data_9FJ1
# 
_entry.id   9FJ1 
# 
_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   9FJ1         pdb_00009fj1 10.2210/pdb9fj1/pdb 
WWPDB D_1292139025 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-03-19 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FJ1 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              guardado@pasteur.fr 
_pdbx_contact_author.name_first         Pablo 
_pdbx_contact_author.name_last          Guardado-Calvo 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7292-5270 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vernuccio, R.'      1 0009-0009-8319-0922 
'Guardado-Calvo, P.' 2 0000-0001-7292-5270 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Microbiol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2058-5276 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                734 
_citation.page_last                 748 
_citation.title                     'Structural insights into tecovirimat antiviral activity and poxvirus resistance.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41564-025-01936-6 
_citation.pdbx_database_id_PubMed   39939832 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vernuccio, R.'         1  0009-0009-8319-0922 
primary 'Martinez Leon, A.'     2  0009-0005-6162-7303 
primary 'Poojari, C.S.'         3  0000-0001-6575-221X 
primary 'Buchrieser, J.'        4  0000-0003-4790-7577 
primary 'Selverian, C.N.'       5  0000-0002-1047-4336 
primary 'Jaleta, Y.'            6  ?                   
primary 'Meola, A.'             7  ?                   
primary 'Guivel-Benhassine, F.' 8  ?                   
primary 'Porrot, F.'            9  0000-0001-8995-3614 
primary 'Haouz, A.'             10 0000-0003-1196-1635 
primary 'Chevreuil, M.'         11 ?                   
primary 'Raynal, B.'            12 0000-0001-5634-0408 
primary 'Mercer, J.'            13 ?                   
primary 'Simon-Loriere, E.'     14 0000-0001-8420-7743 
primary 'Chandran, K.'          15 0000-0003-0232-7077 
primary 'Schwartz, O.'          16 0000-0002-0729-1475 
primary 'Hub, J.S.'             17 0000-0001-7716-1767 
primary 'Guardado-Calvo, P.'    18 0000-0001-7292-5270 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Envelope phospholipase OPG057'                                        44363.062 1 3.1.1.-,3.1.4.4 ? ? ? 
2 non-polymer syn 'CITRIC ACID'                                                          192.124   1 ?               ? ? ? 
3 non-polymer syn GLYCEROL                                                               92.094    2 ?               ? ? ? 
4 non-polymer syn "~{N}'-(4-chloranyl-3-methyl-phenyl)carbonylpyridine-4-carbohydrazide" 289.717   1 ?               ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '37 kDa protein,Envelope phospholipase F13,Palmitoylated EV membrane protein,p37K' 
# 
_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       
;HHHHHHHHGSGAGWSHPQFEKGGSGLVPRGSGSVPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFC
CNPLSTTRGALIFDKLKEASEKGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGN
ASFTGGSIHTIKTLGVYSDYPPLATDLRRRFDTFKAFNSAKNSAANLASAAAALPVSTAYHIKNPIGGVFFTDSPEHLLG
YSRDLDTDVVIDKLKSAKTSIDIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATARSL
DALCVQNDLSVKVFTIQNNTKLLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHHHHHHHGSGAGWSHPQFEKGGSGLVPRGSGSVPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFC
CNPLSTTRGALIFDKLKEASEKGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGN
ASFTGGSIHTIKTLGVYSDYPPLATDLRRRFDTFKAFNSAKNSAANLASAAAALPVSTAYHIKNPIGGVFFTDSPEHLLG
YSRDLDTDVVIDKLKSAKTSIDIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATARSL
DALCVQNDLSVKVFTIQNNTKLLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CITRIC ACID'                                                          CIT   
3 GLYCEROL                                                               GOL   
4 "~{N}'-(4-chloranyl-3-methyl-phenyl)carbonylpyridine-4-carbohydrazide" A1IDM 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   GLY n 
1 10  SER n 
1 11  GLY n 
1 12  ALA n 
1 13  GLY n 
1 14  TRP n 
1 15  SER n 
1 16  HIS n 
1 17  PRO n 
1 18  GLN n 
1 19  PHE n 
1 20  GLU n 
1 21  LYS n 
1 22  GLY n 
1 23  GLY n 
1 24  SER n 
1 25  GLY n 
1 26  LEU n 
1 27  VAL n 
1 28  PRO n 
1 29  ARG n 
1 30  GLY n 
1 31  SER n 
1 32  GLY n 
1 33  SER n 
1 34  VAL n 
1 35  PRO n 
1 36  ALA n 
1 37  GLY n 
1 38  ALA n 
1 39  LYS n 
1 40  CYS n 
1 41  ARG n 
1 42  LEU n 
1 43  VAL n 
1 44  GLU n 
1 45  THR n 
1 46  LEU n 
1 47  PRO n 
1 48  GLU n 
1 49  ASN n 
1 50  MET n 
1 51  ASP n 
1 52  PHE n 
1 53  ARG n 
1 54  SER n 
1 55  ASP n 
1 56  HIS n 
1 57  LEU n 
1 58  THR n 
1 59  THR n 
1 60  PHE n 
1 61  GLU n 
1 62  CYS n 
1 63  PHE n 
1 64  ASN n 
1 65  GLU n 
1 66  ILE n 
1 67  ILE n 
1 68  THR n 
1 69  LEU n 
1 70  ALA n 
1 71  LYS n 
1 72  LYS n 
1 73  TYR n 
1 74  ILE n 
1 75  TYR n 
1 76  ILE n 
1 77  ALA n 
1 78  SER n 
1 79  PHE n 
1 80  CYS n 
1 81  CYS n 
1 82  ASN n 
1 83  PRO n 
1 84  LEU n 
1 85  SER n 
1 86  THR n 
1 87  THR n 
1 88  ARG n 
1 89  GLY n 
1 90  ALA n 
1 91  LEU n 
1 92  ILE n 
1 93  PHE n 
1 94  ASP n 
1 95  LYS n 
1 96  LEU n 
1 97  LYS n 
1 98  GLU n 
1 99  ALA n 
1 100 SER n 
1 101 GLU n 
1 102 LYS n 
1 103 GLY n 
1 104 ILE n 
1 105 LYS n 
1 106 ILE n 
1 107 ILE n 
1 108 VAL n 
1 109 LEU n 
1 110 LEU n 
1 111 ASP n 
1 112 GLU n 
1 113 ARG n 
1 114 GLY n 
1 115 LYS n 
1 116 ARG n 
1 117 ASN n 
1 118 LEU n 
1 119 GLY n 
1 120 GLU n 
1 121 LEU n 
1 122 GLN n 
1 123 SER n 
1 124 HIS n 
1 125 CYS n 
1 126 PRO n 
1 127 ASP n 
1 128 ILE n 
1 129 ASN n 
1 130 PHE n 
1 131 ILE n 
1 132 THR n 
1 133 VAL n 
1 134 ASN n 
1 135 ILE n 
1 136 ASP n 
1 137 LYS n 
1 138 LYS n 
1 139 ASN n 
1 140 ASN n 
1 141 VAL n 
1 142 GLY n 
1 143 LEU n 
1 144 LEU n 
1 145 LEU n 
1 146 GLY n 
1 147 CYS n 
1 148 PHE n 
1 149 TRP n 
1 150 VAL n 
1 151 SER n 
1 152 ASP n 
1 153 ASP n 
1 154 GLU n 
1 155 ARG n 
1 156 CYS n 
1 157 TYR n 
1 158 VAL n 
1 159 GLY n 
1 160 ASN n 
1 161 ALA n 
1 162 SER n 
1 163 PHE n 
1 164 THR n 
1 165 GLY n 
1 166 GLY n 
1 167 SER n 
1 168 ILE n 
1 169 HIS n 
1 170 THR n 
1 171 ILE n 
1 172 LYS n 
1 173 THR n 
1 174 LEU n 
1 175 GLY n 
1 176 VAL n 
1 177 TYR n 
1 178 SER n 
1 179 ASP n 
1 180 TYR n 
1 181 PRO n 
1 182 PRO n 
1 183 LEU n 
1 184 ALA n 
1 185 THR n 
1 186 ASP n 
1 187 LEU n 
1 188 ARG n 
1 189 ARG n 
1 190 ARG n 
1 191 PHE n 
1 192 ASP n 
1 193 THR n 
1 194 PHE n 
1 195 LYS n 
1 196 ALA n 
1 197 PHE n 
1 198 ASN n 
1 199 SER n 
1 200 ALA n 
1 201 LYS n 
1 202 ASN n 
1 203 SER n 
1 204 ALA n 
1 205 ALA n 
1 206 ASN n 
1 207 LEU n 
1 208 ALA n 
1 209 SER n 
1 210 ALA n 
1 211 ALA n 
1 212 ALA n 
1 213 ALA n 
1 214 LEU n 
1 215 PRO n 
1 216 VAL n 
1 217 SER n 
1 218 THR n 
1 219 ALA n 
1 220 TYR n 
1 221 HIS n 
1 222 ILE n 
1 223 LYS n 
1 224 ASN n 
1 225 PRO n 
1 226 ILE n 
1 227 GLY n 
1 228 GLY n 
1 229 VAL n 
1 230 PHE n 
1 231 PHE n 
1 232 THR n 
1 233 ASP n 
1 234 SER n 
1 235 PRO n 
1 236 GLU n 
1 237 HIS n 
1 238 LEU n 
1 239 LEU n 
1 240 GLY n 
1 241 TYR n 
1 242 SER n 
1 243 ARG n 
1 244 ASP n 
1 245 LEU n 
1 246 ASP n 
1 247 THR n 
1 248 ASP n 
1 249 VAL n 
1 250 VAL n 
1 251 ILE n 
1 252 ASP n 
1 253 LYS n 
1 254 LEU n 
1 255 LYS n 
1 256 SER n 
1 257 ALA n 
1 258 LYS n 
1 259 THR n 
1 260 SER n 
1 261 ILE n 
1 262 ASP n 
1 263 ILE n 
1 264 GLU n 
1 265 HIS n 
1 266 LEU n 
1 267 ALA n 
1 268 ILE n 
1 269 VAL n 
1 270 PRO n 
1 271 THR n 
1 272 THR n 
1 273 ARG n 
1 274 VAL n 
1 275 ASP n 
1 276 GLY n 
1 277 ASN n 
1 278 SER n 
1 279 TYR n 
1 280 TYR n 
1 281 TRP n 
1 282 PRO n 
1 283 ASP n 
1 284 ILE n 
1 285 TYR n 
1 286 ASN n 
1 287 SER n 
1 288 ILE n 
1 289 ILE n 
1 290 GLU n 
1 291 ALA n 
1 292 ALA n 
1 293 ILE n 
1 294 ASN n 
1 295 ARG n 
1 296 GLY n 
1 297 VAL n 
1 298 LYS n 
1 299 ILE n 
1 300 ARG n 
1 301 LEU n 
1 302 LEU n 
1 303 VAL n 
1 304 GLY n 
1 305 ASN n 
1 306 TRP n 
1 307 ASP n 
1 308 LYS n 
1 309 ASN n 
1 310 ASP n 
1 311 VAL n 
1 312 TYR n 
1 313 SER n 
1 314 MET n 
1 315 ALA n 
1 316 THR n 
1 317 ALA n 
1 318 ARG n 
1 319 SER n 
1 320 LEU n 
1 321 ASP n 
1 322 ALA n 
1 323 LEU n 
1 324 CYS n 
1 325 VAL n 
1 326 GLN n 
1 327 ASN n 
1 328 ASP n 
1 329 LEU n 
1 330 SER n 
1 331 VAL n 
1 332 LYS n 
1 333 VAL n 
1 334 PHE n 
1 335 THR n 
1 336 ILE n 
1 337 GLN n 
1 338 ASN n 
1 339 ASN n 
1 340 THR n 
1 341 LYS n 
1 342 LEU n 
1 343 LEU n 
1 344 ILE n 
1 345 VAL n 
1 346 ASP n 
1 347 ASP n 
1 348 GLU n 
1 349 TYR n 
1 350 VAL n 
1 351 HIS n 
1 352 ILE n 
1 353 THR n 
1 354 SER n 
1 355 ALA n 
1 356 ASN n 
1 357 PHE n 
1 358 ASP n 
1 359 GLY n 
1 360 THR n 
1 361 HIS n 
1 362 TYR n 
1 363 GLN n 
1 364 ASN n 
1 365 HIS n 
1 366 GLY n 
1 367 PHE n 
1 368 VAL n 
1 369 SER n 
1 370 PHE n 
1 371 ASN n 
1 372 SER n 
1 373 ILE n 
1 374 ASP n 
1 375 LYS n 
1 376 GLN n 
1 377 LEU n 
1 378 VAL n 
1 379 SER n 
1 380 GLU n 
1 381 ALA n 
1 382 LYS n 
1 383 LYS n 
1 384 ILE n 
1 385 PHE n 
1 386 GLU n 
1 387 ARG n 
1 388 ASP n 
1 389 TRP n 
1 390 VAL n 
1 391 SER n 
1 392 SER n 
1 393 HIS n 
1 394 SER n 
1 395 LYS n 
1 396 SER n 
1 397 LEU n 
1 398 LYS n 
1 399 ILE 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                   399 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'OPG057, VACWR052, F13L' 
_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      'Vaccinia virus Western Reserve' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     696871 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_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 
A1IDM non-polymer         . "~{N}'-(4-chloranyl-3-methyl-phenyl)carbonylpyridine-4-carbohydrazide" ?                               
'C14 H12 Cl N3 O2' 289.717 
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 
CIT   non-polymer         . 'CITRIC ACID'                                                          ?                               
'C6 H8 O7'         192.124 
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  
GOL   non-polymer         . GLYCEROL                                                               'GLYCERIN; PROPANE-1,2,3-TRIOL' 
'C3 H8 O3'         92.094  
HIS   'L-peptide linking' y HISTIDINE                                                              ?                               
'C6 H10 N3 O2 1'   156.162 
ILE   'L-peptide linking' y ISOLEUCINE                                                             ?                               
'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ?                               
'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ?                               
'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                             ?                               
'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ?                               
'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                                                ?                               
'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                                                 ?                               
'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                                              ?                               
'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                             ?                               
'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                               ?                               
'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                                                 ?                               
'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   HIS 1   -26 ?   ?   ?   A . n 
A 1 2   HIS 2   -25 ?   ?   ?   A . n 
A 1 3   HIS 3   -24 ?   ?   ?   A . n 
A 1 4   HIS 4   -23 ?   ?   ?   A . n 
A 1 5   HIS 5   -22 ?   ?   ?   A . n 
A 1 6   HIS 6   -21 ?   ?   ?   A . n 
A 1 7   HIS 7   -20 ?   ?   ?   A . n 
A 1 8   HIS 8   -19 ?   ?   ?   A . n 
A 1 9   GLY 9   -18 ?   ?   ?   A . n 
A 1 10  SER 10  -17 ?   ?   ?   A . n 
A 1 11  GLY 11  -16 ?   ?   ?   A . n 
A 1 12  ALA 12  -15 ?   ?   ?   A . n 
A 1 13  GLY 13  -14 ?   ?   ?   A . n 
A 1 14  TRP 14  -13 ?   ?   ?   A . n 
A 1 15  SER 15  -12 ?   ?   ?   A . n 
A 1 16  HIS 16  -11 ?   ?   ?   A . n 
A 1 17  PRO 17  -10 ?   ?   ?   A . n 
A 1 18  GLN 18  -9  ?   ?   ?   A . n 
A 1 19  PHE 19  -8  ?   ?   ?   A . n 
A 1 20  GLU 20  -7  ?   ?   ?   A . n 
A 1 21  LYS 21  -6  ?   ?   ?   A . n 
A 1 22  GLY 22  -5  ?   ?   ?   A . n 
A 1 23  GLY 23  -4  ?   ?   ?   A . n 
A 1 24  SER 24  -3  ?   ?   ?   A . n 
A 1 25  GLY 25  -2  ?   ?   ?   A . n 
A 1 26  LEU 26  -1  ?   ?   ?   A . n 
A 1 27  VAL 27  0   ?   ?   ?   A . n 
A 1 28  PRO 28  1   ?   ?   ?   A . n 
A 1 29  ARG 29  2   ?   ?   ?   A . n 
A 1 30  GLY 30  3   ?   ?   ?   A . n 
A 1 31  SER 31  4   ?   ?   ?   A . n 
A 1 32  GLY 32  5   ?   ?   ?   A . n 
A 1 33  SER 33  6   6   SER SER A . n 
A 1 34  VAL 34  7   7   VAL VAL A . n 
A 1 35  PRO 35  8   8   PRO PRO A . n 
A 1 36  ALA 36  9   9   ALA ALA A . n 
A 1 37  GLY 37  10  10  GLY GLY A . n 
A 1 38  ALA 38  11  11  ALA ALA A . n 
A 1 39  LYS 39  12  12  LYS LYS A . n 
A 1 40  CYS 40  13  13  CYS CYS A . n 
A 1 41  ARG 41  14  14  ARG ARG A . n 
A 1 42  LEU 42  15  15  LEU LEU A . n 
A 1 43  VAL 43  16  16  VAL VAL A . n 
A 1 44  GLU 44  17  17  GLU GLU A . n 
A 1 45  THR 45  18  18  THR THR A . n 
A 1 46  LEU 46  19  19  LEU LEU A . n 
A 1 47  PRO 47  20  20  PRO PRO A . n 
A 1 48  GLU 48  21  21  GLU GLU A . n 
A 1 49  ASN 49  22  22  ASN ASN A . n 
A 1 50  MET 50  23  23  MET MET A . n 
A 1 51  ASP 51  24  24  ASP ASP A . n 
A 1 52  PHE 52  25  25  PHE PHE A . n 
A 1 53  ARG 53  26  26  ARG ARG A . n 
A 1 54  SER 54  27  27  SER SER A . n 
A 1 55  ASP 55  28  28  ASP ASP A . n 
A 1 56  HIS 56  29  29  HIS HIS A . n 
A 1 57  LEU 57  30  30  LEU LEU A . n 
A 1 58  THR 58  31  31  THR THR A . n 
A 1 59  THR 59  32  32  THR THR A . n 
A 1 60  PHE 60  33  33  PHE PHE A . n 
A 1 61  GLU 61  34  34  GLU GLU A . n 
A 1 62  CYS 62  35  35  CYS CYS A . n 
A 1 63  PHE 63  36  36  PHE PHE A . n 
A 1 64  ASN 64  37  37  ASN ASN A . n 
A 1 65  GLU 65  38  38  GLU GLU A . n 
A 1 66  ILE 66  39  39  ILE ILE A . n 
A 1 67  ILE 67  40  40  ILE ILE A . n 
A 1 68  THR 68  41  41  THR THR A . n 
A 1 69  LEU 69  42  42  LEU LEU A . n 
A 1 70  ALA 70  43  43  ALA ALA A . n 
A 1 71  LYS 71  44  44  LYS LYS A . n 
A 1 72  LYS 72  45  45  LYS LYS A . n 
A 1 73  TYR 73  46  46  TYR TYR A . n 
A 1 74  ILE 74  47  47  ILE ILE A . n 
A 1 75  TYR 75  48  48  TYR TYR A . n 
A 1 76  ILE 76  49  49  ILE ILE A . n 
A 1 77  ALA 77  50  50  ALA ALA A . n 
A 1 78  SER 78  51  51  SER SER A . n 
A 1 79  PHE 79  52  52  PHE PHE A . n 
A 1 80  CYS 80  53  53  CYS CYS A . n 
A 1 81  CYS 81  54  54  CYS CYS A . n 
A 1 82  ASN 82  55  55  ASN ASN A . n 
A 1 83  PRO 83  56  56  PRO PRO A . n 
A 1 84  LEU 84  57  57  LEU LEU A . n 
A 1 85  SER 85  58  58  SER SER A . n 
A 1 86  THR 86  59  59  THR THR A . n 
A 1 87  THR 87  60  60  THR THR A . n 
A 1 88  ARG 88  61  61  ARG ARG A . n 
A 1 89  GLY 89  62  62  GLY GLY A . n 
A 1 90  ALA 90  63  63  ALA ALA A . n 
A 1 91  LEU 91  64  64  LEU LEU A . n 
A 1 92  ILE 92  65  65  ILE ILE A . n 
A 1 93  PHE 93  66  66  PHE PHE A . n 
A 1 94  ASP 94  67  67  ASP ASP A . n 
A 1 95  LYS 95  68  68  LYS LYS A . n 
A 1 96  LEU 96  69  69  LEU LEU A . n 
A 1 97  LYS 97  70  70  LYS LYS A . n 
A 1 98  GLU 98  71  71  GLU GLU A . n 
A 1 99  ALA 99  72  72  ALA ALA A . n 
A 1 100 SER 100 73  73  SER SER A . n 
A 1 101 GLU 101 74  74  GLU GLU A . n 
A 1 102 LYS 102 75  75  LYS LYS A . n 
A 1 103 GLY 103 76  76  GLY GLY A . n 
A 1 104 ILE 104 77  77  ILE ILE A . n 
A 1 105 LYS 105 78  78  LYS LYS A . n 
A 1 106 ILE 106 79  79  ILE ILE A . n 
A 1 107 ILE 107 80  80  ILE ILE A . n 
A 1 108 VAL 108 81  81  VAL VAL A . n 
A 1 109 LEU 109 82  82  LEU LEU A . n 
A 1 110 LEU 110 83  83  LEU LEU A . n 
A 1 111 ASP 111 84  84  ASP ASP A . n 
A 1 112 GLU 112 85  85  GLU GLU A . n 
A 1 113 ARG 113 86  86  ARG ARG A . n 
A 1 114 GLY 114 87  87  GLY GLY A . n 
A 1 115 LYS 115 88  88  LYS LYS A . n 
A 1 116 ARG 116 89  89  ARG ARG A . n 
A 1 117 ASN 117 90  90  ASN ASN A . n 
A 1 118 LEU 118 91  91  LEU LEU A . n 
A 1 119 GLY 119 92  92  GLY GLY A . n 
A 1 120 GLU 120 93  93  GLU GLU A . n 
A 1 121 LEU 121 94  94  LEU LEU A . n 
A 1 122 GLN 122 95  95  GLN GLN A . n 
A 1 123 SER 123 96  96  SER SER A . n 
A 1 124 HIS 124 97  97  HIS HIS A . n 
A 1 125 CYS 125 98  98  CYS CYS A . n 
A 1 126 PRO 126 99  99  PRO PRO A . n 
A 1 127 ASP 127 100 100 ASP ASP A . n 
A 1 128 ILE 128 101 101 ILE ILE A . n 
A 1 129 ASN 129 102 102 ASN ASN A . n 
A 1 130 PHE 130 103 103 PHE PHE A . n 
A 1 131 ILE 131 104 104 ILE ILE A . n 
A 1 132 THR 132 105 105 THR THR A . n 
A 1 133 VAL 133 106 106 VAL VAL A . n 
A 1 134 ASN 134 107 107 ASN ASN A . n 
A 1 135 ILE 135 108 108 ILE ILE A . n 
A 1 136 ASP 136 109 109 ASP ASP A . n 
A 1 137 LYS 137 110 110 LYS LYS A . n 
A 1 138 LYS 138 111 111 LYS LYS A . n 
A 1 139 ASN 139 112 112 ASN ASN A . n 
A 1 140 ASN 140 113 113 ASN ASN A . n 
A 1 141 VAL 141 114 114 VAL VAL A . n 
A 1 142 GLY 142 115 115 GLY GLY A . n 
A 1 143 LEU 143 116 116 LEU LEU A . n 
A 1 144 LEU 144 117 117 LEU LEU A . n 
A 1 145 LEU 145 118 118 LEU LEU A . n 
A 1 146 GLY 146 119 119 GLY GLY A . n 
A 1 147 CYS 147 120 120 CYS CYS A . n 
A 1 148 PHE 148 121 121 PHE PHE A . n 
A 1 149 TRP 149 122 122 TRP TRP A . n 
A 1 150 VAL 150 123 123 VAL VAL A . n 
A 1 151 SER 151 124 124 SER SER A . n 
A 1 152 ASP 152 125 125 ASP ASP A . n 
A 1 153 ASP 153 126 126 ASP ASP A . n 
A 1 154 GLU 154 127 127 GLU GLU A . n 
A 1 155 ARG 155 128 128 ARG ARG A . n 
A 1 156 CYS 156 129 129 CYS CYS A . n 
A 1 157 TYR 157 130 130 TYR TYR A . n 
A 1 158 VAL 158 131 131 VAL VAL A . n 
A 1 159 GLY 159 132 132 GLY GLY A . n 
A 1 160 ASN 160 133 133 ASN ASN A . n 
A 1 161 ALA 161 134 134 ALA ALA A . n 
A 1 162 SER 162 135 135 SER SER A . n 
A 1 163 PHE 163 136 136 PHE PHE A . n 
A 1 164 THR 164 137 137 THR THR A . n 
A 1 165 GLY 165 138 138 GLY GLY A . n 
A 1 166 GLY 166 139 139 GLY GLY A . n 
A 1 167 SER 167 140 140 SER SER A . n 
A 1 168 ILE 168 141 141 ILE ILE A . n 
A 1 169 HIS 169 142 142 HIS HIS A . n 
A 1 170 THR 170 143 143 THR THR A . n 
A 1 171 ILE 171 144 144 ILE ILE A . n 
A 1 172 LYS 172 145 145 LYS LYS A . n 
A 1 173 THR 173 146 146 THR THR A . n 
A 1 174 LEU 174 147 147 LEU LEU A . n 
A 1 175 GLY 175 148 148 GLY GLY A . n 
A 1 176 VAL 176 149 149 VAL VAL A . n 
A 1 177 TYR 177 150 150 TYR TYR A . n 
A 1 178 SER 178 151 151 SER SER A . n 
A 1 179 ASP 179 152 152 ASP ASP A . n 
A 1 180 TYR 180 153 153 TYR TYR A . n 
A 1 181 PRO 181 154 154 PRO PRO A . n 
A 1 182 PRO 182 155 155 PRO PRO A . n 
A 1 183 LEU 183 156 156 LEU LEU A . n 
A 1 184 ALA 184 157 157 ALA ALA A . n 
A 1 185 THR 185 158 158 THR THR A . n 
A 1 186 ASP 186 159 159 ASP ASP A . n 
A 1 187 LEU 187 160 160 LEU LEU A . n 
A 1 188 ARG 188 161 161 ARG ARG A . n 
A 1 189 ARG 189 162 162 ARG ARG A . n 
A 1 190 ARG 190 163 163 ARG ARG A . n 
A 1 191 PHE 191 164 164 PHE PHE A . n 
A 1 192 ASP 192 165 165 ASP ASP A . n 
A 1 193 THR 193 166 166 THR THR A . n 
A 1 194 PHE 194 167 167 PHE PHE A . n 
A 1 195 LYS 195 168 168 LYS LYS A . n 
A 1 196 ALA 196 169 169 ALA ALA A . n 
A 1 197 PHE 197 170 170 PHE PHE A . n 
A 1 198 ASN 198 171 171 ASN ASN A . n 
A 1 199 SER 199 172 172 SER SER A . n 
A 1 200 ALA 200 173 173 ALA ALA A . n 
A 1 201 LYS 201 174 174 LYS LYS A . n 
A 1 202 ASN 202 175 175 ASN ASN A . n 
A 1 203 SER 203 176 176 SER SER A . n 
A 1 204 ALA 204 177 177 ALA ALA A . n 
A 1 205 ALA 205 178 178 ALA ALA A . n 
A 1 206 ASN 206 179 179 ASN ASN A . n 
A 1 207 LEU 207 180 180 LEU LEU A . n 
A 1 208 ALA 208 181 181 ALA ALA A . n 
A 1 209 SER 209 182 182 SER SER A . n 
A 1 210 ALA 210 183 183 ALA ALA A . n 
A 1 211 ALA 211 184 184 ALA ALA A . n 
A 1 212 ALA 212 185 185 ALA ALA A . n 
A 1 213 ALA 213 186 186 ALA ALA A . n 
A 1 214 LEU 214 187 187 LEU LEU A . n 
A 1 215 PRO 215 188 188 PRO PRO A . n 
A 1 216 VAL 216 189 189 VAL VAL A . n 
A 1 217 SER 217 190 190 SER SER A . n 
A 1 218 THR 218 191 191 THR THR A . n 
A 1 219 ALA 219 192 192 ALA ALA A . n 
A 1 220 TYR 220 193 193 TYR TYR A . n 
A 1 221 HIS 221 194 194 HIS HIS A . n 
A 1 222 ILE 222 195 195 ILE ILE A . n 
A 1 223 LYS 223 196 196 LYS LYS A . n 
A 1 224 ASN 224 197 197 ASN ASN A . n 
A 1 225 PRO 225 198 198 PRO PRO A . n 
A 1 226 ILE 226 199 199 ILE ILE A . n 
A 1 227 GLY 227 200 200 GLY GLY A . n 
A 1 228 GLY 228 201 201 GLY GLY A . n 
A 1 229 VAL 229 202 202 VAL VAL A . n 
A 1 230 PHE 230 203 203 PHE PHE A . n 
A 1 231 PHE 231 204 204 PHE PHE A . n 
A 1 232 THR 232 205 205 THR THR A . n 
A 1 233 ASP 233 206 206 ASP ASP A . n 
A 1 234 SER 234 207 207 SER SER A . n 
A 1 235 PRO 235 208 208 PRO PRO A . n 
A 1 236 GLU 236 209 209 GLU GLU A . n 
A 1 237 HIS 237 210 210 HIS HIS A . n 
A 1 238 LEU 238 211 211 LEU LEU A . n 
A 1 239 LEU 239 212 212 LEU LEU A . n 
A 1 240 GLY 240 213 213 GLY GLY A . n 
A 1 241 TYR 241 214 214 TYR TYR A . n 
A 1 242 SER 242 215 215 SER SER A . n 
A 1 243 ARG 243 216 216 ARG ARG A . n 
A 1 244 ASP 244 217 217 ASP ASP A . n 
A 1 245 LEU 245 218 218 LEU LEU A . n 
A 1 246 ASP 246 219 219 ASP ASP A . n 
A 1 247 THR 247 220 220 THR THR A . n 
A 1 248 ASP 248 221 221 ASP ASP A . n 
A 1 249 VAL 249 222 222 VAL VAL A . n 
A 1 250 VAL 250 223 223 VAL VAL A . n 
A 1 251 ILE 251 224 224 ILE ILE A . n 
A 1 252 ASP 252 225 225 ASP ASP A . n 
A 1 253 LYS 253 226 226 LYS LYS A . n 
A 1 254 LEU 254 227 227 LEU LEU A . n 
A 1 255 LYS 255 228 228 LYS LYS A . n 
A 1 256 SER 256 229 229 SER SER A . n 
A 1 257 ALA 257 230 230 ALA ALA A . n 
A 1 258 LYS 258 231 231 LYS LYS A . n 
A 1 259 THR 259 232 232 THR THR A . n 
A 1 260 SER 260 233 233 SER SER A . n 
A 1 261 ILE 261 234 234 ILE ILE A . n 
A 1 262 ASP 262 235 235 ASP ASP A . n 
A 1 263 ILE 263 236 236 ILE ILE A . n 
A 1 264 GLU 264 237 237 GLU GLU A . n 
A 1 265 HIS 265 238 238 HIS HIS A . n 
A 1 266 LEU 266 239 239 LEU LEU A . n 
A 1 267 ALA 267 240 240 ALA ALA A . n 
A 1 268 ILE 268 241 241 ILE ILE A . n 
A 1 269 VAL 269 242 242 VAL VAL A . n 
A 1 270 PRO 270 243 243 PRO PRO A . n 
A 1 271 THR 271 244 244 THR THR A . n 
A 1 272 THR 272 245 245 THR THR A . n 
A 1 273 ARG 273 246 246 ARG ARG A . n 
A 1 274 VAL 274 247 247 VAL VAL A . n 
A 1 275 ASP 275 248 248 ASP ASP A . n 
A 1 276 GLY 276 249 249 GLY GLY A . n 
A 1 277 ASN 277 250 250 ASN ASN A . n 
A 1 278 SER 278 251 251 SER SER A . n 
A 1 279 TYR 279 252 252 TYR TYR A . n 
A 1 280 TYR 280 253 253 TYR TYR A . n 
A 1 281 TRP 281 254 254 TRP TRP A . n 
A 1 282 PRO 282 255 255 PRO PRO A . n 
A 1 283 ASP 283 256 256 ASP ASP A . n 
A 1 284 ILE 284 257 257 ILE ILE A . n 
A 1 285 TYR 285 258 258 TYR TYR A . n 
A 1 286 ASN 286 259 259 ASN ASN A . n 
A 1 287 SER 287 260 260 SER SER A . n 
A 1 288 ILE 288 261 261 ILE ILE A . n 
A 1 289 ILE 289 262 262 ILE ILE A . n 
A 1 290 GLU 290 263 263 GLU GLU A . n 
A 1 291 ALA 291 264 264 ALA ALA A . n 
A 1 292 ALA 292 265 265 ALA ALA A . n 
A 1 293 ILE 293 266 266 ILE ILE A . n 
A 1 294 ASN 294 267 267 ASN ASN A . n 
A 1 295 ARG 295 268 268 ARG ARG A . n 
A 1 296 GLY 296 269 269 GLY GLY A . n 
A 1 297 VAL 297 270 270 VAL VAL A . n 
A 1 298 LYS 298 271 271 LYS LYS A . n 
A 1 299 ILE 299 272 272 ILE ILE A . n 
A 1 300 ARG 300 273 273 ARG ARG A . n 
A 1 301 LEU 301 274 274 LEU LEU A . n 
A 1 302 LEU 302 275 275 LEU LEU A . n 
A 1 303 VAL 303 276 276 VAL VAL A . n 
A 1 304 GLY 304 277 277 GLY GLY A . n 
A 1 305 ASN 305 278 278 ASN ASN A . n 
A 1 306 TRP 306 279 279 TRP TRP A . n 
A 1 307 ASP 307 280 280 ASP ASP A . n 
A 1 308 LYS 308 281 281 LYS LYS A . n 
A 1 309 ASN 309 282 282 ASN ASN A . n 
A 1 310 ASP 310 283 283 ASP ASP A . n 
A 1 311 VAL 311 284 284 VAL VAL A . n 
A 1 312 TYR 312 285 285 TYR TYR A . n 
A 1 313 SER 313 286 286 SER SER A . n 
A 1 314 MET 314 287 287 MET MET A . n 
A 1 315 ALA 315 288 288 ALA ALA A . n 
A 1 316 THR 316 289 289 THR THR A . n 
A 1 317 ALA 317 290 290 ALA ALA A . n 
A 1 318 ARG 318 291 291 ARG ARG A . n 
A 1 319 SER 319 292 292 SER SER A . n 
A 1 320 LEU 320 293 293 LEU LEU A . n 
A 1 321 ASP 321 294 294 ASP ASP A . n 
A 1 322 ALA 322 295 295 ALA ALA A . n 
A 1 323 LEU 323 296 296 LEU LEU A . n 
A 1 324 CYS 324 297 297 CYS CYS A . n 
A 1 325 VAL 325 298 298 VAL VAL A . n 
A 1 326 GLN 326 299 299 GLN GLN A . n 
A 1 327 ASN 327 300 300 ASN ASN A . n 
A 1 328 ASP 328 301 301 ASP ASP A . n 
A 1 329 LEU 329 302 302 LEU LEU A . n 
A 1 330 SER 330 303 303 SER SER A . n 
A 1 331 VAL 331 304 304 VAL VAL A . n 
A 1 332 LYS 332 305 305 LYS LYS A . n 
A 1 333 VAL 333 306 306 VAL VAL A . n 
A 1 334 PHE 334 307 307 PHE PHE A . n 
A 1 335 THR 335 308 308 THR THR A . n 
A 1 336 ILE 336 309 309 ILE ILE A . n 
A 1 337 GLN 337 310 310 GLN GLN A . n 
A 1 338 ASN 338 311 311 ASN ASN A . n 
A 1 339 ASN 339 312 312 ASN ASN A . n 
A 1 340 THR 340 313 313 THR THR A . n 
A 1 341 LYS 341 314 314 LYS LYS A . n 
A 1 342 LEU 342 315 315 LEU LEU A . n 
A 1 343 LEU 343 316 316 LEU LEU A . n 
A 1 344 ILE 344 317 317 ILE ILE A . n 
A 1 345 VAL 345 318 318 VAL VAL A . n 
A 1 346 ASP 346 319 319 ASP ASP A . n 
A 1 347 ASP 347 320 320 ASP ASP A . n 
A 1 348 GLU 348 321 321 GLU GLU A . n 
A 1 349 TYR 349 322 322 TYR TYR A . n 
A 1 350 VAL 350 323 323 VAL VAL A . n 
A 1 351 HIS 351 324 324 HIS HIS A . n 
A 1 352 ILE 352 325 325 ILE ILE A . n 
A 1 353 THR 353 326 326 THR THR A . n 
A 1 354 SER 354 327 327 SER SER A . n 
A 1 355 ALA 355 328 328 ALA ALA A . n 
A 1 356 ASN 356 329 329 ASN ASN A . n 
A 1 357 PHE 357 330 330 PHE PHE A . n 
A 1 358 ASP 358 331 331 ASP ASP A . n 
A 1 359 GLY 359 332 332 GLY GLY A . n 
A 1 360 THR 360 333 333 THR THR A . n 
A 1 361 HIS 361 334 334 HIS HIS A . n 
A 1 362 TYR 362 335 335 TYR TYR A . n 
A 1 363 GLN 363 336 336 GLN GLN A . n 
A 1 364 ASN 364 337 337 ASN ASN A . n 
A 1 365 HIS 365 338 338 HIS HIS A . n 
A 1 366 GLY 366 339 339 GLY GLY A . n 
A 1 367 PHE 367 340 340 PHE PHE A . n 
A 1 368 VAL 368 341 341 VAL VAL A . n 
A 1 369 SER 369 342 342 SER SER A . n 
A 1 370 PHE 370 343 343 PHE PHE A . n 
A 1 371 ASN 371 344 344 ASN ASN A . n 
A 1 372 SER 372 345 345 SER SER A . n 
A 1 373 ILE 373 346 346 ILE ILE A . n 
A 1 374 ASP 374 347 347 ASP ASP A . n 
A 1 375 LYS 375 348 348 LYS LYS A . n 
A 1 376 GLN 376 349 349 GLN GLN A . n 
A 1 377 LEU 377 350 350 LEU LEU A . n 
A 1 378 VAL 378 351 351 VAL VAL A . n 
A 1 379 SER 379 352 352 SER SER A . n 
A 1 380 GLU 380 353 353 GLU GLU A . n 
A 1 381 ALA 381 354 354 ALA ALA A . n 
A 1 382 LYS 382 355 355 LYS LYS A . n 
A 1 383 LYS 383 356 356 LYS LYS A . n 
A 1 384 ILE 384 357 357 ILE ILE A . n 
A 1 385 PHE 385 358 358 PHE PHE A . n 
A 1 386 GLU 386 359 359 GLU GLU A . n 
A 1 387 ARG 387 360 360 ARG ARG A . n 
A 1 388 ASP 388 361 361 ASP ASP A . n 
A 1 389 TRP 389 362 362 TRP TRP A . n 
A 1 390 VAL 390 363 363 VAL VAL A . n 
A 1 391 SER 391 364 364 SER SER A . n 
A 1 392 SER 392 365 365 SER SER A . n 
A 1 393 HIS 393 366 366 HIS HIS A . n 
A 1 394 SER 394 367 367 SER SER A . n 
A 1 395 LYS 395 368 368 LYS LYS A . n 
A 1 396 SER 396 369 369 SER SER A . n 
A 1 397 LEU 397 370 370 LEU LEU A . n 
A 1 398 LYS 398 371 371 LYS LYS A . n 
A 1 399 ILE 399 372 372 ILE ILE A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1IDM ? ? A1IDM ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GOL   ? ? GOL   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 CIT   ? ? CIT   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CIT   1 401 401 CIT   CIT A . 
C 3 GOL   1 402 402 GOL   GOL A . 
D 4 A1IDM 1 403 403 A1IDM IMC A . 
E 3 GOL   1 404 404 GOL   GOL A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.21_5207 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FJ1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     282.805 
_cell.length_a_esd                 ? 
_cell.length_b                     282.805 
_cell.length_b_esd                 ? 
_cell.length_c                     282.805 
_cell.length_c_esd                 ? 
_cell.volume                       22618367.211 
_cell.volume_esd                   ? 
_cell.Z_PDB                        96 
_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                         9FJ1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                209 
_symmetry.space_group_name_Hall            'F 4 2 3' 
_symmetry.space_group_name_H-M             'F 4 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FJ1 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             5.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          76.84 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'1 M Na3 citrate, 0.1 M Imidazole pH 8 (cryoprotected with 33% glycerol, soaked with 1 mM IMCBH)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.980112240579 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SOLEIL BEAMLINE PROXIMA 2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.980112240579 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 2' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          158.11 
_reflns.entry_id                                       9FJ1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.80 
_reflns.d_resolution_low                               47.80 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     10019 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                46.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.80 
_reflns_shell.d_res_low                                     4.25 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2745 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.430 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               161.16 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9FJ1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.80 
_refine.ls_d_res_low                             47.13 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     9986 
_refine.ls_number_reflns_R_free                  502 
_refine.ls_number_reflns_R_work                  9484 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.54 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2099 
_refine.ls_R_factor_R_free                       0.2470 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2079 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.8321 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3821 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.80 
_refine_hist.d_res_low                        47.13 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2929 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2884 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         45 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0017 ? 2986 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4223 ? 4047 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0406 ? 459  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0035 ? 517  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 9.5430 ? 1077 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.80 4.19  . . 123 2264 98.31  . . . . 0.3051 . . . . . . . . . . . 0.3661 
'X-RAY DIFFRACTION' 4.19 4.79  . . 129 2314 100.00 . . . . 0.2238 . . . . . . . . . . . 0.2640 
'X-RAY DIFFRACTION' 4.79 6.03  . . 116 2370 100.00 . . . . 0.2255 . . . . . . . . . . . 0.2599 
'X-RAY DIFFRACTION' 6.03 47.13 . . 134 2536 99.81  . . . . 0.1752 . . . . . . . . . . . 0.2154 
# 
_struct.entry_id                     9FJ1 
_struct.title                        'Structure of the F13 protein of Vaccinia virus in complex with IMCBH' 
_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        9FJ1 
_struct_keywords.text            'poxvirus, phospholipase D, vaccinia virus, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PG057_VACCW 
_struct_ref.pdbx_db_accession          P04021 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ASVPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASEKGIKIIVLLD
ERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYPPLATDLRRRF
DTFKAFNSAKNSWLNLCSAACCLPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLKSAKTSIDIEHLAIVPT
TRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATARSLDALCVQNDLSVKVFTIQNNTKLLIVDDEYVH
ITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI
;
_struct_ref.pdbx_align_begin           5 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9FJ1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 32 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 399 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P04021 
_struct_ref_seq.db_align_beg                  5 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  372 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       5 
_struct_ref_seq.pdbx_auth_seq_align_end       372 
# 
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 9FJ1 HIS A 1   ? UNP P04021 ?   ?   'expression tag' -26 1  
1 9FJ1 HIS A 2   ? UNP P04021 ?   ?   'expression tag' -25 2  
1 9FJ1 HIS A 3   ? UNP P04021 ?   ?   'expression tag' -24 3  
1 9FJ1 HIS A 4   ? UNP P04021 ?   ?   'expression tag' -23 4  
1 9FJ1 HIS A 5   ? UNP P04021 ?   ?   'expression tag' -22 5  
1 9FJ1 HIS A 6   ? UNP P04021 ?   ?   'expression tag' -21 6  
1 9FJ1 HIS A 7   ? UNP P04021 ?   ?   'expression tag' -20 7  
1 9FJ1 HIS A 8   ? UNP P04021 ?   ?   'expression tag' -19 8  
1 9FJ1 GLY A 9   ? UNP P04021 ?   ?   'expression tag' -18 9  
1 9FJ1 SER A 10  ? UNP P04021 ?   ?   'expression tag' -17 10 
1 9FJ1 GLY A 11  ? UNP P04021 ?   ?   'expression tag' -16 11 
1 9FJ1 ALA A 12  ? UNP P04021 ?   ?   'expression tag' -15 12 
1 9FJ1 GLY A 13  ? UNP P04021 ?   ?   'expression tag' -14 13 
1 9FJ1 TRP A 14  ? UNP P04021 ?   ?   'expression tag' -13 14 
1 9FJ1 SER A 15  ? UNP P04021 ?   ?   'expression tag' -12 15 
1 9FJ1 HIS A 16  ? UNP P04021 ?   ?   'expression tag' -11 16 
1 9FJ1 PRO A 17  ? UNP P04021 ?   ?   'expression tag' -10 17 
1 9FJ1 GLN A 18  ? UNP P04021 ?   ?   'expression tag' -9  18 
1 9FJ1 PHE A 19  ? UNP P04021 ?   ?   'expression tag' -8  19 
1 9FJ1 GLU A 20  ? UNP P04021 ?   ?   'expression tag' -7  20 
1 9FJ1 LYS A 21  ? UNP P04021 ?   ?   'expression tag' -6  21 
1 9FJ1 GLY A 22  ? UNP P04021 ?   ?   'expression tag' -5  22 
1 9FJ1 GLY A 23  ? UNP P04021 ?   ?   'expression tag' -4  23 
1 9FJ1 SER A 24  ? UNP P04021 ?   ?   'expression tag' -3  24 
1 9FJ1 GLY A 25  ? UNP P04021 ?   ?   'expression tag' -2  25 
1 9FJ1 LEU A 26  ? UNP P04021 ?   ?   'expression tag' -1  26 
1 9FJ1 VAL A 27  ? UNP P04021 ?   ?   'expression tag' 0   27 
1 9FJ1 PRO A 28  ? UNP P04021 ?   ?   'expression tag' 1   28 
1 9FJ1 ARG A 29  ? UNP P04021 ?   ?   'expression tag' 2   29 
1 9FJ1 GLY A 30  ? UNP P04021 ?   ?   'expression tag' 3   30 
1 9FJ1 SER A 31  ? UNP P04021 ?   ?   'expression tag' 4   31 
1 9FJ1 GLY A 32  ? UNP P04021 ALA 5   conflict         5   32 
1 9FJ1 ALA A 204 ? UNP P04021 TRP 177 conflict         177 33 
1 9FJ1 ALA A 205 ? UNP P04021 LEU 178 conflict         178 34 
1 9FJ1 ALA A 208 ? UNP P04021 CYS 181 conflict         181 35 
1 9FJ1 ALA A 212 ? UNP P04021 CYS 185 conflict         185 36 
1 9FJ1 ALA A 213 ? UNP P04021 CYS 186 conflict         186 37 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4670  ? 
1 MORE         -15   ? 
1 'SSA (A^2)'  28700 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'equilibrium centrifugation' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z           1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 
1.0000000000  0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000    
2 'crystal symmetry operation' 28_544 x,-y-1/2,-z-1/2 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 
-1.0000000000 0.0000000000 -141.4025000000 0.0000000000 0.0000000000 -1.0000000000 -141.4025000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 35  ? ALA A 38  ? PRO A 8   ALA A 11  5 ? 4  
HELX_P HELX_P2  AA2 THR A 59  ? LEU A 69  ? THR A 32  LEU A 42  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 82  ? SER A 85  ? ASN A 55  SER A 58  5 ? 4  
HELX_P HELX_P4  AA4 THR A 86  ? LYS A 102 ? THR A 59  LYS A 75  1 ? 17 
HELX_P HELX_P5  AA5 ARG A 113 ? LYS A 115 ? ARG A 86  LYS A 88  5 ? 3  
HELX_P HELX_P6  AA6 ASN A 117 ? CYS A 125 ? ASN A 90  CYS A 98  1 ? 9  
HELX_P HELX_P7  AA7 THR A 164 ? HIS A 169 ? THR A 137 HIS A 142 1 ? 6  
HELX_P HELX_P8  AA8 TYR A 180 ? ALA A 196 ? TYR A 153 ALA A 169 1 ? 17 
HELX_P HELX_P9  AA9 LEU A 207 ? ALA A 213 ? LEU A 180 ALA A 186 1 ? 7  
HELX_P HELX_P10 AB1 PRO A 235 ? LEU A 239 ? PRO A 208 LEU A 212 5 ? 5  
HELX_P HELX_P11 AB2 LEU A 245 ? SER A 256 ? LEU A 218 SER A 229 1 ? 12 
HELX_P HELX_P12 AB3 PRO A 282 ? ASN A 294 ? PRO A 255 ASN A 267 1 ? 13 
HELX_P HELX_P13 AB4 ASP A 310 ? VAL A 325 ? ASP A 283 VAL A 298 1 ? 16 
HELX_P HELX_P14 AB5 ASP A 358 ? HIS A 365 ? ASP A 331 HIS A 338 1 ? 8  
HELX_P HELX_P15 AB6 ASP A 374 ? VAL A 390 ? ASP A 347 VAL A 363 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           234 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            207 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    235 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     208 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       3.79 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 57  ? THR A 58  ? LEU A 30  THR A 31  
AA1 2 CYS A 40  ? THR A 45  ? CYS A 13  THR A 18  
AA1 3 THR A 173 ? SER A 178 ? THR A 146 SER A 151 
AA1 4 ARG A 155 ? GLY A 159 ? ARG A 128 GLY A 132 
AA1 5 PHE A 148 ? SER A 151 ? PHE A 121 SER A 124 
AA1 6 TYR A 73  ? ALA A 77  ? TYR A 46  ALA A 50  
AA1 7 LYS A 105 ? ASP A 111 ? LYS A 78  ASP A 84  
AA1 8 ASN A 129 ? VAL A 133 ? ASN A 102 VAL A 106 
AA2 1 VAL A 229 ? SER A 234 ? VAL A 202 SER A 207 
AA2 2 PHE A 367 ? SER A 372 ? PHE A 340 SER A 345 
AA2 3 TYR A 349 ? ILE A 352 ? TYR A 322 ILE A 325 
AA2 4 LEU A 342 ? VAL A 345 ? LEU A 315 VAL A 318 
AA2 5 SER A 260 ? GLU A 264 ? SER A 233 GLU A 237 
AA2 6 LYS A 298 ? GLY A 304 ? LYS A 271 GLY A 277 
AA2 7 LEU A 329 ? PHE A 334 ? LEU A 302 PHE A 307 
AA2 8 LYS A 395 ? SER A 396 ? LYS A 368 SER A 369 
AA3 1 THR A 271 ? VAL A 274 ? THR A 244 VAL A 247 
AA3 2 ASN A 277 ? TYR A 280 ? ASN A 250 TYR A 253 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 57  ? O LEU A 30  N GLU A 44  ? N GLU A 17  
AA1 2 3 N VAL A 43  ? N VAL A 16  O GLY A 175 ? O GLY A 148 
AA1 3 4 O SER A 178 ? O SER A 151 N CYS A 156 ? N CYS A 129 
AA1 4 5 O ARG A 155 ? O ARG A 128 N SER A 151 ? N SER A 124 
AA1 5 6 O VAL A 150 ? O VAL A 123 N TYR A 75  ? N TYR A 48  
AA1 6 7 N ILE A 76  ? N ILE A 49  O LEU A 109 ? O LEU A 82  
AA1 7 8 N ILE A 106 ? N ILE A 79  O ASN A 129 ? O ASN A 102 
AA2 1 2 N THR A 232 ? N THR A 205 O SER A 369 ? O SER A 342 
AA2 2 3 O SER A 372 ? O SER A 345 N VAL A 350 ? N VAL A 323 
AA2 3 4 O TYR A 349 ? O TYR A 322 N VAL A 345 ? N VAL A 318 
AA2 4 5 O ILE A 344 ? O ILE A 317 N ASP A 262 ? N ASP A 235 
AA2 5 6 N ILE A 263 ? N ILE A 236 O LEU A 302 ? O LEU A 275 
AA2 6 7 N LEU A 301 ? N LEU A 274 O LYS A 332 ? O LYS A 305 
AA2 7 8 N VAL A 333 ? N VAL A 306 O LYS A 395 ? O LYS A 368 
AA3 1 2 N THR A 272 ? N THR A 245 O TYR A 279 ? O TYR A 252 
# 
_pdbx_entry_details.entry_id                   9FJ1 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OH 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   TYR 
_pdbx_validate_close_contact.auth_seq_id_1    46 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OD1 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   ASP 
_pdbx_validate_close_contact.auth_seq_id_2    126 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 55  ? ? -157.61 73.40   
2  1 GLU A 127 ? ? -132.52 -40.60  
3  1 ASP A 152 ? ? -98.36  33.06   
4  1 PHE A 170 ? ? -95.40  33.44   
5  1 LYS A 174 ? ? 65.70   162.05  
6  1 PRO A 188 ? ? -67.12  74.47   
7  1 ASN A 197 ? ? -150.43 73.17   
8  1 ASP A 248 ? ? 53.50   -114.17 
9  1 PHE A 330 ? ? -67.07  91.86   
10 1 ASN A 337 ? ? -130.41 -35.71  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z            
2  x,-z,y           
3  x,z,-y           
4  z,y,-x           
5  -z,y,x           
6  -y,x,z           
7  y,-x,z           
8  z,x,y            
9  y,z,x            
10 -y,-z,x          
11 z,-x,-y          
12 -y,z,-x          
13 -z,-x,y          
14 -z,x,-y          
15 y,-z,-x          
16 x,-y,-z          
17 -x,y,-z          
18 -x,-y,z          
19 y,x,-z           
20 -y,-x,-z         
21 z,-y,x           
22 -z,-y,-x         
23 -x,z,y           
24 -x,-z,-y         
25 x,y+1/2,z+1/2    
26 x,-z+1/2,y+1/2   
27 x,z+1/2,-y+1/2   
28 z,y+1/2,-x+1/2   
29 -z,y+1/2,x+1/2   
30 -y,x+1/2,z+1/2   
31 y,-x+1/2,z+1/2   
32 z,x+1/2,y+1/2    
33 y,z+1/2,x+1/2    
34 -y,-z+1/2,x+1/2  
35 z,-x+1/2,-y+1/2  
36 -y,z+1/2,-x+1/2  
37 -z,-x+1/2,y+1/2  
38 -z,x+1/2,-y+1/2  
39 y,-z+1/2,-x+1/2  
40 x,-y+1/2,-z+1/2  
41 -x,y+1/2,-z+1/2  
42 -x,-y+1/2,z+1/2  
43 y,x+1/2,-z+1/2   
44 -y,-x+1/2,-z+1/2 
45 z,-y+1/2,x+1/2   
46 -z,-y+1/2,-x+1/2 
47 -x,z+1/2,y+1/2   
48 -x,-z+1/2,-y+1/2 
49 x+1/2,y,z+1/2    
50 x+1/2,-z,y+1/2   
51 x+1/2,z,-y+1/2   
52 z+1/2,y,-x+1/2   
53 -z+1/2,y,x+1/2   
54 -y+1/2,x,z+1/2   
55 y+1/2,-x,z+1/2   
56 z+1/2,x,y+1/2    
57 y+1/2,z,x+1/2    
58 -y+1/2,-z,x+1/2  
59 z+1/2,-x,-y+1/2  
60 -y+1/2,z,-x+1/2  
61 -z+1/2,-x,y+1/2  
62 -z+1/2,x,-y+1/2  
63 y+1/2,-z,-x+1/2  
64 x+1/2,-y,-z+1/2  
65 -x+1/2,y,-z+1/2  
66 -x+1/2,-y,z+1/2  
67 y+1/2,x,-z+1/2   
68 -y+1/2,-x,-z+1/2 
69 z+1/2,-y,x+1/2   
70 -z+1/2,-y,-x+1/2 
71 -x+1/2,z,y+1/2   
72 -x+1/2,-z,-y+1/2 
73 x+1/2,y+1/2,z    
74 x+1/2,-z+1/2,y   
75 x+1/2,z+1/2,-y   
76 z+1/2,y+1/2,-x   
77 -z+1/2,y+1/2,x   
78 -y+1/2,x+1/2,z   
79 y+1/2,-x+1/2,z   
80 z+1/2,x+1/2,y    
81 y+1/2,z+1/2,x    
82 -y+1/2,-z+1/2,x  
83 z+1/2,-x+1/2,-y  
84 -y+1/2,z+1/2,-x  
85 -z+1/2,-x+1/2,y  
86 -z+1/2,x+1/2,-y  
87 y+1/2,-z+1/2,-x  
88 x+1/2,-y+1/2,-z  
89 -x+1/2,y+1/2,-z  
90 -x+1/2,-y+1/2,z  
91 y+1/2,x+1/2,-z   
92 -y+1/2,-x+1/2,-z 
93 z+1/2,-y+1/2,x   
94 -z+1/2,-y+1/2,-x 
95 -x+1/2,z+1/2,y   
96 -x+1/2,-z+1/2,-y 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -21.6458774486 -46.4919485099 -44.346584228  1.11187536841  ? -0.152026896271 ? -0.256886632349  ? 
1.51508500881 ? -0.116836980848  ? 1.35888926361 ? 1.54014476    ? 0.356436730597 ? -1.3225764572   ? 1.75401441789  ? 
-0.508228124583 ? 2.88727986838 ? -0.0356827924322 ? -0.230005360667  ? 0.356862289069 ? 0.305567532643 ? 0.0400218743484 ? 
-0.630232192441 ? -0.0351363096243 ? 0.646197294252 ? 0.0514307558663  ? 
2 'X-RAY DIFFRACTION' ? refined -6.07799439623 -41.3088318889 -60.6852466543 2.84482897958  ? 0.131825769215  ? 0.510567584305   ? 
2.78834707202 ? 0.41173941303    ? 2.23725795179 ? 3.6834681235  ? -1.62087949099 ? -3.39295032181  ? 0.970353557451 ? 
1.73860346033   ? 3.44941248439 ? 0.0456674250638  ? 1.87719895477    ? 0.137557828738 ? -2.18324210673 ? -0.38757436084  ? 
-1.31568078362  ? 0.293305597987   ? 1.25393766172  ? 0.912000311534   ? 
3 'X-RAY DIFFRACTION' ? refined -26.4866254283 -65.3341440642 -56.2518706293 0.997742185768 ? 0.0815630135181 ? -0.0587226522561 ? 
1.09120283921 ? -0.0452147552359 ? 1.07407172402 ? 4.86033370448 ? 0.874763492117 ? -0.237066915611 ? 4.88606643323  ? 
0.985685130578  ? 5.35424866384 ? 0.224129474003   ? -0.0170229966616 ? 0.251995838803 ? 0.172948385499 ? -0.204914678638 ? 
-0.570521311894 ? 0.159583113651   ? 0.397130057167 ? -0.0661193645898 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 6   ? A 165 A 170 ? ? 
;chain 'A' and (resid 6 through 170 )
;
2 'X-RAY DIFFRACTION' 2 A 166 A 171 ? A 185 A 190 ? ? 
;chain 'A' and (resid 171 through 190 )
;
3 'X-RAY DIFFRACTION' 3 A 186 A 191 ? A 367 A 372 ? ? 
;chain 'A' and (resid 191 through 372 )
;
# 
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 HIS -26 ? A HIS 1  
2  1 Y 1 A HIS -25 ? A HIS 2  
3  1 Y 1 A HIS -24 ? A HIS 3  
4  1 Y 1 A HIS -23 ? A HIS 4  
5  1 Y 1 A HIS -22 ? A HIS 5  
6  1 Y 1 A HIS -21 ? A HIS 6  
7  1 Y 1 A HIS -20 ? A HIS 7  
8  1 Y 1 A HIS -19 ? A HIS 8  
9  1 Y 1 A GLY -18 ? A GLY 9  
10 1 Y 1 A SER -17 ? A SER 10 
11 1 Y 1 A GLY -16 ? A GLY 11 
12 1 Y 1 A ALA -15 ? A ALA 12 
13 1 Y 1 A GLY -14 ? A GLY 13 
14 1 Y 1 A TRP -13 ? A TRP 14 
15 1 Y 1 A SER -12 ? A SER 15 
16 1 Y 1 A HIS -11 ? A HIS 16 
17 1 Y 1 A PRO -10 ? A PRO 17 
18 1 Y 1 A GLN -9  ? A GLN 18 
19 1 Y 1 A PHE -8  ? A PHE 19 
20 1 Y 1 A GLU -7  ? A GLU 20 
21 1 Y 1 A LYS -6  ? A LYS 21 
22 1 Y 1 A GLY -5  ? A GLY 22 
23 1 Y 1 A GLY -4  ? A GLY 23 
24 1 Y 1 A SER -3  ? A SER 24 
25 1 Y 1 A GLY -2  ? A GLY 25 
26 1 Y 1 A LEU -1  ? A LEU 26 
27 1 Y 1 A VAL 0   ? A VAL 27 
28 1 Y 1 A PRO 1   ? A PRO 28 
29 1 Y 1 A ARG 2   ? A ARG 29 
30 1 Y 1 A GLY 3   ? A GLY 30 
31 1 Y 1 A SER 4   ? A SER 31 
32 1 Y 1 A GLY 5   ? A GLY 32 
# 
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 
A1IDM C01  C  N N 1   
A1IDM C02  C  Y N 2   
A1IDM C03  C  Y N 3   
A1IDM C04  C  Y N 4   
A1IDM C05  C  Y N 5   
A1IDM C06  C  Y N 6   
A1IDM C07  C  Y N 7   
A1IDM C08  C  N N 8   
A1IDM C12  C  N N 9   
A1IDM C14  C  Y N 10  
A1IDM C15  C  Y N 11  
A1IDM C16  C  Y N 12  
A1IDM C18  C  Y N 13  
A1IDM C19  C  Y N 14  
A1IDM N10  N  N N 15  
A1IDM N11  N  N N 16  
A1IDM N17  N  Y N 17  
A1IDM O09  O  N N 18  
A1IDM O13  O  N N 19  
A1IDM CL20 CL N N 20  
A1IDM H013 H  N N 21  
A1IDM H011 H  N N 22  
A1IDM H012 H  N N 23  
A1IDM H041 H  N N 24  
A1IDM H051 H  N N 25  
A1IDM H071 H  N N 26  
A1IDM H151 H  N N 27  
A1IDM H161 H  N N 28  
A1IDM H181 H  N N 29  
A1IDM H191 H  N N 30  
A1IDM H101 H  N N 31  
A1IDM H111 H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CIT   C1   C  N N 106 
CIT   O1   O  N N 107 
CIT   O2   O  N N 108 
CIT   C2   C  N N 109 
CIT   C3   C  N N 110 
CIT   O7   O  N N 111 
CIT   C4   C  N N 112 
CIT   C5   C  N N 113 
CIT   O3   O  N N 114 
CIT   O4   O  N N 115 
CIT   C6   C  N N 116 
CIT   O5   O  N N 117 
CIT   O6   O  N N 118 
CIT   HO2  H  N N 119 
CIT   H21  H  N N 120 
CIT   H22  H  N N 121 
CIT   HO7  H  N N 122 
CIT   H41  H  N N 123 
CIT   H42  H  N N 124 
CIT   HO4  H  N N 125 
CIT   HO6  H  N N 126 
CYS   N    N  N N 127 
CYS   CA   C  N R 128 
CYS   C    C  N N 129 
CYS   O    O  N N 130 
CYS   CB   C  N N 131 
CYS   SG   S  N N 132 
CYS   OXT  O  N N 133 
CYS   H    H  N N 134 
CYS   H2   H  N N 135 
CYS   HA   H  N N 136 
CYS   HB2  H  N N 137 
CYS   HB3  H  N N 138 
CYS   HG   H  N N 139 
CYS   HXT  H  N N 140 
GLN   N    N  N N 141 
GLN   CA   C  N S 142 
GLN   C    C  N N 143 
GLN   O    O  N N 144 
GLN   CB   C  N N 145 
GLN   CG   C  N N 146 
GLN   CD   C  N N 147 
GLN   OE1  O  N N 148 
GLN   NE2  N  N N 149 
GLN   OXT  O  N N 150 
GLN   H    H  N N 151 
GLN   H2   H  N N 152 
GLN   HA   H  N N 153 
GLN   HB2  H  N N 154 
GLN   HB3  H  N N 155 
GLN   HG2  H  N N 156 
GLN   HG3  H  N N 157 
GLN   HE21 H  N N 158 
GLN   HE22 H  N N 159 
GLN   HXT  H  N N 160 
GLU   N    N  N N 161 
GLU   CA   C  N S 162 
GLU   C    C  N N 163 
GLU   O    O  N N 164 
GLU   CB   C  N N 165 
GLU   CG   C  N N 166 
GLU   CD   C  N N 167 
GLU   OE1  O  N N 168 
GLU   OE2  O  N N 169 
GLU   OXT  O  N N 170 
GLU   H    H  N N 171 
GLU   H2   H  N N 172 
GLU   HA   H  N N 173 
GLU   HB2  H  N N 174 
GLU   HB3  H  N N 175 
GLU   HG2  H  N N 176 
GLU   HG3  H  N N 177 
GLU   HE2  H  N N 178 
GLU   HXT  H  N N 179 
GLY   N    N  N N 180 
GLY   CA   C  N N 181 
GLY   C    C  N N 182 
GLY   O    O  N N 183 
GLY   OXT  O  N N 184 
GLY   H    H  N N 185 
GLY   H2   H  N N 186 
GLY   HA2  H  N N 187 
GLY   HA3  H  N N 188 
GLY   HXT  H  N N 189 
GOL   C1   C  N N 190 
GOL   O1   O  N N 191 
GOL   C2   C  N N 192 
GOL   O2   O  N N 193 
GOL   C3   C  N N 194 
GOL   O3   O  N N 195 
GOL   H11  H  N N 196 
GOL   H12  H  N N 197 
GOL   HO1  H  N N 198 
GOL   H2   H  N N 199 
GOL   HO2  H  N N 200 
GOL   H31  H  N N 201 
GOL   H32  H  N N 202 
GOL   HO3  H  N N 203 
HIS   N    N  N N 204 
HIS   CA   C  N S 205 
HIS   C    C  N N 206 
HIS   O    O  N N 207 
HIS   CB   C  N N 208 
HIS   CG   C  Y N 209 
HIS   ND1  N  Y N 210 
HIS   CD2  C  Y N 211 
HIS   CE1  C  Y N 212 
HIS   NE2  N  Y N 213 
HIS   OXT  O  N N 214 
HIS   H    H  N N 215 
HIS   H2   H  N N 216 
HIS   HA   H  N N 217 
HIS   HB2  H  N N 218 
HIS   HB3  H  N N 219 
HIS   HD1  H  N N 220 
HIS   HD2  H  N N 221 
HIS   HE1  H  N N 222 
HIS   HE2  H  N N 223 
HIS   HXT  H  N N 224 
ILE   N    N  N N 225 
ILE   CA   C  N S 226 
ILE   C    C  N N 227 
ILE   O    O  N N 228 
ILE   CB   C  N S 229 
ILE   CG1  C  N N 230 
ILE   CG2  C  N N 231 
ILE   CD1  C  N N 232 
ILE   OXT  O  N N 233 
ILE   H    H  N N 234 
ILE   H2   H  N N 235 
ILE   HA   H  N N 236 
ILE   HB   H  N N 237 
ILE   HG12 H  N N 238 
ILE   HG13 H  N N 239 
ILE   HG21 H  N N 240 
ILE   HG22 H  N N 241 
ILE   HG23 H  N N 242 
ILE   HD11 H  N N 243 
ILE   HD12 H  N N 244 
ILE   HD13 H  N N 245 
ILE   HXT  H  N N 246 
LEU   N    N  N N 247 
LEU   CA   C  N S 248 
LEU   C    C  N N 249 
LEU   O    O  N N 250 
LEU   CB   C  N N 251 
LEU   CG   C  N N 252 
LEU   CD1  C  N N 253 
LEU   CD2  C  N N 254 
LEU   OXT  O  N N 255 
LEU   H    H  N N 256 
LEU   H2   H  N N 257 
LEU   HA   H  N N 258 
LEU   HB2  H  N N 259 
LEU   HB3  H  N N 260 
LEU   HG   H  N N 261 
LEU   HD11 H  N N 262 
LEU   HD12 H  N N 263 
LEU   HD13 H  N N 264 
LEU   HD21 H  N N 265 
LEU   HD22 H  N N 266 
LEU   HD23 H  N N 267 
LEU   HXT  H  N N 268 
LYS   N    N  N N 269 
LYS   CA   C  N S 270 
LYS   C    C  N N 271 
LYS   O    O  N N 272 
LYS   CB   C  N N 273 
LYS   CG   C  N N 274 
LYS   CD   C  N N 275 
LYS   CE   C  N N 276 
LYS   NZ   N  N N 277 
LYS   OXT  O  N N 278 
LYS   H    H  N N 279 
LYS   H2   H  N N 280 
LYS   HA   H  N N 281 
LYS   HB2  H  N N 282 
LYS   HB3  H  N N 283 
LYS   HG2  H  N N 284 
LYS   HG3  H  N N 285 
LYS   HD2  H  N N 286 
LYS   HD3  H  N N 287 
LYS   HE2  H  N N 288 
LYS   HE3  H  N N 289 
LYS   HZ1  H  N N 290 
LYS   HZ2  H  N N 291 
LYS   HZ3  H  N N 292 
LYS   HXT  H  N N 293 
MET   N    N  N N 294 
MET   CA   C  N S 295 
MET   C    C  N N 296 
MET   O    O  N N 297 
MET   CB   C  N N 298 
MET   CG   C  N N 299 
MET   SD   S  N N 300 
MET   CE   C  N N 301 
MET   OXT  O  N N 302 
MET   H    H  N N 303 
MET   H2   H  N N 304 
MET   HA   H  N N 305 
MET   HB2  H  N N 306 
MET   HB3  H  N N 307 
MET   HG2  H  N N 308 
MET   HG3  H  N N 309 
MET   HE1  H  N N 310 
MET   HE2  H  N N 311 
MET   HE3  H  N N 312 
MET   HXT  H  N N 313 
PHE   N    N  N N 314 
PHE   CA   C  N S 315 
PHE   C    C  N N 316 
PHE   O    O  N N 317 
PHE   CB   C  N N 318 
PHE   CG   C  Y N 319 
PHE   CD1  C  Y N 320 
PHE   CD2  C  Y N 321 
PHE   CE1  C  Y N 322 
PHE   CE2  C  Y N 323 
PHE   CZ   C  Y N 324 
PHE   OXT  O  N N 325 
PHE   H    H  N N 326 
PHE   H2   H  N N 327 
PHE   HA   H  N N 328 
PHE   HB2  H  N N 329 
PHE   HB3  H  N N 330 
PHE   HD1  H  N N 331 
PHE   HD2  H  N N 332 
PHE   HE1  H  N N 333 
PHE   HE2  H  N N 334 
PHE   HZ   H  N N 335 
PHE   HXT  H  N N 336 
PRO   N    N  N N 337 
PRO   CA   C  N S 338 
PRO   C    C  N N 339 
PRO   O    O  N N 340 
PRO   CB   C  N N 341 
PRO   CG   C  N N 342 
PRO   CD   C  N N 343 
PRO   OXT  O  N N 344 
PRO   H    H  N N 345 
PRO   HA   H  N N 346 
PRO   HB2  H  N N 347 
PRO   HB3  H  N N 348 
PRO   HG2  H  N N 349 
PRO   HG3  H  N N 350 
PRO   HD2  H  N N 351 
PRO   HD3  H  N N 352 
PRO   HXT  H  N N 353 
SER   N    N  N N 354 
SER   CA   C  N S 355 
SER   C    C  N N 356 
SER   O    O  N N 357 
SER   CB   C  N N 358 
SER   OG   O  N N 359 
SER   OXT  O  N N 360 
SER   H    H  N N 361 
SER   H2   H  N N 362 
SER   HA   H  N N 363 
SER   HB2  H  N N 364 
SER   HB3  H  N N 365 
SER   HG   H  N N 366 
SER   HXT  H  N N 367 
THR   N    N  N N 368 
THR   CA   C  N S 369 
THR   C    C  N N 370 
THR   O    O  N N 371 
THR   CB   C  N R 372 
THR   OG1  O  N N 373 
THR   CG2  C  N N 374 
THR   OXT  O  N N 375 
THR   H    H  N N 376 
THR   H2   H  N N 377 
THR   HA   H  N N 378 
THR   HB   H  N N 379 
THR   HG1  H  N N 380 
THR   HG21 H  N N 381 
THR   HG22 H  N N 382 
THR   HG23 H  N N 383 
THR   HXT  H  N N 384 
TRP   N    N  N N 385 
TRP   CA   C  N S 386 
TRP   C    C  N N 387 
TRP   O    O  N N 388 
TRP   CB   C  N N 389 
TRP   CG   C  Y N 390 
TRP   CD1  C  Y N 391 
TRP   CD2  C  Y N 392 
TRP   NE1  N  Y N 393 
TRP   CE2  C  Y N 394 
TRP   CE3  C  Y N 395 
TRP   CZ2  C  Y N 396 
TRP   CZ3  C  Y N 397 
TRP   CH2  C  Y N 398 
TRP   OXT  O  N N 399 
TRP   H    H  N N 400 
TRP   H2   H  N N 401 
TRP   HA   H  N N 402 
TRP   HB2  H  N N 403 
TRP   HB3  H  N N 404 
TRP   HD1  H  N N 405 
TRP   HE1  H  N N 406 
TRP   HE3  H  N N 407 
TRP   HZ2  H  N N 408 
TRP   HZ3  H  N N 409 
TRP   HH2  H  N N 410 
TRP   HXT  H  N N 411 
TYR   N    N  N N 412 
TYR   CA   C  N S 413 
TYR   C    C  N N 414 
TYR   O    O  N N 415 
TYR   CB   C  N N 416 
TYR   CG   C  Y N 417 
TYR   CD1  C  Y N 418 
TYR   CD2  C  Y N 419 
TYR   CE1  C  Y N 420 
TYR   CE2  C  Y N 421 
TYR   CZ   C  Y N 422 
TYR   OH   O  N N 423 
TYR   OXT  O  N N 424 
TYR   H    H  N N 425 
TYR   H2   H  N N 426 
TYR   HA   H  N N 427 
TYR   HB2  H  N N 428 
TYR   HB3  H  N N 429 
TYR   HD1  H  N N 430 
TYR   HD2  H  N N 431 
TYR   HE1  H  N N 432 
TYR   HE2  H  N N 433 
TYR   HH   H  N N 434 
TYR   HXT  H  N N 435 
VAL   N    N  N N 436 
VAL   CA   C  N S 437 
VAL   C    C  N N 438 
VAL   O    O  N N 439 
VAL   CB   C  N N 440 
VAL   CG1  C  N N 441 
VAL   CG2  C  N N 442 
VAL   OXT  O  N N 443 
VAL   H    H  N N 444 
VAL   H2   H  N N 445 
VAL   HA   H  N N 446 
VAL   HB   H  N N 447 
VAL   HG11 H  N N 448 
VAL   HG12 H  N N 449 
VAL   HG13 H  N N 450 
VAL   HG21 H  N N 451 
VAL   HG22 H  N N 452 
VAL   HG23 H  N N 453 
VAL   HXT  H  N N 454 
# 
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 
A1IDM C02  C01  sing N N 1   
A1IDM C03  C02  doub Y N 2   
A1IDM C05  C04  doub Y N 3   
A1IDM C06  C05  sing Y N 4   
A1IDM C07  C06  doub Y N 5   
A1IDM C08  C06  sing N N 6   
A1IDM O09  C08  doub N N 7   
A1IDM N10  C08  sing N N 8   
A1IDM N11  N10  sing N N 9   
A1IDM C12  N11  sing N N 10  
A1IDM O13  C12  doub N N 11  
A1IDM C14  C12  sing N N 12  
A1IDM C15  C14  doub Y N 13  
A1IDM C16  C15  sing Y N 14  
A1IDM N17  C16  doub Y N 15  
A1IDM C18  N17  sing Y N 16  
A1IDM C19  C18  doub Y N 17  
A1IDM C04  C03  sing Y N 18  
A1IDM CL20 C03  sing N N 19  
A1IDM C02  C07  sing Y N 20  
A1IDM C14  C19  sing Y N 21  
A1IDM C01  H013 sing N N 22  
A1IDM C01  H011 sing N N 23  
A1IDM C01  H012 sing N N 24  
A1IDM C04  H041 sing N N 25  
A1IDM C05  H051 sing N N 26  
A1IDM C07  H071 sing N N 27  
A1IDM C15  H151 sing N N 28  
A1IDM C16  H161 sing N N 29  
A1IDM C18  H181 sing N N 30  
A1IDM C19  H191 sing N N 31  
A1IDM N10  H101 sing N N 32  
A1IDM N11  H111 sing N N 33  
ALA   N    CA   sing N N 34  
ALA   N    H    sing N N 35  
ALA   N    H2   sing N N 36  
ALA   CA   C    sing N N 37  
ALA   CA   CB   sing N N 38  
ALA   CA   HA   sing N N 39  
ALA   C    O    doub N N 40  
ALA   C    OXT  sing N N 41  
ALA   CB   HB1  sing N N 42  
ALA   CB   HB2  sing N N 43  
ALA   CB   HB3  sing N N 44  
ALA   OXT  HXT  sing N N 45  
ARG   N    CA   sing N N 46  
ARG   N    H    sing N N 47  
ARG   N    H2   sing N N 48  
ARG   CA   C    sing N N 49  
ARG   CA   CB   sing N N 50  
ARG   CA   HA   sing N N 51  
ARG   C    O    doub N N 52  
ARG   C    OXT  sing N N 53  
ARG   CB   CG   sing N N 54  
ARG   CB   HB2  sing N N 55  
ARG   CB   HB3  sing N N 56  
ARG   CG   CD   sing N N 57  
ARG   CG   HG2  sing N N 58  
ARG   CG   HG3  sing N N 59  
ARG   CD   NE   sing N N 60  
ARG   CD   HD2  sing N N 61  
ARG   CD   HD3  sing N N 62  
ARG   NE   CZ   sing N N 63  
ARG   NE   HE   sing N N 64  
ARG   CZ   NH1  sing N N 65  
ARG   CZ   NH2  doub N N 66  
ARG   NH1  HH11 sing N N 67  
ARG   NH1  HH12 sing N N 68  
ARG   NH2  HH21 sing N N 69  
ARG   NH2  HH22 sing N N 70  
ARG   OXT  HXT  sing N N 71  
ASN   N    CA   sing N N 72  
ASN   N    H    sing N N 73  
ASN   N    H2   sing N N 74  
ASN   CA   C    sing N N 75  
ASN   CA   CB   sing N N 76  
ASN   CA   HA   sing N N 77  
ASN   C    O    doub N N 78  
ASN   C    OXT  sing N N 79  
ASN   CB   CG   sing N N 80  
ASN   CB   HB2  sing N N 81  
ASN   CB   HB3  sing N N 82  
ASN   CG   OD1  doub N N 83  
ASN   CG   ND2  sing N N 84  
ASN   ND2  HD21 sing N N 85  
ASN   ND2  HD22 sing N N 86  
ASN   OXT  HXT  sing N N 87  
ASP   N    CA   sing N N 88  
ASP   N    H    sing N N 89  
ASP   N    H2   sing N N 90  
ASP   CA   C    sing N N 91  
ASP   CA   CB   sing N N 92  
ASP   CA   HA   sing N N 93  
ASP   C    O    doub N N 94  
ASP   C    OXT  sing N N 95  
ASP   CB   CG   sing N N 96  
ASP   CB   HB2  sing N N 97  
ASP   CB   HB3  sing N N 98  
ASP   CG   OD1  doub N N 99  
ASP   CG   OD2  sing N N 100 
ASP   OD2  HD2  sing N N 101 
ASP   OXT  HXT  sing N N 102 
CIT   C1   O1   doub N N 103 
CIT   C1   O2   sing N N 104 
CIT   C1   C2   sing N N 105 
CIT   O2   HO2  sing N N 106 
CIT   C2   C3   sing N N 107 
CIT   C2   H21  sing N N 108 
CIT   C2   H22  sing N N 109 
CIT   C3   O7   sing N N 110 
CIT   C3   C4   sing N N 111 
CIT   C3   C6   sing N N 112 
CIT   O7   HO7  sing N N 113 
CIT   C4   C5   sing N N 114 
CIT   C4   H41  sing N N 115 
CIT   C4   H42  sing N N 116 
CIT   C5   O3   doub N N 117 
CIT   C5   O4   sing N N 118 
CIT   O4   HO4  sing N N 119 
CIT   C6   O5   doub N N 120 
CIT   C6   O6   sing N N 121 
CIT   O6   HO6  sing N N 122 
CYS   N    CA   sing N N 123 
CYS   N    H    sing N N 124 
CYS   N    H2   sing N N 125 
CYS   CA   C    sing N N 126 
CYS   CA   CB   sing N N 127 
CYS   CA   HA   sing N N 128 
CYS   C    O    doub N N 129 
CYS   C    OXT  sing N N 130 
CYS   CB   SG   sing N N 131 
CYS   CB   HB2  sing N N 132 
CYS   CB   HB3  sing N N 133 
CYS   SG   HG   sing N N 134 
CYS   OXT  HXT  sing N N 135 
GLN   N    CA   sing N N 136 
GLN   N    H    sing N N 137 
GLN   N    H2   sing N N 138 
GLN   CA   C    sing N N 139 
GLN   CA   CB   sing N N 140 
GLN   CA   HA   sing N N 141 
GLN   C    O    doub N N 142 
GLN   C    OXT  sing N N 143 
GLN   CB   CG   sing N N 144 
GLN   CB   HB2  sing N N 145 
GLN   CB   HB3  sing N N 146 
GLN   CG   CD   sing N N 147 
GLN   CG   HG2  sing N N 148 
GLN   CG   HG3  sing N N 149 
GLN   CD   OE1  doub N N 150 
GLN   CD   NE2  sing N N 151 
GLN   NE2  HE21 sing N N 152 
GLN   NE2  HE22 sing N N 153 
GLN   OXT  HXT  sing N N 154 
GLU   N    CA   sing N N 155 
GLU   N    H    sing N N 156 
GLU   N    H2   sing N N 157 
GLU   CA   C    sing N N 158 
GLU   CA   CB   sing N N 159 
GLU   CA   HA   sing N N 160 
GLU   C    O    doub N N 161 
GLU   C    OXT  sing N N 162 
GLU   CB   CG   sing N N 163 
GLU   CB   HB2  sing N N 164 
GLU   CB   HB3  sing N N 165 
GLU   CG   CD   sing N N 166 
GLU   CG   HG2  sing N N 167 
GLU   CG   HG3  sing N N 168 
GLU   CD   OE1  doub N N 169 
GLU   CD   OE2  sing N N 170 
GLU   OE2  HE2  sing N N 171 
GLU   OXT  HXT  sing N N 172 
GLY   N    CA   sing N N 173 
GLY   N    H    sing N N 174 
GLY   N    H2   sing N N 175 
GLY   CA   C    sing N N 176 
GLY   CA   HA2  sing N N 177 
GLY   CA   HA3  sing N N 178 
GLY   C    O    doub N N 179 
GLY   C    OXT  sing N N 180 
GLY   OXT  HXT  sing N N 181 
GOL   C1   O1   sing N N 182 
GOL   C1   C2   sing N N 183 
GOL   C1   H11  sing N N 184 
GOL   C1   H12  sing N N 185 
GOL   O1   HO1  sing N N 186 
GOL   C2   O2   sing N N 187 
GOL   C2   C3   sing N N 188 
GOL   C2   H2   sing N N 189 
GOL   O2   HO2  sing N N 190 
GOL   C3   O3   sing N N 191 
GOL   C3   H31  sing N N 192 
GOL   C3   H32  sing N N 193 
GOL   O3   HO3  sing N N 194 
HIS   N    CA   sing N N 195 
HIS   N    H    sing N N 196 
HIS   N    H2   sing N N 197 
HIS   CA   C    sing N N 198 
HIS   CA   CB   sing N N 199 
HIS   CA   HA   sing N N 200 
HIS   C    O    doub N N 201 
HIS   C    OXT  sing N N 202 
HIS   CB   CG   sing N N 203 
HIS   CB   HB2  sing N N 204 
HIS   CB   HB3  sing N N 205 
HIS   CG   ND1  sing Y N 206 
HIS   CG   CD2  doub Y N 207 
HIS   ND1  CE1  doub Y N 208 
HIS   ND1  HD1  sing N N 209 
HIS   CD2  NE2  sing Y N 210 
HIS   CD2  HD2  sing N N 211 
HIS   CE1  NE2  sing Y N 212 
HIS   CE1  HE1  sing N N 213 
HIS   NE2  HE2  sing N N 214 
HIS   OXT  HXT  sing N N 215 
ILE   N    CA   sing N N 216 
ILE   N    H    sing N N 217 
ILE   N    H2   sing N N 218 
ILE   CA   C    sing N N 219 
ILE   CA   CB   sing N N 220 
ILE   CA   HA   sing N N 221 
ILE   C    O    doub N N 222 
ILE   C    OXT  sing N N 223 
ILE   CB   CG1  sing N N 224 
ILE   CB   CG2  sing N N 225 
ILE   CB   HB   sing N N 226 
ILE   CG1  CD1  sing N N 227 
ILE   CG1  HG12 sing N N 228 
ILE   CG1  HG13 sing N N 229 
ILE   CG2  HG21 sing N N 230 
ILE   CG2  HG22 sing N N 231 
ILE   CG2  HG23 sing N N 232 
ILE   CD1  HD11 sing N N 233 
ILE   CD1  HD12 sing N N 234 
ILE   CD1  HD13 sing N N 235 
ILE   OXT  HXT  sing N N 236 
LEU   N    CA   sing N N 237 
LEU   N    H    sing N N 238 
LEU   N    H2   sing N N 239 
LEU   CA   C    sing N N 240 
LEU   CA   CB   sing N N 241 
LEU   CA   HA   sing N N 242 
LEU   C    O    doub N N 243 
LEU   C    OXT  sing N N 244 
LEU   CB   CG   sing N N 245 
LEU   CB   HB2  sing N N 246 
LEU   CB   HB3  sing N N 247 
LEU   CG   CD1  sing N N 248 
LEU   CG   CD2  sing N N 249 
LEU   CG   HG   sing N N 250 
LEU   CD1  HD11 sing N N 251 
LEU   CD1  HD12 sing N N 252 
LEU   CD1  HD13 sing N N 253 
LEU   CD2  HD21 sing N N 254 
LEU   CD2  HD22 sing N N 255 
LEU   CD2  HD23 sing N N 256 
LEU   OXT  HXT  sing N N 257 
LYS   N    CA   sing N N 258 
LYS   N    H    sing N N 259 
LYS   N    H2   sing N N 260 
LYS   CA   C    sing N N 261 
LYS   CA   CB   sing N N 262 
LYS   CA   HA   sing N N 263 
LYS   C    O    doub N N 264 
LYS   C    OXT  sing N N 265 
LYS   CB   CG   sing N N 266 
LYS   CB   HB2  sing N N 267 
LYS   CB   HB3  sing N N 268 
LYS   CG   CD   sing N N 269 
LYS   CG   HG2  sing N N 270 
LYS   CG   HG3  sing N N 271 
LYS   CD   CE   sing N N 272 
LYS   CD   HD2  sing N N 273 
LYS   CD   HD3  sing N N 274 
LYS   CE   NZ   sing N N 275 
LYS   CE   HE2  sing N N 276 
LYS   CE   HE3  sing N N 277 
LYS   NZ   HZ1  sing N N 278 
LYS   NZ   HZ2  sing N N 279 
LYS   NZ   HZ3  sing N N 280 
LYS   OXT  HXT  sing N N 281 
MET   N    CA   sing N N 282 
MET   N    H    sing N N 283 
MET   N    H2   sing N N 284 
MET   CA   C    sing N N 285 
MET   CA   CB   sing N N 286 
MET   CA   HA   sing N N 287 
MET   C    O    doub N N 288 
MET   C    OXT  sing N N 289 
MET   CB   CG   sing N N 290 
MET   CB   HB2  sing N N 291 
MET   CB   HB3  sing N N 292 
MET   CG   SD   sing N N 293 
MET   CG   HG2  sing N N 294 
MET   CG   HG3  sing N N 295 
MET   SD   CE   sing N N 296 
MET   CE   HE1  sing N N 297 
MET   CE   HE2  sing N N 298 
MET   CE   HE3  sing N N 299 
MET   OXT  HXT  sing N N 300 
PHE   N    CA   sing N N 301 
PHE   N    H    sing N N 302 
PHE   N    H2   sing N N 303 
PHE   CA   C    sing N N 304 
PHE   CA   CB   sing N N 305 
PHE   CA   HA   sing N N 306 
PHE   C    O    doub N N 307 
PHE   C    OXT  sing N N 308 
PHE   CB   CG   sing N N 309 
PHE   CB   HB2  sing N N 310 
PHE   CB   HB3  sing N N 311 
PHE   CG   CD1  doub Y N 312 
PHE   CG   CD2  sing Y N 313 
PHE   CD1  CE1  sing Y N 314 
PHE   CD1  HD1  sing N N 315 
PHE   CD2  CE2  doub Y N 316 
PHE   CD2  HD2  sing N N 317 
PHE   CE1  CZ   doub Y N 318 
PHE   CE1  HE1  sing N N 319 
PHE   CE2  CZ   sing Y N 320 
PHE   CE2  HE2  sing N N 321 
PHE   CZ   HZ   sing N N 322 
PHE   OXT  HXT  sing N N 323 
PRO   N    CA   sing N N 324 
PRO   N    CD   sing N N 325 
PRO   N    H    sing N N 326 
PRO   CA   C    sing N N 327 
PRO   CA   CB   sing N N 328 
PRO   CA   HA   sing N N 329 
PRO   C    O    doub N N 330 
PRO   C    OXT  sing N N 331 
PRO   CB   CG   sing N N 332 
PRO   CB   HB2  sing N N 333 
PRO   CB   HB3  sing N N 334 
PRO   CG   CD   sing N N 335 
PRO   CG   HG2  sing N N 336 
PRO   CG   HG3  sing N N 337 
PRO   CD   HD2  sing N N 338 
PRO   CD   HD3  sing N N 339 
PRO   OXT  HXT  sing N N 340 
SER   N    CA   sing N N 341 
SER   N    H    sing N N 342 
SER   N    H2   sing N N 343 
SER   CA   C    sing N N 344 
SER   CA   CB   sing N N 345 
SER   CA   HA   sing N N 346 
SER   C    O    doub N N 347 
SER   C    OXT  sing N N 348 
SER   CB   OG   sing N N 349 
SER   CB   HB2  sing N N 350 
SER   CB   HB3  sing N N 351 
SER   OG   HG   sing N N 352 
SER   OXT  HXT  sing N N 353 
THR   N    CA   sing N N 354 
THR   N    H    sing N N 355 
THR   N    H2   sing N N 356 
THR   CA   C    sing N N 357 
THR   CA   CB   sing N N 358 
THR   CA   HA   sing N N 359 
THR   C    O    doub N N 360 
THR   C    OXT  sing N N 361 
THR   CB   OG1  sing N N 362 
THR   CB   CG2  sing N N 363 
THR   CB   HB   sing N N 364 
THR   OG1  HG1  sing N N 365 
THR   CG2  HG21 sing N N 366 
THR   CG2  HG22 sing N N 367 
THR   CG2  HG23 sing N N 368 
THR   OXT  HXT  sing N N 369 
TRP   N    CA   sing N N 370 
TRP   N    H    sing N N 371 
TRP   N    H2   sing N N 372 
TRP   CA   C    sing N N 373 
TRP   CA   CB   sing N N 374 
TRP   CA   HA   sing N N 375 
TRP   C    O    doub N N 376 
TRP   C    OXT  sing N N 377 
TRP   CB   CG   sing N N 378 
TRP   CB   HB2  sing N N 379 
TRP   CB   HB3  sing N N 380 
TRP   CG   CD1  doub Y N 381 
TRP   CG   CD2  sing Y N 382 
TRP   CD1  NE1  sing Y N 383 
TRP   CD1  HD1  sing N N 384 
TRP   CD2  CE2  doub Y N 385 
TRP   CD2  CE3  sing Y N 386 
TRP   NE1  CE2  sing Y N 387 
TRP   NE1  HE1  sing N N 388 
TRP   CE2  CZ2  sing Y N 389 
TRP   CE3  CZ3  doub Y N 390 
TRP   CE3  HE3  sing N N 391 
TRP   CZ2  CH2  doub Y N 392 
TRP   CZ2  HZ2  sing N N 393 
TRP   CZ3  CH2  sing Y N 394 
TRP   CZ3  HZ3  sing N N 395 
TRP   CH2  HH2  sing N N 396 
TRP   OXT  HXT  sing N N 397 
TYR   N    CA   sing N N 398 
TYR   N    H    sing N N 399 
TYR   N    H2   sing N N 400 
TYR   CA   C    sing N N 401 
TYR   CA   CB   sing N N 402 
TYR   CA   HA   sing N N 403 
TYR   C    O    doub N N 404 
TYR   C    OXT  sing N N 405 
TYR   CB   CG   sing N N 406 
TYR   CB   HB2  sing N N 407 
TYR   CB   HB3  sing N N 408 
TYR   CG   CD1  doub Y N 409 
TYR   CG   CD2  sing Y N 410 
TYR   CD1  CE1  sing Y N 411 
TYR   CD1  HD1  sing N N 412 
TYR   CD2  CE2  doub Y N 413 
TYR   CD2  HD2  sing N N 414 
TYR   CE1  CZ   doub Y N 415 
TYR   CE1  HE1  sing N N 416 
TYR   CE2  CZ   sing Y N 417 
TYR   CE2  HE2  sing N N 418 
TYR   CZ   OH   sing N N 419 
TYR   OH   HH   sing N N 420 
TYR   OXT  HXT  sing N N 421 
VAL   N    CA   sing N N 422 
VAL   N    H    sing N N 423 
VAL   N    H2   sing N N 424 
VAL   CA   C    sing N N 425 
VAL   CA   CB   sing N N 426 
VAL   CA   HA   sing N N 427 
VAL   C    O    doub N N 428 
VAL   C    OXT  sing N N 429 
VAL   CB   CG1  sing N N 430 
VAL   CB   CG2  sing N N 431 
VAL   CB   HB   sing N N 432 
VAL   CG1  HG11 sing N N 433 
VAL   CG1  HG12 sing N N 434 
VAL   CG1  HG13 sing N N 435 
VAL   CG2  HG21 sing N N 436 
VAL   CG2  HG22 sing N N 437 
VAL   CG2  HG23 sing N N 438 
VAL   OXT  HXT  sing N N 439 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ANR-22-CE11-0003 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'F 4 3 2' 
_space_group.name_Hall        'F 4 2 3' 
_space_group.IT_number        209 
_space_group.crystal_system   cubic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9FJ1 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.003536 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.003536 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.003536 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 5.96793  ? ? ? 14.89577 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 16.91359 ? ? ? 9.84058  ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 6.96715  ? ? ? 11.43723 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 7.96527  ? ? ? 9.05267  ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 15.91112 ? ? ? 10.84690 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . SER   A 1 33  ? -2.71751  -65.49046 -31.43793 1.000 162.39240 ? 6   SER   A N    1 
ATOM   2    C  CA   . SER   A 1 33  ? -3.64643  -66.27541 -32.24224 1.000 186.66014 ? 6   SER   A CA   1 
ATOM   3    C  C    . SER   A 1 33  ? -4.77420  -65.40407 -32.78468 1.000 195.33468 ? 6   SER   A C    1 
ATOM   4    O  O    . SER   A 1 33  ? -5.12519  -64.38435 -32.19059 1.000 199.80134 ? 6   SER   A O    1 
ATOM   5    C  CB   . SER   A 1 33  ? -4.22177  -67.43172 -31.42185 1.000 190.92736 ? 6   SER   A CB   1 
ATOM   6    O  OG   . SER   A 1 33  ? -4.88470  -66.95540 -30.26368 1.000 202.60522 ? 6   SER   A OG   1 
ATOM   7    N  N    . VAL   A 1 34  ? -5.33817  -65.81372 -33.91643 1.000 193.58669 ? 7   VAL   A N    1 
ATOM   8    C  CA   . VAL   A 1 34  ? -6.42038  -65.07244 -34.55881 1.000 181.76630 ? 7   VAL   A CA   1 
ATOM   9    C  C    . VAL   A 1 34  ? -7.75506  -65.67046 -34.12818 1.000 185.75396 ? 7   VAL   A C    1 
ATOM   10   O  O    . VAL   A 1 34  ? -7.83726  -66.88012 -33.86889 1.000 201.47775 ? 7   VAL   A O    1 
ATOM   11   C  CB   . VAL   A 1 34  ? -6.26814  -65.07927 -36.08846 1.000 172.73710 ? 7   VAL   A CB   1 
ATOM   12   C  CG1  . VAL   A 1 34  ? -5.03763  -64.28589 -36.49826 1.000 160.93143 ? 7   VAL   A CG1  1 
ATOM   13   C  CG2  . VAL   A 1 34  ? -6.18063  -66.50575 -36.60966 1.000 174.28953 ? 7   VAL   A CG2  1 
ATOM   14   N  N    . PRO   A 1 35  ? -8.81364  -64.87327 -34.02597 1.000 176.62496 ? 8   PRO   A N    1 
ATOM   15   C  CA   . PRO   A 1 35  ? -10.10698 -65.40854 -33.59518 1.000 188.60978 ? 8   PRO   A CA   1 
ATOM   16   C  C    . PRO   A 1 35  ? -10.86011 -66.07385 -34.73821 1.000 181.98423 ? 8   PRO   A C    1 
ATOM   17   O  O    . PRO   A 1 35  ? -10.66264 -65.77316 -35.91684 1.000 183.32289 ? 8   PRO   A O    1 
ATOM   18   C  CB   . PRO   A 1 35  ? -10.85058 -64.16412 -33.10018 1.000 186.92210 ? 8   PRO   A CB   1 
ATOM   19   C  CG   . PRO   A 1 35  ? -10.29643 -63.06226 -33.93853 1.000 169.04914 ? 8   PRO   A CG   1 
ATOM   20   C  CD   . PRO   A 1 35  ? -8.84744  -63.40855 -34.18695 1.000 166.28683 ? 8   PRO   A CD   1 
ATOM   21   N  N    . ALA   A 1 36  ? -11.74113 -66.99692 -34.35936 1.000 189.38739 ? 9   ALA   A N    1 
ATOM   22   C  CA   . ALA   A 1 36  ? -12.57553 -67.68343 -35.33575 1.000 181.23197 ? 9   ALA   A CA   1 
ATOM   23   C  C    . ALA   A 1 36  ? -13.67064 -66.75050 -35.83533 1.000 174.12989 ? 9   ALA   A C    1 
ATOM   24   O  O    . ALA   A 1 36  ? -14.35836 -66.10026 -35.04207 1.000 182.94650 ? 9   ALA   A O    1 
ATOM   25   C  CB   . ALA   A 1 36  ? -13.18739 -68.94163 -34.72314 1.000 201.20151 ? 9   ALA   A CB   1 
ATOM   26   N  N    . GLY   A 1 37  ? -13.83281 -66.68599 -37.15442 1.000 179.69101 ? 10  GLY   A N    1 
ATOM   27   C  CA   . GLY   A 1 37  ? -14.78789 -65.78324 -37.75643 1.000 180.80565 ? 10  GLY   A CA   1 
ATOM   28   C  C    . GLY   A 1 37  ? -14.33470 -64.34415 -37.85495 1.000 175.47568 ? 10  GLY   A C    1 
ATOM   29   O  O    . GLY   A 1 37  ? -15.07323 -63.52158 -38.41027 1.000 184.48515 ? 10  GLY   A O    1 
ATOM   30   N  N    . ALA   A 1 38  ? -13.15114 -64.01480 -37.32982 1.000 160.22659 ? 11  ALA   A N    1 
ATOM   31   C  CA   . ALA   A 1 38  ? -12.58515 -62.66494 -37.40126 1.000 165.08127 ? 11  ALA   A CA   1 
ATOM   32   C  C    . ALA   A 1 38  ? -13.48620 -61.63749 -36.71860 1.000 169.84601 ? 11  ALA   A C    1 
ATOM   33   O  O    . ALA   A 1 38  ? -13.67926 -60.52731 -37.21932 1.000 166.99174 ? 11  ALA   A O    1 
ATOM   34   C  CB   . ALA   A 1 38  ? -12.29520 -62.25826 -38.84861 1.000 153.70060 ? 11  ALA   A CB   1 
ATOM   35   N  N    . LYS   A 1 39  ? -14.03825 -62.01264 -35.56142 1.000 169.39124 ? 12  LYS   A N    1 
ATOM   36   C  CA   . LYS   A 1 39  ? -14.87776 -61.12700 -34.75024 1.000 175.30874 ? 12  LYS   A CA   1 
ATOM   37   C  C    . LYS   A 1 39  ? -16.05545 -60.56798 -35.54457 1.000 168.16115 ? 12  LYS   A C    1 
ATOM   38   O  O    . LYS   A 1 39  ? -16.51430 -59.45133 -35.29120 1.000 145.62451 ? 12  LYS   A O    1 
ATOM   39   C  CB   . LYS   A 1 39  ? -14.05615 -59.98341 -34.14573 1.000 167.27491 ? 12  LYS   A CB   1 
ATOM   40   C  CG   . LYS   A 1 39  ? -12.97356 -60.43232 -33.17744 1.000 161.74495 ? 12  LYS   A CG   1 
ATOM   41   C  CD   . LYS   A 1 39  ? -13.56713 -60.90946 -31.86121 1.000 184.04916 ? 12  LYS   A CD   1 
ATOM   42   C  CE   . LYS   A 1 39  ? -14.17765 -59.75797 -31.07645 1.000 173.93176 ? 12  LYS   A CE   1 
ATOM   43   N  NZ   . LYS   A 1 39  ? -13.15431 -58.75163 -30.67768 1.000 164.20775 ? 12  LYS   A NZ   1 
ATOM   44   N  N    . CYS   A 1 40  ? -16.55383 -61.33648 -36.50867 1.000 174.82149 ? 13  CYS   A N    1 
ATOM   45   C  CA   . CYS   A 1 40  ? -17.63472 -60.88664 -37.37297 1.000 162.57616 ? 13  CYS   A CA   1 
ATOM   46   C  C    . CYS   A 1 40  ? -18.98361 -61.30502 -36.80604 1.000 165.78630 ? 13  CYS   A C    1 
ATOM   47   O  O    . CYS   A 1 40  ? -19.13491 -62.41005 -36.27699 1.000 170.71542 ? 13  CYS   A O    1 
ATOM   48   C  CB   . CYS   A 1 40  ? -17.46615 -61.45087 -38.78413 1.000 153.69814 ? 13  CYS   A CB   1 
ATOM   49   S  SG   . CYS   A 1 40  ? -16.03541 -60.80612 -39.67776 1.000 153.85700 ? 13  CYS   A SG   1 
ATOM   50   N  N    . ARG   A 1 41  ? -19.96412 -60.41214 -36.92093 1.000 151.19281 ? 14  ARG   A N    1 
ATOM   51   C  CA   . ARG   A 1 41  ? -21.31835 -60.69884 -36.47703 1.000 152.42850 ? 14  ARG   A CA   1 
ATOM   52   C  C    . ARG   A 1 41  ? -22.30594 -60.15082 -37.49472 1.000 152.94615 ? 14  ARG   A C    1 
ATOM   53   O  O    . ARG   A 1 41  ? -22.04252 -59.15104 -38.16998 1.000 158.09936 ? 14  ARG   A O    1 
ATOM   54   C  CB   . ARG   A 1 41  ? -21.60333 -60.11086 -35.08839 1.000 166.47730 ? 14  ARG   A CB   1 
ATOM   55   C  CG   . ARG   A 1 41  ? -21.53526 -58.59617 -35.01293 1.000 142.90397 ? 14  ARG   A CG   1 
ATOM   56   C  CD   . ARG   A 1 41  ? -21.81779 -58.12078 -33.59804 1.000 166.21517 ? 14  ARG   A CD   1 
ATOM   57   N  NE   . ARG   A 1 41  ? -23.08510 -58.63938 -33.09684 1.000 177.64642 ? 14  ARG   A NE   1 
ATOM   58   C  CZ   . ARG   A 1 41  ? -23.48947 -58.54228 -31.83774 1.000 180.46646 ? 14  ARG   A CZ   1 
ATOM   59   N  NH1  . ARG   A 1 41  ? -22.74519 -57.95325 -30.91611 1.000 195.25814 ? 14  ARG   A NH1  1 
ATOM   60   N  NH2  . ARG   A 1 41  ? -24.66849 -59.05271 -31.49374 1.000 180.55522 ? 14  ARG   A NH2  1 
ATOM   61   N  N    . LEU   A 1 42  ? -23.44915 -60.82021 -37.59813 1.000 153.13042 ? 15  LEU   A N    1 
ATOM   62   C  CA   . LEU   A 1 42  ? -24.45100 -60.45124 -38.58471 1.000 139.43975 ? 15  LEU   A CA   1 
ATOM   63   C  C    . LEU   A 1 42  ? -25.19011 -59.19027 -38.15945 1.000 138.61037 ? 15  LEU   A C    1 
ATOM   64   O  O    . LEU   A 1 42  ? -25.48751 -58.98995 -36.97803 1.000 156.29630 ? 15  LEU   A O    1 
ATOM   65   C  CB   . LEU   A 1 42  ? -25.44213 -61.59527 -38.79438 1.000 148.70836 ? 15  LEU   A CB   1 
ATOM   66   C  CG   . LEU   A 1 42  ? -24.85015 -62.89005 -39.35369 1.000 144.20536 ? 15  LEU   A CG   1 
ATOM   67   C  CD1  . LEU   A 1 42  ? -25.95052 -63.88572 -39.68851 1.000 157.00517 ? 15  LEU   A CD1  1 
ATOM   68   C  CD2  . LEU   A 1 42  ? -23.98928 -62.60056 -40.57420 1.000 124.12715 ? 15  LEU   A CD2  1 
ATOM   69   N  N    . VAL   A 1 43  ? -25.47860 -58.33756 -39.13776 1.000 113.94213 ? 16  VAL   A N    1 
ATOM   70   C  CA   . VAL   A 1 43  ? -26.22238 -57.10154 -38.94888 1.000 136.07422 ? 16  VAL   A CA   1 
ATOM   71   C  C    . VAL   A 1 43  ? -27.29359 -57.05655 -40.02683 1.000 145.90954 ? 16  VAL   A C    1 
ATOM   72   O  O    . VAL   A 1 43  ? -27.05004 -57.47077 -41.16410 1.000 153.09576 ? 16  VAL   A O    1 
ATOM   73   C  CB   . VAL   A 1 43  ? -25.29470 -55.86972 -39.03388 1.000 130.28369 ? 16  VAL   A CB   1 
ATOM   74   C  CG1  . VAL   A 1 43  ? -26.09388 -54.58461 -39.01031 1.000 138.35587 ? 16  VAL   A CG1  1 
ATOM   75   C  CG2  . VAL   A 1 43  ? -24.28526 -55.88936 -37.90084 1.000 141.40034 ? 16  VAL   A CG2  1 
ATOM   76   N  N    . GLU   A 1 44  ? -28.48722 -56.58920 -39.67477 1.000 132.66166 ? 17  GLU   A N    1 
ATOM   77   C  CA   . GLU   A 1 44  ? -29.54092 -56.54530 -40.67726 1.000 144.40478 ? 17  GLU   A CA   1 
ATOM   78   C  C    . GLU   A 1 44  ? -30.59069 -55.51818 -40.28654 1.000 144.55774 ? 17  GLU   A C    1 
ATOM   79   O  O    . GLU   A 1 44  ? -30.74670 -55.16656 -39.11428 1.000 126.93492 ? 17  GLU   A O    1 
ATOM   80   C  CB   . GLU   A 1 44  ? -30.17848 -57.92517 -40.88601 1.000 144.60975 ? 17  GLU   A CB   1 
ATOM   81   C  CG   . GLU   A 1 44  ? -30.73910 -58.58203 -39.64439 1.000 153.68654 ? 17  GLU   A CG   1 
ATOM   82   C  CD   . GLU   A 1 44  ? -31.36163 -59.92981 -39.95367 1.000 168.73197 ? 17  GLU   A CD   1 
ATOM   83   O  OE1  . GLU   A 1 44  ? -31.54969 -60.23553 -41.15099 1.000 152.49816 ? 17  GLU   A OE1  1 
ATOM   84   O  OE2  . GLU   A 1 44  ? -31.65975 -60.68444 -39.00547 1.000 181.82346 ? 17  GLU   A OE2  1 
ATOM   85   N  N    . THR   A 1 45  ? -31.30158 -55.03945 -41.30221 1.000 156.85263 ? 18  THR   A N    1 
ATOM   86   C  CA   . THR   A 1 45  ? -32.38977 -54.08425 -41.14393 1.000 129.64857 ? 18  THR   A CA   1 
ATOM   87   C  C    . THR   A 1 45  ? -33.70308 -54.80661 -41.39564 1.000 136.39288 ? 18  THR   A C    1 
ATOM   88   O  O    . THR   A 1 45  ? -33.95924 -55.25876 -42.52026 1.000 134.25220 ? 18  THR   A O    1 
ATOM   89   C  CB   . THR   A 1 45  ? -32.24866 -52.90441 -42.10450 1.000 129.90986 ? 18  THR   A CB   1 
ATOM   90   O  OG1  . THR   A 1 45  ? -30.92762 -52.36167 -42.01148 1.000 132.71966 ? 18  THR   A OG1  1 
ATOM   91   C  CG2  . THR   A 1 45  ? -33.26004 -51.82197 -41.76135 1.000 140.00780 ? 18  THR   A CG2  1 
ATOM   92   N  N    . LEU   A 1 46  ? -34.52192 -54.90692 -40.35020 1.000 150.80390 ? 19  LEU   A N    1 
ATOM   93   C  CA   . LEU   A 1 46  ? -35.83129 -55.55729 -40.40037 1.000 135.92024 ? 19  LEU   A CA   1 
ATOM   94   C  C    . LEU   A 1 46  ? -36.88874 -54.54220 -39.99708 1.000 133.49517 ? 19  LEU   A C    1 
ATOM   95   O  O    . LEU   A 1 46  ? -37.03118 -54.23273 -38.79743 1.000 140.82186 ? 19  LEU   A O    1 
ATOM   96   C  CB   . LEU   A 1 46  ? -35.86978 -56.77182 -39.47531 1.000 129.80425 ? 19  LEU   A CB   1 
ATOM   97   C  CG   . LEU   A 1 46  ? -34.60948 -57.63891 -39.43608 1.000 131.65118 ? 19  LEU   A CG   1 
ATOM   98   C  CD1  . LEU   A 1 46  ? -34.72074 -58.69680 -38.34829 1.000 146.26260 ? 19  LEU   A CD1  1 
ATOM   99   C  CD2  . LEU   A 1 46  ? -34.34565 -58.27986 -40.79123 1.000 124.74049 ? 19  LEU   A CD2  1 
ATOM   100  N  N    . PRO   A 1 47  ? -37.64289 -53.98788 -40.94234 1.000 130.86864 ? 20  PRO   A N    1 
ATOM   101  C  CA   . PRO   A 1 47  ? -38.62621 -52.95416 -40.60336 1.000 144.22700 ? 20  PRO   A CA   1 
ATOM   102  C  C    . PRO   A 1 47  ? -39.72234 -53.48039 -39.68592 1.000 147.88751 ? 20  PRO   A C    1 
ATOM   103  O  O    . PRO   A 1 47  ? -39.94994 -54.68624 -39.56359 1.000 148.99687 ? 20  PRO   A O    1 
ATOM   104  C  CB   . PRO   A 1 47  ? -39.19528 -52.54186 -41.96602 1.000 141.18120 ? 20  PRO   A CB   1 
ATOM   105  C  CG   . PRO   A 1 47  ? -38.14532 -52.93882 -42.95074 1.000 120.00424 ? 20  PRO   A CG   1 
ATOM   106  C  CD   . PRO   A 1 47  ? -37.51512 -54.17760 -42.39723 1.000 128.52718 ? 20  PRO   A CD   1 
ATOM   107  N  N    . GLU   A 1 48  ? -40.41176 -52.53892 -39.03446 1.000 130.54946 ? 21  GLU   A N    1 
ATOM   108  C  CA   . GLU   A 1 48  ? -41.47751 -52.90623 -38.10735 1.000 147.16051 ? 21  GLU   A CA   1 
ATOM   109  C  C    . GLU   A 1 48  ? -42.67865 -53.50043 -38.83161 1.000 151.17872 ? 21  GLU   A C    1 
ATOM   110  O  O    . GLU   A 1 48  ? -43.35460 -54.38084 -38.28713 1.000 170.09182 ? 21  GLU   A O    1 
ATOM   111  C  CB   . GLU   A 1 48  ? -41.91009 -51.69036 -37.28488 1.000 167.31610 ? 21  GLU   A CB   1 
ATOM   112  C  CG   . GLU   A 1 48  ? -40.84767 -51.14703 -36.33830 1.000 173.60508 ? 21  GLU   A CG   1 
ATOM   113  C  CD   . GLU   A 1 48  ? -39.87508 -50.20382 -37.02040 1.000 160.40858 ? 21  GLU   A CD   1 
ATOM   114  O  OE1  . GLU   A 1 48  ? -40.08295 -49.88674 -38.21091 1.000 125.54221 ? 21  GLU   A OE1  1 
ATOM   115  O  OE2  . GLU   A 1 48  ? -38.90272 -49.77700 -36.36303 1.000 154.42166 ? 21  GLU   A OE2  1 
ATOM   116  N  N    . ASN   A 1 49  ? -42.96126 -53.03729 -40.04956 1.000 139.22360 ? 22  ASN   A N    1 
ATOM   117  C  CA   . ASN   A 1 49  ? -44.09105 -53.54763 -40.81753 1.000 149.49352 ? 22  ASN   A CA   1 
ATOM   118  C  C    . ASN   A 1 49  ? -43.85366 -54.94669 -41.36839 1.000 158.63958 ? 22  ASN   A C    1 
