CG  1 
ATOM 977  C CD1 . LEU A 1 146 ? 155.535 156.722 156.153 1.00 88.30  ? 146 LEU A CD1 1 
ATOM 978  C CD2 . LEU A 1 146 ? 157.932 156.612 155.467 1.00 88.30  ? 146 LEU A CD2 1 
ATOM 979  N N   . ALA A 1 147 ? 155.533 154.679 151.008 1.00 100.73 ? 147 ALA A N   1 
ATOM 980  C CA  . ALA A 1 147 ? 155.394 153.515 150.141 1.00 100.73 ? 147 ALA A CA  1 
ATOM 981  C C   . ALA A 1 147 ? 156.407 153.558 149.006 1.00 100.73 ? 147 ALA A C   1 
ATOM 982  O O   . ALA A 1 147 ? 157.048 152.548 148.696 1.00 100.73 ? 147 ALA A O   1 
ATOM 983  C CB  . ALA A 1 147 ? 153.973 153.440 149.587 1.00 100.73 ? 147 ALA A CB  1 
ATOM 984  N N   . ASN A 1 148 ? 156.566 154.717 148.377 1.00 98.26  ? 148 ASN A N   1 
ATOM 985  C CA  . ASN A 1 148 ? 157.600 154.896 147.375 1.00 98.26  ? 148 ASN A CA  1 
ATOM 986  C C   . ASN A 1 148 ? 158.926 155.236 148.049 1.00 98.26  ? 148 ASN A C   1 
ATOM 987  O O   . ASN A 1 148 ? 159.012 155.405 149.267 1.00 98.26  ? 148 ASN A O   1 
ATOM 988  C CB  . ASN A 1 148 ? 157.201 155.990 146.389 1.00 98.26  ? 148 ASN A CB  1 
ATOM 989  C CG  . ASN A 1 148 ? 155.790 155.817 145.871 1.00 98.26  ? 148 ASN A CG  1 
ATOM 990  O OD1 . ASN A 1 148 ? 155.269 154.704 145.821 1.00 98.26  ? 148 ASN A OD1 1 
ATOM 991  N ND2 . ASN A 1 148 ? 155.162 156.920 145.485 1.00 98.26  ? 148 ASN A ND2 1 
ATOM 992  N N   . GLY A 1 149 ? 159.972 155.337 147.237 1.00 101.18 ? 149 GLY A N   1 
ATOM 993  C CA  . GLY A 1 149 ? 161.288 155.650 147.756 1.00 101.18 ? 149 GLY A CA  1 
ATOM 994  C C   . GLY A 1 149 ? 161.553 157.139 147.818 1.00 101.18 ? 149 GLY A C   1 
ATOM 995  O O   . GLY A 1 149 ? 162.704 157.575 147.720 1.00 101.18 ? 149 GLY A O   1 
ATOM 996  N N   . GLN A 1 150 ? 160.498 157.932 147.986 1.00 90.50  ? 150 GLN A N   1 
ATOM 997  C CA  . GLN A 1 150 ? 160.618 159.388 148.011 1.00 90.50  ? 150 GLN A CA  1 
ATOM 998  C C   . GLN A 1 150 ? 161.152 159.796 149.377 1.00 90.50  ? 150 GLN A C   1 
ATOM 999  O O   . GLN A 1 150 ? 160.398 160.064 150.313 1.00 90.50  ? 150 GLN A O   1 
ATOM 1000 C CB  . GLN A 1 150 ? 159.277 160.042 147.711 1.00 90.50  ? 150 GLN A CB  1 
ATOM 1001 C CG  . GLN A 1 150 ? 158.857 159.942 146.258 1.00 90.50  ? 150 GLN A CG  1 
ATOM 1002 C CD  . GLN A 1 150 ? 157.356 160.008 146.084 1.00 90.50  ? 150 GLN A CD  1 
ATOM 1003 O OE1 . GLN A 1 150 ? 156.724 159.038 145.671 1.00 90.50  ? 150 GLN A OE1 1 
ATOM 1004 N NE2 . GLN A 1 150 ? 156.776 161.159 146.401 1.00 90.50  ? 150 GLN A NE2 1 
ATOM 1005 N N   . VAL A 1 151 ? 162.479 159.841 149.489 1.00 88.70  ? 151 VAL A N   1 
ATOM 1006 C CA  . VAL A 1 151 ? 163.110 160.111 150.777 1.00 88.70  ? 151 VAL A CA  1 
ATOM 1007 C C   . VAL A 1 151 ? 162.863 161.551 151.207 1.00 88.70  ? 151 VAL A C   1 
ATOM 1008 O O   . VAL A 1 151 ? 162.500 161.817 152.357 1.00 88.70  ? 151 VAL A O   1 
ATOM 1009 C CB  . VAL A 1 151 ? 164.615 159.798 150.706 1.00 88.70  ? 151 VAL A CB  1 
ATOM 1010 C CG1 . VAL A 1 151 ? 165.293 160.133 152.024 1.00 88.70  ? 151 VAL A CG1 1 
ATOM 1011 C CG2 . VAL A 1 151 ? 164.832 158.339 150.341 1.00 88.70  ? 151 VAL A CG2 1 
ATOM 1012 N N   . LEU A 1 152 ? 163.060 162.500 150.294 1.00 92.18  ? 152 LEU A N   1 
ATOM 1013 C CA  . LEU A 1 152 ? 163.022 163.908 150.683 1.00 92.18  ? 152 LEU A CA  1 
ATOM 1014 C C   . LEU A 1 152 ? 161.688 164.316 151.286 1.00 92.18  ? 152 LEU A C   1 
ATOM 1015 O O   . LEU A 1 152 ? 161.684 164.873 152.397 1.00 92.18  ? 152 LEU A O   1 
ATOM 1016 C CB  . LEU A 1 152 ? 163.371 164.781 149.475 1.00 92.18  ? 152 LEU A CB  1 
ATOM 1017 C CG  . LEU A 1 152 ? 163.385 166.289 149.727 1.00 92.18  ? 152 LEU A CG  1 
ATOM 1018 C CD1 . LEU A 1 152 ? 164.231 166.635 150.941 1.00 92.18  ? 152 LEU A CD1 1 
ATOM 1019 C CD2 . LEU A 1 152 ? 163.892 167.017 148.496 1.00 92.18  ? 152 LEU A CD2 1 
ATOM 1020 N N   . PRO A 1 153 ? 160.541 164.087 150.643 1.00 82.64  ? 153 PRO A N   1 
ATOM 1021 C CA  . PRO A 1 153 ? 159.273 164.431 151.302 1.00 82.64  ? 153 PRO A CA  1 
ATOM 1022 C C   . PRO A 1 153 ? 159.048 163.671 152.592 1.00 82.64  ? 153 PRO A C   1 
ATOM 1023 O O   . PRO A 1 153 ? 158.436 164.213 153.520 1.00 82.64  ? 153 PRO A O   1 
ATOM 1024 C CB  . PRO A 1 153 ? 158.218 164.084 150.244 1.00 82.64  ? 153 PRO A CB  1 
ATOM 1025 C CG  . PRO A 1 153 ? 158.887 163.163 149.312 1.00 82.64  ? 153 PRO A CG  1 
ATOM 1026 C CD  . PRO A 1 153 ? 160.325 163.555 149.289 1.00 82.64  ? 153 PRO A CD  1 
ATOM 1027 N N   . THR A 1 154 ? 159.525 162.428 152.684 1.00 84.57  ? 154 THR A N   1 
ATOM 1028 C CA  . THR A 1 154 ? 159.396 161.688 153.934 1.00 84.57  ? 154 THR A CA  1 
ATOM 1029 C C   . THR A 1 154 ? 160.126 162.391 155.067 1.00 84.57  ? 154 THR A C   1 
ATOM 1030 O O   . THR A 1 154 ? 159.679 162.344 156.218 1.00 84.57  ? 154 THR A O   1 
ATOM 1031 C CB  . THR A 1 154 ? 159.931 160.268 153.765 1.00 84.57  ? 154 THR A CB  1 
ATOM 1032 O OG1 . THR A 1 154 ? 159.133 159.566 152.805 1.00 84.57  ? 154 THR A OG1 1 
ATOM 1033 C CG2 . THR A 1 154 ? 159.893 159.525 155.088 1.00 84.57  ? 154 THR A CG2 1 
ATOM 1034 N N   . ILE A 1 155 ? 161.252 163.040 154.767 1.00 83.98  ? 155 ILE A N   1 
ATOM 1035 C CA  . ILE A 1 155 ? 161.947 163.821 155.784 1.00 83.98  ? 155 ILE A CA  1 
ATOM 1036 C C   . ILE A 1 155 ? 161.063 164.963 156.264 1.00 83.98  ? 155 ILE A C   1 
ATOM 1037 O O   . ILE A 1 155 ? 160.958 165.223 157.468 1.00 83.98  ? 155 ILE A O   1 
ATOM 1038 C CB  . ILE A 1 155 ? 163.289 164.337 155.236 1.00 83.98  ? 155 ILE A CB  1 
ATOM 1039 C CG1 . ILE A 1 155 ? 164.336 163.225 155.282 1.00 83.98  ? 155 ILE A CG1 1 
ATOM 1040 C CG2 . ILE A 1 155 ? 163.758 165.552 156.024 1.00 83.98  ? 155 ILE A CG2 1 
ATOM 1041 C CD1 . ILE A 1 155 ? 165.583 163.527 154.486 1.00 83.98  ? 155 ILE A CD1 1 
ATOM 1042 N N   . PHE A 1 156 ? 160.412 165.662 155.333 1.00 73.81  ? 156 PHE A N   1 
ATOM 1043 C CA  . PHE A 1 156 ? 159.564 166.783 155.719 1.00 73.81  ? 156 PHE A CA  1 
ATOM 1044 C C   . PHE A 1 156 ? 158.454 166.330 156.657 1.00 73.81  ? 156 PHE A C   1 
ATOM 1045 O O   . PHE A 1 156 ? 158.210 166.953 157.695 1.00 73.81  ? 156 PHE A O   1 
ATOM 1046 C CB  . PHE A 1 156 ? 158.975 167.448 154.478 1.00 73.81  ? 156 PHE A CB  1 
ATOM 1047 C CG  . PHE A 1 156 ? 158.009 168.550 154.789 1.00 73.81  ? 156 PHE A CG  1 
ATOM 1048 C CD1 . PHE A 1 156 ? 158.460 169.827 155.060 1.00 73.81  ? 156 PHE A CD1 1 
ATOM 1049 C CD2 . PHE A 1 156 ? 156.648 168.307 154.816 1.00 73.81  ? 156 PHE A CD2 1 
ATOM 1050 C CE1 . PHE A 1 156 ? 157.574 170.842 155.349 1.00 73.81  ? 156 PHE A CE1 1 
ATOM 1051 C CE2 . PHE A 1 156 ? 155.758 169.318 155.105 1.00 73.81  ? 156 PHE A CE2 1 
ATOM 1052 C CZ  . PHE A 1 156 ? 156.221 170.587 155.371 1.00 73.81  ? 156 PHE A CZ  1 
ATOM 1053 N N   . PHE A 1 157 ? 157.770 165.240 156.310 1.00 77.55  ? 157 PHE A N   1 
ATOM 1054 C CA  . PHE A 1 157 ? 156.709 164.742 157.177 1.00 77.55  ? 157 PHE A CA  1 
ATOM 1055 C C   . PHE A 1 157 ? 157.267 164.293 158.520 1.00 77.55  ? 157 PHE A C   1 
ATOM 1056 O O   . PHE A 1 157 ? 156.655 164.534 159.567 1.00 77.55  ? 157 PHE A O   1 
ATOM 1057 C CB  . PHE A 1 157 ? 155.966 163.594 156.499 1.00 77.55  ? 157 PHE A CB  1 
ATOM 1058 C CG  . PHE A 1 157 ? 154.827 163.055 157.308 1.00 77.55  ? 157 PHE A CG  1 
ATOM 1059 C CD1 . PHE A 1 157 ? 153.722 163.841 157.579 1.00 77.55  ? 157 PHE A CD1 1 
ATOM 1060 C CD2 . PHE A 1 157 ? 154.858 161.764 157.799 1.00 77.55  ? 157 PHE A CD2 1 
ATOM 1061 C CE1 . PHE A 1 157 ? 152.671 163.349 158.323 1.00 77.55  ? 157 PHE A CE1 1 
ATOM 1062 C CE2 . PHE A 1 157 ? 153.809 161.267 158.544 1.00 77.55  ? 157 PHE A CE2 1 
ATOM 1063 C CZ  . PHE A 1 157 ? 152.715 162.061 158.806 1.00 77.55  ? 157 PHE A CZ  1 
ATOM 1064 N N   . ALA A 1 158 ? 158.426 163.634 158.511 1.00 74.33  ? 158 ALA A N   1 
ATOM 1065 C CA  . ALA A 1 158 ? 159.020 163.167 159.758 1.00 74.33  ? 158 ALA A CA  1 
ATOM 1066 C C   . ALA A 1 158 ? 159.283 164.328 160.707 1.00 74.33  ? 158 ALA A C   1 
ATOM 1067 O O   . ALA A 1 158 ? 158.905 164.283 161.883 1.00 74.33  ? 158 ALA A O   1 
ATOM 1068 C CB  . ALA A 1 158 ? 160.312 162.407 159.466 1.00 74.33  ? 158 ALA A CB  1 
ATOM 1069 N N   . ILE A 1 159 ? 159.926 165.386 160.211 1.00 74.99  ? 159 ILE A N   1 
ATOM 1070 C CA  . ILE A 1 159 ? 160.206 166.540 161.058 1.00 74.99  ? 159 ILE A CA  1 
ATOM 1071 C C   . ILE A 1 159 ? 158.908 167.204 161.493 1.00 74.99  ? 159 ILE A C   1 
ATOM 1072 O O   . ILE A 1 159 ? 158.743 167.573 162.662 1.00 74.99  ? 159 ILE A O   1 
ATOM 1073 C CB  . ILE A 1 159 ? 161.135 167.525 160.326 1.00 74.99  ? 159 ILE A CB  1 
ATOM 1074 C CG1 . ILE A 1 159 ? 162.426 166.808 159.923 1.00 74.99  ? 159 ILE A CG1 1 
ATOM 1075 C CG2 . ILE A 1 159 ? 161.440 168.732 161.204 1.00 74.99  ? 159 ILE A CG2 1 
ATOM 1076 C CD1 . ILE A 1 159 ? 163.594 167.725 159.651 1.00 74.99  ? 159 ILE A CD1 1 
ATOM 1077 N N   . ILE A 1 160 ? 157.965 167.368 160.564 1.00 77.82  ? 160 ILE A N   1 
ATOM 1078 C CA  . ILE A 1 160 ? 156.681 167.963 160.915 1.00 77.82  ? 160 ILE A CA  1 
ATOM 1079 C C   . ILE A 1 160 ? 155.983 167.118 161.970 1.00 77.82  ? 160 ILE A C   1 
ATOM 1080 O O   . ILE A 1 160 ? 155.438 167.643 162.948 1.00 77.82  ? 160 ILE A O   1 
ATOM 1081 C CB  . ILE A 1 160 ? 155.810 168.130 159.656 1.00 77.82  ? 160 ILE A CB  1 
ATOM 1082 C CG1 . ILE A 1 160 ? 156.343 169.256 158.764 1.00 77.82  ? 160 ILE A CG1 1 
ATOM 1083 C CG2 . ILE A 1 160 ? 154.366 168.410 160.036 1.00 77.82  ? 160 ILE A CG2 1 
ATOM 1084 C CD1 . ILE A 1 160 ? 156.481 170.602 159.447 1.00 77.82  ? 160 ILE A CD1 1 
ATOM 1085 N N   . LEU A 1 161 ? 155.986 165.797 161.790 1.00 79.04  ? 161 LEU A N   1 
ATOM 1086 C CA  . LEU A 1 161 ? 155.418 164.919 162.806 1.00 79.04  ? 161 LEU A CA  1 
ATOM 1087 C C   . LEU A 1 161 ? 156.206 165.005 164.105 1.00 79.04  ? 161 LEU A C   1 
ATOM 1088 O O   . LEU A 1 161 ? 155.622 165.024 165.194 1.00 79.04  ? 161 LEU A O   1 
ATOM 1089 C CB  . LEU A 1 161 ? 155.384 163.481 162.293 1.00 79.04  ? 161 LEU A CB  1 
ATOM 1090 C CG  . LEU A 1 161 ? 154.759 162.445 163.227 1.00 79.04  ? 161 LEU A CG  1 
ATOM 1091 C CD1 . LEU A 1 161 ? 153.344 162.840 163.607 1.00 79.04  ? 161 LEU A CD1 1 
ATOM 1092 C CD2 . LEU A 1 161 ? 154.773 161.073 162.577 1.00 79.04  ? 161 LEU A CD2 1 
ATOM 1093 N N   . GLY A 1 162 ? 157.534 165.059 164.011 1.00 77.33  ? 162 GLY A N   1 
ATOM 1094 C CA  . GLY A 1 162 ? 158.343 165.135 165.217 1.00 77.33  ? 162 GLY A CA  1 
ATOM 1095 C C   . GLY A 1 162 ? 158.083 166.401 166.008 1.00 77.33  ? 162 GLY A C   1 
ATOM 1096 O O   . GLY A 1 162 ? 157.933 166.365 167.231 1.00 77.33  ? 162 GLY A O   1 
ATOM 1097 N N   . ILE A 1 163 ? 158.025 167.542 165.319 1.00 79.88  ? 163 ILE A N   1 
ATOM 1098 C CA  . ILE A 1 163 ? 157.764 168.804 166.004 1.00 79.88  ? 163 ILE A CA  1 
ATOM 1099 C C   . ILE A 1 163 ? 156.369 168.797 166.610 1.00 79.88  ? 163 ILE A C   1 
ATOM 1100 O O   . ILE A 1 163 ? 156.162 169.267 167.735 1.00 79.88  ? 163 ILE A O   1 
ATOM 1101 C CB  . ILE A 1 163 ? 157.952 169.987 165.038 1.00 79.88  ? 163 ILE A CB  1 
ATOM 1102 C CG1 . ILE A 1 163 ? 159.403 170.056 164.565 1.00 79.88  ? 163 ILE A CG1 1 
ATOM 1103 C CG2 . ILE A 1 163 ? 157.553 171.287 165.717 1.00 79.88  ? 163 ILE A CG2 1 
ATOM 1104 C CD1 . ILE A 1 163 ? 159.644 171.079 163.481 1.00 79.88  ? 163 ILE A CD1 1 
ATOM 1105 N N   . ALA A 1 164 ? 155.390 168.268 165.876 1.00 75.98  ? 164 ALA A N   1 
ATOM 1106 C CA  . ALA A 1 164 ? 154.025 168.234 166.388 1.00 75.98  ? 164 ALA A CA  1 
ATOM 1107 C C   . ALA A 1 164 ? 153.941 167.421 167.671 1.00 75.98  ? 164 ALA A C   1 
ATOM 1108 O O   . ALA A 1 164 ? 153.219 167.793 168.603 1.00 75.98  ? 164 ALA A O   1 
ATOM 1109 C CB  . ALA A 1 164 ? 153.085 167.662 165.330 1.00 75.98  ? 164 ALA A CB  1 
ATOM 1110 N N   . ILE A 1 165 ? 154.676 166.310 167.742 1.00 82.12  ? 165 ILE A N   1 
ATOM 1111 C CA  . ILE A 1 165 ? 154.606 165.453 168.922 1.00 82.12  ? 165 ILE A CA  1 
ATOM 1112 C C   . ILE A 1 165 ? 155.034 166.221 170.164 1.00 82.12  ? 165 ILE A C   1 
ATOM 1113 O O   . ILE A 1 165 ? 154.396 166.126 171.219 1.00 82.12  ? 165 ILE A O   1 
ATOM 1114 C CB  . ILE A 1 165 ? 155.460 164.189 168.716 1.00 82.12  ? 165 ILE A CB  1 
ATOM 1115 C CG1 . ILE A 1 165 ? 154.728 163.203 167.807 1.00 82.12  ? 165 ILE A CG1 1 
ATOM 1116 C CG2 . ILE A 1 165 ? 155.777 163.538 170.050 1.00 82.12  ? 165 ILE A CG2 1 
ATOM 1117 C CD1 . ILE A 1 165 ? 155.629 162.162 167.189 1.00 82.12  ? 165 ILE A CD1 1 
ATOM 1118 N N   . THR A 1 166 ? 156.113 167.000 170.063 1.00 78.48  ? 166 THR A N   1 
ATOM 1119 C CA  . THR A 1 166 ? 156.579 167.749 171.226 1.00 78.48  ? 166 THR A CA  1 
ATOM 1120 C C   . THR A 1 166 ? 155.485 168.662 171.757 1.00 78.48  ? 166 THR A C   1 
ATOM 1121 O O   . THR A 1 166 ? 155.258 168.731 172.970 1.00 78.48  ? 166 THR A O   1 
ATOM 1122 C CB  . THR A 1 166 ? 157.819 168.567 170.875 1.00 78.48  ? 166 THR A CB  1 
ATOM 1123 O OG1 . THR A 1 166 ? 157.474 169.571 169.913 1.00 78.48  ? 166 THR A OG1 1 
ATOM 1124 C CG2 . THR A 1 166 ? 158.904 167.678 170.308 1.00 78.48  ? 166 THR A CG2 1 
ATOM 1125 N N   . TYR A 1 167 ? 154.790 169.367 170.864 1.00 83.06  ? 167 TYR A N   1 
ATOM 1126 C CA  . TYR A 1 167 ? 153.700 170.226 171.305 1.00 83.06  ? 167 TYR A CA  1 
ATOM 1127 C C   . TYR A 1 167 ? 152.616 169.424 172.009 1.00 83.06  ? 167 TYR A C   1 
ATOM 1128 O O   . TYR A 1 167 ? 151.956 169.938 172.919 1.00 83.06  ? 167 TYR A O   1 
ATOM 1129 C CB  . TYR A 1 167 ? 153.114 170.982 170.116 1.00 83.06  ? 167 TYR A CB  1 
ATOM 1130 C CG  . TYR A 1 167 ? 153.969 172.137 169.662 1.00 83.06  ? 167 TYR A CG  1 
ATOM 1131 C CD1 . TYR A 1 167 ? 154.034 173.307 170.401 1.00 83.06  ? 167 TYR A CD1 1 
ATOM 1132 C CD2 . TYR A 1 167 ? 154.712 172.057 168.496 1.00 83.06  ? 167 TYR A CD2 1 
ATOM 1133 C CE1 . TYR A 1 167 ? 154.815 174.365 169.992 1.00 83.06  ? 167 TYR A CE1 1 
ATOM 1134 C CE2 . TYR A 1 167 ? 155.496 173.109 168.078 1.00 83.06  ? 167 TYR A CE2 1 
ATOM 1135 C CZ  . TYR A 1 167 ? 155.544 174.261 168.829 1.00 83.06  ? 167 TYR A CZ  1 
ATOM 1136 O OH  . TYR A 1 167 ? 156.325 175.314 168.415 1.00 83.06  ? 167 TYR A OH  1 
ATOM 1137 N N   . LEU A 1 168 ? 152.415 168.169 171.605 1.00 78.75  ? 168 LEU A N   1 
ATOM 1138 C CA  . LEU A 1 168 ? 151.455 167.323 172.304 1.00 78.75  ? 168 LEU A CA  1 
ATOM 1139 C C   . LEU A 1 168 ? 151.981 166.912 173.671 1.00 78.75  ? 168 LEU A C   1 
ATOM 1140 O O   . LEU A 1 168 ? 151.245 166.951 174.662 1.00 78.75  ? 168 LEU A O   1 
ATOM 1141 C CB  . LEU A 1 168 ? 151.131 166.089 171.465 1.00 78.75  ? 168 LEU A CB  1 
ATOM 1142 C CG  . LEU A 1 168 ? 150.501 166.355 170.100 1.00 78.75  ? 168 LEU A CG  1 
ATOM 1143 C CD1 . LEU A 1 168 ? 150.348 165.057 169.332 1.00 78.75  ? 168 LEU A CD1 1 
ATOM 1144 C CD2 . LEU A 1 168 ? 149.162 167.052 170.247 1.00 78.75  ? 168 LEU A CD2 1 
ATOM 1145 N N   . MET A 1 169 ? 153.256 166.525 173.748 1.00 83.49  ? 169 MET A N   1 
ATOM 1146 C CA  . MET A 1 169 ? 153.808 166.069 175.017 1.00 83.49  ? 169 MET A CA  1 
ATOM 1147 C C   . MET A 1 169 ? 153.730 167.140 176.092 1.00 83.49  ? 169 MET A C   1 
ATOM 1148 O O   . MET A 1 169 ? 153.713 166.809 177.281 1.00 83.49  ? 169 MET A O   1 
ATOM 1149 C CB  . MET A 1 169 ? 155.260 165.628 174.839 1.00 83.49  ? 169 MET A CB  1 
ATOM 1150 C CG  . MET A 1 169 ? 155.486 164.689 173.672 1.00 83.49  ? 169 MET A CG  1 
ATOM 1151 S SD  . MET A 1 169 ? 156.752 163.461 174.023 1.00 83.49  ? 169 MET A SD  1 
ATOM 1152 C CE  . MET A 1 169 ? 155.919 162.505 175.283 1.00 83.49  ? 169 MET A CE  1 
ATOM 1153 N N   . ASN A 1 170 ? 153.685 168.410 175.705 1.00 88.62  ? 170 ASN A N   1 
ATOM 1154 C CA  . ASN A 1 170 ? 153.504 169.503 176.648 1.00 88.62  ? 170 ASN A CA  1 
ATOM 1155 C C   . ASN A 1 170 ? 152.042 169.882 176.825 1.00 88.62  ? 170 ASN A C   1 
ATOM 1156 O O   . ASN A 1 170 ? 151.746 170.815 177.578 1.00 88.62  ? 170 ASN A O   1 
ATOM 1157 C CB  . ASN A 1 170 ? 154.298 170.727 176.187 1.00 88.62  ? 170 ASN A CB  1 
ATOM 1158 C CG  . ASN A 1 170 ? 155.786 170.465 176.131 1.00 88.62  ? 170 ASN A CG  1 
ATOM 1159 O OD1 . ASN A 1 170 ? 156.272 169.472 176.671 1.00 88.62  ? 170 ASN A OD1 1 
ATOM 1160 N ND2 . ASN A 1 170 ? 156.519 171.352 175.470 1.00 88.62  ? 170 ASN A ND2 1 
ATOM 1161 N N   . SER A 1 171 ? 151.128 169.186 176.155 1.00 90.82  ? 171 SER A N   1 
ATOM 1162 C CA  . SER A 1 171 ? 149.716 169.517 176.255 1.00 90.82  ? 171 SER A CA  1 
ATOM 1163 C C   . SER A 1 171 ? 149.199 169.241 177.659 1.00 90.82  ? 171 SER A C   1 
ATOM 1164 O O   . SER A 1 171 ? 149.590 168.266 178.305 1.00 90.82  ? 171 SER A O   1 
ATOM 1165 C CB  . SER A 1 171 ? 148.910 168.714 175.237 1.00 90.82  ? 171 SER A CB  1 
ATOM 1166 O OG  . SER A 1 171 ? 147.544 169.088 175.266 1.00 90.82  ? 171 SER A OG  1 
ATOM 1167 N N   . GLU A 1 172 ? 148.310 170.115 178.131 1.00 110.77 ? 172 GLU A N   1 
ATOM 1168 C CA  . GLU A 1 172 ? 147.720 169.937 179.451 1.00 110.77 ? 172 GLU A CA  1 
ATOM 1169 C C   . GLU A 1 172 ? 146.780 168.742 179.506 1.00 110.77 ? 172 GLU A C   1 
ATOM 1170 O O   . GLU A 1 172 ? 146.572 168.184 180.588 1.00 110.77 ? 172 GLU A O   1 
ATOM 1171 C CB  . GLU A 1 172 ? 146.992 171.221 179.867 1.00 110.77 ? 172 GLU A CB  1 
ATOM 1172 C CG  . GLU A 1 172 ? 145.836 171.646 178.958 1.00 110.77 ? 172 GLU A CG  1 
ATOM 1173 C CD  . GLU A 1 172 ? 144.574 170.821 179.145 1.00 110.77 ? 172 GLU A CD  1 
ATOM 1174 O OE1 . GLU A 1 172 ? 143.645 170.968 178.323 1.00 110.77 ? 172 GLU A OE1 1 
ATOM 1175 O OE2 . GLU A 1 172 ? 144.492 170.051 180.125 1.00 110.77 ? 172 GLU A OE2 1 
ATOM 1176 N N   . ASN A 1 173 ? 146.207 168.339 178.375 1.00 99.52  ? 173 ASN A N   1 
ATOM 1177 C CA  . ASN A 1 173 ? 145.281 167.214 178.361 1.00 99.52  ? 173 ASN A CA  1 
ATOM 1178 C C   . ASN A 1 173 ? 146.039 165.923 178.639 1.00 99.52  ? 173 ASN A C   1 
ATOM 1179 O O   . ASN A 1 173 ? 146.935 165.544 177.879 1.00 99.52  ? 173 ASN A O   1 
ATOM 1180 C CB  . ASN A 1 173 ? 144.562 167.138 177.018 1.00 99.52  ? 173 ASN A CB  1 
ATOM 1181 C CG  . ASN A 1 173 ? 143.418 166.147 177.028 1.00 99.52  ? 173 ASN A CG  1 
ATOM 1182 O OD1 . ASN A 1 173 ? 143.286 165.343 177.950 1.00 99.52  ? 173 ASN A OD1 1 
ATOM 1183 N ND2 . ASN A 1 173 ? 142.580 166.201 175.999 1.00 99.52  ? 173 ASN A ND2 1 
ATOM 1184 N N   . GLU A 1 174 ? 145.670 165.242 179.724 1.00 98.02  ? 174 GLU A N   1 
ATOM 1185 C CA  . GLU A 1 174 ? 146.396 164.041 180.121 1.00 98.02  ? 174 GLU A CA  1 
ATOM 1186 C C   . GLU A 1 174 ? 146.325 162.970 179.041 1.00 98.02  ? 174 GLU A C   1 
ATOM 1187 O O   . GLU A 1 174 ? 147.331 162.321 178.734 1.00 98.02  ? 174 GLU A O   1 
ATOM 1188 C CB  . GLU A 1 174 ? 145.836 163.510 181.439 1.00 98.02  ? 174 GLU A CB  1 
ATOM 1189 C CG  . GLU A 1 174 ? 146.373 162.150 181.842 1.00 98.02  ? 174 GLU A CG  1 
ATOM 1190 C CD  . GLU A 1 174 ? 146.075 161.819 183.290 1.00 98.02  ? 174 GLU A CD  1 
ATOM 1191 O OE1 . GLU A 1 174 ? 146.363 162.662 184.165 1.00 98.02  ? 174 GLU A OE1 1 
ATOM 1192 O OE2 . GLU A 1 174 ? 145.552 160.716 183.554 1.00 98.02  ? 174 GLU A OE2 1 
ATOM 1193 N N   . LYS A 1 175 ? 145.146 162.771 178.451 1.00 91.16  ? 175 LYS A N   1 
ATOM 1194 C CA  . LYS A 1 175 ? 145.005 161.747 177.423 1.00 91.16  ? 175 LYS A CA  1 
ATOM 1195 C C   . LYS A 1 175 ? 145.879 162.056 176.215 1.00 91.16  ? 175 LYS A C   1 
ATOM 1196 O O   . LYS A 1 175 ? 146.509 161.155 175.649 1.00 91.16  ? 175 LYS A O   1 
ATOM 1197 C CB  . LYS A 1 175 ? 143.542 161.622 177.005 1.00 91.16  ? 175 LYS A CB  1 
ATOM 1198 C CG  . LYS A 1 175 ? 143.287 160.538 175.972 1.00 91.16  ? 175 LYS A CG  1 
ATOM 1199 C CD  . LYS A 1 175 ? 141.810 160.196 175.882 1.00 91.16  ? 175 LYS A CD  1 
ATOM 1200 C CE  . LYS A 1 175 ? 141.561 159.055 174.910 1.00 91.16  ? 175 LYS A CE  1 
ATOM 1201 N NZ  . LYS A 1 175 ? 141.655 159.499 173.492 1.00 91.16  ? 175 LYS A NZ  1 
ATOM 1202 N N   . VAL A 1 176 ? 145.926 163.322 175.801 1.00 80.13  ? 176 VAL A N   1 
ATOM 1203 C CA  . VAL A 1 176 ? 146.744 163.692 174.649 1.00 80.13  ? 176 VAL A CA  1 
ATOM 1204 C C   . VAL A 1 176 ? 148.213 163.424 174.941 1.00 80.13  ? 176 VAL A C   1 
ATOM 1205 O O   . VAL A 1 176 ? 148.938 162.862 174.112 1.00 80.13  ? 176 VAL A O   1 
ATOM 1206 C CB  . VAL A 1 176 ? 146.508 165.165 174.276 1.00 80.13  ? 176 VAL A CB  1 
ATOM 1207 C CG1 . VAL A 1 176 ? 147.511 165.613 173.230 1.00 80.13  ? 176 VAL A CG1 1 
ATOM 1208 C CG2 . VAL A 1 176 ? 145.088 165.362 173.776 1.00 80.13  ? 176 VAL A CG2 1 
ATOM 1209 N N   . ARG A 1 177 ? 148.675 163.820 176.127 1.00 86.50  ? 177 ARG A N   1 
ATOM 1210 C CA  . ARG A 1 177 ? 150.073 163.601 176.481 1.00 86.50  ? 177 ARG A CA  1 
ATOM 1211 C C   . ARG A 1 177 ? 150.409 162.117 176.495 1.00 86.50  ? 177 ARG A C   1 
ATOM 1212 O O   . ARG A 1 177 ? 151.447 161.703 175.968 1.00 86.50  ? 177 ARG A O   1 
ATOM 1213 C CB  . ARG A 1 177 ? 150.369 164.232 177.840 1.00 86.50  ? 177 ARG A CB  1 
ATOM 1214 C CG  . ARG A 1 177 ? 151.840 164.252 178.202 1.00 86.50  ? 177 ARG A CG  1 
ATOM 1215 C CD  . ARG A 1 177 ? 152.130 165.282 179.278 1.00 86.50  ? 177 ARG A CD  1 
ATOM 1216 N NE  . ARG A 1 177 ? 151.313 165.075 180.468 1.00 86.50  ? 177 ARG A NE  1 
ATOM 1217 C CZ  . ARG A 1 177 ? 150.221 165.766 180.768 1.00 86.50  ? 177 ARG A CZ  1 
ATOM 1218 N NH1 . ARG A 1 177 ? 149.766 166.726 179.978 1.00 86.50  ? 177 ARG A NH1 1 
ATOM 1219 N NH2 . ARG A 1 177 ? 149.565 165.486 181.891 1.00 86.50  ? 177 ARG A NH2 1 
ATOM 1220 N N   . LYS A 1 178 ? 149.542 161.299 177.092 1.00 84.94  ? 178 LYS A N   1 
ATOM 1221 C CA  . LYS A 1 178 ? 149.786 159.861 177.123 1.00 84.94  ? 178 LYS A CA  1 
ATOM 1222 C C   . LYS A 1 178 ? 149.791 159.281 175.715 1.00 84.94  ? 178 LYS A C   1 
ATOM 1223 O O   . LYS A 1 178 ? 150.683 158.507 175.353 1.00 84.94  ? 178 LYS A O   1 
ATOM 1224 C CB  . LYS A 1 178 ? 148.728 159.177 177.989 1.00 84.94  ? 178 LYS A CB  1 
ATOM 1225 C CG  . LYS A 1 178 ? 148.695 157.663 177.869 1.00 84.94  ? 178 LYS A CG  1 
ATOM 1226 C CD  . LYS A 1 178 ? 150.054 157.051 178.151 1.00 84.94  ? 178 LYS A CD  1 
ATOM 1227 C CE  . LYS A 1 178 ? 149.924 155.623 178.655 1.00 84.94  ? 178 LYS A CE  1 
ATOM 1228 N NZ  . LYS A 1 178 ? 149.317 154.722 177.636 1.00 84.94  ? 178 LYS A NZ  1 
ATOM 1229 N N   . SER A 1 179 ? 148.799 159.648 174.903 1.00 86.04  ? 179 SER A N   1 
ATOM 1230 C CA  . SER A 1 179 ? 148.729 159.120 173.545 1.00 86.04  ? 179 SER A CA  1 
ATOM 1231 C C   . SER A 1 179 ? 149.917 159.582 172.714 1.00 86.04  ? 179 SER A C   1 
ATOM 1232 O O   . SER A 1 179 ? 150.504 158.793 171.966 1.00 86.04  ? 179 SER A O   1 
ATOM 1233 C CB  . SER A 1 179 ? 147.417 159.542 172.887 1.00 86.04  ? 179 SER A CB  1 
ATOM 1234 O OG  . SER A 1 179 ? 147.196 160.931 173.043 1.00 86.04  ? 179 SER A OG  1 
ATOM 1235 N N   . ALA A 1 180 ? 150.288 160.857 172.830 1.00 79.96  ? 180 ALA A N   1 
ATOM 1236 C CA  . ALA A 1 180 ? 151.446 161.351 172.093 1.00 79.96  ? 180 ALA A CA  1 
ATOM 1237 C C   . ALA A 1 180 ? 152.717 160.645 172.540 1.00 79.96  ? 180 ALA A C   1 
ATOM 1238 O O   . ALA A 1 180 ? 153.567 160.297 171.713 1.00 79.96  ? 180 ALA A O   1 
ATOM 1239 C CB  . ALA A 1 180 ? 151.581 162.860 172.275 1.00 79.96  ? 180 ALA A CB  1 
ATOM 1240 N N   . GLU A 1 181 ? 152.867 160.426 173.847 1.00 85.62  ? 181 GLU A N   1 
ATOM 1241 C CA  . GLU A 1 181 ? 154.053 159.742 174.348 1.00 85.62  ? 181 GLU A CA  1 
ATOM 1242 C C   . GLU A 1 181 ? 154.136 158.324 173.803 1.00 85.62  ? 181 GLU A C   1 
ATOM 1243 O O   . GLU A 1 181 ? 155.215 157.858 173.422 1.00 85.62  ? 181 GLU A O   1 
ATOM 1244 C CB  . GLU A 1 181 ? 154.040 159.732 175.876 1.00 85.62  ? 181 GLU A CB  1 
ATOM 1245 C CG  . GLU A 1 181 ? 155.117 158.871 176.506 1.00 85.62  ? 181 GLU A CG  1 
ATOM 1246 C CD  . GLU A 1 181 ? 155.133 158.976 178.017 1.00 85.62  ? 181 GLU A CD  1 
ATOM 1247 O OE1 . GLU A 1 181 ? 154.042 159.026 178.621 1.00 85.62  ? 181 GLU A OE1 1 
ATOM 1248 O OE2 . GLU A 1 181 ? 156.238 159.008 178.600 1.00 85.62  ? 181 GLU A OE2 1 
ATOM 1249 N N   . THR A 1 182 ? 153.004 157.620 173.757 1.00 77.10  ? 182 THR A N   1 
ATOM 1250 C CA  . THR A 1 182 ? 153.003 156.261 173.230 1.00 77.10  ? 182 THR A CA  1 
ATOM 1251 C C   . THR A 1 182 ? 153.405 156.240 171.762 1.00 77.10  ? 182 THR A C   1 
ATOM 1252 O O   . THR A 1 182 ? 154.148 155.354 171.327 1.00 77.10  ? 182 THR A O   1 
ATOM 1253 C CB  . THR A 1 182 ? 151.625 155.628 173.413 1.00 77.10  ? 182 THR A CB  1 
ATOM 1254 O OG1 . THR A 1 182 ? 151.367 155.437 174.809 1.00 77.10  ? 182 THR A OG1 1 
ATOM 1255 C CG2 . THR A 1 182 ? 151.552 154.291 172.699 1.00 77.10  ? 182 THR A CG2 1 
ATOM 1256 N N   . LEU A 1 183 ? 152.920 157.205 170.981 1.00 76.67  ? 183 LEU A N   1 
ATOM 1257 C CA  . LEU A 1 183 ? 153.281 157.252 169.569 1.00 76.67  ? 183 LEU A CA  1 
ATOM 1258 C C   . LEU A 1 183 ? 154.782 157.426 169.395 1.00 76.67  ? 183 LEU A C   1 
ATOM 1259 O O   . LEU A 1 183 ? 155.402 156.748 168.568 1.00 76.67  ? 183 LEU A O   1 
ATOM 1260 C CB  . LEU A 1 183 ? 152.528 158.384 168.873 1.00 76.67  ? 183 LEU A CB  1 
ATOM 1261 C CG  . LEU A 1 183 ? 152.948 158.682 167.434 1.00 76.67  ? 183 LEU A CG  1 
ATOM 1262 C CD1 . LEU A 1 183 ? 152.952 157.418 166.597 1.00 76.67  ? 183 LEU A CD1 1 
ATOM 1263 C CD2 . LEU A 1 183 ? 152.025 159.719 166.826 1.00 76.67  ? 183 LEU A CD2 1 
ATOM 1264 N N   . LEU A 1 184 ? 155.387 158.328 170.169 1.00 84.18  ? 184 LEU A N   1 
ATOM 1265 C CA  . LEU A 1 184 ? 156.829 158.517 170.080 1.00 84.18  ? 184 LEU A CA  1 
ATOM 1266 C C   . LEU A 1 184 ? 157.572 157.254 170.492 1.00 84.18  ? 184 LEU A C   1 
ATOM 1267 O O   . LEU A 1 184 ? 158.563 156.873 169.858 1.00 84.18  ? 184 LEU A O   1 
ATOM 1268 C CB  . LEU A 1 184 ? 157.256 159.697 170.950 1.00 84.18  ? 184 LEU A CB  1 
ATOM 1269 C CG  . LEU A 1 184 ? 158.744 160.044 170.911 1.00 84.18  ? 184 LEU A CG  1 
ATOM 1270 C CD1 . LEU A 1 184 ? 159.183 160.371 169.496 1.00 84.18  ? 184 LEU A CD1 1 
ATOM 1271 C CD2 . LEU A 1 184 ? 159.039 161.201 171.846 1.00 84.18  ? 184 LEU A CD2 1 
ATOM 1272 N N   . ASP A 1 185 ? 157.110 156.590 171.553 1.00 84.80  ? 185 ASP A N   1 
ATOM 1273 C CA  . ASP A 1 185 ? 157.759 155.358 171.984 1.00 84.80  ? 185 ASP A CA  1 
ATOM 1274 C C   . ASP A 1 185 ? 157.691 154.296 170.898 1.00 84.80  ? 185 ASP A C   1 
ATOM 1275 O O   . ASP A 1 185 ? 158.680 153.604 170.633 1.00 84.80  ? 185 ASP A O   1 
ATOM 1276 C CB  . ASP A 1 185 ? 157.113 154.848 173.270 1.00 84.80  ? 185 ASP A CB  1 
ATOM 1277 C CG  . ASP A 1 185 ? 157.523 155.650 174.487 1.00 84.80  ? 185 ASP A CG  1 
ATOM 1278 O OD1 . ASP A 1 185 ? 158.427 156.501 174.363 1.00 84.80  ? 185 ASP A OD1 1 
ATOM 1279 O OD2 . ASP A 1 185 ? 156.942 155.428 175.569 1.00 84.80  ? 185 ASP A OD2 1 
ATOM 1280 N N   . ALA A 1 186 ? 156.532 154.150 170.255 1.00 80.31  ? 186 ALA A N   1 
ATOM 1281 C CA  . ALA A 1 186 ? 156.404 153.168 169.185 1.00 80.31  ? 186 ALA A CA  1 
ATOM 1282 C C   . ALA A 1 186 ? 157.360 153.484 168.043 1.00 80.31  ? 186 ALA A C   1 
ATOM 1283 O O   . ALA A 1 186 ? 158.059 152.598 167.539 1.00 80.31  ? 186 ALA A O   1 
ATOM 1284 C CB  . ALA A 1 186 ? 154.961 153.126 168.684 1.00 80.31  ? 186 ALA A CB  1 
ATOM 1285 N N   . ILE A 1 187 ? 157.407 154.748 167.623 1.00 74.11  ? 187 ILE A N   1 
ATOM 1286 C CA  . ILE A 1 187 ? 158.342 155.138 166.573 1.00 74.11  ? 187 ILE A CA  1 
ATOM 1287 C C   . ILE A 1 187 ? 159.776 154.972 167.054 1.00 74.11  ? 187 ILE A C   1 
ATOM 1288 O O   . ILE A 1 187 ? 160.639 154.483 166.317 1.00 74.11  ? 187 ILE A O   1 
ATOM 1289 C CB  . ILE A 1 187 ? 158.061 156.579 166.114 1.00 74.11  ? 187 ILE A CB  1 
ATOM 1290 C CG1 . ILE A 1 187 ? 156.735 156.640 165.357 1.00 74.11  ? 187 ILE A CG1 1 
ATOM 1291 C CG2 . ILE A 1 187 ? 159.196 157.082 165.239 1.00 74.11  ? 187 ILE A CG2 1 
ATOM 1292 C CD1 . ILE A 1 187 ? 156.209 158.040 165.157 1.00 74.11  ? 187 ILE A CD1 1 
ATOM 1293 N N   . ASN A 1 188 ? 160.057 155.372 168.295 1.00 81.36  ? 188 ASN A N   1 
ATOM 1294 C CA  . ASN A 1 188 ? 161.409 155.227 168.819 1.00 81.36  ? 188 ASN A CA  1 
ATOM 1295 C C   . ASN A 1 188 ? 161.836 153.767 168.824 1.00 81.36  ? 188 ASN A C   1 
ATOM 1296 O O   . ASN A 1 188 ? 162.973 153.444 168.464 1.00 81.36  ? 188 ASN A O   1 
ATOM 1297 C CB  . ASN A 1 188 ? 161.495 155.814 170.225 1.00 81.36  ? 188 ASN A CB  1 
ATOM 1298 C CG  . ASN A 1 188 ? 162.877 155.683 170.822 1.00 81.36  ? 188 ASN A CG  1 
ATOM 1299 O OD1 . ASN A 1 188 ? 163.877 155.685 170.105 1.00 81.36  ? 188 ASN A OD1 1 
ATOM 1300 N ND2 . ASN A 1 188 ? 162.943 155.565 172.141 1.00 81.36  ? 188 ASN A ND2 1 
ATOM 1301 N N   . GLY A 1 189 ? 160.938 152.869 169.227 1.00 80.18  ? 189 GLY A N   1 
ATOM 1302 C CA  . GLY A 1 189 ? 161.245 151.453 169.135 1.00 80.18  ? 189 GLY A CA  1 
ATOM 1303 C C   . GLY A 1 189 ? 161.576 151.035 167.717 1.00 80.18  ? 189 GLY A C   1 
ATOM 1304 O O   . GLY A 1 189 ? 162.499 150.251 167.489 1.00 80.18  ? 189 GLY A O   1 
ATOM 1305 N N   . LEU A 1 190 ? 160.832 151.561 166.742 1.00 75.03  ? 190 LEU A N   1 
ATOM 1306 C CA  . LEU A 1 190 ? 161.141 151.275 165.347 1.00 75.03  ? 190 LEU A CA  1 
ATOM 1307 C C   . LEU A 1 190 ? 162.525 151.792 164.978 1.00 75.03  ? 190 LEU A C   1 
ATOM 1308 O O   . LEU A 1 190 ? 163.288 151.108 164.289 1.00 75.03  ? 190 LEU A O   1 
ATOM 1309 C CB  . LEU A 1 190 ? 160.079 151.890 164.438 1.00 75.03  ? 190 LEU A CB  1 
ATOM 1310 C CG  . LEU A 1 190 ? 160.341 151.795 162.935 1.00 75.03  ? 190 LEU A CG  1 
ATOM 1311 C CD1 . LEU A 1 190 ? 160.589 150.357 162.522 1.00 75.03  ? 190 LEU A CD1 1 
ATOM 1312 C CD2 . LEU A 1 190 ? 159.176 152.381 162.159 1.00 75.03  ? 190 LEU A CD2 1 
ATOM 1313 N N   . ALA A 1 191 ? 162.867 152.999 165.431 1.00 82.55  ? 191 ALA A N   1 
ATOM 1314 C CA  . ALA A 1 191 ? 164.195 153.534 165.154 1.00 82.55  ? 191 ALA A CA  1 
ATOM 1315 C C   . ALA A 1 191 ? 165.276 152.668 165.786 1.00 82.55  ? 191 ALA A C   1 
ATOM 1316 O O   . ALA A 1 191 ? 166.304 152.391 165.160 1.00 82.55  ? 191 ALA A O   1 
ATOM 1317 C CB  . ALA A 1 191 ? 164.297 154.971 165.658 1.00 82.55  ? 191 ALA A CB  1 
ATOM 1318 N N   . GLU A 1 192 ? 165.066 152.233 167.030 1.00 81.08  ? 192 GLU A N   1 
ATOM 1319 C CA  . GLU A 1 192 ? 166.030 151.341 167.663 1.00 81.08  ? 192 GLU A CA  1 
ATOM 1320 C C   . GLU A 1 192 ? 166.115 150.018 166.917 1.00 81.08  ? 192 GLU A C   1 
ATOM 1321 O O   . GLU A 1 192 ? 167.211 149.489 166.696 1.00 81.08  ? 192 GLU A O   1 
ATOM 1322 C CB  . GLU A 1 192 ? 165.653 151.116 169.130 1.00 81.08  ? 192 GLU A CB  1 
ATOM 1323 C CG  . GLU A 1 192 ? 166.287 149.886 169.795 1.00 81.08  ? 192 GLU A CG  1 
ATOM 1324 C CD  . GLU A 1 192 ? 165.536 148.586 169.530 1.00 81.08  ? 192 GLU A CD  1 
ATOM 1325 O OE1 . GLU A 1 192 ? 164.556 148.602 168.757 1.00 81.08  ? 192 GLU A OE1 1 
ATOM 1326 O OE2 . GLU A 1 192 ? 165.924 147.546 170.104 1.00 81.08  ? 192 GLU A OE2 1 
ATOM 1327 N N   . ALA A 1 193 ? 164.968 149.468 166.516 1.00 80.49  ? 193 ALA A N   1 
ATOM 1328 C CA  . ALA A 1 193 ? 164.970 148.189 165.816 1.00 80.49  ? 193 ALA A CA  1 
ATOM 1329 C C   . ALA A 1 193 ? 165.745 148.280 164.510 1.00 80.49  ? 193 ALA A C   1 
ATOM 1330 O O   . ALA A 1 193 ? 166.531 147.385 164.183 1.00 80.49  ? 193 ALA A O   1 
ATOM 1331 C CB  . ALA A 1 193 ? 163.537 147.732 165.556 1.00 80.49  ? 193 ALA A CB  1 
ATOM 1332 N N   . MET A 1 194 ? 165.542 149.358 163.752 1.00 85.09  ? 194 MET A N   1 
ATOM 1333 C CA  . MET A 1 194 ? 166.255 149.505 162.489 1.00 85.09  ? 194 MET A CA  1 
ATOM 1334 C C   . MET A 1 194 ? 167.757 149.594 162.719 1.00 85.09  ? 194 MET A C   1 
ATOM 1335 O O   . MET A 1 194 ? 168.543 149.011 161.964 1.00 85.09  ? 194 MET A O   1 
ATOM 1336 C CB  . MET A 1 194 ? 165.750 150.735 161.741 1.00 85.09  ? 194 MET A CB  1 
ATOM 1337 C CG  . MET A 1 194 ? 164.313 150.612 161.265 1.00 85.09  ? 194 MET A CG  1 
ATOM 1338 S SD  . MET A 1 194 ? 164.003 149.228 160.145 1.00 85.09  ? 194 MET A SD  1 
ATOM 1339 C CE  . MET A 1 194 ? 165.495 149.207 159.156 1.00 85.09  ? 194 MET A CE  1 
ATOM 1340 N N   . TYR A 1 195 ? 168.178 150.316 163.757 1.00 82.24  ? 195 TYR A N   1 
ATOM 1341 C CA  . TYR A 1 195 ? 169.596 150.340 164.093 1.00 82.24  ? 195 TYR A CA  1 
ATOM 1342 C C   . TYR A 1 195 ? 170.098 148.939 164.406 1.00 82.24  ? 195 TYR A C   1 
ATOM 1343 O O   . TYR A 1 195 ? 171.200 148.559 163.994 1.00 82.24  ? 195 TYR A O   1 
ATOM 1344 C CB  . TYR A 1 195 ? 169.844 151.272 165.277 1.00 82.24  ? 195 TYR A CB  1 
ATOM 1345 C CG  . TYR A 1 195 ? 169.560 152.729 164.991 1.00 82.24  ? 195 TYR A CG  1 
ATOM 1346 C CD1 . TYR A 1 195 ? 169.816 153.278 163.744 1.00 82.24  ? 195 TYR A CD1 1 
ATOM 1347 C CD2 . TYR A 1 195 ? 169.039 153.556 165.974 1.00 82.24  ? 195 TYR A CD2 1 
ATOM 1348 C CE1 . TYR A 1 195 ? 169.558 154.606 163.485 1.00 82.24  ? 195 TYR A CE1 1 
ATOM 1349 C CE2 . TYR A 1 195 ? 168.779 154.884 165.724 1.00 82.24  ? 195 TYR A CE2 1 
ATOM 1350 C CZ  . TYR A 1 195 ? 169.040 155.404 164.478 1.00 82.24  ? 195 TYR A CZ  1 
ATOM 1351 O OH  . TYR A 1 195 ? 168.781 156.729 164.227 1.00 82.24  ? 195 TYR A OH  1 
ATOM 1352 N N   . LYS A 1 196 ? 169.305 148.153 165.135 1.00 79.98  ? 196 LYS A N   1 
ATOM 1353 C CA  . LYS A 1 196 ? 169.676 146.764 165.372 1.00 79.98  ? 196 LYS A CA  1 
ATOM 1354 C C   . LYS A 1 196 ? 169.734 145.988 164.065 1.00 79.98  ? 196 LYS A C   1 
ATOM 1355 O O   . LYS A 1 196 ? 170.647 145.183 163.852 1.00 79.98  ? 196 LYS A O   1 
ATOM 1356 C CB  . LYS A 1 196 ? 168.689 146.112 166.338 1.00 79.98  ? 196 LYS A CB  1 
ATOM 1357 C CG  . LYS A 1 196 ? 169.137 146.151 167.784 1.00 79.98  ? 196 LYS A CG  1 
ATOM 1358 C CD  . LYS A 1 196 ? 170.249 145.154 168.042 1.00 79.98  ? 196 LYS A CD  1 
ATOM 1359 C CE  . LYS A 1 196 ? 170.553 145.040 169.522 1.00 79.98  ? 196 LYS A CE  1 
ATOM 1360 N NZ  . LYS A 1 196 ? 171.021 146.332 170.092 1.00 79.98  ? 196 LYS A NZ  1 
ATOM 1361 N N   . ILE A 1 197 ? 168.770 146.220 163.173 1.00 75.09  ? 197 ILE A N   1 
ATOM 1362 C CA  . ILE A 1 197 ? 168.798 145.558 161.873 1.00 75.09  ? 197 ILE A CA  1 
ATOM 1363 C C   . ILE A 1 197 ? 170.050 145.957 161.108 1.00 75.09  ? 197 ILE A C   1 
ATOM 1364 O O   . ILE A 1 197 ? 170.652 145.139 160.401 1.00 75.09  ? 197 ILE A O   1 
ATOM 1365 C CB  . ILE A 1 197 ? 167.521 145.883 161.078 1.00 75.09  ? 197 ILE A CB  1 
ATOM 1366 C CG1 . ILE A 1 197 ? 166.312 145.203 161.721 1.00 75.09  ? 197 ILE A CG1 1 
ATOM 1367 C CG2 . ILE A 1 197 ? 167.668 145.434 159.638 1.00 75.09  ? 197 ILE A CG2 1 
ATOM 1368 C CD1 . ILE A 1 197 ? 164.986 145.766 161.273 1.00 75.09  ? 197 ILE A CD1 1 
ATOM 1369 N N   . VAL A 1 198 ? 170.466 147.218 161.234 1.00 81.28  ? 198 VAL A N   1 
ATOM 1370 C CA  . VAL A 1 198 ? 171.683 147.663 160.563 1.00 81.28  ? 198 VAL A CA  1 
ATOM 1371 C C   . VAL A 1 198 ? 172.876 146.858 161.056 1.00 81.28  ? 198 VAL A C   1 
ATOM 1372 O O   . VAL A 1 198 ? 173.704 146.393 160.266 1.00 81.28  ? 198 VAL A O   1 
ATOM 1373 C CB  . VAL A 1 198 ? 171.897 149.170 160.779 1.00 81.28  ? 198 VAL A CB  1 
ATOM 1374 C CG1 . VAL A 1 198 ? 173.226 149.599 160.195 1.00 81.28  ? 198 VAL A CG1 1 
ATOM 1375 C CG2 . VAL A 1 198 ? 170.763 149.959 160.163 1.00 81.28  ? 198 VAL A CG2 1 
ATOM 1376 N N   . ASN A 1 199 ? 172.978 146.676 162.374 1.00 86.74  ? 199 ASN A N   1 
ATOM 1377 C CA  . ASN A 1 199 ? 174.055 145.854 162.913 1.00 86.74  ? 199 ASN A CA  1 
ATOM 1378 C C   . ASN A 1 199 ? 173.993 144.446 162.343 1.00 86.74  ? 199 ASN A C   1 
ATOM 1379 O O   . ASN A 1 199 ? 175.028 143.853 162.019 1.00 86.74  ? 199 ASN A O   1 
ATOM 1380 C CB  . ASN A 1 199 ? 173.977 145.820 164.438 1.00 86.74  ? 199 ASN A CB  1 
ATOM 1381 C CG  . ASN A 1 199 ? 174.234 147.174 165.064 1.00 86.74  ? 199 ASN A CG  1 
ATOM 1382 O OD1 . ASN A 1 199 ? 173.430 147.668 165.855 1.00 86.74  ? 199 ASN A OD1 1 
ATOM 1383 N ND2 . ASN A 1 199 ? 175.358 147.785 164.713 1.00 86.74  ? 199 ASN A ND2 1 
ATOM 1384 N N   . GLY A 1 200 ? 172.787 143.894 162.210 1.00 89.11  ? 200 GLY A N   1 
ATOM 1385 C CA  . GLY A 1 200 ? 172.652 142.592 161.582 1.00 89.11  ? 200 GLY A CA  1 
ATOM 1386 C C   . GLY A 1 200 ? 173.114 142.598 160.139 1.00 89.11  ? 200 GLY A C   1 
ATOM 1387 O O   . GLY A 1 200 ? 173.796 141.674 159.692 1.00 89.11  ? 200 GLY A O   1 
ATOM 1388 N N   . VAL A 1 201 ? 172.752 143.641 159.391 1.00 77.45  ? 201 VAL A N   1 
ATOM 1389 C CA  . VAL A 1 201 ? 173.176 143.731 157.997 1.00 77.45  ? 201 VAL A CA  1 
ATOM 1390 C C   . VAL A 1 201 ? 174.691 143.837 157.910 1.00 77.45  ? 201 VAL A C   1 
ATOM 1391 O O   . VAL A 1 201 ? 175.327 143.186 157.072 1.00 77.45  ? 201 VAL A O   1 
ATOM 1392 C CB  . VAL A 1 201 ? 172.488 144.920 157.304 1.00 77.45  ? 201 VAL A CB  1 
ATOM 1393 C CG1 . VAL A 1 201 ? 173.114 145.172 155.944 1.00 77.45  ? 201 VAL A CG1 1 
ATOM 1394 C CG2 . VAL A 1 201 ? 170.997 144.664 157.174 1.00 77.45  ? 201 VAL A CG2 1 
ATOM 1395 N N   . MET A 1 202 ? 175.296 144.656 158.772 1.00 88.92  ? 202 MET A N   1 
ATOM 1396 C CA  . MET A 1 202 ? 176.744 144.826 158.729 1.00 88.92  ? 202 MET A CA  1 
ATOM 1397 C C   . MET A 1 202 ? 177.467 143.502 158.920 1.00 88.92  ? 202 MET A C   1 
ATOM 1398 O O   . MET A 1 202 ? 178.576 143.324 158.406 1.00 88.92  ? 202 MET A O   1 
ATOM 1399 C CB  . MET A 1 202 ? 177.190 145.825 159.796 1.00 88.92  ? 202 MET A CB  1 
ATOM 1400 C CG  . MET A 1 202 ? 176.777 147.267 159.540 1.00 88.92  ? 202 MET A CG  1 
ATOM 1401 S SD  . MET A 1 202 ? 177.325 147.920 157.953 1.00 88.92  ? 202 MET A SD  1 
ATOM 1402 C CE  . MET A 1 202 ? 175.900 147.571 156.929 1.00 88.92  ? 202 MET A CE  1 
ATOM 1403 N N   . GLN A 1 203 ? 176.867 142.563 159.653 1.00 88.00  ? 203 GLN A N   1 
ATOM 1404 C CA  . GLN A 1 203 ? 177.487 141.251 159.797 1.00 88.00  ? 203 GLN A CA  1 
ATOM 1405 C C   . GLN A 1 203 ? 177.516 140.505 158.471 1.00 88.00  ? 203 GLN A C   1 
