data_8X6C
# 
_entry.id   8X6C 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8X6C         pdb_00008x6c 10.2210/pdb8x6c/pdb 
WWPDB D_1300042730 ?            ?                   
# 
_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       2024-11-27 
# 
_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                        8X6C 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 hylin@mail.ccnu.edu.cn          Lin Hong-Yan ? 'principal investigator/group leader' 0000-0002-5627-3708 
3 dongjin940520@mails.ccnu.edu.cn JIN DONG     ? 'principal investigator/group leader' 0000-0002-3605-5316 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yang, G.-F.' 1 ? 
'Lin, H.-Y.'  2 ? 
'Dong, J.'    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                     'Complex structure of AtHPPD with YH23024' 
_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 'Yang, G.-F.' 1 ? 
primary 'Lin, H.-Y.'  2 ? 
primary 'Dong, J.'    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 nat 
;7-[[2,6-bis(oxidanylidene)cyclohexylidene]-oxidanyl-methyl]-1,6-dimethyl-4-[[4-(trifluoromethyloxy)phenyl]methyl]-3~{H}-1,4-benzodiazepine-2,5-dione
;
516.466   1   ?          ? ? ? 
4 water       nat water 18.015    193 ?          ? ? ? 
# 
_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 
;7-[[2,6-bis(oxidanylidene)cyclohexylidene]-oxidanyl-methyl]-1,6-dimethyl-4-[[4-(trifluoromethyloxy)phenyl]methyl]-3~{H}-1,4-benzodiazepine-2,5-dione
;
YFM 
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 
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 
YFM non-polymer         . 
;7-[[2,6-bis(oxidanylidene)cyclohexylidene]-oxidanyl-methyl]-1,6-dimethyl-4-[[4-(trifluoromethyloxy)phenyl]methyl]-3~{H}-1,4-benzodiazepine-2,5-dione
;
? 'C26 H23 F3 N2 O6' 516.466 
# 
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 223 251 251 ALA ALA A . n 
A 1 224 GLU 224 252 252 GLU GLU 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 234 262 262 GLU GLU 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 YFM 1   502 501 YFM LIG A . 
D 4 HOH 1   601 162 HOH HOH A . 
D 4 HOH 2   602 97  HOH HOH A . 
D 4 HOH 3   603 137 HOH HOH A . 
D 4 HOH 4   604 40  HOH HOH A . 
D 4 HOH 5   605 135 HOH HOH A . 
D 4 HOH 6   606 140 HOH HOH A . 
D 4 HOH 7   607 29  HOH HOH A . 
D 4 HOH 8   608 36  HOH HOH A . 
D 4 HOH 9   609 67  HOH HOH A . 
D 4 HOH 10  610 58  HOH HOH A . 
D 4 HOH 11  611 179 HOH HOH A . 
D 4 HOH 12  612 114 HOH HOH A . 
D 4 HOH 13  613 106 HOH HOH A . 
D 4 HOH 14  614 81  HOH HOH A . 
D 4 HOH 15  615 115 HOH HOH A . 
D 4 HOH 16  616 160 HOH HOH A . 
D 4 HOH 17  617 79  HOH HOH A . 
D 4 HOH 18  618 126 HOH HOH A . 
D 4 HOH 19  619 117 HOH HOH A . 
D 4 HOH 20  620 187 HOH HOH A . 
D 4 HOH 21  621 71  HOH HOH A . 
D 4 HOH 22  622 94  HOH HOH A . 
D 4 HOH 23  623 101 HOH HOH A . 
D 4 HOH 24  624 8   HOH HOH A . 
D 4 HOH 25  625 13  HOH HOH A . 
D 4 HOH 26  626 1   HOH HOH A . 
D 4 HOH 27  627 133 HOH HOH A . 
D 4 HOH 28  628 116 HOH HOH A . 
D 4 HOH 29  629 7   HOH HOH A . 
D 4 HOH 30  630 109 HOH HOH A . 
D 4 HOH 31  631 131 HOH HOH A . 
D 4 HOH 32  632 45  HOH HOH A . 
D 4 HOH 33  633 39  HOH HOH A . 
D 4 HOH 34  634 21  HOH HOH A . 
D 4 HOH 35  635 61  HOH HOH A . 
D 4 HOH 36  636 24  HOH HOH A . 
D 4 HOH 37  637 28  HOH HOH A . 
D 4 HOH 38  638 27  HOH HOH A . 
D 4 HOH 39  639 124 HOH HOH A . 
D 4 HOH 40  640 174 HOH HOH A . 
D 4 HOH 41  641 104 HOH HOH A . 
D 4 HOH 42  642 46  HOH HOH A . 
D 4 HOH 43  643 14  HOH HOH A . 
D 4 HOH 44  644 17  HOH HOH A . 
D 4 HOH 45  645 173 HOH HOH A . 
D 4 HOH 46  646 43  HOH HOH A . 
D 4 HOH 47  647 142 HOH HOH A . 
D 4 HOH 48  648 70  HOH HOH A . 
D 4 HOH 49  649 4   HOH HOH A . 
D 4 HOH 50  650 9   HOH HOH A . 
D 4 HOH 51  651 74  HOH HOH A . 
D 4 HOH 52  652 16  HOH HOH A . 
D 4 HOH 53  653 75  HOH HOH A . 
D 4 HOH 54  654 164 HOH HOH A . 
D 4 HOH 55  655 92  HOH HOH A . 
D 4 HOH 56  656 82  HOH HOH A . 
D 4 HOH 57  657 93  HOH HOH A . 
D 4 HOH 58  658 165 HOH HOH A . 
D 4 HOH 59  659 38  HOH HOH A . 
D 4 HOH 60  660 122 HOH HOH A . 
D 4 HOH 61  661 72  HOH HOH A . 
D 4 HOH 62  662 91  HOH HOH A . 
D 4 HOH 63  663 153 HOH HOH A . 
D 4 HOH 64  664 35  HOH HOH A . 
D 4 HOH 65  665 182 HOH HOH A . 
D 4 HOH 66  666 138 HOH HOH A . 
D 4 HOH 67  667 129 HOH HOH A . 
D 4 HOH 68  668 18  HOH HOH A . 
D 4 HOH 69  669 186 HOH HOH A . 
D 4 HOH 70  670 191 HOH HOH A . 
D 4 HOH 71  671 68  HOH HOH A . 
D 4 HOH 72  672 169 HOH HOH A . 
D 4 HOH 73  673 15  HOH HOH A . 
D 4 HOH 74  674 132 HOH HOH A . 
D 4 HOH 75  675 103 HOH HOH A . 
D 4 HOH 76  676 77  HOH HOH A . 
D 4 HOH 77  677 171 HOH HOH A . 
D 4 HOH 78  678 96  HOH HOH A . 
D 4 HOH 79  679 134 HOH HOH A . 
D 4 HOH 80  680 12  HOH HOH A . 
D 4 HOH 81  681 136 HOH HOH A . 
D 4 HOH 82  682 69  HOH HOH A . 
D 4 HOH 83  683 80  HOH HOH A . 
D 4 HOH 84  684 121 HOH HOH A . 
D 4 HOH 85  685 52  HOH HOH A . 
D 4 HOH 86  686 89  HOH HOH A . 
D 4 HOH 87  687 88  HOH HOH A . 
D 4 HOH 88  688 34  HOH HOH A . 
D 4 HOH 89  689 31  HOH HOH A . 
D 4 HOH 90  690 32  HOH HOH A . 
D 4 HOH 91  691 107 HOH HOH A . 
D 4 HOH 92  692 11  HOH HOH A . 
D 4 HOH 93  693 23  HOH HOH A . 
D 4 HOH 94  694 83  HOH HOH A . 
D 4 HOH 95  695 47  HOH HOH A . 
D 4 HOH 96  696 143 HOH HOH A . 
D 4 HOH 97  697 44  HOH HOH A . 
D 4 HOH 98  698 78  HOH HOH A . 
D 4 HOH 99  699 190 HOH HOH A . 
D 4 HOH 100 700 19  HOH HOH A . 
D 4 HOH 101 701 59  HOH HOH A . 
D 4 HOH 102 702 98  HOH HOH A . 
D 4 HOH 103 703 85  HOH HOH A . 
D 4 HOH 104 704 2   HOH HOH A . 
D 4 HOH 105 705 111 HOH HOH A . 
D 4 HOH 106 706 87  HOH HOH A . 
D 4 HOH 107 707 5   HOH HOH A . 
D 4 HOH 108 708 50  HOH HOH A . 
D 4 HOH 109 709 175 HOH HOH A . 
D 4 HOH 110 710 166 HOH HOH A . 
D 4 HOH 111 711 48  HOH HOH A . 
D 4 HOH 112 712 41  HOH HOH A . 
D 4 HOH 113 713 25  HOH HOH A . 
D 4 HOH 114 714 42  HOH HOH A . 
D 4 HOH 115 715 86  HOH HOH A . 
D 4 HOH 116 716 56  HOH HOH A . 
D 4 HOH 117 717 37  HOH HOH A . 
D 4 HOH 118 718 156 HOH HOH A . 
D 4 HOH 119 719 105 HOH HOH A . 
D 4 HOH 120 720 146 HOH HOH A . 
D 4 HOH 121 721 64  HOH HOH A . 
D 4 HOH 122 722 145 HOH HOH A . 
D 4 HOH 123 723 128 HOH HOH A . 
D 4 HOH 124 724 100 HOH HOH A . 
D 4 HOH 125 725 123 HOH HOH A . 
D 4 HOH 126 726 151 HOH HOH A . 
D 4 HOH 127 727 120 HOH HOH A . 
D 4 HOH 128 728 84  HOH HOH A . 
D 4 HOH 129 729 55  HOH HOH A . 
D 4 HOH 130 730 130 HOH HOH A . 
D 4 HOH 131 731 22  HOH HOH A . 
D 4 HOH 132 732 53  HOH HOH A . 
D 4 HOH 133 733 49  HOH HOH A . 
D 4 HOH 134 734 26  HOH HOH A . 
D 4 HOH 135 735 139 HOH HOH A . 
D 4 HOH 136 736 65  HOH HOH A . 
D 4 HOH 137 737 3   HOH HOH A . 
D 4 HOH 138 738 20  HOH HOH A . 
D 4 HOH 139 739 73  HOH HOH A . 
D 4 HOH 140 740 33  HOH HOH A . 
D 4 HOH 141 741 10  HOH HOH A . 
D 4 HOH 142 742 178 HOH HOH A . 
D 4 HOH 143 743 30  HOH HOH A . 
D 4 HOH 144 744 183 HOH HOH A . 
D 4 HOH 145 745 51  HOH HOH A . 
D 4 HOH 146 746 63  HOH HOH A . 
D 4 HOH 147 747 144 HOH HOH A . 
D 4 HOH 148 748 99  HOH HOH A . 
D 4 HOH 149 749 158 HOH HOH A . 
D 4 HOH 150 750 60  HOH HOH A . 
D 4 HOH 151 751 181 HOH HOH A . 
D 4 HOH 152 752 66  HOH HOH A . 
D 4 HOH 153 753 102 HOH HOH A . 
D 4 HOH 154 754 154 HOH HOH A . 
D 4 HOH 155 755 6   HOH HOH A . 
D 4 HOH 156 756 149 HOH HOH A . 
D 4 HOH 157 757 177 HOH HOH A . 
D 4 HOH 158 758 176 HOH HOH A . 
D 4 HOH 159 759 159 HOH HOH A . 
D 4 HOH 160 760 152 HOH HOH A . 
D 4 HOH 161 761 127 HOH HOH A . 
D 4 HOH 162 762 168 HOH HOH A . 
D 4 HOH 163 763 113 HOH HOH A . 
D 4 HOH 164 764 161 HOH HOH A . 
D 4 HOH 165 765 147 HOH HOH A . 
D 4 HOH 166 766 108 HOH HOH A . 
D 4 HOH 167 767 185 HOH HOH A . 
D 4 HOH 168 768 150 HOH HOH A . 
D 4 HOH 169 769 110 HOH HOH A . 
D 4 HOH 170 770 54  HOH HOH A . 
D 4 HOH 171 771 163 HOH HOH A . 
D 4 HOH 172 772 125 HOH HOH A . 
D 4 HOH 173 773 57  HOH HOH A . 
D 4 HOH 174 774 112 HOH HOH A . 
D 4 HOH 175 775 62  HOH HOH A . 
D 4 HOH 176 776 167 HOH HOH A . 
D 4 HOH 177 777 76  HOH HOH A . 
D 4 HOH 178 778 180 HOH HOH A . 
D 4 HOH 179 779 184 HOH HOH A . 
D 4 HOH 180 780 141 HOH HOH A . 
D 4 HOH 181 781 155 HOH HOH A . 
D 4 HOH 182 782 148 HOH HOH A . 
D 4 HOH 183 783 192 HOH HOH A . 
D 4 HOH 184 784 188 HOH HOH A . 
D 4 HOH 185 785 119 HOH HOH A . 
D 4 HOH 186 786 189 HOH HOH A . 
D 4 HOH 187 787 118 HOH HOH A . 
D 4 HOH 188 788 157 HOH HOH A . 
D 4 HOH 189 789 95  HOH HOH A . 
D 4 HOH 190 790 170 HOH HOH A . 
D 4 HOH 191 791 172 HOH HOH A . 
D 4 HOH 192 792 90  HOH HOH A . 
D 4 HOH 193 793 193 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 LYS 193 ? CG  ? A LYS 165 CG  
10 1 Y 1 A LYS 193 ? CD  ? A LYS 165 CD  
11 1 Y 1 A LYS 193 ? CE  ? A LYS 165 CE  
12 1 Y 1 A LYS 193 ? NZ  ? A LYS 165 NZ  
13 1 Y 1 A GLU 201 ? CG  ? A GLU 173 CG  
14 1 Y 1 A GLU 201 ? CD  ? A GLU 173 CD  
15 1 Y 1 A GLU 201 ? OE1 ? A GLU 173 OE1 
16 1 Y 1 A GLU 201 ? OE2 ? A GLU 173 OE2 
17 1 Y 1 A GLU 210 ? CG  ? A GLU 182 CG  
18 1 Y 1 A GLU 210 ? CD  ? A GLU 182 CD  
19 1 Y 1 A GLU 210 ? OE1 ? A GLU 182 OE1 
20 1 Y 1 A GLU 210 ? OE2 ? A GLU 182 OE2 
21 1 Y 1 A GLU 262 ? CG  ? A GLU 234 CG  
22 1 Y 1 A GLU 262 ? CD  ? A GLU 234 CD  
23 1 Y 1 A GLU 262 ? OE1 ? A GLU 234 OE1 
24 1 Y 1 A GLU 262 ? OE2 ? A GLU 234 OE2 
25 1 Y 1 A ARG 290 ? CG  ? A ARG 262 CG  
26 1 Y 1 A ARG 290 ? CD  ? A ARG 262 CD  
27 1 Y 1 A ARG 290 ? NE  ? A ARG 262 NE  
28 1 Y 1 A ARG 290 ? CZ  ? A ARG 262 CZ  
29 1 Y 1 A ARG 290 ? NH1 ? A ARG 262 NH1 
30 1 Y 1 A ARG 290 ? NH2 ? A ARG 262 NH2 
31 1 Y 1 A GLN 344 ? CG  ? A GLN 316 CG  
32 1 Y 1 A GLN 344 ? CD  ? A GLN 316 CD  
33 1 Y 1 A GLN 344 ? OE1 ? A GLN 316 OE1 
34 1 Y 1 A GLN 344 ? NE2 ? A GLN 316 NE2 
35 1 Y 1 A LYS 347 ? CG  ? A LYS 319 CG  
36 1 Y 1 A LYS 347 ? CD  ? A LYS 319 CD  
37 1 Y 1 A LYS 347 ? CE  ? A LYS 319 CE  
38 1 Y 1 A LYS 347 ? NZ  ? A LYS 319 NZ  
39 1 Y 1 A LYS 348 ? CG  ? A LYS 320 CG  
40 1 Y 1 A LYS 348 ? CD  ? A LYS 320 CD  
41 1 Y 1 A LYS 348 ? CE  ? A LYS 320 CE  
42 1 Y 1 A LYS 348 ? NZ  ? A LYS 320 NZ  
43 1 Y 1 A LYS 360 ? CG  ? A LYS 332 CG  
44 1 Y 1 A LYS 360 ? CD  ? A LYS 332 CD  
45 1 Y 1 A LYS 360 ? CE  ? A LYS 332 CE  
46 1 Y 1 A LYS 360 ? NZ  ? A LYS 332 NZ  
47 1 Y 1 A GLN 374 ? CG  ? A GLN 346 CG  
48 1 Y 1 A GLN 374 ? CD  ? A GLN 346 CD  
49 1 Y 1 A GLN 374 ? OE1 ? A GLN 346 OE1 
50 1 Y 1 A GLN 374 ? NE2 ? A GLN 346 NE2 
51 1 Y 1 A TYR 411 ? CG  ? A TYR 383 CG  
52 1 Y 1 A TYR 411 ? CD1 ? A TYR 383 CD1 
53 1 Y 1 A TYR 411 ? CD2 ? A TYR 383 CD2 
54 1 Y 1 A TYR 411 ? CE1 ? A TYR 383 CE1 
55 1 Y 1 A TYR 411 ? CE2 ? A TYR 383 CE2 
56 1 Y 1 A TYR 411 ? CZ  ? A TYR 383 CZ  
57 1 Y 1 A TYR 411 ? OH  ? A TYR 383 OH  
58 1 Y 1 A PHE 428 ? CG  ? A PHE 400 CG  
59 1 Y 1 A PHE 428 ? CD1 ? A PHE 400 CD1 
60 1 Y 1 A PHE 428 ? CD2 ? A PHE 400 CD2 
61 1 Y 1 A PHE 428 ? CE1 ? A PHE 400 CE1 
62 1 Y 1 A PHE 428 ? CE2 ? A PHE 400 CE2 
63 1 Y 1 A PHE 428 ? CZ  ? A PHE 400 CZ  
64 1 Y 1 A GLU 432 ? CG  ? A GLU 404 CG  
65 1 Y 1 A GLU 432 ? CD  ? A GLU 404 CD  
66 1 Y 1 A GLU 432 ? OE1 ? A GLU 404 OE1 
67 1 Y 1 A GLU 432 ? OE2 ? A GLU 404 OE2 
68 1 Y 1 A GLU 435 ? CG  ? A GLU 407 CG  
69 1 Y 1 A GLU 435 ? CD  ? A GLU 407 CD  
70 1 Y 1 A GLU 435 ? OE1 ? A GLU 407 OE1 
71 1 Y 1 A GLU 435 ? OE2 ? A GLU 407 OE2 
72 1 Y 1 A LYS 436 ? CG  ? A LYS 408 CG  
73 1 Y 1 A LYS 436 ? CD  ? A LYS 408 CD  
74 1 Y 1 A LYS 436 ? CE  ? A LYS 408 CE  
75 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                   100.46 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8X6C 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.690 
_cell.length_a_esd                 ? 
_cell.length_b                     83.760 
_cell.length_b_esd                 ? 
_cell.length_c                     61.620 
_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                         8X6C 
_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                   8X6C 
_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             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.92 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.1M Tris/Bicine pH 8.5, 15% (v/v) MPD, 15% (w/v) PEG 1000, 15% (w/v) PEG 3350, 0.03M NaBr, 0.03M NaF, 0.03M NaI' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-04 
_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   0.9785 
_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        0.9785 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8X6C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.796 
_reflns.d_resolution_low                               34.991 
_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                                     35606 
_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                           96.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.92 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.57 
_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                                   0.999 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.90 
_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                             10898 
_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                                  0.841 
_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                                 8X6C 
_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                            1.796 
_refine.ls_d_res_low                             34.991 
_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                     35606 
_refine.ls_number_reflns_R_free                  1781 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.51 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1863 
_refine.ls_R_factor_R_free                       0.2115 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1850 
_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                 23.57 
_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                            0.19 
_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                       1.796 
_refine_hist.d_res_low                        34.991 
_refine_hist.number_atoms_solvent             193 
_refine_hist.number_atoms_total               3113 
_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        2882 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_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  ? 3011 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.159  ? 4083 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.106 ? 1778 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.056  ? 442  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 531  ? 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' 1.796  1.8442 . . 133 2531 97.00  . . . . 0.2690 . . . . . . . . . . . 0.2908 
'X-RAY DIFFRACTION' 1.8442 1.8984 . . 137 2596 100.00 . . . . 0.2381 . . . . . . . . . . . 0.2717 
'X-RAY DIFFRACTION' 1.8984 1.9597 . . 137 2612 100.00 . . . . 0.2156 . . . . . . . . . . . 0.2489 
'X-RAY DIFFRACTION' 1.9597 2.0297 . . 137 2597 100.00 . . . . 0.2095 . . . . . . . . . . . 0.2330 
'X-RAY DIFFRACTION' 2.0297 2.1110 . . 136 2593 100.00 . . . . 0.1992 . . . . . . . . . . . 0.2508 
'X-RAY DIFFRACTION' 2.1110 2.2070 . . 136 2582 100.00 . . . . 0.2022 . . . . . . . . . . . 0.2471 
'X-RAY DIFFRACTION' 2.2070 2.3234 . . 137 2594 100.00 . . . . 0.1975 . . . . . . . . . . . 0.2472 
'X-RAY DIFFRACTION' 2.3234 2.4689 . . 139 2641 100.00 . . . . 0.2004 . . . . . . . . . . . 0.2443 
'X-RAY DIFFRACTION' 2.4689 2.6595 . . 136 2576 100.00 . . . . 0.2042 . . . . . . . . . . . 0.2852 
'X-RAY DIFFRACTION' 2.6595 2.9270 . . 137 2610 100.00 . . . . 0.1966 . . . . . . . . . . . 0.2287 
'X-RAY DIFFRACTION' 2.9270 3.3503 . . 138 2628 100.00 . . . . 0.1866 . . . . . . . . . . . 0.2059 
'X-RAY DIFFRACTION' 3.3503 4.2198 . . 138 2613 100.00 . . . . 0.1560 . . . . . . . . . . . 0.1734 
'X-RAY DIFFRACTION' 4.2198 8      . . 140 2652 99.00  . . . . 0.1616 . . . . . . . . . . . 0.1640 
# 
_struct.entry_id                     8X6C 
_struct.title                        'Complex structure of AtHPPD with YH23024' 
_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        8X6C 
_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              8X6C 
_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 8X6C GLY A 1 ? UNP P93836 ? ? 'expression tag' 29 1 
1 8X6C SER A 2 ? UNP P93836 ? ? 'expression tag' 30 2 
1 8X6C HIS A 3 ? UNP P93836 ? ? 'expression tag' 31 3 
1 8X6C 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)' 3290  ? 
1 MORE         -14   ? 
1 'SSA (A^2)'  28190 ? 
# 
_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 -22.3741036548 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 121.1919844117 
# 
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 ILE A 84  ? THR A 88  ? ILE A 112 THR A 116 5 ? 5  
HELX_P HELX_P5  AA5 ASP A 96  ? GLY A 108 ? ASP A 124 GLY A 136 1 ? 13 
HELX_P HELX_P6  AA6 ASP A 120 ? ASN A 131 ? ASP A 148 ASN A 159 1 ? 12 
HELX_P HELX_P7  AA7 GLU A 205 ? GLY A 218 ? GLU A 233 GLY A 246 1 ? 14 
HELX_P HELX_P8  AA8 SER A 264 ? GLU A 274 ? SER A 292 GLU A 302 1 ? 11 
HELX_P HELX_P9  AA9 ASP A 287 ? SER A 299 ? ASP A 315 SER A 327 1 ? 13 
HELX_P HELX_P10 AB1 SER A 300 ? GLY A 302 ? SER A 328 GLY A 330 5 ? 3  
HELX_P HELX_P11 AB2 PRO A 311 ? ASN A 317 ? PRO A 339 ASN A 345 1 ? 7  
HELX_P HELX_P12 AB3 LEU A 318 ? GLY A 323 ? LEU A 346 GLY A 351 1 ? 6  
HELX_P HELX_P13 AB4 SER A 327 ? GLY A 338 ? SER A 355 GLY A 366 1 ? 12 
HELX_P HELX_P14 AB5 GLY A 394 ? GLU A 407 ? GLY A 422 GLU A 435 1 ? 14 
# 
_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 ? ? ? ? ? ? ? 2.336 ? ? 
metalc2 metalc ? ? A HIS 280 NE2 ? ? ? 1_555 B CO  .   CO  ? ? A HIS 308 A CO  501 1_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc3 metalc ? ? A GLU 366 OE1 ? ? ? 1_555 B CO  .   CO  ? ? A GLU 394 A CO  501 1_555 ? ? ? ? ? ? ? 2.148 ? ? 
metalc4 metalc ? ? B CO  .   CO  ? ? ? 1_555 C YFM .   O15 ? ? A CO  501 A YFM 502 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc5 metalc ? ? B CO  .   CO  ? ? ? 1_555 C YFM .   O22 ? ? A CO  501 A YFM 502 1_555 ? ? ? ? ? ? ? 2.162 ? ? 
metalc6 metalc ? ? B CO  .   CO  ? ? ? 1_555 D HOH .   O   ? ? A CO  501 A HOH 626 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
# 
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_555 100.5 ? 
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 97.9  ? 
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 85.5  ? 
4  NE2 ? A HIS 198 ? A HIS 226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O15 ? C YFM .   ? A YFM 502 ? 1_555 160.9 ? 
5  NE2 ? A HIS 280 ? A HIS 308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O15 ? C YFM .   ? A YFM 502 ? 1_555 90.9  ? 
6  OE1 ? A GLU 366 ? A GLU 394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O15 ? C YFM .   ? A YFM 502 ? 1_555 98.2  ? 
7  NE2 ? A HIS 198 ? A HIS 226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O22 ? C YFM .   ? A YFM 502 ? 1_555 87.8  ? 
8  NE2 ? A HIS 280 ? A HIS 308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O22 ? C YFM .   ? A YFM 502 ? 1_555 94.3  ? 
9  OE1 ? A GLU 366 ? A GLU 394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O22 ? C YFM .   ? A YFM 502 ? 1_555 174.2 ? 
10 O15 ? C YFM .   ? A YFM 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O22 ? C YFM .   ? A YFM 502 ? 1_555 76.0  ? 
11 NE2 ? A HIS 198 ? A HIS 226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH .   ? A HOH 626 ? 1_555 87.1  ? 
12 NE2 ? A HIS 280 ? A HIS 308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH .   ? A HOH 626 ? 1_555 168.5 ? 
13 OE1 ? A GLU 366 ? A GLU 394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH .   ? A HOH 626 ? 1_555 85.0  ? 
14 O15 ? C YFM .   ? A YFM 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH .   ? A HOH 626 ? 1_555 84.2  ? 
15 O22 ? C YFM .   ? A YFM 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH .   ? A HOH 626 ? 1_555 94.6  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       373 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      388 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       416 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PRO A 135 ? LEU A 142 ? PRO A 163 LEU A 170 
AA1 2 VAL A 146 ? TYR A 154 ? VAL A 174 TYR A 182 
AA1 3 VAL A 157 ? TYR A 164 ? VAL A 185 TYR A 192 
AA1 4 GLY A 110 ? VAL A 118 ? GLY A 138 VAL A 146 
AA1 5 VAL A 16  ? TRP A 25  ? VAL A 44  TRP A 53  
AA1 6 LEU A 67  ? PRO A 74  ? LEU A 95  PRO A 102 
AA1 7 HIS A 57  ? SER A 64  ? HIS A 85  SER A 92  
AA1 8 ARG A 43  ? SER A 48  ? ARG A 71  SER A 76  
AA1 9 GLU A 179 ? ARG A 180 ? GLU A 207 ARG A 208 
AA2 1 HIS A 220 ? GLN A 221 ? HIS A 248 GLN A 249 
AA2 2 LEU A 237 ? ALA A 243 ? LEU A 265 ALA A 271 
AA2 3 LEU A 250 ? PRO A 256 ? LEU A 278 PRO A 284 
AA2 4 ILE A 193 ? ASN A 202 ? ILE A 221 ASN A 230 
AA2 5 GLY A 277 ? SER A 285 ? GLY A 305 SER A 313 
AA2 6 PHE A 364 ? GLY A 372 ? PHE A 392 GLY A 400 
AA2 7 GLY A 347 ? PHE A 353 ? GLY A 375 PHE A 381 
AA2 8 LEU A 340 ? ARG A 343 ? LEU A 368 ARG A 371 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 142 ? N LEU A 170 O VAL A 146 ? O VAL A 174 
AA1 2 3 N ALA A 149 ? N ALA A 177 O TYR A 161 ? O TYR A 189 
AA1 3 4 O VAL A 162 ? O VAL A 190 N VAL A 118 ? N VAL A 146 
AA1 4 5 O GLU A 117 ? O GLU A 145 N LYS A 17  ? N LYS A 45  
AA1 5 6 N PHE A 24  ? N PHE A 52  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 SER A 59  ? O SER A 87  N SER A 48  ? N SER A 76  
AA1 8 9 N LYS A 47  ? N LYS A 75  O GLU A 179 ? O GLU A 207 
AA2 1 2 N HIS A 220 ? N HIS A 248 O ALA A 243 ? O ALA A 271 
AA2 2 3 N LEU A 242 ? N LEU A 270 O LEU A 251 ? O LEU A 279 
AA2 3 4 O ASN A 254 ? O ASN A 282 N GLY A 201 ? N GLY A 229 
AA2 4 5 N ASP A 197 ? N ASP A 225 O ALA A 282 ? O ALA A 310 
AA2 5 6 N LEU A 283 ? N LEU A 311 O GLU A 366 ? O GLU A 394 
AA2 6 7 O GLN A 369 ? O GLN A 397 N LEU A 350 ? N LEU A 378 
AA2 7 8 O LEU A 349 ? O LEU A 377 N ASP A 342 ? N ASP A 370 
# 
_pdbx_entry_details.entry_id                   8X6C 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 45  ? ? -104.02 -83.51  
2  1 ASP A 77  ? ? -163.95 -165.86 
3  1 ALA A 173 ? ? -131.22 -37.98  
4  1 LEU A 181 ? ? -101.91 -62.38  
5  1 PHE A 202 ? ? -57.56  -71.80  
6  1 ASP A 218 ? ? -164.89 113.67  
7  1 LYS A 289 ? ? 77.38   -66.13  
8  1 ASP A 315 ? ? -167.94 85.59   
9  1 VAL A 350 ? ? -140.06 15.31   
10 1 ASP A 372 ? ? -104.12 -164.53 
11 1 THR A 390 ? ? -117.74 -93.78  
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       793 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.84 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 PHE 253 ? A PHE 225 
14 1 Y 1 A THR 254 ? A THR 226 
15 1 Y 1 A ALA 255 ? A ALA 227 
16 1 Y 1 A ASP 256 ? A ASP 228 
17 1 Y 1 A ASP 257 ? A ASP 229 
18 1 Y 1 A VAL 258 ? A VAL 230 
19 1 Y 1 A GLY 259 ? A GLY 231 
20 1 Y 1 A THR 260 ? A THR 232 
21 1 Y 1 A ALA 261 ? A ALA 233 
22 1 Y 1 A LYS 404 ? A LYS 376 
23 1 Y 1 A ASP 405 ? A ASP 377 
24 1 Y 1 A GLU 406 ? A GLU 378 
25 1 Y 1 A GLU 407 ? A GLU 379 
26 1 Y 1 A GLY 408 ? A GLY 380 
27 1 Y 1 A LYS 409 ? A LYS 381 
28 1 Y 1 A ALA 410 ? A ALA 382 
29 1 Y 1 A THR 437 ? A THR 409 
30 1 Y 1 A LEU 438 ? A LEU 410 
31 1 Y 1 A GLU 439 ? A GLU 411 
32 1 Y 1 A ALA 440 ? A ALA 412 
33 1 Y 1 A LYS 441 ? A LYS 413 
34 1 Y 1 A GLN 442 ? A GLN 414 
35 1 Y 1 A LEU 443 ? A LEU 415 
36 1 Y 1 A VAL 444 ? A VAL 416 
37 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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CO  CO   CO N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
YFM C13  C  N N 392 
YFM C17  C  N N 393 
YFM C20  C  N N 394 
YFM C24  C  N N 395 
YFM C26  C  N N 396 
YFM C28  C  Y N 397 
YFM C01  C  Y N 398 
YFM C02  C  Y N 399 
YFM C03  C  Y N 400 
YFM C04  C  Y N 401 
YFM C05  C  Y N 402 
YFM C06  C  Y N 403 
YFM C08  C  N N 404 
YFM C09  C  N N 405 
YFM C11  C  N N 406 
YFM C12  C  N N 407 
YFM C14  C  N N 408 
YFM C16  C  N N 409 
YFM C18  C  N N 410 
YFM C19  C  N N 411 
YFM C27  C  Y N 412 
YFM C29  C  Y N 413 
YFM C30  C  Y N 414 
YFM C31  C  Y N 415 
YFM C32  C  Y N 416 
YFM C34  C  N N 417 
YFM F35  F  N N 418 
YFM F36  F  N N 419 
YFM F37  F  N N 420 
YFM N07  N  N N 421 
YFM N10  N  N N 422 
YFM O15  O  N N 423 
YFM O21  O  N N 424 
YFM O22  O  N N 425 
YFM O23  O  N N 426 
YFM O25  O  N N 427 
YFM O33  O  N N 428 
YFM H1   H  N N 429 
YFM H2   H  N N 430 
YFM H3   H  N N 431 
YFM H4   H  N N 432 
YFM H5   H  N N 433 
YFM H6   H  N N 434 
YFM H7   H  N N 435 
YFM H8   H  N N 436 
YFM H9   H  N N 437 
YFM H10  H  N N 438 
YFM H11  H  N N 439 
YFM H12  H  N N 440 
YFM H13  H  N N 441 
YFM H14  H  N N 442 
YFM H15  H  N N 443 
YFM H18  H  N N 444 
YFM H19  H  N N 445 
YFM H20  H  N N 446 
YFM H21  H  N N 447 
YFM H22  H  N N 448 
YFM H23  H  N N 449 
YFM H24  H  N N 450 
YFM H16  H  N N 451 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
YFM O22 C20  doub N N 376 
YFM O15 C13  sing N N 377 
YFM C12 C06  sing N N 378 
YFM C20 C19  sing N N 379 
YFM C20 C14  sing N N 380 
YFM C13 C14  doub N N 381 
YFM C13 C01  sing N N 382 
YFM C19 C18  sing N N 383 
YFM C14 C16  sing N N 384 
YFM O23 C11  doub N N 385 
YFM C06 C01  doub Y N 386 
YFM C06 C05  sing Y N 387 
YFM C01 C02  sing Y N 388 
YFM C11 C05  sing N N 389 
YFM C11 N10  sing N N 390 
YFM C05 C04  doub Y N 391 
YFM C16 O21  doub N N 392 
YFM C16 C17  sing N N 393 
YFM C24 N10  sing N N 394 
YFM C24 C27  sing N N 395 
YFM C02 C03  doub Y N 396 
YFM C18 C17  sing N N 397 
YFM N10 C09  sing N N 398 
YFM C04 C03  sing Y N 399 
YFM C04 N07  sing N N 400 
YFM C09 C08  sing N N 401 
YFM C27 C32  doub Y N 402 
YFM C27 C28  sing Y N 403 
YFM N07 C08  sing N N 404 
YFM N07 C26  sing N N 405 
YFM C32 C31  sing Y N 406 
YFM C08 O25  doub N N 407 
YFM C28 C29  doub Y N 408 
YFM C31 C30  doub Y N 409 
YFM C29 C30  sing Y N 410 
YFM C30 O33  sing N N 411 
YFM F35 C34  sing N N 412 
YFM O33 C34  sing N N 413 
YFM C34 F37  sing N N 414 
YFM C34 F36  sing N N 415 
YFM C17 H1   sing N N 416 
YFM C17 H2   sing N N 417 
YFM C24 H3   sing N N 418 
YFM C24 H4   sing N N 419 
YFM C26 H5   sing N N 420 
YFM C26 H6   sing N N 421 
YFM C26 H7   sing N N 422 
YFM C28 H8   sing N N 423 
YFM C02 H9   sing N N 424 
YFM C03 H10  sing N N 425 
YFM C09 H11  sing N N 426 
YFM C09 H12  sing N N 427 
YFM C12 H13  sing N N 428 
YFM C12 H14  sing N N 429 
YFM C12 H15  sing N N 430 
YFM C18 H18  sing N N 431 
YFM C18 H19  sing N N 432 
YFM C19 H20  sing N N 433 
YFM C19 H21  sing N N 434 
YFM C29 H22  sing N N 435 
YFM C31 H23  sing N N 436 
YFM C32 H24  sing N N 437 
YFM O15 H16  sing N N 438 
# 
_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                    8X6C 
_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]   0.013040 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002407 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011939 
_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]   0.016503 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CO 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS A 1 7   ? 23.491  -5.303  86.239  1.00 59.07 ? 35  LYS A N   1 
ATOM   2    C  CA  . LYS A 1 7   ? 24.520  -6.128  85.613  1.00 58.81 ? 35  LYS A CA  1 
ATOM   3    C  C   . LYS A 1 7   ? 24.054  -6.659  84.256  1.00 56.76 ? 35  LYS A C   1 
ATOM   4    O  O   . LYS A 1 7   ? 23.032  -7.345  84.162  1.00 56.82 ? 35  LYS A O   1 
ATOM   5    C  CB  . LYS A 1 7   ? 24.908  -7.290  86.532  1.00 63.72 ? 35  LYS A CB  1 
ATOM   6    N  N   . ASN A 1 8   ? 24.804  -6.330  83.206  1.00 50.82 ? 36  ASN A N   1 
ATOM   7    C  CA  . ASN A 1 8   ? 24.498  -6.765  81.842  1.00 48.27 ? 36  ASN A CA  1 
ATOM   8    C  C   . ASN A 1 8   ? 25.633  -7.654  81.365  1.00 45.16 ? 36  ASN A C   1 
ATOM   9    O  O   . ASN A 1 8   ? 26.649  -7.147  80.855  1.00 50.53 ? 36  ASN A O   1 
ATOM   10   C  CB  . ASN A 1 8   ? 24.312  -5.561  80.913  1.00 47.49 ? 36  ASN A CB  1 
ATOM   11   C  CG  . ASN A 1 8   ? 24.064  -5.953  79.448  1.00 44.52 ? 36  ASN A CG  1 
ATOM   12   O  OD1 . ASN A 1 8   ? 24.094  -7.131  79.077  1.00 43.09 ? 36  ASN A OD1 1 
ATOM   13   N  ND2 . ASN A 1 8   ? 23.802  -4.950  78.614  1.00 40.46 ? 36  ASN A ND2 1 
ATOM   14   N  N   . PRO A 1 9   ? 25.507  -8.979  81.486  1.00 45.58 ? 37  PRO A N   1 
ATOM   15   C  CA  . PRO A 1 9   ? 26.606  -9.874  81.095  1.00 46.08 ? 37  PRO A CA  1 
ATOM   16   C  C   . PRO A 1 9   ? 26.809  -9.986  79.593  1.00 45.18 ? 37  PRO A C   1 
ATOM   17   O  O   . PRO A 1 9   ? 27.758  -10.656 79.171  1.00 42.76 ? 37  PRO A O   1 
ATOM   18   C  CB  . PRO A 1 9   ? 26.184  -11.220 81.697  1.00 44.73 ? 37  PRO A CB  1 
ATOM   19   C  CG  . PRO A 1 9   ? 24.700  -11.155 81.720  1.00 46.58 ? 37  PRO A CG  1 
ATOM   20   C  CD  . PRO A 1 9   ? 24.343  -9.722  82.004  1.00 46.08 ? 37  PRO A CD  1 
ATOM   21   N  N   . LYS A 1 10  ? 25.951  -9.357  78.791  1.00 38.40 ? 38  LYS A N   1 
ATOM   22   C  CA  . LYS A 1 10  ? 26.083  -9.288  77.338  1.00 36.98 ? 38  LYS A CA  1 
ATOM   23   C  C   . LYS A 1 10  ? 26.337  -10.671 76.734  1.00 41.44 ? 38  LYS A C   1 
ATOM   24   O  O   . LYS A 1 10  ? 27.337  -10.916 76.055  1.00 40.51 ? 38  LYS A O   1 
ATOM   25   C  CB  . LYS A 1 10  ? 27.176  -8.291  76.946  1.00 41.03 ? 38  LYS A CB  1 
ATOM   26   C  CG  . LYS A 1 10  ? 26.934  -6.876  77.485  1.00 45.22 ? 38  LYS A CG  1 
ATOM   27   C  CD  . LYS A 1 10  ? 27.446  -5.810  76.523  1.00 45.49 ? 38  LYS A CD  1 
ATOM   28   C  CE  . LYS A 1 10  ? 26.784  -4.453  76.778  1.00 47.15 ? 38  LYS A CE  1 
ATOM   29   N  NZ  . LYS A 1 10  ? 27.557  -3.579  77.702  1.00 54.87 ? 38  LYS A NZ  1 
ATOM   30   N  N   . SER A 1 11  ? 25.381  -11.574 76.964  1.00 40.60 ? 39  SER A N   1 
ATOM   31   C  CA  . SER A 1 11  ? 25.555  -12.990 76.653  1.00 38.82 ? 39  SER A CA  1 
ATOM   32   C  C   . SER A 1 11  ? 24.766  -13.451 75.425  1.00 35.48 ? 39  SER A C   1 
ATOM   33   O  O   . SER A 1 11  ? 24.597  -14.661 75.236  1.00 34.53 ? 39  SER A O   1 
ATOM   34   C  CB  . SER A 1 11  ? 25.179  -13.840 77.868  1.00 37.10 ? 39  SER A CB  1 
ATOM   35   O  OG  . SER A 1 11  ? 23.921  -13.456 78.390  1.00 38.15 ? 39  SER A OG  1 
ATOM   36   N  N   . ASP A 1 12  ? 24.299  -12.522 74.580  1.00 33.65 ? 40  ASP A N   1 
ATOM   37   C  CA  . ASP A 1 12  ? 23.640  -12.883 73.319  1.00 35.17 ? 40  ASP A CA  1 
ATOM   38   C  C   . ASP A 1 12  ? 24.458  -13.913 72.555  1.00 37.03 ? 40  ASP A C   1 
ATOM   39   O  O   . ASP A 1 12  ? 25.658  -13.734 72.344  1.00 35.47 ? 40  ASP A O   1 
ATOM   40   C  CB  . ASP A 1 12  ? 23.450  -11.653 72.421  1.00 35.30 ? 40  ASP A CB  1 
ATOM   41   C  CG  . ASP A 1 12  ? 22.433  -10.677 72.958  1.00 31.11 ? 40  ASP A CG  1 
ATOM   42   O  OD1 . ASP A 1 12  ? 21.921  -10.894 74.073  1.00 31.57 ? 40  ASP A OD1 1 
ATOM   43   O  OD2 . ASP A 1 12  ? 22.175  -9.671  72.266  1.00 32.64 ? 40  ASP A OD2 1 
ATOM   44   N  N   . LYS A 1 13  ? 23.798  -14.978 72.114  1.00 32.38 ? 41  LYS A N   1 
ATOM   45   C  CA  . LYS A 1 13  ? 24.499  -16.025 71.389  1.00 34.95 ? 41  LYS A CA  1 
ATOM   46   C  C   . LYS A 1 13  ? 24.659  -15.703 69.909  1.00 38.15 ? 41  LYS A C   1 
ATOM   47   O  O   . LYS A 1 13  ? 25.384  -16.422 69.210  1.00 35.84 ? 41  LYS A O   1 
ATOM   48   C  CB  . LYS A 1 13  ? 23.776  -17.359 71.585  1.00 31.90 ? 41  LYS A CB  1 
ATOM   49   C  CG  . LYS A 1 13  ? 23.729  -17.820 73.044  1.00 30.01 ? 41  LYS A CG  1 
ATOM   50   C  CD  . LYS A 1 13  ? 22.995  -19.139 73.182  1.00 36.99 ? 41  LYS A CD  1 
ATOM   51   C  CE  . LYS A 1 13  ? 23.576  -19.985 74.310  1.00 41.31 ? 41  LYS A CE  1 
ATOM   52   N  NZ  . LYS A 1 13  ? 22.929  -19.750 75.623  1.00 45.16 ? 41  LYS A NZ  1 
ATOM   53   N  N   . PHE A 1 14  ? 24.010  -14.642 69.423  1.00 30.97 ? 42  PHE A N   1 
ATOM   54   C  CA  . PHE A 1 14  ? 24.178  -14.152 68.058  1.00 28.77 ? 42  PHE A CA  1 
ATOM   55   C  C   . PHE A 1 14  ? 23.959  -12.647 68.077  1.00 30.89 ? 42  PHE A C   1 
ATOM   56   O  O   . PHE A 1 14  ? 23.474  -12.095 69.063  1.00 37.04 ? 42  PHE A O   1 
ATOM   57   C  CB  . PHE A 1 14  ? 23.219  -14.848 67.083  1.00 34.97 ? 42  PHE A CB  1 
ATOM   58   C  CG  . PHE A 1 14  ? 21.829  -15.063 67.638  1.00 34.88 ? 42  PHE A CG  1 
ATOM   59   C  CD1 . PHE A 1 14  ? 20.839  -14.107 67.460  1.00 34.44 ? 42  PHE A CD1 1 
ATOM   60   C  CD2 . PHE A 1 14  ? 21.519  -16.222 68.335  1.00 31.88 ? 42  PHE A CD2 1 
ATOM   61   C  CE1 . PHE A 1 14  ? 19.565  -14.305 67.978  1.00 34.24 ? 42  PHE A CE1 1 
ATOM   62   C  CE2 . PHE A 1 14  ? 20.250  -16.433 68.862  1.00 33.16 ? 42  PHE A CE2 1 
ATOM   63   C  CZ  . PHE A 1 14  ? 19.265  -15.470 68.676  1.00 32.56 ? 42  PHE A CZ  1 
ATOM   64   N  N   . LYS A 1 15  ? 24.341  -11.974 66.988  1.00 27.45 ? 43  LYS A N   1 
ATOM   65   C  CA  . LYS A 1 15  ? 24.244  -10.519 66.924  1.00 30.71 ? 43  LYS A CA  1 
ATOM   66   C  C   . LYS A 1 15  ? 22.808  -10.108 66.593  1.00 30.90 ? 43  LYS A C   1 
ATOM   67   O  O   . LYS A 1 15  ? 22.305  -10.399 65.501  1.00 28.20 ? 43  LYS A O   1 
ATOM   68   C  CB  . LYS A 1 15  ? 25.211  -9.948  65.892  1.00 33.25 ? 43  LYS A CB  1 
ATOM   69   N  N   . VAL A 1 16  ? 22.173  -9.414  67.532  1.00 30.11 ? 44  VAL A N   1 
ATOM   70   C  CA  . VAL A 1 16  ? 20.806  -8.913  67.401  1.00 26.80 ? 44  VAL A CA  1 
ATOM   71   C  C   . VAL A 1 16  ? 20.890  -7.407  67.221  1.00 34.64 ? 44  VAL A C   1 
ATOM   72   O  O   . VAL A 1 16  ? 21.715  -6.747  67.865  1.00 36.38 ? 44  VAL A O   1 
ATOM   73   C  CB  . VAL A 1 16  ? 19.973  -9.291  68.642  1.00 28.50 ? 44  VAL A CB  1 
ATOM   74   C  CG1 . VAL A 1 16  ? 18.598  -8.580  68.639  1.00 29.43 ? 44  VAL A CG1 1 
ATOM   75   C  CG2 . VAL A 1 16  ? 19.829  -10.818 68.738  1.00 29.15 ? 44  VAL A CG2 1 
ATOM   76   N  N   . LYS A 1 17  ? 20.066  -6.864  66.324  1.00 28.78 ? 45  LYS A N   1 
ATOM   77   C  CA  . LYS A 1 17  ? 20.112  -5.428  66.078  1.00 31.09 ? 45  LYS A CA  1 
ATOM   78   C  C   . LYS A 1 17  ? 18.931  -4.724  66.742  1.00 34.37 ? 45  LYS A C   1 
ATOM   79   O  O   . LYS A 1 17  ? 19.066  -4.216  67.859  1.00 35.40 ? 45  LYS A O   1 
ATOM   80   C  CB  . LYS A 1 17  ? 20.182  -5.159  64.571  1.00 33.07 ? 45  LYS A CB  1 
ATOM   81   C  CG  . LYS A 1 17  ? 21.505  -5.647  63.965  1.00 36.59 ? 45  LYS A CG  1 
ATOM   82   C  CD  . LYS A 1 17  ? 21.522  -5.621  62.435  1.00 41.52 ? 45  LYS A CD  1 
ATOM   83   C  CE  . LYS A 1 17  ? 21.703  -4.213  61.879  1.00 46.66 ? 45  LYS A CE  1 
ATOM   84   N  NZ  . LYS A 1 17  ? 21.446  -4.138  60.398  1.00 47.87 ? 45  LYS A NZ  1 
ATOM   85   N  N   . ARG A 1 18  ? 17.769  -4.696  66.093  1.00 28.23 ? 46  ARG A N   1 
ATOM   86   C  CA  . ARG A 1 18  ? 16.604  -4.023  66.654  1.00 24.46 ? 46  ARG A CA  1 
ATOM   87   C  C   . ARG A 1 18  ? 15.363  -4.844  66.339  1.00 26.40 ? 46  ARG A C   1 
ATOM   88   O  O   . ARG A 1 18  ? 15.382  -5.735  65.488  1.00 27.80 ? 46  ARG A O   1 
ATOM   89   C  CB  . ARG A 1 18  ? 16.424  -2.603  66.092  1.00 30.63 ? 46  ARG A CB  1 
ATOM   90   C  CG  . ARG A 1 18  ? 17.490  -1.606  66.501  1.00 36.93 ? 46  ARG A CG  1 
ATOM   91   C  CD  . ARG A 1 18  ? 17.340  -1.226  67.962  1.00 35.98 ? 46  ARG A CD  1 
ATOM   92   N  NE  . ARG A 1 18  ? 18.385  -0.285  68.365  1.00 46.48 ? 46  ARG A NE  1 
ATOM   93   C  CZ  . ARG A 1 18  ? 19.599  -0.649  68.776  1.00 42.13 ? 46  ARG A CZ  1 
ATOM   94   N  NH1 . ARG A 1 18  ? 19.922  -1.936  68.844  1.00 37.23 ? 46  ARG A NH1 1 
ATOM   95   N  NH2 . ARG A 1 18  ? 20.489  0.276   69.129  1.00 48.13 ? 46  ARG A NH2 1 
ATOM   96   N  N   . PHE A 1 19  ? 14.283  -4.540  67.050  1.00 23.63 ? 47  PHE A N   1 
ATOM   97   C  CA  . PHE A 1 19  ? 12.966  -4.980  66.600  1.00 23.16 ? 47  PHE A CA  1 
ATOM   98   C  C   . PHE A 1 19  ? 12.786  -4.574  65.148  1.00 22.10 ? 47  PHE A C   1 
ATOM   99   O  O   . PHE A 1 19  ? 13.144  -3.460  64.756  1.00 25.55 ? 47  PHE A O   1 
ATOM   100  C  CB  . PHE A 1 19  ? 11.874  -4.350  67.455  1.00 22.00 ? 47  PHE A CB  1 
ATOM   101  C  CG  . PHE A 1 19  ? 11.643  -5.037  68.774  1.00 19.71 ? 47  PHE A CG  1 
ATOM   102  C  CD1 . PHE A 1 19  ? 11.305  -6.383  68.822  1.00 20.53 ? 47  PHE A CD1 1 
ATOM   103  C  CD2 . PHE A 1 19  ? 11.697  -4.323  69.964  1.00 21.41 ? 47  PHE A CD2 1 
ATOM   104  C  CE1 . PHE A 1 19  ? 11.061  -7.002  70.020  1.00 21.53 ? 47  PHE A CE1 1 
ATOM   105  C  CE2 . PHE A 1 19  ? 11.450  -4.962  71.178  1.00 19.45 ? 47  PHE A CE2 1 
ATOM   106  C  CZ  . PHE A 1 19  ? 11.126  -6.289  71.195  1.00 17.58 ? 47  PHE A CZ  1 
ATOM   107  N  N   . HIS A 1 20  ? 12.264  -5.494  64.338  1.00 21.93 ? 48  HIS A N   1 
ATOM   108  C  CA  . HIS A 1 20  ? 12.062  -5.221  62.922  1.00 21.71 ? 48  HIS A CA  1 
ATOM   109  C  C   . HIS A 1 20  ? 10.599  -4.991  62.570  1.00 26.30 ? 48  HIS A C   1 
ATOM   110  O  O   . HIS A 1 20  ? 10.260  -3.981  61.947  1.00 25.75 ? 48  HIS A O   1 
ATOM   111  C  CB  . HIS A 1 20  ? 12.631  -6.357  62.064  1.00 24.96 ? 48  HIS A CB  1 
ATOM   112  C  CG  . HIS A 1 20  ? 12.693  -6.017  60.610  1.00 23.57 ? 48  HIS A CG  1 
ATOM   113  N  ND1 . HIS A 1 20  ? 11.722  -6.400  59.710  1.00 27.49 ? 48  HIS A ND1 1 
ATOM   114  C  CD2 . HIS A 1 20  ? 13.578  -5.268  59.910  1.00 33.00 ? 48  HIS A CD2 1 
ATOM   115  C  CE1 . HIS A 1 20  ? 12.022  -5.934  58.511  1.00 33.02 ? 48  HIS A CE1 1 
ATOM   116  N  NE2 . HIS A 1 20  ? 13.146  -5.242  58.605  1.00 35.85 ? 48  HIS A NE2 1 
ATOM   117  N  N   . HIS A 1 21  ? 9.722   -5.920  62.929  1.00 23.00 ? 49  HIS A N   1 
ATOM   118  C  CA  . HIS A 1 21  ? 8.302   -5.759  62.634  1.00 23.83 ? 49  HIS A CA  1 
ATOM   119  C  C   . HIS A 1 21  ? 7.523   -6.718  63.513  1.00 22.35 ? 49  HIS A C   1 
ATOM   120  O  O   . HIS A 1 21  ? 8.083   -7.625  64.135  1.00 19.32 ? 49  HIS A O   1 
ATOM   121  C  CB  . HIS A 1 21  ? 7.987   -5.986  61.147  1.00 22.11 ? 49  HIS A CB  1 
ATOM   122  C  CG  . HIS A 1 21  ? 8.184   -7.395  60.671  1.00 21.02 ? 49  HIS A CG  1 
ATOM   123  N  ND1 . HIS A 1 21  ? 9.371   -7.844  60.132  1.00 21.09 ? 49  HIS A ND1 1 
ATOM   124  C  CD2 . HIS A 1 21  ? 7.326   -8.444  60.615  1.00 24.23 ? 49  HIS A CD2 1 
ATOM   125  C  CE1 . HIS A 1 21  ? 9.240   -9.108  59.769  1.00 22.21 ? 49  HIS A CE1 1 
ATOM   126  N  NE2 . HIS A 1 21  ? 8.012   -9.500  60.060  1.00 22.80 ? 49  HIS A NE2 1 
ATOM   127  N  N   . ILE A 1 22  ? 6.213   -6.474  63.582  1.00 18.25 ? 50  ILE A N   1 