ATOM   119  O  O    . ASN   A 1 49  ? -44.77368 -55.52127 -41.96147 1.000 170.96168 ? 22  ASN   A O    1 
ATOM   120  C  CB   . ASN   A 1 49  ? -44.41747 -52.58822 -41.96388 1.000 140.85214 ? 22  ASN   A CB   1 
ATOM   121  C  CG   . ASN   A 1 49  ? -43.21754 -52.30397 -42.84549 1.000 167.59629 ? 22  ASN   A CG   1 
ATOM   122  O  OD1  . ASN   A 1 49  ? -42.42278 -51.40765 -42.56143 1.000 163.59339 ? 22  ASN   A OD1  1 
ATOM   123  N  ND2  . ASN   A 1 49  ? -43.08158 -53.06619 -43.92438 1.000 191.73935 ? 22  ASN   A ND2  1 
ATOM   124  N  N    . MET   A 1 50  ? -42.66133 -55.50549 -41.19004 1.000 146.19730 ? 23  MET   A N    1 
ATOM   125  C  CA   . MET   A 1 50  ? -42.32902 -56.83210 -41.68151 1.000 134.59494 ? 23  MET   A CA   1 
ATOM   126  C  C    . MET   A 1 50  ? -42.19507 -57.80273 -40.51533 1.000 145.42360 ? 23  MET   A C    1 
ATOM   127  O  O    . MET   A 1 50  ? -41.88284 -57.40775 -39.38828 1.000 159.88937 ? 23  MET   A O    1 
ATOM   128  C  CB   . MET   A 1 50  ? -41.03382 -56.80311 -42.49646 1.000 141.70728 ? 23  MET   A CB   1 
ATOM   129  C  CG   . MET   A 1 50  ? -41.06590 -55.82462 -43.65933 1.000 137.46997 ? 23  MET   A CG   1 
ATOM   130  S  SD   . MET   A 1 50  ? -39.58069 -55.88932 -44.67720 1.000 139.74846 ? 23  MET   A SD   1 
ATOM   131  C  CE   . MET   A 1 50  ? -39.92123 -54.58897 -45.86019 1.000 94.46812  ? 23  MET   A CE   1 
ATOM   132  N  N    . ASP   A 1 51  ? -42.43356 -59.08120 -40.79891 1.000 131.07670 ? 24  ASP   A N    1 
ATOM   133  C  CA   . ASP   A 1 51  ? -42.44389 -60.12107 -39.77930 1.000 148.76201 ? 24  ASP   A CA   1 
ATOM   134  C  C    . ASP   A 1 51  ? -41.05860 -60.68466 -39.48494 1.000 170.92636 ? 24  ASP   A C    1 
ATOM   135  O  O    . ASP   A 1 51  ? -40.95415 -61.70843 -38.80144 1.000 171.49814 ? 24  ASP   A O    1 
ATOM   136  C  CB   . ASP   A 1 51  ? -43.38688 -61.25491 -40.19463 1.000 137.93250 ? 24  ASP   A CB   1 
ATOM   137  C  CG   . ASP   A 1 51  ? -42.95668 -61.93221 -41.48349 1.000 152.92403 ? 24  ASP   A CG   1 
ATOM   138  O  OD1  . ASP   A 1 51  ? -42.02529 -62.76369 -41.44076 1.000 154.92055 ? 24  ASP   A OD1  1 
ATOM   139  O  OD2  . ASP   A 1 51  ? -43.55186 -61.63450 -42.54029 1.000 172.33614 ? 24  ASP   A OD2  1 
ATOM   140  N  N    . PHE   A 1 52  ? -39.99968 -60.04899 -39.97937 1.000 149.69913 ? 25  PHE   A N    1 
ATOM   141  C  CA   . PHE   A 1 52  ? -38.64521 -60.53076 -39.74046 1.000 127.87697 ? 25  PHE   A CA   1 
ATOM   142  C  C    . PHE   A 1 52  ? -38.21942 -60.17703 -38.32026 1.000 153.56873 ? 25  PHE   A C    1 
ATOM   143  O  O    . PHE   A 1 52  ? -38.25106 -59.00505 -37.92873 1.000 165.92733 ? 25  PHE   A O    1 
ATOM   144  C  CB   . PHE   A 1 52  ? -37.67591 -59.93437 -40.75823 1.000 129.30447 ? 25  PHE   A CB   1 
ATOM   145  C  CG   . PHE   A 1 52  ? -38.02445 -60.24743 -42.18501 1.000 139.32465 ? 25  PHE   A CG   1 
ATOM   146  C  CD1  . PHE   A 1 52  ? -37.68811 -61.46926 -42.74469 1.000 150.90148 ? 25  PHE   A CD1  1 
ATOM   147  C  CD2  . PHE   A 1 52  ? -38.68159 -59.31582 -42.96931 1.000 147.30321 ? 25  PHE   A CD2  1 
ATOM   148  C  CE1  . PHE   A 1 52  ? -38.00718 -61.75663 -44.05924 1.000 127.42943 ? 25  PHE   A CE1  1 
ATOM   149  C  CE2  . PHE   A 1 52  ? -39.00314 -59.59653 -44.28283 1.000 147.41354 ? 25  PHE   A CE2  1 
ATOM   150  C  CZ   . PHE   A 1 52  ? -38.66534 -60.81821 -44.82889 1.000 121.85815 ? 25  PHE   A CZ   1 
ATOM   151  N  N    . ARG   A 1 53  ? -37.82409 -61.18947 -37.55154 1.000 143.76530 ? 26  ARG   A N    1 
ATOM   152  C  CA   . ARG   A 1 53  ? -37.35785 -61.01256 -36.18424 1.000 157.95218 ? 26  ARG   A CA   1 
ATOM   153  C  C    . ARG   A 1 53  ? -36.04688 -61.76125 -36.00018 1.000 161.08776 ? 26  ARG   A C    1 
ATOM   154  O  O    . ARG   A 1 53  ? -35.87539 -62.86638 -36.52387 1.000 158.55441 ? 26  ARG   A O    1 
ATOM   155  C  CB   . ARG   A 1 53  ? -38.39193 -61.51598 -35.16724 1.000 181.25653 ? 26  ARG   A CB   1 
ATOM   156  C  CG   . ARG   A 1 53  ? -39.73727 -60.81090 -35.23217 1.000 180.85531 ? 26  ARG   A CG   1 
ATOM   157  C  CD   . ARG   A 1 53  ? -39.61377 -59.34289 -34.85999 1.000 182.43578 ? 26  ARG   A CD   1 
ATOM   158  N  NE   . ARG   A 1 53  ? -40.91604 -58.69371 -34.76636 1.000 197.41279 ? 26  ARG   A NE   1 
ATOM   159  C  CZ   . ARG   A 1 53  ? -41.52548 -58.08602 -35.77513 1.000 179.58362 ? 26  ARG   A CZ   1 
ATOM   160  N  NH1  . ARG   A 1 53  ? -40.97609 -58.02143 -36.97684 1.000 164.94090 ? 26  ARG   A NH1  1 
ATOM   161  N  NH2  . ARG   A 1 53  ? -42.71610 -57.52876 -35.57304 1.000 184.83579 ? 26  ARG   A NH2  1 
ATOM   162  N  N    . SER   A 1 54  ? -35.12470 -61.15554 -35.25583 1.000 165.20817 ? 27  SER   A N    1 
ATOM   163  C  CA   . SER   A 1 54  ? -33.83953 -61.78232 -34.98150 1.000 172.13563 ? 27  SER   A CA   1 
ATOM   164  C  C    . SER   A 1 54  ? -33.20908 -61.10655 -33.77461 1.000 165.43103 ? 27  SER   A C    1 
ATOM   165  O  O    . SER   A 1 54  ? -33.53572 -59.96615 -33.43569 1.000 167.61293 ? 27  SER   A O    1 
ATOM   166  C  CB   . SER   A 1 54  ? -32.89882 -61.70109 -36.18880 1.000 159.65820 ? 27  SER   A CB   1 
ATOM   167  O  OG   . SER   A 1 54  ? -32.42265 -60.37934 -36.37751 1.000 156.24895 ? 27  SER   A OG   1 
ATOM   168  N  N    . ASP   A 1 55  ? -32.29659 -61.82983 -33.13198 1.000 155.41862 ? 28  ASP   A N    1 
ATOM   169  C  CA   . ASP   A 1 55  ? -31.53217 -61.30328 -32.01088 1.000 170.59454 ? 28  ASP   A CA   1 
ATOM   170  C  C    . ASP   A 1 55  ? -30.22596 -60.65415 -32.44527 1.000 168.27110 ? 28  ASP   A C    1 
ATOM   171  O  O    . ASP   A 1 55  ? -29.46666 -60.18897 -31.58874 1.000 190.40424 ? 28  ASP   A O    1 
ATOM   172  C  CB   . ASP   A 1 55  ? -31.23787 -62.41817 -31.00138 1.000 190.50549 ? 28  ASP   A CB   1 
ATOM   173  C  CG   . ASP   A 1 55  ? -32.49531 -63.11002 -30.51199 1.000 213.40825 ? 28  ASP   A CG   1 
ATOM   174  O  OD1  . ASP   A 1 55  ? -33.56052 -62.45945 -30.47664 1.000 222.09597 ? 28  ASP   A OD1  1 
ATOM   175  O  OD2  . ASP   A 1 55  ? -32.41765 -64.30588 -30.16041 1.000 232.18700 ? 28  ASP   A OD2  1 
ATOM   176  N  N    . HIS   A 1 56  ? -29.94754 -60.61283 -33.74578 1.000 147.57744 ? 29  HIS   A N    1 
ATOM   177  C  CA   . HIS   A 1 56  ? -28.69287 -60.06362 -34.23128 1.000 154.10718 ? 29  HIS   A CA   1 
ATOM   178  C  C    . HIS   A 1 56  ? -28.69975 -58.53868 -34.14458 1.000 157.14751 ? 29  HIS   A C    1 
ATOM   179  O  O    . HIS   A 1 56  ? -29.69741 -57.90487 -33.78708 1.000 159.96866 ? 29  HIS   A O    1 
ATOM   180  C  CB   . HIS   A 1 56  ? -28.43394 -60.50613 -35.67123 1.000 149.94210 ? 29  HIS   A CB   1 
ATOM   181  C  CG   . HIS   A 1 56  ? -28.22907 -61.98069 -35.82235 1.000 150.58262 ? 29  HIS   A CG   1 
ATOM   182  N  ND1  . HIS   A 1 56  ? -28.97427 -62.74960 -36.68976 1.000 125.89389 ? 29  HIS   A ND1  1 
ATOM   183  C  CD2  . HIS   A 1 56  ? -27.36115 -62.82745 -35.21968 1.000 175.69822 ? 29  HIS   A CD2  1 
ATOM   184  C  CE1  . HIS   A 1 56  ? -28.57801 -64.00737 -36.61174 1.000 135.23407 ? 29  HIS   A CE1  1 
ATOM   185  N  NE2  . HIS   A 1 56  ? -27.59989 -64.08164 -35.72723 1.000 195.25442 ? 29  HIS   A NE2  1 
ATOM   186  N  N    . LEU   A 1 57  ? -27.55905 -57.95056 -34.49024 1.000 151.31357 ? 30  LEU   A N    1 
ATOM   187  C  CA   . LEU   A 1 57  ? -27.42177 -56.50368 -34.46224 1.000 133.58576 ? 30  LEU   A CA   1 
ATOM   188  C  C    . LEU   A 1 57  ? -28.20717 -55.87080 -35.60544 1.000 147.33305 ? 30  LEU   A C    1 
ATOM   189  O  O    . LEU   A 1 57  ? -28.35309 -56.44909 -36.68544 1.000 154.30989 ? 30  LEU   A O    1 
ATOM   190  C  CB   . LEU   A 1 57  ? -25.94637 -56.11122 -34.55377 1.000 133.25632 ? 30  LEU   A CB   1 
ATOM   191  C  CG   . LEU   A 1 57  ? -25.58389 -54.64576 -34.30750 1.000 138.69093 ? 30  LEU   A CG   1 
ATOM   192  C  CD1  . LEU   A 1 57  ? -25.93899 -54.24096 -32.88648 1.000 168.10180 ? 30  LEU   A CD1  1 
ATOM   193  C  CD2  . LEU   A 1 57  ? -24.10749 -54.39525 -34.58303 1.000 109.34519 ? 30  LEU   A CD2  1 
ATOM   194  N  N    . THR   A 1 58  ? -28.72438 -54.67317 -35.35529 1.000 139.60791 ? 31  THR   A N    1 
ATOM   195  C  CA   . THR   A 1 58  ? -29.42487 -53.90823 -36.37367 1.000 138.60277 ? 31  THR   A CA   1 
ATOM   196  C  C    . THR   A 1 58  ? -28.47475 -52.89767 -37.00458 1.000 132.37031 ? 31  THR   A C    1 
ATOM   197  O  O    . THR   A 1 58  ? -27.48697 -52.48114 -36.39412 1.000 139.71603 ? 31  THR   A O    1 
ATOM   198  C  CB   . THR   A 1 58  ? -30.64205 -53.18962 -35.78684 1.000 140.83059 ? 31  THR   A CB   1 
ATOM   199  O  OG1  . THR   A 1 58  ? -30.20741 -52.11783 -34.94061 1.000 119.08212 ? 31  THR   A OG1  1 
ATOM   200  C  CG2  . THR   A 1 58  ? -31.48715 -54.15940 -34.97468 1.000 137.71883 ? 31  THR   A CG2  1 
ATOM   201  N  N    . THR   A 1 59  ? -28.77978 -52.51594 -38.24675 1.000 131.24725 ? 32  THR   A N    1 
ATOM   202  C  CA   . THR   A 1 59  ? -27.93124 -51.56588 -38.95984 1.000 120.60017 ? 32  THR   A CA   1 
ATOM   203  C  C    . THR   A 1 59  ? -27.88317 -50.22260 -38.24298 1.000 116.56765 ? 32  THR   A C    1 
ATOM   204  O  O    . THR   A 1 59  ? -26.84290 -49.55366 -38.22739 1.000 140.76296 ? 32  THR   A O    1 
ATOM   205  C  CB   . THR   A 1 59  ? -28.43214 -51.39718 -40.39337 1.000 132.17515 ? 32  THR   A CB   1 
ATOM   206  O  OG1  . THR   A 1 59  ? -28.57246 -52.68686 -41.00437 1.000 148.72148 ? 32  THR   A OG1  1 
ATOM   207  C  CG2  . THR   A 1 59  ? -27.45582 -50.56911 -41.20507 1.000 127.79697 ? 32  THR   A CG2  1 
ATOM   208  N  N    . PHE   A 1 60  ? -28.99837 -49.81961 -37.63279 1.000 117.48321 ? 33  PHE   A N    1 
ATOM   209  C  CA   . PHE   A 1 60  ? -29.03369 -48.57140 -36.87809 1.000 139.31221 ? 33  PHE   A CA   1 
ATOM   210  C  C    . PHE   A 1 60  ? -28.05323 -48.61148 -35.71151 1.000 140.69661 ? 33  PHE   A C    1 
ATOM   211  O  O    . PHE   A 1 60  ? -27.19680 -47.72681 -35.56919 1.000 145.57436 ? 33  PHE   A O    1 
ATOM   212  C  CB   . PHE   A 1 60  ? -30.46133 -48.31706 -36.39161 1.000 140.15605 ? 33  PHE   A CB   1 
ATOM   213  C  CG   . PHE   A 1 60  ? -30.63119 -47.03627 -35.63136 1.000 145.87782 ? 33  PHE   A CG   1 
ATOM   214  C  CD1  . PHE   A 1 60  ? -30.58594 -45.81632 -36.28388 1.000 149.22721 ? 33  PHE   A CD1  1 
ATOM   215  C  CD2  . PHE   A 1 60  ? -30.86068 -47.05327 -34.26618 1.000 146.10746 ? 33  PHE   A CD2  1 
ATOM   216  C  CE1  . PHE   A 1 60  ? -30.75071 -44.63576 -35.58595 1.000 155.63177 ? 33  PHE   A CE1  1 
ATOM   217  C  CE2  . PHE   A 1 60  ? -31.02654 -45.87749 -33.56313 1.000 148.31969 ? 33  PHE   A CE2  1 
ATOM   218  C  CZ   . PHE   A 1 60  ? -30.97153 -44.66695 -34.22351 1.000 152.95419 ? 33  PHE   A CZ   1 
ATOM   219  N  N    . GLU   A 1 61  ? -28.16630 -49.64101 -34.86598 1.000 144.09926 ? 34  GLU   A N    1 
ATOM   220  C  CA   . GLU   A 1 61  ? -27.22319 -49.81697 -33.76745 1.000 148.42398 ? 34  GLU   A CA   1 
ATOM   221  C  C    . GLU   A 1 61  ? -25.79600 -49.97124 -34.27516 1.000 138.66663 ? 34  GLU   A C    1 
ATOM   222  O  O    . GLU   A 1 61  ? -24.85387 -49.50379 -33.62655 1.000 129.86296 ? 34  GLU   A O    1 
ATOM   223  C  CB   . GLU   A 1 61  ? -27.61632 -51.03422 -32.92774 1.000 160.59167 ? 34  GLU   A CB   1 
ATOM   224  C  CG   . GLU   A 1 61  ? -28.97052 -50.92900 -32.25396 1.000 176.51243 ? 34  GLU   A CG   1 
ATOM   225  C  CD   . GLU   A 1 61  ? -29.41883 -52.24559 -31.64665 1.000 184.31731 ? 34  GLU   A CD   1 
ATOM   226  O  OE1  . GLU   A 1 61  ? -28.97528 -53.30629 -32.13418 1.000 157.10530 ? 34  GLU   A OE1  1 
ATOM   227  O  OE2  . GLU   A 1 61  ? -30.20937 -52.22137 -30.67944 1.000 188.76934 ? 34  GLU   A OE2  1 
ATOM   228  N  N    . CYS   A 1 62  ? -25.61671 -50.61861 -35.42950 1.000 148.81099 ? 35  CYS   A N    1 
ATOM   229  C  CA   . CYS   A 1 62  ? -24.27737 -50.80640 -35.97969 1.000 141.18061 ? 35  CYS   A CA   1 
ATOM   230  C  C    . CYS   A 1 62  ? -23.63328 -49.46946 -36.32547 1.000 137.51306 ? 35  CYS   A C    1 
ATOM   231  O  O    . CYS   A 1 62  ? -22.48239 -49.20465 -35.95509 1.000 147.00493 ? 35  CYS   A O    1 
ATOM   232  C  CB   . CYS   A 1 62  ? -24.34143 -51.71023 -37.21176 1.000 137.94802 ? 35  CYS   A CB   1 
ATOM   233  S  SG   . CYS   A 1 62  ? -22.78879 -51.83241 -38.12444 1.000 142.13272 ? 35  CYS   A SG   1 
ATOM   234  N  N    . PHE   A 1 63  ? -24.36336 -48.61265 -37.04273 1.000 138.25542 ? 36  PHE   A N    1 
ATOM   235  C  CA   . PHE   A 1 63  ? -23.82365 -47.30338 -37.39256 1.000 132.09221 ? 36  PHE   A CA   1 
ATOM   236  C  C    . PHE   A 1 63  ? -23.61527 -46.44720 -36.15017 1.000 131.55228 ? 36  PHE   A C    1 
ATOM   237  O  O    . PHE   A 1 63  ? -22.63842 -45.69097 -36.06536 1.000 131.27074 ? 36  PHE   A O    1 
ATOM   238  C  CB   . PHE   A 1 63  ? -24.74653 -46.59981 -38.38773 1.000 144.03004 ? 36  PHE   A CB   1 
ATOM   239  C  CG   . PHE   A 1 63  ? -24.78237 -47.24515 -39.74661 1.000 131.21896 ? 36  PHE   A CG   1 
ATOM   240  C  CD1  . PHE   A 1 63  ? -23.81416 -48.16315 -40.12190 1.000 126.57797 ? 36  PHE   A CD1  1 
ATOM   241  C  CD2  . PHE   A 1 63  ? -25.78259 -46.92787 -40.65105 1.000 130.80141 ? 36  PHE   A CD2  1 
ATOM   242  C  CE1  . PHE   A 1 63  ? -23.84641 -48.75627 -41.37049 1.000 122.81402 ? 36  PHE   A CE1  1 
ATOM   243  C  CE2  . PHE   A 1 63  ? -25.81875 -47.51561 -41.90200 1.000 127.60510 ? 36  PHE   A CE2  1 
ATOM   244  C  CZ   . PHE   A 1 63  ? -24.84897 -48.43091 -42.26191 1.000 123.24237 ? 36  PHE   A CZ   1 
ATOM   245  N  N    . ASN   A 1 64  ? -24.51680 -46.56011 -35.16848 1.000 140.05271 ? 37  ASN   A N    1 
ATOM   246  C  CA   . ASN   A 1 64  ? -24.32875 -45.83335 -33.91619 1.000 138.76676 ? 37  ASN   A CA   1 
ATOM   247  C  C    . ASN   A 1 64  ? -23.04242 -46.25803 -33.21808 1.000 143.89171 ? 37  ASN   A C    1 
ATOM   248  O  O    . ASN   A 1 64  ? -22.29572 -45.41365 -32.71048 1.000 156.04702 ? 37  ASN   A O    1 
ATOM   249  C  CB   . ASN   A 1 64  ? -25.53099 -46.04195 -32.99535 1.000 158.16586 ? 37  ASN   A CB   1 
ATOM   250  C  CG   . ASN   A 1 64  ? -26.66059 -45.07290 -33.28220 1.000 187.26611 ? 37  ASN   A CG   1 
ATOM   251  O  OD1  . ASN   A 1 64  ? -26.58196 -43.89246 -32.93994 1.000 157.19043 ? 37  ASN   A OD1  1 
ATOM   252  N  ND2  . ASN   A 1 64  ? -27.72451 -45.56950 -33.90219 1.000 197.60110 ? 37  ASN   A ND2  1 
ATOM   253  N  N    . GLU   A 1 65  ? -22.76254 -47.56309 -33.18926 1.000 143.68807 ? 38  GLU   A N    1 
ATOM   254  C  CA   . GLU   A 1 65  ? -21.54489 -48.04489 -32.54447 1.000 139.70402 ? 38  GLU   A CA   1 
ATOM   255  C  C    . GLU   A 1 65  ? -20.30380 -47.62783 -33.32397 1.000 152.13800 ? 38  GLU   A C    1 
ATOM   256  O  O    . GLU   A 1 65  ? -19.27089 -47.30142 -32.72701 1.000 161.56129 ? 38  GLU   A O    1 
ATOM   257  C  CB   . GLU   A 1 65  ? -21.59962 -49.56576 -32.38915 1.000 137.18516 ? 38  GLU   A CB   1 
ATOM   258  C  CG   . GLU   A 1 65  ? -20.36179 -50.18890 -31.74791 1.000 125.95355 ? 38  GLU   A CG   1 
ATOM   259  C  CD   . GLU   A 1 65  ? -20.36316 -50.09953 -30.23028 1.000 166.76419 ? 38  GLU   A CD   1 
ATOM   260  O  OE1  . GLU   A 1 65  ? -21.12678 -49.28357 -29.67210 1.000 166.59385 ? 38  GLU   A OE1  1 
ATOM   261  O  OE2  . GLU   A 1 65  ? -19.60048 -50.85588 -29.59245 1.000 189.10999 ? 38  GLU   A OE2  1 
ATOM   262  N  N    . ILE   A 1 66  ? -20.38500 -47.62947 -34.65716 1.000 156.49752 ? 39  ILE   A N    1 
ATOM   263  C  CA   . ILE   A 1 66  ? -19.24296 -47.20785 -35.46598 1.000 139.25769 ? 39  ILE   A CA   1 
ATOM   264  C  C    . ILE   A 1 66  ? -18.93393 -45.73455 -35.22814 1.000 138.14521 ? 39  ILE   A C    1 
ATOM   265  O  O    . ILE   A 1 66  ? -17.76625 -45.33982 -35.11610 1.000 128.14324 ? 39  ILE   A O    1 
ATOM   266  C  CB   . ILE   A 1 66  ? -19.49944 -47.50058 -36.95655 1.000 147.37631 ? 39  ILE   A CB   1 
ATOM   267  C  CG1  . ILE   A 1 66  ? -19.50055 -49.00909 -37.21012 1.000 156.14796 ? 39  ILE   A CG1  1 
ATOM   268  C  CG2  . ILE   A 1 66  ? -18.45516 -46.81390 -37.82811 1.000 137.94812 ? 39  ILE   A CG2  1 
ATOM   269  C  CD1  . ILE   A 1 66  ? -19.67687 -49.38516 -38.66383 1.000 132.74960 ? 39  ILE   A CD1  1 
ATOM   270  N  N    . ILE   A 1 67  ? -19.97145 -44.89990 -35.13111 1.000 151.32713 ? 40  ILE   A N    1 
ATOM   271  C  CA   . ILE   A 1 67  ? -19.74607 -43.46642 -34.96463 1.000 136.29945 ? 40  ILE   A CA   1 
ATOM   272  C  C    . ILE   A 1 67  ? -19.30895 -43.14685 -33.53814 1.000 141.23674 ? 40  ILE   A C    1 
ATOM   273  O  O    . ILE   A 1 67  ? -18.45871 -42.27566 -33.31622 1.000 159.98012 ? 40  ILE   A O    1 
ATOM   274  C  CB   . ILE   A 1 67  ? -21.00662 -42.67978 -35.36858 1.000 148.82969 ? 40  ILE   A CB   1 
ATOM   275  C  CG1  . ILE   A 1 67  ? -21.28044 -42.85932 -36.86307 1.000 152.60157 ? 40  ILE   A CG1  1 
ATOM   276  C  CG2  . ILE   A 1 67  ? -20.85626 -41.20531 -35.02828 1.000 120.41802 ? 40  ILE   A CG2  1 
ATOM   277  C  CD1  . ILE   A 1 67  ? -22.47640 -42.08625 -37.36538 1.000 117.83142 ? 40  ILE   A CD1  1 
ATOM   278  N  N    . THR   A 1 68  ? -19.86818 -43.84979 -32.55084 1.000 137.66173 ? 41  THR   A N    1 
ATOM   279  C  CA   . THR   A 1 68  ? -19.55217 -43.55325 -31.15595 1.000 147.72574 ? 41  THR   A CA   1 
ATOM   280  C  C    . THR   A 1 68  ? -18.10538 -43.90446 -30.82606 1.000 159.68221 ? 41  THR   A C    1 
ATOM   281  O  O    . THR   A 1 68  ? -17.37524 -43.09208 -30.24557 1.000 166.00996 ? 41  THR   A O    1 
ATOM   282  C  CB   . THR   A 1 68  ? -20.51284 -44.30249 -30.23127 1.000 138.01889 ? 41  THR   A CB   1 
ATOM   283  O  OG1  . THR   A 1 68  ? -21.85134 -43.84496 -30.46059 1.000 148.39957 ? 41  THR   A OG1  1 
ATOM   284  C  CG2  . THR   A 1 68  ? -20.14524 -44.06954 -28.77375 1.000 154.79939 ? 41  THR   A CG2  1 
ATOM   285  N  N    . LEU   A 1 69  ? -17.67183 -45.11050 -31.18715 1.000 161.18019 ? 42  LEU   A N    1 
ATOM   286  C  CA   . LEU   A 1 69  ? -16.30832 -45.54396 -30.90840 1.000 171.37144 ? 42  LEU   A CA   1 
ATOM   287  C  C    . LEU   A 1 69  ? -15.28333 -44.94350 -31.86195 1.000 182.84612 ? 42  LEU   A C    1 
ATOM   288  O  O    . LEU   A 1 69  ? -14.10014 -45.28874 -31.76876 1.000 194.58003 ? 42  LEU   A O    1 
ATOM   289  C  CB   . LEU   A 1 69  ? -16.21909 -47.07129 -30.96003 1.000 164.15132 ? 42  LEU   A CB   1 
ATOM   290  C  CG   . LEU   A 1 69  ? -17.11444 -47.84967 -29.99563 1.000 150.83920 ? 42  LEU   A CG   1 
ATOM   291  C  CD1  . LEU   A 1 69  ? -16.80240 -49.33594 -30.07007 1.000 163.06502 ? 42  LEU   A CD1  1 
ATOM   292  C  CD2  . LEU   A 1 69  ? -16.95679 -47.33257 -28.57419 1.000 163.72860 ? 42  LEU   A CD2  1 
ATOM   293  N  N    . ALA   A 1 70  ? -15.69982 -44.06274 -32.76777 1.000 172.86636 ? 43  ALA   A N    1 
ATOM   294  C  CA   . ALA   A 1 70  ? -14.77241 -43.47369 -33.72290 1.000 167.36570 ? 43  ALA   A CA   1 
ATOM   295  C  C    . ALA   A 1 70  ? -13.85964 -42.46980 -33.03092 1.000 177.90520 ? 43  ALA   A C    1 
ATOM   296  O  O    . ALA   A 1 70  ? -14.31759 -41.62880 -32.25118 1.000 171.58648 ? 43  ALA   A O    1 
ATOM   297  C  CB   . ALA   A 1 70  ? -15.53849 -42.79782 -34.85692 1.000 166.29386 ? 43  ALA   A CB   1 
ATOM   298  N  N    . LYS   A 1 71  ? -12.56239 -42.56312 -33.31816 1.000 188.10667 ? 44  LYS   A N    1 
ATOM   299  C  CA   . LYS   A 1 71  ? -11.57237 -41.64956 -32.76282 1.000 179.92174 ? 44  LYS   A CA   1 
ATOM   300  C  C    . LYS   A 1 71  ? -10.67877 -41.00058 -33.80721 1.000 173.20650 ? 44  LYS   A C    1 
ATOM   301  O  O    . LYS   A 1 71  ? -10.10698 -39.94092 -33.52302 1.000 164.85859 ? 44  LYS   A O    1 
ATOM   302  C  CB   . LYS   A 1 71  ? -10.68271 -42.37568 -31.74140 1.000 174.82795 ? 44  LYS   A CB   1 
ATOM   303  C  CG   . LYS   A 1 71  ? -11.44848 -43.08444 -30.63595 1.000 178.04290 ? 44  LYS   A CG   1 
ATOM   304  C  CD   . LYS   A 1 71  ? -10.50630 -43.81538 -29.69365 1.000 203.45828 ? 44  LYS   A CD   1 
ATOM   305  C  CE   . LYS   A 1 71  ? -11.27387 -44.54166 -28.60144 1.000 194.13013 ? 44  LYS   A CE   1 
ATOM   306  N  NZ   . LYS   A 1 71  ? -10.36290 -45.22930 -27.64542 1.000 208.86781 ? 44  LYS   A NZ   1 
ATOM   307  N  N    . LYS   A 1 72  ? -10.53874 -41.58587 -34.99533 1.000 175.97075 ? 45  LYS   A N    1 
ATOM   308  C  CA   . LYS   A 1 72  ? -9.67927  -41.05431 -36.04437 1.000 161.90728 ? 45  LYS   A CA   1 
ATOM   309  C  C    . LYS   A 1 72  ? -10.45531 -40.60174 -37.27152 1.000 165.26387 ? 45  LYS   A C    1 
ATOM   310  O  O    . LYS   A 1 72  ? -10.30787 -39.45589 -37.70790 1.000 151.58138 ? 45  LYS   A O    1 
ATOM   311  C  CB   . LYS   A 1 72  ? -8.63547  -42.10640 -36.44945 1.000 187.68681 ? 45  LYS   A CB   1 
ATOM   312  C  CG   . LYS   A 1 72  ? -7.74874  -42.57512 -35.30694 1.000 210.89285 ? 45  LYS   A CG   1 
ATOM   313  C  CD   . LYS   A 1 72  ? -6.78461  -43.65779 -35.76252 1.000 189.11652 ? 45  LYS   A CD   1 
ATOM   314  C  CE   . LYS   A 1 72  ? -5.91812  -44.13887 -34.61123 1.000 170.36517 ? 45  LYS   A CE   1 
ATOM   315  N  NZ   . LYS   A 1 72  ? -4.99052  -45.22238 -35.03447 1.000 167.71894 ? 45  LYS   A NZ   1 
ATOM   316  N  N    . TYR   A 1 73  ? -11.28540 -41.47182 -37.84127 1.000 166.67427 ? 46  TYR   A N    1 
ATOM   317  C  CA   . TYR   A 1 73  ? -12.00969 -41.14464 -39.06171 1.000 140.09205 ? 46  TYR   A CA   1 
ATOM   318  C  C    . TYR   A 1 73  ? -13.21574 -42.06493 -39.18466 1.000 144.10695 ? 46  TYR   A C    1 
ATOM   319  O  O    . TYR   A 1 73  ? -13.33385 -43.06937 -38.47842 1.000 154.55855 ? 46  TYR   A O    1 
ATOM   320  C  CB   . TYR   A 1 73  ? -11.10731 -41.26774 -40.29340 1.000 135.95968 ? 46  TYR   A CB   1 
ATOM   321  C  CG   . TYR   A 1 73  ? -10.61470 -42.67597 -40.53813 1.000 147.66025 ? 46  TYR   A CG   1 
ATOM   322  C  CD1  . TYR   A 1 73  ? -9.44235  -43.13444 -39.95210 1.000 173.10821 ? 46  TYR   A CD1  1 
ATOM   323  C  CD2  . TYR   A 1 73  ? -11.32578 -43.54939 -41.35057 1.000 152.14283 ? 46  TYR   A CD2  1 
ATOM   324  C  CE1  . TYR   A 1 73  ? -8.99200  -44.42174 -40.17075 1.000 177.69294 ? 46  TYR   A CE1  1 
ATOM   325  C  CE2  . TYR   A 1 73  ? -10.88483 -44.83661 -41.57295 1.000 148.19349 ? 46  TYR   A CE2  1 
ATOM   326  C  CZ   . TYR   A 1 73  ? -9.71815  -45.26748 -40.98285 1.000 155.37764 ? 46  TYR   A CZ   1 
ATOM   327  O  OH   . TYR   A 1 73  ? -9.28037  -46.55076 -41.20813 1.000 152.99373 ? 46  TYR   A OH   1 
ATOM   328  N  N    . ILE   A 1 74  ? -14.11351 -41.70241 -40.10067 1.000 134.22670 ? 47  ILE   A N    1 
ATOM   329  C  CA   . ILE   A 1 74  ? -15.24326 -42.53938 -40.49550 1.000 129.36867 ? 47  ILE   A CA   1 
ATOM   330  C  C    . ILE   A 1 74  ? -15.36990 -42.42385 -42.00859 1.000 142.19816 ? 47  ILE   A C    1 
ATOM   331  O  O    . ILE   A 1 74  ? -15.76985 -41.37146 -42.51962 1.000 138.71108 ? 47  ILE   A O    1 
ATOM   332  C  CB   . ILE   A 1 74  ? -16.56033 -42.13020 -39.81914 1.000 133.07240 ? 47  ILE   A CB   1 
ATOM   333  C  CG1  . ILE   A 1 74  ? -16.47470 -42.28611 -38.30188 1.000 123.75687 ? 47  ILE   A CG1  1 
ATOM   334  C  CG2  . ILE   A 1 74  ? -17.71862 -42.95018 -40.37148 1.000 135.85646 ? 47  ILE   A CG2  1 
ATOM   335  C  CD1  . ILE   A 1 74  ? -17.73412 -41.85769 -37.58501 1.000 126.87551 ? 47  ILE   A CD1  1 
ATOM   336  N  N    . TYR   A 1 75  ? -15.03091 -43.49162 -42.72498 1.000 139.97843 ? 48  TYR   A N    1 
ATOM   337  C  CA   . TYR   A 1 75  ? -15.13846 -43.52946 -44.17574 1.000 136.39821 ? 48  TYR   A CA   1 
ATOM   338  C  C    . TYR   A 1 75  ? -16.35292 -44.35964 -44.56779 1.000 138.45742 ? 48  TYR   A C    1 
ATOM   339  O  O    . TYR   A 1 75  ? -16.50761 -45.49744 -44.11022 1.000 147.09113 ? 48  TYR   A O    1 
ATOM   340  C  CB   . TYR   A 1 75  ? -13.87124 -44.11186 -44.80271 1.000 142.75444 ? 48  TYR   A CB   1 
ATOM   341  C  CG   . TYR   A 1 75  ? -12.64325 -43.24336 -44.64402 1.000 153.04687 ? 48  TYR   A CG   1 
ATOM   342  C  CD1  . TYR   A 1 75  ? -12.75671 -41.88609 -44.37053 1.000 163.89146 ? 48  TYR   A CD1  1 
ATOM   343  C  CD2  . TYR   A 1 75  ? -11.36949 -43.78045 -44.77502 1.000 157.75329 ? 48  TYR   A CD2  1 
ATOM   344  C  CE1  . TYR   A 1 75  ? -11.63471 -41.08931 -44.22717 1.000 169.89875 ? 48  TYR   A CE1  1 
ATOM   345  C  CE2  . TYR   A 1 75  ? -10.24267 -42.99239 -44.63325 1.000 163.15191 ? 48  TYR   A CE2  1 
ATOM   346  C  CZ   . TYR   A 1 75  ? -10.38071 -41.64839 -44.35974 1.000 167.01458 ? 48  TYR   A CZ   1 
ATOM   347  O  OH   . TYR   A 1 75  ? -9.25951  -40.86298 -44.21927 1.000 176.82992 ? 48  TYR   A OH   1 
ATOM   348  N  N    . ILE   A 1 76  ? -17.20879 -43.78590 -45.41077 1.000 122.07679 ? 49  ILE   A N    1 
ATOM   349  C  CA   . ILE   A 1 76  ? -18.44763 -44.41560 -45.84974 1.000 143.14779 ? 49  ILE   A CA   1 
ATOM   350  C  C    . ILE   A 1 76  ? -18.46986 -44.42148 -47.37120 1.000 155.24586 ? 49  ILE   A C    1 
ATOM   351  O  O    . ILE   A 1 76  ? -18.07112 -43.43929 -48.00707 1.000 145.37205 ? 49  ILE   A O    1 
ATOM   352  C  CB   . ILE   A 1 76  ? -19.68257 -43.67685 -45.29091 1.000 141.46620 ? 49  ILE   A CB   1 
ATOM   353  C  CG1  . ILE   A 1 76  ? -19.59158 -43.55257 -43.76826 1.000 138.65285 ? 49  ILE   A CG1  1 
ATOM   354  C  CG2  . ILE   A 1 76  ? -20.96403 -44.38707 -45.69693 1.000 164.72029 ? 49  ILE   A CG2  1 
ATOM   355  C  CD1  . ILE   A 1 76  ? -20.70250 -42.72812 -43.15844 1.000 142.37864 ? 49  ILE   A CD1  1 
ATOM   356  N  N    . ALA   A 1 77  ? -18.93376 -45.52492 -47.95832 1.000 147.43926 ? 50  ALA   A N    1 
ATOM   357  C  CA   . ALA   A 1 77  ? -19.00329 -45.62618 -49.41064 1.000 121.90172 ? 50  ALA   A CA   1 
ATOM   358  C  C    . ALA   A 1 77  ? -20.28253 -46.33766 -49.82211 1.000 137.81395 ? 50  ALA   A C    1 
ATOM   359  O  O    . ALA   A 1 77  ? -20.55665 -47.44568 -49.35491 1.000 179.86685 ? 50  ALA   A O    1 
ATOM   360  C  CB   . ALA   A 1 77  ? -17.78216 -46.36492 -49.97152 1.000 141.72436 ? 50  ALA   A CB   1 
ATOM   361  N  N    . SER   A 1 78  ? -21.05749 -45.70298 -50.69864 1.000 135.64985 ? 51  SER   A N    1 
ATOM   362  C  CA   . SER   A 1 78  ? -22.26297 -46.30747 -51.24791 1.000 145.30608 ? 51  SER   A CA   1 
ATOM   363  C  C    . SER   A 1 78  ? -22.55822 -45.65229 -52.59009 1.000 145.62660 ? 51  SER   A C    1 
ATOM   364  O  O    . SER   A 1 78  ? -21.79847 -44.80788 -53.07226 1.000 165.93791 ? 51  SER   A O    1 
ATOM   365  C  CB   . SER   A 1 78  ? -23.44796 -46.16948 -50.28577 1.000 136.77658 ? 51  SER   A CB   1 
ATOM   366  O  OG   . SER   A 1 78  ? -23.93725 -44.83956 -50.25761 1.000 115.42735 ? 51  SER   A OG   1 
ATOM   367  N  N    . PHE   A 1 79  ? -23.67494 -46.05123 -53.19785 1.000 128.83079 ? 52  PHE   A N    1 
ATOM   368  C  CA   . PHE   A 1 79  ? -24.07805 -45.45861 -54.47292 1.000 136.46240 ? 52  PHE   A CA   1 
ATOM   369  C  C    . PHE   A 1 79  ? -24.73079 -44.09713 -54.25459 1.000 147.65631 ? 52  PHE   A C    1 
ATOM   370  O  O    . PHE   A 1 79  ? -24.17660 -43.05937 -54.62972 1.000 152.64292 ? 52  PHE   A O    1 
ATOM   371  C  CB   . PHE   A 1 79  ? -25.02058 -46.40632 -55.22103 1.000 148.26271 ? 52  PHE   A CB   1 
ATOM   372  C  CG   . PHE   A 1 79  ? -25.61994 -45.80782 -56.46206 1.000 144.42975 ? 52  PHE   A CG   1 
ATOM   373  C  CD1  . PHE   A 1 79  ? -24.86311 -45.66591 -57.61307 1.000 133.86497 ? 52  PHE   A CD1  1 
ATOM   374  C  CD2  . PHE   A 1 79  ? -26.94148 -45.39138 -56.47913 1.000 166.10521 ? 52  PHE   A CD2  1 
ATOM   375  C  CE1  . PHE   A 1 79  ? -25.41093 -45.11646 -58.75689 1.000 142.16926 ? 52  PHE   A CE1  1 
ATOM   376  C  CE2  . PHE   A 1 79  ? -27.49540 -44.84166 -57.62001 1.000 165.60447 ? 52  PHE   A CE2  1 
ATOM   377  C  CZ   . PHE   A 1 79  ? -26.72887 -44.70440 -58.76034 1.000 163.95352 ? 52  PHE   A CZ   1 
ATOM   378  N  N    . CYS   A 1 80  ? -25.91316 -44.08923 -53.65215 1.000 159.82294 ? 53  CYS   A N    1 
ATOM   379  C  CA   . CYS   A 1 80  ? -26.63249 -42.86362 -53.34771 1.000 157.13079 ? 53  CYS   A CA   1 
ATOM   380  C  C    . CYS   A 1 80  ? -26.47802 -42.52120 -51.87115 1.000 149.11752 ? 53  CYS   A C    1 
ATOM   381  O  O    . CYS   A 1 80  ? -26.16000 -43.37497 -51.03970 1.000 143.04325 ? 53  CYS   A O    1 
ATOM   382  C  CB   . CYS   A 1 80  ? -28.11510 -43.00010 -53.70805 1.000 146.20928 ? 53  CYS   A CB   1 
ATOM   383  S  SG   . CYS   A 1 80  ? -29.05358 -41.45576 -53.62855 1.000 172.03182 ? 53  CYS   A SG   1 
ATOM   384  N  N    . CYS   A 1 81  ? -26.70492 -41.24874 -51.55326 1.000 153.47279 ? 54  CYS   A N    1 
ATOM   385  C  CA   . CYS   A 1 81  ? -26.60644 -40.76300 -50.17942 1.000 147.52251 ? 54  CYS   A CA   1 
ATOM   386  C  C    . CYS   A 1 81  ? -27.80226 -39.86390 -49.90127 1.000 157.78786 ? 54  CYS   A C    1 
ATOM   387  O  O    . CYS   A 1 81  ? -27.88327 -38.75219 -50.43296 1.000 168.19441 ? 54  CYS   A O    1 
ATOM   388  C  CB   . CYS   A 1 81  ? -25.29405 -40.01518 -49.94708 1.000 140.87733 ? 54  CYS   A CB   1 
ATOM   389  S  SG   . CYS   A 1 81  ? -24.97956 -39.59937 -48.21582 1.000 158.11975 ? 54  CYS   A SG   1 
ATOM   390  N  N    . ASN   A 1 82  ? -28.72385 -40.34413 -49.07079 1.000 148.63465 ? 55  ASN   A N    1 
ATOM   391  C  CA   . ASN   A 1 82  ? -29.91631 -39.59237 -48.70373 1.000 144.36347 ? 55  ASN   A CA   1 
ATOM   392  C  C    . ASN   A 1 82  ? -30.45729 -40.12212 -47.38124 1.000 142.27284 ? 55  ASN   A C    1 
ATOM   393  O  O    . ASN   A 1 82  ? -31.48518 -40.81135 -47.36047 1.000 155.70188 ? 55  ASN   A O    1 
ATOM   394  C  CB   . ASN   A 1 82  ? -30.97581 -39.69218 -49.80286 1.000 154.43565 ? 55  ASN   A CB   1 
ATOM   395  C  CG   . ASN   A 1 82  ? -32.11883 -38.71812 -49.60213 1.000 165.29526 ? 55  ASN   A CG   1 
ATOM   396  O  OD1  . ASN   A 1 82  ? -31.95367 -37.66773 -48.98107 1.000 175.33015 ? 55  ASN   A OD1  1 
ATOM   397  N  ND2  . ASN   A 1 82  ? -33.28843 -39.06274 -50.12916 1.000 134.79292 ? 55  ASN   A ND2  1 
ATOM   398  N  N    . PRO   A 1 83  ? -29.79567 -39.82749 -46.25838 1.000 134.57026 ? 56  PRO   A N    1 
ATOM   399  C  CA   . PRO   A 1 83  ? -30.22064 -40.42443 -44.98274 1.000 135.74281 ? 56  PRO   A CA   1 
ATOM   400  C  C    . PRO   A 1 83  ? -31.49337 -39.82275 -44.41582 1.000 148.01198 ? 56  PRO   A C    1 
ATOM   401  O  O    . PRO   A 1 83  ? -32.16948 -40.48942 -43.62253 1.000 169.92861 ? 56  PRO   A O    1 
ATOM   402  C  CB   . PRO   A 1 83  ? -29.02529 -40.16178 -44.05177 1.000 127.97224 ? 56  PRO   A CB   1 
ATOM   403  C  CG   . PRO   A 1 83  ? -27.90457 -39.69038 -44.94686 1.000 125.42256 ? 56  PRO   A CG   1 
ATOM   404  C  CD   . PRO   A 1 83  ? -28.57113 -39.02816 -46.10505 1.000 134.47099 ? 56  PRO   A CD   1 
ATOM   405  N  N    . LEU   A 1 84  ? -31.84902 -38.59652 -44.79814 1.000 133.44373 ? 57  LEU   A N    1 
ATOM   406  C  CA   . LEU   A 1 84  ? -32.96582 -37.89762 -44.17134 1.000 155.81235 ? 57  LEU   A CA   1 
ATOM   407  C  C    . LEU   A 1 84  ? -34.33080 -38.41165 -44.61583 1.000 160.93271 ? 57  LEU   A C    1 
ATOM   408  O  O    . LEU   A 1 84  ? -35.34596 -37.85486 -44.18154 1.000 145.34519 ? 57  LEU   A O    1 
ATOM   409  C  CB   . LEU   A 1 84  ? -32.85899 -36.39862 -44.45590 1.000 141.62200 ? 57  LEU   A CB   1 
ATOM   410  C  CG   . LEU   A 1 84  ? -31.48529 -35.77632 -44.19277 1.000 105.56264 ? 57  LEU   A CG   1 
ATOM   411  C  CD1  . LEU   A 1 84  ? -31.50038 -34.28296 -44.48159 1.000 134.08430 ? 57  LEU   A CD1  1 
ATOM   412  C  CD2  . LEU   A 1 84  ? -31.03093 -36.04553 -42.76591 1.000 120.01458 ? 57  LEU   A CD2  1 
ATOM   413  N  N    . SER   A 1 85  ? -34.38921 -39.45162 -45.45172 1.000 145.35985 ? 58  SER   A N    1 
ATOM   414  C  CA   . SER   A 1 85  ? -35.67306 -39.95674 -45.92562 1.000 145.54428 ? 58  SER   A CA   1 
ATOM   415  C  C    . SER   A 1 85  ? -36.50307 -40.58744 -44.81333 1.000 152.72434 ? 58  SER   A C    1 
ATOM   416  O  O    . SER   A 1 85  ? -37.73295 -40.63302 -44.92599 1.000 166.21533 ? 58  SER   A O    1 
ATOM   417  C  CB   . SER   A 1 85  ? -35.45439 -40.96662 -47.05428 1.000 153.94979 ? 58  SER   A CB   1 
ATOM   418  O  OG   . SER   A 1 85  ? -34.50051 -41.94643 -46.68529 1.000 148.38742 ? 58  SER   A OG   1 
ATOM   419  N  N    . THR   A 1 86  ? -35.86902 -41.07276 -43.74871 1.000 144.33027 ? 59  THR   A N    1 
ATOM   420  C  CA   . THR   A 1 86  ? -36.57171 -41.67245 -42.62273 1.000 156.07667 ? 59  THR   A CA   1 
ATOM   421  C  C    . THR   A 1 86  ? -36.06576 -41.05296 -41.32451 1.000 151.04849 ? 59  THR   A C    1 
ATOM   422  O  O    . THR   A 1 86  ? -35.22745 -40.14634 -41.32503 1.000 138.48439 ? 59  THR   A O    1 
ATOM   423  C  CB   . THR   A 1 86  ? -36.39604 -43.19612 -42.59781 1.000 152.47560 ? 59  THR   A CB   1 
ATOM   424  O  OG1  . THR   A 1 86  ? -35.00690 -43.51675 -42.45693 1.000 132.95281 ? 59  THR   A OG1  1 
ATOM   425  C  CG2  . THR   A 1 86  ? -36.93299 -43.82342 -43.87874 1.000 164.30841 ? 59  THR   A CG2  1 
ATOM   426  N  N    . THR   A 1 87  ? -36.58524 -41.55795 -40.20378 1.000 139.00836 ? 60  THR   A N    1 
ATOM   427  C  CA   . THR   A 1 87  ? -36.21641 -41.02588 -38.89608 1.000 120.60323 ? 60  THR   A CA   1 
ATOM   428  C  C    . THR   A 1 87  ? -34.85361 -41.54365 -38.44793 1.000 143.52170 ? 60  THR   A C    1 
ATOM   429  O  O    . THR   A 1 87  ? -33.97823 -40.75902 -38.06164 1.000 150.50618 ? 60  THR   A O    1 
ATOM   430  C  CB   . THR   A 1 87  ? -37.28816 -41.38467 -37.86357 1.000 120.38574 ? 60  THR   A CB   1 
ATOM   431  O  OG1  . THR   A 1 87  ? -38.57515 -40.97365 -38.34249 1.000 134.72718 ? 60  THR   A OG1  1 
ATOM   432  C  CG2  . THR   A 1 87  ? -37.00189 -40.69806 -36.53540 1.000 123.79667 ? 60  THR   A CG2  1 
ATOM   433  N  N    . ARG   A 1 88  ? -34.66100 -42.86542 -38.49173 1.000 145.98315 ? 61  ARG   A N    1 
ATOM   434  C  CA   . ARG   A 1 88  ? -33.40152 -43.45130 -38.04214 1.000 130.78111 ? 61  ARG   A CA   1 
ATOM   435  C  C    . ARG   A 1 88  ? -32.23265 -42.97892 -38.89837 1.000 136.99782 ? 61  ARG   A C    1 
ATOM   436  O  O    . ARG   A 1 88  ? -31.12470 -42.76600 -38.38895 1.000 144.74542 ? 61  ARG   A O    1 
ATOM   437  C  CB   . ARG   A 1 88  ? -33.49829 -44.97694 -38.06072 1.000 128.38880 ? 61  ARG   A CB   1 
ATOM   438  C  CG   . ARG   A 1 88  ? -34.63925 -45.54626 -37.22914 1.000 143.90377 ? 61  ARG   A CG   1 
ATOM   439  C  CD   . ARG   A 1 88  ? -34.57920 -47.06701 -37.18614 1.000 167.66136 ? 61  ARG   A CD   1 
ATOM   440  N  NE   . ARG   A 1 88  ? -35.77185 -47.65418 -36.58614 1.000 165.48096 ? 61  ARG   A NE   1 
ATOM   441  C  CZ   . ARG   A 1 88  ? -35.92591 -47.88302 -35.28908 1.000 144.41219 ? 61  ARG   A CZ   1 
ATOM   442  N  NH1  . ARG   A 1 88  ? -34.98201 -47.57355 -34.41556 1.000 114.72950 ? 61  ARG   A NH1  1 
ATOM   443  N  NH2  . ARG   A 1 88  ? -37.05626 -48.43543 -34.85756 1.000 155.08658 ? 61  ARG   A NH2  1 
ATOM   444  N  N    . GLY   A 1 89  ? -32.45759 -42.81477 -40.20339 1.000 141.39837 ? 62  GLY   A N    1 
ATOM   445  C  CA   . GLY   A 1 89  ? -31.41177 -42.27751 -41.05731 1.000 140.26675 ? 62  GLY   A CA   1 
ATOM   446  C  C    . GLY   A 1 89  ? -31.02753 -40.86113 -40.67706 1.000 147.67685 ? 62  GLY   A C    1 
ATOM   447  O  O    . GLY   A 1 89  ? -29.84508 -40.50962 -40.66463 1.000 158.78239 ? 62  GLY   A O    1 
ATOM   448  N  N    . ALA   A 1 90  ? -32.02164 -40.03133 -40.34999 1.000 126.62283 ? 63  ALA   A N    1 
ATOM   449  C  CA   . ALA   A 1 90  ? -31.73326 -38.67645 -39.89251 1.000 128.67169 ? 63  ALA   A CA   1 
ATOM   450  C  C    . ALA   A 1 90  ? -30.96849 -38.69082 -38.57480 1.000 141.52382 ? 63  ALA   A C    1 
ATOM   451  O  O    . ALA   A 1 90  ? -30.07706 -37.86195 -38.35933 1.000 150.35871 ? 63  ALA   A O    1 
ATOM   452  C  CB   . ALA   A 1 90  ? -33.03062 -37.88099 -39.75392 1.000 140.50114 ? 63  ALA   A CB   1 
ATOM   453  N  N    . LEU   A 1 91  ? -31.29567 -39.63021 -37.68360 1.000 150.35841 ? 64  LEU   A N    1 
ATOM   454  C  CA   . LEU   A 1 91  ? -30.56279 -39.73322 -36.42355 1.000 147.85619 ? 64  LEU   A CA   1 
ATOM   455  C  C    . LEU   A 1 91  ? -29.10763 -40.12762 -36.65949 1.000 147.16421 ? 64  LEU   A C    1 
ATOM   456  O  O    . LEU   A 1 91  ? -28.19411 -39.57372 -36.03089 1.000 129.84970 ? 64  LEU   A O    1 
ATOM   457  C  CB   . LEU   A 1 91  ? -31.25116 -40.73758 -35.49954 1.000 139.00873 ? 64  LEU   A CB   1 
ATOM   458  C  CG   . LEU   A 1 91  ? -32.71522 -40.44438 -35.16456 1.000 127.68118 ? 64  LEU   A CG   1 
ATOM   459  C  CD1  . LEU   A 1 91  ? -33.31467 -41.56205 -34.32391 1.000 139.96498 ? 64  LEU   A CD1  1 
ATOM   460  C  CD2  . LEU   A 1 91  ? -32.84866 -39.10303 -34.46011 1.000 129.27538 ? 64  LEU   A CD2  1 
ATOM   461  N  N    . ILE   A 1 92  ? -28.87478 -41.08651 -37.55912 1.000 151.00001 ? 65  ILE   A N    1 
ATOM   462  C  CA   . ILE   A 1 92  ? -27.50679 -41.47492 -37.89669 1.000 141.15972 ? 65  ILE   A CA   1 
ATOM   463  C  C    . ILE   A 1 92  ? -26.75829 -40.29932 -38.51302 1.000 143.59546 ? 65  ILE   A C    1 
ATOM   464  O  O    . ILE   A 1 92  ? -25.57868 -40.06554 -38.21522 1.000 148.85811 ? 65  ILE   A O    1 
ATOM   465  C  CB   . ILE   A 1 92  ? -27.51329 -42.69815 -38.83308 1.000 152.03352 ? 65  ILE   A CB   1 
ATOM   466  C  CG1  . ILE   A 1 92  ? -28.08622 -43.91889 -38.11294 1.000 156.67031 ? 65  ILE   A CG1  1 
ATOM   467  C  CG2  . ILE   A 1 92  ? -26.10966 -42.99800 -39.33731 1.000 145.75200 ? 65  ILE   A CG2  1 
ATOM   468  C  CD1  . ILE   A 1 92  ? -27.26653 -44.35843 -36.92331 1.000 141.15330 ? 65  ILE   A CD1  1 
ATOM   469  N  N    . PHE   A 1 93  ? -27.43508 -39.53528 -39.37421 1.000 147.66332 ? 66  PHE   A N    1 
ATOM   470  C  CA   . PHE   A 1 93  ? -26.80257 -38.37652 -39.99531 1.000 146.08916 ? 66  PHE   A CA   1 
ATOM   471  C  C    . PHE   A 1 93  ? -26.45108 -37.31842 -38.95580 1.000 151.79638 ? 66  PHE   A C    1 
ATOM   472  O  O    . PHE   A 1 93  ? -25.40228 -36.67230 -39.04766 1.000 148.05198 ? 66  PHE   A O    1 
ATOM   473  C  CB   . PHE   A 1 93  ? -27.72244 -37.79989 -41.07201 1.000 156.87962 ? 66  PHE   A CB   1 
ATOM   474  C  CG   . PHE   A 1 93  ? -27.01596 -36.93991 -42.08024 1.000 152.94369 ? 66  PHE   A CG   1 
ATOM   475  C  CD1  . PHE   A 1 93  ? -26.04227 -37.47726 -42.90561 1.000 161.36832 ? 66  PHE   A CD1  1 
ATOM   476  C  CD2  . PHE   A 1 93  ? -27.33775 -35.59993 -42.21624 1.000 158.30823 ? 66  PHE   A CD2  1 
ATOM   477  C  CE1  . PHE   A 1 93  ? -25.39317 -36.69216 -43.83918 1.000 163.56436 ? 66  PHE   A CE1  1 
ATOM   478  C  CE2  . PHE   A 1 93  ? -26.69381 -34.80976 -43.14958 1.000 169.25546 ? 66  PHE   A CE2  1 
ATOM   479  C  CZ   . PHE   A 1 93  ? -25.71954 -35.35695 -43.96175 1.000 156.00877 ? 66  PHE   A CZ   1 
ATOM   480  N  N    . ASP   A 1 94  ? -27.30804 -37.13996 -37.94733 1.000 169.04201 ? 67  ASP   A N    1 
ATOM   481  C  CA   . ASP   A 1 94  ? -27.01096 -36.18375 -36.88341 1.000 168.46671 ? 67  ASP   A CA   1 
ATOM   482  C  C    . ASP   A 1 94  ? -25.82697 -36.63950 -36.03839 1.000 165.51486 ? 67  ASP   A C    1 
ATOM   483  O  O    . ASP   A 1 94  ? -24.97747 -35.82332 -35.65629 1.000 175.72923 ? 67  ASP   A O    1 
ATOM   484  C  CB   . ASP   A 1 94  ? -28.24381 -35.97163 -36.00584 1.000 171.41568 ? 67  ASP   A CB   1 
ATOM   485  C  CG   . ASP   A 1 94  ? -29.19664 -34.94446 -36.58054 1.000 193.90353 ? 67  ASP   A CG   1 
ATOM   486  O  OD1  . ASP   A 1 94  ? -28.71855 -33.98537 -37.22210 1.000 191.36416 ? 67  ASP   A OD1  1 
ATOM   487  O  OD2  . ASP   A 1 94  ? -30.42162 -35.09246 -36.38877 1.000 226.10760 ? 67  ASP   A OD2  1 
ATOM   488  N  N    . LYS   A 1 95  ? -25.75881 -37.93560 -35.72435 1.000 144.62128 ? 68  LYS   A N    1 
ATOM   489  C  CA   . LYS   A 1 95  ? -24.60533 -38.44437 -34.98609 1.000 147.85001 ? 68  LYS   A CA   1 
ATOM   490  C  C    . LYS   A 1 95  ? -23.31836 -38.26336 -35.78479 1.000 154.07079 ? 68  LYS   A C    1 
ATOM   491  O  O    . LYS   A 1 95  ? -22.27418 -37.90011 -35.22630 1.000 150.85047 ? 68  LYS   A O    1 
ATOM   492  C  CB   . LYS   A 1 95  ? -24.81584 -39.91372 -34.62144 1.000 162.07629 ? 68  LYS   A CB   1 
ATOM   493  C  CG   . LYS   A 1 95  ? -25.77073 -40.13209 -33.45722 1.000 176.45231 ? 68  LYS   A CG   1 
ATOM   494  C  CD   . LYS   A 1 95  ? -25.22658 -39.51398 -32.17723 1.000 148.37920 ? 68  LYS   A CD   1 
ATOM   495  C  CE   . LYS   A 1 95  ? -26.13565 -39.79633 -30.99022 1.000 177.68598 ? 68  LYS   A CE   1 
ATOM   496  N  NZ   . LYS   A 1 95  ? -27.48560 -39.19040 -31.15715 1.000 165.41735 ? 68  LYS   A NZ   1 
ATOM   497  N  N    . LEU   A 1 96  ? -23.37754 -38.49367 -37.09916 1.000 157.60828 ? 69  LEU   A N    1 
ATOM   498  C  CA   . LEU   A 1 96  ? -22.19885 -38.28601 -37.93601 1.000 148.29548 ? 69  LEU   A CA   1 
ATOM   499  C  C    . LEU   A 1 96  ? -21.82673 -36.80869 -38.00891 1.000 148.72625 ? 69  LEU   A C    1 
ATOM   500  O  O    . LEU   A 1 96  ? -20.64090 -36.46230 -38.06323 1.000 153.94938 ? 69  LEU   A O    1 
ATOM   501  C  CB   . LEU   A 1 96  ? -22.44323 -38.85127 -39.33446 1.000 157.45202 ? 69  LEU   A CB   1 
ATOM   502  C  CG   . LEU   A 1 96  ? -21.21619 -38.99674 -40.23585 1.000 150.78745 ? 69  LEU   A CG   1 
ATOM   503  C  CD1  . LEU   A 1 96  ? -20.21833 -39.97162 -39.62974 1.000 144.68593 ? 69  LEU   A CD1  1 
ATOM   504  C  CD2  . LEU   A 1 96  ? -21.62778 -39.44305 -41.62892 1.000 131.71760 ? 69  LEU   A CD2  1 
ATOM   505  N  N    . LYS   A 1 97  ? -22.82759 -35.92476 -38.00894 1.000 156.81677 ? 70  LYS   A N    1 
ATOM   506  C  CA   . LYS   A 1 97  ? -22.55880 -34.49066 -37.97486 1.000 138.42348 ? 70  LYS   A CA   1 
ATOM   507  C  C    . LYS   A 1 97  ? -21.84646 -34.09661 -36.68839 1.000 165.36110 ? 70  LYS   A C    1 
ATOM   508  O  O    . LYS   A 1 97  ? -20.89045 -33.31206 -36.71231 1.000 186.49474 ? 70  LYS   A O    1 
ATOM   509  C  CB   . LYS   A 1 97  ? -23.86717 -33.71459 -38.12334 1.000 143.39323 ? 70  LYS   A CB   1 
ATOM   510  C  CG   . LYS   A 1 97  ? -23.72991 -32.20770 -37.99021 1.000 159.65111 ? 70  LYS   A CG   1 
ATOM   511  C  CD   . LYS   A 1 97  ? -25.05166 -31.51876 -38.29074 1.000 169.13641 ? 70  LYS   A CD   1 
ATOM   512  C  CE   . LYS   A 1 97  ? -24.96745 -30.01973 -38.06280 1.000 148.99373 ? 70  LYS   A CE   1 
ATOM   513  N  NZ   . LYS   A 1 97  ? -24.85456 -29.68060 -36.61833 1.000 138.04713 ? 70  LYS   A NZ   1 
ATOM   514  N  N    . GLU   A 1 98  ? -22.30277 -34.62996 -35.55299 1.000 172.01044 ? 71  GLU   A N    1 
ATOM   515  C  CA   . GLU   A 1 98  ? -21.62177 -34.36520 -34.28838 1.000 167.35010 ? 71  GLU   A CA   1 
ATOM   516  C  C    . GLU   A 1 98  ? -20.18876 -34.88437 -34.31822 1.000 158.09444 ? 71  GLU   A C    1 
ATOM   517  O  O    . GLU   A 1 98  ? -19.26140 -34.20518 -33.85600 1.000 157.44764 ? 71  GLU   A O    1 
ATOM   518  C  CB   . GLU   A 1 98  ? -22.39666 -34.99335 -33.12996 1.000 165.18442 ? 71  GLU   A CB   1 
ATOM   519  C  CG   . GLU   A 1 98  ? -21.76218 -34.76571 -31.76645 1.000 177.69936 ? 71  GLU   A CG   1 
ATOM   520  C  CD   . GLU   A 1 98  ? -22.55670 -35.39661 -30.64008 1.000 195.18954 ? 71  GLU   A CD   1 
ATOM   521  O  OE1  . GLU   A 1 98  ? -23.59457 -36.03014 -30.92590 1.000 199.09360 ? 71  GLU   A OE1  1 
ATOM   522  O  OE2  . GLU   A 1 98  ? -22.14356 -35.25873 -29.46909 1.000 198.52164 ? 71  GLU   A OE2  1 
ATOM   523  N  N    . ALA   A 1 99  ? -19.98907 -36.08717 -34.86527 1.000 152.45083 ? 72  ALA   A N    1 
ATOM   524  C  CA   . ALA   A 1 99  ? -18.64068 -36.63742 -34.97198 1.000 153.03812 ? 72  ALA   A CA   1 
ATOM   525  C  C    . ALA   A 1 99  ? -17.74161 -35.74385 -35.81929 1.000 169.53574 ? 72  ALA   A C    1 
ATOM   526  O  O    . ALA   A 1 99  ? -16.58428 -35.49676 -35.46030 1.000 173.58690 ? 72  ALA   A O    1 
ATOM   527  C  CB   . ALA   A 1 99  ? -18.69345 -38.05058 -35.55190 1.000 154.18545 ? 72  ALA   A CB   1 
ATOM   528  N  N    . SER   A 1 100 ? -18.25698 -35.24902 -36.94846 1.000 187.87833 ? 73  SER   A N    1 
ATOM   529  C  CA   . SER   A 1 100 ? -17.46959 -34.35623 -37.79411 1.000 154.40474 ? 73  SER   A CA   1 
ATOM   530  C  C    . SER   A 1 100 ? -17.17887 -33.03476 -37.09671 1.000 151.78621 ? 73  SER   A C    1 
ATOM   531  O  O    . SER   A 1 100 ? -16.10765 -32.45097 -37.29784 1.000 181.95134 ? 73  SER   A O    1 
ATOM   532  C  CB   . SER   A 1 100 ? -18.19295 -34.09991 -39.11622 1.000 152.45328 ? 73  SER   A CB   1 
ATOM   533  O  OG   . SER   A 1 100 ? -19.35291 -33.30902 -38.92169 1.000 163.62161 ? 73  SER   A OG   1 
ATOM   534  N  N    . GLU   A 1 101 ? -18.11931 -32.54355 -36.28686 1.000 160.32930 ? 74  GLU   A N    1 
ATOM   535  C  CA   . GLU   A 1 101 ? -17.87968 -31.30855 -35.54902 1.000 171.03654 ? 74  GLU   A CA   1 
ATOM   536  C  C    . GLU   A 1 101 ? -16.82946 -31.49558 -34.46301 1.000 177.92053 ? 74  GLU   A C    1 
ATOM   537  O  O    . GLU   A 1 101 ? -16.09895 -30.55107 -34.14239 1.000 190.38249 ? 74  GLU   A O    1 
ATOM   538  C  CB   . GLU   A 1 101 ? -19.18254 -30.79326 -34.93882 1.000 177.71108 ? 74  GLU   A CB   1 
ATOM   539  C  CG   . GLU   A 1 101 ? -20.18241 -30.27520 -35.95473 1.000 198.46426 ? 74  GLU   A CG   1 
ATOM   540  C  CD   . GLU   A 1 101 ? -21.42477 -29.70260 -35.30481 1.000 188.28217 ? 74  GLU   A CD   1 
ATOM   541  O  OE1  . GLU   A 1 101 ? -21.45083 -29.59623 -34.06058 1.000 180.85545 ? 74  GLU   A OE1  1 
ATOM   542  O  OE2  . GLU   A 1 101 ? -22.37556 -29.35934 -36.03815 1.000 183.10610 ? 74  GLU   A OE2  1 
ATOM   543  N  N    . LYS   A 1 102 ? -16.73596 -32.69555 -33.88647 1.000 178.27913 ? 75  LYS   A N    1 
ATOM   544  C  CA   . LYS   A 1 102 ? -15.75451 -32.92641 -32.83181 1.000 171.27011 ? 75  LYS   A CA   1 
ATOM   545  C  C    . LYS   A 1 102 ? -14.32767 -33.04748 -33.35484 1.000 159.99717 ? 75  LYS   A C    1 
ATOM   546  O  O    . LYS   A 1 102 ? -13.39354 -33.07205 -32.54588 1.000 156.77561 ? 75  LYS   A O    1 
ATOM   547  C  CB   . LYS   A 1 102 ? -16.12179 -34.17950 -32.03555 1.000 155.43417 ? 75  LYS   A CB   1 
ATOM   548  C  CG   . LYS   A 1 102 ? -17.41443 -34.04225 -31.24912 1.000 170.46321 ? 75  LYS   A CG   1 
ATOM   549  C  CD   . LYS   A 1 102 ? -17.37697 -32.82198 -30.34170 1.000 193.42853 ? 75  LYS   A CD   1 
ATOM   550  C  CE   . LYS   A 1 102 ? -18.74853 -32.52736 -29.75607 1.000 182.97170 ? 75  LYS   A CE   1 
ATOM   551  N  NZ   . LYS   A 1 102 ? -19.26446 -33.66417 -28.94605 1.000 185.97115 ? 75  LYS   A NZ   1 
ATOM   552  N  N    . GLY   A 1 103 ? -14.13342 -33.11723 -34.66899 1.000 169.57527 ? 76  GLY   A N    1 
ATOM   553  C  CA   . GLY   A 1 103 ? -12.80492 -33.21454 -35.25263 1.000 162.50306 ? 76  GLY   A CA   1 
ATOM   554  C  C    . GLY   A 1 103 ? -12.53251 -34.49476 -36.01534 1.000 157.36634 ? 76  GLY   A C    1 
ATOM   555  O  O    . GLY   A 1 103 ? -11.41029 -34.66945 -36.51135 1.000 171.12916 ? 76  GLY   A O    1 
ATOM   556  N  N    . ILE   A 1 104 ? -13.49819 -35.39850 -36.13832 1.000 162.39686 ? 77  ILE   A N    1 
ATOM   557  C  CA   . ILE   A 1 104 ? -13.29123 -36.65552 -36.84753 1.000 159.37055 ? 77  ILE   A CA   1 
ATOM   558  C  C    . ILE   A 1 104 ? -13.35842 -36.39642 -38.34638 1.000 159.55622 ? 77  ILE   A C    1 
ATOM   559  O  O    . ILE   A 1 104 ? -14.28961 -35.74568 -38.83569 1.000 167.82981 ? 77  ILE   A O    1 
ATOM   560  C  CB   . ILE   A 1 104 ? -14.33432 -37.69805 -36.41494 1.000 165.85041 ? 77  ILE   A CB   1 
ATOM   561  C  CG1  . ILE   A 1 104 ? -14.34674 -37.83958 -34.89164 1.000 152.53369 ? 77  ILE   A CG1  1 
ATOM   562  C  CG2  . ILE   A 1 104 ? -14.05178 -39.03880 -37.06185 1.000 159.76950 ? 77  ILE   A CG2  1 
ATOM   563  C  CD1  . ILE   A 1 104 ? -13.03180 -38.30969 -34.31175 1.000 160.19059 ? 77  ILE   A CD1  1 
ATOM   564  N  N    . LYS   A 1 105 ? -12.36962 -36.90263 -39.08030 1.000 130.14955 ? 78  LYS   A N    1 
ATOM   565  C  CA   . LYS   A 1 105 ? -12.34176 -36.74131 -40.53064 1.000 147.35252 ? 78  LYS   A CA   1 
ATOM   566  C  C    . LYS   A 1 105 ? -13.39081 -37.65158 -41.15703 1.000 161.91424 ? 78  LYS   A C    1 
ATOM   567  O  O    . LYS   A 1 105 ? -13.24779 -38.87831 -41.14418 1.000 169.12945 ? 78  LYS   A O    1 
ATOM   568  C  CB   . LYS   A 1 105 ? -10.95043 -37.05236 -41.07425 1.000 152.53832 ? 78  LYS   A CB   1 
ATOM   569  C  CG   . LYS   A 1 105 ? -10.78634 -36.74799 -42.55676 1.000 173.29450 ? 78  LYS   A CG   1 
ATOM   570  C  CD   . LYS   A 1 105 ? -9.36202  -37.00199 -43.02756 1.000 179.92801 ? 78  LYS   A CD   1 
ATOM   571  C  CE   . LYS   A 1 105 ? -9.18387  -36.60691 -44.48652 1.000 171.02310 ? 78  LYS   A CE   1 
ATOM   572  N  NZ   . LYS   A 1 105 ? -7.79727  -36.85728 -44.97045 1.000 156.11582 ? 78  LYS   A NZ   1 
ATOM   573  N  N    . ILE   A 1 106 ? -14.44726 -37.05639 -41.70345 1.000 149.67333 ? 79  ILE   A N    1 
ATOM   574  C  CA   . ILE   A 1 106 ? -15.55028 -37.79472 -42.30787 1.000 145.96975 ? 79  ILE   A CA   1 
ATOM   575  C  C    . ILE   A 1 106 ? -15.46791 -37.61692 -43.81689 1.000 157.60306 ? 79  ILE   A C    1 
ATOM   576  O  O    . ILE   A 1 106 ? -15.51369 -36.48737 -44.32030 1.000 178.11655 ? 79  ILE   A O    1 
ATOM   577  C  CB   . ILE   A 1 106 ? -16.91083 -37.32345 -41.77336 1.000 149.65900 ? 79  ILE   A CB   1 
ATOM   578  C  CG1  . ILE   A 1 106 ? -16.88085 -37.22550 -40.24812 1.000 154.95992 ? 79  ILE   A CG1  1 
ATOM   579  C  CG2  . ILE   A 1 106 ? -18.01225 -38.27300 -42.21823 1.000 128.15941 ? 79  ILE   A CG2  1 
ATOM   580  C  CD1  . ILE   A 1 106 ? -16.66239 -38.54441 -39.55649 1.000 131.97157 ? 79  ILE   A CD1  1 
ATOM   581  N  N    . ILE   A 1 107 ? -15.34641 -38.72958 -44.53683 1.000 136.00305 ? 80  ILE   A N    1 
ATOM   582  C  CA   . ILE   A 1 107 ? -15.31381 -38.73389 -45.99405 1.000 139.41244 ? 80  ILE   A CA   1 
ATOM   583  C  C    . ILE   A 1 107 ? -16.38955 -39.68869 -46.48939 1.000 143.43826 ? 80  ILE   A C    1 
ATOM   584  O  O    . ILE   A 1 107 ? -16.41830 -40.85835 -46.09077 1.000 155.97789 ? 80  ILE   A O    1 
ATOM   585  C  CB   . ILE   A 1 107 ? -13.93130 -39.14117 -46.53902 1.000 134.08814 ? 80  ILE   A CB   1 
ATOM   586  C  CG1  . ILE   A 1 107 ? -12.88118 -38.09297 -46.16533 1.000 148.63850 ? 80  ILE   A CG1  1 
ATOM   587  C  CG2  . ILE   A 1 107 ? -13.98550 -39.33259 -48.04736 1.000 143.11312 ? 80  ILE   A CG2  1 
ATOM   588  C  CD1  . ILE   A 1 107 ? -11.50868 -38.37245 -46.73682 1.000 163.49281 ? 80  ILE   A CD1  1 
ATOM   589  N  N    . VAL   A 1 108 ? -17.27127 -39.19155 -47.35253 1.000 128.50318 ? 81  VAL   A N    1 
ATOM   590  C  CA   . VAL   A 1 108 ? -18.39379 -39.96238 -47.87513 1.000 138.24701 ? 81  VAL   A CA   1 
ATOM   591  C  C    . VAL   A 1 108 ? -18.23749 -40.06642 -49.38539 1.000 147.95112 ? 81  VAL   A C    1 
ATOM   592  O  O    . VAL   A 1 108 ? -18.24066 -39.04691 -50.08716 1.000 155.41206 ? 81  VAL   A O    1 
ATOM   593  C  CB   . VAL   A 1 108 ? -19.74285 -39.32629 -47.50594 1.000 135.85166 ? 81  VAL   A CB   1 
ATOM   594  C  CG1  . VAL   A 1 108 ? -20.88876 -40.13224 -48.09612 1.000 132.43282 ? 81  VAL   A CG1  1 
ATOM   595  C  CG2  . VAL   A 1 108 ? -19.88024 -39.21988 -45.99575 1.000 120.96966 ? 81  VAL   A CG2  1 
ATOM   596  N  N    . LEU   A 1 109 ? -18.10386 -41.29344 -49.88295 1.000 138.25829 ? 82  LEU   A N    1 
ATOM   597  C  CA   . LEU   A 1 109 ? -17.97094 -41.55577 -51.31028 1.000 139.23903 ? 82  LEU   A CA   1 
ATOM   598  C  C    . LEU   A 1 109 ? -19.31831 -41.99544 -51.86834 1.000 142.17098 ? 82  LEU   A C    1 
ATOM   599  O  O    . LEU   A 1 109 ? -19.90813 -42.96825 -51.38555 1.000 164.61622 ? 82  LEU   A O    1 
ATOM   600  C  CB   . LEU   A 1 109 ? -16.91383 -42.62631 -51.57959 1.000 140.28496 ? 82  LEU   A CB   1 
ATOM   601  C  CG   . LEU   A 1 109 ? -15.45682 -42.31648 -51.23572 1.000 142.38653 ? 82  LEU   A CG   1 
ATOM   602  C  CD1  . LEU   A 1 109 ? -14.56853 -43.46955 -51.66673 1.000 136.67217 ? 82  LEU   A CD1  1 
ATOM   603  C  CD2  . LEU   A 1 109 ? -15.00201 -41.02342 -51.88506 1.000 136.93539 ? 82  LEU   A CD2  1 
ATOM   604  N  N    . LEU   A 1 110 ? -19.79843 -41.28089 -52.88217 1.000 140.66035 ? 83  LEU   A N    1 
ATOM   605  C  CA   . LEU   A 1 110 ? -21.02418 -41.64108 -53.57627 1.000 148.80289 ? 83  LEU   A CA   1 
ATOM   606  C  C    . LEU   A 1 110 ? -20.81371 -41.44987 -55.06976 1.000 150.96726 ? 83  LEU   A C    1 
ATOM   607  O  O    . LEU   A 1 110 ? -20.03563 -40.59273 -55.49711 1.000 163.39535 ? 83  LEU   A O    1 
ATOM   608  C  CB   . LEU   A 1 110 ? -22.22952 -40.81341 -53.09638 1.000 147.97767 ? 83  LEU   A CB   1 
ATOM   609  C  CG   . LEU   A 1 110 ? -22.27164 -39.30723 -53.37217 1.000 150.14684 ? 83  LEU   A CG   1 
ATOM   610  C  CD1  . LEU   A 1 110 ? -23.69867 -38.79862 -53.25138 1.000 157.20596 ? 83  LEU   A CD1  1 
ATOM   611  C  CD2  . LEU   A 1 110 ? -21.35935 -38.53949 -52.42584 1.000 137.83467 ? 83  LEU   A CD2  1 
ATOM   612  N  N    . ASP   A 1 111 ? -21.50649 -42.26558 -55.85904 1.000 137.84570 ? 84  ASP   A N    1 
ATOM   613  C  CA   . ASP   A 1 111 ? -21.37511 -42.18824 -57.30524 1.000 137.65410 ? 84  ASP   A CA   1 
ATOM   614  C  C    . ASP   A 1 111 ? -21.89488 -40.84968 -57.81570 1.000 146.58510 ? 84  ASP   A C    1 
ATOM   615  O  O    . ASP   A 1 111 ? -22.80323 -40.24639 -57.23771 1.000 160.96833 ? 84  ASP   A O    1 
ATOM   616  C  CB   . ASP   A 1 111 ? -22.12668 -43.34067 -57.97383 1.000 144.67600 ? 84  ASP   A CB   1 
ATOM   617  C  CG   . ASP   A 1 111 ? -21.82920 -43.45151 -59.45970 1.000 153.49439 ? 84  ASP   A CG   1 
ATOM   618  O  OD1  . ASP   A 1 111 ? -22.16459 -42.51584 -60.21610 1.000 166.30324 ? 84  ASP   A OD1  1 
ATOM   619  O  OD2  . ASP   A 1 111 ? -21.24687 -44.47507 -59.87127 1.000 146.51681 ? 84  ASP   A OD2  1 
ATOM   620  N  N    . GLU   A 1 112 ? -21.30335 -40.38806 -58.91971 1.000 136.51695 ? 85  GLU   A N    1 
ATOM   621  C  CA   . GLU   A 1 112 ? -21.68326 -39.10899 -59.50615 1.000 154.24906 ? 85  GLU   A CA   1 
ATOM   622  C  C    . GLU   A 1 112 ? -23.12984 -39.08839 -59.98358 1.000 159.47100 ? 85  GLU   A C    1 
ATOM   623  O  O    . GLU   A 1 112 ? -23.65145 -38.00787 -60.28013 1.000 165.59242 ? 85  GLU   A O    1 
ATOM   624  C  CB   . GLU   A 1 112 ? -20.73896 -38.77252 -60.66296 1.000 162.19109 ? 85  GLU   A CB   1 
ATOM   625  C  CG   . GLU   A 1 112 ? -20.64248 -37.28971 -60.98388 1.000 160.96213 ? 85  GLU   A CG   1 
ATOM   626  C  CD   . GLU   A 1 112 ? -19.53045 -36.98069 -61.96585 1.000 189.12909 ? 85  GLU   A CD   1 
ATOM   627  O  OE1  . GLU   A 1 112 ? -18.88469 -37.93289 -62.45226 1.000 201.02850 ? 85  GLU   A OE1  1 
ATOM   628  O  OE2  . GLU   A 1 112 ? -19.29926 -35.78633 -62.24859 1.000 200.00921 ? 85  GLU   A OE2  1 
ATOM   629  N  N    . ARG   A 1 113 ? -23.78840 -40.24506 -60.06328 1.000 145.36274 ? 86  ARG   A N    1 
ATOM   630  C  CA   . ARG   A 1 113 ? -25.20076 -40.29580 -60.41374 1.000 146.35161 ? 86  ARG   A CA   1 
ATOM   631  C  C    . ARG   A 1 113 ? -26.11449 -40.09365 -59.21228 1.000 154.97508 ? 86  ARG   A C    1 
ATOM   632  O  O    . ARG   A 1 113 ? -27.31560 -39.87171 -59.39923 1.000 169.84334 ? 86  ARG   A O    1 
ATOM   633  C  CB   . ARG   A 1 113 ? -25.52397 -41.62697 -61.09584 1.000 158.68444 ? 86  ARG   A CB   1 
ATOM   634  C  CG   . ARG   A 1 113 ? -24.67986 -41.89431 -62.33069 1.000 164.10185 ? 86  ARG   A CG   1 
ATOM   635  C  CD   . ARG   A 1 113 ? -25.21666 -43.06208 -63.13877 1.000 177.77089 ? 86  ARG   A CD   1 
ATOM   636  N  NE   . ARG   A 1 113 ? -24.40378 -43.31454 -64.32264 1.000 182.51336 ? 86  ARG   A NE   1 
ATOM   637  C  CZ   . ARG   A 1 113 ? -24.71053 -44.18857 -65.27142 1.000 190.36204 ? 86  ARG   A CZ   1 
ATOM   638  N  NH1  . ARG   A 1 113 ? -25.81564 -44.91360 -65.21262 1.000 199.88085 ? 86  ARG   A NH1  1 
ATOM   639  N  NH2  . ARG   A 1 113 ? -23.88907 -44.33696 -66.30682 1.000 182.27379 ? 86  ARG   A NH2  1 
ATOM   640  N  N    . GLY   A 1 114 ? -25.58291 -40.16866 -57.99461 1.000 142.94853 ? 87  GLY   A N    1 
ATOM   641  C  CA   . GLY   A 1 114 ? -26.35124 -39.84060 -56.81033 1.000 157.52756 ? 87  GLY   A CA   1 
ATOM   642  C  C    . GLY   A 1 114 ? -26.09993 -38.41183 -56.37749 1.000 161.03858 ? 87  GLY   A C    1 
ATOM   643  O  O    . GLY   A 1 114 ? -26.16847 -38.08498 -55.18898 1.000 139.66305 ? 87  GLY   A O    1 
ATOM   644  N  N    . LYS   A 1 115 ? -25.81318 -37.54955 -57.35072 1.000 158.22412 ? 88  LYS   A N    1 
ATOM   645  C  CA   . LYS   A 1 115 ? -25.41047 -36.17231 -57.10002 1.000 149.07260 ? 88  LYS   A CA   1 
ATOM   646  C  C    . LYS   A 1 115 ? -26.58728 -35.23660 -56.85053 1.000 165.16444 ? 88  LYS   A C    1 
ATOM   647  O  O    . LYS   A 1 115 ? -26.36515 -34.04794 -56.59466 1.000 156.45879 ? 88  LYS   A O    1 
ATOM   648  C  CB   . LYS   A 1 115 ? -24.58280 -35.66098 -58.28285 1.000 155.36693 ? 88  LYS   A CB   1 
ATOM   649  C  CG   . LYS   A 1 115 ? -23.52084 -34.63687 -57.92568 1.000 182.37891 ? 88  LYS   A CG   1 
ATOM   650  C  CD   . LYS   A 1 115 ? -22.63874 -34.34152 -59.12816 1.000 177.54829 ? 88  LYS   A CD   1 
ATOM   651  C  CE   . LYS   A 1 115 ? -21.50955 -33.38962 -58.77433 1.000 182.48797 ? 88  LYS   A CE   1 
ATOM   652  N  NZ   . LYS   A 1 115 ? -20.60065 -33.16499 -59.93258 1.000 186.13223 ? 88  LYS   A NZ   1 
ATOM   653  N  N    . ARG   A 1 116 ? -27.82444 -35.73452 -56.91607 1.000 178.84690 ? 89  ARG   A N    1 
ATOM   654  C  CA   . ARG   A 1 116 ? -28.98296 -34.87058 -56.70714 1.000 168.30511 ? 89  ARG   A CA   1 
ATOM   655  C  C    . ARG   A 1 116 ? -29.03277 -34.35134 -55.27514 1.000 168.59103 ? 89  ARG   A C    1 
ATOM   656  O  O    . ARG   A 1 116 ? -29.13274 -33.14036 -55.04539 1.000 156.55238 ? 89  ARG   A O    1 
ATOM   657  C  CB   . ARG   A 1 116 ? -30.27009 -35.62238 -57.04867 1.000 168.51079 ? 89  ARG   A CB   1 
ATOM   658  C  CG   . ARG   A 1 116 ? -30.37345 -36.07108 -58.49518 1.000 172.62072 ? 89  ARG   A CG   1 
ATOM   659  C  CD   . ARG   A 1 116 ? -31.70746 -36.75041 -58.75888 1.000 184.06714 ? 89  ARG   A CD   1 
ATOM   660  N  NE   . ARG   A 1 116 ? -31.78268 -37.30309 -60.10562 1.000 211.41063 ? 89  ARG   A NE   1 
ATOM   661  C  CZ   . ARG   A 1 116 ? -31.39200 -38.52683 -60.43433 1.000 221.23136 ? 89  ARG   A CZ   1 
ATOM   662  N  NH1  . ARG   A 1 116 ? -30.89115 -39.35757 -59.53457 1.000 209.77868 ? 89  ARG   A NH1  1 
ATOM   663  N  NH2  . ARG   A 1 116 ? -31.50617 -38.92717 -61.69743 1.000 211.29899 ? 89  ARG   A NH2  1 
ATOM   664  N  N    . ASN   A 1 117 ? -28.96198 -35.25369 -54.29829 1.000 175.26458 ? 90  ASN   A N    1 
ATOM   665  C  CA   . ASN   A 1 117 ? -29.03745 -34.88111 -52.89153 1.000 150.08633 ? 90  ASN   A CA   1 
ATOM   666  C  C    . ASN   A 1 117 ? -27.75305 -34.25090 -52.36862 1.000 161.94428 ? 90  ASN   A C    1 
ATOM   667  O  O    . ASN   A 1 117 ? -27.69739 -33.90294 -51.18386 1.000 180.79028 ? 90  ASN   A O    1 
ATOM   668  C  CB   . ASN   A 1 117 ? -29.38685 -36.10832 -52.04443 1.000 142.95625 ? 90  ASN   A CB   1 
ATOM   669  C  CG   . ASN   A 1 117 ? -30.70517 -36.73968 -52.44815 1.000 190.13468 ? 90  ASN   A CG   1 
ATOM   670  O  OD1  . ASN   A 1 117 ? -30.74014 -37.86109 -52.95564 1.000 207.76615 ? 90  ASN   A OD1  1 
ATOM   671  N  ND2  . ASN   A 1 117 ? -31.79951 -36.02222 -52.22037 1.000 173.82152 ? 90  ASN   A ND2  1 
ATOM   672  N  N    . LEU   A 1 118 ? -26.73254 -34.09093 -53.21633 1.000 172.75361 ? 91  LEU   A N    1 
ATOM   673  C  CA   . LEU   A 1 118 ? -25.44971 -33.56411 -52.75732 1.000 170.48565 ? 91  LEU   A CA   1 
ATOM   674  C  C    . LEU   A 1 118 ? -25.60967 -32.18358 -52.13196 1.000 163.58106 ? 91  LEU   A C    1 
ATOM   675  O  O    . LEU   A 1 118 ? -25.13365 -31.93554 -51.01748 1.000 143.61657 ? 91  LEU   A O    1 
ATOM   676  C  CB   . LEU   A 1 118 ? -24.45779 -33.51809 -53.91987 1.000 162.71988 ? 91  LEU   A CB   1 
ATOM   677  C  CG   . LEU   A 1 118 ? -23.05017 -33.02270 -53.58339 1.000 169.44756 ? 91  LEU   A CG   1 
ATOM   678  C  CD1  . LEU   A 1 118 ? -22.39645 -33.92793 -52.54939 1.000 156.60196 ? 91  LEU   A CD1  1 
ATOM   679  C  CD2  . LEU   A 1 118 ? -22.19735 -32.92952 -54.84048 1.000 184.78126 ? 91  LEU   A CD2  1 
ATOM   680  N  N    . GLY   A 1 119 ? -26.28462 -31.27064 -52.83581 1.000 173.19673 ? 92  GLY   A N    1 
ATOM   681  C  CA   . GLY   A 1 119 ? -26.52921 -29.95144 -52.27788 1.000 179.21350 ? 92  GLY   A CA   1 
ATOM   682  C  C    . GLY   A 1 119 ? -27.32104 -29.99357 -50.98697 1.000 174.36292 ? 92  GLY   A C    1 
ATOM   683  O  O    . GLY   A 1 119 ? -27.22078 -29.08230 -50.16110 1.000 179.11470 ? 92  GLY   A O    1 
ATOM   684  N  N    . GLU   A 1 120 ? -28.11430 -31.04901 -50.79209 1.000 178.00249 ? 93  GLU   A N    1 
ATOM   685  C  CA   . GLU   A 1 120 ? -28.83400 -31.21434 -49.53543 1.000 171.08561 ? 93  GLU   A CA   1 
ATOM   686  C  C    . GLU   A 1 120 ? -27.90483 -31.66488 -48.41489 1.000 168.00904 ? 93  GLU   A C    1 
ATOM   687  O  O    . GLU   A 1 120 ? -28.10650 -31.29019 -47.25364 1.000 148.06114 ? 93  GLU   A O    1 
ATOM   688  C  CB   . GLU   A 1 120 ? -29.97545 -32.21450 -49.72376 1.000 186.12716 ? 93  GLU   A CB   1 
ATOM   689  C  CG   . GLU   A 1 120 ? -30.71081 -32.59005 -48.45159 1.000 176.93300 ? 93  GLU   A CG   1 
ATOM   690  C  CD   . GLU   A 1 120 ? -31.83278 -33.57591 -48.70488 1.000 170.72317 ? 93  GLU   A CD   1 
ATOM   691  O  OE1  . GLU   A 1 120 ? -32.48059 -33.47964 -49.76856 1.000 160.60461 ? 93  GLU   A OE1  1 
ATOM   692  O  OE2  . GLU   A 1 120 ? -32.06232 -34.45241 -47.84489 1.000 149.42113 ? 93  GLU   A OE2  1 
ATOM   693  N  N    . LEU   A 1 121 ? -26.87752 -32.45155 -48.74329 1.000 174.49299 ? 94  LEU   A N    1 
ATOM   694  C  CA   . LEU   A 1 121 ? -25.99525 -32.99339 -47.71459 1.000 149.37282 ? 94  LEU   A CA   1 
ATOM   695  C  C    . LEU   A 1 121 ? -25.04749 -31.92661 -47.18051 1.000 156.49235 ? 94  LEU   A C    1 
ATOM   696  O  O    . LEU   A 1 121 ? -24.97599 -31.69641 -45.96710 1.000 159.26388 ? 94  LEU   A O    1 
ATOM   697  C  CB   . LEU   A 1 121 ? -25.21013 -34.17862 -48.27589 1.000 134.00365 ? 94  LEU   A CB   1 
ATOM   698  C  CG   . LEU   A 1 121 ? -26.03384 -35.35744 -48.79586 1.000 156.03737 ? 94  LEU   A CG   1 
ATOM   699  C  CD1  . LEU   A 1 121 ? -25.15410 -36.31348 -49.58381 1.000 163.08216 ? 94  LEU   A CD1  1 
ATOM   700  C  CD2  . LEU   A 1 121 ? -26.72517 -36.07974 -47.64914 1.000 155.33243 ? 94  LEU   A CD2  1 
ATOM   701  N  N    . GLN   A 1 122 ? -24.31186 -31.26248 -48.07721 1.000 152.32321 ? 95  GLN   A N    1 
ATOM   702  C  CA   . GLN   A 1 122 ? -23.32485 -30.27437 -47.65221 1.000 155.56496 ? 95  GLN   A CA   1 
ATOM   703  C  C    . GLN   A 1 122 ? -23.96500 -29.12596 -46.88389 1.000 169.97086 ? 95  GLN   A C    1 
ATOM   704  O  O    . GLN   A 1 122 ? -23.30098 -28.48475 -46.06126 1.000 165.57473 ? 95  GLN   A O    1 
ATOM   705  C  CB   . GLN   A 1 122 ? -22.56502 -29.73885 -48.86617 1.000 180.52493 ? 95  GLN   A CB   1 
ATOM   706  C  CG   . GLN   A 1 122 ? -21.78972 -30.79737 -49.63413 1.000 182.98060 ? 95  GLN   A CG   1 
ATOM   707  C  CD   . GLN   A 1 122 ? -21.18041 -30.25964 -50.91480 1.000 185.12630 ? 95  GLN   A CD   1 
ATOM   708  O  OE1  . GLN   A 1 122 ? -21.59684 -29.21966 -51.42545 1.000 199.33805 ? 95  GLN   A OE1  1 
ATOM   709  N  NE2  . GLN   A 1 122 ? -20.18657 -30.96701 -51.43980 1.000 164.08064 ? 95  GLN   A NE2  1 
ATOM   710  N  N    . SER   A 1 123 ? -25.24747 -28.85125 -47.13354 1.000 172.42547 ? 96  SER   A N    1 
ATOM   711  C  CA   . SER   A 1 123 ? -25.92579 -27.78371 -46.40738 1.000 167.92952 ? 96  SER   A CA   1 
ATOM   712  C  C    . SER   A 1 123 ? -26.14391 -28.14728 -44.94380 1.000 167.11050 ? 96  SER   A C    1 
ATOM   713  O  O    . SER   A 1 123 ? -26.21629 -27.25542 -44.09054 1.000 162.03547 ? 96  SER   A O    1 
ATOM   714  C  CB   . SER   A 1 123 ? -27.25962 -27.45629 -47.07929 1.000 171.17034 ? 96  SER   A CB   1 
ATOM   715  O  OG   . SER   A 1 123 ? -27.06615 -27.03388 -48.41843 1.000 189.34245 ? 96  SER   A OG   1 
ATOM   716  N  N    . HIS   A 1 124 ? -26.24525 -29.43985 -44.63155 1.000 169.91464 ? 97  HIS   A N    1 
ATOM   717  C  CA   . HIS   A 1 124 ? -26.46656 -29.86774 -43.25571 1.000 174.56405 ? 97  HIS   A CA   1 
ATOM   718  C  C    . HIS   A 1 124 ? -25.17369 -30.21526 -42.53154 1.000 168.63174 ? 97  HIS   A C    1 
ATOM   719  O  O    . HIS   A 1 124 ? -25.08832 -30.03262 -41.31168 1.000 160.98603 ? 97  HIS   A O    1 
ATOM   720  C  CB   . HIS   A 1 124 ? -27.41158 -31.07281 -43.22165 1.000 162.58719 ? 97  HIS   A CB   1 
ATOM   721  C  CG   . HIS   A 1 124 ? -27.98677 -31.35208 -41.86751 1.000 177.84825 ? 97  HIS   A CG   1 
ATOM   722  N  ND1  . HIS   A 1 124 ? -27.52059 -32.36117 -41.05243 1.000 180.64499 ? 97  HIS   A ND1  1 
ATOM   723  C  CD2  . HIS   A 1 124 ? -28.99126 -30.75227 -41.18571 1.000 193.46162 ? 97  HIS   A CD2  1 
ATOM   724  C  CE1  . HIS   A 1 124 ? -28.21352 -32.37157 -39.92759 1.000 181.73253 ? 97  HIS   A CE1  1 
ATOM   725  N  NE2  . HIS   A 1 124 ? -29.11196 -31.40500 -39.98297 1.000 201.28490 ? 97  HIS   A NE2  1 
ATOM   726  N  N    . CYS   A 1 125 ? -24.16687 -30.70960 -43.25028 1.000 164.25433 ? 98  CYS   A N    1 
ATOM   727  C  CA   . CYS   A 1 125 ? -22.87607 -31.07024 -42.66666 1.000 156.45354 ? 98  CYS   A CA   1 
ATOM   728  C  C    . CYS   A 1 125 ? -21.77392 -30.39993 -43.47368 1.000 158.93845 ? 98  CYS   A C    1 
ATOM   729  O  O    . CYS   A 1 125 ? -21.27445 -30.96601 -44.45585 1.000 160.41159 ? 98  CYS   A O    1 
ATOM   730  C  CB   . CYS   A 1 125 ? -22.68615 -32.58424 -42.63280 1.000 165.55203 ? 98  CYS   A CB   1 
ATOM   731  S  SG   . CYS   A 1 125 ? -23.90109 -33.46442 -41.63334 1.000 189.16959 ? 98  CYS   A SG   1 
ATOM   732  N  N    . PRO   A 1 126 ? -21.37054 -29.18570 -43.09181 1.000 162.73630 ? 99  PRO   A N    1 
ATOM   733  C  CA   . PRO   A 1 126 ? -20.27595 -28.52160 -43.81425 1.000 182.54134 ? 99  PRO   A CA   1 
ATOM   734  C  C    . PRO   A 1 126 ? -18.91013 -29.10752 -43.51159 1.000 169.63105 ? 99  PRO   A C    1 
ATOM   735  O  O    . PRO   A 1 126 ? -17.97049 -28.87262 -44.28161 1.000 160.48807 ? 99  PRO   A O    1 
ATOM   736  C  CB   . PRO   A 1 126 ? -20.37596 -27.06863 -43.33672 1.000 184.81623 ? 99  PRO   A CB   1 
ATOM   737  C  CG   . PRO   A 1 126 ? -20.94934 -27.18120 -41.96246 1.000 182.40767 ? 99  PRO   A CG   1 
ATOM   738  C  CD   . PRO   A 1 126 ? -21.90448 -28.34975 -42.00228 1.000 152.64209 ? 99  PRO   A CD   1 
ATOM   739  N  N    . ASP   A 1 127 ? -18.76871 -29.85954 -42.42197 1.000 164.21409 ? 100 ASP   A N    1 
ATOM   740  C  CA   . ASP   A 1 127 ? -17.48940 -30.43847 -42.03922 1.000 172.04669 ? 100 ASP   A CA   1 
ATOM   741  C  C    . ASP   A 1 127 ? -17.27045 -31.83442 -42.60716 1.000 164.65601 ? 100 ASP   A C    1 
ATOM   742  O  O    . ASP   A 1 127 ? -16.15500 -32.35684 -42.50796 1.000 173.94040 ? 100 ASP   A O    1 
ATOM   743  C  CB   . ASP   A 1 127 ? -17.36955 -30.48261 -40.51194 1.000 173.33512 ? 100 ASP   A CB   1 
ATOM   744  C  CG   . ASP   A 1 127 ? -17.58789 -29.12479 -39.87145 1.000 192.42567 ? 100 ASP   A CG   1 
ATOM   745  O  OD1  . ASP   A 1 127 ? -17.18959 -28.10765 -40.47774 1.000 209.01679 ? 100 ASP   A OD1  1 
ATOM   746  O  OD2  . ASP   A 1 127 ? -18.16217 -29.07439 -38.76356 1.000 216.90773 ? 100 ASP   A OD2  1 
ATOM   747  N  N    . ILE   A 1 128 ? -18.29460 -32.44793 -43.19190 1.000 142.75543 ? 101 ILE   A N    1 
ATOM   748  C  CA   . ILE   A 1 128 ? -18.16158 -33.75567 -43.82305 1.000 145.46939 ? 101 ILE   A CA   1 
ATOM   749  C  C    . ILE   A 1 128 ? -17.75050 -33.55707 -45.27502 1.000 157.42343 ? 101 ILE   A C    1 
ATOM   750  O  O    . ILE   A 1 128 ? -18.38635 -32.79418 -46.01249 1.000 162.93086 ? 101 ILE   A O    1 
ATOM   751  C  CB   . ILE   A 1 128 ? -19.47204 -34.55411 -43.72472 1.000 149.42184 ? 101 ILE   A CB   1 
ATOM   752  C  CG1  . ILE   A 1 128 ? -19.79667 -34.87301 -42.26453 1.000 143.34549 ? 101 ILE   A CG1  1 
ATOM   753  C  CG2  . ILE   A 1 128 ? -19.37872 -35.83305 -44.54249 1.000 143.81071 ? 101 ILE   A CG2  1 
ATOM   754  C  CD1  . ILE   A 1 128 ? -21.00516 -35.76595 -42.08838 1.000 154.14685 ? 101 ILE   A CD1  1 
ATOM   755  N  N    . ASN   A 1 129 ? -16.68750 -34.24358 -45.68753 1.000 157.25218 ? 102 ASN   A N    1 
ATOM   756  C  CA   . ASN   A 1 129 ? -16.16183 -34.13008 -47.04383 1.000 161.10661 ? 102 ASN   A CA   1 
ATOM   757  C  C    . ASN   A 1 129 ? -16.87459 -35.14063 -47.93642 1.000 160.81001 ? 102 ASN   A C    1 
ATOM   758  O  O    . ASN   A 1 129 ? -16.62143 -36.34630 -47.84803 1.000 155.46163 ? 102 ASN   A O    1 
ATOM   759  C  CB   . ASN   A 1 129 ? -14.65170 -34.35344 -47.05519 1.000 154.43366 ? 102 ASN   A CB   1 
ATOM   760  C  CG   . ASN   A 1 129 ? -14.03968 -34.12604 -48.42279 1.000 181.29951 ? 102 ASN   A CG   1 
ATOM   761  O  OD1  . ASN   A 1 129 ? -14.60022 -33.41291 -49.25509 1.000 189.60042 ? 102 ASN   A OD1  1 
ATOM   762  N  ND2  . ASN   A 1 129 ? -12.88289 -34.73313 -48.66248 1.000 185.69799 ? 102 ASN   A ND2  1 
ATOM   763  N  N    . PHE   A 1 130 ? -17.76874 -34.65126 -48.79110 1.000 153.35575 ? 103 PHE   A N    1 
ATOM   764  C  CA   . PHE   A 1 130 ? -18.45802 -35.49673 -49.75566 1.000 142.09014 ? 103 PHE   A CA   1 
ATOM   765  C  C    . PHE   A 1 130 ? -17.70893 -35.47723 -51.08116 1.000 154.28730 ? 103 PHE   A C    1 
ATOM   766  O  O    . PHE   A 1 130 ? -17.28320 -34.41857 -51.55192 1.000 173.50579 ? 103 PHE   A O    1 
ATOM   767  C  CB   . PHE   A 1 130 ? -19.90170 -35.03138 -49.95944 1.000 149.94600 ? 103 PHE   A CB   1 
ATOM   768  C  CG   . PHE   A 1 130 ? -20.74127 -35.08595 -48.71303 1.000 157.40618 ? 103 PHE   A CG   1 
ATOM   769  C  CD1  . PHE   A 1 130 ? -21.46793 -36.22305 -48.39706 1.000 151.09366 ? 103 PHE   A CD1  1 
ATOM   770  C  CD2  . PHE   A 1 130 ? -20.80989 -33.99593 -47.86148 1.000 155.35079 ? 103 PHE   A CD2  1 
ATOM   771  C  CE1  . PHE   A 1 130 ? -22.24297 -36.27252 -47.25230 1.000 137.07009 ? 103 PHE   A CE1  1 
ATOM   772  C  CE2  . PHE   A 1 130 ? -21.58250 -34.03905 -46.71662 1.000 144.88741 ? 103 PHE   A CE2  1 
ATOM   773  C  CZ   . PHE   A 1 130 ? -22.30022 -35.17854 -46.41176 1.000 137.45408 ? 103 PHE   A CZ   1 
ATOM   774  N  N    . ILE   A 1 131 ? -17.54821 -36.65578 -51.67906 1.000 145.58354 ? 104 ILE   A N    1 
ATOM   775  C  CA   . ILE   A 1 131 ? -16.76512 -36.82241 -52.89757 1.000 154.87645 ? 104 ILE   A CA   1 
ATOM   776  C  C    . ILE   A 1 131 ? -17.58074 -37.62255 -53.90280 1.000 154.28343 ? 104 ILE   A C    1 
ATOM   777  O  O    . ILE   A 1 131 ? -18.06932 -38.71284 -53.58557 1.000 151.71062 ? 104 ILE   A O    1 
ATOM   778  C  CB   . ILE   A 1 131 ? -15.41973 -37.52046 -52.61930 1.000 136.43335 ? 104 ILE   A CB   1 
ATOM   779  C  CG1  . ILE   A 1 131 ? -14.53059 -36.64274 -51.73615 1.000 148.67457 ? 104 ILE   A CG1  1 
ATOM   780  C  CG2  . ILE   A 1 131 ? -14.71443 -37.86677 -53.92211 1.000 154.63352 ? 104 ILE   A CG2  1 
ATOM   781  C  CD1  . ILE   A 1 131 ? -13.19782 -37.27135 -51.39518 1.000 132.86389 ? 104 ILE   A CD1  1 
ATOM   782  N  N    . THR   A 1 132 ? -17.72261 -37.08271 -55.11154 1.000 154.88272 ? 105 THR   A N    1 
ATOM   783  C  CA   . THR   A 1 132 ? -18.38451 -37.77988 -56.20572 1.000 145.39001 ? 105 THR   A CA   1 
ATOM   784  C  C    . THR   A 1 132 ? -17.37205 -38.65773 -56.93026 1.000 156.68540 ? 105 THR   A C    1 
ATOM   785  O  O    . THR   A 1 132 ? -16.28754 -38.19312 -57.29606 1.000 166.83862 ? 105 THR   A O    1 
ATOM   786  C  CB   . THR   A 1 132 ? -19.01779 -36.78621 -57.18052 1.000 160.38818 ? 105 THR   A CB   1 
ATOM   787  O  OG1  . THR   A 1 132 ? -18.00592 -35.91729 -57.70541 1.000 183.55842 ? 105 THR   A OG1  1 
ATOM   788  C  CG2  . THR   A 1 132 ? -20.07683 -35.95298 -56.47611 1.000 150.07574 ? 105 THR   A CG2  1 
ATOM   789  N  N    . VAL   A 1 133 ? -17.72869 -39.92277 -57.13624 1.000 153.92728 ? 106 VAL   A N    1 
ATOM   790  C  CA   . VAL   A 1 133 ? -16.82994 -40.91774 -57.70850 1.000 150.99304 ? 106 VAL   A CA   1 
ATOM   791  C  C    . VAL   A 1 133 ? -17.43557 -41.43632 -59.00490 1.000 154.83978 ? 106 VAL   A C    1 
ATOM   792  O  O    . VAL   A 1 133 ? -18.62801 -41.75992 -59.05391 1.000 162.95217 ? 106 VAL   A O    1 
ATOM   793  C  CB   . VAL   A 1 133 ? -16.57073 -42.07520 -56.72609 1.000 146.96207 ? 106 VAL   A CB   1 
ATOM   794  C  CG1  . VAL   A 1 133 ? -15.61192 -43.08645 -57.33144 1.000 150.79555 ? 106 VAL   A CG1  1 
ATOM   795  C  CG2  . VAL   A 1 133 ? -16.02975 -41.54315 -55.40747 1.000 152.47388 ? 106 VAL   A CG2  1 
ATOM   796  N  N    . ASN   A 1 134 ? -16.61289 -41.51127 -60.05181 1.000 154.43590 ? 107 ASN   A N    1 
ATOM   797  C  CA   . ASN   A 1 134 ? -16.99238 -42.10060 -61.33687 1.000 164.90513 ? 107 ASN   A CA   1 
ATOM   798  C  C    . ASN   A 1 134 ? -15.88141 -43.07883 -61.70940 1.000 162.34902 ? 107 ASN   A C    1 
ATOM   799  O  O    . ASN   A 1 134 ? -14.90299 -42.70437 -62.36142 1.000 150.38548 ? 107 ASN   A O    1 
ATOM   800  C  CB   . ASN   A 1 134 ? -17.20059 -41.02897 -62.40520 1.000 162.67376 ? 107 ASN   A CB   1 
ATOM   801  C  CG   . ASN   A 1 134 ? -17.81029 -41.58436 -63.67952 1.000 170.06592 ? 107 ASN   A CG   1 
ATOM   802  O  OD1  . ASN   A 1 134 ? -18.15977 -42.76274 -63.75343 1.000 163.18364 ? 107 ASN   A OD1  1 
ATOM   803  N  ND2  . ASN   A 1 134 ? -17.95308 -40.73088 -64.68730 1.000 164.86411 ? 107 ASN   A ND2  1 
ATOM   804  N  N    . ILE   A 1 135 ? -16.03825 -44.33647 -61.28680 1.000 169.36589 ? 108 ILE   A N    1 
ATOM   805  C  CA   . ILE   A 1 135 ? -14.99671 -45.33611 -61.49040 1.000 153.74537 ? 108 ILE   A CA   1 
ATOM   806  C  C    . ILE   A 1 135 ? -14.82727 -45.70007 -62.95808 1.000 150.66348 ? 108 ILE   A C    1 
ATOM   807  O  O    . ILE   A 1 135 ? -13.80700 -46.29105 -63.33099 1.000 161.05302 ? 108 ILE   A O    1 
ATOM   808  C  CB   . ILE   A 1 135 ? -15.29834 -46.59914 -60.66398 1.000 132.94448 ? 108 ILE   A CB   1 
ATOM   809  C  CG1  . ILE   A 1 135 ? -16.62331 -47.21745 -61.11117 1.000 131.87402 ? 108 ILE   A CG1  1 
ATOM   810  C  CG2  . ILE   A 1 135 ? -15.33339 -46.27034 -59.17979 1.000 148.25492 ? 108 ILE   A CG2  1 
ATOM   811  C  CD1  . ILE   A 1 135 ? -16.96725 -48.49871 -60.39756 1.000 145.63516 ? 108 ILE   A CD1  1 
ATOM   812  N  N    . ASP   A 1 136 ? -15.79951 -45.36957 -63.80492 1.000 138.90315 ? 109 ASP   A N    1 
ATOM   813  C  CA   . ASP   A 1 136 ? -15.74803 -45.69476 -65.22883 1.000 152.95502 ? 109 ASP   A CA   1 
ATOM   814  C  C    . ASP   A 1 136 ? -16.13370 -44.44744 -66.01697 1.000 162.62039 ? 109 ASP   A C    1 
ATOM   815  O  O    . ASP   A 1 136 ? -17.32003 -44.13839 -66.16134 1.000 155.31906 ? 109 ASP   A O    1 
ATOM   816  C  CB   . ASP   A 1 136 ? -16.66767 -46.86668 -65.55861 1.000 148.02684 ? 109 ASP   A CB   1 
ATOM   817  C  CG   . ASP   A 1 136 ? -16.54757 -47.31990 -67.00360 1.000 150.47475 ? 109 ASP   A CG   1 
ATOM   818  O  OD1  . ASP   A 1 136 ? -15.61623 -46.86681 -67.70234 1.000 162.33724 ? 109 ASP   A OD1  1 
ATOM   819  O  OD2  . ASP   A 1 136 ? -17.38959 -48.13240 -67.44109 1.000 146.53745 ? 109 ASP   A OD2  1 
ATOM   820  N  N    . LYS   A 1 137 ? -15.13087 -43.73078 -66.51855 1.000 165.06063 ? 110 LYS   A N    1 
ATOM   821  C  CA   . LYS   A 1 137 ? -15.34839 -42.61425 -67.42615 1.000 171.62116 ? 110 LYS   A CA   1 
ATOM   822  C  C    . LYS   A 1 137 ? -15.05029 -42.97642 -68.87335 1.000 174.34933 ? 110 LYS   A C    1 
ATOM   823  O  O    . LYS   A 1 137 ? -15.26207 -42.14733 -69.76374 1.000 189.02209 ? 110 LYS   A O    1 
ATOM   824  C  CB   . LYS   A 1 137 ? -14.49923 -41.41093 -67.00501 1.000 187.87478 ? 110 LYS   A CB   1 
ATOM   825  C  CG   . LYS   A 1 137 ? -14.83992 -40.87265 -65.62722 1.000 190.06870 ? 110 LYS   A CG   1 
ATOM   826  C  CD   . LYS   A 1 137 ? -14.27504 -39.47968 -65.42032 1.000 192.11425 ? 110 LYS   A CD   1 
ATOM   827  C  CE   . LYS   A 1 137 ? -14.68915 -38.91368 -64.07375 1.000 178.26950 ? 110 LYS   A CE   1 
ATOM   828  N  NZ   . LYS   A 1 137 ? -14.16917 -37.53473 -63.87700 1.000 178.33332 ? 110 LYS   A NZ   1 
ATOM   829  N  N    . LYS   A 1 138 ? -14.56096 -44.19191 -69.12583 1.000 158.35358 ? 111 LYS   A N    1 
ATOM   830  C  CA   . LYS   A 1 138 ? -14.34262 -44.63823 -70.49718 1.000 175.82155 ? 111 LYS   A CA   1 
ATOM   831  C  C    . LYS   A 1 138 ? -15.66761 -44.84419 -71.22067 1.000 183.65941 ? 111 LYS   A C    1 
ATOM   832  O  O    . LYS   A 1 138 ? -15.84990 -44.37825 -72.35164 1.000 187.55093 ? 111 LYS   A O    1 
ATOM   833  C  CB   . LYS   A 1 138 ? -13.51900 -45.92647 -70.49992 1.000 177.45688 ? 111 LYS   A CB   1 
ATOM   834  C  CG   . LYS   A 1 138 ? -13.37780 -46.57529 -71.86629 1.000 197.00622 ? 111 LYS   A CG   1 
ATOM   835  C  CD   . LYS   A 1 138 ? -12.68925 -47.92671 -71.76250 1.000 178.62400 ? 111 LYS   A CD   1 
ATOM   836  C  CE   . LYS   A 1 138 ? -12.55517 -48.58532 -73.12554 1.000 169.45683 ? 111 LYS   A CE   1 
ATOM   837  N  NZ   . LYS   A 1 138 ? -11.71453 -47.77892 -74.05290 1.000 207.66068 ? 111 LYS   A NZ   1 
ATOM   838  N  N    . ASN   A 1 139 ? -16.60757 -45.53873 -70.57994 1.000 172.67555 ? 112 ASN   A N    1 
ATOM   839  C  CA   . ASN   A 1 139 ? -17.91582 -45.79829 -71.16064 1.000 167.78895 ? 112 ASN   A CA   1 
ATOM   840  C  C    . ASN   A 1 139 ? -19.06466 -45.33723 -70.27544 1.000 167.48100 ? 112 ASN   A C    1 
ATOM   841  O  O    . ASN   A 1 139 ? -20.22512 -45.45398 -70.68745 1.000 164.47891 ? 112 ASN   A O    1 
ATOM   842  C  CB   . ASN   A 1 139 ? -18.07444 -47.29424 -71.46657 1.000 174.02527 ? 112 ASN   A CB   1 
ATOM   843  C  CG   . ASN   A 1 139 ? -16.95601 -47.83216 -72.33744 1.000 187.59493 ? 112 ASN   A CG   1 
ATOM   844  O  OD1  . ASN   A 1 139 ? -16.19492 -48.70540 -71.92086 1.000 196.47554 ? 112 ASN   A OD1  1 
ATOM   845  N  ND2  . ASN   A 1 139 ? -16.84982 -47.31061 -73.55430 1.000 183.21229 ? 112 ASN   A ND2  1 
ATOM   846  N  N    . ASN   A 1 140 ? -18.77660 -44.82081 -69.07770 1.000 165.72175 ? 113 ASN   A N    1 
ATOM   847  C  CA   . ASN   A 1 140 ? -19.79843 -44.32243 -68.15373 1.000 162.19458 ? 113 ASN   A CA   1 
ATOM   848  C  C    . ASN   A 1 140 ? -20.81697 -45.40715 -67.80936 1.000 164.80220 ? 113 ASN   A C    1 
ATOM   849  O  O    . ASN   A 1 140 ? -22.02628 -45.16827 -67.79118 1.000 181.06481 ? 113 ASN   A O    1 
ATOM   850  C  CB   . ASN   A 1 140 ? -20.49068 -43.07659 -68.71260 1.000 157.57552 ? 113 ASN   A CB   1 
ATOM   851  C  CG   . ASN   A 1 140 ? -19.52963 -41.92025 -68.92022 1.000 186.55360 ? 113 ASN   A CG   1 
ATOM   852  O  OD1  . ASN   A 1 140 ? -18.95801 -41.75829 -69.99851 1.000 211.57225 ? 113 ASN   A OD1  1 
ATOM   853  N  ND2  . ASN   A 1 140 ? -19.34545 -41.11038 -67.88379 1.000 171.51170 ? 113 ASN   A ND2  1 
ATOM   854  N  N    . VAL   A 1 141 ? -20.32231 -46.61090 -67.52964 1.000 151.81391 ? 114 VAL   A N    1 
ATOM   855  C  CA   . VAL   A 1 141 ? -21.16255 -47.74116 -67.17043 1.000 148.19932 ? 114 VAL   A CA   1 
ATOM   856  C  C    . VAL   A 1 141 ? -20.91785 -48.19233 -65.73470 1.000 147.16977 ? 114 VAL   A C    1 
ATOM   857  O  O    . VAL   A 1 141 ? -21.86274 -48.51837 -65.01548 1.000 161.52392 ? 114 VAL   A O    1 
ATOM   858  C  CB   . VAL   A 1 141 ? -20.95780 -48.91311 -68.15516 1.000 145.29035 ? 114 VAL   A CB   1 
ATOM   859  C  CG1  . VAL   A 1 141 ? -21.95097 -50.03019 -67.86793 1.000 140.82812 ? 114 VAL   A CG1  1 
ATOM   860  C  CG2  . VAL   A 1 141 ? -21.08662 -48.43079 -69.59047 1.000 156.79358 ? 114 VAL   A CG2  1 
ATOM   861  N  N    . GLY   A 1 142 ? -19.65880 -48.21590 -65.30454 1.000 148.51057 ? 115 GLY   A N    1 
ATOM   862  C  CA   . GLY   A 1 142 ? -19.35290 -48.66719 -63.95871 1.000 152.35836 ? 115 GLY   A CA   1 
ATOM   863  C  C    . GLY   A 1 142 ? -19.89146 -47.71006 -62.90980 1.000 141.32071 ? 115 GLY   A C    1 
ATOM   864  O  O    . GLY   A 1 142 ? -19.79468 -46.48859 -63.03935 1.000 147.95084 ? 115 GLY   A O    1 
ATOM   865  N  N    . LEU   A 1 143 ? -20.46849 -48.28123 -61.85623 1.000 120.65092 ? 116 LEU   A N    1 
ATOM   866  C  CA   . LEU   A 1 143 ? -21.05167 -47.51655 -60.76625 1.000 142.66739 ? 116 LEU   A CA   1 
ATOM   867  C  C    . LEU   A 1 143 ? -20.41249 -47.92347 -59.44540 1.000 158.63807 ? 116 LEU   A C    1 
ATOM   868  O  O    . LEU   A 1 143 ? -20.00807 -49.07506 -59.26085 1.000 165.74276 ? 116 LEU   A O    1 
ATOM   869  C  CB   . LEU   A 1 143 ? -22.57205 -47.71677 -60.69982 1.000 129.25725 ? 116 LEU   A CB   1 
ATOM   870  C  CG   . LEU   A 1 143 ? -23.35024 -47.29406 -61.94801 1.000 129.30860 ? 116 LEU   A CG   1 
ATOM   871  C  CD1  . LEU   A 1 143 ? -24.84924 -47.45884 -61.74107 1.000 146.47668 ? 116 LEU   A CD1  1 
ATOM   872  C  CD2  . LEU   A 1 143 ? -23.01027 -45.86203 -62.32934 1.000 152.64817 ? 116 LEU   A CD2  1 
ATOM   873  N  N    . LEU   A 1 144 ? -20.32256 -46.96459 -58.52626 1.000 149.57961 ? 117 LEU   A N    1 