ATOM 1406 O O   . GLN A 1 203 ? 178.454 139.743 158.211 1.00 88.00  ? 203 GLN A O   1 
ATOM 1407 C CB  . GLN A 1 203 ? 176.746 140.431 160.850 1.00 88.00  ? 203 GLN A CB  1 
ATOM 1408 C CG  . GLN A 1 203 ? 176.873 140.980 162.257 1.00 88.00  ? 203 GLN A CG  1 
ATOM 1409 C CD  . GLN A 1 203 ? 178.300 140.966 162.760 1.00 88.00  ? 203 GLN A CD  1 
ATOM 1410 O OE1 . GLN A 1 203 ? 179.166 140.311 162.184 1.00 88.00  ? 203 GLN A OE1 1 
ATOM 1411 N NE2 . GLN A 1 203 ? 178.553 141.693 163.841 1.00 88.00  ? 203 GLN A NE2 1 
ATOM 1412 N N   . TYR A 1 204 ? 176.500 140.698 157.631 1.00 82.00  ? 204 TYR A N   1 
ATOM 1413 C CA  . TYR A 1 204 ? 176.493 140.105 156.302 1.00 82.00  ? 204 TYR A CA  1 
ATOM 1414 C C   . TYR A 1 204 ? 177.279 140.930 155.293 1.00 82.00  ? 204 TYR A C   1 
ATOM 1415 O O   . TYR A 1 204 ? 177.605 140.422 154.216 1.00 82.00  ? 204 TYR A O   1 
ATOM 1416 C CB  . TYR A 1 204 ? 175.050 139.936 155.820 1.00 82.00  ? 204 TYR A CB  1 
ATOM 1417 C CG  . TYR A 1 204 ? 174.924 139.600 154.354 1.00 82.00  ? 204 TYR A CG  1 
ATOM 1418 C CD1 . TYR A 1 204 ? 175.195 138.324 153.888 1.00 82.00  ? 204 TYR A CD1 1 
ATOM 1419 C CD2 . TYR A 1 204 ? 174.535 140.562 153.435 1.00 82.00  ? 204 TYR A CD2 1 
ATOM 1420 C CE1 . TYR A 1 204 ? 175.082 138.014 152.550 1.00 82.00  ? 204 TYR A CE1 1 
ATOM 1421 C CE2 . TYR A 1 204 ? 174.419 140.263 152.095 1.00 82.00  ? 204 TYR A CE2 1 
ATOM 1422 C CZ  . TYR A 1 204 ? 174.693 138.988 151.658 1.00 82.00  ? 204 TYR A CZ  1 
ATOM 1423 O OH  . TYR A 1 204 ? 174.578 138.685 150.322 1.00 82.00  ? 204 TYR A OH  1 
ATOM 1424 N N   . ALA A 1 205 ? 177.604 142.178 155.622 1.00 84.47  ? 205 ALA A N   1 
ATOM 1425 C CA  . ALA A 1 205 ? 178.296 143.034 154.665 1.00 84.47  ? 205 ALA A CA  1 
ATOM 1426 C C   . ALA A 1 205 ? 179.608 142.442 154.170 1.00 84.47  ? 205 ALA A C   1 
ATOM 1427 O O   . ALA A 1 205 ? 179.866 142.522 152.957 1.00 84.47  ? 205 ALA A O   1 
ATOM 1428 C CB  . ALA A 1 205 ? 178.527 144.415 155.287 1.00 84.47  ? 205 ALA A CB  1 
ATOM 1429 N N   . PRO A 1 206 ? 180.463 141.856 155.009 1.00 88.45  ? 206 PRO A N   1 
ATOM 1430 C CA  . PRO A 1 206 ? 181.718 141.295 154.481 1.00 88.45  ? 206 PRO A CA  1 
ATOM 1431 C C   . PRO A 1 206 ? 181.497 140.302 153.356 1.00 88.45  ? 206 PRO A C   1 
ATOM 1432 O O   . PRO A 1 206 ? 182.266 140.288 152.388 1.00 88.45  ? 206 PRO A O   1 
ATOM 1433 C CB  . PRO A 1 206 ? 182.350 140.630 155.710 1.00 88.45  ? 206 PRO A CB  1 
ATOM 1434 C CG  . PRO A 1 206 ? 181.747 141.304 156.875 1.00 88.45  ? 206 PRO A CG  1 
ATOM 1435 C CD  . PRO A 1 206 ? 180.383 141.759 156.475 1.00 88.45  ? 206 PRO A CD  1 
ATOM 1436 N N   . ILE A 1 207 ? 180.464 139.468 153.456 1.00 90.40  ? 207 ILE A N   1 
ATOM 1437 C CA  . ILE A 1 207 ? 180.119 138.586 152.347 1.00 90.40  ? 207 ILE A CA  1 
ATOM 1438 C C   . ILE A 1 207 ? 179.573 139.398 151.181 1.00 90.40  ? 207 ILE A C   1 
ATOM 1439 O O   . ILE A 1 207 ? 179.925 139.166 150.020 1.00 90.40  ? 207 ILE A O   1 
ATOM 1440 C CB  . ILE A 1 207 ? 179.115 137.515 152.806 1.00 90.40  ? 207 ILE A CB  1 
ATOM 1441 C CG1 . ILE A 1 207 ? 179.759 136.587 153.836 1.00 90.40  ? 207 ILE A CG1 1 
ATOM 1442 C CG2 . ILE A 1 207 ? 178.615 136.716 151.618 1.00 90.40  ? 207 ILE A CG2 1 
ATOM 1443 C CD1 . ILE A 1 207 ? 178.764 135.931 154.764 1.00 90.40  ? 207 ILE A CD1 1 
ATOM 1444 N N   . GLY A 1 208 ? 178.701 140.362 151.475 1.00 85.50  ? 208 GLY A N   1 
ATOM 1445 C CA  . GLY A 1 208 ? 178.148 141.188 150.415 1.00 85.50  ? 208 GLY A CA  1 
ATOM 1446 C C   . GLY A 1 208 ? 179.199 142.039 149.732 1.00 85.50  ? 208 GLY A C   1 
ATOM 1447 O O   . GLY A 1 208 ? 179.256 142.111 148.502 1.00 85.50  ? 208 GLY A O   1 
ATOM 1448 N N   . VAL A 1 209 ? 180.051 142.693 150.521 1.00 83.18  ? 209 VAL A N   1 
ATOM 1449 C CA  . VAL A 1 209 ? 181.071 143.566 149.947 1.00 83.18  ? 209 VAL A CA  1 
ATOM 1450 C C   . VAL A 1 209 ? 182.006 142.765 149.053 1.00 83.18  ? 209 VAL A C   1 
ATOM 1451 O O   . VAL A 1 209 ? 182.339 143.184 147.939 1.00 83.18  ? 209 VAL A O   1 
ATOM 1452 C CB  . VAL A 1 209 ? 181.846 144.290 151.061 1.00 83.18  ? 209 VAL A CB  1 
ATOM 1453 C CG1 . VAL A 1 209 ? 183.158 144.835 150.526 1.00 83.18  ? 209 VAL A CG1 1 
ATOM 1454 C CG2 . VAL A 1 209 ? 181.002 145.405 151.650 1.00 83.18  ? 209 VAL A CG2 1 
ATOM 1455 N N   . PHE A 1 210 ? 182.444 141.599 149.528 1.00 91.29  ? 210 PHE A N   1 
ATOM 1456 C CA  . PHE A 1 210 ? 183.341 140.768 148.736 1.00 91.29  ? 210 PHE A CA  1 
ATOM 1457 C C   . PHE A 1 210 ? 182.738 140.480 147.369 1.00 91.29  ? 210 PHE A C   1 
ATOM 1458 O O   . PHE A 1 210 ? 183.371 140.701 146.332 1.00 91.29  ? 210 PHE A O   1 
ATOM 1459 C CB  . PHE A 1 210 ? 183.635 139.467 149.482 1.00 91.29  ? 210 PHE A CB  1 
ATOM 1460 C CG  . PHE A 1 210 ? 184.126 138.361 148.596 1.00 91.29  ? 210 PHE A CG  1 
ATOM 1461 C CD1 . PHE A 1 210 ? 185.470 138.243 148.299 1.00 91.29  ? 210 PHE A CD1 1 
ATOM 1462 C CD2 . PHE A 1 210 ? 183.245 137.438 148.064 1.00 91.29  ? 210 PHE A CD2 1 
ATOM 1463 C CE1 . PHE A 1 210 ? 185.926 137.230 147.486 1.00 91.29  ? 210 PHE A CE1 1 
ATOM 1464 C CE2 . PHE A 1 210 ? 183.695 136.422 147.250 1.00 91.29  ? 210 PHE A CE2 1 
ATOM 1465 C CZ  . PHE A 1 210 ? 185.038 136.317 146.961 1.00 91.29  ? 210 PHE A CZ  1 
ATOM 1466 N N   . ALA A 1 211 ? 181.500 139.987 147.351 1.00 92.61  ? 211 ALA A N   1 
ATOM 1467 C CA  . ALA A 1 211 ? 180.831 139.733 146.082 1.00 92.61  ? 211 ALA A CA  1 
ATOM 1468 C C   . ALA A 1 211 ? 180.588 141.029 145.323 1.00 92.61  ? 211 ALA A C   1 
ATOM 1469 O O   . ALA A 1 211 ? 180.741 141.080 144.098 1.00 92.61  ? 211 ALA A O   1 
ATOM 1470 C CB  . ALA A 1 211 ? 179.514 138.999 146.323 1.00 92.61  ? 211 ALA A CB  1 
ATOM 1471 N N   . LEU A 1 212 ? 180.210 142.091 146.036 1.00 88.65  ? 212 LEU A N   1 
ATOM 1472 C CA  . LEU A 1 212 ? 179.881 143.345 145.370 1.00 88.65  ? 212 LEU A CA  1 
ATOM 1473 C C   . LEU A 1 212 ? 181.094 143.957 144.685 1.00 88.65  ? 212 LEU A C   1 
ATOM 1474 O O   . LEU A 1 212 ? 180.947 144.657 143.677 1.00 88.65  ? 212 LEU A O   1 
ATOM 1475 C CB  . LEU A 1 212 ? 179.291 144.329 146.379 1.00 88.65  ? 212 LEU A CB  1 
ATOM 1476 C CG  . LEU A 1 212 ? 178.600 145.573 145.821 1.00 88.65  ? 212 LEU A CG  1 
ATOM 1477 C CD1 . LEU A 1 212 ? 177.561 145.206 144.777 1.00 88.65  ? 212 LEU A CD1 1 
ATOM 1478 C CD2 . LEU A 1 212 ? 177.964 146.359 146.953 1.00 88.65  ? 212 LEU A CD2 1 
ATOM 1479 N N   . ILE A 1 213 ? 182.294 143.711 145.209 1.00 94.67  ? 213 ILE A N   1 
ATOM 1480 C CA  . ILE A 1 213 ? 183.509 144.280 144.637 1.00 94.67  ? 213 ILE A CA  1 
ATOM 1481 C C   . ILE A 1 213 ? 184.156 143.256 143.715 1.00 94.67  ? 213 ILE A C   1 
ATOM 1482 O O   . ILE A 1 213 ? 184.868 143.616 142.772 1.00 94.67  ? 213 ILE A O   1 
ATOM 1483 C CB  . ILE A 1 213 ? 184.489 144.727 145.735 1.00 94.67  ? 213 ILE A CB  1 
ATOM 1484 C CG1 . ILE A 1 213 ? 185.620 145.561 145.135 1.00 94.67  ? 213 ILE A CG1 1 
ATOM 1485 C CG2 . ILE A 1 213 ? 185.075 143.527 146.443 1.00 94.67  ? 213 ILE A CG2 1 
ATOM 1486 C CD1 . ILE A 1 213 ? 185.211 146.968 144.779 1.00 94.67  ? 213 ILE A CD1 1 
ATOM 1487 N N   . ALA A 1 214 ? 183.920 141.971 143.982 1.00 100.20 ? 214 ALA A N   1 
ATOM 1488 C CA  . ALA A 1 214 ? 184.499 140.938 143.133 1.00 100.20 ? 214 ALA A CA  1 
ATOM 1489 C C   . ALA A 1 214 ? 183.994 141.047 141.704 1.00 100.20 ? 214 ALA A C   1 
ATOM 1490 O O   . ALA A 1 214 ? 184.780 140.929 140.758 1.00 100.20 ? 214 ALA A O   1 
ATOM 1491 C CB  . ALA A 1 214 ? 184.186 139.554 143.698 1.00 100.20 ? 214 ALA A CB  1 
ATOM 1492 N N   . TYR A 1 215 ? 182.694 141.278 141.525 1.00 110.07 ? 215 TYR A N   1 
ATOM 1493 C CA  . TYR A 1 215 ? 182.133 141.342 140.181 1.00 110.07 ? 215 TYR A CA  1 
ATOM 1494 C C   . TYR A 1 215 ? 182.694 142.529 139.409 1.00 110.07 ? 215 TYR A C   1 
ATOM 1495 O O   . TYR A 1 215 ? 183.159 142.386 138.273 1.00 110.07 ? 215 TYR A O   1 
ATOM 1496 C CB  . TYR A 1 215 ? 180.609 141.423 140.256 1.00 110.07 ? 215 TYR A CB  1 
ATOM 1497 C CG  . TYR A 1 215 ? 179.986 142.153 139.091 1.00 110.07 ? 215 TYR A CG  1 
ATOM 1498 C CD1 . TYR A 1 215 ? 179.852 141.541 137.854 1.00 110.07 ? 215 TYR A CD1 1 
ATOM 1499 C CD2 . TYR A 1 215 ? 179.533 143.457 139.229 1.00 110.07 ? 215 TYR A CD2 1 
ATOM 1500 C CE1 . TYR A 1 215 ? 179.283 142.205 136.788 1.00 110.07 ? 215 TYR A CE1 1 
ATOM 1501 C CE2 . TYR A 1 215 ? 178.963 144.130 138.169 1.00 110.07 ? 215 TYR A CE2 1 
ATOM 1502 C CZ  . TYR A 1 215 ? 178.840 143.500 136.951 1.00 110.07 ? 215 TYR A CZ  1 
ATOM 1503 O OH  . TYR A 1 215 ? 178.272 144.169 135.892 1.00 110.07 ? 215 TYR A OH  1 
ATOM 1504 N N   . VAL A 1 216 ? 182.663 143.717 140.014 1.00 102.91 ? 216 VAL A N   1 
ATOM 1505 C CA  . VAL A 1 216 ? 183.125 144.910 139.311 1.00 102.91 ? 216 VAL A CA  1 
ATOM 1506 C C   . VAL A 1 216 ? 184.597 144.770 138.947 1.00 102.91 ? 216 VAL A C   1 
ATOM 1507 O O   . VAL A 1 216 ? 185.003 145.052 137.814 1.00 102.91 ? 216 VAL A O   1 
ATOM 1508 C CB  . VAL A 1 216 ? 182.864 146.172 140.154 1.00 102.91 ? 216 VAL A CB  1 
ATOM 1509 C CG1 . VAL A 1 216 ? 183.638 146.126 141.459 1.00 102.91 ? 216 VAL A CG1 1 
ATOM 1510 C CG2 . VAL A 1 216 ? 183.219 147.420 139.363 1.00 102.91 ? 216 VAL A CG2 1 
ATOM 1511 N N   . MET A 1 217 ? 185.415 144.310 139.892 1.00 114.99 ? 217 MET A N   1 
ATOM 1512 C CA  . MET A 1 217 ? 186.834 144.136 139.617 1.00 114.99 ? 217 MET A CA  1 
ATOM 1513 C C   . MET A 1 217 ? 187.102 142.999 138.645 1.00 114.99 ? 217 MET A C   1 
ATOM 1514 O O   . MET A 1 217 ? 188.240 142.856 138.187 1.00 114.99 ? 217 MET A O   1 
ATOM 1515 C CB  . MET A 1 217 ? 187.598 143.887 140.919 1.00 114.99 ? 217 MET A CB  1 
ATOM 1516 C CG  . MET A 1 217 ? 187.872 145.131 141.765 1.00 114.99 ? 217 MET A CG  1 
ATOM 1517 S SD  . MET A 1 217 ? 188.471 146.574 140.859 1.00 114.99 ? 217 MET A SD  1 
ATOM 1518 C CE  . MET A 1 217 ? 186.933 147.402 140.453 1.00 114.99 ? 217 MET A CE  1 
ATOM 1519 N N   . ALA A 1 218 ? 186.094 142.188 138.325 1.00 117.91 ? 218 ALA A N   1 
ATOM 1520 C CA  . ALA A 1 218 ? 186.281 141.124 137.346 1.00 117.91 ? 218 ALA A CA  1 
ATOM 1521 C C   . ALA A 1 218 ? 186.213 141.667 135.925 1.00 117.91 ? 218 ALA A C   1 
ATOM 1522 O O   . ALA A 1 218 ? 187.091 141.392 135.101 1.00 117.91 ? 218 ALA A O   1 
ATOM 1523 C CB  . ALA A 1 218 ? 185.235 140.030 137.555 1.00 117.91 ? 218 ALA A CB  1 
ATOM 1524 N N   . GLU A 1 219 ? 185.173 142.441 135.620 1.00 117.61 ? 219 GLU A N   1 
ATOM 1525 C CA  . GLU A 1 219 ? 185.017 142.983 134.277 1.00 117.61 ? 219 GLU A CA  1 
ATOM 1526 C C   . GLU A 1 219 ? 185.585 144.392 134.135 1.00 117.61 ? 219 GLU A C   1 
ATOM 1527 O O   . GLU A 1 219 ? 185.590 144.925 133.020 1.00 117.61 ? 219 GLU A O   1 
ATOM 1528 C CB  . GLU A 1 219 ? 183.532 142.856 133.868 1.00 117.61 ? 219 GLU A CB  1 
ATOM 1529 C CG  . GLU A 1 219 ? 182.461 143.759 134.515 1.00 117.61 ? 219 GLU A CG  1 
ATOM 1530 C CD  . GLU A 1 219 ? 182.603 145.248 134.278 1.00 117.61 ? 219 GLU A CD  1 
ATOM 1531 O OE1 . GLU A 1 219 ? 181.855 146.006 134.928 1.00 117.61 ? 219 GLU A OE1 1 
ATOM 1532 O OE2 . GLU A 1 219 ? 183.381 145.671 133.405 1.00 117.61 ? 219 GLU A OE2 1 
ATOM 1533 N N   . GLN A 1 220 ? 186.116 144.982 135.208 1.00 113.71 ? 220 GLN A N   1 
ATOM 1534 C CA  . GLN A 1 220 ? 187.032 146.111 135.098 1.00 113.71 ? 220 GLN A CA  1 
ATOM 1535 C C   . GLN A 1 220 ? 188.490 145.676 135.128 1.00 113.71 ? 220 GLN A C   1 
ATOM 1536 O O   . GLN A 1 220 ? 189.380 146.532 135.132 1.00 113.71 ? 220 GLN A O   1 
ATOM 1537 C CB  . GLN A 1 220 ? 186.795 147.136 136.211 1.00 113.71 ? 220 GLN A CB  1 
ATOM 1538 C CG  . GLN A 1 220 ? 185.925 148.308 135.802 1.00 113.71 ? 220 GLN A CG  1 
ATOM 1539 C CD  . GLN A 1 220 ? 184.607 147.873 135.223 1.00 113.71 ? 220 GLN A CD  1 
ATOM 1540 O OE1 . GLN A 1 220 ? 183.909 147.055 135.813 1.00 113.71 ? 220 GLN A OE1 1 
ATOM 1541 N NE2 . GLN A 1 220 ? 184.261 148.404 134.057 1.00 113.71 ? 220 GLN A NE2 1 
ATOM 1542 N N   . GLY A 1 221 ? 188.758 144.371 135.148 1.00 135.10 ? 221 GLY A N   1 
ATOM 1543 C CA  . GLY A 1 221 ? 190.131 143.905 135.108 1.00 135.10 ? 221 GLY A CA  1 
ATOM 1544 C C   . GLY A 1 221 ? 190.905 144.383 133.900 1.00 135.10 ? 221 GLY A C   1 
ATOM 1545 O O   . GLY A 1 221 ? 192.139 144.427 133.953 1.00 135.10 ? 221 GLY A O   1 
ATOM 1546 N N   . VAL A 1 222 ? 190.211 144.738 132.822 1.00 147.42 ? 222 VAL A N   1 
ATOM 1547 C CA  . VAL A 1 222 ? 190.810 145.385 131.667 1.00 147.42 ? 222 VAL A CA  1 
ATOM 1548 C C   . VAL A 1 222 ? 190.383 146.847 131.688 1.00 147.42 ? 222 VAL A C   1 
ATOM 1549 O O   . VAL A 1 222 ? 189.418 147.227 132.355 1.00 147.42 ? 222 VAL A O   1 
ATOM 1550 C CB  . VAL A 1 222 ? 190.402 144.707 130.343 1.00 147.42 ? 222 VAL A CB  1 
ATOM 1551 C CG1 . VAL A 1 222 ? 188.931 144.964 130.040 1.00 147.42 ? 222 VAL A CG1 1 
ATOM 1552 C CG2 . VAL A 1 222 ? 191.286 145.180 129.198 1.00 147.42 ? 222 VAL A CG2 1 
ATOM 1553 N N   . HIS A 1 223 ? 191.122 147.673 130.950 1.00 141.85 ? 223 HIS A N   1 
ATOM 1554 C CA  . HIS A 1 223 ? 190.899 149.114 130.903 1.00 141.85 ? 223 HIS A CA  1 
ATOM 1555 C C   . HIS A 1 223 ? 191.313 149.803 132.196 1.00 141.85 ? 223 HIS A C   1 
ATOM 1556 O O   . HIS A 1 223 ? 190.823 150.893 132.505 1.00 141.85 ? 223 HIS A O   1 
ATOM 1557 C CB  . HIS A 1 223 ? 189.431 149.435 130.593 1.00 141.85 ? 223 HIS A CB  1 
ATOM 1558 C CG  . HIS A 1 223 ? 189.245 150.620 129.698 1.00 141.85 ? 223 HIS A CG  1 
ATOM 1559 N ND1 . HIS A 1 223 ? 189.907 150.756 128.497 1.00 141.85 ? 223 HIS A ND1 1 
ATOM 1560 C CD2 . HIS A 1 223 ? 188.470 151.722 129.827 1.00 141.85 ? 223 HIS A CD2 1 
ATOM 1561 C CE1 . HIS A 1 223 ? 189.548 151.891 127.924 1.00 141.85 ? 223 HIS A CE1 1 
ATOM 1562 N NE2 . HIS A 1 223 ? 188.677 152.497 128.712 1.00 141.85 ? 223 HIS A NE2 1 
ATOM 1563 N N   . VAL A 1 224 ? 192.215 149.183 132.962 1.00 140.14 ? 224 VAL A N   1 
ATOM 1564 C CA  . VAL A 1 224 ? 192.622 149.746 134.246 1.00 140.14 ? 224 VAL A CA  1 
ATOM 1565 C C   . VAL A 1 224 ? 193.285 151.103 134.059 1.00 140.14 ? 224 VAL A C   1 
ATOM 1566 O O   . VAL A 1 224 ? 193.290 151.931 134.978 1.00 140.14 ? 224 VAL A O   1 
ATOM 1567 C CB  . VAL A 1 224 ? 193.554 148.763 134.983 1.00 140.14 ? 224 VAL A CB  1 
ATOM 1568 C CG1 . VAL A 1 224 ? 193.990 149.342 136.320 1.00 140.14 ? 224 VAL A CG1 1 
ATOM 1569 C CG2 . VAL A 1 224 ? 192.863 147.421 135.179 1.00 140.14 ? 224 VAL A CG2 1 
ATOM 1570 N N   . VAL A 1 225 ? 193.858 151.354 132.883 1.00 140.05 ? 225 VAL A N   1 
ATOM 1571 C CA  . VAL A 1 225 ? 194.511 152.621 132.579 1.00 140.05 ? 225 VAL A CA  1 
ATOM 1572 C C   . VAL A 1 225 ? 193.846 153.316 131.391 1.00 140.05 ? 225 VAL A C   1 
ATOM 1573 O O   . VAL A 1 225 ? 194.487 154.083 130.682 1.00 140.05 ? 225 VAL A O   1 
ATOM 1574 C CB  . VAL A 1 225 ? 196.019 152.424 132.330 1.00 140.05 ? 225 VAL A CB  1 
ATOM 1575 C CG1 . VAL A 1 225 ? 196.713 151.975 133.609 1.00 140.05 ? 225 VAL A CG1 1 
ATOM 1576 C CG2 . VAL A 1 225 ? 196.259 151.432 131.196 1.00 140.05 ? 225 VAL A CG2 1 
ATOM 1577 N N   . GLY A 1 226 ? 192.562 153.052 131.169 1.00 136.26 ? 226 GLY A N   1 
ATOM 1578 C CA  . GLY A 1 226 ? 191.823 153.686 130.100 1.00 136.26 ? 226 GLY A CA  1 
ATOM 1579 C C   . GLY A 1 226 ? 191.245 155.022 130.526 1.00 136.26 ? 226 GLY A C   1 
ATOM 1580 O O   . GLY A 1 226 ? 191.642 155.625 131.524 1.00 136.26 ? 226 GLY A O   1 
ATOM 1581 N N   . GLU A 1 227 ? 190.277 155.490 129.736 1.00 122.85 ? 227 GLU A N   1 
ATOM 1582 C CA  . GLU A 1 227 ? 189.610 156.745 130.066 1.00 122.85 ? 227 GLU A CA  1 
ATOM 1583 C C   . GLU A 1 227 ? 188.880 156.640 131.398 1.00 122.85 ? 227 GLU A C   1 
ATOM 1584 O O   . GLU A 1 227 ? 188.909 157.575 132.206 1.00 122.85 ? 227 GLU A O   1 
ATOM 1585 C CB  . GLU A 1 227 ? 188.643 157.138 128.951 1.00 122.85 ? 227 GLU A CB  1 
ATOM 1586 C CG  . GLU A 1 227 ? 189.269 158.018 127.879 1.00 122.85 ? 227 GLU A CG  1 
ATOM 1587 C CD  . GLU A 1 227 ? 188.318 158.317 126.736 1.00 122.85 ? 227 GLU A CD  1 
ATOM 1588 O OE1 . GLU A 1 227 ? 188.170 159.505 126.378 1.00 122.85 ? 227 GLU A OE1 1 
ATOM 1589 O OE2 . GLU A 1 227 ? 187.718 157.364 126.193 1.00 122.85 ? 227 GLU A OE2 1 
ATOM 1590 N N   . LEU A 1 228 ? 188.223 155.504 131.648 1.00 117.23 ? 228 LEU A N   1 
ATOM 1591 C CA  . LEU A 1 228 ? 187.547 155.312 132.926 1.00 117.23 ? 228 LEU A CA  1 
ATOM 1592 C C   . LEU A 1 228 ? 188.517 155.476 134.088 1.00 117.23 ? 228 LEU A C   1 
ATOM 1593 O O   . LEU A 1 228 ? 188.134 155.943 135.166 1.00 117.23 ? 228 LEU A O   1 
ATOM 1594 C CB  . LEU A 1 228 ? 186.893 153.931 132.973 1.00 117.23 ? 228 LEU A CB  1 
ATOM 1595 C CG  . LEU A 1 228 ? 185.715 153.709 132.024 1.00 117.23 ? 228 LEU A CG  1 
ATOM 1596 C CD1 . LEU A 1 228 ? 185.180 152.296 132.171 1.00 117.23 ? 228 LEU A CD1 1 
ATOM 1597 C CD2 . LEU A 1 228 ? 184.616 154.722 132.278 1.00 117.23 ? 228 LEU A CD2 1 
ATOM 1598 N N   . ALA A 1 229 ? 189.781 155.100 133.887 1.00 119.24 ? 229 ALA A N   1 
ATOM 1599 C CA  . ALA A 1 229 ? 190.772 155.286 134.940 1.00 119.24 ? 229 ALA A CA  1 
ATOM 1600 C C   . ALA A 1 229 ? 190.913 156.758 135.298 1.00 119.24 ? 229 ALA A C   1 
ATOM 1601 O O   . ALA A 1 229 ? 190.977 157.115 136.479 1.00 119.24 ? 229 ALA A O   1 
ATOM 1602 C CB  . ALA A 1 229 ? 192.116 154.709 134.503 1.00 119.24 ? 229 ALA A CB  1 
ATOM 1603 N N   . LYS A 1 230 ? 190.956 157.630 134.289 1.00 108.79 ? 230 LYS A N   1 
ATOM 1604 C CA  . LYS A 1 230 ? 190.995 159.060 134.564 1.00 108.79 ? 230 LYS A CA  1 
ATOM 1605 C C   . LYS A 1 230 ? 189.699 159.537 135.203 1.00 108.79 ? 230 LYS A C   1 
ATOM 1606 O O   . LYS A 1 230 ? 189.718 160.461 136.023 1.00 108.79 ? 230 LYS A O   1 
ATOM 1607 C CB  . LYS A 1 230 ? 191.277 159.837 133.279 1.00 108.79 ? 230 LYS A CB  1 
ATOM 1608 C CG  . LYS A 1 230 ? 192.730 159.778 132.842 1.00 108.79 ? 230 LYS A CG  1 
ATOM 1609 C CD  . LYS A 1 230 ? 193.012 160.729 131.693 1.00 108.79 ? 230 LYS A CD  1 
ATOM 1610 C CE  . LYS A 1 230 ? 194.473 160.673 131.276 1.00 108.79 ? 230 LYS A CE  1 
ATOM 1611 N NZ  . LYS A 1 230 ? 195.376 161.229 132.322 1.00 108.79 ? 230 LYS A NZ  1 
ATOM 1612 N N   . VAL A 1 231 ? 188.569 158.924 134.847 1.00 104.14 ? 231 VAL A N   1 
ATOM 1613 C CA  . VAL A 1 231 ? 187.312 159.260 135.508 1.00 104.14 ? 231 VAL A CA  1 
ATOM 1614 C C   . VAL A 1 231 ? 187.397 158.935 136.992 1.00 104.14 ? 231 VAL A C   1 
ATOM 1615 O O   . VAL A 1 231 ? 186.984 159.732 137.843 1.00 104.14 ? 231 VAL A O   1 
ATOM 1616 C CB  . VAL A 1 231 ? 186.138 158.526 134.835 1.00 104.14 ? 231 VAL A CB  1 
ATOM 1617 C CG1 . VAL A 1 231 ? 184.840 158.822 135.564 1.00 104.14 ? 231 VAL A CG1 1 
ATOM 1618 C CG2 . VAL A 1 231 ? 186.030 158.929 133.376 1.00 104.14 ? 231 VAL A CG2 1 
ATOM 1619 N N   . THR A 1 232 ? 187.931 157.760 137.328 1.00 107.78 ? 232 THR A N   1 
ATOM 1620 C CA  . THR A 1 232 ? 188.143 157.422 138.730 1.00 107.78 ? 232 THR A CA  1 
ATOM 1621 C C   . THR A 1 232 ? 189.133 158.383 139.373 1.00 107.78 ? 232 THR A C   1 
ATOM 1622 O O   . THR A 1 232 ? 188.930 158.842 140.503 1.00 107.78 ? 232 THR A O   1 
ATOM 1623 C CB  . THR A 1 232 ? 188.643 155.985 138.854 1.00 107.78 ? 232 THR A CB  1 
ATOM 1624 O OG1 . THR A 1 232 ? 189.842 155.829 138.087 1.00 107.78 ? 232 THR A OG1 1 
ATOM 1625 C CG2 . THR A 1 232 ? 187.597 155.013 138.353 1.00 107.78 ? 232 THR A CG2 1 
ATOM 1626 N N   . ALA A 1 233 ? 190.218 158.699 138.664 1.00 109.13 ? 233 ALA A N   1 
ATOM 1627 C CA  . ALA A 1 233 ? 191.202 159.629 139.205 1.00 109.13 ? 233 ALA A CA  1 
ATOM 1628 C C   . ALA A 1 233 ? 190.586 160.999 139.445 1.00 109.13 ? 233 ALA A C   1 
ATOM 1629 O O   . ALA A 1 233 ? 190.821 161.621 140.488 1.00 109.13 ? 233 ALA A O   1 
ATOM 1630 C CB  . ALA A 1 233 ? 192.395 159.738 138.257 1.00 109.13 ? 233 ALA A CB  1 
ATOM 1631 N N   . ALA A 1 234 ? 189.786 161.485 138.496 1.00 108.28 ? 234 ALA A N   1 
ATOM 1632 C CA  . ALA A 1 234 ? 189.171 162.797 138.656 1.00 108.28 ? 234 ALA A CA  1 
ATOM 1633 C C   . ALA A 1 234 ? 188.263 162.830 139.876 1.00 108.28 ? 234 ALA A C   1 
ATOM 1634 O O   . ALA A 1 234 ? 188.273 163.801 140.640 1.00 108.28 ? 234 ALA A O   1 
ATOM 1635 C CB  . ALA A 1 234 ? 188.390 163.167 137.398 1.00 108.28 ? 234 ALA A CB  1 
ATOM 1636 N N   . VAL A 1 235 ? 187.473 161.777 140.079 1.00 97.86  ? 235 VAL A N   1 
ATOM 1637 C CA  . VAL A 1 235 ? 186.571 161.738 141.225 1.00 97.86  ? 235 VAL A CA  1 
ATOM 1638 C C   . VAL A 1 235 ? 187.362 161.552 142.513 1.00 97.86  ? 235 VAL A C   1 
ATOM 1639 O O   . VAL A 1 235 ? 187.289 162.374 143.432 1.00 97.86  ? 235 VAL A O   1 
ATOM 1640 C CB  . VAL A 1 235 ? 185.525 160.625 141.052 1.00 97.86  ? 235 VAL A CB  1 
ATOM 1641 C CG1 . VAL A 1 235 ? 184.725 160.450 142.329 1.00 97.86  ? 235 VAL A CG1 1 
ATOM 1642 C CG2 . VAL A 1 235 ? 184.608 160.936 139.890 1.00 97.86  ? 235 VAL A CG2 1 
ATOM 1643 N N   . TYR A 1 236 ? 188.143 160.473 142.590 1.00 100.88 ? 236 TYR A N   1 
ATOM 1644 C CA  . TYR A 1 236 ? 188.790 160.123 143.849 1.00 100.88 ? 236 TYR A CA  1 
ATOM 1645 C C   . TYR A 1 236 ? 189.705 161.240 144.328 1.00 100.88 ? 236 TYR A C   1 
ATOM 1646 O O   . TYR A 1 236 ? 189.657 161.638 145.498 1.00 100.88 ? 236 TYR A O   1 
ATOM 1647 C CB  . TYR A 1 236 ? 189.563 158.817 143.694 1.00 100.88 ? 236 TYR A CB  1 
ATOM 1648 C CG  . TYR A 1 236 ? 188.753 157.614 144.099 1.00 100.88 ? 236 TYR A CG  1 
ATOM 1649 C CD1 . TYR A 1 236 ? 187.865 157.024 143.215 1.00 100.88 ? 236 TYR A CD1 1 
ATOM 1650 C CD2 . TYR A 1 236 ? 188.861 157.081 145.372 1.00 100.88 ? 236 TYR A CD2 1 
ATOM 1651 C CE1 . TYR A 1 236 ? 187.117 155.928 143.584 1.00 100.88 ? 236 TYR A CE1 1 
ATOM 1652 C CE2 . TYR A 1 236 ? 188.118 155.986 145.750 1.00 100.88 ? 236 TYR A CE2 1 
ATOM 1653 C CZ  . TYR A 1 236 ? 187.247 155.414 144.853 1.00 100.88 ? 236 TYR A CZ  1 
ATOM 1654 O OH  . TYR A 1 236 ? 186.504 154.320 145.227 1.00 100.88 ? 236 TYR A OH  1 
ATOM 1655 N N   . VAL A 1 237 ? 190.543 161.771 143.438 1.00 103.67 ? 237 VAL A N   1 
ATOM 1656 C CA  . VAL A 1 237 ? 191.348 162.925 143.819 1.00 103.67 ? 237 VAL A CA  1 
ATOM 1657 C C   . VAL A 1 237 ? 190.439 164.105 144.121 1.00 103.67 ? 237 VAL A C   1 
ATOM 1658 O O   . VAL A 1 237 ? 190.744 164.930 144.989 1.00 103.67 ? 237 VAL A O   1 
ATOM 1659 C CB  . VAL A 1 237 ? 192.378 163.260 142.725 1.00 103.67 ? 237 VAL A CB  1 
ATOM 1660 C CG1 . VAL A 1 237 ? 193.290 164.387 143.185 1.00 103.67 ? 237 VAL A CG1 1 
ATOM 1661 C CG2 . VAL A 1 237 ? 193.202 162.030 142.380 1.00 103.67 ? 237 VAL A CG2 1 
ATOM 1662 N N   . GLY A 1 238 ? 189.311 164.206 143.417 1.00 98.50  ? 238 GLY A N   1 
ATOM 1663 C CA  . GLY A 1 238 ? 188.319 165.203 143.777 1.00 98.50  ? 238 GLY A CA  1 
ATOM 1664 C C   . GLY A 1 238 ? 187.808 165.019 145.192 1.00 98.50  ? 238 GLY A C   1 
ATOM 1665 O O   . GLY A 1 238 ? 187.608 165.993 145.922 1.00 98.50  ? 238 GLY A O   1 
ATOM 1666 N N   . LEU A 1 239 ? 187.592 163.767 145.602 1.00 99.54  ? 239 LEU A N   1 
ATOM 1667 C CA  . LEU A 1 239 ? 187.188 163.509 146.979 1.00 99.54  ? 239 LEU A CA  1 
ATOM 1668 C C   . LEU A 1 239 ? 188.252 163.987 147.955 1.00 99.54  ? 239 LEU A C   1 
ATOM 1669 O O   . LEU A 1 239 ? 187.935 164.604 148.979 1.00 99.54  ? 239 LEU A O   1 
ATOM 1670 C CB  . LEU A 1 239 ? 186.918 162.018 147.185 1.00 99.54  ? 239 LEU A CB  1 
ATOM 1671 C CG  . LEU A 1 239 ? 185.958 161.329 146.215 1.00 99.54  ? 239 LEU A CG  1 
ATOM 1672 C CD1 . LEU A 1 239 ? 186.003 159.824 146.420 1.00 99.54  ? 239 LEU A CD1 1 
ATOM 1673 C CD2 . LEU A 1 239 ? 184.544 161.844 146.387 1.00 99.54  ? 239 LEU A CD2 1 
ATOM 1674 N N   . THR A 1 240 ? 189.523 163.715 147.656 1.00 104.26 ? 240 THR A N   1 
ATOM 1675 C CA  . THR A 1 240 ? 190.596 164.147 148.543 1.00 104.26 ? 240 THR A CA  1 
ATOM 1676 C C   . THR A 1 240 ? 190.588 165.661 148.706 1.00 104.26 ? 240 THR A C   1 
ATOM 1677 O O   . THR A 1 240 ? 190.659 166.177 149.827 1.00 104.26 ? 240 THR A O   1 
ATOM 1678 C CB  . THR A 1 240 ? 191.943 163.669 148.005 1.00 104.26 ? 240 THR A CB  1 
ATOM 1679 O OG1 . THR A 1 240 ? 191.996 162.239 148.052 1.00 104.26 ? 240 THR A OG1 1 
ATOM 1680 C CG2 . THR A 1 240 ? 193.084 164.246 148.828 1.00 104.26 ? 240 THR A CG2 1 
ATOM 1681 N N   . LEU A 1 241 ? 190.488 166.392 147.596 1.00 101.77 ? 241 LEU A N   1 
ATOM 1682 C CA  . LEU A 1 241 ? 190.378 167.842 147.693 1.00 101.77 ? 241 LEU A CA  1 
ATOM 1683 C C   . LEU A 1 241 ? 189.123 168.238 148.455 1.00 101.77 ? 241 LEU A C   1 
ATOM 1684 O O   . LEU A 1 241 ? 189.158 169.139 149.300 1.00 101.77 ? 241 LEU A O   1 
ATOM 1685 C CB  . LEU A 1 241 ? 190.379 168.470 146.300 1.00 101.77 ? 241 LEU A CB  1 
ATOM 1686 C CG  . LEU A 1 241 ? 191.570 168.144 145.399 1.00 101.77 ? 241 LEU A CG  1 
ATOM 1687 C CD1 . LEU A 1 241 ? 191.628 169.121 144.238 1.00 101.77 ? 241 LEU A CD1 1 
ATOM 1688 C CD2 . LEU A 1 241 ? 192.874 168.159 146.181 1.00 101.77 ? 241 LEU A CD2 1 
ATOM 1689 N N   . GLN A 1 242 ? 188.004 167.567 148.178 1.00 97.86  ? 242 GLN A N   1 
ATOM 1690 C CA  . GLN A 1 242 ? 186.776 167.852 148.909 1.00 97.86  ? 242 GLN A CA  1 
ATOM 1691 C C   . GLN A 1 242 ? 187.012 167.757 150.410 1.00 97.86  ? 242 GLN A C   1 
ATOM 1692 O O   . GLN A 1 242 ? 186.607 168.639 151.173 1.00 97.86  ? 242 GLN A O   1 
ATOM 1693 C CB  . GLN A 1 242 ? 185.674 166.887 148.471 1.00 97.86  ? 242 GLN A CB  1 
ATOM 1694 C CG  . GLN A 1 242 ? 184.391 166.984 149.278 1.00 97.86  ? 242 GLN A CG  1 
ATOM 1695 C CD  . GLN A 1 242 ? 183.743 168.345 149.180 1.00 97.86  ? 242 GLN A CD  1 
ATOM 1696 O OE1 . GLN A 1 242 ? 184.129 169.170 148.355 1.00 97.86  ? 242 GLN A OE1 1 
ATOM 1697 N NE2 . GLN A 1 242 ? 182.748 168.587 150.022 1.00 97.86  ? 242 GLN A NE2 1 
ATOM 1698 N N   . ILE A 1 243 ? 187.675 166.689 150.851 1.00 97.86  ? 243 ILE A N   1 
ATOM 1699 C CA  . ILE A 1 243 ? 187.964 166.534 152.272 1.00 97.86  ? 243 ILE A CA  1 
ATOM 1700 C C   . ILE A 1 243 ? 188.984 167.571 152.725 1.00 97.86  ? 243 ILE A C   1 
ATOM 1701 O O   . ILE A 1 243 ? 188.789 168.259 153.733 1.00 97.86  ? 243 ILE A O   1 
ATOM 1702 C CB  . ILE A 1 243 ? 188.447 165.103 152.565 1.00 97.86  ? 243 ILE A CB  1 
ATOM 1703 C CG1 . ILE A 1 243 ? 187.340 164.097 152.246 1.00 97.86  ? 243 ILE A CG1 1 
ATOM 1704 C CG2 . ILE A 1 243 ? 188.884 164.978 154.016 1.00 97.86  ? 243 ILE A CG2 1 
ATOM 1705 C CD1 . ILE A 1 243 ? 187.795 162.656 152.273 1.00 97.86  ? 243 ILE A CD1 1 
ATOM 1706 N N   . LEU A 1 244 ? 190.087 167.703 151.985 1.00 97.86  ? 244 LEU A N   1 
ATOM 1707 C CA  . LEU A 1 244 ? 191.175 168.568 152.432 1.00 97.86  ? 244 LEU A CA  1 
ATOM 1708 C C   . LEU A 1 244 ? 190.819 170.041 152.279 1.00 97.86  ? 244 LEU A C   1 
ATOM 1709 O O   . LEU A 1 244 ? 191.057 170.843 153.189 1.00 97.86  ? 244 LEU A O   1 
ATOM 1710 C CB  . LEU A 1 244 ? 192.451 168.246 151.654 1.00 97.86  ? 244 LEU A CB  1 
ATOM 1711 C CG  . LEU A 1 244 ? 193.054 166.847 151.813 1.00 97.86  ? 244 LEU A CG  1 
ATOM 1712 C CD1 . LEU A 1 244 ? 194.528 166.872 151.442 1.00 97.86  ? 244 LEU A CD1 1 
ATOM 1713 C CD2 . LEU A 1 244 ? 192.876 166.308 153.222 1.00 97.86  ? 244 LEU A CD2 1 
ATOM 1714 N N   . LEU A 1 245 ? 190.251 170.420 151.139 1.00 101.19 ? 245 LEU A N   1 
ATOM 1715 C CA  . LEU A 1 245 ? 190.048 171.825 150.816 1.00 101.19 ? 245 LEU A CA  1 
ATOM 1716 C C   . LEU A 1 245 ? 188.681 172.354 151.230 1.00 101.19 ? 245 LEU A C   1 
ATOM 1717 O O   . LEU A 1 245 ? 188.423 173.549 151.053 1.00 101.19 ? 245 LEU A O   1 
ATOM 1718 C CB  . LEU A 1 245 ? 190.244 172.056 149.313 1.00 101.19 ? 245 LEU A CB  1 
ATOM 1719 C CG  . LEU A 1 245 ? 191.689 172.203 148.833 1.00 101.19 ? 245 LEU A CG  1 
ATOM 1720 C CD1 . LEU A 1 245 ? 192.299 173.499 149.344 1.00 101.19 ? 245 LEU A CD1 1 
ATOM 1721 C CD2 . LEU A 1 245 ? 192.528 171.013 149.263 1.00 101.19 ? 245 LEU A CD2 1 
ATOM 1722 N N   . VAL A 1 246 ? 187.799 171.511 151.763 1.00 97.86  ? 246 VAL A N   1 
ATOM 1723 C CA  . VAL A 1 246 ? 186.489 171.975 152.206 1.00 97.86  ? 246 VAL A CA  1 
ATOM 1724 C C   . VAL A 1 246 ? 186.270 171.597 153.663 1.00 97.86  ? 246 VAL A C   1 
ATOM 1725 O O   . VAL A 1 246 ? 186.085 172.467 154.520 1.00 97.86  ? 246 VAL A O   1 
ATOM 1726 C CB  . VAL A 1 246 ? 185.367 171.409 151.319 1.00 97.86  ? 246 VAL A CB  1 
ATOM 1727 C CG1 . VAL A 1 246 ? 184.072 172.162 151.565 1.00 97.86  ? 246 VAL A CG1 1 
ATOM 1728 C CG2 . VAL A 1 246 ? 185.762 171.487 149.855 1.00 97.86  ? 246 VAL A CG2 1 
ATOM 1729 N N   . TYR A 1 247 ? 186.284 170.297 153.956 1.00 97.86  ? 247 TYR A N   1 
ATOM 1730 C CA  . TYR A 1 247 ? 186.006 169.853 155.317 1.00 97.86  ? 247 TYR A CA  1 
ATOM 1731 C C   . TYR A 1 247 ? 187.079 170.336 156.284 1.00 97.86  ? 247 TYR A C   1 
ATOM 1732 O O   . TYR A 1 247 ? 186.771 170.961 157.305 1.00 97.86  ? 247 TYR A O   1 
ATOM 1733 C CB  . TYR A 1 247 ? 185.891 168.330 155.359 1.00 97.86  ? 247 TYR A CB  1 
ATOM 1734 C CG  . TYR A 1 247 ? 184.780 167.768 154.500 1.00 97.86  ? 247 TYR A CG  1 
ATOM 1735 C CD1 . TYR A 1 247 ? 183.759 168.579 154.025 1.00 97.86  ? 247 TYR A CD1 1 
ATOM 1736 C CD2 . TYR A 1 247 ? 184.749 166.422 154.171 1.00 97.86  ? 247 TYR A CD2 1 
ATOM 1737 C CE1 . TYR A 1 247 ? 182.748 168.067 153.244 1.00 97.86  ? 247 TYR A CE1 1 
ATOM 1738 C CE2 . TYR A 1 247 ? 183.740 165.903 153.390 1.00 97.86  ? 247 TYR A CE2 1 
ATOM 1739 C CZ  . TYR A 1 247 ? 182.743 166.730 152.930 1.00 97.86  ? 247 TYR A CZ  1 
ATOM 1740 O OH  . TYR A 1 247 ? 181.733 166.219 152.152 1.00 97.86  ? 247 TYR A OH  1 
ATOM 1741 N N   . PHE A 1 248 ? 188.348 170.069 155.975 1.00 98.02  ? 248 PHE A N   1 
ATOM 1742 C CA  . PHE A 1 248 ? 189.410 170.416 156.913 1.00 98.02  ? 248 PHE A CA  1 
ATOM 1743 C C   . PHE A 1 248 ? 189.495 171.922 157.114 1.00 98.02  ? 248 PHE A C   1 
ATOM 1744 O O   . PHE A 1 248 ? 189.646 172.396 158.246 1.00 98.02  ? 248 PHE A O   1 
ATOM 1745 C CB  . PHE A 1 248 ? 190.750 169.867 156.425 1.00 98.02  ? 248 PHE A CB  1 
ATOM 1746 C CG  . PHE A 1 248 ? 190.920 168.386 156.635 1.00 98.02  ? 248 PHE A CG  1 
ATOM 1747 C CD1 . PHE A 1 248 ? 192.090 167.761 156.249 1.00 98.02  ? 248 PHE A CD1 1 
ATOM 1748 C CD2 . PHE A 1 248 ? 189.907 167.614 157.182 1.00 98.02  ? 248 PHE A CD2 1 
ATOM 1749 C CE1 . PHE A 1 248 ? 192.259 166.406 156.431 1.00 98.02  ? 248 PHE A CE1 1 
ATOM 1750 C CE2 . PHE A 1 248 ? 190.071 166.259 157.363 1.00 98.02  ? 248 PHE A CE2 1 
ATOM 1751 C CZ  . PHE A 1 248 ? 191.248 165.654 156.985 1.00 98.02  ? 248 PHE A CZ  1 
ATOM 1752 N N   . VAL A 1 249 ? 189.398 172.694 156.030 1.00 100.00 ? 249 VAL A N   1 
ATOM 1753 C CA  . VAL A 1 249 ? 189.417 174.147 156.169 1.00 100.00 ? 249 VAL A CA  1 
ATOM 1754 C C   . VAL A 1 249 ? 188.235 174.607 157.010 1.00 100.00 ? 249 VAL A C   1 
ATOM 1755 O O   . VAL A 1 249 ? 188.376 175.464 157.889 1.00 100.00 ? 249 VAL A O   1 
ATOM 1756 C CB  . VAL A 1 249 ? 189.433 174.827 154.787 1.00 100.00 ? 249 VAL A CB  1 
ATOM 1757 C CG1 . VAL A 1 249 ? 188.248 174.387 153.942 1.00 100.00 ? 249 VAL A CG1 1 
ATOM 1758 C CG2 . VAL A 1 249 ? 189.440 176.339 154.945 1.00 100.00 ? 249 VAL A CG2 1 
ATOM 1759 N N   . LEU A 1 250 ? 187.054 174.036 156.765 1.00 97.86  ? 250 LEU A N   1 
ATOM 1760 C CA  . LEU A 1 250 ? 185.893 174.393 157.570 1.00 97.86  ? 250 LEU A CA  1 
ATOM 1761 C C   . LEU A 1 250 ? 186.119 174.050 159.034 1.00 97.86  ? 250 LEU A C   1 
ATOM 1762 O O   . LEU A 1 250 ? 185.796 174.846 159.923 1.00 97.86  ? 250 LEU A O   1 
ATOM 1763 C CB  . LEU A 1 250 ? 184.649 173.684 157.038 1.00 97.86  ? 250 LEU A CB  1 
ATOM 1764 C CG  . LEU A 1 250 ? 184.028 174.311 155.790 1.00 97.86  ? 250 LEU A CG  1 
ATOM 1765 C CD1 . LEU A 1 250 ? 183.081 173.338 155.114 1.00 97.86  ? 250 LEU A CD1 1 
ATOM 1766 C CD2 . LEU A 1 250 ? 183.308 175.599 156.146 1.00 97.86  ? 250 LEU A CD2 1 
ATOM 1767 N N   . LEU A 1 251 ? 186.682 172.871 159.307 1.00 97.86  ? 251 LEU A N   1 
ATOM 1768 C CA  . LEU A 1 251 ? 186.960 172.497 160.688 1.00 97.86  ? 251 LEU A CA  1 
ATOM 1769 C C   . LEU A 1 251 ? 187.967 173.447 161.322 1.00 97.86  ? 251 LEU A C   1 
ATOM 1770 O O   . LEU A 1 251 ? 187.801 173.863 162.474 1.00 97.86  ? 251 LEU A O   1 
ATOM 1771 C CB  . LEU A 1 251 ? 187.470 171.059 160.749 1.00 97.86  ? 251 LEU A CB  1 
ATOM 1772 C CG  . LEU A 1 251 ? 186.389 170.021 161.038 1.00 97.86  ? 251 LEU A CG  1 
ATOM 1773 C CD1 . LEU A 1 251 ? 185.434 169.920 159.873 1.00 97.86  ? 251 LEU A CD1 1 
ATOM 1774 C CD2 . LEU A 1 251 ? 187.001 168.672 161.337 1.00 97.86  ? 251 LEU A CD2 1 
ATOM 1775 N N   . LYS A 1 252 ? 189.020 173.803 160.584 1.00 107.23 ? 252 LYS A N   1 
ATOM 1776 C CA  . LYS A 1 252 ? 189.994 174.751 161.110 1.00 107.23 ? 252 LYS A CA  1 
ATOM 1777 C C   . LYS A 1 252 ? 189.352 176.107 161.363 1.00 107.23 ? 252 LYS A C   1 
ATOM 1778 O O   . LYS A 1 252 ? 189.635 176.757 162.375 1.00 107.23 ? 252 LYS A O   1 
ATOM 1779 C CB  . LYS A 1 252 ? 191.170 174.885 160.144 1.00 107.23 ? 252 LYS A CB  1 
ATOM 1780 C CG  . LYS A 1 252 ? 192.305 175.748 160.671 1.00 107.23 ? 252 LYS A CG  1 
ATOM 1781 C CD  . LYS A 1 252 ? 192.264 177.149 160.079 1.00 107.23 ? 252 LYS A CD  1 
ATOM 1782 C CE  . LYS A 1 252 ? 193.224 178.088 160.793 1.00 107.23 ? 252 LYS A CE  1 
ATOM 1783 N NZ  . LYS A 1 252 ? 192.814 179.513 160.661 1.00 107.23 ? 252 LYS A NZ  1 
ATOM 1784 N N   . ILE A 1 253 ? 188.479 176.549 160.455 1.00 105.31 ? 253 ILE A N   1 
ATOM 1785 C CA  . ILE A 1 253 ? 187.811 177.834 160.637 1.00 105.31 ? 253 ILE A CA  1 
ATOM 1786 C C   . ILE A 1 253 ? 187.012 177.837 161.932 1.00 105.31 ? 253 ILE A C   1 
ATOM 1787 O O   . ILE A 1 253 ? 186.975 178.841 162.653 1.00 105.31 ? 253 ILE A O   1 
ATOM 1788 C CB  . ILE A 1 253 ? 186.917 178.150 159.422 1.00 105.31 ? 253 ILE A CB  1 
ATOM 1789 C CG1 . ILE A 1 253 ? 187.755 178.560 158.204 1.00 105.31 ? 253 ILE A CG1 1 
ATOM 1790 C CG2 . ILE A 1 253 ? 185.923 179.251 159.764 1.00 105.31 ? 253 ILE A CG2 1 
ATOM 1791 C CD1 . ILE A 1 253 ? 188.780 179.648 158.469 1.00 105.31 ? 253 ILE A CD1 1 
ATOM 1792 N N   . TYR A 1 254 ? 186.362 176.721 162.249 1.00 97.86  ? 254 TYR A N   1 
ATOM 1793 C CA  . TYR A 1 254 ? 185.536 176.622 163.443 1.00 97.86  ? 254 TYR A CA  1 
ATOM 1794 C C   . TYR A 1 254 ? 186.300 176.088 164.647 1.00 97.86  ? 254 TYR A C   1 
ATOM 1795 O O   . TYR A 1 254 ? 185.696 175.871 165.702 1.00 97.86  ? 254 TYR A O   1 
ATOM 1796 C CB  . TYR A 1 254 ? 184.314 175.749 163.160 1.00 97.86  ? 254 TYR A CB  1 
ATOM 1797 C CG  . TYR A 1 254 ? 183.175 176.528 162.548 1.00 97.86  ? 254 TYR A CG  1 
ATOM 1798 C CD1 . TYR A 1 254 ? 182.309 177.264 163.343 1.00 97.86  ? 254 TYR A CD1 1 
ATOM 1799 C CD2 . TYR A 1 254 ? 182.975 176.541 161.177 1.00 97.86  ? 254 TYR A CD2 1 
ATOM 1800 C CE1 . TYR A 1 254 ? 181.270 177.983 162.789 1.00 97.86  ? 254 TYR A CE1 1 
ATOM 1801 C CE2 . TYR A 1 254 ? 181.939 177.257 160.614 1.00 97.86  ? 254 TYR A CE2 1 
ATOM 1802 C CZ  . TYR A 1 254 ? 181.090 177.977 161.425 1.00 97.86  ? 254 TYR A CZ  1 
ATOM 1803 O OH  . TYR A 1 254 ? 180.056 178.692 160.869 1.00 97.86  ? 254 TYR A OH  1 
ATOM 1804 N N   . GLY A 1 255 ? 187.606 175.875 164.518 1.00 100.94 ? 255 GLY A N   1 
ATOM 1805 C CA  . GLY A 1 255 ? 188.425 175.561 165.670 1.00 100.94 ? 255 GLY A CA  1 
ATOM 1806 C C   . GLY A 1 255 ? 188.420 174.116 166.105 1.00 100.94 ? 255 GLY A C   1 
ATOM 1807 O O   . GLY A 1 255 ? 188.675 173.838 167.280 1.00 100.94 ? 255 GLY A O   1 
ATOM 1808 N N   . ILE A 1 256 ? 188.133 173.184 165.203 1.00 97.86  ? 256 ILE A N   1 
ATOM 1809 C CA  . ILE A 1 256 ? 188.214 171.756 165.488 1.00 97.86  ? 256 ILE A CA  1 
ATOM 1810 C C   . ILE A 1 256 ? 189.402 171.201 164.719 1.00 97.86  ? 256 ILE A C   1 
ATOM 1811 O O   . ILE A 1 256 ? 189.425 171.245 163.483 1.00 97.86  ? 256 ILE A O   1 
ATOM 1812 C CB  . ILE A 1 256 ? 186.918 171.026 165.110 1.00 97.86  ? 256 ILE A CB  1 
ATOM 1813 C CG1 . ILE A 1 256 ? 185.722 171.680 165.804 1.00 97.86  ? 256 ILE A CG1 1 
ATOM 1814 C CG2 . ILE A 1 256 ? 187.009 169.556 165.489 1.00 97.86  ? 256 ILE A CG2 1 
ATOM 1815 C CD1 . ILE A 1 256 ? 184.923 172.592 164.904 1.00 97.86  ? 256 ILE A CD1 1 
ATOM 1816 N N   . ASP A 1 257 ? 190.388 170.681 165.446 1.00 116.57 ? 257 ASP A N   1 
ATOM 1817 C CA  . ASP A 1 257 ? 191.593 170.156 164.820 1.00 116.57 ? 257 ASP A CA  1 
ATOM 1818 C C   . ASP A 1 257 ? 191.193 169.048 163.854 1.00 116.57 ? 257 ASP A C   1 
ATOM 1819 O O   . ASP A 1 257 ? 190.766 167.973 164.294 1.00 116.57 ? 257 ASP A O   1 
ATOM 1820 C CB  . ASP A 1 257 ? 192.571 169.639 165.879 1.00 116.57 ? 257 ASP A CB  1 
ATOM 1821 C CG  . ASP A 1 257 ? 193.722 168.838 165.285 1.00 116.57 ? 257 ASP A CG  1 
ATOM 1822 O OD1 . ASP A 1 257 ? 193.475 167.852 164.560 1.00 116.57 ? 257 ASP A OD1 1 
ATOM 1823 O OD2 . ASP A 1 257 ? 194.887 169.202 165.547 1.00 116.57 ? 257 ASP A OD2 1 
ATOM 1824 N N   . PRO A 1 258 ? 191.313 169.259 162.541 1.00 102.63 ? 258 PRO A N   1 
ATOM 1825 C CA  . PRO A 1 258 ? 190.873 168.211 161.606 1.00 102.63 ? 258 PRO A CA  1 
ATOM 1826 C C   . PRO A 1 258 ? 191.567 166.880 161.826 1.00 102.63 ? 258 PRO A C   1 
ATOM 1827 O O   . PRO A 1 258 ? 190.933 165.826 161.693 1.00 102.63 ? 258 PRO A O   1 
ATOM 1828 C CB  . PRO A 1 258 ? 191.204 168.807 160.231 1.00 102.63 ? 258 PRO A CB  1 
ATOM 1829 C CG  . PRO A 1 258 ? 191.313 170.271 160.454 1.00 102.63 ? 258 PRO A CG  1 
ATOM 1830 C CD  . PRO A 1 258 ? 191.843 170.437 161.836 1.00 102.63 ? 258 PRO A CD  1 
ATOM 1831 N N   . ILE A 1 259 ? 192.856 166.895 162.167 1.00 108.82 ? 259 ILE A N   1 
ATOM 1832 C CA  . ILE A 1 259 ? 193.583 165.642 162.353 1.00 108.82 ? 259 ILE A CA  1 
ATOM 1833 C C   . ILE A 1 259 ? 192.987 164.857 163.513 1.00 108.82 ? 259 ILE A C   1 