ATOM   128  C  CA  . ILE A 1 22  ? 5.272   -7.334  64.283  1.00 21.93 ? 50  ILE A CA  1 
ATOM   129  C  C   . ILE A 1 22  ? 4.244   -7.768  63.251  1.00 19.36 ? 50  ILE A C   1 
ATOM   130  O  O   . ILE A 1 22  ? 3.729   -6.921  62.516  1.00 20.15 ? 50  ILE A O   1 
ATOM   131  C  CB  . ILE A 1 22  ? 4.593   -6.568  65.439  1.00 24.72 ? 50  ILE A CB  1 
ATOM   132  C  CG1 . ILE A 1 22  ? 5.624   -6.154  66.489  1.00 23.16 ? 50  ILE A CG1 1 
ATOM   133  C  CG2 . ILE A 1 22  ? 3.409   -7.376  66.023  1.00 20.24 ? 50  ILE A CG2 1 
ATOM   134  C  CD1 . ILE A 1 22  ? 6.207   -7.337  67.280  1.00 20.20 ? 50  ILE A CD1 1 
ATOM   135  N  N   . GLU A 1 23  ? 3.942   -9.073  63.186  1.00 19.43 ? 51  GLU A N   1 
ATOM   136  C  CA  . GLU A 1 23  ? 2.954   -9.578  62.232  1.00 19.64 ? 51  GLU A CA  1 
ATOM   137  C  C   . GLU A 1 23  ? 1.702   -10.098 62.940  1.00 21.32 ? 51  GLU A C   1 
ATOM   138  O  O   . GLU A 1 23  ? 1.769   -11.024 63.765  1.00 21.15 ? 51  GLU A O   1 
ATOM   139  C  CB  . GLU A 1 23  ? 3.521   -10.676 61.325  1.00 18.96 ? 51  GLU A CB  1 
ATOM   140  C  CG  . GLU A 1 23  ? 2.452   -11.140 60.329  1.00 18.63 ? 51  GLU A CG  1 
ATOM   141  C  CD  . GLU A 1 23  ? 2.983   -12.164 59.345  1.00 25.01 ? 51  GLU A CD  1 
ATOM   142  O  OE1 . GLU A 1 23  ? 4.073   -12.705 59.620  1.00 24.92 ? 51  GLU A OE1 1 
ATOM   143  O  OE2 . GLU A 1 23  ? 2.311   -12.441 58.324  1.00 22.43 ? 51  GLU A OE2 1 
ATOM   144  N  N   . PHE A 1 24  ? 0.562   -9.519  62.574  1.00 18.36 ? 52  PHE A N   1 
ATOM   145  C  CA  . PHE A 1 24  ? -0.753  -9.962  63.008  1.00 18.10 ? 52  PHE A CA  1 
ATOM   146  C  C   . PHE A 1 24  ? -1.286  -10.979 62.011  1.00 19.14 ? 52  PHE A C   1 
ATOM   147  O  O   . PHE A 1 24  ? -1.233  -10.748 60.794  1.00 17.32 ? 52  PHE A O   1 
ATOM   148  C  CB  . PHE A 1 24  ? -1.719  -8.766  63.096  1.00 17.42 ? 52  PHE A CB  1 
ATOM   149  C  CG  . PHE A 1 24  ? -1.393  -7.795  64.199  1.00 17.43 ? 52  PHE A CG  1 
ATOM   150  C  CD1 . PHE A 1 24  ? -0.492  -6.760  64.005  1.00 20.26 ? 52  PHE A CD1 1 
ATOM   151  C  CD2 . PHE A 1 24  ? -1.981  -7.936  65.451  1.00 22.99 ? 52  PHE A CD2 1 
ATOM   152  C  CE1 . PHE A 1 24  ? -0.182  -5.876  65.040  1.00 21.51 ? 52  PHE A CE1 1 
ATOM   153  C  CE2 . PHE A 1 24  ? -1.675  -7.042  66.484  1.00 23.92 ? 52  PHE A CE2 1 
ATOM   154  C  CZ  . PHE A 1 24  ? -0.773  -6.030  66.278  1.00 20.16 ? 52  PHE A CZ  1 
ATOM   155  N  N   . TRP A 1 25  ? -1.812  -12.092 62.520  1.00 18.13 ? 53  TRP A N   1 
ATOM   156  C  CA  . TRP A 1 25  ? -2.563  -13.022 61.692  1.00 16.96 ? 53  TRP A CA  1 
ATOM   157  C  C   . TRP A 1 25  ? -4.048  -12.730 61.858  1.00 19.89 ? 53  TRP A C   1 
ATOM   158  O  O   . TRP A 1 25  ? -4.549  -12.602 62.982  1.00 16.96 ? 53  TRP A O   1 
ATOM   159  C  CB  . TRP A 1 25  ? -2.226  -14.475 62.033  1.00 21.33 ? 53  TRP A CB  1 
ATOM   160  C  CG  . TRP A 1 25  ? -1.139  -14.975 61.149  1.00 22.02 ? 53  TRP A CG  1 
ATOM   161  C  CD1 . TRP A 1 25  ? -0.481  -14.282 60.162  1.00 23.36 ? 53  TRP A CD1 1 
ATOM   162  C  CD2 . TRP A 1 25  ? -0.579  -16.287 61.157  1.00 24.01 ? 53  TRP A CD2 1 
ATOM   163  N  NE1 . TRP A 1 25  ? 0.448   -15.095 59.550  1.00 22.51 ? 53  TRP A NE1 1 
ATOM   164  C  CE2 . TRP A 1 25  ? 0.418   -16.328 60.149  1.00 22.87 ? 53  TRP A CE2 1 
ATOM   165  C  CE3 . TRP A 1 25  ? -0.810  -17.424 61.930  1.00 20.46 ? 53  TRP A CE3 1 
ATOM   166  C  CZ2 . TRP A 1 25  ? 1.176   -17.487 59.883  1.00 24.88 ? 53  TRP A CZ2 1 
ATOM   167  C  CZ3 . TRP A 1 25  ? -0.029  -18.579 61.678  1.00 21.49 ? 53  TRP A CZ3 1 
ATOM   168  C  CH2 . TRP A 1 25  ? 0.918   -18.597 60.651  1.00 22.60 ? 53  TRP A CH2 1 
ATOM   169  N  N   . CYS A 1 26  ? -4.724  -12.556 60.735  1.00 20.38 ? 54  CYS A N   1 
ATOM   170  C  CA  . CYS A 1 26  ? -6.047  -11.942 60.677  1.00 16.69 ? 54  CYS A CA  1 
ATOM   171  C  C   . CYS A 1 26  ? -6.988  -12.849 59.912  1.00 18.57 ? 54  CYS A C   1 
ATOM   172  O  O   . CYS A 1 26  ? -6.555  -13.743 59.177  1.00 22.37 ? 54  CYS A O   1 
ATOM   173  C  CB  . CYS A 1 26  ? -6.016  -10.580 59.953  1.00 16.27 ? 54  CYS A CB  1 
ATOM   174  S  SG  . CYS A 1 26  ? -4.860  -9.386  60.594  1.00 23.87 ? 54  CYS A SG  1 
ATOM   175  N  N   . GLY A 1 27  ? -8.284  -12.539 60.018  1.00 20.07 ? 55  GLY A N   1 
ATOM   176  C  CA  . GLY A 1 27  ? -9.219  -13.200 59.137  1.00 21.92 ? 55  GLY A CA  1 
ATOM   177  C  C   . GLY A 1 27  ? -9.318  -12.412 57.846  1.00 25.34 ? 55  GLY A C   1 
ATOM   178  O  O   . GLY A 1 27  ? -9.357  -12.986 56.746  1.00 22.66 ? 55  GLY A O   1 
ATOM   179  N  N   . ASP A 1 28  ? -9.421  -11.085 57.984  1.00 24.23 ? 56  ASP A N   1 
ATOM   180  C  CA  . ASP A 1 28  ? -9.409  -10.154 56.856  1.00 17.43 ? 56  ASP A CA  1 
ATOM   181  C  C   . ASP A 1 28  ? -8.349  -9.095  57.141  1.00 19.53 ? 56  ASP A C   1 
ATOM   182  O  O   . ASP A 1 28  ? -8.554  -8.227  57.999  1.00 21.32 ? 56  ASP A O   1 
ATOM   183  C  CB  . ASP A 1 28  ? -10.778 -9.498  56.642  1.00 18.06 ? 56  ASP A CB  1 
ATOM   184  C  CG  . ASP A 1 28  ? -10.805 -8.655  55.389  1.00 19.41 ? 56  ASP A CG  1 
ATOM   185  O  OD1 . ASP A 1 28  ? -11.009 -9.236  54.306  1.00 20.38 ? 56  ASP A OD1 1 
ATOM   186  O  OD2 . ASP A 1 28  ? -10.512 -7.437  55.463  1.00 20.78 ? 56  ASP A OD2 1 
ATOM   187  N  N   . ALA A 1 29  ? -7.226  -9.153  56.418  1.00 18.17 ? 57  ALA A N   1 
ATOM   188  C  CA  . ALA A 1 29  ? -6.134  -8.218  56.691  1.00 18.17 ? 57  ALA A CA  1 
ATOM   189  C  C   . ALA A 1 29  ? -6.495  -6.786  56.313  1.00 19.05 ? 57  ALA A C   1 
ATOM   190  O  O   . ALA A 1 29  ? -6.007  -5.844  56.954  1.00 20.11 ? 57  ALA A O   1 
ATOM   191  C  CB  . ALA A 1 29  ? -4.871  -8.645  55.950  1.00 23.18 ? 57  ALA A CB  1 
ATOM   192  N  N   . THR A 1 30  ? -7.301  -6.611  55.265  1.00 21.81 ? 58  THR A N   1 
ATOM   193  C  CA  . THR A 1 30  ? -7.669  -5.277  54.790  1.00 19.76 ? 58  THR A CA  1 
ATOM   194  C  C   . THR A 1 30  ? -8.353  -4.477  55.892  1.00 20.31 ? 58  THR A C   1 
ATOM   195  O  O   . THR A 1 30  ? -7.965  -3.337  56.179  1.00 20.59 ? 58  THR A O   1 
ATOM   196  C  CB  . THR A 1 30  ? -8.581  -5.391  53.560  1.00 23.83 ? 58  THR A CB  1 
ATOM   197  O  OG1 . THR A 1 30  ? -7.828  -5.869  52.432  1.00 22.41 ? 58  THR A OG1 1 
ATOM   198  C  CG2 . THR A 1 30  ? -9.234  -4.023  53.214  1.00 22.04 ? 58  THR A CG2 1 
ATOM   199  N  N   . ASN A 1 31  ? -9.377  -5.064  56.531  1.00 19.51 ? 59  ASN A N   1 
ATOM   200  C  CA  . ASN A 1 31  ? -10.151 -4.304  57.517  1.00 20.48 ? 59  ASN A CA  1 
ATOM   201  C  C   . ASN A 1 31  ? -9.350  -4.055  58.790  1.00 21.62 ? 59  ASN A C   1 
ATOM   202  O  O   . ASN A 1 31  ? -9.444  -2.979  59.385  1.00 18.82 ? 59  ASN A O   1 
ATOM   203  C  CB  . ASN A 1 31  ? -11.479 -4.998  57.828  1.00 21.03 ? 59  ASN A CB  1 
ATOM   204  C  CG  . ASN A 1 31  ? -12.537 -4.667  56.804  1.00 18.82 ? 59  ASN A CG  1 
ATOM   205  O  OD1 . ASN A 1 31  ? -13.297 -3.697  56.957  1.00 16.04 ? 59  ASN A OD1 1 
ATOM   206  N  ND2 . ASN A 1 31  ? -12.533 -5.406  55.703  1.00 19.29 ? 59  ASN A ND2 1 
ATOM   207  N  N   . VAL A 1 32  ? -8.558  -5.024  59.236  1.00 17.60 ? 60  VAL A N   1 
ATOM   208  C  CA  . VAL A 1 32  ? -7.734  -4.775  60.416  1.00 17.48 ? 60  VAL A CA  1 
ATOM   209  C  C   . VAL A 1 32  ? -6.720  -3.685  60.122  1.00 18.17 ? 60  VAL A C   1 
ATOM   210  O  O   . VAL A 1 32  ? -6.543  -2.753  60.918  1.00 17.50 ? 60  VAL A O   1 
ATOM   211  C  CB  . VAL A 1 32  ? -7.030  -6.057  60.892  1.00 19.95 ? 60  VAL A CB  1 
ATOM   212  C  CG1 . VAL A 1 32  ? -6.166  -5.728  62.103  1.00 17.89 ? 60  VAL A CG1 1 
ATOM   213  C  CG2 . VAL A 1 32  ? -8.062  -7.118  61.234  1.00 21.35 ? 60  VAL A CG2 1 
ATOM   214  N  N   . ALA A 1 33  ? -6.054  -3.769  58.959  1.00 16.63 ? 61  ALA A N   1 
ATOM   215  C  CA  . ALA A 1 33  ? -5.005  -2.793  58.660  1.00 19.87 ? 61  ALA A CA  1 
ATOM   216  C  C   . ALA A 1 33  ? -5.585  -1.393  58.504  1.00 21.71 ? 61  ALA A C   1 
ATOM   217  O  O   . ALA A 1 33  ? -4.966  -0.413  58.928  1.00 19.56 ? 61  ALA A O   1 
ATOM   218  C  CB  . ALA A 1 33  ? -4.235  -3.196  57.400  1.00 21.10 ? 61  ALA A CB  1 
ATOM   219  N  N   . ARG A 1 34  ? -6.769  -1.266  57.894  1.00 18.52 ? 62  ARG A N   1 
ATOM   220  C  CA  . ARG A 1 34  ? -7.342  0.075   57.749  1.00 17.08 ? 62  ARG A CA  1 
ATOM   221  C  C   . ARG A 1 34  ? -7.713  0.666   59.104  1.00 22.40 ? 62  ARG A C   1 
ATOM   222  O  O   . ARG A 1 34  ? -7.466  1.867   59.359  1.00 20.06 ? 62  ARG A O   1 
ATOM   223  C  CB  . ARG A 1 34  ? -8.546  0.045   56.817  1.00 19.74 ? 62  ARG A CB  1 
ATOM   224  C  CG  . ARG A 1 34  ? -8.121  -0.279  55.398  1.00 25.69 ? 62  ARG A CG  1 
ATOM   225  C  CD  . ARG A 1 34  ? -8.801  0.519   54.340  1.00 26.62 ? 62  ARG A CD  1 
ATOM   226  N  NE  . ARG A 1 34  ? -8.128  0.310   53.066  1.00 24.95 ? 62  ARG A NE  1 
ATOM   227  C  CZ  . ARG A 1 34  ? -8.374  1.006   51.959  1.00 29.01 ? 62  ARG A CZ  1 
ATOM   228  N  NH1 . ARG A 1 34  ? -7.682  0.754   50.853  1.00 27.22 ? 62  ARG A NH1 1 
ATOM   229  N  NH2 . ARG A 1 34  ? -9.327  1.934   51.947  1.00 27.54 ? 62  ARG A NH2 1 
ATOM   230  N  N   . ARG A 1 35  ? -8.292  -0.162  59.981  1.00 16.74 ? 63  ARG A N   1 
ATOM   231  C  CA  . ARG A 1 35  ? -8.635  0.272   61.334  1.00 17.57 ? 63  ARG A CA  1 
ATOM   232  C  C   . ARG A 1 35  ? -7.394  0.723   62.089  1.00 19.15 ? 63  ARG A C   1 
ATOM   233  O  O   . ARG A 1 35  ? -7.387  1.796   62.701  1.00 18.14 ? 63  ARG A O   1 
ATOM   234  C  CB  . ARG A 1 35  ? -9.344  -0.867  62.086  1.00 17.20 ? 63  ARG A CB  1 
ATOM   235  C  CG  . ARG A 1 35  ? -10.137 -0.497  63.376  1.00 16.96 ? 63  ARG A CG  1 
ATOM   236  C  CD  . ARG A 1 35  ? -9.208  -0.229  64.532  1.00 18.44 ? 63  ARG A CD  1 
ATOM   237  N  NE  . ARG A 1 35  ? -9.846  0.017   65.824  1.00 19.91 ? 63  ARG A NE  1 
ATOM   238  C  CZ  . ARG A 1 35  ? -9.947  -0.885  66.789  1.00 18.63 ? 63  ARG A CZ  1 
ATOM   239  N  NH1 . ARG A 1 35  ? -10.514 -0.558  67.940  1.00 23.04 ? 63  ARG A NH1 1 
ATOM   240  N  NH2 . ARG A 1 35  ? -9.504  -2.128  66.594  1.00 19.38 ? 63  ARG A NH2 1 
ATOM   241  N  N   . PHE A 1 36  ? -6.352  -0.117  62.109  1.00 16.00 ? 64  PHE A N   1 
ATOM   242  C  CA  . PHE A 1 36  ? -5.124  0.240   62.821  1.00 17.00 ? 64  PHE A CA  1 
ATOM   243  C  C   . PHE A 1 36  ? -4.488  1.495   62.245  1.00 19.22 ? 64  PHE A C   1 
ATOM   244  O  O   . PHE A 1 36  ? -3.956  2.324   62.990  1.00 18.81 ? 64  PHE A O   1 
ATOM   245  C  CB  . PHE A 1 36  ? -4.112  -0.916  62.764  1.00 16.18 ? 64  PHE A CB  1 
ATOM   246  C  CG  . PHE A 1 36  ? -4.311  -1.972  63.835  1.00 17.45 ? 64  PHE A CG  1 
ATOM   247  C  CD1 . PHE A 1 36  ? -5.533  -2.637  63.959  1.00 18.26 ? 64  PHE A CD1 1 
ATOM   248  C  CD2 . PHE A 1 36  ? -3.259  -2.328  64.674  1.00 18.05 ? 64  PHE A CD2 1 
ATOM   249  C  CE1 . PHE A 1 36  ? -5.727  -3.607  64.943  1.00 19.64 ? 64  PHE A CE1 1 
ATOM   250  C  CE2 . PHE A 1 36  ? -3.427  -3.315  65.654  1.00 20.85 ? 64  PHE A CE2 1 
ATOM   251  C  CZ  . PHE A 1 36  ? -4.678  -3.974  65.767  1.00 19.13 ? 64  PHE A CZ  1 
ATOM   252  N  N   . SER A 1 37  ? -4.481  1.624   60.916  1.00 17.88 ? 65  SER A N   1 
ATOM   253  C  CA  . SER A 1 37  ? -3.878  2.791   60.283  1.00 20.42 ? 65  SER A CA  1 
ATOM   254  C  C   . SER A 1 37  ? -4.507  4.078   60.801  1.00 20.16 ? 65  SER A C   1 
ATOM   255  O  O   . SER A 1 37  ? -3.808  4.991   61.257  1.00 19.88 ? 65  SER A O   1 
ATOM   256  C  CB  . SER A 1 37  ? -4.034  2.685   58.765  1.00 20.53 ? 65  SER A CB  1 
ATOM   257  O  OG  . SER A 1 37  ? -3.598  3.888   58.124  1.00 22.63 ? 65  SER A OG  1 
ATOM   258  N  N   . TRP A 1 38  ? -5.838  4.147   60.773  1.00 18.42 ? 66  TRP A N   1 
ATOM   259  C  CA  . TRP A 1 38  ? -6.541  5.321   61.263  1.00 21.48 ? 66  TRP A CA  1 
ATOM   260  C  C   . TRP A 1 38  ? -6.379  5.498   62.767  1.00 20.87 ? 66  TRP A C   1 
ATOM   261  O  O   . TRP A 1 38  ? -6.147  6.624   63.244  1.00 20.03 ? 66  TRP A O   1 
ATOM   262  C  CB  . TRP A 1 38  ? -8.014  5.192   60.893  1.00 16.60 ? 66  TRP A CB  1 
ATOM   263  C  CG  . TRP A 1 38  ? -8.940  6.314   61.367  1.00 20.13 ? 66  TRP A CG  1 
ATOM   264  C  CD1 . TRP A 1 38  ? -10.122 6.157   62.037  1.00 22.35 ? 66  TRP A CD1 1 
ATOM   265  C  CD2 . TRP A 1 38  ? -8.776  7.736   61.176  1.00 21.80 ? 66  TRP A CD2 1 
ATOM   266  N  NE1 . TRP A 1 38  ? -10.703 7.389   62.278  1.00 23.35 ? 66  TRP A NE1 1 
ATOM   267  C  CE2 . TRP A 1 38  ? -9.901  8.369   61.755  1.00 23.42 ? 66  TRP A CE2 1 
ATOM   268  C  CE3 . TRP A 1 38  ? -7.795  8.526   60.564  1.00 19.35 ? 66  TRP A CE3 1 
ATOM   269  C  CZ2 . TRP A 1 38  ? -10.073 9.761   61.747  1.00 21.52 ? 66  TRP A CZ2 1 
ATOM   270  C  CZ3 . TRP A 1 38  ? -7.974  9.919   60.546  1.00 23.40 ? 66  TRP A CZ3 1 
ATOM   271  C  CH2 . TRP A 1 38  ? -9.099  10.509  61.138  1.00 24.67 ? 66  TRP A CH2 1 
ATOM   272  N  N   . GLY A 1 39  ? -6.490  4.404   63.530  1.00 16.98 ? 67  GLY A N   1 
ATOM   273  C  CA  . GLY A 1 39  ? -6.459  4.505   64.985  1.00 17.20 ? 67  GLY A CA  1 
ATOM   274  C  C   . GLY A 1 39  ? -5.099  4.889   65.557  1.00 20.60 ? 67  GLY A C   1 
ATOM   275  O  O   . GLY A 1 39  ? -5.025  5.570   66.587  1.00 20.30 ? 67  GLY A O   1 
ATOM   276  N  N   . LEU A 1 40  ? -4.014  4.440   64.933  1.00 19.61 ? 68  LEU A N   1 
ATOM   277  C  CA  . LEU A 1 40  ? -2.668  4.665   65.449  1.00 17.99 ? 68  LEU A CA  1 
ATOM   278  C  C   . LEU A 1 40  ? -1.858  5.675   64.654  1.00 20.85 ? 68  LEU A C   1 
ATOM   279  O  O   . LEU A 1 40  ? -0.742  6.024   65.074  1.00 21.33 ? 68  LEU A O   1 
ATOM   280  C  CB  . LEU A 1 40  ? -1.883  3.333   65.484  1.00 20.91 ? 68  LEU A CB  1 
ATOM   281  C  CG  . LEU A 1 40  ? -2.350  2.354   66.566  1.00 21.48 ? 68  LEU A CG  1 
ATOM   282  C  CD1 . LEU A 1 40  ? -2.165  0.856   66.150  1.00 19.52 ? 68  LEU A CD1 1 
ATOM   283  C  CD2 . LEU A 1 40  ? -1.578  2.638   67.843  1.00 22.40 ? 68  LEU A CD2 1 
ATOM   284  N  N   . GLY A 1 41  ? -2.361  6.126   63.513  1.00 22.80 ? 69  GLY A N   1 
ATOM   285  C  CA  . GLY A 1 41  ? -1.640  7.065   62.677  1.00 23.98 ? 69  GLY A CA  1 
ATOM   286  C  C   . GLY A 1 41  ? -0.457  6.456   61.968  1.00 23.65 ? 69  GLY A C   1 
ATOM   287  O  O   . GLY A 1 41  ? 0.636   7.027   61.968  1.00 22.49 ? 69  GLY A O   1 
ATOM   288  N  N   . MET A 1 42  ? -0.655  5.295   61.348  1.00 23.53 ? 70  MET A N   1 
ATOM   289  C  CA  . MET A 1 42  ? 0.402   4.626   60.613  1.00 22.83 ? 70  MET A CA  1 
ATOM   290  C  C   . MET A 1 42  ? 0.010   4.633   59.147  1.00 25.77 ? 70  MET A C   1 
ATOM   291  O  O   . MET A 1 42  ? -1.176  4.517   58.813  1.00 28.83 ? 70  MET A O   1 
ATOM   292  C  CB  . MET A 1 42  ? 0.615   3.198   61.140  1.00 18.24 ? 70  MET A CB  1 
ATOM   293  C  CG  . MET A 1 42  ? 0.709   3.134   62.664  1.00 21.95 ? 70  MET A CG  1 
ATOM   294  S  SD  . MET A 1 42  ? 0.888   1.432   63.297  1.00 23.36 ? 70  MET A SD  1 
ATOM   295  C  CE  . MET A 1 42  ? 2.479   0.974   62.635  1.00 22.50 ? 70  MET A CE  1 
ATOM   296  N  N   . ARG A 1 43  ? 0.982   4.800   58.270  1.00 19.69 ? 71  ARG A N   1 
ATOM   297  C  CA  . ARG A 1 43  ? 0.663   4.861   56.853  1.00 27.77 ? 71  ARG A CA  1 
ATOM   298  C  C   . ARG A 1 43  ? 0.856   3.509   56.189  1.00 27.49 ? 71  ARG A C   1 
ATOM   299  O  O   . ARG A 1 43  ? 1.651   2.686   56.649  1.00 26.00 ? 71  ARG A O   1 
ATOM   300  C  CB  . ARG A 1 43  ? 1.517   5.898   56.130  1.00 30.94 ? 71  ARG A CB  1 
ATOM   301  C  CG  . ARG A 1 43  ? 2.985   5.840   56.384  1.00 34.18 ? 71  ARG A CG  1 
ATOM   302  C  CD  . ARG A 1 43  ? 3.637   7.100   55.758  1.00 42.40 ? 71  ARG A CD  1 
ATOM   303  N  NE  . ARG A 1 43  ? 3.185   7.310   54.378  1.00 44.46 ? 71  ARG A NE  1 
ATOM   304  C  CZ  . ARG A 1 43  ? 3.626   8.271   53.566  1.00 50.64 ? 71  ARG A CZ  1 
ATOM   305  N  NH1 . ARG A 1 43  ? 3.141   8.370   52.331  1.00 51.21 ? 71  ARG A NH1 1 
ATOM   306  N  NH2 . ARG A 1 43  ? 4.549   9.137   53.985  1.00 44.10 ? 71  ARG A NH2 1 
ATOM   307  N  N   . PHE A 1 44  ? 0.129   3.299   55.090  1.00 25.50 ? 72  PHE A N   1 
ATOM   308  C  CA  . PHE A 1 44  ? 0.304   2.098   54.273  1.00 30.15 ? 72  PHE A CA  1 
ATOM   309  C  C   . PHE A 1 44  ? 1.587   2.216   53.455  1.00 31.12 ? 72  PHE A C   1 
ATOM   310  O  O   . PHE A 1 44  ? 1.710   3.111   52.610  1.00 31.26 ? 72  PHE A O   1 
ATOM   311  C  CB  . PHE A 1 44  ? -0.888  1.909   53.339  1.00 32.51 ? 72  PHE A CB  1 
ATOM   312  C  CG  . PHE A 1 44  ? -2.039  1.164   53.950  1.00 36.71 ? 72  PHE A CG  1 
ATOM   313  C  CD1 . PHE A 1 44  ? -3.114  1.853   54.485  1.00 37.50 ? 72  PHE A CD1 1 
ATOM   314  C  CD2 . PHE A 1 44  ? -2.064  -0.222  53.966  1.00 39.62 ? 72  PHE A CD2 1 
ATOM   315  C  CE1 . PHE A 1 44  ? -4.201  1.181   55.043  1.00 33.64 ? 72  PHE A CE1 1 
ATOM   316  C  CE2 . PHE A 1 44  ? -3.154  -0.910  54.523  1.00 36.04 ? 72  PHE A CE2 1 
ATOM   317  C  CZ  . PHE A 1 44  ? -4.217  -0.199  55.063  1.00 29.66 ? 72  PHE A CZ  1 
ATOM   318  N  N   . SER A 1 45  ? 2.533   1.313   53.687  1.00 23.06 ? 73  SER A N   1 
ATOM   319  C  CA  . SER A 1 45  ? 3.867   1.423   53.109  1.00 30.53 ? 73  SER A CA  1 
ATOM   320  C  C   . SER A 1 45  ? 4.234   0.327   52.117  1.00 33.65 ? 73  SER A C   1 
ATOM   321  O  O   . SER A 1 45  ? 5.062   0.574   51.240  1.00 30.97 ? 73  SER A O   1 
ATOM   322  C  CB  . SER A 1 45  ? 4.926   1.445   54.224  1.00 34.83 ? 73  SER A CB  1 
ATOM   323  O  OG  . SER A 1 45  ? 4.844   2.667   54.948  1.00 35.69 ? 73  SER A OG  1 
ATOM   324  N  N   . ALA A 1 46  ? 3.677   -0.876  52.235  1.00 26.48 ? 74  ALA A N   1 
ATOM   325  C  CA  . ALA A 1 46  ? 3.997   -1.931  51.280  1.00 24.30 ? 74  ALA A CA  1 
ATOM   326  C  C   . ALA A 1 46  ? 2.851   -2.931  51.274  1.00 25.98 ? 74  ALA A C   1 
ATOM   327  O  O   . ALA A 1 46  ? 2.063   -2.990  52.217  1.00 25.43 ? 74  ALA A O   1 
ATOM   328  C  CB  . ALA A 1 46  ? 5.322   -2.629  51.611  1.00 29.86 ? 74  ALA A CB  1 
ATOM   329  N  N   . LYS A 1 47  ? 2.768   -3.711  50.197  1.00 24.73 ? 75  LYS A N   1 
ATOM   330  C  CA  . LYS A 1 47  ? 1.746   -4.742  50.091  1.00 24.26 ? 75  LYS A CA  1 
ATOM   331  C  C   . LYS A 1 47  ? 2.280   -5.947  49.335  1.00 26.21 ? 75  LYS A C   1 
ATOM   332  O  O   . LYS A 1 47  ? 3.195   -5.842  48.516  1.00 27.97 ? 75  LYS A O   1 
ATOM   333  C  CB  . LYS A 1 47  ? 0.483   -4.245  49.372  1.00 26.45 ? 75  LYS A CB  1 
ATOM   334  C  CG  . LYS A 1 47  ? 0.737   -3.873  47.909  1.00 30.07 ? 75  LYS A CG  1 
ATOM   335  C  CD  . LYS A 1 47  ? -0.540  -3.478  47.190  1.00 33.35 ? 75  LYS A CD  1 
ATOM   336  C  CE  . LYS A 1 47  ? -0.242  -3.051  45.758  1.00 36.77 ? 75  LYS A CE  1 
ATOM   337  N  NZ  . LYS A 1 47  ? -1.473  -2.660  45.038  1.00 35.14 ? 75  LYS A NZ  1 
ATOM   338  N  N   . SER A 1 48  ? 1.680   -7.095  49.630  1.00 22.66 ? 76  SER A N   1 
ATOM   339  C  CA  . SER A 1 48  ? 1.901   -8.336  48.899  1.00 24.35 ? 76  SER A CA  1 
ATOM   340  C  C   . SER A 1 48  ? 0.541   -9.018  48.877  1.00 25.81 ? 76  SER A C   1 
ATOM   341  O  O   . SER A 1 48  ? 0.019   -9.390  49.932  1.00 23.32 ? 76  SER A O   1 
ATOM   342  C  CB  . SER A 1 48  ? 2.957   -9.205  49.578  1.00 24.47 ? 76  SER A CB  1 
ATOM   343  O  OG  . SER A 1 48  ? 3.080   -10.487 48.970  1.00 23.87 ? 76  SER A OG  1 
ATOM   344  N  N   . ASP A 1 49  ? -0.055  -9.133  47.699  1.00 21.60 ? 77  ASP A N   1 
ATOM   345  C  CA  . ASP A 1 49  ? -1.418  -9.641  47.601  1.00 26.32 ? 77  ASP A CA  1 
ATOM   346  C  C   . ASP A 1 49  ? -1.666  -10.029 46.147  1.00 26.11 ? 77  ASP A C   1 
ATOM   347  O  O   . ASP A 1 49  ? -0.718  -10.127 45.357  1.00 28.39 ? 77  ASP A O   1 
ATOM   348  C  CB  . ASP A 1 49  ? -2.427  -8.614  48.147  1.00 23.66 ? 77  ASP A CB  1 
ATOM   349  C  CG  . ASP A 1 49  ? -2.514  -7.343  47.319  1.00 27.88 ? 77  ASP A CG  1 
ATOM   350  O  OD1 . ASP A 1 49  ? -1.920  -7.269  46.228  1.00 28.83 ? 77  ASP A OD1 1 
ATOM   351  O  OD2 . ASP A 1 49  ? -3.242  -6.412  47.751  1.00 28.80 ? 77  ASP A OD2 1 
ATOM   352  N  N   . LEU A 1 50  ? -2.937  -10.242 45.789  1.00 23.59 ? 78  LEU A N   1 
ATOM   353  C  CA  . LEU A 1 50  ? -3.255  -10.646 44.422  1.00 26.52 ? 78  LEU A CA  1 
ATOM   354  C  C   . LEU A 1 50  ? -2.676  -9.676  43.409  1.00 25.78 ? 78  LEU A C   1 
ATOM   355  O  O   . LEU A 1 50  ? -2.258  -10.086 42.323  1.00 27.41 ? 78  LEU A O   1 
ATOM   356  C  CB  . LEU A 1 50  ? -4.770  -10.756 44.211  1.00 23.20 ? 78  LEU A CB  1 
ATOM   357  C  CG  . LEU A 1 50  ? -5.574  -11.859 44.894  1.00 26.42 ? 78  LEU A CG  1 
ATOM   358  C  CD1 . LEU A 1 50  ? -7.079  -11.600 44.655  1.00 26.83 ? 78  LEU A CD1 1 
ATOM   359  C  CD2 . LEU A 1 50  ? -5.185  -13.272 44.461  1.00 27.33 ? 78  LEU A CD2 1 
ATOM   360  N  N   . SER A 1 51  ? -2.672  -8.379  43.726  1.00 26.07 ? 79  SER A N   1 
ATOM   361  C  CA  . SER A 1 51  ? -2.195  -7.405  42.750  1.00 29.66 ? 79  SER A CA  1 
ATOM   362  C  C   . SER A 1 51  ? -0.684  -7.440  42.572  1.00 33.07 ? 79  SER A C   1 
ATOM   363  O  O   . SER A 1 51  ? -0.173  -6.833  41.627  1.00 33.04 ? 79  SER A O   1 
ATOM   364  C  CB  . SER A 1 51  ? -2.622  -5.990  43.153  1.00 30.28 ? 79  SER A CB  1 
ATOM   365  O  OG  . SER A 1 51  ? -1.833  -5.523  44.234  1.00 29.51 ? 79  SER A OG  1 
ATOM   366  N  N   . THR A 1 52  ? 0.045   -8.114  43.455  1.00 28.75 ? 80  THR A N   1 
ATOM   367  C  CA  . THR A 1 52  ? 1.480   -8.295  43.289  1.00 30.53 ? 80  THR A CA  1 
ATOM   368  C  C   . THR A 1 52  ? 1.837   -9.718  42.868  1.00 30.77 ? 80  THR A C   1 
ATOM   369  O  O   . THR A 1 52  ? 3.024   -10.048 42.782  1.00 30.20 ? 80  THR A O   1 
ATOM   370  C  CB  . THR A 1 52  ? 2.211   -7.906  44.577  1.00 28.28 ? 80  THR A CB  1 
ATOM   371  O  OG1 . THR A 1 52  ? 1.972   -8.900  45.582  1.00 26.56 ? 80  THR A OG1 1 
ATOM   372  C  CG2 . THR A 1 52  ? 1.722   -6.532  45.071  1.00 32.28 ? 80  THR A CG2 1 
ATOM   373  N  N   . GLY A 1 53  ? 0.842   -10.561 42.587  1.00 29.20 ? 81  GLY A N   1 
ATOM   374  C  CA  . GLY A 1 53  ? 1.090   -11.924 42.158  1.00 31.09 ? 81  GLY A CA  1 
ATOM   375  C  C   . GLY A 1 53  ? 1.082   -12.964 43.259  1.00 31.22 ? 81  GLY A C   1 
ATOM   376  O  O   . GLY A 1 53  ? 1.346   -14.139 42.982  1.00 29.89 ? 81  GLY A O   1 
ATOM   377  N  N   . ASN A 1 54  ? 0.761   -12.577 44.487  1.00 26.53 ? 82  ASN A N   1 
ATOM   378  C  CA  . ASN A 1 54  ? 0.668   -13.499 45.614  1.00 26.25 ? 82  ASN A CA  1 
ATOM   379  C  C   . ASN A 1 54  ? -0.729  -14.129 45.623  1.00 30.24 ? 82  ASN A C   1 
ATOM   380  O  O   . ASN A 1 54  ? -1.723  -13.449 45.912  1.00 25.39 ? 82  ASN A O   1 
ATOM   381  C  CB  . ASN A 1 54  ? 0.963   -12.725 46.901  1.00 27.39 ? 82  ASN A CB  1 
ATOM   382  C  CG  . ASN A 1 54  ? 1.064   -13.613 48.118  1.00 24.12 ? 82  ASN A CG  1 
ATOM   383  O  OD1 . ASN A 1 54  ? 0.548   -14.723 48.132  1.00 23.32 ? 82  ASN A OD1 1 
ATOM   384  N  ND2 . ASN A 1 54  ? 1.740   -13.122 49.154  1.00 24.46 ? 82  ASN A ND2 1 
ATOM   385  N  N   . MET A 1 55  ? -0.811  -15.427 45.310  1.00 26.99 ? 83  MET A N   1 
ATOM   386  C  CA  . MET A 1 55  ? -2.073  -16.165 45.296  1.00 26.03 ? 83  MET A CA  1 
ATOM   387  C  C   . MET A 1 55  ? -2.346  -16.897 46.600  1.00 24.10 ? 83  MET A C   1 
ATOM   388  O  O   . MET A 1 55  ? -3.348  -17.606 46.704  1.00 24.70 ? 83  MET A O   1 
ATOM   389  C  CB  . MET A 1 55  ? -2.097  -17.185 44.157  1.00 27.76 ? 83  MET A CB  1 
ATOM   390  C  CG  . MET A 1 55  ? -1.779  -16.625 42.795  1.00 30.28 ? 83  MET A CG  1 
ATOM   391  S  SD  . MET A 1 55  ? -3.084  -15.539 42.183  1.00 40.65 ? 83  MET A SD  1 
ATOM   392  C  CE  . MET A 1 55  ? -2.211  -14.001 42.131  1.00 34.70 ? 83  MET A CE  1 
ATOM   393  N  N   . VAL A 1 56  ? -1.497  -16.704 47.600  1.00 24.64 ? 84  VAL A N   1 
ATOM   394  C  CA  . VAL A 1 56  ? -1.545  -17.454 48.843  1.00 23.88 ? 84  VAL A CA  1 
ATOM   395  C  C   . VAL A 1 56  ? -2.092  -16.619 49.986  1.00 20.93 ? 84  VAL A C   1 
ATOM   396  O  O   . VAL A 1 56  ? -3.007  -17.048 50.692  1.00 24.73 ? 84  VAL A O   1 
ATOM   397  C  CB  . VAL A 1 56  ? -0.131  -17.976 49.188  1.00 23.38 ? 84  VAL A CB  1 
ATOM   398  C  CG1 . VAL A 1 56  ? -0.148  -18.617 50.557  1.00 24.47 ? 84  VAL A CG1 1 
ATOM   399  C  CG2 . VAL A 1 56  ? 0.345   -18.960 48.126  1.00 26.34 ? 84  VAL A CG2 1 
ATOM   400  N  N   . HIS A 1 57  ? -1.497  -15.449 50.224  1.00 22.09 ? 85  HIS A N   1 
ATOM   401  C  CA  . HIS A 1 57  ? -1.881  -14.630 51.368  1.00 24.73 ? 85  HIS A CA  1 
ATOM   402  C  C   . HIS A 1 57  ? -1.910  -13.158 50.987  1.00 23.69 ? 85  HIS A C   1 
ATOM   403  O  O   . HIS A 1 57  ? -1.203  -12.717 50.077  1.00 24.52 ? 85  HIS A O   1 
ATOM   404  C  CB  . HIS A 1 57  ? -0.963  -14.845 52.587  1.00 22.44 ? 85  HIS A CB  1 
ATOM   405  C  CG  . HIS A 1 57  ? 0.499   -14.588 52.340  1.00 21.35 ? 85  HIS A CG  1 
ATOM   406  N  ND1 . HIS A 1 57  ? 1.095   -13.362 52.565  1.00 23.00 ? 85  HIS A ND1 1 
ATOM   407  C  CD2 . HIS A 1 57  ? 1.497   -15.421 51.946  1.00 22.85 ? 85  HIS A CD2 1 
ATOM   408  C  CE1 . HIS A 1 57  ? 2.388   -13.446 52.309  1.00 25.15 ? 85  HIS A CE1 1 
ATOM   409  N  NE2 . HIS A 1 57  ? 2.656   -14.682 51.925  1.00 27.06 ? 85  HIS A NE2 1 
ATOM   410  N  N   . ALA A 1 58  ? -2.772  -12.413 51.683  1.00 22.85 ? 86  ALA A N   1 
ATOM   411  C  CA  . ALA A 1 58  ? -2.836  -10.960 51.589  1.00 20.03 ? 86  ALA A CA  1 
ATOM   412  C  C   . ALA A 1 58  ? -2.065  -10.378 52.766  1.00 18.55 ? 86  ALA A C   1 
ATOM   413  O  O   . ALA A 1 58  ? -2.380  -10.679 53.922  1.00 20.12 ? 86  ALA A O   1 
ATOM   414  C  CB  . ALA A 1 58  ? -4.294  -10.480 51.602  1.00 24.55 ? 86  ALA A CB  1 
ATOM   415  N  N   . SER A 1 59  ? -1.060  -9.546  52.489  1.00 19.30 ? 87  SER A N   1 
ATOM   416  C  CA  . SER A 1 59  ? -0.249  -8.960  53.546  1.00 19.58 ? 87  SER A CA  1 
ATOM   417  C  C   . SER A 1 59  ? -0.087  -7.466  53.316  1.00 21.78 ? 87  SER A C   1 
ATOM   418  O  O   . SER A 1 59  ? 0.322   -7.046  52.228  1.00 22.98 ? 87  SER A O   1 
ATOM   419  C  CB  . SER A 1 59  ? 1.146   -9.619  53.619  1.00 21.76 ? 87  SER A CB  1 
ATOM   420  O  OG  . SER A 1 59  ? 1.066   -10.912 54.193  1.00 21.13 ? 87  SER A OG  1 
ATOM   421  N  N   . TYR A 1 60  ? -0.391  -6.661  54.342  1.00 21.07 ? 88  TYR A N   1 
ATOM   422  C  CA  . TYR A 1 60  ? -0.279  -5.208  54.236  1.00 19.11 ? 88  TYR A CA  1 
ATOM   423  C  C   . TYR A 1 60  ? 0.581   -4.666  55.360  1.00 19.65 ? 88  TYR A C   1 
ATOM   424  O  O   . TYR A 1 60  ? 0.390   -5.029  56.528  1.00 21.09 ? 88  TYR A O   1 
ATOM   425  C  CB  . TYR A 1 60  ? -1.683  -4.531  54.254  1.00 16.87 ? 88  TYR A CB  1 
ATOM   426  C  CG  . TYR A 1 60  ? -2.529  -5.088  53.144  1.00 20.71 ? 88  TYR A CG  1 
ATOM   427  C  CD1 . TYR A 1 60  ? -2.205  -4.808  51.817  1.00 22.20 ? 88  TYR A CD1 1 
ATOM   428  C  CD2 . TYR A 1 60  ? -3.611  -5.940  53.404  1.00 22.55 ? 88  TYR A CD2 1 
ATOM   429  C  CE1 . TYR A 1 60  ? -2.941  -5.328  50.781  1.00 22.53 ? 88  TYR A CE1 1 
ATOM   430  C  CE2 . TYR A 1 60  ? -4.367  -6.467  52.359  1.00 21.37 ? 88  TYR A CE2 1 
ATOM   431  C  CZ  . TYR A 1 60  ? -4.018  -6.144  51.053  1.00 22.81 ? 88  TYR A CZ  1 
ATOM   432  O  OH  . TYR A 1 60  ? -4.727  -6.664  50.012  1.00 26.02 ? 88  TYR A OH  1 
ATOM   433  N  N   . LEU A 1 61  ? 1.499   -3.772  55.014  1.00 21.02 ? 89  LEU A N   1 
ATOM   434  C  CA  . LEU A 1 61  ? 2.444   -3.235  55.974  1.00 20.95 ? 89  LEU A CA  1 
ATOM   435  C  C   . LEU A 1 61  ? 2.099   -1.785  56.276  1.00 19.59 ? 89  LEU A C   1 
ATOM   436  O  O   . LEU A 1 61  ? 1.965   -0.965  55.357  1.00 23.37 ? 89  LEU A O   1 
ATOM   437  C  CB  . LEU A 1 61  ? 3.883   -3.340  55.453  1.00 24.48 ? 89  LEU A CB  1 
ATOM   438  C  CG  . LEU A 1 61  ? 4.873   -2.760  56.460  1.00 24.11 ? 89  LEU A CG  1 
ATOM   439  C  CD1 . LEU A 1 61  ? 5.099   -3.768  57.575  1.00 23.68 ? 89  LEU A CD1 1 
ATOM   440  C  CD2 . LEU A 1 61  ? 6.199   -2.367  55.810  1.00 29.93 ? 89  LEU A CD2 1 
ATOM   441  N  N   . LEU A 1 62  ? 1.941   -1.475  57.567  1.00 18.06 ? 90  LEU A N   1 
ATOM   442  C  CA  . LEU A 1 62  ? 1.810   -0.107  58.050  1.00 20.07 ? 90  LEU A CA  1 
ATOM   443  C  C   . LEU A 1 62  ? 3.123   0.308   58.699  1.00 19.58 ? 90  LEU A C   1 
ATOM   444  O  O   . LEU A 1 62  ? 3.774   -0.499  59.359  1.00 20.99 ? 90  LEU A O   1 
ATOM   445  C  CB  . LEU A 1 62  ? 0.695   0.027   59.085  1.00 22.14 ? 90  LEU A CB  1 
ATOM   446  C  CG  . LEU A 1 62  ? -0.703  -0.507  58.737  1.00 20.43 ? 90  LEU A CG  1 
ATOM   447  C  CD1 . LEU A 1 62  ? -1.647  -0.188  59.876  1.00 19.68 ? 90  LEU A CD1 1 
ATOM   448  C  CD2 . LEU A 1 62  ? -1.182  0.127   57.444  1.00 26.25 ? 90  LEU A CD2 1 
ATOM   449  N  N   . THR A 1 63  ? 3.500   1.576   58.548  1.00 22.14 ? 91  THR A N   1 
ATOM   450  C  CA  . THR A 1 63  ? 4.689   2.077   59.221  1.00 22.25 ? 91  THR A CA  1 
ATOM   451  C  C   . THR A 1 63  ? 4.399   3.389   59.944  1.00 24.23 ? 91  THR A C   1 
ATOM   452  O  O   . THR A 1 63  ? 3.536   4.186   59.543  1.00 23.29 ? 91  THR A O   1 
ATOM   453  C  CB  . THR A 1 63  ? 5.836   2.283   58.239  1.00 28.08 ? 91  THR A CB  1 
ATOM   454  O  OG1 . THR A 1 63  ? 5.409   3.217   57.237  1.00 32.44 ? 91  THR A OG1 1 
ATOM   455  C  CG2 . THR A 1 63  ? 6.224   0.950   57.579  1.00 26.01 ? 91  THR A CG2 1 
ATOM   456  N  N   . SER A 1 64  ? 5.109   3.587   61.047  1.00 24.47 ? 92  SER A N   1 
ATOM   457  C  CA  . SER A 1 64  ? 5.172   4.901   61.690  1.00 24.87 ? 92  SER A CA  1 
ATOM   458  C  C   . SER A 1 64  ? 6.575   5.032   62.264  1.00 25.17 ? 92  SER A C   1 
ATOM   459  O  O   . SER A 1 64  ? 6.916   4.328   63.222  1.00 22.96 ? 92  SER A O   1 
ATOM   460  C  CB  . SER A 1 64  ? 4.117   5.041   62.775  1.00 25.81 ? 92  SER A CB  1 
ATOM   461  O  OG  . SER A 1 64  ? 4.026   6.383   63.214  1.00 23.53 ? 92  SER A OG  1 
ATOM   462  N  N   . GLY A 1 65  ? 7.378   5.920   61.696  1.00 26.79 ? 93  GLY A N   1 
ATOM   463  C  CA  . GLY A 1 65  ? 8.780   5.969   62.098  1.00 24.50 ? 93  GLY A CA  1 
ATOM   464  C  C   . GLY A 1 65  ? 9.439   4.630   61.800  1.00 25.89 ? 93  GLY A C   1 
ATOM   465  O  O   . GLY A 1 65  ? 9.416   4.141   60.657  1.00 26.36 ? 93  GLY A O   1 
ATOM   466  N  N   . ASP A 1 66  ? 10.021  4.010   62.826  1.00 21.63 ? 94  ASP A N   1 
ATOM   467  C  CA  . ASP A 1 66  ? 10.652  2.705   62.662  1.00 24.02 ? 94  ASP A CA  1 
ATOM   468  C  C   . ASP A 1 66  ? 9.708   1.559   62.981  1.00 26.09 ? 94  ASP A C   1 
ATOM   469  O  O   . ASP A 1 66  ? 10.122  0.399   62.882  1.00 28.53 ? 94  ASP A O   1 
ATOM   470  C  CB  . ASP A 1 66  ? 11.892  2.534   63.559  1.00 26.67 ? 94  ASP A CB  1 
ATOM   471  C  CG  . ASP A 1 66  ? 13.018  3.489   63.220  1.00 40.18 ? 94  ASP A CG  1 
ATOM   472  O  OD1 . ASP A 1 66  ? 13.151  3.875   62.040  1.00 36.05 ? 94  ASP A OD1 1 
ATOM   473  O  OD2 . ASP A 1 66  ? 13.792  3.822   64.145  1.00 47.05 ? 94  ASP A OD2 1 
ATOM   474  N  N   . LEU A 1 67  ? 8.489   1.851   63.427  1.00 22.34 ? 95  LEU A N   1 
ATOM   475  C  CA  . LEU A 1 67  ? 7.535   0.803   63.772  1.00 25.61 ? 95  LEU A CA  1 
ATOM   476  C  C   . LEU A 1 67  ? 6.935   0.219   62.503  1.00 23.08 ? 95  LEU A C   1 
ATOM   477  O  O   . LEU A 1 67  ? 6.494   0.958   61.623  1.00 23.63 ? 95  LEU A O   1 
ATOM   478  C  CB  . LEU A 1 67  ? 6.434   1.343   64.674  1.00 22.32 ? 95  LEU A CB  1 
ATOM   479  C  CG  . LEU A 1 67  ? 5.367   0.317   65.125  1.00 18.10 ? 95  LEU A CG  1 
ATOM   480  C  CD1 . LEU A 1 67  ? 5.959   -0.746  66.009  1.00 20.24 ? 95  LEU A CD1 1 
ATOM   481  C  CD2 . LEU A 1 67  ? 4.253   1.057   65.861  1.00 18.62 ? 95  LEU A CD2 1 
ATOM   482  N  N   . ARG A 1 68  ? 6.927   -1.113  62.404  1.00 21.40 ? 96  ARG A N   1 
ATOM   483  C  CA  . ARG A 1 68  ? 6.355   -1.797  61.252  1.00 19.88 ? 96  ARG A CA  1 
ATOM   484  C  C   . ARG A 1 68  ? 5.334   -2.802  61.755  1.00 20.57 ? 96  ARG A C   1 
ATOM   485  O  O   . ARG A 1 68  ? 5.693   -3.743  62.467  1.00 20.15 ? 96  ARG A O   1 
ATOM   486  C  CB  . ARG A 1 68  ? 7.426   -2.518  60.426  1.00 25.49 ? 96  ARG A CB  1 
ATOM   487  C  CG  . ARG A 1 68  ? 8.592   -1.649  59.950  1.00 30.56 ? 96  ARG A CG  1 
ATOM   488  C  CD  . ARG A 1 68  ? 9.609   -2.553  59.255  1.00 33.11 ? 96  ARG A CD  1 
ATOM   489  N  NE  . ARG A 1 68  ? 10.738  -1.818  58.709  1.00 43.54 ? 96  ARG A NE  1 
ATOM   490  C  CZ  . ARG A 1 68  ? 11.836  -1.528  59.397  1.00 44.79 ? 96  ARG A CZ  1 
ATOM   491  N  NH1 . ARG A 1 68  ? 11.946  -1.907  60.667  1.00 39.31 ? 96  ARG A NH1 1 
ATOM   492  N  NH2 . ARG A 1 68  ? 12.814  -0.844  58.814  1.00 47.37 ? 96  ARG A NH2 1 
ATOM   493  N  N   . PHE A 1 69  ? 4.079   -2.622  61.354  1.00 18.71 ? 97  PHE A N   1 
ATOM   494  C  CA  . PHE A 1 69  ? 2.995   -3.565  61.639  1.00 19.50 ? 97  PHE A CA  1 
ATOM   495  C  C   . PHE A 1 69  ? 2.597   -4.243  60.336  1.00 19.79 ? 97  PHE A C   1 
ATOM   496  O  O   . PHE A 1 69  ? 2.223   -3.557  59.377  1.00 20.56 ? 97  PHE A O   1 
ATOM   497  C  CB  . PHE A 1 69  ? 1.773   -2.849  62.220  1.00 19.92 ? 97  PHE A CB  1 
ATOM   498  C  CG  . PHE A 1 69  ? 1.814   -2.639  63.720  1.00 22.43 ? 97  PHE A CG  1 
ATOM   499  C  CD1 . PHE A 1 69  ? 2.927   -3.025  64.486  1.00 18.90 ? 97  PHE A CD1 1 
ATOM   500  C  CD2 . PHE A 1 69  ? 0.721   -2.050  64.364  1.00 19.86 ? 97  PHE A CD2 1 
ATOM   501  C  CE1 . PHE A 1 69  ? 2.943   -2.820  65.885  1.00 17.43 ? 97  PHE A CE1 1 
ATOM   502  C  CE2 . PHE A 1 69  ? 0.718   -1.843  65.754  1.00 20.01 ? 97  PHE A CE2 1 
ATOM   503  C  CZ  . PHE A 1 69  ? 1.833   -2.234  66.518  1.00 21.49 ? 97  PHE A CZ  1 
ATOM   504  N  N   . LEU A 1 70  ? 2.627   -5.579  60.324  1.00 17.84 ? 98  LEU A N   1 
ATOM   505  C  CA  . LEU A 1 70  ? 2.243   -6.391  59.176  1.00 18.69 ? 98  LEU A CA  1 
ATOM   506  C  C   . LEU A 1 70  ? 0.946   -7.126  59.494  1.00 19.43 ? 98  LEU A C   1 
ATOM   507  O  O   . LEU A 1 70  ? 0.831   -7.736  60.567  1.00 17.80 ? 98  LEU A O   1 
ATOM   508  C  CB  . LEU A 1 70  ? 3.338   -7.421  58.842  1.00 19.41 ? 98  LEU A CB  1 
ATOM   509  C  CG  . LEU A 1 70  ? 3.174   -8.247  57.573  1.00 20.47 ? 98  LEU A CG  1 
ATOM   510  C  CD1 . LEU A 1 70  ? 3.223   -7.322  56.359  1.00 22.23 ? 98  LEU A CD1 1 
ATOM   511  C  CD2 . LEU A 1 70  ? 4.277   -9.323  57.500  1.00 22.89 ? 98  LEU A CD2 1 
ATOM   512  N  N   . PHE A 1 71  ? -0.012  -7.080  58.559  1.00 20.97 ? 99  PHE A N   1 
ATOM   513  C  CA  . PHE A 1 71  ? -1.329  -7.717  58.692  1.00 16.55 ? 99  PHE A CA  1 
ATOM   514  C  C   . PHE A 1 71  ? -1.479  -8.722  57.567  1.00 18.95 ? 99  PHE A C   1 
ATOM   515  O  O   . PHE A 1 71  ? -1.392  -8.352  56.391  1.00 19.08 ? 99  PHE A O   1 
ATOM   516  C  CB  . PHE A 1 71  ? -2.449  -6.646  58.657  1.00 16.94 ? 99  PHE A CB  1 
ATOM   517  C  CG  . PHE A 1 71  ? -2.281  -5.605  59.728  1.00 15.37 ? 99  PHE A CG  1 
ATOM   518  C  CD1 . PHE A 1 71  ? -1.462  -4.495  59.526  1.00 18.85 ? 99  PHE A CD1 1 
ATOM   519  C  CD2 . PHE A 1 71  ? -2.812  -5.816  60.985  1.00 17.44 ? 99  PHE A CD2 1 
ATOM   520  C  CE1 . PHE A 1 71  ? -1.232  -3.583  60.540  1.00 19.28 ? 99  PHE A CE1 1 
ATOM   521  C  CE2 . PHE A 1 71  ? -2.595  -4.906  62.026  1.00 16.81 ? 99  PHE A CE2 1 
ATOM   522  C  CZ  . PHE A 1 71  ? -1.793  -3.793  61.807  1.00 17.03 ? 99  PHE A CZ  1 
ATOM   523  N  N   . THR A 1 72  ? -1.677  -10.001 57.919  1.00 18.76 ? 100 THR A N   1 
ATOM   524  C  CA  . THR A 1 72  ? -1.701  -11.070 56.927  1.00 16.67 ? 100 THR A CA  1 
ATOM   525  C  C   . THR A 1 72  ? -2.916  -11.964 57.121  1.00 18.35 ? 100 THR A C   1 
ATOM   526  O  O   . THR A 1 72  ? -3.291  -12.285 58.254  1.00 21.10 ? 100 THR A O   1 
ATOM   527  C  CB  . THR A 1 72  ? -0.412  -11.925 57.015  1.00 16.63 ? 100 THR A CB  1 
ATOM   528  O  OG1 . THR A 1 72  ? 0.719   -11.100 56.700  1.00 18.50 ? 100 THR A OG1 1 
ATOM   529  C  CG2 . THR A 1 72  ? -0.469  -13.100 56.052  1.00 18.93 ? 100 THR A CG2 1 
ATOM   530  N  N   . ALA A 1 73  ? -3.530  -12.355 56.011  1.00 18.60 ? 101 ALA A N   1 
ATOM   531  C  CA  . ALA A 1 73  ? -4.651  -13.286 56.033  1.00 15.80 ? 101 ALA A CA  1 
ATOM   532  C  C   . ALA A 1 73  ? -4.556  -14.222 54.839  1.00 18.79 ? 101 ALA A C   1 
ATOM   533  O  O   . ALA A 1 73  ? -4.037  -13.832 53.787  1.00 20.84 ? 101 ALA A O   1 
ATOM   534  C  CB  . ALA A 1 73  ? -6.002  -12.545 55.981  1.00 18.53 ? 101 ALA A CB  1 
ATOM   535  N  N   . PRO A 1 74  ? -5.088  -15.438 54.957  1.00 20.17 ? 102 PRO A N   1 
ATOM   536  C  CA  . PRO A 1 74  ? -5.060  -16.376 53.829  1.00 21.66 ? 102 PRO A CA  1 
ATOM   537  C  C   . PRO A 1 74  ? -6.166  -16.130 52.819  1.00 25.96 ? 102 PRO A C   1 
ATOM   538  O  O   . PRO A 1 74  ? -7.280  -15.753 53.171  1.00 24.10 ? 102 PRO A O   1 
ATOM   539  C  CB  . PRO A 1 74  ? -5.242  -17.745 54.503  1.00 24.47 ? 102 PRO A CB  1 
ATOM   540  C  CG  . PRO A 1 74  ? -5.990  -17.492 55.767  1.00 24.17 ? 102 PRO A CG  1 
ATOM   541  C  CD  . PRO A 1 74  ? -5.588  -16.052 56.202  1.00 19.13 ? 102 PRO A CD  1 
ATOM   542  N  N   . TYR A 1 75  ? -5.839  -16.356 51.540  1.00 24.35 ? 103 TYR A N   1 
ATOM   543  C  CA  . TYR A 1 75  ? -6.857  -16.479 50.502  1.00 25.04 ? 103 TYR A CA  1 
ATOM   544  C  C   . TYR A 1 75  ? -7.431  -17.899 50.520  1.00 26.81 ? 103 TYR A C   1 
ATOM   545  O  O   . TYR A 1 75  ? -7.007  -18.756 51.303  1.00 26.95 ? 103 TYR A O   1 
ATOM   546  C  CB  . TYR A 1 75  ? -6.275  -16.166 49.119  1.00 25.19 ? 103 TYR A CB  1 
ATOM   547  C  CG  . TYR A 1 75  ? -5.850  -14.723 48.895  1.00 24.02 ? 103 TYR A CG  1 
ATOM   548  C  CD1 . TYR A 1 75  ? -6.760  -13.681 49.035  1.00 20.85 ? 103 TYR A CD1 1 
ATOM   549  C  CD2 . TYR A 1 75  ? -4.546  -14.414 48.505  1.00 23.73 ? 103 TYR A CD2 1 
ATOM   550  C  CE1 . TYR A 1 75  ? -6.377  -12.359 48.815  1.00 19.67 ? 103 TYR A CE1 1 
ATOM   551  C  CE2 . TYR A 1 75  ? -4.151  -13.118 48.295  1.00 22.79 ? 103 TYR A CE2 1 
ATOM   552  C  CZ  . TYR A 1 75  ? -5.073  -12.088 48.458  1.00 24.33 ? 103 TYR A CZ  1 
ATOM   553  O  OH  . TYR A 1 75  ? -4.665  -10.806 48.227  1.00 22.16 ? 103 TYR A OH  1 
ATOM   554  N  N   . SER A 1 76  ? -8.407  -18.159 49.654  1.00 25.23 ? 104 SER A N   1 
ATOM   555  C  CA  . SER A 1 76  ? -8.858  -19.536 49.453  1.00 25.63 ? 104 SER A CA  1 
