data_8XQY
# 
_entry.id   8XQY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8XQY         pdb_00008xqy 10.2210/pdb8xqy/pdb 
WWPDB D_1300044039 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8XQY 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gfyang@mail.ccnu.edu.cn 
_pdbx_contact_author.name_first         Guang-Fu 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4384-2593 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dong, J.'    1 ? 
'Lin, H.-Y.'  2 ? 
'Yang, G.-F.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of AtHPPD-Y181183 complex' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dong, J.'    1 ? 
primary 'Lin, H.-Y.'  2 ? 
primary 'Yang, G.-F.' 3 ? 
# 
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 '4-hydroxyphenylpyruvate dioxygenase'                                                                  45952.727 
1   1.13.11.27 ? ? ? 
2 non-polymer syn '4-(3-methylbut-2-enyl)-6-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-1,4-benzothiazin-3-one' 371.450   
1   ?          ? ? ? 
3 non-polymer syn 'COBALT (II) ION'                                                                                      58.933    
1   ?          ? ? ? 
4 water       nat water                                                                                                  18.015    
201 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '4-hydroxyphenylpyruvic acid oxidase,4HPPD,HPD,HPPDase' 
# 
_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       
;GSHMVRKNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLS
AGEIKPTTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLR
YVSYKAEDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSA
VLASNDEMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKK
RVGDVLSDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELF
KSIEEYEKTLEAKQLVG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSHMVRKNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLS
AGEIKPTTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLR
YVSYKAEDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSA
VLASNDEMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKK
RVGDVLSDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELF
KSIEEYEKTLEAKQLVG
;
_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 '4-(3-methylbut-2-enyl)-6-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-1,4-benzothiazin-3-one' A1LWP 
3 'COBALT (II) ION'                                                                                      CO    
4 water                                                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   HIS n 
1 4   MET n 
1 5   VAL n 
1 6   ARG n 
1 7   LYS n 
1 8   ASN n 
1 9   PRO n 
1 10  LYS n 
1 11  SER n 
1 12  ASP n 
1 13  LYS n 
1 14  PHE n 
1 15  LYS n 
1 16  VAL n 
1 17  LYS n 
1 18  ARG n 
1 19  PHE n 
1 20  HIS n 
1 21  HIS n 
1 22  ILE n 
1 23  GLU n 
1 24  PHE n 
1 25  TRP n 
1 26  CYS n 
1 27  GLY n 
1 28  ASP n 
1 29  ALA n 
1 30  THR n 
1 31  ASN n 
1 32  VAL n 
1 33  ALA n 
1 34  ARG n 
1 35  ARG n 
1 36  PHE n 
1 37  SER n 
1 38  TRP n 
1 39  GLY n 
1 40  LEU n 
1 41  GLY n 
1 42  MET n 
1 43  ARG n 
1 44  PHE n 
1 45  SER n 
1 46  ALA n 
1 47  LYS n 
1 48  SER n 
1 49  ASP n 
1 50  LEU n 
1 51  SER n 
1 52  THR n 
1 53  GLY n 
1 54  ASN n 
1 55  MET n 
1 56  VAL n 
1 57  HIS n 
1 58  ALA n 
1 59  SER n 
1 60  TYR n 
1 61  LEU n 
1 62  LEU n 
1 63  THR n 
1 64  SER n 
1 65  GLY n 
1 66  ASP n 
1 67  LEU n 
1 68  ARG n 
1 69  PHE n 
1 70  LEU n 
1 71  PHE n 
1 72  THR n 
1 73  ALA n 
1 74  PRO n 
1 75  TYR n 
1 76  SER n 
1 77  PRO n 
1 78  SER n 
1 79  LEU n 
1 80  SER n 
1 81  ALA n 
1 82  GLY n 
1 83  GLU n 
1 84  ILE n 
1 85  LYS n 
1 86  PRO n 
1 87  THR n 
1 88  THR n 
1 89  THR n 
1 90  ALA n 
1 91  SER n 
1 92  ILE n 
1 93  PRO n 
1 94  SER n 
1 95  PHE n 
1 96  ASP n 
1 97  HIS n 
1 98  GLY n 
1 99  SER n 
1 100 CYS n 
1 101 ARG n 
1 102 SER n 
1 103 PHE n 
1 104 PHE n 
1 105 SER n 
1 106 SER n 
1 107 HIS n 
1 108 GLY n 
1 109 LEU n 
1 110 GLY n 
1 111 VAL n 
1 112 ARG n 
1 113 ALA n 
1 114 VAL n 
1 115 ALA n 
1 116 ILE n 
1 117 GLU n 
1 118 VAL n 
1 119 GLU n 
1 120 ASP n 
1 121 ALA n 
1 122 GLU n 
1 123 SER n 
1 124 ALA n 
1 125 PHE n 
1 126 SER n 
1 127 ILE n 
1 128 SER n 
1 129 VAL n 
1 130 ALA n 
1 131 ASN n 
1 132 GLY n 
1 133 ALA n 
1 134 ILE n 
1 135 PRO n 
1 136 SER n 
1 137 SER n 
1 138 PRO n 
1 139 PRO n 
1 140 ILE n 
1 141 VAL n 
1 142 LEU n 
1 143 ASN n 
1 144 GLU n 
1 145 ALA n 
1 146 VAL n 
1 147 THR n 
1 148 ILE n 
1 149 ALA n 
1 150 GLU n 
1 151 VAL n 
1 152 LYS n 
1 153 LEU n 
1 154 TYR n 
1 155 GLY n 
1 156 ASP n 
1 157 VAL n 
1 158 VAL n 
1 159 LEU n 
1 160 ARG n 
1 161 TYR n 
1 162 VAL n 
1 163 SER n 
1 164 TYR n 
1 165 LYS n 
1 166 ALA n 
1 167 GLU n 
1 168 ASP n 
1 169 THR n 
1 170 GLU n 
1 171 LYS n 
1 172 SER n 
1 173 GLU n 
1 174 PHE n 
1 175 LEU n 
1 176 PRO n 
1 177 GLY n 
1 178 PHE n 
1 179 GLU n 
1 180 ARG n 
1 181 VAL n 
1 182 GLU n 
1 183 ASP n 
1 184 ALA n 
1 185 SER n 
1 186 SER n 
1 187 PHE n 
1 188 PRO n 
1 189 LEU n 
1 190 ASP n 
1 191 TYR n 
1 192 GLY n 
1 193 ILE n 
1 194 ARG n 
1 195 ARG n 
1 196 LEU n 
1 197 ASP n 
1 198 HIS n 
1 199 ALA n 
1 200 VAL n 
1 201 GLY n 
1 202 ASN n 
1 203 VAL n 
1 204 PRO n 
1 205 GLU n 
1 206 LEU n 
1 207 GLY n 
1 208 PRO n 
1 209 ALA n 
1 210 LEU n 
1 211 THR n 
1 212 TYR n 
1 213 VAL n 
1 214 ALA n 
1 215 GLY n 
1 216 PHE n 
1 217 THR n 
1 218 GLY n 
1 219 PHE n 
1 220 HIS n 
1 221 GLN n 
1 222 PHE n 
1 223 ALA n 
1 224 GLU n 
1 225 PHE n 
1 226 THR n 
1 227 ALA n 
1 228 ASP n 
1 229 ASP n 
1 230 VAL n 
1 231 GLY n 
1 232 THR n 
1 233 ALA n 
1 234 GLU n 
1 235 SER n 
1 236 GLY n 
1 237 LEU n 
1 238 ASN n 
1 239 SER n 
1 240 ALA n 
1 241 VAL n 
1 242 LEU n 
1 243 ALA n 
1 244 SER n 
1 245 ASN n 
1 246 ASP n 
1 247 GLU n 
1 248 MET n 
1 249 VAL n 
1 250 LEU n 
1 251 LEU n 
1 252 PRO n 
1 253 ILE n 
1 254 ASN n 
1 255 GLU n 
1 256 PRO n 
1 257 VAL n 
1 258 HIS n 
1 259 GLY n 
1 260 THR n 
1 261 LYS n 
1 262 ARG n 
1 263 LYS n 
1 264 SER n 
1 265 GLN n 
1 266 ILE n 
1 267 GLN n 
1 268 THR n 
1 269 TYR n 
1 270 LEU n 
1 271 GLU n 
1 272 HIS n 
1 273 ASN n 
1 274 GLU n 
1 275 GLY n 
1 276 ALA n 
1 277 GLY n 
1 278 LEU n 
1 279 GLN n 
1 280 HIS n 
1 281 LEU n 
1 282 ALA n 
1 283 LEU n 
1 284 MET n 
1 285 SER n 
1 286 GLU n 
1 287 ASP n 
1 288 ILE n 
1 289 PHE n 
1 290 ARG n 
1 291 THR n 
1 292 LEU n 
1 293 ARG n 
1 294 GLU n 
1 295 MET n 
1 296 ARG n 
1 297 LYS n 
1 298 ARG n 
1 299 SER n 
1 300 SER n 
1 301 ILE n 
1 302 GLY n 
1 303 GLY n 
1 304 PHE n 
1 305 ASP n 
1 306 PHE n 
1 307 MET n 
1 308 PRO n 
1 309 SER n 
1 310 PRO n 
1 311 PRO n 
1 312 PRO n 
1 313 THR n 
1 314 TYR n 
1 315 TYR n 
1 316 GLN n 
1 317 ASN n 
1 318 LEU n 
1 319 LYS n 
1 320 LYS n 
1 321 ARG n 
1 322 VAL n 
1 323 GLY n 
1 324 ASP n 
1 325 VAL n 
1 326 LEU n 
1 327 SER n 
1 328 ASP n 
1 329 ASP n 
1 330 GLN n 
1 331 ILE n 
1 332 LYS n 
1 333 GLU n 
1 334 CYS n 
1 335 GLU n 
1 336 GLU n 
1 337 LEU n 
1 338 GLY n 
1 339 ILE n 
1 340 LEU n 
1 341 VAL n 
1 342 ASP n 
1 343 ARG n 
1 344 ASP n 
1 345 ASP n 
1 346 GLN n 
1 347 GLY n 
1 348 THR n 
1 349 LEU n 
1 350 LEU n 
1 351 GLN n 
1 352 ILE n 
1 353 PHE n 
1 354 THR n 
1 355 LYS n 
1 356 PRO n 
1 357 LEU n 
1 358 GLY n 
1 359 ASP n 
1 360 ARG n 
1 361 PRO n 
1 362 THR n 
1 363 ILE n 
1 364 PHE n 
1 365 ILE n 
1 366 GLU n 
1 367 ILE n 
1 368 ILE n 
1 369 GLN n 
1 370 ARG n 
1 371 VAL n 
1 372 GLY n 
1 373 CYS n 
1 374 MET n 
1 375 MET n 
1 376 LYS n 
1 377 ASP n 
1 378 GLU n 
1 379 GLU n 
1 380 GLY n 
1 381 LYS n 
1 382 ALA n 
1 383 TYR n 
1 384 GLN n 
1 385 SER n 
1 386 GLY n 
1 387 GLY n 
1 388 CYS n 
1 389 GLY n 
1 390 GLY n 
1 391 PHE n 
1 392 GLY n 
1 393 LYS n 
1 394 GLY n 
1 395 ASN n 
1 396 PHE n 
1 397 SER n 
1 398 GLU n 
1 399 LEU n 
1 400 PHE n 
1 401 LYS n 
1 402 SER n 
1 403 ILE n 
1 404 GLU n 
1 405 GLU n 
1 406 TYR n 
1 407 GLU n 
1 408 LYS n 
1 409 THR n 
1 410 LEU n 
1 411 GLU n 
1 412 ALA n 
1 413 LYS n 
1 414 GLN n 
1 415 LEU n 
1 416 VAL n 
1 417 GLY 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                   417 
_entity_src_gen.gene_src_common_name               'thale cress' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HPD, PDS1, At1g06570, F12K11.9' 
_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      'Arabidopsis thaliana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1LWP non-polymer         . '4-(3-methylbut-2-enyl)-6-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-1,4-benzothiazin-3-one' 
? 'C20 H21 N O4 S' 371.450 
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 
CO    non-polymer         . 'COBALT (II) ION'                                                                                      
? 'Co 2'           58.933  
CYS   'L-peptide linking' y CYSTEINE                                                                                               
? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                              
? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                        
? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                                
? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                              
? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                                  
? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                             
? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                                
? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                                 
? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                             
? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                          
? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                                
? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                                 
? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                              
? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                             
? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                               
? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                                 
? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   29  ?   ?   ?   A . n 
A 1 2   SER 2   30  ?   ?   ?   A . n 
A 1 3   HIS 3   31  ?   ?   ?   A . n 
A 1 4   MET 4   32  ?   ?   ?   A . n 
A 1 5   VAL 5   33  ?   ?   ?   A . n 
A 1 6   ARG 6   34  ?   ?   ?   A . n 
A 1 7   LYS 7   35  35  LYS LYS A . n 
A 1 8   ASN 8   36  36  ASN ASN A . n 
A 1 9   PRO 9   37  37  PRO PRO A . n 
A 1 10  LYS 10  38  38  LYS LYS A . n 
A 1 11  SER 11  39  39  SER SER A . n 
A 1 12  ASP 12  40  40  ASP ASP A . n 
A 1 13  LYS 13  41  41  LYS LYS A . n 
A 1 14  PHE 14  42  42  PHE PHE A . n 
A 1 15  LYS 15  43  43  LYS LYS A . n 
A 1 16  VAL 16  44  44  VAL VAL A . n 
A 1 17  LYS 17  45  45  LYS LYS A . n 
A 1 18  ARG 18  46  46  ARG ARG A . n 
A 1 19  PHE 19  47  47  PHE PHE A . n 
A 1 20  HIS 20  48  48  HIS HIS A . n 
A 1 21  HIS 21  49  49  HIS HIS A . n 
A 1 22  ILE 22  50  50  ILE ILE A . n 
A 1 23  GLU 23  51  51  GLU GLU A . n 
A 1 24  PHE 24  52  52  PHE PHE A . n 
A 1 25  TRP 25  53  53  TRP TRP A . n 
A 1 26  CYS 26  54  54  CYS CYS A . n 
A 1 27  GLY 27  55  55  GLY GLY A . n 
A 1 28  ASP 28  56  56  ASP ASP A . n 
A 1 29  ALA 29  57  57  ALA ALA A . n 
A 1 30  THR 30  58  58  THR THR A . n 
A 1 31  ASN 31  59  59  ASN ASN A . n 
A 1 32  VAL 32  60  60  VAL VAL A . n 
A 1 33  ALA 33  61  61  ALA ALA A . n 
A 1 34  ARG 34  62  62  ARG ARG A . n 
A 1 35  ARG 35  63  63  ARG ARG A . n 
A 1 36  PHE 36  64  64  PHE PHE A . n 
A 1 37  SER 37  65  65  SER SER A . n 
A 1 38  TRP 38  66  66  TRP TRP A . n 
A 1 39  GLY 39  67  67  GLY GLY A . n 
A 1 40  LEU 40  68  68  LEU LEU A . n 
A 1 41  GLY 41  69  69  GLY GLY A . n 
A 1 42  MET 42  70  70  MET MET A . n 
A 1 43  ARG 43  71  71  ARG ARG A . n 
A 1 44  PHE 44  72  72  PHE PHE A . n 
A 1 45  SER 45  73  73  SER SER A . n 
A 1 46  ALA 46  74  74  ALA ALA A . n 
A 1 47  LYS 47  75  75  LYS LYS A . n 
A 1 48  SER 48  76  76  SER SER A . n 
A 1 49  ASP 49  77  77  ASP ASP A . n 
A 1 50  LEU 50  78  78  LEU LEU A . n 
A 1 51  SER 51  79  79  SER SER A . n 
A 1 52  THR 52  80  80  THR THR A . n 
A 1 53  GLY 53  81  81  GLY GLY A . n 
A 1 54  ASN 54  82  82  ASN ASN A . n 
A 1 55  MET 55  83  83  MET MET A . n 
A 1 56  VAL 56  84  84  VAL VAL A . n 
A 1 57  HIS 57  85  85  HIS HIS A . n 
A 1 58  ALA 58  86  86  ALA ALA A . n 
A 1 59  SER 59  87  87  SER SER A . n 
A 1 60  TYR 60  88  88  TYR TYR A . n 
A 1 61  LEU 61  89  89  LEU LEU A . n 
A 1 62  LEU 62  90  90  LEU LEU A . n 
A 1 63  THR 63  91  91  THR THR A . n 
A 1 64  SER 64  92  92  SER SER A . n 
A 1 65  GLY 65  93  93  GLY GLY A . n 
A 1 66  ASP 66  94  94  ASP ASP A . n 
A 1 67  LEU 67  95  95  LEU LEU A . n 
A 1 68  ARG 68  96  96  ARG ARG A . n 
A 1 69  PHE 69  97  97  PHE PHE A . n 
A 1 70  LEU 70  98  98  LEU LEU A . n 
A 1 71  PHE 71  99  99  PHE PHE A . n 
A 1 72  THR 72  100 100 THR THR A . n 
A 1 73  ALA 73  101 101 ALA ALA A . n 
A 1 74  PRO 74  102 102 PRO PRO A . n 
A 1 75  TYR 75  103 103 TYR TYR A . n 
A 1 76  SER 76  104 104 SER SER A . n 
A 1 77  PRO 77  105 105 PRO PRO A . n 
A 1 78  SER 78  106 106 SER SER A . n 
A 1 79  LEU 79  107 107 LEU LEU A . n 
A 1 80  SER 80  108 108 SER SER A . n 
A 1 81  ALA 81  109 109 ALA ALA A . n 
A 1 82  GLY 82  110 110 GLY GLY A . n 
A 1 83  GLU 83  111 111 GLU GLU A . n 
A 1 84  ILE 84  112 112 ILE ILE A . n 
A 1 85  LYS 85  113 113 LYS LYS A . n 
A 1 86  PRO 86  114 114 PRO PRO A . n 
A 1 87  THR 87  115 115 THR THR A . n 
A 1 88  THR 88  116 116 THR THR A . n 
A 1 89  THR 89  117 117 THR THR A . n 
A 1 90  ALA 90  118 118 ALA ALA A . n 
A 1 91  SER 91  119 119 SER SER A . n 
A 1 92  ILE 92  120 120 ILE ILE A . n 
A 1 93  PRO 93  121 121 PRO PRO A . n 
A 1 94  SER 94  122 122 SER SER A . n 
A 1 95  PHE 95  123 123 PHE PHE A . n 
A 1 96  ASP 96  124 124 ASP ASP A . n 
A 1 97  HIS 97  125 125 HIS HIS A . n 
A 1 98  GLY 98  126 126 GLY GLY A . n 
A 1 99  SER 99  127 127 SER SER A . n 
A 1 100 CYS 100 128 128 CYS CYS A . n 
A 1 101 ARG 101 129 129 ARG ARG A . n 
A 1 102 SER 102 130 130 SER SER A . n 
A 1 103 PHE 103 131 131 PHE PHE A . n 
A 1 104 PHE 104 132 132 PHE PHE A . n 
A 1 105 SER 105 133 133 SER SER A . n 
A 1 106 SER 106 134 134 SER SER A . n 
A 1 107 HIS 107 135 135 HIS HIS A . n 
A 1 108 GLY 108 136 136 GLY GLY A . n 
A 1 109 LEU 109 137 137 LEU LEU A . n 
A 1 110 GLY 110 138 138 GLY GLY A . n 
A 1 111 VAL 111 139 139 VAL VAL A . n 
A 1 112 ARG 112 140 140 ARG ARG A . n 
A 1 113 ALA 113 141 141 ALA ALA A . n 
A 1 114 VAL 114 142 142 VAL VAL A . n 
A 1 115 ALA 115 143 143 ALA ALA A . n 
A 1 116 ILE 116 144 144 ILE ILE A . n 
A 1 117 GLU 117 145 145 GLU GLU A . n 
A 1 118 VAL 118 146 146 VAL VAL A . n 
A 1 119 GLU 119 147 147 GLU GLU A . n 
A 1 120 ASP 120 148 148 ASP ASP A . n 
A 1 121 ALA 121 149 149 ALA ALA A . n 
A 1 122 GLU 122 150 150 GLU GLU A . n 
A 1 123 SER 123 151 151 SER SER A . n 
A 1 124 ALA 124 152 152 ALA ALA A . n 
A 1 125 PHE 125 153 153 PHE PHE A . n 
A 1 126 SER 126 154 154 SER SER A . n 
A 1 127 ILE 127 155 155 ILE ILE A . n 
A 1 128 SER 128 156 156 SER SER A . n 
A 1 129 VAL 129 157 157 VAL VAL A . n 
A 1 130 ALA 130 158 158 ALA ALA A . n 
A 1 131 ASN 131 159 159 ASN ASN A . n 
A 1 132 GLY 132 160 160 GLY GLY A . n 
A 1 133 ALA 133 161 161 ALA ALA A . n 
A 1 134 ILE 134 162 162 ILE ILE A . n 
A 1 135 PRO 135 163 163 PRO PRO A . n 
A 1 136 SER 136 164 164 SER SER A . n 
A 1 137 SER 137 165 165 SER SER A . n 
A 1 138 PRO 138 166 166 PRO PRO A . n 
A 1 139 PRO 139 167 167 PRO PRO A . n 
A 1 140 ILE 140 168 168 ILE ILE A . n 
A 1 141 VAL 141 169 169 VAL VAL A . n 
A 1 142 LEU 142 170 170 LEU LEU A . n 
A 1 143 ASN 143 171 171 ASN ASN A . n 
A 1 144 GLU 144 172 172 GLU GLU A . n 
A 1 145 ALA 145 173 173 ALA ALA A . n 
A 1 146 VAL 146 174 174 VAL VAL A . n 
A 1 147 THR 147 175 175 THR THR A . n 
A 1 148 ILE 148 176 176 ILE ILE A . n 
A 1 149 ALA 149 177 177 ALA ALA A . n 
A 1 150 GLU 150 178 178 GLU GLU A . n 
A 1 151 VAL 151 179 179 VAL VAL A . n 
A 1 152 LYS 152 180 180 LYS LYS A . n 
A 1 153 LEU 153 181 181 LEU LEU A . n 
A 1 154 TYR 154 182 182 TYR TYR A . n 
A 1 155 GLY 155 183 183 GLY GLY A . n 
A 1 156 ASP 156 184 184 ASP ASP A . n 
A 1 157 VAL 157 185 185 VAL VAL A . n 
A 1 158 VAL 158 186 186 VAL VAL A . n 
A 1 159 LEU 159 187 187 LEU LEU A . n 
A 1 160 ARG 160 188 188 ARG ARG A . n 
A 1 161 TYR 161 189 189 TYR TYR A . n 
A 1 162 VAL 162 190 190 VAL VAL A . n 
A 1 163 SER 163 191 191 SER SER A . n 
A 1 164 TYR 164 192 192 TYR TYR A . n 
A 1 165 LYS 165 193 193 LYS LYS A . n 
A 1 166 ALA 166 194 194 ALA ALA A . n 
A 1 167 GLU 167 195 ?   ?   ?   A . n 
A 1 168 ASP 168 196 ?   ?   ?   A . n 
A 1 169 THR 169 197 ?   ?   ?   A . n 
A 1 170 GLU 170 198 ?   ?   ?   A . n 
A 1 171 LYS 171 199 ?   ?   ?   A . n 
A 1 172 SER 172 200 ?   ?   ?   A . n 
A 1 173 GLU 173 201 201 GLU GLU A . n 
A 1 174 PHE 174 202 202 PHE PHE A . n 
A 1 175 LEU 175 203 203 LEU LEU A . n 
A 1 176 PRO 176 204 204 PRO PRO A . n 
A 1 177 GLY 177 205 205 GLY GLY A . n 
A 1 178 PHE 178 206 206 PHE PHE A . n 
A 1 179 GLU 179 207 207 GLU GLU A . n 
A 1 180 ARG 180 208 208 ARG ARG A . n 
A 1 181 VAL 181 209 209 VAL VAL A . n 
A 1 182 GLU 182 210 210 GLU GLU A . n 
A 1 183 ASP 183 211 211 ASP ASP A . n 
A 1 184 ALA 184 212 212 ALA ALA A . n 
A 1 185 SER 185 213 213 SER SER A . n 
A 1 186 SER 186 214 214 SER SER A . n 
A 1 187 PHE 187 215 215 PHE PHE A . n 
A 1 188 PRO 188 216 216 PRO PRO A . n 
A 1 189 LEU 189 217 217 LEU LEU A . n 
A 1 190 ASP 190 218 218 ASP ASP A . n 
A 1 191 TYR 191 219 219 TYR TYR A . n 
A 1 192 GLY 192 220 220 GLY GLY A . n 
A 1 193 ILE 193 221 221 ILE ILE A . n 
A 1 194 ARG 194 222 222 ARG ARG A . n 
A 1 195 ARG 195 223 223 ARG ARG A . n 
A 1 196 LEU 196 224 224 LEU LEU A . n 
A 1 197 ASP 197 225 225 ASP ASP A . n 
A 1 198 HIS 198 226 226 HIS HIS A . n 
A 1 199 ALA 199 227 227 ALA ALA A . n 
A 1 200 VAL 200 228 228 VAL VAL A . n 
A 1 201 GLY 201 229 229 GLY GLY A . n 
A 1 202 ASN 202 230 230 ASN ASN A . n 
A 1 203 VAL 203 231 231 VAL VAL A . n 
A 1 204 PRO 204 232 232 PRO PRO A . n 
A 1 205 GLU 205 233 233 GLU GLU A . n 
A 1 206 LEU 206 234 234 LEU LEU A . n 
A 1 207 GLY 207 235 235 GLY GLY A . n 
A 1 208 PRO 208 236 236 PRO PRO A . n 
A 1 209 ALA 209 237 237 ALA ALA A . n 
A 1 210 LEU 210 238 238 LEU LEU A . n 
A 1 211 THR 211 239 239 THR THR A . n 
A 1 212 TYR 212 240 240 TYR TYR A . n 
A 1 213 VAL 213 241 241 VAL VAL A . n 
A 1 214 ALA 214 242 242 ALA ALA A . n 
A 1 215 GLY 215 243 243 GLY GLY A . n 
A 1 216 PHE 216 244 244 PHE PHE A . n 
A 1 217 THR 217 245 245 THR THR A . n 
A 1 218 GLY 218 246 246 GLY GLY A . n 
A 1 219 PHE 219 247 247 PHE PHE A . n 
A 1 220 HIS 220 248 248 HIS HIS A . n 
A 1 221 GLN 221 249 249 GLN GLN A . n 
A 1 222 PHE 222 250 250 PHE PHE A . n 
A 1 223 ALA 223 251 ?   ?   ?   A . n 
A 1 224 GLU 224 252 ?   ?   ?   A . n 
A 1 225 PHE 225 253 ?   ?   ?   A . n 
A 1 226 THR 226 254 ?   ?   ?   A . n 
A 1 227 ALA 227 255 ?   ?   ?   A . n 
A 1 228 ASP 228 256 ?   ?   ?   A . n 
A 1 229 ASP 229 257 ?   ?   ?   A . n 
A 1 230 VAL 230 258 ?   ?   ?   A . n 
A 1 231 GLY 231 259 ?   ?   ?   A . n 
A 1 232 THR 232 260 ?   ?   ?   A . n 
A 1 233 ALA 233 261 ?   ?   ?   A . n 
A 1 234 GLU 234 262 ?   ?   ?   A . n 
A 1 235 SER 235 263 263 SER SER A . n 
A 1 236 GLY 236 264 264 GLY GLY A . n 
A 1 237 LEU 237 265 265 LEU LEU A . n 
A 1 238 ASN 238 266 266 ASN ASN A . n 
A 1 239 SER 239 267 267 SER SER A . n 
A 1 240 ALA 240 268 268 ALA ALA A . n 
A 1 241 VAL 241 269 269 VAL VAL A . n 
A 1 242 LEU 242 270 270 LEU LEU A . n 
A 1 243 ALA 243 271 271 ALA ALA A . n 
A 1 244 SER 244 272 272 SER SER A . n 
A 1 245 ASN 245 273 273 ASN ASN A . n 
A 1 246 ASP 246 274 274 ASP ASP A . n 
A 1 247 GLU 247 275 275 GLU GLU A . n 
A 1 248 MET 248 276 276 MET MET A . n 
A 1 249 VAL 249 277 277 VAL VAL A . n 
A 1 250 LEU 250 278 278 LEU LEU A . n 
A 1 251 LEU 251 279 279 LEU LEU A . n 
A 1 252 PRO 252 280 280 PRO PRO A . n 
A 1 253 ILE 253 281 281 ILE ILE A . n 
A 1 254 ASN 254 282 282 ASN ASN A . n 
A 1 255 GLU 255 283 283 GLU GLU A . n 
A 1 256 PRO 256 284 284 PRO PRO A . n 
A 1 257 VAL 257 285 285 VAL VAL A . n 
A 1 258 HIS 258 286 286 HIS HIS A . n 
A 1 259 GLY 259 287 287 GLY GLY A . n 
A 1 260 THR 260 288 288 THR THR A . n 
A 1 261 LYS 261 289 289 LYS LYS A . n 
A 1 262 ARG 262 290 290 ARG ARG A . n 
A 1 263 LYS 263 291 291 LYS LYS A . n 
A 1 264 SER 264 292 292 SER SER A . n 
A 1 265 GLN 265 293 293 GLN GLN A . n 
A 1 266 ILE 266 294 294 ILE ILE A . n 
A 1 267 GLN 267 295 295 GLN GLN A . n 
A 1 268 THR 268 296 296 THR THR A . n 
A 1 269 TYR 269 297 297 TYR TYR A . n 
A 1 270 LEU 270 298 298 LEU LEU A . n 
A 1 271 GLU 271 299 299 GLU GLU A . n 
A 1 272 HIS 272 300 300 HIS HIS A . n 
A 1 273 ASN 273 301 301 ASN ASN A . n 
A 1 274 GLU 274 302 302 GLU GLU A . n 
A 1 275 GLY 275 303 303 GLY GLY A . n 
A 1 276 ALA 276 304 304 ALA ALA A . n 
A 1 277 GLY 277 305 305 GLY GLY A . n 
A 1 278 LEU 278 306 306 LEU LEU A . n 
A 1 279 GLN 279 307 307 GLN GLN A . n 
A 1 280 HIS 280 308 308 HIS HIS A . n 
A 1 281 LEU 281 309 309 LEU LEU A . n 
A 1 282 ALA 282 310 310 ALA ALA A . n 
A 1 283 LEU 283 311 311 LEU LEU A . n 
A 1 284 MET 284 312 312 MET MET A . n 
A 1 285 SER 285 313 313 SER SER A . n 
A 1 286 GLU 286 314 314 GLU GLU A . n 
A 1 287 ASP 287 315 315 ASP ASP A . n 
A 1 288 ILE 288 316 316 ILE ILE A . n 
A 1 289 PHE 289 317 317 PHE PHE A . n 
A 1 290 ARG 290 318 318 ARG ARG A . n 
A 1 291 THR 291 319 319 THR THR A . n 
A 1 292 LEU 292 320 320 LEU LEU A . n 
A 1 293 ARG 293 321 321 ARG ARG A . n 
A 1 294 GLU 294 322 322 GLU GLU A . n 
A 1 295 MET 295 323 323 MET MET A . n 
A 1 296 ARG 296 324 324 ARG ARG A . n 
A 1 297 LYS 297 325 325 LYS LYS A . n 
A 1 298 ARG 298 326 326 ARG ARG A . n 
A 1 299 SER 299 327 327 SER SER A . n 
A 1 300 SER 300 328 328 SER SER A . n 
A 1 301 ILE 301 329 329 ILE ILE A . n 
A 1 302 GLY 302 330 330 GLY GLY A . n 
A 1 303 GLY 303 331 331 GLY GLY A . n 
A 1 304 PHE 304 332 332 PHE PHE A . n 
A 1 305 ASP 305 333 333 ASP ASP A . n 
A 1 306 PHE 306 334 334 PHE PHE A . n 
A 1 307 MET 307 335 335 MET MET A . n 
A 1 308 PRO 308 336 336 PRO PRO A . n 
A 1 309 SER 309 337 337 SER SER A . n 
A 1 310 PRO 310 338 338 PRO PRO A . n 
A 1 311 PRO 311 339 339 PRO PRO A . n 
A 1 312 PRO 312 340 340 PRO PRO A . n 
A 1 313 THR 313 341 341 THR THR A . n 
A 1 314 TYR 314 342 342 TYR TYR A . n 
A 1 315 TYR 315 343 343 TYR TYR A . n 
A 1 316 GLN 316 344 344 GLN GLN A . n 
A 1 317 ASN 317 345 345 ASN ASN A . n 
A 1 318 LEU 318 346 346 LEU LEU A . n 
A 1 319 LYS 319 347 347 LYS LYS A . n 
A 1 320 LYS 320 348 348 LYS LYS A . n 
A 1 321 ARG 321 349 349 ARG ARG A . n 
A 1 322 VAL 322 350 350 VAL VAL A . n 
A 1 323 GLY 323 351 351 GLY GLY A . n 
A 1 324 ASP 324 352 352 ASP ASP A . n 
A 1 325 VAL 325 353 353 VAL VAL A . n 
A 1 326 LEU 326 354 354 LEU LEU A . n 
A 1 327 SER 327 355 355 SER SER A . n 
A 1 328 ASP 328 356 356 ASP ASP A . n 
A 1 329 ASP 329 357 357 ASP ASP A . n 
A 1 330 GLN 330 358 358 GLN GLN A . n 
A 1 331 ILE 331 359 359 ILE ILE A . n 
A 1 332 LYS 332 360 360 LYS LYS A . n 
A 1 333 GLU 333 361 361 GLU GLU A . n 
A 1 334 CYS 334 362 362 CYS CYS A . n 
A 1 335 GLU 335 363 363 GLU GLU A . n 
A 1 336 GLU 336 364 364 GLU GLU A . n 
A 1 337 LEU 337 365 365 LEU LEU A . n 
A 1 338 GLY 338 366 366 GLY GLY A . n 
A 1 339 ILE 339 367 367 ILE ILE A . n 
A 1 340 LEU 340 368 368 LEU LEU A . n 
A 1 341 VAL 341 369 369 VAL VAL A . n 
A 1 342 ASP 342 370 370 ASP ASP A . n 
A 1 343 ARG 343 371 371 ARG ARG A . n 
A 1 344 ASP 344 372 372 ASP ASP A . n 
A 1 345 ASP 345 373 373 ASP ASP A . n 
A 1 346 GLN 346 374 374 GLN GLN A . n 
A 1 347 GLY 347 375 375 GLY GLY A . n 
A 1 348 THR 348 376 376 THR THR A . n 
A 1 349 LEU 349 377 377 LEU LEU A . n 
A 1 350 LEU 350 378 378 LEU LEU A . n 
A 1 351 GLN 351 379 379 GLN GLN A . n 
A 1 352 ILE 352 380 380 ILE ILE A . n 
A 1 353 PHE 353 381 381 PHE PHE A . n 
A 1 354 THR 354 382 382 THR THR A . n 
A 1 355 LYS 355 383 383 LYS LYS A . n 
A 1 356 PRO 356 384 384 PRO PRO A . n 
A 1 357 LEU 357 385 385 LEU LEU A . n 
A 1 358 GLY 358 386 386 GLY GLY A . n 
A 1 359 ASP 359 387 387 ASP ASP A . n 
A 1 360 ARG 360 388 388 ARG ARG A . n 
A 1 361 PRO 361 389 389 PRO PRO A . n 
A 1 362 THR 362 390 390 THR THR A . n 
A 1 363 ILE 363 391 391 ILE ILE A . n 
A 1 364 PHE 364 392 392 PHE PHE A . n 
A 1 365 ILE 365 393 393 ILE ILE A . n 
A 1 366 GLU 366 394 394 GLU GLU A . n 
A 1 367 ILE 367 395 395 ILE ILE A . n 
A 1 368 ILE 368 396 396 ILE ILE A . n 
A 1 369 GLN 369 397 397 GLN GLN A . n 
A 1 370 ARG 370 398 398 ARG ARG A . n 
A 1 371 VAL 371 399 399 VAL VAL A . n 
A 1 372 GLY 372 400 400 GLY GLY A . n 
A 1 373 CYS 373 401 401 CYS CYS A . n 
A 1 374 MET 374 402 402 MET MET A . n 
A 1 375 MET 375 403 403 MET MET A . n 
A 1 376 LYS 376 404 ?   ?   ?   A . n 
A 1 377 ASP 377 405 ?   ?   ?   A . n 
A 1 378 GLU 378 406 ?   ?   ?   A . n 
A 1 379 GLU 379 407 ?   ?   ?   A . n 
A 1 380 GLY 380 408 ?   ?   ?   A . n 
A 1 381 LYS 381 409 ?   ?   ?   A . n 
A 1 382 ALA 382 410 ?   ?   ?   A . n 
A 1 383 TYR 383 411 411 TYR TYR A . n 
A 1 384 GLN 384 412 412 GLN GLN A . n 
A 1 385 SER 385 413 413 SER SER A . n 
A 1 386 GLY 386 414 414 GLY GLY A . n 
A 1 387 GLY 387 415 415 GLY GLY A . n 
A 1 388 CYS 388 416 416 CYS CYS A . n 
A 1 389 GLY 389 417 417 GLY GLY A . n 
A 1 390 GLY 390 418 418 GLY GLY A . n 
A 1 391 PHE 391 419 419 PHE PHE A . n 
A 1 392 GLY 392 420 420 GLY GLY A . n 
A 1 393 LYS 393 421 421 LYS LYS A . n 
A 1 394 GLY 394 422 422 GLY GLY A . n 
A 1 395 ASN 395 423 423 ASN ASN A . n 
A 1 396 PHE 396 424 424 PHE PHE A . n 
A 1 397 SER 397 425 425 SER SER A . n 
A 1 398 GLU 398 426 426 GLU GLU A . n 
A 1 399 LEU 399 427 427 LEU LEU A . n 
A 1 400 PHE 400 428 428 PHE PHE A . n 
A 1 401 LYS 401 429 429 LYS LYS A . n 
A 1 402 SER 402 430 430 SER SER A . n 
A 1 403 ILE 403 431 431 ILE ILE A . n 
A 1 404 GLU 404 432 432 GLU GLU A . n 
A 1 405 GLU 405 433 433 GLU GLU A . n 
A 1 406 TYR 406 434 434 TYR TYR A . n 
A 1 407 GLU 407 435 435 GLU GLU A . n 
A 1 408 LYS 408 436 436 LYS LYS A . n 
A 1 409 THR 409 437 ?   ?   ?   A . n 
A 1 410 LEU 410 438 ?   ?   ?   A . n 
A 1 411 GLU 411 439 ?   ?   ?   A . n 
A 1 412 ALA 412 440 ?   ?   ?   A . n 
A 1 413 LYS 413 441 ?   ?   ?   A . n 
A 1 414 GLN 414 442 ?   ?   ?   A . n 
A 1 415 LEU 415 443 ?   ?   ?   A . n 
A 1 416 VAL 416 444 ?   ?   ?   A . n 
A 1 417 GLY 417 445 ?   ?   ?   A . n 
# 
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 A1LWP 1   501 501 A1LWP LIG A . 
C 3 CO    1   502 601 CO    CO  A . 
D 4 HOH   1   601 185 HOH   HOH A . 
D 4 HOH   2   602 182 HOH   HOH A . 
D 4 HOH   3   603 203 HOH   HOH A . 
D 4 HOH   4   604 198 HOH   HOH A . 
D 4 HOH   5   605 149 HOH   HOH A . 
D 4 HOH   6   606 79  HOH   HOH A . 
D 4 HOH   7   607 51  HOH   HOH A . 
D 4 HOH   8   608 111 HOH   HOH A . 
D 4 HOH   9   609 74  HOH   HOH A . 
D 4 HOH   10  610 102 HOH   HOH A . 
D 4 HOH   11  611 178 HOH   HOH A . 
D 4 HOH   12  612 199 HOH   HOH A . 
D 4 HOH   13  613 57  HOH   HOH A . 
D 4 HOH   14  614 150 HOH   HOH A . 
D 4 HOH   15  615 20  HOH   HOH A . 
D 4 HOH   16  616 3   HOH   HOH A . 
D 4 HOH   17  617 121 HOH   HOH A . 
D 4 HOH   18  618 81  HOH   HOH A . 
D 4 HOH   19  619 136 HOH   HOH A . 
D 4 HOH   20  620 103 HOH   HOH A . 
D 4 HOH   21  621 133 HOH   HOH A . 
D 4 HOH   22  622 6   HOH   HOH A . 
D 4 HOH   23  623 181 HOH   HOH A . 
D 4 HOH   24  624 104 HOH   HOH A . 
D 4 HOH   25  625 76  HOH   HOH A . 
D 4 HOH   26  626 72  HOH   HOH A . 
D 4 HOH   27  627 59  HOH   HOH A . 
D 4 HOH   28  628 168 HOH   HOH A . 
D 4 HOH   29  629 44  HOH   HOH A . 
D 4 HOH   30  630 49  HOH   HOH A . 
D 4 HOH   31  631 84  HOH   HOH A . 
D 4 HOH   32  632 147 HOH   HOH A . 
D 4 HOH   33  633 29  HOH   HOH A . 
D 4 HOH   34  634 80  HOH   HOH A . 
D 4 HOH   35  635 7   HOH   HOH A . 
D 4 HOH   36  636 22  HOH   HOH A . 
D 4 HOH   37  637 85  HOH   HOH A . 
D 4 HOH   38  638 58  HOH   HOH A . 
D 4 HOH   39  639 146 HOH   HOH A . 
D 4 HOH   40  640 2   HOH   HOH A . 
D 4 HOH   41  641 124 HOH   HOH A . 
D 4 HOH   42  642 54  HOH   HOH A . 
D 4 HOH   43  643 70  HOH   HOH A . 
D 4 HOH   44  644 60  HOH   HOH A . 
D 4 HOH   45  645 87  HOH   HOH A . 
D 4 HOH   46  646 27  HOH   HOH A . 
D 4 HOH   47  647 21  HOH   HOH A . 
D 4 HOH   48  648 30  HOH   HOH A . 
D 4 HOH   49  649 40  HOH   HOH A . 
D 4 HOH   50  650 25  HOH   HOH A . 
D 4 HOH   51  651 12  HOH   HOH A . 
D 4 HOH   52  652 35  HOH   HOH A . 
D 4 HOH   53  653 4   HOH   HOH A . 
D 4 HOH   54  654 26  HOH   HOH A . 
D 4 HOH   55  655 141 HOH   HOH A . 
D 4 HOH   56  656 193 HOH   HOH A . 
D 4 HOH   57  657 28  HOH   HOH A . 
D 4 HOH   58  658 105 HOH   HOH A . 
D 4 HOH   59  659 65  HOH   HOH A . 
D 4 HOH   60  660 175 HOH   HOH A . 
D 4 HOH   61  661 67  HOH   HOH A . 
D 4 HOH   62  662 167 HOH   HOH A . 
D 4 HOH   63  663 117 HOH   HOH A . 
D 4 HOH   64  664 173 HOH   HOH A . 
D 4 HOH   65  665 15  HOH   HOH A . 
D 4 HOH   66  666 52  HOH   HOH A . 
D 4 HOH   67  667 17  HOH   HOH A . 
D 4 HOH   68  668 119 HOH   HOH A . 
D 4 HOH   69  669 122 HOH   HOH A . 
D 4 HOH   70  670 179 HOH   HOH A . 
D 4 HOH   71  671 161 HOH   HOH A . 
D 4 HOH   72  672 69  HOH   HOH A . 
D 4 HOH   73  673 10  HOH   HOH A . 
D 4 HOH   74  674 204 HOH   HOH A . 
D 4 HOH   75  675 142 HOH   HOH A . 
D 4 HOH   76  676 56  HOH   HOH A . 
D 4 HOH   77  677 50  HOH   HOH A . 
D 4 HOH   78  678 9   HOH   HOH A . 
D 4 HOH   79  679 19  HOH   HOH A . 
D 4 HOH   80  680 5   HOH   HOH A . 
D 4 HOH   81  681 123 HOH   HOH A . 
D 4 HOH   82  682 166 HOH   HOH A . 
D 4 HOH   83  683 159 HOH   HOH A . 
D 4 HOH   84  684 118 HOH   HOH A . 
D 4 HOH   85  685 106 HOH   HOH A . 
D 4 HOH   86  686 151 HOH   HOH A . 
D 4 HOH   87  687 36  HOH   HOH A . 
D 4 HOH   88  688 38  HOH   HOH A . 
D 4 HOH   89  689 16  HOH   HOH A . 
D 4 HOH   90  690 95  HOH   HOH A . 
D 4 HOH   91  691 8   HOH   HOH A . 
D 4 HOH   92  692 47  HOH   HOH A . 
D 4 HOH   93  693 73  HOH   HOH A . 
D 4 HOH   94  694 11  HOH   HOH A . 
D 4 HOH   95  695 32  HOH   HOH A . 
D 4 HOH   96  696 196 HOH   HOH A . 
D 4 HOH   97  697 125 HOH   HOH A . 
D 4 HOH   98  698 37  HOH   HOH A . 
D 4 HOH   99  699 171 HOH   HOH A . 
D 4 HOH   100 700 23  HOH   HOH A . 
D 4 HOH   101 701 172 HOH   HOH A . 
D 4 HOH   102 702 77  HOH   HOH A . 
D 4 HOH   103 703 55  HOH   HOH A . 
D 4 HOH   104 704 63  HOH   HOH A . 
D 4 HOH   105 705 143 HOH   HOH A . 
D 4 HOH   106 706 91  HOH   HOH A . 
D 4 HOH   107 707 34  HOH   HOH A . 
D 4 HOH   108 708 46  HOH   HOH A . 
D 4 HOH   109 709 24  HOH   HOH A . 
D 4 HOH   110 710 163 HOH   HOH A . 
D 4 HOH   111 711 42  HOH   HOH A . 
D 4 HOH   112 712 68  HOH   HOH A . 
D 4 HOH   113 713 120 HOH   HOH A . 
D 4 HOH   114 714 94  HOH   HOH A . 
D 4 HOH   115 715 130 HOH   HOH A . 
D 4 HOH   116 716 127 HOH   HOH A . 
D 4 HOH   117 717 169 HOH   HOH A . 
D 4 HOH   118 718 109 HOH   HOH A . 
D 4 HOH   119 719 176 HOH   HOH A . 
D 4 HOH   120 720 14  HOH   HOH A . 
D 4 HOH   121 721 188 HOH   HOH A . 
D 4 HOH   122 722 139 HOH   HOH A . 
D 4 HOH   123 723 62  HOH   HOH A . 
D 4 HOH   124 724 33  HOH   HOH A . 
D 4 HOH   125 725 45  HOH   HOH A . 
D 4 HOH   126 726 180 HOH   HOH A . 
D 4 HOH   127 727 1   HOH   HOH A . 
D 4 HOH   128 728 18  HOH   HOH A . 
D 4 HOH   129 729 108 HOH   HOH A . 
D 4 HOH   130 730 174 HOH   HOH A . 
D 4 HOH   131 731 13  HOH   HOH A . 
D 4 HOH   132 732 131 HOH   HOH A . 
D 4 HOH   133 733 112 HOH   HOH A . 
D 4 HOH   134 734 88  HOH   HOH A . 
D 4 HOH   135 735 98  HOH   HOH A . 
D 4 HOH   136 736 115 HOH   HOH A . 
D 4 HOH   137 737 64  HOH   HOH A . 
D 4 HOH   138 738 201 HOH   HOH A . 
D 4 HOH   139 739 137 HOH   HOH A . 
D 4 HOH   140 740 190 HOH   HOH A . 
D 4 HOH   141 741 164 HOH   HOH A . 
D 4 HOH   142 742 194 HOH   HOH A . 
D 4 HOH   143 743 184 HOH   HOH A . 
D 4 HOH   144 744 83  HOH   HOH A . 
D 4 HOH   145 745 89  HOH   HOH A . 
D 4 HOH   146 746 129 HOH   HOH A . 
D 4 HOH   147 747 177 HOH   HOH A . 
D 4 HOH   148 748 200 HOH   HOH A . 
D 4 HOH   149 749 90  HOH   HOH A . 
D 4 HOH   150 750 53  HOH   HOH A . 
D 4 HOH   151 751 39  HOH   HOH A . 
D 4 HOH   152 752 93  HOH   HOH A . 
D 4 HOH   153 753 156 HOH   HOH A . 
D 4 HOH   154 754 113 HOH   HOH A . 
D 4 HOH   155 755 153 HOH   HOH A . 
D 4 HOH   156 756 192 HOH   HOH A . 
D 4 HOH   157 757 170 HOH   HOH A . 
D 4 HOH   158 758 134 HOH   HOH A . 
D 4 HOH   159 759 116 HOH   HOH A . 
D 4 HOH   160 760 100 HOH   HOH A . 
D 4 HOH   161 761 183 HOH   HOH A . 
D 4 HOH   162 762 99  HOH   HOH A . 
D 4 HOH   163 763 61  HOH   HOH A . 
D 4 HOH   164 764 144 HOH   HOH A . 
D 4 HOH   165 765 78  HOH   HOH A . 
D 4 HOH   166 766 41  HOH   HOH A . 
D 4 HOH   167 767 96  HOH   HOH A . 
D 4 HOH   168 768 152 HOH   HOH A . 
D 4 HOH   169 769 158 HOH   HOH A . 
D 4 HOH   170 770 162 HOH   HOH A . 
D 4 HOH   171 771 110 HOH   HOH A . 
D 4 HOH   172 772 86  HOH   HOH A . 
D 4 HOH   173 773 43  HOH   HOH A . 
D 4 HOH   174 774 157 HOH   HOH A . 
D 4 HOH   175 775 145 HOH   HOH A . 
D 4 HOH   176 776 154 HOH   HOH A . 
D 4 HOH   177 777 66  HOH   HOH A . 
D 4 HOH   178 778 191 HOH   HOH A . 
D 4 HOH   179 779 48  HOH   HOH A . 
D 4 HOH   180 780 82  HOH   HOH A . 
D 4 HOH   181 781 71  HOH   HOH A . 
D 4 HOH   182 782 138 HOH   HOH A . 
D 4 HOH   183 783 195 HOH   HOH A . 
D 4 HOH   184 784 165 HOH   HOH A . 
D 4 HOH   185 785 160 HOH   HOH A . 
D 4 HOH   186 786 140 HOH   HOH A . 
D 4 HOH   187 787 186 HOH   HOH A . 
D 4 HOH   188 788 126 HOH   HOH A . 
D 4 HOH   189 789 202 HOH   HOH A . 
D 4 HOH   190 790 75  HOH   HOH A . 
D 4 HOH   191 791 97  HOH   HOH A . 
D 4 HOH   192 792 155 HOH   HOH A . 
D 4 HOH   193 793 114 HOH   HOH A . 
D 4 HOH   194 794 128 HOH   HOH A . 
D 4 HOH   195 795 31  HOH   HOH A . 
D 4 HOH   196 796 187 HOH   HOH A . 
D 4 HOH   197 797 92  HOH   HOH A . 
D 4 HOH   198 798 135 HOH   HOH A . 
D 4 HOH   199 799 189 HOH   HOH A . 
D 4 HOH   200 800 197 HOH   HOH A . 
D 4 HOH   201 801 148 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 35  ? CG  ? A LYS 7   CG  
2  1 Y 1 A LYS 35  ? CD  ? A LYS 7   CD  
3  1 Y 1 A LYS 35  ? CE  ? A LYS 7   CE  
4  1 Y 1 A LYS 35  ? NZ  ? A LYS 7   NZ  
5  1 Y 1 A LYS 193 ? CG  ? A LYS 165 CG  
6  1 Y 1 A LYS 193 ? CD  ? A LYS 165 CD  
7  1 Y 1 A LYS 193 ? CE  ? A LYS 165 CE  
8  1 Y 1 A LYS 193 ? NZ  ? A LYS 165 NZ  
9  1 Y 1 A GLU 201 ? CG  ? A GLU 173 CG  
10 1 Y 1 A GLU 201 ? CD  ? A GLU 173 CD  
11 1 Y 1 A GLU 201 ? OE1 ? A GLU 173 OE1 
12 1 Y 1 A GLU 201 ? OE2 ? A GLU 173 OE2 
13 1 Y 1 A GLU 210 ? CG  ? A GLU 182 CG  
14 1 Y 1 A GLU 210 ? CD  ? A GLU 182 CD  
15 1 Y 1 A GLU 210 ? OE1 ? A GLU 182 OE1 
16 1 Y 1 A GLU 210 ? OE2 ? A GLU 182 OE2 
17 1 Y 1 A ASP 211 ? CG  ? A ASP 183 CG  
18 1 Y 1 A ASP 211 ? OD1 ? A ASP 183 OD1 
19 1 Y 1 A ASP 211 ? OD2 ? A ASP 183 OD2 
20 1 Y 1 A LYS 289 ? CG  ? A LYS 261 CG  
21 1 Y 1 A LYS 289 ? CD  ? A LYS 261 CD  
22 1 Y 1 A LYS 289 ? CE  ? A LYS 261 CE  
23 1 Y 1 A LYS 289 ? NZ  ? A LYS 261 NZ  
24 1 Y 1 A ARG 290 ? CG  ? A ARG 262 CG  
25 1 Y 1 A ARG 290 ? CD  ? A ARG 262 CD  
26 1 Y 1 A ARG 290 ? NE  ? A ARG 262 NE  
27 1 Y 1 A ARG 290 ? CZ  ? A ARG 262 CZ  
28 1 Y 1 A ARG 290 ? NH1 ? A ARG 262 NH1 
29 1 Y 1 A ARG 290 ? NH2 ? A ARG 262 NH2 
30 1 Y 1 A GLN 344 ? CG  ? A GLN 316 CG  
31 1 Y 1 A GLN 344 ? CD  ? A GLN 316 CD  
32 1 Y 1 A GLN 344 ? OE1 ? A GLN 316 OE1 
33 1 Y 1 A GLN 344 ? NE2 ? A GLN 316 NE2 
34 1 Y 1 A LYS 347 ? CG  ? A LYS 319 CG  
35 1 Y 1 A LYS 347 ? CD  ? A LYS 319 CD  
36 1 Y 1 A LYS 347 ? CE  ? A LYS 319 CE  
37 1 Y 1 A LYS 347 ? NZ  ? A LYS 319 NZ  
38 1 Y 1 A LYS 348 ? CG  ? A LYS 320 CG  
39 1 Y 1 A LYS 348 ? CD  ? A LYS 320 CD  
40 1 Y 1 A LYS 348 ? CE  ? A LYS 320 CE  
41 1 Y 1 A LYS 348 ? NZ  ? A LYS 320 NZ  
42 1 Y 1 A ASP 357 ? CG  ? A ASP 329 CG  
43 1 Y 1 A ASP 357 ? OD1 ? A ASP 329 OD1 
44 1 Y 1 A ASP 357 ? OD2 ? A ASP 329 OD2 
45 1 Y 1 A LYS 360 ? CG  ? A LYS 332 CG  
46 1 Y 1 A LYS 360 ? CD  ? A LYS 332 CD  
47 1 Y 1 A LYS 360 ? CE  ? A LYS 332 CE  
48 1 Y 1 A LYS 360 ? NZ  ? A LYS 332 NZ  
49 1 Y 1 A GLN 374 ? CG  ? A GLN 346 CG  
50 1 Y 1 A GLN 374 ? CD  ? A GLN 346 CD  
51 1 Y 1 A GLN 374 ? OE1 ? A GLN 346 OE1 
52 1 Y 1 A GLN 374 ? NE2 ? A GLN 346 NE2 
53 1 Y 1 A TYR 411 ? CG  ? A TYR 383 CG  
54 1 Y 1 A TYR 411 ? CD1 ? A TYR 383 CD1 
55 1 Y 1 A TYR 411 ? CD2 ? A TYR 383 CD2 
56 1 Y 1 A TYR 411 ? CE1 ? A TYR 383 CE1 
57 1 Y 1 A TYR 411 ? CE2 ? A TYR 383 CE2 
58 1 Y 1 A TYR 411 ? CZ  ? A TYR 383 CZ  
59 1 Y 1 A TYR 411 ? OH  ? A TYR 383 OH  
60 1 Y 1 A PHE 428 ? CG  ? A PHE 400 CG  
61 1 Y 1 A PHE 428 ? CD1 ? A PHE 400 CD1 
62 1 Y 1 A PHE 428 ? CD2 ? A PHE 400 CD2 
63 1 Y 1 A PHE 428 ? CE1 ? A PHE 400 CE1 
64 1 Y 1 A PHE 428 ? CE2 ? A PHE 400 CE2 
65 1 Y 1 A PHE 428 ? CZ  ? A PHE 400 CZ  
66 1 Y 1 A LYS 429 ? CG  ? A LYS 401 CG  
67 1 Y 1 A LYS 429 ? CD  ? A LYS 401 CD  
68 1 Y 1 A LYS 429 ? CE  ? A LYS 401 CE  
69 1 Y 1 A LYS 429 ? NZ  ? A LYS 401 NZ  
70 1 Y 1 A GLU 432 ? CG  ? A GLU 404 CG  
71 1 Y 1 A GLU 432 ? CD  ? A GLU 404 CD  
72 1 Y 1 A GLU 432 ? OE1 ? A GLU 404 OE1 
73 1 Y 1 A GLU 432 ? OE2 ? A GLU 404 OE2 
74 1 Y 1 A GLU 433 ? CG  ? A GLU 405 CG  
75 1 Y 1 A GLU 433 ? CD  ? A GLU 405 CD  
76 1 Y 1 A GLU 433 ? OE1 ? A GLU 405 OE1 
77 1 Y 1 A GLU 433 ? OE2 ? A GLU 405 OE2 
78 1 Y 1 A GLU 435 ? CG  ? A GLU 407 CG  
79 1 Y 1 A GLU 435 ? CD  ? A GLU 407 CD  
80 1 Y 1 A GLU 435 ? OE1 ? A GLU 407 OE1 
81 1 Y 1 A GLU 435 ? OE2 ? A GLU 407 OE2 
82 1 Y 1 A LYS 436 ? CG  ? A LYS 408 CG  
83 1 Y 1 A LYS 436 ? CD  ? A LYS 408 CD  
84 1 Y 1 A LYS 436 ? CE  ? A LYS 408 CE  
85 1 Y 1 A LYS 436 ? NZ  ? A LYS 408 NZ  
# 
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 ? ? ? '(1.10.1_2155: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.20 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XQY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.911 
_cell.length_a_esd                 ? 
_cell.length_b                     83.713 
_cell.length_b_esd                 ? 
_cell.length_c                     65.450 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8XQY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8XQY 
_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             2.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.49 
_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' 
_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    
'0.1M Tris/Bicine pH 8.5, 15% (v/v) MPD, 15% (w/v) PEG 1000, 15% (w/v) PEG 3350, 0.03M NaBr, 0.03M NaF, 0.03M NaI' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-25 
_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   0.98 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XQY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.003 
_reflns.d_resolution_low                               45.381 
_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                                     26401 
_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                           98.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.66 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          0.996 
_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                                   0.979 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.003 
_reflns_shell.d_res_low                                     2.12 
_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                             8286 
_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                                  0.856 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8XQY 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.003 
_refine.ls_d_res_low                             45.381 
_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                     26401 
_refine.ls_number_reflns_R_free                  1322 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.98 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2577 
_refine.ls_R_factor_R_free                       0.3087 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2550 
_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                          1.33 
_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       ML 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 37.91 
_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                            0.41 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.003 
_refine_hist.d_res_low                        45.381 
_refine_hist.number_atoms_solvent             201 
_refine_hist.number_atoms_total               3077 
_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        2849 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_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' ? 0.008  ? 2959 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.941  ? 4012 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.348 ? 1748 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.056  ? 439  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 524  ? f_plane_restr      ? ? 
# 
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' 2.0033 2.0835 . . 138 2612 90.00  . . . . 0.5421 . . . . . . . . . . . 0.6023 
'X-RAY DIFFRACTION' 2.0835 2.1783 . . 147 2777 97.00  . . . . 0.3334 . . . . . . . . . . . 0.3503 
'X-RAY DIFFRACTION' 2.1783 2.2932 . . 132 2501 87.00  . . . . 0.4243 . . . . . . . . . . . 0.4873 
'X-RAY DIFFRACTION' 2.2932 2.4368 . . 149 2836 98.00  . . . . 0.2928 . . . . . . . . . . . 0.3546 
'X-RAY DIFFRACTION' 2.4368 2.6250 . . 148 2809 97.00  . . . . 0.3123 . . . . . . . . . . . 0.3997 
'X-RAY DIFFRACTION' 2.6250 2.8891 . . 148 2821 98.00  . . . . 0.2646 . . . . . . . . . . . 0.3140 
'X-RAY DIFFRACTION' 2.8891 3.3071 . . 152 2884 99.00  . . . . 0.2263 . . . . . . . . . . . 0.2455 
'X-RAY DIFFRACTION' 3.3071 4.1661 . . 152 2883 99.00  . . . . 0.1817 . . . . . . . . . . . 0.2673 
'X-RAY DIFFRACTION' 4.1661 8      . . 156 2956 100.00 . . . . 0.1677 . . . . . . . . . . . 0.2020 
# 
_struct.entry_id                     8XQY 
_struct.title                        'Crystal structure of AtHPPD-Y181183 complex' 
_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        8XQY 
_struct_keywords.text            'Complex, Inhibitor, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HPPD_ARATH 
_struct_ref.pdbx_db_accession          P93836 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VRKNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEI
KPTTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSY
KAEDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLAS
NDEMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGD
VLSDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELFKSIE
EYEKTLEAKQLVG
;
_struct_ref.pdbx_align_begin           33 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8XQY 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 5 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 417 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P93836 
_struct_ref_seq.db_align_beg                  33 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  445 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       33 
_struct_ref_seq.pdbx_auth_seq_align_end       445 
# 
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 8XQY GLY A 1 ? UNP P93836 ? ? 'expression tag' 29 1 
1 8XQY SER A 2 ? UNP P93836 ? ? 'expression tag' 30 2 
1 8XQY HIS A 3 ? UNP P93836 ? ? 'expression tag' 31 3 
1 8XQY MET A 4 ? UNP P93836 ? ? 'expression tag' 32 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   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)' 3180  ? 
1 MORE         -14   ? 
1 'SSA (A^2)'  28130 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 2_557 -x,y,-z+2 -1.0000000000 0.0000000000 0.0000000000 -23.1803925078 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 128.8312050832 
# 
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 ASP A 28  ? GLY A 41  ? ASP A 56  GLY A 69  1 ? 14 
HELX_P HELX_P2  AA2 ASP A 49  ? GLY A 53  ? ASP A 77  GLY A 81  5 ? 5  
HELX_P HELX_P3  AA3 SER A 76  ? SER A 80  ? SER A 104 SER A 108 5 ? 5  
HELX_P HELX_P4  AA4 ILE A 84  ? THR A 88  ? ILE A 112 THR A 116 5 ? 5  
HELX_P HELX_P5  AA5 ASP A 96  ? GLY A 108 ? ASP A 124 GLY A 136 1 ? 13 
HELX_P HELX_P6  AA6 ASP A 120 ? ASN A 131 ? ASP A 148 ASN A 159 1 ? 12 
HELX_P HELX_P7  AA7 GLU A 205 ? GLY A 218 ? GLU A 233 GLY A 246 1 ? 14 
HELX_P HELX_P8  AA8 SER A 264 ? GLU A 274 ? SER A 292 GLU A 302 1 ? 11 
HELX_P HELX_P9  AA9 ASP A 287 ? SER A 299 ? ASP A 315 SER A 327 1 ? 13 
HELX_P HELX_P10 AB1 SER A 300 ? GLY A 302 ? SER A 328 GLY A 330 5 ? 3  
HELX_P HELX_P11 AB2 PRO A 311 ? ASN A 317 ? PRO A 339 ASN A 345 1 ? 7  
HELX_P HELX_P12 AB3 ASN A 317 ? GLY A 323 ? ASN A 345 GLY A 351 1 ? 7  
HELX_P HELX_P13 AB4 SER A 327 ? GLY A 338 ? SER A 355 GLY A 366 1 ? 12 
HELX_P HELX_P14 AB5 GLY A 392 ? LYS A 408 ? GLY A 420 LYS A 436 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS   373 SG  ? ? ? 1_555 A CYS 388 SG ? ? A CYS   401 A CYS 416 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc1 metalc ? ? A HIS   198 NE2 ? ? ? 1_555 C CO  .   CO ? ? A HIS   226 A CO  502 1_555 ? ? ? ? ? ? ? 2.558 ? ? 
metalc2 metalc ? ? A HIS   280 NE2 ? ? ? 1_555 C CO  .   CO ? ? A HIS   308 A CO  502 1_555 ? ? ? ? ? ? ? 2.505 ? ? 
metalc3 metalc ? ? A GLU   366 OE1 ? ? ? 1_555 C CO  .   CO ? ? A GLU   394 A CO  502 1_555 ? ? ? ? ? ? ? 2.158 ? ? 
metalc4 metalc ? ? B A1LWP .   O09 ? ? ? 1_555 C CO  .   CO ? ? A A1LWP 501 A CO  502 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc5 metalc ? ? B A1LWP .   O16 ? ? ? 1_555 C CO  .   CO ? ? A A1LWP 501 A CO  502 1_555 ? ? ? ? ? ? ? 2.209 ? ? 
metalc6 metalc ? ? C CO    .   CO  ? ? ? 1_555 D HOH .   O  ? ? A CO    502 A HOH 645 1_555 ? ? ? ? ? ? ? 2.718 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 NE2 ? A HIS   280 ? A HIS   308 ? 1_555 102.1 ? 
2  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 OE1 ? A GLU   366 ? A GLU   394 ? 1_555 89.6  ? 
3  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 OE1 ? A GLU   366 ? A GLU   394 ? 1_555 90.2  ? 
4  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O09 ? B A1LWP .   ? A A1LWP 501 ? 1_555 162.1 ? 
5  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O09 ? B A1LWP .   ? A A1LWP 501 ? 1_555 92.0  ? 
6  OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O09 ? B A1LWP .   ? A A1LWP 501 ? 1_555 101.5 ? 
7  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O16 ? B A1LWP .   ? A A1LWP 501 ? 1_555 90.4  ? 
8  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O16 ? B A1LWP .   ? A A1LWP 501 ? 1_555 94.1  ? 
9  OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O16 ? B A1LWP .   ? A A1LWP 501 ? 1_555 175.6 ? 
10 O09 ? B A1LWP .   ? A A1LWP 501 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O16 ? B A1LWP .   ? A A1LWP 501 ? 1_555 77.4  ? 
11 NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O   ? D HOH   .   ? A HOH   645 ? 1_555 74.2  ? 
12 NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O   ? D HOH   .   ? A HOH   645 ? 1_555 168.1 ? 
13 OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O   ? D HOH   .   ? A HOH   645 ? 1_555 78.5  ? 
14 O09 ? B A1LWP .   ? A A1LWP 501 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O   ? D HOH   .   ? A HOH   645 ? 1_555 94.1  ? 
