data_8XUE
# 
_entry.id   8XUE 
# 
_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   8XUE         pdb_00008xue 10.2210/pdb8xue/pdb 
WWPDB D_1300044223 ?            ?                   
# 
_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                        8XUE 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           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-Y191497 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 'COBALT (II) ION' 58.933    1  ?          ? ? ? 
3 non-polymer syn 
'3-(4-chlorophenyl)-1-methyl-6-nitro-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-quinazoline-2,4-dione' 469.831   1  ? 
? ? ? 
4 water       nat water 18.015    74 ?          ? ? ? 
# 
_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 'COBALT (II) ION'                                                                                                  CO    
3 '3-(4-chlorophenyl)-1-methyl-6-nitro-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-quinazoline-2,4-dione' A1LW6 
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 
A1LW6 non-polymer         . 
'3-(4-chlorophenyl)-1-methyl-6-nitro-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-quinazoline-2,4-dione' ? 
'C22 H16 Cl N3 O7' 469.831 
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 CO    1  501 1  CO    CO  A . 
C 3 A1LW6 1  502 1  A1LW6 LIG A . 
D 4 HOH   1  601 24 HOH   HOH A . 
D 4 HOH   2  602 12 HOH   HOH A . 
D 4 HOH   3  603 61 HOH   HOH A . 
D 4 HOH   4  604 19 HOH   HOH A . 
D 4 HOH   5  605 70 HOH   HOH A . 
D 4 HOH   6  606 41 HOH   HOH A . 
D 4 HOH   7  607 7  HOH   HOH A . 
D 4 HOH   8  608 29 HOH   HOH A . 
D 4 HOH   9  609 15 HOH   HOH A . 
D 4 HOH   10 610 43 HOH   HOH A . 
D 4 HOH   11 611 71 HOH   HOH A . 
D 4 HOH   12 612 20 HOH   HOH A . 
D 4 HOH   13 613 2  HOH   HOH A . 
D 4 HOH   14 614 39 HOH   HOH A . 
D 4 HOH   15 615 3  HOH   HOH A . 
D 4 HOH   16 616 34 HOH   HOH A . 
D 4 HOH   17 617 17 HOH   HOH A . 
D 4 HOH   18 618 52 HOH   HOH A . 
D 4 HOH   19 619 69 HOH   HOH A . 
D 4 HOH   20 620 53 HOH   HOH A . 
D 4 HOH   21 621 37 HOH   HOH A . 
D 4 HOH   22 622 13 HOH   HOH A . 
D 4 HOH   23 623 4  HOH   HOH A . 
D 4 HOH   24 624 8  HOH   HOH A . 
D 4 HOH   25 625 67 HOH   HOH A . 
D 4 HOH   26 626 14 HOH   HOH A . 
D 4 HOH   27 627 48 HOH   HOH A . 
D 4 HOH   28 628 1  HOH   HOH A . 
D 4 HOH   29 629 21 HOH   HOH A . 
D 4 HOH   30 630 46 HOH   HOH A . 
D 4 HOH   31 631 31 HOH   HOH A . 
D 4 HOH   32 632 42 HOH   HOH A . 
D 4 HOH   33 633 32 HOH   HOH A . 
D 4 HOH   34 634 36 HOH   HOH A . 
D 4 HOH   35 635 54 HOH   HOH A . 
D 4 HOH   36 636 63 HOH   HOH A . 
D 4 HOH   37 637 16 HOH   HOH A . 
D 4 HOH   38 638 22 HOH   HOH A . 
D 4 HOH   39 639 26 HOH   HOH A . 
D 4 HOH   40 640 5  HOH   HOH A . 
D 4 HOH   41 641 58 HOH   HOH A . 
D 4 HOH   42 642 23 HOH   HOH A . 
D 4 HOH   43 643 9  HOH   HOH A . 
D 4 HOH   44 644 18 HOH   HOH A . 
D 4 HOH   45 645 40 HOH   HOH A . 
D 4 HOH   46 646 6  HOH   HOH A . 
D 4 HOH   47 647 57 HOH   HOH A . 
D 4 HOH   48 648 62 HOH   HOH A . 
D 4 HOH   49 649 28 HOH   HOH A . 
D 4 HOH   50 650 44 HOH   HOH A . 
D 4 HOH   51 651 30 HOH   HOH A . 
D 4 HOH   52 652 38 HOH   HOH A . 
D 4 HOH   53 653 27 HOH   HOH A . 
D 4 HOH   54 654 72 HOH   HOH A . 
D 4 HOH   55 655 66 HOH   HOH A . 
D 4 HOH   56 656 25 HOH   HOH A . 
D 4 HOH   57 657 50 HOH   HOH A . 
D 4 HOH   58 658 11 HOH   HOH A . 
D 4 HOH   59 659 55 HOH   HOH A . 
D 4 HOH   60 660 68 HOH   HOH A . 
D 4 HOH   61 661 10 HOH   HOH A . 
D 4 HOH   62 662 56 HOH   HOH A . 
D 4 HOH   63 663 59 HOH   HOH A . 
D 4 HOH   64 664 51 HOH   HOH A . 
D 4 HOH   65 665 65 HOH   HOH A . 
D 4 HOH   66 666 35 HOH   HOH A . 
D 4 HOH   67 667 47 HOH   HOH A . 
D 4 HOH   68 668 33 HOH   HOH A . 
D 4 HOH   69 669 45 HOH   HOH A . 
D 4 HOH   70 670 64 HOH   HOH A . 
D 4 HOH   71 671 74 HOH   HOH A . 
D 4 HOH   72 672 60 HOH   HOH A . 
D 4 HOH   73 673 49 HOH   HOH A . 
D 4 HOH   74 674 73 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 43  ? CG  ? A LYS 15  CG  
6  1 Y 1 A LYS 43  ? CD  ? A LYS 15  CD  
7  1 Y 1 A LYS 43  ? CE  ? A LYS 15  CE  
8  1 Y 1 A LYS 43  ? NZ  ? A LYS 15  NZ  
9  1 Y 1 A GLU 172 ? CG  ? A GLU 144 CG  
10 1 Y 1 A GLU 172 ? CD  ? A GLU 144 CD  
11 1 Y 1 A GLU 172 ? OE1 ? A GLU 144 OE1 
12 1 Y 1 A GLU 172 ? OE2 ? A GLU 144 OE2 
13 1 Y 1 A LYS 193 ? CG  ? A LYS 165 CG  
14 1 Y 1 A LYS 193 ? CD  ? A LYS 165 CD  
15 1 Y 1 A LYS 193 ? CE  ? A LYS 165 CE  
16 1 Y 1 A LYS 193 ? NZ  ? A LYS 165 NZ  
17 1 Y 1 A GLU 201 ? CG  ? A GLU 173 CG  
18 1 Y 1 A GLU 201 ? CD  ? A GLU 173 CD  
19 1 Y 1 A GLU 201 ? OE1 ? A GLU 173 OE1 
20 1 Y 1 A GLU 201 ? OE2 ? A GLU 173 OE2 
21 1 Y 1 A ARG 208 ? CG  ? A ARG 180 CG  
22 1 Y 1 A ARG 208 ? CD  ? A ARG 180 CD  
23 1 Y 1 A ARG 208 ? NE  ? A ARG 180 NE  
24 1 Y 1 A ARG 208 ? CZ  ? A ARG 180 CZ  
25 1 Y 1 A ARG 208 ? NH1 ? A ARG 180 NH1 
26 1 Y 1 A ARG 208 ? NH2 ? A ARG 180 NH2 
27 1 Y 1 A LYS 289 ? CG  ? A LYS 261 CG  
28 1 Y 1 A LYS 289 ? CD  ? A LYS 261 CD  
29 1 Y 1 A LYS 289 ? CE  ? A LYS 261 CE  
30 1 Y 1 A LYS 289 ? NZ  ? A LYS 261 NZ  
31 1 Y 1 A ARG 290 ? CG  ? A ARG 262 CG  
32 1 Y 1 A ARG 290 ? CD  ? A ARG 262 CD  
33 1 Y 1 A ARG 290 ? NE  ? A ARG 262 NE  
34 1 Y 1 A ARG 290 ? CZ  ? A ARG 262 CZ  
35 1 Y 1 A ARG 290 ? NH1 ? A ARG 262 NH1 
36 1 Y 1 A ARG 290 ? NH2 ? A ARG 262 NH2 
37 1 Y 1 A GLN 344 ? CG  ? A GLN 316 CG  
38 1 Y 1 A GLN 344 ? CD  ? A GLN 316 CD  
39 1 Y 1 A GLN 344 ? OE1 ? A GLN 316 OE1 
40 1 Y 1 A GLN 344 ? NE2 ? A GLN 316 NE2 
41 1 Y 1 A LYS 347 ? CG  ? A LYS 319 CG  
42 1 Y 1 A LYS 347 ? CD  ? A LYS 319 CD  
43 1 Y 1 A LYS 347 ? CE  ? A LYS 319 CE  
44 1 Y 1 A LYS 347 ? NZ  ? A LYS 319 NZ  
45 1 Y 1 A LYS 348 ? CG  ? A LYS 320 CG  
46 1 Y 1 A LYS 348 ? CD  ? A LYS 320 CD  
47 1 Y 1 A LYS 348 ? CE  ? A LYS 320 CE  
48 1 Y 1 A LYS 348 ? NZ  ? A LYS 320 NZ  
49 1 Y 1 A ASP 357 ? CG  ? A ASP 329 CG  
50 1 Y 1 A ASP 357 ? OD1 ? A ASP 329 OD1 
51 1 Y 1 A ASP 357 ? OD2 ? A ASP 329 OD2 
52 1 Y 1 A LYS 360 ? CG  ? A LYS 332 CG  
53 1 Y 1 A LYS 360 ? CD  ? A LYS 332 CD  
54 1 Y 1 A LYS 360 ? CE  ? A LYS 332 CE  
55 1 Y 1 A LYS 360 ? NZ  ? A LYS 332 NZ  
56 1 Y 1 A GLN 374 ? CG  ? A GLN 346 CG  
57 1 Y 1 A GLN 374 ? CD  ? A GLN 346 CD  
58 1 Y 1 A GLN 374 ? OE1 ? A GLN 346 OE1 
59 1 Y 1 A GLN 374 ? NE2 ? A GLN 346 NE2 
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 435 ? CG  ? A GLU 407 CG  
75 1 Y 1 A GLU 435 ? CD  ? A GLU 407 CD  
76 1 Y 1 A GLU 435 ? OE1 ? A GLU 407 OE1 
77 1 Y 1 A GLU 435 ? OE2 ? A GLU 407 OE2 
78 1 Y 1 A LYS 436 ? CG  ? A LYS 408 CG  
79 1 Y 1 A LYS 436 ? CD  ? A LYS 408 CD  
80 1 Y 1 A LYS 436 ? CE  ? A LYS 408 CE  
81 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                   100.77 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XUE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.893 
_cell.length_a_esd                 ? 
_cell.length_b                     83.819 
_cell.length_b_esd                 ? 
_cell.length_c                     61.674 
_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                         8XUE 
_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                   8XUE 
_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             2.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.10 
_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         2021-06-18 
_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   0.987 
_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        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XUE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.218 
_reflns.d_resolution_low                               37.769 
_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                                     34638 
_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                           92.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.77 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.31 
_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                                   0.996 
_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                                    2.22 
_reflns_shell.d_res_low                                     2.35 
_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                             5487 
_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                                  0.881 
_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                                 8XUE 
_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                            2.218 
_refine.ls_d_res_low                             37.769 
_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                     18069 
_refine.ls_number_reflns_R_free                  904 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.60 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2019 
_refine.ls_R_factor_R_free                       0.2514 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1994 
_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                          1.35 
_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                 29.90 
_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                            0.27 
_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                       2.218 
_refine_hist.d_res_low                        37.769 
_refine_hist.number_atoms_solvent             74 
_refine_hist.number_atoms_total               2961 
_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        2853 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_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  ? 2963 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.955  ? 4022 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.295 ? 1742 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 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' 2.2184 2.3574 . . 151 2865 95.00 . . . . 0.2685 . . . . . . . . . . . 0.3337 
'X-RAY DIFFRACTION' 2.3574 2.5393 . . 151 2873 95.00 . . . . 0.2488 . . . . . . . . . . . 0.3293 
'X-RAY DIFFRACTION' 2.5393 2.7948 . . 153 2894 96.00 . . . . 0.2280 . . . . . . . . . . . 0.2704 
'X-RAY DIFFRACTION' 2.7948 3.1990 . . 152 2880 96.00 . . . . 0.2157 . . . . . . . . . . . 0.2654 
'X-RAY DIFFRACTION' 3.1990 4.0297 . . 149 2840 94.00 . . . . 0.1778 . . . . . . . . . . . 0.2161 
'X-RAY DIFFRACTION' 4.0297 8      . . 148 2813 92.00 . . . . 0.1713 . . . . . . . . . . . 0.2240 
# 
_struct.entry_id                     8XUE 
_struct.title                        'Crystal structure of AtHPPD-Y191497 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        8XUE 
_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              8XUE 
_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 8XUE GLY A 1 ? UNP P93836 ? ? 'expression tag' 29 1 
1 8XUE SER A 2 ? UNP P93836 ? ? 'expression tag' 30 2 
1 8XUE HIS A 3 ? UNP P93836 ? ? 'expression tag' 31 3 
1 8XUE 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)' 3540  ? 
1 MORE         -38   ? 
1 'SSA (A^2)'  27830 ? 
# 
_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 -23.0496663398 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 121.1752531898 
# 
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  ? ALA A 81  ? SER A 104 ALA A 109 5 ? 6  
HELX_P HELX_P4  AA4 ASP A 96  ? GLY A 108 ? ASP A 124 GLY A 136 1 ? 13 
HELX_P HELX_P5  AA5 ASP A 120 ? ASN A 131 ? ASP A 148 ASN A 159 1 ? 12 
HELX_P HELX_P6  AA6 GLU A 205 ? GLY A 218 ? GLU A 233 GLY A 246 1 ? 14 
HELX_P HELX_P7  AA7 SER A 264 ? GLU A 274 ? SER A 292 GLU A 302 1 ? 11 
HELX_P HELX_P8  AA8 ASP A 287 ? ARG A 298 ? ASP A 315 ARG A 326 1 ? 12 
HELX_P HELX_P9  AA9 PRO A 311 ? ASN A 317 ? PRO A 339 ASN A 345 1 ? 7  
HELX_P HELX_P10 AB1 ASN A 317 ? GLY A 323 ? ASN A 345 GLY A 351 1 ? 7  
HELX_P HELX_P11 AB2 SER A 327 ? GLY A 338 ? SER A 355 GLY A 366 1 ? 12 
HELX_P HELX_P12 AB3 GLY A 394 ? LYS A 408 ? GLY A 422 LYS A 436 1 ? 15 
# 
_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 ? ? ? ? ? ? ? 2.037 ? ? 
metalc1 metalc ? ? A HIS 198 NE2 ? ? ? 1_555 B CO    .   CO  ? ? A HIS 226 A CO    501 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc2 metalc ? ? A HIS 280 NE2 ? ? ? 1_555 B CO    .   CO  ? ? A HIS 308 A CO    501 1_555 ? ? ? ? ? ? ? 2.484 ? ? 
metalc3 metalc ? ? A GLU 366 OE1 ? ? ? 1_555 B CO    .   CO  ? ? A GLU 394 A CO    501 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc4 metalc ? ? B CO  .   CO  ? ? ? 1_555 C A1LW6 .   O09 ? ? A CO  501 A A1LW6 502 1_555 ? ? ? ? ? ? ? 2.076 ? ? 
metalc5 metalc ? ? B CO  .   CO  ? ? ? 1_555 C A1LW6 .   O16 ? ? A CO  501 A A1LW6 502 1_555 ? ? ? ? ? ? ? 2.190 ? ? 
metalc6 metalc ? ? B CO  .   CO  ? ? ? 1_555 D HOH   .   O   ? ? A CO  501 A HOH   628 1_555 ? ? ? ? ? ? ? 2.180 ? ? 
# 
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 ? B CO . ? A CO 501 ? 1_555 NE2 ? A HIS   280 ? A HIS   308 ? 1_555 100.7 ? 
2  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 OE1 ? A GLU   366 ? A GLU   394 ? 1_555 91.9  ? 
3  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 OE1 ? A GLU   366 ? A GLU   394 ? 1_555 85.2  ? 
4  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O09 ? C A1LW6 .   ? A A1LW6 502 ? 1_555 164.1 ? 
5  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O09 ? C A1LW6 .   ? A A1LW6 502 ? 1_555 85.7  ? 
6  OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O09 ? C A1LW6 .   ? A A1LW6 502 ? 1_555 103.2 ? 
7  NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O16 ? C A1LW6 .   ? A A1LW6 502 ? 1_555 88.2  ? 
8  NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O16 ? C A1LW6 .   ? A A1LW6 502 ? 1_555 90.9  ? 
9  OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O16 ? C A1LW6 .   ? A A1LW6 502 ? 1_555 176.1 ? 
10 O09 ? C A1LW6 .   ? A A1LW6 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O16 ? C A1LW6 .   ? A A1LW6 502 ? 1_555 77.1  ? 
11 NE2 ? A HIS   198 ? A HIS   226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   628 ? 1_555 85.4  ? 
12 NE2 ? A HIS   280 ? A HIS   308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   628 ? 1_555 167.4 ? 
13 OE1 ? A GLU   366 ? A GLU   394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   628 ? 1_555 83.6  ? 
14 O09 ? C A1LW6 .   ? A A1LW6 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   628 ? 1_555 91.3  ? 
15 O16 ? C A1LW6 .   ? A A1LW6 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH   .   ? A HOH   628 ? 1_555 100.3 ? 
# 
_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 LEU A 153 ? N LEU A 181 O VAL A 157 ? O VAL A 185 
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 ILE A 22  ? N ILE A 50  O LEU A 70  ? O LEU A 98  
AA1 6 7 O PHE A 69  ? O PHE A 97  N LEU A 62  ? N LEU A 90  
AA1 7 8 O LEU A 61  ? O LEU A 89  N ALA A 46  ? N ALA A 74  
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 ARG A 194 ? N ARG A 222 O MET A 284 ? O MET A 312 
AA2 5 6 N SER A 285 ? N SER A 313 O ILE A 368 ? O ILE A 396 
AA2 6 7 O ILE A 367 ? O ILE A 395 N ILE A 352 ? N ILE A 380 
AA2 7 8 O LEU A 349 ? O LEU A 377 N ASP A 342 ? N ASP A 370 
# 
_pdbx_entry_details.entry_id                   8XUE 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 45  ? ? -96.17  -82.40  
2 1 VAL A 84  ? ? -105.92 -60.53  
3 1 LEU A 181 ? ? -99.85  -60.79  
4 1 GLU A 210 ? ? -35.07  117.32  
5 1 ASP A 218 ? ? -170.17 111.67  
6 1 ASP A 315 ? ? -168.36 77.05   
7 1 ASP A 372 ? ? -102.99 -149.49 
8 1 THR A 390 ? ? -124.64 -95.61  
9 1 CYS A 416 ? ? -53.28  108.54  
# 
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 
A1LW6 C10  C  N N 1   
A1LW6 C13  C  N N 2   
A1LW6 C20  C  N N 3   
A1LW6 C24  C  Y N 4   
A1LW6 C26  C  Y N 5   
A1LW6 C28  C  Y N 6   
A1LW6 C01  C  Y N 7   
A1LW6 C02  C  Y N 8   
A1LW6 C03  C  Y N 9   
A1LW6 C04  C  Y N 10  
A1LW6 C05  C  Y N 11  
A1LW6 C06  C  Y N 12  
A1LW6 C07  C  N N 13  
A1LW6 C08  C  N N 14  
A1LW6 C11  C  N N 15  
A1LW6 C12  C  N N 16  
A1LW6 C14  C  N N 17  
A1LW6 C18  C  N N 18  
A1LW6 C23  C  N N 19  
A1LW6 C25  C  Y N 20  
A1LW6 C27  C  Y N 21  
A1LW6 C29  C  Y N 22  
A1LW6 N17  N  N N 23  
A1LW6 N19  N  N N 24  
A1LW6 N31  N  N N 25  
A1LW6 O09  O  N N 26  
A1LW6 O15  O  N N 27  
A1LW6 O16  O  N N 28  
A1LW6 O21  O  N N 29  
A1LW6 O22  O  N N 30  
A1LW6 O32  O  N N 31  
A1LW6 O33  O  N N 32  
A1LW6 CL1  CL N N 33  
A1LW6 H1   H  N N 34  
A1LW6 H2   H  N N 35  
A1LW6 H3   H  N N 36  
A1LW6 H4   H  N N 37  
A1LW6 H5   H  N N 38  
A1LW6 H6   H  N N 39  
A1LW6 H7   H  N N 40  
A1LW6 H8   H  N N 41  
A1LW6 H9   H  N N 42  
A1LW6 H10  H  N N 43  
A1LW6 H11  H  N N 44  
A1LW6 H12  H  N N 45  
A1LW6 H13  H  N N 46  
A1LW6 H14  H  N N 47  
A1LW6 H15  H  N N 48  
A1LW6 H16  H  N N 49  
ALA   N    N  N N 50  
ALA   CA   C  N S 51  
ALA   C    C  N N 52  
ALA   O    O  N N 53  
ALA   CB   C  N N 54  
ALA   OXT  O  N N 55  
ALA   H    H  N N 56  
ALA   H2   H  N N 57  
ALA   HA   H  N N 58  
ALA   HB1  H  N N 59  
ALA   HB2  H  N N 60  
ALA   HB3  H  N N 61  
ALA   HXT  H  N N 62  
ARG   N    N  N N 63  
ARG   CA   C  N S 64  
ARG   C    C  N N 65  
ARG   O    O  N N 66  
ARG   CB   C  N N 67  
ARG   CG   C  N N 68  
ARG   CD   C  N N 69  
ARG   NE   N  N N 70  
ARG   CZ   C  N N 71  
ARG   NH1  N  N N 72  
ARG   NH2  N  N N 73  
ARG   OXT  O  N N 74  
ARG   H    H  N N 75  
ARG   H2   H  N N 76  
ARG   HA   H  N N 77  
ARG   HB2  H  N N 78  
ARG   HB3  H  N N 79  
ARG   HG2  H  N N 80  
ARG   HG3  H  N N 81  
ARG   HD2  H  N N 82  
ARG   HD3  H  N N 83  
ARG   HE   H  N N 84  
ARG   HH11 H  N N 85  
ARG   HH12 H  N N 86  
ARG   HH21 H  N N 87  
ARG   HH22 H  N N 88  
ARG   HXT  H  N N 89  
ASN   N    N  N N 90  
ASN   CA   C  N S 91  
ASN   C    C  N N 92  
ASN   O    O  N N 93  
ASN   CB   C  N N 94  
ASN   CG   C  N N 95  
ASN   OD1  O  N N 96  
ASN   ND2  N  N N 97  
ASN   OXT  O  N N 98  
ASN   H    H  N N 99  
ASN   H2   H  N N 100 
ASN   HA   H  N N 101 
ASN   HB2  H  N N 102 
ASN   HB3  H  N N 103 
ASN   HD21 H  N N 104 
ASN   HD22 H  N N 105 
ASN   HXT  H  N N 106 
ASP   N    N  N N 107 
ASP   CA   C  N S 108 
ASP   C    C  N N 109 
ASP   O    O  N N 110 
ASP   CB   C  N N 111 
ASP   CG   C  N N 112 
ASP   OD1  O  N N 113 
ASP   OD2  O  N N 114 
ASP   OXT  O  N N 115 
ASP   H    H  N N 116 
ASP   H2   H  N N 117 
ASP   HA   H  N N 118 
ASP   HB2  H  N N 119 
ASP   HB3  H  N N 120 
ASP   HD2  H  N N 121 
ASP   HXT  H  N N 122 
CO    CO   CO N N 123 
CYS   N    N  N N 124 
CYS   CA   C  N R 125 
CYS   C    C  N N 126 
CYS   O    O  N N 127 
CYS   CB   C  N N 128 
CYS   SG   S  N N 129 
CYS   OXT  O  N N 130 
CYS   H    H  N N 131 
CYS   H2   H  N N 132 
CYS   HA   H  N N 133 
CYS   HB2  H  N N 134 
CYS   HB3  H  N N 135 
CYS   HG   H  N N 136 
CYS   HXT  H  N N 137 
GLN   N    N  N N 138 
GLN   CA   C  N S 139 
GLN   C    C  N N 140 
GLN   O    O  N N 141 
GLN   CB   C  N N 142 
GLN   CG   C  N N 143 
GLN   CD   C  N N 144 
GLN   OE1  O  N N 145 
GLN   NE2  N  N N 146 
GLN   OXT  O  N N 147 
GLN   H    H  N N 148 
GLN   H2   H  N N 149 
GLN   HA   H  N N 150 
GLN   HB2  H  N N 151 
GLN   HB3  H  N N 152 
GLN   HG2  H  N N 153 
GLN   HG3  H  N N 154 
GLN   HE21 H  N N 155 
GLN   HE22 H  N N 156 
GLN   HXT  H  N N 157 
GLU   N    N  N N 158 
GLU   CA   C  N S 159 
GLU   C    C  N N 160 
GLU   O    O  N N 161 
GLU   CB   C  N N 162 
GLU   CG   C  N N 163 
GLU   CD   C  N N 164 
GLU   OE1  O  N N 165 
GLU   OE2  O  N N 166 
GLU   OXT  O  N N 167 
GLU   H    H  N N 168 
GLU   H2   H  N N 169 
GLU   HA   H  N N 170 
GLU   HB2  H  N N 171 
GLU   HB3  H  N N 172 
GLU   HG2  H  N N 173 
GLU   HG3  H  N N 174 
GLU   HE2  H  N N 175 
GLU   HXT  H  N N 176 
GLY   N    N  N N 177 
GLY   CA   C  N N 178 
GLY   C    C  N N 179 
GLY   O    O  N N 180 
GLY   OXT  O  N N 181 
GLY   H    H  N N 182 
GLY   H2   H  N N 183 
GLY   HA2  H  N N 184 
GLY   HA3  H  N N 185 
GLY   HXT  H  N N 186 
HIS   N    N  N N 187 
HIS   CA   C  N S 188 
HIS   C    C  N N 189 
HIS   O    O  N N 190 
HIS   CB   C  N N 191 
HIS   CG   C  Y N 192 
HIS   ND1  N  Y N 193 
HIS   CD2  C  Y N 194 
HIS   CE1  C  Y N 195 
HIS   NE2  N  Y N 196 
HIS   OXT  O  N N 197 
HIS   H    H  N N 198 
HIS   H2   H  N N 199 
HIS   HA   H  N N 200 
HIS   HB2  H  N N 201 
HIS   HB3  H  N N 202 
HIS   HD1  H  N N 203 
HIS   HD2  H  N N 204 
HIS   HE1  H  N N 205 
HIS   HE2  H  N N 206 
HIS   HXT  H  N N 207 
HOH   O    O  N N 208 
HOH   H1   H  N N 209 
HOH   H2   H  N N 210 
ILE   N    N  N N 211 
ILE   CA   C  N S 212 
ILE   C    C  N N 213 
ILE   O    O  N N 214 
ILE   CB   C  N S 215 
ILE   CG1  C  N N 216 
ILE   CG2  C  N N 217 
ILE   CD1  C  N N 218 
ILE   OXT  O  N N 219 
ILE   H    H  N N 220 
ILE   H2   H  N N 221 
ILE   HA   H  N N 222 
ILE   HB   H  N N 223 
ILE   HG12 H  N N 224 
ILE   HG13 H  N N 225 
ILE   HG21 H  N N 226 
ILE   HG22 H  N N 227 
ILE   HG23 H  N N 228 
ILE   HD11 H  N N 229 
ILE   HD12 H  N N 230 
ILE   HD13 H  N N 231 
ILE   HXT  H  N N 232 
LEU   N    N  N N 233 
LEU   CA   C  N S 234 
LEU   C    C  N N 235 
LEU   O    O  N N 236 
LEU   CB   C  N N 237 
LEU   CG   C  N N 238 
LEU   CD1  C  N N 239 
LEU   CD2  C  N N 240 
LEU   OXT  O  N N 241 
LEU   H    H  N N 242 
LEU   H2   H  N N 243 
LEU   HA   H  N N 244 
LEU   HB2  H  N N 245 
LEU   HB3  H  N N 246 
LEU   HG   H  N N 247 
LEU   HD11 H  N N 248 
LEU   HD12 H  N N 249 
LEU   HD13 H  N N 250 
LEU   HD21 H  N N 251 
LEU   HD22 H  N N 252 
LEU   HD23 H  N N 253 
LEU   HXT  H  N N 254 
LYS   N    N  N N 255 
LYS   CA   C  N S 256 
LYS   C    C  N N 257 
LYS   O    O  N N 258 
LYS   CB   C  N N 259 
LYS   CG   C  N N 260 
LYS   CD   C  N N 261 
LYS   CE   C  N N 262 
LYS   NZ   N  N N 263 
LYS   OXT  O  N N 264 
LYS   H    H  N N 265 
LYS   H2   H  N N 266 
LYS   HA   H  N N 267 
LYS   HB2  H  N N 268 
LYS   HB3  H  N N 269 
LYS   HG2  H  N N 270 
LYS   HG3  H  N N 271 
LYS   HD2  H  N N 272 
LYS   HD3  H  N N 273 
LYS   HE2  H  N N 274 
LYS   HE3  H  N N 275 
LYS   HZ1  H  N N 276 
LYS   HZ2  H  N N 277 
LYS   HZ3  H  N N 278 
LYS   HXT  H  N N 279 
MET   N    N  N N 280 
MET   CA   C  N S 281 
MET   C    C  N N 282 
MET   O    O  N N 283 
MET   CB   C  N N 284 
MET   CG   C  N N 285 
MET   SD   S  N N 286 
MET   CE   C  N N 287 
MET   OXT  O  N N 288 
MET   H    H  N N 289 
MET   H2   H  N N 290 
MET   HA   H  N N 291 
MET   HB2  H  N N 292 
MET   HB3  H  N N 293 
MET   HG2  H  N N 294 
MET   HG3  H  N N 295 
MET   HE1  H  N N 296 
MET   HE2  H  N N 297 
MET   HE3  H  N N 298 
MET   HXT  H  N N 299 
PHE   N    N  N N 300 
PHE   CA   C  N S 301 
PHE   C    C  N N 302 
PHE   O    O  N N 303 
PHE   CB   C  N N 304 
PHE   CG   C  Y N 305 
PHE   CD1  C  Y N 306 
PHE   CD2  C  Y N 307 
PHE   CE1  C  Y N 308 
PHE   CE2  C  Y N 309 
PHE   CZ   C  Y N 310 
PHE   OXT  O  N N 311 
PHE   H    H  N N 312 
PHE   H2   H  N N 313 
PHE   HA   H  N N 314 
PHE   HB2  H  N N 315 
PHE   HB3  H  N N 316 
PHE   HD1  H  N N 317 
PHE   HD2  H  N N 318 
PHE   HE1  H  N N 319 
PHE   HE2  H  N N 320 
PHE   HZ   H  N N 321 
PHE   HXT  H  N N 322 
PRO   N    N  N N 323 
PRO   CA   C  N S 324 
PRO   C    C  N N 325 
PRO   O    O  N N 326 
PRO   CB   C  N N 327 
PRO   CG   C  N N 328 
PRO   CD   C  N N 329 
PRO   OXT  O  N N 330 
PRO   H    H  N N 331 
PRO   HA   H  N N 332 
PRO   HB2  H  N N 333 
PRO   HB3  H  N N 334 
PRO   HG2  H  N N 335 
PRO   HG3  H  N N 336 
PRO   HD2  H  N N 337 
PRO   HD3  H  N N 338 
PRO   HXT  H  N N 339 
SER   N    N  N N 340 
SER   CA   C  N S 341 
SER   C    C  N N 342 
SER   O    O  N N 343 
SER   CB   C  N N 344 
SER   OG   O  N N 345 
SER   OXT  O  N N 346 
SER   H    H  N N 347 
SER   H2   H  N N 348 
SER   HA   H  N N 349 
SER   HB2  H  N N 350 
SER   HB3  H  N N 351 
SER   HG   H  N N 352 
SER   HXT  H  N N 353 
THR   N    N  N N 354 
THR   CA   C  N S 355 
THR   C    C  N N 356 
THR   O    O  N N 357 
THR   CB   C  N R 358 
THR   OG1  O  N N 359 
THR   CG2  C  N N 360 
THR   OXT  O  N N 361 
THR   H    H  N N 362 
THR   H2   H  N N 363 
THR   HA   H  N N 364 
THR   HB   H  N N 365 
THR   HG1  H  N N 366 
THR   HG21 H  N N 367 
THR   HG22 H  N N 368 
THR   HG23 H  N N 369 
THR   HXT  H  N N 370 
TRP   N    N  N N 371 
TRP   CA   C  N S 372 
TRP   C    C  N N 373 
TRP   O    O  N N 374 
TRP   CB   C  N N 375 
TRP   CG   C  Y N 376 
TRP   CD1  C  Y N 377 
TRP   CD2  C  Y N 378 
TRP   NE1  N  Y N 379 
TRP   CE2  C  Y N 380 
TRP   CE3  C  Y N 381 
TRP   CZ2  C  Y N 382 
TRP   CZ3  C  Y N 383 
TRP   CH2  C  Y N 384 
TRP   OXT  O  N N 385 
TRP   H    H  N N 386 
TRP   H2   H  N N 387 
TRP   HA   H  N N 388 
TRP   HB2  H  N N 389 
TRP   HB3  H  N N 390 
TRP   HD1  H  N N 391 
TRP   HE1  H  N N 392 
TRP   HE3  H  N N 393 
TRP   HZ2  H  N N 394 
TRP   HZ3  H  N N 395 
TRP   HH2  H  N N 396 
TRP   HXT  H  N N 397 
TYR   N    N  N N 398 
TYR   CA   C  N S 399 
TYR   C    C  N N 400 
TYR   O    O  N N 401 
TYR   CB   C  N N 402 
TYR   CG   C  Y N 403 
TYR   CD1  C  Y N 404 
TYR   CD2  C  Y N 405 
TYR   CE1  C  Y N 406 
TYR   CE2  C  Y N 407 
TYR   CZ   C  Y N 408 
TYR   OH   O  N N 409 
TYR   OXT  O  N N 410 
TYR   H    H  N N 411 
TYR   H2   H  N N 412 
TYR   HA   H  N N 413 
TYR   HB2  H  N N 414 
TYR   HB3  H  N N 415 
TYR   HD1  H  N N 416 
TYR   HD2  H  N N 417 
TYR   HE1  H  N N 418 
TYR   HE2  H  N N 419 
TYR   HH   H  N N 420 
TYR   HXT  H  N N 421 
VAL   N    N  N N 422 
VAL   CA   C  N S 423 
VAL   C    C  N N 424 
VAL   O    O  N N 425 
VAL   CB   C  N N 426 
VAL   CG1  C  N N 427 
VAL   CG2  C  N N 428 
VAL   OXT  O  N N 429 
VAL   H    H  N N 430 
VAL   H2   H  N N 431 
VAL   HA   H  N N 432 
VAL   HB   H  N N 433 
VAL   HG11 H  N N 434 
VAL   HG12 H  N N 435 
VAL   HG13 H  N N 436 
VAL   HG21 H  N N 437 
VAL   HG22 H  N N 438 
VAL   HG23 H  N N 439 
VAL   HXT  H  N N 440 
# 
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 
A1LW6 O16 C14  doub N N 1   
A1LW6 O09 C07  doub N N 2   
A1LW6 C14 C13  sing N N 3   
A1LW6 C14 C08  sing N N 4   
A1LW6 O32 N31  sing N N 5   
A1LW6 C13 C12  sing N N 6   
A1LW6 C07 C08  sing N N 7   
A1LW6 C07 C06  sing N N 8   
A1LW6 N31 O33  doub N N 9   
A1LW6 N31 C05  sing N N 10  
A1LW6 C08 C10  doub N N 11  
A1LW6 C12 C11  sing N N 12  
A1LW6 C06 C05  doub Y N 13  
A1LW6 C06 C01  sing Y N 14  
A1LW6 C05 C04  sing Y N 15  
A1LW6 C01 C02  doub Y N 16  
A1LW6 C10 C11  sing N N 17  
A1LW6 C10 O15  sing N N 18  
A1LW6 C04 C03  doub Y N 19  
A1LW6 C02 C03  sing Y N 20  
A1LW6 C02 N17  sing N N 21  
A1LW6 C03 C20  sing N N 22  
A1LW6 C23 N17  sing N N 23  
A1LW6 N17 C18  sing N N 24  
A1LW6 C20 O21  doub N N 25  
A1LW6 C20 N19  sing N N 26  
A1LW6 C18 N19  sing N N 27  
A1LW6 C18 O22  doub N N 28  
A1LW6 N19 C24  sing N N 29  
A1LW6 C25 C24  doub Y N 30  
A1LW6 C25 C26  sing Y N 31  
A1LW6 C24 C29  sing Y N 32  
A1LW6 C26 C27  doub Y N 33  
A1LW6 C29 C28  doub Y N 34  
A1LW6 C27 C28  sing Y N 35  
A1LW6 C27 CL1  sing N N 36  
A1LW6 C13 H1   sing N N 37  
A1LW6 C13 H2   sing N N 38  
A1LW6 C26 H3   sing N N 39  
A1LW6 C28 H4   sing N N 40  
A1LW6 C01 H5   sing N N 41  
A1LW6 C04 H6   sing N N 42  
A1LW6 C11 H7   sing N N 43  
A1LW6 C11 H8   sing N N 44  
A1LW6 C12 H9   sing N N 45  
A1LW6 C12 H10  sing N N 46  
A1LW6 C23 H11  sing N N 47  
A1LW6 C23 H12  sing N N 48  
A1LW6 C23 H13  sing N N 49  
A1LW6 C25 H14  sing N N 50  
A1LW6 C29 H15  sing N N 51  
A1LW6 O15 H16  sing N N 52  
ALA   N   CA   sing N N 53  
ALA   N   H    sing N N 54  
ALA   N   H2   sing N N 55  
ALA   CA  C    sing N N 56  
ALA   CA  CB   sing N N 57  
ALA   CA  HA   sing N N 58  
ALA   C   O    doub N N 59  
ALA   C   OXT  sing N N 60  
ALA   CB  HB1  sing N N 61  
ALA   CB  HB2  sing N N 62  
ALA   CB  HB3  sing N N 63  
ALA   OXT HXT  sing N N 64  
ARG   N   CA   sing N N 65  
ARG   N   H    sing N N 66  
ARG   N   H2   sing N N 67  
ARG   CA  C    sing N N 68  
ARG   CA  CB   sing N N 69  
ARG   CA  HA   sing N N 70  
ARG   C   O    doub N N 71  
ARG   C   OXT  sing N N 72  
ARG   CB  CG   sing N N 73  
ARG   CB  HB2  sing N N 74  
ARG   CB  HB3  sing N N 75  
ARG   CG  CD   sing N N 76  
ARG   CG  HG2  sing N N 77  
ARG   CG  HG3  sing N N 78  
ARG   CD  NE   sing N N 79  
ARG   CD  HD2  sing N N 80  
ARG   CD  HD3  sing N N 81  
ARG   NE  CZ   sing N N 82  
ARG   NE  HE   sing N N 83  
ARG   CZ  NH1  sing N N 84  
ARG   CZ  NH2  doub N N 85  
ARG   NH1 HH11 sing N N 86  
ARG   NH1 HH12 sing N N 87  
ARG   NH2 HH21 sing N N 88  
ARG   NH2 HH22 sing N N 89  
ARG   OXT HXT  sing N N 90  
ASN   N   CA   sing N N 91  
ASN   N   H    sing N N 92  
ASN   N   H2   sing N N 93  
ASN   CA  C    sing N N 94  
ASN   CA  CB   sing N N 95  
ASN   CA  HA   sing N N 96  
ASN   C   O    doub N N 97  
ASN   C   OXT  sing N N 98  
ASN   CB  CG   sing N N 99  
ASN   CB  HB2  sing N N 100 
ASN   CB  HB3  sing N N 101 
ASN   CG  OD1  doub N N 102 
ASN   CG  ND2  sing N N 103 
ASN   ND2 HD21 sing N N 104 
ASN   ND2 HD22 sing N N 105 
ASN   OXT HXT  sing N N 106 
ASP   N   CA   sing N N 107 
ASP   N   H    sing N N 108 
ASP   N   H2   sing N N 109 
ASP   CA  C    sing N N 110 
ASP   CA  CB   sing N N 111 
ASP   CA  HA   sing N N 112 
ASP   C   O    doub N N 113 
ASP   C   OXT  sing N N 114 
ASP   CB  CG   sing N N 115 
ASP   CB  HB2  sing N N 116 
ASP   CB  HB3  sing N N 117 
ASP   CG  OD1  doub N N 118 
ASP   CG  OD2  sing N N 119 
ASP   OD2 HD2  sing N N 120 
ASP   OXT HXT  sing N N 121 
CYS   N   CA   sing N N 122 
CYS   N   H    sing N N 123 
CYS   N   H2   sing N N 124 
CYS   CA  C    sing N N 125 
CYS   CA  CB   sing N N 126 
CYS   CA  HA   sing N N 127 
CYS   C   O    doub N N 128 
CYS   C   OXT  sing N N 129 
CYS   CB  SG   sing N N 130 
CYS   CB  HB2  sing N N 131 
CYS   CB  HB3  sing N N 132 
CYS   SG  HG   sing N N 133 
CYS   OXT HXT  sing N N 134 
GLN   N   CA   sing N N 135 
GLN   N   H    sing N N 136 
GLN   N   H2   sing N N 137 
GLN   CA  C    sing N N 138 
GLN   CA  CB   sing N N 139 
GLN   CA  HA   sing N N 140 
GLN   C   O    doub N N 141 
GLN   C   OXT  sing N N 142 
GLN   CB  CG   sing N N 143 
GLN   CB  HB2  sing N N 144 
GLN   CB  HB3  sing N N 145 
GLN   CG  CD   sing N N 146 
GLN   CG  HG2  sing N N 147 
GLN   CG  HG3  sing N N 148 
GLN   CD  OE1  doub N N 149 
GLN   CD  NE2  sing N N 150 
GLN   NE2 HE21 sing N N 151 
GLN   NE2 HE22 sing N N 152 
GLN   OXT HXT  sing N N 153 
GLU   N   CA   sing N N 154 
GLU   N   H    sing N N 155 
GLU   N   H2   sing N N 156 
GLU   CA  C    sing N N 157 
GLU   CA  CB   sing N N 158 
GLU   CA  HA   sing N N 159 
GLU   C   O    doub N N 160 
GLU   C   OXT  sing N N 161 
GLU   CB  CG   sing N N 162 
GLU   CB  HB2  sing N N 163 
GLU   CB  HB3  sing N N 164 
GLU   CG  CD   sing N N 165 
GLU   CG  HG2  sing N N 166 
GLU   CG  HG3  sing N N 167 
GLU   CD  OE1  doub N N 168 
GLU   CD  OE2  sing N N 169 
GLU   OE2 HE2  sing N N 170 
GLU   OXT HXT  sing N N 171 
GLY   N   CA   sing N N 172 
GLY   N   H    sing N N 173 
GLY   N   H2   sing N N 174 
GLY   CA  C    sing N N 175 
GLY   CA  HA2  sing N N 176 
GLY   CA  HA3  sing N N 177 
GLY   C   O    doub N N 178 
GLY   C   OXT  sing N N 179 
GLY   OXT HXT  sing N N 180 
HIS   N   CA   sing N N 181 
HIS   N   H    sing N N 182 
HIS   N   H2   sing N N 183 
HIS   CA  C    sing N N 184 
HIS   CA  CB   sing N N 185 
HIS   CA  HA   sing N N 186 
HIS   C   O    doub N N 187 
HIS   C   OXT  sing N N 188 
HIS   CB  CG   sing N N 189 
HIS   CB  HB2  sing N N 190 
HIS   CB  HB3  sing N N 191 
HIS   CG  ND1  sing Y N 192 
HIS   CG  CD2  doub Y N 193 
HIS   ND1 CE1  doub Y N 194 
HIS   ND1 HD1  sing N N 195 
HIS   CD2 NE2  sing Y N 196 
HIS   CD2 HD2  sing N N 197 
HIS   CE1 NE2  sing Y N 198 
HIS   CE1 HE1  sing N N 199 
HIS   NE2 HE2  sing N N 200 
HIS   OXT HXT  sing N N 201 
HOH   O   H1   sing N N 202 
HOH   O   H2   sing N N 203 
ILE   N   CA   sing N N 204 
ILE   N   H    sing N N 205 
ILE   N   H2   sing N N 206 
ILE   CA  C    sing N N 207 
ILE   CA  CB   sing N N 208 
ILE   CA  HA   sing N N 209 
ILE   C   O    doub N N 210 
ILE   C   OXT  sing N N 211 
ILE   CB  CG1  sing N N 212 
ILE   CB  CG2  sing N N 213 
ILE   CB  HB   sing N N 214 
ILE   CG1 CD1  sing N N 215 
ILE   CG1 HG12 sing N N 216 
ILE   CG1 HG13 sing N N 217 
ILE   CG2 HG21 sing N N 218 
ILE   CG2 HG22 sing N N 219 
ILE   CG2 HG23 sing N N 220 
ILE   CD1 HD11 sing N N 221 
ILE   CD1 HD12 sing N N 222 
ILE   CD1 HD13 sing N N 223 
ILE   OXT HXT  sing N N 224 
LEU   N   CA   sing N N 225 
LEU   N   H    sing N N 226 
LEU   N   H2   sing N N 227 
LEU   CA  C    sing N N 228 
LEU   CA  CB   sing N N 229 
LEU   CA  HA   sing N N 230 
LEU   C   O    doub N N 231 
LEU   C   OXT  sing N N 232 
LEU   CB  CG   sing N N 233 
LEU   CB  HB2  sing N N 234 
LEU   CB  HB3  sing N N 235 
LEU   CG  CD1  sing N N 236 
LEU   CG  CD2  sing N N 237 
LEU   CG  HG   sing N N 238 
LEU   CD1 HD11 sing N N 239 
LEU   CD1 HD12 sing N N 240 
LEU   CD1 HD13 sing N N 241 
LEU   CD2 HD21 sing N N 242 
LEU   CD2 HD22 sing N N 243 
LEU   CD2 HD23 sing N N 244 
LEU   OXT HXT  sing N N 245 
LYS   N   CA   sing N N 246 
LYS   N   H    sing N N 247 
LYS   N   H2   sing N N 248 
LYS   CA  C    sing N N 249 
LYS   CA  CB   sing N N 250 
LYS   CA  HA   sing N N 251 
LYS   C   O    doub N N 252 
LYS   C   OXT  sing N N 253 
LYS   CB  CG   sing N N 254 
LYS   CB  HB2  sing N N 255 
LYS   CB  HB3  sing N N 256 
LYS   CG  CD   sing N N 257 
LYS   CG  HG2  sing N N 258 
LYS   CG  HG3  sing N N 259 
LYS   CD  CE   sing N N 260 
LYS   CD  HD2  sing N N 261 
LYS   CD  HD3  sing N N 262 
LYS   CE  NZ   sing N N 263 
LYS   CE  HE2  sing N N 264 
LYS   CE  HE3  sing N N 265 
LYS   NZ  HZ1  sing N N 266 
LYS   NZ  HZ2  sing N N 267 
LYS   NZ  HZ3  sing N N 268 
LYS   OXT HXT  sing N N 269 
MET   N   CA   sing N N 270 
MET   N   H    sing N N 271 
MET   N   H2   sing N N 272 
MET   CA  C    sing N N 273 
MET   CA  CB   sing N N 274 
MET   CA  HA   sing N N 275 
MET   C   O    doub N N 276 
MET   C   OXT  sing N N 277 
MET   CB  CG   sing N N 278 
MET   CB  HB2  sing N N 279 
MET   CB  HB3  sing N N 280 
MET   CG  SD   sing N N 281 
MET   CG  HG2  sing N N 282 
MET   CG  HG3  sing N N 283 
MET   SD  CE   sing N N 284 
MET   CE  HE1  sing N N 285 
MET   CE  HE2  sing N N 286 
MET   CE  HE3  sing N N 287 
MET   OXT HXT  sing N N 288 
PHE   N   CA   sing N N 289 
PHE   N   H    sing N N 290 
PHE   N   H2   sing N N 291 
PHE   CA  C    sing N N 292 
PHE   CA  CB   sing N N 293 
PHE   CA  HA   sing N N 294 
PHE   C   O    doub N N 295 
PHE   C   OXT  sing N N 296 
PHE   CB  CG   sing N N 297 
PHE   CB  HB2  sing N N 298 
PHE   CB  HB3  sing N N 299 
PHE   CG  CD1  doub Y N 300 
PHE   CG  CD2  sing Y N 301 
PHE   CD1 CE1  sing Y N 302 
PHE   CD1 HD1  sing N N 303 
PHE   CD2 CE2  doub Y N 304 
PHE   CD2 HD2  sing N N 305 
PHE   CE1 CZ   doub Y N 306 
PHE   CE1 HE1  sing N N 307 
PHE   CE2 CZ   sing Y N 308 
PHE   CE2 HE2  sing N N 309 
PHE   CZ  HZ   sing N N 310 
PHE   OXT HXT  sing N N 311 
PRO   N   CA   sing N N 312 
PRO   N   CD   sing N N 313 
PRO   N   H    sing N N 314 
PRO   CA  C    sing N N 315 
PRO   CA  CB   sing N N 316 
PRO   CA  HA   sing N N 317 
PRO   C   O    doub N N 318 
PRO   C   OXT  sing N N 319 
PRO   CB  CG   sing N N 320 
PRO   CB  HB2  sing N N 321 
PRO   CB  HB3  sing N N 322 
PRO   CG  CD   sing N N 323 
PRO   CG  HG2  sing N N 324 
PRO   CG  HG3  sing N N 325 
PRO   CD  HD2  sing N N 326 
PRO   CD  HD3  sing N N 327 
PRO   OXT HXT  sing N N 328 
SER   N   CA   sing N N 329 
SER   N   H    sing N N 330 
SER   N   H2   sing N N 331 
SER   CA  C    sing N N 332 
SER   CA  CB   sing N N 333 
SER   CA  HA   sing N N 334 
SER   C   O    doub N N 335 
SER   C   OXT  sing N N 336 
SER   CB  OG   sing N N 337 
SER   CB  HB2  sing N N 338 
SER   CB  HB3  sing N N 339 
SER   OG  HG   sing N N 340 
SER   OXT HXT  sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_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                    8XUE 
_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]   0.013005 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002475 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011930 
_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]   0.016505 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
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   ? 22.761  -5.180  86.460  1.00 59.09  ? 35  LYS   A N   1 
ATOM   2    C  CA  . LYS   A 1 7   ? 23.701  -6.108  85.836  1.00 59.83  ? 35  LYS   A CA  1 
ATOM   3    C  C   . LYS   A 1 7   ? 23.240  -6.502  84.434  1.00 58.93  ? 35  LYS   A C   1 
ATOM   4    O  O   . LYS   A 1 7   ? 22.050  -6.706  84.188  1.00 54.22  ? 35  LYS   A O   1 
ATOM   5    C  CB  . LYS   A 1 7   ? 23.882  -7.361  86.706  1.00 59.31  ? 35  LYS   A CB  1 
ATOM   6    N  N   . ASN   A 1 8   ? 24.192  -6.595  83.508  1.00 56.41  ? 36  ASN   A N   1 
ATOM   7    C  CA  . ASN   A 1 8   ? 23.905  -6.961  82.122  1.00 53.98  ? 36  ASN   A CA  1 
ATOM   8    C  C   . ASN   A 1 8   ? 25.056  -7.833  81.640  1.00 53.36  ? 36  ASN   A C   1 
ATOM   9    O  O   . ASN   A 1 8   ? 26.085  -7.297  81.188  1.00 57.58  ? 36  ASN   A O   1 
ATOM   10   C  CB  . ASN   A 1 8   ? 23.726  -5.736  81.219  1.00 55.49  ? 36  ASN   A CB  1 
ATOM   11   C  CG  . ASN   A 1 8   ? 23.481  -6.109  79.751  1.00 52.03  ? 36  ASN   A CG  1 
ATOM   12   O  OD1 . ASN   A 1 8   ? 23.443  -7.299  79.389  1.00 48.34  ? 36  ASN   A OD1 1 
ATOM   13   N  ND2 . ASN   A 1 8   ? 23.283  -5.101  78.911  1.00 49.97  ? 36  ASN   A ND2 1 
ATOM   14   N  N   . PRO   A 1 9   ? 24.911  -9.168  81.681  1.00 48.04  ? 37  PRO   A N   1 
ATOM   15   C  CA  . PRO   A 1 9   ? 25.989  -10.047 81.214  1.00 48.65  ? 37  PRO   A CA  1 
ATOM   16   C  C   . PRO   A 1 9   ? 26.198  -10.021 79.708  1.00 52.04  ? 37  PRO   A C   1 
ATOM   17   O  O   . PRO   A 1 9   ? 27.228  -10.530 79.245  1.00 55.25  ? 37  PRO   A O   1 
ATOM   18   C  CB  . PRO   A 1 9   ? 25.575  -11.420 81.699  1.00 49.19  ? 37  PRO   A CB  1 
ATOM   19   C  CG  . PRO   A 1 9   ? 24.278  -11.232 82.493  1.00 55.37  ? 37  PRO   A CG  1 
ATOM   20   C  CD  . PRO   A 1 9   ? 23.729  -9.905  82.094  1.00 50.47  ? 37  PRO   A CD  1 
ATOM   21   N  N   . LYS   A 1 10  ? 25.253  -9.490  78.931  1.00 51.80  ? 38  LYS   A N   1 
ATOM   22   C  CA  . LYS   A 1 10  ? 25.364  -9.398  77.473  1.00 48.21  ? 38  LYS   A CA  1 
ATOM   23   C  C   . LYS   A 1 10  ? 25.655  -10.761 76.845  1.00 46.16  ? 38  LYS   A C   1 
ATOM   24   O  O   . LYS   A 1 10  ? 26.631  -10.938 76.109  1.00 50.82  ? 38  LYS   A O   1 
ATOM   25   C  CB  . LYS   A 1 10  ? 26.431  -8.377  77.078  1.00 48.36  ? 38  LYS   A CB  1 
ATOM   26   C  CG  . LYS   A 1 10  ? 26.263  -7.053  77.820  1.00 56.89  ? 38  LYS   A CG  1 
ATOM   27   C  CD  . LYS   A 1 10  ? 26.964  -5.887  77.148  1.00 53.35  ? 38  LYS   A CD  1 
ATOM   28   C  CE  . LYS   A 1 10  ? 26.705  -4.609  77.931  1.00 53.63  ? 38  LYS   A CE  1 
ATOM   29   N  NZ  . LYS   A 1 10  ? 26.984  -3.395  77.121  1.00 54.03  ? 38  LYS   A NZ  1 
ATOM   30   N  N   . SER   A 1 11  ? 24.765  -11.720 77.095  1.00 47.59  ? 39  SER   A N   1 
ATOM   31   C  CA  . SER   A 1 11  ? 24.972  -13.101 76.687  1.00 42.63  ? 39  SER   A CA  1 
ATOM   32   C  C   . SER   A 1 11  ? 24.266  -13.472 75.390  1.00 42.71  ? 39  SER   A C   1 
ATOM   33   O  O   . SER   A 1 11  ? 24.101  -14.664 75.124  1.00 40.67  ? 39  SER   A O   1 
ATOM   34   C  CB  . SER   A 1 11  ? 24.523  -14.050 77.799  1.00 42.77  ? 39  SER   A CB  1 
ATOM   35   O  OG  . SER   A 1 11  ? 23.383  -13.555 78.473  1.00 40.06  ? 39  SER   A OG  1 