ATOM   556  C  C   . SER A 1 76  ? -7.669  -20.399 49.030  1.00 24.51 ? 104 SER A C   1 
ATOM   557  O  O   . SER A 1 76  ? -6.951  -20.032 48.095  1.00 25.14 ? 104 SER A O   1 
ATOM   558  C  CB  . SER A 1 76  ? -9.943  -19.617 48.384  1.00 24.87 ? 104 SER A CB  1 
ATOM   559  O  OG  . SER A 1 76  ? -10.202 -20.982 48.006  1.00 25.72 ? 104 SER A OG  1 
ATOM   560  N  N   . PRO A 1 77  ? -7.443  -21.544 49.664  1.00 29.60 ? 105 PRO A N   1 
ATOM   561  C  CA  . PRO A 1 77  ? -6.371  -22.439 49.185  1.00 29.96 ? 105 PRO A CA  1 
ATOM   562  C  C   . PRO A 1 77  ? -6.533  -22.794 47.714  1.00 29.56 ? 105 PRO A C   1 
ATOM   563  O  O   . PRO A 1 77  ? -5.559  -23.095 47.023  1.00 31.14 ? 105 PRO A O   1 
ATOM   564  C  CB  . PRO A 1 77  ? -6.517  -23.667 50.088  1.00 29.66 ? 105 PRO A CB  1 
ATOM   565  C  CG  . PRO A 1 77  ? -7.089  -23.122 51.350  1.00 33.75 ? 105 PRO A CG  1 
ATOM   566  C  CD  . PRO A 1 77  ? -8.078  -22.054 50.890  1.00 25.85 ? 105 PRO A CD  1 
ATOM   567  N  N   . SER A 1 78  ? -7.769  -22.720 47.213  1.00 31.31 ? 106 SER A N   1 
ATOM   568  C  CA  . SER A 1 78  ? -8.022  -23.090 45.828  1.00 30.95 ? 106 SER A CA  1 
ATOM   569  C  C   . SER A 1 78  ? -7.226  -22.243 44.844  1.00 30.11 ? 106 SER A C   1 
ATOM   570  O  O   . SER A 1 78  ? -6.900  -22.727 43.753  1.00 33.20 ? 106 SER A O   1 
ATOM   571  C  CB  . SER A 1 78  ? -9.525  -23.010 45.525  1.00 30.09 ? 106 SER A CB  1 
ATOM   572  O  OG  . SER A 1 78  ? -9.986  -21.677 45.578  1.00 30.11 ? 106 SER A OG  1 
ATOM   573  N  N   . LEU A 1 79  ? -6.887  -20.989 45.197  1.00 28.05 ? 107 LEU A N   1 
ATOM   574  C  CA  . LEU A 1 79  ? -6.131  -20.148 44.270  1.00 25.41 ? 107 LEU A CA  1 
ATOM   575  C  C   . LEU A 1 79  ? -4.705  -20.632 44.068  1.00 28.66 ? 107 LEU A C   1 
ATOM   576  O  O   . LEU A 1 79  ? -4.113  -20.333 43.030  1.00 30.12 ? 107 LEU A O   1 
ATOM   577  C  CB  . LEU A 1 79  ? -6.066  -18.689 44.749  1.00 26.08 ? 107 LEU A CB  1 
ATOM   578  C  CG  . LEU A 1 79  ? -7.385  -18.031 45.129  1.00 28.11 ? 107 LEU A CG  1 
ATOM   579  C  CD1 . LEU A 1 79  ? -7.160  -16.549 45.356  1.00 28.46 ? 107 LEU A CD1 1 
ATOM   580  C  CD2 . LEU A 1 79  ? -8.431  -18.274 44.064  1.00 31.03 ? 107 LEU A CD2 1 
ATOM   581  N  N   . SER A 1 80  ? -4.145  -21.353 45.038  1.00 27.50 ? 108 SER A N   1 
ATOM   582  C  CA  . SER A 1 80  ? -2.753  -21.779 45.000  1.00 26.15 ? 108 SER A CA  1 
ATOM   583  C  C   . SER A 1 80  ? -2.635  -23.297 45.021  1.00 29.66 ? 108 SER A C   1 
ATOM   584  O  O   . SER A 1 80  ? -1.573  -23.827 45.362  1.00 31.77 ? 108 SER A O   1 
ATOM   585  C  CB  . SER A 1 80  ? -1.983  -21.178 46.175  1.00 24.88 ? 108 SER A CB  1 
ATOM   586  O  OG  . SER A 1 80  ? -2.556  -21.587 47.406  1.00 25.64 ? 108 SER A OG  1 
ATOM   587  N  N   . ALA A 1 81  ? -3.710  -24.005 44.665  1.00 33.06 ? 109 ALA A N   1 
ATOM   588  C  CA  . ALA A 1 81  ? -3.731  -25.455 44.839  1.00 36.90 ? 109 ALA A CA  1 
ATOM   589  C  C   . ALA A 1 81  ? -2.700  -26.141 43.952  1.00 34.70 ? 109 ALA A C   1 
ATOM   590  O  O   . ALA A 1 81  ? -2.204  -27.223 44.295  1.00 39.44 ? 109 ALA A O   1 
ATOM   591  C  CB  . ALA A 1 81  ? -5.133  -26.000 44.553  1.00 34.61 ? 109 ALA A CB  1 
ATOM   592  N  N   . GLY A 1 82  ? -2.365  -25.533 42.815  1.00 33.05 ? 110 GLY A N   1 
ATOM   593  C  CA  . GLY A 1 82  ? -1.365  -26.116 41.950  1.00 38.91 ? 110 GLY A CA  1 
ATOM   594  C  C   . GLY A 1 82  ? 0.054   -25.895 42.396  1.00 35.00 ? 110 GLY A C   1 
ATOM   595  O  O   . GLY A 1 82  ? 0.965   -26.498 41.826  1.00 38.18 ? 110 GLY A O   1 
ATOM   596  N  N   . GLU A 1 83  ? 0.266   -25.058 43.409  1.00 30.96 ? 111 GLU A N   1 
ATOM   597  C  CA  . GLU A 1 83  ? 1.614   -24.678 43.805  1.00 29.33 ? 111 GLU A CA  1 
ATOM   598  C  C   . GLU A 1 83  ? 2.224   -25.701 44.755  1.00 27.40 ? 111 GLU A C   1 
ATOM   599  O  O   . GLU A 1 83  ? 1.527   -26.408 45.487  1.00 26.42 ? 111 GLU A O   1 
ATOM   600  C  CB  . GLU A 1 83  ? 1.611   -23.301 44.485  1.00 27.76 ? 111 GLU A CB  1 
ATOM   601  C  CG  . GLU A 1 83  ? 1.171   -22.156 43.591  1.00 30.11 ? 111 GLU A CG  1 
ATOM   602  C  CD  . GLU A 1 83  ? 1.209   -20.804 44.304  1.00 34.85 ? 111 GLU A CD  1 
ATOM   603  O  OE1 . GLU A 1 83  ? 1.858   -20.711 45.380  1.00 28.52 ? 111 GLU A OE1 1 
ATOM   604  O  OE2 . GLU A 1 83  ? 0.586   -19.840 43.783  1.00 29.66 ? 111 GLU A OE2 1 
ATOM   605  N  N   . ILE A 1 84  ? 3.553   -25.748 44.761  1.00 31.02 ? 112 ILE A N   1 
ATOM   606  C  CA  . ILE A 1 84  ? 4.297   -26.434 45.804  1.00 31.10 ? 112 ILE A CA  1 
ATOM   607  C  C   . ILE A 1 84  ? 5.287   -25.412 46.340  1.00 28.40 ? 112 ILE A C   1 
ATOM   608  O  O   . ILE A 1 84  ? 5.501   -24.358 45.732  1.00 30.70 ? 112 ILE A O   1 
ATOM   609  C  CB  . ILE A 1 84  ? 5.000   -27.716 45.288  1.00 27.49 ? 112 ILE A CB  1 
ATOM   610  C  CG1 . ILE A 1 84  ? 5.871   -27.401 44.073  1.00 31.50 ? 112 ILE A CG1 1 
ATOM   611  C  CG2 . ILE A 1 84  ? 3.945   -28.784 44.930  1.00 28.29 ? 112 ILE A CG2 1 
ATOM   612  C  CD1 . ILE A 1 84  ? 6.923   -28.523 43.748  1.00 28.68 ? 112 ILE A CD1 1 
ATOM   613  N  N   . LYS A 1 85  ? 5.849   -25.688 47.515  1.00 24.70 ? 113 LYS A N   1 
ATOM   614  C  CA  . LYS A 1 85  ? 6.769   -24.712 48.098  1.00 29.55 ? 113 LYS A CA  1 
ATOM   615  C  C   . LYS A 1 85  ? 7.831   -24.237 47.109  1.00 31.70 ? 113 LYS A C   1 
ATOM   616  O  O   . LYS A 1 85  ? 8.048   -23.014 47.028  1.00 29.34 ? 113 LYS A O   1 
ATOM   617  C  CB  . LYS A 1 85  ? 7.420   -25.281 49.369  1.00 32.26 ? 113 LYS A CB  1 
ATOM   618  C  CG  . LYS A 1 85  ? 6.550   -25.111 50.612  1.00 35.79 ? 113 LYS A CG  1 
ATOM   619  C  CD  A LYS A 1 85  ? 7.178   -25.787 51.820  0.33 38.46 ? 113 LYS A CD  1 
ATOM   620  C  CD  B LYS A 1 85  ? 7.253   -25.544 51.890  0.67 38.75 ? 113 LYS A CD  1 
ATOM   621  C  CE  A LYS A 1 85  ? 6.559   -25.289 53.118  0.33 39.58 ? 113 LYS A CE  1 
ATOM   622  C  CE  B LYS A 1 85  ? 6.272   -25.586 53.064  0.67 39.38 ? 113 LYS A CE  1 
ATOM   623  N  NZ  A LYS A 1 85  ? 6.904   -23.861 53.373  0.33 37.07 ? 113 LYS A NZ  1 
ATOM   624  N  NZ  B LYS A 1 85  ? 6.967   -25.822 54.367  0.67 41.29 ? 113 LYS A NZ  1 
ATOM   625  N  N   . PRO A 1 86  ? 8.468   -25.103 46.302  1.00 30.57 ? 114 PRO A N   1 
ATOM   626  C  CA  . PRO A 1 86  ? 9.413   -24.602 45.285  1.00 35.73 ? 114 PRO A CA  1 
ATOM   627  C  C   . PRO A 1 86  ? 8.812   -23.637 44.272  1.00 31.71 ? 114 PRO A C   1 
ATOM   628  O  O   . PRO A 1 86  ? 9.561   -22.840 43.697  1.00 39.38 ? 114 PRO A O   1 
ATOM   629  C  CB  . PRO A 1 86  ? 9.897   -25.889 44.600  1.00 33.95 ? 114 PRO A CB  1 
ATOM   630  C  CG  . PRO A 1 86  ? 9.813   -26.924 45.682  1.00 34.63 ? 114 PRO A CG  1 
ATOM   631  C  CD  . PRO A 1 86  ? 8.547   -26.575 46.432  1.00 31.97 ? 114 PRO A CD  1 
ATOM   632  N  N   . THR A 1 87  ? 7.502   -23.685 44.024  1.00 29.60 ? 115 THR A N   1 
ATOM   633  C  CA  . THR A 1 87  ? 6.853   -22.819 43.043  1.00 32.86 ? 115 THR A CA  1 
ATOM   634  C  C   . THR A 1 87  ? 5.931   -21.786 43.692  1.00 31.05 ? 115 THR A C   1 
ATOM   635  O  O   . THR A 1 87  ? 5.113   -21.176 42.998  1.00 31.91 ? 115 THR A O   1 
ATOM   636  C  CB  . THR A 1 87  ? 6.058   -23.650 42.027  1.00 30.18 ? 115 THR A CB  1 
ATOM   637  O  OG1 . THR A 1 87  ? 4.957   -24.309 42.671  1.00 29.39 ? 115 THR A OG1 1 
ATOM   638  C  CG2 . THR A 1 87  ? 6.944   -24.713 41.355  1.00 30.49 ? 115 THR A CG2 1 
ATOM   639  N  N   . THR A 1 88  ? 6.038   -21.579 45.005  1.00 29.83 ? 116 THR A N   1 
ATOM   640  C  CA  . THR A 1 88  ? 5.058   -20.755 45.715  1.00 28.16 ? 116 THR A CA  1 
ATOM   641  C  C   . THR A 1 88  ? 5.061   -19.314 45.207  1.00 27.26 ? 116 THR A C   1 
ATOM   642  O  O   . THR A 1 88  ? 6.093   -18.773 44.797  1.00 27.34 ? 116 THR A O   1 
ATOM   643  C  CB  . THR A 1 88  ? 5.347   -20.763 47.221  1.00 30.28 ? 116 THR A CB  1 
ATOM   644  O  OG1 . THR A 1 88  ? 4.263   -20.151 47.917  1.00 30.78 ? 116 THR A OG1 1 
ATOM   645  C  CG2 . THR A 1 88  ? 6.625   -19.990 47.540  1.00 32.83 ? 116 THR A CG2 1 
ATOM   646  N  N   . THR A 1 89  ? 3.879   -18.682 45.245  1.00 27.68 ? 117 THR A N   1 
ATOM   647  C  CA  . THR A 1 89  ? 3.766   -17.241 45.026  1.00 28.06 ? 117 THR A CA  1 
ATOM   648  C  C   . THR A 1 89  ? 3.684   -16.458 46.332  1.00 26.91 ? 117 THR A C   1 
ATOM   649  O  O   . THR A 1 89  ? 3.555   -15.228 46.298  1.00 27.55 ? 117 THR A O   1 
ATOM   650  C  CB  . THR A 1 89  ? 2.543   -16.908 44.155  1.00 29.20 ? 117 THR A CB  1 
ATOM   651  O  OG1 . THR A 1 89  ? 1.346   -17.412 44.759  1.00 28.07 ? 117 THR A OG1 1 
ATOM   652  C  CG2 . THR A 1 89  ? 2.698   -17.491 42.755  1.00 29.29 ? 117 THR A CG2 1 
ATOM   653  N  N   . ALA A 1 90  ? 3.739   -17.139 47.478  1.00 27.04 ? 118 ALA A N   1 
ATOM   654  C  CA  . ALA A 1 90  ? 3.759   -16.451 48.759  1.00 27.12 ? 118 ALA A CA  1 
ATOM   655  C  C   . ALA A 1 90  ? 5.060   -15.674 48.910  1.00 29.06 ? 118 ALA A C   1 
ATOM   656  O  O   . ALA A 1 90  ? 6.139   -16.171 48.576  1.00 30.59 ? 118 ALA A O   1 
ATOM   657  C  CB  . ALA A 1 90  ? 3.606   -17.458 49.900  1.00 25.38 ? 118 ALA A CB  1 
ATOM   658  N  N   . SER A 1 91  ? 4.962   -14.446 49.416  1.00 25.56 ? 119 SER A N   1 
ATOM   659  C  CA  . SER A 1 91  ? 6.158   -13.660 49.689  1.00 28.22 ? 119 SER A CA  1 
ATOM   660  C  C   . SER A 1 91  ? 6.746   -13.961 51.056  1.00 27.81 ? 119 SER A C   1 
ATOM   661  O  O   . SER A 1 91  ? 7.913   -13.631 51.308  1.00 30.47 ? 119 SER A O   1 
ATOM   662  C  CB  . SER A 1 91  ? 5.848   -12.164 49.595  1.00 29.93 ? 119 SER A CB  1 
ATOM   663  O  OG  . SER A 1 91  ? 4.667   -11.885 50.312  1.00 26.12 ? 119 SER A OG  1 
ATOM   664  N  N   . ILE A 1 92  ? 5.963   -14.554 51.948  1.00 25.92 ? 120 ILE A N   1 
ATOM   665  C  CA  . ILE A 1 92  ? 6.467   -14.977 53.248  1.00 26.37 ? 120 ILE A CA  1 
ATOM   666  C  C   . ILE A 1 92  ? 6.445   -16.498 53.256  1.00 28.94 ? 120 ILE A C   1 
ATOM   667  O  O   . ILE A 1 92  ? 5.383   -17.105 53.466  1.00 24.75 ? 120 ILE A O   1 
ATOM   668  C  CB  . ILE A 1 92  ? 5.646   -14.365 54.394  1.00 27.46 ? 120 ILE A CB  1 
ATOM   669  C  CG1 . ILE A 1 92  ? 5.666   -12.842 54.266  1.00 30.16 ? 120 ILE A CG1 1 
ATOM   670  C  CG2 . ILE A 1 92  ? 6.202   -14.809 55.753  1.00 25.72 ? 120 ILE A CG2 1 
ATOM   671  C  CD1 . ILE A 1 92  ? 4.926   -12.112 55.376  1.00 29.48 ? 120 ILE A CD1 1 
ATOM   672  N  N   . PRO A 1 93  ? 7.589   -17.149 53.009  1.00 27.78 ? 121 PRO A N   1 
ATOM   673  C  CA  . PRO A 1 93  ? 7.574   -18.602 52.755  1.00 26.78 ? 121 PRO A CA  1 
ATOM   674  C  C   . PRO A 1 93  ? 7.182   -19.423 53.965  1.00 26.31 ? 121 PRO A C   1 
ATOM   675  O  O   . PRO A 1 93  ? 6.753   -20.573 53.801  1.00 27.58 ? 121 PRO A O   1 
ATOM   676  C  CB  . PRO A 1 93  ? 9.017   -18.894 52.315  1.00 36.50 ? 121 PRO A CB  1 
ATOM   677  C  CG  . PRO A 1 93  ? 9.834   -17.780 52.888  1.00 33.58 ? 121 PRO A CG  1 
ATOM   678  C  CD  . PRO A 1 93  ? 8.935   -16.564 52.873  1.00 31.90 ? 121 PRO A CD  1 
ATOM   679  N  N   . SER A 1 94  ? 7.293   -18.869 55.173  1.00 23.82 ? 122 SER A N   1 
ATOM   680  C  CA  . SER A 1 94  ? 6.812   -19.572 56.348  1.00 26.96 ? 122 SER A CA  1 
ATOM   681  C  C   . SER A 1 94  ? 5.290   -19.640 56.427  1.00 27.29 ? 122 SER A C   1 
ATOM   682  O  O   . SER A 1 94  ? 4.771   -20.370 57.276  1.00 24.76 ? 122 SER A O   1 
ATOM   683  C  CB  . SER A 1 94  ? 7.338   -18.901 57.605  1.00 26.06 ? 122 SER A CB  1 
ATOM   684  O  OG  . SER A 1 94  ? 6.804   -17.594 57.710  1.00 27.41 ? 122 SER A OG  1 
ATOM   685  N  N   . PHE A 1 95  ? 4.569   -18.882 55.606  1.00 25.75 ? 123 PHE A N   1 
ATOM   686  C  CA  . PHE A 1 95  ? 3.114   -18.866 55.722  1.00 23.76 ? 123 PHE A CA  1 
ATOM   687  C  C   . PHE A 1 95  ? 2.507   -20.223 55.369  1.00 27.57 ? 123 PHE A C   1 
ATOM   688  O  O   . PHE A 1 95  ? 2.967   -20.924 54.459  1.00 27.87 ? 123 PHE A O   1 
ATOM   689  C  CB  . PHE A 1 95  ? 2.501   -17.804 54.819  1.00 19.42 ? 123 PHE A CB  1 
ATOM   690  C  CG  . PHE A 1 95  ? 1.011   -17.706 54.953  1.00 24.91 ? 123 PHE A CG  1 
ATOM   691  C  CD1 . PHE A 1 95  ? 0.453   -16.936 55.956  1.00 23.52 ? 123 PHE A CD1 1 
ATOM   692  C  CD2 . PHE A 1 95  ? 0.164   -18.427 54.106  1.00 27.91 ? 123 PHE A CD2 1 
ATOM   693  C  CE1 . PHE A 1 95  ? -0.933  -16.867 56.098  1.00 22.25 ? 123 PHE A CE1 1 
ATOM   694  C  CE2 . PHE A 1 95  ? -1.223  -18.359 54.235  1.00 26.72 ? 123 PHE A CE2 1 
ATOM   695  C  CZ  . PHE A 1 95  ? -1.767  -17.580 55.236  1.00 25.31 ? 123 PHE A CZ  1 
ATOM   696  N  N   . ASP A 1 96  ? 1.451   -20.579 56.085  1.00 24.49 ? 124 ASP A N   1 
ATOM   697  C  CA  . ASP A 1 96  ? 0.720   -21.810 55.808  1.00 26.11 ? 124 ASP A CA  1 
ATOM   698  C  C   . ASP A 1 96  ? -0.767  -21.573 56.051  1.00 27.53 ? 124 ASP A C   1 
ATOM   699  O  O   . ASP A 1 96  ? -1.144  -21.072 57.116  1.00 29.18 ? 124 ASP A O   1 
ATOM   700  C  CB  . ASP A 1 96  ? 1.260   -22.950 56.680  1.00 29.18 ? 124 ASP A CB  1 
ATOM   701  C  CG  . ASP A 1 96  ? 0.440   -24.202 56.566  1.00 32.06 ? 124 ASP A CG  1 
ATOM   702  O  OD1 . ASP A 1 96  ? 0.606   -24.935 55.565  1.00 40.48 ? 124 ASP A OD1 1 
ATOM   703  O  OD2 . ASP A 1 96  ? -0.336  -24.469 57.493  1.00 31.03 ? 124 ASP A OD2 1 
ATOM   704  N  N   . HIS A 1 97  ? -1.604  -21.897 55.054  1.00 27.27 ? 125 HIS A N   1 
ATOM   705  C  CA  . HIS A 1 97  ? -3.049  -21.674 55.191  1.00 28.02 ? 125 HIS A CA  1 
ATOM   706  C  C   . HIS A 1 97  ? -3.580  -22.312 56.468  1.00 27.09 ? 125 HIS A C   1 
ATOM   707  O  O   . HIS A 1 97  ? -4.272  -21.667 57.262  1.00 23.96 ? 125 HIS A O   1 
ATOM   708  C  CB  . HIS A 1 97  ? -3.826  -22.248 53.997  1.00 31.53 ? 125 HIS A CB  1 
ATOM   709  C  CG  . HIS A 1 97  ? -3.604  -21.538 52.695  1.00 32.39 ? 125 HIS A CG  1 
ATOM   710  N  ND1 . HIS A 1 97  ? -4.246  -20.362 52.362  1.00 35.70 ? 125 HIS A ND1 1 
ATOM   711  C  CD2 . HIS A 1 97  ? -2.853  -21.872 51.616  1.00 32.62 ? 125 HIS A CD2 1 
ATOM   712  C  CE1 . HIS A 1 97  ? -3.877  -19.987 51.149  1.00 28.42 ? 125 HIS A CE1 1 
ATOM   713  N  NE2 . HIS A 1 97  ? -3.030  -20.884 50.675  1.00 39.80 ? 125 HIS A NE2 1 
ATOM   714  N  N   . GLY A 1 98  ? -3.269  -23.593 56.673  1.00 27.56 ? 126 GLY A N   1 
ATOM   715  C  CA  . GLY A 1 98  ? -3.821  -24.308 57.815  1.00 27.90 ? 126 GLY A CA  1 
ATOM   716  C  C   . GLY A 1 98  ? -3.321  -23.778 59.143  1.00 26.22 ? 126 GLY A C   1 
ATOM   717  O  O   . GLY A 1 98  ? -4.094  -23.669 60.101  1.00 27.22 ? 126 GLY A O   1 
ATOM   718  N  N   . SER A 1 99  ? -2.020  -23.450 59.229  1.00 24.64 ? 127 SER A N   1 
ATOM   719  C  CA  . SER A 1 99  ? -1.506  -22.856 60.457  1.00 21.53 ? 127 SER A CA  1 
ATOM   720  C  C   . SER A 1 99  ? -2.221  -21.552 60.763  1.00 23.59 ? 127 SER A C   1 
ATOM   721  O  O   . SER A 1 99  ? -2.582  -21.278 61.912  1.00 24.04 ? 127 SER A O   1 
ATOM   722  C  CB  . SER A 1 99  ? 0.002   -22.603 60.347  1.00 27.70 ? 127 SER A CB  1 
ATOM   723  O  OG  . SER A 1 99  ? 0.714   -23.805 60.072  1.00 30.66 ? 127 SER A OG  1 
ATOM   724  N  N   . CYS A 1 100 ? -2.423  -20.736 59.743  1.00 22.92 ? 128 CYS A N   1 
ATOM   725  C  CA  . CYS A 1 100 ? -3.015  -19.421 59.959  1.00 21.93 ? 128 CYS A CA  1 
ATOM   726  C  C   . CYS A 1 100 ? -4.480  -19.532 60.371  1.00 22.84 ? 128 CYS A C   1 
ATOM   727  O  O   . CYS A 1 100 ? -4.934  -18.837 61.293  1.00 21.88 ? 128 CYS A O   1 
ATOM   728  C  CB  . CYS A 1 100 ? -2.846  -18.596 58.693  1.00 20.48 ? 128 CYS A CB  1 
ATOM   729  S  SG  . CYS A 1 100 ? -3.417  -16.877 58.884  1.00 24.53 ? 128 CYS A SG  1 
ATOM   730  N  N   . ARG A 1 101 ? -5.242  -20.406 59.722  1.00 26.92 ? 129 ARG A N   1 
ATOM   731  C  CA  . ARG A 1 101 ? -6.641  -20.550 60.118  1.00 25.55 ? 129 ARG A CA  1 
ATOM   732  C  C   . ARG A 1 101 ? -6.761  -21.173 61.505  1.00 27.72 ? 129 ARG A C   1 
ATOM   733  O  O   . ARG A 1 101 ? -7.595  -20.747 62.311  1.00 25.68 ? 129 ARG A O   1 
ATOM   734  C  CB  . ARG A 1 101 ? -7.400  -21.357 59.070  1.00 28.07 ? 129 ARG A CB  1 
ATOM   735  C  CG  . ARG A 1 101 ? -7.467  -20.624 57.741  1.00 30.73 ? 129 ARG A CG  1 
ATOM   736  C  CD  . ARG A 1 101 ? -8.624  -21.112 56.900  1.00 36.27 ? 129 ARG A CD  1 
ATOM   737  N  NE  . ARG A 1 101 ? -9.021  -20.112 55.907  1.00 40.62 ? 129 ARG A NE  1 
ATOM   738  C  CZ  . ARG A 1 101 ? -8.468  -19.995 54.700  1.00 39.15 ? 129 ARG A CZ  1 
ATOM   739  N  NH1 . ARG A 1 101 ? -7.475  -20.812 54.324  1.00 35.93 ? 129 ARG A NH1 1 
ATOM   740  N  NH2 . ARG A 1 101 ? -8.897  -19.056 53.873  1.00 28.64 ? 129 ARG A NH2 1 
ATOM   741  N  N   . SER A 1 102 ? -5.905  -22.148 61.822  1.00 25.16 ? 130 SER A N   1 
ATOM   742  C  CA  . SER A 1 102 ? -5.927  -22.736 63.156  1.00 25.97 ? 130 SER A CA  1 
ATOM   743  C  C   . SER A 1 102 ? -5.557  -21.712 64.220  1.00 26.28 ? 130 SER A C   1 
ATOM   744  O  O   . SER A 1 102 ? -6.182  -21.662 65.288  1.00 26.33 ? 130 SER A O   1 
ATOM   745  C  CB  . SER A 1 102 ? -4.978  -23.933 63.220  1.00 31.54 ? 130 SER A CB  1 
ATOM   746  O  OG  . SER A 1 102 ? -5.019  -24.536 64.505  1.00 36.29 ? 130 SER A OG  1 
ATOM   747  N  N   . PHE A 1 103 ? -4.513  -20.916 63.963  1.00 23.85 ? 131 PHE A N   1 
ATOM   748  C  CA  . PHE A 1 103 ? -4.131  -19.857 64.889  1.00 21.19 ? 131 PHE A CA  1 
ATOM   749  C  C   . PHE A 1 103 ? -5.303  -18.922 65.137  1.00 22.44 ? 131 PHE A C   1 
ATOM   750  O  O   . PHE A 1 103 ? -5.651  -18.619 66.288  1.00 22.07 ? 131 PHE A O   1 
ATOM   751  C  CB  . PHE A 1 103 ? -2.922  -19.090 64.325  1.00 21.02 ? 131 PHE A CB  1 
ATOM   752  C  CG  . PHE A 1 103 ? -2.468  -17.941 65.184  1.00 23.60 ? 131 PHE A CG  1 
ATOM   753  C  CD1 . PHE A 1 103 ? -3.168  -16.747 65.193  1.00 24.39 ? 131 PHE A CD1 1 
ATOM   754  C  CD2 . PHE A 1 103 ? -1.308  -18.028 65.933  1.00 23.08 ? 131 PHE A CD2 1 
ATOM   755  C  CE1 . PHE A 1 103 ? -2.737  -15.678 65.981  1.00 23.94 ? 131 PHE A CE1 1 
ATOM   756  C  CE2 . PHE A 1 103 ? -0.874  -16.972 66.718  1.00 21.11 ? 131 PHE A CE2 1 
ATOM   757  C  CZ  . PHE A 1 103 ? -1.588  -15.793 66.736  1.00 21.68 ? 131 PHE A CZ  1 
ATOM   758  N  N   . PHE A 1 104 ? -5.927  -18.446 64.066  1.00 21.36 ? 132 PHE A N   1 
ATOM   759  C  CA  . PHE A 1 104 ? -6.986  -17.456 64.249  1.00 22.28 ? 132 PHE A CA  1 
ATOM   760  C  C   . PHE A 1 104 ? -8.219  -18.067 64.915  1.00 25.62 ? 132 PHE A C   1 
ATOM   761  O  O   . PHE A 1 104 ? -8.811  -17.456 65.811  1.00 22.78 ? 132 PHE A O   1 
ATOM   762  C  CB  . PHE A 1 104 ? -7.351  -16.814 62.919  1.00 27.24 ? 132 PHE A CB  1 
ATOM   763  C  CG  . PHE A 1 104 ? -8.193  -15.566 63.069  1.00 26.73 ? 132 PHE A CG  1 
ATOM   764  C  CD1 . PHE A 1 104 ? -7.594  -14.319 63.196  1.00 23.75 ? 132 PHE A CD1 1 
ATOM   765  C  CD2 . PHE A 1 104 ? -9.581  -15.638 63.102  1.00 28.36 ? 132 PHE A CD2 1 
ATOM   766  C  CE1 . PHE A 1 104 ? -8.340  -13.152 63.341  1.00 29.04 ? 132 PHE A CE1 1 
ATOM   767  C  CE2 . PHE A 1 104 ? -10.361 -14.454 63.253  1.00 29.03 ? 132 PHE A CE2 1 
ATOM   768  C  CZ  . PHE A 1 104 ? -9.723  -13.186 63.359  1.00 24.59 ? 132 PHE A CZ  1 
ATOM   769  N  N   . SER A 1 105 ? -8.614  -19.279 64.514  1.00 27.61 ? 133 SER A N   1 
ATOM   770  C  CA  . SER A 1 105 ? -9.758  -19.909 65.172  1.00 27.12 ? 133 SER A CA  1 
ATOM   771  C  C   . SER A 1 105 ? -9.485  -20.105 66.661  1.00 28.07 ? 133 SER A C   1 
ATOM   772  O  O   . SER A 1 105 ? -10.371 -19.886 67.494  1.00 28.70 ? 133 SER A O   1 
ATOM   773  C  CB  . SER A 1 105 ? -10.088 -21.246 64.498  1.00 30.32 ? 133 SER A CB  1 
ATOM   774  O  OG  . SER A 1 105 ? -10.092 -22.282 65.462  1.00 44.85 ? 133 SER A OG  1 
ATOM   775  N  N   . SER A 1 106 ? -8.233  -20.429 67.022  1.00 24.16 ? 134 SER A N   1 
ATOM   776  C  CA  . SER A 1 106 ? -7.883  -20.720 68.409  1.00 25.32 ? 134 SER A CA  1 
ATOM   777  C  C   . SER A 1 106 ? -7.765  -19.459 69.258  1.00 27.27 ? 134 SER A C   1 
ATOM   778  O  O   . SER A 1 106 ? -8.292  -19.401 70.377  1.00 27.41 ? 134 SER A O   1 
ATOM   779  C  CB  . SER A 1 106 ? -6.567  -21.508 68.457  1.00 26.34 ? 134 SER A CB  1 
ATOM   780  O  OG  . SER A 1 106 ? -6.117  -21.623 69.793  1.00 30.04 ? 134 SER A OG  1 
ATOM   781  N  N   . HIS A 1 107 ? -7.067  -18.443 68.750  1.00 23.86 ? 135 HIS A N   1 
ATOM   782  C  CA  . HIS A 1 107 ? -6.696  -17.277 69.543  1.00 27.69 ? 135 HIS A CA  1 
ATOM   783  C  C   . HIS A 1 107 ? -7.441  -16.010 69.162  1.00 25.96 ? 135 HIS A C   1 
ATOM   784  O  O   . HIS A 1 107 ? -7.460  -15.066 69.959  1.00 29.83 ? 135 HIS A O   1 
ATOM   785  C  CB  . HIS A 1 107 ? -5.186  -16.998 69.429  1.00 25.15 ? 135 HIS A CB  1 
ATOM   786  C  CG  . HIS A 1 107 ? -4.331  -18.200 69.648  1.00 27.02 ? 135 HIS A CG  1 
ATOM   787  N  ND1 . HIS A 1 107 ? -4.287  -18.874 70.848  1.00 27.72 ? 135 HIS A ND1 1 
ATOM   788  C  CD2 . HIS A 1 107 ? -3.466  -18.837 68.826  1.00 23.86 ? 135 HIS A CD2 1 
ATOM   789  C  CE1 . HIS A 1 107 ? -3.439  -19.882 70.754  1.00 27.19 ? 135 HIS A CE1 1 
ATOM   790  N  NE2 . HIS A 1 107 ? -2.944  -19.895 69.530  1.00 28.90 ? 135 HIS A NE2 1 
ATOM   791  N  N   . GLY A 1 108 ? -8.089  -15.979 68.006  1.00 25.68 ? 136 GLY A N   1 
ATOM   792  C  CA  . GLY A 1 108 ? -8.625  -14.733 67.508  1.00 23.90 ? 136 GLY A CA  1 
ATOM   793  C  C   . GLY A 1 108 ? -7.479  -13.847 67.029  1.00 24.73 ? 136 GLY A C   1 
ATOM   794  O  O   . GLY A 1 108 ? -6.316  -14.261 66.925  1.00 22.37 ? 136 GLY A O   1 
ATOM   795  N  N   . LEU A 1 109 ? -7.827  -12.596 66.752  1.00 20.09 ? 137 LEU A N   1 
ATOM   796  C  CA  . LEU A 1 109 ? -6.857  -11.636 66.225  1.00 20.61 ? 137 LEU A CA  1 
ATOM   797  C  C   . LEU A 1 109 ? -5.687  -11.433 67.182  1.00 20.05 ? 137 LEU A C   1 
ATOM   798  O  O   . LEU A 1 109 ? -5.875  -11.140 68.369  1.00 20.15 ? 137 LEU A O   1 
ATOM   799  C  CB  . LEU A 1 109 ? -7.548  -10.293 65.959  1.00 19.48 ? 137 LEU A CB  1 
ATOM   800  C  CG  . LEU A 1 109 ? -6.608  -9.152  65.542  1.00 19.00 ? 137 LEU A CG  1 
ATOM   801  C  CD1 . LEU A 1 109 ? -6.034  -9.416  64.172  1.00 20.31 ? 137 LEU A CD1 1 
ATOM   802  C  CD2 . LEU A 1 109 ? -7.392  -7.812  65.552  1.00 19.37 ? 137 LEU A CD2 1 
ATOM   803  N  N   . GLY A 1 110 ? -4.474  -11.576 66.671  1.00 18.55 ? 138 GLY A N   1 
ATOM   804  C  CA  . GLY A 1 110 ? -3.325  -11.392 67.535  1.00 22.22 ? 138 GLY A CA  1 
ATOM   805  C  C   . GLY A 1 110 ? -2.018  -11.496 66.776  1.00 19.79 ? 138 GLY A C   1 
ATOM   806  O  O   . GLY A 1 110 ? -1.985  -11.671 65.548  1.00 20.80 ? 138 GLY A O   1 
ATOM   807  N  N   . VAL A 1 111 ? -0.935  -11.414 67.545  1.00 18.88 ? 139 VAL A N   1 
ATOM   808  C  CA  . VAL A 1 111 ? 0.417   -11.404 66.997  1.00 17.25 ? 139 VAL A CA  1 
ATOM   809  C  C   . VAL A 1 111 ? 0.885   -12.839 66.764  1.00 17.29 ? 139 VAL A C   1 
ATOM   810  O  O   . VAL A 1 111 ? 0.956   -13.639 67.699  1.00 19.41 ? 139 VAL A O   1 
ATOM   811  C  CB  . VAL A 1 111 ? 1.390   -10.661 67.924  1.00 16.71 ? 139 VAL A CB  1 
ATOM   812  C  CG1 . VAL A 1 111 ? 2.828   -10.873 67.460  1.00 15.69 ? 139 VAL A CG1 1 
ATOM   813  C  CG2 . VAL A 1 111 ? 1.060   -9.130  67.976  1.00 18.21 ? 139 VAL A CG2 1 
ATOM   814  N  N   . ARG A 1 112 ? 1.211   -13.157 65.520  1.00 18.05 ? 140 ARG A N   1 
ATOM   815  C  CA  . ARG A 1 112 ? 1.863   -14.412 65.173  1.00 17.96 ? 140 ARG A CA  1 
ATOM   816  C  C   . ARG A 1 112 ? 3.377   -14.322 65.325  1.00 21.37 ? 140 ARG A C   1 
ATOM   817  O  O   . ARG A 1 112 ? 4.013   -15.268 65.826  1.00 20.71 ? 140 ARG A O   1 
ATOM   818  C  CB  . ARG A 1 112 ? 1.499   -14.799 63.736  1.00 18.28 ? 140 ARG A CB  1 
ATOM   819  C  CG  . ARG A 1 112 ? 2.289   -15.964 63.113  1.00 20.92 ? 140 ARG A CG  1 
ATOM   820  C  CD  . ARG A 1 112 ? 2.377   -17.224 63.980  1.00 22.48 ? 140 ARG A CD  1 
ATOM   821  N  NE  . ARG A 1 112 ? 3.022   -18.280 63.196  1.00 24.90 ? 140 ARG A NE  1 
ATOM   822  C  CZ  . ARG A 1 112 ? 3.078   -19.563 63.537  1.00 28.23 ? 140 ARG A CZ  1 
ATOM   823  N  NH1 . ARG A 1 112 ? 2.566   -19.978 64.690  1.00 25.82 ? 140 ARG A NH1 1 
ATOM   824  N  NH2 . ARG A 1 112 ? 3.659   -20.432 62.716  1.00 26.13 ? 140 ARG A NH2 1 
ATOM   825  N  N   . ALA A 1 113 ? 3.978   -13.217 64.882  1.00 19.28 ? 141 ALA A N   1 
ATOM   826  C  CA  . ALA A 1 113 ? 5.435   -13.136 64.806  1.00 18.99 ? 141 ALA A CA  1 
ATOM   827  C  C   . ALA A 1 113 ? 5.947   -11.861 65.453  1.00 20.88 ? 141 ALA A C   1 
ATOM   828  O  O   . ALA A 1 113 ? 5.455   -10.755 65.163  1.00 20.44 ? 141 ALA A O   1 
ATOM   829  C  CB  . ALA A 1 113 ? 5.925   -13.199 63.355  1.00 20.38 ? 141 ALA A CB  1 
ATOM   830  N  N   . VAL A 1 114 ? 6.947   -12.019 66.316  1.00 18.65 ? 142 VAL A N   1 
ATOM   831  C  CA  . VAL A 1 114 ? 7.769   -10.916 66.817  1.00 18.11 ? 142 VAL A CA  1 
ATOM   832  C  C   . VAL A 1 114 ? 9.087   -10.999 66.067  1.00 22.55 ? 142 VAL A C   1 
ATOM   833  O  O   . VAL A 1 114 ? 9.861   -11.944 66.270  1.00 24.16 ? 142 VAL A O   1 
ATOM   834  C  CB  . VAL A 1 114 ? 7.993   -11.014 68.335  1.00 21.14 ? 142 VAL A CB  1 
ATOM   835  C  CG1 . VAL A 1 114 ? 9.004   -9.961  68.823  1.00 20.62 ? 142 VAL A CG1 1 
ATOM   836  C  CG2 . VAL A 1 114 ? 6.679   -10.932 69.108  1.00 23.31 ? 142 VAL A CG2 1 
ATOM   837  N  N   . ALA A 1 115 ? 9.348   -10.057 65.162  1.00 21.96 ? 143 ALA A N   1 
ATOM   838  C  CA  . ALA A 1 115 ? 10.505  -10.175 64.289  1.00 22.62 ? 143 ALA A CA  1 
ATOM   839  C  C   . ALA A 1 115 ? 11.587  -9.223  64.765  1.00 21.95 ? 143 ALA A C   1 
ATOM   840  O  O   . ALA A 1 115 ? 11.309  -8.065  65.073  1.00 22.94 ? 143 ALA A O   1 
ATOM   841  C  CB  . ALA A 1 115 ? 10.158  -9.893  62.831  1.00 20.54 ? 143 ALA A CB  1 
ATOM   842  N  N   . ILE A 1 116 ? 12.806  -9.737  64.868  1.00 22.69 ? 144 ILE A N   1 
ATOM   843  C  CA  . ILE A 1 116 ? 13.975  -8.930  65.187  1.00 22.68 ? 144 ILE A CA  1 
ATOM   844  C  C   . ILE A 1 116 ? 14.971  -9.028  64.040  1.00 26.05 ? 144 ILE A C   1 
ATOM   845  O  O   . ILE A 1 116 ? 15.106  -10.085 63.409  1.00 26.71 ? 144 ILE A O   1 
ATOM   846  C  CB  . ILE A 1 116 ? 14.631  -9.356  66.512  1.00 25.94 ? 144 ILE A CB  1 
ATOM   847  C  CG1 . ILE A 1 116 ? 14.976  -10.843 66.498  1.00 29.15 ? 144 ILE A CG1 1 
ATOM   848  C  CG2 . ILE A 1 116 ? 13.734  -9.001  67.693  1.00 25.25 ? 144 ILE A CG2 1 
ATOM   849  C  CD1 . ILE A 1 116 ? 15.903  -11.252 67.659  1.00 29.14 ? 144 ILE A CD1 1 
ATOM   850  N  N   . GLU A 1 117 ? 15.641  -7.910  63.747  1.00 26.33 ? 145 GLU A N   1 
ATOM   851  C  CA  . GLU A 1 117 ? 16.680  -7.917  62.731  1.00 27.13 ? 145 GLU A CA  1 
ATOM   852  C  C   . GLU A 1 117 ? 17.975  -8.393  63.363  1.00 28.21 ? 145 GLU A C   1 
ATOM   853  O  O   . GLU A 1 117 ? 18.342  -7.963  64.462  1.00 27.47 ? 145 GLU A O   1 
ATOM   854  C  CB  . GLU A 1 117 ? 16.887  -6.542  62.100  1.00 29.16 ? 145 GLU A CB  1 
ATOM   855  C  CG  . GLU A 1 117 ? 17.943  -6.581  60.992  1.00 32.44 ? 145 GLU A CG  1 
ATOM   856  C  CD  . GLU A 1 117 ? 18.234  -5.215  60.374  1.00 40.84 ? 145 GLU A CD  1 
ATOM   857  O  OE1 . GLU A 1 117 ? 19.130  -5.127  59.505  1.00 38.73 ? 145 GLU A OE1 1 
ATOM   858  O  OE2 . GLU A 1 117 ? 17.558  -4.238  60.744  1.00 39.85 ? 145 GLU A OE2 1 
ATOM   859  N  N   . VAL A 1 118 ? 18.640  -9.315  62.684  1.00 28.14 ? 146 VAL A N   1 
ATOM   860  C  CA  . VAL A 1 118 ? 19.879  -9.893  63.163  1.00 29.50 ? 146 VAL A CA  1 
ATOM   861  C  C   . VAL A 1 118 ? 20.920  -9.772  62.073  1.00 28.98 ? 146 VAL A C   1 
ATOM   862  O  O   . VAL A 1 118 ? 20.637  -9.409  60.929  1.00 25.10 ? 146 VAL A O   1 
ATOM   863  C  CB  . VAL A 1 118 ? 19.721  -11.366 63.569  1.00 28.70 ? 146 VAL A CB  1 
ATOM   864  C  CG1 . VAL A 1 118 ? 18.710  -11.502 64.692  1.00 28.94 ? 146 VAL A CG1 1 
ATOM   865  C  CG2 . VAL A 1 118 ? 19.326  -12.181 62.360  1.00 27.81 ? 146 VAL A CG2 1 
ATOM   866  N  N   . GLU A 1 119 ? 22.149  -10.100 62.456  1.00 32.28 ? 147 GLU A N   1 
ATOM   867  C  CA  . GLU A 1 119 ? 23.246  -10.021 61.519  1.00 35.43 ? 147 GLU A CA  1 
ATOM   868  C  C   . GLU A 1 119 ? 23.130  -11.115 60.466  1.00 29.95 ? 147 GLU A C   1 
ATOM   869  O  O   . GLU A 1 119 ? 23.364  -10.870 59.276  1.00 32.51 ? 147 GLU A O   1 
ATOM   870  C  CB  . GLU A 1 119 ? 24.543  -10.107 62.327  1.00 35.18 ? 147 GLU A CB  1 
ATOM   871  C  CG  . GLU A 1 119 ? 25.798  -10.102 61.569  1.00 44.28 ? 147 GLU A CG  1 
ATOM   872  C  CD  . GLU A 1 119 ? 27.032  -10.130 62.493  1.00 52.46 ? 147 GLU A CD  1 
ATOM   873  O  OE1 . GLU A 1 119 ? 27.671  -9.050  62.623  1.00 50.36 ? 147 GLU A OE1 1 
ATOM   874  O  OE2 . GLU A 1 119 ? 27.374  -11.228 63.031  1.00 46.48 ? 147 GLU A OE2 1 
ATOM   875  N  N   . ASP A 1 120 ? 22.718  -12.315 60.875  1.00 28.22 ? 148 ASP A N   1 
ATOM   876  C  CA  . ASP A 1 120 ? 22.679  -13.466 59.975  1.00 31.41 ? 148 ASP A CA  1 
ATOM   877  C  C   . ASP A 1 120 ? 21.580  -14.396 60.487  1.00 32.39 ? 148 ASP A C   1 
ATOM   878  O  O   . ASP A 1 120 ? 21.779  -15.104 61.480  1.00 29.67 ? 148 ASP A O   1 
ATOM   879  C  CB  . ASP A 1 120 ? 24.048  -14.144 59.935  1.00 35.48 ? 148 ASP A CB  1 
ATOM   880  C  CG  . ASP A 1 120 ? 24.084  -15.403 59.058  1.00 40.03 ? 148 ASP A CG  1 
ATOM   881  O  OD1 . ASP A 1 120 ? 23.084  -15.739 58.385  1.00 41.95 ? 148 ASP A OD1 1 
ATOM   882  O  OD2 . ASP A 1 120 ? 25.142  -16.073 59.046  1.00 43.36 ? 148 ASP A OD2 1 
ATOM   883  N  N   . ALA A 1 121 ? 20.421  -14.370 59.810  1.00 32.78 ? 149 ALA A N   1 
ATOM   884  C  CA  . ALA A 1 121 ? 19.261  -15.129 60.272  1.00 28.61 ? 149 ALA A CA  1 
ATOM   885  C  C   . ALA A 1 121 ? 19.511  -16.630 60.243  1.00 30.77 ? 149 ALA A C   1 
ATOM   886  O  O   . ALA A 1 121 ? 19.010  -17.362 61.109  1.00 30.64 ? 149 ALA A O   1 
ATOM   887  C  CB  . ALA A 1 121 ? 18.038  -14.775 59.427  1.00 27.94 ? 149 ALA A CB  1 
ATOM   888  N  N   . GLU A 1 122 ? 20.282  -17.113 59.271  1.00 34.08 ? 150 GLU A N   1 
ATOM   889  C  CA  . GLU A 1 122 ? 20.582  -18.542 59.255  1.00 35.87 ? 150 GLU A CA  1 
ATOM   890  C  C   . GLU A 1 122 ? 21.424  -18.942 60.459  1.00 31.78 ? 150 GLU A C   1 
ATOM   891  O  O   . GLU A 1 122 ? 21.141  -19.951 61.113  1.00 33.57 ? 150 GLU A O   1 
ATOM   892  C  CB  . GLU A 1 122 ? 21.284  -18.927 57.955  1.00 38.93 ? 150 GLU A CB  1 
ATOM   893  C  CG  . GLU A 1 122 ? 21.777  -20.374 57.922  1.00 39.61 ? 150 GLU A CG  1 
ATOM   894  C  CD  . GLU A 1 122 ? 22.008  -20.884 56.509  1.00 49.31 ? 150 GLU A CD  1 
ATOM   895  O  OE1 . GLU A 1 122 ? 22.059  -22.127 56.326  1.00 59.85 ? 150 GLU A OE1 1 
ATOM   896  O  OE2 . GLU A 1 122 ? 22.106  -20.031 55.591  1.00 60.48 ? 150 GLU A OE2 1 
ATOM   897  N  N   . SER A 1 123 ? 22.478  -18.178 60.765  1.00 30.07 ? 151 SER A N   1 
ATOM   898  C  CA  . SER A 1 123 ? 23.269  -18.522 61.940  1.00 31.88 ? 151 SER A CA  1 
ATOM   899  C  C   . SER A 1 123 ? 22.473  -18.317 63.225  1.00 32.37 ? 151 SER A C   1 
ATOM   900  O  O   . SER A 1 123 ? 22.526  -19.162 64.126  1.00 30.43 ? 151 SER A O   1 
ATOM   901  C  CB  . SER A 1 123 ? 24.591  -17.737 61.971  1.00 36.73 ? 151 SER A CB  1 
ATOM   902  O  OG  . SER A 1 123 ? 24.393  -16.342 62.070  1.00 47.01 ? 151 SER A OG  1 
ATOM   903  N  N   . ALA A 1 124 ? 21.685  -17.231 63.320  1.00 32.99 ? 152 ALA A N   1 
ATOM   904  C  CA  . ALA A 1 124 ? 20.821  -17.070 64.491  1.00 32.67 ? 152 ALA A CA  1 
ATOM   905  C  C   . ALA A 1 124 ? 19.893  -18.266 64.663  1.00 26.24 ? 152 ALA A C   1 
ATOM   906  O  O   . ALA A 1 124 ? 19.640  -18.708 65.788  1.00 27.44 ? 152 ALA A O   1 
ATOM   907  C  CB  . ALA A 1 124 ? 19.997  -15.779 64.385  1.00 28.46 ? 152 ALA A CB  1 
ATOM   908  N  N   . PHE A 1 125 ? 19.368  -18.798 63.560  1.00 26.72 ? 153 PHE A N   1 
ATOM   909  C  CA  . PHE A 1 125 ? 18.478  -19.951 63.637  1.00 26.06 ? 153 PHE A CA  1 
ATOM   910  C  C   . PHE A 1 125 ? 19.233  -21.200 64.095  1.00 29.40 ? 153 PHE A C   1 
ATOM   911  O  O   . PHE A 1 125 ? 18.773  -21.937 64.977  1.00 29.91 ? 153 PHE A O   1 
ATOM   912  C  CB  . PHE A 1 125 ? 17.832  -20.198 62.273  1.00 27.50 ? 153 PHE A CB  1 
ATOM   913  C  CG  . PHE A 1 125 ? 16.939  -21.427 62.230  1.00 29.49 ? 153 PHE A CG  1 
ATOM   914  C  CD1 . PHE A 1 125 ? 17.453  -22.677 61.870  1.00 34.12 ? 153 PHE A CD1 1 
ATOM   915  C  CD2 . PHE A 1 125 ? 15.594  -21.334 62.552  1.00 29.49 ? 153 PHE A CD2 1 
ATOM   916  C  CE1 . PHE A 1 125 ? 16.630  -23.793 61.831  1.00 31.39 ? 153 PHE A CE1 1 
ATOM   917  C  CE2 . PHE A 1 125 ? 14.763  -22.447 62.518  1.00 27.69 ? 153 PHE A CE2 1 
ATOM   918  C  CZ  . PHE A 1 125 ? 15.280  -23.681 62.153  1.00 33.28 ? 153 PHE A CZ  1 
ATOM   919  N  N   . SER A 1 126 ? 20.377  -21.468 63.476  1.00 32.84 ? 154 SER A N   1 
ATOM   920  C  CA  . SER A 1 126 ? 21.151  -22.656 63.844  1.00 31.16 ? 154 SER A CA  1 
ATOM   921  C  C   . SER A 1 126 ? 21.580  -22.602 65.305  1.00 30.17 ? 154 SER A C   1 
ATOM   922  O  O   . SER A 1 126 ? 21.367  -23.556 66.060  1.00 33.29 ? 154 SER A O   1 
ATOM   923  C  CB  . SER A 1 126 ? 22.351  -22.788 62.914  1.00 39.69 ? 154 SER A CB  1 
ATOM   924  O  OG  . SER A 1 126 ? 21.892  -22.820 61.569  1.00 42.49 ? 154 SER A OG  1 
ATOM   925  N  N   . ILE A 1 127 ? 22.151  -21.473 65.735  1.00 30.35 ? 155 ILE A N   1 
ATOM   926  C  CA  . ILE A 1 127 ? 22.575  -21.345 67.128  1.00 28.21 ? 155 ILE A CA  1 
ATOM   927  C  C   . ILE A 1 127 ? 21.386  -21.452 68.073  1.00 28.96 ? 155 ILE A C   1 
ATOM   928  O  O   . ILE A 1 127 ? 21.470  -22.086 69.133  1.00 26.87 ? 155 ILE A O   1 
ATOM   929  C  CB  . ILE A 1 127 ? 23.348  -20.029 67.330  1.00 31.42 ? 155 ILE A CB  1 
ATOM   930  C  CG1 . ILE A 1 127 ? 24.635  -20.049 66.500  1.00 37.18 ? 155 ILE A CG1 1 
ATOM   931  C  CG2 . ILE A 1 127 ? 23.653  -19.829 68.793  1.00 30.56 ? 155 ILE A CG2 1 
ATOM   932  C  CD1 . ILE A 1 127 ? 25.330  -18.701 66.378  1.00 40.90 ? 155 ILE A CD1 1 
ATOM   933  N  N   . SER A 1 128 ? 20.259  -20.815 67.724  1.00 28.46 ? 156 SER A N   1 
ATOM   934  C  CA  . SER A 1 128 ? 19.080  -20.921 68.577  1.00 29.31 ? 156 SER A CA  1 
ATOM   935  C  C   . SER A 1 128 ? 18.661  -22.372 68.757  1.00 25.96 ? 156 SER A C   1 
ATOM   936  O  O   . SER A 1 128 ? 18.413  -22.821 69.882  1.00 28.24 ? 156 SER A O   1 
ATOM   937  C  CB  . SER A 1 128 ? 17.919  -20.104 67.990  1.00 26.21 ? 156 SER A CB  1 
ATOM   938  O  OG  . SER A 1 128 ? 18.251  -18.731 68.007  1.00 29.32 ? 156 SER A OG  1 
ATOM   939  N  N   . VAL A 1 129 ? 18.565  -23.121 67.656  1.00 25.03 ? 157 VAL A N   1 
ATOM   940  C  CA  . VAL A 1 129 ? 18.102  -24.504 67.750  1.00 31.26 ? 157 VAL A CA  1 
ATOM   941  C  C   . VAL A 1 129 ? 19.144  -25.366 68.454  1.00 29.41 ? 157 VAL A C   1 
ATOM   942  O  O   . VAL A 1 129 ? 18.796  -26.251 69.246  1.00 30.66 ? 157 VAL A O   1 
ATOM   943  C  CB  . VAL A 1 129 ? 17.748  -25.058 66.355  1.00 31.32 ? 157 VAL A CB  1 
ATOM   944  C  CG1 . VAL A 1 129 ? 17.367  -26.551 66.437  1.00 31.14 ? 157 VAL A CG1 1 
ATOM   945  C  CG2 . VAL A 1 129 ? 16.581  -24.276 65.757  1.00 29.74 ? 157 VAL A CG2 1 
ATOM   946  N  N   . ALA A 1 130 ? 20.435  -25.098 68.202  1.00 27.88 ? 158 ALA A N   1 
ATOM   947  C  CA  . ALA A 1 130 ? 21.496  -25.791 68.934  1.00 33.36 ? 158 ALA A CA  1 
ATOM   948  C  C   . ALA A 1 130 ? 21.343  -25.595 70.428  1.00 36.87 ? 158 ALA A C   1 
ATOM   949  O  O   . ALA A 1 130 ? 21.799  -26.433 71.215  1.00 33.70 ? 158 ALA A O   1 
ATOM   950  C  CB  . ALA A 1 130 ? 22.874  -25.297 68.494  1.00 31.23 ? 158 ALA A CB  1 
ATOM   951  N  N   . ASN A 1 131 ? 20.696  -24.498 70.836  1.00 30.33 ? 159 ASN A N   1 
ATOM   952  C  CA  . ASN A 1 131 ? 20.587  -24.125 72.237  1.00 29.73 ? 159 ASN A CA  1 
ATOM   953  C  C   . ASN A 1 131 ? 19.162  -24.231 72.762  1.00 30.82 ? 159 ASN A C   1 
ATOM   954  O  O   . ASN A 1 131 ? 18.786  -23.514 73.692  1.00 38.19 ? 159 ASN A O   1 
ATOM   955  C  CB  . ASN A 1 131 ? 21.152  -22.721 72.446  1.00 30.17 ? 159 ASN A CB  1 
ATOM   956  C  CG  . ASN A 1 131 ? 22.665  -22.711 72.433  1.00 33.67 ? 159 ASN A CG  1 
ATOM   957  O  OD1 . ASN A 1 131 ? 23.286  -23.027 73.442  1.00 39.09 ? 159 ASN A OD1 1 
ATOM   958  N  ND2 . ASN A 1 131 ? 23.267  -22.363 71.295  1.00 32.65 ? 159 ASN A ND2 1 
ATOM   959  N  N   . GLY A 1 132 ? 18.358  -25.124 72.180  1.00 30.82 ? 160 GLY A N   1 
ATOM   960  C  CA  . GLY A 1 132 ? 17.082  -25.497 72.741  1.00 33.60 ? 160 GLY A CA  1 
ATOM   961  C  C   . GLY A 1 132 ? 15.867  -24.924 72.040  1.00 29.37 ? 160 GLY A C   1 
ATOM   962  O  O   . GLY A 1 132 ? 14.746  -25.319 72.375  1.00 27.85 ? 160 GLY A O   1 
ATOM   963  N  N   . ALA A 1 133 ? 16.048  -24.015 71.083  1.00 31.95 ? 161 ALA A N   1 
ATOM   964  C  CA  . ALA A 1 133 ? 14.893  -23.432 70.398  1.00 28.27 ? 161 ALA A CA  1 
ATOM   965  C  C   . ALA A 1 133 ? 14.153  -24.487 69.587  1.00 29.18 ? 161 ALA A C   1 
ATOM   966  O  O   . ALA A 1 133 ? 14.766  -25.285 68.867  1.00 30.09 ? 161 ALA A O   1 
ATOM   967  C  CB  . ALA A 1 133 ? 15.325  -22.308 69.463  1.00 24.79 ? 161 ALA A CB  1 
ATOM   968  N  N   . ILE A 1 134 ? 12.827  -24.469 69.678  1.00 29.05 ? 162 ILE A N   1 
ATOM   969  C  CA  . ILE A 1 134 ? 12.000  -25.342 68.847  1.00 26.32 ? 162 ILE A CA  1 
ATOM   970  C  C   . ILE A 1 134 ? 11.826  -24.690 67.484  1.00 32.20 ? 162 ILE A C   1 
ATOM   971  O  O   . ILE A 1 134 ? 11.253  -23.582 67.385  1.00 25.62 ? 162 ILE A O   1 
ATOM   972  C  CB  . ILE A 1 134 ? 10.636  -25.617 69.483  1.00 29.76 ? 162 ILE A CB  1 
ATOM   973  C  CG1 . ILE A 1 134 ? 10.815  -26.195 70.883  1.00 36.14 ? 162 ILE A CG1 1 
ATOM   974  C  CG2 . ILE A 1 134 ? 9.828   -26.560 68.588  1.00 31.81 ? 162 ILE A CG2 1 
ATOM   975  C  CD1 . ILE A 1 134 ? 9.527   -26.294 71.649  1.00 37.42 ? 162 ILE A CD1 1 
ATOM   976  N  N   . PRO A 1 135 ? 12.302  -25.326 66.416  1.00 26.05 ? 163 PRO A N   1 
ATOM   977  C  CA  . PRO A 1 135 ? 12.207  -24.709 65.089  1.00 24.48 ? 163 PRO A CA  1 
ATOM   978  C  C   . PRO A 1 135 ? 10.765  -24.571 64.638  1.00 29.56 ? 163 PRO A C   1 
ATOM   979  O  O   . PRO A 1 135 ? 9.903   -25.397 64.945  1.00 26.38 ? 163 PRO A O   1 
ATOM   980  C  CB  . PRO A 1 135 ? 12.986  -25.671 64.183  1.00 30.25 ? 163 PRO A CB  1 
ATOM   981  C  CG  . PRO A 1 135 ? 13.042  -26.962 64.935  1.00 32.59 ? 163 PRO A CG  1 
ATOM   982  C  CD  . PRO A 1 135 ? 13.017  -26.612 66.391  1.00 27.30 ? 163 PRO A CD  1 
ATOM   983  N  N   . SER A 1 136 ? 10.500  -23.484 63.929  1.00 27.08 ? 164 SER A N   1 