15 O16 ? B A1LWP .   ? A A1LWP 501 ? 1_555 CO ? C CO . ? A CO 502 ? 1_555 O   ? D HOH   .   ? A HOH   645 ? 1_555 97.2  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       373 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      388 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       416 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PRO A 135 ? LEU A 142 ? PRO A 163 LEU A 170 
AA1 2 VAL A 146 ? TYR A 154 ? VAL A 174 TYR A 182 
AA1 3 VAL A 157 ? TYR A 164 ? VAL A 185 TYR A 192 
AA1 4 GLY A 110 ? VAL A 118 ? GLY A 138 VAL A 146 
AA1 5 VAL A 16  ? TRP A 25  ? VAL A 44  TRP A 53  
AA1 6 LEU A 67  ? PRO A 74  ? LEU A 95  PRO A 102 
AA1 7 HIS A 57  ? SER A 64  ? HIS A 85  SER A 92  
AA1 8 ARG A 43  ? SER A 48  ? ARG A 71  SER A 76  
AA1 9 GLU A 179 ? ARG A 180 ? GLU A 207 ARG A 208 
AA2 1 HIS A 220 ? GLN A 221 ? HIS A 248 GLN A 249 
AA2 2 LEU A 237 ? ALA A 243 ? LEU A 265 ALA A 271 
AA2 3 LEU A 250 ? PRO A 256 ? LEU A 278 PRO A 284 
AA2 4 ILE A 193 ? ASN A 202 ? ILE A 221 ASN A 230 
AA2 5 GLY A 277 ? SER A 285 ? GLY A 305 SER A 313 
AA2 6 PHE A 364 ? GLY A 372 ? PHE A 392 GLY A 400 
AA2 7 GLY A 347 ? PHE A 353 ? GLY A 375 PHE A 381 
AA2 8 LEU A 340 ? ARG A 343 ? LEU A 368 ARG A 371 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 142 ? N LEU A 170 O VAL A 146 ? O VAL A 174 
AA1 2 3 N ALA A 149 ? N ALA A 177 O TYR A 161 ? O TYR A 189 
AA1 3 4 O VAL A 162 ? O VAL A 190 N VAL A 118 ? N VAL A 146 
AA1 4 5 O GLU A 117 ? O GLU A 145 N ARG A 18  ? N ARG A 46  
AA1 5 6 N PHE A 24  ? N PHE A 52  O LEU A 70  ? O LEU A 98  
AA1 6 7 O ALA A 73  ? O ALA A 101 N ALA A 58  ? N ALA A 86  
AA1 7 8 O THR A 63  ? O THR A 91  N ARG A 43  ? N ARG A 71  
AA1 8 9 N LYS A 47  ? N LYS A 75  O GLU A 179 ? O GLU A 207 
AA2 1 2 N HIS A 220 ? N HIS A 248 O ALA A 243 ? O ALA A 271 
AA2 2 3 N LEU A 242 ? N LEU A 270 O LEU A 251 ? O LEU A 279 
AA2 3 4 O ASN A 254 ? O ASN A 282 N GLY A 201 ? N GLY A 229 
AA2 4 5 N ASP A 197 ? N ASP A 225 O ALA A 282 ? O ALA A 310 
AA2 5 6 N LEU A 283 ? N LEU A 311 O GLU A 366 ? O GLU A 394 
AA2 6 7 O VAL A 371 ? O VAL A 399 N THR A 348 ? N THR A 376 
AA2 7 8 O GLN A 351 ? O GLN A 379 N LEU A 340 ? N LEU A 368 
# 
_pdbx_entry_details.entry_id                   8XQY 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 LYS A 38  ? ? 39.11   61.29   
2  1 LYS A 45  ? ? -104.46 -85.16  
3  1 ASP A 77  ? ? -163.62 -159.41 
4  1 ALA A 173 ? ? -130.73 -36.38  
5  1 PHE A 202 ? ? -74.36  -73.66  
6  1 ASP A 211 ? ? -65.70  93.87   
7  1 ALA A 212 ? ? -178.67 -48.61  
8  1 ASP A 218 ? ? -171.45 109.52  
9  1 LYS A 289 ? ? -59.16  -80.65  
10 1 ASP A 315 ? ? -158.22 85.96   
11 1 VAL A 353 ? ? -123.10 -54.28  
12 1 ASP A 372 ? ? -116.93 -156.92 
13 1 THR A 390 ? ? -119.91 -84.78  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 796 ? 5.93 . 
2 1 O ? A HOH 797 ? 6.03 . 
3 1 O ? A HOH 798 ? 6.76 . 
4 1 O ? A HOH 799 ? 7.36 . 
5 1 O ? A HOH 800 ? 7.89 . 
6 1 O ? A HOH 801 ? 8.32 . 
# 
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 GLY 29  ? A GLY 1   
2  1 Y 1 A SER 30  ? A SER 2   
3  1 Y 1 A HIS 31  ? A HIS 3   
4  1 Y 1 A MET 32  ? A MET 4   
5  1 Y 1 A VAL 33  ? A VAL 5   
6  1 Y 1 A ARG 34  ? A ARG 6   
7  1 Y 1 A GLU 195 ? A GLU 167 
8  1 Y 1 A ASP 196 ? A ASP 168 
9  1 Y 1 A THR 197 ? A THR 169 
10 1 Y 1 A GLU 198 ? A GLU 170 
11 1 Y 1 A LYS 199 ? A LYS 171 
12 1 Y 1 A SER 200 ? A SER 172 
13 1 Y 1 A ALA 251 ? A ALA 223 
14 1 Y 1 A GLU 252 ? A GLU 224 
15 1 Y 1 A PHE 253 ? A PHE 225 
16 1 Y 1 A THR 254 ? A THR 226 
17 1 Y 1 A ALA 255 ? A ALA 227 
18 1 Y 1 A ASP 256 ? A ASP 228 
19 1 Y 1 A ASP 257 ? A ASP 229 
20 1 Y 1 A VAL 258 ? A VAL 230 
21 1 Y 1 A GLY 259 ? A GLY 231 
22 1 Y 1 A THR 260 ? A THR 232 
23 1 Y 1 A ALA 261 ? A ALA 233 
24 1 Y 1 A GLU 262 ? A GLU 234 
25 1 Y 1 A LYS 404 ? A LYS 376 
26 1 Y 1 A ASP 405 ? A ASP 377 
27 1 Y 1 A GLU 406 ? A GLU 378 
28 1 Y 1 A GLU 407 ? A GLU 379 
29 1 Y 1 A GLY 408 ? A GLY 380 
30 1 Y 1 A LYS 409 ? A LYS 381 
31 1 Y 1 A ALA 410 ? A ALA 382 
32 1 Y 1 A THR 437 ? A THR 409 
33 1 Y 1 A LEU 438 ? A LEU 410 
34 1 Y 1 A GLU 439 ? A GLU 411 
35 1 Y 1 A ALA 440 ? A ALA 412 
36 1 Y 1 A LYS 441 ? A LYS 413 
37 1 Y 1 A GLN 442 ? A GLN 414 
38 1 Y 1 A LEU 443 ? A LEU 415 
39 1 Y 1 A VAL 444 ? A VAL 416 
40 1 Y 1 A GLY 445 ? A GLY 417 
# 
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 
A1LWP C10  C  N N 1   
A1LWP C13  C  N N 2   
A1LWP C21  C  N N 3   
A1LWP C22  C  N N 4   
A1LWP C24  C  N N 5   
A1LWP C01  C  Y N 6   
A1LWP C02  C  Y N 7   
A1LWP C03  C  Y N 8   
A1LWP C04  C  Y N 9   
A1LWP C05  C  Y N 10  
A1LWP C06  C  Y N 11  
A1LWP C07  C  N N 12  
A1LWP C08  C  N N 13  
A1LWP C11  C  N N 14  
A1LWP C12  C  N N 15  
A1LWP C14  C  N N 16  
A1LWP C18  C  N N 17  
A1LWP C19  C  N N 18  
A1LWP C23  C  N N 19  
A1LWP C25  C  N N 20  
A1LWP N20  N  N N 21  
A1LWP O09  O  N N 22  
A1LWP O15  O  N N 23  
A1LWP O16  O  N N 24  
A1LWP O26  O  N N 25  
A1LWP S17  S  N N 26  
A1LWP H2   H  N N 27  
A1LWP H3   H  N N 28  
A1LWP H4   H  N N 29  
A1LWP H5   H  N N 30  
A1LWP H6   H  N N 31  
A1LWP H7   H  N N 32  
A1LWP H8   H  N N 33  
A1LWP H9   H  N N 34  
A1LWP H10  H  N N 35  
A1LWP H11  H  N N 36  
A1LWP H12  H  N N 37  
A1LWP H14  H  N N 38  
A1LWP H15  H  N N 39  
A1LWP H16  H  N N 40  
A1LWP H17  H  N N 41  
A1LWP H18  H  N N 42  
A1LWP H19  H  N N 43  
A1LWP H20  H  N N 44  
A1LWP H21  H  N N 45  
A1LWP H22  H  N N 46  
A1LWP H23  H  N N 47  
ALA   N    N  N N 48  
ALA   CA   C  N S 49  
ALA   C    C  N N 50  
ALA   O    O  N N 51  
ALA   CB   C  N N 52  
ALA   OXT  O  N N 53  
ALA   H    H  N N 54  
ALA   H2   H  N N 55  
ALA   HA   H  N N 56  
ALA   HB1  H  N N 57  
ALA   HB2  H  N N 58  
ALA   HB3  H  N N 59  
ALA   HXT  H  N N 60  
ARG   N    N  N N 61  
ARG   CA   C  N S 62  
ARG   C    C  N N 63  
ARG   O    O  N N 64  
ARG   CB   C  N N 65  
ARG   CG   C  N N 66  
ARG   CD   C  N N 67  
ARG   NE   N  N N 68  
ARG   CZ   C  N N 69  
ARG   NH1  N  N N 70  
ARG   NH2  N  N N 71  
ARG   OXT  O  N N 72  
ARG   H    H  N N 73  
ARG   H2   H  N N 74  
ARG   HA   H  N N 75  
ARG   HB2  H  N N 76  
ARG   HB3  H  N N 77  
ARG   HG2  H  N N 78  
ARG   HG3  H  N N 79  
ARG   HD2  H  N N 80  
ARG   HD3  H  N N 81  
ARG   HE   H  N N 82  
ARG   HH11 H  N N 83  
ARG   HH12 H  N N 84  
ARG   HH21 H  N N 85  
ARG   HH22 H  N N 86  
ARG   HXT  H  N N 87  
ASN   N    N  N N 88  
ASN   CA   C  N S 89  
ASN   C    C  N N 90  
ASN   O    O  N N 91  
ASN   CB   C  N N 92  
ASN   CG   C  N N 93  
ASN   OD1  O  N N 94  
ASN   ND2  N  N N 95  
ASN   OXT  O  N N 96  
ASN   H    H  N N 97  
ASN   H2   H  N N 98  
ASN   HA   H  N N 99  
ASN   HB2  H  N N 100 
ASN   HB3  H  N N 101 
ASN   HD21 H  N N 102 
ASN   HD22 H  N N 103 
ASN   HXT  H  N N 104 
ASP   N    N  N N 105 
ASP   CA   C  N S 106 
ASP   C    C  N N 107 
ASP   O    O  N N 108 
ASP   CB   C  N N 109 
ASP   CG   C  N N 110 
ASP   OD1  O  N N 111 
ASP   OD2  O  N N 112 
ASP   OXT  O  N N 113 
ASP   H    H  N N 114 
ASP   H2   H  N N 115 
ASP   HA   H  N N 116 
ASP   HB2  H  N N 117 
ASP   HB3  H  N N 118 
ASP   HD2  H  N N 119 
ASP   HXT  H  N N 120 
CO    CO   CO N N 121 
CYS   N    N  N N 122 
CYS   CA   C  N R 123 
CYS   C    C  N N 124 
CYS   O    O  N N 125 
CYS   CB   C  N N 126 
CYS   SG   S  N N 127 
CYS   OXT  O  N N 128 
CYS   H    H  N N 129 
CYS   H2   H  N N 130 
CYS   HA   H  N N 131 
CYS   HB2  H  N N 132 
CYS   HB3  H  N N 133 
CYS   HG   H  N N 134 
CYS   HXT  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
THR   N    N  N N 352 
THR   CA   C  N S 353 
THR   C    C  N N 354 
THR   O    O  N N 355 
THR   CB   C  N R 356 
THR   OG1  O  N N 357 
THR   CG2  C  N N 358 
THR   OXT  O  N N 359 
THR   H    H  N N 360 
THR   H2   H  N N 361 
THR   HA   H  N N 362 
THR   HB   H  N N 363 
THR   HG1  H  N N 364 
THR   HG21 H  N N 365 
THR   HG22 H  N N 366 
THR   HG23 H  N N 367 
THR   HXT  H  N N 368 
TRP   N    N  N N 369 
TRP   CA   C  N S 370 
TRP   C    C  N N 371 
TRP   O    O  N N 372 
TRP   CB   C  N N 373 
TRP   CG   C  Y N 374 
TRP   CD1  C  Y N 375 
TRP   CD2  C  Y N 376 
TRP   NE1  N  Y N 377 
TRP   CE2  C  Y N 378 
TRP   CE3  C  Y N 379 
TRP   CZ2  C  Y N 380 
TRP   CZ3  C  Y N 381 
TRP   CH2  C  Y N 382 
TRP   OXT  O  N N 383 
TRP   H    H  N N 384 
TRP   H2   H  N N 385 
TRP   HA   H  N N 386 
TRP   HB2  H  N N 387 
TRP   HB3  H  N N 388 
TRP   HD1  H  N N 389 
TRP   HE1  H  N N 390 
TRP   HE3  H  N N 391 
TRP   HZ2  H  N N 392 
TRP   HZ3  H  N N 393 
TRP   HH2  H  N N 394 
TRP   HXT  H  N N 395 
TYR   N    N  N N 396 
TYR   CA   C  N S 397 
TYR   C    C  N N 398 
TYR   O    O  N N 399 
TYR   CB   C  N N 400 
TYR   CG   C  Y N 401 
TYR   CD1  C  Y N 402 
TYR   CD2  C  Y N 403 
TYR   CE1  C  Y N 404 
TYR   CE2  C  Y N 405 
TYR   CZ   C  Y N 406 
TYR   OH   O  N N 407 
TYR   OXT  O  N N 408 
TYR   H    H  N N 409 
TYR   H2   H  N N 410 
TYR   HA   H  N N 411 
TYR   HB2  H  N N 412 
TYR   HB3  H  N N 413 
TYR   HD1  H  N N 414 
TYR   HD2  H  N N 415 
TYR   HE1  H  N N 416 
TYR   HE2  H  N N 417 
TYR   HH   H  N N 418 
TYR   HXT  H  N N 419 
VAL   N    N  N N 420 
VAL   CA   C  N S 421 
VAL   C    C  N N 422 
VAL   O    O  N N 423 
VAL   CB   C  N N 424 
VAL   CG1  C  N N 425 
VAL   CG2  C  N N 426 
VAL   OXT  O  N N 427 
VAL   H    H  N N 428 
VAL   H2   H  N N 429 
VAL   HA   H  N N 430 
VAL   HB   H  N N 431 
VAL   HG11 H  N N 432 
VAL   HG12 H  N N 433 
VAL   HG13 H  N N 434 
VAL   HG21 H  N N 435 
VAL   HG22 H  N N 436 
VAL   HG23 H  N N 437 
VAL   HXT  H  N N 438 
# 
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 
A1LWP O16 C14  doub N N 1   
A1LWP C25 C23  sing N N 2   
A1LWP O09 C07  doub N N 3   
A1LWP C14 C13  sing N N 4   
A1LWP C14 C08  sing N N 5   
A1LWP C23 C24  sing N N 6   
A1LWP C23 C22  doub N N 7   
A1LWP C07 C08  sing N N 8   
A1LWP C07 C01  sing N N 9   
A1LWP C13 C12  sing N N 10  
A1LWP C21 C22  sing N N 11  
A1LWP C21 N20  sing N N 12  
A1LWP C08 C10  doub N N 13  
A1LWP C06 C01  doub Y N 14  
A1LWP C06 C05  sing Y N 15  
A1LWP C01 C02  sing Y N 16  
A1LWP C10 C11  sing N N 17  
A1LWP C10 O15  sing N N 18  
A1LWP N20 C05  sing N N 19  
A1LWP N20 C19  sing N N 20  
A1LWP C12 C11  sing N N 21  
A1LWP O26 C19  doub N N 22  
A1LWP C05 C04  doub Y N 23  
A1LWP C19 C18  sing N N 24  
A1LWP C02 C03  doub Y N 25  
A1LWP C04 C03  sing Y N 26  
A1LWP C04 S17  sing N N 27  
A1LWP C18 S17  sing N N 28  
A1LWP C13 H2   sing N N 29  
A1LWP C13 H3   sing N N 30  
A1LWP C21 H4   sing N N 31  
A1LWP C21 H5   sing N N 32  
A1LWP C22 H6   sing N N 33  
A1LWP C24 H7   sing N N 34  
A1LWP C24 H8   sing N N 35  
A1LWP C24 H9   sing N N 36  
A1LWP C02 H10  sing N N 37  
A1LWP C03 H11  sing N N 38  
A1LWP C06 H12  sing N N 39  
A1LWP C11 H14  sing N N 40  
A1LWP C11 H15  sing N N 41  
A1LWP C12 H16  sing N N 42  
A1LWP C12 H17  sing N N 43  
A1LWP C18 H18  sing N N 44  
A1LWP C18 H19  sing N N 45  
A1LWP C25 H20  sing N N 46  
A1LWP C25 H21  sing N N 47  
A1LWP C25 H22  sing N N 48  
A1LWP O15 H23  sing N N 49  
ALA   N   CA   sing N N 50  
ALA   N   H    sing N N 51  
ALA   N   H2   sing N N 52  
ALA   CA  C    sing N N 53  
ALA   CA  CB   sing N N 54  
ALA   CA  HA   sing N N 55  
ALA   C   O    doub N N 56  
ALA   C   OXT  sing N N 57  
ALA   CB  HB1  sing N N 58  
ALA   CB  HB2  sing N N 59  
ALA   CB  HB3  sing N N 60  
ALA   OXT HXT  sing N N 61  
ARG   N   CA   sing N N 62  
ARG   N   H    sing N N 63  
ARG   N   H2   sing N N 64  
ARG   CA  C    sing N N 65  
ARG   CA  CB   sing N N 66  
ARG   CA  HA   sing N N 67  
ARG   C   O    doub N N 68  
ARG   C   OXT  sing N N 69  
ARG   CB  CG   sing N N 70  
ARG   CB  HB2  sing N N 71  
ARG   CB  HB3  sing N N 72  
ARG   CG  CD   sing N N 73  
ARG   CG  HG2  sing N N 74  
ARG   CG  HG3  sing N N 75  
ARG   CD  NE   sing N N 76  
ARG   CD  HD2  sing N N 77  
ARG   CD  HD3  sing N N 78  
ARG   NE  CZ   sing N N 79  
ARG   NE  HE   sing N N 80  
ARG   CZ  NH1  sing N N 81  
ARG   CZ  NH2  doub N N 82  
ARG   NH1 HH11 sing N N 83  
ARG   NH1 HH12 sing N N 84  
ARG   NH2 HH21 sing N N 85  
ARG   NH2 HH22 sing N N 86  
ARG   OXT HXT  sing N N 87  
ASN   N   CA   sing N N 88  
ASN   N   H    sing N N 89  
ASN   N   H2   sing N N 90  
ASN   CA  C    sing N N 91  
ASN   CA  CB   sing N N 92  
ASN   CA  HA   sing N N 93  
ASN   C   O    doub N N 94  
ASN   C   OXT  sing N N 95  
ASN   CB  CG   sing N N 96  
ASN   CB  HB2  sing N N 97  
ASN   CB  HB3  sing N N 98  
ASN   CG  OD1  doub N N 99  
ASN   CG  ND2  sing N N 100 
ASN   ND2 HD21 sing N N 101 
ASN   ND2 HD22 sing N N 102 
ASN   OXT HXT  sing N N 103 
ASP   N   CA   sing N N 104 
ASP   N   H    sing N N 105 
ASP   N   H2   sing N N 106 
ASP   CA  C    sing N N 107 
ASP   CA  CB   sing N N 108 
ASP   CA  HA   sing N N 109 
ASP   C   O    doub N N 110 
ASP   C   OXT  sing N N 111 
ASP   CB  CG   sing N N 112 
ASP   CB  HB2  sing N N 113 
ASP   CB  HB3  sing N N 114 
ASP   CG  OD1  doub N N 115 
ASP   CG  OD2  sing N N 116 
ASP   OD2 HD2  sing N N 117 
ASP   OXT HXT  sing N N 118 
CYS   N   CA   sing N N 119 
CYS   N   H    sing N N 120 
CYS   N   H2   sing N N 121 
CYS   CA  C    sing N N 122 
CYS   CA  CB   sing N N 123 
CYS   CA  HA   sing N N 124 
CYS   C   O    doub N N 125 
CYS   C   OXT  sing N N 126 
CYS   CB  SG   sing N N 127 
CYS   CB  HB2  sing N N 128 
CYS   CB  HB3  sing N N 129 
CYS   SG  HG   sing N N 130 
CYS   OXT HXT  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5YY6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XQY 
_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]   0.013002 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002340 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011946 
_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]   0.015524 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CO 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS   A 1 7   ? 23.622  -5.600  90.734  1.00 50.53 ? 35  LYS   A N   1 
ATOM   2    C  CA  . LYS   A 1 7   ? 24.512  -6.419  89.909  1.00 60.75 ? 35  LYS   A CA  1 
ATOM   3    C  C   . LYS   A 1 7   ? 23.908  -6.728  88.522  1.00 56.13 ? 35  LYS   A C   1 
ATOM   4    O  O   . LYS   A 1 7   ? 22.820  -7.304  88.418  1.00 51.84 ? 35  LYS   A O   1 
ATOM   5    C  CB  . LYS   A 1 7   ? 24.851  -7.726  90.639  1.00 55.93 ? 35  LYS   A CB  1 
ATOM   6    N  N   . ASN   A 1 8   ? 24.612  -6.335  87.455  1.00 44.59 ? 36  ASN   A N   1 
ATOM   7    C  CA  . ASN   A 1 8   ? 24.194  -6.631  86.085  1.00 36.43 ? 36  ASN   A CA  1 
ATOM   8    C  C   . ASN   A 1 8   ? 25.210  -7.579  85.468  1.00 40.71 ? 36  ASN   A C   1 
ATOM   9    O  O   . ASN   A 1 8   ? 26.198  -7.135  84.864  1.00 41.78 ? 36  ASN   A O   1 
ATOM   10   C  CB  . ASN   A 1 8   ? 24.059  -5.364  85.246  1.00 40.63 ? 36  ASN   A CB  1 
ATOM   11   C  CG  . ASN   A 1 8   ? 23.378  -5.619  83.897  1.00 42.30 ? 36  ASN   A CG  1 
ATOM   12   O  OD1 . ASN   A 1 8   ? 23.247  -6.770  83.456  1.00 32.89 ? 36  ASN   A OD1 1 
ATOM   13   N  ND2 . ASN   A 1 8   ? 22.951  -4.543  83.237  1.00 33.92 ? 36  ASN   A ND2 1 
ATOM   14   N  N   . PRO   A 1 9   ? 24.982  -8.893  85.560  1.00 38.34 ? 37  PRO   A N   1 
ATOM   15   C  CA  . PRO   A 1 9   ? 25.986  -9.866  85.103  1.00 37.03 ? 37  PRO   A CA  1 
ATOM   16   C  C   . PRO   A 1 9   ? 26.179  -9.907  83.596  1.00 39.16 ? 37  PRO   A C   1 
ATOM   17   O  O   . PRO   A 1 9   ? 27.095  -10.602 83.137  1.00 37.67 ? 37  PRO   A O   1 
ATOM   18   C  CB  . PRO   A 1 9   ? 25.422  -11.195 85.609  1.00 34.37 ? 37  PRO   A CB  1 
ATOM   19   C  CG  . PRO   A 1 9   ? 23.928  -10.967 85.589  1.00 31.93 ? 37  PRO   A CG  1 
ATOM   20   C  CD  . PRO   A 1 9   ? 23.751  -9.549  86.033  1.00 42.04 ? 37  PRO   A CD  1 
ATOM   21   N  N   . LYS   A 1 10  ? 25.355  -9.201  82.828  1.00 34.25 ? 38  LYS   A N   1 
ATOM   22   C  CA  . LYS   A 1 10  ? 25.402  -9.201  81.366  1.00 31.95 ? 38  LYS   A CA  1 
ATOM   23   C  C   . LYS   A 1 10  ? 25.694  -10.596 80.813  1.00 33.54 ? 38  LYS   A C   1 
ATOM   24   O  O   . LYS   A 1 10  ? 26.686  -10.835 80.125  1.00 33.13 ? 38  LYS   A O   1 
ATOM   25   C  CB  . LYS   A 1 10  ? 26.418  -8.185  80.860  1.00 34.88 ? 38  LYS   A CB  1 
ATOM   26   C  CG  . LYS   A 1 10  ? 26.205  -6.774  81.433  1.00 37.60 ? 38  LYS   A CG  1 
ATOM   27   C  CD  . LYS   A 1 10  ? 26.521  -5.682  80.418  1.00 37.53 ? 38  LYS   A CD  1 
ATOM   28   C  CE  . LYS   A 1 10  ? 26.073  -4.330  80.943  1.00 33.70 ? 38  LYS   A CE  1 
ATOM   29   N  NZ  . LYS   A 1 10  ? 27.214  -3.566  81.445  1.00 32.24 ? 38  LYS   A NZ  1 
ATOM   30   N  N   . SER   A 1 11  ? 24.788  -11.525 81.115  1.00 35.70 ? 39  SER   A N   1 
ATOM   31   C  CA  . SER   A 1 11  ? 24.994  -12.930 80.797  1.00 31.54 ? 39  SER   A CA  1 
ATOM   32   C  C   . SER   A 1 11  ? 24.213  -13.393 79.573  1.00 27.27 ? 39  SER   A C   1 
ATOM   33   O  O   . SER   A 1 11  ? 24.008  -14.599 79.409  1.00 31.14 ? 39  SER   A O   1 
ATOM   34   C  CB  . SER   A 1 11  ? 24.647  -13.800 82.008  1.00 31.50 ? 39  SER   A CB  1 
ATOM   35   O  OG  . SER   A 1 11  ? 23.401  -13.438 82.572  1.00 26.46 ? 39  SER   A OG  1 
ATOM   36   N  N   . ASP   A 1 12  ? 23.802  -12.475 78.697  1.00 29.68 ? 40  ASP   A N   1 
ATOM   37   C  CA  . ASP   A 1 12  ? 23.126  -12.873 77.465  1.00 27.70 ? 40  ASP   A CA  1 
ATOM   38   C  C   . ASP   A 1 12  ? 23.980  -13.889 76.723  1.00 27.56 ? 40  ASP   A C   1 
ATOM   39   O  O   . ASP   A 1 12  ? 25.203  -13.768 76.685  1.00 27.47 ? 40  ASP   A O   1 
ATOM   40   C  CB  . ASP   A 1 12  ? 22.874  -11.665 76.549  1.00 25.60 ? 40  ASP   A CB  1 
ATOM   41   C  CG  . ASP   A 1 12  ? 21.816  -10.696 77.096  1.00 24.75 ? 40  ASP   A CG  1 
ATOM   42   O  OD1 . ASP   A 1 12  ? 21.220  -10.964 78.155  1.00 27.07 ? 40  ASP   A OD1 1 
ATOM   43   O  OD2 . ASP   A 1 12  ? 21.591  -9.659  76.450  1.00 22.94 ? 40  ASP   A OD2 1 
ATOM   44   N  N   . LYS   A 1 13  ? 23.327  -14.883 76.118  1.00 21.23 ? 41  LYS   A N   1 
ATOM   45   C  CA  . LYS   A 1 13  ? 24.035  -15.927 75.393  1.00 21.09 ? 41  LYS   A CA  1 
ATOM   46   C  C   . LYS   A 1 13  ? 24.214  -15.596 73.919  1.00 21.85 ? 41  LYS   A C   1 
ATOM   47   O  O   . LYS   A 1 13  ? 25.007  -16.256 73.237  1.00 22.10 ? 41  LYS   A O   1 
ATOM   48   C  CB  . LYS   A 1 13  ? 23.317  -17.270 75.584  1.00 23.29 ? 41  LYS   A CB  1 
ATOM   49   C  CG  . LYS   A 1 13  ? 23.287  -17.664 77.052  1.00 21.41 ? 41  LYS   A CG  1 
ATOM   50   C  CD  . LYS   A 1 13  ? 22.711  -19.042 77.336  1.00 27.10 ? 41  LYS   A CD  1 
ATOM   51   C  CE  . LYS   A 1 13  ? 23.218  -19.535 78.701  1.00 26.77 ? 41  LYS   A CE  1 
ATOM   52   N  NZ  . LYS   A 1 13  ? 22.143  -20.110 79.565  1.00 26.17 ? 41  LYS   A NZ  1 
ATOM   53   N  N   . PHE   A 1 14  ? 23.548  -14.559 73.426  1.00 21.74 ? 42  PHE   A N   1 
ATOM   54   C  CA  . PHE   A 1 14  ? 23.757  -14.092 72.067  1.00 16.47 ? 42  PHE   A CA  1 
ATOM   55   C  C   . PHE   A 1 14  ? 23.447  -12.608 72.053  1.00 19.64 ? 42  PHE   A C   1 
ATOM   56   O  O   . PHE   A 1 14  ? 22.789  -12.092 72.957  1.00 24.67 ? 42  PHE   A O   1 
ATOM   57   C  CB  . PHE   A 1 14  ? 22.884  -14.865 71.071  1.00 23.00 ? 42  PHE   A CB  1 
ATOM   58   C  CG  . PHE   A 1 14  ? 21.477  -15.062 71.541  1.00 24.60 ? 42  PHE   A CG  1 
ATOM   59   C  CD1 . PHE   A 1 14  ? 20.517  -14.087 71.315  1.00 25.11 ? 42  PHE   A CD1 1 
ATOM   60   C  CD2 . PHE   A 1 14  ? 21.109  -16.216 72.225  1.00 24.20 ? 42  PHE   A CD2 1 
ATOM   61   C  CE1 . PHE   A 1 14  ? 19.205  -14.258 71.757  1.00 26.39 ? 42  PHE   A CE1 1 
ATOM   62   C  CE2 . PHE   A 1 14  ? 19.801  -16.392 72.672  1.00 23.01 ? 42  PHE   A CE2 1 
ATOM   63   C  CZ  . PHE   A 1 14  ? 18.847  -15.412 72.436  1.00 23.78 ? 42  PHE   A CZ  1 
ATOM   64   N  N   . LYS   A 1 15  ? 23.928  -11.919 71.024  1.00 24.16 ? 43  LYS   A N   1 
ATOM   65   C  CA  . LYS   A 1 15  ? 23.830  -10.462 70.974  1.00 24.06 ? 43  LYS   A CA  1 
ATOM   66   C  C   . LYS   A 1 15  ? 22.409  -10.048 70.597  1.00 23.18 ? 43  LYS   A C   1 
ATOM   67   O  O   . LYS   A 1 15  ? 21.968  -10.250 69.457  1.00 22.92 ? 43  LYS   A O   1 
ATOM   68   C  CB  . LYS   A 1 15  ? 24.834  -9.887  69.988  1.00 20.08 ? 43  LYS   A CB  1 
ATOM   69   C  CG  . LYS   A 1 15  ? 24.633  -8.423  69.734  1.00 23.74 ? 43  LYS   A CG  1 
ATOM   70   C  CD  . LYS   A 1 15  ? 24.957  -7.592  70.945  1.00 32.93 ? 43  LYS   A CD  1 
ATOM   71   C  CE  . LYS   A 1 15  ? 25.153  -6.125  70.554  1.00 31.58 ? 43  LYS   A CE  1 
ATOM   72   N  NZ  . LYS   A 1 15  ? 23.911  -5.346  70.808  1.00 39.19 ? 43  LYS   A NZ  1 
ATOM   73   N  N   . VAL   A 1 16  ? 21.709  -9.458  71.549  1.00 23.64 ? 44  VAL   A N   1 
ATOM   74   C  CA  . VAL   A 1 16  ? 20.354  -8.947  71.373  1.00 29.08 ? 44  VAL   A CA  1 
ATOM   75   C  C   . VAL   A 1 16  ? 20.427  -7.439  71.184  1.00 29.65 ? 44  VAL   A C   1 
ATOM   76   O  O   . VAL   A 1 16  ? 21.208  -6.762  71.861  1.00 34.71 ? 44  VAL   A O   1 
ATOM   77   C  CB  . VAL   A 1 16  ? 19.491  -9.309  72.595  1.00 26.98 ? 44  VAL   A CB  1 
ATOM   78   C  CG1 . VAL   A 1 16  ? 18.104  -8.668  72.494  1.00 27.65 ? 44  VAL   A CG1 1 
ATOM   79   C  CG2 . VAL   A 1 16  ? 19.403  -10.816 72.732  1.00 18.77 ? 44  VAL   A CG2 1 
ATOM   80   N  N   . LYS   A 1 17  ? 19.613  -6.900  70.277  1.00 27.73 ? 45  LYS   A N   1 
ATOM   81   C  CA  . LYS   A 1 17  ? 19.639  -5.456  70.066  1.00 26.85 ? 45  LYS   A CA  1 
ATOM   82   C  C   . LYS   A 1 17  ? 18.435  -4.762  70.695  1.00 23.29 ? 45  LYS   A C   1 
ATOM   83   O  O   . LYS   A 1 17  ? 18.525  -4.283  71.825  1.00 26.37 ? 45  LYS   A O   1 
ATOM   84   C  CB  . LYS   A 1 17  ? 19.760  -5.160  68.571  1.00 23.55 ? 45  LYS   A CB  1 
ATOM   85   C  CG  . LYS   A 1 17  ? 21.158  -5.470  68.076  1.00 25.98 ? 45  LYS   A CG  1 
ATOM   86   C  CD  . LYS   A 1 17  ? 21.238  -5.730  66.583  1.00 29.22 ? 45  LYS   A CD  1 
ATOM   87   C  CE  . LYS   A 1 17  ? 21.803  -4.548  65.822  1.00 35.36 ? 45  LYS   A CE  1 
ATOM   88   N  NZ  . LYS   A 1 17  ? 20.736  -3.560  65.498  1.00 40.17 ? 45  LYS   A NZ  1 
ATOM   89   N  N   . ARG   A 1 18  ? 17.307  -4.697  69.993  1.00 21.59 ? 46  ARG   A N   1 
ATOM   90   C  CA  . ARG   A 1 18  ? 16.134  -4.007  70.507  1.00 18.14 ? 46  ARG   A CA  1 
ATOM   91   C  C   . ARG   A 1 18  ? 14.881  -4.827  70.230  1.00 21.44 ? 46  ARG   A C   1 
ATOM   92   O  O   . ARG   A 1 18  ? 14.863  -5.734  69.390  1.00 15.88 ? 46  ARG   A O   1 
ATOM   93   C  CB  . ARG   A 1 18  ? 15.964  -2.613  69.876  1.00 17.66 ? 46  ARG   A CB  1 
ATOM   94   C  CG  . ARG   A 1 18  ? 17.045  -1.593  70.216  1.00 22.17 ? 46  ARG   A CG  1 
ATOM   95   C  CD  . ARG   A 1 18  ? 16.996  -1.219  71.680  1.00 25.38 ? 46  ARG   A CD  1 
ATOM   96   N  NE  . ARG   A 1 18  ? 17.938  -0.152  72.049  1.00 31.05 ? 46  ARG   A NE  1 
ATOM   97   C  CZ  . ARG   A 1 18  ? 19.136  -0.336  72.608  1.00 30.74 ? 46  ARG   A CZ  1 
ATOM   98   N  NH1 . ARG   A 1 18  ? 19.585  -1.555  72.863  1.00 26.92 ? 46  ARG   A NH1 1 
ATOM   99   N  NH2 . ARG   A 1 18  ? 19.897  0.715   72.914  1.00 33.81 ? 46  ARG   A NH2 1 
ATOM   100  N  N   . PHE   A 1 19  ? 13.822  -4.485  70.947  1.00 18.70 ? 47  PHE   A N   1 
ATOM   101  C  CA  . PHE   A 1 19  ? 12.493  -4.865  70.493  1.00 18.96 ? 47  PHE   A CA  1 
ATOM   102  C  C   . PHE   A 1 19  ? 12.333  -4.460  69.042  1.00 20.50 ? 47  PHE   A C   1 
ATOM   103  O  O   . PHE   A 1 19  ? 12.690  -3.342  68.657  1.00 19.24 ? 47  PHE   A O   1 
ATOM   104  C  CB  . PHE   A 1 19  ? 11.423  -4.195  71.349  1.00 13.85 ? 47  PHE   A CB  1 
ATOM   105  C  CG  . PHE   A 1 19  ? 11.165  -4.911  72.620  1.00 13.19 ? 47  PHE   A CG  1 
ATOM   106  C  CD1 . PHE   A 1 19  ? 10.895  -6.275  72.610  1.00 12.88 ? 47  PHE   A CD1 1 
ATOM   107  C  CD2 . PHE   A 1 19  ? 11.207  -4.242  73.819  1.00 11.90 ? 47  PHE   A CD2 1 
ATOM   108  C  CE1 . PHE   A 1 19  ? 10.656  -6.948  73.775  1.00 13.33 ? 47  PHE   A CE1 1 
ATOM   109  C  CE2 . PHE   A 1 19  ? 10.975  -4.900  74.981  1.00 12.82 ? 47  PHE   A CE2 1 
ATOM   110  C  CZ  . PHE   A 1 19  ? 10.698  -6.243  74.976  1.00 12.88 ? 47  PHE   A CZ  1 
ATOM   111  N  N   . HIS   A 1 20  ? 11.850  -5.389  68.224  1.00 14.72 ? 48  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 20  ? 11.645  -5.098  66.813  1.00 16.69 ? 48  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 20  ? 10.176  -4.977  66.449  1.00 17.42 ? 48  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 20  ? 9.798   -4.010  65.784  1.00 17.61 ? 48  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 20  ? 12.316  -6.159  65.935  1.00 16.98 ? 48  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 20  ? 12.310  -5.815  64.484  1.00 18.65 ? 48  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 20  ? 11.309  -6.223  63.633  1.00 21.27 ? 48  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 20  ? 13.173  -5.091  63.730  1.00 23.11 ? 48  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 20  ? 11.551  -5.765  62.416  1.00 22.55 ? 48  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 20  ? 12.684  -5.083  62.445  1.00 27.38 ? 48  HIS   A NE2 1 
ATOM   121  N  N   . HIS   A 1 21  ? 9.325   -5.922  66.860  1.00 18.46 ? 49  HIS   A N   1 
ATOM   122  C  CA  . HIS   A 1 21  ? 7.904   -5.754  66.564  1.00 16.74 ? 49  HIS   A CA  1 
ATOM   123  C  C   . HIS   A 1 21  ? 7.066   -6.713  67.393  1.00 23.14 ? 49  HIS   A C   1 
ATOM   124  O  O   . HIS   A 1 21  ? 7.566   -7.649  68.019  1.00 17.27 ? 49  HIS   A O   1 
ATOM   125  C  CB  . HIS   A 1 21  ? 7.594   -5.930  65.072  1.00 20.47 ? 49  HIS   A CB  1 
ATOM   126  C  CG  . HIS   A 1 21  ? 7.835   -7.310  64.532  1.00 19.69 ? 49  HIS   A CG  1 
ATOM   127  N  ND1 . HIS   A 1 21  ? 9.083   -7.756  64.153  1.00 20.51 ? 49  HIS   A ND1 1 
ATOM   128  C  CD2 . HIS   A 1 21  ? 6.972   -8.310  64.226  1.00 23.29 ? 49  HIS   A CD2 1 
ATOM   129  C  CE1 . HIS   A 1 21  ? 8.985   -8.981  63.668  1.00 21.93 ? 49  HIS   A CE1 1 
ATOM   130  N  NE2 . HIS   A 1 21  ? 7.716   -9.346  63.708  1.00 19.97 ? 49  HIS   A NE2 1 
ATOM   131  N  N   . ILE   A 1 22  ? 5.768   -6.446  67.395  1.00 19.30 ? 50  ILE   A N   1 
ATOM   132  C  CA  . ILE   A 1 22  ? 4.797   -7.280  68.074  1.00 19.45 ? 50  ILE   A CA  1 
ATOM   133  C  C   . ILE   A 1 22  ? 3.802   -7.719  67.024  1.00 17.69 ? 50  ILE   A C   1 
ATOM   134  O  O   . ILE   A 1 22  ? 3.334   -6.891  66.235  1.00 17.84 ? 50  ILE   A O   1 
ATOM   135  C  CB  . ILE   A 1 22  ? 4.112   -6.515  69.215  1.00 17.67 ? 50  ILE   A CB  1 
ATOM   136  C  CG1 . ILE   A 1 22  ? 5.114   -6.251  70.343  1.00 23.88 ? 50  ILE   A CG1 1 
ATOM   137  C  CG2 . ILE   A 1 22  ? 2.844   -7.236  69.676  1.00 19.50 ? 50  ILE   A CG2 1 
ATOM   138  C  CD1 . ILE   A 1 22  ? 5.746   -7.515  70.989  1.00 20.80 ? 50  ILE   A CD1 1 
ATOM   139  N  N   . GLU   A 1 23  ? 3.523   -9.018  66.963  1.00 15.16 ? 51  GLU   A N   1 
ATOM   140  C  CA  . GLU   A 1 23  ? 2.593   -9.533  65.965  1.00 17.82 ? 51  GLU   A CA  1 
ATOM   141  C  C   . GLU   A 1 23  ? 1.348   -10.062 66.645  1.00 17.68 ? 51  GLU   A C   1 
ATOM   142  O  O   . GLU   A 1 23  ? 1.425   -10.982 67.474  1.00 16.27 ? 51  GLU   A O   1 
ATOM   143  C  CB  . GLU   A 1 23  ? 3.198   -10.620 65.092  1.00 18.06 ? 51  GLU   A CB  1 
ATOM   144  C  CG  . GLU   A 1 23  ? 2.162   -11.195 64.140  1.00 19.28 ? 51  GLU   A CG  1 
ATOM   145  C  CD  . GLU   A 1 23  ? 2.748   -12.143 63.103  1.00 15.07 ? 51  GLU   A CD  1 
ATOM   146  O  OE1 . GLU   A 1 23  ? 3.805   -12.738 63.359  1.00 20.49 ? 51  GLU   A OE1 1 
ATOM   147  O  OE2 . GLU   A 1 23  ? 2.140   -12.302 62.033  1.00 16.17 ? 51  GLU   A OE2 1 
ATOM   148  N  N   . PHE   A 1 24  ? 0.211   -9.474  66.287  1.00 15.18 ? 52  PHE   A N   1 
ATOM   149  C  CA  . PHE   A 1 24  ? -1.095  -9.921  66.745  1.00 15.57 ? 52  PHE   A CA  1 
ATOM   150  C  C   . PHE   A 1 24  ? -1.644  -10.967 65.783  1.00 13.71 ? 52  PHE   A C   1 
ATOM   151  O  O   . PHE   A 1 24  ? -1.569  -10.811 64.566  1.00 16.28 ? 52  PHE   A O   1 
ATOM   152  C  CB  . PHE   A 1 24  ? -2.066  -8.734  66.832  1.00 12.90 ? 52  PHE   A CB  1 
ATOM   153  C  CG  . PHE   A 1 24  ? -1.770  -7.782  67.945  1.00 12.24 ? 52  PHE   A CG  1 
ATOM   154  C  CD1 . PHE   A 1 24  ? -0.821  -6.783  67.782  1.00 16.23 ? 52  PHE   A CD1 1 
ATOM   155  C  CD2 . PHE   A 1 24  ? -2.438  -7.882  69.151  1.00 13.16 ? 52  PHE   A CD2 1 
ATOM   156  C  CE1 . PHE   A 1 24  ? -0.534  -5.891  68.809  1.00 16.00 ? 52  PHE   A CE1 1 
ATOM   157  C  CE2 . PHE   A 1 24  ? -2.160  -7.004  70.185  1.00 16.20 ? 52  PHE   A CE2 1 
ATOM   158  C  CZ  . PHE   A 1 24  ? -1.204  -6.005  70.015  1.00 16.68 ? 52  PHE   A CZ  1 
ATOM   159  N  N   . TRP   A 1 25  ? -2.219  -12.026 66.319  1.00 18.42 ? 53  TRP   A N   1 
ATOM   160  C  CA  . TRP   A 1 25  ? -2.890  -13.009 65.479  1.00 17.77 ? 53  TRP   A CA  1 
ATOM   161  C  C   . TRP   A 1 25  ? -4.382  -12.742 65.615  1.00 13.34 ? 53  TRP   A C   1 
ATOM   162  O  O   . TRP   A 1 25  ? -4.905  -12.689 66.728  1.00 14.65 ? 53  TRP   A O   1 
ATOM   163  C  CB  . TRP   A 1 25  ? -2.484  -14.445 65.854  1.00 17.35 ? 53  TRP   A CB  1 
ATOM   164  C  CG  . TRP   A 1 25  ? -1.384  -15.050 64.900  1.00 15.78 ? 53  TRP   A CG  1 
ATOM   165  C  CD1 . TRP   A 1 25  ? -0.763  -14.413 63.853  1.00 16.52 ? 53  TRP   A CD1 1 
ATOM   166  C  CD2 . TRP   A 1 25  ? -0.833  -16.394 64.916  1.00 19.03 ? 53  TRP   A CD2 1 
ATOM   167  N  NE1 . TRP   A 1 25  ? 0.133   -15.254 63.236  1.00 19.12 ? 53  TRP   A NE1 1 
ATOM   168  C  CE2 . TRP   A 1 25  ? 0.109   -16.476 63.863  1.00 18.84 ? 53  TRP   A CE2 1 
ATOM   169  C  CE3 . TRP   A 1 25  ? -1.035  -17.518 65.722  1.00 17.84 ? 53  TRP   A CE3 1 
ATOM   170  C  CZ2 . TRP   A 1 25  ? 0.830   -17.647 63.583  1.00 16.24 ? 53  TRP   A CZ2 1 
ATOM   171  C  CZ3 . TRP   A 1 25  ? -0.291  -18.688 65.455  1.00 19.05 ? 53  TRP   A CZ3 1 
ATOM   172  C  CH2 . TRP   A 1 25  ? 0.623   -18.737 64.392  1.00 16.07 ? 53  TRP   A CH2 1 
ATOM   173  N  N   . CYS   A 1 26  ? -5.037  -12.485 64.488  1.00 19.45 ? 54  CYS   A N   1 
ATOM   174  C  CA  . CYS   A 1 26  ? -6.382  -11.920 64.403  1.00 14.63 ? 54  CYS   A CA  1 
ATOM   175  C  C   . CYS   A 1 26  ? -7.339  -12.915 63.760  1.00 17.76 ? 54  CYS   A C   1 
ATOM   176  O  O   . CYS   A 1 26  ? -6.928  -13.880 63.107  1.00 16.64 ? 54  CYS   A O   1 
ATOM   177  C  CB  . CYS   A 1 26  ? -6.387  -10.624 63.566  1.00 17.07 ? 54  CYS   A CB  1 
ATOM   178  S  SG  . CYS   A 1 26  ? -5.136  -9.356  64.078  1.00 23.57 ? 54  CYS   A SG  1 
ATOM   179  N  N   . GLY   A 1 27  ? -8.628  -12.646 63.932  1.00 13.27 ? 55  GLY   A N   1 
ATOM   180  C  CA  . GLY   A 1 27  ? -9.620  -13.251 63.072  1.00 13.41 ? 55  GLY   A CA  1 
ATOM   181  C  C   . GLY   A 1 27  ? -9.678  -12.488 61.769  1.00 16.22 ? 55  GLY   A C   1 
ATOM   182  O  O   . GLY   A 1 27  ? -9.682  -13.066 60.673  1.00 12.74 ? 55  GLY   A O   1 
ATOM   183  N  N   . ASP   A 1 28  ? -9.690  -11.161 61.882  1.00 16.23 ? 56  ASP   A N   1 
ATOM   184  C  CA  . ASP   A 1 28  ? -9.728  -10.275 60.721  1.00 17.34 ? 56  ASP   A CA  1 
ATOM   185  C  C   . ASP   A 1 28  ? -8.683  -9.189  60.945  1.00 15.35 ? 56  ASP   A C   1 
ATOM   186  O  O   . ASP   A 1 28  ? -8.808  -8.397  61.880  1.00 16.27 ? 56  ASP   A O   1 
ATOM   187  C  CB  . ASP   A 1 28  ? -11.135 -9.685  60.523  1.00 12.30 ? 56  ASP   A CB  1 
ATOM   188  C  CG  . ASP   A 1 28  ? -11.189 -8.682  59.399  1.00 16.17 ? 56  ASP   A CG  1 
ATOM   189  O  OD1 . ASP   A 1 28  ? -11.360 -9.100  58.238  1.00 15.40 ? 56  ASP   A OD1 1 
ATOM   190  O  OD2 . ASP   A 1 28  ? -11.029 -7.462  59.672  1.00 18.56 ? 56  ASP   A OD2 1 
ATOM   191  N  N   . ALA   A 1 29  ? -7.623  -9.178  60.126  1.00 16.07 ? 57  ALA   A N   1 
ATOM   192  C  CA  . ALA   A 1 29  ? -6.496  -8.296  60.427  1.00 15.17 ? 57  ALA   A CA  1 
ATOM   193  C  C   . ALA   A 1 29  ? -6.859  -6.852  60.136  1.00 17.29 ? 57  ALA   A C   1 
ATOM   194  O  O   . ALA   A 1 29  ? -6.444  -5.937  60.861  1.00 20.33 ? 57  ALA   A O   1 
ATOM   195  C  CB  . ALA   A 1 29  ? -5.254  -8.695  59.624  1.00 12.62 ? 57  ALA   A CB  1 
ATOM   196  N  N   . THR   A 1 30  ? -7.623  -6.642  59.065  1.00 12.92 ? 58  THR   A N   1 
ATOM   197  C  CA  . THR   A 1 30  ? -8.057  -5.309  58.671  1.00 19.03 ? 58  THR   A CA  1 
ATOM   198  C  C   . THR   A 1 30  ? -8.692  -4.542  59.821  1.00 17.37 ? 58  THR   A C   1 
ATOM   199  O  O   . THR   A 1 30  ? -8.252  -3.437  60.162  1.00 21.47 ? 58  THR   A O   1 
ATOM   200  C  CB  . THR   A 1 30  ? -9.027  -5.436  57.516  1.00 13.85 ? 58  THR   A CB  1 
ATOM   201  O  OG1 . THR   A 1 30  ? -8.307  -5.938  56.384  1.00 19.77 ? 58  THR   A OG1 1 
ATOM   202  C  CG2 . THR   A 1 30  ? -9.641  -4.112  57.206  1.00 12.31 ? 58  THR   A CG2 1 
ATOM   203  N  N   . ASN   A 1 31  ? -9.704  -5.124  60.460  1.00 13.14 ? 59  ASN   A N   1 
ATOM   204  C  CA  . ASN   A 1 31  ? -10.492 -4.342  61.406  1.00 16.38 ? 59  ASN   A CA  1 
ATOM   205  C  C   . ASN   A 1 31  ? -9.730  -4.054  62.687  1.00 16.47 ? 59  ASN   A C   1 
ATOM   206  O  O   . ASN   A 1 31  ? -9.903  -2.985  63.277  1.00 13.83 ? 59  ASN   A O   1 
ATOM   207  C  CB  . ASN   A 1 31  ? -11.802 -5.048  61.726  1.00 14.76 ? 59  ASN   A CB  1 
ATOM   208  C  CG  . ASN   A 1 31  ? -12.862 -4.731  60.740  1.00 14.15 ? 59  ASN   A CG  1 
ATOM   209  O  OD1 . ASN   A 1 31  ? -13.666 -3.827  60.957  1.00 16.76 ? 59  ASN   A OD1 1 
ATOM   210  N  ND2 . ASN   A 1 31  ? -12.851 -5.433  59.612  1.00 13.43 ? 59  ASN   A ND2 1 
ATOM   211  N  N   . VAL   A 1 32  ? -8.939  -5.018  63.178  1.00 16.86 ? 60  VAL   A N   1 
ATOM   212  C  CA  . VAL   A 1 32  ? -8.073  -4.724  64.317  1.00 15.14 ? 60  VAL   A CA  1 
ATOM   213  C  C   . VAL   A 1 32  ? -7.055  -3.648  63.945  1.00 19.05 ? 60  VAL   A C   1 
ATOM   214  O  O   . VAL   A 1 32  ? -6.805  -2.709  64.715  1.00 18.07 ? 60  VAL   A O   1 
ATOM   215  C  CB  . VAL   A 1 32  ? -7.384  -6.007  64.819  1.00 20.86 ? 60  VAL   A CB  1 
ATOM   216  C  CG1 . VAL   A 1 32  ? -6.545  -5.709  66.059  1.00 17.10 ? 60  VAL   A CG1 1 
ATOM   217  C  CG2 . VAL   A 1 32  ? -8.410  -7.058  65.127  1.00 16.14 ? 60  VAL   A CG2 1 
ATOM   218  N  N   . ALA   A 1 33  ? -6.464  -3.760  62.750  1.00 18.38 ? 61  ALA   A N   1 
ATOM   219  C  CA  . ALA   A 1 33  ? -5.443  -2.803  62.337  1.00 14.31 ? 61  ALA   A CA  1 
ATOM   220  C  C   . ALA   A 1 33  ? -6.011  -1.394  62.226  1.00 21.18 ? 61  ALA   A C   1 
ATOM   221  O  O   . ALA   A 1 33  ? -5.369  -0.424  62.647  1.00 18.76 ? 61  ALA   A O   1 
ATOM   222  C  CB  . ALA   A 1 33  ? -4.823  -3.234  61.011  1.00 15.55 ? 61  ALA   A CB  1 
ATOM   223  N  N   . ARG   A 1 34  ? -7.216  -1.258  61.660  1.00 21.73 ? 62  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 34  ? -7.839  0.061   61.553  1.00 14.48 ? 62  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 34  ? -8.187  0.625   62.929  1.00 18.59 ? 62  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 34  ? -7.908  1.791   63.212  1.00 16.88 ? 62  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 34  ? -9.085  -0.025  60.679  1.00 18.55 ? 62  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 34  ? -8.794  -0.561  59.315  1.00 16.88 ? 62  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 34  ? -9.095  0.447   58.272  1.00 14.55 ? 62  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 34  ? -8.402  0.184   57.023  1.00 11.97 ? 62  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 34  ? -8.574  0.921   55.939  1.00 18.45 ? 62  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 34  ? -7.910  0.650   54.826  1.00 19.65 ? 62  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 34  ? -9.428  1.942   55.974  1.00 21.22 ? 62  ARG   A NH2 1 
ATOM   234  N  N   . ARG   A 1 35  ? -8.766  -0.199  63.805  1.00 19.61 ? 63  ARG   A N   1 
ATOM   235  C  CA  . ARG   A 1 35  ? -9.067  0.236   65.169  1.00 16.87 ? 63  ARG   A CA  1 
ATOM   236  C  C   . ARG   A 1 35  ? -7.801  0.671   65.910  1.00 19.37 ? 63  ARG   A C   1 
ATOM   237  O  O   . ARG   A 1 35  ? -7.782  1.722   66.561  1.00 18.98 ? 63  ARG   A O   1 
ATOM   238  C  CB  . ARG   A 1 35  ? -9.785  -0.901  65.907  1.00 12.89 ? 63  ARG   A CB  1 
ATOM   239  C  CG  . ARG   A 1 35  ? -10.564 -0.569  67.188  1.00 14.65 ? 63  ARG   A CG  1 
ATOM   240  C  CD  . ARG   A 1 35  ? -9.650  -0.363  68.384  1.00 16.89 ? 63  ARG   A CD  1 
ATOM   241  N  NE  . ARG   A 1 35  ? -10.349 -0.225  69.657  1.00 13.37 ? 63  ARG   A NE  1 
ATOM   242  C  CZ  . ARG   A 1 35  ? -10.372 -1.136  70.618  1.00 13.67 ? 63  ARG   A CZ  1 
ATOM   243  N  NH1 . ARG   A 1 35  ? -11.011 -0.886  71.757  1.00 16.59 ? 63  ARG   A NH1 1 
ATOM   244  N  NH2 . ARG   A 1 35  ? -9.764  -2.301  70.452  1.00 14.30 ? 63  ARG   A NH2 1 
ATOM   245  N  N   . PHE   A 1 36  ? -6.744  -0.144  65.858  1.00 18.11 ? 64  PHE   A N   1 
ATOM   246  C  CA  . PHE   A 1 36  ? -5.527  0.186   66.599  1.00 16.81 ? 64  PHE   A CA  1 
ATOM   247  C  C   . PHE   A 1 36  ? -4.893  1.449   66.060  1.00 18.06 ? 64  PHE   A C   1 
ATOM   248  O  O   . PHE   A 1 36  ? -4.358  2.249   66.829  1.00 15.34 ? 64  PHE   A O   1 
ATOM   249  C  CB  . PHE   A 1 36  ? -4.518  -0.963  66.546  1.00 14.00 ? 64  PHE   A CB  1 
ATOM   250  C  CG  . PHE   A 1 36  ? -4.738  -1.992  67.614  1.00 16.58 ? 64  PHE   A CG  1 
ATOM   251  C  CD1 . PHE   A 1 36  ? -5.971  -2.638  67.726  1.00 12.47 ? 64  PHE   A CD1 1 
ATOM   252  C  CD2 . PHE   A 1 36  ? -3.730  -2.321  68.497  1.00 14.73 ? 64  PHE   A CD2 1 
ATOM   253  C  CE1 . PHE   A 1 36  ? -6.187  -3.565  68.718  1.00 14.32 ? 64  PHE   A CE1 1 
ATOM   254  C  CE2 . PHE   A 1 36  ? -3.938  -3.262  69.491  1.00 14.80 ? 64  PHE   A CE2 1 
ATOM   255  C  CZ  . PHE   A 1 36  ? -5.167  -3.892  69.595  1.00 16.98 ? 64  PHE   A CZ  1 
ATOM   256  N  N   . SER   A 1 37  ? -4.943  1.630   64.740  1.00 16.62 ? 65  SER   A N   1 
ATOM   257  C  CA  . SER   A 1 37  ? -4.368  2.809   64.117  1.00 17.62 ? 65  SER   A CA  1 
ATOM   258  C  C   . SER   A 1 37  ? -5.014  4.077   64.650  1.00 23.17 ? 65  SER   A C   1 
ATOM   259  O  O   . SER   A 1 37  ? -4.328  4.988   65.135  1.00 18.48 ? 65  SER   A O   1 
ATOM   260  C  CB  . SER   A 1 37  ? -4.533  2.717   62.608  1.00 14.64 ? 65  SER   A CB  1 
ATOM   261  O  OG  . SER   A 1 37  ? -3.850  3.788   61.992  1.00 20.08 ? 65  SER   A OG  1 
ATOM   262  N  N   . TRP   A 1 38  ? -6.346  4.136   64.586  1.00 18.01 ? 66  TRP   A N   1 
ATOM   263  C  CA  . TRP   A 1 38  ? -7.065  5.309   65.059  1.00 20.46 ? 66  TRP   A CA  1 
ATOM   264  C  C   . TRP   A 1 38  ? -6.880  5.514   66.552  1.00 18.87 ? 66  TRP   A C   1 
ATOM   265  O  O   . TRP   A 1 38  ? -6.756  6.651   67.018  1.00 16.39 ? 66  TRP   A O   1 
ATOM   266  C  CB  . TRP   A 1 38  ? -8.549  5.155   64.722  1.00 19.25 ? 66  TRP   A CB  1 
ATOM   267  C  CG  . TRP   A 1 38  ? -9.438  6.232   65.249  1.00 22.65 ? 66  TRP   A CG  1 
ATOM   268  C  CD1 . TRP   A 1 38  ? -10.563 6.060   65.999  1.00 22.04 ? 66  TRP   A CD1 1 
ATOM   269  C  CD2 . TRP   A 1 38  ? -9.300  7.650   65.049  1.00 24.66 ? 66  TRP   A CD2 1 
ATOM   270  N  NE1 . TRP   A 1 38  ? -11.136 7.275   66.280  1.00 22.76 ? 66  TRP   A NE1 1 
ATOM   271  C  CE2 . TRP   A 1 38  ? -10.387 8.268   65.703  1.00 23.16 ? 66  TRP   A CE2 1 
ATOM   272  C  CE3 . TRP   A 1 38  ? -8.370  8.454   64.374  1.00 22.41 ? 66  TRP   A CE3 1 
ATOM   273  C  CZ2 . TRP   A 1 38  ? -10.560 9.657   65.722  1.00 18.50 ? 66  TRP   A CZ2 1 
ATOM   274  C  CZ3 . TRP   A 1 38  ? -8.554  9.828   64.375  1.00 23.96 ? 66  TRP   A CZ3 1 
ATOM   275  C  CH2 . TRP   A 1 38  ? -9.645  10.415  65.041  1.00 25.03 ? 66  TRP   A CH2 1 
ATOM   276  N  N   . GLY   A 1 39  ? -6.870  4.427   67.323  1.00 12.82 ? 67  GLY   A N   1 
ATOM   277  C  CA  . GLY   A 1 39  ? -6.907  4.577   68.764  1.00 16.08 ? 67  GLY   A CA  1 
ATOM   278  C  C   . GLY   A 1 39  ? -5.566  4.848   69.406  1.00 18.06 ? 67  GLY   A C   1 
ATOM   279  O  O   . GLY   A 1 39  ? -5.522  5.390   70.512  1.00 19.81 ? 67  GLY   A O   1 
ATOM   280  N  N   . LEU   A 1 40  ? -4.475  4.479   68.745  1.00 20.00 ? 68  LEU   A N   1 
ATOM   281  C  CA  . LEU   A 1 40  ? -3.129  4.705   69.259  1.00 15.77 ? 68  LEU   A CA  1 
ATOM   282  C  C   . LEU   A 1 40  ? -2.343  5.704   68.415  1.00 19.33 ? 68  LEU   A C   1 
ATOM   283  O  O   . LEU   A 1 40  ? -1.209  6.041   68.766  1.00 17.39 ? 68  LEU   A O   1 
ATOM   284  C  CB  . LEU   A 1 40  ? -2.374  3.367   69.339  1.00 19.81 ? 68  LEU   A CB  1 
ATOM   285  C  CG  . LEU   A 1 40  ? -2.931  2.315   70.309  1.00 16.69 ? 68  LEU   A CG  1 
ATOM   286  C  CD1 . LEU   A 1 40  ? -2.692  0.891   69.787  1.00 16.54 ? 68  LEU   A CD1 1 
ATOM   287  C  CD2 . LEU   A 1 40  ? -2.337  2.471   71.682  1.00 16.04 ? 68  LEU   A CD2 1 
ATOM   288  N  N   . GLY   A 1 41  ? -2.909  6.179   67.309  1.00 20.06 ? 69  GLY   A N   1 
ATOM   289  C  CA  . GLY   A 1 41  ? -2.193  7.079   66.440  1.00 21.25 ? 69  GLY   A CA  1 
ATOM   290  C  C   . GLY   A 1 41  ? -0.954  6.425   65.878  1.00 26.59 ? 69  GLY   A C   1 
ATOM   291  O  O   . GLY   A 1 41  ? 0.147   6.992   65.925  1.00 23.39 ? 69  GLY   A O   1 
ATOM   292  N  N   . MET   A 1 42  ? -1.131  5.216   65.357  1.00 20.91 ? 70  MET   A N   1 
ATOM   293  C  CA  . MET   A 1 42  ? -0.096  4.514   64.627  1.00 19.54 ? 70  MET   A CA  1 
ATOM   294  C  C   . MET   A 1 42  ? -0.419  4.539   63.140  1.00 24.52 ? 70  MET   A C   1 
ATOM   295  O  O   . MET   A 1 42  ? -1.585  4.580   62.734  1.00 24.51 ? 70  MET   A O   1 
ATOM   296  C  CB  . MET   A 1 42  ? 0.047   3.072   65.119  1.00 16.15 ? 70  MET   A CB  1 
ATOM   297  C  CG  . MET   A 1 42  ? 0.137   2.974   66.622  1.00 16.52 ? 70  MET   A CG  1 
ATOM   298  S  SD  . MET   A 1 42  ? 0.521   1.310   67.191  1.00 22.69 ? 70  MET   A SD  1 
ATOM   299  C  CE  . MET   A 1 42  ? 2.084   1.112   66.337  1.00 12.94 ? 70  MET   A CE  1 
ATOM   300  N  N   . ARG   A 1 43  ? 0.630   4.478   62.343  1.00 19.76 ? 71  ARG   A N   1 
ATOM   301  C  CA  . ARG   A 1 43  ? 0.592   4.776   60.921  1.00 23.47 ? 71  ARG   A CA  1 
ATOM   302  C  C   . ARG   A 1 43  ? 0.583   3.486   60.115  1.00 20.23 ? 71  ARG   A C   1 
ATOM   303  O  O   . ARG   A 1 43  ? 1.333   2.557   60.414  1.00 21.88 ? 71  ARG   A O   1 
ATOM   304  C  CB  . ARG   A 1 43  ? 1.819   5.609   60.547  1.00 20.67 ? 71  ARG   A CB  1 
ATOM   305  C  CG  . ARG   A 1 43  ? 1.938   6.003   59.113  1.00 26.40 ? 71  ARG   A CG  1 
ATOM   306  C  CD  . ARG   A 1 43  ? 2.810   7.240   58.997  1.00 26.22 ? 71  ARG   A CD  1 
ATOM   307  N  NE  . ARG   A 1 43  ? 2.436   7.959   57.773  1.00 34.21 ? 71  ARG   A NE  1 
ATOM   308  C  CZ  . ARG   A 1 43  ? 3.188   8.856   57.141  1.00 37.81 ? 71  ARG   A CZ  1 
ATOM   309  N  NH1 . ARG   A 1 43  ? 2.717   9.443   56.044  1.00 41.81 ? 71  ARG   A NH1 1 
ATOM   310  N  NH2 . ARG   A 1 43  ? 4.386   9.174   57.641  1.00 33.74 ? 71  ARG   A NH2 1 
ATOM   311  N  N   . PHE   A 1 44  ? -0.212  3.459   59.053  1.00 18.41 ? 72  PHE   A N   1 
ATOM   312  C  CA  . PHE   A 1 44  ? -0.278  2.295   58.165  1.00 25.12 ? 72  PHE   A CA  1 