ATOM   36   N  N   . ASP   A 1 12  ? 23.831  -12.501 74.583  1.00 47.52  ? 40  ASP   A N   1 
ATOM   37   C  CA  . ASP   A 1 12  ? 23.133  -12.845 73.341  1.00 42.04  ? 40  ASP   A CA  1 
ATOM   38   C  C   . ASP   A 1 12  ? 23.942  -13.874 72.571  1.00 42.60  ? 40  ASP   A C   1 
ATOM   39   O  O   . ASP   A 1 12  ? 25.120  -13.649 72.275  1.00 39.15  ? 40  ASP   A O   1 
ATOM   40   C  CB  . ASP   A 1 12  ? 22.922  -11.608 72.466  1.00 37.25  ? 40  ASP   A CB  1 
ATOM   41   C  CG  . ASP   A 1 12  ? 21.849  -10.673 72.995  1.00 36.16  ? 40  ASP   A CG  1 
ATOM   42   O  OD1 . ASP   A 1 12  ? 21.275  -10.893 74.087  1.00 33.85  ? 40  ASP   A OD1 1 
ATOM   43   O  OD2 . ASP   A 1 12  ? 21.616  -9.665  72.315  1.00 39.68  ? 40  ASP   A OD2 1 
ATOM   44   N  N   . LYS   A 1 13  ? 23.317  -15.020 72.275  1.00 37.22  ? 41  LYS   A N   1 
ATOM   45   C  CA  . LYS   A 1 13  ? 23.998  -16.073 71.535  1.00 39.02  ? 41  LYS   A CA  1 
ATOM   46   C  C   . LYS   A 1 13  ? 24.183  -15.710 70.072  1.00 42.07  ? 41  LYS   A C   1 
ATOM   47   O  O   . LYS   A 1 13  ? 24.918  -16.410 69.366  1.00 45.04  ? 41  LYS   A O   1 
ATOM   48   C  CB  . LYS   A 1 13  ? 23.223  -17.387 71.650  1.00 42.15  ? 41  LYS   A CB  1 
ATOM   49   C  CG  . LYS   A 1 13  ? 22.806  -17.726 73.066  1.00 42.72  ? 41  LYS   A CG  1 
ATOM   50   C  CD  . LYS   A 1 13  ? 23.345  -19.073 73.495  1.00 51.45  ? 41  LYS   A CD  1 
ATOM   51   C  CE  . LYS   A 1 13  ? 23.179  -19.298 75.002  1.00 53.47  ? 41  LYS   A CE  1 
ATOM   52   N  NZ  . LYS   A 1 13  ? 22.371  -20.521 75.300  1.00 41.24  ? 41  LYS   A NZ  1 
ATOM   53   N  N   . PHE   A 1 14  ? 23.542  -14.641 69.606  1.00 37.75  ? 42  PHE   A N   1 
ATOM   54   C  CA  . PHE   A 1 14  ? 23.723  -14.175 68.238  1.00 38.33  ? 42  PHE   A CA  1 
ATOM   55   C  C   . PHE   A 1 14  ? 23.435  -12.687 68.211  1.00 37.94  ? 42  PHE   A C   1 
ATOM   56   O  O   . PHE   A 1 14  ? 22.872  -12.130 69.155  1.00 44.85  ? 42  PHE   A O   1 
ATOM   57   C  CB  . PHE   A 1 14  ? 22.834  -14.946 67.257  1.00 42.61  ? 42  PHE   A CB  1 
ATOM   58   C  CG  . PHE   A 1 14  ? 21.458  -15.223 67.774  1.00 42.19  ? 42  PHE   A CG  1 
ATOM   59   C  CD1 . PHE   A 1 14  ? 20.448  -14.281 67.629  1.00 38.43  ? 42  PHE   A CD1 1 
ATOM   60   C  CD2 . PHE   A 1 14  ? 21.166  -16.436 68.393  1.00 39.19  ? 42  PHE   A CD2 1 
ATOM   61   C  CE1 . PHE   A 1 14  ? 19.167  -14.535 68.091  1.00 38.03  ? 42  PHE   A CE1 1 
ATOM   62   C  CE2 . PHE   A 1 14  ? 19.878  -16.704 68.863  1.00 42.47  ? 42  PHE   A CE2 1 
ATOM   63   C  CZ  . PHE   A 1 14  ? 18.873  -15.747 68.707  1.00 37.98  ? 42  PHE   A CZ  1 
ATOM   64   N  N   . LYS   A 1 15  ? 23.858  -12.033 67.134  1.00 37.43  ? 43  LYS   A N   1 
ATOM   65   C  CA  . LYS   A 1 15  ? 23.801  -10.574 67.101  1.00 42.47  ? 43  LYS   A CA  1 
ATOM   66   C  C   . LYS   A 1 15  ? 22.381  -10.145 66.755  1.00 40.80  ? 43  LYS   A C   1 
ATOM   67   O  O   . LYS   A 1 15  ? 21.919  -10.345 65.626  1.00 39.61  ? 43  LYS   A O   1 
ATOM   68   C  CB  . LYS   A 1 15  ? 24.807  -10.000 66.108  1.00 38.81  ? 43  LYS   A CB  1 
ATOM   69   N  N   . VAL   A 1 16  ? 21.700  -9.548  67.726  1.00 43.03  ? 44  VAL   A N   1 
ATOM   70   C  CA  . VAL   A 1 16  ? 20.339  -9.049  67.573  1.00 43.23  ? 44  VAL   A CA  1 
ATOM   71   C  C   . VAL   A 1 16  ? 20.401  -7.540  67.394  1.00 45.84  ? 44  VAL   A C   1 
ATOM   72   O  O   . VAL   A 1 16  ? 21.093  -6.848  68.151  1.00 50.33  ? 44  VAL   A O   1 
ATOM   73   C  CB  . VAL   A 1 16  ? 19.483  -9.424  68.794  1.00 42.69  ? 44  VAL   A CB  1 
ATOM   74   C  CG1 . VAL   A 1 16  ? 18.136  -8.684  68.775  1.00 38.44  ? 44  VAL   A CG1 1 
ATOM   75   C  CG2 . VAL   A 1 16  ? 19.313  -10.948 68.873  1.00 36.22  ? 44  VAL   A CG2 1 
ATOM   76   N  N   . LYS   A 1 17  ? 19.674  -7.021  66.404  1.00 40.77  ? 45  LYS   A N   1 
ATOM   77   C  CA  . LYS   A 1 17  ? 19.682  -5.584  66.180  1.00 42.94  ? 45  LYS   A CA  1 
ATOM   78   C  C   . LYS   A 1 17  ? 18.488  -4.914  66.861  1.00 44.67  ? 45  LYS   A C   1 
ATOM   79   O  O   . LYS   A 1 17  ? 18.638  -4.396  67.971  1.00 48.03  ? 45  LYS   A O   1 
ATOM   80   C  CB  . LYS   A 1 17  ? 19.760  -5.303  64.674  1.00 41.79  ? 45  LYS   A CB  1 
ATOM   81   C  CG  . LYS   A 1 17  ? 21.135  -5.692  64.109  1.00 42.20  ? 45  LYS   A CG  1 
ATOM   82   C  CD  . LYS   A 1 17  ? 21.203  -5.665  62.595  1.00 45.94  ? 45  LYS   A CD  1 
ATOM   83   C  CE  . LYS   A 1 17  ? 20.883  -4.274  62.063  1.00 54.95  ? 45  LYS   A CE  1 
ATOM   84   N  NZ  . LYS   A 1 17  ? 21.098  -4.180  60.582  1.00 55.25  ? 45  LYS   A NZ  1 
ATOM   85   N  N   . ARG   A 1 18  ? 17.304  -4.911  66.246  1.00 41.07  ? 46  ARG   A N   1 
ATOM   86   C  CA  . ARG   A 1 18  ? 16.134  -4.342  66.906  1.00 35.85  ? 46  ARG   A CA  1 
ATOM   87   C  C   . ARG   A 1 18  ? 14.865  -5.034  66.452  1.00 36.67  ? 46  ARG   A C   1 
ATOM   88   O  O   . ARG   A 1 18  ? 14.863  -5.900  65.568  1.00 35.98  ? 46  ARG   A O   1 
ATOM   89   C  CB  . ARG   A 1 18  ? 15.970  -2.837  66.655  1.00 37.54  ? 46  ARG   A CB  1 
ATOM   90   C  CG  . ARG   A 1 18  ? 16.463  -1.981  67.834  1.00 48.56  ? 46  ARG   A CG  1 
ATOM   91   C  CD  . ARG   A 1 18  ? 17.556  -1.082  67.362  1.00 42.58  ? 46  ARG   A CD  1 
ATOM   92   N  NE  . ARG   A 1 18  ? 18.337  -0.354  68.370  1.00 56.98  ? 46  ARG   A NE  1 
ATOM   93   C  CZ  . ARG   A 1 18  ? 19.311  -0.858  69.114  1.00 53.58  ? 46  ARG   A CZ  1 
ATOM   94   N  NH1 . ARG   A 1 18  ? 19.628  -2.148  69.007  1.00 43.16  ? 46  ARG   A NH1 1 
ATOM   95   N  NH2 . ARG   A 1 18  ? 19.974  -0.070  69.937  1.00 57.28  ? 46  ARG   A NH2 1 
ATOM   96   N  N   . PHE   A 1 19  ? 13.777  -4.619  67.094  1.00 35.44  ? 47  PHE   A N   1 
ATOM   97   C  CA  . PHE   A 1 19  ? 12.440  -4.937  66.632  1.00 30.97  ? 47  PHE   A CA  1 
ATOM   98   C  C   . PHE   A 1 19  ? 12.300  -4.513  65.182  1.00 33.92  ? 47  PHE   A C   1 
ATOM   99   O  O   . PHE   A 1 19  ? 12.602  -3.374  64.820  1.00 32.52  ? 47  PHE   A O   1 
ATOM   100  C  CB  . PHE   A 1 19  ? 11.412  -4.238  67.517  1.00 29.14  ? 47  PHE   A CB  1 
ATOM   101  C  CG  . PHE   A 1 19  ? 11.143  -4.964  68.817  1.00 29.09  ? 47  PHE   A CG  1 
ATOM   102  C  CD1 . PHE   A 1 19  ? 10.783  -6.306  68.813  1.00 27.30  ? 47  PHE   A CD1 1 
ATOM   103  C  CD2 . PHE   A 1 19  ? 11.227  -4.301  70.032  1.00 28.76  ? 47  PHE   A CD2 1 
ATOM   104  C  CE1 . PHE   A 1 19  ? 10.515  -6.988  69.994  1.00 24.80  ? 47  PHE   A CE1 1 
ATOM   105  C  CE2 . PHE   A 1 19  ? 10.971  -4.973  71.226  1.00 30.55  ? 47  PHE   A CE2 1 
ATOM   106  C  CZ  . PHE   A 1 19  ? 10.614  -6.323  71.205  1.00 26.62  ? 47  PHE   A CZ  1 
ATOM   107  N  N   . HIS   A 1 20  ? 11.894  -5.458  64.336  1.00 34.16  ? 48  HIS   A N   1 
ATOM   108  C  CA  . HIS   A 1 20  ? 11.731  -5.180  62.917  1.00 31.72  ? 48  HIS   A CA  1 
ATOM   109  C  C   . HIS   A 1 20  ? 10.265  -4.992  62.515  1.00 38.17  ? 48  HIS   A C   1 
ATOM   110  O  O   . HIS   A 1 20  ? 9.934   -4.018  61.830  1.00 36.26  ? 48  HIS   A O   1 
ATOM   111  C  CB  . HIS   A 1 20  ? 12.379  -6.292  62.097  1.00 28.92  ? 48  HIS   A CB  1 
ATOM   112  C  CG  . HIS   A 1 20  ? 12.419  -5.994  60.636  1.00 39.27  ? 48  HIS   A CG  1 
ATOM   113  N  ND1 . HIS   A 1 20  ? 11.510  -6.526  59.747  1.00 39.73  ? 48  HIS   A ND1 1 
ATOM   114  C  CD2 . HIS   A 1 20  ? 13.233  -5.191  59.908  1.00 44.46  ? 48  HIS   A CD2 1 
ATOM   115  C  CE1 . HIS   A 1 20  ? 11.763  -6.068  58.535  1.00 42.37  ? 48  HIS   A CE1 1 
ATOM   116  N  NE2 . HIS   A 1 20  ? 12.806  -5.258  58.603  1.00 50.22  ? 48  HIS   A NE2 1 
ATOM   117  N  N   . HIS   A 1 21  ? 9.374   -5.893  62.930  1.00 32.57  ? 49  HIS   A N   1 
ATOM   118  C  CA  . HIS   A 1 21  ? 7.953   -5.763  62.607  1.00 34.24  ? 49  HIS   A CA  1 
ATOM   119  C  C   . HIS   A 1 21  ? 7.154   -6.738  63.457  1.00 37.08  ? 49  HIS   A C   1 
ATOM   120  O  O   . HIS   A 1 21  ? 7.702   -7.684  64.041  1.00 35.15  ? 49  HIS   A O   1 
ATOM   121  C  CB  . HIS   A 1 21  ? 7.659   -6.001  61.117  1.00 37.12  ? 49  HIS   A CB  1 
ATOM   122  C  CG  . HIS   A 1 21  ? 7.770   -7.433  60.676  1.00 39.91  ? 49  HIS   A CG  1 
ATOM   123  N  ND1 . HIS   A 1 21  ? 8.953   -7.988  60.233  1.00 35.40  ? 49  HIS   A ND1 1 
ATOM   124  C  CD2 . HIS   A 1 21  ? 6.837   -8.413  60.575  1.00 34.31  ? 49  HIS   A CD2 1 
ATOM   125  C  CE1 . HIS   A 1 21  ? 8.747   -9.248  59.887  1.00 32.00  ? 49  HIS   A CE1 1 
ATOM   126  N  NE2 . HIS   A 1 21  ? 7.478   -9.537  60.108  1.00 32.50  ? 49  HIS   A NE2 1 
ATOM   127  N  N   . ILE   A 1 22  ? 5.848   -6.476  63.533  1.00 33.46  ? 50  ILE   A N   1 
ATOM   128  C  CA  . ILE   A 1 22  ? 4.897   -7.324  64.237  1.00 27.71  ? 50  ILE   A CA  1 
ATOM   129  C  C   . ILE   A 1 22  ? 3.853   -7.764  63.225  1.00 29.59  ? 50  ILE   A C   1 
ATOM   130  O  O   . ILE   A 1 22  ? 3.326   -6.932  62.478  1.00 31.00  ? 50  ILE   A O   1 
ATOM   131  C  CB  . ILE   A 1 22  ? 4.234   -6.579  65.412  1.00 27.98  ? 50  ILE   A CB  1 
ATOM   132  C  CG1 . ILE   A 1 22  ? 5.259   -6.209  66.479  1.00 28.51  ? 50  ILE   A CG1 1 
ATOM   133  C  CG2 . ILE   A 1 22  ? 3.145   -7.434  66.047  1.00 27.23  ? 50  ILE   A CG2 1 
ATOM   134  C  CD1 . ILE   A 1 22  ? 5.944   -7.425  67.135  1.00 32.78  ? 50  ILE   A CD1 1 
ATOM   135  N  N   . GLU   A 1 23  ? 3.551   -9.058  63.188  1.00 25.18  ? 51  GLU   A N   1 
ATOM   136  C  CA  . GLU   A 1 23  ? 2.571   -9.567  62.232  1.00 29.01  ? 51  GLU   A CA  1 
ATOM   137  C  C   . GLU   A 1 23  ? 1.330   -10.066 62.945  1.00 30.10  ? 51  GLU   A C   1 
ATOM   138  O  O   . GLU   A 1 23  ? 1.416   -10.944 63.813  1.00 27.16  ? 51  GLU   A O   1 
ATOM   139  C  CB  . GLU   A 1 23  ? 3.113   -10.682 61.354  1.00 27.75  ? 51  GLU   A CB  1 
ATOM   140  C  CG  . GLU   A 1 23  ? 2.062   -11.103 60.340  1.00 23.50  ? 51  GLU   A CG  1 
ATOM   141  C  CD  . GLU   A 1 23  ? 2.572   -12.156 59.398  1.00 27.59  ? 51  GLU   A CD  1 
ATOM   142  O  OE1 . GLU   A 1 23  ? 3.677   -12.695 59.678  1.00 26.36  ? 51  GLU   A OE1 1 
ATOM   143  O  OE2 . GLU   A 1 23  ? 1.880   -12.449 58.390  1.00 23.94  ? 51  GLU   A OE2 1 
ATOM   144  N  N   . PHE   A 1 24  ? 0.187   -9.507  62.562  1.00 26.96  ? 52  PHE   A N   1 
ATOM   145  C  CA  . PHE   A 1 24  ? -1.114  -9.956  63.025  1.00 24.65  ? 52  PHE   A CA  1 
ATOM   146  C  C   . PHE   A 1 24  ? -1.647  -10.959 62.027  1.00 25.80  ? 52  PHE   A C   1 
ATOM   147  O  O   . PHE   A 1 24  ? -1.627  -10.704 60.816  1.00 25.99  ? 52  PHE   A O   1 
ATOM   148  C  CB  . PHE   A 1 24  ? -2.108  -8.792  63.130  1.00 24.03  ? 52  PHE   A CB  1 
ATOM   149  C  CG  . PHE   A 1 24  ? -1.754  -7.781  64.169  1.00 25.01  ? 52  PHE   A CG  1 
ATOM   150  C  CD1 . PHE   A 1 24  ? -0.789  -6.820  63.916  1.00 24.41  ? 52  PHE   A CD1 1 
ATOM   151  C  CD2 . PHE   A 1 24  ? -2.393  -7.783  65.394  1.00 26.69  ? 52  PHE   A CD2 1 
ATOM   152  C  CE1 . PHE   A 1 24  ? -0.437  -5.907  64.878  1.00 25.01  ? 52  PHE   A CE1 1 
ATOM   153  C  CE2 . PHE   A 1 24  ? -2.064  -6.858  66.353  1.00 27.35  ? 52  PHE   A CE2 1 
ATOM   154  C  CZ  . PHE   A 1 24  ? -1.073  -5.919  66.098  1.00 25.41  ? 52  PHE   A CZ  1 
ATOM   155  N  N   . TRP   A 1 25  ? -2.161  -12.070 62.528  1.00 24.11  ? 53  TRP   A N   1 
ATOM   156  C  CA  . TRP   A 1 25  ? -2.881  -13.011 61.689  1.00 29.85  ? 53  TRP   A CA  1 
ATOM   157  C  C   . TRP   A 1 25  ? -4.366  -12.705 61.845  1.00 25.30  ? 53  TRP   A C   1 
ATOM   158  O  O   . TRP   A 1 25  ? -4.886  -12.688 62.965  1.00 28.54  ? 53  TRP   A O   1 
ATOM   159  C  CB  . TRP   A 1 25  ? -2.519  -14.459 62.049  1.00 25.54  ? 53  TRP   A CB  1 
ATOM   160  C  CG  . TRP   A 1 25  ? -1.425  -14.971 61.134  1.00 30.34  ? 53  TRP   A CG  1 
ATOM   161  C  CD1 . TRP   A 1 25  ? -0.771  -14.251 60.169  1.00 30.05  ? 53  TRP   A CD1 1 
ATOM   162  C  CD2 . TRP   A 1 25  ? -0.868  -16.297 61.090  1.00 27.28  ? 53  TRP   A CD2 1 
ATOM   163  N  NE1 . TRP   A 1 25  ? 0.151   -15.051 59.521  1.00 25.70  ? 53  TRP   A NE1 1 
ATOM   164  C  CE2 . TRP   A 1 25  ? 0.109   -16.308 60.067  1.00 28.68  ? 53  TRP   A CE2 1 
ATOM   165  C  CE3 . TRP   A 1 25  ? -1.098  -17.474 61.814  1.00 29.75  ? 53  TRP   A CE3 1 
ATOM   166  C  CZ2 . TRP   A 1 25  ? 0.870   -17.453 59.763  1.00 29.08  ? 53  TRP   A CZ2 1 
ATOM   167  C  CZ3 . TRP   A 1 25  ? -0.348  -18.615 61.500  1.00 30.76  ? 53  TRP   A CZ3 1 
ATOM   168  C  CH2 . TRP   A 1 25  ? 0.618   -18.592 60.483  1.00 30.03  ? 53  TRP   A CH2 1 
ATOM   169  N  N   . CYS   A 1 26  ? -5.028  -12.404 60.735  1.00 29.75  ? 54  CYS   A N   1 
ATOM   170  C  CA  . CYS   A 1 26  ? -6.423  -11.962 60.710  1.00 28.46  ? 54  CYS   A CA  1 
ATOM   171  C  C   . CYS   A 1 26  ? -7.260  -12.880 59.832  1.00 30.27  ? 54  CYS   A C   1 
ATOM   172  O  O   . CYS   A 1 26  ? -6.742  -13.717 59.089  1.00 30.23  ? 54  CYS   A O   1 
ATOM   173  C  CB  . CYS   A 1 26  ? -6.543  -10.538 60.155  1.00 25.93  ? 54  CYS   A CB  1 
ATOM   174  S  SG  . CYS   A 1 26  ? -5.144  -9.505  60.532  1.00 40.80  ? 54  CYS   A SG  1 
ATOM   175  N  N   . GLY   A 1 27  ? -8.569  -12.680 59.884  1.00 28.67  ? 55  GLY   A N   1 
ATOM   176  C  CA  . GLY   A 1 27  ? -9.422  -13.282 58.883  1.00 28.46  ? 55  GLY   A CA  1 
ATOM   177  C  C   . GLY   A 1 27  ? -9.626  -12.386 57.676  1.00 30.42  ? 55  GLY   A C   1 
ATOM   178  O  O   . GLY   A 1 27  ? -9.715  -12.848 56.531  1.00 31.38  ? 55  GLY   A O   1 
ATOM   179  N  N   . ASP   A 1 28  ? -9.693  -11.083 57.908  1.00 30.03  ? 56  ASP   A N   1 
ATOM   180  C  CA  . ASP   A 1 28  ? -9.680  -10.128 56.810  1.00 29.35  ? 56  ASP   A CA  1 
ATOM   181  C  C   . ASP   A 1 28  ? -8.626  -9.071  57.111  1.00 28.03  ? 56  ASP   A C   1 
ATOM   182  O  O   . ASP   A 1 28  ? -8.751  -8.330  58.092  1.00 28.71  ? 56  ASP   A O   1 
ATOM   183  C  CB  . ASP   A 1 28  ? -11.066 -9.511  56.605  1.00 22.57  ? 56  ASP   A CB  1 
ATOM   184  C  CG  . ASP   A 1 28  ? -11.121 -8.642  55.390  1.00 28.05  ? 56  ASP   A CG  1 
ATOM   185  O  OD1 . ASP   A 1 28  ? -11.343 -9.193  54.287  1.00 28.00  ? 56  ASP   A OD1 1 
ATOM   186  O  OD2 . ASP   A 1 28  ? -10.945 -7.416  55.534  1.00 26.40  ? 56  ASP   A OD2 1 
ATOM   187  N  N   . ALA   A 1 29  ? -7.586  -8.994  56.272  1.00 27.24  ? 57  ALA   A N   1 
ATOM   188  C  CA  . ALA   A 1 29  ? -6.470  -8.106  56.587  1.00 25.79  ? 57  ALA   A CA  1 
ATOM   189  C  C   . ALA   A 1 29  ? -6.794  -6.653  56.278  1.00 26.45  ? 57  ALA   A C   1 
ATOM   190  O  O   . ALA   A 1 29  ? -6.328  -5.749  56.976  1.00 33.14  ? 57  ALA   A O   1 
ATOM   191  C  CB  . ALA   A 1 29  ? -5.215  -8.535  55.825  1.00 26.56  ? 57  ALA   A CB  1 
ATOM   192  N  N   . THR   A 1 30  ? -7.573  -6.422  55.232  1.00 30.08  ? 58  THR   A N   1 
ATOM   193  C  CA  . THR   A 1 30  ? -7.979  -5.078  54.848  1.00 24.70  ? 58  THR   A CA  1 
ATOM   194  C  C   . THR   A 1 30  ? -8.669  -4.347  55.993  1.00 30.14  ? 58  THR   A C   1 
ATOM   195  O  O   . THR   A 1 30  ? -8.267  -3.231  56.379  1.00 25.27  ? 58  THR   A O   1 
ATOM   196  C  CB  . THR   A 1 30  ? -8.903  -5.192  53.648  1.00 23.03  ? 58  THR   A CB  1 
ATOM   197  O  OG1 . THR   A 1 30  ? -8.159  -5.797  52.575  1.00 26.70  ? 58  THR   A OG1 1 
ATOM   198  C  CG2 . THR   A 1 30  ? -9.466  -3.826  53.220  1.00 21.78  ? 58  THR   A CG2 1 
ATOM   199  N  N   . ASN   A 1 31  ? -9.718  -4.954  56.550  1.00 23.87  ? 59  ASN   A N   1 
ATOM   200  C  CA  . ASN   A 1 31  ? -10.513 -4.239  57.544  1.00 24.96  ? 59  ASN   A CA  1 
ATOM   201  C  C   . ASN   A 1 31  ? -9.719  -3.950  58.814  1.00 24.82  ? 59  ASN   A C   1 
ATOM   202  O  O   . ASN   A 1 31  ? -9.776  -2.833  59.342  1.00 22.22  ? 59  ASN   A O   1 
ATOM   203  C  CB  . ASN   A 1 31  ? -11.792 -5.010  57.838  1.00 21.47  ? 59  ASN   A CB  1 
ATOM   204  C  CG  . ASN   A 1 31  ? -12.854 -4.720  56.795  1.00 24.01  ? 59  ASN   A CG  1 
ATOM   205  O  OD1 . ASN   A 1 31  ? -13.671 -3.826  56.973  1.00 24.60  ? 59  ASN   A OD1 1 
ATOM   206  N  ND2 . ASN   A 1 31  ? -12.777 -5.403  55.660  1.00 22.26  ? 59  ASN   A ND2 1 
ATOM   207  N  N   . VAL   A 1 32  ? -8.988  -4.941  59.335  1.00 24.02  ? 60  VAL   A N   1 
ATOM   208  C  CA  . VAL   A 1 32  ? -8.151  -4.689  60.505  1.00 20.05  ? 60  VAL   A CA  1 
ATOM   209  C  C   . VAL   A 1 32  ? -7.129  -3.613  60.196  1.00 21.29  ? 60  VAL   A C   1 
ATOM   210  O  O   . VAL   A 1 32  ? -6.882  -2.710  61.004  1.00 22.22  ? 60  VAL   A O   1 
ATOM   211  C  CB  . VAL   A 1 32  ? -7.454  -5.978  60.981  1.00 24.34  ? 60  VAL   A CB  1 
ATOM   212  C  CG1 . VAL   A 1 32  ? -6.648  -5.681  62.218  1.00 21.16  ? 60  VAL   A CG1 1 
ATOM   213  C  CG2 . VAL   A 1 32  ? -8.480  -7.112  61.260  1.00 22.43  ? 60  VAL   A CG2 1 
ATOM   214  N  N   . ALA   A 1 33  ? -6.481  -3.717  59.042  1.00 22.45  ? 61  ALA   A N   1 
ATOM   215  C  CA  . ALA   A 1 33  ? -5.407  -2.780  58.765  1.00 25.70  ? 61  ALA   A CA  1 
ATOM   216  C  C   . ALA   A 1 33  ? -5.967  -1.368  58.636  1.00 29.94  ? 61  ALA   A C   1 
ATOM   217  O  O   . ALA   A 1 33  ? -5.474  -0.428  59.280  1.00 24.33  ? 61  ALA   A O   1 
ATOM   218  C  CB  . ALA   A 1 33  ? -4.639  -3.213  57.512  1.00 24.44  ? 61  ALA   A CB  1 
ATOM   219  N  N   . ARG   A 1 34  ? -7.037  -1.209  57.849  1.00 28.88  ? 62  ARG   A N   1 
ATOM   220  C  CA  . ARG   A 1 34  ? -7.650  0.110   57.720  1.00 24.46  ? 62  ARG   A CA  1 
ATOM   221  C  C   . ARG   A 1 34  ? -8.069  0.657   59.078  1.00 27.07  ? 62  ARG   A C   1 
ATOM   222  O  O   . ARG   A 1 34  ? -7.858  1.844   59.362  1.00 26.80  ? 62  ARG   A O   1 
ATOM   223  C  CB  . ARG   A 1 34  ? -8.825  0.045   56.751  1.00 25.65  ? 62  ARG   A CB  1 
ATOM   224  C  CG  . ARG   A 1 34  ? -8.341  -0.269  55.352  1.00 28.87  ? 62  ARG   A CG  1 
ATOM   225  C  CD  . ARG   A 1 34  ? -9.115  0.439   54.246  1.00 29.39  ? 62  ARG   A CD  1 
ATOM   226  N  NE  . ARG   A 1 34  ? -8.417  0.246   52.979  1.00 32.12  ? 62  ARG   A NE  1 
ATOM   227  C  CZ  . ARG   A 1 34  ? -8.574  1.002   51.896  1.00 37.27  ? 62  ARG   A CZ  1 
ATOM   228  N  NH1 . ARG   A 1 34  ? -7.874  0.728   50.804  1.00 33.96  ? 62  ARG   A NH1 1 
ATOM   229  N  NH2 . ARG   A 1 34  ? -9.419  2.032   51.898  1.00 32.98  ? 62  ARG   A NH2 1 
ATOM   230  N  N   . ARG   A 1 35  ? -8.603  -0.200  59.958  1.00 23.83  ? 63  ARG   A N   1 
ATOM   231  C  CA  . ARG   A 1 35  ? -8.976  0.269   61.294  1.00 22.05  ? 63  ARG   A CA  1 
ATOM   232  C  C   . ARG   A 1 35  ? -7.743  0.717   62.066  1.00 25.58  ? 63  ARG   A C   1 
ATOM   233  O  O   . ARG   A 1 35  ? -7.723  1.810   62.650  1.00 23.34  ? 63  ARG   A O   1 
ATOM   234  C  CB  . ARG   A 1 35  ? -9.737  -0.833  62.047  1.00 24.74  ? 63  ARG   A CB  1 
ATOM   235  C  CG  . ARG   A 1 35  ? -10.493 -0.404  63.348  1.00 21.59  ? 63  ARG   A CG  1 
ATOM   236  C  CD  . ARG   A 1 35  ? -9.561  -0.247  64.546  1.00 26.24  ? 63  ARG   A CD  1 
ATOM   237  N  NE  . ARG   A 1 35  ? -10.232 -0.018  65.825  1.00 22.95  ? 63  ARG   A NE  1 
ATOM   238  C  CZ  . ARG   A 1 35  ? -10.289 -0.915  66.804  1.00 26.20  ? 63  ARG   A CZ  1 
ATOM   239  N  NH1 . ARG   A 1 35  ? -10.903 -0.619  67.944  1.00 26.41  ? 63  ARG   A NH1 1 
ATOM   240  N  NH2 . ARG   A 1 35  ? -9.746  -2.117  66.636  1.00 20.30  ? 63  ARG   A NH2 1 
ATOM   241  N  N   . PHE   A 1 36  ? -6.689  -0.101  62.045  1.00 21.55  ? 64  PHE   A N   1 
ATOM   242  C  CA  . PHE   A 1 36  ? -5.483  0.218   62.798  1.00 25.64  ? 64  PHE   A CA  1 
ATOM   243  C  C   . PHE   A 1 36  ? -4.839  1.489   62.281  1.00 23.76  ? 64  PHE   A C   1 
ATOM   244  O  O   . PHE   A 1 36  ? -4.331  2.298   63.063  1.00 29.05  ? 64  PHE   A O   1 
ATOM   245  C  CB  . PHE   A 1 36  ? -4.489  -0.943  62.710  1.00 20.27  ? 64  PHE   A CB  1 
ATOM   246  C  CG  . PHE   A 1 36  ? -4.695  -1.979  63.770  1.00 26.53  ? 64  PHE   A CG  1 
ATOM   247  C  CD1 . PHE   A 1 36  ? -5.905  -2.673  63.856  1.00 21.83  ? 64  PHE   A CD1 1 
ATOM   248  C  CD2 . PHE   A 1 36  ? -3.696  -2.256  64.687  1.00 24.01  ? 64  PHE   A CD2 1 
ATOM   249  C  CE1 . PHE   A 1 36  ? -6.120  -3.577  64.838  1.00 18.92  ? 64  PHE   A CE1 1 
ATOM   250  C  CE2 . PHE   A 1 36  ? -3.893  -3.196  65.668  1.00 25.56  ? 64  PHE   A CE2 1 
ATOM   251  C  CZ  . PHE   A 1 36  ? -5.104  -3.868  65.741  1.00 29.02  ? 64  PHE   A CZ  1 
ATOM   252  N  N   . SER   A 1 37  ? -4.816  1.648   60.957  1.00 24.48  ? 65  SER   A N   1 
ATOM   253  C  CA  . SER   A 1 37  ? -4.275  2.838   60.328  1.00 28.38  ? 65  SER   A CA  1 
ATOM   254  C  C   . SER   A 1 37  ? -4.911  4.095   60.890  1.00 28.57  ? 65  SER   A C   1 
ATOM   255  O  O   . SER   A 1 37  ? -4.213  4.999   61.373  1.00 32.27  ? 65  SER   A O   1 
ATOM   256  C  CB  . SER   A 1 37  ? -4.499  2.765   58.822  1.00 31.31  ? 65  SER   A CB  1 
ATOM   257  O  OG  . SER   A 1 37  ? -3.870  3.854   58.178  1.00 31.34  ? 65  SER   A OG  1 
ATOM   258  N  N   . TRP   A 1 38  ? -6.244  4.155   60.845  1.00 25.03  ? 66  TRP   A N   1 
ATOM   259  C  CA  . TRP   A 1 38  ? -6.972  5.313   61.345  1.00 25.91  ? 66  TRP   A CA  1 
ATOM   260  C  C   . TRP   A 1 38  ? -6.759  5.490   62.840  1.00 25.77  ? 66  TRP   A C   1 
ATOM   261  O  O   . TRP   A 1 38  ? -6.460  6.595   63.307  1.00 27.30  ? 66  TRP   A O   1 
ATOM   262  C  CB  . TRP   A 1 38  ? -8.465  5.161   61.029  1.00 22.07  ? 66  TRP   A CB  1 
ATOM   263  C  CG  . TRP   A 1 38  ? -9.335  6.310   61.466  1.00 27.17  ? 66  TRP   A CG  1 
ATOM   264  C  CD1 . TRP   A 1 38  ? -10.478 6.241   62.227  1.00 26.94  ? 66  TRP   A CD1 1 
ATOM   265  C  CD2 . TRP   A 1 38  ? -9.144  7.706   61.155  1.00 29.49  ? 66  TRP   A CD2 1 
ATOM   266  N  NE1 . TRP   A 1 38  ? -11.017 7.507   62.393  1.00 28.41  ? 66  TRP   A NE1 1 
ATOM   267  C  CE2 . TRP   A 1 38  ? -10.219 8.421   61.747  1.00 28.97  ? 66  TRP   A CE2 1 
ATOM   268  C  CE3 . TRP   A 1 38  ? -8.186  8.415   60.420  1.00 25.53  ? 66  TRP   A CE3 1 
ATOM   269  C  CZ2 . TRP   A 1 38  ? -10.338 9.814   61.648  1.00 28.21  ? 66  TRP   A CZ2 1 
ATOM   270  C  CZ3 . TRP   A 1 38  ? -8.318  9.818   60.315  1.00 32.41  ? 66  TRP   A CZ3 1 
ATOM   271  C  CH2 . TRP   A 1 38  ? -9.388  10.492  60.923  1.00 28.08  ? 66  TRP   A CH2 1 
ATOM   272  N  N   . GLY   A 1 39  ? -6.899  4.411   63.609  1.00 21.22  ? 67  GLY   A N   1 
ATOM   273  C  CA  . GLY   A 1 39  ? -6.894  4.546   65.056  1.00 24.05  ? 67  GLY   A CA  1 
ATOM   274  C  C   . GLY   A 1 39  ? -5.538  4.898   65.638  1.00 30.19  ? 67  GLY   A C   1 
ATOM   275  O  O   . GLY   A 1 39  ? -5.460  5.511   66.707  1.00 31.46  ? 67  GLY   A O   1 
ATOM   276  N  N   . LEU   A 1 40  ? -4.453  4.520   64.955  1.00 28.40  ? 68  LEU   A N   1 
ATOM   277  C  CA  . LEU   A 1 40  ? -3.107  4.665   65.493  1.00 29.32  ? 68  LEU   A CA  1 
ATOM   278  C  C   . LEU   A 1 40  ? -2.239  5.620   64.689  1.00 29.13  ? 68  LEU   A C   1 
ATOM   279  O  O   . LEU   A 1 40  ? -1.131  5.931   65.121  1.00 29.17  ? 68  LEU   A O   1 
ATOM   280  C  CB  . LEU   A 1 40  ? -2.402  3.300   65.567  1.00 25.46  ? 68  LEU   A CB  1 
ATOM   281  C  CG  . LEU   A 1 40  ? -2.740  2.337   66.713  1.00 33.39  ? 68  LEU   A CG  1 
ATOM   282  C  CD1 . LEU   A 1 40  ? -2.653  0.869   66.276  1.00 22.12  ? 68  LEU   A CD1 1 
ATOM   283  C  CD2 . LEU   A 1 40  ? -1.818  2.576   67.910  1.00 27.22  ? 68  LEU   A CD2 1 
ATOM   284  N  N   . GLY   A 1 41  ? -2.700  6.076   63.530  1.00 31.74  ? 69  GLY   A N   1 
ATOM   285  C  CA  . GLY   A 1 41  ? -1.944  7.054   62.776  1.00 31.54  ? 69  GLY   A CA  1 
ATOM   286  C  C   . GLY   A 1 41  ? -0.777  6.427   62.069  1.00 33.20  ? 69  GLY   A C   1 
ATOM   287  O  O   . GLY   A 1 41  ? 0.337   6.953   62.113  1.00 35.76  ? 69  GLY   A O   1 
ATOM   288  N  N   . MET   A 1 42  ? -1.023  5.300   61.411  1.00 33.51  ? 70  MET   A N   1 
ATOM   289  C  CA  . MET   A 1 42  ? 0.008   4.549   60.713  1.00 28.23  ? 70  MET   A CA  1 
ATOM   290  C  C   . MET   A 1 42  ? -0.252  4.589   59.216  1.00 30.85  ? 70  MET   A C   1 
ATOM   291  O  O   . MET   A 1 42  ? -1.386  4.393   58.759  1.00 35.17  ? 70  MET   A O   1 
ATOM   292  C  CB  . MET   A 1 42  ? 0.064   3.116   61.227  1.00 32.71  ? 70  MET   A CB  1 
ATOM   293  C  CG  . MET   A 1 42  ? 0.323   3.041   62.722  1.00 28.57  ? 70  MET   A CG  1 
ATOM   294  S  SD  . MET   A 1 42  ? 0.523   1.358   63.328  1.00 28.96  ? 70  MET   A SD  1 
ATOM   295  C  CE  . MET   A 1 42  ? 2.060   0.930   62.504  1.00 29.98  ? 70  MET   A CE  1 
ATOM   296  N  N   . ARG   A 1 43  ? 0.793   4.878   58.468  1.00 29.21  ? 71  ARG   A N   1 
ATOM   297  C  CA  . ARG   A 1 43  ? 0.724   4.957   57.022  1.00 37.07  ? 71  ARG   A CA  1 
ATOM   298  C  C   . ARG   A 1 43  ? 0.600   3.561   56.413  1.00 40.29  ? 71  ARG   A C   1 
ATOM   299  O  O   . ARG   A 1 43  ? 1.061   2.572   56.985  1.00 38.48  ? 71  ARG   A O   1 
ATOM   300  C  CB  . ARG   A 1 43  ? 1.988   5.636   56.509  1.00 38.05  ? 71  ARG   A CB  1 
ATOM   301  C  CG  . ARG   A 1 43  ? 1.957   6.020   55.075  1.00 49.95  ? 71  ARG   A CG  1 
ATOM   302  C  CD  . ARG   A 1 43  ? 2.360   7.474   54.940  1.00 54.27  ? 71  ARG   A CD  1 
ATOM   303  N  NE  . ARG   A 1 43  ? 2.032   8.001   53.619  1.00 55.87  ? 71  ARG   A NE  1 
ATOM   304  C  CZ  . ARG   A 1 43  ? 2.882   8.672   52.850  1.00 57.54  ? 71  ARG   A CZ  1 
ATOM   305  N  NH1 . ARG   A 1 43  ? 2.486   9.112   51.658  1.00 61.66  ? 71  ARG   A NH1 1 
ATOM   306  N  NH2 . ARG   A 1 43  ? 4.115   8.914   53.277  1.00 50.64  ? 71  ARG   A NH2 1 
ATOM   307  N  N   . PHE   A 1 44  ? -0.022  3.486   55.237  1.00 38.86  ? 72  PHE   A N   1 
ATOM   308  C  CA  . PHE   A 1 44  ? 0.055   2.288   54.406  1.00 42.67  ? 72  PHE   A CA  1 
ATOM   309  C  C   . PHE   A 1 44  ? 1.346   2.332   53.591  1.00 43.64  ? 72  PHE   A C   1 
ATOM   310  O  O   . PHE   A 1 44  ? 1.475   3.148   52.673  1.00 45.18  ? 72  PHE   A O   1 
ATOM   311  C  CB  . PHE   A 1 44  ? -1.161  2.195   53.488  1.00 43.77  ? 72  PHE   A CB  1 
ATOM   312  C  CG  . PHE   A 1 44  ? -2.305  1.414   54.068  1.00 47.99  ? 72  PHE   A CG  1 
ATOM   313  C  CD1 . PHE   A 1 44  ? -3.347  2.058   54.723  1.00 50.53  ? 72  PHE   A CD1 1 
ATOM   314  C  CD2 . PHE   A 1 44  ? -2.355  0.039   53.947  1.00 48.29  ? 72  PHE   A CD2 1 
ATOM   315  C  CE1 . PHE   A 1 44  ? -4.418  1.337   55.255  1.00 38.56  ? 72  PHE   A CE1 1 
ATOM   316  C  CE2 . PHE   A 1 44  ? -3.432  -0.685  54.476  1.00 49.24  ? 72  PHE   A CE2 1 
ATOM   317  C  CZ  . PHE   A 1 44  ? -4.457  -0.025  55.130  1.00 37.88  ? 72  PHE   A CZ  1 
ATOM   318  N  N   . SER   A 1 45  ? 2.277   1.456   53.894  1.00 39.97  ? 73  SER   A N   1 
ATOM   319  C  CA  . SER   A 1 45  ? 3.556   1.429   53.235  1.00 42.14  ? 73  SER   A CA  1 
ATOM   320  C  C   . SER   A 1 45  ? 3.805   0.372   52.204  1.00 45.94  ? 73  SER   A C   1 
ATOM   321  O  O   . SER   A 1 45  ? 4.505   0.634   51.276  1.00 45.21  ? 73  SER   A O   1 
ATOM   322  C  CB  . SER   A 1 45  ? 4.669   1.325   54.256  1.00 43.59  ? 73  SER   A CB  1 
ATOM   323  O  OG  . SER   A 1 45  ? 4.748   2.474   55.045  1.00 50.20  ? 73  SER   A OG  1 
ATOM   324  N  N   . ALA   A 1 46  ? 3.278   -0.824  52.368  1.00 36.60  ? 74  ALA   A N   1 
ATOM   325  C  CA  . ALA   A 1 46  ? 3.540   -1.872  51.391  1.00 36.14  ? 74  ALA   A CA  1 
ATOM   326  C  C   . ALA   A 1 46  ? 2.423   -2.906  51.397  1.00 34.26  ? 74  ALA   A C   1 
ATOM   327  O  O   . ALA   A 1 46  ? 1.680   -3.051  52.370  1.00 32.55  ? 74  ALA   A O   1 
ATOM   328  C  CB  . ALA   A 1 46  ? 4.885   -2.559  51.652  1.00 37.63  ? 74  ALA   A CB  1 
ATOM   329  N  N   . LYS   A 1 47  ? 2.342   -3.660  50.305  1.00 33.57  ? 75  LYS   A N   1 
ATOM   330  C  CA  . LYS   A 1 47  ? 1.324   -4.684  50.167  1.00 37.75  ? 75  LYS   A CA  1 
ATOM   331  C  C   . LYS   A 1 47  ? 1.903   -5.892  49.446  1.00 37.73  ? 75  LYS   A C   1 
ATOM   332  O  O   . LYS   A 1 47  ? 2.852   -5.779  48.671  1.00 37.24  ? 75  LYS   A O   1 
ATOM   333  C  CB  . LYS   A 1 47  ? 0.095   -4.162  49.405  1.00 31.28  ? 75  LYS   A CB  1 
ATOM   334  C  CG  . LYS   A 1 47  ? 0.395   -3.699  47.999  1.00 38.05  ? 75  LYS   A CG  1 
ATOM   335  C  CD  . LYS   A 1 47  ? -0.897  -3.437  47.202  1.00 37.54  ? 75  LYS   A CD  1 
ATOM   336  C  CE  . LYS   A 1 47  ? -0.571  -3.008  45.777  1.00 40.82  ? 75  LYS   A CE  1 
ATOM   337  N  NZ  . LYS   A 1 47  ? -1.787  -2.712  44.968  1.00 35.31  ? 75  LYS   A NZ  1 
ATOM   338  N  N   . SER   A 1 48  ? 1.319   -7.054  49.723  1.00 33.35  ? 76  SER   A N   1 
ATOM   339  C  CA  . SER   A 1 48  ? 1.597   -8.281  48.981  1.00 33.64  ? 76  SER   A CA  1 
ATOM   340  C  C   . SER   A 1 48  ? 0.266   -9.018  48.912  1.00 34.40  ? 76  SER   A C   1 
ATOM   341  O  O   . SER   A 1 48  ? -0.236  -9.461  49.946  1.00 34.95  ? 76  SER   A O   1 
ATOM   342  C  CB  . SER   A 1 48  ? 2.681   -9.114  49.668  1.00 31.11  ? 76  SER   A CB  1 
ATOM   343  O  OG  . SER   A 1 48  ? 2.835   -10.392 49.057  1.00 31.04  ? 76  SER   A OG  1 
ATOM   344  N  N   . ASP   A 1 49  ? -0.335  -9.085  47.727  1.00 35.07  ? 77  ASP   A N   1 
ATOM   345  C  CA  . ASP   A 1 49  ? -1.679  -9.644  47.590  1.00 36.35  ? 77  ASP   A CA  1 
ATOM   346  C  C   . ASP   A 1 49  ? -1.888  -10.060 46.126  1.00 36.79  ? 77  ASP   A C   1 
ATOM   347  O  O   . ASP   A 1 49  ? -0.916  -10.249 45.383  1.00 38.97  ? 77  ASP   A O   1 
ATOM   348  C  CB  . ASP   A 1 49  ? -2.717  -8.636  48.120  1.00 31.19  ? 77  ASP   A CB  1 
ATOM   349  C  CG  . ASP   A 1 49  ? -2.713  -7.328  47.362  1.00 34.39  ? 77  ASP   A CG  1 
ATOM   350  O  OD1 . ASP   A 1 49  ? -2.017  -7.227  46.332  1.00 36.58  ? 77  ASP   A OD1 1 
ATOM   351  O  OD2 . ASP   A 1 49  ? -3.429  -6.395  47.801  1.00 35.92  ? 77  ASP   A OD2 1 
ATOM   352  N  N   . LEU   A 1 50  ? -3.151  -10.218 45.713  1.00 36.88  ? 78  LEU   A N   1 
ATOM   353  C  CA  . LEU   A 1 50  ? -3.437  -10.572 44.324  1.00 33.28  ? 78  LEU   A CA  1 
ATOM   354  C  C   . LEU   A 1 50  ? -2.806  -9.586  43.353  1.00 37.72  ? 78  LEU   A C   1 
ATOM   355  O  O   . LEU   A 1 50  ? -2.252  -9.989  42.324  1.00 41.51  ? 78  LEU   A O   1 
ATOM   356  C  CB  . LEU   A 1 50  ? -4.943  -10.616 44.081  1.00 31.74  ? 78  LEU   A CB  1 
ATOM   357  C  CG  . LEU   A 1 50  ? -5.752  -11.633 44.865  1.00 39.52  ? 78  LEU   A CG  1 
ATOM   358  C  CD1 . LEU   A 1 50  ? -7.239  -11.359 44.658  1.00 33.92  ? 78  LEU   A CD1 1 
ATOM   359  C  CD2 . LEU   A 1 50  ? -5.376  -13.048 44.448  1.00 33.97  ? 78  LEU   A CD2 1 
ATOM   360  N  N   . SER   A 1 51  ? -2.913  -8.284  43.644  1.00 32.15  ? 79  SER   A N   1 
ATOM   361  C  CA  . SER   A 1 51  ? -2.401  -7.268  42.725  1.00 39.87  ? 79  SER   A CA  1 
ATOM   362  C  C   . SER   A 1 51  ? -0.890  -7.339  42.572  1.00 41.48  ? 79  SER   A C   1 
ATOM   363  O  O   . SER   A 1 51  ? -0.351  -6.814  41.592  1.00 48.39  ? 79  SER   A O   1 
ATOM   364  C  CB  . SER   A 1 51  ? -2.798  -5.861  43.192  1.00 36.56  ? 79  SER   A CB  1 
ATOM   365  O  OG  . SER   A 1 51  ? -2.056  -5.492  44.345  1.00 39.36  ? 79  SER   A OG  1 
ATOM   366  N  N   . THR   A 1 52  ? -0.192  -7.954  43.518  1.00 37.38  ? 80  THR   A N   1 
ATOM   367  C  CA  . THR   A 1 52  ? 1.231   -8.216  43.361  1.00 44.29  ? 80  THR   A CA  1 
ATOM   368  C  C   . THR   A 1 52  ? 1.524   -9.661  42.979  1.00 40.57  ? 80  THR   A C   1 
ATOM   369  O  O   . THR   A 1 52  ? 2.691   -10.067 42.989  1.00 41.22  ? 80  THR   A O   1 
ATOM   370  C  CB  . THR   A 1 52  ? 1.983   -7.857  44.638  1.00 39.79  ? 80  THR   A CB  1 
ATOM   371  O  OG1 . THR   A 1 52  ? 1.644   -8.810  45.647  1.00 38.27  ? 80  THR   A OG1 1 
ATOM   372  C  CG2 . THR   A 1 52  ? 1.601   -6.451  45.111  1.00 37.95  ? 80  THR   A CG2 1 
ATOM   373  N  N   . GLY   A 1 53  ? 0.503   -10.442 42.639  1.00 37.36  ? 81  GLY   A N   1 
ATOM   374  C  CA  . GLY   A 1 53  ? 0.712   -11.804 42.201  1.00 35.68  ? 81  GLY   A CA  1 
ATOM   375  C  C   . GLY   A 1 53  ? 0.730   -12.852 43.292  1.00 38.97  ? 81  GLY   A C   1 
ATOM   376  O  O   . GLY   A 1 53  ? 1.007   -14.018 42.996  1.00 39.25  ? 81  GLY   A O   1 
ATOM   377  N  N   . ASN   A 1 54  ? 0.429   -12.487 44.535  1.00 37.55  ? 82  ASN   A N   1 
ATOM   378  C  CA  . ASN   A 1 54  ? 0.414   -13.429 45.648  1.00 32.99  ? 82  ASN   A CA  1 
ATOM   379  C  C   . ASN   A 1 54  ? -0.970  -14.070 45.721  1.00 39.03  ? 82  ASN   A C   1 
ATOM   380  O  O   . ASN   A 1 54  ? -1.952  -13.410 46.089  1.00 38.22  ? 82  ASN   A O   1 
ATOM   381  C  CB  . ASN   A 1 54  ? 0.786   -12.703 46.940  1.00 33.58  ? 82  ASN   A CB  1 
ATOM   382  C  CG  . ASN   A 1 54  ? 0.822   -13.610 48.143  1.00 34.58  ? 82  ASN   A CG  1 
ATOM   383  O  OD1 . ASN   A 1 54  ? 0.246   -14.707 48.143  1.00 34.50  ? 82  ASN   A OD1 1 
ATOM   384  N  ND2 . ASN   A 1 54  ? 1.487   -13.151 49.197  1.00 31.65  ? 82  ASN   A ND2 1 
ATOM   385  N  N   . MET   A 1 55  ? -1.054  -15.357 45.371  1.00 32.88  ? 83  MET   A N   1 
ATOM   386  C  CA  . MET   A 1 55  ? -2.319  -16.088 45.372  1.00 34.25  ? 83  MET   A CA  1 
ATOM   387  C  C   . MET   A 1 55  ? -2.589  -16.786 46.691  1.00 36.39  ? 83  MET   A C   1 
ATOM   388  O  O   . MET   A 1 55  ? -3.574  -17.527 46.798  1.00 34.72  ? 83  MET   A O   1 
ATOM   389  C  CB  . MET   A 1 55  ? -2.334  -17.130 44.255  1.00 32.29  ? 83  MET   A CB  1 
ATOM   390  C  CG  . MET   A 1 55  ? -2.011  -16.583 42.880  1.00 40.52  ? 83  MET   A CG  1 
ATOM   391  S  SD  . MET   A 1 55  ? -3.394  -15.699 42.128  1.00 59.35  ? 83  MET   A SD  1 
ATOM   392  C  CE  . MET   A 1 55  ? -2.766  -14.030 42.162  1.00 40.08  ? 83  MET   A CE  1 
ATOM   393  N  N   . VAL   A 1 56  ? -1.722  -16.586 47.679  1.00 33.98  ? 84  VAL   A N   1 
ATOM   394  C  CA  . VAL   A 1 56  ? -1.715  -17.367 48.906  1.00 34.42  ? 84  VAL   A CA  1 
ATOM   395  C  C   . VAL   A 1 56  ? -2.269  -16.559 50.069  1.00 31.25  ? 84  VAL   A C   1 
ATOM   396  O  O   . VAL   A 1 56  ? -3.234  -16.963 50.713  1.00 30.35  ? 84  VAL   A O   1 
ATOM   397  C  CB  . VAL   A 1 56  ? -0.293  -17.893 49.220  1.00 33.38  ? 84  VAL   A CB  1 
ATOM   398  C  CG1 . VAL   A 1 56  ? -0.245  -18.518 50.605  1.00 32.80  ? 84  VAL   A CG1 1 
ATOM   399  C  CG2 . VAL   A 1 56  ? 0.153   -18.909 48.177  1.00 37.46  ? 84  VAL   A CG2 1 
ATOM   400  N  N   . HIS   A 1 57  ? -1.630  -15.440 50.394  1.00 30.03  ? 85  HIS   A N   1 
ATOM   401  C  CA  . HIS   A 1 57  ? -2.104  -14.607 51.483  1.00 32.96  ? 85  HIS   A CA  1 
ATOM   402  C  C   . HIS   A 1 57  ? -2.164  -13.152 51.062  1.00 32.18  ? 85  HIS   A C   1 
ATOM   403  O  O   . HIS   A 1 57  ? -1.487  -12.708 50.130  1.00 34.57  ? 85  HIS   A O   1 
ATOM   404  C  CB  . HIS   A 1 57  ? -1.235  -14.724 52.727  1.00 31.35  ? 85  HIS   A CB  1 
ATOM   405  C  CG  . HIS   A 1 57  ? 0.224   -14.508 52.472  1.00 33.63  ? 85  HIS   A CG  1 
ATOM   406  N  ND1 . HIS   A 1 57  ? 0.840   -13.293 52.666  1.00 34.03  ? 85  HIS   A ND1 1 
ATOM   407  C  CD2 . HIS   A 1 57  ? 1.191   -15.358 52.055  1.00 32.51  ? 85  HIS   A CD2 1 
ATOM   408  C  CE1 . HIS   A 1 57  ? 2.126   -13.402 52.384  1.00 34.87  ? 85  HIS   A CE1 1 
ATOM   409  N  NE2 . HIS   A 1 57  ? 2.363   -14.644 52.005  1.00 39.00  ? 85  HIS   A NE2 1 
ATOM   410  N  N   . ALA   A 1 58  ? -2.985  -12.416 51.789  1.00 30.62  ? 86  ALA   A N   1 
ATOM   411  C  CA  . ALA   A 1 58  ? -3.055  -10.973 51.682  1.00 27.89  ? 86  ALA   A CA  1 
ATOM   412  C  C   . ALA   A 1 58  ? -2.315  -10.374 52.869  1.00 26.95  ? 86  ALA   A C   1 
ATOM   413  O  O   . ALA   A 1 58  ? -2.640  -10.692 54.017  1.00 27.96  ? 86  ALA   A O   1 
ATOM   414  C  CB  . ALA   A 1 58  ? -4.517  -10.526 51.671  1.00 25.28  ? 86  ALA   A CB  1 
ATOM   415  N  N   . SER   A 1 59  ? -1.342  -9.500  52.600  1.00 27.01  ? 87  SER   A N   1 
ATOM   416  C  CA  . SER   A 1 59  ? -0.530  -8.889  53.651  1.00 29.86  ? 87  SER   A CA  1 
ATOM   417  C  C   . SER   A 1 59  ? -0.378  -7.396  53.396  1.00 28.27  ? 87  SER   A C   1 
ATOM   418  O  O   . SER   A 1 59  ? 0.114   -6.998  52.334  1.00 30.98  ? 87  SER   A O   1 
ATOM   419  C  CB  . SER   A 1 59  ? 0.863   -9.541  53.720  1.00 29.14  ? 87  SER   A CB  1 
ATOM   420  O  OG  . SER   A 1 59  ? 0.812   -10.773 54.415  1.00 28.69  ? 87  SER   A OG  1 
ATOM   421  N  N   . TYR   A 1 60  ? -0.735  -6.574  54.386  1.00 23.02  ? 88  TYR   A N   1 
ATOM   422  C  CA  . TYR   A 1 60  ? -0.622  -5.122  54.287  1.00 27.93  ? 88  TYR   A CA  1 
ATOM   423  C  C   . TYR   A 1 60  ? 0.236   -4.591  55.431  1.00 28.63  ? 88  TYR   A C   1 
ATOM   424  O  O   . TYR   A 1 60  ? 0.013   -4.932  56.599  1.00 28.87  ? 88  TYR   A O   1 
ATOM   425  C  CB  . TYR   A 1 60  ? -2.019  -4.472  54.276  1.00 27.69  ? 88  TYR   A CB  1 
ATOM   426  C  CG  . TYR   A 1 60  ? -2.873  -5.052  53.160  1.00 24.21  ? 88  TYR   A CG  1 
ATOM   427  C  CD1 . TYR   A 1 60  ? -2.581  -4.760  51.835  1.00 26.61  ? 88  TYR   A CD1 1 
ATOM   428  C  CD2 . TYR   A 1 60  ? -3.916  -5.926  53.422  1.00 24.53  ? 88  TYR   A CD2 1 
ATOM   429  C  CE1 . TYR   A 1 60  ? -3.306  -5.295  50.800  1.00 27.02  ? 88  TYR   A CE1 1 
ATOM   430  C  CE2 . TYR   A 1 60  ? -4.684  -6.484  52.362  1.00 23.31  ? 88  TYR   A CE2 1 
ATOM   431  C  CZ  . TYR   A 1 60  ? -4.349  -6.156  51.060  1.00 24.97  ? 88  TYR   A CZ  1 
ATOM   432  O  OH  . TYR   A 1 60  ? -5.030  -6.673  49.990  1.00 25.71  ? 88  TYR   A OH  1 
ATOM   433  N  N   . LEU   A 1 61  ? 1.212   -3.757  55.096  1.00 28.25  ? 89  LEU   A N   1 
ATOM   434  C  CA  . LEU   A 1 61  ? 2.156   -3.231  56.074  1.00 29.81  ? 89  LEU   A CA  1 
ATOM   435  C  C   . LEU   A 1 61  ? 1.782   -1.799  56.431  1.00 32.01  ? 89  LEU   A C   1 
ATOM   436  O  O   . LEU   A 1 61  ? 1.682   -0.942  55.547  1.00 29.86  ? 89  LEU   A O   1 
ATOM   437  C  CB  . LEU   A 1 61  ? 3.582   -3.283  55.530  1.00 29.63  ? 89  LEU   A CB  1 
ATOM   438  C  CG  . LEU   A 1 61  ? 4.667   -2.862  56.517  1.00 33.76  ? 89  LEU   A CG  1 
ATOM   439  C  CD1 . LEU   A 1 61  ? 4.964   -4.003  57.476  1.00 32.46  ? 89  LEU   A CD1 1 
ATOM   440  C  CD2 . LEU   A 1 61  ? 5.946   -2.420  55.784  1.00 33.62  ? 89  LEU   A CD2 1 
ATOM   441  N  N   . LEU   A 1 62  ? 1.668   -1.535  57.710  1.00 32.77  ? 90  LEU   A N   1 
ATOM   442  C  CA  . LEU   A 1 62  ? 1.395   -0.225  58.233  1.00 29.69  ? 90  LEU   A CA  1 
ATOM   443  C  C   . LEU   A 1 62  ? 2.684   0.246   58.901  1.00 33.49  ? 90  LEU   A C   1 
ATOM   444  O  O   . LEU   A 1 62  ? 3.350   -0.537  59.518  1.00 31.37  ? 90  LEU   A O   1 
ATOM   445  C  CB  . LEU   A 1 62  ? 0.275   -0.314  59.257  1.00 31.93  ? 90  LEU   A CB  1 
ATOM   446  C  CG  . LEU   A 1 62  ? -1.132  -0.578  58.762  1.00 24.85  ? 90  LEU   A CG  1 
ATOM   447  C  CD1 . LEU   A 1 62  ? -2.180  -0.137  59.736  1.00 17.65  ? 90  LEU   A CD1 1 
ATOM   448  C  CD2 . LEU   A 1 62  ? -1.297  0.061   57.401  1.00 25.82  ? 90  LEU   A CD2 1 
ATOM   449  N  N   . THR   A 1 63  ? 2.929   1.539   58.853  1.00 33.78  ? 91  THR   A N   1 
ATOM   450  C  CA  . THR   A 1 63  ? 4.156   2.078   59.317  1.00 34.93  ? 91  THR   A CA  1 
ATOM   451  C  C   . THR   A 1 63  ? 4.046   3.451   59.930  1.00 37.92  ? 91  THR   A C   1 
ATOM   452  O  O   . THR   A 1 63  ? 3.335   4.253   59.434  1.00 29.33  ? 91  THR   A O   1 
ATOM   453  C  CB  . THR   A 1 63  ? 5.001   2.097   58.064  1.00 37.21  ? 91  THR   A CB  1 
ATOM   454  O  OG1 . THR   A 1 63  ? 6.331   1.776   58.367  1.00 41.11  ? 91  THR   A OG1 1 
