data_8X69
# 
_entry.id   8X69 
# 
_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   8X69         pdb_00008x69 10.2210/pdb8x69/pdb 
WWPDB D_1300042718 ?            ?                   
# 
_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       2024-11-20 
# 
_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                        8X69 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-20 
_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 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              2802793197@qq.com 
_pdbx_contact_author.name_first         JIN 
_pdbx_contact_author.name_last          DONG 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   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 YH23010' 
_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 
'4-(2-fluoranylethyl)-1,6-dimethyl-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-3~{H}-1,4-benzodiazepine-2,5-dione' 
388.390   1   ?          ? ? ? 
4 water       nat water 18.015    148 ?          ? ? ? 
# 
_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 '4-(2-fluoranylethyl)-1,6-dimethyl-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-3~{H}-1,4-benzodiazepine-2,5-dione' 
YDF 
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 
YDF non-polymer         . 
'4-(2-fluoranylethyl)-1,6-dimethyl-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-3~{H}-1,4-benzodiazepine-2,5-dione' ? 
'C20 H21 F N2 O5' 388.390 
# 
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 225 253 253 PHE PHE A . n 
A 1 226 THR 226 254 254 THR THR 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 YDF 1   502 501 YDF LIG A . 
D 4 HOH 1   601 50  HOH HOH A . 
D 4 HOH 2   602 116 HOH HOH A . 
D 4 HOH 3   603 24  HOH HOH A . 
D 4 HOH 4   604 79  HOH HOH A . 
D 4 HOH 5   605 130 HOH HOH A . 
D 4 HOH 6   606 82  HOH HOH A . 
D 4 HOH 7   607 123 HOH HOH A . 
D 4 HOH 8   608 98  HOH HOH A . 
D 4 HOH 9   609 143 HOH HOH A . 
D 4 HOH 10  610 55  HOH HOH A . 
D 4 HOH 11  611 108 HOH HOH A . 
D 4 HOH 12  612 52  HOH HOH A . 
D 4 HOH 13  613 107 HOH HOH A . 
D 4 HOH 14  614 90  HOH HOH A . 
D 4 HOH 15  615 43  HOH HOH A . 
D 4 HOH 16  616 138 HOH HOH A . 
D 4 HOH 17  617 48  HOH HOH A . 
D 4 HOH 18  618 42  HOH HOH A . 
D 4 HOH 19  619 28  HOH HOH A . 
D 4 HOH 20  620 37  HOH HOH A . 
D 4 HOH 21  621 62  HOH HOH A . 
D 4 HOH 22  622 18  HOH HOH A . 
D 4 HOH 23  623 1   HOH HOH A . 
D 4 HOH 24  624 22  HOH HOH A . 
D 4 HOH 25  625 87  HOH HOH A . 
D 4 HOH 26  626 3   HOH HOH A . 
D 4 HOH 27  627 19  HOH HOH A . 
D 4 HOH 28  628 97  HOH HOH A . 
D 4 HOH 29  629 106 HOH HOH A . 
D 4 HOH 30  630 20  HOH HOH A . 
D 4 HOH 31  631 13  HOH HOH A . 
D 4 HOH 32  632 145 HOH HOH A . 
D 4 HOH 33  633 95  HOH HOH A . 
D 4 HOH 34  634 63  HOH HOH A . 
D 4 HOH 35  635 35  HOH HOH A . 
D 4 HOH 36  636 54  HOH HOH A . 
D 4 HOH 37  637 6   HOH HOH A . 
D 4 HOH 38  638 26  HOH HOH A . 
D 4 HOH 39  639 76  HOH HOH A . 
D 4 HOH 40  640 101 HOH HOH A . 
D 4 HOH 41  641 100 HOH HOH A . 
D 4 HOH 42  642 16  HOH HOH A . 
D 4 HOH 43  643 9   HOH HOH A . 
D 4 HOH 44  644 39  HOH HOH A . 
D 4 HOH 45  645 89  HOH HOH A . 
D 4 HOH 46  646 126 HOH HOH A . 
D 4 HOH 47  647 44  HOH HOH A . 
D 4 HOH 48  648 112 HOH HOH A . 
D 4 HOH 49  649 12  HOH HOH A . 
D 4 HOH 50  650 11  HOH HOH A . 
D 4 HOH 51  651 150 HOH HOH A . 
D 4 HOH 52  652 67  HOH HOH A . 
D 4 HOH 53  653 23  HOH HOH A . 
D 4 HOH 54  654 69  HOH HOH A . 
D 4 HOH 55  655 8   HOH HOH A . 
D 4 HOH 56  656 86  HOH HOH A . 
D 4 HOH 57  657 33  HOH HOH A . 
D 4 HOH 58  658 73  HOH HOH A . 
D 4 HOH 59  659 57  HOH HOH A . 
D 4 HOH 60  660 30  HOH HOH A . 
D 4 HOH 61  661 84  HOH HOH A . 
D 4 HOH 62  662 109 HOH HOH A . 
D 4 HOH 63  663 14  HOH HOH A . 
D 4 HOH 64  664 99  HOH HOH A . 
D 4 HOH 65  665 121 HOH HOH A . 
D 4 HOH 66  666 49  HOH HOH A . 
D 4 HOH 67  667 70  HOH HOH A . 
D 4 HOH 68  668 94  HOH HOH A . 
D 4 HOH 69  669 36  HOH HOH A . 
D 4 HOH 70  670 10  HOH HOH A . 
D 4 HOH 71  671 88  HOH HOH A . 
D 4 HOH 72  672 80  HOH HOH A . 
D 4 HOH 73  673 136 HOH HOH A . 
D 4 HOH 74  674 137 HOH HOH A . 
D 4 HOH 75  675 96  HOH HOH A . 
D 4 HOH 76  676 41  HOH HOH A . 
D 4 HOH 77  677 110 HOH HOH A . 
D 4 HOH 78  678 31  HOH HOH A . 
D 4 HOH 79  679 32  HOH HOH A . 
D 4 HOH 80  680 46  HOH HOH A . 
D 4 HOH 81  681 147 HOH HOH A . 
D 4 HOH 82  682 38  HOH HOH A . 
D 4 HOH 83  683 45  HOH HOH A . 
D 4 HOH 84  684 65  HOH HOH A . 
D 4 HOH 85  685 71  HOH HOH A . 
D 4 HOH 86  686 61  HOH HOH A . 
D 4 HOH 87  687 74  HOH HOH A . 
D 4 HOH 88  688 113 HOH HOH A . 
D 4 HOH 89  689 115 HOH HOH A . 
D 4 HOH 90  690 53  HOH HOH A . 
D 4 HOH 91  691 104 HOH HOH A . 
D 4 HOH 92  692 5   HOH HOH A . 
D 4 HOH 93  693 111 HOH HOH A . 
D 4 HOH 94  694 40  HOH HOH A . 
D 4 HOH 95  695 127 HOH HOH A . 
D 4 HOH 96  696 34  HOH HOH A . 
D 4 HOH 97  697 146 HOH HOH A . 
D 4 HOH 98  698 21  HOH HOH A . 
D 4 HOH 99  699 114 HOH HOH A . 
D 4 HOH 100 700 105 HOH HOH A . 
D 4 HOH 101 701 77  HOH HOH A . 
D 4 HOH 102 702 51  HOH HOH A . 
D 4 HOH 103 703 78  HOH HOH A . 
D 4 HOH 104 704 17  HOH HOH A . 
D 4 HOH 105 705 56  HOH HOH A . 
D 4 HOH 106 706 27  HOH HOH A . 
D 4 HOH 107 707 117 HOH HOH A . 
D 4 HOH 108 708 25  HOH HOH A . 
D 4 HOH 109 709 2   HOH HOH A . 
D 4 HOH 110 710 75  HOH HOH A . 
D 4 HOH 111 711 128 HOH HOH A . 
D 4 HOH 112 712 85  HOH HOH A . 
D 4 HOH 113 713 133 HOH HOH A . 
D 4 HOH 114 714 68  HOH HOH A . 
D 4 HOH 115 715 129 HOH HOH A . 
D 4 HOH 116 716 83  HOH HOH A . 
D 4 HOH 117 717 64  HOH HOH A . 
D 4 HOH 118 718 47  HOH HOH A . 
D 4 HOH 119 719 142 HOH HOH A . 
D 4 HOH 120 720 72  HOH HOH A . 
D 4 HOH 121 721 103 HOH HOH A . 
D 4 HOH 122 722 4   HOH HOH A . 
D 4 HOH 123 723 29  HOH HOH A . 
D 4 HOH 124 724 149 HOH HOH A . 
D 4 HOH 125 725 15  HOH HOH A . 
D 4 HOH 126 726 118 HOH HOH A . 
D 4 HOH 127 727 7   HOH HOH A . 
D 4 HOH 128 728 59  HOH HOH A . 
D 4 HOH 129 729 131 HOH HOH A . 
D 4 HOH 130 730 144 HOH HOH A . 
D 4 HOH 131 731 141 HOH HOH A . 
D 4 HOH 132 732 58  HOH HOH A . 
D 4 HOH 133 733 139 HOH HOH A . 
D 4 HOH 134 734 92  HOH HOH A . 
D 4 HOH 135 735 125 HOH HOH A . 
D 4 HOH 136 736 60  HOH HOH A . 
D 4 HOH 137 737 140 HOH HOH A . 
D 4 HOH 138 738 93  HOH HOH A . 
D 4 HOH 139 739 119 HOH HOH A . 
D 4 HOH 140 740 124 HOH HOH A . 
D 4 HOH 141 741 132 HOH HOH A . 
D 4 HOH 142 742 120 HOH HOH A . 
D 4 HOH 143 743 66  HOH HOH A . 
D 4 HOH 144 744 102 HOH HOH A . 
D 4 HOH 145 745 134 HOH HOH A . 
D 4 HOH 146 746 135 HOH HOH A . 
D 4 HOH 147 747 81  HOH HOH A . 
D 4 HOH 148 748 91  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 252 ? CG  ? A GLU 224 CG  
18 1 Y 1 A GLU 252 ? CD  ? A GLU 224 CD  
19 1 Y 1 A GLU 252 ? OE1 ? A GLU 224 OE1 
20 1 Y 1 A GLU 252 ? OE2 ? A GLU 224 OE2 
21 1 Y 1 A PHE 253 ? CG  ? A PHE 225 CG  
22 1 Y 1 A PHE 253 ? CD1 ? A PHE 225 CD1 
23 1 Y 1 A PHE 253 ? CD2 ? A PHE 225 CD2 
24 1 Y 1 A PHE 253 ? CE1 ? A PHE 225 CE1 
25 1 Y 1 A PHE 253 ? CE2 ? A PHE 225 CE2 
26 1 Y 1 A PHE 253 ? CZ  ? A PHE 225 CZ  
27 1 Y 1 A GLU 262 ? CG  ? A GLU 234 CG  
28 1 Y 1 A GLU 262 ? CD  ? A GLU 234 CD  
29 1 Y 1 A GLU 262 ? OE1 ? A GLU 234 OE1 
30 1 Y 1 A GLU 262 ? OE2 ? A GLU 234 OE2 
31 1 Y 1 A LYS 289 ? CG  ? A LYS 261 CG  
32 1 Y 1 A LYS 289 ? CD  ? A LYS 261 CD  
33 1 Y 1 A LYS 289 ? CE  ? A LYS 261 CE  
34 1 Y 1 A LYS 289 ? NZ  ? A LYS 261 NZ  
35 1 Y 1 A ARG 290 ? CG  ? A ARG 262 CG  
36 1 Y 1 A ARG 290 ? CD  ? A ARG 262 CD  
37 1 Y 1 A ARG 290 ? NE  ? A ARG 262 NE  
38 1 Y 1 A ARG 290 ? CZ  ? A ARG 262 CZ  
39 1 Y 1 A ARG 290 ? NH1 ? A ARG 262 NH1 
40 1 Y 1 A ARG 290 ? NH2 ? A ARG 262 NH2 
41 1 Y 1 A GLN 344 ? CG  ? A GLN 316 CG  
42 1 Y 1 A GLN 344 ? CD  ? A GLN 316 CD  
43 1 Y 1 A GLN 344 ? OE1 ? A GLN 316 OE1 
44 1 Y 1 A GLN 344 ? NE2 ? A GLN 316 NE2 
45 1 Y 1 A LYS 348 ? CG  ? A LYS 320 CG  
46 1 Y 1 A LYS 348 ? CD  ? A LYS 320 CD  
47 1 Y 1 A LYS 348 ? CE  ? A LYS 320 CE  
48 1 Y 1 A LYS 348 ? NZ  ? A LYS 320 NZ  
49 1 Y 1 A LYS 360 ? CG  ? A LYS 332 CG  
50 1 Y 1 A LYS 360 ? CD  ? A LYS 332 CD  
51 1 Y 1 A LYS 360 ? CE  ? A LYS 332 CE  
52 1 Y 1 A LYS 360 ? NZ  ? A LYS 332 NZ  
53 1 Y 1 A GLN 374 ? CG  ? A GLN 346 CG  
54 1 Y 1 A GLN 374 ? CD  ? A GLN 346 CD  
55 1 Y 1 A GLN 374 ? OE1 ? A GLN 346 OE1 
56 1 Y 1 A GLN 374 ? NE2 ? A GLN 346 NE2 
57 1 Y 1 A PHE 428 ? CG  ? A PHE 400 CG  
58 1 Y 1 A PHE 428 ? CD1 ? A PHE 400 CD1 
59 1 Y 1 A PHE 428 ? CD2 ? A PHE 400 CD2 
60 1 Y 1 A PHE 428 ? CE1 ? A PHE 400 CE1 
61 1 Y 1 A PHE 428 ? CE2 ? A PHE 400 CE2 
62 1 Y 1 A PHE 428 ? CZ  ? A PHE 400 CZ  
63 1 Y 1 A LYS 429 ? CG  ? A LYS 401 CG  
64 1 Y 1 A LYS 429 ? CD  ? A LYS 401 CD  
65 1 Y 1 A LYS 429 ? CE  ? A LYS 401 CE  
66 1 Y 1 A LYS 429 ? NZ  ? A LYS 401 NZ  
67 1 Y 1 A GLU 432 ? CG  ? A GLU 404 CG  
68 1 Y 1 A GLU 432 ? CD  ? A GLU 404 CD  
69 1 Y 1 A GLU 432 ? OE1 ? A GLU 404 OE1 
70 1 Y 1 A GLU 432 ? OE2 ? A GLU 404 OE2 
71 1 Y 1 A GLU 433 ? CG  ? A GLU 405 CG  
72 1 Y 1 A GLU 433 ? CD  ? A GLU 405 CD  
73 1 Y 1 A GLU 433 ? OE1 ? A GLU 405 OE1 
74 1 Y 1 A GLU 433 ? OE2 ? A GLU 405 OE2 
75 1 Y 1 A GLU 435 ? CG  ? A GLU 407 CG  
76 1 Y 1 A GLU 435 ? CD  ? A GLU 407 CD  
77 1 Y 1 A GLU 435 ? OE1 ? A GLU 407 OE1 
78 1 Y 1 A GLU 435 ? OE2 ? A GLU 407 OE2 
79 1 Y 1 A LYS 436 ? CG  ? A LYS 408 CG  
80 1 Y 1 A LYS 436 ? CD  ? A LYS 408 CD  
81 1 Y 1 A LYS 436 ? CE  ? A LYS 408 CE  
82 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                   101.92 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8X69 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.792 
_cell.length_a_esd                 ? 
_cell.length_b                     83.448 
_cell.length_b_esd                 ? 
_cell.length_c                     61.663 
_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                         8X69 
_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                   8X69 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.52 
_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         2023-05-02 
_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                                       8X69 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.796 
_reflns.d_resolution_low                               30.167 
_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                                     35332 
_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                           97.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.18 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.60 
_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                             10833 
_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                                  0.875 
_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                                 8X69 
_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                             30.167 
_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                     35332 
_refine.ls_number_reflns_R_free                  1767 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.48 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1840 
_refine.ls_R_factor_R_free                       0.2163 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1824 
_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                 24.11 
_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                            0.21 
_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                        30.167 
_refine_hist.number_atoms_solvent             148 
_refine_hist.number_atoms_total               3070 
_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        2893 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_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  ? 3001 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.086  ? 4070 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.748 ? 1774 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.057  ? 445  ? 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' 1.7960 1.8445 . . 130 2468 96.00  . . . . 0.2810 . . . . . . . . . . . 0.3288 
'X-RAY DIFFRACTION' 1.8445 1.8988 . . 136 2598 100.00 . . . . 0.2418 . . . . . . . . . . . 0.3119 
'X-RAY DIFFRACTION' 1.8988 1.9601 . . 135 2558 100.00 . . . . 0.2186 . . . . . . . . . . . 0.2426 
'X-RAY DIFFRACTION' 1.9601 2.0301 . . 136 2586 100.00 . . . . 0.2022 . . . . . . . . . . . 0.2620 
'X-RAY DIFFRACTION' 2.0301 2.1114 . . 136 2577 100.00 . . . . 0.1929 . . . . . . . . . . . 0.2245 
'X-RAY DIFFRACTION' 2.1114 2.2075 . . 136 2594 100.00 . . . . 0.1905 . . . . . . . . . . . 0.2182 
'X-RAY DIFFRACTION' 2.2075 2.3238 . . 135 2550 100.00 . . . . 0.1804 . . . . . . . . . . . 0.2185 
'X-RAY DIFFRACTION' 2.3238 2.4693 . . 138 2635 100.00 . . . . 0.1935 . . . . . . . . . . . 0.2317 
'X-RAY DIFFRACTION' 2.4693 2.6599 . . 135 2567 100.00 . . . . 0.1892 . . . . . . . . . . . 0.2397 
'X-RAY DIFFRACTION' 2.6599 2.9274 . . 136 2583 100.00 . . . . 0.1841 . . . . . . . . . . . 0.2364 
'X-RAY DIFFRACTION' 2.9274 3.3505 . . 138 2616 100.00 . . . . 0.1769 . . . . . . . . . . . 0.1994 
'X-RAY DIFFRACTION' 3.3505 4.2194 . . 136 2590 100.00 . . . . 0.1584 . . . . . . . . . . . 0.1670 
'X-RAY DIFFRACTION' 4.2194 30.167 . . 140 2643 99.00  . . . . 0.1713 . . . . . . . . . . . 0.2148 
# 
_struct.entry_id                     8X69 
_struct.title                        'Complex structure of AtHPPD with YH23010' 
_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        8X69 
_struct_keywords.text            'Inhibiton, Complex, 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              8X69 
_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 8X69 GLY A 1 ? UNP P93836 ? ? 'expression tag' 29 1 
1 8X69 SER A 2 ? UNP P93836 ? ? 'expression tag' 30 2 
1 8X69 HIS A 3 ? UNP P93836 ? ? 'expression tag' 31 3 
1 8X69 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)' 3270  ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  28330 ? 
# 
_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 -25.4724595487 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 120.6667148825 
# 
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 ? GLY A 323 ? PRO A 339 GLY A 351 1 ? 13 
HELX_P HELX_P12 AB3 SER A 327 ? GLY A 338 ? SER A 355 GLY A 366 1 ? 12 
HELX_P HELX_P13 AB4 GLY A 394 ? LYS A 408 ? GLY A 422 LYS A 436 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 373 SG  ? ? ? 1_555 A CYS 388 SG  ? ? A CYS 401 A CYS 416 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc1 metalc ? ? A HIS 198 NE2 ? ? ? 1_555 B CO  .   CO  ? ? A HIS 226 A CO  501 1_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc2 metalc ? ? A HIS 280 NE2 ? ? ? 1_555 B CO  .   CO  ? ? A HIS 308 A CO  501 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc3 metalc ? ? A GLU 366 OE1 ? ? ? 1_555 B CO  .   CO  ? ? A GLU 394 A CO  501 1_555 ? ? ? ? ? ? ? 2.158 ? ? 
metalc4 metalc ? ? B CO  .   CO  ? ? ? 1_555 C YDF .   O15 ? ? A CO  501 A YDF 502 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc5 metalc ? ? B CO  .   CO  ? ? ? 1_555 C YDF .   O21 ? ? A CO  501 A YDF 502 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc6 metalc ? ? B CO  .   CO  ? ? ? 1_555 D HOH .   O   ? ? A CO  501 A HOH 623 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
# 
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_555 101.0 ? 
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 99.0  ? 
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 85.1  ? 
4  NE2 ? A HIS 198 ? A HIS 226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O15 ? C YDF .   ? A YDF 502 ? 1_555 160.6 ? 
5  NE2 ? A HIS 280 ? A HIS 308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O15 ? C YDF .   ? A YDF 502 ? 1_555 92.1  ? 
6  OE1 ? A GLU 366 ? A GLU 394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O15 ? C YDF .   ? A YDF 502 ? 1_555 96.4  ? 
7  NE2 ? A HIS 198 ? A HIS 226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O21 ? C YDF .   ? A YDF 502 ? 1_555 85.0  ? 
8  NE2 ? A HIS 280 ? A HIS 308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O21 ? C YDF .   ? A YDF 502 ? 1_555 94.1  ? 
9  OE1 ? A GLU 366 ? A GLU 394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O21 ? C YDF .   ? A YDF 502 ? 1_555 176.0 ? 
10 O15 ? C YDF .   ? A YDF 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O21 ? C YDF .   ? A YDF 502 ? 1_555 79.8  ? 
11 NE2 ? A HIS 198 ? A HIS 226 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH .   ? A HOH 623 ? 1_555 86.7  ? 
12 NE2 ? A HIS 280 ? A HIS 308 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH .   ? A HOH 623 ? 1_555 169.1 ? 
13 OE1 ? A GLU 366 ? A GLU 394 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH .   ? A HOH 623 ? 1_555 86.0  ? 
14 O15 ? C YDF .   ? A YDF 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH .   ? A HOH 623 ? 1_555 82.6  ? 
15 O21 ? C YDF .   ? A YDF 502 ? 1_555 CO ? B CO . ? A CO 501 ? 1_555 O   ? D HOH .   ? A HOH 623 ? 1_555 94.4  ? 
# 
_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 ? PHE A 225 ? HIS A 248 PHE A 253 
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 158 ? O VAL A 186 N ARG A 112 ? N ARG A 140 
AA1 4 5 O GLU A 117 ? O GLU A 145 N ARG A 18  ? N ARG A 46  
AA1 5 6 N PHE A 24  ? N PHE A 52  O LEU A 70  ? O LEU A 98  
AA1 6 7 O PHE A 69  ? O PHE A 97  N LEU A 62  ? N LEU A 90  
AA1 7 8 O LEU A 61  ? O LEU A 89  N SER A 45  ? N SER A 73  
AA1 8 9 N LYS A 47  ? N LYS A 75  O GLU A 179 ? O GLU A 207 
AA2 1 2 N PHE A 222 ? N PHE A 250 O VAL A 241 ? O VAL A 269 
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 VAL A 200 ? N VAL A 228 O GLN A 279 ? O GLN A 307 
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                   8X69 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 45  ? ? -104.42 -80.28  
2  1 ASP A 77  ? ? -162.80 -167.89 
3  1 ALA A 173 ? ? -143.58 -37.94  
4  1 LEU A 181 ? ? -103.88 -64.97  
5  1 ASP A 218 ? ? -163.35 112.96  
6  1 THR A 288 ? ? -110.90 -162.80 
7  1 LYS A 289 ? ? -93.62  -79.46  
8  1 ASP A 315 ? ? -163.23 85.20   
9  1 ASP A 372 ? ? -110.09 -159.65 
10 1 THR A 390 ? ? -126.15 -93.59  
11 1 CYS A 416 ? ? -54.61  109.37  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 29  ? A GLY 1   
2  1 Y 1 A SER 30  ? A SER 2   
3  1 Y 1 A HIS 31  ? A HIS 3   
4  1 Y 1 A MET 32  ? A MET 4   
5  1 Y 1 A VAL 33  ? A VAL 5   
6  1 Y 1 A ARG 34  ? A ARG 6   
7  1 Y 1 A GLU 195 ? A GLU 167 
8  1 Y 1 A ASP 196 ? A ASP 168 
9  1 Y 1 A THR 197 ? A THR 169 
10 1 Y 1 A GLU 198 ? A GLU 170 
11 1 Y 1 A LYS 199 ? A LYS 171 
12 1 Y 1 A SER 200 ? A SER 172 
13 1 Y 1 A ALA 255 ? A ALA 227 
14 1 Y 1 A ASP 256 ? A ASP 228 
15 1 Y 1 A ASP 257 ? A ASP 229 
16 1 Y 1 A VAL 258 ? A VAL 230 
17 1 Y 1 A GLY 259 ? A GLY 231 
18 1 Y 1 A THR 260 ? A THR 232 
19 1 Y 1 A ALA 261 ? A ALA 233 
20 1 Y 1 A LYS 404 ? A LYS 376 
21 1 Y 1 A ASP 405 ? A ASP 377 
22 1 Y 1 A GLU 406 ? A GLU 378 
23 1 Y 1 A GLU 407 ? A GLU 379 
24 1 Y 1 A GLY 408 ? A GLY 380 
25 1 Y 1 A LYS 409 ? A LYS 381 
26 1 Y 1 A ALA 410 ? A ALA 382 
27 1 Y 1 A THR 437 ? A THR 409 
28 1 Y 1 A LEU 438 ? A LEU 410 
29 1 Y 1 A GLU 439 ? A GLU 411 
30 1 Y 1 A ALA 440 ? A ALA 412 
31 1 Y 1 A LYS 441 ? A LYS 413 
32 1 Y 1 A GLN 442 ? A GLN 414 
33 1 Y 1 A LEU 443 ? A LEU 415 
34 1 Y 1 A VAL 444 ? A VAL 416 
35 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 
YDF C13  C  N N 392 
YDF C17  C  N N 393 
YDF C20  C  N N 394 
YDF C24  C  N N 395 
YDF C26  C  N N 396 
YDF C01  C  Y N 397 
YDF C02  C  Y N 398 
YDF C03  C  Y N 399 
YDF C04  C  Y N 400 
YDF C05  C  Y N 401 
YDF C06  C  Y N 402 
YDF C08  C  N N 403 
YDF C09  C  N N 404 
YDF C11  C  N N 405 
YDF C12  C  N N 406 
YDF C14  C  N N 407 
YDF C16  C  N N 408 
YDF C18  C  N N 409 
YDF C19  C  N N 410 
YDF C27  C  N N 411 
YDF F28  F  N N 412 
YDF N07  N  N N 413 
YDF N10  N  N N 414 
YDF O15  O  N N 415 
YDF O21  O  N N 416 
YDF O22  O  N N 417 
YDF O23  O  N N 418 
YDF O25  O  N N 419 
YDF H1   H  N N 420 
YDF H2   H  N N 421 
YDF H3   H  N N 422 
YDF H4   H  N N 423 
YDF H5   H  N N 424 
YDF H6   H  N N 425 
YDF H7   H  N N 426 
YDF H8   H  N N 427 
YDF H9   H  N N 428 
YDF H11  H  N N 429 
YDF H12  H  N N 430 
YDF H13  H  N N 431 
YDF H14  H  N N 432 
YDF H17  H  N N 433 
YDF H18  H  N N 434 
YDF H19  H  N N 435 
YDF H20  H  N N 436 
YDF H21  H  N N 437 
YDF H22  H  N N 438 
YDF H24  H  N N 439 
YDF H10  H  N N 440 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
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 
YDF C13 C01  sing N N 376 
YDF C13 C14  sing N N 377 
YDF C13 O15  doub N N 378 
YDF C17 C16  sing N N 379 
YDF C17 C18  sing N N 380 
YDF C20 C14  sing N N 381 
YDF C20 C19  sing N N 382 
YDF C20 O22  doub N N 383 
YDF C24 C27  sing N N 384 
YDF C24 N10  sing N N 385 
YDF C26 N07  sing N N 386 
YDF C01 C02  doub Y N 387 
YDF C01 C06  sing Y N 388 
YDF C02 C03  sing Y N 389 
YDF C03 C04  doub Y N 390 
YDF C04 C05  sing Y N 391 
YDF C04 N07  sing N N 392 
YDF C05 C06  doub Y N 393 
YDF C05 C11  sing N N 394 
YDF C06 C12  sing N N 395 
YDF C08 C09  sing N N 396 
YDF C08 O25  doub N N 397 
YDF C09 N10  sing N N 398 
YDF C11 N10  sing N N 399 
YDF C11 O23  doub N N 400 
YDF C14 C16  doub N N 401 
YDF C16 O21  sing N N 402 
YDF C18 C19  sing N N 403 
YDF C27 F28  sing N N 404 
YDF C17 H1   sing N N 405 
YDF C17 H2   sing N N 406 
YDF C24 H3   sing N N 407 
YDF C24 H4   sing N N 408 
YDF C26 H5   sing N N 409 
YDF C26 H6   sing N N 410 
YDF C26 H7   sing N N 411 
YDF C02 H8   sing N N 412 
YDF C03 H9   sing N N 413 
YDF C09 H11  sing N N 414 
YDF C12 H12  sing N N 415 
YDF C12 H13  sing N N 416 
YDF C12 H14  sing N N 417 
YDF C18 H17  sing N N 418 
YDF C18 H18  sing N N 419 
YDF C19 H19  sing N N 420 
YDF C19 H20  sing N N 421 
YDF C27 H21  sing N N 422 
YDF C27 H22  sing N N 423 
YDF O21 H24  sing N N 424 
YDF C08 N07  sing N N 425 
YDF C09 H10  sing N N 426 
# 
_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                    8X69 
_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]   0.013022 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002748 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011984 
_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]   0.016574 
_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   ? 21.728  -5.377  86.471  1.00 60.44 ? 35  LYS A N   1 
ATOM   2    C  CA  . LYS A 1 7   ? 22.817  -5.969  85.699  1.00 55.33 ? 35  LYS A CA  1 
ATOM   3    C  C   . LYS A 1 7   ? 22.316  -6.489  84.352  1.00 56.61 ? 35  LYS A C   1 
ATOM   4    O  O   . LYS A 1 7   ? 21.210  -7.031  84.255  1.00 56.71 ? 35  LYS A O   1 
ATOM   5    C  CB  . LYS A 1 7   ? 23.481  -7.095  86.488  1.00 56.31 ? 35  LYS A CB  1 
ATOM   6    N  N   . ASN A 1 8   ? 23.134  -6.305  83.317  1.00 53.17 ? 36  ASN A N   1 
ATOM   7    C  CA  . ASN A 1 8   ? 22.817  -6.736  81.956  1.00 47.00 ? 36  ASN A CA  1 
ATOM   8    C  C   . ASN A 1 8   ? 23.957  -7.621  81.475  1.00 47.68 ? 36  ASN A C   1 
ATOM   9    O  O   . ASN A 1 8   ? 25.006  -7.107  81.048  1.00 50.27 ? 36  ASN A O   1 
ATOM   10   C  CB  . ASN A 1 8   ? 22.613  -5.537  81.029  1.00 48.04 ? 36  ASN A CB  1 
ATOM   11   C  CG  . ASN A 1 8   ? 22.416  -5.933  79.562  1.00 45.52 ? 36  ASN A CG  1 
ATOM   12   O  OD1 . ASN A 1 8   ? 22.365  -7.119  79.218  1.00 41.39 ? 36  ASN A OD1 1 
ATOM   13   N  ND2 . ASN A 1 8   ? 22.288  -4.927  78.692  1.00 40.66 ? 36  ASN A ND2 1 
ATOM   14   N  N   . PRO A 1 9   ? 23.789  -8.946  81.512  1.00 44.70 ? 37  PRO A N   1 
ATOM   15   C  CA  . PRO A 1 9   ? 24.874  -9.852  81.116  1.00 44.14 ? 37  PRO A CA  1 
ATOM   16   C  C   . PRO A 1 9   ? 25.107  -9.939  79.615  1.00 48.86 ? 37  PRO A C   1 
ATOM   17   O  O   . PRO A 1 9   ? 26.057  -10.613 79.199  1.00 49.13 ? 37  PRO A O   1 
ATOM   18   C  CB  . PRO A 1 9   ? 24.403  -11.202 81.671  1.00 47.27 ? 37  PRO A CB  1 
ATOM   19   C  CG  . PRO A 1 9   ? 22.912  -11.107 81.622  1.00 45.49 ? 37  PRO A CG  1 
ATOM   20   C  CD  . PRO A 1 9   ? 22.583  -9.676  81.944  1.00 46.06 ? 37  PRO A CD  1 
ATOM   21   N  N   . LYS A 1 10  ? 24.269  -9.289  78.809  1.00 42.96 ? 38  LYS A N   1 
ATOM   22   C  CA  . LYS A 1 10  ? 24.400  -9.240  77.353  1.00 38.80 ? 38  LYS A CA  1 
ATOM   23   C  C   . LYS A 1 10  ? 24.673  -10.625 76.764  1.00 39.23 ? 38  LYS A C   1 
ATOM   24   O  O   . LYS A 1 10  ? 25.690  -10.876 76.117  1.00 41.70 ? 38  LYS A O   1 
ATOM   25   C  CB  . LYS A 1 10  ? 25.476  -8.237  76.941  1.00 45.45 ? 38  LYS A CB  1 
ATOM   26   C  CG  . LYS A 1 10  ? 25.142  -6.804  77.340  1.00 45.40 ? 38  LYS A CG  1 
ATOM   27   C  CD  . LYS A 1 10  ? 25.834  -5.797  76.433  1.00 48.56 ? 38  LYS A CD  1 
ATOM   28   C  CE  . LYS A 1 10  ? 25.204  -4.413  76.576  1.00 49.12 ? 38  LYS A CE  1 
ATOM   29   N  NZ  . LYS A 1 10  ? 26.009  -3.539  77.466  1.00 52.97 ? 38  LYS A NZ  1 
ATOM   30   N  N   . SER A 1 11  ? 23.712  -11.525 76.965  1.00 41.18 ? 39  SER A N   1 
ATOM   31   C  CA  . SER A 1 11  ? 23.897  -12.933 76.625  1.00 38.39 ? 39  SER A CA  1 
ATOM   32   C  C   . SER A 1 11  ? 23.126  -13.369 75.380  1.00 37.03 ? 39  SER A C   1 
ATOM   33   O  O   . SER A 1 11  ? 22.900  -14.570 75.206  1.00 35.40 ? 39  SER A O   1 
ATOM   34   C  CB  . SER A 1 11  ? 23.494  -13.813 77.807  1.00 36.93 ? 39  SER A CB  1 
ATOM   35   O  OG  . SER A 1 11  ? 22.242  -13.413 78.321  1.00 41.05 ? 39  SER A OG  1 
ATOM   36   N  N   . ASP A 1 12  ? 22.712  -12.433 74.516  1.00 36.15 ? 40  ASP A N   1 
ATOM   37   C  CA  . ASP A 1 12  ? 22.011  -12.803 73.284  1.00 36.75 ? 40  ASP A CA  1 
ATOM   38   C  C   . ASP A 1 12  ? 22.818  -13.832 72.507  1.00 39.97 ? 40  ASP A C   1 
ATOM   39   O  O   . ASP A 1 12  ? 24.006  -13.633 72.251  1.00 35.16 ? 40  ASP A O   1 
ATOM   40   C  CB  . ASP A 1 12  ? 21.781  -11.580 72.393  1.00 36.73 ? 40  ASP A CB  1 
ATOM   41   C  CG  . ASP A 1 12  ? 20.768  -10.613 72.962  1.00 31.12 ? 40  ASP A CG  1 
ATOM   42   O  OD1 . ASP A 1 12  ? 20.245  -10.868 74.066  1.00 34.82 ? 40  ASP A OD1 1 
ATOM   43   O  OD2 . ASP A 1 12  ? 20.543  -9.570  72.314  1.00 32.79 ? 40  ASP A OD2 1 
ATOM   44   N  N   . LYS A 1 13  ? 22.166  -14.927 72.117  1.00 31.44 ? 41  LYS A N   1 