ATOM 1834 O O   . ILE A 1 259 ? 192.751 163.648 163.414 1.00 108.82 ? 259 ILE A O   1 
ATOM 1835 C CB  . ILE A 1 259 ? 195.082 165.915 162.569 1.00 108.82 ? 259 ILE A CB  1 
ATOM 1836 C CG1 . ILE A 1 259 ? 195.609 166.912 161.532 1.00 108.82 ? 259 ILE A CG1 1 
ATOM 1837 C CG2 . ILE A 1 259 ? 195.867 164.616 162.497 1.00 108.82 ? 259 ILE A CG2 1 
ATOM 1838 C CD1 . ILE A 1 259 ? 195.201 166.600 160.106 1.00 108.82 ? 259 ILE A CD1 1 
ATOM 1839 N N   . SER A 1 260 ? 192.737 165.534 164.635 1.00 109.88 ? 260 SER A N   1 
ATOM 1840 C CA  . SER A 1 260 ? 192.096 164.867 165.762 1.00 109.88 ? 260 SER A CA  1 
ATOM 1841 C C   . SER A 1 260 ? 190.692 164.408 165.394 1.00 109.88 ? 260 SER A C   1 
ATOM 1842 O O   . SER A 1 260 ? 190.275 163.303 165.761 1.00 109.88 ? 260 SER A O   1 
ATOM 1843 C CB  . SER A 1 260 ? 192.054 165.802 166.969 1.00 109.88 ? 260 SER A CB  1 
ATOM 1844 O OG  . SER A 1 260 ? 191.422 165.177 168.073 1.00 109.88 ? 260 SER A OG  1 
ATOM 1845 N N   . PHE A 1 261 ? 189.948 165.244 164.669 1.00 101.63 ? 261 PHE A N   1 
ATOM 1846 C CA  . PHE A 1 261 ? 188.589 164.883 164.284 1.00 101.63 ? 261 PHE A CA  1 
ATOM 1847 C C   . PHE A 1 261 ? 188.583 163.647 163.396 1.00 101.63 ? 261 PHE A C   1 
ATOM 1848 O O   . PHE A 1 261 ? 187.849 162.686 163.653 1.00 101.63 ? 261 PHE A O   1 
ATOM 1849 C CB  . PHE A 1 261 ? 187.923 166.062 163.575 1.00 101.63 ? 261 PHE A CB  1 
ATOM 1850 C CG  . PHE A 1 261 ? 186.805 165.666 162.653 1.00 101.63 ? 261 PHE A CG  1 
ATOM 1851 C CD1 . PHE A 1 261 ? 187.051 165.382 161.321 1.00 101.63 ? 261 PHE A CD1 1 
ATOM 1852 C CD2 . PHE A 1 261 ? 185.506 165.592 163.117 1.00 101.63 ? 261 PHE A CD2 1 
ATOM 1853 C CE1 . PHE A 1 261 ? 186.024 165.023 160.475 1.00 101.63 ? 261 PHE A CE1 1 
ATOM 1854 C CE2 . PHE A 1 261 ? 184.475 165.234 162.274 1.00 101.63 ? 261 PHE A CE2 1 
ATOM 1855 C CZ  . PHE A 1 261 ? 184.735 164.950 160.952 1.00 101.63 ? 261 PHE A CZ  1 
ATOM 1856 N N   . ILE A 1 262 ? 189.401 163.650 162.342 1.00 103.77 ? 262 ILE A N   1 
ATOM 1857 C CA  . ILE A 1 262 ? 189.391 162.524 161.417 1.00 103.77 ? 262 ILE A CA  1 
ATOM 1858 C C   . ILE A 1 262 ? 189.864 161.257 162.110 1.00 103.77 ? 262 ILE A C   1 
ATOM 1859 O O   . ILE A 1 262 ? 189.455 160.150 161.740 1.00 103.77 ? 262 ILE A O   1 
ATOM 1860 C CB  . ILE A 1 262 ? 190.241 162.841 160.173 1.00 103.77 ? 262 ILE A CB  1 
ATOM 1861 C CG1 . ILE A 1 262 ? 189.782 161.987 158.990 1.00 103.77 ? 262 ILE A CG1 1 
ATOM 1862 C CG2 . ILE A 1 262 ? 191.713 162.608 160.455 1.00 103.77 ? 262 ILE A CG2 1 
ATOM 1863 C CD1 . ILE A 1 262 ? 190.082 162.598 157.647 1.00 103.77 ? 262 ILE A CD1 1 
ATOM 1864 N N   . LYS A 1 263 ? 190.728 161.385 163.119 1.00 111.09 ? 263 LYS A N   1 
ATOM 1865 C CA  . LYS A 1 263 ? 191.142 160.209 163.874 1.00 111.09 ? 263 LYS A CA  1 
ATOM 1866 C C   . LYS A 1 263 ? 189.942 159.529 164.516 1.00 111.09 ? 263 LYS A C   1 
ATOM 1867 O O   . LYS A 1 263 ? 189.817 158.300 164.471 1.00 111.09 ? 263 LYS A O   1 
ATOM 1868 C CB  . LYS A 1 263 ? 192.167 160.601 164.936 1.00 111.09 ? 263 LYS A CB  1 
ATOM 1869 C CG  . LYS A 1 263 ? 193.590 160.686 164.414 1.00 111.09 ? 263 LYS A CG  1 
ATOM 1870 C CD  . LYS A 1 263 ? 194.569 161.030 165.523 1.00 111.09 ? 263 LYS A CD  1 
ATOM 1871 C CE  . LYS A 1 263 ? 195.979 161.207 164.983 1.00 111.09 ? 263 LYS A CE  1 
ATOM 1872 N NZ  . LYS A 1 263 ? 196.553 159.928 164.483 1.00 111.09 ? 263 LYS A NZ  1 
ATOM 1873 N N   . HIS A 1 264 ? 189.045 160.313 165.117 1.00 103.65 ? 264 HIS A N   1 
ATOM 1874 C CA  . HIS A 1 264 ? 187.823 159.742 165.671 1.00 103.65 ? 264 HIS A CA  1 
ATOM 1875 C C   . HIS A 1 264 ? 186.939 159.166 164.573 1.00 103.65 ? 264 HIS A C   1 
ATOM 1876 O O   . HIS A 1 264 ? 186.353 158.091 164.740 1.00 103.65 ? 264 HIS A O   1 
ATOM 1877 C CB  . HIS A 1 264 ? 187.062 160.802 166.465 1.00 103.65 ? 264 HIS A CB  1 
ATOM 1878 C CG  . HIS A 1 264 ? 187.777 161.261 167.696 1.00 103.65 ? 264 HIS A CG  1 
ATOM 1879 N ND1 . HIS A 1 264 ? 187.481 162.450 168.328 1.00 103.65 ? 264 HIS A ND1 1 
ATOM 1880 C CD2 . HIS A 1 264 ? 188.773 160.692 168.414 1.00 103.65 ? 264 HIS A CD2 1 
ATOM 1881 C CE1 . HIS A 1 264 ? 188.265 162.593 169.381 1.00 103.65 ? 264 HIS A CE1 1 
ATOM 1882 N NE2 . HIS A 1 264 ? 189.059 161.541 169.455 1.00 103.65 ? 264 HIS A NE2 1 
ATOM 1883 N N   . ALA A 1 265 ? 186.833 159.862 163.445 1.00 102.65 ? 265 ALA A N   1 
ATOM 1884 C CA  . ALA A 1 265 ? 185.970 159.441 162.351 1.00 102.65 ? 265 ALA A CA  1 
ATOM 1885 C C   . ALA A 1 265 ? 186.577 158.331 161.505 1.00 102.65 ? 265 ALA A C   1 
ATOM 1886 O O   . ALA A 1 265 ? 186.049 158.040 160.426 1.00 102.65 ? 265 ALA A O   1 
ATOM 1887 C CB  . ALA A 1 265 ? 185.633 160.639 161.461 1.00 102.65 ? 265 ALA A CB  1 
ATOM 1888 N N   . LYS A 1 266 ? 187.664 157.706 161.958 1.00 103.85 ? 266 LYS A N   1 
ATOM 1889 C CA  . LYS A 1 266 ? 188.275 156.636 161.178 1.00 103.85 ? 266 LYS A CA  1 
ATOM 1890 C C   . LYS A 1 266 ? 187.295 155.491 160.963 1.00 103.85 ? 266 LYS A C   1 
ATOM 1891 O O   . LYS A 1 266 ? 187.148 154.984 159.846 1.00 103.85 ? 266 LYS A O   1 
ATOM 1892 C CB  . LYS A 1 266 ? 189.539 156.137 161.877 1.00 103.85 ? 266 LYS A CB  1 
ATOM 1893 C CG  . LYS A 1 266 ? 190.282 155.054 161.114 1.00 103.85 ? 266 LYS A CG  1 
ATOM 1894 C CD  . LYS A 1 266 ? 191.594 154.696 161.790 1.00 103.85 ? 266 LYS A CD  1 
ATOM 1895 C CE  . LYS A 1 266 ? 192.397 153.711 160.956 1.00 103.85 ? 266 LYS A CE  1 
ATOM 1896 N NZ  . LYS A 1 266 ? 193.763 153.493 161.508 1.00 103.85 ? 266 LYS A NZ  1 
ATOM 1897 N N   . ASP A 1 267 ? 186.609 155.072 162.027 1.00 102.58 ? 267 ASP A N   1 
ATOM 1898 C CA  . ASP A 1 267 ? 185.659 153.972 161.901 1.00 102.58 ? 267 ASP A CA  1 
ATOM 1899 C C   . ASP A 1 267 ? 184.517 154.343 160.964 1.00 102.58 ? 267 ASP A C   1 
ATOM 1900 O O   . ASP A 1 267 ? 184.126 153.552 160.099 1.00 102.58 ? 267 ASP A O   1 
ATOM 1901 C CB  . ASP A 1 267 ? 185.121 153.589 163.279 1.00 102.58 ? 267 ASP A CB  1 
ATOM 1902 C CG  . ASP A 1 267 ? 186.020 152.607 164.005 1.00 102.58 ? 267 ASP A CG  1 
ATOM 1903 O OD1 . ASP A 1 267 ? 186.774 151.873 163.334 1.00 102.58 ? 267 ASP A OD1 1 
ATOM 1904 O OD2 . ASP A 1 267 ? 185.972 152.569 165.253 1.00 102.58 ? 267 ASP A OD2 1 
ATOM 1905 N N   . ALA A 1 268 ? 183.971 155.550 161.120 1.00 100.35 ? 268 ALA A N   1 
ATOM 1906 C CA  . ALA A 1 268 ? 182.853 155.961 160.279 1.00 100.35 ? 268 ALA A CA  1 
ATOM 1907 C C   . ALA A 1 268 ? 183.260 156.028 158.815 1.00 100.35 ? 268 ALA A C   1 
ATOM 1908 O O   . ALA A 1 268 ? 182.533 155.546 157.939 1.00 100.35 ? 268 ALA A O   1 
ATOM 1909 C CB  . ALA A 1 268 ? 182.317 157.313 160.745 1.00 100.35 ? 268 ALA A CB  1 
ATOM 1910 N N   . MET A 1 269 ? 184.422 156.615 158.527 1.00 111.94 ? 269 MET A N   1 
ATOM 1911 C CA  . MET A 1 269 ? 184.842 156.777 157.140 1.00 111.94 ? 269 MET A CA  1 
ATOM 1912 C C   . MET A 1 269 ? 185.051 155.426 156.467 1.00 111.94 ? 269 MET A C   1 
ATOM 1913 O O   . MET A 1 269 ? 184.583 155.199 155.346 1.00 111.94 ? 269 MET A O   1 
ATOM 1914 C CB  . MET A 1 269 ? 186.121 157.610 157.077 1.00 111.94 ? 269 MET A CB  1 
ATOM 1915 C CG  . MET A 1 269 ? 185.905 159.087 157.354 1.00 111.94 ? 269 MET A CG  1 
ATOM 1916 S SD  . MET A 1 269 ? 187.409 160.088 157.368 1.00 111.94 ? 269 MET A SD  1 
ATOM 1917 C CE  . MET A 1 269 ? 188.583 159.037 156.516 1.00 111.94 ? 269 MET A CE  1 
ATOM 1918 N N   . LEU A 1 270 ? 185.754 154.512 157.139 1.00 101.25 ? 270 LEU A N   1 
ATOM 1919 C CA  . LEU A 1 270 ? 186.038 153.218 156.527 1.00 101.25 ? 270 LEU A CA  1 
ATOM 1920 C C   . LEU A 1 270 ? 184.768 152.395 156.365 1.00 101.25 ? 270 LEU A C   1 
ATOM 1921 O O   . LEU A 1 270 ? 184.537 151.806 155.303 1.00 101.25 ? 270 LEU A O   1 
ATOM 1922 C CB  . LEU A 1 270 ? 187.070 152.461 157.358 1.00 101.25 ? 270 LEU A CB  1 
ATOM 1923 C CG  . LEU A 1 270 ? 188.427 153.153 157.503 1.00 101.25 ? 270 LEU A CG  1 
ATOM 1924 C CD1 . LEU A 1 270 ? 189.386 152.284 158.297 1.00 101.25 ? 270 LEU A CD1 1 
ATOM 1925 C CD2 . LEU A 1 270 ? 189.014 153.497 156.142 1.00 101.25 ? 270 LEU A CD2 1 
ATOM 1926 N N   . THR A 1 271 ? 183.930 152.340 157.402 1.00 98.31  ? 271 THR A N   1 
ATOM 1927 C CA  . THR A 1 271 ? 182.643 151.669 157.256 1.00 98.31  ? 271 THR A CA  1 
ATOM 1928 C C   . THR A 1 271 ? 181.803 152.350 156.187 1.00 98.31  ? 271 THR A C   1 
ATOM 1929 O O   . THR A 1 271 ? 181.196 151.683 155.342 1.00 98.31  ? 271 THR A O   1 
ATOM 1930 C CB  . THR A 1 271 ? 181.893 151.661 158.587 1.00 98.31  ? 271 THR A CB  1 
ATOM 1931 O OG1 . THR A 1 271 ? 181.868 152.986 159.131 1.00 98.31  ? 271 THR A OG1 1 
ATOM 1932 C CG2 . THR A 1 271 ? 182.563 150.724 159.573 1.00 98.31  ? 271 THR A CG2 1 
ATOM 1933 N N   . ALA A 1 272 ? 181.765 153.681 156.204 1.00 99.50  ? 272 ALA A N   1 
ATOM 1934 C CA  . ALA A 1 272 ? 181.043 154.411 155.170 1.00 99.50  ? 272 ALA A CA  1 
ATOM 1935 C C   . ALA A 1 272 ? 181.651 154.164 153.799 1.00 99.50  ? 272 ALA A C   1 
ATOM 1936 O O   . ALA A 1 272 ? 180.927 153.970 152.816 1.00 99.50  ? 272 ALA A O   1 
ATOM 1937 C CB  . ALA A 1 272 ? 181.049 155.903 155.487 1.00 99.50  ? 272 ALA A CB  1 
ATOM 1938 N N   . PHE A 1 273 ? 182.980 154.174 153.710 1.00 97.86  ? 273 PHE A N   1 
ATOM 1939 C CA  . PHE A 1 273 ? 183.626 154.041 152.411 1.00 97.86  ? 273 PHE A CA  1 
ATOM 1940 C C   . PHE A 1 273 ? 183.309 152.695 151.776 1.00 97.86  ? 273 PHE A C   1 
ATOM 1941 O O   . PHE A 1 273 ? 182.845 152.630 150.633 1.00 97.86  ? 273 PHE A O   1 
ATOM 1942 C CB  . PHE A 1 273 ? 185.137 154.221 152.554 1.00 97.86  ? 273 PHE A CB  1 
ATOM 1943 C CG  . PHE A 1 273 ? 185.911 153.805 151.338 1.00 97.86  ? 273 PHE A CG  1 
ATOM 1944 C CD1 . PHE A 1 273 ? 185.714 154.440 150.126 1.00 97.86  ? 273 PHE A CD1 1 
ATOM 1945 C CD2 . PHE A 1 273 ? 186.835 152.779 151.407 1.00 97.86  ? 273 PHE A CD2 1 
ATOM 1946 C CE1 . PHE A 1 273 ? 186.423 154.060 149.005 1.00 97.86  ? 273 PHE A CE1 1 
ATOM 1947 C CE2 . PHE A 1 273 ? 187.548 152.396 150.290 1.00 97.86  ? 273 PHE A CE2 1 
ATOM 1948 C CZ  . PHE A 1 273 ? 187.341 153.037 149.088 1.00 97.86  ? 273 PHE A CZ  1 
ATOM 1949 N N   . VAL A 1 274 ? 183.540 151.605 152.508 1.00 97.86  ? 274 VAL A N   1 
ATOM 1950 C CA  . VAL A 1 274 ? 183.399 150.283 151.908 1.00 97.86  ? 274 VAL A CA  1 
ATOM 1951 C C   . VAL A 1 274 ? 181.927 149.947 151.707 1.00 97.86  ? 274 VAL A C   1 
ATOM 1952 O O   . VAL A 1 274 ? 181.515 149.513 150.626 1.00 97.86  ? 274 VAL A O   1 
ATOM 1953 C CB  . VAL A 1 274 ? 184.106 149.223 152.767 1.00 97.86  ? 274 VAL A CB  1 
ATOM 1954 C CG1 . VAL A 1 274 ? 183.450 147.866 152.573 1.00 97.86  ? 274 VAL A CG1 1 
ATOM 1955 C CG2 . VAL A 1 274 ? 185.582 149.169 152.428 1.00 97.86  ? 274 VAL A CG2 1 
ATOM 1956 N N   . THR A 1 275 ? 181.114 150.133 152.743 1.00 97.86  ? 275 THR A N   1 
ATOM 1957 C CA  . THR A 1 275 ? 179.678 149.909 152.638 1.00 97.86  ? 275 THR A CA  1 
ATOM 1958 C C   . THR A 1 275 ? 179.061 151.114 151.944 1.00 97.86  ? 275 THR A C   1 
ATOM 1959 O O   . THR A 1 275 ? 179.061 152.222 152.491 1.00 97.86  ? 275 THR A O   1 
ATOM 1960 C CB  . THR A 1 275 ? 179.041 149.684 154.008 1.00 97.86  ? 275 THR A CB  1 
ATOM 1961 O OG1 . THR A 1 275 ? 178.776 150.947 154.630 1.00 97.86  ? 275 THR A OG1 1 
ATOM 1962 C CG2 . THR A 1 275 ? 179.948 148.847 154.898 1.00 97.86  ? 275 THR A CG2 1 
ATOM 1963 N N   . ARG A 1 276 ? 178.525 150.891 150.747 1.00 101.05 ? 276 ARG A N   1 
ATOM 1964 C CA  . ARG A 1 276 ? 178.156 151.994 149.871 1.00 101.05 ? 276 ARG A CA  1 
ATOM 1965 C C   . ARG A 1 276 ? 177.110 152.912 150.488 1.00 101.05 ? 276 ARG A C   1 
ATOM 1966 O O   . ARG A 1 276 ? 177.005 154.072 150.076 1.00 101.05 ? 276 ARG A O   1 
ATOM 1967 C CB  . ARG A 1 276 ? 177.638 151.444 148.541 1.00 101.05 ? 276 ARG A CB  1 
ATOM 1968 C CG  . ARG A 1 276 ? 178.502 150.348 147.924 1.00 101.05 ? 276 ARG A CG  1 
ATOM 1969 C CD  . ARG A 1 276 ? 179.161 150.814 146.646 1.00 101.05 ? 276 ARG A CD  1 
ATOM 1970 N NE  . ARG A 1 276 ? 178.180 151.059 145.596 1.00 101.05 ? 276 ARG A NE  1 
ATOM 1971 C CZ  . ARG A 1 276 ? 177.713 150.131 144.772 1.00 101.05 ? 276 ARG A CZ  1 
ATOM 1972 N NH1 . ARG A 1 276 ? 178.112 148.872 144.847 1.00 101.05 ? 276 ARG A NH1 1 
ATOM 1973 N NH2 . ARG A 1 276 ? 176.819 150.474 143.849 1.00 101.05 ? 276 ARG A NH2 1 
ATOM 1974 N N   . SER A 1 277 ? 176.342 152.433 151.462 1.00 97.86  ? 277 SER A N   1 
ATOM 1975 C CA  . SER A 1 277 ? 175.213 153.186 151.990 1.00 97.86  ? 277 SER A CA  1 
ATOM 1976 C C   . SER A 1 277 ? 175.633 154.009 153.198 1.00 97.86  ? 277 SER A C   1 
ATOM 1977 O O   . SER A 1 277 ? 176.269 153.492 154.121 1.00 97.86  ? 277 SER A O   1 
ATOM 1978 C CB  . SER A 1 277 ? 174.075 152.244 152.380 1.00 97.86  ? 277 SER A CB  1 
ATOM 1979 O OG  . SER A 1 277 ? 173.317 152.786 153.446 1.00 97.86  ? 277 SER A OG  1 
ATOM 1980 N N   . SER A 1 278 ? 175.271 155.293 153.187 1.00 99.74  ? 278 SER A N   1 
ATOM 1981 C CA  . SER A 1 278 ? 175.482 156.125 154.365 1.00 99.74  ? 278 SER A CA  1 
ATOM 1982 C C   . SER A 1 278 ? 174.555 155.707 155.499 1.00 99.74  ? 278 SER A C   1 
ATOM 1983 O O   . SER A 1 278 ? 174.933 155.770 156.674 1.00 99.74  ? 278 SER A O   1 
ATOM 1984 C CB  . SER A 1 278 ? 175.266 157.596 154.015 1.00 99.74  ? 278 SER A CB  1 
ATOM 1985 O OG  . SER A 1 278 ? 173.957 157.812 153.523 1.00 99.74  ? 278 SER A OG  1 
ATOM 1986 N N   . SER A 1 279 ? 173.334 155.283 155.166 1.00 97.86  ? 279 SER A N   1 
ATOM 1987 C CA  . SER A 1 279 ? 172.399 154.842 156.195 1.00 97.86  ? 279 SER A CA  1 
ATOM 1988 C C   . SER A 1 279 ? 172.921 153.610 156.921 1.00 97.86  ? 279 SER A C   1 
ATOM 1989 O O   . SER A 1 279 ? 172.793 153.501 158.146 1.00 97.86  ? 279 SER A O   1 
ATOM 1990 C CB  . SER A 1 279 ? 171.035 154.556 155.572 1.00 97.86  ? 279 SER A CB  1 
ATOM 1991 O OG  . SER A 1 279 ? 170.588 155.660 154.806 1.00 97.86  ? 279 SER A OG  1 
ATOM 1992 N N   . GLY A 1 280 ? 173.512 152.669 156.184 1.00 97.86  ? 280 GLY A N   1 
ATOM 1993 C CA  . GLY A 1 280 ? 174.041 151.473 156.815 1.00 97.86  ? 280 GLY A CA  1 
ATOM 1994 C C   . GLY A 1 280 ? 175.127 151.774 157.827 1.00 97.86  ? 280 GLY A C   1 
ATOM 1995 O O   . GLY A 1 280 ? 175.259 151.071 158.831 1.00 97.86  ? 280 GLY A O   1 
ATOM 1996 N N   . THR A 1 281 ? 175.918 152.812 157.579 1.00 97.86  ? 281 THR A N   1 
ATOM 1997 C CA  . THR A 1 281 ? 176.951 153.249 158.505 1.00 97.86  ? 281 THR A CA  1 
ATOM 1998 C C   . THR A 1 281 ? 176.442 154.294 159.489 1.00 97.86  ? 281 THR A C   1 
ATOM 1999 O O   . THR A 1 281 ? 177.233 154.837 160.264 1.00 97.86  ? 281 THR A O   1 
ATOM 2000 C CB  . THR A 1 281 ? 178.152 153.805 157.734 1.00 97.86  ? 281 THR A CB  1 
ATOM 2001 O OG1 . THR A 1 281 ? 179.163 154.228 158.655 1.00 97.86  ? 281 THR A OG1 1 
ATOM 2002 C CG2 . THR A 1 281 ? 177.743 154.980 156.867 1.00 97.86  ? 281 THR A CG2 1 
ATOM 2003 N N   . LEU A 1 282 ? 175.145 154.593 159.467 1.00 97.86  ? 282 LEU A N   1 
ATOM 2004 C CA  . LEU A 1 282 ? 174.601 155.594 160.381 1.00 97.86  ? 282 LEU A CA  1 
ATOM 2005 C C   . LEU A 1 282 ? 174.814 155.232 161.843 1.00 97.86  ? 282 LEU A C   1 
ATOM 2006 O O   . LEU A 1 282 ? 175.319 156.081 162.597 1.00 97.86  ? 282 LEU A O   1 
ATOM 2007 C CB  . LEU A 1 282 ? 173.115 155.802 160.076 1.00 97.86  ? 282 LEU A CB  1 
ATOM 2008 C CG  . LEU A 1 282 ? 172.405 156.882 160.889 1.00 97.86  ? 282 LEU A CG  1 
ATOM 2009 C CD1 . LEU A 1 282 ? 173.052 158.235 160.669 1.00 97.86  ? 282 LEU A CD1 1 
ATOM 2010 C CD2 . LEU A 1 282 ? 170.935 156.930 160.520 1.00 97.86  ? 282 LEU A CD2 1 
ATOM 2011 N N   . PRO A 1 283 ? 174.466 154.031 162.316 1.00 97.86  ? 283 PRO A N   1 
ATOM 2012 C CA  . PRO A 1 283 ? 174.655 153.752 163.749 1.00 97.86  ? 283 PRO A CA  1 
ATOM 2013 C C   . PRO A 1 283 ? 176.095 153.893 164.202 1.00 97.86  ? 283 PRO A C   1 
ATOM 2014 O O   . PRO A 1 283 ? 176.345 154.397 165.303 1.00 97.86  ? 283 PRO A O   1 
ATOM 2015 C CB  . PRO A 1 283 ? 174.143 152.313 163.898 1.00 97.86  ? 283 PRO A CB  1 
ATOM 2016 C CG  . PRO A 1 283 ? 174.205 151.735 162.542 1.00 97.86  ? 283 PRO A CG  1 
ATOM 2017 C CD  . PRO A 1 283 ? 173.937 152.860 161.598 1.00 97.86  ? 283 PRO A CD  1 
ATOM 2018 N N   . VAL A 1 284 ? 177.056 153.465 163.382 1.00 97.86  ? 284 VAL A N   1 
ATOM 2019 C CA  . VAL A 1 284 ? 178.455 153.672 163.738 1.00 97.86  ? 284 VAL A CA  1 
ATOM 2020 C C   . VAL A 1 284 ? 178.813 155.146 163.625 1.00 97.86  ? 284 VAL A C   1 
ATOM 2021 O O   . VAL A 1 284 ? 179.640 155.651 164.392 1.00 97.86  ? 284 VAL A O   1 
ATOM 2022 C CB  . VAL A 1 284 ? 179.374 152.793 162.870 1.00 97.86  ? 284 VAL A CB  1 
ATOM 2023 C CG1 . VAL A 1 284 ? 179.209 153.116 161.399 1.00 97.86  ? 284 VAL A CG1 1 
ATOM 2024 C CG2 . VAL A 1 284 ? 180.823 152.962 163.295 1.00 97.86  ? 284 VAL A CG2 1 
ATOM 2025 N N   . THR A 1 285 ? 178.206 155.859 162.676 1.00 97.86  ? 285 THR A N   1 
ATOM 2026 C CA  . THR A 1 285 ? 178.422 157.297 162.589 1.00 97.86  ? 285 THR A CA  1 
ATOM 2027 C C   . THR A 1 285 ? 177.933 157.997 163.851 1.00 97.86  ? 285 THR A C   1 
ATOM 2028 O O   . THR A 1 285 ? 178.599 158.901 164.367 1.00 97.86  ? 285 THR A O   1 
ATOM 2029 C CB  . THR A 1 285 ? 177.720 157.856 161.352 1.00 97.86  ? 285 THR A CB  1 
ATOM 2030 O OG1 . THR A 1 285 ? 178.534 157.635 160.195 1.00 97.86  ? 285 THR A OG1 1 
ATOM 2031 C CG2 . THR A 1 285 ? 177.457 159.340 161.500 1.00 97.86  ? 285 THR A CG2 1 
ATOM 2032 N N   . MET A 1 286 ? 176.770 157.592 164.364 1.00 97.86  ? 286 MET A N   1 
ATOM 2033 C CA  . MET A 1 286 ? 176.309 158.125 165.641 1.00 97.86  ? 286 MET A CA  1 
ATOM 2034 C C   . MET A 1 286 ? 177.272 157.756 166.758 1.00 97.86  ? 286 MET A C   1 
ATOM 2035 O O   . MET A 1 286 ? 177.555 158.573 167.642 1.00 97.86  ? 286 MET A O   1 
ATOM 2036 C CB  . MET A 1 286 ? 174.910 157.600 165.954 1.00 97.86  ? 286 MET A CB  1 
ATOM 2037 C CG  . MET A 1 286 ? 173.816 158.191 165.091 1.00 97.86  ? 286 MET A CG  1 
ATOM 2038 S SD  . MET A 1 286 ? 172.225 158.195 165.931 1.00 97.86  ? 286 MET A SD  1 
ATOM 2039 C CE  . MET A 1 286 ? 171.215 159.025 164.714 1.00 97.86  ? 286 MET A CE  1 
ATOM 2040 N N   . ARG A 1 287 ? 177.787 156.526 166.735 1.00 97.86  ? 287 ARG A N   1 
ATOM 2041 C CA  . ARG A 1 287 ? 178.757 156.113 167.742 1.00 97.86  ? 287 ARG A CA  1 
ATOM 2042 C C   . ARG A 1 287 ? 179.987 157.008 167.712 1.00 97.86  ? 287 ARG A C   1 
ATOM 2043 O O   . ARG A 1 287 ? 180.501 157.407 168.763 1.00 97.86  ? 287 ARG A O   1 
ATOM 2044 C CB  . ARG A 1 287 ? 179.146 154.653 167.515 1.00 97.86  ? 287 ARG A CB  1 
ATOM 2045 C CG  . ARG A 1 287 ? 180.063 154.080 168.576 1.00 97.86  ? 287 ARG A CG  1 
ATOM 2046 C CD  . ARG A 1 287 ? 181.419 153.727 167.996 1.00 97.86  ? 287 ARG A CD  1 
ATOM 2047 N NE  . ARG A 1 287 ? 181.350 152.580 167.099 1.00 97.86  ? 287 ARG A NE  1 
ATOM 2048 C CZ  . ARG A 1 287 ? 182.403 152.006 166.534 1.00 97.86  ? 287 ARG A CZ  1 
ATOM 2049 N NH1 . ARG A 1 287 ? 183.631 152.449 166.748 1.00 97.86  ? 287 ARG A NH1 1 
ATOM 2050 N NH2 . ARG A 1 287 ? 182.220 150.960 165.734 1.00 97.86  ? 287 ARG A NH2 1 
ATOM 2051 N N   . VAL A 1 288 ? 180.473 157.338 166.514 1.00 97.86  ? 288 VAL A N   1 
ATOM 2052 C CA  . VAL A 1 288 ? 181.628 158.223 166.403 1.00 97.86  ? 288 VAL A CA  1 
ATOM 2053 C C   . VAL A 1 288 ? 181.314 159.583 167.008 1.00 97.86  ? 288 VAL A C   1 
ATOM 2054 O O   . VAL A 1 288 ? 182.118 160.145 167.761 1.00 97.86  ? 288 VAL A O   1 
ATOM 2055 C CB  . VAL A 1 288 ? 182.062 158.347 164.932 1.00 97.86  ? 288 VAL A CB  1 
ATOM 2056 C CG1 . VAL A 1 288 ? 182.842 159.633 164.709 1.00 97.86  ? 288 VAL A CG1 1 
ATOM 2057 C CG2 . VAL A 1 288 ? 182.891 157.143 164.525 1.00 97.86  ? 288 VAL A CG2 1 
ATOM 2058 N N   . ALA A 1 289 ? 180.140 160.132 166.695 1.00 97.86  ? 289 ALA A N   1 
ATOM 2059 C CA  . ALA A 1 289 ? 179.793 161.455 167.202 1.00 97.86  ? 289 ALA A CA  1 
ATOM 2060 C C   . ALA A 1 289 ? 179.772 161.468 168.724 1.00 97.86  ? 289 ALA A C   1 
ATOM 2061 O O   . ALA A 1 289 ? 180.249 162.421 169.350 1.00 97.86  ? 289 ALA A O   1 
ATOM 2062 C CB  . ALA A 1 289 ? 178.441 161.894 166.643 1.00 97.86  ? 289 ALA A CB  1 
ATOM 2063 N N   . LYS A 1 290 ? 179.227 160.419 169.339 1.00 97.86  ? 290 LYS A N   1 
ATOM 2064 C CA  . LYS A 1 290 ? 179.199 160.356 170.795 1.00 97.86  ? 290 LYS A CA  1 
ATOM 2065 C C   . LYS A 1 290 ? 180.609 160.422 171.365 1.00 97.86  ? 290 LYS A C   1 
ATOM 2066 O O   . LYS A 1 290 ? 180.878 161.181 172.303 1.00 97.86  ? 290 LYS A O   1 
ATOM 2067 C CB  . LYS A 1 290 ? 178.491 159.081 171.250 1.00 97.86  ? 290 LYS A CB  1 
ATOM 2068 C CG  . LYS A 1 290 ? 177.833 159.196 172.612 1.00 97.86  ? 290 LYS A CG  1 
ATOM 2069 C CD  . LYS A 1 290 ? 177.171 157.893 173.022 1.00 97.86  ? 290 LYS A CD  1 
ATOM 2070 C CE  . LYS A 1 290 ? 178.182 156.898 173.567 1.00 97.86  ? 290 LYS A CE  1 
ATOM 2071 N NZ  . LYS A 1 290 ? 177.643 155.511 173.586 1.00 97.86  ? 290 LYS A NZ  1 
ATOM 2072 N N   . GLU A 1 291 ? 181.529 159.637 170.803 1.00 103.25 ? 291 GLU A N   1 
ATOM 2073 C CA  . GLU A 1 291 ? 182.917 159.700 171.240 1.00 103.25 ? 291 GLU A CA  1 
ATOM 2074 C C   . GLU A 1 291 ? 183.554 161.044 170.928 1.00 103.25 ? 291 GLU A C   1 
ATOM 2075 O O   . GLU A 1 291 ? 184.535 161.418 171.579 1.00 103.25 ? 291 GLU A O   1 
ATOM 2076 C CB  . GLU A 1 291 ? 183.731 158.582 170.587 1.00 103.25 ? 291 GLU A CB  1 
ATOM 2077 C CG  . GLU A 1 291 ? 183.220 157.185 170.888 1.00 103.25 ? 291 GLU A CG  1 
ATOM 2078 C CD  . GLU A 1 291 ? 183.815 156.139 169.969 1.00 103.25 ? 291 GLU A CD  1 
ATOM 2079 O OE1 . GLU A 1 291 ? 184.758 156.468 169.220 1.00 103.25 ? 291 GLU A OE1 1 
ATOM 2080 O OE2 . GLU A 1 291 ? 183.345 154.983 170.001 1.00 103.25 ? 291 GLU A OE2 1 
ATOM 2081 N N   . MET A 1 292 ? 183.022 161.777 169.952 1.00 103.81 ? 292 MET A N   1 
ATOM 2082 C CA  . MET A 1 292 ? 183.554 163.086 169.606 1.00 103.81 ? 292 MET A CA  1 
ATOM 2083 C C   . MET A 1 292 ? 183.081 164.183 170.548 1.00 103.81 ? 292 MET A C   1 
ATOM 2084 O O   . MET A 1 292 ? 183.535 165.324 170.419 1.00 103.81 ? 292 MET A O   1 
ATOM 2085 C CB  . MET A 1 292 ? 183.161 163.445 168.173 1.00 103.81 ? 292 MET A CB  1 
ATOM 2086 C CG  . MET A 1 292 ? 184.253 164.145 167.394 1.00 103.81 ? 292 MET A CG  1 
ATOM 2087 S SD  . MET A 1 292 ? 183.723 164.597 165.735 1.00 103.81 ? 292 MET A SD  1 
ATOM 2088 C CE  . MET A 1 292 ? 183.613 162.985 164.969 1.00 103.81 ? 292 MET A CE  1 
ATOM 2089 N N   . GLY A 1 293 ? 182.187 163.872 171.483 1.00 99.82  ? 293 GLY A N   1 
ATOM 2090 C CA  . GLY A 1 293 ? 181.690 164.850 172.424 1.00 99.82  ? 293 GLY A CA  1 
ATOM 2091 C C   . GLY A 1 293 ? 180.502 165.653 171.945 1.00 99.82  ? 293 GLY A C   1 
ATOM 2092 O O   . GLY A 1 293 ? 180.003 166.496 172.701 1.00 99.82  ? 293 GLY A O   1 
ATOM 2093 N N   . ILE A 1 294 ? 180.030 165.422 170.719 1.00 97.86  ? 294 ILE A N   1 
ATOM 2094 C CA  . ILE A 1 294 ? 178.882 166.165 170.218 1.00 97.86  ? 294 ILE A CA  1 
ATOM 2095 C C   . ILE A 1 294 ? 177.667 165.843 171.072 1.00 97.86  ? 294 ILE A C   1 
ATOM 2096 O O   . ILE A 1 294 ? 177.362 164.673 171.334 1.00 97.86  ? 294 ILE A O   1 
ATOM 2097 C CB  . ILE A 1 294 ? 178.632 165.834 168.741 1.00 97.86  ? 294 ILE A CB  1 
ATOM 2098 C CG1 . ILE A 1 294 ? 179.821 166.271 167.887 1.00 97.86  ? 294 ILE A CG1 1 
ATOM 2099 C CG2 . ILE A 1 294 ? 177.367 166.514 168.258 1.00 97.86  ? 294 ILE A CG2 1 
ATOM 2100 C CD1 . ILE A 1 294 ? 180.127 165.328 166.751 1.00 97.86  ? 294 ILE A CD1 1 
ATOM 2101 N N   . SER A 1 295 ? 176.966 166.884 171.510 1.00 97.97  ? 295 SER A N   1 
ATOM 2102 C CA  . SER A 1 295 ? 175.818 166.689 172.382 1.00 97.97  ? 295 SER A CA  1 
ATOM 2103 C C   . SER A 1 295 ? 174.729 165.900 171.669 1.00 97.97  ? 295 SER A C   1 
ATOM 2104 O O   . SER A 1 295 ? 174.429 166.139 170.496 1.00 97.97  ? 295 SER A O   1 
ATOM 2105 C CB  . SER A 1 295 ? 175.269 168.039 172.841 1.00 97.97  ? 295 SER A CB  1 
ATOM 2106 O OG  . SER A 1 295 ? 174.214 167.867 173.771 1.00 97.97  ? 295 SER A OG  1 
ATOM 2107 N N   . GLU A 1 296 ? 174.134 164.954 172.388 1.00 111.00 ? 296 GLU A N   1 
ATOM 2108 C CA  . GLU A 1 296 ? 173.025 164.190 171.840 1.00 111.00 ? 296 GLU A CA  1 
ATOM 2109 C C   . GLU A 1 296 ? 171.834 165.104 171.590 1.00 111.00 ? 296 GLU A C   1 
ATOM 2110 O O   . GLU A 1 296 ? 171.629 166.103 172.284 1.00 111.00 ? 296 GLU A O   1 
ATOM 2111 C CB  . GLU A 1 296 ? 172.632 163.059 172.787 1.00 111.00 ? 296 GLU A CB  1 
ATOM 2112 C CG  . GLU A 1 296 ? 171.728 162.017 172.155 1.00 111.00 ? 296 GLU A CG  1 
ATOM 2113 C CD  . GLU A 1 296 ? 171.471 160.838 173.072 1.00 111.00 ? 296 GLU A CD  1 
ATOM 2114 O OE1 . GLU A 1 296 ? 171.853 160.912 174.258 1.00 111.00 ? 296 GLU A OE1 1 
ATOM 2115 O OE2 . GLU A 1 296 ? 170.887 159.837 172.606 1.00 111.00 ? 296 GLU A OE2 1 
ATOM 2116 N N   . GLY A 1 297 ? 171.045 164.753 170.581 1.00 104.45 ? 297 GLY A N   1 
ATOM 2117 C CA  . GLY A 1 297 ? 169.974 165.590 170.104 1.00 104.45 ? 297 GLY A CA  1 
ATOM 2118 C C   . GLY A 1 297 ? 170.362 166.471 168.938 1.00 104.45 ? 297 GLY A C   1 
ATOM 2119 O O   . GLY A 1 297 ? 169.479 166.962 168.227 1.00 104.45 ? 297 GLY A O   1 
ATOM 2120 N N   . ILE A 1 298 ? 171.656 166.682 168.728 1.00 97.86  ? 298 ILE A N   1 
ATOM 2121 C CA  . ILE A 1 298 ? 172.164 167.364 167.546 1.00 97.86  ? 298 ILE A CA  1 
ATOM 2122 C C   . ILE A 1 298 ? 172.654 166.365 166.511 1.00 97.86  ? 298 ILE A C   1 
ATOM 2123 O O   . ILE A 1 298 ? 172.256 166.418 165.348 1.00 97.86  ? 298 ILE A O   1 
ATOM 2124 C CB  . ILE A 1 298 ? 173.283 168.352 167.940 1.00 97.86  ? 298 ILE A CB  1 
ATOM 2125 C CG1 . ILE A 1 298 ? 172.688 169.598 168.591 1.00 97.86  ? 298 ILE A CG1 1 
ATOM 2126 C CG2 . ILE A 1 298 ? 174.102 168.745 166.723 1.00 97.86  ? 298 ILE A CG2 1 
ATOM 2127 C CD1 . ILE A 1 298 ? 173.619 170.267 169.572 1.00 97.86  ? 298 ILE A CD1 1 
ATOM 2128 N N   . TYR A 1 299 ? 173.525 165.442 166.921 1.00 97.86  ? 299 TYR A N   1 
ATOM 2129 C CA  . TYR A 1 299 ? 173.980 164.407 166.002 1.00 97.86  ? 299 TYR A CA  1 
ATOM 2130 C C   . TYR A 1 299 ? 172.895 163.369 165.757 1.00 97.86  ? 299 TYR A C   1 
ATOM 2131 O O   . TYR A 1 299 ? 172.851 162.764 164.680 1.00 97.86  ? 299 TYR A O   1 
ATOM 2132 C CB  . TYR A 1 299 ? 175.255 163.749 166.539 1.00 97.86  ? 299 TYR A CB  1 
ATOM 2133 C CG  . TYR A 1 299 ? 175.050 162.758 167.665 1.00 97.86  ? 299 TYR A CG  1 
ATOM 2134 C CD1 . TYR A 1 299 ? 174.626 161.462 167.412 1.00 97.86  ? 299 TYR A CD1 1 
ATOM 2135 C CD2 . TYR A 1 299 ? 175.304 163.115 168.981 1.00 97.86  ? 299 TYR A CD2 1 
ATOM 2136 C CE1 . TYR A 1 299 ? 174.445 160.558 168.436 1.00 97.86  ? 299 TYR A CE1 1 
ATOM 2137 C CE2 . TYR A 1 299 ? 175.130 162.214 170.010 1.00 97.86  ? 299 TYR A CE2 1 
ATOM 2138 C CZ  . TYR A 1 299 ? 174.699 160.939 169.733 1.00 97.86  ? 299 TYR A CZ  1 
ATOM 2139 O OH  . TYR A 1 299 ? 174.522 160.038 170.756 1.00 97.86  ? 299 TYR A OH  1 
ATOM 2140 N N   . SER A 1 300 ? 172.012 163.152 166.733 1.00 97.86  ? 300 SER A N   1 
ATOM 2141 C CA  . SER A 1 300 ? 170.928 162.195 166.551 1.00 97.86  ? 300 SER A CA  1 
ATOM 2142 C C   . SER A 1 300 ? 169.927 162.653 165.501 1.00 97.86  ? 300 SER A C   1 
ATOM 2143 O O   . SER A 1 300 ? 169.119 161.842 165.040 1.00 97.86  ? 300 SER A O   1 
ATOM 2144 C CB  . SER A 1 300 ? 170.208 161.956 167.877 1.00 97.86  ? 300 SER A CB  1 
ATOM 2145 O OG  . SER A 1 300 ? 169.563 163.135 168.322 1.00 97.86  ? 300 SER A OG  1 
ATOM 2146 N N   . PHE A 1 301 ? 169.959 163.928 165.119 1.00 97.86  ? 301 PHE A N   1 
ATOM 2147 C CA  . PHE A 1 301 ? 169.059 164.474 164.113 1.00 97.86  ? 301 PHE A CA  1 
ATOM 2148 C C   . PHE A 1 301 ? 169.768 164.813 162.812 1.00 97.86  ? 301 PHE A C   1 
ATOM 2149 O O   . PHE A 1 301 ? 169.321 164.401 161.738 1.00 97.86  ? 301 PHE A O   1 
ATOM 2150 C CB  . PHE A 1 301 ? 168.363 165.727 164.659 1.00 97.86  ? 301 PHE A CB  1 
ATOM 2151 C CG  . PHE A 1 301 ? 167.726 166.572 163.598 1.00 97.86  ? 301 PHE A CG  1 
ATOM 2152 C CD1 . PHE A 1 301 ? 166.661 166.092 162.861 1.00 97.86  ? 301 PHE A CD1 1 
ATOM 2153 C CD2 . PHE A 1 301 ? 168.195 167.845 163.335 1.00 97.86  ? 301 PHE A CD2 1 
ATOM 2154 C CE1 . PHE A 1 301 ? 166.074 166.867 161.884 1.00 97.86  ? 301 PHE A CE1 1 
ATOM 2155 C CE2 . PHE A 1 301 ? 167.611 168.623 162.358 1.00 97.86  ? 301 PHE A CE2 1 
ATOM 2156 C CZ  . PHE A 1 301 ? 166.551 168.133 161.632 1.00 97.86  ? 301 PHE A CZ  1 
ATOM 2157 N N   . THR A 1 302 ? 170.872 165.559 162.878 1.00 97.86  ? 302 THR A N   1 
ATOM 2158 C CA  . THR A 1 302 ? 171.562 165.959 161.656 1.00 97.86  ? 302 THR A CA  1 
ATOM 2159 C C   . THR A 1 302 ? 172.094 164.750 160.899 1.00 97.86  ? 302 THR A C   1 
ATOM 2160 O O   . THR A 1 302 ? 171.986 164.684 159.669 1.00 97.86  ? 302 THR A O   1 
ATOM 2161 C CB  . THR A 1 302 ? 172.703 166.920 161.985 1.00 97.86  ? 302 THR A CB  1 
ATOM 2162 O OG1 . THR A 1 302 ? 173.640 166.273 162.854 1.00 97.86  ? 302 THR A OG1 1 
ATOM 2163 C CG2 . THR A 1 302 ? 172.171 168.173 162.660 1.00 97.86  ? 302 THR A CG2 1 
ATOM 2164 N N   . LEU A 1 303 ? 172.675 163.786 161.611 1.00 97.86  ? 303 LEU A N   1 
ATOM 2165 C CA  . LEU A 1 303 ? 173.279 162.639 160.937 1.00 97.86  ? 303 LEU A CA  1 
ATOM 2166 C C   . LEU A 1 303 ? 172.273 161.846 160.119 1.00 97.86  ? 303 LEU A C   1 
ATOM 2167 O O   . LEU A 1 303 ? 172.528 161.616 158.924 1.00 97.86  ? 303 LEU A O   1 
ATOM 2168 C CB  . LEU A 1 303 ? 173.971 161.746 161.970 1.00 97.86  ? 303 LEU A CB  1 
ATOM 2169 C CG  . LEU A 1 303 ? 175.179 162.372 162.663 1.00 97.86  ? 303 LEU A CG  1 
ATOM 2170 C CD1 . LEU A 1 303 ? 175.628 161.498 163.817 1.00 97.86  ? 303 LEU A CD1 1 
ATOM 2171 C CD2 . LEU A 1 303 ? 176.308 162.592 161.674 1.00 97.86  ? 303 LEU A CD2 1 
ATOM 2172 N N   . PRO A 1 304 ? 171.138 161.400 160.665 1.00 97.86  ? 304 PRO A N   1 
ATOM 2173 C CA  . PRO A 1 304 ? 170.160 160.713 159.807 1.00 97.86  ? 304 PRO A CA  1 
ATOM 2174 C C   . PRO A 1 304 ? 169.692 161.582 158.657 1.00 97.86  ? 304 PRO A C   1 
ATOM 2175 O O   . PRO A 1 304 ? 169.469 161.079 157.550 1.00 97.86  ? 304 PRO A O   1 
ATOM 2176 C CB  . PRO A 1 304 ? 169.019 160.365 160.774 1.00 97.86  ? 304 PRO A CB  1 
ATOM 2177 C CG  . PRO A 1 304 ? 169.230 161.218 161.971 1.00 97.86  ? 304 PRO A CG  1 
ATOM 2178 C CD  . PRO A 1 304 ? 170.696 161.462 162.066 1.00 97.86  ? 304 PRO A CD  1 
ATOM 2179 N N   . LEU A 1 305 ? 169.537 162.884 158.894 1.00 97.86  ? 305 LEU A N   1 
ATOM 2180 C CA  . LEU A 1 305 ? 169.275 163.807 157.796 1.00 97.86  ? 305 LEU A CA  1 
ATOM 2181 C C   . LEU A 1 305 ? 170.450 163.836 156.829 1.00 97.86  ? 305 LEU A C   1 
ATOM 2182 O O   . LEU A 1 305 ? 170.269 163.776 155.608 1.00 97.86  ? 305 LEU A O   1 
ATOM 2183 C CB  . LEU A 1 305 ? 168.998 165.204 158.351 1.00 97.86  ? 305 LEU A CB  1 
ATOM 2184 C CG  . LEU A 1 305 ? 168.336 166.194 157.396 1.00 97.86  ? 305 LEU A CG  1 
ATOM 2185 C CD1 . LEU A 1 305 ? 167.254 166.973 158.117 1.00 97.86  ? 305 LEU A CD1 1 
ATOM 2186 C CD2 . LEU A 1 305 ? 169.371 167.136 156.812 1.00 97.86  ? 305 LEU A CD2 1 
ATOM 2187 N N   . GLY A 1 306 ? 171.669 163.902 157.364 1.00 97.86  ? 306 GLY A N   1 
ATOM 2188 C CA  . GLY A 1 306 ? 172.840 163.984 156.510 1.00 97.86  ? 306 GLY A CA  1 
ATOM 2189 C C   . GLY A 1 306 ? 173.026 162.765 155.633 1.00 97.86  ? 306 GLY A C   1 
ATOM 2190 O O   . GLY A 1 306 ? 173.514 162.876 154.505 1.00 97.86  ? 306 GLY A O   1 
ATOM 2191 N N   . ALA A 1 307 ? 172.647 161.587 156.132 1.00 100.22 ? 307 ALA A N   1 
ATOM 2192 C CA  . ALA A 1 307 ? 172.835 160.367 155.357 1.00 100.22 ? 307 ALA A CA  1 
ATOM 2193 C C   . ALA A 1 307 ? 172.131 160.442 154.010 1.00 100.22 ? 307 ALA A C   1 
ATOM 2194 O O   . ALA A 1 307 ? 172.572 159.809 153.045 1.00 100.22 ? 307 ALA A O   1 
ATOM 2195 C CB  . ALA A 1 307 ? 172.332 159.161 156.148 1.00 100.22 ? 307 ALA A CB  1 
ATOM 2196 N N   . THR A 1 308 ? 171.046 161.206 153.923 1.00 99.39  ? 308 THR A N   1 
ATOM 2197 C CA  . THR A 1 308 ? 170.272 161.325 152.696 1.00 99.39  ? 308 THR A CA  1 
ATOM 2198 C C   . THR A 1 308 ? 170.249 162.730 152.118 1.00 99.39  ? 308 THR A C   1 
ATOM 2199 O O   . THR A 1 308 ? 170.204 162.873 150.895 1.00 99.39  ? 308 THR A O   1 
ATOM 2200 C CB  . THR A 1 308 ? 168.824 160.879 152.937 1.00 99.39  ? 308 THR A CB  1 
ATOM 2201 O OG1 . THR A 1 308 ? 168.261 161.644 154.009 1.00 99.39  ? 308 THR A OG1 1 
ATOM 2202 C CG2 . THR A 1 308 ? 168.776 159.404 153.294 1.00 99.39  ? 308 THR A CG2 1 
ATOM 2203 N N   . ILE A 1 309 ? 170.276 163.766 152.954 1.00 97.86  ? 309 ILE A N   1 
ATOM 2204 C CA  . ILE A 1 309 ? 170.208 165.127 152.437 1.00 97.86  ? 309 ILE A CA  1 
ATOM 2205 C C   . ILE A 1 309 ? 171.552 165.562 151.866 1.00 97.86  ? 309 ILE A C   1 
ATOM 2206 O O   . ILE A 1 309 ? 171.602 166.446 151.005 1.00 97.86  ? 309 ILE A O   1 
ATOM 2207 C CB  . ILE A 1 309 ? 169.726 166.086 153.541 1.00 97.86  ? 309 ILE A CB  1 
ATOM 2208 C CG1 . ILE A 1 309 ? 168.195 166.166 153.563 1.00 97.86  ? 309 ILE A CG1 1 
ATOM 2209 C CG2 . ILE A 1 309 ? 170.320 167.480 153.368 1.00 97.86  ? 309 ILE A CG2 1 
ATOM 2210 C CD1 . ILE A 1 309 ? 167.564 166.745 152.305 1.00 97.86  ? 309 ILE A CD1 1 
ATOM 2211 N N   . ASN A 1 310 ? 172.650 164.964 152.319 1.00 102.96 ? 310 ASN A N   1 
ATOM 2212 C CA  . ASN A 1 310 ? 173.969 165.391 151.873 1.00 102.96 ? 310 ASN A CA  1 
ATOM 2213 C C   . ASN A 1 310 ? 174.075 165.295 150.357 1.00 102.96 ? 310 ASN A C   1 
ATOM 2214 O O   . ASN A 1 310 ? 173.666 164.299 149.754 1.00 102.96 ? 310 ASN A O   1 
ATOM 2215 C CB  . ASN A 1 310 ? 175.048 164.537 152.534 1.00 102.96 ? 310 ASN A CB  1 
ATOM 2216 C CG  . ASN A 1 310 ? 176.445 165.012 152.206 1.00 102.96 ? 310 ASN A CG  1 
ATOM 2217 O OD1 . ASN A 1 310 ? 176.840 165.057 151.042 1.00 102.96 ? 310 ASN A OD1 1 
ATOM 2218 N ND2 . ASN A 1 310 ? 177.203 165.375 153.233 1.00 102.96 ? 310 ASN A ND2 1 
ATOM 2219 N N   . MET A 1 311 ? 174.633 166.339 149.742 1.00 106.87 ? 311 MET A N   1 
ATOM 2220 C CA  . MET A 1 311 ? 174.756 166.419 148.294 1.00 106.87 ? 311 MET A CA  1 
ATOM 2221 C C   . MET A 1 311 ? 176.197 166.513 147.815 1.00 106.87 ? 311 MET A C   1 
ATOM 2222 O O   . MET A 1 311 ? 176.425 166.559 146.602 1.00 106.87 ? 311 MET A O   1 
ATOM 2223 C CB  . MET A 1 311 ? 173.983 167.631 147.754 1.00 106.87 ? 311 MET A CB  1 
ATOM 2224 C CG  . MET A 1 311 ? 172.560 167.764 148.266 1.00 106.87 ? 311 MET A CG  1 
ATOM 2225 S SD  . MET A 1 311 ? 171.958 169.462 148.203 1.00 106.87 ? 311 MET A SD  1 
ATOM 2226 C CE  . MET A 1 311 ? 172.395 170.040 149.840 1.00 106.87 ? 311 MET A CE  1 
ATOM 2227 N N   . ASP A 1 312 ? 177.174 166.544 148.722 1.00 107.20 ? 312 ASP A N   1 
ATOM 2228 C CA  . ASP A 1 312 ? 178.553 166.779 148.305 1.00 107.20 ? 312 ASP A CA  1 
ATOM 2229 C C   . ASP A 1 312 ? 179.072 165.638 147.439 1.00 107.20 ? 312 ASP A C   1 
ATOM 2230 O O   . ASP A 1 312 ? 179.649 165.870 146.371 1.00 107.20 ? 312 ASP A O   1 
ATOM 2231 C CB  . ASP A 1 312 ? 179.450 166.979 149.527 1.00 107.20 ? 312 ASP A CB  1 
ATOM 2232 C CG  . ASP A 1 312 ? 178.756 167.728 150.645 1.00 107.20 ? 312 ASP A CG  1 
ATOM 2233 O OD1 . ASP A 1 312 ? 178.609 168.961 150.529 1.00 107.20 ? 312 ASP A OD1 1 
ATOM 2234 O OD2 . ASP A 1 312 ? 178.365 167.086 151.641 1.00 107.20 ? 312 ASP A OD2 1 
ATOM 2235 N N   . GLY A 1 313 ? 178.878 164.397 147.882 1.00 104.91 ? 313 GLY A N   1 
ATOM 2236 C CA  . GLY A 1 313 ? 179.411 163.272 147.131 1.00 104.91 ? 313 GLY A CA  1 
ATOM 2237 C C   . GLY A 1 313 ? 178.780 163.136 145.760 1.00 104.91 ? 313 GLY A C   1 
ATOM 2238 O O   . GLY A 1 313 ? 179.475 162.956 144.757 1.00 104.91 ? 313 GLY A O   1 
ATOM 2239 N N   . THR A 1 314 ? 177.451 163.222 145.697 1.00 107.61 ? 314 THR A N   1 
ATOM 2240 C CA  . THR A 1 314 ? 176.767 163.054 144.419 1.00 107.61 ? 314 THR A CA  1 
ATOM 2241 C C   . THR A 1 314 ? 177.123 164.171 143.448 1.00 107.61 ? 314 THR A C   1 
ATOM 2242 O O   . THR A 1 314 ? 177.336 163.920 142.257 1.00 107.61 ? 314 THR A O   1 
ATOM 2243 C CB  . THR A 1 314 ? 175.256 162.998 144.636 1.00 107.61 ? 314 THR A CB  1 
ATOM 2244 O OG1 . THR A 1 314 ? 174.966 162.183 145.778 1.00 107.61 ? 314 THR A OG1 1 
ATOM 2245 C CG2 . THR A 1 314 ? 174.565 162.419 143.415 1.00 107.61 ? 314 THR A CG2 1 
ATOM 2246 N N   . ALA A 1 315 ? 177.192 165.411 143.935 1.00 107.89 ? 315 ALA A N   1 
ATOM 2247 C CA  . ALA A 1 315 ? 177.533 166.523 143.056 1.00 107.89 ? 315 ALA A CA  1 
ATOM 2248 C C   . ALA A 1 315 ? 178.915 166.336 142.450 1.00 107.89 ? 315 ALA A C   1 
ATOM 2249 O O   . ALA A 1 315 ? 179.110 166.543 141.247 1.00 107.89 ? 315 ALA A O   1 
ATOM 2250 C CB  . ALA A 1 315 ? 177.462 167.839 143.827 1.00 107.89 ? 315 ALA A CB  1 
ATOM 2251 N N   . LEU A 1 316 ? 179.890 165.941 143.269 1.00 99.17  ? 316 LEU A N   1 
ATOM 2252 C CA  . LEU A 1 316 ? 181.226 165.676 142.751 1.00 99.17  ? 316 LEU A CA  1 
ATOM 2253 C C   . LEU A 1 316 ? 181.213 164.495 141.790 1.00 99.17  ? 316 LEU A C   1 
ATOM 2254 O O   . LEU A 1 316 ? 181.901 164.510 140.764 1.00 99.17  ? 316 LEU A O   1 
ATOM 2255 C CB  . LEU A 1 316 ? 182.186 165.423 143.912 1.00 99.17  ? 316 LEU A CB  1 
ATOM 2256 C CG  . LEU A 1 316 ? 183.597 164.956 143.561 1.00 99.17  ? 316 LEU A CG  1 
ATOM 2257 C CD1 . LEU A 1 316 ? 184.215 165.851 142.510 1.00 99.17  ? 316 LEU A CD1 1 
ATOM 2258 C CD2 . LEU A 1 316 ? 184.457 164.935 144.808 1.00 99.17  ? 316 LEU A CD2 1 
ATOM 2259 N N   . TYR A 1 317 ? 180.433 163.461 142.107 1.00 105.53 ? 317 TYR A N   1 
ATOM 2260 C CA  . TYR A 1 317 ? 180.337 162.304 141.224 1.00 105.53 ? 317 TYR A CA  1 
ATOM 2261 C C   . TYR A 1 317 ? 179.772 162.702 139.866 1.00 105.53 ? 317 TYR A C   1 
ATOM 2262 O O   . TYR A 1 317 ? 180.300 162.307 138.821 1.00 105.53 ? 317 TYR A O   1 