ATOM   455  C  CG2 . THR   A 1 63  ? 4.895   3.364   57.358  1.00 33.19  ? 91  THR   A CG2 1 
ATOM   456  N  N   . SER   A 1 64  ? 4.738   3.686   61.043  1.00 37.73  ? 92  SER   A N   1 
ATOM   457  C  CA  . SER   A 1 64  ? 4.769   4.963   61.749  1.00 31.68  ? 92  SER   A CA  1 
ATOM   458  C  C   . SER   A 1 64  ? 6.145   4.998   62.388  1.00 37.21  ? 92  SER   A C   1 
ATOM   459  O  O   . SER   A 1 64  ? 6.426   4.299   63.338  1.00 32.35  ? 92  SER   A O   1 
ATOM   460  C  CB  . SER   A 1 64  ? 3.664   5.116   62.764  1.00 33.40  ? 92  SER   A CB  1 
ATOM   461  O  OG  . SER   A 1 64  ? 3.585   6.437   63.211  1.00 34.92  ? 92  SER   A OG  1 
ATOM   462  N  N   . GLY   A 1 65  ? 6.985   5.883   61.893  1.00 38.25  ? 93  GLY   A N   1 
ATOM   463  C  CA  . GLY   A 1 65  ? 8.381   5.863   62.300  1.00 35.94  ? 93  GLY   A CA  1 
ATOM   464  C  C   . GLY   A 1 65  ? 8.991   4.523   61.919  1.00 38.50  ? 93  GLY   A C   1 
ATOM   465  O  O   . GLY   A 1 65  ? 8.849   4.065   60.775  1.00 33.08  ? 93  GLY   A O   1 
ATOM   466  N  N   . ASP   A 1 66  ? 9.682   3.889   62.881  1.00 30.80  ? 94  ASP   A N   1 
ATOM   467  C  CA  . ASP   A 1 66  ? 10.243  2.550   62.709  1.00 35.29  ? 94  ASP   A CA  1 
ATOM   468  C  C   . ASP   A 1 66  ? 9.237   1.461   63.022  1.00 33.56  ? 94  ASP   A C   1 
ATOM   469  O  O   . ASP   A 1 66  ? 9.580   0.276   62.927  1.00 32.14  ? 94  ASP   A O   1 
ATOM   470  C  CB  . ASP   A 1 66  ? 11.471  2.323   63.617  1.00 33.76  ? 94  ASP   A CB  1 
ATOM   471  C  CG  . ASP   A 1 66  ? 12.598  3.281   63.331  1.00 40.99  ? 94  ASP   A CG  1 
ATOM   472  O  OD1 . ASP   A 1 66  ? 12.697  3.755   62.184  1.00 40.90  ? 94  ASP   A OD1 1 
ATOM   473  O  OD2 . ASP   A 1 66  ? 13.376  3.581   64.265  1.00 48.39  ? 94  ASP   A OD2 1 
ATOM   474  N  N   . LEU   A 1 67  ? 8.034   1.830   63.454  1.00 33.87  ? 95  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 67  ? 7.048   0.827   63.837  1.00 36.34  ? 95  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 67  ? 6.458   0.196   62.589  1.00 33.81  ? 95  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 67  ? 6.001   0.900   61.689  1.00 31.19  ? 95  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 67  ? 5.952   1.447   64.693  1.00 29.28  ? 95  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 67  ? 4.965   0.406   65.206  1.00 32.55  ? 95  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 67  ? 5.721   -0.734  65.836  1.00 19.26  ? 95  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 67  ? 4.014   1.042   66.210  1.00 27.21  ? 95  LEU   A CD2 1 
ATOM   482  N  N   . ARG   A 1 68  ? 6.513   -1.132  62.514  1.00 33.69  ? 96  ARG   A N   1 
ATOM   483  C  CA  . ARG   A 1 68  ? 5.987   -1.867  61.368  1.00 34.24  ? 96  ARG   A CA  1 
ATOM   484  C  C   . ARG   A 1 68  ? 4.971   -2.883  61.870  1.00 31.82  ? 96  ARG   A C   1 
ATOM   485  O  O   . ARG   A 1 68  ? 5.342   -3.864  62.524  1.00 35.97  ? 96  ARG   A O   1 
ATOM   486  C  CB  . ARG   A 1 68  ? 7.108   -2.541  60.578  1.00 37.41  ? 96  ARG   A CB  1 
ATOM   487  C  CG  . ARG   A 1 68  ? 7.600   -1.714  59.404  1.00 41.28  ? 96  ARG   A CG  1 
ATOM   488  C  CD  . ARG   A 1 68  ? 9.016   -2.085  59.019  1.00 40.83  ? 96  ARG   A CD  1 
ATOM   489  N  NE  . ARG   A 1 68  ? 9.905   -1.856  60.147  1.00 52.88  ? 96  ARG   A NE  1 
ATOM   490  C  CZ  . ARG   A 1 68  ? 11.228  -1.811  60.065  1.00 51.22  ? 96  ARG   A CZ  1 
ATOM   491  N  NH1 . ARG   A 1 68  ? 11.828  -1.987  58.894  1.00 52.97  ? 96  ARG   A NH1 1 
ATOM   492  N  NH2 . ARG   A 1 68  ? 11.944  -1.586  61.158  1.00 48.55  ? 96  ARG   A NH2 1 
ATOM   493  N  N   . PHE   A 1 69  ? 3.694   -2.619  61.593  1.00 29.74  ? 97  PHE   A N   1 
ATOM   494  C  CA  . PHE   A 1 69  ? 2.600   -3.562  61.826  1.00 31.30  ? 97  PHE   A CA  1 
ATOM   495  C  C   . PHE   A 1 69  ? 2.254   -4.236  60.510  1.00 28.49  ? 97  PHE   A C   1 
ATOM   496  O  O   . PHE   A 1 69  ? 1.904   -3.549  59.540  1.00 32.29  ? 97  PHE   A O   1 
ATOM   497  C  CB  . PHE   A 1 69  ? 1.359   -2.857  62.371  1.00 28.52  ? 97  PHE   A CB  1 
ATOM   498  C  CG  . PHE   A 1 69  ? 1.390   -2.624  63.854  1.00 29.00  ? 97  PHE   A CG  1 
ATOM   499  C  CD1 . PHE   A 1 69  ? 2.492   -3.025  64.613  1.00 25.56  ? 97  PHE   A CD1 1 
ATOM   500  C  CD2 . PHE   A 1 69  ? 0.328   -1.996  64.491  1.00 18.00  ? 97  PHE   A CD2 1 
ATOM   501  C  CE1 . PHE   A 1 69  ? 2.527   -2.802  65.993  1.00 26.10  ? 97  PHE   A CE1 1 
ATOM   502  C  CE2 . PHE   A 1 69  ? 0.344   -1.784  65.865  1.00 21.34  ? 97  PHE   A CE2 1 
ATOM   503  C  CZ  . PHE   A 1 69  ? 1.448   -2.183  66.625  1.00 24.86  ? 97  PHE   A CZ  1 
ATOM   504  N  N   . LEU   A 1 70  ? 2.331   -5.567  60.480  1.00 25.12  ? 98  LEU   A N   1 
ATOM   505  C  CA  . LEU   A 1 70  ? 1.946   -6.353  59.313  1.00 30.45  ? 98  LEU   A CA  1 
ATOM   506  C  C   . LEU   A 1 70  ? 0.643   -7.104  59.598  1.00 32.10  ? 98  LEU   A C   1 
ATOM   507  O  O   . LEU   A 1 70  ? 0.477   -7.685  60.680  1.00 31.11  ? 98  LEU   A O   1 
ATOM   508  C  CB  . LEU   A 1 70  ? 3.067   -7.325  58.920  1.00 30.80  ? 98  LEU   A CB  1 
ATOM   509  C  CG  . LEU   A 1 70  ? 2.860   -8.058  57.589  1.00 32.17  ? 98  LEU   A CG  1 
ATOM   510  C  CD1 . LEU   A 1 70  ? 2.728   -7.103  56.415  1.00 29.36  ? 98  LEU   A CD1 1 
ATOM   511  C  CD2 . LEU   A 1 70  ? 3.964   -9.049  57.333  1.00 29.30  ? 98  LEU   A CD2 1 
ATOM   512  N  N   . PHE   A 1 71  ? -0.275  -7.096  58.627  1.00 25.56  ? 99  PHE   A N   1 
ATOM   513  C  CA  . PHE   A 1 71  ? -1.595  -7.702  58.774  1.00 23.88  ? 99  PHE   A CA  1 
ATOM   514  C  C   . PHE   A 1 71  ? -1.766  -8.702  57.641  1.00 26.20  ? 99  PHE   A C   1 
ATOM   515  O  O   . PHE   A 1 71  ? -1.665  -8.337  56.466  1.00 27.87  ? 99  PHE   A O   1 
ATOM   516  C  CB  . PHE   A 1 71  ? -2.715  -6.636  58.752  1.00 26.48  ? 99  PHE   A CB  1 
ATOM   517  C  CG  . PHE   A 1 71  ? -2.598  -5.608  59.861  1.00 24.82  ? 99  PHE   A CG  1 
ATOM   518  C  CD1 . PHE   A 1 71  ? -1.816  -4.464  59.690  1.00 27.62  ? 99  PHE   A CD1 1 
ATOM   519  C  CD2 . PHE   A 1 71  ? -3.201  -5.822  61.096  1.00 23.46  ? 99  PHE   A CD2 1 
ATOM   520  C  CE1 . PHE   A 1 71  ? -1.680  -3.524  60.710  1.00 25.31  ? 99  PHE   A CE1 1 
ATOM   521  C  CE2 . PHE   A 1 71  ? -3.056  -4.890  62.124  1.00 23.66  ? 99  PHE   A CE2 1 
ATOM   522  C  CZ  . PHE   A 1 71  ? -2.310  -3.733  61.922  1.00 23.24  ? 99  PHE   A CZ  1 
ATOM   523  N  N   . THR   A 1 72  ? -1.988  -9.961  57.988  1.00 24.20  ? 100 THR   A N   1 
ATOM   524  C  CA  . THR   A 1 72  ? -1.994  -11.038 57.004  1.00 26.97  ? 100 THR   A CA  1 
ATOM   525  C  C   . THR   A 1 72  ? -3.216  -11.903 57.215  1.00 26.27  ? 100 THR   A C   1 
ATOM   526  O  O   . THR   A 1 72  ? -3.508  -12.276 58.355  1.00 25.60  ? 100 THR   A O   1 
ATOM   527  C  CB  . THR   A 1 72  ? -0.741  -11.911 57.119  1.00 26.12  ? 100 THR   A CB  1 
ATOM   528  O  OG1 . THR   A 1 72  ? 0.424   -11.113 56.882  1.00 23.61  ? 100 THR   A OG1 1 
ATOM   529  C  CG2 . THR   A 1 72  ? -0.791  -13.080 56.123  1.00 27.90  ? 100 THR   A CG2 1 
ATOM   530  N  N   . ALA   A 1 73  ? -3.906  -12.229 56.118  1.00 31.00  ? 101 ALA   A N   1 
ATOM   531  C  CA  . ALA   A 1 73  ? -5.063  -13.112 56.077  1.00 26.25  ? 101 ALA   A CA  1 
ATOM   532  C  C   . ALA   A 1 73  ? -4.921  -14.070 54.902  1.00 30.08  ? 101 ALA   A C   1 
ATOM   533  O  O   . ALA   A 1 73  ? -4.296  -13.720 53.894  1.00 29.56  ? 101 ALA   A O   1 
ATOM   534  C  CB  . ALA   A 1 73  ? -6.370  -12.312 55.927  1.00 28.52  ? 101 ALA   A CB  1 
ATOM   535  N  N   . PRO   A 1 74  ? -5.501  -15.274 54.989  1.00 29.51  ? 102 PRO   A N   1 
ATOM   536  C  CA  . PRO   A 1 74  ? -5.424  -16.205 53.853  1.00 31.56  ? 102 PRO   A CA  1 
ATOM   537  C  C   . PRO   A 1 74  ? -6.536  -16.012 52.834  1.00 30.01  ? 102 PRO   A C   1 
ATOM   538  O  O   . PRO   A 1 74  ? -7.696  -15.795 53.183  1.00 34.67  ? 102 PRO   A O   1 
ATOM   539  C  CB  . PRO   A 1 74  ? -5.562  -17.580 54.525  1.00 32.77  ? 102 PRO   A CB  1 
ATOM   540  C  CG  . PRO   A 1 74  ? -6.410  -17.333 55.723  1.00 33.34  ? 102 PRO   A CG  1 
ATOM   541  C  CD  . PRO   A 1 74  ? -6.072  -15.913 56.193  1.00 28.92  ? 102 PRO   A CD  1 
ATOM   542  N  N   . TYR   A 1 75  ? -6.179  -16.114 51.552  1.00 30.32  ? 103 TYR   A N   1 
ATOM   543  C  CA  . TYR   A 1 75  ? -7.179  -16.355 50.518  1.00 31.01  ? 103 TYR   A CA  1 
ATOM   544  C  C   . TYR   A 1 75  ? -7.667  -17.801 50.589  1.00 35.92  ? 103 TYR   A C   1 
ATOM   545  O  O   . TYR   A 1 75  ? -7.204  -18.617 51.401  1.00 37.57  ? 103 TYR   A O   1 
ATOM   546  C  CB  . TYR   A 1 75  ? -6.614  -16.098 49.125  1.00 30.62  ? 103 TYR   A CB  1 
ATOM   547  C  CG  . TYR   A 1 75  ? -6.169  -14.675 48.851  1.00 35.33  ? 103 TYR   A CG  1 
ATOM   548  C  CD1 . TYR   A 1 75  ? -7.024  -13.593 49.066  1.00 34.03  ? 103 TYR   A CD1 1 
ATOM   549  C  CD2 . TYR   A 1 75  ? -4.880  -14.416 48.392  1.00 34.16  ? 103 TYR   A CD2 1 
ATOM   550  C  CE1 . TYR   A 1 75  ? -6.614  -12.284 48.811  1.00 26.27  ? 103 TYR   A CE1 1 
ATOM   551  C  CE2 . TYR   A 1 75  ? -4.454  -13.115 48.144  1.00 36.62  ? 103 TYR   A CE2 1 
ATOM   552  C  CZ  . TYR   A 1 75  ? -5.329  -12.057 48.352  1.00 33.39  ? 103 TYR   A CZ  1 
ATOM   553  O  OH  . TYR   A 1 75  ? -4.893  -10.778 48.099  1.00 34.91  ? 103 TYR   A OH  1 
ATOM   554  N  N   . SER   A 1 76  ? -8.582  -18.126 49.684  1.00 32.00  ? 104 SER   A N   1 
ATOM   555  C  CA  . SER   A 1 76  ? -9.038  -19.496 49.522  1.00 32.91  ? 104 SER   A CA  1 
ATOM   556  C  C   . SER   A 1 76  ? -7.877  -20.384 49.080  1.00 34.92  ? 104 SER   A C   1 
ATOM   557  O  O   . SER   A 1 76  ? -7.173  -20.043 48.117  1.00 33.44  ? 104 SER   A O   1 
ATOM   558  C  CB  . SER   A 1 76  ? -10.156 -19.569 48.483  1.00 32.17  ? 104 SER   A CB  1 
ATOM   559  O  OG  . SER   A 1 76  ? -10.410 -20.924 48.128  1.00 30.87  ? 104 SER   A OG  1 
ATOM   560  N  N   . PRO   A 1 77  ? -7.676  -21.532 49.704  1.00 32.86  ? 105 PRO   A N   1 
ATOM   561  C  CA  . PRO   A 1 77  ? -6.630  -22.451 49.237  1.00 32.38  ? 105 PRO   A CA  1 
ATOM   562  C  C   . PRO   A 1 77  ? -6.769  -22.825 47.772  1.00 35.76  ? 105 PRO   A C   1 
ATOM   563  O  O   . PRO   A 1 77  ? -5.788  -23.244 47.148  1.00 32.37  ? 105 PRO   A O   1 
ATOM   564  C  CB  . PRO   A 1 77  ? -6.816  -23.681 50.134  1.00 32.22  ? 105 PRO   A CB  1 
ATOM   565  C  CG  . PRO   A 1 77  ? -7.456  -23.147 51.371  1.00 37.30  ? 105 PRO   A CG  1 
ATOM   566  C  CD  . PRO   A 1 77  ? -8.381  -22.049 50.890  1.00 36.24  ? 105 PRO   A CD  1 
ATOM   567  N  N   . SER   A 1 78  ? -7.982  -22.680 47.214  1.00 36.08  ? 106 SER   A N   1 
ATOM   568  C  CA  . SER   A 1 78  ? -8.210  -23.036 45.815  1.00 34.90  ? 106 SER   A CA  1 
ATOM   569  C  C   . SER   A 1 78  ? -7.362  -22.187 44.877  1.00 38.04  ? 106 SER   A C   1 
ATOM   570  O  O   . SER   A 1 78  ? -6.911  -22.675 43.832  1.00 40.59  ? 106 SER   A O   1 
ATOM   571  C  CB  . SER   A 1 78  ? -9.693  -22.887 45.467  1.00 32.15  ? 106 SER   A CB  1 
ATOM   572  O  OG  . SER   A 1 78  ? -10.105 -21.547 45.681  1.00 38.19  ? 106 SER   A OG  1 
ATOM   573  N  N   . LEU   A 1 79  ? -7.105  -20.931 45.240  1.00 34.20  ? 107 LEU   A N   1 
ATOM   574  C  CA  . LEU   A 1 79  ? -6.380  -20.052 44.332  1.00 35.27  ? 107 LEU   A CA  1 
ATOM   575  C  C   . LEU   A 1 79  ? -4.981  -20.576 44.042  1.00 37.41  ? 107 LEU   A C   1 
ATOM   576  O  O   . LEU   A 1 79  ? -4.445  -20.349 42.950  1.00 39.28  ? 107 LEU   A O   1 
ATOM   577  C  CB  . LEU   A 1 79  ? -6.297  -18.640 44.915  1.00 31.78  ? 107 LEU   A CB  1 
ATOM   578  C  CG  . LEU   A 1 79  ? -7.581  -17.886 45.227  1.00 37.31  ? 107 LEU   A CG  1 
ATOM   579  C  CD1 . LEU   A 1 79  ? -7.262  -16.411 45.327  1.00 31.03  ? 107 LEU   A CD1 1 
ATOM   580  C  CD2 . LEU   A 1 79  ? -8.652  -18.153 44.176  1.00 33.92  ? 107 LEU   A CD2 1 
ATOM   581  N  N   . SER   A 1 80  ? -4.377  -21.273 45.004  1.00 35.85  ? 108 SER   A N   1 
ATOM   582  C  CA  . SER   A 1 80  ? -2.995  -21.717 44.900  1.00 38.66  ? 108 SER   A CA  1 
ATOM   583  C  C   . SER   A 1 80  ? -2.885  -23.230 44.973  1.00 41.43  ? 108 SER   A C   1 
ATOM   584  O  O   . SER   A 1 80  ? -1.854  -23.749 45.405  1.00 38.74  ? 108 SER   A O   1 
ATOM   585  C  CB  . SER   A 1 80  ? -2.154  -21.089 46.009  1.00 34.84  ? 108 SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 80  ? -2.724  -21.426 47.268  1.00 36.88  ? 108 SER   A OG  1 
ATOM   587  N  N   . ALA   A 1 81  ? -3.933  -23.950 44.570  1.00 43.44  ? 109 ALA   A N   1 
ATOM   588  C  CA  . ALA   A 1 81  ? -3.928  -25.403 44.715  1.00 43.30  ? 109 ALA   A CA  1 
ATOM   589  C  C   . ALA   A 1 81  ? -2.886  -26.060 43.817  1.00 42.30  ? 109 ALA   A C   1 
ATOM   590  O  O   . ALA   A 1 81  ? -2.436  -27.173 44.110  1.00 42.23  ? 109 ALA   A O   1 
ATOM   591  C  CB  . ALA   A 1 81  ? -5.325  -25.968 44.417  1.00 37.23  ? 109 ALA   A CB  1 
ATOM   592  N  N   . GLY   A 1 82  ? -2.509  -25.414 42.717  1.00 43.96  ? 110 GLY   A N   1 
ATOM   593  C  CA  . GLY   A 1 82  ? -1.501  -25.994 41.856  1.00 42.34  ? 110 GLY   A CA  1 
ATOM   594  C  C   . GLY   A 1 82  ? -0.069  -25.726 42.269  1.00 42.08  ? 110 GLY   A C   1 
ATOM   595  O  O   . GLY   A 1 82  ? 0.856   -26.245 41.641  1.00 41.55  ? 110 GLY   A O   1 
ATOM   596  N  N   . GLU   A 1 83  ? 0.136   -24.938 43.317  1.00 37.37  ? 111 GLU   A N   1 
ATOM   597  C  CA  . GLU   A 1 83  ? 1.463   -24.538 43.753  1.00 36.93  ? 111 GLU   A CA  1 
ATOM   598  C  C   . GLU   A 1 83  ? 2.056   -25.569 44.709  1.00 37.75  ? 111 GLU   A C   1 
ATOM   599  O  O   . GLU   A 1 83  ? 1.344   -26.310 45.389  1.00 38.84  ? 111 GLU   A O   1 
ATOM   600  C  CB  . GLU   A 1 83  ? 1.430   -23.161 44.444  1.00 33.55  ? 111 GLU   A CB  1 
ATOM   601  C  CG  . GLU   A 1 83  ? 1.143   -21.958 43.532  1.00 36.37  ? 111 GLU   A CG  1 
ATOM   602  C  CD  . GLU   A 1 83  ? 0.949   -20.657 44.310  1.00 42.78  ? 111 GLU   A CD  1 
ATOM   603  O  OE1 . GLU   A 1 83  ? 1.414   -20.593 45.471  1.00 39.60  ? 111 GLU   A OE1 1 
ATOM   604  O  OE2 . GLU   A 1 83  ? 0.338   -19.699 43.764  1.00 36.52  ? 111 GLU   A OE2 1 
ATOM   605  N  N   . ILE   A 1 84  ? 3.381   -25.607 44.759  1.00 37.09  ? 112 ILE   A N   1 
ATOM   606  C  CA  . ILE   A 1 84  ? 4.088   -26.263 45.848  1.00 43.00  ? 112 ILE   A CA  1 
ATOM   607  C  C   . ILE   A 1 84  ? 5.063   -25.244 46.415  1.00 39.04  ? 112 ILE   A C   1 
ATOM   608  O  O   . ILE   A 1 84  ? 5.233   -24.155 45.863  1.00 41.69  ? 112 ILE   A O   1 
ATOM   609  C  CB  . ILE   A 1 84  ? 4.800   -27.556 45.412  1.00 38.51  ? 112 ILE   A CB  1 
ATOM   610  C  CG1 . ILE   A 1 84  ? 5.748   -27.303 44.237  1.00 39.39  ? 112 ILE   A CG1 1 
ATOM   611  C  CG2 . ILE   A 1 84  ? 3.760   -28.636 45.054  1.00 35.69  ? 112 ILE   A CG2 1 
ATOM   612  C  CD1 . ILE   A 1 84  ? 6.762   -28.456 44.046  1.00 41.61  ? 112 ILE   A CD1 1 
ATOM   613  N  N   . LYS   A 1 85  ? 5.673   -25.580 47.554  1.00 33.64  ? 113 LYS   A N   1 
ATOM   614  C  CA  . LYS   A 1 85  ? 6.588   -24.623 48.174  1.00 44.39  ? 113 LYS   A CA  1 
ATOM   615  C  C   . LYS   A 1 85  ? 7.646   -24.111 47.202  1.00 39.50  ? 113 LYS   A C   1 
ATOM   616  O  O   . LYS   A 1 85  ? 7.806   -22.885 47.105  1.00 39.72  ? 113 LYS   A O   1 
ATOM   617  C  CB  . LYS   A 1 85  ? 7.222   -25.240 49.430  1.00 39.52  ? 113 LYS   A CB  1 
ATOM   618  C  CG  . LYS   A 1 85  ? 6.241   -25.279 50.602  1.00 39.18  ? 113 LYS   A CG  1 
ATOM   619  C  CD  A LYS   A 1 85  ? 6.943   -25.681 51.888  0.35 40.47  ? 113 LYS   A CD  1 
ATOM   620  C  CD  B LYS   A 1 85  ? 6.913   -25.438 51.954  0.65 40.46  ? 113 LYS   A CD  1 
ATOM   621  C  CE  A LYS   A 1 85  ? 6.397   -24.914 53.085  0.35 39.30  ? 113 LYS   A CE  1 
ATOM   622  C  CE  B LYS   A 1 85  ? 5.869   -25.488 53.074  0.65 37.06  ? 113 LYS   A CE  1 
ATOM   623  N  NZ  A LYS   A 1 85  ? 6.844   -23.485 53.081  0.35 37.47  ? 113 LYS   A NZ  1 
ATOM   624  N  NZ  B LYS   A 1 85  ? 6.480   -25.784 54.408  0.65 37.49  ? 113 LYS   A NZ  1 
ATOM   625  N  N   . PRO   A 1 86  ? 8.333   -24.949 46.409  1.00 40.95  ? 114 PRO   A N   1 
ATOM   626  C  CA  . PRO   A 1 86  ? 9.259   -24.397 45.401  1.00 41.73  ? 114 PRO   A CA  1 
ATOM   627  C  C   . PRO   A 1 86  ? 8.633   -23.371 44.471  1.00 45.18  ? 114 PRO   A C   1 
ATOM   628  O  O   . PRO   A 1 86  ? 9.283   -22.365 44.158  1.00 50.54  ? 114 PRO   A O   1 
ATOM   629  C  CB  . PRO   A 1 86  ? 9.704   -25.639 44.617  1.00 40.57  ? 114 PRO   A CB  1 
ATOM   630  C  CG  . PRO   A 1 86  ? 9.534   -26.753 45.545  1.00 42.37  ? 114 PRO   A CG  1 
ATOM   631  C  CD  . PRO   A 1 86  ? 8.346   -26.424 46.401  1.00 41.25  ? 114 PRO   A CD  1 
ATOM   632  N  N   . THR   A 1 87  ? 7.398   -23.603 44.012  1.00 40.72  ? 115 THR   A N   1 
ATOM   633  C  CA  . THR   A 1 87  ? 6.722   -22.729 43.060  1.00 40.77  ? 115 THR   A CA  1 
ATOM   634  C  C   . THR   A 1 87  ? 5.788   -21.736 43.742  1.00 38.11  ? 115 THR   A C   1 
ATOM   635  O  O   . THR   A 1 87  ? 4.920   -21.157 43.080  1.00 40.14  ? 115 THR   A O   1 
ATOM   636  C  CB  . THR   A 1 87  ? 5.930   -23.561 42.036  1.00 39.45  ? 115 THR   A CB  1 
ATOM   637  O  OG1 . THR   A 1 87  ? 4.784   -24.155 42.667  1.00 36.36  ? 115 THR   A OG1 1 
ATOM   638  C  CG2 . THR   A 1 87  ? 6.792   -24.675 41.438  1.00 42.62  ? 115 THR   A CG2 1 
ATOM   639  N  N   . THR   A 1 88  ? 5.924   -21.535 45.050  1.00 40.58  ? 116 THR   A N   1 
ATOM   640  C  CA  . THR   A 1 88  ? 4.928   -20.743 45.759  1.00 38.77  ? 116 THR   A CA  1 
ATOM   641  C  C   . THR   A 1 88  ? 4.946   -19.289 45.304  1.00 38.80  ? 116 THR   A C   1 
ATOM   642  O  O   . THR   A 1 88  ? 5.964   -18.771 44.844  1.00 38.84  ? 116 THR   A O   1 
ATOM   643  C  CB  . THR   A 1 88  ? 5.149   -20.800 47.265  1.00 39.43  ? 116 THR   A CB  1 
ATOM   644  O  OG1 . THR   A 1 88  ? 3.995   -20.266 47.915  1.00 35.63  ? 116 THR   A OG1 1 
ATOM   645  C  CG2 . THR   A 1 88  ? 6.372   -19.976 47.679  1.00 39.46  ? 116 THR   A CG2 1 
ATOM   646  N  N   . THR   A 1 89  ? 3.785   -18.643 45.415  1.00 42.40  ? 117 THR   A N   1 
ATOM   647  C  CA  . THR   A 1 89  ? 3.636   -17.221 45.140  1.00 38.39  ? 117 THR   A CA  1 
ATOM   648  C  C   . THR   A 1 89  ? 3.438   -16.411 46.410  1.00 39.41  ? 117 THR   A C   1 
ATOM   649  O  O   . THR   A 1 89  ? 3.256   -15.189 46.330  1.00 36.28  ? 117 THR   A O   1 
ATOM   650  C  CB  . THR   A 1 89  ? 2.453   -16.970 44.202  1.00 38.62  ? 117 THR   A CB  1 
ATOM   651  O  OG1 . THR   A 1 89  ? 1.261   -17.497 44.790  1.00 34.89  ? 117 THR   A OG1 1 
ATOM   652  C  CG2 . THR   A 1 89  ? 2.686   -17.632 42.858  1.00 39.32  ? 117 THR   A CG2 1 
ATOM   653  N  N   . ALA   A 1 90  ? 3.436   -17.065 47.569  1.00 36.85  ? 118 ALA   A N   1 
ATOM   654  C  CA  . ALA   A 1 90  ? 3.400   -16.356 48.838  1.00 36.26  ? 118 ALA   A CA  1 
ATOM   655  C  C   . ALA   A 1 90  ? 4.703   -15.600 49.061  1.00 38.50  ? 118 ALA   A C   1 
ATOM   656  O  O   . ALA   A 1 90  ? 5.790   -16.139 48.852  1.00 40.97  ? 118 ALA   A O   1 
ATOM   657  C  CB  . ALA   A 1 90  ? 3.181   -17.346 49.979  1.00 35.16  ? 118 ALA   A CB  1 
ATOM   658  N  N   . SER   A 1 91  ? 4.602   -14.352 49.507  1.00 37.93  ? 119 SER   A N   1 
ATOM   659  C  CA  . SER   A 1 91  ? 5.815   -13.587 49.780  1.00 40.29  ? 119 SER   A CA  1 
ATOM   660  C  C   . SER   A 1 91  ? 6.402   -13.884 51.154  1.00 36.20  ? 119 SER   A C   1 
ATOM   661  O  O   . SER   A 1 91  ? 7.558   -13.535 51.407  1.00 36.74  ? 119 SER   A O   1 
ATOM   662  C  CB  . SER   A 1 91  ? 5.537   -12.086 49.642  1.00 34.30  ? 119 SER   A CB  1 
ATOM   663  O  OG  . SER   A 1 91  ? 4.395   -11.735 50.387  1.00 33.44  ? 119 SER   A OG  1 
ATOM   664  N  N   . ILE   A 1 92  ? 5.637   -14.497 52.045  1.00 35.45  ? 120 ILE   A N   1 
ATOM   665  C  CA  . ILE   A 1 92  ? 6.131   -14.958 53.332  1.00 35.77  ? 120 ILE   A CA  1 
ATOM   666  C  C   . ILE   A 1 92  ? 6.063   -16.476 53.337  1.00 41.29  ? 120 ILE   A C   1 
ATOM   667  O  O   . ILE   A 1 92  ? 4.999   -17.063 53.543  1.00 38.77  ? 120 ILE   A O   1 
ATOM   668  C  CB  . ILE   A 1 92  ? 5.331   -14.353 54.498  1.00 35.53  ? 120 ILE   A CB  1 
ATOM   669  C  CG1 . ILE   A 1 92  ? 5.405   -12.830 54.401  1.00 35.19  ? 120 ILE   A CG1 1 
ATOM   670  C  CG2 . ILE   A 1 92  ? 5.887   -14.819 55.850  1.00 33.08  ? 120 ILE   A CG2 1 
ATOM   671  C  CD1 . ILE   A 1 92  ? 4.918   -12.119 55.614  1.00 38.11  ? 120 ILE   A CD1 1 
ATOM   672  N  N   . PRO   A 1 93  ? 7.183   -17.152 53.068  1.00 41.02  ? 121 PRO   A N   1 
ATOM   673  C  CA  . PRO   A 1 93  ? 7.122   -18.601 52.827  1.00 36.01  ? 121 PRO   A CA  1 
ATOM   674  C  C   . PRO   A 1 93  ? 6.767   -19.412 54.060  1.00 39.76  ? 121 PRO   A C   1 
ATOM   675  O  O   . PRO   A 1 93  ? 6.390   -20.577 53.912  1.00 41.76  ? 121 PRO   A O   1 
ATOM   676  C  CB  . PRO   A 1 93  ? 8.531   -18.930 52.323  1.00 41.90  ? 121 PRO   A CB  1 
ATOM   677  C  CG  . PRO   A 1 93  ? 9.398   -17.876 52.946  1.00 44.84  ? 121 PRO   A CG  1 
ATOM   678  C  CD  . PRO   A 1 93  ? 8.548   -16.621 52.923  1.00 41.80  ? 121 PRO   A CD  1 
ATOM   679  N  N   . SER   A 1 94  ? 6.872   -18.849 55.267  1.00 34.70  ? 122 SER   A N   1 
ATOM   680  C  CA  . SER   A 1 94  ? 6.384   -19.551 56.449  1.00 34.36  ? 122 SER   A CA  1 
ATOM   681  C  C   . SER   A 1 94  ? 4.857   -19.609 56.535  1.00 37.40  ? 122 SER   A C   1 
ATOM   682  O  O   . SER   A 1 94  ? 4.332   -20.342 57.386  1.00 34.11  ? 122 SER   A O   1 
ATOM   683  C  CB  . SER   A 1 94  ? 6.932   -18.887 57.705  1.00 33.31  ? 122 SER   A CB  1 
ATOM   684  O  OG  . SER   A 1 94  ? 6.522   -17.534 57.766  1.00 31.78  ? 122 SER   A OG  1 
ATOM   685  N  N   . PHE   A 1 95  ? 4.132   -18.847 55.709  1.00 34.27  ? 123 PHE   A N   1 
ATOM   686  C  CA  . PHE   A 1 95  ? 2.673   -18.834 55.808  1.00 35.40  ? 123 PHE   A CA  1 
ATOM   687  C  C   . PHE   A 1 95  ? 2.087   -20.197 55.485  1.00 37.31  ? 123 PHE   A C   1 
ATOM   688  O  O   . PHE   A 1 95  ? 2.564   -20.926 54.609  1.00 39.50  ? 123 PHE   A O   1 
ATOM   689  C  CB  . PHE   A 1 95  ? 2.043   -17.814 54.859  1.00 25.36  ? 123 PHE   A CB  1 
ATOM   690  C  CG  . PHE   A 1 95  ? 0.541   -17.731 54.975  1.00 34.03  ? 123 PHE   A CG  1 
ATOM   691  C  CD1 . PHE   A 1 95  ? -0.051  -16.933 55.949  1.00 26.66  ? 123 PHE   A CD1 1 
ATOM   692  C  CD2 . PHE   A 1 95  ? -0.283  -18.471 54.125  1.00 29.95  ? 123 PHE   A CD2 1 
ATOM   693  C  CE1 . PHE   A 1 95  ? -1.423  -16.862 56.062  1.00 33.87  ? 123 PHE   A CE1 1 
ATOM   694  C  CE2 . PHE   A 1 95  ? -1.669  -18.405 54.236  1.00 32.24  ? 123 PHE   A CE2 1 
ATOM   695  C  CZ  . PHE   A 1 95  ? -2.246  -17.612 55.195  1.00 31.51  ? 123 PHE   A CZ  1 
ATOM   696  N  N   . ASP   A 1 96  ? 0.992   -20.509 56.156  1.00 36.05  ? 124 ASP   A N   1 
ATOM   697  C  CA  . ASP   A 1 96  ? 0.308   -21.760 55.897  1.00 31.66  ? 124 ASP   A CA  1 
ATOM   698  C  C   . ASP   A 1 96  ? -1.176  -21.570 56.166  1.00 32.08  ? 124 ASP   A C   1 
ATOM   699  O  O   . ASP   A 1 96  ? -1.550  -21.197 57.282  1.00 32.40  ? 124 ASP   A O   1 
ATOM   700  C  CB  . ASP   A 1 96  ? 0.893   -22.852 56.769  1.00 32.54  ? 124 ASP   A CB  1 
ATOM   701  C  CG  . ASP   A 1 96  ? 0.134   -24.117 56.646  1.00 38.73  ? 124 ASP   A CG  1 
ATOM   702  O  OD1 . ASP   A 1 96  ? 0.316   -24.811 55.619  1.00 43.27  ? 124 ASP   A OD1 1 
ATOM   703  O  OD2 . ASP   A 1 96  ? -0.665  -24.396 57.562  1.00 41.30  ? 124 ASP   A OD2 1 
ATOM   704  N  N   . HIS   A 1 97  ? -2.012  -21.810 55.148  1.00 29.67  ? 125 HIS   A N   1 
ATOM   705  C  CA  . HIS   A 1 97  ? -3.452  -21.633 55.318  1.00 35.91  ? 125 HIS   A CA  1 
ATOM   706  C  C   . HIS   A 1 97  ? -3.935  -22.292 56.603  1.00 35.29  ? 125 HIS   A C   1 
ATOM   707  O  O   . HIS   A 1 97  ? -4.596  -21.656 57.436  1.00 33.27  ? 125 HIS   A O   1 
ATOM   708  C  CB  . HIS   A 1 97  ? -4.214  -22.206 54.118  1.00 36.40  ? 125 HIS   A CB  1 
ATOM   709  C  CG  . HIS   A 1 97  ? -3.962  -21.479 52.836  1.00 38.87  ? 125 HIS   A CG  1 
ATOM   710  N  ND1 . HIS   A 1 97  ? -4.635  -20.323 52.492  1.00 33.96  ? 125 HIS   A ND1 1 
ATOM   711  C  CD2 . HIS   A 1 97  ? -3.136  -21.758 51.799  1.00 35.51  ? 125 HIS   A CD2 1 
ATOM   712  C  CE1 . HIS   A 1 97  ? -4.219  -19.911 51.307  1.00 35.92  ? 125 HIS   A CE1 1 
ATOM   713  N  NE2 . HIS   A 1 97  ? -3.310  -20.764 50.864  1.00 40.81  ? 125 HIS   A NE2 1 
ATOM   714  N  N   . GLY   A 1 98  ? -3.573  -23.561 56.796  1.00 30.14  ? 126 GLY   A N   1 
ATOM   715  C  CA  . GLY   A 1 98  ? -4.121  -24.313 57.913  1.00 31.70  ? 126 GLY   A CA  1 
ATOM   716  C  C   . GLY   A 1 98  ? -3.700  -23.749 59.252  1.00 32.58  ? 126 GLY   A C   1 
ATOM   717  O  O   . GLY   A 1 98  ? -4.528  -23.572 60.149  1.00 33.03  ? 126 GLY   A O   1 
ATOM   718  N  N   . SER   A 1 99  ? -2.405  -23.452 59.401  1.00 27.77  ? 127 SER   A N   1 
ATOM   719  C  CA  . SER   A 1 99  ? -1.916  -22.809 60.619  1.00 32.82  ? 127 SER   A CA  1 
ATOM   720  C  C   . SER   A 1 99  ? -2.577  -21.452 60.842  1.00 31.98  ? 127 SER   A C   1 
ATOM   721  O  O   . SER   A 1 99  ? -2.960  -21.112 61.968  1.00 33.39  ? 127 SER   A O   1 
ATOM   722  C  CB  . SER   A 1 99  ? -0.396  -22.653 60.537  1.00 34.39  ? 127 SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 99  ? 0.195   -23.857 60.083  1.00 33.84  ? 127 SER   A OG  1 
ATOM   724  N  N   . CYS   A 1 100 ? -2.732  -20.665 59.780  1.00 32.43  ? 128 CYS   A N   1 
ATOM   725  C  CA  . CYS   A 1 100 ? -3.367  -19.357 59.919  1.00 34.49  ? 128 CYS   A CA  1 
ATOM   726  C  C   . CYS   A 1 100 ? -4.831  -19.486 60.345  1.00 33.68  ? 128 CYS   A C   1 
ATOM   727  O  O   . CYS   A 1 100 ? -5.249  -18.915 61.361  1.00 30.42  ? 128 CYS   A O   1 
ATOM   728  C  CB  . CYS   A 1 100 ? -3.250  -18.583 58.607  1.00 32.73  ? 128 CYS   A CB  1 
ATOM   729  S  SG  . CYS   A 1 100 ? -3.781  -16.873 58.778  1.00 33.18  ? 128 CYS   A SG  1 
ATOM   730  N  N   . ARG   A 1 101 ? -5.628  -20.244 59.580  1.00 36.13  ? 129 ARG   A N   1 
ATOM   731  C  CA  . ARG   A 1 101 ? -7.027  -20.445 59.951  1.00 31.86  ? 129 ARG   A CA  1 
ATOM   732  C  C   . ARG   A 1 101 ? -7.148  -21.030 61.348  1.00 33.44  ? 129 ARG   A C   1 
ATOM   733  O  O   . ARG   A 1 101 ? -7.981  -20.584 62.141  1.00 34.80  ? 129 ARG   A O   1 
ATOM   734  C  CB  . ARG   A 1 101 ? -7.724  -21.352 58.935  1.00 38.05  ? 129 ARG   A CB  1 
ATOM   735  C  CG  . ARG   A 1 101 ? -7.827  -20.718 57.562  1.00 39.80  ? 129 ARG   A CG  1 
ATOM   736  C  CD  . ARG   A 1 101 ? -9.017  -21.214 56.762  1.00 48.55  ? 129 ARG   A CD  1 
ATOM   737  N  NE  . ARG   A 1 101 ? -8.901  -20.725 55.392  1.00 48.73  ? 129 ARG   A NE  1 
ATOM   738  C  CZ  . ARG   A 1 101 ? -9.251  -19.501 55.008  1.00 45.08  ? 129 ARG   A CZ  1 
ATOM   739  N  NH1 . ARG   A 1 101 ? -9.750  -18.634 55.886  1.00 46.04  ? 129 ARG   A NH1 1 
ATOM   740  N  NH2 . ARG   A 1 101 ? -9.088  -19.135 53.747  1.00 42.11  ? 129 ARG   A NH2 1 
ATOM   741  N  N   . SER   A 1 102 ? -6.306  -22.016 61.679  1.00 34.21  ? 130 SER   A N   1 
ATOM   742  C  CA  . SER   A 1 102 ? -6.354  -22.608 63.013  1.00 31.58  ? 130 SER   A CA  1 
ATOM   743  C  C   . SER   A 1 102 ? -6.001  -21.577 64.080  1.00 34.56  ? 130 SER   A C   1 
ATOM   744  O  O   . SER   A 1 102 ? -6.681  -21.475 65.109  1.00 34.97  ? 130 SER   A O   1 
ATOM   745  C  CB  . SER   A 1 102 ? -5.412  -23.810 63.090  1.00 36.32  ? 130 SER   A CB  1 
ATOM   746  O  OG  . SER   A 1 102 ? -5.425  -24.379 64.388  1.00 45.49  ? 130 SER   A OG  1 
ATOM   747  N  N   . PHE   A 1 103 ? -4.938  -20.798 63.847  1.00 32.32  ? 131 PHE   A N   1 
ATOM   748  C  CA  . PHE   A 1 103 ? -4.578  -19.733 64.781  1.00 28.23  ? 131 PHE   A CA  1 
ATOM   749  C  C   . PHE   A 1 103 ? -5.756  -18.802 65.028  1.00 31.08  ? 131 PHE   A C   1 
ATOM   750  O  O   . PHE   A 1 103 ? -6.114  -18.519 66.179  1.00 33.33  ? 131 PHE   A O   1 
ATOM   751  C  CB  . PHE   A 1 103 ? -3.380  -18.941 64.240  1.00 29.22  ? 131 PHE   A CB  1 
ATOM   752  C  CG  . PHE   A 1 103 ? -2.950  -17.787 65.120  1.00 32.58  ? 131 PHE   A CG  1 
ATOM   753  C  CD1 . PHE   A 1 103 ? -3.620  -16.567 65.078  1.00 26.93  ? 131 PHE   A CD1 1 
ATOM   754  C  CD2 . PHE   A 1 103 ? -1.864  -17.915 65.963  1.00 29.13  ? 131 PHE   A CD2 1 
ATOM   755  C  CE1 . PHE   A 1 103 ? -3.211  -15.496 65.882  1.00 35.02  ? 131 PHE   A CE1 1 
ATOM   756  C  CE2 . PHE   A 1 103 ? -1.453  -16.847 66.773  1.00 28.55  ? 131 PHE   A CE2 1 
ATOM   757  C  CZ  . PHE   A 1 103 ? -2.121  -15.640 66.731  1.00 31.65  ? 131 PHE   A CZ  1 
ATOM   758  N  N   . PHE   A 1 104 ? -6.361  -18.295 63.953  1.00 29.61  ? 132 PHE   A N   1 
ATOM   759  C  CA  . PHE   A 1 104 ? -7.403  -17.282 64.116  1.00 31.77  ? 132 PHE   A CA  1 
ATOM   760  C  C   . PHE   A 1 104 ? -8.664  -17.875 64.728  1.00 34.75  ? 132 PHE   A C   1 
ATOM   761  O  O   . PHE   A 1 104 ? -9.355  -17.208 65.502  1.00 33.62  ? 132 PHE   A O   1 
ATOM   762  C  CB  . PHE   A 1 104 ? -7.726  -16.631 62.775  1.00 26.59  ? 132 PHE   A CB  1 
ATOM   763  C  CG  . PHE   A 1 104 ? -8.581  -15.397 62.887  1.00 30.87  ? 132 PHE   A CG  1 
ATOM   764  C  CD1 . PHE   A 1 104 ? -8.020  -14.163 63.241  1.00 33.33  ? 132 PHE   A CD1 1 
ATOM   765  C  CD2 . PHE   A 1 104 ? -9.944  -15.442 62.616  1.00 35.17  ? 132 PHE   A CD2 1 
ATOM   766  C  CE1 . PHE   A 1 104 ? -8.822  -12.962 63.320  1.00 33.74  ? 132 PHE   A CE1 1 
ATOM   767  C  CE2 . PHE   A 1 104 ? -10.722 -14.270 62.707  1.00 39.70  ? 132 PHE   A CE2 1 
ATOM   768  C  CZ  . PHE   A 1 104 ? -10.142 -12.997 63.047  1.00 19.05  ? 132 PHE   A CZ  1 
ATOM   769  N  N   . SER   A 1 105 ? -8.987  -19.121 64.383  1.00 34.34  ? 133 SER   A N   1 
ATOM   770  C  CA  . SER   A 1 105 ? -10.138 -19.784 64.991  1.00 31.02  ? 133 SER   A CA  1 
ATOM   771  C  C   . SER   A 1 105 ? -9.917  -20.014 66.475  1.00 34.46  ? 133 SER   A C   1 
ATOM   772  O  O   . SER   A 1 105 ? -10.847 -19.893 67.282  1.00 34.15  ? 133 SER   A O   1 
ATOM   773  C  CB  . SER   A 1 105 ? -10.387 -21.118 64.296  1.00 40.31  ? 133 SER   A CB  1 
ATOM   774  O  OG  . SER   A 1 105 ? -10.464 -22.152 65.268  1.00 47.54  ? 133 SER   A OG  1 
ATOM   775  N  N   . SER   A 1 106 ? -8.691  -20.371 66.849  1.00 32.28  ? 134 SER   A N   1 
ATOM   776  C  CA  . SER   A 1 106 ? -8.370  -20.599 68.248  1.00 33.00  ? 134 SER   A CA  1 
ATOM   777  C  C   . SER   A 1 106 ? -8.198  -19.300 69.032  1.00 33.73  ? 134 SER   A C   1 
ATOM   778  O  O   . SER   A 1 106 ? -8.602  -19.225 70.199  1.00 36.22  ? 134 SER   A O   1 
ATOM   779  C  CB  . SER   A 1 106 ? -7.092  -21.433 68.353  1.00 33.92  ? 134 SER   A CB  1 
ATOM   780  O  OG  . SER   A 1 106 ? -6.552  -21.276 69.646  1.00 33.52  ? 134 SER   A OG  1 
ATOM   781  N  N   . HIS   A 1 107 ? -7.566  -18.281 68.439  1.00 33.00  ? 135 HIS   A N   1 
ATOM   782  C  CA  . HIS   A 1 107 ? -7.198  -17.085 69.189  1.00 32.49  ? 135 HIS   A CA  1 
ATOM   783  C  C   . HIS   A 1 107 ? -7.982  -15.835 68.809  1.00 33.79  ? 135 HIS   A C   1 
ATOM   784  O  O   . HIS   A 1 107 ? -7.976  -14.869 69.580  1.00 36.81  ? 135 HIS   A O   1 
ATOM   785  C  CB  . HIS   A 1 107 ? -5.696  -16.798 69.030  1.00 31.53  ? 135 HIS   A CB  1 
ATOM   786  C  CG  . HIS   A 1 107 ? -4.829  -17.952 69.414  1.00 32.73  ? 135 HIS   A CG  1 
ATOM   787  N  ND1 . HIS   A 1 107 ? -4.875  -18.527 70.666  1.00 36.51  ? 135 HIS   A ND1 1 
ATOM   788  C  CD2 . HIS   A 1 107 ? -3.926  -18.670 68.703  1.00 29.86  ? 135 HIS   A CD2 1 
ATOM   789  C  CE1 . HIS   A 1 107 ? -4.026  -19.539 70.715  1.00 30.74  ? 135 HIS   A CE1 1 
ATOM   790  N  NE2 . HIS   A 1 107 ? -3.441  -19.648 69.537  1.00 27.87  ? 135 HIS   A NE2 1 
ATOM   791  N  N   . GLY   A 1 108 ? -8.677  -15.838 67.683  1.00 27.62  ? 136 GLY   A N   1 
ATOM   792  C  CA  . GLY   A 1 108 ? -9.157  -14.589 67.148  1.00 32.24  ? 136 GLY   A CA  1 
ATOM   793  C  C   . GLY   A 1 108 ? -7.972  -13.727 66.737  1.00 34.28  ? 136 GLY   A C   1 
ATOM   794  O  O   . GLY   A 1 108 ? -6.813  -14.176 66.686  1.00 32.97  ? 136 GLY   A O   1 
ATOM   795  N  N   . LEU   A 1 109 ? -8.287  -12.465 66.447  1.00 29.37  ? 137 LEU   A N   1 
ATOM   796  C  CA  . LEU   A 1 109 ? -7.292  -11.488 66.033  1.00 27.33  ? 137 LEU   A CA  1 
ATOM   797  C  C   . LEU   A 1 109 ? -6.150  -11.440 67.035  1.00 25.57  ? 137 LEU   A C   1 
ATOM   798  O  O   . LEU   A 1 109 ? -6.365  -11.263 68.235  1.00 28.23  ? 137 LEU   A O   1 
ATOM   799  C  CB  . LEU   A 1 109 ? -7.948  -10.112 65.890  1.00 27.77  ? 137 LEU   A CB  1 
ATOM   800  C  CG  . LEU   A 1 109 ? -6.979  -9.005  65.459  1.00 24.71  ? 137 LEU   A CG  1 
ATOM   801  C  CD1 . LEU   A 1 109 ? -6.296  -9.346  64.145  1.00 21.19  ? 137 LEU   A CD1 1 
ATOM   802  C  CD2 . LEU   A 1 109 ? -7.691  -7.638  65.378  1.00 27.35  ? 137 LEU   A CD2 1 
ATOM   803  N  N   . GLY   A 1 110 ? -4.935  -11.643 66.550  1.00 27.43  ? 138 GLY   A N   1 
ATOM   804  C  CA  . GLY   A 1 110 ? -3.792  -11.628 67.443  1.00 27.64  ? 138 GLY   A CA  1 
ATOM   805  C  C   . GLY   A 1 110 ? -2.498  -11.612 66.666  1.00 25.44  ? 138 GLY   A C   1 
ATOM   806  O  O   . GLY   A 1 110 ? -2.475  -11.782 65.441  1.00 24.16  ? 138 GLY   A O   1 
ATOM   807  N  N   . VAL   A 1 111 ? -1.414  -11.396 67.412  1.00 24.71  ? 139 VAL   A N   1 
ATOM   808  C  CA  . VAL   A 1 111 ? -0.070  -11.376 66.851  1.00 26.25  ? 139 VAL   A CA  1 
ATOM   809  C  C   . VAL   A 1 111 ? 0.403   -12.803 66.611  1.00 27.82  ? 139 VAL   A C   1 
ATOM   810  O  O   . VAL   A 1 111 ? 0.415   -13.626 67.534  1.00 25.10  ? 139 VAL   A O   1 
ATOM   811  C  CB  . VAL   A 1 111 ? 0.895   -10.638 67.792  1.00 27.80  ? 139 VAL   A CB  1 
ATOM   812  C  CG1 . VAL   A 1 111 ? 2.355   -10.908 67.388  1.00 21.59  ? 139 VAL   A CG1 1 
ATOM   813  C  CG2 . VAL   A 1 111 ? 0.589   -9.129  67.776  1.00 24.84  ? 139 VAL   A CG2 1 
ATOM   814  N  N   . ARG   A 1 112 ? 0.820   -13.093 65.378  1.00 24.95  ? 140 ARG   A N   1 
ATOM   815  C  CA  . ARG   A 1 112 ? 1.444   -14.380 65.092  1.00 28.66  ? 140 ARG   A CA  1 
ATOM   816  C  C   . ARG   A 1 112 ? 2.964   -14.346 65.217  1.00 31.24  ? 140 ARG   A C   1 
ATOM   817  O  O   . ARG   A 1 112 ? 3.553   -15.329 65.675  1.00 31.54  ? 140 ARG   A O   1 
ATOM   818  C  CB  . ARG   A 1 112 ? 1.046   -14.854 63.696  1.00 30.25  ? 140 ARG   A CB  1 
ATOM   819  C  CG  . ARG   A 1 112 ? 1.873   -15.977 63.118  1.00 34.10  ? 140 ARG   A CG  1 
ATOM   820  C  CD  . ARG   A 1 112 ? 1.882   -17.265 63.975  1.00 28.15  ? 140 ARG   A CD  1 
ATOM   821  N  NE  . ARG   A 1 112 ? 2.605   -18.300 63.246  1.00 33.49  ? 140 ARG   A NE  1 
ATOM   822  C  CZ  . ARG   A 1 112 ? 2.677   -19.580 63.604  1.00 33.47  ? 140 ARG   A CZ  1 
ATOM   823  N  NH1 . ARG   A 1 112 ? 2.091   -20.012 64.719  1.00 26.40  ? 140 ARG   A NH1 1 
ATOM   824  N  NH2 . ARG   A 1 112 ? 3.341   -20.425 62.831  1.00 29.69  ? 140 ARG   A NH2 1 
ATOM   825  N  N   . ALA   A 1 113 ? 3.621   -13.247 64.841  1.00 30.26  ? 141 ALA   A N   1 
ATOM   826  C  CA  . ALA   A 1 113 ? 5.079   -13.188 64.823  1.00 27.49  ? 141 ALA   A CA  1 
ATOM   827  C  C   . ALA   A 1 113 ? 5.562   -11.918 65.498  1.00 31.22  ? 141 ALA   A C   1 
ATOM   828  O  O   . ALA   A 1 113 ? 5.067   -10.820 65.202  1.00 30.92  ? 141 ALA   A O   1 
ATOM   829  C  CB  . ALA   A 1 113 ? 5.632   -13.235 63.390  1.00 25.68  ? 141 ALA   A CB  1 
ATOM   830  N  N   . VAL   A 1 114 ? 6.523   -12.064 66.400  1.00 28.09  ? 142 VAL   A N   1 
ATOM   831  C  CA  . VAL   A 1 114 ? 7.332   -10.940 66.872  1.00 27.97  ? 142 VAL   A CA  1 
ATOM   832  C  C   . VAL   A 1 114 ? 8.646   -11.057 66.127  1.00 30.50  ? 142 VAL   A C   1 
ATOM   833  O  O   . VAL   A 1 114 ? 9.365   -12.056 66.284  1.00 32.89  ? 142 VAL   A O   1 
ATOM   834  C  CB  . VAL   A 1 114 ? 7.541   -10.973 68.390  1.00 28.36  ? 142 VAL   A CB  1 
ATOM   835  C  CG1 . VAL   A 1 114 ? 8.332   -9.748  68.857  1.00 28.34  ? 142 VAL   A CG1 1 
ATOM   836  C  CG2 . VAL   A 1 114 ? 6.209   -11.100 69.116  1.00 24.51  ? 142 VAL   A CG2 1 
ATOM   837  N  N   . ALA   A 1 115 ? 8.934   -10.090 65.263  1.00 26.39  ? 143 ALA   A N   1 
ATOM   838  C  CA  . ALA   A 1 115 ? 10.097  -10.175 64.392  1.00 28.51  ? 143 ALA   A CA  1 
ATOM   839  C  C   . ALA   A 1 115 ? 11.172  -9.205  64.849  1.00 32.54  ? 143 ALA   A C   1 
ATOM   840  O  O   . ALA   A 1 115 ? 10.901  -8.010  65.051  1.00 27.00  ? 143 ALA   A O   1 
ATOM   841  C  CB  . ALA   A 1 115 ? 9.743   -9.891  62.940  1.00 26.18  ? 143 ALA   A CB  1 
ATOM   842  N  N   . ILE   A 1 116 ? 12.390  -9.724  64.978  1.00 29.08  ? 144 ILE   A N   1 
ATOM   843  C  CA  . ILE   A 1 116 ? 13.572  -8.938  65.301  1.00 32.60  ? 144 ILE   A CA  1 
ATOM   844  C  C   . ILE   A 1 116 ? 14.560  -9.047  64.148  1.00 32.58  ? 144 ILE   A C   1 
ATOM   845  O  O   . ILE   A 1 116 ? 14.658  -10.093 63.497  1.00 30.58  ? 144 ILE   A O   1 
ATOM   846  C  CB  . ILE   A 1 116 ? 14.206  -9.409  66.616  1.00 29.09  ? 144 ILE   A CB  1 
ATOM   847  C  CG1 . ILE   A 1 116 ? 14.517  -10.912 66.539  1.00 29.98  ? 144 ILE   A CG1 1 
ATOM   848  C  CG2 . ILE   A 1 116 ? 13.277  -9.084  67.778  1.00 27.03  ? 144 ILE   A CG2 1 
ATOM   849  C  CD1 . ILE   A 1 116 ? 15.445  -11.393 67.647  1.00 30.65  ? 144 ILE   A CD1 1 
ATOM   850  N  N   . GLU   A 1 117 ? 15.246  -7.949  63.857  1.00 33.99  ? 145 GLU   A N   1 
ATOM   851  C  CA  . GLU   A 1 117 ? 16.323  -7.988  62.882  1.00 38.70  ? 145 GLU   A CA  1 
ATOM   852  C  C   . GLU   A 1 117 ? 17.578  -8.500  63.571  1.00 37.00  ? 145 GLU   A C   1 
ATOM   853  O  O   . GLU   A 1 117 ? 17.872  -8.120  64.707  1.00 37.73  ? 145 GLU   A O   1 
ATOM   854  C  CB  . GLU   A 1 117 ? 16.566  -6.601  62.291  1.00 41.17  ? 145 GLU   A CB  1 
ATOM   855  C  CG  . GLU   A 1 117 ? 17.475  -6.582  61.081  1.00 41.98  ? 145 GLU   A CG  1 
ATOM   856  C  CD  . GLU   A 1 117 ? 17.855  -5.166  60.695  1.00 46.75  ? 145 GLU   A CD  1 
ATOM   857  O  OE1 . GLU   A 1 117 ? 18.614  -4.984  59.713  1.00 44.25  ? 145 GLU   A OE1 1 
ATOM   858  O  OE2 . GLU   A 1 117 ? 17.397  -4.234  61.396  1.00 45.94  ? 145 GLU   A OE2 1 
ATOM   859  N  N   . VAL   A 1 118 ? 18.289  -9.407  62.901  1.00 41.50  ? 146 VAL   A N   1 
ATOM   860  C  CA  . VAL   A 1 118 ? 19.527  -9.990  63.405  1.00 36.07  ? 146 VAL   A CA  1 
ATOM   861  C  C   . VAL   A 1 118 ? 20.592  -9.845  62.328  1.00 40.39  ? 146 VAL   A C   1 
ATOM   862  O  O   . VAL   A 1 118 ? 20.295  -9.539  61.169  1.00 36.13  ? 146 VAL   A O   1 
ATOM   863  C  CB  . VAL   A 1 118 ? 19.361  -11.471 63.797  1.00 36.36  ? 146 VAL   A CB  1 
ATOM   864  C  CG1 . VAL   A 1 118 ? 18.360  -11.623 64.931  1.00 38.61  ? 146 VAL   A CG1 1 
ATOM   865  C  CG2 . VAL   A 1 118 ? 18.950  -12.301 62.584  1.00 32.74  ? 146 VAL   A CG2 1 
ATOM   866  N  N   . GLU   A 1 119 ? 21.853  -10.071 62.728  1.00 37.82  ? 147 GLU   A N   1 
ATOM   867  C  CA  . GLU   A 1 119 ? 22.948  -10.053 61.763  1.00 37.52  ? 147 GLU   A CA  1 
ATOM   868  C  C   . GLU   A 1 119 ? 22.733  -11.109 60.695  1.00 35.22  ? 147 GLU   A C   1 
ATOM   869  O  O   . GLU   A 1 119 ? 22.835  -10.829 59.494  1.00 40.16  ? 147 GLU   A O   1 
ATOM   870  C  CB  . GLU   A 1 119 ? 24.301  -10.273 62.464  1.00 34.00  ? 147 GLU   A CB  1 
ATOM   871  C  CG  . GLU   A 1 119 ? 25.230  -9.060  62.440  1.00 42.80  ? 147 GLU   A CG  1 
ATOM   872  C  CD  . GLU   A 1 119 ? 26.621  -9.325  63.043  1.00 52.24  ? 147 GLU   A CD  1 
ATOM   873  O  OE1 . GLU   A 1 119 ? 27.056  -8.493  63.869  1.00 52.03  ? 147 GLU   A OE1 1 