ATOM   45   C  CA  . LYS A 1 13  ? 22.877  -15.977 71.400  1.00 33.94 ? 41  LYS A CA  1 
ATOM   46   C  C   . LYS A 1 13  ? 23.031  -15.679 69.916  1.00 38.31 ? 41  LYS A C   1 
ATOM   47   O  O   . LYS A 1 13  ? 23.737  -16.421 69.223  1.00 36.76 ? 41  LYS A O   1 
ATOM   48   C  CB  . LYS A 1 13  ? 22.178  -17.314 71.610  1.00 33.20 ? 41  LYS A CB  1 
ATOM   49   C  CG  . LYS A 1 13  ? 22.155  -17.741 73.067  1.00 33.27 ? 41  LYS A CG  1 
ATOM   50   C  CD  . LYS A 1 13  ? 21.558  -19.124 73.217  1.00 35.51 ? 41  LYS A CD  1 
ATOM   51   C  CE  . LYS A 1 13  ? 21.955  -19.767 74.546  1.00 46.10 ? 41  LYS A CE  1 
ATOM   52   N  NZ  . LYS A 1 13  ? 20.817  -19.984 75.487  1.00 46.82 ? 41  LYS A NZ  1 
ATOM   53   N  N   . PHE A 1 14  ? 22.402  -14.612 69.422  1.00 34.73 ? 42  PHE A N   1 
ATOM   54   C  CA  . PHE A 1 14  ? 22.598  -14.130 68.062  1.00 29.86 ? 42  PHE A CA  1 
ATOM   55   C  C   . PHE A 1 14  ? 22.367  -12.631 68.070  1.00 31.48 ? 42  PHE A C   1 
ATOM   56   O  O   . PHE A 1 14  ? 21.856  -12.075 69.040  1.00 36.01 ? 42  PHE A O   1 
ATOM   57   C  CB  . PHE A 1 14  ? 21.671  -14.830 67.068  1.00 38.12 ? 42  PHE A CB  1 
ATOM   58   C  CG  . PHE A 1 14  ? 20.276  -15.051 67.591  1.00 34.86 ? 42  PHE A CG  1 
ATOM   59   C  CD1 . PHE A 1 14  ? 19.284  -14.105 67.390  1.00 37.38 ? 42  PHE A CD1 1 
ATOM   60   C  CD2 . PHE A 1 14  ? 19.967  -16.200 68.304  1.00 34.38 ? 42  PHE A CD2 1 
ATOM   61   C  CE1 . PHE A 1 14  ? 18.001  -14.318 67.880  1.00 33.07 ? 42  PHE A CE1 1 
ATOM   62   C  CE2 . PHE A 1 14  ? 18.695  -16.416 68.799  1.00 35.85 ? 42  PHE A CE2 1 
ATOM   63   C  CZ  . PHE A 1 14  ? 17.707  -15.467 68.586  1.00 33.15 ? 42  PHE A CZ  1 
ATOM   64   N  N   . LYS A 1 15  ? 22.765  -11.975 66.981  1.00 29.76 ? 43  LYS A N   1 
ATOM   65   C  CA  . LYS A 1 15  ? 22.699  -10.521 66.899  1.00 31.19 ? 43  LYS A CA  1 
ATOM   66   C  C   . LYS A 1 15  ? 21.276  -10.087 66.552  1.00 32.39 ? 43  LYS A C   1 
ATOM   67   O  O   . LYS A 1 15  ? 20.789  -10.371 65.453  1.00 31.10 ? 43  LYS A O   1 
ATOM   68   C  CB  . LYS A 1 15  ? 23.679  -9.992  65.859  1.00 33.66 ? 43  LYS A CB  1 
ATOM   69   N  N   . VAL A 1 16  ? 20.643  -9.373  67.477  1.00 28.07 ? 44  VAL A N   1 
ATOM   70   C  CA  . VAL A 1 16  ? 19.269  -8.885  67.348  1.00 30.80 ? 44  VAL A CA  1 
ATOM   71   C  C   . VAL A 1 16  ? 19.338  -7.377  67.178  1.00 35.22 ? 44  VAL A C   1 
ATOM   72   O  O   . VAL A 1 16  ? 20.150  -6.709  67.831  1.00 35.42 ? 44  VAL A O   1 
ATOM   73   C  CB  . VAL A 1 16  ? 18.427  -9.278  68.581  1.00 28.34 ? 44  VAL A CB  1 
ATOM   74   C  CG1 . VAL A 1 16  ? 17.037  -8.603  68.560  1.00 28.74 ? 44  VAL A CG1 1 
ATOM   75   C  CG2 . VAL A 1 16  ? 18.293  -10.805 68.668  1.00 29.50 ? 44  VAL A CG2 1 
ATOM   76   N  N   . LYS A 1 17  ? 18.520  -6.838  66.278  1.00 27.53 ? 45  LYS A N   1 
ATOM   77   C  CA  . LYS A 1 17  ? 18.557  -5.399  66.061  1.00 29.08 ? 45  LYS A CA  1 
ATOM   78   C  C   . LYS A 1 17  ? 17.357  -4.729  66.711  1.00 34.52 ? 45  LYS A C   1 
ATOM   79   O  O   . LYS A 1 17  ? 17.478  -4.188  67.812  1.00 37.80 ? 45  LYS A O   1 
ATOM   80   C  CB  . LYS A 1 17  ? 18.649  -5.088  64.570  1.00 28.33 ? 45  LYS A CB  1 
ATOM   81   C  CG  . LYS A 1 17  ? 20.014  -5.476  63.993  1.00 34.92 ? 45  LYS A CG  1 
ATOM   82   C  CD  . LYS A 1 17  ? 20.006  -5.524  62.475  1.00 37.52 ? 45  LYS A CD  1 
ATOM   83   C  CE  . LYS A 1 17  ? 20.414  -4.192  61.878  1.00 43.59 ? 45  LYS A CE  1 
ATOM   84   N  NZ  . LYS A 1 17  ? 20.443  -4.263  60.384  1.00 52.78 ? 45  LYS A NZ  1 
ATOM   85   N  N   . ARG A 1 18  ? 16.195  -4.762  66.063  1.00 29.37 ? 46  ARG A N   1 
ATOM   86   C  CA  . ARG A 1 18  ? 15.038  -4.072  66.609  1.00 23.57 ? 46  ARG A CA  1 
ATOM   87   C  C   . ARG A 1 18  ? 13.783  -4.866  66.283  1.00 26.23 ? 46  ARG A C   1 
ATOM   88   O  O   . ARG A 1 18  ? 13.794  -5.763  65.444  1.00 24.25 ? 46  ARG A O   1 
ATOM   89   C  CB  . ARG A 1 18  ? 14.906  -2.656  66.048  1.00 29.44 ? 46  ARG A CB  1 
ATOM   90   C  CG  . ARG A 1 18  ? 15.996  -1.705  66.493  1.00 38.14 ? 46  ARG A CG  1 
ATOM   91   C  CD  . ARG A 1 18  ? 15.578  -0.965  67.753  1.00 39.21 ? 46  ARG A CD  1 
ATOM   92   N  NE  . ARG A 1 18  ? 16.473  0.141   68.063  1.00 42.45 ? 46  ARG A NE  1 
ATOM   93   C  CZ  . ARG A 1 18  ? 17.722  0.007   68.493  1.00 53.82 ? 46  ARG A CZ  1 
ATOM   94   N  NH1 . ARG A 1 18  ? 18.238  -1.209  68.683  1.00 44.97 ? 46  ARG A NH1 1 
ATOM   95   N  NH2 . ARG A 1 18  ? 18.458  1.084   68.747  1.00 53.73 ? 46  ARG A NH2 1 
ATOM   96   N  N   . PHE A 1 19  ? 12.699  -4.517  66.960  1.00 22.72 ? 47  PHE A N   1 
ATOM   97   C  CA  . PHE A 1 19  ? 11.385  -4.948  66.494  1.00 21.39 ? 47  PHE A CA  1 
ATOM   98   C  C   . PHE A 1 19  ? 11.216  -4.532  65.042  1.00 24.92 ? 47  PHE A C   1 
ATOM   99   O  O   . PHE A 1 19  ? 11.581  -3.414  64.655  1.00 24.06 ? 47  PHE A O   1 
ATOM   100  C  CB  . PHE A 1 19  ? 10.296  -4.320  67.357  1.00 23.98 ? 47  PHE A CB  1 
ATOM   101  C  CG  . PHE A 1 19  ? 10.065  -5.029  68.661  1.00 20.06 ? 47  PHE A CG  1 
ATOM   102  C  CD1 . PHE A 1 19  ? 9.702   -6.361  68.673  1.00 20.12 ? 47  PHE A CD1 1 
ATOM   103  C  CD2 . PHE A 1 19  ? 10.153  -4.356  69.862  1.00 23.35 ? 47  PHE A CD2 1 
ATOM   104  C  CE1 . PHE A 1 19  ? 9.462   -7.012  69.845  1.00 21.00 ? 47  PHE A CE1 1 
ATOM   105  C  CE2 . PHE A 1 19  ? 9.895   -5.019  71.048  1.00 21.63 ? 47  PHE A CE2 1 
ATOM   106  C  CZ  . PHE A 1 19  ? 9.551   -6.344  71.030  1.00 19.54 ? 47  PHE A CZ  1 
ATOM   107  N  N   . HIS A 1 20  ? 10.699  -5.447  64.224  1.00 22.75 ? 48  HIS A N   1 
ATOM   108  C  CA  . HIS A 1 20  ? 10.507  -5.173  62.806  1.00 20.71 ? 48  HIS A CA  1 
ATOM   109  C  C   . HIS A 1 20  ? 9.040   -5.019  62.435  1.00 22.82 ? 48  HIS A C   1 
ATOM   110  O  O   . HIS A 1 20  ? 8.659   -4.014  61.819  1.00 22.40 ? 48  HIS A O   1 
ATOM   111  C  CB  . HIS A 1 20  ? 11.129  -6.272  61.941  1.00 23.30 ? 48  HIS A CB  1 
ATOM   112  C  CG  . HIS A 1 20  ? 11.166  -5.922  60.488  1.00 21.91 ? 48  HIS A CG  1 
ATOM   113  N  ND1 . HIS A 1 20  ? 10.184  -6.312  59.602  1.00 25.00 ? 48  HIS A ND1 1 
ATOM   114  C  CD2 . HIS A 1 20  ? 12.032  -5.161  59.779  1.00 29.61 ? 48  HIS A CD2 1 
ATOM   115  C  CE1 . HIS A 1 20  ? 10.461  -5.834  58.402  1.00 28.77 ? 48  HIS A CE1 1 
ATOM   116  N  NE2 . HIS A 1 20  ? 11.578  -5.130  58.483  1.00 31.18 ? 48  HIS A NE2 1 
ATOM   117  N  N   . HIS A 1 21  ? 8.207   -5.994  62.784  1.00 20.60 ? 49  HIS A N   1 
ATOM   118  C  CA  . HIS A 1 21  ? 6.779   -5.831  62.519  1.00 21.15 ? 49  HIS A CA  1 
ATOM   119  C  C   . HIS A 1 21  ? 5.981   -6.781  63.403  1.00 19.79 ? 49  HIS A C   1 
ATOM   120  O  O   . HIS A 1 21  ? 6.521   -7.644  64.094  1.00 19.57 ? 49  HIS A O   1 
ATOM   121  C  CB  . HIS A 1 21  ? 6.447   -6.046  61.036  1.00 21.10 ? 49  HIS A CB  1 
ATOM   122  C  CG  . HIS A 1 21  ? 6.654   -7.448  60.542  1.00 19.97 ? 49  HIS A CG  1 
ATOM   123  N  ND1 . HIS A 1 21  ? 7.817   -7.864  59.927  1.00 20.79 ? 49  HIS A ND1 1 
ATOM   124  C  CD2 . HIS A 1 21  ? 5.816   -8.514  60.519  1.00 20.82 ? 49  HIS A CD2 1 
ATOM   125  C  CE1 . HIS A 1 21  ? 7.701   -9.132  59.577  1.00 20.73 ? 49  HIS A CE1 1 
ATOM   126  N  NE2 . HIS A 1 21  ? 6.493   -9.550  59.917  1.00 21.49 ? 49  HIS A NE2 1 
ATOM   127  N  N   . ILE A 1 22  ? 4.664   -6.586  63.382  1.00 18.75 ? 50  ILE A N   1 
ATOM   128  C  CA  . ILE A 1 22  ? 3.720   -7.428  64.094  1.00 17.99 ? 50  ILE A CA  1 
ATOM   129  C  C   . ILE A 1 22  ? 2.694   -7.833  63.057  1.00 17.56 ? 50  ILE A C   1 
ATOM   130  O  O   . ILE A 1 22  ? 2.200   -6.970  62.329  1.00 18.58 ? 50  ILE A O   1 
ATOM   131  C  CB  . ILE A 1 22  ? 3.035   -6.662  65.248  1.00 22.89 ? 50  ILE A CB  1 
ATOM   132  C  CG1 . ILE A 1 22  ? 4.054   -6.240  66.303  1.00 21.01 ? 50  ILE A CG1 1 
ATOM   133  C  CG2 . ILE A 1 22  ? 1.839   -7.472  65.833  1.00 18.93 ? 50  ILE A CG2 1 
ATOM   134  C  CD1 . ILE A 1 22  ? 4.530   -7.372  67.176  1.00 19.27 ? 50  ILE A CD1 1 
ATOM   135  N  N   . GLU A 1 23  ? 2.378   -9.130  62.977  1.00 18.61 ? 51  GLU A N   1 
ATOM   136  C  CA  . GLU A 1 23  ? 1.405   -9.624  62.007  1.00 18.62 ? 51  GLU A CA  1 
ATOM   137  C  C   . GLU A 1 23  ? 0.158   -10.144 62.716  1.00 21.23 ? 51  GLU A C   1 
ATOM   138  O  O   . GLU A 1 23  ? 0.235   -11.069 63.539  1.00 19.50 ? 51  GLU A O   1 
ATOM   139  C  CB  . GLU A 1 23  ? 1.988   -10.733 61.110  1.00 18.21 ? 51  GLU A CB  1 
ATOM   140  C  CG  . GLU A 1 23  ? 0.957   -11.180 60.066  1.00 18.61 ? 51  GLU A CG  1 
ATOM   141  C  CD  . GLU A 1 23  ? 1.506   -12.216 59.098  1.00 24.65 ? 51  GLU A CD  1 
ATOM   142  O  OE1 . GLU A 1 23  ? 2.621   -12.726 59.338  1.00 22.98 ? 51  GLU A OE1 1 
ATOM   143  O  OE2 . GLU A 1 23  ? 0.812   -12.520 58.108  1.00 21.30 ? 51  GLU A OE2 1 
ATOM   144  N  N   . PHE A 1 24  ? -0.990  -9.567  62.356  1.00 17.61 ? 52  PHE A N   1 
ATOM   145  C  CA  . PHE A 1 24  ? -2.297  -10.026 62.797  1.00 17.93 ? 52  PHE A CA  1 
ATOM   146  C  C   . PHE A 1 24  ? -2.825  -11.036 61.797  1.00 17.99 ? 52  PHE A C   1 
ATOM   147  O  O   . PHE A 1 24  ? -2.772  -10.786 60.588  1.00 18.22 ? 52  PHE A O   1 
ATOM   148  C  CB  . PHE A 1 24  ? -3.271  -8.839  62.872  1.00 17.59 ? 52  PHE A CB  1 
ATOM   149  C  CG  . PHE A 1 24  ? -2.955  -7.866  63.965  1.00 17.22 ? 52  PHE A CG  1 
ATOM   150  C  CD1 . PHE A 1 24  ? -2.034  -6.855  63.772  1.00 18.33 ? 52  PHE A CD1 1 
ATOM   151  C  CD2 . PHE A 1 24  ? -3.592  -7.963  65.195  1.00 19.94 ? 52  PHE A CD2 1 
ATOM   152  C  CE1 . PHE A 1 24  ? -1.742  -5.964  64.792  1.00 23.02 ? 52  PHE A CE1 1 
ATOM   153  C  CE2 . PHE A 1 24  ? -3.291  -7.072  66.212  1.00 21.62 ? 52  PHE A CE2 1 
ATOM   154  C  CZ  . PHE A 1 24  ? -2.376  -6.077  66.010  1.00 18.75 ? 52  PHE A CZ  1 
ATOM   155  N  N   . TRP A 1 25  ? -3.361  -12.159 62.298  1.00 16.61 ? 53  TRP A N   1 
ATOM   156  C  CA  . TRP A 1 25  ? -4.103  -13.079 61.462  1.00 16.55 ? 53  TRP A CA  1 
ATOM   157  C  C   . TRP A 1 25  ? -5.581  -12.772 61.627  1.00 17.63 ? 53  TRP A C   1 
ATOM   158  O  O   . TRP A 1 25  ? -6.084  -12.680 62.754  1.00 17.66 ? 53  TRP A O   1 
ATOM   159  C  CB  . TRP A 1 25  ? -3.781  -14.532 61.794  1.00 20.98 ? 53  TRP A CB  1 
ATOM   160  C  CG  . TRP A 1 25  ? -2.668  -15.033 60.935  1.00 19.96 ? 53  TRP A CG  1 
ATOM   161  C  CD1 . TRP A 1 25  ? -1.982  -14.337 59.972  1.00 22.14 ? 53  TRP A CD1 1 
ATOM   162  C  CD2 . TRP A 1 25  ? -2.105  -16.345 60.957  1.00 22.15 ? 53  TRP A CD2 1 
ATOM   163  N  NE1 . TRP A 1 25  ? -1.041  -15.152 59.375  1.00 19.75 ? 53  TRP A NE1 1 
ATOM   164  C  CE2 . TRP A 1 25  ? -1.095  -16.388 59.967  1.00 21.08 ? 53  TRP A CE2 1 
ATOM   165  C  CE3 . TRP A 1 25  ? -2.362  -17.486 61.717  1.00 20.22 ? 53  TRP A CE3 1 
ATOM   166  C  CZ2 . TRP A 1 25  ? -0.334  -17.551 59.710  1.00 22.34 ? 53  TRP A CZ2 1 
ATOM   167  C  CZ3 . TRP A 1 25  ? -1.595  -18.639 61.466  1.00 21.01 ? 53  TRP A CZ3 1 
ATOM   168  C  CH2 . TRP A 1 25  ? -0.597  -18.650 60.469  1.00 19.97 ? 53  TRP A CH2 1 
ATOM   169  N  N   . CYS A 1 26  ? -6.246  -12.569 60.502  1.00 16.81 ? 54  CYS A N   1 
ATOM   170  C  CA  . CYS A 1 26  ? -7.580  -11.983 60.458  1.00 16.18 ? 54  CYS A CA  1 
ATOM   171  C  C   . CYS A 1 26  ? -8.522  -12.880 59.684  1.00 17.51 ? 54  CYS A C   1 
ATOM   172  O  O   . CYS A 1 26  ? -8.101  -13.776 58.943  1.00 20.89 ? 54  CYS A O   1 
ATOM   173  C  CB  . CYS A 1 26  ? -7.586  -10.614 59.762  1.00 16.30 ? 54  CYS A CB  1 
ATOM   174  S  SG  . CYS A 1 26  ? -6.400  -9.427  60.390  1.00 21.52 ? 54  CYS A SG  1 
ATOM   175  N  N   . GLY A 1 27  ? -9.807  -12.544 59.792  1.00 19.96 ? 55  GLY A N   1 
ATOM   176  C  CA  . GLY A 1 27  ? -10.798 -13.165 58.942  1.00 19.41 ? 55  GLY A CA  1 
ATOM   177  C  C   . GLY A 1 27  ? -10.867 -12.409 57.638  1.00 22.39 ? 55  GLY A C   1 
ATOM   178  O  O   . GLY A 1 27  ? -10.862 -12.994 56.546  1.00 22.08 ? 55  GLY A O   1 
ATOM   179  N  N   . ASP A 1 28  ? -10.983 -11.090 57.751  1.00 21.46 ? 56  ASP A N   1 
ATOM   180  C  CA  . ASP A 1 28  ? -10.928 -10.193 56.601  1.00 17.07 ? 56  ASP A CA  1 
ATOM   181  C  C   . ASP A 1 28  ? -9.865  -9.145  56.897  1.00 18.14 ? 56  ASP A C   1 
ATOM   182  O  O   . ASP A 1 28  ? -10.073 -8.280  57.757  1.00 18.66 ? 56  ASP A O   1 
ATOM   183  C  CB  . ASP A 1 28  ? -12.296 -9.542  56.342  1.00 16.87 ? 56  ASP A CB  1 
ATOM   184  C  CG  . ASP A 1 28  ? -12.301 -8.693  55.085  1.00 18.67 ? 56  ASP A CG  1 
ATOM   185  O  OD1 . ASP A 1 28  ? -12.495 -9.262  53.986  1.00 21.01 ? 56  ASP A OD1 1 
ATOM   186  O  OD2 . ASP A 1 28  ? -12.070 -7.472  55.180  1.00 19.44 ? 56  ASP A OD2 1 
ATOM   187  N  N   . ALA A 1 29  ? -8.732  -9.215  56.190  1.00 17.15 ? 57  ALA A N   1 
ATOM   188  C  CA  . ALA A 1 29  ? -7.640  -8.278  56.470  1.00 17.07 ? 57  ALA A CA  1 
ATOM   189  C  C   . ALA A 1 29  ? -8.007  -6.847  56.091  1.00 18.54 ? 57  ALA A C   1 
ATOM   190  O  O   . ALA A 1 29  ? -7.560  -5.903  56.750  1.00 19.29 ? 57  ALA A O   1 
ATOM   191  C  CB  . ALA A 1 29  ? -6.377  -8.703  55.727  1.00 19.00 ? 57  ALA A CB  1 
ATOM   192  N  N   . THR A 1 30  ? -8.797  -6.677  55.029  1.00 19.12 ? 58  THR A N   1 
ATOM   193  C  CA  . THR A 1 30  ? -9.175  -5.344  54.563  1.00 19.18 ? 58  THR A CA  1 
ATOM   194  C  C   . THR A 1 30  ? -9.852  -4.542  55.667  1.00 18.85 ? 58  THR A C   1 
ATOM   195  O  O   . THR A 1 30  ? -9.460  -3.402  55.952  1.00 18.54 ? 58  THR A O   1 
ATOM   196  C  CB  . THR A 1 30  ? -10.091 -5.465  53.344  1.00 22.31 ? 58  THR A CB  1 
ATOM   197  O  OG1 . THR A 1 30  ? -9.314  -5.892  52.214  1.00 21.45 ? 58  THR A OG1 1 
ATOM   198  C  CG2 . THR A 1 30  ? -10.797 -4.124  53.032  1.00 20.53 ? 58  THR A CG2 1 
ATOM   199  N  N   . ASN A 1 31  ? -10.889 -5.116  56.294  1.00 16.58 ? 59  ASN A N   1 
ATOM   200  C  CA  . ASN A 1 31  ? -11.671 -4.336  57.255  1.00 17.45 ? 59  ASN A CA  1 
ATOM   201  C  C   . ASN A 1 31  ? -10.882 -4.088  58.531  1.00 19.85 ? 59  ASN A C   1 
ATOM   202  O  O   . ASN A 1 31  ? -11.000 -3.023  59.137  1.00 17.03 ? 59  ASN A O   1 
ATOM   203  C  CB  . ASN A 1 31  ? -13.008 -5.024  57.563  1.00 17.06 ? 59  ASN A CB  1 
ATOM   204  C  CG  . ASN A 1 31  ? -14.058 -4.701  56.518  1.00 18.78 ? 59  ASN A CG  1 
ATOM   205  O  OD1 . ASN A 1 31  ? -14.831 -3.749  56.671  1.00 15.16 ? 59  ASN A OD1 1 
ATOM   206  N  ND2 . ASN A 1 31  ? -14.048 -5.448  55.411  1.00 18.62 ? 59  ASN A ND2 1 
ATOM   207  N  N   . VAL A 1 32  ? -10.084 -5.056  58.976  1.00 14.32 ? 60  VAL A N   1 
ATOM   208  C  CA  . VAL A 1 32  ? -9.268  -4.802  60.159  1.00 15.32 ? 60  VAL A CA  1 
ATOM   209  C  C   . VAL A 1 32  ? -8.237  -3.725  59.874  1.00 16.58 ? 60  VAL A C   1 
ATOM   210  O  O   . VAL A 1 32  ? -8.041  -2.807  60.680  1.00 16.36 ? 60  VAL A O   1 
ATOM   211  C  CB  . VAL A 1 32  ? -8.588  -6.090  60.653  1.00 16.41 ? 60  VAL A CB  1 
ATOM   212  C  CG1 . VAL A 1 32  ? -7.755  -5.800  61.884  1.00 17.54 ? 60  VAL A CG1 1 
ATOM   213  C  CG2 . VAL A 1 32  ? -9.660  -7.162  60.970  1.00 17.02 ? 60  VAL A CG2 1 
ATOM   214  N  N   . ALA A 1 33  ? -7.542  -3.830  58.735  1.00 15.22 ? 61  ALA A N   1 
ATOM   215  C  CA  . ALA A 1 33  ? -6.512  -2.833  58.433  1.00 16.52 ? 61  ALA A CA  1 
ATOM   216  C  C   . ALA A 1 33  ? -7.117  -1.439  58.281  1.00 18.14 ? 61  ALA A C   1 
ATOM   217  O  O   . ALA A 1 33  ? -6.530  -0.452  58.729  1.00 17.07 ? 61  ALA A O   1 
ATOM   218  C  CB  . ALA A 1 33  ? -5.740  -3.223  57.169  1.00 19.48 ? 61  ALA A CB  1 
ATOM   219  N  N   . ARG A 1 34  ? -8.283  -1.328  57.640  1.00 15.67 ? 62  ARG A N   1 
ATOM   220  C  CA  . ARG A 1 34  ? -8.884  0.004   57.499  1.00 15.52 ? 62  ARG A CA  1 
ATOM   221  C  C   . ARG A 1 34  ? -9.285  0.592   58.852  1.00 19.39 ? 62  ARG A C   1 
ATOM   222  O  O   . ARG A 1 34  ? -9.087  1.795   59.096  1.00 18.22 ? 62  ARG A O   1 
ATOM   223  C  CB  . ARG A 1 34  ? -10.085 -0.043  56.548  1.00 19.15 ? 62  ARG A CB  1 
ATOM   224  C  CG  . ARG A 1 34  ? -9.697  -0.408  55.138  1.00 24.16 ? 62  ARG A CG  1 
ATOM   225  C  CD  . ARG A 1 34  ? -10.297 0.454   54.077  1.00 24.88 ? 62  ARG A CD  1 
ATOM   226  N  NE  . ARG A 1 34  ? -9.621  0.231   52.806  1.00 22.49 ? 62  ARG A NE  1 
ATOM   227  C  CZ  . ARG A 1 34  ? -9.815  0.948   51.706  1.00 25.94 ? 62  ARG A CZ  1 
ATOM   228  N  NH1 . ARG A 1 34  ? -9.132  0.664   50.597  1.00 26.46 ? 62  ARG A NH1 1 
ATOM   229  N  NH2 . ARG A 1 34  ? -10.704 1.934   51.704  1.00 26.98 ? 62  ARG A NH2 1 
ATOM   230  N  N   . ARG A 1 35  ? -9.869  -0.225  59.731  1.00 15.32 ? 63  ARG A N   1 
ATOM   231  C  CA  . ARG A 1 35  ? -10.211 0.237   61.078  1.00 14.88 ? 63  ARG A CA  1 
ATOM   232  C  C   . ARG A 1 35  ? -8.956  0.675   61.834  1.00 17.18 ? 63  ARG A C   1 
ATOM   233  O  O   . ARG A 1 35  ? -8.912  1.757   62.432  1.00 17.09 ? 63  ARG A O   1 
ATOM   234  C  CB  . ARG A 1 35  ? -10.961 -0.887  61.827  1.00 15.90 ? 63  ARG A CB  1 
ATOM   235  C  CG  . ARG A 1 35  ? -11.735 -0.504  63.125  1.00 15.04 ? 63  ARG A CG  1 
ATOM   236  C  CD  . ARG A 1 35  ? -10.784 -0.250  64.285  1.00 18.18 ? 63  ARG A CD  1 
ATOM   237  N  NE  . ARG A 1 35  ? -11.423 -0.029  65.581  1.00 17.89 ? 63  ARG A NE  1 
ATOM   238  C  CZ  . ARG A 1 35  ? -11.531 -0.956  66.516  1.00 19.77 ? 63  ARG A CZ  1 
ATOM   239  N  NH1 . ARG A 1 35  ? -12.091 -0.666  67.688  1.00 18.90 ? 63  ARG A NH1 1 
ATOM   240  N  NH2 . ARG A 1 35  ? -11.081 -2.184  66.270  1.00 16.64 ? 63  ARG A NH2 1 
ATOM   241  N  N   . PHE A 1 36  ? -7.918  -0.157  61.820  1.00 14.24 ? 64  PHE A N   1 
ATOM   242  C  CA  . PHE A 1 36  ? -6.703  0.194   62.551  1.00 13.67 ? 64  PHE A CA  1 
ATOM   243  C  C   . PHE A 1 36  ? -6.056  1.453   61.990  1.00 16.35 ? 64  PHE A C   1 
ATOM   244  O  O   . PHE A 1 36  ? -5.528  2.272   62.746  1.00 17.37 ? 64  PHE A O   1 
ATOM   245  C  CB  . PHE A 1 36  ? -5.704  -0.971  62.503  1.00 15.21 ? 64  PHE A CB  1 
ATOM   246  C  CG  . PHE A 1 36  ? -5.909  -2.028  63.585  1.00 16.22 ? 64  PHE A CG  1 
ATOM   247  C  CD1 . PHE A 1 36  ? -7.114  -2.708  63.709  1.00 17.74 ? 64  PHE A CD1 1 
ATOM   248  C  CD2 . PHE A 1 36  ? -4.866  -2.375  64.437  1.00 17.67 ? 64  PHE A CD2 1 
ATOM   249  C  CE1 . PHE A 1 36  ? -7.284  -3.706  64.686  1.00 17.43 ? 64  PHE A CE1 1 
ATOM   250  C  CE2 . PHE A 1 36  ? -5.032  -3.370  65.419  1.00 20.32 ? 64  PHE A CE2 1 
ATOM   251  C  CZ  . PHE A 1 36  ? -6.234  -4.049  65.531  1.00 16.85 ? 64  PHE A CZ  1 
ATOM   252  N  N   . SER A 1 37  ? -6.044  1.596   60.665  1.00 14.53 ? 65  SER A N   1 
ATOM   253  C  CA  . SER A 1 37  ? -5.422  2.765   60.046  1.00 16.70 ? 65  SER A CA  1 
ATOM   254  C  C   . SER A 1 37  ? -6.035  4.054   60.583  1.00 20.01 ? 65  SER A C   1 
ATOM   255  O  O   . SER A 1 37  ? -5.328  4.981   61.016  1.00 17.77 ? 65  SER A O   1 
ATOM   256  C  CB  . SER A 1 37  ? -5.608  2.687   58.527  1.00 21.08 ? 65  SER A CB  1 
ATOM   257  O  OG  . SER A 1 37  ? -5.083  3.848   57.877  1.00 23.60 ? 65  SER A OG  1 
ATOM   258  N  N   . TRP A 1 38  ? -7.363  4.118   60.561  1.00 18.20 ? 66  TRP A N   1 
ATOM   259  C  CA  . TRP A 1 38  ? -8.078  5.291   61.041  1.00 18.91 ? 66  TRP A CA  1 
ATOM   260  C  C   . TRP A 1 38  ? -7.949  5.457   62.547  1.00 18.73 ? 66  TRP A C   1 
ATOM   261  O  O   . TRP A 1 38  ? -7.760  6.578   63.045  1.00 20.30 ? 66  TRP A O   1 
ATOM   262  C  CB  . TRP A 1 38  ? -9.542  5.155   60.628  1.00 15.43 ? 66  TRP A CB  1 
ATOM   263  C  CG  . TRP A 1 38  ? -10.473 6.247   61.103  1.00 18.27 ? 66  TRP A CG  1 
ATOM   264  C  CD1 . TRP A 1 38  ? -11.666 6.078   61.776  1.00 20.55 ? 66  TRP A CD1 1 
ATOM   265  C  CD2 . TRP A 1 38  ? -10.325 7.669   60.903  1.00 19.19 ? 66  TRP A CD2 1 
ATOM   266  N  NE1 . TRP A 1 38  ? -12.260 7.311   62.006  1.00 21.66 ? 66  TRP A NE1 1 
ATOM   267  C  CE2 . TRP A 1 38  ? -11.454 8.295   61.485  1.00 20.33 ? 66  TRP A CE2 1 
ATOM   268  C  CE3 . TRP A 1 38  ? -9.347  8.468   60.291  1.00 20.01 ? 66  TRP A CE3 1 
ATOM   269  C  CZ2 . TRP A 1 38  ? -11.628 9.681   61.469  1.00 19.69 ? 66  TRP A CZ2 1 
ATOM   270  C  CZ3 . TRP A 1 38  ? -9.528  9.847   60.263  1.00 23.71 ? 66  TRP A CZ3 1 
ATOM   271  C  CH2 . TRP A 1 38  ? -10.656 10.436  60.855  1.00 22.26 ? 66  TRP A CH2 1 
ATOM   272  N  N   . GLY A 1 39  ? -8.066  4.360   63.294  1.00 18.12 ? 67  GLY A N   1 
ATOM   273  C  CA  . GLY A 1 39  ? -8.055  4.447   64.747  1.00 16.56 ? 67  GLY A CA  1 
ATOM   274  C  C   . GLY A 1 39  ? -6.702  4.834   65.328  1.00 19.35 ? 67  GLY A C   1 
ATOM   275  O  O   . GLY A 1 39  ? -6.650  5.532   66.344  1.00 17.82 ? 67  GLY A O   1 
ATOM   276  N  N   . LEU A 1 40  ? -5.602  4.372   64.716  1.00 16.46 ? 68  LEU A N   1 
ATOM   277  C  CA  . LEU A 1 40  ? -4.253  4.600   65.232  1.00 15.38 ? 68  LEU A CA  1 
ATOM   278  C  C   . LEU A 1 40  ? -3.453  5.626   64.444  1.00 20.01 ? 68  LEU A C   1 
ATOM   279  O  O   . LEU A 1 40  ? -2.381  6.040   64.909  1.00 19.71 ? 68  LEU A O   1 
ATOM   280  C  CB  . LEU A 1 40  ? -3.446  3.277   65.264  1.00 17.82 ? 68  LEU A CB  1 
ATOM   281  C  CG  . LEU A 1 40  ? -3.953  2.289   66.321  1.00 20.15 ? 68  LEU A CG  1 
ATOM   282  C  CD1 . LEU A 1 40  ? -3.687  0.812   65.902  1.00 16.59 ? 68  LEU A CD1 1 
ATOM   283  C  CD2 . LEU A 1 40  ? -3.276  2.583   67.652  1.00 18.51 ? 68  LEU A CD2 1 
ATOM   284  N  N   . GLY A 1 41  ? -3.913  6.011   63.260  1.00 20.74 ? 69  GLY A N   1 
ATOM   285  C  CA  . GLY A 1 41  ? -3.196  6.971   62.450  1.00 21.50 ? 69  GLY A CA  1 
ATOM   286  C  C   . GLY A 1 41  ? -1.997  6.377   61.754  1.00 23.82 ? 69  GLY A C   1 
ATOM   287  O  O   . GLY A 1 41  ? -0.897  6.937   61.807  1.00 20.94 ? 69  GLY A O   1 
ATOM   288  N  N   . MET A 1 42  ? -2.195  5.250   61.082  1.00 18.55 ? 70  MET A N   1 
ATOM   289  C  CA  . MET A 1 42  ? -1.128  4.578   60.367  1.00 18.50 ? 70  MET A CA  1 
ATOM   290  C  C   . MET A 1 42  ? -1.459  4.604   58.884  1.00 24.12 ? 70  MET A C   1 
ATOM   291  O  O   . MET A 1 42  ? -2.629  4.477   58.507  1.00 30.48 ? 70  MET A O   1 
ATOM   292  C  CB  . MET A 1 42  ? -0.968  3.144   60.886  1.00 18.65 ? 70  MET A CB  1 
ATOM   293  C  CG  . MET A 1 42  ? -0.980  3.052   62.417  1.00 19.97 ? 70  MET A CG  1 
ATOM   294  S  SD  . MET A 1 42  ? -0.686  1.375   63.104  1.00 22.65 ? 70  MET A SD  1 
ATOM   295  C  CE  . MET A 1 42  ? 0.881   0.871   62.371  1.00 20.28 ? 70  MET A CE  1 
ATOM   296  N  N   . ARG A 1 43  ? -0.447  4.786   58.040  1.00 19.79 ? 71  ARG A N   1 
ATOM   297  C  CA  . ARG A 1 43  ? -0.670  4.827   56.599  1.00 25.63 ? 71  ARG A CA  1 
ATOM   298  C  C   . ARG A 1 43  ? -0.614  3.437   56.010  1.00 24.24 ? 71  ARG A C   1 
ATOM   299  O  O   . ARG A 1 43  ? 0.201   2.603   56.413  1.00 24.11 ? 71  ARG A O   1 
ATOM   300  C  CB  . ARG A 1 43  ? 0.395   5.611   55.831  1.00 25.06 ? 71  ARG A CB  1 
ATOM   301  C  CG  . ARG A 1 43  ? 1.192   6.579   56.606  1.00 39.92 ? 71  ARG A CG  1 
ATOM   302  C  CD  . ARG A 1 43  ? 2.001   7.345   55.584  1.00 35.32 ? 71  ARG A CD  1 
ATOM   303  N  NE  . ARG A 1 43  ? 3.083   8.127   56.202  1.00 60.61 ? 71  ARG A NE  1 
ATOM   304  C  CZ  . ARG A 1 43  ? 2.905   9.148   57.019  1.00 48.31 ? 71  ARG A CZ  1 
ATOM   305  N  NH1 . ARG A 1 43  ? 3.955   9.806   57.484  1.00 50.13 ? 71  ARG A NH1 1 
ATOM   306  N  NH2 . ARG A 1 43  ? 1.638   9.507   57.320  1.00 42.99 ? 71  ARG A NH2 1 
ATOM   307  N  N   . PHE A 1 44  ? -1.408  3.251   54.972  1.00 23.69 ? 72  PHE A N   1 
ATOM   308  C  CA  . PHE A 1 44  ? -1.329  2.094   54.088  1.00 25.43 ? 72  PHE A CA  1 
ATOM   309  C  C   . PHE A 1 44  ? -0.051  2.202   53.250  1.00 28.99 ? 72  PHE A C   1 
ATOM   310  O  O   . PHE A 1 44  ? 0.052   3.076   52.384  1.00 29.58 ? 72  PHE A O   1 
ATOM   311  C  CB  . PHE A 1 44  ? -2.583  2.131   53.223  1.00 28.95 ? 72  PHE A CB  1 
ATOM   312  C  CG  . PHE A 1 44  ? -2.822  0.915   52.408  1.00 36.79 ? 72  PHE A CG  1 
ATOM   313  C  CD1 . PHE A 1 44  ? -2.247  -0.301  52.730  1.00 36.89 ? 72  PHE A CD1 1 
ATOM   314  C  CD2 . PHE A 1 44  ? -3.678  0.987   51.315  1.00 43.86 ? 72  PHE A CD2 1 
ATOM   315  C  CE1 . PHE A 1 44  ? -2.495  -1.414  51.957  1.00 32.34 ? 72  PHE A CE1 1 
ATOM   316  C  CE2 . PHE A 1 44  ? -3.932  -0.123  50.535  1.00 42.32 ? 72  PHE A CE2 1 
ATOM   317  C  CZ  . PHE A 1 44  ? -3.344  -1.326  50.857  1.00 37.68 ? 72  PHE A CZ  1 
ATOM   318  N  N   . SER A 1 45  ? 0.939   1.333   53.488  1.00 26.26 ? 73  SER A N   1 
ATOM   319  C  CA  . SER A 1 45  ? 2.224   1.504   52.824  1.00 29.98 ? 73  SER A CA  1 
ATOM   320  C  C   . SER A 1 45  ? 2.657   0.360   51.910  1.00 31.31 ? 73  SER A C   1 
ATOM   321  O  O   . SER A 1 45  ? 3.455   0.605   51.005  1.00 31.59 ? 73  SER A O   1 
ATOM   322  C  CB  . SER A 1 45  ? 3.327   1.770   53.861  1.00 30.66 ? 73  SER A CB  1 
ATOM   323  O  OG  . SER A 1 45  ? 3.660   0.579   54.518  1.00 41.27 ? 73  SER A OG  1 
ATOM   324  N  N   . ALA A 1 46  ? 2.149   -0.861  52.081  1.00 27.77 ? 74  ALA A N   1 
ATOM   325  C  CA  . ALA A 1 46  ? 2.491   -1.922  51.140  1.00 26.55 ? 74  ALA A CA  1 
ATOM   326  C  C   . ALA A 1 46  ? 1.358   -2.935  51.099  1.00 27.78 ? 74  ALA A C   1 
ATOM   327  O  O   . ALA A 1 46  ? 0.559   -3.027  52.032  1.00 24.82 ? 74  ALA A O   1 
ATOM   328  C  CB  . ALA A 1 46  ? 3.804   -2.621  51.504  1.00 30.95 ? 74  ALA A CB  1 
ATOM   329  N  N   . LYS A 1 47  ? 1.299   -3.702  50.011  1.00 24.70 ? 75  LYS A N   1 
ATOM   330  C  CA  . LYS A 1 47  ? 0.297   -4.754  49.896  1.00 23.18 ? 75  LYS A CA  1 
ATOM   331  C  C   . LYS A 1 47  ? 0.829   -5.966  49.150  1.00 26.38 ? 75  LYS A C   1 
ATOM   332  O  O   . LYS A 1 47  ? 1.730   -5.868  48.314  1.00 28.78 ? 75  LYS A O   1 
ATOM   333  C  CB  . LYS A 1 47  ? -0.959  -4.265  49.174  1.00 24.03 ? 75  LYS A CB  1 
ATOM   334  C  CG  . LYS A 1 47  ? -0.688  -3.816  47.740  1.00 32.07 ? 75  LYS A CG  1 
ATOM   335  C  CD  . LYS A 1 47  ? -1.956  -3.360  47.040  1.00 32.48 ? 75  LYS A CD  1 
ATOM   336  C  CE  . LYS A 1 47  ? -1.668  -2.921  45.607  1.00 36.12 ? 75  LYS A CE  1 
ATOM   337  N  NZ  . LYS A 1 47  ? -2.940  -2.671  44.877  1.00 33.60 ? 75  LYS A NZ  1 