ATOM   984  C  CA  . SER A 1 136 ? 9.177   -23.269 63.370  1.00 23.90 ? 164 SER A CA  1 
ATOM   985  C  C   . SER A 1 136 ? 9.201   -23.150 61.857  1.00 21.56 ? 164 SER A C   1 
ATOM   986  O  O   . SER A 1 136 ? 8.344   -23.717 61.184  1.00 28.68 ? 164 SER A O   1 
ATOM   987  C  CB  . SER A 1 136 ? 8.545   -22.005 63.987  1.00 23.42 ? 164 SER A CB  1 
ATOM   988  O  OG  . SER A 1 136 ? 7.148   -21.998 63.699  1.00 23.68 ? 164 SER A OG  1 
ATOM   989  N  N   . SER A 1 137 ? 10.173  -22.436 61.300  1.00 27.07 ? 165 SER A N   1 
ATOM   990  C  CA  . SER A 1 137 ? 10.341  -22.358 59.866  1.00 27.10 ? 165 SER A CA  1 
ATOM   991  C  C   . SER A 1 137 ? 11.834  -22.203 59.603  1.00 27.91 ? 165 SER A C   1 
ATOM   992  O  O   . SER A 1 137 ? 12.469  -21.312 60.194  1.00 26.22 ? 165 SER A O   1 
ATOM   993  C  CB  . SER A 1 137 ? 9.569   -21.193 59.250  1.00 33.24 ? 165 SER A CB  1 
ATOM   994  O  OG  . SER A 1 137 ? 9.890   -21.034 57.876  1.00 36.72 ? 165 SER A OG  1 
ATOM   995  N  N   . PRO A 1 138 ? 12.420  -23.035 58.748  1.00 31.86 ? 166 PRO A N   1 
ATOM   996  C  CA  . PRO A 1 138 ? 13.869  -23.003 58.566  1.00 31.47 ? 166 PRO A CA  1 
ATOM   997  C  C   . PRO A 1 138 ? 14.288  -21.773 57.782  1.00 32.58 ? 166 PRO A C   1 
ATOM   998  O  O   . PRO A 1 138 ? 13.442  -21.082 57.180  1.00 33.02 ? 166 PRO A O   1 
ATOM   999  C  CB  . PRO A 1 138 ? 14.158  -24.297 57.789  1.00 37.04 ? 166 PRO A CB  1 
ATOM   1000 C  CG  . PRO A 1 138 ? 12.905  -24.563 57.037  1.00 39.00 ? 166 PRO A CG  1 
ATOM   1001 C  CD  . PRO A 1 138 ? 11.769  -24.053 57.904  1.00 34.78 ? 166 PRO A CD  1 
ATOM   1002 N  N   . PRO A 1 139 ? 15.583  -21.455 57.779  1.00 30.37 ? 167 PRO A N   1 
ATOM   1003 C  CA  . PRO A 1 139 ? 16.042  -20.250 57.077  1.00 33.72 ? 167 PRO A CA  1 
ATOM   1004 C  C   . PRO A 1 139 ? 15.781  -20.368 55.587  1.00 35.88 ? 167 PRO A C   1 
ATOM   1005 O  O   . PRO A 1 139 ? 16.017  -21.411 54.973  1.00 35.22 ? 167 PRO A O   1 
ATOM   1006 C  CB  . PRO A 1 139 ? 17.544  -20.202 57.392  1.00 32.93 ? 167 PRO A CB  1 
ATOM   1007 C  CG  . PRO A 1 139 ? 17.689  -20.985 58.657  1.00 32.22 ? 167 PRO A CG  1 
ATOM   1008 C  CD  . PRO A 1 139 ? 16.679  -22.102 58.519  1.00 32.53 ? 167 PRO A CD  1 
ATOM   1009 N  N   . ILE A 1 140 ? 15.249  -19.299 55.013  1.00 30.63 ? 168 ILE A N   1 
ATOM   1010 C  CA  . ILE A 1 140 ? 14.939  -19.253 53.595  1.00 32.28 ? 168 ILE A CA  1 
ATOM   1011 C  C   . ILE A 1 140 ? 15.471  -17.933 53.082  1.00 36.87 ? 168 ILE A C   1 
ATOM   1012 O  O   . ILE A 1 140 ? 15.264  -16.890 53.715  1.00 36.22 ? 168 ILE A O   1 
ATOM   1013 C  CB  . ILE A 1 140 ? 13.424  -19.395 53.332  1.00 35.03 ? 168 ILE A CB  1 
ATOM   1014 C  CG1 . ILE A 1 140 ? 12.938  -20.797 53.729  1.00 39.49 ? 168 ILE A CG1 1 
ATOM   1015 C  CG2 . ILE A 1 140 ? 13.097  -19.117 51.868  1.00 36.97 ? 168 ILE A CG2 1 
ATOM   1016 C  CD1 . ILE A 1 140 ? 11.499  -20.845 54.238  1.00 42.35 ? 168 ILE A CD1 1 
ATOM   1017 N  N   . VAL A 1 141 ? 16.199  -17.978 51.972  1.00 36.07 ? 169 VAL A N   1 
ATOM   1018 C  CA  . VAL A 1 141 ? 16.799  -16.782 51.391  1.00 39.54 ? 169 VAL A CA  1 
ATOM   1019 C  C   . VAL A 1 141 ? 15.872  -16.282 50.296  1.00 41.60 ? 169 VAL A C   1 
ATOM   1020 O  O   . VAL A 1 141 ? 15.512  -17.035 49.383  1.00 43.36 ? 169 VAL A O   1 
ATOM   1021 C  CB  . VAL A 1 141 ? 18.215  -17.059 50.855  1.00 38.51 ? 169 VAL A CB  1 
ATOM   1022 C  CG1 . VAL A 1 141 ? 18.855  -15.779 50.347  1.00 43.92 ? 169 VAL A CG1 1 
ATOM   1023 C  CG2 . VAL A 1 141 ? 19.067  -17.655 51.946  1.00 37.13 ? 169 VAL A CG2 1 
ATOM   1024 N  N   . LEU A 1 142 ? 15.467  -15.020 50.401  1.00 38.62 ? 170 LEU A N   1 
ATOM   1025 C  CA  . LEU A 1 142 ? 14.528  -14.413 49.471  1.00 40.33 ? 170 LEU A CA  1 
ATOM   1026 C  C   . LEU A 1 142 ? 15.315  -13.547 48.490  1.00 44.16 ? 170 LEU A C   1 
ATOM   1027 O  O   . LEU A 1 142 ? 15.951  -12.567 48.892  1.00 40.42 ? 170 LEU A O   1 
ATOM   1028 C  CB  . LEU A 1 142 ? 13.491  -13.589 50.232  1.00 38.14 ? 170 LEU A CB  1 
ATOM   1029 C  CG  . LEU A 1 142 ? 12.815  -14.288 51.413  1.00 37.65 ? 170 LEU A CG  1 
ATOM   1030 C  CD1 . LEU A 1 142 ? 12.070  -13.265 52.264  1.00 39.47 ? 170 LEU A CD1 1 
ATOM   1031 C  CD2 . LEU A 1 142 ? 11.861  -15.357 50.914  1.00 37.15 ? 170 LEU A CD2 1 
ATOM   1032 N  N   . ASN A 1 143 ? 15.285  -13.927 47.207  1.00 48.03 ? 171 ASN A N   1 
ATOM   1033 C  CA  . ASN A 1 143 ? 15.885  -13.142 46.121  1.00 47.10 ? 171 ASN A CA  1 
ATOM   1034 C  C   . ASN A 1 143 ? 17.353  -12.803 46.393  1.00 48.22 ? 171 ASN A C   1 
ATOM   1035 O  O   . ASN A 1 143 ? 17.840  -11.727 46.033  1.00 48.24 ? 171 ASN A O   1 
ATOM   1036 C  CB  . ASN A 1 143 ? 15.080  -11.868 45.864  1.00 47.80 ? 171 ASN A CB  1 
ATOM   1037 C  CG  . ASN A 1 143 ? 15.296  -11.312 44.466  1.00 54.77 ? 171 ASN A CG  1 
ATOM   1038 O  OD1 . ASN A 1 143 ? 15.501  -12.061 43.511  1.00 55.14 ? 171 ASN A OD1 1 
ATOM   1039 N  ND2 . ASN A 1 143 ? 15.259  -9.989  44.342  1.00 54.16 ? 171 ASN A ND2 1 
ATOM   1040 N  N   . GLU A 1 144 ? 18.066  -13.728 47.040  1.00 47.41 ? 172 GLU A N   1 
ATOM   1041 C  CA  . GLU A 1 144 ? 19.489  -13.549 47.362  1.00 49.39 ? 172 GLU A CA  1 
ATOM   1042 C  C   . GLU A 1 144 ? 19.738  -12.255 48.136  1.00 49.89 ? 172 GLU A C   1 
ATOM   1043 O  O   . GLU A 1 144 ? 20.830  -11.680 48.080  1.00 50.56 ? 172 GLU A O   1 
ATOM   1044 C  CB  . GLU A 1 144 ? 20.358  -13.577 46.099  1.00 51.61 ? 172 GLU A CB  1 
ATOM   1045 C  CG  . GLU A 1 144 ? 20.058  -14.705 45.126  1.00 57.82 ? 172 GLU A CG  1 
ATOM   1046 C  CD  . GLU A 1 144 ? 20.836  -14.559 43.826  1.00 66.58 ? 172 GLU A CD  1 
ATOM   1047 O  OE1 . GLU A 1 144 ? 22.056  -14.305 43.891  1.00 67.68 ? 172 GLU A OE1 1 
ATOM   1048 O  OE2 . GLU A 1 144 ? 20.231  -14.696 42.740  1.00 71.76 ? 172 GLU A OE2 1 
ATOM   1049 N  N   . ALA A 1 145 ? 18.736  -11.783 48.864  1.00 45.28 ? 173 ALA A N   1 
ATOM   1050 C  CA  . ALA A 1 145 ? 18.808  -10.450 49.456  1.00 44.15 ? 173 ALA A CA  1 
ATOM   1051 C  C   . ALA A 1 145 ? 18.439  -10.423 50.928  1.00 41.95 ? 173 ALA A C   1 
ATOM   1052 O  O   . ALA A 1 145 ? 19.042  -9.670  51.698  1.00 38.02 ? 173 ALA A O   1 
ATOM   1053 C  CB  . ALA A 1 145 ? 17.893  -9.498  48.675  1.00 42.42 ? 173 ALA A CB  1 
ATOM   1054 N  N   . VAL A 1 146 ? 17.450  -11.209 51.338  1.00 37.41 ? 174 VAL A N   1 
ATOM   1055 C  CA  . VAL A 1 146 ? 16.972  -11.224 52.712  1.00 35.15 ? 174 VAL A CA  1 
ATOM   1056 C  C   . VAL A 1 146 ? 16.827  -12.673 53.146  1.00 32.40 ? 174 VAL A C   1 
ATOM   1057 O  O   . VAL A 1 146 ? 16.364  -13.517 52.372  1.00 37.44 ? 174 VAL A O   1 
ATOM   1058 C  CB  . VAL A 1 146 ? 15.625  -10.477 52.855  1.00 34.44 ? 174 VAL A CB  1 
ATOM   1059 C  CG1 . VAL A 1 146 ? 15.268  -10.325 54.322  1.00 34.19 ? 174 VAL A CG1 1 
ATOM   1060 C  CG2 . VAL A 1 146 ? 15.704  -9.117  52.188  1.00 35.80 ? 174 VAL A CG2 1 
ATOM   1061 N  N   . THR A 1 147 ? 17.221  -12.965 54.379  1.00 32.34 ? 175 THR A N   1 
ATOM   1062 C  CA  . THR A 1 147 ? 17.015  -14.286 54.947  1.00 36.25 ? 175 THR A CA  1 
ATOM   1063 C  C   . THR A 1 147 ? 16.067  -14.179 56.131  1.00 32.15 ? 175 THR A C   1 
ATOM   1064 O  O   . THR A 1 147 ? 16.202  -13.284 56.967  1.00 27.92 ? 175 THR A O   1 
ATOM   1065 C  CB  . THR A 1 147 ? 18.338  -14.936 55.386  1.00 37.01 ? 175 THR A CB  1 
ATOM   1066 O  OG1 . THR A 1 147 ? 19.242  -14.980 54.268  1.00 34.90 ? 175 THR A OG1 1 
ATOM   1067 C  CG2 . THR A 1 147 ? 18.085  -16.358 55.903  1.00 34.26 ? 175 THR A CG2 1 
ATOM   1068 N  N   . ILE A 1 148 ? 15.115  -15.103 56.195  1.00 30.99 ? 176 ILE A N   1 
ATOM   1069 C  CA  . ILE A 1 148 ? 14.123  -15.140 57.255  1.00 30.08 ? 176 ILE A CA  1 
ATOM   1070 C  C   . ILE A 1 148 ? 14.042  -16.557 57.816  1.00 28.21 ? 176 ILE A C   1 
ATOM   1071 O  O   . ILE A 1 148 ? 14.116  -17.539 57.067  1.00 30.42 ? 176 ILE A O   1 
ATOM   1072 C  CB  . ILE A 1 148 ? 12.755  -14.661 56.727  1.00 31.86 ? 176 ILE A CB  1 
ATOM   1073 C  CG1 . ILE A 1 148 ? 11.692  -14.794 57.800  1.00 31.34 ? 176 ILE A CG1 1 
ATOM   1074 C  CG2 . ILE A 1 148 ? 12.352  -15.452 55.482  1.00 32.66 ? 176 ILE A CG2 1 
ATOM   1075 C  CD1 . ILE A 1 148 ? 10.327  -14.370 57.281  1.00 36.73 ? 176 ILE A CD1 1 
ATOM   1076 N  N   . ALA A 1 149 ? 13.898  -16.658 59.138  1.00 22.58 ? 177 ALA A N   1 
ATOM   1077 C  CA  . ALA A 1 149 ? 13.782  -17.924 59.840  1.00 26.38 ? 177 ALA A CA  1 
ATOM   1078 C  C   . ALA A 1 149 ? 12.967  -17.692 61.105  1.00 26.94 ? 177 ALA A C   1 
ATOM   1079 O  O   . ALA A 1 149 ? 12.879  -16.565 61.601  1.00 24.55 ? 177 ALA A O   1 
ATOM   1080 C  CB  . ALA A 1 149 ? 15.168  -18.507 60.183  1.00 28.99 ? 177 ALA A CB  1 
ATOM   1081 N  N   . GLU A 1 150 ? 12.362  -18.765 61.626  1.00 22.29 ? 178 GLU A N   1 
ATOM   1082 C  CA  . GLU A 1 150 ? 11.450  -18.645 62.756  1.00 23.68 ? 178 GLU A CA  1 
ATOM   1083 C  C   . GLU A 1 150 ? 11.622  -19.784 63.750  1.00 24.64 ? 178 GLU A C   1 
ATOM   1084 O  O   . GLU A 1 150 ? 11.771  -20.946 63.361  1.00 25.59 ? 178 GLU A O   1 
ATOM   1085 C  CB  . GLU A 1 150 ? 9.970   -18.604 62.273  1.00 21.51 ? 178 GLU A CB  1 
ATOM   1086 C  CG  . GLU A 1 150 ? 9.709   -17.435 61.315  1.00 27.09 ? 178 GLU A CG  1 
ATOM   1087 C  CD  . GLU A 1 150 ? 8.313   -17.453 60.680  1.00 24.84 ? 178 GLU A CD  1 
ATOM   1088 O  OE1 . GLU A 1 150 ? 7.448   -18.236 61.115  1.00 24.67 ? 178 GLU A OE1 1 
ATOM   1089 O  OE2 . GLU A 1 150 ? 8.106   -16.680 59.721  1.00 27.97 ? 178 GLU A OE2 1 
ATOM   1090 N  N   . VAL A 1 151 ? 11.554  -19.448 65.041  1.00 26.17 ? 179 VAL A N   1 
ATOM   1091 C  CA  . VAL A 1 151 ? 11.535  -20.435 66.117  1.00 25.08 ? 179 VAL A CA  1 
ATOM   1092 C  C   . VAL A 1 151 ? 10.373  -20.103 67.041  1.00 29.33 ? 179 VAL A C   1 
ATOM   1093 O  O   . VAL A 1 151 ? 9.850   -18.989 67.039  1.00 26.06 ? 179 VAL A O   1 
ATOM   1094 C  CB  . VAL A 1 151 ? 12.860  -20.477 66.919  1.00 23.22 ? 179 VAL A CB  1 
ATOM   1095 C  CG1 . VAL A 1 151 ? 14.000  -20.879 66.024  1.00 25.28 ? 179 VAL A CG1 1 
ATOM   1096 C  CG2 . VAL A 1 151 ? 13.150  -19.111 67.576  1.00 26.08 ? 179 VAL A CG2 1 
ATOM   1097 N  N   . LYS A 1 152 ? 9.965   -21.085 67.841  1.00 24.80 ? 180 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 152 ? 8.834   -20.861 68.734  1.00 26.84 ? 180 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 152 ? 9.264   -19.990 69.906  1.00 26.41 ? 180 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 152 ? 10.352  -20.167 70.465  1.00 25.41 ? 180 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 152 ? 8.267   -22.190 69.240  1.00 27.22 ? 180 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 152 ? 7.745   -23.093 68.158  1.00 27.36 ? 180 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 152 ? 7.009   -24.295 68.762  1.00 32.20 ? 180 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 152 ? 6.327   -25.128 67.688  1.00 40.70 ? 180 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 152 ? 5.218   -25.966 68.243  1.00 38.20 ? 180 LYS A NZ  1 
ATOM   1106 N  N   . LEU A 1 153 ? 8.415   -19.018 70.263  1.00 25.45 ? 181 LEU A N   1 
ATOM   1107 C  CA  . LEU A 1 153 ? 8.682   -18.127 71.390  1.00 21.72 ? 181 LEU A CA  1 
ATOM   1108 C  C   . LEU A 1 153 ? 7.879   -18.530 72.623  1.00 25.03 ? 181 LEU A C   1 
ATOM   1109 O  O   . LEU A 1 153 ? 8.461   -18.864 73.657  1.00 25.85 ? 181 LEU A O   1 
ATOM   1110 C  CB  . LEU A 1 153 ? 8.380   -16.670 70.989  1.00 21.91 ? 181 LEU A CB  1 
ATOM   1111 C  CG  . LEU A 1 153 ? 8.710   -15.550 71.989  1.00 24.27 ? 181 LEU A CG  1 
ATOM   1112 C  CD1 . LEU A 1 153 ? 10.175  -15.556 72.441  1.00 26.48 ? 181 LEU A CD1 1 
ATOM   1113 C  CD2 . LEU A 1 153 ? 8.341   -14.194 71.355  1.00 21.85 ? 181 LEU A CD2 1 
ATOM   1114 N  N   . TYR A 1 154 ? 6.543   -18.484 72.529  1.00 23.27 ? 182 TYR A N   1 
ATOM   1115 C  CA  . TYR A 1 154 ? 5.621   -18.995 73.535  1.00 25.02 ? 182 TYR A CA  1 
ATOM   1116 C  C   . TYR A 1 154 ? 4.257   -19.153 72.860  1.00 25.11 ? 182 TYR A C   1 
ATOM   1117 O  O   . TYR A 1 154 ? 3.955   -18.456 71.887  1.00 25.78 ? 182 TYR A O   1 
ATOM   1118 C  CB  . TYR A 1 154 ? 5.529   -18.081 74.781  1.00 26.92 ? 182 TYR A CB  1 
ATOM   1119 C  CG  . TYR A 1 154 ? 5.672   -16.574 74.526  1.00 24.96 ? 182 TYR A CG  1 
ATOM   1120 C  CD1 . TYR A 1 154 ? 4.748   -15.879 73.748  1.00 26.19 ? 182 TYR A CD1 1 
ATOM   1121 C  CD2 . TYR A 1 154 ? 6.732   -15.850 75.081  1.00 25.51 ? 182 TYR A CD2 1 
ATOM   1122 C  CE1 . TYR A 1 154 ? 4.881   -14.495 73.512  1.00 27.73 ? 182 TYR A CE1 1 
ATOM   1123 C  CE2 . TYR A 1 154 ? 6.873   -14.470 74.858  1.00 26.48 ? 182 TYR A CE2 1 
ATOM   1124 C  CZ  . TYR A 1 154 ? 5.946   -13.800 74.073  1.00 27.58 ? 182 TYR A CZ  1 
ATOM   1125 O  OH  . TYR A 1 154 ? 6.100   -12.430 73.858  1.00 25.73 ? 182 TYR A OH  1 
ATOM   1126 N  N   . GLY A 1 155 ? 3.455   -20.098 73.355  1.00 25.53 ? 183 GLY A N   1 
ATOM   1127 C  CA  . GLY A 1 155 ? 2.183   -20.380 72.702  1.00 25.31 ? 183 GLY A CA  1 
ATOM   1128 C  C   . GLY A 1 155 ? 2.385   -20.657 71.221  1.00 26.80 ? 183 GLY A C   1 
ATOM   1129 O  O   . GLY A 1 155 ? 3.236   -21.459 70.824  1.00 27.46 ? 183 GLY A O   1 
ATOM   1130 N  N   . ASP A 1 156 ? 1.624   -19.962 70.381  1.00 23.76 ? 184 ASP A N   1 
ATOM   1131 C  CA  . ASP A 1 156 ? 1.761   -20.055 68.931  1.00 20.46 ? 184 ASP A CA  1 
ATOM   1132 C  C   . ASP A 1 156 ? 2.403   -18.807 68.338  1.00 23.99 ? 184 ASP A C   1 
ATOM   1133 O  O   . ASP A 1 156 ? 2.269   -18.537 67.134  1.00 24.01 ? 184 ASP A O   1 
ATOM   1134 C  CB  . ASP A 1 156 ? 0.394   -20.320 68.309  1.00 18.87 ? 184 ASP A CB  1 
ATOM   1135 C  CG  . ASP A 1 156 ? -0.155  -21.678 68.701  1.00 27.96 ? 184 ASP A CG  1 
ATOM   1136 O  OD1 . ASP A 1 156 ? 0.654   -22.620 68.798  1.00 27.62 ? 184 ASP A OD1 1 
ATOM   1137 O  OD2 . ASP A 1 156 ? -1.380  -21.794 68.904  1.00 26.79 ? 184 ASP A OD2 1 
ATOM   1138 N  N   . VAL A 1 157 ? 3.106   -18.058 69.166  1.00 22.34 ? 185 VAL A N   1 
ATOM   1139 C  CA  . VAL A 1 157 ? 3.890   -16.906 68.735  1.00 21.87 ? 185 VAL A CA  1 
ATOM   1140 C  C   . VAL A 1 157 ? 5.294   -17.375 68.380  1.00 23.25 ? 185 VAL A C   1 
ATOM   1141 O  O   . VAL A 1 157 ? 5.898   -18.167 69.118  1.00 22.09 ? 185 VAL A O   1 
ATOM   1142 C  CB  . VAL A 1 157 ? 3.938   -15.843 69.842  1.00 24.73 ? 185 VAL A CB  1 
ATOM   1143 C  CG1 . VAL A 1 157 ? 4.689   -14.579 69.325  1.00 20.62 ? 185 VAL A CG1 1 
ATOM   1144 C  CG2 . VAL A 1 157 ? 2.517   -15.492 70.295  1.00 22.54 ? 185 VAL A CG2 1 
ATOM   1145 N  N   . VAL A 1 158 ? 5.819   -16.899 67.249  1.00 22.48 ? 186 VAL A N   1 
ATOM   1146 C  CA  . VAL A 1 158 ? 7.179   -17.210 66.837  1.00 24.39 ? 186 VAL A CA  1 
ATOM   1147 C  C   . VAL A 1 158 ? 8.058   -15.972 66.986  1.00 23.95 ? 186 VAL A C   1 
ATOM   1148 O  O   . VAL A 1 158 ? 7.607   -14.825 66.835  1.00 23.11 ? 186 VAL A O   1 
ATOM   1149 C  CB  . VAL A 1 158 ? 7.253   -17.759 65.389  1.00 20.74 ? 186 VAL A CB  1 
ATOM   1150 C  CG1 . VAL A 1 158 ? 6.479   -19.063 65.262  1.00 24.96 ? 186 VAL A CG1 1 
ATOM   1151 C  CG2 . VAL A 1 158 ? 6.736   -16.710 64.373  1.00 24.31 ? 186 VAL A CG2 1 
ATOM   1152 N  N   . LEU A 1 159 ? 9.324   -16.217 67.311  1.00 21.90 ? 187 LEU A N   1 
ATOM   1153 C  CA  . LEU A 1 159 ? 10.381  -15.220 67.178  1.00 22.45 ? 187 LEU A CA  1 
ATOM   1154 C  C   . LEU A 1 159 ? 10.974  -15.361 65.779  1.00 25.59 ? 187 LEU A C   1 
ATOM   1155 O  O   . LEU A 1 159 ? 11.534  -16.414 65.439  1.00 26.13 ? 187 LEU A O   1 
ATOM   1156 C  CB  . LEU A 1 159 ? 11.450  -15.418 68.255  1.00 21.36 ? 187 LEU A CB  1 
ATOM   1157 C  CG  . LEU A 1 159 ? 12.584  -14.393 68.323  1.00 23.36 ? 187 LEU A CG  1 
ATOM   1158 C  CD1 . LEU A 1 159 ? 12.040  -13.036 68.750  1.00 21.86 ? 187 LEU A CD1 1 
ATOM   1159 C  CD2 . LEU A 1 159 ? 13.628  -14.867 69.322  1.00 24.79 ? 187 LEU A CD2 1 
ATOM   1160 N  N   . ARG A 1 160 ? 10.802  -14.332 64.957  1.00 19.21 ? 188 ARG A N   1 
ATOM   1161 C  CA  . ARG A 1 160 ? 11.247  -14.328 63.564  1.00 19.16 ? 188 ARG A CA  1 
ATOM   1162 C  C   . ARG A 1 160 ? 12.568  -13.576 63.448  1.00 23.14 ? 188 ARG A C   1 
ATOM   1163 O  O   . ARG A 1 160 ? 12.649  -12.413 63.835  1.00 22.43 ? 188 ARG A O   1 
ATOM   1164 C  CB  . ARG A 1 160 ? 10.204  -13.660 62.669  1.00 21.93 ? 188 ARG A CB  1 
ATOM   1165 C  CG  . ARG A 1 160 ? 10.615  -13.535 61.211  1.00 22.04 ? 188 ARG A CG  1 
ATOM   1166 C  CD  . ARG A 1 160 ? 9.488   -12.924 60.379  1.00 23.39 ? 188 ARG A CD  1 
ATOM   1167 N  NE  . ARG A 1 160 ? 8.394   -13.868 60.142  1.00 22.06 ? 188 ARG A NE  1 
ATOM   1168 C  CZ  . ARG A 1 160 ? 7.137   -13.504 59.912  1.00 22.94 ? 188 ARG A CZ  1 
ATOM   1169 N  NH1 . ARG A 1 160 ? 6.800   -12.213 59.914  1.00 24.19 ? 188 ARG A NH1 1 
ATOM   1170 N  NH2 . ARG A 1 160 ? 6.209   -14.426 59.718  1.00 23.40 ? 188 ARG A NH2 1 
ATOM   1171 N  N   . TYR A 1 161 ? 13.584  -14.227 62.883  1.00 22.25 ? 189 TYR A N   1 
ATOM   1172 C  CA  . TYR A 1 161 ? 14.855  -13.575 62.584  1.00 22.04 ? 189 TYR A CA  1 
ATOM   1173 C  C   . TYR A 1 161 ? 14.847  -13.094 61.138  1.00 22.72 ? 189 TYR A C   1 
ATOM   1174 O  O   . TYR A 1 161 ? 14.444  -13.836 60.239  1.00 27.30 ? 189 TYR A O   1 
ATOM   1175 C  CB  . TYR A 1 161 ? 16.019  -14.557 62.800  1.00 22.75 ? 189 TYR A CB  1 
ATOM   1176 C  CG  . TYR A 1 161 ? 16.073  -15.170 64.178  1.00 20.84 ? 189 TYR A CG  1 
ATOM   1177 C  CD1 . TYR A 1 161 ? 15.939  -14.388 65.318  1.00 22.87 ? 189 TYR A CD1 1 
ATOM   1178 C  CD2 . TYR A 1 161 ? 16.295  -16.534 64.339  1.00 24.79 ? 189 TYR A CD2 1 
ATOM   1179 C  CE1 . TYR A 1 161 ? 15.985  -14.943 66.584  1.00 22.45 ? 189 TYR A CE1 1 
ATOM   1180 C  CE2 . TYR A 1 161 ? 16.340  -17.106 65.606  1.00 24.58 ? 189 TYR A CE2 1 
ATOM   1181 C  CZ  . TYR A 1 161 ? 16.206  -16.312 66.719  1.00 24.46 ? 189 TYR A CZ  1 
ATOM   1182 O  OH  . TYR A 1 161 ? 16.255  -16.875 67.968  1.00 25.71 ? 189 TYR A OH  1 
ATOM   1183 N  N   . VAL A 1 162 ? 15.277  -11.855 60.919  1.00 22.86 ? 190 VAL A N   1 
ATOM   1184 C  CA  . VAL A 1 162 ? 15.424  -11.292 59.582  1.00 24.59 ? 190 VAL A CA  1 
ATOM   1185 C  C   . VAL A 1 162 ? 16.836  -10.732 59.456  1.00 28.50 ? 190 VAL A C   1 
ATOM   1186 O  O   . VAL A 1 162 ? 17.308  -10.043 60.363  1.00 29.47 ? 190 VAL A O   1 
ATOM   1187 C  CB  . VAL A 1 162 ? 14.390  -10.181 59.325  1.00 28.77 ? 190 VAL A CB  1 
ATOM   1188 C  CG1 . VAL A 1 162 ? 14.631  -9.554  57.982  1.00 34.94 ? 190 VAL A CG1 1 
ATOM   1189 C  CG2 . VAL A 1 162 ? 12.973  -10.754 59.406  1.00 28.48 ? 190 VAL A CG2 1 
ATOM   1190 N  N   . SER A 1 163 ? 17.501  -10.997 58.327  1.00 26.70 ? 191 SER A N   1 
ATOM   1191 C  CA  . SER A 1 163 ? 18.808  -10.398 58.078  1.00 30.65 ? 191 SER A CA  1 
ATOM   1192 C  C   . SER A 1 163 ? 18.910  -9.972  56.618  1.00 32.00 ? 191 SER A C   1 
ATOM   1193 O  O   . SER A 1 163 ? 18.389  -10.641 55.723  1.00 30.89 ? 191 SER A O   1 
ATOM   1194 C  CB  . SER A 1 163 ? 19.963  -11.362 58.453  1.00 26.73 ? 191 SER A CB  1 
ATOM   1195 O  OG  . SER A 1 163 ? 19.940  -12.525 57.649  1.00 30.20 ? 191 SER A OG  1 
ATOM   1196 N  N   . TYR A 1 164 ? 19.567  -8.840  56.394  1.00 30.77 ? 192 TYR A N   1 
ATOM   1197 C  CA  . TYR A 1 164 ? 19.704  -8.231  55.079  1.00 37.57 ? 192 TYR A CA  1 
ATOM   1198 C  C   . TYR A 1 164 ? 21.168  -8.255  54.670  1.00 39.47 ? 192 TYR A C   1 
ATOM   1199 O  O   . TYR A 1 164 ? 22.037  -7.859  55.451  1.00 42.42 ? 192 TYR A O   1 
ATOM   1200 C  CB  . TYR A 1 164 ? 19.195  -6.781  55.094  1.00 40.18 ? 192 TYR A CB  1 
ATOM   1201 C  CG  . TYR A 1 164 ? 17.710  -6.668  55.330  1.00 40.65 ? 192 TYR A CG  1 
ATOM   1202 C  CD1 . TYR A 1 164 ? 17.191  -6.677  56.619  1.00 40.21 ? 192 TYR A CD1 1 
ATOM   1203 C  CD2 . TYR A 1 164 ? 16.828  -6.535  54.264  1.00 41.92 ? 192 TYR A CD2 1 
ATOM   1204 C  CE1 . TYR A 1 164 ? 15.822  -6.582  56.840  1.00 42.97 ? 192 TYR A CE1 1 
ATOM   1205 C  CE2 . TYR A 1 164 ? 15.456  -6.437  54.471  1.00 44.33 ? 192 TYR A CE2 1 
ATOM   1206 C  CZ  . TYR A 1 164 ? 14.964  -6.462  55.761  1.00 46.00 ? 192 TYR A CZ  1 
ATOM   1207 O  OH  . TYR A 1 164 ? 13.606  -6.358  55.969  1.00 51.77 ? 192 TYR A OH  1 
ATOM   1208 N  N   . LYS A 1 165 ? 21.442  -8.731  53.456  1.00 44.70 ? 193 LYS A N   1 
ATOM   1209 C  CA  . LYS A 1 165 ? 22.782  -8.567  52.900  1.00 47.16 ? 193 LYS A CA  1 
ATOM   1210 C  C   . LYS A 1 165 ? 23.120  -7.086  52.769  1.00 49.21 ? 193 LYS A C   1 
ATOM   1211 O  O   . LYS A 1 165 ? 24.146  -6.618  53.280  1.00 49.76 ? 193 LYS A O   1 
ATOM   1212 C  CB  . LYS A 1 165 ? 22.884  -9.272  51.546  1.00 47.33 ? 193 LYS A CB  1 
ATOM   1213 N  N   . ALA A 1 166 ? 22.248  -6.326  52.116  1.00 47.89 ? 194 ALA A N   1 
ATOM   1214 C  CA  . ALA A 1 166 ? 22.423  -4.880  52.042  1.00 52.67 ? 194 ALA A CA  1 
ATOM   1215 C  C   . ALA A 1 166 ? 21.538  -4.173  53.065  1.00 52.62 ? 194 ALA A C   1 
ATOM   1216 O  O   . ALA A 1 166 ? 21.903  -4.043  54.238  1.00 52.94 ? 194 ALA A O   1 
ATOM   1217 C  CB  . ALA A 1 166 ? 22.119  -4.378  50.640  1.00 53.96 ? 194 ALA A CB  1 
ATOM   1218 N  N   . GLU A 1 173 ? 10.835  -2.210  49.833  1.00 61.52 ? 201 GLU A N   1 
ATOM   1219 C  CA  . GLU A 1 173 ? 12.119  -2.703  50.310  1.00 59.70 ? 201 GLU A CA  1 
ATOM   1220 C  C   . GLU A 1 173 ? 11.980  -3.494  51.621  1.00 53.62 ? 201 GLU A C   1 
ATOM   1221 O  O   . GLU A 1 173 ? 12.988  -3.921  52.200  1.00 54.03 ? 201 GLU A O   1 
ATOM   1222 C  CB  . GLU A 1 173 ? 13.108  -1.542  50.497  1.00 55.19 ? 201 GLU A CB  1 
ATOM   1223 N  N   . PHE A 1 174 ? 10.740  -3.667  52.092  1.00 46.17 ? 202 PHE A N   1 
ATOM   1224 C  CA  . PHE A 1 174 ? 10.462  -4.461  53.288  1.00 36.61 ? 202 PHE A CA  1 
ATOM   1225 C  C   . PHE A 1 174 ? 10.992  -5.875  53.102  1.00 37.78 ? 202 PHE A C   1 
ATOM   1226 O  O   . PHE A 1 174 ? 11.981  -6.274  53.723  1.00 41.46 ? 202 PHE A O   1 
ATOM   1227 C  CB  . PHE A 1 174 ? 8.947   -4.478  53.583  1.00 36.39 ? 202 PHE A CB  1 
ATOM   1228 C  CG  . PHE A 1 174 ? 8.542   -5.372  54.738  1.00 31.82 ? 202 PHE A CG  1 
ATOM   1229 C  CD1 . PHE A 1 174 ? 9.007   -5.123  56.021  1.00 30.63 ? 202 PHE A CD1 1 
ATOM   1230 C  CD2 . PHE A 1 174 ? 7.647   -6.426  54.548  1.00 31.56 ? 202 PHE A CD2 1 
ATOM   1231 C  CE1 . PHE A 1 174 ? 8.635   -5.934  57.094  1.00 31.20 ? 202 PHE A CE1 1 
ATOM   1232 C  CE2 . PHE A 1 174 ? 7.261   -7.252  55.619  1.00 29.04 ? 202 PHE A CE2 1 
ATOM   1233 C  CZ  . PHE A 1 174 ? 7.747   -6.998  56.895  1.00 29.68 ? 202 PHE A CZ  1 
ATOM   1234 N  N   . LEU A 1 175 ? 10.327  -6.642  52.254  1.00 35.15 ? 203 LEU A N   1 
ATOM   1235 C  CA  . LEU A 1 175 ? 10.772  -7.966  51.869  1.00 36.44 ? 203 LEU A CA  1 
ATOM   1236 C  C   . LEU A 1 175 ? 10.651  -8.079  50.360  1.00 36.89 ? 203 LEU A C   1 
ATOM   1237 O  O   . LEU A 1 175 ? 9.804   -7.409  49.751  1.00 33.05 ? 203 LEU A O   1 
ATOM   1238 C  CB  . LEU A 1 175 ? 9.934   -9.069  52.539  1.00 35.30 ? 203 LEU A CB  1 
ATOM   1239 C  CG  . LEU A 1 175 ? 9.971   -9.264  54.061  1.00 36.04 ? 203 LEU A CG  1 
ATOM   1240 C  CD1 . LEU A 1 175 ? 9.040   -10.409 54.488  1.00 32.04 ? 203 LEU A CD1 1 
ATOM   1241 C  CD2 . LEU A 1 175 ? 11.403  -9.515  54.540  1.00 35.00 ? 203 LEU A CD2 1 
ATOM   1242 N  N   . PRO A 1 176 ? 11.480  -8.910  49.728  1.00 36.30 ? 204 PRO A N   1 
ATOM   1243 C  CA  . PRO A 1 176 ? 11.275  -9.197  48.306  1.00 38.83 ? 204 PRO A CA  1 
ATOM   1244 C  C   . PRO A 1 176 ? 9.849   -9.672  48.070  1.00 39.72 ? 204 PRO A C   1 
ATOM   1245 O  O   . PRO A 1 176 ? 9.281   -10.430 48.861  1.00 43.37 ? 204 PRO A O   1 
ATOM   1246 C  CB  . PRO A 1 176 ? 12.291  -10.306 48.012  1.00 39.70 ? 204 PRO A CB  1 
ATOM   1247 C  CG  . PRO A 1 176 ? 13.345  -10.155 49.066  1.00 37.82 ? 204 PRO A CG  1 
ATOM   1248 C  CD  . PRO A 1 176 ? 12.624  -9.655  50.290  1.00 37.87 ? 204 PRO A CD  1 
ATOM   1249 N  N   . GLY A 1 177 ? 9.265   -9.224  46.972  1.00 35.52 ? 205 GLY A N   1 
ATOM   1250 C  CA  . GLY A 1 177 ? 7.909   -9.592  46.650  1.00 38.74 ? 205 GLY A CA  1 
ATOM   1251 C  C   . GLY A 1 177 ? 6.863   -8.618  47.142  1.00 33.02 ? 205 GLY A C   1 
ATOM   1252 O  O   . GLY A 1 177 ? 5.734   -8.646  46.645  1.00 39.20 ? 205 GLY A O   1 
ATOM   1253 N  N   . PHE A 1 178 ? 7.198   -7.771  48.114  1.00 32.87 ? 206 PHE A N   1 
ATOM   1254 C  CA  . PHE A 1 178 ? 6.322   -6.670  48.498  1.00 30.57 ? 206 PHE A CA  1 
ATOM   1255 C  C   . PHE A 1 178 ? 6.540   -5.492  47.559  1.00 34.98 ? 206 PHE A C   1 
ATOM   1256 O  O   . PHE A 1 178 ? 7.670   -5.201  47.155  1.00 38.40 ? 206 PHE A O   1 
ATOM   1257 C  CB  . PHE A 1 178 ? 6.596   -6.242  49.945  1.00 32.72 ? 206 PHE A CB  1 
ATOM   1258 C  CG  . PHE A 1 178 ? 5.958   -7.132  50.979  1.00 28.43 ? 206 PHE A CG  1 
ATOM   1259 C  CD1 . PHE A 1 178 ? 6.510   -8.375  51.276  1.00 27.76 ? 206 PHE A CD1 1 
ATOM   1260 C  CD2 . PHE A 1 178 ? 4.806   -6.727  51.651  1.00 26.03 ? 206 PHE A CD2 1 
ATOM   1261 C  CE1 . PHE A 1 178 ? 5.933   -9.212  52.222  1.00 28.80 ? 206 PHE A CE1 1 
ATOM   1262 C  CE2 . PHE A 1 178 ? 4.200   -7.568  52.607  1.00 25.90 ? 206 PHE A CE2 1 
ATOM   1263 C  CZ  . PHE A 1 178 ? 4.767   -8.811  52.886  1.00 30.83 ? 206 PHE A CZ  1 
ATOM   1264 N  N   . GLU A 1 179 ? 5.461   -4.812  47.213  1.00 32.33 ? 207 GLU A N   1 
ATOM   1265 C  CA  . GLU A 1 179 ? 5.543   -3.576  46.447  1.00 35.07 ? 207 GLU A CA  1 
ATOM   1266 C  C   . GLU A 1 179 ? 5.297   -2.375  47.350  1.00 39.51 ? 207 GLU A C   1 
ATOM   1267 O  O   . GLU A 1 179 ? 4.475   -2.431  48.269  1.00 35.03 ? 207 GLU A O   1 
ATOM   1268 C  CB  . GLU A 1 179 ? 4.543   -3.573  45.295  1.00 37.10 ? 207 GLU A CB  1 
ATOM   1269 C  CG  . GLU A 1 179 ? 4.734   -4.750  44.348  1.00 41.52 ? 207 GLU A CG  1 
ATOM   1270 C  CD  . GLU A 1 179 ? 3.849   -4.666  43.122  1.00 43.71 ? 207 GLU A CD  1 
ATOM   1271 O  OE1 . GLU A 1 179 ? 3.002   -3.744  43.048  1.00 42.19 ? 207 GLU A OE1 1 
ATOM   1272 O  OE2 . GLU A 1 179 ? 4.010   -5.528  42.231  1.00 46.82 ? 207 GLU A OE2 1 
ATOM   1273 N  N   . ARG A 1 180 ? 6.038   -1.299  47.093  1.00 36.89 ? 208 ARG A N   1 
ATOM   1274 C  CA  . ARG A 1 180 ? 5.812   -0.028  47.764  1.00 42.17 ? 208 ARG A CA  1 
ATOM   1275 C  C   . ARG A 1 180 ? 4.455   0.527   47.339  1.00 44.47 ? 208 ARG A C   1 
ATOM   1276 O  O   . ARG A 1 180 ? 4.028   0.345   46.196  1.00 48.11 ? 208 ARG A O   1 
ATOM   1277 C  CB  . ARG A 1 180 ? 6.955   0.930   47.423  1.00 48.78 ? 208 ARG A CB  1 
ATOM   1278 C  CG  . ARG A 1 180 ? 6.589   2.385   47.282  1.00 54.65 ? 208 ARG A CG  1 
ATOM   1279 C  CD  . ARG A 1 180 ? 7.829   3.228   46.962  1.00 63.27 ? 208 ARG A CD  1 
ATOM   1280 N  NE  . ARG A 1 180 ? 8.824   3.222   48.038  1.00 70.32 ? 208 ARG A NE  1 
ATOM   1281 C  CZ  . ARG A 1 180 ? 9.947   2.505   48.027  1.00 73.12 ? 208 ARG A CZ  1 
ATOM   1282 N  NH1 . ARG A 1 180 ? 10.230  1.720   46.995  1.00 70.09 ? 208 ARG A NH1 1 
ATOM   1283 N  NH2 . ARG A 1 180 ? 10.789  2.572   49.053  1.00 71.39 ? 208 ARG A NH2 1 
ATOM   1284 N  N   . VAL A 1 181 ? 3.751   1.173   48.269  1.00 43.37 ? 209 VAL A N   1 
ATOM   1285 C  CA  . VAL A 1 181 ? 2.329   1.443   48.065  1.00 46.27 ? 209 VAL A CA  1 
ATOM   1286 C  C   . VAL A 1 181 ? 2.128   2.751   47.310  1.00 58.14 ? 209 VAL A C   1 
ATOM   1287 O  O   . VAL A 1 181 ? 2.812   3.753   47.565  1.00 54.64 ? 209 VAL A O   1 
ATOM   1288 C  CB  . VAL A 1 181 ? 1.576   1.437   49.408  1.00 43.65 ? 209 VAL A CB  1 
ATOM   1289 C  CG1 . VAL A 1 181 ? 0.205   2.093   49.270  1.00 45.73 ? 209 VAL A CG1 1 
ATOM   1290 C  CG2 . VAL A 1 181 ? 1.416   0.004   49.875  1.00 35.01 ? 209 VAL A CG2 1 
ATOM   1291 N  N   . GLU A 1 182 ? 1.176   2.719   46.366  1.00 62.54 ? 210 GLU A N   1 
ATOM   1292 C  CA  . GLU A 1 182 ? 0.788   3.870   45.555  1.00 59.53 ? 210 GLU A CA  1 
ATOM   1293 C  C   . GLU A 1 182 ? 0.425   5.071   46.419  1.00 62.04 ? 210 GLU A C   1 
ATOM   1294 O  O   . GLU A 1 182 ? -0.394  4.967   47.337  1.00 63.02 ? 210 GLU A O   1 
ATOM   1295 C  CB  . GLU A 1 182 ? -0.401  3.490   44.670  1.00 60.45 ? 210 GLU A CB  1 
ATOM   1296 N  N   . ASP A 1 183 ? 1.011   6.226   46.088  1.00 63.23 ? 211 ASP A N   1 
ATOM   1297 C  CA  . ASP A 1 183 ? 0.913   7.394   46.962  1.00 64.17 ? 211 ASP A CA  1 
ATOM   1298 C  C   . ASP A 1 183 ? -0.527  7.817   47.219  1.00 62.01 ? 211 ASP A C   1 
ATOM   1299 O  O   . ASP A 1 183 ? -0.807  8.433   48.254  1.00 65.71 ? 211 ASP A O   1 
ATOM   1300 C  CB  . ASP A 1 183 ? 1.698   8.565   46.375  1.00 67.05 ? 211 ASP A CB  1 
ATOM   1301 C  CG  . ASP A 1 183 ? 3.170   8.502   46.719  1.00 73.03 ? 211 ASP A CG  1 
ATOM   1302 O  OD1 . ASP A 1 183 ? 3.543   8.984   47.812  1.00 73.93 ? 211 ASP A OD1 1 
ATOM   1303 O  OD2 . ASP A 1 183 ? 3.951   7.966   45.901  1.00 77.10 ? 211 ASP A OD2 1 
ATOM   1304 N  N   . ALA A 1 184 ? -1.449  7.515   46.298  1.00 60.40 ? 212 ALA A N   1 
ATOM   1305 C  CA  . ALA A 1 184 ? -2.848  7.889   46.510  1.00 61.46 ? 212 ALA A CA  1 
ATOM   1306 C  C   . ALA A 1 184 ? -3.452  7.131   47.685  1.00 58.05 ? 212 ALA A C   1 
ATOM   1307 O  O   . ALA A 1 184 ? -4.273  7.680   48.431  1.00 55.34 ? 212 ALA A O   1 
ATOM   1308 C  CB  . ALA A 1 184 ? -3.664  7.644   45.242  1.00 58.92 ? 212 ALA A CB  1 
ATOM   1309 N  N   . SER A 1 185 ? -3.055  5.869   47.862  1.00 58.59 ? 213 SER A N   1 
ATOM   1310 C  CA  . SER A 1 185 ? -3.479  5.081   49.010  1.00 54.77 ? 213 SER A CA  1 
ATOM   1311 C  C   . SER A 1 185 ? -2.630  5.342   50.247  1.00 52.46 ? 213 SER A C   1 
ATOM   1312 O  O   . SER A 1 185 ? -3.062  5.024   51.359  1.00 50.20 ? 213 SER A O   1 
ATOM   1313 C  CB  . SER A 1 185 ? -3.440  3.590   48.655  1.00 56.04 ? 213 SER A CB  1 
ATOM   1314 O  OG  . SER A 1 185 ? -3.975  3.365   47.357  1.00 56.68 ? 213 SER A OG  1 
ATOM   1315 N  N   . SER A 1 186 ? -1.443  5.928   50.089  1.00 47.74 ? 214 SER A N   1 
ATOM   1316 C  CA  . SER A 1 186 ? -0.540  6.138   51.215  1.00 46.26 ? 214 SER A CA  1 
ATOM   1317 C  C   . SER A 1 186 ? -0.702  7.571   51.726  1.00 43.95 ? 214 SER A C   1 
ATOM   1318 O  O   . SER A 1 186 ? 0.074   8.474   51.412  1.00 45.96 ? 214 SER A O   1 
ATOM   1319 C  CB  . SER A 1 186 ? 0.895   5.831   50.813  1.00 44.34 ? 214 SER A CB  1 
ATOM   1320 O  OG  . SER A 1 186 ? 1.742   5.844   51.951  1.00 43.37 ? 214 SER A OG  1 
ATOM   1321 N  N   . PHE A 1 187 ? -1.722  7.760   52.543  1.00 36.92 ? 215 PHE A N   1 
ATOM   1322 C  CA  . PHE A 1 187 ? -1.952  9.030   53.231  1.00 36.69 ? 215 PHE A CA  1 
ATOM   1323 C  C   . PHE A 1 187 ? -0.968  9.177   54.387  1.00 35.65 ? 215 PHE A C   1 
ATOM   1324 O  O   . PHE A 1 187 ? -0.893  8.293   55.242  1.00 32.21 ? 215 PHE A O   1 
ATOM   1325 C  CB  . PHE A 1 187 ? -3.376  9.087   53.754  1.00 31.82 ? 215 PHE A CB  1 
ATOM   1326 C  CG  . PHE A 1 187 ? -3.823  10.461  54.153  1.00 28.85 ? 215 PHE A CG  1 
ATOM   1327 C  CD1 . PHE A 1 187 ? -3.398  11.025  55.345  1.00 29.28 ? 215 PHE A CD1 1 
ATOM   1328 C  CD2 . PHE A 1 187 ? -4.690  11.182  53.342  1.00 32.71 ? 215 PHE A CD2 1 
ATOM   1329 C  CE1 . PHE A 1 187 ? -3.807  12.302  55.712  1.00 29.22 ? 215 PHE A CE1 1 
ATOM   1330 C  CE2 . PHE A 1 187 ? -5.112  12.446  53.710  1.00 32.50 ? 215 PHE A CE2 1 
ATOM   1331 C  CZ  . PHE A 1 187 ? -4.662  13.007  54.891  1.00 32.06 ? 215 PHE A CZ  1 
ATOM   1332 N  N   . PRO A 1 188 ? -0.216  10.304  54.475  1.00 31.48 ? 216 PRO A N   1 
ATOM   1333 C  CA  . PRO A 1 188 ? 0.895   10.380  55.446  1.00 34.93 ? 216 PRO A CA  1 
ATOM   1334 C  C   . PRO A 1 188 ? 0.434   10.651  56.880  1.00 32.41 ? 216 PRO A C   1 
ATOM   1335 O  O   . PRO A 1 188 ? 0.859   11.606  57.531  1.00 30.12 ? 216 PRO A O   1 
ATOM   1336 C  CB  . PRO A 1 188 ? 1.760   11.515  54.868  1.00 27.19 ? 216 PRO A CB  1 
ATOM   1337 C  CG  . PRO A 1 188 ? 0.806   12.384  54.144  1.00 31.16 ? 216 PRO A CG  1 
ATOM   1338 C  CD  . PRO A 1 188 ? -0.275  11.480  53.592  1.00 32.55 ? 216 PRO A CD  1 
ATOM   1339 N  N   . LEU A 1 189 ? -0.417  9.769   57.409  1.00 27.17 ? 217 LEU A N   1 
ATOM   1340 C  CA  . LEU A 1 189 ? -0.796  9.858   58.817  1.00 24.26 ? 217 LEU A CA  1 
ATOM   1341 C  C   . LEU A 1 189 ? 0.424   9.701   59.717  1.00 29.37 ? 217 LEU A C   1 
ATOM   1342 O  O   . LEU A 1 189 ? 1.334   8.915   59.436  1.00 27.38 ? 217 LEU A O   1 
ATOM   1343 C  CB  . LEU A 1 189 ? -1.831  8.777   59.171  1.00 28.11 ? 217 LEU A CB  1 
ATOM   1344 C  CG  . LEU A 1 189 ? -3.211  8.873   58.518  1.00 22.39 ? 217 LEU A CG  1 
ATOM   1345 C  CD1 . LEU A 1 189 ? -4.026  7.579   58.797  1.00 26.33 ? 217 LEU A CD1 1 
ATOM   1346 C  CD2 . LEU A 1 189 ? -3.978  10.148  58.936  1.00 26.32 ? 217 LEU A CD2 1 
ATOM   1347 N  N   . ASP A 1 190 ? 0.428   10.438  60.824  1.00 28.86 ? 218 ASP A N   1 
ATOM   1348 C  CA  . ASP A 1 190 ? 1.501   10.331  61.807  1.00 23.93 ? 218 ASP A CA  1 
ATOM   1349 C  C   . ASP A 1 190 ? 1.032   10.998  63.095  1.00 28.41 ? 218 ASP A C   1 
ATOM   1350 O  O   . ASP A 1 190 ? 0.841   12.222  63.120  1.00 27.83 ? 218 ASP A O   1 
ATOM   1351 C  CB  . ASP A 1 190 ? 2.779   10.980  61.267  1.00 26.94 ? 218 ASP A CB  1 
ATOM   1352 C  CG  . ASP A 1 190 ? 3.892   11.012  62.273  1.00 33.50 ? 218 ASP A CG  1 
ATOM   1353 O  OD1 . ASP A 1 190 ? 3.849   10.222  63.247  1.00 29.58 ? 218 ASP A OD1 1 
ATOM   1354 O  OD2 . ASP A 1 190 ? 4.819   11.843  62.092  1.00 32.20 ? 218 ASP A OD2 1 
ATOM   1355 N  N   . TYR A 1 191 ? 0.852   10.212  64.162  1.00 20.53 ? 219 TYR A N   1 
ATOM   1356 C  CA  . TYR A 1 191 ? 0.488   10.770  65.461  1.00 24.78 ? 219 TYR A CA  1 
ATOM   1357 C  C   . TYR A 1 191 ? 1.666   10.792  66.426  1.00 24.38 ? 219 TYR A C   1 
ATOM   1358 O  O   . TYR A 1 191 ? 1.472   11.045  67.618  1.00 26.16 ? 219 TYR A O   1 
ATOM   1359 C  CB  . TYR A 1 191 ? -0.697  10.014  66.104  1.00 25.32 ? 219 TYR A CB  1 
ATOM   1360 C  CG  . TYR A 1 191 ? -1.893  9.747   65.200  1.00 24.79 ? 219 TYR A CG  1 
ATOM   1361 C  CD1 . TYR A 1 191 ? -2.123  10.505  64.045  1.00 22.57 ? 219 TYR A CD1 1 
ATOM   1362 C  CD2 . TYR A 1 191 ? -2.797  8.721   65.500  1.00 23.32 ? 219 TYR A CD2 1 
ATOM   1363 C  CE1 . TYR A 1 191 ? -3.203  10.259  63.227  1.00 24.49 ? 219 TYR A CE1 1 
ATOM   1364 C  CE2 . TYR A 1 191 ? -3.887  8.471   64.689  1.00 22.93 ? 219 TYR A CE2 1 
ATOM   1365 C  CZ  . TYR A 1 191 ? -4.073  9.219   63.538  1.00 23.14 ? 219 TYR A CZ  1 
ATOM   1366 O  OH  . TYR A 1 191 ? -5.131  8.946   62.708  1.00 23.13 ? 219 TYR A OH  1 
ATOM   1367 N  N   . GLY A 1 192 ? 2.876   10.519  65.946  1.00 24.73 ? 220 GLY A N   1 
ATOM   1368 C  CA  . GLY A 1 192 ? 4.068   10.593  66.767  1.00 24.24 ? 220 GLY A CA  1 
ATOM   1369 C  C   . GLY A 1 192 ? 4.675   9.264   67.171  1.00 24.59 ? 220 GLY A C   1 
ATOM   1370 O  O   . GLY A 1 192 ? 5.730   9.261   67.804  1.00 25.59 ? 220 GLY A O   1 
ATOM   1371 N  N   . ILE A 1 193 ? 4.070   8.128   66.836  1.00 21.16 ? 221 ILE A N   1 
ATOM   1372 C  CA  . ILE A 1 193 ? 4.681   6.857   67.236  1.00 20.95 ? 221 ILE A CA  1 
ATOM   1373 C  C   . ILE A 1 193 ? 5.916   6.579   66.387  1.00 20.94 ? 221 ILE A C   1 
ATOM   1374 O  O   . ILE A 1 193 ? 5.926   6.820   65.170  1.00 22.48 ? 221 ILE A O   1 
ATOM   1375 C  CB  . ILE A 1 193 ? 3.636   5.727   67.138  1.00 19.45 ? 221 ILE A CB  1 
ATOM   1376 C  CG1 . ILE A 1 193 ? 2.502   5.999   68.116  1.00 16.67 ? 221 ILE A CG1 1 
ATOM   1377 C  CG2 . ILE A 1 193 ? 4.277   4.378   67.474  1.00 19.33 ? 221 ILE A CG2 1 
ATOM   1378 C  CD1 . ILE A 1 193 ? 1.281   5.042   67.924  1.00 19.40 ? 221 ILE A CD1 1 
ATOM   1379 N  N   . ARG A 1 194 ? 6.986   6.070   67.027  1.00 22.50 ? 222 ARG A N   1 
ATOM   1380 C  CA  . ARG A 1 194 ? 8.273   5.984   66.357  1.00 23.38 ? 222 ARG A CA  1 
ATOM   1381 C  C   . ARG A 1 194 ? 8.914   4.594   66.357  1.00 21.43 ? 222 ARG A C   1 
ATOM   1382 O  O   . ARG A 1 194 ? 9.582   4.247   65.381  1.00 25.67 ? 222 ARG A O   1 
ATOM   1383 C  CB  . ARG A 1 194 ? 9.236   7.024   66.967  1.00 23.15 ? 222 ARG A CB  1 
ATOM   1384 C  CG  . ARG A 1 194 ? 8.836   8.478   66.593  1.00 23.81 ? 222 ARG A CG  1 
ATOM   1385 C  CD  . ARG A 1 194 ? 8.997   8.732   65.086  1.00 24.77 ? 222 ARG A CD  1 
ATOM   1386 N  NE  . ARG A 1 194 ? 8.602   10.086  64.657  1.00 26.93 ? 222 ARG A NE  1 
ATOM   1387 C  CZ  . ARG A 1 194 ? 7.386   10.405  64.219  1.00 30.95 ? 222 ARG A CZ  1 
ATOM   1388 N  NH1 . ARG A 1 194 ? 6.431   9.482   64.169  1.00 25.59 ? 222 ARG A NH1 1 
ATOM   1389 N  NH2 . ARG A 1 194 ? 7.112   11.644  63.827  1.00 28.95 ? 222 ARG A NH2 1 
ATOM   1390 N  N   . ARG A 1 195 ? 8.728   3.775   67.397  1.00 21.29 ? 223 ARG A N   1 
ATOM   1391 C  CA  . ARG A 1 195 ? 9.310   2.438   67.348  1.00 23.72 ? 223 ARG A CA  1 
ATOM   1392 C  C   . ARG A 1 195 ? 8.652   1.528   68.383  1.00 24.38 ? 223 ARG A C   1 
ATOM   1393 O  O   . ARG A 1 195 ? 7.943   1.987   69.283  1.00 24.34 ? 223 ARG A O   1 
ATOM   1394 C  CB  . ARG A 1 195 ? 10.830  2.495   67.581  1.00 23.83 ? 223 ARG A CB  1 
ATOM   1395 C  CG  . ARG A 1 195 ? 11.215  2.943   68.972  1.00 27.99 ? 223 ARG A CG  1 
ATOM   1396 C  CD  . ARG A 1 195 ? 12.762  2.915   69.175  1.00 31.46 ? 223 ARG A CD  1 
ATOM   1397 N  NE  . ARG A 1 195 ? 13.112  3.231   70.559  1.00 38.28 ? 223 ARG A NE  1 
ATOM   1398 C  CZ  . ARG A 1 195 ? 13.342  2.313   71.495  1.00 35.31 ? 223 ARG A CZ  1 
ATOM   1399 N  NH1 . ARG A 1 195 ? 13.270  1.025   71.188  1.00 32.78 ? 223 ARG A NH1 1 
ATOM   1400 N  NH2 . ARG A 1 195 ? 13.640  2.681   72.737  1.00 37.80 ? 223 ARG A NH2 1 
ATOM   1401 N  N   . LEU A 1 196 ? 8.927   0.224   68.252  1.00 22.40 ? 224 LEU A N   1 
ATOM   1402 C  CA  . LEU A 1 196 ? 8.499   -0.763  69.239  1.00 19.06 ? 224 LEU A CA  1 
ATOM   1403 C  C   . LEU A 1 196 ? 9.443   -0.733  70.425  1.00 24.31 ? 224 LEU A C   1 
ATOM   1404 O  O   . LEU A 1 196 ? 10.652  -0.965  70.270  1.00 25.98 ? 224 LEU A O   1 
ATOM   1405 C  CB  . LEU A 1 196 ? 8.466   -2.177  68.646  1.00 23.20 ? 224 LEU A CB  1 
ATOM   1406 C  CG  . LEU A 1 196 ? 7.917   -3.280  69.573  1.00 21.68 ? 224 LEU A CG  1 
ATOM   1407 C  CD1 . LEU A 1 196 ? 6.419   -3.077  69.904  1.00 23.38 ? 224 LEU A CD1 1 
ATOM   1408 C  CD2 . LEU A 1 196 ? 8.108   -4.664  68.944  1.00 22.21 ? 224 LEU A CD2 1 
ATOM   1409 N  N   . ASP A 1 197 ? 8.904   -0.477  71.611  1.00 24.03 ? 225 ASP A N   1 
ATOM   1410 C  CA  . ASP A 1 197 ? 9.773   -0.452  72.779  1.00 24.71 ? 225 ASP A CA  1 
ATOM   1411 C  C   . ASP A 1 197 ? 9.932   -1.832  73.400  1.00 25.28 ? 225 ASP A C   1 