ATOM 2263 C CB  . TYR A 1 317 ? 179.475 161.227 141.891 1.00 105.53 ? 317 TYR A CB  1 
ATOM 2264 C CG  . TYR A 1 317 ? 179.153 160.016 141.039 1.00 105.53 ? 317 TYR A CG  1 
ATOM 2265 C CD1 . TYR A 1 317 ? 178.292 160.103 139.953 1.00 105.53 ? 317 TYR A CD1 1 
ATOM 2266 C CD2 . TYR A 1 317 ? 179.704 158.777 141.334 1.00 105.53 ? 317 TYR A CD2 1 
ATOM 2267 C CE1 . TYR A 1 317 ? 177.998 158.998 139.184 1.00 105.53 ? 317 TYR A CE1 1 
ATOM 2268 C CE2 . TYR A 1 317 ? 179.415 157.666 140.571 1.00 105.53 ? 317 TYR A CE2 1 
ATOM 2269 C CZ  . TYR A 1 317 ? 178.561 157.782 139.498 1.00 105.53 ? 317 TYR A CZ  1 
ATOM 2270 O OH  . TYR A 1 317 ? 178.270 156.677 138.734 1.00 105.53 ? 317 TYR A OH  1 
ATOM 2271 N N   . GLN A 1 318 ? 178.696 163.491 139.862 1.00 110.17 ? 318 GLN A N   1 
ATOM 2272 C CA  . GLN A 1 318 ? 178.079 163.888 138.600 1.00 110.17 ? 318 GLN A CA  1 
ATOM 2273 C C   . GLN A 1 318 ? 178.923 164.909 137.853 1.00 110.17 ? 318 GLN A C   1 
ATOM 2274 O O   . GLN A 1 318 ? 178.903 164.940 136.618 1.00 110.17 ? 318 GLN A O   1 
ATOM 2275 C CB  . GLN A 1 318 ? 176.685 164.456 138.848 1.00 110.17 ? 318 GLN A CB  1 
ATOM 2276 C CG  . GLN A 1 318 ? 175.576 163.429 138.758 1.00 110.17 ? 318 GLN A CG  1 
ATOM 2277 C CD  . GLN A 1 318 ? 174.420 163.735 139.685 1.00 110.17 ? 318 GLN A CD  1 
ATOM 2278 O OE1 . GLN A 1 318 ? 174.447 164.713 140.431 1.00 110.17 ? 318 GLN A OE1 1 
ATOM 2279 N NE2 . GLN A 1 318 ? 173.389 162.906 139.634 1.00 110.17 ? 318 GLN A NE2 1 
ATOM 2280 N N   . GLY A 1 319 ? 179.658 165.756 138.573 1.00 109.47 ? 319 GLY A N   1 
ATOM 2281 C CA  . GLY A 1 319 ? 180.483 166.746 137.903 1.00 109.47 ? 319 GLY A CA  1 
ATOM 2282 C C   . GLY A 1 319 ? 181.481 166.118 136.951 1.00 109.47 ? 319 GLY A C   1 
ATOM 2283 O O   . GLY A 1 319 ? 181.722 166.635 135.858 1.00 109.47 ? 319 GLY A O   1 
ATOM 2284 N N   . VAL A 1 320 ? 182.070 164.995 137.349 1.00 106.49 ? 320 VAL A N   1 
ATOM 2285 C CA  . VAL A 1 320 ? 183.052 164.309 136.517 1.00 106.49 ? 320 VAL A CA  1 
ATOM 2286 C C   . VAL A 1 320 ? 182.387 163.299 135.596 1.00 106.49 ? 320 VAL A C   1 
ATOM 2287 O O   . VAL A 1 320 ? 182.623 163.293 134.385 1.00 106.49 ? 320 VAL A O   1 
ATOM 2288 C CB  . VAL A 1 320 ? 184.114 163.635 137.411 1.00 106.49 ? 320 VAL A CB  1 
ATOM 2289 C CG1 . VAL A 1 320 ? 184.709 162.416 136.716 1.00 106.49 ? 320 VAL A CG1 1 
ATOM 2290 C CG2 . VAL A 1 320 ? 185.200 164.628 137.784 1.00 106.49 ? 320 VAL A CG2 1 
ATOM 2291 N N   . CYS A 1 321 ? 181.546 162.427 136.153 1.00 110.22 ? 321 CYS A N   1 
ATOM 2292 C CA  . CYS A 1 321 ? 180.963 161.356 135.354 1.00 110.22 ? 321 CYS A CA  1 
ATOM 2293 C C   . CYS A 1 321 ? 180.106 161.912 134.224 1.00 110.22 ? 321 CYS A C   1 
ATOM 2294 O O   . CYS A 1 321 ? 180.173 161.426 133.090 1.00 110.22 ? 321 CYS A O   1 
ATOM 2295 C CB  . CYS A 1 321 ? 180.139 160.432 136.245 1.00 110.22 ? 321 CYS A CB  1 
ATOM 2296 S SG  . CYS A 1 321 ? 178.839 159.554 135.370 1.00 110.22 ? 321 CYS A SG  1 
ATOM 2297 N N   . THR A 1 322 ? 179.295 162.932 134.510 1.00 104.59 ? 322 THR A N   1 
ATOM 2298 C CA  . THR A 1 322 ? 178.487 163.536 133.456 1.00 104.59 ? 322 THR A CA  1 
ATOM 2299 C C   . THR A 1 322 ? 179.372 164.126 132.368 1.00 104.59 ? 322 THR A C   1 
ATOM 2300 O O   . THR A 1 322 ? 179.080 163.987 131.174 1.00 104.59 ? 322 THR A O   1 
ATOM 2301 C CB  . THR A 1 322 ? 177.574 164.612 134.037 1.00 104.59 ? 322 THR A CB  1 
ATOM 2302 O OG1 . THR A 1 322 ? 176.897 164.099 135.191 1.00 104.59 ? 322 THR A OG1 1 
ATOM 2303 C CG2 . THR A 1 322 ? 176.548 165.049 133.006 1.00 104.59 ? 322 THR A CG2 1 
ATOM 2304 N N   . PHE A 1 323 ? 180.461 164.788 132.761 1.00 110.05 ? 323 PHE A N   1 
ATOM 2305 C CA  . PHE A 1 323 ? 181.405 165.304 131.778 1.00 110.05 ? 323 PHE A CA  1 
ATOM 2306 C C   . PHE A 1 323 ? 181.955 164.181 130.913 1.00 110.05 ? 323 PHE A C   1 
ATOM 2307 O O   . PHE A 1 323 ? 182.125 164.345 129.699 1.00 110.05 ? 323 PHE A O   1 
ATOM 2308 C CB  . PHE A 1 323 ? 182.541 166.037 132.488 1.00 110.05 ? 323 PHE A CB  1 
ATOM 2309 C CG  . PHE A 1 323 ? 183.402 166.858 131.574 1.00 110.05 ? 323 PHE A CG  1 
ATOM 2310 C CD1 . PHE A 1 323 ? 182.887 167.964 130.924 1.00 110.05 ? 323 PHE A CD1 1 
ATOM 2311 C CD2 . PHE A 1 323 ? 184.730 166.529 131.375 1.00 110.05 ? 323 PHE A CD2 1 
ATOM 2312 C CE1 . PHE A 1 323 ? 183.680 168.722 130.087 1.00 110.05 ? 323 PHE A CE1 1 
ATOM 2313 C CE2 . PHE A 1 323 ? 185.528 167.283 130.539 1.00 110.05 ? 323 PHE A CE2 1 
ATOM 2314 C CZ  . PHE A 1 323 ? 185.002 168.381 129.895 1.00 110.05 ? 323 PHE A CZ  1 
ATOM 2315 N N   . PHE A 1 324 ? 182.236 163.027 131.521 1.00 108.56 ? 324 PHE A N   1 
ATOM 2316 C CA  . PHE A 1 324 ? 182.750 161.896 130.758 1.00 108.56 ? 324 PHE A CA  1 
ATOM 2317 C C   . PHE A 1 324 ? 181.743 161.432 129.716 1.00 108.56 ? 324 PHE A C   1 
ATOM 2318 O O   . PHE A 1 324 ? 182.112 161.134 128.574 1.00 108.56 ? 324 PHE A O   1 
ATOM 2319 C CB  . PHE A 1 324 ? 183.107 160.750 131.701 1.00 108.56 ? 324 PHE A CB  1 
ATOM 2320 C CG  . PHE A 1 324 ? 183.204 159.420 131.021 1.00 108.56 ? 324 PHE A CG  1 
ATOM 2321 C CD1 . PHE A 1 324 ? 184.317 159.095 130.270 1.00 108.56 ? 324 PHE A CD1 1 
ATOM 2322 C CD2 . PHE A 1 324 ? 182.181 158.498 131.126 1.00 108.56 ? 324 PHE A CD2 1 
ATOM 2323 C CE1 . PHE A 1 324 ? 184.410 157.874 129.640 1.00 108.56 ? 324 PHE A CE1 1 
ATOM 2324 C CE2 . PHE A 1 324 ? 182.268 157.275 130.498 1.00 108.56 ? 324 PHE A CE2 1 
ATOM 2325 C CZ  . PHE A 1 324 ? 183.384 156.963 129.754 1.00 108.56 ? 324 PHE A CZ  1 
ATOM 2326 N N   . ILE A 1 325 ? 180.464 161.363 130.087 1.00 109.38 ? 325 ILE A N   1 
ATOM 2327 C CA  . ILE A 1 325 ? 179.447 160.918 129.140 1.00 109.38 ? 325 ILE A CA  1 
ATOM 2328 C C   . ILE A 1 325 ? 179.394 161.857 127.944 1.00 109.38 ? 325 ILE A C   1 
ATOM 2329 O O   . ILE A 1 325 ? 179.327 161.415 126.791 1.00 109.38 ? 325 ILE A O   1 
ATOM 2330 C CB  . ILE A 1 325 ? 178.078 160.810 129.834 1.00 109.38 ? 325 ILE A CB  1 
ATOM 2331 C CG1 . ILE A 1 325 ? 178.029 159.565 130.720 1.00 109.38 ? 325 ILE A CG1 1 
ATOM 2332 C CG2 . ILE A 1 325 ? 176.960 160.775 128.802 1.00 109.38 ? 325 ILE A CG2 1 
ATOM 2333 C CD1 . ILE A 1 325 ? 177.716 158.288 129.970 1.00 109.38 ? 325 ILE A CD1 1 
ATOM 2334 N N   . ALA A 1 326 ? 179.429 163.166 128.196 1.00 114.96 ? 326 ALA A N   1 
ATOM 2335 C CA  . ALA A 1 326 ? 179.347 164.131 127.106 1.00 114.96 ? 326 ALA A CA  1 
ATOM 2336 C C   . ALA A 1 326 ? 180.430 163.875 126.067 1.00 114.96 ? 326 ALA A C   1 
ATOM 2337 O O   . ALA A 1 326 ? 180.159 163.851 124.861 1.00 114.96 ? 326 ALA A O   1 
ATOM 2338 C CB  . ALA A 1 326 ? 179.457 165.550 127.658 1.00 114.96 ? 326 ALA A CB  1 
ATOM 2339 N N   . ASN A 1 327 ? 181.669 163.674 126.519 1.00 114.42 ? 327 ASN A N   1 
ATOM 2340 C CA  . ASN A 1 327 ? 182.748 163.376 125.585 1.00 114.42 ? 327 ASN A CA  1 
ATOM 2341 C C   . ASN A 1 327 ? 182.573 162.004 124.949 1.00 114.42 ? 327 ASN A C   1 
ATOM 2342 O O   . ASN A 1 327 ? 183.023 161.784 123.820 1.00 114.42 ? 327 ASN A O   1 
ATOM 2343 C CB  . ASN A 1 327 ? 184.097 163.463 126.297 1.00 114.42 ? 327 ASN A CB  1 
ATOM 2344 C CG  . ASN A 1 327 ? 184.235 164.722 127.128 1.00 114.42 ? 327 ASN A CG  1 
ATOM 2345 O OD1 . ASN A 1 327 ? 183.549 165.715 126.890 1.00 114.42 ? 327 ASN A OD1 1 
ATOM 2346 N ND2 . ASN A 1 327 ? 185.130 164.688 128.108 1.00 114.42 ? 327 ASN A ND2 1 
ATOM 2347 N N   . ALA A 1 328 ? 181.926 161.073 125.652 1.00 105.65 ? 328 ALA A N   1 
ATOM 2348 C CA  . ALA A 1 328 ? 181.702 159.750 125.083 1.00 105.65 ? 328 ALA A CA  1 
ATOM 2349 C C   . ALA A 1 328 ? 180.822 159.817 123.843 1.00 105.65 ? 328 ALA A C   1 
ATOM 2350 O O   . ALA A 1 328 ? 180.971 158.995 122.932 1.00 105.65 ? 328 ALA A O   1 
ATOM 2351 C CB  . ALA A 1 328 ? 181.074 158.828 126.127 1.00 105.65 ? 328 ALA A CB  1 
ATOM 2352 N N   . LEU A 1 329 ? 179.903 160.778 123.790 1.00 115.16 ? 329 LEU A N   1 
ATOM 2353 C CA  . LEU A 1 329 ? 179.035 160.969 122.636 1.00 115.16 ? 329 LEU A CA  1 
ATOM 2354 C C   . LEU A 1 329 ? 179.569 162.015 121.668 1.00 115.16 ? 329 LEU A C   1 
ATOM 2355 O O   . LEU A 1 329 ? 178.854 162.402 120.738 1.00 115.16 ? 329 LEU A O   1 
ATOM 2356 C CB  . LEU A 1 329 ? 177.627 161.364 123.092 1.00 115.16 ? 329 LEU A CB  1 
ATOM 2357 C CG  . LEU A 1 329 ? 176.796 160.315 123.841 1.00 115.16 ? 329 LEU A CG  1 
ATOM 2358 C CD1 . LEU A 1 329 ? 176.981 158.923 123.252 1.00 115.16 ? 329 LEU A CD1 1 
ATOM 2359 C CD2 . LEU A 1 329 ? 177.136 160.311 125.318 1.00 115.16 ? 329 LEU A CD2 1 
ATOM 2360 N N   . GLY A 1 330 ? 180.799 162.482 121.863 1.00 120.02 ? 330 GLY A N   1 
ATOM 2361 C CA  . GLY A 1 330 ? 181.359 163.472 120.968 1.00 120.02 ? 330 GLY A CA  1 
ATOM 2362 C C   . GLY A 1 330 ? 180.763 164.851 121.110 1.00 120.02 ? 330 GLY A C   1 
ATOM 2363 O O   . GLY A 1 330 ? 180.823 165.641 120.164 1.00 120.02 ? 330 GLY A O   1 
ATOM 2364 N N   . SER A 1 331 ? 180.185 165.165 122.263 1.00 125.37 ? 331 SER A N   1 
ATOM 2365 C CA  . SER A 1 331 ? 179.592 166.468 122.514 1.00 125.37 ? 331 SER A CA  1 
ATOM 2366 C C   . SER A 1 331 ? 180.567 167.356 123.278 1.00 125.37 ? 331 SER A C   1 
ATOM 2367 O O   . SER A 1 331 ? 181.585 166.903 123.806 1.00 125.37 ? 331 SER A O   1 
ATOM 2368 C CB  . SER A 1 331 ? 178.283 166.320 123.295 1.00 125.37 ? 331 SER A CB  1 
ATOM 2369 O OG  . SER A 1 331 ? 177.570 167.544 123.329 1.00 125.37 ? 331 SER A OG  1 
ATOM 2370 N N   . HIS A 1 332 ? 180.241 168.645 123.323 1.00 134.10 ? 332 HIS A N   1 
ATOM 2371 C CA  . HIS A 1 332 ? 181.020 169.632 124.058 1.00 134.10 ? 332 HIS A CA  1 
ATOM 2372 C C   . HIS A 1 332 ? 180.089 170.385 124.992 1.00 134.10 ? 332 HIS A C   1 
ATOM 2373 O O   . HIS A 1 332 ? 179.044 170.884 124.561 1.00 134.10 ? 332 HIS A O   1 
ATOM 2374 C CB  . HIS A 1 332 ? 181.722 170.606 123.106 1.00 134.10 ? 332 HIS A CB  1 
ATOM 2375 C CG  . HIS A 1 332 ? 182.943 170.038 122.454 1.00 134.10 ? 332 HIS A CG  1 
ATOM 2376 N ND1 . HIS A 1 332 ? 182.991 168.756 121.950 1.00 134.10 ? 332 HIS A ND1 1 
ATOM 2377 C CD2 . HIS A 1 332 ? 184.162 170.579 122.220 1.00 134.10 ? 332 HIS A CD2 1 
ATOM 2378 C CE1 . HIS A 1 332 ? 184.187 168.531 121.436 1.00 134.10 ? 332 HIS A CE1 1 
ATOM 2379 N NE2 . HIS A 1 332 ? 184.916 169.622 121.586 1.00 134.10 ? 332 HIS A NE2 1 
ATOM 2380 N N   . LEU A 1 333 ? 180.464 170.464 126.266 1.00 122.46 ? 333 LEU A N   1 
ATOM 2381 C CA  . LEU A 1 333 ? 179.661 171.123 127.290 1.00 122.46 ? 333 LEU A CA  1 
ATOM 2382 C C   . LEU A 1 333 ? 180.408 172.356 127.778 1.00 122.46 ? 333 LEU A C   1 
ATOM 2383 O O   . LEU A 1 333 ? 181.449 172.238 128.433 1.00 122.46 ? 333 LEU A O   1 
ATOM 2384 C CB  . LEU A 1 333 ? 179.370 170.174 128.451 1.00 122.46 ? 333 LEU A CB  1 
ATOM 2385 C CG  . LEU A 1 333 ? 178.634 168.873 128.126 1.00 122.46 ? 333 LEU A CG  1 
ATOM 2386 C CD1 . LEU A 1 333 ? 178.035 168.285 129.392 1.00 122.46 ? 333 LEU A CD1 1 
ATOM 2387 C CD2 . LEU A 1 333 ? 177.554 169.088 127.078 1.00 122.46 ? 333 LEU A CD2 1 
ATOM 2388 N N   . THR A 1 334 ? 179.878 173.532 127.463 1.00 117.48 ? 334 THR A N   1 
ATOM 2389 C CA  . THR A 1 334 ? 180.419 174.754 128.036 1.00 117.48 ? 334 THR A CA  1 
ATOM 2390 C C   . THR A 1 334 ? 180.162 174.771 129.538 1.00 117.48 ? 334 THR A C   1 
ATOM 2391 O O   . THR A 1 334 ? 179.208 174.167 130.034 1.00 117.48 ? 334 THR A O   1 
ATOM 2392 C CB  . THR A 1 334 ? 179.805 175.992 127.377 1.00 117.48 ? 334 THR A CB  1 
ATOM 2393 O OG1 . THR A 1 334 ? 180.179 177.163 128.114 1.00 117.48 ? 334 THR A OG1 1 
ATOM 2394 C CG2 . THR A 1 334 ? 178.286 175.899 127.324 1.00 117.48 ? 334 THR A CG2 1 
ATOM 2395 N N   . VAL A 1 335 ? 181.033 175.473 130.265 1.00 119.28 ? 335 VAL A N   1 
ATOM 2396 C CA  . VAL A 1 335 ? 180.997 175.411 131.723 1.00 119.28 ? 335 VAL A CA  1 
ATOM 2397 C C   . VAL A 1 335 ? 179.623 175.812 132.241 1.00 119.28 ? 335 VAL A C   1 
ATOM 2398 O O   . VAL A 1 335 ? 179.094 175.200 133.176 1.00 119.28 ? 335 VAL A O   1 
ATOM 2399 C CB  . VAL A 1 335 ? 182.109 176.291 132.324 1.00 119.28 ? 335 VAL A CB  1 
ATOM 2400 C CG1 . VAL A 1 335 ? 181.866 177.763 132.014 1.00 119.28 ? 335 VAL A CG1 1 
ATOM 2401 C CG2 . VAL A 1 335 ? 182.211 176.065 133.823 1.00 119.28 ? 335 VAL A CG2 1 
ATOM 2402 N N   . GLY A 1 336 ? 179.019 176.840 131.645 1.00 123.87 ? 336 GLY A N   1 
ATOM 2403 C CA  . GLY A 1 336 ? 177.688 177.240 132.070 1.00 123.87 ? 336 GLY A CA  1 
ATOM 2404 C C   . GLY A 1 336 ? 176.661 176.148 131.845 1.00 123.87 ? 336 GLY A C   1 
ATOM 2405 O O   . GLY A 1 336 ? 175.846 175.852 132.721 1.00 123.87 ? 336 GLY A O   1 
ATOM 2406 N N   . GLN A 1 337 ? 176.692 175.528 130.664 1.00 121.33 ? 337 GLN A N   1 
ATOM 2407 C CA  . GLN A 1 337 ? 175.738 174.464 130.366 1.00 121.33 ? 337 GLN A CA  1 
ATOM 2408 C C   . GLN A 1 337 ? 175.953 173.265 131.279 1.00 121.33 ? 337 GLN A C   1 
ATOM 2409 O O   . GLN A 1 337 ? 174.991 172.699 131.809 1.00 121.33 ? 337 GLN A O   1 
ATOM 2410 C CB  . GLN A 1 337 ? 175.860 174.048 128.901 1.00 121.33 ? 337 GLN A CB  1 
ATOM 2411 C CG  . GLN A 1 337 ? 175.091 172.790 128.547 1.00 121.33 ? 337 GLN A CG  1 
ATOM 2412 C CD  . GLN A 1 337 ? 174.975 172.588 127.052 1.00 121.33 ? 337 GLN A CD  1 
ATOM 2413 O OE1 . GLN A 1 337 ? 175.977 172.576 126.336 1.00 121.33 ? 337 GLN A OE1 1 
ATOM 2414 N NE2 . GLN A 1 337 ? 173.748 172.432 126.569 1.00 121.33 ? 337 GLN A NE2 1 
ATOM 2415 N N   . GLN A 1 338 ? 177.209 172.865 131.476 1.00 113.63 ? 338 GLN A N   1 
ATOM 2416 C CA  . GLN A 1 338 ? 177.489 171.745 132.367 1.00 113.63 ? 338 GLN A CA  1 
ATOM 2417 C C   . GLN A 1 338 ? 177.054 172.062 133.790 1.00 113.63 ? 338 GLN A C   1 
ATOM 2418 O O   . GLN A 1 338 ? 176.538 171.191 134.499 1.00 113.63 ? 338 GLN A O   1 
ATOM 2419 C CB  . GLN A 1 338 ? 178.977 171.402 132.329 1.00 113.63 ? 338 GLN A CB  1 
ATOM 2420 C CG  . GLN A 1 338 ? 179.357 170.219 133.199 1.00 113.63 ? 338 GLN A CG  1 
ATOM 2421 C CD  . GLN A 1 338 ? 180.827 169.884 133.110 1.00 113.63 ? 338 GLN A CD  1 
ATOM 2422 O OE1 . GLN A 1 338 ? 181.577 170.523 132.374 1.00 113.63 ? 338 GLN A OE1 1 
ATOM 2423 N NE2 . GLN A 1 338 ? 181.250 168.877 133.862 1.00 113.63 ? 338 GLN A NE2 1 
ATOM 2424 N N   . LEU A 1 339 ? 177.256 173.307 134.224 1.00 113.37 ? 339 LEU A N   1 
ATOM 2425 C CA  . LEU A 1 339 ? 176.859 173.688 135.573 1.00 113.37 ? 339 LEU A CA  1 
ATOM 2426 C C   . LEU A 1 339 ? 175.377 173.425 135.800 1.00 113.37 ? 339 LEU A C   1 
ATOM 2427 O O   . LEU A 1 339 ? 174.988 172.879 136.838 1.00 113.37 ? 339 LEU A O   1 
ATOM 2428 C CB  . LEU A 1 339 ? 177.193 175.161 135.813 1.00 113.37 ? 339 LEU A CB  1 
ATOM 2429 C CG  . LEU A 1 339 ? 176.970 175.740 137.214 1.00 113.37 ? 339 LEU A CG  1 
ATOM 2430 C CD1 . LEU A 1 339 ? 175.509 176.118 137.437 1.00 113.37 ? 339 LEU A CD1 1 
ATOM 2431 C CD2 . LEU A 1 339 ? 177.444 174.775 138.290 1.00 113.37 ? 339 LEU A CD2 1 
ATOM 2432 N N   . THR A 1 340 ? 174.533 173.800 134.837 1.00 112.44 ? 340 THR A N   1 
ATOM 2433 C CA  . THR A 1 340 ? 173.102 173.553 134.982 1.00 112.44 ? 340 THR A CA  1 
ATOM 2434 C C   . THR A 1 340 ? 172.805 172.061 135.049 1.00 112.44 ? 340 THR A C   1 
ATOM 2435 O O   . THR A 1 340 ? 171.987 171.620 135.864 1.00 112.44 ? 340 THR A O   1 
ATOM 2436 C CB  . THR A 1 340 ? 172.332 174.190 133.826 1.00 112.44 ? 340 THR A CB  1 
ATOM 2437 O OG1 . THR A 1 340 ? 172.701 173.556 132.595 1.00 112.44 ? 340 THR A OG1 1 
ATOM 2438 C CG2 . THR A 1 340 ? 172.624 175.679 133.740 1.00 112.44 ? 340 THR A CG2 1 
ATOM 2439 N N   . ILE A 1 341 ? 173.462 171.267 134.202 1.00 104.99 ? 341 ILE A N   1 
ATOM 2440 C CA  . ILE A 1 341 ? 173.178 169.835 134.162 1.00 104.99 ? 341 ILE A CA  1 
ATOM 2441 C C   . ILE A 1 341 ? 173.461 169.201 135.517 1.00 104.99 ? 341 ILE A C   1 
ATOM 2442 O O   . ILE A 1 341 ? 172.623 168.483 136.074 1.00 104.99 ? 341 ILE A O   1 
ATOM 2443 C CB  . ILE A 1 341 ? 173.992 169.158 133.045 1.00 104.99 ? 341 ILE A CB  1 
ATOM 2444 C CG1 . ILE A 1 341 ? 173.473 169.588 131.674 1.00 104.99 ? 341 ILE A CG1 1 
ATOM 2445 C CG2 . ILE A 1 341 ? 173.922 167.648 133.182 1.00 104.99 ? 341 ILE A CG2 1 
ATOM 2446 C CD1 . ILE A 1 341 ? 174.466 169.375 130.555 1.00 104.99 ? 341 ILE A CD1 1 
ATOM 2447 N N   . VAL A 1 342 ? 174.645 169.461 136.070 1.00 108.01 ? 342 VAL A N   1 
ATOM 2448 C CA  . VAL A 1 342 ? 174.988 168.889 137.367 1.00 108.01 ? 342 VAL A CA  1 
ATOM 2449 C C   . VAL A 1 342 ? 174.167 169.542 138.471 1.00 108.01 ? 342 VAL A C   1 
ATOM 2450 O O   . VAL A 1 342 ? 173.668 168.862 139.376 1.00 108.01 ? 342 VAL A O   1 
ATOM 2451 C CB  . VAL A 1 342 ? 176.499 169.022 137.629 1.00 108.01 ? 342 VAL A CB  1 
ATOM 2452 C CG1 . VAL A 1 342 ? 176.903 170.482 137.752 1.00 108.01 ? 342 VAL A CG1 1 
ATOM 2453 C CG2 . VAL A 1 342 ? 176.888 168.252 138.878 1.00 108.01 ? 342 VAL A CG2 1 
ATOM 2454 N N   . LEU A 1 343 ? 174.008 170.865 138.416 1.00 104.68 ? 343 LEU A N   1 
ATOM 2455 C CA  . LEU A 1 343 ? 173.289 171.559 139.478 1.00 104.68 ? 343 LEU A CA  1 
ATOM 2456 C C   . LEU A 1 343 ? 171.839 171.102 139.548 1.00 104.68 ? 343 LEU A C   1 
ATOM 2457 O O   . LEU A 1 343 ? 171.303 170.880 140.640 1.00 104.68 ? 343 LEU A O   1 
ATOM 2458 C CB  . LEU A 1 343 ? 173.371 173.069 139.261 1.00 104.68 ? 343 LEU A CB  1 
ATOM 2459 C CG  . LEU A 1 343 ? 172.909 173.958 140.416 1.00 104.68 ? 343 LEU A CG  1 
ATOM 2460 C CD1 . LEU A 1 343 ? 173.573 173.557 141.722 1.00 104.68 ? 343 LEU A CD1 1 
ATOM 2461 C CD2 . LEU A 1 343 ? 173.196 175.415 140.099 1.00 104.68 ? 343 LEU A CD2 1 
ATOM 2462 N N   . THR A 1 344 ? 171.186 170.950 138.395 1.00 107.34 ? 344 THR A N   1 
ATOM 2463 C CA  . THR A 1 344 ? 169.812 170.460 138.396 1.00 107.34 ? 344 THR A CA  1 
ATOM 2464 C C   . THR A 1 344 ? 169.737 169.050 138.964 1.00 107.34 ? 344 THR A C   1 
ATOM 2465 O O   . THR A 1 344 ? 168.813 168.724 139.719 1.00 107.34 ? 344 THR A O   1 
ATOM 2466 C CB  . THR A 1 344 ? 169.233 170.495 136.982 1.00 107.34 ? 344 THR A CB  1 
ATOM 2467 O OG1 . THR A 1 344 ? 170.152 169.884 136.068 1.00 107.34 ? 344 THR A OG1 1 
ATOM 2468 C CG2 . THR A 1 344 ? 168.963 171.929 136.552 1.00 107.34 ? 344 THR A CG2 1 
ATOM 2469 N N   . ALA A 1 345 ? 170.701 168.197 138.614 1.00 103.36 ? 345 ALA A N   1 
ATOM 2470 C CA  . ALA A 1 345 ? 170.720 166.847 139.162 1.00 103.36 ? 345 ALA A CA  1 
ATOM 2471 C C   . ALA A 1 345 ? 170.839 166.877 140.679 1.00 103.36 ? 345 ALA A C   1 
ATOM 2472 O O   . ALA A 1 345 ? 170.148 166.128 141.380 1.00 103.36 ? 345 ALA A O   1 
ATOM 2473 C CB  . ALA A 1 345 ? 171.872 166.052 138.553 1.00 103.36 ? 345 ALA A CB  1 
ATOM 2474 N N   . VAL A 1 346 ? 171.711 167.737 141.205 1.00 107.51 ? 346 VAL A N   1 
ATOM 2475 C CA  . VAL A 1 346 ? 171.833 167.878 142.652 1.00 107.51 ? 346 VAL A CA  1 
ATOM 2476 C C   . VAL A 1 346 ? 170.527 168.392 143.242 1.00 107.51 ? 346 VAL A C   1 
ATOM 2477 O O   . VAL A 1 346 ? 169.997 167.834 144.210 1.00 107.51 ? 346 VAL A O   1 
ATOM 2478 C CB  . VAL A 1 346 ? 173.009 168.806 143.000 1.00 107.51 ? 346 VAL A CB  1 
ATOM 2479 C CG1 . VAL A 1 346 ? 172.975 169.181 144.472 1.00 107.51 ? 346 VAL A CG1 1 
ATOM 2480 C CG2 . VAL A 1 346 ? 174.326 168.146 142.642 1.00 107.51 ? 346 VAL A CG2 1 
ATOM 2481 N N   . LEU A 1 347 ? 169.984 169.463 142.661 1.00 108.43 ? 347 LEU A N   1 
ATOM 2482 C CA  . LEU A 1 347 ? 168.732 170.016 143.163 1.00 108.43 ? 347 LEU A CA  1 
ATOM 2483 C C   . LEU A 1 347 ? 167.593 169.019 143.009 1.00 108.43 ? 347 LEU A C   1 
ATOM 2484 O O   . LEU A 1 347 ? 166.758 168.873 143.910 1.00 108.43 ? 347 LEU A O   1 
ATOM 2485 C CB  . LEU A 1 347 ? 168.403 171.318 142.432 1.00 108.43 ? 347 LEU A CB  1 
ATOM 2486 C CG  . LEU A 1 347 ? 169.341 172.507 142.662 1.00 108.43 ? 347 LEU A CG  1 
ATOM 2487 C CD1 . LEU A 1 347 ? 168.693 173.791 142.166 1.00 108.43 ? 347 LEU A CD1 1 
ATOM 2488 C CD2 . LEU A 1 347 ? 169.737 172.641 144.125 1.00 108.43 ? 347 LEU A CD2 1 
ATOM 2489 N N   . ALA A 1 348 ? 167.543 168.317 141.877 1.00 110.59 ? 348 ALA A N   1 
ATOM 2490 C CA  . ALA A 1 348 ? 166.483 167.346 141.644 1.00 110.59 ? 348 ALA A CA  1 
ATOM 2491 C C   . ALA A 1 348 ? 166.533 166.178 142.616 1.00 110.59 ? 348 ALA A C   1 
ATOM 2492 O O   . ALA A 1 348 ? 165.548 165.441 142.720 1.00 110.59 ? 348 ALA A O   1 
ATOM 2493 C CB  . ALA A 1 348 ? 166.560 166.821 140.211 1.00 110.59 ? 348 ALA A CB  1 
ATOM 2494 N N   . SER A 1 349 ? 167.644 165.991 143.319 1.00 108.09 ? 349 SER A N   1 
ATOM 2495 C CA  . SER A 1 349 ? 167.817 164.900 144.271 1.00 108.09 ? 349 SER A CA  1 
ATOM 2496 C C   . SER A 1 349 ? 168.421 165.420 145.564 1.00 108.09 ? 349 SER A C   1 
ATOM 2497 O O   . SER A 1 349 ? 169.400 164.881 146.084 1.00 108.09 ? 349 SER A O   1 
ATOM 2498 C CB  . SER A 1 349 ? 168.684 163.800 143.678 1.00 108.09 ? 349 SER A CB  1 
ATOM 2499 O OG  . SER A 1 349 ? 169.954 164.301 143.301 1.00 108.09 ? 349 SER A OG  1 
ATOM 2500 N N   . ILE A 1 350 ? 167.845 166.500 146.095 1.00 113.30 ? 350 ILE A N   1 
ATOM 2501 C CA  . ILE A 1 350 ? 168.319 167.042 147.365 1.00 113.30 ? 350 ILE A CA  1 
ATOM 2502 C C   . ILE A 1 350 ? 168.413 165.939 148.406 1.00 113.30 ? 350 ILE A C   1 
ATOM 2503 O O   . ILE A 1 350 ? 169.288 165.968 149.279 1.00 113.30 ? 350 ILE A O   1 
ATOM 2504 C CB  . ILE A 1 350 ? 167.398 168.189 147.830 1.00 113.30 ? 350 ILE A CB  1 
ATOM 2505 C CG1 . ILE A 1 350 ? 167.736 169.477 147.076 1.00 113.30 ? 350 ILE A CG1 1 
ATOM 2506 C CG2 . ILE A 1 350 ? 167.525 168.410 149.329 1.00 113.30 ? 350 ILE A CG2 1 
ATOM 2507 C CD1 . ILE A 1 350 ? 166.594 170.470 147.022 1.00 113.30 ? 350 ILE A CD1 1 
ATOM 2508 N N   . GLY A 1 351 ? 167.521 164.951 148.332 1.00 106.71 ? 351 GLY A N   1 
ATOM 2509 C CA  . GLY A 1 351 ? 167.610 163.754 149.123 1.00 106.71 ? 351 GLY A CA  1 
ATOM 2510 C C   . GLY A 1 351 ? 168.057 162.561 148.305 1.00 106.71 ? 351 GLY A C   1 
ATOM 2511 O O   . GLY A 1 351 ? 168.708 162.692 147.260 1.00 106.71 ? 351 GLY A O   1 
ATOM 2512 N N   . THR A 1 352 ? 167.695 161.374 148.783 1.00 107.63 ? 352 THR A N   1 
ATOM 2513 C CA  . THR A 1 352 ? 167.966 160.121 148.082 1.00 107.63 ? 352 THR A CA  1 
ATOM 2514 C C   . THR A 1 352 ? 169.456 159.891 147.854 1.00 107.63 ? 352 THR A C   1 
ATOM 2515 O O   . THR A 1 352 ? 169.839 159.193 146.910 1.00 107.63 ? 352 THR A O   1 
ATOM 2516 C CB  . THR A 1 352 ? 167.233 160.066 146.737 1.00 107.63 ? 352 THR A CB  1 
ATOM 2517 O OG1 . THR A 1 352 ? 168.054 160.653 145.719 1.00 107.63 ? 352 THR A OG1 1 
ATOM 2518 C CG2 . THR A 1 352 ? 165.903 160.808 146.808 1.00 107.63 ? 352 THR A CG2 1 
ATOM 2519 N N   . ALA A 1 353 ? 170.310 160.469 148.693 1.00 99.80  ? 353 ALA A N   1 
ATOM 2520 C CA  . ALA A 1 353 ? 171.749 160.284 148.587 1.00 99.80  ? 353 ALA A CA  1 
ATOM 2521 C C   . ALA A 1 353 ? 172.275 159.186 149.499 1.00 99.80  ? 353 ALA A C   1 
ATOM 2522 O O   . ALA A 1 353 ? 173.484 158.941 149.515 1.00 99.80  ? 353 ALA A O   1 
ATOM 2523 C CB  . ALA A 1 353 ? 172.473 161.597 148.899 1.00 99.80  ? 353 ALA A CB  1 
ATOM 2524 N N   . GLY A 1 354 ? 171.405 158.523 150.256 1.00 103.35 ? 354 GLY A N   1 
ATOM 2525 C CA  . GLY A 1 354 ? 171.846 157.512 151.195 1.00 103.35 ? 354 GLY A CA  1 
ATOM 2526 C C   . GLY A 1 354 ? 171.793 156.102 150.648 1.00 103.35 ? 354 GLY A C   1 
ATOM 2527 O O   . GLY A 1 354 ? 172.368 155.183 151.239 1.00 103.35 ? 354 GLY A O   1 
ATOM 2528 N N   . VAL A 1 355 ? 171.111 155.911 149.525 1.00 97.86  ? 355 VAL A N   1 
ATOM 2529 C CA  . VAL A 1 355 ? 170.991 154.585 148.926 1.00 97.86  ? 355 VAL A CA  1 
ATOM 2530 C C   . VAL A 1 355 ? 172.328 154.207 148.301 1.00 97.86  ? 355 VAL A C   1 
ATOM 2531 O O   . VAL A 1 355 ? 173.053 155.087 147.816 1.00 97.86  ? 355 VAL A O   1 
ATOM 2532 C CB  . VAL A 1 355 ? 169.861 154.540 147.885 1.00 97.86  ? 355 VAL A CB  1 
ATOM 2533 C CG1 . VAL A 1 355 ? 168.513 154.724 148.561 1.00 97.86  ? 355 VAL A CG1 1 
ATOM 2534 C CG2 . VAL A 1 355 ? 170.074 155.596 146.810 1.00 97.86  ? 355 VAL A CG2 1 
ATOM 2535 N N   . PRO A 1 356 ? 172.701 152.931 148.294 1.00 97.86  ? 356 PRO A N   1 
ATOM 2536 C CA  . PRO A 1 356 ? 173.935 152.535 147.611 1.00 97.86  ? 356 PRO A CA  1 
ATOM 2537 C C   . PRO A 1 356 ? 173.823 152.746 146.111 1.00 97.86  ? 356 PRO A C   1 
ATOM 2538 O O   . PRO A 1 356 ? 172.745 152.639 145.522 1.00 97.86  ? 356 PRO A O   1 
ATOM 2539 C CB  . PRO A 1 356 ? 174.067 151.049 147.958 1.00 97.86  ? 356 PRO A CB  1 
ATOM 2540 C CG  . PRO A 1 356 ? 172.671 150.607 148.186 1.00 97.86  ? 356 PRO A CG  1 
ATOM 2541 C CD  . PRO A 1 356 ? 171.990 151.768 148.848 1.00 97.86  ? 356 PRO A CD  1 
ATOM 2542 N N   . GLY A 1 357 ? 174.959 153.048 145.492 1.00 103.52 ? 357 GLY A N   1 
ATOM 2543 C CA  . GLY A 1 357 ? 174.969 153.275 144.056 1.00 103.52 ? 357 GLY A CA  1 
ATOM 2544 C C   . GLY A 1 357 ? 174.058 154.403 143.625 1.00 103.52 ? 357 GLY A C   1 
ATOM 2545 O O   . GLY A 1 357 ? 173.380 154.295 142.596 1.00 103.52 ? 357 GLY A O   1 
ATOM 2546 N N   . ALA A 1 358 ? 174.022 155.489 144.399 1.00 107.25 ? 358 ALA A N   1 
ATOM 2547 C CA  . ALA A 1 358 ? 173.158 156.611 144.052 1.00 107.25 ? 358 ALA A CA  1 
ATOM 2548 C C   . ALA A 1 358 ? 173.593 157.260 142.745 1.00 107.25 ? 358 ALA A C   1 
ATOM 2549 O O   . ALA A 1 358 ? 172.752 157.650 141.928 1.00 107.25 ? 358 ALA A O   1 
ATOM 2550 C CB  . ALA A 1 358 ? 173.156 157.639 145.183 1.00 107.25 ? 358 ALA A CB  1 
ATOM 2551 N N   . GLY A 1 359 ? 174.903 157.380 142.528 1.00 108.23 ? 359 GLY A N   1 
ATOM 2552 C CA  . GLY A 1 359 ? 175.381 158.095 141.356 1.00 108.23 ? 359 GLY A CA  1 
ATOM 2553 C C   . GLY A 1 359 ? 174.869 157.499 140.060 1.00 108.23 ? 359 GLY A C   1 
ATOM 2554 O O   . GLY A 1 359 ? 174.371 158.212 139.187 1.00 108.23 ? 359 GLY A O   1 
ATOM 2555 N N   . ALA A 1 360 ? 174.975 156.177 139.920 1.00 114.80 ? 360 ALA A N   1 
ATOM 2556 C CA  . ALA A 1 360 ? 174.489 155.528 138.708 1.00 114.80 ? 360 ALA A CA  1 
ATOM 2557 C C   . ALA A 1 360 ? 172.988 155.728 138.552 1.00 114.80 ? 360 ALA A C   1 
ATOM 2558 O O   . ALA A 1 360 ? 172.501 156.051 137.463 1.00 114.80 ? 360 ALA A O   1 
ATOM 2559 C CB  . ALA A 1 360 ? 174.835 154.040 138.734 1.00 114.80 ? 360 ALA A CB  1 
ATOM 2560 N N   . ILE A 1 361 ? 172.238 155.542 139.639 1.00 118.05 ? 361 ILE A N   1 
ATOM 2561 C CA  . ILE A 1 361 ? 170.799 155.784 139.594 1.00 118.05 ? 361 ILE A CA  1 
ATOM 2562 C C   . ILE A 1 361 ? 170.522 157.256 139.333 1.00 118.05 ? 361 ILE A C   1 
ATOM 2563 O O   . ILE A 1 361 ? 169.646 157.607 138.534 1.00 118.05 ? 361 ILE A O   1 
ATOM 2564 C CB  . ILE A 1 361 ? 170.137 155.311 140.902 1.00 118.05 ? 361 ILE A CB  1 
ATOM 2565 C CG1 . ILE A 1 361 ? 170.369 153.812 141.118 1.00 118.05 ? 361 ILE A CG1 1 
ATOM 2566 C CG2 . ILE A 1 361 ? 168.649 155.625 140.885 1.00 118.05 ? 361 ILE A CG2 1 
ATOM 2567 C CD1 . ILE A 1 361 ? 169.953 152.938 139.951 1.00 118.05 ? 361 ILE A CD1 1 
ATOM 2568 N N   . MET A 1 362 ? 171.261 158.139 140.003 1.00 125.04 ? 362 MET A N   1 
ATOM 2569 C CA  . MET A 1 362 ? 171.019 159.567 139.842 1.00 125.04 ? 362 MET A CA  1 
ATOM 2570 C C   . MET A 1 362 ? 171.466 160.053 138.470 1.00 125.04 ? 362 MET A C   1 
ATOM 2571 O O   . MET A 1 362 ? 170.830 160.933 137.881 1.00 125.04 ? 362 MET A O   1 
ATOM 2572 C CB  . MET A 1 362 ? 171.731 160.348 140.944 1.00 125.04 ? 362 MET A CB  1 
ATOM 2573 C CG  . MET A 1 362 ? 170.951 160.450 142.247 1.00 125.04 ? 362 MET A CG  1 
ATOM 2574 S SD  . MET A 1 362 ? 169.262 161.052 142.038 1.00 125.04 ? 362 MET A SD  1 
ATOM 2575 C CE  . MET A 1 362 ? 169.501 162.371 140.846 1.00 125.04 ? 362 MET A CE  1 
ATOM 2576 N N   . LEU A 1 363 ? 172.562 159.505 137.948 1.00 110.96 ? 363 LEU A N   1 
ATOM 2577 C CA  . LEU A 1 363 ? 172.990 159.882 136.607 1.00 110.96 ? 363 LEU A CA  1 
ATOM 2578 C C   . LEU A 1 363 ? 171.976 159.444 135.561 1.00 110.96 ? 363 LEU A C   1 
ATOM 2579 O O   . LEU A 1 363 ? 171.854 160.081 134.510 1.00 110.96 ? 363 LEU A O   1 
ATOM 2580 C CB  . LEU A 1 363 ? 174.357 159.274 136.300 1.00 110.96 ? 363 LEU A CB  1 
ATOM 2581 C CG  . LEU A 1 363 ? 174.970 159.668 134.956 1.00 110.96 ? 363 LEU A CG  1 
ATOM 2582 C CD1 . LEU A 1 363 ? 175.715 160.986 135.073 1.00 110.96 ? 363 LEU A CD1 1 
ATOM 2583 C CD2 . LEU A 1 363 ? 175.882 158.569 134.454 1.00 110.96 ? 363 LEU A CD2 1 
ATOM 2584 N N   . ALA A 1 364 ? 171.242 158.364 135.831 1.00 118.18 ? 364 ALA A N   1 
ATOM 2585 C CA  . ALA A 1 364 ? 170.299 157.845 134.847 1.00 118.18 ? 364 ALA A CA  1 
ATOM 2586 C C   . ALA A 1 364 ? 169.280 158.904 134.451 1.00 118.18 ? 364 ALA A C   1 
ATOM 2587 O O   . ALA A 1 364 ? 169.042 159.139 133.261 1.00 118.18 ? 364 ALA A O   1 
ATOM 2588 C CB  . ALA A 1 364 ? 169.599 156.604 135.400 1.00 118.18 ? 364 ALA A CB  1 
ATOM 2589 N N   . MET A 1 365 ? 168.669 159.563 135.437 1.00 120.95 ? 365 MET A N   1 
ATOM 2590 C CA  . MET A 1 365 ? 167.679 160.584 135.120 1.00 120.95 ? 365 MET A CA  1 
ATOM 2591 C C   . MET A 1 365 ? 168.316 161.829 134.520 1.00 120.95 ? 365 MET A C   1 
ATOM 2592 O O   . MET A 1 365 ? 167.647 162.552 133.776 1.00 120.95 ? 365 MET A O   1 
ATOM 2593 C CB  . MET A 1 365 ? 166.878 160.958 136.368 1.00 120.95 ? 365 MET A CB  1 
ATOM 2594 C CG  . MET A 1 365 ? 167.704 161.541 137.493 1.00 120.95 ? 365 MET A CG  1 
ATOM 2595 S SD  . MET A 1 365 ? 167.709 163.342 137.476 1.00 120.95 ? 365 MET A SD  1 
ATOM 2596 C CE  . MET A 1 365 ? 166.248 163.685 138.449 1.00 120.95 ? 365 MET A CE  1 
ATOM 2597 N N   . VAL A 1 366 ? 169.590 162.092 134.817 1.00 111.00 ? 366 VAL A N   1 
ATOM 2598 C CA  . VAL A 1 366 ? 170.273 163.220 134.190 1.00 111.00 ? 366 VAL A CA  1 
ATOM 2599 C C   . VAL A 1 366 ? 170.303 163.034 132.681 1.00 111.00 ? 366 VAL A C   1 
ATOM 2600 O O   . VAL A 1 366 ? 170.002 163.956 131.914 1.00 111.00 ? 366 VAL A O   1 
ATOM 2601 C CB  . VAL A 1 366 ? 171.692 163.376 134.764 1.00 111.00 ? 366 VAL A CB  1 
ATOM 2602 C CG1 . VAL A 1 366 ? 172.464 164.432 133.989 1.00 111.00 ? 366 VAL A CG1 1 
ATOM 2603 C CG2 . VAL A 1 366 ? 171.627 163.730 136.235 1.00 111.00 ? 366 VAL A CG2 1 
ATOM 2604 N N   . LEU A 1 367 ? 170.664 161.832 132.232 1.00 111.68 ? 367 LEU A N   1 
ATOM 2605 C CA  . LEU A 1 367 ? 170.586 161.529 130.809 1.00 111.68 ? 367 LEU A CA  1 
ATOM 2606 C C   . LEU A 1 367 ? 169.147 161.600 130.322 1.00 111.68 ? 367 LEU A C   1 
ATOM 2607 O O   . LEU A 1 367 ? 168.876 162.104 129.227 1.00 111.68 ? 367 LEU A O   1 
ATOM 2608 C CB  . LEU A 1 367 ? 171.179 160.149 130.531 1.00 111.68 ? 367 LEU A CB  1 
ATOM 2609 C CG  . LEU A 1 367 ? 172.573 159.893 131.105 1.00 111.68 ? 367 LEU A CG  1 
ATOM 2610 C CD1 . LEU A 1 367 ? 172.907 158.414 131.052 1.00 111.68 ? 367 LEU A CD1 1 
ATOM 2611 C CD2 . LEU A 1 367 ? 173.610 160.705 130.354 1.00 111.68 ? 367 LEU A CD2 1 
ATOM 2612 N N   . HIS A 1 368 ? 168.207 161.098 131.126 1.00 113.55 ? 368 HIS A N   1 
ATOM 2613 C CA  . HIS A 1 368 ? 166.801 161.169 130.748 1.00 113.55 ? 368 HIS A CA  1 
ATOM 2614 C C   . HIS A 1 368 ? 166.335 162.614 130.639 1.00 113.55 ? 368 HIS A C   1 
ATOM 2615 O O   . HIS A 1 368 ? 165.596 162.967 129.714 1.00 113.55 ? 368 HIS A O   1 
ATOM 2616 C CB  . HIS A 1 368 ? 165.948 160.407 131.760 1.00 113.55 ? 368 HIS A CB  1 
ATOM 2617 C CG  . HIS A 1 368 ? 164.499 160.341 131.395 1.00 113.55 ? 368 HIS A CG  1 
ATOM 2618 N ND1 . HIS A 1 368 ? 164.041 159.662 130.287 1.00 113.55 ? 368 HIS A ND1 1 
ATOM 2619 C CD2 . HIS A 1 368 ? 163.405 160.871 131.991 1.00 113.55 ? 368 HIS A CD2 1 
ATOM 2620 C CE1 . HIS A 1 368 ? 162.727 159.775 130.216 1.00 113.55 ? 368 HIS A CE1 1 
ATOM 2621 N NE2 . HIS A 1 368 ? 162.316 160.504 131.238 1.00 113.55 ? 368 HIS A NE2 1 
ATOM 2622 N N   . SER A 1 369 ? 166.758 163.466 131.576 1.00 115.90 ? 369 SER A N   1 
ATOM 2623 C CA  . SER A 1 369 ? 166.358 164.868 131.526 1.00 115.90 ? 369 SER A CA  1 
ATOM 2624 C C   . SER A 1 369 ? 166.819 165.519 130.229 1.00 115.90 ? 369 SER A C   1 
ATOM 2625 O O   . SER A 1 369 ? 166.059 166.254 129.589 1.00 115.90 ? 369 SER A O   1 
ATOM 2626 C CB  . SER A 1 369 ? 166.921 165.617 132.732 1.00 115.90 ? 369 SER A CB  1 
ATOM 2627 O OG  . SER A 1 369 ? 166.533 164.991 133.942 1.00 115.90 ? 369 SER A OG  1 
ATOM 2628 N N   . VAL A 1 370 ? 168.061 165.261 129.827 1.00 107.21 ? 370 VAL A N   1 
ATOM 2629 C CA  . VAL A 1 370 ? 168.551 165.692 128.525 1.00 107.21 ? 370 VAL A CA  1 
ATOM 2630 C C   . VAL A 1 370 ? 167.985 164.736 127.486 1.00 107.21 ? 370 VAL A C   1 
ATOM 2631 O O   . VAL A 1 370 ? 167.459 163.672 127.831 1.00 107.21 ? 370 VAL A O   1 
ATOM 2632 C CB  . VAL A 1 370 ? 170.090 165.727 128.487 1.00 107.21 ? 370 VAL A CB  1 
ATOM 2633 C CG1 . VAL A 1 370 ? 170.584 166.388 127.210 1.00 107.21 ? 370 VAL A CG1 1 
ATOM 2634 C CG2 . VAL A 1 370 ? 170.634 166.453 129.708 1.00 107.21 ? 370 VAL A CG2 1 
ATOM 2635 N N   . GLY A 1 371 ? 168.075 165.103 126.211 1.00 119.34 ? 371 GLY A N   1 
ATOM 2636 C CA  . GLY A 1 371 ? 167.571 164.250 125.154 1.00 119.34 ? 371 GLY A CA  1 
ATOM 2637 C C   . GLY A 1 371 ? 168.481 163.075 124.861 1.00 119.34 ? 371 GLY A C   1 
ATOM 2638 O O   . GLY A 1 371 ? 168.846 162.839 123.706 1.00 119.34 ? 371 GLY A O   1 
ATOM 2639 N N   . LEU A 1 372 ? 168.852 162.327 125.899 1.00 118.23 ? 372 LEU A N   1 
ATOM 2640 C CA  . LEU A 1 372 ? 169.752 161.181 125.778 1.00 118.23 ? 372 LEU A CA  1 
ATOM 2641 C C   . LEU A 1 372 ? 169.137 159.991 126.500 1.00 118.23 ? 372 LEU A C   1 
ATOM 2642 O O   . LEU A 1 372 ? 169.638 159.547 127.539 1.00 118.23 ? 372 LEU A O   1 
ATOM 2643 C CB  . LEU A 1 372 ? 171.136 161.508 126.341 1.00 118.23 ? 372 LEU A CB  1 
ATOM 2644 C CG  . LEU A 1 372 ? 171.839 162.717 125.722 1.00 118.23 ? 372 LEU A CG  1 
ATOM 2645 C CD1 . LEU A 1 372 ? 173.087 163.070 126.511 1.00 118.23 ? 372 LEU A CD1 1 
ATOM 2646 C CD2 . LEU A 1 372 ? 172.182 162.453 124.266 1.00 118.23 ? 372 LEU A CD2 1 
ATOM 2647 N N   . PRO A 1 373 ? 168.044 159.447 125.973 1.00 122.90 ? 373 PRO A N   1 
ATOM 2648 C CA  . PRO A 1 373 ? 167.446 158.260 126.590 1.00 122.90 ? 373 PRO A CA  1 
ATOM 2649 C C   . PRO A 1 373 ? 168.371 157.059 126.487 1.00 122.90 ? 373 PRO A C   1 
ATOM 2650 O O   . PRO A 1 373 ? 169.206 156.960 125.586 1.00 122.90 ? 373 PRO A O   1 
ATOM 2651 C CB  . PRO A 1 373 ? 166.161 158.045 125.783 1.00 122.90 ? 373 PRO A CB  1 
ATOM 2652 C CG  . PRO A 1 373 ? 166.414 158.712 124.478 1.00 122.90 ? 373 PRO A CG  1 
ATOM 2653 C CD  . PRO A 1 373 ? 167.311 159.876 124.770 1.00 122.90 ? 373 PRO A CD  1 
ATOM 2654 N N   . LEU A 1 374 ? 168.210 156.135 127.435 1.00 129.06 ? 374 LEU A N   1 
ATOM 2655 C CA  . LEU A 1 374 ? 169.038 154.937 127.462 1.00 129.06 ? 374 LEU A CA  1 
ATOM 2656 C C   . LEU A 1 374 ? 168.773 154.011 126.284 1.00 129.06 ? 374 LEU A C   1 
ATOM 2657 O O   . LEU A 1 374 ? 169.547 153.072 126.072 1.00 129.06 ? 374 LEU A O   1 
ATOM 2658 C CB  . LEU A 1 374 ? 168.814 154.175 128.770 1.00 129.06 ? 374 LEU A CB  1 
ATOM 2659 C CG  . LEU A 1 374 ? 169.459 154.749 130.035 1.00 129.06 ? 374 LEU A CG  1 
ATOM 2660 C CD1 . LEU A 1 374 ? 170.965 154.890 129.871 1.00 129.06 ? 374 LEU A CD1 1 
ATOM 2661 C CD2 . LEU A 1 374 ? 168.835 156.085 130.406 1.00 129.06 ? 374 LEU A CD2 1 
ATOM 2662 N N   . THR A 1 375 ? 167.705 154.246 125.518 1.00 126.63 ? 375 THR A N   1 
ATOM 2663 C CA  . THR A 1 375 ? 167.417 153.390 124.373 1.00 126.63 ? 375 THR A CA  1 
ATOM 2664 C C   . THR A 1 375 ? 168.548 153.434 123.354 1.00 126.63 ? 375 THR A C   1 
ATOM 2665 O O   . THR A 1 375 ? 168.920 152.402 122.783 1.00 126.63 ? 375 THR A O   1 
ATOM 2666 C CB  . THR A 1 375 ? 166.099 153.809 123.724 1.00 126.63 ? 375 THR A CB  1 
ATOM 2667 O OG1 . THR A 1 375 ? 166.093 155.228 123.520 1.00 126.63 ? 375 THR A OG1 1 
ATOM 2668 C CG2 . THR A 1 375 ? 164.923 153.420 124.605 1.00 126.63 ? 375 THR A CG2 1 
ATOM 2669 N N   . ASP A 1 376 ? 169.104 154.613 123.111 1.00 121.86 ? 376 ASP A N   1 
ATOM 2670 C CA  . ASP A 1 376 ? 170.180 154.755 122.142 1.00 121.86 ? 376 ASP A CA  1 
ATOM 2671 C C   . ASP A 1 376 ? 171.363 153.885 122.559 1.00 121.86 ? 376 ASP A C   1 
ATOM 2672 O O   . ASP A 1 376 ? 171.852 154.026 123.690 1.00 121.86 ? 376 ASP A O   1 
ATOM 2673 C CB  . ASP A 1 376 ? 170.603 156.219 122.039 1.00 121.86 ? 376 ASP A CB  1 
ATOM 2674 C CG  . ASP A 1 376 ? 171.815 156.422 121.149 1.00 121.86 ? 376 ASP A CG  1 
ATOM 2675 O OD1 . ASP A 1 376 ? 172.198 155.482 120.423 1.00 121.86 ? 376 ASP A OD1 1 
ATOM 2676 O OD2 . ASP A 1 376 ? 172.388 157.531 121.174 1.00 121.86 ? 376 ASP A OD2 1 
ATOM 2677 N N   . PRO A 1 377 ? 171.852 152.986 121.699 1.00 128.92 ? 377 PRO A N   1 
ATOM 2678 C CA  . PRO A 1 377 ? 172.976 152.132 122.120 1.00 128.92 ? 377 PRO A CA  1 
ATOM 2679 C C   . PRO A 1 377 ? 174.203 152.920 122.538 1.00 128.92 ? 377 PRO A C   1 
ATOM 2680 O O   . PRO A 1 377 ? 174.902 152.515 123.475 1.00 128.92 ? 377 PRO A O   1 
ATOM 2681 C CB  . PRO A 1 377 ? 173.246 151.267 120.879 1.00 128.92 ? 377 PRO A CB  1 
ATOM 2682 C CG  . PRO A 1 377 ? 172.579 151.973 119.746 1.00 128.92 ? 377 PRO A CG  1 
ATOM 2683 C CD  . PRO A 1 377 ? 171.394 152.653 120.340 1.00 128.92 ? 377 PRO A CD  1 
ATOM 2684 N N   . ASN A 1 378 ? 174.490 154.038 121.869 1.00 116.49 ? 378 ASN A N   1 
ATOM 2685 C CA  . ASN A 1 378 ? 175.646 154.841 122.249 1.00 116.49 ? 378 ASN A CA  1 
ATOM 2686 C C   . ASN A 1 378 ? 175.492 155.374 123.668 1.00 116.49 ? 378 ASN A C   1 
ATOM 2687 O O   . ASN A 1 378 ? 176.429 155.312 124.473 1.00 116.49 ? 378 ASN A O   1 
ATOM 2688 C CB  . ASN A 1 378 ? 175.832 155.989 121.259 1.00 116.49 ? 378 ASN A CB  1 
ATOM 2689 C CG  . ASN A 1 378 ? 175.962 155.507 119.831 1.00 116.49 ? 378 ASN A CG  1 
ATOM 2690 O OD1 . ASN A 1 378 ? 175.065 155.708 119.013 1.00 116.49 ? 378 ASN A OD1 1 
ATOM 2691 N ND2 . ASN A 1 378 ? 177.082 154.864 119.523 1.00 116.49 ? 378 ASN A ND2 1 