ATOM   338  N  N   . SER A 1 48  ? 0.217   -7.111  49.443  1.00 22.44 ? 76  SER A N   1 
ATOM   339  C  CA  . SER A 1 48  ? 0.425   -8.338  48.690  1.00 24.53 ? 76  SER A CA  1 
ATOM   340  C  C   . SER A 1 48  ? -0.930  -9.026  48.627  1.00 21.08 ? 76  SER A C   1 
ATOM   341  O  O   . SER A 1 48  ? -1.448  -9.463  49.658  1.00 22.48 ? 76  SER A O   1 
ATOM   342  C  CB  . SER A 1 48  ? 1.480   -9.222  49.357  1.00 24.67 ? 76  SER A CB  1 
ATOM   343  O  OG  . SER A 1 48  ? 1.609   -10.468 48.689  1.00 25.38 ? 76  SER A OG  1 
ATOM   344  N  N   . ASP A 1 49  ? -1.522  -9.101  47.441  1.00 20.47 ? 77  ASP A N   1 
ATOM   345  C  CA  . ASP A 1 49  ? -2.880  -9.636  47.329  1.00 22.86 ? 77  ASP A CA  1 
ATOM   346  C  C   . ASP A 1 49  ? -3.130  -10.000 45.871  1.00 22.99 ? 77  ASP A C   1 
ATOM   347  O  O   . ASP A 1 49  ? -2.197  -10.044 45.065  1.00 25.56 ? 77  ASP A O   1 
ATOM   348  C  CB  . ASP A 1 49  ? -3.905  -8.640  47.894  1.00 21.20 ? 77  ASP A CB  1 
ATOM   349  C  CG  . ASP A 1 49  ? -3.997  -7.339  47.101  1.00 27.59 ? 77  ASP A CG  1 
ATOM   350  O  OD1 . ASP A 1 49  ? -3.340  -7.207  46.049  1.00 27.13 ? 77  ASP A OD1 1 
ATOM   351  O  OD2 . ASP A 1 49  ? -4.785  -6.443  47.519  1.00 25.53 ? 77  ASP A OD2 1 
ATOM   352  N  N   . LEU A 1 50  ? -4.399  -10.271 45.527  1.00 23.48 ? 78  LEU A N   1 
ATOM   353  C  CA  . LEU A 1 50  ? -4.723  -10.656 44.157  1.00 25.23 ? 78  LEU A CA  1 
ATOM   354  C  C   . LEU A 1 50  ? -4.157  -9.673  43.141  1.00 26.47 ? 78  LEU A C   1 
ATOM   355  O  O   . LEU A 1 50  ? -3.734  -10.078 42.053  1.00 26.22 ? 78  LEU A O   1 
ATOM   356  C  CB  . LEU A 1 50  ? -6.237  -10.762 43.968  1.00 24.17 ? 78  LEU A CB  1 
ATOM   357  C  CG  . LEU A 1 50  ? -7.010  -11.851 44.690  1.00 25.44 ? 78  LEU A CG  1 
ATOM   358  C  CD1 . LEU A 1 50  ? -8.525  -11.621 44.470  1.00 27.30 ? 78  LEU A CD1 1 
ATOM   359  C  CD2 . LEU A 1 50  ? -6.598  -13.268 44.260  1.00 25.11 ? 78  LEU A CD2 1 
ATOM   360  N  N   . SER A 1 51  ? -4.171  -8.370  43.460  1.00 26.14 ? 79  SER A N   1 
ATOM   361  C  CA  . SER A 1 51  ? -3.682  -7.378  42.504  1.00 28.69 ? 79  SER A CA  1 
ATOM   362  C  C   . SER A 1 51  ? -2.165  -7.409  42.333  1.00 30.51 ? 79  SER A C   1 
ATOM   363  O  O   . SER A 1 51  ? -1.660  -6.812  41.377  1.00 31.10 ? 79  SER A O   1 
ATOM   364  C  CB  . SER A 1 51  ? -4.117  -5.966  42.921  1.00 28.69 ? 79  SER A CB  1 
ATOM   365  O  OG  . SER A 1 51  ? -3.228  -5.444  43.889  1.00 29.44 ? 79  SER A OG  1 
ATOM   366  N  N   . THR A 1 52  ? -1.428  -8.069  43.222  1.00 27.31 ? 80  THR A N   1 
ATOM   367  C  CA  . THR A 1 52  ? 0.013   -8.241  43.054  1.00 28.38 ? 80  THR A CA  1 
ATOM   368  C  C   . THR A 1 52  ? 0.378   -9.658  42.625  1.00 29.15 ? 80  THR A C   1 
ATOM   369  O  O   . THR A 1 52  ? 1.566   -9.993  42.569  1.00 28.36 ? 80  THR A O   1 
ATOM   370  C  CB  . THR A 1 52  ? 0.757   -7.883  44.342  1.00 26.13 ? 80  THR A CB  1 
ATOM   371  O  OG1 . THR A 1 52  ? 0.510   -8.892  45.332  1.00 26.97 ? 80  THR A OG1 1 
ATOM   372  C  CG2 . THR A 1 52  ? 0.298   -6.522  44.858  1.00 31.79 ? 80  THR A CG2 1 
ATOM   373  N  N   . GLY A 1 53  ? -0.608  -10.493 42.320  1.00 26.24 ? 81  GLY A N   1 
ATOM   374  C  CA  . GLY A 1 53  ? -0.362  -11.853 41.882  1.00 28.80 ? 81  GLY A CA  1 
ATOM   375  C  C   . GLY A 1 53  ? -0.401  -12.897 42.974  1.00 30.99 ? 81  GLY A C   1 
ATOM   376  O  O   . GLY A 1 53  ? -0.118  -14.067 42.697  1.00 27.21 ? 81  GLY A O   1 
ATOM   377  N  N   . ASN A 1 54  ? -0.751  -12.518 44.200  1.00 25.85 ? 82  ASN A N   1 
ATOM   378  C  CA  . ASN A 1 54  ? -0.828  -13.445 45.326  1.00 25.68 ? 82  ASN A CA  1 
ATOM   379  C  C   . ASN A 1 54  ? -2.224  -14.072 45.343  1.00 28.92 ? 82  ASN A C   1 
ATOM   380  O  O   . ASN A 1 54  ? -3.221  -13.393 45.638  1.00 23.07 ? 82  ASN A O   1 
ATOM   381  C  CB  . ASN A 1 54  ? -0.500  -12.694 46.621  1.00 24.97 ? 82  ASN A CB  1 
ATOM   382  C  CG  . ASN A 1 54  ? -0.421  -13.598 47.835  1.00 21.38 ? 82  ASN A CG  1 
ATOM   383  O  OD1 . ASN A 1 54  ? -0.944  -14.709 47.829  1.00 20.68 ? 82  ASN A OD1 1 
ATOM   384  N  ND2 . ASN A 1 54  ? 0.202   -13.110 48.896  1.00 23.30 ? 82  ASN A ND2 1 
ATOM   385  N  N   . MET A 1 55  ? -2.298  -15.371 45.005  1.00 24.71 ? 83  MET A N   1 
ATOM   386  C  CA  . MET A 1 55  ? -3.529  -16.151 44.987  1.00 22.71 ? 83  MET A CA  1 
ATOM   387  C  C   . MET A 1 55  ? -3.805  -16.856 46.299  1.00 21.15 ? 83  MET A C   1 
ATOM   388  O  O   . MET A 1 55  ? -4.804  -17.570 46.401  1.00 24.47 ? 83  MET A O   1 
ATOM   389  C  CB  . MET A 1 55  ? -3.482  -17.210 43.879  1.00 27.45 ? 83  MET A CB  1 
ATOM   390  C  CG  . MET A 1 55  ? -3.177  -16.662 42.507  1.00 28.60 ? 83  MET A CG  1 
ATOM   391  S  SD  . MET A 1 55  ? -4.489  -15.569 41.915  1.00 36.92 ? 83  MET A SD  1 
ATOM   392  C  CE  . MET A 1 55  ? -3.666  -14.004 41.983  1.00 31.18 ? 83  MET A CE  1 
ATOM   393  N  N   . VAL A 1 56  ? -2.943  -16.666 47.294  1.00 24.11 ? 84  VAL A N   1 
ATOM   394  C  CA  . VAL A 1 56  ? -2.966  -17.426 48.532  1.00 21.05 ? 84  VAL A CA  1 
ATOM   395  C  C   . VAL A 1 56  ? -3.537  -16.608 49.684  1.00 19.16 ? 84  VAL A C   1 
ATOM   396  O  O   . VAL A 1 56  ? -4.456  -17.049 50.379  1.00 21.35 ? 84  VAL A O   1 
ATOM   397  C  CB  . VAL A 1 56  ? -1.542  -17.929 48.882  1.00 22.41 ? 84  VAL A CB  1 
ATOM   398  C  CG1 . VAL A 1 56  ? -1.539  -18.535 50.269  1.00 22.33 ? 84  VAL A CG1 1 
ATOM   399  C  CG2 . VAL A 1 56  ? -1.084  -18.952 47.843  1.00 26.61 ? 84  VAL A CG2 1 
ATOM   400  N  N   . HIS A 1 57  ? -2.950  -15.449 49.947  1.00 22.74 ? 85  HIS A N   1 
ATOM   401  C  CA  . HIS A 1 57  ? -3.372  -14.638 51.075  1.00 23.92 ? 85  HIS A CA  1 
ATOM   402  C  C   . HIS A 1 57  ? -3.398  -13.175 50.682  1.00 21.26 ? 85  HIS A C   1 
ATOM   403  O  O   . HIS A 1 57  ? -2.743  -12.749 49.728  1.00 21.41 ? 85  HIS A O   1 
ATOM   404  C  CB  . HIS A 1 57  ? -2.475  -14.846 52.304  1.00 20.99 ? 85  HIS A CB  1 
ATOM   405  C  CG  . HIS A 1 57  ? -1.015  -14.580 52.065  1.00 20.51 ? 85  HIS A CG  1 
ATOM   406  N  ND1 . HIS A 1 57  ? -0.433  -13.346 52.276  1.00 20.94 ? 85  HIS A ND1 1 
ATOM   407  C  CD2 . HIS A 1 57  ? -0.012  -15.402 51.659  1.00 20.63 ? 85  HIS A CD2 1 
ATOM   408  C  CE1 . HIS A 1 57  ? 0.863   -13.420 52.018  1.00 24.55 ? 85  HIS A CE1 1 
ATOM   409  N  NE2 . HIS A 1 57  ? 1.139   -14.650 51.624  1.00 24.31 ? 85  HIS A NE2 1 
ATOM   410  N  N   . ALA A 1 58  ? -4.211  -12.421 51.428  1.00 21.84 ? 86  ALA A N   1 
ATOM   411  C  CA  . ALA A 1 58  ? -4.286  -10.970 51.340  1.00 19.23 ? 86  ALA A CA  1 
ATOM   412  C  C   . ALA A 1 58  ? -3.536  -10.399 52.530  1.00 17.49 ? 86  ALA A C   1 
ATOM   413  O  O   . ALA A 1 58  ? -3.862  -10.726 53.672  1.00 20.68 ? 86  ALA A O   1 
ATOM   414  C  CB  . ALA A 1 58  ? -5.753  -10.498 51.352  1.00 21.77 ? 86  ALA A CB  1 
ATOM   415  N  N   . SER A 1 59  ? -2.545  -9.537  52.274  1.00 18.61 ? 87  SER A N   1 
ATOM   416  C  CA  . SER A 1 59  ? -1.715  -8.990  53.339  1.00 18.21 ? 87  SER A CA  1 
ATOM   417  C  C   . SER A 1 59  ? -1.535  -7.495  53.118  1.00 20.94 ? 87  SER A C   1 
ATOM   418  O  O   . SER A 1 59  ? -1.067  -7.077  52.051  1.00 21.02 ? 87  SER A O   1 
ATOM   419  C  CB  . SER A 1 59  ? -0.333  -9.683  53.395  1.00 19.92 ? 87  SER A CB  1 
ATOM   420  O  OG  . SER A 1 59  ? -0.429  -11.002 53.907  1.00 22.84 ? 87  SER A OG  1 
ATOM   421  N  N   . TYR A 1 60  ? -1.909  -6.690  54.119  1.00 20.10 ? 88  TYR A N   1 
ATOM   422  C  CA  . TYR A 1 60  ? -1.814  -5.235  54.038  1.00 18.19 ? 88  TYR A CA  1 
ATOM   423  C  C   . TYR A 1 60  ? -0.945  -4.699  55.167  1.00 19.38 ? 88  TYR A C   1 
ATOM   424  O  O   . TYR A 1 60  ? -1.131  -5.066  56.336  1.00 18.19 ? 88  TYR A O   1 
ATOM   425  C  CB  . TYR A 1 60  ? -3.224  -4.592  54.062  1.00 18.08 ? 88  TYR A CB  1 
ATOM   426  C  CG  . TYR A 1 60  ? -4.052  -5.145  52.927  1.00 19.36 ? 88  TYR A CG  1 
ATOM   427  C  CD1 . TYR A 1 60  ? -3.696  -4.863  51.609  1.00 21.07 ? 88  TYR A CD1 1 
ATOM   428  C  CD2 . TYR A 1 60  ? -5.131  -6.015  53.149  1.00 22.28 ? 88  TYR A CD2 1 
ATOM   429  C  CE1 . TYR A 1 60  ? -4.414  -5.374  50.550  1.00 22.47 ? 88  TYR A CE1 1 
ATOM   430  C  CE2 . TYR A 1 60  ? -5.863  -6.524  52.084  1.00 18.29 ? 88  TYR A CE2 1 
ATOM   431  C  CZ  . TYR A 1 60  ? -5.490  -6.196  50.784  1.00 23.21 ? 88  TYR A CZ  1 
ATOM   432  O  OH  . TYR A 1 60  ? -6.161  -6.689  49.693  1.00 22.80 ? 88  TYR A OH  1 
ATOM   433  N  N   . LEU A 1 61  ? -0.019  -3.807  54.820  1.00 20.54 ? 89  LEU A N   1 
ATOM   434  C  CA  . LEU A 1 61  ? 0.941   -3.257  55.765  1.00 20.06 ? 89  LEU A CA  1 
ATOM   435  C  C   . LEU A 1 61  ? 0.592   -1.804  56.070  1.00 18.97 ? 89  LEU A C   1 
ATOM   436  O  O   . LEU A 1 61  ? 0.467   -0.989  55.151  1.00 22.28 ? 89  LEU A O   1 
ATOM   437  C  CB  . LEU A 1 61  ? 2.371   -3.350  55.210  1.00 25.32 ? 89  LEU A CB  1 
ATOM   438  C  CG  . LEU A 1 61  ? 3.443   -2.831  56.174  1.00 24.43 ? 89  LEU A CG  1 
ATOM   439  C  CD1 . LEU A 1 61  ? 3.678   -3.844  57.278  1.00 24.97 ? 89  LEU A CD1 1 
ATOM   440  C  CD2 . LEU A 1 61  ? 4.775   -2.448  55.455  1.00 28.69 ? 89  LEU A CD2 1 
ATOM   441  N  N   . LEU A 1 62  ? 0.430   -1.494  57.362  1.00 18.32 ? 90  LEU A N   1 
ATOM   442  C  CA  . LEU A 1 62  ? 0.279   -0.137  57.874  1.00 20.17 ? 90  LEU A CA  1 
ATOM   443  C  C   . LEU A 1 62  ? 1.590   0.284   58.517  1.00 20.89 ? 90  LEU A C   1 
ATOM   444  O  O   . LEU A 1 62  ? 2.235   -0.523  59.185  1.00 21.50 ? 90  LEU A O   1 
ATOM   445  C  CB  . LEU A 1 62  ? -0.814  -0.051  58.940  1.00 18.01 ? 90  LEU A CB  1 
ATOM   446  C  CG  . LEU A 1 62  ? -2.212  -0.552  58.541  1.00 22.01 ? 90  LEU A CG  1 
ATOM   447  C  CD1 . LEU A 1 62  ? -3.221  -0.233  59.615  1.00 18.54 ? 90  LEU A CD1 1 
ATOM   448  C  CD2 . LEU A 1 62  ? -2.634  0.066   57.234  1.00 23.59 ? 90  LEU A CD2 1 
ATOM   449  N  N   . THR A 1 63  ? 1.963   1.554   58.368  1.00 22.56 ? 91  THR A N   1 
ATOM   450  C  CA  . THR A 1 63  ? 3.163   2.042   59.037  1.00 20.21 ? 91  THR A CA  1 
ATOM   451  C  C   . THR A 1 63  ? 2.883   3.372   59.723  1.00 21.05 ? 91  THR A C   1 
ATOM   452  O  O   . THR A 1 63  ? 2.066   4.174   59.267  1.00 21.35 ? 91  THR A O   1 
ATOM   453  C  CB  . THR A 1 63  ? 4.329   2.215   58.063  1.00 27.04 ? 91  THR A CB  1 
ATOM   454  O  OG1 . THR A 1 63  ? 3.966   3.177   57.065  1.00 33.03 ? 91  THR A OG1 1 
ATOM   455  C  CG2 . THR A 1 63  ? 4.645   0.886   57.391  1.00 24.66 ? 91  THR A CG2 1 
ATOM   456  N  N   . SER A 1 64  ? 3.570   3.597   60.835  1.00 24.09 ? 92  SER A N   1 
ATOM   457  C  CA  . SER A 1 64  ? 3.641   4.919   61.453  1.00 23.46 ? 92  SER A CA  1 
ATOM   458  C  C   . SER A 1 64  ? 5.044   5.034   62.035  1.00 25.33 ? 92  SER A C   1 
ATOM   459  O  O   . SER A 1 64  ? 5.385   4.305   62.970  1.00 21.14 ? 92  SER A O   1 
ATOM   460  C  CB  . SER A 1 64  ? 2.572   5.093   62.530  1.00 21.73 ? 92  SER A CB  1 
ATOM   461  O  OG  . SER A 1 64  ? 2.452   6.441   62.942  1.00 22.18 ? 92  SER A OG  1 
ATOM   462  N  N   . GLY A 1 65  ? 5.861   5.930   61.490  1.00 26.39 ? 93  GLY A N   1 
ATOM   463  C  CA  . GLY A 1 65  ? 7.261   5.928   61.894  1.00 22.76 ? 93  GLY A CA  1 
ATOM   464  C  C   . GLY A 1 65  ? 7.886   4.567   61.621  1.00 24.44 ? 93  GLY A C   1 
ATOM   465  O  O   . GLY A 1 65  ? 7.826   4.041   60.505  1.00 29.00 ? 93  GLY A O   1 
ATOM   466  N  N   . ASP A 1 66  ? 8.489   3.968   62.647  1.00 22.11 ? 94  ASP A N   1 
ATOM   467  C  CA  . ASP A 1 66  ? 9.118   2.666   62.479  1.00 23.77 ? 94  ASP A CA  1 
ATOM   468  C  C   . ASP A 1 66  ? 8.177   1.512   62.794  1.00 24.66 ? 94  ASP A C   1 
ATOM   469  O  O   . ASP A 1 66  ? 8.548   0.358   62.572  1.00 23.80 ? 94  ASP A O   1 
ATOM   470  C  CB  . ASP A 1 66  ? 10.361  2.522   63.371  1.00 27.12 ? 94  ASP A CB  1 
ATOM   471  C  CG  . ASP A 1 66  ? 11.513  3.411   62.938  1.00 40.52 ? 94  ASP A CG  1 
ATOM   472  O  OD1 . ASP A 1 66  ? 11.508  3.895   61.785  1.00 36.81 ? 94  ASP A OD1 1 
ATOM   473  O  OD2 . ASP A 1 66  ? 12.447  3.590   63.754  1.00 48.13 ? 94  ASP A OD2 1 
ATOM   474  N  N   . LEU A 1 67  ? 6.990   1.795   63.317  1.00 24.97 ? 95  LEU A N   1 
ATOM   475  C  CA  . LEU A 1 67  ? 6.030   0.743   63.643  1.00 22.63 ? 95  LEU A CA  1 
ATOM   476  C  C   . LEU A 1 67  ? 5.400   0.189   62.370  1.00 22.07 ? 95  LEU A C   1 
ATOM   477  O  O   . LEU A 1 67  ? 4.956   0.951   61.512  1.00 22.43 ? 95  LEU A O   1 
ATOM   478  C  CB  . LEU A 1 67  ? 4.942   1.287   64.569  1.00 21.80 ? 95  LEU A CB  1 
ATOM   479  C  CG  . LEU A 1 67  ? 3.848   0.280   64.976  1.00 20.01 ? 95  LEU A CG  1 
ATOM   480  C  CD1 . LEU A 1 67  ? 4.408   -0.776  65.910  1.00 20.05 ? 95  LEU A CD1 1 
ATOM   481  C  CD2 . LEU A 1 67  ? 2.667   1.002   65.613  1.00 18.67 ? 95  LEU A CD2 1 
ATOM   482  N  N   . ARG A 1 68  ? 5.363   -1.142  62.250  1.00 20.82 ? 96  ARG A N   1 
ATOM   483  C  CA  . ARG A 1 68  ? 4.782   -1.815  61.092  1.00 20.55 ? 96  ARG A CA  1 
ATOM   484  C  C   . ARG A 1 68  ? 3.782   -2.845  61.585  1.00 17.34 ? 96  ARG A C   1 
ATOM   485  O  O   . ARG A 1 68  ? 4.157   -3.777  62.304  1.00 18.79 ? 96  ARG A O   1 
ATOM   486  C  CB  . ARG A 1 68  ? 5.841   -2.512  60.229  1.00 22.00 ? 96  ARG A CB  1 
ATOM   487  C  CG  . ARG A 1 68  ? 6.942   -1.598  59.685  1.00 27.66 ? 96  ARG A CG  1 
ATOM   488  C  CD  . ARG A 1 68  ? 8.081   -2.441  59.133  1.00 31.17 ? 96  ARG A CD  1 
ATOM   489  N  NE  . ARG A 1 68  ? 9.197   -1.613  58.702  1.00 40.90 ? 96  ARG A NE  1 
ATOM   490  C  CZ  . ARG A 1 68  ? 10.260  -1.379  59.458  1.00 40.05 ? 96  ARG A CZ  1 
ATOM   491  N  NH1 . ARG A 1 68  ? 10.320  -1.901  60.672  1.00 36.05 ? 96  ARG A NH1 1 
ATOM   492  N  NH2 . ARG A 1 68  ? 11.248  -0.613  59.009  1.00 48.10 ? 96  ARG A NH2 1 
ATOM   493  N  N   . PHE A 1 69  ? 2.534   -2.697  61.155  1.00 17.15 ? 97  PHE A N   1 
ATOM   494  C  CA  . PHE A 1 69  ? 1.447   -3.640  61.439  1.00 19.13 ? 97  PHE A CA  1 
ATOM   495  C  C   . PHE A 1 69  ? 1.039   -4.298  60.130  1.00 16.24 ? 97  PHE A C   1 
ATOM   496  O  O   . PHE A 1 69  ? 0.613   -3.605  59.197  1.00 18.79 ? 97  PHE A O   1 
ATOM   497  C  CB  . PHE A 1 69  ? 0.222   -2.936  62.034  1.00 18.29 ? 97  PHE A CB  1 
ATOM   498  C  CG  . PHE A 1 69  ? 0.269   -2.732  63.542  1.00 18.63 ? 97  PHE A CG  1 
ATOM   499  C  CD1 . PHE A 1 69  ? 1.376   -3.119  64.301  1.00 18.35 ? 97  PHE A CD1 1 
ATOM   500  C  CD2 . PHE A 1 69  ? -0.816  -2.126  64.192  1.00 19.94 ? 97  PHE A CD2 1 
ATOM   501  C  CE1 . PHE A 1 69  ? 1.387   -2.926  65.696  1.00 18.38 ? 97  PHE A CE1 1 
ATOM   502  C  CE2 . PHE A 1 69  ? -0.814  -1.928  65.562  1.00 20.18 ? 97  PHE A CE2 1 
ATOM   503  C  CZ  . PHE A 1 69  ? 0.293   -2.325  66.322  1.00 19.99 ? 97  PHE A CZ  1 
ATOM   504  N  N   . LEU A 1 70  ? 1.077   -5.630  60.097  1.00 17.49 ? 98  LEU A N   1 
ATOM   505  C  CA  . LEU A 1 70  ? 0.701   -6.424  58.934  1.00 17.95 ? 98  LEU A CA  1 
ATOM   506  C  C   . LEU A 1 70  ? -0.592  -7.168  59.239  1.00 16.76 ? 98  LEU A C   1 
ATOM   507  O  O   . LEU A 1 70  ? -0.703  -7.785  60.302  1.00 16.40 ? 98  LEU A O   1 
ATOM   508  C  CB  . LEU A 1 70  ? 1.806   -7.439  58.600  1.00 18.29 ? 98  LEU A CB  1 
ATOM   509  C  CG  . LEU A 1 70  ? 1.630   -8.265  57.326  1.00 20.29 ? 98  LEU A CG  1 
ATOM   510  C  CD1 . LEU A 1 70  ? 1.633   -7.356  56.093  1.00 21.84 ? 98  LEU A CD1 1 
ATOM   511  C  CD2 . LEU A 1 70  ? 2.742   -9.329  57.234  1.00 20.54 ? 98  LEU A CD2 1 
ATOM   512  N  N   . PHE A 1 71  ? -1.560  -7.108  58.311  1.00 17.96 ? 99  PHE A N   1 
ATOM   513  C  CA  . PHE A 1 71  ? -2.863  -7.767  58.454  1.00 16.40 ? 99  PHE A CA  1 
ATOM   514  C  C   . PHE A 1 71  ? -3.010  -8.765  57.325  1.00 16.38 ? 99  PHE A C   1 
ATOM   515  O  O   . PHE A 1 71  ? -2.930  -8.390  56.151  1.00 18.79 ? 99  PHE A O   1 
ATOM   516  C  CB  . PHE A 1 71  ? -4.007  -6.721  58.450  1.00 13.93 ? 99  PHE A CB  1 
ATOM   517  C  CG  . PHE A 1 71  ? -3.844  -5.686  59.529  1.00 15.17 ? 99  PHE A CG  1 
ATOM   518  C  CD1 . PHE A 1 71  ? -2.994  -4.596  59.340  1.00 17.04 ? 99  PHE A CD1 1 
ATOM   519  C  CD2 . PHE A 1 71  ? -4.446  -5.849  60.765  1.00 15.96 ? 99  PHE A CD2 1 
ATOM   520  C  CE1 . PHE A 1 71  ? -2.785  -3.664  60.345  1.00 16.14 ? 99  PHE A CE1 1 
ATOM   521  C  CE2 . PHE A 1 71  ? -4.234  -4.927  61.796  1.00 14.81 ? 99  PHE A CE2 1 
ATOM   522  C  CZ  . PHE A 1 71  ? -3.387  -3.827  61.579  1.00 15.24 ? 99  PHE A CZ  1 
ATOM   523  N  N   . THR A 1 72  ? -3.203  -10.037 57.676  1.00 17.01 ? 100 THR A N   1 
ATOM   524  C  CA  . THR A 1 72  ? -3.223  -11.113 56.698  1.00 16.50 ? 100 THR A CA  1 
ATOM   525  C  C   . THR A 1 72  ? -4.437  -11.999 56.912  1.00 18.54 ? 100 THR A C   1 
ATOM   526  O  O   . THR A 1 72  ? -4.795  -12.307 58.055  1.00 19.49 ? 100 THR A O   1 
ATOM   527  C  CB  . THR A 1 72  ? -1.941  -11.970 56.797  1.00 15.64 ? 100 THR A CB  1 
ATOM   528  O  OG1 . THR A 1 72  ? -0.795  -11.161 56.510  1.00 17.62 ? 100 THR A OG1 1 
ATOM   529  C  CG2 . THR A 1 72  ? -2.005  -13.114 55.825  1.00 18.57 ? 100 THR A CG2 1 
ATOM   530  N  N   . ALA A 1 73  ? -5.063  -12.402 55.809  1.00 19.89 ? 101 ALA A N   1 
ATOM   531  C  CA  . ALA A 1 73  ? -6.194  -13.328 55.811  1.00 15.86 ? 101 ALA A CA  1 
ATOM   532  C  C   . ALA A 1 73  ? -6.075  -14.249 54.604  1.00 16.85 ? 101 ALA A C   1 
ATOM   533  O  O   . ALA A 1 73  ? -5.521  -13.849 53.572  1.00 18.53 ? 101 ALA A O   1 
ATOM   534  C  CB  . ALA A 1 73  ? -7.536  -12.561 55.755  1.00 17.10 ? 101 ALA A CB  1 
ATOM   535  N  N   . PRO A 1 74  ? -6.602  -15.479 54.694  1.00 21.44 ? 102 PRO A N   1 
ATOM   536  C  CA  . PRO A 1 74  ? -6.518  -16.407 53.555  1.00 20.32 ? 102 PRO A CA  1 
ATOM   537  C  C   . PRO A 1 74  ? -7.615  -16.182 52.534  1.00 23.79 ? 102 PRO A C   1 
ATOM   538  O  O   . PRO A 1 74  ? -8.747  -15.859 52.885  1.00 23.23 ? 102 PRO A O   1 
ATOM   539  C  CB  . PRO A 1 74  ? -6.674  -17.789 54.206  1.00 23.60 ? 102 PRO A CB  1 
ATOM   540  C  CG  . PRO A 1 74  ? -7.492  -17.556 55.436  1.00 22.29 ? 102 PRO A CG  1 
ATOM   541  C  CD  . PRO A 1 74  ? -7.131  -16.123 55.909  1.00 22.13 ? 102 PRO A CD  1 
ATOM   542  N  N   . TYR A 1 75  ? -7.270  -16.347 51.258  1.00 21.42 ? 103 TYR A N   1 
ATOM   543  C  CA  . TYR A 1 75  ? -8.285  -16.488 50.227  1.00 22.28 ? 103 TYR A CA  1 
ATOM   544  C  C   . TYR A 1 75  ? -8.836  -17.909 50.256  1.00 26.38 ? 103 TYR A C   1 
ATOM   545  O  O   . TYR A 1 75  ? -8.393  -18.753 51.038  1.00 24.44 ? 103 TYR A O   1 
ATOM   546  C  CB  . TYR A 1 75  ? -7.712  -16.179 48.847  1.00 22.40 ? 103 TYR A CB  1 
ATOM   547  C  CG  . TYR A 1 75  ? -7.315  -14.738 48.626  1.00 22.97 ? 103 TYR A CG  1 
ATOM   548  C  CD1 . TYR A 1 75  ? -8.220  -13.693 48.820  1.00 19.82 ? 103 TYR A CD1 1 
ATOM   549  C  CD2 . TYR A 1 75  ? -6.038  -14.429 48.179  1.00 22.04 ? 103 TYR A CD2 1 
ATOM   550  C  CE1 . TYR A 1 75  ? -7.825  -12.357 48.593  1.00 18.18 ? 103 TYR A CE1 1 
ATOM   551  C  CE2 . TYR A 1 75  ? -5.639  -13.141 47.959  1.00 24.25 ? 103 TYR A CE2 1 
ATOM   552  C  CZ  . TYR A 1 75  ? -6.543  -12.101 48.165  1.00 22.96 ? 103 TYR A CZ  1 
ATOM   553  O  OH  . TYR A 1 75  ? -6.084  -10.837 47.911  1.00 22.80 ? 103 TYR A OH  1 
ATOM   554  N  N   . SER A 1 76  ? -9.815  -18.179 49.399  1.00 23.35 ? 104 SER A N   1 
ATOM   555  C  CA  . SER A 1 76  ? -10.267 -19.554 49.206  1.00 23.49 ? 104 SER A CA  1 
ATOM   556  C  C   . SER A 1 76  ? -9.086  -20.419 48.778  1.00 23.82 ? 104 SER A C   1 
ATOM   557  O  O   . SER A 1 76  ? -8.358  -20.045 47.850  1.00 23.72 ? 104 SER A O   1 
ATOM   558  C  CB  . SER A 1 76  ? -11.361 -19.637 48.138  1.00 23.82 ? 104 SER A CB  1 
ATOM   559  O  OG  . SER A 1 76  ? -11.615 -21.010 47.779  1.00 25.95 ? 104 SER A OG  1 
ATOM   560  N  N   . PRO A 1 77  ? -8.867  -21.570 49.410  1.00 25.30 ? 105 PRO A N   1 
ATOM   561  C  CA  . PRO A 1 77  ? -7.800  -22.470 48.931  1.00 29.96 ? 105 PRO A CA  1 
ATOM   562  C  C   . PRO A 1 77  ? -7.949  -22.855 47.468  1.00 29.42 ? 105 PRO A C   1 
ATOM   563  O  O   . PRO A 1 77  ? -6.950  -23.199 46.822  1.00 29.18 ? 105 PRO A O   1 
ATOM   564  C  CB  . PRO A 1 77  ? -7.935  -23.688 49.853  1.00 28.47 ? 105 PRO A CB  1 
ATOM   565  C  CG  . PRO A 1 77  ? -8.573  -23.152 51.093  1.00 30.43 ? 105 PRO A CG  1 
ATOM   566  C  CD  . PRO A 1 77  ? -9.559  -22.118 50.588  1.00 23.59 ? 105 PRO A CD  1 
ATOM   567  N  N   . SER A 1 78  ? -9.163  -22.776 46.913  1.00 29.31 ? 106 SER A N   1 
ATOM   568  C  CA  . SER A 1 78  ? -9.371  -23.159 45.524  1.00 28.76 ? 106 SER A CA  1 
ATOM   569  C  C   . SER A 1 78  ? -8.597  -22.288 44.549  1.00 26.43 ? 106 SER A C   1 
ATOM   570  O  O   . SER A 1 78  ? -8.315  -22.740 43.435  1.00 28.96 ? 106 SER A O   1 
ATOM   571  C  CB  . SER A 1 78  ? -10.871 -23.129 45.176  1.00 31.25 ? 106 SER A CB  1 
ATOM   572  O  OG  . SER A 1 78  ? -11.460 -21.874 45.478  1.00 33.23 ? 106 SER A OG  1 
ATOM   573  N  N   . LEU A 1 79  ? -8.243  -21.053 44.923  1.00 25.29 ? 107 LEU A N   1 
ATOM   574  C  CA  . LEU A 1 79  ? -7.519  -20.188 43.993  1.00 22.38 ? 107 LEU A CA  1 
ATOM   575  C  C   . LEU A 1 79  ? -6.099  -20.669 43.757  1.00 25.13 ? 107 LEU A C   1 
ATOM   576  O  O   . LEU A 1 79  ? -5.512  -20.373 42.713  1.00 27.88 ? 107 LEU A O   1 
ATOM   577  C  CB  . LEU A 1 79  ? -7.453  -18.754 44.515  1.00 22.68 ? 107 LEU A CB  1 
ATOM   578  C  CG  . LEU A 1 79  ? -8.766  -18.064 44.844  1.00 24.96 ? 107 LEU A CG  1 
ATOM   579  C  CD1 . LEU A 1 79  ? -8.483  -16.585 45.092  1.00 24.10 ? 107 LEU A CD1 1 
ATOM   580  C  CD2 . LEU A 1 79  ? -9.769  -18.251 43.724  1.00 26.14 ? 107 LEU A CD2 1 
ATOM   581  N  N   . SER A 1 80  ? -5.524  -21.365 44.730  1.00 29.08 ? 108 SER A N   1 
ATOM   582  C  CA  . SER A 1 80  ? -4.141  -21.824 44.662  1.00 24.94 ? 108 SER A CA  1 
ATOM   583  C  C   . SER A 1 80  ? -4.048  -23.344 44.693  1.00 26.47 ? 108 SER A C   1 
ATOM   584  O  O   . SER A 1 80  ? -3.004  -23.883 45.083  1.00 32.52 ? 108 SER A O   1 
ATOM   585  C  CB  . SER A 1 80  ? -3.336  -21.245 45.821  1.00 22.52 ? 108 SER A CB  1 
ATOM   586  O  OG  . SER A 1 80  ? -3.950  -21.622 47.042  1.00 22.87 ? 108 SER A OG  1 
ATOM   587  N  N   . ALA A 1 81  ? -5.116  -24.045 44.302  1.00 29.07 ? 109 ALA A N   1 
ATOM   588  C  CA  . ALA A 1 81  ? -5.163  -25.495 44.492  1.00 34.12 ? 109 ALA A CA  1 
ATOM   589  C  C   . ALA A 1 81  ? -4.068  -26.209 43.714  1.00 34.85 ? 109 ALA A C   1 
ATOM   590  O  O   . ALA A 1 81  ? -3.561  -27.250 44.161  1.00 38.37 ? 109 ALA A O   1 
ATOM   591  C  CB  . ALA A 1 81  ? -6.529  -26.045 44.083  1.00 34.16 ? 109 ALA A CB  1 
ATOM   592  N  N   . GLY A 1 82  ? -3.690  -25.676 42.556  1.00 30.93 ? 110 GLY A N   1 
ATOM   593  C  CA  . GLY A 1 82  ? -2.648  -26.304 41.771  1.00 37.12 ? 110 GLY A CA  1 
ATOM   594  C  C   . GLY A 1 82  ? -1.233  -25.941 42.169  1.00 38.29 ? 110 GLY A C   1 
ATOM   595  O  O   . GLY A 1 82  ? -0.289  -26.546 41.652  1.00 35.66 ? 110 GLY A O   1 
ATOM   596  N  N   . GLU A 1 83  ? -1.057  -24.988 43.081  1.00 26.75 ? 111 GLU A N   1 
ATOM   597  C  CA  . GLU A 1 83  ? 0.283   -24.611 43.510  1.00 27.13 ? 111 GLU A CA  1 
ATOM   598  C  C   . GLU A 1 83  ? 0.873   -25.647 44.463  1.00 27.65 ? 111 GLU A C   1 
ATOM   599  O  O   . GLU A 1 83  ? 0.156   -26.359 45.168  1.00 27.85 ? 111 GLU A O   1 
ATOM   600  C  CB  . GLU A 1 83  ? 0.277   -23.243 44.205  1.00 27.02 ? 111 GLU A CB  1 
ATOM   601  C  CG  . GLU A 1 83  ? -0.276  -22.109 43.364  1.00 27.34 ? 111 GLU A CG  1 
ATOM   602  C  CD  . GLU A 1 83  ? -0.284  -20.775 44.120  1.00 31.88 ? 111 GLU A CD  1 
ATOM   603  O  OE1 . GLU A 1 83  ? 0.356   -20.688 45.199  1.00 25.48 ? 111 GLU A OE1 1 
ATOM   604  O  OE2 . GLU A 1 83  ? -0.934  -19.825 43.629  1.00 28.91 ? 111 GLU A OE2 1 
ATOM   605  N  N   . ILE A 1 84  ? 2.200   -25.714 44.479  1.00 27.59 ? 112 ILE A N   1 
ATOM   606  C  CA  . ILE A 1 84  ? 2.951   -26.360 45.543  1.00 28.29 ? 112 ILE A CA  1 
ATOM   607  C  C   . ILE A 1 84  ? 3.898   -25.304 46.085  1.00 26.71 ? 112 ILE A C   1 
ATOM   608  O  O   . ILE A 1 84  ? 4.064   -24.239 45.491  1.00 28.95 ? 112 ILE A O   1 
ATOM   609  C  CB  . ILE A 1 84  ? 3.720   -27.609 45.054  1.00 24.25 ? 112 ILE A CB  1 
ATOM   610  C  CG1 . ILE A 1 84  ? 4.541   -27.250 43.823  1.00 25.27 ? 112 ILE A CG1 1 
ATOM   611  C  CG2 . ILE A 1 84  ? 2.742   -28.711 44.714  1.00 28.04 ? 112 ILE A CG2 1 
ATOM   612  C  CD1 . ILE A 1 84  ? 5.639   -28.291 43.483  1.00 29.24 ? 112 ILE A CD1 1 
ATOM   613  N  N   . LYS A 1 85  ? 4.526   -25.595 47.221  1.00 26.30 ? 113 LYS A N   1 
ATOM   614  C  CA  . LYS A 1 85  ? 5.433   -24.599 47.791  1.00 26.35 ? 113 LYS A CA  1 
ATOM   615  C  C   . LYS A 1 85  ? 6.482   -24.118 46.794  1.00 26.19 ? 113 LYS A C   1 
ATOM   616  O  O   . LYS A 1 85  ? 6.685   -22.898 46.710  1.00 24.38 ? 113 LYS A O   1 
ATOM   617  C  CB  . LYS A 1 85  ? 6.093   -25.149 49.068  1.00 27.09 ? 113 LYS A CB  1 
ATOM   618  C  CG  . LYS A 1 85  ? 5.196   -24.975 50.308  1.00 33.73 ? 113 LYS A CG  1 
ATOM   619  C  CD  A LYS A 1 85  ? 5.801   -25.664 51.524  0.20 37.12 ? 113 LYS A CD  1 
ATOM   620  C  CD  B LYS A 1 85  ? 5.857   -25.364 51.633  0.80 37.68 ? 113 LYS A CD  1 
ATOM   621  C  CE  A LYS A 1 85  ? 5.136   -25.196 52.808  0.20 38.70 ? 113 LYS A CE  1 
ATOM   622  C  CE  B LYS A 1 85  ? 4.818   -25.340 52.775  0.80 38.82 ? 113 LYS A CE  1 
ATOM   623  N  NZ  A LYS A 1 85  ? 5.383   -23.747 53.044  0.20 34.65 ? 113 LYS A NZ  1 
ATOM   624  N  NZ  B LYS A 1 85  ? 5.410   -25.504 54.139  0.80 40.98 ? 113 LYS A NZ  1 
ATOM   625  N  N   . PRO A 1 86  ? 7.135   -24.972 45.994  1.00 28.63 ? 114 PRO A N   1 
ATOM   626  C  CA  . PRO A 1 86  ? 8.089   -24.453 45.000  1.00 30.97 ? 114 PRO A CA  1 
ATOM   627  C  C   . PRO A 1 86  ? 7.476   -23.535 43.947  1.00 29.79 ? 114 PRO A C   1 
ATOM   628  O  O   . PRO A 1 86  ? 8.219   -22.776 43.317  1.00 35.25 ? 114 PRO A O   1 
ATOM   629  C  CB  . PRO A 1 86  ? 8.659   -25.732 44.363  1.00 30.39 ? 114 PRO A CB  1 
ATOM   630  C  CG  . PRO A 1 86  ? 8.542   -26.765 45.455  1.00 30.48 ? 114 PRO A CG  1 