ATOM   1412 O  O   . ASP A 1 197 ? 11.051  -2.218  73.748  1.00 23.77 ? 225 ASP A O   1 
ATOM   1413 C  CB  . ASP A 1 197 ? 9.255   0.522   73.832  1.00 24.45 ? 225 ASP A CB  1 
ATOM   1414 C  CG  . ASP A 1 197 ? 10.198  0.639   75.011  1.00 25.73 ? 225 ASP A CG  1 
ATOM   1415 O  OD1 . ASP A 1 197 ? 11.099  1.516   74.967  1.00 28.22 ? 225 ASP A OD1 1 
ATOM   1416 O  OD2 . ASP A 1 197 ? 10.040  -0.130  75.983  1.00 27.17 ? 225 ASP A OD2 1 
ATOM   1417 N  N   . HIS A 1 198 ? 8.835   -2.575  73.560  1.00 21.53 ? 226 HIS A N   1 
ATOM   1418 C  CA  . HIS A 1 198 ? 8.917   -3.939  74.066  1.00 20.10 ? 226 HIS A CA  1 
ATOM   1419 C  C   . HIS A 1 198 ? 7.658   -4.707  73.678  1.00 22.43 ? 226 HIS A C   1 
ATOM   1420 O  O   . HIS A 1 198 ? 6.630   -4.119  73.336  1.00 24.24 ? 226 HIS A O   1 
ATOM   1421 C  CB  . HIS A 1 198 ? 9.139   -3.985  75.586  1.00 24.87 ? 226 HIS A CB  1 
ATOM   1422 C  CG  . HIS A 1 198 ? 8.115   -3.256  76.404  1.00 25.72 ? 226 HIS A CG  1 
ATOM   1423 N  ND1 . HIS A 1 198 ? 8.242   -1.925  76.749  1.00 26.56 ? 226 HIS A ND1 1 
ATOM   1424 C  CD2 . HIS A 1 198 ? 6.967   -3.683  76.982  1.00 24.34 ? 226 HIS A CD2 1 
ATOM   1425 C  CE1 . HIS A 1 198 ? 7.224   -1.570  77.515  1.00 22.27 ? 226 HIS A CE1 1 
ATOM   1426 N  NE2 . HIS A 1 198 ? 6.429   -2.615  77.662  1.00 29.49 ? 226 HIS A NE2 1 
ATOM   1427 N  N   . ALA A 1 199 ? 7.772   -6.034  73.721  1.00 21.98 ? 227 ALA A N   1 
ATOM   1428 C  CA  . ALA A 1 199 ? 6.688   -6.943  73.352  1.00 22.03 ? 227 ALA A CA  1 
ATOM   1429 C  C   . ALA A 1 199 ? 6.555   -7.983  74.452  1.00 22.89 ? 227 ALA A C   1 
ATOM   1430 O  O   . ALA A 1 199 ? 7.544   -8.614  74.824  1.00 24.45 ? 227 ALA A O   1 
ATOM   1431 C  CB  . ALA A 1 199 ? 6.960   -7.606  72.000  1.00 20.86 ? 227 ALA A CB  1 
ATOM   1432 N  N   . VAL A 1 200 ? 5.336   -8.187  74.946  1.00 21.45 ? 228 VAL A N   1 
ATOM   1433 C  CA  . VAL A 1 200 ? 5.113   -8.858  76.221  1.00 22.39 ? 228 VAL A CA  1 
ATOM   1434 C  C   . VAL A 1 200 ? 4.265   -10.110 76.011  1.00 25.85 ? 228 VAL A C   1 
ATOM   1435 O  O   . VAL A 1 200 ? 3.193   -10.048 75.393  1.00 21.29 ? 228 VAL A O   1 
ATOM   1436 C  CB  . VAL A 1 200 ? 4.448   -7.909  77.232  1.00 24.35 ? 228 VAL A CB  1 
ATOM   1437 C  CG1 . VAL A 1 200 ? 4.218   -8.633  78.567  1.00 22.84 ? 228 VAL A CG1 1 
ATOM   1438 C  CG2 . VAL A 1 200 ? 5.322   -6.677  77.421  1.00 24.92 ? 228 VAL A CG2 1 
ATOM   1439 N  N   . GLY A 1 201 ? 4.728   -11.232 76.561  1.00 22.20 ? 229 GLY A N   1 
ATOM   1440 C  CA  . GLY A 1 201 ? 3.995   -12.487 76.509  1.00 23.09 ? 229 GLY A CA  1 
ATOM   1441 C  C   . GLY A 1 201 ? 3.336   -12.843 77.831  1.00 25.28 ? 229 GLY A C   1 
ATOM   1442 O  O   . GLY A 1 201 ? 3.849   -12.524 78.899  1.00 28.37 ? 229 GLY A O   1 
ATOM   1443 N  N   . ASN A 1 202 ? 2.173   -13.496 77.750  1.00 26.34 ? 230 ASN A N   1 
ATOM   1444 C  CA  . ASN A 1 202 ? 1.521   -14.106 78.908  1.00 26.21 ? 230 ASN A CA  1 
ATOM   1445 C  C   . ASN A 1 202 ? 1.673   -15.618 78.793  1.00 27.84 ? 230 ASN A C   1 
ATOM   1446 O  O   . ASN A 1 202 ? 1.470   -16.184 77.714  1.00 24.12 ? 230 ASN A O   1 
ATOM   1447 C  CB  . ASN A 1 202 ? 0.032   -13.743 78.983  1.00 23.37 ? 230 ASN A CB  1 
ATOM   1448 C  CG  . ASN A 1 202 ? -0.216  -12.350 79.520  1.00 26.56 ? 230 ASN A CG  1 
ATOM   1449 O  OD1 . ASN A 1 202 ? 0.694   -11.689 80.044  1.00 25.64 ? 230 ASN A OD1 1 
ATOM   1450 N  ND2 . ASN A 1 202 ? -1.465  -11.898 79.405  1.00 22.75 ? 230 ASN A ND2 1 
ATOM   1451 N  N   . VAL A 1 203 ? 2.082   -16.268 79.884  1.00 27.95 ? 231 VAL A N   1 
ATOM   1452 C  CA  . VAL A 1 203 ? 2.275   -17.717 79.899  1.00 30.01 ? 231 VAL A CA  1 
ATOM   1453 C  C   . VAL A 1 203 ? 1.702   -18.273 81.189  1.00 28.31 ? 231 VAL A C   1 
ATOM   1454 O  O   . VAL A 1 203 ? 1.548   -17.550 82.187  1.00 30.21 ? 231 VAL A O   1 
ATOM   1455 C  CB  . VAL A 1 203 ? 3.765   -18.125 79.774  1.00 29.36 ? 231 VAL A CB  1 
ATOM   1456 C  CG1 . VAL A 1 203 ? 4.365   -17.673 78.439  1.00 29.70 ? 231 VAL A CG1 1 
ATOM   1457 C  CG2 . VAL A 1 203 ? 4.576   -17.593 80.950  1.00 30.16 ? 231 VAL A CG2 1 
ATOM   1458 N  N   . PRO A 1 204 ? 1.352   -19.559 81.196  1.00 31.35 ? 232 PRO A N   1 
ATOM   1459 C  CA  . PRO A 1 204 ? 0.897   -20.161 82.461  1.00 34.41 ? 232 PRO A CA  1 
ATOM   1460 C  C   . PRO A 1 204 ? 2.005   -20.265 83.500  1.00 34.70 ? 232 PRO A C   1 
ATOM   1461 O  O   . PRO A 1 204 ? 1.731   -20.080 84.693  1.00 36.44 ? 232 PRO A O   1 
ATOM   1462 C  CB  . PRO A 1 204 ? 0.365   -21.541 82.030  1.00 37.17 ? 232 PRO A CB  1 
ATOM   1463 C  CG  . PRO A 1 204 ? 1.055   -21.835 80.729  1.00 36.75 ? 232 PRO A CG  1 
ATOM   1464 C  CD  . PRO A 1 204 ? 1.253   -20.489 80.057  1.00 30.34 ? 232 PRO A CD  1 
ATOM   1465 N  N   . GLU A 1 205 ? 3.251   -20.525 83.090  1.00 34.25 ? 233 GLU A N   1 
ATOM   1466 C  CA  . GLU A 1 205 ? 4.364   -20.687 84.022  1.00 35.70 ? 233 GLU A CA  1 
ATOM   1467 C  C   . GLU A 1 205 ? 5.569   -19.871 83.570  1.00 30.61 ? 233 GLU A C   1 
ATOM   1468 O  O   . GLU A 1 205 ? 6.182   -20.172 82.542  1.00 30.61 ? 233 GLU A O   1 
ATOM   1469 C  CB  . GLU A 1 205 ? 4.743   -22.163 84.162  1.00 34.52 ? 233 GLU A CB  1 
ATOM   1470 C  CG  . GLU A 1 205 ? 3.586   -23.050 84.563  1.00 37.66 ? 233 GLU A CG  1 
ATOM   1471 C  CD  . GLU A 1 205 ? 4.011   -24.480 84.794  1.00 43.14 ? 233 GLU A CD  1 
ATOM   1472 O  OE1 . GLU A 1 205 ? 5.231   -24.752 84.805  1.00 45.66 ? 233 GLU A OE1 1 
ATOM   1473 O  OE2 . GLU A 1 205 ? 3.118   -25.334 84.961  1.00 46.67 ? 233 GLU A OE2 1 
ATOM   1474 N  N   . LEU A 1 206 ? 5.934   -18.871 84.370  1.00 31.39 ? 234 LEU A N   1 
ATOM   1475 C  CA  . LEU A 1 206 ? 7.010   -17.951 83.993  1.00 30.17 ? 234 LEU A CA  1 
ATOM   1476 C  C   . LEU A 1 206 ? 8.371   -18.640 83.967  1.00 32.96 ? 234 LEU A C   1 
ATOM   1477 O  O   . LEU A 1 206 ? 9.185   -18.384 83.072  1.00 33.35 ? 234 LEU A O   1 
ATOM   1478 C  CB  . LEU A 1 206 ? 7.027   -16.768 84.957  1.00 32.10 ? 234 LEU A CB  1 
ATOM   1479 C  CG  . LEU A 1 206 ? 8.137   -15.713 84.840  1.00 31.63 ? 234 LEU A CG  1 
ATOM   1480 C  CD1 . LEU A 1 206 ? 8.151   -15.060 83.463  1.00 32.65 ? 234 LEU A CD1 1 
ATOM   1481 C  CD2 . LEU A 1 206 ? 7.970   -14.657 85.932  1.00 35.41 ? 234 LEU A CD2 1 
ATOM   1482 N  N   . GLY A 1 207 ? 8.644   -19.499 84.945  1.00 33.66 ? 235 GLY A N   1 
ATOM   1483 C  CA  . GLY A 1 207 ? 9.951   -20.106 85.091  1.00 34.73 ? 235 GLY A CA  1 
ATOM   1484 C  C   . GLY A 1 207 ? 10.424  -20.842 83.855  1.00 32.41 ? 235 GLY A C   1 
ATOM   1485 O  O   . GLY A 1 207 ? 11.484  -20.544 83.300  1.00 34.82 ? 235 GLY A O   1 
ATOM   1486 N  N   . PRO A 1 208 ? 9.639   -21.824 83.397  1.00 34.03 ? 236 PRO A N   1 
ATOM   1487 C  CA  . PRO A 1 208 ? 10.029  -22.551 82.175  1.00 33.63 ? 236 PRO A CA  1 
ATOM   1488 C  C   . PRO A 1 208 ? 10.079  -21.674 80.936  1.00 33.67 ? 236 PRO A C   1 
ATOM   1489 O  O   . PRO A 1 208 ? 10.915  -21.900 80.052  1.00 34.12 ? 236 PRO A O   1 
ATOM   1490 C  CB  . PRO A 1 208 ? 8.951   -23.632 82.049  1.00 31.60 ? 236 PRO A CB  1 
ATOM   1491 C  CG  . PRO A 1 208 ? 8.320   -23.732 83.386  1.00 34.68 ? 236 PRO A CG  1 
ATOM   1492 C  CD  . PRO A 1 208 ? 8.446   -22.404 84.035  1.00 36.22 ? 236 PRO A CD  1 
ATOM   1493 N  N   . ALA A 1 209 ? 9.177   -20.695 80.830  1.00 33.76 ? 237 ALA A N   1 
ATOM   1494 C  CA  . ALA A 1 209 ? 9.207   -19.795 79.682  1.00 31.40 ? 237 ALA A CA  1 
ATOM   1495 C  C   . ALA A 1 209 ? 10.517  -19.014 79.638  1.00 28.92 ? 237 ALA A C   1 
ATOM   1496 O  O   . ALA A 1 209 ? 11.155  -18.909 78.585  1.00 30.93 ? 237 ALA A O   1 
ATOM   1497 C  CB  . ALA A 1 209 ? 8.005   -18.852 79.727  1.00 28.71 ? 237 ALA A CB  1 
ATOM   1498 N  N   . LEU A 1 210 ? 10.935  -18.462 80.779  1.00 29.77 ? 238 LEU A N   1 
ATOM   1499 C  CA  . LEU A 1 210 ? 12.186  -17.701 80.831  1.00 34.57 ? 238 LEU A CA  1 
ATOM   1500 C  C   . LEU A 1 210 ? 13.380  -18.574 80.482  1.00 32.61 ? 238 LEU A C   1 
ATOM   1501 O  O   . LEU A 1 210 ? 14.227  -18.200 79.663  1.00 32.31 ? 238 LEU A O   1 
ATOM   1502 C  CB  . LEU A 1 210 ? 12.388  -17.117 82.221  1.00 33.49 ? 238 LEU A CB  1 
ATOM   1503 C  CG  . LEU A 1 210 ? 11.725  -15.810 82.603  1.00 37.46 ? 238 LEU A CG  1 
ATOM   1504 C  CD1 . LEU A 1 210 ? 12.092  -15.566 84.053  1.00 36.82 ? 238 LEU A CD1 1 
ATOM   1505 C  CD2 . LEU A 1 210 ? 12.216  -14.680 81.709  1.00 37.64 ? 238 LEU A CD2 1 
ATOM   1506 N  N   . THR A 1 211 ? 13.471  -19.737 81.123  1.00 33.03 ? 239 THR A N   1 
ATOM   1507 C  CA  . THR A 1 211 ? 14.597  -20.636 80.902  1.00 33.99 ? 239 THR A CA  1 
ATOM   1508 C  C   . THR A 1 211 ? 14.718  -21.006 79.430  1.00 34.43 ? 239 THR A C   1 
ATOM   1509 O  O   . THR A 1 211 ? 15.815  -20.987 78.863  1.00 31.90 ? 239 THR A O   1 
ATOM   1510 C  CB  . THR A 1 211 ? 14.413  -21.886 81.760  1.00 35.82 ? 239 THR A CB  1 
ATOM   1511 O  OG1 . THR A 1 211 ? 14.252  -21.500 83.133  1.00 39.36 ? 239 THR A OG1 1 
ATOM   1512 C  CG2 . THR A 1 211 ? 15.607  -22.811 81.624  1.00 41.92 ? 239 THR A CG2 1 
ATOM   1513 N  N   . TYR A 1 212 ? 13.584  -21.304 78.790  1.00 33.64 ? 240 TYR A N   1 
ATOM   1514 C  CA  . TYR A 1 212 ? 13.580  -21.657 77.377  1.00 29.48 ? 240 TYR A CA  1 
ATOM   1515 C  C   . TYR A 1 212 ? 14.100  -20.516 76.511  1.00 27.85 ? 240 TYR A C   1 
ATOM   1516 O  O   . TYR A 1 212 ? 15.032  -20.697 75.722  1.00 29.97 ? 240 TYR A O   1 
ATOM   1517 C  CB  . TYR A 1 212 ? 12.160  -22.047 76.953  1.00 29.35 ? 240 TYR A CB  1 
ATOM   1518 C  CG  . TYR A 1 212 ? 11.984  -22.123 75.455  1.00 32.33 ? 240 TYR A CG  1 
ATOM   1519 C  CD1 . TYR A 1 212 ? 12.583  -23.138 74.723  1.00 30.91 ? 240 TYR A CD1 1 
ATOM   1520 C  CD2 . TYR A 1 212 ? 11.207  -21.179 74.767  1.00 28.76 ? 240 TYR A CD2 1 
ATOM   1521 C  CE1 . TYR A 1 212 ? 12.441  -23.222 73.343  1.00 29.62 ? 240 TYR A CE1 1 
ATOM   1522 C  CE2 . TYR A 1 212 ? 11.043  -21.263 73.386  1.00 26.92 ? 240 TYR A CE2 1 
ATOM   1523 C  CZ  . TYR A 1 212 ? 11.654  -22.293 72.677  1.00 31.21 ? 240 TYR A CZ  1 
ATOM   1524 O  OH  . TYR A 1 212 ? 11.515  -22.393 71.302  1.00 26.45 ? 240 TYR A OH  1 
ATOM   1525 N  N   . VAL A 1 213 ? 13.495  -19.325 76.626  1.00 27.67 ? 241 VAL A N   1 
ATOM   1526 C  CA  . VAL A 1 213 ? 13.874  -18.228 75.739  1.00 28.47 ? 241 VAL A CA  1 
ATOM   1527 C  C   . VAL A 1 213 ? 15.296  -17.751 76.026  1.00 24.58 ? 241 VAL A C   1 
ATOM   1528 O  O   . VAL A 1 213 ? 16.101  -17.571 75.107  1.00 27.44 ? 241 VAL A O   1 
ATOM   1529 C  CB  . VAL A 1 213 ? 12.868  -17.069 75.843  1.00 26.35 ? 241 VAL A CB  1 
ATOM   1530 C  CG1 . VAL A 1 213 ? 13.304  -15.939 74.930  1.00 28.73 ? 241 VAL A CG1 1 
ATOM   1531 C  CG2 . VAL A 1 213 ? 11.481  -17.580 75.492  1.00 27.81 ? 241 VAL A CG2 1 
ATOM   1532 N  N   . ALA A 1 214 ? 15.612  -17.475 77.290  1.00 27.30 ? 242 ALA A N   1 
ATOM   1533 C  CA  . ALA A 1 214 ? 16.989  -17.084 77.605  1.00 28.49 ? 242 ALA A CA  1 
ATOM   1534 C  C   . ALA A 1 214 ? 17.978  -18.185 77.223  1.00 30.96 ? 242 ALA A C   1 
ATOM   1535 O  O   . ALA A 1 214 ? 19.133  -17.898 76.868  1.00 31.55 ? 242 ALA A O   1 
ATOM   1536 C  CB  . ALA A 1 214 ? 17.108  -16.737 79.091  1.00 27.14 ? 242 ALA A CB  1 
ATOM   1537 N  N   . GLY A 1 215 ? 17.530  -19.439 77.273  1.00 33.23 ? 243 GLY A N   1 
ATOM   1538 C  CA  . GLY A 1 215 ? 18.386  -20.555 76.891  1.00 34.16 ? 243 GLY A CA  1 
ATOM   1539 C  C   . GLY A 1 215 ? 18.891  -20.462 75.463  1.00 35.58 ? 243 GLY A C   1 
ATOM   1540 O  O   . GLY A 1 215 ? 20.089  -20.628 75.209  1.00 33.04 ? 243 GLY A O   1 
ATOM   1541 N  N   . PHE A 1 216 ? 17.990  -20.179 74.507  1.00 27.73 ? 244 PHE A N   1 
ATOM   1542 C  CA  . PHE A 1 216 ? 18.382  -20.213 73.100  1.00 26.19 ? 244 PHE A CA  1 
ATOM   1543 C  C   . PHE A 1 216 ? 18.819  -18.852 72.548  1.00 31.03 ? 244 PHE A C   1 
ATOM   1544 O  O   . PHE A 1 216 ? 19.475  -18.813 71.498  1.00 28.12 ? 244 PHE A O   1 
ATOM   1545 C  CB  . PHE A 1 216 ? 17.267  -20.862 72.230  1.00 29.82 ? 244 PHE A CB  1 
ATOM   1546 C  CG  . PHE A 1 216 ? 16.039  -19.981 71.923  1.00 29.39 ? 244 PHE A CG  1 
ATOM   1547 C  CD1 . PHE A 1 216 ? 14.797  -20.291 72.471  1.00 27.83 ? 244 PHE A CD1 1 
ATOM   1548 C  CD2 . PHE A 1 216 ? 16.118  -18.916 71.019  1.00 26.87 ? 244 PHE A CD2 1 
ATOM   1549 C  CE1 . PHE A 1 216 ? 13.656  -19.515 72.172  1.00 28.57 ? 244 PHE A CE1 1 
ATOM   1550 C  CE2 . PHE A 1 216 ? 14.981  -18.141 70.711  1.00 28.01 ? 244 PHE A CE2 1 
ATOM   1551 C  CZ  . PHE A 1 216 ? 13.757  -18.451 71.290  1.00 28.43 ? 244 PHE A CZ  1 
ATOM   1552 N  N   . THR A 1 217 ? 18.513  -17.740 73.226  1.00 26.57 ? 245 THR A N   1 
ATOM   1553 C  CA  . THR A 1 217 ? 18.956  -16.433 72.745  1.00 29.44 ? 245 THR A CA  1 
ATOM   1554 C  C   . THR A 1 217 ? 20.237  -15.952 73.404  1.00 28.26 ? 245 THR A C   1 
ATOM   1555 O  O   . THR A 1 217 ? 20.998  -15.217 72.778  1.00 30.94 ? 245 THR A O   1 
ATOM   1556 C  CB  . THR A 1 217 ? 17.907  -15.336 72.992  1.00 24.75 ? 245 THR A CB  1 
ATOM   1557 O  OG1 . THR A 1 217 ? 17.712  -15.190 74.401  1.00 28.62 ? 245 THR A OG1 1 
ATOM   1558 C  CG2 . THR A 1 217 ? 16.562  -15.645 72.310  1.00 27.50 ? 245 THR A CG2 1 
ATOM   1559 N  N   . GLY A 1 218 ? 20.465  -16.318 74.659  1.00 33.13 ? 246 GLY A N   1 
ATOM   1560 C  CA  . GLY A 1 218 ? 21.458  -15.636 75.454  1.00 32.67 ? 246 GLY A CA  1 
ATOM   1561 C  C   . GLY A 1 218 ? 20.991  -14.323 76.035  1.00 32.31 ? 246 GLY A C   1 
ATOM   1562 O  O   . GLY A 1 218 ? 21.810  -13.593 76.602  1.00 27.67 ? 246 GLY A O   1 
ATOM   1563 N  N   . PHE A 1 219 ? 19.707  -13.981 75.891  1.00 31.99 ? 247 PHE A N   1 
ATOM   1564 C  CA  . PHE A 1 219 ? 19.206  -12.744 76.473  1.00 28.16 ? 247 PHE A CA  1 
ATOM   1565 C  C   . PHE A 1 219 ? 19.300  -12.821 77.988  1.00 29.70 ? 247 PHE A C   1 
ATOM   1566 O  O   . PHE A 1 219 ? 19.074  -13.877 78.586  1.00 30.08 ? 247 PHE A O   1 
ATOM   1567 C  CB  . PHE A 1 219 ? 17.741  -12.479 76.055  1.00 29.71 ? 247 PHE A CB  1 
ATOM   1568 C  CG  . PHE A 1 219 ? 17.569  -12.097 74.606  1.00 29.62 ? 247 PHE A CG  1 
ATOM   1569 C  CD1 . PHE A 1 219 ? 18.662  -11.755 73.821  1.00 29.58 ? 247 PHE A CD1 1 
ATOM   1570 C  CD2 . PHE A 1 219 ? 16.297  -12.066 74.033  1.00 28.74 ? 247 PHE A CD2 1 
ATOM   1571 C  CE1 . PHE A 1 219 ? 18.511  -11.410 72.496  1.00 27.38 ? 247 PHE A CE1 1 
ATOM   1572 C  CE2 . PHE A 1 219 ? 16.131  -11.720 72.703  1.00 30.50 ? 247 PHE A CE2 1 
ATOM   1573 C  CZ  . PHE A 1 219 ? 17.227  -11.384 71.928  1.00 31.03 ? 247 PHE A CZ  1 
ATOM   1574 N  N   . HIS A 1 220 ? 19.652  -11.701 78.611  1.00 29.65 ? 248 HIS A N   1 
ATOM   1575 C  CA  . HIS A 1 220 ? 19.845  -11.656 80.051  1.00 33.52 ? 248 HIS A CA  1 
ATOM   1576 C  C   . HIS A 1 220 ? 18.635  -11.032 80.730  1.00 33.88 ? 248 HIS A C   1 
ATOM   1577 O  O   . HIS A 1 220 ? 17.829  -10.340 80.107  1.00 37.36 ? 248 HIS A O   1 
ATOM   1578 C  CB  . HIS A 1 220 ? 21.111  -10.870 80.409  1.00 33.56 ? 248 HIS A CB  1 
ATOM   1579 C  CG  . HIS A 1 220 ? 21.059  -9.432  80.008  1.00 33.34 ? 248 HIS A CG  1 
ATOM   1580 N  ND1 . HIS A 1 220 ? 21.353  -9.003  78.731  1.00 31.42 ? 248 HIS A ND1 1 
ATOM   1581 C  CD2 . HIS A 1 220 ? 20.732  -8.321  80.712  1.00 34.92 ? 248 HIS A CD2 1 
ATOM   1582 C  CE1 . HIS A 1 220 ? 21.217  -7.692  78.668  1.00 31.80 ? 248 HIS A CE1 1 
ATOM   1583 N  NE2 . HIS A 1 220 ? 20.839  -7.254  79.856  1.00 32.98 ? 248 HIS A NE2 1 
ATOM   1584 N  N   . GLN A 1 221 ? 18.526  -11.274 82.030  1.00 33.22 ? 249 GLN A N   1 
ATOM   1585 C  CA  . GLN A 1 221 ? 17.442  -10.695 82.809  1.00 37.22 ? 249 GLN A CA  1 
ATOM   1586 C  C   . GLN A 1 221 ? 17.698  -9.211  83.036  1.00 40.86 ? 249 GLN A C   1 
ATOM   1587 O  O   . GLN A 1 221 ? 18.739  -8.824  83.579  1.00 37.88 ? 249 GLN A O   1 
ATOM   1588 C  CB  . GLN A 1 221 ? 17.293  -11.423 84.139  1.00 42.11 ? 249 GLN A CB  1 
ATOM   1589 C  CG  . GLN A 1 221 ? 16.336  -10.730 85.079  1.00 45.18 ? 249 GLN A CG  1 
ATOM   1590 C  CD  . GLN A 1 221 ? 15.457  -11.697 85.841  1.00 49.35 ? 249 GLN A CD  1 
ATOM   1591 O  OE1 . GLN A 1 221 ? 15.600  -12.916 85.723  1.00 50.48 ? 249 GLN A OE1 1 
ATOM   1592 N  NE2 . GLN A 1 221 ? 14.524  -11.154 86.617  1.00 51.27 ? 249 GLN A NE2 1 
ATOM   1593 N  N   . PHE A 1 222 ? 16.749  -8.384  82.608  1.00 37.44 ? 250 PHE A N   1 
ATOM   1594 C  CA  . PHE A 1 222 ? 16.832  -6.937  82.743  1.00 39.81 ? 250 PHE A CA  1 
ATOM   1595 C  C   . PHE A 1 222 ? 16.331  -6.529  84.124  1.00 45.82 ? 250 PHE A C   1 
ATOM   1596 O  O   . PHE A 1 222 ? 15.280  -6.995  84.580  1.00 44.27 ? 250 PHE A O   1 
ATOM   1597 C  CB  . PHE A 1 222 ? 16.011  -6.268  81.633  1.00 40.75 ? 250 PHE A CB  1 
ATOM   1598 C  CG  . PHE A 1 222 ? 16.043  -4.762  81.650  1.00 41.10 ? 250 PHE A CG  1 
ATOM   1599 C  CD1 . PHE A 1 222 ? 15.160  -4.040  82.443  1.00 44.81 ? 250 PHE A CD1 1 
ATOM   1600 C  CD2 . PHE A 1 222 ? 16.938  -4.067  80.851  1.00 43.93 ? 250 PHE A CD2 1 
ATOM   1601 C  CE1 . PHE A 1 222 ? 15.180  -2.657  82.457  1.00 40.88 ? 250 PHE A CE1 1 
ATOM   1602 C  CE2 . PHE A 1 222 ? 16.959  -2.682  80.852  1.00 43.35 ? 250 PHE A CE2 1 
ATOM   1603 C  CZ  . PHE A 1 222 ? 16.078  -1.974  81.661  1.00 42.88 ? 250 PHE A CZ  1 
ATOM   1604 N  N   . ALA A 1 223 ? 17.083  -5.637  84.773  1.00 51.64 ? 251 ALA A N   1 
ATOM   1605 C  CA  . ALA A 1 223 ? 16.926  -5.355  86.198  1.00 59.58 ? 251 ALA A CA  1 
ATOM   1606 C  C   . ALA A 1 223 ? 15.653  -4.565  86.496  1.00 60.98 ? 251 ALA A C   1 
ATOM   1607 O  O   . ALA A 1 223 ? 15.418  -3.502  85.913  1.00 58.65 ? 251 ALA A O   1 
ATOM   1608 C  CB  . ALA A 1 223 ? 18.146  -4.588  86.710  1.00 59.71 ? 251 ALA A CB  1 
ATOM   1609 N  N   . GLU A 1 224 ? 14.845  -5.076  87.427  1.00 61.81 ? 252 GLU A N   1 
ATOM   1610 C  CA  . GLU A 1 224 ? 13.602  -4.412  87.814  1.00 65.97 ? 252 GLU A CA  1 
ATOM   1611 C  C   . GLU A 1 224 ? 13.793  -3.543  89.061  1.00 68.76 ? 252 GLU A C   1 
ATOM   1612 O  O   . GLU A 1 224 ? 14.490  -3.927  90.003  1.00 69.46 ? 252 GLU A O   1 
ATOM   1613 C  CB  . GLU A 1 224 ? 12.493  -5.443  88.056  1.00 65.65 ? 252 GLU A CB  1 
ATOM   1614 C  CG  . GLU A 1 224 ? 11.076  -4.927  87.762  1.00 62.31 ? 252 GLU A CG  1 
ATOM   1615 C  CD  . GLU A 1 224 ? 10.754  -4.926  86.271  1.00 60.23 ? 252 GLU A CD  1 
ATOM   1616 O  OE1 . GLU A 1 224 ? 9.622   -4.535  85.884  1.00 45.22 ? 252 GLU A OE1 1 
ATOM   1617 O  OE2 . GLU A 1 224 ? 11.639  -5.334  85.485  1.00 62.00 ? 252 GLU A OE2 1 
ATOM   1618 N  N   . GLU A 1 234 ? -0.075  -7.689  96.032  1.00 69.01 ? 262 GLU A N   1 
ATOM   1619 C  CA  . GLU A 1 234 ? -0.515  -8.732  95.108  1.00 71.10 ? 262 GLU A CA  1 
ATOM   1620 C  C   . GLU A 1 234 ? -1.585  -8.207  94.156  1.00 67.01 ? 262 GLU A C   1 
ATOM   1621 O  O   . GLU A 1 234 ? -2.698  -7.876  94.577  1.00 63.26 ? 262 GLU A O   1 
ATOM   1622 C  CB  . GLU A 1 234 ? -1.049  -9.947  95.872  1.00 71.88 ? 262 GLU A CB  1 
ATOM   1623 N  N   . SER A 1 235 ? -1.241  -8.139  92.863  1.00 66.04 ? 263 SER A N   1 
ATOM   1624 C  CA  . SER A 1 235 ? -2.158  -7.632  91.851  1.00 60.82 ? 263 SER A CA  1 
ATOM   1625 C  C   . SER A 1 235 ? -1.882  -8.311  90.505  1.00 55.52 ? 263 SER A C   1 
ATOM   1626 O  O   . SER A 1 235 ? -1.504  -7.698  89.503  1.00 50.89 ? 263 SER A O   1 
ATOM   1627 C  CB  . SER A 1 235 ? -2.056  -6.115  91.716  1.00 58.85 ? 263 SER A CB  1 
ATOM   1628 O  OG  . SER A 1 235 ? -1.023  -5.812  90.800  1.00 60.88 ? 263 SER A OG  1 
ATOM   1629 N  N   . GLY A 1 236 ? -2.077  -9.620  90.464  1.00 50.70 ? 264 GLY A N   1 
ATOM   1630 C  CA  . GLY A 1 236 ? -2.272  -10.275 89.191  1.00 50.71 ? 264 GLY A CA  1 
ATOM   1631 C  C   . GLY A 1 236 ? -1.145  -11.120 88.642  1.00 43.43 ? 264 GLY A C   1 
ATOM   1632 O  O   . GLY A 1 236 ? -1.416  -12.139 88.002  1.00 42.42 ? 264 GLY A O   1 
ATOM   1633 N  N   . LEU A 1 237 ? 0.111   -10.731 88.855  1.00 41.82 ? 265 LEU A N   1 
ATOM   1634 C  CA  . LEU A 1 237 ? 1.160   -11.337 88.048  1.00 41.47 ? 265 LEU A CA  1 
ATOM   1635 C  C   . LEU A 1 237 ? 2.494   -11.363 88.775  1.00 38.59 ? 265 LEU A C   1 
ATOM   1636 O  O   . LEU A 1 237 ? 2.729   -10.616 89.726  1.00 37.53 ? 265 LEU A O   1 
ATOM   1637 C  CB  . LEU A 1 237 ? 1.341   -10.590 86.720  1.00 37.68 ? 265 LEU A CB  1 
ATOM   1638 C  CG  . LEU A 1 237 ? 2.170   -9.290  86.734  1.00 42.41 ? 265 LEU A CG  1 
ATOM   1639 C  CD1 . LEU A 1 237 ? 2.221   -8.692  85.341  1.00 41.87 ? 265 LEU A CD1 1 
ATOM   1640 C  CD2 . LEU A 1 237 ? 1.641   -8.252  87.712  1.00 47.56 ? 265 LEU A CD2 1 
ATOM   1641 N  N   . ASN A 1 238 ? 3.356   -12.260 88.306  1.00 36.79 ? 266 ASN A N   1 
ATOM   1642 C  CA  . ASN A 1 238 ? 4.802   -12.140 88.399  1.00 37.47 ? 266 ASN A CA  1 
ATOM   1643 C  C   . ASN A 1 238 ? 5.328   -11.924 86.992  1.00 37.86 ? 266 ASN A C   1 
ATOM   1644 O  O   . ASN A 1 238 ? 4.747   -12.417 86.021  1.00 37.34 ? 266 ASN A O   1 
ATOM   1645 C  CB  . ASN A 1 238 ? 5.459   -13.400 88.987  1.00 38.80 ? 266 ASN A CB  1 
ATOM   1646 C  CG  . ASN A 1 238 ? 4.929   -13.756 90.353  1.00 40.22 ? 266 ASN A CG  1 
ATOM   1647 O  OD1 . ASN A 1 238 ? 4.768   -12.890 91.216  1.00 42.48 ? 266 ASN A OD1 1 
ATOM   1648 N  ND2 . ASN A 1 238 ? 4.653   -15.036 90.562  1.00 39.72 ? 266 ASN A ND2 1 
ATOM   1649 N  N   . SER A 1 239 ? 6.436   -11.201 86.873  1.00 33.57 ? 267 SER A N   1 
ATOM   1650 C  CA  . SER A 1 239 ? 7.000   -11.013 85.547  1.00 36.16 ? 267 SER A CA  1 
ATOM   1651 C  C   . SER A 1 239 ? 8.513   -10.885 85.632  1.00 37.67 ? 267 SER A C   1 
ATOM   1652 O  O   . SER A 1 239 ? 9.082   -10.662 86.702  1.00 40.31 ? 267 SER A O   1 
ATOM   1653 C  CB  . SER A 1 239 ? 6.405   -9.783  84.853  1.00 39.09 ? 267 SER A CB  1 
ATOM   1654 O  OG  . SER A 1 239 ? 7.008   -8.608  85.336  1.00 44.01 ? 267 SER A OG  1 
ATOM   1655 N  N   . ALA A 1 240 ? 9.153   -11.056 84.476  1.00 33.92 ? 268 ALA A N   1 
ATOM   1656 C  CA  . ALA A 1 240 ? 10.579  -10.836 84.306  1.00 36.99 ? 268 ALA A CA  1 
ATOM   1657 C  C   . ALA A 1 240 ? 10.812  -10.419 82.861  1.00 35.94 ? 268 ALA A C   1 
ATOM   1658 O  O   . ALA A 1 240 ? 10.005  -10.704 81.971  1.00 29.52 ? 268 ALA A O   1 
ATOM   1659 C  CB  . ALA A 1 240 ? 11.400  -12.083 84.653  1.00 34.98 ? 268 ALA A CB  1 
ATOM   1660 N  N   . VAL A 1 241 ? 11.923  -9.734  82.632  1.00 30.49 ? 269 VAL A N   1 
ATOM   1661 C  CA  . VAL A 1 241 ? 12.204  -9.117  81.342  1.00 28.68 ? 269 VAL A CA  1 
ATOM   1662 C  C   . VAL A 1 241 ? 13.530  -9.647  80.818  1.00 33.11 ? 269 VAL A C   1 
ATOM   1663 O  O   . VAL A 1 241 ? 14.558  -9.543  81.502  1.00 32.17 ? 269 VAL A O   1 
ATOM   1664 C  CB  . VAL A 1 241 ? 12.247  -7.590  81.458  1.00 27.65 ? 269 VAL A CB  1 
ATOM   1665 C  CG1 . VAL A 1 241 ? 12.530  -6.971  80.100  1.00 30.14 ? 269 VAL A CG1 1 
ATOM   1666 C  CG2 . VAL A 1 241 ? 10.938  -7.078  82.047  1.00 29.68 ? 269 VAL A CG2 1 
ATOM   1667 N  N   . LEU A 1 242 ? 13.519  -10.175 79.594  1.00 29.40 ? 270 LEU A N   1 
ATOM   1668 C  CA  . LEU A 1 242 ? 14.742  -10.576 78.903  1.00 30.63 ? 270 LEU A CA  1 
ATOM   1669 C  C   . LEU A 1 242 ? 15.161  -9.487  77.925  1.00 31.93 ? 270 LEU A C   1 
ATOM   1670 O  O   . LEU A 1 242 ? 14.309  -8.873  77.282  1.00 25.43 ? 270 LEU A O   1 
ATOM   1671 C  CB  . LEU A 1 242 ? 14.538  -11.886 78.149  1.00 26.77 ? 270 LEU A CB  1 
ATOM   1672 C  CG  . LEU A 1 242 ? 14.295  -13.101 79.039  1.00 31.98 ? 270 LEU A CG  1 
ATOM   1673 C  CD1 . LEU A 1 242 ? 13.903  -14.318 78.211  1.00 31.24 ? 270 LEU A CD1 1 
ATOM   1674 C  CD2 . LEU A 1 242 ? 15.561  -13.389 79.848  1.00 32.40 ? 270 LEU A CD2 1 
ATOM   1675 N  N   . ALA A 1 243 ? 16.478  -9.265  77.797  1.00 28.53 ? 271 ALA A N   1 
ATOM   1676 C  CA  . ALA A 1 243 ? 17.012  -8.184  76.974  1.00 28.87 ? 271 ALA A CA  1 
ATOM   1677 C  C   . ALA A 1 243 ? 18.243  -8.631  76.189  1.00 30.52 ? 271 ALA A C   1 
ATOM   1678 O  O   . ALA A 1 243 ? 19.012  -9.490  76.638  1.00 31.79 ? 271 ALA A O   1 
ATOM   1679 C  CB  . ALA A 1 243 ? 17.379  -6.962  77.834  1.00 32.35 ? 271 ALA A CB  1 
ATOM   1680 N  N   . SER A 1 244 ? 18.434  -8.016  75.015  1.00 30.46 ? 272 SER A N   1 
ATOM   1681 C  CA  . SER A 1 244 ? 19.593  -8.252  74.172  1.00 30.73 ? 272 SER A CA  1 
ATOM   1682 C  C   . SER A 1 244 ? 20.783  -7.463  74.727  1.00 30.78 ? 272 SER A C   1 
ATOM   1683 O  O   . SER A 1 244 ? 20.663  -6.754  75.729  1.00 32.13 ? 272 SER A O   1 
ATOM   1684 C  CB  . SER A 1 244 ? 19.287  -7.868  72.723  1.00 27.35 ? 272 SER A CB  1 
ATOM   1685 O  OG  . SER A 1 244 ? 19.034  -6.474  72.602  1.00 28.75 ? 272 SER A OG  1 
ATOM   1686 N  N   . ASN A 1 245 ? 21.935  -7.564  74.053  1.00 33.26 ? 273 ASN A N   1 
ATOM   1687 C  CA  . ASN A 1 245 ? 23.181  -7.019  74.604  1.00 30.97 ? 273 ASN A CA  1 
ATOM   1688 C  C   . ASN A 1 245 ? 23.064  -5.523  74.905  1.00 35.94 ? 273 ASN A C   1 
ATOM   1689 O  O   . ASN A 1 245 ? 23.420  -5.070  76.001  1.00 35.90 ? 273 ASN A O   1 
ATOM   1690 C  CB  . ASN A 1 245 ? 24.343  -7.293  73.642  1.00 29.91 ? 273 ASN A CB  1 
ATOM   1691 C  CG  . ASN A 1 245 ? 24.929  -8.694  73.801  1.00 36.10 ? 273 ASN A CG  1 
ATOM   1692 O  OD1 . ASN A 1 245 ? 24.490  -9.485  74.644  1.00 33.91 ? 273 ASN A OD1 1 
ATOM   1693 N  ND2 . ASN A 1 245 ? 25.931  -9.005  72.984  1.00 35.16 ? 273 ASN A ND2 1 
ATOM   1694 N  N   . ASP A 1 246 ? 22.568  -4.735  73.953  1.00 30.47 ? 274 ASP A N   1 
ATOM   1695 C  CA  . ASP A 1 246 ? 22.407  -3.306  74.203  1.00 33.43 ? 274 ASP A CA  1 
ATOM   1696 C  C   . ASP A 1 246 ? 21.048  -2.967  74.813  1.00 37.29 ? 274 ASP A C   1 
ATOM   1697 O  O   . ASP A 1 246 ? 20.717  -1.782  74.943  1.00 31.07 ? 274 ASP A O   1 
ATOM   1698 C  CB  . ASP A 1 246 ? 22.634  -2.494  72.917  1.00 35.98 ? 274 ASP A CB  1 
ATOM   1699 C  CG  . ASP A 1 246 ? 21.654  -2.834  71.792  1.00 39.39 ? 274 ASP A CG  1 
ATOM   1700 O  OD1 . ASP A 1 246 ? 20.634  -3.539  72.018  1.00 31.17 ? 274 ASP A OD1 1 
ATOM   1701 O  OD2 . ASP A 1 246 ? 21.911  -2.369  70.658  1.00 36.28 ? 274 ASP A OD2 1 
ATOM   1702 N  N   . GLU A 1 247 ? 20.260  -3.987  75.167  1.00 33.14 ? 275 GLU A N   1 
ATOM   1703 C  CA  . GLU A 1 247 ? 18.988  -3.842  75.873  1.00 31.41 ? 275 GLU A CA  1 
ATOM   1704 C  C   . GLU A 1 247 ? 17.971  -3.033  75.062  1.00 33.35 ? 275 GLU A C   1 
ATOM   1705 O  O   . GLU A 1 247 ? 17.068  -2.403  75.617  1.00 28.71 ? 275 GLU A O   1 
ATOM   1706 C  CB  . GLU A 1 247 ? 19.216  -3.267  77.278  1.00 35.70 ? 275 GLU A CB  1 
ATOM   1707 C  CG  . GLU A 1 247 ? 20.266  -4.099  78.076  1.00 34.95 ? 275 GLU A CG  1 
ATOM   1708 C  CD  . GLU A 1 247 ? 20.304  -3.787  79.574  1.00 39.84 ? 275 GLU A CD  1 
ATOM   1709 O  OE1 . GLU A 1 247 ? 20.477  -4.732  80.373  1.00 38.21 ? 275 GLU A OE1 1 
ATOM   1710 O  OE2 . GLU A 1 247 ? 20.172  -2.599  79.952  1.00 44.96 ? 275 GLU A OE2 1 
ATOM   1711 N  N   . MET A 1 248 ? 18.106  -3.080  73.732  1.00 29.23 ? 276 MET A N   1 
ATOM   1712 C  CA  . MET A 1 248 ? 17.152  -2.471  72.812  1.00 30.96 ? 276 MET A CA  1 
ATOM   1713 C  C   . MET A 1 248 ? 16.069  -3.440  72.353  1.00 28.53 ? 276 MET A C   1 
ATOM   1714 O  O   . MET A 1 248 ? 15.043  -3.003  71.823  1.00 28.01 ? 276 MET A O   1 
ATOM   1715 C  CB  . MET A 1 248 ? 17.890  -1.931  71.583  1.00 34.25 ? 276 MET A CB  1 
ATOM   1716 C  CG  . MET A 1 248 ? 18.769  -0.734  71.893  1.00 31.36 ? 276 MET A CG  1 
ATOM   1717 S  SD  . MET A 1 248 ? 17.750  0.728   71.987  1.00 47.73 ? 276 MET A SD  1 
ATOM   1718 C  CE  . MET A 1 248 ? 17.640  0.896   73.713  1.00 30.98 ? 276 MET A CE  1 
ATOM   1719 N  N   . VAL A 1 249 ? 16.292  -4.738  72.492  1.00 27.53 ? 277 VAL A N   1 
ATOM   1720 C  CA  . VAL A 1 249 ? 15.240  -5.725  72.313  1.00 22.61 ? 277 VAL A CA  1 
ATOM   1721 C  C   . VAL A 1 249 ? 14.840  -6.181  73.705  1.00 27.67 ? 277 VAL A C   1 
ATOM   1722 O  O   . VAL A 1 249 ? 15.674  -6.719  74.447  1.00 26.51 ? 277 VAL A O   1 
ATOM   1723 C  CB  . VAL A 1 249 ? 15.703  -6.901  71.441  1.00 25.92 ? 277 VAL A CB  1 
ATOM   1724 C  CG1 . VAL A 1 249 ? 14.708  -8.041  71.531  1.00 21.51 ? 277 VAL A CG1 1 
ATOM   1725 C  CG2 . VAL A 1 249 ? 15.858  -6.446  70.005  1.00 25.34 ? 277 VAL A CG2 1 
ATOM   1726 N  N   . LEU A 1 250 ? 13.578  -5.920  74.074  1.00 24.28 ? 278 LEU A N   1 
ATOM   1727 C  CA  . LEU A 1 250 ? 13.072  -6.163  75.422  1.00 23.79 ? 278 LEU A CA  1 
ATOM   1728 C  C   . LEU A 1 250 ? 11.830  -7.031  75.340  1.00 24.94 ? 278 LEU A C   1 
ATOM   1729 O  O   . LEU A 1 250 ? 10.835  -6.641  74.720  1.00 24.28 ? 278 LEU A O   1 
ATOM   1730 C  CB  . LEU A 1 250 ? 12.748  -4.849  76.136  1.00 25.46 ? 278 LEU A CB  1 
ATOM   1731 C  CG  . LEU A 1 250 ? 13.898  -3.858  76.222  1.00 26.98 ? 278 LEU A CG  1 
ATOM   1732 C  CD1 . LEU A 1 250 ? 13.396  -2.515  76.747  1.00 28.06 ? 278 LEU A CD1 1 
ATOM   1733 C  CD2 . LEU A 1 250 ? 14.985  -4.413  77.124  1.00 26.63 ? 278 LEU A CD2 1 
ATOM   1734 N  N   . LEU A 1 251 ? 11.883  -8.184  75.997  1.00 24.88 ? 279 LEU A N   1 
ATOM   1735 C  CA  . LEU A 1 251 ? 10.825  -9.191  75.938  1.00 25.12 ? 279 LEU A CA  1 
ATOM   1736 C  C   . LEU A 1 251 ? 10.393  -9.543  77.351  1.00 25.27 ? 279 LEU A C   1 
ATOM   1737 O  O   . LEU A 1 251 ? 10.866  -10.538 77.922  1.00 26.16 ? 279 LEU A O   1 
ATOM   1738 C  CB  . LEU A 1 251 ? 11.304  -10.442 75.202  1.00 21.18 ? 279 LEU A CB  1 
ATOM   1739 C  CG  . LEU A 1 251 ? 11.678  -10.243 73.737  1.00 23.27 ? 279 LEU A CG  1 
ATOM   1740 C  CD1 . LEU A 1 251 ? 12.235  -11.533 73.166  1.00 24.01 ? 279 LEU A CD1 1 
ATOM   1741 C  CD2 . LEU A 1 251 ? 10.458  -9.780  72.929  1.00 21.82 ? 279 LEU A CD2 1 
ATOM   1742 N  N   . PRO A 1 252 ? 9.496   -8.760  77.940  1.00 22.83 ? 280 PRO A N   1 
ATOM   1743 C  CA  . PRO A 1 252 ? 8.906   -9.154  79.223  1.00 23.20 ? 280 PRO A CA  1 
ATOM   1744 C  C   . PRO A 1 252 ? 7.985   -10.361 79.060  1.00 28.20 ? 280 PRO A C   1 
ATOM   1745 O  O   . PRO A 1 252 ? 7.396   -10.589 77.996  1.00 26.56 ? 280 PRO A O   1 
ATOM   1746 C  CB  . PRO A 1 252 ? 8.113   -7.910  79.655  1.00 25.57 ? 280 PRO A CB  1 
ATOM   1747 C  CG  . PRO A 1 252 ? 8.649   -6.757  78.808  1.00 23.69 ? 280 PRO A CG  1 
ATOM   1748 C  CD  . PRO A 1 252 ? 9.072   -7.406  77.512  1.00 21.64 ? 280 PRO A CD  1 
ATOM   1749 N  N   . ILE A 1 253 ? 7.878   -11.146 80.134  1.00 26.68 ? 281 ILE A N   1 
ATOM   1750 C  CA  . ILE A 1 253 ? 6.995   -12.311 80.181  1.00 24.86 ? 281 ILE A CA  1 
ATOM   1751 C  C   . ILE A 1 253 ? 6.289   -12.313 81.534  1.00 28.31 ? 281 ILE A C   1 
ATOM   1752 O  O   . ILE A 1 253 ? 6.931   -12.075 82.563  1.00 31.51 ? 281 ILE A O   1 
ATOM   1753 C  CB  . ILE A 1 253 ? 7.766   -13.630 79.966  1.00 26.77 ? 281 ILE A CB  1 
ATOM   1754 C  CG1 . ILE A 1 253 ? 8.561   -13.593 78.648  1.00 24.46 ? 281 ILE A CG1 1 
ATOM   1755 C  CG2 . ILE A 1 253 ? 6.793   -14.823 80.012  1.00 24.93 ? 281 ILE A CG2 1 
ATOM   1756 C  CD1 . ILE A 1 253 ? 9.360   -14.876 78.344  1.00 27.78 ? 281 ILE A CD1 1 
ATOM   1757 N  N   . ASN A 1 254 ? 4.967   -12.545 81.533  1.00 25.93 ? 282 ASN A N   1 
ATOM   1758 C  CA  . ASN A 1 254 ? 4.144   -12.549 82.736  1.00 28.92 ? 282 ASN A CA  1 
ATOM   1759 C  C   . ASN A 1 254 ? 3.563   -13.934 82.975  1.00 31.81 ? 282 ASN A C   1 
ATOM   1760 O  O   . ASN A 1 254 ? 3.321   -14.695 82.032  1.00 31.02 ? 282 ASN A O   1 
ATOM   1761 C  CB  . ASN A 1 254 ? 2.939   -11.579 82.664  1.00 27.59 ? 282 ASN A CB  1 
ATOM   1762 C  CG  . ASN A 1 254 ? 3.304   -10.188 82.206  1.00 29.53 ? 282 ASN A CG  1 
ATOM   1763 O  OD1 . ASN A 1 254 ? 4.361   -9.662  82.540  1.00 32.19 ? 282 ASN A OD1 1 
ATOM   1764 N  ND2 . ASN A 1 254 ? 2.393   -9.568  81.442  1.00 27.12 ? 282 ASN A ND2 1 
ATOM   1765 N  N   . GLU A 1 255 ? 3.305   -14.239 84.243  1.00 31.82 ? 283 GLU A N   1 
ATOM   1766 C  CA  . GLU A 1 255 ? 2.526   -15.395 84.651  1.00 30.65 ? 283 GLU A CA  1 
ATOM   1767 C  C   . GLU A 1 255 ? 1.471   -14.934 85.644  1.00 33.68 ? 283 GLU A C   1 
ATOM   1768 O  O   . GLU A 1 255 ? 1.638   -13.901 86.301  1.00 34.32 ? 283 GLU A O   1 
ATOM   1769 C  CB  . GLU A 1 255 ? 3.407   -16.481 85.289  1.00 33.04 ? 283 GLU A CB  1 
ATOM   1770 C  CG  . GLU A 1 255 ? 3.783   -16.208 86.732  1.00 33.80 ? 283 GLU A CG  1 
ATOM   1771 C  CD  . GLU A 1 255 ? 4.596   -17.344 87.348  1.00 38.07 ? 283 GLU A CD  1 
ATOM   1772 O  OE1 . GLU A 1 255 ? 5.185   -17.138 88.426  1.00 39.07 ? 283 GLU A OE1 1 
ATOM   1773 O  OE2 . GLU A 1 255 ? 4.646   -18.445 86.756  1.00 35.94 ? 283 GLU A OE2 1 
ATOM   1774 N  N   . PRO A 1 256 ? 0.366   -15.662 85.770  1.00 34.14 ? 284 PRO A N   1 
ATOM   1775 C  CA  . PRO A 1 256 ? -0.660  -15.248 86.734  1.00 37.16 ? 284 PRO A CA  1 
ATOM   1776 C  C   . PRO A 1 256 ? -0.235  -15.546 88.165  1.00 41.16 ? 284 PRO A C   1 
ATOM   1777 O  O   . PRO A 1 256 ? 0.578   -16.435 88.430  1.00 37.91 ? 284 PRO A O   1 
ATOM   1778 C  CB  . PRO A 1 256 ? -1.889  -16.082 86.343  1.00 38.77 ? 284 PRO A CB  1 
ATOM   1779 C  CG  . PRO A 1 256 ? -1.517  -16.812 85.092  1.00 40.94 ? 284 PRO A CG  1 
ATOM   1780 C  CD  . PRO A 1 256 ? -0.025  -16.874 85.039  1.00 33.94 ? 284 PRO A CD  1 
ATOM   1781 N  N   . VAL A 1 257 ? -0.781  -14.769 89.092  1.00 44.84 ? 285 VAL A N   1 
ATOM   1782 C  CA  . VAL A 1 257 ? -0.846  -15.156 90.495  1.00 52.10 ? 285 VAL A CA  1 
ATOM   1783 C  C   . VAL A 1 257 ? -2.289  -15.558 90.762  1.00 54.62 ? 285 VAL A C   1 
ATOM   1784 O  O   . VAL A 1 257 ? -3.214  -14.854 90.348  1.00 60.78 ? 285 VAL A O   1 
ATOM   1785 C  CB  . VAL A 1 257 ? -0.386  -14.017 91.420  1.00 51.49 ? 285 VAL A CB  1 
ATOM   1786 C  CG1 . VAL A 1 257 ? -0.567  -14.411 92.876  1.00 53.97 ? 285 VAL A CG1 1 
ATOM   1787 C  CG2 . VAL A 1 257 ? 1.068   -13.683 91.145  1.00 44.73 ? 285 VAL A CG2 1 
ATOM   1788 N  N   . HIS A 1 258 ? -2.489  -16.712 91.391  1.00 60.89 ? 286 HIS A N   1 
ATOM   1789 C  CA  . HIS A 1 258 ? -3.811  -17.321 91.468  1.00 63.98 ? 286 HIS A CA  1 
ATOM   1790 C  C   . HIS A 1 258 ? -4.460  -17.116 92.834  1.00 71.10 ? 286 HIS A C   1 
ATOM   1791 O  O   . HIS A 1 258 ? -3.780  -17.005 93.860  1.00 70.37 ? 286 HIS A O   1 
ATOM   1792 C  CB  . HIS A 1 258 ? -3.734  -18.818 91.156  1.00 62.63 ? 286 HIS A CB  1 
ATOM   1793 C  CG  . HIS A 1 258 ? -3.615  -19.125 89.697  1.00 61.10 ? 286 HIS A CG  1 
ATOM   1794 N  ND1 . HIS A 1 258 ? -2.819  -20.142 89.212  1.00 64.65 ? 286 HIS A ND1 1 
ATOM   1795 C  CD2 . HIS A 1 258 ? -4.198  -18.554 88.616  1.00 58.42 ? 286 HIS A CD2 1 
ATOM   1796 C  CE1 . HIS A 1 258 ? -2.915  -20.183 87.895  1.00 61.94 ? 286 HIS A CE1 1 
ATOM   1797 N  NE2 . HIS A 1 258 ? -3.746  -19.231 87.508  1.00 59.96 ? 286 HIS A NE2 1 
ATOM   1798 N  N   . GLY A 1 259 ? -5.797  -17.063 92.827  1.00 74.75 ? 287 GLY A N   1 
ATOM   1799 C  CA  . GLY A 1 259 ? -6.610  -16.921 94.026  1.00 73.66 ? 287 GLY A CA  1 
ATOM   1800 C  C   . GLY A 1 259 ? -6.364  -15.632 94.782  1.00 77.31 ? 287 GLY A C   1 
ATOM   1801 O  O   . GLY A 1 259 ? -5.951  -15.664 95.944  1.00 80.17 ? 287 GLY A O   1 
ATOM   1802 N  N   . THR A 1 260 ? -6.646  -14.489 94.144  1.00 76.98 ? 288 THR A N   1 
ATOM   1803 C  CA  . THR A 1 260 ? -6.053  -13.212 94.531  1.00 71.70 ? 288 THR A CA  1 
ATOM   1804 C  C   . THR A 1 260 ? -7.070  -12.141 94.902  1.00 71.36 ? 288 THR A C   1 
ATOM   1805 O  O   . THR A 1 260 ? -6.718  -10.955 94.880  1.00 74.38 ? 288 THR A O   1 
ATOM   1806 C  CB  . THR A 1 260 ? -5.177  -12.680 93.398  1.00 70.79 ? 288 THR A CB  1 
ATOM   1807 O  OG1 . THR A 1 260 ? -6.008  -12.049 92.414  1.00 69.88 ? 288 THR A OG1 1 
ATOM   1808 C  CG2 . THR A 1 260 ? -4.443  -13.803 92.752  1.00 66.35 ? 288 THR A CG2 1 
ATOM   1809 N  N   . LYS A 1 261 ? -8.309  -12.524 95.232  1.00 72.35 ? 289 LYS A N   1 
ATOM   1810 C  CA  . LYS A 1 261 ? -9.399  -11.596 95.548  1.00 71.55 ? 289 LYS A CA  1 
ATOM   1811 C  C   . LYS A 1 261 ? -9.975  -10.985 94.268  1.00 74.30 ? 289 LYS A C   1 
ATOM   1812 O  O   . LYS A 1 261 ? -11.130 -11.259 93.922  1.00 74.70 ? 289 LYS A O   1 
ATOM   1813 C  CB  . LYS A 1 261 ? -8.930  -10.521 96.544  1.00 68.38 ? 289 LYS A CB  1 
ATOM   1814 C  CG  . LYS A 1 261 ? -9.560  -9.147  96.394  1.00 67.63 ? 289 LYS A CG  1 
ATOM   1815 C  CD  . LYS A 1 261 ? -8.785  -8.116  97.192  1.00 67.48 ? 289 LYS A CD  1 
ATOM   1816 C  CE  . LYS A 1 261 ? -8.687  -8.522  98.653  1.00 66.02 ? 289 LYS A CE  1 
ATOM   1817 N  NZ  . LYS A 1 261 ? -10.031 -8.648  99.288  1.00 60.12 ? 289 LYS A NZ  1 
ATOM   1818 N  N   . ARG A 1 262 ? -9.189  -10.176 93.552  1.00 73.40 ? 290 ARG A N   1 
ATOM   1819 C  CA  . ARG A 1 262 ? -9.553  -9.669  92.232  1.00 65.53 ? 290 ARG A CA  1 
ATOM   1820 C  C   . ARG A 1 262 ? -8.873  -10.529 91.174  1.00 63.42 ? 290 ARG A C   1 
ATOM   1821 O  O   . ARG A 1 262 ? -7.683  -10.836 91.297  1.00 64.61 ? 290 ARG A O   1 
ATOM   1822 C  CB  . ARG A 1 262 ? -9.146  -8.203  92.073  1.00 65.08 ? 290 ARG A CB  1 
ATOM   1823 N  N   . LYS A 1 263 ? -9.624  -10.919 90.141  1.00 60.18 ? 291 LYS A N   1 
ATOM   1824 C  CA  . LYS A 1 263 ? -9.129  -11.922 89.203  1.00 56.87 ? 291 LYS A CA  1 
ATOM   1825 C  C   . LYS A 1 263 ? -7.929  -11.408 88.419  1.00 53.60 ? 291 LYS A C   1 
ATOM   1826 O  O   . LYS A 1 263 ? -7.906  -10.263 87.963  1.00 48.72 ? 291 LYS A O   1 
ATOM   1827 C  CB  . LYS A 1 263 ? -10.225 -12.360 88.233  1.00 54.67 ? 291 LYS A CB  1 
ATOM   1828 C  CG  . LYS A 1 263 ? -9.845  -13.609 87.445  1.00 52.93 ? 291 LYS A CG  1 
ATOM   1829 C  CD  . LYS A 1 263 ? -10.828 -13.924 86.327  1.00 51.82 ? 291 LYS A CD  1 
ATOM   1830 C  CE  . LYS A 1 263 ? -10.665 -15.363 85.864  1.00 50.56 ? 291 LYS A CE  1 
ATOM   1831 N  NZ  . LYS A 1 263 ? -11.520 -15.668 84.680  1.00 53.26 ? 291 LYS A NZ  1 
ATOM   1832 N  N   . SER A 1 264 ? -6.930  -12.276 88.267  1.00 48.89 ? 292 SER A N   1 
ATOM   1833 C  CA  . SER A 1 264 ? -5.717  -11.914 87.545  1.00 46.05 ? 292 SER A CA  1 
ATOM   1834 C  C   . SER A 1 264 ? -6.014  -11.650 86.076  1.00 38.57 ? 292 SER A C   1 
ATOM   1835 O  O   . SER A 1 264 ? -6.616  -12.481 85.392  1.00 39.40 ? 292 SER A O   1 
ATOM   1836 C  CB  . SER A 1 264 ? -4.683  -13.029 87.666  1.00 40.72 ? 292 SER A CB  1 
ATOM   1837 O  OG  . SER A 1 264 ? -3.564  -12.731 86.856  1.00 42.78 ? 292 SER A OG  1 
ATOM   1838 N  N   . GLN A 1 265 ? -5.559  -10.499 85.586  1.00 38.67 ? 293 GLN A N   1 
ATOM   1839 C  CA  . GLN A 1 265 ? -5.735  -10.198 84.172  1.00 38.00 ? 293 GLN A CA  1 