ATOM   874  O  OE2 . GLU   A 1 119 ? 27.281  -10.346 62.702  1.00 46.96  ? 147 GLU   A OE2 1 
ATOM   875  N  N   . ASP   A 1 120 ? 22.429  -12.335 61.111  1.00 33.00  ? 148 ASP   A N   1 
ATOM   876  C  CA  . ASP   A 1 120 ? 22.333  -13.456 60.183  1.00 38.28  ? 148 ASP   A CA  1 
ATOM   877  C  C   . ASP   A 1 120 ? 21.224  -14.373 60.672  1.00 43.52  ? 148 ASP   A C   1 
ATOM   878  O  O   . ASP   A 1 120 ? 21.374  -15.016 61.717  1.00 41.16  ? 148 ASP   A O   1 
ATOM   879  C  CB  . ASP   A 1 120 ? 23.657  -14.212 60.077  1.00 46.13  ? 148 ASP   A CB  1 
ATOM   880  C  CG  . ASP   A 1 120 ? 23.659  -15.210 58.935  1.00 52.64  ? 148 ASP   A CG  1 
ATOM   881  O  OD1 . ASP   A 1 120 ? 24.364  -14.970 57.931  1.00 57.03  ? 148 ASP   A OD1 1 
ATOM   882  O  OD2 . ASP   A 1 120 ? 22.911  -16.211 59.022  1.00 51.90  ? 148 ASP   A OD2 1 
ATOM   883  N  N   . ALA   A 1 121 ? 20.119  -14.432 59.910  1.00 43.53  ? 149 ALA   A N   1 
ATOM   884  C  CA  . ALA   A 1 121 ? 18.949  -15.202 60.319  1.00 35.22  ? 149 ALA   A CA  1 
ATOM   885  C  C   . ALA   A 1 121 ? 19.191  -16.705 60.240  1.00 40.06  ? 149 ALA   A C   1 
ATOM   886  O  O   . ALA   A 1 121 ? 18.608  -17.460 61.027  1.00 41.48  ? 149 ALA   A O   1 
ATOM   887  C  CB  . ALA   A 1 121 ? 17.746  -14.815 59.462  1.00 34.72  ? 149 ALA   A CB  1 
ATOM   888  N  N   . GLU   A 1 122 ? 20.014  -17.164 59.291  1.00 42.05  ? 150 GLU   A N   1 
ATOM   889  C  CA  . GLU   A 1 122 ? 20.327  -18.594 59.224  1.00 47.13  ? 150 GLU   A CA  1 
ATOM   890  C  C   . GLU   A 1 122 ? 21.090  -19.032 60.461  1.00 44.22  ? 150 GLU   A C   1 
ATOM   891  O  O   . GLU   A 1 122 ? 20.754  -20.042 61.089  1.00 43.45  ? 150 GLU   A O   1 
ATOM   892  C  CB  . GLU   A 1 122 ? 21.137  -18.915 57.967  1.00 49.66  ? 150 GLU   A CB  1 
ATOM   893  C  CG  . GLU   A 1 122 ? 21.659  -20.360 57.924  1.00 51.50  ? 150 GLU   A CG  1 
ATOM   894  C  CD  . GLU   A 1 122 ? 22.074  -20.795 56.523  1.00 59.56  ? 150 GLU   A CD  1 
ATOM   895  O  OE1 . GLU   A 1 122 ? 23.184  -21.345 56.366  1.00 64.34  ? 150 GLU   A OE1 1 
ATOM   896  O  OE2 . GLU   A 1 122 ? 21.289  -20.580 55.574  1.00 62.97  ? 150 GLU   A OE2 1 
ATOM   897  N  N   . SER   A 1 123 ? 22.112  -18.257 60.831  1.00 37.21  ? 151 SER   A N   1 
ATOM   898  C  CA  . SER   A 1 123 ? 22.880  -18.541 62.031  1.00 40.22  ? 151 SER   A CA  1 
ATOM   899  C  C   . SER   A 1 123 ? 22.006  -18.458 63.273  1.00 40.34  ? 151 SER   A C   1 
ATOM   900  O  O   . SER   A 1 123 ? 21.990  -19.381 64.096  1.00 42.15  ? 151 SER   A O   1 
ATOM   901  C  CB  . SER   A 1 123 ? 24.057  -17.568 62.128  1.00 48.17  ? 151 SER   A CB  1 
ATOM   902  O  OG  . SER   A 1 123 ? 24.552  -17.495 63.459  1.00 54.37  ? 151 SER   A OG  1 
ATOM   903  N  N   . ALA   A 1 124 ? 21.255  -17.360 63.417  1.00 41.65  ? 152 ALA   A N   1 
ATOM   904  C  CA  . ALA   A 1 124 ? 20.403  -17.191 64.590  1.00 38.41  ? 152 ALA   A CA  1 
ATOM   905  C  C   . ALA   A 1 124 ? 19.401  -18.332 64.741  1.00 41.50  ? 152 ALA   A C   1 
ATOM   906  O  O   . ALA   A 1 124 ? 19.064  -18.712 65.869  1.00 41.74  ? 152 ALA   A O   1 
ATOM   907  C  CB  . ALA   A 1 124 ? 19.673  -15.848 64.522  1.00 41.96  ? 152 ALA   A CB  1 
ATOM   908  N  N   . PHE   A 1 125 ? 18.920  -18.898 63.631  1.00 37.85  ? 153 PHE   A N   1 
ATOM   909  C  CA  . PHE   A 1 125 ? 18.038  -20.056 63.729  1.00 37.84  ? 153 PHE   A CA  1 
ATOM   910  C  C   . PHE   A 1 125 ? 18.807  -21.293 64.193  1.00 40.20  ? 153 PHE   A C   1 
ATOM   911  O  O   . PHE   A 1 125 ? 18.366  -22.006 65.106  1.00 34.94  ? 153 PHE   A O   1 
ATOM   912  C  CB  . PHE   A 1 125 ? 17.351  -20.305 62.381  1.00 37.75  ? 153 PHE   A CB  1 
ATOM   913  C  CG  . PHE   A 1 125 ? 16.523  -21.575 62.334  1.00 43.31  ? 153 PHE   A CG  1 
ATOM   914  C  CD1 . PHE   A 1 125 ? 17.130  -22.817 62.133  1.00 42.99  ? 153 PHE   A CD1 1 
ATOM   915  C  CD2 . PHE   A 1 125 ? 15.145  -21.528 62.468  1.00 39.88  ? 153 PHE   A CD2 1 
ATOM   916  C  CE1 . PHE   A 1 125 ? 16.390  -23.976 62.079  1.00 39.98  ? 153 PHE   A CE1 1 
ATOM   917  C  CE2 . PHE   A 1 125 ? 14.392  -22.692 62.407  1.00 39.04  ? 153 PHE   A CE2 1 
ATOM   918  C  CZ  . PHE   A 1 125 ? 15.022  -23.924 62.212  1.00 40.21  ? 153 PHE   A CZ  1 
ATOM   919  N  N   . SER   A 1 126 ? 19.951  -21.577 63.564  1.00 44.92  ? 154 SER   A N   1 
ATOM   920  C  CA  . SER   A 1 126 ? 20.746  -22.743 63.956  1.00 44.06  ? 154 SER   A CA  1 
ATOM   921  C  C   . SER   A 1 126 ? 21.110  -22.688 65.432  1.00 36.75  ? 154 SER   A C   1 
ATOM   922  O  O   . SER   A 1 126 ? 20.795  -23.605 66.202  1.00 37.29  ? 154 SER   A O   1 
ATOM   923  C  CB  . SER   A 1 126 ? 22.008  -22.837 63.100  1.00 43.43  ? 154 SER   A CB  1 
ATOM   924  O  OG  . SER   A 1 126 ? 21.666  -23.166 61.764  1.00 56.67  ? 154 SER   A OG  1 
ATOM   925  N  N   . ILE   A 1 127 ? 21.776  -21.608 65.840  1.00 37.81  ? 155 ILE   A N   1 
ATOM   926  C  CA  . ILE   A 1 127 ? 22.150  -21.438 67.239  1.00 33.50  ? 155 ILE   A CA  1 
ATOM   927  C  C   . ILE   A 1 127 ? 20.927  -21.531 68.137  1.00 38.54  ? 155 ILE   A C   1 
ATOM   928  O  O   . ILE   A 1 127 ? 20.974  -22.150 69.208  1.00 38.24  ? 155 ILE   A O   1 
ATOM   929  C  CB  . ILE   A 1 127 ? 22.885  -20.097 67.425  1.00 40.81  ? 155 ILE   A CB  1 
ATOM   930  C  CG1 . ILE   A 1 127 ? 24.311  -20.172 66.868  1.00 40.14  ? 155 ILE   A CG1 1 
ATOM   931  C  CG2 . ILE   A 1 127 ? 22.865  -19.676 68.882  1.00 39.62  ? 155 ILE   A CG2 1 
ATOM   932  C  CD1 . ILE   A 1 127 ? 24.889  -18.795 66.523  1.00 37.43  ? 155 ILE   A CD1 1 
ATOM   933  N  N   . SER   A 1 128 ? 19.810  -20.916 67.723  1.00 35.58  ? 156 SER   A N   1 
ATOM   934  C  CA  . SER   A 1 128 ? 18.596  -21.006 68.524  1.00 32.72  ? 156 SER   A CA  1 
ATOM   935  C  C   . SER   A 1 128 ? 18.175  -22.450 68.691  1.00 31.57  ? 156 SER   A C   1 
ATOM   936  O  O   . SER   A 1 128 ? 17.923  -22.914 69.811  1.00 33.83  ? 156 SER   A O   1 
ATOM   937  C  CB  . SER   A 1 128 ? 17.453  -20.211 67.882  1.00 37.34  ? 156 SER   A CB  1 
ATOM   938  O  OG  . SER   A 1 128 ? 17.543  -18.839 68.199  1.00 36.38  ? 156 SER   A OG  1 
ATOM   939  N  N   . VAL   A 1 129 ? 18.050  -23.170 67.576  1.00 32.32  ? 157 VAL   A N   1 
ATOM   940  C  CA  . VAL   A 1 129 ? 17.603  -24.551 67.655  1.00 34.32  ? 157 VAL   A CA  1 
ATOM   941  C  C   . VAL   A 1 129 ? 18.629  -25.390 68.399  1.00 38.54  ? 157 VAL   A C   1 
ATOM   942  O  O   . VAL   A 1 129 ? 18.271  -26.204 69.256  1.00 37.65  ? 157 VAL   A O   1 
ATOM   943  C  CB  . VAL   A 1 129 ? 17.309  -25.111 66.255  1.00 40.13  ? 157 VAL   A CB  1 
ATOM   944  C  CG1 . VAL   A 1 129 ? 16.992  -26.605 66.340  1.00 40.85  ? 157 VAL   A CG1 1 
ATOM   945  C  CG2 . VAL   A 1 129 ? 16.140  -24.371 65.626  1.00 38.84  ? 157 VAL   A CG2 1 
ATOM   946  N  N   . ALA   A 1 130 ? 19.923  -25.163 68.138  1.00 42.52  ? 158 ALA   A N   1 
ATOM   947  C  CA  . ALA   A 1 130 ? 20.941  -25.867 68.918  1.00 41.94  ? 158 ALA   A CA  1 
ATOM   948  C  C   . ALA   A 1 130 ? 20.765  -25.631 70.405  1.00 42.78  ? 158 ALA   A C   1 
ATOM   949  O  O   . ALA   A 1 130 ? 21.217  -26.451 71.209  1.00 41.46  ? 158 ALA   A O   1 
ATOM   950  C  CB  . ALA   A 1 130 ? 22.349  -25.446 68.507  1.00 34.58  ? 158 ALA   A CB  1 
ATOM   951  N  N   . ASN   A 1 131 ? 20.074  -24.552 70.792  1.00 40.21  ? 159 ASN   A N   1 
ATOM   952  C  CA  . ASN   A 1 131 ? 19.994  -24.151 72.188  1.00 34.63  ? 159 ASN   A CA  1 
ATOM   953  C  C   . ASN   A 1 131 ? 18.597  -24.258 72.776  1.00 36.10  ? 159 ASN   A C   1 
ATOM   954  O  O   . ASN   A 1 131 ? 18.278  -23.567 73.744  1.00 42.62  ? 159 ASN   A O   1 
ATOM   955  C  CB  . ASN   A 1 131 ? 20.548  -22.746 72.352  1.00 40.65  ? 159 ASN   A CB  1 
ATOM   956  C  CG  . ASN   A 1 131 ? 22.016  -22.774 72.611  1.00 36.44  ? 159 ASN   A CG  1 
ATOM   957  O  OD1 . ASN   A 1 131 ? 22.432  -23.094 73.720  1.00 43.87  ? 159 ASN   A OD1 1 
ATOM   958  N  ND2 . ASN   A 1 131 ? 22.819  -22.481 71.592  1.00 30.42  ? 159 ASN   A ND2 1 
ATOM   959  N  N   . GLY   A 1 132 ? 17.773  -25.153 72.238  1.00 35.84  ? 160 GLY   A N   1 
ATOM   960  C  CA  . GLY   A 1 132 ? 16.501  -25.479 72.843  1.00 38.35  ? 160 GLY   A CA  1 
ATOM   961  C  C   . GLY   A 1 132 ? 15.288  -24.958 72.103  1.00 37.49  ? 160 GLY   A C   1 
ATOM   962  O  O   . GLY   A 1 132 ? 14.176  -25.408 72.400  1.00 35.18  ? 160 GLY   A O   1 
ATOM   963  N  N   . ALA   A 1 133 ? 15.461  -24.049 71.143  1.00 34.13  ? 161 ALA   A N   1 
ATOM   964  C  CA  . ALA   A 1 133 ? 14.319  -23.466 70.446  1.00 37.93  ? 161 ALA   A CA  1 
ATOM   965  C  C   . ALA   A 1 133 ? 13.564  -24.532 69.659  1.00 36.46  ? 161 ALA   A C   1 
ATOM   966  O  O   . ALA   A 1 133 ? 14.166  -25.349 68.956  1.00 37.70  ? 161 ALA   A O   1 
ATOM   967  C  CB  . ALA   A 1 133 ? 14.776  -22.357 69.502  1.00 33.75  ? 161 ALA   A CB  1 
ATOM   968  N  N   . ILE   A 1 134 ? 12.244  -24.524 69.770  1.00 33.76  ? 162 ILE   A N   1 
ATOM   969  C  CA  . ILE   A 1 134 ? 11.433  -25.383 68.921  1.00 30.01  ? 162 ILE   A CA  1 
ATOM   970  C  C   . ILE   A 1 134 ? 11.330  -24.712 67.559  1.00 34.39  ? 162 ILE   A C   1 
ATOM   971  O  O   . ILE   A 1 134 ? 10.783  -23.601 67.454  1.00 38.27  ? 162 ILE   A O   1 
ATOM   972  C  CB  . ILE   A 1 134 ? 10.054  -25.646 69.539  1.00 37.84  ? 162 ILE   A CB  1 
ATOM   973  C  CG1 . ILE   A 1 134 ? 10.216  -26.093 70.994  1.00 37.69  ? 162 ILE   A CG1 1 
ATOM   974  C  CG2 . ILE   A 1 134 ? 9.283   -26.673 68.699  1.00 39.58  ? 162 ILE   A CG2 1 
ATOM   975  C  CD1 . ILE   A 1 134 ? 8.945   -26.643 71.632  1.00 41.83  ? 162 ILE   A CD1 1 
ATOM   976  N  N   . PRO   A 1 135 ? 11.846  -25.328 66.499  1.00 34.04  ? 163 PRO   A N   1 
ATOM   977  C  CA  . PRO   A 1 135 ? 11.831  -24.667 65.189  1.00 33.07  ? 163 PRO   A CA  1 
ATOM   978  C  C   . PRO   A 1 135 ? 10.413  -24.577 64.645  1.00 34.63  ? 163 PRO   A C   1 
ATOM   979  O  O   . PRO   A 1 135 ? 9.595   -25.474 64.848  1.00 32.71  ? 163 PRO   A O   1 
ATOM   980  C  CB  . PRO   A 1 135 ? 12.723  -25.566 64.322  1.00 34.20  ? 163 PRO   A CB  1 
ATOM   981  C  CG  . PRO   A 1 135 ? 12.699  -26.901 64.997  1.00 36.64  ? 163 PRO   A CG  1 
ATOM   982  C  CD  . PRO   A 1 135 ? 12.467  -26.665 66.458  1.00 33.30  ? 163 PRO   A CD  1 
ATOM   983  N  N   . SER   A 1 136 ? 10.105  -23.458 63.994  1.00 36.54  ? 164 SER   A N   1 
ATOM   984  C  CA  . SER   A 1 136 ? 8.785   -23.296 63.395  1.00 29.39  ? 164 SER   A CA  1 
ATOM   985  C  C   . SER   A 1 136 ? 8.827   -23.178 61.883  1.00 30.68  ? 164 SER   A C   1 
ATOM   986  O  O   . SER   A 1 136 ? 7.955   -23.718 61.208  1.00 36.34  ? 164 SER   A O   1 
ATOM   987  C  CB  . SER   A 1 136 ? 8.069   -22.073 63.983  1.00 34.09  ? 164 SER   A CB  1 
ATOM   988  O  OG  . SER   A 1 136 ? 6.808   -21.876 63.353  1.00 34.05  ? 164 SER   A OG  1 
ATOM   989  N  N   . SER   A 1 137 ? 9.818   -22.489 61.323  1.00 33.11  ? 165 SER   A N   1 
ATOM   990  C  CA  . SER   A 1 137 ? 9.955   -22.442 59.877  1.00 36.24  ? 165 SER   A CA  1 
ATOM   991  C  C   . SER   A 1 137 ? 11.450  -22.248 59.651  1.00 38.93  ? 165 SER   A C   1 
ATOM   992  O  O   . SER   A 1 137 ? 12.042  -21.331 60.257  1.00 35.52  ? 165 SER   A O   1 
ATOM   993  C  CB  . SER   A 1 137 ? 9.165   -21.314 59.212  1.00 32.70  ? 165 SER   A CB  1 
ATOM   994  O  OG  . SER   A 1 137 ? 9.498   -21.194 57.835  1.00 39.83  ? 165 SER   A OG  1 
ATOM   995  N  N   . PRO   A 1 138 ? 12.076  -23.066 58.804  1.00 38.49  ? 166 PRO   A N   1 
ATOM   996  C  CA  . PRO   A 1 138 ? 13.536  -23.048 58.690  1.00 39.32  ? 166 PRO   A CA  1 
ATOM   997  C  C   . PRO   A 1 138 ? 13.991  -21.819 57.924  1.00 42.55  ? 166 PRO   A C   1 
ATOM   998  O  O   . PRO   A 1 138 ? 13.155  -21.091 57.362  1.00 42.04  ? 166 PRO   A O   1 
ATOM   999  C  CB  . PRO   A 1 138 ? 13.841  -24.351 57.930  1.00 38.51  ? 166 PRO   A CB  1 
ATOM   1000 C  CG  . PRO   A 1 138 ? 12.637  -24.554 57.070  1.00 45.57  ? 166 PRO   A CG  1 
ATOM   1001 C  CD  . PRO   A 1 138 ? 11.451  -23.952 57.806  1.00 36.28  ? 166 PRO   A CD  1 
ATOM   1002 N  N   . PRO   A 1 139 ? 15.293  -21.519 57.910  1.00 38.11  ? 167 PRO   A N   1 
ATOM   1003 C  CA  . PRO   A 1 139 ? 15.744  -20.312 57.202  1.00 38.46  ? 167 PRO   A CA  1 
ATOM   1004 C  C   . PRO   A 1 139 ? 15.499  -20.451 55.708  1.00 45.20  ? 167 PRO   A C   1 
ATOM   1005 O  O   . PRO   A 1 139 ? 15.862  -21.454 55.089  1.00 44.98  ? 167 PRO   A O   1 
ATOM   1006 C  CB  . PRO   A 1 139 ? 17.241  -20.236 57.527  1.00 41.74  ? 167 PRO   A CB  1 
ATOM   1007 C  CG  . PRO   A 1 139 ? 17.414  -21.060 58.765  1.00 39.76  ? 167 PRO   A CG  1 
ATOM   1008 C  CD  . PRO   A 1 139 ? 16.397  -22.168 58.644  1.00 39.03  ? 167 PRO   A CD  1 
ATOM   1009 N  N   . ILE   A 1 140 ? 14.852  -19.443 55.133  1.00 38.45  ? 168 ILE   A N   1 
ATOM   1010 C  CA  . ILE   A 1 140 ? 14.623  -19.386 53.700  1.00 40.55  ? 168 ILE   A CA  1 
ATOM   1011 C  C   . ILE   A 1 140 ? 15.186  -18.064 53.219  1.00 45.26  ? 168 ILE   A C   1 
ATOM   1012 O  O   . ILE   A 1 140 ? 15.096  -17.053 53.926  1.00 43.28  ? 168 ILE   A O   1 
ATOM   1013 C  CB  . ILE   A 1 140 ? 13.120  -19.535 53.368  1.00 43.61  ? 168 ILE   A CB  1 
ATOM   1014 C  CG1 . ILE   A 1 140 ? 12.601  -20.863 53.937  1.00 47.94  ? 168 ILE   A CG1 1 
ATOM   1015 C  CG2 . ILE   A 1 140 ? 12.868  -19.466 51.861  1.00 43.87  ? 168 ILE   A CG2 1 
ATOM   1016 C  CD1 . ILE   A 1 140 ? 11.184  -20.798 54.509  1.00 50.88  ? 168 ILE   A CD1 1 
ATOM   1017 N  N   . VAL   A 1 141 ? 15.803  -18.072 52.040  1.00 47.87  ? 169 VAL   A N   1 
ATOM   1018 C  CA  . VAL   A 1 141 ? 16.428  -16.876 51.484  1.00 48.99  ? 169 VAL   A CA  1 
ATOM   1019 C  C   . VAL   A 1 141 ? 15.526  -16.356 50.373  1.00 51.49  ? 169 VAL   A C   1 
ATOM   1020 O  O   . VAL   A 1 141 ? 15.181  -17.095 49.440  1.00 52.50  ? 169 VAL   A O   1 
ATOM   1021 C  CB  . VAL   A 1 141 ? 17.849  -17.163 50.973  1.00 50.26  ? 169 VAL   A CB  1 
ATOM   1022 C  CG1 . VAL   A 1 141 ? 18.358  -16.010 50.107  1.00 55.22  ? 169 VAL   A CG1 1 
ATOM   1023 C  CG2 . VAL   A 1 141 ? 18.779  -17.397 52.138  1.00 49.73  ? 169 VAL   A CG2 1 
ATOM   1024 N  N   . LEU   A 1 142 ? 15.131  -15.089 50.473  1.00 49.24  ? 170 LEU   A N   1 
ATOM   1025 C  CA  . LEU   A 1 142 ? 14.175  -14.506 49.542  1.00 50.08  ? 170 LEU   A CA  1 
ATOM   1026 C  C   . LEU   A 1 142 ? 14.915  -13.625 48.543  1.00 54.01  ? 170 LEU   A C   1 
ATOM   1027 O  O   . LEU   A 1 142 ? 15.543  -12.633 48.930  1.00 53.10  ? 170 LEU   A O   1 
ATOM   1028 C  CB  . LEU   A 1 142 ? 13.107  -13.715 50.291  1.00 49.07  ? 170 LEU   A CB  1 
ATOM   1029 C  CG  . LEU   A 1 142 ? 12.403  -14.466 51.421  1.00 48.88  ? 170 LEU   A CG  1 
ATOM   1030 C  CD1 . LEU   A 1 142 ? 11.673  -13.493 52.342  1.00 51.24  ? 170 LEU   A CD1 1 
ATOM   1031 C  CD2 . LEU   A 1 142 ? 11.444  -15.506 50.855  1.00 45.89  ? 170 LEU   A CD2 1 
ATOM   1032 N  N   . ASN   A 1 143 ? 14.863  -14.017 47.266  1.00 54.40  ? 171 ASN   A N   1 
ATOM   1033 C  CA  . ASN   A 1 143 ? 15.486  -13.273 46.173  1.00 54.14  ? 171 ASN   A CA  1 
ATOM   1034 C  C   . ASN   A 1 143 ? 16.958  -12.971 46.461  1.00 59.39  ? 171 ASN   A C   1 
ATOM   1035 O  O   . ASN   A 1 143 ? 17.475  -11.906 46.102  1.00 57.63  ? 171 ASN   A O   1 
ATOM   1036 C  CB  . ASN   A 1 143 ? 14.705  -11.992 45.891  1.00 56.22  ? 171 ASN   A CB  1 
ATOM   1037 C  CG  . ASN   A 1 143 ? 15.181  -11.278 44.647  1.00 63.42  ? 171 ASN   A CG  1 
ATOM   1038 O  OD1 . ASN   A 1 143 ? 15.683  -11.902 43.710  1.00 63.71  ? 171 ASN   A OD1 1 
ATOM   1039 N  ND2 . ASN   A 1 143 ? 15.063  -9.951  44.647  1.00 64.49  ? 171 ASN   A ND2 1 
ATOM   1040 N  N   . GLU   A 1 144 ? 17.644  -13.906 47.126  1.00 57.34  ? 172 GLU   A N   1 
ATOM   1041 C  CA  . GLU   A 1 144 ? 19.062  -13.767 47.468  1.00 59.56  ? 172 GLU   A CA  1 
ATOM   1042 C  C   . GLU   A 1 144 ? 19.343  -12.471 48.232  1.00 58.22  ? 172 GLU   A C   1 
ATOM   1043 O  O   . GLU   A 1 144 ? 20.487  -12.006 48.280  1.00 61.46  ? 172 GLU   A O   1 
ATOM   1044 C  CB  . GLU   A 1 144 ? 19.945  -13.855 46.215  1.00 56.37  ? 172 GLU   A CB  1 
ATOM   1045 N  N   . ALA   A 1 145 ? 18.318  -11.885 48.853  1.00 57.16  ? 173 ALA   A N   1 
ATOM   1046 C  CA  . ALA   A 1 145 ? 18.422  -10.557 49.452  1.00 54.69  ? 173 ALA   A CA  1 
ATOM   1047 C  C   . ALA   A 1 145 ? 18.113  -10.523 50.940  1.00 52.98  ? 173 ALA   A C   1 
ATOM   1048 O  O   . ALA   A 1 145 ? 18.719  -9.736  51.675  1.00 55.87  ? 173 ALA   A O   1 
ATOM   1049 C  CB  . ALA   A 1 145 ? 17.488  -9.581  48.727  1.00 50.45  ? 173 ALA   A CB  1 
ATOM   1050 N  N   . VAL   A 1 146 ? 17.175  -11.332 51.412  1.00 51.21  ? 174 VAL   A N   1 
ATOM   1051 C  CA  . VAL   A 1 146 ? 16.772  -11.299 52.811  1.00 48.01  ? 174 VAL   A CA  1 
ATOM   1052 C  C   . VAL   A 1 146 ? 16.518  -12.724 53.251  1.00 45.09  ? 174 VAL   A C   1 
ATOM   1053 O  O   . VAL   A 1 146 ? 16.015  -13.548 52.481  1.00 50.97  ? 174 VAL   A O   1 
ATOM   1054 C  CB  . VAL   A 1 146 ? 15.521  -10.417 53.039  1.00 46.99  ? 174 VAL   A CB  1 
ATOM   1055 C  CG1 . VAL   A 1 146 ? 14.371  -10.996 52.330  1.00 47.21  ? 174 VAL   A CG1 1 
ATOM   1056 C  CG2 . VAL   A 1 146 ? 15.178  -10.312 54.519  1.00 46.97  ? 174 VAL   A CG2 1 
ATOM   1057 N  N   . THR   A 1 147 ? 16.872  -13.015 54.487  1.00 42.77  ? 175 THR   A N   1 
ATOM   1058 C  CA  . THR   A 1 147 ? 16.728  -14.347 55.031  1.00 43.61  ? 175 THR   A CA  1 
ATOM   1059 C  C   . THR   A 1 147 ? 15.774  -14.273 56.207  1.00 39.45  ? 175 THR   A C   1 
ATOM   1060 O  O   . THR   A 1 147 ? 15.881  -13.376 57.045  1.00 36.50  ? 175 THR   A O   1 
ATOM   1061 C  CB  . THR   A 1 147 ? 18.091  -14.903 55.458  1.00 41.77  ? 175 THR   A CB  1 
ATOM   1062 O  OG1 . THR   A 1 147 ? 18.951  -14.937 54.311  1.00 39.55  ? 175 THR   A OG1 1 
ATOM   1063 C  CG2 . THR   A 1 147 ? 17.939  -16.290 56.021  1.00 33.88  ? 175 THR   A CG2 1 
ATOM   1064 N  N   . ILE   A 1 148 ? 14.838  -15.209 56.260  1.00 37.70  ? 176 ILE   A N   1 
ATOM   1065 C  CA  . ILE   A 1 148 ? 13.817  -15.222 57.294  1.00 37.47  ? 176 ILE   A CA  1 
ATOM   1066 C  C   . ILE   A 1 148 ? 13.745  -16.621 57.886  1.00 36.17  ? 176 ILE   A C   1 
ATOM   1067 O  O   . ILE   A 1 148 ? 13.912  -17.617 57.173  1.00 33.63  ? 176 ILE   A O   1 
ATOM   1068 C  CB  . ILE   A 1 148 ? 12.454  -14.768 56.731  1.00 37.84  ? 176 ILE   A CB  1 
ATOM   1069 C  CG1 . ILE   A 1 148 ? 11.366  -14.843 57.784  1.00 35.88  ? 176 ILE   A CG1 1 
ATOM   1070 C  CG2 . ILE   A 1 148 ? 12.048  -15.603 55.534  1.00 38.07  ? 176 ILE   A CG2 1 
ATOM   1071 C  CD1 . ILE   A 1 148 ? 10.103  -14.111 57.338  1.00 36.08  ? 176 ILE   A CD1 1 
ATOM   1072 N  N   . ALA   A 1 149 ? 13.510  -16.689 59.193  1.00 29.83  ? 177 ALA   A N   1 
ATOM   1073 C  CA  . ALA   A 1 149 ? 13.447  -17.946 59.907  1.00 28.88  ? 177 ALA   A CA  1 
ATOM   1074 C  C   . ALA   A 1 149 ? 12.624  -17.719 61.159  1.00 30.72  ? 177 ALA   A C   1 
ATOM   1075 O  O   . ALA   A 1 149 ? 12.548  -16.597 61.663  1.00 30.59  ? 177 ALA   A O   1 
ATOM   1076 C  CB  . ALA   A 1 149 ? 14.848  -18.457 60.264  1.00 29.91  ? 177 ALA   A CB  1 
ATOM   1077 N  N   . GLU   A 1 150 ? 12.019  -18.798 61.667  1.00 29.34  ? 178 GLU   A N   1 
ATOM   1078 C  CA  . GLU   A 1 150 ? 11.081  -18.687 62.772  1.00 30.65  ? 178 GLU   A CA  1 
ATOM   1079 C  C   . GLU   A 1 150 ? 11.275  -19.827 63.750  1.00 33.07  ? 178 GLU   A C   1 
ATOM   1080 O  O   . GLU   A 1 150 ? 11.483  -20.978 63.347  1.00 34.39  ? 178 GLU   A O   1 
ATOM   1081 C  CB  . GLU   A 1 150 ? 9.618   -18.677 62.253  1.00 28.19  ? 178 GLU   A CB  1 
ATOM   1082 C  CG  . GLU   A 1 150 ? 9.281   -17.376 61.547  1.00 29.32  ? 178 GLU   A CG  1 
ATOM   1083 C  CD  . GLU   A 1 150 ? 7.986   -17.439 60.742  1.00 33.86  ? 178 GLU   A CD  1 
ATOM   1084 O  OE1 . GLU   A 1 150 ? 7.058   -18.173 61.151  1.00 32.95  ? 178 GLU   A OE1 1 
ATOM   1085 O  OE2 . GLU   A 1 150 ? 7.913   -16.762 59.689  1.00 28.01  ? 178 GLU   A OE2 1 
ATOM   1086 N  N   . VAL   A 1 151 ? 11.167  -19.503 65.035  1.00 31.11  ? 179 VAL   A N   1 
ATOM   1087 C  CA  . VAL   A 1 151 ? 11.135  -20.493 66.105  1.00 33.41  ? 179 VAL   A CA  1 
ATOM   1088 C  C   . VAL   A 1 151 ? 9.953   -20.162 67.004  1.00 35.97  ? 179 VAL   A C   1 
ATOM   1089 O  O   . VAL   A 1 151 ? 9.535   -19.005 67.104  1.00 33.92  ? 179 VAL   A O   1 
ATOM   1090 C  CB  . VAL   A 1 151 ? 12.451  -20.523 66.921  1.00 32.83  ? 179 VAL   A CB  1 
ATOM   1091 C  CG1 . VAL   A 1 151 ? 13.623  -20.872 66.018  1.00 28.18  ? 179 VAL   A CG1 1 
ATOM   1092 C  CG2 . VAL   A 1 151 ? 12.686  -19.180 67.616  1.00 29.48  ? 179 VAL   A CG2 1 
ATOM   1093 N  N   . LYS   A 1 152 ? 9.409   -21.182 67.658  1.00 34.62  ? 180 LYS   A N   1 
ATOM   1094 C  CA  . LYS   A 1 152 ? 8.324   -20.955 68.602  1.00 31.51  ? 180 LYS   A CA  1 
ATOM   1095 C  C   . LYS   A 1 152 ? 8.763   -20.059 69.757  1.00 36.82  ? 180 LYS   A C   1 
ATOM   1096 O  O   . LYS   A 1 152 ? 9.832   -20.261 70.347  1.00 34.71  ? 180 LYS   A O   1 
ATOM   1097 C  CB  . LYS   A 1 152 ? 7.816   -22.284 69.129  1.00 32.27  ? 180 LYS   A CB  1 
ATOM   1098 C  CG  . LYS   A 1 152 ? 7.217   -23.142 68.064  1.00 30.58  ? 180 LYS   A CG  1 
ATOM   1099 C  CD  . LYS   A 1 152 ? 6.562   -24.356 68.707  1.00 38.86  ? 180 LYS   A CD  1 
ATOM   1100 C  CE  . LYS   A 1 152 ? 5.731   -25.139 67.713  1.00 43.89  ? 180 LYS   A CE  1 
ATOM   1101 N  NZ  . LYS   A 1 152 ? 4.702   -25.929 68.448  1.00 49.80  ? 180 LYS   A NZ  1 
ATOM   1102 N  N   . LEU   A 1 153 ? 7.933   -19.055 70.077  1.00 32.80  ? 181 LEU   A N   1 
ATOM   1103 C  CA  . LEU   A 1 153 ? 8.208   -18.164 71.207  1.00 32.66  ? 181 LEU   A CA  1 
ATOM   1104 C  C   . LEU   A 1 153 ? 7.396   -18.565 72.434  1.00 33.38  ? 181 LEU   A C   1 
ATOM   1105 O  O   . LEU   A 1 153 ? 7.965   -18.905 73.476  1.00 30.77  ? 181 LEU   A O   1 
ATOM   1106 C  CB  . LEU   A 1 153 ? 7.932   -16.699 70.822  1.00 30.53  ? 181 LEU   A CB  1 
ATOM   1107 C  CG  . LEU   A 1 153 ? 8.270   -15.605 71.848  1.00 37.36  ? 181 LEU   A CG  1 
ATOM   1108 C  CD1 . LEU   A 1 153 ? 9.760   -15.638 72.282  1.00 29.94  ? 181 LEU   A CD1 1 
ATOM   1109 C  CD2 . LEU   A 1 153 ? 7.854   -14.167 71.354  1.00 26.80  ? 181 LEU   A CD2 1 
ATOM   1110 N  N   . TYR   A 1 154 ? 6.070   -18.538 72.321  1.00 25.89  ? 182 TYR   A N   1 
ATOM   1111 C  CA  . TYR   A 1 154 ? 5.179   -19.077 73.337  1.00 28.14  ? 182 TYR   A CA  1 
ATOM   1112 C  C   . TYR   A 1 154 ? 3.794   -19.213 72.707  1.00 29.86  ? 182 TYR   A C   1 
ATOM   1113 O  O   . TYR   A 1 154 ? 3.442   -18.467 71.790  1.00 31.47  ? 182 TYR   A O   1 
ATOM   1114 C  CB  . TYR   A 1 154 ? 5.136   -18.203 74.603  1.00 25.15  ? 182 TYR   A CB  1 
ATOM   1115 C  CG  . TYR   A 1 154 ? 5.243   -16.702 74.351  1.00 30.20  ? 182 TYR   A CG  1 
ATOM   1116 C  CD1 . TYR   A 1 154 ? 4.294   -16.024 73.591  1.00 27.40  ? 182 TYR   A CD1 1 
ATOM   1117 C  CD2 . TYR   A 1 154 ? 6.304   -15.970 74.877  1.00 30.61  ? 182 TYR   A CD2 1 
ATOM   1118 C  CE1 . TYR   A 1 154 ? 4.402   -14.647 73.360  1.00 27.87  ? 182 TYR   A CE1 1 
ATOM   1119 C  CE2 . TYR   A 1 154 ? 6.424   -14.593 74.654  1.00 32.93  ? 182 TYR   A CE2 1 
ATOM   1120 C  CZ  . TYR   A 1 154 ? 5.480   -13.936 73.899  1.00 32.74  ? 182 TYR   A CZ  1 
ATOM   1121 O  OH  . TYR   A 1 154 ? 5.635   -12.575 73.702  1.00 30.67  ? 182 TYR   A OH  1 
ATOM   1122 N  N   . GLY   A 1 155 ? 3.029   -20.188 73.186  1.00 30.57  ? 183 GLY   A N   1 
ATOM   1123 C  CA  . GLY   A 1 155 ? 1.743   -20.469 72.567  1.00 32.56  ? 183 GLY   A CA  1 
ATOM   1124 C  C   . GLY   A 1 155 ? 1.914   -20.701 71.081  1.00 32.69  ? 183 GLY   A C   1 
ATOM   1125 O  O   . GLY   A 1 155 ? 2.759   -21.488 70.652  1.00 25.66  ? 183 GLY   A O   1 
ATOM   1126 N  N   . ASP   A 1 156 ? 1.147   -19.977 70.262  1.00 29.46  ? 184 ASP   A N   1 
ATOM   1127 C  CA  . ASP   A 1 156 ? 1.323   -20.043 68.816  1.00 28.87  ? 184 ASP   A CA  1 
ATOM   1128 C  C   . ASP   A 1 156 ? 2.021   -18.804 68.267  1.00 31.39  ? 184 ASP   A C   1 
ATOM   1129 O  O   . ASP   A 1 156 ? 1.879   -18.487 67.080  1.00 31.73  ? 184 ASP   A O   1 
ATOM   1130 C  CB  . ASP   A 1 156 ? -0.019  -20.246 68.117  1.00 34.24  ? 184 ASP   A CB  1 
ATOM   1131 C  CG  . ASP   A 1 156 ? -0.673  -21.570 68.481  1.00 31.97  ? 184 ASP   A CG  1 
ATOM   1132 O  OD1 . ASP   A 1 156 ? 0.031   -22.589 68.579  1.00 34.40  ? 184 ASP   A OD1 1 
ATOM   1133 O  OD2 . ASP   A 1 156 ? -1.896  -21.580 68.687  1.00 38.67  ? 184 ASP   A OD2 1 
ATOM   1134 N  N   . VAL   A 1 157 ? 2.773   -18.104 69.099  1.00 28.89  ? 185 VAL   A N   1 
ATOM   1135 C  CA  . VAL   A 1 157 ? 3.519   -16.932 68.660  1.00 30.06  ? 185 VAL   A CA  1 
ATOM   1136 C  C   . VAL   A 1 157 ? 4.938   -17.372 68.338  1.00 32.42  ? 185 VAL   A C   1 
ATOM   1137 O  O   . VAL   A 1 157 ? 5.581   -18.054 69.146  1.00 36.34  ? 185 VAL   A O   1 
ATOM   1138 C  CB  . VAL   A 1 157 ? 3.507   -15.836 69.741  1.00 26.10  ? 185 VAL   A CB  1 
ATOM   1139 C  CG1 . VAL   A 1 157 ? 4.369   -14.643 69.321  1.00 26.02  ? 185 VAL   A CG1 1 
ATOM   1140 C  CG2 . VAL   A 1 157 ? 2.069   -15.406 70.027  1.00 26.54  ? 185 VAL   A CG2 1 
ATOM   1141 N  N   . VAL   A 1 158 ? 5.428   -16.990 67.153  1.00 30.26  ? 186 VAL   A N   1 
ATOM   1142 C  CA  . VAL   A 1 158 ? 6.793   -17.291 66.736  1.00 33.60  ? 186 VAL   A CA  1 
ATOM   1143 C  C   . VAL   A 1 158 ? 7.669   -16.058 66.914  1.00 31.81  ? 186 VAL   A C   1 
ATOM   1144 O  O   . VAL   A 1 158 ? 7.223   -14.919 66.704  1.00 30.74  ? 186 VAL   A O   1 
ATOM   1145 C  CB  . VAL   A 1 158 ? 6.834   -17.789 65.276  1.00 34.46  ? 186 VAL   A CB  1 
ATOM   1146 C  CG1 . VAL   A 1 158 ? 6.039   -19.081 65.132  1.00 32.66  ? 186 VAL   A CG1 1 
ATOM   1147 C  CG2 . VAL   A 1 158 ? 6.325   -16.707 64.317  1.00 29.97  ? 186 VAL   A CG2 1 
ATOM   1148 N  N   . LEU   A 1 159 ? 8.921   -16.279 67.312  1.00 34.24  ? 187 LEU   A N   1 
ATOM   1149 C  CA  . LEU   A 1 159 ? 9.948   -15.244 67.219  1.00 33.32  ? 187 LEU   A CA  1 
ATOM   1150 C  C   . LEU   A 1 159 ? 10.580  -15.361 65.842  1.00 35.17  ? 187 LEU   A C   1 
ATOM   1151 O  O   . LEU   A 1 159 ? 11.121  -16.416 65.498  1.00 33.96  ? 187 LEU   A O   1 
ATOM   1152 C  CB  . LEU   A 1 159 ? 11.006  -15.396 68.307  1.00 32.84  ? 187 LEU   A CB  1 
ATOM   1153 C  CG  . LEU   A 1 159 ? 12.086  -14.318 68.348  1.00 30.55  ? 187 LEU   A CG  1 
ATOM   1154 C  CD1 . LEU   A 1 159 ? 11.520  -13.000 68.849  1.00 27.09  ? 187 LEU   A CD1 1 
ATOM   1155 C  CD2 . LEU   A 1 159 ? 13.255  -14.792 69.234  1.00 27.66  ? 187 LEU   A CD2 1 
ATOM   1156 N  N   . ARG   A 1 160 ? 10.482  -14.302 65.045  1.00 30.98  ? 188 ARG   A N   1 
ATOM   1157 C  CA  . ARG   A 1 160 ? 10.885  -14.341 63.644  1.00 28.08  ? 188 ARG   A CA  1 
ATOM   1158 C  C   . ARG   A 1 160 ? 12.190  -13.576 63.456  1.00 36.40  ? 188 ARG   A C   1 
ATOM   1159 O  O   . ARG   A 1 160 ? 12.239  -12.364 63.713  1.00 29.12  ? 188 ARG   A O   1 
ATOM   1160 C  CB  . ARG   A 1 160 ? 9.793   -13.742 62.769  1.00 32.34  ? 188 ARG   A CB  1 
ATOM   1161 C  CG  . ARG   A 1 160 ? 10.211  -13.558 61.342  1.00 33.27  ? 188 ARG   A CG  1 
ATOM   1162 C  CD  . ARG   A 1 160 ? 9.069   -12.980 60.555  1.00 28.04  ? 188 ARG   A CD  1 
ATOM   1163 N  NE  . ARG   A 1 160 ? 8.016   -13.957 60.265  1.00 26.09  ? 188 ARG   A NE  1 
ATOM   1164 C  CZ  . ARG   A 1 160 ? 6.754   -13.601 60.029  1.00 24.82  ? 188 ARG   A CZ  1 
ATOM   1165 N  NH1 . ARG   A 1 160 ? 6.410   -12.314 60.068  1.00 21.36  ? 188 ARG   A NH1 1 
ATOM   1166 N  NH2 . ARG   A 1 160 ? 5.835   -14.515 59.763  1.00 23.09  ? 188 ARG   A NH2 1 
ATOM   1167 N  N   . TYR   A 1 161 ? 13.235  -14.273 62.987  1.00 28.67  ? 189 TYR   A N   1 
ATOM   1168 C  CA  . TYR   A 1 161 ? 14.504  -13.622 62.676  1.00 34.70  ? 189 TYR   A CA  1 
ATOM   1169 C  C   . TYR   A 1 161 ? 14.501  -13.141 61.235  1.00 31.55  ? 189 TYR   A C   1 
ATOM   1170 O  O   . TYR   A 1 161 ? 14.127  -13.882 60.327  1.00 34.68  ? 189 TYR   A O   1 
ATOM   1171 C  CB  . TYR   A 1 161 ? 15.694  -14.571 62.880  1.00 33.19  ? 189 TYR   A CB  1 
ATOM   1172 C  CG  . TYR   A 1 161 ? 15.740  -15.229 64.236  1.00 30.42  ? 189 TYR   A CG  1 
ATOM   1173 C  CD1 . TYR   A 1 161 ? 15.533  -14.488 65.402  1.00 29.98  ? 189 TYR   A CD1 1 
ATOM   1174 C  CD2 . TYR   A 1 161 ? 15.983  -16.596 64.356  1.00 32.43  ? 189 TYR   A CD2 1 
ATOM   1175 C  CE1 . TYR   A 1 161 ? 15.570  -15.094 66.652  1.00 31.95  ? 189 TYR   A CE1 1 
ATOM   1176 C  CE2 . TYR   A 1 161 ? 16.016  -17.210 65.593  1.00 29.56  ? 189 TYR   A CE2 1 
ATOM   1177 C  CZ  . TYR   A 1 161 ? 15.817  -16.459 66.736  1.00 31.16  ? 189 TYR   A CZ  1 
ATOM   1178 O  OH  . TYR   A 1 161 ? 15.831  -17.083 67.960  1.00 29.96  ? 189 TYR   A OH  1 
ATOM   1179 N  N   . VAL   A 1 162 ? 14.958  -11.910 61.024  1.00 35.13  ? 190 VAL   A N   1 
ATOM   1180 C  CA  . VAL   A 1 162 ? 15.106  -11.350 59.688  1.00 33.39  ? 190 VAL   A CA  1 
ATOM   1181 C  C   . VAL   A 1 162 ? 16.505  -10.771 59.571  1.00 39.83  ? 190 VAL   A C   1 
ATOM   1182 O  O   . VAL   A 1 162 ? 17.010  -10.167 60.523  1.00 38.66  ? 190 VAL   A O   1 
ATOM   1183 C  CB  . VAL   A 1 162 ? 14.032  -10.283 59.410  1.00 36.31  ? 190 VAL   A CB  1 
ATOM   1184 C  CG1 . VAL   A 1 162 ? 14.453  -9.396  58.283  1.00 44.35  ? 190 VAL   A CG1 1 
ATOM   1185 C  CG2 . VAL   A 1 162 ? 12.723  -10.973 59.065  1.00 35.58  ? 190 VAL   A CG2 1 
ATOM   1186 N  N   . SER   A 1 163 ? 17.150  -10.985 58.422  1.00 40.03  ? 191 SER   A N   1 
ATOM   1187 C  CA  . SER   A 1 163 ? 18.456  -10.385 58.177  1.00 42.40  ? 191 SER   A CA  1 
ATOM   1188 C  C   . SER   A 1 163 ? 18.557  -9.983  56.712  1.00 42.37  ? 191 SER   A C   1 
ATOM   1189 O  O   . SER   A 1 163 ? 17.986  -10.631 55.833  1.00 43.97  ? 191 SER   A O   1 
ATOM   1190 C  CB  . SER   A 1 163 ? 19.616  -11.337 58.569  1.00 41.42  ? 191 SER   A CB  1 
ATOM   1191 O  OG  . SER   A 1 163 ? 19.659  -12.493 57.743  1.00 36.42  ? 191 SER   A OG  1 
ATOM   1192 N  N   . TYR   A 1 164 ? 19.281  -8.896  56.467  1.00 44.82  ? 192 TYR   A N   1 
ATOM   1193 C  CA  . TYR   A 1 164 ? 19.457  -8.323  55.139  1.00 52.70  ? 192 TYR   A CA  1 
ATOM   1194 C  C   . TYR   A 1 164 ? 20.930  -8.358  54.764  1.00 54.30  ? 192 TYR   A C   1 
ATOM   1195 O  O   . TYR   A 1 164 ? 21.787  -7.984  55.572  1.00 50.25  ? 192 TYR   A O   1 
ATOM   1196 C  CB  . TYR   A 1 164 ? 18.951  -6.868  55.075  1.00 49.22  ? 192 TYR   A CB  1 
ATOM   1197 C  CG  . TYR   A 1 164 ? 17.483  -6.732  55.392  1.00 51.15  ? 192 TYR   A CG  1 
ATOM   1198 C  CD1 . TYR   A 1 164 ? 16.538  -6.692  54.370  1.00 51.84  ? 192 TYR   A CD1 1 
ATOM   1199 C  CD2 . TYR   A 1 164 ? 17.037  -6.659  56.703  1.00 47.61  ? 192 TYR   A CD2 1 
ATOM   1200 C  CE1 . TYR   A 1 164 ? 15.193  -6.591  54.643  1.00 49.99  ? 192 TYR   A CE1 1 
ATOM   1201 C  CE2 . TYR   A 1 164 ? 15.693  -6.548  56.989  1.00 51.37  ? 192 TYR   A CE2 1 
ATOM   1202 C  CZ  . TYR   A 1 164 ? 14.772  -6.523  55.952  1.00 55.28  ? 192 TYR   A CZ  1 
ATOM   1203 O  OH  . TYR   A 1 164 ? 13.421  -6.426  56.217  1.00 56.24  ? 192 TYR   A OH  1 
ATOM   1204 N  N   . LYS   A 1 165 ? 21.223  -8.792  53.537  1.00 54.00  ? 193 LYS   A N   1 
ATOM   1205 C  CA  . LYS   A 1 165 ? 22.564  -8.592  53.002  1.00 58.80  ? 193 LYS   A CA  1 
ATOM   1206 C  C   . LYS   A 1 165 ? 22.877  -7.099  52.900  1.00 57.73  ? 193 LYS   A C   1 
ATOM   1207 O  O   . LYS   A 1 165 ? 23.867  -6.613  53.461  1.00 63.66  ? 193 LYS   A O   1 
ATOM   1208 C  CB  . LYS   A 1 165 ? 22.699  -9.286  51.643  1.00 53.30  ? 193 LYS   A CB  1 
ATOM   1209 N  N   . ALA   A 1 166 ? 22.016  -6.347  52.222  1.00 55.11  ? 194 ALA   A N   1 
ATOM   1210 C  CA  . ALA   A 1 166 ? 22.197  -4.904  52.088  1.00 61.14  ? 194 ALA   A CA  1 
ATOM   1211 C  C   . ALA   A 1 166 ? 21.659  -4.128  53.296  1.00 56.92  ? 194 ALA   A C   1 
ATOM   1212 O  O   . ALA   A 1 166 ? 21.897  -4.493  54.449  1.00 57.16  ? 194 ALA   A O   1 
ATOM   1213 C  CB  . ALA   A 1 166 ? 21.525  -4.410  50.810  1.00 62.00  ? 194 ALA   A CB  1 
ATOM   1214 N  N   . GLU   A 1 173 ? 10.965  -1.665  50.619  1.00 66.50  ? 201 GLU   A N   1 
ATOM   1215 C  CA  . GLU   A 1 173 ? 12.183  -2.396  50.965  1.00 62.10  ? 201 GLU   A CA  1 
ATOM   1216 C  C   . GLU   A 1 173 ? 11.915  -3.403  52.088  1.00 58.05  ? 201 GLU   A C   1 
ATOM   1217 O  O   . GLU   A 1 173 ? 12.841  -4.037  52.597  1.00 61.15  ? 201 GLU   A O   1 
ATOM   1218 C  CB  . GLU   A 1 173 ? 13.296  -1.423  51.379  1.00 50.17  ? 201 GLU   A CB  1 
ATOM   1219 N  N   . PHE   A 1 174 ? 10.646  -3.539  52.478  1.00 53.74  ? 202 PHE   A N   1 
ATOM   1220 C  CA  . PHE   A 1 174 ? 10.285  -4.401  53.597  1.00 47.39  ? 202 PHE   A CA  1 
ATOM   1221 C  C   . PHE   A 1 174 ? 10.705  -5.840  53.307  1.00 47.17  ? 202 PHE   A C   1 
ATOM   1222 O  O   . PHE   A 1 174 ? 11.629  -6.355  53.937  1.00 47.29  ? 202 PHE   A O   1 
ATOM   1223 C  CB  . PHE   A 1 174 ? 8.784   -4.291  53.886  1.00 46.59  ? 202 PHE   A CB  1 
ATOM   1224 C  CG  . PHE   A 1 174 ? 8.299   -5.217  54.968  1.00 45.06  ? 202 PHE   A CG  1 
ATOM   1225 C  CD1 . PHE   A 1 174 ? 8.744   -5.080  56.270  1.00 39.62  ? 202 PHE   A CD1 1 
ATOM   1226 C  CD2 . PHE   A 1 174 ? 7.384   -6.222  54.681  1.00 40.43  ? 202 PHE   A CD2 1 
ATOM   1227 C  CE1 . PHE   A 1 174 ? 8.291   -5.937  57.270  1.00 41.90  ? 202 PHE   A CE1 1 
ATOM   1228 C  CE2 . PHE   A 1 174 ? 6.934   -7.092  55.675  1.00 35.09  ? 202 PHE   A CE2 1 
ATOM   1229 C  CZ  . PHE   A 1 174 ? 7.381   -6.953  56.966  1.00 34.57  ? 202 PHE   A CZ  1 
ATOM   1230 N  N   . LEU   A 1 175 ? 10.066  -6.491  52.348  1.00 45.46  ? 203 LEU   A N   1 
ATOM   1231 C  CA  . LEU   A 1 175 ? 10.430  -7.842  51.958  1.00 46.07  ? 203 LEU   A CA  1 
ATOM   1232 C  C   . LEU   A 1 175 ? 10.308  -7.968  50.449  1.00 46.10  ? 203 LEU   A C   1 
ATOM   1233 O  O   . LEU   A 1 175 ? 9.550   -7.224  49.818  1.00 50.01  ? 203 LEU   A O   1 
ATOM   1234 C  CB  . LEU   A 1 175 ? 9.543   -8.897  52.637  1.00 46.44  ? 203 LEU   A CB  1 
ATOM   1235 C  CG  . LEU   A 1 175 ? 9.763   -9.212  54.119  1.00 46.29  ? 203 LEU   A CG  1 
ATOM   1236 C  CD1 . LEU   A 1 175 ? 8.751   -10.250 54.613  1.00 35.99  ? 203 LEU   A CD1 1 
ATOM   1237 C  CD2 . LEU   A 1 175 ? 11.184  -9.692  54.346  1.00 49.78  ? 203 LEU   A CD2 1 
ATOM   1238 N  N   . PRO   A 1 176 ? 11.055  -8.888  49.840  1.00 47.04  ? 204 PRO   A N   1 
ATOM   1239 C  CA  . PRO   A 1 176 ? 10.825  -9.203  48.429  1.00 50.36  ? 204 PRO   A CA  1 
ATOM   1240 C  C   . PRO   A 1 176 ? 9.382   -9.620  48.190  1.00 49.78  ? 204 PRO   A C   1 
ATOM   1241 O  O   . PRO   A 1 176 ? 8.733   -10.235 49.042  1.00 46.65  ? 204 PRO   A O   1 
ATOM   1242 C  CB  . PRO   A 1 176 ? 11.797  -10.359 48.164  1.00 47.72  ? 204 PRO   A CB  1 
ATOM   1243 C  CG  . PRO   A 1 176 ? 12.916  -10.113 49.118  1.00 45.96  ? 204 PRO   A CG  1 
ATOM   1244 C  CD  . PRO   A 1 176 ? 12.249  -9.565  50.360  1.00 48.21  ? 204 PRO   A CD  1 
ATOM   1245 N  N   . GLY   A 1 177 ? 8.882   -9.280  47.006  1.00 54.17  ? 205 GLY   A N   1 
ATOM   1246 C  CA  . GLY   A 1 177 ? 7.510   -9.567  46.649  1.00 48.31  ? 205 GLY   A CA  1 
ATOM   1247 C  C   . GLY   A 1 177 ? 6.509   -8.566  47.166  1.00 41.84  ? 205 GLY   A C   1 
ATOM   1248 O  O   . GLY   A 1 177 ? 5.364   -8.568  46.711  1.00 45.77  ? 205 GLY   A O   1 
ATOM   1249 N  N   . PHE   A 1 178 ? 6.897   -7.713  48.112  1.00 44.77  ? 206 PHE   A N   1 
ATOM   1250 C  CA  . PHE   A 1 178 ? 6.041   -6.608  48.502  1.00 44.30  ? 206 PHE   A CA  1 
ATOM   1251 C  C   . PHE   A 1 178 ? 6.262   -5.446  47.544  1.00 45.94  ? 206 PHE   A C   1 
ATOM   1252 O  O   . PHE   A 1 178 ? 7.309   -5.330  46.908  1.00 52.78  ? 206 PHE   A O   1 
ATOM   1253 C  CB  . PHE   A 1 178 ? 6.324   -6.177  49.943  1.00 42.52  ? 206 PHE   A CB  1 
ATOM   1254 C  CG  . PHE   A 1 178 ? 5.758   -7.112  50.996  1.00 37.03  ? 206 PHE   A CG  1 
ATOM   1255 C  CD1 . PHE   A 1 178 ? 6.368   -8.323  51.271  1.00 35.60  ? 206 PHE   A CD1 1 
ATOM   1256 C  CD2 . PHE   A 1 178 ? 4.635   -6.753  51.733  1.00 32.96  ? 206 PHE   A CD2 1 
ATOM   1257 C  CE1 . PHE   A 1 178 ? 5.863   -9.174  52.245  1.00 37.18  ? 206 PHE   A CE1 1 
ATOM   1258 C  CE2 . PHE   A 1 178 ? 4.117   -7.604  52.708  1.00 36.01  ? 206 PHE   A CE2 1 
ATOM   1259 C  CZ  . PHE   A 1 178 ? 4.734   -8.819  52.955  1.00 40.51  ? 206 PHE   A CZ  1 
ATOM   1260 N  N   . GLU   A 1 179 ? 5.258   -4.595  47.424  1.00 45.17  ? 207 GLU   A N   1 
ATOM   1261 C  CA  . GLU   A 1 179 ? 5.363   -3.387  46.628  1.00 44.71  ? 207 GLU   A CA  1 
ATOM   1262 C  C   . GLU   A 1 179 ? 5.039   -2.194  47.504  1.00 46.50  ? 207 GLU   A C   1 
ATOM   1263 O  O   . GLU   A 1 179 ? 4.198   -2.292  48.403  1.00 46.65  ? 207 GLU   A O   1 
ATOM   1264 C  CB  . GLU   A 1 179 ? 4.428   -3.426  45.431  1.00 48.02  ? 207 GLU   A CB  1 
ATOM   1265 C  CG  . GLU   A 1 179 ? 4.542   -4.692  44.625  1.00 52.31  ? 207 GLU   A CG  1 
ATOM   1266 C  CD  . GLU   A 1 179 ? 3.758   -4.617  43.335  1.00 56.67  ? 207 GLU   A CD  1 
ATOM   1267 O  OE1 . GLU   A 1 179 ? 3.904   -5.545  42.504  1.00 58.95  ? 207 GLU   A OE1 1 
ATOM   1268 O  OE2 . GLU   A 1 179 ? 3.010   -3.625  43.152  1.00 52.15  ? 207 GLU   A OE2 1 
ATOM   1269 N  N   . ARG   A 1 180 ? 5.747   -1.088  47.265  1.00 49.78  ? 208 ARG   A N   1 
ATOM   1270 C  CA  . ARG   A 1 180 ? 5.358   0.187   47.845  1.00 56.26  ? 208 ARG   A CA  1 
ATOM   1271 C  C   . ARG   A 1 180 ? 3.970   0.562   47.334  1.00 51.62  ? 208 ARG   A C   1 
ATOM   1272 O  O   . ARG   A 1 180 ? 3.593   0.240   46.202  1.00 56.74  ? 208 ARG   A O   1 
ATOM   1273 C  CB  . ARG   A 1 180 ? 6.385   1.273   47.494  1.00 49.61  ? 208 ARG   A CB  1 
ATOM   1274 N  N   . VAL   A 1 181 ? 3.190   1.215   48.188  1.00 55.16  ? 209 VAL   A N   1 
ATOM   1275 C  CA  . VAL   A 1 181 ? 1.777   1.451   47.902  1.00 56.21  ? 209 VAL   A CA  1 
ATOM   1276 C  C   . VAL   A 1 181 ? 1.612   2.764   47.149  1.00 66.27  ? 209 VAL   A C   1 
ATOM   1277 O  O   . VAL   A 1 181 ? 2.358   3.729   47.379  1.00 61.51  ? 209 VAL   A O   1 
ATOM   1278 C  CB  . VAL   A 1 181 ? 0.945   1.453   49.199  1.00 54.16  ? 209 VAL   A CB  1 
ATOM   1279 C  CG1 . VAL   A 1 181 ? -0.529  1.602   48.885  1.00 59.21  ? 209 VAL   A CG1 1 
ATOM   1280 C  CG2 . VAL   A 1 181 ? 1.154   0.179   49.957  1.00 52.03  ? 209 VAL   A CG2 1 
ATOM   1281 N  N   . GLU   A 1 182 ? 0.633   2.779   46.230  1.00 67.89  ? 210 GLU   A N   1 
ATOM   1282 C  CA  . GLU   A 1 182 ? 0.078   3.966   45.587  1.00 62.52  ? 210 GLU   A CA  1 
ATOM   1283 C  C   . GLU   A 1 182 ? 0.031   5.154   46.533  1.00 66.66  ? 210 GLU   A C   1 
ATOM   1284 O  O   . GLU   A 1 182 ? -0.684  5.113   47.540  1.00 67.91  ? 210 GLU   A O   1 
ATOM   1285 C  CB  . GLU   A 1 182 ? -1.349  3.692   45.101  1.00 69.23  ? 210 GLU   A CB  1 
ATOM   1286 C  CG  . GLU   A 1 182 ? -1.519  2.610   44.048  1.00 72.12  ? 210 GLU   A CG  1 
ATOM   1287 C  CD  . GLU   A 1 182 ? -2.843  2.754   43.299  1.00 78.29  ? 210 GLU   A CD  1 
ATOM   1288 O  OE1 . GLU   A 1 182 ? -2.822  2.738   42.048  1.00 78.02  ? 210 GLU   A OE1 1 
ATOM   1289 O  OE2 . GLU   A 1 182 ? -3.900  2.899   43.960  1.00 72.62  ? 210 GLU   A OE2 1 
ATOM   1290 N  N   . ASP   A 1 183 ? 0.759   6.227   46.218  1.00 71.06  ? 211 ASP   A N   1 
ATOM   1291 C  CA  . ASP   A 1 183 ? 0.727   7.394   47.092  1.00 68.29  ? 211 ASP   A CA  1 
ATOM   1292 C  C   . ASP   A 1 183 ? -0.681  7.951   47.256  1.00 68.27  ? 211 ASP   A C   1 