ATOM   631  C  CD  . PRO A 1 86  ? 7.224   -26.441 46.117  1.00 29.93 ? 114 PRO A CD  1 
ATOM   632  N  N   . THR A 1 87  ? 6.161   -23.580 43.721  1.00 29.78 ? 115 THR A N   1 
ATOM   633  C  CA  . THR A 1 87  ? 5.512   -22.703 42.749  1.00 31.01 ? 115 THR A CA  1 
ATOM   634  C  C   . THR A 1 87  ? 4.566   -21.701 43.403  1.00 30.41 ? 115 THR A C   1 
ATOM   635  O  O   . THR A 1 87  ? 3.685   -21.164 42.724  1.00 30.64 ? 115 THR A O   1 
ATOM   636  C  CB  . THR A 1 87  ? 4.738   -23.516 41.702  1.00 29.47 ? 115 THR A CB  1 
ATOM   637  O  OG1 . THR A 1 87  ? 3.620   -24.175 42.310  1.00 26.23 ? 115 THR A OG1 1 
ATOM   638  C  CG2 . THR A 1 87  ? 5.644   -24.583 41.060  1.00 29.83 ? 115 THR A CG2 1 
ATOM   639  N  N   . THR A 1 88  ? 4.716   -21.437 44.699  1.00 28.67 ? 116 THR A N   1 
ATOM   640  C  CA  . THR A 1 88  ? 3.678   -20.669 45.381  1.00 25.54 ? 116 THR A CA  1 
ATOM   641  C  C   . THR A 1 88  ? 3.672   -19.218 44.913  1.00 22.80 ? 116 THR A C   1 
ATOM   642  O  O   . THR A 1 88  ? 4.706   -18.648 44.555  1.00 24.90 ? 116 THR A O   1 
ATOM   643  C  CB  . THR A 1 88  ? 3.855   -20.723 46.904  1.00 28.35 ? 116 THR A CB  1 
ATOM   644  O  OG1 . THR A 1 88  ? 2.686   -20.164 47.526  1.00 33.47 ? 116 THR A OG1 1 
ATOM   645  C  CG2 . THR A 1 88  ? 5.058   -19.927 47.345  1.00 29.44 ? 116 THR A CG2 1 
ATOM   646  N  N   . THR A 1 89  ? 2.480   -18.617 44.925  1.00 25.57 ? 117 THR A N   1 
ATOM   647  C  CA  . THR A 1 89  ? 2.345   -17.180 44.739  1.00 26.64 ? 117 THR A CA  1 
ATOM   648  C  C   . THR A 1 89  ? 2.255   -16.428 46.062  1.00 25.01 ? 117 THR A C   1 
ATOM   649  O  O   . THR A 1 89  ? 2.087   -15.202 46.050  1.00 26.09 ? 117 THR A O   1 
ATOM   650  C  CB  . THR A 1 89  ? 1.107   -16.858 43.892  1.00 24.13 ? 117 THR A CB  1 
ATOM   651  O  OG1 . THR A 1 89  ? -0.051  -17.378 44.541  1.00 25.75 ? 117 THR A OG1 1 
ATOM   652  C  CG2 . THR A 1 89  ? 1.222   -17.455 42.478  1.00 26.00 ? 117 THR A CG2 1 
ATOM   653  N  N   . ALA A 1 90  ? 2.338   -17.125 47.196  1.00 26.22 ? 118 ALA A N   1 
ATOM   654  C  CA  . ALA A 1 90  ? 2.342   -16.444 48.485  1.00 25.07 ? 118 ALA A CA  1 
ATOM   655  C  C   . ALA A 1 90  ? 3.620   -15.645 48.639  1.00 28.74 ? 118 ALA A C   1 
ATOM   656  O  O   . ALA A 1 90  ? 4.710   -16.123 48.312  1.00 30.77 ? 118 ALA A O   1 
ATOM   657  C  CB  . ALA A 1 90  ? 2.224   -17.443 49.634  1.00 25.77 ? 118 ALA A CB  1 
ATOM   658  N  N   . SER A 1 91  ? 3.493   -14.423 49.155  1.00 25.06 ? 119 SER A N   1 
ATOM   659  C  CA  . SER A 1 91  ? 4.674   -13.628 49.445  1.00 27.42 ? 119 SER A CA  1 
ATOM   660  C  C   . SER A 1 91  ? 5.259   -13.928 50.816  1.00 27.83 ? 119 SER A C   1 
ATOM   661  O  O   . SER A 1 91  ? 6.411   -13.569 51.077  1.00 28.98 ? 119 SER A O   1 
ATOM   662  C  CB  . SER A 1 91  ? 4.348   -12.132 49.350  1.00 29.66 ? 119 SER A CB  1 
ATOM   663  O  OG  . SER A 1 91  ? 3.224   -11.827 50.150  1.00 27.59 ? 119 SER A OG  1 
ATOM   664  N  N   . ILE A 1 92  ? 4.488   -14.544 51.703  1.00 27.48 ? 120 ILE A N   1 
ATOM   665  C  CA  . ILE A 1 92  ? 4.998   -14.966 53.004  1.00 27.50 ? 120 ILE A CA  1 
ATOM   666  C  C   . ILE A 1 92  ? 4.979   -16.489 53.029  1.00 29.76 ? 120 ILE A C   1 
ATOM   667  O  O   . ILE A 1 92  ? 3.940   -17.101 53.297  1.00 25.31 ? 120 ILE A O   1 
ATOM   668  C  CB  . ILE A 1 92  ? 4.188   -14.346 54.153  1.00 28.88 ? 120 ILE A CB  1 
ATOM   669  C  CG1 . ILE A 1 92  ? 4.245   -12.820 54.056  1.00 32.80 ? 120 ILE A CG1 1 
ATOM   670  C  CG2 . ILE A 1 92  ? 4.744   -14.805 55.509  1.00 23.24 ? 120 ILE A CG2 1 
ATOM   671  C  CD1 . ILE A 1 92  ? 3.405   -12.112 55.106  1.00 30.56 ? 120 ILE A CD1 1 
ATOM   672  N  N   . PRO A 1 93  ? 6.111   -17.141 52.749  1.00 31.11 ? 121 PRO A N   1 
ATOM   673  C  CA  . PRO A 1 93  ? 6.085   -18.597 52.513  1.00 27.80 ? 121 PRO A CA  1 
ATOM   674  C  C   . PRO A 1 93  ? 5.650   -19.413 53.716  1.00 26.60 ? 121 PRO A C   1 
ATOM   675  O  O   . PRO A 1 93  ? 5.204   -20.548 53.539  1.00 29.87 ? 121 PRO A O   1 
ATOM   676  C  CB  . PRO A 1 93  ? 7.536   -18.915 52.118  1.00 35.91 ? 121 PRO A CB  1 
ATOM   677  C  CG  . PRO A 1 93  ? 8.355   -17.798 52.729  1.00 35.02 ? 121 PRO A CG  1 
ATOM   678  C  CD  . PRO A 1 93  ? 7.462   -16.569 52.632  1.00 34.55 ? 121 PRO A CD  1 
ATOM   679  N  N   . SER A 1 94  ? 5.768   -18.883 54.932  1.00 25.55 ? 122 SER A N   1 
ATOM   680  C  CA  . SER A 1 94  ? 5.287   -19.611 56.097  1.00 25.19 ? 122 SER A CA  1 
ATOM   681  C  C   . SER A 1 94  ? 3.768   -19.695 56.169  1.00 23.25 ? 122 SER A C   1 
ATOM   682  O  O   . SER A 1 94  ? 3.247   -20.434 57.008  1.00 25.53 ? 122 SER A O   1 
ATOM   683  C  CB  . SER A 1 94  ? 5.802   -18.953 57.371  1.00 28.17 ? 122 SER A CB  1 
ATOM   684  O  OG  . SER A 1 94  ? 5.313   -17.624 57.480  1.00 29.05 ? 122 SER A OG  1 
ATOM   685  N  N   . PHE A 1 95  ? 3.047   -18.944 55.348  1.00 25.10 ? 123 PHE A N   1 
ATOM   686  C  CA  . PHE A 1 95  ? 1.595   -18.925 55.479  1.00 22.55 ? 123 PHE A CA  1 
ATOM   687  C  C   . PHE A 1 95  ? 0.989   -20.272 55.108  1.00 26.16 ? 123 PHE A C   1 
ATOM   688  O  O   . PHE A 1 95  ? 1.447   -20.953 54.184  1.00 28.49 ? 123 PHE A O   1 
ATOM   689  C  CB  . PHE A 1 95  ? 0.986   -17.831 54.606  1.00 20.50 ? 123 PHE A CB  1 
ATOM   690  C  CG  . PHE A 1 95  ? -0.497  -17.708 54.771  1.00 24.21 ? 123 PHE A CG  1 
ATOM   691  C  CD1 . PHE A 1 95  ? -1.026  -16.932 55.790  1.00 23.24 ? 123 PHE A CD1 1 
ATOM   692  C  CD2 . PHE A 1 95  ? -1.369  -18.414 53.939  1.00 26.96 ? 123 PHE A CD2 1 
ATOM   693  C  CE1 . PHE A 1 95  ? -2.398  -16.853 55.963  1.00 25.59 ? 123 PHE A CE1 1 
ATOM   694  C  CE2 . PHE A 1 95  ? -2.739  -18.316 54.093  1.00 24.70 ? 123 PHE A CE2 1 
ATOM   695  C  CZ  . PHE A 1 95  ? -3.254  -17.545 55.113  1.00 23.39 ? 123 PHE A CZ  1 
ATOM   696  N  N   . ASP A 1 96  ? -0.056  -20.648 55.835  1.00 22.90 ? 124 ASP A N   1 
ATOM   697  C  CA  . ASP A 1 96  ? -0.800  -21.864 55.536  1.00 25.56 ? 124 ASP A CA  1 
ATOM   698  C  C   . ASP A 1 96  ? -2.283  -21.617 55.779  1.00 25.80 ? 124 ASP A C   1 
ATOM   699  O  O   . ASP A 1 96  ? -2.652  -21.130 56.852  1.00 26.41 ? 124 ASP A O   1 
ATOM   700  C  CB  . ASP A 1 96  ? -0.281  -23.028 56.394  1.00 29.97 ? 124 ASP A CB  1 
ATOM   701  C  CG  . ASP A 1 96  ? -1.074  -24.285 56.192  1.00 31.14 ? 124 ASP A CG  1 
ATOM   702  O  OD1 . ASP A 1 96  ? -0.754  -25.034 55.241  1.00 40.92 ? 124 ASP A OD1 1 
ATOM   703  O  OD2 . ASP A 1 96  ? -1.991  -24.537 56.991  1.00 31.90 ? 124 ASP A OD2 1 
ATOM   704  N  N   . HIS A 1 97  ? -3.124  -21.917 54.775  1.00 26.00 ? 125 HIS A N   1 
ATOM   705  C  CA  . HIS A 1 97  ? -4.563  -21.661 54.901  1.00 25.13 ? 125 HIS A CA  1 
ATOM   706  C  C   . HIS A 1 97  ? -5.122  -22.300 56.167  1.00 29.06 ? 125 HIS A C   1 
ATOM   707  O  O   . HIS A 1 97  ? -5.853  -21.660 56.935  1.00 25.10 ? 125 HIS A O   1 
ATOM   708  C  CB  . HIS A 1 97  ? -5.345  -22.204 53.695  1.00 29.55 ? 125 HIS A CB  1 
ATOM   709  C  CG  . HIS A 1 97  ? -5.030  -21.558 52.379  1.00 27.86 ? 125 HIS A CG  1 
ATOM   710  N  ND1 . HIS A 1 97  ? -5.738  -20.476 51.893  1.00 31.28 ? 125 HIS A ND1 1 
ATOM   711  C  CD2 . HIS A 1 97  ? -4.164  -21.909 51.397  1.00 23.48 ? 125 HIS A CD2 1 
ATOM   712  C  CE1 . HIS A 1 97  ? -5.272  -20.146 50.702  1.00 24.78 ? 125 HIS A CE1 1 
ATOM   713  N  NE2 . HIS A 1 97  ? -4.321  -21.006 50.375  1.00 32.75 ? 125 HIS A NE2 1 
ATOM   714  N  N   . GLY A 1 98  ? -4.821  -23.587 56.374  1.00 26.56 ? 126 GLY A N   1 
ATOM   715  C  CA  . GLY A 1 98  ? -5.373  -24.295 57.519  1.00 24.03 ? 126 GLY A CA  1 
ATOM   716  C  C   . GLY A 1 98  ? -4.856  -23.785 58.850  1.00 22.79 ? 126 GLY A C   1 
ATOM   717  O  O   . GLY A 1 98  ? -5.615  -23.695 59.821  1.00 27.18 ? 126 GLY A O   1 
ATOM   718  N  N   . SER A 1 99  ? -3.552  -23.478 58.931  1.00 24.19 ? 127 SER A N   1 
ATOM   719  C  CA  . SER A 1 99  ? -3.017  -22.892 60.159  1.00 21.39 ? 127 SER A CA  1 
ATOM   720  C  C   . SER A 1 99  ? -3.715  -21.575 60.484  1.00 25.17 ? 127 SER A C   1 
ATOM   721  O  O   . SER A 1 99  ? -4.022  -21.289 61.646  1.00 24.46 ? 127 SER A O   1 
ATOM   722  C  CB  . SER A 1 99  ? -1.515  -22.655 60.029  1.00 26.85 ? 127 SER A CB  1 
ATOM   723  O  OG  . SER A 1 99  ? -0.813  -23.869 59.809  1.00 29.63 ? 127 SER A OG  1 
ATOM   724  N  N   . CYS A 1 100 ? -3.969  -20.765 59.465  1.00 22.74 ? 128 CYS A N   1 
ATOM   725  C  CA  . CYS A 1 100 ? -4.557  -19.448 59.706  1.00 23.46 ? 128 CYS A CA  1 
ATOM   726  C  C   . CYS A 1 100 ? -6.024  -19.556 60.117  1.00 21.72 ? 128 CYS A C   1 
ATOM   727  O  O   . CYS A 1 100 ? -6.467  -18.893 61.070  1.00 21.51 ? 128 CYS A O   1 
ATOM   728  C  CB  . CYS A 1 100 ? -4.393  -18.596 58.454  1.00 21.82 ? 128 CYS A CB  1 
ATOM   729  S  SG  . CYS A 1 100 ? -4.938  -16.876 58.710  1.00 24.05 ? 128 CYS A SG  1 
ATOM   730  N  N   . ARG A 1 101 ? -6.793  -20.409 59.439  1.00 25.63 ? 129 ARG A N   1 
ATOM   731  C  CA  . ARG A 1 101 ? -8.182  -20.591 59.838  1.00 22.99 ? 129 ARG A CA  1 
ATOM   732  C  C   . ARG A 1 101 ? -8.283  -21.211 61.228  1.00 25.59 ? 129 ARG A C   1 
ATOM   733  O  O   . ARG A 1 101 ? -9.131  -20.809 62.026  1.00 25.03 ? 129 ARG A O   1 
ATOM   734  C  CB  . ARG A 1 101 ? -8.918  -21.438 58.804  1.00 28.85 ? 129 ARG A CB  1 
ATOM   735  C  CG  . ARG A 1 101 ? -8.982  -20.743 57.454  1.00 29.02 ? 129 ARG A CG  1 
ATOM   736  C  CD  . ARG A 1 101 ? -10.109 -21.283 56.589  1.00 36.10 ? 129 ARG A CD  1 
ATOM   737  N  NE  . ARG A 1 101 ? -10.560 -20.257 55.653  1.00 36.98 ? 129 ARG A NE  1 
ATOM   738  C  CZ  . ARG A 1 101 ? -10.026 -20.064 54.452  1.00 36.37 ? 129 ARG A CZ  1 
ATOM   739  N  NH1 . ARG A 1 101 ? -9.021  -20.828 54.040  1.00 40.70 ? 129 ARG A NH1 1 
ATOM   740  N  NH2 . ARG A 1 101 ? -10.494 -19.111 53.665  1.00 30.25 ? 129 ARG A NH2 1 
ATOM   741  N  N   . SER A 1 102 ? -7.398  -22.156 61.554  1.00 25.99 ? 130 SER A N   1 
ATOM   742  C  CA  . SER A 1 102 ? -7.429  -22.761 62.883  1.00 27.16 ? 130 SER A CA  1 
ATOM   743  C  C   . SER A 1 102 ? -7.061  -21.761 63.972  1.00 24.94 ? 130 SER A C   1 
ATOM   744  O  O   . SER A 1 102 ? -7.694  -21.735 65.035  1.00 22.71 ? 130 SER A O   1 
ATOM   745  C  CB  . SER A 1 102 ? -6.488  -23.962 62.940  1.00 28.59 ? 130 SER A CB  1 
ATOM   746  O  OG  . SER A 1 102 ? -6.493  -24.497 64.247  1.00 39.80 ? 130 SER A OG  1 
ATOM   747  N  N   . PHE A 1 103 ? -5.995  -20.984 63.753  1.00 23.57 ? 131 PHE A N   1 
ATOM   748  C  CA  . PHE A 1 103 ? -5.640  -19.905 64.671  1.00 21.56 ? 131 PHE A CA  1 
ATOM   749  C  C   . PHE A 1 103 ? -6.838  -19.003 64.933  1.00 20.89 ? 131 PHE A C   1 
ATOM   750  O  O   . PHE A 1 103 ? -7.184  -18.714 66.085  1.00 20.67 ? 131 PHE A O   1 
ATOM   751  C  CB  . PHE A 1 103 ? -4.473  -19.101 64.077  1.00 17.69 ? 131 PHE A CB  1 
ATOM   752  C  CG  . PHE A 1 103 ? -3.990  -17.959 64.942  1.00 19.44 ? 131 PHE A CG  1 
ATOM   753  C  CD1 . PHE A 1 103 ? -4.667  -16.745 64.966  1.00 19.09 ? 131 PHE A CD1 1 
ATOM   754  C  CD2 . PHE A 1 103 ? -2.846  -18.088 65.704  1.00 22.92 ? 131 PHE A CD2 1 
ATOM   755  C  CE1 . PHE A 1 103 ? -4.216  -15.684 65.765  1.00 21.45 ? 131 PHE A CE1 1 
ATOM   756  C  CE2 . PHE A 1 103 ? -2.375  -17.031 66.488  1.00 20.63 ? 131 PHE A CE2 1 
ATOM   757  C  CZ  . PHE A 1 103 ? -3.079  -15.820 66.519  1.00 21.76 ? 131 PHE A CZ  1 
ATOM   758  N  N   . PHE A 1 104 ? -7.473  -18.521 63.867  1.00 22.09 ? 132 PHE A N   1 
ATOM   759  C  CA  . PHE A 1 104 ? -8.525  -17.528 64.065  1.00 20.33 ? 132 PHE A CA  1 
ATOM   760  C  C   . PHE A 1 104 ? -9.768  -18.149 64.694  1.00 22.59 ? 132 PHE A C   1 
ATOM   761  O  O   . PHE A 1 104 ? -10.417 -17.531 65.549  1.00 22.90 ? 132 PHE A O   1 
ATOM   762  C  CB  . PHE A 1 104 ? -8.876  -16.858 62.745  1.00 24.62 ? 132 PHE A CB  1 
ATOM   763  C  CG  . PHE A 1 104 ? -9.739  -15.639 62.916  1.00 24.31 ? 132 PHE A CG  1 
ATOM   764  C  CD1 . PHE A 1 104 ? -9.162  -14.393 63.027  1.00 22.02 ? 132 PHE A CD1 1 
ATOM   765  C  CD2 . PHE A 1 104 ? -11.120 -15.739 62.976  1.00 25.17 ? 132 PHE A CD2 1 
ATOM   766  C  CE1 . PHE A 1 104 ? -9.929  -13.270 63.207  1.00 22.45 ? 132 PHE A CE1 1 
ATOM   767  C  CE2 . PHE A 1 104 ? -11.904 -14.605 63.154  1.00 26.02 ? 132 PHE A CE2 1 
ATOM   768  C  CZ  . PHE A 1 104 ? -11.301 -13.357 63.266  1.00 21.58 ? 132 PHE A CZ  1 
ATOM   769  N  N   . SER A 1 105 ? -10.135 -19.357 64.261  1.00 22.82 ? 133 SER A N   1 
ATOM   770  C  CA  . SER A 1 105 ? -11.265 -20.037 64.884  1.00 25.00 ? 133 SER A CA  1 
ATOM   771  C  C   . SER A 1 105 ? -11.032 -20.218 66.378  1.00 24.12 ? 133 SER A C   1 
ATOM   772  O  O   . SER A 1 105 ? -11.941 -20.014 67.189  1.00 30.17 ? 133 SER A O   1 
ATOM   773  C  CB  . SER A 1 105 ? -11.502 -21.381 64.190  1.00 24.54 ? 133 SER A CB  1 
ATOM   774  O  OG  . SER A 1 105 ? -12.348 -22.197 64.977  1.00 40.81 ? 133 SER A OG  1 
ATOM   775  N  N   . SER A 1 106 ? -9.792  -20.513 66.769  1.00 22.97 ? 134 SER A N   1 
ATOM   776  C  CA  . SER A 1 106 ? -9.503  -20.800 68.164  1.00 23.19 ? 134 SER A CA  1 
ATOM   777  C  C   . SER A 1 106 ? -9.391  -19.535 68.999  1.00 22.88 ? 134 SER A C   1 
ATOM   778  O  O   . SER A 1 106 ? -9.927  -19.479 70.111  1.00 24.26 ? 134 SER A O   1 
ATOM   779  C  CB  . SER A 1 106 ? -8.206  -21.608 68.271  1.00 25.70 ? 134 SER A CB  1 
ATOM   780  O  OG  . SER A 1 106 ? -7.757  -21.615 69.604  1.00 29.77 ? 134 SER A OG  1 
ATOM   781  N  N   . HIS A 1 107 ? -8.692  -18.515 68.486  1.00 21.27 ? 135 HIS A N   1 
ATOM   782  C  CA  . HIS A 1 107 ? -8.314  -17.350 69.279  1.00 24.27 ? 135 HIS A CA  1 
ATOM   783  C  C   . HIS A 1 107 ? -9.063  -16.081 68.915  1.00 25.81 ? 135 HIS A C   1 
ATOM   784  O  O   . HIS A 1 107 ? -9.089  -15.149 69.728  1.00 24.47 ? 135 HIS A O   1 
ATOM   785  C  CB  . HIS A 1 107 ? -6.811  -17.054 69.129  1.00 22.39 ? 135 HIS A CB  1 
ATOM   786  C  CG  . HIS A 1 107 ? -5.934  -18.234 69.376  1.00 23.26 ? 135 HIS A CG  1 
ATOM   787  N  ND1 . HIS A 1 107 ? -5.865  -18.870 70.596  1.00 24.03 ? 135 HIS A ND1 1 
ATOM   788  C  CD2 . HIS A 1 107 ? -5.093  -18.902 68.554  1.00 20.26 ? 135 HIS A CD2 1 
ATOM   789  C  CE1 . HIS A 1 107 ? -5.016  -19.879 70.516  1.00 23.46 ? 135 HIS A CE1 1 
ATOM   790  N  NE2 . HIS A 1 107 ? -4.546  -19.932 69.281  1.00 25.10 ? 135 HIS A NE2 1 
ATOM   791  N  N   . GLY A 1 108 ? -9.672  -16.019 67.734  1.00 23.45 ? 136 GLY A N   1 
ATOM   792  C  CA  . GLY A 1 108 ? -10.214 -14.754 67.280  1.00 21.47 ? 136 GLY A CA  1 
ATOM   793  C  C   . GLY A 1 108 ? -9.053  -13.885 66.803  1.00 21.04 ? 136 GLY A C   1 
ATOM   794  O  O   . GLY A 1 108 ? -7.907  -14.314 66.714  1.00 20.26 ? 136 GLY A O   1 
ATOM   795  N  N   . LEU A 1 109 ? -9.385  -12.638 66.495  1.00 17.15 ? 137 LEU A N   1 
ATOM   796  C  CA  . LEU A 1 109 ? -8.398  -11.694 65.976  1.00 16.56 ? 137 LEU A CA  1 
ATOM   797  C  C   . LEU A 1 109 ? -7.257  -11.501 66.959  1.00 19.05 ? 137 LEU A C   1 
ATOM   798  O  O   . LEU A 1 109 ? -7.479  -11.230 68.145  1.00 20.29 ? 137 LEU A O   1 
ATOM   799  C  CB  . LEU A 1 109 ? -9.077  -10.346 65.698  1.00 16.59 ? 137 LEU A CB  1 
ATOM   800  C  CG  . LEU A 1 109 ? -8.128  -9.183  65.349  1.00 16.93 ? 137 LEU A CG  1 
ATOM   801  C  CD1 . LEU A 1 109 ? -7.499  -9.399  64.017  1.00 20.25 ? 137 LEU A CD1 1 
ATOM   802  C  CD2 . LEU A 1 109 ? -9.006  -7.903  65.344  1.00 20.24 ? 137 LEU A CD2 1 
ATOM   803  N  N   . GLY A 1 110 ? -6.034  -11.607 66.459  1.00 16.75 ? 138 GLY A N   1 
ATOM   804  C  CA  . GLY A 1 110 ? -4.880  -11.427 67.323  1.00 19.62 ? 138 GLY A CA  1 
ATOM   805  C  C   . GLY A 1 110 ? -3.577  -11.550 66.566  1.00 20.19 ? 138 GLY A C   1 
ATOM   806  O  O   . GLY A 1 110 ? -3.544  -11.742 65.346  1.00 19.20 ? 138 GLY A O   1 
ATOM   807  N  N   . VAL A 1 111 ? -2.492  -11.469 67.332  1.00 18.21 ? 139 VAL A N   1 
ATOM   808  C  CA  . VAL A 1 111 ? -1.146  -11.450 66.778  1.00 18.69 ? 139 VAL A CA  1 
ATOM   809  C  C   . VAL A 1 111 ? -0.687  -12.889 66.565  1.00 17.72 ? 139 VAL A C   1 
ATOM   810  O  O   . VAL A 1 111 ? -0.653  -13.680 67.505  1.00 18.62 ? 139 VAL A O   1 
ATOM   811  C  CB  . VAL A 1 111 ? -0.179  -10.703 67.705  1.00 16.55 ? 139 VAL A CB  1 
ATOM   812  C  CG1 . VAL A 1 111 ? 1.267   -10.878 67.210  1.00 16.29 ? 139 VAL A CG1 1 
ATOM   813  C  CG2 . VAL A 1 111 ? -0.559  -9.191  67.788  1.00 18.22 ? 139 VAL A CG2 1 
ATOM   814  N  N   . ARG A 1 112 ? -0.377  -13.229 65.324  1.00 17.67 ? 140 ARG A N   1 
ATOM   815  C  CA  . ARG A 1 112 ? 0.297   -14.476 64.985  1.00 18.34 ? 140 ARG A CA  1 
ATOM   816  C  C   . ARG A 1 112 ? 1.800   -14.352 65.138  1.00 18.78 ? 140 ARG A C   1 
ATOM   817  O  O   . ARG A 1 112 ? 2.453   -15.292 65.618  1.00 21.14 ? 140 ARG A O   1 
ATOM   818  C  CB  . ARG A 1 112 ? -0.045  -14.874 63.543  1.00 17.94 ? 140 ARG A CB  1 
ATOM   819  C  CG  . ARG A 1 112 ? 0.822   -15.986 62.937  1.00 20.67 ? 140 ARG A CG  1 
ATOM   820  C  CD  . ARG A 1 112 ? 0.826   -17.259 63.767  1.00 20.65 ? 140 ARG A CD  1 
ATOM   821  N  NE  . ARG A 1 112 ? 1.474   -18.319 62.986  1.00 26.31 ? 140 ARG A NE  1 
ATOM   822  C  CZ  . ARG A 1 112 ? 1.533   -19.599 63.335  1.00 27.01 ? 140 ARG A CZ  1 
ATOM   823  N  NH1 . ARG A 1 112 ? 1.036   -20.005 64.494  1.00 24.28 ? 140 ARG A NH1 1 
ATOM   824  N  NH2 . ARG A 1 112 ? 2.100   -20.470 62.514  1.00 24.74 ? 140 ARG A NH2 1 
ATOM   825  N  N   . ALA A 1 113 ? 2.379   -13.222 64.731  1.00 19.43 ? 141 ALA A N   1 
ATOM   826  C  CA  . ALA A 1 113 ? 3.837   -13.143 64.653  1.00 17.80 ? 141 ALA A CA  1 
ATOM   827  C  C   . ALA A 1 113 ? 4.357   -11.866 65.280  1.00 19.20 ? 141 ALA A C   1 
ATOM   828  O  O   . ALA A 1 113 ? 3.902   -10.762 64.952  1.00 18.91 ? 141 ALA A O   1 
ATOM   829  C  CB  . ALA A 1 113 ? 4.329   -13.235 63.200  1.00 17.98 ? 141 ALA A CB  1 
ATOM   830  N  N   . VAL A 1 114 ? 5.353   -12.029 66.146  1.00 18.98 ? 142 VAL A N   1 
ATOM   831  C  CA  . VAL A 1 114 ? 6.174   -10.941 66.656  1.00 18.78 ? 142 VAL A CA  1 
ATOM   832  C  C   . VAL A 1 114 ? 7.495   -11.035 65.911  1.00 22.07 ? 142 VAL A C   1 
ATOM   833  O  O   . VAL A 1 114 ? 8.234   -12.012 66.075  1.00 22.84 ? 142 VAL A O   1 
ATOM   834  C  CB  . VAL A 1 114 ? 6.380   -11.067 68.171  1.00 21.31 ? 142 VAL A CB  1 
ATOM   835  C  CG1 . VAL A 1 114 ? 7.379   -10.016 68.671  1.00 21.30 ? 142 VAL A CG1 1 
ATOM   836  C  CG2 . VAL A 1 114 ? 5.033   -11.016 68.906  1.00 20.96 ? 142 VAL A CG2 1 
ATOM   837  N  N   . ALA A 1 115 ? 7.779   -10.071 65.049  1.00 21.31 ? 143 ALA A N   1 
ATOM   838  C  CA  . ALA A 1 115 ? 8.916   -10.163 64.148  1.00 22.88 ? 143 ALA A CA  1 
ATOM   839  C  C   . ALA A 1 115 ? 10.014  -9.235  64.628  1.00 23.92 ? 143 ALA A C   1 
ATOM   840  O  O   . ALA A 1 115 ? 9.757   -8.069  64.937  1.00 21.45 ? 143 ALA A O   1 
ATOM   841  C  CB  . ALA A 1 115 ? 8.527   -9.816  62.713  1.00 19.10 ? 143 ALA A CB  1 
ATOM   842  N  N   . ILE A 1 116 ? 11.233  -9.761  64.714  1.00 23.04 ? 144 ILE A N   1 
ATOM   843  C  CA  . ILE A 1 116 ? 12.396  -8.951  65.054  1.00 22.39 ? 144 ILE A CA  1 
ATOM   844  C  C   . ILE A 1 116 ? 13.408  -9.012  63.918  1.00 25.04 ? 144 ILE A C   1 
ATOM   845  O  O   . ILE A 1 116 ? 13.557  -10.045 63.257  1.00 27.42 ? 144 ILE A O   1 
ATOM   846  C  CB  . ILE A 1 116 ? 13.042  -9.384  66.384  1.00 25.57 ? 144 ILE A CB  1 
ATOM   847  C  CG1 . ILE A 1 116 ? 13.384  -10.870 66.387  1.00 25.83 ? 144 ILE A CG1 1 
ATOM   848  C  CG2 . ILE A 1 116 ? 12.137  -9.013  67.563  1.00 24.86 ? 144 ILE A CG2 1 
ATOM   849  C  CD1 . ILE A 1 116 ? 14.298  -11.274 67.554  1.00 26.71 ? 144 ILE A CD1 1 
ATOM   850  N  N   . GLU A 1 117 ? 14.088  -7.889  63.679  1.00 24.19 ? 145 GLU A N   1 
ATOM   851  C  CA  . GLU A 1 117 ? 15.130  -7.850  62.668  1.00 28.72 ? 145 GLU A CA  1 
ATOM   852  C  C   . GLU A 1 117 ? 16.425  -8.313  63.312  1.00 26.61 ? 145 GLU A C   1 
ATOM   853  O  O   . GLU A 1 117 ? 16.787  -7.858  64.403  1.00 25.30 ? 145 GLU A O   1 
ATOM   854  C  CB  . GLU A 1 117 ? 15.313  -6.458  62.063  1.00 33.53 ? 145 GLU A CB  1 
ATOM   855  C  CG  . GLU A 1 117 ? 16.351  -6.467  60.934  1.00 30.95 ? 145 GLU A CG  1 
ATOM   856  C  CD  . GLU A 1 117 ? 16.607  -5.090  60.357  1.00 39.64 ? 145 GLU A CD  1 
ATOM   857  O  OE1 . GLU A 1 117 ? 17.487  -4.966  59.484  1.00 42.50 ? 145 GLU A OE1 1 
ATOM   858  O  OE2 . GLU A 1 117 ? 15.920  -4.135  60.762  1.00 42.32 ? 145 GLU A OE2 1 
ATOM   859  N  N   . VAL A 1 118 ? 17.087  -9.255  62.663  1.00 27.84 ? 146 VAL A N   1 
ATOM   860  C  CA  . VAL A 1 118 ? 18.329  -9.807  63.175  1.00 30.22 ? 146 VAL A CA  1 
ATOM   861  C  C   . VAL A 1 118 ? 19.396  -9.659  62.106  1.00 28.56 ? 146 VAL A C   1 
ATOM   862  O  O   . VAL A 1 118 ? 19.126  -9.294  60.962  1.00 27.31 ? 146 VAL A O   1 
ATOM   863  C  CB  . VAL A 1 118 ? 18.183  -11.279 63.596  1.00 27.40 ? 146 VAL A CB  1 
ATOM   864  C  CG1 . VAL A 1 118 ? 17.227  -11.414 64.794  1.00 25.05 ? 146 VAL A CG1 1 
ATOM   865  C  CG2 . VAL A 1 118 ? 17.736  -12.127 62.416  1.00 28.10 ? 146 VAL A CG2 1 
ATOM   866  N  N   . GLU A 1 119 ? 20.632  -9.976  62.495  1.00 33.97 ? 147 GLU A N   1 
ATOM   867  C  CA  . GLU A 1 119 ? 21.727  -9.887  61.545  1.00 33.38 ? 147 GLU A CA  1 
ATOM   868  C  C   . GLU A 1 119 ? 21.581  -10.929 60.449  1.00 27.97 ? 147 GLU A C   1 
ATOM   869  O  O   . GLU A 1 119 ? 21.795  -10.635 59.267  1.00 33.66 ? 147 GLU A O   1 
ATOM   870  C  CB  . GLU A 1 119 ? 23.055  -10.052 62.286  1.00 35.88 ? 147 GLU A CB  1 
ATOM   871  C  CG  . GLU A 1 119 ? 24.260  -9.903  61.424  1.00 43.60 ? 147 GLU A CG  1 
ATOM   872  C  CD  . GLU A 1 119 ? 25.542  -9.927  62.241  1.00 43.94 ? 147 GLU A CD  1 
ATOM   873  O  OE1 . GLU A 1 119 ? 26.211  -8.875  62.299  1.00 45.13 ? 147 GLU A OE1 1 
ATOM   874  O  OE2 . GLU A 1 119 ? 25.868  -10.994 62.823  1.00 41.66 ? 147 GLU A OE2 1 
ATOM   875  N  N   . ASP A 1 120 ? 21.203  -12.146 60.817  1.00 24.31 ? 148 ASP A N   1 
ATOM   876  C  CA  . ASP A 1 120 ? 21.104  -13.230 59.851  1.00 30.07 ? 148 ASP A CA  1 
ATOM   877  C  C   . ASP A 1 120 ? 20.044  -14.214 60.322  1.00 31.27 ? 148 ASP A C   1 
ATOM   878  O  O   . ASP A 1 120 ? 20.269  -14.955 61.283  1.00 29.33 ? 148 ASP A O   1 
ATOM   879  C  CB  . ASP A 1 120 ? 22.447  -13.929 59.679  1.00 35.69 ? 148 ASP A CB  1 
ATOM   880  C  CG  . ASP A 1 120 ? 22.429  -14.882 58.522  1.00 43.02 ? 148 ASP A CG  1 
ATOM   881  O  OD1 . ASP A 1 120 ? 22.200  -16.088 58.756  1.00 44.95 ? 148 ASP A OD1 1 
ATOM   882  O  OD2 . ASP A 1 120 ? 22.604  -14.409 57.375  1.00 47.15 ? 148 ASP A OD2 1 
ATOM   883  N  N   . ALA A 1 121 ? 18.903  -14.235 59.623  1.00 34.50 ? 149 ALA A N   1 
ATOM   884  C  CA  . ALA A 1 121 ? 17.755  -15.004 60.090  1.00 29.78 ? 149 ALA A CA  1 
ATOM   885  C  C   . ALA A 1 121 ? 18.043  -16.497 60.093  1.00 31.86 ? 149 ALA A C   1 
ATOM   886  O  O   . ALA A 1 121 ? 17.551  -17.226 60.965  1.00 32.64 ? 149 ALA A O   1 
ATOM   887  C  CB  . ALA A 1 121 ? 16.532  -14.691 59.223  1.00 28.32 ? 149 ALA A CB  1 
ATOM   888  N  N   . GLU A 1 122 ? 18.835  -16.980 59.130  1.00 34.32 ? 150 GLU A N   1 
ATOM   889  C  CA  . GLU A 1 122 ? 19.176  -18.403 59.132  1.00 36.61 ? 150 GLU A CA  1 
ATOM   890  C  C   . GLU A 1 122 ? 20.022  -18.763 60.348  1.00 33.18 ? 150 GLU A C   1 
ATOM   891  O  O   . GLU A 1 122 ? 19.774  -19.777 61.010  1.00 33.08 ? 150 GLU A O   1 
ATOM   892  C  CB  . GLU A 1 122 ? 19.894  -18.792 57.840  1.00 37.78 ? 150 GLU A CB  1 
ATOM   893  C  CG  . GLU A 1 122 ? 20.561  -20.161 57.933  1.00 42.79 ? 150 GLU A CG  1 
ATOM   894  C  CD  . GLU A 1 122 ? 20.539  -20.927 56.629  1.00 48.66 ? 150 GLU A CD  1 
ATOM   895  O  OE1 . GLU A 1 122 ? 20.107  -22.103 56.626  1.00 56.26 ? 150 GLU A OE1 1 
ATOM   896  O  OE2 . GLU A 1 122 ? 20.946  -20.345 55.601  1.00 53.83 ? 150 GLU A OE2 1 
ATOM   897  N  N   . SER A 1 123 ? 21.022  -17.936 60.671  1.00 32.77 ? 151 SER A N   1 
ATOM   898  C  CA  . SER A 1 123 ? 21.821  -18.197 61.866  1.00 32.92 ? 151 SER A CA  1 
ATOM   899  C  C   . SER A 1 123 ? 20.965  -18.121 63.126  1.00 33.34 ? 151 SER A C   1 
ATOM   900  O  O   . SER A 1 123 ? 21.017  -19.013 63.981  1.00 31.35 ? 151 SER A O   1 
ATOM   901  C  CB  . SER A 1 123 ? 22.990  -17.214 61.948  1.00 41.02 ? 151 SER A CB  1 
ATOM   902  O  OG  . SER A 1 123 ? 23.708  -17.200 60.729  1.00 44.30 ? 151 SER A OG  1 
ATOM   903  N  N   . ALA A 1 124 ? 20.153  -17.060 63.251  1.00 32.28 ? 152 ALA A N   1 
ATOM   904  C  CA  . ALA A 1 124 ? 19.274  -16.937 64.413  1.00 33.82 ? 152 ALA A CA  1 
ATOM   905  C  C   . ALA A 1 124 ? 18.384  -18.164 64.574  1.00 26.71 ? 152 ALA A C   1 
ATOM   906  O  O   . ALA A 1 124 ? 18.145  -18.623 65.697  1.00 30.72 ? 152 ALA A O   1 
ATOM   907  C  CB  . ALA A 1 124 ? 18.415  -15.668 64.297  1.00 29.50 ? 152 ALA A CB  1 
ATOM   908  N  N   . PHE A 1 125 ? 17.854  -18.690 63.467  1.00 30.00 ? 153 PHE A N   1 
ATOM   909  C  CA  . PHE A 1 125 ? 16.977  -19.854 63.540  1.00 28.44 ? 153 PHE A CA  1 
ATOM   910  C  C   . PHE A 1 125 ? 17.739  -21.097 63.996  1.00 32.61 ? 153 PHE A C   1 
ATOM   911  O  O   . PHE A 1 125 ? 17.292  -21.827 64.889  1.00 32.53 ? 153 PHE A O   1 
ATOM   912  C  CB  . PHE A 1 125 ? 16.333  -20.102 62.175  1.00 29.84 ? 153 PHE A CB  1 
ATOM   913  C  CG  . PHE A 1 125 ? 15.479  -21.336 62.121  1.00 30.37 ? 153 PHE A CG  1 
ATOM   914  C  CD1 . PHE A 1 125 ? 16.027  -22.574 61.784  1.00 33.98 ? 153 PHE A CD1 1 
ATOM   915  C  CD2 . PHE A 1 125 ? 14.116  -21.269 62.390  1.00 29.63 ? 153 PHE A CD2 1 
ATOM   916  C  CE1 . PHE A 1 125 ? 15.232  -23.707 61.740  1.00 34.71 ? 153 PHE A CE1 1 
ATOM   917  C  CE2 . PHE A 1 125 ? 13.329  -22.392 62.340  1.00 28.68 ? 153 PHE A CE2 1 
ATOM   918  C  CZ  . PHE A 1 125 ? 13.881  -23.620 62.009  1.00 35.12 ? 153 PHE A CZ  1 
ATOM   919  N  N   . SER A 1 126 ? 18.871  -21.371 63.361  1.00 33.74 ? 154 SER A N   1 
ATOM   920  C  CA  . SER A 1 126 ? 19.660  -22.547 63.724  1.00 35.04 ? 154 SER A CA  1 
ATOM   921  C  C   . SER A 1 126 ? 20.081  -22.491 65.188  1.00 31.35 ? 154 SER A C   1 
ATOM   922  O  O   . SER A 1 126 ? 19.818  -23.421 65.961  1.00 34.71 ? 154 SER A O   1 