ATOM   874  C  CA   . LEU   A 1 144 ? -19.72584 -47.20568 -57.21607 1.000 132.72738 ? 117 LEU   A CA   1 
ATOM   875  C  C    . LEU   A 1 144 ? -20.76382 -47.84739 -56.30218 1.000 145.57572 ? 117 LEU   A C    1 
ATOM   876  O  O    . LEU   A 1 144 ? -21.71788 -47.18935 -55.87533 1.000 146.04071 ? 117 LEU   A O    1 
ATOM   877  C  CB   . LEU   A 1 144 ? -19.20108 -45.90339 -56.61785 1.000 132.61572 ? 117 LEU   A CB   1 
ATOM   878  C  CG   . LEU   A 1 144 ? -18.62573 -46.02558 -55.20461 1.000 138.18285 ? 117 LEU   A CG   1 
ATOM   879  C  CD1  . LEU   A 1 144 ? -17.47508 -47.02030 -55.18016 1.000 150.65164 ? 117 LEU   A CD1  1 
ATOM   880  C  CD2  . LEU   A 1 144 ? -18.18116 -44.67100 -54.67328 1.000 148.85707 ? 117 LEU   A CD2  1 
ATOM   881  N  N    . LEU   A 1 145 ? -20.58105 -49.13270 -55.99965 1.000 168.15673 ? 118 LEU   A N    1 
ATOM   882  C  CA   . LEU   A 1 145 ? -21.46860 -49.83341 -55.07912 1.000 156.16491 ? 118 LEU   A CA   1 
ATOM   883  C  C    . LEU   A 1 145 ? -20.69121 -50.35281 -53.87728 1.000 164.94066 ? 118 LEU   A C    1 
ATOM   884  O  O    . LEU   A 1 145 ? -20.81992 -51.52468 -53.50893 1.000 185.28793 ? 118 LEU   A O    1 
ATOM   885  C  CB   . LEU   A 1 145 ? -22.18659 -50.98984 -55.78178 1.000 136.00087 ? 118 LEU   A CB   1 
ATOM   886  C  CG   . LEU   A 1 145 ? -23.49566 -50.69607 -56.52015 1.000 131.74323 ? 118 LEU   A CG   1 
ATOM   887  C  CD1  . LEU   A 1 145 ? -23.25903 -49.83512 -57.75027 1.000 142.22893 ? 118 LEU   A CD1  1 
ATOM   888  C  CD2  . LEU   A 1 145 ? -24.19416 -51.99375 -56.89819 1.000 141.00283 ? 118 LEU   A CD2  1 
ATOM   889  N  N    . GLY   A 1 146 ? -19.88179 -49.49208 -53.26457 1.000 135.29532 ? 119 GLY   A N    1 
ATOM   890  C  CA   . GLY   A 1 146 ? -19.12630 -49.87390 -52.08802 1.000 143.93561 ? 119 GLY   A CA   1 
ATOM   891  C  C    . GLY   A 1 146 ? -20.01001 -50.37718 -50.96644 1.000 164.99949 ? 119 GLY   A C    1 
ATOM   892  O  O    . GLY   A 1 146 ? -19.93561 -51.55155 -50.59082 1.000 145.86420 ? 119 GLY   A O    1 
ATOM   893  N  N    . CYS   A 1 147 ? -20.84738 -49.49098 -50.42476 1.000 179.47539 ? 120 CYS   A N    1 
ATOM   894  C  CA   . CYS   A 1 147 ? -21.84301 -49.85378 -49.41718 1.000 167.31519 ? 120 CYS   A CA   1 
ATOM   895  C  C    . CYS   A 1 147 ? -21.18170 -50.44617 -48.17094 1.000 177.17652 ? 120 CYS   A C    1 
ATOM   896  O  O    . CYS   A 1 147 ? -21.54320 -51.52685 -47.70102 1.000 172.19748 ? 120 CYS   A O    1 
ATOM   897  C  CB   . CYS   A 1 147 ? -22.87655 -50.81710 -50.00812 1.000 142.95765 ? 120 CYS   A CB   1 
ATOM   898  S  SG   . CYS   A 1 147 ? -24.43268 -50.91656 -49.11017 1.000 194.09142 ? 120 CYS   A SG   1 
ATOM   899  N  N    . PHE   A 1 148 ? -20.19903 -49.72431 -47.63209 1.000 149.54395 ? 121 PHE   A N    1 
ATOM   900  C  CA   . PHE   A 1 148 ? -19.48286 -50.18420 -46.45168 1.000 122.94356 ? 121 PHE   A CA   1 
ATOM   901  C  C    . PHE   A 1 148 ? -18.93300 -48.99167 -45.68059 1.000 127.52675 ? 121 PHE   A C    1 
ATOM   902  O  O    . PHE   A 1 148 ? -18.74171 -47.89817 -46.22484 1.000 144.09118 ? 121 PHE   A O    1 
ATOM   903  C  CB   . PHE   A 1 148 ? -18.35182 -51.15692 -46.81903 1.000 137.14352 ? 121 PHE   A CB   1 
ATOM   904  C  CG   . PHE   A 1 148 ? -17.25669 -50.54102 -47.64412 1.000 155.93607 ? 121 PHE   A CG   1 
ATOM   905  C  CD1  . PHE   A 1 148 ? -17.35671 -50.49168 -49.02246 1.000 154.63019 ? 121 PHE   A CD1  1 
ATOM   906  C  CD2  . PHE   A 1 148 ? -16.12075 -50.02454 -47.04239 1.000 147.73883 ? 121 PHE   A CD2  1 
ATOM   907  C  CE1  . PHE   A 1 148 ? -16.35166 -49.93265 -49.78674 1.000 137.44460 ? 121 PHE   A CE1  1 
ATOM   908  C  CE2  . PHE   A 1 148 ? -15.11033 -49.46381 -47.80164 1.000 143.38313 ? 121 PHE   A CE2  1 
ATOM   909  C  CZ   . PHE   A 1 148 ? -15.22715 -49.41791 -49.17600 1.000 146.48538 ? 121 PHE   A CZ   1 
ATOM   910  N  N    . TRP   A 1 149 ? -18.68517 -49.22784 -44.39340 1.000 127.29913 ? 122 TRP   A N    1 
ATOM   911  C  CA   . TRP   A 1 149 ? -18.10912 -48.25272 -43.48120 1.000 135.12494 ? 122 TRP   A CA   1 
ATOM   912  C  C    . TRP   A 1 149 ? -16.82702 -48.81208 -42.88034 1.000 143.57926 ? 122 TRP   A C    1 
ATOM   913  O  O    . TRP   A 1 149 ? -16.72190 -50.01450 -42.61995 1.000 152.58104 ? 122 TRP   A O    1 
ATOM   914  C  CB   . TRP   A 1 149 ? -19.06391 -47.90330 -42.32970 1.000 122.15036 ? 122 TRP   A CB   1 
ATOM   915  C  CG   . TRP   A 1 149 ? -20.37603 -47.28517 -42.70714 1.000 139.68463 ? 122 TRP   A CG   1 
ATOM   916  C  CD1  . TRP   A 1 149 ? -21.10897 -47.51022 -43.83699 1.000 135.30197 ? 122 TRP   A CD1  1 
ATOM   917  C  CD2  . TRP   A 1 149 ? -21.11646 -46.33779 -41.93128 1.000 149.84283 ? 122 TRP   A CD2  1 
ATOM   918  N  NE1  . TRP   A 1 149 ? -22.26012 -46.75911 -43.81090 1.000 135.18116 ? 122 TRP   A NE1  1 
ATOM   919  C  CE2  . TRP   A 1 149 ? -22.28640 -46.02874 -42.65172 1.000 146.49930 ? 122 TRP   A CE2  1 
ATOM   920  C  CE3  . TRP   A 1 149 ? -20.90053 -45.71846 -40.69619 1.000 137.80830 ? 122 TRP   A CE3  1 
ATOM   921  C  CZ2  . TRP   A 1 149 ? -23.23732 -45.12769 -42.17770 1.000 141.50895 ? 122 TRP   A CZ2  1 
ATOM   922  C  CZ3  . TRP   A 1 149 ? -21.84358 -44.82581 -40.22780 1.000 133.79052 ? 122 TRP   A CZ3  1 
ATOM   923  C  CH2  . TRP   A 1 149 ? -22.99797 -44.53828 -40.96632 1.000 142.84597 ? 122 TRP   A CH2  1 
ATOM   924  N  N    . VAL   A 1 150 ? -15.86792 -47.92472 -42.62702 1.000 138.64456 ? 123 VAL   A N    1 
ATOM   925  C  CA   . VAL   A 1 150 ? -14.62638 -48.28556 -41.94849 1.000 142.11967 ? 123 VAL   A CA   1 
ATOM   926  C  C    . VAL   A 1 150 ? -14.21015 -47.13210 -41.04205 1.000 152.58202 ? 123 VAL   A C    1 
ATOM   927  O  O    . VAL   A 1 150 ? -14.25856 -45.96371 -41.44065 1.000 136.09733 ? 123 VAL   A O    1 
ATOM   928  C  CB   . VAL   A 1 150 ? -13.51256 -48.64740 -42.95625 1.000 139.27087 ? 123 VAL   A CB   1 
ATOM   929  C  CG1  . VAL   A 1 150 ? -13.37828 -47.57348 -44.02188 1.000 143.28951 ? 123 VAL   A CG1  1 
ATOM   930  C  CG2  . VAL   A 1 150 ? -12.18783 -48.87032 -42.23976 1.000 152.01471 ? 123 VAL   A CG2  1 
ATOM   931  N  N    . SER   A 1 151 ? -13.80184 -47.45831 -39.81549 1.000 151.12609 ? 124 SER   A N    1 
ATOM   932  C  CA   . SER   A 1 151 ? -13.48652 -46.44612 -38.81696 1.000 139.13964 ? 124 SER   A CA   1 
ATOM   933  C  C    . SER   A 1 151 ? -12.26794 -46.86284 -38.00699 1.000 152.80611 ? 124 SER   A C    1 
ATOM   934  O  O    . SER   A 1 151 ? -12.22543 -47.97319 -37.46280 1.000 178.07290 ? 124 SER   A O    1 
ATOM   935  C  CB   . SER   A 1 151 ? -14.67980 -46.20686 -37.88355 1.000 135.53820 ? 124 SER   A CB   1 
ATOM   936  O  OG   . SER   A 1 151 ? -14.37342 -45.23226 -36.90208 1.000 156.03374 ? 124 SER   A OG   1 
ATOM   937  N  N    . ASP   A 1 152 ? -11.28169 -45.96341 -37.94617 1.000 142.87990 ? 125 ASP   A N    1 
ATOM   938  C  CA   . ASP   A 1 152 ? -10.11679 -46.05200 -37.06460 1.000 158.17239 ? 125 ASP   A CA   1 
ATOM   939  C  C    . ASP   A 1 152 ? -9.22484  -47.25134 -37.36272 1.000 162.69504 ? 125 ASP   A C    1 
ATOM   940  O  O    . ASP   A 1 152 ? -8.38059  -47.60974 -36.53417 1.000 182.46769 ? 125 ASP   A O    1 
ATOM   941  C  CB   . ASP   A 1 152 ? -10.53713 -46.07855 -35.59019 1.000 173.29034 ? 125 ASP   A CB   1 
ATOM   942  C  CG   . ASP   A 1 152 ? -11.22542 -44.80223 -35.15707 1.000 180.78893 ? 125 ASP   A CG   1 
ATOM   943  O  OD1  . ASP   A 1 152 ? -11.46970 -43.93319 -36.01925 1.000 184.49076 ? 125 ASP   A OD1  1 
ATOM   944  O  OD2  . ASP   A 1 152 ? -11.52011 -44.66669 -33.95165 1.000 179.17464 ? 125 ASP   A OD2  1 
ATOM   945  N  N    . ASP   A 1 153 ? -9.38052  -47.87351 -38.53429 1.000 147.92038 ? 126 ASP   A N    1 
ATOM   946  C  CA   . ASP   A 1 153 ? -8.68670  -49.12427 -38.85393 1.000 149.03400 ? 126 ASP   A CA   1 
ATOM   947  C  C    . ASP   A 1 153 ? -8.94061  -50.17996 -37.78262 1.000 154.56838 ? 126 ASP   A C    1 
ATOM   948  O  O    . ASP   A 1 153 ? -8.10274  -51.04885 -37.53236 1.000 158.39621 ? 126 ASP   A O    1 
ATOM   949  C  CB   . ASP   A 1 153 ? -7.18261  -48.90275 -39.04373 1.000 158.59081 ? 126 ASP   A CB   1 
ATOM   950  C  CG   . ASP   A 1 153 ? -6.85054  -48.25118 -40.36958 1.000 176.42841 ? 126 ASP   A CG   1 
ATOM   951  O  OD1  . ASP   A 1 153 ? -7.76016  -48.12245 -41.21434 1.000 180.37848 ? 126 ASP   A OD1  1 
ATOM   952  O  OD2  . ASP   A 1 153 ? -5.67862  -47.86780 -40.56778 1.000 170.53577 ? 126 ASP   A OD2  1 
ATOM   953  N  N    . GLU   A 1 154 ? -10.09506 -50.09932 -37.13840 1.000 161.35861 ? 127 GLU   A N    1 
ATOM   954  C  CA   . GLU   A 1 154 ? -10.46786 -50.99730 -36.05274 1.000 148.97114 ? 127 GLU   A CA   1 
ATOM   955  C  C    . GLU   A 1 154 ? -11.87225 -51.55785 -36.20638 1.000 163.07133 ? 127 GLU   A C    1 
ATOM   956  O  O    . GLU   A 1 154 ? -12.08373 -52.74228 -35.93725 1.000 179.54450 ? 127 GLU   A O    1 
ATOM   957  C  CB   . GLU   A 1 154 ? -10.34122 -50.27401 -34.69773 1.000 131.52742 ? 127 GLU   A CB   1 
ATOM   958  C  CG   . GLU   A 1 154 ? -8.91358  -49.92340 -34.30216 1.000 173.73837 ? 127 GLU   A CG   1 
ATOM   959  C  CD   . GLU   A 1 154 ? -8.83838  -49.20368 -32.96859 1.000 202.12559 ? 127 GLU   A CD   1 
ATOM   960  O  OE1  . GLU   A 1 154 ? -9.90094  -48.98622 -32.34930 1.000 188.88032 ? 127 GLU   A OE1  1 
ATOM   961  O  OE2  . GLU   A 1 154 ? -7.71778  -48.85495 -32.53942 1.000 206.02109 ? 127 GLU   A OE2  1 
ATOM   962  N  N    . ARG   A 1 155 ? -12.83518 -50.74437 -36.63414 1.000 154.31871 ? 128 ARG   A N    1 
ATOM   963  C  CA   . ARG   A 1 155 ? -14.21092 -51.19165 -36.79133 1.000 134.34324 ? 128 ARG   A CA   1 
ATOM   964  C  C    . ARG   A 1 155 ? -14.64090 -51.05395 -38.24410 1.000 152.17519 ? 128 ARG   A C    1 
ATOM   965  O  O    . ARG   A 1 155 ? -14.15482 -50.18402 -38.97119 1.000 152.51411 ? 128 ARG   A O    1 
ATOM   966  C  CB   . ARG   A 1 155 ? -15.15682 -50.39912 -35.88378 1.000 142.78623 ? 128 ARG   A CB   1 
ATOM   967  C  CG   . ARG   A 1 155 ? -15.05500 -50.78545 -34.42031 1.000 149.44615 ? 128 ARG   A CG   1 
ATOM   968  C  CD   . ARG   A 1 155 ? -15.57451 -49.68418 -33.51818 1.000 140.03287 ? 128 ARG   A CD   1 
ATOM   969  N  NE   . ARG   A 1 155 ? -14.74665 -48.48760 -33.60472 1.000 137.28128 ? 128 ARG   A NE   1 
ATOM   970  C  CZ   . ARG   A 1 155 ? -13.59221 -48.32998 -32.97148 1.000 163.88687 ? 128 ARG   A CZ   1 
ATOM   971  N  NH1  . ARG   A 1 155 ? -13.09006 -49.28196 -32.20175 1.000 155.88951 ? 128 ARG   A NH1  1 
ATOM   972  N  NH2  . ARG   A 1 155 ? -12.92339 -47.18962 -33.11579 1.000 188.86929 ? 128 ARG   A NH2  1 
ATOM   973  N  N    . CYS   A 1 156 ? -15.55449 -51.92367 -38.66790 1.000 163.91840 ? 129 CYS   A N    1 
ATOM   974  C  CA   . CYS   A 1 156 ? -16.00278 -51.87324 -40.05109 1.000 147.05639 ? 129 CYS   A CA   1 
ATOM   975  C  C    . CYS   A 1 156 ? -17.33932 -52.58371 -40.19405 1.000 148.34909 ? 129 CYS   A C    1 
ATOM   976  O  O    . CYS   A 1 156 ? -17.66011 -53.50512 -39.43725 1.000 156.91961 ? 129 CYS   A O    1 
ATOM   977  C  CB   . CYS   A 1 156 ? -14.97016 -52.49672 -40.99759 1.000 137.79396 ? 129 CYS   A CB   1 
ATOM   978  S  SG   . CYS   A 1 156 ? -14.54556 -54.20892 -40.61408 1.000 148.38862 ? 129 CYS   A SG   1 
ATOM   979  N  N    . TYR   A 1 157 ? -18.11269 -52.12747 -41.17567 1.000 142.46420 ? 130 TYR   A N    1 
ATOM   980  C  CA   . TYR   A 1 157 ? -19.34893 -52.76829 -41.59764 1.000 132.22934 ? 130 TYR   A CA   1 
ATOM   981  C  C    . TYR   A 1 157 ? -19.31417 -52.92683 -43.10789 1.000 135.85556 ? 130 TYR   A C    1 
ATOM   982  O  O    . TYR   A 1 157 ? -18.81749 -52.04749 -43.81535 1.000 131.49132 ? 130 TYR   A O    1 
ATOM   983  C  CB   . TYR   A 1 157 ? -20.58867 -51.95328 -41.19020 1.000 135.98606 ? 130 TYR   A CB   1 
ATOM   984  C  CG   . TYR   A 1 157 ? -21.85863 -52.37655 -41.90369 1.000 143.64686 ? 130 TYR   A CG   1 
ATOM   985  C  CD1  . TYR   A 1 157 ? -22.58738 -53.47600 -41.46978 1.000 158.12501 ? 130 TYR   A CD1  1 
ATOM   986  C  CD2  . TYR   A 1 157 ? -22.32651 -51.67777 -43.01258 1.000 113.69921 ? 130 TYR   A CD2  1 
ATOM   987  C  CE1  . TYR   A 1 157 ? -23.74384 -53.86958 -42.11803 1.000 144.14498 ? 130 TYR   A CE1  1 
ATOM   988  C  CE2  . TYR   A 1 157 ? -23.48254 -52.06547 -43.66796 1.000 107.52356 ? 130 TYR   A CE2  1 
ATOM   989  C  CZ   . TYR   A 1 157 ? -24.18678 -53.16173 -43.21498 1.000 128.37167 ? 130 TYR   A CZ   1 
ATOM   990  O  OH   . TYR   A 1 157 ? -25.33769 -53.55579 -43.85774 1.000 122.02982 ? 130 TYR   A OH   1 
ATOM   991  N  N    . VAL   A 1 158 ? -19.84210 -54.04282 -43.60122 1.000 140.99231 ? 131 VAL   A N    1 
ATOM   992  C  CA   . VAL   A 1 158 ? -19.95351 -54.26810 -45.03865 1.000 139.98729 ? 131 VAL   A CA   1 
ATOM   993  C  C    . VAL   A 1 158 ? -21.23778 -55.03693 -45.31139 1.000 136.13874 ? 131 VAL   A C    1 
ATOM   994  O  O    . VAL   A 1 158 ? -21.48531 -56.08190 -44.70284 1.000 144.14026 ? 131 VAL   A O    1 
ATOM   995  C  CB   . VAL   A 1 158 ? -18.72821 -55.01368 -45.60855 1.000 132.62229 ? 131 VAL   A CB   1 
ATOM   996  C  CG1  . VAL   A 1 158 ? -18.41590 -56.26376 -44.79360 1.000 146.43211 ? 131 VAL   A CG1  1 
ATOM   997  C  CG2  . VAL   A 1 158 ? -18.95028 -55.36076 -47.07376 1.000 113.84545 ? 131 VAL   A CG2  1 
ATOM   998  N  N    . GLY   A 1 159 ? -22.06097 -54.51406 -46.21376 1.000 123.27302 ? 132 GLY   A N    1 
ATOM   999  C  CA   . GLY   A 1 159 ? -23.31115 -55.16501 -46.54465 1.000 129.46360 ? 132 GLY   A CA   1 
ATOM   1000 C  C    . GLY   A 1 159 ? -24.04953 -54.48336 -47.67448 1.000 152.68464 ? 132 GLY   A C    1 
ATOM   1001 O  O    . GLY   A 1 159 ? -23.43516 -53.83853 -48.52969 1.000 177.11767 ? 132 GLY   A O    1 
ATOM   1002 N  N    . ASN   A 1 160 ? -25.37364 -54.62410 -47.68916 1.000 140.84559 ? 133 ASN   A N    1 
ATOM   1003 C  CA   . ASN   A 1 160 ? -26.22118 -54.00413 -48.69841 1.000 137.02587 ? 133 ASN   A CA   1 
ATOM   1004 C  C    . ASN   A 1 160 ? -27.10691 -52.91262 -48.10268 1.000 150.54719 ? 133 ASN   A C    1 
ATOM   1005 O  O    . ASN   A 1 160 ? -28.17845 -52.61229 -48.63429 1.000 147.36147 ? 133 ASN   A O    1 
ATOM   1006 C  CB   . ASN   A 1 160 ? -27.06661 -55.06029 -49.40784 1.000 132.22477 ? 133 ASN   A CB   1 
ATOM   1007 C  CG   . ASN   A 1 160 ? -27.68964 -56.05324 -48.44612 1.000 143.88390 ? 133 ASN   A CG   1 
ATOM   1008 O  OD1  . ASN   A 1 160 ? -28.76230 -55.81085 -47.89395 1.000 160.54427 ? 133 ASN   A OD1  1 
ATOM   1009 N  ND2  . ASN   A 1 160 ? -27.02033 -57.18335 -48.24608 1.000 123.20905 ? 133 ASN   A ND2  1 
ATOM   1010 N  N    . ALA   A 1 161 ? -26.66729 -52.30918 -47.00239 1.000 151.12514 ? 134 ALA   A N    1 
ATOM   1011 C  CA   . ALA   A 1 161 ? -27.36866 -51.19893 -46.36173 1.000 136.60019 ? 134 ALA   A CA   1 
ATOM   1012 C  C    . ALA   A 1 161 ? -26.59500 -49.92046 -46.67448 1.000 146.28371 ? 134 ALA   A C    1 
ATOM   1013 O  O    . ALA   A 1 161 ? -25.67881 -49.53552 -45.94581 1.000 147.92927 ? 134 ALA   A O    1 
ATOM   1014 C  CB   . ALA   A 1 161 ? -27.50090 -51.42020 -44.85764 1.000 112.64304 ? 134 ALA   A CB   1 
ATOM   1015 N  N    . SER   A 1 162 ? -26.97110 -49.26506 -47.76946 1.000 151.22152 ? 135 SER   A N    1 
ATOM   1016 C  CA   . SER   A 1 162 ? -26.30512 -48.03926 -48.17795 1.000 147.65042 ? 135 SER   A CA   1 
ATOM   1017 C  C    . SER   A 1 162 ? -26.59452 -46.91608 -47.18370 1.000 147.14738 ? 135 SER   A C    1 
ATOM   1018 O  O    . SER   A 1 162 ? -27.42785 -47.03968 -46.28207 1.000 145.25128 ? 135 SER   A O    1 
ATOM   1019 C  CB   . SER   A 1 162 ? -26.74356 -47.63445 -49.58536 1.000 132.56751 ? 135 SER   A CB   1 
ATOM   1020 O  OG   . SER   A 1 162 ? -26.34101 -48.59987 -50.54106 1.000 153.91902 ? 135 SER   A OG   1 
ATOM   1021 N  N    . PHE   A 1 163 ? -25.88665 -45.79950 -47.35932 1.000 147.20678 ? 136 PHE   A N    1 
ATOM   1022 C  CA   . PHE   A 1 163 ? -26.04091 -44.64105 -46.48002 1.000 148.57635 ? 136 PHE   A CA   1 
ATOM   1023 C  C    . PHE   A 1 163 ? -27.28049 -43.85116 -46.90353 1.000 150.75184 ? 136 PHE   A C    1 
ATOM   1024 O  O    . PHE   A 1 163 ? -27.21353 -42.73335 -47.41901 1.000 158.53615 ? 136 PHE   A O    1 
ATOM   1025 C  CB   . PHE   A 1 163 ? -24.78794 -43.77761 -46.50321 1.000 153.44576 ? 136 PHE   A CB   1 
ATOM   1026 C  CG   . PHE   A 1 163 ? -24.70578 -42.79910 -45.36574 1.000 141.31021 ? 136 PHE   A CG   1 
ATOM   1027 C  CD1  . PHE   A 1 163 ? -25.59148 -42.87367 -44.30186 1.000 124.80072 ? 136 PHE   A CD1  1 
ATOM   1028 C  CD2  . PHE   A 1 163 ? -23.74727 -41.80033 -45.36265 1.000 149.79209 ? 136 PHE   A CD2  1 
ATOM   1029 C  CE1  . PHE   A 1 163 ? -25.51946 -41.97356 -43.25513 1.000 122.90881 ? 136 PHE   A CE1  1 
ATOM   1030 C  CE2  . PHE   A 1 163 ? -23.67026 -40.89618 -44.31803 1.000 163.48801 ? 136 PHE   A CE2  1 
ATOM   1031 C  CZ   . PHE   A 1 163 ? -24.55742 -40.98329 -43.26342 1.000 156.69837 ? 136 PHE   A CZ   1 
ATOM   1032 N  N    . THR   A 1 164 ? -28.43652 -44.46859 -46.67465 1.000 134.74565 ? 137 THR   A N    1 
ATOM   1033 C  CA   . THR   A 1 164 ? -29.72534 -43.85066 -46.94180 1.000 126.80488 ? 137 THR   A CA   1 
ATOM   1034 C  C    . THR   A 1 164 ? -30.67043 -44.17992 -45.79640 1.000 144.53290 ? 137 THR   A C    1 
ATOM   1035 O  O    . THR   A 1 164 ? -30.46625 -45.14460 -45.05607 1.000 153.53552 ? 137 THR   A O    1 
ATOM   1036 C  CB   . THR   A 1 164 ? -30.32696 -44.32656 -48.27252 1.000 152.40814 ? 137 THR   A CB   1 
ATOM   1037 O  OG1  . THR   A 1 164 ? -30.25594 -45.75632 -48.34906 1.000 168.06820 ? 137 THR   A OG1  1 
ATOM   1038 C  CG2  . THR   A 1 164 ? -29.58365 -43.71790 -49.45227 1.000 172.75448 ? 137 THR   A CG2  1 
ATOM   1039 N  N    . GLY   A 1 165 ? -31.71565 -43.36282 -45.65613 1.000 144.69479 ? 138 GLY   A N    1 
ATOM   1040 C  CA   . GLY   A 1 165 ? -32.69131 -43.60791 -44.60902 1.000 138.90015 ? 138 GLY   A CA   1 
ATOM   1041 C  C    . GLY   A 1 165 ? -33.46062 -44.89753 -44.80718 1.000 136.67903 ? 138 GLY   A C    1 
ATOM   1042 O  O    . GLY   A 1 165 ? -33.81621 -45.56867 -43.83443 1.000 150.68880 ? 138 GLY   A O    1 
ATOM   1043 N  N    . GLY   A 1 166 ? -33.72525 -45.26445 -46.06224 1.000 120.48753 ? 139 GLY   A N    1 
ATOM   1044 C  CA   . GLY   A 1 166 ? -34.44358 -46.50011 -46.32278 1.000 138.55419 ? 139 GLY   A CA   1 
ATOM   1045 C  C    . GLY   A 1 166 ? -33.65091 -47.72963 -45.92397 1.000 142.11001 ? 139 GLY   A C    1 
ATOM   1046 O  O    . GLY   A 1 166 ? -34.18796 -48.64952 -45.30071 1.000 160.79592 ? 139 GLY   A O    1 
ATOM   1047 N  N    . SER   A 1 167 ? -32.36071 -47.76071 -46.26722 1.000 134.40560 ? 140 SER   A N    1 
ATOM   1048 C  CA   . SER   A 1 167 ? -31.51422 -48.89766 -45.92443 1.000 124.95712 ? 140 SER   A CA   1 
ATOM   1049 C  C    . SER   A 1 167 ? -31.30314 -49.04847 -44.42385 1.000 132.48760 ? 140 SER   A C    1 
ATOM   1050 O  O    . SER   A 1 167 ? -30.79219 -50.08675 -43.99097 1.000 150.10057 ? 140 SER   A O    1 
ATOM   1051 C  CB   . SER   A 1 167 ? -30.15780 -48.77539 -46.62312 1.000 129.98783 ? 140 SER   A CB   1 
ATOM   1052 O  OG   . SER   A 1 167 ? -30.29436 -48.83369 -48.03252 1.000 130.23991 ? 140 SER   A OG   1 
ATOM   1053 N  N    . ILE   A 1 168 ? -31.67748 -48.04857 -43.62755 1.000 124.92589 ? 141 ILE   A N    1 
ATOM   1054 C  CA   . ILE   A 1 168 ? -31.53216 -48.11883 -42.18522 1.000 128.51696 ? 141 ILE   A CA   1 
ATOM   1055 C  C    . ILE   A 1 168 ? -32.86811 -48.31755 -41.47492 1.000 128.72073 ? 141 ILE   A C    1 
ATOM   1056 O  O    . ILE   A 1 168 ? -32.89556 -48.90816 -40.38835 1.000 144.84583 ? 141 ILE   A O    1 
ATOM   1057 C  CB   . ILE   A 1 168 ? -30.81457 -46.85837 -41.65477 1.000 124.04423 ? 141 ILE   A CB   1 
ATOM   1058 C  CG1  . ILE   A 1 168 ? -29.50729 -46.62917 -42.41410 1.000 127.06521 ? 141 ILE   A CG1  1 
ATOM   1059 C  CG2  . ILE   A 1 168 ? -30.52915 -46.97663 -40.16249 1.000 126.54738 ? 141 ILE   A CG2  1 
ATOM   1060 C  CD1  . ILE   A 1 168 ? -28.78214 -45.36749 -42.00514 1.000 113.77586 ? 141 ILE   A CD1  1 
ATOM   1061 N  N    . HIS   A 1 169 ? -33.97653 -47.86966 -42.06170 1.000 135.60866 ? 142 HIS   A N    1 
ATOM   1062 C  CA   . HIS   A 1 169 ? -35.25428 -47.85493 -41.36112 1.000 135.59460 ? 142 HIS   A CA   1 
ATOM   1063 C  C    . HIS   A 1 169 ? -36.32400 -48.70132 -42.03351 1.000 135.39461 ? 142 HIS   A C    1 
ATOM   1064 O  O    . HIS   A 1 169 ? -36.97414 -49.51168 -41.36177 1.000 137.46455 ? 142 HIS   A O    1 
ATOM   1065 C  CB   . HIS   A 1 169 ? -35.74141 -46.40397 -41.22337 1.000 150.44467 ? 142 HIS   A CB   1 
ATOM   1066 C  CG   . HIS   A 1 169 ? -36.77029 -46.20406 -40.15478 1.000 152.62088 ? 142 HIS   A CG   1 
ATOM   1067 N  ND1  . HIS   A 1 169 ? -37.41903 -47.25118 -39.53669 1.000 169.99647 ? 142 HIS   A ND1  1 
ATOM   1068 C  CD2  . HIS   A 1 169 ? -37.25821 -45.07387 -39.59059 1.000 152.83709 ? 142 HIS   A CD2  1 
ATOM   1069 C  CE1  . HIS   A 1 169 ? -38.26478 -46.77488 -38.64064 1.000 188.94530 ? 142 HIS   A CE1  1 
ATOM   1070 N  NE2  . HIS   A 1 169 ? -38.18624 -45.45642 -38.65300 1.000 187.69461 ? 142 HIS   A NE2  1 
ATOM   1071 N  N    . THR   A 1 170 ? -36.53182 -48.54321 -43.34244 1.000 145.91413 ? 143 THR   A N    1 
ATOM   1072 C  CA   . THR   A 1 170 ? -37.70126 -49.10816 -44.00362 1.000 141.30820 ? 143 THR   A CA   1 
ATOM   1073 C  C    . THR   A 1 170 ? -37.39512 -50.22740 -44.98978 1.000 129.02734 ? 143 THR   A C    1 
ATOM   1074 O  O    . THR   A 1 170 ? -38.32712 -50.91970 -45.41376 1.000 140.87156 ? 143 THR   A O    1 
ATOM   1075 C  CB   . THR   A 1 170 ? -38.47756 -48.00471 -44.73815 1.000 144.25388 ? 143 THR   A CB   1 
ATOM   1076 O  OG1  . THR   A 1 170 ? -37.62735 -47.38600 -45.71159 1.000 146.46436 ? 143 THR   A OG1  1 
ATOM   1077 C  CG2  . THR   A 1 170 ? -38.96076 -46.95144 -43.75485 1.000 151.29814 ? 143 THR   A CG2  1 
ATOM   1078 N  N    . ILE   A 1 171 ? -36.13722 -50.42512 -45.37203 1.000 131.41861 ? 144 ILE   A N    1 
ATOM   1079 C  CA   . ILE   A 1 171 ? -35.75565 -51.45691 -46.32986 1.000 113.39281 ? 144 ILE   A CA   1 
ATOM   1080 C  C    . ILE   A 1 171 ? -34.98968 -52.54219 -45.58896 1.000 135.51389 ? 144 ILE   A C    1 
ATOM   1081 O  O    . ILE   A 1 171 ? -34.00711 -52.25286 -44.89541 1.000 171.13229 ? 144 ILE   A O    1 
ATOM   1082 C  CB   . ILE   A 1 171 ? -34.91524 -50.87717 -47.48138 1.000 119.40818 ? 144 ILE   A CB   1 
ATOM   1083 C  CG1  . ILE   A 1 171 ? -35.74015 -49.87388 -48.29105 1.000 131.86601 ? 144 ILE   A CG1  1 
ATOM   1084 C  CG2  . ILE   A 1 171 ? -34.38836 -51.99091 -48.37539 1.000 120.12271 ? 144 ILE   A CG2  1 
ATOM   1085 C  CD1  . ILE   A 1 171 ? -34.98695 -49.25445 -49.44735 1.000 139.95296 ? 144 ILE   A CD1  1 
ATOM   1086 N  N    . LYS   A 1 172 ? -35.44257 -53.78687 -45.72829 1.000 122.78879 ? 145 LYS   A N    1 
ATOM   1087 C  CA   . LYS   A 1 172 ? -34.71638 -54.90875 -45.14928 1.000 145.85427 ? 145 LYS   A CA   1 
ATOM   1088 C  C    . LYS   A 1 172 ? -33.34972 -55.03676 -45.80675 1.000 150.16641 ? 145 LYS   A C    1 
ATOM   1089 O  O    . LYS   A 1 172 ? -33.24430 -55.11440 -47.03427 1.000 153.50300 ? 145 LYS   A O    1 
ATOM   1090 C  CB   . LYS   A 1 172 ? -35.50495 -56.20609 -45.32434 1.000 116.67012 ? 145 LYS   A CB   1 
ATOM   1091 C  CG   . LYS   A 1 172 ? -34.75404 -57.43426 -44.83482 1.000 134.62677 ? 145 LYS   A CG   1 
ATOM   1092 C  CD   . LYS   A 1 172 ? -35.40833 -58.72469 -45.29185 1.000 119.45136 ? 145 LYS   A CD   1 
ATOM   1093 C  CE   . LYS   A 1 172 ? -34.64239 -59.92929 -44.76819 1.000 136.50113 ? 145 LYS   A CE   1 
ATOM   1094 N  NZ   . LYS   A 1 172 ? -33.20620 -59.89263 -45.16516 1.000 115.87322 ? 145 LYS   A NZ   1 
ATOM   1095 N  N    . THR   A 1 173 ? -32.29711 -55.04172 -44.99102 1.000 141.77030 ? 146 THR   A N    1 
ATOM   1096 C  CA   . THR   A 1 173 ? -30.93627 -55.16307 -45.50355 1.000 140.01688 ? 146 THR   A CA   1 
ATOM   1097 C  C    . THR   A 1 173 ? -30.17928 -56.20882 -44.69804 1.000 136.80007 ? 146 THR   A C    1 
ATOM   1098 O  O    . THR   A 1 173 ? -30.61369 -56.62209 -43.62295 1.000 139.64369 ? 146 THR   A O    1 
ATOM   1099 C  CB   . THR   A 1 173 ? -30.17291 -53.82931 -45.45394 1.000 146.37839 ? 146 THR   A CB   1 
ATOM   1100 O  OG1  . THR   A 1 173 ? -29.87407 -53.49497 -44.09301 1.000 149.51966 ? 146 THR   A OG1  1 
ATOM   1101 C  CG2  . THR   A 1 173 ? -30.98156 -52.70491 -46.08929 1.000 135.04892 ? 146 THR   A CG2  1 
ATOM   1102 N  N    . LEU   A 1 174 ? -29.01518 -56.60612 -45.21427 1.000 140.84930 ? 147 LEU   A N    1 
ATOM   1103 C  CA   . LEU   A 1 174 ? -28.16618 -57.59283 -44.56128 1.000 132.72726 ? 147 LEU   A CA   1 
ATOM   1104 C  C    . LEU   A 1 174 ? -26.70265 -57.20442 -44.73526 1.000 138.68533 ? 147 LEU   A C    1 
ATOM   1105 O  O    . LEU   A 1 174 ? -26.32592 -56.56694 -45.72212 1.000 150.95634 ? 147 LEU   A O    1 
ATOM   1106 C  CB   . LEU   A 1 174 ? -28.41648 -59.00200 -45.12124 1.000 125.76086 ? 147 LEU   A CB   1 
ATOM   1107 C  CG   . LEU   A 1 174 ? -27.74945 -60.18307 -44.41159 1.000 113.91691 ? 147 LEU   A CG   1 
ATOM   1108 C  CD1  . LEU   A 1 174 ? -28.19303 -60.25882 -42.95930 1.000 120.45772 ? 147 LEU   A CD1  1 
ATOM   1109 C  CD2  . LEU   A 1 174 ? -28.05186 -61.48620 -45.13536 1.000 115.84345 ? 147 LEU   A CD2  1 
ATOM   1110 N  N    . GLY   A 1 175 ? -25.88473 -57.59609 -43.76467 1.000 132.92237 ? 148 GLY   A N    1 
ATOM   1111 C  CA   . GLY   A 1 175 ? -24.46838 -57.28845 -43.79951 1.000 125.32448 ? 148 GLY   A CA   1 
ATOM   1112 C  C    . GLY   A 1 175 ? -23.77734 -57.84218 -42.57180 1.000 138.12010 ? 148 GLY   A C    1 
ATOM   1113 O  O    . GLY   A 1 175 ? -24.36732 -58.58512 -41.78515 1.000 148.32425 ? 148 GLY   A O    1 
ATOM   1114 N  N    . VAL   A 1 176 ? -22.51158 -57.46223 -42.40881 1.000 135.87113 ? 149 VAL   A N    1 
ATOM   1115 C  CA   . VAL   A 1 176 ? -21.67200 -57.96208 -41.32460 1.000 137.10362 ? 149 VAL   A CA   1 
ATOM   1116 C  C    . VAL   A 1 176 ? -20.90901 -56.79656 -40.70626 1.000 135.31717 ? 149 VAL   A C    1 
ATOM   1117 O  O    . VAL   A 1 176 ? -20.47307 -55.87854 -41.41083 1.000 128.98647 ? 149 VAL   A O    1 
ATOM   1118 C  CB   . VAL   A 1 176 ? -20.69195 -59.05099 -41.81758 1.000 129.75939 ? 149 VAL   A CB   1 
ATOM   1119 C  CG1  . VAL   A 1 176 ? -19.90959 -59.63461 -40.65443 1.000 136.09800 ? 149 VAL   A CG1  1 
ATOM   1120 C  CG2  . VAL   A 1 176 ? -21.43059 -60.15456 -42.56375 1.000 133.88993 ? 149 VAL   A CG2  1 
ATOM   1121 N  N    . TYR   A 1 177 ? -20.74629 -56.83838 -39.38344 1.000 132.32032 ? 150 TYR   A N    1 
ATOM   1122 C  CA   . TYR   A 1 177 ? -19.94472 -55.87230 -38.64463 1.000 114.55151 ? 150 TYR   A CA   1 
ATOM   1123 C  C    . TYR   A 1 177 ? -18.81840 -56.59466 -37.91918 1.000 147.56644 ? 150 TYR   A C    1 
ATOM   1124 O  O    . TYR   A 1 177 ? -18.99846 -57.71627 -37.43225 1.000 155.63655 ? 150 TYR   A O    1 
ATOM   1125 C  CB   . TYR   A 1 177 ? -20.79905 -55.09053 -37.63725 1.000 118.98068 ? 150 TYR   A CB   1 
ATOM   1126 C  CG   . TYR   A 1 177 ? -19.99990 -54.33023 -36.59789 1.000 136.23572 ? 150 TYR   A CG   1 
ATOM   1127 C  CD1  . TYR   A 1 177 ? -19.46563 -53.07960 -36.87988 1.000 148.91792 ? 150 TYR   A CD1  1 
ATOM   1128 C  CD2  . TYR   A 1 177 ? -19.78624 -54.86169 -35.33122 1.000 140.67340 ? 150 TYR   A CD2  1 
ATOM   1129 C  CE1  . TYR   A 1 177 ? -18.73547 -52.38219 -35.93146 1.000 138.21187 ? 150 TYR   A CE1  1 
ATOM   1130 C  CE2  . TYR   A 1 177 ? -19.05764 -54.17268 -34.37836 1.000 142.74845 ? 150 TYR   A CE2  1 
ATOM   1131 C  CZ   . TYR   A 1 177 ? -18.53573 -52.93407 -34.68304 1.000 150.58072 ? 150 TYR   A CZ   1 
ATOM   1132 O  OH   . TYR   A 1 177 ? -17.81295 -52.24716 -33.73445 1.000 153.74521 ? 150 TYR   A OH   1 
ATOM   1133 N  N    . SER   A 1 178 ? -17.65856 -55.94530 -37.83744 1.000 151.57339 ? 151 SER   A N    1 
ATOM   1134 C  CA   . SER   A 1 178 ? -16.51659 -56.53769 -37.15695 1.000 149.11059 ? 151 SER   A CA   1 
ATOM   1135 C  C    . SER   A 1 178 ? -15.65050 -55.44626 -36.54726 1.000 157.65311 ? 151 SER   A C    1 
ATOM   1136 O  O    . SER   A 1 178 ? -15.36063 -54.43463 -37.19357 1.000 163.52707 ? 151 SER   A O    1 
ATOM   1137 C  CB   . SER   A 1 178 ? -15.67941 -57.39751 -38.11101 1.000 149.15376 ? 151 SER   A CB   1 
ATOM   1138 O  OG   . SER   A 1 178 ? -14.58829 -57.99553 -37.43162 1.000 166.32639 ? 151 SER   A OG   1 
ATOM   1139 N  N    . ASP   A 1 179 ? -15.23642 -55.66748 -35.29845 1.000 157.99845 ? 152 ASP   A N    1 
ATOM   1140 C  CA   . ASP   A 1 179 ? -14.28362 -54.80468 -34.61219 1.000 156.50310 ? 152 ASP   A CA   1 
ATOM   1141 C  C    . ASP   A 1 179 ? -12.86597 -55.36507 -34.66492 1.000 169.12147 ? 152 ASP   A C    1 
ATOM   1142 O  O    . ASP   A 1 179 ? -12.08693 -55.18144 -33.72314 1.000 167.84128 ? 152 ASP   A O    1 
ATOM   1143 C  CB   . ASP   A 1 179 ? -14.71538 -54.57898 -33.16266 1.000 165.64690 ? 152 ASP   A CB   1 
ATOM   1144 C  CG   . ASP   A 1 179 ? -14.87140 -55.87550 -32.38901 1.000 180.48980 ? 152 ASP   A CG   1 
ATOM   1145 O  OD1  . ASP   A 1 179 ? -14.84280 -56.95503 -33.01635 1.000 186.93560 ? 152 ASP   A OD1  1 
ATOM   1146 O  OD2  . ASP   A 1 179 ? -15.02068 -55.81506 -31.15023 1.000 166.71441 ? 152 ASP   A OD2  1 
ATOM   1147 N  N    . TYR   A 1 180 ? -12.51814 -56.05029 -35.75470 1.000 176.21516 ? 153 TYR   A N    1 
ATOM   1148 C  CA   . TYR   A 1 180 ? -11.19798 -56.64083 -35.90549 1.000 167.49338 ? 153 TYR   A CA   1 
ATOM   1149 C  C    . TYR   A 1 180 ? -10.32299 -55.70915 -36.72689 1.000 169.13817 ? 153 TYR   A C    1 
ATOM   1150 O  O    . TYR   A 1 180 ? -10.65530 -55.42987 -37.89010 1.000 165.54504 ? 153 TYR   A O    1 
ATOM   1151 C  CB   . TYR   A 1 180 ? -11.29834 -58.00685 -36.57301 1.000 157.72708 ? 153 TYR   A CB   1 
ATOM   1152 C  CG   . TYR   A 1 180 ? -10.07746 -58.87385 -36.37997 1.000 160.42227 ? 153 TYR   A CG   1 
ATOM   1153 C  CD1  . TYR   A 1 180 ? -9.61649  -59.18496 -35.10684 1.000 172.97178 ? 153 TYR   A CD1  1 
ATOM   1154 C  CD2  . TYR   A 1 180 ? -9.39502  -59.39486 -37.46796 1.000 159.97510 ? 153 TYR   A CD2  1 
ATOM   1155 C  CE1  . TYR   A 1 180 ? -8.50032  -59.98064 -34.92516 1.000 174.79181 ? 153 TYR   A CE1  1 
ATOM   1156 C  CE2  . TYR   A 1 180 ? -8.28215  -60.19060 -37.29514 1.000 153.11558 ? 153 TYR   A CE2  1 
ATOM   1157 C  CZ   . TYR   A 1 180 ? -7.83769  -60.48194 -36.02465 1.000 157.19171 ? 153 TYR   A CZ   1 
ATOM   1158 O  OH   . TYR   A 1 180 ? -6.72677  -61.27709 -35.85698 1.000 176.98940 ? 153 TYR   A OH   1 
ATOM   1159 N  N    . PRO   A 1 181 ? -9.22169  -55.20617 -36.17541 1.000 152.47668 ? 154 PRO   A N    1 
ATOM   1160 C  CA   . PRO   A 1 181 ? -8.43621  -54.16291 -36.85979 1.000 155.46839 ? 154 PRO   A CA   1 
ATOM   1161 C  C    . PRO   A 1 181 ? -7.89413  -54.60576 -38.21201 1.000 158.43043 ? 154 PRO   A C    1 
ATOM   1162 O  O    . PRO   A 1 181 ? -7.95841  -53.82291 -39.17197 1.000 162.50787 ? 154 PRO   A O    1 
ATOM   1163 C  CB   . PRO   A 1 181 ? -7.30387  -53.86585 -35.86364 1.000 153.28799 ? 154 PRO   A CB   1 
ATOM   1164 C  CG   . PRO   A 1 181 ? -7.89524  -54.19898 -34.53427 1.000 156.97873 ? 154 PRO   A CG   1 
ATOM   1165 C  CD   . PRO   A 1 181 ? -8.81213  -55.37282 -34.76900 1.000 146.08699 ? 154 PRO   A CD   1 
ATOM   1166 N  N    . PRO   A 1 182 ? -7.32739  -55.81894 -38.34897 1.000 157.40283 ? 155 PRO   A N    1 
ATOM   1167 C  CA   . PRO   A 1 182 ? -6.79323  -56.19178 -39.67489 1.000 159.94259 ? 155 PRO   A CA   1 
ATOM   1168 C  C    . PRO   A 1 182 ? -7.84574  -56.22162 -40.77179 1.000 146.18350 ? 155 PRO   A C    1 
ATOM   1169 O  O    . PRO   A 1 182 ? -7.58831  -55.75244 -41.88913 1.000 161.37025 ? 155 PRO   A O    1 
ATOM   1170 C  CB   . PRO   A 1 182 ? -6.18688  -57.58088 -39.42876 1.000 144.59959 ? 155 PRO   A CB   1 
ATOM   1171 C  CG   . PRO   A 1 182 ? -5.86792  -57.59612 -37.98778 1.000 143.59880 ? 155 PRO   A CG   1 
ATOM   1172 C  CD   . PRO   A 1 182 ? -6.99270  -56.85039 -37.34712 1.000 146.74720 ? 155 PRO   A CD   1 
ATOM   1173 N  N    . LEU   A 1 183 ? -9.03080  -56.76234 -40.48270 1.000 140.49446 ? 156 LEU   A N    1 
ATOM   1174 C  CA   . LEU   A 1 183 ? -10.09665 -56.78853 -41.47938 1.000 151.12485 ? 156 LEU   A CA   1 
ATOM   1175 C  C    . LEU   A 1 183 ? -10.55281 -55.37620 -41.82976 1.000 159.20522 ? 156 LEU   A C    1 
ATOM   1176 O  O    . LEU   A 1 183 ? -10.78411 -55.05656 -43.00553 1.000 157.13930 ? 156 LEU   A O    1 
ATOM   1177 C  CB   . LEU   A 1 183 ? -11.26516 -57.62433 -40.95628 1.000 150.04332 ? 156 LEU   A CB   1 
ATOM   1178 C  CG   . LEU   A 1 183 ? -12.19133 -58.29430 -41.97005 1.000 156.40612 ? 156 LEU   A CG   1 
ATOM   1179 C  CD1  . LEU   A 1 183 ? -11.40564 -59.24411 -42.85761 1.000 147.69898 ? 156 LEU   A CD1  1 
ATOM   1180 C  CD2  . LEU   A 1 183 ? -13.30769 -59.03317 -41.25036 1.000 168.06282 ? 156 LEU   A CD2  1 
ATOM   1181 N  N    . ALA   A 1 184 ? -10.67733 -54.51288 -40.81828 1.000 150.65399 ? 157 ALA   A N    1 
ATOM   1182 C  CA   . ALA   A 1 184 ? -11.06213 -53.12834 -41.06650 1.000 152.18266 ? 157 ALA   A CA   1 
ATOM   1183 C  C    . ALA   A 1 184 ? -10.02892 -52.41509 -41.92848 1.000 146.36820 ? 157 ALA   A C    1 
ATOM   1184 O  O    . ALA   A 1 184 ? -10.38286 -51.59505 -42.78079 1.000 143.73985 ? 157 ALA   A O    1 
ATOM   1185 C  CB   . ALA   A 1 184 ? -11.26005 -52.39210 -39.74165 1.000 140.86936 ? 157 ALA   A CB   1 
ATOM   1186 N  N    . THR   A 1 185 ? -8.74504  -52.72547 -41.73521 1.000 141.67296 ? 158 THR   A N    1 
ATOM   1187 C  CA   . THR   A 1 185 ? -7.70895  -52.10263 -42.55479 1.000 155.16642 ? 158 THR   A CA   1 
ATOM   1188 C  C    . THR   A 1 185 ? -7.74055  -52.63754 -43.98261 1.000 167.09697 ? 158 THR   A C    1 
ATOM   1189 O  O    . THR   A 1 185 ? -7.53367  -51.88339 -44.94359 1.000 185.39104 ? 158 THR   A O    1 
ATOM   1190 C  CB   . THR   A 1 185 ? -6.33320  -52.32743 -41.92578 1.000 159.03161 ? 158 THR   A CB   1 
ATOM   1191 O  OG1  . THR   A 1 185 ? -6.35367  -51.89465 -40.55971 1.000 138.75253 ? 158 THR   A OG1  1 
ATOM   1192 C  CG2  . THR   A 1 185 ? -5.26842  -51.54268 -42.67795 1.000 155.40328 ? 158 THR   A CG2  1 
ATOM   1193 N  N    . ASP   A 1 186 ? -8.00206  -53.93702 -44.14303 1.000 158.18040 ? 159 ASP   A N    1 
ATOM   1194 C  CA   . ASP   A 1 186 ? -8.12228  -54.49420 -45.48607 1.000 168.47330 ? 159 ASP   A CA   1 
ATOM   1195 C  C    . ASP   A 1 186 ? -9.32308  -53.91351 -46.22445 1.000 168.14078 ? 159 ASP   A C    1 
ATOM   1196 O  O    . ASP   A 1 186 ? -9.31588  -53.84316 -47.45873 1.000 184.23042 ? 159 ASP   A O    1 
ATOM   1197 C  CB   . ASP   A 1 186 ? -8.21928  -56.01789 -45.42223 1.000 177.91228 ? 159 ASP   A CB   1 
ATOM   1198 C  CG   . ASP   A 1 186 ? -7.73645  -56.68306 -46.69558 1.000 186.95717 ? 159 ASP   A CG   1 
ATOM   1199 O  OD1  . ASP   A 1 186 ? -7.14305  -55.98231 -47.54304 1.000 183.53504 ? 159 ASP   A OD1  1 
ATOM   1200 O  OD2  . ASP   A 1 186 ? -7.94920  -57.90377 -46.84977 1.000 192.84951 ? 159 ASP   A OD2  1 
ATOM   1201 N  N    . LEU   A 1 187 ? -10.35942 -53.49874 -45.49122 1.000 159.38887 ? 160 LEU   A N    1 
ATOM   1202 C  CA   . LEU   A 1 187 ? -11.48678 -52.81305 -46.12225 1.000 154.00406 ? 160 LEU   A CA   1 
ATOM   1203 C  C    . LEU   A 1 187 ? -11.16939 -51.34189 -46.39367 1.000 152.28658 ? 160 LEU   A C    1 
ATOM   1204 O  O    . LEU   A 1 187 ? -11.61466 -50.77189 -47.40216 1.000 159.09828 ? 160 LEU   A O    1 
ATOM   1205 C  CB   . LEU   A 1 187 ? -12.72887 -52.94577 -45.24247 1.000 143.46179 ? 160 LEU   A CB   1 
ATOM   1206 C  CG   . LEU   A 1 187 ? -14.07307 -52.56922 -45.86221 1.000 129.61757 ? 160 LEU   A CG   1 
ATOM   1207 C  CD1  . LEU   A 1 187 ? -14.32798 -53.37318 -47.12881 1.000 121.39723 ? 160 LEU   A CD1  1 
ATOM   1208 C  CD2  . LEU   A 1 187 ? -15.19782 -52.77518 -44.86010 1.000 132.29817 ? 160 LEU   A CD2  1 
ATOM   1209 N  N    . ARG   A 1 188 ? -10.39827 -50.71498 -45.50301 1.000 155.05054 ? 161 ARG   A N    1 
ATOM   1210 C  CA   . ARG   A 1 188 ? -9.94657  -49.34842 -45.73449 1.000 153.52996 ? 161 ARG   A CA   1 
ATOM   1211 C  C    . ARG   A 1 188 ? -9.07102  -49.26018 -46.97631 1.000 171.82119 ? 161 ARG   A C    1 
ATOM   1212 O  O    . ARG   A 1 188 ? -9.04540  -48.22315 -47.64521 1.000 182.52713 ? 161 ARG   A O    1 
ATOM   1213 C  CB   . ARG   A 1 188 ? -9.19598  -48.83516 -44.50287 1.000 158.07620 ? 161 ARG   A CB   1 
ATOM   1214 C  CG   . ARG   A 1 188 ? -8.87803  -47.34580 -44.51649 1.000 156.80620 ? 161 ARG   A CG   1 
ATOM   1215 C  CD   . ARG   A 1 188 ? -7.46178  -47.07263 -45.00477 1.000 158.74661 ? 161 ARG   A CD   1 
ATOM   1216 N  NE   . ARG   A 1 188 ? -6.45247  -47.64927 -44.12442 1.000 157.11575 ? 161 ARG   A NE   1 
ATOM   1217 C  CZ   . ARG   A 1 188 ? -5.14454  -47.55918 -44.32445 1.000 175.88522 ? 161 ARG   A CZ   1 
ATOM   1218 N  NH1  . ARG   A 1 188 ? -4.64768  -46.92387 -45.37328 1.000 194.42790 ? 161 ARG   A NH1  1 
ATOM   1219 N  NH2  . ARG   A 1 188 ? -4.31407  -48.12036 -43.45009 1.000 175.91200 ? 161 ARG   A NH2  1 
ATOM   1220 N  N    . ARG   A 1 189 ? -8.34661  -50.33315 -47.29891 1.000 179.63573 ? 162 ARG   A N    1 
ATOM   1221 C  CA   . ARG   A 1 189 ? -7.58576  -50.35265 -48.54690 1.000 178.33274 ? 162 ARG   A CA   1 
ATOM   1222 C  C    . ARG   A 1 189 ? -8.51011  -50.28565 -49.76049 1.000 172.79266 ? 162 ARG   A C    1 
ATOM   1223 O  O    . ARG   A 1 189 ? -8.21481  -49.58925 -50.74188 1.000 177.70466 ? 162 ARG   A O    1 
ATOM   1224 C  CB   . ARG   A 1 189 ? -6.70100  -51.59741 -48.60711 1.000 183.05954 ? 162 ARG   A CB   1 
ATOM   1225 C  CG   . ARG   A 1 189 ? -5.26887  -51.34991 -48.16204 1.000 186.71184 ? 162 ARG   A CG   1 
ATOM   1226 C  CD   . ARG   A 1 189 ? -4.43757  -52.61947 -48.22190 1.000 197.75298 ? 162 ARG   A CD   1 
ATOM   1227 N  NE   . ARG   A 1 189 ? -4.66077  -53.47594 -47.06386 1.000 178.66754 ? 162 ARG   A NE   1 
ATOM   1228 C  CZ   . ARG   A 1 189 ? -3.90444  -53.47007 -45.97480 1.000 180.37457 ? 162 ARG   A CZ   1 
ATOM   1229 N  NH1  . ARG   A 1 189 ? -2.86045  -52.66503 -45.86275 1.000 175.78412 ? 162 ARG   A NH1  1 
ATOM   1230 N  NH2  . ARG   A 1 189 ? -4.20164  -54.29348 -44.97382 1.000 174.94648 ? 162 ARG   A NH2  1 
ATOM   1231 N  N    . ARG   A 1 190 ? -9.63585  -51.00347 -49.71297 1.000 164.97106 ? 163 ARG   A N    1 
ATOM   1232 C  CA   . ARG   A 1 190 ? -10.62275 -50.90032 -50.78387 1.000 170.22055 ? 163 ARG   A CA   1 
ATOM   1233 C  C    . ARG   A 1 190 ? -11.18506 -49.48760 -50.86965 1.000 161.71128 ? 163 ARG   A C    1 
ATOM   1234 O  O    . ARG   A 1 190 ? -11.38876 -48.95118 -51.96856 1.000 165.61936 ? 163 ARG   A O    1 
ATOM   1235 C  CB   . ARG   A 1 190 ? -11.75235 -51.90476 -50.55718 1.000 164.38443 ? 163 ARG   A CB   1 
ATOM   1236 C  CG   . ARG   A 1 190 ? -11.30051 -53.30073 -50.15684 1.000 161.40618 ? 163 ARG   A CG   1 
ATOM   1237 C  CD   . ARG   A 1 190 ? -10.54675 -53.99311 -51.27774 1.000 170.94309 ? 163 ARG   A CD   1 
ATOM   1238 N  NE   . ARG   A 1 190 ? -10.46467 -55.43360 -51.06528 1.000 165.20205 ? 163 ARG   A NE   1 
ATOM   1239 C  CZ   . ARG   A 1 190 ? -9.49401  -56.04103 -50.39683 1.000 165.57956 ? 163 ARG   A CZ   1 
ATOM   1240 N  NH1  . ARG   A 1 190 ? -8.49791  -55.36072 -49.85403 1.000 185.92188 ? 163 ARG   A NH1  1 
ATOM   1241 N  NH2  . ARG   A 1 190 ? -9.52356  -57.36472 -50.26987 1.000 148.75130 ? 163 ARG   A NH2  1 
ATOM   1242 N  N    . PHE   A 1 191 ? -11.45395 -48.87455 -49.71385 1.000 163.00473 ? 164 PHE   A N    1 
ATOM   1243 C  CA   . PHE   A 1 191 ? -11.91652 -47.48772 -49.71433 1.000 170.09197 ? 164 PHE   A CA   1 
ATOM   1244 C  C    . PHE   A 1 191 ? -10.88339 -46.56292 -50.35120 1.000 166.65049 ? 164 PHE   A C    1 
ATOM   1245 O  O    . PHE   A 1 191 ? -11.23919 -45.62949 -51.08113 1.000 164.09107 ? 164 PHE   A O    1 
ATOM   1246 C  CB   . PHE   A 1 191 ? -12.23889 -47.02635 -48.29242 1.000 174.67638 ? 164 PHE   A CB   1 
ATOM   1247 C  CG   . PHE   A 1 191 ? -12.79259 -45.62696 -48.22244 1.000 172.34432 ? 164 PHE   A CG   1 
ATOM   1248 C  CD1  . PHE   A 1 191 ? -11.94795 -44.53523 -48.08796 1.000 154.72553 ? 164 PHE   A CD1  1 
ATOM   1249 C  CD2  . PHE   A 1 191 ? -14.15768 -45.40360 -48.29870 1.000 167.43514 ? 164 PHE   A CD2  1 
ATOM   1250 C  CE1  . PHE   A 1 191 ? -12.45389 -43.24956 -48.03025 1.000 136.51155 ? 164 PHE   A CE1  1 
ATOM   1251 C  CE2  . PHE   A 1 191 ? -14.66999 -44.11989 -48.23764 1.000 158.86196 ? 164 PHE   A CE2  1 
ATOM   1252 C  CZ   . PHE   A 1 191 ? -13.81619 -43.04156 -48.10510 1.000 151.31274 ? 164 PHE   A CZ   1 
ATOM   1253 N  N    . ASP   A 1 192 ? -9.59958  -46.79849 -50.07014 1.000 180.14474 ? 165 ASP   A N    1 
ATOM   1254 C  CA   . ASP   A 1 192 ? -8.53719  -46.00548 -50.68277 1.000 182.67693 ? 165 ASP   A CA   1 
ATOM   1255 C  C    . ASP   A 1 192 ? -8.54132  -46.16844 -52.19515 1.000 175.44530 ? 165 ASP   A C    1 
ATOM   1256 O  O    . ASP   A 1 192 ? -8.41327  -45.18944 -52.93997 1.000 177.93321 ? 165 ASP   A O    1 
ATOM   1257 C  CB   . ASP   A 1 192 ? -7.17698  -46.41247 -50.11496 1.000 191.96462 ? 165 ASP   A CB   1 
ATOM   1258 C  CG   . ASP   A 1 192 ? -7.03286  -46.08295 -48.64711 1.000 190.66102 ? 165 ASP   A CG   1 
ATOM   1259 O  OD1  . ASP   A 1 192 ? -7.66360  -45.10819 -48.18832 1.000 203.28105 ? 165 ASP   A OD1  1 
ATOM   1260 O  OD2  . ASP   A 1 192 ? -6.28170  -46.79883 -47.95293 1.000 182.61015 ? 165 ASP   A OD2  1 
ATOM   1261 N  N    . THR   A 1 193 ? -8.67158  -47.41067 -52.66500 1.000 183.26250 ? 166 THR   A N    1 
ATOM   1262 C  CA   . THR   A 1 193 ? -8.72494  -47.65315 -54.10337 1.000 170.50209 ? 166 THR   A CA   1 
ATOM   1263 C  C    . THR   A 1 193 ? -9.90005  -46.92078 -54.74104 1.000 156.03841 ? 166 THR   A C    1 
ATOM   1264 O  O    . THR   A 1 193 ? -9.77218  -46.35662 -55.83444 1.000 154.24860 ? 166 THR   A O    1 
ATOM   1265 C  CB   . THR   A 1 193 ? -8.81048  -49.15463 -54.38233 1.000 165.13567 ? 166 THR   A CB   1 
ATOM   1266 O  OG1  . THR   A 1 193 ? -7.61237  -49.79590 -53.92677 1.000 183.42443 ? 166 THR   A OG1  1 
ATOM   1267 C  CG2  . THR   A 1 193 ? -8.98217  -49.41619 -55.87219 1.000 159.52867 ? 166 THR   A CG2  1 
ATOM   1268 N  N    . PHE   A 1 194 ? -11.04831 -46.89912 -54.06226 1.000 173.63503 ? 167 PHE   A N    1 
ATOM   1269 C  CA   . PHE   A 1 194 ? -12.22890 -46.26652 -54.64375 1.000 163.64127 ? 167 PHE   A CA   1 
ATOM   1270 C  C    . PHE   A 1 194 ? -12.17569 -44.74235 -54.58083 1.000 154.96777 ? 167 PHE   A C    1 
ATOM   1271 O  O    . PHE   A 1 194 ? -12.75459 -44.07542 -55.44619 1.000 128.60005 ? 167 PHE   A O    1 
ATOM   1272 C  CB   . PHE   A 1 194 ? -13.49380 -46.77730 -53.95203 1.000 149.47642 ? 167 PHE   A CB   1 
ATOM   1273 C  CG   . PHE   A 1 194 ? -13.94495 -48.12637 -54.43670 1.000 122.86959 ? 167 PHE   A CG   1 
ATOM   1274 C  CD1  . PHE   A 1 194 ? -13.69420 -48.52780 -55.73910 1.000 135.28615 ? 167 PHE   A CD1  1 
ATOM   1275 C  CD2  . PHE   A 1 194 ? -14.61710 -48.99371 -53.59163 1.000 142.26281 ? 167 PHE   A CD2  1 
ATOM   1276 C  CE1  . PHE   A 1 194 ? -14.10749 -49.76850 -56.19047 1.000 154.73448 ? 167 PHE   A CE1  1 
ATOM   1277 C  CE2  . PHE   A 1 194 ? -15.03251 -50.23613 -54.03698 1.000 173.92054 ? 167 PHE   A CE2  1 
ATOM   1278 C  CZ   . PHE   A 1 194 ? -14.77712 -50.62343 -55.33786 1.000 172.67284 ? 167 PHE   A CZ   1 
ATOM   1279 N  N    . LYS   A 1 195 ? -11.49641 -44.17325 -53.58034 1.000 163.27442 ? 168 LYS   A N    1 
ATOM   1280 C  CA   . LYS   A 1 195 ? -11.48897 -42.71932 -53.43179 1.000 163.95209 ? 168 LYS   A CA   1 
ATOM   1281 C  C    . LYS   A 1 195 ? -10.76778 -42.02784 -54.58296 1.000 166.29101 ? 168 LYS   A C    1 
ATOM   1282 O  O    . LYS   A 1 195 ? -11.13346 -40.90697 -54.95766 1.000 161.36364 ? 168 LYS   A O    1 
ATOM   1283 C  CB   . LYS   A 1 195 ? -10.84458 -42.32638 -52.10087 1.000 164.24735 ? 168 LYS   A CB   1 
ATOM   1284 C  CG   . LYS   A 1 195 ? -10.80377 -40.82350 -51.85705 1.000 160.26982 ? 168 LYS   A CG   1 
ATOM   1285 C  CD   . LYS   A 1 195 ? -9.91657  -40.46406 -50.67824 1.000 164.53466 ? 168 LYS   A CD   1 
ATOM   1286 C  CE   . LYS   A 1 195 ? -9.79393  -38.95561 -50.52859 1.000 171.30142 ? 168 LYS   A CE   1 
ATOM   1287 N  NZ   . LYS   A 1 195 ? -8.85087  -38.57968 -49.44014 1.000 146.44192 ? 168 LYS   A NZ   1 
ATOM   1288 N  N    . ALA   A 1 196 ? -9.75806  -42.67882 -55.16367 1.000 166.00245 ? 169 ALA   A N    1 
ATOM   1289 C  CA   . ALA   A 1 196 ? -8.91556  -42.03688 -56.16632 1.000 170.56873 ? 169 ALA   A CA   1 
ATOM   1290 C  C    . ALA   A 1 196 ? -9.66205  -41.68088 -57.44581 1.000 179.54985 ? 169 ALA   A C    1 
ATOM   1291 O  O    . ALA   A 1 196 ? -9.09822  -40.97881 -58.29236 1.000 210.87489 ? 169 ALA   A O    1 
ATOM   1292 C  CB   . ALA   A 1 196 ? -7.72704  -42.93949 -56.50012 1.000 156.00436 ? 169 ALA   A CB   1 
ATOM   1293 N  N    . PHE   A 1 197 ? -10.90488 -42.13405 -57.61115 1.000 156.14434 ? 170 PHE   A N    1 
ATOM   1294 C  CA   . PHE   A 1 197 ? -11.67465 -41.88113 -58.82268 1.000 172.79362 ? 170 PHE   A CA   1 
ATOM   1295 C  C    . PHE   A 1 197 ? -12.59063 -40.66893 -58.69086 1.000 167.96637 ? 170 PHE   A C    1 
ATOM   1296 O  O    . PHE   A 1 197 ? -13.68106 -40.64863 -59.27227 1.000 182.00221 ? 170 PHE   A O    1 
ATOM   1297 C  CB   . PHE   A 1 197 ? -12.47903 -43.12267 -59.20452 1.000 177.37215 ? 170 PHE   A CB   1 
ATOM   1298 C  CG   . PHE   A 1 197 ? -11.62926 -44.27197 -59.65943 1.000 178.75514 ? 170 PHE   A CG   1 
ATOM   1299 C  CD1  . PHE   A 1 197 ? -11.08238 -45.15334 -58.74171 1.000 169.94003 ? 170 PHE   A CD1  1 
ATOM   1300 C  CD2  . PHE   A 1 197 ? -11.36940 -44.46571 -61.00540 1.000 190.14535 ? 170 PHE   A CD2  1 
ATOM   1301 C  CE1  . PHE   A 1 197 ? -10.29615 -46.20822 -59.15879 1.000 172.51396 ? 170 PHE   A CE1  1 
ATOM   1302 C  CE2  . PHE   A 1 197 ? -10.58487 -45.51854 -61.42812 1.000 173.48692 ? 170 PHE   A CE2  1 
ATOM   1303 C  CZ   . PHE   A 1 197 ? -10.04618 -46.38890 -60.50324 1.000 163.42722 ? 170 PHE   A CZ   1 
ATOM   1304 N  N    . ASN   A 1 198 ? -12.16734 -39.65603 -57.93849 1.000 182.73702 ? 171 ASN   A N    1 
ATOM   1305 C  CA   . ASN   A 1 198 ? -12.93312 -38.42115 -57.85382 1.000 180.62590 ? 171 ASN   A CA   1 
ATOM   1306 C  C    . ASN   A 1 198 ? -12.94434 -37.71786 -59.20679 1.000 206.76037 ? 171 ASN   A C    1 
ATOM   1307 O  O    . ASN   A 1 198 ? -11.99762 -37.81554 -59.99186 1.000 213.82869 ? 171 ASN   A O    1 
ATOM   1308 C  CB   . ASN   A 1 198 ? -12.34589 -37.50436 -56.77907 1.000 177.65213 ? 171 ASN   A CB   1 
ATOM   1309 C  CG   . ASN   A 1 198 ? -13.15557 -36.23423 -56.58316 1.000 182.84853 ? 171 ASN   A CG   1 
ATOM   1310 O  OD1  . ASN   A 1 198 ? -14.30733 -36.14226 -57.00885 1.000 189.49001 ? 171 ASN   A OD1  1 
ATOM   1311 N  ND2  . ASN   A 1 198 ? -12.55450 -35.24780 -55.92895 1.000 201.30080 ? 171 ASN   A ND2  1 
ATOM   1312 N  N    . SER   A 1 199 ? -14.03652 -37.00174 -59.47827 1.000 204.49560 ? 172 SER   A N    1 
ATOM   1313 C  CA   . SER   A 1 199 ? -14.20711 -36.38337 -60.78838 1.000 210.20205 ? 172 SER   A CA   1 
ATOM   1314 C  C    . SER   A 1 199 ? -13.42664 -35.07905 -60.90983 1.000 232.88651 ? 172 SER   A C    1 
ATOM   1315 O  O    . SER   A 1 199 ? -12.82558 -34.80970 -61.95630 1.000 246.79060 ? 172 SER   A O    1 
ATOM   1316 C  CB   . SER   A 1 199 ? -15.69150 -36.14213 -61.06358 1.000 203.08875 ? 172 SER   A CB   1 
ATOM   1317 O  OG   . SER   A 1 199 ? -16.25755 -35.27514 -60.09650 1.000 199.78349 ? 172 SER   A OG   1 
ATOM   1318 N  N    . ALA   A 1 200 ? -13.42391 -34.26144 -59.85969 1.000 227.64586 ? 173 ALA   A N    1 
ATOM   1319 C  CA   . ALA   A 1 200 ? -12.75508 -32.96899 -59.91875 1.000 233.66127 ? 173 ALA   A CA   1 
ATOM   1320 C  C    . ALA   A 1 200 ? -11.24057 -33.13980 -59.90876 1.000 244.92306 ? 173 ALA   A C    1 
ATOM   1321 O  O    . ALA   A 1 200 ? -10.69487 -33.93412 -59.13712 1.000 231.57131 ? 173 ALA   A O    1 
ATOM   1322 C  CB   . ALA   A 1 200 ? -13.19614 -32.08957 -58.74847 1.000 232.13161 ? 173 ALA   A CB   1 
ATOM   1323 N  N    . LYS   A 1 201 ? -10.56809 -32.38594 -60.78499 1.000 253.78456 ? 174 LYS   A N    1 
ATOM   1324 C  CA   . LYS   A 1 201 ? -9.11296  -32.37585 -60.92333 1.000 259.94269 ? 174 LYS   A CA   1 
ATOM   1325 C  C    . LYS   A 1 201 ? -8.57343  -33.71199 -61.42498 1.000 272.52030 ? 174 LYS   A C    1 
ATOM   1326 O  O    . LYS   A 1 201 ? -9.26311  -34.73573 -61.36629 1.000 276.12140 ? 174 LYS   A O    1 
ATOM   1327 C  CB   . LYS   A 1 201 ? -8.44532  -31.99444 -59.59751 1.000 259.96768 ? 174 LYS   A CB   1 
ATOM   1328 C  CG   . LYS   A 1 201 ? -8.81292  -30.60687 -59.09400 1.000 239.63631 ? 174 LYS   A CG   1 
ATOM   1329 C  CD   . LYS   A 1 201 ? -8.14446  -30.30515 -57.76180 1.000 233.76523 ? 174 LYS   A CD   1 
ATOM   1330 C  CE   . LYS   A 1 201 ? -8.49313  -28.90744 -57.27472 1.000 218.52751 ? 174 LYS   A CE   1 
ATOM   1331 N  NZ   . LYS   A 1 201 ? -7.86248  -28.60259 -55.96017 1.000 212.79666 ? 174 LYS   A NZ   1 
ATOM   1332 N  N    . ASN   A 1 202 ? -7.34121  -33.70465 -61.93169 1.000 266.33889 ? 175 ASN   A N    1 
ATOM   1333 C  CA   . ASN   A 1 202 ? -6.73774  -34.92325 -62.45472 1.000 265.92729 ? 175 ASN   A CA   1 
ATOM   1334 C  C    . ASN   A 1 202 ? -6.55350  -35.94661 -61.34222 1.000 280.11850 ? 175 ASN   A C    1 
ATOM   1335 O  O    . ASN   A 1 202 ? -6.02453  -35.63298 -60.27186 1.000 286.70170 ? 175 ASN   A O    1 
ATOM   1336 C  CB   . ASN   A 1 202 ? -5.39369  -34.61110 -63.11369 1.000 250.24077 ? 175 ASN   A CB   1 
ATOM   1337 C  CG   . ASN   A 1 202 ? -5.54185  -33.80641 -64.38891 1.000 264.22421 ? 175 ASN   A CG   1 
ATOM   1338 O  OD1  . ASN   A 1 202 ? -6.63256  -33.70617 -64.94948 1.000 274.49115 ? 175 ASN   A OD1  1 
ATOM   1339 N  ND2  . ASN   A 1 202 ? -4.43935  -33.23532 -64.86011 1.000 237.56682 ? 175 ASN   A ND2  1 
ATOM   1340 N  N    . SER   A 1 203 ? -6.99500  -37.17261 -61.60001 1.000 289.54022 ? 176 SER   A N    1 
ATOM   1341 C  CA   . SER   A 1 203 ? -6.90536  -38.24775 -60.61985 1.000 290.67322 ? 176 SER   A CA   1 
ATOM   1342 C  C    . SER   A 1 203 ? -6.94961  -39.57764 -61.37977 1.000 301.40418 ? 176 SER   A C    1 
ATOM   1343 O  O    . SER   A 1 203 ? -6.69474  -39.62605 -62.57482 1.000 305.25842 ? 176 SER   A O    1 
ATOM   1344 C  CB   . SER   A 1 203 ? -8.02316  -38.11507 -59.57369 1.000 277.21880 ? 176 SER   A CB   1 
ATOM   1345 O  OG   . SER   A 1 203 ? -9.30140  -38.11679 -60.18582 1.000 275.83427 ? 176 SER   A OG   1 
ATOM   1346 N  N    . ALA   A 1 204 ? -7.28244  -40.65439 -60.65587 1.000 285.23335 ? 177 ALA   A N    1 
ATOM   1347 C  CA   . ALA   A 1 204 ? -7.37486  -41.97111 -61.27457 1.000 271.20519 ? 177 ALA   A CA   1 
ATOM   1348 C  C    . ALA   A 1 204 ? -8.55146  -42.09324 -62.23199 1.000 272.66411 ? 177 ALA   A C    1 
ATOM   1349 O  O    . ALA   A 1 204 ? -8.59952  -43.05630 -63.00475 1.000 270.25390 ? 177 ALA   A O    1 
ATOM   1350 C  CB   . ALA   A 1 204 ? -7.47455  -43.05217 -60.19833 1.000 241.78554 ? 177 ALA   A CB   1 
ATOM   1351 N  N    . ALA   A 1 205 ? -9.49577  -41.15486 -62.19810 1.000 275.44688 ? 178 ALA   A N    1 
ATOM   1352 C  CA   . ALA   A 1 205 ? -10.62007 -41.15534 -63.12222 1.000 258.84896 ? 178 ALA   A CA   1 
ATOM   1353 C  C    . ALA   A 1 205 ? -10.37982 -40.28914 -64.35062 1.000 287.78264 ? 178 ALA   A C    1 
ATOM   1354 O  O    . ALA   A 1 205 ? -11.19166 -40.32333 -65.28121 1.000 277.07712 ? 178 ALA   A O    1 
ATOM   1355 C  CB   . ALA   A 1 205 ? -11.89250 -40.68427 -62.40965 1.000 231.78099 ? 178 ALA   A CB   1 
ATOM   1356 N  N    . ASN   A 1 206 ? -9.29382  -39.51979 -64.37857 1.000 336.05282 ? 179 ASN   A N    1 
ATOM   1357 C  CA   . ASN   A 1 206 ? -8.99001  -38.63774 -65.49810 1.000 347.37794 ? 179 ASN   A CA   1 
ATOM   1358 C  C    . ASN   A 1 206 ? -7.71812  -39.03557 -66.22799 1.000 358.87534 ? 179 ASN   A C    1 
ATOM   1359 O  O    . ASN   A 1 206 ? -7.73043  -39.16783 -67.45781 1.000 381.76733 ? 179 ASN   A O    1 
ATOM   1360 C  CB   . ASN   A 1 206 ? -8.87911  -37.18569 -65.00781 1.000 329.85607 ? 179 ASN   A CB   1 
ATOM   1361 C  CG   . ASN   A 1 206 ? -8.51570  -36.22368 -66.11989 1.000 335.24639 ? 179 ASN   A CG   1 
ATOM   1362 O  OD1  . ASN   A 1 206 ? -7.33951  -36.01674 -66.41758 1.000 325.01958 ? 179 ASN   A OD1  1 
ATOM   1363 N  ND2  . ASN   A 1 206 ? -9.52681  -35.63097 -66.74330 1.000 346.42448 ? 179 ASN   A ND2  1 
ATOM   1364 N  N    . LEU   A 1 207 ? -6.61822  -39.22770 -65.50746 1.000 321.68465 ? 180 LEU   A N    1 
ATOM   1365 C  CA   . LEU   A 1 207 ? -5.34235  -39.58947 -66.10422 1.000 317.03697 ? 180 LEU   A CA   1 
ATOM   1366 C  C    . LEU   A 1 207 ? -5.12160  -41.09540 -66.03330 1.000 325.22150 ? 180 LEU   A C    1 
ATOM   1367 O  O    . LEU   A 1 207 ? -5.58045  -41.76949 -65.10717 1.000 324.47770 ? 180 LEU   A O    1 
ATOM   1368 C  CB   . LEU   A 1 207 ? -4.18665  -38.86790 -65.40640 1.000 295.90387 ? 180 LEU   A CB   1 
ATOM   1369 C  CG   . LEU   A 1 207 ? -4.14981  -37.34344 -65.51400 1.000 272.44635 ? 180 LEU   A CG   1 
ATOM   1370 C  CD1  . LEU   A 1 207 ? -2.92603  -36.79079 -64.79979 1.000 262.01932 ? 180 LEU   A CD1  1 
ATOM   1371 C  CD2  . LEU   A 1 207 ? -4.16624  -36.90931 -66.97075 1.000 237.51850 ? 180 LEU   A CD2  1 
ATOM   1372 N  N    . ALA   A 1 208 ? -4.40867  -41.61547 -67.03220 1.000 330.81915 ? 181 ALA   A N    1 
ATOM   1373 C  CA   . ALA   A 1 208 ? -4.01724  -43.01855 -67.06681 1.000 318.32807 ? 181 ALA   A CA   1 
ATOM   1374 C  C    . ALA   A 1 208 ? -2.74653  -43.27375 -66.26641 1.000 321.65615 ? 181 ALA   A C    1 
ATOM   1375 O  O    . ALA   A 1 208 ? -2.64810  -44.28692 -65.56615 1.000 328.71492 ? 181 ALA   A O    1 
ATOM   1376 C  CB   . ALA   A 1 208 ? -3.82268  -43.47756 -68.51606 1.000 278.93477 ? 181 ALA   A CB   1 
ATOM   1377 N  N    . SER   A 1 209 ? -1.76946  -42.36786 -66.35389 1.000 317.74474 ? 182 SER   A N    1 
ATOM   1378 C  CA   . SER   A 1 209 ? -0.53440  -42.53713 -65.59485 1.000 301.19535 ? 182 SER   A CA   1 
ATOM   1379 C  C    . SER   A 1 209 ? -0.78161  -42.39819 -64.09747 1.000 304.33833 ? 182 SER   A C    1 
ATOM   1380 O  O    . SER   A 1 209 ? -0.20914  -43.14627 -63.29593 1.000 278.83560 ? 182 SER   A O    1 
ATOM   1381 C  CB   . SER   A 1 209 ? 0.51126   -41.52567 -66.06356 1.000 290.59930 ? 182 SER   A CB   1 
ATOM   1382 O  OG   . SER   A 1 209 ? 0.05747   -40.19699 -65.87072 1.000 302.78416 ? 182 SER   A OG   1 
ATOM   1383 N  N    . ALA   A 1 210 ? -1.63106  -41.44702 -63.70128 1.000 310.81620 ? 183 ALA   A N    1 
ATOM   1384 C  CA   . ALA   A 1 210 ? -1.94862  -41.28347 -62.28647 1.000 299.43726 ? 183 ALA   A CA   1 
ATOM   1385 C  C    . ALA   A 1 210 ? -2.74616  -42.46881 -61.75875 1.000 303.41436 ? 183 ALA   A C    1 
ATOM   1386 O  O    . ALA   A 1 210 ? -2.57270  -42.87484 -60.60393 1.000 286.42687 ? 183 ALA   A O    1 
ATOM   1387 C  CB   . ALA   A 1 210 ? -2.71179  -39.97850 -62.06529 1.000 278.85610 ? 183 ALA   A CB   1 
ATOM   1388 N  N    . ALA   A 1 211 ? -3.62437  -43.03718 -62.58881 1.000 319.40142 ? 184 ALA   A N    1 
ATOM   1389 C  CA   . ALA   A 1 211 ? -4.35571  -44.23170 -62.18188 1.000 306.06159 ? 184 ALA   A CA   1 
ATOM   1390 C  C    . ALA   A 1 211 ? -3.43839  -45.44325 -62.08742 1.000 315.56913 ? 184 ALA   A C    1 
ATOM   1391 O  O    . ALA   A 1 211 ? -3.65027  -46.31497 -61.23639 1.000 315.30309 ? 184 ALA   A O    1 
ATOM   1392 C  CB   . ALA   A 1 211 ? -5.50125  -44.50742 -63.15555 1.000 301.28454 ? 184 ALA   A CB   1 
ATOM   1393 N  N    . ALA   A 1 212 ? -2.41830  -45.51580 -62.94651 1.000 304.52010 ? 185 ALA   A N    1 
ATOM   1394 C  CA   . ALA   A 1 212 ? -1.45970  -46.61167 -62.87688 1.000 279.76183 ? 185 ALA   A CA   1 
ATOM   1395 C  C    . ALA   A 1 212 ? -0.61234  -46.55902 -61.61316 1.000 274.44680 ? 185 ALA   A C    1 
ATOM   1396 O  O    . ALA   A 1 212 ? -0.03670  -47.58105 -61.22536 1.000 267.87836 ? 185 ALA   A O    1 
ATOM   1397 C  CB   . ALA   A 1 212 ? -0.55688  -46.60304 -64.11203 1.000 241.57904 ? 185 ALA   A CB   1 
ATOM   1398 N  N    . ALA   A 1 213 ? -0.52393  -45.39632 -60.96389 1.000 273.84942 ? 186 ALA   A N    1 
ATOM   1399 C  CA   . ALA   A 1 213 ? 0.22972   -45.24008 -59.72643 1.000 256.25084 ? 186 ALA   A CA   1 
ATOM   1400 C  C    . ALA   A 1 213 ? -0.62529  -45.46769 -58.48667 1.000 249.40712 ? 186 ALA   A C    1 
ATOM   1401 O  O    . ALA   A 1 213 ? -0.31571  -44.92541 -57.41777 1.000 244.70488 ? 186 ALA   A O    1 
ATOM   1402 C  CB   . ALA   A 1 213 ? 0.87871   -43.85643 -59.67816 1.000 237.93776 ? 186 ALA   A CB   1 
ATOM   1403 N  N    . LEU   A 1 214 ? -1.69752  -46.25311 -58.60122 1.000 245.90676 ? 187 LEU   A N    1 
ATOM   1404 C  CA   . LEU   A 1 214 ? -2.57133  -46.53261 -57.46991 1.000 235.57751 ? 187 LEU   A CA   1 
ATOM   1405 C  C    . LEU   A 1 214 ? -2.08432  -47.78504 -56.75535 1.000 244.55936 ? 187 LEU   A C    1 
ATOM   1406 O  O    . LEU   A 1 214 ? -2.14393  -48.87844 -57.33904 1.000 245.91199 ? 187 LEU   A O    1 
ATOM   1407 C  CB   . LEU   A 1 214 ? -4.00968  -46.71616 -57.93453 1.000 210.51814 ? 187 LEU   A CB   1 
ATOM   1408 C  CG   . LEU   A 1 214 ? -4.98826  -45.57026 -57.67075 1.000 214.87379 ? 187 LEU   A CG   1 
ATOM   1409 C  CD1  . LEU   A 1 214 ? -4.52760  -44.29065 -58.35062 1.000 214.59825 ? 187 LEU   A CD1  1 
ATOM   1410 C  CD2  . LEU   A 1 214 ? -6.38679  -45.95448 -58.12916 1.000 199.34899 ? 187 LEU   A CD2  1 
ATOM   1411 N  N    . PRO   A 1 215 ? -1.59714  -47.68762 -55.51645 1.000 252.18258 ? 188 PRO   A N    1 
ATOM   1412 C  CA   . PRO   A 1 215 ? -1.21697  -48.90058 -54.78013 1.000 254.12610 ? 188 PRO   A CA   1 
ATOM   1413 C  C    . PRO   A 1 215 ? -2.42258  -49.76324 -54.44355 1.000 260.66723 ? 188 PRO   A C    1 
ATOM   1414 O  O    . PRO   A 1 215 ? -2.86862  -49.80010 -53.29217 1.000 261.69755 ? 188 PRO   A O    1 
ATOM   1415 C  CB   . PRO   A 1 215 ? -0.54574  -48.35100 -53.51321 1.000 241.81763 ? 188 PRO   A CB   1 
ATOM   1416 C  CG   . PRO   A 1 215 ? -0.16940  -46.93911 -53.85346 1.000 228.73686 ? 188 PRO   A CG   1 
ATOM   1417 C  CD   . PRO   A 1 215 ? -1.24179  -46.46328 -54.78164 1.000 248.24374 ? 188 PRO   A CD   1 
ATOM   1418 N  N    . VAL   A 1 216 ? -2.96172  -50.45403 -55.44700 1.000 257.18883 ? 189 VAL   A N    1 
ATOM   1419 C  CA   . VAL   A 1 216 ? -4.09948  -51.34452 -55.25137 1.000 224.23074 ? 189 VAL   A CA   1 
ATOM   1420 C  C    . VAL   A 1 216 ? -3.62986  -52.56642 -54.47442 1.000 224.26123 ? 189 VAL   A C    1 
ATOM   1421 O  O    . VAL   A 1 216 ? -3.10943  -53.52562 -55.05531 1.000 222.80564 ? 189 VAL   A O    1 
ATOM   1422 C  CB   . VAL   A 1 216 ? -4.73409  -51.74311 -56.59628 1.000 204.59171 ? 189 VAL   A CB   1 
ATOM   1423 C  CG1  . VAL   A 1 216 ? -5.92742  -52.65382 -56.37272 1.000 202.44304 ? 189 VAL   A CG1  1 
ATOM   1424 C  CG2  . VAL   A 1 216 ? -5.13989  -50.50255 -57.37762 1.000 204.39845 ? 189 VAL   A CG2  1 
ATOM   1425 N  N    . SER   A 1 217 ? -3.80934  -52.53989 -53.15746 1.000 217.94826 ? 190 SER   A N    1 
ATOM   1426 C  CA   . SER   A 1 217 ? -3.29362  -53.57627 -52.27953 1.000 216.51279 ? 190 SER   A CA   1 
ATOM   1427 C  C    . SER   A 1 217 ? -4.43359  -54.31115 -51.58814 1.000 202.25945 ? 190 SER   A C    1 
ATOM   1428 O  O    . SER   A 1 217 ? -5.54484  -53.79381 -51.44496 1.000 196.16066 ? 190 SER   A O    1 
ATOM   1429 C  CB   . SER   A 1 217 ? -2.34463  -52.98762 -51.22605 1.000 233.91859 ? 190 SER   A CB   1 
ATOM   1430 O  OG   . SER   A 1 217 ? -1.26530  -52.30189 -51.83521 1.000 286.67882 ? 190 SER   A OG   1 
ATOM   1431 N  N    . THR   A 1 218 ? -4.13429  -55.53640 -51.16312 1.000 196.73108 ? 191 THR   A N    1 
ATOM   1432 C  CA   . THR   A 1 218 ? -5.04544  -56.33813 -50.36137 1.000 188.69961 ? 191 THR   A CA   1 
ATOM   1433 C  C    . THR   A 1 218 ? -4.21820  -57.20751 -49.42686 1.000 191.93246 ? 191 THR   A C    1 
ATOM   1434 O  O    . THR   A 1 218 ? -3.16307  -57.71856 -49.81325 1.000 212.67011 ? 191 THR   A O    1 
ATOM   1435 C  CB   . THR   A 1 218 ? -5.96531  -57.20762 -51.23025 1.000 187.78306 ? 191 THR   A CB   1 
ATOM   1436 O  OG1  . THR   A 1 218 ? -6.73529  -58.08040 -50.39297 1.000 180.79869 ? 191 THR   A OG1  1 
ATOM   1437 C  CG2  . THR   A 1 218 ? -5.15677  -58.03672 -52.21735 1.000 176.80305 ? 191 THR   A CG2  1 
ATOM   1438 N  N    . ALA   A 1 219 ? -4.69409  -57.35603 -48.19170 1.000 185.64391 ? 192 ALA   A N    1 
ATOM   1439 C  CA   . ALA   A 1 219 ? -3.99267  -58.15623 -47.19942 1.000 196.05035 ? 192 ALA   A CA   1 
ATOM   1440 C  C    . ALA   A 1 219 ? -4.48754  -59.59253 -47.12635 1.000 189.51622 ? 192 ALA   A C    1 
ATOM   1441 O  O    . ALA   A 1 219 ? -3.73091  -60.46763 -46.69177 1.000 215.85535 ? 192 ALA   A O    1 
ATOM   1442 C  CB   . ALA   A 1 219 ? -4.11306  -57.51233 -45.81213 1.000 205.19635 ? 192 ALA   A CB   1 
ATOM   1443 N  N    . TYR   A 1 220 ? -5.72612  -59.85721 -47.53952 1.000 176.65711 ? 193 TYR   A N    1 
ATOM   1444 C  CA   . TYR   A 1 220 ? -6.30667  -61.18764 -47.44346 1.000 175.50343 ? 193 TYR   A CA   1 
ATOM   1445 C  C    . TYR   A 1 220 ? -7.18814  -61.44887 -48.65382 1.000 180.13890 ? 193 TYR   A C    1 
ATOM   1446 O  O    . TYR   A 1 220 ? -7.89533  -60.55293 -49.12385 1.000 180.52264 ? 193 TYR   A O    1 
ATOM   1447 C  CB   . TYR   A 1 220 ? -7.12316  -61.34655 -46.15397 1.000 177.07850 ? 193 TYR   A CB   1 
ATOM   1448 C  CG   . TYR   A 1 220 ? -6.39970  -60.85054 -44.92449 1.000 181.49742 ? 193 TYR   A CG   1 
ATOM   1449 C  CD1  . TYR   A 1 220 ? -5.42086  -61.62215 -44.31320 1.000 188.57952 ? 193 TYR   A CD1  1 
ATOM   1450 C  CD2  . TYR   A 1 220 ? -6.68539  -59.60392 -44.38311 1.000 185.14050 ? 193 TYR   A CD2  1 
ATOM   1451 C  CE1  . TYR   A 1 220 ? -4.75099  -61.16939 -43.19266 1.000 186.02291 ? 193 TYR   A CE1  1 
ATOM   1452 C  CE2  . TYR   A 1 220 ? -6.02182  -59.14306 -43.26240 1.000 176.06330 ? 193 TYR   A CE2  1 
ATOM   1453 C  CZ   . TYR   A 1 220 ? -5.05407  -59.92890 -42.67328 1.000 174.69691 ? 193 TYR   A CZ   1 
ATOM   1454 O  OH   . TYR   A 1 220 ? -4.39021  -59.47655 -41.55619 1.000 188.11760 ? 193 TYR   A OH   1 
ATOM   1455 N  N    . HIS   A 1 221 ? -7.13854  -62.68056 -49.15097 1.000 171.46361 ? 194 HIS   A N    1 
ATOM   1456 C  CA   . HIS   A 1 221 ? -7.96330  -63.10645 -50.27281 1.000 170.22609 ? 194 HIS   A CA   1 
ATOM   1457 C  C    . HIS   A 1 221 ? -8.29198  -64.58460 -50.08478 1.000 169.45622 ? 194 HIS   A C    1 
ATOM   1458 O  O    . HIS   A 1 221 ? -8.08177  -65.15019 -49.00757 1.000 177.76064 ? 194 HIS   A O    1 
ATOM   1459 C  CB   . HIS   A 1 221 ? -7.25773  -62.80741 -51.60212 1.000 172.94425 ? 194 HIS   A CB   1 
ATOM   1460 C  CG   . HIS   A 1 221 ? -5.79118  -63.10815 -51.59397 1.000 178.82157 ? 194 HIS   A CG   1 
ATOM   1461 N  ND1  . HIS   A 1 221 ? -5.28448  -64.35178 -51.90289 1.000 199.90742 ? 194 HIS   A ND1  1 
ATOM   1462 C  CD2  . HIS   A 1 221 ? -4.72160  -62.32396 -51.31977 1.000 180.07500 ? 194 HIS   A CD2  1 
ATOM   1463 C  CE1  . HIS   A 1 221 ? -3.96642  -64.32159 -51.81760 1.000 203.03611 ? 194 HIS   A CE1  1 
ATOM   1464 N  NE2  . HIS   A 1 221 ? -3.59941  -63.10289 -51.46524 1.000 192.78629 ? 194 HIS   A NE2  1 
ATOM   1465 N  N    . ILE   A 1 222 ? -8.81742  -65.21606 -51.13859 1.000 174.40932 ? 195 ILE   A N    1 
ATOM   1466 C  CA   . ILE   A 1 222 ? -9.25116  -66.60568 -51.01489 1.000 174.00468 ? 195 ILE   A CA   1 
ATOM   1467 C  C    . ILE   A 1 222 ? -8.05759  -67.53033 -50.80989 1.000 177.76979 ? 195 ILE   A C    1 
ATOM   1468 O  O    . ILE   A 1 222 ? -8.19629  -68.61628 -50.23307 1.000 166.92343 ? 195 ILE   A O    1 
ATOM   1469 C  CB   . ILE   A 1 222 ? -10.09091 -67.02306 -52.23872 1.000 161.25961 ? 195 ILE   A CB   1 
ATOM   1470 C  CG1  . ILE   A 1 222 ? -10.84908 -68.32176 -51.95234 1.000 147.69119 ? 195 ILE   A CG1  1 
ATOM   1471 C  CG2  . ILE   A 1 222 ? -9.21330  -67.19086 -53.46957 1.000 166.03850 ? 195 ILE   A CG2  1 
ATOM   1472 C  CD1  . ILE   A 1 222 ? -11.71493 -68.79109 -53.10394 1.000 147.16239 ? 195 ILE   A CD1  1 
ATOM   1473 N  N    . LYS   A 1 223 ? -6.87157  -67.12219 -51.26091 1.000 180.12085 ? 196 LYS   A N    1 
ATOM   1474 C  CA   . LYS   A 1 223 ? -5.67010  -67.91928 -51.05840 1.000 188.77378 ? 196 LYS   A CA   1 
ATOM   1475 C  C    . LYS   A 1 223 ? -5.01927  -67.67211 -49.70452 1.000 183.84423 ? 196 LYS   A C    1 
ATOM   1476 O  O    . LYS   A 1 223 ? -4.14603  -68.44974 -49.30455 1.000 206.05066 ? 196 LYS   A O    1 
ATOM   1477 C  CB   . LYS   A 1 223 ? -4.66126  -67.64166 -52.17589 1.000 186.96839 ? 196 LYS   A CB   1 
ATOM   1478 C  CG   . LYS   A 1 223 ? -5.16600  -67.99828 -53.56488 1.000 186.69868 ? 196 LYS   A CG   1 
ATOM   1479 C  CD   . LYS   A 1 223 ? -4.14132  -67.65765 -54.63454 1.000 175.61542 ? 196 LYS   A CD   1 
ATOM   1480 C  CE   . LYS   A 1 223 ? -3.95652  -66.15509 -54.76659 1.000 173.61123 ? 196 LYS   A CE   1 
ATOM   1481 N  NZ   . LYS   A 1 223 ? -5.21488  -65.47718 -55.18486 1.000 159.76824 ? 196 LYS   A NZ   1 
ATOM   1482 N  N    . ASN   A 1 224 ? -5.42003  -66.61724 -48.99268 1.000 182.78331 ? 197 ASN   A N    1 
ATOM   1483 C  CA   . ASN   A 1 224 ? -4.88170  -66.31710 -47.66475 1.000 188.49558 ? 197 ASN   A CA   1 
ATOM   1484 C  C    . ASN   A 1 224 ? -5.94903  -65.60094 -46.85037 1.000 182.51851 ? 197 ASN   A C    1 
ATOM   1485 O  O    . ASN   A 1 224 ? -5.87064  -64.38967 -46.60988 1.000 174.11973 ? 197 ASN   A O    1 
ATOM   1486 C  CB   . ASN   A 1 224 ? -3.60835  -65.47903 -47.77320 1.000 195.60568 ? 197 ASN   A CB   1 
ATOM   1487 C  CG   . ASN   A 1 224 ? -2.97522  -65.20188 -46.42399 1.000 201.72779 ? 197 ASN   A CG   1 
ATOM   1488 O  OD1  . ASN   A 1 224 ? -2.97288  -64.06677 -45.94708 1.000 215.74435 ? 197 ASN   A OD1  1 
ATOM   1489 N  ND2  . ASN   A 1 224 ? -2.44140  -66.24303 -45.79683 1.000 206.53308 ? 197 ASN   A ND2  1 
ATOM   1490 N  N    . PRO   A 1 225 ? -6.97389  -66.32315 -46.40751 1.000 178.44794 ? 198 PRO   A N    1 
ATOM   1491 C  CA   . PRO   A 1 225 ? -8.02527  -65.70083 -45.60234 1.000 165.39213 ? 198 PRO   A CA   1 
ATOM   1492 C  C    . PRO   A 1 225 ? -7.58355  -65.51214 -44.15893 1.000 189.75297 ? 198 PRO   A C    1 
ATOM   1493 O  O    . PRO   A 1 225 ? -6.62106  -66.11870 -43.68487 1.000 188.95997 ? 198 PRO   A O    1 
ATOM   1494 C  CB   . PRO   A 1 225 ? -9.17834  -66.70374 -45.69757 1.000 139.08708 ? 198 PRO   A CB   1 
ATOM   1495 C  CG   . PRO   A 1 225 ? -8.48926  -68.01804 -45.83264 1.000 142.06486 ? 198 PRO   A CG   1 
ATOM   1496 C  CD   . PRO   A 1 225 ? -7.23169  -67.75841 -46.63132 1.000 165.84307 ? 198 PRO   A CD   1 
ATOM   1497 N  N    . ILE   A 1 226 ? -8.31477  -64.64919 -43.45941 1.000 189.30444 ? 199 ILE   A N    1 
ATOM   1498 C  CA   . ILE   A 1 226 ? -8.04804  -64.34387 -42.05899 1.000 184.06487 ? 199 ILE   A CA   1 
ATOM   1499 C  C    . ILE   A 1 226 ? -9.27641  -64.73181 -41.24617 1.000 169.39460 ? 199 ILE   A C    1 
ATOM   1500 O  O    . ILE   A 1 226 ? -10.37980 -64.22736 -41.49290 1.000 160.96938 ? 199 ILE   A O    1 
ATOM   1501 C  CB   . ILE   A 1 226 ? -7.67749  -62.86503 -41.85436 1.000 171.09038 ? 199 ILE   A CB   1 
ATOM   1502 C  CG1  . ILE   A 1 226 ? -7.51691  -62.55426 -40.36617 1.000 152.72239 ? 199 ILE   A CG1  1 
ATOM   1503 C  CG2  . ILE   A 1 226 ? -8.69407  -61.93441 -42.52095 1.000 160.84037 ? 199 ILE   A CG2  1 
ATOM   1504 C  CD1  . ILE   A 1 226 ? -6.76336  -61.27819 -40.10372 1.000 167.09966 ? 199 ILE   A CD1  1 
ATOM   1505 N  N    . GLY   A 1 227 ? -9.08720  -65.64054 -40.29112 1.000 168.30967 ? 200 GLY   A N    1 
ATOM   1506 C  CA   . GLY   A 1 227 ? -10.18163 -66.13817 -39.48067 1.000 163.32646 ? 200 GLY   A CA   1 
ATOM   1507 C  C    . GLY   A 1 227 ? -11.30401 -66.73439 -40.30463 1.000 159.77411 ? 200 GLY   A C    1 
ATOM   1508 O  O    . GLY   A 1 227 ? -12.46382 -66.73349 -39.88142 1.000 168.61540 ? 200 GLY   A O    1 
ATOM   1509 N  N    . GLY   A 1 228 ? -10.96858 -67.24695 -41.48602 1.000 151.20759 ? 201 GLY   A N    1 
ATOM   1510 C  CA   . GLY   A 1 228 ? -11.97879 -67.74783 -42.39729 1.000 174.10886 ? 201 GLY   A CA   1 
ATOM   1511 C  C    . GLY   A 1 228 ? -12.81932 -66.66815 -43.04004 1.000 172.24846 ? 201 GLY   A C    1 
ATOM   1512 O  O    . GLY   A 1 228 ? -14.00291 -66.89245 -43.30814 1.000 152.88608 ? 201 GLY   A O    1 
ATOM   1513 N  N    . VAL   A 1 229 ? -12.23926 -65.49632 -43.29191 1.000 166.11795 ? 202 VAL   A N    1 
ATOM   1514 C  CA   . VAL   A 1 229 ? -12.95734 -64.35434 -43.84832 1.000 156.05316 ? 202 VAL   A CA   1 
ATOM   1515 C  C    . VAL   A 1 229 ? -12.05380 -63.65612 -44.85535 1.000 159.57080 ? 202 VAL   A C    1 
ATOM   1516 O  O    . VAL   A 1 229 ? -10.85836 -63.46983 -44.60434 1.000 169.23858 ? 202 VAL   A O    1 
ATOM   1517 C  CB   . VAL   A 1 229 ? -13.40115 -63.37093 -42.74247 1.000 159.13760 ? 202 VAL   A CB   1 
ATOM   1518 C  CG1  . VAL   A 1 229 ? -13.87288 -62.05878 -43.34695 1.000 154.92089 ? 202 VAL   A CG1  1 
ATOM   1519 C  CG2  . VAL   A 1 229 ? -14.49514 -63.98437 -41.87913 1.000 158.76195 ? 202 VAL   A CG2  1 
ATOM   1520 N  N    . PHE   A 1 230 ? -12.62180 -63.27006 -45.99780 1.000 150.17517 ? 203 PHE   A N    1 
ATOM   1521 C  CA   . PHE   A 1 230 ? -11.86369 -62.50570 -46.97817 1.000 162.42321 ? 203 PHE   A CA   1 
ATOM   1522 C  C    . PHE   A 1 230 ? -12.80001 -61.63273 -47.80501 1.000 156.82565 ? 203 PHE   A C    1 
ATOM   1523 O  O    . PHE   A 1 230 ? -14.02410 -61.80612 -47.80441 1.000 147.16336 ? 203 PHE   A O    1 
ATOM   1524 C  CB   . PHE   A 1 230 ? -11.01898 -63.41912 -47.88127 1.000 162.06753 ? 203 PHE   A CB   1 
ATOM   1525 C  CG   . PHE   A 1 230 ? -11.81849 -64.41097 -48.67967 1.000 162.27951 ? 203 PHE   A CG   1 
ATOM   1526 C  CD1  . PHE   A 1 230 ? -12.19910 -65.62436 -48.12804 1.000 160.21591 ? 203 PHE   A CD1  1 
ATOM   1527 C  CD2  . PHE   A 1 230 ? -12.16370 -64.14106 -49.99337 1.000 162.00772 ? 203 PHE   A CD2  1 
ATOM   1528 C  CE1  . PHE   A 1 230 ? -12.92546 -66.54071 -48.86714 1.000 159.46848 ? 203 PHE   A CE1  1 
ATOM   1529 C  CE2  . PHE   A 1 230 ? -12.88839 -65.05241 -50.73703 1.000 157.98981 ? 203 PHE   A CE2  1 
ATOM   1530 C  CZ   . PHE   A 1 230 ? -13.26834 -66.25462 -50.17406 1.000 154.37283 ? 203 PHE   A CZ   1 
ATOM   1531 N  N    . PHE   A 1 231 ? -12.20126 -60.66336 -48.49146 1.000 153.45184 ? 204 PHE   A N    1 
ATOM   1532 C  CA   . PHE   A 1 231 ? -12.92512 -59.71825 -49.32907 1.000 152.25530 ? 204 PHE   A CA   1 
ATOM   1533 C  C    . PHE   A 1 231 ? -12.66364 -60.02692 -50.79549 1.000 148.61075 ? 204 PHE   A C    1 
ATOM   1534 O  O    . PHE   A 1 231 ? -11.50944 -60.19826 -51.20260 1.000 144.19797 ? 204 PHE   A O    1 
ATOM   1535 C  CB   . PHE   A 1 231 ? -12.50828 -58.27577 -49.02905 1.000 147.01602 ? 204 PHE   A CB   1 
ATOM   1536 C  CG   . PHE   A 1 231 ? -13.00560 -57.75410 -47.71243 1.000 141.83687 ? 204 PHE   A CG   1 
ATOM   1537 C  CD1  . PHE   A 1 231 ? -14.34720 -57.46280 -47.52987 1.000 148.82518 ? 204 PHE   A CD1  1 
ATOM   1538 C  CD2  . PHE   A 1 231 ? -12.12772 -57.53140 -46.66469 1.000 145.69143 ? 204 PHE   A CD2  1 
ATOM   1539 C  CE1  . PHE   A 1 231 ? -14.80683 -56.97445 -46.32165 1.000 155.68706 ? 204 PHE   A CE1  1 
ATOM   1540 C  CE2  . PHE   A 1 231 ? -12.58109 -57.04180 -45.45414 1.000 136.73931 ? 204 PHE   A CE2  1 
ATOM   1541 C  CZ   . PHE   A 1 231 ? -13.92237 -56.76326 -45.28264 1.000 137.20506 ? 204 PHE   A CZ   1 
ATOM   1542 N  N    . THR   A 1 232 ? -13.73127 -60.09771 -51.58029 1.000 140.50784 ? 205 THR   A N    1 
ATOM   1543 C  CA   . THR   A 1 232 ? -13.62522 -60.11199 -53.03085 1.000 142.85185 ? 205 THR   A CA   1 
ATOM   1544 C  C    . THR   A 1 232 ? -14.00941 -58.74071 -53.57316 1.000 150.63291 ? 205 THR   A C    1 
ATOM   1545 O  O    . THR   A 1 232 ? -14.71962 -57.97198 -52.92456 1.000 153.42326 ? 205 THR   A O    1 
ATOM   1546 C  CB   . THR   A 1 232 ? -14.51059 -61.20098 -53.64169 1.000 141.52477 ? 205 THR   A CB   1 
ATOM   1547 O  OG1  . THR   A 1 232 ? -15.84477 -61.07917 -53.13505 1.000 143.18795 ? 205 THR   A OG1  1 
ATOM   1548 C  CG2  . THR   A 1 232 ? -13.96497 -62.57741 -53.29861 1.000 141.97872 ? 205 THR   A CG2  1 
ATOM   1549 N  N    . ASP   A 1 233 ? -13.52122 -58.43015 -54.76982 1.000 147.90471 ? 206 ASP   A N    1 
ATOM   1550 C  CA   . ASP   A 1 233 ? -13.64005 -57.08223 -55.30253 1.000 144.33045 ? 206 ASP   A CA   1 
ATOM   1551 C  C    . ASP   A 1 233 ? -14.10342 -57.11515 -56.75159 1.000 161.13388 ? 206 ASP   A C    1 
ATOM   1552 O  O    . ASP   A 1 233 ? -14.01371 -58.13692 -57.43721 1.000 164.52475 ? 206 ASP   A O    1 
ATOM   1553 C  CB   . ASP   A 1 233 ? -12.30973 -56.32922 -55.18767 1.000 159.95740 ? 206 ASP   A CB   1 
ATOM   1554 C  CG   . ASP   A 1 233 ? -11.79699 -56.27786 -53.76302 1.000 179.09323 ? 206 ASP   A CG   1 
ATOM   1555 O  OD1  . ASP   A 1 233 ? -12.59704 -55.97355 -52.85368 1.000 186.31793 ? 206 ASP   A OD1  1 
ATOM   1556 O  OD2  . ASP   A 1 233 ? -10.60048 -56.55850 -53.54693 1.000 166.94095 ? 206 ASP   A OD2  1 
ATOM   1557 N  N    . SER   A 1 234 ? -14.60995 -55.97072 -57.20439 1.000 161.96629 ? 207 SER   A N    1 
ATOM   1558 C  CA   . SER   A 1 234 ? -15.09032 -55.80436 -58.56744 1.000 147.78891 ? 207 SER   A CA   1 
ATOM   1559 C  C    . SER   A 1 234 ? -14.96859 -54.33247 -58.92832 1.000 149.26801 ? 207 SER   A C    1 
ATOM   1560 O  O    . SER   A 1 234 ? -15.07637 -53.47479 -58.04356 1.000 171.29317 ? 207 SER   A O    1 
ATOM   1561 C  CB   . SER   A 1 234 ? -16.54560 -56.27809 -58.69883 1.000 136.51608 ? 207 SER   A CB   1 
ATOM   1562 O  OG   . SER   A 1 234 ? -16.89989 -56.54462 -60.04388 1.000 139.50263 ? 207 SER   A OG   1 
ATOM   1563 N  N    . PRO   A 1 235 ? -14.75303 -53.99995 -60.21237 1.000 146.78030 ? 208 PRO   A N    1 
ATOM   1564 C  CA   . PRO   A 1 235 ? -14.68325 -54.86907 -61.39363 1.000 169.98009 ? 208 PRO   A CA   1 
ATOM   1565 C  C    . PRO   A 1 235 ? -13.29122 -55.42647 -61.66184 1.000 192.70795 ? 208 PRO   A C    1 
ATOM   1566 O  O    . PRO   A 1 235 ? -12.40725 -55.36231 -60.81338 1.000 197.78428 ? 208 PRO   A O    1 
ATOM   1567 C  CB   . PRO   A 1 235 ? -15.13633 -53.93014 -62.51353 1.000 165.41104 ? 208 PRO   A CB   1 
ATOM   1568 C  CG   . PRO   A 1 235 ? -14.55292 -52.60677 -62.10357 1.000 148.15577 ? 208 PRO   A CG   1 
ATOM   1569 C  CD   . PRO   A 1 235 ? -14.60765 -52.58187 -60.58884 1.000 136.90577 ? 208 PRO   A CD   1 
ATOM   1570 N  N    . GLU   A 1 236 ? -13.07794 -55.97206 -62.86182 1.000 194.52896 ? 209 GLU   A N    1 
ATOM   1571 C  CA   . GLU   A 1 236 ? -11.80449 -56.61443 -63.16944 1.000 187.56948 ? 209 GLU   A CA   1 
ATOM   1572 C  C    . GLU   A 1 236 ? -10.70281 -55.58881 -63.40782 1.000 181.64960 ? 209 GLU   A C    1 
ATOM   1573 O  O    . GLU   A 1 236 ? -9.55049  -55.80816 -63.01649 1.000 197.13953 ? 209 GLU   A O    1 
ATOM   1574 C  CB   . GLU   A 1 236 ? -11.95971 -57.52925 -64.38446 1.000 190.78344 ? 209 GLU   A CB   1 
ATOM   1575 C  CG   . GLU   A 1 236 ? -10.71776 -58.34409 -64.71135 1.000 199.05690 ? 209 GLU   A CG   1 
ATOM   1576 C  CD   . GLU   A 1 236 ? -10.93879 -59.31009 -65.85856 1.000 228.28997 ? 209 GLU   A CD   1 
ATOM   1577 O  OE1  . GLU   A 1 236 ? -12.02520 -59.26645 -66.47318 1.000 250.20529 ? 209 GLU   A OE1  1 
ATOM   1578 O  OE2  . GLU   A 1 236 ? -10.02712 -60.11480 -66.14419 1.000 229.51404 ? 209 GLU   A OE2  1 
ATOM   1579 N  N    . HIS   A 1 237 ? -11.03051 -54.46347 -64.04027 1.000 173.09119 ? 210 HIS   A N    1 
ATOM   1580 C  CA   . HIS   A 1 237 ? -10.02486 -53.45329 -64.34490 1.000 188.89907 ? 210 HIS   A CA   1 
ATOM   1581 C  C    . HIS   A 1 237 ? -9.63254  -52.61528 -63.13193 1.000 185.81555 ? 210 HIS   A C    1 
ATOM   1582 O  O    . HIS   A 1 237 ? -8.86623  -51.65793 -63.28593 1.000 159.68267 ? 210 HIS   A O    1 
ATOM   1583 C  CB   . HIS   A 1 237 ? -10.51112 -52.54398 -65.47871 1.000 199.86814 ? 210 HIS   A CB   1 
ATOM   1584 C  CG   . HIS   A 1 237 ? -11.74854 -51.76800 -65.15086 1.000 197.86976 ? 210 HIS   A CG   1 
ATOM   1585 N  ND1  . HIS   A 1 237 ? -11.71134 -50.50509 -64.60019 1.000 194.97360 ? 210 HIS   A ND1  1 
ATOM   1586 C  CD2  . HIS   A 1 237 ? -13.05891 -52.07275 -65.30428 1.000 191.57501 ? 210 HIS   A CD2  1 
ATOM   1587 C  CE1  . HIS   A 1 237 ? -12.94521 -50.06660 -64.42532 1.000 197.55661 ? 210 HIS   A CE1  1 
ATOM   1588 N  NE2  . HIS   A 1 237 ? -13.78175 -50.99839 -64.84542 1.000 190.23857 ? 210 HIS   A NE2  1 
ATOM   1589 N  N    . LEU   A 1 238 ? -10.12307 -52.95574 -61.93818 1.000 193.73990 ? 211 LEU   A N    1 
ATOM   1590 C  CA   . LEU   A 1 238 ? -9.74705  -52.26367 -60.71063 1.000 186.16716 ? 211 LEU   A CA   1 
ATOM   1591 C  C    . LEU   A 1 238 ? -9.12147  -53.19608 -59.67998 1.000 189.92722 ? 211 LEU   A C    1 
ATOM   1592 O  O    . LEU   A 1 238 ? -8.92925  -52.78961 -58.52799 1.000 182.60862 ? 211 LEU   A O    1 
ATOM   1593 C  CB   . LEU   A 1 238 ? -10.96063 -51.55788 -60.09796 1.000 178.78726 ? 211 LEU   A CB   1 
ATOM   1594 C  CG   . LEU   A 1 238 ? -11.63951 -50.46439 -60.92332 1.000 179.04729 ? 211 LEU   A CG   1 
ATOM   1595 C  CD1  . LEU   A 1 238 ? -12.57585 -49.64568 -60.04573 1.000 163.87528 ? 211 LEU   A CD1  1 
ATOM   1596 C  CD2  . LEU   A 1 238 ? -10.61305 -49.57309 -61.59539 1.000 146.46657 ? 211 LEU   A CD2  1 
ATOM   1597 N  N    . LEU   A 1 239 ? -8.79677  -54.43063 -60.06102 1.000 188.10622 ? 212 LEU   A N    1 
ATOM   1598 C  CA   . LEU   A 1 239 ? -8.22430  -55.40201 -59.13677 1.000 187.54142 ? 212 LEU   A CA   1 
ATOM   1599 C  C    . LEU   A 1 239 ? -6.71426  -55.28937 -59.00808 1.000 199.53714 ? 212 LEU   A C    1 
ATOM   1600 O  O    . LEU   A 1 239 ? -6.16160  -55.66107 -57.96600 1.000 200.41708 ? 212 LEU   A O    1 
ATOM   1601 C  CB   . LEU   A 1 239 ? -8.56695  -56.82560 -59.58461 1.000 181.37309 ? 212 LEU   A CB   1 
ATOM   1602 C  CG   . LEU   A 1 239 ? -10.04375 -57.19792 -59.68992 1.000 190.75441 ? 212 LEU   A CG   1 
ATOM   1603 C  CD1  . LEU   A 1 239 ? -10.18035 -58.53028 -60.39619 1.000 205.16146 ? 212 LEU   A CD1  1 
ATOM   1604 C  CD2  . LEU   A 1 239 ? -10.67131 -57.24987 -58.31216 1.000 193.27389 ? 212 LEU   A CD2  1 
ATOM   1605 N  N    . GLY   A 1 240 ? -6.03401  -54.79615 -60.03928 1.000 185.25356 ? 213 GLY   A N    1 
ATOM   1606 C  CA   . GLY   A 1 240 ? -4.58434  -54.86328 -60.03679 1.000 177.40964 ? 213 GLY   A CA   1 
ATOM   1607 C  C    . GLY   A 1 240 ? -4.12507  -56.28084 -60.31914 1.000 203.95064 ? 213 GLY   A C    1 
ATOM   1608 O  O    . GLY   A 1 240 ? -4.66812  -56.97538 -61.18536 1.000 217.78752 ? 213 GLY   A O    1 
ATOM   1609 N  N    . TYR   A 1 241 ? -3.11889  -56.72869 -59.56887 1.000 202.73852 ? 214 TYR   A N    1 
ATOM   1610 C  CA   . TYR   A 1 241 ? -2.59098  -58.07581 -59.72017 1.000 201.57420 ? 214 TYR   A CA   1 
ATOM   1611 C  C    . TYR   A 1 241 ? -2.80896  -58.95566 -58.49830 1.000 185.70643 ? 214 TYR   A C    1 
ATOM   1612 O  O    . TYR   A 1 241 ? -2.62741  -60.17347 -58.59768 1.000 182.11557 ? 214 TYR   A O    1 
ATOM   1613 C  CB   . TYR   A 1 241 ? -1.08814  -58.03106 -60.03825 1.000 230.37273 ? 214 TYR   A CB   1 
ATOM   1614 C  CG   . TYR   A 1 241 ? -0.73586  -57.24224 -61.27882 1.000 239.78992 ? 214 TYR   A CG   1 
ATOM   1615 C  CD1  . TYR   A 1 241 ? -0.88165  -57.79656 -62.54370 1.000 240.61444 ? 214 TYR   A CD1  1 
ATOM   1616 C  CD2  . TYR   A 1 241 ? -0.24723  -55.94603 -61.18395 1.000 240.16975 ? 214 TYR   A CD2  1 
ATOM   1617 C  CE1  . TYR   A 1 241 ? -0.55834  -57.07837 -63.68014 1.000 234.84957 ? 214 TYR   A CE1  1 
ATOM   1618 C  CE2  . TYR   A 1 241 ? 0.07942   -55.22012 -62.31367 1.000 246.58010 ? 214 TYR   A CE2  1 
ATOM   1619 C  CZ   . TYR   A 1 241 ? -0.07794  -55.79070 -63.55907 1.000 238.51964 ? 214 TYR   A CZ   1 
ATOM   1620 O  OH   . TYR   A 1 241 ? 0.24621   -55.07120 -64.68644 1.000 226.29545 ? 214 TYR   A OH   1 
ATOM   1621 N  N    . SER   A 1 242 ? -3.19608  -58.38405 -57.35910 1.000 190.12626 ? 215 SER   A N    1 
ATOM   1622 C  CA   . SER   A 1 242 ? -3.31638  -59.13118 -56.11230 1.000 178.14573 ? 215 SER   A CA   1 
ATOM   1623 C  C    . SER   A 1 242 ? -4.75286  -59.48770 -55.75564 1.000 164.10441 ? 215 SER   A C    1 
ATOM   1624 O  O    . SER   A 1 242 ? -5.01715  -60.61851 -55.33540 1.000 167.76408 ? 215 SER   A O    1 
ATOM   1625 C  CB   . SER   A 1 242 ? -2.69497  -58.33285 -54.96192 1.000 190.86269 ? 215 SER   A CB   1 
ATOM   1626 O  OG   . SER   A 1 242 ? -3.35739  -57.09136 -54.79049 1.000 176.59179 ? 215 SER   A OG   1 
ATOM   1627 N  N    . ARG   A 1 243 ? -5.68494  -58.55185 -55.91101 1.000 158.49755 ? 216 ARG   A N    1 
ATOM   1628 C  CA   . ARG   A 1 243 ? -7.05813  -58.77686 -55.48799 1.000 168.29040 ? 216 ARG   A CA   1 