ATOM   1293 O  O   . ASP   A 1 183 ? -0.947  8.641   48.246  1.00 73.67  ? 211 ASP   A O   1 
ATOM   1294 C  CB  . ASP   A 1 183 ? 1.666   8.481   46.568  1.00 71.46  ? 211 ASP   A CB  1 
ATOM   1295 C  CG  . ASP   A 1 183 ? 3.001   8.485   47.286  1.00 70.20  ? 211 ASP   A CG  1 
ATOM   1296 O  OD1 . ASP   A 1 183 ? 3.173   7.683   48.232  1.00 76.72  ? 211 ASP   A OD1 1 
ATOM   1297 O  OD2 . ASP   A 1 183 ? 3.873   9.295   46.919  1.00 69.15  ? 211 ASP   A OD2 1 
ATOM   1298 N  N   . ALA   A 1 184 ? -1.590  7.658   46.322  1.00 68.49  ? 212 ALA   A N   1 
ATOM   1299 C  CA  . ALA   A 1 184 ? -2.973  8.100   46.474  1.00 70.50  ? 212 ALA   A CA  1 
ATOM   1300 C  C   . ALA   A 1 184 ? -3.640  7.423   47.670  1.00 71.98  ? 212 ALA   A C   1 
ATOM   1301 O  O   . ALA   A 1 184 ? -4.324  8.083   48.461  1.00 69.35  ? 212 ALA   A O   1 
ATOM   1302 C  CB  . ALA   A 1 184 ? -3.759  7.831   45.187  1.00 69.99  ? 212 ALA   A CB  1 
ATOM   1303 N  N   . SER   A 1 185 ? -3.445  6.108   47.824  1.00 69.71  ? 213 SER   A N   1 
ATOM   1304 C  CA  . SER   A 1 185 ? -3.986  5.378   48.967  1.00 64.26  ? 213 SER   A CA  1 
ATOM   1305 C  C   . SER   A 1 185 ? -3.117  5.497   50.215  1.00 64.88  ? 213 SER   A C   1 
ATOM   1306 O  O   . SER   A 1 185 ? -3.570  5.129   51.304  1.00 61.85  ? 213 SER   A O   1 
ATOM   1307 C  CB  . SER   A 1 185 ? -4.163  3.896   48.617  1.00 67.16  ? 213 SER   A CB  1 
ATOM   1308 O  OG  . SER   A 1 185 ? -3.019  3.389   47.950  1.00 65.70  ? 213 SER   A OG  1 
ATOM   1309 N  N   . SER   A 1 186 ? -1.890  6.007   50.095  1.00 65.88  ? 214 SER   A N   1 
ATOM   1310 C  CA  . SER   A 1 186 ? -0.992  6.139   51.240  1.00 54.83  ? 214 SER   A CA  1 
ATOM   1311 C  C   . SER   A 1 186 ? -1.066  7.572   51.770  1.00 55.55  ? 214 SER   A C   1 
ATOM   1312 O  O   . SER   A 1 186 ? -0.183  8.399   51.534  1.00 58.96  ? 214 SER   A O   1 
ATOM   1313 C  CB  . SER   A 1 186 ? 0.427   5.745   50.849  1.00 58.25  ? 214 SER   A CB  1 
ATOM   1314 O  OG  . SER   A 1 186 ? 1.297   5.779   51.968  1.00 55.13  ? 214 SER   A OG  1 
ATOM   1315 N  N   . PHE   A 1 187 ? -2.142  7.856   52.513  1.00 51.05  ? 215 PHE   A N   1 
ATOM   1316 C  CA  . PHE   A 1 187 ? -2.286  9.156   53.173  1.00 49.22  ? 215 PHE   A CA  1 
ATOM   1317 C  C   . PHE   A 1 187 ? -1.352  9.213   54.378  1.00 48.55  ? 215 PHE   A C   1 
ATOM   1318 O  O   . PHE   A 1 187 ? -1.347  8.280   55.197  1.00 43.00  ? 215 PHE   A O   1 
ATOM   1319 C  CB  . PHE   A 1 187 ? -3.747  9.403   53.603  1.00 42.91  ? 215 PHE   A CB  1 
ATOM   1320 C  CG  . PHE   A 1 187 ? -3.953  10.679  54.419  1.00 45.18  ? 215 PHE   A CG  1 
ATOM   1321 C  CD1 . PHE   A 1 187 ? -3.589  10.743  55.763  1.00 45.71  ? 215 PHE   A CD1 1 
ATOM   1322 C  CD2 . PHE   A 1 187 ? -4.496  11.830  53.840  1.00 51.03  ? 215 PHE   A CD2 1 
ATOM   1323 C  CE1 . PHE   A 1 187 ? -3.762  11.911  56.512  1.00 42.40  ? 215 PHE   A CE1 1 
ATOM   1324 C  CE2 . PHE   A 1 187 ? -4.669  13.011  54.596  1.00 44.64  ? 215 PHE   A CE2 1 
ATOM   1325 C  CZ  . PHE   A 1 187 ? -4.301  13.038  55.929  1.00 40.78  ? 215 PHE   A CZ  1 
ATOM   1326 N  N   . PRO   A 1 188 ? -0.529  10.343  54.545  1.00 41.92  ? 216 PRO   A N   1 
ATOM   1327 C  CA  . PRO   A 1 188 ? 0.546   10.366  55.560  1.00 41.36  ? 216 PRO   A CA  1 
ATOM   1328 C  C   . PRO   A 1 188 ? 0.058   10.636  56.980  1.00 40.57  ? 216 PRO   A C   1 
ATOM   1329 O  O   . PRO   A 1 188 ? 0.463   11.610  57.626  1.00 40.01  ? 216 PRO   A O   1 
ATOM   1330 C  CB  . PRO   A 1 188 ? 1.466   11.480  55.041  1.00 35.27  ? 216 PRO   A CB  1 
ATOM   1331 C  CG  . PRO   A 1 188 ? 0.558   12.395  54.259  1.00 40.23  ? 216 PRO   A CG  1 
ATOM   1332 C  CD  . PRO   A 1 188 ? -0.431  11.459  53.591  1.00 42.69  ? 216 PRO   A CD  1 
ATOM   1333 N  N   . LEU   A 1 189 ? -0.783  9.740   57.498  1.00 31.19  ? 217 LEU   A N   1 
ATOM   1334 C  CA  . LEU   A 1 189 ? -1.155  9.798   58.909  1.00 34.28  ? 217 LEU   A CA  1 
ATOM   1335 C  C   . LEU   A 1 189 ? 0.085   9.708   59.792  1.00 36.09  ? 217 LEU   A C   1 
ATOM   1336 O  O   . LEU   A 1 189 ? 1.074   9.065   59.437  1.00 38.28  ? 217 LEU   A O   1 
ATOM   1337 C  CB  . LEU   A 1 189 ? -2.125  8.664   59.257  1.00 30.65  ? 217 LEU   A CB  1 
ATOM   1338 C  CG  . LEU   A 1 189 ? -3.536  8.752   58.666  1.00 38.88  ? 217 LEU   A CG  1 
ATOM   1339 C  CD1 . LEU   A 1 189 ? -4.325  7.445   58.876  1.00 31.38  ? 217 LEU   A CD1 1 
ATOM   1340 C  CD2 . LEU   A 1 189 ? -4.283  9.945   59.268  1.00 32.40  ? 217 LEU   A CD2 1 
ATOM   1341 N  N   . ASP   A 1 190 ? 0.028   10.367  60.954  1.00 36.42  ? 218 ASP   A N   1 
ATOM   1342 C  CA  . ASP   A 1 190 ? 1.098   10.301  61.951  1.00 37.68  ? 218 ASP   A CA  1 
ATOM   1343 C  C   . ASP   A 1 190 ? 0.652   10.947  63.254  1.00 36.16  ? 218 ASP   A C   1 
ATOM   1344 O  O   . ASP   A 1 190 ? 0.496   12.166  63.308  1.00 36.22  ? 218 ASP   A O   1 
ATOM   1345 C  CB  . ASP   A 1 190 ? 2.373   10.994  61.451  1.00 36.82  ? 218 ASP   A CB  1 
ATOM   1346 C  CG  . ASP   A 1 190 ? 3.512   10.957  62.482  1.00 40.51  ? 218 ASP   A CG  1 
ATOM   1347 O  OD1 . ASP   A 1 190 ? 3.360   10.293  63.536  1.00 37.95  ? 218 ASP   A OD1 1 
ATOM   1348 O  OD2 . ASP   A 1 190 ? 4.576   11.569  62.227  1.00 40.15  ? 218 ASP   A OD2 1 
ATOM   1349 N  N   . TYR   A 1 191 ? 0.470   10.166  64.319  1.00 30.87  ? 219 TYR   A N   1 
ATOM   1350 C  CA  . TYR   A 1 191 ? 0.107   10.744  65.607  1.00 31.71  ? 219 TYR   A CA  1 
ATOM   1351 C  C   . TYR   A 1 191 ? 1.275   10.751  66.593  1.00 35.64  ? 219 TYR   A C   1 
ATOM   1352 O  O   . TYR   A 1 191 ? 1.060   10.955  67.792  1.00 33.31  ? 219 TYR   A O   1 
ATOM   1353 C  CB  . TYR   A 1 191 ? -1.088  10.017  66.234  1.00 31.08  ? 219 TYR   A CB  1 
ATOM   1354 C  CG  . TYR   A 1 191 ? -2.271  9.741   65.324  1.00 32.38  ? 219 TYR   A CG  1 
ATOM   1355 C  CD1 . TYR   A 1 191 ? -2.571  10.558  64.225  1.00 29.82  ? 219 TYR   A CD1 1 
ATOM   1356 C  CD2 . TYR   A 1 191 ? -3.100  8.653   65.575  1.00 29.23  ? 219 TYR   A CD2 1 
ATOM   1357 C  CE1 . TYR   A 1 191 ? -3.672  10.283  63.398  1.00 30.19  ? 219 TYR   A CE1 1 
ATOM   1358 C  CE2 . TYR   A 1 191 ? -4.191  8.378   64.767  1.00 29.96  ? 219 TYR   A CE2 1 
ATOM   1359 C  CZ  . TYR   A 1 191 ? -4.471  9.176   63.676  1.00 28.34  ? 219 TYR   A CZ  1 
ATOM   1360 O  OH  . TYR   A 1 191 ? -5.549  8.837   62.887  1.00 25.52  ? 219 TYR   A OH  1 
ATOM   1361 N  N   . GLY   A 1 192 ? 2.500   10.540  66.129  1.00 29.29  ? 220 GLY   A N   1 
ATOM   1362 C  CA  . GLY   A 1 192 ? 3.656   10.616  67.004  1.00 35.25  ? 220 GLY   A CA  1 
ATOM   1363 C  C   . GLY   A 1 192 ? 4.273   9.286   67.406  1.00 33.13  ? 220 GLY   A C   1 
ATOM   1364 O  O   . GLY   A 1 192 ? 5.318   9.296   68.071  1.00 34.35  ? 220 GLY   A O   1 
ATOM   1365 N  N   . ILE   A 1 193 ? 3.680   8.147   67.038  1.00 32.21  ? 221 ILE   A N   1 
ATOM   1366 C  CA  . ILE   A 1 193 ? 4.245   6.852   67.420  1.00 30.61  ? 221 ILE   A CA  1 
ATOM   1367 C  C   . ILE   A 1 193 ? 5.468   6.549   66.567  1.00 28.36  ? 221 ILE   A C   1 
ATOM   1368 O  O   . ILE   A 1 193 ? 5.451   6.729   65.339  1.00 28.00  ? 221 ILE   A O   1 
ATOM   1369 C  CB  . ILE   A 1 193 ? 3.191   5.735   67.286  1.00 30.10  ? 221 ILE   A CB  1 
ATOM   1370 C  CG1 . ILE   A 1 193 ? 2.066   5.941   68.295  1.00 31.57  ? 221 ILE   A CG1 1 
ATOM   1371 C  CG2 . ILE   A 1 193 ? 3.841   4.371   67.512  1.00 29.97  ? 221 ILE   A CG2 1 
ATOM   1372 C  CD1 . ILE   A 1 193 ? 0.761   5.205   67.959  1.00 26.77  ? 221 ILE   A CD1 1 
ATOM   1373 N  N   . ARG   A 1 194 ? 6.535   6.049   67.204  1.00 30.26  ? 222 ARG   A N   1 
ATOM   1374 C  CA  . ARG   A 1 194 ? 7.820   5.951   66.522  1.00 29.13  ? 222 ARG   A CA  1 
ATOM   1375 C  C   . ARG   A 1 194 ? 8.424   4.554   66.488  1.00 31.65  ? 222 ARG   A C   1 
ATOM   1376 O  O   . ARG   A 1 194 ? 9.068   4.198   65.488  1.00 29.95  ? 222 ARG   A O   1 
ATOM   1377 C  CB  . ARG   A 1 194 ? 8.813   6.938   67.156  1.00 31.75  ? 222 ARG   A CB  1 
ATOM   1378 C  CG  . ARG   A 1 194 ? 8.476   8.394   66.788  1.00 29.09  ? 222 ARG   A CG  1 
ATOM   1379 C  CD  . ARG   A 1 194 ? 8.641   8.625   65.281  1.00 27.41  ? 222 ARG   A CD  1 
ATOM   1380 N  NE  . ARG   A 1 194 ? 8.181   9.933   64.806  1.00 29.82  ? 222 ARG   A NE  1 
ATOM   1381 C  CZ  . ARG   A 1 194 ? 6.938   10.188  64.386  1.00 37.97  ? 222 ARG   A CZ  1 
ATOM   1382 N  NH1 . ARG   A 1 194 ? 6.007   9.232   64.381  1.00 29.79  ? 222 ARG   A NH1 1 
ATOM   1383 N  NH2 . ARG   A 1 194 ? 6.619   11.395  63.952  1.00 29.02  ? 222 ARG   A NH2 1 
ATOM   1384 N  N   . ARG   A 1 195 ? 8.219   3.733   67.509  1.00 28.23  ? 223 ARG   A N   1 
ATOM   1385 C  CA  . ARG   A 1 195 ? 8.807   2.404   67.436  1.00 25.42  ? 223 ARG   A CA  1 
ATOM   1386 C  C   . ARG   A 1 195 ? 8.170   1.513   68.490  1.00 27.48  ? 223 ARG   A C   1 
ATOM   1387 O  O   . ARG   A 1 195 ? 7.458   1.983   69.383  1.00 25.18  ? 223 ARG   A O   1 
ATOM   1388 C  CB  . ARG   A 1 195 ? 10.322  2.477   67.643  1.00 31.75  ? 223 ARG   A CB  1 
ATOM   1389 C  CG  . ARG   A 1 195 ? 10.687  2.833   69.058  1.00 30.79  ? 223 ARG   A CG  1 
ATOM   1390 C  CD  . ARG   A 1 195 ? 12.209  2.789   69.242  1.00 40.77  ? 223 ARG   A CD  1 
ATOM   1391 N  NE  . ARG   A 1 195 ? 12.621  3.086   70.608  1.00 35.45  ? 223 ARG   A NE  1 
ATOM   1392 C  CZ  . ARG   A 1 195 ? 12.896  2.143   71.504  1.00 43.44  ? 223 ARG   A CZ  1 
ATOM   1393 N  NH1 . ARG   A 1 195 ? 12.760  0.867   71.164  1.00 40.08  ? 223 ARG   A NH1 1 
ATOM   1394 N  NH2 . ARG   A 1 195 ? 13.291  2.466   72.734  1.00 39.76  ? 223 ARG   A NH2 1 
ATOM   1395 N  N   . LEU   A 1 196 ? 8.488   0.222   68.407  1.00 25.16  ? 224 LEU   A N   1 
ATOM   1396 C  CA  . LEU   A 1 196 ? 8.018   -0.739  69.388  1.00 29.56  ? 224 LEU   A CA  1 
ATOM   1397 C  C   . LEU   A 1 196 ? 8.974   -0.750  70.572  1.00 32.16  ? 224 LEU   A C   1 
ATOM   1398 O  O   . LEU   A 1 196 ? 10.191  -0.903  70.408  1.00 29.24  ? 224 LEU   A O   1 
ATOM   1399 C  CB  . LEU   A 1 196 ? 7.906   -2.135  68.769  1.00 28.81  ? 224 LEU   A CB  1 
ATOM   1400 C  CG  . LEU   A 1 196 ? 7.371   -3.271  69.634  1.00 32.60  ? 224 LEU   A CG  1 
ATOM   1401 C  CD1 . LEU   A 1 196 ? 5.912   -3.002  70.012  1.00 28.36  ? 224 LEU   A CD1 1 
ATOM   1402 C  CD2 . LEU   A 1 196 ? 7.505   -4.627  68.883  1.00 25.60  ? 224 LEU   A CD2 1 
ATOM   1403 N  N   . ASP   A 1 197 ? 8.423   -0.592  71.767  1.00 34.81  ? 225 ASP   A N   1 
ATOM   1404 C  CA  . ASP   A 1 197 ? 9.278   -0.585  72.939  1.00 31.68  ? 225 ASP   A CA  1 
ATOM   1405 C  C   . ASP   A 1 197 ? 9.424   -1.980  73.533  1.00 35.96  ? 225 ASP   A C   1 
ATOM   1406 O  O   . ASP   A 1 197 ? 10.546  -2.432  73.805  1.00 33.00  ? 225 ASP   A O   1 
ATOM   1407 C  CB  . ASP   A 1 197 ? 8.723   0.373   73.980  1.00 29.40  ? 225 ASP   A CB  1 
ATOM   1408 C  CG  . ASP   A 1 197 ? 9.664   0.558   75.123  1.00 33.40  ? 225 ASP   A CG  1 
ATOM   1409 O  OD1 . ASP   A 1 197 ? 10.580  1.406   74.994  1.00 33.66  ? 225 ASP   A OD1 1 
ATOM   1410 O  OD2 . ASP   A 1 197 ? 9.481   -0.128  76.148  1.00 36.38  ? 225 ASP   A OD2 1 
ATOM   1411 N  N   . HIS   A 1 198 ? 8.302   -2.664  73.750  1.00 30.06  ? 226 HIS   A N   1 
ATOM   1412 C  CA  . HIS   A 1 198 ? 8.359   -4.052  74.193  1.00 31.03  ? 226 HIS   A CA  1 
ATOM   1413 C  C   . HIS   A 1 198 ? 7.112   -4.801  73.747  1.00 29.75  ? 226 HIS   A C   1 
ATOM   1414 O  O   . HIS   A 1 198 ? 6.052   -4.206  73.507  1.00 27.34  ? 226 HIS   A O   1 
ATOM   1415 C  CB  . HIS   A 1 198 ? 8.526   -4.152  75.707  1.00 30.47  ? 226 HIS   A CB  1 
ATOM   1416 C  CG  . HIS   A 1 198 ? 7.539   -3.355  76.503  1.00 31.31  ? 226 HIS   A CG  1 
ATOM   1417 N  ND1 . HIS   A 1 198 ? 7.766   -2.046  76.880  1.00 32.25  ? 226 HIS   A ND1 1 
ATOM   1418 C  CD2 . HIS   A 1 198 ? 6.350   -3.702  77.053  1.00 32.43  ? 226 HIS   A CD2 1 
ATOM   1419 C  CE1 . HIS   A 1 198 ? 6.764   -1.626  77.633  1.00 31.45  ? 226 HIS   A CE1 1 
ATOM   1420 N  NE2 . HIS   A 1 198 ? 5.885   -2.608  77.742  1.00 32.91  ? 226 HIS   A NE2 1 
ATOM   1421 N  N   . ALA   A 1 199 ? 7.249   -6.126  73.646  1.00 31.75  ? 227 ALA   A N   1 
ATOM   1422 C  CA  . ALA   A 1 199 ? 6.132   -7.011  73.325  1.00 29.63  ? 227 ALA   A CA  1 
ATOM   1423 C  C   . ALA   A 1 199 ? 6.018   -8.079  74.406  1.00 31.78  ? 227 ALA   A C   1 
ATOM   1424 O  O   . ALA   A 1 199 ? 6.972   -8.822  74.656  1.00 32.68  ? 227 ALA   A O   1 
ATOM   1425 C  CB  . ALA   A 1 199 ? 6.300   -7.635  71.939  1.00 27.95  ? 227 ALA   A CB  1 
ATOM   1426 N  N   . VAL   A 1 200 ? 4.844   -8.166  75.027  1.00 31.62  ? 228 VAL   A N   1 
ATOM   1427 C  CA  . VAL   A 1 200 ? 4.637   -8.898  76.270  1.00 30.36  ? 228 VAL   A CA  1 
ATOM   1428 C  C   . VAL   A 1 200 ? 3.820   -10.157 76.006  1.00 33.54  ? 228 VAL   A C   1 
ATOM   1429 O  O   . VAL   A 1 200 ? 2.744   -10.084 75.396  1.00 32.08  ? 228 VAL   A O   1 
ATOM   1430 C  CB  . VAL   A 1 200 ? 3.933   -8.005  77.299  1.00 34.57  ? 228 VAL   A CB  1 
ATOM   1431 C  CG1 . VAL   A 1 200 ? 3.550   -8.823  78.522  1.00 32.84  ? 228 VAL   A CG1 1 
ATOM   1432 C  CG2 . VAL   A 1 200 ? 4.840   -6.801  77.654  1.00 31.11  ? 228 VAL   A CG2 1 
ATOM   1433 N  N   . GLY   A 1 201 ? 4.312   -11.302 76.480  1.00 31.66  ? 229 GLY   A N   1 
ATOM   1434 C  CA  . GLY   A 1 201 ? 3.578   -12.561 76.392  1.00 30.66  ? 229 GLY   A CA  1 
ATOM   1435 C  C   . GLY   A 1 201 ? 2.900   -12.903 77.708  1.00 32.15  ? 229 GLY   A C   1 
ATOM   1436 O  O   . GLY   A 1 201 ? 3.441   -12.648 78.780  1.00 38.86  ? 229 GLY   A O   1 
ATOM   1437 N  N   . ASN   A 1 202 ? 1.696   -13.458 77.624  1.00 31.73  ? 230 ASN   A N   1 
ATOM   1438 C  CA  . ASN   A 1 202 ? 1.043   -14.063 78.781  1.00 34.43  ? 230 ASN   A CA  1 
ATOM   1439 C  C   . ASN   A 1 202 ? 1.206   -15.575 78.680  1.00 37.83  ? 230 ASN   A C   1 
ATOM   1440 O  O   . ASN   A 1 202 ? 0.862   -16.169 77.650  1.00 37.41  ? 230 ASN   A O   1 
ATOM   1441 C  CB  . ASN   A 1 202 ? -0.444  -13.718 78.844  1.00 32.11  ? 230 ASN   A CB  1 
ATOM   1442 C  CG  . ASN   A 1 202 ? -0.730  -12.384 79.513  1.00 41.10  ? 230 ASN   A CG  1 
ATOM   1443 O  OD1 . ASN   A 1 202 ? 0.181   -11.627 79.893  1.00 37.41  ? 230 ASN   A OD1 1 
ATOM   1444 N  ND2 . ASN   A 1 202 ? -2.025  -12.075 79.648  1.00 35.68  ? 230 ASN   A ND2 1 
ATOM   1445 N  N   . VAL   A 1 203 ? 1.740   -16.198 79.729  1.00 40.32  ? 231 VAL   A N   1 
ATOM   1446 C  CA  . VAL   A 1 203 ? 1.839   -17.659 79.764  1.00 39.03  ? 231 VAL   A CA  1 
ATOM   1447 C  C   . VAL   A 1 203 ? 1.206   -18.150 81.058  1.00 39.77  ? 231 VAL   A C   1 
ATOM   1448 O  O   . VAL   A 1 203 ? 0.997   -17.368 82.003  1.00 39.14  ? 231 VAL   A O   1 
ATOM   1449 C  CB  . VAL   A 1 203 ? 3.306   -18.141 79.634  1.00 37.10  ? 231 VAL   A CB  1 
ATOM   1450 C  CG1 . VAL   A 1 203 ? 3.956   -17.585 78.364  1.00 31.61  ? 231 VAL   A CG1 1 
ATOM   1451 C  CG2 . VAL   A 1 203 ? 4.126   -17.783 80.895  1.00 34.93  ? 231 VAL   A CG2 1 
ATOM   1452 N  N   . PRO   A 1 204 ? 0.861   -19.458 81.130  1.00 39.68  ? 232 PRO   A N   1 
ATOM   1453 C  CA  . PRO   A 1 204 ? 0.311   -20.005 82.379  1.00 37.81  ? 232 PRO   A CA  1 
ATOM   1454 C  C   . PRO   A 1 204 ? 1.380   -20.235 83.440  1.00 41.49  ? 232 PRO   A C   1 
ATOM   1455 O  O   . PRO   A 1 204 ? 1.064   -20.227 84.636  1.00 41.74  ? 232 PRO   A O   1 
ATOM   1456 C  CB  . PRO   A 1 204 ? -0.336  -21.324 81.931  1.00 42.86  ? 232 PRO   A CB  1 
ATOM   1457 C  CG  . PRO   A 1 204 ? 0.446   -21.727 80.736  1.00 45.54  ? 232 PRO   A CG  1 
ATOM   1458 C  CD  . PRO   A 1 204 ? 0.793   -20.439 80.031  1.00 35.30  ? 232 PRO   A CD  1 
ATOM   1459 N  N   . GLU   A 1 205 ? 2.639   -20.424 83.025  1.00 38.08  ? 233 GLU   A N   1 
ATOM   1460 C  CA  . GLU   A 1 205 ? 3.749   -20.660 83.951  1.00 42.08  ? 233 GLU   A CA  1 
ATOM   1461 C  C   . GLU   A 1 205 ? 4.962   -19.843 83.533  1.00 34.81  ? 233 GLU   A C   1 
ATOM   1462 O  O   . GLU   A 1 205 ? 5.588   -20.134 82.509  1.00 36.55  ? 233 GLU   A O   1 
ATOM   1463 C  CB  . GLU   A 1 205 ? 4.115   -22.142 83.997  1.00 43.64  ? 233 GLU   A CB  1 
ATOM   1464 C  CG  . GLU   A 1 205 ? 2.992   -23.047 84.424  1.00 45.03  ? 233 GLU   A CG  1 
ATOM   1465 C  CD  . GLU   A 1 205 ? 3.488   -24.438 84.723  1.00 56.04  ? 233 GLU   A CD  1 
ATOM   1466 O  OE1 . GLU   A 1 205 ? 3.113   -24.975 85.783  1.00 63.25  ? 233 GLU   A OE1 1 
ATOM   1467 O  OE2 . GLU   A 1 205 ? 4.260   -24.992 83.909  1.00 60.23  ? 233 GLU   A OE2 1 
ATOM   1468 N  N   . LEU   A 1 206 ? 5.327   -18.855 84.347  1.00 38.95  ? 234 LEU   A N   1 
ATOM   1469 C  CA  . LEU   A 1 206 ? 6.436   -17.966 83.995  1.00 40.88  ? 234 LEU   A CA  1 
ATOM   1470 C  C   . LEU   A 1 206 ? 7.760   -18.724 83.857  1.00 42.17  ? 234 LEU   A C   1 
ATOM   1471 O  O   . LEU   A 1 206 ? 8.447   -18.612 82.833  1.00 42.16  ? 234 LEU   A O   1 
ATOM   1472 C  CB  . LEU   A 1 206 ? 6.553   -16.860 85.043  1.00 44.02  ? 234 LEU   A CB  1 
ATOM   1473 C  CG  . LEU   A 1 206 ? 7.636   -15.793 84.882  1.00 47.51  ? 234 LEU   A CG  1 
ATOM   1474 C  CD1 . LEU   A 1 206 ? 7.407   -14.955 83.628  1.00 41.28  ? 234 LEU   A CD1 1 
ATOM   1475 C  CD2 . LEU   A 1 206 ? 7.662   -14.901 86.114  1.00 45.44  ? 234 LEU   A CD2 1 
ATOM   1476 N  N   . GLY   A 1 207 ? 8.141   -19.494 84.882  1.00 44.53  ? 235 GLY   A N   1 
ATOM   1477 C  CA  . GLY   A 1 207 ? 9.445   -20.129 84.948  1.00 37.31  ? 235 GLY   A CA  1 
ATOM   1478 C  C   . GLY   A 1 207 ? 9.874   -20.860 83.688  1.00 39.91  ? 235 GLY   A C   1 
ATOM   1479 O  O   . GLY   A 1 207 ? 10.915  -20.544 83.095  1.00 37.09  ? 235 GLY   A O   1 
ATOM   1480 N  N   . PRO   A 1 208 ? 9.080   -21.856 83.252  1.00 36.00  ? 236 PRO   A N   1 
ATOM   1481 C  CA  . PRO   A 1 208 ? 9.434   -22.592 82.023  1.00 31.46  ? 236 PRO   A CA  1 
ATOM   1482 C  C   . PRO   A 1 208 ? 9.473   -21.728 80.776  1.00 34.72  ? 236 PRO   A C   1 
ATOM   1483 O  O   . PRO   A 1 208 ? 10.305  -21.960 79.894  1.00 37.18  ? 236 PRO   A O   1 
ATOM   1484 C  CB  . PRO   A 1 208 ? 8.330   -23.653 81.924  1.00 33.34  ? 236 PRO   A CB  1 
ATOM   1485 C  CG  . PRO   A 1 208 ? 7.770   -23.769 83.290  1.00 37.38  ? 236 PRO   A CG  1 
ATOM   1486 C  CD  . PRO   A 1 208 ? 7.887   -22.423 83.909  1.00 36.90  ? 236 PRO   A CD  1 
ATOM   1487 N  N   . ALA   A 1 209 ? 8.570   -20.753 80.652  1.00 41.05  ? 237 ALA   A N   1 
ATOM   1488 C  CA  . ALA   A 1 209 ? 8.634   -19.851 79.508  1.00 36.55  ? 237 ALA   A CA  1 
ATOM   1489 C  C   . ALA   A 1 209 ? 9.932   -19.053 79.521  1.00 36.40  ? 237 ALA   A C   1 
ATOM   1490 O  O   . ALA   A 1 209 ? 10.656  -19.000 78.517  1.00 38.17  ? 237 ALA   A O   1 
ATOM   1491 C  CB  . ALA   A 1 209 ? 7.423   -18.918 79.502  1.00 38.48  ? 237 ALA   A CB  1 
ATOM   1492 N  N   . LEU   A 1 210 ? 10.244  -18.418 80.652  1.00 37.80  ? 238 LEU   A N   1 
ATOM   1493 C  CA  . LEU   A 1 210 ? 11.515  -17.710 80.774  1.00 39.17  ? 238 LEU   A CA  1 
ATOM   1494 C  C   . LEU   A 1 210 ? 12.676  -18.626 80.419  1.00 40.06  ? 238 LEU   A C   1 
ATOM   1495 O  O   . LEU   A 1 210 ? 13.466  -18.335 79.515  1.00 43.03  ? 238 LEU   A O   1 
ATOM   1496 C  CB  . LEU   A 1 210 ? 11.701  -17.181 82.196  1.00 35.97  ? 238 LEU   A CB  1 
ATOM   1497 C  CG  . LEU   A 1 210 ? 11.222  -15.783 82.559  1.00 43.16  ? 238 LEU   A CG  1 
ATOM   1498 C  CD1 . LEU   A 1 210 ? 11.968  -15.344 83.816  1.00 48.84  ? 238 LEU   A CD1 1 
ATOM   1499 C  CD2 . LEU   A 1 210 ? 11.481  -14.822 81.421  1.00 37.03  ? 238 LEU   A CD2 1 
ATOM   1500 N  N   . THR   A 1 211 ? 12.787  -19.747 81.133  1.00 39.66  ? 239 THR   A N   1 
ATOM   1501 C  CA  . THR   A 1 211 ? 13.920  -20.648 80.934  1.00 41.69  ? 239 THR   A CA  1 
ATOM   1502 C  C   . THR   A 1 211 ? 14.045  -21.049 79.472  1.00 41.10  ? 239 THR   A C   1 
ATOM   1503 O  O   . THR   A 1 211 ? 15.133  -20.988 78.889  1.00 39.42  ? 239 THR   A O   1 
ATOM   1504 C  CB  . THR   A 1 211 ? 13.758  -21.878 81.828  1.00 45.66  ? 239 THR   A CB  1 
ATOM   1505 O  OG1 . THR   A 1 211 ? 13.800  -21.468 83.205  1.00 49.05  ? 239 THR   A OG1 1 
ATOM   1506 C  CG2 . THR   A 1 211 ? 14.862  -22.897 81.559  1.00 41.15  ? 239 THR   A CG2 1 
ATOM   1507 N  N   . TYR   A 1 212 ? 12.919  -21.417 78.851  1.00 40.29  ? 240 TYR   A N   1 
ATOM   1508 C  CA  . TYR   A 1 212 ? 12.919  -21.746 77.431  1.00 36.03  ? 240 TYR   A CA  1 
ATOM   1509 C  C   . TYR   A 1 212 ? 13.471  -20.597 76.592  1.00 39.96  ? 240 TYR   A C   1 
ATOM   1510 O  O   . TYR   A 1 212 ? 14.434  -20.770 75.836  1.00 41.73  ? 240 TYR   A O   1 
ATOM   1511 C  CB  . TYR   A 1 212 ? 11.504  -22.113 76.984  1.00 32.78  ? 240 TYR   A CB  1 
ATOM   1512 C  CG  . TYR   A 1 212 ? 11.364  -22.189 75.478  1.00 41.92  ? 240 TYR   A CG  1 
ATOM   1513 C  CD1 . TYR   A 1 212 ? 12.026  -23.175 74.750  1.00 38.81  ? 240 TYR   A CD1 1 
ATOM   1514 C  CD2 . TYR   A 1 212 ? 10.553  -21.285 74.778  1.00 38.86  ? 240 TYR   A CD2 1 
ATOM   1515 C  CE1 . TYR   A 1 212 ? 11.900  -23.257 73.358  1.00 41.20  ? 240 TYR   A CE1 1 
ATOM   1516 C  CE2 . TYR   A 1 212 ? 10.416  -21.364 73.385  1.00 37.36  ? 240 TYR   A CE2 1 
ATOM   1517 C  CZ  . TYR   A 1 212 ? 11.093  -22.352 72.682  1.00 38.76  ? 240 TYR   A CZ  1 
ATOM   1518 O  OH  . TYR   A 1 212 ? 10.983  -22.435 71.305  1.00 31.93  ? 240 TYR   A OH  1 
ATOM   1519 N  N   . VAL   A 1 213 ? 12.880  -19.405 76.719  1.00 34.23  ? 241 VAL   A N   1 
ATOM   1520 C  CA  . VAL   A 1 213 ? 13.246  -18.312 75.827  1.00 32.34  ? 241 VAL   A CA  1 
ATOM   1521 C  C   . VAL   A 1 213 ? 14.643  -17.785 76.158  1.00 33.98  ? 241 VAL   A C   1 
ATOM   1522 O  O   . VAL   A 1 213 ? 15.478  -17.586 75.265  1.00 34.20  ? 241 VAL   A O   1 
ATOM   1523 C  CB  . VAL   A 1 213 ? 12.188  -17.193 75.882  1.00 35.16  ? 241 VAL   A CB  1 
ATOM   1524 C  CG1 . VAL   A 1 213 ? 12.619  -16.035 75.005  1.00 29.38  ? 241 VAL   A CG1 1 
ATOM   1525 C  CG2 . VAL   A 1 213 ? 10.818  -17.732 75.443  1.00 31.30  ? 241 VAL   A CG2 1 
ATOM   1526 N  N   . ALA   A 1 214 ? 14.919  -17.523 77.436  1.00 33.77  ? 242 ALA   A N   1 
ATOM   1527 C  CA  . ALA   A 1 214 ? 16.289  -17.147 77.791  1.00 39.10  ? 242 ALA   A CA  1 
ATOM   1528 C  C   . ALA   A 1 214 ? 17.266  -18.234 77.371  1.00 38.02  ? 242 ALA   A C   1 
ATOM   1529 O  O   . ALA   A 1 214 ? 18.389  -17.931 76.945  1.00 37.49  ? 242 ALA   A O   1 
ATOM   1530 C  CB  . ALA   A 1 214 ? 16.413  -16.869 79.287  1.00 34.04  ? 242 ALA   A CB  1 
ATOM   1531 N  N   . GLY   A 1 215 ? 16.822  -19.497 77.413  1.00 38.83  ? 243 GLY   A N   1 
ATOM   1532 C  CA  . GLY   A 1 215 ? 17.696  -20.600 77.046  1.00 40.20  ? 243 GLY   A CA  1 
ATOM   1533 C  C   . GLY   A 1 215 ? 18.245  -20.486 75.635  1.00 42.26  ? 243 GLY   A C   1 
ATOM   1534 O  O   . GLY   A 1 215 ? 19.443  -20.685 75.412  1.00 35.74  ? 243 GLY   A O   1 
ATOM   1535 N  N   . PHE   A 1 216 ? 17.378  -20.165 74.653  1.00 32.58  ? 244 PHE   A N   1 
ATOM   1536 C  CA  . PHE   A 1 216 ? 17.824  -20.235 73.265  1.00 28.36  ? 244 PHE   A CA  1 
ATOM   1537 C  C   . PHE   A 1 216 ? 18.226  -18.890 72.676  1.00 37.60  ? 244 PHE   A C   1 
ATOM   1538 O  O   . PHE   A 1 216 ? 18.825  -18.865 71.592  1.00 38.04  ? 244 PHE   A O   1 
ATOM   1539 C  CB  . PHE   A 1 216 ? 16.768  -20.926 72.367  1.00 37.25  ? 244 PHE   A CB  1 
ATOM   1540 C  CG  . PHE   A 1 216 ? 15.584  -20.057 71.967  1.00 37.53  ? 244 PHE   A CG  1 
ATOM   1541 C  CD1 . PHE   A 1 216 ? 14.342  -20.239 72.572  1.00 38.24  ? 244 PHE   A CD1 1 
ATOM   1542 C  CD2 . PHE   A 1 216 ? 15.699  -19.092 70.962  1.00 36.92  ? 244 PHE   A CD2 1 
ATOM   1543 C  CE1 . PHE   A 1 216 ? 13.234  -19.462 72.203  1.00 35.14  ? 244 PHE   A CE1 1 
ATOM   1544 C  CE2 . PHE   A 1 216 ? 14.583  -18.302 70.583  1.00 37.22  ? 244 PHE   A CE2 1 
ATOM   1545 C  CZ  . PHE   A 1 216 ? 13.360  -18.489 71.206  1.00 27.35  ? 244 PHE   A CZ  1 
ATOM   1546 N  N   . THR   A 1 217 ? 17.918  -17.775 73.337  1.00 36.61  ? 245 THR   A N   1 
ATOM   1547 C  CA  . THR   A 1 217 ? 18.366  -16.482 72.830  1.00 36.22  ? 245 THR   A CA  1 
ATOM   1548 C  C   . THR   A 1 217 ? 19.647  -16.006 73.499  1.00 37.66  ? 245 THR   A C   1 
ATOM   1549 O  O   . THR   A 1 217 ? 20.498  -15.403 72.838  1.00 31.18  ? 245 THR   A O   1 
ATOM   1550 C  CB  . THR   A 1 217 ? 17.289  -15.399 73.017  1.00 34.08  ? 245 THR   A CB  1 
ATOM   1551 O  OG1 . THR   A 1 217 ? 17.143  -15.092 74.411  1.00 37.64  ? 245 THR   A OG1 1 
ATOM   1552 C  CG2 . THR   A 1 217 ? 15.929  -15.839 72.447  1.00 32.45  ? 245 THR   A CG2 1 
ATOM   1553 N  N   . GLY   A 1 218 ? 19.804  -16.270 74.792  1.00 39.64  ? 246 GLY   A N   1 
ATOM   1554 C  CA  . GLY   A 1 218 ? 20.840  -15.622 75.566  1.00 42.48  ? 246 GLY   A CA  1 
ATOM   1555 C  C   . GLY   A 1 218 ? 20.404  -14.313 76.176  1.00 44.79  ? 246 GLY   A C   1 
ATOM   1556 O  O   . GLY   A 1 218 ? 21.236  -13.626 76.777  1.00 43.62  ? 246 GLY   A O   1 
ATOM   1557 N  N   . PHE   A 1 219 ? 19.131  -13.939 76.021  1.00 37.66  ? 247 PHE   A N   1 
ATOM   1558 C  CA  . PHE   A 1 219 ? 18.617  -12.727 76.646  1.00 41.96  ? 247 PHE   A CA  1 
ATOM   1559 C  C   . PHE   A 1 219 ? 18.671  -12.857 78.163  1.00 43.83  ? 247 PHE   A C   1 
ATOM   1560 O  O   . PHE   A 1 219 ? 18.469  -13.942 78.719  1.00 36.71  ? 247 PHE   A O   1 
ATOM   1561 C  CB  . PHE   A 1 219 ? 17.172  -12.451 76.204  1.00 39.21  ? 247 PHE   A CB  1 
ATOM   1562 C  CG  . PHE   A 1 219 ? 17.026  -12.082 74.752  1.00 39.31  ? 247 PHE   A CG  1 
ATOM   1563 C  CD1 . PHE   A 1 219 ? 18.133  -11.722 73.986  1.00 39.78  ? 247 PHE   A CD1 1 
ATOM   1564 C  CD2 . PHE   A 1 219 ? 15.769  -12.076 74.156  1.00 43.33  ? 247 PHE   A CD2 1 
ATOM   1565 C  CE1 . PHE   A 1 219 ? 17.997  -11.377 72.652  1.00 37.91  ? 247 PHE   A CE1 1 
ATOM   1566 C  CE2 . PHE   A 1 219 ? 15.613  -11.724 72.823  1.00 38.14  ? 247 PHE   A CE2 1 
ATOM   1567 C  CZ  . PHE   A 1 219 ? 16.724  -11.367 72.070  1.00 42.90  ? 247 PHE   A CZ  1 
ATOM   1568 N  N   . HIS   A 1 220 ? 18.921  -11.734 78.831  1.00 42.45  ? 248 HIS   A N   1 
ATOM   1569 C  CA  . HIS   A 1 220 ? 19.068  -11.683 80.275  1.00 41.12  ? 248 HIS   A CA  1 
ATOM   1570 C  C   . HIS   A 1 220 ? 17.896  -10.959 80.922  1.00 41.42  ? 248 HIS   A C   1 
ATOM   1571 O  O   . HIS   A 1 220 ? 17.230  -10.129 80.306  1.00 46.10  ? 248 HIS   A O   1 
ATOM   1572 C  CB  . HIS   A 1 220 ? 20.363  -10.968 80.650  1.00 43.41  ? 248 HIS   A CB  1 
ATOM   1573 C  CG  . HIS   A 1 220 ? 20.400  -9.542  80.207  1.00 41.20  ? 248 HIS   A CG  1 
ATOM   1574 N  ND1 . HIS   A 1 220 ? 20.781  -9.171  78.934  1.00 41.02  ? 248 HIS   A ND1 1 
ATOM   1575 C  CD2 . HIS   A 1 220 ? 20.087  -8.398  80.858  1.00 39.69  ? 248 HIS   A CD2 1 
ATOM   1576 C  CE1 . HIS   A 1 220 ? 20.716  -7.857  78.824  1.00 40.16  ? 248 HIS   A CE1 1 
ATOM   1577 N  NE2 . HIS   A 1 220 ? 20.307  -7.362  79.980  1.00 44.06  ? 248 HIS   A NE2 1 
ATOM   1578 N  N   . GLN   A 1 221 ? 17.686  -11.256 82.199  1.00 40.95  ? 249 GLN   A N   1 
ATOM   1579 C  CA  . GLN   A 1 221 ? 16.647  -10.598 82.974  1.00 41.00  ? 249 GLN   A CA  1 
ATOM   1580 C  C   . GLN   A 1 221 ? 16.974  -9.120  83.195  1.00 47.74  ? 249 GLN   A C   1 
ATOM   1581 O  O   . GLN   A 1 221 ? 18.093  -8.757  83.581  1.00 44.81  ? 249 GLN   A O   1 
ATOM   1582 C  CB  . GLN   A 1 221 ? 16.471  -11.325 84.309  1.00 47.74  ? 249 GLN   A CB  1 
ATOM   1583 C  CG  . GLN   A 1 221 ? 15.383  -10.756 85.207  1.00 49.11  ? 249 GLN   A CG  1 
ATOM   1584 C  CD  . GLN   A 1 221 ? 14.611  -11.844 85.925  1.00 54.72  ? 249 GLN   A CD  1 
ATOM   1585 O  OE1 . GLN   A 1 221 ? 14.977  -13.023 85.862  1.00 53.44  ? 249 GLN   A OE1 1 
ATOM   1586 N  NE2 . GLN   A 1 221 ? 13.526  -11.460 86.601  1.00 48.40  ? 249 GLN   A NE2 1 
ATOM   1587 N  N   . PHE   A 1 222 ? 15.986  -8.271  82.935  1.00 47.11  ? 250 PHE   A N   1 
ATOM   1588 C  CA  . PHE   A 1 222 ? 16.070  -6.831  83.115  1.00 44.55  ? 250 PHE   A CA  1 
ATOM   1589 C  C   . PHE   A 1 222 ? 15.339  -6.504  84.412  1.00 49.72  ? 250 PHE   A C   1 
ATOM   1590 O  O   . PHE   A 1 222 ? 15.866  -5.798  85.271  1.00 58.45  ? 250 PHE   A O   1 
ATOM   1591 C  CB  . PHE   A 1 222 ? 15.444  -6.121  81.897  1.00 44.63  ? 250 PHE   A CB  1 
ATOM   1592 C  CG  . PHE   A 1 222 ? 15.457  -4.601  81.950  1.00 52.72  ? 250 PHE   A CG  1 
ATOM   1593 C  CD1 . PHE   A 1 222 ? 14.638  -3.894  82.828  1.00 49.40  ? 250 PHE   A CD1 1 
ATOM   1594 C  CD2 . PHE   A 1 222 ? 16.248  -3.881  81.067  1.00 49.08  ? 250 PHE   A CD2 1 
ATOM   1595 C  CE1 . PHE   A 1 222 ? 14.638  -2.515  82.850  1.00 47.11  ? 250 PHE   A CE1 1 
ATOM   1596 C  CE2 . PHE   A 1 222 ? 16.246  -2.493  81.081  1.00 50.70  ? 250 PHE   A CE2 1 
ATOM   1597 C  CZ  . PHE   A 1 222 ? 15.444  -1.810  81.976  1.00 47.55  ? 250 PHE   A CZ  1 
ATOM   1598 N  N   . SER   A 1 235 ? -2.055  -7.644  92.936  1.00 59.04  ? 263 SER   A N   1 
ATOM   1599 C  CA  . SER   A 1 235 ? -1.515  -7.203  91.647  1.00 59.49  ? 263 SER   A CA  1 
ATOM   1600 C  C   . SER   A 1 235 ? -2.049  -8.061  90.505  1.00 64.62  ? 263 SER   A C   1 
ATOM   1601 O  O   . SER   A 1 235 ? -2.403  -7.542  89.443  1.00 62.30  ? 263 SER   A O   1 
ATOM   1602 C  CB  . SER   A 1 235 ? 0.012   -7.250  91.648  1.00 61.94  ? 263 SER   A CB  1 
ATOM   1603 O  OG  . SER   A 1 235 ? 0.472   -8.577  91.450  1.00 64.26  ? 263 SER   A OG  1 
ATOM   1604 N  N   . GLY   A 1 236 ? -2.087  -9.381  90.727  1.00 55.61  ? 264 GLY   A N   1 
ATOM   1605 C  CA  . GLY   A 1 236 ? -2.709  -10.326 89.823  1.00 54.01  ? 264 GLY   A CA  1 
ATOM   1606 C  C   . GLY   A 1 236 ? -1.723  -11.168 89.038  1.00 52.61  ? 264 GLY   A C   1 
ATOM   1607 O  O   . GLY   A 1 236 ? -2.070  -12.280 88.614  1.00 53.21  ? 264 GLY   A O   1 
ATOM   1608 N  N   . LEU   A 1 237 ? -0.504  -10.672 88.850  1.00 52.36  ? 265 LEU   A N   1 
ATOM   1609 C  CA  . LEU   A 1 237 ? 0.487   -11.336 88.019  1.00 53.30  ? 265 LEU   A CA  1 
ATOM   1610 C  C   . LEU   A 1 237 ? 1.844   -11.375 88.712  1.00 49.77  ? 265 LEU   A C   1 
ATOM   1611 O  O   . LEU   A 1 237 ? 2.099   -10.663 89.685  1.00 47.13  ? 265 LEU   A O   1 
ATOM   1612 C  CB  . LEU   A 1 237 ? 0.635   -10.637 86.653  1.00 51.95  ? 265 LEU   A CB  1 
ATOM   1613 C  CG  . LEU   A 1 237 ? 0.970   -9.134  86.611  1.00 52.46  ? 265 LEU   A CG  1 
ATOM   1614 C  CD1 . LEU   A 1 237 ? 2.446   -8.862  86.793  1.00 52.94  ? 265 LEU   A CD1 1 
ATOM   1615 C  CD2 . LEU   A 1 237 ? 0.487   -8.516  85.307  1.00 51.48  ? 265 LEU   A CD2 1 
ATOM   1616 N  N   . ASN   A 1 238 ? 2.692   -12.262 88.206  1.00 43.37  ? 266 ASN   A N   1 
ATOM   1617 C  CA  . ASN   A 1 238 ? 4.135   -12.164 88.315  1.00 44.20  ? 266 ASN   A CA  1 
ATOM   1618 C  C   . ASN   A 1 238 ? 4.663   -12.053 86.899  1.00 45.59  ? 266 ASN   A C   1 
ATOM   1619 O  O   . ASN   A 1 238 ? 4.084   -12.621 85.964  1.00 43.35  ? 266 ASN   A O   1 
ATOM   1620 C  CB  . ASN   A 1 238 ? 4.778   -13.390 88.993  1.00 48.09  ? 266 ASN   A CB  1 
ATOM   1621 C  CG  . ASN   A 1 238 ? 4.249   -13.637 90.388  1.00 52.21  ? 266 ASN   A CG  1 
ATOM   1622 O  OD1 . ASN   A 1 238 ? 4.232   -12.732 91.233  1.00 54.70  ? 266 ASN   A OD1 1 
ATOM   1623 N  ND2 . ASN   A 1 238 ? 3.806   -14.868 90.640  1.00 46.17  ? 266 ASN   A ND2 1 
ATOM   1624 N  N   . SER   A 1 239 ? 5.755   -11.316 86.741  1.00 43.75  ? 267 SER   A N   1 
ATOM   1625 C  CA  . SER   A 1 239 ? 6.323   -11.114 85.420  1.00 44.73  ? 267 SER   A CA  1 
ATOM   1626 C  C   . SER   A 1 239 ? 7.833   -10.988 85.536  1.00 43.17  ? 267 SER   A C   1 
ATOM   1627 O  O   . SER   A 1 239 ? 8.384   -10.854 86.629  1.00 45.93  ? 267 SER   A O   1 
ATOM   1628 C  CB  . SER   A 1 239 ? 5.729   -9.878  84.743  1.00 43.22  ? 267 SER   A CB  1 
ATOM   1629 O  OG  . SER   A 1 239 ? 6.460   -8.725  85.122  1.00 57.58  ? 267 SER   A OG  1 
ATOM   1630 N  N   . ALA   A 1 240 ? 8.493   -11.043 84.383  1.00 40.57  ? 268 ALA   A N   1 
ATOM   1631 C  CA  . ALA   A 1 240 ? 9.931   -10.853 84.270  1.00 39.61  ? 268 ALA   A CA  1 
ATOM   1632 C  C   . ALA   A 1 240 ? 10.238  -10.482 82.824  1.00 43.04  ? 268 ALA   A C   1 
ATOM   1633 O  O   . ALA   A 1 240 ? 9.506   -10.862 81.904  1.00 38.47  ? 268 ALA   A O   1 
ATOM   1634 C  CB  . ALA   A 1 240 ? 10.708  -12.105 84.692  1.00 41.73  ? 268 ALA   A CB  1 
ATOM   1635 N  N   . VAL   A 1 241 ? 11.322  -9.738  82.632  1.00 39.34  ? 269 VAL   A N   1 
ATOM   1636 C  CA  . VAL   A 1 241 ? 11.610  -9.096  81.358  1.00 38.65  ? 269 VAL   A CA  1 
ATOM   1637 C  C   . VAL   A 1 241 ? 12.945  -9.582  80.825  1.00 43.39  ? 269 VAL   A C   1 
ATOM   1638 O  O   . VAL   A 1 241 ? 13.990  -9.342  81.449  1.00 46.41  ? 269 VAL   A O   1 
ATOM   1639 C  CB  . VAL   A 1 241 ? 11.634  -7.571  81.490  1.00 35.16  ? 269 VAL   A CB  1 
ATOM   1640 C  CG1 . VAL   A 1 241 ? 11.981  -6.973  80.148  1.00 34.27  ? 269 VAL   A CG1 1 
ATOM   1641 C  CG2 . VAL   A 1 241 ? 10.309  -7.076  82.010  1.00 38.30  ? 269 VAL   A CG2 1 
ATOM   1642 N  N   . LEU   A 1 242 ? 12.918  -10.199 79.644  1.00 35.28  ? 270 LEU   A N   1 
ATOM   1643 C  CA  . LEU   A 1 242 ? 14.126  -10.607 78.941  1.00 39.95  ? 270 LEU   A CA  1 
ATOM   1644 C  C   . LEU   A 1 242 ? 14.560  -9.524  77.961  1.00 39.42  ? 270 LEU   A C   1 
ATOM   1645 O  O   . LEU   A 1 242 ? 13.728  -8.841  77.366  1.00 42.29  ? 270 LEU   A O   1 
ATOM   1646 C  CB  . LEU   A 1 242 ? 13.898  -11.924 78.204  1.00 38.32  ? 270 LEU   A CB  1 
ATOM   1647 C  CG  . LEU   A 1 242 ? 13.778  -13.158 79.103  1.00 42.09  ? 270 LEU   A CG  1 
ATOM   1648 C  CD1 . LEU   A 1 242 ? 13.251  -14.352 78.329  1.00 37.27  ? 270 LEU   A CD1 1 
ATOM   1649 C  CD2 . LEU   A 1 242 ? 15.147  -13.493 79.740  1.00 40.85  ? 270 LEU   A CD2 1 
ATOM   1650 N  N   . ALA   A 1 243 ? 15.876  -9.376  77.791  1.00 41.68  ? 271 ALA   A N   1 
ATOM   1651 C  CA  . ALA   A 1 243 ? 16.428  -8.273  77.011  1.00 37.13  ? 271 ALA   A CA  1 
ATOM   1652 C  C   . ALA   A 1 243 ? 17.720  -8.683  76.315  1.00 43.76  ? 271 ALA   A C   1 
ATOM   1653 O  O   . ALA   A 1 243 ? 18.543  -9.407  76.882  1.00 46.34  ? 271 ALA   A O   1 
ATOM   1654 C  CB  . ALA   A 1 243 ? 16.698  -7.056  77.901  1.00 40.87  ? 271 ALA   A CB  1 
ATOM   1655 N  N   . SER   A 1 244 ? 17.912  -8.177  75.101  1.00 38.39  ? 272 SER   A N   1 
ATOM   1656 C  CA  . SER   A 1 244 ? 19.133  -8.424  74.352  1.00 35.15  ? 272 SER   A CA  1 
ATOM   1657 C  C   . SER   A 1 244 ? 20.297  -7.593  74.915  1.00 43.66  ? 272 SER   A C   1 
ATOM   1658 O  O   . SER   A 1 244 ? 20.168  -6.865  75.909  1.00 40.07  ? 272 SER   A O   1 
ATOM   1659 C  CB  . SER   A 1 244 ? 18.901  -8.097  72.886  1.00 35.39  ? 272 SER   A CB  1 
ATOM   1660 O  OG  . SER   A 1 244 ? 18.463  -6.749  72.769  1.00 39.84  ? 272 SER   A OG  1 
ATOM   1661 N  N   . ASN   A 1 245 ? 21.439  -7.676  74.222  1.00 40.30  ? 273 ASN   A N   1 
ATOM   1662 C  CA  . ASN   A 1 245 ? 22.682  -7.077  74.710  1.00 43.99  ? 273 ASN   A CA  1 
ATOM   1663 C  C   . ASN   A 1 245 ? 22.532  -5.579  74.989  1.00 44.07  ? 273 ASN   A C   1 
ATOM   1664 O  O   . ASN   A 1 245 ? 22.855  -5.110  76.088  1.00 42.47  ? 273 ASN   A O   1 
ATOM   1665 C  CB  . ASN   A 1 245 ? 23.800  -7.340  73.705  1.00 35.09  ? 273 ASN   A CB  1 
ATOM   1666 C  CG  . ASN   A 1 245 ? 24.452  -8.698  73.911  1.00 43.79  ? 273 ASN   A CG  1 
ATOM   1667 O  OD1 . ASN   A 1 245 ? 23.988  -9.506  74.714  1.00 41.53  ? 273 ASN   A OD1 1 
ATOM   1668 N  ND2 . ASN   A 1 245 ? 25.536  -8.952  73.187  1.00 42.49  ? 273 ASN   A ND2 1 
ATOM   1669 N  N   . ASP   A 1 246 ? 22.042  -4.807  74.021  1.00 40.21  ? 274 ASP   A N   1 
ATOM   1670 C  CA  . ASP   A 1 246 ? 21.863  -3.376  74.256  1.00 40.47  ? 274 ASP   A CA  1 
ATOM   1671 C  C   . ASP   A 1 246 ? 20.503  -3.051  74.878  1.00 46.55  ? 274 ASP   A C   1 
ATOM   1672 O  O   . ASP   A 1 246 ? 20.139  -1.870  74.985  1.00 46.85  ? 274 ASP   A O   1 
ATOM   1673 C  CB  . ASP   A 1 246 ? 22.086  -2.574  72.956  1.00 38.57  ? 274 ASP   A CB  1 
ATOM   1674 C  CG  . ASP   A 1 246 ? 21.071  -2.894  71.850  1.00 45.49  ? 274 ASP   A CG  1 
ATOM   1675 O  OD1 . ASP   A 1 246 ? 20.017  -3.509  72.121  1.00 44.16  ? 274 ASP   A OD1 1 
ATOM   1676 O  OD2 . ASP   A 1 246 ? 21.320  -2.495  70.691  1.00 44.85  ? 274 ASP   A OD2 1 
ATOM   1677 N  N   . GLU   A 1 247 ? 19.746  -4.079  75.270  1.00 45.07  ? 275 GLU   A N   1 
ATOM   1678 C  CA  . GLU   A 1 247 ? 18.476  -3.939  75.982  1.00 42.39  ? 275 GLU   A CA  1 
ATOM   1679 C  C   . GLU   A 1 247 ? 17.430  -3.162  75.179  1.00 43.89  ? 275 GLU   A C   1 
ATOM   1680 O  O   . GLU   A 1 247 ? 16.527  -2.539  75.744  1.00 39.18  ? 275 GLU   A O   1 
ATOM   1681 C  CB  . GLU   A 1 247 ? 18.705  -3.316  77.359  1.00 45.20  ? 275 GLU   A CB  1 
ATOM   1682 C  CG  . GLU   A 1 247 ? 19.874  -4.006  78.107  1.00 46.32  ? 275 GLU   A CG  1 
ATOM   1683 C  CD  . GLU   A 1 247 ? 19.738  -3.922  79.620  1.00 48.09  ? 275 GLU   A CD  1 
ATOM   1684 O  OE1 . GLU   A 1 247 ? 19.904  -4.961  80.291  1.00 46.95  ? 275 GLU   A OE1 1 
ATOM   1685 O  OE2 . GLU   A 1 247 ? 19.441  -2.820  80.136  1.00 52.72  ? 275 GLU   A OE2 1 
ATOM   1686 N  N   . MET   A 1 248 ? 17.518  -3.221  73.851  1.00 40.05  ? 276 MET   A N   1 
ATOM   1687 C  CA  . MET   A 1 248 ? 16.556  -2.583  72.967  1.00 38.10  ? 276 MET   A CA  1 
ATOM   1688 C  C   . MET   A 1 248 ? 15.526  -3.554  72.411  1.00 40.38  ? 276 MET   A C   1 
ATOM   1689 O  O   . MET   A 1 248 ? 14.582  -3.126  71.736  1.00 39.77  ? 276 MET   A O   1 
ATOM   1690 C  CB  . MET   A 1 248 ? 17.312  -1.918  71.822  1.00 45.28  ? 276 MET   A CB  1 
ATOM   1691 C  CG  . MET   A 1 248 ? 18.159  -0.736  72.300  1.00 44.71  ? 276 MET   A CG  1 
ATOM   1692 S  SD  . MET   A 1 248 ? 17.129  0.690   72.582  1.00 52.78  ? 276 MET   A SD  1 
ATOM   1693 C  CE  . MET   A 1 248 ? 16.910  0.710   74.348  1.00 56.21  ? 276 MET   A CE  1 
ATOM   1694 N  N   . VAL   A 1 249 ? 15.723  -4.842  72.622  1.00 33.34  ? 277 VAL   A N   1 
ATOM   1695 C  CA  . VAL   A 1 249 ? 14.716  -5.848  72.352  1.00 36.28  ? 277 VAL   A CA  1 
ATOM   1696 C  C   . VAL   A 1 249 ? 14.258  -6.327  73.718  1.00 39.24  ? 277 VAL   A C   1 
ATOM   1697 O  O   . VAL   A 1 249 ? 15.019  -6.989  74.440  1.00 31.92  ? 277 VAL   A O   1 
ATOM   1698 C  CB  . VAL   A 1 249 ? 15.271  -6.979  71.482  1.00 34.97  ? 277 VAL   A CB  1 
ATOM   1699 C  CG1 . VAL   A 1 249 ? 14.250  -8.096  71.325  1.00 34.64  ? 277 VAL   A CG1 1 
ATOM   1700 C  CG2 . VAL   A 1 249 ? 15.669  -6.398  70.127  1.00 36.75  ? 277 VAL   A CG2 1 
ATOM   1701 N  N   . LEU   A 1 250 ? 13.048  -5.922  74.111  1.00 29.96  ? 278 LEU   A N   1 
ATOM   1702 C  CA  . LEU   A 1 250 ? 12.532  -6.195  75.444  1.00 25.94  ? 278 LEU   A CA  1 
ATOM   1703 C  C   . LEU   A 1 250 ? 11.312  -7.086  75.305  1.00 34.46  ? 278 LEU   A C   1 
ATOM   1704 O  O   . LEU   A 1 250 ? 10.365  -6.743  74.582  1.00 30.86  ? 278 LEU   A O   1 
ATOM   1705 C  CB  . LEU   A 1 250 ? 12.197  -4.906  76.196  1.00 28.31  ? 278 LEU   A CB  1 
ATOM   1706 C  CG  . LEU   A 1 250 ? 13.330  -3.891  76.296  1.00 32.31  ? 278 LEU   A CG  1 
ATOM   1707 C  CD1 . LEU   A 1 250 ? 12.804  -2.501  76.683  1.00 30.25  ? 278 LEU   A CD1 1 
ATOM   1708 C  CD2 . LEU   A 1 250 ? 14.351  -4.347  77.291  1.00 33.01  ? 278 LEU   A CD2 1 
ATOM   1709 N  N   . LEU   A 1 251 ? 11.342  -8.226  75.996  1.00 33.47  ? 279 LEU   A N   1 
ATOM   1710 C  CA  . LEU   A 1 251 ? 10.316  -9.260  75.885  1.00 34.43  ? 279 LEU   A CA  1 
ATOM   1711 C  C   . LEU   A 1 251 ? 9.838   -9.661  77.276  1.00 38.36  ? 279 LEU   A C   1 