ATOM   923  C  CB  . SER A 1 126 ? 20.872  -22.633 62.807  1.00 43.32 ? 154 SER A CB  1 
ATOM   924  O  OG  . SER A 1 126 ? 20.440  -22.775 61.462  1.00 50.70 ? 154 SER A OG  1 
ATOM   925  N  N   . ILE A 1 127 ? 20.691  -21.376 65.595  1.00 33.99 ? 155 ILE A N   1 
ATOM   926  C  CA  . ILE A 1 127 ? 21.091  -21.205 66.989  1.00 30.46 ? 155 ILE A CA  1 
ATOM   927  C  C   . ILE A 1 127 ? 19.894  -21.357 67.924  1.00 31.50 ? 155 ILE A C   1 
ATOM   928  O  O   . ILE A 1 127 ? 19.992  -22.005 68.973  1.00 29.76 ? 155 ILE A O   1 
ATOM   929  C  CB  . ILE A 1 127 ? 21.806  -19.851 67.173  1.00 36.39 ? 155 ILE A CB  1 
ATOM   930  C  CG1 . ILE A 1 127 ? 23.062  -19.783 66.292  1.00 39.66 ? 155 ILE A CG1 1 
ATOM   931  C  CG2 . ILE A 1 127 ? 22.178  -19.620 68.633  1.00 35.56 ? 155 ILE A CG2 1 
ATOM   932  C  CD1 . ILE A 1 127 ? 23.681  -18.406 66.183  1.00 37.92 ? 155 ILE A CD1 1 
ATOM   933  N  N   . SER A 1 128 ? 18.735  -20.781 67.561  1.00 31.53 ? 156 SER A N   1 
ATOM   934  C  CA  . SER A 1 128 ? 17.578  -20.862 68.448  1.00 28.55 ? 156 SER A CA  1 
ATOM   935  C  C   . SER A 1 128 ? 17.129  -22.299 68.635  1.00 27.55 ? 156 SER A C   1 
ATOM   936  O  O   . SER A 1 128 ? 16.841  -22.732 69.758  1.00 27.31 ? 156 SER A O   1 
ATOM   937  C  CB  . SER A 1 128 ? 16.409  -20.019 67.905  1.00 27.09 ? 156 SER A CB  1 
ATOM   938  O  OG  . SER A 1 128 ? 16.776  -18.666 67.838  1.00 28.91 ? 156 SER A OG  1 
ATOM   939  N  N   . VAL A 1 129 ? 17.006  -23.040 67.530  1.00 28.08 ? 157 VAL A N   1 
ATOM   940  C  CA  . VAL A 1 129 ? 16.550  -24.423 67.617  1.00 29.25 ? 157 VAL A CA  1 
ATOM   941  C  C   . VAL A 1 129 ? 17.607  -25.290 68.291  1.00 30.04 ? 157 VAL A C   1 
ATOM   942  O  O   . VAL A 1 129 ? 17.280  -26.159 69.109  1.00 31.52 ? 157 VAL A O   1 
ATOM   943  C  CB  . VAL A 1 129 ? 16.180  -24.948 66.219  1.00 32.71 ? 157 VAL A CB  1 
ATOM   944  C  CG1 . VAL A 1 129 ? 15.890  -26.456 66.254  1.00 30.06 ? 157 VAL A CG1 1 
ATOM   945  C  CG2 . VAL A 1 129 ? 14.954  -24.182 65.679  1.00 28.42 ? 157 VAL A CG2 1 
ATOM   946  N  N   . ALA A 1 130 ? 18.889  -25.040 67.996  1.00 28.25 ? 158 ALA A N   1 
ATOM   947  C  CA  . ALA A 1 130 ? 19.947  -25.754 68.709  1.00 36.05 ? 158 ALA A CA  1 
ATOM   948  C  C   . ALA A 1 130 ? 19.872  -25.508 70.206  1.00 39.98 ? 158 ALA A C   1 
ATOM   949  O  O   . ALA A 1 130 ? 20.402  -26.306 70.985  1.00 39.88 ? 158 ALA A O   1 
ATOM   950  C  CB  . ALA A 1 130 ? 21.324  -25.340 68.191  1.00 35.04 ? 158 ALA A CB  1 
ATOM   951  N  N   . ASN A 1 131 ? 19.211  -24.425 70.626  1.00 33.87 ? 159 ASN A N   1 
ATOM   952  C  CA  . ASN A 1 131 ? 19.108  -24.076 72.034  1.00 29.82 ? 159 ASN A CA  1 
ATOM   953  C  C   . ASN A 1 131 ? 17.699  -24.258 72.587  1.00 31.16 ? 159 ASN A C   1 
ATOM   954  O  O   . ASN A 1 131 ? 17.366  -23.685 73.627  1.00 39.07 ? 159 ASN A O   1 
ATOM   955  C  CB  . ASN A 1 131 ? 19.608  -22.647 72.242  1.00 31.45 ? 159 ASN A CB  1 
ATOM   956  C  CG  . ASN A 1 131 ? 21.123  -22.576 72.308  1.00 34.60 ? 159 ASN A CG  1 
ATOM   957  O  OD1 . ASN A 1 131 ? 21.705  -22.789 73.370  1.00 36.88 ? 159 ASN A OD1 1 
ATOM   958  N  ND2 . ASN A 1 131 ? 21.767  -22.274 71.181  1.00 31.96 ? 159 ASN A ND2 1 
ATOM   959  N  N   . GLY A 1 132 ? 16.863  -25.049 71.920  1.00 32.21 ? 160 GLY A N   1 
ATOM   960  C  CA  . GLY A 1 132 ? 15.612  -25.499 72.487  1.00 28.05 ? 160 GLY A CA  1 
ATOM   961  C  C   . GLY A 1 132 ? 14.361  -24.907 71.857  1.00 28.28 ? 160 GLY A C   1 
ATOM   962  O  O   . GLY A 1 132 ? 13.260  -25.299 72.249  1.00 28.37 ? 160 GLY A O   1 
ATOM   963  N  N   . ALA A 1 133 ? 14.488  -23.984 70.906  1.00 31.35 ? 161 ALA A N   1 
ATOM   964  C  CA  . ALA A 1 133 ? 13.300  -23.404 70.279  1.00 28.61 ? 161 ALA A CA  1 
ATOM   965  C  C   . ALA A 1 133 ? 12.562  -24.452 69.462  1.00 31.65 ? 161 ALA A C   1 
ATOM   966  O  O   . ALA A 1 133 ? 13.180  -25.247 68.745  1.00 32.04 ? 161 ALA A O   1 
ATOM   967  C  CB  . ALA A 1 133 ? 13.683  -22.240 69.367  1.00 26.16 ? 161 ALA A CB  1 
ATOM   968  N  N   . ILE A 1 134 ? 11.236  -24.439 69.547  1.00 29.94 ? 162 ILE A N   1 
ATOM   969  C  CA  . ILE A 1 134 ? 10.430  -25.309 68.695  1.00 26.71 ? 162 ILE A CA  1 
ATOM   970  C  C   . ILE A 1 134 ? 10.301  -24.641 67.335  1.00 33.33 ? 162 ILE A C   1 
ATOM   971  O  O   . ILE A 1 134 ? 9.761   -23.519 67.234  1.00 25.21 ? 162 ILE A O   1 
ATOM   972  C  CB  . ILE A 1 134 ? 9.052   -25.597 69.293  1.00 30.33 ? 162 ILE A CB  1 
ATOM   973  C  CG1 . ILE A 1 134 ? 9.179   -26.224 70.673  1.00 36.62 ? 162 ILE A CG1 1 
ATOM   974  C  CG2 . ILE A 1 134 ? 8.244   -26.503 68.361  1.00 31.37 ? 162 ILE A CG2 1 
ATOM   975  C  CD1 . ILE A 1 134 ? 7.874   -26.241 71.440  1.00 39.31 ? 162 ILE A CD1 1 
ATOM   976  N  N   . PRO A 1 135 ? 10.797  -25.272 66.275  1.00 28.91 ? 163 PRO A N   1 
ATOM   977  C  CA  . PRO A 1 135 ? 10.714  -24.655 64.948  1.00 26.88 ? 163 PRO A CA  1 
ATOM   978  C  C   . PRO A 1 135 ? 9.274   -24.556 64.470  1.00 27.55 ? 163 PRO A C   1 
ATOM   979  O  O   . PRO A 1 135 ? 8.426   -25.395 64.780  1.00 26.59 ? 163 PRO A O   1 
ATOM   980  C  CB  . PRO A 1 135 ? 11.544  -25.594 64.059  1.00 34.89 ? 163 PRO A CB  1 
ATOM   981  C  CG  . PRO A 1 135 ? 11.690  -26.860 64.835  1.00 31.47 ? 163 PRO A CG  1 
ATOM   982  C  CD  . PRO A 1 135 ? 11.637  -26.482 66.281  1.00 31.33 ? 163 PRO A CD  1 
ATOM   983  N  N   . SER A 1 136 ? 8.999   -23.492 63.733  1.00 27.78 ? 164 SER A N   1 
ATOM   984  C  CA  . SER A 1 136 ? 7.692   -23.317 63.117  1.00 23.77 ? 164 SER A CA  1 
ATOM   985  C  C   . SER A 1 136 ? 7.777   -23.204 61.608  1.00 20.82 ? 164 SER A C   1 
ATOM   986  O  O   . SER A 1 136 ? 6.999   -23.839 60.905  1.00 33.62 ? 164 SER A O   1 
ATOM   987  C  CB  . SER A 1 136 ? 7.001   -22.068 63.696  1.00 25.68 ? 164 SER A CB  1 
ATOM   988  O  OG  . SER A 1 136 ? 5.621   -22.087 63.351  1.00 25.59 ? 164 SER A OG  1 
ATOM   989  N  N   . SER A 1 137 ? 8.715   -22.417 61.091  1.00 25.82 ? 165 SER A N   1 
ATOM   990  C  CA  . SER A 1 137 ? 8.933   -22.313 59.668  1.00 27.01 ? 165 SER A CA  1 
ATOM   991  C  C   . SER A 1 137 ? 10.427  -22.131 59.429  1.00 31.28 ? 165 SER A C   1 
ATOM   992  O  O   . SER A 1 137 ? 11.031  -21.216 60.013  1.00 28.99 ? 165 SER A O   1 
ATOM   993  C  CB  . SER A 1 137 ? 8.165   -21.156 59.045  1.00 31.40 ? 165 SER A CB  1 
ATOM   994  O  OG  . SER A 1 137 ? 8.542   -20.983 57.694  1.00 34.94 ? 165 SER A OG  1 
ATOM   995  N  N   . PRO A 1 138 ? 11.042  -22.964 58.591  1.00 32.90 ? 166 PRO A N   1 
ATOM   996  C  CA  . PRO A 1 138 ? 12.490  -22.899 58.396  1.00 31.83 ? 166 PRO A CA  1 
ATOM   997  C  C   . PRO A 1 138 ? 12.881  -21.652 57.620  1.00 37.06 ? 166 PRO A C   1 
ATOM   998  O  O   . PRO A 1 138 ? 12.013  -20.980 57.034  1.00 34.53 ? 166 PRO A O   1 
ATOM   999  C  CB  . PRO A 1 138 ? 12.786  -24.178 57.595  1.00 37.22 ? 166 PRO A CB  1 
ATOM   1000 C  CG  . PRO A 1 138 ? 11.516  -24.438 56.851  1.00 41.27 ? 166 PRO A CG  1 
ATOM   1001 C  CD  . PRO A 1 138 ? 10.416  -24.026 57.786  1.00 36.41 ? 166 PRO A CD  1 
ATOM   1002 N  N   . PRO A 1 139 ? 14.171  -21.306 57.592  1.00 31.40 ? 167 PRO A N   1 
ATOM   1003 C  CA  . PRO A 1 139 ? 14.590  -20.080 56.900  1.00 33.44 ? 167 PRO A CA  1 
ATOM   1004 C  C   . PRO A 1 139 ? 14.325  -20.171 55.409  1.00 39.95 ? 167 PRO A C   1 
ATOM   1005 O  O   . PRO A 1 139 ? 14.641  -21.168 54.763  1.00 40.24 ? 167 PRO A O   1 
ATOM   1006 C  CB  . PRO A 1 139 ? 16.093  -19.998 57.198  1.00 36.63 ? 167 PRO A CB  1 
ATOM   1007 C  CG  . PRO A 1 139 ? 16.294  -20.840 58.393  1.00 31.19 ? 167 PRO A CG  1 
ATOM   1008 C  CD  . PRO A 1 139 ? 15.318  -21.962 58.251  1.00 29.87 ? 167 PRO A CD  1 
ATOM   1009 N  N   . ILE A 1 140 ? 13.734  -19.120 54.857  1.00 33.88 ? 168 ILE A N   1 
ATOM   1010 C  CA  . ILE A 1 140 ? 13.457  -19.072 53.432  1.00 35.46 ? 168 ILE A CA  1 
ATOM   1011 C  C   . ILE A 1 140 ? 13.987  -17.755 52.899  1.00 38.90 ? 168 ILE A C   1 
ATOM   1012 O  O   . ILE A 1 140 ? 13.778  -16.702 53.514  1.00 34.81 ? 168 ILE A O   1 
ATOM   1013 C  CB  . ILE A 1 140 ? 11.955  -19.233 53.133  1.00 37.02 ? 168 ILE A CB  1 
ATOM   1014 C  CG1 . ILE A 1 140 ? 11.472  -20.613 53.580  1.00 40.48 ? 168 ILE A CG1 1 
ATOM   1015 C  CG2 . ILE A 1 140 ? 11.683  -19.023 51.651  1.00 39.68 ? 168 ILE A CG2 1 
ATOM   1016 C  CD1 . ILE A 1 140 ? 10.189  -20.580 54.374  1.00 45.21 ? 168 ILE A CD1 1 
ATOM   1017 N  N   . VAL A 1 141 ? 14.697  -17.816 51.779  1.00 37.24 ? 169 VAL A N   1 
ATOM   1018 C  CA  . VAL A 1 141 ? 15.296  -16.632 51.181  1.00 40.92 ? 169 VAL A CA  1 
ATOM   1019 C  C   . VAL A 1 141 ? 14.360  -16.145 50.086  1.00 42.39 ? 169 VAL A C   1 
ATOM   1020 O  O   . VAL A 1 141 ? 13.977  -16.913 49.196  1.00 45.11 ? 169 VAL A O   1 
ATOM   1021 C  CB  . VAL A 1 141 ? 16.706  -16.923 50.647  1.00 41.44 ? 169 VAL A CB  1 
ATOM   1022 C  CG1 . VAL A 1 141 ? 17.352  -15.648 50.171  1.00 47.14 ? 169 VAL A CG1 1 
ATOM   1023 C  CG2 . VAL A 1 141 ? 17.539  -17.545 51.732  1.00 39.71 ? 169 VAL A CG2 1 
ATOM   1024 N  N   . LEU A 1 142 ? 13.968  -14.877 50.164  1.00 38.49 ? 170 LEU A N   1 
ATOM   1025 C  CA  . LEU A 1 142 ? 13.031  -14.292 49.220  1.00 38.81 ? 170 LEU A CA  1 
ATOM   1026 C  C   . LEU A 1 142 ? 13.803  -13.452 48.212  1.00 42.95 ? 170 LEU A C   1 
ATOM   1027 O  O   . LEU A 1 142 ? 14.420  -12.448 48.583  1.00 41.13 ? 170 LEU A O   1 
ATOM   1028 C  CB  . LEU A 1 142 ? 11.983  -13.447 49.947  1.00 34.97 ? 170 LEU A CB  1 
ATOM   1029 C  CG  . LEU A 1 142 ? 11.335  -14.115 51.164  1.00 35.07 ? 170 LEU A CG  1 
ATOM   1030 C  CD1 . LEU A 1 142 ? 10.480  -13.102 51.934  1.00 35.63 ? 170 LEU A CD1 1 
ATOM   1031 C  CD2 . LEU A 1 142 ? 10.519  -15.330 50.760  1.00 37.22 ? 170 LEU A CD2 1 
ATOM   1032 N  N   . ASN A 1 143 ? 13.777  -13.874 46.944  1.00 45.84 ? 171 ASN A N   1 
ATOM   1033 C  CA  . ASN A 1 143 ? 14.402  -13.121 45.855  1.00 49.66 ? 171 ASN A CA  1 
ATOM   1034 C  C   . ASN A 1 143 ? 15.874  -12.830 46.142  1.00 47.67 ? 171 ASN A C   1 
ATOM   1035 O  O   . ASN A 1 143 ? 16.415  -11.813 45.699  1.00 51.33 ? 171 ASN A O   1 
ATOM   1036 C  CB  . ASN A 1 143 ? 13.643  -11.819 45.589  1.00 47.81 ? 171 ASN A CB  1 
ATOM   1037 C  CG  . ASN A 1 143 ? 13.887  -11.274 44.195  1.00 53.11 ? 171 ASN A CG  1 
ATOM   1038 O  OD1 . ASN A 1 143 ? 14.190  -12.022 43.265  1.00 57.44 ? 171 ASN A OD1 1 
ATOM   1039 N  ND2 . ASN A 1 143 ? 13.764  -9.962  44.046  1.00 53.61 ? 171 ASN A ND2 1 
ATOM   1040 N  N   . GLU A 1 144 ? 16.518  -13.721 46.900  1.00 47.39 ? 172 GLU A N   1 
ATOM   1041 C  CA  . GLU A 1 144 ? 17.917  -13.580 47.316  1.00 49.35 ? 172 GLU A CA  1 
ATOM   1042 C  C   . GLU A 1 144 ? 18.194  -12.188 47.880  1.00 51.94 ? 172 GLU A C   1 
ATOM   1043 O  O   . GLU A 1 144 ? 19.173  -11.528 47.526  1.00 51.67 ? 172 GLU A O   1 
ATOM   1044 C  CB  . GLU A 1 144 ? 18.870  -13.905 46.161  1.00 55.54 ? 172 GLU A CB  1 
ATOM   1045 C  CG  . GLU A 1 144 ? 18.569  -15.215 45.413  1.00 58.48 ? 172 GLU A CG  1 
ATOM   1046 C  CD  . GLU A 1 144 ? 18.150  -16.370 46.328  1.00 62.81 ? 172 GLU A CD  1 
ATOM   1047 O  OE1 . GLU A 1 144 ? 16.934  -16.518 46.591  1.00 66.06 ? 172 GLU A OE1 1 
ATOM   1048 O  OE2 . GLU A 1 144 ? 19.030  -17.143 46.771  1.00 67.94 ? 172 GLU A OE2 1 
ATOM   1049 N  N   . ALA A 1 145 ? 17.314  -11.736 48.774  1.00 45.46 ? 173 ALA A N   1 
ATOM   1050 C  CA  . ALA A 1 145 ? 17.401  -10.375 49.289  1.00 45.64 ? 173 ALA A CA  1 
ATOM   1051 C  C   . ALA A 1 145 ? 17.013  -10.310 50.759  1.00 43.87 ? 173 ALA A C   1 
ATOM   1052 O  O   . ALA A 1 145 ? 17.596  -9.539  51.529  1.00 41.74 ? 173 ALA A O   1 
ATOM   1053 C  CB  . ALA A 1 145 ? 16.504  -9.440  48.476  1.00 48.24 ? 173 ALA A CB  1 
ATOM   1054 N  N   . VAL A 1 146 ? 16.010  -11.094 51.145  1.00 36.69 ? 174 VAL A N   1 
ATOM   1055 C  CA  . VAL A 1 146 ? 15.488  -11.102 52.504  1.00 39.16 ? 174 VAL A CA  1 
ATOM   1056 C  C   . VAL A 1 146 ? 15.319  -12.543 52.944  1.00 31.54 ? 174 VAL A C   1 
ATOM   1057 O  O   . VAL A 1 146 ? 14.835  -13.381 52.180  1.00 35.94 ? 174 VAL A O   1 
ATOM   1058 C  CB  . VAL A 1 146 ? 14.136  -10.359 52.621  1.00 35.47 ? 174 VAL A CB  1 
ATOM   1059 C  CG1 . VAL A 1 146 ? 13.752  -10.228 54.082  1.00 33.56 ? 174 VAL A CG1 1 
ATOM   1060 C  CG2 . VAL A 1 146 ? 14.213  -9.003  51.960  1.00 36.69 ? 174 VAL A CG2 1 
ATOM   1061 N  N   . THR A 1 147 ? 15.693  -12.824 54.182  1.00 32.98 ? 175 THR A N   1 
ATOM   1062 C  CA  . THR A 1 147 ? 15.554  -14.153 54.745  1.00 33.49 ? 175 THR A CA  1 
ATOM   1063 C  C   . THR A 1 147 ? 14.580  -14.101 55.909  1.00 30.29 ? 175 THR A C   1 
ATOM   1064 O  O   . THR A 1 147 ? 14.623  -13.177 56.726  1.00 28.03 ? 175 THR A O   1 
ATOM   1065 C  CB  . THR A 1 147 ? 16.906  -14.698 55.198  1.00 37.68 ? 175 THR A CB  1 
ATOM   1066 O  OG1 . THR A 1 147 ? 17.803  -14.702 54.076  1.00 37.74 ? 175 THR A OG1 1 
ATOM   1067 C  CG2 . THR A 1 147 ? 16.764  -16.109 55.749  1.00 35.00 ? 175 THR A CG2 1 
ATOM   1068 N  N   . ILE A 1 148 ? 13.718  -15.107 55.980  1.00 32.16 ? 176 ILE A N   1 
ATOM   1069 C  CA  . ILE A 1 148 ? 12.638  -15.162 56.949  1.00 29.74 ? 176 ILE A CA  1 
ATOM   1070 C  C   . ILE A 1 148 ? 12.602  -16.548 57.583  1.00 27.51 ? 176 ILE A C   1 
ATOM   1071 O  O   . ILE A 1 148 ? 12.750  -17.558 56.889  1.00 33.81 ? 176 ILE A O   1 
ATOM   1072 C  CB  . ILE A 1 148 ? 11.288  -14.819 56.274  1.00 29.88 ? 176 ILE A CB  1 
ATOM   1073 C  CG1 . ILE A 1 148 ? 10.193  -14.975 57.280  1.00 35.68 ? 176 ILE A CG1 1 
ATOM   1074 C  CG2 . ILE A 1 148 ? 11.002  -15.712 55.076  1.00 34.57 ? 176 ILE A CG2 1 
ATOM   1075 C  CD1 . ILE A 1 148 ? 10.494  -14.161 58.387  1.00 34.15 ? 176 ILE A CD1 1 
ATOM   1076 N  N   . ALA A 1 149 ? 12.390  -16.600 58.901  1.00 23.76 ? 177 ALA A N   1 
ATOM   1077 C  CA  . ALA A 1 149 ? 12.262  -17.868 59.618  1.00 22.36 ? 177 ALA A CA  1 
ATOM   1078 C  C   . ALA A 1 149 ? 11.451  -17.644 60.889  1.00 24.92 ? 177 ALA A C   1 
ATOM   1079 O  O   . ALA A 1 149 ? 11.332  -16.515 61.369  1.00 24.02 ? 177 ALA A O   1 
ATOM   1080 C  CB  . ALA A 1 149 ? 13.632  -18.459 59.970  1.00 30.09 ? 177 ALA A CB  1 
ATOM   1081 N  N   . GLU A 1 150 ? 10.876  -18.724 61.430  1.00 24.01 ? 178 GLU A N   1 
ATOM   1082 C  CA  . GLU A 1 150 ? 9.955   -18.599 62.556  1.00 25.28 ? 178 GLU A CA  1 
ATOM   1083 C  C   . GLU A 1 150 ? 10.100  -19.745 63.547  1.00 26.57 ? 178 GLU A C   1 
ATOM   1084 O  O   . GLU A 1 150 ? 10.208  -20.909 63.148  1.00 25.64 ? 178 GLU A O   1 
ATOM   1085 C  CB  . GLU A 1 150 ? 8.478   -18.547 62.061  1.00 22.44 ? 178 GLU A CB  1 
ATOM   1086 C  CG  . GLU A 1 150 ? 8.217   -17.375 61.142  1.00 26.52 ? 178 GLU A CG  1 
ATOM   1087 C  CD  . GLU A 1 150 ? 6.840   -17.417 60.466  1.00 23.08 ? 178 GLU A CD  1 
ATOM   1088 O  OE1 . GLU A 1 150 ? 5.982   -18.209 60.884  1.00 22.99 ? 178 GLU A OE1 1 
ATOM   1089 O  OE2 . GLU A 1 150 ? 6.650   -16.643 59.513  1.00 26.29 ? 178 GLU A OE2 1 
ATOM   1090 N  N   . VAL A 1 151 ? 10.037  -19.412 64.846  1.00 24.10 ? 179 VAL A N   1 
ATOM   1091 C  CA  . VAL A 1 151 ? 10.015  -20.386 65.933  1.00 25.72 ? 179 VAL A CA  1 
ATOM   1092 C  C   . VAL A 1 151 ? 8.842   -20.086 66.860  1.00 27.47 ? 179 VAL A C   1 
ATOM   1093 O  O   . VAL A 1 151 ? 8.338   -18.965 66.923  1.00 25.19 ? 179 VAL A O   1 
ATOM   1094 C  CB  . VAL A 1 151 ? 11.332  -20.394 66.749  1.00 23.87 ? 179 VAL A CB  1 
ATOM   1095 C  CG1 . VAL A 1 151 ? 12.488  -20.747 65.860  1.00 27.61 ? 179 VAL A CG1 1 
ATOM   1096 C  CG2 . VAL A 1 151 ? 11.560  -19.025 67.408  1.00 23.35 ? 179 VAL A CG2 1 
ATOM   1097 N  N   . LYS A 1 152 ? 8.417   -21.098 67.612  1.00 23.09 ? 180 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 152 ? 7.291   -20.874 68.518  1.00 27.14 ? 180 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 152 ? 7.706   -19.989 69.691  1.00 27.94 ? 180 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 152 ? 8.798   -20.131 70.240  1.00 25.78 ? 180 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 152 ? 6.730   -22.206 69.016  1.00 26.27 ? 180 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 152 ? 6.166   -23.054 67.900  1.00 27.58 ? 180 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 152 ? 5.428   -24.267 68.433  1.00 30.82 ? 180 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 152 ? 4.682   -24.974 67.312  1.00 39.11 ? 180 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 152 ? 3.706   -25.936 67.865  1.00 37.38 ? 180 LYS A NZ  1 
ATOM   1106 N  N   . LEU A 1 153 ? 6.834   -19.045 70.063  1.00 27.89 ? 181 LEU A N   1 
ATOM   1107 C  CA  . LEU A 1 153 ? 7.098   -18.149 71.189  1.00 23.21 ? 181 LEU A CA  1 
ATOM   1108 C  C   . LEU A 1 153 ? 6.293   -18.550 72.423  1.00 25.85 ? 181 LEU A C   1 
ATOM   1109 O  O   . LEU A 1 153 ? 6.879   -18.900 73.451  1.00 26.12 ? 181 LEU A O   1 
ATOM   1110 C  CB  . LEU A 1 153 ? 6.800   -16.687 70.791  1.00 22.02 ? 181 LEU A CB  1 
ATOM   1111 C  CG  . LEU A 1 153 ? 7.132   -15.551 71.779  1.00 23.56 ? 181 LEU A CG  1 
ATOM   1112 C  CD1 . LEU A 1 153 ? 8.631   -15.471 72.125  1.00 25.04 ? 181 LEU A CD1 1 
ATOM   1113 C  CD2 . LEU A 1 153 ? 6.649   -14.206 71.220  1.00 21.85 ? 181 LEU A CD2 1 
ATOM   1114 N  N   . TYR A 1 154 ? 4.960   -18.457 72.348  1.00 23.58 ? 182 TYR A N   1 
ATOM   1115 C  CA  . TYR A 1 154 ? 4.032   -18.985 73.339  1.00 23.50 ? 182 TYR A CA  1 
ATOM   1116 C  C   . TYR A 1 154 ? 2.683   -19.172 72.646  1.00 24.66 ? 182 TYR A C   1 
ATOM   1117 O  O   . TYR A 1 154 ? 2.382   -18.483 71.667  1.00 26.63 ? 182 TYR A O   1 
ATOM   1118 C  CB  . TYR A 1 154 ? 3.901   -18.077 74.587  1.00 22.86 ? 182 TYR A CB  1 
ATOM   1119 C  CG  . TYR A 1 154 ? 4.044   -16.581 74.336  1.00 25.81 ? 182 TYR A CG  1 
ATOM   1120 C  CD1 . TYR A 1 154 ? 3.101   -15.887 73.601  1.00 25.31 ? 182 TYR A CD1 1 
ATOM   1121 C  CD2 . TYR A 1 154 ? 5.118   -15.870 74.852  1.00 25.68 ? 182 TYR A CD2 1 
ATOM   1122 C  CE1 . TYR A 1 154 ? 3.231   -14.529 73.362  1.00 23.50 ? 182 TYR A CE1 1 
ATOM   1123 C  CE2 . TYR A 1 154 ? 5.262   -14.503 74.626  1.00 24.68 ? 182 TYR A CE2 1 
ATOM   1124 C  CZ  . TYR A 1 154 ? 4.315   -13.838 73.873  1.00 25.11 ? 182 TYR A CZ  1 
ATOM   1125 O  OH  . TYR A 1 154 ? 4.457   -12.484 73.649  1.00 23.39 ? 182 TYR A OH  1 
ATOM   1126 N  N   . GLY A 1 155 ? 1.891   -20.123 73.142  1.00 25.23 ? 183 GLY A N   1 
ATOM   1127 C  CA  . GLY A 1 155 ? 0.642   -20.471 72.476  1.00 24.44 ? 183 GLY A CA  1 
ATOM   1128 C  C   . GLY A 1 155 ? 0.858   -20.717 70.996  1.00 26.10 ? 183 GLY A C   1 
ATOM   1129 O  O   . GLY A 1 155 ? 1.759   -21.456 70.596  1.00 27.07 ? 183 GLY A O   1 
ATOM   1130 N  N   . ASP A 1 156 ? 0.043   -20.071 70.158  1.00 23.45 ? 184 ASP A N   1 
ATOM   1131 C  CA  . ASP A 1 156 ? 0.203   -20.120 68.707  1.00 20.35 ? 184 ASP A CA  1 
ATOM   1132 C  C   . ASP A 1 156 ? 0.866   -18.863 68.141  1.00 23.97 ? 184 ASP A C   1 
ATOM   1133 O  O   . ASP A 1 156 ? 0.739   -18.579 66.939  1.00 22.71 ? 184 ASP A O   1 
ATOM   1134 C  CB  . ASP A 1 156 ? -1.158  -20.367 68.052  1.00 19.78 ? 184 ASP A CB  1 
ATOM   1135 C  CG  . ASP A 1 156 ? -1.709  -21.743 68.403  1.00 26.56 ? 184 ASP A CG  1 
ATOM   1136 O  OD1 . ASP A 1 156 ? -0.900  -22.688 68.422  1.00 29.25 ? 184 ASP A OD1 1 
ATOM   1137 O  OD2 . ASP A 1 156 ? -2.916  -21.882 68.651  1.00 28.09 ? 184 ASP A OD2 1 
ATOM   1138 N  N   . VAL A 1 157 ? 1.578   -18.128 68.973  1.00 21.81 ? 185 VAL A N   1 
ATOM   1139 C  CA  . VAL A 1 157 ? 2.342   -16.956 68.558  1.00 19.57 ? 185 VAL A CA  1 
ATOM   1140 C  C   . VAL A 1 157 ? 3.754   -17.398 68.198  1.00 21.41 ? 185 VAL A C   1 
ATOM   1141 O  O   . VAL A 1 157 ? 4.374   -18.177 68.934  1.00 22.82 ? 185 VAL A O   1 
ATOM   1142 C  CB  . VAL A 1 157 ? 2.369   -15.897 69.674  1.00 22.37 ? 185 VAL A CB  1 
ATOM   1143 C  CG1 . VAL A 1 157 ? 3.125   -14.625 69.187  1.00 17.98 ? 185 VAL A CG1 1 
ATOM   1144 C  CG2 . VAL A 1 157 ? 0.950   -15.531 70.105  1.00 22.70 ? 185 VAL A CG2 1 
ATOM   1145 N  N   . VAL A 1 158 ? 4.272   -16.908 67.073  1.00 21.49 ? 186 VAL A N   1 
ATOM   1146 C  CA  . VAL A 1 158 ? 5.627   -17.228 66.655  1.00 24.58 ? 186 VAL A CA  1 
ATOM   1147 C  C   . VAL A 1 158 ? 6.497   -15.987 66.804  1.00 25.17 ? 186 VAL A C   1 
ATOM   1148 O  O   . VAL A 1 158 ? 6.044   -14.844 66.638  1.00 20.50 ? 186 VAL A O   1 
ATOM   1149 C  CB  . VAL A 1 158 ? 5.699   -17.776 65.207  1.00 21.32 ? 186 VAL A CB  1 
ATOM   1150 C  CG1 . VAL A 1 158 ? 4.854   -19.040 65.065  1.00 22.70 ? 186 VAL A CG1 1 
ATOM   1151 C  CG2 . VAL A 1 158 ? 5.247   -16.710 64.184  1.00 24.47 ? 186 VAL A CG2 1 
ATOM   1152 N  N   . LEU A 1 159 ? 7.757   -16.222 67.157  1.00 23.29 ? 187 LEU A N   1 
ATOM   1153 C  CA  . LEU A 1 159 ? 8.788   -15.207 67.044  1.00 21.16 ? 187 LEU A CA  1 
ATOM   1154 C  C   . LEU A 1 159 ? 9.390   -15.353 65.655  1.00 25.80 ? 187 LEU A C   1 
ATOM   1155 O  O   . LEU A 1 159 ? 9.894   -16.424 65.297  1.00 27.59 ? 187 LEU A O   1 
ATOM   1156 C  CB  . LEU A 1 159 ? 9.844   -15.387 68.137  1.00 23.70 ? 187 LEU A CB  1 
ATOM   1157 C  CG  . LEU A 1 159 ? 10.929  -14.330 68.295  1.00 23.52 ? 187 LEU A CG  1 
ATOM   1158 C  CD1 . LEU A 1 159 ? 10.350  -12.955 68.676  1.00 19.13 ? 187 LEU A CD1 1 
ATOM   1159 C  CD2 . LEU A 1 159 ? 11.972  -14.804 69.333  1.00 23.65 ? 187 LEU A CD2 1 
ATOM   1160 N  N   . ARG A 1 160 ? 9.296   -14.304 64.859  1.00 20.01 ? 188 ARG A N   1 
ATOM   1161 C  CA  . ARG A 1 160 ? 9.706   -14.336 63.462  1.00 21.01 ? 188 ARG A CA  1 
ATOM   1162 C  C   . ARG A 1 160 ? 11.020  -13.576 63.302  1.00 25.42 ? 188 ARG A C   1 
ATOM   1163 O  O   . ARG A 1 160 ? 11.133  -12.429 63.738  1.00 23.56 ? 188 ARG A O   1 
ATOM   1164 C  CB  . ARG A 1 160 ? 8.615   -13.718 62.582  1.00 24.39 ? 188 ARG A CB  1 
ATOM   1165 C  CG  . ARG A 1 160 ? 9.040   -13.486 61.158  1.00 23.35 ? 188 ARG A CG  1 
ATOM   1166 C  CD  . ARG A 1 160 ? 7.923   -12.907 60.284  1.00 22.31 ? 188 ARG A CD  1 
ATOM   1167 N  NE  . ARG A 1 160 ? 6.859   -13.870 60.023  1.00 19.63 ? 188 ARG A NE  1 
ATOM   1168 C  CZ  . ARG A 1 160 ? 5.617   -13.528 59.698  1.00 22.86 ? 188 ARG A CZ  1 
ATOM   1169 N  NH1 . ARG A 1 160 ? 5.287   -12.248 59.603  1.00 23.73 ? 188 ARG A NH1 1 
ATOM   1170 N  NH2 . ARG A 1 160 ? 4.705   -14.467 59.493  1.00 20.24 ? 188 ARG A NH2 1 
ATOM   1171 N  N   . TYR A 1 161 ? 12.017  -14.211 62.686  1.00 23.32 ? 189 TYR A N   1 
ATOM   1172 C  CA  . TYR A 1 161 ? 13.291  -13.550 62.414  1.00 22.86 ? 189 TYR A CA  1 
ATOM   1173 C  C   . TYR A 1 161 ? 13.327  -13.058 60.972  1.00 21.20 ? 189 TYR A C   1 
ATOM   1174 O  O   . TYR A 1 161 ? 12.984  -13.808 60.058  1.00 25.32 ? 189 TYR A O   1 
ATOM   1175 C  CB  . TYR A 1 161 ? 14.460  -14.521 62.653  1.00 23.83 ? 189 TYR A CB  1 
ATOM   1176 C  CG  . TYR A 1 161 ? 14.495  -15.135 64.031  1.00 21.81 ? 189 TYR A CG  1 
ATOM   1177 C  CD1 . TYR A 1 161 ? 14.384  -14.347 65.170  1.00 24.55 ? 189 TYR A CD1 1 
ATOM   1178 C  CD2 . TYR A 1 161 ? 14.643  -16.509 64.193  1.00 25.03 ? 189 TYR A CD2 1 
ATOM   1179 C  CE1 . TYR A 1 161 ? 14.414  -14.905 66.430  1.00 23.14 ? 189 TYR A CE1 1 
ATOM   1180 C  CE2 . TYR A 1 161 ? 14.669  -17.082 65.452  1.00 27.39 ? 189 TYR A CE2 1 
ATOM   1181 C  CZ  . TYR A 1 161 ? 14.580  -16.278 66.563  1.00 26.03 ? 189 TYR A CZ  1 
ATOM   1182 O  OH  . TYR A 1 161 ? 14.608  -16.849 67.813  1.00 26.85 ? 189 TYR A OH  1 
ATOM   1183 N  N   . VAL A 1 162 ? 13.762  -11.815 60.764  1.00 24.34 ? 190 VAL A N   1 
ATOM   1184 C  CA  . VAL A 1 162 ? 13.898  -11.242 59.424  1.00 25.82 ? 190 VAL A CA  1 
ATOM   1185 C  C   . VAL A 1 162 ? 15.291  -10.634 59.298  1.00 29.97 ? 190 VAL A C   1 
ATOM   1186 O  O   . VAL A 1 162 ? 15.715  -9.878  60.178  1.00 29.22 ? 190 VAL A O   1 
ATOM   1187 C  CB  . VAL A 1 162 ? 12.829  -10.173 59.136  1.00 27.08 ? 190 VAL A CB  1 
ATOM   1188 C  CG1 . VAL A 1 162 ? 13.029  -9.599  57.764  1.00 31.17 ? 190 VAL A CG1 1 
ATOM   1189 C  CG2 . VAL A 1 162 ? 11.448  -10.787 59.204  1.00 31.62 ? 190 VAL A CG2 1 
ATOM   1190 N  N   . SER A 1 163 ? 15.982  -10.919 58.189  1.00 28.35 ? 191 SER A N   1 
ATOM   1191 C  CA  . SER A 1 163 ? 17.277  -10.288 57.941  1.00 30.43 ? 191 SER A CA  1 
ATOM   1192 C  C   . SER A 1 163 ? 17.377  -9.856  56.485  1.00 29.20 ? 191 SER A C   1 
ATOM   1193 O  O   . SER A 1 163 ? 16.889  -10.550 55.592  1.00 31.92 ? 191 SER A O   1 
ATOM   1194 C  CB  . SER A 1 163 ? 18.454  -11.221 58.272  1.00 29.45 ? 191 SER A CB  1 
ATOM   1195 O  OG  . SER A 1 163 ? 18.426  -12.364 57.453  1.00 29.08 ? 191 SER A OG  1 
ATOM   1196 N  N   . TYR A 1 164 ? 18.015  -8.709  56.254  1.00 28.35 ? 192 TYR A N   1 
ATOM   1197 C  CA  . TYR A 1 164 ? 18.147  -8.121  54.929  1.00 33.72 ? 192 TYR A CA  1 
ATOM   1198 C  C   . TYR A 1 164 ? 19.604  -8.120  54.483  1.00 39.20 ? 192 TYR A C   1 
ATOM   1199 O  O   . TYR A 1 164 ? 20.498  -7.754  55.252  1.00 40.26 ? 192 TYR A O   1 
ATOM   1200 C  CB  . TYR A 1 164 ? 17.623  -6.684  54.916  1.00 33.77 ? 192 TYR A CB  1 
ATOM   1201 C  CG  . TYR A 1 164 ? 16.134  -6.594  55.147  1.00 37.97 ? 192 TYR A CG  1 
ATOM   1202 C  CD1 . TYR A 1 164 ? 15.261  -6.402  54.089  1.00 40.10 ? 192 TYR A CD1 1 
ATOM   1203 C  CD2 . TYR A 1 164 ? 15.604  -6.718  56.423  1.00 36.21 ? 192 TYR A CD2 1 
ATOM   1204 C  CE1 . TYR A 1 164 ? 13.888  -6.327  54.298  1.00 43.12 ? 192 TYR A CE1 1 
ATOM   1205 C  CE2 . TYR A 1 164 ? 14.238  -6.644  56.644  1.00 37.37 ? 192 TYR A CE2 1 
ATOM   1206 C  CZ  . TYR A 1 164 ? 13.386  -6.456  55.581  1.00 44.97 ? 192 TYR A CZ  1 
ATOM   1207 O  OH  . TYR A 1 164 ? 12.023  -6.381  55.807  1.00 45.87 ? 192 TYR A OH  1 
ATOM   1208 N  N   . LYS A 1 165 ? 19.837  -8.516  53.231  1.00 44.06 ? 193 LYS A N   1 
ATOM   1209 C  CA  . LYS A 1 165 ? 21.183  -8.417  52.673  1.00 48.99 ? 193 LYS A CA  1 
ATOM   1210 C  C   . LYS A 1 165 ? 21.638  -6.967  52.626  1.00 51.87 ? 193 LYS A C   1 
ATOM   1211 O  O   . LYS A 1 165 ? 22.700  -6.616  53.156  1.00 52.84 ? 193 LYS A O   1 
ATOM   1212 C  CB  . LYS A 1 165 ? 21.227  -9.041  51.277  1.00 50.56 ? 193 LYS A CB  1 
ATOM   1213 N  N   . ALA A 1 166 ? 20.832  -6.103  52.019  1.00 51.03 ? 194 ALA A N   1 
ATOM   1214 C  CA  . ALA A 1 166 ? 21.201  -4.701  51.895  1.00 54.98 ? 194 ALA A CA  1 