ATOM   313  C  C   . PHE   A 1 44  ? 0.954   2.318   57.265  1.00 24.88 ? 72  PHE   A C   1 
ATOM   314  O  O   . PHE   A 1 44  ? 1.007   3.064   56.287  1.00 22.64 ? 72  PHE   A O   1 
ATOM   315  C  CB  . PHE   A 1 44  ? -1.579  2.310   57.365  1.00 22.43 ? 72  PHE   A CB  1 
ATOM   316  C  CG  . PHE   A 1 44  ? -1.778  1.097   56.485  1.00 24.73 ? 72  PHE   A CG  1 
ATOM   317  C  CD1 . PHE   A 1 44  ? -1.170  -0.112  56.785  1.00 22.79 ? 72  PHE   A CD1 1 
ATOM   318  C  CD2 . PHE   A 1 44  ? -2.559  1.179   55.349  1.00 26.89 ? 72  PHE   A CD2 1 
ATOM   319  C  CE1 . PHE   A 1 44  ? -1.344  -1.219  55.970  1.00 26.25 ? 72  PHE   A CE1 1 
ATOM   320  C  CE2 . PHE   A 1 44  ? -2.741  0.079   54.523  1.00 22.97 ? 72  PHE   A CE2 1 
ATOM   321  C  CZ  . PHE   A 1 44  ? -2.135  -1.124  54.836  1.00 25.86 ? 72  PHE   A CZ  1 
ATOM   322  N  N   . SER   A 1 45  ? 1.965   1.494   57.576  1.00 20.53 ? 73  SER   A N   1 
ATOM   323  C  CA  . SER   A 1 45  ? 3.230   1.624   56.861  1.00 23.06 ? 73  SER   A CA  1 
ATOM   324  C  C   . SER   A 1 45  ? 3.583   0.470   55.931  1.00 28.11 ? 73  SER   A C   1 
ATOM   325  O  O   . SER   A 1 45  ? 4.340   0.687   54.979  1.00 32.52 ? 73  SER   A O   1 
ATOM   326  C  CB  . SER   A 1 45  ? 4.383   1.830   57.848  1.00 23.30 ? 73  SER   A CB  1 
ATOM   327  O  OG  . SER   A 1 45  ? 4.488   0.742   58.732  1.00 31.98 ? 73  SER   A OG  1 
ATOM   328  N  N   . ALA   A 1 46  ? 3.051   -0.730  56.145  1.00 20.52 ? 74  ALA   A N   1 
ATOM   329  C  CA  . ALA   A 1 46  ? 3.390   -1.834  55.262  1.00 23.79 ? 74  ALA   A CA  1 
ATOM   330  C  C   . ALA   A 1 46  ? 2.282   -2.873  55.260  1.00 22.34 ? 74  ALA   A C   1 
ATOM   331  O  O   . ALA   A 1 46  ? 1.510   -2.996  56.213  1.00 22.04 ? 74  ALA   A O   1 
ATOM   332  C  CB  . ALA   A 1 46  ? 4.709   -2.490  55.665  1.00 23.11 ? 74  ALA   A CB  1 
ATOM   333  N  N   . LYS   A 1 47  ? 2.233   -3.644  54.180  1.00 26.45 ? 75  LYS   A N   1 
ATOM   334  C  CA  . LYS   A 1 47  ? 1.243   -4.698  54.046  1.00 21.37 ? 75  LYS   A CA  1 
ATOM   335  C  C   . LYS   A 1 47  ? 1.845   -5.892  53.330  1.00 22.34 ? 75  LYS   A C   1 
ATOM   336  O  O   . LYS   A 1 47  ? 2.740   -5.752  52.494  1.00 26.18 ? 75  LYS   A O   1 
ATOM   337  C  CB  . LYS   A 1 47  ? -0.003  -4.221  53.288  1.00 22.15 ? 75  LYS   A CB  1 
ATOM   338  C  CG  . LYS   A 1 47  ? 0.265   -3.653  51.910  1.00 21.57 ? 75  LYS   A CG  1 
ATOM   339  C  CD  . LYS   A 1 47  ? -1.046  -3.312  51.191  1.00 24.87 ? 75  LYS   A CD  1 
ATOM   340  C  CE  . LYS   A 1 47  ? -0.787  -2.945  49.734  1.00 25.65 ? 75  LYS   A CE  1 
ATOM   341  N  NZ  . LYS   A 1 47  ? -2.033  -2.628  49.001  1.00 26.57 ? 75  LYS   A NZ  1 
ATOM   342  N  N   . SER   A 1 48  ? 1.351   -7.072  53.691  1.00 16.65 ? 76  SER   A N   1 
ATOM   343  C  CA  . SER   A 1 48  ? 1.497   -8.284  52.896  1.00 18.69 ? 76  SER   A CA  1 
ATOM   344  C  C   . SER   A 1 48  ? 0.125   -8.942  52.836  1.00 20.60 ? 76  SER   A C   1 
ATOM   345  O  O   . SER   A 1 48  ? -0.428  -9.299  53.880  1.00 19.68 ? 76  SER   A O   1 
ATOM   346  C  CB  . SER   A 1 48  ? 2.521   -9.229  53.515  1.00 16.30 ? 76  SER   A CB  1 
ATOM   347  O  OG  . SER   A 1 48  ? 2.809   -10.286 52.627  1.00 21.59 ? 76  SER   A OG  1 
ATOM   348  N  N   . ASP   A 1 49  ? -0.440  -9.070  51.639  1.00 20.26 ? 77  ASP   A N   1 
ATOM   349  C  CA  . ASP   A 1 49  ? -1.777  -9.650  51.526  1.00 21.73 ? 77  ASP   A CA  1 
ATOM   350  C  C   . ASP   A 1 49  ? -2.041  -10.065 50.077  1.00 19.68 ? 77  ASP   A C   1 
ATOM   351  O  O   . ASP   A 1 49  ? -1.107  -10.222 49.282  1.00 21.38 ? 77  ASP   A O   1 
ATOM   352  C  CB  . ASP   A 1 49  ? -2.834  -8.665  52.065  1.00 17.99 ? 77  ASP   A CB  1 
ATOM   353  C  CG  . ASP   A 1 49  ? -2.917  -7.377  51.269  1.00 22.08 ? 77  ASP   A CG  1 
ATOM   354  O  OD1 . ASP   A 1 49  ? -2.371  -7.314  50.144  1.00 21.60 ? 77  ASP   A OD1 1 
ATOM   355  O  OD2 . ASP   A 1 49  ? -3.569  -6.429  51.762  1.00 20.43 ? 77  ASP   A OD2 1 
ATOM   356  N  N   . LEU   A 1 50  ? -3.317  -10.207 49.726  1.00 20.14 ? 78  LEU   A N   1 
ATOM   357  C  CA  . LEU   A 1 50  ? -3.675  -10.590 48.368  1.00 18.32 ? 78  LEU   A CA  1 
ATOM   358  C  C   . LEU   A 1 50  ? -3.099  -9.629  47.339  1.00 25.93 ? 78  LEU   A C   1 
ATOM   359  O  O   . LEU   A 1 50  ? -2.641  -10.059 46.275  1.00 24.57 ? 78  LEU   A O   1 
ATOM   360  C  CB  . LEU   A 1 50  ? -5.192  -10.650 48.233  1.00 18.49 ? 78  LEU   A CB  1 
ATOM   361  C  CG  . LEU   A 1 50  ? -5.901  -11.757 49.016  1.00 24.00 ? 78  LEU   A CG  1 
ATOM   362  C  CD1 . LEU   A 1 50  ? -7.397  -11.647 48.780  1.00 19.56 ? 78  LEU   A CD1 1 
ATOM   363  C  CD2 . LEU   A 1 50  ? -5.369  -13.157 48.684  1.00 17.09 ? 78  LEU   A CD2 1 
ATOM   364  N  N   . SER   A 1 51  ? -3.134  -8.319  47.626  1.00 21.47 ? 79  SER   A N   1 
ATOM   365  C  CA  . SER   A 1 51  ? -2.704  -7.335  46.638  1.00 29.00 ? 79  SER   A CA  1 
ATOM   366  C  C   . SER   A 1 51  ? -1.206  -7.378  46.399  1.00 28.20 ? 79  SER   A C   1 
ATOM   367  O  O   . SER   A 1 51  ? -0.741  -6.843  45.388  1.00 29.45 ? 79  SER   A O   1 
ATOM   368  C  CB  . SER   A 1 51  ? -3.098  -5.919  47.061  1.00 22.77 ? 79  SER   A CB  1 
ATOM   369  O  OG  . SER   A 1 51  ? -2.215  -5.448  48.067  1.00 26.22 ? 79  SER   A OG  1 
ATOM   370  N  N   . THR   A 1 52  ? -0.440  -7.974  47.309  1.00 25.48 ? 80  THR   A N   1 
ATOM   371  C  CA  . THR   A 1 52  ? 0.983   -8.189  47.095  1.00 28.24 ? 80  THR   A CA  1 
ATOM   372  C  C   . THR   A 1 52  ? 1.302   -9.644  46.766  1.00 27.59 ? 80  THR   A C   1 
ATOM   373  O  O   . THR   A 1 52  ? 2.477   -10.010 46.681  1.00 30.55 ? 80  THR   A O   1 
ATOM   374  C  CB  . THR   A 1 52  ? 1.787   -7.730  48.313  1.00 28.02 ? 80  THR   A CB  1 
ATOM   375  O  OG1 . THR   A 1 52  ? 1.518   -8.589  49.435  1.00 23.90 ? 80  THR   A OG1 1 
ATOM   376  C  CG2 . THR   A 1 52  ? 1.446   -6.290  48.656  1.00 26.09 ? 80  THR   A CG2 1 
ATOM   377  N  N   . GLY   A 1 53  ? 0.293   -10.477 46.567  1.00 23.86 ? 81  GLY   A N   1 
ATOM   378  C  CA  . GLY   A 1 53  ? 0.531   -11.831 46.121  1.00 22.52 ? 81  GLY   A CA  1 
ATOM   379  C  C   . GLY   A 1 53  ? 0.638   -12.854 47.220  1.00 24.51 ? 81  GLY   A C   1 
ATOM   380  O  O   . GLY   A 1 53  ? 0.948   -14.015 46.935  1.00 19.59 ? 81  GLY   A O   1 
ATOM   381  N  N   . ASN   A 1 54  ? 0.414   -12.463 48.465  1.00 21.48 ? 82  ASN   A N   1 
ATOM   382  C  CA  . ASN   A 1 54  ? 0.307   -13.422 49.554  1.00 23.65 ? 82  ASN   A CA  1 
ATOM   383  C  C   . ASN   A 1 54  ? -1.103  -14.011 49.534  1.00 24.29 ? 82  ASN   A C   1 
ATOM   384  O  O   . ASN   A 1 54  ? -2.079  -13.305 49.816  1.00 19.55 ? 82  ASN   A O   1 
ATOM   385  C  CB  . ASN   A 1 54  ? 0.604   -12.740 50.883  1.00 19.21 ? 82  ASN   A CB  1 
ATOM   386  C  CG  . ASN   A 1 54  ? 0.588   -13.703 52.036  1.00 20.99 ? 82  ASN   A CG  1 
ATOM   387  O  OD1 . ASN   A 1 54  ? 0.018   -14.790 51.944  1.00 19.96 ? 82  ASN   A OD1 1 
ATOM   388  N  ND2 . ASN   A 1 54  ? 1.186   -13.299 53.152  1.00 20.04 ? 82  ASN   A ND2 1 
ATOM   389  N  N   . MET   A 1 55  ? -1.203  -15.296 49.188  1.00 20.15 ? 83  MET   A N   1 
ATOM   390  C  CA  . MET   A 1 55  ? -2.443  -16.066 49.185  1.00 20.45 ? 83  MET   A CA  1 
ATOM   391  C  C   . MET   A 1 55  ? -2.696  -16.782 50.499  1.00 24.83 ? 83  MET   A C   1 
ATOM   392  O  O   . MET   A 1 55  ? -3.715  -17.471 50.628  1.00 26.67 ? 83  MET   A O   1 
ATOM   393  C  CB  . MET   A 1 55  ? -2.413  -17.118 48.066  1.00 21.86 ? 83  MET   A CB  1 
ATOM   394  C  CG  . MET   A 1 55  ? -1.959  -16.610 46.716  1.00 24.15 ? 83  MET   A CG  1 
ATOM   395  S  SD  . MET   A 1 55  ? -3.205  -15.552 45.934  1.00 36.41 ? 83  MET   A SD  1 
ATOM   396  C  CE  . MET   A 1 55  ? -2.612  -13.924 46.355  1.00 27.14 ? 83  MET   A CE  1 
ATOM   397  N  N   . VAL   A 1 56  ? -1.797  -16.641 51.464  1.00 19.53 ? 84  VAL   A N   1 
ATOM   398  C  CA  . VAL   A 1 56  ? -1.815  -17.424 52.689  1.00 22.10 ? 84  VAL   A CA  1 
ATOM   399  C  C   . VAL   A 1 56  ? -2.353  -16.610 53.855  1.00 22.92 ? 84  VAL   A C   1 
ATOM   400  O  O   . VAL   A 1 56  ? -3.296  -17.026 54.527  1.00 22.14 ? 84  VAL   A O   1 
ATOM   401  C  CB  . VAL   A 1 56  ? -0.410  -17.986 53.005  1.00 18.84 ? 84  VAL   A CB  1 
ATOM   402  C  CG1 . VAL   A 1 56  ? -0.392  -18.599 54.384  1.00 17.95 ? 84  VAL   A CG1 1 
ATOM   403  C  CG2 . VAL   A 1 56  ? -0.016  -19.028 51.969  1.00 17.92 ? 84  VAL   A CG2 1 
ATOM   404  N  N   . HIS   A 1 57  ? -1.733  -15.466 54.145  1.00 18.64 ? 85  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 57  ? -2.147  -14.659 55.280  1.00 20.06 ? 85  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 57  ? -2.301  -13.203 54.866  1.00 20.26 ? 85  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 57  ? -1.798  -12.763 53.830  1.00 18.79 ? 85  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 57  ? -1.178  -14.783 56.472  1.00 21.70 ? 85  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 57  ? 0.256   -14.448 56.153  1.00 20.29 ? 85  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 57  ? 0.800   -13.203 56.391  1.00 14.44 ? 85  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 57  ? 1.268   -15.216 55.681  1.00 16.91 ? 85  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 57  ? 2.070   -13.204 56.034  1.00 17.30 ? 85  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 57  ? 2.380   -14.414 55.595  1.00 20.56 ? 85  HIS   A NE2 1 
ATOM   414  N  N   . ALA   A 1 58  ? -3.059  -12.478 55.672  1.00 16.30 ? 86  ALA   A N   1 
ATOM   415  C  CA  . ALA   A 1 58  ? -3.179  -11.037 55.558  1.00 12.94 ? 86  ALA   A CA  1 
ATOM   416  C  C   . ALA   A 1 58  ? -2.450  -10.416 56.732  1.00 15.50 ? 86  ALA   A C   1 
ATOM   417  O  O   . ALA   A 1 58  ? -2.769  -10.727 57.882  1.00 16.71 ? 86  ALA   A O   1 
ATOM   418  C  CB  . ALA   A 1 58  ? -4.649  -10.593 55.554  1.00 12.03 ? 86  ALA   A CB  1 
ATOM   419  N  N   . SER   A 1 59  ? -1.493  -9.527  56.444  1.00 12.25 ? 87  SER   A N   1 
ATOM   420  C  CA  . SER   A 1 59  ? -0.658  -8.924  57.470  1.00 12.69 ? 87  SER   A CA  1 
ATOM   421  C  C   . SER   A 1 59  ? -0.496  -7.447  57.181  1.00 16.60 ? 87  SER   A C   1 
ATOM   422  O  O   . SER   A 1 59  ? -0.071  -7.087  56.081  1.00 17.07 ? 87  SER   A O   1 
ATOM   423  C  CB  . SER   A 1 59  ? 0.736   -9.590  57.530  1.00 14.23 ? 87  SER   A CB  1 
ATOM   424  O  OG  . SER   A 1 59  ? 0.646   -10.885 58.069  1.00 16.27 ? 87  SER   A OG  1 
ATOM   425  N  N   . TYR   A 1 60  ? -0.785  -6.610  58.185  1.00 12.30 ? 88  TYR   A N   1 
ATOM   426  C  CA  . TYR   A 1 60  ? -0.729  -5.158  58.066  1.00 14.87 ? 88  TYR   A CA  1 
ATOM   427  C  C   . TYR   A 1 60  ? 0.110   -4.597  59.201  1.00 15.93 ? 88  TYR   A C   1 
ATOM   428  O  O   . TYR   A 1 60  ? -0.151  -4.892  60.373  1.00 17.46 ? 88  TYR   A O   1 
ATOM   429  C  CB  . TYR   A 1 60  ? -2.151  -4.543  58.074  1.00 12.34 ? 88  TYR   A CB  1 
ATOM   430  C  CG  . TYR   A 1 60  ? -2.965  -5.098  56.945  1.00 16.51 ? 88  TYR   A CG  1 
ATOM   431  C  CD1 . TYR   A 1 60  ? -2.695  -4.713  55.640  1.00 15.10 ? 88  TYR   A CD1 1 
ATOM   432  C  CD2 . TYR   A 1 60  ? -3.978  -6.044  57.161  1.00 15.18 ? 88  TYR   A CD2 1 
ATOM   433  C  CE1 . TYR   A 1 60  ? -3.403  -5.238  54.578  1.00 17.34 ? 88  TYR   A CE1 1 
ATOM   434  C  CE2 . TYR   A 1 60  ? -4.708  -6.580  56.083  1.00 12.39 ? 88  TYR   A CE2 1 
ATOM   435  C  CZ  . TYR   A 1 60  ? -4.396  -6.172  54.800  1.00 13.82 ? 88  TYR   A CZ  1 
ATOM   436  O  OH  . TYR   A 1 60  ? -5.063  -6.658  53.719  1.00 13.91 ? 88  TYR   A OH  1 
ATOM   437  N  N   . LEU   A 1 61  ? 1.103   -3.778  58.856  1.00 14.02 ? 89  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 61  ? 2.030   -3.225  59.836  1.00 14.99 ? 89  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 61  ? 1.675   -1.779  60.141  1.00 15.50 ? 89  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 61  ? 1.491   -0.980  59.224  1.00 16.76 ? 89  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 61  ? 3.467   -3.319  59.333  1.00 16.46 ? 89  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 61  ? 4.479   -2.936  60.388  1.00 19.60 ? 89  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 61  ? 4.601   -4.054  61.419  1.00 18.73 ? 89  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 61  ? 5.826   -2.640  59.721  1.00 22.44 ? 89  LEU   A CD2 1 
ATOM   445  N  N   . LEU   A 1 62  ? 1.548   -1.465  61.427  1.00 14.88 ? 90  LEU   A N   1 
ATOM   446  C  CA  . LEU   A 1 62  ? 1.371   -0.109  61.912  1.00 15.96 ? 90  LEU   A CA  1 
ATOM   447  C  C   . LEU   A 1 62  ? 2.662   0.327   62.585  1.00 19.64 ? 90  LEU   A C   1 
ATOM   448  O  O   . LEU   A 1 62  ? 3.341   -0.487  63.217  1.00 16.33 ? 90  LEU   A O   1 
ATOM   449  C  CB  . LEU   A 1 62  ? 0.220   -0.002  62.914  1.00 19.06 ? 90  LEU   A CB  1 
ATOM   450  C  CG  . LEU   A 1 62  ? -1.173  -0.544  62.543  1.00 18.33 ? 90  LEU   A CG  1 
ATOM   451  C  CD1 . LEU   A 1 62  ? -2.203  -0.146  63.591  1.00 17.40 ? 90  LEU   A CD1 1 
ATOM   452  C  CD2 . LEU   A 1 62  ? -1.593  -0.080  61.175  1.00 17.62 ? 90  LEU   A CD2 1 
ATOM   453  N  N   . THR   A 1 63  ? 2.987   1.618   62.471  1.00 18.02 ? 91  THR   A N   1 
ATOM   454  C  CA  . THR   A 1 63  ? 4.225   2.144   63.033  1.00 18.57 ? 91  THR   A CA  1 
ATOM   455  C  C   . THR   A 1 63  ? 3.970   3.450   63.754  1.00 19.15 ? 91  THR   A C   1 
ATOM   456  O  O   . THR   A 1 63  ? 3.231   4.316   63.269  1.00 19.81 ? 91  THR   A O   1 
ATOM   457  C  CB  . THR   A 1 63  ? 5.297   2.376   61.972  1.00 18.90 ? 91  THR   A CB  1 
ATOM   458  O  OG1 . THR   A 1 63  ? 4.744   3.119   60.875  1.00 23.38 ? 91  THR   A OG1 1 
ATOM   459  C  CG2 . THR   A 1 63  ? 5.846   1.052   61.457  1.00 13.05 ? 91  THR   A CG2 1 
ATOM   460  N  N   . SER   A 1 64  ? 4.603   3.589   64.912  1.00 19.88 ? 92  SER   A N   1 
ATOM   461  C  CA  . SER   A 1 64  ? 4.705   4.880   65.581  1.00 19.95 ? 92  SER   A CA  1 
ATOM   462  C  C   . SER   A 1 64  ? 6.080   4.956   66.229  1.00 17.23 ? 92  SER   A C   1 
ATOM   463  O  O   . SER   A 1 64  ? 6.377   4.178   67.138  1.00 20.26 ? 92  SER   A O   1 
ATOM   464  C  CB  . SER   A 1 64  ? 3.594   5.050   66.609  1.00 18.13 ? 92  SER   A CB  1 
ATOM   465  O  OG  . SER   A 1 64  ? 3.450   6.408   66.941  1.00 21.69 ? 92  SER   A OG  1 
ATOM   466  N  N   . GLY   A 1 65  ? 6.922   5.879   65.769  1.00 18.05 ? 93  GLY   A N   1 
ATOM   467  C  CA  . GLY   A 1 65  ? 8.296   5.881   66.254  1.00 22.77 ? 93  GLY   A CA  1 
ATOM   468  C  C   . GLY   A 1 65  ? 8.968   4.562   65.902  1.00 18.37 ? 93  GLY   A C   1 
ATOM   469  O  O   . GLY   A 1 65  ? 8.916   4.100   64.756  1.00 18.14 ? 93  GLY   A O   1 
ATOM   470  N  N   . ASP   A 1 66  ? 9.593   3.932   66.892  1.00 17.53 ? 94  ASP   A N   1 
ATOM   471  C  CA  . ASP   A 1 66  ? 10.207  2.626   66.684  1.00 18.33 ? 94  ASP   A CA  1 
ATOM   472  C  C   . ASP   A 1 66  ? 9.239   1.473   66.900  1.00 23.72 ? 94  ASP   A C   1 
ATOM   473  O  O   . ASP   A 1 66  ? 9.602   0.320   66.630  1.00 21.52 ? 94  ASP   A O   1 
ATOM   474  C  CB  . ASP   A 1 66  ? 11.406  2.445   67.619  1.00 22.83 ? 94  ASP   A CB  1 
ATOM   475  C  CG  . ASP   A 1 66  ? 12.582  3.270   67.197  1.00 31.17 ? 94  ASP   A CG  1 
ATOM   476  O  OD1 . ASP   A 1 66  ? 12.740  3.477   65.974  1.00 28.97 ? 94  ASP   A OD1 1 
ATOM   477  O  OD2 . ASP   A 1 66  ? 13.333  3.724   68.086  1.00 40.28 ? 94  ASP   A OD2 1 
ATOM   478  N  N   . LEU   A 1 67  ? 8.031   1.757   67.390  1.00 18.41 ? 95  LEU   A N   1 
ATOM   479  C  CA  . LEU   A 1 67  ? 7.063   0.715   67.689  1.00 20.50 ? 95  LEU   A CA  1 
ATOM   480  C  C   . LEU   A 1 67  ? 6.444   0.186   66.398  1.00 22.73 ? 95  LEU   A C   1 
ATOM   481  O  O   . LEU   A 1 67  ? 5.938   0.955   65.571  1.00 20.68 ? 95  LEU   A O   1 
ATOM   482  C  CB  . LEU   A 1 67  ? 5.987   1.256   68.624  1.00 12.26 ? 95  LEU   A CB  1 
ATOM   483  C  CG  . LEU   A 1 67  ? 4.891   0.283   69.039  1.00 17.31 ? 95  LEU   A CG  1 
ATOM   484  C  CD1 . LEU   A 1 67  ? 5.388   -0.729  70.050  1.00 11.47 ? 95  LEU   A CD1 1 
ATOM   485  C  CD2 . LEU   A 1 67  ? 3.721   1.056   69.596  1.00 11.32 ? 95  LEU   A CD2 1 
ATOM   486  N  N   . ARG   A 1 68  ? 6.495   -1.127  66.225  1.00 19.05 ? 96  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 68  ? 5.887   -1.802  65.087  1.00 20.28 ? 96  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 68  ? 4.854   -2.791  65.615  1.00 16.72 ? 96  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 68  ? 5.213   -3.718  66.345  1.00 16.37 ? 96  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 68  ? 6.944   -2.526  64.253  1.00 19.14 ? 96  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 68  ? 8.042   -1.648  63.716  1.00 19.75 ? 96  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 68  ? 9.079   -2.497  63.005  1.00 27.36 ? 96  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 68  ? 10.298  -1.768  62.659  1.00 25.56 ? 96  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 68  ? 11.359  -1.650  63.446  1.00 29.61 ? 96  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 68  ? 11.379  -2.214  64.648  1.00 24.21 ? 96  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 68  ? 12.411  -0.968  63.020  1.00 31.97 ? 96  ARG   A NH2 1 
ATOM   497  N  N   . PHE   A 1 69  ? 3.579   -2.558  65.295  1.00 17.62 ? 97  PHE   A N   1 
ATOM   498  C  CA  . PHE   A 1 69  ? 2.500   -3.522  65.542  1.00 17.60 ? 97  PHE   A CA  1 
ATOM   499  C  C   . PHE   A 1 69  ? 2.113   -4.197  64.237  1.00 16.27 ? 97  PHE   A C   1 
ATOM   500  O  O   . PHE   A 1 69  ? 1.684   -3.526  63.294  1.00 19.80 ? 97  PHE   A O   1 
ATOM   501  C  CB  . PHE   A 1 69  ? 1.261   -2.866  66.155  1.00 13.86 ? 97  PHE   A CB  1 
ATOM   502  C  CG  . PHE   A 1 69  ? 1.336   -2.690  67.660  1.00 16.76 ? 97  PHE   A CG  1 
ATOM   503  C  CD1 . PHE   A 1 69  ? 2.479   -3.064  68.368  1.00 18.41 ? 97  PHE   A CD1 1 
ATOM   504  C  CD2 . PHE   A 1 69  ? 0.273   -2.140  68.362  1.00 16.67 ? 97  PHE   A CD2 1 
ATOM   505  C  CE1 . PHE   A 1 69  ? 2.553   -2.895  69.750  1.00 15.67 ? 97  PHE   A CE1 1 
ATOM   506  C  CE2 . PHE   A 1 69  ? 0.334   -1.964  69.737  1.00 15.38 ? 97  PHE   A CE2 1 
ATOM   507  C  CZ  . PHE   A 1 69  ? 1.469   -2.350  70.437  1.00 18.50 ? 97  PHE   A CZ  1 
ATOM   508  N  N   . LEU   A 1 70  ? 2.233   -5.522  64.192  1.00 18.26 ? 98  LEU   A N   1 
ATOM   509  C  CA  . LEU   A 1 70  ? 1.868   -6.322  63.028  1.00 17.12 ? 98  LEU   A CA  1 
ATOM   510  C  C   . LEU   A 1 70  ? 0.586   -7.095  63.319  1.00 13.86 ? 98  LEU   A C   1 
ATOM   511  O  O   . LEU   A 1 70  ? 0.473   -7.744  64.363  1.00 17.96 ? 98  LEU   A O   1 
ATOM   512  C  CB  . LEU   A 1 70  ? 2.988   -7.303  62.665  1.00 17.05 ? 98  LEU   A CB  1 
ATOM   513  C  CG  . LEU   A 1 70  ? 2.802   -8.140  61.402  1.00 14.37 ? 98  LEU   A CG  1 
ATOM   514  C  CD1 . LEU   A 1 70  ? 2.906   -7.289  60.148  1.00 15.74 ? 98  LEU   A CD1 1 
ATOM   515  C  CD2 . LEU   A 1 70  ? 3.817   -9.291  61.343  1.00 14.30 ? 98  LEU   A CD2 1 
ATOM   516  N  N   . PHE   A 1 71  ? -0.359  -7.056  62.386  1.00 14.65 ? 99  PHE   A N   1 
ATOM   517  C  CA  . PHE   A 1 71  ? -1.673  -7.684  62.551  1.00 15.30 ? 99  PHE   A CA  1 
ATOM   518  C  C   . PHE   A 1 71  ? -1.844  -8.698  61.438  1.00 13.07 ? 99  PHE   A C   1 
ATOM   519  O  O   . PHE   A 1 71  ? -1.787  -8.334  60.263  1.00 19.04 ? 99  PHE   A O   1 
ATOM   520  C  CB  . PHE   A 1 71  ? -2.801  -6.638  62.524  1.00 13.72 ? 99  PHE   A CB  1 
ATOM   521  C  CG  . PHE   A 1 71  ? -2.676  -5.622  63.608  1.00 15.42 ? 99  PHE   A CG  1 
ATOM   522  C  CD1 . PHE   A 1 71  ? -1.869  -4.499  63.435  1.00 18.89 ? 99  PHE   A CD1 1 
ATOM   523  C  CD2 . PHE   A 1 71  ? -3.271  -5.830  64.835  1.00 11.57 ? 99  PHE   A CD2 1 
ATOM   524  C  CE1 . PHE   A 1 71  ? -1.705  -3.584  64.443  1.00 12.29 ? 99  PHE   A CE1 1 
ATOM   525  C  CE2 . PHE   A 1 71  ? -3.105  -4.929  65.853  1.00 14.38 ? 99  PHE   A CE2 1 
ATOM   526  C  CZ  . PHE   A 1 71  ? -2.321  -3.782  65.645  1.00 14.81 ? 99  PHE   A CZ  1 
ATOM   527  N  N   . THR   A 1 72  ? -2.056  -9.962  61.802  1.00 16.27 ? 100 THR   A N   1 
ATOM   528  C  CA  . THR   A 1 72  ? -2.086  -11.057 60.840  1.00 15.99 ? 100 THR   A CA  1 
ATOM   529  C  C   . THR   A 1 72  ? -3.309  -11.950 61.046  1.00 12.35 ? 100 THR   A C   1 
ATOM   530  O  O   . THR   A 1 72  ? -3.728  -12.209 62.177  1.00 14.50 ? 100 THR   A O   1 
ATOM   531  C  CB  . THR   A 1 72  ? -0.792  -11.910 60.933  1.00 17.76 ? 100 THR   A CB  1 
ATOM   532  O  OG1 . THR   A 1 72  ? 0.347   -11.106 60.584  1.00 17.31 ? 100 THR   A OG1 1 
ATOM   533  C  CG2 . THR   A 1 72  ? -0.866  -13.117 59.999  1.00 16.23 ? 100 THR   A CG2 1 
ATOM   534  N  N   . ALA   A 1 73  ? -3.857  -12.440 59.943  1.00 14.00 ? 101 ALA   A N   1 
ATOM   535  C  CA  . ALA   A 1 73  ? -4.994  -13.341 59.960  1.00 14.22 ? 101 ALA   A CA  1 
ATOM   536  C  C   . ALA   A 1 73  ? -4.846  -14.271 58.773  1.00 16.75 ? 101 ALA   A C   1 
ATOM   537  O  O   . ALA   A 1 73  ? -4.275  -13.869 57.752  1.00 18.31 ? 101 ALA   A O   1 
ATOM   538  C  CB  . ALA   A 1 73  ? -6.327  -12.571 59.876  1.00 11.01 ? 101 ALA   A CB  1 
ATOM   539  N  N   . PRO   A 1 74  ? -5.374  -15.496 58.853  1.00 15.66 ? 102 PRO   A N   1 
ATOM   540  C  CA  . PRO   A 1 74  ? -5.308  -16.400 57.702  1.00 18.58 ? 102 PRO   A CA  1 
ATOM   541  C  C   . PRO   A 1 74  ? -6.449  -16.162 56.729  1.00 17.19 ? 102 PRO   A C   1 
ATOM   542  O  O   . PRO   A 1 74  ? -7.580  -15.886 57.124  1.00 20.75 ? 102 PRO   A O   1 
ATOM   543  C  CB  . PRO   A 1 74  ? -5.411  -17.793 58.345  1.00 16.36 ? 102 PRO   A CB  1 
ATOM   544  C  CG  . PRO   A 1 74  ? -6.246  -17.582 59.545  1.00 17.35 ? 102 PRO   A CG  1 
ATOM   545  C  CD  . PRO   A 1 74  ? -5.963  -16.157 60.036  1.00 16.03 ? 102 PRO   A CD  1 
ATOM   546  N  N   . TYR   A 1 75  ? -6.120  -16.236 55.441  1.00 21.07 ? 103 TYR   A N   1 
ATOM   547  C  CA  . TYR   A 1 75  ? -7.105  -16.403 54.387  1.00 19.31 ? 103 TYR   A CA  1 
ATOM   548  C  C   . TYR   A 1 75  ? -7.668  -17.822 54.413  1.00 19.42 ? 103 TYR   A C   1 
ATOM   549  O  O   . TYR   A 1 75  ? -7.337  -18.639 55.273  1.00 22.73 ? 103 TYR   A O   1 
ATOM   550  C  CB  . TYR   A 1 75  ? -6.486  -16.128 53.024  1.00 18.21 ? 103 TYR   A CB  1 
ATOM   551  C  CG  . TYR   A 1 75  ? -6.143  -14.687 52.756  1.00 17.46 ? 103 TYR   A CG  1 
ATOM   552  C  CD1 . TYR   A 1 75  ? -7.084  -13.675 52.933  1.00 18.44 ? 103 TYR   A CD1 1 
ATOM   553  C  CD2 . TYR   A 1 75  ? -4.874  -14.338 52.327  1.00 17.26 ? 103 TYR   A CD2 1 
ATOM   554  C  CE1 . TYR   A 1 75  ? -6.775  -12.368 52.672  1.00 16.35 ? 103 TYR   A CE1 1 
ATOM   555  C  CE2 . TYR   A 1 75  ? -4.538  -13.044 52.094  1.00 20.26 ? 103 TYR   A CE2 1 
ATOM   556  C  CZ  . TYR   A 1 75  ? -5.495  -12.051 52.263  1.00 21.11 ? 103 TYR   A CZ  1 
ATOM   557  O  OH  . TYR   A 1 75  ? -5.136  -10.757 52.015  1.00 18.20 ? 103 TYR   A OH  1 
ATOM   558  N  N   . SER   A 1 76  ? -8.521  -18.126 53.440  1.00 22.20 ? 104 SER   A N   1 
ATOM   559  C  CA  . SER   A 1 76  ? -9.031  -19.489 53.304  1.00 24.37 ? 104 SER   A CA  1 
ATOM   560  C  C   . SER   A 1 76  ? -7.933  -20.400 52.761  1.00 24.00 ? 104 SER   A C   1 
ATOM   561  O  O   . SER   A 1 76  ? -7.280  -20.051 51.770  1.00 23.06 ? 104 SER   A O   1 
ATOM   562  C  CB  . SER   A 1 76  ? -10.247 -19.518 52.379  1.00 23.24 ? 104 SER   A CB  1 
ATOM   563  O  OG  . SER   A 1 76  ? -10.576 -20.840 52.000  1.00 20.10 ? 104 SER   A OG  1 
ATOM   564  N  N   . PRO   A 1 77  ? -7.713  -21.580 53.354  1.00 24.14 ? 105 PRO   A N   1 
ATOM   565  C  CA  . PRO   A 1 77  ? -6.672  -22.463 52.811  1.00 23.31 ? 105 PRO   A CA  1 
ATOM   566  C  C   . PRO   A 1 77  ? -6.874  -22.773 51.347  1.00 26.20 ? 105 PRO   A C   1 
ATOM   567  O  O   . PRO   A 1 77  ? -5.888  -22.963 50.627  1.00 27.02 ? 105 PRO   A O   1 
ATOM   568  C  CB  . PRO   A 1 77  ? -6.782  -23.709 53.689  1.00 21.34 ? 105 PRO   A CB  1 
ATOM   569  C  CG  . PRO   A 1 77  ? -7.221  -23.165 55.004  1.00 28.62 ? 105 PRO   A CG  1 
ATOM   570  C  CD  . PRO   A 1 77  ? -8.204  -22.058 54.659  1.00 21.93 ? 105 PRO   A CD  1 
ATOM   571  N  N   . SER   A 1 78  ? -8.120  -22.758 50.865  1.00 24.17 ? 106 SER   A N   1 
ATOM   572  C  CA  . SER   A 1 78  ? -8.385  -23.042 49.460  1.00 23.16 ? 106 SER   A CA  1 
ATOM   573  C  C   . SER   A 1 78  ? -7.629  -22.108 48.532  1.00 27.26 ? 106 SER   A C   1 
ATOM   574  O  O   . SER   A 1 78  ? -7.497  -22.414 47.343  1.00 31.28 ? 106 SER   A O   1 
ATOM   575  C  CB  . SER   A 1 78  ? -9.896  -22.962 49.168  1.00 27.18 ? 106 SER   A CB  1 
ATOM   576  O  OG  . SER   A 1 78  ? -10.391 -21.630 49.274  1.00 24.74 ? 106 SER   A OG  1 
ATOM   577  N  N   . LEU   A 1 79  ? -7.126  -20.980 49.031  1.00 25.68 ? 107 LEU   A N   1 
ATOM   578  C  CA  . LEU   A 1 79  ? -6.350  -20.107 48.165  1.00 26.95 ? 107 LEU   A CA  1 
ATOM   579  C  C   . LEU   A 1 79  ? -4.920  -20.592 47.991  1.00 25.28 ? 107 LEU   A C   1 
ATOM   580  O  O   . LEU   A 1 79  ? -4.278  -20.228 47.005  1.00 24.61 ? 107 LEU   A O   1 
ATOM   581  C  CB  . LEU   A 1 79  ? -6.357  -18.671 48.692  1.00 26.94 ? 107 LEU   A CB  1 
ATOM   582  C  CG  . LEU   A 1 79  ? -7.714  -18.045 49.035  1.00 24.21 ? 107 LEU   A CG  1 
ATOM   583  C  CD1 . LEU   A 1 79  ? -7.554  -16.552 49.349  1.00 24.34 ? 107 LEU   A CD1 1 
ATOM   584  C  CD2 . LEU   A 1 79  ? -8.778  -18.300 47.941  1.00 19.38 ? 107 LEU   A CD2 1 
ATOM   585  N  N   . SER   A 1 80  ? -4.420  -21.430 48.896  1.00 27.40 ? 108 SER   A N   1 
ATOM   586  C  CA  . SER   A 1 80  ? -3.021  -21.847 48.862  1.00 28.97 ? 108 SER   A CA  1 
ATOM   587  C  C   . SER   A 1 80  ? -2.872  -23.350 49.042  1.00 28.11 ? 108 SER   A C   1 
ATOM   588  O  O   . SER   A 1 80  ? -1.776  -23.826 49.346  1.00 29.36 ? 108 SER   A O   1 
ATOM   589  C  CB  . SER   A 1 80  ? -2.203  -21.095 49.924  1.00 22.16 ? 108 SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 80  ? -2.667  -21.388 51.232  1.00 23.61 ? 108 SER   A OG  1 
ATOM   591  N  N   . ALA   A 1 81  ? -3.947  -24.106 48.843  1.00 28.63 ? 109 ALA   A N   1 
ATOM   592  C  CA  . ALA   A 1 81  ? -3.863  -25.550 49.032  1.00 35.26 ? 109 ALA   A CA  1 
ATOM   593  C  C   . ALA   A 1 81  ? -2.888  -26.189 48.055  1.00 30.86 ? 109 ALA   A C   1 
ATOM   594  O  O   . ALA   A 1 81  ? -2.346  -27.260 48.337  1.00 32.99 ? 109 ALA   A O   1 
ATOM   595  C  CB  . ALA   A 1 81  ? -5.248  -26.200 48.890  1.00 30.70 ? 109 ALA   A CB  1 
ATOM   596  N  N   . GLY   A 1 82  ? -2.639  -25.546 46.912  1.00 31.30 ? 110 GLY   A N   1 
ATOM   597  C  CA  . GLY   A 1 82  ? -1.682  -26.090 45.970  1.00 26.72 ? 110 GLY   A CA  1 
ATOM   598  C  C   . GLY   A 1 82  ? -0.239  -25.877 46.372  1.00 28.66 ? 110 GLY   A C   1 
ATOM   599  O  O   . GLY   A 1 82  ? 0.637   -26.659 45.988  1.00 25.25 ? 110 GLY   A O   1 
ATOM   600  N  N   . GLU   A 1 83  ? 0.040   -24.831 47.138  1.00 28.35 ? 111 GLU   A N   1 
ATOM   601  C  CA  . GLU   A 1 83  ? 1.423   -24.533 47.473  1.00 22.51 ? 111 GLU   A CA  1 
ATOM   602  C  C   . GLU   A 1 83  ? 1.986   -25.561 48.458  1.00 22.48 ? 111 GLU   A C   1 
ATOM   603  O  O   . GLU   A 1 83  ? 1.262   -26.244 49.172  1.00 19.22 ? 111 GLU   A O   1 
ATOM   604  C  CB  . GLU   A 1 83  ? 1.535   -23.130 48.068  1.00 21.29 ? 111 GLU   A CB  1 
ATOM   605  C  CG  . GLU   A 1 83  ? 0.910   -21.999 47.220  1.00 20.43 ? 111 GLU   A CG  1 
ATOM   606  C  CD  . GLU   A 1 83  ? 0.879   -20.689 47.982  1.00 23.02 ? 111 GLU   A CD  1 
ATOM   607  O  OE1 . GLU   A 1 83  ? 1.332   -20.706 49.147  1.00 22.16 ? 111 GLU   A OE1 1 
ATOM   608  O  OE2 . GLU   A 1 83  ? 0.387   -19.658 47.443  1.00 20.77 ? 111 GLU   A OE2 1 
ATOM   609  N  N   . ILE   A 1 84  ? 3.312   -25.645 48.502  1.00 24.25 ? 112 ILE   A N   1 
ATOM   610  C  CA  . ILE   A 1 84  ? 4.021   -26.309 49.584  1.00 25.96 ? 112 ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 84  ? 5.003   -25.297 50.150  1.00 23.19 ? 112 ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 84  ? 5.258   -24.253 49.549  1.00 21.96 ? 112 ILE   A O   1 
ATOM   613  C  CB  . ILE   A 1 84  ? 4.744   -27.584 49.118  1.00 22.48 ? 112 ILE   A CB  1 
ATOM   614  C  CG1 . ILE   A 1 84  ? 5.687   -27.242 47.964  1.00 26.51 ? 112 ILE   A CG1 1 
ATOM   615  C  CG2 . ILE   A 1 84  ? 3.719   -28.645 48.699  1.00 26.06 ? 112 ILE   A CG2 1 
ATOM   616  C  CD1 . ILE   A 1 84  ? 6.746   -28.285 47.679  1.00 28.89 ? 112 ILE   A CD1 1 
ATOM   617  N  N   . LYS   A 1 85  ? 5.552   -25.606 51.321  1.00 22.35 ? 113 LYS   A N   1 
ATOM   618  C  CA  . LYS   A 1 85  ? 6.473   -24.665 51.956  1.00 22.35 ? 113 LYS   A CA  1 
ATOM   619  C  C   . LYS   A 1 85  ? 7.555   -24.150 51.008  1.00 25.30 ? 113 LYS   A C   1 
ATOM   620  O  O   . LYS   A 1 85  ? 7.750   -22.925 50.944  1.00 17.56 ? 113 LYS   A O   1 
ATOM   621  C  CB  . LYS   A 1 85  ? 7.064   -25.298 53.222  1.00 20.25 ? 113 LYS   A CB  1 
ATOM   622  C  CG  . LYS   A 1 85  ? 6.144   -25.202 54.408  1.00 23.68 ? 113 LYS   A CG  1 
ATOM   623  C  CD  . LYS   A 1 85  ? 6.784   -25.734 55.687  1.00 28.71 ? 113 LYS   A CD  1 
ATOM   624  C  CE  . LYS   A 1 85  ? 5.812   -25.643 56.867  1.00 28.67 ? 113 LYS   A CE  1 
ATOM   625  N  NZ  . LYS   A 1 85  ? 6.426   -25.106 58.121  1.00 33.48 ? 113 LYS   A NZ  1 
ATOM   626  N  N   . PRO   A 1 86  ? 8.236   -24.985 50.216  1.00 25.85 ? 114 PRO   A N   1 
ATOM   627  C  CA  . PRO   A 1 86  ? 9.151   -24.438 49.198  1.00 26.86 ? 114 PRO   A CA  1 
ATOM   628  C  C   . PRO   A 1 86  ? 8.537   -23.422 48.233  1.00 28.24 ? 114 PRO   A C   1 
ATOM   629  O  O   . PRO   A 1 86  ? 9.275   -22.587 47.699  1.00 28.74 ? 114 PRO   A O   1 
ATOM   630  C  CB  . PRO   A 1 86  ? 9.604   -25.697 48.448  1.00 28.64 ? 114 PRO   A CB  1 
ATOM   631  C  CG  . PRO   A 1 86  ? 9.544   -26.769 49.474  1.00 29.56 ? 114 PRO   A CG  1 
ATOM   632  C  CD  . PRO   A 1 86  ? 8.353   -26.454 50.319  1.00 24.76 ? 114 PRO   A CD  1 
ATOM   633  N  N   . THR   A 1 87  ? 7.233   -23.487 47.949  1.00 29.37 ? 115 THR   A N   1 
ATOM   634  C  CA  . THR   A 1 87  ? 6.607   -22.616 46.955  1.00 24.41 ? 115 THR   A CA  1 
ATOM   635  C  C   . THR   A 1 87  ? 5.693   -21.573 47.576  1.00 22.27 ? 115 THR   A C   1 
ATOM   636  O  O   . THR   A 1 87  ? 5.027   -20.842 46.843  1.00 25.36 ? 115 THR   A O   1 
ATOM   637  C  CB  . THR   A 1 87  ? 5.809   -23.426 45.916  1.00 26.35 ? 115 THR   A CB  1 
ATOM   638  O  OG1 . THR   A 1 87  ? 4.885   -24.322 46.561  1.00 27.58 ? 115 THR   A OG1 1 
ATOM   639  C  CG2 . THR   A 1 87  ? 6.732   -24.226 44.997  1.00 30.92 ? 115 THR   A CG2 1 
ATOM   640  N  N   . THR   A 1 88  ? 5.687   -21.453 48.900  1.00 24.96 ? 116 THR   A N   1 
ATOM   641  C  CA  . THR   A 1 88  ? 4.671   -20.680 49.598  1.00 21.93 ? 116 THR   A CA  1 
ATOM   642  C  C   . THR   A 1 88  ? 4.642   -19.228 49.112  1.00 20.58 ? 116 THR   A C   1 
ATOM   643  O  O   . THR   A 1 88  ? 5.663   -18.660 48.738  1.00 16.78 ? 116 THR   A O   1 
ATOM   644  C  CB  . THR   A 1 88  ? 4.925   -20.743 51.111  1.00 17.66 ? 116 THR   A CB  1 
ATOM   645  O  OG1 . THR   A 1 88  ? 3.827   -20.138 51.799  1.00 21.74 ? 116 THR   A OG1 1 
ATOM   646  C  CG2 . THR   A 1 88  ? 6.207   -20.013 51.494  1.00 18.26 ? 116 THR   A CG2 1 
ATOM   647  N  N   . THR   A 1 89  ? 3.444   -18.631 49.074  1.00 18.34 ? 117 THR   A N   1 
ATOM   648  C  CA  . THR   A 1 89  ? 3.367   -17.183 48.904  1.00 19.92 ? 117 THR   A CA  1 
ATOM   649  C  C   . THR   A 1 89  ? 3.304   -16.439 50.231  1.00 20.49 ? 117 THR   A C   1 
ATOM   650  O  O   . THR   A 1 89  ? 3.139   -15.212 50.231  1.00 26.17 ? 117 THR   A O   1 
ATOM   651  C  CB  . THR   A 1 89  ? 2.155   -16.776 48.069  1.00 21.32 ? 117 THR   A CB  1 
ATOM   652  O  OG1 . THR   A 1 89  ? 0.975   -17.329 48.655  1.00 19.68 ? 117 THR   A OG1 1 
ATOM   653  C  CG2 . THR   A 1 89  ? 2.294   -17.248 46.634  1.00 21.74 ? 117 THR   A CG2 1 
ATOM   654  N  N   . ALA   A 1 90  ? 3.407   -17.140 51.357  1.00 19.11 ? 118 ALA   A N   1 
ATOM   655  C  CA  . ALA   A 1 90  ? 3.432   -16.449 52.635  1.00 19.71 ? 118 ALA   A CA  1 
ATOM   656  C  C   . ALA   A 1 90  ? 4.703   -15.614 52.760  1.00 21.35 ? 118 ALA   A C   1 
ATOM   657  O  O   . ALA   A 1 90  ? 5.802   -16.058 52.406  1.00 17.21 ? 118 ALA   A O   1 
ATOM   658  C  CB  . ALA   A 1 90  ? 3.349   -17.452 53.780  1.00 19.11 ? 118 ALA   A CB  1 
ATOM   659  N  N   . SER   A 1 91  ? 4.553   -14.393 53.273  1.00 23.72 ? 119 SER   A N   1 
ATOM   660  C  CA  . SER   A 1 91  ? 5.726   -13.565 53.546  1.00 22.74 ? 119 SER   A CA  1 
ATOM   661  C  C   . SER   A 1 91  ? 6.381   -13.900 54.876  1.00 18.90 ? 119 SER   A C   1 
ATOM   662  O  O   . SER   A 1 91  ? 7.561   -13.589 55.076  1.00 22.53 ? 119 SER   A O   1 
ATOM   663  C  CB  . SER   A 1 91  ? 5.340   -12.086 53.524  1.00 21.09 ? 119 SER   A CB  1 
ATOM   664  O  OG  . SER   A 1 91  ? 4.339   -11.819 54.492  1.00 22.76 ? 119 SER   A OG  1 
ATOM   665  N  N   . ILE   A 1 92  ? 5.649   -14.520 55.791  1.00 23.68 ? 120 ILE   A N   1 
ATOM   666  C  CA  . ILE   A 1 92  ? 6.166   -14.911 57.097  1.00 20.23 ? 120 ILE   A CA  1 
ATOM   667  C  C   . ILE   A 1 92  ? 6.183   -16.436 57.143  1.00 23.92 ? 120 ILE   A C   1 
ATOM   668  O  O   . ILE   A 1 92  ? 5.112   -17.064 57.231  1.00 23.79 ? 120 ILE   A O   1 
ATOM   669  C  CB  . ILE   A 1 92  ? 5.322   -14.319 58.234  1.00 16.91 ? 120 ILE   A CB  1 
ATOM   670  C  CG1 . ILE   A 1 92  ? 5.254   -12.791 58.088  1.00 20.30 ? 120 ILE   A CG1 1 
ATOM   671  C  CG2 . ILE   A 1 92  ? 5.939   -14.659 59.573  1.00 17.66 ? 120 ILE   A CG2 1 
ATOM   672  C  CD1 . ILE   A 1 92  ? 4.558   -12.100 59.233  1.00 9.88  ? 120 ILE   A CD1 1 
ATOM   673  N  N   . PRO   A 1 93  ? 7.361   -17.075 57.077  1.00 25.92 ? 121 PRO   A N   1 
ATOM   674  C  CA  . PRO   A 1 93  ? 7.402   -18.543 56.899  1.00 20.57 ? 121 PRO   A CA  1 
ATOM   675  C  C   . PRO   A 1 93  ? 6.895   -19.327 58.090  1.00 21.59 ? 121 PRO   A C   1 
ATOM   676  O  O   . PRO   A 1 93  ? 6.448   -20.465 57.913  1.00 26.06 ? 121 PRO   A O   1 
ATOM   677  C  CB  . PRO   A 1 93  ? 8.898   -18.829 56.640  1.00 27.29 ? 121 PRO   A CB  1 
ATOM   678  C  CG  . PRO   A 1 93  ? 9.619   -17.669 57.256  1.00 27.40 ? 121 PRO   A CG  1 
ATOM   679  C  CD  . PRO   A 1 93  ? 8.705   -16.474 57.038  1.00 26.96 ? 121 PRO   A CD  1 
ATOM   680  N  N   . SER   A 1 94  ? 6.932   -18.769 59.295  1.00 17.63 ? 122 SER   A N   1 
ATOM   681  C  CA  . SER   A 1 94  ? 6.387   -19.499 60.426  1.00 21.57 ? 122 SER   A CA  1 
ATOM   682  C  C   . SER   A 1 94  ? 4.864   -19.577 60.414  1.00 22.20 ? 122 SER   A C   1 
ATOM   683  O  O   . SER   A 1 94  ? 4.303   -20.321 61.222  1.00 22.27 ? 122 SER   A O   1 
ATOM   684  C  CB  . SER   A 1 94  ? 6.845   -18.853 61.723  1.00 21.65 ? 122 SER   A CB  1 
ATOM   685  O  OG  . SER   A 1 94  ? 6.485   -17.486 61.735  1.00 20.98 ? 122 SER   A OG  1 
ATOM   686  N  N   . PHE   A 1 95  ? 4.191   -18.828 59.545  1.00 22.08 ? 123 PHE   A N   1 
ATOM   687  C  CA  . PHE   A 1 95  ? 2.734   -18.797 59.571  1.00 25.81 ? 123 PHE   A CA  1 
ATOM   688  C  C   . PHE   A 1 95  ? 2.146   -20.161 59.238  1.00 18.39 ? 123 PHE   A C   1 
ATOM   689  O  O   . PHE   A 1 95  ? 2.657   -20.905 58.407  1.00 24.15 ? 123 PHE   A O   1 
ATOM   690  C  CB  . PHE   A 1 95  ? 2.166   -17.763 58.588  1.00 18.64 ? 123 PHE   A CB  1 
ATOM   691  C  CG  . PHE   A 1 95  ? 0.687   -17.630 58.688  1.00 18.42 ? 123 PHE   A CG  1 
ATOM   692  C  CD1 . PHE   A 1 95  ? 0.123   -16.789 59.628  1.00 19.41 ? 123 PHE   A CD1 1 
ATOM   693  C  CD2 . PHE   A 1 95  ? -0.145  -18.402 57.898  1.00 22.43 ? 123 PHE   A CD2 1 
ATOM   694  C  CE1 . PHE   A 1 95  ? -1.244  -16.694 59.750  1.00 18.83 ? 123 PHE   A CE1 1 
ATOM   695  C  CE2 . PHE   A 1 95  ? -1.512  -18.311 58.011  1.00 23.76 ? 123 PHE   A CE2 1 
ATOM   696  C  CZ  . PHE   A 1 95  ? -2.062  -17.451 58.937  1.00 17.84 ? 123 PHE   A CZ  1 
ATOM   697  N  N   . ASP   A 1 96  ? 1.036   -20.470 59.878  1.00 24.53 ? 124 ASP   A N   1 
ATOM   698  C  CA  . ASP   A 1 96  ? 0.355   -21.731 59.624  1.00 22.64 ? 124 ASP   A CA  1 
ATOM   699  C  C   . ASP   A 1 96  ? -1.133  -21.522 59.855  1.00 21.11 ? 124 ASP   A C   1 
ATOM   700  O  O   . ASP   A 1 96  ? -1.511  -21.087 60.948  1.00 20.50 ? 124 ASP   A O   1 
ATOM   701  C  CB  . ASP   A 1 96  ? 0.908   -22.820 60.544  1.00 26.62 ? 124 ASP   A CB  1 
ATOM   702  C  CG  . ASP   A 1 96  ? 0.199   -24.117 60.365  1.00 25.05 ? 124 ASP   A CG  1 
ATOM   703  O  OD1 . ASP   A 1 96  ? 0.456   -24.768 59.328  1.00 29.67 ? 124 ASP   A OD1 1 
ATOM   704  O  OD2 . ASP   A 1 96  ? -0.628  -24.470 61.239  1.00 23.60 ? 124 ASP   A OD2 1 
ATOM   705  N  N   . HIS   A 1 97  ? -1.969  -21.817 58.841  1.00 22.90 ? 125 HIS   A N   1 
ATOM   706  C  CA  . HIS   A 1 97  ? -3.418  -21.610 58.986  1.00 24.23 ? 125 HIS   A CA  1 
ATOM   707  C  C   . HIS   A 1 97  ? -3.930  -22.268 60.251  1.00 22.90 ? 125 HIS   A C   1 
ATOM   708  O  O   . HIS   A 1 97  ? -4.632  -21.641 61.054  1.00 25.08 ? 125 HIS   A O   1 
ATOM   709  C  CB  . HIS   A 1 97  ? -4.216  -22.164 57.797  1.00 19.97 ? 125 HIS   A CB  1 
ATOM   710  C  CG  . HIS   A 1 97  ? -3.972  -21.475 56.485  1.00 27.14 ? 125 HIS   A CG  1 
ATOM   711  N  ND1 . HIS   A 1 97  ? -3.090  -21.966 55.545  1.00 27.67 ? 125 HIS   A ND1 1 
ATOM   712  C  CD2 . HIS   A 1 97  ? -4.534  -20.371 55.930  1.00 23.35 ? 125 HIS   A CD2 1 
ATOM   713  C  CE1 . HIS   A 1 97  ? -3.111  -21.192 54.475  1.00 25.23 ? 125 HIS   A CE1 1 
ATOM   714  N  NE2 . HIS   A 1 97  ? -3.986  -20.222 54.679  1.00 23.35 ? 125 HIS   A NE2 1 
ATOM   715  N  N   . GLY   A 1 98  ? -3.548  -23.527 60.460  1.00 22.16 ? 126 GLY   A N   1 
ATOM   716  C  CA  . GLY   A 1 98  ? -4.086  -24.280 61.577  1.00 19.42 ? 126 GLY   A CA  1 
ATOM   717  C  C   . GLY   A 1 98  ? -3.646  -23.731 62.911  1.00 17.88 ? 126 GLY   A C   1 
ATOM   718  O  O   . GLY   A 1 98  ? -4.452  -23.615 63.840  1.00 18.68 ? 126 GLY   A O   1 
ATOM   719  N  N   . SER   A 1 99  ? -2.366  -23.355 63.012  1.00 22.61 ? 127 SER   A N   1 
ATOM   720  C  CA  . SER   A 1 99  ? -1.847  -22.742 64.226  1.00 18.28 ? 127 SER   A CA  1 
ATOM   721  C  C   . SER   A 1 99  ? -2.528  -21.409 64.509  1.00 17.18 ? 127 SER   A C   1 
ATOM   722  O  O   . SER   A 1 99  ? -2.897  -21.117 65.651  1.00 18.71 ? 127 SER   A O   1 
ATOM   723  C  CB  . SER   A 1 99  ? -0.331  -22.543 64.106  1.00 24.75 ? 127 SER   A CB  1 
ATOM   724  O  OG  . SER   A 1 99  ? 0.349   -23.744 63.774  1.00 24.79 ? 127 SER   A OG  1 
ATOM   725  N  N   . CYS   A 1 100 ? -2.685  -20.576 63.486  1.00 20.02 ? 128 CYS   A N   1 
ATOM   726  C  CA  . CYS   A 1 100 ? -3.322  -19.282 63.696  1.00 20.09 ? 128 CYS   A CA  1 
ATOM   727  C  C   . CYS   A 1 100 ? -4.787  -19.448 64.097  1.00 18.37 ? 128 CYS   A C   1 
ATOM   728  O  O   . CYS   A 1 100 ? -5.259  -18.821 65.056  1.00 18.98 ? 128 CYS   A O   1 
ATOM   729  C  CB  . CYS   A 1 100 ? -3.196  -18.431 62.438  1.00 16.81 ? 128 CYS   A CB  1 
ATOM   730  S  SG  . CYS   A 1 100 ? -3.780  -16.780 62.731  1.00 24.15 ? 128 CYS   A SG  1 
ATOM   731  N  N   . ARG   A 1 101 ? -5.521  -20.310 63.390  1.00 21.65 ? 129 ARG   A N   1 
ATOM   732  C  CA  . ARG   A 1 101 ? -6.919  -20.533 63.748  1.00 18.51 ? 129 ARG   A CA  1 
ATOM   733  C  C   . ARG   A 1 101 ? -7.038  -21.155 65.132  1.00 20.46 ? 129 ARG   A C   1 
ATOM   734  O  O   . ARG   A 1 101 ? -7.873  -20.736 65.939  1.00 19.91 ? 129 ARG   A O   1 
ATOM   735  C  CB  . ARG   A 1 101 ? -7.594  -21.400 62.688  1.00 18.74 ? 129 ARG   A CB  1 
ATOM   736  C  CG  . ARG   A 1 101 ? -7.864  -20.613 61.420  1.00 22.41 ? 129 ARG   A CG  1 
ATOM   737  C  CD  . ARG   A 1 101 ? -8.826  -21.320 60.487  1.00 33.39 ? 129 ARG   A CD  1 
ATOM   738  N  NE  . ARG   A 1 101 ? -9.329  -20.402 59.463  1.00 28.43 ? 129 ARG   A NE  1 
ATOM   739  C  CZ  . ARG   A 1 101 ? -8.659  -20.068 58.362  1.00 22.87 ? 129 ARG   A CZ  1 
ATOM   740  N  NH1 . ARG   A 1 101 ? -7.449  -20.560 58.137  1.00 27.93 ? 129 ARG   A NH1 1 
ATOM   741  N  NH2 . ARG   A 1 101 ? -9.188  -19.230 57.488  1.00 26.81 ? 129 ARG   A NH2 1 
ATOM   742  N  N   . SER   A 1 102 ? -6.190  -22.136 65.436  1.00 20.49 ? 130 SER   A N   1 
ATOM   743  C  CA  . SER   A 1 102 ? -6.202  -22.731 66.767  1.00 19.64 ? 130 SER   A CA  1 
ATOM   744  C  C   . SER   A 1 102 ? -5.869  -21.693 67.837  1.00 15.59 ? 130 SER   A C   1 
ATOM   745  O  O   . SER   A 1 102 ? -6.596  -21.545 68.821  1.00 19.03 ? 130 SER   A O   1 
ATOM   746  C  CB  . SER   A 1 102 ? -5.220  -23.910 66.805  1.00 21.08 ? 130 SER   A CB  1 
ATOM   747  O  OG  . SER   A 1 102 ? -5.308  -24.651 68.013  1.00 26.70 ? 130 SER   A OG  1 
ATOM   748  N  N   . PHE   A 1 103 ? -4.749  -20.991 67.679  1.00 18.25 ? 131 PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 103 ? -4.376  -19.928 68.613  1.00 18.44 ? 131 PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 103 ? -5.547  -18.990 68.887  1.00 15.00 ? 131 PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 103 ? -5.951  -18.792 70.037  1.00 15.14 ? 131 PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 103 ? -3.189  -19.148 68.045  1.00 16.05 ? 131 PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 103 ? -2.752  -17.986 68.885  1.00 17.21 ? 131 PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 103 ? -3.424  -16.770 68.821  1.00 15.20 ? 131 PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 103 ? -1.627  -18.085 69.694  1.00 15.75 ? 131 PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 103 ? -3.003  -15.681 69.587  1.00 17.76 ? 131 PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 103 ? -1.205  -17.005 70.456  1.00 14.92 ? 131 PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 103 ? -1.897  -15.806 70.408  1.00 13.05 ? 131 PHE   A CZ  1 
ATOM   759  N  N   . PHE   A 1 104 ? -6.103  -18.408 67.825  1.00 14.11 ? 132 PHE   A N   1 
ATOM   760  C  CA  . PHE   A 1 104 ? -7.130  -17.379 67.990  1.00 13.21 ? 132 PHE   A CA  1 
ATOM   761  C  C   . PHE   A 1 104 ? -8.402  -17.948 68.599  1.00 16.73 ? 132 PHE   A C   1 
ATOM   762  O  O   . PHE   A 1 104 ? -8.997  -17.346 69.497  1.00 17.16 ? 132 PHE   A O   1 
ATOM   763  C  CB  . PHE   A 1 104 ? -7.440  -16.725 66.652  1.00 9.63  ? 132 PHE   A CB  1 
ATOM   764  C  CG  . PHE   A 1 104 ? -8.434  -15.597 66.752  1.00 18.11 ? 132 PHE   A CG  1 
ATOM   765  C  CD1 . PHE   A 1 104 ? -8.040  -14.344 67.203  1.00 14.11 ? 132 PHE   A CD1 1 
ATOM   766  C  CD2 . PHE   A 1 104 ? -9.755  -15.786 66.389  1.00 15.65 ? 132 PHE   A CD2 1 
ATOM   767  C  CE1 . PHE   A 1 104 ? -8.957  -13.298 67.305  1.00 17.88 ? 132 PHE   A CE1 1 
ATOM   768  C  CE2 . PHE   A 1 104 ? -10.674 -14.743 66.490  1.00 17.72 ? 132 PHE   A CE2 1 
ATOM   769  C  CZ  . PHE   A 1 104 ? -10.274 -13.498 66.948  1.00 15.92 ? 132 PHE   A CZ  1 
ATOM   770  N  N   . SER   A 1 105 ? -8.859  -19.098 68.120  1.00 16.07 ? 133 SER   A N   1 
ATOM   771  C  CA  . SER   A 1 105 ? -10.083 -19.604 68.714  1.00 17.43 ? 133 SER   A CA  1 