ATOM   1712 O  O   . LEU   A 1 251 ? 10.187  -10.741 77.776  1.00 43.86  ? 279 LEU   A O   1 
ATOM   1713 C  CB  . LEU   A 1 251 ? 10.853  -10.474 75.126  1.00 34.19  ? 279 LEU   A CB  1 
ATOM   1714 C  CG  . LEU   A 1 251 ? 11.108  -10.281 73.632  1.00 30.83  ? 279 LEU   A CG  1 
ATOM   1715 C  CD1 . LEU   A 1 251 ? 11.836  -11.485 73.057  1.00 29.24  ? 279 LEU   A CD1 1 
ATOM   1716 C  CD2 . LEU   A 1 251 ? 9.817   -10.055 72.886  1.00 27.69  ? 279 LEU   A CD2 1 
ATOM   1717 N  N   . PRO   A 1 252 ? 9.043   -8.813  77.933  1.00 32.60  ? 280 PRO   A N   1 
ATOM   1718 C  CA  . PRO   A 1 252 ? 8.394   -9.238  79.176  1.00 34.67  ? 280 PRO   A CA  1 
ATOM   1719 C  C   . PRO   A 1 252 ? 7.538   -10.484 78.971  1.00 38.78  ? 280 PRO   A C   1 
ATOM   1720 O  O   . PRO   A 1 252 ? 7.078   -10.791 77.863  1.00 35.72  ? 280 PRO   A O   1 
ATOM   1721 C  CB  . PRO   A 1 252 ? 7.525   -8.040  79.555  1.00 36.52  ? 280 PRO   A CB  1 
ATOM   1722 C  CG  . PRO   A 1 252 ? 8.170   -6.855  78.866  1.00 36.18  ? 280 PRO   A CG  1 
ATOM   1723 C  CD  . PRO   A 1 252 ? 8.730   -7.412  77.587  1.00 33.57  ? 280 PRO   A CD  1 
ATOM   1724 N  N   . ILE   A 1 253 ? 7.312   -11.205 80.071  1.00 35.63  ? 281 ILE   A N   1 
ATOM   1725 C  CA  . ILE   A 1 253 ? 6.404   -12.350 80.078  1.00 37.77  ? 281 ILE   A CA  1 
ATOM   1726 C  C   . ILE   A 1 253 ? 5.627   -12.328 81.387  1.00 42.36  ? 281 ILE   A C   1 
ATOM   1727 O  O   . ILE   A 1 253 ? 6.212   -12.118 82.454  1.00 44.81  ? 281 ILE   A O   1 
ATOM   1728 C  CB  . ILE   A 1 253 ? 7.150   -13.682 79.907  1.00 38.33  ? 281 ILE   A CB  1 
ATOM   1729 C  CG1 . ILE   A 1 253 ? 7.848   -13.735 78.539  1.00 36.20  ? 281 ILE   A CG1 1 
ATOM   1730 C  CG2 . ILE   A 1 253 ? 6.177   -14.846 80.105  1.00 29.94  ? 281 ILE   A CG2 1 
ATOM   1731 C  CD1 . ILE   A 1 253 ? 8.725   -14.963 78.317  1.00 36.50  ? 281 ILE   A CD1 1 
ATOM   1732 N  N   . ASN   A 1 254 ? 4.310   -12.507 81.304  1.00 39.59  ? 282 ASN   A N   1 
ATOM   1733 C  CA  . ASN   A 1 254 ? 3.431   -12.512 82.463  1.00 40.87  ? 282 ASN   A CA  1 
ATOM   1734 C  C   . ASN   A 1 254 ? 2.897   -13.907 82.752  1.00 41.42  ? 282 ASN   A C   1 
ATOM   1735 O  O   . ASN   A 1 254 ? 2.682   -14.713 81.842  1.00 39.97  ? 282 ASN   A O   1 
ATOM   1736 C  CB  . ASN   A 1 254 ? 2.225   -11.603 82.265  1.00 38.17  ? 282 ASN   A CB  1 
ATOM   1737 C  CG  . ASN   A 1 254 ? 2.604   -10.172 82.064  1.00 45.14  ? 282 ASN   A CG  1 
ATOM   1738 O  OD1 . ASN   A 1 254 ? 3.695   -9.746  82.460  1.00 43.25  ? 282 ASN   A OD1 1 
ATOM   1739 N  ND2 . ASN   A 1 254 ? 1.693   -9.397  81.444  1.00 37.73  ? 282 ASN   A ND2 1 
ATOM   1740 N  N   . GLU   A 1 255 ? 2.634   -14.151 84.028  1.00 41.37  ? 283 GLU   A N   1 
ATOM   1741 C  CA  . GLU   A 1 255 ? 1.881   -15.299 84.499  1.00 40.65  ? 283 GLU   A CA  1 
ATOM   1742 C  C   . GLU   A 1 255 ? 0.914   -14.803 85.559  1.00 45.65  ? 283 GLU   A C   1 
ATOM   1743 O  O   . GLU   A 1 255 ? 1.136   -13.748 86.162  1.00 45.18  ? 283 GLU   A O   1 
ATOM   1744 C  CB  . GLU   A 1 255 ? 2.801   -16.381 85.079  1.00 44.66  ? 283 GLU   A CB  1 
ATOM   1745 C  CG  . GLU   A 1 255 ? 2.822   -16.414 86.584  1.00 46.71  ? 283 GLU   A CG  1 
ATOM   1746 C  CD  . GLU   A 1 255 ? 3.893   -17.337 87.128  1.00 47.91  ? 283 GLU   A CD  1 
ATOM   1747 O  OE1 . GLU   A 1 255 ? 4.580   -16.917 88.084  1.00 48.91  ? 283 GLU   A OE1 1 
ATOM   1748 O  OE2 . GLU   A 1 255 ? 4.050   -18.464 86.600  1.00 42.79  ? 283 GLU   A OE2 1 
ATOM   1749 N  N   . PRO   A 1 256 ? -0.176  -15.527 85.798  1.00 46.09  ? 284 PRO   A N   1 
ATOM   1750 C  CA  . PRO   A 1 256 ? -1.152  -15.094 86.800  1.00 45.69  ? 284 PRO   A CA  1 
ATOM   1751 C  C   . PRO   A 1 256 ? -0.752  -15.511 88.209  1.00 52.55  ? 284 PRO   A C   1 
ATOM   1752 O  O   . PRO   A 1 256 ? 0.118   -16.356 88.426  1.00 49.66  ? 284 PRO   A O   1 
ATOM   1753 C  CB  . PRO   A 1 256 ? -2.440  -15.812 86.380  1.00 47.88  ? 284 PRO   A CB  1 
ATOM   1754 C  CG  . PRO   A 1 256 ? -2.064  -16.727 85.245  1.00 47.53  ? 284 PRO   A CG  1 
ATOM   1755 C  CD  . PRO   A 1 256 ? -0.588  -16.781 85.151  1.00 43.72  ? 284 PRO   A CD  1 
ATOM   1756 N  N   . VAL   A 1 257 ? -1.429  -14.895 89.174  1.00 54.12  ? 285 VAL   A N   1 
ATOM   1757 C  CA  . VAL   A 1 257 ? -1.399  -15.311 90.571  1.00 54.74  ? 285 VAL   A CA  1 
ATOM   1758 C  C   . VAL   A 1 257 ? -2.832  -15.644 90.964  1.00 57.17  ? 285 VAL   A C   1 
ATOM   1759 O  O   . VAL   A 1 257 ? -3.694  -14.758 91.008  1.00 58.28  ? 285 VAL   A O   1 
ATOM   1760 C  CB  . VAL   A 1 257 ? -0.806  -14.231 91.484  1.00 55.13  ? 285 VAL   A CB  1 
ATOM   1761 C  CG1 . VAL   A 1 257 ? -0.786  -14.721 92.919  1.00 52.99  ? 285 VAL   A CG1 1 
ATOM   1762 C  CG2 . VAL   A 1 257 ? 0.602   -13.873 91.018  1.00 51.28  ? 285 VAL   A CG2 1 
ATOM   1763 N  N   . HIS   A 1 258 ? -3.093  -16.918 91.234  1.00 59.95  ? 286 HIS   A N   1 
ATOM   1764 C  CA  . HIS   A 1 258 ? -4.453  -17.373 91.476  1.00 58.17  ? 286 HIS   A CA  1 
ATOM   1765 C  C   . HIS   A 1 258 ? -4.848  -17.182 92.940  1.00 63.04  ? 286 HIS   A C   1 
ATOM   1766 O  O   . HIS   A 1 258 ? -4.006  -17.000 93.823  1.00 67.59  ? 286 HIS   A O   1 
ATOM   1767 C  CB  . HIS   A 1 258 ? -4.591  -18.843 91.078  1.00 59.76  ? 286 HIS   A CB  1 
ATOM   1768 C  CG  . HIS   A 1 258 ? -4.233  -19.115 89.650  1.00 58.28  ? 286 HIS   A CG  1 
ATOM   1769 N  ND1 . HIS   A 1 258 ? -3.191  -19.943 89.286  1.00 58.95  ? 286 HIS   A ND1 1 
ATOM   1770 C  CD2 . HIS   A 1 258 ? -4.771  -18.657 88.494  1.00 53.14  ? 286 HIS   A CD2 1 
ATOM   1771 C  CE1 . HIS   A 1 258 ? -3.108  -19.988 87.968  1.00 58.38  ? 286 HIS   A CE1 1 
ATOM   1772 N  NE2 . HIS   A 1 258 ? -4.054  -19.215 87.464  1.00 56.63  ? 286 HIS   A NE2 1 
ATOM   1773 N  N   . GLY   A 1 259 ? -6.158  -17.233 93.189  1.00 59.66  ? 287 GLY   A N   1 
ATOM   1774 C  CA  . GLY   A 1 259 ? -6.709  -17.094 94.522  1.00 65.17  ? 287 GLY   A CA  1 
ATOM   1775 C  C   . GLY   A 1 259 ? -6.907  -15.668 94.982  1.00 71.85  ? 287 GLY   A C   1 
ATOM   1776 O  O   . GLY   A 1 259 ? -7.506  -15.447 96.043  1.00 73.87  ? 287 GLY   A O   1 
ATOM   1777 N  N   . THR   A 1 260 ? -6.455  -14.699 94.197  1.00 72.12  ? 288 THR   A N   1 
ATOM   1778 C  CA  . THR   A 1 260 ? -6.402  -13.303 94.592  1.00 73.15  ? 288 THR   A CA  1 
ATOM   1779 C  C   . THR   A 1 260 ? -7.799  -12.703 94.801  1.00 74.31  ? 288 THR   A C   1 
ATOM   1780 O  O   . THR   A 1 260 ? -8.828  -13.280 94.439  1.00 72.16  ? 288 THR   A O   1 
ATOM   1781 C  CB  . THR   A 1 260 ? -5.634  -12.521 93.536  1.00 72.72  ? 288 THR   A CB  1 
ATOM   1782 O  OG1 . THR   A 1 260 ? -5.737  -11.115 93.798  1.00 79.90  ? 288 THR   A OG1 1 
ATOM   1783 C  CG2 . THR   A 1 260 ? -6.155  -12.877 92.145  1.00 65.99  ? 288 THR   A CG2 1 
ATOM   1784 N  N   . LYS   A 1 261 ? -7.806  -11.504 95.397  1.00 78.38  ? 289 LYS   A N   1 
ATOM   1785 C  CA  . LYS   A 1 261 ? -9.054  -10.820 95.730  1.00 81.22  ? 289 LYS   A CA  1 
ATOM   1786 C  C   . LYS   A 1 261 ? -9.934  -10.643 94.497  1.00 80.42  ? 289 LYS   A C   1 
ATOM   1787 O  O   . LYS   A 1 261 ? -11.074 -11.116 94.460  1.00 81.79  ? 289 LYS   A O   1 
ATOM   1788 C  CB  . LYS   A 1 261 ? -8.750  -9.466  96.384  1.00 76.66  ? 289 LYS   A CB  1 
ATOM   1789 N  N   . ARG   A 1 262 ? -9.414  -9.962  93.475  1.00 80.10  ? 290 ARG   A N   1 
ATOM   1790 C  CA  . ARG   A 1 262 ? -10.055 -9.851  92.169  1.00 74.31  ? 290 ARG   A CA  1 
ATOM   1791 C  C   . ARG   A 1 262 ? -9.328  -10.746 91.171  1.00 71.51  ? 290 ARG   A C   1 
ATOM   1792 O  O   . ARG   A 1 262 ? -8.094  -10.773 91.140  1.00 71.21  ? 290 ARG   A O   1 
ATOM   1793 C  CB  . ARG   A 1 262 ? -10.050 -8.402  91.671  1.00 68.58  ? 290 ARG   A CB  1 
ATOM   1794 N  N   . LYS   A 1 263 ? -10.100 -11.464 90.352  1.00 67.25  ? 291 LYS   A N   1 
ATOM   1795 C  CA  . LYS   A 1 263 ? -9.547  -12.475 89.454  1.00 62.83  ? 291 LYS   A CA  1 
ATOM   1796 C  C   . LYS   A 1 263 ? -8.361  -11.938 88.666  1.00 57.18  ? 291 LYS   A C   1 
ATOM   1797 O  O   . LYS   A 1 263 ? -8.333  -10.772 88.269  1.00 58.23  ? 291 LYS   A O   1 
ATOM   1798 C  CB  . LYS   A 1 263 ? -10.624 -12.970 88.483  1.00 56.98  ? 291 LYS   A CB  1 
ATOM   1799 C  CG  . LYS   A 1 263 ? -10.214 -14.194 87.669  1.00 56.02  ? 291 LYS   A CG  1 
ATOM   1800 C  CD  . LYS   A 1 263 ? -11.163 -14.422 86.497  1.00 48.40  ? 291 LYS   A CD  1 
ATOM   1801 C  CE  . LYS   A 1 263 ? -10.867 -15.739 85.793  1.00 53.49  ? 291 LYS   A CE  1 
ATOM   1802 N  NZ  . LYS   A 1 263 ? -11.996 -16.219 84.942  1.00 50.14  ? 291 LYS   A NZ  1 
ATOM   1803 N  N   . SER   A 1 264 ? -7.371  -12.797 88.453  1.00 58.71  ? 292 SER   A N   1 
ATOM   1804 C  CA  . SER   A 1 264 ? -6.225  -12.411 87.644  1.00 55.59  ? 292 SER   A CA  1 
ATOM   1805 C  C   . SER   A 1 264 ? -6.662  -12.157 86.208  1.00 53.35  ? 292 SER   A C   1 
ATOM   1806 O  O   . SER   A 1 264 ? -7.376  -12.964 85.607  1.00 49.27  ? 292 SER   A O   1 
ATOM   1807 C  CB  . SER   A 1 264 ? -5.153  -13.498 87.687  1.00 47.44  ? 292 SER   A CB  1 
ATOM   1808 O  OG  . SER   A 1 264 ? -4.106  -13.171 86.796  1.00 52.26  ? 292 SER   A OG  1 
ATOM   1809 N  N   . GLN   A 1 265 ? -6.241  -11.021 85.661  1.00 50.93  ? 293 GLN   A N   1 
ATOM   1810 C  CA  . GLN   A 1 265 ? -6.520  -10.730 84.263  1.00 49.92  ? 293 GLN   A CA  1 
ATOM   1811 C  C   . GLN   A 1 265 ? -5.562  -11.451 83.323  1.00 45.04  ? 293 GLN   A C   1 
ATOM   1812 O  O   . GLN   A 1 265 ? -5.882  -11.628 82.143  1.00 40.32  ? 293 GLN   A O   1 
ATOM   1813 C  CB  . GLN   A 1 265 ? -6.473  -9.217  84.020  1.00 49.14  ? 293 GLN   A CB  1 
ATOM   1814 C  CG  . GLN   A 1 265 ? -5.231  -8.499  84.586  1.00 55.41  ? 293 GLN   A CG  1 
ATOM   1815 C  CD  . GLN   A 1 265 ? -5.348  -8.124  86.077  1.00 65.42  ? 293 GLN   A CD  1 
ATOM   1816 O  OE1 . GLN   A 1 265 ? -6.233  -8.610  86.793  1.00 64.34  ? 293 GLN   A OE1 1 
ATOM   1817 N  NE2 . GLN   A 1 265 ? -4.468  -7.229  86.534  1.00 61.03  ? 293 GLN   A NE2 1 
ATOM   1818 N  N   . ILE   A 1 266 ? -4.392  -11.866 83.808  1.00 47.01  ? 294 ILE   A N   1 
ATOM   1819 C  CA  . ILE   A 1 266 ? -3.586  -12.799 83.027  1.00 41.44  ? 294 ILE   A CA  1 
ATOM   1820 C  C   . ILE   A 1 266 ? -4.351  -14.095 82.829  1.00 42.32  ? 294 ILE   A C   1 
ATOM   1821 O  O   . ILE   A 1 266 ? -4.288  -14.720 81.765  1.00 39.68  ? 294 ILE   A O   1 
ATOM   1822 C  CB  . ILE   A 1 266 ? -2.239  -13.055 83.710  1.00 39.80  ? 294 ILE   A CB  1 
ATOM   1823 C  CG1 . ILE   A 1 266 ? -1.558  -11.723 84.052  1.00 47.35  ? 294 ILE   A CG1 1 
ATOM   1824 C  CG2 . ILE   A 1 266 ? -1.375  -13.955 82.822  1.00 39.64  ? 294 ILE   A CG2 1 
ATOM   1825 C  CD1 . ILE   A 1 266 ? -1.294  -10.832 82.861  1.00 40.09  ? 294 ILE   A CD1 1 
ATOM   1826 N  N   . GLN   A 1 267 ? -5.089  -14.520 83.855  1.00 45.68  ? 295 GLN   A N   1 
ATOM   1827 C  CA  . GLN   A 1 267 ? -5.905  -15.713 83.712  1.00 42.82  ? 295 GLN   A CA  1 
ATOM   1828 C  C   . GLN   A 1 267 ? -7.040  -15.474 82.725  1.00 44.30  ? 295 GLN   A C   1 
ATOM   1829 O  O   . GLN   A 1 267 ? -7.270  -16.305 81.834  1.00 41.64  ? 295 GLN   A O   1 
ATOM   1830 C  CB  . GLN   A 1 267 ? -6.438  -16.161 85.073  1.00 47.24  ? 295 GLN   A CB  1 
ATOM   1831 C  CG  . GLN   A 1 267 ? -7.359  -17.384 85.004  1.00 46.19  ? 295 GLN   A CG  1 
ATOM   1832 C  CD  . GLN   A 1 267 ? -6.612  -18.668 84.673  1.00 42.41  ? 295 GLN   A CD  1 
ATOM   1833 O  OE1 . GLN   A 1 267 ? -5.417  -18.790 84.930  1.00 48.03  ? 295 GLN   A OE1 1 
ATOM   1834 N  NE2 . GLN   A 1 267 ? -7.317  -19.626 84.079  1.00 47.06  ? 295 GLN   A NE2 1 
ATOM   1835 N  N   . THR   A 1 268 ? -7.736  -14.329 82.836  1.00 43.61  ? 296 THR   A N   1 
ATOM   1836 C  CA  . THR   A 1 268 ? -8.803  -14.021 81.880  1.00 39.44  ? 296 THR   A CA  1 
ATOM   1837 C  C   . THR   A 1 268 ? -8.272  -14.049 80.457  1.00 37.52  ? 296 THR   A C   1 
ATOM   1838 O  O   . THR   A 1 268 ? -8.936  -14.557 79.548  1.00 39.05  ? 296 THR   A O   1 
ATOM   1839 C  CB  . THR   A 1 268 ? -9.435  -12.659 82.183  1.00 43.03  ? 296 THR   A CB  1 
ATOM   1840 O  OG1 . THR   A 1 268 ? -10.287 -12.771 83.328  1.00 47.90  ? 296 THR   A OG1 1 
ATOM   1841 C  CG2 . THR   A 1 268 ? -10.283 -12.165 80.990  1.00 36.19  ? 296 THR   A CG2 1 
ATOM   1842 N  N   . TYR   A 1 269 ? -7.058  -13.536 80.250  1.00 36.54  ? 297 TYR   A N   1 
ATOM   1843 C  CA  . TYR   A 1 269 ? -6.433  -13.647 78.938  1.00 38.43  ? 297 TYR   A CA  1 
ATOM   1844 C  C   . TYR   A 1 269 ? -6.333  -15.108 78.512  1.00 36.25  ? 297 TYR   A C   1 
ATOM   1845 O  O   . TYR   A 1 269 ? -6.808  -15.491 77.436  1.00 39.11  ? 297 TYR   A O   1 
ATOM   1846 C  CB  . TYR   A 1 269 ? -5.044  -13.000 78.948  1.00 34.17  ? 297 TYR   A CB  1 
ATOM   1847 C  CG  . TYR   A 1 269 ? -4.349  -13.104 77.602  1.00 34.54  ? 297 TYR   A CG  1 
ATOM   1848 C  CD1 . TYR   A 1 269 ? -3.759  -14.301 77.185  1.00 33.12  ? 297 TYR   A CD1 1 
ATOM   1849 C  CD2 . TYR   A 1 269 ? -4.274  -12.011 76.753  1.00 30.65  ? 297 TYR   A CD2 1 
ATOM   1850 C  CE1 . TYR   A 1 269 ? -3.141  -14.409 75.965  1.00 31.59  ? 297 TYR   A CE1 1 
ATOM   1851 C  CE2 . TYR   A 1 269 ? -3.642  -12.109 75.527  1.00 30.17  ? 297 TYR   A CE2 1 
ATOM   1852 C  CZ  . TYR   A 1 269 ? -3.088  -13.314 75.134  1.00 30.98  ? 297 TYR   A CZ  1 
ATOM   1853 O  OH  . TYR   A 1 269 ? -2.465  -13.428 73.911  1.00 30.25  ? 297 TYR   A OH  1 
ATOM   1854 N  N   . LEU   A 1 270 ? -5.696  -15.938 79.340  1.00 31.64  ? 298 LEU   A N   1 
ATOM   1855 C  CA  . LEU   A 1 270 ? -5.486  -17.336 78.964  1.00 38.67  ? 298 LEU   A CA  1 
ATOM   1856 C  C   . LEU   A 1 270 ? -6.801  -18.044 78.652  1.00 31.55  ? 298 LEU   A C   1 
ATOM   1857 O  O   . LEU   A 1 270 ? -6.852  -18.864 77.729  1.00 33.87  ? 298 LEU   A O   1 
ATOM   1858 C  CB  . LEU   A 1 270 ? -4.735  -18.085 80.066  1.00 35.36  ? 298 LEU   A CB  1 
ATOM   1859 C  CG  . LEU   A 1 270 ? -3.355  -17.569 80.447  1.00 34.61  ? 298 LEU   A CG  1 
ATOM   1860 C  CD1 . LEU   A 1 270 ? -2.983  -18.245 81.733  1.00 38.90  ? 298 LEU   A CD1 1 
ATOM   1861 C  CD2 . LEU   A 1 270 ? -2.341  -17.859 79.342  1.00 31.52  ? 298 LEU   A CD2 1 
ATOM   1862 N  N   . GLU   A 1 271 ? -7.873  -17.738 79.395  1.00 32.06  ? 299 GLU   A N   1 
ATOM   1863 C  CA  . GLU   A 1 271 ? -9.170  -18.382 79.130  1.00 43.76  ? 299 GLU   A CA  1 
ATOM   1864 C  C   . GLU   A 1 271 ? -9.738  -17.963 77.777  1.00 38.06  ? 299 GLU   A C   1 
ATOM   1865 O  O   . GLU   A 1 271 ? -10.145 -18.811 76.975  1.00 36.58  ? 299 GLU   A O   1 
ATOM   1866 C  CB  . GLU   A 1 271 ? -10.180 -18.065 80.246  1.00 43.54  ? 299 GLU   A CB  1 
ATOM   1867 C  CG  . GLU   A 1 271 ? -9.557  -18.075 81.639  1.00 51.06  ? 299 GLU   A CG  1 
ATOM   1868 C  CD  . GLU   A 1 271 ? -10.536 -18.178 82.802  1.00 48.52  ? 299 GLU   A CD  1 
ATOM   1869 O  OE1 . GLU   A 1 271 ? -10.289 -19.028 83.689  1.00 50.24  ? 299 GLU   A OE1 1 
ATOM   1870 O  OE2 . GLU   A 1 271 ? -11.518 -17.412 82.849  1.00 44.94  ? 299 GLU   A OE2 1 
ATOM   1871 N  N   . HIS   A 1 272 ? -9.768  -16.655 77.500  1.00 35.06  ? 300 HIS   A N   1 
ATOM   1872 C  CA  . HIS   A 1 272 ? -10.372 -16.179 76.262  1.00 33.45  ? 300 HIS   A CA  1 
ATOM   1873 C  C   . HIS   A 1 272 ? -9.455  -16.333 75.052  1.00 34.95  ? 300 HIS   A C   1 
ATOM   1874 O  O   . HIS   A 1 272 ? -9.948  -16.349 73.917  1.00 34.53  ? 300 HIS   A O   1 
ATOM   1875 C  CB  . HIS   A 1 272 ? -10.795 -14.720 76.431  1.00 35.33  ? 300 HIS   A CB  1 
ATOM   1876 C  CG  . HIS   A 1 272 ? -11.953 -14.537 77.363  1.00 35.94  ? 300 HIS   A CG  1 
ATOM   1877 N  ND1 . HIS   A 1 272 ? -13.234 -14.268 76.920  1.00 35.21  ? 300 HIS   A ND1 1 
ATOM   1878 C  CD2 . HIS   A 1 272 ? -12.027 -14.606 78.713  1.00 31.41  ? 300 HIS   A CD2 1 
ATOM   1879 C  CE1 . HIS   A 1 272 ? -14.043 -14.167 77.961  1.00 33.64  ? 300 HIS   A CE1 1 
ATOM   1880 N  NE2 . HIS   A 1 272 ? -13.337 -14.385 79.059  1.00 32.68  ? 300 HIS   A NE2 1 
ATOM   1881 N  N   . ASN   A 1 273 ? -8.149  -16.461 75.259  1.00 30.14  ? 301 ASN   A N   1 
ATOM   1882 C  CA  . ASN   A 1 273 ? -7.213  -16.649 74.159  1.00 34.41  ? 301 ASN   A CA  1 
ATOM   1883 C  C   . ASN   A 1 273 ? -7.010  -18.104 73.770  1.00 33.31  ? 301 ASN   A C   1 
ATOM   1884 O  O   . ASN   A 1 273 ? -6.294  -18.364 72.794  1.00 33.53  ? 301 ASN   A O   1 
ATOM   1885 C  CB  . ASN   A 1 273 ? -5.826  -16.079 74.502  1.00 34.75  ? 301 ASN   A CB  1 
ATOM   1886 C  CG  . ASN   A 1 273 ? -5.009  -15.795 73.265  1.00 32.91  ? 301 ASN   A CG  1 
ATOM   1887 O  OD1 . ASN   A 1 273 ? -5.496  -15.149 72.342  1.00 36.38  ? 301 ASN   A OD1 1 
ATOM   1888 N  ND2 . ASN   A 1 273 ? -3.791  -16.312 73.212  1.00 30.26  ? 301 ASN   A ND2 1 
ATOM   1889 N  N   . GLU   A 1 274 ? -7.605  -19.045 74.502  1.00 29.73  ? 302 GLU   A N   1 
ATOM   1890 C  CA  . GLU   A 1 274 ? -7.260  -20.462 74.411  1.00 31.23  ? 302 GLU   A CA  1 
ATOM   1891 C  C   . GLU   A 1 274 ? -5.753  -20.671 74.548  1.00 33.80  ? 302 GLU   A C   1 
ATOM   1892 O  O   . GLU   A 1 274 ? -5.107  -21.328 73.731  1.00 39.62  ? 302 GLU   A O   1 
ATOM   1893 C  CB  . GLU   A 1 274 ? -7.794  -21.077 73.118  1.00 31.68  ? 302 GLU   A CB  1 
ATOM   1894 C  CG  . GLU   A 1 274 ? -9.332  -21.097 73.061  1.00 35.99  ? 302 GLU   A CG  1 
ATOM   1895 C  CD  . GLU   A 1 274 ? -9.884  -21.857 71.866  1.00 27.03  ? 302 GLU   A CD  1 
ATOM   1896 O  OE1 . GLU   A 1 274 ? -9.100  -22.484 71.137  1.00 31.09  ? 302 GLU   A OE1 1 
ATOM   1897 O  OE2 . GLU   A 1 274 ? -11.104 -21.783 71.629  1.00 33.16  ? 302 GLU   A OE2 1 
ATOM   1898 N  N   . GLY   A 1 275 ? -5.187  -20.106 75.593  1.00 31.29  ? 303 GLY   A N   1 
ATOM   1899 C  CA  . GLY   A 1 275 ? -3.813  -20.405 75.947  1.00 32.23  ? 303 GLY   A CA  1 
ATOM   1900 C  C   . GLY   A 1 275 ? -2.902  -19.205 75.777  1.00 39.40  ? 303 GLY   A C   1 
ATOM   1901 O  O   . GLY   A 1 275 ? -3.331  -18.083 75.470  1.00 35.77  ? 303 GLY   A O   1 
ATOM   1902 N  N   . ALA   A 1 276 ? -1.616  -19.466 75.980  1.00 33.48  ? 304 ALA   A N   1 
ATOM   1903 C  CA  . ALA   A 1 276 ? -0.616  -18.415 75.917  1.00 32.27  ? 304 ALA   A CA  1 
ATOM   1904 C  C   . ALA   A 1 276 ? -0.661  -17.697 74.576  1.00 32.62  ? 304 ALA   A C   1 
ATOM   1905 O  O   . ALA   A 1 276 ? -1.068  -18.263 73.556  1.00 31.02  ? 304 ALA   A O   1 
ATOM   1906 C  CB  . ALA   A 1 276 ? 0.780   -19.005 76.147  1.00 37.71  ? 304 ALA   A CB  1 
ATOM   1907 N  N   . GLY   A 1 277 ? -0.248  -16.431 74.598  1.00 31.93  ? 305 GLY   A N   1 
ATOM   1908 C  CA  . GLY   A 1 277 ? -0.054  -15.643 73.396  1.00 31.48  ? 305 GLY   A CA  1 
ATOM   1909 C  C   . GLY   A 1 277 ? 0.464   -14.263 73.761  1.00 32.65  ? 305 GLY   A C   1 
ATOM   1910 O  O   . GLY   A 1 277 ? 0.684   -13.939 74.933  1.00 35.11  ? 305 GLY   A O   1 
ATOM   1911 N  N   . LEU   A 1 278 ? 0.643   -13.440 72.738  1.00 31.18  ? 306 LEU   A N   1 
ATOM   1912 C  CA  . LEU   A 1 278 ? 1.023   -12.054 72.961  1.00 29.09  ? 306 LEU   A CA  1 
ATOM   1913 C  C   . LEU   A 1 278 ? -0.105  -11.296 73.657  1.00 32.59  ? 306 LEU   A C   1 
ATOM   1914 O  O   . LEU   A 1 278 ? -1.250  -11.294 73.187  1.00 33.72  ? 306 LEU   A O   1 
ATOM   1915 C  CB  . LEU   A 1 278 ? 1.352   -11.383 71.636  1.00 27.79  ? 306 LEU   A CB  1 
ATOM   1916 C  CG  . LEU   A 1 278 ? 1.963   -10.001 71.897  1.00 34.47  ? 306 LEU   A CG  1 
ATOM   1917 C  CD1 . LEU   A 1 278 ? 3.317   -9.947  71.253  1.00 30.58  ? 306 LEU   A CD1 1 
ATOM   1918 C  CD2 . LEU   A 1 278 ? 1.089   -8.869  71.390  1.00 29.81  ? 306 LEU   A CD2 1 
ATOM   1919 N  N   . GLN   A 1 279 ? 0.223   -10.637 74.773  1.00 28.08  ? 307 GLN   A N   1 
ATOM   1920 C  CA  . GLN   A 1 279 ? -0.759  -9.869  75.530  1.00 28.04  ? 307 GLN   A CA  1 
ATOM   1921 C  C   . GLN   A 1 279 ? -0.823  -8.409  75.071  1.00 33.18  ? 307 GLN   A C   1 
ATOM   1922 O  O   . GLN   A 1 279 ? -1.895  -7.913  74.721  1.00 30.96  ? 307 GLN   A O   1 
ATOM   1923 C  CB  . GLN   A 1 279 ? -0.449  -9.931  77.027  1.00 31.40  ? 307 GLN   A CB  1 
ATOM   1924 C  CG  . GLN   A 1 279 ? -1.471  -9.198  77.896  1.00 33.19  ? 307 GLN   A CG  1 
ATOM   1925 C  CD  . GLN   A 1 279 ? -0.852  -8.595  79.159  1.00 35.01  ? 307 GLN   A CD  1 
ATOM   1926 O  OE1 . GLN   A 1 279 ? 0.329   -8.228  79.172  1.00 34.84  ? 307 GLN   A OE1 1 
ATOM   1927 N  NE2 . GLN   A 1 279 ? -1.650  -8.496  80.228  1.00 29.55  ? 307 GLN   A NE2 1 
ATOM   1928 N  N   . HIS   A 1 280 ? 0.306   -7.702  75.068  1.00 29.57  ? 308 HIS   A N   1 
ATOM   1929 C  CA  . HIS   A 1 280 ? 0.240   -6.320  74.635  1.00 31.45  ? 308 HIS   A CA  1 
ATOM   1930 C  C   . HIS   A 1 280 ? 1.522   -5.898  73.939  1.00 31.00  ? 308 HIS   A C   1 
ATOM   1931 O  O   . HIS   A 1 280 ? 2.586   -6.492  74.114  1.00 31.36  ? 308 HIS   A O   1 
ATOM   1932 C  CB  . HIS   A 1 280 ? -0.122  -5.371  75.791  1.00 29.72  ? 308 HIS   A CB  1 
ATOM   1933 C  CG  . HIS   A 1 280 ? 0.968   -5.119  76.789  1.00 36.01  ? 308 HIS   A CG  1 
ATOM   1934 N  ND1 . HIS   A 1 280 ? 1.214   -5.959  77.854  1.00 34.25  ? 308 HIS   A ND1 1 
ATOM   1935 C  CD2 . HIS   A 1 280 ? 1.796   -4.054  76.951  1.00 33.46  ? 308 HIS   A CD2 1 
ATOM   1936 C  CE1 . HIS   A 1 280 ? 2.170   -5.442  78.605  1.00 37.99  ? 308 HIS   A CE1 1 
ATOM   1937 N  NE2 . HIS   A 1 280 ? 2.549   -4.294  78.070  1.00 33.20  ? 308 HIS   A NE2 1 
ATOM   1938 N  N   . LEU   A 1 281 ? 1.364   -4.898  73.079  1.00 28.84  ? 309 LEU   A N   1 
ATOM   1939 C  CA  . LEU   A 1 281 ? 2.441   -4.239  72.363  1.00 29.08  ? 309 LEU   A CA  1 
ATOM   1940 C  C   . LEU   A 1 281 ? 2.571   -2.828  72.924  1.00 33.22  ? 309 LEU   A C   1 
ATOM   1941 O  O   . LEU   A 1 281 ? 1.583   -2.083  72.954  1.00 29.87  ? 309 LEU   A O   1 
ATOM   1942 C  CB  . LEU   A 1 281 ? 2.139   -4.178  70.862  1.00 24.22  ? 309 LEU   A CB  1 
ATOM   1943 C  CG  . LEU   A 1 281 ? 1.897   -5.486  70.106  1.00 30.93  ? 309 LEU   A CG  1 
ATOM   1944 C  CD1 . LEU   A 1 281 ? 1.291   -5.184  68.755  1.00 24.80  ? 309 LEU   A CD1 1 
ATOM   1945 C  CD2 . LEU   A 1 281 ? 3.193   -6.299  69.923  1.00 25.54  ? 309 LEU   A CD2 1 
ATOM   1946 N  N   . ALA   A 1 282 ? 3.772   -2.450  73.360  1.00 28.21  ? 310 ALA   A N   1 
ATOM   1947 C  CA  . ALA   A 1 282 ? 4.003   -1.096  73.864  1.00 27.89  ? 310 ALA   A CA  1 
ATOM   1948 C  C   . ALA   A 1 282 ? 4.720   -0.261  72.812  1.00 27.36  ? 310 ALA   A C   1 
ATOM   1949 O  O   . ALA   A 1 282 ? 5.880   -0.531  72.481  1.00 28.51  ? 310 ALA   A O   1 
ATOM   1950 C  CB  . ALA   A 1 282 ? 4.806   -1.121  75.155  1.00 29.12  ? 310 ALA   A CB  1 
ATOM   1951 N  N   . LEU   A 1 283 ? 4.043   0.767   72.312  1.00 31.46  ? 311 LEU   A N   1 
ATOM   1952 C  CA  . LEU   A 1 283 ? 4.542   1.574   71.207  1.00 30.86  ? 311 LEU   A CA  1 
ATOM   1953 C  C   . LEU   A 1 283 ? 5.084   2.893   71.747  1.00 32.88  ? 311 LEU   A C   1 
ATOM   1954 O  O   . LEU   A 1 283 ? 4.385   3.603   72.481  1.00 33.48  ? 311 LEU   A O   1 
ATOM   1955 C  CB  . LEU   A 1 283 ? 3.429   1.825   70.189  1.00 32.88  ? 311 LEU   A CB  1 
ATOM   1956 C  CG  . LEU   A 1 283 ? 2.443   0.654   69.988  1.00 28.91  ? 311 LEU   A CG  1 
ATOM   1957 C  CD1 . LEU   A 1 283 ? 1.392   1.004   68.958  1.00 25.53  ? 311 LEU   A CD1 1 
ATOM   1958 C  CD2 . LEU   A 1 283 ? 3.167   -0.570  69.554  1.00 22.75  ? 311 LEU   A CD2 1 
ATOM   1959 N  N   . MET   A 1 284 ? 6.321   3.228   71.386  1.00 32.09  ? 312 MET   A N   1 
ATOM   1960 C  CA  . MET   A 1 284 ? 6.902   4.479   71.874  1.00 32.50  ? 312 MET   A CA  1 
ATOM   1961 C  C   . MET   A 1 284 ? 6.431   5.654   71.028  1.00 29.52  ? 312 MET   A C   1 
ATOM   1962 O  O   . MET   A 1 284 ? 6.470   5.602   69.794  1.00 31.90  ? 312 MET   A O   1 
ATOM   1963 C  CB  A MET   A 1 284 ? 8.432   4.420   71.879  0.55 31.53  ? 312 MET   A CB  1 
ATOM   1964 C  CB  B MET   A 1 284 ? 8.432   4.407   71.863  0.45 33.10  ? 312 MET   A CB  1 
ATOM   1965 C  CG  A MET   A 1 284 ? 9.078   5.642   72.585  0.55 30.30  ? 312 MET   A CG  1 
ATOM   1966 C  CG  B MET   A 1 284 ? 9.138   5.709   72.315  0.45 30.54  ? 312 MET   A CG  1 
ATOM   1967 S  SD  A MET   A 1 284 ? 10.868  5.586   72.721  0.55 40.95  ? 312 MET   A SD  1 
ATOM   1968 S  SD  B MET   A 1 284 ? 9.779   6.657   70.915  0.45 39.71  ? 312 MET   A SD  1 
ATOM   1969 C  CE  A MET   A 1 284 ? 11.093  4.495   74.124  0.55 34.86  ? 312 MET   A CE  1 
ATOM   1970 C  CE  B MET   A 1 284 ? 10.200  8.235   71.681  0.45 29.57  ? 312 MET   A CE  1 
ATOM   1971 N  N   . SER   A 1 285 ? 6.008   6.722   71.690  1.00 25.97  ? 313 SER   A N   1 
ATOM   1972 C  CA  . SER   A 1 285 ? 5.674   7.967   71.012  1.00 30.81  ? 313 SER   A CA  1 
ATOM   1973 C  C   . SER   A 1 285 ? 6.728   9.030   71.314  1.00 36.23  ? 313 SER   A C   1 
ATOM   1974 O  O   . SER   A 1 285 ? 7.219   9.130   72.443  1.00 34.12  ? 313 SER   A O   1 
ATOM   1975 C  CB  . SER   A 1 285 ? 4.311   8.485   71.444  1.00 29.35  ? 313 SER   A CB  1 
ATOM   1976 O  OG  . SER   A 1 285 ? 4.114   9.785   70.932  1.00 34.80  ? 313 SER   A OG  1 
ATOM   1977 N  N   . GLU   A 1 286 ? 7.079   9.814   70.299  1.00 37.80  ? 314 GLU   A N   1 
ATOM   1978 C  CA  . GLU   A 1 286 ? 7.936   10.977  70.499  1.00 41.96  ? 314 GLU   A CA  1 
ATOM   1979 C  C   . GLU   A 1 286 ? 7.178   12.163  71.083  1.00 41.25  ? 314 GLU   A C   1 
ATOM   1980 O  O   . GLU   A 1 286 ? 7.766   13.234  71.259  1.00 42.38  ? 314 GLU   A O   1 
ATOM   1981 C  CB  . GLU   A 1 286 ? 8.597   11.385  69.181  1.00 41.44  ? 314 GLU   A CB  1 
ATOM   1982 C  CG  . GLU   A 1 286 ? 7.626   11.981  68.161  1.00 38.88  ? 314 GLU   A CG  1 
ATOM   1983 C  CD  . GLU   A 1 286 ? 8.349   12.791  67.095  1.00 48.73  ? 314 GLU   A CD  1 
ATOM   1984 O  OE1 . GLU   A 1 286 ? 9.577   12.594  66.918  1.00 49.18  ? 314 GLU   A OE1 1 
ATOM   1985 O  OE2 . GLU   A 1 286 ? 7.692   13.624  66.435  1.00 52.33  ? 314 GLU   A OE2 1 
ATOM   1986 N  N   . ASP   A 1 287 ? 5.900   11.992  71.405  1.00 39.69  ? 315 ASP   A N   1 
ATOM   1987 C  CA  . ASP   A 1 287 ? 5.089   13.048  72.000  1.00 37.50  ? 315 ASP   A CA  1 
ATOM   1988 C  C   . ASP   A 1 287 ? 3.800   12.404  72.488  1.00 38.51  ? 315 ASP   A C   1 
ATOM   1989 O  O   . ASP   A 1 287 ? 2.763   12.515  71.818  1.00 36.67  ? 315 ASP   A O   1 
ATOM   1990 C  CB  . ASP   A 1 287 ? 4.824   14.156  70.972  1.00 39.41  ? 315 ASP   A CB  1 
ATOM   1991 C  CG  . ASP   A 1 287 ? 4.064   15.353  71.542  1.00 34.23  ? 315 ASP   A CG  1 
ATOM   1992 O  OD1 . ASP   A 1 287 ? 3.539   15.296  72.681  1.00 32.93  ? 315 ASP   A OD1 1 
ATOM   1993 O  OD2 . ASP   A 1 287 ? 3.982   16.365  70.811  1.00 41.53  ? 315 ASP   A OD2 1 
ATOM   1994 N  N   . ILE   A 1 288 ? 3.864   11.704  73.631  1.00 33.50  ? 316 ILE   A N   1 
ATOM   1995 C  CA  . ILE   A 1 288 ? 2.718   10.937  74.091  1.00 36.14  ? 316 ILE   A CA  1 
ATOM   1996 C  C   . ILE   A 1 288 ? 1.483   11.809  74.226  1.00 35.81  ? 316 ILE   A C   1 
ATOM   1997 O  O   . ILE   A 1 288 ? 0.361   11.301  74.179  1.00 35.76  ? 316 ILE   A O   1 
ATOM   1998 C  CB  . ILE   A 1 288 ? 2.995   10.209  75.423  1.00 34.36  ? 316 ILE   A CB  1 
ATOM   1999 C  CG1 . ILE   A 1 288 ? 1.953   9.083   75.621  1.00 36.25  ? 316 ILE   A CG1 1 
ATOM   2000 C  CG2 . ILE   A 1 288 ? 2.930   11.179  76.582  1.00 37.87  ? 316 ILE   A CG2 1 
ATOM   2001 C  CD1 . ILE   A 1 288 ? 2.035   8.330   76.951  1.00 32.86  ? 316 ILE   A CD1 1 
ATOM   2002 N  N   . PHE   A 1 289 ? 1.651   13.117  74.389  1.00 39.30  ? 317 PHE   A N   1 
ATOM   2003 C  CA  . PHE   A 1 289 ? 0.476   13.962  74.550  1.00 42.08  ? 317 PHE   A CA  1 
ATOM   2004 C  C   . PHE   A 1 289 ? -0.250  14.164  73.230  1.00 35.60  ? 317 PHE   A C   1 
ATOM   2005 O  O   . PHE   A 1 289 ? -1.482  14.111  73.185  1.00 38.57  ? 317 PHE   A O   1 
ATOM   2006 C  CB  . PHE   A 1 289 ? 0.879   15.298  75.169  1.00 41.46  ? 317 PHE   A CB  1 
ATOM   2007 C  CG  . PHE   A 1 289 ? 1.222   15.196  76.618  1.00 41.55  ? 317 PHE   A CG  1 
ATOM   2008 C  CD1 . PHE   A 1 289 ? 2.533   15.104  77.031  1.00 43.71  ? 317 PHE   A CD1 1 
ATOM   2009 C  CD2 . PHE   A 1 289 ? 0.228   15.157  77.574  1.00 46.16  ? 317 PHE   A CD2 1 
ATOM   2010 C  CE1 . PHE   A 1 289 ? 2.856   15.009  78.375  1.00 49.10  ? 317 PHE   A CE1 1 
ATOM   2011 C  CE2 . PHE   A 1 289 ? 0.547   15.061  78.924  1.00 54.70  ? 317 PHE   A CE2 1 
ATOM   2012 C  CZ  . PHE   A 1 289 ? 1.865   14.987  79.321  1.00 47.04  ? 317 PHE   A CZ  1 
ATOM   2013 N  N   . ARG   A 1 290 ? 0.494   14.392  72.148  1.00 35.89  ? 318 ARG   A N   1 
ATOM   2014 C  CA  . ARG   A 1 290 ? -0.143  14.546  70.849  1.00 38.58  ? 318 ARG   A CA  1 
ATOM   2015 C  C   . ARG   A 1 290 ? -0.754  13.224  70.382  1.00 37.78  ? 318 ARG   A C   1 
ATOM   2016 O  O   . ARG   A 1 290 ? -1.886  13.196  69.872  1.00 34.09  ? 318 ARG   A O   1 
ATOM   2017 C  CB  . ARG   A 1 290 ? 0.876   15.075  69.845  1.00 37.23  ? 318 ARG   A CB  1 
ATOM   2018 C  CG  . ARG   A 1 290 ? 0.378   15.088  68.431  1.00 34.81  ? 318 ARG   A CG  1 
ATOM   2019 C  CD  . ARG   A 1 290 ? 1.389   15.759  67.531  1.00 37.67  ? 318 ARG   A CD  1 
ATOM   2020 N  NE  . ARG   A 1 290 ? 1.522   15.021  66.284  1.00 45.84  ? 318 ARG   A NE  1 
ATOM   2021 C  CZ  . ARG   A 1 290 ? 2.486   14.138  66.051  1.00 42.08  ? 318 ARG   A CZ  1 
ATOM   2022 N  NH1 . ARG   A 1 290 ? 3.405   13.911  66.983  1.00 46.32  ? 318 ARG   A NH1 1 
ATOM   2023 N  NH2 . ARG   A 1 290 ? 2.545   13.498  64.886  1.00 41.83  ? 318 ARG   A NH2 1 
ATOM   2024 N  N   . THR   A 1 291 ? -0.029  12.117  70.568  1.00 34.38  ? 319 THR   A N   1 
ATOM   2025 C  CA  . THR   A 1 291 ? -0.578  10.805  70.241  1.00 32.62  ? 319 THR   A CA  1 
ATOM   2026 C  C   . THR   A 1 291 ? -1.909  10.585  70.933  1.00 34.44  ? 319 THR   A C   1 
ATOM   2027 O  O   . THR   A 1 291 ? -2.917  10.286  70.283  1.00 35.19  ? 319 THR   A O   1 
ATOM   2028 C  CB  . THR   A 1 291 ? 0.411   9.720   70.630  1.00 32.62  ? 319 THR   A CB  1 
ATOM   2029 O  OG1 . THR   A 1 291 ? 1.646   9.988   69.969  1.00 32.48  ? 319 THR   A OG1 1 
ATOM   2030 C  CG2 . THR   A 1 291 ? -0.110  8.330   70.216  1.00 31.71  ? 319 THR   A CG2 1 
ATOM   2031 N  N   . LEU   A 1 292 ? -1.939  10.776  72.253  1.00 30.29  ? 320 LEU   A N   1 
ATOM   2032 C  CA  . LEU   A 1 292 ? -3.153  10.492  72.998  1.00 32.65  ? 320 LEU   A CA  1 
ATOM   2033 C  C   . LEU   A 1 292 ? -4.285  11.449  72.655  1.00 36.56  ? 320 LEU   A C   1 
ATOM   2034 O  O   . LEU   A 1 292 ? -5.450  11.030  72.646  1.00 36.32  ? 320 LEU   A O   1 
ATOM   2035 C  CB  . LEU   A 1 292 ? -2.862  10.507  74.488  1.00 38.00  ? 320 LEU   A CB  1 
ATOM   2036 C  CG  . LEU   A 1 292 ? -2.865  9.041   74.934  1.00 39.97  ? 320 LEU   A CG  1 
ATOM   2037 C  CD1 . LEU   A 1 292 ? -1.697  8.296   74.347  1.00 34.57  ? 320 LEU   A CD1 1 
ATOM   2038 C  CD2 . LEU   A 1 292 ? -2.850  8.968   76.413  1.00 39.68  ? 320 LEU   A CD2 1 
ATOM   2039 N  N   . ARG   A 1 293 ? -3.987  12.725  72.376  1.00 33.98  ? 321 ARG   A N   1 
ATOM   2040 C  CA  . ARG   A 1 293 ? -5.036  13.599  71.852  1.00 34.66  ? 321 ARG   A CA  1 
ATOM   2041 C  C   . ARG   A 1 293 ? -5.575  13.048  70.538  1.00 30.65  ? 321 ARG   A C   1 
ATOM   2042 O  O   . ARG   A 1 293 ? -6.792  12.952  70.333  1.00 31.63  ? 321 ARG   A O   1 
ATOM   2043 C  CB  . ARG   A 1 293 ? -4.511  15.023  71.628  1.00 37.47  ? 321 ARG   A CB  1 
ATOM   2044 C  CG  . ARG   A 1 293 ? -4.251  15.848  72.891  1.00 42.04  ? 321 ARG   A CG  1 
ATOM   2045 C  CD  . ARG   A 1 293 ? -4.113  17.349  72.570  1.00 32.00  ? 321 ARG   A CD  1 
ATOM   2046 N  NE  . ARG   A 1 293 ? -3.046  17.620  71.611  1.00 33.21  ? 321 ARG   A NE  1 
ATOM   2047 C  CZ  . ARG   A 1 293 ? -1.779  17.847  71.950  1.00 40.53  ? 321 ARG   A CZ  1 
ATOM   2048 N  NH1 . ARG   A 1 293 ? -1.418  17.831  73.234  1.00 39.37  ? 321 ARG   A NH1 1 
ATOM   2049 N  NH2 . ARG   A 1 293 ? -0.872  18.089  71.008  1.00 37.10  ? 321 ARG   A NH2 1 
ATOM   2050 N  N   . GLU   A 1 294 ? -4.669  12.704  69.624  1.00 30.35  ? 322 GLU   A N   1 
ATOM   2051 C  CA  . GLU   A 1 294 ? -5.086  12.297  68.295  1.00 30.79  ? 322 GLU   A CA  1 
ATOM   2052 C  C   . GLU   A 1 294 ? -5.838  10.967  68.333  1.00 34.01  ? 322 GLU   A C   1 
ATOM   2053 O  O   . GLU   A 1 294 ? -6.852  10.807  67.650  1.00 28.94  ? 322 GLU   A O   1 
ATOM   2054 C  CB  . GLU   A 1 294 ? -3.873  12.233  67.369  1.00 28.65  ? 322 GLU   A CB  1 
ATOM   2055 C  CG  . GLU   A 1 294 ? -3.364  13.609  66.915  1.00 34.56  ? 322 GLU   A CG  1 
ATOM   2056 C  CD  . GLU   A 1 294 ? -4.253  14.198  65.825  1.00 41.71  ? 322 GLU   A CD  1 
ATOM   2057 O  OE1 . GLU   A 1 294 ? -5.473  14.291  66.034  1.00 45.30  ? 322 GLU   A OE1 1 
ATOM   2058 O  OE2 . GLU   A 1 294 ? -3.754  14.536  64.739  1.00 48.19  ? 322 GLU   A OE2 1 
ATOM   2059 N  N   . MET   A 1 295 ? -5.387  10.019  69.152  1.00 30.89  ? 323 MET   A N   1 
ATOM   2060 C  CA  . MET   A 1 295 ? -6.079  8.733   69.219  1.00 35.82  ? 323 MET   A CA  1 
ATOM   2061 C  C   . MET   A 1 295 ? -7.433  8.873   69.901  1.00 33.75  ? 323 MET   A C   1 
ATOM   2062 O  O   . MET   A 1 295 ? -8.401  8.201   69.514  1.00 27.06  ? 323 MET   A O   1 
ATOM   2063 C  CB  . MET   A 1 295 ? -5.228  7.690   69.955  1.00 24.88  ? 323 MET   A CB  1 
ATOM   2064 C  CG  . MET   A 1 295 ? -3.957  7.243   69.217  1.00 27.54  ? 323 MET   A CG  1 
ATOM   2065 S  SD  . MET   A 1 295 ? -3.111  5.890   70.104  1.00 26.78  ? 323 MET   A SD  1 
ATOM   2066 C  CE  . MET   A 1 295 ? -4.357  4.595   69.926  1.00 24.05  ? 323 MET   A CE  1 
ATOM   2067 N  N   . ARG   A 1 296 ? -7.507  9.705   70.947  1.00 32.51  ? 324 ARG   A N   1 
ATOM   2068 C  CA  . ARG   A 1 296 ? -8.766  9.867   71.667  1.00 34.36  ? 324 ARG   A CA  1 
ATOM   2069 C  C   . ARG   A 1 296 ? -9.790  10.610  70.818  1.00 35.47  ? 324 ARG   A C   1 
ATOM   2070 O  O   . ARG   A 1 296 ? -10.987 10.299  70.876  1.00 32.02  ? 324 ARG   A O   1 
ATOM   2071 C  CB  . ARG   A 1 296 ? -8.545  10.599  72.990  1.00 33.04  ? 324 ARG   A CB  1 
ATOM   2072 C  CG  . ARG   A 1 296 ? -8.024  9.737   74.125  1.00 32.31  ? 324 ARG   A CG  1 
ATOM   2073 C  CD  . ARG   A 1 296 ? -8.117  10.489  75.447  1.00 38.83  ? 324 ARG   A CD  1 
ATOM   2074 N  NE  . ARG   A 1 296 ? -7.571  9.735   76.575  1.00 43.58  ? 324 ARG   A NE  1 
ATOM   2075 C  CZ  . ARG   A 1 296 ? -8.246  8.821   77.265  1.00 39.90  ? 324 ARG   A CZ  1 
ATOM   2076 N  NH1 . ARG   A 1 296 ? -9.497  8.537   76.945  1.00 36.09  ? 324 ARG   A NH1 1 
ATOM   2077 N  NH2 . ARG   A 1 296 ? -7.666  8.185   78.276  1.00 42.94  ? 324 ARG   A NH2 1 
ATOM   2078 N  N   . LYS   A 1 297 ? -9.341  11.573  70.003  1.00 29.15  ? 325 LYS   A N   1 
ATOM   2079 C  CA  . LYS   A 1 297 ? -10.267 12.182  69.048  1.00 32.95  ? 325 LYS   A CA  1 
ATOM   2080 C  C   . LYS   A 1 297 ? -10.941 11.125  68.196  1.00 33.59  ? 325 LYS   A C   1 
ATOM   2081 O  O   . LYS   A 1 297 ? -12.054 11.332  67.710  1.00 33.53  ? 325 LYS   A O   1 
ATOM   2082 C  CB  . LYS   A 1 297 ? -9.552  13.176  68.126  1.00 32.34  ? 325 LYS   A CB  1 
ATOM   2083 C  CG  . LYS   A 1 297 ? -9.029  14.422  68.819  1.00 35.73  ? 325 LYS   A CG  1 
ATOM   2084 C  CD  . LYS   A 1 297 ? -9.038  15.639  67.913  1.00 34.68  ? 325 LYS   A CD  1 
ATOM   2085 C  CE  . LYS   A 1 297 ? -7.681  15.924  67.331  1.00 37.47  ? 325 LYS   A CE  1 
ATOM   2086 N  NZ  . LYS   A 1 297 ? -7.359  17.375  67.356  1.00 47.55  ? 325 LYS   A NZ  1 
ATOM   2087 N  N   . ARG   A 1 298 ? -10.301 9.975   68.011  1.00 33.23  ? 326 ARG   A N   1 
ATOM   2088 C  CA  . ARG   A 1 298 ? -10.811 8.999   67.067  1.00 28.18  ? 326 ARG   A CA  1 
ATOM   2089 C  C   . ARG   A 1 298 ? -11.409 7.775   67.728  1.00 28.62  ? 326 ARG   A C   1 
ATOM   2090 O  O   . ARG   A 1 298 ? -11.911 6.899   67.016  1.00 27.12  ? 326 ARG   A O   1 
ATOM   2091 C  CB  . ARG   A 1 298 ? -9.703  8.609   66.089  1.00 33.02  ? 326 ARG   A CB  1 
ATOM   2092 C  CG  . ARG   A 1 298 ? -9.198  9.831   65.304  1.00 31.51  ? 326 ARG   A CG  1 
ATOM   2093 C  CD  . ARG   A 1 298 ? -7.960  9.469   64.568  1.00 30.21  ? 326 ARG   A CD  1 
ATOM   2094 N  NE  . ARG   A 1 298 ? -7.557  10.422  63.535  1.00 31.64  ? 326 ARG   A NE  1 
ATOM   2095 C  CZ  . ARG   A 1 298 ? -6.950  11.582  63.778  1.00 34.07  ? 326 ARG   A CZ  1 
ATOM   2096 N  NH1 . ARG   A 1 298 ? -6.752  11.989  65.026  1.00 31.35  ? 326 ARG   A NH1 1 
ATOM   2097 N  NH2 . ARG   A 1 298 ? -6.571  12.351  62.767  1.00 32.71  ? 326 ARG   A NH2 1 
ATOM   2098 N  N   . SER   A 1 299 ? -11.464 7.746   69.065  1.00 30.15  ? 327 SER   A N   1 
ATOM   2099 C  CA  . SER   A 1 299 ? -11.870 6.546   69.794  1.00 30.85  ? 327 SER   A CA  1 
ATOM   2100 C  C   . SER   A 1 299 ? -13.244 6.060   69.364  1.00 36.49  ? 327 SER   A C   1 
ATOM   2101 O  O   . SER   A 1 299 ? -13.486 4.848   69.262  1.00 32.19  ? 327 SER   A O   1 
ATOM   2102 C  CB  . SER   A 1 299 ? -11.874 6.822   71.297  1.00 32.23  ? 327 SER   A CB  1 
ATOM   2103 O  OG  . SER   A 1 299 ? -10.573 7.129   71.775  1.00 38.79  ? 327 SER   A OG  1 
ATOM   2104 N  N   . SER   A 1 300 ? -14.160 6.989   69.124  1.00 34.00  ? 328 SER   A N   1 
ATOM   2105 C  CA  . SER   A 1 300 ? -15.549 6.681   68.860  1.00 31.49  ? 328 SER   A CA  1 
ATOM   2106 C  C   . SER   A 1 300 ? -15.893 6.746   67.382  1.00 33.08  ? 328 SER   A C   1 
ATOM   2107 O  O   . SER   A 1 300 ? -17.063 6.566   67.022  1.00 36.87  ? 328 SER   A O   1 
ATOM   2108 C  CB  . SER   A 1 300 ? -16.433 7.649   69.638  1.00 40.77  ? 328 SER   A CB  1 
ATOM   2109 O  OG  . SER   A 1 300 ? -16.100 8.984   69.282  1.00 49.25  ? 328 SER   A OG  1 
ATOM   2110 N  N   . ILE   A 1 301 ? -14.914 7.021   66.524  1.00 29.72  ? 329 ILE   A N   1 
ATOM   2111 C  CA  . ILE   A 1 301 ? -15.148 7.076   65.085  1.00 28.25  ? 329 ILE   A CA  1 
ATOM   2112 C  C   . ILE   A 1 301 ? -14.174 6.141   64.380  1.00 25.82  ? 329 ILE   A C   1 
ATOM   2113 O  O   . ILE   A 1 301 ? -13.561 6.508   63.373  1.00 23.74  ? 329 ILE   A O   1 
ATOM   2114 C  CB  . ILE   A 1 301 ? -15.023 8.514   64.539  1.00 28.75  ? 329 ILE   A CB  1 
ATOM   2115 C  CG1 . ILE   A 1 301 ? -13.690 9.138   64.959  1.00 25.56  ? 329 ILE   A CG1 1 
ATOM   2116 C  CG2 . ILE   A 1 301 ? -16.223 9.386   64.990  1.00 26.71  ? 329 ILE   A CG2 1 
ATOM   2117 C  CD1 . ILE   A 1 301 ? -13.407 10.480  64.274  1.00 30.91  ? 329 ILE   A CD1 1 
ATOM   2118 N  N   . GLY   A 1 302 ? -14.035 4.918   64.888  1.00 25.83  ? 330 GLY   A N   1 
ATOM   2119 C  CA  . GLY   A 1 302 ? -13.275 3.885   64.213  1.00 25.74  ? 330 GLY   A CA  1 
ATOM   2120 C  C   . GLY   A 1 302 ? -11.961 3.544   64.878  1.00 26.92  ? 330 GLY   A C   1 
ATOM   2121 O  O   . GLY   A 1 302 ? -11.370 2.485   64.572  1.00 25.88  ? 330 GLY   A O   1 
ATOM   2122 N  N   . GLY   A 1 303 ? -11.491 4.390   65.784  1.00 29.33  ? 331 GLY   A N   1 
ATOM   2123 C  CA  . GLY   A 1 303 ? -10.176 4.184   66.375  1.00 29.29  ? 331 GLY   A CA  1 
ATOM   2124 C  C   . GLY   A 1 303 ? -10.182 3.213   67.539  1.00 31.54  ? 331 GLY   A C   1 
ATOM   2125 O  O   . GLY   A 1 303 ? -10.919 2.211   67.547  1.00 28.05  ? 331 GLY   A O   1 
ATOM   2126 N  N   . PHE   A 1 304 ? -9.381  3.521   68.552  1.00 28.65  ? 332 PHE   A N   1 
ATOM   2127 C  CA  . PHE   A 1 304 ? -9.236  2.659   69.710  1.00 29.64  ? 332 PHE   A CA  1 
ATOM   2128 C  C   . PHE   A 1 304 ? -9.757  3.352   70.961  1.00 31.73  ? 332 PHE   A C   1 
ATOM   2129 O  O   . PHE   A 1 304 ? -9.673  4.576   71.102  1.00 31.17  ? 332 PHE   A O   1 
ATOM   2130 C  CB  . PHE   A 1 304 ? -7.775  2.246   69.889  1.00 24.59  ? 332 PHE   A CB  1 