ATOM   1629 C  C    . ARG   A 1 243 ? -7.72915  -59.84119 -56.35312 1.000 169.02857 ? 216 ARG   A C    1 
ATOM   1630 O  O    . ARG   A 1 243 ? -7.33099  -60.10257 -57.49171 1.000 167.44292 ? 216 ARG   A O    1 
ATOM   1631 C  CB   . ARG   A 1 243 ? -7.85362  -57.47215 -55.54269 1.000 172.88587 ? 216 ARG   A CB   1 
ATOM   1632 C  CG   . ARG   A 1 243 ? -7.26733  -56.36139 -54.68416 1.000 184.13428 ? 216 ARG   A CG   1 
ATOM   1633 C  CD   . ARG   A 1 243 ? -8.10150  -55.09373 -54.75540 1.000 174.92596 ? 216 ARG   A CD   1 
ATOM   1634 N  NE   . ARG   A 1 243 ? -7.59914  -54.06333 -53.85444 1.000 199.35235 ? 216 ARG   A NE   1 
ATOM   1635 C  CZ   . ARG   A 1 243 ? -8.17874  -52.88605 -53.66446 1.000 188.28417 ? 216 ARG   A CZ   1 
ATOM   1636 N  NH1  . ARG   A 1 243 ? -9.29413  -52.55512 -54.29417 1.000 175.00845 ? 216 ARG   A NH1  1 
ATOM   1637 N  NH2  . ARG   A 1 243 ? -7.62552  -52.01913 -52.82103 1.000 174.76743 ? 216 ARG   A NH2  1 
ATOM   1638 N  N    . ASP   A 1 244 ? -8.76226  -60.46191 -55.79045 1.000 159.09233 ? 217 ASP   A N    1 
ATOM   1639 C  CA   . ASP   A 1 244 ? -9.50412  -61.51711 -56.46473 1.000 166.70879 ? 217 ASP   A CA   1 
ATOM   1640 C  C    . ASP   A 1 244 ? -10.83475 -60.98618 -56.97907 1.000 166.05301 ? 217 ASP   A C    1 
ATOM   1641 O  O    . ASP   A 1 244 ? -11.52861 -60.23640 -56.28561 1.000 181.63757 ? 217 ASP   A O    1 
ATOM   1642 C  CB   . ASP   A 1 244 ? -9.74708  -62.70214 -55.52882 1.000 138.67296 ? 217 ASP   A CB   1 
ATOM   1643 C  CG   . ASP   A 1 244 ? -8.46333  -63.39498 -55.12275 1.000 180.87338 ? 217 ASP   A CG   1 
ATOM   1644 O  OD1  . ASP   A 1 244 ? -7.43134  -63.18040 -55.79360 1.000 198.91328 ? 217 ASP   A OD1  1 
ATOM   1645 O  OD2  . ASP   A 1 244 ? -8.48889  -64.16151 -54.13845 1.000 180.34341 ? 217 ASP   A OD2  1 
ATOM   1646 N  N    . LEU   A 1 245 ? -11.18548 -61.38656 -58.19842 1.000 150.82705 ? 218 LEU   A N    1 
ATOM   1647 C  CA   . LEU   A 1 245 ? -12.44866 -60.97369 -58.79277 1.000 156.78652 ? 218 LEU   A CA   1 
ATOM   1648 C  C    . LEU   A 1 245 ? -13.60665 -61.69926 -58.12202 1.000 156.65327 ? 218 LEU   A C    1 
ATOM   1649 O  O    . LEU   A 1 245 ? -13.57601 -62.92301 -57.95956 1.000 147.91183 ? 218 LEU   A O    1 
ATOM   1650 C  CB   . LEU   A 1 245 ? -12.44555 -61.25774 -60.29373 1.000 156.95532 ? 218 LEU   A CB   1 
ATOM   1651 C  CG   . LEU   A 1 245 ? -13.69210 -60.83755 -61.07320 1.000 171.35509 ? 218 LEU   A CG   1 
ATOM   1652 C  CD1  . LEU   A 1 245 ? -13.97455 -59.35618 -60.88070 1.000 168.45804 ? 218 LEU   A CD1  1 
ATOM   1653 C  CD2  . LEU   A 1 245 ? -13.52988 -61.16638 -62.54817 1.000 183.88686 ? 218 LEU   A CD2  1 
ATOM   1654 N  N    . ASP   A 1 246 ? -14.63138 -60.93829 -57.73030 1.000 146.44150 ? 219 ASP   A N    1 
ATOM   1655 C  CA   . ASP   A 1 246 ? -15.80252 -61.54426 -57.10736 1.000 149.76843 ? 219 ASP   A CA   1 
ATOM   1656 C  C    . ASP   A 1 246 ? -16.52313 -62.47759 -58.07037 1.000 151.50932 ? 219 ASP   A C    1 
ATOM   1657 O  O    . ASP   A 1 246 ? -17.09919 -63.48615 -57.64457 1.000 162.86983 ? 219 ASP   A O    1 
ATOM   1658 C  CB   . ASP   A 1 246 ? -16.75206 -60.45463 -56.60872 1.000 139.01985 ? 219 ASP   A CB   1 
ATOM   1659 C  CG   . ASP   A 1 246 ? -17.77974 -60.98120 -55.62683 1.000 154.39402 ? 219 ASP   A CG   1 
ATOM   1660 O  OD1  . ASP   A 1 246 ? -17.59969 -62.10998 -55.12342 1.000 156.79170 ? 219 ASP   A OD1  1 
ATOM   1661 O  OD2  . ASP   A 1 246 ? -18.76859 -60.26681 -55.35917 1.000 156.43741 ? 219 ASP   A OD2  1 
ATOM   1662 N  N    . THR   A 1 247 ? -16.49187 -62.16279 -59.36765 1.000 145.33292 ? 220 THR   A N    1 
ATOM   1663 C  CA   . THR   A 1 247 ? -17.14042 -63.00913 -60.36439 1.000 154.80198 ? 220 THR   A CA   1 
ATOM   1664 C  C    . THR   A 1 247 ? -16.56969 -64.42139 -60.33995 1.000 151.68362 ? 220 THR   A C    1 
ATOM   1665 O  O    . THR   A 1 247 ? -17.31271 -65.40484 -60.21993 1.000 145.43604 ? 220 THR   A O    1 
ATOM   1666 C  CB   . THR   A 1 247 ? -16.97707 -62.39232 -61.75504 1.000 134.62695 ? 220 THR   A CB   1 
ATOM   1667 O  OG1  . THR   A 1 247 ? -17.43135 -61.03309 -61.73651 1.000 140.27704 ? 220 THR   A OG1  1 
ATOM   1668 C  CG2  . THR   A 1 247 ? -17.77248 -63.17714 -62.78717 1.000 140.22280 ? 220 THR   A CG2  1 
ATOM   1669 N  N    . ASP   A 1 248 ? -15.24393 -64.53693 -60.45588 1.000 151.06799 ? 221 ASP   A N    1 
ATOM   1670 C  CA   . ASP   A 1 248 ? -14.60979 -65.84999 -60.48267 1.000 159.88505 ? 221 ASP   A CA   1 
ATOM   1671 C  C    . ASP   A 1 248 ? -14.82974 -66.59799 -59.17605 1.000 157.21754 ? 221 ASP   A C    1 
ATOM   1672 O  O    . ASP   A 1 248 ? -15.07303 -67.80862 -59.18252 1.000 176.00411 ? 221 ASP   A O    1 
ATOM   1673 C  CB   . ASP   A 1 248 ? -13.11565 -65.70707 -60.77160 1.000 161.24065 ? 221 ASP   A CB   1 
ATOM   1674 C  CG   . ASP   A 1 248 ? -12.83881 -65.21408 -62.17687 1.000 176.43123 ? 221 ASP   A CG   1 
ATOM   1675 O  OD1  . ASP   A 1 248 ? -13.68081 -65.45248 -63.06794 1.000 192.07132 ? 221 ASP   A OD1  1 
ATOM   1676 O  OD2  . ASP   A 1 248 ? -11.77765 -64.59187 -62.39185 1.000 181.64951 ? 221 ASP   A OD2  1 
ATOM   1677 N  N    . VAL   A 1 249 ? -14.75885 -65.89331 -58.04527 1.000 136.90213 ? 222 VAL   A N    1 
ATOM   1678 C  CA   . VAL   A 1 249 ? -14.92736 -66.54723 -56.74948 1.000 147.64025 ? 222 VAL   A CA   1 
ATOM   1679 C  C    . VAL   A 1 249 ? -16.33704 -67.11222 -56.61639 1.000 144.34935 ? 222 VAL   A C    1 
ATOM   1680 O  O    . VAL   A 1 249 ? -16.52793 -68.26130 -56.19722 1.000 135.15764 ? 222 VAL   A O    1 
ATOM   1681 C  CB   . VAL   A 1 249 ? -14.59687 -65.56859 -55.60853 1.000 125.36771 ? 222 VAL   A CB   1 
ATOM   1682 C  CG1  . VAL   A 1 249 ? -14.95009 -66.18083 -54.26243 1.000 121.26470 ? 222 VAL   A CG1  1 
ATOM   1683 C  CG2  . VAL   A 1 249 ? -13.12425 -65.19029 -55.65314 1.000 145.35203 ? 222 VAL   A CG2  1 
ATOM   1684 N  N    . VAL   A 1 250 ? -17.34619 -66.31683 -56.98098 1.000 143.16631 ? 223 VAL   A N    1 
ATOM   1685 C  CA   . VAL   A 1 250 ? -18.72557 -66.78227 -56.87083 1.000 134.44554 ? 223 VAL   A CA   1 
ATOM   1686 C  C    . VAL   A 1 250 ? -18.98056 -67.94063 -57.82890 1.000 147.43426 ? 223 VAL   A C    1 
ATOM   1687 O  O    . VAL   A 1 250 ? -19.62708 -68.93223 -57.46508 1.000 149.27800 ? 223 VAL   A O    1 
ATOM   1688 C  CB   . VAL   A 1 250 ? -19.70605 -65.61817 -57.10656 1.000 121.11885 ? 223 VAL   A CB   1 
ATOM   1689 C  CG1  . VAL   A 1 250 ? -21.13396 -66.13355 -57.19575 1.000 129.26959 ? 223 VAL   A CG1  1 
ATOM   1690 C  CG2  . VAL   A 1 250 ? -19.58868 -64.59415 -55.98875 1.000 128.22663 ? 223 VAL   A CG2  1 
ATOM   1691 N  N    . ILE   A 1 251 ? -18.46603 -67.84962 -59.05871 1.000 155.50922 ? 224 ILE   A N    1 
ATOM   1692 C  CA   . ILE   A 1 251 ? -18.68851 -68.92436 -60.02188 1.000 145.16100 ? 224 ILE   A CA   1 
ATOM   1693 C  C    . ILE   A 1 251 ? -17.99609 -70.20555 -59.56856 1.000 149.58395 ? 224 ILE   A C    1 
ATOM   1694 O  O    . ILE   A 1 251 ? -18.53083 -71.30767 -59.73911 1.000 155.36844 ? 224 ILE   A O    1 
ATOM   1695 C  CB   . ILE   A 1 251 ? -18.23221 -68.48923 -61.42678 1.000 144.83640 ? 224 ILE   A CB   1 
ATOM   1696 C  CG1  . ILE   A 1 251 ? -19.13143 -67.36702 -61.95004 1.000 156.77890 ? 224 ILE   A CG1  1 
ATOM   1697 C  CG2  . ILE   A 1 251 ? -18.25123 -69.66665 -62.39007 1.000 129.14901 ? 224 ILE   A CG2  1 
ATOM   1698 C  CD1  . ILE   A 1 251 ? -18.81659 -66.93923 -63.36628 1.000 169.51766 ? 224 ILE   A CD1  1 
ATOM   1699 N  N    . ASP   A 1 252 ? -16.81020 -70.08604 -58.96512 1.000 158.55681 ? 225 ASP   A N    1 
ATOM   1700 C  CA   . ASP   A 1 252 ? -16.11077 -71.26831 -58.47351 1.000 152.83505 ? 225 ASP   A CA   1 
ATOM   1701 C  C    . ASP   A 1 252 ? -16.83905 -71.88960 -57.28920 1.000 157.06343 ? 225 ASP   A C    1 
ATOM   1702 O  O    . ASP   A 1 252 ? -16.93963 -73.11818 -57.19236 1.000 166.77304 ? 225 ASP   A O    1 
ATOM   1703 C  CB   . ASP   A 1 252 ? -14.67375 -70.91060 -58.09231 1.000 160.23643 ? 225 ASP   A CB   1 
ATOM   1704 C  CG   . ASP   A 1 252 ? -13.81013 -70.59752 -59.29951 1.000 194.71343 ? 225 ASP   A CG   1 
ATOM   1705 O  OD1  . ASP   A 1 252 ? -14.31218 -70.71421 -60.43712 1.000 197.76547 ? 225 ASP   A OD1  1 
ATOM   1706 O  OD2  . ASP   A 1 252 ? -12.62928 -70.23489 -59.11135 1.000 241.60803 ? 225 ASP   A OD2  1 
ATOM   1707 N  N    . LYS   A 1 253 ? -17.35490 -71.06070 -56.37755 1.000 153.25047 ? 226 LYS   A N    1 
ATOM   1708 C  CA   . LYS   A 1 253 ? -18.08568 -71.60218 -55.23664 1.000 154.21048 ? 226 LYS   A CA   1 
ATOM   1709 C  C    . LYS   A 1 253 ? -19.41176 -72.22064 -55.66035 1.000 147.71686 ? 226 LYS   A C    1 
ATOM   1710 O  O    . LYS   A 1 253 ? -19.90987 -73.13206 -54.98965 1.000 142.53124 ? 226 LYS   A O    1 
ATOM   1711 C  CB   . LYS   A 1 253 ? -18.31162 -70.51451 -54.18687 1.000 152.17331 ? 226 LYS   A CB   1 
ATOM   1712 C  CG   . LYS   A 1 253 ? -17.03176 -70.02157 -53.53323 1.000 140.99471 ? 226 LYS   A CG   1 
ATOM   1713 C  CD   . LYS   A 1 253 ? -16.21948 -71.18083 -52.97745 1.000 144.26675 ? 226 LYS   A CD   1 
ATOM   1714 C  CE   . LYS   A 1 253 ? -14.88883 -70.70586 -52.41798 1.000 145.96459 ? 226 LYS   A CE   1 
ATOM   1715 N  NZ   . LYS   A 1 253 ? -14.06089 -71.83831 -51.91821 1.000 136.88980 ? 226 LYS   A NZ   1 
ATOM   1716 N  N    . LEU   A 1 254 ? -19.99582 -71.74654 -56.76308 1.000 142.38961 ? 227 LEU   A N    1 
ATOM   1717 C  CA   . LEU   A 1 254 ? -21.22271 -72.35953 -57.26156 1.000 141.17570 ? 227 LEU   A CA   1 
ATOM   1718 C  C    . LEU   A 1 254 ? -20.93927 -73.65326 -58.01731 1.000 138.75666 ? 227 LEU   A C    1 
ATOM   1719 O  O    . LEU   A 1 254 ? -21.71028 -74.61414 -57.91606 1.000 143.11785 ? 227 LEU   A O    1 
ATOM   1720 C  CB   . LEU   A 1 254 ? -21.98045 -71.37485 -58.15203 1.000 150.96203 ? 227 LEU   A CB   1 
ATOM   1721 C  CG   . LEU   A 1 254 ? -22.63919 -70.19900 -57.42911 1.000 126.59259 ? 227 LEU   A CG   1 
ATOM   1722 C  CD1  . LEU   A 1 254 ? -23.33394 -69.28406 -58.42029 1.000 113.49224 ? 227 LEU   A CD1  1 
ATOM   1723 C  CD2  . LEU   A 1 254 ? -23.62003 -70.69818 -56.38062 1.000 138.06583 ? 227 LEU   A CD2  1 
ATOM   1724 N  N    . LYS   A 1 255 ? -19.84332 -73.69821 -58.77916 1.000 145.15555 ? 228 LYS   A N    1 
ATOM   1725 C  CA   . LYS   A 1 255 ? -19.49085 -74.91324 -59.50453 1.000 162.13813 ? 228 LYS   A CA   1 
ATOM   1726 C  C    . LYS   A 1 255 ? -18.92984 -75.99343 -58.59017 1.000 165.31915 ? 228 LYS   A C    1 
ATOM   1727 O  O    . LYS   A 1 255 ? -18.95537 -77.17266 -58.95865 1.000 169.76567 ? 228 LYS   A O    1 
ATOM   1728 C  CB   . LYS   A 1 255 ? -18.48182 -74.60003 -60.61126 1.000 158.03483 ? 228 LYS   A CB   1 
ATOM   1729 C  CG   . LYS   A 1 255 ? -19.07783 -73.91261 -61.83020 1.000 165.82185 ? 228 LYS   A CG   1 
ATOM   1730 C  CD   . LYS   A 1 255 ? -18.02103 -73.68714 -62.90177 1.000 147.28421 ? 228 LYS   A CD   1 
ATOM   1731 C  CE   . LYS   A 1 255 ? -18.61020 -73.02570 -64.13860 1.000 165.31424 ? 228 LYS   A CE   1 
ATOM   1732 N  NZ   . LYS   A 1 255 ? -19.59151 -73.90462 -64.83299 1.000 191.16433 ? 228 LYS   A NZ   1 
ATOM   1733 N  N    . SER   A 1 256 ? -18.42207 -75.62191 -57.41472 1.000 160.89803 ? 229 SER   A N    1 
ATOM   1734 C  CA   . SER   A 1 256 ? -17.89119 -76.57653 -56.45189 1.000 164.48103 ? 229 SER   A CA   1 
ATOM   1735 C  C    . SER   A 1 256 ? -18.89676 -76.91569 -55.35727 1.000 146.46617 ? 229 SER   A C    1 
ATOM   1736 O  O    . SER   A 1 256 ? -18.49939 -77.34354 -54.26847 1.000 145.64710 ? 229 SER   A O    1 
ATOM   1737 C  CB   . SER   A 1 256 ? -16.59653 -76.04465 -55.83489 1.000 180.20263 ? 229 SER   A CB   1 
ATOM   1738 O  OG   . SER   A 1 256 ? -16.83272 -74.86288 -55.09013 1.000 182.32914 ? 229 SER   A OG   1 
ATOM   1739 N  N    . ALA   A 1 257 ? -20.18601 -76.72829 -55.62188 1.000 141.95926 ? 230 ALA   A N    1 
ATOM   1740 C  CA   . ALA   A 1 257 ? -21.21986 -77.08614 -54.66463 1.000 143.04598 ? 230 ALA   A CA   1 
ATOM   1741 C  C    . ALA   A 1 257 ? -21.56172 -78.56598 -54.78072 1.000 154.53535 ? 230 ALA   A C    1 
ATOM   1742 O  O    . ALA   A 1 257 ? -21.53310 -79.14880 -55.86801 1.000 157.70181 ? 230 ALA   A O    1 
ATOM   1743 C  CB   . ALA   A 1 257 ? -22.47361 -76.24104 -54.88674 1.000 135.38232 ? 230 ALA   A CB   1 
ATOM   1744 N  N    . LYS   A 1 258 ? -21.88924 -79.17405 -53.64121 1.000 160.72892 ? 231 LYS   A N    1 
ATOM   1745 C  CA   . LYS   A 1 258 ? -22.18981 -80.60010 -53.60750 1.000 161.47205 ? 231 LYS   A CA   1 
ATOM   1746 C  C    . LYS   A 1 258 ? -23.53736 -80.88302 -52.95675 1.000 166.25076 ? 231 LYS   A C    1 
ATOM   1747 O  O    . LYS   A 1 258 ? -24.21636 -81.84701 -53.32416 1.000 168.08458 ? 231 LYS   A O    1 
ATOM   1748 C  CB   . LYS   A 1 258 ? -21.08972 -81.36571 -52.86559 1.000 166.58437 ? 231 LYS   A CB   1 
ATOM   1749 C  CG   . LYS   A 1 258 ? -19.87487 -81.72742 -53.71185 1.000 182.87402 ? 231 LYS   A CG   1 
ATOM   1750 C  CD   . LYS   A 1 258 ? -18.91464 -80.55813 -53.87004 1.000 204.98006 ? 231 LYS   A CD   1 
ATOM   1751 C  CE   . LYS   A 1 258 ? -17.67736 -80.96349 -54.65821 1.000 193.23723 ? 231 LYS   A CE   1 
ATOM   1752 N  NZ   . LYS   A 1 258 ? -16.71215 -79.83812 -54.79832 1.000 199.49047 ? 231 LYS   A NZ   1 
ATOM   1753 N  N    . THR   A 1 259 ? -23.93507 -80.05309 -51.99299 1.000 173.64934 ? 232 THR   A N    1 
ATOM   1754 C  CA   . THR   A 1 259 ? -25.10703 -80.32666 -51.17089 1.000 175.57661 ? 232 THR   A CA   1 
ATOM   1755 C  C    . THR   A 1 259 ? -26.24237 -79.33954 -51.41362 1.000 160.12212 ? 232 THR   A C    1 
ATOM   1756 O  O    . THR   A 1 259 ? -27.32629 -79.74493 -51.84235 1.000 145.99358 ? 232 THR   A O    1 
ATOM   1757 C  CB   . THR   A 1 259 ? -24.71292 -80.33223 -49.68719 1.000 183.26053 ? 232 THR   A CB   1 
ATOM   1758 O  OG1  . THR   A 1 259 ? -23.64131 -81.26147 -49.48188 1.000 174.41914 ? 232 THR   A OG1  1 
ATOM   1759 C  CG2  . THR   A 1 259 ? -25.89832 -80.73179 -48.82152 1.000 200.72942 ? 232 THR   A CG2  1 
ATOM   1760 N  N    . SER   A 1 260 ? -26.03317 -78.05172 -51.14420 1.000 162.78617 ? 233 SER   A N    1 
ATOM   1761 C  CA   . SER   A 1 260 ? -27.11463 -77.08291 -51.24568 1.000 155.10747 ? 233 SER   A CA   1 
ATOM   1762 C  C    . SER   A 1 260 ? -26.57807 -75.74997 -51.74429 1.000 150.52627 ? 233 SER   A C    1 
ATOM   1763 O  O    . SER   A 1 260 ? -25.41973 -75.39791 -51.50523 1.000 166.59883 ? 233 SER   A O    1 
ATOM   1764 C  CB   . SER   A 1 260 ? -27.81938 -76.88416 -49.89901 1.000 163.12330 ? 233 SER   A CB   1 
ATOM   1765 O  OG   . SER   A 1 260 ? -26.97263 -76.22669 -48.97176 1.000 159.31875 ? 233 SER   A OG   1 
ATOM   1766 N  N    . ILE   A 1 261 ? -27.44242 -75.01290 -52.43852 1.000 129.26235 ? 234 ILE   A N    1 
ATOM   1767 C  CA   . ILE   A 1 261 ? -27.17589 -73.64356 -52.86348 1.000 137.98212 ? 234 ILE   A CA   1 
ATOM   1768 C  C    . ILE   A 1 261 ? -28.39885 -72.81143 -52.50852 1.000 150.61909 ? 234 ILE   A C    1 
ATOM   1769 O  O    . ILE   A 1 261 ? -29.50359 -73.09290 -52.98723 1.000 144.40069 ? 234 ILE   A O    1 
ATOM   1770 C  CB   . ILE   A 1 261 ? -26.87628 -73.54362 -54.36867 1.000 138.38301 ? 234 ILE   A CB   1 
ATOM   1771 C  CG1  . ILE   A 1 261 ? -25.58843 -74.29087 -54.71733 1.000 138.90104 ? 234 ILE   A CG1  1 
ATOM   1772 C  CG2  . ILE   A 1 261 ? -26.78077 -72.08551 -54.79599 1.000 124.41069 ? 234 ILE   A CG2  1 
ATOM   1773 C  CD1  . ILE   A 1 261 ? -25.19481 -74.16877 -56.17246 1.000 151.10140 ? 234 ILE   A CD1  1 
ATOM   1774 N  N    . ASP   A 1 262 ? -28.20779 -71.79472 -51.67267 1.000 159.47474 ? 235 ASP   A N    1 
ATOM   1775 C  CA   . ASP   A 1 262 ? -29.29371 -70.93488 -51.21302 1.000 152.65879 ? 235 ASP   A CA   1 
ATOM   1776 C  C    . ASP   A 1 262 ? -28.94817 -69.49616 -51.57029 1.000 142.20767 ? 235 ASP   A C    1 
ATOM   1777 O  O    . ASP   A 1 262 ? -28.00285 -68.92578 -51.01690 1.000 148.86123 ? 235 ASP   A O    1 
ATOM   1778 C  CB   . ASP   A 1 262 ? -29.50959 -71.09245 -49.71005 1.000 157.00094 ? 235 ASP   A CB   1 
ATOM   1779 C  CG   . ASP   A 1 262 ? -29.78208 -72.52779 -49.30945 1.000 162.55638 ? 235 ASP   A CG   1 
ATOM   1780 O  OD1  . ASP   A 1 262 ? -30.47530 -73.24003 -50.06622 1.000 152.80978 ? 235 ASP   A OD1  1 
ATOM   1781 O  OD2  . ASP   A 1 262 ? -29.29756 -72.94582 -48.23863 1.000 160.99232 ? 235 ASP   A OD2  1 
ATOM   1782 N  N    . ILE   A 1 263 ? -29.70981 -68.90761 -52.48799 1.000 119.91483 ? 236 ILE   A N    1 
ATOM   1783 C  CA   . ILE   A 1 263 ? -29.43604 -67.56719 -52.99001 1.000 123.44479 ? 236 ILE   A CA   1 
ATOM   1784 C  C    . ILE   A 1 263 ? -30.64705 -66.68474 -52.73041 1.000 127.31916 ? 236 ILE   A C    1 
ATOM   1785 O  O    . ILE   A 1 263 ? -31.76566 -67.01720 -53.13974 1.000 128.29906 ? 236 ILE   A O    1 
ATOM   1786 C  CB   . ILE   A 1 263 ? -29.08422 -67.58130 -54.48787 1.000 122.63734 ? 236 ILE   A CB   1 
ATOM   1787 C  CG1  . ILE   A 1 263 ? -27.93547 -68.55522 -54.74730 1.000 134.41194 ? 236 ILE   A CG1  1 
ATOM   1788 C  CG2  . ILE   A 1 263 ? -28.72007 -66.18207 -54.95905 1.000 123.29728 ? 236 ILE   A CG2  1 
ATOM   1789 C  CD1  . ILE   A 1 263 ? -27.37582 -68.48409 -56.14172 1.000 143.02498 ? 236 ILE   A CD1  1 
ATOM   1790 N  N    . GLU   A 1 264 ? -30.41948 -65.56424 -52.05073 1.000 123.93963 ? 237 GLU   A N    1 
ATOM   1791 C  CA   . GLU   A 1 264 ? -31.42586 -64.52961 -51.83287 1.000 114.07441 ? 237 GLU   A CA   1 
ATOM   1792 C  C    . GLU   A 1 264 ? -30.87382 -63.24151 -52.43670 1.000 125.79863 ? 237 GLU   A C    1 
ATOM   1793 O  O    . GLU   A 1 264 ? -30.19071 -62.46589 -51.76259 1.000 139.63904 ? 237 GLU   A O    1 
ATOM   1794 C  CB   . GLU   A 1 264 ? -31.75499 -64.36187 -50.34984 1.000 113.97929 ? 237 GLU   A CB   1 
ATOM   1795 C  CG   . GLU   A 1 264 ? -32.77210 -63.26434 -50.07113 1.000 121.38679 ? 237 GLU   A CG   1 
ATOM   1796 C  CD   . GLU   A 1 264 ? -33.04230 -63.07567 -48.59268 1.000 137.57326 ? 237 GLU   A CD   1 
ATOM   1797 O  OE1  . GLU   A 1 264 ? -32.77550 -64.01462 -47.81420 1.000 165.04831 ? 237 GLU   A OE1  1 
ATOM   1798 O  OE2  . GLU   A 1 264 ? -33.51818 -61.98616 -48.20854 1.000 111.80002 ? 237 GLU   A OE2  1 
ATOM   1799 N  N    . HIS   A 1 265 ? -31.15491 -63.03133 -53.71619 1.000 116.86338 ? 238 HIS   A N    1 
ATOM   1800 C  CA   . HIS   A 1 265 ? -30.80848 -61.81104 -54.42952 1.000 136.22462 ? 238 HIS   A CA   1 
ATOM   1801 C  C    . HIS   A 1 265 ? -32.07550 -61.21694 -55.03753 1.000 131.33216 ? 238 HIS   A C    1 
ATOM   1802 O  O    . HIS   A 1 265 ? -33.17609 -61.75052 -54.87906 1.000 133.01334 ? 238 HIS   A O    1 
ATOM   1803 C  CB   . HIS   A 1 265 ? -29.74524 -62.08227 -55.49958 1.000 144.43642 ? 238 HIS   A CB   1 
ATOM   1804 C  CG   . HIS   A 1 265 ? -28.34454 -62.10730 -54.96858 1.000 144.73942 ? 238 HIS   A CG   1 
ATOM   1805 N  ND1  . HIS   A 1 265 ? -27.34661 -61.29463 -55.46273 1.000 130.93072 ? 238 HIS   A ND1  1 
ATOM   1806 C  CD2  . HIS   A 1 265 ? -27.77685 -62.84146 -53.98235 1.000 146.37917 ? 238 HIS   A CD2  1 
ATOM   1807 C  CE1  . HIS   A 1 265 ? -26.22388 -61.53066 -54.80768 1.000 140.57336 ? 238 HIS   A CE1  1 
ATOM   1808 N  NE2  . HIS   A 1 265 ? -26.45823 -62.46361 -53.90249 1.000 139.86790 ? 238 HIS   A NE2  1 
ATOM   1809 N  N    . LEU   A 1 266 ? -31.91393 -60.09450 -55.73939 1.000 139.67107 ? 239 LEU   A N    1 
ATOM   1810 C  CA   . LEU   A 1 266 ? -33.07141 -59.41574 -56.31300 1.000 124.22211 ? 239 LEU   A CA   1 
ATOM   1811 C  C    . LEU   A 1 266 ? -33.64503 -60.20508 -57.48480 1.000 139.84378 ? 239 LEU   A C    1 
ATOM   1812 O  O    . LEU   A 1 266 ? -34.84904 -60.48521 -57.52779 1.000 137.29801 ? 239 LEU   A O    1 
ATOM   1813 C  CB   . LEU   A 1 266 ? -32.68639 -57.99939 -56.74128 1.000 118.69359 ? 239 LEU   A CB   1 
ATOM   1814 C  CG   . LEU   A 1 266 ? -33.84124 -57.02478 -56.97470 1.000 119.10940 ? 239 LEU   A CG   1 
ATOM   1815 C  CD1  . LEU   A 1 266 ? -34.76236 -56.99477 -55.76514 1.000 139.94327 ? 239 LEU   A CD1  1 
ATOM   1816 C  CD2  . LEU   A 1 266 ? -33.30952 -55.63273 -57.27722 1.000 153.45958 ? 239 LEU   A CD2  1 
ATOM   1817 N  N    . ALA   A 1 267 ? -32.79684 -60.57656 -58.44149 1.000 119.13192 ? 240 ALA   A N    1 
ATOM   1818 C  CA   . ALA   A 1 267 ? -33.21840 -61.37442 -59.58440 1.000 133.18469 ? 240 ALA   A CA   1 
ATOM   1819 C  C    . ALA   A 1 267 ? -31.98652 -62.00078 -60.21906 1.000 123.47395 ? 240 ALA   A C    1 
ATOM   1820 O  O    . ALA   A 1 267 ? -30.88286 -61.45648 -60.12820 1.000 127.07160 ? 240 ALA   A O    1 
ATOM   1821 C  CB   . ALA   A 1 267 ? -33.98560 -60.53609 -60.61390 1.000 138.81705 ? 240 ALA   A CB   1 
ATOM   1822 N  N    . ILE   A 1 268 ? -32.18635 -63.15446 -60.85738 1.000 129.04330 ? 241 ILE   A N    1 
ATOM   1823 C  CA   . ILE   A 1 268 ? -31.08691 -63.88379 -61.48232 1.000 118.92910 ? 241 ILE   A CA   1 
ATOM   1824 C  C    . ILE   A 1 268 ? -31.36086 -64.05313 -62.97409 1.000 130.39294 ? 241 ILE   A C    1 
ATOM   1825 O  O    . ILE   A 1 268 ? -31.00514 -65.07610 -63.57242 1.000 124.29621 ? 241 ILE   A O    1 
ATOM   1826 C  CB   . ILE   A 1 268 ? -30.86111 -65.24677 -60.79836 1.000 100.75131 ? 241 ILE   A CB   1 
ATOM   1827 C  CG1  . ILE   A 1 268 ? -31.12691 -65.15128 -59.29364 1.000 140.95030 ? 241 ILE   A CG1  1 
ATOM   1828 C  CG2  . ILE   A 1 268 ? -29.42809 -65.72785 -61.01744 1.000 143.85070 ? 241 ILE   A CG2  1 
ATOM   1829 C  CD1  . ILE   A 1 268 ? -30.08656 -64.34813 -58.53299 1.000 152.08807 ? 241 ILE   A CD1  1 
ATOM   1830 N  N    . VAL   A 1 269 ? -31.99677 -63.05528 -63.58255 1.000 141.34813 ? 242 VAL   A N    1 
ATOM   1831 C  CA   . VAL   A 1 269 ? -32.18171 -63.08787 -65.03804 1.000 118.59633 ? 242 VAL   A CA   1 
ATOM   1832 C  C    . VAL   A 1 269 ? -30.81987 -62.99484 -65.70543 1.000 138.29019 ? 242 VAL   A C    1 
ATOM   1833 O  O    . VAL   A 1 269 ? -30.02787 -62.09197 -65.37535 1.000 162.26975 ? 242 VAL   A O    1 
ATOM   1834 C  CB   . VAL   A 1 269 ? -33.08664 -61.93543 -65.50449 1.000 144.56021 ? 242 VAL   A CB   1 
ATOM   1835 C  CG1  . VAL   A 1 269 ? -33.31009 -62.02353 -67.00971 1.000 160.63363 ? 242 VAL   A CG1  1 
ATOM   1836 C  CG2  . VAL   A 1 269 ? -34.40668 -61.95133 -64.75978 1.000 142.75801 ? 242 VAL   A CG2  1 
ATOM   1837 N  N    . PRO   A 1 270 ? -30.48949 -63.88742 -66.64280 1.000 134.11052 ? 243 PRO   A N    1 
ATOM   1838 C  CA   . PRO   A 1 270 ? -29.20394 -63.80129 -67.34271 1.000 138.59367 ? 243 PRO   A CA   1 
ATOM   1839 C  C    . PRO   A 1 270 ? -29.09712 -62.64915 -68.32803 1.000 151.24636 ? 243 PRO   A C    1 
ATOM   1840 O  O    . PRO   A 1 270 ? -28.12161 -62.59809 -69.08259 1.000 157.56348 ? 243 PRO   A O    1 
ATOM   1841 C  CB   . PRO   A 1 270 ? -29.13813 -65.15307 -68.07511 1.000 130.88613 ? 243 PRO   A CB   1 
ATOM   1842 C  CG   . PRO   A 1 270 ? -30.56867 -65.48266 -68.33146 1.000 134.07586 ? 243 PRO   A CG   1 
ATOM   1843 C  CD   . PRO   A 1 270 ? -31.29601 -65.03257 -67.09430 1.000 147.01763 ? 243 PRO   A CD   1 
ATOM   1844 N  N    . THR   A 1 271 ? -30.06224 -61.72941 -68.35427 1.000 142.38098 ? 244 THR   A N    1 
ATOM   1845 C  CA   . THR   A 1 271 ? -30.04638 -60.60649 -69.28409 1.000 147.60383 ? 244 THR   A CA   1 
ATOM   1846 C  C    . THR   A 1 271 ? -30.41864 -59.33683 -68.53818 1.000 155.64831 ? 244 THR   A C    1 
ATOM   1847 O  O    . THR   A 1 271 ? -31.46583 -59.28079 -67.88711 1.000 156.40641 ? 244 THR   A O    1 
ATOM   1848 C  CB   . THR   A 1 271 ? -31.01104 -60.83940 -70.44858 1.000 144.46021 ? 244 THR   A CB   1 
ATOM   1849 O  OG1  . THR   A 1 271 ? -30.60457 -62.00006 -71.18661 1.000 167.37444 ? 244 THR   A OG1  1 
ATOM   1850 C  CG2  . THR   A 1 271 ? -31.02507 -59.63535 -71.36518 1.000 157.65278 ? 244 THR   A CG2  1 
ATOM   1851 N  N    . THR   A 1 272 ? -29.55454 -58.33589 -68.61669 1.000 154.22914 ? 245 THR   A N    1 
ATOM   1852 C  CA   . THR   A 1 272 ? -29.83616 -57.00984 -68.09092 1.000 146.68212 ? 245 THR   A CA   1 
ATOM   1853 C  C    . THR   A 1 272 ? -30.11712 -56.05704 -69.25002 1.000 156.94627 ? 245 THR   A C    1 
ATOM   1854 O  O    . THR   A 1 272 ? -30.08104 -56.43469 -70.42346 1.000 168.84374 ? 245 THR   A O    1 
ATOM   1855 C  CB   . THR   A 1 272 ? -28.67563 -56.50620 -67.22896 1.000 138.21256 ? 245 THR   A CB   1 
ATOM   1856 O  OG1  . THR   A 1 272 ? -27.52152 -56.29217 -68.05099 1.000 161.20341 ? 245 THR   A OG1  1 
ATOM   1857 C  CG2  . THR   A 1 272 ? -28.33908 -57.52237 -66.14848 1.000 127.09775 ? 245 THR   A CG2  1 
ATOM   1858 N  N    . ARG   A 1 273 ? -30.39586 -54.80011 -68.91679 1.000 152.47660 ? 246 ARG   A N    1 
ATOM   1859 C  CA   . ARG   A 1 273 ? -30.62576 -53.76951 -69.92454 1.000 172.78306 ? 246 ARG   A CA   1 
ATOM   1860 C  C    . ARG   A 1 273 ? -29.74652 -52.57091 -69.60011 1.000 175.61849 ? 246 ARG   A C    1 
ATOM   1861 O  O    . ARG   A 1 273 ? -30.02317 -51.83165 -68.64959 1.000 169.20904 ? 246 ARG   A O    1 
ATOM   1862 C  CB   . ARG   A 1 273 ? -32.10035 -53.36905 -69.99099 1.000 168.69337 ? 246 ARG   A CB   1 
ATOM   1863 C  CG   . ARG   A 1 273 ? -32.42435 -52.42344 -71.14214 1.000 166.18244 ? 246 ARG   A CG   1 
ATOM   1864 C  CD   . ARG   A 1 273 ? -33.92219 -52.30206 -71.36371 1.000 176.75281 ? 246 ARG   A CD   1 
ATOM   1865 N  NE   . ARG   A 1 273 ? -34.23478 -51.40082 -72.46636 1.000 195.25465 ? 246 ARG   A NE   1 
ATOM   1866 C  CZ   . ARG   A 1 273 ? -34.27559 -51.76242 -73.74156 1.000 194.11867 ? 246 ARG   A CZ   1 
ATOM   1867 N  NH1  . ARG   A 1 273 ? -34.02294 -53.00595 -74.11621 1.000 173.86984 ? 246 ARG   A NH1  1 
ATOM   1868 N  NH2  . ARG   A 1 273 ? -34.57663 -50.85325 -74.66436 1.000 201.07139 ? 246 ARG   A NH2  1 
ATOM   1869 N  N    . VAL   A 1 274 ? -28.69071 -52.38117 -70.38744 1.000 193.60703 ? 247 VAL   A N    1 
ATOM   1870 C  CA   . VAL   A 1 274 ? -27.79111 -51.24430 -70.23934 1.000 193.94556 ? 247 VAL   A CA   1 
ATOM   1871 C  C    . VAL   A 1 274 ? -28.20688 -50.18149 -71.24522 1.000 206.26620 ? 247 VAL   A C    1 
ATOM   1872 O  O    . VAL   A 1 274 ? -28.31685 -50.46150 -72.44671 1.000 211.42329 ? 247 VAL   A O    1 
ATOM   1873 C  CB   . VAL   A 1 274 ? -26.32173 -51.65968 -70.43264 1.000 173.51534 ? 247 VAL   A CB   1 
ATOM   1874 C  CG1  . VAL   A 1 274 ? -25.81202 -52.37343 -69.19180 1.000 145.44462 ? 247 VAL   A CG1  1 
ATOM   1875 C  CG2  . VAL   A 1 274 ? -26.16800 -52.55445 -71.65692 1.000 165.74476 ? 247 VAL   A CG2  1 
ATOM   1876 N  N    . ASP   A 1 275 ? -28.45081 -48.96559 -70.75178 1.000 188.14059 ? 248 ASP   A N    1 
ATOM   1877 C  CA   . ASP   A 1 275 ? -29.01147 -47.88820 -71.56008 1.000 216.03714 ? 248 ASP   A CA   1 
ATOM   1878 C  C    . ASP   A 1 275 ? -30.29858 -48.34913 -72.23239 1.000 215.16154 ? 248 ASP   A C    1 
ATOM   1879 O  O    . ASP   A 1 275 ? -31.29291 -48.63022 -71.55558 1.000 187.64161 ? 248 ASP   A O    1 
ATOM   1880 C  CB   . ASP   A 1 275 ? -28.00129 -47.40281 -72.60352 1.000 232.86305 ? 248 ASP   A CB   1 
ATOM   1881 C  CG   . ASP   A 1 275 ? -26.75670 -46.80868 -71.97668 1.000 231.61292 ? 248 ASP   A CG   1 
ATOM   1882 O  OD1  . ASP   A 1 275 ? -26.86271 -46.23072 -70.87485 1.000 237.06729 ? 248 ASP   A OD1  1 
ATOM   1883 O  OD2  . ASP   A 1 275 ? -25.67183 -46.91934 -72.58524 1.000 229.97281 ? 248 ASP   A OD2  1 
ATOM   1884 N  N    . GLY   A 1 276 ? -30.28654 -48.43945 -73.55926 1.000 224.71178 ? 249 GLY   A N    1 
ATOM   1885 C  CA   . GLY   A 1 276 ? -31.44014 -48.92250 -74.29085 1.000 211.44571 ? 249 GLY   A CA   1 
ATOM   1886 C  C    . GLY   A 1 276 ? -31.15738 -50.19332 -75.06500 1.000 203.51571 ? 249 GLY   A C    1 
ATOM   1887 O  O    . GLY   A 1 276 ? -31.79345 -50.45743 -76.08987 1.000 205.28449 ? 249 GLY   A O    1 
ATOM   1888 N  N    . ASN   A 1 277 ? -30.20530 -50.99165 -74.58398 1.000 196.08044 ? 250 ASN   A N    1 
ATOM   1889 C  CA   . ASN   A 1 277 ? -29.80130 -52.22000 -75.25284 1.000 193.92284 ? 250 ASN   A CA   1 
ATOM   1890 C  C    . ASN   A 1 277 ? -29.71245 -53.35881 -74.24743 1.000 182.46966 ? 250 ASN   A C    1 
ATOM   1891 O  O    . ASN   A 1 277 ? -29.19334 -53.18725 -73.13969 1.000 174.38909 ? 250 ASN   A O    1 
ATOM   1892 C  CB   . ASN   A 1 277 ? -28.45388 -52.04916 -75.96778 1.000 187.35484 ? 250 ASN   A CB   1 
ATOM   1893 C  CG   . ASN   A 1 277 ? -28.50671 -51.00967 -77.07067 1.000 213.73003 ? 250 ASN   A CG   1 
ATOM   1894 O  OD1  . ASN   A 1 277 ? -28.85744 -51.31390 -78.21123 1.000 210.05903 ? 250 ASN   A OD1  1 
ATOM   1895 N  ND2  . ASN   A 1 277 ? -28.15608 -49.77381 -76.73536 1.000 226.28717 ? 250 ASN   A ND2  1 
ATOM   1896 N  N    . SER   A 1 278 ? -30.20980 -54.52542 -74.64832 1.000 186.14021 ? 251 SER   A N    1 
ATOM   1897 C  CA   . SER   A 1 278 ? -30.18261 -55.70081 -73.79126 1.000 151.18206 ? 251 SER   A CA   1 
ATOM   1898 C  C    . SER   A 1 278 ? -28.81404 -56.36666 -73.84072 1.000 147.14225 ? 251 SER   A C    1 
ATOM   1899 O  O    . SER   A 1 278 ? -28.19315 -56.46882 -74.90227 1.000 170.41014 ? 251 SER   A O    1 
ATOM   1900 C  CB   . SER   A 1 278 ? -31.26281 -56.69343 -74.21653 1.000 163.33700 ? 251 SER   A CB   1 
ATOM   1901 O  OG   . SER   A 1 278 ? -32.53741 -56.07618 -74.23539 1.000 168.18047 ? 251 SER   A OG   1 
ATOM   1902 N  N    . TYR   A 1 279 ? -28.35167 -56.82880 -72.68215 1.000 127.85916 ? 252 TYR   A N    1 
ATOM   1903 C  CA   . TYR   A 1 279 ? -27.03464 -57.43286 -72.52821 1.000 153.64716 ? 252 TYR   A CA   1 
ATOM   1904 C  C    . TYR   A 1 279 ? -27.20108 -58.81611 -71.91614 1.000 160.14456 ? 252 TYR   A C    1 
ATOM   1905 O  O    . TYR   A 1 279 ? -27.78434 -58.95467 -70.83527 1.000 162.23705 ? 252 TYR   A O    1 
ATOM   1906 C  CB   . TYR   A 1 279 ? -26.13479 -56.55203 -71.65899 1.000 176.38758 ? 252 TYR   A CB   1 
ATOM   1907 C  CG   . TYR   A 1 279 ? -24.76364 -57.12822 -71.38929 1.000 189.88560 ? 252 TYR   A CG   1 
ATOM   1908 C  CD1  . TYR   A 1 279 ? -23.78988 -57.14994 -72.37899 1.000 194.60656 ? 252 TYR   A CD1  1 
ATOM   1909 C  CD2  . TYR   A 1 279 ? -24.43724 -57.63520 -70.13853 1.000 187.51516 ? 252 TYR   A CD2  1 
ATOM   1910 C  CE1  . TYR   A 1 279 ? -22.53221 -57.67176 -72.13331 1.000 202.68591 ? 252 TYR   A CE1  1 
ATOM   1911 C  CE2  . TYR   A 1 279 ? -23.18362 -58.15740 -69.88343 1.000 180.79369 ? 252 TYR   A CE2  1 
ATOM   1912 C  CZ   . TYR   A 1 279 ? -22.23479 -58.17344 -70.88385 1.000 198.89976 ? 252 TYR   A CZ   1 
ATOM   1913 O  OH   . TYR   A 1 279 ? -20.98455 -58.69271 -70.63418 1.000 187.94265 ? 252 TYR   A OH   1 
ATOM   1914 N  N    . TYR   A 1 280 ? -26.68374 -59.83114 -72.60320 1.000 157.54558 ? 253 TYR   A N    1 
ATOM   1915 C  CA   . TYR   A 1 280 ? -26.84316 -61.22502 -72.20845 1.000 150.15728 ? 253 TYR   A CA   1 
ATOM   1916 C  C    . TYR   A 1 280 ? -25.58129 -61.69764 -71.49414 1.000 159.33831 ? 253 TYR   A C    1 
ATOM   1917 O  O    . TYR   A 1 280 ? -24.47616 -61.58445 -72.03582 1.000 160.85980 ? 253 TYR   A O    1 
ATOM   1918 C  CB   . TYR   A 1 280 ? -27.13898 -62.09071 -73.43339 1.000 143.05782 ? 253 TYR   A CB   1 
ATOM   1919 C  CG   . TYR   A 1 280 ? -27.28432 -63.56704 -73.14649 1.000 153.84629 ? 253 TYR   A CG   1 
ATOM   1920 C  CD1  . TYR   A 1 280 ? -28.27009 -64.03553 -72.28919 1.000 162.22712 ? 253 TYR   A CD1  1 
ATOM   1921 C  CD2  . TYR   A 1 280 ? -26.44908 -64.49527 -73.75336 1.000 143.15284 ? 253 TYR   A CD2  1 
ATOM   1922 C  CE1  . TYR   A 1 280 ? -28.40776 -65.38647 -72.03032 1.000 145.52002 ? 253 TYR   A CE1  1 
ATOM   1923 C  CE2  . TYR   A 1 280 ? -26.58111 -65.84728 -73.50279 1.000 128.67816 ? 253 TYR   A CE2  1 
ATOM   1924 C  CZ   . TYR   A 1 280 ? -27.56527 -66.28747 -72.64285 1.000 135.15510 ? 253 TYR   A CZ   1 
ATOM   1925 O  OH   . TYR   A 1 280 ? -27.70221 -67.63290 -72.38608 1.000 139.19734 ? 253 TYR   A OH   1 
ATOM   1926 N  N    . TRP   A 1 281 ? -25.75074 -62.22879 -70.28426 1.000 147.60342 ? 254 TRP   A N    1 
ATOM   1927 C  CA   . TRP   A 1 281 ? -24.62324 -62.65712 -69.45555 1.000 155.61289 ? 254 TRP   A CA   1 
ATOM   1928 C  C    . TRP   A 1 281 ? -25.10574 -63.77487 -68.54442 1.000 158.74529 ? 254 TRP   A C    1 
ATOM   1929 O  O    . TRP   A 1 281 ? -25.59079 -63.52908 -67.43134 1.000 171.86920 ? 254 TRP   A O    1 
ATOM   1930 C  CB   . TRP   A 1 281 ? -24.05462 -61.49367 -68.64533 1.000 165.16065 ? 254 TRP   A CB   1 
ATOM   1931 C  CG   . TRP   A 1 281 ? -22.72043 -61.75634 -68.01493 1.000 148.45233 ? 254 TRP   A CG   1 
ATOM   1932 C  CD1  . TRP   A 1 281 ? -21.49599 -61.61189 -68.59890 1.000 156.12057 ? 254 TRP   A CD1  1 
ATOM   1933 C  CD2  . TRP   A 1 281 ? -22.47533 -62.18700 -66.67072 1.000 153.19570 ? 254 TRP   A CD2  1 
ATOM   1934 N  NE1  . TRP   A 1 281 ? -20.50400 -61.93538 -67.70531 1.000 160.41817 ? 254 TRP   A NE1  1 
ATOM   1935 C  CE2  . TRP   A 1 281 ? -21.07935 -62.29137 -66.51384 1.000 156.26389 ? 254 TRP   A CE2  1 
ATOM   1936 C  CE3  . TRP   A 1 281 ? -23.30109 -62.49997 -65.58640 1.000 165.58416 ? 254 TRP   A CE3  1 
ATOM   1937 C  CZ2  . TRP   A 1 281 ? -20.49111 -62.69454 -65.31668 1.000 163.30623 ? 254 TRP   A CZ2  1 
ATOM   1938 C  CZ3  . TRP   A 1 281 ? -22.71552 -62.89926 -64.39936 1.000 154.77178 ? 254 TRP   A CZ3  1 
ATOM   1939 C  CH2  . TRP   A 1 281 ? -21.32418 -62.99372 -64.27410 1.000 134.35334 ? 254 TRP   A CH2  1 
ATOM   1940 N  N    . PRO   A 1 282 ? -24.99595 -65.02836 -68.98984 1.000 148.22364 ? 255 PRO   A N    1 
ATOM   1941 C  CA   . PRO   A 1 282 ? -25.61710 -66.13206 -68.24909 1.000 148.68733 ? 255 PRO   A CA   1 
ATOM   1942 C  C    . PRO   A 1 282 ? -24.64121 -66.95295 -67.42213 1.000 139.70488 ? 255 PRO   A C    1 
ATOM   1943 O  O    . PRO   A 1 282 ? -24.89261 -68.13595 -67.17421 1.000 161.00573 ? 255 PRO   A O    1 
ATOM   1944 C  CB   . PRO   A 1 282 ? -26.21424 -66.97873 -69.37393 1.000 159.72089 ? 255 PRO   A CB   1 
ATOM   1945 C  CG   . PRO   A 1 282 ? -25.15547 -66.86588 -70.44680 1.000 144.71859 ? 255 PRO   A CG   1 
ATOM   1946 C  CD   . PRO   A 1 282 ? -24.57078 -65.46018 -70.33278 1.000 145.98801 ? 255 PRO   A CD   1 
ATOM   1947 N  N    . ASP   A 1 283 ? -23.53162 -66.35058 -66.99314 1.000 141.99309 ? 256 ASP   A N    1 
ATOM   1948 C  CA   . ASP   A 1 283 ? -22.48468 -67.11547 -66.32101 1.000 167.11440 ? 256 ASP   A CA   1 
ATOM   1949 C  C    . ASP   A 1 283 ? -22.99473 -67.73292 -65.02182 1.000 150.91644 ? 256 ASP   A C    1 
ATOM   1950 O  O    . ASP   A 1 283 ? -22.94658 -68.95553 -64.83752 1.000 167.12987 ? 256 ASP   A O    1 
ATOM   1951 C  CB   . ASP   A 1 283 ? -21.26937 -66.22082 -66.07122 1.000 151.43635 ? 256 ASP   A CB   1 
ATOM   1952 C  CG   . ASP   A 1 283 ? -20.60015 -65.78037 -67.36114 1.000 150.82546 ? 256 ASP   A CG   1 
ATOM   1953 O  OD1  . ASP   A 1 283 ? -21.03194 -66.24062 -68.43974 1.000 157.22447 ? 256 ASP   A OD1  1 
ATOM   1954 O  OD2  . ASP   A 1 283 ? -19.64576 -64.97707 -67.29976 1.000 163.06580 ? 256 ASP   A OD2  1 
ATOM   1955 N  N    . ILE   A 1 284 ? -23.49890 -66.89921 -64.11005 1.000 129.75376 ? 257 ILE   A N    1 
ATOM   1956 C  CA   . ILE   A 1 284 ? -24.02994 -67.41104 -62.84982 1.000 141.54772 ? 257 ILE   A CA   1 
ATOM   1957 C  C    . ILE   A 1 284 ? -25.27107 -68.26052 -63.09788 1.000 146.34877 ? 257 ILE   A C    1 
ATOM   1958 O  O    . ILE   A 1 284 ? -25.46298 -69.30830 -62.46700 1.000 153.29124 ? 257 ILE   A O    1 
ATOM   1959 C  CB   . ILE   A 1 284 ? -24.31884 -66.24350 -61.89001 1.000 121.45826 ? 257 ILE   A CB   1 
ATOM   1960 C  CG1  . ILE   A 1 284 ? -23.04360 -65.43461 -61.64565 1.000 118.80264 ? 257 ILE   A CG1  1 
ATOM   1961 C  CG2  . ILE   A 1 284 ? -24.88985 -66.75310 -60.58003 1.000 133.31723 ? 257 ILE   A CG2  1 
ATOM   1962 C  CD1  . ILE   A 1 284 ? -23.22731 -64.27893 -60.69220 1.000 129.27970 ? 257 ILE   A CD1  1 
ATOM   1963 N  N    . TYR   A 1 285 ? -26.13028 -67.81751 -64.01761 1.000 124.32816 ? 258 TYR   A N    1 
ATOM   1964 C  CA   . TYR   A 1 285 ? -27.31207 -68.58153 -64.40615 1.000 128.08102 ? 258 TYR   A CA   1 
ATOM   1965 C  C    . TYR   A 1 285 ? -26.94214 -70.00661 -64.80972 1.000 143.29525 ? 258 TYR   A C    1 
ATOM   1966 O  O    . TYR   A 1 285 ? -27.47692 -70.98592 -64.26877 1.000 142.65923 ? 258 TYR   A O    1 
ATOM   1967 C  CB   . TYR   A 1 285 ? -28.00917 -67.84289 -65.55217 1.000 126.49351 ? 258 TYR   A CB   1 
ATOM   1968 C  CG   . TYR   A 1 285 ? -29.37381 -68.35038 -65.95468 1.000 118.54706 ? 258 TYR   A CG   1 
ATOM   1969 C  CD1  . TYR   A 1 285 ? -30.49394 -68.08254 -65.17970 1.000 113.51563 ? 258 TYR   A CD1  1 
ATOM   1970 C  CD2  . TYR   A 1 285 ? -29.54957 -69.05505 -67.13805 1.000 154.11417 ? 258 TYR   A CD2  1 
ATOM   1971 C  CE1  . TYR   A 1 285 ? -31.74790 -68.52981 -65.55725 1.000 127.83159 ? 258 TYR   A CE1  1 
ATOM   1972 C  CE2  . TYR   A 1 285 ? -30.79760 -69.50303 -67.52464 1.000 163.61837 ? 258 TYR   A CE2  1 
ATOM   1973 C  CZ   . TYR   A 1 285 ? -31.89342 -69.23972 -66.73046 1.000 145.42954 ? 258 TYR   A CZ   1 
ATOM   1974 O  OH   . TYR   A 1 285 ? -33.13885 -69.68612 -67.11170 1.000 147.32038 ? 258 TYR   A OH   1 
ATOM   1975 N  N    . ASN   A 1 286 ? -25.99986 -70.13772 -65.74683 1.000 143.09572 ? 259 ASN   A N    1 
ATOM   1976 C  CA   . ASN   A 1 286 ? -25.62400 -71.45679 -66.24000 1.000 133.11504 ? 259 ASN   A CA   1 
ATOM   1977 C  C    . ASN   A 1 286 ? -24.85898 -72.26071 -65.19895 1.000 141.94792 ? 259 ASN   A C    1 
ATOM   1978 O  O    . ASN   A 1 286 ? -24.99007 -73.48624 -65.16072 1.000 158.96975 ? 259 ASN   A O    1 
ATOM   1979 C  CB   . ASN   A 1 286 ? -24.80249 -71.32973 -67.52093 1.000 146.34731 ? 259 ASN   A CB   1 
ATOM   1980 C  CG   . ASN   A 1 286 ? -25.62163 -70.81371 -68.68309 1.000 146.76218 ? 259 ASN   A CG   1 
ATOM   1981 O  OD1  . ASN   A 1 286 ? -25.16089 -69.98026 -69.46043 1.000 165.38383 ? 259 ASN   A OD1  1 
ATOM   1982 N  ND2  . ASN   A 1 286 ? -26.85108 -71.30231 -68.80237 1.000 145.86113 ? 259 ASN   A ND2  1 
ATOM   1983 N  N    . SER   A 1 287 ? -24.06363 -71.60708 -64.34792 1.000 144.02137 ? 260 SER   A N    1 
ATOM   1984 C  CA   . SER   A 1 287 ? -23.39223 -72.34621 -63.28254 1.000 147.07666 ? 260 SER   A CA   1 
ATOM   1985 C  C    . SER   A 1 287 ? -24.40611 -72.95249 -62.31866 1.000 150.54890 ? 260 SER   A C    1 
ATOM   1986 O  O    . SER   A 1 287 ? -24.27097 -74.11236 -61.90622 1.000 149.89229 ? 260 SER   A O    1 
ATOM   1987 C  CB   . SER   A 1 287 ? -22.41270 -71.43619 -62.54034 1.000 139.02175 ? 260 SER   A CB   1 
ATOM   1988 O  OG   . SER   A 1 287 ? -23.09106 -70.40307 -61.84835 1.000 149.63283 ? 260 SER   A OG   1 
ATOM   1989 N  N    . ILE   A 1 288 ? -25.44869 -72.19360 -61.97340 1.000 148.21987 ? 261 ILE   A N    1 
ATOM   1990 C  CA   . ILE   A 1 288 ? -26.47187 -72.71390 -61.07143 1.000 141.95913 ? 261 ILE   A CA   1 
ATOM   1991 C  C    . ILE   A 1 288 ? -27.25796 -73.83831 -61.73710 1.000 134.21517 ? 261 ILE   A C    1 
ATOM   1992 O  O    . ILE   A 1 288 ? -27.58106 -74.84800 -61.09773 1.000 136.17624 ? 261 ILE   A O    1 
ATOM   1993 C  CB   . ILE   A 1 288 ? -27.39542 -71.57864 -60.59706 1.000 138.55035 ? 261 ILE   A CB   1 
ATOM   1994 C  CG1  . ILE   A 1 288 ? -26.59098 -70.51939 -59.84663 1.000 151.76314 ? 261 ILE   A CG1  1 
ATOM   1995 C  CG2  . ILE   A 1 288 ? -28.49184 -72.12319 -59.69772 1.000 103.81948 ? 261 ILE   A CG2  1 
ATOM   1996 C  CD1  . ILE   A 1 288 ? -27.35450 -69.24180 -59.61670 1.000 135.10787 ? 261 ILE   A CD1  1 
ATOM   1997 N  N    . ILE   A 1 289 ? -27.58079 -73.69081 -63.02599 1.000 131.13454 ? 262 ILE   A N    1 
ATOM   1998 C  CA   . ILE   A 1 289 ? -28.29805 -74.76460 -63.71492 1.000 132.50721 ? 262 ILE   A CA   1 
ATOM   1999 C  C    . ILE   A 1 289 ? -27.43031 -76.01687 -63.80104 1.000 134.05457 ? 262 ILE   A C    1 
ATOM   2000 O  O    . ILE   A 1 289 ? -27.92269 -77.14480 -63.66567 1.000 129.60637 ? 262 ILE   A O    1 
ATOM   2001 C  CB   . ILE   A 1 289 ? -28.77045 -74.30090 -65.10528 1.000 144.80818 ? 262 ILE   A CB   1 
ATOM   2002 C  CG1  . ILE   A 1 289 ? -29.75257 -73.13708 -64.97093 1.000 124.73044 ? 262 ILE   A CG1  1 
ATOM   2003 C  CG2  . ILE   A 1 289 ? -29.43652 -75.44706 -65.85174 1.000 135.71958 ? 262 ILE   A CG2  1 
ATOM   2004 C  CD1  . ILE   A 1 289 ? -30.39278 -72.72576 -66.27687 1.000 135.60435 ? 262 ILE   A CD1  1 
ATOM   2005 N  N    . GLU   A 1 290 ? -26.12551 -75.83753 -64.02111 1.000 134.10539 ? 263 GLU   A N    1 
ATOM   2006 C  CA   . GLU   A 1 290 ? -25.19631 -76.96178 -64.02660 1.000 128.66517 ? 263 GLU   A CA   1 
ATOM   2007 C  C    . GLU   A 1 290 ? -25.16377 -77.64969 -62.66897 1.000 128.50734 ? 263 GLU   A C    1 
ATOM   2008 O  O    . GLU   A 1 290 ? -25.08227 -78.88103 -62.58712 1.000 142.15875 ? 263 GLU   A O    1 
ATOM   2009 C  CB   . GLU   A 1 290 ? -23.80338 -76.46583 -64.41841 1.000 142.62742 ? 263 GLU   A CB   1 
ATOM   2010 C  CG   . GLU   A 1 290 ? -22.74030 -77.53866 -64.55890 1.000 154.43764 ? 263 GLU   A CG   1 
ATOM   2011 C  CD   . GLU   A 1 290 ? -21.38627 -76.95197 -64.91306 1.000 172.70973 ? 263 GLU   A CD   1 
ATOM   2012 O  OE1  . GLU   A 1 290 ? -21.18363 -75.74253 -64.67270 1.000 174.73763 ? 263 GLU   A OE1  1 
ATOM   2013 O  OE2  . GLU   A 1 290 ? -20.52874 -77.69345 -65.43689 1.000 195.91000 ? 263 GLU   A OE2  1 
ATOM   2014 N  N    . ALA   A 1 291 ? -25.22564 -76.86650 -61.59054 1.000 123.24065 ? 264 ALA   A N    1 
ATOM   2015 C  CA   . ALA   A 1 291 ? -25.28997 -77.45359 -60.25606 1.000 127.28214 ? 264 ALA   A CA   1 
ATOM   2016 C  C    . ALA   A 1 291 ? -26.59059 -78.22107 -60.04978 1.000 132.84074 ? 264 ALA   A C    1 
ATOM   2017 O  O    . ALA   A 1 291 ? -26.60616 -79.26957 -59.39391 1.000 132.75233 ? 264 ALA   A O    1 
ATOM   2018 C  CB   . ALA   A 1 291 ? -25.14017 -76.36253 -59.19659 1.000 132.90285 ? 264 ALA   A CB   1 
ATOM   2019 N  N    . ALA   A 1 292 ? -27.69102 -77.71622 -60.60960 1.000 131.47602 ? 265 ALA   A N    1 
ATOM   2020 C  CA   . ALA   A 1 292 ? -29.00219 -78.29382 -60.32962 1.000 117.25121 ? 265 ALA   A CA   1 
ATOM   2021 C  C    . ALA   A 1 292 ? -29.26257 -79.56438 -61.13246 1.000 126.72110 ? 265 ALA   A C    1 
ATOM   2022 O  O    . ALA   A 1 292 ? -29.80911 -80.53446 -60.59602 1.000 127.04916 ? 265 ALA   A O    1 
ATOM   2023 C  CB   . ALA   A 1 292 ? -30.09688 -77.26415 -60.60581 1.000 117.11010 ? 265 ALA   A CB   1 
ATOM   2024 N  N    . ILE   A 1 293 ? -28.89276 -79.58174 -62.40966 1.000 136.12273 ? 266 ILE   A N    1 
ATOM   2025 C  CA   . ILE   A 1 293 ? -29.22483 -80.71003 -63.27889 1.000 141.35877 ? 266 ILE   A CA   1 
ATOM   2026 C  C    . ILE   A 1 293 ? -28.15909 -81.79619 -63.22131 1.000 146.23508 ? 266 ILE   A C    1 
ATOM   2027 O  O    . ILE   A 1 293 ? -28.46499 -82.96888 -62.98870 1.000 162.83195 ? 266 ILE   A O    1 
ATOM   2028 C  CB   . ILE   A 1 293 ? -29.44837 -80.21876 -64.72508 1.000 136.34325 ? 266 ILE   A CB   1 
ATOM   2029 C  CG1  . ILE   A 1 293 ? -30.72887 -79.38741 -64.81114 1.000 140.49335 ? 266 ILE   A CG1  1 
ATOM   2030 C  CG2  . ILE   A 1 293 ? -29.50525 -81.39586 -65.68723 1.000 139.62647 ? 266 ILE   A CG2  1 
ATOM   2031 C  CD1  . ILE   A 1 293 ? -31.07731 -78.94972 -66.21267 1.000 121.63089 ? 266 ILE   A CD1  1 
ATOM   2032 N  N    . ASN   A 1 294 ? -26.89421 -81.42862 -63.43246 1.000 132.09171 ? 267 ASN   A N    1 
ATOM   2033 C  CA   . ASN   A 1 294 ? -25.83509 -82.43084 -63.50027 1.000 145.40309 ? 267 ASN   A CA   1 
ATOM   2034 C  C    . ASN   A 1 294 ? -25.50105 -82.98285 -62.11984 1.000 168.02567 ? 267 ASN   A C    1 
ATOM   2035 O  O    . ASN   A 1 294 ? -25.37882 -84.20028 -61.94077 1.000 180.84633 ? 267 ASN   A O    1 
ATOM   2036 C  CB   . ASN   A 1 294 ? -24.59072 -81.83400 -64.15655 1.000 133.06948 ? 267 ASN   A CB   1 
ATOM   2037 C  CG   . ASN   A 1 294 ? -24.82636 -81.44474 -65.59939 1.000 154.34771 ? 267 ASN   A CG   1 
ATOM   2038 O  OD1  . ASN   A 1 294 ? -24.62727 -80.29309 -65.98580 1.000 149.48916 ? 267 ASN   A OD1  1 
ATOM   2039 N  ND2  . ASN   A 1 294 ? -25.25582 -82.40663 -66.40624 1.000 179.13222 ? 267 ASN   A ND2  1 
ATOM   2040 N  N    . ARG   A 1 295 ? -25.34382 -82.10379 -61.13114 1.000 146.61532 ? 268 ARG   A N    1 
ATOM   2041 C  CA   . ARG   A 1 295 ? -24.95206 -82.51810 -59.79149 1.000 146.57569 ? 268 ARG   A CA   1 
ATOM   2042 C  C    . ARG   A 1 295 ? -26.13075 -82.69797 -58.84335 1.000 160.71689 ? 268 ARG   A C    1 
ATOM   2043 O  O    . ARG   A 1 295 ? -25.93335 -83.19065 -57.72743 1.000 172.76489 ? 268 ARG   A O    1 
ATOM   2044 C  CB   . ARG   A 1 295 ? -23.95636 -81.51140 -59.19898 1.000 145.71377 ? 268 ARG   A CB   1 
ATOM   2045 C  CG   . ARG   A 1 295 ? -22.57494 -81.59569 -59.83426 1.000 139.62309 ? 268 ARG   A CG   1 
ATOM   2046 C  CD   . ARG   A 1 295 ? -21.58413 -80.61772 -59.21945 1.000 152.98160 ? 268 ARG   A CD   1 
ATOM   2047 N  NE   . ARG   A 1 295 ? -21.55960 -79.33847 -59.91893 1.000 147.76968 ? 268 ARG   A NE   1 
ATOM   2048 C  CZ   . ARG   A 1 295 ? -22.02766 -78.20195 -59.42233 1.000 152.60132 ? 268 ARG   A CZ   1 
ATOM   2049 N  NH1  . ARG   A 1 295 ? -22.55813 -78.14328 -58.21194 1.000 164.29495 ? 268 ARG   A NH1  1 
ATOM   2050 N  NH2  . ARG   A 1 295 ? -21.95714 -77.09531 -60.15689 1.000 144.99936 ? 268 ARG   A NH2  1 
ATOM   2051 N  N    . GLY   A 1 296 ? -27.33850 -82.32445 -59.25555 1.000 152.62638 ? 269 GLY   A N    1 
ATOM   2052 C  CA   . GLY   A 1 296 ? -28.51588 -82.54630 -58.42794 1.000 158.46285 ? 269 GLY   A CA   1 
ATOM   2053 C  C    . GLY   A 1 296 ? -28.48535 -81.82346 -57.09943 1.000 152.99378 ? 269 GLY   A C    1 
ATOM   2054 O  O    . GLY   A 1 296 ? -28.93525 -82.37167 -56.08534 1.000 137.43846 ? 269 GLY   A O    1 
ATOM   2055 N  N    . VAL   A 1 297 ? -27.96390 -80.60197 -57.08102 1.000 150.96014 ? 270 VAL   A N    1 
ATOM   2056 C  CA   . VAL   A 1 297 ? -27.85208 -79.83167 -55.84772 1.000 157.78080 ? 270 VAL   A CA   1 
ATOM   2057 C  C    . VAL   A 1 297 ? -29.20983 -79.23166 -55.50761 1.000 151.26132 ? 270 VAL   A C    1 
ATOM   2058 O  O    . VAL   A 1 297 ? -29.87580 -78.64370 -56.36802 1.000 145.14514 ? 270 VAL   A O    1 
ATOM   2059 C  CB   . VAL   A 1 297 ? -26.77964 -78.73936 -55.98834 1.000 152.19162 ? 270 VAL   A CB   1 
ATOM   2060 C  CG1  . VAL   A 1 297 ? -26.73180 -77.87192 -54.74229 1.000 147.25160 ? 270 VAL   A CG1  1 
ATOM   2061 C  CG2  . VAL   A 1 297 ? -25.41897 -79.36405 -56.26106 1.000 136.32177 ? 270 VAL   A CG2  1 
ATOM   2062 N  N    . LYS   A 1 298 ? -29.62775 -79.38485 -54.25184 1.000 150.81162 ? 271 LYS   A N    1 
ATOM   2063 C  CA   . LYS   A 1 298 ? -30.87004 -78.77974 -53.78042 1.000 137.00693 ? 271 LYS   A CA   1 
ATOM   2064 C  C    . LYS   A 1 298 ? -30.69199 -77.26888 -53.70552 1.000 134.62850 ? 271 LYS   A C    1 
ATOM   2065 O  O    . LYS   A 1 298 ? -29.97259 -76.76237 -52.83868 1.000 139.03310 ? 271 LYS   A O    1 
ATOM   2066 C  CB   . LYS   A 1 298 ? -31.25887 -79.35228 -52.42097 1.000 164.33714 ? 271 LYS   A CB   1 
ATOM   2067 C  CG   . LYS   A 1 298 ? -31.55684 -80.84247 -52.43384 1.000 193.22838 ? 271 LYS   A CG   1 
ATOM   2068 C  CD   . LYS   A 1 298 ? -32.09134 -81.30866 -51.08880 1.000 217.65521 ? 271 LYS   A CD   1 
ATOM   2069 C  CE   . LYS   A 1 298 ? -32.41701 -82.79357 -51.10743 1.000 207.96534 ? 271 LYS   A CE   1 
ATOM   2070 N  NZ   . LYS   A 1 298 ? -32.99456 -83.25151 -49.81351 1.000 218.52743 ? 271 LYS   A NZ   1 
ATOM   2071 N  N    . ILE   A 1 299 ? -31.34676 -76.54543 -54.60913 1.000 141.42373 ? 272 ILE   A N    1 
ATOM   2072 C  CA   . ILE   A 1 299 ? -31.17472 -75.10497 -54.74502 1.000 145.19073 ? 272 ILE   A CA   1 
ATOM   2073 C  C    . ILE   A 1 299 ? -32.50565 -74.42376 -54.45854 1.000 152.38371 ? 272 ILE   A C    1 
ATOM   2074 O  O    . ILE   A 1 299 ? -33.54549 -74.82994 -54.99187 1.000 149.71844 ? 272 ILE   A O    1 
ATOM   2075 C  CB   . ILE   A 1 299 ? -30.64973 -74.73103 -56.14322 1.000 127.87501 ? 272 ILE   A CB   1 
ATOM   2076 C  CG1  . ILE   A 1 299 ? -29.33554 -75.46196 -56.42495 1.000 144.22194 ? 272 ILE   A CG1  1 
ATOM   2077 C  CG2  . ILE   A 1 299 ? -30.45663 -73.23050 -56.25783 1.000 129.55277 ? 272 ILE   A CG2  1 
ATOM   2078 C  CD1  . ILE   A 1 299 ? -28.79232 -75.23720 -57.81526 1.000 138.31212 ? 272 ILE   A CD1  1 
ATOM   2079 N  N    . ARG   A 1 300 ? -32.46898 -73.39775 -53.60994 1.000 141.53918 ? 273 ARG   A N    1 
ATOM   2080 C  CA   . ARG   A 1 300 ? -33.63927 -72.60354 -53.25699 1.000 133.39401 ? 273 ARG   A CA   1 
ATOM   2081 C  C    . ARG   A 1 300 ? -33.33170 -71.14114 -53.54170 1.000 128.69484 ? 273 ARG   A C    1 
ATOM   2082 O  O    . ARG   A 1 300 ? -32.41139 -70.57019 -52.94709 1.000 123.48328 ? 273 ARG   A O    1 
ATOM   2083 C  CB   . ARG   A 1 300 ? -34.01897 -72.79920 -51.78768 1.000 140.94312 ? 273 ARG   A CB   1 
ATOM   2084 C  CG   . ARG   A 1 300 ? -34.49414 -74.20209 -51.44257 1.000 156.79176 ? 273 ARG   A CG   1 
ATOM   2085 C  CD   . ARG   A 1 300 ? -34.80575 -74.32306 -49.95893 1.000 155.76679 ? 273 ARG   A CD   1 
ATOM   2086 N  NE   . ARG   A 1 300 ? -33.64959 -73.98786 -49.13642 1.000 134.62871 ? 273 ARG   A NE   1 
ATOM   2087 C  CZ   . ARG   A 1 300 ? -33.65136 -73.97057 -47.81062 1.000 156.47264 ? 273 ARG   A CZ   1 
ATOM   2088 N  NH1  . ARG   A 1 300 ? -34.73781 -74.26795 -47.11661 1.000 174.23713 ? 273 ARG   A NH1  1 
ATOM   2089 N  NH2  . ARG   A 1 300 ? -32.53504 -73.64565 -47.16473 1.000 161.13826 ? 273 ARG   A NH2  1 
ATOM   2090 N  N    . LEU   A 1 301 ? -34.10182 -70.53991 -54.44274 1.000 137.93058 ? 274 LEU   A N    1 
ATOM   2091 C  CA   . LEU   A 1 301 ? -33.88493 -69.16923 -54.88829 1.000 133.34596 ? 274 LEU   A CA   1 
ATOM   2092 C  C    . LEU   A 1 301 ? -35.02011 -68.29084 -54.37993 1.000 138.18227 ? 274 LEU   A C    1 
ATOM   2093 O  O    . LEU   A 1 301 ? -36.18954 -68.54782 -54.68285 1.000 148.72652 ? 274 LEU   A O    1 
ATOM   2094 C  CB   . LEU   A 1 301 ? -33.79619 -69.10274 -56.41283 1.000 106.56832 ? 274 LEU   A CB   1 
ATOM   2095 C  CG   . LEU   A 1 301 ? -32.75186 -70.00928 -57.06780 1.000 119.98224 ? 274 LEU   A CG   1 
ATOM   2096 C  CD1  . LEU   A 1 301 ? -32.81835 -69.91373 -58.58525 1.000 124.92608 ? 274 LEU   A CD1  1 
ATOM   2097 C  CD2  . LEU   A 1 301 ? -31.35349 -69.67144 -56.57117 1.000 137.59181 ? 274 LEU   A CD2  1 
ATOM   2098 N  N    . LEU   A 1 302 ? -34.67276 -67.26043 -53.61434 1.000 129.13578 ? 275 LEU   A N    1 
ATOM   2099 C  CA   . LEU   A 1 302 ? -35.62949 -66.28788 -53.09074 1.000 126.82808 ? 275 LEU   A CA   1 
ATOM   2100 C  C    . LEU   A 1 302 ? -35.33868 -64.95490 -53.77199 1.000 128.06391 ? 275 LEU   A C    1 
ATOM   2101 O  O    . LEU   A 1 302 ? -34.41741 -64.23413 -53.37706 1.000 121.05114 ? 275 LEU   A O    1 
ATOM   2102 C  CB   . LEU   A 1 302 ? -35.52263 -66.18091 -51.57229 1.000 124.42478 ? 275 LEU   A CB   1 
ATOM   2103 C  CG   . LEU   A 1 302 ? -36.47824 -65.20488 -50.88458 1.000 110.96670 ? 275 LEU   A CG   1 
ATOM   2104 C  CD1  . LEU   A 1 302 ? -37.92162 -65.56566 -51.19168 1.000 123.09086 ? 275 LEU   A CD1  1 
ATOM   2105 C  CD2  . LEU   A 1 302 ? -36.23539 -65.18277 -49.38299 1.000 120.66034 ? 275 LEU   A CD2  1 
ATOM   2106 N  N    . VAL   A 1 303 ? -36.12470 -64.62877 -54.79611 1.000 132.88835 ? 276 VAL   A N    1 
ATOM   2107 C  CA   . VAL   A 1 303 ? -35.85885 -63.46793 -55.63428 1.000 118.55239 ? 276 VAL   A CA   1 
ATOM   2108 C  C    . VAL   A 1 303 ? -37.04157 -62.50905 -55.56162 1.000 138.25937 ? 276 VAL   A C    1 
ATOM   2109 O  O    . VAL   A 1 303 ? -38.11614 -62.84258 -55.06580 1.000 152.89105 ? 276 VAL   A O    1 
ATOM   2110 C  CB   . VAL   A 1 303 ? -35.56435 -63.85718 -57.09513 1.000 88.15525  ? 276 VAL   A CB   1 
ATOM   2111 C  CG1  . VAL   A 1 303 ? -34.41025 -64.84584 -57.15628 1.000 105.63045 ? 276 VAL   A CG1  1 
ATOM   2112 C  CG2  . VAL   A 1 303 ? -36.80881 -64.43373 -57.74899 1.000 127.59398 ? 276 VAL   A CG2  1 
ATOM   2113 N  N    . GLY   A 1 304 ? -36.82006 -61.29480 -56.05940 1.000 123.07665 ? 277 GLY   A N    1 
ATOM   2114 C  CA   . GLY   A 1 304 ? -37.88572 -60.31652 -56.11208 1.000 123.87761 ? 277 GLY   A CA   1 
ATOM   2115 C  C    . GLY   A 1 304 ? -38.77980 -60.52165 -57.32024 1.000 140.75261 ? 277 GLY   A C    1 
ATOM   2116 O  O    . GLY   A 1 304 ? -38.36799 -61.06252 -58.34593 1.000 149.36605 ? 277 GLY   A O    1 
ATOM   2117 N  N    . ASN   A 1 305 ? -40.02955 -60.08181 -57.18766 1.000 149.80192 ? 278 ASN   A N    1 
ATOM   2118 C  CA   . ASN   A 1 305 ? -40.98422 -60.22568 -58.27591 1.000 150.13432 ? 278 ASN   A CA   1 
ATOM   2119 C  C    . ASN   A 1 305 ? -40.53378 -59.41923 -59.49138 1.000 164.34528 ? 278 ASN   A C    1 
ATOM   2120 O  O    . ASN   A 1 305 ? -39.69375 -58.51917 -59.40271 1.000 181.38439 ? 278 ASN   A O    1 
ATOM   2121 C  CB   . ASN   A 1 305 ? -42.37930 -59.78177 -57.83593 1.000 155.82719 ? 278 ASN   A CB   1 
ATOM   2122 C  CG   . ASN   A 1 305 ? -42.46453 -58.29047 -57.58600 1.000 195.23019 ? 278 ASN   A CG   1 
ATOM   2123 O  OD1  . ASN   A 1 305 ? -41.51299 -57.67422 -57.10648 1.000 214.07813 ? 278 ASN   A OD1  1 
ATOM   2124 N  ND2  . ASN   A 1 305 ? -43.60820 -57.69997 -57.91488 1.000 183.96256 ? 278 ASN   A ND2  1 
ATOM   2125 N  N    . TRP   A 1 306 ? -41.11179 -59.75443 -60.64085 1.000 161.69120 ? 279 TRP   A N    1 
ATOM   2126 C  CA   . TRP   A 1 306 ? -40.70568 -59.19740 -61.92044 1.000 174.37266 ? 279 TRP   A CA   1 
ATOM   2127 C  C    . TRP   A 1 306 ? -41.91162 -58.58642 -62.62027 1.000 181.86077 ? 279 TRP   A C    1 
ATOM   2128 O  O    . TRP   A 1 306 ? -43.06554 -58.84347 -62.26586 1.000 191.98278 ? 279 TRP   A O    1 
ATOM   2129 C  CB   . TRP   A 1 306 ? -40.05578 -60.26849 -62.80875 1.000 175.10561 ? 279 TRP   A CB   1 
ATOM   2130 C  CG   . TRP   A 1 306 ? -41.00131 -61.35736 -63.24225 1.000 181.14956 ? 279 TRP   A CG   1 
ATOM   2131 C  CD1  . TRP   A 1 306 ? -41.55375 -61.51835 -64.48121 1.000 200.15477 ? 279 TRP   A CD1  1 
ATOM   2132 C  CD2  . TRP   A 1 306 ? -41.50734 -62.43167 -62.43682 1.000 172.15409 ? 279 TRP   A CD2  1 
ATOM   2133 N  NE1  . TRP   A 1 306 ? -42.36719 -62.62562 -64.49746 1.000 215.73776 ? 279 TRP   A NE1  1 
ATOM   2134 C  CE2  . TRP   A 1 306 ? -42.35680 -63.20304 -63.25515 1.000 196.60968 ? 279 TRP   A CE2  1 
ATOM   2135 C  CE3  . TRP   A 1 306 ? -41.32564 -62.81515 -61.10421 1.000 162.12682 ? 279 TRP   A CE3  1 
ATOM   2136 C  CZ2  . TRP   A 1 306 ? -43.02063 -64.33428 -62.78507 1.000 192.63835 ? 279 TRP   A CZ2  1 
ATOM   2137 C  CZ3  . TRP   A 1 306 ? -41.98401 -63.93847 -60.64086 1.000 184.33085 ? 279 TRP   A CZ3  1 
ATOM   2138 C  CH2  . TRP   A 1 306 ? -42.82194 -64.68372 -61.47822 1.000 198.64722 ? 279 TRP   A CH2  1 
ATOM   2139 N  N    . ASP   A 1 307 ? -41.62706 -57.76462 -63.62688 1.000 182.66484 ? 280 ASP   A N    1 
ATOM   2140 C  CA   . ASP   A 1 307 ? -42.67446 -57.12648 -64.40970 1.000 196.22926 ? 280 ASP   A CA   1 
ATOM   2141 C  C    . ASP   A 1 307 ? -43.19718 -58.09501 -65.46192 1.000 197.58081 ? 280 ASP   A C    1 
ATOM   2142 O  O    . ASP   A 1 307 ? -42.41641 -58.72440 -66.18326 1.000 183.69732 ? 280 ASP   A O    1 
ATOM   2143 C  CB   . ASP   A 1 307 ? -42.14620 -55.85567 -65.07467 1.000 205.30291 ? 280 ASP   A CB   1 
ATOM   2144 C  CG   . ASP   A 1 307 ? -43.23942 -55.05709 -65.75771 1.000 217.10624 ? 280 ASP   A CG   1 
ATOM   2145 O  OD1  . ASP   A 1 307 ? -44.43083 -55.33085 -65.50048 1.000 212.26975 ? 280 ASP   A OD1  1 
ATOM   2146 O  OD2  . ASP   A 1 307 ? -42.90749 -54.15615 -66.55586 1.000 223.68177 ? 280 ASP   A OD2  1 
ATOM   2147 N  N    . LYS   A 1 308 ? -44.52404 -58.21282 -65.54581 1.000 201.59594 ? 281 LYS   A N    1 
ATOM   2148 C  CA   . LYS   A 1 308 ? -45.13619 -59.06983 -66.55281 1.000 185.99831 ? 281 LYS   A CA   1 
ATOM   2149 C  C    . LYS   A 1 308 ? -44.88297 -58.56501 -67.96699 1.000 184.80716 ? 281 LYS   A C    1 
ATOM   2150 O  O    . LYS   A 1 308 ? -44.98954 -59.34522 -68.91922 1.000 170.94355 ? 281 LYS   A O    1 
ATOM   2151 C  CB   . LYS   A 1 308 ? -46.63960 -59.18528 -66.29512 1.000 199.10359 ? 281 LYS   A CB   1 
ATOM   2152 C  CG   . LYS   A 1 308 ? -46.98669 -59.66285 -64.89368 1.000 184.25519 ? 281 LYS   A CG   1 
ATOM   2153 C  CD   . LYS   A 1 308 ? -48.48855 -59.67008 -64.66185 1.000 218.57258 ? 281 LYS   A CD   1 
ATOM   2154 C  CE   . LYS   A 1 308 ? -48.81941 -60.08564 -63.23813 1.000 188.86715 ? 281 LYS   A CE   1 
ATOM   2155 N  NZ   . LYS   A 1 308 ? -50.28548 -60.08237 -62.98246 1.000 159.20636 ? 281 LYS   A NZ   1 
ATOM   2156 N  N    . ASN   A 1 309 ? -44.54924 -57.28219 -68.12385 1.000 202.69304 ? 282 ASN   A N    1 
ATOM   2157 C  CA   . ASN   A 1 309 ? -44.23916 -56.73171 -69.43654 1.000 207.50897 ? 282 ASN   A CA   1 
ATOM   2158 C  C    . ASN   A 1 309 ? -42.83125 -57.07710 -69.90127 1.000 206.60142 ? 282 ASN   A C    1 
ATOM   2159 O  O    . ASN   A 1 309 ? -42.55985 -57.02049 -71.10565 1.000 219.23840 ? 282 ASN   A O    1 
ATOM   2160 C  CB   . ASN   A 1 309 ? -44.41125 -55.21120 -69.42516 1.000 217.16463 ? 282 ASN   A CB   1 
ATOM   2161 C  CG   . ASN   A 1 309 ? -45.82789 -54.78679 -69.09693 1.000 231.27657 ? 282 ASN   A CG   1 
ATOM   2162 O  OD1  . ASN   A 1 309 ? -46.05997 -54.03979 -68.14622 1.000 236.76324 ? 282 ASN   A OD1  1 
ATOM   2163 N  ND2  . ASN   A 1 309 ? -46.78514 -55.26060 -69.88578 1.000 239.76337 ? 282 ASN   A ND2  1 
ATOM   2164 N  N    . ASP   A 1 310 ? -41.93513 -57.42756 -68.98162 1.000 180.44947 ? 283 ASP   A N    1 
ATOM   2165 C  CA   . ASP   A 1 310 ? -40.55936 -57.76625 -69.33017 1.000 165.15411 ? 283 ASP   A CA   1 
ATOM   2166 C  C    . ASP   A 1 310 ? -40.52158 -59.19930 -69.84667 1.000 163.46472 ? 283 ASP   A C    1 
ATOM   2167 O  O    . ASP   A 1 310 ? -40.76488 -60.14633 -69.09151 1.000 168.92391 ? 283 ASP   A O    1 
ATOM   2168 C  CB   . ASP   A 1 310 ? -39.64555 -57.58990 -68.12129 1.000 156.51285 ? 283 ASP   A CB   1 
ATOM   2169 C  CG   . ASP   A 1 310 ? -38.17948 -57.76255 -68.46746 1.000 178.50901 ? 283 ASP   A CG   1 
ATOM   2170 O  OD1  . ASP   A 1 310 ? -37.84626 -57.78984 -69.67156 1.000 190.10041 ? 283 ASP   A OD1  1 
ATOM   2171 O  OD2  . ASP   A 1 310 ? -37.35917 -57.87346 -67.53250 1.000 183.67962 ? 283 ASP   A OD2  1 
ATOM   2172 N  N    . VAL   A 1 311 ? -40.20926 -59.36113 -71.13473 1.000 168.92505 ? 284 VAL   A N    1 
ATOM   2173 C  CA   . VAL   A 1 311 ? -40.22327 -60.69097 -71.73545 1.000 153.63419 ? 284 VAL   A CA   1 
ATOM   2174 C  C    . VAL   A 1 311 ? -39.03154 -61.51732 -71.27052 1.000 145.94215 ? 284 VAL   A C    1 
ATOM   2175 O  O    . VAL   A 1 311 ? -39.11624 -62.74835 -71.19832 1.000 154.31772 ? 284 VAL   A O    1 
ATOM   2176 C  CB   . VAL   A 1 311 ? -40.27111 -60.58578 -73.27114 1.000 141.60623 ? 284 VAL   A CB   1 
ATOM   2177 C  CG1  . VAL   A 1 311 ? -41.58129 -59.95865 -73.71590 1.000 166.31017 ? 284 VAL   A CG1  1 
ATOM   2178 C  CG2  . VAL   A 1 311 ? -39.08864 -59.78169 -73.79147 1.000 122.02358 ? 284 VAL   A CG2  1 
ATOM   2179 N  N    . TYR   A 1 312 ? -37.90820 -60.87077 -70.95021 1.000 138.60518 ? 285 TYR   A N    1 
ATOM   2180 C  CA   . TYR   A 1 312 ? -36.74900 -61.61138 -70.46175 1.000 145.39930 ? 285 TYR   A CA   1 
ATOM   2181 C  C    . TYR   A 1 312 ? -37.02604 -62.22862 -69.09724 1.000 137.71641 ? 285 TYR   A C    1 
ATOM   2182 O  O    . TYR   A 1 312 ? -36.67833 -63.39094 -68.84977 1.000 139.34729 ? 285 TYR   A O    1 
ATOM   2183 C  CB   . TYR   A 1 312 ? -35.52880 -60.69337 -70.40075 1.000 144.66563 ? 285 TYR   A CB   1 
ATOM   2184 C  CG   . TYR   A 1 312 ? -34.98316 -60.31149 -71.75750 1.000 147.91875 ? 285 TYR   A CG   1 
ATOM   2185 C  CD1  . TYR   A 1 312 ? -34.97267 -61.22340 -72.80453 1.000 149.89687 ? 285 TYR   A CD1  1 
ATOM   2186 C  CD2  . TYR   A 1 312 ? -34.48430 -59.03797 -71.99359 1.000 160.29330 ? 285 TYR   A CD2  1 
ATOM   2187 C  CE1  . TYR   A 1 312 ? -34.47518 -60.87924 -74.04757 1.000 143.51699 ? 285 TYR   A CE1  1 
ATOM   2188 C  CE2  . TYR   A 1 312 ? -33.98612 -58.68463 -73.23322 1.000 171.63903 ? 285 TYR   A CE2  1 
ATOM   2189 C  CZ   . TYR   A 1 312 ? -33.98314 -59.60852 -74.25632 1.000 153.69889 ? 285 TYR   A CZ   1 
ATOM   2190 O  OH   . TYR   A 1 312 ? -33.48676 -59.25971 -75.49203 1.000 155.98818 ? 285 TYR   A OH   1 
ATOM   2191 N  N    . SER   A 1 313 ? -37.65807 -61.46652 -68.20258 1.000 138.75143 ? 286 SER   A N    1 
ATOM   2192 C  CA   . SER   A 1 313 ? -37.99756 -61.99429 -66.88663 1.000 144.22649 ? 286 SER   A CA   1 
ATOM   2193 C  C    . SER   A 1 313 ? -39.00788 -63.12942 -66.99090 1.000 151.72728 ? 286 SER   A C    1 
ATOM   2194 O  O    . SER   A 1 313 ? -38.88922 -64.13751 -66.28645 1.000 146.10649 ? 286 SER   A O    1 
ATOM   2195 C  CB   . SER   A 1 313 ? -38.53516 -60.87388 -65.99885 1.000 147.90957 ? 286 SER   A CB   1 
ATOM   2196 O  OG   . SER   A 1 313 ? -37.58313 -59.83420 -65.85831 1.000 148.11693 ? 286 SER   A OG   1 
ATOM   2197 N  N    . MET   A 1 314 ? -40.00318 -62.99052 -67.87041 1.000 157.07654 ? 287 MET   A N    1 
ATOM   2198 C  CA   . MET   A 1 314 ? -40.98177 -64.05941 -68.04733 1.000 147.46839 ? 287 MET   A CA   1 
ATOM   2199 C  C    . MET   A 1 314 ? -40.33986 -65.30184 -68.65351 1.000 153.25263 ? 287 MET   A C    1 
ATOM   2200 O  O    . MET   A 1 314 ? -40.69074 -66.43068 -68.28739 1.000 155.00913 ? 287 MET   A O    1 
ATOM   2201 C  CB   . MET   A 1 314 ? -42.14177 -63.57216 -68.91548 1.000 159.75604 ? 287 MET   A CB   1 
ATOM   2202 C  CG   . MET   A 1 314 ? -43.00481 -62.50502 -68.25971 1.000 181.39995 ? 287 MET   A CG   1 
ATOM   2203 S  SD   . MET   A 1 314 ? -43.81015 -63.08977 -66.75689 1.000 194.16405 ? 287 MET   A SD   1 
ATOM   2204 C  CE   . MET   A 1 314 ? -44.71405 -64.50107 -67.38572 1.000 183.09044 ? 287 MET   A CE   1 
ATOM   2205 N  N    . ALA   A 1 315 ? -39.39765 -65.11419 -69.58066 1.000 152.46997 ? 288 ALA   A N    1 
ATOM   2206 C  CA   . ALA   A 1 315 ? -38.68359 -66.24806 -70.15665 1.000 147.87329 ? 288 ALA   A CA   1 
ATOM   2207 C  C    . ALA   A 1 315 ? -37.87491 -66.97533 -69.09272 1.000 148.40301 ? 288 ALA   A C    1 
ATOM   2208 O  O    . ALA   A 1 315 ? -37.90564 -68.20742 -69.00813 1.000 172.18575 ? 288 ALA   A O    1 
ATOM   2209 C  CB   . ALA   A 1 315 ? -37.77770 -65.77629 -71.29363 1.000 157.92675 ? 288 ALA   A CB   1 
ATOM   2210 N  N    . THR   A 1 316 ? -37.14570 -66.22146 -68.26559 1.000 136.65340 ? 289 THR   A N    1 
ATOM   2211 C  CA   . THR   A 1 316 ? -36.40597 -66.82840 -67.16274 1.000 148.97290 ? 289 THR   A CA   1 
ATOM   2212 C  C    . THR   A 1 316 ? -37.34172 -67.57045 -66.21503 1.000 150.17000 ? 289 THR   A C    1 
ATOM   2213 O  O    . THR   A 1 316 ? -37.03682 -68.68515 -65.76938 1.000 142.53872 ? 289 THR   A O    1 
ATOM   2214 C  CB   . THR   A 1 316 ? -35.62462 -65.75328 -66.40625 1.000 150.31173 ? 289 THR   A CB   1 
ATOM   2215 O  OG1  . THR   A 1 316 ? -34.88131 -64.95658 -67.33670 1.000 149.88941 ? 289 THR   A OG1  1 
ATOM   2216 C  CG2  . THR   A 1 316 ? -34.66439 -66.38761 -65.41373 1.000 143.90576 ? 289 THR   A CG2  1 
ATOM   2217 N  N    . ALA   A 1 317 ? -38.49309 -66.96922 -65.90703 1.000 148.59975 ? 290 ALA   A N    1 
ATOM   2218 C  CA   . ALA   A 1 317 ? -39.43591 -67.58083 -64.97800 1.000 159.61356 ? 290 ALA   A CA   1 
ATOM   2219 C  C    . ALA   A 1 317 ? -39.96503 -68.90200 -65.51891 1.000 147.49087 ? 290 ALA   A C    1 
ATOM   2220 O  O    . ALA   A 1 317 ? -39.93810 -69.92333 -64.82438 1.000 166.23894 ? 290 ALA   A O    1 
ATOM   2221 C  CB   . ALA   A 1 317 ? -40.58508 -66.61405 -64.69183 1.000 178.81239 ? 290 ALA   A CB   1 
ATOM   2222 N  N    . ARG   A 1 318 ? -40.45872 -68.90151 -66.75946 1.000 131.42856 ? 291 ARG   A N    1 
ATOM   2223 C  CA   . ARG   A 1 318 ? -40.98757 -70.13156 -67.33818 1.000 156.95338 ? 291 ARG   A CA   1 
ATOM   2224 C  C    . ARG   A 1 318 ? -39.89249 -71.13753 -67.66390 1.000 159.89533 ? 291 ARG   A C    1 
ATOM   2225 O  O    . ARG   A 1 318 ? -40.19082 -72.32438 -67.83593 1.000 155.98723 ? 291 ARG   A O    1 
ATOM   2226 C  CB   . ARG   A 1 318 ? -41.80827 -69.82392 -68.59057 1.000 173.12177 ? 291 ARG   A CB   1 
ATOM   2227 C  CG   . ARG   A 1 318 ? -43.22328 -69.35914 -68.29007 1.000 167.28046 ? 291 ARG   A CG   1 
ATOM   2228 C  CD   . ARG   A 1 318 ? -44.07932 -69.33548 -69.54273 1.000 174.31824 ? 291 ARG   A CD   1 
ATOM   2229 N  NE   . ARG   A 1 318 ? -43.63697 -68.32128 -70.49104 1.000 190.97005 ? 291 ARG   A NE   1 
ATOM   2230 C  CZ   . ARG   A 1 318 ? -44.16207 -67.10769 -70.58457 1.000 202.54507 ? 291 ARG   A CZ   1 
ATOM   2231 N  NH1  . ARG   A 1 318 ? -45.15781 -66.72389 -69.80284 1.000 188.55051 ? 291 ARG   A NH1  1 
ATOM   2232 N  NH2  . ARG   A 1 318 ? -43.67841 -66.25915 -71.48706 1.000 203.45645 ? 291 ARG   A NH2  1 
ATOM   2233 N  N    . SER   A 1 319 ? -38.63724 -70.69587 -67.75221 1.000 164.47318 ? 292 SER   A N    1 
ATOM   2234 C  CA   . SER   A 1 319 ? -37.53523 -71.63829 -67.89049 1.000 146.86417 ? 292 SER   A CA   1 
ATOM   2235 C  C    . SER   A 1 319 ? -37.27786 -72.36124 -66.57594 1.000 130.76153 ? 292 SER   A C    1 
ATOM   2236 O  O    . SER   A 1 319 ? -37.14430 -73.58998 -66.54529 1.000 144.97321 ? 292 SER   A O    1 
ATOM   2237 C  CB   . SER   A 1 319 ? -36.28126 -70.90389 -68.36352 1.000 134.26737 ? 292 SER   A CB   1 
ATOM   2238 O  OG   . SER   A 1 319 ? -36.48460 -70.31220 -69.63512 1.000 163.08413 ? 292 SER   A OG   1 
ATOM   2239 N  N    . LEU   A 1 320 ? -37.21905 -71.61198 -65.47312 1.000 122.08096 ? 293 LEU   A N    1 
ATOM   2240 C  CA   . LEU   A 1 320 ? -37.01167 -72.23398 -64.16997 1.000 135.85423 ? 293 LEU   A CA   1 
ATOM   2241 C  C    . LEU   A 1 320 ? -38.23572 -73.01242 -63.69950 1.000 152.26228 ? 293 LEU   A C    1 
ATOM   2242 O  O    . LEU   A 1 320 ? -38.10103 -73.90939 -62.85799 1.000 163.75889 ? 293 LEU   A O    1 
ATOM   2243 C  CB   . LEU   A 1 320 ? -36.63740 -71.17260 -63.13397 1.000 156.08367 ? 293 LEU   A CB   1 
ATOM   2244 C  CG   . LEU   A 1 320 ? -35.50546 -70.21510 -63.51766 1.000 143.56384 ? 293 LEU   A CG   1 
ATOM   2245 C  CD1  . LEU   A 1 320 ? -35.19562 -69.25241 -62.37912 1.000 156.14664 ? 293 LEU   A CD1  1 
ATOM   2246 C  CD2  . LEU   A 1 320 ? -34.25865 -70.97581 -63.94480 1.000 152.95238 ? 293 LEU   A CD2  1 
ATOM   2247 N  N    . ASP   A 1 321 ? -39.42156 -72.68874 -64.22310 1.000 162.77398 ? 294 ASP   A N    1 
ATOM   2248 C  CA   . ASP   A 1 321 ? -40.63825 -73.37285 -63.79718 1.000 174.28984 ? 294 ASP   A CA   1 
ATOM   2249 C  C    . ASP   A 1 321 ? -40.62018 -74.83993 -64.20473 1.000 168.82437 ? 294 ASP   A C    1 
ATOM   2250 O  O    . ASP   A 1 321 ? -41.07641 -75.70626 -63.44939 1.000 191.48722 ? 294 ASP   A O    1 
ATOM   2251 C  CB   . ASP   A 1 321 ? -41.86192 -72.66645 -64.38158 1.000 179.85089 ? 294 ASP   A CB   1 
ATOM   2252 C  CG   . ASP   A 1 321 ? -43.15867 -73.11064 -63.73374 1.000 193.53340 ? 294 ASP   A CG   1 
ATOM   2253 O  OD1  . ASP   A 1 321 ? -43.39184 -72.74826 -62.56152 1.000 164.41766 ? 294 ASP   A OD1  1 
ATOM   2254 O  OD2  . ASP   A 1 321 ? -43.94625 -73.81831 -64.39602 1.000 209.68245 ? 294 ASP   A OD2  1 
ATOM   2255 N  N    . ALA   A 1 322 ? -40.10151 -75.13815 -65.39488 1.000 150.81100 ? 295 ALA   A N    1 
ATOM   2256 C  CA   . ALA   A 1 322 ? -39.98611 -76.51799 -65.84291 1.000 156.43731 ? 295 ALA   A CA   1 
ATOM   2257 C  C    . ALA   A 1 322 ? -38.80012 -77.24034 -65.22089 1.000 136.98832 ? 295 ALA   A C    1 
ATOM   2258 O  O    . ALA   A 1 322 ? -38.71860 -78.46850 -65.32620 1.000 144.90649 ? 295 ALA   A O    1 
ATOM   2259 C  CB   . ALA   A 1 322 ? -39.88168 -76.56905 -67.36815 1.000 154.02110 ? 295 ALA   A CB   1 
ATOM   2260 N  N    . LEU   A 1 323 ? -37.88607 -76.51465 -64.57998 1.000 138.56989 ? 296 LEU   A N    1 
ATOM   2261 C  CA   . LEU   A 1 323 ? -36.75549 -77.13505 -63.90417 1.000 148.84625 ? 296 LEU   A CA   1 
ATOM   2262 C  C    . LEU   A 1 323 ? -37.04818 -77.43689 -62.44238 1.000 171.70982 ? 296 LEU   A C    1 
ATOM   2263 O  O    . LEU   A 1 323 ? -36.50547 -78.40621 -61.89768 1.000 170.72569 ? 296 LEU   A O    1 
ATOM   2264 C  CB   . LEU   A 1 323 ? -35.52275 -76.23386 -64.00867 1.000 149.86646 ? 296 LEU   A CB   1 
ATOM   2265 C  CG   . LEU   A 1 323 ? -35.10988 -75.84361 -65.42964 1.000 162.32203 ? 296 LEU   A CG   1 
ATOM   2266 C  CD1  . LEU   A 1 323 ? -33.92418 -74.89164 -65.40920 1.000 138.17489 ? 296 LEU   A CD1  1 
ATOM   2267 C  CD2  . LEU   A 1 323 ? -34.79649 -77.07750 -66.26247 1.000 155.49493 ? 296 LEU   A CD2  1 
ATOM   2268 N  N    . CYS   A 1 324 ? -37.89009 -76.62439 -61.79496 1.000 180.61574 ? 297 CYS   A N    1 
ATOM   2269 C  CA   . CYS   A 1 324 ? -38.29641 -76.92318 -60.42496 1.000 181.73292 ? 297 CYS   A CA   1 
ATOM   2270 C  C    . CYS   A 1 324 ? -39.06333 -78.23596 -60.34720 1.000 174.52899 ? 297 CYS   A C    1 
ATOM   2271 O  O    . CYS   A 1 324 ? -38.95117 -78.96555 -59.35492 1.000 176.64012 ? 297 CYS   A O    1 
ATOM   2272 C  CB   . CYS   A 1 324 ? -39.14915 -75.78264 -59.86081 1.000 189.97916 ? 297 CYS   A CB   1 
ATOM   2273 S  SG   . CYS   A 1 324 ? -38.23364 -74.29078 -59.41498 1.000 211.24927 ? 297 CYS   A SG   1 
ATOM   2274 N  N    . VAL   A 1 325 ? -39.84390 -78.55440 -61.38114 1.000 165.97957 ? 298 VAL   A N    1 
ATOM   2275 C  CA   . VAL   A 1 325 ? -40.65291 -79.76717 -61.35562 1.000 167.33056 ? 298 VAL   A CA   1 
ATOM   2276 C  C    . VAL   A 1 325 ? -39.86635 -80.99998 -61.77827 1.000 152.92171 ? 298 VAL   A C    1 
ATOM   2277 O  O    . VAL   A 1 325 ? -40.29705 -82.12454 -61.49541 1.000 165.98589 ? 298 VAL   A O    1 
ATOM   2278 C  CB   . VAL   A 1 325 ? -41.89450 -79.60926 -62.24820 1.000 173.13772 ? 298 VAL   A CB   1 
ATOM   2279 C  CG1  . VAL   A 1 325 ? -42.76861 -78.47013 -61.74145 1.000 208.91871 ? 298 VAL   A CG1  1 
ATOM   2280 C  CG2  . VAL   A 1 325 ? -41.48107 -79.37348 -63.69525 1.000 135.18327 ? 298 VAL   A CG2  1 
ATOM   2281 N  N    . GLN   A 1 326 ? -38.72559 -80.82581 -62.44233 1.000 154.07917 ? 299 GLN   A N    1 
ATOM   2282 C  CA   . GLN   A 1 326 ? -37.90670 -81.94536 -62.89114 1.000 155.68911 ? 299 GLN   A CA   1 
ATOM   2283 C  C    . GLN   A 1 326 ? -36.78558 -82.29063 -61.92101 1.000 154.55225 ? 299 GLN   A C    1 
ATOM   2284 O  O    . GLN   A 1 326 ? -36.56291 -83.47105 -61.63446 1.000 152.91953 ? 299 GLN   A O    1 
ATOM   2285 C  CB   . GLN   A 1 326 ? -37.31164 -81.64422 -64.27108 1.000 165.99111 ? 299 GLN   A CB   1 
ATOM   2286 C  CG   . GLN   A 1 326 ? -36.43902 -82.75630 -64.83418 1.000 180.95008 ? 299 GLN   A CG   1 
ATOM   2287 C  CD   . GLN   A 1 326 ? -37.21171 -84.02939 -65.11743 1.000 173.48484 ? 299 GLN   A CD   1 
ATOM   2288 O  OE1  . GLN   A 1 326 ? -38.43449 -84.01209 -65.26302 1.000 159.16402 ? 299 GLN   A OE1  1 
ATOM   2289 N  NE2  . GLN   A 1 326 ? -36.49752 -85.14566 -65.19643 1.000 182.02519 ? 299 GLN   A NE2  1 
ATOM   2290 N  N    . ASN   A 1 327 ? -36.07555 -81.29182 -61.41085 1.000 154.23630 ? 300 ASN   A N    1 
ATOM   2291 C  CA   . ASN   A 1 327 ? -34.98383 -81.48548 -60.47016 1.000 153.57891 ? 300 ASN   A CA   1 
ATOM   2292 C  C    . ASN   A 1 327 ? -35.35807 -80.88269 -59.11936 1.000 158.60144 ? 300 ASN   A C    1 
ATOM   2293 O  O    . ASN   A 1 327 ? -36.44673 -80.33077 -58.93519 1.000 159.05792 ? 300 ASN   A O    1 
ATOM   2294 C  CB   . ASN   A 1 327 ? -33.69271 -80.87368 -61.01730 1.000 139.96888 ? 300 ASN   A CB   1 
ATOM   2295 C  CG   . ASN   A 1 327 ? -33.32323 -81.42175 -62.38185 1.000 157.82414 ? 300 ASN   A CG   1 
ATOM   2296 O  OD1  . ASN   A 1 327 ? -33.79915 -80.93581 -63.40860 1.000 147.86110 ? 300 ASN   A OD1  1 
ATOM   2297 N  ND2  . ASN   A 1 327 ? -32.47182 -82.44126 -62.39967 1.000 170.04020 ? 300 ASN   A ND2  1 
ATOM   2298 N  N    . ASP   A 1 328 ? -34.43590 -80.99429 -58.16223 1.000 159.62235 ? 301 ASP   A N    1 
ATOM   2299 C  CA   . ASP   A 1 328 ? -34.66947 -80.50365 -56.80396 1.000 156.61316 ? 301 ASP   A CA   1 
ATOM   2300 C  C    . ASP   A 1 328 ? -34.32712 -79.01651 -56.76093 1.000 165.05157 ? 301 ASP   A C    1 
ATOM   2301 O  O    . ASP   A 1 328 ? -33.25049 -78.59774 -56.32868 1.000 167.10585 ? 301 ASP   A O    1 
ATOM   2302 C  CB   . ASP   A 1 328 ? -33.85838 -81.30774 -55.79568 1.000 160.26508 ? 301 ASP   A CB   1 
ATOM   2303 C  CG   . ASP   A 1 328 ? -34.43699 -81.24057 -54.39433 1.000 185.70084 ? 301 ASP   A CG   1 
ATOM   2304 O  OD1  . ASP   A 1 328 ? -34.98146 -80.18081 -54.01908 1.000 184.01237 ? 301 ASP   A OD1  1 
ATOM   2305 O  OD2  . ASP   A 1 328 ? -34.35193 -82.25311 -53.66843 1.000 211.82392 ? 301 ASP   A OD2  1 
ATOM   2306 N  N    . LEU   A 1 329 ? -35.27764 -78.20636 -57.22472 1.000 169.45632 ? 302 LEU   A N    1 
ATOM   2307 C  CA   . LEU   A 1 329 ? -35.13492 -76.75818 -57.25369 1.000 165.55019 ? 302 LEU   A CA   1 
ATOM   2308 C  C    . LEU   A 1 329 ? -36.42396 -76.11775 -56.76188 1.000 171.84457 ? 302 LEU   A C    1 
ATOM   2309 O  O    . LEU   A 1 329 ? -37.52008 -76.56258 -57.11373 1.000 178.46597 ? 302 LEU   A O    1 
ATOM   2310 C  CB   . LEU   A 1 329 ? -34.80016 -76.25784 -58.66713 1.000 136.20573 ? 302 LEU   A CB   1 
ATOM   2311 C  CG   . LEU   A 1 329 ? -34.75310 -74.74380 -58.89710 1.000 140.80858 ? 302 LEU   A CG   1 
ATOM   2312 C  CD1  . LEU   A 1 329 ? -33.59693 -74.10275 -58.14726 1.000 129.57026 ? 302 LEU   A CD1  1 
ATOM   2313 C  CD2  . LEU   A 1 329 ? -34.67989 -74.41993 -60.38422 1.000 134.73158 ? 302 LEU   A CD2  1 
ATOM   2314 N  N    . SER   A 1 330 ? -36.28756 -75.07740 -55.94265 1.000 157.22409 ? 303 SER   A N    1 
ATOM   2315 C  CA   . SER   A 1 330 ? -37.42999 -74.34052 -55.42206 1.000 161.16467 ? 303 SER   A CA   1 
ATOM   2316 C  C    . SER   A 1 330 ? -37.20330 -72.84995 -55.61966 1.000 151.57497 ? 303 SER   A C    1 
ATOM   2317 O  O    . SER   A 1 330 ? -36.07464 -72.36408 -55.50339 1.000 149.80155 ? 303 SER   A O    1 
ATOM   2318 C  CB   . SER   A 1 330 ? -37.66902 -74.64895 -53.93850 1.000 172.30086 ? 303 SER   A CB   1 
ATOM   2319 O  OG   . SER   A 1 330 ? -38.08446 -75.99183 -53.75700 1.000 161.88965 ? 303 SER   A OG   1 
ATOM   2320 N  N    . VAL   A 1 331 ? -38.27999 -72.12980 -55.92687 1.000 144.33580 ? 304 VAL   A N    1 
ATOM   2321 C  CA   . VAL   A 1 331 ? -38.21769 -70.69932 -56.20631 1.000 135.20751 ? 304 VAL   A CA   1 
ATOM   2322 C  C    . VAL   A 1 331 ? -39.36451 -70.00694 -55.48379 1.000 146.56054 ? 304 VAL   A C    1 
ATOM   2323 O  O    . VAL   A 1 331 ? -40.52055 -70.42855 -55.59407 1.000 165.49500 ? 304 VAL   A O    1 
ATOM   2324 C  CB   . VAL   A 1 331 ? -38.28222 -70.40649 -57.71874 1.000 120.06796 ? 304 VAL   A CB   1 
ATOM   2325 C  CG1  . VAL   A 1 331 ? -38.41145 -68.91280 -57.96449 1.000 120.56542 ? 304 VAL   A CG1  1 
ATOM   2326 C  CG2  . VAL   A 1 331 ? -37.05188 -70.95837 -58.42298 1.000 139.31189 ? 304 VAL   A CG2  1 
ATOM   2327 N  N    . LYS   A 1 332 ? -39.04318 -68.94951 -54.74129 1.000 136.49898 ? 305 LYS   A N    1 
ATOM   2328 C  CA   . LYS   A 1 332 ? -40.03590 -68.08921 -54.11813 1.000 130.61168 ? 305 LYS   A CA   1 
ATOM   2329 C  C    . LYS   A 1 332 ? -39.72219 -66.63665 -54.44813 1.000 131.36927 ? 305 LYS   A C    1 
ATOM   2330 O  O    . LYS   A 1 332 ? -38.56571 -66.26779 -54.68483 1.000 139.49902 ? 305 LYS   A O    1 
ATOM   2331 C  CB   . LYS   A 1 332 ? -40.09300 -68.28990 -52.59585 1.000 142.00200 ? 305 LYS   A CB   1 
ATOM   2332 C  CG   . LYS   A 1 332 ? -40.71000 -69.61534 -52.17555 1.000 144.47339 ? 305 LYS   A CG   1 
ATOM   2333 C  CD   . LYS   A 1 332 ? -41.04840 -69.63094 -50.69385 1.000 138.84025 ? 305 LYS   A CD   1 
ATOM   2334 C  CE   . LYS   A 1 332 ? -41.79287 -70.90169 -50.31498 1.000 144.99604 ? 305 LYS   A CE   1 
ATOM   2335 N  NZ   . LYS   A 1 332 ? -42.23859 -70.88374 -48.89472 1.000 130.74803 ? 305 LYS   A NZ   1 
ATOM   2336 N  N    . VAL   A 1 333 ? -40.77042 -65.81745 -54.47220 1.000 137.84557 ? 306 VAL   A N    1 
ATOM   2337 C  CA   . VAL   A 1 333 ? -40.66101 -64.41666 -54.85262 1.000 126.87032 ? 306 VAL   A CA   1 
ATOM   2338 C  C    . VAL   A 1 333 ? -41.15162 -63.54406 -53.70698 1.000 129.60009 ? 306 VAL   A C    1 
ATOM   2339 O  O    . VAL   A 1 333 ? -42.02985 -63.92971 -52.92816 1.000 141.51082 ? 306 VAL   A O    1 
ATOM   2340 C  CB   . VAL   A 1 333 ? -41.44625 -64.10736 -56.14675 1.000 125.02138 ? 306 VAL   A CB   1 
ATOM   2341 C  CG1  . VAL   A 1 333 ? -40.88646 -64.91037 -57.31197 1.000 144.10771 ? 306 VAL   A CG1  1 
ATOM   2342 C  CG2  . VAL   A 1 333 ? -42.92985 -64.39321 -55.95407 1.000 148.18124 ? 306 VAL   A CG2  1 
ATOM   2343 N  N    . PHE   A 1 334 ? -40.55802 -62.35899 -53.60570 1.000 133.91354 ? 307 PHE   A N    1 
ATOM   2344 C  CA   . PHE   A 1 334 ? -40.95709 -61.35503 -52.63137 1.000 138.18195 ? 307 PHE   A CA   1 
ATOM   2345 C  C    . PHE   A 1 334 ? -41.19516 -60.02964 -53.34103 1.000 146.45309 ? 307 PHE   A C    1 
ATOM   2346 O  O    . PHE   A 1 334 ? -40.61150 -59.75696 -54.39368 1.000 166.22777 ? 307 PHE   A O    1 
ATOM   2347 C  CB   . PHE   A 1 334 ? -39.90517 -61.18332 -51.51390 1.000 150.19238 ? 307 PHE   A CB   1 
ATOM   2348 C  CG   . PHE   A 1 334 ? -38.57408 -60.66074 -51.99165 1.000 152.09346 ? 307 PHE   A CG   1 
ATOM   2349 C  CD1  . PHE   A 1 334 ? -38.34667 -59.29735 -52.10328 1.000 154.39377 ? 307 PHE   A CD1  1 
ATOM   2350 C  CD2  . PHE   A 1 334 ? -37.54237 -61.53151 -52.30304 1.000 125.72629 ? 307 PHE   A CD2  1 
ATOM   2351 C  CE1  . PHE   A 1 334 ? -37.12623 -58.81407 -52.53616 1.000 137.10682 ? 307 PHE   A CE1  1 
ATOM   2352 C  CE2  . PHE   A 1 334 ? -36.31625 -61.05207 -52.73273 1.000 116.69615 ? 307 PHE   A CE2  1 
ATOM   2353 C  CZ   . PHE   A 1 334 ? -36.10979 -59.69221 -52.85037 1.000 123.35085 ? 307 PHE   A CZ   1 
ATOM   2354 N  N    . THR   A 1 335 ? -42.06161 -59.20476 -52.75089 1.000 117.22522 ? 308 THR   A N    1 
ATOM   2355 C  CA   . THR   A 1 335 ? -42.40247 -57.90442 -53.30989 1.000 137.85299 ? 308 THR   A CA   1 
ATOM   2356 C  C    . THR   A 1 335 ? -41.91645 -56.73510 -52.46572 1.000 157.78885 ? 308 THR   A C    1 
ATOM   2357 O  O    . THR   A 1 335 ? -41.98803 -55.59011 -52.92586 1.000 174.27274 ? 308 THR   A O    1 
ATOM   2358 C  CB   . THR   A 1 335 ? -43.92293 -57.78595 -53.49544 1.000 146.67187 ? 308 THR   A CB   1 
ATOM   2359 O  OG1  . THR   A 1 335 ? -44.57529 -57.96953 -52.23240 1.000 181.60334 ? 308 THR   A OG1  1 
ATOM   2360 C  CG2  . THR   A 1 335 ? -44.42526 -58.83428 -54.47922 1.000 150.64703 ? 308 THR   A CG2  1 
ATOM   2361 N  N    . ILE   A 1 336 ? -41.42702 -56.98838 -51.25386 1.000 149.38862 ? 309 ILE   A N    1 
ATOM   2362 C  CA   . ILE   A 1 336 ? -40.99406 -55.91316 -50.37168 1.000 138.62862 ? 309 ILE   A CA   1 
ATOM   2363 C  C    . ILE   A 1 336 ? -39.65931 -55.35082 -50.84917 1.000 135.14820 ? 309 ILE   A C    1 
ATOM   2364 O  O    . ILE   A 1 336 ? -38.91604 -55.98433 -51.60256 1.000 146.43261 ? 309 ILE   A O    1 
ATOM   2365 C  CB   . ILE   A 1 336 ? -40.90023 -56.40500 -48.91733 1.000 124.71441 ? 309 ILE   A CB   1 
ATOM   2366 C  CG1  . ILE   A 1 336 ? -39.88650 -57.54568 -48.81247 1.000 119.12774 ? 309 ILE   A CG1  1 
ATOM   2367 C  CG2  . ILE   A 1 336 ? -42.26430 -56.85188 -48.41897 1.000 173.24489 ? 309 ILE   A CG2  1 
ATOM   2368 C  CD1  . ILE   A 1 336 ? -39.79119 -58.15776 -47.43525 1.000 137.23035 ? 309 ILE   A CD1  1 
ATOM   2369 N  N    . GLN   A 1 337 ? -39.35486 -54.13735 -50.39614 1.000 123.02020 ? 310 GLN   A N    1 
ATOM   2370 C  CA   . GLN   A 1 337 ? -38.06399 -53.51159 -50.67301 1.000 137.38339 ? 310 GLN   A CA   1 
ATOM   2371 C  C    . GLN   A 1 337 ? -36.99416 -54.23282 -49.86430 1.000 140.10549 ? 310 GLN   A C    1 
ATOM   2372 O  O    . GLN   A 1 337 ? -36.88097 -54.04600 -48.65095 1.000 142.22879 ? 310 GLN   A O    1 
ATOM   2373 C  CB   . GLN   A 1 337 ? -38.10407 -52.02517 -50.33648 1.000 128.58650 ? 310 GLN   A CB   1 
ATOM   2374 C  CG   . GLN   A 1 337 ? -38.90601 -51.18345 -51.31572 1.000 127.11268 ? 310 GLN   A CG   1 
ATOM   2375 C  CD   . GLN   A 1 337 ? -38.90421 -49.70987 -50.95509 1.000 166.01456 ? 310 GLN   A CD   1 
ATOM   2376 O  OE1  . GLN   A 1 337 ? -38.81060 -49.34562 -49.78271 1.000 170.47256 ? 310 GLN   A OE1  1 
ATOM   2377 N  NE2  . GLN   A 1 337 ? -39.00208 -48.85320 -51.96531 1.000 200.68785 ? 310 GLN   A NE2  1 
ATOM   2378 N  N    . ASN   A 1 338 ? -36.20696 -55.07110 -50.53535 1.000 114.18507 ? 311 ASN   A N    1 
ATOM   2379 C  CA   . ASN   A 1 338 ? -35.17036 -55.86111 -49.88094 1.000 120.82731 ? 311 ASN   A CA   1 
ATOM   2380 C  C    . ASN   A 1 338 ? -33.91029 -55.80804 -50.72917 1.000 129.89442 ? 311 ASN   A C    1 
ATOM   2381 O  O    . ASN   A 1 338 ? -33.91643 -56.25725 -51.87927 1.000 144.35611 ? 311 ASN   A O    1 
ATOM   2382 C  CB   . ASN   A 1 338 ? -35.62658 -57.31044 -49.68029 1.000 111.28107 ? 311 ASN   A CB   1 
ATOM   2383 C  CG   . ASN   A 1 338 ? -34.62527 -58.13603 -48.89631 1.000 122.93719 ? 311 ASN   A CG   1 
ATOM   2384 O  OD1  . ASN   A 1 338 ? -33.86336 -57.60653 -48.08926 1.000 144.96523 ? 311 ASN   A OD1  1 