ATOM 2692 N N   . VAL A 1 379 ? 174.310 155.896 123.995 1.00 117.37 ? 379 VAL A N   1 
ATOM 2693 C CA  . VAL A 1 379 ? 174.059 156.363 125.355 1.00 117.37 ? 379 VAL A CA  1 
ATOM 2694 C C   . VAL A 1 379 ? 174.153 155.200 126.333 1.00 117.37 ? 379 VAL A C   1 
ATOM 2695 O O   . VAL A 1 379 ? 174.797 155.296 127.384 1.00 117.37 ? 379 VAL A O   1 
ATOM 2696 C CB  . VAL A 1 379 ? 172.690 157.059 125.438 1.00 117.37 ? 379 VAL A CB  1 
ATOM 2697 C CG1 . VAL A 1 379 ? 172.372 157.433 126.880 1.00 117.37 ? 379 VAL A CG1 1 
ATOM 2698 C CG2 . VAL A 1 379 ? 172.666 158.283 124.532 1.00 117.37 ? 379 VAL A CG2 1 
ATOM 2699 N N   . ALA A 1 380 ? 173.513 154.079 125.997 1.00 117.80 ? 380 ALA A N   1 
ATOM 2700 C CA  . ALA A 1 380 ? 173.595 152.904 126.856 1.00 117.80 ? 380 ALA A CA  1 
ATOM 2701 C C   . ALA A 1 380 ? 175.029 152.407 126.962 1.00 117.80 ? 380 ALA A C   1 
ATOM 2702 O O   . ALA A 1 380 ? 175.490 152.045 128.050 1.00 117.80 ? 380 ALA A O   1 
ATOM 2703 C CB  . ALA A 1 380 ? 172.683 151.800 126.324 1.00 117.80 ? 380 ALA A CB  1 
ATOM 2704 N N   . ALA A 1 381 ? 175.750 152.382 125.841 1.00 109.79 ? 381 ALA A N   1 
ATOM 2705 C CA  . ALA A 1 381 ? 177.139 151.938 125.869 1.00 109.79 ? 381 ALA A CA  1 
ATOM 2706 C C   . ALA A 1 381 ? 177.978 152.835 126.768 1.00 109.79 ? 381 ALA A C   1 
ATOM 2707 O O   . ALA A 1 381 ? 178.706 152.353 127.642 1.00 109.79 ? 381 ALA A O   1 
ATOM 2708 C CB  . ALA A 1 381 ? 177.707 151.913 124.450 1.00 109.79 ? 381 ALA A CB  1 
ATOM 2709 N N   . ALA A 1 382 ? 177.886 154.151 126.569 1.00 114.30 ? 382 ALA A N   1 
ATOM 2710 C CA  . ALA A 1 382 ? 178.641 155.072 127.411 1.00 114.30 ? 382 ALA A CA  1 
ATOM 2711 C C   . ALA A 1 382 ? 178.189 154.980 128.862 1.00 114.30 ? 382 ALA A C   1 
ATOM 2712 O O   . ALA A 1 382 ? 179.019 154.937 129.778 1.00 114.30 ? 382 ALA A O   1 
ATOM 2713 C CB  . ALA A 1 382 ? 178.490 156.501 126.892 1.00 114.30 ? 382 ALA A CB  1 
ATOM 2714 N N   . TYR A 1 383 ? 176.876 154.946 129.092 1.00 111.97 ? 383 TYR A N   1 
ATOM 2715 C CA  . TYR A 1 383 ? 176.375 154.797 130.453 1.00 111.97 ? 383 TYR A CA  1 
ATOM 2716 C C   . TYR A 1 383 ? 176.773 153.449 131.038 1.00 111.97 ? 383 TYR A C   1 
ATOM 2717 O O   . TYR A 1 383 ? 177.170 153.363 132.206 1.00 111.97 ? 383 TYR A O   1 
ATOM 2718 C CB  . TYR A 1 383 ? 174.857 154.959 130.476 1.00 111.97 ? 383 TYR A CB  1 
ATOM 2719 C CG  . TYR A 1 383 ? 174.251 154.708 131.834 1.00 111.97 ? 383 TYR A CG  1 
ATOM 2720 C CD1 . TYR A 1 383 ? 174.536 155.541 132.903 1.00 111.97 ? 383 TYR A CD1 1 
ATOM 2721 C CD2 . TYR A 1 383 ? 173.395 153.638 132.049 1.00 111.97 ? 383 TYR A CD2 1 
ATOM 2722 C CE1 . TYR A 1 383 ? 173.987 155.319 134.148 1.00 111.97 ? 383 TYR A CE1 1 
ATOM 2723 C CE2 . TYR A 1 383 ? 172.840 153.407 133.291 1.00 111.97 ? 383 TYR A CE2 1 
ATOM 2724 C CZ  . TYR A 1 383 ? 173.140 154.251 134.337 1.00 111.97 ? 383 TYR A CZ  1 
ATOM 2725 O OH  . TYR A 1 383 ? 172.592 154.029 135.578 1.00 111.97 ? 383 TYR A OH  1 
ATOM 2726 N N   . ALA A 1 384 ? 176.675 152.384 130.240 1.00 114.59 ? 384 ALA A N   1 
ATOM 2727 C CA  . ALA A 1 384 ? 177.042 151.060 130.730 1.00 114.59 ? 384 ALA A CA  1 
ATOM 2728 C C   . ALA A 1 384 ? 178.475 151.046 131.237 1.00 114.59 ? 384 ALA A C   1 
ATOM 2729 O O   . ALA A 1 384 ? 178.778 150.408 132.252 1.00 114.59 ? 384 ALA A O   1 
ATOM 2730 C CB  . ALA A 1 384 ? 176.856 150.020 129.625 1.00 114.59 ? 384 ALA A CB  1 
ATOM 2731 N N   . MET A 1 385 ? 179.374 151.747 130.544 1.00 120.00 ? 385 MET A N   1 
ATOM 2732 C CA  . MET A 1 385 ? 180.751 151.841 131.012 1.00 120.00 ? 385 MET A CA  1 
ATOM 2733 C C   . MET A 1 385 ? 180.809 152.501 132.382 1.00 120.00 ? 385 MET A C   1 
ATOM 2734 O O   . MET A 1 385 ? 181.537 152.048 133.272 1.00 120.00 ? 385 MET A O   1 
ATOM 2735 C CB  . MET A 1 385 ? 181.598 152.615 130.001 1.00 120.00 ? 385 MET A CB  1 
ATOM 2736 C CG  . MET A 1 385 ? 181.791 151.888 128.679 1.00 120.00 ? 385 MET A CG  1 
ATOM 2737 S SD  . MET A 1 385 ? 183.434 152.126 127.977 1.00 120.00 ? 385 MET A SD  1 
ATOM 2738 C CE  . MET A 1 385 ? 183.393 153.877 127.609 1.00 120.00 ? 385 MET A CE  1 
ATOM 2739 N N   . ILE A 1 386 ? 180.037 153.573 132.574 1.00 109.74 ? 386 ILE A N   1 
ATOM 2740 C CA  . ILE A 1 386 ? 179.984 154.222 133.880 1.00 109.74 ? 386 ILE A CA  1 
ATOM 2741 C C   . ILE A 1 386 ? 179.409 153.272 134.921 1.00 109.74 ? 386 ILE A C   1 
ATOM 2742 O O   . ILE A 1 386 ? 179.913 153.182 136.047 1.00 109.74 ? 386 ILE A O   1 
ATOM 2743 C CB  . ILE A 1 386 ? 179.170 155.526 133.797 1.00 109.74 ? 386 ILE A CB  1 
ATOM 2744 C CG1 . ILE A 1 386 ? 180.032 156.662 133.240 1.00 109.74 ? 386 ILE A CG1 1 
ATOM 2745 C CG2 . ILE A 1 386 ? 178.604 155.894 135.163 1.00 109.74 ? 386 ILE A CG2 1 
ATOM 2746 C CD1 . ILE A 1 386 ? 181.172 157.094 134.148 1.00 109.74 ? 386 ILE A CD1 1 
ATOM 2747 N N   . LEU A 1 387 ? 178.343 152.553 134.567 1.00 107.39 ? 387 LEU A N   1 
ATOM 2748 C CA  . LEU A 1 387 ? 177.750 151.613 135.510 1.00 107.39 ? 387 LEU A CA  1 
ATOM 2749 C C   . LEU A 1 387 ? 178.755 150.543 135.915 1.00 107.39 ? 387 LEU A C   1 
ATOM 2750 O O   . LEU A 1 387 ? 178.803 150.134 137.080 1.00 107.39 ? 387 LEU A O   1 
ATOM 2751 C CB  . LEU A 1 387 ? 176.503 150.975 134.899 1.00 107.39 ? 387 LEU A CB  1 
ATOM 2752 C CG  . LEU A 1 387 ? 175.383 150.634 135.883 1.00 107.39 ? 387 LEU A CG  1 
ATOM 2753 C CD1 . LEU A 1 387 ? 174.107 150.282 135.136 1.00 107.39 ? 387 LEU A CD1 1 
ATOM 2754 C CD2 . LEU A 1 387 ? 175.797 149.497 136.804 1.00 107.39 ? 387 LEU A CD2 1 
ATOM 2755 N N   . GLY A 1 388 ? 179.570 150.082 134.966 1.00 101.08 ? 388 GLY A N   1 
ATOM 2756 C CA  . GLY A 1 388 ? 180.577 149.088 135.291 1.00 101.08 ? 388 GLY A CA  1 
ATOM 2757 C C   . GLY A 1 388 ? 181.610 149.591 136.278 1.00 101.08 ? 388 GLY A C   1 
ATOM 2758 O O   . GLY A 1 388 ? 182.225 148.799 136.995 1.00 101.08 ? 388 GLY A O   1 
ATOM 2759 N N   . ILE A 1 389 ? 181.820 150.909 136.330 1.00 110.02 ? 389 ILE A N   1 
ATOM 2760 C CA  . ILE A 1 389 ? 182.785 151.499 137.254 1.00 110.02 ? 389 ILE A CA  1 
ATOM 2761 C C   . ILE A 1 389 ? 182.110 152.099 138.481 1.00 110.02 ? 389 ILE A C   1 
ATOM 2762 O O   . ILE A 1 389 ? 182.802 152.417 139.462 1.00 110.02 ? 389 ILE A O   1 
ATOM 2763 C CB  . ILE A 1 389 ? 183.650 152.566 136.539 1.00 110.02 ? 389 ILE A CB  1 
ATOM 2764 C CG1 . ILE A 1 389 ? 184.560 153.314 137.514 1.00 110.02 ? 389 ILE A CG1 1 
ATOM 2765 C CG2 . ILE A 1 389 ? 182.781 153.584 135.840 1.00 110.02 ? 389 ILE A CG2 1 
ATOM 2766 C CD1 . ILE A 1 389 ? 185.523 152.427 138.254 1.00 110.02 ? 389 ILE A CD1 1 
ATOM 2767 N N   . ASP A 1 390 ? 180.782 152.225 138.476 1.00 113.28 ? 390 ASP A N   1 
ATOM 2768 C CA  . ASP A 1 390 ? 180.091 152.871 139.586 1.00 113.28 ? 390 ASP A CA  1 
ATOM 2769 C C   . ASP A 1 390 ? 180.402 152.189 140.911 1.00 113.28 ? 390 ASP A C   1 
ATOM 2770 O O   . ASP A 1 390 ? 180.381 152.839 141.962 1.00 113.28 ? 390 ASP A O   1 
ATOM 2771 C CB  . ASP A 1 390 ? 178.583 152.862 139.321 1.00 113.28 ? 390 ASP A CB  1 
ATOM 2772 C CG  . ASP A 1 390 ? 177.759 153.123 140.568 1.00 113.28 ? 390 ASP A CG  1 
ATOM 2773 O OD1 . ASP A 1 390 ? 178.238 153.826 141.479 1.00 113.28 ? 390 ASP A OD1 1 
ATOM 2774 O OD2 . ASP A 1 390 ? 176.623 152.610 140.641 1.00 113.28 ? 390 ASP A OD2 1 
ATOM 2775 N N   . ALA A 1 391 ? 180.715 150.893 140.885 1.00 103.87 ? 391 ALA A N   1 
ATOM 2776 C CA  . ALA A 1 391 ? 180.906 150.153 142.127 1.00 103.87 ? 391 ALA A CA  1 
ATOM 2777 C C   . ALA A 1 391 ? 181.935 150.829 143.024 1.00 103.87 ? 391 ALA A C   1 
ATOM 2778 O O   . ALA A 1 391 ? 181.687 151.053 144.213 1.00 103.87 ? 391 ALA A O   1 
ATOM 2779 C CB  . ALA A 1 391 ? 181.326 148.718 141.819 1.00 103.87 ? 391 ALA A CB  1 
ATOM 2780 N N   . ILE A 1 392 ? 183.097 151.170 142.471 1.00 104.27 ? 392 ILE A N   1 
ATOM 2781 C CA  . ILE A 1 392 ? 184.132 151.802 143.282 1.00 104.27 ? 392 ILE A CA  1 
ATOM 2782 C C   . ILE A 1 392 ? 184.017 153.322 143.253 1.00 104.27 ? 392 ILE A C   1 
ATOM 2783 O O   . ILE A 1 392 ? 184.395 153.986 144.222 1.00 104.27 ? 392 ILE A O   1 
ATOM 2784 C CB  . ILE A 1 392 ? 185.535 151.356 142.840 1.00 104.27 ? 392 ILE A CB  1 
ATOM 2785 C CG1 . ILE A 1 392 ? 185.717 151.508 141.331 1.00 104.27 ? 392 ILE A CG1 1 
ATOM 2786 C CG2 . ILE A 1 392 ? 185.782 149.915 143.248 1.00 104.27 ? 392 ILE A CG2 1 
ATOM 2787 C CD1 . ILE A 1 392 ? 187.166 151.679 140.929 1.00 104.27 ? 392 ILE A CD1 1 
ATOM 2788 N N   . LEU A 1 393 ? 183.505 153.894 142.163 1.00 104.58 ? 393 LEU A N   1 
ATOM 2789 C CA  . LEU A 1 393 ? 183.297 155.337 142.127 1.00 104.58 ? 393 LEU A CA  1 
ATOM 2790 C C   . LEU A 1 393 ? 182.343 155.768 143.230 1.00 104.58 ? 393 LEU A C   1 
ATOM 2791 O O   . LEU A 1 393 ? 182.591 156.752 143.936 1.00 104.58 ? 393 LEU A O   1 
ATOM 2792 C CB  . LEU A 1 393 ? 182.757 155.758 140.758 1.00 104.58 ? 393 LEU A CB  1 
ATOM 2793 C CG  . LEU A 1 393 ? 183.695 156.444 139.762 1.00 104.58 ? 393 LEU A CG  1 
ATOM 2794 C CD1 . LEU A 1 393 ? 182.874 157.193 138.730 1.00 104.58 ? 393 LEU A CD1 1 
ATOM 2795 C CD2 . LEU A 1 393 ? 184.667 157.396 140.438 1.00 104.58 ? 393 LEU A CD2 1 
ATOM 2796 N N   . ASP A 1 394 ? 181.242 155.035 143.399 1.00 113.83 ? 394 ASP A N   1 
ATOM 2797 C CA  . ASP A 1 394 ? 180.305 155.341 144.470 1.00 113.83 ? 394 ASP A CA  1 
ATOM 2798 C C   . ASP A 1 394 ? 180.854 154.947 145.834 1.00 113.83 ? 394 ASP A C   1 
ATOM 2799 O O   . ASP A 1 394 ? 180.417 155.501 146.847 1.00 113.83 ? 394 ASP A O   1 
ATOM 2800 C CB  . ASP A 1 394 ? 178.973 154.638 144.209 1.00 113.83 ? 394 ASP A CB  1 
ATOM 2801 C CG  . ASP A 1 394 ? 178.126 154.516 145.453 1.00 113.83 ? 394 ASP A CG  1 
ATOM 2802 O OD1 . ASP A 1 394 ? 178.376 153.592 146.251 1.00 113.83 ? 394 ASP A OD1 1 
ATOM 2803 O OD2 . ASP A 1 394 ? 177.210 155.344 145.635 1.00 113.83 ? 394 ASP A OD2 1 
ATOM 2804 N N   . MET A 1 395 ? 181.803 154.011 145.882 1.00 103.03 ? 395 MET A N   1 
ATOM 2805 C CA  . MET A 1 395 ? 182.436 153.665 147.150 1.00 103.03 ? 395 MET A CA  1 
ATOM 2806 C C   . MET A 1 395 ? 183.078 154.892 147.780 1.00 103.03 ? 395 MET A C   1 
ATOM 2807 O O   . MET A 1 395 ? 182.885 155.171 148.968 1.00 103.03 ? 395 MET A O   1 
ATOM 2808 C CB  . MET A 1 395 ? 183.479 152.570 146.925 1.00 103.03 ? 395 MET A CB  1 
ATOM 2809 C CG  . MET A 1 395 ? 183.669 151.633 148.100 1.00 103.03 ? 395 MET A CG  1 
ATOM 2810 S SD  . MET A 1 395 ? 184.328 150.031 147.605 1.00 103.03 ? 395 MET A SD  1 
ATOM 2811 C CE  . MET A 1 395 ? 182.815 149.103 147.375 1.00 103.03 ? 395 MET A CE  1 
ATOM 2812 N N   . GLY A 1 396 ? 183.850 155.640 146.992 1.00 115.49 ? 396 GLY A N   1 
ATOM 2813 C CA  . GLY A 1 396 ? 184.419 156.879 147.492 1.00 115.49 ? 396 GLY A CA  1 
ATOM 2814 C C   . GLY A 1 396 ? 183.364 157.936 147.757 1.00 115.49 ? 396 GLY A C   1 
ATOM 2815 O O   . GLY A 1 396 ? 183.478 158.716 148.705 1.00 115.49 ? 396 GLY A O   1 
ATOM 2816 N N   . ARG A 1 397 ? 182.322 157.975 146.923 1.00 109.75 ? 397 ARG A N   1 
ATOM 2817 C CA  . ARG A 1 397 ? 181.265 158.965 147.095 1.00 109.75 ? 397 ARG A CA  1 
ATOM 2818 C C   . ARG A 1 397 ? 180.727 158.946 148.518 1.00 109.75 ? 397 ARG A C   1 
ATOM 2819 O O   . ARG A 1 397 ? 180.567 159.995 149.151 1.00 109.75 ? 397 ARG A O   1 
ATOM 2820 C CB  . ARG A 1 397 ? 180.142 158.700 146.092 1.00 109.75 ? 397 ARG A CB  1 
ATOM 2821 C CG  . ARG A 1 397 ? 178.968 159.662 146.186 1.00 109.75 ? 397 ARG A CG  1 
ATOM 2822 C CD  . ARG A 1 397 ? 177.713 159.065 145.573 1.00 109.75 ? 397 ARG A CD  1 
ATOM 2823 N NE  . ARG A 1 397 ? 177.286 157.854 146.264 1.00 109.75 ? 397 ARG A NE  1 
ATOM 2824 C CZ  . ARG A 1 397 ? 176.550 157.836 147.367 1.00 109.75 ? 397 ARG A CZ  1 
ATOM 2825 N NH1 . ARG A 1 397 ? 176.143 158.953 147.947 1.00 109.75 ? 397 ARG A NH1 1 
ATOM 2826 N NH2 . ARG A 1 397 ? 176.215 156.666 147.903 1.00 109.75 ? 397 ARG A NH2 1 
ATOM 2827 N N   . THR A 1 398 ? 180.444 157.753 149.041 1.00 103.74 ? 398 THR A N   1 
ATOM 2828 C CA  . THR A 1 398 ? 179.940 157.658 150.405 1.00 103.74 ? 398 THR A CA  1 
ATOM 2829 C C   . THR A 1 398 ? 180.968 158.145 151.415 1.00 103.74 ? 398 THR A C   1 
ATOM 2830 O O   . THR A 1 398 ? 180.599 158.581 152.511 1.00 103.74 ? 398 THR A O   1 
ATOM 2831 C CB  . THR A 1 398 ? 179.537 156.218 150.714 1.00 103.74 ? 398 THR A CB  1 
ATOM 2832 O OG1 . THR A 1 398 ? 178.617 155.754 149.719 1.00 103.74 ? 398 THR A OG1 1 
ATOM 2833 C CG2 . THR A 1 398 ? 178.881 156.130 152.081 1.00 103.74 ? 398 THR A CG2 1 
ATOM 2834 N N   . MET A 1 399 ? 182.255 158.082 151.070 1.00 113.66 ? 399 MET A N   1 
ATOM 2835 C CA  . MET A 1 399 ? 183.287 158.540 151.993 1.00 113.66 ? 399 MET A CA  1 
ATOM 2836 C C   . MET A 1 399 ? 183.119 160.021 152.305 1.00 113.66 ? 399 MET A C   1 
ATOM 2837 O O   . MET A 1 399 ? 183.093 160.423 153.474 1.00 113.66 ? 399 MET A O   1 
ATOM 2838 C CB  . MET A 1 399 ? 184.669 158.267 151.402 1.00 113.66 ? 399 MET A CB  1 
ATOM 2839 C CG  . MET A 1 399 ? 185.784 158.192 152.429 1.00 113.66 ? 399 MET A CG  1 
ATOM 2840 S SD  . MET A 1 399 ? 187.249 157.367 151.779 1.00 113.66 ? 399 MET A SD  1 
ATOM 2841 C CE  . MET A 1 399 ? 188.321 157.383 153.213 1.00 113.66 ? 399 MET A CE  1 
ATOM 2842 N N   . VAL A 1 400 ? 183.001 160.851 151.268 1.00 103.51 ? 400 VAL A N   1 
ATOM 2843 C CA  . VAL A 1 400 ? 182.812 162.280 151.491 1.00 103.51 ? 400 VAL A CA  1 
ATOM 2844 C C   . VAL A 1 400 ? 181.422 162.555 152.047 1.00 103.51 ? 400 VAL A C   1 
ATOM 2845 O O   . VAL A 1 400 ? 181.248 163.411 152.922 1.00 103.51 ? 400 VAL A O   1 
ATOM 2846 C CB  . VAL A 1 400 ? 183.072 163.069 150.195 1.00 103.51 ? 400 VAL A CB  1 
ATOM 2847 C CG1 . VAL A 1 400 ? 184.546 163.020 149.836 1.00 103.51 ? 400 VAL A CG1 1 
ATOM 2848 C CG2 . VAL A 1 400 ? 182.223 162.540 149.049 1.00 103.51 ? 400 VAL A CG2 1 
ATOM 2849 N N   . ASN A 1 401 ? 180.411 161.838 151.555 1.00 105.87 ? 401 ASN A N   1 
ATOM 2850 C CA  . ASN A 1 401 ? 179.050 162.057 152.033 1.00 105.87 ? 401 ASN A CA  1 
ATOM 2851 C C   . ASN A 1 401 ? 178.949 161.787 153.527 1.00 105.87 ? 401 ASN A C   1 
ATOM 2852 O O   . ASN A 1 401 ? 178.356 162.573 154.274 1.00 105.87 ? 401 ASN A O   1 
ATOM 2853 C CB  . ASN A 1 401 ? 178.074 161.171 151.261 1.00 105.87 ? 401 ASN A CB  1 
ATOM 2854 C CG  . ASN A 1 401 ? 177.288 161.939 150.223 1.00 105.87 ? 401 ASN A CG  1 
ATOM 2855 O OD1 . ASN A 1 401 ? 177.820 162.825 149.558 1.00 105.87 ? 401 ASN A OD1 1 
ATOM 2856 N ND2 . ASN A 1 401 ? 176.014 161.600 150.075 1.00 105.87 ? 401 ASN A ND2 1 
ATOM 2857 N N   . VAL A 1 402 ? 179.529 160.675 153.985 1.00 99.19  ? 402 VAL A N   1 
ATOM 2858 C CA  . VAL A 1 402 ? 179.502 160.347 155.408 1.00 99.19  ? 402 VAL A CA  1 
ATOM 2859 C C   . VAL A 1 402 ? 180.599 161.052 156.184 1.00 99.19  ? 402 VAL A C   1 
ATOM 2860 O O   . VAL A 1 402 ? 180.582 161.031 157.420 1.00 99.19  ? 402 VAL A O   1 
ATOM 2861 C CB  . VAL A 1 402 ? 179.611 158.825 155.610 1.00 99.19  ? 402 VAL A CB  1 
ATOM 2862 C CG1 . VAL A 1 402 ? 179.555 158.474 157.088 1.00 99.19  ? 402 VAL A CG1 1 
ATOM 2863 C CG2 . VAL A 1 402 ? 178.500 158.118 154.851 1.00 99.19  ? 402 VAL A CG2 1 
ATOM 2864 N N   . THR A 1 403 ? 181.557 161.672 155.500 1.00 95.27  ? 403 THR A N   1 
ATOM 2865 C CA  . THR A 1 403 ? 182.502 162.553 156.170 1.00 95.27  ? 403 THR A CA  1 
ATOM 2866 C C   . THR A 1 403 ? 181.967 163.975 156.261 1.00 95.27  ? 403 THR A C   1 
ATOM 2867 O O   . THR A 1 403 ? 182.194 164.661 157.263 1.00 95.27  ? 403 THR A O   1 
ATOM 2868 C CB  . THR A 1 403 ? 183.843 162.551 155.435 1.00 95.27  ? 403 THR A CB  1 
ATOM 2869 O OG1 . THR A 1 403 ? 184.291 161.203 155.259 1.00 95.27  ? 403 THR A OG1 1 
ATOM 2870 C CG2 . THR A 1 403 ? 184.884 163.329 156.223 1.00 95.27  ? 403 THR A CG2 1 
ATOM 2871 N N   . GLY A 1 404 ? 181.253 164.429 155.230 1.00 103.91 ? 404 GLY A N   1 
ATOM 2872 C CA  . GLY A 1 404 ? 180.708 165.775 155.260 1.00 103.91 ? 404 GLY A CA  1 
ATOM 2873 C C   . GLY A 1 404 ? 179.680 165.958 156.358 1.00 103.91 ? 404 GLY A C   1 
ATOM 2874 O O   . GLY A 1 404 ? 179.719 166.937 157.107 1.00 103.91 ? 404 GLY A O   1 
ATOM 2875 N N   . ASP A 1 405 ? 178.745 165.013 156.473 1.00 104.22 ? 405 ASP A N   1 
ATOM 2876 C CA  . ASP A 1 405 ? 177.742 165.110 157.528 1.00 104.22 ? 405 ASP A CA  1 
ATOM 2877 C C   . ASP A 1 405 ? 178.393 165.031 158.901 1.00 104.22 ? 405 ASP A C   1 
ATOM 2878 O O   . ASP A 1 405 ? 177.946 165.689 159.848 1.00 104.22 ? 405 ASP A O   1 
ATOM 2879 C CB  . ASP A 1 405 ? 176.690 164.015 157.365 1.00 104.22 ? 405 ASP A CB  1 
ATOM 2880 C CG  . ASP A 1 405 ? 177.298 162.661 157.111 1.00 104.22 ? 405 ASP A CG  1 
ATOM 2881 O OD1 . ASP A 1 405 ? 178.484 162.479 157.446 1.00 104.22 ? 405 ASP A OD1 1 
ATOM 2882 O OD2 . ASP A 1 405 ? 176.594 161.782 156.573 1.00 104.22 ? 405 ASP A OD2 1 
ATOM 2883 N N   . LEU A 1 406 ? 179.454 164.232 159.030 1.00 95.62  ? 406 LEU A N   1 
ATOM 2884 C CA  . LEU A 1 406 ? 180.228 164.245 160.266 1.00 95.62  ? 406 LEU A CA  1 
ATOM 2885 C C   . LEU A 1 406 ? 180.806 165.628 160.521 1.00 95.62  ? 406 LEU A C   1 
ATOM 2886 O O   . LEU A 1 406 ? 180.749 166.137 161.646 1.00 95.62  ? 406 LEU A O   1 
ATOM 2887 C CB  . LEU A 1 406 ? 181.346 163.207 160.200 1.00 95.62  ? 406 LEU A CB  1 
ATOM 2888 C CG  . LEU A 1 406 ? 181.046 161.867 160.865 1.00 95.62  ? 406 LEU A CG  1 
ATOM 2889 C CD1 . LEU A 1 406 ? 181.036 162.012 162.375 1.00 95.62  ? 406 LEU A CD1 1 
ATOM 2890 C CD2 . LEU A 1 406 ? 179.723 161.328 160.371 1.00 95.62  ? 406 LEU A CD2 1 
ATOM 2891 N N   . THR A 1 407 ? 181.364 166.254 159.485 1.00 91.35  ? 407 THR A N   1 
ATOM 2892 C CA  . THR A 1 407 ? 181.843 167.623 159.623 1.00 91.35  ? 407 THR A CA  1 
ATOM 2893 C C   . THR A 1 407 ? 180.695 168.564 159.959 1.00 91.35  ? 407 THR A C   1 
ATOM 2894 O O   . THR A 1 407 ? 180.780 169.353 160.906 1.00 91.35  ? 407 THR A O   1 
ATOM 2895 C CB  . THR A 1 407 ? 182.540 168.060 158.338 1.00 91.35  ? 407 THR A CB  1 
ATOM 2896 O OG1 . THR A 1 407 ? 183.847 167.477 158.282 1.00 91.35  ? 407 THR A OG1 1 
ATOM 2897 C CG2 . THR A 1 407 ? 182.653 169.576 158.271 1.00 91.35  ? 407 THR A CG2 1 
ATOM 2898 N N   . GLY A 1 408 ? 179.601 168.482 159.202 1.00 94.95  ? 408 GLY A N   1 
ATOM 2899 C CA  . GLY A 1 408 ? 178.462 169.337 159.483 1.00 94.95  ? 408 GLY A CA  1 
ATOM 2900 C C   . GLY A 1 408 ? 177.955 169.167 160.900 1.00 94.95  ? 408 GLY A C   1 
ATOM 2901 O O   . GLY A 1 408 ? 177.649 170.146 161.584 1.00 94.95  ? 408 GLY A O   1 
ATOM 2902 N N   . THR A 1 409 ? 177.870 167.921 161.366 1.00 90.83  ? 409 THR A N   1 
ATOM 2903 C CA  . THR A 1 409 ? 177.463 167.682 162.744 1.00 90.83  ? 409 THR A CA  1 
ATOM 2904 C C   . THR A 1 409 ? 178.445 168.318 163.717 1.00 90.83  ? 409 THR A C   1 
ATOM 2905 O O   . THR A 1 409 ? 178.038 168.937 164.707 1.00 90.83  ? 409 THR A O   1 
ATOM 2906 C CB  . THR A 1 409 ? 177.350 166.182 163.003 1.00 90.83  ? 409 THR A CB  1 
ATOM 2907 O OG1 . THR A 1 409 ? 176.536 165.582 161.988 1.00 90.83  ? 409 THR A OG1 1 
ATOM 2908 C CG2 . THR A 1 409 ? 176.729 165.923 164.361 1.00 90.83  ? 409 THR A CG2 1 
ATOM 2909 N N   . ALA A 1 410 ? 179.744 168.182 163.451 1.00 90.96  ? 410 ALA A N   1 
ATOM 2910 C CA  . ALA A 1 410 ? 180.741 168.793 164.322 1.00 90.96  ? 410 ALA A CA  1 
ATOM 2911 C C   . ALA A 1 410 ? 180.633 170.312 164.296 1.00 90.96  ? 410 ALA A C   1 
ATOM 2912 O O   . ALA A 1 410 ? 180.595 170.959 165.348 1.00 90.96  ? 410 ALA A O   1 
ATOM 2913 C CB  . ALA A 1 410 ? 182.141 168.345 163.907 1.00 90.96  ? 410 ALA A CB  1 
ATOM 2914 N N   . ILE A 1 411 ? 180.572 170.900 163.100 1.00 88.94  ? 411 ILE A N   1 
ATOM 2915 C CA  . ILE A 1 411 ? 180.495 172.355 162.994 1.00 88.94  ? 411 ILE A CA  1 
ATOM 2916 C C   . ILE A 1 411 ? 179.215 172.864 163.641 1.00 88.94  ? 411 ILE A C   1 
ATOM 2917 O O   . ILE A 1 411 ? 179.226 173.843 164.396 1.00 88.94  ? 411 ILE A O   1 
ATOM 2918 C CB  . ILE A 1 411 ? 180.590 172.794 161.521 1.00 88.94  ? 411 ILE A CB  1 
ATOM 2919 C CG1 . ILE A 1 411 ? 181.896 172.311 160.880 1.00 88.94  ? 411 ILE A CG1 1 
ATOM 2920 C CG2 . ILE A 1 411 ? 180.476 174.305 161.417 1.00 88.94  ? 411 ILE A CG2 1 
ATOM 2921 C CD1 . ILE A 1 411 ? 183.092 172.298 161.806 1.00 88.94  ? 411 ILE A CD1 1 
ATOM 2922 N N   . VAL A 1 412 ? 178.091 172.205 163.357 1.00 88.78  ? 412 VAL A N   1 
ATOM 2923 C CA  . VAL A 1 412 ? 176.826 172.620 163.955 1.00 88.78  ? 412 VAL A CA  1 
ATOM 2924 C C   . VAL A 1 412 ? 176.915 172.552 165.472 1.00 88.78  ? 412 VAL A C   1 
ATOM 2925 O O   . VAL A 1 412 ? 176.394 173.421 166.181 1.00 88.78  ? 412 VAL A O   1 
ATOM 2926 C CB  . VAL A 1 412 ? 175.672 171.758 163.414 1.00 88.78  ? 412 VAL A CB  1 
ATOM 2927 C CG1 . VAL A 1 412 ? 174.425 171.960 164.252 1.00 88.78  ? 412 VAL A CG1 1 
ATOM 2928 C CG2 . VAL A 1 412 ? 175.398 172.099 161.962 1.00 88.78  ? 412 VAL A CG2 1 
ATOM 2929 N N   . ALA A 1 413 ? 177.578 171.521 165.996 1.00 87.63  ? 413 ALA A N   1 
ATOM 2930 C CA  . ALA A 1 413 ? 177.800 171.423 167.431 1.00 87.63  ? 413 ALA A CA  1 
ATOM 2931 C C   . ALA A 1 413 ? 178.726 172.511 167.954 1.00 87.63  ? 413 ALA A C   1 
ATOM 2932 O O   . ALA A 1 413 ? 178.808 172.694 169.173 1.00 87.63  ? 413 ALA A O   1 
ATOM 2933 C CB  . ALA A 1 413 ? 178.375 170.050 167.778 1.00 87.63  ? 413 ALA A CB  1 
ATOM 2934 N N   . LYS A 1 414 ? 179.420 173.226 167.075 1.00 83.86  ? 414 LYS A N   1 
ATOM 2935 C CA  . LYS A 1 414 ? 180.316 174.300 167.486 1.00 83.86  ? 414 LYS A CA  1 
ATOM 2936 C C   . LYS A 1 414 ? 181.426 173.761 168.378 1.00 83.86  ? 414 LYS A C   1 
ATOM 2937 O O   . LYS A 1 414 ? 182.595 174.105 168.207 1.00 83.86  ? 414 LYS A O   1 
ATOM 2938 C CB  . LYS A 1 414 ? 179.542 175.401 168.216 1.00 83.86  ? 414 LYS A CB  1 
ATOM 2939 C CG  . LYS A 1 414 ? 178.350 175.949 167.445 1.00 83.86  ? 414 LYS A CG  1 
ATOM 2940 C CD  . LYS A 1 414 ? 177.295 176.503 168.387 1.00 83.86  ? 414 LYS A CD  1 
ATOM 2941 C CE  . LYS A 1 414 ? 176.433 175.392 168.967 1.00 83.86  ? 414 LYS A CE  1 
ATOM 2942 N NZ  . LYS A 1 414 ? 175.676 175.836 170.170 1.00 83.86  ? 414 LYS A NZ  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
574  N N   . ALA A 76  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 76  ALA A N   
575  C CA  . ALA A 76  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 76  ALA A CA  
576  C C   . ALA A 76  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 76  ALA A C   
577  O O   . ALA A 76  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 76  ALA A O   
578  C CB  . ALA A 76  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 76  ALA A CB  
579  N N   . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A N   
580  C CA  . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A CA  
581  C C   . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A C   
582  O O   . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A O   
583  C CB  . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A CB  
584  C CG  . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A CG  
585  C CD  . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A CD  
586  N NE  . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A NE  
587  C CZ  . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A CZ  
588  N NH1 . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A NH1 
589  N NH2 . ARG A 77  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 77  ARG A NH2 
590  N N   . LEU A 78  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 78  LEU A N   
591  C CA  . LEU A 78  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 78  LEU A CA  
592  C C   . LEU A 78  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 78  LEU A C   
593  O O   . LEU A 78  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 78  LEU A O   
594  C CB  . LEU A 78  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 78  LEU A CB  
595  C CG  . LEU A 78  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 78  LEU A CG  
596  C CD1 . LEU A 78  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 78  LEU A CD1 
597  C CD2 . LEU A 78  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 78  LEU A CD2 
598  N N   . GLY A 79  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 79  GLY A N   
599  C CA  . GLY A 79  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 79  GLY A CA  
600  C C   . GLY A 79  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 79  GLY A C   
601  O O   . GLY A 79  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 79  GLY A O   
602  N N   . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A N   
603  C CA  . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A CA  
604  C C   . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A C   
605  O O   . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A O   
606  C CB  . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A CB  
607  C CG  . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A CG  
608  C CD  . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A CD  
609  N NE  . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A NE  
610  C CZ  . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A CZ  
611  N NH1 . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A NH1 
612  N NH2 . ARG A 80  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 80  ARG A NH2 
613  N N   . VAL A 81  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 81  VAL A N   
614  C CA  . VAL A 81  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 81  VAL A CA  
615  C C   . VAL A 81  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 81  VAL A C   
616  O O   . VAL A 81  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 81  VAL A O   
617  C CB  . VAL A 81  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 81  VAL A CB  
618  C CG1 . VAL A 81  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 81  VAL A CG1 
619  C CG2 . VAL A 81  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 81  VAL A CG2 
620  N N   . GLY A 82  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 82  GLY A N   
621  C CA  . GLY A 82  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 82  GLY A CA  
622  C C   . GLY A 82  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 82  GLY A C   
623  O O   . GLY A 82  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 82  GLY A O   
624  N N   . VAL A 83  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 83  VAL A N   
625  C CA  . VAL A 83  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 83  VAL A CA  
626  C C   . VAL A 83  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 83  VAL A C   
627  O O   . VAL A 83  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 83  VAL A O   
628  C CB  . VAL A 83  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 83  VAL A CB  
629  C CG1 . VAL A 83  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 83  VAL A CG1 
630  C CG2 . VAL A 83  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 83  VAL A CG2 
631  N N   . LYS A 84  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 84  LYS A N   
632  C CA  . LYS A 84  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 84  LYS A CA  
633  C C   . LYS A 84  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 84  LYS A C   
634  O O   . LYS A 84  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 84  LYS A O   
635  C CB  . LYS A 84  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 84  LYS A CB  
636  C CG  . LYS A 84  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 84  LYS A CG  
637  C CD  . LYS A 84  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 84  LYS A CD  
638  C CE  . LYS A 84  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 84  LYS A CE  
639  N NZ  . LYS A 84  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 84  LYS A NZ  
640  N N   . ILE A 85  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 85  ILE A N   
641  C CA  . ILE A 85  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 85  ILE A CA  
642  C C   . ILE A 85  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 85  ILE A C   
643  O O   . ILE A 85  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 85  ILE A O   
644  C CB  . ILE A 85  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 85  ILE A CB  
645  C CG1 . ILE A 85  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 85  ILE A CG1 
646  C CG2 . ILE A 85  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 85  ILE A CG2 
647  C CD1 . ILE A 85  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 85  ILE A CD1 
648  N N   . VAL A 86  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 86  VAL A N   
649  C CA  . VAL A 86  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 86  VAL A CA  
650  C C   . VAL A 86  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 86  VAL A C   
651  O O   . VAL A 86  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 86  VAL A O   
652  C CB  . VAL A 86  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 86  VAL A CB  
653  C CG1 . VAL A 86  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 86  VAL A CG1 
654  C CG2 . VAL A 86  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 86  VAL A CG2 
655  N N   . VAL A 87  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 87  VAL A N   
656  C CA  . VAL A 87  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 87  VAL A CA  
657  C C   . VAL A 87  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 87  VAL A C   
658  O O   . VAL A 87  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 87  VAL A O   
659  C CB  . VAL A 87  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 87  VAL A CB  
660  C CG1 . VAL A 87  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 87  VAL A CG1 
661  C CG2 . VAL A 87  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 87  VAL A CG2 
662  N N   . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A N   
663  C CA  . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A CA  
664  C C   . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A C   
665  O O   . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A O   
666  C CB  . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A CB  
667  C CG  . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A CG  
668  C CD1 . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A CD1 
669  C CD2 . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A CD2 
670  C CE1 . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A CE1 
671  C CE2 . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A CE2 
672  C CZ  . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A CZ  
673  O OH  . TYR A 88  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 88  TYR A OH  
674  N N   . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A N   
675  C CA  . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A CA  
676  C C   . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A C   
677  O O   . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A O   
678  C CB  . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A CB  
679  C CG  . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A CG  
680  C CD1 . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A CD1 
681  C CD2 . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A CD2 
682  C CE1 . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A CE1 
683  C CE2 . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A CE2 
684  C CZ  . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A CZ  
685  O OH  . TYR A 89  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 89  TYR A OH  
686  N N   . LEU A 90  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 90  LEU A N   
687  C CA  . LEU A 90  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 90  LEU A CA  
688  C C   . LEU A 90  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 90  LEU A C   
689  O O   . LEU A 90  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 90  LEU A O   
690  C CB  . LEU A 90  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 90  LEU A CB  
691  C CG  . LEU A 90  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 90  LEU A CG  
692  C CD1 . LEU A 90  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 90  LEU A CD1 
693  C CD2 . LEU A 90  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 90  LEU A CD2 
694  N N   . LEU A 91  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 91  LEU A N   
695  C CA  . LEU A 91  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 91  LEU A CA  
696  C C   . LEU A 91  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 91  LEU A C   
697  O O   . LEU A 91  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 91  LEU A O   
698  C CB  . LEU A 91  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 91  LEU A CB  
699  C CG  . LEU A 91  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 91  LEU A CG  
700  C CD1 . LEU A 91  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 91  LEU A CD1 
701  C CD2 . LEU A 91  ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 91  LEU A CD2 
702  N N   . THR A 92  ? 1.2870 1.2870 1.2870 0.0000  0.0000  -0.0000 92  THR A N   
703  C CA  . THR A 92  ? 1.2870 1.2870 1.2870 0.0000  0.0000  -0.0000 92  THR A CA  
704  C C   . THR A 92  ? 1.2870 1.2870 1.2870 0.0000  0.0000  -0.0000 92  THR A C   
705  O O   . THR A 92  ? 1.2870 1.2870 1.2870 0.0000  0.0000  -0.0000 92  THR A O   
706  C CB  . THR A 92  ? 1.2870 1.2870 1.2870 0.0000  0.0000  -0.0000 92  THR A CB  
707  O OG1 . THR A 92  ? 1.2870 1.2870 1.2870 0.0000  0.0000  -0.0000 92  THR A OG1 
708  C CG2 . THR A 92  ? 1.2870 1.2870 1.2870 0.0000  0.0000  -0.0000 92  THR A CG2 
709  N N   . SER A 93  ? 1.3355 1.3355 1.3355 -0.0000 -0.0000 -0.0000 93  SER A N   
710  C CA  . SER A 93  ? 1.3355 1.3355 1.3355 -0.0000 -0.0000 -0.0000 93  SER A CA  
711  C C   . SER A 93  ? 1.3355 1.3355 1.3355 -0.0000 -0.0000 -0.0000 93  SER A C   
712  O O   . SER A 93  ? 1.3355 1.3355 1.3355 -0.0000 -0.0000 -0.0000 93  SER A O   
713  C CB  . SER A 93  ? 1.3355 1.3355 1.3355 -0.0000 -0.0000 -0.0000 93  SER A CB  
714  O OG  . SER A 93  ? 1.3355 1.3355 1.3355 -0.0000 -0.0000 -0.0000 93  SER A OG  
715  N N   . ALA A 94  ? 1.3652 1.3652 1.3652 0.0000  0.0000  0.0000  94  ALA A N   
716  C CA  . ALA A 94  ? 1.3652 1.3652 1.3652 0.0000  0.0000  0.0000  94  ALA A CA  
717  C C   . ALA A 94  ? 1.3652 1.3652 1.3652 0.0000  0.0000  0.0000  94  ALA A C   
718  O O   . ALA A 94  ? 1.3652 1.3652 1.3652 0.0000  0.0000  0.0000  94  ALA A O   
719  C CB  . ALA A 94  ? 1.3652 1.3652 1.3652 0.0000  0.0000  0.0000  94  ALA A CB  
720  N N   . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A N   
721  C CA  . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A CA  
722  C C   . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A C   
723  O O   . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A O   
724  C CB  . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A CB  
725  C CG  . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A CG  
726  C CD1 . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A CD1 
727  C CD2 . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A CD2 
728  C CE1 . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A CE1 
729  C CE2 . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A CE2 
730  C CZ  . PHE A 95  ? 1.2789 1.2789 1.2789 0.0000  0.0000  -0.0000 95  PHE A CZ  
731  N N   . ALA A 96  ? 1.3874 1.3874 1.3874 0.0000  -0.0000 -0.0000 96  ALA A N   
732  C CA  . ALA A 96  ? 1.3874 1.3874 1.3874 0.0000  -0.0000 -0.0000 96  ALA A CA  
733  C C   . ALA A 96  ? 1.3874 1.3874 1.3874 0.0000  -0.0000 -0.0000 96  ALA A C   
734  O O   . ALA A 96  ? 1.3874 1.3874 1.3874 0.0000  -0.0000 -0.0000 96  ALA A O   
735  C CB  . ALA A 96  ? 1.3874 1.3874 1.3874 0.0000  -0.0000 -0.0000 96  ALA A CB  
736  N N   . VAL A 97  ? 1.4131 1.4131 1.4131 0.0000  0.0000  -0.0000 97  VAL A N   
737  C CA  . VAL A 97  ? 1.4131 1.4131 1.4131 0.0000  0.0000  -0.0000 97  VAL A CA  
738  C C   . VAL A 97  ? 1.4131 1.4131 1.4131 0.0000  0.0000  -0.0000 97  VAL A C   
739  O O   . VAL A 97  ? 1.4131 1.4131 1.4131 0.0000  0.0000  -0.0000 97  VAL A O   
740  C CB  . VAL A 97  ? 1.4131 1.4131 1.4131 0.0000  0.0000  -0.0000 97  VAL A CB  
741  C CG1 . VAL A 97  ? 1.4131 1.4131 1.4131 0.0000  0.0000  -0.0000 97  VAL A CG1 
742  C CG2 . VAL A 97  ? 1.4131 1.4131 1.4131 0.0000  0.0000  -0.0000 97  VAL A CG2 
743  N N   . THR A 98  ? 1.4560 1.4560 1.4560 -0.0000 -0.0000 0.0000  98  THR A N   
744  C CA  . THR A 98  ? 1.4560 1.4560 1.4560 -0.0000 -0.0000 0.0000  98  THR A CA  
745  C C   . THR A 98  ? 1.4560 1.4560 1.4560 -0.0000 -0.0000 0.0000  98  THR A C   
746  O O   . THR A 98  ? 1.4560 1.4560 1.4560 -0.0000 -0.0000 0.0000  98  THR A O   
747  C CB  . THR A 98  ? 1.4560 1.4560 1.4560 -0.0000 -0.0000 0.0000  98  THR A CB  
748  O OG1 . THR A 98  ? 1.4560 1.4560 1.4560 -0.0000 -0.0000 0.0000  98  THR A OG1 
749  C CG2 . THR A 98  ? 1.4560 1.4560 1.4560 -0.0000 -0.0000 0.0000  98  THR A CG2 
750  N N   . LEU A 99  ? 1.3776 1.3776 1.3776 0.0000  0.0000  -0.0000 99  LEU A N   
751  C CA  . LEU A 99  ? 1.3776 1.3776 1.3776 0.0000  0.0000  -0.0000 99  LEU A CA  
752  C C   . LEU A 99  ? 1.3776 1.3776 1.3776 0.0000  0.0000  -0.0000 99  LEU A C   
753  O O   . LEU A 99  ? 1.3776 1.3776 1.3776 0.0000  0.0000  -0.0000 99  LEU A O   
754  C CB  . LEU A 99  ? 1.3776 1.3776 1.3776 0.0000  0.0000  -0.0000 99  LEU A CB  
755  C CG  . LEU A 99  ? 1.3776 1.3776 1.3776 0.0000  0.0000  -0.0000 99  LEU A CG  