ATOM   1840 C  C   . GLN A 1 265 ? -4.921  -11.146 83.301  1.00 36.76 ? 293 GLN A C   1 
ATOM   1841 O  O   . GLN A 1 265 ? -5.271  -11.376 82.137  1.00 33.07 ? 293 GLN A O   1 
ATOM   1842 C  CB  . GLN A 1 265 ? -5.364  -8.741  83.889  1.00 38.64 ? 293 GLN A CB  1 
ATOM   1843 C  CG  . GLN A 1 265 ? -3.868  -8.431  83.933  1.00 37.88 ? 293 GLN A CG  1 
ATOM   1844 C  CD  . GLN A 1 265 ? -3.380  -8.012  85.308  1.00 44.79 ? 293 GLN A CD  1 
ATOM   1845 O  OE1 . GLN A 1 265 ? -4.164  -7.895  86.254  1.00 41.75 ? 293 GLN A OE1 1 
ATOM   1846 N  NE2 . GLN A 1 265 ? -2.069  -7.786  85.426  1.00 41.02 ? 293 GLN A NE2 1 
ATOM   1847 N  N   . ILE A 1 266 ? -3.839  -11.712 83.842  1.00 34.81 ? 294 ILE A N   1 
ATOM   1848 C  CA  . ILE A 1 266 ? -3.089  -12.716 83.097  1.00 31.10 ? 294 ILE A CA  1 
ATOM   1849 C  C   . ILE A 1 266 ? -3.923  -13.975 82.917  1.00 33.62 ? 294 ILE A C   1 
ATOM   1850 O  O   . ILE A 1 266 ? -3.907  -14.598 81.850  1.00 30.97 ? 294 ILE A O   1 
ATOM   1851 C  CB  . ILE A 1 266 ? -1.760  -13.034 83.803  1.00 30.83 ? 294 ILE A CB  1 
ATOM   1852 C  CG1 . ILE A 1 266 ? -1.026  -11.743 84.174  1.00 31.13 ? 294 ILE A CG1 1 
ATOM   1853 C  CG2 . ILE A 1 266 ? -0.895  -13.934 82.930  1.00 31.53 ? 294 ILE A CG2 1 
ATOM   1854 C  CD1 . ILE A 1 266 ? -0.809  -10.793 82.993  1.00 28.88 ? 294 ILE A CD1 1 
ATOM   1855 N  N   . GLN A 1 267 ? -4.638  -14.390 83.966  1.00 34.90 ? 295 GLN A N   1 
ATOM   1856 C  CA  . GLN A 1 267 ? -5.443  -15.602 83.874  1.00 36.42 ? 295 GLN A CA  1 
ATOM   1857 C  C   . GLN A 1 267 ? -6.622  -15.403 82.931  1.00 34.85 ? 295 GLN A C   1 
ATOM   1858 O  O   . GLN A 1 267 ? -6.953  -16.301 82.148  1.00 34.27 ? 295 GLN A O   1 
ATOM   1859 C  CB  . GLN A 1 267 ? -5.926  -16.022 85.262  1.00 39.05 ? 295 GLN A CB  1 
ATOM   1860 C  CG  . GLN A 1 267 ? -6.830  -17.261 85.253  1.00 42.39 ? 295 GLN A CG  1 
ATOM   1861 C  CD  . GLN A 1 267 ? -6.093  -18.522 84.849  1.00 39.24 ? 295 GLN A CD  1 
ATOM   1862 O  OE1 . GLN A 1 267 ? -4.876  -18.616 84.991  1.00 46.52 ? 295 GLN A OE1 1 
ATOM   1863 N  NE2 . GLN A 1 267 ? -6.830  -19.500 84.344  1.00 40.51 ? 295 GLN A NE2 1 
ATOM   1864 N  N   . THR A 1 268 ? -7.257  -14.229 82.982  1.00 34.74 ? 296 THR A N   1 
ATOM   1865 C  CA  . THR A 1 268 ? -8.322  -13.919 82.030  1.00 37.18 ? 296 THR A CA  1 
ATOM   1866 C  C   . THR A 1 268 ? -7.808  -14.014 80.599  1.00 31.61 ? 296 THR A C   1 
ATOM   1867 O  O   . THR A 1 268 ? -8.457  -14.608 79.727  1.00 27.66 ? 296 THR A O   1 
ATOM   1868 C  CB  . THR A 1 268 ? -8.886  -12.525 82.312  1.00 41.51 ? 296 THR A CB  1 
ATOM   1869 O  OG1 . THR A 1 268 ? -9.474  -12.497 83.621  1.00 41.04 ? 296 THR A OG1 1 
ATOM   1870 C  CG2 . THR A 1 268 ? -9.933  -12.132 81.259  1.00 36.31 ? 296 THR A CG2 1 
ATOM   1871 N  N   . TYR A 1 269 ? -6.631  -13.433 80.345  1.00 31.29 ? 297 TYR A N   1 
ATOM   1872 C  CA  . TYR A 1 269 ? -5.989  -13.556 79.038  1.00 26.74 ? 297 TYR A CA  1 
ATOM   1873 C  C   . TYR A 1 269 ? -5.894  -15.017 78.609  1.00 25.14 ? 297 TYR A C   1 
ATOM   1874 O  O   . TYR A 1 269 ? -6.312  -15.382 77.505  1.00 28.46 ? 297 TYR A O   1 
ATOM   1875 C  CB  . TYR A 1 269 ? -4.585  -12.926 79.069  1.00 26.49 ? 297 TYR A CB  1 
ATOM   1876 C  CG  . TYR A 1 269 ? -3.890  -13.049 77.729  1.00 24.29 ? 297 TYR A CG  1 
ATOM   1877 C  CD1 . TYR A 1 269 ? -3.272  -14.238 77.348  1.00 23.53 ? 297 TYR A CD1 1 
ATOM   1878 C  CD2 . TYR A 1 269 ? -3.875  -11.978 76.833  1.00 23.62 ? 297 TYR A CD2 1 
ATOM   1879 C  CE1 . TYR A 1 269 ? -2.667  -14.370 76.112  1.00 22.92 ? 297 TYR A CE1 1 
ATOM   1880 C  CE2 . TYR A 1 269 ? -3.278  -12.097 75.590  1.00 24.03 ? 297 TYR A CE2 1 
ATOM   1881 C  CZ  . TYR A 1 269 ? -2.669  -13.298 75.242  1.00 22.02 ? 297 TYR A CZ  1 
ATOM   1882 O  OH  . TYR A 1 269 ? -2.083  -13.469 74.015  1.00 20.15 ? 297 TYR A OH  1 
ATOM   1883 N  N   . LEU A 1 270 ? -5.296  -15.862 79.455  1.00 26.73 ? 298 LEU A N   1 
ATOM   1884 C  CA  . LEU A 1 270 ? -5.034  -17.236 79.051  1.00 27.62 ? 298 LEU A CA  1 
ATOM   1885 C  C   . LEU A 1 270 ? -6.336  -17.970 78.747  1.00 27.07 ? 298 LEU A C   1 
ATOM   1886 O  O   . LEU A 1 270 ? -6.386  -18.785 77.824  1.00 26.05 ? 298 LEU A O   1 
ATOM   1887 C  CB  . LEU A 1 270 ? -4.241  -17.969 80.144  1.00 31.02 ? 298 LEU A CB  1 
ATOM   1888 C  CG  . LEU A 1 270 ? -2.829  -17.444 80.455  1.00 28.35 ? 298 LEU A CG  1 
ATOM   1889 C  CD1 . LEU A 1 270 ? -2.306  -18.056 81.747  1.00 33.37 ? 298 LEU A CD1 1 
ATOM   1890 C  CD2 . LEU A 1 270 ? -1.878  -17.732 79.297  1.00 26.62 ? 298 LEU A CD2 1 
ATOM   1891 N  N   . GLU A 1 271 ? -7.401  -17.648 79.482  1.00 27.41 ? 299 GLU A N   1 
ATOM   1892 C  CA  . GLU A 1 271 ? -8.699  -18.276 79.243  1.00 31.02 ? 299 GLU A CA  1 
ATOM   1893 C  C   . GLU A 1 271 ? -9.265  -17.866 77.888  1.00 27.17 ? 299 GLU A C   1 
ATOM   1894 O  O   . GLU A 1 271 ? -9.636  -18.719 77.071  1.00 27.89 ? 299 GLU A O   1 
ATOM   1895 C  CB  . GLU A 1 271 ? -9.657  -17.918 80.380  1.00 31.58 ? 299 GLU A CB  1 
ATOM   1896 C  CG  . GLU A 1 271 ? -9.446  -18.797 81.618  1.00 38.35 ? 299 GLU A CG  1 
ATOM   1897 C  CD  . GLU A 1 271 ? -9.972  -18.177 82.907  1.00 43.95 ? 299 GLU A CD  1 
ATOM   1898 O  OE1 . GLU A 1 271 ? -10.652 -17.132 82.848  1.00 44.79 ? 299 GLU A OE1 1 
ATOM   1899 O  OE2 . GLU A 1 271 ? -9.693  -18.750 83.984  1.00 46.48 ? 299 GLU A OE2 1 
ATOM   1900 N  N   . HIS A 1 272 ? -9.292  -16.562 77.606  1.00 28.55 ? 300 HIS A N   1 
ATOM   1901 C  CA  . HIS A 1 272 ? -9.917  -16.118 76.369  1.00 25.14 ? 300 HIS A CA  1 
ATOM   1902 C  C   . HIS A 1 272 ? -9.046  -16.335 75.143  1.00 26.35 ? 300 HIS A C   1 
ATOM   1903 O  O   . HIS A 1 272 ? -9.587  -16.450 74.039  1.00 25.32 ? 300 HIS A O   1 
ATOM   1904 C  CB  . HIS A 1 272 ? -10.333 -14.657 76.513  1.00 24.82 ? 300 HIS A CB  1 
ATOM   1905 C  CG  . HIS A 1 272 ? -11.493 -14.481 77.436  1.00 27.53 ? 300 HIS A CG  1 
ATOM   1906 N  ND1 . HIS A 1 272 ? -12.785 -14.302 76.983  1.00 26.71 ? 300 HIS A ND1 1 
ATOM   1907 C  CD2 . HIS A 1 272 ? -11.567 -14.510 78.788  1.00 29.20 ? 300 HIS A CD2 1 
ATOM   1908 C  CE1 . HIS A 1 272 ? -13.601 -14.209 78.018  1.00 29.63 ? 300 HIS A CE1 1 
ATOM   1909 N  NE2 . HIS A 1 272 ? -12.888 -14.335 79.124  1.00 29.46 ? 300 HIS A NE2 1 
ATOM   1910 N  N   . ASN A 1 273 ? -7.726  -16.434 75.312  1.00 25.63 ? 301 ASN A N   1 
ATOM   1911 C  CA  . ASN A 1 273 ? -6.793  -16.643 74.212  1.00 25.09 ? 301 ASN A CA  1 
ATOM   1912 C  C   . ASN A 1 273 ? -6.551  -18.112 73.910  1.00 27.15 ? 301 ASN A C   1 
ATOM   1913 O  O   . ASN A 1 273 ? -5.824  -18.417 72.959  1.00 25.77 ? 301 ASN A O   1 
ATOM   1914 C  CB  . ASN A 1 273 ? -5.445  -15.984 74.529  1.00 24.44 ? 301 ASN A CB  1 
ATOM   1915 C  CG  . ASN A 1 273 ? -4.590  -15.762 73.291  1.00 23.56 ? 301 ASN A CG  1 
ATOM   1916 O  OD1 . ASN A 1 273 ? -4.952  -14.980 72.414  1.00 27.18 ? 301 ASN A OD1 1 
ATOM   1917 N  ND2 . ASN A 1 273 ? -3.423  -16.401 73.247  1.00 23.66 ? 301 ASN A ND2 1 
ATOM   1918 N  N   . GLU A 1 274 ? -7.121  -19.020 74.706  1.00 25.86 ? 302 GLU A N   1 
ATOM   1919 C  CA  . GLU A 1 274 ? -6.773  -20.441 74.642  1.00 23.03 ? 302 GLU A CA  1 
ATOM   1920 C  C   . GLU A 1 274 ? -5.266  -20.627 74.834  1.00 26.61 ? 302 GLU A C   1 
ATOM   1921 O  O   . GLU A 1 274 ? -4.586  -21.235 74.009  1.00 27.56 ? 302 GLU A O   1 
ATOM   1922 C  CB  . GLU A 1 274 ? -7.231  -21.075 73.329  1.00 24.29 ? 302 GLU A CB  1 
ATOM   1923 C  CG  . GLU A 1 274 ? -8.762  -21.125 73.158  1.00 25.18 ? 302 GLU A CG  1 
ATOM   1924 C  CD  . GLU A 1 274 ? -9.210  -21.944 71.961  1.00 28.16 ? 302 GLU A CD  1 
ATOM   1925 O  OE1 . GLU A 1 274 ? -8.363  -22.593 71.307  1.00 28.12 ? 302 GLU A OE1 1 
ATOM   1926 O  OE2 . GLU A 1 274 ? -10.430 -21.965 71.692  1.00 30.19 ? 302 GLU A OE2 1 
ATOM   1927 N  N   . GLY A 1 275 ? -4.742  -20.068 75.915  1.00 26.17 ? 303 GLY A N   1 
ATOM   1928 C  CA  . GLY A 1 275 ? -3.370  -20.318 76.315  1.00 26.38 ? 303 GLY A CA  1 
ATOM   1929 C  C   . GLY A 1 275 ? -2.445  -19.139 76.083  1.00 29.66 ? 303 GLY A C   1 
ATOM   1930 O  O   . GLY A 1 275 ? -2.866  -17.995 75.870  1.00 26.99 ? 303 GLY A O   1 
ATOM   1931 N  N   . ALA A 1 276 ? -1.148  -19.442 76.115  1.00 27.39 ? 304 ALA A N   1 
ATOM   1932 C  CA  . ALA A 1 276 ? -0.126  -18.412 76.071  1.00 24.10 ? 304 ALA A CA  1 
ATOM   1933 C  C   . ALA A 1 276 ? -0.141  -17.675 74.738  1.00 24.15 ? 304 ALA A C   1 
ATOM   1934 O  O   . ALA A 1 276 ? -0.496  -18.231 73.687  1.00 23.07 ? 304 ALA A O   1 
ATOM   1935 C  CB  . ALA A 1 276 ? 1.256   -19.027 76.300  1.00 24.80 ? 304 ALA A CB  1 
ATOM   1936 N  N   . GLY A 1 277 ? 0.275   -16.415 74.796  1.00 24.66 ? 305 GLY A N   1 
ATOM   1937 C  CA  . GLY A 1 277 ? 0.379   -15.591 73.607  1.00 23.01 ? 305 GLY A CA  1 
ATOM   1938 C  C   . GLY A 1 277 ? 0.869   -14.213 73.986  1.00 25.48 ? 305 GLY A C   1 
ATOM   1939 O  O   . GLY A 1 277 ? 1.141   -13.916 75.156  1.00 24.96 ? 305 GLY A O   1 
ATOM   1940 N  N   . LEU A 1 278 ? 0.957   -13.351 72.976  1.00 20.57 ? 306 LEU A N   1 
ATOM   1941 C  CA  . LEU A 1 278 ? 1.434   -11.999 73.215  1.00 20.54 ? 306 LEU A CA  1 
ATOM   1942 C  C   . LEU A 1 278 ? 0.338   -11.173 73.887  1.00 23.75 ? 306 LEU A C   1 
ATOM   1943 O  O   . LEU A 1 278 ? -0.801  -11.116 73.398  1.00 22.26 ? 306 LEU A O   1 
ATOM   1944 C  CB  . LEU A 1 278 ? 1.861   -11.358 71.896  1.00 19.63 ? 306 LEU A CB  1 
ATOM   1945 C  CG  . LEU A 1 278 ? 2.607   -10.028 72.035  1.00 22.34 ? 306 LEU A CG  1 
ATOM   1946 C  CD1 . LEU A 1 278 ? 3.717   -9.949  70.999  1.00 24.96 ? 306 LEU A CD1 1 
ATOM   1947 C  CD2 . LEU A 1 278 ? 1.649   -8.855  71.888  1.00 24.47 ? 306 LEU A CD2 1 
ATOM   1948 N  N   . GLN A 1 279 ? 0.676   -10.546 75.019  1.00 21.70 ? 307 GLN A N   1 
ATOM   1949 C  CA  . GLN A 1 279 ? -0.262  -9.719  75.777  1.00 22.37 ? 307 GLN A CA  1 
ATOM   1950 C  C   . GLN A 1 279 ? -0.328  -8.281  75.263  1.00 21.74 ? 307 GLN A C   1 
ATOM   1951 O  O   . GLN A 1 279 ? -1.421  -7.762  74.995  1.00 21.55 ? 307 GLN A O   1 
ATOM   1952 C  CB  . GLN A 1 279 ? 0.109   -9.686  77.266  1.00 23.77 ? 307 GLN A CB  1 
ATOM   1953 C  CG  . GLN A 1 279 ? -0.865  -8.855  78.119  1.00 24.18 ? 307 GLN A CG  1 
ATOM   1954 C  CD  . GLN A 1 279 ? -0.242  -8.335  79.424  1.00 27.62 ? 307 GLN A CD  1 
ATOM   1955 O  OE1 . GLN A 1 279 ? 0.912   -7.897  79.447  1.00 25.76 ? 307 GLN A OE1 1 
ATOM   1956 N  NE2 . GLN A 1 279 ? -1.010  -8.391  80.512  1.00 27.32 ? 307 GLN A NE2 1 
ATOM   1957 N  N   . HIS A 1 280 ? 0.816   -7.606  75.156  1.00 20.88 ? 308 HIS A N   1 
ATOM   1958 C  CA  . HIS A 1 280 ? 0.748   -6.229  74.692  1.00 23.33 ? 308 HIS A CA  1 
ATOM   1959 C  C   . HIS A 1 280 ? 2.012   -5.847  73.938  1.00 22.11 ? 308 HIS A C   1 
ATOM   1960 O  O   . HIS A 1 280 ? 3.074   -6.464  74.081  1.00 23.25 ? 308 HIS A O   1 
ATOM   1961 C  CB  . HIS A 1 280 ? 0.416   -5.243  75.851  1.00 20.58 ? 308 HIS A CB  1 
ATOM   1962 C  CG  . HIS A 1 280 ? 1.546   -4.929  76.794  1.00 24.59 ? 308 HIS A CG  1 
ATOM   1963 N  ND1 . HIS A 1 280 ? 1.801   -5.671  77.932  1.00 24.19 ? 308 HIS A ND1 1 
ATOM   1964 C  CD2 . HIS A 1 280 ? 2.427   -3.896  76.821  1.00 26.82 ? 308 HIS A CD2 1 
ATOM   1965 C  CE1 . HIS A 1 280 ? 2.807   -5.130  78.597  1.00 25.86 ? 308 HIS A CE1 1 
ATOM   1966 N  NE2 . HIS A 1 280 ? 3.217   -4.060  77.937  1.00 24.33 ? 308 HIS A NE2 1 
ATOM   1967 N  N   . LEU A 1 281 ? 1.848   -4.847  73.073  1.00 20.40 ? 309 LEU A N   1 
ATOM   1968 C  CA  . LEU A 1 281 ? 2.927   -4.189  72.354  1.00 20.22 ? 309 LEU A CA  1 
ATOM   1969 C  C   . LEU A 1 281 ? 3.063   -2.780  72.900  1.00 21.67 ? 309 LEU A C   1 
ATOM   1970 O  O   . LEU A 1 281 ? 2.078   -2.031  72.929  1.00 21.29 ? 309 LEU A O   1 
ATOM   1971 C  CB  . LEU A 1 281 ? 2.636   -4.127  70.848  1.00 19.13 ? 309 LEU A CB  1 
ATOM   1972 C  CG  . LEU A 1 281 ? 2.367   -5.492  70.199  1.00 20.63 ? 309 LEU A CG  1 
ATOM   1973 C  CD1 . LEU A 1 281 ? 1.692   -5.348  68.853  1.00 19.86 ? 309 LEU A CD1 1 
ATOM   1974 C  CD2 . LEU A 1 281 ? 3.700   -6.216  70.038  1.00 18.81 ? 309 LEU A CD2 1 
ATOM   1975 N  N   . ALA A 1 282 ? 4.276   -2.405  73.294  1.00 19.53 ? 310 ALA A N   1 
ATOM   1976 C  CA  . ALA A 1 282 ? 4.546   -1.055  73.789  1.00 23.61 ? 310 ALA A CA  1 
ATOM   1977 C  C   . ALA A 1 282 ? 5.208   -0.218  72.702  1.00 23.32 ? 310 ALA A C   1 
ATOM   1978 O  O   . ALA A 1 282 ? 6.304   -0.548  72.238  1.00 22.85 ? 310 ALA A O   1 
ATOM   1979 C  CB  . ALA A 1 282 ? 5.428   -1.098  75.027  1.00 22.93 ? 310 ALA A CB  1 
ATOM   1980 N  N   . LEU A 1 283 ? 4.558   0.887   72.334  1.00 22.10 ? 311 LEU A N   1 
ATOM   1981 C  CA  . LEU A 1 283 ? 4.958   1.712   71.203  1.00 17.82 ? 311 LEU A CA  1 
ATOM   1982 C  C   . LEU A 1 283 ? 5.495   3.032   71.737  1.00 22.54 ? 311 LEU A C   1 
ATOM   1983 O  O   . LEU A 1 283 ? 4.758   3.794   72.369  1.00 21.30 ? 311 LEU A O   1 
ATOM   1984 C  CB  . LEU A 1 283 ? 3.786   1.949   70.253  1.00 20.79 ? 311 LEU A CB  1 
ATOM   1985 C  CG  . LEU A 1 283 ? 2.916   0.689   69.982  1.00 18.52 ? 311 LEU A CG  1 
ATOM   1986 C  CD1 . LEU A 1 283 ? 1.779   1.042   69.013  1.00 19.92 ? 311 LEU A CD1 1 
ATOM   1987 C  CD2 . LEU A 1 283 ? 3.728   -0.480  69.449  1.00 18.20 ? 311 LEU A CD2 1 
ATOM   1988 N  N   . MET A 1 284 ? 6.777   3.284   71.503  1.00 24.31 ? 312 MET A N   1 
ATOM   1989 C  CA  . MET A 1 284 ? 7.370   4.542   71.938  1.00 25.17 ? 312 MET A CA  1 
ATOM   1990 C  C   . MET A 1 284 ? 6.911   5.686   71.050  1.00 22.02 ? 312 MET A C   1 
ATOM   1991 O  O   . MET A 1 284 ? 6.942   5.598   69.818  1.00 23.45 ? 312 MET A O   1 
ATOM   1992 C  CB  A MET A 1 284 ? 8.898   4.439   71.936  0.56 26.44 ? 312 MET A CB  1 
ATOM   1993 C  CB  B MET A 1 284 ? 8.901   4.456   71.928  0.44 26.55 ? 312 MET A CB  1 
ATOM   1994 C  CG  A MET A 1 284 ? 9.598   5.683   72.516  0.56 28.79 ? 312 MET A CG  1 
ATOM   1995 C  CG  B MET A 1 284 ? 9.604   5.823   72.137  0.44 28.32 ? 312 MET A CG  1 
ATOM   1996 S  SD  A MET A 1 284 ? 11.370  5.405   72.705  0.56 35.86 ? 312 MET A SD  1 
ATOM   1997 S  SD  B MET A 1 284 ? 9.841   6.730   70.587  0.44 27.26 ? 312 MET A SD  1 
ATOM   1998 C  CE  A MET A 1 284 ? 11.439  4.585   74.297  0.56 30.78 ? 312 MET A CE  1 
ATOM   1999 C  CE  B MET A 1 284 ? 10.625  8.252   71.153  0.44 23.65 ? 312 MET A CE  1 
ATOM   2000 N  N   . SER A 1 285 ? 6.528   6.783   71.678  1.00 24.93 ? 313 SER A N   1 
ATOM   2001 C  CA  . SER A 1 285 ? 6.146   7.993   70.972  1.00 23.61 ? 313 SER A CA  1 
ATOM   2002 C  C   . SER A 1 285 ? 7.219   9.055   71.203  1.00 27.24 ? 313 SER A C   1 
ATOM   2003 O  O   . SER A 1 285 ? 7.778   9.138   72.300  1.00 25.41 ? 313 SER A O   1 
ATOM   2004 C  CB  . SER A 1 285 ? 4.791   8.497   71.471  1.00 22.43 ? 313 SER A CB  1 
ATOM   2005 O  OG  . SER A 1 285 ? 4.512   9.808   70.989  1.00 26.06 ? 313 SER A OG  1 
ATOM   2006 N  N   . GLU A 1 286 ? 7.506   9.853   70.165  1.00 27.35 ? 314 GLU A N   1 
ATOM   2007 C  CA  . GLU A 1 286 ? 8.351   11.044  70.311  1.00 32.75 ? 314 GLU A CA  1 
ATOM   2008 C  C   . GLU A 1 286 ? 7.653   12.173  71.056  1.00 33.62 ? 314 GLU A C   1 
ATOM   2009 O  O   . GLU A 1 286 ? 8.301   13.181  71.359  1.00 32.58 ? 314 GLU A O   1 
ATOM   2010 C  CB  . GLU A 1 286 ? 8.794   11.584  68.942  1.00 28.57 ? 314 GLU A CB  1 
ATOM   2011 C  CG  . GLU A 1 286 ? 7.603   11.930  68.063  1.00 34.53 ? 314 GLU A CG  1 
ATOM   2012 C  CD  . GLU A 1 286 ? 7.847   13.055  67.067  1.00 42.08 ? 314 GLU A CD  1 
ATOM   2013 O  OE1 . GLU A 1 286 ? 9.017   13.316  66.720  1.00 39.94 ? 314 GLU A OE1 1 
ATOM   2014 O  OE2 . GLU A 1 286 ? 6.838   13.672  66.625  1.00 43.41 ? 314 GLU A OE2 1 
ATOM   2015 N  N   . ASP A 1 287 ? 6.357   12.041  71.342  1.00 31.56 ? 315 ASP A N   1 
ATOM   2016 C  CA  . ASP A 1 287 ? 5.568   13.108  71.956  1.00 30.98 ? 315 ASP A CA  1 
ATOM   2017 C  C   . ASP A 1 287 ? 4.248   12.489  72.397  1.00 27.49 ? 315 ASP A C   1 
ATOM   2018 O  O   . ASP A 1 287 ? 3.266   12.523  71.648  1.00 26.94 ? 315 ASP A O   1 
ATOM   2019 C  CB  . ASP A 1 287 ? 5.363   14.258  70.955  1.00 30.78 ? 315 ASP A CB  1 
ATOM   2020 C  CG  . ASP A 1 287 ? 4.525   15.423  71.506  1.00 34.75 ? 315 ASP A CG  1 
ATOM   2021 O  OD1 . ASP A 1 287 ? 3.973   15.349  72.635  1.00 28.49 ? 315 ASP A OD1 1 
ATOM   2022 O  OD2 . ASP A 1 287 ? 4.433   16.439  70.765  1.00 32.90 ? 315 ASP A OD2 1 
ATOM   2023 N  N   . ILE A 1 288 ? 4.231   11.905  73.599  1.00 27.41 ? 316 ILE A N   1 
ATOM   2024 C  CA  . ILE A 1 288 ? 3.100   11.088  74.006  1.00 27.59 ? 316 ILE A CA  1 
ATOM   2025 C  C   . ILE A 1 288 ? 1.860   11.946  74.170  1.00 29.69 ? 316 ILE A C   1 
ATOM   2026 O  O   . ILE A 1 288 ? 0.736   11.462  74.000  1.00 23.79 ? 316 ILE A O   1 
ATOM   2027 C  CB  . ILE A 1 288 ? 3.430   10.300  75.289  1.00 28.81 ? 316 ILE A CB  1 
ATOM   2028 C  CG1 . ILE A 1 288 ? 2.315   9.283   75.589  1.00 25.61 ? 316 ILE A CG1 1 
ATOM   2029 C  CG2 . ILE A 1 288 ? 3.659   11.247  76.481  1.00 28.18 ? 316 ILE A CG2 1 
ATOM   2030 C  CD1 . ILE A 1 288 ? 2.675   8.229   76.635  1.00 29.57 ? 316 ILE A CD1 1 
ATOM   2031 N  N   . PHE A 1 289 ? 2.030   13.233  74.483  1.00 29.60 ? 317 PHE A N   1 
ATOM   2032 C  CA  . PHE A 1 289 ? 0.866   14.100  74.605  1.00 30.60 ? 317 PHE A CA  1 
ATOM   2033 C  C   . PHE A 1 289 ? 0.166   14.257  73.263  1.00 23.09 ? 317 PHE A C   1 
ATOM   2034 O  O   . PHE A 1 289 ? -1.064  14.170  73.183  1.00 29.27 ? 317 PHE A O   1 
ATOM   2035 C  CB  . PHE A 1 289 ? 1.282   15.466  75.172  1.00 34.10 ? 317 PHE A CB  1 
ATOM   2036 C  CG  . PHE A 1 289 ? 1.749   15.402  76.601  1.00 38.14 ? 317 PHE A CG  1 
ATOM   2037 C  CD1 . PHE A 1 289 ? 1.135   14.555  77.498  1.00 41.56 ? 317 PHE A CD1 1 
ATOM   2038 C  CD2 . PHE A 1 289 ? 2.774   16.214  77.059  1.00 47.04 ? 317 PHE A CD2 1 
ATOM   2039 C  CE1 . PHE A 1 289 ? 1.554   14.482  78.822  1.00 44.17 ? 317 PHE A CE1 1 
ATOM   2040 C  CE2 . PHE A 1 289 ? 3.191   16.148  78.389  1.00 46.76 ? 317 PHE A CE2 1 
ATOM   2041 C  CZ  . PHE A 1 289 ? 2.577   15.268  79.265  1.00 38.77 ? 317 PHE A CZ  1 
ATOM   2042 N  N   . ARG A 1 290 ? 0.932   14.496  72.196  1.00 26.04 ? 318 ARG A N   1 
ATOM   2043 C  CA  . ARG A 1 290 ? 0.310   14.613  70.885  1.00 28.19 ? 318 ARG A CA  1 
ATOM   2044 C  C   . ARG A 1 290 ? -0.276  13.276  70.446  1.00 26.63 ? 318 ARG A C   1 
ATOM   2045 O  O   . ARG A 1 290 ? -1.385  13.233  69.902  1.00 24.79 ? 318 ARG A O   1 
ATOM   2046 C  CB  . ARG A 1 290 ? 1.307   15.123  69.848  1.00 33.16 ? 318 ARG A CB  1 
ATOM   2047 C  CG  . ARG A 1 290 ? 0.924   14.736  68.428  1.00 37.70 ? 318 ARG A CG  1 
ATOM   2048 C  CD  . ARG A 1 290 ? 1.643   15.515  67.337  1.00 38.14 ? 318 ARG A CD  1 
ATOM   2049 N  NE  A ARG A 1 290 ? 1.889   14.722  66.130  0.55 37.77 ? 318 ARG A NE  1 
ATOM   2050 N  NE  B ARG A 1 290 ? 1.312   14.936  66.026  0.45 38.88 ? 318 ARG A NE  1 
ATOM   2051 C  CZ  A ARG A 1 290 ? 3.049   14.152  65.830  0.55 36.19 ? 318 ARG A CZ  1 
ATOM   2052 C  CZ  B ARG A 1 290 ? 0.236   15.256  65.306  0.45 35.52 ? 318 ARG A CZ  1 
ATOM   2053 N  NH1 A ARG A 1 290 ? 4.089   14.270  66.649  0.55 37.93 ? 318 ARG A NH1 1 
ATOM   2054 N  NH1 B ARG A 1 290 ? -0.625  16.163  65.750  0.45 36.49 ? 318 ARG A NH1 1 
ATOM   2055 N  NH2 A ARG A 1 290 ? 3.172   13.469  64.700  0.55 36.05 ? 318 ARG A NH2 1 
ATOM   2056 N  NH2 B ARG A 1 290 ? 0.023   14.675  64.132  0.45 35.03 ? 318 ARG A NH2 1 
ATOM   2057 N  N   . THR A 1 291 ? 0.434   12.174  70.701  1.00 26.52 ? 319 THR A N   1 
ATOM   2058 C  CA  . THR A 1 291 ? -0.101  10.866  70.309  1.00 23.65 ? 319 THR A CA  1 
ATOM   2059 C  C   . THR A 1 291 ? -1.446  10.603  70.974  1.00 24.40 ? 319 THR A C   1 
ATOM   2060 O  O   . THR A 1 291 ? -2.405  10.159  70.329  1.00 24.37 ? 319 THR A O   1 
ATOM   2061 C  CB  . THR A 1 291 ? 0.890   9.765   70.660  1.00 23.09 ? 319 THR A CB  1 
ATOM   2062 O  OG1 . THR A 1 291 ? 2.108   9.982   69.947  1.00 25.64 ? 319 THR A OG1 1 
ATOM   2063 C  CG2 . THR A 1 291 ? 0.293   8.377   70.257  1.00 20.94 ? 319 THR A CG2 1 
ATOM   2064 N  N   . LEU A 1 292 ? -1.537  10.860  72.275  1.00 24.26 ? 320 LEU A N   1 
ATOM   2065 C  CA  . LEU A 1 292 ? -2.779  10.573  72.974  1.00 24.35 ? 320 LEU A CA  1 
ATOM   2066 C  C   . LEU A 1 292 ? -3.892  11.534  72.566  1.00 26.56 ? 320 LEU A C   1 
ATOM   2067 O  O   . LEU A 1 292 ? -5.051  11.120  72.449  1.00 24.09 ? 320 LEU A O   1 
ATOM   2068 C  CB  . LEU A 1 292 ? -2.536  10.600  74.478  1.00 27.11 ? 320 LEU A CB  1 
ATOM   2069 C  CG  . LEU A 1 292 ? -2.346  9.212   75.094  1.00 31.56 ? 320 LEU A CG  1 
ATOM   2070 C  CD1 . LEU A 1 292 ? -3.681  8.470   75.060  1.00 33.72 ? 320 LEU A CD1 1 
ATOM   2071 C  CD2 . LEU A 1 292 ? -1.287  8.412   74.346  1.00 29.23 ? 320 LEU A CD2 1 
ATOM   2072 N  N   . ARG A 1 293 ? -3.571  12.812  72.324  1.00 24.12 ? 321 ARG A N   1 
ATOM   2073 C  CA  . ARG A 1 293 ? -4.595  13.721  71.803  1.00 25.80 ? 321 ARG A CA  1 
ATOM   2074 C  C   . ARG A 1 293 ? -5.166  13.184  70.501  1.00 25.96 ? 321 ARG A C   1 
ATOM   2075 O  O   . ARG A 1 293 ? -6.388  13.143  70.311  1.00 25.98 ? 321 ARG A O   1 
ATOM   2076 C  CB  . ARG A 1 293 ? -4.033  15.133  71.580  1.00 30.26 ? 321 ARG A CB  1 
ATOM   2077 C  CG  . ARG A 1 293 ? -3.810  15.936  72.850  1.00 34.01 ? 321 ARG A CG  1 
ATOM   2078 C  CD  . ARG A 1 293 ? -3.559  17.434  72.536  1.00 32.71 ? 321 ARG A CD  1 
ATOM   2079 N  NE  . ARG A 1 293 ? -2.449  17.649  71.599  1.00 38.07 ? 321 ARG A NE  1 
ATOM   2080 C  CZ  . ARG A 1 293 ? -1.177  17.849  71.959  1.00 37.33 ? 321 ARG A CZ  1 
ATOM   2081 N  NH1 . ARG A 1 293 ? -0.840  17.865  73.245  1.00 37.39 ? 321 ARG A NH1 1 
ATOM   2082 N  NH2 . ARG A 1 293 ? -0.238  18.041  71.035  1.00 38.13 ? 321 ARG A NH2 1 
ATOM   2083 N  N   . GLU A 1 294 ? -4.285  12.748  69.596  1.00 25.92 ? 322 GLU A N   1 
ATOM   2084 C  CA  . GLU A 1 294 ? -4.739  12.319  68.281  1.00 23.74 ? 322 GLU A CA  1 
ATOM   2085 C  C   . GLU A 1 294 ? -5.485  10.992  68.369  1.00 24.37 ? 322 GLU A C   1 
ATOM   2086 O  O   . GLU A 1 294 ? -6.545  10.834  67.753  1.00 20.30 ? 322 GLU A O   1 
ATOM   2087 C  CB  . GLU A 1 294 ? -3.557  12.224  67.314  1.00 26.66 ? 322 GLU A CB  1 
ATOM   2088 C  CG  . GLU A 1 294 ? -2.904  13.576  66.952  1.00 29.61 ? 322 GLU A CG  1 
ATOM   2089 C  CD  . GLU A 1 294 ? -3.905  14.625  66.468  1.00 32.56 ? 322 GLU A CD  1 
ATOM   2090 O  OE1 . GLU A 1 294 ? -4.793  14.300  65.654  1.00 32.06 ? 322 GLU A OE1 1 
ATOM   2091 O  OE2 . GLU A 1 294 ? -3.798  15.793  66.910  1.00 37.45 ? 322 GLU A OE2 1 
ATOM   2092 N  N   . MET A 1 295 ? -4.969  10.036  69.149  1.00 21.85 ? 323 MET A N   1 
ATOM   2093 C  CA  . MET A 1 295 ? -5.679  8.760   69.270  1.00 24.95 ? 323 MET A CA  1 
ATOM   2094 C  C   . MET A 1 295 ? -7.034  8.942   69.947  1.00 24.43 ? 323 MET A C   1 
ATOM   2095 O  O   . MET A 1 295 ? -8.035  8.329   69.540  1.00 21.20 ? 323 MET A O   1 
ATOM   2096 C  CB  . MET A 1 295 ? -4.821  7.747   70.037  1.00 20.99 ? 323 MET A CB  1 
ATOM   2097 C  CG  . MET A 1 295 ? -3.606  7.289   69.262  1.00 23.66 ? 323 MET A CG  1 
ATOM   2098 S  SD  . MET A 1 295 ? -2.695  5.933   70.058  1.00 20.45 ? 323 MET A SD  1 
ATOM   2099 C  CE  . MET A 1 295 ? -3.849  4.546   69.820  1.00 17.53 ? 323 MET A CE  1 
ATOM   2100 N  N   . ARG A 1 296 ? -7.098  9.795   70.976  1.00 25.18 ? 324 ARG A N   1 
ATOM   2101 C  CA  . ARG A 1 296 ? -8.355  9.941   71.702  1.00 27.50 ? 324 ARG A CA  1 
ATOM   2102 C  C   . ARG A 1 296 ? -9.419  10.645  70.866  1.00 25.19 ? 324 ARG A C   1 
ATOM   2103 O  O   . ARG A 1 296 ? -10.608 10.317  70.985  1.00 22.66 ? 324 ARG A O   1 
ATOM   2104 C  CB  . ARG A 1 296 ? -8.123  10.673  73.018  1.00 31.41 ? 324 ARG A CB  1 
ATOM   2105 C  CG  . ARG A 1 296 ? -7.591  9.791   74.132  1.00 26.70 ? 324 ARG A CG  1 
ATOM   2106 C  CD  . ARG A 1 296 ? -7.743  10.545  75.425  1.00 30.87 ? 324 ARG A CD  1 
ATOM   2107 N  NE  . ARG A 1 296 ? -7.314  9.803   76.602  1.00 32.49 ? 324 ARG A NE  1 
ATOM   2108 C  CZ  . ARG A 1 296 ? -8.032  8.870   77.216  1.00 30.02 ? 324 ARG A CZ  1 
ATOM   2109 N  NH1 . ARG A 1 296 ? -9.225  8.523   76.761  1.00 30.61 ? 324 ARG A NH1 1 
ATOM   2110 N  NH2 . ARG A 1 296 ? -7.548  8.285   78.298  1.00 33.16 ? 324 ARG A NH2 1 
ATOM   2111 N  N   . LYS A 1 297 ? -9.017  11.570  69.987  1.00 25.93 ? 325 LYS A N   1 
ATOM   2112 C  CA  . LYS A 1 297 ? -9.982  12.179  69.076  1.00 25.89 ? 325 LYS A CA  1 
ATOM   2113 C  C   . LYS A 1 297 ? -10.666 11.134  68.205  1.00 23.63 ? 325 LYS A C   1 
ATOM   2114 O  O   . LYS A 1 297 ? -11.798 11.344  67.742  1.00 24.41 ? 325 LYS A O   1 
ATOM   2115 C  CB  . LYS A 1 297 ? -9.295  13.201  68.176  1.00 27.69 ? 325 LYS A CB  1 
ATOM   2116 C  CG  . LYS A 1 297 ? -8.784  14.420  68.891  1.00 36.05 ? 325 LYS A CG  1 
ATOM   2117 C  CD  . LYS A 1 297 ? -8.834  15.624  67.984  1.00 42.55 ? 325 LYS A CD  1 
ATOM   2118 C  CE  . LYS A 1 297 ? -7.638  15.679  67.070  1.00 42.64 ? 325 LYS A CE  1 
ATOM   2119 N  NZ  . LYS A 1 297 ? -6.847  16.920  67.317  1.00 41.34 ? 325 LYS A NZ  1 
ATOM   2120 N  N   . ARG A 1 298 ? -10.001 10.001  67.981  1.00 27.01 ? 326 ARG A N   1 
ATOM   2121 C  CA  . ARG A 1 298 ? -10.478 9.016   67.031  1.00 24.18 ? 326 ARG A CA  1 
ATOM   2122 C  C   . ARG A 1 298 ? -11.066 7.779   67.683  1.00 22.90 ? 326 ARG A C   1 
ATOM   2123 O  O   . ARG A 1 298 ? -11.554 6.906   66.964  1.00 22.24 ? 326 ARG A O   1 
ATOM   2124 C  CB  . ARG A 1 298 ? -9.345  8.622   66.084  1.00 24.86 ? 326 ARG A CB  1 
ATOM   2125 C  CG  . ARG A 1 298 ? -8.865  9.818   65.273  1.00 25.51 ? 326 ARG A CG  1 
ATOM   2126 C  CD  . ARG A 1 298 ? -7.554  9.537   64.631  1.00 22.92 ? 326 ARG A CD  1 
ATOM   2127 N  NE  . ARG A 1 298 ? -7.155  10.547  63.648  1.00 27.05 ? 326 ARG A NE  1 
ATOM   2128 C  CZ  . ARG A 1 298 ? -6.613  11.726  63.940  1.00 26.14 ? 326 ARG A CZ  1 
ATOM   2129 N  NH1 . ARG A 1 298 ? -6.455  12.104  65.205  1.00 25.26 ? 326 ARG A NH1 1 
ATOM   2130 N  NH2 . ARG A 1 298 ? -6.260  12.547  62.956  1.00 27.43 ? 326 ARG A NH2 1 
ATOM   2131 N  N   . SER A 1 299 ? -11.085 7.706   69.016  1.00 22.35 ? 327 SER A N   1 
ATOM   2132 C  CA  . SER A 1 299 ? -11.554 6.505   69.698  1.00 20.87 ? 327 SER A CA  1 
ATOM   2133 C  C   . SER A 1 299 ? -12.945 6.089   69.235  1.00 26.80 ? 327 SER A C   1 
ATOM   2134 O  O   . SER A 1 299 ? -13.187 4.913   68.940  1.00 28.91 ? 327 SER A O   1 
ATOM   2135 C  CB  . SER A 1 299 ? -11.551 6.736   71.206  1.00 25.71 ? 327 SER A CB  1 
ATOM   2136 O  OG  . SER A 1 299 ? -10.221 6.872   71.676  1.00 22.25 ? 327 SER A OG  1 
ATOM   2137 N  N   . SER A 1 300 ? -13.868 7.039   69.151  1.00 26.32 ? 328 SER A N   1 
ATOM   2138 C  CA  . SER A 1 300 ? -15.253 6.707   68.845  1.00 30.43 ? 328 SER A CA  1 
ATOM   2139 C  C   . SER A 1 300 ? -15.591 6.830   67.367  1.00 24.85 ? 328 SER A C   1 
ATOM   2140 O  O   . SER A 1 300 ? -16.757 6.628   66.992  1.00 27.34 ? 328 SER A O   1 
ATOM   2141 C  CB  . SER A 1 300 ? -16.181 7.584   69.682  1.00 37.14 ? 328 SER A CB  1 
ATOM   2142 O  OG  . SER A 1 300 ? -16.042 7.238   71.052  1.00 40.52 ? 328 SER A OG  1 
ATOM   2143 N  N   . ILE A 1 301 ? -14.606 7.121   66.522  1.00 20.90 ? 329 ILE A N   1 
ATOM   2144 C  CA  . ILE A 1 301 ? -14.813 7.150   65.078  1.00 21.70 ? 329 ILE A CA  1 
ATOM   2145 C  C   . ILE A 1 301 ? -13.842 6.204   64.372  1.00 21.05 ? 329 ILE A C   1 
ATOM   2146 O  O   . ILE A 1 301 ? -13.277 6.539   63.322  1.00 18.33 ? 329 ILE A O   1 
ATOM   2147 C  CB  . ILE A 1 301 ? -14.701 8.585   64.532  1.00 22.94 ? 329 ILE A CB  1 
ATOM   2148 C  CG1 . ILE A 1 301 ? -13.347 9.205   64.914  1.00 22.15 ? 329 ILE A CG1 1 
ATOM   2149 C  CG2 . ILE A 1 301 ? -15.897 9.429   65.025  1.00 22.66 ? 329 ILE A CG2 1 
ATOM   2150 C  CD1 . ILE A 1 301 ? -13.096 10.615  64.285  1.00 23.39 ? 329 ILE A CD1 1 
ATOM   2151 N  N   . GLY A 1 302 ? -13.693 4.987   64.905  1.00 21.92 ? 330 GLY A N   1 
ATOM   2152 C  CA  . GLY A 1 302 ? -12.945 3.942   64.231  1.00 19.96 ? 330 GLY A CA  1 
ATOM   2153 C  C   . GLY A 1 302 ? -11.615 3.577   64.863  1.00 21.84 ? 330 GLY A C   1 
ATOM   2154 O  O   . GLY A 1 302 ? -11.038 2.529   64.505  1.00 19.10 ? 330 GLY A O   1 
ATOM   2155 N  N   . GLY A 1 303 ? -11.113 4.378   65.790  1.00 19.45 ? 331 GLY A N   1 
ATOM   2156 C  CA  . GLY A 1 303 ? -9.798  4.160   66.375  1.00 17.87 ? 331 GLY A CA  1 
ATOM   2157 C  C   . GLY A 1 303 ? -9.857  3.251   67.584  1.00 23.68 ? 331 GLY A C   1 
ATOM   2158 O  O   . GLY A 1 303 ? -10.659 2.303   67.651  1.00 22.99 ? 331 GLY A O   1 
ATOM   2159 N  N   . PHE A 1 304 ? -8.996  3.535   68.554  1.00 18.02 ? 332 PHE A N   1 
ATOM   2160 C  CA  . PHE A 1 304 ? -8.826  2.682   69.721  1.00 20.81 ? 332 PHE A CA  1 
ATOM   2161 C  C   . PHE A 1 304 ? -9.324  3.384   70.970  1.00 22.63 ? 332 PHE A C   1 
ATOM   2162 O  O   . PHE A 1 304 ? -9.142  4.592   71.120  1.00 23.47 ? 332 PHE A O   1 
ATOM   2163 C  CB  . PHE A 1 304 ? -7.352  2.283   69.899  1.00 16.84 ? 332 PHE A CB  1 
ATOM   2164 C  CG  . PHE A 1 304 ? -6.850  1.399   68.785  1.00 22.03 ? 332 PHE A CG  1 
ATOM   2165 C  CD1 . PHE A 1 304 ? -7.087  0.022   68.823  1.00 23.59 ? 332 PHE A CD1 1 
ATOM   2166 C  CD2 . PHE A 1 304 ? -6.215  1.946   67.675  1.00 21.57 ? 332 PHE A CD2 1 
ATOM   2167 C  CE1 . PHE A 1 304 ? -6.652  -0.806  67.797  1.00 20.76 ? 332 PHE A CE1 1 
ATOM   2168 C  CE2 . PHE A 1 304 ? -5.759  1.119   66.631  1.00 19.69 ? 332 PHE A CE2 1 
ATOM   2169 C  CZ  . PHE A 1 304 ? -5.997  -0.255  66.689  1.00 17.36 ? 332 PHE A CZ  1 
ATOM   2170 N  N   . ASP A 1 305 ? -9.934  2.619   71.861  1.00 24.47 ? 333 ASP A N   1 
ATOM   2171 C  CA  . ASP A 1 305 ? -10.342 3.112   73.166  1.00 26.65 ? 333 ASP A CA  1 
ATOM   2172 C  C   . ASP A 1 305 ? -9.204  2.925   74.146  1.00 27.67 ? 333 ASP A C   1 
ATOM   2173 O  O   . ASP A 1 305 ? -8.306  2.112   73.932  1.00 26.56 ? 333 ASP A O   1 
ATOM   2174 C  CB  . ASP A 1 305 ? -11.571 2.368   73.692  1.00 25.21 ? 333 ASP A CB  1 
ATOM   2175 C  CG  . ASP A 1 305 ? -12.766 2.487   72.777  1.00 26.84 ? 333 ASP A CG  1 
ATOM   2176 O  OD1 . ASP A 1 305 ? -12.846 3.459   72.012  1.00 29.42 ? 333 ASP A OD1 1 
ATOM   2177 O  OD2 . ASP A 1 305 ? -13.631 1.600   72.822  1.00 32.13 ? 333 ASP A OD2 1 
ATOM   2178 N  N   . PHE A 1 306 ? -9.267  3.663   75.247  1.00 25.45 ? 334 PHE A N   1 
ATOM   2179 C  CA  . PHE A 1 306 ? -8.254  3.559   76.280  1.00 27.88 ? 334 PHE A CA  1 
ATOM   2180 C  C   . PHE A 1 306 ? -8.897  3.046   77.560  1.00 29.54 ? 334 PHE A C   1 
ATOM   2181 O  O   . PHE A 1 306 ? -10.100 3.221   77.782  1.00 27.87 ? 334 PHE A O   1 
ATOM   2182 C  CB  . PHE A 1 306 ? -7.547  4.914   76.487  1.00 27.96 ? 334 PHE A CB  1 
ATOM   2183 C  CG  . PHE A 1 306 ? -6.654  5.283   75.342  1.00 25.29 ? 334 PHE A CG  1 
ATOM   2184 C  CD1 . PHE A 1 306 ? -5.345  4.807   75.288  1.00 22.96 ? 334 PHE A CD1 1 
ATOM   2185 C  CD2 . PHE A 1 306 ? -7.135  6.036   74.283  1.00 26.87 ? 334 PHE A CD2 1 
ATOM   2186 C  CE1 . PHE A 1 306 ? -4.525  5.094   74.217  1.00 23.54 ? 334 PHE A CE1 1 
ATOM   2187 C  CE2 . PHE A 1 306 ? -6.310  6.352   73.206  1.00 27.50 ? 334 PHE A CE2 1 
ATOM   2188 C  CZ  . PHE A 1 306 ? -4.997  5.874   73.177  1.00 23.00 ? 334 PHE A CZ  1 
ATOM   2189 N  N   . MET A 1 307 ? -8.096  2.358   78.376  1.00 26.48 ? 335 MET A N   1 
ATOM   2190 C  CA  . MET A 1 307 ? -8.595  1.850   79.645  1.00 31.87 ? 335 MET A CA  1 
ATOM   2191 C  C   . MET A 1 307 ? -9.054  3.013   80.531  1.00 32.88 ? 335 MET A C   1 
ATOM   2192 O  O   . MET A 1 307 ? -8.663  4.162   80.314  1.00 32.59 ? 335 MET A O   1 
ATOM   2193 C  CB  . MET A 1 307 ? -7.519  1.017   80.343  1.00 30.59 ? 335 MET A CB  1 
ATOM   2194 C  CG  . MET A 1 307 ? -7.330  -0.349  79.705  1.00 31.75 ? 335 MET A CG  1 
ATOM   2195 S  SD  . MET A 1 307 ? -5.993  -1.271  80.478  1.00 41.39 ? 335 MET A SD  1 
ATOM   2196 C  CE  . MET A 1 307 ? -5.899  -2.749  79.453  1.00 38.68 ? 335 MET A CE  1 
ATOM   2197 N  N   . PRO A 1 308 ? -9.925  2.739   81.504  1.00 36.60 ? 336 PRO A N   1 
ATOM   2198 C  CA  . PRO A 1 308 ? -10.434 3.820   82.360  1.00 39.62 ? 336 PRO A CA  1 
ATOM   2199 C  C   . PRO A 1 308 ? -9.312  4.602   83.034  1.00 39.39 ? 336 PRO A C   1 
ATOM   2200 O  O   . PRO A 1 308 ? -8.339  4.032   83.534  1.00 40.39 ? 336 PRO A O   1 
ATOM   2201 C  CB  . PRO A 1 308 ? -11.315 3.085   83.382  1.00 38.93 ? 336 PRO A CB  1 
ATOM   2202 C  CG  . PRO A 1 308 ? -11.159 1.625   83.109  1.00 43.57 ? 336 PRO A CG  1 
ATOM   2203 C  CD  . PRO A 1 308 ? -10.664 1.483   81.707  1.00 40.17 ? 336 PRO A CD  1 
ATOM   2204 N  N   . SER A 1 309 ? -9.454  5.927   83.023  1.00 39.95 ? 337 SER A N   1 
ATOM   2205 C  CA  . SER A 1 309 ? -8.429  6.813   83.545  1.00 40.19 ? 337 SER A CA  1 
ATOM   2206 C  C   . SER A 1 309 ? -8.362  6.716   85.067  1.00 43.96 ? 337 SER A C   1 
ATOM   2207 O  O   . SER A 1 309 ? -9.330  6.316   85.717  1.00 43.91 ? 337 SER A O   1 
ATOM   2208 C  CB  . SER A 1 309 ? -8.713  8.252   83.128  1.00 40.66 ? 337 SER A CB  1 
ATOM   2209 O  OG  . SER A 1 309 ? -8.666  8.397   81.722  1.00 38.56 ? 337 SER A OG  1 
ATOM   2210 N  N   . PRO A 1 310 ? -7.224  7.059   85.663  1.00 43.51 ? 338 PRO A N   1 
ATOM   2211 C  CA  . PRO A 1 310 ? -7.140  7.058   87.125  1.00 46.93 ? 338 PRO A CA  1 
ATOM   2212 C  C   . PRO A 1 310 ? -7.936  8.214   87.707  1.00 49.07 ? 338 PRO A C   1 
ATOM   2213 O  O   . PRO A 1 310 ? -8.251  9.183   86.998  1.00 47.89 ? 338 PRO A O   1 
ATOM   2214 C  CB  . PRO A 1 310 ? -5.636  7.203   87.401  1.00 43.64 ? 338 PRO A CB  1 
ATOM   2215 C  CG  . PRO A 1 310 ? -5.061  7.776   86.173  1.00 44.51 ? 338 PRO A CG  1 
ATOM   2216 C  CD  . PRO A 1 310 ? -5.929  7.358   85.026  1.00 42.24 ? 338 PRO A CD  1 
ATOM   2217 N  N   . PRO A 1 311 ? -8.315  8.135   88.980  1.00 53.70 ? 339 PRO A N   1 
ATOM   2218 C  CA  . PRO A 1 311 ? -9.043  9.241   89.612  1.00 53.65 ? 339 PRO A CA  1 
ATOM   2219 C  C   . PRO A 1 311 ? -8.132  10.439  89.815  1.00 52.95 ? 339 PRO A C   1 
ATOM   2220 O  O   . PRO A 1 311 ? -6.901  10.317  89.697  1.00 47.89 ? 339 PRO A O   1 
ATOM   2221 C  CB  . PRO A 1 311 ? -9.497  8.639   90.951  1.00 56.03 ? 339 PRO A CB  1 
ATOM   2222 C  CG  . PRO A 1 311 ? -8.490  7.583   91.241  1.00 58.28 ? 339 PRO A CG  1 
ATOM   2223 C  CD  . PRO A 1 311 ? -8.109  7.008   89.905  1.00 55.78 ? 339 PRO A CD  1 
ATOM   2224 N  N   . PRO A 1 312 ? -8.692  11.620  90.103  1.00 52.33 ? 340 PRO A N   1 
ATOM   2225 C  CA  . PRO A 1 312 ? -7.837  12.808  90.274  1.00 50.01 ? 340 PRO A CA  1 
ATOM   2226 C  C   . PRO A 1 312 ? -6.840  12.673  91.400  1.00 49.19 ? 340 PRO A C   1 
ATOM   2227 O  O   . PRO A 1 312 ? -5.802  13.344  91.367  1.00 50.84 ? 340 PRO A O   1 
ATOM   2228 C  CB  . PRO A 1 312 ? -8.844  13.934  90.547  1.00 52.88 ? 340 PRO A CB  1 
ATOM   2229 C  CG  . PRO A 1 312 ? -10.069 13.236  91.022  1.00 53.49 ? 340 PRO A CG  1 
ATOM   2230 C  CD  . PRO A 1 312 ? -10.118 11.946  90.277  1.00 54.27 ? 340 PRO A CD  1 
ATOM   2231 N  N   . THR A 1 313 ? -7.118  11.824  92.391  1.00 53.83 ? 341 THR A N   1 
ATOM   2232 C  CA  . THR A 1 313 ? -6.149  11.586  93.455  1.00 56.68 ? 341 THR A CA  1 
ATOM   2233 C  C   . THR A 1 313 ? -4.821  11.097  92.892  1.00 55.35 ? 341 THR A C   1 
ATOM   2234 O  O   . THR A 1 313 ? -3.754  11.468  93.395  1.00 53.36 ? 341 THR A O   1 
ATOM   2235 C  CB  . THR A 1 313 ? -6.707  10.578  94.458  1.00 58.03 ? 341 THR A CB  1 
ATOM   2236 O  OG1 . THR A 1 313 ? -7.087  9.385   93.767  1.00 60.02 ? 341 THR A OG1 1 
ATOM   2237 C  CG2 . THR A 1 313 ? -7.920  11.156  95.171  1.00 59.17 ? 341 THR A CG2 1 
ATOM   2238 N  N   . TYR A 1 314 ? -4.866  10.267  91.844  1.00 53.53 ? 342 TYR A N   1 
ATOM   2239 C  CA  . TYR A 1 314 ? -3.634  9.806   91.212  1.00 48.75 ? 342 TYR A CA  1 
ATOM   2240 C  C   . TYR A 1 314 ? -2.799  10.982  90.726  1.00 50.78 ? 342 TYR A C   1 
ATOM   2241 O  O   . TYR A 1 314 ? -1.570  10.984  90.867  1.00 47.10 ? 342 TYR A O   1 
ATOM   2242 C  CB  . TYR A 1 314 ? -3.956  8.861   90.049  1.00 47.81 ? 342 TYR A CB  1 
ATOM   2243 C  CG  . TYR A 1 314 ? -2.733  8.335   89.324  1.00 46.04 ? 342 TYR A CG  1 
ATOM   2244 C  CD1 . TYR A 1 314 ? -2.157  7.114   89.672  1.00 47.68 ? 342 TYR A CD1 1 
ATOM   2245 C  CD2 . TYR A 1 314 ? -2.141  9.070   88.302  1.00 43.85 ? 342 TYR A CD2 1 
ATOM   2246 C  CE1 . TYR A 1 314 ? -1.026  6.635   89.008  1.00 44.23 ? 342 TYR A CE1 1 
ATOM   2247 C  CE2 . TYR A 1 314 ? -1.018  8.609   87.643  1.00 41.05 ? 342 TYR A CE2 1 
ATOM   2248 C  CZ  . TYR A 1 314 ? -0.466  7.392   87.995  1.00 41.26 ? 342 TYR A CZ  1 
ATOM   2249 O  OH  . TYR A 1 314 ? 0.651   6.944   87.325  1.00 37.80 ? 342 TYR A OH  1 
ATOM   2250 N  N   . TYR A 1 315 ? -3.445  11.993  90.145  1.00 45.74 ? 343 TYR A N   1 
ATOM   2251 C  CA  . TYR A 1 315 ? -2.686  13.126  89.638  1.00 47.81 ? 343 TYR A CA  1 
ATOM   2252 C  C   . TYR A 1 315 ? -2.322  14.101  90.748  1.00 49.46 ? 343 TYR A C   1 
ATOM   2253 O  O   . TYR A 1 315 ? -1.271  14.750  90.671  1.00 51.38 ? 343 TYR A O   1 
ATOM   2254 C  CB  . TYR A 1 315 ? -3.465  13.797  88.504  1.00 49.91 ? 343 TYR A CB  1 
ATOM   2255 C  CG  . TYR A 1 315 ? -3.593  12.841  87.345  1.00 47.03 ? 343 TYR A CG  1 
ATOM   2256 C  CD1 . TYR A 1 315 ? -4.762  12.129  87.126  1.00 46.57 ? 343 TYR A CD1 1 
ATOM   2257 C  CD2 . TYR A 1 315 ? -2.508  12.598  86.512  1.00 46.04 ? 343 TYR A CD2 1 
ATOM   2258 C  CE1 . TYR A 1 315 ? -4.856  11.225  86.081  1.00 43.25 ? 343 TYR A CE1 1 
ATOM   2259 C  CE2 . TYR A 1 315 ? -2.585  11.692  85.471  1.00 43.54 ? 343 TYR A CE2 1 
ATOM   2260 C  CZ  . TYR A 1 315 ? -3.764  11.013  85.256  1.00 42.59 ? 343 TYR A CZ  1 
ATOM   2261 O  OH  . TYR A 1 315 ? -3.838  10.102  84.217  1.00 43.01 ? 343 TYR A OH  1 
ATOM   2262 N  N   . GLN A 1 316 ? -3.151  14.196  91.792  1.00 53.21 ? 344 GLN A N   1 
ATOM   2263 C  CA  . GLN A 1 316 ? -2.745  14.931  92.985  1.00 52.51 ? 344 GLN A CA  1 
ATOM   2264 C  C   . GLN A 1 316 ? -1.471  14.347  93.583  1.00 55.30 ? 344 GLN A C   1 
ATOM   2265 O  O   . GLN A 1 316 ? -0.607  15.095  94.059  1.00 54.30 ? 344 GLN A O   1 
ATOM   2266 C  CB  . GLN A 1 316 ? -3.871  14.924  94.019  1.00 56.03 ? 344 GLN A CB  1 
ATOM   2267 N  N   . ASN A 1 317 ? -1.324  13.022  93.545  1.00 51.68 ? 345 ASN A N   1 