ATOM   1215 C  C   . ALA A 1 166 ? 20.372  -3.829  52.832  1.00 52.78 ? 194 ALA A C   1 
ATOM   1216 O  O   . ALA A 1 166 ? 20.662  -3.740  54.025  1.00 59.59 ? 194 ALA A O   1 
ATOM   1217 C  CB  . ALA A 1 166 ? 21.043  -4.238  50.456  1.00 58.25 ? 194 ALA A CB  1 
ATOM   1218 N  N   . GLU A 1 173 ? 9.464   -2.065  49.948  1.00 60.56 ? 201 GLU A N   1 
ATOM   1219 C  CA  . GLU A 1 173 ? 10.741  -2.560  50.454  1.00 58.66 ? 201 GLU A CA  1 
ATOM   1220 C  C   . GLU A 1 173 ? 10.546  -3.425  51.703  1.00 53.58 ? 201 GLU A C   1 
ATOM   1221 O  O   . GLU A 1 173 ? 11.520  -3.860  52.322  1.00 53.13 ? 201 GLU A O   1 
ATOM   1222 C  CB  . GLU A 1 173 ? 11.687  -1.393  50.763  1.00 54.50 ? 201 GLU A CB  1 
ATOM   1223 N  N   . PHE A 1 174 ? 9.285   -3.673  52.066  1.00 45.23 ? 202 PHE A N   1 
ATOM   1224 C  CA  . PHE A 1 174 ? 8.971   -4.485  53.238  1.00 38.56 ? 202 PHE A CA  1 
ATOM   1225 C  C   . PHE A 1 174 ? 9.464   -5.907  53.037  1.00 35.54 ? 202 PHE A C   1 
ATOM   1226 O  O   . PHE A 1 174 ? 10.385  -6.356  53.722  1.00 40.62 ? 202 PHE A O   1 
ATOM   1227 C  CB  . PHE A 1 174 ? 7.461   -4.469  53.521  1.00 34.14 ? 202 PHE A CB  1 
ATOM   1228 C  CG  . PHE A 1 174 ? 7.033   -5.396  54.630  1.00 29.94 ? 202 PHE A CG  1 
ATOM   1229 C  CD1 . PHE A 1 174 ? 7.435   -5.166  55.932  1.00 27.88 ? 202 PHE A CD1 1 
ATOM   1230 C  CD2 . PHE A 1 174 ? 6.182   -6.473  54.377  1.00 33.18 ? 202 PHE A CD2 1 
ATOM   1231 C  CE1 . PHE A 1 174 ? 7.037   -6.000  56.964  1.00 26.20 ? 202 PHE A CE1 1 
ATOM   1232 C  CE2 . PHE A 1 174 ? 5.772   -7.330  55.414  1.00 27.02 ? 202 PHE A CE2 1 
ATOM   1233 C  CZ  . PHE A 1 174 ? 6.195   -7.088  56.710  1.00 27.78 ? 202 PHE A CZ  1 
ATOM   1234 N  N   . LEU A 1 175 ? 8.838   -6.631  52.120  1.00 37.02 ? 203 LEU A N   1 
ATOM   1235 C  CA  . LEU A 1 175 ? 9.260   -7.961  51.730  1.00 36.59 ? 203 LEU A CA  1 
ATOM   1236 C  C   . LEU A 1 175 ? 9.189   -8.036  50.215  1.00 36.00 ? 203 LEU A C   1 
ATOM   1237 O  O   . LEU A 1 175 ? 8.395   -7.318  49.596  1.00 34.98 ? 203 LEU A O   1 
ATOM   1238 C  CB  . LEU A 1 175 ? 8.379   -9.065  52.346  1.00 33.12 ? 203 LEU A CB  1 
ATOM   1239 C  CG  . LEU A 1 175 ? 8.450   -9.322  53.857  1.00 30.91 ? 203 LEU A CG  1 
ATOM   1240 C  CD1 . LEU A 1 175 ? 7.585   -10.520 54.264  1.00 31.60 ? 203 LEU A CD1 1 
ATOM   1241 C  CD2 . LEU A 1 175 ? 9.906   -9.499  54.323  1.00 36.00 ? 203 LEU A CD2 1 
ATOM   1242 N  N   . PRO A 1 176 ? 10.019  -8.868  49.589  1.00 35.18 ? 204 PRO A N   1 
ATOM   1243 C  CA  . PRO A 1 176 ? 9.834   -9.133  48.161  1.00 37.06 ? 204 PRO A CA  1 
ATOM   1244 C  C   . PRO A 1 176 ? 8.420   -9.630  47.898  1.00 39.97 ? 204 PRO A C   1 
ATOM   1245 O  O   . PRO A 1 176 ? 7.845   -10.384 48.688  1.00 42.10 ? 204 PRO A O   1 
ATOM   1246 C  CB  . PRO A 1 176 ? 10.877  -10.216 47.858  1.00 39.92 ? 204 PRO A CB  1 
ATOM   1247 C  CG  . PRO A 1 176 ? 11.920  -10.036 48.912  1.00 41.79 ? 204 PRO A CG  1 
ATOM   1248 C  CD  . PRO A 1 176 ? 11.188  -9.575  50.144  1.00 37.92 ? 204 PRO A CD  1 
ATOM   1249 N  N   . GLY A 1 177 ? 7.861   -9.213  46.774  1.00 37.22 ? 205 GLY A N   1 
ATOM   1250 C  CA  . GLY A 1 177 ? 6.510   -9.593  46.437  1.00 37.44 ? 205 GLY A CA  1 
ATOM   1251 C  C   . GLY A 1 177 ? 5.453   -8.646  46.952  1.00 33.23 ? 205 GLY A C   1 
ATOM   1252 O  O   . GLY A 1 177 ? 4.294   -8.756  46.541  1.00 37.67 ? 205 GLY A O   1 
ATOM   1253 N  N   . PHE A 1 178 ? 5.810   -7.732  47.849  1.00 32.49 ? 206 PHE A N   1 
ATOM   1254 C  CA  . PHE A 1 178 ? 4.912   -6.664  48.255  1.00 31.37 ? 206 PHE A CA  1 
ATOM   1255 C  C   . PHE A 1 178 ? 5.101   -5.478  47.322  1.00 35.53 ? 206 PHE A C   1 
ATOM   1256 O  O   . PHE A 1 178 ? 6.195   -5.235  46.806  1.00 37.11 ? 206 PHE A O   1 
ATOM   1257 C  CB  . PHE A 1 178 ? 5.169   -6.250  49.710  1.00 30.72 ? 206 PHE A CB  1 
ATOM   1258 C  CG  . PHE A 1 178 ? 4.476   -7.127  50.730  1.00 29.76 ? 206 PHE A CG  1 
ATOM   1259 C  CD1 . PHE A 1 178 ? 4.914   -8.424  50.958  1.00 29.28 ? 206 PHE A CD1 1 
ATOM   1260 C  CD2 . PHE A 1 178 ? 3.396   -6.647  51.472  1.00 25.29 ? 206 PHE A CD2 1 
ATOM   1261 C  CE1 . PHE A 1 178 ? 4.299   -9.239  51.890  1.00 30.11 ? 206 PHE A CE1 1 
ATOM   1262 C  CE2 . PHE A 1 178 ? 2.766   -7.462  52.411  1.00 24.04 ? 206 PHE A CE2 1 
ATOM   1263 C  CZ  . PHE A 1 178 ? 3.208   -8.758  52.618  1.00 28.16 ? 206 PHE A CZ  1 
ATOM   1264 N  N   . GLU A 1 179 ? 4.018   -4.763  47.075  1.00 32.44 ? 207 GLU A N   1 
ATOM   1265 C  CA  . GLU A 1 179 ? 4.052   -3.544  46.286  1.00 32.50 ? 207 GLU A CA  1 
ATOM   1266 C  C   . GLU A 1 179 ? 3.778   -2.356  47.185  1.00 38.65 ? 207 GLU A C   1 
ATOM   1267 O  O   . GLU A 1 179 ? 2.898   -2.414  48.048  1.00 34.98 ? 207 GLU A O   1 
ATOM   1268 C  CB  . GLU A 1 179 ? 3.018   -3.575  45.169  1.00 34.72 ? 207 GLU A CB  1 
ATOM   1269 C  CG  . GLU A 1 179 ? 3.254   -4.670  44.160  1.00 43.51 ? 207 GLU A CG  1 
ATOM   1270 C  CD  . GLU A 1 179 ? 2.447   -4.465  42.902  1.00 43.02 ? 207 GLU A CD  1 
ATOM   1271 O  OE1 . GLU A 1 179 ? 1.693   -3.466  42.825  1.00 51.41 ? 207 GLU A OE1 1 
ATOM   1272 O  OE2 . GLU A 1 179 ? 2.580   -5.301  41.987  1.00 48.82 ? 207 GLU A OE2 1 
ATOM   1273 N  N   . ARG A 1 180 ? 4.551   -1.290  46.989  1.00 36.81 ? 208 ARG A N   1 
ATOM   1274 C  CA  . ARG A 1 180 ? 4.247   -0.015  47.619  1.00 42.17 ? 208 ARG A CA  1 
ATOM   1275 C  C   . ARG A 1 180 ? 2.873   0.457   47.169  1.00 41.09 ? 208 ARG A C   1 
ATOM   1276 O  O   . ARG A 1 180 ? 2.457   0.230   46.031  1.00 46.34 ? 208 ARG A O   1 
ATOM   1277 C  CB  . ARG A 1 180 ? 5.307   1.025   47.260  1.00 45.90 ? 208 ARG A CB  1 
ATOM   1278 C  CG  . ARG A 1 180 ? 6.613   0.842   47.998  1.00 49.65 ? 208 ARG A CG  1 
ATOM   1279 C  CD  . ARG A 1 180 ? 6.826   1.963   48.998  1.00 58.24 ? 208 ARG A CD  1 
ATOM   1280 N  NE  . ARG A 1 180 ? 7.955   1.708   49.890  1.00 64.02 ? 208 ARG A NE  1 
ATOM   1281 C  CZ  . ARG A 1 180 ? 7.913   0.888   50.939  1.00 63.90 ? 208 ARG A CZ  1 
ATOM   1282 N  NH1 . ARG A 1 180 ? 6.794   0.234   51.240  1.00 55.50 ? 208 ARG A NH1 1 
ATOM   1283 N  NH2 . ARG A 1 180 ? 8.994   0.723   51.691  1.00 62.43 ? 208 ARG A NH2 1 
ATOM   1284 N  N   . VAL A 1 181 ? 2.164   1.112   48.064  1.00 43.01 ? 209 VAL A N   1 
ATOM   1285 C  CA  . VAL A 1 181 ? 0.750   1.390   47.844  1.00 48.59 ? 209 VAL A CA  1 
ATOM   1286 C  C   . VAL A 1 181 ? 0.580   2.698   47.084  1.00 57.59 ? 209 VAL A C   1 
ATOM   1287 O  O   . VAL A 1 181 ? 1.289   3.681   47.336  1.00 56.51 ? 209 VAL A O   1 
ATOM   1288 C  CB  . VAL A 1 181 ? -0.003  1.403   49.186  1.00 41.80 ? 209 VAL A CB  1 
ATOM   1289 C  CG1 . VAL A 1 181 ? -1.324  2.138   49.060  1.00 44.74 ? 209 VAL A CG1 1 
ATOM   1290 C  CG2 . VAL A 1 181 ? -0.215  -0.037  49.645  1.00 36.03 ? 209 VAL A CG2 1 
ATOM   1291 N  N   . GLU A 1 182 ? -0.372  2.694   46.139  1.00 58.73 ? 210 GLU A N   1 
ATOM   1292 C  CA  . GLU A 1 182 ? -0.662  3.846   45.292  1.00 60.22 ? 210 GLU A CA  1 
ATOM   1293 C  C   . GLU A 1 182 ? -1.080  5.050   46.130  1.00 61.60 ? 210 GLU A C   1 
ATOM   1294 O  O   . GLU A 1 182 ? -2.048  4.985   46.896  1.00 61.04 ? 210 GLU A O   1 
ATOM   1295 C  CB  . GLU A 1 182 ? -1.751  3.486   44.278  1.00 62.73 ? 210 GLU A CB  1 
ATOM   1296 C  CG  . GLU A 1 182 ? -3.046  2.952   44.884  1.00 62.61 ? 210 GLU A CG  1 
ATOM   1297 C  CD  . GLU A 1 182 ? -4.224  3.011   43.918  1.00 71.37 ? 210 GLU A CD  1 
ATOM   1298 O  OE1 . GLU A 1 182 ? -5.382  2.883   44.380  1.00 65.84 ? 210 GLU A OE1 1 
ATOM   1299 O  OE2 . GLU A 1 182 ? -3.995  3.184   42.700  1.00 74.20 ? 210 GLU A OE2 1 
ATOM   1300 N  N   . ASP A 1 183 ? -0.352  6.153   45.958  1.00 59.35 ? 211 ASP A N   1 
ATOM   1301 C  CA  . ASP A 1 183 ? -0.486  7.361   46.768  1.00 60.43 ? 211 ASP A CA  1 
ATOM   1302 C  C   . ASP A 1 183 ? -1.927  7.771   47.069  1.00 56.95 ? 211 ASP A C   1 
ATOM   1303 O  O   . ASP A 1 183 ? -2.195  8.317   48.145  1.00 59.17 ? 211 ASP A O   1 
ATOM   1304 C  CB  . ASP A 1 183 ? 0.246   8.516   46.080  1.00 66.84 ? 211 ASP A CB  1 
ATOM   1305 C  CG  . ASP A 1 183 ? 1.758   8.406   46.209  1.00 68.87 ? 211 ASP A CG  1 
ATOM   1306 O  OD1 . ASP A 1 183 ? 2.362   9.269   46.879  1.00 72.51 ? 211 ASP A OD1 1 
ATOM   1307 O  OD2 . ASP A 1 183 ? 2.342   7.452   45.649  1.00 68.31 ? 211 ASP A OD2 1 
ATOM   1308 N  N   . ALA A 1 184 ? -2.859  7.521   46.143  1.00 56.36 ? 212 ALA A N   1 
ATOM   1309 C  CA  . ALA A 1 184 ? -4.247  7.918   46.379  1.00 58.08 ? 212 ALA A CA  1 
ATOM   1310 C  C   . ALA A 1 184 ? -4.868  7.124   47.524  1.00 54.24 ? 212 ALA A C   1 
ATOM   1311 O  O   . ALA A 1 184 ? -5.604  7.681   48.347  1.00 52.86 ? 212 ALA A O   1 
ATOM   1312 C  CB  . ALA A 1 184 ? -5.073  7.754   45.103  1.00 60.08 ? 212 ALA A CB  1 
ATOM   1313 N  N   . SER A 1 185 ? -4.595  5.822   47.589  1.00 58.86 ? 213 SER A N   1 
ATOM   1314 C  CA  . SER A 1 185 ? -5.012  5.014   48.728  1.00 54.53 ? 213 SER A CA  1 
ATOM   1315 C  C   . SER A 1 185 ? -4.120  5.215   49.942  1.00 47.31 ? 213 SER A C   1 
ATOM   1316 O  O   . SER A 1 185 ? -4.489  4.802   51.045  1.00 49.01 ? 213 SER A O   1 
ATOM   1317 C  CB  . SER A 1 185 ? -5.036  3.530   48.344  1.00 53.10 ? 213 SER A CB  1 
ATOM   1318 O  OG  . SER A 1 185 ? -5.765  3.334   47.142  1.00 56.13 ? 213 SER A OG  1 
ATOM   1319 N  N   . SER A 1 186 ? -2.962  5.845   49.771  1.00 48.12 ? 214 SER A N   1 
ATOM   1320 C  CA  . SER A 1 186 ? -2.032  6.054   50.869  1.00 40.03 ? 214 SER A CA  1 
ATOM   1321 C  C   . SER A 1 186 ? -2.240  7.468   51.414  1.00 39.05 ? 214 SER A C   1 
ATOM   1322 O  O   . SER A 1 186 ? -1.512  8.403   51.091  1.00 42.92 ? 214 SER A O   1 
ATOM   1323 C  CB  . SER A 1 186 ? -0.606  5.822   50.395  1.00 44.48 ? 214 SER A CB  1 
ATOM   1324 O  OG  . SER A 1 186 ? 0.294   5.866   51.481  1.00 43.53 ? 214 SER A OG  1 
ATOM   1325 N  N   . PHE A 1 187 ? -3.254  7.617   52.248  1.00 36.62 ? 215 PHE A N   1 
ATOM   1326 C  CA  . PHE A 1 187 ? -3.477  8.892   52.926  1.00 34.49 ? 215 PHE A CA  1 
ATOM   1327 C  C   . PHE A 1 187 ? -2.496  9.027   54.084  1.00 30.84 ? 215 PHE A C   1 
ATOM   1328 O  O   . PHE A 1 187 ? -2.407  8.124   54.917  1.00 29.38 ? 215 PHE A O   1 
ATOM   1329 C  CB  . PHE A 1 187 ? -4.902  8.987   53.441  1.00 33.56 ? 215 PHE A CB  1 
ATOM   1330 C  CG  . PHE A 1 187 ? -5.286  10.361  53.882  1.00 29.30 ? 215 PHE A CG  1 
ATOM   1331 C  CD1 . PHE A 1 187 ? -4.859  10.868  55.100  1.00 27.65 ? 215 PHE A CD1 1 
ATOM   1332 C  CD2 . PHE A 1 187 ? -6.063  11.165  53.063  1.00 37.31 ? 215 PHE A CD2 1 
ATOM   1333 C  CE1 . PHE A 1 187 ? -5.211  12.157  55.495  1.00 33.06 ? 215 PHE A CE1 1 
ATOM   1334 C  CE2 . PHE A 1 187 ? -6.419  12.449  53.456  1.00 32.34 ? 215 PHE A CE2 1 
ATOM   1335 C  CZ  . PHE A 1 187 ? -5.988  12.946  54.667  1.00 34.08 ? 215 PHE A CZ  1 
ATOM   1336 N  N   . PRO A 1 188 ? -1.733  10.179  54.192  1.00 27.65 ? 216 PRO A N   1 
ATOM   1337 C  CA  . PRO A 1 188 ? -0.613  10.220  55.151  1.00 30.05 ? 216 PRO A CA  1 
ATOM   1338 C  C   . PRO A 1 188 ? -1.057  10.511  56.583  1.00 30.04 ? 216 PRO A C   1 
ATOM   1339 O  O   . PRO A 1 188 ? -0.649  11.495  57.200  1.00 28.49 ? 216 PRO A O   1 
ATOM   1340 C  CB  . PRO A 1 188 ? 0.280   11.329  54.565  1.00 25.41 ? 216 PRO A CB  1 
ATOM   1341 C  CG  . PRO A 1 188 ? -0.655  12.245  53.873  1.00 29.10 ? 216 PRO A CG  1 
ATOM   1342 C  CD  . PRO A 1 188 ? -1.774  11.367  53.320  1.00 28.57 ? 216 PRO A CD  1 
ATOM   1343 N  N   . LEU A 1 189 ? -1.892  9.634   57.137  1.00 25.32 ? 217 LEU A N   1 
ATOM   1344 C  CA  . LEU A 1 189 ? -2.279  9.763   58.539  1.00 23.47 ? 217 LEU A CA  1 
ATOM   1345 C  C   . LEU A 1 189 ? -1.068  9.614   59.445  1.00 23.96 ? 217 LEU A C   1 
ATOM   1346 O  O   . LEU A 1 189 ? -0.172  8.809   59.192  1.00 26.36 ? 217 LEU A O   1 
ATOM   1347 C  CB  . LEU A 1 189 ? -3.314  8.698   58.919  1.00 26.40 ? 217 LEU A CB  1 
ATOM   1348 C  CG  . LEU A 1 189 ? -4.672  8.776   58.252  1.00 20.60 ? 217 LEU A CG  1 
ATOM   1349 C  CD1 . LEU A 1 189 ? -5.480  7.482   58.558  1.00 25.22 ? 217 LEU A CD1 1 
ATOM   1350 C  CD2 . LEU A 1 189 ? -5.453  10.029  58.678  1.00 23.32 ? 217 LEU A CD2 1 
ATOM   1351 N  N   . ASP A 1 190 ? -1.067  10.369  60.537  1.00 25.51 ? 218 ASP A N   1 
ATOM   1352 C  CA  . ASP A 1 190 ? -0.002  10.258  61.529  1.00 25.44 ? 218 ASP A CA  1 
ATOM   1353 C  C   . ASP A 1 190 ? -0.485  10.917  62.815  1.00 25.47 ? 218 ASP A C   1 
ATOM   1354 O  O   . ASP A 1 190 ? -0.650  12.139  62.842  1.00 24.19 ? 218 ASP A O   1 
ATOM   1355 C  CB  . ASP A 1 190 ? 1.271   10.923  61.006  1.00 25.62 ? 218 ASP A CB  1 
ATOM   1356 C  CG  . ASP A 1 190 ? 2.387   10.924  62.022  1.00 31.86 ? 218 ASP A CG  1 
ATOM   1357 O  OD1 . ASP A 1 190 ? 2.341   10.113  62.964  1.00 28.79 ? 218 ASP A OD1 1 
ATOM   1358 O  OD2 . ASP A 1 190 ? 3.316   11.751  61.879  1.00 33.23 ? 218 ASP A OD2 1 
ATOM   1359 N  N   . TYR A 1 191 ? -0.691  10.130  63.879  1.00 19.14 ? 219 TYR A N   1 
ATOM   1360 C  CA  . TYR A 1 191 ? -1.060  10.700  65.171  1.00 22.09 ? 219 TYR A CA  1 
ATOM   1361 C  C   . TYR A 1 191 ? 0.102   10.712  66.150  1.00 21.77 ? 219 TYR A C   1 
ATOM   1362 O  O   . TYR A 1 191 ? -0.108  10.973  67.337  1.00 25.07 ? 219 TYR A O   1 
ATOM   1363 C  CB  . TYR A 1 191 ? -2.251  9.964   65.822  1.00 20.58 ? 219 TYR A CB  1 
ATOM   1364 C  CG  . TYR A 1 191 ? -3.456  9.715   64.923  1.00 22.21 ? 219 TYR A CG  1 
ATOM   1365 C  CD1 . TYR A 1 191 ? -3.670  10.462  63.769  1.00 21.95 ? 219 TYR A CD1 1 
ATOM   1366 C  CD2 . TYR A 1 191 ? -4.369  8.705   65.231  1.00 21.42 ? 219 TYR A CD2 1 
ATOM   1367 C  CE1 . TYR A 1 191 ? -4.753  10.223  62.951  1.00 22.79 ? 219 TYR A CE1 1 
ATOM   1368 C  CE2 . TYR A 1 191 ? -5.460  8.452   64.421  1.00 20.98 ? 219 TYR A CE2 1 
ATOM   1369 C  CZ  . TYR A 1 191 ? -5.636  9.193   63.272  1.00 22.63 ? 219 TYR A CZ  1 
ATOM   1370 O  OH  . TYR A 1 191 ? -6.703  8.932   62.461  1.00 21.33 ? 219 TYR A OH  1 
ATOM   1371 N  N   . GLY A 1 192 ? 1.310   10.441  65.687  1.00 22.37 ? 220 GLY A N   1 
ATOM   1372 C  CA  . GLY A 1 192 ? 2.497   10.547  66.516  1.00 21.64 ? 220 GLY A CA  1 
ATOM   1373 C  C   . GLY A 1 192 ? 3.134   9.226   66.898  1.00 22.79 ? 220 GLY A C   1 
ATOM   1374 O  O   . GLY A 1 192 ? 4.243   9.225   67.453  1.00 24.36 ? 220 GLY A O   1 
ATOM   1375 N  N   . ILE A 1 193 ? 2.490   8.093   66.627  1.00 21.51 ? 221 ILE A N   1 
ATOM   1376 C  CA  . ILE A 1 193 ? 3.103   6.822   67.004  1.00 18.03 ? 221 ILE A CA  1 
ATOM   1377 C  C   . ILE A 1 193 ? 4.334   6.547   66.149  1.00 21.26 ? 221 ILE A C   1 
ATOM   1378 O  O   . ILE A 1 193 ? 4.328   6.767   64.929  1.00 21.95 ? 221 ILE A O   1 
ATOM   1379 C  CB  . ILE A 1 193 ? 2.048   5.703   66.882  1.00 18.00 ? 221 ILE A CB  1 
ATOM   1380 C  CG1 . ILE A 1 193 ? 0.932   5.941   67.888  1.00 14.58 ? 221 ILE A CG1 1 
ATOM   1381 C  CG2 . ILE A 1 193 ? 2.691   4.367   67.140  1.00 20.31 ? 221 ILE A CG2 1 
ATOM   1382 C  CD1 . ILE A 1 193 ? -0.304  5.009   67.679  1.00 17.63 ? 221 ILE A CD1 1 
ATOM   1383 N  N   . ARG A 1 194 ? 5.415   6.047   66.787  1.00 22.04 ? 222 ARG A N   1 
ATOM   1384 C  CA  . ARG A 1 194 ? 6.715   5.949   66.126  1.00 24.76 ? 222 ARG A CA  1 
ATOM   1385 C  C   . ARG A 1 194 ? 7.360   4.559   66.138  1.00 24.48 ? 222 ARG A C   1 
ATOM   1386 O  O   . ARG A 1 194 ? 8.072   4.216   65.187  1.00 23.21 ? 222 ARG A O   1 
ATOM   1387 C  CB  . ARG A 1 194 ? 7.681   6.974   66.744  1.00 24.76 ? 222 ARG A CB  1 
ATOM   1388 C  CG  . ARG A 1 194 ? 7.339   8.418   66.381  1.00 23.33 ? 222 ARG A CG  1 
ATOM   1389 C  CD  . ARG A 1 194 ? 7.412   8.621   64.873  1.00 24.68 ? 222 ARG A CD  1 
ATOM   1390 N  NE  . ARG A 1 194 ? 7.048   9.977   64.458  1.00 27.66 ? 222 ARG A NE  1 
ATOM   1391 C  CZ  . ARG A 1 194 ? 5.860   10.321  63.965  1.00 29.71 ? 222 ARG A CZ  1 
ATOM   1392 N  NH1 . ARG A 1 194 ? 4.897   9.411   63.828  1.00 24.89 ? 222 ARG A NH1 1 
ATOM   1393 N  NH2 . ARG A 1 194 ? 5.630   11.576  63.609  1.00 30.58 ? 222 ARG A NH2 1 
ATOM   1394 N  N   . ARG A 1 195 ? 7.134   3.742   67.176  1.00 22.25 ? 223 ARG A N   1 
ATOM   1395 C  CA  . ARG A 1 195 ? 7.728   2.413   67.179  1.00 19.74 ? 223 ARG A CA  1 
ATOM   1396 C  C   . ARG A 1 195 ? 7.083   1.521   68.241  1.00 20.60 ? 223 ARG A C   1 
ATOM   1397 O  O   . ARG A 1 195 ? 6.381   1.996   69.141  1.00 22.16 ? 223 ARG A O   1 
ATOM   1398 C  CB  . ARG A 1 195 ? 9.249   2.494   67.421  1.00 22.32 ? 223 ARG A CB  1 
ATOM   1399 C  CG  . ARG A 1 195 ? 9.611   2.857   68.847  1.00 24.46 ? 223 ARG A CG  1 
ATOM   1400 C  CD  . ARG A 1 195 ? 11.173  2.799   69.055  1.00 27.23 ? 223 ARG A CD  1 
ATOM   1401 N  NE  . ARG A 1 195 ? 11.556  3.147   70.423  1.00 35.47 ? 223 ARG A NE  1 
ATOM   1402 C  CZ  . ARG A 1 195 ? 11.739  2.251   71.395  1.00 31.15 ? 223 ARG A CZ  1 
ATOM   1403 N  NH1 . ARG A 1 195 ? 11.597  0.961   71.146  1.00 27.79 ? 223 ARG A NH1 1 
ATOM   1404 N  NH2 . ARG A 1 195 ? 12.087  2.642   72.613  1.00 36.33 ? 223 ARG A NH2 1 
ATOM   1405 N  N   . LEU A 1 196 ? 7.326   0.212   68.111  1.00 19.76 ? 224 LEU A N   1 
ATOM   1406 C  CA  . LEU A 1 196 ? 6.885   -0.765  69.102  1.00 20.00 ? 224 LEU A CA  1 
ATOM   1407 C  C   . LEU A 1 196 ? 7.850   -0.779  70.275  1.00 23.32 ? 224 LEU A C   1 
ATOM   1408 O  O   . LEU A 1 196 ? 9.049   -1.018  70.091  1.00 24.07 ? 224 LEU A O   1 
ATOM   1409 C  CB  . LEU A 1 196 ? 6.796   -2.167  68.494  1.00 22.14 ? 224 LEU A CB  1 
ATOM   1410 C  CG  . LEU A 1 196 ? 6.245   -3.270  69.411  1.00 22.03 ? 224 LEU A CG  1 
ATOM   1411 C  CD1 . LEU A 1 196 ? 4.765   -3.085  69.784  1.00 20.92 ? 224 LEU A CD1 1 
ATOM   1412 C  CD2 . LEU A 1 196 ? 6.454   -4.644  68.762  1.00 21.92 ? 224 LEU A CD2 1 
ATOM   1413 N  N   . ASP A 1 197 ? 7.336   -0.530  71.476  1.00 22.02 ? 225 ASP A N   1 
ATOM   1414 C  CA  . ASP A 1 197 ? 8.188   -0.490  72.655  1.00 23.58 ? 225 ASP A CA  1 
ATOM   1415 C  C   . ASP A 1 197 ? 8.323   -1.863  73.296  1.00 24.17 ? 225 ASP A C   1 
ATOM   1416 O  O   . ASP A 1 197 ? 9.436   -2.278  73.652  1.00 24.02 ? 225 ASP A O   1 
ATOM   1417 C  CB  . ASP A 1 197 ? 7.643   0.498   73.683  1.00 23.02 ? 225 ASP A CB  1 
ATOM   1418 C  CG  . ASP A 1 197 ? 8.561   0.636   74.888  1.00 26.27 ? 225 ASP A CG  1 
ATOM   1419 O  OD1 . ASP A 1 197 ? 9.427   1.546   74.866  1.00 24.65 ? 225 ASP A OD1 1 
ATOM   1420 O  OD2 . ASP A 1 197 ? 8.405   -0.150  75.853  1.00 24.69 ? 225 ASP A OD2 1 
ATOM   1421 N  N   . HIS A 1 198 ? 7.205   -2.572  73.467  1.00 20.99 ? 226 HIS A N   1 
ATOM   1422 C  CA  . HIS A 1 198 ? 7.273   -3.945  73.944  1.00 18.76 ? 226 HIS A CA  1 
ATOM   1423 C  C   . HIS A 1 198 ? 6.008   -4.693  73.541  1.00 22.02 ? 226 HIS A C   1 
ATOM   1424 O  O   . HIS A 1 198 ? 5.005   -4.093  73.163  1.00 20.69 ? 226 HIS A O   1 
ATOM   1425 C  CB  . HIS A 1 198 ? 7.477   -4.021  75.460  1.00 23.88 ? 226 HIS A CB  1 
ATOM   1426 C  CG  . HIS A 1 198 ? 6.462   -3.289  76.278  1.00 22.25 ? 226 HIS A CG  1 
ATOM   1427 N  ND1 . HIS A 1 198 ? 6.572   -1.948  76.587  1.00 24.44 ? 226 HIS A ND1 1 
ATOM   1428 C  CD2 . HIS A 1 198 ? 5.330   -3.721  76.883  1.00 21.94 ? 226 HIS A CD2 1 
ATOM   1429 C  CE1 . HIS A 1 198 ? 5.571   -1.595  77.372  1.00 21.29 ? 226 HIS A CE1 1 
ATOM   1430 N  NE2 . HIS A 1 198 ? 4.786   -2.646  77.544  1.00 27.25 ? 226 HIS A NE2 1 
ATOM   1431 N  N   . ALA A 1 199 ? 6.079   -6.017  73.649  1.00 22.10 ? 227 ALA A N   1 
ATOM   1432 C  CA  . ALA A 1 199 ? 5.001   -6.914  73.237  1.00 20.20 ? 227 ALA A CA  1 
ATOM   1433 C  C   . ALA A 1 199 ? 4.879   -7.985  74.303  1.00 21.95 ? 227 ALA A C   1 
ATOM   1434 O  O   . ALA A 1 199 ? 5.880   -8.618  74.649  1.00 23.39 ? 227 ALA A O   1 
ATOM   1435 C  CB  . ALA A 1 199 ? 5.298   -7.544  71.872  1.00 19.30 ? 227 ALA A CB  1 
ATOM   1436 N  N   . VAL A 1 200 ? 3.671   -8.200  74.815  1.00 21.14 ? 228 VAL A N   1 
ATOM   1437 C  CA  . VAL A 1 200 ? 3.479   -8.890  76.085  1.00 21.14 ? 228 VAL A CA  1 
ATOM   1438 C  C   . VAL A 1 200 ? 2.649   -10.154 75.880  1.00 22.86 ? 228 VAL A C   1 
ATOM   1439 O  O   . VAL A 1 200 ? 1.581   -10.116 75.252  1.00 21.61 ? 228 VAL A O   1 
ATOM   1440 C  CB  . VAL A 1 200 ? 2.815   -7.967  77.116  1.00 21.31 ? 228 VAL A CB  1 
ATOM   1441 C  CG1 . VAL A 1 200 ? 2.624   -8.702  78.435  1.00 20.34 ? 228 VAL A CG1 1 
ATOM   1442 C  CG2 . VAL A 1 200 ? 3.668   -6.701  77.308  1.00 20.94 ? 228 VAL A CG2 1 
ATOM   1443 N  N   . GLY A 1 201 ? 3.122   -11.264 76.432  1.00 23.32 ? 229 GLY A N   1 
ATOM   1444 C  CA  . GLY A 1 201 ? 2.380   -12.514 76.388  1.00 22.22 ? 229 GLY A CA  1 
ATOM   1445 C  C   . GLY A 1 201 ? 1.702   -12.859 77.701  1.00 24.16 ? 229 GLY A C   1 
ATOM   1446 O  O   . GLY A 1 201 ? 2.212   -12.558 78.776  1.00 24.10 ? 229 GLY A O   1 
ATOM   1447 N  N   . ASN A 1 202 ? 0.540   -13.518 77.604  1.00 23.75 ? 230 ASN A N   1 
ATOM   1448 C  CA  . ASN A 1 202 ? -0.131  -14.129 78.750  1.00 22.45 ? 230 ASN A CA  1 
ATOM   1449 C  C   . ASN A 1 202 ? 0.002   -15.643 78.626  1.00 27.67 ? 230 ASN A C   1 
ATOM   1450 O  O   . ASN A 1 202 ? -0.296  -16.201 77.564  1.00 24.17 ? 230 ASN A O   1 
ATOM   1451 C  CB  . ASN A 1 202 ? -1.620  -13.767 78.799  1.00 24.53 ? 230 ASN A CB  1 
ATOM   1452 C  CG  . ASN A 1 202 ? -1.886  -12.395 79.374  1.00 24.90 ? 230 ASN A CG  1 
ATOM   1453 O  OD1 . ASN A 1 202 ? -1.007  -11.751 79.952  1.00 24.00 ? 230 ASN A OD1 1 
ATOM   1454 N  ND2 . ASN A 1 202 ? -3.127  -11.950 79.234  1.00 21.88 ? 230 ASN A ND2 1 
ATOM   1455 N  N   . VAL A 1 203 ? 0.445   -16.303 79.696  1.00 27.29 ? 231 VAL A N   1 
ATOM   1456 C  CA  . VAL A 1 203 ? 0.624   -17.760 79.698  1.00 29.75 ? 231 VAL A CA  1 
ATOM   1457 C  C   . VAL A 1 203 ? 0.051   -18.335 80.991  1.00 29.13 ? 231 VAL A C   1 
ATOM   1458 O  O   . VAL A 1 203 ? -0.102  -17.626 81.989  1.00 32.21 ? 231 VAL A O   1 
ATOM   1459 C  CB  . VAL A 1 203 ? 2.110   -18.160 79.555  1.00 31.57 ? 231 VAL A CB  1 
ATOM   1460 C  CG1 . VAL A 1 203 ? 2.736   -17.581 78.276  1.00 30.34 ? 231 VAL A CG1 1 
ATOM   1461 C  CG2 . VAL A 1 203 ? 2.913   -17.700 80.779  1.00 33.61 ? 231 VAL A CG2 1 
ATOM   1462 N  N   . PRO A 1 204 ? -0.288  -19.634 80.990  1.00 37.57 ? 232 PRO A N   1 
ATOM   1463 C  CA  . PRO A 1 204 ? -0.747  -20.250 82.250  1.00 35.98 ? 232 PRO A CA  1 
ATOM   1464 C  C   . PRO A 1 204 ? 0.347   -20.364 83.297  1.00 35.31 ? 232 PRO A C   1 
ATOM   1465 O  O   . PRO A 1 204 ? 0.048   -20.290 84.497  1.00 37.87 ? 232 PRO A O   1 
ATOM   1466 C  CB  . PRO A 1 204 ? -1.232  -21.641 81.811  1.00 36.02 ? 232 PRO A CB  1 
ATOM   1467 C  CG  . PRO A 1 204 ? -0.458  -21.934 80.576  1.00 35.08 ? 232 PRO A CG  1 
ATOM   1468 C  CD  . PRO A 1 204 ? -0.299  -20.596 79.875  1.00 35.01 ? 232 PRO A CD  1 
ATOM   1469 N  N   . GLU A 1 205 ? 1.599   -20.537 82.880  1.00 34.17 ? 233 GLU A N   1 
ATOM   1470 C  CA  . GLU A 1 205 ? 2.710   -20.813 83.792  1.00 40.48 ? 233 GLU A CA  1 
ATOM   1471 C  C   . GLU A 1 205 ? 3.915   -19.995 83.360  1.00 34.86 ? 233 GLU A C   1 
ATOM   1472 O  O   . GLU A 1 205 ? 4.543   -20.298 82.342  1.00 35.42 ? 233 GLU A O   1 
ATOM   1473 C  CB  . GLU A 1 205 ? 3.066   -22.297 83.806  1.00 42.38 ? 233 GLU A CB  1 
ATOM   1474 C  CG  . GLU A 1 205 ? 1.889   -23.217 83.924  1.00 45.27 ? 233 GLU A CG  1 
ATOM   1475 C  CD  . GLU A 1 205 ? 2.315   -24.634 84.197  1.00 52.83 ? 233 GLU A CD  1 
ATOM   1476 O  OE1 . GLU A 1 205 ? 3.114   -25.181 83.406  1.00 53.91 ? 233 GLU A OE1 1 
ATOM   1477 O  OE2 . GLU A 1 205 ? 1.843   -25.200 85.202  1.00 60.16 ? 233 GLU A OE2 1 
ATOM   1478 N  N   . LEU A 1 206 ? 4.268   -18.996 84.163  1.00 34.65 ? 234 LEU A N   1 
ATOM   1479 C  CA  . LEU A 1 206 ? 5.337   -18.073 83.789  1.00 32.99 ? 234 LEU A CA  1 
ATOM   1480 C  C   . LEU A 1 206 ? 6.712   -18.745 83.785  1.00 35.46 ? 234 LEU A C   1 
ATOM   1481 O  O   . LEU A 1 206 ? 7.530   -18.495 82.891  1.00 33.70 ? 234 LEU A O   1 
ATOM   1482 C  CB  . LEU A 1 206 ? 5.322   -16.887 84.745  1.00 35.33 ? 234 LEU A CB  1 
ATOM   1483 C  CG  . LEU A 1 206 ? 6.365   -15.783 84.569  1.00 35.83 ? 234 LEU A CG  1 
ATOM   1484 C  CD1 . LEU A 1 206 ? 6.271   -15.204 83.168  1.00 29.98 ? 234 LEU A CD1 1 
ATOM   1485 C  CD2 . LEU A 1 206 ? 6.155   -14.708 85.631  1.00 31.23 ? 234 LEU A CD2 1 
ATOM   1486 N  N   . GLY A 1 207 ? 6.992   -19.589 84.774  1.00 35.20 ? 235 GLY A N   1 
ATOM   1487 C  CA  . GLY A 1 207 ? 8.309   -20.167 84.925  1.00 32.30 ? 235 GLY A CA  1 
ATOM   1488 C  C   . GLY A 1 207 ? 8.807   -20.902 83.696  1.00 32.71 ? 235 GLY A C   1 
ATOM   1489 O  O   . GLY A 1 207 ? 9.850   -20.575 83.126  1.00 33.99 ? 235 GLY A O   1 
ATOM   1490 N  N   . PRO A 1 208 ? 8.057   -21.917 83.262  1.00 35.54 ? 236 PRO A N   1 
ATOM   1491 C  CA  . PRO A 1 208 ? 8.423   -22.616 82.022  1.00 33.25 ? 236 PRO A CA  1 
ATOM   1492 C  C   . PRO A 1 208 ? 8.474   -21.712 80.810  1.00 32.00 ? 236 PRO A C   1 
ATOM   1493 O  O   . PRO A 1 208 ? 9.342   -21.894 79.947  1.00 33.48 ? 236 PRO A O   1 
ATOM   1494 C  CB  . PRO A 1 208 ? 7.323   -23.670 81.881  1.00 34.40 ? 236 PRO A CB  1 
ATOM   1495 C  CG  . PRO A 1 208 ? 6.810   -23.875 83.255  1.00 34.12 ? 236 PRO A CG  1 
ATOM   1496 C  CD  . PRO A 1 208 ? 6.978   -22.596 83.992  1.00 34.33 ? 236 PRO A CD  1 
ATOM   1497 N  N   . ALA A 1 209 ? 7.558   -20.749 80.709  1.00 34.96 ? 237 ALA A N   1 
ATOM   1498 C  CA  . ALA A 1 209 ? 7.583   -19.835 79.577  1.00 32.71 ? 237 ALA A CA  1 
ATOM   1499 C  C   . ALA A 1 209 ? 8.876   -19.027 79.559  1.00 29.72 ? 237 ALA A C   1 
ATOM   1500 O  O   . ALA A 1 209 ? 9.543   -18.925 78.524  1.00 30.38 ? 237 ALA A O   1 
ATOM   1501 C  CB  . ALA A 1 209 ? 6.353   -18.922 79.623  1.00 31.16 ? 237 ALA A CB  1 
ATOM   1502 N  N   . LEU A 1 210 ? 9.266   -18.477 80.709  1.00 30.41 ? 238 LEU A N   1 
ATOM   1503 C  CA  . LEU A 1 210 ? 10.502  -17.694 80.780  1.00 32.49 ? 238 LEU A CA  1 
ATOM   1504 C  C   . LEU A 1 210 ? 11.716  -18.550 80.450  1.00 32.35 ? 238 LEU A C   1 
ATOM   1505 O  O   . LEU A 1 210 ? 12.584  -18.149 79.666  1.00 34.80 ? 238 LEU A O   1 
ATOM   1506 C  CB  . LEU A 1 210 ? 10.668  -17.095 82.171  1.00 38.93 ? 238 LEU A CB  1 
ATOM   1507 C  CG  . LEU A 1 210 ? 9.933   -15.823 82.570  1.00 37.81 ? 238 LEU A CG  1 