756  C CD1 . LEU A 99  ? 1.3776 1.3776 1.3776 0.0000  0.0000  -0.0000 99  LEU A CD1 
757  C CD2 . LEU A 99  ? 1.3776 1.3776 1.3776 0.0000  0.0000  -0.0000 99  LEU A CD2 
758  N N   . GLY A 100 ? 1.3657 1.3657 1.3657 0.0000  0.0000  -0.0000 100 GLY A N   
759  C CA  . GLY A 100 ? 1.3657 1.3657 1.3657 0.0000  0.0000  -0.0000 100 GLY A CA  
760  C C   . GLY A 100 ? 1.3657 1.3657 1.3657 0.0000  0.0000  -0.0000 100 GLY A C   
761  O O   . GLY A 100 ? 1.3657 1.3657 1.3657 0.0000  0.0000  -0.0000 100 GLY A O   
762  N N   . ILE A 101 ? 1.3460 1.3460 1.3460 0.0000  0.0000  -0.0000 101 ILE A N   
763  C CA  . ILE A 101 ? 1.3460 1.3460 1.3460 0.0000  0.0000  -0.0000 101 ILE A CA  
764  C C   . ILE A 101 ? 1.3460 1.3460 1.3460 0.0000  0.0000  -0.0000 101 ILE A C   
765  O O   . ILE A 101 ? 1.3460 1.3460 1.3460 0.0000  0.0000  -0.0000 101 ILE A O   
766  C CB  . ILE A 101 ? 1.3460 1.3460 1.3460 0.0000  0.0000  -0.0000 101 ILE A CB  
767  C CG1 . ILE A 101 ? 1.3460 1.3460 1.3460 0.0000  0.0000  -0.0000 101 ILE A CG1 
768  C CG2 . ILE A 101 ? 1.3460 1.3460 1.3460 0.0000  0.0000  -0.0000 101 ILE A CG2 
769  C CD1 . ILE A 101 ? 1.3460 1.3460 1.3460 0.0000  0.0000  -0.0000 101 ILE A CD1 
770  N N   . ILE A 102 ? 1.3993 1.3993 1.3993 0.0000  0.0000  -0.0000 102 ILE A N   
771  C CA  . ILE A 102 ? 1.3993 1.3993 1.3993 0.0000  0.0000  -0.0000 102 ILE A CA  
772  C C   . ILE A 102 ? 1.3993 1.3993 1.3993 0.0000  0.0000  -0.0000 102 ILE A C   
773  O O   . ILE A 102 ? 1.3993 1.3993 1.3993 0.0000  0.0000  -0.0000 102 ILE A O   
774  C CB  . ILE A 102 ? 1.3993 1.3993 1.3993 0.0000  0.0000  -0.0000 102 ILE A CB  
775  C CG1 . ILE A 102 ? 1.3993 1.3993 1.3993 0.0000  0.0000  -0.0000 102 ILE A CG1 
776  C CG2 . ILE A 102 ? 1.3993 1.3993 1.3993 0.0000  0.0000  -0.0000 102 ILE A CG2 
777  C CD1 . ILE A 102 ? 1.3993 1.3993 1.3993 0.0000  0.0000  -0.0000 102 ILE A CD1 
778  N N   . MET A 103 ? 1.4179 1.4179 1.4179 0.0000  0.0000  -0.0000 103 MET A N   
779  C CA  . MET A 103 ? 1.4179 1.4179 1.4179 0.0000  0.0000  -0.0000 103 MET A CA  
780  C C   . MET A 103 ? 1.4179 1.4179 1.4179 0.0000  0.0000  -0.0000 103 MET A C   
781  O O   . MET A 103 ? 1.4179 1.4179 1.4179 0.0000  0.0000  -0.0000 103 MET A O   
782  C CB  . MET A 103 ? 1.4179 1.4179 1.4179 0.0000  0.0000  -0.0000 103 MET A CB  
783  C CG  . MET A 103 ? 1.4179 1.4179 1.4179 0.0000  0.0000  -0.0000 103 MET A CG  
784  S SD  . MET A 103 ? 1.4179 1.4179 1.4179 0.0000  0.0000  -0.0000 103 MET A SD  
785  C CE  . MET A 103 ? 1.4179 1.4179 1.4179 0.0000  0.0000  -0.0000 103 MET A CE  
786  N N   . ALA A 104 ? 1.4045 1.4045 1.4045 0.0000  0.0000  -0.0000 104 ALA A N   
787  C CA  . ALA A 104 ? 1.4045 1.4045 1.4045 0.0000  0.0000  -0.0000 104 ALA A CA  
788  C C   . ALA A 104 ? 1.4045 1.4045 1.4045 0.0000  0.0000  -0.0000 104 ALA A C   
789  O O   . ALA A 104 ? 1.4045 1.4045 1.4045 0.0000  0.0000  -0.0000 104 ALA A O   
790  C CB  . ALA A 104 ? 1.4045 1.4045 1.4045 0.0000  0.0000  -0.0000 104 ALA A CB  
791  N N   . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A N   
792  C CA  . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A CA  
793  C C   . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A C   
794  O O   . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A O   
795  C CB  . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A CB  
796  C CG  . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A CG  
797  C CD  . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A CD  
798  N NE  . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A NE  
799  C CZ  . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A CZ  
800  N NH1 . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A NH1 
801  N NH2 . ARG A 105 ? 1.3549 1.3549 1.3549 0.0000  0.0000  -0.0000 105 ARG A NH2 
802  N N   . LEU A 106 ? 1.4251 1.4251 1.4251 0.0000  0.0000  -0.0000 106 LEU A N   
803  C CA  . LEU A 106 ? 1.4251 1.4251 1.4251 0.0000  0.0000  -0.0000 106 LEU A CA  
804  C C   . LEU A 106 ? 1.4251 1.4251 1.4251 0.0000  0.0000  -0.0000 106 LEU A C   
805  O O   . LEU A 106 ? 1.4251 1.4251 1.4251 0.0000  0.0000  -0.0000 106 LEU A O   
806  C CB  . LEU A 106 ? 1.4251 1.4251 1.4251 0.0000  0.0000  -0.0000 106 LEU A CB  
807  C CG  . LEU A 106 ? 1.4251 1.4251 1.4251 0.0000  0.0000  -0.0000 106 LEU A CG  
808  C CD1 . LEU A 106 ? 1.4251 1.4251 1.4251 0.0000  0.0000  -0.0000 106 LEU A CD1 
809  C CD2 . LEU A 106 ? 1.4251 1.4251 1.4251 0.0000  0.0000  -0.0000 106 LEU A CD2 
810  N N   . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A N   
811  C CA  . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A CA  
812  C C   . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A C   
813  O O   . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A O   
814  C CB  . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A CB  
815  C CG  . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A CG  
816  C CD1 . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A CD1 
817  C CD2 . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A CD2 
818  C CE1 . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A CE1 
819  C CE2 . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A CE2 
820  C CZ  . PHE A 107 ? 1.4007 1.4007 1.4007 -0.0000 -0.0000 0.0000  107 PHE A CZ  
821  N N   . ASN A 108 ? 1.5252 1.5252 1.5252 0.0000  0.0000  -0.0000 108 ASN A N   
822  C CA  . ASN A 108 ? 1.5252 1.5252 1.5252 0.0000  0.0000  -0.0000 108 ASN A CA  
823  C C   . ASN A 108 ? 1.5252 1.5252 1.5252 0.0000  0.0000  -0.0000 108 ASN A C   
824  O O   . ASN A 108 ? 1.5252 1.5252 1.5252 0.0000  0.0000  -0.0000 108 ASN A O   
825  C CB  . ASN A 108 ? 1.5252 1.5252 1.5252 0.0000  0.0000  -0.0000 108 ASN A CB  
826  C CG  . ASN A 108 ? 1.5252 1.5252 1.5252 0.0000  0.0000  -0.0000 108 ASN A CG  
827  O OD1 . ASN A 108 ? 1.5252 1.5252 1.5252 0.0000  0.0000  -0.0000 108 ASN A OD1 
828  N ND2 . ASN A 108 ? 1.5252 1.5252 1.5252 0.0000  0.0000  -0.0000 108 ASN A ND2 
829  N N   . PRO A 109 ? 1.2819 1.2819 1.2819 0.0000  0.0000  -0.0000 109 PRO A N   
830  C CA  . PRO A 109 ? 1.2819 1.2819 1.2819 0.0000  0.0000  -0.0000 109 PRO A CA  
831  C C   . PRO A 109 ? 1.2819 1.2819 1.2819 0.0000  0.0000  -0.0000 109 PRO A C   
832  O O   . PRO A 109 ? 1.2819 1.2819 1.2819 0.0000  0.0000  -0.0000 109 PRO A O   
833  C CB  . PRO A 109 ? 1.2819 1.2819 1.2819 0.0000  0.0000  -0.0000 109 PRO A CB  
834  C CG  . PRO A 109 ? 1.2819 1.2819 1.2819 0.0000  0.0000  -0.0000 109 PRO A CG  
835  C CD  . PRO A 109 ? 1.2819 1.2819 1.2819 0.0000  0.0000  -0.0000 109 PRO A CD  
1577 N N   . GLY A 226 ? 1.7258 1.7258 1.7258 0.0000  -0.0000 0.0000  226 GLY A N   
1578 C CA  . GLY A 226 ? 1.7258 1.7258 1.7258 0.0000  -0.0000 0.0000  226 GLY A CA  
1579 C C   . GLY A 226 ? 1.7258 1.7258 1.7258 0.0000  -0.0000 0.0000  226 GLY A C   
1580 O O   . GLY A 226 ? 1.7258 1.7258 1.7258 0.0000  -0.0000 0.0000  226 GLY A O   
1581 N N   . GLU A 227 ? 1.5559 1.5559 1.5559 -0.0000 0.0000  0.0000  227 GLU A N   
1582 C CA  . GLU A 227 ? 1.5559 1.5559 1.5559 -0.0000 0.0000  0.0000  227 GLU A CA  
1583 C C   . GLU A 227 ? 1.5559 1.5559 1.5559 -0.0000 0.0000  0.0000  227 GLU A C   
1584 O O   . GLU A 227 ? 1.5559 1.5559 1.5559 -0.0000 0.0000  0.0000  227 GLU A O   
1585 C CB  . GLU A 227 ? 1.5559 1.5559 1.5559 -0.0000 0.0000  0.0000  227 GLU A CB  
1586 C CG  . GLU A 227 ? 1.5559 1.5559 1.5559 -0.0000 0.0000  0.0000  227 GLU A CG  
1587 C CD  . GLU A 227 ? 1.5559 1.5559 1.5559 -0.0000 0.0000  0.0000  227 GLU A CD  
1588 O OE1 . GLU A 227 ? 1.5559 1.5559 1.5559 -0.0000 0.0000  0.0000  227 GLU A OE1 
1589 O OE2 . GLU A 227 ? 1.5559 1.5559 1.5559 -0.0000 0.0000  0.0000  227 GLU A OE2 
1590 N N   . LEU A 228 ? 1.4847 1.4847 1.4847 0.0000  0.0000  -0.0000 228 LEU A N   
1591 C CA  . LEU A 228 ? 1.4847 1.4847 1.4847 0.0000  0.0000  -0.0000 228 LEU A CA  
1592 C C   . LEU A 228 ? 1.4847 1.4847 1.4847 0.0000  0.0000  -0.0000 228 LEU A C   
1593 O O   . LEU A 228 ? 1.4847 1.4847 1.4847 0.0000  0.0000  -0.0000 228 LEU A O   
1594 C CB  . LEU A 228 ? 1.4847 1.4847 1.4847 0.0000  0.0000  -0.0000 228 LEU A CB  
1595 C CG  . LEU A 228 ? 1.4847 1.4847 1.4847 0.0000  0.0000  -0.0000 228 LEU A CG  
1596 C CD1 . LEU A 228 ? 1.4847 1.4847 1.4847 0.0000  0.0000  -0.0000 228 LEU A CD1 
1597 C CD2 . LEU A 228 ? 1.4847 1.4847 1.4847 0.0000  0.0000  -0.0000 228 LEU A CD2 
1598 N N   . ALA A 229 ? 1.5102 1.5102 1.5102 0.0000  -0.0000 0.0000  229 ALA A N   
1599 C CA  . ALA A 229 ? 1.5102 1.5102 1.5102 0.0000  -0.0000 0.0000  229 ALA A CA  
1600 C C   . ALA A 229 ? 1.5102 1.5102 1.5102 0.0000  -0.0000 0.0000  229 ALA A C   
1601 O O   . ALA A 229 ? 1.5102 1.5102 1.5102 0.0000  -0.0000 0.0000  229 ALA A O   
1602 C CB  . ALA A 229 ? 1.5102 1.5102 1.5102 0.0000  -0.0000 0.0000  229 ALA A CB  
1603 N N   . LYS A 230 ? 1.3779 1.3779 1.3779 0.0000  0.0000  -0.0000 230 LYS A N   
1604 C CA  . LYS A 230 ? 1.3779 1.3779 1.3779 0.0000  0.0000  -0.0000 230 LYS A CA  
1605 C C   . LYS A 230 ? 1.3779 1.3779 1.3779 0.0000  0.0000  -0.0000 230 LYS A C   
1606 O O   . LYS A 230 ? 1.3779 1.3779 1.3779 0.0000  0.0000  -0.0000 230 LYS A O   
1607 C CB  . LYS A 230 ? 1.3779 1.3779 1.3779 0.0000  0.0000  -0.0000 230 LYS A CB  
1608 C CG  . LYS A 230 ? 1.3779 1.3779 1.3779 0.0000  0.0000  -0.0000 230 LYS A CG  
1609 C CD  . LYS A 230 ? 1.3779 1.3779 1.3779 0.0000  0.0000  -0.0000 230 LYS A CD  
1610 C CE  . LYS A 230 ? 1.3779 1.3779 1.3779 0.0000  0.0000  -0.0000 230 LYS A CE  
1611 N NZ  . LYS A 230 ? 1.3779 1.3779 1.3779 0.0000  0.0000  -0.0000 230 LYS A NZ  
1612 N N   . VAL A 231 ? 1.3190 1.3190 1.3190 0.0000  0.0000  -0.0000 231 VAL A N   
1613 C CA  . VAL A 231 ? 1.3190 1.3190 1.3190 0.0000  0.0000  -0.0000 231 VAL A CA  
1614 C C   . VAL A 231 ? 1.3190 1.3190 1.3190 0.0000  0.0000  -0.0000 231 VAL A C   
1615 O O   . VAL A 231 ? 1.3190 1.3190 1.3190 0.0000  0.0000  -0.0000 231 VAL A O   
1616 C CB  . VAL A 231 ? 1.3190 1.3190 1.3190 0.0000  0.0000  -0.0000 231 VAL A CB  
1617 C CG1 . VAL A 231 ? 1.3190 1.3190 1.3190 0.0000  0.0000  -0.0000 231 VAL A CG1 
1618 C CG2 . VAL A 231 ? 1.3190 1.3190 1.3190 0.0000  0.0000  -0.0000 231 VAL A CG2 
1619 N N   . THR A 232 ? 1.3650 1.3650 1.3650 0.0000  0.0000  -0.0000 232 THR A N   
1620 C CA  . THR A 232 ? 1.3650 1.3650 1.3650 0.0000  0.0000  -0.0000 232 THR A CA  
1621 C C   . THR A 232 ? 1.3650 1.3650 1.3650 0.0000  0.0000  -0.0000 232 THR A C   
1622 O O   . THR A 232 ? 1.3650 1.3650 1.3650 0.0000  0.0000  -0.0000 232 THR A O   
1623 C CB  . THR A 232 ? 1.3650 1.3650 1.3650 0.0000  0.0000  -0.0000 232 THR A CB  
1624 O OG1 . THR A 232 ? 1.3650 1.3650 1.3650 0.0000  0.0000  -0.0000 232 THR A OG1 
1625 C CG2 . THR A 232 ? 1.3650 1.3650 1.3650 0.0000  0.0000  -0.0000 232 THR A CG2 
1626 N N   . ALA A 233 ? 1.3822 1.3822 1.3822 0.0000  0.0000  -0.0000 233 ALA A N   
1627 C CA  . ALA A 233 ? 1.3822 1.3822 1.3822 0.0000  0.0000  -0.0000 233 ALA A CA  
1628 C C   . ALA A 233 ? 1.3822 1.3822 1.3822 0.0000  0.0000  -0.0000 233 ALA A C   
1629 O O   . ALA A 233 ? 1.3822 1.3822 1.3822 0.0000  0.0000  -0.0000 233 ALA A O   
1630 C CB  . ALA A 233 ? 1.3822 1.3822 1.3822 0.0000  0.0000  -0.0000 233 ALA A CB  
1631 N N   . ALA A 234 ? 1.3713 1.3713 1.3713 0.0000  0.0000  0.0000  234 ALA A N   
1632 C CA  . ALA A 234 ? 1.3713 1.3713 1.3713 0.0000  0.0000  0.0000  234 ALA A CA  
1633 C C   . ALA A 234 ? 1.3713 1.3713 1.3713 0.0000  0.0000  0.0000  234 ALA A C   
1634 O O   . ALA A 234 ? 1.3713 1.3713 1.3713 0.0000  0.0000  0.0000  234 ALA A O   
1635 C CB  . ALA A 234 ? 1.3713 1.3713 1.3713 0.0000  0.0000  0.0000  234 ALA A CB  
1636 N N   . VAL A 235 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 235 VAL A N   
1637 C CA  . VAL A 235 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 235 VAL A CA  
1638 C C   . VAL A 235 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 235 VAL A C   
1639 O O   . VAL A 235 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 235 VAL A O   
1640 C CB  . VAL A 235 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 235 VAL A CB  
1641 C CG1 . VAL A 235 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 235 VAL A CG1 
1642 C CG2 . VAL A 235 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 235 VAL A CG2 
1643 N N   . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A N   
1644 C CA  . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A CA  
1645 C C   . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A C   
1646 O O   . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A O   
1647 C CB  . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A CB  
1648 C CG  . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A CG  
1649 C CD1 . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A CD1 
1650 C CD2 . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A CD2 
1651 C CE1 . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A CE1 
1652 C CE2 . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A CE2 
1653 C CZ  . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A CZ  
1654 O OH  . TYR A 236 ? 1.2777 1.2777 1.2777 0.0000  0.0000  -0.0000 236 TYR A OH  
1655 N N   . VAL A 237 ? 1.3130 1.3130 1.3130 0.0000  0.0000  -0.0000 237 VAL A N   
1656 C CA  . VAL A 237 ? 1.3130 1.3130 1.3130 0.0000  0.0000  -0.0000 237 VAL A CA  
1657 C C   . VAL A 237 ? 1.3130 1.3130 1.3130 0.0000  0.0000  -0.0000 237 VAL A C   
1658 O O   . VAL A 237 ? 1.3130 1.3130 1.3130 0.0000  0.0000  -0.0000 237 VAL A O   
1659 C CB  . VAL A 237 ? 1.3130 1.3130 1.3130 0.0000  0.0000  -0.0000 237 VAL A CB  
1660 C CG1 . VAL A 237 ? 1.3130 1.3130 1.3130 0.0000  0.0000  -0.0000 237 VAL A CG1 
1661 C CG2 . VAL A 237 ? 1.3130 1.3130 1.3130 0.0000  0.0000  -0.0000 237 VAL A CG2 
1662 N N   . GLY A 238 ? 1.2476 1.2476 1.2476 0.0000  0.0000  -0.0000 238 GLY A N   
1663 C CA  . GLY A 238 ? 1.2476 1.2476 1.2476 0.0000  0.0000  -0.0000 238 GLY A CA  
1664 C C   . GLY A 238 ? 1.2476 1.2476 1.2476 0.0000  0.0000  -0.0000 238 GLY A C   
1665 O O   . GLY A 238 ? 1.2476 1.2476 1.2476 0.0000  0.0000  -0.0000 238 GLY A O   
1666 N N   . LEU A 239 ? 1.2607 1.2607 1.2607 0.0000  0.0000  -0.0000 239 LEU A N   
1667 C CA  . LEU A 239 ? 1.2607 1.2607 1.2607 0.0000  0.0000  -0.0000 239 LEU A CA  
1668 C C   . LEU A 239 ? 1.2607 1.2607 1.2607 0.0000  0.0000  -0.0000 239 LEU A C   
1669 O O   . LEU A 239 ? 1.2607 1.2607 1.2607 0.0000  0.0000  -0.0000 239 LEU A O   
1670 C CB  . LEU A 239 ? 1.2607 1.2607 1.2607 0.0000  0.0000  -0.0000 239 LEU A CB  
1671 C CG  . LEU A 239 ? 1.2607 1.2607 1.2607 0.0000  0.0000  -0.0000 239 LEU A CG  
1672 C CD1 . LEU A 239 ? 1.2607 1.2607 1.2607 0.0000  0.0000  -0.0000 239 LEU A CD1 
1673 C CD2 . LEU A 239 ? 1.2607 1.2607 1.2607 0.0000  0.0000  -0.0000 239 LEU A CD2 
1674 N N   . THR A 240 ? 1.3205 1.3205 1.3205 0.0000  0.0000  -0.0000 240 THR A N   
1675 C CA  . THR A 240 ? 1.3205 1.3205 1.3205 0.0000  0.0000  -0.0000 240 THR A CA  
1676 C C   . THR A 240 ? 1.3205 1.3205 1.3205 0.0000  0.0000  -0.0000 240 THR A C   
1677 O O   . THR A 240 ? 1.3205 1.3205 1.3205 0.0000  0.0000  -0.0000 240 THR A O   
1678 C CB  . THR A 240 ? 1.3205 1.3205 1.3205 0.0000  0.0000  -0.0000 240 THR A CB  
1679 O OG1 . THR A 240 ? 1.3205 1.3205 1.3205 0.0000  0.0000  -0.0000 240 THR A OG1 
1680 C CG2 . THR A 240 ? 1.3205 1.3205 1.3205 0.0000  0.0000  -0.0000 240 THR A CG2 
1681 N N   . LEU A 241 ? 1.2889 1.2889 1.2889 0.0000  -0.0000 0.0000  241 LEU A N   
1682 C CA  . LEU A 241 ? 1.2889 1.2889 1.2889 0.0000  -0.0000 0.0000  241 LEU A CA  
1683 C C   . LEU A 241 ? 1.2889 1.2889 1.2889 0.0000  -0.0000 0.0000  241 LEU A C   
1684 O O   . LEU A 241 ? 1.2889 1.2889 1.2889 0.0000  -0.0000 0.0000  241 LEU A O   
1685 C CB  . LEU A 241 ? 1.2889 1.2889 1.2889 0.0000  -0.0000 0.0000  241 LEU A CB  
1686 C CG  . LEU A 241 ? 1.2889 1.2889 1.2889 0.0000  -0.0000 0.0000  241 LEU A CG  
1687 C CD1 . LEU A 241 ? 1.2889 1.2889 1.2889 0.0000  -0.0000 0.0000  241 LEU A CD1 
1688 C CD2 . LEU A 241 ? 1.2889 1.2889 1.2889 0.0000  -0.0000 0.0000  241 LEU A CD2 
1689 N N   . GLN A 242 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 242 GLN A N   
1690 C CA  . GLN A 242 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 242 GLN A CA  
1691 C C   . GLN A 242 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 242 GLN A C   
1692 O O   . GLN A 242 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 242 GLN A O   
1693 C CB  . GLN A 242 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 242 GLN A CB  
1694 C CG  . GLN A 242 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 242 GLN A CG  
1695 C CD  . GLN A 242 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 242 GLN A CD  
1696 O OE1 . GLN A 242 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 242 GLN A OE1 
1697 N NE2 . GLN A 242 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 242 GLN A NE2 
1698 N N   . ILE A 243 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 243 ILE A N   
1699 C CA  . ILE A 243 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 243 ILE A CA  
1700 C C   . ILE A 243 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 243 ILE A C   
1701 O O   . ILE A 243 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 243 ILE A O   
1702 C CB  . ILE A 243 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 243 ILE A CB  
1703 C CG1 . ILE A 243 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 243 ILE A CG1 
1704 C CG2 . ILE A 243 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 243 ILE A CG2 
1705 C CD1 . ILE A 243 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 243 ILE A CD1 
1706 N N   . LEU A 244 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 244 LEU A N   
1707 C CA  . LEU A 244 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 244 LEU A CA  
1708 C C   . LEU A 244 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 244 LEU A C   
1709 O O   . LEU A 244 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 244 LEU A O   
1710 C CB  . LEU A 244 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 244 LEU A CB  
1711 C CG  . LEU A 244 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 244 LEU A CG  
1712 C CD1 . LEU A 244 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 244 LEU A CD1 
1713 C CD2 . LEU A 244 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 244 LEU A CD2 
1714 N N   . LEU A 245 ? 1.2815 1.2815 1.2815 -0.0000 0.0000  -0.0000 245 LEU A N   
1715 C CA  . LEU A 245 ? 1.2815 1.2815 1.2815 -0.0000 0.0000  -0.0000 245 LEU A CA  
1716 C C   . LEU A 245 ? 1.2815 1.2815 1.2815 -0.0000 0.0000  -0.0000 245 LEU A C   
1717 O O   . LEU A 245 ? 1.2815 1.2815 1.2815 -0.0000 0.0000  -0.0000 245 LEU A O   
1718 C CB  . LEU A 245 ? 1.2815 1.2815 1.2815 -0.0000 0.0000  -0.0000 245 LEU A CB  
1719 C CG  . LEU A 245 ? 1.2815 1.2815 1.2815 -0.0000 0.0000  -0.0000 245 LEU A CG  
1720 C CD1 . LEU A 245 ? 1.2815 1.2815 1.2815 -0.0000 0.0000  -0.0000 245 LEU A CD1 
1721 C CD2 . LEU A 245 ? 1.2815 1.2815 1.2815 -0.0000 0.0000  -0.0000 245 LEU A CD2 
1722 N N   . VAL A 246 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 246 VAL A N   
1723 C CA  . VAL A 246 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 246 VAL A CA  
1724 C C   . VAL A 246 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 246 VAL A C   
1725 O O   . VAL A 246 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 246 VAL A O   
1726 C CB  . VAL A 246 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 246 VAL A CB  
1727 C CG1 . VAL A 246 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 246 VAL A CG1 
1728 C CG2 . VAL A 246 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 246 VAL A CG2 
1729 N N   . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A N   
1730 C CA  . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A CA  
1731 C C   . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A C   
1732 O O   . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A O   
1733 C CB  . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A CB  
1734 C CG  . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A CG  
1735 C CD1 . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A CD1 
1736 C CD2 . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A CD2 
1737 C CE1 . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A CE1 
1738 C CE2 . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A CE2 
1739 C CZ  . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A CZ  
1740 O OH  . TYR A 247 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 247 TYR A OH  
1741 N N   . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A N   
1742 C CA  . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A CA  
1743 C C   . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A C   
1744 O O   . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A O   
1745 C CB  . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A CB  
1746 C CG  . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A CG  
1747 C CD1 . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A CD1 
1748 C CD2 . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A CD2 
1749 C CE1 . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A CE1 
1750 C CE2 . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A CE2 
1751 C CZ  . PHE A 248 ? 1.2414 1.2414 1.2414 -0.0000 -0.0000 0.0000  248 PHE A CZ  
1752 N N   . VAL A 249 ? 1.2665 1.2665 1.2665 0.0000  0.0000  -0.0000 249 VAL A N   
1753 C CA  . VAL A 249 ? 1.2665 1.2665 1.2665 0.0000  0.0000  -0.0000 249 VAL A CA  
1754 C C   . VAL A 249 ? 1.2665 1.2665 1.2665 0.0000  0.0000  -0.0000 249 VAL A C   
1755 O O   . VAL A 249 ? 1.2665 1.2665 1.2665 0.0000  0.0000  -0.0000 249 VAL A O   
1756 C CB  . VAL A 249 ? 1.2665 1.2665 1.2665 0.0000  0.0000  -0.0000 249 VAL A CB  
1757 C CG1 . VAL A 249 ? 1.2665 1.2665 1.2665 0.0000  0.0000  -0.0000 249 VAL A CG1 
1758 C CG2 . VAL A 249 ? 1.2665 1.2665 1.2665 0.0000  0.0000  -0.0000 249 VAL A CG2 
1759 N N   . LEU A 250 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 250 LEU A N   
1760 C CA  . LEU A 250 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 250 LEU A CA  
1761 C C   . LEU A 250 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 250 LEU A C   
1762 O O   . LEU A 250 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 250 LEU A O   
1763 C CB  . LEU A 250 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 250 LEU A CB  
1764 C CG  . LEU A 250 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 250 LEU A CG  
1765 C CD1 . LEU A 250 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 250 LEU A CD1 
1766 C CD2 . LEU A 250 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 250 LEU A CD2 
1767 N N   . LEU A 251 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 251 LEU A N   
1768 C CA  . LEU A 251 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 251 LEU A CA  
1769 C C   . LEU A 251 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 251 LEU A C   
1770 O O   . LEU A 251 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 251 LEU A O   
1771 C CB  . LEU A 251 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 251 LEU A CB  
1772 C CG  . LEU A 251 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 251 LEU A CG  
1773 C CD1 . LEU A 251 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 251 LEU A CD1 
1774 C CD2 . LEU A 251 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 251 LEU A CD2 
1775 N N   . LYS A 252 ? 1.3580 1.3580 1.3580 0.0000  0.0000  -0.0000 252 LYS A N   
1776 C CA  . LYS A 252 ? 1.3580 1.3580 1.3580 0.0000  0.0000  -0.0000 252 LYS A CA  
1777 C C   . LYS A 252 ? 1.3580 1.3580 1.3580 0.0000  0.0000  -0.0000 252 LYS A C   
1778 O O   . LYS A 252 ? 1.3580 1.3580 1.3580 0.0000  0.0000  -0.0000 252 LYS A O   
1779 C CB  . LYS A 252 ? 1.3580 1.3580 1.3580 0.0000  0.0000  -0.0000 252 LYS A CB  
1780 C CG  . LYS A 252 ? 1.3580 1.3580 1.3580 0.0000  0.0000  -0.0000 252 LYS A CG  
1781 C CD  . LYS A 252 ? 1.3580 1.3580 1.3580 0.0000  0.0000  -0.0000 252 LYS A CD  
1782 C CE  . LYS A 252 ? 1.3580 1.3580 1.3580 0.0000  0.0000  -0.0000 252 LYS A CE  
1783 N NZ  . LYS A 252 ? 1.3580 1.3580 1.3580 0.0000  0.0000  -0.0000 252 LYS A NZ  
1784 N N   . ILE A 253 ? 1.3337 1.3337 1.3337 0.0000  0.0000  -0.0000 253 ILE A N   
1785 C CA  . ILE A 253 ? 1.3337 1.3337 1.3337 0.0000  0.0000  -0.0000 253 ILE A CA  
1786 C C   . ILE A 253 ? 1.3337 1.3337 1.3337 0.0000  0.0000  -0.0000 253 ILE A C   
1787 O O   . ILE A 253 ? 1.3337 1.3337 1.3337 0.0000  0.0000  -0.0000 253 ILE A O   
1788 C CB  . ILE A 253 ? 1.3337 1.3337 1.3337 0.0000  0.0000  -0.0000 253 ILE A CB  
1789 C CG1 . ILE A 253 ? 1.3337 1.3337 1.3337 0.0000  0.0000  -0.0000 253 ILE A CG1 
1790 C CG2 . ILE A 253 ? 1.3337 1.3337 1.3337 0.0000  0.0000  -0.0000 253 ILE A CG2 
1791 C CD1 . ILE A 253 ? 1.3337 1.3337 1.3337 0.0000  0.0000  -0.0000 253 ILE A CD1 
1792 N N   . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A N   
1793 C CA  . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A CA  
1794 C C   . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A C   
1795 O O   . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A O   
1796 C CB  . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A CB  
1797 C CG  . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A CG  
1798 C CD1 . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A CD1 
1799 C CD2 . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A CD2 
1800 C CE1 . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A CE1 
1801 C CE2 . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A CE2 
1802 C CZ  . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A CZ  
1803 O OH  . TYR A 254 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 254 TYR A OH  
1804 N N   . GLY A 255 ? 1.2785 1.2785 1.2785 0.0000  0.0000  -0.0000 255 GLY A N   
1805 C CA  . GLY A 255 ? 1.2785 1.2785 1.2785 0.0000  0.0000  -0.0000 255 GLY A CA  
1806 C C   . GLY A 255 ? 1.2785 1.2785 1.2785 0.0000  0.0000  -0.0000 255 GLY A C   
1807 O O   . GLY A 255 ? 1.2785 1.2785 1.2785 0.0000  0.0000  -0.0000 255 GLY A O   
1808 N N   . ILE A 256 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 256 ILE A N   
1809 C CA  . ILE A 256 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 256 ILE A CA  
1810 C C   . ILE A 256 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 256 ILE A C   
1811 O O   . ILE A 256 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 256 ILE A O   
1812 C CB  . ILE A 256 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 256 ILE A CB  
1813 C CG1 . ILE A 256 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 256 ILE A CG1 
1814 C CG2 . ILE A 256 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 256 ILE A CG2 
1815 C CD1 . ILE A 256 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 256 ILE A CD1 
1816 N N   . ASP A 257 ? 1.4764 1.4764 1.4764 0.0000  0.0000  0.0000  257 ASP A N   
1817 C CA  . ASP A 257 ? 1.4764 1.4764 1.4764 0.0000  0.0000  0.0000  257 ASP A CA  
1818 C C   . ASP A 257 ? 1.4764 1.4764 1.4764 0.0000  0.0000  0.0000  257 ASP A C   
1819 O O   . ASP A 257 ? 1.4764 1.4764 1.4764 0.0000  0.0000  0.0000  257 ASP A O   
1820 C CB  . ASP A 257 ? 1.4764 1.4764 1.4764 0.0000  0.0000  0.0000  257 ASP A CB  
1821 C CG  . ASP A 257 ? 1.4764 1.4764 1.4764 0.0000  0.0000  0.0000  257 ASP A CG  
1822 O OD1 . ASP A 257 ? 1.4764 1.4764 1.4764 0.0000  0.0000  0.0000  257 ASP A OD1 
1823 O OD2 . ASP A 257 ? 1.4764 1.4764 1.4764 0.0000  0.0000  0.0000  257 ASP A OD2 
1824 N N   . PRO A 258 ? 1.2998 1.2998 1.2998 0.0000  0.0000  -0.0000 258 PRO A N   
1825 C CA  . PRO A 258 ? 1.2998 1.2998 1.2998 0.0000  0.0000  -0.0000 258 PRO A CA  
1826 C C   . PRO A 258 ? 1.2998 1.2998 1.2998 0.0000  0.0000  -0.0000 258 PRO A C   
1827 O O   . PRO A 258 ? 1.2998 1.2998 1.2998 0.0000  0.0000  -0.0000 258 PRO A O   
1828 C CB  . PRO A 258 ? 1.2998 1.2998 1.2998 0.0000  0.0000  -0.0000 258 PRO A CB  
1829 C CG  . PRO A 258 ? 1.2998 1.2998 1.2998 0.0000  0.0000  -0.0000 258 PRO A CG  
1830 C CD  . PRO A 258 ? 1.2998 1.2998 1.2998 0.0000  0.0000  -0.0000 258 PRO A CD  
1831 N N   . ILE A 259 ? 1.3782 1.3782 1.3782 0.0000  0.0000  -0.0000 259 ILE A N   
1832 C CA  . ILE A 259 ? 1.3782 1.3782 1.3782 0.0000  0.0000  -0.0000 259 ILE A CA  
1833 C C   . ILE A 259 ? 1.3782 1.3782 1.3782 0.0000  0.0000  -0.0000 259 ILE A C   
1834 O O   . ILE A 259 ? 1.3782 1.3782 1.3782 0.0000  0.0000  -0.0000 259 ILE A O   
1835 C CB  . ILE A 259 ? 1.3782 1.3782 1.3782 0.0000  0.0000  -0.0000 259 ILE A CB  
1836 C CG1 . ILE A 259 ? 1.3782 1.3782 1.3782 0.0000  0.0000  -0.0000 259 ILE A CG1 
1837 C CG2 . ILE A 259 ? 1.3782 1.3782 1.3782 0.0000  0.0000  -0.0000 259 ILE A CG2 
1838 C CD1 . ILE A 259 ? 1.3782 1.3782 1.3782 0.0000  0.0000  -0.0000 259 ILE A CD1 
1839 N N   . SER A 260 ? 1.3916 1.3916 1.3916 0.0000  0.0000  0.0000  260 SER A N   
1840 C CA  . SER A 260 ? 1.3916 1.3916 1.3916 0.0000  0.0000  0.0000  260 SER A CA  
1841 C C   . SER A 260 ? 1.3916 1.3916 1.3916 0.0000  0.0000  0.0000  260 SER A C   
1842 O O   . SER A 260 ? 1.3916 1.3916 1.3916 0.0000  0.0000  0.0000  260 SER A O   
1843 C CB  . SER A 260 ? 1.3916 1.3916 1.3916 0.0000  0.0000  0.0000  260 SER A CB  
1844 O OG  . SER A 260 ? 1.3916 1.3916 1.3916 0.0000  0.0000  0.0000  260 SER A OG  
1845 N N   . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A N   
1846 C CA  . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A CA  
1847 C C   . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A C   
1848 O O   . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A O   
1849 C CB  . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A CB  
1850 C CG  . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A CG  
1851 C CD1 . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A CD1 
1852 C CD2 . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A CD2 
1853 C CE1 . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A CE1 
1854 C CE2 . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A CE2 
1855 C CZ  . PHE A 261 ? 1.2871 1.2871 1.2871 0.0000  0.0000  -0.0000 261 PHE A CZ  
1856 N N   . ILE A 262 ? 1.3143 1.3143 1.3143 0.0000  -0.0000 0.0000  262 ILE A N   
1857 C CA  . ILE A 262 ? 1.3143 1.3143 1.3143 0.0000  -0.0000 0.0000  262 ILE A CA  
1858 C C   . ILE A 262 ? 1.3143 1.3143 1.3143 0.0000  -0.0000 0.0000  262 ILE A C   
1859 O O   . ILE A 262 ? 1.3143 1.3143 1.3143 0.0000  -0.0000 0.0000  262 ILE A O   
1860 C CB  . ILE A 262 ? 1.3143 1.3143 1.3143 0.0000  -0.0000 0.0000  262 ILE A CB  
1861 C CG1 . ILE A 262 ? 1.3143 1.3143 1.3143 0.0000  -0.0000 0.0000  262 ILE A CG1 
1862 C CG2 . ILE A 262 ? 1.3143 1.3143 1.3143 0.0000  -0.0000 0.0000  262 ILE A CG2 
1863 C CD1 . ILE A 262 ? 1.3143 1.3143 1.3143 0.0000  -0.0000 0.0000  262 ILE A CD1 
1864 N N   . LYS A 263 ? 1.4070 1.4070 1.4070 0.0000  0.0000  -0.0000 263 LYS A N   
1865 C CA  . LYS A 263 ? 1.4070 1.4070 1.4070 0.0000  0.0000  -0.0000 263 LYS A CA  
1866 C C   . LYS A 263 ? 1.4070 1.4070 1.4070 0.0000  0.0000  -0.0000 263 LYS A C   
1867 O O   . LYS A 263 ? 1.4070 1.4070 1.4070 0.0000  0.0000  -0.0000 263 LYS A O   
1868 C CB  . LYS A 263 ? 1.4070 1.4070 1.4070 0.0000  0.0000  -0.0000 263 LYS A CB  
1869 C CG  . LYS A 263 ? 1.4070 1.4070 1.4070 0.0000  0.0000  -0.0000 263 LYS A CG  
1870 C CD  . LYS A 263 ? 1.4070 1.4070 1.4070 0.0000  0.0000  -0.0000 263 LYS A CD  
1871 C CE  . LYS A 263 ? 1.4070 1.4070 1.4070 0.0000  0.0000  -0.0000 263 LYS A CE  
1872 N NZ  . LYS A 263 ? 1.4070 1.4070 1.4070 0.0000  0.0000  -0.0000 263 LYS A NZ  
1873 N N   . HIS A 264 ? 1.3128 1.3128 1.3128 0.0000  0.0000  -0.0000 264 HIS A N   
1874 C CA  . HIS A 264 ? 1.3128 1.3128 1.3128 0.0000  0.0000  -0.0000 264 HIS A CA  
1875 C C   . HIS A 264 ? 1.3128 1.3128 1.3128 0.0000  0.0000  -0.0000 264 HIS A C   
1876 O O   . HIS A 264 ? 1.3128 1.3128 1.3128 0.0000  0.0000  -0.0000 264 HIS A O   
1877 C CB  . HIS A 264 ? 1.3128 1.3128 1.3128 0.0000  0.0000  -0.0000 264 HIS A CB  
1878 C CG  . HIS A 264 ? 1.3128 1.3128 1.3128 0.0000  0.0000  -0.0000 264 HIS A CG  
1879 N ND1 . HIS A 264 ? 1.3128 1.3128 1.3128 0.0000  0.0000  -0.0000 264 HIS A ND1 
1880 C CD2 . HIS A 264 ? 1.3128 1.3128 1.3128 0.0000  0.0000  -0.0000 264 HIS A CD2 
1881 C CE1 . HIS A 264 ? 1.3128 1.3128 1.3128 0.0000  0.0000  -0.0000 264 HIS A CE1 
1882 N NE2 . HIS A 264 ? 1.3128 1.3128 1.3128 0.0000  0.0000  -0.0000 264 HIS A NE2 
1883 N N   . ALA A 265 ? 1.3001 1.3001 1.3001 -0.0000 0.0000  0.0000  265 ALA A N   
1884 C CA  . ALA A 265 ? 1.3001 1.3001 1.3001 -0.0000 0.0000  0.0000  265 ALA A CA  
1885 C C   . ALA A 265 ? 1.3001 1.3001 1.3001 -0.0000 0.0000  0.0000  265 ALA A C   
1886 O O   . ALA A 265 ? 1.3001 1.3001 1.3001 -0.0000 0.0000  0.0000  265 ALA A O   
1887 C CB  . ALA A 265 ? 1.3001 1.3001 1.3001 -0.0000 0.0000  0.0000  265 ALA A CB  
1888 N N   . LYS A 266 ? 1.3153 1.3153 1.3153 -0.0000 0.0000  -0.0000 266 LYS A N   
1889 C CA  . LYS A 266 ? 1.3153 1.3153 1.3153 -0.0000 0.0000  -0.0000 266 LYS A CA  
1890 C C   . LYS A 266 ? 1.3153 1.3153 1.3153 -0.0000 0.0000  -0.0000 266 LYS A C   
1891 O O   . LYS A 266 ? 1.3153 1.3153 1.3153 -0.0000 0.0000  -0.0000 266 LYS A O   
1892 C CB  . LYS A 266 ? 1.3153 1.3153 1.3153 -0.0000 0.0000  -0.0000 266 LYS A CB  
1893 C CG  . LYS A 266 ? 1.3153 1.3153 1.3153 -0.0000 0.0000  -0.0000 266 LYS A CG  
1894 C CD  . LYS A 266 ? 1.3153 1.3153 1.3153 -0.0000 0.0000  -0.0000 266 LYS A CD  
1895 C CE  . LYS A 266 ? 1.3153 1.3153 1.3153 -0.0000 0.0000  -0.0000 266 LYS A CE  
1896 N NZ  . LYS A 266 ? 1.3153 1.3153 1.3153 -0.0000 0.0000  -0.0000 266 LYS A NZ  
1897 N N   . ASP A 267 ? 1.2992 1.2992 1.2992 0.0000  0.0000  -0.0000 267 ASP A N   
1898 C CA  . ASP A 267 ? 1.2992 1.2992 1.2992 0.0000  0.0000  -0.0000 267 ASP A CA  
1899 C C   . ASP A 267 ? 1.2992 1.2992 1.2992 0.0000  0.0000  -0.0000 267 ASP A C   
1900 O O   . ASP A 267 ? 1.2992 1.2992 1.2992 0.0000  0.0000  -0.0000 267 ASP A O   
1901 C CB  . ASP A 267 ? 1.2992 1.2992 1.2992 0.0000  0.0000  -0.0000 267 ASP A CB  
1902 C CG  . ASP A 267 ? 1.2992 1.2992 1.2992 0.0000  0.0000  -0.0000 267 ASP A CG  
1903 O OD1 . ASP A 267 ? 1.2992 1.2992 1.2992 0.0000  0.0000  -0.0000 267 ASP A OD1 
1904 O OD2 . ASP A 267 ? 1.2992 1.2992 1.2992 0.0000  0.0000  -0.0000 267 ASP A OD2 
1905 N N   . ALA A 268 ? 1.2709 1.2709 1.2709 -0.0000 0.0000  -0.0000 268 ALA A N   
1906 C CA  . ALA A 268 ? 1.2709 1.2709 1.2709 -0.0000 0.0000  -0.0000 268 ALA A CA  
1907 C C   . ALA A 268 ? 1.2709 1.2709 1.2709 -0.0000 0.0000  -0.0000 268 ALA A C   
1908 O O   . ALA A 268 ? 1.2709 1.2709 1.2709 -0.0000 0.0000  -0.0000 268 ALA A O   
1909 C CB  . ALA A 268 ? 1.2709 1.2709 1.2709 -0.0000 0.0000  -0.0000 268 ALA A CB  
1910 N N   . MET A 269 ? 1.4177 1.4177 1.4177 -0.0000 -0.0000 0.0000  269 MET A N   
1911 C CA  . MET A 269 ? 1.4177 1.4177 1.4177 -0.0000 -0.0000 0.0000  269 MET A CA  
1912 C C   . MET A 269 ? 1.4177 1.4177 1.4177 -0.0000 -0.0000 0.0000  269 MET A C   
1913 O O   . MET A 269 ? 1.4177 1.4177 1.4177 -0.0000 -0.0000 0.0000  269 MET A O   
1914 C CB  . MET A 269 ? 1.4177 1.4177 1.4177 -0.0000 -0.0000 0.0000  269 MET A CB  
1915 C CG  . MET A 269 ? 1.4177 1.4177 1.4177 -0.0000 -0.0000 0.0000  269 MET A CG  
1916 S SD  . MET A 269 ? 1.4177 1.4177 1.4177 -0.0000 -0.0000 0.0000  269 MET A SD  
1917 C CE  . MET A 269 ? 1.4177 1.4177 1.4177 -0.0000 -0.0000 0.0000  269 MET A CE  
1918 N N   . LEU A 270 ? 1.2824 1.2824 1.2824 0.0000  0.0000  -0.0000 270 LEU A N   
1919 C CA  . LEU A 270 ? 1.2824 1.2824 1.2824 0.0000  0.0000  -0.0000 270 LEU A CA  
1920 C C   . LEU A 270 ? 1.2824 1.2824 1.2824 0.0000  0.0000  -0.0000 270 LEU A C   
1921 O O   . LEU A 270 ? 1.2824 1.2824 1.2824 0.0000  0.0000  -0.0000 270 LEU A O   
1922 C CB  . LEU A 270 ? 1.2824 1.2824 1.2824 0.0000  0.0000  -0.0000 270 LEU A CB  
1923 C CG  . LEU A 270 ? 1.2824 1.2824 1.2824 0.0000  0.0000  -0.0000 270 LEU A CG  
1924 C CD1 . LEU A 270 ? 1.2824 1.2824 1.2824 0.0000  0.0000  -0.0000 270 LEU A CD1 
1925 C CD2 . LEU A 270 ? 1.2824 1.2824 1.2824 0.0000  0.0000  -0.0000 270 LEU A CD2 
1926 N N   . THR A 271 ? 1.2451 1.2451 1.2451 0.0000  0.0000  0.0000  271 THR A N   
1927 C CA  . THR A 271 ? 1.2451 1.2451 1.2451 0.0000  0.0000  0.0000  271 THR A CA  
1928 C C   . THR A 271 ? 1.2451 1.2451 1.2451 0.0000  0.0000  0.0000  271 THR A C   
1929 O O   . THR A 271 ? 1.2451 1.2451 1.2451 0.0000  0.0000  0.0000  271 THR A O   
1930 C CB  . THR A 271 ? 1.2451 1.2451 1.2451 0.0000  0.0000  0.0000  271 THR A CB  
1931 O OG1 . THR A 271 ? 1.2451 1.2451 1.2451 0.0000  0.0000  0.0000  271 THR A OG1 
1932 C CG2 . THR A 271 ? 1.2451 1.2451 1.2451 0.0000  0.0000  0.0000  271 THR A CG2 
1933 N N   . ALA A 272 ? 1.2602 1.2602 1.2602 0.0000  0.0000  -0.0000 272 ALA A N   
1934 C CA  . ALA A 272 ? 1.2602 1.2602 1.2602 0.0000  0.0000  -0.0000 272 ALA A CA  
1935 C C   . ALA A 272 ? 1.2602 1.2602 1.2602 0.0000  0.0000  -0.0000 272 ALA A C   
1936 O O   . ALA A 272 ? 1.2602 1.2602 1.2602 0.0000  0.0000  -0.0000 272 ALA A O   
1937 C CB  . ALA A 272 ? 1.2602 1.2602 1.2602 0.0000  0.0000  -0.0000 272 ALA A CB  
1938 N N   . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A N   
1939 C CA  . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A CA  
1940 C C   . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A C   
1941 O O   . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A O   