ATOM   772  C  C   . SER   A 1 105 ? -9.864  -20.025 70.156  1.00 15.78 ? 133 SER   A C   1 
ATOM   773  O  O   . SER   A 1 105 ? -10.832 -20.144 70.906  1.00 21.01 ? 133 SER   A O   1 
ATOM   774  C  CB  . SER   A 1 105 ? -10.655 -20.765 67.894  1.00 17.36 ? 133 SER   A CB  1 
ATOM   775  O  OG  . SER   A 1 105 ? -10.061 -21.958 68.298  1.00 27.54 ? 133 SER   A OG  1 
ATOM   776  N  N   . SER   A 1 106 ? -8.616  -20.221 70.571  1.00 16.96 ? 134 SER   A N   1 
ATOM   777  C  CA  . SER   A 1 106 ? -8.332  -20.591 71.951  1.00 18.79 ? 134 SER   A CA  1 
ATOM   778  C  C   . SER   A 1 106 ? -8.203  -19.379 72.873  1.00 16.07 ? 134 SER   A C   1 
ATOM   779  O  O   . SER   A 1 106 ? -8.759  -19.373 73.976  1.00 17.07 ? 134 SER   A O   1 
ATOM   780  C  CB  . SER   A 1 106 ? -7.051  -21.437 72.003  1.00 21.76 ? 134 SER   A CB  1 
ATOM   781  O  OG  . SER   A 1 106 ? -6.708  -21.762 73.338  1.00 20.16 ? 134 SER   A OG  1 
ATOM   782  N  N   . HIS   A 1 107 ? -7.462  -18.353 72.449  1.00 17.72 ? 135 HIS   A N   1 
ATOM   783  C  CA  . HIS   A 1 107 ? -7.138  -17.225 73.314  1.00 13.72 ? 135 HIS   A CA  1 
ATOM   784  C  C   . HIS   A 1 107 ? -7.895  -15.954 72.972  1.00 19.94 ? 135 HIS   A C   1 
ATOM   785  O  O   . HIS   A 1 107 ? -7.873  -15.009 73.769  1.00 21.95 ? 135 HIS   A O   1 
ATOM   786  C  CB  . HIS   A 1 107 ? -5.639  -16.918 73.255  1.00 16.94 ? 135 HIS   A CB  1 
ATOM   787  C  CG  . HIS   A 1 107 ? -4.774  -18.122 73.415  1.00 17.23 ? 135 HIS   A CG  1 
ATOM   788  N  ND1 . HIS   A 1 107 ? -4.535  -18.705 74.638  1.00 23.42 ? 135 HIS   A ND1 1 
ATOM   789  C  CD2 . HIS   A 1 107 ? -4.099  -18.860 72.506  1.00 17.29 ? 135 HIS   A CD2 1 
ATOM   790  C  CE1 . HIS   A 1 107 ? -3.758  -19.760 74.474  1.00 19.11 ? 135 HIS   A CE1 1 
ATOM   791  N  NE2 . HIS   A 1 107 ? -3.476  -19.874 73.190  1.00 18.46 ? 135 HIS   A NE2 1 
ATOM   792  N  N   . GLY   A 1 108 ? -8.566  -15.910 71.828  1.00 16.88 ? 136 GLY   A N   1 
ATOM   793  C  CA  . GLY   A 1 108 ? -9.095  -14.679 71.329  1.00 14.88 ? 136 GLY   A CA  1 
ATOM   794  C  C   . GLY   A 1 108 ? -7.937  -13.834 70.836  1.00 21.16 ? 136 GLY   A C   1 
ATOM   795  O  O   . GLY   A 1 108 ? -6.790  -14.274 70.754  1.00 20.38 ? 136 GLY   A O   1 
ATOM   796  N  N   . LEU   A 1 109 ? -8.273  -12.600 70.479  1.00 16.38 ? 137 LEU   A N   1 
ATOM   797  C  CA  . LEU   A 1 109 ? -7.273  -11.639 70.040  1.00 18.48 ? 137 LEU   A CA  1 
ATOM   798  C  C   . LEU   A 1 109 ? -6.159  -11.476 71.072  1.00 18.61 ? 137 LEU   A C   1 
ATOM   799  O  O   . LEU   A 1 109 ? -6.402  -11.169 72.245  1.00 21.54 ? 137 LEU   A O   1 
ATOM   800  C  CB  . LEU   A 1 109 ? -7.945  -10.292 69.733  1.00 18.18 ? 137 LEU   A CB  1 
ATOM   801  C  CG  . LEU   A 1 109 ? -7.063  -9.044  69.795  1.00 20.09 ? 137 LEU   A CG  1 
ATOM   802  C  CD1 . LEU   A 1 109 ? -6.007  -9.101  68.773  1.00 14.87 ? 137 LEU   A CD1 1 
ATOM   803  C  CD2 . LEU   A 1 109 ? -7.932  -7.776  69.562  1.00 17.22 ? 137 LEU   A CD2 1 
ATOM   804  N  N   . GLY   A 1 110 ? -4.934  -11.696 70.623  1.00 19.76 ? 138 GLY   A N   1 
ATOM   805  C  CA  . GLY   A 1 110 ? -3.782  -11.367 71.435  1.00 18.55 ? 138 GLY   A CA  1 
ATOM   806  C  C   . GLY   A 1 110 ? -2.485  -11.546 70.671  1.00 15.19 ? 138 GLY   A C   1 
ATOM   807  O  O   . GLY   A 1 110 ? -2.478  -11.784 69.460  1.00 14.32 ? 138 GLY   A O   1 
ATOM   808  N  N   . VAL   A 1 111 ? -1.381  -11.439 71.409  1.00 12.67 ? 139 VAL   A N   1 
ATOM   809  C  CA  . VAL   A 1 111 ? -0.050  -11.379 70.811  1.00 16.65 ? 139 VAL   A CA  1 
ATOM   810  C  C   . VAL   A 1 111 ? 0.446   -12.787 70.541  1.00 13.80 ? 139 VAL   A C   1 
ATOM   811  O  O   . VAL   A 1 111 ? 0.521   -13.610 71.458  1.00 15.79 ? 139 VAL   A O   1 
ATOM   812  C  CB  . VAL   A 1 111 ? 0.933   -10.626 71.722  1.00 17.93 ? 139 VAL   A CB  1 
ATOM   813  C  CG1 . VAL   A 1 111 ? 2.401   -10.928 71.310  1.00 14.12 ? 139 VAL   A CG1 1 
ATOM   814  C  CG2 . VAL   A 1 111 ? 0.636   -9.143  71.683  1.00 13.74 ? 139 VAL   A CG2 1 
ATOM   815  N  N   . ARG   A 1 112 ? 0.775   -13.070 69.286  1.00 12.77 ? 140 ARG   A N   1 
ATOM   816  C  CA  . ARG   A 1 112 ? 1.432   -14.331 68.965  1.00 14.96 ? 140 ARG   A CA  1 
ATOM   817  C  C   . ARG   A 1 112 ? 2.951   -14.253 69.133  1.00 18.03 ? 140 ARG   A C   1 
ATOM   818  O  O   . ARG   A 1 112 ? 3.572   -15.205 69.625  1.00 14.94 ? 140 ARG   A O   1 
ATOM   819  C  CB  . ARG   A 1 112 ? 1.087   -14.756 67.537  1.00 14.08 ? 140 ARG   A CB  1 
ATOM   820  C  CG  . ARG   A 1 112 ? 2.015   -15.817 66.953  1.00 14.93 ? 140 ARG   A CG  1 
ATOM   821  C  CD  . ARG   A 1 112 ? 1.934   -17.163 67.706  1.00 11.92 ? 140 ARG   A CD  1 
ATOM   822  N  NE  . ARG   A 1 112 ? 2.611   -18.196 66.926  1.00 17.26 ? 140 ARG   A NE  1 
ATOM   823  C  CZ  . ARG   A 1 112 ? 2.679   -19.475 67.270  1.00 16.60 ? 140 ARG   A CZ  1 
ATOM   824  N  NH1 . ARG   A 1 112 ? 2.098   -19.896 68.387  1.00 14.96 ? 140 ARG   A NH1 1 
ATOM   825  N  NH2 . ARG   A 1 112 ? 3.315   -20.332 66.488  1.00 20.03 ? 140 ARG   A NH2 1 
ATOM   826  N  N   . ALA   A 1 113 ? 3.567   -13.131 68.751  1.00 15.15 ? 141 ALA   A N   1 
ATOM   827  C  CA  . ALA   A 1 113 ? 5.019   -13.032 68.689  1.00 18.68 ? 141 ALA   A CA  1 
ATOM   828  C  C   . ALA   A 1 113 ? 5.514   -11.758 69.351  1.00 18.16 ? 141 ALA   A C   1 
ATOM   829  O  O   . ALA   A 1 113 ? 5.082   -10.651 68.998  1.00 20.58 ? 141 ALA   A O   1 
ATOM   830  C  CB  . ALA   A 1 113 ? 5.505   -13.081 67.237  1.00 20.14 ? 141 ALA   A CB  1 
ATOM   831  N  N   . VAL   A 1 114 ? 6.424   -11.915 70.305  1.00 19.30 ? 142 VAL   A N   1 
ATOM   832  C  CA  . VAL   A 1 114 ? 7.279   -10.826 70.770  1.00 15.33 ? 142 VAL   A CA  1 
ATOM   833  C  C   . VAL   A 1 114 ? 8.589   -10.938 70.003  1.00 22.38 ? 142 VAL   A C   1 
ATOM   834  O  O   . VAL   A 1 114 ? 9.309   -11.938 70.122  1.00 19.14 ? 142 VAL   A O   1 
ATOM   835  C  CB  . VAL   A 1 114 ? 7.511   -10.881 72.289  1.00 17.64 ? 142 VAL   A CB  1 
ATOM   836  C  CG1 . VAL   A 1 114 ? 8.385   -9.699  72.742  1.00 12.84 ? 142 VAL   A CG1 1 
ATOM   837  C  CG2 . VAL   A 1 114 ? 6.179   -10.894 73.040  1.00 11.58 ? 142 VAL   A CG2 1 
ATOM   838  N  N   . ALA   A 1 115 ? 8.891   -9.938  69.189  1.00 20.24 ? 143 ALA   A N   1 
ATOM   839  C  CA  . ALA   A 1 115 ? 9.984   -10.043 68.235  1.00 22.16 ? 143 ALA   A CA  1 
ATOM   840  C  C   . ALA   A 1 115 ? 11.093  -9.078  68.621  1.00 20.29 ? 143 ALA   A C   1 
ATOM   841  O  O   . ALA   A 1 115 ? 10.838  -7.884  68.808  1.00 19.57 ? 143 ALA   A O   1 
ATOM   842  C  CB  . ALA   A 1 115 ? 9.503   -9.746  66.817  1.00 15.83 ? 143 ALA   A CB  1 
ATOM   843  N  N   . ILE   A 1 116 ? 12.313  -9.594  68.717  1.00 19.69 ? 144 ILE   A N   1 
ATOM   844  C  CA  . ILE   A 1 116 ? 13.499  -8.800  69.034  1.00 19.21 ? 144 ILE   A CA  1 
ATOM   845  C  C   . ILE   A 1 116 ? 14.496  -8.909  67.891  1.00 19.41 ? 144 ILE   A C   1 
ATOM   846  O  O   . ILE   A 1 116 ? 14.615  -9.951  67.241  1.00 20.07 ? 144 ILE   A O   1 
ATOM   847  C  CB  . ILE   A 1 116 ? 14.170  -9.267  70.335  1.00 17.43 ? 144 ILE   A CB  1 
ATOM   848  C  CG1 . ILE   A 1 116 ? 14.529  -10.753 70.231  1.00 20.10 ? 144 ILE   A CG1 1 
ATOM   849  C  CG2 . ILE   A 1 116 ? 13.290  -8.982  71.527  1.00 20.55 ? 144 ILE   A CG2 1 
ATOM   850  C  CD1 . ILE   A 1 116 ? 15.378  -11.286 71.377  1.00 15.49 ? 144 ILE   A CD1 1 
ATOM   851  N  N   . GLU   A 1 117 ? 15.231  -7.833  67.656  1.00 17.57 ? 145 GLU   A N   1 
ATOM   852  C  CA  . GLU   A 1 117 ? 16.301  -7.866  66.682  1.00 19.03 ? 145 GLU   A CA  1 
ATOM   853  C  C   . GLU   A 1 117 ? 17.563  -8.399  67.345  1.00 19.35 ? 145 GLU   A C   1 
ATOM   854  O  O   . GLU   A 1 117 ? 17.863  -8.066  68.492  1.00 20.79 ? 145 GLU   A O   1 
ATOM   855  C  CB  . GLU   A 1 117 ? 16.545  -6.482  66.097  1.00 22.28 ? 145 GLU   A CB  1 
ATOM   856  C  CG  . GLU   A 1 117 ? 17.309  -6.514  64.809  1.00 25.36 ? 145 GLU   A CG  1 
ATOM   857  C  CD  . GLU   A 1 117 ? 17.803  -5.144  64.413  1.00 31.17 ? 145 GLU   A CD  1 
ATOM   858  O  OE1 . GLU   A 1 117 ? 18.667  -5.075  63.520  1.00 34.57 ? 145 GLU   A OE1 1 
ATOM   859  O  OE2 . GLU   A 1 117 ? 17.324  -4.142  64.988  1.00 29.69 ? 145 GLU   A OE2 1 
ATOM   860  N  N   . VAL   A 1 118 ? 18.277  -9.265  66.634  1.00 21.86 ? 146 VAL   A N   1 
ATOM   861  C  CA  . VAL   A 1 118 ? 19.496  -9.879  67.144  1.00 20.59 ? 146 VAL   A CA  1 
ATOM   862  C  C   . VAL   A 1 118 ? 20.564  -9.721  66.077  1.00 21.66 ? 146 VAL   A C   1 
ATOM   863  O  O   . VAL   A 1 118 ? 20.268  -9.420  64.920  1.00 25.04 ? 146 VAL   A O   1 
ATOM   864  C  CB  . VAL   A 1 118 ? 19.310  -11.369 67.503  1.00 21.57 ? 146 VAL   A CB  1 
ATOM   865  C  CG1 . VAL   A 1 118 ? 18.269  -11.544 68.599  1.00 17.26 ? 146 VAL   A CG1 1 
ATOM   866  C  CG2 . VAL   A 1 118 ? 18.962  -12.155 66.271  1.00 20.02 ? 146 VAL   A CG2 1 
ATOM   867  N  N   . GLU   A 1 119 ? 21.825  -9.920  66.475  1.00 24.77 ? 147 GLU   A N   1 
ATOM   868  C  CA  . GLU   A 1 119 ? 22.894  -9.901  65.481  1.00 21.69 ? 147 GLU   A CA  1 
ATOM   869  C  C   . GLU   A 1 119 ? 22.695  -11.004 64.449  1.00 20.64 ? 147 GLU   A C   1 
ATOM   870  O  O   . GLU   A 1 119 ? 22.856  -10.777 63.242  1.00 22.16 ? 147 GLU   A O   1 
ATOM   871  C  CB  . GLU   A 1 119 ? 24.265  -10.013 66.162  1.00 25.25 ? 147 GLU   A CB  1 
ATOM   872  C  CG  . GLU   A 1 119 ? 25.048  -8.707  66.179  1.00 30.56 ? 147 GLU   A CG  1 
ATOM   873  C  CD  . GLU   A 1 119 ? 26.532  -8.879  66.538  1.00 41.83 ? 147 GLU   A CD  1 
ATOM   874  O  OE1 . GLU   A 1 119 ? 27.375  -9.012  65.627  1.00 44.66 ? 147 GLU   A OE1 1 
ATOM   875  O  OE2 . GLU   A 1 119 ? 26.874  -8.856  67.738  1.00 41.70 ? 147 GLU   A OE2 1 
ATOM   876  N  N   . ASP   A 1 120 ? 22.321  -12.202 64.897  1.00 23.30 ? 148 ASP   A N   1 
ATOM   877  C  CA  . ASP   A 1 120 ? 22.254  -13.363 64.010  1.00 24.16 ? 148 ASP   A CA  1 
ATOM   878  C  C   . ASP   A 1 120 ? 21.110  -14.242 64.510  1.00 23.54 ? 148 ASP   A C   1 
ATOM   879  O  O   . ASP   A 1 120 ? 21.260  -14.929 65.527  1.00 22.76 ? 148 ASP   A O   1 
ATOM   880  C  CB  . ASP   A 1 120 ? 23.582  -14.114 63.999  1.00 27.77 ? 148 ASP   A CB  1 
ATOM   881  C  CG  . ASP   A 1 120 ? 23.666  -15.174 62.897  1.00 29.70 ? 148 ASP   A CG  1 
ATOM   882  O  OD1 . ASP   A 1 120 ? 22.642  -15.552 62.309  1.00 27.51 ? 148 ASP   A OD1 1 
ATOM   883  O  OD2 . ASP   A 1 120 ? 24.774  -15.655 62.620  1.00 35.99 ? 148 ASP   A OD2 1 
ATOM   884  N  N   . ALA   A 1 121 ? 19.970  -14.198 63.805  1.00 28.88 ? 149 ALA   A N   1 
ATOM   885  C  CA  . ALA   A 1 121 ? 18.816  -15.008 64.197  1.00 21.64 ? 149 ALA   A CA  1 
ATOM   886  C  C   . ALA   A 1 121 ? 19.174  -16.488 64.293  1.00 24.82 ? 149 ALA   A C   1 
ATOM   887  O  O   . ALA   A 1 121 ? 18.790  -17.163 65.254  1.00 23.26 ? 149 ALA   A O   1 
ATOM   888  C  CB  . ALA   A 1 121 ? 17.672  -14.805 63.208  1.00 21.20 ? 149 ALA   A CB  1 
ATOM   889  N  N   . GLU   A 1 122 ? 19.928  -17.004 63.315  1.00 25.60 ? 150 GLU   A N   1 
ATOM   890  C  CA  . GLU   A 1 122 ? 20.288  -18.427 63.308  1.00 30.98 ? 150 GLU   A CA  1 
ATOM   891  C  C   . GLU   A 1 122 ? 21.132  -18.813 64.522  1.00 25.48 ? 150 GLU   A C   1 
ATOM   892  O  O   . GLU   A 1 122 ? 20.827  -19.794 65.207  1.00 25.96 ? 150 GLU   A O   1 
ATOM   893  C  CB  . GLU   A 1 122 ? 21.031  -18.783 62.020  1.00 33.14 ? 150 GLU   A CB  1 
ATOM   894  C  CG  . GLU   A 1 122 ? 21.884  -20.035 62.149  1.00 30.64 ? 150 GLU   A CG  1 
ATOM   895  C  CD  . GLU   A 1 122 ? 21.892  -20.859 60.890  1.00 37.02 ? 150 GLU   A CD  1 
ATOM   896  O  OE1 . GLU   A 1 122 ? 21.536  -22.050 60.970  1.00 39.01 ? 150 GLU   A OE1 1 
ATOM   897  O  OE2 . GLU   A 1 122 ? 22.238  -20.322 59.820  1.00 42.44 ? 150 GLU   A OE2 1 
ATOM   898  N  N   . SER   A 1 123 ? 22.216  -18.071 64.787  1.00 25.04 ? 151 SER   A N   1 
ATOM   899  C  CA  . SER   A 1 123 ? 22.998  -18.334 65.993  1.00 24.43 ? 151 SER   A CA  1 
ATOM   900  C  C   . SER   A 1 123 ? 22.123  -18.240 67.232  1.00 24.12 ? 151 SER   A C   1 
ATOM   901  O  O   . SER   A 1 123 ? 22.190  -19.100 68.122  1.00 22.78 ? 151 SER   A O   1 
ATOM   902  C  CB  . SER   A 1 123 ? 24.165  -17.353 66.114  1.00 23.57 ? 151 SER   A CB  1 
ATOM   903  O  OG  . SER   A 1 123 ? 24.771  -17.124 64.861  1.00 33.16 ? 151 SER   A OG  1 
ATOM   904  N  N   . ALA   A 1 124 ? 21.282  -17.204 67.292  1.00 21.46 ? 152 ALA   A N   1 
ATOM   905  C  CA  . ALA   A 1 124 ? 20.397  -17.018 68.435  1.00 21.11 ? 152 ALA   A CA  1 
ATOM   906  C  C   . ALA   A 1 124 ? 19.448  -18.198 68.596  1.00 19.89 ? 152 ALA   A C   1 
ATOM   907  O  O   . ALA   A 1 124 ? 19.248  -18.690 69.711  1.00 23.55 ? 152 ALA   A O   1 
ATOM   908  C  CB  . ALA   A 1 124 ? 19.616  -15.709 68.286  1.00 23.85 ? 152 ALA   A CB  1 
ATOM   909  N  N   . PHE   A 1 125 ? 18.854  -18.673 67.500  1.00 21.04 ? 153 PHE   A N   1 
ATOM   910  C  CA  . PHE   A 1 125 ? 18.000  -19.855 67.605  1.00 19.78 ? 153 PHE   A CA  1 
ATOM   911  C  C   . PHE   A 1 125 ? 18.819  -21.063 68.051  1.00 18.46 ? 153 PHE   A C   1 
ATOM   912  O  O   . PHE   A 1 125 ? 18.490  -21.719 69.045  1.00 21.76 ? 153 PHE   A O   1 
ATOM   913  C  CB  . PHE   A 1 125 ? 17.292  -20.125 66.277  1.00 20.10 ? 153 PHE   A CB  1 
ATOM   914  C  CG  . PHE   A 1 125 ? 16.517  -21.431 66.248  1.00 20.63 ? 153 PHE   A CG  1 
ATOM   915  C  CD1 . PHE   A 1 125 ? 17.159  -22.632 65.954  1.00 22.79 ? 153 PHE   A CD1 1 
ATOM   916  C  CD2 . PHE   A 1 125 ? 15.159  -21.457 66.506  1.00 18.23 ? 153 PHE   A CD2 1 
ATOM   917  C  CE1 . PHE   A 1 125 ? 16.461  -23.830 65.925  1.00 22.64 ? 153 PHE   A CE1 1 
ATOM   918  C  CE2 . PHE   A 1 125 ? 14.448  -22.640 66.461  1.00 16.72 ? 153 PHE   A CE2 1 
ATOM   919  C  CZ  . PHE   A 1 125 ? 15.097  -23.831 66.171  1.00 19.06 ? 153 PHE   A CZ  1 
ATOM   920  N  N   . SER   A 1 126 ? 19.928  -21.334 67.363  1.00 24.67 ? 154 SER   A N   1 
ATOM   921  C  CA  . SER   A 1 126 ? 20.751  -22.495 67.710  1.00 20.45 ? 154 SER   A CA  1 
ATOM   922  C  C   . SER   A 1 126 ? 21.169  -22.458 69.169  1.00 19.86 ? 154 SER   A C   1 
ATOM   923  O  O   . SER   A 1 126 ? 20.883  -23.388 69.930  1.00 20.46 ? 154 SER   A O   1 
ATOM   924  C  CB  . SER   A 1 126 ? 21.961  -22.566 66.794  1.00 25.85 ? 154 SER   A CB  1 
ATOM   925  O  OG  . SER   A 1 126 ? 21.552  -22.955 65.488  1.00 30.71 ? 154 SER   A OG  1 
ATOM   926  N  N   . ILE   A 1 127 ? 21.791  -21.356 69.594  1.00 21.21 ? 155 ILE   A N   1 
ATOM   927  C  CA  . ILE   A 1 127 ? 22.203  -21.211 70.990  1.00 18.08 ? 155 ILE   A CA  1 
ATOM   928  C  C   . ILE   A 1 127 ? 21.023  -21.388 71.942  1.00 18.52 ? 155 ILE   A C   1 
ATOM   929  O  O   . ILE   A 1 127 ? 21.130  -22.088 72.961  1.00 21.70 ? 155 ILE   A O   1 
ATOM   930  C  CB  . ILE   A 1 127 ? 22.913  -19.855 71.183  1.00 21.69 ? 155 ILE   A CB  1 
ATOM   931  C  CG1 . ILE   A 1 127 ? 24.279  -19.911 70.500  1.00 17.15 ? 155 ILE   A CG1 1 
ATOM   932  C  CG2 . ILE   A 1 127 ? 23.030  -19.511 72.655  1.00 23.49 ? 155 ILE   A CG2 1 
ATOM   933  C  CD1 . ILE   A 1 127 ? 24.835  -18.597 70.077  1.00 16.60 ? 155 ILE   A CD1 1 
ATOM   934  N  N   . SER   A 1 128 ? 19.876  -20.773 71.620  1.00 20.52 ? 156 SER   A N   1 
ATOM   935  C  CA  . SER   A 1 128 ? 18.675  -20.908 72.454  1.00 18.87 ? 156 SER   A CA  1 
ATOM   936  C  C   . SER   A 1 128 ? 18.245  -22.361 72.600  1.00 20.01 ? 156 SER   A C   1 
ATOM   937  O  O   . SER   A 1 128 ? 17.956  -22.830 73.711  1.00 21.79 ? 156 SER   A O   1 
ATOM   938  C  CB  . SER   A 1 128 ? 17.518  -20.091 71.856  1.00 20.26 ? 156 SER   A CB  1 
ATOM   939  O  OG  . SER   A 1 128 ? 17.888  -18.731 71.732  1.00 19.11 ? 156 SER   A OG  1 
ATOM   940  N  N   . VAL   A 1 129 ? 18.133  -23.077 71.482  1.00 19.26 ? 157 VAL   A N   1 
ATOM   941  C  CA  . VAL   A 1 129 ? 17.694  -24.465 71.557  1.00 22.01 ? 157 VAL   A CA  1 
ATOM   942  C  C   . VAL   A 1 129 ? 18.682  -25.287 72.376  1.00 25.11 ? 157 VAL   A C   1 
ATOM   943  O  O   . VAL   A 1 129 ? 18.285  -26.041 73.273  1.00 22.61 ? 157 VAL   A O   1 
ATOM   944  C  CB  . VAL   A 1 129 ? 17.492  -25.038 70.145  1.00 26.85 ? 157 VAL   A CB  1 
ATOM   945  C  CG1 . VAL   A 1 129 ? 17.127  -26.502 70.229  1.00 25.53 ? 157 VAL   A CG1 1 
ATOM   946  C  CG2 . VAL   A 1 129 ? 16.390  -24.252 69.427  1.00 23.46 ? 157 VAL   A CG2 1 
ATOM   947  N  N   . ALA   A 1 130 ? 19.988  -25.112 72.117  1.00 20.82 ? 158 ALA   A N   1 
ATOM   948  C  CA  . ALA   A 1 130 ? 21.025  -25.783 72.900  1.00 19.50 ? 158 ALA   A CA  1 
ATOM   949  C  C   . ALA   A 1 130 ? 20.946  -25.438 74.378  1.00 23.61 ? 158 ALA   A C   1 
ATOM   950  O  O   . ALA   A 1 130 ? 21.456  -26.196 75.208  1.00 26.09 ? 158 ALA   A O   1 
ATOM   951  C  CB  . ALA   A 1 130 ? 22.419  -25.422 72.386  1.00 23.10 ? 158 ALA   A CB  1 
ATOM   952  N  N   . ASN   A 1 131 ? 20.314  -24.326 74.740  1.00 20.78 ? 159 ASN   A N   1 
ATOM   953  C  CA  . ASN   A 1 131 ? 20.128  -24.022 76.146  1.00 20.59 ? 159 ASN   A CA  1 
ATOM   954  C  C   . ASN   A 1 131 ? 18.674  -24.193 76.593  1.00 23.45 ? 159 ASN   A C   1 
ATOM   955  O  O   . ASN   A 1 131 ? 18.252  -23.600 77.587  1.00 26.47 ? 159 ASN   A O   1 
ATOM   956  C  CB  . ASN   A 1 131 ? 20.677  -22.632 76.446  1.00 23.04 ? 159 ASN   A CB  1 
ATOM   957  C  CG  . ASN   A 1 131 ? 22.220  -22.632 76.543  1.00 25.50 ? 159 ASN   A CG  1 
ATOM   958  O  OD1 . ASN   A 1 131 ? 22.784  -22.770 77.627  1.00 21.02 ? 159 ASN   A OD1 1 
ATOM   959  N  ND2 . ASN   A 1 131 ? 22.891  -22.495 75.398  1.00 19.92 ? 159 ASN   A ND2 1 
ATOM   960  N  N   . GLY   A 1 132 ? 17.913  -25.048 75.901  1.00 20.67 ? 160 GLY   A N   1 
ATOM   961  C  CA  . GLY   A 1 132 ? 16.631  -25.526 76.386  1.00 22.20 ? 160 GLY   A CA  1 
ATOM   962  C  C   . GLY   A 1 132 ? 15.397  -24.926 75.734  1.00 24.57 ? 160 GLY   A C   1 
ATOM   963  O  O   . GLY   A 1 132 ? 14.290  -25.400 76.012  1.00 23.08 ? 160 GLY   A O   1 
ATOM   964  N  N   . ALA   A 1 133 ? 15.535  -23.899 74.901  1.00 24.37 ? 161 ALA   A N   1 
ATOM   965  C  CA  . ALA   A 1 133 ? 14.378  -23.326 74.222  1.00 23.28 ? 161 ALA   A CA  1 
ATOM   966  C  C   . ALA   A 1 133 ? 13.632  -24.403 73.445  1.00 22.77 ? 161 ALA   A C   1 
ATOM   967  O  O   . ALA   A 1 133 ? 14.244  -25.298 72.859  1.00 20.38 ? 161 ALA   A O   1 
ATOM   968  C  CB  . ALA   A 1 133 ? 14.818  -22.217 73.263  1.00 18.78 ? 161 ALA   A CB  1 
ATOM   969  N  N   . ILE   A 1 134 ? 12.305  -24.319 73.448  1.00 20.14 ? 162 ILE   A N   1 
ATOM   970  C  CA  . ILE   A 1 134 ? 11.508  -25.183 72.586  1.00 19.23 ? 162 ILE   A CA  1 
ATOM   971  C  C   . ILE   A 1 134 ? 11.490  -24.549 71.202  1.00 22.88 ? 162 ILE   A C   1 
ATOM   972  O  O   . ILE   A 1 134 ? 11.056  -23.396 71.061  1.00 23.15 ? 162 ILE   A O   1 
ATOM   973  C  CB  . ILE   A 1 134 ? 10.088  -25.381 73.133  1.00 24.23 ? 162 ILE   A CB  1 
ATOM   974  C  CG1 . ILE   A 1 134 ? 10.120  -26.010 74.526  1.00 19.05 ? 162 ILE   A CG1 1 
ATOM   975  C  CG2 . ILE   A 1 134 ? 9.274   -26.285 72.190  1.00 23.76 ? 162 ILE   A CG2 1 
ATOM   976  C  CD1 . ILE   A 1 134 ? 10.331  -27.506 74.489  1.00 27.20 ? 162 ILE   A CD1 1 
ATOM   977  N  N   . PRO   A 1 135 ? 11.959  -25.238 70.162  1.00 18.40 ? 163 PRO   A N   1 
ATOM   978  C  CA  . PRO   A 1 135 ? 11.872  -24.671 68.813  1.00 15.85 ? 163 PRO   A CA  1 
ATOM   979  C  C   . PRO   A 1 135 ? 10.428  -24.592 68.351  1.00 22.23 ? 163 PRO   A C   1 
ATOM   980  O  O   . PRO   A 1 135 ? 9.628   -25.490 68.614  1.00 24.46 ? 163 PRO   A O   1 
ATOM   981  C  CB  . PRO   A 1 135 ? 12.681  -25.654 67.956  1.00 20.75 ? 163 PRO   A CB  1 
ATOM   982  C  CG  . PRO   A 1 135 ? 12.788  -26.916 68.790  1.00 18.12 ? 163 PRO   A CG  1 
ATOM   983  C  CD  . PRO   A 1 135 ? 12.752  -26.478 70.208  1.00 18.51 ? 163 PRO   A CD  1 
ATOM   984  N  N   . SER   A 1 136 ? 10.093  -23.489 67.680  1.00 21.72 ? 164 SER   A N   1 
ATOM   985  C  CA  . SER   A 1 136 ? 8.790   -23.311 67.055  1.00 21.14 ? 164 SER   A CA  1 
ATOM   986  C  C   . SER   A 1 136 ? 8.893   -23.171 65.544  1.00 15.50 ? 164 SER   A C   1 
ATOM   987  O  O   . SER   A 1 136 ? 8.215   -23.897 64.816  1.00 20.51 ? 164 SER   A O   1 
ATOM   988  C  CB  . SER   A 1 136 ? 8.078   -22.093 67.660  1.00 18.41 ? 164 SER   A CB  1 
ATOM   989  O  OG  . SER   A 1 136 ? 6.764   -21.976 67.143  1.00 21.65 ? 164 SER   A OG  1 
ATOM   990  N  N   . SER   A 1 137 ? 9.747   -22.280 65.047  1.00 17.03 ? 165 SER   A N   1 
ATOM   991  C  CA  . SER   A 1 137 ? 10.033  -22.204 63.619  1.00 17.93 ? 165 SER   A CA  1 
ATOM   992  C  C   . SER   A 1 137 ? 11.543  -22.102 63.445  1.00 19.90 ? 165 SER   A C   1 
ATOM   993  O  O   . SER   A 1 137 ? 12.186  -21.234 64.079  1.00 19.09 ? 165 SER   A O   1 
ATOM   994  C  CB  . SER   A 1 137 ? 9.357   -21.015 62.935  1.00 16.91 ? 165 SER   A CB  1 
ATOM   995  O  OG  . SER   A 1 137 ? 9.623   -21.008 61.529  1.00 17.99 ? 165 SER   A OG  1 
ATOM   996  N  N   . PRO   A 1 138 ? 12.137  -22.920 62.577  1.00 19.88 ? 166 PRO   A N   1 
ATOM   997  C  CA  . PRO   A 1 138 ? 13.588  -22.897 62.403  1.00 16.09 ? 166 PRO   A CA  1 
ATOM   998  C  C   . PRO   A 1 138 ? 14.036  -21.592 61.766  1.00 24.56 ? 166 PRO   A C   1 
ATOM   999  O  O   . PRO   A 1 138 ? 13.195  -20.794 61.322  1.00 21.66 ? 166 PRO   A O   1 
ATOM   1000 C  CB  . PRO   A 1 138 ? 13.855  -24.095 61.477  1.00 24.83 ? 166 PRO   A CB  1 
ATOM   1001 C  CG  . PRO   A 1 138 ? 12.566  -24.322 60.738  1.00 20.95 ? 166 PRO   A CG  1 
ATOM   1002 C  CD  . PRO   A 1 138 ? 11.478  -23.919 61.712  1.00 21.22 ? 166 PRO   A CD  1 
ATOM   1003 N  N   . PRO   A 1 139 ? 15.346  -21.324 61.728  1.00 15.87 ? 167 PRO   A N   1 
ATOM   1004 C  CA  . PRO   A 1 139 ? 15.847  -20.149 60.995  1.00 20.56 ? 167 PRO   A CA  1 
ATOM   1005 C  C   . PRO   A 1 139 ? 15.558  -20.262 59.509  1.00 20.64 ? 167 PRO   A C   1 
ATOM   1006 O  O   . PRO   A 1 139 ? 15.951  -21.232 58.861  1.00 25.35 ? 167 PRO   A O   1 
ATOM   1007 C  CB  . PRO   A 1 139 ? 17.361  -20.189 61.258  1.00 22.07 ? 167 PRO   A CB  1 
ATOM   1008 C  CG  . PRO   A 1 139 ? 17.533  -20.961 62.449  1.00 18.70 ? 167 PRO   A CG  1 
ATOM   1009 C  CD  . PRO   A 1 139 ? 16.439  -22.026 62.412  1.00 15.02 ? 167 PRO   A CD  1 
ATOM   1010 N  N   . ILE   A 1 140 ? 14.879  -19.259 58.960  1.00 21.37 ? 168 ILE   A N   1 
ATOM   1011 C  CA  . ILE   A 1 140 ? 14.656  -19.169 57.520  1.00 23.36 ? 168 ILE   A CA  1 
ATOM   1012 C  C   . ILE   A 1 140 ? 15.183  -17.828 57.049  1.00 28.10 ? 168 ILE   A C   1 
ATOM   1013 O  O   . ILE   A 1 140 ? 15.001  -16.816 57.730  1.00 24.43 ? 168 ILE   A O   1 
ATOM   1014 C  CB  . ILE   A 1 140 ? 13.169  -19.349 57.124  1.00 27.23 ? 168 ILE   A CB  1 
ATOM   1015 C  CG1 . ILE   A 1 140 ? 12.736  -20.803 57.292  1.00 25.72 ? 168 ILE   A CG1 1 
ATOM   1016 C  CG2 . ILE   A 1 140 ? 12.907  -18.900 55.700  1.00 15.20 ? 168 ILE   A CG2 1 
ATOM   1017 C  CD1 . ILE   A 1 140 ? 12.292  -21.133 58.642  1.00 20.73 ? 168 ILE   A CD1 1 
ATOM   1018 N  N   . VAL   A 1 141 ? 15.869  -17.829 55.909  1.00 30.02 ? 169 VAL   A N   1 
ATOM   1019 C  CA  . VAL   A 1 141 ? 16.443  -16.612 55.349  1.00 27.92 ? 169 VAL   A CA  1 
ATOM   1020 C  C   . VAL   A 1 141 ? 15.543  -16.128 54.220  1.00 30.50 ? 169 VAL   A C   1 
ATOM   1021 O  O   . VAL   A 1 141 ? 15.159  -16.905 53.336  1.00 26.17 ? 169 VAL   A O   1 
ATOM   1022 C  CB  . VAL   A 1 141 ? 17.898  -16.827 54.885  1.00 25.93 ? 169 VAL   A CB  1 
ATOM   1023 C  CG1 . VAL   A 1 141 ? 18.724  -17.325 56.046  1.00 26.51 ? 169 VAL   A CG1 1 
ATOM   1024 C  CG2 . VAL   A 1 141 ? 17.992  -17.805 53.709  1.00 34.95 ? 169 VAL   A CG2 1 
ATOM   1025 N  N   . LEU   A 1 142 ? 15.167  -14.855 54.278  1.00 29.80 ? 170 LEU   A N   1 
ATOM   1026 C  CA  . LEU   A 1 142 ? 14.196  -14.271 53.366  1.00 27.54 ? 170 LEU   A CA  1 
ATOM   1027 C  C   . LEU   A 1 142 ? 14.935  -13.363 52.388  1.00 34.01 ? 170 LEU   A C   1 
ATOM   1028 O  O   . LEU   A 1 142 ? 15.490  -12.333 52.788  1.00 32.86 ? 170 LEU   A O   1 
ATOM   1029 C  CB  . LEU   A 1 142 ? 13.141  -13.496 54.149  1.00 30.11 ? 170 LEU   A CB  1 
ATOM   1030 C  CG  . LEU   A 1 142 ? 12.395  -14.290 55.219  1.00 30.40 ? 170 LEU   A CG  1 
ATOM   1031 C  CD1 . LEU   A 1 142 ? 11.663  -13.347 56.172  1.00 28.54 ? 170 LEU   A CD1 1 
ATOM   1032 C  CD2 . LEU   A 1 142 ? 11.424  -15.222 54.547  1.00 23.17 ? 170 LEU   A CD2 1 
ATOM   1033 N  N   . ASN   A 1 143 ? 14.959  -13.764 51.117  1.00 35.78 ? 171 ASN   A N   1 
ATOM   1034 C  CA  . ASN   A 1 143 ? 15.492  -12.945 50.030  1.00 39.59 ? 171 ASN   A CA  1 
ATOM   1035 C  C   . ASN   A 1 143 ? 16.938  -12.530 50.285  1.00 37.36 ? 171 ASN   A C   1 
ATOM   1036 O  O   . ASN   A 1 143 ? 17.329  -11.390 50.031  1.00 40.06 ? 171 ASN   A O   1 
ATOM   1037 C  CB  . ASN   A 1 143 ? 14.616  -11.717 49.785  1.00 39.72 ? 171 ASN   A CB  1 
ATOM   1038 C  CG  . ASN   A 1 143 ? 14.827  -11.137 48.411  1.00 46.14 ? 171 ASN   A CG  1 
ATOM   1039 O  OD1 . ASN   A 1 143 ? 15.199  -11.860 47.482  1.00 40.93 ? 171 ASN   A OD1 1 
ATOM   1040 N  ND2 . ASN   A 1 143 ? 14.614  -9.828  48.270  1.00 38.71 ? 171 ASN   A ND2 1 
ATOM   1041 N  N   . GLU   A 1 144 ? 17.737  -13.461 50.802  1.00 39.89 ? 172 GLU   A N   1 
ATOM   1042 C  CA  . GLU   A 1 144 ? 19.158  -13.229 51.064  1.00 43.15 ? 172 GLU   A CA  1 
ATOM   1043 C  C   . GLU   A 1 144 ? 19.385  -12.003 51.942  1.00 36.10 ? 172 GLU   A C   1 
ATOM   1044 O  O   . GLU   A 1 144 ? 20.473  -11.431 51.944  1.00 40.62 ? 172 GLU   A O   1 
ATOM   1045 C  CB  . GLU   A 1 144 ? 19.942  -13.095 49.753  1.00 43.58 ? 172 GLU   A CB  1 
ATOM   1046 C  CG  . GLU   A 1 144 ? 20.788  -14.308 49.364  1.00 48.14 ? 172 GLU   A CG  1 
ATOM   1047 C  CD  . GLU   A 1 144 ? 21.516  -14.094 48.044  1.00 61.14 ? 172 GLU   A CD  1 
ATOM   1048 O  OE1 . GLU   A 1 144 ? 20.827  -14.025 47.000  1.00 61.65 ? 172 GLU   A OE1 1 
ATOM   1049 O  OE2 . GLU   A 1 144 ? 22.766  -13.962 48.052  1.00 64.89 ? 172 GLU   A OE2 1 
ATOM   1050 N  N   . ALA   A 1 145 ? 18.377  -11.594 52.699  1.00 38.00 ? 173 ALA   A N   1 
ATOM   1051 C  CA  . ALA   A 1 145 ? 18.401  -10.300 53.371  1.00 31.71 ? 173 ALA   A CA  1 
ATOM   1052 C  C   . ALA   A 1 145 ? 18.043  -10.363 54.848  1.00 33.05 ? 173 ALA   A C   1 
ATOM   1053 O  O   . ALA   A 1 145 ? 18.604  -9.603  55.641  1.00 32.10 ? 173 ALA   A O   1 
ATOM   1054 C  CB  . ALA   A 1 145 ? 17.446  -9.344  52.638  1.00 36.61 ? 173 ALA   A CB  1 
ATOM   1055 N  N   . VAL   A 1 146 ? 17.109  -11.226 55.243  1.00 29.01 ? 174 VAL   A N   1 
ATOM   1056 C  CA  . VAL   A 1 146 ? 16.614  -11.249 56.615  1.00 27.71 ? 174 VAL   A CA  1 
ATOM   1057 C  C   . VAL   A 1 146 ? 16.513  -12.689 57.080  1.00 24.13 ? 174 VAL   A C   1 
ATOM   1058 O  O   . VAL   A 1 146 ? 15.997  -13.551 56.364  1.00 24.65 ? 174 VAL   A O   1 
ATOM   1059 C  CB  . VAL   A 1 146 ? 15.238  -10.561 56.761  1.00 29.03 ? 174 VAL   A CB  1 
ATOM   1060 C  CG1 . VAL   A 1 146 ? 14.908  -10.352 58.229  1.00 26.60 ? 174 VAL   A CG1 1 
ATOM   1061 C  CG2 . VAL   A 1 146 ? 15.195  -9.232  56.008  1.00 27.73 ? 174 VAL   A CG2 1 
ATOM   1062 N  N   . THR   A 1 147 ? 16.969  -12.942 58.294  1.00 24.57 ? 175 THR   A N   1 
ATOM   1063 C  CA  . THR   A 1 147 ? 16.763  -14.230 58.934  1.00 28.71 ? 175 THR   A CA  1 
ATOM   1064 C  C   . THR   A 1 147 ? 15.778  -14.066 60.079  1.00 27.10 ? 175 THR   A C   1 
ATOM   1065 O  O   . THR   A 1 147 ? 15.830  -13.080 60.826  1.00 26.36 ? 175 THR   A O   1 
ATOM   1066 C  CB  . THR   A 1 147 ? 18.085  -14.817 59.428  1.00 28.16 ? 175 THR   A CB  1 
ATOM   1067 O  OG1 . THR   A 1 147 ? 18.972  -14.914 58.315  1.00 26.70 ? 175 THR   A OG1 1 
ATOM   1068 C  CG2 . THR   A 1 147 ? 17.879  -16.201 60.001  1.00 24.69 ? 175 THR   A CG2 1 
ATOM   1069 N  N   . ILE   A 1 148 ? 14.863  -15.024 60.187  1.00 24.70 ? 176 ILE   A N   1 
ATOM   1070 C  CA  . ILE   A 1 148 ? 13.821  -15.018 61.200  1.00 22.14 ? 176 ILE   A CA  1 
ATOM   1071 C  C   . ILE   A 1 148 ? 13.706  -16.426 61.775  1.00 22.25 ? 176 ILE   A C   1 
ATOM   1072 O  O   . ILE   A 1 148 ? 13.745  -17.411 61.037  1.00 17.87 ? 176 ILE   A O   1 
ATOM   1073 C  CB  . ILE   A 1 148 ? 12.480  -14.525 60.603  1.00 27.42 ? 176 ILE   A CB  1 
ATOM   1074 C  CG1 . ILE   A 1 148 ? 11.337  -14.703 61.587  1.00 23.42 ? 176 ILE   A CG1 1 
ATOM   1075 C  CG2 . ILE   A 1 148 ? 12.153  -15.231 59.278  1.00 26.27 ? 176 ILE   A CG2 1 
ATOM   1076 C  CD1 . ILE   A 1 148 ? 10.010  -14.153 61.055  1.00 27.24 ? 176 ILE   A CD1 1 
ATOM   1077 N  N   . ALA   A 1 149 ? 13.611  -16.525 63.096  1.00 19.56 ? 177 ALA   A N   1 
ATOM   1078 C  CA  . ALA   A 1 149 ? 13.452  -17.820 63.744  1.00 22.31 ? 177 ALA   A CA  1 
ATOM   1079 C  C   . ALA   A 1 149 ? 12.618  -17.604 64.990  1.00 17.10 ? 177 ALA   A C   1 
ATOM   1080 O  O   . ALA   A 1 149 ? 12.555  -16.494 65.522  1.00 16.25 ? 177 ALA   A O   1 
ATOM   1081 C  CB  . ALA   A 1 149 ? 14.802  -18.479 64.118  1.00 15.89 ? 177 ALA   A CB  1 
ATOM   1082 N  N   . GLU   A 1 150 ? 11.982  -18.680 65.460  1.00 16.61 ? 178 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 150 ? 11.064  -18.568 66.581  1.00 17.75 ? 178 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 150 ? 11.286  -19.693 67.576  1.00 16.46 ? 178 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 150 ? 11.546  -20.831 67.185  1.00 20.42 ? 178 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 150 ? 9.611   -18.548 66.072  1.00 13.88 ? 178 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 150 ? 9.406   -17.415 65.079  1.00 14.73 ? 178 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 150 ? 8.017   -17.344 64.474  1.00 17.43 ? 178 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 150 ? 7.106   -18.056 64.930  1.00 19.05 ? 178 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 150 ? 7.853   -16.563 63.510  1.00 22.65 ? 178 GLU   A OE2 1 
ATOM   1091 N  N   . VAL   A 1 151 ? 11.185  -19.359 68.867  1.00 17.50 ? 179 VAL   A N   1 
ATOM   1092 C  CA  . VAL   A 1 151 ? 11.167  -20.335 69.950  1.00 20.04 ? 179 VAL   A CA  1 
ATOM   1093 C  C   . VAL   A 1 151 ? 9.976   -20.026 70.854  1.00 20.63 ? 179 VAL   A C   1 
ATOM   1094 O  O   . VAL   A 1 151 ? 9.430   -18.924 70.839  1.00 16.43 ? 179 VAL   A O   1 
ATOM   1095 C  CB  . VAL   A 1 151 ? 12.489  -20.333 70.772  1.00 17.80 ? 179 VAL   A CB  1 
ATOM   1096 C  CG1 . VAL   A 1 151 ? 13.667  -20.654 69.877  1.00 18.89 ? 179 VAL   A CG1 1 
ATOM   1097 C  CG2 . VAL   A 1 151 ? 12.698  -18.994 71.451  1.00 21.36 ? 179 VAL   A CG2 1 
ATOM   1098 N  N   . LYS   A 1 152 ? 9.581   -21.007 71.665  1.00 19.98 ? 180 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 152 ? 8.457   -20.793 72.570  1.00 21.34 ? 180 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 152 ? 8.873   -19.932 73.756  1.00 23.14 ? 180 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 152 ? 9.928   -20.151 74.361  1.00 23.45 ? 180 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 152 ? 7.891   -22.120 73.060  1.00 19.83 ? 180 LYS   A CB  1 
ATOM   1103 C  CG  . LYS   A 1 152 ? 7.457   -23.029 71.939  1.00 17.14 ? 180 LYS   A CG  1 
ATOM   1104 C  CD  . LYS   A 1 152 ? 6.473   -24.065 72.463  1.00 26.01 ? 180 LYS   A CD  1 
ATOM   1105 C  CE  . LYS   A 1 152 ? 5.895   -24.928 71.357  1.00 26.00 ? 180 LYS   A CE  1 
ATOM   1106 N  NZ  . LYS   A 1 152 ? 4.656   -25.610 71.831  1.00 29.97 ? 180 LYS   A NZ  1 
ATOM   1107 N  N   . LEU   A 1 153 ? 8.048   -18.935 74.078  1.00 24.26 ? 181 LEU   A N   1 
ATOM   1108 C  CA  . LEU   A 1 153 ? 8.301   -18.057 75.219  1.00 26.10 ? 181 LEU   A CA  1 
ATOM   1109 C  C   . LEU   A 1 153 ? 7.472   -18.485 76.423  1.00 22.78 ? 181 LEU   A C   1 
ATOM   1110 O  O   . LEU   A 1 153 ? 8.026   -18.835 77.468  1.00 21.37 ? 181 LEU   A O   1 
ATOM   1111 C  CB  . LEU   A 1 153 ? 8.020   -16.591 74.838  1.00 20.05 ? 181 LEU   A CB  1 
ATOM   1112 C  CG  . LEU   A 1 153 ? 8.245   -15.476 75.857  1.00 18.01 ? 181 LEU   A CG  1 
ATOM   1113 C  CD1 . LEU   A 1 153 ? 9.683   -15.457 76.378  1.00 19.73 ? 181 LEU   A CD1 1 
ATOM   1114 C  CD2 . LEU   A 1 153 ? 7.879   -14.123 75.264  1.00 21.92 ? 181 LEU   A CD2 1 
ATOM   1115 N  N   . TYR   A 1 154 ? 6.148   -18.489 76.272  1.00 22.83 ? 182 TYR   A N   1 
ATOM   1116 C  CA  . TYR   A 1 154 ? 5.214   -18.980 77.271  1.00 16.05 ? 182 TYR   A CA  1 
ATOM   1117 C  C   . TYR   A 1 154 ? 3.834   -19.075 76.627  1.00 18.31 ? 182 TYR   A C   1 
ATOM   1118 O  O   . TYR   A 1 154 ? 3.482   -18.245 75.781  1.00 20.79 ? 182 TYR   A O   1 
ATOM   1119 C  CB  . TYR   A 1 154 ? 5.192   -18.075 78.520  1.00 22.98 ? 182 TYR   A CB  1 
ATOM   1120 C  CG  . TYR   A 1 154 ? 5.345   -16.567 78.282  1.00 23.54 ? 182 TYR   A CG  1 
ATOM   1121 C  CD1 . TYR   A 1 154 ? 4.380   -15.832 77.576  1.00 20.78 ? 182 TYR   A CD1 1 
ATOM   1122 C  CD2 . TYR   A 1 154 ? 6.438   -15.872 78.801  1.00 25.45 ? 182 TYR   A CD2 1 
ATOM   1123 C  CE1 . TYR   A 1 154 ? 4.516   -14.454 77.380  1.00 19.14 ? 182 TYR   A CE1 1 
ATOM   1124 C  CE2 . TYR   A 1 154 ? 6.586   -14.496 78.602  1.00 18.59 ? 182 TYR   A CE2 1 
ATOM   1125 C  CZ  . TYR   A 1 154 ? 5.624   -13.791 77.888  1.00 25.71 ? 182 TYR   A CZ  1 
ATOM   1126 O  OH  . TYR   A 1 154 ? 5.773   -12.421 77.695  1.00 20.17 ? 182 TYR   A OH  1 
ATOM   1127 N  N   . GLY   A 1 155 ? 3.065   -20.099 77.015  1.00 19.13 ? 183 GLY   A N   1 
ATOM   1128 C  CA  . GLY   A 1 155 ? 1.795   -20.342 76.347  1.00 14.50 ? 183 GLY   A CA  1 
ATOM   1129 C  C   . GLY   A 1 155 ? 2.042   -20.596 74.873  1.00 21.69 ? 183 GLY   A C   1 
ATOM   1130 O  O   . GLY   A 1 155 ? 2.988   -21.289 74.488  1.00 19.88 ? 183 GLY   A O   1 
ATOM   1131 N  N   . ASP   A 1 156 ? 1.212   -20.005 74.021  1.00 18.83 ? 184 ASP   A N   1 
ATOM   1132 C  CA  . ASP   A 1 156 ? 1.434   -20.086 72.583  1.00 19.23 ? 184 ASP   A CA  1 
ATOM   1133 C  C   . ASP   A 1 156 ? 2.103   -18.833 72.037  1.00 20.10 ? 184 ASP   A C   1 
ATOM   1134 O  O   . ASP   A 1 156 ? 2.037   -18.552 70.832  1.00 23.07 ? 184 ASP   A O   1 
ATOM   1135 C  CB  . ASP   A 1 156 ? 0.116   -20.367 71.880  1.00 18.01 ? 184 ASP   A CB  1 
ATOM   1136 C  CG  . ASP   A 1 156 ? -0.441  -21.711 72.268  1.00 26.17 ? 184 ASP   A CG  1 
ATOM   1137 O  OD1 . ASP   A 1 156 ? 0.344   -22.685 72.270  1.00 23.56 ? 184 ASP   A OD1 1 
ATOM   1138 O  OD2 . ASP   A 1 156 ? -1.633  -21.787 72.619  1.00 25.50 ? 184 ASP   A OD2 1 
ATOM   1139 N  N   . VAL   A 1 157 ? 2.753   -18.090 72.899  1.00 22.96 ? 185 VAL   A N   1 
ATOM   1140 C  CA  . VAL   A 1 157 ? 3.504   -16.915 72.502  1.00 20.10 ? 185 VAL   A CA  1 
ATOM   1141 C  C   . VAL   A 1 157 ? 4.921   -17.359 72.193  1.00 24.08 ? 185 VAL   A C   1 
ATOM   1142 O  O   . VAL   A 1 157 ? 5.557   -18.053 72.998  1.00 23.56 ? 185 VAL   A O   1 
ATOM   1143 C  CB  . VAL   A 1 157 ? 3.484   -15.862 73.617  1.00 19.92 ? 185 VAL   A CB  1 
ATOM   1144 C  CG1 . VAL   A 1 157 ? 3.979   -14.512 73.097  1.00 24.20 ? 185 VAL   A CG1 1 
ATOM   1145 C  CG2 . VAL   A 1 157 ? 2.090   -15.771 74.206  1.00 17.56 ? 185 VAL   A CG2 1 
ATOM   1146 N  N   . VAL   A 1 158 ? 5.413   -16.974 71.028  1.00 19.06 ? 186 VAL   A N   1 
ATOM   1147 C  CA  . VAL   A 1 158 ? 6.782   -17.273 70.641  1.00 19.42 ? 186 VAL   A CA  1 
ATOM   1148 C  C   . VAL   A 1 158 ? 7.623   -16.004 70.763  1.00 18.12 ? 186 VAL   A C   1 
ATOM   1149 O  O   . VAL   A 1 158 ? 7.136   -14.871 70.598  1.00 16.34 ? 186 VAL   A O   1 
ATOM   1150 C  CB  . VAL   A 1 158 ? 6.857   -17.856 69.213  1.00 14.87 ? 186 VAL   A CB  1 
ATOM   1151 C  CG1 . VAL   A 1 158 ? 6.089   -19.144 69.134  1.00 18.67 ? 186 VAL   A CG1 1 
ATOM   1152 C  CG2 . VAL   A 1 158 ? 6.342   -16.853 68.196  1.00 15.63 ? 186 VAL   A CG2 1 
ATOM   1153 N  N   . LEU   A 1 159 ? 8.884   -16.205 71.120  1.00 18.12 ? 187 LEU   A N   1 
ATOM   1154 C  CA  . LEU   A 1 159 ? 9.920   -15.184 71.005  1.00 17.80 ? 187 LEU   A CA  1 
ATOM   1155 C  C   . LEU   A 1 159 ? 10.510  -15.287 69.608  1.00 17.07 ? 187 LEU   A C   1 
ATOM   1156 O  O   . LEU   A 1 159 ? 11.067  -16.331 69.246  1.00 17.84 ? 187 LEU   A O   1 
ATOM   1157 C  CB  . LEU   A 1 159 ? 10.998  -15.410 72.064  1.00 18.77 ? 187 LEU   A CB  1 
ATOM   1158 C  CG  . LEU   A 1 159 ? 12.156  -14.422 72.155  1.00 20.91 ? 187 LEU   A CG  1 
ATOM   1159 C  CD1 . LEU   A 1 159 ? 11.623  -13.028 72.507  1.00 23.10 ? 187 LEU   A CD1 1 
ATOM   1160 C  CD2 . LEU   A 1 159 ? 13.140  -14.892 73.201  1.00 18.99 ? 187 LEU   A CD2 1 
ATOM   1161 N  N   . ARG   A 1 160 ? 10.346  -14.241 68.805  1.00 18.10 ? 188 ARG   A N   1 
ATOM   1162 C  CA  . ARG   A 1 160 ? 10.824  -14.250 67.425  1.00 19.00 ? 188 ARG   A CA  1 
ATOM   1163 C  C   . ARG   A 1 160 ? 12.134  -13.473 67.315  1.00 21.04 ? 188 ARG   A C   1 
ATOM   1164 O  O   . ARG   A 1 160 ? 12.186  -12.287 67.666  1.00 15.58 ? 188 ARG   A O   1 
ATOM   1165 C  CB  . ARG   A 1 160 ? 9.779   -13.663 66.484  1.00 17.89 ? 188 ARG   A CB  1 
ATOM   1166 C  CG  . ARG   A 1 160 ? 10.255  -13.460 65.063  1.00 18.82 ? 188 ARG   A CG  1 
ATOM   1167 C  CD  . ARG   A 1 160 ? 9.126   -12.844 64.250  1.00 18.58 ? 188 ARG   A CD  1 
ATOM   1168 N  NE  . ARG   A 1 160 ? 8.004   -13.776 64.149  1.00 21.01 ? 188 ARG   A NE  1 
ATOM   1169 C  CZ  . ARG   A 1 160 ? 6.746   -13.419 63.912  1.00 17.19 ? 188 ARG   A CZ  1 
ATOM   1170 N  NH1 . ARG   A 1 160 ? 6.431   -12.138 63.768  1.00 14.78 ? 188 ARG   A NH1 1 
ATOM   1171 N  NH2 . ARG   A 1 160 ? 5.804   -14.347 63.837  1.00 15.29 ? 188 ARG   A NH2 1 
ATOM   1172 N  N   . TYR   A 1 161 ? 13.179  -14.137 66.812  1.00 13.92 ? 189 TYR   A N   1 
ATOM   1173 C  CA  . TYR   A 1 161 ? 14.461  -13.489 66.556  1.00 17.40 ? 189 TYR   A CA  1 
ATOM   1174 C  C   . TYR   A 1 161 ? 14.514  -13.005 65.111  1.00 17.95 ? 189 TYR   A C   1 
ATOM   1175 O  O   . TYR   A 1 161 ? 14.146  -13.729 64.186  1.00 17.52 ? 189 TYR   A O   1 
ATOM   1176 C  CB  . TYR   A 1 161 ? 15.639  -14.448 66.806  1.00 18.47 ? 189 TYR   A CB  1 
ATOM   1177 C  CG  . TYR   A 1 161 ? 15.676  -15.117 68.158  1.00 14.04 ? 189 TYR   A CG  1 
ATOM   1178 C  CD1 . TYR   A 1 161 ? 15.552  -14.383 69.330  1.00 19.34 ? 189 TYR   A CD1 1 
ATOM   1179 C  CD2 . TYR   A 1 161 ? 15.845  -16.484 68.257  1.00 15.38 ? 189 TYR   A CD2 1 
ATOM   1180 C  CE1 . TYR   A 1 161 ? 15.610  -15.005 70.571  1.00 14.10 ? 189 TYR   A CE1 1 
ATOM   1181 C  CE2 . TYR   A 1 161 ? 15.890  -17.116 69.478  1.00 12.90 ? 189 TYR   A CE2 1 
ATOM   1182 C  CZ  . TYR   A 1 161 ? 15.778  -16.377 70.627  1.00 17.02 ? 189 TYR   A CZ  1 
ATOM   1183 O  OH  . TYR   A 1 161 ? 15.822  -17.020 71.837  1.00 21.50 ? 189 TYR   A OH  1 
ATOM   1184 N  N   . VAL   A 1 162 ? 15.005  -11.790 64.917  1.00 20.52 ? 190 VAL   A N   1 
ATOM   1185 C  CA  . VAL   A 1 162 ? 15.059  -11.157 63.604  1.00 19.91 ? 190 VAL   A CA  1 
ATOM   1186 C  C   . VAL   A 1 162 ? 16.447  -10.541 63.427  1.00 22.27 ? 190 VAL   A C   1 
ATOM   1187 O  O   . VAL   A 1 162 ? 16.917  -9.822  64.314  1.00 21.03 ? 190 VAL   A O   1 
ATOM   1188 C  CB  . VAL   A 1 162 ? 13.971  -10.074 63.473  1.00 21.48 ? 190 VAL   A CB  1 
ATOM   1189 C  CG1 . VAL   A 1 162 ? 14.184  -9.285  62.226  1.00 22.51 ? 190 VAL   A CG1 1 
ATOM   1190 C  CG2 . VAL   A 1 162 ? 12.560  -10.697 63.506  1.00 19.02 ? 190 VAL   A CG2 1 
ATOM   1191 N  N   . SER   A 1 163 ? 17.097  -10.803 62.285  1.00 22.46 ? 191 SER   A N   1 
ATOM   1192 C  CA  . SER   A 1 163 ? 18.409  -10.222 62.012  1.00 23.50 ? 191 SER   A CA  1 
ATOM   1193 C  C   . SER   A 1 163 ? 18.504  -9.829  60.543  1.00 27.54 ? 191 SER   A C   1 
ATOM   1194 O  O   . SER   A 1 163 ? 17.907  -10.471 59.683  1.00 22.56 ? 191 SER   A O   1 
ATOM   1195 C  CB  . SER   A 1 163 ? 19.536  -11.186 62.355  1.00 20.75 ? 191 SER   A CB  1 
ATOM   1196 O  OG  . SER   A 1 163 ? 19.735  -12.085 61.288  1.00 27.14 ? 191 SER   A OG  1 
ATOM   1197 N  N   . TYR   A 1 164 ? 19.277  -8.779  60.257  1.00 24.25 ? 192 TYR   A N   1 
ATOM   1198 C  CA  . TYR   A 1 164 ? 19.397  -8.225  58.911  1.00 29.19 ? 192 TYR   A CA  1 
ATOM   1199 C  C   . TYR   A 1 164 ? 20.849  -8.181  58.452  1.00 33.16 ? 192 TYR   A C   1 
ATOM   1200 O  O   . TYR   A 1 164 ? 21.736  -7.811  59.224  1.00 32.25 ? 192 TYR   A O   1 
ATOM   1201 C  CB  . TYR   A 1 164 ? 18.847  -6.804  58.858  1.00 37.53 ? 192 TYR   A CB  1 
ATOM   1202 C  CG  . TYR   A 1 164 ? 17.394  -6.633  59.256  1.00 33.18 ? 192 TYR   A CG  1 
ATOM   1203 C  CD1 . TYR   A 1 164 ? 16.997  -6.690  60.581  1.00 29.04 ? 192 TYR   A CD1 1 
ATOM   1204 C  CD2 . TYR   A 1 164 ? 16.433  -6.368  58.296  1.00 33.50 ? 192 TYR   A CD2 1 
ATOM   1205 C  CE1 . TYR   A 1 164 ? 15.668  -6.515  60.927  1.00 35.68 ? 192 TYR   A CE1 1 
ATOM   1206 C  CE2 . TYR   A 1 164 ? 15.117  -6.187  58.627  1.00 39.90 ? 192 TYR   A CE2 1 
ATOM   1207 C  CZ  . TYR   A 1 164 ? 14.730  -6.263  59.937  1.00 41.47 ? 192 TYR   A CZ  1 
ATOM   1208 O  OH  . TYR   A 1 164 ? 13.395  -6.080  60.226  1.00 39.59 ? 192 TYR   A OH  1 
ATOM   1209 N  N   . LYS   A 1 165 ? 21.084  -8.508  57.177  1.00 36.10 ? 193 LYS   A N   1 
ATOM   1210 C  CA  . LYS   A 1 165 ? 22.404  -8.327  56.579  1.00 40.30 ? 193 LYS   A CA  1 
ATOM   1211 C  C   . LYS   A 1 165 ? 22.836  -6.873  56.711  1.00 42.01 ? 193 LYS   A C   1 
ATOM   1212 O  O   . LYS   A 1 165 ? 23.779  -6.555  57.450  1.00 43.49 ? 193 LYS   A O   1 
ATOM   1213 C  CB  . LYS   A 1 165 ? 22.409  -8.743  55.106  1.00 30.85 ? 193 LYS   A CB  1 
ATOM   1214 N  N   . ALA   A 1 166 ? 22.150  -5.982  56.005  1.00 42.86 ? 194 ALA   A N   1 
ATOM   1215 C  CA  . ALA   A 1 166 ? 22.414  -4.556  56.142  1.00 43.46 ? 194 ALA   A CA  1 
ATOM   1216 C  C   . ALA   A 1 166 ? 21.368  -3.917  57.043  1.00 43.75 ? 194 ALA   A C   1 
ATOM   1217 O  O   . ALA   A 1 166 ? 21.457  -4.009  58.272  1.00 43.03 ? 194 ALA   A O   1 
ATOM   1218 C  CB  . ALA   A 1 166 ? 22.441  -3.880  54.782  1.00 44.64 ? 194 ALA   A CB  1 
ATOM   1219 N  N   . GLU   A 1 173 ? 12.089  -2.908  54.041  1.00 51.77 ? 201 GLU   A N   1 
ATOM   1220 C  CA  . GLU   A 1 173 ? 12.209  -2.222  55.325  1.00 58.15 ? 201 GLU   A CA  1 
ATOM   1221 C  C   . GLU   A 1 173 ? 11.843  -3.170  56.467  1.00 48.53 ? 201 GLU   A C   1 
ATOM   1222 O  O   . GLU   A 1 173 ? 12.697  -3.569  57.263  1.00 41.04 ? 201 GLU   A O   1 
ATOM   1223 C  CB  . GLU   A 1 173 ? 11.321  -0.968  55.358  1.00 57.03 ? 201 GLU   A CB  1 
ATOM   1224 N  N   . PHE   A 1 174 ? 10.564  -3.529  56.553  1.00 44.06 ? 202 PHE   A N   1 
ATOM   1225 C  CA  . PHE   A 1 174 ? 10.168  -4.488  57.569  1.00 32.79 ? 202 PHE   A CA  1 
ATOM   1226 C  C   . PHE   A 1 174 ? 10.635  -5.876  57.143  1.00 31.39 ? 202 PHE   A C   1 
ATOM   1227 O  O   . PHE   A 1 174 ? 11.610  -6.397  57.695  1.00 34.99 ? 202 PHE   A O   1 
ATOM   1228 C  CB  . PHE   A 1 174 ? 8.656   -4.440  57.811  1.00 22.41 ? 202 PHE   A CB  1 
ATOM   1229 C  CG  . PHE   A 1 174 ? 8.210   -5.290  58.965  1.00 20.73 ? 202 PHE   A CG  1 
ATOM   1230 C  CD1 . PHE   A 1 174 ? 8.571   -4.968  60.265  1.00 20.57 ? 202 PHE   A CD1 1 
ATOM   1231 C  CD2 . PHE   A 1 174 ? 7.442   -6.424  58.749  1.00 24.06 ? 202 PHE   A CD2 1 
ATOM   1232 C  CE1 . PHE   A 1 174 ? 8.179   -5.762  61.329  1.00 20.85 ? 202 PHE   A CE1 1 