ATOM   1508 C  CD1 . LEU A 1 210 ? 10.428  -15.441 83.950  1.00 41.49 ? 238 LEU A CD1 1 
ATOM   1509 C  CD2 . LEU A 1 210 ? 10.184  -14.701 81.574  1.00 33.19 ? 238 LEU A CD2 1 
ATOM   1510 N  N   . THR A 1 211 ? 11.791  -19.740 81.053  1.00 34.70 ? 239 THR A N   1 
ATOM   1511 C  CA  . THR A 1 211 ? 12.931  -20.624 80.838  1.00 35.97 ? 239 THR A CA  1 
ATOM   1512 C  C   . THR A 1 211 ? 13.091  -20.965 79.363  1.00 33.84 ? 239 THR A C   1 
ATOM   1513 O  O   . THR A 1 211 ? 14.202  -20.918 78.821  1.00 32.13 ? 239 THR A O   1 
ATOM   1514 C  CB  . THR A 1 211 ? 12.751  -21.889 81.676  1.00 40.47 ? 239 THR A CB  1 
ATOM   1515 O  OG1 . THR A 1 211 ? 12.608  -21.522 83.056  1.00 41.68 ? 239 THR A OG1 1 
ATOM   1516 C  CG2 . THR A 1 211 ? 13.947  -22.821 81.511  1.00 44.44 ? 239 THR A CG2 1 
ATOM   1517 N  N   . TYR A 1 212 ? 11.975  -21.248 78.687  1.00 33.79 ? 240 TYR A N   1 
ATOM   1518 C  CA  . TYR A 1 212 ? 12.006  -21.608 77.274  1.00 28.02 ? 240 TYR A CA  1 
ATOM   1519 C  C   . TYR A 1 212 ? 12.527  -20.463 76.415  1.00 29.25 ? 240 TYR A C   1 
ATOM   1520 O  O   . TYR A 1 212 ? 13.464  -20.638 75.625  1.00 29.75 ? 240 TYR A O   1 
ATOM   1521 C  CB  . TYR A 1 212 ? 10.598  -22.029 76.831  1.00 30.29 ? 240 TYR A CB  1 
ATOM   1522 C  CG  . TYR A 1 212 ? 10.411  -22.118 75.333  1.00 32.39 ? 240 TYR A CG  1 
ATOM   1523 C  CD1 . TYR A 1 212 ? 11.025  -23.117 74.595  1.00 30.43 ? 240 TYR A CD1 1 
ATOM   1524 C  CD2 . TYR A 1 212 ? 9.595   -21.202 74.653  1.00 29.87 ? 240 TYR A CD2 1 
ATOM   1525 C  CE1 . TYR A 1 212 ? 10.855  -23.210 73.218  1.00 29.20 ? 240 TYR A CE1 1 
ATOM   1526 C  CE2 . TYR A 1 212 ? 9.417   -21.290 73.281  1.00 24.44 ? 240 TYR A CE2 1 
ATOM   1527 C  CZ  . TYR A 1 212 ? 10.037  -22.306 72.565  1.00 29.20 ? 240 TYR A CZ  1 
ATOM   1528 O  OH  . TYR A 1 212 ? 9.881   -22.407 71.196  1.00 27.60 ? 240 TYR A OH  1 
ATOM   1529 N  N   . VAL A 1 213 ? 11.930  -19.275 76.553  1.00 28.40 ? 241 VAL A N   1 
ATOM   1530 C  CA  . VAL A 1 213 ? 12.289  -18.168 75.672  1.00 25.48 ? 241 VAL A CA  1 
ATOM   1531 C  C   . VAL A 1 213 ? 13.698  -17.677 75.970  1.00 24.43 ? 241 VAL A C   1 
ATOM   1532 O  O   . VAL A 1 213 ? 14.512  -17.492 75.060  1.00 26.51 ? 241 VAL A O   1 
ATOM   1533 C  CB  . VAL A 1 213 ? 11.258  -17.032 75.788  1.00 27.50 ? 241 VAL A CB  1 
ATOM   1534 C  CG1 . VAL A 1 213 ? 11.636  -15.895 74.847  1.00 28.59 ? 241 VAL A CG1 1 
ATOM   1535 C  CG2 . VAL A 1 213 ? 9.878   -17.577 75.480  1.00 28.96 ? 241 VAL A CG2 1 
ATOM   1536 N  N   . ALA A 1 214 ? 14.001  -17.432 77.245  1.00 28.63 ? 242 ALA A N   1 
ATOM   1537 C  CA  . ALA A 1 214 ? 15.369  -17.051 77.596  1.00 29.71 ? 242 ALA A CA  1 
ATOM   1538 C  C   . ALA A 1 214 ? 16.358  -18.152 77.214  1.00 30.16 ? 242 ALA A C   1 
ATOM   1539 O  O   . ALA A 1 214 ? 17.501  -17.863 76.833  1.00 32.95 ? 242 ALA A O   1 
ATOM   1540 C  CB  . ALA A 1 214 ? 15.458  -16.730 79.091  1.00 27.96 ? 242 ALA A CB  1 
ATOM   1541 N  N   . GLY A 1 215 ? 15.911  -19.409 77.254  1.00 31.45 ? 243 GLY A N   1 
ATOM   1542 C  CA  . GLY A 1 215 ? 16.772  -20.515 76.855  1.00 35.47 ? 243 GLY A CA  1 
ATOM   1543 C  C   . GLY A 1 215 ? 17.282  -20.396 75.429  1.00 34.63 ? 243 GLY A C   1 
ATOM   1544 O  O   . GLY A 1 215 ? 18.481  -20.553 75.178  1.00 32.98 ? 243 GLY A O   1 
ATOM   1545 N  N   . PHE A 1 216 ? 16.385  -20.100 74.467  1.00 27.99 ? 244 PHE A N   1 
ATOM   1546 C  CA  . PHE A 1 216 ? 16.805  -20.124 73.066  1.00 26.38 ? 244 PHE A CA  1 
ATOM   1547 C  C   . PHE A 1 216 ? 17.237  -18.768 72.514  1.00 28.88 ? 244 PHE A C   1 
ATOM   1548 O  O   . PHE A 1 216 ? 17.891  -18.728 71.464  1.00 29.99 ? 244 PHE A O   1 
ATOM   1549 C  CB  . PHE A 1 216 ? 15.715  -20.766 72.168  1.00 30.00 ? 244 PHE A CB  1 
ATOM   1550 C  CG  . PHE A 1 216 ? 14.514  -19.878 71.827  1.00 29.75 ? 244 PHE A CG  1 
ATOM   1551 C  CD1 . PHE A 1 216 ? 13.282  -20.098 72.429  1.00 29.75 ? 244 PHE A CD1 1 
ATOM   1552 C  CD2 . PHE A 1 216 ? 14.605  -18.897 70.847  1.00 27.70 ? 244 PHE A CD2 1 
ATOM   1553 C  CE1 . PHE A 1 216 ? 12.162  -19.316 72.094  1.00 30.16 ? 244 PHE A CE1 1 
ATOM   1554 C  CE2 . PHE A 1 216 ? 13.483  -18.103 70.507  1.00 28.73 ? 244 PHE A CE2 1 
ATOM   1555 C  CZ  . PHE A 1 216 ? 12.279  -18.321 71.133  1.00 28.18 ? 244 PHE A CZ  1 
ATOM   1556 N  N   . THR A 1 217 ? 16.922  -17.660 73.181  1.00 26.43 ? 245 THR A N   1 
ATOM   1557 C  CA  . THR A 1 217 ? 17.380  -16.361 72.708  1.00 27.50 ? 245 THR A CA  1 
ATOM   1558 C  C   . THR A 1 217 ? 18.648  -15.886 73.390  1.00 29.61 ? 245 THR A C   1 
ATOM   1559 O  O   . THR A 1 217 ? 19.399  -15.115 72.792  1.00 32.57 ? 245 THR A O   1 
ATOM   1560 C  CB  . THR A 1 217 ? 16.328  -15.274 72.936  1.00 23.93 ? 245 THR A CB  1 
ATOM   1561 O  OG1 . THR A 1 217 ? 16.028  -15.206 74.332  1.00 28.51 ? 245 THR A OG1 1 
ATOM   1562 C  CG2 . THR A 1 217 ? 15.051  -15.556 72.142  1.00 27.80 ? 245 THR A CG2 1 
ATOM   1563 N  N   . GLY A 1 218 ? 18.869  -16.288 74.637  1.00 32.60 ? 246 GLY A N   1 
ATOM   1564 C  CA  . GLY A 1 218 ? 19.841  -15.615 75.469  1.00 32.15 ? 246 GLY A CA  1 
ATOM   1565 C  C   . GLY A 1 218 ? 19.373  -14.285 76.016  1.00 32.52 ? 246 GLY A C   1 
ATOM   1566 O  O   . GLY A 1 218 ? 20.171  -13.572 76.634  1.00 29.89 ? 246 GLY A O   1 
ATOM   1567 N  N   . PHE A 1 219 ? 18.113  -13.909 75.780  1.00 29.41 ? 247 PHE A N   1 
ATOM   1568 C  CA  . PHE A 1 219 ? 17.589  -12.691 76.378  1.00 24.72 ? 247 PHE A CA  1 
ATOM   1569 C  C   . PHE A 1 219 ? 17.675  -12.777 77.894  1.00 29.19 ? 247 PHE A C   1 
ATOM   1570 O  O   . PHE A 1 219 ? 17.478  -13.844 78.481  1.00 29.96 ? 247 PHE A O   1 
ATOM   1571 C  CB  . PHE A 1 219 ? 16.126  -12.459 75.964  1.00 27.76 ? 247 PHE A CB  1 
ATOM   1572 C  CG  . PHE A 1 219 ? 15.951  -12.077 74.523  1.00 27.98 ? 247 PHE A CG  1 
ATOM   1573 C  CD1 . PHE A 1 219 ? 17.041  -11.757 73.730  1.00 27.31 ? 247 PHE A CD1 1 
ATOM   1574 C  CD2 . PHE A 1 219 ? 14.677  -12.012 73.965  1.00 27.86 ? 247 PHE A CD2 1 
ATOM   1575 C  CE1 . PHE A 1 219 ? 16.875  -11.390 72.415  1.00 27.17 ? 247 PHE A CE1 1 
ATOM   1576 C  CE2 . PHE A 1 219 ? 14.504  -11.650 72.646  1.00 27.49 ? 247 PHE A CE2 1 
ATOM   1577 C  CZ  . PHE A 1 219 ? 15.591  -11.337 71.867  1.00 27.65 ? 247 PHE A CZ  1 
ATOM   1578 N  N   . HIS A 1 220 ? 17.961  -11.643 78.532  1.00 29.91 ? 248 HIS A N   1 
ATOM   1579 C  CA  . HIS A 1 220 ? 18.150  -11.603 79.974  1.00 29.74 ? 248 HIS A CA  1 
ATOM   1580 C  C   . HIS A 1 220 ? 16.943  -10.992 80.668  1.00 31.07 ? 248 HIS A C   1 
ATOM   1581 O  O   . HIS A 1 220 ? 16.154  -10.262 80.067  1.00 33.25 ? 248 HIS A O   1 
ATOM   1582 C  CB  . HIS A 1 220 ? 19.413  -10.813 80.332  1.00 29.12 ? 248 HIS A CB  1 
ATOM   1583 C  CG  . HIS A 1 220 ? 19.375  -9.376  79.915  1.00 27.77 ? 248 HIS A CG  1 
ATOM   1584 N  ND1 . HIS A 1 220 ? 19.745  -8.956  78.655  1.00 27.87 ? 248 HIS A ND1 1 
ATOM   1585 C  CD2 . HIS A 1 220 ? 19.025  -8.258  80.596  1.00 28.40 ? 248 HIS A CD2 1 
ATOM   1586 C  CE1 . HIS A 1 220 ? 19.625  -7.642  78.579  1.00 29.20 ? 248 HIS A CE1 1 
ATOM   1587 N  NE2 . HIS A 1 220 ? 19.189  -7.195  79.742  1.00 32.27 ? 248 HIS A NE2 1 
ATOM   1588 N  N   . GLN A 1 221 ? 16.809  -11.300 81.958  1.00 31.79 ? 249 GLN A N   1 
ATOM   1589 C  CA  . GLN A 1 221 ? 15.732  -10.735 82.760  1.00 33.76 ? 249 GLN A CA  1 
ATOM   1590 C  C   . GLN A 1 221 ? 15.989  -9.256  83.014  1.00 39.68 ? 249 GLN A C   1 
ATOM   1591 O  O   . GLN A 1 221 ? 16.982  -8.882  83.649  1.00 36.48 ? 249 GLN A O   1 
ATOM   1592 C  CB  . GLN A 1 221 ? 15.592  -11.502 84.070  1.00 39.87 ? 249 GLN A CB  1 
ATOM   1593 C  CG  . GLN A 1 221 ? 14.311  -11.209 84.827  1.00 46.01 ? 249 GLN A CG  1 
ATOM   1594 C  CD  . GLN A 1 221 ? 13.887  -12.368 85.721  1.00 46.79 ? 249 GLN A CD  1 
ATOM   1595 O  OE1 . GLN A 1 221 ? 14.401  -13.475 85.600  1.00 57.83 ? 249 GLN A OE1 1 
ATOM   1596 N  NE2 . GLN A 1 221 ? 12.945  -12.115 86.617  1.00 53.98 ? 249 GLN A NE2 1 
ATOM   1597 N  N   . PHE A 1 222 ? 15.095  -8.412  82.499  1.00 35.04 ? 250 PHE A N   1 
ATOM   1598 C  CA  . PHE A 1 222 ? 15.175  -6.964  82.648  1.00 39.32 ? 250 PHE A CA  1 
ATOM   1599 C  C   . PHE A 1 222 ? 14.463  -6.488  83.905  1.00 41.58 ? 250 PHE A C   1 
ATOM   1600 O  O   . PHE A 1 222 ? 14.933  -5.562  84.572  1.00 49.02 ? 250 PHE A O   1 
ATOM   1601 C  CB  . PHE A 1 222 ? 14.574  -6.295  81.403  1.00 34.05 ? 250 PHE A CB  1 
ATOM   1602 C  CG  . PHE A 1 222 ? 14.501  -4.788  81.463  1.00 39.91 ? 250 PHE A CG  1 
ATOM   1603 C  CD1 . PHE A 1 222 ? 13.470  -4.146  82.132  1.00 39.70 ? 250 PHE A CD1 1 
ATOM   1604 C  CD2 . PHE A 1 222 ? 15.442  -4.014  80.803  1.00 44.96 ? 250 PHE A CD2 1 
ATOM   1605 C  CE1 . PHE A 1 222 ? 13.398  -2.761  82.170  1.00 39.18 ? 250 PHE A CE1 1 
ATOM   1606 C  CE2 . PHE A 1 222 ? 15.371  -2.635  80.832  1.00 45.19 ? 250 PHE A CE2 1 
ATOM   1607 C  CZ  . PHE A 1 222 ? 14.343  -2.004  81.519  1.00 38.77 ? 250 PHE A CZ  1 
ATOM   1608 N  N   . ALA A 1 223 ? 13.327  -7.101  84.223  1.00 40.18 ? 251 ALA A N   1 
ATOM   1609 C  CA  . ALA A 1 223 ? 12.493  -6.702  85.346  1.00 39.49 ? 251 ALA A CA  1 
ATOM   1610 C  C   . ALA A 1 223 ? 11.614  -7.885  85.714  1.00 44.80 ? 251 ALA A C   1 
ATOM   1611 O  O   . ALA A 1 223 ? 11.502  -8.858  84.965  1.00 39.31 ? 251 ALA A O   1 
ATOM   1612 C  CB  . ALA A 1 223 ? 11.635  -5.475  85.011  1.00 44.96 ? 251 ALA A CB  1 
ATOM   1613 N  N   . GLU A 1 224 ? 10.968  -7.773  86.869  1.00 51.28 ? 252 GLU A N   1 
ATOM   1614 C  CA  . GLU A 1 224 ? 10.147  -8.837  87.428  1.00 48.47 ? 252 GLU A CA  1 
ATOM   1615 C  C   . GLU A 1 224 ? 9.375   -8.251  88.593  1.00 54.08 ? 252 GLU A C   1 
ATOM   1616 O  O   . GLU A 1 224 ? 9.855   -7.329  89.256  1.00 53.09 ? 252 GLU A O   1 
ATOM   1617 C  CB  . GLU A 1 224 ? 11.003  -10.016 87.910  1.00 53.13 ? 252 GLU A CB  1 
ATOM   1618 N  N   . PHE A 1 225 ? 8.186   -8.791  88.841  1.00 50.96 ? 253 PHE A N   1 
ATOM   1619 C  CA  . PHE A 1 225 ? 7.483   -8.477  90.078  1.00 53.91 ? 253 PHE A CA  1 
ATOM   1620 C  C   . PHE A 1 225 ? 6.328   -9.437  90.256  1.00 57.92 ? 253 PHE A C   1 
ATOM   1621 O  O   . PHE A 1 225 ? 5.766   -9.945  89.282  1.00 51.48 ? 253 PHE A O   1 
ATOM   1622 C  CB  . PHE A 1 225 ? 6.935   -7.044  90.111  1.00 57.86 ? 253 PHE A CB  1 
ATOM   1623 N  N   . THR A 1 226 ? 5.930   -9.591  91.511  1.00 57.48 ? 254 THR A N   1 
ATOM   1624 C  CA  . THR A 1 226 ? 4.911   -10.545 91.914  1.00 53.16 ? 254 THR A CA  1 
ATOM   1625 C  C   . THR A 1 226 ? 3.606   -9.847  92.275  1.00 58.15 ? 254 THR A C   1 
ATOM   1626 O  O   . THR A 1 226 ? 3.601   -8.882  93.041  1.00 64.11 ? 254 THR A O   1 
ATOM   1627 C  CB  . THR A 1 226 ? 5.382   -11.370 93.121  1.00 55.40 ? 254 THR A CB  1 
ATOM   1628 O  OG1 . THR A 1 226 ? 5.366   -10.544 94.295  1.00 63.28 ? 254 THR A OG1 1 
ATOM   1629 C  CG2 . THR A 1 226 ? 6.791   -11.906 92.897  1.00 55.17 ? 254 THR A CG2 1 
ATOM   1630 N  N   . GLU A 1 234 ? -1.923  -9.575  94.477  1.00 69.75 ? 262 GLU A N   1 
ATOM   1631 C  CA  . GLU A 1 234 ? -3.113  -8.825  94.866  1.00 69.82 ? 262 GLU A CA  1 
ATOM   1632 C  C   . GLU A 1 234 ? -3.758  -8.172  93.651  1.00 68.17 ? 262 GLU A C   1 
ATOM   1633 O  O   . GLU A 1 234 ? -4.918  -7.763  93.694  1.00 70.35 ? 262 GLU A O   1 
ATOM   1634 C  CB  . GLU A 1 234 ? -2.758  -7.762  95.908  1.00 66.94 ? 262 GLU A CB  1 
ATOM   1635 N  N   . SER A 1 235 ? -2.992  -8.093  92.563  1.00 66.80 ? 263 SER A N   1 
ATOM   1636 C  CA  . SER A 1 235 ? -3.382  -7.365  91.365  1.00 61.41 ? 263 SER A CA  1 
ATOM   1637 C  C   . SER A 1 235 ? -3.670  -8.271  90.177  1.00 59.39 ? 263 SER A C   1 
ATOM   1638 O  O   . SER A 1 235 ? -3.913  -7.765  89.074  1.00 57.47 ? 263 SER A O   1 
ATOM   1639 C  CB  . SER A 1 235 ? -2.289  -6.363  90.987  1.00 59.54 ? 263 SER A CB  1 
ATOM   1640 O  OG  . SER A 1 235 ? -1.058  -7.035  90.784  1.00 62.45 ? 263 SER A OG  1 
ATOM   1641 N  N   . GLY A 1 236 ? -3.618  -9.588  90.356  1.00 55.65 ? 264 GLY A N   1 
ATOM   1642 C  CA  . GLY A 1 236 ? -4.042  -10.531 89.347  1.00 53.13 ? 264 GLY A CA  1 
ATOM   1643 C  C   . GLY A 1 236 ? -2.932  -11.271 88.626  1.00 47.90 ? 264 GLY A C   1 
ATOM   1644 O  O   . GLY A 1 236 ? -3.222  -12.273 87.956  1.00 41.02 ? 264 GLY A O   1 
ATOM   1645 N  N   . LEU A 1 237 ? -1.672  -10.846 88.752  1.00 43.77 ? 265 LEU A N   1 
ATOM   1646 C  CA  . LEU A 1 237 ? -0.650  -11.415 87.882  1.00 40.44 ? 265 LEU A CA  1 
ATOM   1647 C  C   . LEU A 1 237 ? 0.715   -11.465 88.557  1.00 37.93 ? 265 LEU A C   1 
ATOM   1648 O  O   . LEU A 1 237 ? 0.971   -10.784 89.553  1.00 40.67 ? 265 LEU A O   1 
ATOM   1649 C  CB  . LEU A 1 237 ? -0.542  -10.622 86.571  1.00 41.10 ? 265 LEU A CB  1 
ATOM   1650 C  CG  . LEU A 1 237 ? 0.266   -9.314  86.577  1.00 41.41 ? 265 LEU A CG  1 
ATOM   1651 C  CD1 . LEU A 1 237 ? 0.357   -8.720  85.180  1.00 33.39 ? 265 LEU A CD1 1 
ATOM   1652 C  CD2 . LEU A 1 237 ? -0.327  -8.295  87.533  1.00 47.06 ? 265 LEU A CD2 1 
ATOM   1653 N  N   . ASN A 1 238 ? 1.581   -12.311 87.996  1.00 34.64 ? 266 ASN A N   1 
ATOM   1654 C  CA  . ASN A 1 238 ? 3.028   -12.216 88.146  1.00 36.12 ? 266 ASN A CA  1 
ATOM   1655 C  C   . ASN A 1 238 ? 3.632   -11.990 86.766  1.00 36.16 ? 266 ASN A C   1 
ATOM   1656 O  O   . ASN A 1 238 ? 3.163   -12.563 85.777  1.00 33.11 ? 266 ASN A O   1 
ATOM   1657 C  CB  . ASN A 1 238 ? 3.629   -13.477 88.767  1.00 36.01 ? 266 ASN A CB  1 
ATOM   1658 C  CG  . ASN A 1 238 ? 3.108   -13.749 90.159  1.00 38.95 ? 266 ASN A CG  1 
ATOM   1659 O  OD1 . ASN A 1 238 ? 2.924   -12.829 90.957  1.00 44.70 ? 266 ASN A OD1 1 
ATOM   1660 N  ND2 . ASN A 1 238 ? 2.862   -15.020 90.460  1.00 41.74 ? 266 ASN A ND2 1 
ATOM   1661 N  N   . SER A 1 239 ? 4.673   -11.165 86.690  1.00 30.21 ? 267 SER A N   1 
ATOM   1662 C  CA  . SER A 1 239 ? 5.229   -10.794 85.399  1.00 32.27 ? 267 SER A CA  1 
ATOM   1663 C  C   . SER A 1 239 ? 6.749   -10.786 85.444  1.00 33.63 ? 267 SER A C   1 
ATOM   1664 O  O   . SER A 1 239 ? 7.356   -10.529 86.486  1.00 37.30 ? 267 SER A O   1 
ATOM   1665 C  CB  . SER A 1 239 ? 4.723   -9.409  84.966  1.00 35.67 ? 267 SER A CB  1 
ATOM   1666 O  OG  . SER A 1 239 ? 5.112   -9.124  83.633  1.00 38.61 ? 267 SER A OG  1 
ATOM   1667 N  N   . ALA A 1 240 ? 7.361   -11.030 84.289  1.00 29.78 ? 268 ALA A N   1 
ATOM   1668 C  CA  . ALA A 1 240 ? 8.800   -10.857 84.149  1.00 33.63 ? 268 ALA A CA  1 
ATOM   1669 C  C   . ALA A 1 240 ? 9.108   -10.463 82.712  1.00 32.41 ? 268 ALA A C   1 
ATOM   1670 O  O   . ALA A 1 240 ? 8.374   -10.816 81.785  1.00 29.93 ? 268 ALA A O   1 
ATOM   1671 C  CB  . ALA A 1 240 ? 9.564   -12.122 84.545  1.00 33.51 ? 268 ALA A CB  1 
ATOM   1672 N  N   . VAL A 1 241 ? 10.179  -9.698  82.531  1.00 24.28 ? 269 VAL A N   1 
ATOM   1673 C  CA  . VAL A 1 241 ? 10.493  -9.105  81.240  1.00 27.37 ? 269 VAL A CA  1 
ATOM   1674 C  C   . VAL A 1 241 ? 11.834  -9.622  80.750  1.00 31.60 ? 269 VAL A C   1 
ATOM   1675 O  O   . VAL A 1 241 ? 12.842  -9.513  81.456  1.00 30.92 ? 269 VAL A O   1 
ATOM   1676 C  CB  . VAL A 1 241 ? 10.518  -7.572  81.319  1.00 26.96 ? 269 VAL A CB  1 
ATOM   1677 C  CG1 . VAL A 1 241 ? 10.871  -6.989  79.947  1.00 26.61 ? 269 VAL A CG1 1 
ATOM   1678 C  CG2 . VAL A 1 241 ? 9.186   -7.058  81.851  1.00 26.03 ? 269 VAL A CG2 1 
ATOM   1679 N  N   . LEU A 1 242 ? 11.849  -10.141 79.528  1.00 28.02 ? 270 LEU A N   1 
ATOM   1680 C  CA  . LEU A 1 242 ? 13.065  -10.540 78.836  1.00 25.94 ? 270 LEU A CA  1 
ATOM   1681 C  C   . LEU A 1 242 ? 13.504  -9.455  77.861  1.00 31.58 ? 270 LEU A C   1 
ATOM   1682 O  O   . LEU A 1 242 ? 12.674  -8.785  77.242  1.00 28.38 ? 270 LEU A O   1 
ATOM   1683 C  CB  . LEU A 1 242 ? 12.842  -11.844 78.082  1.00 26.20 ? 270 LEU A CB  1 
ATOM   1684 C  CG  . LEU A 1 242 ? 12.607  -13.054 78.984  1.00 31.87 ? 270 LEU A CG  1 
ATOM   1685 C  CD1 . LEU A 1 242 ? 12.292  -14.277 78.144  1.00 30.69 ? 270 LEU A CD1 1 
ATOM   1686 C  CD2 . LEU A 1 242 ? 13.857  -13.302 79.826  1.00 30.63 ? 270 LEU A CD2 1 
ATOM   1687 N  N   . ALA A 1 243 ? 14.819  -9.281  77.723  1.00 28.94 ? 271 ALA A N   1 
ATOM   1688 C  CA  . ALA A 1 243 ? 15.338  -8.202  76.891  1.00 27.84 ? 271 ALA A CA  1 
ATOM   1689 C  C   . ALA A 1 243 ? 16.566  -8.633  76.097  1.00 30.09 ? 271 ALA A C   1 
ATOM   1690 O  O   . ALA A 1 243 ? 17.345  -9.491  76.524  1.00 29.93 ? 271 ALA A O   1 
ATOM   1691 C  CB  . ALA A 1 243 ? 15.690  -6.968  77.738  1.00 30.73 ? 271 ALA A CB  1 
ATOM   1692 N  N   . SER A 1 244 ? 16.748  -7.993  74.944  1.00 29.87 ? 272 SER A N   1 
ATOM   1693 C  CA  . SER A 1 244 ? 17.931  -8.197  74.126  1.00 28.70 ? 272 SER A CA  1 
ATOM   1694 C  C   . SER A 1 244 ? 19.113  -7.414  74.717  1.00 29.40 ? 272 SER A C   1 
ATOM   1695 O  O   . SER A 1 244 ? 18.982  -6.714  75.725  1.00 30.84 ? 272 SER A O   1 
ATOM   1696 C  CB  . SER A 1 244 ? 17.641  -7.789  72.687  1.00 23.04 ? 272 SER A CB  1 
ATOM   1697 O  OG  . SER A 1 244 ? 17.331  -6.401  72.611  1.00 28.30 ? 272 SER A OG  1 
ATOM   1698 N  N   . ASN A 1 245 ? 20.277  -7.520  74.068  1.00 30.78 ? 273 ASN A N   1 
ATOM   1699 C  CA  . ASN A 1 245 ? 21.514  -6.979  74.644  1.00 34.62 ? 273 ASN A CA  1 
ATOM   1700 C  C   . ASN A 1 245 ? 21.406  -5.485  74.935  1.00 36.74 ? 273 ASN A C   1 
ATOM   1701 O  O   . ASN A 1 245 ? 21.819  -5.020  76.007  1.00 37.73 ? 273 ASN A O   1 
ATOM   1702 C  CB  . ASN A 1 245 ? 22.693  -7.250  73.712  1.00 34.68 ? 273 ASN A CB  1 
ATOM   1703 C  CG  . ASN A 1 245 ? 23.219  -8.656  73.840  1.00 34.17 ? 273 ASN A CG  1 
ATOM   1704 O  OD1 . ASN A 1 245 ? 22.796  -9.411  74.718  1.00 32.87 ? 273 ASN A OD1 1 
ATOM   1705 N  ND2 . ASN A 1 245 ? 24.164  -9.017  72.974  1.00 36.68 ? 273 ASN A ND2 1 
ATOM   1706 N  N   . ASP A 1 246 ? 20.884  -4.710  73.987  1.00 30.76 ? 274 ASP A N   1 
ATOM   1707 C  CA  . ASP A 1 246 ? 20.714  -3.281  74.210  1.00 30.38 ? 274 ASP A CA  1 
ATOM   1708 C  C   . ASP A 1 246 ? 19.341  -2.945  74.789  1.00 34.82 ? 274 ASP A C   1 
ATOM   1709 O  O   . ASP A 1 246 ? 18.997  -1.767  74.917  1.00 27.82 ? 274 ASP A O   1 
ATOM   1710 C  CB  . ASP A 1 246 ? 20.966  -2.500  72.912  1.00 36.07 ? 274 ASP A CB  1 
ATOM   1711 C  CG  . ASP A 1 246 ? 20.016  -2.885  71.783  1.00 40.47 ? 274 ASP A CG  1 
ATOM   1712 O  OD1 . ASP A 1 246 ? 18.999  -3.584  72.022  1.00 35.27 ? 274 ASP A OD1 1 
ATOM   1713 O  OD2 . ASP A 1 246 ? 20.304  -2.482  70.635  1.00 39.06 ? 274 ASP A OD2 1 
ATOM   1714 N  N   . GLU A 1 247 ? 18.564  -3.966  75.141  1.00 31.94 ? 275 GLU A N   1 
ATOM   1715 C  CA  . GLU A 1 247 ? 17.273  -3.826  75.811  1.00 31.55 ? 275 GLU A CA  1 
ATOM   1716 C  C   . GLU A 1 247 ? 16.301  -2.993  74.985  1.00 29.19 ? 275 GLU A C   1 
ATOM   1717 O  O   . GLU A 1 247 ? 15.421  -2.325  75.528  1.00 29.78 ? 275 GLU A O   1 
ATOM   1718 C  CB  . GLU A 1 247 ? 17.453  -3.275  77.233  1.00 33.08 ? 275 GLU A CB  1 
ATOM   1719 C  CG  . GLU A 1 247 ? 18.627  -3.987  77.974  1.00 33.54 ? 275 GLU A CG  1 
ATOM   1720 C  CD  . GLU A 1 247 ? 18.702  -3.676  79.463  1.00 37.69 ? 275 GLU A CD  1 
ATOM   1721 O  OE1 . GLU A 1 247 ? 18.771  -4.635  80.263  1.00 44.96 ? 275 GLU A OE1 1 
ATOM   1722 O  OE2 . GLU A 1 247 ? 18.694  -2.481  79.834  1.00 37.13 ? 275 GLU A OE2 1 
ATOM   1723 N  N   . MET A 1 248 ? 16.455  -3.045  73.656  1.00 27.84 ? 276 MET A N   1 
ATOM   1724 C  CA  . MET A 1 248 ? 15.491  -2.456  72.732  1.00 29.02 ? 276 MET A CA  1 
ATOM   1725 C  C   . MET A 1 248 ? 14.396  -3.429  72.302  1.00 25.35 ? 276 MET A C   1 
ATOM   1726 O  O   . MET A 1 248 ? 13.343  -2.990  71.832  1.00 28.73 ? 276 MET A O   1 
ATOM   1727 C  CB  . MET A 1 248 ? 16.195  -1.943  71.477  1.00 33.79 ? 276 MET A CB  1 
ATOM   1728 C  CG  . MET A 1 248 ? 17.027  -0.707  71.703  1.00 32.38 ? 276 MET A CG  1 
ATOM   1729 S  SD  . MET A 1 248 ? 16.001  0.709   72.121  1.00 47.91 ? 276 MET A SD  1 
ATOM   1730 C  CE  . MET A 1 248 ? 16.682  1.064   73.691  1.00 43.34 ? 276 MET A CE  1 
ATOM   1731 N  N   . VAL A 1 249 ? 14.626  -4.730  72.408  1.00 26.71 ? 277 VAL A N   1 
ATOM   1732 C  CA  . VAL A 1 249 ? 13.570  -5.717  72.230  1.00 22.95 ? 277 VAL A CA  1 
ATOM   1733 C  C   . VAL A 1 249 ? 13.185  -6.187  73.624  1.00 26.00 ? 277 VAL A C   1 
ATOM   1734 O  O   . VAL A 1 249 ? 14.031  -6.696  74.370  1.00 25.98 ? 277 VAL A O   1 
ATOM   1735 C  CB  . VAL A 1 249 ? 14.017  -6.872  71.316  1.00 24.13 ? 277 VAL A CB  1 
ATOM   1736 C  CG1 . VAL A 1 249 ? 12.997  -7.998  71.299  1.00 22.08 ? 277 VAL A CG1 1 
ATOM   1737 C  CG2 . VAL A 1 249 ? 14.225  -6.334  69.896  1.00 25.04 ? 277 VAL A CG2 1 
ATOM   1738 N  N   . LEU A 1 250 ? 11.931  -5.928  74.005  1.00 23.46 ? 278 LEU A N   1 
ATOM   1739 C  CA  . LEU A 1 250 ? 11.427  -6.167  75.355  1.00 19.10 ? 278 LEU A CA  1 
ATOM   1740 C  C   . LEU A 1 250 ? 10.208  -7.062  75.243  1.00 24.60 ? 278 LEU A C   1 
ATOM   1741 O  O   . LEU A 1 250 ? 9.243   -6.696  74.566  1.00 22.88 ? 278 LEU A O   1 
ATOM   1742 C  CB  . LEU A 1 250 ? 11.045  -4.856  76.051  1.00 24.39 ? 278 LEU A CB  1 
ATOM   1743 C  CG  . LEU A 1 250 ? 12.216  -3.883  76.235  1.00 25.95 ? 278 LEU A CG  1 
ATOM   1744 C  CD1 . LEU A 1 250 ? 11.740  -2.522  76.680  1.00 25.80 ? 278 LEU A CD1 1 
ATOM   1745 C  CD2 . LEU A 1 250 ? 13.170  -4.471  77.249  1.00 26.81 ? 278 LEU A CD2 1 
ATOM   1746 N  N   . LEU A 1 251 ? 10.240  -8.205  75.931  1.00 24.18 ? 279 LEU A N   1 
ATOM   1747 C  CA  . LEU A 1 251 ? 9.180   -9.215  75.861  1.00 24.08 ? 279 LEU A CA  1 
ATOM   1748 C  C   . LEU A 1 251 ? 8.702   -9.573  77.261  1.00 25.45 ? 279 LEU A C   1 
ATOM   1749 O  O   . LEU A 1 251 ? 9.143   -10.579 77.834  1.00 27.23 ? 279 LEU A O   1 
ATOM   1750 C  CB  . LEU A 1 251 ? 9.673   -10.477 75.145  1.00 20.44 ? 279 LEU A CB  1 
ATOM   1751 C  CG  . LEU A 1 251 ? 10.056  -10.273 73.684  1.00 20.91 ? 279 LEU A CG  1 
ATOM   1752 C  CD1 . LEU A 1 251 ? 10.697  -11.513 73.074  1.00 25.46 ? 279 LEU A CD1 1 
ATOM   1753 C  CD2 . LEU A 1 251 ? 8.814   -9.874  72.885  1.00 21.50 ? 279 LEU A CD2 1 
ATOM   1754 N  N   . PRO A 1 252 ? 7.793   -8.790  77.836  1.00 22.42 ? 280 PRO A N   1 
ATOM   1755 C  CA  . PRO A 1 252 ? 7.185   -9.189  79.109  1.00 22.10 ? 280 PRO A CA  1 
ATOM   1756 C  C   . PRO A 1 252 ? 6.267   -10.403 78.938  1.00 28.91 ? 280 PRO A C   1 
ATOM   1757 O  O   . PRO A 1 252 ? 5.674   -10.621 77.875  1.00 24.20 ? 280 PRO A O   1 
ATOM   1758 C  CB  . PRO A 1 252 ? 6.386   -7.948  79.523  1.00 23.18 ? 280 PRO A CB  1 
ATOM   1759 C  CG  . PRO A 1 252 ? 6.987   -6.809  78.764  1.00 22.26 ? 280 PRO A CG  1 
ATOM   1760 C  CD  . PRO A 1 252 ? 7.451   -7.399  77.468  1.00 22.24 ? 280 PRO A CD  1 
ATOM   1761 N  N   . ILE A 1 253 ? 6.163   -11.200 80.005  1.00 24.04 ? 281 ILE A N   1 
ATOM   1762 C  CA  . ILE A 1 253 ? 5.291   -12.375 80.043  1.00 23.04 ? 281 ILE A CA  1 
ATOM   1763 C  C   . ILE A 1 253 ? 4.590   -12.405 81.398  1.00 28.12 ? 281 ILE A C   1 
ATOM   1764 O  O   . ILE A 1 253 ? 5.237   -12.206 82.431  1.00 27.88 ? 281 ILE A O   1 
ATOM   1765 C  CB  . ILE A 1 253 ? 6.072   -13.686 79.811  1.00 24.97 ? 281 ILE A CB  1 
ATOM   1766 C  CG1 . ILE A 1 253 ? 6.869   -13.627 78.502  1.00 24.92 ? 281 ILE A CG1 1 
ATOM   1767 C  CG2 . ILE A 1 253 ? 5.108   -14.906 79.823  1.00 23.32 ? 281 ILE A CG2 1 
ATOM   1768 C  CD1 . ILE A 1 253 ? 7.761   -14.849 78.241  1.00 26.96 ? 281 ILE A CD1 1 
ATOM   1769 N  N   . ASN A 1 254 ? 3.264   -12.628 81.395  1.00 23.89 ? 282 ASN A N   1 
ATOM   1770 C  CA  . ASN A 1 254 ? 2.447   -12.668 82.601  1.00 24.16 ? 282 ASN A CA  1 
ATOM   1771 C  C   . ASN A 1 254 ? 1.834   -14.056 82.783  1.00 30.00 ? 282 ASN A C   1 
ATOM   1772 O  O   . ASN A 1 254 ? 1.597   -14.772 81.807  1.00 29.29 ? 282 ASN A O   1 
ATOM   1773 C  CB  . ASN A 1 254 ? 1.270   -11.656 82.568  1.00 22.87 ? 282 ASN A CB  1 
ATOM   1774 C  CG  . ASN A 1 254 ? 1.657   -10.285 82.045  1.00 30.02 ? 282 ASN A CG  1 
ATOM   1775 O  OD1 . ASN A 1 254 ? 2.679   -9.711  82.434  1.00 30.26 ? 282 ASN A OD1 1 
ATOM   1776 N  ND2 . ASN A 1 254 ? 0.797   -9.729  81.192  1.00 24.26 ? 282 ASN A ND2 1 
ATOM   1777 N  N   . GLU A 1 255 ? 1.552   -14.410 84.033  1.00 29.08 ? 283 GLU A N   1 
ATOM   1778 C  CA  . GLU A 1 255 ? 0.744   -15.560 84.417  1.00 26.23 ? 283 GLU A CA  1 
ATOM   1779 C  C   . GLU A 1 255 ? -0.289  -15.094 85.431  1.00 30.62 ? 283 GLU A C   1 
ATOM   1780 O  O   . GLU A 1 255 ? -0.078  -14.088 86.118  1.00 35.04 ? 283 GLU A O   1 
ATOM   1781 C  CB  . GLU A 1 255 ? 1.608   -16.678 85.026  1.00 31.55 ? 283 GLU A CB  1 
ATOM   1782 C  CG  . GLU A 1 255 ? 2.115   -16.331 86.420  1.00 33.77 ? 283 GLU A CG  1 
ATOM   1783 C  CD  . GLU A 1 255 ? 2.950   -17.425 87.077  1.00 42.68 ? 283 GLU A CD  1 
ATOM   1784 O  OE1 . GLU A 1 255 ? 3.454   -17.155 88.187  1.00 39.73 ? 283 GLU A OE1 1 
ATOM   1785 O  OE2 . GLU A 1 255 ? 3.114   -18.535 86.505  1.00 35.93 ? 283 GLU A OE2 1 
ATOM   1786 N  N   . PRO A 1 256 ? -1.425  -15.783 85.545  1.00 32.40 ? 284 PRO A N   1 
ATOM   1787 C  CA  . PRO A 1 256 ? -2.419  -15.380 86.550  1.00 36.19 ? 284 PRO A CA  1 
ATOM   1788 C  C   . PRO A 1 256 ? -1.964  -15.769 87.948  1.00 39.69 ? 284 PRO A C   1 
ATOM   1789 O  O   . PRO A 1 256 ? -1.187  -16.705 88.133  1.00 41.69 ? 284 PRO A O   1 
ATOM   1790 C  CB  . PRO A 1 256 ? -3.684  -16.158 86.158  1.00 37.31 ? 284 PRO A CB  1 
ATOM   1791 C  CG  . PRO A 1 256 ? -3.341  -16.932 84.931  1.00 38.34 ? 284 PRO A CG  1 
ATOM   1792 C  CD  . PRO A 1 256 ? -1.855  -16.975 84.798  1.00 31.87 ? 284 PRO A CD  1 
ATOM   1793 N  N   . VAL A 1 257 ? -2.459  -15.042 88.947  1.00 45.78 ? 285 VAL A N   1 
ATOM   1794 C  CA  . VAL A 1 257 ? -2.335  -15.489 90.333  1.00 56.09 ? 285 VAL A CA  1 
ATOM   1795 C  C   . VAL A 1 257 ? -3.730  -15.903 90.791  1.00 52.58 ? 285 VAL A C   1 
ATOM   1796 O  O   . VAL A 1 257 ? -4.615  -15.065 91.000  1.00 50.62 ? 285 VAL A O   1 
ATOM   1797 C  CB  . VAL A 1 257 ? -1.700  -14.435 91.254  1.00 49.60 ? 285 VAL A CB  1 
ATOM   1798 C  CG1 . VAL A 1 257 ? -0.247  -14.219 90.876  1.00 46.95 ? 285 VAL A CG1 1 
ATOM   1799 C  CG2 . VAL A 1 257 ? -2.437  -13.127 91.225  1.00 55.01 ? 285 VAL A CG2 1 
ATOM   1800 N  N   . HIS A 1 258 ? -3.935  -17.217 90.915  1.00 60.16 ? 286 HIS A N   1 