ATOM   2385 N  ND2  . ASN   A 1 338 ? -34.62327 -59.44305 -49.13094 1.000 113.98264 ? 311 ASN   A ND2  1 
ATOM   2386 N  N    . ASN   A 1 339 ? -32.83745 -55.25690 -50.16578 1.000 121.52216 ? 312 ASN   A N    1 
ATOM   2387 C  CA   . ASN   A 1 339 ? -31.54860 -55.18149 -50.83921 1.000 134.22931 ? 312 ASN   A CA   1 
ATOM   2388 C  C    . ASN   A 1 339 ? -30.64700 -56.36510 -50.51502 1.000 134.97161 ? 312 ASN   A C    1 
ATOM   2389 O  O    . ASN   A 1 339 ? -29.47852 -56.36370 -50.91482 1.000 144.77536 ? 312 ASN   A O    1 
ATOM   2390 C  CB   . ASN   A 1 339 ? -30.83524 -53.87632 -50.47310 1.000 127.04927 ? 312 ASN   A CB   1 
ATOM   2391 C  CG   . ASN   A 1 339 ? -31.59463 -52.64732 -50.93089 1.000 131.71894 ? 312 ASN   A CG   1 
ATOM   2392 O  OD1  . ASN   A 1 339 ? -32.35331 -52.69672 -51.89911 1.000 153.25629 ? 312 ASN   A OD1  1 
ATOM   2393 N  ND2  . ASN   A 1 339 ? -31.38985 -51.53321 -50.23763 1.000 122.80719 ? 312 ASN   A ND2  1 
ATOM   2394 N  N    . THR   A 1 340 ? -31.16453 -57.36958 -49.80951 1.000 122.99118 ? 313 THR   A N    1 
ATOM   2395 C  CA   . THR   A 1 340 ? -30.34562 -58.49192 -49.36880 1.000 130.99302 ? 313 THR   A CA   1 
ATOM   2396 C  C    . THR   A 1 340 ? -29.74742 -59.23300 -50.55827 1.000 134.70502 ? 313 THR   A C    1 
ATOM   2397 O  O    . THR   A 1 340 ? -30.45340 -59.58813 -51.50651 1.000 154.19465 ? 313 THR   A O    1 
ATOM   2398 C  CB   . THR   A 1 340 ? -31.18239 -59.44974 -48.51896 1.000 118.36436 ? 313 THR   A CB   1 
ATOM   2399 O  OG1  . THR   A 1 340 ? -31.66899 -58.76282 -47.35865 1.000 142.87992 ? 313 THR   A OG1  1 
ATOM   2400 C  CG2  . THR   A 1 340 ? -30.34942 -60.64518 -48.08192 1.000 121.28358 ? 313 THR   A CG2  1 
ATOM   2401 N  N    . LYS   A 1 341 ? -28.43411 -59.45842 -50.50325 1.000 121.63033 ? 314 LYS   A N    1 
ATOM   2402 C  CA   . LYS   A 1 341 ? -27.69298 -60.20283 -51.52243 1.000 128.89768 ? 314 LYS   A CA   1 
ATOM   2403 C  C    . LYS   A 1 341 ? -26.90340 -61.28684 -50.79124 1.000 130.52898 ? 314 LYS   A C    1 
ATOM   2404 O  O    . LYS   A 1 341 ? -25.74267 -61.08034 -50.42671 1.000 122.56342 ? 314 LYS   A O    1 
ATOM   2405 C  CB   . LYS   A 1 341 ? -26.77959 -59.28032 -52.32622 1.000 138.45820 ? 314 LYS   A CB   1 
ATOM   2406 C  CG   . LYS   A 1 341 ? -27.45362 -58.03369 -52.87921 1.000 130.50428 ? 314 LYS   A CG   1 
ATOM   2407 C  CD   . LYS   A 1 341 ? -28.52879 -58.38397 -53.89219 1.000 135.56595 ? 314 LYS   A CD   1 
ATOM   2408 C  CE   . LYS   A 1 341 ? -29.01059 -57.14637 -54.63180 1.000 125.46490 ? 314 LYS   A CE   1 
ATOM   2409 N  NZ   . LYS   A 1 341 ? -29.51615 -56.10002 -53.70268 1.000 118.76355 ? 314 LYS   A NZ   1 
ATOM   2410 N  N    . LEU   A 1 342 ? -27.53161 -62.44109 -50.57860 1.000 126.39352 ? 315 LEU   A N    1 
ATOM   2411 C  CA   . LEU   A 1 342 ? -26.95617 -63.51456 -49.77971 1.000 113.99829 ? 315 LEU   A CA   1 
ATOM   2412 C  C    . LEU   A 1 342 ? -26.76384 -64.76634 -50.62476 1.000 119.46603 ? 315 LEU   A C    1 
ATOM   2413 O  O    . LEU   A 1 342 ? -27.63565 -65.13100 -51.41884 1.000 135.16614 ? 315 LEU   A O    1 
ATOM   2414 C  CB   . LEU   A 1 342 ? -27.84818 -63.83501 -48.57229 1.000 114.16473 ? 315 LEU   A CB   1 
ATOM   2415 C  CG   . LEU   A 1 342 ? -27.48562 -65.06800 -47.73984 1.000 128.98592 ? 315 LEU   A CG   1 
ATOM   2416 C  CD1  . LEU   A 1 342 ? -26.11764 -64.90514 -47.09546 1.000 144.17192 ? 315 LEU   A CD1  1 
ATOM   2417 C  CD2  . LEU   A 1 342 ? -28.55050 -65.34744 -46.68794 1.000 102.61658 ? 315 LEU   A CD2  1 
ATOM   2418 N  N    . LEU   A 1 343 ? -25.62093 -65.42606 -50.44184 1.000 118.42078 ? 316 LEU   A N    1 
ATOM   2419 C  CA   . LEU   A 1 343 ? -25.33045 -66.70123 -51.08314 1.000 115.47104 ? 316 LEU   A CA   1 
ATOM   2420 C  C    . LEU   A 1 343 ? -24.76923 -67.65396 -50.03891 1.000 122.96320 ? 316 LEU   A C    1 
ATOM   2421 O  O    . LEU   A 1 343 ? -23.85870 -67.28927 -49.29073 1.000 136.57266 ? 316 LEU   A O    1 
ATOM   2422 C  CB   . LEU   A 1 343 ? -24.33933 -66.52389 -52.24030 1.000 118.23915 ? 316 LEU   A CB   1 
ATOM   2423 C  CG   . LEU   A 1 343 ? -23.66434 -67.77285 -52.81291 1.000 104.81231 ? 316 LEU   A CG   1 
ATOM   2424 C  CD1  . LEU   A 1 343 ? -24.68985 -68.77852 -53.30352 1.000 103.86004 ? 316 LEU   A CD1  1 
ATOM   2425 C  CD2  . LEU   A 1 343 ? -22.71192 -67.39009 -53.93558 1.000 126.07943 ? 316 LEU   A CD2  1 
ATOM   2426 N  N    . ILE   A 1 344 ? -25.31514 -68.86560 -49.98198 1.000 130.94800 ? 317 ILE   A N    1 
ATOM   2427 C  CA   . ILE   A 1 344 ? -24.89022 -69.87905 -49.02453 1.000 136.92407 ? 317 ILE   A CA   1 
ATOM   2428 C  C    . ILE   A 1 344 ? -24.67076 -71.18159 -49.77686 1.000 146.78871 ? 317 ILE   A C    1 
ATOM   2429 O  O    . ILE   A 1 344 ? -25.56031 -71.64416 -50.49952 1.000 143.86077 ? 317 ILE   A O    1 
ATOM   2430 C  CB   . ILE   A 1 344 ? -25.92110 -70.07089 -47.89654 1.000 142.87867 ? 317 ILE   A CB   1 
ATOM   2431 C  CG1  . ILE   A 1 344 ? -26.04312 -68.79113 -47.06779 1.000 127.43060 ? 317 ILE   A CG1  1 
ATOM   2432 C  CG2  . ILE   A 1 344 ? -25.53719 -71.25229 -47.01646 1.000 137.86652 ? 317 ILE   A CG2  1 
ATOM   2433 C  CD1  . ILE   A 1 344 ? -27.13066 -68.84432 -46.02934 1.000 139.69711 ? 317 ILE   A CD1  1 
ATOM   2434 N  N    . VAL   A 1 345 ? -23.49102 -71.77030 -49.60994 1.000 156.08379 ? 318 VAL   A N    1 
ATOM   2435 C  CA   . VAL   A 1 345 ? -23.10449 -72.97649 -50.33008 1.000 147.19380 ? 318 VAL   A CA   1 
ATOM   2436 C  C    . VAL   A 1 345 ? -22.74752 -74.05580 -49.31796 1.000 152.64187 ? 318 VAL   A C    1 
ATOM   2437 O  O    . VAL   A 1 345 ? -21.80079 -73.89314 -48.53406 1.000 167.16397 ? 318 VAL   A O    1 
ATOM   2438 C  CB   . VAL   A 1 345 ? -21.93515 -72.71869 -51.29264 1.000 126.08600 ? 318 VAL   A CB   1 
ATOM   2439 C  CG1  . VAL   A 1 345 ? -21.60172 -73.98698 -52.06281 1.000 148.48668 ? 318 VAL   A CG1  1 
ATOM   2440 C  CG2  . VAL   A 1 345 ? -22.27865 -71.58328 -52.24886 1.000 104.36442 ? 318 VAL   A CG2  1 
ATOM   2441 N  N    . ASP   A 1 346 ? -23.52739 -75.14330 -49.32603 1.000 143.57474 ? 319 ASP   A N    1 
ATOM   2442 C  CA   . ASP   A 1 346 ? -23.20389 -76.38725 -48.62174 1.000 154.29786 ? 319 ASP   A CA   1 
ATOM   2443 C  C    . ASP   A 1 346 ? -23.08860 -76.18190 -47.11410 1.000 165.83485 ? 319 ASP   A C    1 
ATOM   2444 O  O    . ASP   A 1 346 ? -22.41892 -76.95185 -46.42283 1.000 165.53319 ? 319 ASP   A O    1 
ATOM   2445 C  CB   . ASP   A 1 346 ? -21.92368 -77.01477 -49.18315 1.000 181.69472 ? 319 ASP   A CB   1 
ATOM   2446 C  CG   . ASP   A 1 346 ? -22.09930 -77.52007 -50.59870 1.000 168.56969 ? 319 ASP   A CG   1 
ATOM   2447 O  OD1  . ASP   A 1 346 ? -23.19567 -77.31994 -51.16309 1.000 158.73542 ? 319 ASP   A OD1  1 
ATOM   2448 O  OD2  . ASP   A 1 346 ? -21.14787 -78.11898 -51.14208 1.000 165.78230 ? 319 ASP   A OD2  1 
ATOM   2449 N  N    . ASP   A 1 347 ? -23.73297 -75.13241 -46.59825 1.000 161.39138 ? 320 ASP   A N    1 
ATOM   2450 C  CA   . ASP   A 1 347 ? -23.66521 -74.78041 -45.17862 1.000 177.52791 ? 320 ASP   A CA   1 
ATOM   2451 C  C    . ASP   A 1 347 ? -22.21316 -74.68148 -44.71883 1.000 173.18376 ? 320 ASP   A C    1 
ATOM   2452 O  O    . ASP   A 1 347 ? -21.88088 -74.93243 -43.56024 1.000 158.26830 ? 320 ASP   A O    1 
ATOM   2453 C  CB   . ASP   A 1 347 ? -24.46843 -75.76892 -44.32733 1.000 165.52680 ? 320 ASP   A CB   1 
ATOM   2454 C  CG   . ASP   A 1 347 ? -25.93326 -75.84561 -44.75930 1.000 168.97464 ? 320 ASP   A CG   1 
ATOM   2455 O  OD1  . ASP   A 1 347 ? -26.28888 -75.18585 -45.75922 1.000 182.65158 ? 320 ASP   A OD1  1 
ATOM   2456 O  OD2  . ASP   A 1 347 ? -26.73119 -76.55824 -44.11224 1.000 154.78455 ? 320 ASP   A OD2  1 
ATOM   2457 N  N    . GLU   A 1 348 ? -21.34283 -74.28497 -45.64809 1.000 167.99374 ? 321 GLU   A N    1 
ATOM   2458 C  CA   . GLU   A 1 348 ? -19.90951 -74.13351 -45.40476 1.000 158.39746 ? 321 GLU   A CA   1 
ATOM   2459 C  C    . GLU   A 1 348 ? -19.33598 -72.83350 -45.95158 1.000 150.88696 ? 321 GLU   A C    1 
ATOM   2460 O  O    . GLU   A 1 348 ? -18.32100 -72.35973 -45.42957 1.000 158.39877 ? 321 GLU   A O    1 
ATOM   2461 C  CB   . GLU   A 1 348 ? -19.13005 -75.31122 -46.01804 1.000 158.24442 ? 321 GLU   A CB   1 
ATOM   2462 C  CG   . GLU   A 1 348 ? -17.69188 -75.43659 -45.56282 1.000 190.88690 ? 321 GLU   A CG   1 
ATOM   2463 C  CD   . GLU   A 1 348 ? -17.04110 -76.67393 -46.13305 1.000 203.65319 ? 321 GLU   A CD   1 
ATOM   2464 O  OE1  . GLU   A 1 348 ? -17.72792 -77.39659 -46.88420 1.000 181.66121 ? 321 GLU   A OE1  1 
ATOM   2465 O  OE2  . GLU   A 1 348 ? -15.85293 -76.92481 -45.83253 1.000 211.80820 ? 321 GLU   A OE2  1 
ATOM   2466 N  N    . TYR   A 1 349 ? -19.94832 -72.21848 -46.96121 1.000 132.66137 ? 322 TYR   A N    1 
ATOM   2467 C  CA   . TYR   A 1 349 ? -19.47813 -70.95282 -47.50688 1.000 136.69207 ? 322 TYR   A CA   1 
ATOM   2468 C  C    . TYR   A 1 349 ? -20.62283 -69.94754 -47.52095 1.000 144.38600 ? 322 TYR   A C    1 
ATOM   2469 O  O    . TYR   A 1 349 ? -21.76200 -70.29454 -47.84856 1.000 146.75638 ? 322 TYR   A O    1 
ATOM   2470 C  CB   . TYR   A 1 349 ? -18.90070 -71.14443 -48.92187 1.000 142.44783 ? 322 TYR   A CB   1 
ATOM   2471 C  CG   . TYR   A 1 349 ? -18.62634 -69.85588 -49.65817 1.000 148.05551 ? 322 TYR   A CG   1 
ATOM   2472 C  CD1  . TYR   A 1 349 ? -17.49302 -69.10281 -49.38517 1.000 141.16672 ? 322 TYR   A CD1  1 
ATOM   2473 C  CD2  . TYR   A 1 349 ? -19.49639 -69.39815 -50.63469 1.000 146.98046 ? 322 TYR   A CD2  1 
ATOM   2474 C  CE1  . TYR   A 1 349 ? -17.23629 -67.91634 -50.06219 1.000 147.18708 ? 322 TYR   A CE1  1 
ATOM   2475 C  CE2  . TYR   A 1 349 ? -19.25292 -68.21648 -51.31929 1.000 137.64948 ? 322 TYR   A CE2  1 
ATOM   2476 C  CZ   . TYR   A 1 349 ? -18.12034 -67.47798 -51.02914 1.000 145.62232 ? 322 TYR   A CZ   1 
ATOM   2477 O  OH   . TYR   A 1 349 ? -17.87060 -66.30354 -51.70420 1.000 157.15961 ? 322 TYR   A OH   1 
ATOM   2478 N  N    . VAL   A 1 350 ? -20.32113 -68.70363 -47.14898 1.000 145.24087 ? 323 VAL   A N    1 
ATOM   2479 C  CA   . VAL   A 1 350 ? -21.29629 -67.61976 -47.17821 1.000 124.22107 ? 323 VAL   A CA   1 
ATOM   2480 C  C    . VAL   A 1 350 ? -20.68980 -66.42204 -47.89986 1.000 133.37601 ? 323 VAL   A C    1 
ATOM   2481 O  O    . VAL   A 1 350 ? -19.49795 -66.12515 -47.75302 1.000 152.43225 ? 323 VAL   A O    1 
ATOM   2482 C  CB   . VAL   A 1 350 ? -21.77849 -67.23029 -45.76093 1.000 127.18126 ? 323 VAL   A CB   1 
ATOM   2483 C  CG1  . VAL   A 1 350 ? -20.63350 -66.69544 -44.91372 1.000 124.49875 ? 323 VAL   A CG1  1 
ATOM   2484 C  CG2  . VAL   A 1 350 ? -22.91717 -66.23169 -45.83475 1.000 107.86290 ? 323 VAL   A CG2  1 
ATOM   2485 N  N    . HIS   A 1 351 ? -21.52227 -65.73785 -48.68323 1.000 134.99376 ? 324 HIS   A N    1 
ATOM   2486 C  CA   . HIS   A 1 351 ? -21.10095 -64.62609 -49.53078 1.000 139.39175 ? 324 HIS   A CA   1 
ATOM   2487 C  C    . HIS   A 1 351 ? -22.17493 -63.54887 -49.46702 1.000 137.65610 ? 324 HIS   A C    1 
ATOM   2488 O  O    . HIS   A 1 351 ? -23.29762 -63.75637 -49.94053 1.000 124.19308 ? 324 HIS   A O    1 
ATOM   2489 C  CB   . HIS   A 1 351 ? -20.87479 -65.09462 -50.96955 1.000 132.12963 ? 324 HIS   A CB   1 
ATOM   2490 C  CG   . HIS   A 1 351 ? -20.87425 -63.98893 -51.97882 1.000 133.54274 ? 324 HIS   A CG   1 
ATOM   2491 N  ND1  . HIS   A 1 351 ? -19.76429 -63.21346 -52.23720 1.000 140.24849 ? 324 HIS   A ND1  1 
ATOM   2492 C  CD2  . HIS   A 1 351 ? -21.84999 -63.53402 -52.79991 1.000 126.24990 ? 324 HIS   A CD2  1 
ATOM   2493 C  CE1  . HIS   A 1 351 ? -20.05775 -62.32593 -53.17085 1.000 125.77964 ? 324 HIS   A CE1  1 
ATOM   2494 N  NE2  . HIS   A 1 351 ? -21.31727 -62.49885 -53.52881 1.000 136.44013 ? 324 HIS   A NE2  1 
ATOM   2495 N  N    . ILE   A 1 352 ? -21.83193 -62.40074 -48.89070 1.000 139.05175 ? 325 ILE   A N    1 
ATOM   2496 C  CA   . ILE   A 1 352 ? -22.75244 -61.27843 -48.75937 1.000 127.50387 ? 325 ILE   A CA   1 
ATOM   2497 C  C    . ILE   A 1 352 ? -22.17118 -60.09068 -49.51130 1.000 133.79777 ? 325 ILE   A C    1 
ATOM   2498 O  O    . ILE   A 1 352 ? -21.00918 -59.72275 -49.30341 1.000 149.69447 ? 325 ILE   A O    1 
ATOM   2499 C  CB   . ILE   A 1 352 ? -23.01408 -60.92185 -47.28503 1.000 120.31395 ? 325 ILE   A CB   1 
ATOM   2500 C  CG1  . ILE   A 1 352 ? -23.60069 -62.12427 -46.54291 1.000 109.55671 ? 325 ILE   A CG1  1 
ATOM   2501 C  CG2  . ILE   A 1 352 ? -23.95360 -59.72883 -47.18686 1.000 130.91467 ? 325 ILE   A CG2  1 
ATOM   2502 C  CD1  . ILE   A 1 352 ? -23.97069 -61.83484 -45.10656 1.000 110.56960 ? 325 ILE   A CD1  1 
ATOM   2503 N  N    . THR   A 1 353 ? -22.98076 -59.48706 -50.37723 1.000 130.03416 ? 326 THR   A N    1 
ATOM   2504 C  CA   . THR   A 1 353 ? -22.52772 -58.38949 -51.21619 1.000 140.07194 ? 326 THR   A CA   1 
ATOM   2505 C  C    . THR   A 1 353 ? -23.61825 -57.33057 -51.29084 1.000 133.37315 ? 326 THR   A C    1 
ATOM   2506 O  O    . THR   A 1 353 ? -24.71061 -57.48687 -50.73662 1.000 148.03169 ? 326 THR   A O    1 
ATOM   2507 C  CB   . THR   A 1 353 ? -22.15103 -58.88239 -52.61873 1.000 134.08034 ? 326 THR   A CB   1 
ATOM   2508 O  OG1  . THR   A 1 353 ? -21.91676 -57.75855 -53.47639 1.000 148.41881 ? 326 THR   A OG1  1 
ATOM   2509 C  CG2  . THR   A 1 353 ? -23.26609 -59.73610 -53.20138 1.000 123.32081 ? 326 THR   A CG2  1 
ATOM   2510 N  N    . SER   A 1 354 ? -23.30292 -56.23331 -51.97732 1.000 119.01195 ? 327 SER   A N    1 
ATOM   2511 C  CA   . SER   A 1 354 ? -24.27692 -55.19417 -52.27401 1.000 133.60232 ? 327 SER   A CA   1 
ATOM   2512 C  C    . SER   A 1 354 ? -24.74517 -55.22145 -53.72032 1.000 133.06607 ? 327 SER   A C    1 
ATOM   2513 O  O    . SER   A 1 354 ? -25.76700 -54.60278 -54.03737 1.000 145.61707 ? 327 SER   A O    1 
ATOM   2514 C  CB   . SER   A 1 354 ? -23.69280 -53.81161 -51.96112 1.000 164.57167 ? 327 SER   A CB   1 
ATOM   2515 O  OG   . SER   A 1 354 ? -22.50762 -53.57931 -52.70250 1.000 156.39854 ? 327 SER   A OG   1 
ATOM   2516 N  N    . ALA   A 1 355 ? -24.02893 -55.92080 -54.59368 1.000 126.49264 ? 328 ALA   A N    1 
ATOM   2517 C  CA   . ALA   A 1 355 ? -24.40302 -56.03406 -55.99305 1.000 141.39796 ? 328 ALA   A CA   1 
ATOM   2518 C  C    . ALA   A 1 355 ? -25.22277 -57.29644 -56.22537 1.000 144.90116 ? 328 ALA   A C    1 
ATOM   2519 O  O    . ALA   A 1 355 ? -25.11157 -58.28004 -55.48870 1.000 140.59742 ? 328 ALA   A O    1 
ATOM   2520 C  CB   . ALA   A 1 355 ? -23.16193 -56.04761 -56.88523 1.000 134.23180 ? 328 ALA   A CB   1 
ATOM   2521 N  N    . ASN   A 1 356 ? -26.05038 -57.25772 -57.26345 1.000 141.66218 ? 329 ASN   A N    1 
ATOM   2522 C  CA   . ASN   A 1 356 ? -26.90889 -58.37839 -57.61093 1.000 133.76222 ? 329 ASN   A CA   1 
ATOM   2523 C  C    . ASN   A 1 356 ? -26.23624 -59.26427 -58.65355 1.000 147.52394 ? 329 ASN   A C    1 
ATOM   2524 O  O    . ASN   A 1 356 ? -25.47289 -58.79244 -59.50079 1.000 154.89478 ? 329 ASN   A O    1 
ATOM   2525 C  CB   . ASN   A 1 356 ? -28.25616 -57.87682 -58.13438 1.000 143.13635 ? 329 ASN   A CB   1 
ATOM   2526 C  CG   . ASN   A 1 356 ? -29.21598 -59.00472 -58.45275 1.000 148.34405 ? 329 ASN   A CG   1 
ATOM   2527 O  OD1  . ASN   A 1 356 ? -29.90268 -59.51920 -57.57051 1.000 156.84749 ? 329 ASN   A OD1  1 
ATOM   2528 N  ND2  . ASN   A 1 356 ? -29.27052 -59.39394 -59.72077 1.000 155.65298 ? 329 ASN   A ND2  1 
ATOM   2529 N  N    . PHE   A 1 357 ? -26.52483 -60.56412 -58.57518 1.000 130.73919 ? 330 PHE   A N    1 
ATOM   2530 C  CA   . PHE   A 1 357 ? -25.97239 -61.54078 -59.50588 1.000 139.53717 ? 330 PHE   A CA   1 
ATOM   2531 C  C    . PHE   A 1 357 ? -26.51818 -61.31907 -60.90985 1.000 136.34489 ? 330 PHE   A C    1 
ATOM   2532 O  O    . PHE   A 1 357 ? -27.56832 -61.86393 -61.26673 1.000 140.69075 ? 330 PHE   A O    1 
ATOM   2533 C  CB   . PHE   A 1 357 ? -26.28752 -62.96529 -59.04513 1.000 135.51501 ? 330 PHE   A CB   1 
ATOM   2534 C  CG   . PHE   A 1 357 ? -25.54099 -63.38826 -57.81255 1.000 137.38932 ? 330 PHE   A CG   1 
ATOM   2535 C  CD1  . PHE   A 1 357 ? -24.34578 -62.78225 -57.46179 1.000 141.82432 ? 330 PHE   A CD1  1 
ATOM   2536 C  CD2  . PHE   A 1 357 ? -26.03285 -64.40226 -57.00812 1.000 144.63869 ? 330 PHE   A CD2  1 
ATOM   2537 C  CE1  . PHE   A 1 357 ? -23.65917 -63.17798 -56.32939 1.000 142.35988 ? 330 PHE   A CE1  1 
ATOM   2538 C  CE2  . PHE   A 1 357 ? -25.35094 -64.80245 -55.87430 1.000 127.85514 ? 330 PHE   A CE2  1 
ATOM   2539 C  CZ   . PHE   A 1 357 ? -24.16292 -64.18912 -55.53457 1.000 124.54365 ? 330 PHE   A CZ   1 
ATOM   2540 N  N    . ASP   A 1 358 ? -25.81482 -60.52876 -61.71441 1.000 128.80318 ? 331 ASP   A N    1 
ATOM   2541 C  CA   . ASP   A 1 358 ? -26.22011 -60.29677 -63.09426 1.000 144.06213 ? 331 ASP   A CA   1 
ATOM   2542 C  C    . ASP   A 1 358 ? -25.00236 -59.84287 -63.89220 1.000 151.31593 ? 331 ASP   A C    1 
ATOM   2543 O  O    . ASP   A 1 358 ? -23.88001 -59.80145 -63.38417 1.000 157.24139 ? 331 ASP   A O    1 
ATOM   2544 C  CB   . ASP   A 1 358 ? -27.36559 -59.28320 -63.16831 1.000 151.21648 ? 331 ASP   A CB   1 
ATOM   2545 C  CG   . ASP   A 1 358 ? -26.97098 -57.91085 -62.65950 1.000 154.42981 ? 331 ASP   A CG   1 
ATOM   2546 O  OD1  . ASP   A 1 358 ? -26.30050 -57.16934 -63.40954 1.000 154.71679 ? 331 ASP   A OD1  1 
ATOM   2547 O  OD2  . ASP   A 1 358 ? -27.34383 -57.56865 -61.51695 1.000 157.13492 ? 331 ASP   A OD2  1 
ATOM   2548 N  N    . GLY   A 1 359 ? -25.24014 -59.49349 -65.15727 1.000 153.43903 ? 332 GLY   A N    1 
ATOM   2549 C  CA   . GLY   A 1 359 ? -24.13635 -59.14924 -66.04060 1.000 152.89312 ? 332 GLY   A CA   1 
ATOM   2550 C  C    . GLY   A 1 359 ? -23.58614 -57.75669 -65.79792 1.000 139.87187 ? 332 GLY   A C    1 
ATOM   2551 O  O    . GLY   A 1 359 ? -22.37707 -57.57646 -65.63179 1.000 151.90214 ? 332 GLY   A O    1 
ATOM   2552 N  N    . THR   A 1 360 ? -24.46734 -56.75766 -65.78635 1.000 135.95602 ? 333 THR   A N    1 
ATOM   2553 C  CA   . THR   A 1 360 ? -24.02162 -55.37462 -65.63390 1.000 138.96112 ? 333 THR   A CA   1 
ATOM   2554 C  C    . THR   A 1 360 ? -23.21184 -55.18721 -64.35322 1.000 154.53651 ? 333 THR   A C    1 
ATOM   2555 O  O    . THR   A 1 360 ? -22.14134 -54.56205 -64.36217 1.000 169.65920 ? 333 THR   A O    1 
ATOM   2556 C  CB   . THR   A 1 360 ? -25.23026 -54.43732 -65.64885 1.000 139.67267 ? 333 THR   A CB   1 
ATOM   2557 O  OG1  . THR   A 1 360 ? -25.98559 -54.65475 -66.84287 1.000 159.04830 ? 333 THR   A OG1  1 
ATOM   2558 C  CG2  . THR   A 1 360 ? -24.79025 -52.98820 -65.59668 1.000 167.48054 ? 333 THR   A CG2  1 
ATOM   2559 N  N    . HIS   A 1 361 ? -23.70465 -55.73571 -63.24150 1.000 144.01568 ? 334 HIS   A N    1 
ATOM   2560 C  CA   . HIS   A 1 361 ? -23.04663 -55.55007 -61.95249 1.000 153.66568 ? 334 HIS   A CA   1 
ATOM   2561 C  C    . HIS   A 1 361 ? -21.64801 -56.15781 -61.94826 1.000 156.82681 ? 334 HIS   A C    1 
ATOM   2562 O  O    . HIS   A 1 361 ? -20.65451 -55.46242 -61.70865 1.000 158.87627 ? 334 HIS   A O    1 
ATOM   2563 C  CB   . HIS   A 1 361 ? -23.90555 -56.15431 -60.84083 1.000 129.99553 ? 334 HIS   A CB   1 
ATOM   2564 C  CG   . HIS   A 1 361 ? -25.06998 -55.30124 -60.44728 1.000 138.07294 ? 334 HIS   A CG   1 
ATOM   2565 N  ND1  . HIS   A 1 361 ? -25.23013 -54.80701 -59.17107 1.000 141.21506 ? 334 HIS   A ND1  1 
ATOM   2566 C  CD2  . HIS   A 1 361 ? -26.12609 -54.84669 -61.16223 1.000 158.51161 ? 334 HIS   A CD2  1 
ATOM   2567 C  CE1  . HIS   A 1 361 ? -26.33829 -54.09060 -59.11450 1.000 144.54162 ? 334 HIS   A CE1  1 
ATOM   2568 N  NE2  . HIS   A 1 361 ? -26.90101 -54.09890 -60.30945 1.000 153.09622 ? 334 HIS   A NE2  1 
ATOM   2569 N  N    . TYR   A 1 362 ? -21.54924 -57.45870 -62.21469 1.000 142.26784 ? 335 TYR   A N    1 
ATOM   2570 C  CA   . TYR   A 1 362 ? -20.26537 -58.14529 -62.14073 1.000 130.42372 ? 335 TYR   A CA   1 
ATOM   2571 C  C    . TYR   A 1 362 ? -19.39177 -57.92485 -63.36812 1.000 136.12265 ? 335 TYR   A C    1 
ATOM   2572 O  O    . TYR   A 1 362 ? -18.30372 -58.50618 -63.44343 1.000 134.76033 ? 335 TYR   A O    1 
ATOM   2573 C  CB   . TYR   A 1 362 ? -20.48269 -59.64325 -61.91416 1.000 120.56376 ? 335 TYR   A CB   1 
ATOM   2574 C  CG   . TYR   A 1 362 ? -20.77170 -59.98197 -60.47111 1.000 111.26666 ? 335 TYR   A CG   1 
ATOM   2575 C  CD1  . TYR   A 1 362 ? -22.05791 -59.88499 -59.95836 1.000 125.08883 ? 335 TYR   A CD1  1 
ATOM   2576 C  CD2  . TYR   A 1 362 ? -19.75411 -60.38274 -59.61618 1.000 132.03563 ? 335 TYR   A CD2  1 
ATOM   2577 C  CE1  . TYR   A 1 362 ? -22.32406 -60.18671 -58.63506 1.000 129.97735 ? 335 TYR   A CE1  1 
ATOM   2578 C  CE2  . TYR   A 1 362 ? -20.01017 -60.68728 -58.29269 1.000 150.10482 ? 335 TYR   A CE2  1 
ATOM   2579 C  CZ   . TYR   A 1 362 ? -21.29616 -60.58765 -57.80732 1.000 149.09402 ? 335 TYR   A CZ   1 
ATOM   2580 O  OH   . TYR   A 1 362 ? -21.55368 -60.88933 -56.48986 1.000 163.64139 ? 335 TYR   A OH   1 
ATOM   2581 N  N    . GLN   A 1 363 ? -19.82915 -57.10635 -64.32335 1.000 142.05377 ? 336 GLN   A N    1 
ATOM   2582 C  CA   . GLN   A 1 363 ? -18.99608 -56.73875 -65.45909 1.000 139.78425 ? 336 GLN   A CA   1 
ATOM   2583 C  C    . GLN   A 1 363 ? -18.51708 -55.29677 -65.42521 1.000 142.51568 ? 336 GLN   A C    1 
ATOM   2584 O  O    . GLN   A 1 363 ? -17.45258 -55.00572 -65.97371 1.000 159.42845 ? 336 GLN   A O    1 
ATOM   2585 C  CB   . GLN   A 1 363 ? -19.74696 -56.97804 -66.77650 1.000 156.75937 ? 336 GLN   A CB   1 
ATOM   2586 C  CG   . GLN   A 1 363 ? -19.83834 -58.43944 -67.19827 1.000 144.92530 ? 336 GLN   A CG   1 
ATOM   2587 C  CD   . GLN   A 1 363 ? -18.49964 -59.01932 -67.60481 1.000 157.80621 ? 336 GLN   A CD   1 
ATOM   2588 O  OE1  . GLN   A 1 363 ? -17.76567 -59.55676 -66.77583 1.000 175.71512 ? 336 GLN   A OE1  1 
ATOM   2589 N  NE2  . GLN   A 1 363 ? -18.17616 -58.91766 -68.88926 1.000 148.61007 ? 336 GLN   A NE2  1 
ATOM   2590 N  N    . ASN   A 1 364 ? -19.25946 -54.39121 -64.79570 1.000 150.02415 ? 337 ASN   A N    1 
ATOM   2591 C  CA   . ASN   A 1 364 ? -18.86468 -52.98727 -64.83940 1.000 170.14339 ? 337 ASN   A CA   1 
ATOM   2592 C  C    . ASN   A 1 364 ? -18.83744 -52.32192 -63.47138 1.000 163.58185 ? 337 ASN   A C    1 
ATOM   2593 O  O    . ASN   A 1 364 ? -17.97178 -51.47777 -63.22447 1.000 155.39547 ? 337 ASN   A O    1 
ATOM   2594 C  CB   . ASN   A 1 364 ? -19.80850 -52.21675 -65.77629 1.000 163.38648 ? 337 ASN   A CB   1 
ATOM   2595 C  CG   . ASN   A 1 364 ? -19.90308 -52.84645 -67.15325 1.000 172.78541 ? 337 ASN   A CG   1 
ATOM   2596 O  OD1  . ASN   A 1 364 ? -20.77611 -53.67557 -67.41056 1.000 153.71345 ? 337 ASN   A OD1  1 
ATOM   2597 N  ND2  . ASN   A 1 364 ? -18.99849 -52.45928 -68.04494 1.000 202.44431 ? 337 ASN   A ND2  1 
ATOM   2598 N  N    . HIS   A 1 365 ? -19.75302 -52.68025 -62.57595 1.000 157.72791 ? 338 HIS   A N    1 
ATOM   2599 C  CA   . HIS   A 1 365 ? -19.85404 -51.98867 -61.29882 1.000 151.92881 ? 338 HIS   A CA   1 
ATOM   2600 C  C    . HIS   A 1 365 ? -18.69214 -52.35175 -60.37992 1.000 148.36351 ? 338 HIS   A C    1 
ATOM   2601 O  O    . HIS   A 1 365 ? -18.12361 -53.44427 -60.45562 1.000 157.05010 ? 338 HIS   A O    1 
ATOM   2602 C  CB   . HIS   A 1 365 ? -21.18135 -52.31834 -60.61741 1.000 145.08984 ? 338 HIS   A CB   1 
ATOM   2603 C  CG   . HIS   A 1 365 ? -22.37965 -51.81304 -61.35763 1.000 143.74877 ? 338 HIS   A CG   1 
ATOM   2604 N  ND1  . HIS   A 1 365 ? -22.28325 -50.93422 -62.41477 1.000 149.70995 ? 338 HIS   A ND1  1 
ATOM   2605 C  CD2  . HIS   A 1 365 ? -23.70045 -52.06339 -61.19554 1.000 151.35480 ? 338 HIS   A CD2  1 
ATOM   2606 C  CE1  . HIS   A 1 365 ? -23.49285 -50.66447 -62.87187 1.000 152.10354 ? 338 HIS   A CE1  1 
ATOM   2607 N  NE2  . HIS   A 1 365 ? -24.37079 -51.33659 -62.14928 1.000 158.38621 ? 338 HIS   A NE2  1 
ATOM   2608 N  N    . GLY   A 1 366 ? -18.34164 -51.41211 -59.50431 1.000 141.26820 ? 339 GLY   A N    1 
ATOM   2609 C  CA   . GLY   A 1 366 ? -17.27142 -51.61750 -58.54891 1.000 157.13725 ? 339 GLY   A CA   1 
ATOM   2610 C  C    . GLY   A 1 366 ? -17.77278 -51.76692 -57.12937 1.000 141.53650 ? 339 GLY   A C    1 
ATOM   2611 O  O    . GLY   A 1 366 ? -18.42534 -50.86460 -56.59583 1.000 139.42995 ? 339 GLY   A O    1 
ATOM   2612 N  N    . PHE   A 1 367 ? -17.46846 -52.89995 -56.50221 1.000 149.67552 ? 340 PHE   A N    1 
ATOM   2613 C  CA   . PHE   A 1 367 ? -17.97957 -53.18450 -55.17150 1.000 121.68778 ? 340 PHE   A CA   1 
ATOM   2614 C  C    . PHE   A 1 367 ? -17.02771 -54.12459 -54.44710 1.000 139.87128 ? 340 PHE   A C    1 
ATOM   2615 O  O    . PHE   A 1 367 ? -16.11123 -54.70313 -55.03926 1.000 168.19231 ? 340 PHE   A O    1 
ATOM   2616 C  CB   . PHE   A 1 367 ? -19.39021 -53.78288 -55.23488 1.000 143.53454 ? 340 PHE   A CB   1 
ATOM   2617 C  CG   . PHE   A 1 367 ? -19.51925 -54.94897 -56.17864 1.000 139.76243 ? 340 PHE   A CG   1 
ATOM   2618 C  CD1  . PHE   A 1 367 ? -19.30083 -56.24459 -55.73779 1.000 139.02009 ? 340 PHE   A CD1  1 
ATOM   2619 C  CD2  . PHE   A 1 367 ? -19.87096 -54.74919 -57.50440 1.000 131.13781 ? 340 PHE   A CD2  1 
ATOM   2620 C  CE1  . PHE   A 1 367 ? -19.42398 -57.31823 -56.60246 1.000 128.59063 ? 340 PHE   A CE1  1 
ATOM   2621 C  CE2  . PHE   A 1 367 ? -19.99558 -55.81873 -58.37453 1.000 137.77357 ? 340 PHE   A CE2  1 
ATOM   2622 C  CZ   . PHE   A 1 367 ? -19.77442 -57.10523 -57.92159 1.000 139.26094 ? 340 PHE   A CZ   1 
ATOM   2623 N  N    . VAL   A 1 368 ? -17.25806 -54.26135 -53.14326 1.000 122.83493 ? 341 VAL   A N    1 
ATOM   2624 C  CA   . VAL   A 1 368 ? -16.53884 -55.20200 -52.29518 1.000 139.07566 ? 341 VAL   A CA   1 
ATOM   2625 C  C    . VAL   A 1 368 ? -17.55227 -56.15925 -51.68422 1.000 145.73857 ? 341 VAL   A C    1 
ATOM   2626 O  O    . VAL   A 1 368 ? -18.68451 -55.76888 -51.37797 1.000 145.24289 ? 341 VAL   A O    1 
ATOM   2627 C  CB   . VAL   A 1 368 ? -15.72352 -54.48267 -51.20012 1.000 132.43010 ? 341 VAL   A CB   1 
ATOM   2628 C  CG1  . VAL   A 1 368 ? -14.67140 -53.58773 -51.83279 1.000 158.55938 ? 341 VAL   A CG1  1 
ATOM   2629 C  CG2  . VAL   A 1 368 ? -16.63688 -53.67346 -50.29614 1.000 138.47594 ? 341 VAL   A CG2  1 
ATOM   2630 N  N    . SER   A 1 369 ? -17.14733 -57.41507 -51.51829 1.000 148.41651 ? 342 SER   A N    1 
ATOM   2631 C  CA   . SER   A 1 369 ? -18.03859 -58.47326 -51.06991 1.000 139.11544 ? 342 SER   A CA   1 
ATOM   2632 C  C    . SER   A 1 369 ? -17.37249 -59.28229 -49.96810 1.000 144.63244 ? 342 SER   A C    1 
ATOM   2633 O  O    . SER   A 1 369 ? -16.19164 -59.63414 -50.06522 1.000 152.98574 ? 342 SER   A O    1 
ATOM   2634 C  CB   . SER   A 1 369 ? -18.43189 -59.39636 -52.22929 1.000 133.76127 ? 342 SER   A CB   1 
ATOM   2635 O  OG   . SER   A 1 369 ? -18.99074 -58.65868 -53.30238 1.000 129.45795 ? 342 SER   A OG   1 
ATOM   2636 N  N    . PHE   A 1 370 ? -18.14536 -59.57182 -48.92525 1.000 146.69588 ? 343 PHE   A N    1 
ATOM   2637 C  CA   . PHE   A 1 370 ? -17.69082 -60.34259 -47.77954 1.000 152.79154 ? 343 PHE   A CA   1 
ATOM   2638 C  C    . PHE   A 1 370 ? -17.87605 -61.82630 -48.06836 1.000 143.46732 ? 343 PHE   A C    1 
ATOM   2639 O  O    . PHE   A 1 370 ? -18.94533 -62.24444 -48.52668 1.000 127.57809 ? 343 PHE   A O    1 
ATOM   2640 C  CB   . PHE   A 1 370 ? -18.48536 -59.91674 -46.54113 1.000 142.23175 ? 343 PHE   A CB   1 
ATOM   2641 C  CG   . PHE   A 1 370 ? -18.35440 -60.84161 -45.36274 1.000 131.93326 ? 343 PHE   A CG   1 
ATOM   2642 C  CD1  . PHE   A 1 370 ? -19.22450 -61.90970 -45.19781 1.000 138.39208 ? 343 PHE   A CD1  1 
ATOM   2643 C  CD2  . PHE   A 1 370 ? -17.39206 -60.61487 -44.39482 1.000 140.45317 ? 343 PHE   A CD2  1 
ATOM   2644 C  CE1  . PHE   A 1 370 ? -19.11363 -62.74938 -44.10973 1.000 140.45655 ? 343 PHE   A CE1  1 
ATOM   2645 C  CE2  . PHE   A 1 370 ? -17.28064 -61.45005 -43.30166 1.000 147.00259 ? 343 PHE   A CE2  1 
ATOM   2646 C  CZ   . PHE   A 1 370 ? -18.14092 -62.51757 -43.15987 1.000 135.94481 ? 343 PHE   A CZ   1 
ATOM   2647 N  N    . ASN   A 1 371 ? -16.83948 -62.61981 -47.79921 1.000 134.57481 ? 344 ASN   A N    1 
ATOM   2648 C  CA   . ASN   A 1 371 ? -16.89772 -64.06332 -47.96828 1.000 141.49324 ? 344 ASN   A CA   1 
ATOM   2649 C  C    . ASN   A 1 371 ? -16.36456 -64.70612 -46.70036 1.000 154.02929 ? 344 ASN   A C    1 
ATOM   2650 O  O    . ASN   A 1 371 ? -15.33900 -64.26986 -46.16849 1.000 158.40457 ? 344 ASN   A O    1 
ATOM   2651 C  CB   . ASN   A 1 371 ? -16.07758 -64.51668 -49.18072 1.000 131.41615 ? 344 ASN   A CB   1 
ATOM   2652 C  CG   . ASN   A 1 371 ? -16.36857 -63.69724 -50.42477 1.000 150.35117 ? 344 ASN   A CG   1 
ATOM   2653 O  OD1  . ASN   A 1 371 ? -17.15202 -64.10464 -51.28168 1.000 173.55533 ? 344 ASN   A OD1  1 
ATOM   2654 N  ND2  . ASN   A 1 371 ? -15.73488 -62.53439 -50.52931 1.000 154.17707 ? 344 ASN   A ND2  1 
ATOM   2655 N  N    . SER   A 1 372 ? -17.05690 -65.73154 -46.21249 1.000 153.65452 ? 345 SER   A N    1 
ATOM   2656 C  CA   . SER   A 1 372 ? -16.63224 -66.40057 -44.99334 1.000 143.67962 ? 345 SER   A CA   1 
ATOM   2657 C  C    . SER   A 1 372 ? -16.87860 -67.89693 -45.09920 1.000 144.83297 ? 345 SER   A C    1 
ATOM   2658 O  O    . SER   A 1 372 ? -17.76104 -68.35323 -45.83076 1.000 146.22119 ? 345 SER   A O    1 
ATOM   2659 C  CB   . SER   A 1 372 ? -17.34848 -65.84353 -43.75787 1.000 157.23367 ? 345 SER   A CB   1 
ATOM   2660 O  OG   . SER   A 1 372 ? -16.77143 -66.35063 -42.56717 1.000 148.73842 ? 345 SER   A OG   1 
ATOM   2661 N  N    . ILE   A 1 373 ? -16.07041 -68.65821 -44.35973 1.000 153.40501 ? 346 ILE   A N    1 
ATOM   2662 C  CA   . ILE   A 1 373 ? -16.22453 -70.10301 -44.26381 1.000 168.65241 ? 346 ILE   A CA   1 
ATOM   2663 C  C    . ILE   A 1 373 ? -16.33088 -70.58159 -42.82564 1.000 170.39948 ? 346 ILE   A C    1 
ATOM   2664 O  O    . ILE   A 1 373 ? -16.39736 -71.78986 -42.59139 1.000 166.38512 ? 346 ILE   A O    1 
ATOM   2665 C  CB   . ILE   A 1 373 ? -15.07666 -70.83956 -44.98448 1.000 152.50414 ? 346 ILE   A CB   1 
ATOM   2666 C  CG1  . ILE   A 1 373 ? -13.72598 -70.40620 -44.41323 1.000 157.94402 ? 346 ILE   A CG1  1 
ATOM   2667 C  CG2  . ILE   A 1 373 ? -15.13826 -70.58766 -46.48427 1.000 162.39118 ? 346 ILE   A CG2  1 
ATOM   2668 C  CD1  . ILE   A 1 373 ? -12.54195 -71.06911 -45.07761 1.000 205.93356 ? 346 ILE   A CD1  1 
ATOM   2669 N  N    . ASP   A 1 374 ? -16.34173 -69.67147 -41.85221 1.000 156.96310 ? 347 ASP   A N    1 
ATOM   2670 C  CA   . ASP   A 1 374 ? -16.50140 -70.05780 -40.45714 1.000 154.82655 ? 347 ASP   A CA   1 
ATOM   2671 C  C    . ASP   A 1 374 ? -17.85389 -70.72534 -40.24747 1.000 163.75720 ? 347 ASP   A C    1 
ATOM   2672 O  O    . ASP   A 1 374 ? -18.89760 -70.15790 -40.58240 1.000 177.21934 ? 347 ASP   A O    1 
ATOM   2673 C  CB   . ASP   A 1 374 ? -16.36459 -68.83201 -39.55425 1.000 166.72406 ? 347 ASP   A CB   1 
ATOM   2674 C  CG   . ASP   A 1 374 ? -16.58115 -69.15899 -38.09172 1.000 181.88484 ? 347 ASP   A CG   1 
ATOM   2675 O  OD1  . ASP   A 1 374 ? -15.73149 -69.86422 -37.50816 1.000 171.92484 ? 347 ASP   A OD1  1 
ATOM   2676 O  OD2  . ASP   A 1 374 ? -17.59928 -68.70814 -37.52625 1.000 177.54621 ? 347 ASP   A OD2  1 
ATOM   2677 N  N    . LYS   A 1 375 ? -17.82799 -71.93780 -39.68508 1.000 187.48235 ? 348 LYS   A N    1 
ATOM   2678 C  CA   . LYS   A 1 375 ? -19.04770 -72.73055 -39.56201 1.000 184.89449 ? 348 LYS   A CA   1 
ATOM   2679 C  C    . LYS   A 1 375 ? -20.10717 -72.02556 -38.72353 1.000 193.62644 ? 348 LYS   A C    1 
ATOM   2680 O  O    . LYS   A 1 375 ? -21.30196 -72.14930 -39.01042 1.000 198.53160 ? 348 LYS   A O    1 
ATOM   2681 C  CB   . LYS   A 1 375 ? -18.72354 -74.10405 -38.96968 1.000 200.04603 ? 348 LYS   A CB   1 
ATOM   2682 C  CG   . LYS   A 1 375 ? -18.09751 -75.07332 -39.95894 1.000 201.63084 ? 348 LYS   A CG   1 
ATOM   2683 C  CD   . LYS   A 1 375 ? -19.05828 -75.38882 -41.09570 1.000 179.71420 ? 348 LYS   A CD   1 
ATOM   2684 C  CE   . LYS   A 1 375 ? -18.49213 -76.44847 -42.02512 1.000 185.33902 ? 348 LYS   A CE   1 
ATOM   2685 N  NZ   . LYS   A 1 375 ? -19.47890 -76.85842 -43.06237 1.000 187.71869 ? 348 LYS   A NZ   1 
ATOM   2686 N  N    . GLN   A 1 376 ? -19.69804 -71.27804 -37.69592 1.000 185.79723 ? 349 GLN   A N    1 
ATOM   2687 C  CA   . GLN   A 1 376 ? -20.66830 -70.57161 -36.86259 1.000 172.56258 ? 349 GLN   A CA   1 
ATOM   2688 C  C    . GLN   A 1 376 ? -21.35315 -69.45106 -37.63887 1.000 175.80459 ? 349 GLN   A C    1 
ATOM   2689 O  O    . GLN   A 1 376 ? -22.58514 -69.31972 -37.61123 1.000 188.92005 ? 349 GLN   A O    1 
ATOM   2690 C  CB   . GLN   A 1 376 ? -19.97898 -70.02177 -35.61321 1.000 184.08360 ? 349 GLN   A CB   1 
ATOM   2691 C  CG   . GLN   A 1 376 ? -19.76373 -71.04961 -34.51761 1.000 201.80252 ? 349 GLN   A CG   1 
ATOM   2692 C  CD   . GLN   A 1 376 ? -21.03711 -71.35655 -33.75455 1.000 209.51616 ? 349 GLN   A CD   1 
ATOM   2693 O  OE1  . GLN   A 1 376 ? -21.98702 -70.57265 -33.76728 1.000 208.85147 ? 349 GLN   A OE1  1 
ATOM   2694 N  NE2  . GLN   A 1 376 ? -21.06313 -72.50191 -33.08391 1.000 218.01706 ? 349 GLN   A NE2  1 
ATOM   2695 N  N    . LEU   A 1 377 ? -20.56652 -68.62929 -38.33640 1.000 170.66126 ? 350 LEU   A N    1 
ATOM   2696 C  CA   . LEU   A 1 377 ? -21.13788 -67.52292 -39.09593 1.000 169.45182 ? 350 LEU   A CA   1 
ATOM   2697 C  C    . LEU   A 1 377 ? -21.99570 -68.03155 -40.24861 1.000 160.36017 ? 350 LEU   A C    1 
ATOM   2698 O  O    . LEU   A 1 377 ? -23.07798 -67.49170 -40.51186 1.000 161.66603 ? 350 LEU   A O    1 
ATOM   2699 C  CB   . LEU   A 1 377 ? -20.01843 -66.61679 -39.60621 1.000 171.75243 ? 350 LEU   A CB   1 
ATOM   2700 C  CG   . LEU   A 1 377 ? -20.38854 -65.18937 -40.00590 1.000 165.12692 ? 350 LEU   A CG   1 
ATOM   2701 C  CD1  . LEU   A 1 377 ? -21.11195 -64.48853 -38.86816 1.000 177.33928 ? 350 LEU   A CD1  1 
ATOM   2702 C  CD2  . LEU   A 1 377 ? -19.13788 -64.42224 -40.39411 1.000 163.80769 ? 350 LEU   A CD2  1 
ATOM   2703 N  N    . VAL   A 1 378 ? -21.53576 -69.07853 -40.93865 1.000 158.55097 ? 351 VAL   A N    1 
ATOM   2704 C  CA   . VAL   A 1 378 ? -22.33140 -69.66266 -42.01310 1.000 144.67736 ? 351 VAL   A CA   1 
ATOM   2705 C  C    . VAL   A 1 378 ? -23.60715 -70.28771 -41.46044 1.000 157.66828 ? 351 VAL   A C    1 
ATOM   2706 O  O    . VAL   A 1 378 ? -24.65517 -70.25049 -42.11352 1.000 166.94629 ? 351 VAL   A O    1 
ATOM   2707 C  CB   . VAL   A 1 378 ? -21.49242 -70.68261 -42.80748 1.000 157.09191 ? 351 VAL   A CB   1 
ATOM   2708 C  CG1  . VAL   A 1 378 ? -22.32696 -71.32954 -43.89985 1.000 156.01665 ? 351 VAL   A CG1  1 
ATOM   2709 C  CG2  . VAL   A 1 378 ? -20.27448 -70.00812 -43.41393 1.000 156.94150 ? 351 VAL   A CG2  1 
ATOM   2710 N  N    . SER   A 1 379 ? -23.55638 -70.84854 -40.24916 1.000 162.47546 ? 352 SER   A N    1 
ATOM   2711 C  CA   . SER   A 1 379 ? -24.76333 -71.40708 -39.64663 1.000 153.04430 ? 352 SER   A CA   1 
ATOM   2712 C  C    . SER   A 1 379 ? -25.76777 -70.31239 -39.30615 1.000 153.21073 ? 352 SER   A C    1 
ATOM   2713 O  O    . SER   A 1 379 ? -26.97584 -70.48303 -39.51077 1.000 141.33488 ? 352 SER   A O    1 
ATOM   2714 C  CB   . SER   A 1 379 ? -24.40311 -72.21465 -38.39958 1.000 156.38498 ? 352 SER   A CB   1 
ATOM   2715 O  OG   . SER   A 1 379 ? -23.80584 -71.39206 -37.41281 1.000 174.70013 ? 352 SER   A OG   1 
ATOM   2716 N  N    . GLU   A 1 380 ? -25.28874 -69.18109 -38.78428 1.000 158.17810 ? 353 GLU   A N    1 
ATOM   2717 C  CA   . GLU   A 1 380 ? -26.18795 -68.05758 -38.52971 1.000 144.81085 ? 353 GLU   A CA   1 
ATOM   2718 C  C    . GLU   A 1 380 ? -26.78844 -67.52852 -39.82953 1.000 146.88610 ? 353 GLU   A C    1 
ATOM   2719 O  O    . GLU   A 1 380 ? -27.97685 -67.18042 -39.88308 1.000 162.35110 ? 353 GLU   A O    1 
ATOM   2720 C  CB   . GLU   A 1 380 ? -25.44685 -66.94770 -37.78357 1.000 126.76356 ? 353 GLU   A CB   1 
ATOM   2721 C  CG   . GLU   A 1 380 ? -25.06412 -67.29581 -36.34993 1.000 167.71545 ? 353 GLU   A CG   1 
ATOM   2722 C  CD   . GLU   A 1 380 ? -26.24921 -67.27820 -35.39842 1.000 187.48617 ? 353 GLU   A CD   1 
ATOM   2723 O  OE1  . GLU   A 1 380 ? -27.34890 -66.85308 -35.81228 1.000 172.97530 ? 353 GLU   A OE1  1 
ATOM   2724 O  OE2  . GLU   A 1 380 ? -26.07910 -67.68770 -34.23081 1.000 195.08074 ? 353 GLU   A OE2  1 
ATOM   2725 N  N    . ALA   A 1 381 ? -25.98295 -67.47018 -40.89323 1.000 141.31848 ? 354 ALA   A N    1 
ATOM   2726 C  CA   . ALA   A 1 381 ? -26.50413 -67.04634 -42.18996 1.000 125.69627 ? 354 ALA   A CA   1 
ATOM   2727 C  C    . ALA   A 1 381 ? -27.55403 -68.02250 -42.71037 1.000 141.17762 ? 354 ALA   A C    1 
ATOM   2728 O  O    . ALA   A 1 381 ? -28.55635 -67.61122 -43.30867 1.000 143.47608 ? 354 ALA   A O    1 
ATOM   2729 C  CB   . ALA   A 1 381 ? -25.36019 -66.90153 -43.19243 1.000 122.60814 ? 354 ALA   A CB   1 
ATOM   2730 N  N    . LYS   A 1 382 ? -27.33522 -69.32257 -42.49963 1.000 148.46181 ? 355 LYS   A N    1 
ATOM   2731 C  CA   . LYS   A 1 382 ? -28.32617 -70.31853 -42.89299 1.000 141.92906 ? 355 LYS   A CA   1 
ATOM   2732 C  C    . LYS   A 1 382 ? -29.61108 -70.14941 -42.09534 1.000 153.32879 ? 355 LYS   A C    1 
ATOM   2733 O  O    . LYS   A 1 382 ? -30.71069 -70.31517 -42.63298 1.000 154.51214 ? 355 LYS   A O    1 
ATOM   2734 C  CB   . LYS   A 1 382 ? -27.75806 -71.72594 -42.70609 1.000 147.89440 ? 355 LYS   A CB   1 
ATOM   2735 C  CG   . LYS   A 1 382 ? -28.65960 -72.84740 -43.20770 1.000 146.73622 ? 355 LYS   A CG   1 
ATOM   2736 C  CD   . LYS   A 1 382 ? -28.57697 -72.99722 -44.71996 1.000 147.75092 ? 355 LYS   A CD   1 
ATOM   2737 C  CE   . LYS   A 1 382 ? -29.34205 -74.22349 -45.19801 1.000 164.64468 ? 355 LYS   A CE   1 
ATOM   2738 N  NZ   . LYS   A 1 382 ? -29.07065 -74.52931 -46.63067 1.000 169.52597 ? 355 LYS   A NZ   1 
ATOM   2739 N  N    . LYS   A 1 383 ? -29.48859 -69.82124 -40.80770 1.000 160.46401 ? 356 LYS   A N    1 
ATOM   2740 C  CA   . LYS   A 1 383 ? -30.66533 -69.51879 -39.99777 1.000 156.43673 ? 356 LYS   A CA   1 
ATOM   2741 C  C    . LYS   A 1 383 ? -31.44018 -68.34285 -40.58065 1.000 147.45814 ? 356 LYS   A C    1 
ATOM   2742 O  O    . LYS   A 1 383 ? -32.67360 -68.38116 -40.68318 1.000 138.00482 ? 356 LYS   A O    1 
ATOM   2743 C  CB   . LYS   A 1 383 ? -30.24395 -69.22556 -38.55718 1.000 167.13326 ? 356 LYS   A CB   1 
ATOM   2744 C  CG   . LYS   A 1 383 ? -31.35155 -68.66008 -37.68416 1.000 172.21572 ? 356 LYS   A CG   1 
ATOM   2745 C  CD   . LYS   A 1 383 ? -30.84337 -68.34237 -36.28745 1.000 175.94202 ? 356 LYS   A CD   1 
ATOM   2746 C  CE   . LYS   A 1 383 ? -31.95785 -67.80671 -35.40517 1.000 176.99430 ? 356 LYS   A CE   1 
ATOM   2747 N  NZ   . LYS   A 1 383 ? -31.49462 -67.56562 -34.01137 1.000 148.64001 ? 356 LYS   A NZ   1 
ATOM   2748 N  N    . ILE   A 1 384 ? -30.72479 -67.28518 -40.97099 1.000 148.59004 ? 357 ILE   A N    1 
ATOM   2749 C  CA   . ILE   A 1 384 ? -31.38460 -66.11341 -41.54613 1.000 138.23580 ? 357 ILE   A CA   1 
ATOM   2750 C  C    . ILE   A 1 384 ? -32.08854 -66.47786 -42.84957 1.000 136.69441 ? 357 ILE   A C    1 
ATOM   2751 O  O    . ILE   A 1 384 ? -33.23285 -66.06728 -43.09347 1.000 143.15011 ? 357 ILE   A O    1 
ATOM   2752 C  CB   . ILE   A 1 384 ? -30.37148 -64.97129 -41.74893 1.000 127.62946 ? 357 ILE   A CB   1 
ATOM   2753 C  CG1  . ILE   A 1 384 ? -29.76399 -64.55527 -40.40912 1.000 153.38871 ? 357 ILE   A CG1  1 
ATOM   2754 C  CG2  . ILE   A 1 384 ? -31.03714 -63.77715 -42.41706 1.000 123.62177 ? 357 ILE   A CG2  1 
ATOM   2755 C  CD1  . ILE   A 1 384 ? -30.78645 -64.08444 -39.39927 1.000 165.42150 ? 357 ILE   A CD1  1 
ATOM   2756 N  N    . PHE   A 1 385 ? -31.42157 -67.25661 -43.70645 1.000 131.20484 ? 358 PHE   A N    1 
ATOM   2757 C  CA   . PHE   A 1 385 ? -32.03645 -67.62974 -44.97759 1.000 138.99209 ? 358 PHE   A CA   1 
ATOM   2758 C  C    . PHE   A 1 385 ? -33.24864 -68.52824 -44.76606 1.000 136.45753 ? 358 PHE   A C    1 
ATOM   2759 O  O    . PHE   A 1 385 ? -34.23153 -68.43371 -45.50898 1.000 134.80519 ? 358 PHE   A O    1 
ATOM   2760 C  CB   . PHE   A 1 385 ? -31.02541 -68.31794 -45.89481 1.000 138.02852 ? 358 PHE   A CB   1 
ATOM   2761 C  CG   . PHE   A 1 385 ? -31.60523 -68.72461 -47.22415 1.000 134.47032 ? 358 PHE   A CG   1 
ATOM   2762 C  CD1  . PHE   A 1 385 ? -31.64740 -67.82778 -48.27951 1.000 134.02994 ? 358 PHE   A CD1  1 
ATOM   2763 C  CD2  . PHE   A 1 385 ? -32.12711 -69.99585 -47.41191 1.000 130.90873 ? 358 PHE   A CD2  1 
ATOM   2764 C  CE1  . PHE   A 1 385 ? -32.18928 -68.19360 -49.49937 1.000 125.81891 ? 358 PHE   A CE1  1 
ATOM   2765 C  CE2  . PHE   A 1 385 ? -32.67407 -70.36568 -48.62744 1.000 131.46153 ? 358 PHE   A CE2  1 
ATOM   2766 C  CZ   . PHE   A 1 385 ? -32.70195 -69.46432 -49.67323 1.000 119.86312 ? 358 PHE   A CZ   1 
ATOM   2767 N  N    . GLU   A 1 386 ? -33.19612 -69.41617 -43.77084 1.000 142.54846 ? 359 GLU   A N    1 
ATOM   2768 C  CA   . GLU   A 1 386 ? -34.34991 -70.26312 -43.48889 1.000 129.19539 ? 359 GLU   A CA   1 
ATOM   2769 C  C    . GLU   A 1 386 ? -35.51441 -69.43899 -42.95981 1.000 139.64686 ? 359 GLU   A C    1 
ATOM   2770 O  O    . GLU   A 1 386 ? -36.67354 -69.70228 -43.30105 1.000 134.47624 ? 359 GLU   A O    1 
ATOM   2771 C  CB   . GLU   A 1 386 ? -33.97485 -71.36267 -42.49457 1.000 155.71597 ? 359 GLU   A CB   1 
ATOM   2772 C  CG   . GLU   A 1 386 ? -33.04220 -72.42959 -43.05005 1.000 132.46030 ? 359 GLU   A CG   1 
ATOM   2773 C  CD   . GLU   A 1 386 ? -33.71850 -73.34646 -44.05259 1.000 136.50442 ? 359 GLU   A CD   1 
ATOM   2774 O  OE1  . GLU   A 1 386 ? -34.96352 -73.31645 -44.15303 1.000 136.35480 ? 359 GLU   A OE1  1 
ATOM   2775 O  OE2  . GLU   A 1 386 ? -33.00085 -74.10252 -44.74029 1.000 159.02907 ? 359 GLU   A OE2  1 
ATOM   2776 N  N    . ARG   A 1 387 ? -35.22581 -68.43757 -42.12439 1.000 147.10700 ? 360 ARG   A N    1 
ATOM   2777 C  CA   . ARG   A 1 387 ? -36.28017 -67.54104 -41.66225 1.000 141.37737 ? 360 ARG   A CA   1 
ATOM   2778 C  C    . ARG   A 1 387 ? -36.90935 -66.78908 -42.82778 1.000 144.49516 ? 360 ARG   A C    1 
ATOM   2779 O  O    . ARG   A 1 387 ? -38.13282 -66.61476 -42.87795 1.000 159.47758 ? 360 ARG   A O    1 
ATOM   2780 C  CB   . ARG   A 1 387 ? -35.72348 -66.55776 -40.63441 1.000 153.31333 ? 360 ARG   A CB   1 
ATOM   2781 C  CG   . ARG   A 1 387 ? -36.73920 -65.54140 -40.14267 1.000 147.75232 ? 360 ARG   A CG   1 
ATOM   2782 C  CD   . ARG   A 1 387 ? -36.04970 -64.29997 -39.61416 1.000 139.72835 ? 360 ARG   A CD   1 
ATOM   2783 N  NE   . ARG   A 1 387 ? -35.26492 -63.64052 -40.65070 1.000 121.84207 ? 360 ARG   A NE   1 
ATOM   2784 C  CZ   . ARG   A 1 387 ? -34.53827 -62.54903 -40.45688 1.000 145.89895 ? 360 ARG   A CZ   1 
ATOM   2785 N  NH1  . ARG   A 1 387 ? -34.46913 -61.96740 -39.27095 1.000 170.23267 ? 360 ARG   A NH1  1 
ATOM   2786 N  NH2  . ARG   A 1 387 ? -33.86407 -62.02820 -41.47819 1.000 131.61006 ? 360 ARG   A NH2  1 
ATOM   2787 N  N    . ASP   A 1 388 ? -36.08718 -66.33988 -43.77917 1.000 132.07271 ? 361 ASP   A N    1 
ATOM   2788 C  CA   . ASP   A 1 388 ? -36.62168 -65.59753 -44.91772 1.000 140.58138 ? 361 ASP   A CA   1 
ATOM   2789 C  C    . ASP   A 1 388 ? -37.38977 -66.49703 -45.87913 1.000 131.81868 ? 361 ASP   A C    1 
ATOM   2790 O  O    . ASP   A 1 388 ? -38.34149 -66.04070 -46.52369 1.000 130.45247 ? 361 ASP   A O    1 
ATOM   2791 C  CB   . ASP   A 1 388 ? -35.49347 -64.88446 -45.66161 1.000 147.34161 ? 361 ASP   A CB   1 
ATOM   2792 C  CG   . ASP   A 1 388 ? -34.85437 -63.78881 -44.83605 1.000 144.39897 ? 361 ASP   A CG   1 
ATOM   2793 O  OD1  . ASP   A 1 388 ? -35.19725 -63.66837 -43.64147 1.000 159.13871 ? 361 ASP   A OD1  1 
ATOM   2794 O  OD2  . ASP   A 1 388 ? -34.01311 -63.04445 -45.38148 1.000 116.20330 ? 361 ASP   A OD2  1 
ATOM   2795 N  N    . TRP   A 1 389 ? -36.99541 -67.76805 -45.99058 1.000 137.86210 ? 362 TRP   A N    1 
ATOM   2796 C  CA   . TRP   A 1 389 ? -37.59645 -68.64957 -46.98769 1.000 146.81201 ? 362 TRP   A CA   1 
ATOM   2797 C  C    . TRP   A 1 389 ? -39.04084 -68.98906 -46.64303 1.000 142.12389 ? 362 TRP   A C    1 
ATOM   2798 O  O    . TRP   A 1 389 ? -39.88560 -69.10235 -47.53812 1.000 151.91014 ? 362 TRP   A O    1 
ATOM   2799 C  CB   . TRP   A 1 389 ? -36.76767 -69.92619 -47.12615 1.000 157.50814 ? 362 TRP   A CB   1 
ATOM   2800 C  CG   . TRP   A 1 389 ? -37.32582 -70.91389 -48.10691 1.000 148.44078 ? 362 TRP   A CG   1 
ATOM   2801 C  CD1  . TRP   A 1 389 ? -38.01472 -72.05683 -47.82013 1.000 156.67760 ? 362 TRP   A CD1  1 
ATOM   2802 C  CD2  . TRP   A 1 389 ? -37.23392 -70.84843 -49.53424 1.000 142.04039 ? 362 TRP   A CD2  1 
ATOM   2803 N  NE1  . TRP   A 1 389 ? -38.35702 -72.70719 -48.98184 1.000 173.30545 ? 362 TRP   A NE1  1 
ATOM   2804 C  CE2  . TRP   A 1 389 ? -37.88944 -71.98485 -50.04833 1.000 159.58785 ? 362 TRP   A CE2  1 
ATOM   2805 C  CE3  . TRP   A 1 389 ? -36.66131 -69.93827 -50.42754 1.000 137.66324 ? 362 TRP   A CE3  1 
ATOM   2806 C  CZ2  . TRP   A 1 389 ? -37.98803 -72.23428 -51.41596 1.000 148.74715 ? 362 TRP   A CZ2  1 
ATOM   2807 C  CZ3  . TRP   A 1 389 ? -36.75976 -70.18764 -51.78418 1.000 144.61033 ? 362 TRP   A CZ3  1 
ATOM   2808 C  CH2  . TRP   A 1 389 ? -37.41766 -71.32606 -52.26543 1.000 144.23671 ? 362 TRP   A CH2  1 
ATOM   2809 N  N    . VAL   A 1 390 ? -39.34612 -69.15289 -45.35827 1.000 124.63585 ? 363 VAL   A N    1 
ATOM   2810 C  CA   . VAL   A 1 390 ? -40.67724 -69.56987 -44.93421 1.000 138.71269 ? 363 VAL   A CA   1 
ATOM   2811 C  C    . VAL   A 1 390 ? -41.47186 -68.35088 -44.49361 1.000 154.93802 ? 363 VAL   A C    1 
ATOM   2812 O  O    . VAL   A 1 390 ? -42.56407 -68.47995 -43.92994 1.000 185.89028 ? 363 VAL   A O    1 
ATOM   2813 C  CB   . VAL   A 1 390 ? -40.59507 -70.61326 -43.80720 1.000 161.46816 ? 363 VAL   A CB   1 
ATOM   2814 C  CG1  . VAL   A 1 390 ? -39.84606 -71.84124 -44.29324 1.000 173.45277 ? 363 VAL   A CG1  1 
ATOM   2815 C  CG2  . VAL   A 1 390 ? -39.91885 -70.00689 -42.58319 1.000 162.81194 ? 363 VAL   A CG2  1 
ATOM   2816 N  N    . SER   A 1 391 ? -40.92826 -67.16310 -44.74215 1.000 138.97846 ? 364 SER   A N    1 
ATOM   2817 C  CA   . SER   A 1 391 ? -41.61250 -65.93929 -44.35963 1.000 138.01210 ? 364 SER   A CA   1 
ATOM   2818 C  C    . SER   A 1 391 ? -42.89491 -65.75624 -45.16883 1.000 148.48515 ? 364 SER   A C    1 
ATOM   2819 O  O    . SER   A 1 391 ? -43.07360 -66.32898 -46.24731 1.000 155.66038 ? 364 SER   A O    1 
ATOM   2820 C  CB   . SER   A 1 391 ? -40.69676 -64.73189 -44.55044 1.000 142.83443 ? 364 SER   A CB   1 
ATOM   2821 O  OG   . SER   A 1 391 ? -41.37601 -63.52836 -44.25639 1.000 144.41106 ? 364 SER   A OG   1 
ATOM   2822 N  N    . SER   A 1 392 ? -43.80411 -64.94682 -44.62002 1.000 145.73388 ? 365 SER   A N    1 
ATOM   2823 C  CA   . SER   A 1 392 ? -45.05782 -64.67247 -45.31149 1.000 164.29916 ? 365 SER   A CA   1 
ATOM   2824 C  C    . SER   A 1 392 ? -44.82901 -63.85202 -46.57301 1.000 155.26597 ? 365 SER   A C    1 
ATOM   2825 O  O    . SER   A 1 392 ? -45.58194 -63.98742 -47.54388 1.000 172.74306 ? 365 SER   A O    1 
ATOM   2826 C  CB   . SER   A 1 392 ? -46.02555 -63.95493 -44.37282 1.000 171.22863 ? 365 SER   A CB   1 
ATOM   2827 O  OG   . SER   A 1 392 ? -45.50401 -62.69934 -43.97750 1.000 149.26243 ? 365 SER   A OG   1 
ATOM   2828 N  N    . HIS   A 1 393 ? -43.79479 -63.00822 -46.58375 1.000 134.46392 ? 366 HIS   A N    1 
ATOM   2829 C  CA   . HIS   A 1 393 ? -43.46440 -62.23650 -47.77467 1.000 143.83297 ? 366 HIS   A CA   1 
ATOM   2830 C  C    . HIS   A 1 393 ? -42.88739 -63.09750 -48.88820 1.000 156.74415 ? 366 HIS   A C    1 
ATOM   2831 O  O    . HIS   A 1 393 ? -42.70978 -62.59778 -50.00425 1.000 169.90544 ? 366 HIS   A O    1 
ATOM   2832 C  CB   . HIS   A 1 393 ? -42.47441 -61.12400 -47.42629 1.000 148.64027 ? 366 HIS   A CB   1 
ATOM   2833 C  CG   . HIS   A 1 393 ? -42.90831 -60.26593 -46.27998 1.000 158.64882 ? 366 HIS   A CG   1 
ATOM   2834 N  ND1  . HIS   A 1 393 ? -43.94449 -59.36236 -46.37630 1.000 165.49823 ? 366 HIS   A ND1  1 
ATOM   2835 C  CD2  . HIS   A 1 393 ? -42.44312 -60.17152 -45.01197 1.000 153.66206 ? 366 HIS   A CD2  1 
ATOM   2836 C  CE1  . HIS   A 1 393 ? -44.10099 -58.75060 -45.21587 1.000 167.47582 ? 366 HIS   A CE1  1 
ATOM   2837 N  NE2  . HIS   A 1 393 ? -43.20237 -59.22319 -44.37097 1.000 140.05828 ? 366 HIS   A NE2  1 
ATOM   2838 N  N    . SER   A 1 394 ? -42.59373 -64.36683 -48.61512 1.000 150.54498 ? 367 SER   A N    1 
ATOM   2839 C  CA   . SER   A 1 394 ? -42.02815 -65.28277 -49.60346 1.000 142.91681 ? 367 SER   A CA   1 
ATOM   2840 C  C    . SER   A 1 394 ? -43.14502 -66.19724 -50.09447 1.000 163.08461 ? 367 SER   A C    1 
ATOM   2841 O  O    . SER   A 1 394 ? -43.35604 -67.29023 -49.56801 1.000 167.53458 ? 367 SER   A O    1 
ATOM   2842 C  CB   . SER   A 1 394 ? -40.87333 -66.07912 -49.00749 1.000 141.15346 ? 367 SER   A CB   1 
ATOM   2843 O  OG   . SER   A 1 394 ? -39.84972 -65.21857 -48.54286 1.000 134.43757 ? 367 SER   A OG   1 
ATOM   2844 N  N    . LYS   A 1 395 ? -43.86953 -65.74021 -51.11070 1.000 159.68529 ? 368 LYS   A N    1 
ATOM   2845 C  CA   . LYS   A 1 395 ? -44.87387 -66.57700 -51.74615 1.000 163.24280 ? 368 LYS   A CA   1 
ATOM   2846 C  C    . LYS   A 1 395 ? -44.22607 -67.47864 -52.78892 1.000 166.65662 ? 368 LYS   A C    1 
ATOM   2847 O  O    . LYS   A 1 395 ? -43.25696 -67.10125 -53.45351 1.000 154.58239 ? 368 LYS   A O    1 
ATOM   2848 C  CB   . LYS   A 1 395 ? -45.96574 -65.72453 -52.39490 1.000 161.48526 ? 368 LYS   A CB   1 
ATOM   2849 C  CG   . LYS   A 1 395 ? -46.93372 -65.09183 -51.40716 1.000 187.10703 ? 368 LYS   A CG   1 
ATOM   2850 C  CD   . LYS   A 1 395 ? -48.15704 -64.53315 -52.11866 1.000 220.45173 ? 368 LYS   A CD   1 
ATOM   2851 C  CE   . LYS   A 1 395 ? -49.19936 -64.04745 -51.12337 1.000 194.03865 ? 368 LYS   A CE   1 
ATOM   2852 N  NZ   . LYS   A 1 395 ? -50.44417 -63.58820 -51.80012 1.000 163.57562 ? 368 LYS   A NZ   1 
ATOM   2853 N  N    . SER   A 1 396 ? -44.77088 -68.68507 -52.92042 1.000 169.44736 ? 369 SER   A N    1 
ATOM   2854 C  CA   . SER   A 1 396 ? -44.23258 -69.64986 -53.86759 1.000 149.97218 ? 369 SER   A CA   1 
ATOM   2855 C  C    . SER   A 1 396 ? -44.38193 -69.14205 -55.29796 1.000 154.19518 ? 369 SER   A C    1 
ATOM   2856 O  O    . SER   A 1 396 ? -45.31425 -68.40302 -55.62733 1.000 145.09207 ? 369 SER   A O    1 
ATOM   2857 C  CB   . SER   A 1 396 ? -44.93774 -70.99686 -53.70747 1.000 170.51599 ? 369 SER   A CB   1 
ATOM   2858 O  OG   . SER   A 1 396 ? -46.34639 -70.83623 -53.71170 1.000 201.20908 ? 369 SER   A OG   1 
ATOM   2859 N  N    . LEU   A 1 397 ? -43.44312 -69.54579 -56.15133 1.000 161.80798 ? 370 LEU   A N    1 
ATOM   2860 C  CA   . LEU   A 1 397 ? -43.46800 -69.13251 -57.54786 1.000 159.76231 ? 370 LEU   A CA   1 
ATOM   2861 C  C    . LEU   A 1 397 ? -44.66587 -69.74540 -58.26137 1.000 162.70161 ? 370 LEU   A C    1 
ATOM   2862 O  O    . LEU   A 1 397 ? -44.89534 -70.95654 -58.18762 1.000 180.34072 ? 370 LEU   A O    1 
ATOM   2863 C  CB   . LEU   A 1 397 ? -42.17377 -69.54178 -58.24827 1.000 159.28613 ? 370 LEU   A CB   1 
ATOM   2864 C  CG   . LEU   A 1 397 ? -42.16735 -69.33973 -59.76461 1.000 149.05007 ? 370 LEU   A CG   1 
ATOM   2865 C  CD1  . LEU   A 1 397 ? -42.24830 -67.86100 -60.10432 1.000 134.20248 ? 370 LEU   A CD1  1 
ATOM   2866 C  CD2  . LEU   A 1 397 ? -40.94058 -69.97902 -60.39650 1.000 134.50399 ? 370 LEU   A CD2  1 
ATOM   2867 N  N    . LYS   A 1 398 ? -45.43025 -68.90345 -58.95296 1.000 147.92467 ? 371 LYS   A N    1 
ATOM   2868 C  CA   . LYS   A 1 398 ? -46.59679 -69.34006 -59.70483 1.000 166.64711 ? 371 LYS   A CA   1 
ATOM   2869 C  C    . LYS   A 1 398 ? -46.58955 -68.66719 -61.06759 1.000 169.72033 ? 371 LYS   A C    1 
ATOM   2870 O  O    . LYS   A 1 398 ? -46.33388 -67.46439 -61.17205 1.000 170.09927 ? 371 LYS   A O    1 
ATOM   2871 C  CB   . LYS   A 1 398 ? -47.89987 -69.01315 -58.96423 1.000 182.59016 ? 371 LYS   A CB   1 
ATOM   2872 C  CG   . LYS   A 1 398 ? -48.02186 -69.68428 -57.60808 1.000 184.94921 ? 371 LYS   A CG   1 
ATOM   2873 C  CD   . LYS   A 1 398 ? -49.31116 -69.29792 -56.90807 1.000 186.82174 ? 371 LYS   A CD   1 
ATOM   2874 C  CE   . LYS   A 1 398 ? -49.40343 -69.95531 -55.54164 1.000 203.62998 ? 371 LYS   A CE   1 
ATOM   2875 N  NZ   . LYS   A 1 398 ? -50.66113 -69.59599 -54.83248 1.000 221.08603 ? 371 LYS   A NZ   1 
ATOM   2876 N  N    . ILE   A 1 399 ? -46.86019 -69.44985 -62.10763 1.000 184.35454 ? 372 ILE   A N    1 
ATOM   2877 C  CA   . ILE   A 1 399 ? -46.88701 -68.93617 -63.47214 1.000 191.51874 ? 372 ILE   A CA   1 
ATOM   2878 C  C    . ILE   A 1 399 ? -48.12950 -69.44032 -64.19694 1.000 216.76117 ? 372 ILE   A C    1 
ATOM   2879 O  O    . ILE   A 1 399 ? -48.47471 -70.61869 -64.11028 1.000 233.48388 ? 372 ILE   A O    1 
ATOM   2880 C  CB   . ILE   A 1 399 ? -45.61296 -69.32936 -64.24139 1.000 167.29164 ? 372 ILE   A CB   1 
ATOM   2881 C  CG1  . ILE   A 1 399 ? -44.37453 -68.72813 -63.57655 1.000 162.70033 ? 372 ILE   A CG1  1 
ATOM   2882 C  CG2  . ILE   A 1 399 ? -45.70464 -68.88405 -65.69242 1.000 147.91631 ? 372 ILE   A CG2  1 
ATOM   2883 C  CD1  . ILE   A 1 399 ? -43.08364 -69.19695 -64.18445 1.000 165.68326 ? 372 ILE   A CD1  1 
ATOM   2884 O  OXT  . ILE   A 1 399 ? -48.81530 -68.68840 -64.89038 1.000 222.76624 ? 372 ILE   A OXT  1 
HETATM 2885 C  C1   . CIT   B 2 .   ? -33.36675 -44.16749 -50.70218 1.000 200.17987 ? 401 CIT   A C1   1 
HETATM 2886 O  O1   . CIT   B 2 .   ? -33.35653 -44.63812 -49.54254 1.000 172.35214 ? 401 CIT   A O1   1 
HETATM 2887 O  O2   . CIT   B 2 .   ? -33.11737 -42.98249 -51.00784 1.000 187.58810 ? 401 CIT   A O2   1 
HETATM 2888 C  C2   . CIT   B 2 .   ? -33.71641 -45.12413 -51.85888 1.000 220.11730 ? 401 CIT   A C2   1 
HETATM 2889 C  C3   . CIT   B 2 .   ? -32.51380 -45.87868 -52.45390 1.000 237.15832 ? 401 CIT   A C3   1 
HETATM 2890 O  O7   . CIT   B 2 .   ? -31.34600 -45.34553 -51.86794 1.000 244.43386 ? 401 CIT   A O7   1 
HETATM 2891 C  C4   . CIT   B 2 .   ? -32.58633 -47.39413 -52.19692 1.000 226.34163 ? 401 CIT   A C4   1 
HETATM 2892 C  C5   . CIT   B 2 .   ? -31.84314 -47.86488 -50.93909 1.000 203.69154 ? 401 CIT   A C5   1 
HETATM 2893 O  O3   . CIT   B 2 .   ? -30.93839 -48.70561 -51.06980 1.000 189.54581 ? 401 CIT   A O3   1 
HETATM 2894 O  O4   . CIT   B 2 .   ? -32.21342 -47.36085 -49.84121 1.000 200.34956 ? 401 CIT   A O4   1 
HETATM 2895 C  C6   . CIT   B 2 .   ? -32.55631 -45.65129 -53.99737 1.000 234.67460 ? 401 CIT   A C6   1 
HETATM 2896 O  O5   . CIT   B 2 .   ? -33.08830 -44.58285 -54.37374 1.000 228.27206 ? 401 CIT   A O5   1 
HETATM 2897 O  O6   . CIT   B 2 .   ? -32.06933 -46.52912 -54.73401 1.000 234.61887 ? 401 CIT   A O6   1 
HETATM 2898 C  C1   . GOL   C 3 .   ? -28.40092 -50.09592 -57.56362 1.000 171.10941 ? 402 GOL   A C1   1 
HETATM 2899 O  O1   . GOL   C 3 .   ? -27.89555 -48.81733 -57.26005 1.000 167.29438 ? 402 GOL   A O1   1 
HETATM 2900 C  C2   . GOL   C 3 .   ? -28.49174 -50.25637 -59.06662 1.000 173.85394 ? 402 GOL   A C2   1 
HETATM 2901 O  O2   . GOL   C 3 .   ? -27.20079 -50.11031 -59.61416 1.000 160.68372 ? 402 GOL   A O2   1 
HETATM 2902 C  C3   . GOL   C 3 .   ? -29.45566 -49.23631 -59.65039 1.000 182.15540 ? 402 GOL   A C3   1 
HETATM 2903 O  O3   . GOL   C 3 .   ? -28.91840 -47.95325 -59.41445 1.000 171.06889 ? 402 GOL   A O3   1 
HETATM 2904 C  C01  . A1IDM D 4 .   ? -31.85317 -76.56277 -68.80004 0.514 160.02740 ? 403 A1IDM A C01  1 
HETATM 2905 C  C02  . A1IDM D 4 .   ? -32.50694 -75.49125 -69.66507 0.514 158.53446 ? 403 A1IDM A C02  1 
HETATM 2906 C  C03  . A1IDM D 4 .   ? -33.49902 -75.84158 -70.56645 0.514 160.24728 ? 403 A1IDM A C03  1 
HETATM 2907 C  C04  . A1IDM D 4 .   ? -34.09450 -74.86998 -71.35304 0.514 154.76413 ? 403 A1IDM A C04  1 
HETATM 2908 C  C05  . A1IDM D 4 .   ? -33.69723 -73.54748 -71.23662 0.514 152.69458 ? 403 A1IDM A C05  1 
HETATM 2909 C  C06  . A1IDM D 4 .   ? -32.70065 -73.19861 -70.33848 0.514 155.96311 ? 403 A1IDM A C06  1 
HETATM 2910 C  C07  . A1IDM D 4 .   ? -32.10819 -74.16862 -69.54839 0.514 158.13983 ? 403 A1IDM A C07  1 
HETATM 2911 C  C08  . A1IDM D 4 .   ? -32.27122 -71.73768 -70.20887 0.514 150.05165 ? 403 A1IDM A C08  1 
HETATM 2912 C  C12  . A1IDM D 4 .   ? -33.26199 -68.43406 -71.37523 0.514 156.24122 ? 403 A1IDM A C12  1 
HETATM 2913 C  C14  . A1IDM D 4 .   ? -32.95259 -66.94384 -71.27993 0.514 157.80851 ? 403 A1IDM A C14  1 
HETATM 2914 C  C15  . A1IDM D 4 .   ? -31.98239 -66.36883 -72.08815 0.514 158.49876 ? 403 A1IDM A C15  1 
HETATM 2915 C  C16  . A1IDM D 4 .   ? -31.75154 -65.00932 -71.95977 0.514 159.77996 ? 403 A1IDM A C16  1 
HETATM 2916 C  C18  . A1IDM D 4 .   ? -33.35519 -64.80130 -70.32530 0.514 163.32538 ? 403 A1IDM A C18  1 
HETATM 2917 C  C19  . A1IDM D 4 .   ? -33.65556 -66.15132 -70.38300 0.514 157.60333 ? 403 A1IDM A C19  1 
HETATM 2918 N  N10  . A1IDM D 4 .   ? -33.26913 -70.69971 -70.38922 0.514 150.55473 ? 403 A1IDM A N10  1 
HETATM 2919 N  N11  . A1IDM D 4 .   ? -32.95471 -69.32821 -70.27429 0.514 150.99082 ? 403 A1IDM A N11  1 
HETATM 2920 N  N17  . A1IDM D 4 .   ? -32.42715 -64.27281 -71.09883 0.514 163.00710 ? 403 A1IDM A N17  1 
HETATM 2921 O  O09  . A1IDM D 4 .   ? -31.14658 -71.46024 -69.96297 0.514 136.44681 ? 403 A1IDM A O09  1 
HETATM 2922 O  O13  . A1IDM D 4 .   ? -33.75381 -68.86160 -72.36092 0.514 153.53831 ? 403 A1IDM A O13  1 
HETATM 2923 CL CL20 . A1IDM D 4 .   ? -34.00781 -77.54489 -70.71242 0.514 178.01220 ? 403 A1IDM A CL20 1 
HETATM 2924 C  C1   . GOL   E 3 .   ? -36.08795 -64.25522 -62.66570 1.000 146.27607 ? 404 GOL   A C1   1 
HETATM 2925 O  O1   . GOL   E 3 .   ? -36.19941 -63.11628 -61.84299 1.000 144.89921 ? 404 GOL   A O1   1 
HETATM 2926 C  C2   . GOL   E 3 .   ? -36.95861 -65.36386 -62.11266 1.000 126.21801 ? 404 GOL   A C2   1 
HETATM 2927 O  O2   . GOL   E 3 .   ? -36.62836 -65.56190 -60.75654 1.000 160.17775 ? 404 GOL   A O2   1 
HETATM 2928 C  C3   . GOL   E 3 .   ? -38.42150 -64.97951 -62.25469 1.000 147.24742 ? 404 GOL   A C3   1 
HETATM 2929 O  O3   . GOL   E 3 .   ? -38.54132 -63.62823 -61.86700 1.000 164.44148 ? 404 GOL   A O3   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 33  ? 1.55682 2.63586 1.97750 0.42686  -0.44552 0.20631  6   SER A N   
2    C CA  . SER A 33  ? 1.91081 2.89323 2.28820 0.43608  -0.40480 0.20288  6   SER A CA  
3    C C   . SER A 33  ? 2.04668 2.97511 2.40003 0.39021  -0.39817 0.17039  6   SER A C   
4    O O   . SER A 33  ? 2.10030 3.04405 2.44719 0.35617  -0.42509 0.15168  6   SER A O   
5    C CB  . SER A 33  ? 2.00581 2.92939 2.31917 0.46746  -0.39710 0.21865  6   SER A CB  
6    O OG  . SER A 33  ? 2.17060 3.08514 2.44234 0.44679  -0.42559 0.20713  6   SER A OG  
7    N N   . VAL A 34  ? 2.05038 2.91554 2.38950 0.38985  -0.36159 0.16427  7   VAL A N   
8    C CA  . VAL A 34  ? 1.92488 2.73889 2.24252 0.34973  -0.35207 0.13636  7   VAL A CA  
9    C C   . VAL A 34  ? 2.02904 2.75660 2.27216 0.34921  -0.34056 0.13031  7   VAL A C   
10   O O   . VAL A 34  ? 2.25184 2.94157 2.46183 0.38265  -0.32407 0.14793  7   VAL A O   
11   C CB  . VAL A 34  ? 1.80546 2.60608 2.15168 0.34526  -0.32064 0.13201  7   VAL A CB  
12   C CG1 . VAL A 34  ? 1.60218 2.48952 2.02297 0.33816  -0.33355 0.13429  7   VAL A CG1 
13   C CG2 . VAL A 34  ? 1.84698 2.60170 2.17353 0.38402  -0.28497 0.15071  7   VAL A CG2 
14   N N   . PRO A 35  ? 1.93387 2.62803 2.14905 0.31287  -0.34751 0.10664  8   PRO A N   
15   C CA  . PRO A 35  ? 2.13452 2.75063 2.28117 0.31061  -0.33675 0.10064  8   PRO A CA  
16   C C   . PRO A 35  ? 2.08236 2.62835 2.20386 0.31040  -0.29800 0.09620  8   PRO A C   
17   O O   . PRO A 35  ? 2.08707 2.63886 2.23950 0.29952  -0.28219 0.08986  8   PRO A O   
18   C CB  . PRO A 35  ? 2.11631 2.73398 2.25189 0.27086  -0.35959 0.07703  8   PRO A CB  
19   C CG  . PRO A 35  ? 1.85520 2.52060 2.04729 0.24649  -0.36494 0.06552  8   PRO A CG  
20   C CD  . PRO A 35  ? 1.78109 2.51057 2.02648 0.27266  -0.36696 0.08522  8   PRO A CD  
21   N N   . ALA A 36  ? 2.21837 2.69691 2.28058 0.32134  -0.28260 0.09943  9   ALA A N   
22   C CA  . ALA A 36  ? 2.14976 2.55686 2.17937 0.31784  -0.24650 0.09372  9   ALA A CA  
23   C C   . ALA A 36  ? 2.07093 2.45478 2.09044 0.27600  -0.24659 0.06850  9   ALA A C   
24   O O   . ALA A 36  ? 2.19009 2.57122 2.18983 0.25623  -0.26639 0.05703  9   ALA A O   
25   C CB  . ALA A 36  ? 2.44470 2.78696 2.41308 0.34009  -0.23008 0.10457  9   ALA A CB  
26   N N   . GLY A 37  ? 2.14268 2.50982 2.17494 0.26340  -0.22369 0.06064  10  GLY A N   
27   C CA  . GLY A 37  ? 2.16345 2.51464 2.19170 0.22591  -0.22293 0.03938  10  GLY A CA  
28   C C   . GLY A 37  ? 2.05956 2.47055 2.13717 0.20297  -0.24685 0.02912  10  GLY A C   
29   O O   . GLY A 37  ? 2.17721 2.57728 2.25510 0.17316  -0.24558 0.01291  10  GLY A O   
30   N N   . ALA A 38  ? 1.83162 2.30573 1.95053 0.21554  -0.26823 0.03852  11  ALA A N   
31   C CA  . ALA A 38  ? 1.85691 2.39052 2.02490 0.19315  -0.29051 0.02909  11  ALA A CA  
32   C C   . ALA A 38  ? 1.92689 2.45156 2.07492 0.16315  -0.31027 0.01119  11  ALA A C   
33   O O   . ALA A 38  ? 1.87927 2.41657 2.04908 0.13514  -0.31462 -0.00308 11  ALA A O   
34   C CB  . ALA A 38  ? 1.69732 2.24085 1.90175 0.18066  -0.27252 0.02415  11  ALA A CB  
35   N N   . LYS A 39  ? 1.94343 2.44418 2.04849 0.17002  -0.32079 0.01262  12  LYS A N   
36   C CA  . LYS A 39  ? 2.02971 2.51995 2.11127 0.14521  -0.33886 -0.00316 12  LYS A CA  
37   C C   . LYS A 39  ? 1.95744 2.40699 2.02493 0.11802  -0.32356 -0.01947 12  LYS A C   
38   O O   . LYS A 39  ? 1.66944 2.12430 1.73933 0.09262  -0.33638 -0.03422 12  LYS A O   
39   C CB  . LYS A 39  ? 1.89462 2.44746 2.01361 0.13118  -0.36931 -0.00894 12  LYS A CB  
40   C CG  . LYS A 39  ? 1.80513 2.40495 1.93549 0.15515  -0.39002 0.00676  12  LYS A CG  
41   C CD  . LYS A 39  ? 2.11481 2.68644 2.19178 0.16454  -0.40108 0.00945  12  LYS A CD  
42   C CE  . LYS A 39  ? 1.99274 2.56284 2.05304 0.13414  -0.42125 -0.01012 12  LYS A CE  
43   N NZ  . LYS A 39  ? 1.83303 2.47123 1.93489 0.11991  -0.44936 -0.01501 12  LYS A NZ  
44   N N   . CYS A 40  ? 2.06062 2.46940 2.11239 0.12314  -0.29561 -0.01662 13  CYS A N   
45   C CA  . CYS A 40  ? 1.92047 2.29578 1.96089 0.09869  -0.28054 -0.02971 13  CYS A CA  
46   C C   . CYS A 40  ? 1.99733 2.31917 1.98263 0.09377  -0.27427 -0.03483 13  CYS A C   
47   O O   . CYS A 40  ? 2.08110 2.37374 2.03157 0.11332  -0.26683 -0.02560 13  CYS A O   
48   C CB  . CYS A 40  ? 1.80856 2.17076 1.86051 0.10303  -0.25380 -0.02521 13  CYS A CB  
49   S SG  . CYS A 40  ? 1.76797 2.19082 1.88708 0.10328  -0.25660 -0.02137 13  CYS A SG  
50   N N   . ARG A 41  ? 1.81912 2.12829 1.79722 0.06806  -0.27612 -0.04879 14  ARG A N   
51   C CA  . ARG A 41  ? 1.86620 2.12870 1.79670 0.06041  -0.26890 -0.05445 14  ARG A CA  
52   C C   . ARG A 41  ? 1.87802 2.12359 1.80964 0.03686  -0.25524 -0.06432 14  ARG A C   
53   O O   . ARG A 41  ? 1.92244 2.19488 1.88974 0.02247  -0.25918 -0.06976 14  ARG A O   
54   C CB  . ARG A 41  ? 2.04826 2.31536 1.96177 0.05572  -0.29059 -0.06043 14  ARG A CB  
55   C CG  . ARG A 41  ? 1.72997 2.02719 1.67254 0.03383  -0.30711 -0.07281 14  ARG A CG  
56   C CD  . ARG A 41  ? 2.03345 2.32947 1.95250 0.02977  -0.32625 -0.07933 14  ARG A CD  
57   N NE  . ARG A 41  ? 2.21011 2.45914 2.08050 0.02917  -0.31575 -0.08139 14  ARG A NE  
58   C CZ  . ARG A 41  ? 2.26072 2.49730 2.09889 0.02931  -0.32704 -0.08516 14  ARG A CZ  
59   N NH1 . ARG A 41  ? 2.43539 2.70198 2.28154 0.02929  -0.35034 -0.08790 14  ARG A NH1 
60   N NH2 . ARG A 41  ? 2.29019 2.48392 2.08617 0.02820  -0.31436 -0.08648 14  ARG A NH2 
61   N N   . LEU A 42  ? 1.90818 2.10995 1.80012 0.03276  -0.23895 -0.06582 15  LEU A N   
62   C CA  . LEU A 42  ? 1.74033 1.92744 1.63031 0.01161  -0.22532 -0.07309 15  LEU A CA  
63   C C   . LEU A 42  ? 1.72519 1.92110 1.62027 -0.00716 -0.23791 -0.08336 15  LEU A C   
64   O O   . LEU A 42  ? 1.95731 2.14752 1.83372 -0.00562 -0.24999 -0.08651 15  LEU A O   
65   C CB  . LEU A 42  ? 1.88799 2.02847 1.73378 0.01125  -0.20427 -0.07166 15  LEU A CB  
66   C CG  . LEU A 42  ? 1.84101 1.96225 1.67588 0.02802  -0.18589 -0.06253 15  LEU A CG  
67   C CD1 . LEU A 42  ? 2.03411 2.10699 1.82438 0.02048  -0.16344 -0.06415 15  LEU A CD1 
68   C CD2 . LEU A 42  ? 1.56498 1.71251 1.43877 0.02718  -0.18025 -0.06066 15  LEU A CD2 
69   N N   . VAL A 43  ? 1.40062 1.60892 1.31974 -0.02412 -0.23379 -0.08800 16  VAL A N   
70   C CA  . VAL A 43  ? 1.67662 1.89073 1.60285 -0.04140 -0.24123 -0.09646 16  VAL A CA  
71   C C   . VAL A 43  ? 1.80763 2.00815 1.72812 -0.05605 -0.22469 -0.09730 16  VAL A C   
72   O O   . VAL A 43  ? 1.89501 2.09737 1.82456 -0.05723 -0.21229 -0.09326 16  VAL A O   
73   C CB  . VAL A 43  ? 1.57692 1.82764 1.54562 -0.04709 -0.25565 -0.09991 16  VAL A CB  
74   C CG1 . VAL A 43  ? 1.67686 1.92778 1.65225 -0.06466 -0.25863 -0.10790 16  VAL A CG1 
75   C CG2 . VAL A 43  ? 1.71009 1.97908 1.68340 -0.03519 -0.27432 -0.09956 16  VAL A CG2 
76   N N   . GLU A 44  ? 1.64942 1.83730 1.55382 -0.06695 -0.22393 -0.10203 17  GLU A N   
77   C CA  . GLU A 44  ? 1.80190 1.98281 1.70201 -0.08088 -0.20974 -0.10139 17  GLU A CA  
78   C C   . GLU A 44  ? 1.80371 1.98524 1.70359 -0.09179 -0.21315 -0.10586 17  GLU A C   
79   O O   . GLU A 44  ? 1.58613 1.76146 1.47536 -0.08845 -0.22255 -0.11042 17  GLU A O   
80   C CB  . GLU A 44  ? 1.82607 1.97845 1.68999 -0.07986 -0.19415 -0.09856 17  GLU A CB  
81   C CG  . GLU A 44  ? 1.96195 2.08834 1.78910 -0.07345 -0.19496 -0.10001 17  GLU A CG  
82   C CD  . GLU A 44  ? 2.17460 2.27039 1.96606 -0.07524 -0.17711 -0.09766 17  GLU A CD  
83   O OE1 . GLU A 44  ? 1.96808 2.06389 1.76227 -0.08496 -0.16453 -0.09638 17  GLU A OE1 
84   O OE2 . GLU A 44  ? 2.35987 2.43008 2.11852 -0.06804 -0.17497 -0.09735 17  GLU A OE2 
85   N N   . THR A 45  ? 1.95305 2.14243 1.86420 -0.10424 -0.20466 -0.10381 18  THR A N   
86   C CA  . THR A 45  ? 1.60693 1.79862 1.52051 -0.11331 -0.20432 -0.10531 18  THR A CA  
87   C C   . THR A 45  ? 1.70528 1.88435 1.59267 -0.12068 -0.19182 -0.10274 18  THR A C   
88   O O   . THR A 45  ? 1.67660 1.86037 1.56400 -0.12856 -0.18198 -0.09843 18  THR A O   
89   C CB  . THR A 45  ? 1.59143 1.80510 1.53945 -0.12111 -0.20431 -0.10267 18  THR A CB  
90   O OG1 . THR A 45  ? 1.61419 1.84097 1.58758 -0.11668 -0.21432 -0.10517 18  THR A OG1 
91   C CG2 . THR A 45  ? 1.71789 1.93213 1.66964 -0.12635 -0.20406 -0.10340 18  THR A CG2 
92   N N   . LEU A 46  ? 1.90046 2.06445 1.76495 -0.11946 -0.19198 -0.10577 19  LEU A N   
93   C CA  . LEU A 46  ? 1.72369 1.87730 1.56336 -0.12759 -0.18046 -0.10399 19  LEU A CA  
94   C C   . LEU A 46  ? 1.68812 1.84945 1.53464 -0.13175 -0.18030 -0.10405 19  LEU A C   
95   O O   . LEU A 46  ? 1.78876 1.93778 1.62406 -0.12552 -0.18498 -0.10887 19  LEU A O   
96   C CB  . LEU A 46  ? 1.66807 1.79333 1.47057 -0.12121 -0.17747 -0.10651 19  LEU A CB  
97   C CG  . LEU A 46  ? 1.69742 1.81155 1.49317 -0.10968 -0.17991 -0.10607 19  LEU A CG  
98   C CD1 . LEU A 46  ? 1.90536 1.98926 1.66269 -0.10105 -0.17720 -0.10707 19  LEU A CD1 
99   C CD2 . LEU A 46  ? 1.60738 1.72462 1.40757 -0.11576 -0.16944 -0.10241 19  LEU A CD2 
100  N N   . PRO A 47  ? 1.64232 1.82383 1.50626 -0.14119 -0.17452 -0.09820 20  PRO A N   
101  C CA  . PRO A 47  ? 1.80515 1.99562 1.67920 -0.14223 -0.17280 -0.09619 20  PRO A CA  
102  C C   . PRO A 47  ? 1.86511 2.04208 1.71186 -0.14327 -0.16633 -0.09799 20  PRO A C   
103  O O   . PRO A 47  ? 1.89254 2.05603 1.71264 -0.14712 -0.16104 -0.09924 20  PRO A O   
104  C CB  . PRO A 47  ? 1.75037 1.96798 1.64589 -0.15161 -0.16710 -0.08666 20  PRO A CB  
105  C CG  . PRO A 47  ? 1.47786 1.70010 1.38165 -0.15393 -0.16911 -0.08586 20  PRO A CG  
106  C CD  . PRO A 47  ? 1.60256 1.80110 1.47979 -0.14990 -0.16967 -0.09232 20  PRO A CD  
107  N N   . GLU A 48  ? 1.64287 1.82155 1.49586 -0.13979 -0.16499 -0.09807 21  GLU A N   
108  C CA  . GLU A 48  ? 1.86496 2.03213 1.69434 -0.14011 -0.15759 -0.09961 21  GLU A CA  
109  C C   . GLU A 48  ? 1.91073 2.09596 1.73742 -0.15222 -0.14680 -0.09213 21  GLU A C   
110  O O   . GLU A 48  ? 2.16295 2.33635 1.96342 -0.15672 -0.13979 -0.09399 21  GLU A O   
111  C CB  . GLU A 48  ? 2.11850 2.28258 1.95618 -0.13276 -0.15659 -0.10144 21  GLU A CB  
112  C CG  . GLU A 48  ? 2.20666 2.35002 2.03953 -0.12392 -0.16702 -0.11130 21  GLU A CG  
113  C CD  . GLU A 48  ? 2.02566 2.18037 1.88876 -0.12301 -0.17474 -0.11101 21  GLU A CD  
114  O OE1 . GLU A 48  ? 1.56852 1.74551 1.45600 -0.12756 -0.17106 -0.10225 21  GLU A OE1 
115  O OE2 . GLU A 48  ? 1.95441 2.09672 1.81618 -0.11873 -0.18454 -0.11940 21  GLU A OE2 
116  N N   . ASN A 49  ? 1.74089 1.95562 1.59336 -0.15866 -0.14535 -0.08344 22  ASN A N   
117  C CA  . ASN A 49  ? 1.86322 2.10187 1.71499 -0.17237 -0.13698 -0.07584 22  ASN A CA  
118  C C   . ASN A 49  ? 1.98992 2.21953 1.81813 -0.18484 -0.13425 -0.07891 22  ASN A C   
119  O O   . ASN A 49  ? 2.14229 2.38919 1.96429 -0.19993 -0.12719 -0.07475 22  ASN A O   
120  C CB  . ASN A 49  ? 1.73063 2.00517 1.61594 -0.17462 -0.13742 -0.06430 22  ASN A CB  
121  C CG  . ASN A 49  ? 2.06395 2.33978 1.96417 -0.17325 -0.14462 -0.06405 22  ASN A CG  
122  O OD1 . ASN A 49  ? 2.01121 2.27813 1.92647 -0.16238 -0.15024 -0.06636 22  ASN A OD1 
123  N ND2 . ASN A 49  ? 2.36795 2.65427 2.26300 -0.18562 -0.14348 -0.06180 22  ASN A ND2 
124  N N   . MET A 50  ? 1.84548 2.04908 1.66027 -0.17926 -0.13884 -0.08584 23  MET A N   
125  C CA  . MET A 50  ? 1.71179 1.89998 1.50223 -0.18844 -0.13381 -0.08890 23  MET A CA  
126  C C   . MET A 50  ? 1.87293 2.02429 1.62821 -0.18317 -0.13033 -0.09587 23  MET A C   
127  O O   . MET A 50  ? 2.06214 2.19888 1.81405 -0.16957 -0.13599 -0.09933 23  MET A O   
128  C CB  . MET A 50  ? 1.79796 1.98548 1.60079 -0.18436 -0.13922 -0.08925 23  MET A CB  
129  C CG  . MET A 50  ? 1.72212 1.94321 1.55791 -0.18876 -0.14230 -0.08169 23  MET A CG  
130  S SD  . MET A 50  ? 1.74708 1.96718 1.59554 -0.18589 -0.14580 -0.08209 23  MET A SD  
131  C CE  . MET A 50  ? 1.14848 1.40782 1.03306 -0.19112 -0.14829 -0.07141 23  MET A CE  
132  N N   . ASP A 51  ? 1.70636 1.84100 1.43296 -0.19473 -0.12027 -0.09789 24  ASP A N   
133  C CA  . ASP A 51  ? 1.95531 2.05250 1.64447 -0.19131 -0.11380 -0.10281 24  ASP A CA  
134  C C   . ASP A 51  ? 2.25005 2.31802 1.92635 -0.17611 -0.11763 -0.10565 24  ASP A C   
135  O O   . ASP A 51  ? 2.28001 2.31383 1.92230 -0.17242 -0.11074 -0.10803 24  ASP A O   
136  C CB  . ASP A 51  ? 1.82995 1.91907 1.49178 -0.21220 -0.09884 -0.10378 24  ASP A CB  
137  C CG  . ASP A 51  ? 2.02195 2.10959 1.67888 -0.22407 -0.09337 -0.10433 24  ASP A CG  
138  O OD1 . ASP A 51  ? 2.06512 2.11972 1.70144 -0.21653 -0.08942 -0.10738 24  ASP A OD1 
139  O OD2 . ASP A 51  ? 2.25185 2.37151 1.92463 -0.24038 -0.09245 -0.10115 24  ASP A OD2 
140  N N   . PHE A 52  ? 1.96778 2.04923 1.67087 -0.16675 -0.12770 -0.10443 25  PHE A N   
141  C CA  . PHE A 52  ? 1.70030 1.76150 1.39694 -0.15121 -0.13194 -0.10558 25  PHE A CA  
142  C C   . PHE A 52  ? 2.03129 2.08111 1.72252 -0.13429 -0.14255 -0.10761 25  PHE A C   
143  O O   . PHE A 52  ? 2.17425 2.24244 1.88779 -0.13061 -0.15294 -0.10864 25  PHE A O   
144  C CB  . PHE A 52  ? 1.69999 1.78346 1.42953 -0.14843 -0.13858 -0.10346 25  PHE A CB  
145  C CG  . PHE A 52  ? 1.82208 1.91691 1.55471 -0.16519 -0.12875 -0.10153 25  PHE A CG  
146  C CD1 . PHE A 52  ? 1.98477 2.05588 1.69292 -0.16911 -0.11646 -0.10276 25  PHE A CD1 
147  C CD2 . PHE A 52  ? 1.90354 2.03163 1.66167 -0.17673 -0.13112 -0.09809 25  PHE A CD2 
148  C CE1 . PHE A 52  ? 1.68483 1.76501 1.39190 -0.18663 -0.10719 -0.10231 25  PHE A CE1 
149  C CE2 . PHE A 52  ? 1.90049 2.04139 1.65917 -0.19305 -0.12338 -0.09591 25  PHE A CE2 
150  C CZ  . PHE A 52  ? 1.59367 1.71053 1.32586 -0.19918 -0.11167 -0.09888 25  PHE A CZ  
151  N N   . ARG A 53  ? 1.92837 1.94630 1.58776 -0.12425 -0.13920 -0.10799 26  ARG A N   
152  C CA  . ARG A 53  ? 2.11584 2.12162 1.76400 -0.10813 -0.14965 -0.10924 26  ARG A CA  
153  C C   . ARG A 53  ? 2.16359 2.15409 1.80291 -0.09097 -0.15326 -0.10612 26  ARG A C   
154  O O   . ARG A 53  ? 2.14441 2.11435 1.76558 -0.09102 -0.14057 -0.10333 26  ARG A O   
155  C CB  . ARG A 53  ? 2.43118 2.41234 2.04341 -0.11125 -0.14118 -0.11067 26  ARG A CB  
156  C CG  . ARG A 53  ? 2.41728 2.41561 2.03879 -0.12615 -0.13639 -0.11249 26  ARG A CG  
157  C CD  . ARG A 53  ? 2.41979 2.44168 2.07026 -0.12089 -0.14976 -0.11478 26  ARG A CD  
158  N NE  . ARG A 53  ? 2.60272 2.63807 2.26000 -0.13103 -0.14329 -0.11505 26  ARG A NE  
159  C CZ  . ARG A 53  ? 2.35780 2.42225 2.04331 -0.14202 -0.14008 -0.11184 26  ARG A CZ  
160  N NH1 . ARG A 53  ? 2.15925 2.24084 1.86691 -0.14603 -0.14261 -0.10903 26  ARG A NH1 
161  N NH2 . ARG A 53  ? 2.41790 2.49558 2.10943 -0.14829 -0.13365 -0.11046 26  ARG A NH2 
162  N N   . SER A 54  ? 2.20809 2.20910 1.85997 -0.07650 -0.16995 -0.10642 27  SER A N   
163  C CA  . SER A 54  ? 2.29958 2.29355 1.94723 -0.05786 -0.17571 -0.10166 27  SER A CA  
164  C C   . SER A 54  ? 2.21015 2.21437 1.86111 -0.04573 -0.19508 -0.10323 27  SER A C   
165  O O   . SER A 54  ? 2.22732 2.24798 1.89323 -0.05287 -0.20443 -0.10927 27  SER A O   
166  C CB  . SER A 54  ? 2.12389 2.13844 1.80395 -0.05637 -0.17601 -0.09899 27  SER A CB  
167  O OG  . SER A 54  ? 2.05581 2.10540 1.77553 -0.05891 -0.19107 -0.10210 27  SER A OG  
168  N N   . ASP A 55  ? 2.09194 2.08582 1.72744 -0.02724 -0.20042 -0.09739 28  ASP A N   
169  C CA  . ASP A 55  ? 2.27910 2.28635 1.91637 -0.01544 -0.22071 -0.09794 28  ASP A CA  
170  C C   . ASP A 55  ? 2.22315 2.26782 1.90257 -0.00985 -0.23604 -0.09704 28  ASP A C   
171  O O   . ASP A 55  ? 2.49600 2.55785 2.18064 -0.00193 -0.25468 -0.09780 28  ASP A O   
172  C CB  . ASP A 55  ? 2.55364 2.53372 2.15099 0.00286  -0.21995 -0.09008 28  ASP A CB  
173  C CG  . ASP A 55  ? 2.87142 2.81221 2.42490 -0.00316 -0.20353 -0.09074 28  ASP A CG  
174  O OD1 . ASP A 55  ? 2.98145 2.92240 2.53478 -0.01971 -0.19966 -0.09861 28  ASP A OD1 
175  O OD2 . ASP A 55  ? 3.13098 3.04060 2.65047 0.00908  -0.19339 -0.08272 28  ASP A OD2 
176  N N   . HIS A 56  ? 1.94668 2.00534 1.65525 -0.01504 -0.22854 -0.09563 29  HIS A N   
177  C CA  . HIS A 56  ? 2.00379 2.09809 1.75349 -0.01016 -0.24056 -0.09408 29  HIS A CA  
178  C C   . HIS A 56  ? 2.02359 2.14496 1.80234 -0.02374 -0.25448 -0.10324 29  HIS A C   
179  O O   . HIS A 56  ? 2.06610 2.17784 1.83415 -0.03563 -0.25326 -0.11023 29  HIS A O   
180  C CB  . HIS A 56  ? 1.94369 2.04117 1.71225 -0.01209 -0.22578 -0.08990 29  HIS A CB  
181  C CG  . HIS A 56  ? 1.97008 2.03935 1.71202 0.00227  -0.21055 -0.08118 29  HIS A CG  
182  N ND1 . HIS A 56  ? 1.67278 1.71471 1.39590 -0.00637 -0.18863 -0.08097 29  HIS A ND1 
183  C CD2 . HIS A 56  ? 2.29431 2.35730 2.02412 0.02476  -0.21313 -0.07195 29  HIS A CD2 
184  C CE1 . HIS A 56  ? 1.80812 1.82333 1.50682 0.00958  -0.17667 -0.07307 29  HIS A CE1 
185  N NE2 . HIS A 56  ? 2.56273 2.59029 2.26577 0.03024  -0.19093 -0.06645 29  HIS A NE2 
186  N N   . LEU A 57  ? 1.92604 2.08088 1.74231 -0.02176 -0.26621 -0.10288 30  LEU A N   
187  C CA  . LEU A 57  ? 1.68413 1.86272 1.52879 -0.03527 -0.27814 -0.11164 30  LEU A CA  
188  C C   . LEU A 57  ? 1.85248 2.03082 1.71468 -0.05119 -0.26526 -0.11444 30  LEU A C   
189  O O   . LEU A 57  ? 1.94045 2.11514 1.80748 -0.05191 -0.25116 -0.10912 30  LEU A O   
190  C CB  . LEU A 57  ? 1.65544 1.87148 1.53622 -0.03029 -0.29326 -0.11007 30  LEU A CB  
191  C CG  . LEU A 57  ? 1.70746 1.94745 1.61472 -0.04447 -0.30780 -0.12001 30  LEU A CG  
192  C CD1 . LEU A 57  ? 2.09338 2.32173 1.97200 -0.04698 -0.32012 -0.12801 30  LEU A CD1 
193  C CD2 . LEU A 57  ? 1.30933 1.58966 1.25563 -0.04113 -0.32021 -0.11732 30  LEU A CD2 
194  N N   . THR A 58  ? 1.75112 1.93241 1.62094 -0.06376 -0.26954 -0.12249 31  THR A N   
195  C CA  . THR A 58  ? 1.73076 1.91561 1.61990 -0.07730 -0.25910 -0.12357 31  THR A CA  
196  C C   . THR A 58  ? 1.62845 1.84169 1.55932 -0.08351 -0.26628 -0.12535 31  THR A C   
197  O O   . THR A 58  ? 1.71193 1.94141 1.65523 -0.08164 -0.28125 -0.12931 31  THR A O   
198  C CB  . THR A 58  ? 1.76980 1.93838 1.64274 -0.08559 -0.25573 -0.12951 31  THR A CB  
199  O OG1 . THR A 58  ? 1.49001 1.66456 1.37000 -0.08908 -0.26904 -0.13818 31  THR A OG1 
200  C CG2 . THR A 58  ? 1.75336 1.89496 1.58436 -0.07981 -0.24981 -0.12852 31  THR A CG2 
201  N N   . THR A 59  ? 1.60488 1.82521 1.55671 -0.09195 -0.25541 -0.12204 32  THR A N   
202  C CA  . THR A 59  ? 1.44885 1.69369 1.43972 -0.09878 -0.25928 -0.12274 32  THR A CA  
203  C C   . THR A 59  ? 1.39405 1.64097 1.39402 -0.10750 -0.26885 -0.13185 32  THR A C   
204  O O   . THR A 59  ? 1.68518 1.95203 1.71114 -0.11181 -0.27853 -0.13553 32  THR A O   
205  C CB  . THR A 59  ? 1.58933 1.83777 1.59496 -0.10633 -0.24473 -0.11661 32  THR A CB  
206  O OG1 . THR A 59  ? 1.80636 2.04759 1.79679 -0.10052 -0.23438 -0.11008 32  THR A OG1 
207  C CG2 . THR A 59  ? 1.51283 1.78538 1.55749 -0.11225 -0.24684 -0.11583 32  THR A CG2 
208  N N   . PHE A 60  ? 1.41998 1.64573 1.39812 -0.11089 -0.26508 -0.13597 33  PHE A N   
209  C CA  . PHE A 60  ? 1.69745 1.91779 1.67799 -0.11894 -0.27134 -0.14573 33  PHE A CA  
210  C C   . PHE A 60  ? 1.71527 1.94216 1.68839 -0.11688 -0.28926 -0.15369 33  PHE A C   
211  O O   . PHE A 60  ? 1.76534 2.00654 1.75929 -0.12558 -0.29875 -0.16045 33  PHE A O   
212  C CB  . PHE A 60  ? 1.72510 1.92001 1.68018 -0.11984 -0.26163 -0.14749 33  PHE A CB  
213  C CG  . PHE A 60  ? 1.80240 1.98478 1.75551 -0.12738 -0.26385 -0.15773 33  PHE A CG  
214  C CD1 . PHE A 60  ? 1.83509 2.02044 1.81443 -0.13629 -0.25804 -0.15842 33  PHE A CD1 
215  C CD2 . PHE A 60  ? 1.82174 1.98589 1.74379 -0.12565 -0.26997 -0.16660 33  PHE A CD2 
216  C CE1 . PHE A 60  ? 1.92355 2.09158 1.89817 -0.14347 -0.25732 -0.16845 33  PHE A CE1 
217  C CE2 . PHE A 60  ? 1.85689 2.00524 1.77335 -0.13352 -0.27000 -0.17735 33  PHE A CE2 
218  C CZ  . PHE A 60  ? 1.90662 2.05563 1.84932 -0.14250 -0.26308 -0.17859 33  PHE A CZ  
219  N N   . GLU A 61  ? 1.77180 1.98903 1.71429 -0.10621 -0.29407 -0.15259 34  GLU A N   
220  C CA  . GLU A 61  ? 1.82629 2.05356 1.75958 -0.10228 -0.31240 -0.15762 34  GLU A CA  
221  C C   . GLU A 61  ? 1.67979 1.94215 1.64676 -0.10006 -0.32246 -0.15364 34  GLU A C   
222  O O   . GLU A 61  ? 1.55850 1.84064 1.53505 -0.10457 -0.33902 -0.15992 34  GLU A O   
223  C CB  . GLU A 61  ? 1.99933 2.20915 1.89327 -0.08861 -0.31325 -0.15358 34  GLU A CB  
224  C CG  . GLU A 61  ? 2.22349 2.40061 2.08256 -0.09065 -0.30401 -0.15790 34  GLU A CG  
225  C CD  . GLU A 61  ? 2.34127 2.49931 2.16264 -0.07771 -0.30076 -0.15192 34  GLU A CD  
226  O OE1 . GLU A 61  ? 1.99369 2.15805 1.81755 -0.06728 -0.29864 -0.14235 34  GLU A OE1 
227  O OE2 . GLU A 61  ? 2.41665 2.55107 2.20465 -0.07787 -0.29875 -0.15672 34  GLU A OE2 
228  N N   . CYS A 62  ? 1.79913 2.07089 1.78412 -0.09401 -0.31229 -0.14348 35  CYS A N   
229  C CA  . CYS A 62  ? 1.67992 1.98559 1.69871 -0.09033 -0.31894 -0.13855 35  CYS A CA  
230  C C   . CYS A 62  ? 1.61448 1.94140 1.66899 -0.10673 -0.32431 -0.14560 35  CYS A C   
231  O O   . CYS A 62  ? 1.71804 2.07452 1.79296 -0.10922 -0.33935 -0.14845 35  CYS A O   
232  C CB  . CYS A 62  ? 1.63642 1.94156 1.66341 -0.08201 -0.30311 -0.12740 35  CYS A CB  
233  S SG  . CYS A 62  ? 1.66064 2.00631 1.73344 -0.07796 -0.30557 -0.12071 35  CYS A SG  
234  N N   . PHE A 63  ? 1.62577 1.93889 1.68842 -0.11834 -0.31173 -0.14778 36  PHE A N   
235  C CA  . PHE A 63  ? 1.53286 1.85958 1.62646 -0.13454 -0.31385 -0.15418 36  PHE A CA  
236  C C   . PHE A 63  ? 1.53084 1.85386 1.61369 -0.14536 -0.32789 -0.16783 36  PHE A C   
237  O O   . PHE A 63  ? 1.51165 1.85680 1.61923 -0.15766 -0.33763 -0.17439 36  PHE A O   
238  C CB  . PHE A 63  ? 1.68768 1.99681 1.78800 -0.14207 -0.29608 -0.15147 36  PHE A CB  
239  C CG  . PHE A 63  ? 1.51783 1.83530 1.63259 -0.13628 -0.28315 -0.13941 36  PHE A CG  
240  C CD1 . PHE A 63  ? 1.44672 1.78724 1.57543 -0.12713 -0.28619 -0.13318 36  PHE A CD1 
241  C CD2 . PHE A 63  ? 1.51781 1.82067 1.63138 -0.13974 -0.26745 -0.13388 36  PHE A CD2 
242  C CE1 . PHE A 63  ? 1.39457 1.73905 1.53275 -0.12282 -0.27259 -0.12339 36  PHE A CE1 
243  C CE2 . PHE A 63  ? 1.47160 1.78205 1.59477 -0.13651 -0.25602 -0.12368 36  PHE A CE2 
244  C CZ  . PHE A 63  ? 1.40648 1.73563 1.54054 -0.12871 -0.25799 -0.11930 36  PHE A CZ  