ATOM   1233 C  CE2 . PHE   A 1 174 ? 7.049   -7.231  59.808  1.00 21.96 ? 202 PHE   A CE2 1 
ATOM   1234 C  CZ  . PHE   A 1 174 ? 7.418   -6.891  61.102  1.00 24.57 ? 202 PHE   A CZ  1 
ATOM   1235 N  N   . LEU   A 1 175 ? 9.973   -6.474  56.156  1.00 28.83 ? 203 LEU   A N   1 
ATOM   1236 C  CA  . LEU   A 1 175 ? 10.347  -7.796  55.685  1.00 26.89 ? 203 LEU   A CA  1 
ATOM   1237 C  C   . LEU   A 1 175 ? 10.226  -7.878  54.174  1.00 25.84 ? 203 LEU   A C   1 
ATOM   1238 O  O   . LEU   A 1 175 ? 9.386   -7.192  53.574  1.00 25.73 ? 203 LEU   A O   1 
ATOM   1239 C  CB  . LEU   A 1 175 ? 9.480   -8.895  56.320  1.00 26.76 ? 203 LEU   A CB  1 
ATOM   1240 C  CG  . LEU   A 1 175 ? 9.703   -9.248  57.785  1.00 28.56 ? 203 LEU   A CG  1 
ATOM   1241 C  CD1 . LEU   A 1 175 ? 8.731   -10.344 58.215  1.00 19.61 ? 203 LEU   A CD1 1 
ATOM   1242 C  CD2 . LEU   A 1 175 ? 11.154  -9.670  58.003  1.00 27.96 ? 203 LEU   A CD2 1 
ATOM   1243 N  N   . PRO   A 1 176 ? 11.038  -8.725  53.532  1.00 28.83 ? 204 PRO   A N   1 
ATOM   1244 C  CA  . PRO   A 1 176 ? 10.793  -9.042  52.124  1.00 32.55 ? 204 PRO   A CA  1 
ATOM   1245 C  C   . PRO   A 1 176 ? 9.378   -9.556  51.977  1.00 26.22 ? 204 PRO   A C   1 
ATOM   1246 O  O   . PRO   A 1 176 ? 8.829   -10.171 52.890  1.00 31.87 ? 204 PRO   A O   1 
ATOM   1247 C  CB  . PRO   A 1 176 ? 11.821  -10.139 51.813  1.00 35.26 ? 204 PRO   A CB  1 
ATOM   1248 C  CG  . PRO   A 1 176 ? 12.860  -10.012 52.868  1.00 30.88 ? 204 PRO   A CG  1 
ATOM   1249 C  CD  . PRO   A 1 176 ? 12.143  -9.525  54.089  1.00 33.28 ? 204 PRO   A CD  1 
ATOM   1250 N  N   . GLY   A 1 177 ? 8.778   -9.288  50.826  1.00 32.27 ? 205 GLY   A N   1 
ATOM   1251 C  CA  . GLY   A 1 177 ? 7.395   -9.652  50.613  1.00 26.69 ? 205 GLY   A CA  1 
ATOM   1252 C  C   . GLY   A 1 177 ? 6.395   -8.666  51.159  1.00 27.87 ? 205 GLY   A C   1 
ATOM   1253 O  O   . GLY   A 1 177 ? 5.212   -8.756  50.810  1.00 27.18 ? 205 GLY   A O   1 
ATOM   1254 N  N   . PHE   A 1 178 ? 6.822   -7.739  52.015  1.00 25.39 ? 206 PHE   A N   1 
ATOM   1255 C  CA  . PHE   A 1 178 ? 5.981   -6.634  52.448  1.00 23.99 ? 206 PHE   A CA  1 
ATOM   1256 C  C   . PHE   A 1 178 ? 6.183   -5.434  51.534  1.00 23.73 ? 206 PHE   A C   1 
ATOM   1257 O  O   . PHE   A 1 178 ? 7.291   -5.176  51.062  1.00 25.76 ? 206 PHE   A O   1 
ATOM   1258 C  CB  . PHE   A 1 178 ? 6.288   -6.238  53.895  1.00 27.16 ? 206 PHE   A CB  1 
ATOM   1259 C  CG  . PHE   A 1 178 ? 5.614   -7.107  54.929  1.00 23.73 ? 206 PHE   A CG  1 
ATOM   1260 C  CD1 . PHE   A 1 178 ? 6.082   -8.388  55.196  1.00 25.27 ? 206 PHE   A CD1 1 
ATOM   1261 C  CD2 . PHE   A 1 178 ? 4.516   -6.636  55.643  1.00 21.46 ? 206 PHE   A CD2 1 
ATOM   1262 C  CE1 . PHE   A 1 178 ? 5.472   -9.189  56.152  1.00 21.75 ? 206 PHE   A CE1 1 
ATOM   1263 C  CE2 . PHE   A 1 178 ? 3.903   -7.431  56.607  1.00 21.10 ? 206 PHE   A CE2 1 
ATOM   1264 C  CZ  . PHE   A 1 178 ? 4.381   -8.710  56.851  1.00 23.34 ? 206 PHE   A CZ  1 
ATOM   1265 N  N   . GLU   A 1 179 ? 5.100   -4.719  51.268  1.00 22.32 ? 207 GLU   A N   1 
ATOM   1266 C  CA  . GLU   A 1 179 ? 5.152   -3.468  50.526  1.00 30.34 ? 207 GLU   A CA  1 
ATOM   1267 C  C   . GLU   A 1 179 ? 5.009   -2.291  51.466  1.00 32.83 ? 207 GLU   A C   1 
ATOM   1268 O  O   . GLU   A 1 179 ? 4.250   -2.355  52.438  1.00 29.01 ? 207 GLU   A O   1 
ATOM   1269 C  CB  . GLU   A 1 179 ? 4.033   -3.343  49.500  1.00 36.15 ? 207 GLU   A CB  1 
ATOM   1270 C  CG  . GLU   A 1 179 ? 4.165   -4.123  48.234  1.00 37.13 ? 207 GLU   A CG  1 
ATOM   1271 C  CD  . GLU   A 1 179 ? 3.183   -3.605  47.195  1.00 42.49 ? 207 GLU   A CD  1 
ATOM   1272 O  OE1 . GLU   A 1 179 ? 2.443   -2.638  47.512  1.00 42.40 ? 207 GLU   A OE1 1 
ATOM   1273 O  OE2 . GLU   A 1 179 ? 3.144   -4.158  46.074  1.00 45.37 ? 207 GLU   A OE2 1 
ATOM   1274 N  N   . ARG   A 1 180 ? 5.699   -1.200  51.138  1.00 31.64 ? 208 ARG   A N   1 
ATOM   1275 C  CA  . ARG   A 1 180 ? 5.363   0.082   51.732  1.00 36.41 ? 208 ARG   A CA  1 
ATOM   1276 C  C   . ARG   A 1 180 ? 4.058   0.596   51.139  1.00 34.49 ? 208 ARG   A C   1 
ATOM   1277 O  O   . ARG   A 1 180 ? 3.834   0.527   49.928  1.00 43.18 ? 208 ARG   A O   1 
ATOM   1278 C  CB  . ARG   A 1 180 ? 6.485   1.103   51.491  1.00 38.84 ? 208 ARG   A CB  1 
ATOM   1279 C  CG  . ARG   A 1 180 ? 7.662   0.969   52.404  1.00 49.53 ? 208 ARG   A CG  1 
ATOM   1280 C  CD  . ARG   A 1 180 ? 7.373   1.779   53.621  1.00 57.00 ? 208 ARG   A CD  1 
ATOM   1281 N  NE  . ARG   A 1 180 ? 8.037   3.070   53.506  1.00 61.20 ? 208 ARG   A NE  1 
ATOM   1282 C  CZ  . ARG   A 1 180 ? 9.312   3.285   53.811  1.00 61.26 ? 208 ARG   A CZ  1 
ATOM   1283 N  NH1 . ARG   A 1 180 ? 10.064  2.261   54.251  1.00 60.38 ? 208 ARG   A NH1 1 
ATOM   1284 N  NH2 . ARG   A 1 180 ? 9.814   4.506   53.667  1.00 58.40 ? 208 ARG   A NH2 1 
ATOM   1285 N  N   . VAL   A 1 181 ? 3.201   1.133   51.981  1.00 33.96 ? 209 VAL   A N   1 
ATOM   1286 C  CA  . VAL   A 1 181 ? 2.018   1.805   51.471  1.00 37.89 ? 209 VAL   A CA  1 
ATOM   1287 C  C   . VAL   A 1 181 ? 2.392   3.258   51.214  1.00 42.64 ? 209 VAL   A C   1 
ATOM   1288 O  O   . VAL   A 1 181 ? 3.112   3.881   52.006  1.00 40.15 ? 209 VAL   A O   1 
ATOM   1289 C  CB  . VAL   A 1 181 ? 0.811   1.661   52.425  1.00 35.28 ? 209 VAL   A CB  1 
ATOM   1290 C  CG1 . VAL   A 1 181 ? 1.016   0.551   53.460  1.00 26.36 ? 209 VAL   A CG1 1 
ATOM   1291 C  CG2 . VAL   A 1 181 ? 0.434   2.958   53.073  1.00 34.13 ? 209 VAL   A CG2 1 
ATOM   1292 N  N   . GLU   A 1 182 ? 1.961   3.771   50.068  1.00 47.68 ? 210 GLU   A N   1 
ATOM   1293 C  CA  . GLU   A 1 182 ? 2.292   5.128   49.664  1.00 56.45 ? 210 GLU   A CA  1 
ATOM   1294 C  C   . GLU   A 1 182 ? 1.475   6.143   50.453  1.00 52.53 ? 210 GLU   A C   1 
ATOM   1295 O  O   . GLU   A 1 182 ? 0.334   5.883   50.859  1.00 54.77 ? 210 GLU   A O   1 
ATOM   1296 C  CB  . GLU   A 1 182 ? 2.045   5.308   48.165  1.00 56.12 ? 210 GLU   A CB  1 
ATOM   1297 N  N   . ASP   A 1 183 ? 2.064   7.318   50.651  1.00 56.76 ? 211 ASP   A N   1 
ATOM   1298 C  CA  . ASP   A 1 183 ? 1.421   8.382   51.419  1.00 49.51 ? 211 ASP   A CA  1 
ATOM   1299 C  C   . ASP   A 1 183 ? 0.178   8.862   50.675  1.00 53.93 ? 211 ASP   A C   1 
ATOM   1300 O  O   . ASP   A 1 183 ? 0.251   9.720   49.791  1.00 50.66 ? 211 ASP   A O   1 
ATOM   1301 C  CB  . ASP   A 1 183 ? 2.401   9.518   51.670  1.00 47.10 ? 211 ASP   A CB  1 
ATOM   1302 N  N   . ALA   A 1 184 ? -0.963  8.277   51.035  1.00 49.77 ? 212 ALA   A N   1 
ATOM   1303 C  CA  . ALA   A 1 184 ? -2.294  8.673   50.597  1.00 50.87 ? 212 ALA   A CA  1 
ATOM   1304 C  C   . ALA   A 1 184 ? -3.242  7.724   51.308  1.00 49.98 ? 212 ALA   A C   1 
ATOM   1305 O  O   . ALA   A 1 184 ? -4.228  8.142   51.933  1.00 45.10 ? 212 ALA   A O   1 
ATOM   1306 C  CB  . ALA   A 1 184 ? -2.454  8.590   49.077  1.00 49.83 ? 212 ALA   A CB  1 
ATOM   1307 N  N   . SER   A 1 185 ? -2.917  6.433   51.227  1.00 52.21 ? 213 SER   A N   1 
ATOM   1308 C  CA  . SER   A 1 185 ? -3.523  5.450   52.109  1.00 48.28 ? 213 SER   A CA  1 
ATOM   1309 C  C   . SER   A 1 185 ? -2.908  5.476   53.500  1.00 48.49 ? 213 SER   A C   1 
ATOM   1310 O  O   . SER   A 1 185 ? -3.488  4.896   54.424  1.00 41.76 ? 213 SER   A O   1 
ATOM   1311 C  CB  . SER   A 1 185 ? -3.372  4.039   51.506  1.00 46.75 ? 213 SER   A CB  1 
ATOM   1312 O  OG  . SER   A 1 185 ? -3.790  4.025   50.146  1.00 50.68 ? 213 SER   A OG  1 
ATOM   1313 N  N   . SER   A 1 186 ? -1.759  6.136   53.666  1.00 45.15 ? 214 SER   A N   1 
ATOM   1314 C  CA  . SER   A 1 186 ? -1.052  6.208   54.942  1.00 36.50 ? 214 SER   A CA  1 
ATOM   1315 C  C   . SER   A 1 186 ? -1.204  7.612   55.512  1.00 33.06 ? 214 SER   A C   1 
ATOM   1316 O  O   . SER   A 1 186 ? -0.428  8.514   55.197  1.00 38.91 ? 214 SER   A O   1 
ATOM   1317 C  CB  . SER   A 1 186 ? 0.413   5.858   54.772  1.00 37.62 ? 214 SER   A CB  1 
ATOM   1318 O  OG  . SER   A 1 186 ? 1.088   5.809   56.015  1.00 31.47 ? 214 SER   A OG  1 
ATOM   1319 N  N   . PHE   A 1 187 ? -2.202  7.786   56.357  1.00 28.44 ? 215 PHE   A N   1 
ATOM   1320 C  CA  . PHE   A 1 187 ? -2.374  9.038   57.068  1.00 26.70 ? 215 PHE   A CA  1 
ATOM   1321 C  C   . PHE   A 1 187 ? -1.349  9.169   58.183  1.00 28.38 ? 215 PHE   A C   1 
ATOM   1322 O  O   . PHE   A 1 187 ? -1.301  8.305   59.071  1.00 22.20 ? 215 PHE   A O   1 
ATOM   1323 C  CB  . PHE   A 1 187 ? -3.768  9.145   57.645  1.00 24.50 ? 215 PHE   A CB  1 
ATOM   1324 C  CG  . PHE   A 1 187 ? -4.125  10.528  58.059  1.00 21.94 ? 215 PHE   A CG  1 
ATOM   1325 C  CD1 . PHE   A 1 187 ? -3.727  11.028  59.287  1.00 20.48 ? 215 PHE   A CD1 1 
ATOM   1326 C  CD2 . PHE   A 1 187 ? -4.842  11.341  57.208  1.00 29.83 ? 215 PHE   A CD2 1 
ATOM   1327 C  CE1 . PHE   A 1 187 ? -4.043  12.293  59.660  1.00 26.30 ? 215 PHE   A CE1 1 
ATOM   1328 C  CE2 . PHE   A 1 187 ? -5.169  12.628  57.581  1.00 26.74 ? 215 PHE   A CE2 1 
ATOM   1329 C  CZ  . PHE   A 1 187 ? -4.763  13.103  58.803  1.00 30.42 ? 215 PHE   A CZ  1 
ATOM   1330 N  N   . PRO   A 1 188 ? -0.559  10.256  58.221  1.00 31.49 ? 216 PRO   A N   1 
ATOM   1331 C  CA  . PRO   A 1 188 ? 0.566   10.323  59.161  1.00 26.14 ? 216 PRO   A CA  1 
ATOM   1332 C  C   . PRO   A 1 188 ? 0.127   10.548  60.592  1.00 24.53 ? 216 PRO   A C   1 
ATOM   1333 O  O   . PRO   A 1 188 ? 0.560   11.524  61.215  1.00 23.61 ? 216 PRO   A O   1 
ATOM   1334 C  CB  . PRO   A 1 188 ? 1.371   11.521  58.647  1.00 27.56 ? 216 PRO   A CB  1 
ATOM   1335 C  CG  . PRO   A 1 188 ? 0.341   12.428  58.107  1.00 24.28 ? 216 PRO   A CG  1 
ATOM   1336 C  CD  . PRO   A 1 188 ? -0.754  11.541  57.518  1.00 27.40 ? 216 PRO   A CD  1 
ATOM   1337 N  N   . LEU   A 1 189 ? -0.729  9.671   61.114  1.00 21.70 ? 217 LEU   A N   1 
ATOM   1338 C  CA  . LEU   A 1 189 ? -1.164  9.780   62.498  1.00 20.09 ? 217 LEU   A CA  1 
ATOM   1339 C  C   . LEU   A 1 189 ? 0.012   9.578   63.441  1.00 21.18 ? 217 LEU   A C   1 
ATOM   1340 O  O   . LEU   A 1 189 ? 0.924   8.802   63.161  1.00 23.27 ? 217 LEU   A O   1 
ATOM   1341 C  CB  . LEU   A 1 189 ? -2.234  8.731   62.808  1.00 22.97 ? 217 LEU   A CB  1 
ATOM   1342 C  CG  . LEU   A 1 189 ? -3.652  8.976   62.300  1.00 24.57 ? 217 LEU   A CG  1 
ATOM   1343 C  CD1 . LEU   A 1 189 ? -4.498  7.753   62.559  1.00 20.42 ? 217 LEU   A CD1 1 
ATOM   1344 C  CD2 . LEU   A 1 189 ? -4.239  10.235  62.957  1.00 26.20 ? 217 LEU   A CD2 1 
ATOM   1345 N  N   . ASP   A 1 190 ? -0.061  10.226  64.603  1.00 19.30 ? 218 ASP   A N   1 
ATOM   1346 C  CA  . ASP   A 1 190 ? 1.029   10.257  65.568  1.00 19.10 ? 218 ASP   A CA  1 
ATOM   1347 C  C   . ASP   A 1 190 ? 0.545   10.894  66.854  1.00 25.63 ? 218 ASP   A C   1 
ATOM   1348 O  O   . ASP   A 1 190 ? 0.306   12.108  66.883  1.00 27.82 ? 218 ASP   A O   1 
ATOM   1349 C  CB  . ASP   A 1 190 ? 2.225   11.042  65.001  1.00 25.27 ? 218 ASP   A CB  1 
ATOM   1350 C  CG  . ASP   A 1 190 ? 3.409   11.142  65.981  1.00 17.87 ? 218 ASP   A CG  1 
ATOM   1351 O  OD1 . ASP   A 1 190 ? 3.360   10.559  67.086  1.00 17.69 ? 218 ASP   A OD1 1 
ATOM   1352 O  OD2 . ASP   A 1 190 ? 4.408   11.807  65.626  1.00 24.47 ? 218 ASP   A OD2 1 
ATOM   1353 N  N   . TYR   A 1 191 ? 0.393   10.115  67.926  1.00 17.78 ? 219 TYR   A N   1 
ATOM   1354 C  CA  . TYR   A 1 191 ? 0.029   10.705  69.210  1.00 22.06 ? 219 TYR   A CA  1 
ATOM   1355 C  C   . TYR   A 1 191 ? 1.206   10.752  70.173  1.00 22.71 ? 219 TYR   A C   1 
ATOM   1356 O  O   . TYR   A 1 191 ? 1.005   11.004  71.366  1.00 23.23 ? 219 TYR   A O   1 
ATOM   1357 C  CB  . TYR   A 1 191 ? -1.147  9.961   69.871  1.00 24.04 ? 219 TYR   A CB  1 
ATOM   1358 C  CG  . TYR   A 1 191 ? -2.370  9.727   68.987  1.00 21.21 ? 219 TYR   A CG  1 
ATOM   1359 C  CD1 . TYR   A 1 191 ? -2.593  10.480  67.838  1.00 18.66 ? 219 TYR   A CD1 1 
ATOM   1360 C  CD2 . TYR   A 1 191 ? -3.299  8.741   69.317  1.00 22.83 ? 219 TYR   A CD2 1 
ATOM   1361 C  CE1 . TYR   A 1 191 ? -3.690  10.245  67.025  1.00 19.77 ? 219 TYR   A CE1 1 
ATOM   1362 C  CE2 . TYR   A 1 191 ? -4.426  8.508   68.520  1.00 21.00 ? 219 TYR   A CE2 1 
ATOM   1363 C  CZ  . TYR   A 1 191 ? -4.602  9.261   67.370  1.00 24.27 ? 219 TYR   A CZ  1 
ATOM   1364 O  OH  . TYR   A 1 191 ? -5.682  9.031   66.565  1.00 20.94 ? 219 TYR   A OH  1 
ATOM   1365 N  N   . GLY   A 1 192 ? 2.425   10.508  69.691  1.00 25.56 ? 220 GLY   A N   1 
ATOM   1366 C  CA  . GLY   A 1 192 ? 3.617   10.609  70.510  1.00 22.65 ? 220 GLY   A CA  1 
ATOM   1367 C  C   . GLY   A 1 192 ? 4.220   9.301   70.988  1.00 24.16 ? 220 GLY   A C   1 
ATOM   1368 O  O   . GLY   A 1 192 ? 5.192   9.342   71.753  1.00 23.10 ? 220 GLY   A O   1 
ATOM   1369 N  N   . ILE   A 1 193 ? 3.689   8.144   70.570  1.00 18.56 ? 221 ILE   A N   1 
ATOM   1370 C  CA  . ILE   A 1 193 ? 4.242   6.859   70.992  1.00 20.18 ? 221 ILE   A CA  1 
ATOM   1371 C  C   . ILE   A 1 193 ? 5.447   6.519   70.127  1.00 19.11 ? 221 ILE   A C   1 
ATOM   1372 O  O   . ILE   A 1 193 ? 5.411   6.684   68.898  1.00 17.91 ? 221 ILE   A O   1 
ATOM   1373 C  CB  . ILE   A 1 193 ? 3.174   5.752   70.928  1.00 16.82 ? 221 ILE   A CB  1 
ATOM   1374 C  CG1 . ILE   A 1 193 ? 2.075   6.025   71.950  1.00 21.10 ? 221 ILE   A CG1 1 
ATOM   1375 C  CG2 . ILE   A 1 193 ? 3.810   4.347   71.208  1.00 15.79 ? 221 ILE   A CG2 1 
ATOM   1376 C  CD1 . ILE   A 1 193 ? 0.954   4.983   71.961  1.00 15.64 ? 221 ILE   A CD1 1 
ATOM   1377 N  N   . ARG   A 1 194 ? 6.526   6.037   70.766  1.00 19.19 ? 222 ARG   A N   1 
ATOM   1378 C  CA  . ARG   A 1 194 ? 7.822   5.992   70.091  1.00 17.79 ? 222 ARG   A CA  1 
ATOM   1379 C  C   . ARG   A 1 194 ? 8.512   4.630   70.096  1.00 19.78 ? 222 ARG   A C   1 
ATOM   1380 O  O   . ARG   A 1 194 ? 9.289   4.333   69.181  1.00 18.68 ? 222 ARG   A O   1 
ATOM   1381 C  CB  . ARG   A 1 194 ? 8.753   7.047   70.707  1.00 19.26 ? 222 ARG   A CB  1 
ATOM   1382 C  CG  . ARG   A 1 194 ? 8.361   8.486   70.369  1.00 18.45 ? 222 ARG   A CG  1 
ATOM   1383 C  CD  . ARG   A 1 194 ? 8.467   8.732   68.877  1.00 15.27 ? 222 ARG   A CD  1 
ATOM   1384 N  NE  . ARG   A 1 194 ? 8.084   10.091  68.481  1.00 23.33 ? 222 ARG   A NE  1 
ATOM   1385 C  CZ  . ARG   A 1 194 ? 6.853   10.468  68.108  1.00 23.52 ? 222 ARG   A CZ  1 
ATOM   1386 N  NH1 . ARG   A 1 194 ? 5.845   9.604   68.065  1.00 15.58 ? 222 ARG   A NH1 1 
ATOM   1387 N  NH2 . ARG   A 1 194 ? 6.632   11.724  67.758  1.00 23.35 ? 222 ARG   A NH2 1 
ATOM   1388 N  N   . ARG   A 1 195 ? 8.260   3.791   71.096  1.00 14.00 ? 223 ARG   A N   1 
ATOM   1389 C  CA  . ARG   A 1 195 ? 8.934   2.497   71.096  1.00 18.73 ? 223 ARG   A CA  1 
ATOM   1390 C  C   . ARG   A 1 195 ? 8.268   1.589   72.119  1.00 16.55 ? 223 ARG   A C   1 
ATOM   1391 O  O   . ARG   A 1 195 ? 7.495   2.036   72.967  1.00 15.37 ? 223 ARG   A O   1 
ATOM   1392 C  CB  . ARG   A 1 195 ? 10.441  2.641   71.381  1.00 17.65 ? 223 ARG   A CB  1 
ATOM   1393 C  CG  . ARG   A 1 195 ? 10.814  2.910   72.835  1.00 21.33 ? 223 ARG   A CG  1 
ATOM   1394 C  CD  . ARG   A 1 195 ? 12.345  3.045   72.990  1.00 21.35 ? 223 ARG   A CD  1 
ATOM   1395 N  NE  . ARG   A 1 195 ? 12.733  3.191   74.389  1.00 25.03 ? 223 ARG   A NE  1 
ATOM   1396 C  CZ  . ARG   A 1 195 ? 12.905  2.176   75.241  1.00 33.00 ? 223 ARG   A CZ  1 
ATOM   1397 N  NH1 . ARG   A 1 195 ? 12.726  0.923   74.838  1.00 28.19 ? 223 ARG   A NH1 1 
ATOM   1398 N  NH2 . ARG   A 1 195 ? 13.259  2.406   76.504  1.00 32.38 ? 223 ARG   A NH2 1 
ATOM   1399 N  N   . LEU   A 1 196 ? 8.597   0.302   72.040  1.00 18.22 ? 224 LEU   A N   1 
ATOM   1400 C  CA  . LEU   A 1 196 ? 8.069   -0.689  72.969  1.00 18.11 ? 224 LEU   A CA  1 
ATOM   1401 C  C   . LEU   A 1 196 ? 8.966   -0.754  74.195  1.00 19.23 ? 224 LEU   A C   1 
ATOM   1402 O  O   . LEU   A 1 196 ? 10.160  -1.031  74.079  1.00 22.76 ? 224 LEU   A O   1 
ATOM   1403 C  CB  . LEU   A 1 196 ? 7.977   -2.065  72.312  1.00 14.95 ? 224 LEU   A CB  1 
ATOM   1404 C  CG  . LEU   A 1 196 ? 7.560   -3.209  73.241  1.00 18.02 ? 224 LEU   A CG  1 
ATOM   1405 C  CD1 . LEU   A 1 196 ? 6.186   -2.972  73.840  1.00 17.11 ? 224 LEU   A CD1 1 
ATOM   1406 C  CD2 . LEU   A 1 196 ? 7.598   -4.536  72.496  1.00 17.74 ? 224 LEU   A CD2 1 
ATOM   1407 N  N   . ASP   A 1 197 ? 8.392   -0.540  75.368  1.00 20.41 ? 225 ASP   A N   1 
ATOM   1408 C  CA  . ASP   A 1 197 ? 9.237   -0.483  76.547  1.00 15.88 ? 225 ASP   A CA  1 
ATOM   1409 C  C   . ASP   A 1 197 ? 9.421   -1.845  77.194  1.00 21.42 ? 225 ASP   A C   1 
ATOM   1410 O  O   . ASP   A 1 197 ? 10.549  -2.227  77.526  1.00 22.10 ? 225 ASP   A O   1 
ATOM   1411 C  CB  . ASP   A 1 197 ? 8.663   0.493   77.560  1.00 19.36 ? 225 ASP   A CB  1 
ATOM   1412 C  CG  . ASP   A 1 197 ? 9.566   0.668   78.728  1.00 21.40 ? 225 ASP   A CG  1 
ATOM   1413 O  OD1 . ASP   A 1 197 ? 10.426  1.568   78.655  1.00 23.25 ? 225 ASP   A OD1 1 
ATOM   1414 O  OD2 . ASP   A 1 197 ? 9.439   -0.109  79.699  1.00 23.67 ? 225 ASP   A OD2 1 
ATOM   1415 N  N   . HIS   A 1 198 ? 8.339   -2.603  77.341  1.00 20.65 ? 226 HIS   A N   1 
ATOM   1416 C  CA  . HIS   A 1 198 ? 8.423   -3.958  77.854  1.00 18.50 ? 226 HIS   A CA  1 
ATOM   1417 C  C   . HIS   A 1 198 ? 7.133   -4.704  77.526  1.00 23.70 ? 226 HIS   A C   1 
ATOM   1418 O  O   . HIS   A 1 198 ? 6.078   -4.100  77.297  1.00 15.87 ? 226 HIS   A O   1 
ATOM   1419 C  CB  . HIS   A 1 198 ? 8.704   -3.951  79.361  1.00 18.52 ? 226 HIS   A CB  1 
ATOM   1420 C  CG  . HIS   A 1 198 ? 7.697   -3.193  80.172  1.00 20.57 ? 226 HIS   A CG  1 
ATOM   1421 N  ND1 . HIS   A 1 198 ? 7.880   -1.879  80.549  1.00 23.52 ? 226 HIS   A ND1 1 
ATOM   1422 C  CD2 . HIS   A 1 198 ? 6.526   -3.583  80.731  1.00 25.69 ? 226 HIS   A CD2 1 
ATOM   1423 C  CE1 . HIS   A 1 198 ? 6.868   -1.492  81.302  1.00 20.07 ? 226 HIS   A CE1 1 
ATOM   1424 N  NE2 . HIS   A 1 198 ? 6.024   -2.503  81.416  1.00 26.91 ? 226 HIS   A NE2 1 
ATOM   1425 N  N   . ALA   A 1 199 ? 7.243   -6.029  77.482  1.00 22.29 ? 227 ALA   A N   1 
ATOM   1426 C  CA  . ALA   A 1 199 ? 6.115   -6.915  77.207  1.00 21.52 ? 227 ALA   A CA  1 
ATOM   1427 C  C   . ALA   A 1 199 ? 6.007   -7.903  78.353  1.00 22.59 ? 227 ALA   A C   1 
ATOM   1428 O  O   . ALA   A 1 199 ? 7.001   -8.544  78.707  1.00 25.25 ? 227 ALA   A O   1 
ATOM   1429 C  CB  . ALA   A 1 199 ? 6.295   -7.662  75.885  1.00 21.51 ? 227 ALA   A CB  1 
ATOM   1430 N  N   . VAL   A 1 200 ? 4.810   -8.038  78.922  1.00 18.60 ? 228 VAL   A N   1 
ATOM   1431 C  CA  . VAL   A 1 200 ? 4.606   -8.760  80.175  1.00 18.84 ? 228 VAL   A CA  1 
ATOM   1432 C  C   . VAL   A 1 200 ? 3.784   -10.015 79.931  1.00 22.66 ? 228 VAL   A C   1 
ATOM   1433 O  O   . VAL   A 1 200 ? 2.719   -9.949  79.306  1.00 23.22 ? 228 VAL   A O   1 
ATOM   1434 C  CB  . VAL   A 1 200 ? 3.900   -7.876  81.201  1.00 19.58 ? 228 VAL   A CB  1 
ATOM   1435 C  CG1 . VAL   A 1 200 ? 3.561   -8.699  82.428  1.00 19.28 ? 228 VAL   A CG1 1 
ATOM   1436 C  CG2 . VAL   A 1 200 ? 4.779   -6.661  81.517  1.00 23.50 ? 228 VAL   A CG2 1 
ATOM   1437 N  N   . GLY   A 1 201 ? 4.234   -11.136 80.487  1.00 20.47 ? 229 GLY   A N   1 
ATOM   1438 C  CA  . GLY   A 1 201 ? 3.564   -12.415 80.322  1.00 22.01 ? 229 GLY   A CA  1 
ATOM   1439 C  C   . GLY   A 1 201 ? 2.904   -12.862 81.608  1.00 20.42 ? 229 GLY   A C   1 
ATOM   1440 O  O   . GLY   A 1 201 ? 3.461   -12.692 82.694  1.00 20.27 ? 229 GLY   A O   1 
ATOM   1441 N  N   . ASN   A 1 202 ? 1.709   -13.435 81.489  1.00 20.27 ? 230 ASN   A N   1 
ATOM   1442 C  CA  . ASN   A 1 202 ? 1.033   -14.044 82.626  1.00 19.60 ? 230 ASN   A CA  1 
ATOM   1443 C  C   . ASN   A 1 202 ? 1.194   -15.548 82.524  1.00 16.92 ? 230 ASN   A C   1 
ATOM   1444 O  O   . ASN   A 1 202 ? 1.022   -16.114 81.444  1.00 23.30 ? 230 ASN   A O   1 
ATOM   1445 C  CB  . ASN   A 1 202 ? -0.447  -13.662 82.684  1.00 20.90 ? 230 ASN   A CB  1 
ATOM   1446 C  CG  . ASN   A 1 202 ? -0.674  -12.330 83.353  1.00 21.64 ? 230 ASN   A CG  1 
ATOM   1447 O  OD1 . ASN   A 1 202 ? 0.249   -11.735 83.911  1.00 24.40 ? 230 ASN   A OD1 1 
ATOM   1448 N  ND2 . ASN   A 1 202 ? -1.909  -11.850 83.310  1.00 23.45 ? 230 ASN   A ND2 1 
ATOM   1449 N  N   . VAL   A 1 203 ? 1.527   -16.188 83.642  1.00 23.03 ? 231 VAL   A N   1 
ATOM   1450 C  CA  . VAL   A 1 203 ? 1.918   -17.601 83.643  1.00 19.94 ? 231 VAL   A CA  1 
ATOM   1451 C  C   . VAL   A 1 203 ? 1.368   -18.268 84.895  1.00 25.00 ? 231 VAL   A C   1 
ATOM   1452 O  O   . VAL   A 1 203 ? 1.162   -17.620 85.930  1.00 24.45 ? 231 VAL   A O   1 
ATOM   1453 C  CB  . VAL   A 1 203 ? 3.469   -17.755 83.584  1.00 23.51 ? 231 VAL   A CB  1 
ATOM   1454 C  CG1 . VAL   A 1 203 ? 4.129   -17.612 84.959  1.00 21.48 ? 231 VAL   A CG1 1 
ATOM   1455 C  CG2 . VAL   A 1 203 ? 3.895   -19.001 82.886  1.00 29.85 ? 231 VAL   A CG2 1 
ATOM   1456 N  N   . PRO   A 1 204 ? 1.079   -19.576 84.818  1.00 24.98 ? 232 PRO   A N   1 
ATOM   1457 C  CA  . PRO   A 1 204 ? 0.573   -20.256 86.026  1.00 23.91 ? 232 PRO   A CA  1 
ATOM   1458 C  C   . PRO   A 1 204 ? 1.594   -20.359 87.147  1.00 25.71 ? 232 PRO   A C   1 
ATOM   1459 O  O   . PRO   A 1 204 ? 1.212   -20.256 88.319  1.00 33.09 ? 232 PRO   A O   1 
ATOM   1460 C  CB  . PRO   A 1 204 ? 0.143   -21.640 85.507  1.00 29.04 ? 232 PRO   A CB  1 
ATOM   1461 C  CG  . PRO   A 1 204 ? 0.767   -21.780 84.160  1.00 29.01 ? 232 PRO   A CG  1 
ATOM   1462 C  CD  . PRO   A 1 204 ? 0.896   -20.395 83.612  1.00 22.64 ? 232 PRO   A CD  1 
ATOM   1463 N  N   . GLU   A 1 205 ? 2.875   -20.566 86.832  1.00 27.71 ? 233 GLU   A N   1 
ATOM   1464 C  CA  . GLU   A 1 205 ? 3.934   -20.675 87.837  1.00 28.14 ? 233 GLU   A CA  1 
ATOM   1465 C  C   . GLU   A 1 205 ? 5.135   -19.854 87.392  1.00 25.11 ? 233 GLU   A C   1 
ATOM   1466 O  O   . GLU   A 1 205 ? 5.696   -20.109 86.322  1.00 21.88 ? 233 GLU   A O   1 
ATOM   1467 C  CB  . GLU   A 1 205 ? 4.354   -22.131 88.052  1.00 30.96 ? 233 GLU   A CB  1 
ATOM   1468 C  CG  . GLU   A 1 205 ? 3.216   -23.107 88.286  1.00 33.32 ? 233 GLU   A CG  1 
ATOM   1469 C  CD  . GLU   A 1 205 ? 3.711   -24.521 88.541  1.00 41.90 ? 233 GLU   A CD  1 
ATOM   1470 O  OE1 . GLU   A 1 205 ? 3.774   -24.920 89.723  1.00 49.01 ? 233 GLU   A OE1 1 
ATOM   1471 O  OE2 . GLU   A 1 205 ? 4.055   -25.226 87.562  1.00 40.88 ? 233 GLU   A OE2 1 
ATOM   1472 N  N   . LEU   A 1 206 ? 5.549   -18.894 88.224  1.00 24.78 ? 234 LEU   A N   1 
ATOM   1473 C  CA  . LEU   A 1 206 ? 6.659   -18.015 87.860  1.00 25.92 ? 234 LEU   A CA  1 
ATOM   1474 C  C   . LEU   A 1 206 ? 7.986   -18.772 87.804  1.00 24.89 ? 234 LEU   A C   1 
ATOM   1475 O  O   . LEU   A 1 206 ? 8.705   -18.701 86.800  1.00 26.14 ? 234 LEU   A O   1 
ATOM   1476 C  CB  . LEU   A 1 206 ? 6.740   -16.847 88.846  1.00 28.63 ? 234 LEU   A CB  1 
ATOM   1477 C  CG  . LEU   A 1 206 ? 7.689   -15.677 88.560  1.00 27.78 ? 234 LEU   A CG  1 
ATOM   1478 C  CD1 . LEU   A 1 206 ? 7.532   -15.174 87.141  1.00 26.21 ? 234 LEU   A CD1 1 
ATOM   1479 C  CD2 . LEU   A 1 206 ? 7.441   -14.536 89.529  1.00 27.21 ? 234 LEU   A CD2 1 
ATOM   1480 N  N   . GLY   A 1 207 ? 8.319   -19.509 88.869  1.00 31.72 ? 235 GLY   A N   1 
ATOM   1481 C  CA  . GLY   A 1 207 ? 9.567   -20.245 88.974  1.00 20.35 ? 235 GLY   A CA  1 
ATOM   1482 C  C   . GLY   A 1 207 ? 9.993   -20.913 87.684  1.00 26.14 ? 235 GLY   A C   1 
ATOM   1483 O  O   . GLY   A 1 207 ? 10.993  -20.536 87.064  1.00 26.92 ? 235 GLY   A O   1 
ATOM   1484 N  N   . PRO   A 1 208 ? 9.216   -21.905 87.230  1.00 29.00 ? 236 PRO   A N   1 
ATOM   1485 C  CA  . PRO   A 1 208 ? 9.611   -22.626 86.007  1.00 25.70 ? 236 PRO   A CA  1 
ATOM   1486 C  C   . PRO   A 1 208 ? 9.625   -21.752 84.765  1.00 25.54 ? 236 PRO   A C   1 
ATOM   1487 O  O   . PRO   A 1 208 ? 10.465  -21.953 83.880  1.00 25.78 ? 236 PRO   A O   1 
ATOM   1488 C  CB  . PRO   A 1 208 ? 8.560   -23.739 85.901  1.00 25.22 ? 236 PRO   A CB  1 
ATOM   1489 C  CG  . PRO   A 1 208 ? 7.986   -23.870 87.272  1.00 33.87 ? 236 PRO   A CG  1 
ATOM   1490 C  CD  . PRO   A 1 208 ? 8.053   -22.517 87.893  1.00 22.12 ? 236 PRO   A CD  1 
ATOM   1491 N  N   . ALA   A 1 209 ? 8.691   -20.805 84.658  1.00 26.88 ? 237 ALA   A N   1 
ATOM   1492 C  CA  . ALA   A 1 209 ? 8.687   -19.889 83.522  1.00 26.94 ? 237 ALA   A CA  1 
ATOM   1493 C  C   . ALA   A 1 209 ? 9.980   -19.082 83.466  1.00 24.82 ? 237 ALA   A C   1 
ATOM   1494 O  O   . ALA   A 1 209 ? 10.614  -18.970 82.409  1.00 24.15 ? 237 ALA   A O   1 
ATOM   1495 C  CB  . ALA   A 1 209 ? 7.479   -18.959 83.610  1.00 25.49 ? 237 ALA   A CB  1 
ATOM   1496 N  N   . LEU   A 1 210 ? 10.369  -18.491 84.597  1.00 22.70 ? 238 LEU   A N   1 
ATOM   1497 C  CA  . LEU   A 1 210 ? 11.651  -17.791 84.689  1.00 29.33 ? 238 LEU   A CA  1 
ATOM   1498 C  C   . LEU   A 1 210 ? 12.814  -18.692 84.301  1.00 27.30 ? 238 LEU   A C   1 
ATOM   1499 O  O   . LEU   A 1 210 ? 13.643  -18.331 83.458  1.00 26.99 ? 238 LEU   A O   1 
ATOM   1500 C  CB  . LEU   A 1 210 ? 11.861  -17.277 86.109  1.00 26.57 ? 238 LEU   A CB  1 
ATOM   1501 C  CG  . LEU   A 1 210 ? 11.040  -16.055 86.482  1.00 27.37 ? 238 LEU   A CG  1 
ATOM   1502 C  CD1 . LEU   A 1 210 ? 11.323  -15.664 87.922  1.00 31.65 ? 238 LEU   A CD1 1 
ATOM   1503 C  CD2 . LEU   A 1 210 ? 11.378  -14.930 85.536  1.00 23.42 ? 238 LEU   A CD2 1 
ATOM   1504 N  N   . THR   A 1 211 ? 12.906  -19.861 84.940  1.00 29.12 ? 239 THR   A N   1 
ATOM   1505 C  CA  . THR   A 1 211 ? 14.032  -20.762 84.709  1.00 27.16 ? 239 THR   A CA  1 
ATOM   1506 C  C   . THR   A 1 211 ? 14.147  -21.137 83.240  1.00 28.78 ? 239 THR   A C   1 
ATOM   1507 O  O   . THR   A 1 211 ? 15.256  -21.329 82.725  1.00 24.06 ? 239 THR   A O   1 
ATOM   1508 C  CB  . THR   A 1 211 ? 13.855  -22.014 85.564  1.00 27.62 ? 239 THR   A CB  1 
ATOM   1509 O  OG1 . THR   A 1 211 ? 14.117  -21.692 86.930  1.00 27.28 ? 239 THR   A OG1 1 
ATOM   1510 C  CG2 . THR   A 1 211 ? 14.799  -23.119 85.114  1.00 27.86 ? 239 THR   A CG2 1 
ATOM   1511 N  N   . TYR   A 1 212 ? 13.012  -21.223 82.543  1.00 25.16 ? 240 TYR   A N   1 
ATOM   1512 C  CA  . TYR   A 1 212 ? 13.042  -21.611 81.138  1.00 28.39 ? 240 TYR   A CA  1 
ATOM   1513 C  C   . TYR   A 1 212 ? 13.582  -20.474 80.270  1.00 23.44 ? 240 TYR   A C   1 
ATOM   1514 O  O   . TYR   A 1 212 ? 14.459  -20.685 79.423  1.00 21.33 ? 240 TYR   A O   1 
ATOM   1515 C  CB  . TYR   A 1 212 ? 11.634  -22.053 80.694  1.00 22.43 ? 240 TYR   A CB  1 
ATOM   1516 C  CG  . TYR   A 1 212 ? 11.469  -22.127 79.196  1.00 25.98 ? 240 TYR   A CG  1 
ATOM   1517 C  CD1 . TYR   A 1 212 ? 12.109  -23.111 78.453  1.00 22.37 ? 240 TYR   A CD1 1 
ATOM   1518 C  CD2 . TYR   A 1 212 ? 10.673  -21.206 78.522  1.00 23.98 ? 240 TYR   A CD2 1 
ATOM   1519 C  CE1 . TYR   A 1 212 ? 11.975  -23.177 77.083  1.00 20.29 ? 240 TYR   A CE1 1 
ATOM   1520 C  CE2 . TYR   A 1 212 ? 10.522  -21.266 77.150  1.00 24.65 ? 240 TYR   A CE2 1 
ATOM   1521 C  CZ  . TYR   A 1 212 ? 11.171  -22.255 76.433  1.00 20.25 ? 240 TYR   A CZ  1 
ATOM   1522 O  OH  . TYR   A 1 212 ? 11.042  -22.296 75.063  1.00 16.45 ? 240 TYR   A OH  1 
ATOM   1523 N  N   . VAL   A 1 213 ? 13.093  -19.255 80.488  1.00 22.30 ? 241 VAL   A N   1 
ATOM   1524 C  CA  . VAL   A 1 213 ? 13.436  -18.149 79.597  1.00 20.36 ? 241 VAL   A CA  1 
ATOM   1525 C  C   . VAL   A 1 213 ? 14.835  -17.628 79.891  1.00 21.26 ? 241 VAL   A C   1 
ATOM   1526 O  O   . VAL   A 1 213 ? 15.617  -17.341 78.975  1.00 17.31 ? 241 VAL   A O   1 
ATOM   1527 C  CB  . VAL   A 1 213 ? 12.388  -17.017 79.704  1.00 22.71 ? 241 VAL   A CB  1 
ATOM   1528 C  CG1 . VAL   A 1 213 ? 12.792  -15.846 78.806  1.00 14.23 ? 241 VAL   A CG1 1 
ATOM   1529 C  CG2 . VAL   A 1 213 ? 10.984  -17.534 79.372  1.00 14.84 ? 241 VAL   A CG2 1 
ATOM   1530 N  N   . ALA   A 1 214 ? 15.163  -17.454 81.170  1.00 20.74 ? 242 ALA   A N   1 
ATOM   1531 C  CA  . ALA   A 1 214 ? 16.522  -17.035 81.494  1.00 22.13 ? 242 ALA   A CA  1 
ATOM   1532 C  C   . ALA   A 1 214 ? 17.508  -18.126 81.157  1.00 22.13 ? 242 ALA   A C   1 
ATOM   1533 O  O   . ALA   A 1 214 ? 18.693  -17.841 80.930  1.00 24.49 ? 242 ALA   A O   1 
ATOM   1534 C  CB  . ALA   A 1 214 ? 16.647  -16.657 82.971  1.00 19.77 ? 242 ALA   A CB  1 
ATOM   1535 N  N   . GLY   A 1 215 ? 17.025  -19.366 81.083  1.00 24.91 ? 243 GLY   A N   1 
ATOM   1536 C  CA  . GLY   A 1 215 ? 17.914  -20.469 80.796  1.00 21.00 ? 243 GLY   A CA  1 
ATOM   1537 C  C   . GLY   A 1 215 ? 18.413  -20.429 79.369  1.00 24.51 ? 243 GLY   A C   1 
ATOM   1538 O  O   . GLY   A 1 215 ? 19.615  -20.559 79.125  1.00 24.38 ? 243 GLY   A O   1 
ATOM   1539 N  N   . PHE   A 1 216 ? 17.504  -20.227 78.405  1.00 24.43 ? 244 PHE   A N   1 
ATOM   1540 C  CA  . PHE   A 1 216 ? 17.943  -20.251 77.018  1.00 21.95 ? 244 PHE   A CA  1 
ATOM   1541 C  C   . PHE   A 1 216 ? 18.429  -18.894 76.510  1.00 22.92 ? 244 PHE   A C   1 
ATOM   1542 O  O   . PHE   A 1 216 ? 19.198  -18.861 75.540  1.00 19.86 ? 244 PHE   A O   1 
ATOM   1543 C  CB  . PHE   A 1 216 ? 16.852  -20.861 76.105  1.00 21.06 ? 244 PHE   A CB  1 
ATOM   1544 C  CG  . PHE   A 1 216 ? 15.625  -19.992 75.855  1.00 27.34 ? 244 PHE   A CG  1 
ATOM   1545 C  CD1 . PHE   A 1 216 ? 14.408  -20.303 76.459  1.00 24.93 ? 244 PHE   A CD1 1 
ATOM   1546 C  CD2 . PHE   A 1 216 ? 15.656  -18.937 74.941  1.00 17.78 ? 244 PHE   A CD2 1 
ATOM   1547 C  CE1 . PHE   A 1 216 ? 13.252  -19.545 76.200  1.00 20.58 ? 244 PHE   A CE1 1 
ATOM   1548 C  CE2 . PHE   A 1 216 ? 14.508  -18.188 74.671  1.00 20.52 ? 244 PHE   A CE2 1 
ATOM   1549 C  CZ  . PHE   A 1 216 ? 13.310  -18.485 75.307  1.00 19.62 ? 244 PHE   A CZ  1 
ATOM   1550 N  N   . THR   A 1 217 ? 18.067  -17.785 77.171  1.00 23.05 ? 245 THR   A N   1 
ATOM   1551 C  CA  . THR   A 1 217 ? 18.457  -16.456 76.710  1.00 20.91 ? 245 THR   A CA  1 
ATOM   1552 C  C   . THR   A 1 217 ? 19.728  -15.955 77.372  1.00 21.98 ? 245 THR   A C   1 
ATOM   1553 O  O   . THR   A 1 217 ? 20.522  -15.258 76.739  1.00 23.53 ? 245 THR   A O   1 
ATOM   1554 C  CB  . THR   A 1 217 ? 17.373  -15.408 76.997  1.00 22.20 ? 245 THR   A CB  1 
ATOM   1555 O  OG1 . THR   A 1 217 ? 17.080  -15.393 78.404  1.00 22.13 ? 245 THR   A OG1 1 
ATOM   1556 C  CG2 . THR   A 1 217 ? 16.103  -15.645 76.176  1.00 16.49 ? 245 THR   A CG2 1 
ATOM   1557 N  N   . GLY   A 1 218 ? 19.908  -16.252 78.644  1.00 23.52 ? 246 GLY   A N   1 
ATOM   1558 C  CA  . GLY   A 1 218 ? 20.927  -15.600 79.412  1.00 23.83 ? 246 GLY   A CA  1 
ATOM   1559 C  C   . GLY   A 1 218 ? 20.485  -14.298 80.022  1.00 26.15 ? 246 GLY   A C   1 
ATOM   1560 O  O   . GLY   A 1 218 ? 21.304  -13.635 80.668  1.00 26.17 ? 246 GLY   A O   1 
ATOM   1561 N  N   . PHE   A 1 219 ? 19.218  -13.916 79.850  1.00 20.82 ? 247 PHE   A N   1 
ATOM   1562 C  CA  . PHE   A 1 219 ? 18.720  -12.689 80.461  1.00 25.14 ? 247 PHE   A CA  1 
ATOM   1563 C  C   . PHE   A 1 219 ? 18.811  -12.796 81.971  1.00 22.53 ? 247 PHE   A C   1 
ATOM   1564 O  O   . PHE   A 1 219 ? 18.585  -13.863 82.547  1.00 23.66 ? 247 PHE   A O   1 
ATOM   1565 C  CB  . PHE   A 1 219 ? 17.262  -12.408 80.067  1.00 23.05 ? 247 PHE   A CB  1 
ATOM   1566 C  CG  . PHE   A 1 219 ? 17.069  -12.082 78.625  1.00 25.76 ? 247 PHE   A CG  1 
ATOM   1567 C  CD1 . PHE   A 1 219 ? 18.151  -11.810 77.815  1.00 18.19 ? 247 PHE   A CD1 1 
ATOM   1568 C  CD2 . PHE   A 1 219 ? 15.791  -12.045 78.075  1.00 19.56 ? 247 PHE   A CD2 1 
ATOM   1569 C  CE1 . PHE   A 1 219 ? 17.966  -11.525 76.483  1.00 22.38 ? 247 PHE   A CE1 1 
ATOM   1570 C  CE2 . PHE   A 1 219 ? 15.608  -11.757 76.750  1.00 15.85 ? 247 PHE   A CE2 1 
ATOM   1571 C  CZ  . PHE   A 1 219 ? 16.679  -11.492 75.953  1.00 22.88 ? 247 PHE   A CZ  1 
ATOM   1572 N  N   . HIS   A 1 220 ? 19.129  -11.679 82.611  1.00 20.28 ? 248 HIS   A N   1 
ATOM   1573 C  CA  . HIS   A 1 220 ? 19.249  -11.613 84.058  1.00 22.50 ? 248 HIS   A CA  1 
ATOM   1574 C  C   . HIS   A 1 220 ? 18.014  -10.967 84.655  1.00 22.97 ? 248 HIS   A C   1 
ATOM   1575 O  O   . HIS   A 1 220 ? 17.312  -10.191 83.999  1.00 28.10 ? 248 HIS   A O   1 
ATOM   1576 C  CB  . HIS   A 1 220 ? 20.491  -10.821 84.473  1.00 19.62 ? 248 HIS   A CB  1 
ATOM   1577 C  CG  . HIS   A 1 220 ? 20.448  -9.392  84.041  1.00 24.50 ? 248 HIS   A CG  1 
ATOM   1578 N  ND1 . HIS   A 1 220 ? 20.804  -8.989  82.770  1.00 19.62 ? 248 HIS   A ND1 1 
ATOM   1579 C  CD2 . HIS   A 1 220 ? 20.036  -8.277  84.690  1.00 21.48 ? 248 HIS   A CD2 1 
ATOM   1580 C  CE1 . HIS   A 1 220 ? 20.639  -7.684  82.663  1.00 19.72 ? 248 HIS   A CE1 1 
ATOM   1581 N  NE2 . HIS   A 1 220 ? 20.180  -7.227  83.815  1.00 25.28 ? 248 HIS   A NE2 1 
ATOM   1582 N  N   . GLN   A 1 221 ? 17.775  -11.277 85.923  1.00 19.04 ? 249 GLN   A N   1 
ATOM   1583 C  CA  . GLN   A 1 221 ? 16.659  -10.706 86.661  1.00 23.28 ? 249 GLN   A CA  1 
ATOM   1584 C  C   . GLN   A 1 221 ? 16.950  -9.245  86.990  1.00 25.28 ? 249 GLN   A C   1 
ATOM   1585 O  O   . GLN   A 1 221 ? 17.959  -8.930  87.628  1.00 25.45 ? 249 GLN   A O   1 
ATOM   1586 C  CB  . GLN   A 1 221 ? 16.403  -11.516 87.927  1.00 29.07 ? 249 GLN   A CB  1 
ATOM   1587 C  CG  . GLN   A 1 221 ? 15.355  -10.914 88.827  1.00 33.07 ? 249 GLN   A CG  1 
ATOM   1588 C  CD  . GLN   A 1 221 ? 14.748  -11.933 89.768  1.00 36.48 ? 249 GLN   A CD  1 
ATOM   1589 O  OE1 . GLN   A 1 221 ? 15.006  -13.130 89.662  1.00 38.51 ? 249 GLN   A OE1 1 
ATOM   1590 N  NE2 . GLN   A 1 221 ? 13.929  -11.458 90.697  1.00 44.50 ? 249 GLN   A NE2 1 
ATOM   1591 N  N   . PHE   A 1 222 ? 16.064  -8.359  86.557  1.00 28.05 ? 250 PHE   A N   1 
ATOM   1592 C  CA  . PHE   A 1 222 ? 16.237  -6.915  86.694  1.00 30.73 ? 250 PHE   A CA  1 
ATOM   1593 C  C   . PHE   A 1 222 ? 16.028  -6.487  88.141  1.00 30.39 ? 250 PHE   A C   1 
ATOM   1594 O  O   . PHE   A 1 222 ? 16.669  -5.539  88.603  1.00 30.22 ? 250 PHE   A O   1 
ATOM   1595 C  CB  . PHE   A 1 222 ? 15.269  -6.192  85.750  1.00 32.57 ? 250 PHE   A CB  1 
ATOM   1596 C  CG  . PHE   A 1 222 ? 15.349  -4.684  85.790  1.00 28.22 ? 250 PHE   A CG  1 
ATOM   1597 C  CD1 . PHE   A 1 222 ? 14.744  -3.964  86.811  1.00 27.04 ? 250 PHE   A CD1 1 
ATOM   1598 C  CD2 . PHE   A 1 222 ? 15.959  -3.991  84.763  1.00 27.91 ? 250 PHE   A CD2 1 
ATOM   1599 C  CE1 . PHE   A 1 222 ? 14.794  -2.582  86.836  1.00 31.20 ? 250 PHE   A CE1 1 
ATOM   1600 C  CE2 . PHE   A 1 222 ? 16.007  -2.608  84.774  1.00 26.65 ? 250 PHE   A CE2 1 
ATOM   1601 C  CZ  . PHE   A 1 222 ? 15.424  -1.903  85.813  1.00 29.92 ? 250 PHE   A CZ  1 
ATOM   1602 N  N   . SER   A 1 235 ? -1.274  -6.217  94.831  1.00 48.83 ? 263 SER   A N   1 
ATOM   1603 C  CA  . SER   A 1 235 ? -1.709  -7.473  95.428  1.00 48.28 ? 263 SER   A CA  1 
ATOM   1604 C  C   . SER   A 1 235 ? -2.292  -8.424  94.390  1.00 42.99 ? 263 SER   A C   1 
ATOM   1605 O  O   . SER   A 1 235 ? -2.864  -8.001  93.390  1.00 46.12 ? 263 SER   A O   1 
ATOM   1606 C  CB  . SER   A 1 235 ? -2.740  -7.218  96.524  1.00 49.11 ? 263 SER   A CB  1 
ATOM   1607 O  OG  . SER   A 1 235 ? -2.701  -8.250  97.500  1.00 52.61 ? 263 SER   A OG  1 
ATOM   1608 N  N   . GLY   A 1 236 ? -2.140  -9.717  94.638  1.00 41.12 ? 264 GLY   A N   1 
ATOM   1609 C  CA  . GLY   A 1 236 ? -2.640  -10.733 93.741  1.00 40.50 ? 264 GLY   A CA  1 
ATOM   1610 C  C   . GLY   A 1 236 ? -1.661  -11.247 92.712  1.00 32.59 ? 264 GLY   A C   1 
ATOM   1611 O  O   . GLY   A 1 236 ? -2.098  -11.846 91.723  1.00 30.11 ? 264 GLY   A O   1 
ATOM   1612 N  N   . LEU   A 1 237 ? -0.361  -11.043 92.910  1.00 36.05 ? 265 LEU   A N   1 
ATOM   1613 C  CA  . LEU   A 1 237 ? 0.639   -11.508 91.956  1.00 37.51 ? 265 LEU   A CA  1 
ATOM   1614 C  C   . LEU   A 1 237 ? 2.012   -11.482 92.613  1.00 32.27 ? 265 LEU   A C   1 
ATOM   1615 O  O   . LEU   A 1 237 ? 2.235   -10.736 93.566  1.00 35.55 ? 265 LEU   A O   1 
ATOM   1616 C  CB  . LEU   A 1 237 ? 0.659   -10.641 90.692  1.00 37.36 ? 265 LEU   A CB  1 
ATOM   1617 C  CG  . LEU   A 1 237 ? 1.366   -9.278  90.792  1.00 38.14 ? 265 LEU   A CG  1 
ATOM   1618 C  CD1 . LEU   A 1 237 ? 1.533   -8.676  89.410  1.00 31.49 ? 265 LEU   A CD1 1 
ATOM   1619 C  CD2 . LEU   A 1 237 ? 0.643   -8.296  91.723  1.00 40.36 ? 265 LEU   A CD2 1 
ATOM   1620 N  N   . ASN   A 1 238 ? 2.909   -12.330 92.119  1.00 32.28 ? 266 ASN   A N   1 
ATOM   1621 C  CA  . ASN   A 1 238 ? 4.343   -12.097 92.230  1.00 32.13 ? 266 ASN   A CA  1 
ATOM   1622 C  C   . ASN   A 1 238 ? 4.889   -11.956 90.825  1.00 28.86 ? 266 ASN   A C   1 
ATOM   1623 O  O   . ASN   A 1 238 ? 4.343   -12.521 89.874  1.00 31.22 ? 266 ASN   A O   1 
ATOM   1624 C  CB  . ASN   A 1 238 ? 5.104   -13.211 92.928  1.00 31.53 ? 266 ASN   A CB  1 
ATOM   1625 C  CG  . ASN   A 1 238 ? 4.358   -13.789 94.081  1.00 35.75 ? 266 ASN   A CG  1 
ATOM   1626 O  OD1 . ASN   A 1 238 ? 4.117   -13.118 95.083  1.00 46.18 ? 266 ASN   A OD1 1 
ATOM   1627 N  ND2 . ASN   A 1 238 ? 4.004   -15.064 93.964  1.00 39.22 ? 266 ASN   A ND2 1 
ATOM   1628 N  N   . SER   A 1 239 ? 5.975   -11.208 90.700  1.00 28.89 ? 267 SER   A N   1 
ATOM   1629 C  CA  . SER   A 1 239 ? 6.473   -10.837 89.387  1.00 29.97 ? 267 SER   A CA  1 
ATOM   1630 C  C   . SER   A 1 239 ? 7.978   -10.652 89.436  1.00 32.30 ? 267 SER   A C   1 
ATOM   1631 O  O   . SER   A 1 239 ? 8.505   -10.055 90.375  1.00 35.22 ? 267 SER   A O   1 
ATOM   1632 C  CB  . SER   A 1 239 ? 5.822   -9.542  88.898  1.00 31.61 ? 267 SER   A CB  1 
ATOM   1633 O  OG  . SER   A 1 239 ? 6.207   -9.278  87.561  1.00 30.28 ? 267 SER   A OG  1 
ATOM   1634 N  N   . ALA   A 1 240 ? 8.654   -11.152 88.415  1.00 27.18 ? 268 ALA   A N   1 
ATOM   1635 C  CA  . ALA   A 1 240 ? 10.060  -10.873 88.200  1.00 24.94 ? 268 ALA   A CA  1 
ATOM   1636 C  C   . ALA   A 1 240 ? 10.246  -10.459 86.746  1.00 26.82 ? 268 ALA   A C   1 
ATOM   1637 O  O   . ALA   A 1 240 ? 9.413   -10.754 85.883  1.00 27.42 ? 268 ALA   A O   1 
ATOM   1638 C  CB  . ALA   A 1 240 ? 10.945  -12.076 88.545  1.00 28.25 ? 268 ALA   A CB  1 
ATOM   1639 N  N   . VAL   A 1 241 ? 11.348  -9.764  86.484  1.00 19.87 ? 269 VAL   A N   1 
ATOM   1640 C  CA  . VAL   A 1 241 ? 11.598  -9.118  85.202  1.00 24.12 ? 269 VAL   A CA  1 
ATOM   1641 C  C   . VAL   A 1 241 ? 12.936  -9.609  84.663  1.00 25.85 ? 269 VAL   A C   1 
ATOM   1642 O  O   . VAL   A 1 241 ? 13.970  -9.465  85.329  1.00 22.63 ? 269 VAL   A O   1 
ATOM   1643 C  CB  . VAL   A 1 241 ? 11.593  -7.589  85.335  1.00 21.77 ? 269 VAL   A CB  1 
ATOM   1644 C  CG1 . VAL   A 1 241 ? 11.823  -6.927  83.967  1.00 21.90 ? 269 VAL   A CG1 1 
ATOM   1645 C  CG2 . VAL   A 1 241 ? 10.302  -7.121  85.953  1.00 21.36 ? 269 VAL   A CG2 1 
ATOM   1646 N  N   . LEU   A 1 242 ? 12.918  -10.171 83.458  1.00 24.18 ? 270 LEU   A N   1 
ATOM   1647 C  CA  . LEU   A 1 242 ? 14.126  -10.609 82.773  1.00 25.21 ? 270 LEU   A CA  1 
ATOM   1648 C  C   . LEU   A 1 242 ? 14.589  -9.526  81.805  1.00 21.57 ? 270 LEU   A C   1 
ATOM   1649 O  O   . LEU   A 1 242 ? 13.767  -8.867  81.170  1.00 24.45 ? 270 LEU   A O   1 
ATOM   1650 C  CB  . LEU   A 1 242 ? 13.873  -11.918 82.022  1.00 22.37 ? 270 LEU   A CB  1 
ATOM   1651 C  CG  . LEU   A 1 242 ? 13.916  -13.220 82.826  1.00 27.55 ? 270 LEU   A CG  1 
ATOM   1652 C  CD1 . LEU   A 1 242 ? 13.640  -14.427 81.946  1.00 22.09 ? 270 LEU   A CD1 1 
ATOM   1653 C  CD2 . LEU   A 1 242 ? 15.272  -13.367 83.495  1.00 22.78 ? 270 LEU   A CD2 1 
ATOM   1654 N  N   . ALA   A 1 243 ? 15.906  -9.352  81.677  1.00 26.51 ? 271 ALA   A N   1 
ATOM   1655 C  CA  . ALA   A 1 243 ? 16.462  -8.235  80.920  1.00 20.73 ? 271 ALA   A CA  1 
ATOM   1656 C  C   . ALA   A 1 243 ? 17.724  -8.647  80.170  1.00 23.59 ? 271 ALA   A C   1 
ATOM   1657 O  O   . ALA   A 1 243 ? 18.530  -9.441  80.664  1.00 26.90 ? 271 ALA   A O   1 
ATOM   1658 C  CB  . ALA   A 1 243 ? 16.784  -7.045  81.833  1.00 21.29 ? 271 ALA   A CB  1 
ATOM   1659 N  N   . SER   A 1 244 ? 17.906  -8.071  78.983  1.00 19.97 ? 272 SER   A N   1 
ATOM   1660 C  CA  . SER   A 1 244 ? 19.115  -8.291  78.201  1.00 22.71 ? 272 SER   A CA  1 
ATOM   1661 C  C   . SER   A 1 244 ? 20.270  -7.473  78.782  1.00 25.12 ? 272 SER   A C   1 
ATOM   1662 O  O   . SER   A 1 244 ? 20.115  -6.737  79.763  1.00 19.50 ? 272 SER   A O   1 
ATOM   1663 C  CB  . SER   A 1 244 ? 18.880  -7.927  76.739  1.00 21.79 ? 272 SER   A CB  1 
ATOM   1664 O  OG  . SER   A 1 244 ? 18.528  -6.563  76.641  1.00 22.39 ? 272 SER   A OG  1 
ATOM   1665 N  N   . ASN   A 1 245 ? 21.443  -7.585  78.142  1.00 27.68 ? 273 ASN   A N   1 
ATOM   1666 C  CA  . ASN   A 1 245 ? 22.672  -7.043  78.724  1.00 27.98 ? 273 ASN   A CA  1 
ATOM   1667 C  C   . ASN   A 1 245 ? 22.542  -5.546  78.995  1.00 26.31 ? 273 ASN   A C   1 
ATOM   1668 O  O   . ASN   A 1 245 ? 22.723  -5.097  80.133  1.00 28.63 ? 273 ASN   A O   1 
ATOM   1669 C  CB  . ASN   A 1 245 ? 23.867  -7.347  77.816  1.00 24.44 ? 273 ASN   A CB  1 
ATOM   1670 C  CG  . ASN   A 1 245 ? 24.320  -8.810  77.906  1.00 30.72 ? 273 ASN   A CG  1 
ATOM   1671 O  OD1 . ASN   A 1 245 ? 23.878  -9.561  78.778  1.00 32.00 ? 273 ASN   A OD1 1 
ATOM   1672 N  ND2 . ASN   A 1 245 ? 25.202  -9.213  77.002  1.00 24.08 ? 273 ASN   A ND2 1 
ATOM   1673 N  N   . ASP   A 1 246 ? 22.180  -4.766  77.972  1.00 25.17 ? 274 ASP   A N   1 
ATOM   1674 C  CA  . ASP   A 1 246 ? 21.927  -3.336  78.142  1.00 24.30 ? 274 ASP   A CA  1 
ATOM   1675 C  C   . ASP   A 1 246 ? 20.542  -3.030  78.732  1.00 29.30 ? 274 ASP   A C   1 
ATOM   1676 O  O   . ASP   A 1 246 ? 20.195  -1.853  78.887  1.00 27.40 ? 274 ASP   A O   1 
ATOM   1677 C  CB  . ASP   A 1 246 ? 22.124  -2.597  76.797  1.00 25.43 ? 274 ASP   A CB  1 
ATOM   1678 C  CG  . ASP   A 1 246 ? 21.103  -2.998  75.718  1.00 24.98 ? 274 ASP   A CG  1 
ATOM   1679 O  OD1 . ASP   A 1 246 ? 20.048  -3.555  76.054  1.00 25.46 ? 274 ASP   A OD1 1 
ATOM   1680 O  OD2 . ASP   A 1 246 ? 21.336  -2.722  74.522  1.00 26.82 ? 274 ASP   A OD2 1 
ATOM   1681 N  N   . GLU   A 1 247 ? 19.740  -4.052  79.051  1.00 27.83 ? 275 GLU   A N   1 
ATOM   1682 C  CA  . GLU   A 1 247 ? 18.432  -3.895  79.705  1.00 24.75 ? 275 GLU   A CA  1 
ATOM   1683 C  C   . GLU   A 1 247 ? 17.442  -3.084  78.855  1.00 28.53 ? 275 GLU   A C   1 
ATOM   1684 O  O   . GLU   A 1 247 ? 16.567  -2.397  79.385  1.00 24.18 ? 275 GLU   A O   1 
ATOM   1685 C  CB  . GLU   A 1 247 ? 18.593  -3.305  81.117  1.00 24.17 ? 275 GLU   A CB  1 
ATOM   1686 C  CG  . GLU   A 1 247 ? 19.442  -4.229  82.043  1.00 30.38 ? 275 GLU   A CG  1 
ATOM   1687 C  CD  . GLU   A 1 247 ? 19.549  -3.770  83.501  1.00 30.47 ? 275 GLU   A CD  1 
ATOM   1688 O  OE1 . GLU   A 1 247 ? 19.664  -4.634  84.395  1.00 28.05 ? 275 GLU   A OE1 1 
ATOM   1689 O  OE2 . GLU   A 1 247 ? 19.551  -2.551  83.758  1.00 33.44 ? 275 GLU   A OE2 1 
ATOM   1690 N  N   . MET   A 1 248 ? 17.559  -3.177  77.524  1.00 27.45 ? 276 MET   A N   1 
ATOM   1691 C  CA  . MET   A 1 248 ? 16.597  -2.587  76.598  1.00 23.67 ? 276 MET   A CA  1 
ATOM   1692 C  C   . MET   A 1 248 ? 15.521  -3.572  76.159  1.00 23.68 ? 276 MET   A C   1 
ATOM   1693 O  O   . MET   A 1 248 ? 14.470  -3.151  75.662  1.00 27.64 ? 276 MET   A O   1 
ATOM   1694 C  CB  . MET   A 1 248 ? 17.323  -2.042  75.364  1.00 24.53 ? 276 MET   A CB  1 