ATOM   2131 C  CG  . PHE   A 1 304 ? -7.268  1.357   68.782  1.00 28.06  ? 332 PHE   A CG  1 
ATOM   2132 C  CD1 . PHE   A 1 304 ? -7.500  -0.013  68.807  1.00 29.05  ? 332 PHE   A CD1 1 
ATOM   2133 C  CD2 . PHE   A 1 304 ? -6.591  1.893   67.696  1.00 26.68  ? 332 PHE   A CD2 1 
ATOM   2134 C  CE1 . PHE   A 1 304 ? -7.057  -0.825  67.764  1.00 26.22  ? 332 PHE   A CE1 1 
ATOM   2135 C  CE2 . PHE   A 1 304 ? -6.129  1.087   66.666  1.00 22.67  ? 332 PHE   A CE2 1 
ATOM   2136 C  CZ  . PHE   A 1 304 ? -6.363  -0.264  66.692  1.00 24.22  ? 332 PHE   A CZ  1 
ATOM   2137 N  N   . ASP   A 1 305 ? -10.305 2.550   71.859  1.00 28.33  ? 333 ASP   A N   1 
ATOM   2138 C  CA  . ASP   A 1 305 ? -10.738 3.001   73.163  1.00 23.71  ? 333 ASP   A CA  1 
ATOM   2139 C  C   . ASP   A 1 305 ? -9.599  2.839   74.153  1.00 34.61  ? 333 ASP   A C   1 
ATOM   2140 O  O   . ASP   A 1 305 ? -8.722  1.982   73.985  1.00 33.29  ? 333 ASP   A O   1 
ATOM   2141 C  CB  . ASP   A 1 305 ? -11.953 2.200   73.625  1.00 29.63  ? 333 ASP   A CB  1 
ATOM   2142 C  CG  . ASP   A 1 305 ? -13.135 2.377   72.706  1.00 30.07  ? 333 ASP   A CG  1 
ATOM   2143 O  OD1 . ASP   A 1 305 ? -13.114 3.331   71.907  1.00 33.74  ? 333 ASP   A OD1 1 
ATOM   2144 O  OD2 . ASP   A 1 305 ? -14.088 1.586   72.776  1.00 32.64  ? 333 ASP   A OD2 1 
ATOM   2145 N  N   . PHE   A 1 306 ? -9.615  3.670   75.188  1.00 31.02  ? 334 PHE   A N   1 
ATOM   2146 C  CA  . PHE   A 1 306 ? -8.594  3.646   76.221  1.00 38.09  ? 334 PHE   A CA  1 
ATOM   2147 C  C   . PHE   A 1 306 ? -9.202  3.147   77.518  1.00 35.91  ? 334 PHE   A C   1 
ATOM   2148 O  O   . PHE   A 1 306 ? -10.419 3.226   77.714  1.00 32.77  ? 334 PHE   A O   1 
ATOM   2149 C  CB  . PHE   A 1 306 ? -7.959  5.035   76.399  1.00 34.13  ? 334 PHE   A CB  1 
ATOM   2150 C  CG  . PHE   A 1 306 ? -7.053  5.394   75.273  1.00 35.08  ? 334 PHE   A CG  1 
ATOM   2151 C  CD1 . PHE   A 1 306 ? -5.744  4.944   75.261  1.00 30.88  ? 334 PHE   A CD1 1 
ATOM   2152 C  CD2 . PHE   A 1 306 ? -7.532  6.086   74.177  1.00 34.12  ? 334 PHE   A CD2 1 
ATOM   2153 C  CE1 . PHE   A 1 306 ? -4.923  5.220   74.211  1.00 28.54  ? 334 PHE   A CE1 1 
ATOM   2154 C  CE2 . PHE   A 1 306 ? -6.707  6.375   73.118  1.00 30.49  ? 334 PHE   A CE2 1 
ATOM   2155 C  CZ  . PHE   A 1 306 ? -5.401  5.943   73.139  1.00 32.34  ? 334 PHE   A CZ  1 
ATOM   2156 N  N   . MET   A 1 307 ? -8.342  2.609   78.393  1.00 34.78  ? 335 MET   A N   1 
ATOM   2157 C  CA  . MET   A 1 307 ? -8.774  2.120   79.701  1.00 42.65  ? 335 MET   A CA  1 
ATOM   2158 C  C   . MET   A 1 307 ? -9.497  3.239   80.443  1.00 44.86  ? 335 MET   A C   1 
ATOM   2159 O  O   . MET   A 1 307 ? -9.378  4.411   80.059  1.00 45.35  ? 335 MET   A O   1 
ATOM   2160 C  CB  . MET   A 1 307 ? -7.573  1.627   80.520  1.00 43.90  ? 335 MET   A CB  1 
ATOM   2161 C  CG  . MET   A 1 307 ? -6.967  2.727   81.414  1.00 45.64  ? 335 MET   A CG  1 
ATOM   2162 S  SD  . MET   A 1 307 ? -5.421  2.277   82.247  1.00 51.23  ? 335 MET   A SD  1 
ATOM   2163 C  CE  . MET   A 1 307 ? -4.302  3.139   81.179  1.00 39.22  ? 335 MET   A CE  1 
ATOM   2164 N  N   . PRO   A 1 308 ? -10.276 2.938   81.478  1.00 48.95  ? 336 PRO   A N   1 
ATOM   2165 C  CA  . PRO   A 1 308 ? -10.912 4.027   82.235  1.00 51.13  ? 336 PRO   A CA  1 
ATOM   2166 C  C   . PRO   A 1 308 ? -9.857  4.915   82.893  1.00 58.50  ? 336 PRO   A C   1 
ATOM   2167 O  O   . PRO   A 1 308 ? -8.801  4.440   83.323  1.00 53.58  ? 336 PRO   A O   1 
ATOM   2168 C  CB  . PRO   A 1 308 ? -11.774 3.285   83.264  1.00 47.49  ? 336 PRO   A CB  1 
ATOM   2169 C  CG  . PRO   A 1 308 ? -12.036 1.938   82.623  1.00 49.50  ? 336 PRO   A CG  1 
ATOM   2170 C  CD  . PRO   A 1 308 ? -10.756 1.610   81.906  1.00 42.92  ? 336 PRO   A CD  1 
ATOM   2171 N  N   . SER   A 1 309 ? -10.130 6.224   82.932  1.00 55.30  ? 337 SER   A N   1 
ATOM   2172 C  CA  . SER   A 1 309 ? -9.155  7.155   83.496  1.00 60.33  ? 337 SER   A CA  1 
ATOM   2173 C  C   . SER   A 1 309 ? -9.064  6.976   85.011  1.00 57.95  ? 337 SER   A C   1 
ATOM   2174 O  O   . SER   A 1 309 ? -10.084 6.771   85.678  1.00 58.21  ? 337 SER   A O   1 
ATOM   2175 C  CB  . SER   A 1 309 ? -9.514  8.610   83.166  1.00 64.47  ? 337 SER   A CB  1 
ATOM   2176 O  OG  . SER   A 1 309 ? -8.846  9.070   81.998  1.00 54.39  ? 337 SER   A OG  1 
ATOM   2177 N  N   . PRO   A 1 310 ? -7.867  7.056   85.584  1.00 59.39  ? 338 PRO   A N   1 
ATOM   2178 C  CA  . PRO   A 1 310 ? -7.732  6.937   87.040  1.00 63.17  ? 338 PRO   A CA  1 
ATOM   2179 C  C   . PRO   A 1 310 ? -8.384  8.120   87.732  1.00 67.42  ? 338 PRO   A C   1 
ATOM   2180 O  O   . PRO   A 1 310 ? -8.583  9.177   87.112  1.00 65.77  ? 338 PRO   A O   1 
ATOM   2181 C  CB  . PRO   A 1 310 ? -6.214  6.918   87.256  1.00 55.69  ? 338 PRO   A CB  1 
ATOM   2182 C  CG  . PRO   A 1 310 ? -5.658  7.601   86.068  1.00 60.09  ? 338 PRO   A CG  1 
ATOM   2183 C  CD  . PRO   A 1 310 ? -6.581  7.330   84.922  1.00 56.61  ? 338 PRO   A CD  1 
ATOM   2184 N  N   . PRO   A 1 311 ? -8.764  7.977   89.000  1.00 68.22  ? 339 PRO   A N   1 
ATOM   2185 C  CA  . PRO   A 1 311 ? -9.471  9.062   89.690  1.00 67.55  ? 339 PRO   A CA  1 
ATOM   2186 C  C   . PRO   A 1 311 ? -8.562  10.264  89.871  1.00 67.02  ? 339 PRO   A C   1 
ATOM   2187 O  O   . PRO   A 1 311 ? -7.333  10.146  89.740  1.00 64.07  ? 339 PRO   A O   1 
ATOM   2188 C  CB  . PRO   A 1 311 ? -9.856  8.433   91.038  1.00 68.59  ? 339 PRO   A CB  1 
ATOM   2189 C  CG  . PRO   A 1 311 ? -8.885  7.322   91.228  1.00 66.57  ? 339 PRO   A CG  1 
ATOM   2190 C  CD  . PRO   A 1 311 ? -8.583  6.795   89.862  1.00 65.44  ? 339 PRO   A CD  1 
ATOM   2191 N  N   . PRO   A 1 312 ? -9.126  11.446  90.142  1.00 69.77  ? 340 PRO   A N   1 
ATOM   2192 C  CA  . PRO   A 1 312 ? -8.278  12.636  90.352  1.00 67.69  ? 340 PRO   A CA  1 
ATOM   2193 C  C   . PRO   A 1 312 ? -7.283  12.483  91.491  1.00 66.89  ? 340 PRO   A C   1 
ATOM   2194 O  O   . PRO   A 1 312 ? -6.279  13.212  91.523  1.00 64.60  ? 340 PRO   A O   1 
ATOM   2195 C  CB  . PRO   A 1 312 ? -9.298  13.745  90.645  1.00 67.39  ? 340 PRO   A CB  1 
ATOM   2196 C  CG  . PRO   A 1 312 ? -10.545 13.010  91.064  1.00 68.47  ? 340 PRO   A CG  1 
ATOM   2197 C  CD  . PRO   A 1 312 ? -10.558 11.771  90.244  1.00 64.70  ? 340 PRO   A CD  1 
ATOM   2198 N  N   . THR   A 1 313 ? -7.539  11.569  92.430  1.00 67.78  ? 341 THR   A N   1 
ATOM   2199 C  CA  . THR   A 1 313 ? -6.560  11.271  93.468  1.00 66.68  ? 341 THR   A CA  1 
ATOM   2200 C  C   . THR   A 1 313 ? -5.214  10.901  92.868  1.00 64.69  ? 341 THR   A C   1 
ATOM   2201 O  O   . THR   A 1 313 ? -4.170  11.361  93.342  1.00 66.79  ? 341 THR   A O   1 
ATOM   2202 C  CB  . THR   A 1 313 ? -7.073  10.139  94.356  1.00 71.63  ? 341 THR   A CB  1 
ATOM   2203 O  OG1 . THR   A 1 313 ? -7.472  9.035   93.535  1.00 70.14  ? 341 THR   A OG1 1 
ATOM   2204 C  CG2 . THR   A 1 313 ? -8.268  10.611  95.152  1.00 73.46  ? 341 THR   A CG2 1 
ATOM   2205 N  N   . TYR   A 1 314 ? -5.215  10.071  91.820  1.00 65.96  ? 342 TYR   A N   1 
ATOM   2206 C  CA  . TYR   A 1 314 ? -3.952  9.671   91.204  1.00 63.96  ? 342 TYR   A CA  1 
ATOM   2207 C  C   . TYR   A 1 314 ? -3.181  10.878  90.695  1.00 63.62  ? 342 TYR   A C   1 
ATOM   2208 O  O   . TYR   A 1 314 ? -1.943  10.869  90.685  1.00 65.43  ? 342 TYR   A O   1 
ATOM   2209 C  CB  . TYR   A 1 314 ? -4.204  8.676   90.065  1.00 60.85  ? 342 TYR   A CB  1 
ATOM   2210 C  CG  . TYR   A 1 314 ? -2.948  8.219   89.334  1.00 54.93  ? 342 TYR   A CG  1 
ATOM   2211 C  CD1 . TYR   A 1 314 ? -2.226  7.114   89.763  1.00 52.18  ? 342 TYR   A CD1 1 
ATOM   2212 C  CD2 . TYR   A 1 314 ? -2.489  8.902   88.211  1.00 58.14  ? 342 TYR   A CD2 1 
ATOM   2213 C  CE1 . TYR   A 1 314 ? -1.083  6.702   89.094  1.00 49.50  ? 342 TYR   A CE1 1 
ATOM   2214 C  CE2 . TYR   A 1 314 ? -1.345  8.507   87.543  1.00 50.13  ? 342 TYR   A CE2 1 
ATOM   2215 C  CZ  . TYR   A 1 314 ? -0.650  7.406   87.982  1.00 51.75  ? 342 TYR   A CZ  1 
ATOM   2216 O  OH  . TYR   A 1 314 ? 0.483   7.017   87.297  1.00 52.96  ? 342 TYR   A OH  1 
ATOM   2217 N  N   . TYR   A 1 315 ? -3.887  11.932  90.292  1.00 64.20  ? 343 TYR   A N   1 
ATOM   2218 C  CA  . TYR   A 1 315 ? -3.216  13.113  89.764  1.00 65.34  ? 343 TYR   A CA  1 
ATOM   2219 C  C   . TYR   A 1 315 ? -2.875  14.133  90.837  1.00 64.57  ? 343 TYR   A C   1 
ATOM   2220 O  O   . TYR   A 1 315 ? -1.856  14.826  90.714  1.00 66.22  ? 343 TYR   A O   1 
ATOM   2221 C  CB  . TYR   A 1 315 ? -4.058  13.747  88.654  1.00 63.15  ? 343 TYR   A CB  1 
ATOM   2222 C  CG  . TYR   A 1 315 ? -4.094  12.833  87.462  1.00 63.88  ? 343 TYR   A CG  1 
ATOM   2223 C  CD1 . TYR   A 1 315 ? -3.157  12.968  86.442  1.00 61.22  ? 343 TYR   A CD1 1 
ATOM   2224 C  CD2 . TYR   A 1 315 ? -5.050  11.831  87.345  1.00 61.34  ? 343 TYR   A CD2 1 
ATOM   2225 C  CE1 . TYR   A 1 315 ? -3.145  12.110  85.351  1.00 58.75  ? 343 TYR   A CE1 1 
ATOM   2226 C  CE2 . TYR   A 1 315 ? -5.064  10.978  86.247  1.00 59.22  ? 343 TYR   A CE2 1 
ATOM   2227 C  CZ  . TYR   A 1 315 ? -4.110  11.130  85.251  1.00 56.45  ? 343 TYR   A CZ  1 
ATOM   2228 O  OH  . TYR   A 1 315 ? -4.108  10.298  84.157  1.00 56.33  ? 343 TYR   A OH  1 
ATOM   2229 N  N   . GLN   A 1 316 ? -3.696  14.243  91.883  1.00 64.21  ? 344 GLN   A N   1 
ATOM   2230 C  CA  . GLN   A 1 316 ? -3.282  15.012  93.050  1.00 64.31  ? 344 GLN   A CA  1 
ATOM   2231 C  C   . GLN   A 1 316 ? -1.961  14.483  93.597  1.00 65.85  ? 344 GLN   A C   1 
ATOM   2232 O  O   . GLN   A 1 316 ? -1.050  15.260  93.914  1.00 64.65  ? 344 GLN   A O   1 
ATOM   2233 C  CB  . GLN   A 1 316 ? -4.371  14.973  94.122  1.00 64.89  ? 344 GLN   A CB  1 
ATOM   2234 N  N   . ASN   A 1 317 ? -1.826  13.153  93.683  1.00 59.43  ? 345 ASN   A N   1 
ATOM   2235 C  CA  . ASN   A 1 317 ? -0.607  12.537  94.192  1.00 57.03  ? 345 ASN   A CA  1 
ATOM   2236 C  C   . ASN   A 1 317 ? 0.549   12.616  93.207  1.00 60.69  ? 345 ASN   A C   1 
ATOM   2237 O  O   . ASN   A 1 317 ? 1.682   12.296  93.582  1.00 55.82  ? 345 ASN   A O   1 
ATOM   2238 C  CB  . ASN   A 1 317 ? -0.854  11.073  94.555  1.00 56.78  ? 345 ASN   A CB  1 
ATOM   2239 C  CG  . ASN   A 1 317 ? -2.047  10.894  95.467  1.00 62.91  ? 345 ASN   A CG  1 
ATOM   2240 O  OD1 . ASN   A 1 317 ? -2.544  11.856  96.050  1.00 70.43  ? 345 ASN   A OD1 1 
ATOM   2241 N  ND2 . ASN   A 1 317 ? -2.518  9.661   95.593  1.00 64.74  ? 345 ASN   A ND2 1 
ATOM   2242 N  N   . LEU   A 1 318 ? 0.300   13.036  91.966  1.00 61.77  ? 346 LEU   A N   1 
ATOM   2243 C  CA  . LEU   A 1 318 ? 1.371   13.029  90.976  1.00 60.94  ? 346 LEU   A CA  1 
ATOM   2244 C  C   . LEU   A 1 318 ? 2.453   14.038  91.316  1.00 56.24  ? 346 LEU   A C   1 
ATOM   2245 O  O   . LEU   A 1 318 ? 3.639   13.772  91.093  1.00 61.73  ? 346 LEU   A O   1 
ATOM   2246 C  CB  . LEU   A 1 318 ? 0.813   13.310  89.584  1.00 61.40  ? 346 LEU   A CB  1 
ATOM   2247 C  CG  . LEU   A 1 318 ? 0.603   12.091  88.687  1.00 61.71  ? 346 LEU   A CG  1 
ATOM   2248 C  CD1 . LEU   A 1 318 ? 0.084   12.546  87.344  1.00 56.99  ? 346 LEU   A CD1 1 
ATOM   2249 C  CD2 . LEU   A 1 318 ? 1.896   11.275  88.536  1.00 56.71  ? 346 LEU   A CD2 1 
ATOM   2250 N  N   . LYS   A 1 319 ? 2.062   15.206  91.842  1.00 58.50  ? 347 LYS   A N   1 
ATOM   2251 C  CA  . LYS   A 1 319 ? 3.029   16.270  92.104  1.00 62.33  ? 347 LYS   A CA  1 
ATOM   2252 C  C   . LYS   A 1 319 ? 4.147   15.788  93.020  1.00 58.89  ? 347 LYS   A C   1 
ATOM   2253 O  O   . LYS   A 1 319 ? 5.326   16.016  92.736  1.00 54.38  ? 347 LYS   A O   1 
ATOM   2254 C  CB  . LYS   A 1 319 ? 2.328   17.492  92.706  1.00 60.14  ? 347 LYS   A CB  1 
ATOM   2255 N  N   . LYS   A 1 320 ? 3.797   15.074  94.097  1.00 60.88  ? 348 LYS   A N   1 
ATOM   2256 C  CA  . LYS   A 1 320 ? 4.781   14.666  95.096  1.00 55.70  ? 348 LYS   A CA  1 
ATOM   2257 C  C   . LYS   A 1 320 ? 5.767   13.619  94.582  1.00 60.59  ? 348 LYS   A C   1 
ATOM   2258 O  O   . LYS   A 1 320 ? 6.797   13.404  95.230  1.00 56.97  ? 348 LYS   A O   1 
ATOM   2259 C  CB  . LYS   A 1 320 ? 4.074   14.129  96.343  1.00 56.92  ? 348 LYS   A CB  1 
ATOM   2260 N  N   . ARG   A 1 321 ? 5.492   12.951  93.455  1.00 59.46  ? 349 ARG   A N   1 
ATOM   2261 C  CA  . ARG   A 1 321 ? 6.438   11.956  92.959  1.00 59.39  ? 349 ARG   A CA  1 
ATOM   2262 C  C   . ARG   A 1 321 ? 7.125   12.335  91.650  1.00 58.12  ? 349 ARG   A C   1 
ATOM   2263 O  O   . ARG   A 1 321 ? 8.301   11.994  91.474  1.00 56.74  ? 349 ARG   A O   1 
ATOM   2264 C  CB  . ARG   A 1 321 ? 5.764   10.583  92.813  1.00 58.42  ? 349 ARG   A CB  1 
ATOM   2265 C  CG  . ARG   A 1 321 ? 4.271   10.600  92.664  1.00 56.76  ? 349 ARG   A CG  1 
ATOM   2266 C  CD  . ARG   A 1 321 ? 3.691   9.193   92.764  1.00 62.55  ? 349 ARG   A CD  1 
ATOM   2267 N  NE  . ARG   A 1 321 ? 3.910   8.449   91.573  1.00 64.37  ? 349 ARG   A NE  1 
ATOM   2268 C  CZ  . ARG   A 1 321 ? 3.066   8.339   90.602  1.00 56.63  ? 349 ARG   A CZ  1 
ATOM   2269 N  NH1 . ARG   A 1 321 ? 1.904   8.905   90.665  1.00 59.42  ? 349 ARG   A NH1 1 
ATOM   2270 N  NH2 . ARG   A 1 321 ? 3.392   7.648   89.564  1.00 54.67  ? 349 ARG   A NH2 1 
ATOM   2271 N  N   . VAL   A 1 322 ? 6.455   13.046  90.737  1.00 57.89  ? 350 VAL   A N   1 
ATOM   2272 C  CA  . VAL   A 1 322 ? 7.102   13.477  89.505  1.00 59.30  ? 350 VAL   A CA  1 
ATOM   2273 C  C   . VAL   A 1 322 ? 7.040   14.989  89.308  1.00 58.53  ? 350 VAL   A C   1 
ATOM   2274 O  O   . VAL   A 1 322 ? 7.361   15.482  88.221  1.00 55.35  ? 350 VAL   A O   1 
ATOM   2275 C  CB  . VAL   A 1 322 ? 6.520   12.750  88.280  1.00 57.45  ? 350 VAL   A CB  1 
ATOM   2276 C  CG1 . VAL   A 1 322 ? 6.705   11.244  88.416  1.00 49.20  ? 350 VAL   A CG1 1 
ATOM   2277 C  CG2 . VAL   A 1 322 ? 5.052   13.131  88.084  1.00 57.29  ? 350 VAL   A CG2 1 
ATOM   2278 N  N   . GLY   A 1 323 ? 6.657   15.745  90.340  1.00 56.86  ? 351 GLY   A N   1 
ATOM   2279 C  CA  . GLY   A 1 323 ? 6.635   17.199  90.234  1.00 60.16  ? 351 GLY   A CA  1 
ATOM   2280 C  C   . GLY   A 1 323 ? 7.967   17.828  89.866  1.00 55.38  ? 351 GLY   A C   1 
ATOM   2281 O  O   . GLY   A 1 323 ? 7.991   18.961  89.376  1.00 57.31  ? 351 GLY   A O   1 
ATOM   2282 N  N   . ASP   A 1 324 ? 9.076   17.126  90.093  1.00 54.18  ? 352 ASP   A N   1 
ATOM   2283 C  CA  . ASP   A 1 324 ? 10.373  17.595  89.625  1.00 56.05  ? 352 ASP   A CA  1 
ATOM   2284 C  C   . ASP   A 1 324 ? 10.635  17.257  88.164  1.00 57.88  ? 352 ASP   A C   1 
ATOM   2285 O  O   . ASP   A 1 324 ? 11.704  17.602  87.646  1.00 55.10  ? 352 ASP   A O   1 
ATOM   2286 C  CB  . ASP   A 1 324 ? 11.491  16.999  90.483  1.00 59.16  ? 352 ASP   A CB  1 
ATOM   2287 C  CG  . ASP   A 1 324 ? 11.567  15.489  90.367  1.00 62.66  ? 352 ASP   A CG  1 
ATOM   2288 O  OD1 . ASP   A 1 324 ? 12.662  14.970  90.064  1.00 63.78  ? 352 ASP   A OD1 1 
ATOM   2289 O  OD2 . ASP   A 1 324 ? 10.523  14.822  90.565  1.00 64.52  ? 352 ASP   A OD2 1 
ATOM   2290 N  N   . VAL   A 1 325 ? 9.704   16.575  87.491  1.00 61.70  ? 353 VAL   A N   1 
ATOM   2291 C  CA  . VAL   A 1 325 ? 9.920   16.082  86.139  1.00 58.10  ? 353 VAL   A CA  1 
ATOM   2292 C  C   . VAL   A 1 325 ? 8.950   16.702  85.146  1.00 54.89  ? 353 VAL   A C   1 
ATOM   2293 O  O   . VAL   A 1 325 ? 9.320   16.977  84.000  1.00 59.03  ? 353 VAL   A O   1 
ATOM   2294 C  CB  . VAL   A 1 325 ? 9.844   14.538  86.085  1.00 61.38  ? 353 VAL   A CB  1 
ATOM   2295 C  CG1 . VAL   A 1 325 ? 10.304  14.019  84.723  1.00 53.78  ? 353 VAL   A CG1 1 
ATOM   2296 C  CG2 . VAL   A 1 325 ? 10.700  13.930  87.191  1.00 55.29  ? 353 VAL   A CG2 1 
ATOM   2297 N  N   . LEU   A 1 326 ? 7.717   16.953  85.564  1.00 54.73  ? 354 LEU   A N   1 
ATOM   2298 C  CA  . LEU   A 1 326 ? 6.708   17.543  84.701  1.00 52.98  ? 354 LEU   A CA  1 
ATOM   2299 C  C   . LEU   A 1 326 ? 6.104   18.745  85.409  1.00 56.56  ? 354 LEU   A C   1 
ATOM   2300 O  O   . LEU   A 1 326 ? 5.883   18.716  86.622  1.00 52.03  ? 354 LEU   A O   1 
ATOM   2301 C  CB  . LEU   A 1 326 ? 5.603   16.531  84.339  1.00 55.53  ? 354 LEU   A CB  1 
ATOM   2302 C  CG  . LEU   A 1 326 ? 6.053   15.151  83.837  1.00 52.37  ? 354 LEU   A CG  1 
ATOM   2303 C  CD1 . LEU   A 1 326 ? 5.013   14.059  84.184  1.00 53.29  ? 354 LEU   A CD1 1 
ATOM   2304 C  CD2 . LEU   A 1 326 ? 6.355   15.188  82.336  1.00 51.64  ? 354 LEU   A CD2 1 
ATOM   2305 N  N   . SER   A 1 327 ? 5.834   19.799  84.642  1.00 59.65  ? 355 SER   A N   1 
ATOM   2306 C  CA  . SER   A 1 327 ? 5.195   20.995  85.171  1.00 55.37  ? 355 SER   A CA  1 
ATOM   2307 C  C   . SER   A 1 327 ? 3.797   20.685  85.686  1.00 59.04  ? 355 SER   A C   1 
ATOM   2308 O  O   . SER   A 1 327 ? 3.311   19.559  85.545  1.00 63.50  ? 355 SER   A O   1 
ATOM   2309 C  CB  . SER   A 1 327 ? 5.104   22.062  84.092  1.00 54.60  ? 355 SER   A CB  1 
ATOM   2310 O  OG  . SER   A 1 327 ? 3.848   21.969  83.439  1.00 59.32  ? 355 SER   A OG  1 
ATOM   2311 N  N   . ASP   A 1 328 ? 3.131   21.677  86.270  1.00 58.06  ? 356 ASP   A N   1 
ATOM   2312 C  CA  . ASP   A 1 328 ? 1.734   21.488  86.630  1.00 58.66  ? 356 ASP   A CA  1 
ATOM   2313 C  C   . ASP   A 1 328 ? 0.848   21.440  85.399  1.00 60.13  ? 356 ASP   A C   1 
ATOM   2314 O  O   . ASP   A 1 328 ? -0.177  20.744  85.406  1.00 60.24  ? 356 ASP   A O   1 
ATOM   2315 C  CB  . ASP   A 1 328 ? 1.281   22.587  87.586  1.00 58.68  ? 356 ASP   A CB  1 
ATOM   2316 C  CG  . ASP   A 1 328 ? 1.917   22.445  88.952  1.00 68.18  ? 356 ASP   A CG  1 
ATOM   2317 O  OD1 . ASP   A 1 328 ? 1.506   23.164  89.888  1.00 69.22  ? 356 ASP   A OD1 1 
ATOM   2318 O  OD2 . ASP   A 1 328 ? 2.825   21.592  89.089  1.00 71.23  ? 356 ASP   A OD2 1 
ATOM   2319 N  N   . ASP   A 1 329 ? 1.221   22.156  84.334  1.00 57.89  ? 357 ASP   A N   1 
ATOM   2320 C  CA  . ASP   A 1 329 ? 0.471   22.049  83.086  1.00 59.54  ? 357 ASP   A CA  1 
ATOM   2321 C  C   . ASP   A 1 329 ? 0.677   20.675  82.450  1.00 57.79  ? 357 ASP   A C   1 
ATOM   2322 O  O   . ASP   A 1 329 ? -0.287  20.012  82.048  1.00 56.66  ? 357 ASP   A O   1 
ATOM   2323 C  CB  . ASP   A 1 329 ? 0.880   23.175  82.132  1.00 59.33  ? 357 ASP   A CB  1 
ATOM   2324 N  N   . GLN   A 1 330 ? 1.932   20.220  82.375  1.00 58.20  ? 358 GLN   A N   1 
ATOM   2325 C  CA  . GLN   A 1 330 ? 2.209   18.873  81.884  1.00 58.98  ? 358 GLN   A CA  1 
ATOM   2326 C  C   . GLN   A 1 330 ? 1.470   17.826  82.704  1.00 58.72  ? 358 GLN   A C   1 
ATOM   2327 O  O   . GLN   A 1 330 ? 0.989   16.825  82.160  1.00 61.04  ? 358 GLN   A O   1 
ATOM   2328 C  CB  . GLN   A 1 330 ? 3.711   18.598  81.915  1.00 56.77  ? 358 GLN   A CB  1 
ATOM   2329 C  CG  . GLN   A 1 330 ? 4.527   19.772  81.483  1.00 57.73  ? 358 GLN   A CG  1 
ATOM   2330 C  CD  . GLN   A 1 330 ? 5.355   19.491  80.273  1.00 57.58  ? 358 GLN   A CD  1 
ATOM   2331 O  OE1 . GLN   A 1 330 ? 5.138   18.497  79.586  1.00 61.36  ? 358 GLN   A OE1 1 
ATOM   2332 N  NE2 . GLN   A 1 330 ? 6.323   20.366  79.996  1.00 54.20  ? 358 GLN   A NE2 1 
ATOM   2333 N  N   . ILE   A 1 331 ? 1.372   18.036  84.017  1.00 56.71  ? 359 ILE   A N   1 
ATOM   2334 C  CA  . ILE   A 1 331 ? 0.591   17.125  84.845  1.00 53.52  ? 359 ILE   A CA  1 
ATOM   2335 C  C   . ILE   A 1 331 ? -0.896  17.266  84.537  1.00 53.99  ? 359 ILE   A C   1 
ATOM   2336 O  O   . ILE   A 1 331 ? -1.619  16.265  84.466  1.00 52.61  ? 359 ILE   A O   1 
ATOM   2337 C  CB  . ILE   A 1 331 ? 0.902   17.358  86.336  1.00 54.20  ? 359 ILE   A CB  1 
ATOM   2338 C  CG1 . ILE   A 1 331 ? 2.266   16.753  86.701  1.00 56.20  ? 359 ILE   A CG1 1 
ATOM   2339 C  CG2 . ILE   A 1 331 ? -0.185  16.776  87.220  1.00 53.30  ? 359 ILE   A CG2 1 
ATOM   2340 C  CD1 . ILE   A 1 331 ? 2.635   16.901  88.160  1.00 58.70  ? 359 ILE   A CD1 1 
ATOM   2341 N  N   . LYS   A 1 332 ? -1.375  18.500  84.327  1.00 57.49  ? 360 LYS   A N   1 
ATOM   2342 C  CA  . LYS   A 1 332 ? -2.794  18.702  84.018  1.00 56.36  ? 360 LYS   A CA  1 
ATOM   2343 C  C   . LYS   A 1 332 ? -3.176  18.042  82.695  1.00 55.11  ? 360 LYS   A C   1 
ATOM   2344 O  O   . LYS   A 1 332 ? -4.268  17.475  82.567  1.00 51.83  ? 360 LYS   A O   1 
ATOM   2345 C  CB  . LYS   A 1 332 ? -3.129  20.197  83.977  1.00 54.97  ? 360 LYS   A CB  1 
ATOM   2346 N  N   . GLU   A 1 333 ? -2.288  18.121  81.699  1.00 59.23  ? 361 GLU   A N   1 
ATOM   2347 C  CA  . GLU   A 1 333 ? -2.486  17.410  80.439  1.00 56.44  ? 361 GLU   A CA  1 
ATOM   2348 C  C   . GLU   A 1 333 ? -2.637  15.907  80.677  1.00 56.76  ? 361 GLU   A C   1 
ATOM   2349 O  O   . GLU   A 1 333 ? -3.584  15.282  80.182  1.00 55.45  ? 361 GLU   A O   1 
ATOM   2350 C  CB  . GLU   A 1 333 ? -1.311  17.705  79.505  1.00 54.35  ? 361 GLU   A CB  1 
ATOM   2351 C  CG  . GLU   A 1 333 ? -1.665  18.153  78.102  1.00 48.82  ? 361 GLU   A CG  1 
ATOM   2352 C  CD  . GLU   A 1 333 ? -0.446  18.688  77.369  1.00 58.02  ? 361 GLU   A CD  1 
ATOM   2353 O  OE1 . GLU   A 1 333 ? -0.372  18.546  76.128  1.00 57.93  ? 361 GLU   A OE1 1 
ATOM   2354 O  OE2 . GLU   A 1 333 ? 0.457   19.236  78.047  1.00 62.68  ? 361 GLU   A OE2 1 
ATOM   2355 N  N   . CYS   A 1 334 ? -1.712  15.312  81.446  1.00 51.78  ? 362 CYS   A N   1 
ATOM   2356 C  CA  . CYS   A 1 334 ? -1.855  13.912  81.845  1.00 51.82  ? 362 CYS   A CA  1 
ATOM   2357 C  C   . CYS   A 1 334 ? -3.259  13.606  82.344  1.00 55.21  ? 362 CYS   A C   1 
ATOM   2358 O  O   . CYS   A 1 334 ? -3.828  12.556  82.017  1.00 49.72  ? 362 CYS   A O   1 
ATOM   2359 C  CB  . CYS   A 1 334 ? -0.849  13.550  82.942  1.00 49.08  ? 362 CYS   A CB  1 
ATOM   2360 S  SG  . CYS   A 1 334 ? 0.846   13.466  82.420  1.00 46.23  ? 362 CYS   A SG  1 
ATOM   2361 N  N   . GLU   A 1 335 ? -3.834  14.504  83.150  1.00 55.48  ? 363 GLU   A N   1 
ATOM   2362 C  CA  . GLU   A 1 335 ? -5.148  14.205  83.712  1.00 56.07  ? 363 GLU   A CA  1 
ATOM   2363 C  C   . GLU   A 1 335 ? -6.221  14.249  82.636  1.00 52.92  ? 363 GLU   A C   1 
ATOM   2364 O  O   . GLU   A 1 335 ? -7.148  13.430  82.643  1.00 52.07  ? 363 GLU   A O   1 
ATOM   2365 C  CB  . GLU   A 1 335 ? -5.478  15.168  84.852  1.00 59.14  ? 363 GLU   A CB  1 
ATOM   2366 C  CG  . GLU   A 1 335 ? -6.736  14.776  85.625  1.00 60.02  ? 363 GLU   A CG  1 
ATOM   2367 C  CD  . GLU   A 1 335 ? -7.111  15.796  86.679  1.00 64.85  ? 363 GLU   A CD  1 
ATOM   2368 O  OE1 . GLU   A 1 335 ? -7.644  15.402  87.740  1.00 66.08  ? 363 GLU   A OE1 1 
ATOM   2369 O  OE2 . GLU   A 1 335 ? -6.868  16.996  86.443  1.00 70.31  ? 363 GLU   A OE2 1 
ATOM   2370 N  N   . GLU   A 1 336 ? -6.111  15.196  81.702  1.00 55.23  ? 364 GLU   A N   1 
ATOM   2371 C  CA  . GLU   A 1 336 ? -7.055  15.240  80.590  1.00 55.80  ? 364 GLU   A CA  1 
ATOM   2372 C  C   . GLU   A 1 336 ? -7.058  13.915  79.839  1.00 53.45  ? 364 GLU   A C   1 
ATOM   2373 O  O   . GLU   A 1 336 ? -8.124  13.392  79.483  1.00 54.20  ? 364 GLU   A O   1 
ATOM   2374 C  CB  . GLU   A 1 336 ? -6.699  16.385  79.637  1.00 54.63  ? 364 GLU   A CB  1 
ATOM   2375 C  CG  . GLU   A 1 336 ? -6.787  17.796  80.218  1.00 61.31  ? 364 GLU   A CG  1 
ATOM   2376 C  CD  . GLU   A 1 336 ? -6.023  18.799  79.368  1.00 63.59  ? 364 GLU   A CD  1 
ATOM   2377 O  OE1 . GLU   A 1 336 ? -5.903  18.551  78.150  1.00 67.73  ? 364 GLU   A OE1 1 
ATOM   2378 O  OE2 . GLU   A 1 336 ? -5.527  19.815  79.907  1.00 63.32  ? 364 GLU   A OE2 1 
ATOM   2379 N  N   . LEU   A 1 337 ? -5.874  13.336  79.633  1.00 48.27  ? 365 LEU   A N   1 
ATOM   2380 C  CA  . LEU   A 1 337 ? -5.690  12.217  78.724  1.00 46.39  ? 365 LEU   A CA  1 
ATOM   2381 C  C   . LEU   A 1 337 ? -5.688  10.864  79.418  1.00 47.48  ? 365 LEU   A C   1 
ATOM   2382 O  O   . LEU   A 1 337 ? -5.650  9.839   78.734  1.00 50.11  ? 365 LEU   A O   1 
ATOM   2383 C  CB  . LEU   A 1 337 ? -4.391  12.399  77.939  1.00 44.28  ? 365 LEU   A CB  1 
ATOM   2384 C  CG  . LEU   A 1 337 ? -4.255  13.770  77.276  1.00 40.03  ? 365 LEU   A CG  1 
ATOM   2385 C  CD1 . LEU   A 1 337 ? -2.924  13.865  76.578  1.00 42.02  ? 365 LEU   A CD1 1 
ATOM   2386 C  CD2 . LEU   A 1 337 ? -5.385  14.017  76.286  1.00 43.89  ? 365 LEU   A CD2 1 
ATOM   2387 N  N   . GLY   A 1 338 ? -5.771  10.826  80.745  1.00 46.80  ? 366 GLY   A N   1 
ATOM   2388 C  CA  . GLY   A 1 338 ? -5.706  9.552   81.431  1.00 48.04  ? 366 GLY   A CA  1 
ATOM   2389 C  C   . GLY   A 1 338 ? -4.330  8.929   81.439  1.00 47.72  ? 366 GLY   A C   1 
ATOM   2390 O  O   . GLY   A 1 338 ? -4.196  7.725   81.703  1.00 41.16  ? 366 GLY   A O   1 
ATOM   2391 N  N   . ILE   A 1 339 ? -3.298  9.725   81.153  1.00 45.68  ? 367 ILE   A N   1 
ATOM   2392 C  CA  . ILE   A 1 339 ? -1.935  9.219   81.115  1.00 46.09  ? 367 ILE   A CA  1 
ATOM   2393 C  C   . ILE   A 1 339 ? -1.515  8.791   82.512  1.00 47.60  ? 367 ILE   A C   1 
ATOM   2394 O  O   . ILE   A 1 339 ? -1.925  9.390   83.516  1.00 55.87  ? 367 ILE   A O   1 
ATOM   2395 C  CB  . ILE   A 1 339 ? -0.994  10.286  80.534  1.00 45.69  ? 367 ILE   A CB  1 
ATOM   2396 C  CG1 . ILE   A 1 339 ? -1.348  10.555  79.066  1.00 39.86  ? 367 ILE   A CG1 1 
ATOM   2397 C  CG2 . ILE   A 1 339 ? 0.473   9.883   80.694  1.00 46.82  ? 367 ILE   A CG2 1 
ATOM   2398 C  CD1 . ILE   A 1 339 ? -0.414  11.558  78.367  1.00 44.88  ? 367 ILE   A CD1 1 
ATOM   2399 N  N   . LEU   A 1 340 ? -0.730  7.721   82.581  1.00 42.12  ? 368 LEU   A N   1 
ATOM   2400 C  CA  . LEU   A 1 340 ? -0.141  7.223   83.815  1.00 45.47  ? 368 LEU   A CA  1 
ATOM   2401 C  C   . LEU   A 1 340 ? 1.334   7.590   83.816  1.00 46.48  ? 368 LEU   A C   1 
ATOM   2402 O  O   . LEU   A 1 340 ? 1.975   7.596   82.760  1.00 47.99  ? 368 LEU   A O   1 
ATOM   2403 C  CB  . LEU   A 1 340 ? -0.292  5.699   83.914  1.00 46.61  ? 368 LEU   A CB  1 
ATOM   2404 C  CG  . LEU   A 1 340 ? -1.675  5.035   83.847  1.00 47.86  ? 368 LEU   A CG  1 
ATOM   2405 C  CD1 . LEU   A 1 340 ? -1.521  3.512   83.695  1.00 49.94  ? 368 LEU   A CD1 1 
ATOM   2406 C  CD2 . LEU   A 1 340 ? -2.529  5.378   85.077  1.00 51.95  ? 368 LEU   A CD2 1 
ATOM   2407 N  N   . VAL   A 1 341 ? 1.874   7.902   84.992  1.00 43.84  ? 369 VAL   A N   1 
ATOM   2408 C  CA  . VAL   A 1 341 ? 3.289   8.233   85.128  1.00 44.35  ? 369 VAL   A CA  1 
ATOM   2409 C  C   . VAL   A 1 341 ? 3.887   7.377   86.231  1.00 47.26  ? 369 VAL   A C   1 
ATOM   2410 O  O   . VAL   A 1 341 ? 3.331   7.303   87.333  1.00 49.72  ? 369 VAL   A O   1 
ATOM   2411 C  CB  . VAL   A 1 341 ? 3.529   9.724   85.441  1.00 47.85  ? 369 VAL   A CB  1 
ATOM   2412 C  CG1 . VAL   A 1 341 ? 5.025   10.008  85.455  1.00 41.22  ? 369 VAL   A CG1 1 
ATOM   2413 C  CG2 . VAL   A 1 341 ? 2.817   10.621  84.437  1.00 41.66  ? 369 VAL   A CG2 1 
ATOM   2414 N  N   . ASP   A 1 342 ? 5.017   6.741   85.941  1.00 41.98  ? 370 ASP   A N   1 
ATOM   2415 C  CA  . ASP   A 1 342 ? 5.777   6.025   86.951  1.00 47.56  ? 370 ASP   A CA  1 
ATOM   2416 C  C   . ASP   A 1 342 ? 7.250   6.380   86.813  1.00 46.24  ? 370 ASP   A C   1 
ATOM   2417 O  O   . ASP   A 1 342 ? 7.702   6.905   85.788  1.00 41.40  ? 370 ASP   A O   1 
ATOM   2418 C  CB  . ASP   A 1 342 ? 5.590   4.506   86.852  1.00 47.38  ? 370 ASP   A CB  1 
ATOM   2419 C  CG  . ASP   A 1 342 ? 6.020   3.778   88.126  1.00 52.80  ? 370 ASP   A CG  1 
ATOM   2420 O  OD1 . ASP   A 1 342 ? 5.983   4.399   89.208  1.00 52.17  ? 370 ASP   A OD1 1 
ATOM   2421 O  OD2 . ASP   A 1 342 ? 6.388   2.587   88.047  1.00 49.60  ? 370 ASP   A OD2 1 
ATOM   2422 N  N   . ARG   A 1 343 ? 8.002   6.060   87.858  1.00 47.18  ? 371 ARG   A N   1 
ATOM   2423 C  CA  . ARG   A 1 343 ? 9.398   6.450   87.939  1.00 46.53  ? 371 ARG   A CA  1 
ATOM   2424 C  C   . ARG   A 1 343 ? 10.185  5.374   88.667  1.00 49.30  ? 371 ARG   A C   1 
ATOM   2425 O  O   . ARG   A 1 343 ? 9.769   4.920   89.738  1.00 50.15  ? 371 ARG   A O   1 
ATOM   2426 C  CB  . ARG   A 1 343 ? 9.520   7.784   88.669  1.00 52.91  ? 371 ARG   A CB  1 
ATOM   2427 C  CG  . ARG   A 1 343 ? 10.907  8.342   88.698  1.00 54.38  ? 371 ARG   A CG  1 
ATOM   2428 C  CD  . ARG   A 1 343 ? 10.918  9.600   89.513  1.00 55.46  ? 371 ARG   A CD  1 
ATOM   2429 N  NE  . ARG   A 1 343 ? 12.098  10.402  89.226  1.00 60.84  ? 371 ARG   A NE  1 
ATOM   2430 C  CZ  . ARG   A 1 343 ? 12.173  11.697  89.489  1.00 57.97  ? 371 ARG   A CZ  1 
ATOM   2431 N  NH1 . ARG   A 1 343 ? 11.132  12.311  90.041  1.00 63.63  ? 371 ARG   A NH1 1 
ATOM   2432 N  NH2 . ARG   A 1 343 ? 13.275  12.373  89.195  1.00 63.29  ? 371 ARG   A NH2 1 
ATOM   2433 N  N   . ASP   A 1 344 ? 11.309  4.958   88.079  1.00 49.13  ? 372 ASP   A N   1 
ATOM   2434 C  CA  . ASP   A 1 344 ? 12.258  4.133   88.812  1.00 46.67  ? 372 ASP   A CA  1 
ATOM   2435 C  C   . ASP   A 1 344 ? 13.432  5.008   89.243  1.00 54.96  ? 372 ASP   A C   1 
ATOM   2436 O  O   . ASP   A 1 344 ? 13.255  6.204   89.490  1.00 53.85  ? 372 ASP   A O   1 
ATOM   2437 C  CB  . ASP   A 1 344 ? 12.697  2.906   87.989  1.00 50.63  ? 372 ASP   A CB  1 
ATOM   2438 C  CG  . ASP   A 1 344 ? 13.471  3.253   86.709  1.00 52.84  ? 372 ASP   A CG  1 
ATOM   2439 O  OD1 . ASP   A 1 344 ? 13.724  2.307   85.918  1.00 52.18  ? 372 ASP   A OD1 1 
ATOM   2440 O  OD2 . ASP   A 1 344 ? 13.840  4.425   86.483  1.00 50.07  ? 372 ASP   A OD2 1 
ATOM   2441 N  N   . ASP   A 1 345 ? 14.628  4.432   89.350  1.00 58.19  ? 373 ASP   A N   1 
ATOM   2442 C  CA  . ASP   A 1 345 ? 15.792  5.181   89.805  1.00 60.37  ? 373 ASP   A CA  1 
ATOM   2443 C  C   . ASP   A 1 345 ? 16.563  5.836   88.670  1.00 62.84  ? 373 ASP   A C   1 
ATOM   2444 O  O   . ASP   A 1 345 ? 17.378  6.730   88.929  1.00 61.58  ? 373 ASP   A O   1 
ATOM   2445 C  CB  . ASP   A 1 345 ? 16.738  4.267   90.592  1.00 57.58  ? 373 ASP   A CB  1 
ATOM   2446 C  CG  . ASP   A 1 345 ? 17.055  2.973   89.856  1.00 63.14  ? 373 ASP   A CG  1 
ATOM   2447 O  OD1 . ASP   A 1 345 ? 16.110  2.316   89.354  1.00 60.03  ? 373 ASP   A OD1 1 
ATOM   2448 O  OD2 . ASP   A 1 345 ? 18.255  2.608   89.796  1.00 70.86  ? 373 ASP   A OD2 1 
ATOM   2449 N  N   . GLN   A 1 346 ? 16.325  5.419   87.429  1.00 54.96  ? 374 GLN   A N   1 
ATOM   2450 C  CA  . GLN   A 1 346 ? 17.041  5.964   86.287  1.00 51.07  ? 374 GLN   A CA  1 
ATOM   2451 C  C   . GLN   A 1 346 ? 16.213  6.947   85.475  1.00 56.47  ? 374 GLN   A C   1 
ATOM   2452 O  O   . GLN   A 1 346 ? 16.774  7.921   84.956  1.00 56.85  ? 374 GLN   A O   1 
ATOM   2453 C  CB  . GLN   A 1 346 ? 17.525  4.829   85.377  1.00 56.47  ? 374 GLN   A CB  1 
ATOM   2454 N  N   . GLY   A 1 347 ? 14.898  6.737   85.361  1.00 50.59  ? 375 GLY   A N   1 
ATOM   2455 C  CA  . GLY   A 1 347 ? 14.106  7.600   84.502  1.00 43.06  ? 375 GLY   A CA  1 
ATOM   2456 C  C   . GLY   A 1 347 ? 12.644  7.651   84.888  1.00 44.16  ? 375 GLY   A C   1 
ATOM   2457 O  O   . GLY   A 1 347 ? 12.210  7.062   85.881  1.00 46.65  ? 375 GLY   A O   1 
ATOM   2458 N  N   . THR   A 1 348 ? 11.882  8.377   84.077  1.00 46.32  ? 376 THR   A N   1 
ATOM   2459 C  CA  . THR   A 1 348 ? 10.442  8.529   84.257  1.00 47.98  ? 376 THR   A CA  1 
ATOM   2460 C  C   . THR   A 1 348 ? 9.719   7.926   83.054  1.00 45.13  ? 376 THR   A C   1 
ATOM   2461 O  O   . THR   A 1 348 ? 10.153  8.090   81.905  1.00 41.39  ? 376 THR   A O   1 
ATOM   2462 C  CB  . THR   A 1 348 ? 10.056  10.016  84.432  1.00 46.55  ? 376 THR   A CB  1 
ATOM   2463 O  OG1 . THR   A 1 348 ? 10.544  10.513  85.686  1.00 56.44  ? 376 THR   A OG1 1 
ATOM   2464 C  CG2 . THR   A 1 348 ? 8.554   10.215  84.352  1.00 43.53  ? 376 THR   A CG2 1 
ATOM   2465 N  N   . LEU   A 1 349 ? 8.627   7.216   83.319  1.00 38.78  ? 377 LEU   A N   1 
ATOM   2466 C  CA  . LEU   A 1 349 ? 7.846   6.566   82.275  1.00 40.68  ? 377 LEU   A CA  1 
ATOM   2467 C  C   . LEU   A 1 349 ? 6.442   7.156   82.234  1.00 42.05  ? 377 LEU   A C   1 
ATOM   2468 O  O   . LEU   A 1 349 ? 5.763   7.228   83.265  1.00 42.45  ? 377 LEU   A O   1 
ATOM   2469 C  CB  . LEU   A 1 349 ? 7.788   5.057   82.509  1.00 41.36  ? 377 LEU   A CB  1 
ATOM   2470 C  CG  . LEU   A 1 349 ? 6.598   4.305   81.927  1.00 43.10  ? 377 LEU   A CG  1 
ATOM   2471 C  CD1 . LEU   A 1 349 ? 6.724   4.232   80.413  1.00 38.75  ? 377 LEU   A CD1 1 
ATOM   2472 C  CD2 . LEU   A 1 349 ? 6.536   2.912   82.536  1.00 44.58  ? 377 LEU   A CD2 1 
ATOM   2473 N  N   . LEU   A 1 350 ? 6.017   7.588   81.047  1.00 42.09  ? 378 LEU   A N   1 
ATOM   2474 C  CA  . LEU   A 1 350 ? 4.624   7.946   80.788  1.00 38.14  ? 378 LEU   A CA  1 
ATOM   2475 C  C   . LEU   A 1 350 ? 3.954   6.839   79.969  1.00 37.47  ? 378 LEU   A C   1 
ATOM   2476 O  O   . LEU   A 1 350 ? 4.461   6.452   78.911  1.00 35.63  ? 378 LEU   A O   1 
ATOM   2477 C  CB  . LEU   A 1 350 ? 4.542   9.273   80.039  1.00 41.19  ? 378 LEU   A CB  1 
ATOM   2478 C  CG  . LEU   A 1 350 ? 5.331   10.486  80.530  1.00 44.80  ? 378 LEU   A CG  1 
ATOM   2479 C  CD1 . LEU   A 1 350 ? 6.625   10.622  79.754  1.00 47.23  ? 378 LEU   A CD1 1 
ATOM   2480 C  CD2 . LEU   A 1 350 ? 4.491   11.740  80.343  1.00 50.49  ? 378 LEU   A CD2 1 
ATOM   2481 N  N   . GLN   A 1 351 ? 2.803   6.351   80.431  1.00 36.33  ? 379 GLN   A N   1 
ATOM   2482 C  CA  . GLN   A 1 351 ? 2.186   5.212   79.763  1.00 39.22  ? 379 GLN   A CA  1 
ATOM   2483 C  C   . GLN   A 1 351 ? 0.669   5.298   79.827  1.00 39.36  ? 379 GLN   A C   1 
ATOM   2484 O  O   . GLN   A 1 351 ? 0.099   5.891   80.744  1.00 43.47  ? 379 GLN   A O   1 
ATOM   2485 C  CB  . GLN   A 1 351 ? 2.641   3.893   80.401  1.00 39.07  ? 379 GLN   A CB  1 
ATOM   2486 C  CG  . GLN   A 1 351 ? 2.185   3.798   81.832  1.00 38.26  ? 379 GLN   A CG  1 
ATOM   2487 C  CD  . GLN   A 1 351 ? 2.750   2.613   82.560  1.00 41.54  ? 379 GLN   A CD  1 
ATOM   2488 O  OE1 . GLN   A 1 351 ? 2.604   2.505   83.780  1.00 40.86  ? 379 GLN   A OE1 1 
ATOM   2489 N  NE2 . GLN   A 1 351 ? 3.395   1.709   81.825  1.00 39.49  ? 379 GLN   A NE2 1 
ATOM   2490 N  N   . ILE   A 1 352 ? 0.014   4.649   78.863  1.00 31.92  ? 380 ILE   A N   1 
ATOM   2491 C  CA  . ILE   A 1 352 ? -1.423  4.413   78.921  1.00 35.99  ? 380 ILE   A CA  1 
ATOM   2492 C  C   . ILE   A 1 352 ? -1.755  3.160   78.112  1.00 33.35  ? 380 ILE   A C   1 
ATOM   2493 O  O   . ILE   A 1 352 ? -1.020  2.771   77.202  1.00 35.85  ? 380 ILE   A O   1 
ATOM   2494 C  CB  . ILE   A 1 352 ? -2.213  5.633   78.395  1.00 33.62  ? 380 ILE   A CB  1 
ATOM   2495 C  CG1 . ILE   A 1 352 ? -3.686  5.540   78.801  1.00 30.56  ? 380 ILE   A CG1 1 
ATOM   2496 C  CG2 . ILE   A 1 352 ? -2.056  5.732   76.887  1.00 30.97  ? 380 ILE   A CG2 1 
ATOM   2497 C  CD1 . ILE   A 1 352 ? -4.529  6.750   78.371  1.00 38.01  ? 380 ILE   A CD1 1 
ATOM   2498 N  N   . PHE   A 1 353 ? -2.884  2.531   78.450  1.00 32.89  ? 381 PHE   A N   1 
ATOM   2499 C  CA  . PHE   A 1 353 ? -3.323  1.264   77.873  1.00 36.84  ? 381 PHE   A CA  1 
ATOM   2500 C  C   . PHE   A 1 353 ? -4.633  1.433   77.118  1.00 32.66  ? 381 PHE   A C   1 
ATOM   2501 O  O   . PHE   A 1 353 ? -5.578  2.043   77.626  1.00 37.73  ? 381 PHE   A O   1 
ATOM   2502 C  CB  . PHE   A 1 353 ? -3.534  0.208   78.958  1.00 37.37  ? 381 PHE   A CB  1 
ATOM   2503 C  CG  . PHE   A 1 353 ? -2.303  -0.090  79.743  1.00 37.10  ? 381 PHE   A CG  1 
ATOM   2504 C  CD1 . PHE   A 1 353 ? -2.003  0.636   80.876  1.00 36.43  ? 381 PHE   A CD1 1 
ATOM   2505 C  CD2 . PHE   A 1 353 ? -1.448  -1.108  79.348  1.00 38.00  ? 381 PHE   A CD2 1 
ATOM   2506 C  CE1 . PHE   A 1 353 ? -0.855  0.369   81.602  1.00 41.11  ? 381 PHE   A CE1 1 
ATOM   2507 C  CE2 . PHE   A 1 353 ? -0.306  -1.380  80.064  1.00 40.11  ? 381 PHE   A CE2 1 
ATOM   2508 C  CZ  . PHE   A 1 353 ? -0.009  -0.635  81.192  1.00 39.82  ? 381 PHE   A CZ  1 
ATOM   2509 N  N   . THR   A 1 354 ? -4.700  0.872   75.916  1.00 31.29  ? 382 THR   A N   1 
ATOM   2510 C  CA  . THR   A 1 354 ? -5.984  0.781   75.233  1.00 33.49  ? 382 THR   A CA  1 
ATOM   2511 C  C   . THR   A 1 354 ? -6.852  -0.296  75.868  1.00 32.52  ? 382 THR   A C   1 
ATOM   2512 O  O   . THR   A 1 354 ? -6.373  -1.148  76.621  1.00 31.29  ? 382 THR   A O   1 
ATOM   2513 C  CB  . THR   A 1 354 ? -5.802  0.423   73.771  1.00 31.35  ? 382 THR   A CB  1 
ATOM   2514 O  OG1 . THR   A 1 354 ? -5.354  -0.938  73.704  1.00 30.71  ? 382 THR   A OG1 1 
ATOM   2515 C  CG2 . THR   A 1 354 ? -4.762  1.322   73.124  1.00 29.12  ? 382 THR   A CG2 1 
ATOM   2516 N  N   . LYS   A 1 355 ? -8.148  -0.254  75.540  1.00 33.11  ? 383 LYS   A N   1 
ATOM   2517 C  CA  . LYS   A 1 355 ? -9.012  -1.414  75.686  1.00 33.06  ? 383 LYS   A CA  1 
ATOM   2518 C  C   . LYS   A 1 355 ? -8.607  -2.466  74.650  1.00 34.31  ? 383 LYS   A C   1 
ATOM   2519 O  O   . LYS   A 1 355 ? -7.840  -2.174  73.727  1.00 31.79  ? 383 LYS   A O   1 
ATOM   2520 C  CB  . LYS   A 1 355 ? -10.481 -1.009  75.530  1.00 34.55  ? 383 LYS   A CB  1 
ATOM   2521 C  CG  . LYS   A 1 355 ? -11.000 -0.213  76.730  1.00 40.99  ? 383 LYS   A CG  1 
ATOM   2522 C  CD  . LYS   A 1 355 ? -12.512 -0.062  76.711  1.00 41.86  ? 383 LYS   A CD  1 
ATOM   2523 C  CE  . LYS   A 1 355 ? -13.010 0.526   78.031  1.00 45.83  ? 383 LYS   A CE  1 
ATOM   2524 N  NZ  . LYS   A 1 355 ? -14.250 -0.149  78.527  1.00 53.92  ? 383 LYS   A NZ  1 
ATOM   2525 N  N   . PRO   A 1 356 ? -9.108  -3.704  74.771  1.00 29.86  ? 384 PRO   A N   1 
ATOM   2526 C  CA  . PRO   A 1 356 ? -8.689  -4.758  73.836  1.00 29.53  ? 384 PRO   A CA  1 
ATOM   2527 C  C   . PRO   A 1 356 ? -8.917  -4.367  72.383  1.00 31.00  ? 384 PRO   A C   1 
ATOM   2528 O  O   . PRO   A 1 356 ? -9.875  -3.666  72.048  1.00 32.69  ? 384 PRO   A O   1 
ATOM   2529 C  CB  . PRO   A 1 356 ? -9.558  -5.947  74.245  1.00 34.82  ? 384 PRO   A CB  1 
ATOM   2530 C  CG  . PRO   A 1 356 ? -9.764  -5.733  75.702  1.00 32.56  ? 384 PRO   A CG  1 
ATOM   2531 C  CD  . PRO   A 1 356 ? -9.938  -4.251  75.861  1.00 28.32  ? 384 PRO   A CD  1 
ATOM   2532 N  N   . LEU   A 1 357 ? -8.006  -4.818  71.510  1.00 27.15  ? 385 LEU   A N   1 
ATOM   2533 C  CA  . LEU   A 1 357 ? -8.051  -4.379  70.116  1.00 26.09  ? 385 LEU   A CA  1 
ATOM   2534 C  C   . LEU   A 1 357 ? -9.129  -5.073  69.297  1.00 25.96  ? 385 LEU   A C   1 
ATOM   2535 O  O   . LEU   A 1 357 ? -9.397  -4.641  68.167  1.00 25.47  ? 385 LEU   A O   1 
ATOM   2536 C  CB  . LEU   A 1 357 ? -6.710  -4.613  69.436  1.00 25.51  ? 385 LEU   A CB  1 
ATOM   2537 C  CG  . LEU   A 1 357 ? -5.461  -4.309  70.252  1.00 28.19  ? 385 LEU   A CG  1 
ATOM   2538 C  CD1 . LEU   A 1 357 ? -4.241  -4.661  69.413  1.00 28.39  ? 385 LEU   A CD1 1 
ATOM   2539 C  CD2 . LEU   A 1 357 ? -5.439  -2.832  70.656  1.00 30.01  ? 385 LEU   A CD2 1 
ATOM   2540 N  N   . GLY   A 1 358 ? -9.730  -6.138  69.820  1.00 23.12  ? 386 GLY   A N   1 
ATOM   2541 C  CA  . GLY   A 1 358 ? -10.682 -6.930  69.066  1.00 25.01  ? 386 GLY   A CA  1 
ATOM   2542 C  C   . GLY   A 1 358 ? -11.833 -7.373  69.937  1.00 26.46  ? 386 GLY   A C   1 
ATOM   2543 O  O   . GLY   A 1 358 ? -12.048 -6.828  71.025  1.00 32.21  ? 386 GLY   A O   1 
ATOM   2544 N  N   . ASP   A 1 359 ? -12.573 -8.376  69.469  1.00 27.12  ? 387 ASP   A N   1 
ATOM   2545 C  CA  . ASP   A 1 359 ? -13.702 -8.904  70.230  1.00 28.23  ? 387 ASP   A CA  1 
ATOM   2546 C  C   . ASP   A 1 359 ? -13.282 -9.445  71.590  1.00 27.29  ? 387 ASP   A C   1 
ATOM   2547 O  O   . ASP   A 1 359 ? -13.978 -9.232  72.590  1.00 27.65  ? 387 ASP   A O   1 
ATOM   2548 C  CB  . ASP   A 1 359 ? -14.407 -9.997  69.417  1.00 28.02  ? 387 ASP   A CB  1 
ATOM   2549 C  CG  . ASP   A 1 359 ? -14.965 -9.459  68.133  1.00 27.46  ? 387 ASP   A CG  1 