245  N N   . ASN A 64  ? 1.66053 1.95557 1.70527 -0.14236 -0.32851 -0.17288 37  ASN A N   
246  C CA  . ASN A 64  ? 1.65200 1.94056 1.67994 -0.15272 -0.34152 -0.18680 37  ASN A CA  
247  C C   . ASN A 64  ? 1.70352 2.02586 1.73785 -0.15091 -0.36332 -0.18848 37  ASN A C   
248  O O   . ASN A 64  ? 1.84920 2.18629 1.89359 -0.16638 -0.37602 -0.19950 37  ASN A O   
249  C CB  . ASN A 64  ? 1.92449 2.17715 1.90794 -0.14740 -0.33680 -0.19048 37  ASN A CB  
250  C CG  . ASN A 64  ? 2.30493 2.52690 2.28343 -0.15511 -0.31936 -0.19419 37  ASN A CG  
251  O OD1 . ASN A 64  ? 1.92706 2.13812 1.90734 -0.16932 -0.31944 -0.20558 37  ASN A OD1 
252  N ND2 . ASN A 64  ? 2.44281 2.65073 2.41440 -0.14587 -0.30368 -0.18432 37  ASN A ND2 
253  N N   . GLU A 65  ? 1.69847 2.03402 1.72700 -0.13234 -0.36744 -0.17720 38  GLU A N   
254  C CA  . GLU A 65  ? 1.63340 2.00511 1.66961 -0.12677 -0.38803 -0.17540 38  GLU A CA  
255  C C   . GLU A 65  ? 1.76016 2.17429 1.84610 -0.13457 -0.39318 -0.17360 38  GLU A C   
256  O O   . GLU A 65  ? 1.86352 2.31138 1.96369 -0.14245 -0.41213 -0.17874 38  GLU A O   
257  C CB  . GLU A 65  ? 1.60820 1.97889 1.62531 -0.10227 -0.38744 -0.16165 38  GLU A CB  
258  C CG  . GLU A 65  ? 1.45012 1.86014 1.47540 -0.09127 -0.40775 -0.15568 38  GLU A CG  
259  C CD  . GLU A 65  ? 1.97986 2.38657 1.96985 -0.09333 -0.42627 -0.16329 38  GLU A CD  
260  O OE1 . GLU A 65  ? 1.99552 2.37333 1.96096 -0.10825 -0.42470 -0.17676 38  GLU A OE1 
261  O OE2 . GLU A 65  ? 2.25564 2.68842 2.24125 -0.07909 -0.44176 -0.15507 38  GLU A OE2 
262  N N   . ILE A 66  ? 1.80627 2.22115 1.91877 -0.13355 -0.37655 -0.16628 39  ILE A N   
263  C CA  . ILE A 66  ? 1.55915 2.01267 1.71934 -0.14148 -0.37861 -0.16425 39  ILE A CA  
264  C C   . ILE A 66  ? 1.53885 1.99659 1.71345 -0.16763 -0.38461 -0.17901 39  ILE A C   
265  O O   . ILE A 66  ? 1.38909 1.88613 1.59364 -0.17821 -0.39788 -0.18253 39  ILE A O   
266  C CB  . ILE A 66  ? 1.65728 2.10534 1.83701 -0.13568 -0.35761 -0.15367 39  ILE A CB  
267  C CG1 . ILE A 66  ? 1.77160 2.22052 1.94080 -0.11144 -0.35219 -0.13986 39  ILE A CG1 
268  C CG2 . ILE A 66  ? 1.51063 1.99251 1.73826 -0.14782 -0.35657 -0.15338 39  ILE A CG2 
269  C CD1 . ILE A 66  ? 1.47157 1.91580 1.65650 -0.10670 -0.33182 -0.13032 39  ILE A CD1 
270  N N   . ILE A 67  ? 1.72634 2.14366 1.87974 -0.17870 -0.37410 -0.18777 40  ILE A N   
271  C CA  . ILE A 67  ? 1.53412 1.94669 1.69794 -0.20373 -0.37552 -0.20203 40  ILE A CA  
272  C C   . ILE A 67  ? 1.60094 2.02076 1.74466 -0.21494 -0.39634 -0.21592 40  ILE A C   
273  O O   . ILE A 67  ? 1.82525 2.26538 1.98788 -0.23617 -0.40617 -0.22678 40  ILE A O   
274  C CB  . ILE A 67  ? 1.71368 2.07931 1.86187 -0.20912 -0.35501 -0.20491 40  ILE A CB  
275  C CG1 . ILE A 67  ? 1.75340 2.11931 1.92546 -0.20196 -0.33654 -0.19128 40  ILE A CG1 
276  C CG2 . ILE A 67  ? 1.35791 1.70885 1.50858 -0.23391 -0.35446 -0.22061 40  ILE A CG2 
277  C CD1 . ILE A 67  ? 1.32961 1.65644 1.49101 -0.20555 -0.31683 -0.19084 40  ILE A CD1 
278  N N   . THR A 68  ? 1.57432 1.97809 1.67811 -0.20237 -0.40330 -0.21604 41  THR A N   
279  C CA  . THR A 68  ? 1.70927 2.11649 1.78715 -0.21322 -0.42277 -0.22940 41  THR A CA  
280  C C   . THR A 68  ? 1.83293 2.29813 1.93613 -0.21493 -0.44640 -0.22714 41  THR A C   
281  O O   . THR A 68  ? 1.90445 2.38922 2.01395 -0.23736 -0.46119 -0.24060 41  THR A O   
282  C CB  . THR A 68  ? 1.61329 1.98939 1.64141 -0.19751 -0.42303 -0.22798 41  THR A CB  
283  O OG1 . THR A 68  ? 1.76840 2.09474 1.77537 -0.19823 -0.40156 -0.23112 41  THR A OG1 
284  C CG2 . THR A 68  ? 1.83420 2.21539 1.83208 -0.20804 -0.44410 -0.24099 41  THR A CG2 
285  N N   . LEU A 69  ? 1.83744 2.33133 1.95534 -0.19171 -0.44963 -0.21004 42  LEU A N   
286  C CA  . LEU A 69  ? 1.93764 2.49099 2.08271 -0.18853 -0.47105 -0.20429 42  LEU A CA  
287  C C   . LEU A 69  ? 2.05120 2.64446 2.25165 -0.20257 -0.46989 -0.20389 42  LEU A C   
288  O O   . LEU A 69  ? 2.17103 2.82008 2.40204 -0.19956 -0.48603 -0.19749 42  LEU A O   
289  C CB  . LEU A 69  ? 1.84369 2.40958 1.98373 -0.15595 -0.47179 -0.18474 42  LEU A CB  
290  C CG  . LEU A 69  ? 1.70486 2.23555 1.79079 -0.13970 -0.47333 -0.18242 42  LEU A CG  
291  C CD1 . LEU A 69  ? 1.85456 2.40138 1.93979 -0.10842 -0.47416 -0.16235 42  LEU A CD1 
292  C CD2 . LEU A 69  ? 1.87678 2.41139 1.93277 -0.15423 -0.49499 -0.19609 42  LEU A CD2 
293  N N   . ALA A 70  ? 1.92860 2.49635 2.14319 -0.21702 -0.45088 -0.20938 43  ALA A N   
294  C CA  . ALA A 70  ? 1.83065 2.43227 2.09622 -0.23097 -0.44713 -0.20860 43  ALA A CA  
295  C C   . ALA A 70  ? 1.94955 2.58126 2.22878 -0.26064 -0.46554 -0.22451 43  ALA A C   
296  O O   . ALA A 70  ? 1.89002 2.49077 2.13872 -0.28004 -0.46864 -0.24138 43  ALA A O   
297  C CB  . ALA A 70  ? 1.82804 2.39023 2.10014 -0.23761 -0.42102 -0.20897 43  ALA A CB  
298  N N   . LYS A 71  ? 2.04323 2.73580 2.36817 -0.26489 -0.47691 -0.21939 44  LYS A N   
299  C CA  . LYS A 71  ? 1.92045 2.65093 2.26484 -0.29565 -0.49504 -0.23381 44  LYS A CA  
300  C C   . LYS A 71  ? 1.80623 2.56953 2.20531 -0.31300 -0.48696 -0.23326 44  LYS A C   
301  O O   . LYS A 71  ? 1.69167 2.46898 2.10322 -0.34579 -0.49451 -0.24903 44  LYS A O   
302  C CB  . LYS A 71  ? 1.83608 2.62403 2.18256 -0.28776 -0.52462 -0.22927 44  LYS A CB  
303  C CG  . LYS A 71  ? 1.90434 2.66442 2.19606 -0.27003 -0.53428 -0.22845 44  LYS A CG  
304  C CD  . LYS A 71  ? 2.20461 3.02539 2.50048 -0.26029 -0.56362 -0.22095 44  LYS A CD  
305  C CE  . LYS A 71  ? 2.11564 2.90608 2.35434 -0.24194 -0.57198 -0.21893 44  LYS A CE  
306  N NZ  . LYS A 71  ? 2.28208 3.13189 2.52206 -0.23160 -0.60141 -0.21013 44  LYS A NZ  
307  N N   . LYS A 72  ? 1.82730 2.60149 2.25730 -0.29380 -0.47092 -0.21648 45  LYS A N   
308  C CA  . LYS A 72  ? 1.62114 2.42723 2.10337 -0.30801 -0.46134 -0.21408 45  LYS A CA  
309  C C   . LYS A 72  ? 1.67989 2.43689 2.16249 -0.30843 -0.43162 -0.21134 45  LYS A C   
310  O O   . LYS A 72  ? 1.50536 2.25101 2.00304 -0.33498 -0.42178 -0.22119 45  LYS A O   
311  C CB  . LYS A 72  ? 1.91215 2.78258 2.43651 -0.28585 -0.46776 -0.19558 45  LYS A CB  
312  C CG  . LYS A 72  ? 2.18429 3.11363 2.71505 -0.28324 -0.49810 -0.19462 45  LYS A CG  
313  C CD  . LYS A 72  ? 1.87425 2.86420 2.44712 -0.25636 -0.50092 -0.17353 45  LYS A CD  
314  C CE  . LYS A 72  ? 1.61372 2.66593 2.19345 -0.25112 -0.53196 -0.16983 45  LYS A CE  
315  N NZ  . LYS A 72  ? 1.54674 2.65774 2.16807 -0.22104 -0.53305 -0.14711 45  LYS A NZ  
316  N N   . TYR A 73  ? 1.71356 2.44083 2.17848 -0.28033 -0.41681 -0.19787 46  TYR A N   
317  C CA  . TYR A 73  ? 1.39003 2.07709 1.85574 -0.27888 -0.38993 -0.19279 46  TYR A CA  
318  C C   . TYR A 73  ? 1.46731 2.11315 1.89495 -0.25197 -0.37970 -0.18332 46  TYR A C   
319  O O   . TYR A 73  ? 1.60439 2.25672 2.01142 -0.23237 -0.39120 -0.17845 46  TYR A O   
320  C CB  . TYR A 73  ? 1.30880 2.03310 1.82395 -0.27740 -0.37858 -0.18150 46  TYR A CB  
321  C CG  . TYR A 73  ? 1.44030 2.20024 1.96988 -0.24775 -0.38122 -0.16479 46  TYR A CG  
322  C CD1 . TYR A 73  ? 1.73287 2.55410 2.29035 -0.24395 -0.40100 -0.16169 46  TYR A CD1 
323  C CD2 . TYR A 73  ? 1.51141 2.24355 2.02578 -0.22361 -0.36327 -0.15183 46  TYR A CD2 
324  C CE1 . TYR A 73  ? 1.77680 2.62771 2.34701 -0.21421 -0.40106 -0.14504 46  TYR A CE1 
325  C CE2 . TYR A 73  ? 1.44947 2.20763 1.97357 -0.19660 -0.36279 -0.13725 46  TYR A CE2 
326  C CZ  . TYR A 73  ? 1.51181 2.32782 2.06401 -0.19065 -0.38082 -0.13337 46  TYR A CZ  
327  O OH  . TYR A 73  ? 1.47080 2.30990 2.03236 -0.16116 -0.37797 -0.11746 46  TYR A OH  
328  N N   . ILE A 74  ? 1.35919 1.96326 1.77755 -0.25189 -0.35760 -0.18016 47  ILE A N   
329  C CA  . ILE A 74  ? 1.31925 1.88838 1.70779 -0.22926 -0.34470 -0.16996 47  ILE A CA  
330  C C   . ILE A 74  ? 1.47733 2.03955 1.88600 -0.22782 -0.32239 -0.15965 47  ILE A C   
331  O O   . ILE A 74  ? 1.44071 1.97820 1.85148 -0.24322 -0.30994 -0.16332 47  ILE A O   
332  C CB  . ILE A 74  ? 1.39823 1.91598 1.74194 -0.23161 -0.34212 -0.17818 47  ILE A CB  
333  C CG1 . ILE A 74  ? 1.28737 1.80902 1.60581 -0.23282 -0.36344 -0.18853 47  ILE A CG1 
334  C CG2 . ILE A 74  ? 1.45239 1.93908 1.77045 -0.21117 -0.32741 -0.16698 47  ILE A CG2 
335  C CD1 . ILE A 74  ? 1.35842 1.82955 1.63271 -0.23539 -0.35954 -0.19735 47  ILE A CD1 
336  N N   . TYR A 75  ? 1.43838 2.02038 1.85978 -0.20914 -0.31629 -0.14644 48  TYR A N   
337  C CA  . TYR A 75  ? 1.39002 1.96619 1.82630 -0.20654 -0.29508 -0.13616 48  TYR A CA  
338  C C   . TYR A 75  ? 1.43994 1.98035 1.84047 -0.18917 -0.28319 -0.12823 48  TYR A C   
339  O O   . TYR A 75  ? 1.55569 2.09622 1.93688 -0.17087 -0.28845 -0.12423 48  TYR A O   
340  C CB  . TYR A 75  ? 1.44190 2.06440 1.91772 -0.19955 -0.29344 -0.12754 48  TYR A CB  
341  C CG  . TYR A 75  ? 1.54476 2.20797 2.06235 -0.21951 -0.30235 -0.13407 48  TYR A CG  
342  C CD1 . TYR A 75  ? 1.68636 2.33520 2.20557 -0.24539 -0.30424 -0.14629 48  TYR A CD1 
343  C CD2 . TYR A 75  ? 1.57405 2.29008 2.12978 -0.21285 -0.30759 -0.12782 48  TYR A CD2 
344  C CE1 . TYR A 75  ? 1.73793 2.42325 2.29420 -0.26696 -0.31173 -0.15347 48  TYR A CE1 
345  C CE2 . TYR A 75  ? 1.61486 2.37302 2.21115 -0.23306 -0.31607 -0.13376 48  TYR A CE2 
346  C CZ  . TYR A 75  ? 1.66926 2.41155 2.26498 -0.26152 -0.31839 -0.14724 48  TYR A CZ  
347  O OH  . TYR A 75  ? 1.76676 2.55024 2.40173 -0.28480 -0.32622 -0.15432 48  TYR A OH  
348  N N   . ILE A 76  ? 1.24538 1.75605 1.63694 -0.19547 -0.26702 -0.12546 49  ILE A N   
349  C CA  . ILE A 76  ? 1.53377 2.01269 1.89251 -0.18348 -0.25561 -0.11844 49  ILE A CA  
350  C C   . ILE A 76  ? 1.68266 2.16166 2.05432 -0.18409 -0.23653 -0.10796 49  ILE A C   
351  O O   . ILE A 76  ? 1.54757 2.03241 1.94349 -0.19801 -0.22951 -0.10766 49  ILE A O   
352  C CB  . ILE A 76  ? 1.53433 1.97656 1.86418 -0.18983 -0.25547 -0.12436 49  ILE A CB  
353  C CG1 . ILE A 76  ? 1.50383 1.94477 1.81957 -0.19189 -0.27372 -0.13628 49  ILE A CG1 
354  C CG2 . ILE A 76  ? 1.84815 2.26425 2.14623 -0.17814 -0.24508 -0.11668 49  ILE A CG2 
355  C CD1 . ILE A 76  ? 1.57205 1.97653 1.86116 -0.19874 -0.27200 -0.14335 49  ILE A CD1 
356  N N   . ALA A 77  ? 1.59272 2.06343 1.94587 -0.17017 -0.22733 -0.09967 50  ALA A N   
357  C CA  . ALA A 77  ? 1.26758 1.73708 1.62705 -0.17106 -0.20913 -0.09005 50  ALA A CA  
358  C C   . ALA A 77  ? 1.49062 1.93274 1.81294 -0.16378 -0.20014 -0.08462 50  ALA A C   
359  O O   . ALA A 77  ? 2.03331 2.46821 2.33260 -0.15145 -0.20312 -0.08489 50  ALA A O   
360  C CB  . ALA A 77  ? 1.50049 1.99929 1.88510 -0.16348 -0.20422 -0.08522 50  ALA A CB  
361  N N   . SER A 78  ? 1.46992 1.89785 1.78631 -0.17187 -0.18895 -0.07908 51  SER A N   
362  C CA  . SER A 78  ? 1.60946 2.01776 1.89375 -0.16807 -0.18017 -0.07295 51  SER A CA  
363  C C   . SER A 78  ? 1.61182 2.01905 1.90228 -0.17691 -0.16617 -0.06366 51  SER A C   
364  O O   . SER A 78  ? 1.85585 2.27476 2.17427 -0.18478 -0.16214 -0.06199 51  SER A O   
365  C CB  . SER A 78  ? 1.51716 1.90467 1.77506 -0.16661 -0.18792 -0.07695 51  SER A CB  
366  O OG  . SER A 78  ? 1.24722 1.62619 1.51230 -0.17569 -0.18716 -0.07649 51  SER A OG  
367  N N   . PHE A 79  ? 1.41244 1.80671 1.67584 -0.17638 -0.15875 -0.05713 52  PHE A N   
368  C CA  . PHE A 79  ? 1.50855 1.90301 1.77339 -0.18409 -0.14657 -0.04652 52  PHE A CA  
369  C C   . PHE A 79  ? 1.65120 2.03692 1.92215 -0.18957 -0.14821 -0.04345 52  PHE A C   
370  O O   . PHE A 79  ? 1.70531 2.09463 1.99979 -0.19642 -0.14380 -0.04073 52  PHE A O   
371  C CB  . PHE A 79  ? 1.67083 2.05866 1.90381 -0.18318 -0.13898 -0.04054 52  PHE A CB  
372  C CG  . PHE A 79  ? 1.62275 2.01271 1.85222 -0.19097 -0.12882 -0.02839 52  PHE A CG  
373  C CD1 . PHE A 79  ? 1.48154 1.88098 1.72374 -0.19586 -0.11756 -0.02258 52  PHE A CD1 
374  C CD2 . PHE A 79  ? 1.90447 2.28879 2.11799 -0.19265 -0.13018 -0.02166 52  PHE A CD2 
375  C CE1 . PHE A 79  ? 1.58787 1.98960 1.82431 -0.20268 -0.10863 -0.01022 52  PHE A CE1 
376  C CE2 . PHE A 79  ? 1.89735 2.28717 2.10770 -0.19842 -0.12186 -0.00837 52  PHE A CE2 
377  C CZ  . PHE A 79  ? 1.87042 2.26819 2.09087 -0.20364 -0.11146 -0.00260 52  PHE A CZ  
378  N N   . CYS A 80  ? 1.81672 2.18949 2.06634 -0.18633 -0.15282 -0.04347 53  CYS A N   
379  C CA  . CYS A 80  ? 1.78541 2.14672 2.03812 -0.18846 -0.15269 -0.04014 53  CYS A CA  
380  C C   . CYS A 80  ? 1.68678 2.03750 1.94151 -0.18665 -0.16387 -0.05286 53  CYS A C   
381  O O   . CYS A 80  ? 1.61198 1.96446 1.85856 -0.18202 -0.17321 -0.06228 53  CYS A O   
382  C CB  . CYS A 80  ? 1.65632 2.01331 1.88565 -0.18566 -0.14882 -0.03005 53  CYS A CB  
383  S SG  . CYS A 80  ? 1.98557 2.33021 2.22064 -0.18490 -0.14386 -0.02058 53  CYS A SG  
384  N N   . CYS A 81  ? 1.74333 2.08103 2.00691 -0.19031 -0.16190 -0.05275 54  CYS A N   
385  C CA  . CYS A 81  ? 1.67294 1.99684 1.93540 -0.19102 -0.17087 -0.06559 54  CYS A CA  
386  C C   . CYS A 81  ? 1.81382 2.11632 2.06508 -0.18827 -0.16483 -0.06079 54  CYS A C   
387  O O   . CYS A 81  ? 1.94471 2.23808 2.20783 -0.19200 -0.15470 -0.05347 54  CYS A O   
388  C CB  . CYS A 81  ? 1.57859 1.90680 1.86732 -0.20141 -0.17367 -0.07431 54  CYS A CB  
389  S SG  . CYS A 81  ? 1.80279 2.11822 2.08683 -0.20550 -0.18741 -0.09294 54  CYS A SG  
390  N N   . ASN A 82  ? 1.70838 2.00216 1.93689 -0.18089 -0.16959 -0.06407 55  ASN A N   
391  C CA  . ASN A 82  ? 1.66416 1.93924 1.88175 -0.17587 -0.16313 -0.05940 55  ASN A CA  
392  C C   . ASN A 82  ? 1.64879 1.91297 1.84395 -0.17046 -0.17135 -0.07008 55  ASN A C   
393  O O   . ASN A 82  ? 1.82359 2.09121 2.00116 -0.16356 -0.17042 -0.06449 55  ASN A O   
394  C CB  . ASN A 82  ? 1.78979 2.07506 2.00301 -0.17057 -0.15361 -0.04096 55  ASN A CB  
395  C CG  . ASN A 82  ? 1.93376 2.20359 2.14312 -0.16368 -0.14437 -0.03228 55  ASN A CG  
396  O OD1 . ASN A 82  ? 2.06680 2.31362 2.28133 -0.16460 -0.14028 -0.03795 55  ASN A OD1 
397  N ND2 . ASN A 82  ? 1.54625 1.82903 1.74624 -0.15699 -0.14026 -0.01833 55  ASN A ND2 
398  N N   . PRO A 83  ? 1.55573 1.80759 1.74974 -0.17462 -0.17944 -0.08554 56  PRO A N   
399  C CA  . PRO A 83  ? 1.58199 1.82387 1.75175 -0.16961 -0.18792 -0.09585 56  PRO A CA  
400  C C   . PRO A 83  ? 1.74995 1.96990 1.90393 -0.16345 -0.17958 -0.09379 56  PRO A C   
401  O O   . PRO A 83  ? 2.03670 2.25145 2.16836 -0.15739 -0.18317 -0.09757 56  PRO A O   
402  C CB  . PRO A 83  ? 1.48301 1.72154 1.65780 -0.17785 -0.19950 -0.11223 56  PRO A CB  
403  C CG  . PRO A 83  ? 1.43593 1.68924 1.64031 -0.18723 -0.19785 -0.11002 56  PRO A CG  
404  C CD  . PRO A 83  ? 1.54877 1.79811 1.76241 -0.18575 -0.18218 -0.09476 56  PRO A CD  
405  N N   . LEU A 84  ? 1.56653 1.77263 1.73109 -0.16386 -0.16709 -0.08707 57  LEU A N   
406  C CA  . LEU A 84  ? 1.86206 2.04460 2.01349 -0.15652 -0.15710 -0.08555 57  LEU A CA  
407  C C   . LEU A 84  ? 1.92522 2.12062 2.06887 -0.14525 -0.15058 -0.07018 57  LEU A C   
408  O O   . LEU A 84  ? 1.73544 1.91580 1.87121 -0.13697 -0.14063 -0.06611 57  LEU A O   
409  C CB  . LEU A 84  ? 1.68512 1.84562 1.85025 -0.15934 -0.14361 -0.08228 57  LEU A CB  
410  C CG  . LEU A 84  ? 1.22817 1.37832 1.40441 -0.17434 -0.14839 -0.09666 57  LEU A CG  
411  C CD1 . LEU A 84  ? 1.59542 1.71762 1.78154 -0.17758 -0.13174 -0.09295 57  LEU A CD1 
412  C CD2 . LEU A 84  ? 1.42103 1.55982 1.57916 -0.18040 -0.16107 -0.11757 57  LEU A CD2 
413  N N   . SER A 85  ? 1.71829 1.94124 1.86348 -0.14535 -0.15513 -0.06188 58  SER A N   
414  C CA  . SER A 85  ? 1.71755 1.95688 1.85559 -0.13813 -0.14984 -0.04774 58  SER A CA  
415  C C   . SER A 85  ? 1.81866 2.05064 1.93353 -0.13296 -0.15212 -0.05457 58  SER A C   
416  O O   . SER A 85  ? 1.98805 2.22870 2.09867 -0.12622 -0.14485 -0.04365 58  SER A O   
417  C CB  . SER A 85  ? 1.81378 2.08102 1.95459 -0.14291 -0.15397 -0.04013 58  SER A CB  
418  O OG  . SER A 85  ? 1.74560 2.01377 1.87868 -0.14807 -0.16494 -0.05319 58  SER A OG  
419  N N   . THR A 86  ? 1.72178 1.94016 1.82196 -0.13587 -0.16191 -0.07137 59  THR A N   
420  C CA  . THR A 86  ? 1.88225 2.09034 1.95761 -0.13137 -0.16374 -0.07859 59  THR A CA  
421  C C   . THR A 86  ? 1.83171 2.01108 1.89637 -0.13242 -0.16707 -0.09498 59  THR A C   
422  O O   . THR A 86  ? 1.67208 1.84041 1.74928 -0.13784 -0.16759 -0.10079 59  THR A O   
423  C CB  . THR A 86  ? 1.83757 2.05844 1.89737 -0.13375 -0.17295 -0.08178 59  THR A CB  
424  O OG1 . THR A 86  ? 1.58948 1.80958 1.65255 -0.13867 -0.18422 -0.09193 59  THR A OG1 
425  C CG2 . THR A 86  ? 1.97667 2.22366 2.04265 -0.13567 -0.16882 -0.06737 59  THR A CG2 
426  N N   . THR A 87  ? 1.69184 1.85866 1.73119 -0.12873 -0.16897 -0.10294 60  THR A N   
427  C CA  . THR A 87  ? 1.47351 1.61227 1.49660 -0.13042 -0.17209 -0.11909 60  THR A CA  
428  C C   . THR A 87  ? 1.76429 1.90576 1.78312 -0.13794 -0.18926 -0.13203 60  THR A C   
429  O O   . THR A 87  ? 1.85484 1.98494 1.87876 -0.14544 -0.19387 -0.14274 60  THR A O   
430  C CB  . THR A 87  ? 1.48459 1.60916 1.48036 -0.12341 -0.16691 -0.12209 60  THR A CB  
431  O OG1 . THR A 87  ? 1.66186 1.79138 1.66578 -0.11531 -0.15102 -0.10785 60  THR A OG1 
432  C CG2 . THR A 87  ? 1.54516 1.63752 1.52103 -0.12567 -0.16778 -0.13876 60  THR A CG2 
433  N N   . ARG A 88  ? 1.79343 1.95039 1.80287 -0.13618 -0.19823 -0.13078 61  ARG A N   
434  C CA  . ARG A 88  ? 1.60010 1.76295 1.60603 -0.13991 -0.21426 -0.14045 61  ARG A CA  
435  C C   . ARG A 88  ? 1.66320 1.84232 1.69977 -0.14725 -0.21865 -0.13958 61  ARG A C   
436  O O   . ARG A 88  ? 1.75917 1.94041 1.80009 -0.15336 -0.23026 -0.14997 61  ARG A O   
437  C CB  . ARG A 88  ? 1.57153 1.74493 1.56172 -0.13434 -0.21910 -0.13647 61  ARG A CB  
438  C CG  . ARG A 88  ? 1.78349 1.94148 1.74272 -0.12841 -0.21399 -0.13702 61  ARG A CG  
439  C CD  . ARG A 88  ? 2.08859 2.25203 2.02975 -0.12426 -0.21834 -0.13434 61  ARG A CD  
440  N NE  . ARG A 88  ? 2.07453 2.22492 1.98807 -0.12038 -0.21068 -0.13296 61  ARG A NE  
441  C CZ  . ARG A 88  ? 1.82385 1.95476 1.70840 -0.11689 -0.21415 -0.14118 61  ARG A CZ  
442  N NH1 . ARG A 88  ? 1.45283 1.57594 1.33043 -0.11709 -0.22657 -0.15164 61  ARG A NH1 
443  N NH2 . ARG A 88  ? 1.97022 2.09075 1.83161 -0.11417 -0.20500 -0.13873 61  ARG A NH2 
444  N N   . GLY A 89  ? 1.70723 1.90011 1.76515 -0.14749 -0.20962 -0.12693 62  GLY A N   
445  C CA  . GLY A 89  ? 1.67870 1.88516 1.76565 -0.15481 -0.21109 -0.12533 62  GLY A CA  
446  C C   . GLY A 89  ? 1.77497 1.96449 1.87159 -0.16293 -0.20871 -0.13356 62  GLY A C   
447  O O   . GLY A 89  ? 1.90793 2.10477 2.02030 -0.17214 -0.21640 -0.14088 62  GLY A O   
448  N N   . ALA A 90  ? 1.51925 1.68548 1.60635 -0.16001 -0.19689 -0.13257 63  ALA A N   
449  C CA  . ALA A 90  ? 1.55223 1.69407 1.64264 -0.16798 -0.19176 -0.14184 63  ALA A CA  
450  C C   . ALA A 90  ? 1.72407 1.85564 1.79755 -0.17613 -0.20551 -0.16110 63  ALA A C   
451  O O   . ALA A 90  ? 1.83521 1.95987 1.91787 -0.18918 -0.20865 -0.17165 63  ALA A O   
452  C CB  . ALA A 90  ? 1.71359 1.83035 1.79446 -0.16000 -0.17412 -0.13586 63  ALA A CB  
453  N N   . LEU A 91  ? 1.84470 1.97589 1.89235 -0.16974 -0.21393 -0.16575 64  LEU A N   
454  C CA  . LEU A 91  ? 1.82129 1.94634 1.85024 -0.17676 -0.22888 -0.18262 64  LEU A CA  
455  C C   . LEU A 91  ? 1.79585 1.95080 1.84491 -0.18455 -0.24550 -0.18592 64  LEU A C   
456  O O   . LEU A 91  ? 1.57630 1.73080 1.62660 -0.19746 -0.25558 -0.19935 64  LEU A O   
457  C CB  . LEU A 91  ? 1.72226 1.84110 1.71835 -0.16659 -0.23329 -0.18416 64  LEU A CB  
458  C CG  . LEU A 91  ? 1.59406 1.68696 1.57029 -0.15823 -0.21673 -0.18088 64  LEU A CG  
459  C CD1 . LEU A 91  ? 1.76105 1.85087 1.70611 -0.14934 -0.22105 -0.18164 64  LEU A CD1 
460  C CD2 . LEU A 91  ? 1.62883 1.68834 1.59470 -0.16552 -0.20801 -0.19292 64  LEU A CD2 
461  N N   . ILE A 92  ? 1.83020 2.01218 1.89493 -0.17741 -0.24793 -0.17392 65  ILE A N   
462  C CA  . ILE A 92  ? 1.68764 1.90036 1.77542 -0.18233 -0.26092 -0.17473 65  ILE A CA  
463  C C   . ILE A 92  ? 1.70721 1.92395 1.82481 -0.19681 -0.25697 -0.17746 65  ILE A C   
464  O O   . ILE A 92  ? 1.76350 1.99715 1.89528 -0.20799 -0.26916 -0.18631 65  ILE A O   
465  C CB  . ILE A 92  ? 1.81516 2.04992 1.91150 -0.17107 -0.25952 -0.16089 65  ILE A CB  
466  C CG1 . ILE A 92  ? 1.88618 2.11534 1.95124 -0.15875 -0.26409 -0.15979 65  ILE A CG1 
467  C CG2 . ILE A 92  ? 1.71545 1.98219 1.84027 -0.17467 -0.26891 -0.15988 65  ILE A CG2 
468  C CD1 . ILE A 92  ? 1.69196 1.92786 1.74337 -0.15819 -0.28203 -0.16952 65  ILE A CD1 
469  N N   . PHE A 93  ? 1.76018 1.96255 1.88780 -0.19711 -0.23964 -0.16919 66  PHE A N   
470  C CA  . PHE A 93  ? 1.73218 1.93285 1.88569 -0.21065 -0.23285 -0.17055 66  PHE A CA  
471  C C   . PHE A 93  ? 1.81555 1.99311 1.95891 -0.22572 -0.23564 -0.18820 66  PHE A C   
472  O O   . PHE A 93  ? 1.75874 1.94482 1.92174 -0.24196 -0.23967 -0.19588 66  PHE A O   
473  C CB  . PHE A 93  ? 1.87057 2.05790 2.03224 -0.20510 -0.21292 -0.15594 66  PHE A CB  
474  C CG  . PHE A 93  ? 1.80896 2.00161 2.00059 -0.21575 -0.20485 -0.15149 66  PHE A CG  
475  C CD1 . PHE A 93  ? 1.89640 2.12185 2.11302 -0.21872 -0.21055 -0.14642 66  PHE A CD1 
476  C CD2 . PHE A 93  ? 1.88612 2.04887 2.08000 -0.22200 -0.18953 -0.15163 66  PHE A CD2 
477  C CE1 . PHE A 93  ? 1.91366 2.14378 2.15727 -0.22902 -0.20191 -0.14201 66  PHE A CE1 
478  C CE2 . PHE A 93  ? 2.01542 2.18037 2.23514 -0.23209 -0.18066 -0.14679 66  PHE A CE2 
479  C CZ  . PHE A 93  ? 1.82775 2.02735 2.07252 -0.23621 -0.18721 -0.14212 66  PHE A CZ  
480  N N   . ASP A 94  ? 2.05442 2.20244 2.16597 -0.22195 -0.23290 -0.19557 67  ASP A N   
481  C CA  . ASP A 94  ? 2.06120 2.18321 2.15655 -0.23734 -0.23489 -0.21425 67  ASP A CA  
482  C C   . ASP A 94  ? 2.01615 2.16322 2.10944 -0.24847 -0.25843 -0.22777 67  ASP A C   
483  O O   . ASP A 94  ? 2.14448 2.28923 2.24320 -0.26863 -0.26365 -0.24181 67  ASP A O   
484  C CB  . ASP A 94  ? 2.12300 2.20739 2.18263 -0.22895 -0.22493 -0.21835 67  ASP A CB  
485  C CG  . ASP A 94  ? 2.41762 2.46978 2.48005 -0.22428 -0.20007 -0.21020 67  ASP A CG  
486  O OD1 . ASP A 94  ? 2.38119 2.42566 2.46411 -0.23514 -0.19107 -0.20983 67  ASP A OD1 
487  O OD2 . ASP A 94  ? 2.83703 2.87228 2.88175 -0.20932 -0.18885 -0.20328 67  ASP A OD2 
488  N N   . LYS A 95  ? 1.74626 1.91769 1.83099 -0.23597 -0.27257 -0.22337 68  LYS A N   
489  C CA  . LYS A 95  ? 1.77692 1.97821 1.86250 -0.24323 -0.29571 -0.23255 68  LYS A CA  
490  C C   . LYS A 95  ? 1.82979 2.06738 1.95682 -0.25451 -0.30194 -0.23053 68  LYS A C   
491  O O   . LYS A 95  ? 1.78043 2.03599 1.91521 -0.27146 -0.31641 -0.24280 68  LYS A O   
492  C CB  . LYS A 95  ? 1.95700 2.17495 2.02621 -0.22435 -0.30647 -0.22477 68  LYS A CB  
493  C CG  . LYS A 95  ? 2.16393 2.35160 2.18886 -0.21759 -0.30627 -0.23116 68  LYS A CG  
494  C CD  . LYS A 95  ? 1.81829 1.99747 1.82197 -0.23402 -0.31948 -0.25039 68  LYS A CD  
495  C CE  . LYS A 95  ? 2.21508 2.36424 2.17194 -0.22682 -0.31905 -0.25666 68  LYS A CE  
496  N NZ  . LYS A 95  ? 2.07826 2.18589 2.02096 -0.22163 -0.29513 -0.25486 68  LYS A NZ  
497  N N   . LEU A 96  ? 1.86150 2.11161 2.01528 -0.24653 -0.29083 -0.21526 69  LEU A N   
498  C CA  . LEU A 96  ? 1.71922 2.00221 1.91312 -0.25688 -0.29350 -0.21247 69  LEU A CA  
499  C C   . LEU A 96  ? 1.72657 1.99213 1.93221 -0.28012 -0.28561 -0.22325 69  LEU A C   
500  O O   . LEU A 96  ? 1.77525 2.06767 2.00645 -0.29698 -0.29441 -0.22980 69  LEU A O   
501  C CB  . LEU A 96  ? 1.82436 2.11949 2.03861 -0.24327 -0.28119 -0.19396 69  LEU A CB  
502  C CG  . LEU A 96  ? 1.71342 2.04782 1.96799 -0.24875 -0.28396 -0.18839 69  LEU A CG  
503  C CD1 . LEU A 96  ? 1.62068 1.99450 1.88222 -0.24424 -0.30452 -0.19063 69  LEU A CD1 
504  C CD2 . LEU A 96  ? 1.46655 1.80428 1.73384 -0.23659 -0.26868 -0.17111 69  LEU A CD2 
505  N N   . LYS A 97  ? 1.85010 2.07060 2.03762 -0.28131 -0.26788 -0.22480 70  LYS A N   
506  C CA  . LYS A 97  ? 1.62441 1.81855 1.81651 -0.30308 -0.25754 -0.23596 70  LYS A CA  
507  C C   . LYS A 97  ? 1.97078 2.16451 2.14768 -0.32377 -0.27342 -0.25783 70  LYS A C   
508  O O   . LYS A 97  ? 2.22993 2.43130 2.42472 -0.34756 -0.27581 -0.26838 70  LYS A O   
509  C CB  . LYS A 97  ? 1.71102 1.85450 1.88277 -0.29569 -0.23430 -0.23178 70  LYS A CB  
510  C CG  . LYS A 97  ? 1.93067 2.03553 2.09981 -0.31619 -0.21976 -0.24353 70  LYS A CG  
511  C CD  . LYS A 97  ? 2.07173 2.12971 2.22498 -0.30328 -0.19444 -0.23447 70  LYS A CD  
512  C CE  . LYS A 97  ? 1.83492 1.84605 1.98011 -0.32210 -0.17713 -0.24660 70  LYS A CE  
513  N NZ  . LYS A 97  ? 1.71569 1.70190 1.82757 -0.33700 -0.18441 -0.27029 70  LYS A NZ  
514  N N   . GLU A 98  ? 2.06926 2.25454 2.21181 -0.31646 -0.28429 -0.26508 71  GLU A N   
515  C CA  . GLU A 98  ? 2.01516 2.20401 2.13938 -0.33594 -0.30197 -0.28550 71  GLU A CA  
516  C C   . GLU A 98  ? 1.86803 2.11596 2.02288 -0.34554 -0.32482 -0.28653 71  GLU A C   
517  O O   . GLU A 98  ? 1.85372 2.11328 2.01529 -0.37172 -0.33480 -0.30203 71  GLU A O   
518  C CB  . GLU A 98  ? 2.00788 2.17975 2.08863 -0.32316 -0.30944 -0.29014 71  GLU A CB  
519  C CG  . GLU A 98  ? 2.17374 2.34868 2.22935 -0.34277 -0.32865 -0.31099 71  GLU A CG  
520  C CD  . GLU A 98  ? 2.41677 2.57274 2.42680 -0.32934 -0.33452 -0.31455 71  GLU A CD  
521  O OE1 . GLU A 98  ? 2.47417 2.61599 2.47449 -0.30523 -0.32337 -0.30082 71  GLU A OE1 
522  O OE2 . GLU A 98  ? 2.46792 2.62399 2.45101 -0.34405 -0.35022 -0.33113 71  GLU A OE2 
523  N N   . ALA A 99  ? 1.77742 2.06369 1.95133 -0.32496 -0.33244 -0.27004 72  ALA A N   
524  C CA  . ALA A 99  ? 1.75429 2.09938 1.96108 -0.32979 -0.35190 -0.26793 72  ALA A CA  
525  C C   . ALA A 99  ? 1.94447 2.30559 2.19152 -0.35126 -0.34518 -0.27005 72  ALA A C   
526  O O   . ALA A 99  ? 1.97713 2.37464 2.24374 -0.37125 -0.36098 -0.27965 72  ALA A O   
527  C CB  . ALA A 99  ? 1.75518 2.12933 1.97383 -0.30167 -0.35495 -0.24849 72  ALA A CB  
528  N N   . SER A 100 ? 2.18082 2.51697 2.44073 -0.34798 -0.32183 -0.26055 73  SER A N   
529  C CA  . SER A 100 ? 1.74180 2.08748 2.03740 -0.36831 -0.31237 -0.26165 73  SER A CA  
530  C C   . SER A 100 ? 1.72134 2.04042 2.00543 -0.39986 -0.31087 -0.28286 73  SER A C   
531  O O   . SER A 100 ? 2.08570 2.42917 2.39846 -0.42417 -0.31436 -0.29017 73  SER A O   
532  C CB  . SER A 100 ? 1.72219 2.04242 2.02792 -0.35651 -0.28698 -0.24567 73  SER A CB  
533  O OG  . SER A 100 ? 1.89333 2.15552 2.16803 -0.35547 -0.26954 -0.24889 73  SER A OG  
534  N N   . GLU A 101 ? 1.86061 2.12868 2.10249 -0.40086 -0.30419 -0.29331 74  GLU A N   
535  C CA  . GLU A 101 ? 2.01262 2.24897 2.23701 -0.43160 -0.30122 -0.31541 74  GLU A CA  
536  C C   . GLU A 101 ? 2.08726 2.36335 2.30956 -0.45227 -0.32941 -0.33220 74  GLU A C   
537  O O   . GLU A 101 ? 2.24453 2.51842 2.47072 -0.48510 -0.33133 -0.34971 74  GLU A O   
538  C CB  . GLU A 101 ? 2.13463 2.30510 2.31249 -0.42487 -0.28514 -0.32177 74  GLU A CB  
539  C CG  . GLU A 101 ? 2.41089 2.53884 2.59101 -0.40998 -0.25538 -0.30708 74  GLU A CG  
540  C CD  . GLU A 101 ? 2.31729 2.38245 2.45413 -0.40318 -0.23830 -0.31321 74  GLU A CD  
541  O OE1 . GLU A 101 ? 2.23963 2.28926 2.34279 -0.41382 -0.24802 -0.33152 74  GLU A OE1 
542  O OE2 . GLU A 101 ? 2.26273 2.29540 2.39907 -0.38674 -0.21487 -0.29912 74  GLU A OE2 
543  N N   . LYS A 102 ? 2.08189 2.39470 2.29720 -0.43437 -0.35125 -0.32686 75  LYS A N   
544  C CA  . LYS A 102 ? 1.97982 2.33524 2.19243 -0.45154 -0.37990 -0.34032 75  LYS A CA  
545  C C   . LYS A 102 ? 1.79751 2.21963 2.06203 -0.46527 -0.39352 -0.33688 75  LYS A C   
546  O O   . LYS A 102 ? 1.74158 2.20521 2.00997 -0.48425 -0.41747 -0.34840 75  LYS A O   
547  C CB  . LYS A 102 ? 1.78238 2.15412 1.96929 -0.42588 -0.39783 -0.33363 75  LYS A CB  
548  C CG  . LYS A 102 ? 2.01099 2.32225 2.14358 -0.41696 -0.38795 -0.34060 75  LYS A CG  
549  C CD  . LYS A 102 ? 2.32481 2.59840 2.42619 -0.44932 -0.38609 -0.36626 75  LYS A CD  
550  C CE  . LYS A 102 ? 2.23179 2.43772 2.28259 -0.43935 -0.36863 -0.37202 75  LYS A CE  
551  N NZ  . LYS A 102 ? 2.27737 2.49114 2.29755 -0.41570 -0.38259 -0.36623 75  LYS A NZ  
552  N N   . GLY A 103 ? 1.90119 2.33663 2.20526 -0.45663 -0.37900 -0.32119 76  GLY A N   
553  C CA  . GLY A 103 ? 1.77345 2.27151 2.12942 -0.46849 -0.38833 -0.31673 76  GLY A CA  
554  C C   . GLY A 103 ? 1.68268 2.22693 2.06959 -0.43764 -0.39235 -0.29378 76  GLY A C   
555  O O   . GLY A 103 ? 1.82327 2.42334 2.25552 -0.44412 -0.39934 -0.28831 76  GLY A O   
556  N N   . ILE A 104 ? 1.76090 2.28410 2.12534 -0.40514 -0.38696 -0.28040 77  ILE A N   
557  C CA  . ILE A 104 ? 1.70237 2.26246 2.09052 -0.37598 -0.38852 -0.25961 77  ILE A CA  
558  C C   . ILE A 104 ? 1.69777 2.24944 2.11519 -0.37264 -0.36449 -0.24725 77  ILE A C   
559  O O   . ILE A 104 ? 1.82547 2.32528 2.22602 -0.37342 -0.34356 -0.24685 77  ILE A O   
560  C CB  . ILE A 104 ? 1.80514 2.34160 2.15482 -0.34567 -0.39015 -0.25126 77  ILE A CB  
561  C CG1 . ILE A 104 ? 1.64766 2.18543 1.96250 -0.35049 -0.41216 -0.26419 77  ILE A CG1 
562  C CG2 . ILE A 104 ? 1.70918 2.28151 2.07982 -0.31710 -0.39164 -0.23135 77  ILE A CG2 
563  C CD1 . ILE A 104 ? 1.71415 2.31920 2.05316 -0.35572 -0.43889 -0.26490 77  ILE A CD1 
564  N N   . LYS A 105 ? 1.29350 1.89702 1.75457 -0.36806 -0.36687 -0.23622 78  LYS A N   
565  C CA  . LYS A 105 ? 1.50343 2.10314 1.99216 -0.36452 -0.34449 -0.22370 78  LYS A CA  
566  C C   . LYS A 105 ? 1.70354 2.27672 2.17174 -0.33331 -0.33165 -0.20780 78  LYS A C   
567  O O   . LYS A 105 ? 1.78557 2.38492 2.25566 -0.31015 -0.33933 -0.19721 78  LYS A O   
568  C CB  . LYS A 105 ? 1.53019 2.19462 2.07095 -0.36855 -0.35016 -0.21705 78  LYS A CB  
569  C CG  . LYS A 105 ? 1.78414 2.44590 2.35436 -0.36967 -0.32644 -0.20595 78  LYS A CG  
570  C CD  . LYS A 105 ? 1.82847 2.55621 2.45177 -0.37512 -0.33116 -0.20038 78  LYS A CD  
571  C CE  . LYS A 105 ? 1.70855 2.43078 2.35877 -0.37886 -0.30614 -0.19042 78  LYS A CE  
572  N NZ  . LYS A 105 ? 1.48026 2.26758 2.18385 -0.38364 -0.30845 -0.18453 78  LYS A NZ  
573  N N   . ILE A 106 ? 1.57245 2.09391 2.02054 -0.33286 -0.31162 -0.20573 79  ILE A N   
574  C CA  . ILE A 106 ? 1.54150 2.03656 1.96813 -0.30731 -0.29903 -0.19174 79  ILE A CA  
575  C C   . ILE A 106 ? 1.68032 2.17606 2.13182 -0.30587 -0.27851 -0.17858 79  ILE A C   
576  O O   . ILE A 106 ? 1.94458 2.41886 2.40418 -0.32268 -0.26458 -0.18091 79  ILE A O   
577  C CB  . ILE A 106 ? 1.62087 2.06072 2.00478 -0.30523 -0.29226 -0.19710 79  ILE A CB  
578  C CG1 . ILE A 106 ? 1.69772 2.13357 2.05648 -0.31303 -0.31100 -0.21322 79  ILE A CG1 
579  C CG2 . ILE A 106 ? 1.36190 1.78410 1.72347 -0.27914 -0.28381 -0.18326 79  ILE A CG2 
580  C CD1 . ILE A 106 ? 1.39978 1.86526 1.74929 -0.29475 -0.32981 -0.20981 79  ILE A CD1 
581  N N   . ILE A 107 ? 1.39624 1.91392 1.85734 -0.28592 -0.27545 -0.16468 80  ILE A N   
582  C CA  . ILE A 107 ? 1.43296 1.95154 1.91254 -0.28232 -0.25595 -0.15134 80  ILE A CA  
583  C C   . ILE A 107 ? 1.50007 1.99789 1.95204 -0.25914 -0.24753 -0.13938 80  ILE A C   
584  O O   . ILE A 107 ? 1.65851 2.16894 2.09900 -0.24194 -0.25663 -0.13665 80  ILE A O   
585  C CB  . ILE A 107 ? 1.33416 1.90402 1.85656 -0.28384 -0.25766 -0.14657 80  ILE A CB  
586  C CG1 . ILE A 107 ? 1.50079 2.09338 2.05341 -0.31101 -0.26434 -0.15834 80  ILE A CG1 
587  C CG2 . ILE A 107 ? 1.44499 2.01297 1.97969 -0.27702 -0.23652 -0.13212 80  ILE A CG2 
588  C CD1 . ILE A 107 ? 1.65520 2.30193 2.25485 -0.31442 -0.26444 -0.15317 80  ILE A CD1 
589  N N   . VAL A 108 ? 1.32514 1.79157 1.76583 -0.25921 -0.22998 -0.13184 81  VAL A N   
590  C CA  . VAL A 108 ? 1.46415 1.91090 1.87770 -0.24129 -0.22147 -0.12094 81  VAL A CA  
591  C C   . VAL A 108 ? 1.57955 2.03349 2.00842 -0.23956 -0.20425 -0.10759 81  VAL A C   
592  O O   . VAL A 108 ? 1.67393 2.11675 2.11427 -0.25130 -0.19177 -0.10410 81  VAL A O   
593  C CB  . VAL A 108 ? 1.45796 1.86318 1.84059 -0.24121 -0.21687 -0.12236 81  VAL A CB  
594  C CG1 . VAL A 108 ? 1.42758 1.81907 1.78520 -0.22489 -0.20868 -0.11057 81  VAL A CG1 
595  C CG2 . VAL A 108 ? 1.27862 1.67451 1.64317 -0.24361 -0.23257 -0.13650 81  VAL A CG2 
596  N N   . LEU A 109 ? 1.45232 1.92203 1.87884 -0.22504 -0.20233 -0.10007 82  LEU A N   
597  C CA  . LEU A 109 ? 1.45971 1.93544 1.89530 -0.22256 -0.18564 -0.08799 82  LEU A CA  
598  C C   . LEU A 109 ? 1.51688 1.96658 1.91839 -0.21312 -0.17682 -0.07925 82  LEU A C   
599  O O   . LEU A 109 ? 1.81180 2.25478 2.18809 -0.20101 -0.18276 -0.08018 82  LEU A O   
600  C CB  . LEU A 109 ? 1.45581 1.96432 1.91006 -0.21329 -0.18624 -0.08547 82  LEU A CB  
601  C CG  . LEU A 109 ? 1.45652 2.00220 1.95131 -0.22171 -0.19372 -0.09110 82  LEU A CG  
602  C CD1 . LEU A 109 ? 1.36850 1.94459 1.87983 -0.20782 -0.19012 -0.08497 82  LEU A CD1 
603  C CD2 . LEU A 109 ? 1.37821 1.92568 1.89903 -0.24150 -0.18368 -0.09088 82  LEU A CD2 
604  N N   . LEU A 110 ? 1.50245 1.93889 1.90311 -0.21923 -0.16266 -0.07022 83  LEU A N   
605  C CA  . LEU A 110 ? 1.62100 2.03997 1.99286 -0.21229 -0.15411 -0.06008 83  LEU A CA  
606  C C   . LEU A 110 ? 1.64368 2.06806 2.02433 -0.21658 -0.13764 -0.04812 83  LEU A C   
607  O O   . LEU A 110 ? 1.79017 2.22135 2.19677 -0.22685 -0.13105 -0.04683 83  LEU A O   
608  C CB  . LEU A 110 ? 1.62548 2.01809 1.97890 -0.21344 -0.15525 -0.05943 83  LEU A CB  
609  C CG  . LEU A 110 ? 1.65326 2.03161 2.02002 -0.22424 -0.14677 -0.05607 83  LEU A CG  
610  C CD1 . LEU A 110 ? 1.75875 2.11213 2.10222 -0.21925 -0.14311 -0.04953 83  LEU A CD1 
611  C CD2 . LEU A 110 ? 1.49007 1.86953 1.87749 -0.23542 -0.15451 -0.06968 83  LEU A CD2 
612  N N   . ASP A 111 ? 1.48646 1.90744 1.84360 -0.21005 -0.13063 -0.03979 84  ASP A N   
613  C CA  . ASP A 111 ? 1.48183 1.90732 1.84108 -0.21410 -0.11504 -0.02829 84  ASP A CA  
614  C C   . ASP A 111 ? 1.59815 2.01082 1.96059 -0.22167 -0.10749 -0.01881 84  ASP A C   
615  O O   . ASP A 111 ? 1.78934 2.18578 2.14095 -0.22035 -0.11221 -0.01821 84  ASP A O   
616  C CB  . ASP A 111 ? 1.58234 2.00473 1.90997 -0.20782 -0.11008 -0.02273 84  ASP A CB  
617  C CG  . ASP A 111 ? 1.69218 2.12087 2.01904 -0.21240 -0.09399 -0.01268 84  ASP A CG  
618  O OD1 . ASP A 111 ? 1.85519 2.27978 2.18380 -0.21890 -0.08630 -0.00219 84  ASP A OD1 
619  O OD2 . ASP A 111 ? 1.60251 2.03876 1.92570 -0.20883 -0.08793 -0.01483 84  ASP A OD2 
620  N N   . GLU A 112 ? 1.46373 1.88264 1.84066 -0.22862 -0.09406 -0.01047 85  GLU A N   
621  C CA  . GLU A 112 ? 1.69164 2.09713 2.07199 -0.23501 -0.08443 0.00066  85  GLU A CA  
622  C C   . GLU A 112 ? 1.77145 2.16569 2.12202 -0.22911 -0.08221 0.01359  85  GLU A C   
623  O O   . GLU A 112 ? 1.85341 2.23430 2.20405 -0.23062 -0.07569 0.02427  85  GLU A O   
624  C CB  . GLU A 112 ? 1.78278 2.19806 2.18169 -0.24323 -0.06932 0.00789  85  GLU A CB  
625  C CG  . GLU A 112 ? 1.76729 2.16806 2.18048 -0.25232 -0.05928 0.01552  85  GLU A CG  
626  C CD  . GLU A 112 ? 2.11303 2.52477 2.54825 -0.26199 -0.04452 0.02025  85  GLU A CD  
627  O OE1 . GLU A 112 ? 2.25603 2.68740 2.69474 -0.26038 -0.04140 0.01837  85  GLU A OE1 
628  O OE2 . GLU A 112 ? 2.25073 2.64961 2.69910 -0.27104 -0.03442 0.02596  85  GLU A OE2 
629  N N   . ARG A 113 ? 1.59928 1.99911 1.92472 -0.22264 -0.08686 0.01346  86  ARG A N   
630  C CA  . ARG A 113 ? 1.62236 2.01754 1.92080 -0.21835 -0.08703 0.02485  86  ARG A CA  
631  C C   . ARG A 113 ? 1.73795 2.12186 2.02853 -0.21190 -0.09794 0.01997  86  ARG A C   
632  O O   . ARG A 113 ? 1.93249 2.31398 2.20681 -0.20776 -0.09765 0.03085  86  ARG A O   
633  C CB  . ARG A 113 ? 1.78363 2.18928 2.05638 -0.21774 -0.08573 0.02617  86  ARG A CB  
634  C CG  . ARG A 113 ? 1.84825 2.26282 2.12405 -0.22377 -0.07286 0.03083  86  ARG A CG  
635  C CD  . ARG A 113 ? 2.03041 2.45032 2.27375 -0.22534 -0.06923 0.03364  86  ARG A CD  
636  N NE  . ARG A 113 ? 2.08855 2.51420 2.33192 -0.23114 -0.05509 0.03743  86  ARG A NE  
637  C CZ  . ARG A 113 ? 2.19692 2.62504 2.41093 -0.23562 -0.04790 0.04049  86  ARG A CZ  
638  N NH1 . ARG A 113 ? 2.32814 2.75544 2.51098 -0.23653 -0.05403 0.04026  86  ARG A NH1 
639  N NH2 . ARG A 113 ? 2.09317 2.52432 2.30808 -0.24064 -0.03339 0.04330  86  ARG A NH2 
640  N N   . GLY A 114 ? 1.58364 1.96264 1.88511 -0.21084 -0.10734 0.00458  87  GLY A N   
641  C CA  . GLY A 114 ? 1.77530 2.14045 2.06958 -0.20565 -0.11600 -0.00097 87  GLY A CA  
642  C C   . GLY A 114 ? 1.81927 2.16771 2.13175 -0.20952 -0.11253 -0.00190 87  GLY A C   
643  O O   . GLY A 114 ? 1.55267 1.88805 1.86584 -0.20859 -0.11984 -0.01298 87  GLY A O   
644  N N   . LYS A 115 ? 1.78033 2.12647 2.10500 -0.21463 -0.10011 0.00963  88  LYS A N   
645  C CA  . LYS A 115 ? 1.66496 1.99188 2.00724 -0.22086 -0.09320 0.00889  88  LYS A CA  
646  C C   . LYS A 115 ? 1.88003 2.18418 2.21128 -0.21338 -0.08780 0.01861  88  LYS A C   
647  O O   . LYS A 115 ? 1.77393 2.05512 2.11567 -0.21784 -0.07975 0.01804  88  LYS A O   
648  C CB  . LYS A 115 ? 1.73743 2.06934 2.09646 -0.22943 -0.07993 0.01817  88  LYS A CB  
649  C CG  . LYS A 115 ? 2.07515 2.39517 2.45925 -0.24208 -0.07503 0.00939  88  LYS A CG  
650  C CD  . LYS A 115 ? 2.00539 2.33452 2.40612 -0.25101 -0.06164 0.01809  88  LYS A CD  
651  C CE  . LYS A 115 ? 2.06183 2.38252 2.48936 -0.26665 -0.05667 0.00808  88  LYS A CE  
652  N NZ  . LYS A 115 ? 2.09847 2.43013 2.54358 -0.27599 -0.04276 0.01617  88  LYS A NZ  
653  N N   . ARG A 116 ? 2.05829 2.36803 2.36905 -0.20242 -0.09082 0.02761  89  ARG A N   
654  C CA  . ARG A 116 ? 1.93332 2.22554 2.23598 -0.19269 -0.08459 0.03910  89  ARG A CA  
655  C C   . ARG A 116 ? 1.94521 2.21244 2.24804 -0.19200 -0.08820 0.02380  89  ARG A C   
656  O O   . ARG A 116 ? 1.80011 2.04011 2.10805 -0.19152 -0.07759 0.02666  89  ARG A O   
657  C CB  . ARG A 116 ? 1.93626 2.24712 2.21926 -0.18252 -0.08853 0.05127  89  ARG A CB  
658  C CG  . ARG A 116 ? 1.98226 2.31674 2.25980 -0.18436 -0.08457 0.06722  89  ARG A CG  
659  C CD  . ARG A 116 ? 2.12711 2.48178 2.38482 -0.17700 -0.08934 0.07839  89  ARG A CD  
660  N NE  . ARG A 116 ? 2.46879 2.84713 2.71671 -0.18170 -0.08715 0.09099  89  ARG A NE  
661  C CZ  . ARG A 116 ? 2.59208 2.98501 2.82870 -0.18961 -0.09242 0.08206  89  ARG A CZ  
662  N NH1 . ARG A 116 ? 2.44914 2.83720 2.68430 -0.19201 -0.10049 0.06217  89  ARG A NH1 
663  N NH2 . ARG A 116 ? 2.46416 2.87551 2.68873 -0.19491 -0.08864 0.09376  89  ARG A NH2 
664  N N   . ASN A 117 ? 2.03034 2.30382 2.32510 -0.19209 -0.10198 0.00748  90  ASN A N   
665  C CA  . ASN A 117 ? 1.72044 1.97156 2.01060 -0.19199 -0.10675 -0.00806 90  ASN A CA  
666  C C   . ASN A 117 ? 1.86948 2.10779 2.17588 -0.20620 -0.10767 -0.02400 90  ASN A C   
667  O O   . ASN A 117 ? 2.11640 2.33547 2.41734 -0.20913 -0.11210 -0.03887 90  ASN A O   
668  C CB  . ASN A 117 ? 1.63166 1.89461 1.90542 -0.18732 -0.12124 -0.01895 90  ASN A CB  
669  C CG  . ASN A 117 ? 2.23036 2.50649 2.48741 -0.17612 -0.12059 -0.00518 90  ASN A CG  
670  O OD1 . ASN A 117 ? 2.44857 2.74725 2.69834 -0.17636 -0.12615 -0.00303 90  ASN A OD1 
671  N ND2 . ASN A 117 ? 2.03045 2.29273 2.28124 -0.16668 -0.11290 0.00418  90  ASN A ND2 
672  N N   . LEU A 118 ? 1.99633 2.24577 2.32175 -0.21622 -0.10331 -0.02151 91  LEU A N   
673  C CA  . LEU A 118 ? 1.96315 2.20746 2.30707 -0.23219 -0.10511 -0.03687 91  LEU A CA  
674  C C   . LEU A 118 ? 1.88901 2.09496 2.23136 -0.23785 -0.09526 -0.04182 91  LEU A C   
675  O O   . LEU A 118 ? 1.64016 1.83469 1.98193 -0.24753 -0.10262 -0.06060 91  LEU A O   
676  C CB  . LEU A 118 ? 1.85162 2.11384 2.21715 -0.24127 -0.09809 -0.03000 91  LEU A CB  
677  C CG  . LEU A 118 ? 1.92790 2.19287 2.31746 -0.25979 -0.09958 -0.04459 91  LEU A CG  
678  C CD1 . LEU A 118 ? 1.75696 2.04361 2.14959 -0.26255 -0.11895 -0.06270 91  LEU A CD1 
679  C CD2 . LEU A 118 ? 2.10944 2.39130 2.52010 -0.26745 -0.08922 -0.03503 91  LEU A CD2 
680  N N   . GLY A 119 ? 2.01883 2.20332 2.35854 -0.23183 -0.07789 -0.02480 92  GLY A N   
681  C CA  . GLY A 119 ? 2.11086 2.25263 2.44581 -0.23499 -0.06486 -0.02807 92  GLY A CA  
682  C C   . GLY A 119 ? 2.06257 2.18538 2.37705 -0.22753 -0.07048 -0.03912 92  GLY A C   
683  O O   . GLY A 119 ? 2.13653 2.22399 2.44502 -0.23518 -0.06389 -0.05127 92  GLY A O   
684  N N   . GLU A 120 ? 2.10582 2.24994 2.40752 -0.21375 -0.08148 -0.03573 93  GLU A N   
685  C CA  . GLU A 120 ? 2.02994 2.15896 2.31157 -0.20695 -0.08733 -0.04680 93  GLU A CA  
686  C C   . GLU A 120 ? 1.98995 2.12374 2.26988 -0.22060 -0.10409 -0.07166 93  GLU A C   
687  O O   . GLU A 120 ? 1.75095 1.85918 2.01553 -0.22300 -0.10530 -0.08595 93  GLU A O   
688  C CB  . GLU A 120 ? 2.21708 2.36879 2.48611 -0.18960 -0.09286 -0.03468 93  GLU A CB  
689  C CG  . GLU A 120 ? 2.11105 2.25241 2.35918 -0.18244 -0.09970 -0.04575 93  GLU A CG  
690  C CD  . GLU A 120 ? 2.02794 2.19353 2.26523 -0.16774 -0.10394 -0.03335 93  GLU A CD  
691  O OE1 . GLU A 120 ? 1.89363 2.07238 2.13624 -0.15917 -0.09559 -0.01246 93  GLU A OE1 
692  O OE2 . GLU A 120 ? 1.76082 1.93308 1.98343 -0.16575 -0.11567 -0.04428 93  GLU A OE2 
693  N N   . LEU A 121 ? 2.05611 2.22276 2.35107 -0.22916 -0.11650 -0.07648 94  LEU A N   
694  C CA  . LEU A 121 ? 1.73386 1.91281 2.02881 -0.23960 -0.13429 -0.09718 94  LEU A CA  
695  C C   . LEU A 121 ? 1.82731 1.98702 2.13167 -0.26012 -0.13203 -0.11286 94  LEU A C   
696  O O   . LEU A 121 ? 1.87275 2.01579 2.16276 -0.26712 -0.13906 -0.13016 94  LEU A O   
697  C CB  . LEU A 121 ? 1.52025 1.74140 1.82988 -0.23966 -0.14625 -0.09517 94  LEU A CB  
698  C CG  . LEU A 121 ? 1.79698 2.03697 2.09475 -0.22303 -0.14893 -0.08240 94  LEU A CG  
699  C CD1 . LEU A 121 ? 1.86936 2.14399 2.18303 -0.22453 -0.15448 -0.07907 94  LEU A CD1 
700  C CD2 . LEU A 121 ? 1.79784 2.03321 2.07087 -0.21412 -0.16000 -0.09088 94  LEU A CD2 
701  N N   . GLN A 122 ? 1.76654 1.92773 2.09332 -0.27153 -0.12172 -0.10748 95  GLN A N   
702  C CA  . GLN A 122 ? 1.80912 1.95480 2.14684 -0.29477 -0.11905 -0.12289 95  GLN A CA  
703  C C   . GLN A 122 ? 2.01607 2.10982 2.33223 -0.29825 -0.10630 -0.13058 95  GLN A C   
704  O O   . GLN A 122 ? 1.96664 2.04383 2.28062 -0.31847 -0.10867 -0.14994 95  GLN A O   
705  C CB  . GLN A 122 ? 2.11388 2.26708 2.47817 -0.30519 -0.10642 -0.11292 95  GLN A CB  
706  C CG  . GLN A 122 ? 2.12107 2.32360 2.50776 -0.30367 -0.11637 -0.10687 95  GLN A CG  
707  C CD  . GLN A 122 ? 2.13891 2.34622 2.54883 -0.31197 -0.10096 -0.09477 95  GLN A CD  
708  O OE1 . GLN A 122 ? 2.33139 2.50512 2.73744 -0.31308 -0.08176 -0.08514 95  GLN A OE1 
709  N NE2 . GLN A 122 ? 1.85083 2.09900 2.28449 -0.31681 -0.10797 -0.09437 95  GLN A NE2 
710  N N   . SER A 123 ? 2.06116 2.12935 2.36087 -0.27917 -0.09216 -0.11575 96  SER A N   
711  C CA  . SER A 123 ? 2.02873 2.04494 2.30689 -0.27899 -0.07712 -0.12165 96  SER A CA  
712  C C   . SER A 123 ? 2.02899 2.03717 2.28328 -0.28042 -0.09063 -0.14147 96  SER A C   
713  O O   . SER A 123 ? 1.98457 1.95086 2.22118 -0.29032 -0.08200 -0.15590 96  SER A O   
714  C CB  . SER A 123 ? 2.07878 2.07623 2.34869 -0.25513 -0.05862 -0.09788 96  SER A CB  
715  O OG  . SER A 123 ? 2.30121 2.30311 2.58984 -0.25407 -0.04537 -0.07878 96  SER A OG  
716  N N   . HIS A 124 ? 2.05347 2.09819 2.30432 -0.27118 -0.11049 -0.14266 97  HIS A N   
717  C CA  . HIS A 124 ? 2.12260 2.16125 2.34879 -0.27126 -0.12374 -0.15983 97  HIS A CA  
718  C C   . HIS A 124 ? 2.03754 2.09983 2.26987 -0.29180 -0.14469 -0.18025 97  HIS A C   
719  O O   . HIS A 124 ? 1.95362 1.99866 2.16445 -0.30121 -0.15199 -0.19906 97  HIS A O   
720  C CB  . HIS A 124 ? 1.96735 2.02808 2.18214 -0.24884 -0.13205 -0.14916 97  HIS A CB  
721  C CG  . HIS A 124 ? 2.17627 2.22042 2.36074 -0.24454 -0.13894 -0.16256 97  HIS A CG  
722  N ND1 . HIS A 124 ? 2.20645 2.27514 2.38209 -0.24737 -0.16083 -0.17468 97  HIS A ND1 
723  C CD2 . HIS A 124 ? 2.39533 2.40001 2.55532 -0.23671 -0.12558 -0.16495 97  HIS A CD2 
724  C CE1 . HIS A 124 ? 2.23824 2.28293 2.38383 -0.24262 -0.16123 -0.18435 97  HIS A CE1 
725  N NE2 . HIS A 124 ? 2.50208 2.50782 2.63801 -0.23632 -0.13962 -0.17921 97  HIS A NE2 
726  N N   . CYS A 125 ? 1.95901 2.06196 2.21994 -0.29871 -0.15427 -0.17647 98  CYS A N   
727  C CA  . CYS A 125 ? 1.84570 1.98010 2.11872 -0.31672 -0.17457 -0.19276 98  CYS A CA  
728  C C   . CYS A 125 ? 1.86261 2.00867 2.16765 -0.33620 -0.16838 -0.19254 98  CYS A C   
729  O O   . CYS A 125 ? 1.86078 2.04222 2.19191 -0.33189 -0.17010 -0.18028 98  CYS A O   
730  C CB  . CYS A 125 ? 1.94427 2.12426 2.22170 -0.30290 -0.19409 -0.18792 98  CYS A CB  
731  S SG  . CYS A 125 ? 2.26006 2.42812 2.49940 -0.28224 -0.20180 -0.18891 98  CYS A SG  
732  N N   . PRO A 126 ? 1.92189 2.03688 2.22447 -0.35889 -0.15952 -0.20640 99  PRO A N   
733  C CA  . PRO A 126 ? 2.15884 2.28474 2.49215 -0.38049 -0.15294 -0.20739 99  PRO A CA  
734  C C   . PRO A 126 ? 1.96914 2.14861 2.32745 -0.39677 -0.17542 -0.21851 99  PRO A C   
735  O O   . PRO A 126 ? 1.83478 2.03780 2.22524 -0.41036 -0.17180 -0.21533 99  PRO A O   
736  C CB  . PRO A 126 ? 2.21197 2.28184 2.52836 -0.40044 -0.13577 -0.22083 99  PRO A CB  
737  C CG  . PRO A 126 ? 2.20058 2.24870 2.48138 -0.39835 -0.14512 -0.23651 99  PRO A CG  
738  C CD  . PRO A 126 ? 1.82142 1.88692 2.09137 -0.36689 -0.15295 -0.22219 99  PRO A CD  
739  N N   . ASP A 127 ? 1.89776 2.09868 2.24295 -0.39508 -0.19794 -0.23024 100 ASP A N   
740  C CA  . ASP A 127 ? 1.97085 2.22649 2.33965 -0.40826 -0.22082 -0.23942 100 ASP A CA  
741  C C   . ASP A 127 ? 1.85432 2.15958 2.24228 -0.38591 -0.23204 -0.22391 100 ASP A C   
742  O O   . ASP A 127 ? 1.94635 2.30189 2.36070 -0.39305 -0.24822 -0.22698 100 ASP A O   
743  C CB  . ASP A 127 ? 1.99642 2.25025 2.33927 -0.41922 -0.24007 -0.26007 100 ASP A CB  
744  C CG  . ASP A 127 ? 2.26421 2.46432 2.58276 -0.44276 -0.22791 -0.27790 100 ASP A CG  
745  O OD1 . ASP A 127 ? 2.47509 2.65716 2.80944 -0.46200 -0.21127 -0.27961 100 ASP A OD1 
746  O OD2 . ASP A 127 ? 2.59555 2.76864 2.87731 -0.44217 -0.23341 -0.29030 100 ASP A OD2 
747  N N   . ILE A 128 ? 1.58528 1.87823 1.96054 -0.35962 -0.22327 -0.20741 101 ILE A N   
748  C CA  . ILE A 128 ? 1.60193 1.93413 1.99112 -0.33914 -0.22996 -0.19285 101 ILE A CA  
749  C C   . ILE A 128 ? 1.73904 2.08364 2.15868 -0.34054 -0.21429 -0.17870 101 ILE A C   
750  O O   . ILE A 128 ? 1.82153 2.13269 2.23642 -0.34025 -0.19434 -0.17020 101 ILE A O   
751  C CB  . ILE A 128 ? 1.66854 1.98209 2.02672 -0.31324 -0.22837 -0.18338 101 ILE A CB  
752  C CG1 . ILE A 128 ? 1.60459 1.90937 1.93252 -0.31116 -0.24437 -0.19694 101 ILE A CG1 
753  C CG2 . ILE A 128 ? 1.58243 1.92911 1.95262 -0.29424 -0.23061 -0.16817 101 ILE A CG2 
754  C CD1 . ILE A 128 ? 1.75568 2.04674 2.05445 -0.28699 -0.24387 -0.18837 101 ILE A CD1 
755  N N   . ASN A 129 ? 1.71052 2.10337 2.16098 -0.34094 -0.22247 -0.17517 102 ASN A N   
756  C CA  . ASN A 129 ? 1.74405 2.15289 2.22438 -0.34307 -0.20787 -0.16253 102 ASN A CA  
757  C C   . ASN A 129 ? 1.74266 2.15371 2.21367 -0.31768 -0.20080 -0.14478 102 ASN A C   
758  O O   . ASN A 129 ? 1.66411 2.10515 2.13758 -0.30329 -0.21160 -0.14152 102 ASN A O   
759  C CB  . ASN A 129 ? 1.62903 2.09013 2.14862 -0.35608 -0.21826 -0.16737 102 ASN A CB  
760  C CG  . ASN A 129 ? 1.95370 2.43000 2.50486 -0.36096 -0.20124 -0.15563 102 ASN A CG  
761  O OD1 . ASN A 129 ? 2.07223 2.51492 2.61680 -0.36279 -0.18147 -0.14730 102 ASN A OD1 
762  N ND2 . ASN A 129 ? 1.98078 2.50857 2.56633 -0.36207 -0.20813 -0.15387 102 ASN A ND2 
763  N N   . PHE A 130 ? 1.66299 2.04189 2.12195 -0.31247 -0.18228 -0.13304 103 PHE A N   
764  C CA  . PHE A 130 ? 1.52278 1.90390 1.97209 -0.29251 -0.17437 -0.11627 103 PHE A CA  
765  C C   . PHE A 130 ? 1.66113 2.06298 2.13810 -0.29664 -0.16155 -0.10530 103 PHE A C   
766  O O   . PHE A 130 ? 1.90210 2.29468 2.39565 -0.31244 -0.14958 -0.10468 103 PHE A O   
767  C CB  . PHE A 130 ? 1.64547 1.98590 2.06590 -0.28334 -0.16265 -0.10770 103 PHE A CB  
768  C CG  . PHE A 130 ? 1.75689 2.07532 2.14851 -0.27746 -0.17240 -0.11722 103 PHE A CG  
769  C CD1 . PHE A 130 ? 1.68238 2.00620 2.05229 -0.25982 -0.18083 -0.11427 103 PHE A CD1 
770  C CD2 . PHE A 130 ? 1.74288 2.03260 2.12714 -0.29050 -0.17142 -0.12957 103 PHE A CD2 
771  C CE1 . PHE A 130 ? 1.52056 1.82393 1.86354 -0.25461 -0.18846 -0.12267 103 PHE A CE1 
772  C CE2 . PHE A 130 ? 1.62710 1.89498 1.98297 -0.28503 -0.17874 -0.13860 103 PHE A CE2 
773  C CZ  . PHE A 130 ? 1.53693 1.81280 1.87290 -0.26670 -0.18742 -0.13473 103 PHE A CZ  
774  N N   . ILE A 131 ? 1.54145 1.96866 2.02140 -0.28274 -0.16250 -0.09689 104 ILE A N   
775  C CA  . ILE A 131 ? 1.64328 2.09321 2.14811 -0.28505 -0.15046 -0.08724 104 ILE A CA  
776  C C   . ILE A 131 ? 1.64478 2.08835 2.12893 -0.26864 -0.14064 -0.07249 104 ILE A C   
777  O O   . ILE A 131 ? 1.61777 2.06457 2.08198 -0.25383 -0.14867 -0.07239 104 ILE A O   
778  C CB  . ILE A 131 ? 1.38470 1.87949 1.91965 -0.28664 -0.16076 -0.09342 104 ILE A CB  
779  C CG1 . ILE A 131 ? 1.52789 2.03482 2.08625 -0.30734 -0.17052 -0.10782 104 ILE A CG1 
780  C CG2 . ILE A 131 ? 1.60032 2.11750 2.15756 -0.28519 -0.14603 -0.08229 104 ILE A CG2 
781  C CD1 . ILE A 131 ? 1.29959 1.85754 1.89109 -0.30902 -0.18250 -0.11280 104 ILE A CD1 
782  N N   . THR A 132 ? 1.65456 2.08857 2.14170 -0.27248 -0.12303 -0.06015 105 THR A N   
783  C CA  . THR A 132 ? 1.54141 1.97304 2.00971 -0.26060 -0.11297 -0.04600 105 THR A CA  
784  C C   . THR A 132 ? 1.66824 2.13039 2.15470 -0.25823 -0.10798 -0.04347 105 THR A C   
785  O O   . THR A 132 ? 1.78087 2.26005 2.29819 -0.26930 -0.10130 -0.04423 105 THR A O   
786  C CB  . THR A 132 ? 1.74164 2.14996 2.20242 -0.26497 -0.09654 -0.03233 105 THR A CB  
787  O OG1 . THR A 132 ? 2.02367 2.43749 2.51323 -0.27996 -0.08541 -0.03136 105 THR A OG1 
788  C CG2 . THR A 132 ? 1.62767 2.00448 2.07005 -0.26395 -0.09912 -0.03319 105 THR A CG2 
789  N N   . VAL A 133 ? 1.63795 2.10573 2.10485 -0.24420 -0.10964 -0.04060 106 VAL A N   
790  C CA  . VAL A 133 ? 1.58820 2.08109 2.06776 -0.23853 -0.10399 -0.03899 106 VAL A CA  
791  C C   . VAL A 133 ? 1.64832 2.13129 2.10359 -0.23364 -0.08894 -0.02686 106 VAL A C   
792  O O   . VAL A 133 ? 1.76840 2.23268 2.19037 -0.22782 -0.09083 -0.02308 106 VAL A O   
793  C CB  . VAL A 133 ? 1.53363 2.04038 2.00988 -0.22591 -0.11818 -0.04760 106 VAL A CB  
794  C CG1 . VAL A 133 ? 1.56947 2.10026 2.05981 -0.21773 -0.10955 -0.04471 106 VAL A CG1 
795  C CG2 . VAL A 133 ? 1.59291 2.11103 2.08938 -0.23196 -0.13507 -0.05954 106 VAL A CG2 
796  N N   . ASN A 134 ? 1.63312 2.13009 2.10465 -0.23711 -0.07385 -0.02097 107 ASN A N   
797  C CA  . ASN A 134 ? 1.77578 2.26606 2.22380 -0.23387 -0.05847 -0.01071 107 ASN A CA  
798  C C   . ASN A 134 ? 1.73110 2.24299 2.19443 -0.22766 -0.04982 -0.01271 107 ASN A C   
799  O O   . ASN A 134 ? 1.56523 2.09288 2.05585 -0.23409 -0.03744 -0.00949 107 ASN A O   
800  C CB  . ASN A 134 ? 1.75086 2.23102 2.19898 -0.24482 -0.04450 0.00111  107 ASN A CB  
801  C CG  . ASN A 134 ? 1.85790 2.32964 2.27419 -0.24271 -0.03126 0.01206  107 ASN A CG  
802  O OD1 . ASN A 134 ? 1.77941 2.24969 2.17114 -0.23456 -0.03217 0.00962  107 ASN A OD1 
803  N ND2 . ASN A 134 ? 1.79507 2.25977 2.20925 -0.25094 -0.01850 0.02423  107 ASN A ND2 
804  N N   . ILE A 135 ? 1.82608 2.33745 2.27160 -0.21453 -0.05484 -0.01751 108 ILE A N   
805  C CA  . ILE A 135 ? 1.61738 2.14722 2.07702 -0.20483 -0.04630 -0.01918 108 ILE A CA  
806  C C   . ILE A 135 ? 1.58399 2.10921 2.03132 -0.20650 -0.02334 -0.01122 108 ILE A C   
807  O O   . ILE A 135 ? 1.70411 2.24576 2.16941 -0.20013 -0.01111 -0.01096 108 ILE A O   
808  C CB  . ILE A 135 ? 1.36309 1.88673 1.80146 -0.18925 -0.05555 -0.02524 108 ILE A CB  
809  C CG1 . ILE A 135 ? 1.37630 1.86971 1.76460 -0.18825 -0.05179 -0.02287 108 ILE A CG1 
810  C CG2 . ILE A 135 ? 1.55044 2.08113 2.00145 -0.18730 -0.07804 -0.03325 108 ILE A CG2 
811  C CD1 . ILE A 135 ? 1.56281 2.04479 1.92587 -0.17454 -0.05749 -0.02853 108 ILE A CD1 
812  N N   . ASP A 136 ? 1.45224 1.95665 1.86880 -0.21445 -0.01674 -0.00413 109 ASP A N   
813  C CA  . ASP A 136 ? 1.63860 2.13648 2.03651 -0.21793 0.00445  0.00339  109 ASP A CA  
814  C C   . ASP A 136 ? 1.76315 2.25527 2.16041 -0.23166 0.00992  0.01364  109 ASP A C   
815  O O   . ASP A 136 ? 1.68570 2.16158 2.05414 -0.23538 0.00421  0.01887  109 ASP A O   
816  C CB  . ASP A 136 ? 1.59944 2.07616 1.94874 -0.21295 0.00772  0.00232  109 ASP A CB  
817  C CG  . ASP A 136 ? 1.64082 2.10974 1.96680 -0.21745 0.03028  0.00804  109 ASP A CG  
818  O OD1 . ASP A 136 ? 1.77880 2.26021 2.12906 -0.22132 0.04467  0.01261  109 ASP A OD1 
819  O OD2 . ASP A 136 ? 1.61193 2.06196 1.89387 -0.21846 0.03414  0.00747  109 ASP A OD2 
820  N N   . LYS A 137 ? 1.77845 2.28487 2.20823 -0.23863 0.02156  0.01749  110 LYS A N   
821  C CA  . LYS A 137 ? 1.86460 2.36353 2.29270 -0.25087 0.03149  0.02898  110 LYS A CA  
822  C C   . LYS A 137 ? 1.90531 2.40223 2.31694 -0.25405 0.05426  0.03699  110 LYS A C   
823  O O   . LYS A 137 ? 2.09603 2.58555 2.50040 -0.26345 0.06429  0.04841  110 LYS A O   
824  C CB  . LYS A 137 ? 2.05113 2.56301 2.52425 -0.25988 0.03025  0.02807  110 LYS A CB  
825  C CG  . LYS A 137 ? 2.07554 2.58529 2.56092 -0.25990 0.00902  0.02002  110 LYS A CG  
826  C CD  . LYS A 137 ? 2.08934 2.60199 2.60813 -0.27357 0.01053  0.02061  110 LYS A CD  
827  C CE  . LYS A 137 ? 1.91446 2.41973 2.43924 -0.27497 -0.00907 0.01171  110 LYS A CE  
828  N NZ  . LYS A 137 ? 1.90668 2.40932 2.45985 -0.29067 -0.00585 0.01095  110 LYS A NZ  
829  N N   . LYS A 138 ? 1.70393 2.20517 2.10762 -0.24591 0.06385  0.03166  111 LYS A N   
830  C CA  . LYS A 138 ? 1.93470 2.42981 2.31590 -0.24903 0.08687  0.03775  111 LYS A CA  
831  C C   . LYS A 138 ? 2.05923 2.53240 2.38659 -0.25415 0.08654  0.04420  111 LYS A C   
832  O O   . LYS A 138 ? 2.11636 2.58365 2.42607 -0.26338 0.09929  0.05503  111 LYS A O   
833  C CB  . LYS A 138 ? 1.95226 2.45364 2.33665 -0.23739 0.09851  0.02973  111 LYS A CB  
834  C CG  . LYS A 138 ? 2.21446 2.70359 2.56728 -0.23984 0.12370  0.03358  111 LYS A CG  
835  C CD  . LYS A 138 ? 1.98215 2.47120 2.33355 -0.22570 0.13599  0.02523  111 LYS A CD  
836  C CE  . LYS A 138 ? 1.88355 2.35571 2.19932 -0.22898 0.16337  0.02757  111 LYS A CE  
837  N NZ  . LYS A 138 ? 2.35513 2.84054 2.69449 -0.23716 0.18204  0.03611  111 LYS A NZ  
838  N N   . ASN A 139 ? 1.93250 2.39532 2.23306 -0.24894 0.07181  0.03820  112 ASN A N   
839  C CA  . ASN A 139 ? 1.89224 2.33960 2.14338 -0.25493 0.06900  0.04348  112 ASN A CA  
840  C C   . ASN A 139 ? 1.89104 2.33568 2.13679 -0.25409 0.04651  0.04464  112 ASN A C   
841  O O   . ASN A 139 ? 1.86770 2.30510 2.07665 -0.25923 0.04194  0.05044  112 ASN A O   
842  C CB  . ASN A 139 ? 1.98821 2.42245 2.20151 -0.25211 0.07763  0.03494  112 ASN A CB  
843  C CG  . ASN A 139 ? 2.15937 2.59317 2.37521 -0.25110 0.10263  0.03334  112 ASN A CG  
844  O OD1 . ASN A 139 ? 2.26792 2.70181 2.49544 -0.24010 0.10934  0.02408  112 ASN A OD1 
845  N ND2 . ASN A 139 ? 2.10783 2.54105 2.31235 -0.26145 0.11758  0.04337  112 ASN A ND2 
846  N N   . ASN A 140 ? 1.85470 2.30637 2.13560 -0.24830 0.03274  0.03930  113 ASN A N   
847  C CA  . ASN A 140 ? 1.81234 2.25984 2.09047 -0.24653 0.01311  0.03967  113 ASN A CA  
848  C C   . ASN A 140 ? 1.86074 2.29912 2.10187 -0.24307 0.00414  0.03388  113 ASN A C   
849  O O   . ASN A 140 ? 2.07542 2.50983 2.29439 -0.24581 -0.00505 0.03992  113 ASN A O   
850  C CB  . ASN A 140 ? 1.75606 2.20073 2.03036 -0.25350 0.01319  0.05492  113 ASN A CB  
851  C CG  . ASN A 140 ? 2.10935 2.55860 2.42023 -0.25812 0.02214  0.06008  113 ASN A CG  
852  O OD1 . ASN A 140 ? 2.42548 2.87699 2.73631 -0.26400 0.03906  0.06732  113 ASN A OD1 
853  N ND2 . ASN A 140 ? 1.90894 2.35820 2.24952 -0.25686 0.01173  0.05576  113 ASN A ND2 
854  N N   . VAL A 141 ? 1.69931 2.13460 1.93433 -0.23671 0.00785  0.02272  114 VAL A N   
855  C CA  . VAL A 141 ? 1.66945 2.09248 1.86897 -0.23420 0.00198  0.01567  114 VAL A CA  
856  C C   . VAL A 141 ? 1.65119 2.07364 1.86695 -0.22238 -0.01095 0.00447  114 VAL A C   
857  O O   . VAL A 141 ? 1.84188 2.25644 2.03885 -0.22069 -0.02353 0.00087  114 VAL A O   
858  C CB  . VAL A 141 ? 1.64740 2.05918 1.81380 -0.23737 0.02029  0.01256  114 VAL A CB  
859  C CG1 . VAL A 141 ? 1.61011 2.00586 1.73486 -0.23867 0.01548  0.00542  114 VAL A CG1 
860  C CG2 . VAL A 141 ? 1.79790 2.21161 1.94792 -0.24963 0.03340  0.02373  114 VAL A CG2 
861  N N   . GLY A 142 ? 1.65304 2.08597 1.90372 -0.21428 -0.00811 -0.00040 115 GLY A N   
862  C CA  . GLY A 142 ? 1.69606 2.13135 1.96151 -0.20241 -0.02086 -0.00980 115 GLY A CA  
863  C C   . GLY A 142 ? 1.55009 1.98904 1.83041 -0.20350 -0.04060 -0.01049 115 GLY A C   
864  O O   . GLY A 142 ? 1.62416 2.07082 1.92648 -0.21046 -0.04267 -0.00506 115 GLY A O   
865  N N   . LEU A 143 ? 1.29599 1.72625 1.56195 -0.19657 -0.05355 -0.01738 116 LEU A N   
866  C CA  . LEU A 143 ? 1.57214 2.00208 1.84649 -0.19654 -0.07133 -0.01957 116 LEU A CA  
867  C C   . LEU A 143 ? 1.76698 2.20258 2.05796 -0.18561 -0.08320 -0.02922 116 LEU A C   
868  O O   . LEU A 143 ? 1.86082 2.29387 2.14278 -0.17577 -0.07958 -0.03345 116 LEU A O   
869  C CB  . LEU A 143 ? 1.41947 1.83444 1.65729 -0.19970 -0.07689 -0.01743 116 LEU A CB  
870  C CG  . LEU A 143 ? 1.42667 1.84045 1.64601 -0.21036 -0.06820 -0.00614 116 LEU A CG  
871  C CD1 . LEU A 143 ? 1.65682 2.06302 1.84560 -0.21312 -0.07599 -0.00363 116 LEU A CD1 
872  C CD2 . LEU A 143 ? 1.70991 2.13250 1.95753 -0.21565 -0.06620 0.00231  116 LEU A CD2 
873  N N   . LEU A 144 ? 1.64257 2.08466 1.95611 -0.18732 -0.09677 -0.03231 117 LEU A N   
874  C CA  . LEU A 144 ? 1.42107 1.87166 1.75030 -0.17881 -0.11056 -0.04117 117 LEU A CA  
875  C C   . LEU A 144 ? 1.60047 2.03302 1.89772 -0.17244 -0.12102 -0.04576 117 LEU A C   
876  O O   . LEU A 144 ? 1.61336 2.03531 1.90021 -0.17719 -0.12869 -0.04588 117 LEU A O   
877  C CB  . LEU A 144 ? 1.40426 1.86746 1.76707 -0.18644 -0.12011 -0.04419 117 LEU A CB  
878  C CG  . LEU A 144 ? 1.46602 1.94072 1.84358 -0.18041 -0.13697 -0.05376 117 LEU A CG  
879  C CD1 . LEU A 144 ? 1.61159 2.10733 2.00516 -0.16906 -0.13446 -0.05448 117 LEU A CD1 
880  C CD2 . LEU A 144 ? 1.58849 2.07255 1.99485 -0.19235 -0.14534 -0.05826 117 LEU A CD2 
881  N N   . LEU A 145 ? 1.89338 2.32108 2.17473 -0.16104 -0.11973 -0.04896 118 LEU A N   
882  C CA  . LEU A 145 ? 1.75770 2.16738 2.00848 -0.15477 -0.12845 -0.05350 118 LEU A CA  
883  C C   . LEU A 145 ? 1.86259 2.28026 2.12415 -0.14170 -0.13960 -0.05934 118 LEU A C   
884  O O   . LEU A 145 ? 2.13243 2.53709 2.37057 -0.13074 -0.13786 -0.06088 118 LEU A O   
885  C CB  . LEU A 145 ? 1.52187 1.91156 1.73398 -0.15409 -0.11570 -0.05153 118 LEU A CB  
886  C CG  . LEU A 145 ? 1.47999 1.85885 1.66680 -0.16660 -0.11137 -0.04688 118 LEU A CG  
887  C CD1 . LEU A 145 ? 1.60359 1.99416 1.80630 -0.17669 -0.10204 -0.03913 118 LEU A CD1 
888  C CD2 . LEU A 145 ? 1.61772 1.97652 1.76322 -0.16721 -0.10179 -0.04817 118 LEU A CD2 
889  N N   . GLY A 146 ? 1.46871 1.90759 1.76430 -0.14338 -0.15080 -0.06226 119 GLY A N   
890  C CA  . GLY A 146 ? 1.56968 2.02208 1.87713 -0.13220 -0.16413 -0.06698 119 GLY A CA  
891  C C   . GLY A 146 ? 1.85405 2.28592 2.12926 -0.12581 -0.17503 -0.07154 119 GLY A C   
892  O O   . GLY A 146 ? 1.62061 2.04421 1.87736 -0.11196 -0.17377 -0.07100 119 GLY A O   
893  N N   . CYS A 147 ? 2.04337 2.46499 2.31089 -0.13522 -0.18408 -0.07557 120 CYS A N   
894  C CA  . CYS A 147 ? 1.90726 2.30747 2.14249 -0.13109 -0.19245 -0.07976 120 CYS A CA  
895  C C   . CYS A 147 ? 2.02957 2.43756 2.26478 -0.11856 -0.20596 -0.08402 120 CYS A C   
896  O O   . CYS A 147 ? 1.98124 2.37326 2.18822 -0.10726 -0.20547 -0.08356 120 CYS A O   
897  C CB  . CYS A 147 ? 1.61873 1.99525 1.81776 -0.12908 -0.18003 -0.07590 120 CYS A CB  
898  S SG  . CYS A 147 ? 2.28744 2.63809 2.44906 -0.13057 -0.18603 -0.07946 120 CYS A SG  
899  N N   . PHE A 148 ? 1.66077 2.09407 1.92715 -0.12140 -0.21807 -0.08781 121 PHE A N   
900  C CA  . PHE A 148 ? 1.31800 1.76584 1.58745 -0.11038 -0.23324 -0.09078 121 PHE A CA  
901  C C   . PHE A 148 ? 1.36128 1.82918 1.65498 -0.12227 -0.24945 -0.09868 121 PHE A C   
902  O O   . PHE A 148 ? 1.56072 2.03635 1.87774 -0.13744 -0.24632 -0.10062 121 PHE A O   
903  C CB  . PHE A 148 ? 1.48479 1.95442 1.77162 -0.09524 -0.22796 -0.08369 121 PHE A CB  
904  C CG  . PHE A 148 ? 1.69740 2.19930 2.02816 -0.10210 -0.22327 -0.08114 121 PHE A CG  
905  C CD1 . PHE A 148 ? 1.68115 2.17709 2.01700 -0.10744 -0.20429 -0.07617 121 PHE A CD1 
906  C CD2 . PHE A 148 ? 1.56914 2.10887 1.93538 -0.10429 -0.23773 -0.08364 121 PHE A CD2 
907  C CE1 . PHE A 148 ? 1.44081 1.96532 1.81614 -0.11393 -0.19839 -0.07347 121 PHE A CE1 
908  C CE2 . PHE A 148 ? 1.48958 2.06062 1.89771 -0.11194 -0.23237 -0.08128 121 PHE A CE2 
909  C CZ  . PHE A 148 ? 1.53034 2.09249 1.94295 -0.11625 -0.21194 -0.07603 121 PHE A CZ  
910  N N   . TRP A 149 ? 1.35903 1.83348 1.64428 -0.11595 -0.26631 -0.10331 122 TRP A N   
911  C CA  . TRP A 149 ? 1.44582 1.93985 1.74847 -0.12766 -0.28389 -0.11240 122 TRP A CA  
912  C C   . TRP A 149 ? 1.53277 2.06595 1.85663 -0.11700 -0.29769 -0.10992 122 TRP A C   
913  O O   . TRP A 149 ? 1.65170 2.18470 1.96098 -0.09697 -0.29773 -0.10274 122 TRP A O   
914  C CB  . TRP A 149 ? 1.30189 1.76868 1.57059 -0.13192 -0.29379 -0.12133 122 TRP A CB  
915  C CG  . TRP A 149 ? 1.54259 1.97386 1.79093 -0.14090 -0.28210 -0.12336 122 TRP A CG  
916  C CD1 . TRP A 149 ? 1.49470 1.90963 1.73652 -0.13958 -0.26450 -0.11580 122 TRP A CD1 
917  C CD2 . TRP A 149 ? 1.68416 2.09351 1.91568 -0.15195 -0.28701 -0.13293 122 TRP A CD2 
918  N NE1 . TRP A 149 ? 1.50772 1.89602 1.73253 -0.14800 -0.25919 -0.11860 122 TRP A NE1 
919  C CE2 . TRP A 149 ? 1.65508 2.03767 1.87355 -0.15482 -0.27157 -0.12906 122 TRP A CE2 
920  C CE3 . TRP A 149 ? 1.53371 1.94357 1.75881 -0.15990 -0.30243 -0.14443 122 TRP A CE3 
921  C CZ2 . TRP A 149 ? 1.60612 1.96263 1.80794 -0.16283 -0.26975 -0.13509 122 TRP A CZ2 
922  C CZ3 . TRP A 149 ? 1.49956 1.87911 1.70477 -0.16945 -0.29970 -0.15220 122 TRP A CZ3 
923  C CH2 . TRP A 149 ? 1.62644 1.97962 1.82143 -0.16964 -0.28282 -0.14693 122 TRP A CH2 
924  N N   . VAL A 150 ? 1.44777 2.01466 1.80543 -0.13072 -0.30930 -0.11553 123 VAL A N   
925  C CA  . VAL A 150 ? 1.46858 2.08103 1.85029 -0.12336 -0.32594 -0.11346 123 VAL A CA  
926  C C   . VAL A 150 ? 1.59101 2.22202 1.98439 -0.14495 -0.34500 -0.12647 123 VAL A C   
927  O O   . VAL A 150 ? 1.37928 2.00484 1.78696 -0.16697 -0.34033 -0.13429 123 VAL A O   
928  C CB  . VAL A 150 ? 1.40599 2.05564 1.83003 -0.11620 -0.31616 -0.10320 123 VAL A CB  
929  C CG1 . VAL A 150 ? 1.44717 2.09869 1.89849 -0.13689 -0.30358 -0.10628 123 VAL A CG1 
930  C CG2 . VAL A 150 ? 1.53850 2.24343 1.99394 -0.10998 -0.33463 -0.10031 123 VAL A CG2 
931  N N   . SER A 151 ? 1.56862 2.21995 1.95354 -0.13925 -0.36595 -0.12876 124 SER A N   
932  C CA  . SER A 151 ? 1.41137 2.07682 1.79849 -0.16098 -0.38539 -0.14284 124 SER A CA  
933  C C   . SER A 151 ? 1.55858 2.28030 1.96706 -0.15478 -0.40786 -0.13952 124 SER A C   
934  O O   . SER A 151 ? 1.88219 2.61000 2.27377 -0.13081 -0.41475 -0.12987 124 SER A O   
935  C CB  . SER A 151 ? 1.39807 2.01660 1.73517 -0.16497 -0.38941 -0.15289 124 SER A CB  
936  O OG  . SER A 151 ? 1.65514 2.28344 1.98999 -0.18709 -0.40694 -0.16792 124 SER A OG  
937  N N   . ASP A 152 ? 1.40651 2.16993 1.85235 -0.17679 -0.41866 -0.14681 125 ASP A N   
938  C CA  . ASP A 152 ? 1.57265 2.39610 2.04108 -0.17894 -0.44393 -0.14674 125 ASP A CA  
939  C C   . ASP A 152 ? 1.60505 2.47449 2.10212 -0.15014 -0.44477 -0.12731 125 ASP A C   
940  O O   . ASP A 152 ? 1.83469 2.75378 2.34447 -0.14334 -0.46648 -0.12271 125 ASP A O   
941  C CB  . ASP A 152 ? 1.78266 2.59349 2.20809 -0.18081 -0.46490 -0.15552 125 ASP A CB  
942  C CG  . ASP A 152 ? 1.89902 2.67081 2.29933 -0.21107 -0.46552 -0.17609 125 ASP A CG  
943  O OD1 . ASP A 152 ? 1.94851 2.69864 2.36265 -0.22826 -0.44851 -0.18211 125 ASP A OD1 
944  O OD2 . ASP A 152 ? 1.89384 2.65494 2.25903 -0.21701 -0.48193 -0.18579 125 ASP A OD2 
945  N N   . ASP A 153 ? 1.41955 2.27415 1.92660 -0.13285 -0.42105 -0.11536 126 ASP A N   
946  C CA  . ASP A 153 ? 1.41675 2.30250 1.94336 -0.10150 -0.41651 -0.09626 126 ASP A CA  
947  C C   . ASP A 153 ? 1.50119 2.38010 1.99160 -0.07618 -0.42928 -0.08847 126 ASP A C   
948  O O   . ASP A 153 ? 1.52975 2.45006 2.03853 -0.05247 -0.43634 -0.07362 126 ASP A O   
949  C CB  . ASP A 153 ? 1.49235 2.45357 2.07980 -0.10581 -0.42566 -0.09063 126 ASP A CB  
950  C CG  . ASP A 153 ? 1.70371 2.67067 2.32909 -0.12112 -0.40550 -0.09195 126 ASP A CG  
951  O OD1 . ASP A 153 ? 1.77874 2.69213 2.38269 -0.12384 -0.38372 -0.09446 126 ASP A OD1 
952  O OD2 . ASP A 153 ? 1.59197 2.61893 2.26869 -0.13078 -0.41149 -0.08990 126 ASP A OD2 
953  N N   . GLU A 154 ? 1.62169 2.44851 2.06070 -0.08031 -0.43142 -0.09751 127 GLU A N   
954  C CA  . GLU A 154 ? 1.48312 2.29595 1.88116 -0.05958 -0.44288 -0.09183 127 GLU A CA  
955  C C   . GLU A 154 ? 1.70221 2.44462 2.04914 -0.04948 -0.42476 -0.09205 127 GLU A C   
956  O O   . GLU A 154 ? 1.92440 2.65130 2.24617 -0.02267 -0.42064 -0.07990 127 GLU A O   
957  C CB  . GLU A 154 ? 1.26118 2.09151 1.64475 -0.07824 -0.47110 -0.10453 127 GLU A CB  
958  C CG  . GLU A 154 ? 1.75477 2.66226 2.18424 -0.08630 -0.49396 -0.10273 127 GLU A CG  
959  C CD  . GLU A 154 ? 2.11620 3.03795 2.52570 -0.10790 -0.52173 -0.11705 127 GLU A CD  
960  O OE1 . GLU A 154 ? 1.98283 2.85165 2.34211 -0.11487 -0.52162 -0.12815 127 GLU A OE1 
961  O OE2 . GLU A 154 ? 2.13245 3.11936 2.57605 -0.11873 -0.54330 -0.11744 127 GLU A OE2 
962  N N   . ARG A 155 ? 1.61060 2.31082 1.94199 -0.07009 -0.41317 -0.10475 128 ARG A N   
963  C CA  . ARG A 155 ? 1.39339 2.03188 1.67916 -0.06346 -0.39663 -0.10539 128 ARG A CA  
964  C C   . ARG A 155 ? 1.62254 2.23875 1.92067 -0.06815 -0.37141 -0.10378 128 ARG A C   
965  O O   . ARG A 155 ? 1.60804 2.24465 1.94215 -0.08493 -0.36784 -0.10778 128 ARG A O   
966  C CB  . ARG A 155 ? 1.52347 2.12895 1.77280 -0.08142 -0.40530 -0.12068 128 ARG A CB  
967  C CG  . ARG A 155 ? 1.61519 2.22764 1.83545 -0.07330 -0.42665 -0.12131 128 ARG A CG  
968  C CD  . ARG A 155 ? 1.50953 2.10454 1.70654 -0.09738 -0.43840 -0.13930 128 ARG A CD  
969  N NE  . ARG A 155 ? 1.45078 2.08092 1.68436 -0.12281 -0.44894 -0.15005 128 ARG A NE  
970  C CZ  . ARG A 155 ? 1.76262 2.44568 2.01866 -0.12800 -0.47152 -0.15078 128 ARG A CZ  
971  N NH1 . ARG A 155 ? 1.65540 2.36514 1.90255 -0.10722 -0.48694 -0.13978 128 ARG A NH1 
972  N NH2 . ARG A 155 ? 2.05909 2.76991 2.34717 -0.15502 -0.47861 -0.16220 128 ARG A NH2 
973  N N   . CYS A 156 ? 1.79573 2.37003 2.06240 -0.05433 -0.35369 -0.09782 129 CYS A N   
974  C CA  . CYS A 156 ? 1.58658 2.14038 1.86051 -0.05886 -0.33038 -0.09572 129 CYS A CA  
975  C C   . CYS A 156 ? 1.63563 2.13729 1.86367 -0.05185 -0.31549 -0.09433 129 CYS A C   
976  O O   . CYS A 156 ? 1.76072 2.24506 1.95645 -0.03608 -0.31836 -0.09035 129 CYS A O   
977  C CB  . CYS A 156 ? 1.44785 2.03117 1.75652 -0.04529 -0.31944 -0.08385 129 CYS A CB  
978  S SG  . CYS A 156 ? 1.58705 2.17137 1.87967 -0.01024 -0.31640 -0.06833 129 CYS A SG  
979  N N   . TYR A 157 ? 1.56961 2.04802 1.79536 -0.06456 -0.29957 -0.09714 130 TYR A N   
980  C CA  . TYR A 157 ? 1.46663 1.90203 1.65546 -0.06118 -0.28309 -0.09514 130 TYR A CA  
981  C C   . TYR A 157 ? 1.50825 1.94174 1.71190 -0.06345 -0.26283 -0.08959 130 TYR A C   
982  O O   . TYR A 157 ? 1.43490 1.88931 1.67186 -0.07566 -0.26103 -0.09092 130 TYR A O   
983  C CB  . TYR A 157 ? 1.53147 1.93902 1.69636 -0.07649 -0.28500 -0.10444 130 TYR A CB  
984  C CG  . TYR A 157 ? 1.64951 2.02192 1.78650 -0.07818 -0.26693 -0.10207 130 TYR A CG  
985  C CD1 . TYR A 157 ? 1.85523 2.19956 1.95324 -0.06705 -0.26179 -0.09937 130 TYR A CD1 
986  C CD2 . TYR A 157 ? 1.26736 1.63611 1.41657 -0.09173 -0.25507 -0.10200 130 TYR A CD2 
987  C CE1 . TYR A 157 ? 1.69582 2.01188 1.76915 -0.07139 -0.24593 -0.09783 130 TYR A CE1 
988  C CE2 . TYR A 157 ? 1.20609 1.54870 1.33062 -0.09448 -0.24032 -0.09923 130 TYR A CE2 
989  C CZ  . TYR A 157 ? 1.49088 1.80846 1.57819 -0.08531 -0.23612 -0.09774 130 TYR A CZ  
990  O OH  . TYR A 157 ? 1.42608 1.72109 1.48941 -0.09074 -0.22206 -0.09564 130 TYR A OH  
991  N N   . VAL A 158 ? 1.59123 1.99792 1.76792 -0.05301 -0.24682 -0.08379 131 VAL A N   
992  C CA  . VAL A 158 ? 1.57916 1.97860 1.76111 -0.05674 -0.22644 -0.07953 131 VAL A CA  
993  C C   . VAL A 158 ? 1.55869 1.91712 1.69684 -0.05747 -0.21271 -0.07932 131 VAL A C   
994  O O   . VAL A 158 ? 1.67700 2.01455 1.78513 -0.04447 -0.21089 -0.07723 131 VAL A O   
995  C CB  . VAL A 158 ? 1.47137 1.89139 1.67629 -0.04144 -0.21766 -0.07114 131 VAL A CB  
996  C CG1 . VAL A 158 ? 1.65566 2.06755 1.84054 -0.01819 -0.21925 -0.06520 131 VAL A CG1 
997  C CG2 . VAL A 158 ? 1.23969 1.64509 1.44083 -0.04565 -0.19447 -0.06772 131 VAL A CG2 
998  N N   . GLY A 159 ? 1.40058 1.74850 1.53474 -0.07323 -0.20312 -0.08094 132 GLY A N   
999  C CA  . GLY A 159 ? 1.50284 1.81793 1.59825 -0.07757 -0.19090 -0.08098 132 GLY A CA  
1000 C C   . GLY A 159 ? 1.79630 2.11027 1.89474 -0.09487 -0.18172 -0.08062 132 GLY A C   
1001 O O   . GLY A 159 ? 2.08948 2.42310 2.21709 -0.10060 -0.17827 -0.07831 132 GLY A O   
1002 N N   . ASN A 160 ? 1.66332 1.95619 1.73197 -0.10320 -0.17755 -0.08195 133 ASN A N   
1003 C CA  . ASN A 160 ? 1.61449 1.90865 1.68322 -0.11879 -0.17018 -0.07982 133 ASN A CA  
1004 C C   . ASN A 160 ? 1.78432 2.08024 1.85555 -0.12649 -0.18009 -0.08204 133 ASN A C   
1005 O O   . ASN A 160 ? 1.74849 2.04099 1.80959 -0.13673 -0.17475 -0.07928 133 ASN A O   
1006 C CB  . ASN A 160 ? 1.57232 1.84540 1.60622 -0.12410 -0.15518 -0.07825 133 ASN A CB  
1007 C CG  . ASN A 160 ? 1.74010 1.98798 1.73885 -0.11818 -0.15543 -0.08157 133 ASN A CG  
1008 O OD1 . ASN A 160 ? 1.95844 2.19936 1.94214 -0.12417 -0.16000 -0.08347 133 ASN A OD1 
1009 N ND2 . ASN A 160 ? 1.48761 1.72085 1.47293 -0.10553 -0.14900 -0.08143 133 ASN A ND2 
1010 N N   . ALA A 161 ? 1.78528 2.08728 1.86951 -0.12159 -0.19405 -0.08672 134 ALA A N   
1011 C CA  . ALA A 161 ? 1.60079 1.90141 1.68799 -0.12783 -0.20200 -0.08994 134 ALA A CA  
1012 C C   . ALA A 161 ? 1.70495 2.02453 1.82863 -0.13391 -0.20619 -0.09028 134 ALA A C   
1013 O O   . ALA A 161 ? 1.71675 2.04662 1.85727 -0.13137 -0.21721 -0.09555 134 ALA A O   
1014 C CB  . ALA A 161 ? 1.30717 1.59611 1.37665 -0.12041 -0.21335 -0.09651 134 ALA A CB  
1015 N N   . SER A 162 ? 1.76208 2.08676 1.89690 -0.14291 -0.19722 -0.08430 135 SER A N   
1016 C CA  . SER A 162 ? 1.70132 2.04002 1.86870 -0.14987 -0.19809 -0.08354 135 SER A CA  
1017 C C   . SER A 162 ? 1.69601 2.02739 1.86753 -0.15334 -0.20668 -0.08973 135 SER A C   
1018 O O   . SER A 162 ? 1.68457 2.00072 1.83360 -0.15021 -0.21069 -0.09349 135 SER A O   
1019 C CB  . SER A 162 ? 1.50682 1.84984 1.68030 -0.15759 -0.18545 -0.07391 135 SER A CB  
1020 O OG  . SER A 162 ? 1.77675 2.12535 1.94613 -0.15619 -0.17642 -0.06970 135 SER A OG  
1021 N N   . PHE A 163 ? 1.68444 2.02483 1.88392 -0.16076 -0.20791 -0.09124 136 PHE A N   
1022 C CA  . PHE A 163 ? 1.70400 2.03389 1.90734 -0.16623 -0.21379 -0.09844 136 PHE A CA  
1023 C C   . PHE A 163 ? 1.73909 2.05378 1.93501 -0.16887 -0.20347 -0.09151 136 PHE A C   
1024 O O   . PHE A 163 ? 1.83253 2.14523 2.04589 -0.17568 -0.19692 -0.08797 136 PHE A O   
1025 C CB  . PHE A 163 ? 1.75052 2.09439 1.98533 -0.17526 -0.21786 -0.10342 136 PHE A CB  
1026 C CG  . PHE A 163 ? 1.60081 1.93301 1.83532 -0.18229 -0.22621 -0.11484 136 PHE A CG  
1027 C CD1 . PHE A 163 ? 1.40795 1.71959 1.61432 -0.17784 -0.23072 -0.12052 136 PHE A CD1 
1028 C CD2 . PHE A 163 ? 1.69677 2.03716 1.95748 -0.19485 -0.22833 -0.12059 136 PHE A CD2 
1029 C CE1 . PHE A 163 ? 1.39005 1.68770 1.59223 -0.18524 -0.23698 -0.13217 136 PHE A CE1 
1030 C CE2 . PHE A 163 ? 1.87615 2.20273 2.13292 -0.20395 -0.23505 -0.13279 136 PHE A CE2 
1031 C CZ  . PHE A 163 ? 1.80775 2.11197 2.03411 -0.19888 -0.23925 -0.13881 136 PHE A CZ  
1032 N N   . THR A 164 ? 1.54851 1.85301 1.71820 -0.16281 -0.20135 -0.08860 137 THR A N   
1033 C CA  . THR A 164 ? 1.45393 1.74836 1.61572 -0.16274 -0.19253 -0.08082 137 THR A CA  
1034 C C   . THR A 164 ? 1.69230 1.97131 1.82798 -0.15704 -0.19605 -0.08609 137 THR A C   
1035 O O   . THR A 164 ? 1.81265 2.08925 1.93175 -0.15294 -0.20366 -0.09304 137 THR A O   
1036 C CB  . THR A 164 ? 1.77514 2.08148 1.93419 -0.16330 -0.18292 -0.06743 137 THR A CB  
1037 O OG1 . THR A 164 ? 1.97772 2.28873 2.11938 -0.16065 -0.18488 -0.06904 137 THR A OG1 
1038 C CG2 . THR A 164 ? 2.02064 2.33886 2.20439 -0.16922 -0.17659 -0.06036 137 THR A CG2 
1039 N N   . GLY A 165 ? 1.69925 1.96729 1.83120 -0.15574 -0.18916 -0.08170 138 GLY A N   
1040 C CA  . GLY A 165 ? 1.63857 1.89234 1.74667 -0.15026 -0.19002 -0.08584 138 GLY A CA  
1041 C C   . GLY A 165 ? 1.61481 1.87591 1.70247 -0.14737 -0.18873 -0.08109 138 GLY A C   
1042 O O   . GLY A 165 ? 1.80327 2.05382 1.86840 -0.14367 -0.19265 -0.08775 138 GLY A O   
1043 N N   . GLY A 166 ? 1.40235 1.68027 1.49535 -0.15037 -0.18266 -0.06993 139 GLY A N   
1044 C CA  . GLY A 166 ? 1.63622 1.92014 1.70807 -0.15114 -0.18042 -0.06653 139 GLY A CA  
1045 C C   . GLY A 166 ? 1.68816 1.96616 1.74521 -0.14985 -0.18642 -0.07528 139 GLY A C   
1046 O O   . GLY A 166 ? 1.93622 2.20489 1.96840 -0.14784 -0.18681 -0.07874 139 GLY A O   
1047 N N   . SER A 167 ? 1.58366 1.86695 1.65620 -0.15021 -0.19011 -0.07810 140 SER A N   
1048 C CA  . SER A 167 ? 1.46886 1.74836 1.53059 -0.14602 -0.19484 -0.08429 140 SER A CA  
1049 C C   . SER A 167 ? 1.57333 1.83886 1.62173 -0.13928 -0.20470 -0.09414 140 SER A C   
1050 O O   . SER A 167 ? 1.80286 2.06320 1.83708 -0.13332 -0.20834 -0.09759 140 SER A O   
1051 C CB  . SER A 167 ? 1.51992 1.81274 1.60629 -0.14681 -0.19590 -0.08385 140 SER A CB  
1052 O OG  . SER A 167 ? 1.51719 1.82100 1.61034 -0.15288 -0.18596 -0.07495 140 SER A OG  
1053 N N   . ILE A 168 ? 1.47939 1.73721 1.53002 -0.13959 -0.20815 -0.09827 141 ILE A N   
1054 C CA  . ILE A 168 ? 1.53497 1.77868 1.56941 -0.13469 -0.21743 -0.10813 141 ILE A CA  
1055 C C   . ILE A 168 ? 1.55181 1.77950 1.55950 -0.13257 -0.21280 -0.10850 141 ILE A C   
1056 O O   . ILE A 168 ? 1.76839 1.98261 1.75248 -0.12751 -0.21821 -0.11479 141 ILE A O   
1057 C CB  . ILE A 168 ? 1.47219 1.71570 1.52523 -0.13824 -0.22478 -0.11559 141 ILE A CB  
1058 C CG1 . ILE A 168 ? 1.49408 1.75697 1.57686 -0.14200 -0.22821 -0.11463 141 ILE A CG1 
1059 C CG2 . ILE A 168 ? 1.51439 1.74552 1.54831 -0.13470 -0.23620 -0.12668 141 ILE A CG2 
1060 C CD1 . ILE A 168 ? 1.31896 1.58269 1.42132 -0.14925 -0.23423 -0.12234 141 ILE A CD1 
1061 N N   . HIS A 169 ? 1.63697 1.86770 1.64784 -0.13579 -0.20266 -0.10088 142 HIS A N   
1062 C CA  . HIS A 169 ? 1.64720 1.86643 1.63834 -0.13372 -0.19726 -0.10073 142 HIS A CA  
1063 C C   . HIS A 169 ? 1.64572 1.87352 1.62513 -0.13684 -0.18831 -0.09201 142 HIS A C   
1064 O O   . HIS A 169 ? 1.68398 1.90124 1.63781 -0.13559 -0.18634 -0.09445 142 HIS A O   
1065 C CB  . HIS A 169 ? 1.83167 2.04714 1.83740 -0.13351 -0.19237 -0.09938 142 HIS A CB  
1066 C CG  . HIS A 169 ? 1.87119 2.07034 1.85737 -0.12921 -0.18778 -0.10267 142 HIS A CG  
1067 N ND1 . HIS A 169 ? 2.10252 2.29499 2.06157 -0.12726 -0.18674 -0.10437 142 HIS A ND1 
1068 C CD2 . HIS A 169 ? 1.87745 2.06343 1.86624 -0.12637 -0.18207 -0.10464 142 HIS A CD2 
1069 C CE1 . HIS A 169 ? 2.35121 2.52966 2.29820 -0.12344 -0.18107 -0.10705 142 HIS A CE1 
1070 N NE2 . HIS A 169 ? 2.33117 2.50486 2.29552 -0.12229 -0.17783 -0.10739 142 HIS A NE2 
1071 N N   . THR A 170 ? 1.76704 2.01406 1.76297 -0.14226 -0.18269 -0.08198 143 THR A N   
1072 C CA  . THR A 170 ? 1.70746 1.96736 1.69425 -0.14796 -0.17450 -0.07323 143 THR A CA  
1073 C C   . THR A 170 ? 1.55214 1.81965 1.53066 -0.15541 -0.17241 -0.07097 143 THR A C   
1074 O O   . THR A 170 ? 1.70426 1.97974 1.66848 -0.16301 -0.16630 -0.06646 143 THR A O   
1075 C CB  . THR A 170 ? 1.73124 2.00995 1.73980 -0.14883 -0.16846 -0.06125 143 THR A CB  
1076 O OG1 . THR A 170 ? 1.74831 2.03674 1.77993 -0.15058 -0.16956 -0.05679 143 THR A OG1 
1077 C CG2 . THR A 170 ? 1.82293 2.08988 1.83583 -0.14078 -0.16650 -0.06305 143 THR A CG2 
1078 N N   . ILE A 171 ? 1.58035 1.84596 1.56700 -0.15431 -0.17626 -0.07417 144 ILE A N   
1079 C CA  . ILE A 171 ? 1.35386 1.62279 1.33176 -0.16034 -0.17190 -0.07261 144 ILE A CA  
1080 C C   . ILE A 171 ? 1.64749 1.89574 1.60568 -0.15402 -0.17454 -0.08117 144 ILE A C   
1081 O O   . ILE A 171 ? 2.09734 2.33991 2.06500 -0.14519 -0.18271 -0.08650 144 ILE A O   
1082 C CB  . ILE A 171 ? 1.41651 1.70062 1.41984 -0.16280 -0.17123 -0.06755 144 ILE A CB  
1083 C CG1 . ILE A 171 ? 1.56215 1.86630 1.58185 -0.16805 -0.16751 -0.05645 144 ILE A CG1 
1084 C CG2 . ILE A 171 ? 1.42993 1.71275 1.42144 -0.16778 -0.16529 -0.06772 144 ILE A CG2 
1085 C CD1 . ILE A 171 ? 1.65242 1.97014 1.69502 -0.17088 -0.16558 -0.05016 144 ILE A CD1 
1086 N N   . LYS A 172 ? 1.49930 1.73663 1.42948 -0.15886 -0.16735 -0.08200 145 LYS A N   
1087 C CA  . LYS A 172 ? 1.80577 2.02086 1.71516 -0.15132 -0.16711 -0.08783 145 LYS A CA  
1088 C C   . LYS A 172 ? 1.85347 2.07304 1.77913 -0.14627 -0.16758 -0.08746 145 LYS A C   
1089 O O   . LYS A 172 ? 1.89015 2.11980 1.82246 -0.15412 -0.16042 -0.08346 145 LYS A O   
1090 C CB  . LYS A 172 ? 1.45310 1.65205 1.32778 -0.15970 -0.15594 -0.08851 145 LYS A CB  
1091 C CG  . LYS A 172 ? 1.69765 1.86919 1.54836 -0.15054 -0.15243 -0.09272 145 LYS A CG  
1092 C CD  . LYS A 172 ? 1.52346 1.67555 1.33959 -0.16171 -0.13787 -0.09370 145 LYS A CD  
1093 C CE  . LYS A 172 ? 1.75843 1.87848 1.54951 -0.14981 -0.13219 -0.09648 145 LYS A CE  
1094 N NZ  . LYS A 172 ? 1.48886 1.61369 1.30011 -0.13709 -0.13440 -0.09483 145 LYS A NZ  
1095 N N   . THR A 173 ? 1.74658 1.96100 1.67904 -0.13334 -0.17603 -0.09122 146 THR A N   
1096 C CA  . THR A 173 ? 1.71529 1.93788 1.66683 -0.12677 -0.17670 -0.09026 146 THR A CA  
1097 C C   . THR A 173 ? 1.68564 1.89156 1.62058 -0.11245 -0.17822 -0.09244 146 THR A C   
1098 O O   . THR A 173 ? 1.73518 1.92410 1.64654 -0.10732 -0.18153 -0.09515 146 THR A O   
1099 C CB  . THR A 173 ? 1.77616 2.02056 1.76499 -0.12540 -0.18738 -0.09062 146 THR A CB  
1100 O OG1 . THR A 173 ? 1.81719 2.05799 1.80589 -0.11731 -0.20020 -0.09606 146 THR A OG1 
1101 C CG2 . THR A 173 ? 1.62351 1.88062 1.62712 -0.13676 -0.18548 -0.08700 146 THR A CG2 
1102 N N   . LEU A 174 ? 1.73049 1.94235 1.67879 -0.10475 -0.17530 -0.09017 147 LEU A N   
1103 C CA  . LEU A 174 ? 1.63549 1.83520 1.57235 -0.08796 -0.17573 -0.08943 147 LEU A CA  
1104 C C   . LEU A 174 ? 1.69040 1.91556 1.66345 -0.07826 -0.18253 -0.08710 147 LEU A C   
1105 O O   . LEU A 174 ? 1.83039 2.07478 1.83048 -0.08560 -0.17963 -0.08561 147 LEU A O   
1106 C CB  . LEU A 174 ? 1.56740 1.73914 1.47180 -0.08708 -0.15723 -0.08755 147 LEU A CB  
1107 C CG  . LEU A 174 ? 1.43121 1.58166 1.31545 -0.06787 -0.15366 -0.08502 147 LEU A CG  
1108 C CD1 . LEU A 174 ? 1.52486 1.66310 1.38888 -0.06129 -0.16452 -0.08685 147 LEU A CD1 
1109 C CD2 . LEU A 174 ? 1.47757 1.59547 1.32849 -0.07013 -0.13155 -0.08412 147 LEU A CD2 
1110 N N   . GLY A 175 ? 1.61665 1.84368 1.59011 -0.06187 -0.19160 -0.08602 148 GLY A N   
1111 C CA  . GLY A 175 ? 1.49868 1.75508 1.50800 -0.05202 -0.19952 -0.08316 148 GLY A CA  
1112 C C   . GLY A 175 ? 1.66243 1.92048 1.66502 -0.03328 -0.21084 -0.08068 148 GLY A C   
1113 O O   . GLY A 175 ? 1.81247 2.04381 1.77937 -0.02668 -0.20975 -0.08047 148 GLY A O   
1114 N N   . VAL A 176 ? 1.61101 1.90283 1.64864 -0.02515 -0.22198 -0.07812 149 VAL A N   
1115 C CA  . VAL A 176 ? 1.62301 1.92609 1.66021 -0.00593 -0.23448 -0.07346 149 VAL A CA  
1116 C C   . VAL A 176 ? 1.57567 1.91853 1.64724 -0.01151 -0.25677 -0.07768 149 VAL A C   
1117 O O   . VAL A 176 ? 1.47534 1.84324 1.58232 -0.02369 -0.25793 -0.08040 149 VAL A O   
1118 C CB  . VAL A 176 ? 1.52620 1.83310 1.57096 0.01464  -0.22226 -0.06278 149 VAL A CB  
1119 C CG1 . VAL A 176 ? 1.60355 1.92234 1.64521 0.03716  -0.23514 -0.05530 149 VAL A CG1 
1120 C CG2 . VAL A 176 ? 1.60479 1.86842 1.61400 0.01628  -0.19736 -0.06060 149 VAL A CG2 
1121 N N   . TYR A 177 ? 1.54036 1.88791 1.59930 -0.00382 -0.27401 -0.07846 150 TYR A N   
1122 C CA  . TYR A 177 ? 1.29354 1.67900 1.37990 -0.00919 -0.29662 -0.08299 150 TYR A CA  
1123 C C   . TYR A 177 ? 1.70043 2.11217 1.79425 0.01266  -0.30836 -0.07332 150 TYR A C   
1124 O O   . TYR A 177 ? 1.82052 2.21000 1.88296 0.03145  -0.30377 -0.06544 150 TYR A O   