ATOM   1695 C  CG  . MET   A 1 248 ? 18.230  -0.866  75.689  1.00 23.88 ? 276 MET   A CG  1 
ATOM   1696 S  SD  . MET   A 1 248 ? 17.295  0.421   76.522  1.00 38.26 ? 276 MET   A SD  1 
ATOM   1697 C  CE  . MET   A 1 248 ? 18.655  1.261   77.341  1.00 35.69 ? 276 MET   A CE  1 
ATOM   1698 N  N   . VAL   A 1 249 ? 15.760  -4.861  76.327  1.00 21.40 ? 277 VAL   A N   1 
ATOM   1699 C  CA  . VAL   A 1 249 ? 14.733  -5.880  76.168  1.00 23.95 ? 277 VAL   A CA  1 
ATOM   1700 C  C   . VAL   A 1 249 ? 14.296  -6.283  77.567  1.00 21.23 ? 277 VAL   A C   1 
ATOM   1701 O  O   . VAL   A 1 249 ? 15.036  -6.955  78.285  1.00 26.62 ? 277 VAL   A O   1 
ATOM   1702 C  CB  . VAL   A 1 249 ? 15.249  -7.079  75.366  1.00 22.19 ? 277 VAL   A CB  1 
ATOM   1703 C  CG1 . VAL   A 1 249 ? 14.248  -8.250  75.426  1.00 24.13 ? 277 VAL   A CG1 1 
ATOM   1704 C  CG2 . VAL   A 1 249 ? 15.500  -6.674  73.930  1.00 19.63 ? 277 VAL   A CG2 1 
ATOM   1705 N  N   . LEU   A 1 250 ? 13.107  -5.856  77.979  1.00 18.45 ? 278 LEU   A N   1 
ATOM   1706 C  CA  . LEU   A 1 250 ? 12.579  -6.154  79.302  1.00 16.62 ? 278 LEU   A CA  1 
ATOM   1707 C  C   . LEU   A 1 250 ? 11.359  -7.053  79.160  1.00 22.75 ? 278 LEU   A C   1 
ATOM   1708 O  O   . LEU   A 1 250 ? 10.411  -6.708  78.450  1.00 17.70 ? 278 LEU   A O   1 
ATOM   1709 C  CB  . LEU   A 1 250 ? 12.210  -4.865  80.036  1.00 13.54 ? 278 LEU   A CB  1 
ATOM   1710 C  CG  . LEU   A 1 250 ? 13.335  -3.823  80.085  1.00 19.44 ? 278 LEU   A CG  1 
ATOM   1711 C  CD1 . LEU   A 1 250 ? 12.845  -2.457  80.589  1.00 19.99 ? 278 LEU   A CD1 1 
ATOM   1712 C  CD2 . LEU   A 1 250 ? 14.456  -4.344  80.961  1.00 15.93 ? 278 LEU   A CD2 1 
ATOM   1713 N  N   . LEU   A 1 251 ? 11.379  -8.199  79.843  1.00 21.70 ? 279 LEU   A N   1 
ATOM   1714 C  CA  . LEU   A 1 251 ? 10.324  -9.209  79.740  1.00 18.43 ? 279 LEU   A CA  1 
ATOM   1715 C  C   . LEU   A 1 251 ? 9.847   -9.573  81.135  1.00 21.95 ? 279 LEU   A C   1 
ATOM   1716 O  O   . LEU   A 1 251 ? 10.274  -10.587 81.695  1.00 22.09 ? 279 LEU   A O   1 
ATOM   1717 C  CB  . LEU   A 1 251 ? 10.816  -10.462 79.006  1.00 16.73 ? 279 LEU   A CB  1 
ATOM   1718 C  CG  . LEU   A 1 251 ? 11.226  -10.319 77.545  1.00 13.17 ? 279 LEU   A CG  1 
ATOM   1719 C  CD1 . LEU   A 1 251 ? 11.778  -11.613 77.002  1.00 17.53 ? 279 LEU   A CD1 1 
ATOM   1720 C  CD2 . LEU   A 1 251 ? 10.005  -9.844  76.741  1.00 17.75 ? 279 LEU   A CD2 1 
ATOM   1721 N  N   . PRO   A 1 252 ? 8.952   -8.784  81.725  1.00 23.33 ? 280 PRO   A N   1 
ATOM   1722 C  CA  . PRO   A 1 252 ? 8.376   -9.181  83.011  1.00 23.00 ? 280 PRO   A CA  1 
ATOM   1723 C  C   . PRO   A 1 252 ? 7.447   -10.373 82.826  1.00 24.94 ? 280 PRO   A C   1 
ATOM   1724 O  O   . PRO   A 1 252 ? 6.997   -10.689 81.719  1.00 20.58 ? 280 PRO   A O   1 
ATOM   1725 C  CB  . PRO   A 1 252 ? 7.621   -7.930  83.473  1.00 24.00 ? 280 PRO   A CB  1 
ATOM   1726 C  CG  . PRO   A 1 252 ? 8.191   -6.795  82.620  1.00 21.76 ? 280 PRO   A CG  1 
ATOM   1727 C  CD  . PRO   A 1 252 ? 8.474   -7.460  81.306  1.00 24.66 ? 280 PRO   A CD  1 
ATOM   1728 N  N   . ILE   A 1 253 ? 7.223   -11.087 83.929  1.00 27.89 ? 281 ILE   A N   1 
ATOM   1729 C  CA  . ILE   A 1 253 ? 6.417   -12.311 83.947  1.00 22.30 ? 281 ILE   A CA  1 
ATOM   1730 C  C   . ILE   A 1 253 ? 5.691   -12.371 85.277  1.00 26.03 ? 281 ILE   A C   1 
ATOM   1731 O  O   . ILE   A 1 253 ? 6.321   -12.252 86.330  1.00 26.49 ? 281 ILE   A O   1 
ATOM   1732 C  CB  . ILE   A 1 253 ? 7.268   -13.587 83.750  1.00 27.14 ? 281 ILE   A CB  1 
ATOM   1733 C  CG1 . ILE   A 1 253 ? 8.136   -13.488 82.490  1.00 22.03 ? 281 ILE   A CG1 1 
ATOM   1734 C  CG2 . ILE   A 1 253 ? 6.383   -14.845 83.767  1.00 22.42 ? 281 ILE   A CG2 1 
ATOM   1735 C  CD1 . ILE   A 1 253 ? 9.151   -14.617 82.347  1.00 25.98 ? 281 ILE   A CD1 1 
ATOM   1736 N  N   . ASN   A 1 254 ? 4.374   -12.552 85.234  1.00 22.89 ? 282 ASN   A N   1 
ATOM   1737 C  CA  . ASN   A 1 254 ? 3.556   -12.616 86.433  1.00 23.90 ? 282 ASN   A CA  1 
ATOM   1738 C  C   . ASN   A 1 254 ? 3.039   -14.028 86.669  1.00 23.46 ? 282 ASN   A C   1 
ATOM   1739 O  O   . ASN   A 1 254 ? 2.859   -14.820 85.735  1.00 17.47 ? 282 ASN   A O   1 
ATOM   1740 C  CB  . ASN   A 1 254 ? 2.362   -11.669 86.339  1.00 24.32 ? 282 ASN   A CB  1 
ATOM   1741 C  CG  . ASN   A 1 254 ? 2.772   -10.260 86.011  1.00 24.70 ? 282 ASN   A CG  1 
ATOM   1742 O  OD1 . ASN   A 1 254 ? 3.866   -9.816  86.383  1.00 25.04 ? 282 ASN   A OD1 1 
ATOM   1743 N  ND2 . ASN   A 1 254 ? 1.906   -9.545  85.306  1.00 26.62 ? 282 ASN   A ND2 1 
ATOM   1744 N  N   . GLU   A 1 255 ? 2.812   -14.328 87.940  1.00 24.63 ? 283 GLU   A N   1 
ATOM   1745 C  CA  . GLU   A 1 255 ? 2.110   -15.516 88.386  1.00 29.57 ? 283 GLU   A CA  1 
ATOM   1746 C  C   . GLU   A 1 255 ? 1.041   -15.075 89.374  1.00 32.02 ? 283 GLU   A C   1 
ATOM   1747 O  O   . GLU   A 1 255 ? 1.163   -14.008 89.990  1.00 30.35 ? 283 GLU   A O   1 
ATOM   1748 C  CB  . GLU   A 1 255 ? 3.062   -16.529 89.039  1.00 24.15 ? 283 GLU   A CB  1 
ATOM   1749 C  CG  . GLU   A 1 255 ? 3.139   -16.468 90.547  1.00 26.37 ? 283 GLU   A CG  1 
ATOM   1750 C  CD  . GLU   A 1 255 ? 4.044   -17.547 91.119  1.00 31.54 ? 283 GLU   A CD  1 
ATOM   1751 O  OE1 . GLU   A 1 255 ? 4.638   -17.312 92.185  1.00 37.86 ? 283 GLU   A OE1 1 
ATOM   1752 O  OE2 . GLU   A 1 255 ? 4.180   -18.629 90.510  1.00 29.97 ? 283 GLU   A OE2 1 
ATOM   1753 N  N   . PRO   A 1 256 ? -0.037  -15.838 89.509  1.00 31.65 ? 284 PRO   A N   1 
ATOM   1754 C  CA  . PRO   A 1 256 ? -1.083  -15.448 90.453  1.00 34.51 ? 284 PRO   A CA  1 
ATOM   1755 C  C   . PRO   A 1 256 ? -0.717  -15.821 91.882  1.00 32.15 ? 284 PRO   A C   1 
ATOM   1756 O  O   . PRO   A 1 256 ? -0.054  -16.825 92.149  1.00 33.59 ? 284 PRO   A O   1 
ATOM   1757 C  CB  . PRO   A 1 256 ? -2.309  -16.228 89.959  1.00 29.92 ? 284 PRO   A CB  1 
ATOM   1758 C  CG  . PRO   A 1 256 ? -1.740  -17.427 89.297  1.00 32.25 ? 284 PRO   A CG  1 
ATOM   1759 C  CD  . PRO   A 1 256 ? -0.382  -17.063 88.766  1.00 25.79 ? 284 PRO   A CD  1 
ATOM   1760 N  N   . VAL   A 1 257 ? -1.129  -14.966 92.803  1.00 37.74 ? 285 VAL   A N   1 
ATOM   1761 C  CA  . VAL   A 1 257 ? -1.035  -15.236 94.229  1.00 39.67 ? 285 VAL   A CA  1 
ATOM   1762 C  C   . VAL   A 1 257 ? -2.419  -15.702 94.650  1.00 40.89 ? 285 VAL   A C   1 
ATOM   1763 O  O   . VAL   A 1 257 ? -3.355  -14.907 94.738  1.00 36.65 ? 285 VAL   A O   1 
ATOM   1764 C  CB  . VAL   A 1 257 ? -0.572  -14.009 95.017  1.00 38.11 ? 285 VAL   A CB  1 
ATOM   1765 C  CG1 . VAL   A 1 257 ? -0.938  -14.148 96.494  1.00 37.33 ? 285 VAL   A CG1 1 
ATOM   1766 C  CG2 . VAL   A 1 257 ? 0.925   -13.847 94.866  1.00 38.97 ? 285 VAL   A CG2 1 
ATOM   1767 N  N   . HIS   A 1 258 ? -2.556  -17.004 94.879  1.00 43.27 ? 286 HIS   A N   1 
ATOM   1768 C  CA  . HIS   A 1 258 ? -3.860  -17.563 95.190  1.00 47.63 ? 286 HIS   A CA  1 
ATOM   1769 C  C   . HIS   A 1 258 ? -4.192  -17.390 96.672  1.00 50.32 ? 286 HIS   A C   1 
ATOM   1770 O  O   . HIS   A 1 258 ? -3.320  -17.166 97.518  1.00 50.25 ? 286 HIS   A O   1 
ATOM   1771 C  CB  . HIS   A 1 258 ? -3.911  -19.041 94.796  1.00 45.06 ? 286 HIS   A CB  1 
ATOM   1772 C  CG  . HIS   A 1 258 ? -3.820  -19.275 93.318  1.00 43.34 ? 286 HIS   A CG  1 
ATOM   1773 N  ND1 . HIS   A 1 258 ? -2.873  -20.101 92.750  1.00 42.73 ? 286 HIS   A ND1 1 
ATOM   1774 C  CD2 . HIS   A 1 258 ? -4.565  -18.796 92.294  1.00 36.10 ? 286 HIS   A CD2 1 
ATOM   1775 C  CE1 . HIS   A 1 258 ? -3.032  -20.114 91.439  1.00 39.28 ? 286 HIS   A CE1 1 
ATOM   1776 N  NE2 . HIS   A 1 258 ? -4.053  -19.331 91.137  1.00 36.36 ? 286 HIS   A NE2 1 
ATOM   1777 N  N   . GLY   A 1 259 ? -5.484  -17.480 96.973  1.00 53.42 ? 287 GLY   A N   1 
ATOM   1778 C  CA  . GLY   A 1 259 ? -5.953  -17.518 98.338  1.00 49.62 ? 287 GLY   A CA  1 
ATOM   1779 C  C   . GLY   A 1 259 ? -6.294  -16.182 98.950  1.00 49.68 ? 287 GLY   A C   1 
ATOM   1780 O  O   . GLY   A 1 259 ? -6.739  -16.146 100.103 1.00 53.59 ? 287 GLY   A O   1 
ATOM   1781 N  N   . THR   A 1 260 ? -6.124  -15.086 98.225  1.00 48.50 ? 288 THR   A N   1 
ATOM   1782 C  CA  . THR   A 1 260 ? -6.265  -13.776 98.833  1.00 45.19 ? 288 THR   A CA  1 
ATOM   1783 C  C   . THR   A 1 260 ? -7.706  -13.273 98.727  1.00 55.28 ? 288 THR   A C   1 
ATOM   1784 O  O   . THR   A 1 260 ? -8.593  -13.939 98.184  1.00 53.38 ? 288 THR   A O   1 
ATOM   1785 C  CB  . THR   A 1 260 ? -5.285  -12.801 98.194  1.00 50.43 ? 288 THR   A CB  1 
ATOM   1786 O  OG1 . THR   A 1 260 ? -5.475  -11.494 98.755  1.00 52.14 ? 288 THR   A OG1 1 
ATOM   1787 C  CG2 . THR   A 1 260 ? -5.488  -12.780 96.678  1.00 47.09 ? 288 THR   A CG2 1 
ATOM   1788 N  N   . LYS   A 1 261 ? -7.937  -12.074 99.267  1.00 48.44 ? 289 LYS   A N   1 
ATOM   1789 C  CA  . LYS   A 1 261 ? -9.267  -11.486 99.359  1.00 53.17 ? 289 LYS   A CA  1 
ATOM   1790 C  C   . LYS   A 1 261 ? -9.902  -11.329 97.983  1.00 58.54 ? 289 LYS   A C   1 
ATOM   1791 O  O   . LYS   A 1 261 ? -10.735 -12.151 97.581  1.00 56.42 ? 289 LYS   A O   1 
ATOM   1792 C  CB  . LYS   A 1 261 ? -9.198  -10.131 100.067 1.00 52.28 ? 289 LYS   A CB  1 
ATOM   1793 N  N   . ARG   A 1 262 ? -9.528  -10.271 97.264  1.00 56.47 ? 290 ARG   A N   1 
ATOM   1794 C  CA  . ARG   A 1 262 ? -9.972  -10.122 95.886  1.00 50.97 ? 290 ARG   A CA  1 
ATOM   1795 C  C   . ARG   A 1 262 ? -9.288  -11.167 95.013  1.00 48.25 ? 290 ARG   A C   1 
ATOM   1796 O  O   . ARG   A 1 262 ? -8.129  -11.531 95.242  1.00 48.16 ? 290 ARG   A O   1 
ATOM   1797 C  CB  . ARG   A 1 262 ? -9.675  -8.712  95.369  1.00 40.91 ? 290 ARG   A CB  1 
ATOM   1798 N  N   . LYS   A 1 263 ? -10.024 -11.667 94.022  1.00 50.89 ? 291 LYS   A N   1 
ATOM   1799 C  CA  . LYS   A 1 263 ? -9.470  -12.658 93.109  1.00 41.95 ? 291 LYS   A CA  1 
ATOM   1800 C  C   . LYS   A 1 263 ? -8.288  -12.066 92.357  1.00 38.21 ? 291 LYS   A C   1 
ATOM   1801 O  O   . LYS   A 1 263 ? -8.284  -10.885 91.999  1.00 41.53 ? 291 LYS   A O   1 
ATOM   1802 C  CB  . LYS   A 1 263 ? -10.534 -13.134 92.119  1.00 32.03 ? 291 LYS   A CB  1 
ATOM   1803 C  CG  . LYS   A 1 263 ? -10.152 -14.394 91.378  1.00 38.44 ? 291 LYS   A CG  1 
ATOM   1804 C  CD  . LYS   A 1 263 ? -11.089 -14.691 90.217  1.00 32.12 ? 291 LYS   A CD  1 
ATOM   1805 C  CE  . LYS   A 1 263 ? -10.661 -15.961 89.495  1.00 35.96 ? 291 LYS   A CE  1 
ATOM   1806 N  NZ  . LYS   A 1 263 ? -11.495 -16.219 88.295  1.00 38.28 ? 291 LYS   A NZ  1 
ATOM   1807 N  N   . SER   A 1 264 ? -7.276  -12.888 92.136  1.00 37.01 ? 292 SER   A N   1 
ATOM   1808 C  CA  . SER   A 1 264 ? -6.087  -12.419 91.447  1.00 34.09 ? 292 SER   A CA  1 
ATOM   1809 C  C   . SER   A 1 264 ? -6.424  -12.087 90.003  1.00 29.83 ? 292 SER   A C   1 
ATOM   1810 O  O   . SER   A 1 264 ? -6.974  -12.920 89.282  1.00 32.07 ? 292 SER   A O   1 
ATOM   1811 C  CB  . SER   A 1 264 ? -4.984  -13.473 91.508  1.00 31.40 ? 292 SER   A CB  1 
ATOM   1812 O  OG  . SER   A 1 264 ? -3.932  -13.151 90.618  1.00 29.50 ? 292 SER   A OG  1 
ATOM   1813 N  N   . GLN   A 1 265 ? -6.080  -10.868 89.579  1.00 29.17 ? 293 GLN   A N   1 
ATOM   1814 C  CA  . GLN   A 1 265 ? -6.262  -10.497 88.185  1.00 30.97 ? 293 GLN   A CA  1 
ATOM   1815 C  C   . GLN   A 1 265 ? -5.430  -11.375 87.249  1.00 30.52 ? 293 GLN   A C   1 
ATOM   1816 O  O   . GLN   A 1 265 ? -5.799  -11.544 86.080  1.00 25.96 ? 293 GLN   A O   1 
ATOM   1817 C  CB  . GLN   A 1 265 ? -5.951  -9.011  88.005  1.00 32.29 ? 293 GLN   A CB  1 
ATOM   1818 C  CG  . GLN   A 1 265 ? -4.474  -8.651  88.081  1.00 35.70 ? 293 GLN   A CG  1 
ATOM   1819 C  CD  . GLN   A 1 265 ? -3.961  -8.314  89.496  1.00 46.28 ? 293 GLN   A CD  1 
ATOM   1820 O  OE1 . GLN   A 1 265 ? -4.364  -8.939  90.503  1.00 42.38 ? 293 GLN   A OE1 1 
ATOM   1821 N  NE2 . GLN   A 1 265 ? -3.022  -7.337  89.562  1.00 38.66 ? 293 GLN   A NE2 1 
ATOM   1822 N  N   . ILE   A 1 266 ? -4.338  -11.969 87.740  1.00 32.36 ? 294 ILE   A N   1 
ATOM   1823 C  CA  . ILE   A 1 266 ? -3.549  -12.875 86.906  1.00 27.00 ? 294 ILE   A CA  1 
ATOM   1824 C  C   . ILE   A 1 266 ? -4.310  -14.169 86.650  1.00 24.41 ? 294 ILE   A C   1 
ATOM   1825 O  O   . ILE   A 1 266 ? -4.335  -14.681 85.525  1.00 25.34 ? 294 ILE   A O   1 
ATOM   1826 C  CB  . ILE   A 1 266 ? -2.180  -13.158 87.549  1.00 26.25 ? 294 ILE   A CB  1 
ATOM   1827 C  CG1 . ILE   A 1 266 ? -1.485  -11.852 87.912  1.00 28.70 ? 294 ILE   A CG1 1 
ATOM   1828 C  CG2 . ILE   A 1 266 ? -1.327  -13.979 86.597  1.00 22.84 ? 294 ILE   A CG2 1 
ATOM   1829 C  CD1 . ILE   A 1 266 ? -1.378  -10.909 86.769  1.00 24.40 ? 294 ILE   A CD1 1 
ATOM   1830 N  N   . GLN   A 1 267 ? -4.918  -14.738 87.692  1.00 29.18 ? 295 GLN   A N   1 
ATOM   1831 C  CA  . GLN   A 1 267 ? -5.716  -15.947 87.501  1.00 26.45 ? 295 GLN   A CA  1 
ATOM   1832 C  C   . GLN   A 1 267 ? -6.921  -15.672 86.606  1.00 27.54 ? 295 GLN   A C   1 
ATOM   1833 O  O   . GLN   A 1 267 ? -7.250  -16.482 85.728  1.00 25.38 ? 295 GLN   A O   1 
ATOM   1834 C  CB  . GLN   A 1 267 ? -6.165  -16.511 88.849  1.00 26.27 ? 295 GLN   A CB  1 
ATOM   1835 C  CG  . GLN   A 1 267 ? -7.114  -17.716 88.761  1.00 27.65 ? 295 GLN   A CG  1 
ATOM   1836 C  CD  . GLN   A 1 267 ? -6.431  -18.980 88.258  1.00 25.34 ? 295 GLN   A CD  1 
ATOM   1837 O  OE1 . GLN   A 1 267 ? -5.205  -19.083 88.271  1.00 25.94 ? 295 GLN   A OE1 1 
ATOM   1838 N  NE2 . GLN   A 1 267 ? -7.220  -19.944 87.810  1.00 20.05 ? 295 GLN   A NE2 1 
ATOM   1839 N  N   . THR   A 1 268 ? -7.588  -14.529 86.803  1.00 26.26 ? 296 THR   A N   1 
ATOM   1840 C  CA  . THR   A 1 268 ? -8.663  -14.148 85.888  1.00 24.99 ? 296 THR   A CA  1 
ATOM   1841 C  C   . THR   A 1 268 ? -8.175  -14.175 84.447  1.00 23.68 ? 296 THR   A C   1 
ATOM   1842 O  O   . THR   A 1 268 ? -8.859  -14.697 83.557  1.00 20.55 ? 296 THR   A O   1 
ATOM   1843 C  CB  . THR   A 1 268 ? -9.202  -12.762 86.246  1.00 28.63 ? 296 THR   A CB  1 
ATOM   1844 O  OG1 . THR   A 1 268 ? -9.893  -12.831 87.495  1.00 27.94 ? 296 THR   A OG1 1 
ATOM   1845 C  CG2 . THR   A 1 268 ? -10.157 -12.236 85.163  1.00 21.53 ? 296 THR   A CG2 1 
ATOM   1846 N  N   . TYR   A 1 269 ? -6.960  -13.668 84.212  1.00 22.71 ? 297 TYR   A N   1 
ATOM   1847 C  CA  . TYR   A 1 269 ? -6.384  -13.712 82.874  1.00 23.09 ? 297 TYR   A CA  1 
ATOM   1848 C  C   . TYR   A 1 269 ? -6.288  -15.139 82.370  1.00 22.61 ? 297 TYR   A C   1 
ATOM   1849 O  O   . TYR   A 1 269 ? -6.704  -15.439 81.246  1.00 22.88 ? 297 TYR   A O   1 
ATOM   1850 C  CB  . TYR   A 1 269 ? -4.993  -13.066 82.862  1.00 22.79 ? 297 TYR   A CB  1 
ATOM   1851 C  CG  . TYR   A 1 269 ? -4.317  -13.146 81.505  1.00 19.43 ? 297 TYR   A CG  1 
ATOM   1852 C  CD1 . TYR   A 1 269 ? -3.623  -14.295 81.089  1.00 18.39 ? 297 TYR   A CD1 1 
ATOM   1853 C  CD2 . TYR   A 1 269 ? -4.383  -12.078 80.633  1.00 19.42 ? 297 TYR   A CD2 1 
ATOM   1854 C  CE1 . TYR   A 1 269 ? -3.026  -14.351 79.840  1.00 14.09 ? 297 TYR   A CE1 1 
ATOM   1855 C  CE2 . TYR   A 1 269 ? -3.780  -12.121 79.396  1.00 20.11 ? 297 TYR   A CE2 1 
ATOM   1856 C  CZ  . TYR   A 1 269 ? -3.111  -13.257 79.000  1.00 17.31 ? 297 TYR   A CZ  1 
ATOM   1857 O  OH  . TYR   A 1 269 ? -2.541  -13.260 77.749  1.00 19.53 ? 297 TYR   A OH  1 
ATOM   1858 N  N   . LEU   A 1 270 ? -5.696  -16.028 83.181  1.00 22.52 ? 298 LEU   A N   1 
ATOM   1859 C  CA  . LEU   A 1 270 ? -5.458  -17.405 82.758  1.00 20.29 ? 298 LEU   A CA  1 
ATOM   1860 C  C   . LEU   A 1 270 ? -6.763  -18.136 82.448  1.00 20.42 ? 298 LEU   A C   1 
ATOM   1861 O  O   . LEU   A 1 270 ? -6.806  -18.984 81.555  1.00 23.85 ? 298 LEU   A O   1 
ATOM   1862 C  CB  . LEU   A 1 270 ? -4.685  -18.143 83.845  1.00 17.14 ? 298 LEU   A CB  1 
ATOM   1863 C  CG  . LEU   A 1 270 ? -3.286  -17.608 84.152  1.00 22.77 ? 298 LEU   A CG  1 
ATOM   1864 C  CD1 . LEU   A 1 270 ? -2.699  -18.350 85.323  1.00 20.81 ? 298 LEU   A CD1 1 
ATOM   1865 C  CD2 . LEU   A 1 270 ? -2.382  -17.709 82.921  1.00 21.17 ? 298 LEU   A CD2 1 
ATOM   1866 N  N   . GLU   A 1 271 ? -7.838  -17.796 83.149  1.00 21.97 ? 299 GLU   A N   1 
ATOM   1867 C  CA  . GLU   A 1 271 ? -9.110  -18.472 82.917  1.00 25.93 ? 299 GLU   A CA  1 
ATOM   1868 C  C   . GLU   A 1 271 ? -9.789  -17.975 81.647  1.00 20.55 ? 299 GLU   A C   1 
ATOM   1869 O  O   . GLU   A 1 271 ? -10.317 -18.776 80.872  1.00 24.13 ? 299 GLU   A O   1 
ATOM   1870 C  CB  . GLU   A 1 271 ? -10.010 -18.294 84.136  1.00 24.68 ? 299 GLU   A CB  1 
ATOM   1871 C  CG  . GLU   A 1 271 ? -9.476  -18.999 85.388  1.00 20.49 ? 299 GLU   A CG  1 
ATOM   1872 C  CD  . GLU   A 1 271 ? -10.224 -18.612 86.643  1.00 27.30 ? 299 GLU   A CD  1 
ATOM   1873 O  OE1 . GLU   A 1 271 ? -11.060 -17.694 86.549  1.00 29.87 ? 299 GLU   A OE1 1 
ATOM   1874 O  OE2 . GLU   A 1 271 ? -9.976  -19.212 87.718  1.00 28.24 ? 299 GLU   A OE2 1 
ATOM   1875 N  N   . HIS   A 1 272 ? -9.753  -16.668 81.393  1.00 22.48 ? 300 HIS   A N   1 
ATOM   1876 C  CA  . HIS   A 1 272 ? -10.387 -16.134 80.193  1.00 20.04 ? 300 HIS   A CA  1 
ATOM   1877 C  C   . HIS   A 1 272 ? -9.520  -16.302 78.954  1.00 22.58 ? 300 HIS   A C   1 
ATOM   1878 O  O   . HIS   A 1 272 ? -10.053 -16.373 77.836  1.00 20.73 ? 300 HIS   A O   1 
ATOM   1879 C  CB  . HIS   A 1 272 ? -10.738 -14.665 80.408  1.00 19.26 ? 300 HIS   A CB  1 
ATOM   1880 C  CG  . HIS   A 1 272 ? -11.934 -14.469 81.282  1.00 19.09 ? 300 HIS   A CG  1 
ATOM   1881 N  ND1 . HIS   A 1 272 ? -13.205 -14.320 80.778  1.00 18.25 ? 300 HIS   A ND1 1 
ATOM   1882 C  CD2 . HIS   A 1 272 ? -12.057 -14.439 82.630  1.00 21.89 ? 300 HIS   A CD2 1 
ATOM   1883 C  CE1 . HIS   A 1 272 ? -14.060 -14.183 81.776  1.00 22.02 ? 300 HIS   A CE1 1 
ATOM   1884 N  NE2 . HIS   A 1 272 ? -13.389 -14.261 82.911  1.00 19.68 ? 300 HIS   A NE2 1 
ATOM   1885 N  N   . ASN   A 1 273 ? -8.197  -16.391 79.131  1.00 17.51 ? 301 ASN   A N   1 
ATOM   1886 C  CA  . ASN   A 1 273 ? -7.266  -16.564 78.025  1.00 20.51 ? 301 ASN   A CA  1 
ATOM   1887 C  C   . ASN   A 1 273 ? -7.054  -18.024 77.644  1.00 23.14 ? 301 ASN   A C   1 
ATOM   1888 O  O   . ASN   A 1 273 ? -6.469  -18.296 76.582  1.00 22.48 ? 301 ASN   A O   1 
ATOM   1889 C  CB  . ASN   A 1 273 ? -5.894  -15.935 78.370  1.00 19.55 ? 301 ASN   A CB  1 
ATOM   1890 C  CG  . ASN   A 1 273 ? -5.041  -15.709 77.147  1.00 18.48 ? 301 ASN   A CG  1 
ATOM   1891 O  OD1 . ASN   A 1 273 ? -5.452  -14.998 76.227  1.00 20.64 ? 301 ASN   A OD1 1 
ATOM   1892 N  ND2 . ASN   A 1 273 ? -3.852  -16.308 77.118  1.00 16.28 ? 301 ASN   A ND2 1 
ATOM   1893 N  N   . GLU   A 1 274 ? -7.517  -18.962 78.471  1.00 20.76 ? 302 GLU   A N   1 
ATOM   1894 C  CA  . GLU   A 1 274 ? -7.230  -20.384 78.285  1.00 21.05 ? 302 GLU   A CA  1 
ATOM   1895 C  C   . GLU   A 1 274 ? -5.727  -20.642 78.413  1.00 20.06 ? 302 GLU   A C   1 
ATOM   1896 O  O   . GLU   A 1 274 ? -5.111  -21.283 77.565  1.00 25.77 ? 302 GLU   A O   1 
ATOM   1897 C  CB  . GLU   A 1 274 ? -7.765  -20.912 76.948  1.00 22.23 ? 302 GLU   A CB  1 
ATOM   1898 C  CG  . GLU   A 1 274 ? -9.301  -21.161 76.928  1.00 24.44 ? 302 GLU   A CG  1 
ATOM   1899 C  CD  . GLU   A 1 274 ? -9.768  -22.006 75.746  1.00 24.53 ? 302 GLU   A CD  1 
ATOM   1900 O  OE1 . GLU   A 1 274 ? -8.942  -22.753 75.163  1.00 22.54 ? 302 GLU   A OE1 1 
ATOM   1901 O  OE2 . GLU   A 1 274 ? -10.973 -21.939 75.412  1.00 23.74 ? 302 GLU   A OE2 1 
ATOM   1902 N  N   . GLY   A 1 275 ? -5.136  -20.111 79.475  1.00 13.92 ? 303 GLY   A N   1 
ATOM   1903 C  CA  . GLY   A 1 275 ? -3.765  -20.413 79.815  1.00 21.09 ? 303 GLY   A CA  1 
ATOM   1904 C  C   . GLY   A 1 275 ? -2.849  -19.225 79.616  1.00 23.97 ? 303 GLY   A C   1 
ATOM   1905 O  O   . GLY   A 1 275 ? -3.280  -18.085 79.402  1.00 18.51 ? 303 GLY   A O   1 
ATOM   1906 N  N   . ALA   A 1 276 ? -1.553  -19.527 79.679  1.00 16.57 ? 304 ALA   A N   1 
ATOM   1907 C  CA  . ALA   A 1 276 ? -0.518  -18.509 79.679  1.00 15.69 ? 304 ALA   A CA  1 
ATOM   1908 C  C   . ALA   A 1 276 ? -0.554  -17.673 78.408  1.00 17.38 ? 304 ALA   A C   1 
ATOM   1909 O  O   . ALA   A 1 276 ? -0.951  -18.144 77.341  1.00 18.22 ? 304 ALA   A O   1 
ATOM   1910 C  CB  . ALA   A 1 276 ? 0.856   -19.172 79.815  1.00 19.55 ? 304 ALA   A CB  1 
ATOM   1911 N  N   . GLY   A 1 277 ? -0.114  -16.421 78.523  1.00 18.20 ? 305 GLY   A N   1 
ATOM   1912 C  CA  . GLY   A 1 277 ? -0.034  -15.554 77.361  1.00 18.16 ? 305 GLY   A CA  1 
ATOM   1913 C  C   . GLY   A 1 277 ? 0.474   -14.186 77.760  1.00 20.98 ? 305 GLY   A C   1 
ATOM   1914 O  O   . GLY   A 1 277 ? 0.667   -13.892 78.940  1.00 20.86 ? 305 GLY   A O   1 
ATOM   1915 N  N   . LEU   A 1 278 ? 0.676   -13.341 76.749  1.00 16.68 ? 306 LEU   A N   1 
ATOM   1916 C  CA  . LEU   A 1 278 ? 1.098   -11.968 76.982  1.00 17.23 ? 306 LEU   A CA  1 
ATOM   1917 C  C   . LEU   A 1 278 ? -0.037  -11.155 77.613  1.00 20.50 ? 306 LEU   A C   1 
ATOM   1918 O  O   . LEU   A 1 278 ? -1.151  -11.097 77.070  1.00 22.11 ? 306 LEU   A O   1 
ATOM   1919 C  CB  . LEU   A 1 278 ? 1.554   -11.338 75.671  1.00 15.89 ? 306 LEU   A CB  1 
ATOM   1920 C  CG  . LEU   A 1 278 ? 2.196   -9.944  75.810  1.00 23.80 ? 306 LEU   A CG  1 
ATOM   1921 C  CD1 . LEU   A 1 278 ? 3.394   -9.781  74.872  1.00 23.23 ? 306 LEU   A CD1 1 
ATOM   1922 C  CD2 . LEU   A 1 278 ? 1.204   -8.827  75.550  1.00 18.82 ? 306 LEU   A CD2 1 
ATOM   1923 N  N   . GLN   A 1 279 ? 0.257   -10.513 78.751  1.00 15.45 ? 307 GLN   A N   1 
ATOM   1924 C  CA  . GLN   A 1 279 ? -0.723  -9.703  79.461  1.00 17.38 ? 307 GLN   A CA  1 
ATOM   1925 C  C   . GLN   A 1 279 ? -0.774  -8.262  78.943  1.00 19.74 ? 307 GLN   A C   1 
ATOM   1926 O  O   . GLN   A 1 279 ? -1.855  -7.742  78.652  1.00 22.14 ? 307 GLN   A O   1 
ATOM   1927 C  CB  . GLN   A 1 279 ? -0.415  -9.709  80.959  1.00 19.76 ? 307 GLN   A CB  1 
ATOM   1928 C  CG  . GLN   A 1 279 ? -1.478  -9.011  81.803  1.00 17.98 ? 307 GLN   A CG  1 
ATOM   1929 C  CD  . GLN   A 1 279 ? -0.966  -8.516  83.159  1.00 20.16 ? 307 GLN   A CD  1 
ATOM   1930 O  OE1 . GLN   A 1 279 ? 0.091   -7.883  83.247  1.00 19.70 ? 307 GLN   A OE1 1 
ATOM   1931 N  NE2 . GLN   A 1 279 ? -1.732  -8.783  84.213  1.00 22.87 ? 307 GLN   A NE2 1 
ATOM   1932 N  N   . HIS   A 1 280 ? 0.369   -7.580  78.844  1.00 20.89 ? 308 HIS   A N   1 
ATOM   1933 C  CA  . HIS   A 1 280 ? 0.318   -6.204  78.369  1.00 18.89 ? 308 HIS   A CA  1 
ATOM   1934 C  C   . HIS   A 1 280 ? 1.622   -5.770  77.725  1.00 21.51 ? 308 HIS   A C   1 
ATOM   1935 O  O   . HIS   A 1 280 ? 2.701   -6.299  78.002  1.00 22.33 ? 308 HIS   A O   1 
ATOM   1936 C  CB  . HIS   A 1 280 ? -0.071  -5.213  79.477  1.00 22.07 ? 308 HIS   A CB  1 
ATOM   1937 C  CG  . HIS   A 1 280 ? 0.962   -5.004  80.544  1.00 25.87 ? 308 HIS   A CG  1 
ATOM   1938 N  ND1 . HIS   A 1 280 ? 1.050   -5.804  81.663  1.00 24.47 ? 308 HIS   A ND1 1 
ATOM   1939 C  CD2 . HIS   A 1 280 ? 1.892   -4.028  80.704  1.00 20.13 ? 308 HIS   A CD2 1 
ATOM   1940 C  CE1 . HIS   A 1 280 ? 2.010   -5.350  82.449  1.00 27.31 ? 308 HIS   A CE1 1 
ATOM   1941 N  NE2 . HIS   A 1 280 ? 2.540   -4.276  81.887  1.00 20.10 ? 308 HIS   A NE2 1 
ATOM   1942 N  N   . LEU   A 1 281 ? 1.475   -4.804  76.827  1.00 19.87 ? 309 LEU   A N   1 
ATOM   1943 C  CA  . LEU   A 1 281 ? 2.567   -4.138  76.147  1.00 22.03 ? 309 LEU   A CA  1 
ATOM   1944 C  C   . LEU   A 1 281 ? 2.695   -2.748  76.741  1.00 20.11 ? 309 LEU   A C   1 
ATOM   1945 O  O   . LEU   A 1 281 ? 1.714   -1.992  76.757  1.00 19.74 ? 309 LEU   A O   1 
ATOM   1946 C  CB  . LEU   A 1 281 ? 2.283   -4.045  74.646  1.00 19.16 ? 309 LEU   A CB  1 
ATOM   1947 C  CG  . LEU   A 1 281 ? 1.918   -5.392  74.025  1.00 20.72 ? 309 LEU   A CG  1 
ATOM   1948 C  CD1 . LEU   A 1 281 ? 1.293   -5.213  72.643  1.00 17.40 ? 309 LEU   A CD1 1 
ATOM   1949 C  CD2 . LEU   A 1 281 ? 3.160   -6.293  73.957  1.00 20.61 ? 309 LEU   A CD2 1 
ATOM   1950 N  N   . ALA   A 1 282 ? 3.884   -2.398  77.226  1.00 19.91 ? 310 ALA   A N   1 
ATOM   1951 C  CA  . ALA   A 1 282 ? 4.124   -1.026  77.668  1.00 20.51 ? 310 ALA   A CA  1 
ATOM   1952 C  C   . ALA   A 1 282 ? 4.769   -0.235  76.546  1.00 19.76 ? 310 ALA   A C   1 
ATOM   1953 O  O   . ALA   A 1 282 ? 5.862   -0.576  76.074  1.00 19.83 ? 310 ALA   A O   1 
ATOM   1954 C  CB  . ALA   A 1 282 ? 4.997   -0.945  78.906  1.00 18.88 ? 310 ALA   A CB  1 
ATOM   1955 N  N   . LEU   A 1 283 ? 4.104   0.835   76.154  1.00 23.31 ? 311 LEU   A N   1 
ATOM   1956 C  CA  . LEU   A 1 283 ? 4.512   1.654   75.029  1.00 19.39 ? 311 LEU   A CA  1 
ATOM   1957 C  C   . LEU   A 1 283 ? 5.057   2.962   75.600  1.00 19.31 ? 311 LEU   A C   1 
ATOM   1958 O  O   . LEU   A 1 283 ? 4.358   3.661   76.349  1.00 18.77 ? 311 LEU   A O   1 
ATOM   1959 C  CB  . LEU   A 1 283 ? 3.331   1.875   74.086  1.00 19.08 ? 311 LEU   A CB  1 
ATOM   1960 C  CG  . LEU   A 1 283 ? 2.427   0.629   73.936  1.00 18.82 ? 311 LEU   A CG  1 
ATOM   1961 C  CD1 . LEU   A 1 283 ? 1.252   0.918   73.061  1.00 15.57 ? 311 LEU   A CD1 1 
ATOM   1962 C  CD2 . LEU   A 1 283 ? 3.146   -0.569  73.369  1.00 15.06 ? 311 LEU   A CD2 1 
ATOM   1963 N  N   . MET   A 1 284 ? 6.317   3.264   75.292  1.00 20.25 ? 312 MET   A N   1 
ATOM   1964 C  CA  . MET   A 1 284 ? 6.893   4.528   75.721  1.00 23.09 ? 312 MET   A CA  1 
ATOM   1965 C  C   . MET   A 1 284 ? 6.389   5.659   74.841  1.00 19.96 ? 312 MET   A C   1 
ATOM   1966 O  O   . MET   A 1 284 ? 6.388   5.567   73.607  1.00 18.78 ? 312 MET   A O   1 
ATOM   1967 C  CB  A MET   A 1 284 ? 8.419   4.475   75.698  0.58 23.63 ? 312 MET   A CB  1 
ATOM   1968 C  CB  B MET   A 1 284 ? 8.423   4.468   75.683  0.42 22.25 ? 312 MET   A CB  1 
ATOM   1969 C  CG  A MET   A 1 284 ? 9.068   5.645   76.432  0.58 21.63 ? 312 MET   A CG  1 
ATOM   1970 C  CG  B MET   A 1 284 ? 9.128   5.786   76.036  0.42 22.56 ? 312 MET   A CG  1 
ATOM   1971 S  SD  A MET   A 1 284 ? 10.861  5.547   76.419  0.58 30.20 ? 312 MET   A SD  1 
ATOM   1972 S  SD  B MET   A 1 284 ? 9.601   6.776   74.587  0.42 27.09 ? 312 MET   A SD  1 
ATOM   1973 C  CE  A MET   A 1 284 ? 11.149  4.564   77.886  0.58 24.10 ? 312 MET   A CE  1 
ATOM   1974 C  CE  B MET   A 1 284 ? 10.230  8.265   75.364  0.42 25.95 ? 312 MET   A CE  1 
ATOM   1975 N  N   . SER   A 1 285 ? 5.964   6.729   75.479  1.00 23.40 ? 313 SER   A N   1 
ATOM   1976 C  CA  . SER   A 1 285 ? 5.583   7.941   74.781  1.00 20.51 ? 313 SER   A CA  1 
ATOM   1977 C  C   . SER   A 1 285 ? 6.586   9.037   75.107  1.00 25.87 ? 313 SER   A C   1 
ATOM   1978 O  O   . SER   A 1 285 ? 6.982   9.190   76.270  1.00 22.64 ? 313 SER   A O   1 
ATOM   1979 C  CB  . SER   A 1 285 ? 4.187   8.384   75.194  1.00 18.15 ? 313 SER   A CB  1 
ATOM   1980 O  OG  . SER   A 1 285 ? 4.055   9.782   75.024  1.00 23.05 ? 313 SER   A OG  1 
ATOM   1981 N  N   . GLU   A 1 286 ? 6.985   9.800   74.078  1.00 22.87 ? 314 GLU   A N   1 
ATOM   1982 C  CA  . GLU   A 1 286 ? 7.862   10.957  74.281  1.00 23.36 ? 314 GLU   A CA  1 
ATOM   1983 C  C   . GLU   A 1 286 ? 7.165   12.095  75.000  1.00 27.44 ? 314 GLU   A C   1 
ATOM   1984 O  O   . GLU   A 1 286 ? 7.829   13.047  75.426  1.00 25.03 ? 314 GLU   A O   1 
ATOM   1985 C  CB  . GLU   A 1 286 ? 8.381   11.495  72.948  1.00 20.23 ? 314 GLU   A CB  1 
ATOM   1986 C  CG  . GLU   A 1 286 ? 7.287   12.041  72.091  1.00 23.51 ? 314 GLU   A CG  1 
ATOM   1987 C  CD  . GLU   A 1 286 ? 7.788   12.734  70.829  1.00 28.02 ? 314 GLU   A CD  1 
ATOM   1988 O  OE1 . GLU   A 1 286 ? 8.971   12.561  70.472  1.00 28.11 ? 314 GLU   A OE1 1 
ATOM   1989 O  OE2 . GLU   A 1 286 ? 6.980   13.447  70.189  1.00 33.51 ? 314 GLU   A OE2 1 
ATOM   1990 N  N   . ASP   A 1 287 ? 5.840   12.042  75.104  1.00 27.04 ? 315 ASP   A N   1 
ATOM   1991 C  CA  . ASP   A 1 287 ? 5.084   13.103  75.768  1.00 24.20 ? 315 ASP   A CA  1 
ATOM   1992 C  C   . ASP   A 1 287 ? 3.763   12.448  76.167  1.00 23.64 ? 315 ASP   A C   1 
ATOM   1993 O  O   . ASP   A 1 287 ? 2.788   12.484  75.418  1.00 22.87 ? 315 ASP   A O   1 
ATOM   1994 C  CB  . ASP   A 1 287 ? 4.883   14.317  74.882  1.00 24.55 ? 315 ASP   A CB  1 
ATOM   1995 C  CG  . ASP   A 1 287 ? 3.983   15.373  75.518  1.00 26.10 ? 315 ASP   A CG  1 
ATOM   1996 O  OD1 . ASP   A 1 287 ? 3.603   15.258  76.708  1.00 23.10 ? 315 ASP   A OD1 1 
ATOM   1997 O  OD2 . ASP   A 1 287 ? 3.677   16.346  74.814  1.00 26.54 ? 315 ASP   A OD2 1 
ATOM   1998 N  N   . ILE   A 1 288 ? 3.776   11.812  77.335  1.00 24.64 ? 316 ILE   A N   1 
ATOM   1999 C  CA  . ILE   A 1 288 ? 2.635   11.023  77.732  1.00 22.73 ? 316 ILE   A CA  1 
ATOM   2000 C  C   . ILE   A 1 288 ? 1.419   11.912  77.905  1.00 26.48 ? 316 ILE   A C   1 
ATOM   2001 O  O   . ILE   A 1 288 ? 0.283   11.426  77.857  1.00 27.48 ? 316 ILE   A O   1 
ATOM   2002 C  CB  . ILE   A 1 288 ? 2.964   10.212  79.006  1.00 22.84 ? 316 ILE   A CB  1 
ATOM   2003 C  CG1 . ILE   A 1 288 ? 1.830   9.225   79.325  1.00 26.22 ? 316 ILE   A CG1 1 
ATOM   2004 C  CG2 . ILE   A 1 288 ? 3.292   11.139  80.180  1.00 22.67 ? 316 ILE   A CG2 1 
ATOM   2005 C  CD1 . ILE   A 1 288 ? 2.116   8.318   80.502  1.00 22.27 ? 316 ILE   A CD1 1 
ATOM   2006 N  N   . PHE   A 1 289 ? 1.626   13.219  78.065  1.00 23.58 ? 317 PHE   A N   1 
ATOM   2007 C  CA  . PHE   A 1 289 ? 0.485   14.114  78.202  1.00 28.42 ? 317 PHE   A CA  1 
ATOM   2008 C  C   . PHE   A 1 289 ? -0.237  14.256  76.876  1.00 22.72 ? 317 PHE   A C   1 
ATOM   2009 O  O   . PHE   A 1 289 ? -1.460  14.108  76.809  1.00 23.51 ? 317 PHE   A O   1 
ATOM   2010 C  CB  . PHE   A 1 289 ? 0.931   15.475  78.747  1.00 30.13 ? 317 PHE   A CB  1 
ATOM   2011 C  CG  . PHE   A 1 289 ? 1.325   15.432  80.196  1.00 33.50 ? 317 PHE   A CG  1 
ATOM   2012 C  CD1 . PHE   A 1 289 ? 0.697   14.563  81.062  1.00 33.15 ? 317 PHE   A CD1 1 
ATOM   2013 C  CD2 . PHE   A 1 289 ? 2.315   16.258  80.692  1.00 38.49 ? 317 PHE   A CD2 1 
ATOM   2014 C  CE1 . PHE   A 1 289 ? 1.059   14.506  82.402  1.00 40.19 ? 317 PHE   A CE1 1 
ATOM   2015 C  CE2 . PHE   A 1 289 ? 2.683   16.201  82.032  1.00 41.67 ? 317 PHE   A CE2 1 
ATOM   2016 C  CZ  . PHE   A 1 289 ? 2.054   15.318  82.884  1.00 36.92 ? 317 PHE   A CZ  1 
ATOM   2017 N  N   . ARG   A 1 290 ? 0.504   14.526  75.801  1.00 23.01 ? 318 ARG   A N   1 
ATOM   2018 C  CA  . ARG   A 1 290 ? -0.141  14.595  74.499  1.00 27.67 ? 318 ARG   A CA  1 
ATOM   2019 C  C   . ARG   A 1 290 ? -0.763  13.252  74.128  1.00 25.41 ? 318 ARG   A C   1 
ATOM   2020 O  O   . ARG   A 1 290 ? -1.921  13.193  73.701  1.00 21.44 ? 318 ARG   A O   1 
ATOM   2021 C  CB  . ARG   A 1 290 ? 0.847   15.061  73.436  1.00 27.10 ? 318 ARG   A CB  1 
ATOM   2022 C  CG  . ARG   A 1 290 ? 0.248   15.033  72.064  1.00 28.34 ? 318 ARG   A CG  1 
ATOM   2023 C  CD  . ARG   A 1 290 ? 1.041   15.868  71.090  1.00 28.09 ? 318 ARG   A CD  1 
ATOM   2024 N  NE  . ARG   A 1 290 ? 2.424   15.425  71.026  1.00 36.29 ? 318 ARG   A NE  1 
ATOM   2025 C  CZ  . ARG   A 1 290 ? 2.815   14.336  70.368  1.00 37.54 ? 318 ARG   A CZ  1 
ATOM   2026 N  NH1 . ARG   A 1 290 ? 1.911   13.613  69.722  1.00 35.14 ? 318 ARG   A NH1 1 
ATOM   2027 N  NH2 . ARG   A 1 290 ? 4.098   13.980  70.348  1.00 37.54 ? 318 ARG   A NH2 1 
ATOM   2028 N  N   . THR   A 1 291 ? -0.018  12.156  74.312  1.00 24.78 ? 319 THR   A N   1 
ATOM   2029 C  CA  . THR   A 1 291 ? -0.549  10.833  73.993  1.00 20.93 ? 319 THR   A CA  1 
ATOM   2030 C  C   . THR   A 1 291 ? -1.877  10.575  74.678  1.00 22.58 ? 319 THR   A C   1 
ATOM   2031 O  O   . THR   A 1 291 ? -2.834  10.086  74.066  1.00 20.36 ? 319 THR   A O   1 
ATOM   2032 C  CB  . THR   A 1 291 ? 0.429   9.746   74.427  1.00 22.71 ? 319 THR   A CB  1 
ATOM   2033 O  OG1 . THR   A 1 291 ? 1.686   9.979   73.814  1.00 21.83 ? 319 THR   A OG1 1 
ATOM   2034 C  CG2 . THR   A 1 291 ? -0.111  8.368   74.020  1.00 19.70 ? 319 THR   A CG2 1 
ATOM   2035 N  N   . LEU   A 1 292 ? -1.936  10.841  75.974  1.00 21.71 ? 320 LEU   A N   1 
ATOM   2036 C  CA  . LEU   A 1 292 ? -3.137  10.486  76.697  1.00 19.74 ? 320 LEU   A CA  1 
ATOM   2037 C  C   . LEU   A 1 292 ? -4.284  11.428  76.358  1.00 18.88 ? 320 LEU   A C   1 
ATOM   2038 O  O   . LEU   A 1 292 ? -5.439  10.994  76.277  1.00 25.38 ? 320 LEU   A O   1 
ATOM   2039 C  CB  . LEU   A 1 292 ? -2.843  10.458  78.184  1.00 24.67 ? 320 LEU   A CB  1 
ATOM   2040 C  CG  . LEU   A 1 292 ? -2.819  9.014   78.673  1.00 29.02 ? 320 LEU   A CG  1 
ATOM   2041 C  CD1 . LEU   A 1 292 ? -1.685  8.193   78.055  1.00 22.53 ? 320 LEU   A CD1 1 
ATOM   2042 C  CD2 . LEU   A 1 292 ? -2.702  9.051   80.150  1.00 30.38 ? 320 LEU   A CD2 1 
ATOM   2043 N  N   . ARG   A 1 293 ? -3.994  12.705  76.114  1.00 21.95 ? 321 ARG   A N   1 
ATOM   2044 C  CA  . ARG   A 1 293 ? -5.039  13.598  75.619  1.00 23.04 ? 321 ARG   A CA  1 
ATOM   2045 C  C   . ARG   A 1 293 ? -5.610  13.078  74.308  1.00 17.82 ? 321 ARG   A C   1 
ATOM   2046 O  O   . ARG   A 1 293 ? -6.823  12.916  74.172  1.00 23.34 ? 321 ARG   A O   1 
ATOM   2047 C  CB  . ARG   A 1 293 ? -4.508  15.021  75.444  1.00 23.97 ? 321 ARG   A CB  1 
ATOM   2048 C  CG  . ARG   A 1 293 ? -4.366  15.809  76.751  1.00 26.79 ? 321 ARG   A CG  1 
ATOM   2049 C  CD  . ARG   A 1 293 ? -4.103  17.290  76.496  1.00 27.63 ? 321 ARG   A CD  1 
ATOM   2050 N  NE  . ARG   A 1 293 ? -2.903  17.540  75.703  1.00 30.96 ? 321 ARG   A NE  1 
ATOM   2051 C  CZ  . ARG   A 1 293 ? -1.691  17.774  76.204  1.00 26.41 ? 321 ARG   A CZ  1 
ATOM   2052 N  NH1 . ARG   A 1 293 ? -1.492  17.780  77.518  1.00 27.54 ? 321 ARG   A NH1 1 
ATOM   2053 N  NH2 . ARG   A 1 293 ? -0.673  17.997  75.382  1.00 25.83 ? 321 ARG   A NH2 1 
ATOM   2054 N  N   . GLU   A 1 294 ? -4.744  12.789  73.337  1.00 21.16 ? 322 GLU   A N   1 
ATOM   2055 C  CA  . GLU   A 1 294 ? -5.214  12.293  72.046  1.00 23.66 ? 322 GLU   A CA  1 
ATOM   2056 C  C   . GLU   A 1 294 ? -5.968  10.975  72.189  1.00 22.06 ? 322 GLU   A C   1 
ATOM   2057 O  O   . GLU   A 1 294 ? -7.033  10.803  71.598  1.00 21.64 ? 322 GLU   A O   1 
ATOM   2058 C  CB  . GLU   A 1 294 ? -4.046  12.129  71.080  1.00 23.49 ? 322 GLU   A CB  1 
ATOM   2059 C  CG  . GLU   A 1 294 ? -3.342  13.415  70.733  1.00 26.48 ? 322 GLU   A CG  1 
ATOM   2060 C  CD  . GLU   A 1 294 ? -4.148  14.291  69.808  1.00 26.03 ? 322 GLU   A CD  1 
ATOM   2061 O  OE1 . GLU   A 1 294 ? -5.353  14.040  69.606  1.00 25.78 ? 322 GLU   A OE1 1 
ATOM   2062 O  OE2 . GLU   A 1 294 ? -3.562  15.238  69.261  1.00 32.71 ? 322 GLU   A OE2 1 
ATOM   2063 N  N   . MET   A 1 295 ? -5.430  10.028  72.964  1.00 23.11 ? 323 MET   A N   1 
ATOM   2064 C  CA  . MET   A 1 295 ? -6.107  8.740   73.097  1.00 20.13 ? 323 MET   A CA  1 
ATOM   2065 C  C   . MET   A 1 295 ? -7.462  8.893   73.773  1.00 22.46 ? 323 MET   A C   1 
ATOM   2066 O  O   . MET   A 1 295 ? -8.440  8.248   73.375  1.00 16.63 ? 323 MET   A O   1 
ATOM   2067 C  CB  . MET   A 1 295 ? -5.244  7.751   73.871  1.00 17.31 ? 323 MET   A CB  1 
ATOM   2068 C  CG  . MET   A 1 295 ? -3.978  7.313   73.143  1.00 23.57 ? 323 MET   A CG  1 
ATOM   2069 S  SD  . MET   A 1 295 ? -3.114  5.953   73.969  1.00 22.94 ? 323 MET   A SD  1 
ATOM   2070 C  CE  . MET   A 1 295 ? -4.366  4.662   73.939  1.00 12.93 ? 323 MET   A CE  1 
ATOM   2071 N  N   . ARG   A 1 296 ? -7.533  9.735   74.808  1.00 25.00 ? 324 ARG   A N   1 
ATOM   2072 C  CA  . ARG   A 1 296 ? -8.769  9.876   75.566  1.00 23.30 ? 324 ARG   A CA  1 
ATOM   2073 C  C   . ARG   A 1 296 ? -9.850  10.549  74.733  1.00 23.81 ? 324 ARG   A C   1 
ATOM   2074 O  O   . ARG   A 1 296 ? -11.022 10.184  74.832  1.00 23.42 ? 324 ARG   A O   1 
ATOM   2075 C  CB  . ARG   A 1 296 ? -8.522  10.669  76.854  1.00 26.79 ? 324 ARG   A CB  1 
ATOM   2076 C  CG  . ARG   A 1 296 ? -7.861  9.883   77.987  1.00 26.42 ? 324 ARG   A CG  1 
ATOM   2077 C  CD  . ARG   A 1 296 ? -8.181  10.515  79.328  1.00 29.15 ? 324 ARG   A CD  1 
ATOM   2078 N  NE  . ARG   A 1 296 ? -7.705  9.723   80.456  1.00 33.17 ? 324 ARG   A NE  1 
ATOM   2079 C  CZ  . ARG   A 1 296 ? -8.438  8.827   81.112  1.00 31.34 ? 324 ARG   A CZ  1 
ATOM   2080 N  NH1 . ARG   A 1 296 ? -9.688  8.616   80.759  1.00 30.33 ? 324 ARG   A NH1 1 
ATOM   2081 N  NH2 . ARG   A 1 296 ? -7.921  8.149   82.133  1.00 33.58 ? 324 ARG   A NH2 1 
ATOM   2082 N  N   . LYS   A 1 297 ? -9.473  11.529  73.907  1.00 22.09 ? 325 LYS   A N   1 
ATOM   2083 C  CA  . LYS   A 1 297 ? -10.414 12.143  72.975  1.00 26.67 ? 325 LYS   A CA  1 
ATOM   2084 C  C   . LYS   A 1 297 ? -11.104 11.124  72.090  1.00 26.07 ? 325 LYS   A C   1 
ATOM   2085 O  O   . LYS   A 1 297 ? -12.196 11.403  71.569  1.00 17.91 ? 325 LYS   A O   1 
ATOM   2086 C  CB  . LYS   A 1 297 ? -9.711  13.144  72.058  1.00 21.24 ? 325 LYS   A CB  1 
ATOM   2087 C  CG  . LYS   A 1 297 ? -9.040  14.281  72.761  1.00 31.08 ? 325 LYS   A CG  1 
ATOM   2088 C  CD  . LYS   A 1 297 ? -9.060  15.539  71.932  1.00 29.70 ? 325 LYS   A CD  1 
ATOM   2089 C  CE  . LYS   A 1 297 ? -7.666  15.898  71.461  1.00 27.10 ? 325 LYS   A CE  1 
ATOM   2090 N  NZ  . LYS   A 1 297 ? -7.669  16.659  70.189  1.00 35.37 ? 325 LYS   A NZ  1 
ATOM   2091 N  N   . ARG   A 1 298 ? -10.487 9.958   71.897  1.00 19.04 ? 326 ARG   A N   1 
ATOM   2092 C  CA  . ARG   A 1 298 ? -10.949 8.993   70.910  1.00 21.74 ? 326 ARG   A CA  1 
ATOM   2093 C  C   . ARG   A 1 298 ? -11.476 7.699   71.507  1.00 17.95 ? 326 ARG   A C   1 
ATOM   2094 O  O   . ARG   A 1 298 ? -12.036 6.878   70.766  1.00 15.02 ? 326 ARG   A O   1 
ATOM   2095 C  CB  . ARG   A 1 298 ? -9.822  8.672   69.924  1.00 21.81 ? 326 ARG   A CB  1 
ATOM   2096 C  CG  . ARG   A 1 298 ? -9.370  9.878   69.114  1.00 21.39 ? 326 ARG   A CG  1 
ATOM   2097 C  CD  . ARG   A 1 298 ? -8.072  9.570   68.412  1.00 21.73 ? 326 ARG   A CD  1 
ATOM   2098 N  NE  . ARG   A 1 298 ? -7.702  10.571  67.417  1.00 21.15 ? 326 ARG   A NE  1 
ATOM   2099 C  CZ  . ARG   A 1 298 ? -7.077  11.707  67.705  1.00 23.22 ? 326 ARG   A CZ  1 
ATOM   2100 N  NH1 . ARG   A 1 298 ? -6.783  11.996  68.960  1.00 21.13 ? 326 ARG   A NH1 1 
ATOM   2101 N  NH2 . ARG   A 1 298 ? -6.764  12.560  66.740  1.00 21.90 ? 326 ARG   A NH2 1 
ATOM   2102 N  N   . SER   A 1 299 ? -11.348 7.520   72.818  1.00 19.39 ? 327 SER   A N   1 
ATOM   2103 C  CA  . SER   A 1 299 ? -11.884 6.349   73.491  1.00 19.04 ? 327 SER   A CA  1 
ATOM   2104 C  C   . SER   A 1 299 ? -13.259 5.926   72.973  1.00 23.19 ? 327 SER   A C   1 
ATOM   2105 O  O   . SER   A 1 299 ? -13.445 4.786   72.529  1.00 18.71 ? 327 SER   A O   1 
ATOM   2106 C  CB  . SER   A 1 299 ? -11.939 6.643   74.987  1.00 21.57 ? 327 SER   A CB  1 
ATOM   2107 O  OG  . SER   A 1 299 ? -10.624 6.680   75.510  1.00 19.41 ? 327 SER   A OG  1 
ATOM   2108 N  N   . SER   A 1 300 ? -14.227 6.845   72.982  1.00 18.51 ? 328 SER   A N   1 
ATOM   2109 C  CA  . SER   A 1 300 ? -15.609 6.490   72.688  1.00 21.09 ? 328 SER   A CA  1 
ATOM   2110 C  C   . SER   A 1 300 ? -15.980 6.673   71.225  1.00 18.60 ? 328 SER   A C   1 
ATOM   2111 O  O   . SER   A 1 300 ? -17.159 6.509   70.876  1.00 20.16 ? 328 SER   A O   1 
ATOM   2112 C  CB  . SER   A 1 300 ? -16.552 7.305   73.560  1.00 24.29 ? 328 SER   A CB  1 
ATOM   2113 O  OG  . SER   A 1 300 ? -16.186 8.670   73.482  1.00 28.17 ? 328 SER   A OG  1 
ATOM   2114 N  N   . ILE   A 1 301 ? -15.017 7.008   70.369  1.00 13.54 ? 329 ILE   A N   1 
ATOM   2115 C  CA  . ILE   A 1 301 ? -15.269 7.059   68.930  1.00 13.97 ? 329 ILE   A CA  1 
ATOM   2116 C  C   . ILE   A 1 301 ? -14.329 6.108   68.182  1.00 16.52 ? 329 ILE   A C   1 
ATOM   2117 O  O   . ILE   A 1 301 ? -13.813 6.432   67.104  1.00 17.73 ? 329 ILE   A O   1 
ATOM   2118 C  CB  . ILE   A 1 301 ? -15.161 8.499   68.399  1.00 18.29 ? 329 ILE   A CB  1 
ATOM   2119 C  CG1 . ILE   A 1 301 ? -13.866 9.145   68.865  1.00 13.53 ? 329 ILE   A CG1 1 
ATOM   2120 C  CG2 . ILE   A 1 301 ? -16.405 9.319   68.842  1.00 17.23 ? 329 ILE   A CG2 1 
ATOM   2121 C  CD1 . ILE   A 1 301 ? -13.469 10.392  68.034  1.00 15.54 ? 329 ILE   A CD1 1 
ATOM   2122 N  N   . GLY   A 1 302 ? -14.148 4.901   68.724  1.00 15.00 ? 330 GLY   A N   1 
ATOM   2123 C  CA  . GLY   A 1 302 ? -13.365 3.870   68.069  1.00 15.04 ? 330 GLY   A CA  1 
ATOM   2124 C  C   . GLY   A 1 302 ? -12.036 3.563   68.738  1.00 17.65 ? 330 GLY   A C   1 
ATOM   2125 O  O   . GLY   A 1 302 ? -11.403 2.546   68.396  1.00 14.04 ? 330 GLY   A O   1 
ATOM   2126 N  N   . GLY   A 1 303 ? -11.602 4.389   69.692  1.00 15.65 ? 331 GLY   A N   1 
ATOM   2127 C  CA  . GLY   A 1 303 ? -10.320 4.211   70.347  1.00 18.72 ? 331 GLY   A CA  1 
ATOM   2128 C  C   . GLY   A 1 303 ? -10.351 3.171   71.448  1.00 18.34 ? 331 GLY   A C   1 
ATOM   2129 O  O   . GLY   A 1 303 ? -11.107 2.195   71.403  1.00 18.06 ? 331 GLY   A O   1 
ATOM   2130 N  N   . PHE   A 1 304 ? -9.521  3.387   72.459  1.00 17.13 ? 332 PHE   A N   1 
ATOM   2131 C  CA  . PHE   A 1 304 ? -9.403  2.482   73.586  1.00 20.96 ? 332 PHE   A CA  1 
ATOM   2132 C  C   . PHE   A 1 304 ? -9.912  3.155   74.852  1.00 21.83 ? 332 PHE   A C   1 
ATOM   2133 O  O   . PHE   A 1 304 ? -9.676  4.345   75.076  1.00 23.47 ? 332 PHE   A O   1 
ATOM   2134 C  CB  . PHE   A 1 304 ? -7.944  2.024   73.775  1.00 19.54 ? 332 PHE   A CB  1 
ATOM   2135 C  CG  . PHE   A 1 304 ? -7.419  1.218   72.623  1.00 19.49 ? 332 PHE   A CG  1 
ATOM   2136 C  CD1 . PHE   A 1 304 ? -7.569  -0.164  72.594  1.00 17.05 ? 332 PHE   A CD1 1 
ATOM   2137 C  CD2 . PHE   A 1 304 ? -6.784  1.846   71.554  1.00 18.20 ? 332 PHE   A CD2 1 
ATOM   2138 C  CE1 . PHE   A 1 304 ? -7.086  -0.908  71.514  1.00 16.97 ? 332 PHE   A CE1 1 
ATOM   2139 C  CE2 . PHE   A 1 304 ? -6.297  1.115   70.471  1.00 15.48 ? 332 PHE   A CE2 1 
ATOM   2140 C  CZ  . PHE   A 1 304 ? -6.441  -0.264  70.453  1.00 16.99 ? 332 PHE   A CZ  1 
ATOM   2141 N  N   . ASP   A 1 305 ? -10.630 2.384   75.659  1.00 21.27 ? 333 ASP   A N   1 
ATOM   2142 C  CA  . ASP   A 1 305 ? -11.021 2.816   76.984  1.00 21.80 ? 333 ASP   A CA  1 
ATOM   2143 C  C   . ASP   A 1 305 ? -9.848  2.686   77.941  1.00 26.17 ? 333 ASP   A C   1 
ATOM   2144 O  O   . ASP   A 1 305 ? -9.005  1.784   77.814  1.00 24.56 ? 333 ASP   A O   1 
ATOM   2145 C  CB  . ASP   A 1 305 ? -12.184 1.970   77.507  1.00 22.89 ? 333 ASP   A CB  1 
ATOM   2146 C  CG  . ASP   A 1 305 ? -13.472 2.211   76.761  1.00 23.48 ? 333 ASP   A CG  1 
ATOM   2147 O  OD1 . ASP   A 1 305 ? -13.487 3.087   75.862  1.00 23.14 ? 333 ASP   A OD1 1 
ATOM   2148 O  OD2 . ASP   A 1 305 ? -14.478 1.534   77.105  1.00 23.22 ? 333 ASP   A OD2 1 
ATOM   2149 N  N   . PHE   A 1 306 ? -9.810  3.576   78.927  1.00 24.47 ? 334 PHE   A N   1 
ATOM   2150 C  CA  . PHE   A 1 306 ? -8.800  3.479   79.963  1.00 22.22 ? 334 PHE   A CA  1 
ATOM   2151 C  C   . PHE   A 1 306 ? -9.407  2.923   81.247  1.00 31.19 ? 334 PHE   A C   1 
ATOM   2152 O  O   . PHE   A 1 306 ? -10.624 2.961   81.460  1.00 33.07 ? 334 PHE   A O   1 
ATOM   2153 C  CB  . PHE   A 1 306 ? -8.144  4.839   80.206  1.00 26.09 ? 334 PHE   A CB  1 
ATOM   2154 C  CG  . PHE   A 1 306 ? -7.241  5.262   79.089  1.00 24.39 ? 334 PHE   A CG  1 
ATOM   2155 C  CD1 . PHE   A 1 306 ? -5.911  4.870   79.073  1.00 17.73 ? 334 PHE   A CD1 1 
ATOM   2156 C  CD2 . PHE   A 1 306 ? -7.730  6.016   78.031  1.00 23.98 ? 334 PHE   A CD2 1 
ATOM   2157 C  CE1 . PHE   A 1 306 ? -5.086  5.235   78.049  1.00 16.18 ? 334 PHE   A CE1 1 