ATOM   2268 C  CA  . ASN A 1 317 ? -0.141  12.364  94.089  1.00 49.49 ? 345 ASN A CA  1 
ATOM   2269 C  C   . ASN A 1 317 ? 1.059   12.418  93.153  1.00 49.94 ? 345 ASN A C   1 
ATOM   2270 O  O   . ASN A 1 317 ? 2.156   12.024  93.560  1.00 46.61 ? 345 ASN A O   1 
ATOM   2271 C  CB  . ASN A 1 317 ? -0.462  10.906  94.432  1.00 50.93 ? 345 ASN A CB  1 
ATOM   2272 C  CG  . ASN A 1 317 ? -1.584  10.781  95.444  1.00 54.56 ? 345 ASN A CG  1 
ATOM   2273 O  OD1 . ASN A 1 317 ? -1.955  11.757  96.096  1.00 55.37 ? 345 ASN A OD1 1 
ATOM   2274 N  ND2 . ASN A 1 317 ? -2.132  9.576   95.581  1.00 54.00 ? 345 ASN A ND2 1 
ATOM   2275 N  N   . LEU A 1 318 ? 0.886   12.905  91.922  1.00 49.68 ? 346 LEU A N   1 
ATOM   2276 C  CA  . LEU A 1 318 ? 1.999   12.933  90.977  1.00 49.79 ? 346 LEU A CA  1 
ATOM   2277 C  C   . LEU A 1 318 ? 3.040   13.974  91.361  1.00 50.35 ? 346 LEU A C   1 
ATOM   2278 O  O   . LEU A 1 318 ? 4.240   13.760  91.146  1.00 49.07 ? 346 LEU A O   1 
ATOM   2279 C  CB  . LEU A 1 318 ? 1.490   13.201  89.561  1.00 49.13 ? 346 LEU A CB  1 
ATOM   2280 C  CG  . LEU A 1 318 ? 1.156   11.962  88.732  1.00 47.64 ? 346 LEU A CG  1 
ATOM   2281 C  CD1 . LEU A 1 318 ? 0.756   12.378  87.335  1.00 47.36 ? 346 LEU A CD1 1 
ATOM   2282 C  CD2 . LEU A 1 318 ? 2.350   11.026  88.695  1.00 45.67 ? 346 LEU A CD2 1 
ATOM   2283 N  N   . LYS A 1 319 ? 2.604   15.113  91.906  1.00 47.51 ? 347 LYS A N   1 
ATOM   2284 C  CA  . LYS A 1 319 ? 3.551   16.174  92.244  1.00 51.42 ? 347 LYS A CA  1 
ATOM   2285 C  C   . LYS A 1 319 ? 4.640   15.661  93.179  1.00 48.64 ? 347 LYS A C   1 
ATOM   2286 O  O   . LYS A 1 319 ? 5.828   15.919  92.957  1.00 50.43 ? 347 LYS A O   1 
ATOM   2287 C  CB  . LYS A 1 319 ? 2.818   17.365  92.869  1.00 48.45 ? 347 LYS A CB  1 
ATOM   2288 N  N   . LYS A 1 320 ? 4.255   14.898  94.206  1.00 49.17 ? 348 LYS A N   1 
ATOM   2289 C  CA  . LYS A 1 320 ? 5.206   14.380  95.183  1.00 48.04 ? 348 LYS A CA  1 
ATOM   2290 C  C   . LYS A 1 320 ? 6.143   13.328  94.605  1.00 54.56 ? 348 LYS A C   1 
ATOM   2291 O  O   . LYS A 1 320 ? 7.176   13.041  95.223  1.00 50.36 ? 348 LYS A O   1 
ATOM   2292 C  CB  . LYS A 1 320 ? 4.463   13.784  96.382  1.00 47.49 ? 348 LYS A CB  1 
ATOM   2293 N  N   . ARG A 1 321 ? 5.818   12.743  93.451  1.00 50.77 ? 349 ARG A N   1 
ATOM   2294 C  CA  . ARG A 1 321 ? 6.613   11.652  92.908  1.00 50.20 ? 349 ARG A CA  1 
ATOM   2295 C  C   . ARG A 1 321 ? 7.460   12.040  91.711  1.00 50.91 ? 349 ARG A C   1 
ATOM   2296 O  O   . ARG A 1 321 ? 8.518   11.440  91.508  1.00 51.55 ? 349 ARG A O   1 
ATOM   2297 C  CB  . ARG A 1 321 ? 5.706   10.489  92.499  1.00 50.84 ? 349 ARG A CB  1 
ATOM   2298 C  CG  . ARG A 1 321 ? 4.757   10.052  93.577  1.00 50.48 ? 349 ARG A CG  1 
ATOM   2299 C  CD  . ARG A 1 321 ? 3.634   9.276   92.957  1.00 57.16 ? 349 ARG A CD  1 
ATOM   2300 N  NE  . ARG A 1 321 ? 4.166   8.360   91.956  1.00 53.86 ? 349 ARG A NE  1 
ATOM   2301 C  CZ  . ARG A 1 321 ? 3.525   7.999   90.852  1.00 52.08 ? 349 ARG A CZ  1 
ATOM   2302 N  NH1 . ARG A 1 321 ? 2.306   8.454   90.605  1.00 52.54 ? 349 ARG A NH1 1 
ATOM   2303 N  NH2 . ARG A 1 321 ? 4.102   7.167   89.998  1.00 46.59 ? 349 ARG A NH2 1 
ATOM   2304 N  N   . VAL A 1 322 ? 7.021   13.005  90.903  1.00 46.27 ? 350 VAL A N   1 
ATOM   2305 C  CA  . VAL A 1 322 ? 7.732   13.343  89.674  1.00 46.08 ? 350 VAL A CA  1 
ATOM   2306 C  C   . VAL A 1 322 ? 7.752   14.853  89.464  1.00 48.98 ? 350 VAL A C   1 
ATOM   2307 O  O   . VAL A 1 322 ? 8.064   15.329  88.364  1.00 47.80 ? 350 VAL A O   1 
ATOM   2308 C  CB  . VAL A 1 322 ? 7.103   12.635  88.456  1.00 48.35 ? 350 VAL A CB  1 
ATOM   2309 C  CG1 . VAL A 1 322 ? 7.248   11.107  88.563  1.00 41.76 ? 350 VAL A CG1 1 
ATOM   2310 C  CG2 . VAL A 1 322 ? 5.644   13.048  88.293  1.00 48.09 ? 350 VAL A CG2 1 
ATOM   2311 N  N   . GLY A 1 323 ? 7.437   15.617  90.516  1.00 51.25 ? 351 GLY A N   1 
ATOM   2312 C  CA  . GLY A 1 323 ? 7.400   17.070  90.408  1.00 50.21 ? 351 GLY A CA  1 
ATOM   2313 C  C   . GLY A 1 323 ? 8.711   17.700  89.978  1.00 48.16 ? 351 GLY A C   1 
ATOM   2314 O  O   . GLY A 1 323 ? 8.721   18.854  89.543  1.00 50.96 ? 351 GLY A O   1 
ATOM   2315 N  N   . ASP A 1 324 ? 9.816   16.970  90.093  1.00 50.78 ? 352 ASP A N   1 
ATOM   2316 C  CA  . ASP A 1 324 ? 11.117  17.409  89.607  1.00 55.64 ? 352 ASP A CA  1 
ATOM   2317 C  C   . ASP A 1 324 ? 11.356  17.063  88.143  1.00 57.29 ? 352 ASP A C   1 
ATOM   2318 O  O   . ASP A 1 324 ? 12.315  17.574  87.551  1.00 54.39 ? 352 ASP A O   1 
ATOM   2319 C  CB  . ASP A 1 324 ? 12.220  16.777  90.452  1.00 53.87 ? 352 ASP A CB  1 
ATOM   2320 C  CG  . ASP A 1 324 ? 12.151  15.267  90.443  1.00 54.72 ? 352 ASP A CG  1 
ATOM   2321 O  OD1 . ASP A 1 324 ? 13.214  14.622  90.349  1.00 60.74 ? 352 ASP A OD1 1 
ATOM   2322 O  OD2 . ASP A 1 324 ? 11.024  14.725  90.517  1.00 55.53 ? 352 ASP A OD2 1 
ATOM   2323 N  N   . VAL A 1 325 ? 10.528  16.201  87.558  1.00 52.92 ? 353 VAL A N   1 
ATOM   2324 C  CA  . VAL A 1 325 ? 10.655  15.818  86.160  1.00 49.50 ? 353 VAL A CA  1 
ATOM   2325 C  C   . VAL A 1 325 ? 9.633   16.532  85.289  1.00 45.40 ? 353 VAL A C   1 
ATOM   2326 O  O   . VAL A 1 325 ? 9.945   16.941  84.171  1.00 50.99 ? 353 VAL A O   1 
ATOM   2327 C  CB  . VAL A 1 325 ? 10.533  14.286  86.012  1.00 50.80 ? 353 VAL A CB  1 
ATOM   2328 C  CG1 . VAL A 1 325 ? 10.876  13.853  84.585  1.00 46.60 ? 353 VAL A CG1 1 
ATOM   2329 C  CG2 . VAL A 1 325 ? 11.419  13.588  87.024  1.00 52.13 ? 353 VAL A CG2 1 
ATOM   2330 N  N   . LEU A 1 326 ? 8.414   16.695  85.791  1.00 46.87 ? 354 LEU A N   1 
ATOM   2331 C  CA  . LEU A 1 326 ? 7.314   17.261  85.025  1.00 48.40 ? 354 LEU A CA  1 
ATOM   2332 C  C   . LEU A 1 326 ? 6.797   18.519  85.704  1.00 46.50 ? 354 LEU A C   1 
ATOM   2333 O  O   . LEU A 1 326 ? 6.606   18.548  86.924  1.00 46.18 ? 354 LEU A O   1 
ATOM   2334 C  CB  . LEU A 1 326 ? 6.164   16.259  84.875  1.00 46.52 ? 354 LEU A CB  1 
ATOM   2335 C  CG  . LEU A 1 326 ? 6.497   14.862  84.338  1.00 46.07 ? 354 LEU A CG  1 
ATOM   2336 C  CD1 . LEU A 1 326 ? 5.248   13.987  84.325  1.00 42.39 ? 354 LEU A CD1 1 
ATOM   2337 C  CD2 . LEU A 1 326 ? 7.115   14.960  82.954  1.00 45.29 ? 354 LEU A CD2 1 
ATOM   2338 N  N   . SER A 1 327 ? 6.556   19.550  84.905  1.00 45.76 ? 355 SER A N   1 
ATOM   2339 C  CA  . SER A 1 327 ? 5.968   20.768  85.429  1.00 47.45 ? 355 SER A CA  1 
ATOM   2340 C  C   . SER A 1 327 ? 4.511   20.527  85.829  1.00 48.84 ? 355 SER A C   1 
ATOM   2341 O  O   . SER A 1 327 ? 3.911   19.492  85.524  1.00 45.67 ? 355 SER A O   1 
ATOM   2342 C  CB  . SER A 1 327 ? 6.060   21.887  84.394  1.00 47.23 ? 355 SER A CB  1 
ATOM   2343 O  OG  . SER A 1 327 ? 5.136   21.685  83.342  1.00 50.47 ? 355 SER A OG  1 
ATOM   2344 N  N   . ASP A 1 328 ? 3.943   21.507  86.536  1.00 47.33 ? 356 ASP A N   1 
ATOM   2345 C  CA  . ASP A 1 328 ? 2.523   21.454  86.861  1.00 46.10 ? 356 ASP A CA  1 
ATOM   2346 C  C   . ASP A 1 328 ? 1.679   21.357  85.599  1.00 48.59 ? 356 ASP A C   1 
ATOM   2347 O  O   . ASP A 1 328 ? 0.702   20.597  85.551  1.00 47.26 ? 356 ASP A O   1 
ATOM   2348 C  CB  . ASP A 1 328 ? 2.112   22.689  87.670  1.00 46.37 ? 356 ASP A CB  1 
ATOM   2349 C  CG  . ASP A 1 328 ? 2.565   22.624  89.119  1.00 51.72 ? 356 ASP A CG  1 
ATOM   2350 O  OD1 . ASP A 1 328 ? 2.934   21.527  89.586  1.00 55.22 ? 356 ASP A OD1 1 
ATOM   2351 O  OD2 . ASP A 1 328 ? 2.536   23.675  89.801  1.00 56.69 ? 356 ASP A OD2 1 
ATOM   2352 N  N   . ASP A 1 329 ? 2.033   22.133  84.570  1.00 44.56 ? 357 ASP A N   1 
ATOM   2353 C  CA  . ASP A 1 329 ? 1.294   22.077  83.312  1.00 49.09 ? 357 ASP A CA  1 
ATOM   2354 C  C   . ASP A 1 329 ? 1.424   20.704  82.663  1.00 48.37 ? 357 ASP A C   1 
ATOM   2355 O  O   . ASP A 1 329 ? 0.446   20.161  82.135  1.00 46.28 ? 357 ASP A O   1 
ATOM   2356 C  CB  . ASP A 1 329 ? 1.798   23.163  82.361  1.00 49.62 ? 357 ASP A CB  1 
ATOM   2357 C  CG  . ASP A 1 329 ? 1.415   24.558  82.816  1.00 59.93 ? 357 ASP A CG  1 
ATOM   2358 O  OD1 . ASP A 1 329 ? 0.308   24.730  83.375  1.00 61.33 ? 357 ASP A OD1 1 
ATOM   2359 O  OD2 . ASP A 1 329 ? 2.224   25.487  82.614  1.00 64.66 ? 357 ASP A OD2 1 
ATOM   2360 N  N   . GLN A 1 330 ? 2.634   20.136  82.689  1.00 46.15 ? 358 GLN A N   1 
ATOM   2361 C  CA  . GLN A 1 330 ? 2.866   18.817  82.110  1.00 47.93 ? 358 GLN A CA  1 
ATOM   2362 C  C   . GLN A 1 330 ? 2.177   17.722  82.914  1.00 44.52 ? 358 GLN A C   1 
ATOM   2363 O  O   . GLN A 1 330 ? 1.721   16.724  82.341  1.00 44.17 ? 358 GLN A O   1 
ATOM   2364 C  CB  . GLN A 1 330 ? 4.376   18.572  81.993  1.00 43.85 ? 358 GLN A CB  1 
ATOM   2365 C  CG  . GLN A 1 330 ? 4.997   19.382  80.866  1.00 44.83 ? 358 GLN A CG  1 
ATOM   2366 C  CD  . GLN A 1 330 ? 6.437   19.802  81.119  1.00 49.90 ? 358 GLN A CD  1 
ATOM   2367 O  OE1 . GLN A 1 330 ? 7.114   19.271  82.006  1.00 47.00 ? 358 GLN A OE1 1 
ATOM   2368 N  NE2 . GLN A 1 330 ? 6.915   20.764  80.328  1.00 44.47 ? 358 GLN A NE2 1 
ATOM   2369 N  N   . ILE A 1 331 ? 2.084   17.892  84.234  1.00 44.07 ? 359 ILE A N   1 
ATOM   2370 C  CA  . ILE A 1 331 ? 1.304   16.969  85.049  1.00 40.27 ? 359 ILE A CA  1 
ATOM   2371 C  C   . ILE A 1 331 ? -0.182  17.140  84.770  1.00 44.78 ? 359 ILE A C   1 
ATOM   2372 O  O   . ILE A 1 331 ? -0.920  16.156  84.656  1.00 44.67 ? 359 ILE A O   1 
ATOM   2373 C  CB  . ILE A 1 331 ? 1.634   17.159  86.542  1.00 43.74 ? 359 ILE A CB  1 
ATOM   2374 C  CG1 . ILE A 1 331 ? 3.068   16.702  86.835  1.00 44.48 ? 359 ILE A CG1 1 
ATOM   2375 C  CG2 . ILE A 1 331 ? 0.636   16.415  87.424  1.00 45.76 ? 359 ILE A CG2 1 
ATOM   2376 C  CD1 . ILE A 1 331 ? 3.518   16.943  88.275  1.00 45.94 ? 359 ILE A CD1 1 
ATOM   2377 N  N   . LYS A 1 332 ? -0.650  18.387  84.648  1.00 41.97 ? 360 LYS A N   1 
ATOM   2378 C  CA  . LYS A 1 332 ? -2.057  18.599  84.315  1.00 41.62 ? 360 LYS A CA  1 
ATOM   2379 C  C   . LYS A 1 332 ? -2.380  18.066  82.924  1.00 43.25 ? 360 LYS A C   1 
ATOM   2380 O  O   . LYS A 1 332 ? -3.503  17.614  82.674  1.00 43.12 ? 360 LYS A O   1 
ATOM   2381 C  CB  . LYS A 1 332 ? -2.411  20.086  84.416  1.00 47.80 ? 360 LYS A CB  1 
ATOM   2382 N  N   . GLU A 1 333 ? -1.409  18.105  82.009  1.00 44.14 ? 361 GLU A N   1 
ATOM   2383 C  CA  . GLU A 1 333 ? -1.624  17.547  80.676  1.00 45.16 ? 361 GLU A CA  1 
ATOM   2384 C  C   . GLU A 1 333 ? -1.754  16.026  80.731  1.00 43.11 ? 361 GLU A C   1 
ATOM   2385 O  O   . GLU A 1 333 ? -2.593  15.443  80.031  1.00 39.22 ? 361 GLU A O   1 
ATOM   2386 C  CB  . GLU A 1 333 ? -0.484  17.977  79.758  1.00 45.21 ? 361 GLU A CB  1 
ATOM   2387 C  CG  . GLU A 1 333 ? -0.795  17.922  78.283  1.00 47.38 ? 361 GLU A CG  1 
ATOM   2388 C  CD  . GLU A 1 333 ? 0.207   18.723  77.484  1.00 50.71 ? 361 GLU A CD  1 
ATOM   2389 O  OE1 . GLU A 1 333 ? 0.166   18.671  76.236  1.00 51.92 ? 361 GLU A OE1 1 
ATOM   2390 O  OE2 . GLU A 1 333 ? 1.041   19.414  78.114  1.00 54.55 ? 361 GLU A OE2 1 
ATOM   2391 N  N   . CYS A 1 334 ? -0.944  15.371  81.572  1.00 37.04 ? 362 CYS A N   1 
ATOM   2392 C  CA  . CYS A 1 334 ? -1.150  13.948  81.850  1.00 38.55 ? 362 CYS A CA  1 
ATOM   2393 C  C   . CYS A 1 334 ? -2.569  13.683  82.335  1.00 40.29 ? 362 CYS A C   1 
ATOM   2394 O  O   . CYS A 1 334 ? -3.215  12.720  81.902  1.00 38.00 ? 362 CYS A O   1 
ATOM   2395 C  CB  . CYS A 1 334 ? -0.148  13.449  82.896  1.00 33.68 ? 362 CYS A CB  1 
ATOM   2396 S  SG  . CYS A 1 334 ? 1.553   13.333  82.318  1.00 41.15 ? 362 CYS A SG  1 
ATOM   2397 N  N   . GLU A 1 335 ? -3.075  14.526  83.238  1.00 40.20 ? 363 GLU A N   1 
ATOM   2398 C  CA  . GLU A 1 335 ? -4.404  14.280  83.791  1.00 39.04 ? 363 GLU A CA  1 
ATOM   2399 C  C   . GLU A 1 335 ? -5.480  14.378  82.720  1.00 38.04 ? 363 GLU A C   1 
ATOM   2400 O  O   . GLU A 1 335 ? -6.430  13.587  82.714  1.00 40.75 ? 363 GLU A O   1 
ATOM   2401 C  CB  . GLU A 1 335 ? -4.706  15.257  84.931  1.00 43.99 ? 363 GLU A CB  1 
ATOM   2402 C  CG  . GLU A 1 335 ? -6.049  14.980  85.609  1.00 44.11 ? 363 GLU A CG  1 
ATOM   2403 C  CD  . GLU A 1 335 ? -6.305  15.869  86.810  1.00 52.33 ? 363 GLU A CD  1 
ATOM   2404 O  OE1 . GLU A 1 335 ? -7.006  15.420  87.749  1.00 48.74 ? 363 GLU A OE1 1 
ATOM   2405 O  OE2 . GLU A 1 335 ? -5.795  17.010  86.813  1.00 50.05 ? 363 GLU A OE2 1 
ATOM   2406 N  N   . GLU A 1 336 ? -5.362  15.347  81.811  1.00 38.12 ? 364 GLU A N   1 
ATOM   2407 C  CA  . GLU A 1 336 ? -6.370  15.479  80.762  1.00 39.85 ? 364 GLU A CA  1 
ATOM   2408 C  C   . GLU A 1 336 ? -6.440  14.219  79.908  1.00 39.98 ? 364 GLU A C   1 
ATOM   2409 O  O   . GLU A 1 336 ? -7.522  13.807  79.478  1.00 40.05 ? 364 GLU A O   1 
ATOM   2410 C  CB  . GLU A 1 336 ? -6.063  16.684  79.877  1.00 44.42 ? 364 GLU A CB  1 
ATOM   2411 C  CG  . GLU A 1 336 ? -6.063  18.019  80.580  1.00 50.21 ? 364 GLU A CG  1 
ATOM   2412 C  CD  . GLU A 1 336 ? -5.375  19.081  79.748  1.00 56.96 ? 364 GLU A CD  1 
ATOM   2413 O  OE1 . GLU A 1 336 ? -4.897  18.744  78.642  1.00 55.63 ? 364 GLU A OE1 1 
ATOM   2414 O  OE2 . GLU A 1 336 ? -5.322  20.250  80.190  1.00 61.54 ? 364 GLU A OE2 1 
ATOM   2415 N  N   . LEU A 1 337 ? -5.297  13.579  79.685  1.00 41.14 ? 365 LEU A N   1 
ATOM   2416 C  CA  . LEU A 1 337 ? -5.174  12.481  78.735  1.00 34.24 ? 365 LEU A CA  1 
ATOM   2417 C  C   . LEU A 1 337 ? -5.219  11.104  79.383  1.00 37.39 ? 365 LEU A C   1 
ATOM   2418 O  O   . LEU A 1 337 ? -5.186  10.100  78.664  1.00 34.44 ? 365 LEU A O   1 
ATOM   2419 C  CB  . LEU A 1 337 ? -3.872  12.642  77.948  1.00 34.56 ? 365 LEU A CB  1 
ATOM   2420 C  CG  . LEU A 1 337 ? -3.809  13.952  77.172  1.00 36.97 ? 365 LEU A CG  1 
ATOM   2421 C  CD1 . LEU A 1 337 ? -2.417  14.148  76.602  1.00 37.58 ? 365 LEU A CD1 1 
ATOM   2422 C  CD2 . LEU A 1 337 ? -4.881  13.974  76.071  1.00 34.27 ? 365 LEU A CD2 1 
ATOM   2423 N  N   . GLY A 1 338 ? -5.309  11.029  80.710  1.00 34.45 ? 366 GLY A N   1 
ATOM   2424 C  CA  . GLY A 1 338 ? -5.284  9.758   81.403  1.00 31.87 ? 366 GLY A CA  1 
ATOM   2425 C  C   . GLY A 1 338 ? -3.928  9.085   81.470  1.00 35.28 ? 366 GLY A C   1 
ATOM   2426 O  O   . GLY A 1 338 ? -3.858  7.890   81.773  1.00 35.09 ? 366 GLY A O   1 
ATOM   2427 N  N   . ILE A 1 339 ? -2.844  9.820   81.209  1.00 31.11 ? 367 ILE A N   1 
ATOM   2428 C  CA  . ILE A 1 339 ? -1.511  9.224   81.180  1.00 27.59 ? 367 ILE A CA  1 
ATOM   2429 C  C   . ILE A 1 339 ? -1.067  8.848   82.587  1.00 35.33 ? 367 ILE A C   1 
ATOM   2430 O  O   . ILE A 1 339 ? -1.292  9.594   83.554  1.00 34.08 ? 367 ILE A O   1 
ATOM   2431 C  CB  . ILE A 1 339 ? -0.526  10.193  80.513  1.00 29.55 ? 367 ILE A CB  1 
ATOM   2432 C  CG1 . ILE A 1 339 ? -0.976  10.477  79.076  1.00 33.90 ? 367 ILE A CG1 1 
ATOM   2433 C  CG2 . ILE A 1 339 ? 0.929   9.680   80.578  1.00 29.29 ? 367 ILE A CG2 1 
ATOM   2434 C  CD1 . ILE A 1 339 ? -0.079  11.427  78.328  1.00 37.75 ? 367 ILE A CD1 1 
ATOM   2435 N  N   . LEU A 1 340 ? -0.428  7.678   82.700  1.00 30.72 ? 368 LEU A N   1 
ATOM   2436 C  CA  . LEU A 1 340 ? 0.197   7.186   83.919  1.00 35.87 ? 368 LEU A CA  1 
ATOM   2437 C  C   . LEU A 1 340 ? 1.681   7.521   83.915  1.00 32.57 ? 368 LEU A C   1 
ATOM   2438 O  O   . LEU A 1 340 ? 2.312   7.612   82.861  1.00 32.07 ? 368 LEU A O   1 
ATOM   2439 C  CB  . LEU A 1 340 ? 0.037   5.664   84.043  1.00 33.80 ? 368 LEU A CB  1 
ATOM   2440 C  CG  . LEU A 1 340 ? -1.332  5.075   83.689  1.00 37.05 ? 368 LEU A CG  1 
ATOM   2441 C  CD1 . LEU A 1 340 ? -1.282  3.558   83.641  1.00 36.66 ? 368 LEU A CD1 1 
ATOM   2442 C  CD2 . LEU A 1 340 ? -2.367  5.527   84.694  1.00 39.70 ? 368 LEU A CD2 1 
ATOM   2443 N  N   . VAL A 1 341 ? 2.244   7.675   85.111  1.00 36.22 ? 369 VAL A N   1 
ATOM   2444 C  CA  . VAL A 1 341 ? 3.657   7.998   85.278  1.00 34.52 ? 369 VAL A CA  1 
ATOM   2445 C  C   . VAL A 1 341 ? 4.260   7.046   86.302  1.00 31.96 ? 369 VAL A C   1 
ATOM   2446 O  O   . VAL A 1 341 ? 3.704   6.868   87.390  1.00 34.30 ? 369 VAL A O   1 
ATOM   2447 C  CB  . VAL A 1 341 ? 3.868   9.461   85.727  1.00 36.78 ? 369 VAL A CB  1 
ATOM   2448 C  CG1 . VAL A 1 341 ? 5.350   9.821   85.649  1.00 34.46 ? 369 VAL A CG1 1 
ATOM   2449 C  CG2 . VAL A 1 341 ? 3.040   10.426  84.882  1.00 38.53 ? 369 VAL A CG2 1 
ATOM   2450 N  N   . ASP A 1 342 ? 5.395   6.433   85.959  1.00 34.09 ? 370 ASP A N   1 
ATOM   2451 C  CA  . ASP A 1 342 ? 6.185   5.689   86.928  1.00 37.83 ? 370 ASP A CA  1 
ATOM   2452 C  C   . ASP A 1 342 ? 7.636   6.132   86.823  1.00 39.66 ? 370 ASP A C   1 
ATOM   2453 O  O   . ASP A 1 342 ? 8.038   6.833   85.890  1.00 36.95 ? 370 ASP A O   1 
ATOM   2454 C  CB  . ASP A 1 342 ? 6.089   4.168   86.728  1.00 38.41 ? 370 ASP A CB  1 
ATOM   2455 C  CG  . ASP A 1 342 ? 6.356   3.388   88.018  1.00 43.52 ? 370 ASP A CG  1 
ATOM   2456 O  OD1 . ASP A 1 342 ? 6.292   3.994   89.109  1.00 43.20 ? 370 ASP A OD1 1 
ATOM   2457 O  OD2 . ASP A 1 342 ? 6.631   2.169   87.942  1.00 40.88 ? 370 ASP A OD2 1 
ATOM   2458 N  N   . ARG A 1 343 ? 8.419   5.744   87.801  1.00 41.25 ? 371 ARG A N   1 
ATOM   2459 C  CA  . ARG A 1 343 ? 9.798   6.139   87.847  1.00 41.69 ? 371 ARG A CA  1 
ATOM   2460 C  C   . ARG A 1 343 ? 10.640  5.082   88.524  1.00 46.26 ? 371 ARG A C   1 
ATOM   2461 O  O   . ARG A 1 343 ? 10.193  4.400   89.417  1.00 46.89 ? 371 ARG A O   1 
ATOM   2462 C  CB  . ARG A 1 343 ? 9.885   7.431   88.626  1.00 45.80 ? 371 ARG A CB  1 
ATOM   2463 C  CG  . ARG A 1 343 ? 11.238  8.079   88.716  1.00 50.18 ? 371 ARG A CG  1 
ATOM   2464 C  CD  . ARG A 1 343 ? 11.196  9.221   89.685  1.00 53.36 ? 371 ARG A CD  1 
ATOM   2465 N  NE  . ARG A 1 343 ? 12.320  10.089  89.448  1.00 58.51 ? 371 ARG A NE  1 
ATOM   2466 C  CZ  . ARG A 1 343 ? 12.370  11.346  89.814  1.00 58.12 ? 371 ARG A CZ  1 
ATOM   2467 N  NH1 . ARG A 1 343 ? 11.353  11.892  90.446  1.00 54.35 ? 371 ARG A NH1 1 
ATOM   2468 N  NH2 . ARG A 1 343 ? 13.440  12.041  89.536  1.00 61.55 ? 371 ARG A NH2 1 
ATOM   2469 N  N   . ASP A 1 344 ? 11.855  4.980   88.038  1.00 47.78 ? 372 ASP A N   1 
ATOM   2470 C  CA  . ASP A 1 344 ? 12.893  4.114   88.487  1.00 50.82 ? 372 ASP A CA  1 
ATOM   2471 C  C   . ASP A 1 344 ? 13.893  4.891   89.268  1.00 52.97 ? 372 ASP A C   1 
ATOM   2472 O  O   . ASP A 1 344 ? 13.702  6.015   89.610  1.00 52.08 ? 372 ASP A O   1 
ATOM   2473 C  CB  . ASP A 1 344 ? 13.679  3.698   87.256  1.00 49.15 ? 372 ASP A CB  1 
ATOM   2474 C  CG  . ASP A 1 344 ? 13.695  2.281   87.066  1.00 51.08 ? 372 ASP A CG  1 
ATOM   2475 O  OD1 . ASP A 1 344 ? 13.161  1.578   87.905  1.00 58.75 ? 372 ASP A OD1 1 
ATOM   2476 O  OD2 . ASP A 1 344 ? 14.231  1.848   86.054  1.00 57.69 ? 372 ASP A OD2 1 
ATOM   2477 N  N   . ASP A 1 345 ? 15.035  4.257   89.447  1.00 58.19 ? 373 ASP A N   1 
ATOM   2478 C  CA  . ASP A 1 345 ? 16.188  4.860   90.071  1.00 59.29 ? 373 ASP A CA  1 
ATOM   2479 C  C   . ASP A 1 345 ? 16.961  5.613   88.993  1.00 60.62 ? 373 ASP A C   1 
ATOM   2480 O  O   . ASP A 1 345 ? 17.733  6.475   89.291  1.00 64.58 ? 373 ASP A O   1 
ATOM   2481 C  CB  . ASP A 1 345 ? 17.093  3.787   90.665  1.00 59.47 ? 373 ASP A CB  1 
ATOM   2482 C  CG  . ASP A 1 345 ? 17.623  2.835   89.629  1.00 62.56 ? 373 ASP A CG  1 
ATOM   2483 O  OD1 . ASP A 1 345 ? 16.910  1.932   89.175  1.00 62.56 ? 373 ASP A OD1 1 
ATOM   2484 O  OD2 . ASP A 1 345 ? 18.747  3.037   89.193  1.00 68.73 ? 373 ASP A OD2 1 
ATOM   2485 N  N   . GLN A 1 346 ? 16.715  5.288   87.738  1.00 58.09 ? 374 GLN A N   1 
ATOM   2486 C  CA  . GLN A 1 346 ? 17.374  5.846   86.618  1.00 55.87 ? 374 GLN A CA  1 
ATOM   2487 C  C   . GLN A 1 346 ? 16.557  6.863   85.884  1.00 54.50 ? 374 GLN A C   1 
ATOM   2488 O  O   . GLN A 1 346 ? 17.075  7.920   85.561  1.00 55.89 ? 374 GLN A O   1 
ATOM   2489 C  CB  . GLN A 1 346 ? 17.682  4.704   85.658  1.00 57.26 ? 374 GLN A CB  1 
ATOM   2490 N  N   . GLY A 1 347 ? 15.298  6.552   85.609  1.00 46.24 ? 375 GLY A N   1 
ATOM   2491 C  CA  . GLY A 1 347 ? 14.473  7.435   84.802  1.00 44.56 ? 375 GLY A CA  1 
ATOM   2492 C  C   . GLY A 1 347 ? 12.992  7.454   85.033  1.00 41.26 ? 375 GLY A C   1 
ATOM   2493 O  O   . GLY A 1 347 ? 12.530  6.858   85.964  1.00 38.86 ? 375 GLY A O   1 
ATOM   2494 N  N   . THR A 1 348 ? 12.255  8.114   84.146  1.00 37.68 ? 376 THR A N   1 
ATOM   2495 C  CA  . THR A 1 348 ? 10.813  8.283   84.313  1.00 36.67 ? 376 THR A CA  1 
ATOM   2496 C  C   . THR A 1 348 ? 10.077  7.750   83.086  1.00 36.72 ? 376 THR A C   1 
ATOM   2497 O  O   . THR A 1 348 ? 10.544  7.909   81.955  1.00 36.35 ? 376 THR A O   1 
ATOM   2498 C  CB  . THR A 1 348 ? 10.454  9.780   84.539  1.00 40.98 ? 376 THR A CB  1 
ATOM   2499 O  OG1 . THR A 1 348 ? 11.091  10.256  85.733  1.00 42.89 ? 376 THR A OG1 1 
ATOM   2500 C  CG2 . THR A 1 348 ? 8.946   9.992   84.667  1.00 35.81 ? 376 THR A CG2 1 
ATOM   2501 N  N   . LEU A 1 349 ? 8.921   7.124   83.317  1.00 32.60 ? 377 LEU A N   1 
ATOM   2502 C  CA  . LEU A 1 349 ? 8.116   6.511   82.269  1.00 33.53 ? 377 LEU A CA  1 
ATOM   2503 C  C   . LEU A 1 349 ? 6.729   7.141   82.247  1.00 33.57 ? 377 LEU A C   1 
ATOM   2504 O  O   . LEU A 1 349 ? 6.050   7.191   83.276  1.00 33.00 ? 377 LEU A O   1 
ATOM   2505 C  CB  . LEU A 1 349 ? 8.012   4.996   82.497  1.00 33.58 ? 377 LEU A CB  1 
ATOM   2506 C  CG  . LEU A 1 349 ? 6.918   4.216   81.765  1.00 33.59 ? 377 LEU A CG  1 
ATOM   2507 C  CD1 . LEU A 1 349 ? 7.342   4.054   80.313  1.00 37.19 ? 377 LEU A CD1 1 
ATOM   2508 C  CD2 . LEU A 1 349 ? 6.715   2.846   82.397  1.00 40.36 ? 377 LEU A CD2 1 
ATOM   2509 N  N   . LEU A 1 350 ? 6.319   7.631   81.083  1.00 30.25 ? 378 LEU A N   1 
ATOM   2510 C  CA  . LEU A 1 350 ? 4.927   7.978   80.825  1.00 27.87 ? 378 LEU A CA  1 
ATOM   2511 C  C   . LEU A 1 350 ? 4.306   6.847   80.004  1.00 26.04 ? 378 LEU A C   1 
ATOM   2512 O  O   . LEU A 1 350 ? 4.911   6.398   79.025  1.00 25.73 ? 378 LEU A O   1 
ATOM   2513 C  CB  . LEU A 1 350 ? 4.818   9.301   80.068  1.00 29.05 ? 378 LEU A CB  1 
ATOM   2514 C  CG  . LEU A 1 350 ? 5.615   10.492  80.614  1.00 36.54 ? 378 LEU A CG  1 
ATOM   2515 C  CD1 . LEU A 1 350 ? 5.580   11.649  79.625  1.00 37.04 ? 378 LEU A CD1 1 
ATOM   2516 C  CD2 . LEU A 1 350 ? 5.065   10.921  81.955  1.00 41.92 ? 378 LEU A CD2 1 
ATOM   2517 N  N   . GLN A 1 351 ? 3.111   6.399   80.386  1.00 29.20 ? 379 GLN A N   1 
ATOM   2518 C  CA  . GLN A 1 351 ? 2.511   5.238   79.729  1.00 25.79 ? 379 GLN A CA  1 
ATOM   2519 C  C   . GLN A 1 351 ? 0.990   5.312   79.796  1.00 26.96 ? 379 GLN A C   1 
ATOM   2520 O  O   . GLN A 1 351 ? 0.410   5.924   80.695  1.00 27.65 ? 379 GLN A O   1 
ATOM   2521 C  CB  . GLN A 1 351 ? 2.983   3.921   80.363  1.00 24.36 ? 379 GLN A CB  1 
ATOM   2522 C  CG  . GLN A 1 351 ? 2.758   3.879   81.871  1.00 30.18 ? 379 GLN A CG  1 
ATOM   2523 C  CD  . GLN A 1 351 ? 3.061   2.536   82.529  1.00 32.77 ? 379 GLN A CD  1 
ATOM   2524 O  OE1 . GLN A 1 351 ? 2.884   2.388   83.739  1.00 33.00 ? 379 GLN A OE1 1 
ATOM   2525 N  NE2 . GLN A 1 351 ? 3.488   1.545   81.737  1.00 29.56 ? 379 GLN A NE2 1 
ATOM   2526 N  N   . ILE A 1 352 ? 0.342   4.609   78.868  1.00 24.35 ? 380 ILE A N   1 
ATOM   2527 C  CA  . ILE A 1 352 ? -1.106  4.468   78.898  1.00 21.25 ? 380 ILE A CA  1 
ATOM   2528 C  C   . ILE A 1 352 ? -1.457  3.264   78.037  1.00 24.91 ? 380 ILE A C   1 
ATOM   2529 O  O   . ILE A 1 352 ? -0.703  2.886   77.144  1.00 24.98 ? 380 ILE A O   1 
ATOM   2530 C  CB  . ILE A 1 352 ? -1.805  5.763   78.411  1.00 26.91 ? 380 ILE A CB  1 
ATOM   2531 C  CG1 . ILE A 1 352 ? -3.299  5.740   78.768  1.00 26.21 ? 380 ILE A CG1 1 
ATOM   2532 C  CG2 . ILE A 1 352 ? -1.550  5.976   76.904  1.00 26.47 ? 380 ILE A CG2 1 
ATOM   2533 C  CD1 . ILE A 1 352 ? -4.058  7.018   78.349  1.00 25.29 ? 380 ILE A CD1 1 
ATOM   2534 N  N   . PHE A 1 353 ? -2.618  2.671   78.298  1.00 22.28 ? 381 PHE A N   1 
ATOM   2535 C  CA  . PHE A 1 353 ? -2.986  1.374   77.738  1.00 23.26 ? 381 PHE A CA  1 
ATOM   2536 C  C   . PHE A 1 353 ? -4.310  1.463   76.997  1.00 24.89 ? 381 PHE A C   1 
ATOM   2537 O  O   . PHE A 1 353 ? -5.266  2.069   77.498  1.00 25.04 ? 381 PHE A O   1 
ATOM   2538 C  CB  . PHE A 1 353 ? -3.065  0.335   78.844  1.00 26.49 ? 381 PHE A CB  1 
ATOM   2539 C  CG  . PHE A 1 353 ? -1.755  0.093   79.516  1.00 25.96 ? 381 PHE A CG  1 
ATOM   2540 C  CD1 . PHE A 1 353 ? -1.358  0.859   80.595  1.00 27.93 ? 381 PHE A CD1 1 
ATOM   2541 C  CD2 . PHE A 1 353 ? -0.913  -0.908  79.058  1.00 28.68 ? 381 PHE A CD2 1 
ATOM   2542 C  CE1 . PHE A 1 353 ? -0.136  0.626   81.214  1.00 30.23 ? 381 PHE A CE1 1 
ATOM   2543 C  CE2 . PHE A 1 353 ? 0.325   -1.140  79.671  1.00 27.34 ? 381 PHE A CE2 1 
ATOM   2544 C  CZ  . PHE A 1 353 ? 0.702   -0.376  80.745  1.00 29.37 ? 381 PHE A CZ  1 
ATOM   2545 N  N   . THR A 1 354 ? -4.364  0.868   75.803  1.00 21.86 ? 382 THR A N   1 
ATOM   2546 C  CA  . THR A 1 354 ? -5.641  0.782   75.115  1.00 21.28 ? 382 THR A CA  1 
ATOM   2547 C  C   . THR A 1 354 ? -6.489  -0.323  75.723  1.00 22.70 ? 382 THR A C   1 
ATOM   2548 O  O   . THR A 1 354 ? -5.996  -1.222  76.404  1.00 23.98 ? 382 THR A O   1 
ATOM   2549 C  CB  . THR A 1 354 ? -5.471  0.498   73.615  1.00 17.60 ? 382 THR A CB  1 
ATOM   2550 O  OG1 . THR A 1 354 ? -5.089  -0.875  73.433  1.00 21.57 ? 382 THR A OG1 1 
ATOM   2551 C  CG2 . THR A 1 354 ? -4.408  1.427   72.990  1.00 21.02 ? 382 THR A CG2 1 
ATOM   2552 N  N   . LYS A 1 355 ? -7.786  -0.261  75.445  1.00 23.47 ? 383 LYS A N   1 
ATOM   2553 C  CA  . LYS A 1 355 ? -8.614  -1.429  75.632  1.00 20.98 ? 383 LYS A CA  1 
ATOM   2554 C  C   . LYS A 1 355 ? -8.192  -2.488  74.614  1.00 21.78 ? 383 LYS A C   1 
ATOM   2555 O  O   . LYS A 1 355 ? -7.439  -2.196  73.675  1.00 20.29 ? 383 LYS A O   1 
ATOM   2556 C  CB  . LYS A 1 355 ? -10.087 -1.051  75.479  1.00 22.15 ? 383 LYS A CB  1 
ATOM   2557 C  CG  . LYS A 1 355 ? -10.614 -0.254  76.666  1.00 26.51 ? 383 LYS A CG  1 
ATOM   2558 C  CD  . LYS A 1 355 ? -12.124 -0.078  76.591  1.00 26.49 ? 383 LYS A CD  1 
ATOM   2559 C  CE  . LYS A 1 355 ? -12.641 0.629   77.829  1.00 33.21 ? 383 LYS A CE  1 
ATOM   2560 N  NZ  . LYS A 1 355 ? -14.141 0.726   77.786  1.00 40.94 ? 383 LYS A NZ  1 
ATOM   2561 N  N   . PRO A 1 356 ? -8.674  -3.726  74.755  1.00 22.05 ? 384 PRO A N   1 
ATOM   2562 C  CA  . PRO A 1 356 ? -8.247  -4.777  73.822  1.00 19.59 ? 384 PRO A CA  1 
ATOM   2563 C  C   . PRO A 1 356 ? -8.480  -4.359  72.377  1.00 20.91 ? 384 PRO A C   1 
ATOM   2564 O  O   . PRO A 1 356 ? -9.459  -3.677  72.055  1.00 20.88 ? 384 PRO A O   1 
ATOM   2565 C  CB  . PRO A 1 356 ? -9.115  -5.972  74.224  1.00 23.36 ? 384 PRO A CB  1 
ATOM   2566 C  CG  . PRO A 1 356 ? -9.244  -5.793  75.725  1.00 25.54 ? 384 PRO A CG  1 
ATOM   2567 C  CD  . PRO A 1 356 ? -9.447  -4.286  75.885  1.00 23.09 ? 384 PRO A CD  1 
ATOM   2568 N  N   . LEU A 1 357 ? -7.566  -4.787  71.508  1.00 18.64 ? 385 LEU A N   1 
ATOM   2569 C  CA  . LEU A 1 357 ? -7.586  -4.374  70.112  1.00 20.59 ? 385 LEU A CA  1 
ATOM   2570 C  C   . LEU A 1 357 ? -8.716  -5.034  69.328  1.00 19.99 ? 385 LEU A C   1 
ATOM   2571 O  O   . LEU A 1 357 ? -9.075  -4.546  68.254  1.00 19.40 ? 385 LEU A O   1 
ATOM   2572 C  CB  . LEU A 1 357 ? -6.257  -4.715  69.450  1.00 21.38 ? 385 LEU A CB  1 
ATOM   2573 C  CG  . LEU A 1 357 ? -4.991  -4.311  70.208  1.00 18.25 ? 385 LEU A CG  1 
ATOM   2574 C  CD1 . LEU A 1 357 ? -3.784  -4.654  69.367  1.00 18.53 ? 385 LEU A CD1 1 
ATOM   2575 C  CD2 . LEU A 1 357 ? -5.006  -2.790  70.561  1.00 19.97 ? 385 LEU A CD2 1 
ATOM   2576 N  N   . GLY A 1 358 ? -9.231  -6.160  69.799  1.00 19.44 ? 386 GLY A N   1 
ATOM   2577 C  CA  . GLY A 1 358 ? -10.250 -6.867  69.045  1.00 20.62 ? 386 GLY A CA  1 
ATOM   2578 C  C   . GLY A 1 358 ? -11.346 -7.401  69.939  1.00 20.98 ? 386 GLY A C   1 
ATOM   2579 O  O   . GLY A 1 358 ? -11.550 -6.886  71.043  1.00 22.55 ? 386 GLY A O   1 
ATOM   2580 N  N   . ASP A 1 359 ? -12.055 -8.439  69.465  1.00 20.39 ? 387 ASP A N   1 
ATOM   2581 C  CA  . ASP A 1 359 ? -13.215 -8.959  70.190  1.00 21.64 ? 387 ASP A CA  1 
ATOM   2582 C  C   . ASP A 1 359 ? -12.835 -9.509  71.558  1.00 20.57 ? 387 ASP A C   1 
ATOM   2583 O  O   . ASP A 1 359 ? -13.587 -9.347  72.529  1.00 21.35 ? 387 ASP A O   1 
ATOM   2584 C  CB  . ASP A 1 359 ? -13.901 -10.073 69.388  1.00 21.33 ? 387 ASP A CB  1 
ATOM   2585 C  CG  . ASP A 1 359 ? -14.571 -9.573  68.131  1.00 22.67 ? 387 ASP A CG  1 
ATOM   2586 O  OD1 . ASP A 1 359 ? -14.922 -8.365  68.060  1.00 21.13 ? 387 ASP A OD1 1 
ATOM   2587 O  OD2 . ASP A 1 359 ? -14.726 -10.396 67.204  1.00 23.15 ? 387 ASP A OD2 1 
ATOM   2588 N  N   . ARG A 1 360 ? -11.669 -10.203 71.645  1.00 19.80 ? 388 ARG A N   1 
ATOM   2589 C  CA  . ARG A 1 360 ? -11.368 -10.896 72.887  1.00 23.00 ? 388 ARG A CA  1 
ATOM   2590 C  C   . ARG A 1 360 ? -10.548 -10.015 73.813  1.00 21.86 ? 388 ARG A C   1 
ATOM   2591 O  O   . ARG A 1 360 ? -9.769  -9.171  73.353  1.00 22.77 ? 388 ARG A O   1 
ATOM   2592 C  CB  . ARG A 1 360 ? -10.603 -12.178 72.615  1.00 19.46 ? 388 ARG A CB  1 
ATOM   2593 C  CG  . ARG A 1 360 ? -11.231 -13.064 71.542  1.00 22.15 ? 388 ARG A CG  1 
ATOM   2594 C  CD  . ARG A 1 360 ? -10.474 -14.384 71.502  1.00 22.32 ? 388 ARG A CD  1 
ATOM   2595 N  NE  . ARG A 1 360 ? -10.949 -15.278 70.449  1.00 22.79 ? 388 ARG A NE  1 
ATOM   2596 C  CZ  . ARG A 1 360 ? -10.608 -16.561 70.363  1.00 24.61 ? 388 ARG A CZ  1 
ATOM   2597 N  NH1 . ARG A 1 360 ? -11.078 -17.295 69.363  1.00 26.29 ? 388 ARG A NH1 1 
ATOM   2598 N  NH2 . ARG A 1 360 ? -9.790  -17.110 71.268  1.00 26.48 ? 388 ARG A NH2 1 
ATOM   2599 N  N   . PRO A 1 361 ? -10.738 -10.193 75.227  1.00 23.15 ? 389 PRO A N   1 
ATOM   2600 C  CA  . PRO A 1 361 ? -9.959  -9.399  76.192  1.00 24.98 ? 389 PRO A CA  1 
ATOM   2601 C  C   . PRO A 1 361 ? -8.529  -9.918  76.310  1.00 26.95 ? 389 PRO A C   1 
ATOM   2602 O  O   . PRO A 1 361 ? -8.097  -10.389 77.359  1.00 26.53 ? 389 PRO A O   1 
ATOM   2603 C  CB  . PRO A 1 361 ? -10.761 -9.581  77.486  1.00 23.35 ? 389 PRO A CB  1 
ATOM   2604 C  CG  . PRO A 1 361 ? -11.363 -10.958 77.355  1.00 24.05 ? 389 PRO A CG  1 
ATOM   2605 C  CD  . PRO A 1 361 ? -11.722 -11.079 75.886  1.00 24.89 ? 389 PRO A CD  1 
ATOM   2606 N  N   . THR A 1 362 ? -7.805  -9.887  75.194  1.00 21.50 ? 390 THR A N   1 
ATOM   2607 C  CA  . THR A 1 362 ? -6.500  -10.528 75.123  1.00 22.16 ? 390 THR A CA  1 
ATOM   2608 C  C   . THR A 1 362 ? -5.447  -9.452  74.848  1.00 21.48 ? 390 THR A C   1 
ATOM   2609 O  O   . THR A 1 362 ? -5.006  -8.774  75.781  1.00 22.70 ? 390 THR A O   1 
ATOM   2610 C  CB  . THR A 1 362 ? -6.507  -11.632 74.059  1.00 22.91 ? 390 THR A CB  1 
ATOM   2611 O  OG1 . THR A 1 362 ? -7.055  -11.120 72.835  1.00 23.54 ? 390 THR A OG1 1 
ATOM   2612 C  CG2 . THR A 1 362 ? -7.370  -12.808 74.539  1.00 20.48 ? 390 THR A CG2 1 
ATOM   2613 N  N   . ILE A 1 363 ? -5.099  -9.222  73.579  1.00 20.17 ? 391 ILE A N   1 
ATOM   2614 C  CA  . ILE A 1 363 ? -4.021  -8.288  73.249  1.00 20.76 ? 391 ILE A CA  1 
ATOM   2615 C  C   . ILE A 1 363 ? -4.503  -6.839  73.360  1.00 21.32 ? 391 ILE A C   1 
ATOM   2616 O  O   . ILE A 1 363 ? -5.639  -6.499  73.001  1.00 18.28 ? 391 ILE A O   1 
ATOM   2617 C  CB  . ILE A 1 363 ? -3.458  -8.606  71.843  1.00 18.69 ? 391 ILE A CB  1 
ATOM   2618 C  CG1 . ILE A 1 363 ? -2.313  -7.648  71.471  1.00 22.45 ? 391 ILE A CG1 1 
ATOM   2619 C  CG2 . ILE A 1 363 ? -4.571  -8.591  70.772  1.00 20.91 ? 391 ILE A CG2 1 
ATOM   2620 C  CD1 . ILE A 1 363 ? -1.589  -8.087  70.182  1.00 23.64 ? 391 ILE A CD1 1 
ATOM   2621 N  N   . PHE A 1 364 ? -3.642  -5.977  73.887  1.00 20.15 ? 392 PHE A N   1 
ATOM   2622 C  CA  . PHE A 1 364 ? -3.866  -4.530  73.874  1.00 22.10 ? 392 PHE A CA  1 
ATOM   2623 C  C   . PHE A 1 364 ? -2.538  -3.861  73.541  1.00 21.01 ? 392 PHE A C   1 
ATOM   2624 O  O   . PHE A 1 364 ? -1.507  -4.527  73.393  1.00 22.10 ? 392 PHE A O   1 
ATOM   2625 C  CB  . PHE A 1 364 ? -4.438  -4.022  75.210  1.00 21.25 ? 392 PHE A CB  1 
ATOM   2626 C  CG  . PHE A 1 364 ? -3.688  -4.514  76.440  1.00 23.83 ? 392 PHE A CG  1 
ATOM   2627 C  CD1 . PHE A 1 364 ? -4.003  -5.736  77.023  1.00 25.58 ? 392 PHE A CD1 1 
ATOM   2628 C  CD2 . PHE A 1 364 ? -2.692  -3.732  77.028  1.00 27.49 ? 392 PHE A CD2 1 
ATOM   2629 C  CE1 . PHE A 1 364 ? -3.320  -6.185  78.156  1.00 28.56 ? 392 PHE A CE1 1 
ATOM   2630 C  CE2 . PHE A 1 364 ? -2.012  -4.166  78.160  1.00 26.06 ? 392 PHE A CE2 1 
ATOM   2631 C  CZ  . PHE A 1 364 ? -2.318  -5.391  78.726  1.00 27.90 ? 392 PHE A CZ  1 
ATOM   2632 N  N   . ILE A 1 365 ? -2.566  -2.537  73.413  1.00 21.96 ? 393 ILE A N   1 
ATOM   2633 C  CA  . ILE A 1 365 ? -1.391  -1.743  73.072  1.00 21.70 ? 393 ILE A CA  1 
ATOM   2634 C  C   . ILE A 1 365 ? -1.105  -0.773  74.208  1.00 22.29 ? 393 ILE A C   1 
ATOM   2635 O  O   . ILE A 1 365 ? -2.026  -0.302  74.888  1.00 24.53 ? 393 ILE A O   1 
ATOM   2636 C  CB  . ILE A 1 365 ? -1.589  -1.018  71.718  1.00 19.54 ? 393 ILE A CB  1 
ATOM   2637 C  CG1 . ILE A 1 365 ? -1.227  -1.984  70.578  1.00 18.97 ? 393 ILE A CG1 1 
ATOM   2638 C  CG2 . ILE A 1 365 ? -0.743  0.295   71.609  1.00 20.85 ? 393 ILE A CG2 1 
ATOM   2639 C  CD1 . ILE A 1 365 ? -1.595  -1.478  69.197  1.00 19.32 ? 393 ILE A CD1 1 
ATOM   2640 N  N   . GLU A 1 366 ? 0.186   -0.535  74.453  1.00 21.60 ? 394 GLU A N   1 
ATOM   2641 C  CA  . GLU A 1 366 ? 0.659   0.485   75.378  1.00 26.51 ? 394 GLU A CA  1 
ATOM   2642 C  C   . GLU A 1 366 ? 1.378   1.573   74.588  1.00 23.71 ? 394 GLU A C   1 
ATOM   2643 O  O   . GLU A 1 366 ? 2.160   1.274   73.680  1.00 22.04 ? 394 GLU A O   1 
ATOM   2644 C  CB  . GLU A 1 366 ? 1.605   -0.133  76.409  1.00 25.38 ? 394 GLU A CB  1 
ATOM   2645 C  CG  . GLU A 1 366 ? 2.207   0.832   77.408  1.00 25.44 ? 394 GLU A CG  1 
ATOM   2646 C  CD  . GLU A 1 366 ? 3.219   0.127   78.290  1.00 27.48 ? 394 GLU A CD  1 
ATOM   2647 O  OE1 . GLU A 1 366 ? 3.439   -1.079  78.059  1.00 24.32 ? 394 GLU A OE1 1 
ATOM   2648 O  OE2 . GLU A 1 366 ? 3.795   0.757   79.202  1.00 29.29 ? 394 GLU A OE2 1 
ATOM   2649 N  N   . ILE A 1 367 ? 1.094   2.836   74.901  1.00 22.42 ? 395 ILE A N   1 
ATOM   2650 C  CA  . ILE A 1 367 ? 1.861   3.954   74.360  1.00 24.33 ? 395 ILE A CA  1 
ATOM   2651 C  C   . ILE A 1 367 ? 2.778   4.436   75.469  1.00 22.86 ? 395 ILE A C   1 
ATOM   2652 O  O   . ILE A 1 367 ? 2.341   4.560   76.621  1.00 26.66 ? 395 ILE A O   1 
ATOM   2653 C  CB  . ILE A 1 367 ? 0.948   5.094   73.869  1.00 24.97 ? 395 ILE A CB  1 
ATOM   2654 C  CG1 . ILE A 1 367 ? -0.131  4.569   72.919  1.00 23.93 ? 395 ILE A CG1 1 
ATOM   2655 C  CG2 . ILE A 1 367 ? 1.797   6.202   73.204  1.00 22.29 ? 395 ILE A CG2 1 
ATOM   2656 C  CD1 . ILE A 1 367 ? 0.399   3.875   71.657  1.00 23.20 ? 395 ILE A CD1 1 
ATOM   2657 N  N   . ILE A 1 368 ? 4.048   4.682   75.148  1.00 25.39 ? 396 ILE A N   1 
ATOM   2658 C  CA  . ILE A 1 368 ? 5.007   5.082   76.169  1.00 25.12 ? 396 ILE A CA  1 
ATOM   2659 C  C   . ILE A 1 368 ? 5.930   6.178   75.653  1.00 28.66 ? 396 ILE A C   1 
ATOM   2660 O  O   . ILE A 1 368 ? 6.170   6.333   74.448  1.00 25.83 ? 396 ILE A O   1 
ATOM   2661 C  CB  . ILE A 1 368 ? 5.870   3.907   76.700  1.00 26.75 ? 396 ILE A CB  1 
ATOM   2662 C  CG1 . ILE A 1 368 ? 6.784   3.332   75.619  1.00 28.66 ? 396 ILE A CG1 1 
ATOM   2663 C  CG2 . ILE A 1 368 ? 5.007   2.788   77.236  1.00 29.48 ? 396 ILE A CG2 1 
ATOM   2664 C  CD1 . ILE A 1 368 ? 8.105   2.887   76.202  1.00 33.80 ? 396 ILE A CD1 1 
ATOM   2665 N  N   . GLN A 1 369 ? 6.461   6.929   76.606  1.00 25.69 ? 397 GLN A N   1 
ATOM   2666 C  CA  . GLN A 1 369 ? 7.611   7.787   76.362  1.00 28.26 ? 397 GLN A CA  1 
ATOM   2667 C  C   . GLN A 1 369 ? 8.471   7.783   77.614  1.00 28.32 ? 397 GLN A C   1 
ATOM   2668 O  O   . GLN A 1 369 ? 7.947   7.782   78.734  1.00 31.35 ? 397 GLN A O   1 
ATOM   2669 C  CB  . GLN A 1 369 ? 7.198   9.213   75.993  1.00 29.09 ? 397 GLN A CB  1 
ATOM   2670 C  CG  . GLN A 1 369 ? 8.382   10.064  75.534  1.00 27.92 ? 397 GLN A CG  1 
ATOM   2671 C  CD  . GLN A 1 369 ? 7.937   11.280  74.745  1.00 32.25 ? 397 GLN A CD  1 
ATOM   2672 O  OE1 . GLN A 1 369 ? 6.802   11.751  74.885  1.00 28.89 ? 397 GLN A OE1 1 
ATOM   2673 N  NE2 . GLN A 1 369 ? 8.838   11.796  73.909  1.00 33.32 ? 397 GLN A NE2 1 
ATOM   2674 N  N   . ARG A 1 370 ? 9.784   7.761   77.413  1.00 28.22 ? 398 ARG A N   1 
ATOM   2675 C  CA  . ARG A 1 370 ? 10.759  7.625   78.485  1.00 31.93 ? 398 ARG A CA  1 
ATOM   2676 C  C   . ARG A 1 370 ? 11.599  8.892   78.605  1.00 29.51 ? 398 ARG A C   1 
ATOM   2677 O  O   . ARG A 1 370 ? 11.993  9.479   77.594  1.00 28.70 ? 398 ARG A O   1 
ATOM   2678 C  CB  . ARG A 1 370 ? 11.679  6.433   78.236  1.00 31.96 ? 398 ARG A CB  1 
ATOM   2679 C  CG  . ARG A 1 370 ? 10.947  5.106   78.015  1.00 32.48 ? 398 ARG A CG  1 
ATOM   2680 C  CD  . ARG A 1 370 ? 11.942  3.959   77.919  1.00 30.01 ? 398 ARG A CD  1 
ATOM   2681 N  NE  . ARG A 1 370 ? 11.318  2.639   77.796  1.00 28.74 ? 398 ARG A NE  1 
ATOM   2682 C  CZ  . ARG A 1 370 ? 10.919  1.899   78.830  1.00 32.52 ? 398 ARG A CZ  1 
ATOM   2683 N  NH1 . ARG A 1 370 ? 11.060  2.351   80.069  1.00 29.50 ? 398 ARG A NH1 1 
ATOM   2684 N  NH2 . ARG A 1 370 ? 10.380  0.699   78.629  1.00 27.73 ? 398 ARG A NH2 1 
ATOM   2685 N  N   . VAL A 1 371 ? 11.871  9.297   79.843  1.00 30.37 ? 399 VAL A N   1 
ATOM   2686 C  CA  . VAL A 1 371 ? 12.646  10.503  80.145  1.00 33.05 ? 399 VAL A CA  1 
ATOM   2687 C  C   . VAL A 1 371 ? 13.851  10.093  80.979  1.00 34.70 ? 399 VAL A C   1 
ATOM   2688 O  O   . VAL A 1 371 ? 13.688  9.517   82.065  1.00 36.10 ? 399 VAL A O   1 
ATOM   2689 C  CB  . VAL A 1 371 ? 11.814  11.549  80.907  1.00 36.45 ? 399 VAL A CB  1 
ATOM   2690 C  CG1 . VAL A 1 371 ? 12.591  12.865  81.027  1.00 39.33 ? 399 VAL A CG1 1 
ATOM   2691 C  CG2 . VAL A 1 371 ? 10.471  11.757  80.252  1.00 37.65 ? 399 VAL A CG2 1 
ATOM   2692 N  N   . GLY A 1 372 ? 15.051  10.406  80.489  1.00 39.72 ? 400 GLY A N   1 
ATOM   2693 C  CA  . GLY A 1 372 ? 16.273  10.150  81.239  1.00 40.63 ? 400 GLY A CA  1 
ATOM   2694 C  C   . GLY A 1 372 ? 17.269  9.248   80.536  1.00 45.56 ? 400 GLY A C   1 
ATOM   2695 O  O   . GLY A 1 372 ? 17.169  9.032   79.325  1.00 43.71 ? 400 GLY A O   1 
ATOM   2696 N  N   . CYS A 1 373 ? 18.240  8.725   81.291  1.00 50.64 ? 401 CYS A N   1 