1125 C CB  . TYR A 177 ? 1.36250 1.73277 1.42545 -0.02282 -0.30888 -0.09404 150 TYR A CB  
1126 C CG  . TYR A 177 ? 1.56500 1.96803 1.64331 -0.02707 -0.33327 -0.09941 150 TYR A CG  
1127 C CD1 . TYR A 177 ? 1.70402 2.13552 1.81866 -0.04533 -0.34137 -0.10722 150 TYR A CD1 
1128 C CD2 . TYR A 177 ? 1.62870 2.03335 1.68289 -0.01419 -0.34791 -0.09680 150 TYR A CD2 
1129 C CE1 . TYR A 177 ? 1.55449 2.01578 1.68115 -0.05269 -0.36359 -0.11373 150 TYR A CE1 
1130 C CE2 . TYR A 177 ? 1.64046 2.07720 1.70613 -0.02027 -0.37139 -0.10233 150 TYR A CE2 
1131 C CZ  . TYR A 177 ? 1.71810 2.18329 1.81998 -0.04060 -0.37924 -0.11153 150 TYR A CZ  
1132 O OH  . TYR A 177 ? 1.74448 2.24136 1.85578 -0.04996 -0.40251 -0.11857 150 TYR A OH  
1133 N N   . SER A 178 ? 1.72112 2.18129 1.85669 0.01007  -0.32329 -0.07318 151 SER A N   
1134 C CA  . SER A 178 ? 1.67375 2.16910 1.82267 0.03072  -0.33674 -0.06254 151 SER A CA  
1135 C C   . SER A 178 ? 1.75419 2.29948 1.93643 0.01710  -0.36170 -0.06908 151 SER A C   
1136 O O   . SER A 178 ? 1.81053 2.37613 2.02663 -0.00257 -0.36179 -0.07661 151 SER A O   
1137 C CB  . SER A 178 ? 1.66111 2.17104 1.83502 0.05019  -0.32060 -0.04885 151 SER A CB  
1138 O OG  . SER A 178 ? 1.86159 2.40812 2.04994 0.07323  -0.33312 -0.03615 151 SER A OG  
1139 N N   . ASP A 179 ? 1.75609 2.32045 1.92669 0.02679  -0.38255 -0.06602 152 ASP A N   
1140 C CA  . ASP A 179 ? 1.70966 2.32698 1.90977 0.01512  -0.40844 -0.07100 152 ASP A CA  
1141 C C   . ASP A 179 ? 1.83738 2.51152 2.07694 0.03525  -0.41632 -0.05546 152 ASP A C   
1142 O O   . ASP A 179 ? 1.80272 2.52120 2.05328 0.03642  -0.44097 -0.05358 152 ASP A O   
1143 C CB  . ASP A 179 ? 1.84177 2.44876 2.00330 0.00986  -0.42865 -0.07853 152 ASP A CB  
1144 C CG  . ASP A 179 ? 2.04817 2.63778 2.17183 0.03850  -0.42956 -0.06474 152 ASP A CG  
1145 O OD1 . ASP A 179 ? 2.13551 2.70999 2.25720 0.06127  -0.41100 -0.05084 152 ASP A OD1 
1146 O OD2 . ASP A 179 ? 1.88407 2.47270 1.97762 0.03794  -0.44777 -0.06784 152 ASP A OD2 
1147 N N   . TYR A 180 ? 1.91990 2.59479 2.18068 0.05119  -0.39535 -0.04396 153 TYR A N   
1148 C CA  . TYR A 180 ? 1.77873 2.50615 2.07911 0.07356  -0.39841 -0.02737 153 TYR A CA  
1149 C C   . TYR A 180 ? 1.76426 2.53961 2.12261 0.05548  -0.39938 -0.03185 153 TYR A C   
1150 O O   . TYR A 180 ? 1.72279 2.47615 2.09103 0.04470  -0.37842 -0.03663 153 TYR A O   
1151 C CB  . TYR A 180 ? 1.67000 2.36638 1.95652 0.10361  -0.37211 -0.01173 153 TYR A CB  
1152 C CG  . TYR A 180 ? 1.67988 2.42174 1.99369 0.13561  -0.37545 0.00900  153 TYR A CG  
1153 C CD1 . TYR A 180 ? 1.83163 2.60326 2.13724 0.15103  -0.39930 0.01826  153 TYR A CD1 
1154 C CD2 . TYR A 180 ? 1.65886 2.41396 2.00551 0.15167  -0.35394 0.02034  153 TYR A CD2 
1155 C CE1 . TYR A 180 ? 1.83074 2.64748 2.16307 0.18283  -0.40247 0.03971  153 TYR A CE1 
1156 C CE2 . TYR A 180 ? 1.54892 2.34640 1.92238 0.18353  -0.35512 0.04084  153 TYR A CE2 
1157 C CZ  . TYR A 180 ? 1.59185 2.42141 1.95931 0.19978  -0.37969 0.05124  153 TYR A CZ  
1158 O OH  . TYR A 180 ? 1.81783 2.69303 2.21393 0.23393  -0.38083 0.07405  153 TYR A OH  
1159 N N   . PRO A 181 ? 1.51861 2.35968 1.91513 0.05038  -0.42288 -0.03042 154 PRO A N   
1160 C CA  . PRO A 181 ? 1.52339 2.40977 1.97393 0.02714  -0.42517 -0.03738 154 PRO A CA  
1161 C C   . PRO A 181 ? 1.54552 2.44205 2.03207 0.04020  -0.39995 -0.02638 154 PRO A C   
1162 O O   . PRO A 181 ? 1.59160 2.48347 2.09948 0.01876  -0.38757 -0.03532 154 PRO A O   
1163 C CB  . PRO A 181 ? 1.46145 2.42063 1.94216 0.02512  -0.45617 -0.03417 154 PRO A CB  
1164 C CG  . PRO A 181 ? 1.53256 2.46942 1.96250 0.03176  -0.47390 -0.03556 154 PRO A CG  
1165 C CD  . PRO A 181 ? 1.43075 2.30397 1.81592 0.05844  -0.45131 -0.02611 154 PRO A CD  
1166 N N   . PRO A 182 ? 1.52552 2.43531 2.01976 0.07510  -0.39035 -0.00672 155 PRO A N   
1167 C CA  . PRO A 182 ? 1.54386 2.46146 2.07177 0.08629  -0.36396 0.00249  155 PRO A CA  
1168 C C   . PRO A 182 ? 1.40139 2.25231 1.90061 0.07705  -0.33569 -0.00548 155 PRO A C   
1169 O O   . PRO A 182 ? 1.58158 2.43963 2.11012 0.06470  -0.32005 -0.00838 155 PRO A O   
1170 C CB  . PRO A 182 ? 1.34482 2.27596 1.87335 0.12840  -0.35782 0.02498  155 PRO A CB  
1171 C CG  . PRO A 182 ? 1.32242 2.28895 1.84473 0.13455  -0.38938 0.02906  155 PRO A CG  
1172 C CD  . PRO A 182 ? 1.39102 2.31537 1.86933 0.10657  -0.40231 0.00935  155 PRO A CD  
1173 N N   . LEU A 183 ? 1.36934 2.15729 1.81151 0.08195  -0.32885 -0.00870 156 LEU A N   
1174 C CA  . LEU A 183 ? 1.53357 2.26171 1.94677 0.07127  -0.30416 -0.01630 156 LEU A CA  
1175 C C   . LEU A 183 ? 1.63361 2.35912 2.05635 0.03537  -0.30916 -0.03316 156 LEU A C   
1176 O O   . LEU A 183 ? 1.60992 2.31953 2.04113 0.02367  -0.28996 -0.03650 156 LEU A O   
1177 C CB  . LEU A 183 ? 1.56075 2.22790 1.91231 0.08179  -0.29853 -0.01653 156 LEU A CB  
1178 C CG  . LEU A 183 ? 1.67263 2.27984 1.99025 0.08378  -0.26865 -0.01719 156 LEU A CG  
1179 C CD1 . LEU A 183 ? 1.55440 2.16753 1.88995 0.10738  -0.24538 -0.00344 156 LEU A CD1 
1180 C CD2 . LEU A 183 ? 1.85777 2.41129 2.11656 0.09097  -0.26701 -0.01832 156 LEU A CD2 
1181 N N   . ALA A 184 ? 1.52165 2.26117 1.94135 0.01781  -0.33402 -0.04356 157 ALA A N   
1182 C CA  . ALA A 184 ? 1.53956 2.27478 1.96791 -0.01533 -0.33808 -0.05920 157 ALA A CA  
1183 C C   . ALA A 184 ? 1.43215 2.21281 1.91637 -0.02785 -0.33398 -0.05873 157 ALA A C   
1184 O O   . ALA A 184 ? 1.40179 2.16637 1.89330 -0.04854 -0.32229 -0.06637 157 ALA A O   
1185 C CB  . ALA A 184 ? 1.39872 2.14111 1.81257 -0.03063 -0.36469 -0.07055 157 ALA A CB  
1186 N N   . THR A 185 ? 1.33974 2.17865 1.86454 -0.01485 -0.34267 -0.04861 158 THR A N   
1187 C CA  . THR A 185 ? 1.47632 2.36223 2.05706 -0.02632 -0.33750 -0.04726 158 THR A CA  
1188 C C   . THR A 185 ? 1.63229 2.49734 2.21930 -0.01550 -0.30619 -0.03924 158 THR A C   
1189 O O   . THR A 185 ? 1.85313 2.72464 2.46624 -0.03378 -0.29429 -0.04334 158 THR A O   
1190 C CB  . THR A 185 ? 1.48616 2.44568 2.11064 -0.01450 -0.35577 -0.03739 158 THR A CB  
1191 O OG1 . THR A 185 ? 1.22772 2.20457 1.83967 -0.02508 -0.38575 -0.04520 158 THR A OG1 
1192 C CG2 . THR A 185 ? 1.40252 2.41486 2.08724 -0.03129 -0.35225 -0.03786 158 THR A CG2 
1193 N N   . ASP A 186 ? 1.53743 2.37467 2.09804 0.01336  -0.29141 -0.02803 159 ASP A N   
1194 C CA  . ASP A 186 ? 1.67757 2.48785 2.23580 0.02218  -0.26032 -0.02212 159 ASP A CA  
1195 C C   . ASP A 186 ? 1.70149 2.45863 2.22847 -0.00034 -0.24766 -0.03359 159 ASP A C   
1196 O O   . ASP A 186 ? 1.90614 2.65225 2.44152 -0.00540 -0.22560 -0.03234 159 ASP A O   
1197 C CB  . ASP A 186 ? 1.81515 2.59960 2.34510 0.05623  -0.24626 -0.00923 159 ASP A CB  
1198 C CG  . ASP A 186 ? 1.92612 2.70649 2.47091 0.07077  -0.21581 0.00022  159 ASP A CG  
1199 O OD1 . ASP A 186 ? 1.86023 2.66900 2.44426 0.05679  -0.20822 -0.00131 159 ASP A OD1 
1200 O OD2 . ASP A 186 ? 2.02188 2.76822 2.53730 0.09556  -0.19807 0.00885  159 ASP A OD2 
1201 N N   . LEU A 187 ? 1.61334 2.33863 2.10408 -0.01326 -0.26086 -0.04390 160 LEU A N   
1202 C CA  . LEU A 187 ? 1.56775 2.24996 2.03374 -0.03490 -0.25118 -0.05364 160 LEU A CA  
1203 C C   . LEU A 187 ? 1.52685 2.23293 2.02642 -0.06290 -0.25771 -0.06225 160 LEU A C   
1204 O O   . LEU A 187 ? 1.62014 2.30597 2.11890 -0.07772 -0.24261 -0.06498 160 LEU A O   
1205 C CB  . LEU A 187 ? 1.46511 2.10475 1.88104 -0.03646 -0.26047 -0.06034 160 LEU A CB  
1206 C CG  . LEU A 187 ? 1.31692 1.90811 1.69985 -0.05184 -0.24814 -0.06701 160 LEU A CG  
1207 C CD1 . LEU A 187 ? 1.22514 1.79181 1.59559 -0.04369 -0.22172 -0.06016 160 LEU A CD1 
1208 C CD2 . LEU A 187 ? 1.37780 1.93368 1.71525 -0.05098 -0.25789 -0.07252 160 LEU A CD2 
1209 N N   . ARG A 188 ? 1.53828 2.28693 2.06601 -0.07115 -0.27982 -0.06637 161 ARG A N   
1210 C CA  . ARG A 188 ? 1.49950 2.27254 2.06140 -0.09872 -0.28488 -0.07475 161 ARG A CA  
1211 C C   . ARG A 188 ? 1.70823 2.50840 2.31179 -0.09994 -0.26657 -0.06758 161 ARG A C   
1212 O O   . ARG A 188 ? 1.83840 2.63769 2.45911 -0.12245 -0.25944 -0.07292 161 ARG A O   
1213 C CB  . ARG A 188 ? 1.53534 2.35247 2.11836 -0.10763 -0.31248 -0.08073 161 ARG A CB  
1214 C CG  . ARG A 188 ? 1.50502 2.33866 2.11425 -0.14059 -0.31949 -0.09291 161 ARG A CG  
1215 C CD  . ARG A 188 ? 1.48957 2.38416 2.15792 -0.14656 -0.31853 -0.08812 161 ARG A CD  
1216 N NE  . ARG A 188 ? 1.44191 2.39331 2.13446 -0.13296 -0.33830 -0.08203 161 ARG A NE  
1217 C CZ  . ARG A 188 ? 1.64024 2.65570 2.38690 -0.13464 -0.34156 -0.07617 161 ARG A CZ  
1218 N NH1 . ARG A 188 ? 1.85852 2.88808 2.64078 -0.15007 -0.32543 -0.07628 161 ARG A NH1 
1219 N NH2 . ARG A 188 ? 1.61642 2.68500 2.38244 -0.12019 -0.36131 -0.06905 161 ARG A NH2 
1220 N N   . ARG A 189 ? 1.79449 2.61705 2.41380 -0.07527 -0.25717 -0.05495 162 ARG A N   
1221 C CA  . ARG A 189 ? 1.75935 2.60252 2.41397 -0.07422 -0.23583 -0.04761 162 ARG A CA  
1222 C C   . ARG A 189 ? 1.71571 2.50768 2.34194 -0.08107 -0.21157 -0.04863 162 ARG A C   
1223 O O   . ARG A 189 ? 1.76784 2.56688 2.41725 -0.09632 -0.19813 -0.04890 162 ARG A O   
1224 C CB  . ARG A 189 ? 1.80355 2.67566 2.47622 -0.04301 -0.22824 -0.03318 162 ARG A CB  
1225 C CG  . ARG A 189 ? 1.80555 2.75229 2.53636 -0.04172 -0.24238 -0.02816 162 ARG A CG  
1226 C CD  . ARG A 189 ? 1.93027 2.90473 2.67871 -0.00673 -0.23302 -0.01148 162 ARG A CD  
1227 N NE  . ARG A 189 ? 1.69930 2.66866 2.42059 0.01576  -0.24903 -0.00649 162 ARG A NE  
1228 C CZ  . ARG A 189 ? 1.69456 2.71784 2.44101 0.02214  -0.27433 -0.00228 162 ARG A CZ  
1229 N NH1 . ARG A 189 ? 1.59618 2.68555 2.39727 0.00645  -0.28748 -0.00329 162 ARG A NH1 
1230 N NH2 . ARG A 189 ? 1.64007 2.65174 2.35536 0.04381  -0.28679 0.00334  162 ARG A NH2 
1231 N N   . ARG A 190 ? 1.65043 2.39189 2.22583 -0.07085 -0.20579 -0.04880 163 ARG A N   
1232 C CA  . ARG A 190 ? 1.74234 2.43769 2.28758 -0.07978 -0.18611 -0.05021 163 ARG A CA  
1233 C C   . ARG A 190 ? 1.63794 2.32253 2.18382 -0.10764 -0.19224 -0.05929 163 ARG A C   
1234 O O   . ARG A 190 ? 1.69058 2.36291 2.23929 -0.12022 -0.17626 -0.05827 163 ARG A O   
1235 C CB  . ARG A 190 ? 1.70252 2.34981 2.19353 -0.06637 -0.18180 -0.04980 163 ARG A CB  
1236 C CG  . ARG A 190 ? 1.66623 2.31695 2.14952 -0.03760 -0.17843 -0.04146 163 ARG A CG  
1237 C CD  . ARG A 190 ? 1.77881 2.43751 2.27873 -0.02442 -0.15343 -0.03228 163 ARG A CD  
1238 N NE  . ARG A 190 ? 1.71935 2.36102 2.19656 0.00354  -0.14337 -0.02446 163 ARG A NE  
1239 C CZ  . ARG A 190 ? 1.70508 2.38023 2.20596 0.02641  -0.14966 -0.01571 163 ARG A CZ  
1240 N NH1 . ARG A 190 ? 1.92737 2.65997 2.47685 0.02345  -0.16784 -0.01415 163 ARG A NH1 
1241 N NH2 . ARG A 190 ? 1.50879 2.15958 1.98350 0.05262  -0.13704 -0.00784 163 ARG A NH2 
1242 N N   . PHE A 191 ? 1.65533 2.34197 2.19614 -0.11695 -0.21424 -0.06781 164 PHE A N   
1243 C CA  . PHE A 191 ? 1.74852 2.42334 2.29087 -0.14253 -0.21880 -0.07656 164 PHE A CA  
1244 C C   . PHE A 191 ? 1.67769 2.38690 2.26737 -0.15917 -0.21350 -0.07646 164 PHE A C   
1245 O O   . PHE A 191 ? 1.65081 2.34244 2.24146 -0.17666 -0.20306 -0.07815 164 PHE A O   
1246 C CB  . PHE A 191 ? 1.81170 2.48417 2.34103 -0.14935 -0.24241 -0.08669 164 PHE A CB  
1247 C CG  . PHE A 191 ? 1.78993 2.44269 2.31568 -0.17404 -0.24486 -0.09613 164 PHE A CG  
1248 C CD1 . PHE A 191 ? 1.54546 2.22636 2.10705 -0.19463 -0.25133 -0.10249 164 PHE A CD1 
1249 C CD2 . PHE A 191 ? 1.75634 2.36229 2.24315 -0.17666 -0.23939 -0.09819 164 PHE A CD2 
1250 C CE1 . PHE A 191 ? 1.32473 1.98162 1.88047 -0.21673 -0.25075 -0.11103 164 PHE A CE1 
1251 C CE2 . PHE A 191 ? 1.65559 2.24136 2.13908 -0.19648 -0.23938 -0.10527 164 PHE A CE2 
1252 C CZ  . PHE A 191 ? 1.54143 2.14976 2.05800 -0.21622 -0.24426 -0.11184 164 PHE A CZ  
1253 N N   . ASP A 192 ? 1.81836 2.57808 2.44824 -0.15386 -0.22037 -0.07364 165 ASP A N   
1254 C CA  . ASP A 192 ? 1.82175 2.61911 2.50003 -0.16979 -0.21422 -0.07301 165 ASP A CA  
1255 C C   . ASP A 192 ? 1.73362 2.51757 2.41493 -0.16755 -0.18656 -0.06450 165 ASP A C   
1256 O O   . ASP A 192 ? 1.76027 2.54257 2.45781 -0.18725 -0.17609 -0.06572 165 ASP A O   
1257 C CB  . ASP A 192 ? 1.90418 2.76372 2.62588 -0.16094 -0.22628 -0.06933 165 ASP A CB  
1258 C CG  . ASP A 192 ? 1.88062 2.76066 2.60297 -0.16811 -0.25521 -0.07835 165 ASP A CG  
1259 O OD1 . ASP A 192 ? 2.05490 2.90960 2.75926 -0.18945 -0.26406 -0.09016 165 ASP A OD1 
1260 O OD2 . ASP A 192 ? 1.75905 2.68041 2.49890 -0.15189 -0.26850 -0.07313 165 ASP A OD2 
1261 N N   . THR A 193 ? 1.84235 2.61475 2.50604 -0.14401 -0.17340 -0.05582 166 THR A N   
1262 C CA  . THR A 193 ? 1.68743 2.44361 2.34726 -0.14193 -0.14639 -0.04852 166 THR A CA  
1263 C C   . THR A 193 ? 1.53039 2.24087 2.15748 -0.15832 -0.13839 -0.05143 166 THR A C   
1264 O O   . THR A 193 ? 1.50546 2.21260 2.14268 -0.17001 -0.12145 -0.04792 166 THR A O   
1265 C CB  . THR A 193 ? 1.63164 2.37414 2.26862 -0.11483 -0.13362 -0.04083 166 THR A CB  
1266 O OG1 . THR A 193 ? 1.83597 2.62455 2.50877 -0.09715 -0.13770 -0.03505 166 THR A OG1 
1267 C CG2 . THR A 193 ? 1.57239 2.29207 2.19690 -0.11488 -0.10522 -0.03503 166 THR A CG2 
1268 N N   . PHE A 194 ? 1.77741 2.45409 2.36584 -0.15888 -0.15014 -0.05680 167 PHE A N   
1269 C CA  . PHE A 194 ? 1.67466 2.31079 2.23217 -0.17138 -0.14272 -0.05746 167 PHE A CA  
1270 C C   . PHE A 194 ? 1.55759 2.19608 2.13440 -0.19482 -0.14727 -0.06236 167 PHE A C   
1271 O O   . PHE A 194 ? 1.23506 1.85029 1.80086 -0.20559 -0.13469 -0.05884 167 PHE A O   
1272 C CB  . PHE A 194 ? 1.52226 2.12346 2.03370 -0.16345 -0.15202 -0.06074 167 PHE A CB  
1273 C CG  . PHE A 194 ? 1.20266 1.78365 1.68217 -0.14625 -0.13974 -0.05531 167 PHE A CG  
1274 C CD1 . PHE A 194 ? 1.36071 1.93917 1.84038 -0.14417 -0.11777 -0.04827 167 PHE A CD1 
1275 C CD2 . PHE A 194 ? 1.46543 2.02750 1.91241 -0.13341 -0.14884 -0.05783 167 PHE A CD2 
1276 C CE1 . PHE A 194 ? 1.62550 2.18145 2.07225 -0.13066 -0.10495 -0.04490 167 PHE A CE1 
1277 C CE2 . PHE A 194 ? 1.88437 2.42405 2.29977 -0.11977 -0.13586 -0.05380 167 PHE A CE2 
1278 C CZ  . PHE A 194 ? 1.87005 2.40597 2.28476 -0.11893 -0.11382 -0.04788 167 PHE A CZ  
1279 N N   . LYS A 195 ? 1.64499 2.31008 2.24861 -0.20342 -0.16444 -0.07016 168 LYS A N   
1280 C CA  . LYS A 195 ? 1.65049 2.31124 2.26770 -0.22738 -0.16780 -0.07666 168 LYS A CA  
1281 C C   . LYS A 195 ? 1.66525 2.33950 2.31355 -0.24101 -0.14970 -0.07132 168 LYS A C   
1282 O O   . LYS A 195 ? 1.61095 2.26332 2.25682 -0.25820 -0.14265 -0.07216 168 LYS A O   
1283 C CB  . LYS A 195 ? 1.63836 2.32650 2.27580 -0.23600 -0.19021 -0.08763 168 LYS A CB  
1284 C CG  . LYS A 195 ? 1.58708 2.26673 2.23570 -0.26295 -0.19288 -0.09664 168 LYS A CG  
1285 C CD  . LYS A 195 ? 1.62072 2.33621 2.29464 -0.27523 -0.21386 -0.10802 168 LYS A CD  
1286 C CE  . LYS A 195 ? 1.70663 2.41073 2.39131 -0.30506 -0.21307 -0.11810 168 LYS A CE  
1287 N NZ  . LYS A 195 ? 1.37043 2.11318 2.08052 -0.32137 -0.23343 -0.13039 168 LYS A NZ  
1288 N N   . ALA A 196 ? 1.64080 2.34905 2.31749 -0.23266 -0.14032 -0.06497 169 ALA A N   
1289 C CA  . ALA A 196 ? 1.68092 2.40803 2.39188 -0.24624 -0.12331 -0.06035 169 ALA A CA  
1290 C C   . ALA A 196 ? 1.81505 2.50502 2.50200 -0.25059 -0.10191 -0.05231 169 ALA A C   
1291 O O   . ALA A 196 ? 2.20130 2.89944 2.91154 -0.26422 -0.08674 -0.04825 169 ALA A O   
1292 C CB  . ALA A 196 ? 1.47035 2.24196 2.21514 -0.23263 -0.11625 -0.05422 169 ALA A CB  
1293 N N   . PHE A 197 ? 1.54665 2.19818 2.18795 -0.24022 -0.10040 -0.04938 170 PHE A N   
1294 C CA  . PHE A 197 ? 1.77653 2.39664 2.39220 -0.24322 -0.08203 -0.04039 170 PHE A CA  
1295 C C   . PHE A 197 ? 1.73157 2.31982 2.33056 -0.25716 -0.08475 -0.04135 170 PHE A C   
1296 O O   . PHE A 197 ? 1.93097 2.48851 2.49578 -0.25412 -0.07778 -0.03442 170 PHE A O   
1297 C CB  . PHE A 197 ? 1.85431 2.45464 2.43038 -0.22516 -0.07706 -0.03565 170 PHE A CB  
1298 C CG  . PHE A 197 ? 1.86062 2.48301 2.44825 -0.21102 -0.06628 -0.03226 170 PHE A CG  
1299 C CD1 . PHE A 197 ? 1.73786 2.38218 2.33690 -0.19625 -0.07793 -0.03662 170 PHE A CD1 
1300 C CD2 . PHE A 197 ? 2.00619 2.62636 2.59211 -0.21154 -0.04333 -0.02396 170 PHE A CD2 
1301 C CE1 . PHE A 197 ? 1.76066 2.42338 2.37071 -0.18069 -0.06574 -0.03214 170 PHE A CE1 
1302 C CE2 . PHE A 197 ? 1.78637 2.42361 2.38174 -0.19756 -0.03066 -0.02103 170 PHE A CE2 
1303 C CZ  . PHE A 197 ? 1.64765 2.30583 2.25601 -0.18136 -0.04132 -0.02482 170 PHE A CZ  
1304 N N   . ASN A 198 ? 2.61887 2.35468 1.96962 0.04446  0.20711  0.37570  171 ASN A N   
1305 C CA  . ASN A 198 ? 2.60195 2.32101 1.94000 0.01815  0.16924  0.40825  171 ASN A CA  
1306 C C   . ASN A 198 ? 2.96624 2.68421 2.20549 0.02303  0.19706  0.43799  171 ASN A C   
1307 O O   . ASN A 198 ? 3.05309 2.79915 2.27227 0.03712  0.25270  0.45128  171 ASN A O   
1308 C CB  . ASN A 198 ? 2.51217 2.26583 1.97197 -0.00880 0.16459  0.44646  171 ASN A CB  
1309 C CG  . ASN A 198 ? 2.58727 2.31829 2.04185 -0.03733 0.12634  0.47961  171 ASN A CG  
1310 O OD1 . ASN A 198 ? 2.71466 2.40201 2.08309 -0.03548 0.09049  0.46912  171 ASN A OD1 
1311 N ND2 . ASN A 198 ? 2.77862 2.54255 2.32734 -0.06363 0.13528  0.51766  171 ASN A ND2 
1312 N N   . SER A 199 ? 2.96962 2.65570 2.14458 0.01397  0.15862  0.44942  172 SER A N   
1313 C CA  . SER A 199 ? 3.07935 2.76153 2.14584 0.02624  0.18158  0.47640  172 SER A CA  
1314 C C   . SER A 199 ? 3.34797 3.04915 2.45151 0.01001  0.21957  0.54230  172 SER A C   
1315 O O   . SER A 199 ? 3.53822 3.25312 2.58558 0.02462  0.27101  0.56806  172 SER A O   
1316 C CB  . SER A 199 ? 3.03079 2.67701 2.00865 0.02861  0.12740  0.46232  172 SER A CB  
1317 O OG  . SER A 199 ? 2.97526 2.60357 2.01203 0.00108  0.08308  0.48598  172 SER A OG  
1318 N N   . ALA A 200 ? 3.24985 2.95151 2.44815 -0.02075 0.19809  0.56852  173 ALA A N   
1319 C CA  . ALA A 200 ? 3.30781 3.02308 2.54718 -0.04119 0.23617  0.62743  173 ALA A CA  
1320 C C   . ALA A 200 ? 3.40825 3.17455 2.72316 -0.04332 0.29847  0.63613  173 ALA A C   
1321 O O   . ALA A 200 ? 3.20113 2.99916 2.59836 -0.04354 0.29562  0.60548  173 ALA A O   
1322 C CB  . ALA A 200 ? 3.26322 2.96769 2.58903 -0.07597 0.19554  0.64628  173 ALA A CB  
1323 N N   . LYS A 201 ? 3.52797 3.30276 2.81192 -0.04243 0.35701  0.67866  174 LYS A N   
1324 C CA  . LYS A 201 ? 3.56777 3.39248 2.91639 -0.04632 0.42315  0.69152  174 LYS A CA  
1325 C C   . LYS A 201 ? 3.72977 3.57816 3.04660 -0.01464 0.44503  0.65233  174 LYS A C   
1326 O O   . LYS A 201 ? 3.79607 3.62558 3.06970 0.00482  0.40599  0.60840  174 LYS A O   
1327 C CB  . LYS A 201 ? 3.50215 3.37015 3.00529 -0.08045 0.42097  0.69388  174 LYS A CB  
1328 C CG  . LYS A 201 ? 3.23608 3.08511 2.78390 -0.11632 0.41023  0.73306  174 LYS A CG  
1329 C CD  . LYS A 201 ? 3.09145 2.99432 2.79625 -0.15001 0.40680  0.72706  174 LYS A CD  
1330 C CE  . LYS A 201 ? 2.88917 2.77229 2.64159 -0.18860 0.40075  0.76359  174 LYS A CE  
1331 N NZ  . LYS A 201 ? 2.74409 2.68839 2.65282 -0.22279 0.39608  0.75252  174 LYS A NZ  
1332 N N   . ASN A 202 ? 3.63103 3.51921 2.96943 -0.01015 0.51063  0.66673  175 ASN A N   
1333 C CA  . ASN A 202 ? 3.62766 3.53942 2.93696 0.02035  0.53819  0.63303  175 ASN A CA  
1334 C C   . ASN A 202 ? 3.76948 3.70736 3.16639 0.02370  0.50982  0.58926  175 ASN A C   
1335 O O   . ASN A 202 ? 3.79979 3.77700 3.31657 0.00211  0.50606  0.59443  175 ASN A O   
1336 C CB  . ASN A 202 ? 3.40864 3.36231 2.73705 0.02114  0.61509  0.65981  175 ASN A CB  
1337 C CG  . ASN A 202 ? 3.63130 3.55449 2.85352 0.02860  0.65187  0.70111  175 ASN A CG  
1338 O OD1 . ASN A 202 ? 3.81202 3.68871 2.92868 0.04301  0.62086  0.70341  175 ASN A OD1 
1339 N ND2 . ASN A 202 ? 3.27522 3.22742 2.52382 0.02101  0.72017  0.73324  175 ASN A ND2 
1340 N N   . SER A 203 ? 3.91588 3.83316 3.25216 0.05228  0.49254  0.54508  176 SER A N   
1341 C CA  . SER A 203 ? 3.90330 3.83362 3.30734 0.06253  0.46997  0.50340  176 SER A CA  
1342 C C   . SER A 203 ? 4.07175 3.98545 3.39479 0.09811  0.48707  0.46124  176 SER A C   
1343 O O   . SER A 203 ? 4.14839 4.06137 3.38867 0.11289  0.52536  0.46742  176 SER A O   
1344 C CB  . SER A 203 ? 3.73386 3.63038 3.16881 0.04589  0.40055  0.49044  176 SER A CB  
1345 O OG  . SER A 203 ? 3.77184 3.61106 3.09755 0.05012  0.36454  0.47822  176 SER A OG  
1346 N N   . ALA A 204 ? 3.86328 3.76211 3.21218 0.11191  0.46064  0.41782  177 ALA A N   
1347 C CA  . ALA A 204 ? 3.71587 3.59313 2.99556 0.14341  0.47860  0.37235  177 ALA A CA  
1348 C C   . ALA A 204 ? 3.79295 3.62060 2.94645 0.14794  0.45582  0.34977  177 ALA A C   
1349 O O   . ALA A 204 ? 3.79030 3.60508 2.87303 0.17164  0.47854  0.31259  177 ALA A O   
1350 C CB  . ALA A 204 ? 3.32628 3.19277 2.66769 0.15722  0.46024  0.33341  177 ALA A CB  
1351 N N   . ALA A 205 ? 3.84577 3.64969 2.97027 0.12706  0.41261  0.36897  178 ALA A N   
1352 C CA  . ALA A 205 ? 3.68737 3.45666 2.69105 0.13356  0.38923  0.34954  178 ALA A CA  
1353 C C   . ALA A 205 ? 4.07523 3.85983 2.99937 0.13866  0.42148  0.39032  178 ALA A C   
1354 O O   . ALA A 205 ? 3.98179 3.75017 2.79571 0.15169  0.40978  0.37479  178 ALA A O   
1355 C CB  . ALA A 205 ? 3.35490 3.08904 2.36268 0.11314  0.32142  0.34442  178 ALA A CB  
1356 N N   . ASN A 206 ? 4.65792 4.47587 3.63468 0.13004  0.46360  0.44030  179 ASN A N   
1357 C CA  . ASN A 206 ? 4.82131 4.64921 3.72826 0.13517  0.50177  0.48479  179 ASN A CA  
1358 C C   . ASN A 206 ? 4.95589 4.81991 3.85983 0.15251  0.57050  0.49072  179 ASN A C   
1359 O O   . ASN A 206 ? 5.27987 5.14436 4.08119 0.17500  0.59877  0.49006  179 ASN A O   
1360 C CB  . ASN A 206 ? 4.58000 4.40892 3.54410 0.10613  0.49845  0.54334  179 ASN A CB  
1361 C CG  . ASN A 206 ? 4.66976 4.50218 3.56590 0.11234  0.54607  0.59449  179 ASN A CG  
1362 O OD1 . ASN A 206 ? 4.51818 4.38164 3.44944 0.11132  0.60502  0.61935  179 ASN A OD1 
1363 N ND2 . ASN A 206 ? 4.85464 4.65632 3.65159 0.12103  0.52266  0.61062  179 ASN A ND2 
1364 N N   . LEU A 207 ? 4.43665 4.33605 3.44985 0.14439  0.59802  0.49561  180 LEU A N   
1365 C CA  . LEU A 207 ? 4.36158 4.30063 3.38375 0.15963  0.66365  0.50128  180 LEU A CA  
1366 C C   . LEU A 207 ? 4.46364 4.40685 3.48645 0.18487  0.67094  0.44686  180 LEU A C   
1367 O O   . LEU A 207 ? 4.44464 4.37179 3.51224 0.18452  0.63319  0.41250  180 LEU A O   
1368 C CB  . LEU A 207 ? 4.03781 4.02393 3.18126 0.13712  0.69536  0.53780  180 LEU A CB  
1369 C CG  . LEU A 207 ? 3.73748 3.72154 2.89270 0.10976  0.70693  0.59401  180 LEU A CG  
1370 C CD1 . LEU A 207 ? 3.54331 3.58358 2.82864 0.08593  0.74345  0.61706  180 LEU A CD1 
1371 C CD2 . LEU A 207 ? 3.34011 3.30723 2.37729 0.12574  0.74667  0.62165  180 LEU A CD2 
1372 N N   . ALA A 208 ? 4.54548 4.50740 3.51674 0.20788  0.72350  0.44029  181 ALA A N   
1373 C CA  . ALA A 208 ? 4.38501 4.35247 3.35753 0.23362  0.74413  0.39292  181 ALA A CA  
1374 C C   . ALA A 208 ? 4.37177 4.38789 3.46181 0.23516  0.77644  0.40094  181 ALA A C   
1375 O O   . ALA A 208 ? 4.44652 4.46106 3.58209 0.25007  0.77027  0.36584  181 ALA A O   
1376 C CB  . ALA A 208 ? 3.92194 3.89088 2.78542 0.25856  0.78664  0.38023  181 ALA A CB  
1377 N N   . SER A 209 ? 4.29037 4.35183 3.43066 0.22144  0.81339  0.44572  182 SER A N   
1378 C CA  . SER A 209 ? 4.02201 4.14391 3.27813 0.22262  0.84392  0.45130  182 SER A CA  
1379 C C   . SER A 209 ? 4.02296 4.15513 3.38538 0.20698  0.79805  0.44753  182 SER A C   
1380 O O   . SER A 209 ? 3.66363 3.82902 3.10184 0.22345  0.80359  0.42761  182 SER A O   
1381 C CB  . SER A 209 ? 3.86191 4.03162 3.14792 0.20678  0.89546  0.49611  182 SER A CB  
1382 O OG  . SER A 209 ? 4.01604 4.17270 3.31568 0.17333  0.87482  0.53392  182 SER A OG  
1383 N N   . ALA A 210 ? 4.11212 4.21764 3.47984 0.17802  0.75344  0.46739  183 ALA A N   
1384 C CA  . ALA A 210 ? 3.93291 4.04666 3.39768 0.16221  0.70658  0.46316  183 ALA A CA  
1385 C C   . ALA A 210 ? 4.00350 4.07464 3.45023 0.18383  0.66796  0.41722  183 ALA A C   
1386 O O   . ALA A 210 ? 3.75201 3.84459 3.28632 0.18948  0.64997  0.40403  183 ALA A O   
1387 C CB  . ALA A 210 ? 3.67940 3.76921 3.14665 0.12605  0.67013  0.49522  183 ALA A CB  
1388 N N   . ALA A 211 ? 4.26288 4.27577 3.59715 0.19698  0.65731  0.39073  184 ALA A N   
1389 C CA  . ALA A 211 ? 4.11555 4.08384 3.42955 0.21644  0.63044  0.34149  184 ALA A CA  
1390 C C   . ALA A 211 ? 4.21876 4.20999 3.56144 0.25091  0.67484  0.31617  184 ALA A C   
1391 O O   . ALA A 211 ? 4.20873 4.18163 3.58972 0.26734  0.66011  0.28696  184 ALA A O   
1392 C CB  . ALA A 211 ? 4.11654 4.02623 3.30466 0.21949  0.61192  0.31379  184 ALA A CB  
1393 N N   . ALA A 212 ? 4.07258 4.10173 3.39606 0.26422  0.73158  0.32816  185 ALA A N   
1394 C CA  . ALA A 212 ? 3.74024 3.79642 3.09301 0.29883  0.77764  0.30804  185 ALA A CA  
1395 C C   . ALA A 212 ? 3.60990 3.72680 3.09103 0.30458  0.77967  0.32242  185 ALA A C   
1396 O O   . ALA A 212 ? 3.51068 3.64274 3.02474 0.33884  0.80549  0.30210  185 ALA A O   
1397 C CB  . ALA A 212 ? 3.26301 3.34977 2.56612 0.30961  0.83713  0.31986  185 ALA A CB  
1398 N N   . ALA A 213 ? 3.56548 3.72021 3.11935 0.27372  0.75488  0.35582  186 ALA A N   
1399 C CA  . ALA A 213 ? 3.27725 3.50169 2.95742 0.27651  0.75214  0.36675  186 ALA A CA  
1400 C C   . ALA A 213 ? 3.18557 3.38082 2.90994 0.27615  0.69620  0.35166  186 ALA A C   
1401 O O   . ALA A 213 ? 3.07383 3.32382 2.90002 0.26512  0.67656  0.36668  186 ALA A O   
1402 C CB  . ALA A 213 ? 3.00221 3.29153 2.74681 0.24106  0.76222  0.40653  186 ALA A CB  
1403 N N   . LEU A 214 ? 3.19284 3.30576 2.84474 0.28709  0.67138  0.31979  187 LEU A N   
1404 C CA  . LEU A 214 ? 3.06270 3.13888 2.74929 0.28747  0.62083  0.30322  187 LEU A CA  
1405 C C   . LEU A 214 ? 3.15954 3.24448 2.88812 0.33371  0.64357  0.28006  187 LEU A C   
1406 O O   . LEU A 214 ? 3.21350 3.25315 2.87688 0.36230  0.67484  0.25029  187 LEU A O   
1407 C CB  . LEU A 214 ? 2.80820 2.79230 2.39823 0.27383  0.58413  0.27748  187 LEU A CB  
1408 C CG  . LEU A 214 ? 2.87090 2.83355 2.45978 0.23226  0.52658  0.29572  187 LEU A CG  
1409 C CD1 . LEU A 214 ? 2.85522 2.85881 2.43972 0.20403  0.54056  0.33771  187 LEU A CD1 
1410 C CD2 . LEU A 214 ? 2.73478 2.61314 2.22643 0.22616  0.49329  0.26164  187 LEU A CD2 
1411 N N   . PRO A 215 ? 3.20162 3.34456 3.03561 0.34485  0.63195  0.29186  188 PRO A N   
1412 C CA  . PRO A 215 ? 3.21356 3.36014 3.08194 0.39574  0.65312  0.27248  188 PRO A CA  
1413 C C   . PRO A 215 ? 3.34606 3.39210 3.16601 0.40670  0.62706  0.23911  188 PRO A C   
1414 O O   . PRO A 215 ? 3.34344 3.38227 3.21760 0.41126  0.59107  0.23808  188 PRO A O   
1415 C CB  . PRO A 215 ? 2.98471 3.22598 2.97728 0.39958  0.63692  0.29537  188 PRO A CB  
1416 C CG  . PRO A 215 ? 2.78796 3.09009 2.81291 0.35277  0.63015  0.32522  188 PRO A CG  
1417 C CD  . PRO A 215 ? 3.09527 3.31301 3.02385 0.31472  0.60678  0.32369  188 PRO A CD  
1418 N N   . VAL A 216 ? 3.36090 3.33115 3.07995 0.40997  0.64649  0.20922  189 VAL A N   
1419 C CA  . VAL A 216 ? 2.99282 2.86539 2.66153 0.41800  0.63039  0.16941  189 VAL A CA  
1420 C C   . VAL A 216 ? 2.98325 2.84740 2.69025 0.47209  0.66586  0.15542  189 VAL A C   
1421 O O   . VAL A 216 ? 2.98249 2.83133 2.65178 0.50552  0.72164  0.13749  189 VAL A O   
1422 C CB  . VAL A 216 ? 2.80457 2.61125 2.35773 0.40614  0.64637  0.13587  189 VAL A CB  
1423 C CG1 . VAL A 216 ? 2.82489 2.53459 2.33244 0.41016  0.63202  0.08793  189 VAL A CG1 
1424 C CG2 . VAL A 216 ? 2.81114 2.63229 2.32278 0.36036  0.61479  0.15556  189 VAL A CG2 
1425 N N   . SER A 217 ? 2.87563 2.74933 2.65608 0.48349  0.63579  0.16462  190 SER A N   
1426 C CA  . SER A 217 ? 2.84125 2.71841 2.66683 0.54075  0.66852  0.16043  190 SER A CA  
1427 C C   . SER A 217 ? 2.69949 2.47828 2.50716 0.54952  0.64895  0.13084  190 SER A C   
1428 O O   . SER A 217 ? 2.64329 2.37610 2.43382 0.50892  0.59634  0.12104  190 SER A O   
1429 C CB  . SER A 217 ? 2.98724 2.97691 2.92369 0.55788  0.65798  0.19813  190 SER A CB  
1430 O OG  . SER A 217 ? 3.61655 3.69980 3.57614 0.54750  0.67990  0.22215  190 SER A OG  
1431 N N   . THR A 218 ? 1.70160 2.83629 2.93699 -0.29574 -0.21857 -0.20740 191 THR A N   
1432 C CA  . THR A 218 ? 1.64897 2.72532 2.79544 -0.25493 -0.25399 -0.20107 191 THR A CA  
1433 C C   . THR A 218 ? 1.64510 2.81134 2.83612 -0.22979 -0.31171 -0.20905 191 THR A C   
1434 O O   . THR A 218 ? 1.84250 3.11012 3.12788 -0.21367 -0.31382 -0.20895 191 THR A O   
1435 C CB  . THR A 218 ? 1.67810 2.69230 2.76450 -0.20593 -0.22382 -0.17465 191 THR A CB  
1436 O OG1 . THR A 218 ? 1.63067 2.59887 2.63999 -0.16872 -0.25997 -0.16869 191 THR A OG1 
1437 C CG2 . THR A 218 ? 1.48782 2.58083 2.64906 -0.17431 -0.20194 -0.16450 191 THR A CG2 
1438 N N   . ALA A 219 ? 1.60014 2.73052 2.72297 -0.22618 -0.35838 -0.21596 192 ALA A N   
1439 C CA  . ALA A 219 ? 1.69830 2.90330 2.84741 -0.20205 -0.41983 -0.21978 192 ALA A CA  
1440 C C   . ALA A 219 ? 1.64241 2.81853 2.73981 -0.13700 -0.43614 -0.19427 192 ALA A C   
1441 O O   . ALA A 219 ? 1.93707 3.18563 3.07882 -0.10339 -0.47837 -0.18934 192 ALA A O   
1442 C CB  . ALA A 219 ? 1.83565 3.02458 2.93630 -0.23875 -0.46592 -0.24254 192 ALA A CB  
1443 N N   . TYR A 220 ? 1.54389 2.61645 2.55182 -0.11863 -0.40507 -0.17795 193 TYR A N   
1444 C CA  . TYR A 220 ? 1.56228 2.59378 2.51227 -0.06335 -0.41820 -0.15481 193 TYR A CA  
1445 C C   . TYR A 220 ? 1.65581 2.61835 2.57031 -0.04429 -0.36290 -0.13911 193 TYR A C   
1446 O O   . TYR A 220 ? 1.69122 2.59589 2.57192 -0.07436 -0.32533 -0.14307 193 TYR A O   
1447 C CB  . TYR A 220 ? 1.63887 2.60523 2.48408 -0.06506 -0.45675 -0.15372 193 TYR A CB  
1448 C CG  . TYR A 220 ? 1.67059 2.69347 2.53202 -0.09482 -0.50973 -0.17348 193 TYR A CG  
1449 C CD1 . TYR A 220 ? 1.71751 2.82182 2.62584 -0.06810 -0.56346 -0.16804 193 TYR A CD1 
1450 C CD2 . TYR A 220 ? 1.73630 2.73120 2.56699 -0.14882 -0.50757 -0.19893 193 TYR A CD2 
1451 C CE1 . TYR A 220 ? 1.66174 2.82321 2.58307 -0.09634 -0.61623 -0.18672 193 TYR A CE1 
1452 C CE2 . TYR A 220 ? 1.60037 2.64723 2.44200 -0.17921 -0.55696 -0.22098 193 TYR A CE2 
1453 C CZ  . TYR A 220 ? 1.53955 2.67254 2.42560 -0.15388 -0.61237 -0.21448 193 TYR A CZ  
1454 O OH  . TYR A 220 ? 1.68776 2.87745 2.58240 -0.18490 -0.66591 -0.23684 193 TYR A OH  
1455 N N   . HIS A 221 ? 1.54176 2.50940 2.46368 0.00660  -0.36010 -0.12192 194 HIS A N   
1456 C CA  . HIS A 221 ? 1.55954 2.46488 2.44340 0.02841  -0.31325 -0.10835 194 HIS A CA  
1457 C C   . HIS A 221 ? 1.57361 2.44760 2.41736 0.08184  -0.33351 -0.09092 194 HIS A C   
1458 O O   . HIS A 221 ? 1.68167 2.56393 2.50849 0.09773  -0.38270 -0.08588 194 HIS A O   
1459 C CB  . HIS A 221 ? 1.54800 2.50924 2.51386 0.02378  -0.26723 -0.11219 194 HIS A CB  
1460 C CG  . HIS A 221 ? 1.54603 2.62389 2.62449 0.03617  -0.28464 -0.12088 194 HIS A CG  
1461 N ND1 . HIS A 221 ? 1.78679 2.90331 2.90546 0.08961  -0.29163 -0.11415 194 HIS A ND1 
1462 C CD2 . HIS A 221 ? 1.50337 2.67055 2.66812 0.00221  -0.29624 -0.13760 194 HIS A CD2 
1463 C CE1 . HIS A 221 ? 1.75209 2.98171 2.98065 0.09129  -0.30707 -0.12599 194 HIS A CE1 
1464 N NE2 . HIS A 221 ? 1.60010 2.86551 2.85939 0.03673  -0.31051 -0.14034 194 HIS A NE2 
1465 N N   . ILE A 222 ? 1.65637 2.48998 2.48041 0.10838  -0.29615 -0.08118 195 ILE A N   
1466 C CA  . ILE A 222 ? 1.68182 2.46931 2.46026 0.15518  -0.31088 -0.06571 195 ILE A CA  
1467 C C   . ILE A 222 ? 1.68007 2.54029 2.53409 0.19646  -0.34213 -0.06340 195 ILE A C   
1468 O O   . ILE A 222 ? 1.56498 2.39276 2.38458 0.23292  -0.37416 -0.04896 195 ILE A O   
1469 C CB  . ILE A 222 ? 1.55260 2.28119 2.29335 0.17000  -0.26319 -0.06037 195 ILE A CB  
1470 C CG1 . ILE A 222 ? 1.42804 2.08436 2.09920 0.20602  -0.27830 -0.04567 195 ILE A CG1 
1471 C CG2 . ILE A 222 ? 1.56453 2.35675 2.38742 0.18676  -0.22874 -0.06773 195 ILE A CG2 
1472 C CD1 . ILE A 222 ? 1.45414 2.05248 2.08488 0.21849  -0.23592 -0.04348 195 ILE A CD1 
1473 N N   . LYS A 223 ? 1.64168 2.60083 2.60126 0.19182  -0.33361 -0.07675 196 LYS A N   
1474 C CA  . LYS A 223 ? 1.69439 2.73695 2.74121 0.23258  -0.36441 -0.07736 196 LYS A CA  
1475 C C   . LYS A 223 ? 1.60659 2.70248 2.67617 0.22228  -0.42660 -0.07837 196 LYS A C   
1476 O O   . LYS A 223 ? 1.84852 3.00375 2.97671 0.26219  -0.46554 -0.07387 196 LYS A O   
1477 C CB  . LYS A 223 ? 1.60327 2.73955 2.76114 0.23293  -0.32464 -0.09348 196 LYS A CB  
1478 C CG  . LYS A 223 ? 1.62108 2.71438 2.75824 0.24773  -0.26487 -0.09366 196 LYS A CG  
1479 C CD  . LYS A 223 ? 1.41351 2.60350 2.65558 0.24290  -0.22214 -0.11019 196 LYS A CD  
1480 C CE  . LYS A 223 ? 1.36897 2.59299 2.63448 0.17860  -0.20064 -0.11884 196 LYS A CE  
1481 N NZ  . LYS A 223 ? 1.26094 2.38382 2.42570 0.14530  -0.16890 -0.11029 196 LYS A NZ  
1482 N N   . ASN A 224 ? 1.61486 2.69093 2.63915 0.17141  -0.43814 -0.08524 197 ASN A N   
1483 C CA  . ASN A 224 ? 1.66955 2.79117 2.70126 0.15555  -0.49830 -0.08935 197 ASN A CA  
1484 C C   . ASN A 224 ? 1.65782 2.69684 2.58020 0.11375  -0.50516 -0.09101 197 ASN A C   
1485 O O   . ASN A 224 ? 1.54237 2.59959 2.47380 0.06273  -0.50047 -0.11062 197 ASN A O   
1486 C CB  . ASN A 224 ? 1.67878 2.92281 2.83054 0.12738  -0.50286 -0.11172 197 ASN A CB  
1487 C CG  . ASN A 224 ? 1.73263 3.03423 2.89788 0.11101  -0.56963 -0.11883 197 ASN A CG  
1488 O OD1 . ASN A 224 ? 1.90952 3.22107 3.06671 0.05602  -0.57502 -0.13764 197 ASN A OD1 
1489 N ND2 . ASN A 224 ? 1.77614 3.11236 2.95882 0.15923  -0.62247 -0.10396 197 ASN A ND2 
1490 N N   . PRO A 225 ? 1.67226 2.61766 2.49029 0.13308  -0.51407 -0.07230 198 PRO A N   
1491 C CA  . PRO A 225 ? 1.56660 2.43680 2.28074 0.09591  -0.51773 -0.07578 198 PRO A CA  
1492 C C   . PRO A 225 ? 1.87195 2.77396 2.56384 0.08020  -0.57877 -0.08003 198 PRO A C   
1493 O O   . PRO A 225 ? 1.82419 2.79182 2.56361 0.10724  -0.62599 -0.07211 198 PRO A O   
1494 C CB  . PRO A 225 ? 1.29753 2.06823 1.91892 0.12511  -0.50461 -0.05329 198 PRO A CB  
1495 C CG  . PRO A 225 ? 1.31296 2.11023 1.97463 0.18045  -0.52873 -0.03431 198 PRO A CG  
1496 C CD  . PRO A 225 ? 1.53623 2.43788 2.32717 0.18873  -0.51845 -0.04846 198 PRO A CD  
1497 N N   . ILE A 226 ? 1.90682 2.76175 2.52413 0.03689  -0.57793 -0.09386 199 ILE A N   
1498 C CA  . ILE A 226 ? 1.84729 2.72219 2.42414 0.01388  -0.63171 -0.10265 199 ILE A CA  
1499 C C   . ILE A 226 ? 1.73879 2.51596 2.18147 0.01294  -0.63636 -0.08986 199 ILE A C   
1500 O O   . ILE A 226 ? 1.67467 2.38082 2.06061 -0.00869 -0.59363 -0.09828 199 ILE A O   
1501 C CB  . ILE A 226 ? 1.65732 2.57283 2.27051 -0.04321 -0.62758 -0.13836 199 ILE A CB  
1502 C CG1 . ILE A 226 ? 1.43985 2.36767 1.99524 -0.06979 -0.68272 -0.15136 199 ILE A CG1 
1503 C CG2 . ILE A 226 ? 1.56211 2.40574 2.14335 -0.07418 -0.56690 -0.15238 199 ILE A CG2 
1504 C CD1 . ILE A 226 ? 1.58051 2.57301 2.19551 -0.12160 -0.69321 -0.18820 199 ILE A CD1 
1505 N N   . GLY A 227 ? 1.74224 2.51711 2.13565 0.03718  -0.68771 -0.06820 200 GLY A N   
1506 C CA  . GLY A 227 ? 1.75204 2.43751 2.01612 0.03647  -0.69284 -0.05194 200 GLY A CA  
1507 C C   . GLY A 227 ? 1.74818 2.34984 1.97267 0.05536  -0.64185 -0.03583 200 GLY A C   
1508 O O   . GLY A 227 ? 1.91799 2.44377 2.04486 0.03891  -0.62353 -0.03389 200 GLY A O   
1509 N N   . GLY A 228 ? 1.60849 2.22726 1.90945 0.08863  -0.61794 -0.02658 201 GLY A N   
1510 C CA  . GLY A 228 ? 1.93206 2.47901 2.20427 0.10369  -0.56889 -0.01601 201 GLY A CA  
1511 C C   . GLY A 228 ? 1.91950 2.43897 2.18618 0.06866  -0.51600 -0.03919 201 GLY A C   
1512 O O   . GLY A 228 ? 1.71886 2.16637 1.92375 0.06727  -0.48345 -0.03369 201 GLY A O   
1513 N N   . VAL A 229 ? 1.80183 2.37647 2.13342 0.03993  -0.50754 -0.06446 202 VAL A N   
1514 C CA  . VAL A 229 ? 1.68485 2.23111 2.01335 0.00647  -0.46139 -0.08540 202 VAL A CA  
1515 C C   . VAL A 229 ? 1.67293 2.28316 2.10688 -0.00131 -0.44089 -0.09784 202 VAL A C   
1516 O O   . VAL A 229 ? 1.74654 2.43459 2.24917 -0.00563 -0.47010 -0.10543 202 VAL A O   
1517 C CB  . VAL A 229 ? 1.75092 2.27621 2.01937 -0.03613 -0.47246 -0.10823 202 VAL A CB  
1518 C CG1 . VAL A 229 ? 1.69767 2.20358 1.98504 -0.06858 -0.42922 -0.13202 202 VAL A CG1 
1519 C CG2 . VAL A 229 ? 1.80656 2.26203 1.96364 -0.03312 -0.47867 -0.09711 202 VAL A CG2 
1520 N N   . PHE A 230 ? 1.55966 2.14001 2.00630 -0.00445 -0.39098 -0.09923 203 PHE A N   
1521 C CA  . PHE A 230 ? 1.66819 2.30001 2.20314 -0.01831 -0.36504 -0.10934 203 PHE A CA  
1522 C C   . PHE A 230 ? 1.62311 2.19903 2.13652 -0.03841 -0.31596 -0.11449 203 PHE A C   
1523 O O   . PHE A 230 ? 1.54811 2.05356 1.98987 -0.03270 -0.30012 -0.10891 203 PHE A O   
1524 C CB  . PHE A 230 ? 1.62213 2.30713 2.22857 0.01943  -0.35990 -0.09567 203 PHE A CB  
1525 C CG  . PHE A 230 ? 1.65603 2.28608 2.22377 0.05480  -0.33380 -0.07758 203 PHE A CG  
1526 C CD1 . PHE A 230 ? 1.66004 2.25336 2.17407 0.08673  -0.35860 -0.06113 203 PHE A CD1 
1527 C CD2 . PHE A 230 ? 1.65281 2.26680 2.23594 0.05439  -0.28540 -0.07667 203 PHE A CD2 
1528 C CE1 . PHE A 230 ? 1.67936 2.22016 2.15955 0.11527  -0.33455 -0.04754 203 PHE A CE1 
1529 C CE2 . PHE A 230 ? 1.62989 2.19639 2.17661 0.08424  -0.26353 -0.06360 203 PHE A CE2 
1530 C CZ  . PHE A 230 ? 1.61257 2.14260 2.11029 0.11377  -0.28771 -0.05072 203 PHE A CZ  
1531 N N   . PHE A 231 ? 1.54751 2.15735 2.12561 -0.06334 -0.29301 -0.12465 204 PHE A N   
1532 C CA  . PHE A 231 ? 1.55306 2.11318 2.11877 -0.08304 -0.24897 -0.12664 204 PHE A CA  
1533 C C   . PHE A 231 ? 1.48626 2.06496 2.09531 -0.06461 -0.21272 -0.11143 204 PHE A C   
1534 O O   . PHE A 231 ? 1.38103 2.03237 2.06546 -0.06155 -0.21304 -0.11156 204 PHE A O   
1535 C CB  . PHE A 231 ? 1.47342 2.04288 2.06964 -0.13070 -0.24632 -0.14814 204 PHE A CB  
1536 C CG  . PHE A 231 ? 1.43852 1.97224 1.97840 -0.15358 -0.27152 -0.16844 204 PHE A CG  
1537 C CD1 . PHE A 231 ? 1.57858 2.03192 2.04419 -0.15378 -0.25491 -0.17115 204 PHE A CD1 
1538 C CD2 . PHE A 231 ? 1.46271 2.04756 2.02534 -0.17561 -0.31131 -0.18723 204 PHE A CD2 
1539 C CE1 . PHE A 231 ? 1.69350 2.11574 2.10616 -0.17490 -0.27350 -0.19353 204 PHE A CE1 
1540 C CE2 . PHE A 231 ? 1.38020 1.93162 1.88365 -0.19856 -0.33303 -0.20904 204 PHE A CE2 
1541 C CZ  . PHE A 231 ? 1.43902 1.90777 1.86637 -0.19810 -0.31191 -0.21293 204 PHE A CZ  
1542 N N   . THR A 232 ? 1.41961 1.93740 1.98164 -0.05282 -0.18164 -0.09999 205 THR A N   
1543 C CA  . THR A 232 ? 1.43803 1.96266 2.02704 -0.04402 -0.14248 -0.08763 205 THR A CA  
1544 C C   . THR A 232 ? 1.55059 2.03756 2.13522 -0.07677 -0.11225 -0.08844 205 THR A C   
1545 O O   . THR A 232 ? 1.61528 2.05247 2.16163 -0.09587 -0.11793 -0.09756 205 THR A O   
1546 C CB  . THR A 232 ? 1.45089 1.93619 1.99021 -0.00722 -0.13086 -0.07339 205 THR A CB  
1547 O OG1 . THR A 232 ? 1.51971 1.93529 1.98549 -0.00907 -0.13474 -0.07377 205 THR A OG1 
1548 C CG2 . THR A 232 ? 1.44051 1.96032 1.99371 0.02711  -0.15618 -0.07021 205 THR A CG2 
1549 N N   . ASP A 233 ? 1.49594 2.00486 2.11891 -0.08283 -0.07885 -0.07873 206 ASP A N   
1550 C CA  . ASP A 233 ? 1.45991 1.93683 2.08716 -0.11701 -0.05122 -0.07576 206 ASP A CA  
1551 C C   . ASP A 233 ? 1.68904 2.13923 2.29407 -0.10480 -0.01266 -0.05428 206 ASP A C   
1552 O O   . ASP A 233 ? 1.72410 2.19900 2.32809 -0.07532 -0.00357 -0.04622 206 ASP A O   
1553 C CB  . ASP A 233 ? 1.61175 2.14958 2.31633 -0.15401 -0.04958 -0.08636 206 ASP A CB  
1554 C CG  . ASP A 233 ? 1.83586 2.40680 2.56207 -0.16821 -0.09193 -0.10927 206 ASP A CG  
1555 O OD1 . ASP A 233 ? 1.96284 2.48006 2.63633 -0.17333 -0.11114 -0.11976 206 ASP A OD1 
1556 O OD2 . ASP A 233 ? 1.63106 2.28532 2.42661 -0.17341 -0.10655 -0.11777 206 ASP A OD2 
1557 N N   . SER A 234 ? 1.72485 2.12037 2.30876 -0.12750 0.00886  -0.04551 207 SER A N   
1558 C CA  . SER A 234 ? 1.56562 1.92935 2.12033 -0.12030 0.04297  -0.02213 207 SER A CA  
1559 C C   . SER A 234 ? 1.59415 1.91991 2.15745 -0.15828 0.06471  -0.01298 207 SER A C   
1560 O O   . SER A 234 ? 1.88199 2.17666 2.44971 -0.18160 0.05060  -0.02673 207 SER A O   
1561 C CB  . SER A 234 ? 1.46589 1.77148 1.94962 -0.08933 0.03735  -0.01477 207 SER A CB  
1562 O OG  . SER A 234 ? 1.51691 1.81138 1.97217 -0.07403 0.06353  0.00590  207 SER A OG  
1563 N N   . PRO A 235 ? 1.56459 1.88664 2.12575 -0.16646 0.09985  0.01000  208 PRO A N   
1564 C CA  . PRO A 235 ? 1.85387 2.20456 2.40004 -0.14244 0.12228  0.02529  208 PRO A CA  
1565 C C   . PRO A 235 ? 2.08892 2.53110 2.70200 -0.14844 0.13571  0.01702  208 PRO A C   
1566 O O   . PRO A 235 ? 2.11567 2.60906 2.79017 -0.16471 0.11936  -0.00191 208 PRO A O   
1567 C CB  . PRO A 235 ? 1.82864 2.12161 2.33461 -0.15672 0.15281  0.05448  208 PRO A CB  
1568 C CG  . PRO A 235 ? 1.60383 1.87846 2.14695 -0.20203 0.15897  0.05335  208 PRO A CG  
1569 C CD  . PRO A 235 ? 1.45300 1.72989 2.01891 -0.20482 0.12194  0.02342  208 PRO A CD  
1570 N N   . GLU A 236 ? 2.10689 2.57434 2.70998 -0.13501 0.16583  0.02949  209 GLU A N   
1571 C CA  . GLU A 236 ? 1.96592 2.52545 2.63541 -0.13388 0.18190  0.01848  209 GLU A CA  
1572 C C   . GLU A 236 ? 1.85774 2.45607 2.58805 -0.18184 0.20885  0.02176  209 GLU A C   
1573 O O   . GLU A 236 ? 1.99876 2.68110 2.81055 -0.19171 0.20631  0.00370  209 GLU A O   
1574 C CB  . GLU A 236 ? 2.01412 2.58584 2.64893 -0.10461 0.20892  0.02626  209 GLU A CB  
1575 C CG  . GLU A 236 ? 2.06395 2.73152 2.76779 -0.09425 0.22701  0.01040  209 GLU A CG  
1576 C CD  . GLU A 236 ? 2.44610 3.11897 3.10891 -0.06297 0.25322  0.01217  209 GLU A CD  
1577 O OE1 . GLU A 236 ? 2.77408 3.37908 3.35351 -0.05453 0.25766  0.02811  209 GLU A OE1 
1578 O OE2 . GLU A 236 ? 2.41943 3.16612 3.13494 -0.04605 0.26861  -0.00440 209 GLU A OE2 
1579 N N   . HIS A 237 ? 1.78113 2.31998 2.47557 -0.21265 0.23394  0.04532  210 HIS A N   
1580 C CA  . HIS A 237 ? 1.95493 2.52109 2.70129 -0.26383 0.26422  0.05157  210 HIS A CA  
1581 C C   . HIS A 237 ? 1.89917 2.46436 2.69662 -0.29887 0.23825  0.03378  210 HIS A C   
1582 O O   . HIS A 237 ? 1.54981 2.12727 2.39013 -0.34797 0.26092  0.03754  210 HIS A O   
1583 C CB  . HIS A 237 ? 2.13945 2.63246 2.82216 -0.28518 0.30036  0.08740  210 HIS A CB  
1584 C CG  . HIS A 237 ? 2.17240 2.55621 2.78954 -0.28264 0.27938  0.10179  210 HIS A CG  
1585 N ND1 . HIS A 237 ? 2.14869 2.47971 2.77971 -0.32158 0.27506  0.10403  210 HIS A ND1 
1586 C CD2 . HIS A 237 ? 2.13914 2.45884 2.68100 -0.24526 0.26230  0.11253  210 HIS A CD2 
1587 C CE1 . HIS A 237 ? 2.23336 2.47152 2.80136 -0.30456 0.25702  0.11536  210 HIS A CE1 
1588 N NE2 . HIS A 237 ? 2.15956 2.39352 2.67511 -0.25869 0.24859  0.12118  210 HIS A NE2 
1589 N N   . LEU A 238 ? 2.00622 2.55728 2.79774 -0.27792 0.19270  0.01354  211 LEU A N   
1590 C CA  . LEU A 238 ? 1.89463 2.44968 2.72920 -0.30937 0.16425  -0.00878 211 LEU A CA  
1591 C C   . LEU A 238 ? 1.89633 2.53463 2.78541 -0.29031 0.12599  -0.03748 211 LEU A C   
1592 O O   . LEU A 238 ? 1.79439 2.43666 2.70724 -0.30998 0.09359  -0.05886 211 LEU A O   
1593 C CB  . LEU A 238 ? 1.85820 2.30763 2.62727 -0.30878 0.14391  -0.00736 211 LEU A CB  
1594 C CG  . LEU A 238 ? 1.91054 2.26508 2.62736 -0.32687 0.17311  0.02126  211 LEU A CG  
1595 C CD1 . LEU A 238 ? 1.76077 2.02581 2.43994 -0.33135 0.14969  0.01209  211 LEU A CD1 
1596 C CD2 . LEU A 238 ? 1.47651 1.84965 2.23890 -0.37850 0.21037  0.03342  211 LEU A CD2 
1597 N N   . LEU A 239 ? 1.84617 2.54803 2.75298 -0.25191 0.12784  -0.03872 212 LEU A N   
1598 C CA  . LEU A 239 ? 1.79815 2.57399 2.75358 -0.22661 0.08943  -0.06114 212 LEU A CA  
1599 C C   . LEU A 239 ? 1.87684 2.76386 2.94080 -0.25267 0.09236  -0.07725 212 LEU A C   
1600 O O   . LEU A 239 ? 1.85275 2.79734 2.96485 -0.24675 0.05130  -0.09765 212 LEU A O   
1601 C CB  . LEU A 239 ? 1.72541 2.51274 2.65320 -0.17007 0.08885  -0.05636 212 LEU A CB  
1602 C CG  . LEU A 239 ? 1.90874 2.60212 2.73694 -0.13959 0.08207  -0.04371 212 LEU A CG  
1603 C CD1 . LEU A 239 ? 2.09096 2.80227 2.90197 -0.09293 0.09194  -0.04027 212 LEU A CD1 
1604 C CD2 . LEU A 239 ? 1.96337 2.61893 2.76123 -0.13324 0.03556  -0.05565 212 LEU A CD2 
1605 N N   . GLY A 240 ? 1.67100 2.59317 2.77462 -0.28188 0.13940  -0.06811 213 GLY A N   
1606 C CA  . GLY A 240 ? 1.49370 2.53741 2.70965 -0.30156 0.14693  -0.08470 213 GLY A CA  
1607 C C   . GLY A 240 ? 1.79103 2.91355 3.04461 -0.24769 0.14499  -0.09202 213 GLY A C   
1608 O O   . GLY A 240 ? 1.99436 3.08566 3.19491 -0.21194 0.16907  -0.07902 213 GLY A O   
1609 N N   . TYR A 241 ? 1.71070 2.93549 3.05696 -0.24028 0.11380  -0.11432 214 TYR A N   
1610 C CA  . TYR A 241 ? 1.65426 2.95647 3.04817 -0.18538 0.10704  -0.12345 214 TYR A CA  
1611 C C   . TYR A 241 ? 1.45669 2.75784 2.84147 -0.14248 0.04290  -0.13269 214 TYR A C   
1612 O O   . TYR A 241 ? 1.39408 2.72943 2.79606 -0.08841 0.03351  -0.13591 214 TYR A O   
1613 C CB  . TYR A 241 ? 1.92884 3.37021 3.45407 -0.20319 0.12864  -0.14018 214 TYR A CB  
1614 C CG  . TYR A 241 ? 2.03896 3.49323 3.57873 -0.24768 0.19709  -0.13047 214 TYR A CG  
1615 C CD1 . TYR A 241 ? 2.06117 3.51039 3.57069 -0.22253 0.24785  -0.12030 214 TYR A CD1 
1616 C CD2 . TYR A 241 ? 2.02559 3.49444 3.60533 -0.31727 0.21167  -0.13172 214 TYR A CD2 
1617 C CE1 . TYR A 241 ? 1.98340 3.44295 3.49686 -0.26505 0.31156  -0.10880 214 TYR A CE1 
1618 C CE2 . TYR A 241 ? 2.10211 3.57706 3.68975 -0.36110 0.27582  -0.11891 214 TYR A CE2 
1619 C CZ  . TYR A 241 ? 2.01309 3.48435 3.56522 -0.33451 0.32574  -0.10610 214 TYR A CZ  
1620 O OH  . TYR A 241 ? 1.85719 3.33300 3.40800 -0.37984 0.39068  -0.09084 214 TYR A OH  
1621 N N   . SER A 242 ? 1.53706 2.79572 2.89115 -0.16497 -0.00006 -0.13697 215 SER A N   
1622 C CA  . SER A 242 ? 1.38774 2.65004 2.73094 -0.13145 -0.06236 -0.14457 215 SER A CA  
1623 C C   . SER A 242 ? 1.29031 2.43288 2.51203 -0.10642 -0.07910 -0.13112 215 SER A C   
1624 O O   . SER A 242 ? 1.34825 2.48156 2.54446 -0.05794 -0.10876 -0.12793 215 SER A O   
1625 C CB  . SER A 242 ? 1.51711 2.82547 2.90933 -0.17392 -0.10336 -0.16304 215 SER A CB  
1626 O OG  . SER A 242 ? 1.38294 2.60880 2.71794 -0.22433 -0.09303 -0.16235 215 SER A OG  
1627 N N   . ARG A 243 ? 1.27406 2.32494 2.42318 -0.13824 -0.06036 -0.12296 216 ARG A N   
1628 C CA  . ARG A 243 ? 1.46867 2.41449 2.51110 -0.11934 -0.07652 -0.11355 216 ARG A CA  
1629 C C   . ARG A 243 ? 1.50679 2.41546 2.50007 -0.07209 -0.05521 -0.09837 216 ARG A C   
1630 O O   . ARG A 243 ? 1.46593 2.40732 2.48882 -0.06258 -0.01629 -0.09337 216 ARG A O   
1631 C CB  . ARG A 243 ? 1.57281 2.43521 2.56086 -0.16184 -0.05837 -0.10984 216 ARG A CB  
1632 C CG  . ARG A 243 ? 1.69397 2.57924 2.72305 -0.21273 -0.07774 -0.12864 216 ARG A CG  
1633 C CD  . ARG A 243 ? 1.62745 2.41809 2.60085 -0.24993 -0.05839 -0.12570 216 ARG A CD  
1634 N NE  . ARG A 243 ? 1.92203 2.72442 2.92803 -0.29899 -0.07884 -0.14832 216 ARG A NE  
1635 C CZ  . ARG A 243 ? 1.82124 2.54383 2.78887 -0.33469 -0.06918 -0.15312 216 ARG A CZ  
1636 N NH1 . ARG A 243 ? 1.70784 2.33576 2.60593 -0.32484 -0.04151 -0.13459 216 ARG A NH1 
1637 N NH2 . ARG A 243 ? 1.63360 2.37176 2.63501 -0.38049 -0.08920 -0.17847 216 ARG A NH2 
1638 N N   . ASP A 244 ? 1.42975 2.26974 2.34529 -0.04491 -0.08006 -0.09296 217 ASP A N   
1639 C CA  . ASP A 244 ? 1.55821 2.35513 2.42083 -0.00276 -0.06597 -0.08141 217 ASP A CA  
1640 C C   . ASP A 244 ? 1.60925 2.31304 2.38697 -0.01386 -0.04236 -0.06940 217 ASP A C   
1641 O O   . ASP A 244 ? 1.83787 2.48963 2.57389 -0.03636 -0.05641 -0.07067 217 ASP A O   
1642 C CB  . ASP A 244 ? 1.21601 2.00086 2.05206 0.03603  -0.10905 -0.08183 217 ASP A CB  
1643 C CG  . ASP A 244 ? 1.69215 2.56804 2.61217 0.05848  -0.13507 -0.09022 217 ASP A CG  
1644 O OD1 . ASP A 244 ? 1.86735 2.82097 2.86948 0.05184  -0.11173 -0.09723 217 ASP A OD1 
1645 O OD2 . ASP A 244 ? 1.69230 2.56329 2.59664 0.08337  -0.17863 -0.08884 217 ASP A OD2 
1646 N N   . LEU A 245 ? 1.43063 2.11628 2.18383 0.00348  -0.00722 -0.05945 218 LEU A N   
1647 C CA  . LEU A 245 ? 1.55900 2.16373 2.23444 -0.00200 0.01261  -0.04653 218 LEU A CA  
1648 C C   . LEU A 245 ? 1.60040 2.14427 2.20744 0.02221  -0.01449 -0.04587 218 LEU A C   
1649 O O   . LEU A 245 ? 1.48864 2.04050 2.09084 0.05573  -0.02896 -0.04865 218 LEU A O   
1650 C CB  . LEU A 245 ? 1.56313 2.17218 2.22828 0.00913  0.05492  -0.03720 218 LEU A CB  
1651 C CG  . LEU A 245 ? 1.79651 2.33053 2.38368 0.00515  0.07453  -0.02152 218 LEU A CG  
1652 C CD1 . LEU A 245 ? 1.77491 2.27222 2.35351 -0.03345 0.07886  -0.01295 218 LEU A CD1 
1653 C CD2 . LEU A 245 ? 1.95424 2.50242 2.53020 0.01467  0.11446  -0.01396 218 LEU A CD2 
1654 N N   . ASP A 246 ? 1.50888 1.99049 2.06474 0.00481  -0.01972 -0.04261 219 ASP A N   
1655 C CA  . ASP A 246 ? 1.59062 2.01744 2.08246 0.02271  -0.04042 -0.04278 219 ASP A CA  
1656 C C   . ASP A 246 ? 1.63545 2.03568 2.08554 0.05077  -0.02384 -0.03477 219 ASP A C   
1657 O O   . ASP A 246 ? 1.79898 2.17515 2.21418 0.07278  -0.04111 -0.03660 219 ASP A O   
1658 C CB  . ASP A 246 ? 1.48569 1.85739 1.93905 -0.00090 -0.04314 -0.04378 219 ASP A CB  
1659 C CG  . ASP A 246 ? 1.71226 2.04242 2.11159 0.01048  -0.06737 -0.04911 219 ASP A CG  
1660 O OD1 . ASP A 246 ? 1.73986 2.08382 2.13369 0.03119  -0.08769 -0.05083 219 ASP A OD1 
1661 O OD2 . ASP A 246 ? 1.76606 2.04886 2.12899 -0.00101 -0.06484 -0.05120 219 ASP A OD2 
1662 N N   . THR A 247 ? 1.55656 1.95922 2.00620 0.04783  0.00956  -0.02601 220 THR A N   
1663 C CA  . THR A 247 ? 1.69793 2.07852 2.10532 0.07148  0.02547  -0.02141 220 THR A CA  
1664 C C   . THR A 247 ? 1.64276 2.05184 2.06869 0.10235  0.01805  -0.03083 220 THR A C   
1665 O O   . THR A 247 ? 1.58924 1.96312 1.97355 0.12323  0.00686  -0.03335 220 THR A O   
1666 C CB  . THR A 247 ? 1.44098 1.82847 1.84577 0.06063  0.06247  -0.01021 220 THR A CB  
1667 O OG1 . THR A 247 ? 1.52799 1.88278 1.91912 0.03330  0.06749  0.00124  220 THR A OG1 
1668 C CG2 . THR A 247 ? 1.53872 1.89980 1.88930 0.08170  0.07620  -0.00733 220 THR A CG2 
1669 N N   . ASP A 248 ? 1.59171 2.06448 2.08371 0.10555  0.02478  -0.03675 221 ASP A N   
1670 C CA  . ASP A 248 ? 1.68476 2.18656 2.20359 0.13988  0.01891  -0.04649 221 ASP A CA  
1671 C C   . ASP A 248 ? 1.66202 2.14220 2.16934 0.15594  -0.02275 -0.04849 221 ASP A C   
1672 O O   . ASP A 248 ? 1.91540 2.37119 2.40077 0.18566  -0.03082 -0.05132 221 ASP A O   
1673 C CB  . ASP A 248 ? 1.64590 2.23073 2.24978 0.13966  0.03325  -0.05381 221 ASP A CB  
1674 C CG  . ASP A 248 ? 1.82911 2.43607 2.43841 0.12686  0.08025  -0.05150 221 ASP A CG  
1675 O OD1 . ASP A 248 ? 2.06281 2.62519 2.60984 0.13292  0.09967  -0.04728 221 ASP A OD1 
1676 O OD2 . ASP A 248 ? 1.85226 2.52308 2.52652 0.10872  0.09769  -0.05383 221 ASP A OD2 
1677 N N   . VAL A 249 ? 1.40032 1.88436 1.91698 0.13498  -0.04901 -0.04706 222 VAL A N   
1678 C CA  . VAL A 249 ? 1.54891 2.01362 2.04713 0.14693  -0.08919 -0.04673 222 VAL A CA  
1679 C C   . VAL A 249 ? 1.55930 1.94825 1.97707 0.15313  -0.09279 -0.04176 222 VAL A C   
1680 O O   . VAL A 249 ? 1.45956 1.82223 1.85359 0.17690  -0.11075 -0.03960 222 VAL A O   
1681 C CB  . VAL A 249 ? 1.25380 1.73876 1.77084 0.11823  -0.11427 -0.04942 222 VAL A CB  
1682 C CG1 . VAL A 249 ? 1.22443 1.68045 1.70262 0.12656  -0.15444 -0.04697 222 VAL A CG1 
1683 C CG2 . VAL A 249 ? 1.44965 2.01828 2.05479 0.11247  -0.11571 -0.05633 222 VAL A CG2 
1684 N N   . VAL A 250 ? 1.56986 1.92268 1.94713 0.13175  -0.07574 -0.03936 223 VAL A N   
1685 C CA  . VAL A 250 ? 1.50273 1.79374 1.81185 0.13457  -0.07797 -0.03679 223 VAL A CA  
1686 C C   . VAL A 250 ? 1.67960 1.95272 1.96951 0.15974  -0.06342 -0.03792 223 VAL A C   
1687 O O   . VAL A 250 ? 1.72983 1.96198 1.98007 0.17174  -0.07556 -0.03760 223 VAL A O   
1688 C CB  . VAL A 250 ? 1.35211 1.61680 1.63306 0.11001  -0.06377 -0.03496 223 VAL A CB  
1689 C CG1 . VAL A 250 ? 1.49227 1.70602 1.71337 0.11425  -0.06239 -0.03423 223 VAL A CG1 
1690 C CG2 . VAL A 250 ? 1.43746 1.70633 1.72824 0.08586  -0.08010 -0.03870 223 VAL A CG2 
1691 N N   . ILE A 251 ? 1.76409 2.06553 2.07902 0.16589  -0.03588 -0.04044 224 ILE A N   
1692 C CA  . ILE A 251 ? 1.64606 1.93007 1.93933 0.18847  -0.02008 -0.04640 224 ILE A CA  
1693 C C   . ILE A 251 ? 1.69415 1.98065 2.00871 0.21872  -0.03650 -0.05174 224 ILE A C   
1694 O O   . ILE A 251 ? 1.79394 2.03684 2.07252 0.23568  -0.03823 -0.05612 224 ILE A O   
1695 C CB  . ILE A 251 ? 1.62532 1.94212 1.93569 0.18651  0.01532  -0.04890 224 ILE A CB  
1696 C CG1 . ILE A 251 ? 1.79504 2.09230 2.06954 0.16112  0.02846  -0.03919 224 ILE A CG1 
1697 C CG2 . ILE A 251 ? 1.43654 1.74182 1.72872 0.21155  0.03211  -0.06087 224 ILE A CG2 
1698 C CD1 . ILE A 251 ? 1.94893 2.26882 2.22315 0.15671  0.06290  -0.03681 224 ILE A CD1 
1699 N N   . ASP A 252 ? 1.77145 2.10713 2.14585 0.22599  -0.05076 -0.05139 225 ASP A N   
1700 C CA  . ASP A 252 ? 1.68952 2.02855 2.08896 0.25946  -0.07125 -0.05359 225 ASP A CA  
1701 C C   . ASP A 252 ? 1.77941 2.06008 2.12820 0.26101  -0.10454 -0.04355 225 ASP A C   
1702 O O   . ASP A 252 ? 1.92220 2.16269 2.25173 0.28690  -0.11386 -0.04305 225 ASP A O   
1703 C CB  . ASP A 252 ? 1.73013 2.14617 2.21195 0.26617  -0.08218 -0.05531 225 ASP A CB  
1704 C CG  . ASP A 252 ? 2.12765 2.60499 2.66558 0.26976  -0.04525 -0.06664 225 ASP A CG  
1705 O OD1 . ASP A 252 ? 2.18441 2.64001 2.68977 0.26934  -0.01239 -0.07244 225 ASP A OD1 
1706 O OD2 . ASP A 252 ? 2.67192 3.22239 3.28570 0.27121  -0.04884 -0.07033 225 ASP A OD2 
1707 N N   . LYS A 253 ? 1.74236 2.01398 2.06649 0.23252  -0.12079 -0.03600 226 LYS A N   
1708 C CA  . LYS A 253 ? 1.79070 2.00861 2.05999 0.22943  -0.14818 -0.02628 226 LYS A CA  
1709 C C   . LYS A 253 ? 1.75170 1.90410 1.95678 0.22549  -0.13373 -0.02720 226 LYS A C   
1710 O O   . LYS A 253 ? 1.71755 1.81851 1.87948 0.23090  -0.15025 -0.01963 226 LYS A O   
1711 C CB  . LYS A 253 ? 1.76551 1.99341 2.02298 0.19855  -0.16472 -0.02293 226 LYS A CB  
1712 C CG  . LYS A 253 ? 1.58400 1.87358 1.89958 0.19898  -0.18762 -0.02306 226 LYS A CG  
1713 C CD  . LYS A 253 ? 1.61777 1.91262 1.95109 0.23269  -0.21785 -0.01462 226 LYS A CD  
1714 C CE  . LYS A 253 ? 1.59150 1.96120 1.99329 0.23492  -0.24301 -0.01644 226 LYS A CE  
1715 N NZ  . LYS A 253 ? 1.46532 1.84474 1.89113 0.27382  -0.27588 -0.00651 226 LYS A NZ  
1716 N N   . LEU A 254 ? 1.68656 1.84020 1.88340 0.21450  -0.10417 -0.03541 227 LEU A N   
1717 C CA  . LEU A 254 ? 1.70682 1.80779 1.84941 0.21042  -0.09213 -0.03919 227 LEU A CA  
1718 C C   . LEU A 254 ? 1.68390 1.76222 1.82601 0.23833  -0.08359 -0.04726 227 LEU A C   
1719 O O   . LEU A 254 ? 1.77266 1.79455 1.87061 0.23970  -0.08713 -0.04829 227 LEU A O   
1720 C CB  . LEU A 254 ? 1.83084 1.94269 1.96235 0.19025  -0.06879 -0.04386 227 LEU A CB  
1721 C CG  . LEU A 254 ? 1.52518 1.63960 1.64517 0.16320  -0.07492 -0.03890 227 LEU A CG  
1722 C CD1 . LEU A 254 ? 1.35922 1.48107 1.47190 0.15035  -0.05358 -0.04087 227 LEU A CD1 
1723 C CD2 . LEU A 254 ? 1.70047 1.77132 1.77408 0.15260  -0.09068 -0.03624 227 LEU A CD2 
1724 N N   . LYS A 255 ? 1.73425 1.85507 1.92593 0.25932  -0.07014 -0.05509 228 LYS A N   
1725 C CA  . LYS A 255 ? 1.95495 2.05523 2.15033 0.28920  -0.05946 -0.06744 228 LYS A CA  
1726 C C   . LYS A 255 ? 2.00139 2.07315 2.20684 0.31682  -0.08656 -0.06021 228 LYS A C   
1727 O O   . LYS A 255 ? 2.07725 2.10406 2.26901 0.33989  -0.08255 -0.06885 228 LYS A O   
1728 C CB  . LYS A 255 ? 1.86587 2.02596 2.11277 0.30324  -0.03220 -0.08033 228 LYS A CB  
1729 C CG  . LYS A 255 ? 1.96950 2.14026 2.19072 0.28293  -0.00148 -0.08787 228 LYS A CG  
1730 C CD  . LYS A 255 ? 1.70041 1.92886 1.96686 0.29547  0.02886  -0.09970 228 LYS A CD  
1731 C CE  . LYS A 255 ? 1.93898 2.17337 2.16885 0.27507  0.05807  -0.10333 228 LYS A CE  
1732 N NZ  . LYS A 255 ? 2.30483 2.48562 2.47292 0.27811  0.06473  -0.11724 228 LYS A NZ  
1733 N N   . SER A 256 ? 1.93114 2.02469 2.15756 0.31532  -0.11530 -0.04465 229 SER A N   
1734 C CA  . SER A 256 ? 1.98402 2.05056 2.21495 0.34184  -0.14715 -0.03213 229 SER A CA  
1735 C C   . SER A 256 ? 1.80171 1.80094 1.96239 0.32222  -0.16930 -0.01491 229 SER A C   
1736 O O   . SER A 256 ? 1.79852 1.78178 1.95362 0.33407  -0.20190 0.00278  229 SER A O   
1737 C CB  . SER A 256 ? 2.13639 2.27537 2.43512 0.35451  -0.16907 -0.02582 229 SER A CB  
1738 O OG  . SER A 256 ? 2.15694 2.32370 2.44704 0.31964  -0.18061 -0.01817 229 SER A OG  
1739 N N   . ALA A 257 ? 1.77448 1.73764 1.88169 0.29206  -0.15241 -0.01923 230 ALA A N   
1740 C CA  . ALA A 257 ? 1.83047 1.73281 1.87181 0.26994  -0.16636 -0.00565 230 ALA A CA  
1741 C C   . ALA A 257 ? 2.01443 1.83778 2.01943 0.28527  -0.16733 -0.00362 230 ALA A C   
1742 O O   . ALA A 257 ? 2.05599 1.86491 2.07105 0.30076  -0.14718 -0.02081 230 ALA A O   
1743 C CB  . ALA A 257 ? 1.74331 1.64829 1.75230 0.23173  -0.14743 -0.01314 230 ALA A CB  
1744 N N   . LYS A 258 ? 2.12701 1.89495 2.08501 0.27892  -0.19014 0.01726  231 LYS A N   
1745 C CA  . LYS A 258 ? 2.17831 1.85925 2.09764 0.29099  -0.19340 0.02361  231 LYS A CA  
1746 C C   . LYS A 258 ? 2.28357 1.90378 2.12943 0.25139  -0.19090 0.03362  231 LYS A C   
1747 O O   . LYS A 258 ? 2.34081 1.89336 2.15228 0.24476  -0.17920 0.02868  231 LYS A O   
1748 C CB  . LYS A 258 ? 2.24549 1.90430 2.17966 0.32982  -0.22591 0.04489  231 LYS A CB  
1749 C CG  . LYS A 258 ? 2.41770 2.10803 2.42264 0.37770  -0.22283 0.03074  231 LYS A CG  
1750 C CD  . LYS A 258 ? 2.63855 2.43549 2.71426 0.38487  -0.22434 0.02298  231 LYS A CD  
1751 C CE  . LYS A 258 ? 2.45203 2.28708 2.60302 0.43239  -0.21880 0.00823  231 LYS A CE  
1752 N NZ  . LYS A 258 ? 2.47108 2.41343 2.69522 0.43488  -0.21844 0.00093  231 LYS A NZ  
1753 N N   . THR A 259 ? 2.37691 2.02162 2.19935 0.22301  -0.19986 0.04516  232 THR A N   
1754 C CA  . THR A 259 ? 2.44151 2.03449 2.19511 0.18574  -0.19787 0.05694  232 THR A CA  
1755 C C   . THR A 259 ? 2.23477 1.86674 1.98241 0.14768  -0.17380 0.03933  232 THR A C   
1756 O O   . THR A 259 ? 2.07458 1.67572 1.79679 0.12465  -0.15409 0.02896  232 THR A O   
1757 C CB  . THR A 259 ? 2.55518 2.13442 2.27347 0.18381  -0.22845 0.08597  232 THR A CB  
1758 O OG1 . THR A 259 ? 2.45144 1.99589 2.17980 0.22446  -0.25506 0.10458  232 THR A OG1 
1759 C CG2 . THR A 259 ? 2.82176 2.34253 2.46252 0.14392  -0.22247 0.09969  232 THR A CG2 
1760 N N   . SER A 260 ? 2.23778 1.93655 2.01080 0.14057  -0.17577 0.03471  233 SER A N   
1761 C CA  . SER A 260 ? 2.13123 1.86284 1.89931 0.10835  -0.15538 0.01981  233 SER A CA  
1762 C C   . SER A 260 ? 2.03087 1.83517 1.85327 0.11605  -0.15135 0.00709  233 SER A C   
1763 O O   . SER A 260 ? 2.21360 2.04850 2.06790 0.13522  -0.16813 0.01286  233 SER A O   
1764 C CB  . SER A 260 ? 2.25547 1.97126 1.97121 0.07723  -0.15971 0.03069  233 SER A CB  
1765 O OG  . SER A 260 ? 2.19642 1.94117 1.91580 0.08310  -0.18172 0.04044  233 SER A OG  
1766 N N   . ILE A 261 ? 1.74873 1.58017 1.58248 0.10004  -0.12978 -0.00948 234 ILE A N   
1767 C CA  . ILE A 261 ? 1.82555 1.71555 1.70159 0.10080  -0.12299 -0.01938 234 ILE A CA  
1768 C C   . ILE A 261 ? 1.98704 1.88879 1.84701 0.07285  -0.11046 -0.02825 234 ILE A C   
1769 O O   . ILE A 261 ? 1.91665 1.80725 1.76267 0.06034  -0.09579 -0.03659 234 ILE A O   
1770 C CB  . ILE A 261 ? 1.81062 1.72361 1.72370 0.11801  -0.10837 -0.02990 234 ILE A CB  
1771 C CG1 . ILE A 261 ? 1.80987 1.71993 1.74780 0.14855  -0.11709 -0.02534 234 ILE A CG1 
1772 C CG2 . ILE A 261 ? 1.60518 1.56884 1.55302 0.11341  -0.09910 -0.03630 234 ILE A CG2 
1773 C CD1 . ILE A 261 ? 1.94446 1.88120 1.91550 0.16450  -0.09906 -0.03736 234 ILE A CD1 
1774 N N   . ASP A 262 ? 2.08937 2.01575 1.95419 0.06330  -0.11636 -0.02901 235 ASP A N   
1775 C CA  . ASP A 262 ? 2.00283 1.94125 1.85626 0.04022  -0.10369 -0.04030 235 ASP A CA  
1776 C C   . ASP A 262 ? 1.84287 1.82163 1.73875 0.04390  -0.09930 -0.04933 235 ASP A C   
1777 O O   . ASP A 262 ? 1.91754 1.91154 1.82697 0.04582  -0.11216 -0.04745 235 ASP A O   
1778 C CB  . ASP A 262 ? 2.07984 1.99872 1.88676 0.02106  -0.11218 -0.03557 235 ASP A CB  
1779 C CG  . ASP A 262 ? 2.18246 2.05202 1.94192 0.01549  -0.11686 -0.02142 235 ASP A CG  
1780 O OD1 . ASP A 262 ? 2.06591 1.91714 1.82303 0.01343  -0.10418 -0.02422 235 ASP A OD1 
1781 O OD2 . ASP A 262 ? 2.18281 2.02930 1.90487 0.01212  -0.13448 -0.00692 235 ASP A OD2 
1782 N N   . ILE A 263 ? 1.54844 1.54301 1.46476 0.04394  -0.08280 -0.05842 236 ILE A N   
1783 C CA  . ILE A 263 ? 1.57115 1.59374 1.52545 0.04846  -0.07707 -0.06332 236 ILE A CA  
1784 C C   . ILE A 263 ? 1.61809 1.64737 1.57208 0.03644  -0.06461 -0.07625 236 ILE A C   
1785 O O   . ILE A 263 ? 1.63286 1.66207 1.57985 0.03359  -0.05500 -0.08114 236 ILE A O   
1786 C CB  . ILE A 263 ? 1.54793 1.58297 1.52876 0.06526  -0.07011 -0.05852 236 ILE A CB  
1787 C CG1 . ILE A 263 ? 1.69721 1.72771 1.68212 0.08007  -0.07891 -0.04994 236 ILE A CG1 
1788 C CG2 . ILE A 263 ? 1.53770 1.59431 1.55272 0.06722  -0.06383 -0.05867 236 ILE A CG2 
1789 C CD1 . ILE A 263 ? 1.79192 1.83979 1.80259 0.09552  -0.06890 -0.04760 236 ILE A CD1 
1790 N N   . GLU A 264 ? 1.56910 1.60593 1.53412 0.02967  -0.06505 -0.08405 237 GLU A N   
1791 C CA  . GLU A 264 ? 1.43903 1.48201 1.41327 0.02361  -0.05211 -0.09902 237 GLU A CA  
1792 C C   . GLU A 264 ? 1.57257 1.62262 1.58458 0.03176  -0.04998 -0.09823 237 GLU A C   
1793 O O   . GLU A 264 ? 1.74620 1.79399 1.76545 0.02378  -0.05448 -0.10466 237 GLU A O   
1794 C CB  . GLU A 264 ? 1.44977 1.48590 1.39502 0.00528  -0.05112 -0.11328 237 GLU A CB  
1795 C CG  . GLU A 264 ? 1.53640 1.57984 1.49590 0.00188  -0.03487 -0.13360 237 GLU A CG  
1796 C CD  . GLU A 264 ? 1.75436 1.79229 1.68051 -0.01751 -0.03034 -0.15164 237 GLU A CD  
1797 O OE1 . GLU A 264 ? 2.12013 2.14797 2.00298 -0.03046 -0.03857 -0.14500 237 GLU A OE1 
1798 O OE2 . GLU A 264 ? 1.42234 1.46305 1.36251 -0.01923 -0.01827 -0.17246 237 GLU A OE2 
1799 N N   . HIS A 265 ? 1.45047 1.50689 1.48291 0.04546  -0.04377 -0.08975 238 HIS A N   
1800 C CA  . HIS A 265 ? 1.68564 1.74181 1.74847 0.05258  -0.03910 -0.08440 238 HIS A CA  
1801 C C   . HIS A 265 ? 1.61952 1.67713 1.69337 0.06310  -0.03071 -0.08682 238 HIS A C   
1802 O O   . HIS A 265 ? 1.64104 1.70791 1.70495 0.06330  -0.02827 -0.09543 238 HIS A O   
1803 C CB  . HIS A 265 ? 1.78345 1.84694 1.85754 0.06053  -0.04068 -0.06675 238 HIS A CB  
1804 C CG  . HIS A 265 ? 1.78174 1.85121 1.86648 0.05274  -0.04858 -0.06521 238 HIS A CG  
1805 N ND1 . HIS A 265 ? 1.59489 1.67104 1.70885 0.05033  -0.04483 -0.05754 238 HIS A ND1 
1806 C CD2 . HIS A 265 ? 1.80580 1.87842 1.87753 0.04628  -0.06149 -0.06954 238 HIS A CD2 
1807 C CE1 . HIS A 265 ? 1.70860 1.79888 1.83367 0.04265  -0.05550 -0.05997 238 HIS A CE1 
1808 N NE2 . HIS A 265 ? 1.70940 1.79704 1.80791 0.04208  -0.06769 -0.06628 238 HIS A NE2 
1809 N N   . LEU A 266 ? 1.72042 1.76951 1.81693 0.07157  -0.02689 -0.07812 239 LEU A N   
1810 C CA  . LEU A 266 ? 1.52019 1.56910 1.63059 0.08637  -0.02297 -0.07761 239 LEU A CA  
1811 C C   . LEU A 266 ? 1.71502 1.78267 1.81574 0.09789  -0.02700 -0.06554 239 LEU A C   
1812 O O   . LEU A 266 ? 1.67617 1.76118 1.77935 0.10357  -0.02819 -0.07421 239 LEU A O   
1813 C CB  . LEU A 266 ? 1.45117 1.47544 1.58320 0.09240  -0.01922 -0.06747 239 LEU A CB  
1814 C CG  . LEU A 266 ? 1.45307 1.46756 1.60498 0.11046  -0.01691 -0.06986 239 LEU A CG  
1815 C CD1 . LEU A 266 ? 1.71193 1.73461 1.87066 0.10806  -0.01179 -0.09932 239 LEU A CD1 
1816 C CD2 . LEU A 266 ? 1.89531 1.87126 2.06419 0.11349  -0.01286 -0.05831 239 LEU A CD2 
1817 N N   . ALA A 267 ? 1.45588 1.52401 1.54658 0.10000  -0.02839 -0.04813 240 ALA A N   
1818 C CA  . ALA A 267 ? 1.63413 1.71804 1.70825 0.10853  -0.03218 -0.03972 240 ALA A CA  
1819 C C   . ALA A 267 ? 1.51579 1.59947 1.57618 0.10606  -0.02916 -0.02895 240 ALA A C   
1820 O O   . ALA A 267 ? 1.56017 1.63571 1.63226 0.10147  -0.02379 -0.02134 240 ALA A O   
1821 C CB  . ALA A 267 ? 1.70250 1.78865 1.78327 0.12503  -0.03568 -0.02634 240 ALA A CB  
1822 N N   . ILE A 268 ? 1.58999 1.68448 1.62859 0.10828  -0.03153 -0.03108 241 ILE A N   
1823 C CA  . ILE A 268 ? 1.46538 1.56141 1.49197 0.10923  -0.02628 -0.02578 241 ILE A CA  
1824 C C   . ILE A 268 ? 1.61506 1.71996 1.61932 0.11805  -0.02445 -0.01703 241 ILE A C   
1825 O O   . ILE A 268 ? 1.54327 1.65179 1.52762 0.11970  -0.02117 -0.02217 241 ILE A O   
1826 C CB  . ILE A 268 ? 1.24026 1.33198 1.25585 0.10393  -0.02970 -0.03925 241 ILE A CB  
1827 C CG1 . ILE A 268 ? 1.74959 1.83299 1.77289 0.09335  -0.03506 -0.04875 241 ILE A CG1 
1828 C CG2 . ILE A 268 ? 1.78399 1.87726 1.80442 0.10792  -0.02407 -0.03540 241 ILE A CG2 
1829 C CD1 . ILE A 268 ? 1.88444 1.96525 1.92896 0.08881  -0.03477 -0.04526 241 ILE A CD1 
1830 N N   . VAL A 269 ? 1.75327 1.85937 1.75794 0.12481  -0.02738 -0.00422 242 VAL A N   
1831 C CA  . VAL A 269 ? 1.47201 1.58630 1.44782 0.13267  -0.02771 0.00804  242 VAL A CA  
1832 C C   . VAL A 269 ? 1.72531 1.83683 1.69226 0.13069  -0.01109 0.02038  242 VAL A C   
1833 O O   . VAL A 269 ? 2.02495 2.12660 2.01396 0.12593  -0.00207 0.03194  242 VAL A O   
1834 C CB  . VAL A 269 ? 1.80052 1.91326 1.77885 0.14329  -0.03741 0.02445  242 VAL A CB  
1835 C CG1 . VAL A 269 ? 2.01404 2.13627 1.95304 0.15079  -0.04168 0.03894  242 VAL A CG1 
1836 C CG2 . VAL A 269 ? 1.76678 1.89113 1.76625 0.14649  -0.05091 0.00920  242 VAL A CG2 
1837 N N   . PRO A 270 ? 1.67904 1.80048 1.61606 0.13244  -0.00453 0.01603  243 PRO A N   
1838 C CA  . PRO A 270 ? 1.73636 1.86245 1.66712 0.13071  0.01596  0.02559  243 PRO A CA  
1839 C C   . PRO A 270 ? 1.90444 2.02570 1.81653 0.13049  0.02366  0.05351  243 PRO A C   
1840 O O   . PRO A 270 ? 1.98612 2.11480 1.88578 0.12639  0.04421  0.06219  243 PRO A O   
1841 C CB  . PRO A 270 ? 1.64619 1.78182 1.54507 0.13456  0.02041  0.00759  243 PRO A CB  
1842 C CG  . PRO A 270 ? 1.69469 1.83068 1.56889 0.13648  0.00052  0.00016  243 PRO A CG  
1843 C CD  . PRO A 270 ? 1.84923 1.97894 1.75782 0.13420  -0.01387 -0.00131 243 PRO A CD  
1844 N N   . THR A 271 ? 1.79723 1.90564 1.70695 0.13538  0.00893  0.06857  244 THR A N   
1845 C CA  . THR A 271 ? 1.87586 1.96983 1.76258 0.13704  0.01296  0.10015  244 THR A CA  
1846 C C   . THR A 271 ? 1.97566 2.04300 1.89527 0.13911  0.00494  0.11332  244 THR A C   
1847 O O   . THR A 271 ? 1.97917 2.04634 1.91721 0.14843  -0.01353 0.10247  244 THR A O   
1848 C CB  . THR A 271 ? 1.84983 1.95269 1.68631 0.14747  -0.00186 0.10814  244 THR A CB  
1849 O OG1 . THR A 271 ? 2.14503 2.26802 1.94641 0.14384  0.00846  0.09214  244 THR A OG1 
1850 C CG2 . THR A 271 ? 2.03386 2.11543 1.84079 0.15073  -0.00079 0.14633  244 THR A CG2 
1851 N N   . THR A 272 ? 1.96201 2.00701 1.89099 0.12902  0.02095  0.13409  245 THR A N   
1852 C CA  . THR A 272 ? 1.87022 1.87878 1.82425 0.13034  0.01598  0.14865  245 THR A CA  
1853 C C   . THR A 272 ? 2.02232 2.00208 1.93884 0.13727  0.01480  0.18701  245 THR A C   
1854 O O   . THR A 272 ? 2.18505 2.17733 2.05291 0.13905  0.01773  0.20155  245 THR A O   
1855 C CB  . THR A 272 ? 1.75346 1.75053 1.74746 0.11010  0.03292  0.14318  245 THR A CB  
1856 O OG1 . THR A 272 ? 2.04881 2.04752 2.02867 0.09390  0.05678  0.16220  245 THR A OG1 
1857 C CG2 . THR A 272 ? 1.59320 1.61988 1.61605 0.10496  0.03077  0.10935  245 THR A CG2 
1858 N N   . ARG A 273 ? 1.97380 1.91040 1.90922 0.14142  0.01034  0.20379  246 ARG A N   
1859 C CA  . ARG A 273 ? 2.25607 2.15255 2.15635 0.14893  0.00795  0.24556  246 ARG A CA  
1860 C C   . ARG A 273 ? 2.30171 2.14795 2.22305 0.12972  0.02735  0.26278  246 ARG A C   
1861 O O   . ARG A 273 ? 2.21744 2.03221 2.17951 0.13314  0.02171  0.25306  246 ARG A O   
1862 C CB  . ARG A 273 ? 2.20760 2.09351 2.10847 0.18016  -0.02258 0.25279  246 ARG A CB  
1863 C CG  . ARG A 273 ? 2.20419 2.04953 2.06045 0.19342  -0.03150 0.30033  246 ARG A CG  
1864 C CD  . ARG A 273 ? 2.33477 2.18934 2.19169 0.22884  -0.06700 0.30519  246 ARG A CD  
1865 N NE  . ARG A 273 ? 2.59813 2.41174 2.40892 0.24488  -0.08029 0.35458  246 ARG A NE  
1866 C CZ  . ARG A 273 ? 2.60106 2.43061 2.34395 0.24571  -0.08786 0.37958  246 ARG A CZ  
1867 N NH1 . ARG A 273 ? 2.33560 2.21993 2.05074 0.23172  -0.08172 0.35687  246 ARG A NH1 
1868 N NH2 . ARG A 273 ? 2.71871 2.50437 2.41672 0.26125  -0.10224 0.42850  246 ARG A NH2 
1869 N N   . VAL A 274 ? 2.54107 2.38033 2.43479 0.10739  0.05208  0.28595  247 VAL A N   
1870 C CA  . VAL A 274 ? 2.55573 2.34746 2.46586 0.08257  0.07348  0.30536  247 VAL A CA  
1871 C C   . VAL A 274 ? 2.74755 2.47906 2.61057 0.09078  0.06995  0.35488  247 VAL A C   
1872 O O   . VAL A 274 ? 2.82974 2.57110 2.63228 0.09545  0.07073  0.38112  247 VAL A O   
1873 C CB  . VAL A 274 ? 2.28345 2.10926 2.20009 0.04947  0.10605  0.29993  247 VAL A CB  
1874 C CG1 . VAL A 274 ? 1.89414 1.76306 1.86904 0.04112  0.10620  0.25524  247 VAL A CG1 
1875 C CG2 . VAL A 274 ? 2.19013 2.05604 2.05138 0.05209  0.11585  0.30962  247 VAL A CG2 
1876 N N   . ASP A 275 ? 2.53196 2.19754 2.41899 0.09332  0.06517  0.36748  248 ASP A N   
1877 C CA  . ASP A 275 ? 2.92167 2.51798 2.76878 0.10853  0.05549  0.41572  248 ASP A CA  
1878 C C   . ASP A 275 ? 2.91514 2.53433 2.72569 0.14833  0.02245  0.42608  248 ASP A C   
1879 O O   . ASP A 275 ? 2.54747 2.18852 2.39354 0.17608  -0.00243 0.39849  248 ASP A O   
1880 C CB  . ASP A 275 ? 3.16123 2.72731 2.95920 0.07716  0.08490  0.45844  248 ASP A CB  
1881 C CG  . ASP A 275 ? 3.13914 2.68175 2.97935 0.03474  0.11669  0.45033  248 ASP A CG  
1882 O OD1 . ASP A 275 ? 3.20072 2.71135 3.09541 0.03417  0.11073  0.42773  248 ASP A OD1 
1883 O OD2 . ASP A 275 ? 3.11944 2.67904 2.93944 0.00067  0.14832  0.46427  248 ASP A OD2 
1884 N N   . GLY A 276 ? 3.06005 2.67872 2.79925 0.14923  0.02237  0.46431  249 GLY A N   
1885 C CA  . GLY A 276 ? 2.89557 2.54326 2.59515 0.18318  -0.01129 0.47382  249 GLY A CA  
1886 C C   . GLY A 276 ? 2.78814 2.50414 2.44038 0.17247  -0.00435 0.46159  249 GLY A C   
1887 O O   . GLY A 276 ? 2.82581 2.55641 2.41766 0.18904  -0.02504 0.48266  249 GLY A O   
1888 N N   . ASN A 277 ? 2.67108 2.42903 2.35005 0.14596  0.02327  0.42624  250 ASN A N   
1889 C CA  . ASN A 277 ? 2.63669 2.45472 2.27677 0.13532  0.03541  0.40926  250 ASN A CA  
1890 C C   . ASN A 277 ? 2.45475 2.32765 2.15061 0.13403  0.03600  0.35411  250 ASN A C   
1891 O O   . ASN A 277 ? 2.33351 2.20152 2.09096 0.12246  0.04728  0.33274  250 ASN A O   
1892 C CB  . ASN A 277 ? 2.56769 2.37892 2.17202 0.10125  0.07733  0.43003  250 ASN A CB  
1893 C CG  . ASN A 277 ? 2.94420 2.69835 2.47822 0.09841  0.07958  0.48914  250 ASN A CG  
1894 O OD1 . ASN A 277 ? 2.91954 2.68518 2.37656 0.10580  0.07133  0.50992  250 ASN A OD1 
1895 N ND2 . ASN A 277 ? 3.11784 2.80622 2.67382 0.08630  0.09022  0.51689  250 ASN A ND2 
1896 N N   . SER A 278 ? 2.49350 2.41558 2.16341 0.14441  0.02303  0.33181  251 SER A N   
1897 C CA  . SER A 278 ? 2.02115 1.98891 1.73417 0.14360  0.02250  0.28299  251 SER A CA  
1898 C C   . SER A 278 ? 1.96017 1.95350 1.67707 0.11992  0.05811  0.26625  251 SER A C   
1899 O O   . SER A 278 ? 2.26970 2.26954 1.93557 0.10850  0.07950  0.28214  251 SER A O   
1900 C CB  . SER A 278 ? 2.17195 2.17720 1.85691 0.16118  -0.00479 0.26456  251 SER A CB  
1901 O OG  . SER A 278 ? 2.23680 2.22896 1.92433 0.18509  -0.03902 0.28006  251 SER A OG  
1902 N N   . TYR A 279 ? 1.68999 1.70048 1.46760 0.11368  0.06425  0.23364  252 TYR A N   
1903 C CA  . TYR A 279 ? 1.99992 2.03903 1.79894 0.09559  0.09422  0.21525  252 TYR A CA  
1904 C C   . TYR A 279 ? 2.06303 2.13807 1.88367 0.10464  0.08490  0.17376  252 TYR A C   
1905 O O   . TYR A 279 ? 2.07792 2.14987 1.93648 0.11217  0.06500  0.15570  252 TYR A O   
1906 C CB  . TYR A 279 ? 2.27513 2.29677 2.13002 0.07689  0.10944  0.21970  252 TYR A CB  
1907 C CG  . TYR A 279 ? 2.42115 2.48146 2.31218 0.05986  0.13649  0.19955  252 TYR A CG  
1908 C CD1 . TYR A 279 ? 2.48244 2.56169 2.35004 0.04428  0.16951  0.21207  252 TYR A CD1 
1909 C CD2 . TYR A 279 ? 2.36491 2.44560 2.31420 0.05995  0.12895  0.16852  252 TYR A CD2 
1910 C CE1 . TYR A 279 ? 2.55575 2.67878 2.46661 0.03169  0.19441  0.19172  252 TYR A CE1 
1911 C CE2 . TYR A 279 ? 2.25360 2.37410 2.24164 0.04846  0.14931  0.15117  252 TYR A CE2 
1912 C CZ  . TYR A 279 ? 2.47982 2.62403 2.45343 0.03552  0.18207  0.16171  252 TYR A CZ  
1913 O OH  . TYR A 279 ? 2.30902 2.50106 2.33088 0.02697  0.20257  0.14251  252 TYR A OH  
1914 N N   . TYR A 280 ? 2.02878 2.13417 1.82306 0.10330  0.10115  0.15857  253 TYR A N   
1915 C CA  . TYR A 280 ? 1.92341 2.05379 1.72810 0.11256  0.09353  0.12125  253 TYR A CA  
1916 C C   . TYR A 280 ? 2.01507 2.16697 1.87209 0.10560  0.11348  0.10158  253 TYR A C   
1917 O O   . TYR A 280 ? 2.02772 2.19743 1.88679 0.09543  0.14304  0.10702  253 TYR A O   
1918 C CB  . TYR A 280 ? 1.84972 1.99510 1.59072 0.11810  0.09670  0.11279  253 TYR A CB  
1919 C CG  . TYR A 280 ? 1.97908 2.14100 1.72538 0.12605  0.09121  0.07368  253 TYR A CG  
1920 C CD1 . TYR A 280 ? 2.08063 2.23594 1.84732 0.13302  0.06317  0.05682  253 TYR A CD1 
1921 C CD2 . TYR A 280 ? 1.84258 2.02404 1.57254 0.12610  0.11612  0.05319  253 TYR A CD2 
1922 C CE1 . TYR A 280 ? 1.86659 2.02795 1.63456 0.13727  0.05910  0.02371  253 TYR A CE1 
1923 C CE2 . TYR A 280 ? 1.65655 1.84254 1.39010 0.13451  0.11113  0.01783  253 TYR A CE2 
1924 C CZ  . TYR A 280 ? 1.73732 1.90998 1.48798 0.13882  0.08192  0.00482  253 TYR A CZ  
1925 O OH  . TYR A 280 ? 1.78972 1.95819 1.54096 0.14422  0.07775  -0.02784 253 TYR A OH  
1926 N N   . TRP A 281 ? 1.85192 2.00521 1.75113 0.11102  0.09711  0.07940  254 TRP A N   
1927 C CA  . TRP A 281 ? 1.92878 2.10268 1.88112 0.10764  0.10771  0.06247  254 TRP A CA  
1928 C C   . TRP A 281 ? 1.96468 2.13688 1.93004 0.11916  0.08711  0.03599  254 TRP A C   
1929 O O   . TRP A 281 ? 2.12757 2.28580 2.11687 0.11777  0.06781  0.03317  254 TRP A O   
1930 C CB  . TRP A 281 ? 2.03624 2.20371 2.03541 0.09275  0.10970  0.07602  254 TRP A CB  
1931 C CG  . TRP A 281 ? 1.79562 1.99474 1.85015 0.08623  0.12193  0.06294  254 TRP A CG  
1932 C CD1 . TRP A 281 ? 1.87555 2.10646 1.94987 0.07602  0.15101  0.06696  254 TRP A CD1 
1933 C CD2 . TRP A 281 ? 1.83837 2.04519 1.93717 0.08924  0.10425  0.04434  254 TRP A CD2 
1934 N NE1 . TRP A 281 ? 1.89891 2.16181 2.03443 0.07455  0.15025  0.05070  254 TRP A NE1 
1935 C CE2 . TRP A 281 ? 1.84785 2.09407 1.99540 0.08308  0.11994  0.03802  254 TRP A CE2 
1936 C CE3 . TRP A 281 ? 2.00143 2.18823 2.10178 0.09573  0.07715  0.03287  254 TRP A CE3 
1937 C CZ2 . TRP A 281 ? 1.91472 2.17973 2.11044 0.08555  0.10442  0.02231  254 TRP A CZ2 
1938 C CZ3 . TRP A 281 ? 1.84669 2.04699 1.98695 0.09574  0.06499  0.01837  254 TRP A CZ3 
1939 C CH2 . TRP A 281 ? 1.55993 1.79843 1.74646 0.09186  0.07618  0.01399  254 TRP A CH2 
1940 N N   . PRO A 282 ? 1.83434 2.01662 1.78086 0.12958  0.09228  0.01556  255 PRO A N   
1941 C CA  . PRO A 282 ? 1.84408 2.01375 1.79161 0.13831  0.07264  -0.00652 255 PRO A CA  
1942 C C   . PRO A 282 ? 1.71349 1.89250 1.70216 0.14570  0.07485  -0.02270 255 PRO A C   
1943 O O   . PRO A 282 ? 1.99075 2.15642 1.97031 0.15527  0.06662  -0.04157 255 PRO A O   
1944 C CB  . PRO A 282 ? 2.00280 2.16910 1.89677 0.14420  0.07526  -0.01902 255 PRO A CB  
1945 C CG  . PRO A 282 ? 1.80905 1.99750 1.69210 0.14457  0.10557  -0.01562 255 PRO A CG  
1946 C CD  . PRO A 282 ? 1.81337 2.01090 1.72260 0.13255  0.11572  0.01206  255 PRO A CD  
1947 N N   . ASP A 283 ? 1.71985 1.92070 1.75455 0.14111  0.08432  -0.01512 256 ASP A N   
1948 C CA  . ASP A 283 ? 2.01747 2.23639 2.09572 0.15167  0.08474  -0.02902 256 ASP A CA  
1949 C C   . ASP A 283 ? 1.81851 2.01286 1.90277 0.15604  0.05696  -0.03698 256 ASP A C   
1950 O O   . ASP A 283 ? 2.02974 2.21159 2.10884 0.17071  0.05132  -0.05187 256 ASP A O   
1951 C CB  . ASP A 283 ? 1.78935 2.04383 1.92071 0.14161  0.09678  -0.01924 256 ASP A CB  
1952 C CG  . ASP A 283 ? 1.77415 2.05594 1.90059 0.13564  0.13011  -0.01212 256 ASP A CG  
1953 O OD1 . ASP A 283 ? 1.87418 2.14760 1.95203 0.14203  0.14279  -0.01631 256 ASP A OD1 
1954 O OD2 . ASP A 283 ? 1.90493 2.21722 2.07361 0.12195  0.14433  -0.00308 256 ASP A OD2 
1955 N N   . ILE A 284 ? 1.55179 1.73480 1.64346 0.14281  0.04085  -0.02731 257 ILE A N   
1956 C CA  . ILE A 284 ? 1.70941 1.86962 1.79914 0.14307  0.01730  -0.03367 257 ILE A CA  
1957 C C   . ILE A 284 ? 1.79517 1.92534 1.84007 0.14586  0.01062  -0.04236 257 ILE A C   
1958 O O   . ILE A 284 ? 1.89321 2.00211 1.92904 0.15115  -0.00083 -0.05167 257 ILE A O   
1959 C CB  . ILE A 284 ? 1.45140 1.60791 1.55556 0.12683  0.00604  -0.02524 257 ILE A CB  
1960 C CG1 . ILE A 284 ? 1.39212 1.57884 1.54299 0.11944  0.01185  -0.01959 257 ILE A CG1 
1961 C CG2 . ILE A 284 ? 1.61213 1.74680 1.70651 0.12444  -0.01508 -0.03212 257 ILE A CG2 
1962 C CD1 . ILE A 284 ? 1.52268 1.70182 1.68754 0.10171  0.00154  -0.01579 257 ILE A CD1 
1963 N N   . TYR A 285 ? 1.52668 1.65437 1.54286 0.14107  0.01642  -0.03843 258 TYR A N   
1964 C CA  . TYR A 285 ? 1.59351 1.70208 1.57091 0.14085  0.00978  -0.04887 258 TYR A CA  
1965 C C   . TYR A 285 ? 1.79515 1.89158 1.75784 0.15206  0.01509  -0.06604 258 TYR A C   
1966 O O   . TYR A 285 ? 1.80071 1.86995 1.74974 0.15087  0.00434  -0.07715 258 TYR A O   
1967 C CB  . TYR A 285 ? 1.57881 1.69670 1.53066 0.13764  0.01457  -0.04024 258 TYR A CB  
1968 C CG  . TYR A 285 ? 1.49241 1.60150 1.41034 0.13409  0.00317  -0.05000 258 TYR A CG  
1969 C CD1 . TYR A 285 ? 1.42827 1.53261 1.35220 0.12607  -0.01226 -0.05053 258 TYR A CD1 
1970 C CD2 . TYR A 285 ? 1.95461 2.06507 1.83595 0.13726  0.00871  -0.06088 258 TYR A CD2 
1971 C CE1 . TYR A 285 ? 1.61647 1.72258 1.51797 0.12080  -0.02291 -0.06090 258 TYR A CE1 
1972 C CE2 . TYR A 285 ? 2.08517 2.19322 1.93836 0.13089  -0.00432 -0.07188 258 TYR A CE2 
1973 C CZ  . TYR A 285 ? 1.85009 1.95857 1.71700 0.12240  -0.02063 -0.07129 258 TYR A CZ  
1974 O OH  . TYR A 285 ? 1.87830 1.99358 1.72562 0.11415  -0.03386 -0.08382 258 TYR A OH  
1975 N N   . ASN A 286 ? 1.78581 1.89970 1.75147 0.16242  0.03395  -0.06911 259 ASN A N   
1976 C CA  . ASN A 286 ? 1.66832 1.76876 1.62068 0.17622  0.04237  -0.08935 259 ASN A CA  
1977 C C   . ASN A 286 ? 1.77421 1.86090 1.75826 0.18931  0.03430  -0.09415 259 ASN A C   
1978 O O   . ASN A 286 ? 2.00613 2.05974 1.97425 0.19845  0.03118  -0.10963 259 ASN A O   
1979 C CB  . ASN A 286 ? 1.82848 1.95606 1.77600 0.18425  0.06876  -0.09362 259 ASN A CB  
1980 C CG  . ASN A 286 ? 1.84781 1.98078 1.74771 0.17344  0.07408  -0.08971 259 ASN A CG  
1981 O OD1 . ASN A 286 ? 2.07660 2.23507 1.97216 0.17023  0.09119  -0.07705 259 ASN A OD1 
1982 N ND2 . ASN A 286 ? 1.85625 1.96625 1.71956 0.16634  0.05838  -0.09930 259 ASN A ND2 
1983 N N   . SER A 287 ? 1.77875 1.88747 1.80594 0.19018  0.02895  -0.08097 260 SER A N   
1984 C CA  . SER A 287 ? 1.81236 1.90942 1.86647 0.20356  0.01472  -0.08228 260 SER A CA  
1985 C C   . SER A 287 ? 1.88173 1.93265 1.90579 0.19451  -0.00641 -0.08147 260 SER A C   
1986 O O   . SER A 287 ? 1.88744 1.90357 1.90422 0.20678  -0.01479 -0.08745 260 SER A O   
1987 C CB  . SER A 287 ? 1.68079 1.81633 1.78508 0.20184  0.00926  -0.06937 260 SER A CB  
1988 O OG  . SER A 287 ? 1.81796 1.95165 1.91576 0.18003  -0.00224 -0.05737 260 SER A OG  
1989 N N   . ILE A 288 ? 1.85909 1.90734 1.86525 0.17311  -0.01346 -0.07415 261 ILE A N   
1990 C CA  . ILE A 288 ? 1.80144 1.81257 1.77979 0.16024  -0.02864 -0.07445 261 ILE A CA  
1991 C C   . ILE A 288 ? 1.72709 1.70374 1.66873 0.15862  -0.02457 -0.08965 261 ILE A C   
1992 O O   . ILE A 288 ? 1.77245 1.70671 1.69491 0.15577  -0.03352 -0.09258 261 ILE A O   
1993 C CB  . ILE A 288 ? 1.75494 1.77913 1.73022 0.13979  -0.03336 -0.06697 261 ILE A CB  
1994 C CG1 . ILE A 288 ? 1.90240 1.95241 1.91150 0.13857  -0.03812 -0.05574 261 ILE A CG1 
1995 C CG2 . ILE A 288 ? 1.33463 1.32757 1.28246 0.12386  -0.04383 -0.06953 261 ILE A CG2 
1996 C CD1 . ILE A 288 ? 1.68656 1.74909 1.69784 0.12281  -0.03792 -0.05123 261 ILE A CD1 
1997 N N   . ILE A 289 ? 1.68789 1.67926 1.61536 0.15816  -0.01162 -0.09934 262 ILE A N   
1998 C CA  . ILE A 289 ? 1.72752 1.68804 1.61911 0.15404  -0.00881 -0.11828 262 ILE A CA  
1999 C C   . ILE A 289 ? 1.75838 1.68467 1.65041 0.17420  -0.00392 -0.13039 262 ILE A C   
2000 O O   . ILE A 289 ? 1.72672 1.60438 1.59335 0.16951  -0.00807 -0.14240 262 ILE A O   
2001 C CB  . ILE A 289 ? 1.88114 1.86853 1.75238 0.14970  0.00126  -0.12621 262 ILE A CB  
2002 C CG1 . ILE A 289 ? 1.61730 1.63194 1.48996 0.13366  -0.00739 -0.11332 262 ILE A CG1 
2003 C CG2 . ILE A 289 ? 1.78871 1.74625 1.62176 0.14361  0.00288  -0.15051 262 ILE A CG2 
2004 C CD1 . ILE A 289 ? 1.75587 1.79372 1.60276 0.12952  -0.00442 -0.11753 262 ILE A CD1 