ATOM   2158 C  CE2 . PHE   A 1 306 ? -6.896  6.387   76.988  1.00 24.07 ? 334 PHE   A CE2 1 
ATOM   2159 C  CZ  . PHE   A 1 306 ? -5.571  6.000   77.004  1.00 20.90 ? 334 PHE   A CZ  1 
ATOM   2160 N  N   . MET   A 1 307 ? -8.536  2.363   82.088  1.00 20.46 ? 335 MET   A N   1 
ATOM   2161 C  CA  . MET   A 1 307 ? -8.952  1.847   83.377  1.00 29.58 ? 335 MET   A CA  1 
ATOM   2162 C  C   . MET   A 1 307 ? -9.444  2.994   84.262  1.00 33.57 ? 335 MET   A C   1 
ATOM   2163 O  O   . MET   A 1 307 ? -9.078  4.153   84.053  1.00 34.15 ? 335 MET   A O   1 
ATOM   2164 C  CB  . MET   A 1 307 ? -7.785  1.117   84.050  1.00 27.18 ? 335 MET   A CB  1 
ATOM   2165 C  CG  . MET   A 1 307 ? -7.491  -0.262  83.491  1.00 33.19 ? 335 MET   A CG  1 
ATOM   2166 S  SD  . MET   A 1 307 ? -8.750  -1.452  83.977  1.00 33.77 ? 335 MET   A SD  1 
ATOM   2167 C  CE  . MET   A 1 307 ? -7.982  -2.999  83.476  1.00 38.12 ? 335 MET   A CE  1 
ATOM   2168 N  N   . PRO   A 1 308 ? -10.254 2.687   85.275  1.00 32.54 ? 336 PRO   A N   1 
ATOM   2169 C  CA  . PRO   A 1 308 ? -10.783 3.748   86.142  1.00 34.01 ? 336 PRO   A CA  1 
ATOM   2170 C  C   . PRO   A 1 308 ? -9.675  4.597   86.755  1.00 40.63 ? 336 PRO   A C   1 
ATOM   2171 O  O   . PRO   A 1 308 ? -8.608  4.098   87.131  1.00 36.53 ? 336 PRO   A O   1 
ATOM   2172 C  CB  . PRO   A 1 308 ? -11.559 2.971   87.211  1.00 30.40 ? 336 PRO   A CB  1 
ATOM   2173 C  CG  . PRO   A 1 308 ? -11.988 1.718   86.506  1.00 35.74 ? 336 PRO   A CG  1 
ATOM   2174 C  CD  . PRO   A 1 308 ? -10.823 1.369   85.607  1.00 36.12 ? 336 PRO   A CD  1 
ATOM   2175 N  N   . SER   A 1 309 ? -9.936  5.899   86.830  1.00 40.39 ? 337 SER   A N   1 
ATOM   2176 C  CA  . SER   A 1 309 ? -8.983  6.808   87.439  1.00 41.86 ? 337 SER   A CA  1 
ATOM   2177 C  C   . SER   A 1 309 ? -8.817  6.484   88.927  1.00 40.55 ? 337 SER   A C   1 
ATOM   2178 O  O   . SER   A 1 309 ? -9.712  5.913   89.555  1.00 39.22 ? 337 SER   A O   1 
ATOM   2179 C  CB  . SER   A 1 309 ? -9.439  8.256   87.264  1.00 44.15 ? 337 SER   A CB  1 
ATOM   2180 O  OG  . SER   A 1 309 ? -9.003  8.804   86.027  1.00 38.06 ? 337 SER   A OG  1 
ATOM   2181 N  N   . PRO   A 1 310 ? -7.664  6.808   89.505  1.00 47.05 ? 338 PRO   A N   1 
ATOM   2182 C  CA  . PRO   A 1 310 ? -7.503  6.700   90.957  1.00 51.00 ? 338 PRO   A CA  1 
ATOM   2183 C  C   . PRO   A 1 310 ? -8.210  7.849   91.651  1.00 47.22 ? 338 PRO   A C   1 
ATOM   2184 O  O   . PRO   A 1 310 ? -8.517  8.863   91.010  1.00 52.19 ? 338 PRO   A O   1 
ATOM   2185 C  CB  . PRO   A 1 310 ? -5.980  6.780   91.145  1.00 42.30 ? 338 PRO   A CB  1 
ATOM   2186 C  CG  . PRO   A 1 310 ? -5.513  7.570   89.987  1.00 44.15 ? 338 PRO   A CG  1 
ATOM   2187 C  CD  . PRO   A 1 310 ? -6.410  7.199   88.838  1.00 43.57 ? 338 PRO   A CD  1 
ATOM   2188 N  N   . PRO   A 1 311 ? -8.486  7.739   92.949  1.00 47.09 ? 339 PRO   A N   1 
ATOM   2189 C  CA  . PRO   A 1 311 ? -9.172  8.826   93.652  1.00 49.74 ? 339 PRO   A CA  1 
ATOM   2190 C  C   . PRO   A 1 311 ? -8.262  10.034  93.784  1.00 54.81 ? 339 PRO   A C   1 
ATOM   2191 O  O   . PRO   A 1 311 ? -7.029  9.894   93.725  1.00 52.28 ? 339 PRO   A O   1 
ATOM   2192 C  CB  . PRO   A 1 311 ? -9.489  8.214   95.020  1.00 51.35 ? 339 PRO   A CB  1 
ATOM   2193 C  CG  . PRO   A 1 311 ? -8.407  7.225   95.221  1.00 54.48 ? 339 PRO   A CG  1 
ATOM   2194 C  CD  . PRO   A 1 311 ? -8.128  6.639   93.863  1.00 48.97 ? 339 PRO   A CD  1 
ATOM   2195 N  N   . PRO   A 1 312 ? -8.830  11.235  93.958  1.00 50.40 ? 340 PRO   A N   1 
ATOM   2196 C  CA  . PRO   A 1 312 ? -7.986  12.436  94.075  1.00 48.65 ? 340 PRO   A CA  1 
ATOM   2197 C  C   . PRO   A 1 312 ? -6.998  12.372  95.223  1.00 47.85 ? 340 PRO   A C   1 
ATOM   2198 O  O   . PRO   A 1 312 ? -5.932  12.997  95.138  1.00 44.20 ? 340 PRO   A O   1 
ATOM   2199 C  CB  . PRO   A 1 312 ? -9.009  13.564  94.270  1.00 44.61 ? 340 PRO   A CB  1 
ATOM   2200 C  CG  . PRO   A 1 312 ? -10.247 12.873  94.766  1.00 47.51 ? 340 PRO   A CG  1 
ATOM   2201 C  CD  . PRO   A 1 312 ? -10.262 11.567  94.041  1.00 54.08 ? 340 PRO   A CD  1 
ATOM   2202 N  N   . THR   A 1 313 ? -7.322  11.645  96.294  1.00 49.75 ? 341 THR   A N   1 
ATOM   2203 C  CA  . THR   A 1 313 ? -6.368  11.390  97.366  1.00 50.56 ? 341 THR   A CA  1 
ATOM   2204 C  C   . THR   A 1 313 ? -5.018  10.975  96.790  1.00 50.05 ? 341 THR   A C   1 
ATOM   2205 O  O   . THR   A 1 313 ? -3.974  11.426  97.270  1.00 49.11 ? 341 THR   A O   1 
ATOM   2206 C  CB  . THR   A 1 313 ? -6.897  10.317  98.325  1.00 56.77 ? 341 THR   A CB  1 
ATOM   2207 O  OG1 . THR   A 1 313 ? -7.590  9.303   97.585  1.00 61.20 ? 341 THR   A OG1 1 
ATOM   2208 C  CG2 . THR   A 1 313 ? -7.834  10.920  99.353  1.00 52.23 ? 341 THR   A CG2 1 
ATOM   2209 N  N   . TYR   A 1 314 ? -5.034  10.147  95.740  1.00 47.30 ? 342 TYR   A N   1 
ATOM   2210 C  CA  . TYR   A 1 314 ? -3.792  9.746   95.083  1.00 48.93 ? 342 TYR   A CA  1 
ATOM   2211 C  C   . TYR   A 1 314 ? -3.025  10.957  94.564  1.00 50.48 ? 342 TYR   A C   1 
ATOM   2212 O  O   . TYR   A 1 314 ? -1.788  11.003  94.635  1.00 44.51 ? 342 TYR   A O   1 
ATOM   2213 C  CB  . TYR   A 1 314 ? -4.093  8.773   93.938  1.00 42.25 ? 342 TYR   A CB  1 
ATOM   2214 C  CG  . TYR   A 1 314 ? -2.865  8.240   93.239  1.00 37.19 ? 342 TYR   A CG  1 
ATOM   2215 C  CD1 . TYR   A 1 314 ? -2.194  7.119   93.710  1.00 38.78 ? 342 TYR   A CD1 1 
ATOM   2216 C  CD2 . TYR   A 1 314 ? -2.374  8.865   92.105  1.00 40.37 ? 342 TYR   A CD2 1 
ATOM   2217 C  CE1 . TYR   A 1 314 ? -1.065  6.638   93.067  1.00 33.27 ? 342 TYR   A CE1 1 
ATOM   2218 C  CE2 . TYR   A 1 314 ? -1.250  8.401   91.469  1.00 36.09 ? 342 TYR   A CE2 1 
ATOM   2219 C  CZ  . TYR   A 1 314 ? -0.604  7.287   91.945  1.00 32.77 ? 342 TYR   A CZ  1 
ATOM   2220 O  OH  . TYR   A 1 314 ? 0.512   6.845   91.273  1.00 34.25 ? 342 TYR   A OH  1 
ATOM   2221 N  N   . TYR   A 1 315 ? -3.740  11.945  94.034  1.00 44.80 ? 343 TYR   A N   1 
ATOM   2222 C  CA  . TYR   A 1 315 ? -3.061  13.096  93.460  1.00 48.45 ? 343 TYR   A CA  1 
ATOM   2223 C  C   . TYR   A 1 315 ? -2.734  14.144  94.512  1.00 51.40 ? 343 TYR   A C   1 
ATOM   2224 O  O   . TYR   A 1 315 ? -1.733  14.859  94.374  1.00 45.89 ? 343 TYR   A O   1 
ATOM   2225 C  CB  . TYR   A 1 315 ? -3.906  13.675  92.329  1.00 48.22 ? 343 TYR   A CB  1 
ATOM   2226 C  CG  . TYR   A 1 315 ? -3.964  12.729  91.162  1.00 44.46 ? 343 TYR   A CG  1 
ATOM   2227 C  CD1 . TYR   A 1 315 ? -5.080  11.940  90.940  1.00 43.23 ? 343 TYR   A CD1 1 
ATOM   2228 C  CD2 . TYR   A 1 315 ? -2.882  12.597  90.303  1.00 41.88 ? 343 TYR   A CD2 1 
ATOM   2229 C  CE1 . TYR   A 1 315 ? -5.127  11.064  89.885  1.00 40.18 ? 343 TYR   A CE1 1 
ATOM   2230 C  CE2 . TYR   A 1 315 ? -2.917  11.719  89.248  1.00 39.28 ? 343 TYR   A CE2 1 
ATOM   2231 C  CZ  . TYR   A 1 315 ? -4.045  10.956  89.043  1.00 37.57 ? 343 TYR   A CZ  1 
ATOM   2232 O  OH  . TYR   A 1 315 ? -4.089  10.074  87.990  1.00 38.69 ? 343 TYR   A OH  1 
ATOM   2233 N  N   . GLN   A 1 316 ? -3.552  14.242  95.563  1.00 50.00 ? 344 GLN   A N   1 
ATOM   2234 C  CA  . GLN   A 1 316 ? -3.144  15.008  96.731  1.00 50.34 ? 344 GLN   A CA  1 
ATOM   2235 C  C   . GLN   A 1 316 ? -1.798  14.510  97.237  1.00 51.52 ? 344 GLN   A C   1 
ATOM   2236 O  O   . GLN   A 1 316 ? -0.853  15.292  97.386  1.00 51.78 ? 344 GLN   A O   1 
ATOM   2237 C  CB  . GLN   A 1 316 ? -4.207  14.916  97.827  1.00 48.80 ? 344 GLN   A CB  1 
ATOM   2238 N  N   . ASN   A 1 317 ? -1.681  13.194  97.456  1.00 44.27 ? 345 ASN   A N   1 
ATOM   2239 C  CA  . ASN   A 1 317 ? -0.440  12.615  97.965  1.00 47.03 ? 345 ASN   A CA  1 
ATOM   2240 C  C   . ASN   A 1 317 ? 0.710   12.696  96.976  1.00 47.04 ? 345 ASN   A C   1 
ATOM   2241 O  O   . ASN   A 1 317 ? 1.859   12.491  97.372  1.00 46.97 ? 345 ASN   A O   1 
ATOM   2242 C  CB  . ASN   A 1 317 ? -0.635  11.153  98.345  1.00 45.98 ? 345 ASN   A CB  1 
ATOM   2243 C  CG  . ASN   A 1 317 ? -1.704  10.965  99.384  1.00 53.62 ? 345 ASN   A CG  1 
ATOM   2244 O  OD1 . ASN   A 1 317 ? -1.946  11.848  100.212 1.00 57.26 ? 345 ASN   A OD1 1 
ATOM   2245 N  ND2 . ASN   A 1 317 ? -2.366  9.811   99.347  1.00 54.58 ? 345 ASN   A ND2 1 
ATOM   2246 N  N   . LEU   A 1 318 ? 0.435   12.975  95.704  1.00 46.85 ? 346 LEU   A N   1 
ATOM   2247 C  CA  . LEU   A 1 318 ? 1.509   12.973  94.720  1.00 50.81 ? 346 LEU   A CA  1 
ATOM   2248 C  C   . LEU   A 1 318 ? 2.571   14.009  95.040  1.00 49.23 ? 346 LEU   A C   1 
ATOM   2249 O  O   . LEU   A 1 318 ? 3.757   13.772  94.787  1.00 46.06 ? 346 LEU   A O   1 
ATOM   2250 C  CB  . LEU   A 1 318 ? 0.949   13.212  93.320  1.00 50.08 ? 346 LEU   A CB  1 
ATOM   2251 C  CG  . LEU   A 1 318 ? 0.745   11.924  92.524  1.00 48.78 ? 346 LEU   A CG  1 
ATOM   2252 C  CD1 . LEU   A 1 318 ? 0.466   12.278  91.085  1.00 44.90 ? 346 LEU   A CD1 1 
ATOM   2253 C  CD2 . LEU   A 1 318 ? 1.958   10.981  92.659  1.00 44.55 ? 346 LEU   A CD2 1 
ATOM   2254 N  N   . LYS   A 1 319 ? 2.168   15.159  95.591  1.00 52.69 ? 347 LYS   A N   1 
ATOM   2255 C  CA  . LYS   A 1 319 ? 3.133   16.197  95.946  1.00 54.21 ? 347 LYS   A CA  1 
ATOM   2256 C  C   . LYS   A 1 319 ? 4.205   15.660  96.893  1.00 47.73 ? 347 LYS   A C   1 
ATOM   2257 O  O   . LYS   A 1 319 ? 5.394   15.949  96.725  1.00 47.09 ? 347 LYS   A O   1 
ATOM   2258 C  CB  . LYS   A 1 319 ? 2.404   17.395  96.565  1.00 52.81 ? 347 LYS   A CB  1 
ATOM   2259 N  N   . LYS   A 1 320 ? 3.805   14.846  97.874  1.00 52.08 ? 348 LYS   A N   1 
ATOM   2260 C  CA  . LYS   A 1 320 ? 4.759   14.320  98.845  1.00 46.92 ? 348 LYS   A CA  1 
ATOM   2261 C  C   . LYS   A 1 320 ? 5.793   13.405  98.195  1.00 53.99 ? 348 LYS   A C   1 
ATOM   2262 O  O   . LYS   A 1 320 ? 6.964   13.405  98.596  1.00 52.58 ? 348 LYS   A O   1 
ATOM   2263 C  CB  . LYS   A 1 320 ? 4.014   13.578  99.958  1.00 45.04 ? 348 LYS   A CB  1 
ATOM   2264 N  N   . ARG   A 1 321 ? 5.391   12.630  97.190  1.00 48.01 ? 349 ARG   A N   1 
ATOM   2265 C  CA  . ARG   A 1 321 ? 6.271   11.622  96.616  1.00 48.44 ? 349 ARG   A CA  1 
ATOM   2266 C  C   . ARG   A 1 321 ? 7.152   12.161  95.502  1.00 50.99 ? 349 ARG   A C   1 
ATOM   2267 O  O   . ARG   A 1 321 ? 8.286   11.695  95.335  1.00 51.20 ? 349 ARG   A O   1 
ATOM   2268 C  CB  . ARG   A 1 321 ? 5.440   10.467  96.059  1.00 45.26 ? 349 ARG   A CB  1 
ATOM   2269 C  CG  . ARG   A 1 321 ? 4.667   9.692   97.096  1.00 51.06 ? 349 ARG   A CG  1 
ATOM   2270 C  CD  . ARG   A 1 321 ? 3.934   8.540   96.441  1.00 49.40 ? 349 ARG   A CD  1 
ATOM   2271 N  NE  . ARG   A 1 321 ? 2.520   8.846   96.292  1.00 51.25 ? 349 ARG   A NE  1 
ATOM   2272 C  CZ  . ARG   A 1 321 ? 1.786   8.462   95.256  1.00 50.65 ? 349 ARG   A CZ  1 
ATOM   2273 N  NH1 . ARG   A 1 321 ? 2.354   7.765   94.277  1.00 45.28 ? 349 ARG   A NH1 1 
ATOM   2274 N  NH2 . ARG   A 1 321 ? 0.492   8.783   95.194  1.00 43.59 ? 349 ARG   A NH2 1 
ATOM   2275 N  N   . VAL   A 1 322 ? 6.656   13.123  94.734  1.00 48.74 ? 350 VAL   A N   1 
ATOM   2276 C  CA  . VAL   A 1 322 ? 7.236   13.435  93.436  1.00 46.90 ? 350 VAL   A CA  1 
ATOM   2277 C  C   . VAL   A 1 322 ? 7.323   14.949  93.276  1.00 44.64 ? 350 VAL   A C   1 
ATOM   2278 O  O   . VAL   A 1 322 ? 7.452   15.468  92.162  1.00 40.39 ? 350 VAL   A O   1 
ATOM   2279 C  CB  . VAL   A 1 322 ? 6.404   12.764  92.319  1.00 46.88 ? 350 VAL   A CB  1 
ATOM   2280 C  CG1 . VAL   A 1 322 ? 5.139   13.560  92.011  1.00 47.11 ? 350 VAL   A CG1 1 
ATOM   2281 C  CG2 . VAL   A 1 322 ? 7.237   12.522  91.071  1.00 47.17 ? 350 VAL   A CG2 1 
ATOM   2282 N  N   . GLY   A 1 323 ? 7.280   15.667  94.402  1.00 49.38 ? 351 GLY   A N   1 
ATOM   2283 C  CA  . GLY   A 1 323 ? 7.279   17.121  94.353  1.00 50.28 ? 351 GLY   A CA  1 
ATOM   2284 C  C   . GLY   A 1 323 ? 8.542   17.721  93.765  1.00 47.73 ? 351 GLY   A C   1 
ATOM   2285 O  O   . GLY   A 1 323 ? 8.495   18.779  93.128  1.00 46.66 ? 351 GLY   A O   1 
ATOM   2286 N  N   . ASP   A 1 324 ? 9.681   17.067  93.964  1.00 46.77 ? 352 ASP   A N   1 
ATOM   2287 C  CA  . ASP   A 1 324 ? 10.947  17.541  93.419  1.00 47.43 ? 352 ASP   A CA  1 
ATOM   2288 C  C   . ASP   A 1 324 ? 11.132  17.192  91.940  1.00 51.19 ? 352 ASP   A C   1 
ATOM   2289 O  O   . ASP   A 1 324 ? 12.209  17.450  91.391  1.00 47.46 ? 352 ASP   A O   1 
ATOM   2290 C  CB  . ASP   A 1 324 ? 12.111  16.979  94.246  1.00 50.12 ? 352 ASP   A CB  1 
ATOM   2291 C  CG  . ASP   A 1 324 ? 12.165  15.451  94.246  1.00 55.88 ? 352 ASP   A CG  1 
ATOM   2292 O  OD1 . ASP   A 1 324 ? 13.289  14.902  94.290  1.00 58.79 ? 352 ASP   A OD1 1 
ATOM   2293 O  OD2 . ASP   A 1 324 ? 11.098  14.796  94.201  1.00 52.80 ? 352 ASP   A OD2 1 
ATOM   2294 N  N   . VAL   A 1 325 ? 10.106  16.634  91.286  1.00 51.45 ? 353 VAL   A N   1 
ATOM   2295 C  CA  . VAL   A 1 325 ? 10.203  16.116  89.925  1.00 49.71 ? 353 VAL   A CA  1 
ATOM   2296 C  C   . VAL   A 1 325 ? 9.188   16.776  88.999  1.00 43.59 ? 353 VAL   A C   1 
ATOM   2297 O  O   . VAL   A 1 325 ? 9.546   17.303  87.939  1.00 39.00 ? 353 VAL   A O   1 
ATOM   2298 C  CB  . VAL   A 1 325 ? 10.035  14.582  89.898  1.00 46.74 ? 353 VAL   A CB  1 
ATOM   2299 C  CG1 . VAL   A 1 325 ? 10.274  14.048  88.490  1.00 43.16 ? 353 VAL   A CG1 1 
ATOM   2300 C  CG2 . VAL   A 1 325 ? 10.958  13.936  90.906  1.00 40.23 ? 353 VAL   A CG2 1 
ATOM   2301 N  N   . LEU   A 1 326 ? 7.912   16.738  89.371  1.00 43.09 ? 354 LEU   A N   1 
ATOM   2302 C  CA  . LEU   A 1 326 ? 6.842   17.339  88.586  1.00 44.08 ? 354 LEU   A CA  1 
ATOM   2303 C  C   . LEU   A 1 326 ? 6.303   18.560  89.314  1.00 47.72 ? 354 LEU   A C   1 
ATOM   2304 O  O   . LEU   A 1 326 ? 6.079   18.517  90.528  1.00 47.49 ? 354 LEU   A O   1 
ATOM   2305 C  CB  . LEU   A 1 326 ? 5.713   16.340  88.341  1.00 39.29 ? 354 LEU   A CB  1 
ATOM   2306 C  CG  . LEU   A 1 326 ? 6.056   15.070  87.565  1.00 41.87 ? 354 LEU   A CG  1 
ATOM   2307 C  CD1 . LEU   A 1 326 ? 4.827   14.197  87.425  1.00 37.36 ? 354 LEU   A CD1 1 
ATOM   2308 C  CD2 . LEU   A 1 326 ? 6.623   15.422  86.211  1.00 34.88 ? 354 LEU   A CD2 1 
ATOM   2309 N  N   . SER   A 1 327 ? 6.086   19.640  88.571  1.00 48.30 ? 355 SER   A N   1 
ATOM   2310 C  CA  . SER   A 1 327 ? 5.510   20.830  89.169  1.00 49.09 ? 355 SER   A CA  1 
ATOM   2311 C  C   . SER   A 1 327 ? 4.060   20.562  89.559  1.00 50.88 ? 355 SER   A C   1 
ATOM   2312 O  O   . SER   A 1 327 ? 3.481   19.522  89.233  1.00 47.63 ? 355 SER   A O   1 
ATOM   2313 C  CB  . SER   A 1 327 ? 5.600   22.012  88.207  1.00 40.73 ? 355 SER   A CB  1 
ATOM   2314 O  OG  . SER   A 1 327 ? 4.686   21.859  87.140  1.00 42.81 ? 355 SER   A OG  1 
ATOM   2315 N  N   . ASP   A 1 328 ? 3.475   21.520  90.281  1.00 53.02 ? 356 ASP   A N   1 
ATOM   2316 C  CA  . ASP   A 1 328 ? 2.058   21.425  90.614  1.00 45.45 ? 356 ASP   A CA  1 
ATOM   2317 C  C   . ASP   A 1 328 ? 1.206   21.373  89.354  1.00 44.26 ? 356 ASP   A C   1 
ATOM   2318 O  O   . ASP   A 1 328 ? 0.262   20.578  89.268  1.00 45.91 ? 356 ASP   A O   1 
ATOM   2319 C  CB  . ASP   A 1 328 ? 1.652   22.602  91.497  1.00 45.73 ? 356 ASP   A CB  1 
ATOM   2320 C  CG  . ASP   A 1 328 ? 2.349   22.592  92.848  1.00 53.85 ? 356 ASP   A CG  1 
ATOM   2321 O  OD1 . ASP   A 1 328 ? 2.547   21.495  93.420  1.00 52.48 ? 356 ASP   A OD1 1 
ATOM   2322 O  OD2 . ASP   A 1 328 ? 2.703   23.686  93.339  1.00 58.37 ? 356 ASP   A OD2 1 
ATOM   2323 N  N   . ASP   A 1 329 ? 1.540   22.196  88.355  1.00 40.45 ? 357 ASP   A N   1 
ATOM   2324 C  CA  . ASP   A 1 329 ? 0.777   22.193  87.108  1.00 46.85 ? 357 ASP   A CA  1 
ATOM   2325 C  C   . ASP   A 1 329 ? 0.922   20.863  86.363  1.00 46.69 ? 357 ASP   A C   1 
ATOM   2326 O  O   . ASP   A 1 329 ? -0.067  20.316  85.860  1.00 44.71 ? 357 ASP   A O   1 
ATOM   2327 C  CB  . ASP   A 1 329 ? 1.212   23.366  86.230  1.00 35.93 ? 357 ASP   A CB  1 
ATOM   2328 N  N   . GLN   A 1 330 ? 2.145   20.327  86.283  1.00 42.15 ? 358 GLN   A N   1 
ATOM   2329 C  CA  . GLN   A 1 330 ? 2.345   19.017  85.667  1.00 41.41 ? 358 GLN   A CA  1 
ATOM   2330 C  C   . GLN   A 1 330 ? 1.568   17.939  86.409  1.00 45.35 ? 358 GLN   A C   1 
ATOM   2331 O  O   . GLN   A 1 330 ? 0.869   17.125  85.794  1.00 46.03 ? 358 GLN   A O   1 
ATOM   2332 C  CB  . GLN   A 1 330 ? 3.835   18.676  85.635  1.00 41.46 ? 358 GLN   A CB  1 
ATOM   2333 C  CG  . GLN   A 1 330 ? 4.558   19.239  84.437  1.00 38.77 ? 358 GLN   A CG  1 
ATOM   2334 C  CD  . GLN   A 1 330 ? 5.940   19.776  84.782  1.00 42.80 ? 358 GLN   A CD  1 
ATOM   2335 O  OE1 . GLN   A 1 330 ? 6.585   19.312  85.726  1.00 42.68 ? 358 GLN   A OE1 1 
ATOM   2336 N  NE2 . GLN   A 1 330 ? 6.394   20.772  84.025  1.00 33.16 ? 358 GLN   A NE2 1 
ATOM   2337 N  N   . ILE   A 1 331 ? 1.681   17.915  87.738  1.00 47.32 ? 359 ILE   A N   1 
ATOM   2338 C  CA  . ILE   A 1 331 ? 0.908   16.965  88.531  1.00 44.09 ? 359 ILE   A CA  1 
ATOM   2339 C  C   . ILE   A 1 331 ? -0.581  17.179  88.305  1.00 45.56 ? 359 ILE   A C   1 
ATOM   2340 O  O   . ILE   A 1 331 ? -1.353  16.216  88.226  1.00 44.81 ? 359 ILE   A O   1 
ATOM   2341 C  CB  . ILE   A 1 331 ? 1.283   17.078  90.019  1.00 44.57 ? 359 ILE   A CB  1 
ATOM   2342 C  CG1 . ILE   A 1 331 ? 2.749   16.675  90.229  1.00 48.81 ? 359 ILE   A CG1 1 
ATOM   2343 C  CG2 . ILE   A 1 331 ? 0.333   16.247  90.883  1.00 46.06 ? 359 ILE   A CG2 1 
ATOM   2344 C  CD1 . ILE   A 1 331 ? 3.205   16.666  91.683  1.00 49.03 ? 359 ILE   A CD1 1 
ATOM   2345 N  N   . LYS   A 1 332 ? -1.007  18.441  88.179  1.00 46.60 ? 360 LYS   A N   1 
ATOM   2346 C  CA  . LYS   A 1 332 ? -2.398  18.721  87.830  1.00 42.10 ? 360 LYS   A CA  1 
ATOM   2347 C  C   . LYS   A 1 332 ? -2.786  18.005  86.544  1.00 42.99 ? 360 LYS   A C   1 
ATOM   2348 O  O   . LYS   A 1 332 ? -3.843  17.368  86.470  1.00 35.86 ? 360 LYS   A O   1 
ATOM   2349 C  CB  . LYS   A 1 332 ? -2.622  20.231  87.689  1.00 42.39 ? 360 LYS   A CB  1 
ATOM   2350 N  N   . GLU   A 1 333 ? -1.930  18.095  85.518  1.00 44.31 ? 361 GLU   A N   1 
ATOM   2351 C  CA  . GLU   A 1 333 ? -2.193  17.392  84.266  1.00 41.50 ? 361 GLU   A CA  1 
ATOM   2352 C  C   . GLU   A 1 333 ? -2.371  15.894  84.501  1.00 40.98 ? 361 GLU   A C   1 
ATOM   2353 O  O   . GLU   A 1 333 ? -3.288  15.279  83.940  1.00 38.66 ? 361 GLU   A O   1 
ATOM   2354 C  CB  . GLU   A 1 333 ? -1.065  17.657  83.260  1.00 41.52 ? 361 GLU   A CB  1 
ATOM   2355 C  CG  . GLU   A 1 333 ? -1.218  18.941  82.463  1.00 36.82 ? 361 GLU   A CG  1 
ATOM   2356 C  CD  . GLU   A 1 333 ? -0.594  18.861  81.078  1.00 43.74 ? 361 GLU   A CD  1 
ATOM   2357 O  OE1 . GLU   A 1 333 ? 0.449   19.515  80.836  1.00 38.80 ? 361 GLU   A OE1 1 
ATOM   2358 O  OE2 . GLU   A 1 333 ? -1.149  18.128  80.227  1.00 42.11 ? 361 GLU   A OE2 1 
ATOM   2359 N  N   . CYS   A 1 334 ? -1.521  15.295  85.347  1.00 41.00 ? 362 CYS   A N   1 
ATOM   2360 C  CA  . CYS   A 1 334 ? -1.661  13.873  85.662  1.00 39.04 ? 362 CYS   A CA  1 
ATOM   2361 C  C   . CYS   A 1 334 ? -3.070  13.537  86.138  1.00 40.08 ? 362 CYS   A C   1 
ATOM   2362 O  O   . CYS   A 1 334 ? -3.647  12.521  85.727  1.00 37.23 ? 362 CYS   A O   1 
ATOM   2363 C  CB  . CYS   A 1 334 ? -0.635  13.445  86.717  1.00 34.97 ? 362 CYS   A CB  1 
ATOM   2364 S  SG  . CYS   A 1 334 ? 1.103   13.441  86.162  1.00 39.67 ? 362 CYS   A SG  1 
ATOM   2365 N  N   . GLU   A 1 335 ? -3.655  14.374  86.999  1.00 37.89 ? 363 GLU   A N   1 
ATOM   2366 C  CA  . GLU   A 1 335 ? -4.947  13.981  87.554  1.00 37.86 ? 363 GLU   A CA  1 
ATOM   2367 C  C   . GLU   A 1 335 ? -6.074  14.204  86.556  1.00 33.65 ? 363 GLU   A C   1 
ATOM   2368 O  O   . GLU   A 1 335 ? -7.076  13.475  86.583  1.00 23.87 ? 363 GLU   A O   1 
ATOM   2369 C  CB  . GLU   A 1 335 ? -5.218  14.722  88.866  1.00 41.32 ? 363 GLU   A CB  1 
ATOM   2370 C  CG  . GLU   A 1 335 ? -6.658  14.607  89.351  1.00 35.85 ? 363 GLU   A CG  1 
ATOM   2371 C  CD  . GLU   A 1 335 ? -6.949  15.458  90.581  1.00 41.44 ? 363 GLU   A CD  1 
ATOM   2372 O  OE1 . GLU   A 1 335 ? -6.448  16.612  90.669  1.00 42.32 ? 363 GLU   A OE1 1 
ATOM   2373 O  OE2 . GLU   A 1 335 ? -7.680  14.985  91.495  1.00 47.92 ? 363 GLU   A OE2 1 
ATOM   2374 N  N   . GLU   A 1 336 ? -5.906  15.158  85.639  1.00 34.23 ? 364 GLU   A N   1 
ATOM   2375 C  CA  . GLU   A 1 336 ? -6.861  15.267  84.548  1.00 37.61 ? 364 GLU   A CA  1 
ATOM   2376 C  C   . GLU   A 1 336 ? -6.910  13.975  83.734  1.00 40.31 ? 364 GLU   A C   1 
ATOM   2377 O  O   . GLU   A 1 336 ? -7.994  13.457  83.426  1.00 34.36 ? 364 GLU   A O   1 
ATOM   2378 C  CB  . GLU   A 1 336 ? -6.507  16.460  83.676  1.00 35.81 ? 364 GLU   A CB  1 
ATOM   2379 C  CG  . GLU   A 1 336 ? -7.315  17.711  84.009  1.00 46.02 ? 364 GLU   A CG  1 
ATOM   2380 C  CD  . GLU   A 1 336 ? -6.512  19.020  83.895  1.00 56.87 ? 364 GLU   A CD  1 
ATOM   2381 O  OE1 . GLU   A 1 336 ? -7.040  20.098  84.303  1.00 60.97 ? 364 GLU   A OE1 1 
ATOM   2382 O  OE2 . GLU   A 1 336 ? -5.351  18.994  83.399  1.00 46.50 ? 364 GLU   A OE2 1 
ATOM   2383 N  N   . LEU   A 1 337 ? -5.750  13.399  83.441  1.00 41.20 ? 365 LEU   A N   1 
ATOM   2384 C  CA  . LEU   A 1 337 ? -5.659  12.237  82.569  1.00 29.96 ? 365 LEU   A CA  1 
ATOM   2385 C  C   . LEU   A 1 337 ? -5.698  10.912  83.315  1.00 30.82 ? 365 LEU   A C   1 
ATOM   2386 O  O   . LEU   A 1 337 ? -5.730  9.862   82.669  1.00 37.19 ? 365 LEU   A O   1 
ATOM   2387 C  CB  . LEU   A 1 337 ? -4.384  12.333  81.732  1.00 34.09 ? 365 LEU   A CB  1 
ATOM   2388 C  CG  . LEU   A 1 337 ? -4.290  13.676  81.000  1.00 28.03 ? 365 LEU   A CG  1 
ATOM   2389 C  CD1 . LEU   A 1 337 ? -2.863  13.998  80.620  1.00 27.86 ? 365 LEU   A CD1 1 
ATOM   2390 C  CD2 . LEU   A 1 337 ? -5.183  13.696  79.761  1.00 23.57 ? 365 LEU   A CD2 1 
ATOM   2391 N  N   . GLY   A 1 338 ? -5.742  10.922  84.642  1.00 27.84 ? 366 GLY   A N   1 
ATOM   2392 C  CA  . GLY   A 1 338 ? -5.688  9.665   85.354  1.00 32.62 ? 366 GLY   A CA  1 
ATOM   2393 C  C   . GLY   A 1 338 ? -4.340  8.978   85.298  1.00 30.44 ? 366 GLY   A C   1 
ATOM   2394 O  O   . GLY   A 1 338 ? -4.270  7.755   85.462  1.00 27.96 ? 366 GLY   A O   1 
ATOM   2395 N  N   . ILE   A 1 339 ? -3.264  9.739   85.078  1.00 26.85 ? 367 ILE   A N   1 
ATOM   2396 C  CA  . ILE   A 1 339 ? -1.927  9.168   84.974  1.00 30.07 ? 367 ILE   A CA  1 
ATOM   2397 C  C   . ILE   A 1 339 ? -1.416  8.781   86.354  1.00 33.18 ? 367 ILE   A C   1 
ATOM   2398 O  O   . ILE   A 1 339 ? -1.566  9.532   87.329  1.00 27.30 ? 367 ILE   A O   1 
ATOM   2399 C  CB  . ILE   A 1 339 ? -0.970  10.163  84.298  1.00 28.77 ? 367 ILE   A CB  1 
ATOM   2400 C  CG1 . ILE   A 1 339 ? -1.482  10.544  82.917  1.00 33.37 ? 367 ILE   A CG1 1 
ATOM   2401 C  CG2 . ILE   A 1 339 ? 0.418   9.584   84.186  1.00 29.89 ? 367 ILE   A CG2 1 
ATOM   2402 C  CD1 . ILE   A 1 339 ? -0.474  11.329  82.069  1.00 31.52 ? 367 ILE   A CD1 1 
ATOM   2403 N  N   . LEU   A 1 340 ? -0.811  7.604   86.443  1.00 27.92 ? 368 LEU   A N   1 
ATOM   2404 C  CA  . LEU   A 1 340 ? -0.179  7.176   87.681  1.00 30.67 ? 368 LEU   A CA  1 
ATOM   2405 C  C   . LEU   A 1 340 ? 1.300   7.551   87.666  1.00 32.11 ? 368 LEU   A C   1 
ATOM   2406 O  O   . LEU   A 1 340 ? 1.901   7.752   86.607  1.00 29.80 ? 368 LEU   A O   1 
ATOM   2407 C  CB  . LEU   A 1 340 ? -0.356  5.671   87.885  1.00 30.16 ? 368 LEU   A CB  1 
ATOM   2408 C  CG  . LEU   A 1 340 ? -1.814  5.218   87.959  1.00 28.34 ? 368 LEU   A CG  1 
ATOM   2409 C  CD1 . LEU   A 1 340 ? -2.288  4.659   86.618  1.00 33.91 ? 368 LEU   A CD1 1 
ATOM   2410 C  CD2 . LEU   A 1 340 ? -1.997  4.194   89.070  1.00 34.26 ? 368 LEU   A CD2 1 
ATOM   2411 N  N   . VAL   A 1 341 ? 1.881   7.678   88.861  1.00 34.99 ? 369 VAL   A N   1 
ATOM   2412 C  CA  . VAL   A 1 341 ? 3.287   8.061   88.992  1.00 34.16 ? 369 VAL   A CA  1 
ATOM   2413 C  C   . VAL   A 1 341 ? 3.940   7.206   90.065  1.00 34.80 ? 369 VAL   A C   1 
ATOM   2414 O  O   . VAL   A 1 341 ? 3.458   7.143   91.200  1.00 35.66 ? 369 VAL   A O   1 
ATOM   2415 C  CB  . VAL   A 1 341 ? 3.477   9.554   89.331  1.00 33.23 ? 369 VAL   A CB  1 
ATOM   2416 C  CG1 . VAL   A 1 341 ? 4.948   9.890   89.368  1.00 30.53 ? 369 VAL   A CG1 1 
ATOM   2417 C  CG2 . VAL   A 1 341 ? 2.767   10.453  88.312  1.00 31.47 ? 369 VAL   A CG2 1 
ATOM   2418 N  N   . ASP   A 1 342 ? 5.050   6.567   89.708  1.00 34.78 ? 370 ASP   A N   1 
ATOM   2419 C  CA  . ASP   A 1 342 ? 5.894   5.853   90.646  1.00 33.30 ? 370 ASP   A CA  1 
ATOM   2420 C  C   . ASP   A 1 342 ? 7.332   6.323   90.467  1.00 36.78 ? 370 ASP   A C   1 
ATOM   2421 O  O   . ASP   A 1 342 ? 7.673   7.014   89.499  1.00 36.83 ? 370 ASP   A O   1 
ATOM   2422 C  CB  . ASP   A 1 342 ? 5.786   4.333   90.441  1.00 32.29 ? 370 ASP   A CB  1 
ATOM   2423 C  CG  . ASP   A 1 342 ? 6.202   3.548   91.668  1.00 35.19 ? 370 ASP   A CG  1 
ATOM   2424 O  OD1 . ASP   A 1 342 ? 6.148   4.112   92.770  1.00 34.11 ? 370 ASP   A OD1 1 
ATOM   2425 O  OD2 . ASP   A 1 342 ? 6.590   2.367   91.535  1.00 35.72 ? 370 ASP   A OD2 1 
ATOM   2426 N  N   . ARG   A 1 343 ? 8.187   5.936   91.410  1.00 37.74 ? 371 ARG   A N   1 
ATOM   2427 C  CA  . ARG   A 1 343 ? 9.606   6.242   91.288  1.00 41.04 ? 371 ARG   A CA  1 
ATOM   2428 C  C   . ARG   A 1 343 ? 10.391  5.323   92.210  1.00 41.35 ? 371 ARG   A C   1 
ATOM   2429 O  O   . ARG   A 1 343 ? 9.900   4.908   93.266  1.00 44.01 ? 371 ARG   A O   1 
ATOM   2430 C  CB  . ARG   A 1 343 ? 9.910   7.715   91.613  1.00 41.89 ? 371 ARG   A CB  1 
ATOM   2431 C  CG  . ARG   A 1 343 ? 10.332  7.985   93.053  1.00 45.71 ? 371 ARG   A CG  1 
ATOM   2432 C  CD  . ARG   A 1 343 ? 10.343  9.471   93.390  1.00 46.08 ? 371 ARG   A CD  1 
ATOM   2433 N  NE  . ARG   A 1 343 ? 11.540  10.167  92.922  1.00 54.51 ? 371 ARG   A NE  1 
ATOM   2434 C  CZ  . ARG   A 1 343 ? 11.827  11.432  93.224  1.00 48.02 ? 371 ARG   A CZ  1 
ATOM   2435 N  NH1 . ARG   A 1 343 ? 11.006  12.130  93.994  1.00 49.16 ? 371 ARG   A NH1 1 
ATOM   2436 N  NH2 . ARG   A 1 343 ? 12.937  11.998  92.762  1.00 52.40 ? 371 ARG   A NH2 1 
ATOM   2437 N  N   . ASP   A 1 344 ? 11.610  4.996   91.785  1.00 43.77 ? 372 ASP   A N   1 
ATOM   2438 C  CA  . ASP   A 1 344 ? 12.537  4.253   92.629  1.00 38.64 ? 372 ASP   A CA  1 
ATOM   2439 C  C   . ASP   A 1 344 ? 13.764  5.097   92.922  1.00 41.69 ? 372 ASP   A C   1 
ATOM   2440 O  O   . ASP   A 1 344 ? 13.719  6.326   92.830  1.00 42.49 ? 372 ASP   A O   1 
ATOM   2441 C  CB  . ASP   A 1 344 ? 12.933  2.916   91.985  1.00 38.24 ? 372 ASP   A CB  1 
ATOM   2442 C  CG  . ASP   A 1 344 ? 13.631  3.075   90.634  1.00 41.07 ? 372 ASP   A CG  1 
ATOM   2443 O  OD1 . ASP   A 1 344 ? 13.693  2.073   89.881  1.00 36.01 ? 372 ASP   A OD1 1 
ATOM   2444 O  OD2 . ASP   A 1 344 ? 14.121  4.183   90.315  1.00 42.07 ? 372 ASP   A OD2 1 
ATOM   2445 N  N   . ASP   A 1 345 ? 14.875  4.442   93.255  1.00 49.31 ? 373 ASP   A N   1 
ATOM   2446 C  CA  . ASP   A 1 345 ? 16.073  5.172   93.648  1.00 44.12 ? 373 ASP   A CA  1 
ATOM   2447 C  C   . ASP   A 1 345 ? 16.715  5.892   92.468  1.00 45.31 ? 373 ASP   A C   1 
ATOM   2448 O  O   . ASP   A 1 345 ? 17.332  6.945   92.652  1.00 42.20 ? 373 ASP   A O   1 
ATOM   2449 C  CB  . ASP   A 1 345 ? 17.072  4.212   94.306  1.00 47.88 ? 373 ASP   A CB  1 
ATOM   2450 C  CG  . ASP   A 1 345 ? 17.475  3.058   93.394  1.00 48.50 ? 373 ASP   A CG  1 
ATOM   2451 O  OD1 . ASP   A 1 345 ? 17.289  1.889   93.798  1.00 47.45 ? 373 ASP   A OD1 1 
ATOM   2452 O  OD2 . ASP   A 1 345 ? 18.004  3.316   92.287  1.00 54.25 ? 373 ASP   A OD2 1 
ATOM   2453 N  N   . GLN   A 1 346 ? 16.588  5.345   91.257  1.00 44.49 ? 374 GLN   A N   1 
ATOM   2454 C  CA  . GLN   A 1 346 ? 17.264  5.909   90.094  1.00 39.69 ? 374 GLN   A CA  1 
ATOM   2455 C  C   . GLN   A 1 346 ? 16.403  6.919   89.342  1.00 41.79 ? 374 GLN   A C   1 
ATOM   2456 O  O   . GLN   A 1 346 ? 16.902  7.977   88.941  1.00 42.11 ? 374 GLN   A O   1 
ATOM   2457 C  CB  . GLN   A 1 346 ? 17.699  4.785   89.146  1.00 32.52 ? 374 GLN   A CB  1 
ATOM   2458 N  N   . GLY   A 1 347 ? 15.119  6.618   89.137  1.00 42.98 ? 375 GLY   A N   1 
ATOM   2459 C  CA  . GLY   A 1 347 ? 14.281  7.451   88.293  1.00 36.75 ? 375 GLY   A CA  1 
ATOM   2460 C  C   . GLY   A 1 347 ? 12.816  7.478   88.677  1.00 34.67 ? 375 GLY   A C   1 
ATOM   2461 O  O   . GLY   A 1 347 ? 12.419  6.907   89.702  1.00 31.74 ? 375 GLY   A O   1 
ATOM   2462 N  N   . THR   A 1 348 ? 12.009  8.156   87.854  1.00 33.70 ? 376 THR   A N   1 
ATOM   2463 C  CA  . THR   A 1 348 ? 10.587  8.383   88.107  1.00 36.04 ? 376 THR   A CA  1 
ATOM   2464 C  C   . THR   A 1 348 ? 9.779   7.958   86.888  1.00 29.21 ? 376 THR   A C   1 
ATOM   2465 O  O   . THR   A 1 348 ? 10.115  8.323   85.757  1.00 30.32 ? 376 THR   A O   1 
ATOM   2466 C  CB  . THR   A 1 348 ? 10.307  9.862   88.432  1.00 36.94 ? 376 THR   A CB  1 
ATOM   2467 O  OG1 . THR   A 1 348 ? 10.985  10.223  89.641  1.00 45.39 ? 376 THR   A OG1 1 
ATOM   2468 C  CG2 . THR   A 1 348 ? 8.811   10.110  88.603  1.00 30.75 ? 376 THR   A CG2 1 
ATOM   2469 N  N   . LEU   A 1 349 ? 8.705   7.211   87.119  1.00 34.48 ? 377 LEU   A N   1 
ATOM   2470 C  CA  . LEU   A 1 349 ? 7.917   6.610   86.051  1.00 29.82 ? 377 LEU   A CA  1 
ATOM   2471 C  C   . LEU   A 1 349 ? 6.480   7.137   86.054  1.00 31.78 ? 377 LEU   A C   1 
ATOM   2472 O  O   . LEU   A 1 349 ? 5.804   7.108   87.088  1.00 30.66 ? 377 LEU   A O   1 
ATOM   2473 C  CB  . LEU   A 1 349 ? 7.944   5.091   86.205  1.00 31.82 ? 377 LEU   A CB  1 
ATOM   2474 C  CG  . LEU   A 1 349 ? 6.843   4.295   85.520  1.00 35.99 ? 377 LEU   A CG  1 
ATOM   2475 C  CD1 . LEU   A 1 349 ? 7.003   4.341   84.006  1.00 38.33 ? 377 LEU   A CD1 1 
ATOM   2476 C  CD2 . LEU   A 1 349 ? 6.881   2.878   86.046  1.00 35.27 ? 377 LEU   A CD2 1 
ATOM   2477 N  N   . LEU   A 1 350 ? 6.016   7.606   84.892  1.00 23.00 ? 378 LEU   A N   1 
ATOM   2478 C  CA  . LEU   A 1 350 ? 4.611   7.933   84.668  1.00 24.62 ? 378 LEU   A CA  1 
ATOM   2479 C  C   . LEU   A 1 350 ? 3.939   6.822   83.863  1.00 25.64 ? 378 LEU   A C   1 
ATOM   2480 O  O   . LEU   A 1 350 ? 4.485   6.355   82.860  1.00 24.41 ? 378 LEU   A O   1 
ATOM   2481 C  CB  . LEU   A 1 350 ? 4.450   9.270   83.926  1.00 23.28 ? 378 LEU   A CB  1 
ATOM   2482 C  CG  . LEU   A 1 350 ? 4.950   10.574  84.559  1.00 29.15 ? 378 LEU   A CG  1 
ATOM   2483 C  CD1 . LEU   A 1 350 ? 6.455   10.656  84.569  1.00 20.27 ? 378 LEU   A CD1 1 
ATOM   2484 C  CD2 . LEU   A 1 350 ? 4.376   11.801  83.842  1.00 28.12 ? 378 LEU   A CD2 1 
ATOM   2485 N  N   . GLN   A 1 351 ? 2.735   6.428   84.272  1.00 28.73 ? 379 GLN   A N   1 
ATOM   2486 C  CA  . GLN   A 1 351 ? 2.107   5.281   83.628  1.00 25.74 ? 379 GLN   A CA  1 
ATOM   2487 C  C   . GLN   A 1 351 ? 0.591   5.371   83.714  1.00 27.02 ? 379 GLN   A C   1 
ATOM   2488 O  O   . GLN   A 1 351 ? 0.034   5.961   84.647  1.00 26.09 ? 379 GLN   A O   1 
ATOM   2489 C  CB  . GLN   A 1 351 ? 2.604   3.971   84.260  1.00 27.61 ? 379 GLN   A CB  1 
ATOM   2490 C  CG  . GLN   A 1 351 ? 2.282   3.865   85.739  1.00 28.09 ? 379 GLN   A CG  1 
ATOM   2491 C  CD  . GLN   A 1 351 ? 2.761   2.575   86.371  1.00 29.37 ? 379 GLN   A CD  1 
ATOM   2492 O  OE1 . GLN   A 1 351 ? 2.585   2.365   87.569  1.00 27.57 ? 379 GLN   A OE1 1 
ATOM   2493 N  NE2 . GLN   A 1 351 ? 3.364   1.704   85.571  1.00 29.00 ? 379 GLN   A NE2 1 
ATOM   2494 N  N   . ILE   A 1 352 ? -0.071  4.774   82.721  1.00 24.29 ? 380 ILE   A N   1 
ATOM   2495 C  CA  . ILE   A 1 352 ? -1.518  4.580   82.734  1.00 28.11 ? 380 ILE   A CA  1 
ATOM   2496 C  C   . ILE   A 1 352 ? -1.858  3.317   81.943  1.00 24.03 ? 380 ILE   A C   1 
ATOM   2497 O  O   . ILE   A 1 352 ? -1.101  2.875   81.071  1.00 22.33 ? 380 ILE   A O   1 
ATOM   2498 C  CB  . ILE   A 1 352 ? -2.275  5.797   82.155  1.00 25.10 ? 380 ILE   A CB  1 
ATOM   2499 C  CG1 . ILE   A 1 352 ? -3.707  5.819   82.702  1.00 26.60 ? 380 ILE   A CG1 1 
ATOM   2500 C  CG2 . ILE   A 1 352 ? -2.241  5.739   80.626  1.00 23.41 ? 380 ILE   A CG2 1 
ATOM   2501 C  CD1 . ILE   A 1 352 ? -4.527  6.998   82.276  1.00 24.79 ? 380 ILE   A CD1 1 
ATOM   2502 N  N   . PHE   A 1 353 ? -3.017  2.735   82.245  1.00 26.84 ? 381 PHE   A N   1 
ATOM   2503 C  CA  . PHE   A 1 353 ? -3.401  1.438   81.697  1.00 24.56 ? 381 PHE   A CA  1 
ATOM   2504 C  C   . PHE   A 1 353 ? -4.732  1.522   80.978  1.00 23.97 ? 381 PHE   A C   1 
ATOM   2505 O  O   . PHE   A 1 353 ? -5.693  2.087   81.506  1.00 27.40 ? 381 PHE   A O   1 
ATOM   2506 C  CB  . PHE   A 1 353 ? -3.470  0.384   82.800  1.00 23.28 ? 381 PHE   A CB  1 
ATOM   2507 C  CG  . PHE   A 1 353 ? -2.184  0.207   83.511  1.00 23.54 ? 381 PHE   A CG  1 
ATOM   2508 C  CD1 . PHE   A 1 353 ? -1.953  0.844   84.711  1.00 28.11 ? 381 PHE   A CD1 1 
ATOM   2509 C  CD2 . PHE   A 1 353 ? -1.187  -0.579  82.967  1.00 25.89 ? 381 PHE   A CD2 1 
ATOM   2510 C  CE1 . PHE   A 1 353 ? -0.754  0.694   85.362  1.00 31.06 ? 381 PHE   A CE1 1 
ATOM   2511 C  CE2 . PHE   A 1 353 ? 0.011   -0.739  83.618  1.00 27.77 ? 381 PHE   A CE2 1 
ATOM   2512 C  CZ  . PHE   A 1 353 ? 0.230   -0.096  84.811  1.00 30.24 ? 381 PHE   A CZ  1 
ATOM   2513 N  N   . THR   A 1 354 ? -4.778  0.960   79.773  1.00 24.51 ? 382 THR   A N   1 
ATOM   2514 C  CA  . THR   A 1 354 ? -6.031  0.812   79.051  1.00 20.93 ? 382 THR   A CA  1 
ATOM   2515 C  C   . THR   A 1 354 ? -6.840  -0.351  79.597  1.00 22.89 ? 382 THR   A C   1 
ATOM   2516 O  O   . THR   A 1 354 ? -6.296  -1.337  80.109  1.00 22.81 ? 382 THR   A O   1 
ATOM   2517 C  CB  . THR   A 1 354 ? -5.787  0.541   77.574  1.00 21.46 ? 382 THR   A CB  1 
ATOM   2518 O  OG1 . THR   A 1 354 ? -5.438  -0.843  77.414  1.00 16.83 ? 382 THR   A OG1 1 
ATOM   2519 C  CG2 . THR   A 1 354 ? -4.678  1.414   77.072  1.00 19.79 ? 382 THR   A CG2 1 
ATOM   2520 N  N   . LYS   A 1 355 ? -8.156  -0.242  79.448  1.00 20.10 ? 383 LYS   A N   1 
ATOM   2521 C  CA  . LYS   A 1 355 ? -9.040  -1.388  79.590  1.00 19.86 ? 383 LYS   A CA  1 
ATOM   2522 C  C   . LYS   A 1 355 ? -8.653  -2.431  78.552  1.00 19.05 ? 383 LYS   A C   1 
ATOM   2523 O  O   . LYS   A 1 355 ? -7.903  -2.107  77.622  1.00 15.96 ? 383 LYS   A O   1 
ATOM   2524 C  CB  . LYS   A 1 355 ? -10.500 -0.958  79.416  1.00 16.70 ? 383 LYS   A CB  1 
ATOM   2525 C  CG  . LYS   A 1 355 ? -11.091 -0.384  80.683  1.00 22.72 ? 383 LYS   A CG  1 
ATOM   2526 C  CD  . LYS   A 1 355 ? -12.555 -0.063  80.529  1.00 30.58 ? 383 LYS   A CD  1 
ATOM   2527 C  CE  . LYS   A 1 355 ? -13.197 0.082   81.889  1.00 33.14 ? 383 LYS   A CE  1 
ATOM   2528 N  NZ  . LYS   A 1 355 ? -14.610 0.516   81.792  1.00 43.98 ? 383 LYS   A NZ  1 
ATOM   2529 N  N   . PRO   A 1 356 ? -9.152  -3.674  78.657  1.00 18.54 ? 384 PRO   A N   1 
ATOM   2530 C  CA  . PRO   A 1 356 ? -8.797  -4.705  77.670  1.00 17.71 ? 384 PRO   A CA  1 
ATOM   2531 C  C   . PRO   A 1 356 ? -8.992  -4.231  76.237  1.00 17.88 ? 384 PRO   A C   1 
ATOM   2532 O  O   . PRO   A 1 356 ? -9.857  -3.399  75.943  1.00 23.12 ? 384 PRO   A O   1 
ATOM   2533 C  CB  . PRO   A 1 356 ? -9.744  -5.860  78.017  1.00 23.93 ? 384 PRO   A CB  1 
ATOM   2534 C  CG  . PRO   A 1 356 ? -9.880  -5.762  79.504  1.00 22.89 ? 384 PRO   A CG  1 
ATOM   2535 C  CD  . PRO   A 1 356 ? -9.832  -4.258  79.826  1.00 20.44 ? 384 PRO   A CD  1 
ATOM   2536 N  N   . LEU   A 1 357 ? -8.155  -4.767  75.350  1.00 15.70 ? 385 LEU   A N   1 
ATOM   2537 C  CA  . LEU   A 1 357 ? -8.104  -4.387  73.945  1.00 16.37 ? 385 LEU   A CA  1 
ATOM   2538 C  C   . LEU   A 1 357 ? -9.142  -5.095  73.089  1.00 17.14 ? 385 LEU   A C   1 
ATOM   2539 O  O   . LEU   A 1 357 ? -9.336  -4.709  71.929  1.00 16.84 ? 385 LEU   A O   1 
ATOM   2540 C  CB  . LEU   A 1 357 ? -6.720  -4.681  73.367  1.00 14.04 ? 385 LEU   A CB  1 
ATOM   2541 C  CG  . LEU   A 1 357 ? -5.477  -4.303  74.178  1.00 16.22 ? 385 LEU   A CG  1 
ATOM   2542 C  CD1 . LEU   A 1 357 ? -4.237  -4.475  73.293  1.00 13.90 ? 385 LEU   A CD1 1 
ATOM   2543 C  CD2 . LEU   A 1 357 ? -5.589  -2.878  74.716  1.00 17.01 ? 385 LEU   A CD2 1 
ATOM   2544 N  N   . GLY   A 1 358 ? -9.760  -6.151  73.591  1.00 20.78 ? 386 GLY   A N   1 
ATOM   2545 C  CA  . GLY   A 1 358 ? -10.783 -6.807  72.808  1.00 16.71 ? 386 GLY   A CA  1 
ATOM   2546 C  C   . GLY   A 1 358 ? -11.817 -7.449  73.703  1.00 16.92 ? 386 GLY   A C   1 
ATOM   2547 O  O   . GLY   A 1 358 ? -11.972 -7.058  74.869  1.00 16.44 ? 386 GLY   A O   1 
ATOM   2548 N  N   . ASP   A 1 359 ? -12.497 -8.473  73.177  1.00 16.62 ? 387 ASP   A N   1 
ATOM   2549 C  CA  . ASP   A 1 359 ? -13.632 -9.061  73.881  1.00 14.92 ? 387 ASP   A CA  1 
ATOM   2550 C  C   . ASP   A 1 359 ? -13.248 -9.546  75.276  1.00 15.18 ? 387 ASP   A C   1 
ATOM   2551 O  O   . ASP   A 1 359 ? -13.975 -9.312  76.245  1.00 15.82 ? 387 ASP   A O   1 
ATOM   2552 C  CB  . ASP   A 1 359 ? -14.213 -10.215 73.057  1.00 12.35 ? 387 ASP   A CB  1 
ATOM   2553 C  CG  . ASP   A 1 359 ? -14.890 -9.750  71.786  1.00 18.13 ? 387 ASP   A CG  1 
ATOM   2554 O  OD1 . ASP   A 1 359 ? -15.275 -8.561  71.702  1.00 16.78 ? 387 ASP   A OD1 1 
ATOM   2555 O  OD2 . ASP   A 1 359 ? -15.046 -10.583 70.865  1.00 20.51 ? 387 ASP   A OD2 1 
ATOM   2556 N  N   . ARG   A 1 360 ? -12.043 -10.249 75.410  1.00 16.53 ? 388 ARG   A N   1 
ATOM   2557 C  CA  . ARG   A 1 360 ? -11.779 -10.936 76.662  1.00 14.79 ? 388 ARG   A CA  1 
ATOM   2558 C  C   . ARG   A 1 360 ? -11.000 -10.045 77.628  1.00 18.81 ? 388 ARG   A C   1 
ATOM   2559 O  O   . ARG   A 1 360 ? -10.172 -9.236  77.201  1.00 20.51 ? 388 ARG   A O   1 
ATOM   2560 C  CB  . ARG   A 1 360 ? -10.982 -12.204 76.406  1.00 15.07 ? 388 ARG   A CB  1 
ATOM   2561 C  CG  . ARG   A 1 360 ? -11.492 -13.025 75.246  1.00 16.79 ? 388 ARG   A CG  1 
ATOM   2562 C  CD  . ARG   A 1 360 ? -10.997 -14.445 75.361  1.00 15.60 ? 388 ARG   A CD  1 
ATOM   2563 N  NE  . ARG   A 1 360 ? -11.535 -15.298 74.311  1.00 17.18 ? 388 ARG   A NE  1 
ATOM   2564 C  CZ  . ARG   A 1 360 ? -11.171 -16.554 74.125  1.00 16.05 ? 388 ARG   A CZ  1 
ATOM   2565 N  NH1 . ARG   A 1 360 ? -11.711 -17.259 73.138  1.00 19.16 ? 388 ARG   A NH1 1 
ATOM   2566 N  NH2 . ARG   A 1 360 ? -10.272 -17.110 74.942  1.00 19.91 ? 388 ARG   A NH2 1 
ATOM   2567 N  N   . PRO   A 1 361 ? -11.249 -10.212 78.954  1.00 16.86 ? 389 PRO   A N   1 
ATOM   2568 C  CA  . PRO   A 1 361 ? -10.488 -9.474  79.968  1.00 17.71 ? 389 PRO   A CA  1 
ATOM   2569 C  C   . PRO   A 1 361 ? -9.081  -10.017 80.110  1.00 21.94 ? 389 PRO   A C   1 
ATOM   2570 O  O   . PRO   A 1 361 ? -8.699  -10.521 81.169  1.00 17.63 ? 389 PRO   A O   1 
ATOM   2571 C  CB  . PRO   A 1 361 ? -11.295 -9.700  81.250  1.00 14.53 ? 389 PRO   A CB  1 
ATOM   2572 C  CG  . PRO   A 1 361 ? -11.969 -11.015 81.031  1.00 17.10 ? 389 PRO   A CG  1 
ATOM   2573 C  CD  . PRO   A 1 361 ? -12.280 -11.073 79.555  1.00 16.42 ? 389 PRO   A CD  1 
ATOM   2574 N  N   . THR   A 1 362 ? -8.307  -9.922  79.039  1.00 19.77 ? 390 THR   A N   1 
ATOM   2575 C  CA  . THR   A 1 362 ? -6.998  -10.536 79.001  1.00 17.84 ? 390 THR   A CA  1 
ATOM   2576 C  C   . THR   A 1 362 ? -5.924  -9.479  78.778  1.00 18.83 ? 390 THR   A C   1 
ATOM   2577 O  O   . THR   A 1 362 ? -5.348  -8.966  79.743  1.00 17.58 ? 390 THR   A O   1 
ATOM   2578 C  CB  . THR   A 1 362 ? -6.945  -11.581 77.896  1.00 20.62 ? 390 THR   A CB  1 
ATOM   2579 O  OG1 . THR   A 1 362 ? -7.462  -11.011 76.677  1.00 12.89 ? 390 THR   A OG1 1 
ATOM   2580 C  CG2 . THR   A 1 362 ? -7.742  -12.844 78.301  1.00 19.40 ? 390 THR   A CG2 1 
ATOM   2581 N  N   . ILE   A 1 363 ? -5.674  -9.125  77.514  1.00 12.99 ? 391 ILE   A N   1 
ATOM   2582 C  CA  . ILE   A 1 363 ? -4.527  -8.293  77.175  1.00 17.07 ? 391 ILE   A CA  1 
ATOM   2583 C  C   . ILE   A 1 363 ? -4.930  -6.825  77.204  1.00 19.92 ? 391 ILE   A C   1 
ATOM   2584 O  O   . ILE   A 1 363 ? -6.051  -6.452  76.822  1.00 17.74 ? 391 ILE   A O   1 
ATOM   2585 C  CB  . ILE   A 1 363 ? -3.940  -8.695  75.808  1.00 21.89 ? 391 ILE   A CB  1 
ATOM   2586 C  CG1 . ILE   A 1 363 ? -2.707  -7.833  75.477  1.00 16.82 ? 391 ILE   A CG1 1 
ATOM   2587 C  CG2 . ILE   A 1 363 ? -5.009  -8.630  74.727  1.00 17.63 ? 391 ILE   A CG2 1 
ATOM   2588 C  CD1 . ILE   A 1 363 ? -2.101  -8.140  74.144  1.00 16.13 ? 391 ILE   A CD1 1 
ATOM   2589 N  N   . PHE   A 1 364 ? -4.018  -5.989  77.692  1.00 17.17 ? 392 PHE   A N   1 
ATOM   2590 C  CA  . PHE   A 1 364 ? -4.240  -4.560  77.752  1.00 17.12 ? 392 PHE   A CA  1 
ATOM   2591 C  C   . PHE   A 1 364 ? -2.931  -3.862  77.417  1.00 19.46 ? 392 PHE   A C   1 
ATOM   2592 O  O   . PHE   A 1 364 ? -1.923  -4.506  77.104  1.00 17.54 ? 392 PHE   A O   1 
ATOM   2593 C  CB  . PHE   A 1 364 ? -4.811  -4.149  79.117  1.00 20.72 ? 392 PHE   A CB  1 
ATOM   2594 C  CG  . PHE   A 1 364 ? -3.996  -4.602  80.313  1.00 21.04 ? 392 PHE   A CG  1 
ATOM   2595 C  CD1 . PHE   A 1 364 ? -4.281  -5.800  80.948  1.00 19.36 ? 392 PHE   A CD1 1 
ATOM   2596 C  CD2 . PHE   A 1 364 ? -2.985  -3.798  80.832  1.00 22.05 ? 392 PHE   A CD2 1 
ATOM   2597 C  CE1 . PHE   A 1 364 ? -3.572  -6.203  82.063  1.00 20.09 ? 392 PHE   A CE1 1 
ATOM   2598 C  CE2 . PHE   A 1 364 ? -2.250  -4.193  81.954  1.00 20.63 ? 392 PHE   A CE2 1 
ATOM   2599 C  CZ  . PHE   A 1 364 ? -2.544  -5.395  82.571  1.00 23.63 ? 392 PHE   A CZ  1 
ATOM   2600 N  N   . ILE   A 1 365 ? -2.949  -2.531  77.459  1.00 22.06 ? 393 ILE   A N   1 
ATOM   2601 C  CA  . ILE   A 1 365 ? -1.816  -1.713  77.030  1.00 17.04 ? 393 ILE   A CA  1 
ATOM   2602 C  C   . ILE   A 1 365 ? -1.522  -0.698  78.122  1.00 16.24 ? 393 ILE   A C   1 
ATOM   2603 O  O   . ILE   A 1 365 ? -2.430  -0.263  78.831  1.00 19.51 ? 393 ILE   A O   1 
ATOM   2604 C  CB  . ILE   A 1 365 ? -2.105  -1.040  75.670  1.00 17.74 ? 393 ILE   A CB  1 
ATOM   2605 C  CG1 . ILE   A 1 365 ? -1.666  -1.960  74.535  1.00 12.51 ? 393 ILE   A CG1 1 
ATOM   2606 C  CG2 . ILE   A 1 365 ? -1.495  0.349   75.571  1.00 15.83 ? 393 ILE   A CG2 1 
ATOM   2607 C  CD1 . ILE   A 1 365 ? -2.087  -1.511  73.154  1.00 10.83 ? 393 ILE   A CD1 1 
ATOM   2608 N  N   . GLU   A 1 366 ? -0.237  -0.408  78.324  1.00 18.25 ? 394 GLU   A N   1 
ATOM   2609 C  CA  . GLU   A 1 366 ? 0.231   0.601   79.264  1.00 17.01 ? 394 GLU   A CA  1 
ATOM   2610 C  C   . GLU   A 1 366 ? 0.936   1.686   78.466  1.00 19.78 ? 394 GLU   A C   1 
ATOM   2611 O  O   . GLU   A 1 366 ? 1.649   1.396   77.502  1.00 20.44 ? 394 GLU   A O   1 
ATOM   2612 C  CB  . GLU   A 1 366 ? 1.167   -0.032  80.307  1.00 23.63 ? 394 GLU   A CB  1 
ATOM   2613 C  CG  . GLU   A 1 366 ? 1.794   0.901   81.314  1.00 24.79 ? 394 GLU   A CG  1 
ATOM   2614 C  CD  . GLU   A 1 366 ? 2.861   0.205   82.162  1.00 28.42 ? 394 GLU   A CD  1 
ATOM   2615 O  OE1 . GLU   A 1 366 ? 3.091   -1.011  81.962  1.00 29.50 ? 394 GLU   A OE1 1 
ATOM   2616 O  OE2 . GLU   A 1 366 ? 3.470   0.869   83.035  1.00 27.82 ? 394 GLU   A OE2 1 
ATOM   2617 N  N   . ILE   A 1 367 ? 0.686   2.940   78.812  1.00 21.04 ? 395 ILE   A N   1 
ATOM   2618 C  CA  . ILE   A 1 367 ? 1.448   4.059   78.279  1.00 17.37 ? 395 ILE   A CA  1 
ATOM   2619 C  C   . ILE   A 1 367 ? 2.408   4.508   79.367  1.00 24.09 ? 395 ILE   A C   1 