ATOM   2697 C  CA  . CYS A 1 373 ? 19.207  7.734   80.801  1.00 45.44 ? 401 CYS A CA  1 
ATOM   2698 C  C   . CYS A 1 373 ? 19.886  8.181   79.508  1.00 50.26 ? 401 CYS A C   1 
ATOM   2699 O  O   . CYS A 1 373 ? 19.967  7.437   78.531  1.00 51.21 ? 401 CYS A O   1 
ATOM   2700 C  CB  . CYS A 1 373 ? 18.543  6.370   80.607  1.00 47.92 ? 401 CYS A CB  1 
ATOM   2701 S  SG  . CYS A 1 373 ? 17.442  5.880   81.931  1.00 47.48 ? 401 CYS A SG  1 
ATOM   2702 N  N   . MET A 1 374 ? 20.326  9.413   79.499  1.00 49.83 ? 402 MET A N   1 
ATOM   2703 C  CA  . MET A 1 374 ? 20.970  9.915   78.342  1.00 54.34 ? 402 MET A CA  1 
ATOM   2704 C  C   . MET A 1 374 ? 22.433  9.548   78.421  1.00 57.27 ? 402 MET A C   1 
ATOM   2705 O  O   . MET A 1 374 ? 23.072  9.726   79.435  1.00 57.42 ? 402 MET A O   1 
ATOM   2706 C  CB  . MET A 1 374 ? 20.782  11.414  78.260  1.00 51.86 ? 402 MET A CB  1 
ATOM   2707 C  CG  . MET A 1 374 ? 19.359  11.846  77.965  1.00 51.18 ? 402 MET A CG  1 
ATOM   2708 S  SD  . MET A 1 374 ? 18.542  10.831  76.755  1.00 56.21 ? 402 MET A SD  1 
ATOM   2709 C  CE  . MET A 1 374 ? 19.301  11.289  75.222  1.00 53.72 ? 402 MET A CE  1 
ATOM   2710 N  N   . MET A 1 375 ? 22.927  8.979   77.347  1.00 59.07 ? 403 MET A N   1 
ATOM   2711 C  CA  . MET A 1 375 ? 24.311  8.592   77.245  1.00 63.20 ? 403 MET A CA  1 
ATOM   2712 C  C   . MET A 1 375 ? 24.871  9.177   75.959  1.00 65.32 ? 403 MET A C   1 
ATOM   2713 O  O   . MET A 1 375 ? 24.134  9.606   75.088  1.00 64.41 ? 403 MET A O   1 
ATOM   2714 C  CB  . MET A 1 375 ? 24.454  7.075   77.202  1.00 63.98 ? 403 MET A CB  1 
ATOM   2715 C  CG  . MET A 1 375 ? 23.570  6.354   78.168  1.00 60.14 ? 403 MET A CG  1 
ATOM   2716 S  SD  . MET A 1 375 ? 24.311  6.370   79.789  1.00 74.49 ? 403 MET A SD  1 
ATOM   2717 C  CE  . MET A 1 375 ? 25.339  4.926   79.639  1.00 63.21 ? 403 MET A CE  1 
ATOM   2718 N  N   . TYR A 1 383 ? 22.367  9.338   73.223  1.00 59.70 ? 411 TYR A N   1 
ATOM   2719 C  CA  . TYR A 1 383 ? 21.241  8.453   73.029  1.00 58.23 ? 411 TYR A CA  1 
ATOM   2720 C  C   . TYR A 1 383 ? 20.643  8.047   74.354  1.00 58.18 ? 411 TYR A C   1 
ATOM   2721 O  O   . TYR A 1 383 ? 21.163  8.394   75.390  1.00 55.06 ? 411 TYR A O   1 
ATOM   2722 C  CB  . TYR A 1 383 ? 21.683  7.220   72.277  1.00 61.48 ? 411 TYR A CB  1 
ATOM   2723 N  N   . GLN A 1 384 ? 19.507  7.355   74.305  1.00 55.06 ? 412 GLN A N   1 
ATOM   2724 C  CA  . GLN A 1 384 ? 18.845  6.922   75.528  1.00 51.22 ? 412 GLN A CA  1 
ATOM   2725 C  C   . GLN A 1 384 ? 18.993  5.413   75.668  1.00 52.30 ? 412 GLN A C   1 
ATOM   2726 O  O   . GLN A 1 384 ? 18.806  4.674   74.694  1.00 52.74 ? 412 GLN A O   1 
ATOM   2727 C  CB  . GLN A 1 384 ? 17.365  7.310   75.519  1.00 49.20 ? 412 GLN A CB  1 
ATOM   2728 C  CG  . GLN A 1 384 ? 16.682  7.120   76.858  1.00 48.03 ? 412 GLN A CG  1 
ATOM   2729 C  CD  . GLN A 1 384 ? 15.217  7.513   76.822  1.00 45.06 ? 412 GLN A CD  1 
ATOM   2730 O  OE1 . GLN A 1 384 ? 14.415  6.907   76.104  1.00 40.25 ? 412 GLN A OE1 1 
ATOM   2731 N  NE2 . GLN A 1 384 ? 14.860  8.545   77.592  1.00 43.16 ? 412 GLN A NE2 1 
ATOM   2732 N  N   . SER A 1 385 ? 19.340  4.956   76.870  1.00 45.72 ? 413 SER A N   1 
ATOM   2733 C  CA  . SER A 1 385 ? 19.488  3.520   77.052  1.00 45.08 ? 413 SER A CA  1 
ATOM   2734 C  C   . SER A 1 385 ? 18.115  2.868   77.175  1.00 40.33 ? 413 SER A C   1 
ATOM   2735 O  O   . SER A 1 385 ? 17.122  3.509   77.524  1.00 37.63 ? 413 SER A O   1 
ATOM   2736 C  CB  . SER A 1 385 ? 20.358  3.199   78.272  1.00 47.74 ? 413 SER A CB  1 
ATOM   2737 O  OG  . SER A 1 385 ? 19.782  3.659   79.482  1.00 48.07 ? 413 SER A OG  1 
ATOM   2738 N  N   . GLY A 1 386 ? 18.065  1.577   76.869  1.00 39.67 ? 414 GLY A N   1 
ATOM   2739 C  CA  . GLY A 1 386 ? 16.786  0.900   76.783  1.00 33.07 ? 414 GLY A CA  1 
ATOM   2740 C  C   . GLY A 1 386 ? 16.179  0.625   78.140  1.00 37.33 ? 414 GLY A C   1 
ATOM   2741 O  O   . GLY A 1 386 ? 16.873  0.394   79.127  1.00 35.12 ? 414 GLY A O   1 
ATOM   2742 N  N   . GLY A 1 387 ? 14.848  0.626   78.174  1.00 34.92 ? 415 GLY A N   1 
ATOM   2743 C  CA  . GLY A 1 387 ? 14.166  0.352   79.415  1.00 33.24 ? 415 GLY A CA  1 
ATOM   2744 C  C   . GLY A 1 387 ? 14.240  1.462   80.432  1.00 33.14 ? 415 GLY A C   1 
ATOM   2745 O  O   . GLY A 1 387 ? 13.880  1.235   81.590  1.00 34.82 ? 415 GLY A O   1 
ATOM   2746 N  N   . CYS A 1 388 ? 14.683  2.657   80.033  1.00 30.96 ? 416 CYS A N   1 
ATOM   2747 C  CA  . CYS A 1 388 ? 14.780  3.801   80.937  1.00 37.05 ? 416 CYS A CA  1 
ATOM   2748 C  C   . CYS A 1 388 ? 13.476  4.106   81.669  1.00 36.29 ? 416 CYS A C   1 
ATOM   2749 O  O   . CYS A 1 388 ? 12.504  4.568   81.060  1.00 35.26 ? 416 CYS A O   1 
ATOM   2750 C  CB  . CYS A 1 388 ? 15.224  5.039   80.160  1.00 36.21 ? 416 CYS A CB  1 
ATOM   2751 S  SG  . CYS A 1 388 ? 15.601  6.419   81.245  1.00 44.77 ? 416 CYS A SG  1 
ATOM   2752 N  N   . GLY A 1 389 ? 13.448  3.892   82.987  1.00 37.65 ? 417 GLY A N   1 
ATOM   2753 C  CA  . GLY A 1 389 ? 12.253  4.107   83.776  1.00 33.97 ? 417 GLY A CA  1 
ATOM   2754 C  C   . GLY A 1 389 ? 11.487  2.842   84.091  1.00 37.03 ? 417 GLY A C   1 
ATOM   2755 O  O   . GLY A 1 389 ? 10.586  2.870   84.941  1.00 36.51 ? 417 GLY A O   1 
ATOM   2756 N  N   . GLY A 1 390 ? 11.829  1.733   83.444  1.00 33.95 ? 418 GLY A N   1 
ATOM   2757 C  CA  . GLY A 1 390 ? 11.212  0.462   83.761  1.00 34.17 ? 418 GLY A CA  1 
ATOM   2758 C  C   . GLY A 1 390 ? 10.001  0.184   82.898  1.00 33.30 ? 418 GLY A C   1 
ATOM   2759 O  O   . GLY A 1 390 ? 9.957   0.580   81.729  1.00 31.49 ? 418 GLY A O   1 
ATOM   2760 N  N   . PHE A 1 391 ? 9.013   -0.508  83.462  1.00 32.34 ? 419 PHE A N   1 
ATOM   2761 C  CA  . PHE A 1 391 ? 7.848   -0.943  82.703  1.00 30.01 ? 419 PHE A CA  1 
ATOM   2762 C  C   . PHE A 1 391 ? 6.541   -0.529  83.368  1.00 33.92 ? 419 PHE A C   1 
ATOM   2763 O  O   . PHE A 1 391 ? 5.459   -0.887  82.877  1.00 33.07 ? 419 PHE A O   1 
ATOM   2764 C  CB  . PHE A 1 391 ? 7.936   -2.461  82.471  1.00 30.53 ? 419 PHE A CB  1 
ATOM   2765 C  CG  . PHE A 1 391 ? 9.158   -2.849  81.680  1.00 29.19 ? 419 PHE A CG  1 
ATOM   2766 C  CD1 . PHE A 1 391 ? 10.379  -3.083  82.321  1.00 33.01 ? 419 PHE A CD1 1 
ATOM   2767 C  CD2 . PHE A 1 391 ? 9.120   -2.875  80.291  1.00 26.12 ? 419 PHE A CD2 1 
ATOM   2768 C  CE1 . PHE A 1 391 ? 11.513  -3.385  81.599  1.00 31.64 ? 419 PHE A CE1 1 
ATOM   2769 C  CE2 . PHE A 1 391 ? 10.262  -3.165  79.558  1.00 28.63 ? 419 PHE A CE2 1 
ATOM   2770 C  CZ  . PHE A 1 391 ? 11.465  -3.427  80.220  1.00 33.03 ? 419 PHE A CZ  1 
ATOM   2771 N  N   . GLY A 1 392 ? 6.607   0.251   84.444  1.00 35.32 ? 420 GLY A N   1 
ATOM   2772 C  CA  . GLY A 1 392 ? 5.418   0.779   85.076  1.00 34.73 ? 420 GLY A CA  1 
ATOM   2773 C  C   . GLY A 1 392 ? 4.871   -0.065  86.196  1.00 39.67 ? 420 GLY A C   1 
ATOM   2774 O  O   . GLY A 1 392 ? 3.726   0.154   86.613  1.00 37.62 ? 420 GLY A O   1 
ATOM   2775 N  N   . LYS A 1 393 ? 5.655   -1.016  86.705  1.00 36.03 ? 421 LYS A N   1 
ATOM   2776 C  CA  . LYS A 1 393 ? 5.155   -1.925  87.731  1.00 42.27 ? 421 LYS A CA  1 
ATOM   2777 C  C   . LYS A 1 393 ? 4.743   -1.176  88.990  1.00 41.52 ? 421 LYS A C   1 
ATOM   2778 O  O   . LYS A 1 393 ? 3.841   -1.624  89.706  1.00 44.06 ? 421 LYS A O   1 
ATOM   2779 C  CB  . LYS A 1 393 ? 6.213   -2.987  88.053  1.00 42.84 ? 421 LYS A CB  1 
ATOM   2780 C  CG  . LYS A 1 393 ? 6.130   -4.247  87.181  1.00 49.26 ? 421 LYS A CG  1 
ATOM   2781 C  CD  . LYS A 1 393 ? 7.101   -5.334  87.658  1.00 50.03 ? 421 LYS A CD  1 
ATOM   2782 C  CE  . LYS A 1 393 ? 6.473   -6.711  87.588  1.00 49.16 ? 421 LYS A CE  1 
ATOM   2783 N  NZ  . LYS A 1 393 ? 5.361   -6.913  88.568  1.00 49.77 ? 421 LYS A NZ  1 
ATOM   2784 N  N   . GLY A 1 394 ? 5.380   -0.034  89.271  1.00 41.77 ? 422 GLY A N   1 
ATOM   2785 C  CA  . GLY A 1 394 ? 4.976   0.785   90.399  1.00 39.87 ? 422 GLY A CA  1 
ATOM   2786 C  C   . GLY A 1 394 ? 3.590   1.377   90.252  1.00 46.59 ? 422 GLY A C   1 
ATOM   2787 O  O   . GLY A 1 394 ? 3.021   1.870   91.235  1.00 44.93 ? 422 GLY A O   1 
ATOM   2788 N  N   . ASN A 1 395 ? 3.032   1.349   89.044  1.00 40.88 ? 423 ASN A N   1 
ATOM   2789 C  CA  . ASN A 1 395 ? 1.708   1.915   88.848  1.00 44.36 ? 423 ASN A CA  1 
ATOM   2790 C  C   . ASN A 1 395 ? 0.590   0.977   89.284  1.00 44.24 ? 423 ASN A C   1 
ATOM   2791 O  O   . ASN A 1 395 ? -0.552  1.429   89.395  1.00 43.38 ? 423 ASN A O   1 
ATOM   2792 C  CB  . ASN A 1 395 ? 1.526   2.318   87.385  1.00 38.38 ? 423 ASN A CB  1 
ATOM   2793 C  CG  . ASN A 1 395 ? 1.874   3.760   87.130  1.00 39.08 ? 423 ASN A CG  1 
ATOM   2794 O  OD1 . ASN A 1 395 ? 1.595   4.630   87.954  1.00 43.26 ? 423 ASN A OD1 1 
ATOM   2795 N  ND2 . ASN A 1 395 ? 2.480   4.030   85.977  1.00 38.59 ? 423 ASN A ND2 1 
ATOM   2796 N  N   . PHE A 1 396 ? 0.880   -0.302  89.550  1.00 40.82 ? 424 PHE A N   1 
ATOM   2797 C  CA  . PHE A 1 396 ? -0.146  -1.185  90.106  1.00 48.09 ? 424 PHE A CA  1 
ATOM   2798 C  C   . PHE A 1 396 ? -0.566  -0.718  91.495  1.00 50.05 ? 424 PHE A C   1 
ATOM   2799 O  O   . PHE A 1 396 ? -1.750  -0.474  91.754  1.00 52.17 ? 424 PHE A O   1 
ATOM   2800 C  CB  . PHE A 1 396 ? 0.354   -2.633  90.163  1.00 45.70 ? 424 PHE A CB  1 
ATOM   2801 C  CG  . PHE A 1 396 ? 0.410   -3.317  88.823  1.00 43.58 ? 424 PHE A CG  1 
ATOM   2802 C  CD1 . PHE A 1 396 ? 1.618   -3.490  88.170  1.00 46.61 ? 424 PHE A CD1 1 
ATOM   2803 C  CD2 . PHE A 1 396 ? -0.745  -3.789  88.220  1.00 48.48 ? 424 PHE A CD2 1 
ATOM   2804 C  CE1 . PHE A 1 396 ? 1.676   -4.122  86.938  1.00 46.22 ? 424 PHE A CE1 1 
ATOM   2805 C  CE2 . PHE A 1 396 ? -0.694  -4.422  86.986  1.00 46.41 ? 424 PHE A CE2 1 
ATOM   2806 C  CZ  . PHE A 1 396 ? 0.518   -4.586  86.347  1.00 40.04 ? 424 PHE A CZ  1 
ATOM   2807 N  N   . SER A 1 397 ? 0.402   -0.579  92.402  1.00 51.33 ? 425 SER A N   1 
ATOM   2808 C  CA  . SER A 1 397 ? 0.094   -0.097  93.744  1.00 53.75 ? 425 SER A CA  1 
ATOM   2809 C  C   . SER A 1 397 ? -0.397  1.346   93.718  1.00 53.94 ? 425 SER A C   1 
ATOM   2810 O  O   . SER A 1 397 ? -1.365  1.689   94.402  1.00 58.65 ? 425 SER A O   1 
ATOM   2811 C  CB  . SER A 1 397 ? 1.320   -0.219  94.645  1.00 54.42 ? 425 SER A CB  1 
ATOM   2812 O  OG  . SER A 1 397 ? 2.128   0.933   94.517  1.00 62.22 ? 425 SER A OG  1 
ATOM   2813 N  N   . GLU A 1 398 ? 0.261   2.215   92.944  1.00 51.98 ? 426 GLU A N   1 
ATOM   2814 C  CA  . GLU A 1 398 ? -0.122  3.624   92.963  1.00 54.08 ? 426 GLU A CA  1 
ATOM   2815 C  C   . GLU A 1 398 ? -1.514  3.836   92.383  1.00 58.42 ? 426 GLU A C   1 
ATOM   2816 O  O   . GLU A 1 398 ? -2.220  4.774   92.777  1.00 56.68 ? 426 GLU A O   1 
ATOM   2817 C  CB  . GLU A 1 398 ? 0.894   4.472   92.205  1.00 52.81 ? 426 GLU A CB  1 
ATOM   2818 C  CG  . GLU A 1 398 ? 1.796   5.288   93.140  1.00 58.58 ? 426 GLU A CG  1 
ATOM   2819 C  CD  . GLU A 1 398 ? 1.098   6.445   93.860  1.00 59.25 ? 426 GLU A CD  1 
ATOM   2820 O  OE1 . GLU A 1 398 ? 1.840   7.297   94.396  1.00 60.41 ? 426 GLU A OE1 1 
ATOM   2821 O  OE2 . GLU A 1 398 ? -0.158  6.541   93.835  1.00 57.79 ? 426 GLU A OE2 1 
ATOM   2822 N  N   . LEU A 1 399 ? -1.930  2.984   91.445  1.00 54.73 ? 427 LEU A N   1 
ATOM   2823 C  CA  . LEU A 1 399 ? -3.311  3.050   90.991  1.00 58.00 ? 427 LEU A CA  1 
ATOM   2824 C  C   . LEU A 1 399 ? -4.251  2.577   92.084  1.00 62.14 ? 427 LEU A C   1 
ATOM   2825 O  O   . LEU A 1 399 ? -5.196  3.287   92.440  1.00 64.20 ? 427 LEU A O   1 
ATOM   2826 C  CB  . LEU A 1 399 ? -3.503  2.227   89.722  1.00 57.17 ? 427 LEU A CB  1 
ATOM   2827 C  CG  . LEU A 1 399 ? -3.703  3.075   88.477  1.00 57.10 ? 427 LEU A CG  1 
ATOM   2828 C  CD1 . LEU A 1 399 ? -4.037  2.181   87.322  1.00 56.30 ? 427 LEU A CD1 1 
ATOM   2829 C  CD2 . LEU A 1 399 ? -4.816  4.077   88.713  1.00 52.35 ? 427 LEU A CD2 1 
ATOM   2830 N  N   . PHE A 1 400 ? -3.998  1.383   92.633  1.00 58.87 ? 428 PHE A N   1 
ATOM   2831 C  CA  . PHE A 1 400 ? -4.844  0.828   93.687  1.00 61.54 ? 428 PHE A CA  1 
ATOM   2832 C  C   . PHE A 1 400 ? -5.018  1.808   94.842  1.00 65.19 ? 428 PHE A C   1 
ATOM   2833 O  O   . PHE A 1 400 ? -6.136  2.029   95.323  1.00 67.72 ? 428 PHE A O   1 
ATOM   2834 C  CB  . PHE A 1 400 ? -4.251  -0.492  94.186  1.00 61.10 ? 428 PHE A CB  1 
ATOM   2835 N  N   . LYS A 1 401 ? -3.916  2.407   95.305  1.00 64.72 ? 429 LYS A N   1 
ATOM   2836 C  CA  . LYS A 1 401 ? -4.011  3.419   96.353  1.00 63.42 ? 429 LYS A CA  1 
ATOM   2837 C  C   . LYS A 1 401 ? -4.919  4.564   95.923  1.00 65.62 ? 429 LYS A C   1 
ATOM   2838 O  O   . LYS A 1 401 ? -5.828  4.960   96.660  1.00 67.06 ? 429 LYS A O   1 
ATOM   2839 C  CB  . LYS A 1 401 ? -2.622  3.945   96.714  1.00 60.98 ? 429 LYS A CB  1 
ATOM   2840 C  CG  . LYS A 1 401 ? -1.721  2.923   97.379  1.00 63.88 ? 429 LYS A CG  1 
ATOM   2841 C  CD  . LYS A 1 401 ? -0.857  3.574   98.447  1.00 67.25 ? 429 LYS A CD  1 
ATOM   2842 C  CE  . LYS A 1 401 ? -0.222  4.862   97.943  1.00 63.78 ? 429 LYS A CE  1 
ATOM   2843 N  NZ  . LYS A 1 401 ? 0.939   4.593   97.050  1.00 66.62 ? 429 LYS A NZ  1 
ATOM   2844 N  N   . SER A 1 402 ? -4.699  5.089   94.714  1.00 62.48 ? 430 SER A N   1 
ATOM   2845 C  CA  . SER A 1 402 ? -5.480  6.225   94.234  1.00 64.90 ? 430 SER A CA  1 
ATOM   2846 C  C   . SER A 1 402 ? -6.976  5.939   94.268  1.00 68.20 ? 430 SER A C   1 
ATOM   2847 O  O   . SER A 1 402 ? -7.774  6.830   94.585  1.00 67.32 ? 430 SER A O   1 
ATOM   2848 C  CB  . SER A 1 402 ? -5.045  6.595   92.817  1.00 60.00 ? 430 SER A CB  1 
ATOM   2849 O  OG  . SER A 1 402 ? -3.737  7.130   92.821  1.00 63.44 ? 430 SER A OG  1 
ATOM   2850 N  N   . ILE A 1 403 ? -7.380  4.706   93.939  1.00 65.26 ? 431 ILE A N   1 
ATOM   2851 C  CA  . ILE A 1 403 ? -8.805  4.388   93.917  1.00 69.21 ? 431 ILE A CA  1 
ATOM   2852 C  C   . ILE A 1 403 ? -9.374  4.388   95.330  1.00 72.68 ? 431 ILE A C   1 
ATOM   2853 O  O   . ILE A 1 403 ? -10.457 4.933   95.576  1.00 74.72 ? 431 ILE A O   1 
ATOM   2854 C  CB  . ILE A 1 403 ? -9.074  3.042   93.215  1.00 70.17 ? 431 ILE A CB  1 
ATOM   2855 C  CG1 . ILE A 1 403 ? -8.083  2.776   92.084  1.00 66.51 ? 431 ILE A CG1 1 
ATOM   2856 C  CG2 . ILE A 1 403 ? -10.490 3.015   92.654  1.00 74.74 ? 431 ILE A CG2 1 
ATOM   2857 C  CD1 . ILE A 1 403 ? -8.233  3.686   90.900  1.00 63.67 ? 431 ILE A CD1 1 
ATOM   2858 N  N   . GLU A 1 404 ? -8.663  3.772   96.278  1.00 70.98 ? 432 GLU A N   1 
ATOM   2859 C  CA  . GLU A 1 404 ? -9.149  3.749   97.654  1.00 72.78 ? 432 GLU A CA  1 
ATOM   2860 C  C   . GLU A 1 404 ? -9.091  5.137   98.284  1.00 74.36 ? 432 GLU A C   1 
ATOM   2861 O  O   . GLU A 1 404 ? -9.984  5.512   99.052  1.00 77.08 ? 432 GLU A O   1 
ATOM   2862 C  CB  . GLU A 1 404 ? -8.349  2.739   98.477  1.00 72.62 ? 432 GLU A CB  1 
ATOM   2863 N  N   . GLU A 1 405 ? -8.050  5.915   97.969  1.00 70.82 ? 433 GLU A N   1 
ATOM   2864 C  CA  . GLU A 1 405 ? -7.986  7.298   98.435  1.00 72.55 ? 433 GLU A CA  1 
ATOM   2865 C  C   . GLU A 1 405 ? -9.161  8.109   97.897  1.00 76.31 ? 433 GLU A C   1 
ATOM   2866 O  O   . GLU A 1 405 ? -9.840  8.818   98.649  1.00 77.89 ? 433 GLU A O   1 
ATOM   2867 C  CB  . GLU A 1 405 ? -6.657  7.939   98.020  1.00 66.76 ? 433 GLU A CB  1 
ATOM   2868 C  CG  . GLU A 1 405 ? -5.422  7.317   98.659  1.00 69.48 ? 433 GLU A CG  1 
ATOM   2869 C  CD  . GLU A 1 405 ? -4.117  7.897   98.125  1.00 69.76 ? 433 GLU A CD  1 
ATOM   2870 O  OE1 . GLU A 1 405 ? -4.168  8.884   97.358  1.00 66.43 ? 433 GLU A OE1 1 
ATOM   2871 O  OE2 . GLU A 1 405 ? -3.038  7.360   98.470  1.00 68.57 ? 433 GLU A OE2 1 
ATOM   2872 N  N   . TYR A 1 406 ? -9.421  8.006   96.589  1.00 75.00 ? 434 TYR A N   1 
ATOM   2873 C  CA  . TYR A 1 406 ? -10.508 8.761   95.976  1.00 73.97 ? 434 TYR A CA  1 
ATOM   2874 C  C   . TYR A 1 406 ? -11.881 8.280   96.427  1.00 76.40 ? 434 TYR A C   1 
ATOM   2875 O  O   . TYR A 1 406 ? -12.855 9.032   96.306  1.00 76.22 ? 434 TYR A O   1 
ATOM   2876 C  CB  . TYR A 1 406 ? -10.408 8.687   94.453  1.00 68.65 ? 434 TYR A CB  1 
ATOM   2877 C  CG  . TYR A 1 406 ? -11.427 9.539   93.741  1.00 66.23 ? 434 TYR A CG  1 
ATOM   2878 C  CD1 . TYR A 1 406 ? -11.333 10.924  93.759  1.00 67.14 ? 434 TYR A CD1 1 
ATOM   2879 C  CD2 . TYR A 1 406 ? -12.487 8.961   93.055  1.00 70.28 ? 434 TYR A CD2 1 
ATOM   2880 C  CE1 . TYR A 1 406 ? -12.267 11.709  93.116  1.00 68.77 ? 434 TYR A CE1 1 
ATOM   2881 C  CE2 . TYR A 1 406 ? -13.424 9.739   92.402  1.00 69.66 ? 434 TYR A CE2 1 
ATOM   2882 C  CZ  . TYR A 1 406 ? -13.307 11.111  92.436  1.00 70.05 ? 434 TYR A CZ  1 
ATOM   2883 O  OH  . TYR A 1 406 ? -14.238 11.892  91.791  1.00 77.21 ? 434 TYR A OH  1 
ATOM   2884 N  N   . GLU A 1 407 ? -11.980 7.053   96.949  1.00 76.44 ? 435 GLU A N   1 
ATOM   2885 C  CA  . GLU A 1 407 ? -13.259 6.559   97.450  1.00 78.37 ? 435 GLU A CA  1 
ATOM   2886 C  C   . GLU A 1 407 ? -13.832 7.466   98.533  1.00 82.72 ? 435 GLU A C   1 
ATOM   2887 O  O   . GLU A 1 407 ? -15.055 7.523   98.700  1.00 85.67 ? 435 GLU A O   1 
ATOM   2888 C  CB  . GLU A 1 407 ? -13.098 5.134   97.979  1.00 75.41 ? 435 GLU A CB  1 
ATOM   2889 N  N   . LYS A 1 408 ? -12.964 8.173   99.265  1.00 81.98 ? 436 LYS A N   1 
ATOM   2890 C  CA  . LYS A 1 408 ? -13.294 9.162   100.309 1.00 81.19 ? 436 LYS A CA  1 
ATOM   2891 C  C   . LYS A 1 408 ? -14.781 9.459   100.546 1.00 82.74 ? 436 LYS A C   1 
ATOM   2892 O  O   . LYS A 1 408 ? -15.431 10.145  99.754  1.00 80.85 ? 436 LYS A O   1 
ATOM   2893 C  CB  . LYS A 1 408 ? -12.575 10.482  99.995  1.00 74.17 ? 436 LYS A CB  1 
HETATM 2894 CO CO  . CO  B 2 .   ? 4.553   -2.623  79.054  1.00 26.78 ? 501 CO  A CO  1 
HETATM 2895 C  C13 . YFM C 3 .   ? 3.173   -3.519  81.594  1.00 34.83 ? 502 YFM A C13 1 
HETATM 2896 C  C17 . YFM C 3 .   ? 4.792   -6.495  83.645  1.00 33.76 ? 502 YFM A C17 1 
HETATM 2897 C  C20 . YFM C 3 .   ? 5.329   -4.817  81.200  1.00 32.15 ? 502 YFM A C20 1 
HETATM 2898 C  C24 . YFM C 3 .   ? -4.279  -3.339  83.192  1.00 38.08 ? 502 YFM A C24 1 
HETATM 2899 C  C26 . YFM C 3 .   ? -0.366  0.362   85.544  1.00 47.45 ? 502 YFM A C26 1 
HETATM 2900 C  C28 . YFM C 3 .   ? -4.384  -3.974  85.796  1.00 49.03 ? 502 YFM A C28 1 
HETATM 2901 C  C01 . YFM C 3 .   ? 2.002   -3.019  82.347  1.00 32.50 ? 502 YFM A C01 1 
HETATM 2902 C  C02 . YFM C 3 .   ? 2.442   -1.857  83.224  1.00 37.14 ? 502 YFM A C02 1 
HETATM 2903 C  C03 . YFM C 3 .   ? 1.343   -1.169  83.982  1.00 40.93 ? 502 YFM A C03 1 
HETATM 2904 C  C04 . YFM C 3 .   ? -0.074  -1.674  83.812  1.00 40.34 ? 502 YFM A C04 1 
HETATM 2905 C  C05 . YFM C 3 .   ? -0.593  -2.850  82.924  1.00 37.24 ? 502 YFM A C05 1 
HETATM 2906 C  C06 . YFM C 3 .   ? 0.570   -3.542  82.137  1.00 32.94 ? 502 YFM A C06 1 
HETATM 2907 C  C08 . YFM C 3 .   ? -2.626  -0.846  84.941  1.00 48.81 ? 502 YFM A C08 1 
HETATM 2908 C  C09 . YFM C 3 .   ? -3.177  -1.846  84.104  1.00 52.74 ? 502 YFM A C09 1 
HETATM 2909 C  C11 . YFM C 3 .   ? -1.858  -3.224  82.827  1.00 43.34 ? 502 YFM A C11 1 
HETATM 2910 C  C12 . YFM C 3 .   ? 0.427   -4.708  81.171  1.00 30.24 ? 502 YFM A C12 1 
HETATM 2911 C  C14 . YFM C 3 .   ? 3.994   -4.736  81.898  1.00 31.07 ? 502 YFM A C14 1 
HETATM 2912 C  C16 . YFM C 3 .   ? 3.706   -5.536  83.152  1.00 34.74 ? 502 YFM A C16 1 
HETATM 2913 C  C18 . YFM C 3 .   ? 6.189   -5.954  83.319  1.00 30.96 ? 502 YFM A C18 1 
HETATM 2914 C  C19 . YFM C 3 .   ? 6.398   -5.709  81.817  1.00 30.10 ? 502 YFM A C19 1 
HETATM 2915 C  C27 . YFM C 3 .   ? -4.936  -3.168  84.595  1.00 47.53 ? 502 YFM A C27 1 
HETATM 2916 C  C29 . YFM C 3 .   ? -4.942  -3.749  87.197  1.00 55.21 ? 502 YFM A C29 1 
HETATM 2917 C  C30 . YFM C 3 .   ? -6.066  -2.743  87.412  1.00 61.91 ? 502 YFM A C30 1 
HETATM 2918 C  C31 . YFM C 3 .   ? -6.619  -1.924  86.244  1.00 60.30 ? 502 YFM A C31 1 
HETATM 2919 C  C32 . YFM C 3 .   ? -6.067  -2.135  84.836  1.00 55.92 ? 502 YFM A C32 1 
HETATM 2920 C  C34 . YFM C 3 .   ? -5.681  -1.719  89.442  1.00 68.20 ? 502 YFM A C34 1 
HETATM 2921 F  F35 . YFM C 3 .   ? -5.075  -0.820  88.600  1.00 65.26 ? 502 YFM A F35 1 
HETATM 2922 F  F36 . YFM C 3 .   ? -6.376  -1.018  90.385  1.00 71.74 ? 502 YFM A F36 1 
HETATM 2923 F  F37 . YFM C 3 .   ? -4.716  -2.464  90.067  1.00 62.75 ? 502 YFM A F37 1 
HETATM 2924 N  N07 . YFM C 3 .   ? -1.014  -0.691  84.814  1.00 43.73 ? 502 YFM A N07 1 
HETATM 2925 N  N10 . YFM C 3 .   ? -2.951  -2.715  83.427  1.00 43.65 ? 502 YFM A N10 1 
HETATM 2926 O  O15 . YFM C 3 .   ? 3.418   -2.786  80.683  1.00 29.73 ? 502 YFM A O15 1 
HETATM 2927 O  O21 . YFM C 3 .   ? 2.378   -5.651  83.556  1.00 35.37 ? 502 YFM A O21 1 
HETATM 2928 O  O22 . YFM C 3 .   ? 5.522   -4.171  80.212  1.00 28.79 ? 502 YFM A O22 1 
HETATM 2929 O  O23 . YFM C 3 .   ? -2.111  -4.137  82.133  1.00 47.19 ? 502 YFM A O23 1 
HETATM 2930 O  O25 . YFM C 3 .   ? -3.276  -0.146  85.621  1.00 56.03 ? 502 YFM A O25 1 
HETATM 2931 O  O33 . YFM C 3 .   ? -6.554  -2.555  88.708  1.00 68.80 ? 502 YFM A O33 1 
HETATM 2932 O  O   . HOH D 4 .   ? 1.946   -0.101  45.470  1.00 51.98 ? 601 HOH A O   1 
HETATM 2933 O  O   . HOH D 4 .   ? -1.822  17.850  75.476  1.00 41.89 ? 602 HOH A O   1 
HETATM 2934 O  O   . HOH D 4 .   ? 3.840   -20.768 59.328  1.00 48.73 ? 603 HOH A O   1 
HETATM 2935 O  O   . HOH D 4 .   ? 3.207   -27.059 86.474  1.00 41.23 ? 604 HOH A O   1 
HETATM 2936 O  O   . HOH D 4 .   ? 0.271   8.938   91.582  1.00 43.35 ? 605 HOH A O   1 
HETATM 2937 O  O   . HOH D 4 .   ? 23.587  -2.379  54.247  1.00 52.98 ? 606 HOH A O   1 
HETATM 2938 O  O   . HOH D 4 .   ? 23.335  -9.026  70.299  1.00 29.48 ? 607 HOH A O   1 
HETATM 2939 O  O   . HOH D 4 .   ? -9.313  -12.686 54.379  1.00 26.86 ? 608 HOH A O   1 
HETATM 2940 O  O   . HOH D 4 .   ? 19.831  -5.377  70.621  1.00 32.28 ? 609 HOH A O   1 
HETATM 2941 O  O   . HOH D 4 .   ? 9.562   -12.752 49.467  1.00 39.00 ? 610 HOH A O   1 
HETATM 2942 O  O   . HOH D 4 .   ? -5.981  -8.643  94.812  1.00 69.32 ? 611 HOH A O   1 
HETATM 2943 O  O   . HOH D 4 .   ? 25.396  -18.093 57.624  1.00 47.78 ? 612 HOH A O   1 
HETATM 2944 O  O   . HOH D 4 .   ? -2.919  17.398  68.625  1.00 37.39 ? 613 HOH A O   1 
HETATM 2945 O  O   . HOH D 4 .   ? 19.632  -0.253  79.247  1.00 39.80 ? 614 HOH A O   1 
HETATM 2946 O  O   . HOH D 4 .   ? -3.209  -20.402 84.418  1.00 45.00 ? 615 HOH A O   1 
HETATM 2947 O  O   . HOH D 4 .   ? 8.507   -17.007 48.952  1.00 45.02 ? 616 HOH A O   1 
HETATM 2948 O  O   . HOH D 4 .   ? 0.952   -7.409  90.935  1.00 53.04 ? 617 HOH A O   1 
HETATM 2949 O  O   . HOH D 4 .   ? 1.559   19.260  74.188  1.00 50.92 ? 618 HOH A O   1 
HETATM 2950 O  O   . HOH D 4 .   ? -6.886  -14.441 89.635  1.00 57.85 ? 619 HOH A O   1 
HETATM 2951 O  O   . HOH D 4 .   ? 8.907   -3.845  50.247  1.00 58.11 ? 620 HOH A O   1 
HETATM 2952 O  O   . HOH D 4 .   ? 5.089   -23.208 64.682  1.00 42.31 ? 621 HOH A O   1 
HETATM 2953 O  O   . HOH D 4 .   ? -6.176  15.517  63.841  1.00 40.46 ? 622 HOH A O   1 
HETATM 2954 O  O   . HOH D 4 .   ? -8.788  11.502  85.981  1.00 48.30 ? 623 HOH A O   1 
HETATM 2955 O  O   . HOH D 4 .   ? -0.355  -18.157 71.102  1.00 24.22 ? 624 HOH A O   1 
HETATM 2956 O  O   . HOH D 4 .   ? -6.169  -8.782  48.836  1.00 25.31 ? 625 HOH A O   1 
HETATM 2957 O  O   . HOH D 4 .   ? 5.547   -0.880  80.209  1.00 25.65 ? 626 HOH A O   1 
HETATM 2958 O  O   . HOH D 4 .   ? 15.185  12.117  78.535  1.00 47.21 ? 627 HOH A O   1 
HETATM 2959 O  O   . HOH D 4 .   ? 9.375   -23.577 54.144  1.00 43.44 ? 628 HOH A O   1 
HETATM 2960 O  O   . HOH D 4 .   ? 2.884   -14.707 57.173  1.00 20.95 ? 629 HOH A O   1 
HETATM 2961 O  O   . HOH D 4 .   ? 8.432   -22.955 56.890  1.00 44.70 ? 630 HOH A O   1 
HETATM 2962 O  O   . HOH D 4 .   ? 2.081   21.313  79.569  1.00 57.14 ? 631 HOH A O   1 
HETATM 2963 O  O   . HOH D 4 .   ? 5.086   -22.819 54.931  1.00 33.60 ? 632 HOH A O   1 
HETATM 2964 O  O   . HOH D 4 .   ? -5.430  -8.888  78.356  1.00 32.25 ? 633 HOH A O   1 
HETATM 2965 O  O   . HOH D 4 .   ? 13.409  -1.177  73.308  1.00 24.89 ? 634 HOH A O   1 
HETATM 2966 O  O   . HOH D 4 .   ? -4.050  -4.313  46.406  1.00 35.86 ? 635 HOH A O   1 
HETATM 2967 O  O   . HOH D 4 .   ? 4.385   -16.754 58.284  1.00 27.38 ? 636 HOH A O   1 
HETATM 2968 O  O   . HOH D 4 .   ? 14.726  -2.683  69.237  1.00 29.42 ? 637 HOH A O   1 
HETATM 2969 O  O   . HOH D 4 .   ? -7.100  -12.528 70.615  1.00 29.62 ? 638 HOH A O   1 
HETATM 2970 O  O   . HOH D 4 .   ? -0.969  -2.190  42.499  1.00 54.32 ? 639 HOH A O   1 
HETATM 2971 O  O   . HOH D 4 .   ? 22.898  -6.498  57.535  1.00 57.57 ? 640 HOH A O   1 
HETATM 2972 O  O   . HOH D 4 .   ? 3.650   -25.490 40.707  1.00 41.90 ? 641 HOH A O   1 
HETATM 2973 O  O   . HOH D 4 .   ? 10.741  13.782  72.184  1.00 32.24 ? 642 HOH A O   1 
HETATM 2974 O  O   . HOH D 4 .   ? 13.663  0.946   75.278  1.00 28.88 ? 643 HOH A O   1 
HETATM 2975 O  O   . HOH D 4 .   ? -11.826 -11.726 53.927  1.00 24.27 ? 644 HOH A O   1 
HETATM 2976 O  O   . HOH D 4 .   ? 17.366  -16.277 46.841  1.00 53.07 ? 645 HOH A O   1 
HETATM 2977 O  O   . HOH D 4 .   ? 4.781   -13.045 45.426  1.00 34.06 ? 646 HOH A O   1 
HETATM 2978 O  O   . HOH D 4 .   ? 11.621  -21.368 44.484  1.00 48.36 ? 647 HOH A O   1 
HETATM 2979 O  O   . HOH D 4 .   ? -13.242 13.560  67.949  1.00 34.91 ? 648 HOH A O   1 
HETATM 2980 O  O   . HOH D 4 .   ? 7.924   -11.232 75.372  1.00 26.23 ? 649 HOH A O   1 
HETATM 2981 O  O   . HOH D 4 .   ? -4.311  -19.701 48.097  1.00 27.34 ? 650 HOH A O   1 
HETATM 2982 O  O   . HOH D 4 .   ? -18.106 4.865   65.522  1.00 33.67 ? 651 HOH A O   1 
HETATM 2983 O  O   . HOH D 4 .   ? 3.916   -10.582 46.441  1.00 29.38 ? 652 HOH A O   1 
HETATM 2984 O  O   . HOH D 4 .   ? 1.393   -15.014 40.461  1.00 38.55 ? 653 HOH A O   1 
HETATM 2985 O  O   . HOH D 4 .   ? 13.184  -8.552  85.171  1.00 44.81 ? 654 HOH A O   1 
HETATM 2986 O  O   . HOH D 4 .   ? -13.206 -1.044  72.900  1.00 39.72 ? 655 HOH A O   1 
HETATM 2987 O  O   . HOH D 4 .   ? 8.580   1.549   86.138  1.00 37.74 ? 656 HOH A O   1 
HETATM 2988 O  O   . HOH D 4 .   ? -14.999 1.957   75.105  1.00 46.75 ? 657 HOH A O   1 
HETATM 2989 O  O   . HOH D 4 .   ? 5.258   -19.122 90.237  1.00 47.44 ? 658 HOH A O   1 
HETATM 2990 O  O   . HOH D 4 .   ? 16.365  -27.331 69.639  1.00 33.27 ? 659 HOH A O   1 
HETATM 2991 O  O   . HOH D 4 .   ? 20.660  -7.628  58.913  1.00 36.44 ? 660 HOH A O   1 
HETATM 2992 O  O   . HOH D 4 .   ? -7.325  6.498   80.310  1.00 39.38 ? 661 HOH A O   1 
HETATM 2993 O  O   . HOH D 4 .   ? -9.544  -14.429 52.556  1.00 31.23 ? 662 HOH A O   1 
HETATM 2994 O  O   . HOH D 4 .   ? -11.885 -24.200 72.075  1.00 42.98 ? 663 HOH A O   1 
HETATM 2995 O  O   . HOH D 4 .   ? 6.581   -20.792 61.252  1.00 30.07 ? 664 HOH A O   1 
HETATM 2996 O  O   . HOH D 4 .   ? 9.146   5.421   58.291  1.00 45.23 ? 665 HOH A O   1 
HETATM 2997 O  O   . HOH D 4 .   ? 17.157  -3.074  63.152  1.00 39.06 ? 666 HOH A O   1 
HETATM 2998 O  O   . HOH D 4 .   ? 20.603  0.591   76.240  1.00 42.15 ? 667 HOH A O   1 
HETATM 2999 O  O   . HOH D 4 .   ? 4.763   -18.078 60.807  1.00 27.41 ? 668 HOH A O   1 
HETATM 3000 O  O   . HOH D 4 .   ? 2.263   -21.978 47.935  1.00 33.37 ? 669 HOH A O   1 
HETATM 3001 O  O   . HOH D 4 .   ? -8.461  18.645  65.972  1.00 54.73 ? 670 HOH A O   1 
HETATM 3002 O  O   . HOH D 4 .   ? 3.482   7.644   60.525  1.00 31.62 ? 671 HOH A O   1 
HETATM 3003 O  O   . HOH D 4 .   ? -1.217  -5.222  95.868  1.00 63.47 ? 672 HOH A O   1 
HETATM 3004 O  O   . HOH D 4 .   ? -14.752 3.666   67.081  1.00 28.80 ? 673 HOH A O   1 
HETATM 3005 O  O   . HOH D 4 .   ? 3.403   -23.427 60.391  1.00 41.07 ? 674 HOH A O   1 
HETATM 3006 O  O   . HOH D 4 .   ? -10.165 -21.389 77.340  1.00 37.77 ? 675 HOH A O   1 
HETATM 3007 O  O   . HOH D 4 .   ? 22.294  -10.801 76.782  1.00 34.78 ? 676 HOH A O   1 
HETATM 3008 O  O   . HOH D 4 .   ? 14.463  -1.978  62.871  1.00 52.43 ? 677 HOH A O   1 
HETATM 3009 O  O   . HOH D 4 .   ? 11.832  -24.479 79.850  1.00 39.99 ? 678 HOH A O   1 
HETATM 3010 O  O   . HOH D 4 .   ? 4.721   13.419  59.833  1.00 40.54 ? 679 HOH A O   1 
HETATM 3011 O  O   . HOH D 4 .   ? -0.229  -13.749 70.200  1.00 23.19 ? 680 HOH A O   1 
HETATM 3012 O  O   . HOH D 4 .   ? 3.601   -23.202 62.752  1.00 41.64 ? 681 HOH A O   1 
HETATM 3013 O  O   . HOH D 4 .   ? -5.635  4.093   84.144  1.00 38.68 ? 682 HOH A O   1 
HETATM 3014 O  O   . HOH D 4 .   ? 19.440  -6.977  51.157  1.00 38.28 ? 683 HOH A O   1 
HETATM 3015 O  O   . HOH D 4 .   ? -14.755 8.718   73.020  1.00 44.53 ? 684 HOH A O   1 
HETATM 3016 O  O   . HOH D 4 .   ? -8.994  -15.480 55.575  1.00 28.75 ? 685 HOH A O   1 
HETATM 3017 O  O   . HOH D 4 .   ? -7.157  -4.861  49.930  1.00 42.81 ? 686 HOH A O   1 
HETATM 3018 O  O   . HOH D 4 .   ? -13.639 9.798   69.400  1.00 31.78 ? 687 HOH A O   1 
HETATM 3019 O  O   . HOH D 4 .   ? -1.641  5.402   54.675  1.00 27.15 ? 688 HOH A O   1 
HETATM 3020 O  O   . HOH D 4 .   ? 5.337   -20.860 68.681  1.00 27.87 ? 689 HOH A O   1 
HETATM 3021 O  O   . HOH D 4 .   ? 13.052  -1.008  66.076  1.00 28.69 ? 690 HOH A O   1 
HETATM 3022 O  O   . HOH D 4 .   ? 5.511   23.911  81.698  1.00 56.86 ? 691 HOH A O   1 
HETATM 3023 O  O   . HOH D 4 .   ? -11.000 -2.164  70.180  1.00 23.73 ? 692 HOH A O   1 
HETATM 3024 O  O   . HOH D 4 .   ? -7.868  -8.083  71.600  1.00 25.27 ? 693 HOH A O   1 
HETATM 3025 O  O   . HOH D 4 .   ? -12.904 -5.754  73.226  1.00 38.83 ? 694 HOH A O   1 
HETATM 3026 O  O   . HOH D 4 .   ? 12.838  -0.585  68.546  1.00 27.63 ? 695 HOH A O   1 
HETATM 3027 O  O   . HOH D 4 .   ? 2.314   -21.654 51.823  1.00 40.47 ? 696 HOH A O   1 
HETATM 3028 O  O   . HOH D 4 .   ? 16.354  -23.169 75.482  1.00 33.41 ? 697 HOH A O   1 
HETATM 3029 O  O   . HOH D 4 .   ? 4.774   -21.463 80.476  1.00 35.14 ? 698 HOH A O   1 
HETATM 3030 O  O   . HOH D 4 .   ? 26.037  -22.295 70.792  1.00 48.90 ? 699 HOH A O   1 
HETATM 3031 O  O   . HOH D 4 .   ? -13.243 -13.917 74.231  1.00 25.40 ? 700 HOH A O   1 
HETATM 3032 O  O   . HOH D 4 .   ? -5.392  5.524   81.856  1.00 34.59 ? 701 HOH A O   1 
HETATM 3033 O  O   . HOH D 4 .   ? -0.312  -22.951 52.771  1.00 41.03 ? 702 HOH A O   1 
HETATM 3034 O  O   . HOH D 4 .   ? -10.626 8.048   74.217  1.00 31.70 ? 703 HOH A O   1 
HETATM 3035 O  O   . HOH D 4 .   ? 1.660   7.569   64.802  1.00 18.91 ? 704 HOH A O   1 
HETATM 3036 O  O   . HOH D 4 .   ? -2.059  -25.538 54.802  1.00 36.60 ? 705 HOH A O   1 
HETATM 3037 O  O   . HOH D 4 .   ? 8.849   -1.811  86.092  1.00 40.24 ? 706 HOH A O   1 
HETATM 3038 O  O   . HOH D 4 .   ? -7.405  5.852   68.110  1.00 20.78 ? 707 HOH A O   1 
HETATM 3039 O  O   . HOH D 4 .   ? -4.138  -12.554 71.179  1.00 30.19 ? 708 HOH A O   1 
HETATM 3040 O  O   . HOH D 4 .   ? 11.163  7.681   74.929  1.00 46.44 ? 709 HOH A O   1 
HETATM 3041 O  O   . HOH D 4 .   ? 8.301   -19.513 76.420  1.00 44.18 ? 710 HOH A O   1 
HETATM 3042 O  O   . HOH D 4 .   ? 27.262  -11.563 73.243  1.00 35.09 ? 711 HOH A O   1 
HETATM 3043 O  O   . HOH D 4 .   ? -1.728  -20.767 73.290  1.00 28.35 ? 712 HOH A O   1 
HETATM 3044 O  O   . HOH D 4 .   ? -3.505  -9.742  80.230  1.00 27.77 ? 713 HOH A O   1 
HETATM 3045 O  O   . HOH D 4 .   ? 23.057  -12.864 63.653  1.00 32.73 ? 714 HOH A O   1 
HETATM 3046 O  O   . HOH D 4 .   ? -3.180  -24.169 48.455  1.00 34.43 ? 715 HOH A O   1 
HETATM 3047 O  O   . HOH D 4 .   ? -10.668 -17.011 54.795  1.00 33.02 ? 716 HOH A O   1 
HETATM 3048 O  O   . HOH D 4 .   ? -6.889  -16.555 59.565  1.00 29.61 ? 717 HOH A O   1 
HETATM 3049 O  O   . HOH D 4 .   ? -2.161  -23.873 70.708  1.00 45.30 ? 718 HOH A O   1 
HETATM 3050 O  O   . HOH D 4 .   ? 8.862   1.367   89.550  1.00 49.57 ? 719 HOH A O   1 
HETATM 3051 O  O   . HOH D 4 .   ? 7.820   -1.220  44.849  1.00 43.43 ? 720 HOH A O   1 
HETATM 3052 O  O   . HOH D 4 .   ? -11.839 -3.225  73.588  1.00 30.97 ? 721 HOH A O   1 
HETATM 3053 O  O   . HOH D 4 .   ? 23.086  -4.275  68.380  1.00 43.06 ? 722 HOH A O   1 
HETATM 3054 O  O   . HOH D 4 .   ? 24.691  -17.150 76.674  1.00 43.78 ? 723 HOH A O   1 
HETATM 3055 O  O   . HOH D 4 .   ? 4.305   -21.915 75.419  1.00 41.46 ? 724 HOH A O   1 
HETATM 3056 O  O   . HOH D 4 .   ? -5.349  3.313   51.790  1.00 39.74 ? 725 HOH A O   1 
HETATM 3057 O  O   . HOH D 4 .   ? 9.012   9.038   93.047  1.00 53.49 ? 726 HOH A O   1 
HETATM 3058 O  O   . HOH D 4 .   ? 0.097   -28.886 44.886  1.00 43.80 ? 727 HOH A O   1 
HETATM 3059 O  O   . HOH D 4 .   ? 11.376  -18.503 57.021  1.00 38.25 ? 728 HOH A O   1 
HETATM 3060 O  O   . HOH D 4 .   ? 9.305   -17.001 56.126  1.00 31.33 ? 729 HOH A O   1 
HETATM 3061 O  O   . HOH D 4 .   ? 16.633  -20.627 50.858  1.00 42.07 ? 730 HOH A O   1 
HETATM 3062 O  O   . HOH D 4 .   ? -9.248  -0.198  71.659  1.00 25.25 ? 731 HOH A O   1 
HETATM 3063 O  O   . HOH D 4 .   ? -15.570 4.368   71.547  1.00 35.21 ? 732 HOH A O   1 
HETATM 3064 O  O   . HOH D 4 .   ? -0.461  -22.148 76.959  1.00 28.15 ? 733 HOH A O   1 
HETATM 3065 O  O   . HOH D 4 .   ? -11.317 5.732   75.404  1.00 30.65 ? 734 HOH A O   1 
HETATM 3066 O  O   . HOH D 4 .   ? 6.154   6.028   57.600  1.00 37.38 ? 735 HOH A O   1 
HETATM 3067 O  O   . HOH D 4 .   ? 20.590  -12.640 53.118  1.00 42.61 ? 736 HOH A O   1 
HETATM 3068 O  O   . HOH D 4 .   ? -2.110  -15.932 70.664  1.00 24.79 ? 737 HOH A O   1 
HETATM 3069 O  O   . HOH D 4 .   ? 10.410  -0.733  65.902  1.00 25.46 ? 738 HOH A O   1 
HETATM 3070 O  O   . HOH D 4 .   ? -0.349  -7.086  83.147  1.00 34.10 ? 739 HOH A O   1 
HETATM 3071 O  O   . HOH D 4 .   ? -9.603  -10.889 69.659  1.00 27.57 ? 740 HOH A O   1 
HETATM 3072 O  O   . HOH D 4 .   ? -9.808  -16.418 47.727  1.00 25.35 ? 741 HOH A O   1 
HETATM 3073 O  O   . HOH D 4 .   ? 14.045  6.031   70.689  1.00 39.67 ? 742 HOH A O   1 
HETATM 3074 O  O   . HOH D 4 .   ? -4.018  3.020   80.877  1.00 30.77 ? 743 HOH A O   1 
HETATM 3075 O  O   . HOH D 4 .   ? 9.933   -21.352 48.587  1.00 47.40 ? 744 HOH A O   1 
HETATM 3076 O  O   . HOH D 4 .   ? -7.615  -8.861  69.166  1.00 25.66 ? 745 HOH A O   1 
HETATM 3077 O  O   . HOH D 4 .   ? -7.629  1.149   83.753  1.00 41.30 ? 746 HOH A O   1 
HETATM 3078 O  O   . HOH D 4 .   ? 14.606  -3.379  56.799  1.00 50.76 ? 747 HOH A O   1 
HETATM 3079 O  O   . HOH D 4 .   ? 13.743  11.221  84.781  1.00 46.12 ? 748 HOH A O   1 
HETATM 3080 O  O   . HOH D 4 .   ? -8.092  -24.376 66.200  1.00 52.34 ? 749 HOH A O   1 
HETATM 3081 O  O   . HOH D 4 .   ? -3.859  -14.268 68.643  1.00 26.39 ? 750 HOH A O   1 
HETATM 3082 O  O   . HOH D 4 .   ? 15.856  -3.026  52.220  1.00 60.41 ? 751 HOH A O   1 
HETATM 3083 O  O   . HOH D 4 .   ? -2.455  -0.155  46.378  1.00 40.67 ? 752 HOH A O   1 
HETATM 3084 O  O   . HOH D 4 .   ? 22.800  -14.093 81.108  1.00 41.24 ? 753 HOH A O   1 
HETATM 3085 O  O   . HOH D 4 .   ? 21.547  -4.745  57.151  1.00 49.88 ? 754 HOH A O   1 
HETATM 3086 O  O   . HOH D 4 .   ? -1.776  -11.675 70.595  1.00 29.16 ? 755 HOH A O   1 
HETATM 3087 O  O   . HOH D 4 .   ? -9.660  -9.531  84.194  1.00 49.86 ? 756 HOH A O   1 
HETATM 3088 O  O   . HOH D 4 .   ? 15.298  -19.924 48.474  1.00 54.60 ? 757 HOH A O   1 
HETATM 3089 O  O   . HOH D 4 .   ? -2.685  14.009  62.926  1.00 45.77 ? 758 HOH A O   1 
HETATM 3090 O  O   . HOH D 4 .   ? -10.245 -19.594 61.348  1.00 55.46 ? 759 HOH A O   1 
HETATM 3091 O  O   . HOH D 4 .   ? 22.123  -11.715 55.648  1.00 43.14 ? 760 HOH A O   1 
HETATM 3092 O  O   . HOH D 4 .   ? -11.578 7.387   81.350  1.00 44.68 ? 761 HOH A O   1 
HETATM 3093 O  O   . HOH D 4 .   ? 7.523   -10.093 89.557  1.00 46.81 ? 762 HOH A O   1 
HETATM 3094 O  O   . HOH D 4 .   ? 6.082   7.669   59.484  1.00 42.14 ? 763 HOH A O   1 
HETATM 3095 O  O   . HOH D 4 .   ? 29.322  -7.277  60.678  1.00 50.88 ? 764 HOH A O   1 
HETATM 3096 O  O   . HOH D 4 .   ? 28.604  -13.636 79.456  1.00 52.66 ? 765 HOH A O   1 
HETATM 3097 O  O   . HOH D 4 .   ? -10.236 6.522   78.997  1.00 44.42 ? 766 HOH A O   1 
HETATM 3098 O  O   . HOH D 4 .   ? -10.043 -10.220 61.244  1.00 24.07 ? 767 HOH A O   1 
HETATM 3099 O  O   . HOH D 4 .   ? -5.724  -22.126 82.976  1.00 56.39 ? 768 HOH A O   1 
HETATM 3100 O  O   . HOH D 4 .   ? 26.294  -8.386  69.895  1.00 47.34 ? 769 HOH A O   1 
HETATM 3101 O  O   . HOH D 4 .   ? 22.388  -6.145  71.114  1.00 32.45 ? 770 HOH A O   1 
HETATM 3102 O  O   . HOH D 4 .   ? -1.652  12.894  60.977  1.00 33.26 ? 771 HOH A O   1 
HETATM 3103 O  O   . HOH D 4 .   ? 15.728  -2.297  58.550  1.00 53.75 ? 772 HOH A O   1 
HETATM 3104 O  O   . HOH D 4 .   ? 4.002   -22.033 66.877  1.00 30.40 ? 773 HOH A O   1 
HETATM 3105 O  O   . HOH D 4 .   ? 4.636   -12.966 42.888  1.00 45.35 ? 774 HOH A O   1 
HETATM 3106 O  O   . HOH D 4 .   ? -4.793  1.761   83.332  1.00 37.86 ? 775 HOH A O   1 
HETATM 3107 O  O   . HOH D 4 .   ? 8.311   -7.237  90.131  1.00 49.27 ? 776 HOH A O   1 
HETATM 3108 O  O   . HOH D 4 .   ? -8.897  -2.362  50.313  1.00 37.24 ? 777 HOH A O   1 
HETATM 3109 O  O   . HOH D 4 .   ? 14.637  0.524   63.229  1.00 51.44 ? 778 HOH A O   1 
HETATM 3110 O  O   . HOH D 4 .   ? 0.612   -3.882  96.026  1.00 65.48 ? 779 HOH A O   1 
HETATM 3111 O  O   . HOH D 4 .   ? 2.198   14.984  60.715  1.00 42.93 ? 780 HOH A O   1 
HETATM 3112 O  O   . HOH D 4 .   ? 7.475   -13.304 46.211  1.00 41.36 ? 781 HOH A O   1 
HETATM 3113 O  O   . HOH D 4 .   ? 18.905  -1.365  63.098  1.00 49.13 ? 782 HOH A O   1 
HETATM 3114 O  O   . HOH D 4 .   ? 23.709  1.827   70.995  1.00 64.35 ? 783 HOH A O   1 
HETATM 3115 O  O   . HOH D 4 .   ? 13.721  -25.331 78.560  1.00 60.38 ? 784 HOH A O   1 
HETATM 3116 O  O   . HOH D 4 .   ? -9.645  -17.818 59.870  1.00 37.81 ? 785 HOH A O   1 
HETATM 3117 O  O   . HOH D 4 .   ? 23.310  3.415   68.078  1.00 63.27 ? 786 HOH A O   1 
HETATM 3118 O  O   . HOH D 4 .   ? 12.475  -25.401 82.363  1.00 42.01 ? 787 HOH A O   1 
HETATM 3119 O  O   . HOH D 4 .   ? 15.361  -25.431 76.742  1.00 45.60 ? 788 HOH A O   1 
HETATM 3120 O  O   . HOH D 4 .   ? 6.746   -21.344 76.933  1.00 48.04 ? 789 HOH A O   1 
HETATM 3121 O  O   . HOH D 4 .   ? 19.557  -18.044 47.162  1.00 49.07 ? 790 HOH A O   1 
HETATM 3122 O  O   . HOH D 4 .   ? 10.262  -19.155 48.381  1.00 49.70 ? 791 HOH A O   1 
HETATM 3123 O  O   . HOH D 4 .   ? 2.151   -22.742 77.444  1.00 42.13 ? 792 HOH A O   1 
HETATM 3124 O  O   . HOH D 4 .   ? 24.651  4.328   69.702  1.00 69.23 ? 793 HOH A O   1 
# 