1942 C CB  . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A CB  
1943 C CG  . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A CG  
1944 C CD1 . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A CD1 
1945 C CD2 . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A CD2 
1946 C CE1 . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A CE1 
1947 C CE2 . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A CE2 
1948 C CZ  . PHE A 273 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 273 PHE A CZ  
1949 N N   . VAL A 274 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 274 VAL A N   
1950 C CA  . VAL A 274 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 274 VAL A CA  
1951 C C   . VAL A 274 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 274 VAL A C   
1952 O O   . VAL A 274 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 274 VAL A O   
1953 C CB  . VAL A 274 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 274 VAL A CB  
1954 C CG1 . VAL A 274 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 274 VAL A CG1 
1955 C CG2 . VAL A 274 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 274 VAL A CG2 
1956 N N   . THR A 275 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 275 THR A N   
1957 C CA  . THR A 275 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 275 THR A CA  
1958 C C   . THR A 275 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 275 THR A C   
1959 O O   . THR A 275 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 275 THR A O   
1960 C CB  . THR A 275 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 275 THR A CB  
1961 O OG1 . THR A 275 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 275 THR A OG1 
1962 C CG2 . THR A 275 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 275 THR A CG2 
1963 N N   . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A N   
1964 C CA  . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A CA  
1965 C C   . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A C   
1966 O O   . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A O   
1967 C CB  . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A CB  
1968 C CG  . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A CG  
1969 C CD  . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A CD  
1970 N NE  . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A NE  
1971 C CZ  . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A CZ  
1972 N NH1 . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A NH1 
1973 N NH2 . ARG A 276 ? 1.2797 1.2797 1.2797 -0.0000 0.0000  -0.0000 276 ARG A NH2 
1974 N N   . SER A 277 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 277 SER A N   
1975 C CA  . SER A 277 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 277 SER A CA  
1976 C C   . SER A 277 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 277 SER A C   
1977 O O   . SER A 277 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 277 SER A O   
1978 C CB  . SER A 277 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 277 SER A CB  
1979 O OG  . SER A 277 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 277 SER A OG  
1980 N N   . SER A 278 ? 1.2632 1.2632 1.2632 0.0000  -0.0000 -0.0000 278 SER A N   
1981 C CA  . SER A 278 ? 1.2632 1.2632 1.2632 0.0000  -0.0000 -0.0000 278 SER A CA  
1982 C C   . SER A 278 ? 1.2632 1.2632 1.2632 0.0000  -0.0000 -0.0000 278 SER A C   
1983 O O   . SER A 278 ? 1.2632 1.2632 1.2632 0.0000  -0.0000 -0.0000 278 SER A O   
1984 C CB  . SER A 278 ? 1.2632 1.2632 1.2632 0.0000  -0.0000 -0.0000 278 SER A CB  
1985 O OG  . SER A 278 ? 1.2632 1.2632 1.2632 0.0000  -0.0000 -0.0000 278 SER A OG  
1986 N N   . SER A 279 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 279 SER A N   
1987 C CA  . SER A 279 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 279 SER A CA  
1988 C C   . SER A 279 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 279 SER A C   
1989 O O   . SER A 279 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 279 SER A O   
1990 C CB  . SER A 279 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 279 SER A CB  
1991 O OG  . SER A 279 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 279 SER A OG  
1992 N N   . GLY A 280 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 280 GLY A N   
1993 C CA  . GLY A 280 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 280 GLY A CA  
1994 C C   . GLY A 280 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 280 GLY A C   
1995 O O   . GLY A 280 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 280 GLY A O   
1996 N N   . THR A 281 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 281 THR A N   
1997 C CA  . THR A 281 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 281 THR A CA  
1998 C C   . THR A 281 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 281 THR A C   
1999 O O   . THR A 281 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 281 THR A O   
2000 C CB  . THR A 281 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 281 THR A CB  
2001 O OG1 . THR A 281 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 281 THR A OG1 
2002 C CG2 . THR A 281 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 281 THR A CG2 
2003 N N   . LEU A 282 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 282 LEU A N   
2004 C CA  . LEU A 282 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 282 LEU A CA  
2005 C C   . LEU A 282 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 282 LEU A C   
2006 O O   . LEU A 282 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 282 LEU A O   
2007 C CB  . LEU A 282 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 282 LEU A CB  
2008 C CG  . LEU A 282 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 282 LEU A CG  
2009 C CD1 . LEU A 282 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 282 LEU A CD1 
2010 C CD2 . LEU A 282 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 282 LEU A CD2 
2011 N N   . PRO A 283 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 283 PRO A N   
2012 C CA  . PRO A 283 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 283 PRO A CA  
2013 C C   . PRO A 283 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 283 PRO A C   
2014 O O   . PRO A 283 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 283 PRO A O   
2015 C CB  . PRO A 283 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 283 PRO A CB  
2016 C CG  . PRO A 283 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 283 PRO A CG  
2017 C CD  . PRO A 283 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 283 PRO A CD  
2018 N N   . VAL A 284 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 284 VAL A N   
2019 C CA  . VAL A 284 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 284 VAL A CA  
2020 C C   . VAL A 284 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 284 VAL A C   
2021 O O   . VAL A 284 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 284 VAL A O   
2022 C CB  . VAL A 284 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 284 VAL A CB  
2023 C CG1 . VAL A 284 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 284 VAL A CG1 
2024 C CG2 . VAL A 284 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 284 VAL A CG2 
2025 N N   . THR A 285 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 285 THR A N   
2026 C CA  . THR A 285 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 285 THR A CA  
2027 C C   . THR A 285 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 285 THR A C   
2028 O O   . THR A 285 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 285 THR A O   
2029 C CB  . THR A 285 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 285 THR A CB  
2030 O OG1 . THR A 285 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 285 THR A OG1 
2031 C CG2 . THR A 285 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 285 THR A CG2 
2032 N N   . MET A 286 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 286 MET A N   
2033 C CA  . MET A 286 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 286 MET A CA  
2034 C C   . MET A 286 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 286 MET A C   
2035 O O   . MET A 286 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 286 MET A O   
2036 C CB  . MET A 286 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 286 MET A CB  
2037 C CG  . MET A 286 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 286 MET A CG  
2038 S SD  . MET A 286 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 286 MET A SD  
2039 C CE  . MET A 286 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 286 MET A CE  
2040 N N   . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A N   
2041 C CA  . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A CA  
2042 C C   . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A C   
2043 O O   . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A O   
2044 C CB  . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A CB  
2045 C CG  . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A CG  
2046 C CD  . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A CD  
2047 N NE  . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A NE  
2048 C CZ  . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A CZ  
2049 N NH1 . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A NH1 
2050 N NH2 . ARG A 287 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 287 ARG A NH2 
2051 N N   . VAL A 288 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 288 VAL A N   
2052 C CA  . VAL A 288 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 288 VAL A CA  
2053 C C   . VAL A 288 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 288 VAL A C   
2054 O O   . VAL A 288 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 288 VAL A O   
2055 C CB  . VAL A 288 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 288 VAL A CB  
2056 C CG1 . VAL A 288 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 288 VAL A CG1 
2057 C CG2 . VAL A 288 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 288 VAL A CG2 
2058 N N   . ALA A 289 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 289 ALA A N   
2059 C CA  . ALA A 289 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 289 ALA A CA  
2060 C C   . ALA A 289 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 289 ALA A C   
2061 O O   . ALA A 289 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 289 ALA A O   
2062 C CB  . ALA A 289 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 289 ALA A CB  
2063 N N   . LYS A 290 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 290 LYS A N   
2064 C CA  . LYS A 290 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 290 LYS A CA  
2065 C C   . LYS A 290 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 290 LYS A C   
2066 O O   . LYS A 290 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 290 LYS A O   
2067 C CB  . LYS A 290 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 290 LYS A CB  
2068 C CG  . LYS A 290 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 290 LYS A CG  
2069 C CD  . LYS A 290 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 290 LYS A CD  
2070 C CE  . LYS A 290 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 290 LYS A CE  
2071 N NZ  . LYS A 290 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 290 LYS A NZ  
2072 N N   . GLU A 291 ? 1.3077 1.3077 1.3077 0.0000  0.0000  -0.0000 291 GLU A N   
2073 C CA  . GLU A 291 ? 1.3077 1.3077 1.3077 0.0000  0.0000  -0.0000 291 GLU A CA  
2074 C C   . GLU A 291 ? 1.3077 1.3077 1.3077 0.0000  0.0000  -0.0000 291 GLU A C   
2075 O O   . GLU A 291 ? 1.3077 1.3077 1.3077 0.0000  0.0000  -0.0000 291 GLU A O   
2076 C CB  . GLU A 291 ? 1.3077 1.3077 1.3077 0.0000  0.0000  -0.0000 291 GLU A CB  
2077 C CG  . GLU A 291 ? 1.3077 1.3077 1.3077 0.0000  0.0000  -0.0000 291 GLU A CG  
2078 C CD  . GLU A 291 ? 1.3077 1.3077 1.3077 0.0000  0.0000  -0.0000 291 GLU A CD  
2079 O OE1 . GLU A 291 ? 1.3077 1.3077 1.3077 0.0000  0.0000  -0.0000 291 GLU A OE1 
2080 O OE2 . GLU A 291 ? 1.3077 1.3077 1.3077 0.0000  0.0000  -0.0000 291 GLU A OE2 
2081 N N   . MET A 292 ? 1.3148 1.3148 1.3148 0.0000  0.0000  -0.0000 292 MET A N   
2082 C CA  . MET A 292 ? 1.3148 1.3148 1.3148 0.0000  0.0000  -0.0000 292 MET A CA  
2083 C C   . MET A 292 ? 1.3148 1.3148 1.3148 0.0000  0.0000  -0.0000 292 MET A C   
2084 O O   . MET A 292 ? 1.3148 1.3148 1.3148 0.0000  0.0000  -0.0000 292 MET A O   
2085 C CB  . MET A 292 ? 1.3148 1.3148 1.3148 0.0000  0.0000  -0.0000 292 MET A CB  
2086 C CG  . MET A 292 ? 1.3148 1.3148 1.3148 0.0000  0.0000  -0.0000 292 MET A CG  
2087 S SD  . MET A 292 ? 1.3148 1.3148 1.3148 0.0000  0.0000  -0.0000 292 MET A SD  
2088 C CE  . MET A 292 ? 1.3148 1.3148 1.3148 0.0000  0.0000  -0.0000 292 MET A CE  
2089 N N   . GLY A 293 ? 1.2642 1.2642 1.2642 0.0000  0.0000  -0.0000 293 GLY A N   
2090 C CA  . GLY A 293 ? 1.2642 1.2642 1.2642 0.0000  0.0000  -0.0000 293 GLY A CA  
2091 C C   . GLY A 293 ? 1.2642 1.2642 1.2642 0.0000  0.0000  -0.0000 293 GLY A C   
2092 O O   . GLY A 293 ? 1.2642 1.2642 1.2642 0.0000  0.0000  -0.0000 293 GLY A O   
2093 N N   . ILE A 294 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 294 ILE A N   
2094 C CA  . ILE A 294 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 294 ILE A CA  
2095 C C   . ILE A 294 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 294 ILE A C   
2096 O O   . ILE A 294 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 294 ILE A O   
2097 C CB  . ILE A 294 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 294 ILE A CB  
2098 C CG1 . ILE A 294 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 294 ILE A CG1 
2099 C CG2 . ILE A 294 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 294 ILE A CG2 
2100 C CD1 . ILE A 294 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 294 ILE A CD1 
2101 N N   . SER A 295 ? 1.2408 1.2408 1.2408 -0.0000 0.0000  0.0000  295 SER A N   
2102 C CA  . SER A 295 ? 1.2408 1.2408 1.2408 -0.0000 0.0000  0.0000  295 SER A CA  
2103 C C   . SER A 295 ? 1.2408 1.2408 1.2408 -0.0000 0.0000  0.0000  295 SER A C   
2104 O O   . SER A 295 ? 1.2408 1.2408 1.2408 -0.0000 0.0000  0.0000  295 SER A O   
2105 C CB  . SER A 295 ? 1.2408 1.2408 1.2408 -0.0000 0.0000  0.0000  295 SER A CB  
2106 O OG  . SER A 295 ? 1.2408 1.2408 1.2408 -0.0000 0.0000  0.0000  295 SER A OG  
2107 N N   . GLU A 296 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 296 GLU A N   
2108 C CA  . GLU A 296 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 296 GLU A CA  
2109 C C   . GLU A 296 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 296 GLU A C   
2110 O O   . GLU A 296 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 296 GLU A O   
2111 C CB  . GLU A 296 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 296 GLU A CB  
2112 C CG  . GLU A 296 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 296 GLU A CG  
2113 C CD  . GLU A 296 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 296 GLU A CD  
2114 O OE1 . GLU A 296 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 296 GLU A OE1 
2115 O OE2 . GLU A 296 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 296 GLU A OE2 
2116 N N   . GLY A 297 ? 1.3228 1.3228 1.3228 0.0000  0.0000  -0.0000 297 GLY A N   
2117 C CA  . GLY A 297 ? 1.3228 1.3228 1.3228 0.0000  0.0000  -0.0000 297 GLY A CA  
2118 C C   . GLY A 297 ? 1.3228 1.3228 1.3228 0.0000  0.0000  -0.0000 297 GLY A C   
2119 O O   . GLY A 297 ? 1.3228 1.3228 1.3228 0.0000  0.0000  -0.0000 297 GLY A O   
2120 N N   . ILE A 298 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 298 ILE A N   
2121 C CA  . ILE A 298 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 298 ILE A CA  
2122 C C   . ILE A 298 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 298 ILE A C   
2123 O O   . ILE A 298 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 298 ILE A O   
2124 C CB  . ILE A 298 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 298 ILE A CB  
2125 C CG1 . ILE A 298 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 298 ILE A CG1 
2126 C CG2 . ILE A 298 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 298 ILE A CG2 
2127 C CD1 . ILE A 298 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 298 ILE A CD1 
2128 N N   . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A N   
2129 C CA  . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A CA  
2130 C C   . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A C   
2131 O O   . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A O   
2132 C CB  . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A CB  
2133 C CG  . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A CG  
2134 C CD1 . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A CD1 
2135 C CD2 . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A CD2 
2136 C CE1 . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A CE1 
2137 C CE2 . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A CE2 
2138 C CZ  . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A CZ  
2139 O OH  . TYR A 299 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 299 TYR A OH  
2140 N N   . SER A 300 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 300 SER A N   
2141 C CA  . SER A 300 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 300 SER A CA  
2142 C C   . SER A 300 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 300 SER A C   
2143 O O   . SER A 300 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 300 SER A O   
2144 C CB  . SER A 300 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 300 SER A CB  
2145 O OG  . SER A 300 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 300 SER A OG  
2146 N N   . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A N   
2147 C CA  . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A CA  
2148 C C   . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A C   
2149 O O   . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A O   
2150 C CB  . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A CB  
2151 C CG  . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A CG  
2152 C CD1 . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A CD1 
2153 C CD2 . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A CD2 
2154 C CE1 . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A CE1 
2155 C CE2 . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A CE2 
2156 C CZ  . PHE A 301 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 301 PHE A CZ  
2157 N N   . THR A 302 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 302 THR A N   
2158 C CA  . THR A 302 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 302 THR A CA  
2159 C C   . THR A 302 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 302 THR A C   
2160 O O   . THR A 302 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 302 THR A O   
2161 C CB  . THR A 302 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 302 THR A CB  
2162 O OG1 . THR A 302 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 302 THR A OG1 
2163 C CG2 . THR A 302 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 302 THR A CG2 
2164 N N   . LEU A 303 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 303 LEU A N   
2165 C CA  . LEU A 303 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 303 LEU A CA  
2166 C C   . LEU A 303 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 303 LEU A C   
2167 O O   . LEU A 303 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 303 LEU A O   
2168 C CB  . LEU A 303 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 303 LEU A CB  
2169 C CG  . LEU A 303 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 303 LEU A CG  
2170 C CD1 . LEU A 303 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 303 LEU A CD1 
2171 C CD2 . LEU A 303 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 303 LEU A CD2 
2172 N N   . PRO A 304 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 304 PRO A N   
2173 C CA  . PRO A 304 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 304 PRO A CA  
2174 C C   . PRO A 304 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 304 PRO A C   
2175 O O   . PRO A 304 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 304 PRO A O   
2176 C CB  . PRO A 304 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 304 PRO A CB  
2177 C CG  . PRO A 304 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 304 PRO A CG  
2178 C CD  . PRO A 304 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 304 PRO A CD  
2179 N N   . LEU A 305 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 305 LEU A N   
2180 C CA  . LEU A 305 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 305 LEU A CA  
2181 C C   . LEU A 305 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 305 LEU A C   
2182 O O   . LEU A 305 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 305 LEU A O   
2183 C CB  . LEU A 305 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 305 LEU A CB  
2184 C CG  . LEU A 305 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 305 LEU A CG  
2185 C CD1 . LEU A 305 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 305 LEU A CD1 
2186 C CD2 . LEU A 305 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 305 LEU A CD2 
2187 N N   . GLY A 306 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 306 GLY A N   
2188 C CA  . GLY A 306 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 306 GLY A CA  
2189 C C   . GLY A 306 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 306 GLY A C   
2190 O O   . GLY A 306 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 306 GLY A O   
2191 N N   . ALA A 307 ? 1.2693 1.2693 1.2693 0.0000  -0.0000 0.0000  307 ALA A N   
2192 C CA  . ALA A 307 ? 1.2693 1.2693 1.2693 0.0000  -0.0000 0.0000  307 ALA A CA  
2193 C C   . ALA A 307 ? 1.2693 1.2693 1.2693 0.0000  -0.0000 0.0000  307 ALA A C   
2194 O O   . ALA A 307 ? 1.2693 1.2693 1.2693 0.0000  -0.0000 0.0000  307 ALA A O   
2195 C CB  . ALA A 307 ? 1.2693 1.2693 1.2693 0.0000  -0.0000 0.0000  307 ALA A CB  
2196 N N   . THR A 308 ? 1.2588 1.2588 1.2588 0.0000  0.0000  -0.0000 308 THR A N   
2197 C CA  . THR A 308 ? 1.2588 1.2588 1.2588 0.0000  0.0000  -0.0000 308 THR A CA  
2198 C C   . THR A 308 ? 1.2588 1.2588 1.2588 0.0000  0.0000  -0.0000 308 THR A C   
2199 O O   . THR A 308 ? 1.2588 1.2588 1.2588 0.0000  0.0000  -0.0000 308 THR A O   
2200 C CB  . THR A 308 ? 1.2588 1.2588 1.2588 0.0000  0.0000  -0.0000 308 THR A CB  
2201 O OG1 . THR A 308 ? 1.2588 1.2588 1.2588 0.0000  0.0000  -0.0000 308 THR A OG1 
2202 C CG2 . THR A 308 ? 1.2588 1.2588 1.2588 0.0000  0.0000  -0.0000 308 THR A CG2 
2203 N N   . ILE A 309 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 309 ILE A N   
2204 C CA  . ILE A 309 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 309 ILE A CA  
2205 C C   . ILE A 309 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 309 ILE A C   
2206 O O   . ILE A 309 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 309 ILE A O   
2207 C CB  . ILE A 309 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 309 ILE A CB  
2208 C CG1 . ILE A 309 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 309 ILE A CG1 
2209 C CG2 . ILE A 309 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 309 ILE A CG2 
2210 C CD1 . ILE A 309 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 309 ILE A CD1 
2211 N N   . ASN A 310 ? 1.3040 1.3040 1.3040 -0.0000 0.0000  -0.0000 310 ASN A N   
2212 C CA  . ASN A 310 ? 1.3040 1.3040 1.3040 -0.0000 0.0000  -0.0000 310 ASN A CA  
2213 C C   . ASN A 310 ? 1.3040 1.3040 1.3040 -0.0000 0.0000  -0.0000 310 ASN A C   
2214 O O   . ASN A 310 ? 1.3040 1.3040 1.3040 -0.0000 0.0000  -0.0000 310 ASN A O   
2215 C CB  . ASN A 310 ? 1.3040 1.3040 1.3040 -0.0000 0.0000  -0.0000 310 ASN A CB  
2216 C CG  . ASN A 310 ? 1.3040 1.3040 1.3040 -0.0000 0.0000  -0.0000 310 ASN A CG  
2217 O OD1 . ASN A 310 ? 1.3040 1.3040 1.3040 -0.0000 0.0000  -0.0000 310 ASN A OD1 
2218 N ND2 . ASN A 310 ? 1.3040 1.3040 1.3040 -0.0000 0.0000  -0.0000 310 ASN A ND2 
2219 N N   . MET A 311 ? 1.3535 1.3535 1.3535 -0.0000 0.0000  -0.0000 311 MET A N   
2220 C CA  . MET A 311 ? 1.3535 1.3535 1.3535 -0.0000 0.0000  -0.0000 311 MET A CA  
2221 C C   . MET A 311 ? 1.3535 1.3535 1.3535 -0.0000 0.0000  -0.0000 311 MET A C   
2222 O O   . MET A 311 ? 1.3535 1.3535 1.3535 -0.0000 0.0000  -0.0000 311 MET A O   
2223 C CB  . MET A 311 ? 1.3535 1.3535 1.3535 -0.0000 0.0000  -0.0000 311 MET A CB  
2224 C CG  . MET A 311 ? 1.3535 1.3535 1.3535 -0.0000 0.0000  -0.0000 311 MET A CG  
2225 S SD  . MET A 311 ? 1.3535 1.3535 1.3535 -0.0000 0.0000  -0.0000 311 MET A SD  
2226 C CE  . MET A 311 ? 1.3535 1.3535 1.3535 -0.0000 0.0000  -0.0000 311 MET A CE  
2227 N N   . ASP A 312 ? 1.3577 1.3577 1.3577 0.0000  0.0000  -0.0000 312 ASP A N   
2228 C CA  . ASP A 312 ? 1.3577 1.3577 1.3577 0.0000  0.0000  -0.0000 312 ASP A CA  
2229 C C   . ASP A 312 ? 1.3577 1.3577 1.3577 0.0000  0.0000  -0.0000 312 ASP A C   
2230 O O   . ASP A 312 ? 1.3577 1.3577 1.3577 0.0000  0.0000  -0.0000 312 ASP A O   
2231 C CB  . ASP A 312 ? 1.3577 1.3577 1.3577 0.0000  0.0000  -0.0000 312 ASP A CB  
2232 C CG  . ASP A 312 ? 1.3577 1.3577 1.3577 0.0000  0.0000  -0.0000 312 ASP A CG  
2233 O OD1 . ASP A 312 ? 1.3577 1.3577 1.3577 0.0000  0.0000  -0.0000 312 ASP A OD1 
2234 O OD2 . ASP A 312 ? 1.3577 1.3577 1.3577 0.0000  0.0000  -0.0000 312 ASP A OD2 
2235 N N   . GLY A 313 ? 1.3287 1.3287 1.3287 -0.0000 0.0000  -0.0000 313 GLY A N   
2236 C CA  . GLY A 313 ? 1.3287 1.3287 1.3287 -0.0000 0.0000  -0.0000 313 GLY A CA  
2237 C C   . GLY A 313 ? 1.3287 1.3287 1.3287 -0.0000 0.0000  -0.0000 313 GLY A C   
2238 O O   . GLY A 313 ? 1.3287 1.3287 1.3287 -0.0000 0.0000  -0.0000 313 GLY A O   
2239 N N   . THR A 314 ? 1.3629 1.3629 1.3629 0.0000  0.0000  -0.0000 314 THR A N   
2240 C CA  . THR A 314 ? 1.3629 1.3629 1.3629 0.0000  0.0000  -0.0000 314 THR A CA  
2241 C C   . THR A 314 ? 1.3629 1.3629 1.3629 0.0000  0.0000  -0.0000 314 THR A C   
2242 O O   . THR A 314 ? 1.3629 1.3629 1.3629 0.0000  0.0000  -0.0000 314 THR A O   
2243 C CB  . THR A 314 ? 1.3629 1.3629 1.3629 0.0000  0.0000  -0.0000 314 THR A CB  
2244 O OG1 . THR A 314 ? 1.3629 1.3629 1.3629 0.0000  0.0000  -0.0000 314 THR A OG1 
2245 C CG2 . THR A 314 ? 1.3629 1.3629 1.3629 0.0000  0.0000  -0.0000 314 THR A CG2 
2246 N N   . ALA A 315 ? 1.3665 1.3665 1.3665 0.0000  0.0000  -0.0000 315 ALA A N   
2247 C CA  . ALA A 315 ? 1.3665 1.3665 1.3665 0.0000  0.0000  -0.0000 315 ALA A CA  
2248 C C   . ALA A 315 ? 1.3665 1.3665 1.3665 0.0000  0.0000  -0.0000 315 ALA A C   
2249 O O   . ALA A 315 ? 1.3665 1.3665 1.3665 0.0000  0.0000  -0.0000 315 ALA A O   
2250 C CB  . ALA A 315 ? 1.3665 1.3665 1.3665 0.0000  0.0000  -0.0000 315 ALA A CB  
2251 N N   . LEU A 316 ? 1.2560 1.2560 1.2560 -0.0000 0.0000  -0.0000 316 LEU A N   
2252 C CA  . LEU A 316 ? 1.2560 1.2560 1.2560 -0.0000 0.0000  -0.0000 316 LEU A CA  
2253 C C   . LEU A 316 ? 1.2560 1.2560 1.2560 -0.0000 0.0000  -0.0000 316 LEU A C   
2254 O O   . LEU A 316 ? 1.2560 1.2560 1.2560 -0.0000 0.0000  -0.0000 316 LEU A O   
2255 C CB  . LEU A 316 ? 1.2560 1.2560 1.2560 -0.0000 0.0000  -0.0000 316 LEU A CB  
2256 C CG  . LEU A 316 ? 1.2560 1.2560 1.2560 -0.0000 0.0000  -0.0000 316 LEU A CG  
2257 C CD1 . LEU A 316 ? 1.2560 1.2560 1.2560 -0.0000 0.0000  -0.0000 316 LEU A CD1 
2258 C CD2 . LEU A 316 ? 1.2560 1.2560 1.2560 -0.0000 0.0000  -0.0000 316 LEU A CD2 
2259 N N   . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A N   
2260 C CA  . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A CA  
2261 C C   . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A C   
2262 O O   . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A O   
2263 C CB  . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A CB  
2264 C CG  . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A CG  
2265 C CD1 . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A CD1 
2266 C CD2 . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A CD2 
2267 C CE1 . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A CE1 
2268 C CE2 . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A CE2 
2269 C CZ  . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A CZ  
2270 O OH  . TYR A 317 ? 1.3365 1.3365 1.3365 -0.0000 0.0000  0.0000  317 TYR A OH  
2271 N N   . GLN A 318 ? 1.3953 1.3953 1.3953 0.0000  0.0000  -0.0000 318 GLN A N   
2272 C CA  . GLN A 318 ? 1.3953 1.3953 1.3953 0.0000  0.0000  -0.0000 318 GLN A CA  
2273 C C   . GLN A 318 ? 1.3953 1.3953 1.3953 0.0000  0.0000  -0.0000 318 GLN A C   
2274 O O   . GLN A 318 ? 1.3953 1.3953 1.3953 0.0000  0.0000  -0.0000 318 GLN A O   
2275 C CB  . GLN A 318 ? 1.3953 1.3953 1.3953 0.0000  0.0000  -0.0000 318 GLN A CB  
2276 C CG  . GLN A 318 ? 1.3953 1.3953 1.3953 0.0000  0.0000  -0.0000 318 GLN A CG  
2277 C CD  . GLN A 318 ? 1.3953 1.3953 1.3953 0.0000  0.0000  -0.0000 318 GLN A CD  
2278 O OE1 . GLN A 318 ? 1.3953 1.3953 1.3953 0.0000  0.0000  -0.0000 318 GLN A OE1 
2279 N NE2 . GLN A 318 ? 1.3953 1.3953 1.3953 0.0000  0.0000  -0.0000 318 GLN A NE2 
2280 N N   . GLY A 319 ? 1.3864 1.3864 1.3864 0.0000  -0.0000 0.0000  319 GLY A N   
2281 C CA  . GLY A 319 ? 1.3864 1.3864 1.3864 0.0000  -0.0000 0.0000  319 GLY A CA  
2282 C C   . GLY A 319 ? 1.3864 1.3864 1.3864 0.0000  -0.0000 0.0000  319 GLY A C   
2283 O O   . GLY A 319 ? 1.3864 1.3864 1.3864 0.0000  -0.0000 0.0000  319 GLY A O   
2284 N N   . VAL A 320 ? 1.3488 1.3488 1.3488 -0.0000 -0.0000 0.0000  320 VAL A N   
2285 C CA  . VAL A 320 ? 1.3488 1.3488 1.3488 -0.0000 -0.0000 0.0000  320 VAL A CA  
2286 C C   . VAL A 320 ? 1.3488 1.3488 1.3488 -0.0000 -0.0000 0.0000  320 VAL A C   
2287 O O   . VAL A 320 ? 1.3488 1.3488 1.3488 -0.0000 -0.0000 0.0000  320 VAL A O   
2288 C CB  . VAL A 320 ? 1.3488 1.3488 1.3488 -0.0000 -0.0000 0.0000  320 VAL A CB  
2289 C CG1 . VAL A 320 ? 1.3488 1.3488 1.3488 -0.0000 -0.0000 0.0000  320 VAL A CG1 
2290 C CG2 . VAL A 320 ? 1.3488 1.3488 1.3488 -0.0000 -0.0000 0.0000  320 VAL A CG2 
2291 N N   . CYS A 321 ? 1.3960 1.3960 1.3960 0.0000  0.0000  -0.0000 321 CYS A N   
2292 C CA  . CYS A 321 ? 1.3960 1.3960 1.3960 0.0000  0.0000  -0.0000 321 CYS A CA  
2293 C C   . CYS A 321 ? 1.3960 1.3960 1.3960 0.0000  0.0000  -0.0000 321 CYS A C   
2294 O O   . CYS A 321 ? 1.3960 1.3960 1.3960 0.0000  0.0000  -0.0000 321 CYS A O   
2297 N N   . THR A 322 ? 1.3247 1.3247 1.3247 0.0000  0.0000  -0.0000 322 THR A N   
2298 C CA  . THR A 322 ? 1.3247 1.3247 1.3247 0.0000  0.0000  -0.0000 322 THR A CA  
2299 C C   . THR A 322 ? 1.3247 1.3247 1.3247 0.0000  0.0000  -0.0000 322 THR A C   
2300 O O   . THR A 322 ? 1.3247 1.3247 1.3247 0.0000  0.0000  -0.0000 322 THR A O   
2301 C CB  . THR A 322 ? 1.3247 1.3247 1.3247 0.0000  0.0000  -0.0000 322 THR A CB  
2302 O OG1 . THR A 322 ? 1.3247 1.3247 1.3247 0.0000  0.0000  -0.0000 322 THR A OG1 
2303 C CG2 . THR A 322 ? 1.3247 1.3247 1.3247 0.0000  0.0000  -0.0000 322 THR A CG2 
2304 N N   . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A N   
2305 C CA  . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A CA  
2306 C C   . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A C   
2307 O O   . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A O   
2308 C CB  . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A CB  
2309 C CG  . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A CG  
2310 C CD1 . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A CD1 
2311 C CD2 . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A CD2 
2312 C CE1 . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A CE1 
2313 C CE2 . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A CE2 
2314 C CZ  . PHE A 323 ? 1.3939 1.3939 1.3939 -0.0000 0.0000  -0.0000 323 PHE A CZ  
2315 N N   . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A N   
2316 C CA  . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A CA  
2317 C C   . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A C   
2318 O O   . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A O   
2319 C CB  . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A CB  
2320 C CG  . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A CG  
2321 C CD1 . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A CD1 
2322 C CD2 . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A CD2 
2323 C CE1 . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A CE1 
2324 C CE2 . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A CE2 
2325 C CZ  . PHE A 324 ? 1.3749 1.3749 1.3749 0.0000  0.0000  -0.0000 324 PHE A CZ  
2326 N N   . ILE A 325 ? 1.3854 1.3854 1.3854 0.0000  -0.0000 0.0000  325 ILE A N   
2327 C CA  . ILE A 325 ? 1.3854 1.3854 1.3854 0.0000  -0.0000 0.0000  325 ILE A CA  
2328 C C   . ILE A 325 ? 1.3854 1.3854 1.3854 0.0000  -0.0000 0.0000  325 ILE A C   
2329 O O   . ILE A 325 ? 1.3854 1.3854 1.3854 0.0000  -0.0000 0.0000  325 ILE A O   
2330 C CB  . ILE A 325 ? 1.3854 1.3854 1.3854 0.0000  -0.0000 0.0000  325 ILE A CB  
2331 C CG1 . ILE A 325 ? 1.3854 1.3854 1.3854 0.0000  -0.0000 0.0000  325 ILE A CG1 
2332 C CG2 . ILE A 325 ? 1.3854 1.3854 1.3854 0.0000  -0.0000 0.0000  325 ILE A CG2 
2333 C CD1 . ILE A 325 ? 1.3854 1.3854 1.3854 0.0000  -0.0000 0.0000  325 ILE A CD1 
2334 N N   . ALA A 326 ? 1.4560 1.4560 1.4560 0.0000  0.0000  0.0000  326 ALA A N   
2335 C CA  . ALA A 326 ? 1.4560 1.4560 1.4560 0.0000  0.0000  0.0000  326 ALA A CA  
2336 C C   . ALA A 326 ? 1.4560 1.4560 1.4560 0.0000  0.0000  0.0000  326 ALA A C   
2337 O O   . ALA A 326 ? 1.4560 1.4560 1.4560 0.0000  0.0000  0.0000  326 ALA A O   
2338 C CB  . ALA A 326 ? 1.4560 1.4560 1.4560 0.0000  0.0000  0.0000  326 ALA A CB  
2339 N N   . ASN A 327 ? 1.4491 1.4491 1.4491 0.0000  0.0000  -0.0000 327 ASN A N   
2340 C CA  . ASN A 327 ? 1.4491 1.4491 1.4491 0.0000  0.0000  -0.0000 327 ASN A CA  
2341 C C   . ASN A 327 ? 1.4491 1.4491 1.4491 0.0000  0.0000  -0.0000 327 ASN A C   
2342 O O   . ASN A 327 ? 1.4491 1.4491 1.4491 0.0000  0.0000  -0.0000 327 ASN A O   
2343 C CB  . ASN A 327 ? 1.4491 1.4491 1.4491 0.0000  0.0000  -0.0000 327 ASN A CB  
2344 C CG  . ASN A 327 ? 1.4491 1.4491 1.4491 0.0000  0.0000  -0.0000 327 ASN A CG  
2345 O OD1 . ASN A 327 ? 1.4491 1.4491 1.4491 0.0000  0.0000  -0.0000 327 ASN A OD1 
2346 N ND2 . ASN A 327 ? 1.4491 1.4491 1.4491 0.0000  0.0000  -0.0000 327 ASN A ND2 
2347 N N   . ALA A 328 ? 1.3380 1.3380 1.3380 -0.0000 -0.0000 0.0000  328 ALA A N   
2348 C CA  . ALA A 328 ? 1.3380 1.3380 1.3380 -0.0000 -0.0000 0.0000  328 ALA A CA  
2349 C C   . ALA A 328 ? 1.3380 1.3380 1.3380 -0.0000 -0.0000 0.0000  328 ALA A C   
2350 O O   . ALA A 328 ? 1.3380 1.3380 1.3380 -0.0000 -0.0000 0.0000  328 ALA A O   
2351 C CB  . ALA A 328 ? 1.3380 1.3380 1.3380 -0.0000 -0.0000 0.0000  328 ALA A CB  
2352 N N   . LEU A 329 ? 1.4585 1.4585 1.4585 0.0000  -0.0000 0.0000  329 LEU A N   
2353 C CA  . LEU A 329 ? 1.4585 1.4585 1.4585 0.0000  -0.0000 0.0000  329 LEU A CA  
2354 C C   . LEU A 329 ? 1.4585 1.4585 1.4585 0.0000  -0.0000 0.0000  329 LEU A C   
2355 O O   . LEU A 329 ? 1.4585 1.4585 1.4585 0.0000  -0.0000 0.0000  329 LEU A O   
2356 C CB  . LEU A 329 ? 1.4585 1.4585 1.4585 0.0000  -0.0000 0.0000  329 LEU A CB  
2357 C CG  . LEU A 329 ? 1.4585 1.4585 1.4585 0.0000  -0.0000 0.0000  329 LEU A CG  
2358 C CD1 . LEU A 329 ? 1.4585 1.4585 1.4585 0.0000  -0.0000 0.0000  329 LEU A CD1 
2359 C CD2 . LEU A 329 ? 1.4585 1.4585 1.4585 0.0000  -0.0000 0.0000  329 LEU A CD2 
2380 N N   . LEU A 333 ? 1.5510 1.5510 1.5510 0.0000  0.0000  -0.0000 333 LEU A N   
2381 C CA  . LEU A 333 ? 1.5510 1.5510 1.5510 0.0000  0.0000  -0.0000 333 LEU A CA  
2382 C C   . LEU A 333 ? 1.5510 1.5510 1.5510 0.0000  0.0000  -0.0000 333 LEU A C   
2383 O O   . LEU A 333 ? 1.5510 1.5510 1.5510 0.0000  0.0000  -0.0000 333 LEU A O   
2384 C CB  . LEU A 333 ? 1.5510 1.5510 1.5510 0.0000  0.0000  -0.0000 333 LEU A CB  
2385 C CG  . LEU A 333 ? 1.5510 1.5510 1.5510 0.0000  0.0000  -0.0000 333 LEU A CG  
2386 C CD1 . LEU A 333 ? 1.5510 1.5510 1.5510 0.0000  0.0000  -0.0000 333 LEU A CD1 
2387 C CD2 . LEU A 333 ? 1.5510 1.5510 1.5510 0.0000  0.0000  -0.0000 333 LEU A CD2 
2388 N N   . THR A 334 ? 1.4880 1.4880 1.4880 -0.0000 0.0000  -0.0000 334 THR A N   
2389 C CA  . THR A 334 ? 1.4880 1.4880 1.4880 -0.0000 0.0000  -0.0000 334 THR A CA  
2390 C C   . THR A 334 ? 1.4880 1.4880 1.4880 -0.0000 0.0000  -0.0000 334 THR A C   
2391 O O   . THR A 334 ? 1.4880 1.4880 1.4880 -0.0000 0.0000  -0.0000 334 THR A O   
2392 C CB  . THR A 334 ? 1.4880 1.4880 1.4880 -0.0000 0.0000  -0.0000 334 THR A CB  
2393 O OG1 . THR A 334 ? 1.4880 1.4880 1.4880 -0.0000 0.0000  -0.0000 334 THR A OG1 
2394 C CG2 . THR A 334 ? 1.4880 1.4880 1.4880 -0.0000 0.0000  -0.0000 334 THR A CG2 
2395 N N   . VAL A 335 ? 1.5107 1.5107 1.5107 -0.0000 -0.0000 -0.0000 335 VAL A N   
2396 C CA  . VAL A 335 ? 1.5107 1.5107 1.5107 -0.0000 -0.0000 -0.0000 335 VAL A CA  
2397 C C   . VAL A 335 ? 1.5107 1.5107 1.5107 -0.0000 -0.0000 -0.0000 335 VAL A C   
2398 O O   . VAL A 335 ? 1.5107 1.5107 1.5107 -0.0000 -0.0000 -0.0000 335 VAL A O   
2399 C CB  . VAL A 335 ? 1.5107 1.5107 1.5107 -0.0000 -0.0000 -0.0000 335 VAL A CB  
2400 C CG1 . VAL A 335 ? 1.5107 1.5107 1.5107 -0.0000 -0.0000 -0.0000 335 VAL A CG1 