2005 N N   . GLU A 290 ? 1.74015 1.69080 1.66445 0.19691  0.00569  -0.12808 263 GLU A N   
2006 C CA  . GLU A 290 ? 1.67629 1.59975 1.61265 0.22279  0.00969  -0.13932 263 GLU A CA  
2007 C C   . GLU A 290 ? 1.68802 1.56753 1.62714 0.22600  -0.01137 -0.12766 263 GLU A C   
2008 O O   . GLU A 290 ? 1.88347 1.70926 1.80865 0.23828  -0.01376 -0.13743 263 GLU A O   
2009 C CB  . GLU A 290 ? 1.82103 1.79467 1.80349 0.24515  0.02404  -0.13773 263 GLU A CB  
2010 C CG  . GLU A 290 ? 1.96758 1.92600 1.97435 0.27831  0.03121  -0.15222 263 GLU A CG  
2011 C CD  . GLU A 290 ? 2.15927 2.18160 2.22131 0.29728  0.04730  -0.15142 263 GLU A CD  
2012 O OE1 . GLU A 290 ? 2.16143 2.23106 2.24674 0.28292  0.04598  -0.13402 263 GLU A OE1 
2013 O OE2 . GLU A 290 ? 2.44452 2.47008 2.52909 0.32559  0.06288  -0.16983 263 GLU A OE2 
2014 N N   . ALA A 291 ? 1.61091 1.50812 1.56355 0.21464  -0.02669 -0.10660 264 ALA A N   
2015 C CA  . ALA A 291 ? 1.67915 1.53458 1.62241 0.21332  -0.04762 -0.09263 264 ALA A CA  
2016 C C   . ALA A 291 ? 1.78456 1.58395 1.67884 0.18959  -0.05047 -0.09748 264 ALA A C   
2017 O O   . ALA A 291 ? 1.80964 1.55048 1.68387 0.19295  -0.06063 -0.09249 264 ALA A O   
2018 C CB  . ALA A 291 ? 1.73272 1.62288 1.69410 0.20218  -0.06142 -0.07323 264 ALA A CB  
2019 N N   . ALA A 292 ? 1.76754 1.58437 1.64358 0.16496  -0.04217 -0.10627 265 ALA A N   
2020 C CA  . ALA A 292 ? 1.61284 1.39091 1.45126 0.13658  -0.04484 -0.11135 265 ALA A CA  
2021 C C   . ALA A 292 ? 1.75817 1.48621 1.57044 0.13729  -0.03736 -0.13290 265 ALA A C   
2022 O O   . ALA A 292 ? 1.79128 1.46041 1.57560 0.12236  -0.04203 -0.13324 265 ALA A O   
2023 C CB  . ALA A 292 ? 1.59641 1.41950 1.43374 0.11247  -0.04148 -0.11396 265 ALA A CB  
2024 N N   . ILE A 293 ? 1.86932 1.61646 1.68627 0.15182  -0.02438 -0.15186 266 ILE A N   
2025 C CA  . ILE A 293 ? 1.96038 1.66238 1.74823 0.14928  -0.01592 -0.17875 266 ILE A CA  
2026 C C   . ILE A 293 ? 2.03770 1.68697 1.83160 0.18056  -0.01313 -0.18468 266 ILE A C   
2027 O O   . ILE A 293 ? 2.28061 1.85716 2.04910 0.17516  -0.01581 -0.19279 266 ILE A O   
2028 C CB  . ILE A 293 ? 1.88443 1.63180 1.66419 0.14733  -0.00314 -0.19898 266 ILE A CB  
2029 C CG1 . ILE A 293 ? 1.92697 1.71407 1.69708 0.11671  -0.01020 -0.19527 266 ILE A CG1 
2030 C CG2 . ILE A 293 ? 1.95111 1.65313 1.70094 0.14994  0.00730  -0.23175 266 ILE A CG2 
2031 C CD1 . ILE A 293 ? 1.68020 1.50767 1.43356 0.11329  -0.00327 -0.21169 266 ILE A CD1 
2032 N N   . ASN A 294 ? 1.83455 1.51900 1.66533 0.21385  -0.00723 -0.18102 267 ASN A N   
2033 C CA  . ASN A 294 ? 2.01147 1.65546 1.85772 0.24996  -0.00331 -0.19020 267 ASN A CA  
2034 C C   . ASN A 294 ? 2.31206 1.90746 2.16468 0.26056  -0.02475 -0.16487 267 ASN A C   
2035 O O   . ASN A 294 ? 2.50483 2.02429 2.34222 0.27384  -0.02814 -0.17044 267 ASN A O   
2036 C CB  . ASN A 294 ? 1.81885 1.52720 1.70999 0.28085  0.01152  -0.19532 267 ASN A CB  
2037 C CG  . ASN A 294 ? 2.08139 1.82767 1.95545 0.27266  0.03486  -0.21993 267 ASN A CG  
2038 O OD1 . ASN A 294 ? 1.99211 1.80575 1.88204 0.26748  0.04260  -0.21137 267 ASN A OD1 
2039 N ND2 . ASN A 294 ? 2.42328 2.12255 2.26038 0.26989  0.04570  -0.25043 267 ASN A ND2 
2040 N N   . ARG A 295 ? 2.02183 1.65588 1.89300 0.25485  -0.04015 -0.13671 268 ARG A N   
2041 C CA  . ARG A 295 ? 2.03356 1.62970 1.90595 0.26510  -0.06339 -0.10987 268 ARG A CA  
2042 C C   . ARG A 295 ? 2.24357 1.79463 2.06831 0.22707  -0.07446 -0.09396 268 ARG A C   
2043 O O   . ARG A 295 ? 2.41614 1.92196 2.22618 0.23131  -0.09324 -0.07023 268 ARG A O   
2044 C CB  . ARG A 295 ? 1.98371 1.64926 1.90348 0.28157  -0.07531 -0.09079 268 ARG A CB  
2045 C CG  . ARG A 295 ? 1.87564 1.57876 1.85064 0.32391  -0.06755 -0.10193 268 ARG A CG  
2046 C CD  . ARG A 295 ? 2.00330 1.77902 2.03029 0.33559  -0.08077 -0.08457 268 ARG A CD  
2047 N NE  . ARG A 295 ? 1.90447 1.75602 1.95408 0.31963  -0.06254 -0.09211 268 ARG A NE  
2048 C CZ  . ARG A 295 ? 1.95612 1.84172 2.00032 0.29063  -0.06862 -0.07899 268 ARG A CZ  
2049 N NH1 . ARG A 295 ? 2.12230 1.98103 2.13913 0.27289  -0.09058 -0.06028 268 ARG A NH1 
2050 N NH2 . ARG A 295 ? 1.83348 1.77823 1.89761 0.27914  -0.05090 -0.08489 268 ARG A NH2 
2051 N N   . GLY A 296 ? 2.14463 1.70929 1.94518 0.19052  -0.06342 -0.10586 269 GLY A N   
2052 C CA  . GLY A 296 ? 2.24427 1.77217 2.00442 0.15190  -0.06874 -0.09514 269 GLY A CA  
2053 C C   . GLY A 296 ? 2.16778 1.71797 1.92732 0.14219  -0.08355 -0.06689 269 GLY A C   
2054 O O   . GLY A 296 ? 2.00023 1.49851 1.72329 0.12362  -0.09201 -0.04954 269 GLY A O   
2055 N N   . VAL A 297 ? 2.10564 1.72922 1.90094 0.15197  -0.08570 -0.06252 270 VAL A N   
2056 C CA  . VAL A 297 ? 2.18383 1.83204 1.97908 0.14315  -0.09982 -0.04057 270 VAL A CA  
2057 C C   . VAL A 297 ? 2.10324 1.76805 1.87595 0.10300  -0.09137 -0.04337 270 VAL A C   
2058 O O   . VAL A 297 ? 2.00848 1.71225 1.79412 0.09168  -0.07770 -0.06062 270 VAL A O   
2059 C CB  . VAL A 297 ? 2.07310 1.79131 1.91818 0.16550  -0.10407 -0.03844 270 VAL A CB  
2060 C CG1 . VAL A 297 ? 2.00279 1.74707 1.84504 0.15211  -0.11848 -0.02124 270 VAL A CG1 
2061 C CG2 . VAL A 297 ? 1.86411 1.57516 1.74033 0.20627  -0.11168 -0.03700 270 VAL A CG2 
2062 N N   . LYS A 298 ? 2.11821 1.75526 1.85668 0.08232  -0.09946 -0.02624 271 LYS A N   
2063 C CA  . LYS A 298 ? 1.94150 1.60076 1.66338 0.04543  -0.08919 -0.03001 271 LYS A CA  
2064 C C   . LYS A 298 ? 1.87593 1.60743 1.63191 0.04890  -0.08888 -0.03329 271 LYS A C   
2065 O O   . LYS A 298 ? 1.92653 1.67100 1.68509 0.05667  -0.10202 -0.02007 271 LYS A O   
2066 C CB  . LYS A 298 ? 2.32090 1.93090 1.99226 0.02211  -0.09482 -0.01040 271 LYS A CB  
2067 C CG  . LYS A 298 ? 2.72739 2.25459 2.35981 0.01268  -0.09329 -0.00472 271 LYS A CG  
2068 C CD  . LYS A 298 ? 3.07155 2.55133 2.64703 -0.01785 -0.09466 0.01716  271 LYS A CD  
2069 C CE  . LYS A 298 ? 2.99327 2.38089 2.52757 -0.03106 -0.09162 0.02494  271 LYS A CE  
2070 N NZ  . LYS A 298 ? 3.16426 2.50247 2.63632 -0.06606 -0.08947 0.04919  271 LYS A NZ  
2071 N N   . ILE A 299 ? 1.93893 1.71491 1.71961 0.04278  -0.07561 -0.05075 272 ILE A N   
2072 C CA  . ILE A 299 ? 1.95509 1.79119 1.77030 0.04857  -0.07384 -0.05412 272 ILE A CA  
2073 C C   . ILE A 299 ? 2.03816 1.90075 1.85097 0.02222  -0.06290 -0.06348 272 ILE A C   
2074 O O   . ILE A 299 ? 2.00667 1.86824 1.81371 0.00673  -0.05360 -0.07527 272 ILE A O   
2075 C CB  . ILE A 299 ? 1.71450 1.58088 1.56329 0.07042  -0.06862 -0.06303 272 ILE A CB  
2076 C CG1 . ILE A 299 ? 1.92560 1.77116 1.78301 0.09808  -0.07561 -0.05766 272 ILE A CG1 
2077 C CG2 . ILE A 299 ? 1.70755 1.62606 1.58880 0.07416  -0.06632 -0.06277 272 ILE A CG2 
2078 C CD1 . ILE A 299 ? 1.83255 1.70591 1.71677 0.11756  -0.06556 -0.06808 272 ILE A CD1 
2079 N N   . ARG A 300 ? 1.88981 1.77823 1.70980 0.01726  -0.06419 -0.06073 273 ARG A N   
2080 C CA  . ARG A 300 ? 1.77480 1.69333 1.60023 -0.00245 -0.05232 -0.07200 273 ARG A CA  
2081 C C   . ARG A 300 ? 1.68860 1.64930 1.55192 0.01123  -0.05192 -0.07618 273 ARG A C   
2082 O O   . ARG A 300 ? 1.62010 1.58350 1.48820 0.01847  -0.06016 -0.06977 273 ARG A O   
2083 C CB  . ARG A 300 ? 1.88896 1.78874 1.67750 -0.02581 -0.05007 -0.06776 273 ARG A CB  
2084 C CG  . ARG A 300 ? 2.11979 1.97164 1.86594 -0.04575 -0.04715 -0.06118 273 ARG A CG  
2085 C CD  . ARG A 300 ? 2.12792 1.96098 1.82953 -0.07058 -0.04332 -0.05357 273 ARG A CD  
2086 N NE  . ARG A 300 ? 1.86837 1.69241 1.55450 -0.05714 -0.06124 -0.03945 273 ARG A NE  
2087 C CZ  . ARG A 300 ? 2.16506 1.97415 1.80604 -0.07455 -0.06327 -0.03106 273 ARG A CZ  
2088 N NH1 . ARG A 300 ? 2.40499 2.20490 2.01032 -0.10711 -0.04438 -0.03450 273 ARG A NH1 
2089 N NH2 . ARG A 300 ? 2.22833 2.03524 1.85894 -0.06077 -0.08449 -0.01975 273 ARG A NH2 
2090 N N   . LEU A 301 ? 1.78648 1.77824 1.67602 0.01390  -0.04400 -0.08631 274 LEU A N   
2091 C CA  . LEU A 301 ? 1.70662 1.72941 1.63051 0.02790  -0.04305 -0.08748 274 LEU A CA  
2092 C C   . LEU A 301 ? 1.75508 1.80244 1.69277 0.01779  -0.03365 -0.09998 274 LEU A C   
2093 O O   . LEU A 301 ? 1.88141 1.94539 1.82413 0.00934  -0.02728 -0.10972 274 LEU A O   
2094 C CB  . LEU A 301 ? 1.35732 1.39385 1.29794 0.04390  -0.04335 -0.08569 274 LEU A CB  
2095 C CG  . LEU A 301 ? 1.53741 1.55382 1.46755 0.05594  -0.04776 -0.07873 274 LEU A CG  
2096 C CD1 . LEU A 301 ? 1.59205 1.62462 1.52995 0.06806  -0.04475 -0.08013 274 LEU A CD1 
2097 C CD2 . LEU A 301 ? 1.75814 1.77071 1.69901 0.06637  -0.05352 -0.06857 274 LEU A CD2 
2098 N N   . LEU A 302 ? 1.63586 1.68778 1.58294 0.01868  -0.03267 -0.10227 275 LEU A N   
2099 C CA  . LEU A 302 ? 1.59383 1.66682 1.55824 0.01369  -0.02175 -0.11743 275 LEU A CA  
2100 C C   . LEU A 302 ? 1.59375 1.67803 1.59407 0.03289  -0.02316 -0.11545 275 LEU A C   
2101 O O   . LEU A 302 ? 1.50724 1.58039 1.51176 0.03527  -0.02649 -0.11290 275 LEU A O   
2102 C CB  . LEU A 302 ? 1.57596 1.63732 1.51429 -0.00350 -0.01741 -0.12530 275 LEU A CB  
2103 C CG  . LEU A 302 ? 1.39364 1.47534 1.34725 -0.00908 -0.00184 -0.14644 275 LEU A CG  
2104 C CD1 . LEU A 302 ? 1.53258 1.64261 1.50170 -0.01500 0.01103  -0.15760 275 LEU A CD1 
2105 C CD2 . LEU A 302 ? 1.53390 1.60122 1.44942 -0.02842 0.00245  -0.15488 275 LEU A CD2 
2106 N N   . VAL A 303 ? 1.63967 1.74480 1.66468 0.04516  -0.02198 -0.11572 276 VAL A N   
2107 C CA  . VAL A 303 ? 1.44801 1.55602 1.50043 0.06450  -0.02473 -0.10722 276 VAL A CA  
2108 C C   . VAL A 303 ? 1.68059 1.80852 1.76411 0.07359  -0.01875 -0.11943 276 VAL A C   
2109 O O   . VAL A 303 ? 1.85680 2.00671 1.94565 0.06555  -0.01178 -0.13543 276 VAL A O   
2110 C CB  . VAL A 303 ? 1.06278 1.17442 1.11230 0.07642  -0.03225 -0.09126 276 VAL A CB  
2111 C CG1 . VAL A 303 ? 1.29815 1.39218 1.32314 0.07116  -0.03565 -0.08307 276 VAL A CG1 
2112 C CG2 . VAL A 303 ? 1.55286 1.69026 1.60487 0.07708  -0.03493 -0.09756 276 VAL A CG2 
2113 N N   . GLY A 304 ? 1.48347 1.60287 1.59001 0.09076  -0.02048 -0.11148 277 GLY A N   
2114 C CA  . GLY A 304 ? 1.47735 1.61104 1.61840 0.10674  -0.01719 -0.12061 277 GLY A CA  
2115 C C   . GLY A 304 ? 1.67650 1.83967 1.83179 0.12247  -0.02755 -0.11178 277 GLY A C   
2116 O O   . GLY A 304 ? 1.79212 1.95474 1.92836 0.12427  -0.03720 -0.09463 277 GLY A O   
2117 N N   . ASN A 305 ? 1.76949 1.96259 1.95971 0.13439  -0.02576 -0.12583 278 ASN A N   
2118 C CA  . ASN A 305 ? 1.75498 1.98518 1.96427 0.15019  -0.03989 -0.11945 278 ASN A CA  
2119 C C   . ASN A 305 ? 1.94287 2.15194 2.14957 0.17347  -0.05420 -0.09100 278 ASN A C   
2120 O O   . ASN A 305 ? 2.17378 2.34105 2.37695 0.17934  -0.04987 -0.07918 278 ASN A O   
2121 C CB  . ASN A 305 ? 1.79652 2.06922 2.05498 0.16212  -0.03548 -0.14114 278 ASN A CB  
2122 C CG  . ASN A 305 ? 2.29164 2.54299 2.58322 0.18839  -0.03173 -0.14216 278 ASN A CG  
2123 O OD1 . ASN A 305 ? 2.55173 2.75469 2.82757 0.18488  -0.02350 -0.13880 278 ASN A OD1 
2124 N ND2 . ASN A 305 ? 2.12066 2.40788 2.46120 0.21533  -0.03886 -0.14786 278 ASN A ND2 
2125 N N   . TRP A 306 ? 1.89994 2.13813 2.10546 0.18402  -0.07149 -0.07994 279 TRP A N   
2126 C CA  . TRP A 306 ? 2.07219 2.29241 2.26077 0.20234  -0.08601 -0.04962 279 TRP A CA  
2127 C C   . TRP A 306 ? 2.14501 2.39876 2.36612 0.23107  -0.10571 -0.04333 279 TRP A C   
2128 O O   . TRP A 306 ? 2.24438 2.54716 2.50293 0.23406  -0.10930 -0.06482 279 TRP A O   
2129 C CB  . TRP A 306 ? 2.09720 2.31748 2.23854 0.18752  -0.09102 -0.03930 279 TRP A CB  
2130 C CG  . TRP A 306 ? 2.15863 2.42647 2.29776 0.17951  -0.10303 -0.05359 279 TRP A CG  
2131 C CD1 . TRP A 306 ? 2.39394 2.68962 2.52140 0.18999  -0.12422 -0.04347 279 TRP A CD1 
2132 C CD2 . TRP A 306 ? 2.03437 2.32603 2.18067 0.15603  -0.09501 -0.08082 279 TRP A CD2 
2133 N NE1 . TRP A 306 ? 2.57604 2.91365 2.70737 0.17327  -0.13041 -0.06588 279 TRP A NE1 
2134 C CE2 . TRP A 306 ? 2.33111 2.66464 2.47452 0.15157  -0.11126 -0.08795 279 TRP A CE2 
2135 C CE3 . TRP A 306 ? 1.90987 2.18973 2.06048 0.13630  -0.07611 -0.09885 279 TRP A CE3 
2136 C CZ2 . TRP A 306 ? 2.26982 2.63079 2.41877 0.12600  -0.10692 -0.11280 279 TRP A CZ2 
2137 C CZ3 . TRP A 306 ? 2.18277 2.48760 2.33337 0.11260  -0.07154 -0.11991 279 TRP A CZ3 
2138 C CH2 . TRP A 306 ? 2.35068 2.69436 2.50265 0.10662  -0.08575 -0.12694 279 TRP A CH2 
2139 N N   . ASP A 307 ? 2.16823 2.39672 2.37548 0.25214  -0.11878 -0.01225 280 ASP A N   
2140 C CA  . ASP A 307 ? 2.32274 2.57779 2.55529 0.28413  -0.14319 0.00100  280 ASP A CA  
2141 C C   . ASP A 307 ? 2.33145 2.63521 2.54051 0.27954  -0.16520 0.00360  280 ASP A C   
2142 O O   . ASP A 307 ? 2.17862 2.46741 2.33363 0.26344  -0.16509 0.01563  280 ASP A O   
2143 C CB  . ASP A 307 ? 2.46081 2.66056 2.67921 0.30718  -0.14934 0.03774  280 ASP A CB  
2144 C CG  . ASP A 307 ? 2.59385 2.81318 2.84202 0.34645  -0.17698 0.05448  280 ASP A CG  
2145 O OD1 . ASP A 307 ? 2.49643 2.77691 2.79194 0.35799  -0.18831 0.03181  280 ASP A OD1 
2146 O OD2 . ASP A 307 ? 2.69967 2.87428 2.92494 0.36571  -0.18770 0.09147  280 ASP A OD2 
2147 N N   . LYS A 308 ? 2.34735 2.71274 2.59964 0.29316  -0.18354 -0.01067 281 LYS A N   
2148 C CA  . LYS A 308 ? 2.13844 2.55576 2.37289 0.28795  -0.20862 -0.01148 281 LYS A CA  
2149 C C   . LYS A 308 ? 2.14434 2.54392 2.33357 0.30810  -0.23377 0.02689  281 LYS A C   
2150 O O   . LYS A 308 ? 1.97323 2.39942 2.12242 0.29720  -0.25105 0.02873  281 LYS A O   
2151 C CB  . LYS A 308 ? 2.25611 2.75122 2.55770 0.29848  -0.22395 -0.03582 281 LYS A CB  
2152 C CG  . LYS A 308 ? 2.04689 2.56333 2.39064 0.27632  -0.19603 -0.07335 281 LYS A CG  
2153 C CD  . LYS A 308 ? 2.42856 3.02912 2.84708 0.28741  -0.20771 -0.09774 281 LYS A CD  
2154 C CE  . LYS A 308 ? 2.03371 2.65352 2.48886 0.26296  -0.17465 -0.13386 281 LYS A CE  
2155 N NZ  . LYS A 308 ? 1.60136 2.31114 2.13662 0.27170  -0.18093 -0.16033 281 LYS A NZ  
2156 N N   . ASN A 309 ? 2.38663 2.73801 2.57677 0.33529  -0.23541 0.05728  282 ASN A N   
2157 C CA  . ASN A 309 ? 2.47375 2.79845 2.61220 0.35245  -0.25642 0.09938  282 ASN A CA  
2158 C C   . ASN A 309 ? 2.50299 2.77776 2.56916 0.32661  -0.23608 0.11523  282 ASN A C   
2159 O O   . ASN A 309 ? 2.68563 2.95067 2.69377 0.33016  -0.25038 0.14408  282 ASN A O   
2160 C CB  . ASN A 309 ? 2.60107 2.88369 2.76651 0.39035  -0.26451 0.12861  282 ASN A CB  
2161 C CG  . ASN A 309 ? 2.73649 3.07242 2.97854 0.42391  -0.28673 0.11466  282 ASN A CG  
2162 O OD1 . ASN A 309 ? 2.79310 3.11153 3.09130 0.44030  -0.27271 0.10217  282 ASN A OD1 
2163 N ND2 . ASN A 309 ? 2.81934 3.22429 3.06628 0.43428  -0.32148 0.11410  282 ASN A ND2 
2164 N N   . ASP A 310 ? 2.18042 2.42703 2.24881 0.30141  -0.20343 0.09693  283 ASP A N   
2165 C CA  . ASP A 310 ? 2.01845 2.22556 2.03109 0.27838  -0.18202 0.10825  283 ASP A CA  
2166 C C   . ASP A 310 ? 1.99755 2.24054 1.97283 0.25625  -0.18428 0.08866  283 ASP A C   
2167 O O   . ASP A 310 ? 2.05090 2.31901 2.04842 0.23872  -0.17665 0.05504  283 ASP A O   
2168 C CB  . ASP A 310 ? 1.91394 2.08359 1.94925 0.26232  -0.15115 0.09512  283 ASP A CB  
2169 C CG  . ASP A 310 ? 2.21956 2.35300 2.20997 0.24219  -0.12932 0.10870  283 ASP A CG  
2170 O OD1 . ASP A 310 ? 2.38487 2.51337 2.32471 0.24299  -0.13426 0.13271  283 ASP A OD1 
2171 O OD2 . ASP A 310 ? 2.28638 2.40028 2.29233 0.22534  -0.10720 0.09459  283 ASP A OD2 
2172 N N   . VAL A 311 ? 2.08777 2.32860 2.00201 0.25579  -0.19343 0.10940  284 VAL A N   
2173 C CA  . VAL A 311 ? 1.89714 2.16858 1.77168 0.23626  -0.19668 0.08805  284 VAL A CA  
2174 C C   . VAL A 311 ? 1.81307 2.05957 1.67249 0.21133  -0.16412 0.07033  284 VAL A C   
2175 O O   . VAL A 311 ? 1.91580 2.18149 1.76609 0.19359  -0.16137 0.04081  284 VAL A O   
2176 C CB  . VAL A 311 ? 1.76510 2.04277 1.57253 0.24355  -0.21621 0.11339  284 VAL A CB  
2177 C CG1 . VAL A 311 ? 2.05998 2.37299 1.88606 0.27004  -0.25608 0.12776  284 VAL A CG1 
2178 C CG2 . VAL A 311 ? 1.54925 1.77417 1.31292 0.24487  -0.19617 0.14989  284 VAL A CG2 
2179 N N   . TYR A 312 ? 1.73461 1.93803 1.59372 0.20960  -0.14015 0.08746  285 TYR A N   
2180 C CA  . TYR A 312 ? 1.82814 2.01429 1.68208 0.18969  -0.11205 0.07123  285 TYR A CA  
2181 C C   . TYR A 312 ? 1.71263 1.90695 1.61301 0.17982  -0.10707 0.04035  285 TYR A C   
2182 O O   . TYR A 312 ? 1.73538 1.93280 1.62638 0.16437  -0.09756 0.01728  285 TYR A O   
2183 C CB  . TYR A 312 ? 1.83273 1.97941 1.68450 0.18841  -0.08979 0.09612  285 TYR A CB  
2184 C CG  . TYR A 312 ? 1.89685 2.03187 1.69152 0.18991  -0.08518 0.12577  285 TYR A CG  
2185 C CD1 . TYR A 312 ? 1.93284 2.08883 1.67373 0.18436  -0.08728 0.11793  285 TYR A CD1 
2186 C CD2 . TYR A 312 ? 2.06680 2.16654 1.85708 0.19458  -0.07714 0.16095  285 TYR A CD2 
2187 C CE1 . TYR A 312 ? 1.87525 2.02181 1.55593 0.18376  -0.08046 0.14450  285 TYR A CE1 
2188 C CE2 . TYR A 312 ? 2.23431 2.32122 1.96597 0.19263  -0.07017 0.19102  285 TYR A CE2 
2189 C CZ  . TYR A 312 ? 2.01733 2.13000 1.69253 0.18742  -0.07138 0.18279  285 TYR A CZ  
2190 O OH  . TYR A 312 ? 2.07217 2.17326 1.68141 0.18363  -0.06192 0.21220  285 TYR A OH  
2191 N N   . SER A 313 ? 1.70980 1.90455 1.65757 0.18897  -0.11249 0.03964  286 SER A N   
2192 C CA  . SER A 313 ? 1.76352 1.96728 1.74915 0.17788  -0.10630 0.01146  286 SER A CA  
2193 C C   . SER A 313 ? 1.84577 2.08847 1.83071 0.16820  -0.11901 -0.01342 286 SER A C   
2194 O O   . SER A 313 ? 1.77446 2.01580 1.76113 0.14948  -0.10907 -0.03581 286 SER A O   
2195 C CB  . SER A 313 ? 1.79587 1.99464 1.82938 0.19081  -0.10743 0.01323  286 SER A CB  
2196 O OG  . SER A 313 ? 1.81209 1.96908 1.84660 0.19524  -0.09509 0.03350  286 SER A OG  
2197 N N   . MET A 314 ? 1.90328 2.17996 1.88495 0.17949  -0.14239 -0.00903 287 MET A N   
2198 C CA  . MET A 314 ? 1.76710 2.08553 1.75049 0.16617  -0.15602 -0.03463 287 MET A CA  
2199 C C   . MET A 314 ? 1.86164 2.16712 1.79414 0.14698  -0.14923 -0.04680 287 MET A C   
2200 O O   . MET A 314 ? 1.88020 2.19474 1.81470 0.12610  -0.14683 -0.07368 287 MET A O   
2201 C CB  . MET A 314 ? 1.90431 2.26814 1.89756 0.18397  -0.18696 -0.02651 287 MET A CB  
2202 C CG  . MET A 314 ? 2.15080 2.53547 2.20610 0.20567  -0.19500 -0.02218 287 MET A CG  
2203 S SD  . MET A 314 ? 2.28221 2.69771 2.39743 0.18677  -0.18075 -0.05973 287 MET A SD  
2204 C CE  . MET A 314 ? 2.12738 2.59692 2.23231 0.16173  -0.19833 -0.08642 287 MET A CE  
2205 N N   . ALA A 315 ? 1.87505 2.15680 1.76131 0.15306  -0.14386 -0.02815 288 ALA A N   
2206 C CA  . ALA A 315 ? 1.83740 2.10425 1.67686 0.13835  -0.13296 -0.04241 288 ALA A CA  
2207 C C   . ALA A 315 ? 1.84977 2.08572 1.70315 0.12534  -0.10969 -0.05769 288 ALA A C   
2208 O O   . ALA A 315 ? 2.15763 2.38720 1.99745 0.10941  -0.10603 -0.08224 288 ALA A O   
2209 C CB  . ALA A 315 ? 1.98652 2.23723 1.77675 0.14790  -0.12624 -0.01875 288 ALA A CB  
2210 N N   . THR A 316 ? 1.69964 1.91357 1.57900 0.13178  -0.09555 -0.04312 289 THR A N   
2211 C CA  . THR A 316 ? 1.85932 2.04766 1.75332 0.12142  -0.07861 -0.05484 289 THR A CA  
2212 C C   . THR A 316 ? 1.86442 2.06143 1.77992 0.10626  -0.08363 -0.07721 289 THR A C   
2213 O O   . THR A 316 ? 1.77810 1.95462 1.68310 0.09272  -0.07586 -0.09299 289 THR A O   
2214 C CB  . THR A 316 ? 1.87315 2.04393 1.79408 0.12889  -0.06762 -0.03697 289 THR A CB  
2215 O OG1 . THR A 316 ? 1.87609 2.04028 1.77874 0.13924  -0.06196 -0.01372 289 THR A OG1 
2216 C CG2 . THR A 316 ? 1.79705 1.94437 1.72634 0.12007  -0.05356 -0.04614 289 THR A CG2 
2217 N N   . ALA A 317 ? 1.82432 2.05103 1.77076 0.10856  -0.09553 -0.07836 290 ALA A N   
2218 C CA  . ALA A 317 ? 1.95077 2.19245 1.92137 0.09118  -0.09615 -0.09950 290 ALA A CA  
2219 C C   . ALA A 317 ? 1.80219 2.05213 1.74967 0.07194  -0.10265 -0.12077 290 ALA A C   
2220 O O   . ALA A 317 ? 2.04867 2.27723 1.99043 0.05162  -0.09334 -0.13605 290 ALA A O   
2221 C CB  . ALA A 317 ? 2.16601 2.44747 2.18058 0.10090  -0.10625 -0.09868 290 ALA A CB  
2222 N N   . ARG A 318 ? 1.59519 1.87278 1.52571 0.07672  -0.11971 -0.12182 291 ARG A N   
2223 C CA  . ARG A 318 ? 1.92361 2.20929 1.83061 0.05566  -0.12749 -0.14610 291 ARG A CA  
2224 C C   . ARG A 318 ? 1.99236 2.22881 1.85413 0.04946  -0.11353 -0.15362 291 ARG A C   
2225 O O   . ARG A 318 ? 1.95305 2.17776 1.79599 0.02841  -0.11411 -0.17750 291 ARG A O   
2226 C CB  . ARG A 318 ? 2.11589 2.44849 2.01346 0.06240  -0.15319 -0.14637 291 ARG A CB  
2227 C CG  . ARG A 318 ? 2.00466 2.39672 1.95451 0.06150  -0.17100 -0.15234 291 ARG A CG  
2228 C CD  . ARG A 318 ? 2.08073 2.52337 2.01920 0.06430  -0.20182 -0.15703 291 ARG A CD  
2229 N NE  . ARG A 318 ? 2.30143 2.74241 2.21216 0.09379  -0.21397 -0.12720 291 ARG A NE  
2230 C CZ  . ARG A 318 ? 2.42728 2.89852 2.36999 0.12031  -0.23083 -0.10514 291 ARG A CZ  
2231 N NH1 . ARG A 318 ? 2.21416 2.72666 2.22324 0.12402  -0.23696 -0.11273 291 ARG A NH1 
2232 N NH2 . ARG A 318 ? 2.45515 2.91319 2.36208 0.14401  -0.24030 -0.07462 291 ARG A NH2 
2233 N N   . SER A 319 ? 2.06459 2.27242 1.91221 0.06701  -0.10022 -0.13551 292 SER A N   
2234 C CA  . SER A 319 ? 1.86625 2.03063 1.68328 0.06525  -0.08431 -0.14401 292 SER A CA  
2235 C C   . SER A 319 ? 1.66867 1.79780 1.50187 0.05365  -0.07335 -0.15086 292 SER A C   
2236 O O   . SER A 319 ? 1.86652 1.96242 1.67938 0.04124  -0.06842 -0.16908 292 SER A O   
2237 C CB  . SER A 319 ? 1.71367 1.86862 1.51926 0.08626  -0.07218 -0.12305 292 SER A CB  
2238 O OG  . SER A 319 ? 2.07916 2.25968 1.85761 0.09490  -0.08109 -0.11387 292 SER A OG  
2239 N N   . LEU A 320 ? 1.54692 1.67880 1.41280 0.05722  -0.06997 -0.13636 293 LEU A N   
2240 C CA  . LEU A 320 ? 1.72945 1.82905 1.60335 0.04529  -0.06165 -0.13964 293 LEU A CA  
2241 C C   . LEU A 320 ? 1.93470 2.03858 1.81199 0.01805  -0.06536 -0.15757 293 LEU A C   
2242 O O   . LEU A 320 ? 2.09640 2.16188 1.96381 0.00300  -0.05819 -0.16238 293 LEU A O   
2243 C CB  . LEU A 320 ? 1.97478 2.07877 1.87691 0.05409  -0.05736 -0.12220 293 LEU A CB  
2244 C CG  . LEU A 320 ? 1.81421 1.91916 1.72141 0.07593  -0.05302 -0.10369 293 LEU A CG  
2245 C CD1 . LEU A 320 ? 1.96453 2.06928 1.89905 0.07898  -0.04974 -0.09189 293 LEU A CD1 
2246 C CD2 . LEU A 320 ? 1.94927 2.02628 1.83594 0.08416  -0.04458 -0.10452 293 LEU A CD2 
2247 N N   . ASP A 321 ? 2.04728 2.19811 1.93929 0.01084  -0.07691 -0.16632 294 ASP A N   
2248 C CA  . ASP A 321 ? 2.18401 2.35022 2.08799 -0.01867 -0.07896 -0.18520 294 ASP A CA  
2249 C C   . ASP A 321 ? 2.13915 2.26658 2.00883 -0.04005 -0.07753 -0.20488 294 ASP A C   
2250 O O   . ASP A 321 ? 2.43460 2.53851 2.30253 -0.06776 -0.07026 -0.21515 294 ASP A O   
2251 C CB  . ASP A 321 ? 2.22120 2.45614 2.15618 -0.01782 -0.09493 -0.19118 294 ASP A CB  
2252 C CG  . ASP A 321 ? 2.37384 2.64082 2.33873 -0.04807 -0.09378 -0.20976 294 ASP A CG  
2253 O OD1 . ASP A 321 ? 1.99498 2.26679 1.98535 -0.05327 -0.08105 -0.20575 294 ASP A OD1 
2254 O OD2 . ASP A 321 ? 2.57152 2.86132 2.53414 -0.06884 -0.10451 -0.23010 294 ASP A OD2 
2255 N N   . ALA A 322 ? 1.92477 2.04136 1.76401 -0.02902 -0.08259 -0.21106 295 ALA A N   
2256 C CA  . ALA A 322 ? 2.02263 2.09447 1.82680 -0.04632 -0.07973 -0.23339 295 ALA A CA  
2257 C C   . ALA A 322 ? 1.80644 1.80724 1.59125 -0.03815 -0.06448 -0.22693 295 ALA A C   
2258 O O   . ALA A 322 ? 1.93237 1.88211 1.69131 -0.05277 -0.05998 -0.24446 295 ALA A O   
2259 C CB  . ALA A 322 ? 1.99663 2.08463 1.77084 -0.03732 -0.08936 -0.24637 295 ALA A CB  
2260 N N   . LEU A 323 ? 1.82369 1.81932 1.62201 -0.01490 -0.05807 -0.20299 296 LEU A N   
2261 C CA  . LEU A 323 ? 1.97717 1.91417 1.76414 -0.00412 -0.04810 -0.19451 296 LEU A CA  
2262 C C   . LEU A 323 ? 2.27346 2.18395 2.06677 -0.02208 -0.04499 -0.18485 296 LEU A C   
2263 O O   . LEU A 323 ? 2.28774 2.13747 2.06159 -0.02391 -0.04064 -0.18276 296 LEU A O   
2264 C CB  . LEU A 323 ? 1.98191 1.93144 1.78090 0.02830  -0.04414 -0.17527 296 LEU A CB  
2265 C CG  . LEU A 323 ? 2.13500 2.11016 1.92233 0.04566  -0.04285 -0.18026 296 LEU A CG  
2266 C CD1 . LEU A 323 ? 1.81848 1.80842 1.62312 0.07151  -0.03579 -0.15938 296 LEU A CD1 
2267 C CD2 . LEU A 323 ? 2.07240 2.00927 1.82643 0.04540  -0.03706 -0.20429 296 LEU A CD2 
2268 N N   . CYS A 324 ? 2.36372 2.31704 2.18181 -0.03415 -0.04660 -0.17860 297 CYS A N   
2269 C CA  . CYS A 324 ? 2.38509 2.31744 2.20249 -0.05632 -0.04041 -0.17192 297 CYS A CA  
2270 C C   . CYS A 324 ? 2.31345 2.20851 2.10935 -0.09084 -0.03662 -0.18784 297 CYS A C   
2271 O O   . CYS A 324 ? 2.36462 2.20749 2.13941 -0.10656 -0.02996 -0.17915 297 CYS A O   
2272 C CB  . CYS A 324 ? 2.45853 2.45049 2.30933 -0.06252 -0.03930 -0.16863 297 CYS A CB  
2273 S SG  . CYS A 324 ? 2.71329 2.72776 2.58546 -0.03055 -0.04018 -0.14779 297 CYS A SG  
2274 N N   . VAL A 325 ? 2.19650 2.11541 1.99456 -0.10495 -0.04174 -0.21048 298 VAL A N   
2275 C CA  . VAL A 325 ? 2.22993 2.11642 2.01145 -0.14367 -0.03799 -0.22921 298 VAL A CA  
2276 C C   . VAL A 325 ? 2.08763 1.89256 1.83014 -0.13979 -0.03617 -0.23698 298 VAL A C   
2277 O O   . VAL A 325 ? 2.27792 2.02932 1.99947 -0.17140 -0.03047 -0.24699 298 VAL A O   
2278 C CB  . VAL A 325 ? 2.27407 2.22636 2.07802 -0.16426 -0.04708 -0.25382 298 VAL A CB  
2279 C CG1 . VAL A 325 ? 2.68567 2.71705 2.53524 -0.16687 -0.04784 -0.24793 298 VAL A CG1 
2280 C CG2 . VAL A 325 ? 1.79025 1.76182 1.58428 -0.13930 -0.05980 -0.26459 298 VAL A CG2 
2281 N N   . GLN A 326 ? 2.10942 1.90173 1.84316 -0.10242 -0.03889 -0.23352 299 GLN A N   
2282 C CA  . GLN A 326 ? 2.16492 1.88318 1.86737 -0.09174 -0.03527 -0.24403 299 GLN A CA  
2283 C C   . GLN A 326 ? 2.17399 1.83103 1.86726 -0.06994 -0.03129 -0.21985 299 GLN A C   
2284 O O   . GLN A 326 ? 2.18852 1.76588 1.85584 -0.07704 -0.02782 -0.22258 299 GLN A O   
2285 C CB  . GLN A 326 ? 2.28831 2.03232 1.98627 -0.06397 -0.03760 -0.25863 299 GLN A CB  
2286 C CG  . GLN A 326 ? 2.51098 2.18418 2.18013 -0.04871 -0.03052 -0.27542 299 GLN A CG  
2287 C CD  . GLN A 326 ? 2.44352 2.06262 2.08550 -0.08373 -0.02938 -0.30450 299 GLN A CD  
2288 O OE1 . GLN A 326 ? 2.24972 1.90236 1.89543 -0.12022 -0.03545 -0.31824 299 GLN A OE1 
2289 N NE2 . GLN A 326 ? 2.58767 2.12270 2.20576 -0.07273 -0.02174 -0.31535 299 GLN A NE2 
2290 N N   . ASN A 327 ? 2.15183 1.84256 1.86589 -0.04366 -0.03354 -0.19622 300 ASN A N   
2291 C CA  . ASN A 327 ? 2.15945 1.80635 1.86949 -0.02131 -0.03482 -0.17231 300 ASN A CA  
2292 C C   . ASN A 327 ? 2.21561 1.87953 1.93099 -0.03665 -0.03653 -0.14956 300 ASN A C   
2293 O O   . ASN A 327 ? 2.20256 1.91198 1.92894 -0.06256 -0.03360 -0.15427 300 ASN A O   
2294 C CB  . ASN A 327 ? 1.97162 1.64466 1.70190 0.02116  -0.03584 -0.16716 300 ASN A CB  
2295 C CG  . ASN A 327 ? 2.20457 1.86610 1.92593 0.03600  -0.02976 -0.19245 300 ASN A CG  
2296 O OD1 . ASN A 327 ? 2.06225 1.77080 1.78499 0.03085  -0.02796 -0.20847 300 ASN A OD1 
2297 N ND2 . ASN A 327 ? 2.38424 1.98218 2.09433 0.05589  -0.02696 -0.19655 300 ASN A ND2 
2298 N N   . ASP A 328 ? 2.24246 1.87209 1.95037 -0.01934 -0.04176 -0.12613 301 ASP A N   
2299 C CA  . ASP A 328 ? 2.20342 1.84152 1.90564 -0.03374 -0.04356 -0.10507 301 ASP A CA  
2300 C C   . ASP A 328 ? 2.27452 1.98553 2.01116 -0.01597 -0.04645 -0.09978 301 ASP A C   
2301 O O   . ASP A 328 ? 2.29623 2.01084 2.04219 0.00899  -0.05473 -0.08444 301 ASP A O   
2302 C CB  . ASP A 328 ? 2.28320 1.85062 1.95553 -0.02426 -0.05201 -0.08130 301 ASP A CB  
2303 C CG  . ASP A 328 ? 2.61891 2.17397 2.26291 -0.05372 -0.05043 -0.06273 301 ASP A CG  
2304 O OD1 . ASP A 328 ? 2.57174 2.18808 2.23181 -0.06624 -0.04519 -0.06491 301 ASP A OD1 
2305 O OD2 . ASP A 328 ? 2.98817 2.46908 2.59110 -0.06418 -0.05334 -0.04593 301 ASP A OD2 
2306 N N   . LEU A 329 ? 2.30358 2.07331 2.06168 -0.02957 -0.04062 -0.11324 302 LEU A N   
2307 C CA  . LEU A 329 ? 2.22236 2.05500 2.01279 -0.01547 -0.04192 -0.10967 302 LEU A CA  
2308 C C   . LEU A 329 ? 2.28453 2.15838 2.08640 -0.04128 -0.03495 -0.11616 302 LEU A C   
2309 O O   . LEU A 329 ? 2.36558 2.24834 2.16697 -0.06499 -0.02980 -0.13114 302 LEU A O   
2310 C CB  . LEU A 329 ? 1.83193 1.69924 1.64402 0.00666  -0.04294 -0.11931 302 LEU A CB  
2311 C CG  . LEU A 329 ? 1.86006 1.78601 1.70401 0.01960  -0.04356 -0.11474 302 LEU A CG  
2312 C CD1 . LEU A 329 ? 1.71416 1.63948 1.56944 0.03693  -0.04699 -0.09802 302 LEU A CD1 
2313 C CD2 . LEU A 329 ? 1.77092 1.72483 1.62344 0.03415  -0.04351 -0.12299 302 LEU A CD2 
2314 N N   . SER A 330 ? 2.08581 1.98704 1.90095 -0.03698 -0.03436 -0.10753 303 SER A N   
2315 C CA  . SER A 330 ? 2.11575 2.06004 1.94774 -0.05583 -0.02523 -0.11609 303 SER A CA  
2316 C C   . SER A 330 ? 1.96701 1.95796 1.83419 -0.03409 -0.02751 -0.11557 303 SER A C   
2317 O O   . SER A 330 ? 1.94666 1.92911 1.81601 -0.01388 -0.03400 -0.10409 303 SER A O   
2318 C CB  . SER A 330 ? 2.27483 2.19451 2.07731 -0.07987 -0.01726 -0.10892 303 SER A CB  
2319 O OG  . SER A 330 ? 2.16940 2.04307 1.93859 -0.10558 -0.01252 -0.10827 303 SER A OG  
2320 N N   . VAL A 331 ? 1.84879 1.88878 1.74653 -0.03835 -0.02271 -0.12815 304 VAL A N   
2321 C CA  . VAL A 331 ? 1.70904 1.78703 1.64120 -0.01706 -0.02485 -0.12749 304 VAL A CA  
2322 C C   . VAL A 331 ? 1.83203 1.94804 1.78857 -0.02868 -0.01393 -0.14040 304 VAL A C   
2323 O O   . VAL A 331 ? 2.05913 2.20164 2.02729 -0.04639 -0.00836 -0.15388 304 VAL A O   
2324 C CB  . VAL A 331 ? 1.50348 1.60507 1.45348 0.00135  -0.03400 -0.12799 304 VAL A CB  
2325 C CG1 . VAL A 331 ? 1.48723 1.62242 1.47129 0.02128  -0.03590 -0.12468 304 VAL A CG1 
2326 C CG2 . VAL A 331 ? 1.76547 1.83403 1.69372 0.01521  -0.03986 -0.11801 304 VAL A CG2 
2327 N N   . LYS A 332 ? 1.69949 1.82032 1.66653 -0.01961 -0.00987 -0.13907 305 LYS A N   
2328 C CA  . LYS A 332 ? 1.60291 1.76089 1.59885 -0.02341 0.00245  -0.15451 305 LYS A CA  
2329 C C   . LYS A 332 ? 1.59743 1.76840 1.62561 0.00424  -0.00206 -0.15239 305 LYS A C   
2330 O O   . LYS A 332 ? 1.71191 1.85711 1.73130 0.01803  -0.01060 -0.13848 305 LYS A O   
2331 C CB  . LYS A 332 ? 1.76193 1.90433 1.72917 -0.04654 0.01726  -0.16026 305 LYS A CB  
2332 C CG  . LYS A 332 ? 1.80679 1.93812 1.74443 -0.07880 0.02669  -0.16272 305 LYS A CG  
2333 C CD  . LYS A 332 ? 1.74607 1.87294 1.65628 -0.10369 0.04586  -0.16997 305 LYS A CD  
2334 C CE  . LYS A 332 ? 1.83698 1.95324 1.71897 -0.14022 0.05899  -0.17106 305 LYS A CE  
2335 N NZ  . LYS A 332 ? 1.66647 1.78339 1.51796 -0.16779 0.08208  -0.17822 305 LYS A NZ  
2336 N N   . VAL A 333 ? 1.65245 1.86370 1.72136 0.01213  0.00432  -0.16645 306 VAL A N   
2337 C CA  . VAL A 333 ? 1.49978 1.71845 1.60226 0.03989  0.00004  -0.16415 306 VAL A CA  
2338 C C   . VAL A 333 ? 1.52459 1.75371 1.64592 0.03881  0.01692  -0.18384 306 VAL A C   
2339 O O   . VAL A 333 ? 1.66626 1.92006 1.79044 0.02046  0.03279  -0.20227 306 VAL A O   
2340 C CB  . VAL A 333 ? 1.45247 1.70721 1.59057 0.06005  -0.01243 -0.16101 306 VAL A CB  
2341 C CG1 . VAL A 333 ? 1.70723 1.94903 1.81918 0.06073  -0.02756 -0.14444 306 VAL A CG1 
2342 C CG2 . VAL A 333 ? 1.71697 2.02511 1.88813 0.05073  -0.00528 -0.18188 306 VAL A CG2 
2343 N N   . PHE A 334 ? 1.58229 1.79066 1.71515 0.05660  0.01563  -0.18135 307 PHE A N   
2344 C CA  . PHE A 334 ? 1.62857 1.84058 1.78114 0.06022  0.03148  -0.20322 307 PHE A CA  
2345 C C   . PHE A 334 ? 1.71775 1.93100 1.91580 0.09306  0.02566  -0.20086 307 PHE A C   
2346 O O   . PHE A 334 ? 1.97364 2.16933 2.17292 0.10859  0.00952  -0.17738 307 PHE A O   
2347 C CB  . PHE A 334 ? 1.80674 1.97954 1.92035 0.04429  0.03662  -0.20688 307 PHE A CB  
2348 C CG  . PHE A 334 ? 1.84560 1.98140 1.95186 0.05400  0.02176  -0.18751 307 PHE A CG  
2349 C CD1 . PHE A 334 ? 1.87170 1.98958 2.00498 0.07123  0.02245  -0.19095 307 PHE A CD1 
2350 C CD2 . PHE A 334 ? 1.52795 1.64621 1.60286 0.04506  0.00888  -0.16707 307 PHE A CD2 
2351 C CE1 . PHE A 334 ? 1.66487 1.75096 1.79361 0.07476  0.01162  -0.17336 307 PHE A CE1 
2352 C CE2 . PHE A 334 ? 1.42181 1.51535 1.49676 0.05203  -0.00172 -0.15132 307 PHE A CE2 
2353 C CZ  . PHE A 334 ? 1.50216 1.58096 1.60365 0.06444  0.00025  -0.15406 307 PHE A CZ  
2354 N N   . THR A 335 ? 1.32937 1.56129 1.56336 0.10400  0.04039  -0.22516 308 THR A N   
2355 C CA  . THR A 335 ? 1.57661 1.80423 1.85694 0.13863  0.03558  -0.22430 308 THR A CA  
2356 C C   . THR A 335 ? 1.84260 2.02817 2.12449 0.14333  0.04780  -0.24010 308 THR A C   
2357 O O   . THR A 335 ? 2.04781 2.21155 2.36220 0.17153  0.04321  -0.23594 308 THR A O   
2358 C CB  . THR A 335 ? 1.64983 1.93706 1.98598 0.15674  0.04020  -0.24149 308 THR A CB  
2359 O OG1 . THR A 335 ? 2.08157 2.39577 2.42276 0.13904  0.06715  -0.27553 308 THR A OG1 
2360 C CG2 . THR A 335 ? 1.68519 2.01478 2.02393 0.15223  0.02382  -0.22682 308 THR A CG2 
2361 N N   . ILE A 336 ? 1.75378 1.92394 1.99837 0.11596  0.06190  -0.25777 309 ILE A N   
2362 C CA  . ILE A 336 ? 1.63115 1.76316 1.87295 0.11591  0.07363  -0.27897 309 ILE A CA  
2363 C C   . ILE A 336 ? 1.60950 1.68890 1.83661 0.11667  0.05765  -0.25606 309 ILE A C   
2364 O O   . ILE A 336 ? 1.76038 1.83530 1.96809 0.11062  0.04122  -0.22648 309 ILE A O   
2365 C CB  . ILE A 336 ? 1.46810 1.60402 1.66646 0.08371  0.09159  -0.30506 309 ILE A CB  
2366 C CG1 . ILE A 336 ? 1.41974 1.54422 1.56235 0.05590  0.07758  -0.28240 309 ILE A CG1 
2367 C CG2 . ILE A 336 ? 2.05888 2.24847 2.27516 0.08019  0.11359  -0.32970 309 ILE A CG2 
2368 C CD1 . ILE A 336 ? 1.66594 1.79211 1.75608 0.02397  0.09063  -0.30043 309 ILE A CD1 
2369 N N   . GLN A 337 ? 1.46550 1.50490 1.70380 0.12277  0.06478  -0.27247 310 GLN A N   
2370 C CA  . GLN A 337 ? 1.66806 1.65720 1.89469 0.11639  0.05359  -0.25601 310 GLN A CA  
2371 C C   . GLN A 337 ? 1.71968 1.70620 1.89749 0.08163  0.04921  -0.25826 310 GLN A C   
2372 O O   . GLN A 337 ? 1.75660 1.73553 1.91192 0.06351  0.05934  -0.28774 310 GLN A O   
2373 C CB  . GLN A 337 ? 1.56358 1.50625 1.81587 0.12920  0.06360  -0.27707 310 GLN A CB  
2374 C CG  . GLN A 337 ? 1.53243 1.46356 1.83371 0.16862  0.06126  -0.26475 310 GLN A CG  
2375 C CD  . GLN A 337 ? 2.03644 1.90928 2.36208 0.18226  0.07170  -0.28574 310 GLN A CD  
2376 O OE1 . GLN A 337 ? 2.10189 1.95942 2.41587 0.16679  0.08749  -0.32411 310 GLN A OE1 
2377 N NE2 . GLN A 337 ? 2.47818 2.31361 2.83343 0.21069  0.06273  -0.26055 310 GLN A NE2 
2378 N N   . ASN A 338 ? 1.39475 1.38878 1.55498 0.07363  0.03328  -0.22774 311 ASN A N   
2379 C CA  . ASN A 338 ? 1.49191 1.48764 1.61134 0.04639  0.02449  -0.22499 311 ASN A CA  
2380 C C   . ASN A 338 ? 1.61009 1.59095 1.73435 0.04461  0.00951  -0.19665 311 ASN A C   
2381 O O   . ASN A 338 ? 1.78651 1.77839 1.91997 0.05749  0.00335  -0.17035 311 ASN A O   
2382 C CB  . ASN A 338 ? 1.36919 1.39877 1.46022 0.03754  0.02359  -0.21998 311 ASN A CB  
2383 C CG  . ASN A 338 ? 1.53252 1.55947 1.57906 0.01326  0.01253  -0.21608 311 ASN A CG  
2384 O OD1 . ASN A 338 ? 1.82197 1.83181 1.85424 -0.00108 0.00871  -0.22898 311 ASN A OD1 
2385 N ND2 . ASN A 338 ? 1.42126 1.46379 1.44578 0.00899  0.00548  -0.19862 311 ASN A ND2 
2386 N N   . ASN A 339 ? 1.51310 1.47264 1.63155 0.02693  0.00463  -0.20415 312 ASN A N   
2387 C CA  . ASN A 339 ? 1.67304 1.62591 1.80116 0.02038  -0.00678 -0.18109 312 ASN A CA  
2388 C C   . ASN A 339 ? 1.68213 1.66088 1.78529 0.00606  -0.02136 -0.17164 312 ASN A C   
2389 O O   . ASN A 339 ? 1.80101 1.78350 1.91629 -0.00098 -0.03046 -0.15694 312 ASN A O   
2390 C CB  . ASN A 339 ? 1.58823 1.50637 1.73269 0.00680  -0.00491 -0.19494 312 ASN A CB  
2391 C CG  . ASN A 339 ? 1.65054 1.53133 1.82284 0.02467  0.00820  -0.19928 312 ASN A CG  
2392 O OD1 . ASN A 339 ? 1.91768 1.80137 2.10400 0.04927  0.01125  -0.18035 312 ASN A OD1 
2393 N ND2 . ASN A 339 ? 1.54759 1.39109 1.72744 0.01309  0.01425  -0.22474 312 ASN A ND2 
2394 N N   . THR A 340 ? 1.53540 1.53168 1.60602 0.00204  -0.02300 -0.17896 313 THR A N   
2395 C CA  . THR A 340 ? 1.64044 1.65307 1.68363 -0.00909 -0.03902 -0.16940 313 THR A CA  
2396 C C   . THR A 340 ? 1.67809 1.70390 1.73620 0.00328  -0.04606 -0.14077 313 THR A C   
2397 O O   . THR A 340 ? 1.92135 1.95130 1.98605 0.01871  -0.03877 -0.12911 313 THR A O   
2398 C CB  . THR A 340 ? 1.49194 1.51210 1.49327 -0.01526 -0.03618 -0.17786 313 THR A CB  
2399 O OG1 . THR A 340 ? 1.81164 1.82265 1.79449 -0.02860 -0.02666 -0.20749 313 THR A OG1 
2400 C CG2 . THR A 340 ? 1.53687 1.56483 1.50652 -0.02336 -0.05517 -0.16336 313 THR A CG2 
2401 N N   . LYS A 341 ? 1.50677 1.54296 1.57167 -0.00358 -0.06041 -0.13186 314 LYS A N   
2402 C CA  . LYS A 341 ? 1.58823 1.64081 1.66849 0.00789  -0.06538 -0.10889 314 LYS A CA  
2403 C C   . LYS A 341 ? 1.61064 1.67743 1.67144 0.00399  -0.08470 -0.10504 314 LYS A C   
2404 O O   . LYS A 341 ? 1.49886 1.58125 1.57674 -0.00416 -0.09850 -0.10561 314 LYS A O   
2405 C CB  . LYS A 341 ? 1.69467 1.75078 1.81533 0.00612  -0.06106 -0.10062 314 LYS A CB  
2406 C CG  . LYS A 341 ? 1.59693 1.62812 1.73352 0.00874  -0.04524 -0.10245 314 LYS A CG  
2407 C CD  . LYS A 341 ? 1.66447 1.69262 1.79380 0.02907  -0.03577 -0.09007 314 LYS A CD  
2408 C CE  . LYS A 341 ? 1.53835 1.54202 1.68673 0.03647  -0.02420 -0.08410 314 LYS A CE  
2409 N NZ  . LYS A 341 ? 1.46037 1.43826 1.61384 0.02991  -0.02022 -0.10663 314 LYS A NZ  
2410 N N   . LEU A 342 ? 1.57151 1.63260 1.59827 0.00951  -0.08688 -0.10040 315 LEU A N   
2411 C CA  . LEU A 342 ? 1.42308 1.48620 1.42214 0.00765  -0.10638 -0.09399 315 LEU A CA  
2412 C C   . LEU A 342 ? 1.49201 1.55521 1.49195 0.02584  -0.10836 -0.07619 315 LEU A C   
2413 O O   . LEU A 342 ? 1.69552 1.74957 1.69061 0.03318  -0.09406 -0.07357 315 LEU A O   
2414 C CB  . LEU A 342 ? 1.44842 1.49386 1.39546 -0.00648 -0.10653 -0.10409 315 LEU A CB  
2415 C CG  . LEU A 342 ? 1.65368 1.68952 1.55768 -0.00839 -0.12615 -0.09187 315 LEU A CG  
2416 C CD1 . LEU A 342 ? 1.83747 1.89071 1.74970 -0.01082 -0.15311 -0.08939 315 LEU A CD1 
2417 C CD2 . LEU A 342 ? 1.34518 1.36120 1.19258 -0.02605 -0.11843 -0.10032 315 LEU A CD2 
2418 N N   . LEU A 343 ? 1.47234 1.54701 1.48010 0.03379  -0.12723 -0.06602 316 LEU A N   
2419 C CA  . LEU A 343 ? 1.43701 1.50629 1.44407 0.05332  -0.13060 -0.05203 316 LEU A CA  
2420 C C   . LEU A 343 ? 1.54453 1.60368 1.52383 0.05636  -0.15615 -0.04270 316 LEU A C   
2421 O O   . LEU A 343 ? 1.70607 1.78630 1.69677 0.05225  -0.17639 -0.04341 316 LEU A O   
2422 C CB  . LEU A 343 ? 1.44511 1.54334 1.50409 0.06856  -0.12496 -0.04738 316 LEU A CB  
2423 C CG  . LEU A 343 ? 1.27127 1.37112 1.34000 0.09217  -0.13016 -0.03736 316 LEU A CG  
2424 C CD1 . LEU A 343 ? 1.28348 1.34713 1.31559 0.09846  -0.11973 -0.03541 316 LEU A CD1 
2425 C CD2 . LEU A 343 ? 1.51072 1.64716 1.63257 0.10318  -0.11822 -0.03689 316 LEU A CD2 
2426 N N   . ILE A 344 ? 1.66951 1.69477 1.61115 0.06243  -0.15686 -0.03332 317 ILE A N   
2427 C CA  . ILE A 344 ? 1.76443 1.76736 1.67070 0.06714  -0.18142 -0.01901 317 ILE A CA  
2428 C C   . ILE A 344 ? 1.89619 1.87525 1.80587 0.09108  -0.18182 -0.00710 317 ILE A C   
2429 O O   . ILE A 344 ? 1.87143 1.82644 1.76818 0.08974  -0.16208 -0.01031 317 ILE A O   
2430 C CB  . ILE A 344 ? 1.87302 1.84275 1.71297 0.04345  -0.18051 -0.01877 317 ILE A CB  
2431 C CG1 . ILE A 344 ? 1.67166 1.66371 1.50641 0.02153  -0.18031 -0.03500 317 ILE A CG1 
2432 C CG2 . ILE A 344 ? 1.83634 1.77185 1.63010 0.04909  -0.20546 0.00239  317 ILE A CG2 
2433 C CD1 . ILE A 344 ? 1.85647 1.82307 1.62831 -0.00337 -0.17167 -0.04014 317 ILE A CD1 
2434 N N   . VAL A 345 ? 2.00469 1.99160 1.93418 0.11353  -0.20504 0.00448  318 VAL A N   
2435 C CA  . VAL A 345 ? 1.89584 1.86022 1.83662 0.14170  -0.20577 0.01275  318 VAL A CA  
2436 C C   . VAL A 345 ? 1.99081 1.91557 1.89331 0.15304  -0.23510 0.03360  318 VAL A C   
2437 O O   . VAL A 345 ? 2.16217 2.11232 2.07697 0.16132  -0.26425 0.04231  318 VAL A O   
2438 C CB  . VAL A 345 ? 1.58782 1.60217 1.60070 0.16598  -0.20271 0.00636  318 VAL A CB  
2439 C CG1 . VAL A 345 ? 1.87696 1.86499 1.89986 0.19680  -0.19933 0.00977  318 VAL A CG1 
2440 C CG2 . VAL A 345 ? 1.29197 1.33963 1.33377 0.15211  -0.17464 -0.00922 318 VAL A CG2 
2441 N N   . ASP A 346 ? 1.91318 1.77446 1.76754 0.15155  -0.22865 0.04234  319 ASP A N   
2442 C CA  . ASP A 346 ? 2.07979 1.88649 1.89633 0.16746  -0.25338 0.06607  319 ASP A CA  
2443 C C   . ASP A 346 ? 2.24368 2.04530 2.01199 0.15214  -0.28124 0.08306  319 ASP A C   
2444 O O   . ASP A 346 ? 2.25545 2.03038 2.00368 0.17140  -0.31259 0.10635  319 ASP A O   
2445 C CB  . ASP A 346 ? 2.40422 2.22351 2.27585 0.21156  -0.26865 0.07039  319 ASP A CB  
2446 C CG  . ASP A 346 ? 2.23258 2.03936 2.13294 0.22702  -0.24061 0.05445  319 ASP A CG  
2447 O OD1 . ASP A 346 ? 2.11945 1.91301 1.99876 0.20257  -0.21288 0.04099  319 ASP A OD1 
2448 O OD2 . ASP A 346 ? 2.18063 1.99347 2.12487 0.26406  -0.24672 0.05377  319 ASP A OD2 
2449 N N   . ASP A 347 ? 2.18590 2.01250 1.93373 0.11884  -0.27071 0.07096  320 ASP A N   
2450 C CA  . ASP A 347 ? 2.40671 2.23457 2.10397 0.09971  -0.29355 0.08076  320 ASP A CA  
2451 C C   . ASP A 347 ? 2.32786 2.19434 2.05799 0.12418  -0.33393 0.09083  320 ASP A C   
2452 O O   . ASP A 347 ? 2.15948 2.01261 1.84139 0.12141  -0.36585 0.10950  320 ASP A O   
2453 C CB  . ASP A 347 ? 2.30833 2.06343 1.91749 0.08289  -0.29531 0.10292  320 ASP A CB  
2454 C CG  . ASP A 347 ? 2.36929 2.09694 1.95404 0.05483  -0.25490 0.09003  320 ASP A CG  
2455 O OD1 . ASP A 347 ? 2.51355 2.27689 2.14949 0.05376  -0.22985 0.06593  320 ASP A OD1 
2456 O OD2 . ASP A 347 ? 2.23100 1.90369 1.74642 0.03298  -0.24850 0.10466  320 ASP A OD2 
2457 N N   . GLU A 348 ? 2.21655 2.13622 2.03022 0.14689  -0.33236 0.07792  321 GLU A N   
2458 C CA  . GLU A 348 ? 2.05964 2.03255 1.92619 0.17100  -0.36736 0.08252  321 GLU A CA  
2459 C C   . GLU A 348 ? 1.91415 1.96399 1.85488 0.16321  -0.35697 0.05740  321 GLU A C   
2460 O O   . GLU A 348 ? 1.98010 2.08315 1.95518 0.16635  -0.38642 0.05598  321 GLU A O   
2461 C CB  . GLU A 348 ? 2.04951 2.00833 1.95472 0.21635  -0.37932 0.09686  321 GLU A CB  
2462 C CG  . GLU A 348 ? 2.43012 2.43857 2.38414 0.24653  -0.42261 0.10740  321 GLU A CG  
2463 C CD  . GLU A 348 ? 2.58740 2.57344 2.57706 0.29509  -0.43186 0.12056  321 GLU A CD  
2464 O OE1 . GLU A 348 ? 2.33448 2.26229 2.30552 0.30115  -0.40312 0.11931  321 GLU A OE1 
2465 O OE2 . GLU A 348 ? 2.66062 2.68816 2.69897 0.32758  -0.46819 0.13014  321 GLU A OE2 
2466 N N   . TYR A 349 ? 1.67269 1.72999 1.63784 0.15119  -0.31776 0.03846  322 TYR A N   
2467 C CA  . TYR A 349 ? 1.68206 1.80115 1.71046 0.14034  -0.30468 0.01788  322 TYR A CA  
2468 C C   . TYR A 349 ? 1.79388 1.89938 1.79274 0.10658  -0.27647 0.00167  322 TYR A C   
2469 O O   . TYR A 349 ? 1.85125 1.91326 1.81156 0.10052  -0.25319 0.00190  322 TYR A O   
2470 C CB  . TYR A 349 ? 1.72233 1.86952 1.82052 0.16542  -0.28419 0.01264  322 TYR A CB  
2471 C CG  . TYR A 349 ? 1.75804 1.95605 1.91135 0.14952  -0.26159 -0.00543 322 TYR A CG  
2472 C CD1 . TYR A 349 ? 1.63058 1.89211 1.84101 0.14444  -0.27822 -0.01222 322 TYR A CD1 
2473 C CD2 . TYR A 349 ? 1.75167 1.93329 1.89962 0.13850  -0.22488 -0.01442 322 TYR A CD2 
2474 C CE1 . TYR A 349 ? 1.67774 1.97842 1.93629 0.12597  -0.25541 -0.02674 322 TYR A CE1 
2475 C CE2 . TYR A 349 ? 1.60627 1.82532 1.79846 0.12402  -0.20447 -0.02626 322 TYR A CE2 
2476 C CZ  . TYR A 349 ? 1.67051 1.94562 1.91685 0.11653  -0.21816 -0.03193 322 TYR A CZ  
2477 O OH  . TYR A 349 ? 1.79277 2.09791 2.08067 0.09842  -0.19606 -0.04172 322 TYR A OH  
2478 N N   . VAL A 350 ? 1.78514 1.92827 1.80508 0.08480  -0.27941 -0.01381 323 VAL A N   
2479 C CA  . VAL A 350 ? 1.52823 1.66065 1.53095 0.05696  -0.25325 -0.03160 323 VAL A CA  
2480 C C   . VAL A 350 ? 1.60729 1.78346 1.67693 0.04960  -0.24030 -0.04612 323 VAL A C   
2481 O O   . VAL A 350 ? 1.81753 2.03983 1.93437 0.05096  -0.25961 -0.04819 323 VAL A O   
2482 C CB  . VAL A 350 ? 1.59189 1.70757 1.53286 0.03076  -0.26669 -0.03893 323 VAL A CB  
2483 C CG1 . VAL A 350 ? 1.53789 1.69536 1.49713 0.02218  -0.30022 -0.04488 323 VAL A CG1 
2484 C CG2 . VAL A 350 ? 1.35788 1.45749 1.28293 0.00787  -0.23578 -0.05904 323 VAL A CG2 
2485 N N   . HIS A 351 ? 1.63097 1.79288 1.70530 0.04102  -0.20811 -0.05501 324 HIS A N   
2486 C CA  . HIS A 351 ? 1.65889 1.84860 1.78876 0.03359  -0.19032 -0.06391 324 HIS A CA  
2487 C C   . HIS A 351 ? 1.65302 1.81553 1.76175 0.01348  -0.16949 -0.07789 324 HIS A C   
2488 O O   . HIS A 351 ? 1.50080 1.63400 1.58397 0.01875  -0.15011 -0.07590 324 HIS A O   
2489 C CB  . HIS A 351 ? 1.55179 1.75172 1.71681 0.05516  -0.17062 -0.05386 324 HIS A CB  
2490 C CG  . HIS A 351 ? 1.55428 1.76497 1.75477 0.04548  -0.14426 -0.05834 324 HIS A CG  
2491 N ND1 . HIS A 351 ? 1.60680 1.85866 1.86334 0.03547  -0.14328 -0.06173 324 HIS A ND1 
2492 C CD2 . HIS A 351 ? 1.47516 1.65986 1.66190 0.04372  -0.11887 -0.05790 324 HIS A CD2 
2493 C CE1 . HIS A 351 ? 1.42174 1.66531 1.69200 0.02675  -0.11658 -0.06107 324 HIS A CE1 
2494 N NE2 . HIS A 351 ? 1.58433 1.78751 1.81226 0.03371  -0.10331 -0.05804 324 HIS A NE2 
2495 N N   . ILE A 352 ? 1.66252 1.83557 1.78524 -0.00891 -0.17414 -0.09371 325 ILE A N   
2496 C CA  . ILE A 352 ? 1.53038 1.67518 1.63901 -0.02571 -0.15519 -0.11009 325 ILE A CA  
2497 C C   . ILE A 352 ? 1.58842 1.74483 1.75045 -0.03607 -0.14170 -0.11423 325 ILE A C   
2498 O O   . ILE A 352 ? 1.76653 1.95547 1.96570 -0.04849 -0.15537 -0.11850 325 ILE A O   
2499 C CB  . ILE A 352 ? 1.45760 1.59051 1.52328 -0.04642 -0.16955 -0.12972 325 ILE A CB  
2500 C CG1 . ILE A 352 ? 1.34657 1.46388 1.35220 -0.03941 -0.18035 -0.12136 325 ILE A CG1 
2501 C CG2 . ILE A 352 ? 1.60442 1.70728 1.66246 -0.05994 -0.14693 -0.15060 325 ILE A CG2 
2502 C CD1 . ILE A 352 ? 1.38209 1.48611 1.33294 -0.06100 -0.19025 -0.13993 325 ILE A CD1 
2503 N N   . THR A 353 ? 1.54809 1.67836 1.71426 -0.03212 -0.11585 -0.11197 326 THR A N   
2504 C CA  . THR A 353 ? 1.66089 1.79109 1.87011 -0.04139 -0.09994 -0.10975 326 THR A CA  
2505 C C   . THR A 353 ? 1.59535 1.68080 1.79142 -0.04567 -0.08187 -0.11924 326 THR A C   
2506 O O   . THR A 353 ? 1.80034 1.86399 1.96020 -0.04020 -0.08009 -0.12947 326 THR A O   
2507 C CB  . THR A 353 ? 1.57034 1.71909 1.80501 -0.02439 -0.08638 -0.08723 326 THR A CB  
2508 O OG1 . THR A 353 ? 1.74530 1.88406 2.00988 -0.03523 -0.06672 -0.08138 326 THR A OG1 
2509 C CG2 . THR A 353 ? 1.45185 1.58194 1.65184 -0.00128 -0.07744 -0.07694 326 THR A CG2 
2510 N N   . SER A 354 ? 1.40741 1.47906 1.63544 -0.05551 -0.06745 -0.11551 327 SER A N   
2511 C CA  . SER A 354 ? 1.60973 1.63429 1.83226 -0.05339 -0.05012 -0.11902 327 SER A CA  
2512 C C   . SER A 354 ? 1.60502 1.61928 1.83161 -0.03359 -0.03330 -0.09262 327 SER A C   
2513 O O   . SER A 354 ? 1.77879 1.75743 1.99656 -0.02254 -0.02277 -0.09128 327 SER A O   
2514 C CB  . SER A 354 ? 2.00137 2.00185 2.24975 -0.08003 -0.04636 -0.13313 327 SER A CB  
2515 O OG  . SER A 354 ? 1.87767 1.89991 2.16485 -0.09382 -0.04203 -0.11756 327 SER A OG  
2516 N N   . ALA A 355 ? 1.50694 1.55315 1.74605 -0.02762 -0.03123 -0.07285 328 ALA A N   
2517 C CA  . ALA A 355 ? 1.69929 1.73956 1.93363 -0.01067 -0.01619 -0.04849 328 ALA A CA  
2518 C C   . ALA A 355 ? 1.74947 1.80245 1.95366 0.01260  -0.02094 -0.04514 328 ALA A C   
2519 O O   . ALA A 355 ? 1.69204 1.76501 1.88501 0.01474  -0.03413 -0.05517 328 ALA A O   
2520 C CB  . ALA A 355 ? 1.58975 1.65801 1.85243 -0.01947 -0.00595 -0.03181 328 ALA A CB  
2521 N N   . ASN A 356 ? 1.71808 1.75703 1.90740 0.02881  -0.01142 -0.03008 329 ASN A N   
2522 C CA  . ASN A 356 ? 1.62355 1.67307 1.78573 0.04751  -0.01513 -0.02837 329 ASN A CA  
2523 C C   . ASN A 356 ? 1.79029 1.86523 1.94971 0.05503  -0.00966 -0.01435 329 ASN A C   
2524 O O   . ASN A 356 ? 1.87730 1.95750 2.05050 0.05029  0.00267  0.00022  329 ASN A O   
2525 C CB  . ASN A 356 ? 1.75406 1.78120 1.90327 0.06163  -0.01161 -0.02320 329 ASN A CB  
2526 C CG  . ASN A 356 ? 1.82313 1.86526 1.94801 0.07627  -0.01663 -0.02503 329 ASN A CG  
2527 O OD1 . ASN A 356 ? 1.93281 1.97840 2.04828 0.07546  -0.02285 -0.04173 329 ASN A OD1 
2528 N ND2 . ASN A 356 ? 1.91711 1.96796 2.02903 0.08677  -0.01283 -0.00880 329 ASN A ND2 
2529 N N   . PHE A 357 ? 1.57968 1.66803 1.71979 0.06548  -0.01671 -0.02009 330 PHE A N   
2530 C CA  . PHE A 357 ? 1.68613 1.79479 1.82086 0.07546  -0.01094 -0.01275 330 PHE A CA  
2531 C C   . PHE A 357 ? 1.65393 1.75700 1.76955 0.08435  0.00073  0.00171  330 PHE A C   
2532 O O   . PHE A 357 ? 1.71972 1.81721 1.80868 0.09436  -0.00375 -0.00056 330 PHE A O   
2533 C CB  . PHE A 357 ? 1.64099 1.75241 1.75556 0.08408  -0.02184 -0.02339 330 PHE A CB  
2534 C CG  . PHE A 357 ? 1.65806 1.77719 1.78493 0.07852  -0.03556 -0.03216 330 PHE A CG  
2535 C CD1 . PHE A 357 ? 1.69610 1.83465 1.85793 0.06904  -0.03716 -0.03160 330 PHE A CD1 
2536 C CD2 . PHE A 357 ? 1.76204 1.86954 1.86403 0.08114  -0.04809 -0.03984 330 PHE A CD2 
2537 C CE1 . PHE A 357 ? 1.69556 1.84598 1.86749 0.06508  -0.05488 -0.03900 330 PHE A CE1 
2538 C CE2 . PHE A 357 ? 1.54674 1.65867 1.65251 0.07730  -0.06404 -0.04397 330 PHE A CE2 
2539 C CZ  . PHE A 357 ? 1.48522 1.62077 1.62610 0.07069  -0.06938 -0.04376 330 PHE A CZ  
2540 N N   . ASP A 358 ? 1.55370 1.65952 1.68072 0.07861  0.01516  0.01708  331 ASP A N   
2541 C CA  . ASP A 358 ? 1.75778 1.85764 1.85829 0.08590  0.02577  0.03467  331 ASP A CA  
2542 C C   . ASP A 358 ? 1.84092 1.95425 1.95415 0.07562  0.04652  0.04941  331 ASP A C   
2543 O O   . ASP A 358 ? 1.89722 2.03083 2.04641 0.06407  0.05162  0.04335  331 ASP A O   
2544 C CB  . ASP A 358 ? 1.86211 1.93165 1.95177 0.08974  0.01935  0.04429  331 ASP A CB  
2545 C CG  . ASP A 358 ? 1.90209 1.94713 2.01841 0.07603  0.02368  0.05063  331 ASP A CG  
2546 O OD1 . ASP A 358 ? 1.90800 1.94412 2.02641 0.06678  0.03835  0.07049  331 ASP A OD1 
2547 O OD2 . ASP A 358 ? 1.93528 1.96749 2.06764 0.07256  0.01402  0.03485  331 ASP A OD2 
2548 N N   . GLY A 359 ? 1.88065 1.98583 1.96350 0.07865  0.05831  0.06932  332 GLY A N   
2549 C CA  . GLY A 359 ? 1.86748 1.98744 1.95432 0.06676  0.08316  0.08441  332 GLY A CA  
2550 C C   . GLY A 359 ? 1.70035 1.80011 1.81404 0.04538  0.09244  0.09952  332 GLY A C   
2551 O O   . GLY A 359 ? 1.83225 1.95639 1.98295 0.02772  0.10712  0.09714  332 GLY A O   
2552 N N   . THR A 360 ? 1.67061 1.72581 1.76929 0.04679  0.08392  0.11418  333 THR A N   
2553 C CA  . THR A 360 ? 1.71289 1.73505 1.83195 0.02596  0.09361  0.12966  333 THR A CA  
2554 C C   . THR A 360 ? 1.88814 1.92346 2.06008 0.00730  0.09015  0.10703  333 THR A C   
2555 O O   . THR A 360 ? 2.06768 2.10899 2.26960 -0.01841 0.10628  0.11225  333 THR A O   
2556 C CB  . THR A 360 ? 1.74676 1.71450 1.84566 0.03789  0.08031  0.14394  333 THR A CB  
2557 O OG1 . THR A 360 ? 2.01053 1.97289 2.05969 0.05620  0.07818  0.16540  333 THR A OG1 
2558 C CG2 . THR A 360 ? 2.10940 2.02985 2.22424 0.01684  0.09179  0.16193  333 THR A CG2 
2559 N N   . HIS A 361 ? 1.74909 1.79151 1.93134 0.01756  0.06898  0.08159  334 HIS A N   
2560 C CA  . HIS A 361 ? 1.85403 1.90730 2.07726 0.00060  0.06056  0.05947  334 HIS A CA  
2561 C C   . HIS A 361 ? 1.86436 1.97224 2.12210 -0.01147 0.06887  0.05261  334 HIS A C   
2562 O O   . HIS A 361 ? 1.87412 1.99248 2.16998 -0.03726 0.07727  0.05166  334 HIS A O   
2563 C CB  . HIS A 361 ? 1.55745 1.60905 1.77274 0.01472  0.03777  0.03611  334 HIS A CB  
2564 C CG  . HIS A 361 ? 1.67956 1.68421 1.88237 0.02077  0.03055  0.03395  334 HIS A CG  
2565 N ND1 . HIS A 361 ? 1.71988 1.70806 1.93759 0.01123  0.02051  0.01166  334 HIS A ND1 
2566 C CD2 . HIS A 361 ? 1.95701 1.93007 2.13565 0.03724  0.03162  0.04989  334 HIS A CD2 
2567 C CE1 . HIS A 361 ? 1.77903 1.72716 1.98573 0.02277  0.01877  0.01193  334 HIS A CE1 
2568 N NE2 . HIS A 361 ? 1.89719 1.83672 2.08305 0.03992  0.02372  0.03618  334 HIS A NE2 
2569 N N   . TYR A 362 ? 1.67084 1.81494 1.91975 0.00704  0.06666  0.04623  335 TYR A N   
2570 C CA  . TYR A 362 ? 1.48928 1.68893 1.77730 0.00303  0.07208  0.03678  335 TYR A CA  
2571 C C   . TYR A 362 ? 1.54946 1.77449 1.84810 -0.00733 0.10303  0.05258  335 TYR A C   
2572 O O   . TYR A 362 ? 1.50140 1.78026 1.83862 -0.00815 0.11183  0.04379  335 TYR A O   
2573 C CB  . TYR A 362 ? 1.36162 1.58229 1.63696 0.02909  0.05832  0.02282  335 TYR A CB  
2574 C CG  . TYR A 362 ? 1.24412 1.45894 1.52457 0.03174  0.02990  0.00527  335 TYR A CG  
2575 C CD1 . TYR A 362 ? 1.44466 1.61900 1.68914 0.03739  0.01640  0.00172  335 TYR A CD1 
2576 C CD2 . TYR A 362 ? 1.48083 1.73409 1.80184 0.02820  0.01654  -0.00746 335 TYR A CD2 
2577 C CE1 . TYR A 362 ? 1.50914 1.67815 1.75127 0.03677  -0.00585 -0.01400 335 TYR A CE1 
2578 C CE2 . TYR A 362 ? 1.71396 1.95975 2.02959 0.02920  -0.01047 -0.02088 335 TYR A CE2 
2579 C CZ  . TYR A 362 ? 1.73006 1.93195 2.00288 0.03205  -0.01967 -0.02405 335 TYR A CZ  
2580 O OH  . TYR A 362 ? 1.92079 2.11535 2.18149 0.03022  -0.04289 -0.03714 335 TYR A OH  
2581 N N   . GLN A 363 ? 1.64752 1.83676 1.91311 -0.01452 0.12012  0.07616  336 GLN A N   
2582 C CA  . GLN A 363 ? 1.61135 1.81951 1.88031 -0.03080 0.15308  0.09430  336 GLN A CA  
2583 C C   . GLN A 363 ? 1.64719 1.82973 1.93802 -0.06531 0.16676  0.10997  336 GLN A C   
2584 O O   . GLN A 363 ? 1.84166 2.05620 2.15970 -0.08855 0.19436  0.11777  336 GLN A O   
2585 C CB  . GLN A 363 ? 1.85520 2.04220 2.05875 -0.01509 0.16531  0.11403  336 GLN A CB  
2586 C CG  . GLN A 363 ? 1.70023 1.92163 1.88464 0.01117  0.16489  0.09819  336 GLN A CG  
2587 C CD  . GLN A 363 ? 1.83036 2.11336 2.05219 0.00640  0.19092  0.08791  336 GLN A CD  
2588 O OE1 . GLN A 363 ? 2.02569 2.34848 2.30220 0.00976  0.18222  0.06671  336 GLN A OE1 
2589 N NE2 . GLN A 363 ? 1.72028 2.01385 1.91238 -0.00034 0.22297  0.10288  336 GLN A NE2 
2590 N N   . ASN A 364 ? 1.76435 1.88970 2.04618 -0.07041 0.15040  0.11311  337 ASN A N   
2591 C CA  . ASN A 364 ? 2.02678 2.11383 2.32407 -0.10362 0.16465  0.12889  337 ASN A CA  
2592 C C   . ASN A 364 ? 1.93862 2.00437 2.27238 -0.11929 0.14461  0.10708  337 ASN A C   
2593 O O   . ASN A 364 ? 1.82224 1.88700 2.19508 -0.15479 0.15577  0.10586  337 ASN A O   
2594 C CB  . ASN A 364 ? 1.98359 2.00172 2.22263 -0.09656 0.17178  0.16273  337 ASN A CB  
2595 C CG  . ASN A 364 ? 2.11229 2.14921 2.30355 -0.08250 0.18948  0.18383  337 ASN A CG  
2596 O OD1 . ASN A 364 ? 1.88161 1.92311 2.03568 -0.05128 0.17465  0.17994  337 ASN A OD1 
2597 N ND2 . ASN A 364 ? 2.48405 2.53329 2.67463 -0.10836 0.22268  0.20456  337 ASN A ND2 
2598 N N   . HIS A 365 ? 1.87405 1.92404 2.19486 -0.09667 0.11687  0.08803  338 HIS A N   
2599 C CA  . HIS A 365 ? 1.80195 1.82495 2.14571 -0.11101 0.09951  0.06571  338 HIS A CA  
2600 C C   . HIS A 365 ? 1.71901 1.80254 2.11559 -0.13117 0.09016  0.03957  338 HIS A C   
2601 O O   . HIS A 365 ? 1.80261 1.94938 2.21520 -0.11991 0.08746  0.03330  338 HIS A O   
2602 C CB  . HIS A 365 ? 1.73502 1.73027 2.04747 -0.08174 0.07631  0.05183  338 HIS A CB  
2603 C CG  . HIS A 365 ? 1.75090 1.68905 2.02185 -0.06131 0.07984  0.07408  338 HIS A CG  
2604 N ND1 . HIS A 365 ? 1.84413 1.74290 2.10127 -0.07060 0.09917  0.10605  338 HIS A ND1 
2605 C CD2 . HIS A 365 ? 1.86405 1.78080 2.10594 -0.03186 0.06530  0.07008  338 HIS A CD2 
2606 C CE1 . HIS A 365 ? 1.90125 1.75606 2.12193 -0.04445 0.09281  0.12188  338 HIS A CE1 
2607 N NE2 . HIS A 365 ? 1.97792 1.84688 2.19316 -0.02076 0.07268  0.09883  338 HIS A NE2 
2608 N N   . GLY A 366 ? 1.62685 1.68945 2.05125 -0.16034 0.08361  0.02322  339 GLY A N   
2609 C CA  . GLY A 366 ? 1.79201 1.91175 2.26674 -0.18229 0.06924  -0.00294 339 GLY A CA  
2610 C C   . GLY A 366 ? 1.60122 1.71120 2.06532 -0.17610 0.03833  -0.03289 339 GLY A C   
2611 O O   . GLY A 366 ? 1.60073 1.64953 2.04745 -0.18445 0.03477  -0.04318 339 GLY A O   
2612 N N   . PHE A 367 ? 1.68249 1.84987 2.15463 -0.16099 0.01672  -0.04709 340 PHE A N   
2613 C CA  . PHE A 367 ? 1.33786 1.49752 1.78820 -0.15412 -0.01205 -0.07218 340 PHE A CA  
2614 C C   . PHE A 367 ? 1.53393 1.76671 2.01384 -0.15344 -0.03674 -0.08575 340 PHE A C   
2615 O O   . PHE A 367 ? 1.86050 2.15119 2.37885 -0.14975 -0.03097 -0.07610 340 PHE A O   
2616 C CB  . PHE A 367 ? 1.64541 1.76866 2.03959 -0.11901 -0.01457 -0.06663 340 PHE A CB  
2617 C CG  . PHE A 367 ? 1.59243 1.74372 1.97418 -0.08948 -0.00742 -0.04683 340 PHE A CG  
2618 C CD1 . PHE A 367 ? 1.56982 1.76354 1.94877 -0.07110 -0.02560 -0.05304 340 PHE A CD1 
2619 C CD2 . PHE A 367 ? 1.49461 1.62504 1.86299 -0.08016 0.01665  -0.02219 340 PHE A CD2 
2620 C CE1 . PHE A 367 ? 1.43554 1.64798 1.80234 -0.04461 -0.01793 -0.03873 340 PHE A CE1 
2621 C CE2 . PHE A 367 ? 1.57581 1.73070 1.92826 -0.05503 0.02344  -0.00855 340 PHE A CE2 
2622 C CZ  . PHE A 367 ? 1.58112 1.77570 1.93446 -0.03748 0.00709  -0.01872 340 PHE A CZ  
2623 N N   . VAL A 368 ? 1.32559 1.55542 1.78616 -0.15587 -0.06450 -0.10853 341 VAL A N   
2624 C CA  . VAL A 368 ? 1.50645 1.79632 1.98147 -0.15023 -0.09534 -0.11924 341 VAL A CA  
2625 C C   . VAL A 368 ? 1.61833 1.88568 2.03339 -0.12138 -0.11109 -0.12013 341 VAL A C   
2626 O O   . VAL A 368 ? 1.64581 1.85754 2.01522 -0.11950 -0.10534 -0.12676 341 VAL A O   
2627 C CB  . VAL A 368 ? 1.40506 1.71814 1.90854 -0.18643 -0.11817 -0.14566 341 VAL A CB  
2628 C CG1 . VAL A 368 ? 1.70528 2.04511 2.27415 -0.21967 -0.10075 -0.14472 341 VAL A CG1 
2629 C CG2 . VAL A 368 ? 1.51895 1.76786 1.97465 -0.20060 -0.12273 -0.16756 341 VAL A CG2 
2630 N N   . SER A 369 ? 1.63718 1.94715 2.05482 -0.09879 -0.12949 -0.11337 342 SER A N   
2631 C CA  . SER A 369 ? 1.54553 1.83320 1.90702 -0.07238 -0.14156 -0.10925 342 SER A CA  
2632 C C   . SER A 369 ? 1.60329 1.92915 1.96293 -0.06809 -0.17900 -0.11508 342 SER A C   
2633 O O   . SER A 369 ? 1.67229 2.05649 2.08398 -0.06493 -0.19263 -0.11205 342 SER A O   
2634 C CB  . SER A 369 ? 1.48167 1.76518 1.83546 -0.04159 -0.12283 -0.08823 342 SER A CB  
2635 O OG  . SER A 369 ? 1.43785 1.69027 1.79069 -0.04463 -0.09178 -0.07962 342 SER A OG  
2636 N N   . PHE A 370 ? 1.65999 1.95439 1.95940 -0.06740 -0.19526 -0.12270 343 PHE A N   
2637 C CA  . PHE A 370 ? 1.73618 2.05440 2.01480 -0.06339 -0.23310 -0.12461 343 PHE A CA  
2638 C C   . PHE A 370 ? 1.62559 1.94116 1.88436 -0.02807 -0.23857 -0.10251 343 PHE A C   
2639 O O   . PHE A 370 ? 1.45140 1.72403 1.67196 -0.01483 -0.21795 -0.09424 343 PHE A O   
2640 C CB  . PHE A 370 ? 1.63665 1.91697 1.85054 -0.08271 -0.24305 -0.14314 343 PHE A CB  
2641 C CG  . PHE A 370 ? 1.51961 1.80774 1.68551 -0.07659 -0.27896 -0.13941 343 PHE A CG  
2642 C CD1 . PHE A 370 ? 1.63240 1.88570 1.74016 -0.05647 -0.27725 -0.12360 343 PHE A CD1 
2643 C CD2 . PHE A 370 ? 1.61125 1.93919 1.78615 -0.09373 -0.31529 -0.15134 343 PHE A CD2 
2644 C CE1 . PHE A 370 ? 1.67606 1.92843 1.73222 -0.05249 -0.30958 -0.11580 343 PHE A CE1 
2645 C CE2 . PHE A 370 ? 1.71026 2.04222 1.83295 -0.08754 -0.35118 -0.14422 343 PHE A CE2 
2646 C CZ  . PHE A 370 ? 1.60450 1.89533 1.66545 -0.06662 -0.34748 -0.12467 343 PHE A CZ  
2647 N N   . ASN A 371 ? 1.48828 1.84936 1.77559 -0.01260 -0.26734 -0.09401 344 ASN A N   
2648 C CA  . ASN A 371 ? 1.58443 1.93739 1.85428 0.02236  -0.27640 -0.07385 344 ASN A CA  
2649 C C   . ASN A 371 ? 1.74589 2.11449 1.99202 0.02780  -0.32208 -0.06895 344 ASN A C   
2650 O O   . ASN A 371 ? 1.77019 2.19195 2.05652 0.01626  -0.34906 -0.07785 344 ASN A O   
2651 C CB  . ASN A 371 ? 1.42057 1.81372 1.75893 0.04642  -0.26249 -0.06491 344 ASN A CB  
2652 C CG  . ASN A 371 ? 1.65348 2.04119 2.01799 0.03572  -0.22038 -0.06888 344 ASN A CG  
2653 O OD1 . ASN A 371 ? 1.96723 2.31972 2.30737 0.05001  -0.19504 -0.06086 344 ASN A OD1 
2654 N ND2 . ASN A 371 ? 1.67507 2.09604 2.08691 0.00875  -0.21397 -0.08058 344 ASN A ND2 
2655 N N   . SER A 372 ? 1.77862 2.10121 1.95834 0.04337  -0.33192 -0.05398 345 SER A N   
2656 C CA  . SER A 372 ? 1.66286 1.99006 1.80625 0.04964  -0.37651 -0.04354 345 SER A CA  
2657 C C   . SER A 372 ? 1.70112 1.98998 1.81189 0.08383  -0.38368 -0.01743 345 SER A C   
2658 O O   . SER A 372 ? 1.74096 1.98454 1.83023 0.09236  -0.35263 -0.01202 345 SER A O   
2659 C CB  . SER A 372 ? 1.87050 2.16702 1.93664 0.01772  -0.38588 -0.05529 345 SER A CB  
2660 O OG  . SER A 372 ? 1.77022 2.07985 1.80131 0.02032  -0.43311 -0.04522 345 SER A OG  
2661 N N   . ILE A 373 ? 1.80461 2.11120 1.91288 0.10340  -0.42720 -0.00131 346 ILE A N   
2662 C CA  . ILE A 373 ? 2.02539 2.28627 2.09637 0.13602  -0.44071 0.02607  346 ILE A CA  
2663 C C   . ILE A 373 ? 2.08463 2.31585 2.07393 0.13059  -0.48109 0.04373  346 ILE A C   
2664 O O   . ILE A 373 ? 2.06135 2.24789 2.01263 0.15638  -0.49780 0.07075  346 ILE A O   
2665 C CB  . ILE A 373 ? 1.77956 2.08242 1.93248 0.17883  -0.45329 0.03539  346 ILE A CB  
2666 C CG1 . ILE A 373 ? 1.80025 2.18620 2.01469 0.18152  -0.49509 0.03052  346 ILE A CG1 
2667 C CG2 . ILE A 373 ? 1.87931 2.19714 2.09368 0.18525  -0.40711 0.02131  346 ILE A CG2 
2668 C CD1 . ILE A 373 ? 2.35901 2.79957 2.66596 0.22505  -0.50707 0.03633  346 ILE A CD1 
2669 N N   . ASP A 374 ? 1.91879 2.16950 1.87559 0.09694  -0.49707 0.02929  347 ASP A N   
2670 C CA  . ASP A 374 ? 1.93161 2.15345 1.79764 0.08704  -0.53337 0.04504  347 ASP A CA  
2671 C C   . ASP A 374 ? 2.10443 2.24069 1.87691 0.07850  -0.50755 0.05952  347 ASP A C   
2672 O O   . ASP A 374 ? 2.28891 2.40126 2.04337 0.05424  -0.46459 0.04084  347 ASP A O   
2673 C CB  . ASP A 374 ? 2.07691 2.33462 1.92323 0.04738  -0.54727 0.01850  347 ASP A CB  
2674 C CG  . ASP A 374 ? 2.31395 2.54243 2.05442 0.03262  -0.58226 0.03220  347 ASP A CG  
2675 O OD1 . ASP A 374 ? 2.18436 2.43022 1.91778 0.05507  -0.63288 0.05677  347 ASP A OD1 
2676 O OD2 . ASP A 374 ? 2.29754 2.48709 1.96132 -0.00052 -0.55905 0.01857  347 ASP A OD2 
2677 N N   . LYS A 375 ? 2.43925 2.52980 2.15443 0.09849  -0.53454 0.09376  348 LYS A N   
2678 C CA  . LYS A 375 ? 2.46192 2.46911 2.09411 0.09028  -0.50903 0.11089  348 LYS A CA  
2679 C C   . LYS A 375 ? 2.60692 2.59280 2.15720 0.04425  -0.48821 0.09467  348 LYS A C   
2680 O O   . LYS A 375 ? 2.69508 2.63671 2.21150 0.02788  -0.44661 0.09005  348 LYS A O   
2681 C CB  . LYS A 375 ? 2.68812 2.64515 2.26757 0.11724  -0.54645 0.15351  348 LYS A CB  
2682 C CG  . LYS A 375 ? 2.68768 2.63695 2.33642 0.16545  -0.55105 0.16933  348 LYS A CG  
2683 C CD  . LYS A 375 ? 2.42023 2.32623 2.08186 0.16387  -0.49807 0.15964  348 LYS A CD  
2684 C CE  . LYS A 375 ? 2.47893 2.36652 2.19659 0.21089  -0.50090 0.17306  348 LYS A CE  
2685 N NZ  . LYS A 375 ? 2.52567 2.36448 2.24231 0.20628  -0.45288 0.16367  348 LYS A NZ  
2686 N N   . GLN A 376 ? 2.50634 2.52660 2.02651 0.02257  -0.51567 0.08288  349 GLN A N   
2687 C CA  . GLN A 376 ? 2.37082 2.37307 1.81270 -0.02039 -0.49374 0.06237  349 GLN A CA  
2688 C C   . GLN A 376 ? 2.38855 2.40934 1.88188 -0.03861 -0.44480 0.02331  349 GLN A C   
2689 O O   . GLN A 376 ? 2.58038 2.56635 2.03138 -0.05956 -0.40460 0.01256  349 GLN A O   
2690 C CB  . GLN A 376 ? 2.52001 2.55643 1.91790 -0.03880 -0.53704 0.05501  349 GLN A CB  
2691 C CG  . GLN A 376 ? 2.78859 2.78835 2.09064 -0.03321 -0.57947 0.09474  349 GLN A CG  
2692 C CD  . GLN A 376 ? 2.94731 2.88197 2.13138 -0.06472 -0.55058 0.10201  349 GLN A CD  
2693 O OE1 . GLN A 376 ? 2.94421 2.87667 2.11452 -0.09535 -0.50551 0.06900  349 GLN A OE1 
2694 N NE2 . GLN A 376 ? 3.10100 2.98201 2.20064 -0.05704 -0.57546 0.14592  349 GLN A NE2 
2695 N N   . LEU A 377 ? 2.27380 2.35026 1.86029 -0.03086 -0.44764 0.00271  350 LEU A N   
2696 C CA  . LEU A 377 ? 2.23793 2.32722 1.87325 -0.04591 -0.40475 -0.03038 350 LEU A CA  
2697 C C   . LEU A 377 ? 2.12574 2.18280 1.78441 -0.03086 -0.36467 -0.02236 350 LEU A C   
2698 O O   . LEU A 377 ? 2.15107 2.19087 1.80064 -0.04731 -0.32568 -0.04113 350 LEU A O   
2699 C CB  . LEU A 377 ? 2.21562 2.36711 1.94307 -0.04261 -0.41775 -0.04874 350 LEU A CB  
2700 C CG  . LEU A 377 ? 2.11473 2.27938 1.87996 -0.06630 -0.38484 -0.08526 350 LEU A CG  
2701 C CD1 . LEU A 377 ? 2.30135 2.44531 1.99143 -0.10045 -0.37818 -0.11037 350 LEU A CD1 
2702 C CD2 . LEU A 377 ? 2.04948 2.27385 1.90061 -0.06703 -0.40246 -0.09847 350 LEU A CD2 
2703 N N   . VAL A 378 ? 2.09502 2.14469 1.78450 0.00129  -0.37472 0.00367  351 VAL A N   
2704 C CA  . VAL A 378 ? 1.92515 1.94215 1.62978 0.01404  -0.33996 0.01004  351 VAL A CA  
2705 C C   . VAL A 378 ? 2.13721 2.09643 1.75704 -0.00380 -0.32117 0.01890  351 VAL A C   
2706 O O   . VAL A 378 ? 2.25950 2.20049 1.88321 -0.01092 -0.28393 0.00945  351 VAL A O   
2707 C CB  . VAL A 378 ? 2.06577 2.08461 1.81840 0.05262  -0.35544 0.03222  351 VAL A CB  
2708 C CG1 . VAL A 378 ? 2.06184 2.04369 1.82239 0.06300  -0.32084 0.03566  351 VAL A CG1 
2709 C CG2 . VAL A 378 ? 2.01140 2.09657 1.85508 0.06685  -0.36699 0.02044  351 VAL A CG2 
2710 N N   . SER A 379 ? 2.23312 2.16556 1.77464 -0.01332 -0.34630 0.03727  352 SER A N   
2711 C CA  . SER A 379 ? 2.15970 2.03894 1.61634 -0.03642 -0.32501 0.04593  352 SER A CA  
2712 C C   . SER A 379 ? 2.16362 2.05635 1.60133 -0.06975 -0.29067 0.01231  352 SER A C   
2713 O O   . SER A 379 ? 2.02784 1.89673 1.44551 -0.08450 -0.25392 0.00628  352 SER A O   
2714 C CB  . SER A 379 ? 2.24201 2.08784 1.61207 -0.04013 -0.36098 0.07657  352 SER A CB  
2715 O OG  . SER A 379 ? 2.46987 2.35206 1.81588 -0.05473 -0.38794 0.06386  352 SER A OG  
2716 N N   . GLU A 380 ? 2.21022 2.14226 1.65757 -0.08189 -0.30197 -0.01205 353 GLU A N   
2717 C CA  . GLU A 380 ? 2.03988 1.98322 1.47905 -0.10873 -0.26811 -0.04848 353 GLU A CA  
2718 C C   . GLU A 380 ? 2.03662 1.99211 1.55228 -0.09887 -0.23234 -0.06581 353 GLU A C   
2719 O O   . GLU A 380 ? 2.23840 2.18611 1.74409 -0.11339 -0.19573 -0.08411 353 GLU A O   
2720 C CB  . GLU A 380 ? 1.79981 1.77790 1.23873 -0.12288 -0.28945 -0.07356 353 GLU A CB  
2721 C CG  . GLU A 380 ? 2.35222 2.32071 1.69949 -0.13958 -0.32262 -0.06261 353 GLU A CG  
2722 C CD  . GLU A 380 ? 2.64297 2.58228 1.89837 -0.17117 -0.29338 -0.07423 353 GLU A CD  
2723 O OE1 . GLU A 380 ? 2.45465 2.38943 1.72819 -0.17988 -0.24758 -0.09650 353 GLU A OE1 
2724 O OE2 . GLU A 380 ? 2.77456 2.69832 1.93930 -0.18710 -0.31628 -0.06090 353 GLU A OE2 
2725 N N   . ALA A 381 ? 1.93318 1.91067 1.52561 -0.07365 -0.24250 -0.05986 354 ALA A N   
2726 C CA  . ALA A 381 ? 1.71077 1.69709 1.36803 -0.06299 -0.21179 -0.07103 354 ALA A CA  
2727 C C   . ALA A 381 ? 1.92348 1.87815 1.56247 -0.05943 -0.18856 -0.05794 354 ALA A C   
2728 O O   . ALA A 381 ? 1.94462 1.90190 1.60492 -0.06358 -0.15722 -0.07330 354 ALA A O   
2729 C CB  . ALA A 381 ? 1.63633 1.65216 1.37006 -0.03890 -0.22652 -0.06456 354 ALA A CB  
2730 N N   . LYS A 382 ? 2.03852 1.96227 1.64008 -0.05159 -0.20512 -0.02963 355 LYS A N   
2731 C CA  . LYS A 382 ? 1.97562 1.86317 1.55387 -0.05413 -0.18398 -0.01809 355 LYS A CA  
2732 C C   . LYS A 382 ? 2.14235 2.01783 1.66562 -0.08607 -0.15685 -0.03105 355 LYS A C   
2733 O O   . LYS A 382 ? 2.15545 2.02662 1.68869 -0.09377 -0.12708 -0.03910 355 LYS A O   
2734 C CB  . LYS A 382 ? 2.07616 1.92275 1.62040 -0.04018 -0.20896 0.01551  355 LYS A CB  
2735 C CG  . LYS A 382 ? 2.08312 1.88496 1.60722 -0.04349 -0.18891 0.02755  355 LYS A CG  
2736 C CD  . LYS A 382 ? 2.06932 1.88211 1.66244 -0.01992 -0.17841 0.02151  355 LYS A CD  
2737 C CE  . LYS A 382 ? 2.30693 2.07102 1.87780 -0.02389 -0.16380 0.03234  355 LYS A CE  
2738 N NZ  . LYS A 382 ? 2.34776 2.11736 1.97609 0.00156  -0.15911 0.02746  355 LYS A NZ  
2739 N N   . LYS A 383 ? 2.25234 2.12681 1.71776 -0.10579 -0.16647 -0.03497 356 LYS A N   
2740 C CA  . LYS A 383 ? 2.21937 2.09032 1.63420 -0.13719 -0.13625 -0.05290 356 LYS A CA  
2741 C C   . LYS A 383 ? 2.07432 1.98087 1.54755 -0.13838 -0.10449 -0.08862 356 LYS A C   
2742 O O   . LYS A 383 ? 1.95432 1.86329 1.42595 -0.15196 -0.07096 -0.10112 356 LYS A O   
2743 C CB  . LYS A 383 ? 2.37988 2.24819 1.72223 -0.15670 -0.15401 -0.05512 356 LYS A CB  
2744 C CG  . LYS A 383 ? 2.45832 2.33248 1.75261 -0.18889 -0.11940 -0.08257 356 LYS A CG  
2745 C CD  . LYS A 383 ? 2.53216 2.40425 1.74858 -0.20858 -0.13910 -0.08715 356 LYS A CD  
2746 C CE  . LYS A 383 ? 2.56065 2.43904 1.72529 -0.24103 -0.09976 -0.11794 356 LYS A CE  
2747 N NZ  . LYS A 383 ? 2.23306 2.10664 1.30794 -0.26335 -0.11828 -0.12314 356 LYS A NZ  
2748 N N   . ILE A 384 ? 2.06104 1.99571 1.58899 -0.12415 -0.11517 -0.10469 357 ILE A N   
2749 C CA  . ILE A 384 ? 1.90279 1.86312 1.48642 -0.12145 -0.08834 -0.13524 357 ILE A CA  
2750 C C   . ILE A 384 ? 1.86524 1.82932 1.49921 -0.10622 -0.07044 -0.12917 357 ILE A C   
2751 O O   . ILE A 384 ? 1.93597 1.91359 1.58950 -0.11084 -0.04142 -0.14813 357 ILE A O   
2752 C CB  . ILE A 384 ? 1.74632 1.72678 1.37624 -0.11142 -0.10502 -0.14893 357 ILE A CB  
2753 C CG1 . ILE A 384 ? 2.08992 2.07053 1.66762 -0.13080 -0.12343 -0.16089 357 ILE A CG1 
2754 C CG2 . ILE A 384 ? 1.67144 1.66735 1.35828 -0.10541 -0.07864 -0.17565 357 ILE A CG2 
2755 C CD1 . ILE A 384 ? 2.26054 2.23719 1.78753 -0.15547 -0.09628 -0.18930 357 ILE A CD1 
2756 N N   . PHE A 385 ? 1.79117 1.74626 1.44776 -0.08706 -0.08808 -0.10460 358 PHE A N   
2757 C CA  . PHE A 385 ? 1.87478 1.83322 1.57307 -0.07398 -0.07355 -0.10063 358 PHE A CA  
2758 C C   . PHE A 385 ? 1.85954 1.80261 1.52261 -0.09219 -0.05320 -0.09837 358 PHE A C   
2759 O O   . PHE A 385 ? 1.82213 1.78174 1.51811 -0.09145 -0.03261 -0.10926 358 PHE A O   
2760 C CB  . PHE A 385 ? 1.85653 1.80697 1.58096 -0.05051 -0.09438 -0.07853 358 PHE A CB  
2761 C CG  . PHE A 385 ? 1.79899 1.75176 1.55851 -0.03848 -0.08090 -0.07662 358 PHE A CG  
2762 C CD1 . PHE A 385 ? 1.76602 1.74558 1.58093 -0.02407 -0.07287 -0.08672 358 PHE A CD1 
2763 C CD2 . PHE A 385 ? 1.77206 1.69714 1.50474 -0.04374 -0.07682 -0.06472 358 PHE A CD2 
2764 C CE1 . PHE A 385 ? 1.65223 1.63615 1.49217 -0.01398 -0.06324 -0.08516 358 PHE A CE1 
2765 C CE2 . PHE A 385 ? 1.76804 1.69705 1.52985 -0.03555 -0.06617 -0.06682 358 PHE A CE2 
2766 C CZ  . PHE A 385 ? 1.59304 1.55415 1.40706 -0.02010 -0.06045 -0.07719 358 PHE A CZ  
2767 N N   . GLU A 386 ? 1.96930 1.88142 1.56547 -0.10994 -0.05960 -0.08302 359 GLU A N   
2768 C CA  . GLU A 386 ? 1.81809 1.71330 1.37745 -0.13396 -0.03701 -0.08034 359 GLU A CA  
2769 C C   . GLU A 386 ? 1.93942 1.86649 1.50003 -0.15427 -0.00485 -0.11006 359 GLU A C   
2770 O O   . GLU A 386 ? 1.86383 1.80505 1.44061 -0.16631 0.02054  -0.11966 359 GLU A O   
2771 C CB  . GLU A 386 ? 2.19644 2.04365 1.67641 -0.14953 -0.05130 -0.05296 359 GLU A CB  
2772 C CG  . GLU A 386 ? 1.91458 1.72365 1.39466 -0.12790 -0.07907 -0.02306 359 GLU A CG  
2773 C CD  . GLU A 386 ? 1.96524 1.75541 1.46589 -0.12799 -0.06510 -0.01861 359 GLU A CD  
2774 O OE1 . GLU A 386 ? 1.95689 1.76185 1.46212 -0.15051 -0.03568 -0.03434 359 GLU A OE1 
2775 O OE2 . GLU A 386 ? 2.25499 2.01797 1.76942 -0.10571 -0.08351 -0.00176 359 GLU A OE2 
2776 N N   . ARG A 387 ? 2.03378 1.97504 1.58057 -0.15838 -0.00528 -0.12763 360 ARG A N   
2777 C CA  . ARG A 387 ? 1.94766 1.92051 1.50353 -0.17222 0.02712  -0.16123 360 ARG A CA  
2778 C C   . ARG A 387 ? 1.94727 1.95546 1.58743 -0.15126 0.04064  -0.17968 360 ARG A C   
2779 O O   . ARG A 387 ? 2.12018 2.15663 1.78262 -0.15966 0.06968  -0.19935 360 ARG A O   
2780 C CB  . ARG A 387 ? 2.10746 2.08354 1.63421 -0.17799 0.02157  -0.18006 360 ARG A CB  
2781 C CG  . ARG A 387 ? 2.02298 2.02896 1.56197 -0.18815 0.05651  -0.22002 360 ARG A CG  
2782 C CD  . ARG A 387 ? 1.92016 1.92886 1.46002 -0.18348 0.04737  -0.24431 360 ARG A CD  
2783 N NE  . ARG A 387 ? 1.67018 1.68165 1.27762 -0.15509 0.02624  -0.24046 360 ARG A NE  
2784 C CZ  . ARG A 387 ? 1.96997 1.98054 1.59298 -0.14971 0.01497  -0.25847 360 ARG A CZ  
2785 N NH1 . ARG A 387 ? 2.29506 2.30213 1.87088 -0.16899 0.02032  -0.28473 360 ARG A NH1 
2786 N NH2 . ARG A 387 ? 1.76801 1.78002 1.45255 -0.12716 -0.00082 -0.25102 360 ARG A NH2 
2787 N N   . ASP A 388 ? 1.77348 1.78300 1.46168 -0.12386 0.01964  -0.17260 361 ASP A N   
2788 C CA  . ASP A 388 ? 1.84762 1.88546 1.60836 -0.10257 0.02888  -0.18506 361 ASP A CA  
2789 C C   . ASP A 388 ? 1.72647 1.77311 1.50893 -0.10085 0.03498  -0.17472 361 ASP A C   
2790 O O   . ASP A 388 ? 1.68216 1.76127 1.51317 -0.09242 0.04956  -0.18957 361 ASP A O   
2791 C CB  . ASP A 388 ? 1.92212 1.95578 1.72041 -0.07821 0.00696  -0.17765 361 ASP A CB  
2792 C CG  . ASP A 388 ? 1.88871 1.91873 1.67906 -0.08153 0.00259  -0.19467 361 ASP A CG  
2793 O OD1 . ASP A 388 ? 2.09054 2.11863 1.83738 -0.10188 0.01401  -0.21151 361 ASP A OD1 
2794 O OD2 . ASP A 388 ? 1.52031 1.54907 1.34581 -0.06641 -0.01091 -0.19251 361 ASP A OD2 
2795 N N   . TRP A 389 ? 1.82415 1.84158 1.57241 -0.10802 0.02243  -0.15045 362 TRP A N   
2796 C CA  . TRP A 389 ? 1.93016 1.95012 1.69791 -0.10740 0.02534  -0.14265 362 TRP A CA  
2797 C C   . TRP A 389 ? 1.86395 1.90676 1.62935 -0.13315 0.05290  -0.15786 362 TRP A C   
2798 O O   . TRP A 389 ? 1.96398 2.03576 1.77216 -0.13016 0.06016  -0.16590 362 TRP A O   
2799 C CB  . TRP A 389 ? 2.09329 2.06762 1.82368 -0.10792 0.00611  -0.11541 362 TRP A CB  
2800 C CG  . TRP A 389 ? 1.97632 1.94439 1.71937 -0.11049 0.00889  -0.11039 362 TRP A CG  
2801 C CD1 . TRP A 389 ? 2.09974 2.04446 1.80884 -0.13753 0.01967  -0.10514 362 TRP A CD1 
2802 C CD2 . TRP A 389 ? 1.87502 1.85798 1.66389 -0.08814 0.00098  -0.11131 362 TRP A CD2 
2803 N NE1 . TRP A 389 ? 2.30210 2.24645 2.03626 -0.13371 0.01777  -0.10574 362 TRP A NE1 
2804 C CE2 . TRP A 389 ? 2.10459 2.07380 1.88523 -0.10276 0.00593  -0.10976 362 TRP A CE2 
2805 C CE3 . TRP A 389 ? 1.79815 1.80256 1.62987 -0.05978 -0.00891 -0.11300 362 TRP A CE3 
2806 C CZ2 . TRP A 389 ? 1.95369 1.93280 1.76523 -0.08882 -0.00031 -0.11258 362 TRP A CZ2 
2807 C CZ3 . TRP A 389 ? 1.87389 1.88749 1.73316 -0.04572 -0.01361 -0.11213 362 TRP A CZ3 
2808 C CH2 . TRP A 389 ? 1.87663 1.87905 1.72466 -0.05962 -0.01012 -0.11325 362 TRP A CH2 
2809 N N   . VAL A 390 ? 1.66181 1.69622 1.37757 -0.16013 0.06862  -0.16261 363 VAL A N   
2810 C CA  . VAL A 390 ? 1.83420 1.89194 1.54430 -0.19028 0.09904  -0.17635 363 VAL A CA  
2811 C C   . VAL A 390 ? 2.01106 2.11956 1.75632 -0.18823 0.12365  -0.20973 363 VAL A C   
2812 O O   . VAL A 390 ? 2.39368 2.53204 2.13726 -0.21331 0.15418  -0.22725 363 VAL A O   
2813 C CB  . VAL A 390 ? 2.16478 2.17869 1.79158 -0.22505 0.10572  -0.15877 363 VAL A CB  
2814 C CG1 . VAL A 390 ? 2.34481 2.30284 1.94276 -0.22233 0.08110  -0.12640 363 VAL A CG1 
2815 C CG2 . VAL A 390 ? 2.20414 2.20329 1.77868 -0.22849 0.10254  -0.16055 363 VAL A CG2 
2816 N N   . SER A 391 ? 1.79470 1.91215 1.57369 -0.15894 0.11245  -0.21975 364 SER A N   
2817 C CA  . SER A 391 ? 1.75720 1.91404 1.57259 -0.15153 0.13454  -0.25300 364 SER A CA  
2818 C C   . SER A 391 ? 1.84723 2.05935 1.73518 -0.14250 0.15017  -0.26989 364 SER A C   
2819 O O   . SER A 391 ? 1.92585 2.14577 1.84276 -0.13535 0.13686  -0.25596 364 SER A O   
2820 C CB  . SER A 391 ? 1.81540 1.95943 1.65223 -0.12278 0.11703  -0.25767 364 SER A CB  
2821 O OG  . SER A 391 ? 1.81227 1.98644 1.68825 -0.11193 0.13821  -0.29105 364 SER A OG  
2822 N N   . SER A 392 ? 1.78850 2.04218 1.70654 -0.14238 0.17838  -0.30252 365 SER A N   
2823 C CA  . SER A 392 ? 1.97688 2.29290 1.97283 -0.13005 0.19188  -0.32124 365 SER A CA  
2824 C C   . SER A 392 ? 1.83975 2.16191 1.89775 -0.08724 0.16662  -0.31528 365 SER A C   
2825 O O   . SER A 392 ? 2.02909 2.39213 2.14223 -0.07520 0.16095  -0.31510 365 SER A O   
2826 C CB  . SER A 392 ? 2.04270 2.40310 2.06011 -0.13589 0.22970  -0.35999 365 SER A CB  
2827 O OG  . SER A 392 ? 1.77001 2.11079 1.79049 -0.11243 0.22915  -0.37667 365 SER A OG  
2828 N N   . HIS A 393 ? 1.59306 1.87530 1.64065 -0.06628 0.15049  -0.30945 366 HIS A N   
2829 C CA  . HIS A 393 ? 1.69697 1.97509 1.79293 -0.02916 0.12738  -0.29842 366 HIS A CA  
2830 C C   . HIS A 393 ? 1.86959 2.13066 1.95531 -0.02683 0.10045  -0.26610 366 HIS A C   
2831 O O   . HIS A 393 ? 2.02406 2.28624 2.14533 0.00096  0.08228  -0.25422 366 HIS A O   
2832 C CB  . HIS A 393 ? 1.77531 2.01187 1.86048 -0.01426 0.12052  -0.30160 366 HIS A CB  
2833 C CG  . HIS A 393 ? 1.89939 2.14303 1.98551 -0.01755 0.14714  -0.33722 366 HIS A CG  
2834 N ND1 . HIS A 393 ? 1.95321 2.23285 2.10212 0.00562  0.16460  -0.36424 366 HIS A ND1 
2835 C CD2 . HIS A 393 ? 1.86278 2.08237 1.89331 -0.04018 0.15904  -0.35210 366 HIS A CD2 
2836 C CE1 . HIS A 393 ? 1.98485 2.26069 2.11778 -0.00270 0.18952  -0.39695 366 HIS A CE1 
2837 N NE2 . HIS A 393 ? 1.67471 1.91445 1.73242 -0.03220 0.18635  -0.39039 366 HIS A NE2 
2838 N N   . SER A 394 ? 1.81430 2.05613 1.84959 -0.05479 0.09840  -0.25178 367 SER A N   
2839 C CA  . SER A 394 ? 1.72914 1.95014 1.75091 -0.05339 0.07585  -0.22535 367 SER A CA  
2840 C C   . SER A 394 ? 1.96618 2.22348 2.00682 -0.06893 0.08220  -0.22985 367 SER A C   
2841 O O   . SER A 394 ? 2.03894 2.28469 2.04192 -0.10055 0.09186  -0.22722 367 SER A O   
2842 C CB  . SER A 394 ? 1.74616 1.91457 1.70245 -0.06996 0.06635  -0.20619 367 SER A CB  
2843 O OG  . SER A 394 ? 1.67356 1.81688 1.61757 -0.05850 0.05844  -0.20474 367 SER A OG  
2844 N N   . LYS A 395 ? 1.88941 2.18985 1.98805 -0.04777 0.07542  -0.23601 368 LYS A N   
2845 C CA  . LYS A 395 ? 1.91321 2.25375 2.03552 -0.06193 0.07543  -0.24121 368 LYS A CA  
2846 C C   . LYS A 395 ? 1.97556 2.28464 2.07199 -0.06206 0.05244  -0.21991 368 LYS A C   
2847 O O   . LYS A 395 ? 1.83531 2.11503 1.92309 -0.03801 0.03418  -0.20312 368 LYS A O   
2848 C CB  . LYS A 395 ? 1.84386 2.25086 2.04099 -0.03768 0.07373  -0.25746 368 LYS A CB  
2849 C CG  . LYS A 395 ? 2.14073 2.59373 2.37476 -0.04135 0.10205  -0.28617 368 LYS A CG  
2850 C CD  . LYS A 395 ? 2.51045 3.03927 2.82644 -0.01867 0.09796  -0.30238 368 LYS A CD  
2851 C CE  . LYS A 395 ? 2.14321 2.72668 2.50269 -0.02381 0.13071  -0.33536 368 LYS A CE  
2852 N NZ  . LYS A 395 ? 1.69977 2.36689 2.14847 -0.00025 0.12515  -0.35220 368 LYS A NZ  
2853 N N   . SER A 396 ? 2.01323 2.32779 2.09720 -0.09145 0.05596  -0.22264 369 SER A N   
2854 C CA  . SER A 396 ? 1.78664 2.06800 1.84362 -0.09419 0.03735  -0.20806 369 SER A CA  
2855 C C   . SER A 396 ? 1.81721 2.13020 1.91130 -0.06528 0.01557  -0.20653 369 SER A C   
2856 O O   . SER A 396 ? 1.66458 2.03649 1.81176 -0.05202 0.01388  -0.21897 369 SER A O   
2857 C CB  . SER A 396 ? 2.05300 2.33276 2.09307 -0.13482 0.04731  -0.21547 369 SER A CB  
2858 O OG  . SER A 396 ? 2.40016 2.75202 2.49285 -0.14871 0.05892  -0.23818 369 SER A OG  
2859 N N   . LEU A 397 ? 1.93653 2.21044 2.00100 -0.05419 -0.00128 -0.19068 370 LEU A N   
2860 C CA  . LEU A 397 ? 1.89629 2.19316 1.98080 -0.02910 -0.02173 -0.18609 370 LEU A CA  
2861 C C   . LEU A 397 ? 1.90922 2.25489 2.01781 -0.04499 -0.02910 -0.20240 370 LEU A C   
2862 O O   . LEU A 397 ? 2.14526 2.47555 2.23132 -0.07614 -0.02454 -0.21054 370 LEU A O   
2863 C CB  . LEU A 397 ? 1.92121 2.16666 1.96427 -0.01794 -0.03264 -0.16877 370 LEU A CB  
2864 C CG  . LEU A 397 ? 1.78376 2.04783 1.83163 0.00175  -0.05164 -0.16392 370 LEU A CG  
2865 C CD1 . LEU A 397 ? 1.57574 1.86688 1.65646 0.03264  -0.05888 -0.15431 370 LEU A CD1 
2866 C CD2 . LEU A 397 ? 1.63015 1.84556 1.63483 0.00706  -0.05587 -0.15257 370 LEU A CD2 
2867 N N   . LYS A 398 ? 1.68732 2.09064 1.84251 -0.02379 -0.04217 -0.20694 371 LYS A N   
2868 C CA  . LYS A 398 ? 1.89424 2.35708 2.08051 -0.03555 -0.05497 -0.22324 371 LYS A CA  
2869 C C   . LYS A 398 ? 1.92177 2.40865 2.11818 -0.00282 -0.08314 -0.21235 371 LYS A C   
2870 O O   . LYS A 398 ? 1.92032 2.40884 2.13383 0.03105  -0.08840 -0.19809 371 LYS A O   
2871 C CB  . LYS A 398 ? 2.05324 2.58423 2.30013 -0.04600 -0.04186 -0.24426 371 LYS A CB  
2872 C CG  . LYS A 398 ? 2.09481 2.60617 2.32625 -0.08305 -0.01109 -0.25472 371 LYS A CG  
2873 C CD  . LYS A 398 ? 2.07251 2.65884 2.36703 -0.09299 0.00657  -0.27794 371 LYS A CD  
2874 C CE  . LYS A 398 ? 2.30162 2.86521 2.57018 -0.13306 0.04044  -0.28605 371 LYS A CE  
2875 N NZ  . LYS A 398 ? 2.47593 3.11775 2.80658 -0.14530 0.06372  -0.31164 371 LYS A NZ  
2876 N N   . ILE A 399 ? 2.10768 2.60846 2.28849 -0.01462 -0.10114 -0.21885 372 ILE A N   
2877 C CA  . ILE A 399 ? 2.19154 2.71553 2.36977 0.01238  -0.12985 -0.20803 372 ILE A CA  
2878 C C   . ILE A 399 ? 2.47817 3.07239 2.68537 -0.00325 -0.15106 -0.22874 372 ILE A C   
2879 O O   . ILE A 399 ? 2.69349 3.28789 2.88994 -0.04130 -0.14575 -0.24935 372 ILE A O   
2880 C CB  . ILE A 399 ? 1.92788 2.38878 2.03966 0.01775  -0.13324 -0.19278 372 ILE A CB  
2881 C CG1 . ILE A 399 ? 1.89537 2.29835 1.98816 0.03434  -0.11553 -0.17232 372 ILE A CG1 
2882 C CG2 . ILE A 399 ? 1.67850 2.16462 1.77703 0.04037  -0.16150 -0.18202 372 ILE A CG2 
2883 C CD1 . ILE A 399 ? 1.97060 2.31750 2.00711 0.03750  -0.11351 -0.16059 372 ILE A CD1 
2884 O OXT . ILE A 399 ? 2.52332 3.17507 2.76572 0.02109  -0.17562 -0.22520 372 ILE A OXT 
# 