ATOM   2550 O  OD1 . ASP   A 1 359 ? -15.283 -8.264  68.122  1.00 27.74  ? 387 ASP   A OD1 1 
ATOM   2551 O  OD2 . ASP   A 1 359 ? -15.055 -10.189 67.133  1.00 29.52  ? 387 ASP   A OD2 1 
ATOM   2552 N  N   . ARG   A 1 360 ? -12.179 -10.138 71.649  1.00 28.37  ? 388 ARG   A N   1 
ATOM   2553 C  CA  . ARG   A 1 360 ? -11.872 -10.813 72.901  1.00 26.78  ? 388 ARG   A CA  1 
ATOM   2554 C  C   . ARG   A 1 360 ? -11.065 -9.912  73.833  1.00 31.19  ? 388 ARG   A C   1 
ATOM   2555 O  O   . ARG   A 1 360 ? -10.283 -9.071  73.379  1.00 30.88  ? 388 ARG   A O   1 
ATOM   2556 C  CB  . ARG   A 1 360 ? -11.082 -12.084 72.631  1.00 24.26  ? 388 ARG   A CB  1 
ATOM   2557 C  CG  . ARG   A 1 360 ? -11.690 -12.946 71.548  1.00 28.24  ? 388 ARG   A CG  1 
ATOM   2558 C  CD  . ARG   A 1 360 ? -11.002 -14.283 71.480  1.00 32.85  ? 388 ARG   A CD  1 
ATOM   2559 N  NE  . ARG   A 1 360 ? -11.559 -15.088 70.407  1.00 34.84  ? 388 ARG   A NE  1 
ATOM   2560 C  CZ  . ARG   A 1 360 ? -11.188 -16.331 70.142  1.00 34.81  ? 388 ARG   A CZ  1 
ATOM   2561 N  NH1 . ARG   A 1 360 ? -11.757 -16.972 69.129  1.00 35.35  ? 388 ARG   A NH1 1 
ATOM   2562 N  NH2 . ARG   A 1 360 ? -10.255 -16.926 70.886  1.00 28.23  ? 388 ARG   A NH2 1 
ATOM   2563 N  N   . PRO   A 1 361 ? -11.221 -10.094 75.150  1.00 29.89  ? 389 PRO   A N   1 
ATOM   2564 C  CA  . PRO   A 1 361 ? -10.389 -9.359  76.115  1.00 29.23  ? 389 PRO   A CA  1 
ATOM   2565 C  C   . PRO   A 1 361 ? -9.006  -9.995  76.212  1.00 32.61  ? 389 PRO   A C   1 
ATOM   2566 O  O   . PRO   A 1 361 ? -8.629  -10.595 77.206  1.00 30.56  ? 389 PRO   A O   1 
ATOM   2567 C  CB  . PRO   A 1 361 ? -11.197 -9.494  77.405  1.00 26.90  ? 389 PRO   A CB  1 
ATOM   2568 C  CG  . PRO   A 1 361 ? -11.793 -10.915 77.278  1.00 29.09  ? 389 PRO   A CG  1 
ATOM   2569 C  CD  . PRO   A 1 361 ? -12.115 -11.069 75.811  1.00 31.73  ? 389 PRO   A CD  1 
ATOM   2570 N  N   . THR   A 1 362 ? -8.226  -9.879  75.130  1.00 29.68  ? 390 THR   A N   1 
ATOM   2571 C  CA  . THR   A 1 362 ? -6.919  -10.511 75.045  1.00 33.00  ? 390 THR   A CA  1 
ATOM   2572 C  C   . THR   A 1 362 ? -5.887  -9.445  74.729  1.00 31.53  ? 390 THR   A C   1 
ATOM   2573 O  O   . THR   A 1 362 ? -5.396  -8.765  75.649  1.00 29.42  ? 390 THR   A O   1 
ATOM   2574 C  CB  . THR   A 1 362 ? -6.936  -11.641 74.011  1.00 31.73  ? 390 THR   A CB  1 
ATOM   2575 O  OG1 . THR   A 1 362 ? -7.521  -11.157 72.793  1.00 29.59  ? 390 THR   A OG1 1 
ATOM   2576 C  CG2 . THR   A 1 362 ? -7.748  -12.814 74.520  1.00 31.25  ? 390 THR   A CG2 1 
ATOM   2577 N  N   . ILE   A 1 363 ? -5.523  -9.246  73.465  1.00 29.05  ? 391 ILE   A N   1 
ATOM   2578 C  CA  . ILE   A 1 363 ? -4.434  -8.344  73.122  1.00 26.95  ? 391 ILE   A CA  1 
ATOM   2579 C  C   . ILE   A 1 363 ? -4.884  -6.896  73.285  1.00 31.86  ? 391 ILE   A C   1 
ATOM   2580 O  O   . ILE   A 1 363 ? -6.033  -6.546  72.985  1.00 29.34  ? 391 ILE   A O   1 
ATOM   2581 C  CB  . ILE   A 1 363 ? -3.956  -8.623  71.685  1.00 27.83  ? 391 ILE   A CB  1 
ATOM   2582 C  CG1 . ILE   A 1 363 ? -2.893  -7.606  71.248  1.00 28.52  ? 391 ILE   A CG1 1 
ATOM   2583 C  CG2 . ILE   A 1 363 ? -5.166  -8.604  70.738  1.00 22.67  ? 391 ILE   A CG2 1 
ATOM   2584 C  CD1 . ILE   A 1 363 ? -2.068  -8.049  70.036  1.00 24.32  ? 391 ILE   A CD1 1 
ATOM   2585 N  N   . PHE   A 1 364 ? -3.983  -6.043  73.774  1.00 30.44  ? 392 PHE   A N   1 
ATOM   2586 C  CA  . PHE   A 1 364 ? -4.234  -4.606  73.802  1.00 31.19  ? 392 PHE   A CA  1 
ATOM   2587 C  C   . PHE   A 1 364 ? -2.928  -3.892  73.486  1.00 32.35  ? 392 PHE   A C   1 
ATOM   2588 O  O   . PHE   A 1 364 ? -1.882  -4.522  73.261  1.00 28.10  ? 392 PHE   A O   1 
ATOM   2589 C  CB  . PHE   A 1 364 ? -4.831  -4.156  75.148  1.00 33.03  ? 392 PHE   A CB  1 
ATOM   2590 C  CG  . PHE   A 1 364 ? -4.029  -4.580  76.365  1.00 34.80  ? 392 PHE   A CG  1 
ATOM   2591 C  CD1 . PHE   A 1 364 ? -4.220  -5.831  76.946  1.00 30.20  ? 392 PHE   A CD1 1 
ATOM   2592 C  CD2 . PHE   A 1 364 ? -3.094  -3.723  76.929  1.00 32.60  ? 392 PHE   A CD2 1 
ATOM   2593 C  CE1 . PHE   A 1 364 ? -3.498  -6.217  78.066  1.00 33.96  ? 392 PHE   A CE1 1 
ATOM   2594 C  CE2 . PHE   A 1 364 ? -2.351  -4.111  78.040  1.00 35.99  ? 392 PHE   A CE2 1 
ATOM   2595 C  CZ  . PHE   A 1 364 ? -2.552  -5.360  78.612  1.00 31.83  ? 392 PHE   A CZ  1 
ATOM   2596 N  N   . ILE   A 1 365 ? -2.983  -2.568  73.459  1.00 30.21  ? 393 ILE   A N   1 
ATOM   2597 C  CA  . ILE   A 1 365 ? -1.824  -1.766  73.096  1.00 28.78  ? 393 ILE   A CA  1 
ATOM   2598 C  C   . ILE   A 1 365 ? -1.544  -0.799  74.236  1.00 28.92  ? 393 ILE   A C   1 
ATOM   2599 O  O   . ILE   A 1 365 ? -2.454  -0.402  74.971  1.00 33.94  ? 393 ILE   A O   1 
ATOM   2600 C  CB  . ILE   A 1 365 ? -2.053  -1.034  71.751  1.00 34.01  ? 393 ILE   A CB  1 
ATOM   2601 C  CG1 . ILE   A 1 365 ? -1.891  -2.016  70.583  1.00 27.33  ? 393 ILE   A CG1 1 
ATOM   2602 C  CG2 . ILE   A 1 365 ? -1.129  0.184   71.597  1.00 25.00  ? 393 ILE   A CG2 1 
ATOM   2603 C  CD1 . ILE   A 1 365 ? -2.149  -1.403  69.212  1.00 23.54  ? 393 ILE   A CD1 1 
ATOM   2604 N  N   . GLU   A 1 366 ? -0.264  -0.481  74.421  1.00 29.42  ? 394 GLU   A N   1 
ATOM   2605 C  CA  . GLU   A 1 366 ? 0.214   0.460   75.426  1.00 33.64  ? 394 GLU   A CA  1 
ATOM   2606 C  C   . GLU   A 1 366 ? 0.967   1.563   74.702  1.00 30.62  ? 394 GLU   A C   1 
ATOM   2607 O  O   . GLU   A 1 366 ? 1.784   1.274   73.822  1.00 29.85  ? 394 GLU   A O   1 
ATOM   2608 C  CB  . GLU   A 1 366 ? 1.142   -0.243  76.430  1.00 35.58  ? 394 GLU   A CB  1 
ATOM   2609 C  CG  . GLU   A 1 366 ? 1.364   0.456   77.777  1.00 33.93  ? 394 GLU   A CG  1 
ATOM   2610 C  CD  . GLU   A 1 366 ? 2.598   -0.093  78.536  1.00 38.04  ? 394 GLU   A CD  1 
ATOM   2611 O  OE1 . GLU   A 1 366 ? 3.022   -1.232  78.259  1.00 36.15  ? 394 GLU   A OE1 1 
ATOM   2612 O  OE2 . GLU   A 1 366 ? 3.175   0.626   79.388  1.00 38.04  ? 394 GLU   A OE2 1 
ATOM   2613 N  N   . ILE   A 1 367 ? 0.679   2.820   75.037  1.00 31.67  ? 395 ILE   A N   1 
ATOM   2614 C  CA  . ILE   A 1 367 ? 1.390   3.955   74.461  1.00 28.07  ? 395 ILE   A CA  1 
ATOM   2615 C  C   . ILE   A 1 367 ? 2.384   4.462   75.491  1.00 32.80  ? 395 ILE   A C   1 
ATOM   2616 O  O   . ILE   A 1 367 ? 2.026   4.666   76.660  1.00 36.17  ? 395 ILE   A O   1 
ATOM   2617 C  CB  . ILE   A 1 367 ? 0.426   5.075   74.025  1.00 33.70  ? 395 ILE   A CB  1 
ATOM   2618 C  CG1 . ILE   A 1 367 ? -0.670  4.518   73.102  1.00 30.20  ? 395 ILE   A CG1 1 
ATOM   2619 C  CG2 . ILE   A 1 367 ? 1.222   6.246   73.395  1.00 28.46  ? 395 ILE   A CG2 1 
ATOM   2620 C  CD1 . ILE   A 1 367 ? -0.153  3.701   71.928  1.00 26.12  ? 395 ILE   A CD1 1 
ATOM   2621 N  N   . ILE   A 1 368 ? 3.627   4.677   75.058  1.00 32.58  ? 396 ILE   A N   1 
ATOM   2622 C  CA  . ILE   A 1 368 ? 4.770   4.864   75.958  1.00 34.86  ? 396 ILE   A CA  1 
ATOM   2623 C  C   . ILE   A 1 368 ? 5.575   6.071   75.519  1.00 32.54  ? 396 ILE   A C   1 
ATOM   2624 O  O   . ILE   A 1 368 ? 5.697   6.351   74.319  1.00 34.13  ? 396 ILE   A O   1 
ATOM   2625 C  CB  . ILE   A 1 368 ? 5.686   3.612   75.993  1.00 29.07  ? 396 ILE   A CB  1 
ATOM   2626 C  CG1 . ILE   A 1 368 ? 5.247   2.663   77.073  1.00 37.13  ? 396 ILE   A CG1 1 
ATOM   2627 C  CG2 . ILE   A 1 368 ? 7.146   3.919   76.151  1.00 38.47  ? 396 ILE   A CG2 1 
ATOM   2628 C  CD1 . ILE   A 1 368 ? 4.003   2.030   76.699  1.00 37.96  ? 396 ILE   A CD1 1 
ATOM   2629 N  N   . GLN   A 1 369 ? 6.115   6.793   76.493  1.00 34.55  ? 397 GLN   A N   1 
ATOM   2630 C  CA  . GLN   A 1 369 ? 7.232   7.689   76.237  1.00 34.80  ? 397 GLN   A CA  1 
ATOM   2631 C  C   . GLN   A 1 369 ? 8.098   7.715   77.486  1.00 35.70  ? 397 GLN   A C   1 
ATOM   2632 O  O   . GLN   A 1 369 ? 7.580   7.758   78.607  1.00 38.75  ? 397 GLN   A O   1 
ATOM   2633 C  CB  . GLN   A 1 369 ? 6.775   9.100   75.845  1.00 32.62  ? 397 GLN   A CB  1 
ATOM   2634 C  CG  . GLN   A 1 369 ? 7.918   9.947   75.312  1.00 37.73  ? 397 GLN   A CG  1 
ATOM   2635 C  CD  . GLN   A 1 369 ? 7.466   11.235  74.637  1.00 40.58  ? 397 GLN   A CD  1 
ATOM   2636 O  OE1 . GLN   A 1 369 ? 8.144   11.732  73.740  1.00 44.96  ? 397 GLN   A OE1 1 
ATOM   2637 N  NE2 . GLN   A 1 369 ? 6.334   11.775  75.059  1.00 31.26  ? 397 GLN   A NE2 1 
ATOM   2638 N  N   . ARG   A 1 370 ? 9.410   7.675   77.285  1.00 29.30  ? 398 ARG   A N   1 
ATOM   2639 C  CA  . ARG   A 1 370 ? 10.367  7.582   78.378  1.00 40.50  ? 398 ARG   A CA  1 
ATOM   2640 C  C   . ARG   A 1 370 ? 11.210  8.852   78.469  1.00 39.59  ? 398 ARG   A C   1 
ATOM   2641 O  O   . ARG   A 1 370 ? 11.654  9.385   77.448  1.00 39.18  ? 398 ARG   A O   1 
ATOM   2642 C  CB  . ARG   A 1 370 ? 11.269  6.370   78.172  1.00 38.39  ? 398 ARG   A CB  1 
ATOM   2643 C  CG  . ARG   A 1 370 ? 10.505  5.074   77.902  1.00 36.25  ? 398 ARG   A CG  1 
ATOM   2644 C  CD  . ARG   A 1 370 ? 11.469  3.880   77.780  1.00 38.96  ? 398 ARG   A CD  1 
ATOM   2645 N  NE  . ARG   A 1 370 ? 10.766  2.610   77.817  1.00 39.14  ? 398 ARG   A NE  1 
ATOM   2646 C  CZ  . ARG   A 1 370 ? 10.388  1.982   78.932  1.00 44.33  ? 398 ARG   A CZ  1 
ATOM   2647 N  NH1 . ARG   A 1 370 ? 10.668  2.486   80.127  1.00 38.76  ? 398 ARG   A NH1 1 
ATOM   2648 N  NH2 . ARG   A 1 370 ? 9.740   0.827   78.847  1.00 36.45  ? 398 ARG   A NH2 1 
ATOM   2649 N  N   . VAL   A 1 371 ? 11.444  9.340   79.685  1.00 35.77  ? 399 VAL   A N   1 
ATOM   2650 C  CA  . VAL   A 1 371 ? 12.321  10.494  79.903  1.00 45.08  ? 399 VAL   A CA  1 
ATOM   2651 C  C   . VAL   A 1 371 ? 13.487  10.090  80.796  1.00 42.87  ? 399 VAL   A C   1 
ATOM   2652 O  O   . VAL   A 1 371 ? 13.285  9.546   81.889  1.00 41.12  ? 399 VAL   A O   1 
ATOM   2653 C  CB  . VAL   A 1 371 ? 11.570  11.698  80.494  1.00 46.09  ? 399 VAL   A CB  1 
ATOM   2654 C  CG1 . VAL   A 1 371 ? 10.895  12.454  79.412  1.00 48.83  ? 399 VAL   A CG1 1 
ATOM   2655 C  CG2 . VAL   A 1 371 ? 10.497  11.226  81.411  1.00 48.07  ? 399 VAL   A CG2 1 
ATOM   2656 N  N   . GLY   A 1 372 ? 14.703  10.365  80.330  1.00 45.52  ? 400 GLY   A N   1 
ATOM   2657 C  CA  . GLY   A 1 372 ? 15.906  10.113  81.110  1.00 52.95  ? 400 GLY   A CA  1 
ATOM   2658 C  C   . GLY   A 1 372 ? 16.884  9.178   80.426  1.00 53.88  ? 400 GLY   A C   1 
ATOM   2659 O  O   . GLY   A 1 372 ? 16.747  8.896   79.231  1.00 55.77  ? 400 GLY   A O   1 
ATOM   2660 N  N   . CYS   A 1 373 ? 17.881  8.704   81.171  1.00 51.56  ? 401 CYS   A N   1 
ATOM   2661 C  CA  . CYS   A 1 373 ? 18.829  7.693   80.692  1.00 56.76  ? 401 CYS   A CA  1 
ATOM   2662 C  C   . CYS   A 1 373 ? 19.391  8.041   79.316  1.00 60.59  ? 401 CYS   A C   1 
ATOM   2663 O  O   . CYS   A 1 373 ? 19.433  7.206   78.412  1.00 62.42  ? 401 CYS   A O   1 
ATOM   2664 C  CB  . CYS   A 1 373 ? 18.186  6.304   80.651  1.00 50.71  ? 401 CYS   A CB  1 
ATOM   2665 S  SG  . CYS   A 1 373 ? 17.046  5.941   81.983  1.00 53.23  ? 401 CYS   A SG  1 
ATOM   2666 N  N   . MET   A 1 374 ? 19.823  9.288   79.152  1.00 61.91  ? 402 MET   A N   1 
ATOM   2667 C  CA  . MET   A 1 374 ? 20.478  9.707   77.919  1.00 66.14  ? 402 MET   A CA  1 
ATOM   2668 C  C   . MET   A 1 374 ? 21.993  9.664   78.096  1.00 71.42  ? 402 MET   A C   1 
ATOM   2669 O  O   . MET   A 1 374 ? 22.520  10.137  79.107  1.00 71.17  ? 402 MET   A O   1 
ATOM   2670 C  CB  . MET   A 1 374 ? 20.021  11.103  77.484  1.00 68.20  ? 402 MET   A CB  1 
ATOM   2671 C  CG  . MET   A 1 374 ? 18.505  11.233  77.318  1.00 57.91  ? 402 MET   A CG  1 
ATOM   2672 S  SD  . MET   A 1 374 ? 17.971  10.768  75.656  1.00 68.23  ? 402 MET   A SD  1 
ATOM   2673 C  CE  . MET   A 1 374 ? 19.233  11.545  74.641  1.00 64.62  ? 402 MET   A CE  1 
ATOM   2674 N  N   . MET   A 1 375 ? 22.691  9.052   77.134  1.00 70.38  ? 403 MET   A N   1 
ATOM   2675 C  CA  . MET   A 1 375 ? 24.159  9.056   77.177  1.00 74.96  ? 403 MET   A CA  1 
ATOM   2676 C  C   . MET   A 1 375 ? 24.662  9.544   75.804  1.00 79.25  ? 403 MET   A C   1 
ATOM   2677 O  O   . MET   A 1 375 ? 23.868  9.957   74.940  1.00 77.79  ? 403 MET   A O   1 
ATOM   2678 C  CB  . MET   A 1 375 ? 24.768  7.659   77.550  1.00 75.71  ? 403 MET   A CB  1 
ATOM   2679 C  CG  . MET   A 1 375 ? 23.874  6.673   78.297  1.00 66.39  ? 403 MET   A CG  1 
ATOM   2680 S  SD  . MET   A 1 375 ? 24.408  5.418   79.534  1.00 91.81  ? 403 MET   A SD  1 
ATOM   2681 C  CE  . MET   A 1 375 ? 25.487  4.294   78.759  1.00 68.77  ? 403 MET   A CE  1 
ATOM   2682 N  N   . TYR   A 1 383 ? 21.762  9.400   73.013  1.00 68.38  ? 411 TYR   A N   1 
ATOM   2683 C  CA  . TYR   A 1 383 ? 20.748  8.356   72.869  1.00 63.73  ? 411 TYR   A CA  1 
ATOM   2684 C  C   . TYR   A 1 383 ? 20.073  8.061   74.200  1.00 65.84  ? 411 TYR   A C   1 
ATOM   2685 O  O   . TYR   A 1 383 ? 20.571  8.462   75.249  1.00 66.82  ? 411 TYR   A O   1 
ATOM   2686 C  CB  . TYR   A 1 383 ? 21.386  7.083   72.317  1.00 65.55  ? 411 TYR   A CB  1 
ATOM   2687 C  CG  . TYR   A 1 383 ? 22.303  6.363   73.354  1.00 73.23  ? 411 TYR   A CG  1 
ATOM   2688 C  CD1 . TYR   A 1 383 ? 23.707  6.450   73.263  1.00 71.16  ? 411 TYR   A CD1 1 
ATOM   2689 C  CD2 . TYR   A 1 383 ? 21.779  5.572   74.412  1.00 70.53  ? 411 TYR   A CD2 1 
ATOM   2690 C  CE1 . TYR   A 1 383 ? 24.530  5.807   74.194  1.00 70.36  ? 411 TYR   A CE1 1 
ATOM   2691 C  CE2 . TYR   A 1 383 ? 22.640  4.940   75.336  1.00 69.95  ? 411 TYR   A CE2 1 
ATOM   2692 C  CZ  . TYR   A 1 383 ? 23.989  5.060   75.200  1.00 72.24  ? 411 TYR   A CZ  1 
ATOM   2693 O  OH  . TYR   A 1 383 ? 24.832  4.432   76.091  1.00 76.83  ? 411 TYR   A OH  1 
ATOM   2694 N  N   . GLN   A 1 384 ? 18.956  7.334   74.165  1.00 65.42  ? 412 GLN   A N   1 
ATOM   2695 C  CA  . GLN   A 1 384 ? 18.283  6.874   75.376  1.00 61.97  ? 412 GLN   A CA  1 
ATOM   2696 C  C   . GLN   A 1 384 ? 18.404  5.362   75.501  1.00 64.36  ? 412 GLN   A C   1 
ATOM   2697 O  O   . GLN   A 1 384 ? 18.092  4.631   74.553  1.00 63.42  ? 412 GLN   A O   1 
ATOM   2698 C  CB  . GLN   A 1 384 ? 16.810  7.269   75.387  1.00 54.32  ? 412 GLN   A CB  1 
ATOM   2699 C  CG  . GLN   A 1 384 ? 16.118  6.840   76.667  1.00 53.71  ? 412 GLN   A CG  1 
ATOM   2700 C  CD  . GLN   A 1 384 ? 14.654  7.241   76.716  1.00 55.69  ? 412 GLN   A CD  1 
ATOM   2701 O  OE1 . GLN   A 1 384 ? 13.835  6.777   75.915  1.00 55.53  ? 412 GLN   A OE1 1 
ATOM   2702 N  NE2 . GLN   A 1 384 ? 14.317  8.115   77.660  1.00 55.99  ? 412 GLN   A NE2 1 
ATOM   2703 N  N   . SER   A 1 385 ? 18.836  4.897   76.672  1.00 56.12  ? 413 SER   A N   1 
ATOM   2704 C  CA  . SER   A 1 385 ? 18.975  3.466   76.899  1.00 56.69  ? 413 SER   A CA  1 
ATOM   2705 C  C   . SER   A 1 385 ? 17.608  2.817   77.103  1.00 53.23  ? 413 SER   A C   1 
ATOM   2706 O  O   . SER   A 1 385 ? 16.661  3.444   77.591  1.00 52.98  ? 413 SER   A O   1 
ATOM   2707 C  CB  . SER   A 1 385 ? 19.884  3.186   78.101  1.00 54.72  ? 413 SER   A CB  1 
ATOM   2708 O  OG  . SER   A 1 385 ? 19.340  3.703   79.302  1.00 54.87  ? 413 SER   A OG  1 
ATOM   2709 N  N   . GLY   A 1 386 ? 17.517  1.544   76.721  1.00 48.53  ? 414 GLY   A N   1 
ATOM   2710 C  CA  . GLY   A 1 386 ? 16.246  0.854   76.760  1.00 44.89  ? 414 GLY   A CA  1 
ATOM   2711 C  C   . GLY   A 1 386 ? 15.728  0.634   78.168  1.00 46.57  ? 414 GLY   A C   1 
ATOM   2712 O  O   . GLY   A 1 386 ? 16.483  0.550   79.135  1.00 44.57  ? 414 GLY   A O   1 
ATOM   2713 N  N   . GLY   A 1 387 ? 14.402  0.520   78.269  1.00 42.80  ? 415 GLY   A N   1 
ATOM   2714 C  CA  . GLY   A 1 387 ? 13.739  0.293   79.533  1.00 41.33  ? 415 GLY   A CA  1 
ATOM   2715 C  C   . GLY   A 1 387 ? 13.699  1.491   80.447  1.00 42.03  ? 415 GLY   A C   1 
ATOM   2716 O  O   . GLY   A 1 387 ? 13.174  1.379   81.564  1.00 43.00  ? 415 GLY   A O   1 
ATOM   2717 N  N   . CYS   A 1 388 ? 14.223  2.634   80.009  1.00 39.57  ? 416 CYS   A N   1 
ATOM   2718 C  CA  . CYS   A 1 388 ? 14.373  3.788   80.881  1.00 37.94  ? 416 CYS   A CA  1 
ATOM   2719 C  C   . CYS   A 1 388 ? 13.065  4.153   81.557  1.00 43.31  ? 416 CYS   A C   1 
ATOM   2720 O  O   . CYS   A 1 388 ? 12.141  4.662   80.910  1.00 45.41  ? 416 CYS   A O   1 
ATOM   2721 C  CB  . CYS   A 1 388 ? 14.898  4.983   80.101  1.00 44.95  ? 416 CYS   A CB  1 
ATOM   2722 S  SG  . CYS   A 1 388 ? 15.234  6.389   81.167  1.00 52.14  ? 416 CYS   A SG  1 
ATOM   2723 N  N   . GLY   A 1 389 ? 12.981  3.899   82.857  1.00 41.64  ? 417 GLY   A N   1 
ATOM   2724 C  CA  . GLY   A 1 389 ? 11.788  4.161   83.633  1.00 42.24  ? 417 GLY   A CA  1 
ATOM   2725 C  C   . GLY   A 1 389 ? 11.034  2.913   84.004  1.00 40.09  ? 417 GLY   A C   1 
ATOM   2726 O  O   . GLY   A 1 389 ? 10.091  2.988   84.801  1.00 44.93  ? 417 GLY   A O   1 
ATOM   2727 N  N   . GLY   A 1 390 ? 11.419  1.769   83.461  1.00 41.80  ? 418 GLY   A N   1 
ATOM   2728 C  CA  . GLY   A 1 390 ? 10.791  0.521   83.844  1.00 43.53  ? 418 GLY   A CA  1 
ATOM   2729 C  C   . GLY   A 1 390 ? 9.577   0.228   82.992  1.00 41.41  ? 418 GLY   A C   1 
ATOM   2730 O  O   . GLY   A 1 390 ? 9.541   0.586   81.808  1.00 42.09  ? 418 GLY   A O   1 
ATOM   2731 N  N   . PHE   A 1 391 ? 8.570   -0.415  83.588  1.00 38.87  ? 419 PHE   A N   1 
ATOM   2732 C  CA  . PHE   A 1 391 ? 7.372   -0.812  82.859  1.00 37.69  ? 419 PHE   A CA  1 
ATOM   2733 C  C   . PHE   A 1 391 ? 6.093   -0.461  83.608  1.00 41.06  ? 419 PHE   A C   1 
ATOM   2734 O  O   . PHE   A 1 391 ? 5.001   -0.864  83.181  1.00 44.51  ? 419 PHE   A O   1 
ATOM   2735 C  CB  . PHE   A 1 391 ? 7.430   -2.311  82.542  1.00 37.38  ? 419 PHE   A CB  1 
ATOM   2736 C  CG  . PHE   A 1 391 ? 8.646   -2.695  81.734  1.00 42.47  ? 419 PHE   A CG  1 
ATOM   2737 C  CD1 . PHE   A 1 391 ? 9.860   -2.999  82.366  1.00 39.48  ? 419 PHE   A CD1 1 
ATOM   2738 C  CD2 . PHE   A 1 391 ? 8.595   -2.698  80.347  1.00 35.56  ? 419 PHE   A CD2 1 
ATOM   2739 C  CE1 . PHE   A 1 391 ? 10.977  -3.332  81.625  1.00 36.79  ? 419 PHE   A CE1 1 
ATOM   2740 C  CE2 . PHE   A 1 391 ? 9.703   -3.025  79.603  1.00 37.19  ? 419 PHE   A CE2 1 
ATOM   2741 C  CZ  . PHE   A 1 391 ? 10.907  -3.349  80.244  1.00 39.40  ? 419 PHE   A CZ  1 
ATOM   2742 N  N   . GLY   A 1 392 ? 6.191   0.300   84.685  1.00 40.08  ? 420 GLY   A N   1 
ATOM   2743 C  CA  . GLY   A 1 392 ? 5.027   0.774   85.387  1.00 44.31  ? 420 GLY   A CA  1 
ATOM   2744 C  C   . GLY   A 1 392 ? 4.762   0.073   86.686  1.00 45.10  ? 420 GLY   A C   1 
ATOM   2745 O  O   . GLY   A 1 392 ? 3.647   0.184   87.208  1.00 47.61  ? 420 GLY   A O   1 
ATOM   2746 N  N   . LYS   A 1 393 ? 5.755   -0.631  87.231  1.00 51.45  ? 421 LYS   A N   1 
ATOM   2747 C  CA  . LYS   A 1 393 ? 5.542   -1.416  88.442  1.00 57.55  ? 421 LYS   A CA  1 
ATOM   2748 C  C   . LYS   A 1 393 ? 4.891   -0.577  89.539  1.00 60.00  ? 421 LYS   A C   1 
ATOM   2749 O  O   . LYS   A 1 393 ? 3.910   -1.000  90.165  1.00 57.99  ? 421 LYS   A O   1 
ATOM   2750 C  CB  . LYS   A 1 393 ? 6.873   -2.008  88.915  1.00 50.86  ? 421 LYS   A CB  1 
ATOM   2751 C  CG  . LYS   A 1 393 ? 6.720   -2.972  90.076  1.00 55.60  ? 421 LYS   A CG  1 
ATOM   2752 C  CD  . LYS   A 1 393 ? 7.627   -4.178  89.928  1.00 55.53  ? 421 LYS   A CD  1 
ATOM   2753 C  CE  . LYS   A 1 393 ? 7.080   -5.360  90.723  1.00 61.34  ? 421 LYS   A CE  1 
ATOM   2754 N  NZ  . LYS   A 1 393 ? 5.626   -5.571  90.455  1.00 57.84  ? 421 LYS   A NZ  1 
ATOM   2755 N  N   . GLY   A 1 394 ? 5.395   0.643   89.745  1.00 54.17  ? 422 GLY   A N   1 
ATOM   2756 C  CA  . GLY   A 1 394 ? 4.895   1.474   90.821  1.00 50.45  ? 422 GLY   A CA  1 
ATOM   2757 C  C   . GLY   A 1 394 ? 3.450   1.885   90.672  1.00 56.86  ? 422 GLY   A C   1 
ATOM   2758 O  O   . GLY   A 1 394 ? 2.854   2.363   91.642  1.00 62.86  ? 422 GLY   A O   1 
ATOM   2759 N  N   . ASN   A 1 395 ? 2.866   1.714   89.480  1.00 58.28  ? 423 ASN   A N   1 
ATOM   2760 C  CA  . ASN   A 1 395 ? 1.507   2.182   89.242  1.00 55.10  ? 423 ASN   A CA  1 
ATOM   2761 C  C   . ASN   A 1 395 ? 0.452   1.220   89.778  1.00 57.10  ? 423 ASN   A C   1 
ATOM   2762 O  O   . ASN   A 1 395 ? -0.713  1.610   89.912  1.00 51.51  ? 423 ASN   A O   1 
ATOM   2763 C  CB  . ASN   A 1 395 ? 1.284   2.436   87.743  1.00 52.19  ? 423 ASN   A CB  1 
ATOM   2764 C  CG  . ASN   A 1 395 ? 1.450   3.911   87.362  1.00 50.96  ? 423 ASN   A CG  1 
ATOM   2765 O  OD1 . ASN   A 1 395 ? 1.091   4.802   88.125  1.00 50.64  ? 423 ASN   A OD1 1 
ATOM   2766 N  ND2 . ASN   A 1 395 ? 1.992   4.165   86.173  1.00 48.29  ? 423 ASN   A ND2 1 
ATOM   2767 N  N   . PHE   A 1 396 ? 0.822   -0.022  90.092  1.00 54.85  ? 424 PHE   A N   1 
ATOM   2768 C  CA  . PHE   A 1 396 ? -0.122  -0.902  90.776  1.00 59.30  ? 424 PHE   A CA  1 
ATOM   2769 C  C   . PHE   A 1 396 ? -0.444  -0.359  92.162  1.00 60.14  ? 424 PHE   A C   1 
ATOM   2770 O  O   . PHE   A 1 396 ? -1.614  -0.203  92.530  1.00 62.11  ? 424 PHE   A O   1 
ATOM   2771 C  CB  . PHE   A 1 396 ? 0.444   -2.318  90.865  1.00 56.37  ? 424 PHE   A CB  1 
ATOM   2772 C  CG  . PHE   A 1 396 ? 0.461   -3.051  89.554  1.00 54.76  ? 424 PHE   A CG  1 
ATOM   2773 C  CD1 . PHE   A 1 396 ? 1.535   -2.926  88.692  1.00 52.29  ? 424 PHE   A CD1 1 
ATOM   2774 C  CD2 . PHE   A 1 396 ? -0.587  -3.882  89.195  1.00 54.33  ? 424 PHE   A CD2 1 
ATOM   2775 C  CE1 . PHE   A 1 396 ? 1.557   -3.607  87.492  1.00 50.46  ? 424 PHE   A CE1 1 
ATOM   2776 C  CE2 . PHE   A 1 396 ? -0.569  -4.564  88.000  1.00 51.63  ? 424 PHE   A CE2 1 
ATOM   2777 C  CZ  . PHE   A 1 396 ? 0.504   -4.426  87.148  1.00 48.99  ? 424 PHE   A CZ  1 
ATOM   2778 N  N   . SER   A 1 397 ? 0.594   -0.034  92.933  1.00 65.28  ? 425 SER   A N   1 
ATOM   2779 C  CA  . SER   A 1 397 ? 0.388   0.517   94.267  1.00 61.74  ? 425 SER   A CA  1 
ATOM   2780 C  C   . SER   A 1 397 ? -0.277  1.885   94.201  1.00 59.89  ? 425 SER   A C   1 
ATOM   2781 O  O   . SER   A 1 397 ? -1.214  2.168   94.954  1.00 59.32  ? 425 SER   A O   1 
ATOM   2782 C  CB  . SER   A 1 397 ? 1.724   0.598   95.002  1.00 59.40  ? 425 SER   A CB  1 
ATOM   2783 O  OG  . SER   A 1 397 ? 1.516   0.619   96.400  1.00 63.81  ? 425 SER   A OG  1 
ATOM   2784 N  N   . GLU   A 1 398 ? 0.194   2.749   93.298  1.00 62.38  ? 426 GLU   A N   1 
ATOM   2785 C  CA  . GLU   A 1 398 ? -0.339  4.107   93.223  1.00 58.56  ? 426 GLU   A CA  1 
ATOM   2786 C  C   . GLU   A 1 398 ? -1.812  4.109   92.847  1.00 65.75  ? 426 GLU   A C   1 
ATOM   2787 O  O   . GLU   A 1 398 ? -2.581  4.954   93.323  1.00 66.77  ? 426 GLU   A O   1 
ATOM   2788 C  CB  . GLU   A 1 398 ? 0.467   4.932   92.223  1.00 57.67  ? 426 GLU   A CB  1 
ATOM   2789 C  CG  . GLU   A 1 398 ? 1.802   5.381   92.766  1.00 63.00  ? 426 GLU   A CG  1 
ATOM   2790 C  CD  . GLU   A 1 398 ? 1.639   6.163   94.057  1.00 65.81  ? 426 GLU   A CD  1 
ATOM   2791 O  OE1 . GLU   A 1 398 ? 2.403   5.895   95.014  1.00 64.91  ? 426 GLU   A OE1 1 
ATOM   2792 O  OE2 . GLU   A 1 398 ? 0.727   7.021   94.118  1.00 61.45  ? 426 GLU   A OE2 1 
ATOM   2793 N  N   . LEU   A 1 399 ? -2.227  3.169   91.999  1.00 63.99  ? 427 LEU   A N   1 
ATOM   2794 C  CA  . LEU   A 1 399 ? -3.634  3.076   91.631  1.00 63.63  ? 427 LEU   A CA  1 
ATOM   2795 C  C   . LEU   A 1 399 ? -4.459  2.462   92.752  1.00 67.81  ? 427 LEU   A C   1 
ATOM   2796 O  O   . LEU   A 1 399 ? -5.470  3.034   93.172  1.00 72.78  ? 427 LEU   A O   1 
ATOM   2797 C  CB  . LEU   A 1 399 ? -3.785  2.275   90.340  1.00 59.66  ? 427 LEU   A CB  1 
ATOM   2798 C  CG  . LEU   A 1 399 ? -3.479  3.162   89.137  1.00 60.60  ? 427 LEU   A CG  1 
ATOM   2799 C  CD1 . LEU   A 1 399 ? -3.241  2.340   87.882  1.00 52.67  ? 427 LEU   A CD1 1 
ATOM   2800 C  CD2 . LEU   A 1 399 ? -4.616  4.170   88.947  1.00 55.52  ? 427 LEU   A CD2 1 
ATOM   2801 N  N   . PHE   A 1 400 ? -4.045  1.291   93.244  1.00 63.46  ? 428 PHE   A N   1 
ATOM   2802 C  CA  . PHE   A 1 400 ? -4.725  0.667   94.376  1.00 67.73  ? 428 PHE   A CA  1 
ATOM   2803 C  C   . PHE   A 1 400 ? -4.987  1.685   95.482  1.00 71.12  ? 428 PHE   A C   1 
ATOM   2804 O  O   . PHE   A 1 400 ? -6.110  1.795   95.991  1.00 70.01  ? 428 PHE   A O   1 
ATOM   2805 C  CB  . PHE   A 1 400 ? -3.890  -0.510  94.897  1.00 61.18  ? 428 PHE   A CB  1 
ATOM   2806 N  N   . LYS   A 1 401 ? -3.962  2.475   95.823  1.00 66.50  ? 429 LYS   A N   1 
ATOM   2807 C  CA  . LYS   A 1 401 ? -4.108  3.514   96.838  1.00 68.65  ? 429 LYS   A CA  1 
ATOM   2808 C  C   . LYS   A 1 401 ? -5.089  4.590   96.388  1.00 73.71  ? 429 LYS   A C   1 
ATOM   2809 O  O   . LYS   A 1 401 ? -6.090  4.857   97.065  1.00 75.78  ? 429 LYS   A O   1 
ATOM   2810 C  CB  . LYS   A 1 401 ? -2.739  4.128   97.163  1.00 62.37  ? 429 LYS   A CB  1 
ATOM   2811 N  N   . SER   A 1 402 ? -4.822  5.217   95.234  1.00 71.08  ? 430 SER   A N   1 
ATOM   2812 C  CA  . SER   A 1 402 ? -5.647  6.346   94.806  1.00 71.03  ? 430 SER   A CA  1 
ATOM   2813 C  C   . SER   A 1 402 ? -7.105  5.944   94.603  1.00 71.11  ? 430 SER   A C   1 
ATOM   2814 O  O   . SER   A 1 402 ? -8.003  6.759   94.838  1.00 73.13  ? 430 SER   A O   1 
ATOM   2815 C  CB  . SER   A 1 402 ? -5.081  6.987   93.535  1.00 66.24  ? 430 SER   A CB  1 
ATOM   2816 O  OG  . SER   A 1 402 ? -4.952  6.063   92.475  1.00 71.38  ? 430 SER   A OG  1 
ATOM   2817 N  N   . ILE   A 1 403 ? -7.369  4.705   94.184  1.00 70.17  ? 431 ILE   A N   1 
ATOM   2818 C  CA  . ILE   A 1 403 ? -8.739  4.207   94.239  1.00 70.73  ? 431 ILE   A CA  1 
ATOM   2819 C  C   . ILE   A 1 403 ? -9.290  4.315   95.654  1.00 76.84  ? 431 ILE   A C   1 
ATOM   2820 O  O   . ILE   A 1 403 ? -10.430 4.746   95.859  1.00 81.20  ? 431 ILE   A O   1 
ATOM   2821 C  CB  . ILE   A 1 403 ? -8.814  2.762   93.705  1.00 72.25  ? 431 ILE   A CB  1 
ATOM   2822 C  CG1 . ILE   A 1 403 ? -9.076  2.736   92.195  1.00 68.69  ? 431 ILE   A CG1 1 
ATOM   2823 C  CG2 . ILE   A 1 403 ? -9.850  1.941   94.480  1.00 73.74  ? 431 ILE   A CG2 1 
ATOM   2824 C  CD1 . ILE   A 1 403 ? -7.893  3.144   91.357  1.00 69.54  ? 431 ILE   A CD1 1 
ATOM   2825 N  N   . GLU   A 1 404 ? -8.487  3.939   96.647  1.00 83.12  ? 432 GLU   A N   1 
ATOM   2826 C  CA  . GLU   A 1 404 ? -8.983  3.891   98.018  1.00 82.89  ? 432 GLU   A CA  1 
ATOM   2827 C  C   . GLU   A 1 404 ? -9.163  5.292   98.594  1.00 82.08  ? 432 GLU   A C   1 
ATOM   2828 O  O   . GLU   A 1 404 ? -10.225 5.619   99.141  1.00 83.46  ? 432 GLU   A O   1 
ATOM   2829 C  CB  . GLU   A 1 404 ? -8.040  3.060   98.898  1.00 78.72  ? 432 GLU   A CB  1 
ATOM   2830 N  N   . GLU   A 1 405 ? -8.147  6.145   98.455  1.00 81.43  ? 433 GLU   A N   1 
ATOM   2831 C  CA  . GLU   A 1 405 ? -8.256  7.520   98.935  1.00 82.75  ? 433 GLU   A CA  1 
ATOM   2832 C  C   . GLU   A 1 405 ? -9.194  8.381   98.087  1.00 84.51  ? 433 GLU   A C   1 
ATOM   2833 O  O   . GLU   A 1 405 ? -9.336  9.574   98.376  1.00 86.69  ? 433 GLU   A O   1 
ATOM   2834 C  CB  . GLU   A 1 405 ? -6.868  8.169   99.015  1.00 74.50  ? 433 GLU   A CB  1 
ATOM   2835 C  CG  . GLU   A 1 405 ? -6.083  8.177   97.714  1.00 72.99  ? 433 GLU   A CG  1 
ATOM   2836 C  CD  . GLU   A 1 405 ? -4.643  8.670   97.885  1.00 75.05  ? 433 GLU   A CD  1 
ATOM   2837 O  OE1 . GLU   A 1 405 ? -3.865  8.048   98.651  1.00 72.02  ? 433 GLU   A OE1 1 
ATOM   2838 O  OE2 . GLU   A 1 405 ? -4.286  9.681   97.242  1.00 71.77  ? 433 GLU   A OE2 1 
ATOM   2839 N  N   . TYR   A 1 406 ? -9.844  7.823   97.064  1.00 84.24  ? 434 TYR   A N   1 
ATOM   2840 C  CA  . TYR   A 1 406 ? -10.861 8.576   96.341  1.00 84.25  ? 434 TYR   A CA  1 
ATOM   2841 C  C   . TYR   A 1 406 ? -12.258 8.360   96.901  1.00 86.95  ? 434 TYR   A C   1 
ATOM   2842 O  O   . TYR   A 1 406 ? -13.087 9.278   96.837  1.00 86.39  ? 434 TYR   A O   1 
ATOM   2843 C  CB  . TYR   A 1 406 ? -10.867 8.216   94.854  1.00 80.98  ? 434 TYR   A CB  1 
ATOM   2844 C  CG  . TYR   A 1 406 ? -11.924 8.983   94.109  1.00 79.03  ? 434 TYR   A CG  1 
ATOM   2845 C  CD1 . TYR   A 1 406 ? -11.728 10.318  93.779  1.00 80.42  ? 434 TYR   A CD1 1 
ATOM   2846 C  CD2 . TYR   A 1 406 ? -13.138 8.392   93.777  1.00 83.68  ? 434 TYR   A CD2 1 
ATOM   2847 C  CE1 . TYR   A 1 406 ? -12.697 11.039  93.118  1.00 81.41  ? 434 TYR   A CE1 1 
ATOM   2848 C  CE2 . TYR   A 1 406 ? -14.118 9.104   93.115  1.00 83.03  ? 434 TYR   A CE2 1 
ATOM   2849 C  CZ  . TYR   A 1 406 ? -13.892 10.426  92.787  1.00 85.11  ? 434 TYR   A CZ  1 
ATOM   2850 O  OH  . TYR   A 1 406 ? -14.863 11.141  92.128  1.00 92.36  ? 434 TYR   A OH  1 
ATOM   2851 N  N   . GLU   A 1 407 ? -12.546 7.162   97.422  1.00 85.33  ? 435 GLU   A N   1 
ATOM   2852 C  CA  . GLU   A 1 407 ? -13.800 6.946   98.138  1.00 87.43  ? 435 GLU   A CA  1 
ATOM   2853 C  C   . GLU   A 1 407 ? -14.032 8.051   99.163  1.00 89.71  ? 435 GLU   A C   1 
ATOM   2854 O  O   . GLU   A 1 407 ? -15.145 8.580   99.278  1.00 89.82  ? 435 GLU   A O   1 
ATOM   2855 C  CB  . GLU   A 1 407 ? -13.793 5.569   98.809  1.00 85.69  ? 435 GLU   A CB  1 
ATOM   2856 N  N   . LYS   A 1 408 ? -12.986 8.420   99.902  1.00 88.80  ? 436 LYS   A N   1 
ATOM   2857 C  CA  . LYS   A 1 408 ? -12.957 9.641   100.713 1.00 91.51  ? 436 LYS   A CA  1 
ATOM   2858 C  C   . LYS   A 1 408 ? -14.170 9.806   101.630 1.00 96.88  ? 436 LYS   A C   1 
ATOM   2859 O  O   . LYS   A 1 408 ? -15.027 10.661  101.391 1.00 100.67 ? 436 LYS   A O   1 
ATOM   2860 C  CB  . LYS   A 1 408 ? -12.833 10.869  99.801  1.00 83.71  ? 436 LYS   A CB  1 
HETATM 2861 CO CO  . CO    B 2 .   ? 4.056   -2.728  79.272  1.00 42.89  ? 501 CO    A CO  1 
HETATM 2862 C  C10 . A1LW6 C 3 .   ? 3.933   -5.355  83.473  1.00 41.47  ? 502 A1LW6 A C10 1 
HETATM 2863 C  C13 . A1LW6 C 3 .   ? 6.317   -5.673  81.793  1.00 37.53  ? 502 A1LW6 A C13 1 
HETATM 2864 C  C20 . A1LW6 C 3 .   ? -1.839  -2.829  84.989  1.00 51.09  ? 502 A1LW6 A C20 1 
HETATM 2865 C  C24 . A1LW6 C 3 .   ? -3.031  -1.307  86.430  1.00 48.66  ? 502 A1LW6 A C24 1 
HETATM 2866 C  C26 . A1LW6 C 3 .   ? -5.273  -0.466  86.642  1.00 51.92  ? 502 A1LW6 A C26 1 
HETATM 2867 C  C28 . A1LW6 C 3 .   ? -4.032  -1.153  88.590  1.00 53.01  ? 502 A1LW6 A C28 1 
HETATM 2868 C  C01 . A1LW6 C 3 .   ? 1.351   -2.509  83.346  1.00 41.50  ? 502 A1LW6 A C01 1 
HETATM 2869 C  C02 . A1LW6 C 3 .   ? 0.241   -2.226  84.114  1.00 45.09  ? 502 A1LW6 A C02 1 
HETATM 2870 C  C03 . A1LW6 C 3 .   ? -0.758  -3.146  84.221  1.00 48.07  ? 502 A1LW6 A C03 1 
HETATM 2871 C  C04 . A1LW6 C 3 .   ? -0.654  -4.367  83.539  1.00 41.37  ? 502 A1LW6 A C04 1 
HETATM 2872 C  C05 . A1LW6 C 3 .   ? 0.457   -4.650  82.755  1.00 42.79  ? 502 A1LW6 A C05 1 
HETATM 2873 C  C06 . A1LW6 C 3 .   ? 1.459   -3.694  82.669  1.00 43.16  ? 502 A1LW6 A C06 1 
HETATM 2874 C  C07 . A1LW6 C 3 .   ? 2.755   -3.804  81.877  1.00 41.74  ? 502 A1LW6 A C07 1 
HETATM 2875 C  C08 . A1LW6 C 3 .   ? 3.916   -4.718  82.302  1.00 38.73  ? 502 A1LW6 A C08 1 
HETATM 2876 C  C11 . A1LW6 C 3 .   ? 5.089   -6.276  83.841  1.00 42.59  ? 502 A1LW6 A C11 1 
HETATM 2877 C  C12 . A1LW6 C 3 .   ? 5.786   -6.838  82.611  1.00 42.19  ? 502 A1LW6 A C12 1 
HETATM 2878 C  C14 . A1LW6 C 3 .   ? 5.097   -4.880  81.339  1.00 39.08  ? 502 A1LW6 A C14 1 
HETATM 2879 C  C18 . A1LW6 C 3 .   ? -0.887  -0.758  85.496  1.00 49.69  ? 502 A1LW6 A C18 1 
HETATM 2880 C  C23 . A1LW6 C 3 .   ? 1.250   -0.092  84.619  1.00 44.14  ? 502 A1LW6 A C23 1 
HETATM 2881 C  C25 . A1LW6 C 3 .   ? -4.184  -0.800  85.849  1.00 53.85  ? 502 A1LW6 A C25 1 
HETATM 2882 C  C27 . A1LW6 C 3 .   ? -5.180  -0.649  88.010  1.00 49.98  ? 502 A1LW6 A C27 1 
HETATM 2883 C  C29 . A1LW6 C 3 .   ? -2.950  -1.484  87.798  1.00 53.69  ? 502 A1LW6 A C29 1 
HETATM 2884 N  N17 . A1LW6 C 3 .   ? 0.179   -1.061  84.739  1.00 48.73  ? 502 A1LW6 A N17 1 
HETATM 2885 N  N19 . A1LW6 C 3 .   ? -1.895  -1.651  85.608  1.00 49.19  ? 502 A1LW6 A N19 1 
HETATM 2886 N  N31 . A1LW6 C 3 .   ? 0.523   -5.944  82.066  1.00 44.97  ? 502 A1LW6 A N31 1 
HETATM 2887 O  O09 . A1LW6 C 3 .   ? 2.858   -3.095  80.927  1.00 38.76  ? 502 A1LW6 A O09 1 
HETATM 2888 O  O15 . A1LW6 C 3 .   ? 3.050   -5.023  84.511  1.00 39.73  ? 502 A1LW6 A O15 1 
HETATM 2889 O  O16 . A1LW6 C 3 .   ? 5.075   -4.402  80.250  1.00 38.10  ? 502 A1LW6 A O16 1 
HETATM 2890 O  O21 . A1LW6 C 3 .   ? -2.736  -3.595  85.116  1.00 47.22  ? 502 A1LW6 A O21 1 
HETATM 2891 O  O22 . A1LW6 C 3 .   ? -0.932  0.289   86.049  1.00 52.78  ? 502 A1LW6 A O22 1 
HETATM 2892 O  O32 . A1LW6 C 3 .   ? 1.491   -6.297  81.474  1.00 38.54  ? 502 A1LW6 A O32 1 
HETATM 2893 O  O33 . A1LW6 C 3 .   ? -0.598  -6.797  82.116  1.00 39.14  ? 502 A1LW6 A O33 1 
HETATM 2894 CL CL1 . A1LW6 C 3 .   ? -6.546  -0.256  89.065  1.00 67.28  ? 502 A1LW6 A CL1 1 
HETATM 2895 O  O   . HOH   D 4 .   ? 19.172  -5.828  70.870  1.00 37.09  ? 601 HOH   A O   1 
HETATM 2896 O  O   . HOH   D 4 .   ? 22.707  -8.737  70.571  1.00 36.78  ? 602 HOH   A O   1 
HETATM 2897 O  O   . HOH   D 4 .   ? 15.335  -3.699  85.967  1.00 63.58  ? 603 HOH   A O   1 
HETATM 2898 O  O   . HOH   D 4 .   ? 2.481   -26.822 86.969  1.00 52.28  ? 604 HOH   A O   1 
HETATM 2899 O  O   . HOH   D 4 .   ? 26.785  -11.629 73.931  1.00 48.24  ? 605 HOH   A O   1 
HETATM 2900 O  O   . HOH   D 4 .   ? -7.690  -12.669 70.302  1.00 46.77  ? 606 HOH   A O   1 
HETATM 2901 O  O   . HOH   D 4 .   ? 7.457   -10.972 75.435  1.00 31.64  ? 607 HOH   A O   1 
HETATM 2902 O  O   . HOH   D 4 .   ? 21.290  -11.031 77.542  1.00 57.61  ? 608 HOH   A O   1 
HETATM 2903 O  O   . HOH   D 4 .   ? 14.181  -3.176  68.941  1.00 39.11  ? 609 HOH   A O   1 
HETATM 2904 O  O   . HOH   D 4 .   ? -12.088 -11.355 53.612  1.00 30.51  ? 610 HOH   A O   1 
HETATM 2905 O  O   . HOH   D 4 .   ? 6.831   -20.695 86.478  1.00 52.62  ? 611 HOH   A O   1 
HETATM 2906 O  O   . HOH   D 4 .   ? 22.554  -12.732 63.466  1.00 38.97  ? 612 HOH   A O   1 
HETATM 2907 O  O   . HOH   D 4 .   ? -1.005  -18.108 71.163  1.00 30.40  ? 613 HOH   A O   1 
HETATM 2908 O  O   . HOH   D 4 .   ? -0.897  -19.951 41.671  1.00 48.99  ? 614 HOH   A O   1 
HETATM 2909 O  O   . HOH   D 4 .   ? -4.509  -19.449 47.999  1.00 30.04  ? 615 HOH   A O   1 
HETATM 2910 O  O   . HOH   D 4 .   ? -3.295  13.609  62.461  1.00 52.25  ? 616 HOH   A O   1 
HETATM 2911 O  O   . HOH   D 4 .   ? -11.188 -2.105  69.943  1.00 28.53  ? 617 HOH   A O   1 
HETATM 2912 O  O   . HOH   D 4 .   ? 8.279   1.876   86.131  1.00 45.66  ? 618 HOH   A O   1 
HETATM 2913 O  O   . HOH   D 4 .   ? 9.428   -12.646 49.082  1.00 61.35  ? 619 HOH   A O   1 
HETATM 2914 O  O   . HOH   D 4 .   ? -9.167  -24.155 66.070  1.00 45.91  ? 620 HOH   A O   1 
HETATM 2915 O  O   . HOH   D 4 .   ? -13.011 -14.066 68.614  1.00 40.46  ? 621 HOH   A O   1 
HETATM 2916 O  O   . HOH   D 4 .   ? -7.668  5.849   67.907  1.00 28.49  ? 622 HOH   A O   1 
HETATM 2917 O  O   . HOH   D 4 .   ? -0.615  -13.960 69.829  1.00 20.72  ? 623 HOH   A O   1 
HETATM 2918 O  O   . HOH   D 4 .   ? -6.284  -8.634  48.910  1.00 31.05  ? 624 HOH   A O   1 
HETATM 2919 O  O   . HOH   D 4 .   ? 12.739  -0.038  86.469  1.00 57.02  ? 625 HOH   A O   1 
HETATM 2920 O  O   . HOH   D 4 .   ? -6.027  -9.009  78.174  1.00 38.43  ? 626 HOH   A O   1 
HETATM 2921 O  O   . HOH   D 4 .   ? 3.709   3.400   49.618  1.00 72.01  ? 627 HOH   A O   1 
HETATM 2922 O  O   . HOH   D 4 .   ? 5.015   -1.048  80.278  1.00 32.57  ? 628 HOH   A O   1 
HETATM 2923 O  O   . HOH   D 4 .   ? 4.014   -16.895 58.423  1.00 31.96  ? 629 HOH   A O   1 
HETATM 2924 O  O   . HOH   D 4 .   ? -1.141  -21.076 85.882  1.00 41.55  ? 630 HOH   A O   1 
HETATM 2925 O  O   . HOH   D 4 .   ? 9.834   -0.532  66.217  1.00 25.21  ? 631 HOH   A O   1 
HETATM 2926 O  O   . HOH   D 4 .   ? 19.393  -0.302  79.222  1.00 44.20  ? 632 HOH   A O   1 
HETATM 2927 O  O   . HOH   D 4 .   ? 2.545   -14.711 57.087  1.00 30.99  ? 633 HOH   A O   1 
HETATM 2928 O  O   . HOH   D 4 .   ? -6.008  5.702   81.987  1.00 44.21  ? 634 HOH   A O   1 
HETATM 2929 O  O   . HOH   D 4 .   ? 26.478  -12.651 70.119  1.00 52.92  ? 635 HOH   A O   1 
HETATM 2930 O  O   . HOH   D 4 .   ? 6.412   -20.825 60.722  1.00 53.45  ? 636 HOH   A O   1 
HETATM 2931 O  O   . HOH   D 4 .   ? 13.270  0.783   75.112  1.00 34.40  ? 637 HOH   A O   1 
HETATM 2932 O  O   . HOH   D 4 .   ? -3.392  -24.365 47.976  1.00 32.58  ? 638 HOH   A O   1 
HETATM 2933 O  O   . HOH   D 4 .   ? -4.142  -9.684  80.485  1.00 38.05  ? 639 HOH   A O   1 
HETATM 2934 O  O   . HOH   D 4 .   ? 4.291   -17.944 61.047  1.00 24.30  ? 640 HOH   A O   1 
HETATM 2935 O  O   . HOH   D 4 .   ? 3.859   -22.201 74.934  1.00 54.82  ? 641 HOH   A O   1 
HETATM 2936 O  O   . HOH   D 4 .   ? -13.706 -13.866 74.177  1.00 32.02  ? 642 HOH   A O   1 
HETATM 2937 O  O   . HOH   D 4 .   ? 1.321   7.533   64.891  1.00 29.07  ? 643 HOH   A O   1 
HETATM 2938 O  O   . HOH   D 4 .   ? -2.017  -11.749 70.180  1.00 25.99  ? 644 HOH   A O   1 
HETATM 2939 O  O   . HOH   D 4 .   ? 1.856   -22.147 48.296  1.00 36.50  ? 645 HOH   A O   1 
HETATM 2940 O  O   . HOH   D 4 .   ? -2.471  -15.889 70.691  1.00 23.02  ? 646 HOH   A O   1 
HETATM 2941 O  O   . HOH   D 4 .   ? 19.618  -12.689 83.790  1.00 45.91  ? 647 HOH   A O   1 
HETATM 2942 O  O   . HOH   D 4 .   ? -2.318  -20.804 73.003  1.00 49.36  ? 648 HOH   A O   1 
HETATM 2943 O  O   . HOH   D 4 .   ? 26.430  -18.566 70.561  1.00 42.84  ? 649 HOH   A O   1 
HETATM 2944 O  O   . HOH   D 4 .   ? 15.836  -23.302 75.563  1.00 39.53  ? 650 HOH   A O   1 
HETATM 2945 O  O   . HOH   D 4 .   ? -1.034  -22.099 77.185  1.00 34.59  ? 651 HOH   A O   1 
HETATM 2946 O  O   . HOH   D 4 .   ? -2.159  5.371   54.431  1.00 40.95  ? 652 HOH   A O   1 
HETATM 2947 O  O   . HOH   D 4 .   ? 4.458   -12.854 44.955  1.00 38.57  ? 653 HOH   A O   1 
HETATM 2948 O  O   . HOH   D 4 .   ? 8.896   2.044   89.536  1.00 50.54  ? 654 HOH   A O   1 
HETATM 2949 O  O   . HOH   D 4 .   ? 21.706  -6.460  71.050  1.00 55.39  ? 655 HOH   A O   1 
HETATM 2950 O  O   . HOH   D 4 .   ? 13.786  -5.193  87.330  1.00 51.85  ? 656 HOH   A O   1 
HETATM 2951 O  O   . HOH   D 4 .   ? 10.696  13.705  71.851  1.00 39.25  ? 657 HOH   A O   1 
HETATM 2952 O  O   . HOH   D 4 .   ? -15.366 3.560   67.270  1.00 32.40  ? 658 HOH   A O   1 
HETATM 2953 O  O   . HOH   D 4 .   ? -9.675  -0.413  71.796  1.00 36.44  ? 659 HOH   A O   1 
HETATM 2954 O  O   . HOH   D 4 .   ? 1.494   13.870  59.438  1.00 62.63  ? 660 HOH   A O   1 
HETATM 2955 O  O   . HOH   D 4 .   ? -6.172  -1.654  51.772  1.00 35.75  ? 661 HOH   A O   1 
HETATM 2956 O  O   . HOH   D 4 .   ? 12.330  -8.593  85.334  1.00 48.91  ? 662 HOH   A O   1 
HETATM 2957 O  O   . HOH   D 4 .   ? -2.030  12.715  60.894  1.00 58.55  ? 663 HOH   A O   1 
HETATM 2958 O  O   . HOH   D 4 .   ? -1.064  14.083  58.915  1.00 43.12  ? 664 HOH   A O   1 
HETATM 2959 O  O   . HOH   D 4 .   ? 17.124  -2.897  84.695  1.00 57.62  ? 665 HOH   A O   1 
HETATM 2960 O  O   . HOH   D 4 .   ? 3.849   -22.272 66.187  1.00 40.65  ? 666 HOH   A O   1 
HETATM 2961 O  O   . HOH   D 4 .   ? 4.715   -21.009 68.052  1.00 34.30  ? 667 HOH   A O   1 
HETATM 2962 O  O   . HOH   D 4 .   ? 12.414  -0.623  68.003  1.00 32.64  ? 668 HOH   A O   1 
HETATM 2963 O  O   . HOH   D 4 .   ? -4.446  -12.423 70.756  1.00 34.23  ? 669 HOH   A O   1 
HETATM 2964 O  O   . HOH   D 4 .   ? 26.852  8.123   74.040  1.00 68.40  ? 670 HOH   A O   1 
HETATM 2965 O  O   . HOH   D 4 .   ? 2.054   -22.790 76.085  1.00 52.73  ? 671 HOH   A O   1 
HETATM 2966 O  O   . HOH   D 4 .   ? -2.859  -22.068 78.897  1.00 36.09  ? 672 HOH   A O   1 
HETATM 2967 O  O   . HOH   D 4 .   ? 1.291   -23.843 49.972  1.00 54.20  ? 673 HOH   A O   1 
HETATM 2968 O  O   . HOH   D 4 .   ? 1.776   -24.227 78.664  1.00 57.85  ? 674 HOH   A O   1 
# 