2401 C CG2 . VAL A 335 ? 1.5107 1.5107 1.5107 -0.0000 -0.0000 -0.0000 335 VAL A CG2 
2402 N N   . GLY A 336 ? 1.5688 1.5688 1.5688 0.0000  0.0000  -0.0000 336 GLY A N   
2403 C CA  . GLY A 336 ? 1.5688 1.5688 1.5688 0.0000  0.0000  -0.0000 336 GLY A CA  
2404 C C   . GLY A 336 ? 1.5688 1.5688 1.5688 0.0000  0.0000  -0.0000 336 GLY A C   
2405 O O   . GLY A 336 ? 1.5688 1.5688 1.5688 0.0000  0.0000  -0.0000 336 GLY A O   
2406 N N   . GLN A 337 ? 1.5367 1.5367 1.5367 -0.0000 -0.0000 -0.0000 337 GLN A N   
2407 C CA  . GLN A 337 ? 1.5367 1.5367 1.5367 -0.0000 -0.0000 -0.0000 337 GLN A CA  
2408 C C   . GLN A 337 ? 1.5367 1.5367 1.5367 -0.0000 -0.0000 -0.0000 337 GLN A C   
2409 O O   . GLN A 337 ? 1.5367 1.5367 1.5367 -0.0000 -0.0000 -0.0000 337 GLN A O   
2410 C CB  . GLN A 337 ? 1.5367 1.5367 1.5367 -0.0000 -0.0000 -0.0000 337 GLN A CB  
2411 C CG  . GLN A 337 ? 1.5367 1.5367 1.5367 -0.0000 -0.0000 -0.0000 337 GLN A CG  
2412 C CD  . GLN A 337 ? 1.5367 1.5367 1.5367 -0.0000 -0.0000 -0.0000 337 GLN A CD  
2413 O OE1 . GLN A 337 ? 1.5367 1.5367 1.5367 -0.0000 -0.0000 -0.0000 337 GLN A OE1 
2414 N NE2 . GLN A 337 ? 1.5367 1.5367 1.5367 -0.0000 -0.0000 -0.0000 337 GLN A NE2 
2415 N N   . GLN A 338 ? 1.4391 1.4391 1.4391 0.0000  0.0000  -0.0000 338 GLN A N   
2416 C CA  . GLN A 338 ? 1.4391 1.4391 1.4391 0.0000  0.0000  -0.0000 338 GLN A CA  
2417 C C   . GLN A 338 ? 1.4391 1.4391 1.4391 0.0000  0.0000  -0.0000 338 GLN A C   
2418 O O   . GLN A 338 ? 1.4391 1.4391 1.4391 0.0000  0.0000  -0.0000 338 GLN A O   
2419 C CB  . GLN A 338 ? 1.4391 1.4391 1.4391 0.0000  0.0000  -0.0000 338 GLN A CB  
2420 C CG  . GLN A 338 ? 1.4391 1.4391 1.4391 0.0000  0.0000  -0.0000 338 GLN A CG  
2421 C CD  . GLN A 338 ? 1.4391 1.4391 1.4391 0.0000  0.0000  -0.0000 338 GLN A CD  
2422 O OE1 . GLN A 338 ? 1.4391 1.4391 1.4391 0.0000  0.0000  -0.0000 338 GLN A OE1 
2423 N NE2 . GLN A 338 ? 1.4391 1.4391 1.4391 0.0000  0.0000  -0.0000 338 GLN A NE2 
2424 N N   . LEU A 339 ? 1.4359 1.4359 1.4359 -0.0000 0.0000  -0.0000 339 LEU A N   
2425 C CA  . LEU A 339 ? 1.4359 1.4359 1.4359 -0.0000 0.0000  -0.0000 339 LEU A CA  
2426 C C   . LEU A 339 ? 1.4359 1.4359 1.4359 -0.0000 0.0000  -0.0000 339 LEU A C   
2427 O O   . LEU A 339 ? 1.4359 1.4359 1.4359 -0.0000 0.0000  -0.0000 339 LEU A O   
2428 C CB  . LEU A 339 ? 1.4359 1.4359 1.4359 -0.0000 0.0000  -0.0000 339 LEU A CB  
2429 C CG  . LEU A 339 ? 1.4359 1.4359 1.4359 -0.0000 0.0000  -0.0000 339 LEU A CG  
2430 C CD1 . LEU A 339 ? 1.4359 1.4359 1.4359 -0.0000 0.0000  -0.0000 339 LEU A CD1 
2431 C CD2 . LEU A 339 ? 1.4359 1.4359 1.4359 -0.0000 0.0000  -0.0000 339 LEU A CD2 
2432 N N   . THR A 340 ? 1.4241 1.4241 1.4241 0.0000  0.0000  -0.0000 340 THR A N   
2433 C CA  . THR A 340 ? 1.4241 1.4241 1.4241 0.0000  0.0000  -0.0000 340 THR A CA  
2434 C C   . THR A 340 ? 1.4241 1.4241 1.4241 0.0000  0.0000  -0.0000 340 THR A C   
2435 O O   . THR A 340 ? 1.4241 1.4241 1.4241 0.0000  0.0000  -0.0000 340 THR A O   
2436 C CB  . THR A 340 ? 1.4241 1.4241 1.4241 0.0000  0.0000  -0.0000 340 THR A CB  
2437 O OG1 . THR A 340 ? 1.4241 1.4241 1.4241 0.0000  0.0000  -0.0000 340 THR A OG1 
2438 C CG2 . THR A 340 ? 1.4241 1.4241 1.4241 0.0000  0.0000  -0.0000 340 THR A CG2 
2439 N N   . ILE A 341 ? 1.3297 1.3297 1.3297 0.0000  0.0000  -0.0000 341 ILE A N   
2440 C CA  . ILE A 341 ? 1.3297 1.3297 1.3297 0.0000  0.0000  -0.0000 341 ILE A CA  
2441 C C   . ILE A 341 ? 1.3297 1.3297 1.3297 0.0000  0.0000  -0.0000 341 ILE A C   
2442 O O   . ILE A 341 ? 1.3297 1.3297 1.3297 0.0000  0.0000  -0.0000 341 ILE A O   
2443 C CB  . ILE A 341 ? 1.3297 1.3297 1.3297 0.0000  0.0000  -0.0000 341 ILE A CB  
2444 C CG1 . ILE A 341 ? 1.3297 1.3297 1.3297 0.0000  0.0000  -0.0000 341 ILE A CG1 
2445 C CG2 . ILE A 341 ? 1.3297 1.3297 1.3297 0.0000  0.0000  -0.0000 341 ILE A CG2 
2446 C CD1 . ILE A 341 ? 1.3297 1.3297 1.3297 0.0000  0.0000  -0.0000 341 ILE A CD1 
2447 N N   . VAL A 342 ? 1.3680 1.3680 1.3680 -0.0000 0.0000  -0.0000 342 VAL A N   
2448 C CA  . VAL A 342 ? 1.3680 1.3680 1.3680 -0.0000 0.0000  -0.0000 342 VAL A CA  
2449 C C   . VAL A 342 ? 1.3680 1.3680 1.3680 -0.0000 0.0000  -0.0000 342 VAL A C   
2450 O O   . VAL A 342 ? 1.3680 1.3680 1.3680 -0.0000 0.0000  -0.0000 342 VAL A O   
2451 C CB  . VAL A 342 ? 1.3680 1.3680 1.3680 -0.0000 0.0000  -0.0000 342 VAL A CB  
2452 C CG1 . VAL A 342 ? 1.3680 1.3680 1.3680 -0.0000 0.0000  -0.0000 342 VAL A CG1 
2453 C CG2 . VAL A 342 ? 1.3680 1.3680 1.3680 -0.0000 0.0000  -0.0000 342 VAL A CG2 
2454 N N   . LEU A 343 ? 1.3258 1.3258 1.3258 0.0000  0.0000  0.0000  343 LEU A N   
2455 C CA  . LEU A 343 ? 1.3258 1.3258 1.3258 0.0000  0.0000  0.0000  343 LEU A CA  
2456 C C   . LEU A 343 ? 1.3258 1.3258 1.3258 0.0000  0.0000  0.0000  343 LEU A C   
2457 O O   . LEU A 343 ? 1.3258 1.3258 1.3258 0.0000  0.0000  0.0000  343 LEU A O   
2458 C CB  . LEU A 343 ? 1.3258 1.3258 1.3258 0.0000  0.0000  0.0000  343 LEU A CB  
2459 C CG  . LEU A 343 ? 1.3258 1.3258 1.3258 0.0000  0.0000  0.0000  343 LEU A CG  
2460 C CD1 . LEU A 343 ? 1.3258 1.3258 1.3258 0.0000  0.0000  0.0000  343 LEU A CD1 
2461 C CD2 . LEU A 343 ? 1.3258 1.3258 1.3258 0.0000  0.0000  0.0000  343 LEU A CD2 
2462 N N   . THR A 344 ? 1.3595 1.3595 1.3595 0.0000  0.0000  -0.0000 344 THR A N   
2463 C CA  . THR A 344 ? 1.3595 1.3595 1.3595 0.0000  0.0000  -0.0000 344 THR A CA  
2464 C C   . THR A 344 ? 1.3595 1.3595 1.3595 0.0000  0.0000  -0.0000 344 THR A C   
2465 O O   . THR A 344 ? 1.3595 1.3595 1.3595 0.0000  0.0000  -0.0000 344 THR A O   
2466 C CB  . THR A 344 ? 1.3595 1.3595 1.3595 0.0000  0.0000  -0.0000 344 THR A CB  
2467 O OG1 . THR A 344 ? 1.3595 1.3595 1.3595 0.0000  0.0000  -0.0000 344 THR A OG1 
2468 C CG2 . THR A 344 ? 1.3595 1.3595 1.3595 0.0000  0.0000  -0.0000 344 THR A CG2 
2469 N N   . ALA A 345 ? 1.3091 1.3091 1.3091 0.0000  0.0000  -0.0000 345 ALA A N   
2470 C CA  . ALA A 345 ? 1.3091 1.3091 1.3091 0.0000  0.0000  -0.0000 345 ALA A CA  
2471 C C   . ALA A 345 ? 1.3091 1.3091 1.3091 0.0000  0.0000  -0.0000 345 ALA A C   
2472 O O   . ALA A 345 ? 1.3091 1.3091 1.3091 0.0000  0.0000  -0.0000 345 ALA A O   
2473 C CB  . ALA A 345 ? 1.3091 1.3091 1.3091 0.0000  0.0000  -0.0000 345 ALA A CB  
2474 N N   . VAL A 346 ? 1.3616 1.3616 1.3616 0.0000  0.0000  -0.0000 346 VAL A N   
2475 C CA  . VAL A 346 ? 1.3616 1.3616 1.3616 0.0000  0.0000  -0.0000 346 VAL A CA  
2476 C C   . VAL A 346 ? 1.3616 1.3616 1.3616 0.0000  0.0000  -0.0000 346 VAL A C   
2477 O O   . VAL A 346 ? 1.3616 1.3616 1.3616 0.0000  0.0000  -0.0000 346 VAL A O   
2478 C CB  . VAL A 346 ? 1.3616 1.3616 1.3616 0.0000  0.0000  -0.0000 346 VAL A CB  
2479 C CG1 . VAL A 346 ? 1.3616 1.3616 1.3616 0.0000  0.0000  -0.0000 346 VAL A CG1 
2480 C CG2 . VAL A 346 ? 1.3616 1.3616 1.3616 0.0000  0.0000  -0.0000 346 VAL A CG2 
2481 N N   . LEU A 347 ? 1.3733 1.3733 1.3733 0.0000  0.0000  -0.0000 347 LEU A N   
2482 C CA  . LEU A 347 ? 1.3733 1.3733 1.3733 0.0000  0.0000  -0.0000 347 LEU A CA  
2483 C C   . LEU A 347 ? 1.3733 1.3733 1.3733 0.0000  0.0000  -0.0000 347 LEU A C   
2484 O O   . LEU A 347 ? 1.3733 1.3733 1.3733 0.0000  0.0000  -0.0000 347 LEU A O   
2485 C CB  . LEU A 347 ? 1.3733 1.3733 1.3733 0.0000  0.0000  -0.0000 347 LEU A CB  
2486 C CG  . LEU A 347 ? 1.3733 1.3733 1.3733 0.0000  0.0000  -0.0000 347 LEU A CG  
2487 C CD1 . LEU A 347 ? 1.3733 1.3733 1.3733 0.0000  0.0000  -0.0000 347 LEU A CD1 
2488 C CD2 . LEU A 347 ? 1.3733 1.3733 1.3733 0.0000  0.0000  -0.0000 347 LEU A CD2 
2489 N N   . ALA A 348 ? 1.4006 1.4006 1.4006 -0.0000 0.0000  0.0000  348 ALA A N   
2490 C CA  . ALA A 348 ? 1.4006 1.4006 1.4006 -0.0000 0.0000  0.0000  348 ALA A CA  
2491 C C   . ALA A 348 ? 1.4006 1.4006 1.4006 -0.0000 0.0000  0.0000  348 ALA A C   
2492 O O   . ALA A 348 ? 1.4006 1.4006 1.4006 -0.0000 0.0000  0.0000  348 ALA A O   
2493 C CB  . ALA A 348 ? 1.4006 1.4006 1.4006 -0.0000 0.0000  0.0000  348 ALA A CB  
2494 N N   . SER A 349 ? 1.3690 1.3690 1.3690 0.0000  0.0000  -0.0000 349 SER A N   
2495 C CA  . SER A 349 ? 1.3690 1.3690 1.3690 0.0000  0.0000  -0.0000 349 SER A CA  
2496 C C   . SER A 349 ? 1.3690 1.3690 1.3690 0.0000  0.0000  -0.0000 349 SER A C   
2497 O O   . SER A 349 ? 1.3690 1.3690 1.3690 0.0000  0.0000  -0.0000 349 SER A O   
2498 C CB  . SER A 349 ? 1.3690 1.3690 1.3690 0.0000  0.0000  -0.0000 349 SER A CB  
2499 O OG  . SER A 349 ? 1.3690 1.3690 1.3690 0.0000  0.0000  -0.0000 349 SER A OG  
2500 N N   . ILE A 350 ? 1.4350 1.4350 1.4350 -0.0000 0.0000  -0.0000 350 ILE A N   
2501 C CA  . ILE A 350 ? 1.4350 1.4350 1.4350 -0.0000 0.0000  -0.0000 350 ILE A CA  
2502 C C   . ILE A 350 ? 1.4350 1.4350 1.4350 -0.0000 0.0000  -0.0000 350 ILE A C   
2503 O O   . ILE A 350 ? 1.4350 1.4350 1.4350 -0.0000 0.0000  -0.0000 350 ILE A O   
2504 C CB  . ILE A 350 ? 1.4350 1.4350 1.4350 -0.0000 0.0000  -0.0000 350 ILE A CB  
2505 C CG1 . ILE A 350 ? 1.4350 1.4350 1.4350 -0.0000 0.0000  -0.0000 350 ILE A CG1 
2506 C CG2 . ILE A 350 ? 1.4350 1.4350 1.4350 -0.0000 0.0000  -0.0000 350 ILE A CG2 
2507 C CD1 . ILE A 350 ? 1.4350 1.4350 1.4350 -0.0000 0.0000  -0.0000 350 ILE A CD1 
2508 N N   . GLY A 351 ? 1.3515 1.3515 1.3515 0.0000  0.0000  -0.0000 351 GLY A N   
2509 C CA  . GLY A 351 ? 1.3515 1.3515 1.3515 0.0000  0.0000  -0.0000 351 GLY A CA  
2510 C C   . GLY A 351 ? 1.3515 1.3515 1.3515 0.0000  0.0000  -0.0000 351 GLY A C   
2511 O O   . GLY A 351 ? 1.3515 1.3515 1.3515 0.0000  0.0000  -0.0000 351 GLY A O   
2512 N N   . THR A 352 ? 1.3632 1.3632 1.3632 0.0000  -0.0000 -0.0000 352 THR A N   
2513 C CA  . THR A 352 ? 1.3632 1.3632 1.3632 0.0000  -0.0000 -0.0000 352 THR A CA  
2514 C C   . THR A 352 ? 1.3632 1.3632 1.3632 0.0000  -0.0000 -0.0000 352 THR A C   
2515 O O   . THR A 352 ? 1.3632 1.3632 1.3632 0.0000  -0.0000 -0.0000 352 THR A O   
2516 C CB  . THR A 352 ? 1.3632 1.3632 1.3632 0.0000  -0.0000 -0.0000 352 THR A CB  
2517 O OG1 . THR A 352 ? 1.3632 1.3632 1.3632 0.0000  -0.0000 -0.0000 352 THR A OG1 
2518 C CG2 . THR A 352 ? 1.3632 1.3632 1.3632 0.0000  -0.0000 -0.0000 352 THR A CG2 
2519 N N   . ALA A 353 ? 1.2640 1.2640 1.2640 0.0000  0.0000  -0.0000 353 ALA A N   
2520 C CA  . ALA A 353 ? 1.2640 1.2640 1.2640 0.0000  0.0000  -0.0000 353 ALA A CA  
2521 C C   . ALA A 353 ? 1.2640 1.2640 1.2640 0.0000  0.0000  -0.0000 353 ALA A C   
2522 O O   . ALA A 353 ? 1.2640 1.2640 1.2640 0.0000  0.0000  -0.0000 353 ALA A O   
2523 C CB  . ALA A 353 ? 1.2640 1.2640 1.2640 0.0000  0.0000  -0.0000 353 ALA A CB  
2524 N N   . GLY A 354 ? 1.3090 1.3090 1.3090 0.0000  -0.0000 0.0000  354 GLY A N   
2525 C CA  . GLY A 354 ? 1.3090 1.3090 1.3090 0.0000  -0.0000 0.0000  354 GLY A CA  
2526 C C   . GLY A 354 ? 1.3090 1.3090 1.3090 0.0000  -0.0000 0.0000  354 GLY A C   
2527 O O   . GLY A 354 ? 1.3090 1.3090 1.3090 0.0000  -0.0000 0.0000  354 GLY A O   
2528 N N   . VAL A 355 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 355 VAL A N   
2529 C CA  . VAL A 355 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 355 VAL A CA  
2530 C C   . VAL A 355 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 355 VAL A C   
2531 O O   . VAL A 355 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 355 VAL A O   
2532 C CB  . VAL A 355 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 355 VAL A CB  
2533 C CG1 . VAL A 355 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 355 VAL A CG1 
2534 C CG2 . VAL A 355 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 355 VAL A CG2 
2535 N N   . PRO A 356 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 356 PRO A N   
2536 C CA  . PRO A 356 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 356 PRO A CA  
2537 C C   . PRO A 356 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 356 PRO A C   
2538 O O   . PRO A 356 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 356 PRO A O   
2539 C CB  . PRO A 356 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 356 PRO A CB  
2540 C CG  . PRO A 356 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 356 PRO A CG  
2541 C CD  . PRO A 356 ? 1.2394 1.2394 1.2394 0.0000  0.0000  -0.0000 356 PRO A CD  
2542 N N   . GLY A 357 ? 1.3110 1.3110 1.3110 0.0000  0.0000  -0.0000 357 GLY A N   
2543 C CA  . GLY A 357 ? 1.3110 1.3110 1.3110 0.0000  0.0000  -0.0000 357 GLY A CA  
2544 C C   . GLY A 357 ? 1.3110 1.3110 1.3110 0.0000  0.0000  -0.0000 357 GLY A C   
2545 O O   . GLY A 357 ? 1.3110 1.3110 1.3110 0.0000  0.0000  -0.0000 357 GLY A O   
2546 N N   . ALA A 358 ? 1.3584 1.3584 1.3584 0.0000  0.0000  -0.0000 358 ALA A N   
2547 C CA  . ALA A 358 ? 1.3584 1.3584 1.3584 0.0000  0.0000  -0.0000 358 ALA A CA  
2548 C C   . ALA A 358 ? 1.3584 1.3584 1.3584 0.0000  0.0000  -0.0000 358 ALA A C   
2549 O O   . ALA A 358 ? 1.3584 1.3584 1.3584 0.0000  0.0000  -0.0000 358 ALA A O   
2550 C CB  . ALA A 358 ? 1.3584 1.3584 1.3584 0.0000  0.0000  -0.0000 358 ALA A CB  
2551 N N   . GLY A 359 ? 1.3707 1.3707 1.3707 0.0000  0.0000  0.0000  359 GLY A N   
2552 C CA  . GLY A 359 ? 1.3707 1.3707 1.3707 0.0000  0.0000  0.0000  359 GLY A CA  
2553 C C   . GLY A 359 ? 1.3707 1.3707 1.3707 0.0000  0.0000  0.0000  359 GLY A C   
2554 O O   . GLY A 359 ? 1.3707 1.3707 1.3707 0.0000  0.0000  0.0000  359 GLY A O   
2555 N N   . ALA A 360 ? 1.4540 1.4540 1.4540 0.0000  0.0000  -0.0000 360 ALA A N   
2556 C CA  . ALA A 360 ? 1.4540 1.4540 1.4540 0.0000  0.0000  -0.0000 360 ALA A CA  
2557 C C   . ALA A 360 ? 1.4540 1.4540 1.4540 0.0000  0.0000  -0.0000 360 ALA A C   
2558 O O   . ALA A 360 ? 1.4540 1.4540 1.4540 0.0000  0.0000  -0.0000 360 ALA A O   
2559 C CB  . ALA A 360 ? 1.4540 1.4540 1.4540 0.0000  0.0000  -0.0000 360 ALA A CB  
2560 N N   . ILE A 361 ? 1.4951 1.4951 1.4951 0.0000  0.0000  -0.0000 361 ILE A N   
2561 C CA  . ILE A 361 ? 1.4951 1.4951 1.4951 0.0000  0.0000  -0.0000 361 ILE A CA  
2562 C C   . ILE A 361 ? 1.4951 1.4951 1.4951 0.0000  0.0000  -0.0000 361 ILE A C   
2563 O O   . ILE A 361 ? 1.4951 1.4951 1.4951 0.0000  0.0000  -0.0000 361 ILE A O   
2564 C CB  . ILE A 361 ? 1.4951 1.4951 1.4951 0.0000  0.0000  -0.0000 361 ILE A CB  
2565 C CG1 . ILE A 361 ? 1.4951 1.4951 1.4951 0.0000  0.0000  -0.0000 361 ILE A CG1 
2566 C CG2 . ILE A 361 ? 1.4951 1.4951 1.4951 0.0000  0.0000  -0.0000 361 ILE A CG2 
2567 C CD1 . ILE A 361 ? 1.4951 1.4951 1.4951 0.0000  0.0000  -0.0000 361 ILE A CD1 
2568 N N   . MET A 362 ? 1.5837 1.5837 1.5837 0.0000  0.0000  -0.0000 362 MET A N   
2569 C CA  . MET A 362 ? 1.5837 1.5837 1.5837 0.0000  0.0000  -0.0000 362 MET A CA  
2570 C C   . MET A 362 ? 1.5837 1.5837 1.5837 0.0000  0.0000  -0.0000 362 MET A C   
2571 O O   . MET A 362 ? 1.5837 1.5837 1.5837 0.0000  0.0000  -0.0000 362 MET A O   
2572 C CB  . MET A 362 ? 1.5837 1.5837 1.5837 0.0000  0.0000  -0.0000 362 MET A CB  
2573 C CG  . MET A 362 ? 1.5837 1.5837 1.5837 0.0000  0.0000  -0.0000 362 MET A CG  
2574 S SD  . MET A 362 ? 1.5837 1.5837 1.5837 0.0000  0.0000  -0.0000 362 MET A SD  
2575 C CE  . MET A 362 ? 1.5837 1.5837 1.5837 0.0000  0.0000  -0.0000 362 MET A CE  
2576 N N   . LEU A 363 ? 1.4053 1.4053 1.4053 0.0000  0.0000  -0.0000 363 LEU A N   
2577 C CA  . LEU A 363 ? 1.4053 1.4053 1.4053 0.0000  0.0000  -0.0000 363 LEU A CA  
2578 C C   . LEU A 363 ? 1.4053 1.4053 1.4053 0.0000  0.0000  -0.0000 363 LEU A C   
2579 O O   . LEU A 363 ? 1.4053 1.4053 1.4053 0.0000  0.0000  -0.0000 363 LEU A O   
2580 C CB  . LEU A 363 ? 1.4053 1.4053 1.4053 0.0000  0.0000  -0.0000 363 LEU A CB  
2581 C CG  . LEU A 363 ? 1.4053 1.4053 1.4053 0.0000  0.0000  -0.0000 363 LEU A CG  
2582 C CD1 . LEU A 363 ? 1.4053 1.4053 1.4053 0.0000  0.0000  -0.0000 363 LEU A CD1 
2583 C CD2 . LEU A 363 ? 1.4053 1.4053 1.4053 0.0000  0.0000  -0.0000 363 LEU A CD2 
2584 N N   . ALA A 364 ? 1.4968 1.4968 1.4968 -0.0000 -0.0000 -0.0000 364 ALA A N   
2585 C CA  . ALA A 364 ? 1.4968 1.4968 1.4968 -0.0000 -0.0000 -0.0000 364 ALA A CA  
2586 C C   . ALA A 364 ? 1.4968 1.4968 1.4968 -0.0000 -0.0000 -0.0000 364 ALA A C   
2587 O O   . ALA A 364 ? 1.4968 1.4968 1.4968 -0.0000 -0.0000 -0.0000 364 ALA A O   
2588 C CB  . ALA A 364 ? 1.4968 1.4968 1.4968 -0.0000 -0.0000 -0.0000 364 ALA A CB  
2589 N N   . MET A 365 ? 1.5318 1.5318 1.5318 0.0000  0.0000  0.0000  365 MET A N   
2590 C CA  . MET A 365 ? 1.5318 1.5318 1.5318 0.0000  0.0000  0.0000  365 MET A CA  
2591 C C   . MET A 365 ? 1.5318 1.5318 1.5318 0.0000  0.0000  0.0000  365 MET A C   
2592 O O   . MET A 365 ? 1.5318 1.5318 1.5318 0.0000  0.0000  0.0000  365 MET A O   
2593 C CB  . MET A 365 ? 1.5318 1.5318 1.5318 0.0000  0.0000  0.0000  365 MET A CB  
2594 C CG  . MET A 365 ? 1.5318 1.5318 1.5318 0.0000  0.0000  0.0000  365 MET A CG  
2595 S SD  . MET A 365 ? 1.5318 1.5318 1.5318 0.0000  0.0000  0.0000  365 MET A SD  
2596 C CE  . MET A 365 ? 1.5318 1.5318 1.5318 0.0000  0.0000  0.0000  365 MET A CE  
2597 N N   . VAL A 366 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 366 VAL A N   
2598 C CA  . VAL A 366 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 366 VAL A CA  
2599 C C   . VAL A 366 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 366 VAL A C   
2600 O O   . VAL A 366 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 366 VAL A O   
2601 C CB  . VAL A 366 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 366 VAL A CB  
2602 C CG1 . VAL A 366 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 366 VAL A CG1 
2603 C CG2 . VAL A 366 ? 1.4058 1.4058 1.4058 0.0000  0.0000  -0.0000 366 VAL A CG2 
2604 N N   . LEU A 367 ? 1.4145 1.4145 1.4145 0.0000  0.0000  -0.0000 367 LEU A N   
2605 C CA  . LEU A 367 ? 1.4145 1.4145 1.4145 0.0000  0.0000  -0.0000 367 LEU A CA  
2606 C C   . LEU A 367 ? 1.4145 1.4145 1.4145 0.0000  0.0000  -0.0000 367 LEU A C   
2607 O O   . LEU A 367 ? 1.4145 1.4145 1.4145 0.0000  0.0000  -0.0000 367 LEU A O   
2608 C CB  . LEU A 367 ? 1.4145 1.4145 1.4145 0.0000  0.0000  -0.0000 367 LEU A CB  
2609 C CG  . LEU A 367 ? 1.4145 1.4145 1.4145 0.0000  0.0000  -0.0000 367 LEU A CG  
2610 C CD1 . LEU A 367 ? 1.4145 1.4145 1.4145 0.0000  0.0000  -0.0000 367 LEU A CD1 
2611 C CD2 . LEU A 367 ? 1.4145 1.4145 1.4145 0.0000  0.0000  -0.0000 367 LEU A CD2 
2612 N N   . HIS A 368 ? 1.4381 1.4381 1.4381 0.0000  0.0000  -0.0000 368 HIS A N   
2613 C CA  . HIS A 368 ? 1.4381 1.4381 1.4381 0.0000  0.0000  -0.0000 368 HIS A CA  
2614 C C   . HIS A 368 ? 1.4381 1.4381 1.4381 0.0000  0.0000  -0.0000 368 HIS A C   
2615 O O   . HIS A 368 ? 1.4381 1.4381 1.4381 0.0000  0.0000  -0.0000 368 HIS A O   
2616 C CB  . HIS A 368 ? 1.4381 1.4381 1.4381 0.0000  0.0000  -0.0000 368 HIS A CB  
2617 C CG  . HIS A 368 ? 1.4381 1.4381 1.4381 0.0000  0.0000  -0.0000 368 HIS A CG  
2618 N ND1 . HIS A 368 ? 1.4381 1.4381 1.4381 0.0000  0.0000  -0.0000 368 HIS A ND1 
2619 C CD2 . HIS A 368 ? 1.4381 1.4381 1.4381 0.0000  0.0000  -0.0000 368 HIS A CD2 
2620 C CE1 . HIS A 368 ? 1.4381 1.4381 1.4381 0.0000  0.0000  -0.0000 368 HIS A CE1 
2621 N NE2 . HIS A 368 ? 1.4381 1.4381 1.4381 0.0000  0.0000  -0.0000 368 HIS A NE2 
2622 N N   . SER A 369 ? 1.4679 1.4679 1.4679 0.0000  0.0000  -0.0000 369 SER A N   
2623 C CA  . SER A 369 ? 1.4679 1.4679 1.4679 0.0000  0.0000  -0.0000 369 SER A CA  
2624 C C   . SER A 369 ? 1.4679 1.4679 1.4679 0.0000  0.0000  -0.0000 369 SER A C   
2625 O O   . SER A 369 ? 1.4679 1.4679 1.4679 0.0000  0.0000  -0.0000 369 SER A O   
2626 C CB  . SER A 369 ? 1.4679 1.4679 1.4679 0.0000  0.0000  -0.0000 369 SER A CB  
2627 O OG  . SER A 369 ? 1.4679 1.4679 1.4679 0.0000  0.0000  -0.0000 369 SER A OG  
2628 N N   . VAL A 370 ? 1.3578 1.3578 1.3578 0.0000  0.0000  -0.0000 370 VAL A N   
2629 C CA  . VAL A 370 ? 1.3578 1.3578 1.3578 0.0000  0.0000  -0.0000 370 VAL A CA  
2630 C C   . VAL A 370 ? 1.3578 1.3578 1.3578 0.0000  0.0000  -0.0000 370 VAL A C   
2631 O O   . VAL A 370 ? 1.3578 1.3578 1.3578 0.0000  0.0000  -0.0000 370 VAL A O   
2632 C CB  . VAL A 370 ? 1.3578 1.3578 1.3578 0.0000  0.0000  -0.0000 370 VAL A CB  
2633 C CG1 . VAL A 370 ? 1.3578 1.3578 1.3578 0.0000  0.0000  -0.0000 370 VAL A CG1 
2634 C CG2 . VAL A 370 ? 1.3578 1.3578 1.3578 0.0000  0.0000  -0.0000 370 VAL A CG2 
2635 N N   . GLY A 371 ? 1.5114 1.5114 1.5114 0.0000  0.0000  -0.0000 371 GLY A N   
2636 C CA  . GLY A 371 ? 1.5114 1.5114 1.5114 0.0000  0.0000  -0.0000 371 GLY A CA  
2637 C C   . GLY A 371 ? 1.5114 1.5114 1.5114 0.0000  0.0000  -0.0000 371 GLY A C   
2638 O O   . GLY A 371 ? 1.5114 1.5114 1.5114 0.0000  0.0000  -0.0000 371 GLY A O   
2639 N N   . LEU A 372 ? 1.4974 1.4974 1.4974 0.0000  0.0000  -0.0000 372 LEU A N   
2640 C CA  . LEU A 372 ? 1.4974 1.4974 1.4974 0.0000  0.0000  -0.0000 372 LEU A CA  
2641 C C   . LEU A 372 ? 1.4974 1.4974 1.4974 0.0000  0.0000  -0.0000 372 LEU A C   
2642 O O   . LEU A 372 ? 1.4974 1.4974 1.4974 0.0000  0.0000  -0.0000 372 LEU A O   
2643 C CB  . LEU A 372 ? 1.4974 1.4974 1.4974 0.0000  0.0000  -0.0000 372 LEU A CB  
2644 C CG  . LEU A 372 ? 1.4974 1.4974 1.4974 0.0000  0.0000  -0.0000 372 LEU A CG  
2645 C CD1 . LEU A 372 ? 1.4974 1.4974 1.4974 0.0000  0.0000  -0.0000 372 LEU A CD1 
2646 C CD2 . LEU A 372 ? 1.4974 1.4974 1.4974 0.0000  0.0000  -0.0000 372 LEU A CD2 
2647 N N   . PRO A 373 ? 1.5566 1.5566 1.5566 0.0000  -0.0000 0.0000  373 PRO A N   
2648 C CA  . PRO A 373 ? 1.5566 1.5566 1.5566 0.0000  -0.0000 0.0000  373 PRO A CA  
2649 C C   . PRO A 373 ? 1.5566 1.5566 1.5566 0.0000  -0.0000 0.0000  373 PRO A C   
2650 O O   . PRO A 373 ? 1.5566 1.5566 1.5566 0.0000  -0.0000 0.0000  373 PRO A O   
2651 C CB  . PRO A 373 ? 1.5566 1.5566 1.5566 0.0000  -0.0000 0.0000  373 PRO A CB  
2652 C CG  . PRO A 373 ? 1.5566 1.5566 1.5566 0.0000  -0.0000 0.0000  373 PRO A CG  
2653 C CD  . PRO A 373 ? 1.5566 1.5566 1.5566 0.0000  -0.0000 0.0000  373 PRO A CD  
2654 N N   . LEU A 374 ? 1.6345 1.6345 1.6345 0.0000  0.0000  -0.0000 374 LEU A N   
2655 C CA  . LEU A 374 ? 1.6345 1.6345 1.6345 0.0000  0.0000  -0.0000 374 LEU A CA  
2656 C C   . LEU A 374 ? 1.6345 1.6345 1.6345 0.0000  0.0000  -0.0000 374 LEU A C   
2657 O O   . LEU A 374 ? 1.6345 1.6345 1.6345 0.0000  0.0000  -0.0000 374 LEU A O   
2658 C CB  . LEU A 374 ? 1.6345 1.6345 1.6345 0.0000  0.0000  -0.0000 374 LEU A CB  
2659 C CG  . LEU A 374 ? 1.6345 1.6345 1.6345 0.0000  0.0000  -0.0000 374 LEU A CG  
2660 C CD1 . LEU A 374 ? 1.6345 1.6345 1.6345 0.0000  0.0000  -0.0000 374 LEU A CD1 
2661 C CD2 . LEU A 374 ? 1.6345 1.6345 1.6345 0.0000  0.0000  -0.0000 374 LEU A CD2 
2662 N N   . THR A 375 ? 1.6038 1.6038 1.6038 0.0000  -0.0000 0.0000  375 THR A N   
2663 C CA  . THR A 375 ? 1.6038 1.6038 1.6038 0.0000  -0.0000 0.0000  375 THR A CA  
2664 C C   . THR A 375 ? 1.6038 1.6038 1.6038 0.0000  -0.0000 0.0000  375 THR A C   
2665 O O   . THR A 375 ? 1.6038 1.6038 1.6038 0.0000  -0.0000 0.0000  375 THR A O   
2666 C CB  . THR A 375 ? 1.6038 1.6038 1.6038 0.0000  -0.0000 0.0000  375 THR A CB  
2667 O OG1 . THR A 375 ? 1.6038 1.6038 1.6038 0.0000  -0.0000 0.0000  375 THR A OG1 
2668 C CG2 . THR A 375 ? 1.6038 1.6038 1.6038 0.0000  -0.0000 0.0000  375 THR A CG2 
2669 N N   . ASP A 376 ? 1.5433 1.5433 1.5433 0.0000  0.0000  0.0000  376 ASP A N   
2670 C CA  . ASP A 376 ? 1.5433 1.5433 1.5433 0.0000  0.0000  0.0000  376 ASP A CA  
2671 C C   . ASP A 376 ? 1.5433 1.5433 1.5433 0.0000  0.0000  0.0000  376 ASP A C   
2672 O O   . ASP A 376 ? 1.5433 1.5433 1.5433 0.0000  0.0000  0.0000  376 ASP A O   
2673 C CB  . ASP A 376 ? 1.5433 1.5433 1.5433 0.0000  0.0000  0.0000  376 ASP A CB  
2674 C CG  . ASP A 376 ? 1.5433 1.5433 1.5433 0.0000  0.0000  0.0000  376 ASP A CG  
2675 O OD1 . ASP A 376 ? 1.5433 1.5433 1.5433 0.0000  0.0000  0.0000  376 ASP A OD1 
2676 O OD2 . ASP A 376 ? 1.5433 1.5433 1.5433 0.0000  0.0000  0.0000  376 ASP A OD2 
2677 N N   . PRO A 377 ? 1.6328 1.6328 1.6328 0.0000  0.0000  -0.0000 377 PRO A N   
2678 C CA  . PRO A 377 ? 1.6328 1.6328 1.6328 0.0000  0.0000  -0.0000 377 PRO A CA  
2679 C C   . PRO A 377 ? 1.6328 1.6328 1.6328 0.0000  0.0000  -0.0000 377 PRO A C   
2680 O O   . PRO A 377 ? 1.6328 1.6328 1.6328 0.0000  0.0000  -0.0000 377 PRO A O   
2681 C CB  . PRO A 377 ? 1.6328 1.6328 1.6328 0.0000  0.0000  -0.0000 377 PRO A CB  
2682 C CG  . PRO A 377 ? 1.6328 1.6328 1.6328 0.0000  0.0000  -0.0000 377 PRO A CG  
2683 C CD  . PRO A 377 ? 1.6328 1.6328 1.6328 0.0000  0.0000  -0.0000 377 PRO A CD  
2684 N N   . ASN A 378 ? 1.4753 1.4753 1.4753 -0.0000 -0.0000 -0.0000 378 ASN A N   
2685 C CA  . ASN A 378 ? 1.4753 1.4753 1.4753 -0.0000 -0.0000 -0.0000 378 ASN A CA  
2686 C C   . ASN A 378 ? 1.4753 1.4753 1.4753 -0.0000 -0.0000 -0.0000 378 ASN A C   
2687 O O   . ASN A 378 ? 1.4753 1.4753 1.4753 -0.0000 -0.0000 -0.0000 378 ASN A O   
2688 C CB  . ASN A 378 ? 1.4753 1.4753 1.4753 -0.0000 -0.0000 -0.0000 378 ASN A CB  
2689 C CG  . ASN A 378 ? 1.4753 1.4753 1.4753 -0.0000 -0.0000 -0.0000 378 ASN A CG  
2690 O OD1 . ASN A 378 ? 1.4753 1.4753 1.4753 -0.0000 -0.0000 -0.0000 378 ASN A OD1 
2691 N ND2 . ASN A 378 ? 1.4753 1.4753 1.4753 -0.0000 -0.0000 -0.0000 378 ASN A ND2 
2692 N N   . VAL A 379 ? 1.4865 1.4865 1.4865 0.0000  0.0000  -0.0000 379 VAL A N   
2693 C CA  . VAL A 379 ? 1.4865 1.4865 1.4865 0.0000  0.0000  -0.0000 379 VAL A CA  
2694 C C   . VAL A 379 ? 1.4865 1.4865 1.4865 0.0000  0.0000  -0.0000 379 VAL A C   
2695 O O   . VAL A 379 ? 1.4865 1.4865 1.4865 0.0000  0.0000  -0.0000 379 VAL A O   
2696 C CB  . VAL A 379 ? 1.4865 1.4865 1.4865 0.0000  0.0000  -0.0000 379 VAL A CB  
2697 C CG1 . VAL A 379 ? 1.4865 1.4865 1.4865 0.0000  0.0000  -0.0000 379 VAL A CG1 
2698 C CG2 . VAL A 379 ? 1.4865 1.4865 1.4865 0.0000  0.0000  -0.0000 379 VAL A CG2 
2699 N N   . ALA A 380 ? 1.4920 1.4920 1.4920 0.0000  0.0000  -0.0000 380 ALA A N   
2700 C CA  . ALA A 380 ? 1.4920 1.4920 1.4920 0.0000  0.0000  -0.0000 380 ALA A CA  
2701 C C   . ALA A 380 ? 1.4920 1.4920 1.4920 0.0000  0.0000  -0.0000 380 ALA A C   
2702 O O   . ALA A 380 ? 1.4920 1.4920 1.4920 0.0000  0.0000  -0.0000 380 ALA A O   
2704 N N   . ALA A 381 ? 1.3905 1.3905 1.3905 0.0000  0.0000  -0.0000 381 ALA A N   
2705 C CA  . ALA A 381 ? 1.3905 1.3905 1.3905 0.0000  0.0000  -0.0000 381 ALA A CA  
2706 C C   . ALA A 381 ? 1.3905 1.3905 1.3905 0.0000  0.0000  -0.0000 381 ALA A C   
2707 O O   . ALA A 381 ? 1.3905 1.3905 1.3905 0.0000  0.0000  -0.0000 381 ALA A O   
2708 C CB  . ALA A 381 ? 1.3905 1.3905 1.3905 0.0000  0.0000  -0.0000 381 ALA A CB  
2709 N N   . ALA A 382 ? 1.4476 1.4476 1.4476 0.0000  -0.0000 -0.0000 382 ALA A N   
2710 C CA  . ALA A 382 ? 1.4476 1.4476 1.4476 0.0000  -0.0000 -0.0000 382 ALA A CA  
2711 C C   . ALA A 382 ? 1.4476 1.4476 1.4476 0.0000  -0.0000 -0.0000 382 ALA A C   
2712 O O   . ALA A 382 ? 1.4476 1.4476 1.4476 0.0000  -0.0000 -0.0000 382 ALA A O   
2713 C CB  . ALA A 382 ? 1.4476 1.4476 1.4476 0.0000  -0.0000 -0.0000 382 ALA A CB  
2714 N N   . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A N   
2715 C CA  . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A CA  
2716 C C   . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A C   
2717 O O   . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A O   
2718 C CB  . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A CB  
2719 C CG  . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A CG  
2720 C CD1 . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A CD1 
2721 C CD2 . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A CD2 
2722 C CE1 . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A CE1 
2723 C CE2 . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A CE2 
2724 C CZ  . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A CZ  
2725 O OH  . TYR A 383 ? 1.4182 1.4182 1.4182 0.0000  0.0000  -0.0000 383 TYR A OH  
2726 N N   . ALA A 384 ? 1.4513 1.4513 1.4513 0.0000  0.0000  0.0000  384 ALA A N   
2727 C CA  . ALA A 384 ? 1.4513 1.4513 1.4513 0.0000  0.0000  0.0000  384 ALA A CA  
2728 C C   . ALA A 384 ? 1.4513 1.4513 1.4513 0.0000  0.0000  0.0000  384 ALA A C   
2729 O O   . ALA A 384 ? 1.4513 1.4513 1.4513 0.0000  0.0000  0.0000  384 ALA A O   
2730 C CB  . ALA A 384 ? 1.4513 1.4513 1.4513 0.0000  0.0000  0.0000  384 ALA A CB  
2731 N N   . MET A 385 ? 1.5198 1.5198 1.5198 0.0000  0.0000  -0.0000 385 MET A N   
2732 C CA  . MET A 385 ? 1.5198 1.5198 1.5198 0.0000  0.0000  -0.0000 385 MET A CA  
2733 C C   . MET A 385 ? 1.5198 1.5198 1.5198 0.0000  0.0000  -0.0000 385 MET A C   
2734 O O   . MET A 385 ? 1.5198 1.5198 1.5198 0.0000  0.0000  -0.0000 385 MET A O   
2735 C CB  . MET A 385 ? 1.5198 1.5198 1.5198 0.0000  0.0000  -0.0000 385 MET A CB  
2736 C CG  . MET A 385 ? 1.5198 1.5198 1.5198 0.0000  0.0000  -0.0000 385 MET A CG  
2737 S SD  . MET A 385 ? 1.5198 1.5198 1.5198 0.0000  0.0000  -0.0000 385 MET A SD  
2738 C CE  . MET A 385 ? 1.5198 1.5198 1.5198 0.0000  0.0000  -0.0000 385 MET A CE  
2739 N N   . ILE A 386 ? 1.3898 1.3898 1.3898 0.0000  -0.0000 0.0000  386 ILE A N   
2740 C CA  . ILE A 386 ? 1.3898 1.3898 1.3898 0.0000  -0.0000 0.0000  386 ILE A CA  
2741 C C   . ILE A 386 ? 1.3898 1.3898 1.3898 0.0000  -0.0000 0.0000  386 ILE A C   
2742 O O   . ILE A 386 ? 1.3898 1.3898 1.3898 0.0000  -0.0000 0.0000  386 ILE A O   
2743 C CB  . ILE A 386 ? 1.3898 1.3898 1.3898 0.0000  -0.0000 0.0000  386 ILE A CB  
2744 C CG1 . ILE A 386 ? 1.3898 1.3898 1.3898 0.0000  -0.0000 0.0000  386 ILE A CG1 
2745 C CG2 . ILE A 386 ? 1.3898 1.3898 1.3898 0.0000  -0.0000 0.0000  386 ILE A CG2 
2746 C CD1 . ILE A 386 ? 1.3898 1.3898 1.3898 0.0000  -0.0000 0.0000  386 ILE A CD1 
2747 N N   . LEU A 387 ? 1.3601 1.3601 1.3601 0.0000  0.0000  -0.0000 387 LEU A N   
2748 C CA  . LEU A 387 ? 1.3601 1.3601 1.3601 0.0000  0.0000  -0.0000 387 LEU A CA  
2749 C C   . LEU A 387 ? 1.3601 1.3601 1.3601 0.0000  0.0000  -0.0000 387 LEU A C   
2750 O O   . LEU A 387 ? 1.3601 1.3601 1.3601 0.0000  0.0000  -0.0000 387 LEU A O   
2751 C CB  . LEU A 387 ? 1.3601 1.3601 1.3601 0.0000  0.0000  -0.0000 387 LEU A CB  
2752 C CG  . LEU A 387 ? 1.3601 1.3601 1.3601 0.0000  0.0000  -0.0000 387 LEU A CG  
2753 C CD1 . LEU A 387 ? 1.3601 1.3601 1.3601 0.0000  0.0000  -0.0000 387 LEU A CD1 
2754 C CD2 . LEU A 387 ? 1.3601 1.3601 1.3601 0.0000  0.0000  -0.0000 387 LEU A CD2 
2755 N N   . GLY A 388 ? 1.2802 1.2802 1.2802 0.0000  0.0000  0.0000  388 GLY A N   
2756 C CA  . GLY A 388 ? 1.2802 1.2802 1.2802 0.0000  0.0000  0.0000  388 GLY A CA  
2757 C C   . GLY A 388 ? 1.2802 1.2802 1.2802 0.0000  0.0000  0.0000  388 GLY A C   
2758 O O   . GLY A 388 ? 1.2802 1.2802 1.2802 0.0000  0.0000  0.0000  388 GLY A O   
2759 N N   . ILE A 389 ? 1.3934 1.3934 1.3934 0.0000  0.0000  -0.0000 389 ILE A N   
2760 C CA  . ILE A 389 ? 1.3934 1.3934 1.3934 0.0000  0.0000  -0.0000 389 ILE A CA  
2761 C C   . ILE A 389 ? 1.3934 1.3934 1.3934 0.0000  0.0000  -0.0000 389 ILE A C   
2762 O O   . ILE A 389 ? 1.3934 1.3934 1.3934 0.0000  0.0000  -0.0000 389 ILE A O   
2763 C CB  . ILE A 389 ? 1.3934 1.3934 1.3934 0.0000  0.0000  -0.0000 389 ILE A CB  
2764 C CG1 . ILE A 389 ? 1.3934 1.3934 1.3934 0.0000  0.0000  -0.0000 389 ILE A CG1 
2765 C CG2 . ILE A 389 ? 1.3934 1.3934 1.3934 0.0000  0.0000  -0.0000 389 ILE A CG2 
2766 C CD1 . ILE A 389 ? 1.3934 1.3934 1.3934 0.0000  0.0000  -0.0000 389 ILE A CD1 
2767 N N   . ASP A 390 ? 1.4348 1.4348 1.4348 0.0000  0.0000  -0.0000 390 ASP A N   
2768 C CA  . ASP A 390 ? 1.4348 1.4348 1.4348 0.0000  0.0000  -0.0000 390 ASP A CA  
2769 C C   . ASP A 390 ? 1.4348 1.4348 1.4348 0.0000  0.0000  -0.0000 390 ASP A C   
2770 O O   . ASP A 390 ? 1.4348 1.4348 1.4348 0.0000  0.0000  -0.0000 390 ASP A O   
2771 C CB  . ASP A 390 ? 1.4348 1.4348 1.4348 0.0000  0.0000  -0.0000 390 ASP A CB  
2772 C CG  . ASP A 390 ? 1.4348 1.4348 1.4348 0.0000  0.0000  -0.0000 390 ASP A CG  
2773 O OD1 . ASP A 390 ? 1.4348 1.4348 1.4348 0.0000  0.0000  -0.0000 390 ASP A OD1 
2774 O OD2 . ASP A 390 ? 1.4348 1.4348 1.4348 0.0000  0.0000  -0.0000 390 ASP A OD2 
2775 N N   . ALA A 391 ? 1.3155 1.3155 1.3155 0.0000  0.0000  -0.0000 391 ALA A N   
2776 C CA  . ALA A 391 ? 1.3155 1.3155 1.3155 0.0000  0.0000  -0.0000 391 ALA A CA  
2777 C C   . ALA A 391 ? 1.3155 1.3155 1.3155 0.0000  0.0000  -0.0000 391 ALA A C   
2778 O O   . ALA A 391 ? 1.3155 1.3155 1.3155 0.0000  0.0000  -0.0000 391 ALA A O   
2779 C CB  . ALA A 391 ? 1.3155 1.3155 1.3155 0.0000  0.0000  -0.0000 391 ALA A CB  
2780 N N   . ILE A 392 ? 1.3206 1.3206 1.3206 0.0000  -0.0000 -0.0000 392 ILE A N   
2781 C CA  . ILE A 392 ? 1.3206 1.3206 1.3206 0.0000  -0.0000 -0.0000 392 ILE A CA  
2782 C C   . ILE A 392 ? 1.3206 1.3206 1.3206 0.0000  -0.0000 -0.0000 392 ILE A C   
2783 O O   . ILE A 392 ? 1.3206 1.3206 1.3206 0.0000  -0.0000 -0.0000 392 ILE A O   
2784 C CB  . ILE A 392 ? 1.3206 1.3206 1.3206 0.0000  -0.0000 -0.0000 392 ILE A CB  
2785 C CG1 . ILE A 392 ? 1.3206 1.3206 1.3206 0.0000  -0.0000 -0.0000 392 ILE A CG1 
2786 C CG2 . ILE A 392 ? 1.3206 1.3206 1.3206 0.0000  -0.0000 -0.0000 392 ILE A CG2 
2787 C CD1 . ILE A 392 ? 1.3206 1.3206 1.3206 0.0000  -0.0000 -0.0000 392 ILE A CD1 
2788 N N   . LEU A 393 ? 1.3245 1.3245 1.3245 0.0000  0.0000  -0.0000 393 LEU A N   
2789 C CA  . LEU A 393 ? 1.3245 1.3245 1.3245 0.0000  0.0000  -0.0000 393 LEU A CA  
2790 C C   . LEU A 393 ? 1.3245 1.3245 1.3245 0.0000  0.0000  -0.0000 393 LEU A C   
2791 O O   . LEU A 393 ? 1.3245 1.3245 1.3245 0.0000  0.0000  -0.0000 393 LEU A O   
2792 C CB  . LEU A 393 ? 1.3245 1.3245 1.3245 0.0000  0.0000  -0.0000 393 LEU A CB  
2793 C CG  . LEU A 393 ? 1.3245 1.3245 1.3245 0.0000  0.0000  -0.0000 393 LEU A CG  
2794 C CD1 . LEU A 393 ? 1.3245 1.3245 1.3245 0.0000  0.0000  -0.0000 393 LEU A CD1 
2795 C CD2 . LEU A 393 ? 1.3245 1.3245 1.3245 0.0000  0.0000  -0.0000 393 LEU A CD2 
2796 N N   . ASP A 394 ? 1.4417 1.4417 1.4417 0.0000  0.0000  -0.0000 394 ASP A N   
2797 C CA  . ASP A 394 ? 1.4417 1.4417 1.4417 0.0000  0.0000  -0.0000 394 ASP A CA  
2798 C C   . ASP A 394 ? 1.4417 1.4417 1.4417 0.0000  0.0000  -0.0000 394 ASP A C   
2799 O O   . ASP A 394 ? 1.4417 1.4417 1.4417 0.0000  0.0000  -0.0000 394 ASP A O   
2800 C CB  . ASP A 394 ? 1.4417 1.4417 1.4417 0.0000  0.0000  -0.0000 394 ASP A CB  
2801 C CG  . ASP A 394 ? 1.4417 1.4417 1.4417 0.0000  0.0000  -0.0000 394 ASP A CG  
2802 O OD1 . ASP A 394 ? 1.4417 1.4417 1.4417 0.0000  0.0000  -0.0000 394 ASP A OD1 
2803 O OD2 . ASP A 394 ? 1.4417 1.4417 1.4417 0.0000  0.0000  -0.0000 394 ASP A OD2 
2804 N N   . MET A 395 ? 1.3049 1.3049 1.3049 0.0000  0.0000  -0.0000 395 MET A N   
2805 C CA  . MET A 395 ? 1.3049 1.3049 1.3049 0.0000  0.0000  -0.0000 395 MET A CA  
2806 C C   . MET A 395 ? 1.3049 1.3049 1.3049 0.0000  0.0000  -0.0000 395 MET A C   
2807 O O   . MET A 395 ? 1.3049 1.3049 1.3049 0.0000  0.0000  -0.0000 395 MET A O   
2808 C CB  . MET A 395 ? 1.3049 1.3049 1.3049 0.0000  0.0000  -0.0000 395 MET A CB  
2809 C CG  . MET A 395 ? 1.3049 1.3049 1.3049 0.0000  0.0000  -0.0000 395 MET A CG  
2810 S SD  . MET A 395 ? 1.3049 1.3049 1.3049 0.0000  0.0000  -0.0000 395 MET A SD  
2811 C CE  . MET A 395 ? 1.3049 1.3049 1.3049 0.0000  0.0000  -0.0000 395 MET A CE  
2812 N N   . GLY A 396 ? 1.4628 1.4628 1.4628 0.0000  -0.0000 -0.0000 396 GLY A N   
2813 C CA  . GLY A 396 ? 1.4628 1.4628 1.4628 0.0000  -0.0000 -0.0000 396 GLY A CA  
2814 C C   . GLY A 396 ? 1.4628 1.4628 1.4628 0.0000  -0.0000 -0.0000 396 GLY A C   
2815 O O   . GLY A 396 ? 1.4628 1.4628 1.4628 0.0000  -0.0000 -0.0000 396 GLY A O   
2816 N N   . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A N   
2817 C CA  . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A CA  
2818 C C   . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A C   
2819 O O   . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A O   
2820 C CB  . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A CB  
2821 C CG  . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A CG  
2822 C CD  . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A CD  
2823 N NE  . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A NE  
2824 C CZ  . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A CZ  
2825 N NH1 . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A NH1 
2826 N NH2 . ARG A 397 ? 1.3901 1.3901 1.3901 0.0000  0.0000  -0.0000 397 ARG A NH2 
2827 N N   . THR A 398 ? 1.3139 1.3139 1.3139 0.0000  0.0000  -0.0000 398 THR A N   
2828 C CA  . THR A 398 ? 1.3139 1.3139 1.3139 0.0000  0.0000  -0.0000 398 THR A CA  
2829 C C   . THR A 398 ? 1.3139 1.3139 1.3139 0.0000  0.0000  -0.0000 398 THR A C   
2830 O O   . THR A 398 ? 1.3139 1.3139 1.3139 0.0000  0.0000  -0.0000 398 THR A O   
2831 C CB  . THR A 398 ? 1.3139 1.3139 1.3139 0.0000  0.0000  -0.0000 398 THR A CB  
2832 O OG1 . THR A 398 ? 1.3139 1.3139 1.3139 0.0000  0.0000  -0.0000 398 THR A OG1 
2833 C CG2 . THR A 398 ? 1.3139 1.3139 1.3139 0.0000  0.0000  -0.0000 398 THR A CG2 
2834 N N   . MET A 399 ? 1.4395 1.4395 1.4395 0.0000  0.0000  -0.0000 399 MET A N   
2835 C CA  . MET A 399 ? 1.4395 1.4395 1.4395 0.0000  0.0000  -0.0000 399 MET A CA  
2836 C C   . MET A 399 ? 1.4395 1.4395 1.4395 0.0000  0.0000  -0.0000 399 MET A C   
2837 O O   . MET A 399 ? 1.4395 1.4395 1.4395 0.0000  0.0000  -0.0000 399 MET A O   
2838 C CB  . MET A 399 ? 1.4395 1.4395 1.4395 0.0000  0.0000  -0.0000 399 MET A CB  
2839 C CG  . MET A 399 ? 1.4395 1.4395 1.4395 0.0000  0.0000  -0.0000 399 MET A CG  
2840 S SD  . MET A 399 ? 1.4395 1.4395 1.4395 0.0000  0.0000  -0.0000 399 MET A SD  
2841 C CE  . MET A 399 ? 1.4395 1.4395 1.4395 0.0000  0.0000  -0.0000 399 MET A CE  
# 