ATOM   2620 O  O   . ILE   A 1 367 ? 1.988   4.745   80.507  1.00 21.58 ? 395 ILE   A O   1 
ATOM   2621 C  CB  . ILE   A 1 367 ? 0.539   5.222   77.851  1.00 25.50 ? 395 ILE   A CB  1 
ATOM   2622 C  CG1 . ILE   A 1 367 ? -0.562  4.736   76.912  1.00 16.98 ? 395 ILE   A CG1 1 
ATOM   2623 C  CG2 . ILE   A 1 367 ? 1.374   6.347   77.221  1.00 26.39 ? 395 ILE   A CG2 1 
ATOM   2624 C  CD1 . ILE   A 1 367 ? -0.034  3.976   75.709  1.00 20.93 ? 395 ILE   A CD1 1 
ATOM   2625 N  N   . ILE   A 1 368 ? 3.695   4.632   79.028  1.00 22.77 ? 396 ILE   A N   1 
ATOM   2626 C  CA  . ILE   A 1 368 ? 4.676   5.037   80.027  1.00 20.54 ? 396 ILE   A CA  1 
ATOM   2627 C  C   . ILE   A 1 368 ? 5.582   6.131   79.488  1.00 21.59 ? 396 ILE   A C   1 
ATOM   2628 O  O   . ILE   A 1 368 ? 5.830   6.243   78.279  1.00 21.05 ? 396 ILE   A O   1 
ATOM   2629 C  CB  . ILE   A 1 368 ? 5.551   3.867   80.544  1.00 24.04 ? 396 ILE   A CB  1 
ATOM   2630 C  CG1 . ILE   A 1 368 ? 6.471   3.340   79.457  1.00 25.52 ? 396 ILE   A CG1 1 
ATOM   2631 C  CG2 . ILE   A 1 368 ? 4.725   2.764   81.047  1.00 26.20 ? 396 ILE   A CG2 1 
ATOM   2632 C  CD1 . ILE   A 1 368 ? 7.888   3.157   79.970  1.00 28.45 ? 396 ILE   A CD1 1 
ATOM   2633 N  N   . GLN   A 1 369 ? 6.070   6.948   80.415  1.00 18.58 ? 397 GLN   A N   1 
ATOM   2634 C  CA  . GLN   A 1 369 ? 7.190   7.842   80.177  1.00 22.41 ? 397 GLN   A CA  1 
ATOM   2635 C  C   . GLN   A 1 369 ? 8.065   7.855   81.416  1.00 21.59 ? 397 GLN   A C   1 
ATOM   2636 O  O   . GLN   A 1 369 ? 7.559   7.975   82.532  1.00 24.03 ? 397 GLN   A O   1 
ATOM   2637 C  CB  . GLN   A 1 369 ? 6.744   9.264   79.858  1.00 20.77 ? 397 GLN   A CB  1 
ATOM   2638 C  CG  . GLN   A 1 369 ? 7.873   10.104  79.359  1.00 23.36 ? 397 GLN   A CG  1 
ATOM   2639 C  CD  . GLN   A 1 369 ? 7.396   11.350  78.657  1.00 29.25 ? 397 GLN   A CD  1 
ATOM   2640 O  OE1 . GLN   A 1 369 ? 6.249   11.773  78.822  1.00 28.21 ? 397 GLN   A OE1 1 
ATOM   2641 N  NE2 . GLN   A 1 369 ? 8.276   11.953  77.869  1.00 29.03 ? 397 GLN   A NE2 1 
ATOM   2642 N  N   . ARG   A 1 370 ? 9.375   7.771   81.204  1.00 22.66 ? 398 ARG   A N   1 
ATOM   2643 C  CA  . ARG   A 1 370 ? 10.359  7.683   82.274  1.00 26.17 ? 398 ARG   A CA  1 
ATOM   2644 C  C   . ARG   A 1 370 ? 11.215  8.947   82.349  1.00 26.03 ? 398 ARG   A C   1 
ATOM   2645 O  O   . ARG   A 1 370 ? 11.706  9.447   81.329  1.00 22.09 ? 398 ARG   A O   1 
ATOM   2646 C  CB  . ARG   A 1 370 ? 11.271  6.472   82.069  1.00 28.02 ? 398 ARG   A CB  1 
ATOM   2647 C  CG  . ARG   A 1 370 ? 10.548  5.172   81.832  1.00 22.38 ? 398 ARG   A CG  1 
ATOM   2648 C  CD  . ARG   A 1 370 ? 11.566  4.068   81.651  1.00 29.67 ? 398 ARG   A CD  1 
ATOM   2649 N  NE  . ARG   A 1 370 ? 10.969  2.755   81.450  1.00 27.01 ? 398 ARG   A NE  1 
ATOM   2650 C  CZ  . ARG   A 1 370 ? 10.529  1.986   82.436  1.00 24.20 ? 398 ARG   A CZ  1 
ATOM   2651 N  NH1 . ARG   A 1 370 ? 10.607  2.421   83.673  1.00 18.97 ? 398 ARG   A NH1 1 
ATOM   2652 N  NH2 . ARG   A 1 370 ? 10.005  0.793   82.182  1.00 23.39 ? 398 ARG   A NH2 1 
ATOM   2653 N  N   . VAL   A 1 371 ? 11.401  9.459   83.562  1.00 19.52 ? 399 VAL   A N   1 
ATOM   2654 C  CA  . VAL   A 1 371 ? 12.236  10.632  83.794  1.00 28.24 ? 399 VAL   A CA  1 
ATOM   2655 C  C   . VAL   A 1 371 ? 13.478  10.181  84.556  1.00 27.33 ? 399 VAL   A C   1 
ATOM   2656 O  O   . VAL   A 1 371 ? 13.372  9.584   85.637  1.00 29.78 ? 399 VAL   A O   1 
ATOM   2657 C  CB  . VAL   A 1 371 ? 11.476  11.728  84.558  1.00 29.45 ? 399 VAL   A CB  1 
ATOM   2658 C  CG1 . VAL   A 1 371 ? 12.188  13.087  84.427  1.00 34.40 ? 399 VAL   A CG1 1 
ATOM   2659 C  CG2 . VAL   A 1 371 ? 10.032  11.827  84.058  1.00 31.28 ? 399 VAL   A CG2 1 
ATOM   2660 N  N   . GLY   A 1 372 ? 14.653  10.438  83.976  1.00 32.51 ? 400 GLY   A N   1 
ATOM   2661 C  CA  . GLY   A 1 372 ? 15.912  10.192  84.666  1.00 34.99 ? 400 GLY   A CA  1 
ATOM   2662 C  C   . GLY   A 1 372 ? 16.912  9.279   83.976  1.00 36.90 ? 400 GLY   A C   1 
ATOM   2663 O  O   . GLY   A 1 372 ? 16.890  9.109   82.750  1.00 32.77 ? 400 GLY   A O   1 
ATOM   2664 N  N   . CYS   A 1 373 ? 17.813  8.717   84.783  1.00 32.50 ? 401 CYS   A N   1 
ATOM   2665 C  CA  . CYS   A 1 373 ? 18.853  7.782   84.350  1.00 40.47 ? 401 CYS   A CA  1 
ATOM   2666 C  C   . CYS   A 1 373 ? 19.485  8.201   83.027  1.00 41.22 ? 401 CYS   A C   1 
ATOM   2667 O  O   . CYS   A 1 373 ? 19.641  7.406   82.097  1.00 44.84 ? 401 CYS   A O   1 
ATOM   2668 C  CB  . CYS   A 1 373 ? 18.305  6.359   84.266  1.00 30.77 ? 401 CYS   A CB  1 
ATOM   2669 S  SG  . CYS   A 1 373 ? 17.208  5.900   85.647  1.00 31.58 ? 401 CYS   A SG  1 
ATOM   2670 N  N   . MET   A 1 374 ? 19.863  9.472   82.947  1.00 41.22 ? 402 MET   A N   1 
ATOM   2671 C  CA  . MET   A 1 374 ? 20.480  10.001  81.739  1.00 39.64 ? 402 MET   A CA  1 
ATOM   2672 C  C   . MET   A 1 374 ? 21.991  9.791   81.782  1.00 51.89 ? 402 MET   A C   1 
ATOM   2673 O  O   . MET   A 1 374 ? 22.649  10.113  82.778  1.00 47.94 ? 402 MET   A O   1 
ATOM   2674 C  CB  . MET   A 1 374 ? 20.143  11.481  81.560  1.00 41.62 ? 402 MET   A CB  1 
ATOM   2675 C  CG  . MET   A 1 374 ? 18.679  11.733  81.263  1.00 35.60 ? 402 MET   A CG  1 
ATOM   2676 S  SD  . MET   A 1 374 ? 18.142  10.975  79.717  1.00 45.39 ? 402 MET   A SD  1 
ATOM   2677 C  CE  . MET   A 1 374 ? 19.211  11.825  78.562  1.00 45.22 ? 402 MET   A CE  1 
ATOM   2678 N  N   . MET   A 1 375 ? 22.526  9.222   80.706  1.00 48.01 ? 403 MET   A N   1 
ATOM   2679 C  CA  . MET   A 1 375 ? 23.958  9.052   80.526  1.00 45.47 ? 403 MET   A CA  1 
ATOM   2680 C  C   . MET   A 1 375 ? 24.289  9.279   79.058  1.00 51.78 ? 403 MET   A C   1 
ATOM   2681 O  O   . MET   A 1 375 ? 23.500  9.889   78.328  1.00 45.46 ? 403 MET   A O   1 
ATOM   2682 C  CB  . MET   A 1 375 ? 24.410  7.663   80.970  1.00 49.49 ? 403 MET   A CB  1 
ATOM   2683 C  CG  . MET   A 1 375 ? 24.056  7.318   82.405  1.00 50.65 ? 403 MET   A CG  1 
ATOM   2684 S  SD  . MET   A 1 375 ? 24.057  5.551   82.679  1.00 70.51 ? 403 MET   A SD  1 
ATOM   2685 C  CE  . MET   A 1 375 ? 25.810  5.275   82.987  1.00 58.57 ? 403 MET   A CE  1 
ATOM   2686 N  N   . TYR   A 1 383 ? 21.543  9.459   76.238  1.00 52.97 ? 411 TYR   A N   1 
ATOM   2687 C  CA  . TYR   A 1 383 ? 20.651  8.301   76.245  1.00 39.68 ? 411 TYR   A CA  1 
ATOM   2688 C  C   . TYR   A 1 383 ? 20.158  7.962   77.670  1.00 41.56 ? 411 TYR   A C   1 
ATOM   2689 O  O   . TYR   A 1 383 ? 20.780  8.333   78.656  1.00 39.92 ? 411 TYR   A O   1 
ATOM   2690 C  CB  . TYR   A 1 383 ? 21.353  7.097   75.613  1.00 47.47 ? 411 TYR   A CB  1 
ATOM   2691 N  N   . GLN   A 1 384 ? 19.030  7.261   77.768  1.00 47.18 ? 412 GLN   A N   1 
ATOM   2692 C  CA  . GLN   A 1 384 ? 18.418  6.904   79.044  1.00 38.05 ? 412 GLN   A CA  1 
ATOM   2693 C  C   . GLN   A 1 384 ? 18.503  5.399   79.246  1.00 39.35 ? 412 GLN   A C   1 
ATOM   2694 O  O   . GLN   A 1 384 ? 18.268  4.627   78.312  1.00 40.60 ? 412 GLN   A O   1 
ATOM   2695 C  CB  . GLN   A 1 384 ? 16.948  7.348   79.088  1.00 34.83 ? 412 GLN   A CB  1 
ATOM   2696 C  CG  . GLN   A 1 384 ? 16.127  6.744   80.220  1.00 33.16 ? 412 GLN   A CG  1 
ATOM   2697 C  CD  . GLN   A 1 384 ? 14.713  7.326   80.303  1.00 36.44 ? 412 GLN   A CD  1 
ATOM   2698 O  OE1 . GLN   A 1 384 ? 13.941  7.263   79.342  1.00 29.25 ? 412 GLN   A OE1 1 
ATOM   2699 N  NE2 . GLN   A 1 384 ? 14.376  7.899   81.450  1.00 31.45 ? 412 GLN   A NE2 1 
ATOM   2700 N  N   . SER   A 1 385 ? 18.832  4.972   80.459  1.00 35.81 ? 413 SER   A N   1 
ATOM   2701 C  CA  . SER   A 1 385 ? 18.991  3.547   80.691  1.00 38.40 ? 413 SER   A CA  1 
ATOM   2702 C  C   . SER   A 1 385 ? 17.624  2.879   80.786  1.00 34.38 ? 413 SER   A C   1 
ATOM   2703 O  O   . SER   A 1 385 ? 16.675  3.440   81.348  1.00 29.71 ? 413 SER   A O   1 
ATOM   2704 C  CB  . SER   A 1 385 ? 19.806  3.277   81.955  1.00 32.15 ? 413 SER   A CB  1 
ATOM   2705 O  OG  . SER   A 1 385 ? 18.988  3.383   83.100  1.00 43.95 ? 413 SER   A OG  1 
ATOM   2706 N  N   . GLY   A 1 386 ? 17.542  1.671   80.237  1.00 29.66 ? 414 GLY   A N   1 
ATOM   2707 C  CA  . GLY   A 1 386 ? 16.265  0.991   80.126  1.00 29.72 ? 414 GLY   A CA  1 
ATOM   2708 C  C   . GLY   A 1 386 ? 15.687  0.671   81.492  1.00 29.11 ? 414 GLY   A C   1 
ATOM   2709 O  O   . GLY   A 1 386 ? 16.404  0.345   82.442  1.00 26.74 ? 414 GLY   A O   1 
ATOM   2710 N  N   . GLY   A 1 387 ? 14.370  0.786   81.588  1.00 25.71 ? 415 GLY   A N   1 
ATOM   2711 C  CA  . GLY   A 1 387 ? 13.690  0.483   82.826  1.00 30.06 ? 415 GLY   A CA  1 
ATOM   2712 C  C   . GLY   A 1 387 ? 13.836  1.536   83.893  1.00 28.06 ? 415 GLY   A C   1 
ATOM   2713 O  O   . GLY   A 1 387 ? 13.565  1.250   85.065  1.00 24.76 ? 415 GLY   A O   1 
ATOM   2714 N  N   . CYS   A 1 388 ? 14.261  2.743   83.526  1.00 27.91 ? 416 CYS   A N   1 
ATOM   2715 C  CA  . CYS   A 1 388 ? 14.533  3.782   84.514  1.00 26.47 ? 416 CYS   A CA  1 
ATOM   2716 C  C   . CYS   A 1 388 ? 13.321  4.050   85.394  1.00 28.00 ? 416 CYS   A C   1 
ATOM   2717 O  O   . CYS   A 1 388 ? 12.297  4.545   84.914  1.00 29.08 ? 416 CYS   A O   1 
ATOM   2718 C  CB  . CYS   A 1 388 ? 14.968  5.073   83.825  1.00 29.33 ? 416 CYS   A CB  1 
ATOM   2719 S  SG  . CYS   A 1 388 ? 15.363  6.402   84.973  1.00 34.26 ? 416 CYS   A SG  1 
ATOM   2720 N  N   . GLY   A 1 389 ? 13.421  3.721   86.682  1.00 26.48 ? 417 GLY   A N   1 
ATOM   2721 C  CA  . GLY   A 1 389 ? 12.345  3.979   87.610  1.00 26.70 ? 417 GLY   A CA  1 
ATOM   2722 C  C   . GLY   A 1 389 ? 11.438  2.805   87.876  1.00 28.05 ? 417 GLY   A C   1 
ATOM   2723 O  O   . GLY   A 1 389 ? 10.529  2.922   88.704  1.00 28.00 ? 417 GLY   A O   1 
ATOM   2724 N  N   . GLY   A 1 390 ? 11.643  1.686   87.197  1.00 25.99 ? 418 GLY   A N   1 
ATOM   2725 C  CA  . GLY   A 1 390 ? 10.949  0.475   87.568  1.00 27.79 ? 418 GLY   A CA  1 
ATOM   2726 C  C   . GLY   A 1 390 ? 9.719   0.234   86.726  1.00 23.48 ? 418 GLY   A C   1 
ATOM   2727 O  O   . GLY   A 1 390 ? 9.683   0.590   85.544  1.00 22.65 ? 418 GLY   A O   1 
ATOM   2728 N  N   . PHE   A 1 391 ? 8.708   -0.377  87.322  1.00 26.64 ? 419 PHE   A N   1 
ATOM   2729 C  CA  . PHE   A 1 391 ? 7.533   -0.768  86.558  1.00 23.99 ? 419 PHE   A CA  1 
ATOM   2730 C  C   . PHE   A 1 391 ? 6.233   -0.441  87.264  1.00 29.74 ? 419 PHE   A C   1 
ATOM   2731 O  O   . PHE   A 1 391 ? 5.163   -0.753  86.727  1.00 32.05 ? 419 PHE   A O   1 
ATOM   2732 C  CB  . PHE   A 1 391 ? 7.603   -2.262  86.226  1.00 25.34 ? 419 PHE   A CB  1 
ATOM   2733 C  CG  . PHE   A 1 391 ? 8.848   -2.634  85.485  1.00 25.51 ? 419 PHE   A CG  1 
ATOM   2734 C  CD1 . PHE   A 1 391 ? 9.996   -3.023  86.172  1.00 27.35 ? 419 PHE   A CD1 1 
ATOM   2735 C  CD2 . PHE   A 1 391 ? 8.896   -2.546  84.107  1.00 22.91 ? 419 PHE   A CD2 1 
ATOM   2736 C  CE1 . PHE   A 1 391 ? 11.155  -3.339  85.488  1.00 23.69 ? 419 PHE   A CE1 1 
ATOM   2737 C  CE2 . PHE   A 1 391 ? 10.047  -2.863  83.425  1.00 22.70 ? 419 PHE   A CE2 1 
ATOM   2738 C  CZ  . PHE   A 1 391 ? 11.181  -3.257  84.119  1.00 21.53 ? 419 PHE   A CZ  1 
ATOM   2739 N  N   . GLY   A 1 392 ? 6.290   0.182   88.438  1.00 32.93 ? 420 GLY   A N   1 
ATOM   2740 C  CA  . GLY   A 1 392 ? 5.121   0.684   89.116  1.00 33.80 ? 420 GLY   A CA  1 
ATOM   2741 C  C   . GLY   A 1 392 ? 4.687   -0.106  90.323  1.00 35.05 ? 420 GLY   A C   1 
ATOM   2742 O  O   . GLY   A 1 392 ? 3.571   0.111   90.803  1.00 37.23 ? 420 GLY   A O   1 
ATOM   2743 N  N   . LYS   A 1 393 ? 5.519   -1.012  90.841  1.00 35.55 ? 421 LYS   A N   1 
ATOM   2744 C  CA  . LYS   A 1 393 ? 5.032   -1.873  91.912  1.00 39.76 ? 421 LYS   A CA  1 
ATOM   2745 C  C   . LYS   A 1 393 ? 4.693   -1.065  93.157  1.00 39.32 ? 421 LYS   A C   1 
ATOM   2746 O  O   . LYS   A 1 393 ? 3.838   -1.478  93.950  1.00 45.69 ? 421 LYS   A O   1 
ATOM   2747 C  CB  . LYS   A 1 393 ? 6.047   -2.979  92.222  1.00 41.35 ? 421 LYS   A CB  1 
ATOM   2748 C  CG  . LYS   A 1 393 ? 6.356   -3.886  91.021  1.00 41.84 ? 421 LYS   A CG  1 
ATOM   2749 C  CD  . LYS   A 1 393 ? 7.161   -5.131  91.415  1.00 41.15 ? 421 LYS   A CD  1 
ATOM   2750 C  CE  . LYS   A 1 393 ? 7.685   -5.874  90.178  1.00 46.28 ? 421 LYS   A CE  1 
ATOM   2751 N  NZ  . LYS   A 1 393 ? 8.629   -5.041  89.327  1.00 37.91 ? 421 LYS   A NZ  1 
ATOM   2752 N  N   . GLY   A 1 394 ? 5.316   0.102   93.328  1.00 42.26 ? 422 GLY   A N   1 
ATOM   2753 C  CA  . GLY   A 1 394 ? 4.933   0.967   94.427  1.00 44.12 ? 422 GLY   A CA  1 
ATOM   2754 C  C   . GLY   A 1 394 ? 3.496   1.437   94.325  1.00 41.37 ? 422 GLY   A C   1 
ATOM   2755 O  O   . GLY   A 1 394 ? 2.859   1.724   95.342  1.00 39.09 ? 422 GLY   A O   1 
ATOM   2756 N  N   . ASN   A 1 395 ? 2.961   1.497   93.101  1.00 43.29 ? 423 ASN   A N   1 
ATOM   2757 C  CA  . ASN   A 1 395 ? 1.617   2.011   92.876  1.00 42.43 ? 423 ASN   A CA  1 
ATOM   2758 C  C   . ASN   A 1 395 ? 0.527   1.051   93.340  1.00 44.45 ? 423 ASN   A C   1 
ATOM   2759 O  O   . ASN   A 1 395 ? -0.588  1.501   93.621  1.00 47.85 ? 423 ASN   A O   1 
ATOM   2760 C  CB  . ASN   A 1 395 ? 1.438   2.363   91.400  1.00 35.90 ? 423 ASN   A CB  1 
ATOM   2761 C  CG  . ASN   A 1 395 ? 1.821   3.799   91.104  1.00 33.86 ? 423 ASN   A CG  1 
ATOM   2762 O  OD1 . ASN   A 1 395 ? 1.522   4.698   91.885  1.00 32.72 ? 423 ASN   A OD1 1 
ATOM   2763 N  ND2 . ASN   A 1 395 ? 2.489   4.022   89.985  1.00 29.99 ? 423 ASN   A ND2 1 
ATOM   2764 N  N   . PHE   A 1 396 ? 0.809   -0.251  93.436  1.00 43.31 ? 424 PHE   A N   1 
ATOM   2765 C  CA  . PHE   A 1 396 ? -0.110  -1.126  94.154  1.00 44.77 ? 424 PHE   A CA  1 
ATOM   2766 C  C   . PHE   A 1 396 ? -0.334  -0.601  95.571  1.00 47.48 ? 424 PHE   A C   1 
ATOM   2767 O  O   . PHE   A 1 396 ? -1.475  -0.440  96.019  1.00 50.23 ? 424 PHE   A O   1 
ATOM   2768 C  CB  . PHE   A 1 396 ? 0.421   -2.566  94.181  1.00 46.57 ? 424 PHE   A CB  1 
ATOM   2769 C  CG  . PHE   A 1 396 ? 0.338   -3.285  92.851  1.00 46.68 ? 424 PHE   A CG  1 
ATOM   2770 C  CD1 . PHE   A 1 396 ? 1.392   -3.231  91.945  1.00 47.17 ? 424 PHE   A CD1 1 
ATOM   2771 C  CD2 . PHE   A 1 396 ? -0.779  -4.036  92.520  1.00 45.29 ? 424 PHE   A CD2 1 
ATOM   2772 C  CE1 . PHE   A 1 396 ? 1.324   -3.901  90.730  1.00 41.86 ? 424 PHE   A CE1 1 
ATOM   2773 C  CE2 . PHE   A 1 396 ? -0.856  -4.702  91.304  1.00 43.84 ? 424 PHE   A CE2 1 
ATOM   2774 C  CZ  . PHE   A 1 396 ? 0.196   -4.632  90.407  1.00 41.85 ? 424 PHE   A CZ  1 
ATOM   2775 N  N   . SER   A 1 397 ? 0.755   -0.279  96.273  1.00 47.48 ? 425 SER   A N   1 
ATOM   2776 C  CA  . SER   A 1 397 ? 0.637   0.214   97.641  1.00 45.58 ? 425 SER   A CA  1 
ATOM   2777 C  C   . SER   A 1 397 ? -0.029  1.585   97.686  1.00 49.16 ? 425 SER   A C   1 
ATOM   2778 O  O   . SER   A 1 397 ? -0.913  1.825   98.518  1.00 51.46 ? 425 SER   A O   1 
ATOM   2779 C  CB  . SER   A 1 397 ? 2.018   0.261   98.296  1.00 47.45 ? 425 SER   A CB  1 
ATOM   2780 O  OG  . SER   A 1 397 ? 1.928   0.737   99.626  1.00 43.52 ? 425 SER   A OG  1 
ATOM   2781 N  N   . GLU   A 1 398 ? 0.383   2.499   96.805  1.00 46.19 ? 426 GLU   A N   1 
ATOM   2782 C  CA  . GLU   A 1 398 ? -0.163  3.852   96.830  1.00 47.76 ? 426 GLU   A CA  1 
ATOM   2783 C  C   . GLU   A 1 398 ? -1.644  3.894   96.493  1.00 50.08 ? 426 GLU   A C   1 
ATOM   2784 O  O   . GLU   A 1 398 ? -2.317  4.850   96.879  1.00 51.79 ? 426 GLU   A O   1 
ATOM   2785 C  CB  . GLU   A 1 398 ? 0.597   4.757   95.864  1.00 42.58 ? 426 GLU   A CB  1 
ATOM   2786 C  CG  . GLU   A 1 398 ? 2.063   4.916   96.200  1.00 49.27 ? 426 GLU   A CG  1 
ATOM   2787 C  CD  . GLU   A 1 398 ? 2.281   5.636   97.522  1.00 53.19 ? 426 GLU   A CD  1 
ATOM   2788 O  OE1 . GLU   A 1 398 ? 3.208   5.241   98.267  1.00 54.55 ? 426 GLU   A OE1 1 
ATOM   2789 O  OE2 . GLU   A 1 398 ? 1.520   6.589   97.811  1.00 45.31 ? 426 GLU   A OE2 1 
ATOM   2790 N  N   . LEU   A 1 399 ? -2.166  2.894   95.783  1.00 49.63 ? 427 LEU   A N   1 
ATOM   2791 C  CA  . LEU   A 1 399 ? -3.583  2.912   95.444  1.00 48.59 ? 427 LEU   A CA  1 
ATOM   2792 C  C   . LEU   A 1 399 ? -4.446  2.376   96.582  1.00 51.77 ? 427 LEU   A C   1 
ATOM   2793 O  O   . LEU   A 1 399 ? -5.476  2.977   96.908  1.00 55.31 ? 427 LEU   A O   1 
ATOM   2794 C  CB  . LEU   A 1 399 ? -3.821  2.127   94.161  1.00 47.44 ? 427 LEU   A CB  1 
ATOM   2795 C  CG  . LEU   A 1 399 ? -3.358  2.868   92.908  1.00 45.38 ? 427 LEU   A CG  1 
ATOM   2796 C  CD1 . LEU   A 1 399 ? -3.231  1.897   91.744  1.00 37.18 ? 427 LEU   A CD1 1 
ATOM   2797 C  CD2 . LEU   A 1 399 ? -4.314  4.017   92.577  1.00 38.22 ? 427 LEU   A CD2 1 
ATOM   2798 N  N   . PHE   A 1 400 ? -4.054  1.258   97.200  1.00 50.88 ? 428 PHE   A N   1 
ATOM   2799 C  CA  . PHE   A 1 400 ? -4.783  0.778   98.372  1.00 52.82 ? 428 PHE   A CA  1 
ATOM   2800 C  C   . PHE   A 1 400 ? -4.916  1.892   99.402  1.00 55.68 ? 428 PHE   A C   1 
ATOM   2801 O  O   . PHE   A 1 400 ? -6.027  2.315   99.747  1.00 53.68 ? 428 PHE   A O   1 
ATOM   2802 C  CB  . PHE   A 1 400 ? -4.083  -0.443  98.977  1.00 43.30 ? 428 PHE   A CB  1 
ATOM   2803 N  N   . LYS   A 1 401 ? -3.772  2.420   99.858  1.00 54.15 ? 429 LYS   A N   1 
ATOM   2804 C  CA  . LYS   A 1 401 ? -3.783  3.555   100.775 1.00 56.43 ? 429 LYS   A CA  1 
ATOM   2805 C  C   . LYS   A 1 401 ? -4.510  4.762   100.180 1.00 60.36 ? 429 LYS   A C   1 
ATOM   2806 O  O   . LYS   A 1 401 ? -5.082  5.567   100.923 1.00 60.73 ? 429 LYS   A O   1 
ATOM   2807 C  CB  . LYS   A 1 401 ? -2.352  3.931   101.164 1.00 46.65 ? 429 LYS   A CB  1 
ATOM   2808 N  N   . SER   A 1 402 ? -4.517  4.897   98.852  1.00 55.78 ? 430 SER   A N   1 
ATOM   2809 C  CA  . SER   A 1 402 ? -5.186  6.037   98.235  1.00 55.58 ? 430 SER   A CA  1 
ATOM   2810 C  C   . SER   A 1 402 ? -6.685  6.018   98.518  1.00 61.29 ? 430 SER   A C   1 
ATOM   2811 O  O   . SER   A 1 402 ? -7.257  7.017   98.978  1.00 61.84 ? 430 SER   A O   1 
ATOM   2812 C  CB  . SER   A 1 402 ? -4.941  6.043   96.731  1.00 51.46 ? 430 SER   A CB  1 
ATOM   2813 O  OG  . SER   A 1 402 ? -5.377  7.259   96.173  1.00 53.59 ? 430 SER   A OG  1 
ATOM   2814 N  N   . ILE   A 1 403 ? -7.346  4.945   98.219  1.00 60.32 ? 431 ILE   A N   1 
ATOM   2815 C  CA  . ILE   A 1 403 ? -8.752  4.901   98.445  1.00 60.21 ? 431 ILE   A CA  1 
ATOM   2816 C  C   . ILE   A 1 403 ? -8.961  4.966   100.007 1.00 63.07 ? 431 ILE   A C   1 
ATOM   2817 O  O   . ILE   A 1 403 ? -9.778  5.653   100.551 1.00 69.33 ? 431 ILE   A O   1 
ATOM   2818 C  CB  . ILE   A 1 403 ? -9.325  3.621   97.828  1.00 60.22 ? 431 ILE   A CB  1 
ATOM   2819 C  CG1 . ILE   A 1 403 ? -8.956  2.417   98.665  1.00 56.61 ? 431 ILE   A CG1 1 
ATOM   2820 C  CG2 . ILE   A 1 403 ? -8.772  3.267   96.422  1.00 60.20 ? 431 ILE   A CG2 1 
ATOM   2821 C  CD1 . ILE   A 1 403 ? -9.618  1.170   98.130  1.00 48.24 ? 431 ILE   A CD1 1 
ATOM   2822 N  N   . GLU   A 1 404 ? -8.076  4.322   100.700 1.00 60.54 ? 432 GLU   A N   1 
ATOM   2823 C  CA  . GLU   A 1 404 ? -8.162  4.140   102.100 1.00 59.39 ? 432 GLU   A CA  1 
ATOM   2824 C  C   . GLU   A 1 404 ? -8.542  5.427   102.774 1.00 62.71 ? 432 GLU   A C   1 
ATOM   2825 O  O   . GLU   A 1 404 ? -9.421  5.420   103.592 1.00 67.68 ? 432 GLU   A O   1 
ATOM   2826 C  CB  . GLU   A 1 404 ? -6.831  3.721   102.641 1.00 57.58 ? 432 GLU   A CB  1 
ATOM   2827 N  N   . GLU   A 1 405 ? -7.842  6.511   102.479 1.00 63.67 ? 433 GLU   A N   1 
ATOM   2828 C  CA  . GLU   A 1 405 ? -8.242  7.791   103.015 1.00 65.98 ? 433 GLU   A CA  1 
ATOM   2829 C  C   . GLU   A 1 405 ? -9.376  8.360   102.205 1.00 70.05 ? 433 GLU   A C   1 
ATOM   2830 O  O   . GLU   A 1 405 ? -10.213 9.099   102.698 1.00 76.48 ? 433 GLU   A O   1 
ATOM   2831 C  CB  . GLU   A 1 405 ? -7.091  8.787   103.014 1.00 64.99 ? 433 GLU   A CB  1 
ATOM   2832 N  N   . TYR   A 1 406 ? -9.388  8.079   100.924 1.00 67.87 ? 434 TYR   A N   1 
ATOM   2833 C  CA  . TYR   A 1 406 ? -10.494 8.669   100.178 1.00 64.86 ? 434 TYR   A CA  1 
ATOM   2834 C  C   . TYR   A 1 406 ? -11.827 8.313   100.819 1.00 66.87 ? 434 TYR   A C   1 
ATOM   2835 O  O   . TYR   A 1 406 ? -12.660 9.196   101.064 1.00 69.96 ? 434 TYR   A O   1 
ATOM   2836 C  CB  . TYR   A 1 406 ? -10.463 8.217   98.723  1.00 62.59 ? 434 TYR   A CB  1 
ATOM   2837 C  CG  . TYR   A 1 406 ? -11.540 8.858   97.888  1.00 63.10 ? 434 TYR   A CG  1 
ATOM   2838 C  CD1 . TYR   A 1 406 ? -11.337 10.096  97.293  1.00 60.77 ? 434 TYR   A CD1 1 
ATOM   2839 C  CD2 . TYR   A 1 406 ? -12.768 8.232   97.701  1.00 62.79 ? 434 TYR   A CD2 1 
ATOM   2840 C  CE1 . TYR   A 1 406 ? -12.316 10.687  96.533  1.00 57.15 ? 434 TYR   A CE1 1 
ATOM   2841 C  CE2 . TYR   A 1 406 ? -13.758 8.821   96.936  1.00 65.20 ? 434 TYR   A CE2 1 
ATOM   2842 C  CZ  . TYR   A 1 406 ? -13.521 10.049  96.353  1.00 59.00 ? 434 TYR   A CZ  1 
ATOM   2843 O  OH  . TYR   A 1 406 ? -14.488 10.649  95.587  1.00 65.54 ? 434 TYR   A OH  1 
ATOM   2844 N  N   . GLU   A 1 407 ? -12.047 7.018   101.083 1.00 64.97 ? 435 GLU   A N   1 
ATOM   2845 C  CA  . GLU   A 1 407 ? -13.208 6.567   101.843 1.00 67.03 ? 435 GLU   A CA  1 
ATOM   2846 C  C   . GLU   A 1 407 ? -13.441 7.473   103.048 1.00 69.01 ? 435 GLU   A C   1 
ATOM   2847 O  O   . GLU   A 1 407 ? -14.522 8.053   103.211 1.00 70.96 ? 435 GLU   A O   1 
ATOM   2848 C  CB  . GLU   A 1 407 ? -13.013 5.109   102.279 1.00 53.84 ? 435 GLU   A CB  1 
ATOM   2849 N  N   . LYS   A 1 408 ? -12.411 7.629   103.876 1.00 64.49 ? 436 LYS   A N   1 
ATOM   2850 C  CA  . LYS   A 1 408 ? -12.382 8.646   104.916 1.00 64.48 ? 436 LYS   A CA  1 
ATOM   2851 C  C   . LYS   A 1 408 ? -13.540 8.478   105.895 1.00 58.02 ? 436 LYS   A C   1 
ATOM   2852 O  O   . LYS   A 1 408 ? -14.593 9.090   105.729 1.00 60.83 ? 436 LYS   A O   1 
ATOM   2853 C  CB  . LYS   A 1 408 ? -12.402 10.046  104.285 1.00 58.68 ? 436 LYS   A CB  1 
HETATM 2854 C  C10 . A1LWP B 2 .   ? 3.268   -5.383  86.929  1.00 34.75 ? 501 A1LWP A C10 1 
HETATM 2855 C  C13 . A1LWP B 2 .   ? 6.016   -5.619  85.817  1.00 27.48 ? 501 A1LWP A C13 1 
HETATM 2856 C  C21 . A1LWP B 2 .   ? -2.177  -3.335  86.028  1.00 28.26 ? 501 A1LWP A C21 1 
HETATM 2857 C  C22 . A1LWP B 2 .   ? -3.388  -4.221  86.291  1.00 33.51 ? 501 A1LWP A C22 1 
HETATM 2858 C  C24 . A1LWP B 2 .   ? -5.710  -4.908  85.850  1.00 45.69 ? 501 A1LWP A C24 1 
HETATM 2859 C  C01 . A1LWP B 2 .   ? 1.847   -2.541  86.763  1.00 35.13 ? 501 A1LWP A C01 1 
HETATM 2860 C  C02 . A1LWP B 2 .   ? 2.313   -1.803  87.839  1.00 34.53 ? 501 A1LWP A C02 1 
HETATM 2861 C  C03 . A1LWP B 2 .   ? 1.359   -1.224  88.667  1.00 40.69 ? 501 A1LWP A C03 1 
HETATM 2862 C  C04 . A1LWP B 2 .   ? 0.002   -1.403  88.391  1.00 39.86 ? 501 A1LWP A C04 1 
HETATM 2863 C  C05 . A1LWP B 2 .   ? -0.462  -2.149  87.305  1.00 34.06 ? 501 A1LWP A C05 1 
HETATM 2864 C  C06 . A1LWP B 2 .   ? 0.500   -2.724  86.491  1.00 33.45 ? 501 A1LWP A C06 1 
HETATM 2865 C  C07 . A1LWP B 2 .   ? 2.840   -3.187  85.798  1.00 34.07 ? 501 A1LWP A C07 1 
HETATM 2866 C  C08 . A1LWP B 2 .   ? 3.703   -4.404  86.148  1.00 35.24 ? 501 A1LWP A C08 1 
HETATM 2867 C  C11 . A1LWP B 2 .   ? 4.214   -6.541  87.245  1.00 35.23 ? 501 A1LWP A C11 1 
HETATM 2868 C  C12 . A1LWP B 2 .   ? 5.658   -6.070  87.218  1.00 28.70 ? 501 A1LWP A C12 1 
HETATM 2869 C  C14 . A1LWP B 2 .   ? 4.946   -4.675  85.287  1.00 28.91 ? 501 A1LWP A C14 1 
HETATM 2870 C  C18 . A1LWP B 2 .   ? -2.710  -0.348  88.598  1.00 41.29 ? 501 A1LWP A C18 1 
HETATM 2871 C  C19 . A1LWP B 2 .   ? -2.965  -1.460  87.586  1.00 36.85 ? 501 A1LWP A C19 1 
HETATM 2872 C  C23 . A1LWP B 2 .   ? -4.490  -4.028  85.589  1.00 35.99 ? 501 A1LWP A C23 1 
HETATM 2873 C  C25 . A1LWP B 2 .   ? -4.556  -2.928  84.525  1.00 27.65 ? 501 A1LWP A C25 1 
HETATM 2874 N  N20 . A1LWP B 2 .   ? -1.897  -2.296  87.022  1.00 35.41 ? 501 A1LWP A N20 1 
HETATM 2875 O  O09 . A1LWP B 2 .   ? 2.947   -2.694  84.718  1.00 32.64 ? 501 A1LWP A O09 1 
HETATM 2876 O  O15 . A1LWP B 2 .   ? 2.203   -5.184  87.818  1.00 39.59 ? 501 A1LWP A O15 1 
HETATM 2877 O  O16 . A1LWP B 2 .   ? 5.088   -4.166  84.221  1.00 27.28 ? 501 A1LWP A O16 1 
HETATM 2878 O  O26 . A1LWP B 2 .   ? -4.103  -1.623  87.287  1.00 36.07 ? 501 A1LWP A O26 1 
HETATM 2879 S  S17 . A1LWP B 2 .   ? -1.173  -0.607  89.515  1.00 42.95 ? 501 A1LWP A S17 1 
HETATM 2880 CO CO  . CO    C 3 .   ? 4.042   -2.628  83.029  1.00 34.23 ? 502 CO    A CO  1 
HETATM 2881 O  O   . HOH   D 4 .   ? -12.150 -20.963 72.471  1.00 28.59 ? 601 HOH   A O   1 
HETATM 2882 O  O   . HOH   D 4 .   ? 1.090   -18.638 92.732  1.00 42.26 ? 602 HOH   A O   1 
HETATM 2883 O  O   . HOH   D 4 .   ? -4.472  4.817   60.097  1.00 39.14 ? 603 HOH   A O   1 
HETATM 2884 O  O   . HOH   D 4 .   ? -1.291  -9.617  98.595  1.00 57.96 ? 604 HOH   A O   1 
HETATM 2885 O  O   . HOH   D 4 .   ? -0.244  7.988   97.889  1.00 45.35 ? 605 HOH   A O   1 
HETATM 2886 O  O   . HOH   D 4 .   ? 5.343   8.663   59.631  1.00 33.49 ? 606 HOH   A O   1 
HETATM 2887 O  O   . HOH   D 4 .   ? 19.334  -5.350  74.811  1.00 22.85 ? 607 HOH   A O   1 
HETATM 2888 O  O   . HOH   D 4 .   ? 1.317   14.132  67.282  1.00 37.41 ? 608 HOH   A O   1 
HETATM 2889 O  O   . HOH   D 4 .   ? 20.652  -2.436  63.493  1.00 43.57 ? 609 HOH   A O   1 
HETATM 2890 O  O   . HOH   D 4 .   ? -3.526  -20.651 88.403  1.00 25.18 ? 610 HOH   A O   1 
HETATM 2891 O  O   . HOH   D 4 .   ? -9.600  12.043  82.569  1.00 37.84 ? 611 HOH   A O   1 
HETATM 2892 O  O   . HOH   D 4 .   ? -9.674  6.320   83.494  1.00 41.75 ? 612 HOH   A O   1 
HETATM 2893 O  O   . HOH   D 4 .   ? 26.841  -11.419 77.886  1.00 28.05 ? 613 HOH   A O   1 
HETATM 2894 O  O   . HOH   D 4 .   ? 23.615  -3.221  58.699  1.00 35.86 ? 614 HOH   A O   1 
HETATM 2895 O  O   . HOH   D 4 .   ? -13.322 -14.619 72.937  1.00 23.88 ? 615 HOH   A O   1 
HETATM 2896 O  O   . HOH   D 4 .   ? 22.556  -12.529 67.227  1.00 21.99 ? 616 HOH   A O   1 
HETATM 2897 O  O   . HOH   D 4 .   ? 10.714  7.264   79.308  1.00 28.96 ? 617 HOH   A O   1 
HETATM 2898 O  O   . HOH   D 4 .   ? 20.240  -7.703  63.277  1.00 26.54 ? 618 HOH   A O   1 
HETATM 2899 O  O   . HOH   D 4 .   ? 13.300  -3.170  59.545  1.00 39.90 ? 619 HOH   A O   1 
HETATM 2900 O  O   . HOH   D 4 .   ? 4.653   16.597  72.619  1.00 29.83 ? 620 HOH   A O   1 
HETATM 2901 O  O   . HOH   D 4 .   ? 10.036  -20.822 49.167  1.00 26.04 ? 621 HOH   A O   1 
HETATM 2902 O  O   . HOH   D 4 .   ? 7.422   -11.066 79.345  1.00 19.88 ? 622 HOH   A O   1 
HETATM 2903 O  O   . HOH   D 4 .   ? -6.083  6.609   52.344  1.00 48.85 ? 623 HOH   A O   1 
HETATM 2904 O  O   . HOH   D 4 .   ? 17.193  -5.218  90.970  1.00 35.40 ? 624 HOH   A O   1 
HETATM 2905 O  O   . HOH   D 4 .   ? 8.364   1.326   90.191  1.00 31.42 ? 625 HOH   A O   1 
HETATM 2906 O  O   . HOH   D 4 .   ? 21.966  -10.791 80.499  1.00 27.52 ? 626 HOH   A O   1 
HETATM 2907 O  O   . HOH   D 4 .   ? 22.460  9.795   85.231  1.00 39.03 ? 627 HOH   A O   1 
HETATM 2908 O  O   . HOH   D 4 .   ? -10.291 -21.232 81.228  1.00 23.06 ? 628 HOH   A O   1 
HETATM 2909 O  O   . HOH   D 4 .   ? 2.427   -23.900 71.623  1.00 29.77 ? 629 HOH   A O   1 
HETATM 2910 O  O   . HOH   D 4 .   ? -3.572  17.970  79.643  1.00 33.93 ? 630 HOH   A O   1 
HETATM 2911 O  O   . HOH   D 4 .   ? 12.446  -0.673  72.922  1.00 22.54 ? 631 HOH   A O   1 
HETATM 2912 O  O   . HOH   D 4 .   ? -9.282  11.093  90.142  1.00 40.87 ? 632 HOH   A O   1 
HETATM 2913 O  O   . HOH   D 4 .   ? 1.875   -21.724 51.705  1.00 17.65 ? 633 HOH   A O   1 
HETATM 2914 O  O   . HOH   D 4 .   ? -13.830 9.527   73.707  1.00 25.02 ? 634 HOH   A O   1 
HETATM 2915 O  O   . HOH   D 4 .   ? -15.283 3.689   71.194  1.00 15.40 ? 635 HOH   A O   1 
HETATM 2916 O  O   . HOH   D 4 .   ? 16.087  -27.300 73.140  1.00 25.38 ? 636 HOH   A O   1 
HETATM 2917 O  O   . HOH   D 4 .   ? 15.230  -4.170  90.197  1.00 29.61 ? 637 HOH   A O   1 
HETATM 2918 O  O   . HOH   D 4 .   ? 2.503   -14.473 60.744  1.00 18.39 ? 638 HOH   A O   1 
HETATM 2919 O  O   . HOH   D 4 .   ? 14.191  5.509   77.496  1.00 34.83 ? 639 HOH   A O   1 
HETATM 2920 O  O   . HOH   D 4 .   ? -11.659 -2.413  73.722  1.00 15.22 ? 640 HOH   A O   1 
HETATM 2921 O  O   . HOH   D 4 .   ? 9.136   -3.518  54.413  1.00 33.93 ? 641 HOH   A O   1 
HETATM 2922 O  O   . HOH   D 4 .   ? 3.553   -10.602 50.132  1.00 25.22 ? 642 HOH   A O   1 
HETATM 2923 O  O   . HOH   D 4 .   ? 12.860  -1.214  77.016  1.00 21.17 ? 643 HOH   A O   1 
HETATM 2924 O  O   . HOH   D 4 .   ? 20.427  -26.059 69.760  1.00 32.37 ? 644 HOH   A O   1 
HETATM 2925 O  O   . HOH   D 4 .   ? 5.523   -0.499  83.842  1.00 27.87 ? 645 HOH   A O   1 
HETATM 2926 O  O   . HOH   D 4 .   ? 11.190  -19.015 60.960  1.00 19.19 ? 646 HOH   A O   1 
HETATM 2927 O  O   . HOH   D 4 .   ? -7.927  13.206  64.508  1.00 37.07 ? 647 HOH   A O   1 
HETATM 2928 O  O   . HOH   D 4 .   ? 14.070  -2.883  72.983  1.00 23.71 ? 648 HOH   A O   1 
HETATM 2929 O  O   . HOH   D 4 .   ? 2.998   7.782   64.371  1.00 26.22 ? 649 HOH   A O   1 
HETATM 2930 O  O   . HOH   D 4 .   ? 9.292   -12.737 53.124  1.00 23.67 ? 650 HOH   A O   1 
HETATM 2931 O  O   . HOH   D 4 .   ? -4.545  -19.587 51.927  1.00 18.25 ? 651 HOH   A O   1 
HETATM 2932 O  O   . HOH   D 4 .   ? 19.283  -0.172  82.684  1.00 24.05 ? 652 HOH   A O   1 
HETATM 2933 O  O   . HOH   D 4 .   ? -6.549  -8.622  52.624  1.00 12.51 ? 653 HOH   A O   1 
HETATM 2934 O  O   . HOH   D 4 .   ? -7.393  -12.473 74.488  1.00 20.87 ? 654 HOH   A O   1 
HETATM 2935 O  O   . HOH   D 4 .   ? 11.305  9.307   78.730  1.00 47.86 ? 655 HOH   A O   1 
HETATM 2936 O  O   . HOH   D 4 .   ? 4.385   -21.451 84.470  1.00 26.84 ? 656 HOH   A O   1 
HETATM 2937 O  O   . HOH   D 4 .   ? -7.140  -16.490 62.738  1.00 22.12 ? 657 HOH   A O   1 
HETATM 2938 O  O   . HOH   D 4 .   ? 9.900   -0.722  69.971  1.00 21.05 ? 658 HOH   A O   1 
HETATM 2939 O  O   . HOH   D 4 .   ? 28.084  -12.959 83.845  1.00 31.90 ? 659 HOH   A O   1 
HETATM 2940 O  O   . HOH   D 4 .   ? 4.776   -20.909 72.564  1.00 21.97 ? 660 HOH   A O   1 
HETATM 2941 O  O   . HOH   D 4 .   ? 16.224  -20.141 54.650  1.00 30.74 ? 661 HOH   A O   1 
HETATM 2942 O  O   . HOH   D 4 .   ? -0.739  -22.663 56.640  1.00 34.93 ? 662 HOH   A O   1 
HETATM 2943 O  O   . HOH   D 4 .   ? 21.821  -4.616  60.843  1.00 33.92 ? 663 HOH   A O   1 
HETATM 2944 O  O   . HOH   D 4 .   ? -9.994  10.659  84.368  1.00 34.82 ? 664 HOH   A O   1 
HETATM 2945 O  O   . HOH   D 4 .   ? 3.945   -16.772 62.207  1.00 17.72 ? 665 HOH   A O   1 
HETATM 2946 O  O   . HOH   D 4 .   ? -1.172  -19.773 45.263  1.00 30.05 ? 666 HOH   A O   1 
HETATM 2947 O  O   . HOH   D 4 .   ? -9.618  -12.850 57.995  1.00 21.13 ? 667 HOH   A O   1 
HETATM 2948 O  O   . HOH   D 4 .   ? 8.509   -22.254 59.424  1.00 28.31 ? 668 HOH   A O   1 
HETATM 2949 O  O   . HOH   D 4 .   ? -12.172 -16.806 70.529  1.00 24.22 ? 669 HOH   A O   1 
HETATM 2950 O  O   . HOH   D 4 .   ? 7.073   -15.996 50.034  1.00 25.68 ? 670 HOH   A O   1 
HETATM 2951 O  O   . HOH   D 4 .   ? 23.838  -6.551  60.346  1.00 43.56 ? 671 HOH   A O   1 
HETATM 2952 O  O   . HOH   D 4 .   ? -4.044  -10.168 84.118  1.00 21.61 ? 672 HOH   A O   1 
HETATM 2953 O  O   . HOH   D 4 .   ? -8.914  -0.140  75.924  1.00 18.07 ? 673 HOH   A O   1 
HETATM 2954 O  O   . HOH   D 4 .   ? -8.416  -25.130 76.340  1.00 53.47 ? 674 HOH   A O   1 
HETATM 2955 O  O   . HOH   D 4 .   ? -5.604  -8.591  92.896  1.00 36.41 ? 675 HOH   A O   1 
HETATM 2956 O  O   . HOH   D 4 .   ? 22.782  -8.691  74.199  1.00 23.95 ? 676 HOH   A O   1 
HETATM 2957 O  O   . HOH   D 4 .   ? 4.417   -17.890 64.444  1.00 21.51 ? 677 HOH   A O   1 
HETATM 2958 O  O   . HOH   D 4 .   ? -10.894 -11.834 70.834  1.00 14.70 ? 678 HOH   A O   1 
HETATM 2959 O  O   . HOH   D 4 .   ? 13.087  0.859   78.788  1.00 25.11 ? 679 HOH   A O   1 
HETATM 2960 O  O   . HOH   D 4 .   ? -0.592  -13.932 73.960  1.00 7.79  ? 680 HOH   A O   1 
HETATM 2961 O  O   . HOH   D 4 .   ? 25.184  -21.629 78.370  1.00 26.95 ? 681 HOH   A O   1 
HETATM 2962 O  O   . HOH   D 4 .   ? -8.495  3.616   90.497  1.00 39.16 ? 682 HOH   A O   1 
HETATM 2963 O  O   . HOH   D 4 .   ? 20.889  -18.379 82.524  1.00 27.58 ? 683 HOH   A O   1 
HETATM 2964 O  O   . HOH   D 4 .   ? 4.928   -22.844 58.697  1.00 29.00 ? 684 HOH   A O   1 
HETATM 2965 O  O   . HOH   D 4 .   ? 4.660   -27.842 52.701  1.00 24.43 ? 685 HOH   A O   1 
HETATM 2966 O  O   . HOH   D 4 .   ? 1.152   7.525   68.600  1.00 14.82 ? 686 HOH   A O   1 
HETATM 2967 O  O   . HOH   D 4 .   ? -13.937 13.509  72.100  1.00 24.48 ? 687 HOH   A O   1 
HETATM 2968 O  O   . HOH   D 4 .   ? -0.902  -22.077 80.607  1.00 17.25 ? 688 HOH   A O   1 
HETATM 2969 O  O   . HOH   D 4 .   ? -7.933  5.876   71.840  1.00 16.56 ? 689 HOH   A O   1 
HETATM 2970 O  O   . HOH   D 4 .   ? -10.871 8.077   77.922  1.00 23.97 ? 690 HOH   A O   1 
HETATM 2971 O  O   . HOH   D 4 .   ? -0.754  -18.039 74.549  1.00 12.70 ? 691 HOH   A O   1 
HETATM 2972 O  O   . HOH   D 4 .   ? -13.763 -14.020 78.044  1.00 16.05 ? 692 HOH   A O   1 
HETATM 2973 O  O   . HOH   D 4 .   ? 27.387  -14.792 63.175  1.00 28.96 ? 693 HOH   A O   1 
HETATM 2974 O  O   . HOH   D 4 .   ? 8.705   -2.512  67.892  1.00 19.52 ? 694 HOH   A O   1 
HETATM 2975 O  O   . HOH   D 4 .   ? -6.017  -8.429  82.422  1.00 21.06 ? 695 HOH   A O   1 
HETATM 2976 O  O   . HOH   D 4 .   ? 10.399  2.717   51.484  1.00 46.16 ? 696 HOH   A O   1 
HETATM 2977 O  O   . HOH   D 4 .   ? -1.358  -7.807  99.948  1.00 43.89 ? 697 HOH   A O   1 
HETATM 2978 O  O   . HOH   D 4 .   ? -11.596 -0.214  75.018  1.00 17.88 ? 698 HOH   A O   1 
HETATM 2979 O  O   . HOH   D 4 .   ? -3.116  -0.568  50.638  1.00 33.59 ? 699 HOH   A O   1 
HETATM 2980 O  O   . HOH   D 4 .   ? 25.429  -21.253 75.776  1.00 27.22 ? 700 HOH   A O   1 
HETATM 2981 O  O   . HOH   D 4 .   ? -8.515  -24.081 69.414  1.00 30.91 ? 701 HOH   A O   1 
HETATM 2982 O  O   . HOH   D 4 .   ? 19.191  -6.804  55.385  1.00 37.42 ? 702 HOH   A O   1 
HETATM 2983 O  O   . HOH   D 4 .   ? 0.710   -6.466  85.718  1.00 31.08 ? 703 HOH   A O   1 
HETATM 2984 O  O   . HOH   D 4 .   ? 25.706  -8.142  74.354  1.00 23.97 ? 704 HOH   A O   1 
HETATM 2985 O  O   . HOH   D 4 .   ? -6.548  -14.716 94.269  1.00 43.11 ? 705 HOH   A O   1 
HETATM 2986 O  O   . HOH   D 4 .   ? -2.208  5.433   58.289  1.00 26.41 ? 706 HOH   A O   1 
HETATM 2987 O  O   . HOH   D 4 .   ? -2.009  -11.465 74.310  1.00 14.61 ? 707 HOH   A O   1 
HETATM 2988 O  O   . HOH   D 4 .   ? 4.807   11.938  56.821  1.00 28.76 ? 708 HOH   A O   1 
HETATM 2989 O  O   . HOH   D 4 .   ? -11.833 5.657   79.240  1.00 24.84 ? 709 HOH   A O   1 
HETATM 2990 O  O   . HOH   D 4 .   ? -8.672  -9.312  72.279  1.00 41.13 ? 710 HOH   A O   1 
HETATM 2991 O  O   . HOH   D 4 .   ? 26.499  -18.610 74.169  1.00 26.64 ? 711 HOH   A O   1 
HETATM 2992 O  O   . HOH   D 4 .   ? -4.751  -12.578 74.711  1.00 17.92 ? 712 HOH   A O   1 
HETATM 2993 O  O   . HOH   D 4 .   ? 9.123   -17.129 60.397  1.00 19.71 ? 713 HOH   A O   1 
HETATM 2994 O  O   . HOH   D 4 .   ? -10.103 -10.910 73.285  1.00 19.14 ? 714 HOH   A O   1 
HETATM 2995 O  O   . HOH   D 4 .   ? -9.357  -21.859 88.873  1.00 34.70 ? 715 HOH   A O   1 
HETATM 2996 O  O   . HOH   D 4 .   ? -11.771 10.462  79.680  1.00 31.98 ? 716 HOH   A O   1 
HETATM 2997 O  O   . HOH   D 4 .   ? 3.830   -23.172 67.250  1.00 38.68 ? 717 HOH   A O   1 
HETATM 2998 O  O   . HOH   D 4 .   ? 26.430  -13.219 69.996  1.00 25.93 ? 718 HOH   A O   1 
HETATM 2999 O  O   . HOH   D 4 .   ? -13.006 -16.302 77.285  1.00 17.51 ? 719 HOH   A O   1 
HETATM 3000 O  O   . HOH   D 4 .   ? -4.332  3.051   84.934  1.00 20.91 ? 720 HOH   A O   1 
HETATM 3001 O  O   . HOH   D 4 .   ? 11.253  -6.426  89.899  1.00 40.08 ? 721 HOH   A O   1 
HETATM 3002 O  O   . HOH   D 4 .   ? 14.015  1.208   69.621  1.00 24.50 ? 722 HOH   A O   1 
HETATM 3003 O  O   . HOH   D 4 .   ? 14.796  -8.015  50.685  1.00 41.41 ? 723 HOH   A O   1 
HETATM 3004 O  O   . HOH   D 4 .   ? -13.433 -16.247 85.206  1.00 26.74 ? 724 HOH   A O   1 
HETATM 3005 O  O   . HOH   D 4 .   ? 16.021  -23.414 79.637  1.00 23.55 ? 725 HOH   A O   1 
HETATM 3006 O  O   . HOH   D 4 .   ? 7.231   -22.873 61.146  1.00 42.21 ? 726 HOH   A O   1 
HETATM 3007 O  O   . HOH   D 4 .   ? -10.350 -10.271 64.798  1.00 5.95  ? 727 HOH   A O   1 
HETATM 3008 O  O   . HOH   D 4 .   ? 12.712  -0.897  70.498  1.00 17.85 ? 728 HOH   A O   1 
HETATM 3009 O  O   . HOH   D 4 .   ? -5.854  5.163   85.843  1.00 30.00 ? 729 HOH   A O   1 
HETATM 3010 O  O   . HOH   D 4 .   ? -0.403  -0.674  101.033 1.00 37.67 ? 730 HOH   A O   1 
HETATM 3011 O  O   . HOH   D 4 .   ? -2.485  -15.881 74.395  1.00 11.56 ? 731 HOH   A O   1 
HETATM 3012 O  O   . HOH   D 4 .   ? -5.574  2.897   55.519  1.00 30.62 ? 732 HOH   A O   1 
HETATM 3013 O  O   . HOH   D 4 .   ? 16.438  -16.098 49.713  1.00 31.76 ? 733 HOH   A O   1 
HETATM 3014 O  O   . HOH   D 4 .   ? -4.289  -14.151 72.590  1.00 23.04 ? 734 HOH   A O   1 
HETATM 3015 O  O   . HOH   D 4 .   ? -3.275  -23.527 70.087  1.00 29.27 ? 735 HOH   A O   1 
HETATM 3016 O  O   . HOH   D 4 .   ? 21.985  -6.007  75.117  1.00 23.34 ? 736 HOH   A O   1 
HETATM 3017 O  O   . HOH   D 4 .   ? -5.680  -23.035 80.435  1.00 28.93 ? 737 HOH   A O   1 
HETATM 3018 O  O   . HOH   D 4 .   ? 6.681   -19.908 91.880  1.00 41.55 ? 738 HOH   A O   1 
HETATM 3019 O  O   . HOH   D 4 .   ? 5.940   -28.035 70.334  1.00 28.08 ? 739 HOH   A O   1 
HETATM 3020 O  O   . HOH   D 4 .   ? 2.306   -20.655 92.007  1.00 35.46 ? 740 HOH   A O   1 
HETATM 3021 O  O   . HOH   D 4 .   ? 11.992  13.934  97.090  1.00 39.05 ? 741 HOH   A O   1 
HETATM 3022 O  O   . HOH   D 4 .   ? -1.797  -5.896  42.580  1.00 37.07 ? 742 HOH   A O   1 
HETATM 3023 O  O   . HOH   D 4 .   ? -4.934  -4.382  49.784  1.00 26.80 ? 743 HOH   A O   1 
HETATM 3024 O  O   . HOH   D 4 .   ? -5.960  -1.775  56.551  1.00 18.75 ? 744 HOH   A O   1 
HETATM 3025 O  O   . HOH   D 4 .   ? -2.298  12.467  64.491  1.00 26.96 ? 745 HOH   A O   1 
HETATM 3026 O  O   . HOH   D 4 .   ? 11.802  -13.596 50.460  1.00 41.46 ? 746 HOH   A O   1 
HETATM 3027 O  O   . HOH   D 4 .   ? -16.287 4.466   75.030  1.00 30.41 ? 747 HOH   A O   1 
HETATM 3028 O  O   . HOH   D 4 .   ? -5.430  2.555   53.287  1.00 44.73 ? 748 HOH   A O   1 
HETATM 3029 O  O   . HOH   D 4 .   ? 4.845   -12.757 48.939  1.00 28.72 ? 749 HOH   A O   1 
HETATM 3030 O  O   . HOH   D 4 .   ? 3.668   -7.916  94.346  1.00 41.36 ? 750 HOH   A O   1 
HETATM 3031 O  O   . HOH   D 4 .   ? 0.562   14.354  64.532  1.00 23.59 ? 751 HOH   A O   1 
HETATM 3032 O  O   . HOH   D 4 .   ? -14.313 -17.576 86.878  1.00 29.14 ? 752 HOH   A O   1 
HETATM 3033 O  O   . HOH   D 4 .   ? 8.203   -2.228  49.297  1.00 32.72 ? 753 HOH   A O   1 
HETATM 3034 O  O   . HOH   D 4 .   ? 9.637   -24.140 58.023  1.00 32.53 ? 754 HOH   A O   1 
HETATM 3035 O  O   . HOH   D 4 .   ? 8.451   17.074  97.677  1.00 33.30 ? 755 HOH   A O   1 
HETATM 3036 O  O   . HOH   D 4 .   ? 15.425  -2.315  62.206  1.00 47.51 ? 756 HOH   A O   1 
HETATM 3037 O  O   . HOH   D 4 .   ? 10.201  14.566  98.804  1.00 35.71 ? 757 HOH   A O   1 
HETATM 3038 O  O   . HOH   D 4 .   ? 1.010   -5.254  97.238  1.00 44.14 ? 758 HOH   A O   1 
HETATM 3039 O  O   . HOH   D 4 .   ? 5.400   6.462   61.600  1.00 33.12 ? 759 HOH   A O   1 
HETATM 3040 O  O   . HOH   D 4 .   ? 4.313   -21.933 70.191  1.00 31.17 ? 760 HOH   A O   1 
HETATM 3041 O  O   . HOH   D 4 .   ? 13.376  6.069   72.455  1.00 41.50 ? 761 HOH   A O   1 
HETATM 3042 O  O   . HOH   D 4 .   ? 4.915   12.203  59.537  1.00 29.06 ? 762 HOH   A O   1 
HETATM 3043 O  O   . HOH   D 4 .   ? -1.655  13.883  62.918  1.00 34.66 ? 763 HOH   A O   1 
HETATM 3044 O  O   . HOH   D 4 .   ? 13.385  -5.597  51.804  1.00 33.96 ? 764 HOH   A O   1 
HETATM 3045 O  O   . HOH   D 4 .   ? 26.094  -15.116 46.811  1.00 35.85 ? 765 HOH   A O   1 
HETATM 3046 O  O   . HOH   D 4 .   ? 13.084  6.879   74.916  1.00 32.04 ? 766 HOH   A O   1 
HETATM 3047 O  O   . HOH   D 4 .   ? -4.991  -0.365  58.505  1.00 20.16 ? 767 HOH   A O   1 
HETATM 3048 O  O   . HOH   D 4 .   ? -10.068 -16.928 60.718  1.00 21.93 ? 768 HOH   A O   1 
HETATM 3049 O  O   . HOH   D 4 .   ? 18.311  -20.700 55.535  1.00 30.75 ? 769 HOH   A O   1 
HETATM 3050 O  O   . HOH   D 4 .   ? -5.996  13.199  63.044  1.00 33.56 ? 770 HOH   A O   1 
HETATM 3051 O  O   . HOH   D 4 .   ? 1.409   -27.690 71.639  1.00 34.06 ? 771 HOH   A O   1 
HETATM 3052 O  O   . HOH   D 4 .   ? -17.588 2.656   70.626  1.00 19.58 ? 772 HOH   A O   1 
HETATM 3053 O  O   . HOH   D 4 .   ? -4.438  -24.881 79.023  1.00 26.67 ? 773 HOH   A O   1 
HETATM 3054 O  O   . HOH   D 4 .   ? -2.721  6.240   104.070 1.00 36.77 ? 774 HOH   A O   1 
HETATM 3055 O  O   . HOH   D 4 .   ? 19.850  -0.266  63.386  1.00 46.27 ? 775 HOH   A O   1 
HETATM 3056 O  O   . HOH   D 4 .   ? 10.735  -1.953  50.296  1.00 41.77 ? 776 HOH   A O   1 
HETATM 3057 O  O   . HOH   D 4 .   ? -2.176  -22.395 82.544  1.00 25.60 ? 777 HOH   A O   1 
HETATM 3058 O  O   . HOH   D 4 .   ? 20.376  -21.389 56.269  1.00 31.31 ? 778 HOH   A O   1 
HETATM 3059 O  O   . HOH   D 4 .   ? -7.164  -6.388  82.539  1.00 26.05 ? 779 HOH   A O   1 
HETATM 3060 O  O   . HOH   D 4 .   ? -12.416 -9.618  88.669  1.00 33.92 ? 780 HOH   A O   1 
HETATM 3061 O  O   . HOH   D 4 .   ? 7.785   -24.239 81.474  1.00 31.16 ? 781 HOH   A O   1 
HETATM 3062 O  O   . HOH   D 4 .   ? 9.682   -14.452 51.292  1.00 29.61 ? 782 HOH   A O   1 
HETATM 3063 O  O   . HOH   D 4 .   ? -0.918  8.063   103.159 1.00 43.56 ? 783 HOH   A O   1 
HETATM 3064 O  O   . HOH   D 4 .   ? 27.450  -2.665  70.639  1.00 37.65 ? 784 HOH   A O   1 
HETATM 3065 O  O   . HOH   D 4 .   ? 6.938   -29.450 71.917  1.00 35.40 ? 785 HOH   A O   1 
HETATM 3066 O  O   . HOH   D 4 .   ? 6.616   -22.103 80.209  1.00 40.20 ? 786 HOH   A O   1 
HETATM 3067 O  O   . HOH   D 4 .   ? 10.532  1.001   49.919  1.00 46.20 ? 787 HOH   A O   1 
HETATM 3068 O  O   . HOH   D 4 .   ? 14.761  -25.304 80.551  1.00 25.83 ? 788 HOH   A O   1 
HETATM 3069 O  O   . HOH   D 4 .   ? 17.314  -1.040  61.597  1.00 43.10 ? 789 HOH   A O   1 
HETATM 3070 O  O   . HOH   D 4 .   ? 3.292   -5.876  95.385  1.00 42.64 ? 790 HOH   A O   1 
HETATM 3071 O  O   . HOH   D 4 .   ? -13.227 -11.052 90.203  1.00 32.37 ? 791 HOH   A O   1 
HETATM 3072 O  O   . HOH   D 4 .   ? 10.523  18.694  98.298  1.00 27.38 ? 792 HOH   A O   1 
HETATM 3073 O  O   . HOH   D 4 .   ? 6.719   -23.614 76.458  1.00 30.85 ? 793 HOH   A O   1 
HETATM 3074 O  O   . HOH   D 4 .   ? 4.897   -27.754 67.597  1.00 27.84 ? 794 HOH   A O   1 
HETATM 3075 O  O   . HOH   D 4 .   ? 7.223   -24.418 78.726  1.00 31.83 ? 795 HOH   A O   1 
HETATM 3076 O  O   . HOH   D 4 .   ? -12.928 -24.312 88.362  1.00 42.22 ? 796 HOH   A O   1 
HETATM 3077 O  O   . HOH   D 4 .   ? 0.112   -28.958 73.957  1.00 23.77 ? 797 HOH   A O   1 
HETATM 3078 O  O   . HOH   D 4 .   ? -15.964 -10.597 90.982  1.00 32.78 ? 798 HOH   A O   1 
HETATM 3079 O  O   . HOH   D 4 .   ? -11.250 -26.432 87.093  1.00 43.08 ? 799 HOH   A O   1 
HETATM 3080 O  O   . HOH   D 4 .   ? -14.411 -25.737 87.520  1.00 37.85 ? 800 HOH   A O   1 
HETATM 3081 O  O   . HOH   D 4 .   ? -16.891 -8.672  89.234  1.00 28.94 ? 801 HOH   A O   1 
# 