ATOM   1801 C  CA  . HIS A 1 258 ? -5.220  -17.769 91.325  1.00 64.10 ? 286 HIS A CA  1 
ATOM   1802 C  C   . HIS A 1 258 ? -5.362  -17.700 92.841  1.00 67.99 ? 286 HIS A C   1 
ATOM   1803 O  O   . HIS A 1 258 ? -4.424  -18.033 93.576  1.00 61.14 ? 286 HIS A O   1 
ATOM   1804 C  CB  . HIS A 1 258 ? -5.355  -19.222 90.864  1.00 61.80 ? 286 HIS A CB  1 
ATOM   1805 C  CG  . HIS A 1 258 ? -5.223  -19.411 89.384  1.00 61.06 ? 286 HIS A CG  1 
ATOM   1806 N  ND1 . HIS A 1 258 ? -4.392  -20.362 88.828  1.00 64.57 ? 286 HIS A ND1 1 
ATOM   1807 C  CD2 . HIS A 1 258 ? -5.830  -18.788 88.346  1.00 53.74 ? 286 HIS A CD2 1 
ATOM   1808 C  CE1 . HIS A 1 258 ? -4.483  -20.308 87.511  1.00 60.04 ? 286 HIS A CE1 1 
ATOM   1809 N  NE2 . HIS A 1 258 ? -5.352  -19.364 87.193  1.00 52.00 ? 286 HIS A NE2 1 
ATOM   1810 N  N   . GLY A 1 259 ? -6.535  -17.271 93.304  1.00 69.06 ? 287 GLY A N   1 
ATOM   1811 C  CA  . GLY A 1 259 ? -6.848  -17.283 94.721  1.00 70.39 ? 287 GLY A CA  1 
ATOM   1812 C  C   . GLY A 1 259 ? -7.073  -15.912 95.326  1.00 74.18 ? 287 GLY A C   1 
ATOM   1813 O  O   . GLY A 1 259 ? -6.787  -15.703 96.508  1.00 78.83 ? 287 GLY A O   1 
ATOM   1814 N  N   . THR A 1 260 ? -7.597  -14.975 94.537  1.00 79.30 ? 288 THR A N   1 
ATOM   1815 C  CA  . THR A 1 260 ? -7.772  -13.589 94.942  1.00 75.75 ? 288 THR A CA  1 
ATOM   1816 C  C   . THR A 1 260 ? -9.261  -13.256 95.101  1.00 82.14 ? 288 THR A C   1 
ATOM   1817 O  O   . THR A 1 260 ? -10.105 -14.158 95.222  1.00 82.75 ? 288 THR A O   1 
ATOM   1818 C  CB  . THR A 1 260 ? -7.069  -12.689 93.920  1.00 78.79 ? 288 THR A CB  1 
ATOM   1819 O  OG1 . THR A 1 260 ? -7.462  -11.324 94.125  1.00 79.65 ? 288 THR A OG1 1 
ATOM   1820 C  CG2 . THR A 1 260 ? -7.415  -13.123 92.499  1.00 74.40 ? 288 THR A CG2 1 
ATOM   1821 N  N   . LYS A 1 261 ? -9.579  -11.958 95.118  1.00 81.52 ? 289 LYS A N   1 
ATOM   1822 C  CA  . LYS A 1 261 ? -10.960 -11.497 95.216  1.00 80.20 ? 289 LYS A CA  1 
ATOM   1823 C  C   . LYS A 1 261 ? -11.532 -11.252 93.826  1.00 79.99 ? 289 LYS A C   1 
ATOM   1824 O  O   . LYS A 1 261 ? -12.281 -12.086 93.302  1.00 80.13 ? 289 LYS A O   1 
ATOM   1825 C  CB  . LYS A 1 261 ? -11.046 -10.223 96.061  1.00 76.98 ? 289 LYS A CB  1 
ATOM   1826 N  N   . ARG A 1 262 ? -11.195 -10.107 93.231  1.00 78.65 ? 290 ARG A N   1 
ATOM   1827 C  CA  . ARG A 1 262 ? -11.512 -9.868  91.829  1.00 72.62 ? 290 ARG A CA  1 
ATOM   1828 C  C   . ARG A 1 262 ? -10.753 -10.861 90.959  1.00 69.79 ? 290 ARG A C   1 
ATOM   1829 O  O   . ARG A 1 262 ? -9.617  -11.231 91.264  1.00 69.55 ? 290 ARG A O   1 
ATOM   1830 C  CB  . ARG A 1 262 ? -11.156 -8.435  91.437  1.00 70.55 ? 290 ARG A CB  1 
ATOM   1831 N  N   . LYS A 1 263 ? -11.390 -11.304 89.877  1.00 68.52 ? 291 LYS A N   1 
ATOM   1832 C  CA  . LYS A 1 263 ? -10.808 -12.358 89.056  1.00 64.60 ? 291 LYS A CA  1 
ATOM   1833 C  C   . LYS A 1 263 ? -9.572  -11.852 88.322  1.00 56.32 ? 291 LYS A C   1 
ATOM   1834 O  O   . LYS A 1 263 ? -9.506  -10.693 87.902  1.00 55.80 ? 291 LYS A O   1 
ATOM   1835 C  CB  . LYS A 1 263 ? -11.836 -12.888 88.056  1.00 59.06 ? 291 LYS A CB  1 
ATOM   1836 C  CG  . LYS A 1 263 ? -11.560 -14.309 87.554  1.00 57.98 ? 291 LYS A CG  1 
ATOM   1837 C  CD  . LYS A 1 263 ? -12.202 -14.529 86.188  1.00 53.22 ? 291 LYS A CD  1 
ATOM   1838 C  CE  . LYS A 1 263 ? -12.271 -15.998 85.818  1.00 52.36 ? 291 LYS A CE  1 
ATOM   1839 N  NZ  . LYS A 1 263 ? -13.264 -16.246 84.718  1.00 52.83 ? 291 LYS A NZ  1 
ATOM   1840 N  N   . SER A 1 264 ? -8.581  -12.729 88.188  1.00 56.58 ? 292 SER A N   1 
ATOM   1841 C  CA  . SER A 1 264 ? -7.389  -12.405 87.418  1.00 48.56 ? 292 SER A CA  1 
ATOM   1842 C  C   . SER A 1 264 ? -7.771  -12.089 85.980  1.00 44.97 ? 292 SER A C   1 
ATOM   1843 O  O   . SER A 1 264 ? -8.363  -12.927 85.288  1.00 42.45 ? 292 SER A O   1 
ATOM   1844 C  CB  . SER A 1 264 ? -6.405  -13.572 87.458  1.00 42.15 ? 292 SER A CB  1 
ATOM   1845 O  OG  . SER A 1 264 ? -5.219  -13.255 86.742  1.00 46.35 ? 292 SER A OG  1 
ATOM   1846 N  N   . GLN A 1 265 ? -7.438  -10.878 85.533  1.00 37.32 ? 293 GLN A N   1 
ATOM   1847 C  CA  . GLN A 1 265 ? -7.624  -10.549 84.130  1.00 38.88 ? 293 GLN A CA  1 
ATOM   1848 C  C   . GLN A 1 265 ? -6.761  -11.423 83.233  1.00 35.85 ? 293 GLN A C   1 
ATOM   1849 O  O   . GLN A 1 265 ? -7.115  -11.630 82.068  1.00 33.75 ? 293 GLN A O   1 
ATOM   1850 C  CB  . GLN A 1 265 ? -7.337  -9.062  83.882  1.00 37.32 ? 293 GLN A CB  1 
ATOM   1851 C  CG  . GLN A 1 265 ? -5.859  -8.663  83.813  1.00 43.00 ? 293 GLN A CG  1 
ATOM   1852 C  CD  . GLN A 1 265 ? -5.280  -8.286  85.165  1.00 50.98 ? 293 GLN A CD  1 
ATOM   1853 O  OE1 . GLN A 1 265 ? -6.009  -8.185  86.154  1.00 49.86 ? 293 GLN A OE1 1 
ATOM   1854 N  NE2 . GLN A 1 265 ? -3.963  -8.052  85.212  1.00 40.61 ? 293 GLN A NE2 1 
ATOM   1855 N  N   . ILE A 1 266 ? -5.641  -11.948 83.743  1.00 33.95 ? 294 ILE A N   1 
ATOM   1856 C  CA  . ILE A 1 266 ? -4.872  -12.901 82.950  1.00 29.03 ? 294 ILE A CA  1 
ATOM   1857 C  C   . ILE A 1 266 ? -5.672  -14.176 82.738  1.00 33.92 ? 294 ILE A C   1 
ATOM   1858 O  O   . ILE A 1 266 ? -5.687  -14.739 81.637  1.00 29.11 ? 294 ILE A O   1 
ATOM   1859 C  CB  . ILE A 1 266 ? -3.514  -13.201 83.606  1.00 27.82 ? 294 ILE A CB  1 
ATOM   1860 C  CG1 . ILE A 1 266 ? -2.828  -11.902 84.036  1.00 29.85 ? 294 ILE A CG1 1 
ATOM   1861 C  CG2 . ILE A 1 266 ? -2.645  -13.987 82.647  1.00 26.98 ? 294 ILE A CG2 1 
ATOM   1862 C  CD1 . ILE A 1 266 ? -2.629  -10.879 82.895  1.00 26.54 ? 294 ILE A CD1 1 
ATOM   1863 N  N   . GLN A 1 267 ? -6.334  -14.663 83.790  1.00 31.47 ? 295 GLN A N   1 
ATOM   1864 C  CA  . GLN A 1 267 ? -7.154  -15.860 83.651  1.00 35.05 ? 295 GLN A CA  1 
ATOM   1865 C  C   . GLN A 1 267 ? -8.306  -15.618 82.687  1.00 31.14 ? 295 GLN A C   1 
ATOM   1866 O  O   . GLN A 1 267 ? -8.598  -16.463 81.831  1.00 31.88 ? 295 GLN A O   1 
ATOM   1867 C  CB  . GLN A 1 267 ? -7.682  -16.297 85.017  1.00 39.45 ? 295 GLN A CB  1 
ATOM   1868 C  CG  . GLN A 1 267 ? -8.606  -17.515 84.961  1.00 42.40 ? 295 GLN A CG  1 
ATOM   1869 C  CD  . GLN A 1 267 ? -7.882  -18.774 84.543  1.00 39.85 ? 295 GLN A CD  1 
ATOM   1870 O  OE1 . GLN A 1 267 ? -6.666  -18.864 84.652  1.00 44.53 ? 295 GLN A OE1 1 
ATOM   1871 N  NE2 . GLN A 1 267 ? -8.633  -19.762 84.061  1.00 41.86 ? 295 GLN A NE2 1 
ATOM   1872 N  N   . THR A 1 268 ? -8.969  -14.466 82.812  1.00 32.23 ? 296 THR A N   1 
ATOM   1873 C  CA  . THR A 1 268 ? -10.018 -14.102 81.865  1.00 32.15 ? 296 THR A CA  1 
ATOM   1874 C  C   . THR A 1 268 ? -9.496  -14.122 80.436  1.00 30.55 ? 296 THR A C   1 
ATOM   1875 O  O   . THR A 1 268 ? -10.160 -14.653 79.536  1.00 28.05 ? 296 THR A O   1 
ATOM   1876 C  CB  . THR A 1 268 ? -10.582 -12.724 82.214  1.00 38.11 ? 296 THR A CB  1 
ATOM   1877 O  OG1 . THR A 1 268 ? -11.259 -12.786 83.476  1.00 38.57 ? 296 THR A OG1 1 
ATOM   1878 C  CG2 . THR A 1 268 ? -11.561 -12.250 81.144  1.00 34.37 ? 296 THR A CG2 1 
ATOM   1879 N  N   . TYR A 1 269 ? -8.306  -13.545 80.207  1.00 28.00 ? 297 TYR A N   1 
ATOM   1880 C  CA  . TYR A 1 269 ? -7.686  -13.613 78.885  1.00 26.20 ? 297 TYR A CA  1 
ATOM   1881 C  C   . TYR A 1 269 ? -7.559  -15.059 78.419  1.00 26.32 ? 297 TYR A C   1 
ATOM   1882 O  O   . TYR A 1 269 ? -7.933  -15.394 77.289  1.00 24.32 ? 297 TYR A O   1 
ATOM   1883 C  CB  . TYR A 1 269 ? -6.301  -12.934 78.900  1.00 24.04 ? 297 TYR A CB  1 
ATOM   1884 C  CG  . TYR A 1 269 ? -5.573  -13.043 77.564  1.00 22.25 ? 297 TYR A CG  1 
ATOM   1885 C  CD1 . TYR A 1 269 ? -4.955  -14.228 77.185  1.00 22.49 ? 297 TYR A CD1 1 
ATOM   1886 C  CD2 . TYR A 1 269 ? -5.523  -11.970 76.677  1.00 21.84 ? 297 TYR A CD2 1 
ATOM   1887 C  CE1 . TYR A 1 269 ? -4.330  -14.362 75.970  1.00 22.63 ? 297 TYR A CE1 1 
ATOM   1888 C  CE2 . TYR A 1 269 ? -4.895  -12.093 75.444  1.00 21.36 ? 297 TYR A CE2 1 
ATOM   1889 C  CZ  . TYR A 1 269 ? -4.298  -13.294 75.100  1.00 20.39 ? 297 TYR A CZ  1 
ATOM   1890 O  OH  . TYR A 1 269 ? -3.675  -13.459 73.878  1.00 20.42 ? 297 TYR A OH  1 
ATOM   1891 N  N   . LEU A 1 270 ? -6.976  -15.926 79.260  1.00 27.71 ? 298 LEU A N   1 
ATOM   1892 C  CA  . LEU A 1 270 ? -6.700  -17.293 78.830  1.00 26.66 ? 298 LEU A CA  1 
ATOM   1893 C  C   . LEU A 1 270 ? -7.986  -18.042 78.504  1.00 25.14 ? 298 LEU A C   1 
ATOM   1894 O  O   . LEU A 1 270 ? -8.017  -18.857 77.578  1.00 27.48 ? 298 LEU A O   1 
ATOM   1895 C  CB  . LEU A 1 270 ? -5.911  -18.043 79.907  1.00 31.49 ? 298 LEU A CB  1 
ATOM   1896 C  CG  . LEU A 1 270 ? -4.532  -17.503 80.251  1.00 29.56 ? 298 LEU A CG  1 
ATOM   1897 C  CD1 . LEU A 1 270 ? -4.052  -18.094 81.579  1.00 36.39 ? 298 LEU A CD1 1 
ATOM   1898 C  CD2 . LEU A 1 270 ? -3.541  -17.822 79.122  1.00 27.68 ? 298 LEU A CD2 1 
ATOM   1899 N  N   . GLU A 1 271 ? -9.060  -17.751 79.231  1.00 25.17 ? 299 GLU A N   1 
ATOM   1900 C  CA  . GLU A 1 271 ? -10.340 -18.407 78.964  1.00 30.20 ? 299 GLU A CA  1 
ATOM   1901 C  C   . GLU A 1 271 ? -10.909 -17.986 77.608  1.00 29.36 ? 299 GLU A C   1 
ATOM   1902 O  O   . GLU A 1 271 ? -11.255 -18.838 76.774  1.00 27.67 ? 299 GLU A O   1 
ATOM   1903 C  CB  . GLU A 1 271 ? -11.318 -18.104 80.104  1.00 37.67 ? 299 GLU A CB  1 
ATOM   1904 C  CG  . GLU A 1 271 ? -11.054 -18.954 81.365  1.00 40.59 ? 299 GLU A CG  1 
ATOM   1905 C  CD  . GLU A 1 271 ? -11.718 -18.413 82.630  1.00 40.65 ? 299 GLU A CD  1 
ATOM   1906 O  OE1 . GLU A 1 271 ? -12.514 -17.452 82.553  1.00 42.10 ? 299 GLU A OE1 1 
ATOM   1907 O  OE2 . GLU A 1 271 ? -11.434 -18.968 83.713  1.00 45.72 ? 299 GLU A OE2 1 
ATOM   1908 N  N   . HIS A 1 272 ? -10.967 -16.677 77.346  1.00 25.54 ? 300 HIS A N   1 
ATOM   1909 C  CA  . HIS A 1 272 ? -11.593 -16.202 76.117  1.00 22.78 ? 300 HIS A CA  1 
ATOM   1910 C  C   . HIS A 1 272 ? -10.704 -16.389 74.894  1.00 24.04 ? 300 HIS A C   1 
ATOM   1911 O  O   . HIS A 1 272 ? -11.223 -16.470 73.776  1.00 24.17 ? 300 HIS A O   1 
ATOM   1912 C  CB  . HIS A 1 272 ? -11.998 -14.737 76.281  1.00 26.88 ? 300 HIS A CB  1 
ATOM   1913 C  CG  . HIS A 1 272 ? -13.165 -14.541 77.201  1.00 27.79 ? 300 HIS A CG  1 
ATOM   1914 N  ND1 . HIS A 1 272 ? -14.451 -14.334 76.744  1.00 25.78 ? 300 HIS A ND1 1 
ATOM   1915 C  CD2 . HIS A 1 272 ? -13.247 -14.577 78.552  1.00 27.75 ? 300 HIS A CD2 1 
ATOM   1916 C  CE1 . HIS A 1 272 ? -15.265 -14.202 77.777  1.00 27.43 ? 300 HIS A CE1 1 
ATOM   1917 N  NE2 . HIS A 1 272 ? -14.561 -14.362 78.884  1.00 29.96 ? 300 HIS A NE2 1 
ATOM   1918 N  N   . ASN A 1 273 ? -9.388  -16.487 75.079  1.00 22.41 ? 301 ASN A N   1 
ATOM   1919 C  CA  . ASN A 1 273 ? -8.441  -16.687 73.989  1.00 22.75 ? 301 ASN A CA  1 
ATOM   1920 C  C   . ASN A 1 273 ? -8.210  -18.153 73.659  1.00 25.29 ? 301 ASN A C   1 
ATOM   1921 O  O   . ASN A 1 273 ? -7.482  -18.449 72.704  1.00 24.52 ? 301 ASN A O   1 
ATOM   1922 C  CB  . ASN A 1 273 ? -7.078  -16.071 74.345  1.00 23.07 ? 301 ASN A CB  1 
ATOM   1923 C  CG  . ASN A 1 273 ? -6.224  -15.824 73.128  1.00 24.51 ? 301 ASN A CG  1 
ATOM   1924 O  OD1 . ASN A 1 273 ? -6.605  -15.036 72.268  1.00 26.90 ? 301 ASN A OD1 1 
ATOM   1925 N  ND2 . ASN A 1 273 ? -5.045  -16.455 73.065  1.00 21.46 ? 301 ASN A ND2 1 
ATOM   1926 N  N   . GLU A 1 274 ? -8.788  -19.069 74.434  1.00 24.46 ? 302 GLU A N   1 
ATOM   1927 C  CA  . GLU A 1 274 ? -8.438  -20.487 74.352  1.00 20.81 ? 302 GLU A CA  1 
ATOM   1928 C  C   . GLU A 1 274 ? -6.936  -20.678 74.544  1.00 23.10 ? 302 GLU A C   1 
ATOM   1929 O  O   . GLU A 1 274 ? -6.261  -21.274 73.708  1.00 28.92 ? 302 GLU A O   1 
ATOM   1930 C  CB  . GLU A 1 274 ? -8.892  -21.107 73.028  1.00 25.59 ? 302 GLU A CB  1 
ATOM   1931 C  CG  . GLU A 1 274 ? -10.399 -21.157 72.866  1.00 23.05 ? 302 GLU A CG  1 
ATOM   1932 C  CD  . GLU A 1 274 ? -10.867 -21.989 71.675  1.00 25.37 ? 302 GLU A CD  1 
ATOM   1933 O  OE1 . GLU A 1 274 ? -10.029 -22.607 70.997  1.00 27.80 ? 302 GLU A OE1 1 
ATOM   1934 O  OE2 . GLU A 1 274 ? -12.095 -22.022 71.413  1.00 27.62 ? 302 GLU A OE2 1 
ATOM   1935 N  N   . GLY A 1 275 ? -6.411  -20.125 75.629  1.00 23.03 ? 303 GLY A N   1 
ATOM   1936 C  CA  . GLY A 1 275 ? -5.044  -20.393 76.038  1.00 24.89 ? 303 GLY A CA  1 
ATOM   1937 C  C   . GLY A 1 275 ? -4.126  -19.197 75.849  1.00 26.36 ? 303 GLY A C   1 
ATOM   1938 O  O   . GLY A 1 275 ? -4.558  -18.062 75.653  1.00 26.72 ? 303 GLY A O   1 
ATOM   1939 N  N   . ALA A 1 276 ? -2.826  -19.493 75.891  1.00 25.73 ? 304 ALA A N   1 
ATOM   1940 C  CA  . ALA A 1 276 ? -1.796  -18.462 75.867  1.00 23.63 ? 304 ALA A CA  1 
ATOM   1941 C  C   . ALA A 1 276 ? -1.797  -17.700 74.546  1.00 22.66 ? 304 ALA A C   1 
ATOM   1942 O  O   . ALA A 1 276 ? -2.162  -18.230 73.489  1.00 24.49 ? 304 ALA A O   1 
ATOM   1943 C  CB  . ALA A 1 276 ? -0.422  -19.094 76.089  1.00 24.74 ? 304 ALA A CB  1 
ATOM   1944 N  N   . GLY A 1 277 ? -1.353  -16.450 74.612  1.00 23.10 ? 305 GLY A N   1 
ATOM   1945 C  CA  . GLY A 1 277 ? -1.241  -15.624 73.428  1.00 21.49 ? 305 GLY A CA  1 
ATOM   1946 C  C   . GLY A 1 277 ? -0.761  -14.239 73.805  1.00 24.17 ? 305 GLY A C   1 
ATOM   1947 O  O   . GLY A 1 277 ? -0.445  -13.947 74.965  1.00 23.94 ? 305 GLY A O   1 
ATOM   1948 N  N   . LEU A 1 278 ? -0.717  -13.378 72.803  1.00 20.12 ? 306 LEU A N   1 
ATOM   1949 C  CA  . LEU A 1 278 ? -0.231  -12.025 73.017  1.00 19.51 ? 306 LEU A CA  1 
ATOM   1950 C  C   . LEU A 1 278 ? -1.318  -11.190 73.698  1.00 24.73 ? 306 LEU A C   1 
ATOM   1951 O  O   . LEU A 1 278 ? -2.467  -11.142 73.232  1.00 21.65 ? 306 LEU A O   1 
ATOM   1952 C  CB  . LEU A 1 278 ? 0.183   -11.427 71.680  1.00 19.32 ? 306 LEU A CB  1 
ATOM   1953 C  CG  . LEU A 1 278 ? 0.954   -10.124 71.849  1.00 20.95 ? 306 LEU A CG  1 
ATOM   1954 C  CD1 . LEU A 1 278 ? 2.125   -10.041 70.888  1.00 24.08 ? 306 LEU A CD1 1 
ATOM   1955 C  CD2 . LEU A 1 278 ? -0.012  -8.960  71.655  1.00 22.38 ? 306 LEU A CD2 1 
ATOM   1956 N  N   . GLN A 1 279 ? -0.961  -10.561 74.825  1.00 20.78 ? 307 GLN A N   1 
ATOM   1957 C  CA  . GLN A 1 279 ? -1.911  -9.755  75.591  1.00 22.35 ? 307 GLN A CA  1 
ATOM   1958 C  C   . GLN A 1 279 ? -1.979  -8.311  75.101  1.00 20.42 ? 307 GLN A C   1 
ATOM   1959 O  O   . GLN A 1 279 ? -3.078  -7.796  74.851  1.00 20.76 ? 307 GLN A O   1 
ATOM   1960 C  CB  . GLN A 1 279 ? -1.571  -9.751  77.089  1.00 23.31 ? 307 GLN A CB  1 
ATOM   1961 C  CG  . GLN A 1 279 ? -2.480  -8.804  77.914  1.00 23.21 ? 307 GLN A CG  1 
ATOM   1962 C  CD  . GLN A 1 279 ? -1.841  -8.328  79.219  1.00 24.97 ? 307 GLN A CD  1 
ATOM   1963 O  OE1 . GLN A 1 279 ? -0.695  -7.875  79.226  1.00 24.89 ? 307 GLN A OE1 1 
ATOM   1964 N  NE2 . GLN A 1 279 ? -2.584  -8.414  80.319  1.00 25.32 ? 307 GLN A NE2 1 
ATOM   1965 N  N   . HIS A 1 280 ? -0.835  -7.632  74.994  1.00 22.16 ? 308 HIS A N   1 
ATOM   1966 C  CA  . HIS A 1 280 ? -0.885  -6.257  74.525  1.00 20.18 ? 308 HIS A CA  1 
ATOM   1967 C  C   . HIS A 1 280 ? 0.388   -5.851  73.790  1.00 19.44 ? 308 HIS A C   1 
ATOM   1968 O  O   . HIS A 1 280 ? 1.472   -6.431  73.965  1.00 20.46 ? 308 HIS A O   1 
ATOM   1969 C  CB  . HIS A 1 280 ? -1.236  -5.273  75.671  1.00 19.76 ? 308 HIS A CB  1 
ATOM   1970 C  CG  . HIS A 1 280 ? -0.117  -4.946  76.626  1.00 23.40 ? 308 HIS A CG  1 
ATOM   1971 N  ND1 . HIS A 1 280 ? 0.141   -5.689  77.760  1.00 22.63 ? 308 HIS A ND1 1 
ATOM   1972 C  CD2 . HIS A 1 280 ? 0.742   -3.898  76.664  1.00 22.47 ? 308 HIS A CD2 1 
ATOM   1973 C  CE1 . HIS A 1 280 ? 1.129   -5.129  78.438  1.00 24.40 ? 308 HIS A CE1 1 
ATOM   1974 N  NE2 . HIS A 1 280 ? 1.516   -4.047  77.789  1.00 22.18 ? 308 HIS A NE2 1 
ATOM   1975 N  N   . LEU A 1 281 ? 0.207   -4.875  72.903  1.00 17.47 ? 309 LEU A N   1 
ATOM   1976 C  CA  . LEU A 1 281 ? 1.287   -4.205  72.197  1.00 18.75 ? 309 LEU A CA  1 
ATOM   1977 C  C   . LEU A 1 281 ? 1.400   -2.799  72.752  1.00 18.47 ? 309 LEU A C   1 
ATOM   1978 O  O   . LEU A 1 281 ? 0.402   -2.071  72.798  1.00 19.22 ? 309 LEU A O   1 
ATOM   1979 C  CB  . LEU A 1 281 ? 1.002   -4.161  70.698  1.00 17.45 ? 309 LEU A CB  1 
ATOM   1980 C  CG  . LEU A 1 281 ? 0.749   -5.522  70.045  1.00 19.95 ? 309 LEU A CG  1 
ATOM   1981 C  CD1 . LEU A 1 281 ? 0.014   -5.356  68.716  1.00 20.93 ? 309 LEU A CD1 1 
ATOM   1982 C  CD2 . LEU A 1 281 ? 2.086   -6.253  69.858  1.00 19.35 ? 309 LEU A CD2 1 
ATOM   1983 N  N   . ALA A 1 282 ? 2.598   -2.406  73.167  1.00 19.63 ? 310 ALA A N   1 
ATOM   1984 C  CA  . ALA A 1 282 ? 2.826   -1.049  73.653  1.00 20.49 ? 310 ALA A CA  1 
ATOM   1985 C  C   . ALA A 1 282 ? 3.527   -0.247  72.566  1.00 20.14 ? 310 ALA A C   1 
ATOM   1986 O  O   . ALA A 1 282 ? 4.612   -0.626  72.114  1.00 21.19 ? 310 ALA A O   1 
ATOM   1987 C  CB  . ALA A 1 282 ? 3.663   -1.042  74.931  1.00 22.15 ? 310 ALA A CB  1 
ATOM   1988 N  N   . LEU A 1 283 ? 2.918   0.870   72.177  1.00 19.87 ? 311 LEU A N   1 
ATOM   1989 C  CA  . LEU A 1 283 ? 3.342   1.663   71.033  1.00 17.26 ? 311 LEU A CA  1 
ATOM   1990 C  C   . LEU A 1 283 ? 3.879   2.988   71.546  1.00 21.35 ? 311 LEU A C   1 
ATOM   1991 O  O   . LEU A 1 283 ? 3.147   3.740   72.199  1.00 19.61 ? 311 LEU A O   1 
ATOM   1992 C  CB  . LEU A 1 283 ? 2.180   1.893   70.071  1.00 19.74 ? 311 LEU A CB  1 
ATOM   1993 C  CG  . LEU A 1 283 ? 1.315   0.632   69.816  1.00 16.25 ? 311 LEU A CG  1 
ATOM   1994 C  CD1 . LEU A 1 283 ? 0.247   0.963   68.776  1.00 16.84 ? 311 LEU A CD1 1 
ATOM   1995 C  CD2 . LEU A 1 283 ? 2.127   -0.563  69.345  1.00 17.77 ? 311 LEU A CD2 1 
ATOM   1996 N  N   . MET A 1 284 ? 5.158   3.253   71.281  1.00 22.59 ? 312 MET A N   1 
ATOM   1997 C  CA  . MET A 1 284 ? 5.755   4.504   71.720  1.00 22.19 ? 312 MET A CA  1 
ATOM   1998 C  C   . MET A 1 284 ? 5.302   5.647   70.825  1.00 21.78 ? 312 MET A C   1 
ATOM   1999 O  O   . MET A 1 284 ? 5.326   5.544   69.593  1.00 22.89 ? 312 MET A O   1 
ATOM   2000 C  CB  A MET A 1 284 ? 7.280   4.410   71.718  0.54 24.05 ? 312 MET A CB  1 
ATOM   2001 C  CB  B MET A 1 284 ? 7.285   4.408   71.727  0.46 24.02 ? 312 MET A CB  1 
ATOM   2002 C  CG  A MET A 1 284 ? 7.969   5.706   72.151  0.54 25.71 ? 312 MET A CG  1 
ATOM   2003 C  CG  B MET A 1 284 ? 8.008   5.737   72.041  0.46 25.71 ? 312 MET A CG  1 
ATOM   2004 S  SD  A MET A 1 284 ? 9.661   5.380   72.648  0.54 39.53 ? 312 MET A SD  1 
ATOM   2005 S  SD  B MET A 1 284 ? 8.300   6.692   70.534  0.46 28.20 ? 312 MET A SD  1 
ATOM   2006 C  CE  A MET A 1 284 ? 9.394   4.777   74.315  0.54 28.72 ? 312 MET A CE  1 
ATOM   2007 C  CE  B MET A 1 284 ? 9.096   8.185   71.154  0.46 25.65 ? 312 MET A CE  1 
ATOM   2008 N  N   . SER A 1 285 ? 4.904   6.741   71.453  1.00 22.56 ? 313 SER A N   1 
ATOM   2009 C  CA  . SER A 1 285 ? 4.514   7.949   70.757  1.00 21.28 ? 313 SER A CA  1 
ATOM   2010 C  C   . SER A 1 285 ? 5.590   9.010   70.990  1.00 25.01 ? 313 SER A C   1 
ATOM   2011 O  O   . SER A 1 285 ? 6.162   9.089   72.082  1.00 23.89 ? 313 SER A O   1 
ATOM   2012 C  CB  . SER A 1 285 ? 3.160   8.433   71.265  1.00 21.99 ? 313 SER A CB  1 
ATOM   2013 O  OG  . SER A 1 285 ? 2.855   9.748   70.822  1.00 24.36 ? 313 SER A OG  1 
ATOM   2014 N  N   . GLU A 1 286 ? 5.871   9.812   69.965  1.00 23.81 ? 314 GLU A N   1 
ATOM   2015 C  CA  . GLU A 1 286 ? 6.762   10.959  70.164  1.00 27.60 ? 314 GLU A CA  1 
ATOM   2016 C  C   . GLU A 1 286 ? 6.040   12.146  70.784  1.00 31.32 ? 314 GLU A C   1 
ATOM   2017 O  O   . GLU A 1 286 ? 6.676   13.167  71.069  1.00 30.43 ? 314 GLU A O   1 
ATOM   2018 C  CB  . GLU A 1 286 ? 7.393   11.386  68.840  1.00 26.22 ? 314 GLU A CB  1 
ATOM   2019 C  CG  . GLU A 1 286 ? 6.398   11.990  67.872  1.00 31.66 ? 314 GLU A CG  1 
ATOM   2020 C  CD  . GLU A 1 286 ? 7.064   12.843  66.808  1.00 38.77 ? 314 GLU A CD  1 
ATOM   2021 O  OE1 . GLU A 1 286 ? 8.302   12.775  66.666  1.00 46.31 ? 314 GLU A OE1 1 
ATOM   2022 O  OE2 . GLU A 1 286 ? 6.345   13.587  66.120  1.00 43.01 ? 314 GLU A OE2 1 
ATOM   2023 N  N   . ASP A 1 287 ? 4.730   12.038  70.990  1.00 26.33 ? 315 ASP A N   1 
ATOM   2024 C  CA  . ASP A 1 287 ? 3.958   13.107  71.619  1.00 28.52 ? 315 ASP A CA  1 
ATOM   2025 C  C   . ASP A 1 287 ? 2.644   12.479  72.062  1.00 26.34 ? 315 ASP A C   1 
ATOM   2026 O  O   . ASP A 1 287 ? 1.638   12.566  71.349  1.00 25.48 ? 315 ASP A O   1 
ATOM   2027 C  CB  . ASP A 1 287 ? 3.739   14.265  70.668  1.00 26.93 ? 315 ASP A CB  1 
ATOM   2028 C  CG  . ASP A 1 287 ? 2.897   15.372  71.264  1.00 31.47 ? 315 ASP A CG  1 
ATOM   2029 O  OD1 . ASP A 1 287 ? 2.345   15.238  72.386  1.00 27.71 ? 315 ASP A OD1 1 
ATOM   2030 O  OD2 . ASP A 1 287 ? 2.788   16.399  70.566  1.00 34.07 ? 315 ASP A OD2 1 
ATOM   2031 N  N   . ILE A 1 288 ? 2.653   11.878  73.252  1.00 27.80 ? 316 ILE A N   1 
ATOM   2032 C  CA  . ILE A 1 288 ? 1.507   11.084  73.672  1.00 25.83 ? 316 ILE A CA  1 
ATOM   2033 C  C   . ILE A 1 288 ? 0.269   11.956  73.831  1.00 29.55 ? 316 ILE A C   1 
ATOM   2034 O  O   . ILE A 1 288 ? -0.865  11.475  73.672  1.00 25.07 ? 316 ILE A O   1 
ATOM   2035 C  CB  . ILE A 1 288 ? 1.832   10.309  74.962  1.00 28.30 ? 316 ILE A CB  1 
ATOM   2036 C  CG1 . ILE A 1 288 ? 0.737   9.274   75.240  1.00 24.50 ? 316 ILE A CG1 1 
ATOM   2037 C  CG2 . ILE A 1 288 ? 2.020   11.270  76.143  1.00 28.41 ? 316 ILE A CG2 1 
ATOM   2038 C  CD1 . ILE A 1 288 ? 1.031   8.344   76.423  1.00 26.15 ? 316 ILE A CD1 1 
ATOM   2039 N  N   . PHE A 1 289 ? 0.455   13.240  74.149  1.00 29.82 ? 317 PHE A N   1 
ATOM   2040 C  CA  . PHE A 1 289 ? -0.680  14.146  74.264  1.00 28.91 ? 317 PHE A CA  1 
ATOM   2041 C  C   . PHE A 1 289 ? -1.396  14.284  72.930  1.00 24.92 ? 317 PHE A C   1 
ATOM   2042 O  O   . PHE A 1 289 ? -2.625  14.237  72.869  1.00 28.63 ? 317 PHE A O   1 
ATOM   2043 C  CB  . PHE A 1 289 ? -0.212  15.521  74.764  1.00 30.62 ? 317 PHE A CB  1 
ATOM   2044 C  CG  . PHE A 1 289 ? 0.188   15.543  76.218  1.00 36.24 ? 317 PHE A CG  1 
ATOM   2045 C  CD1 . PHE A 1 289 ? 0.835   16.655  76.759  1.00 41.43 ? 317 PHE A CD1 1 
ATOM   2046 C  CD2 . PHE A 1 289 ? -0.082  14.473  77.045  1.00 34.76 ? 317 PHE A CD2 1 
ATOM   2047 C  CE1 . PHE A 1 289 ? 1.197   16.682  78.100  1.00 36.53 ? 317 PHE A CE1 1 
ATOM   2048 C  CE2 . PHE A 1 289 ? 0.283   14.490  78.383  1.00 38.71 ? 317 PHE A CE2 1 
ATOM   2049 C  CZ  . PHE A 1 289 ? 0.925   15.591  78.911  1.00 38.63 ? 317 PHE A CZ  1 
ATOM   2050 N  N   . ARG A 1 290 ? -0.639  14.481  71.847  1.00 25.90 ? 318 ARG A N   1 
ATOM   2051 C  CA  . ARG A 1 290 ? -1.277  14.581  70.542  1.00 26.46 ? 318 ARG A CA  1 
ATOM   2052 C  C   . ARG A 1 290 ? -1.866  13.235  70.118  1.00 24.45 ? 318 ARG A C   1 
ATOM   2053 O  O   . ARG A 1 290 ? -2.995  13.179  69.619  1.00 23.65 ? 318 ARG A O   1 
ATOM   2054 C  CB  . ARG A 1 290 ? -0.283  15.098  69.499  1.00 30.36 ? 318 ARG A CB  1 
ATOM   2055 C  CG  . ARG A 1 290 ? -0.692  14.730  68.083  1.00 35.71 ? 318 ARG A CG  1 
ATOM   2056 C  CD  . ARG A 1 290 ? -0.023  15.534  66.976  1.00 42.16 ? 318 ARG A CD  1 
ATOM   2057 N  NE  A ARG A 1 290 ? 0.282   14.726  65.796  0.55 38.40 ? 318 ARG A NE  1 
ATOM   2058 N  NE  B ARG A 1 290 ? -0.411  14.965  65.676  0.45 40.50 ? 318 ARG A NE  1 
ATOM   2059 C  CZ  A ARG A 1 290 ? 1.454   14.149  65.593  0.55 35.20 ? 318 ARG A CZ  1 
ATOM   2060 C  CZ  B ARG A 1 290 ? -1.520  15.283  65.007  0.45 36.64 ? 318 ARG A CZ  1 
ATOM   2061 N  NH1 A ARG A 1 290 ? 2.415   14.291  66.493  0.55 37.99 ? 318 ARG A NH1 1 
ATOM   2062 N  NH1 B ARG A 1 290 ? -2.362  16.195  65.484  0.45 39.10 ? 318 ARG A NH1 1 
ATOM   2063 N  NH2 A ARG A 1 290 ? 1.672   13.443  64.497  0.55 35.64 ? 318 ARG A NH2 1 
ATOM   2064 N  NH2 B ARG A 1 290 ? -1.779  14.702  63.844  0.45 36.03 ? 318 ARG A NH2 1 
ATOM   2065 N  N   . THR A 1 291 ? -1.138  12.137  70.337  1.00 25.27 ? 319 THR A N   1 
ATOM   2066 C  CA  . THR A 1 291 ? -1.690  10.815  69.996  1.00 24.53 ? 319 THR A CA  1 
ATOM   2067 C  C   . THR A 1 291 ? -3.035  10.577  70.673  1.00 25.75 ? 319 THR A C   1 
ATOM   2068 O  O   . THR A 1 291 ? -4.009  10.150  70.037  1.00 23.07 ? 319 THR A O   1 
ATOM   2069 C  CB  . THR A 1 291 ? -0.703  9.713   70.386  1.00 23.33 ? 319 THR A CB  1 
ATOM   2070 O  OG1 . THR A 1 291 ? 0.541   9.946   69.736  1.00 23.49 ? 319 THR A OG1 1 
ATOM   2071 C  CG2 . THR A 1 291 ? -1.256  8.316   69.939  1.00 19.72 ? 319 THR A CG2 1 
ATOM   2072 N  N   . LEU A 1 292 ? -3.115  10.840  71.974  1.00 24.73 ? 320 LEU A N   1 
ATOM   2073 C  CA  . LEU A 1 292 ? -4.350  10.536  72.673  1.00 22.85 ? 320 LEU A CA  1 
ATOM   2074 C  C   . LEU A 1 292 ? -5.463  11.501  72.295  1.00 26.39 ? 320 LEU A C   1 
ATOM   2075 O  O   . LEU A 1 292 ? -6.628  11.097  72.246  1.00 22.72 ? 320 LEU A O   1 
ATOM   2076 C  CB  . LEU A 1 292 ? -4.115  10.540  74.178  1.00 27.53 ? 320 LEU A CB  1 
ATOM   2077 C  CG  . LEU A 1 292 ? -3.952  9.163   74.804  1.00 32.52 ? 320 LEU A CG  1 
ATOM   2078 C  CD1 . LEU A 1 292 ? -5.327  8.494   74.845  1.00 33.40 ? 320 LEU A CD1 1 
ATOM   2079 C  CD2 . LEU A 1 292 ? -2.984  8.349   73.975  1.00 28.29 ? 320 LEU A CD2 1 
ATOM   2080 N  N   . ARG A 1 293 ? -5.138  12.767  72.008  1.00 25.54 ? 321 ARG A N   1 
ATOM   2081 C  CA  . ARG A 1 293 ? -6.188  13.658  71.533  1.00 25.98 ? 321 ARG A CA  1 
ATOM   2082 C  C   . ARG A 1 293 ? -6.759  13.152  70.212  1.00 25.16 ? 321 ARG A C   1 
ATOM   2083 O  O   . ARG A 1 293 ? -7.983  13.105  70.035  1.00 25.27 ? 321 ARG A O   1 
ATOM   2084 C  CB  . ARG A 1 293 ? -5.667  15.093  71.413  1.00 32.42 ? 321 ARG A CB  1 
ATOM   2085 C  CG  . ARG A 1 293 ? -5.462  15.756  72.780  1.00 36.20 ? 321 ARG A CG  1 
ATOM   2086 C  CD  . ARG A 1 293 ? -5.148  17.245  72.672  1.00 40.94 ? 321 ARG A CD  1 
ATOM   2087 N  NE  . ARG A 1 293 ? -3.913  17.606  73.373  1.00 49.04 ? 321 ARG A NE  1 
ATOM   2088 C  CZ  . ARG A 1 293 ? -2.753  17.842  72.765  1.00 44.19 ? 321 ARG A CZ  1 
ATOM   2089 N  NH1 . ARG A 1 293 ? -2.670  17.750  71.444  1.00 44.50 ? 321 ARG A NH1 1 
ATOM   2090 N  NH2 . ARG A 1 293 ? -1.679  18.180  73.468  1.00 49.58 ? 321 ARG A NH2 1 
ATOM   2091 N  N   . GLU A 1 294 ? -5.889  12.716  69.295  1.00 23.98 ? 322 GLU A N   1 
ATOM   2092 C  CA  . GLU A 1 294 ? -6.358  12.246  67.997  1.00 22.91 ? 322 GLU A CA  1 
ATOM   2093 C  C   . GLU A 1 294 ? -7.109  10.924  68.126  1.00 20.42 ? 322 GLU A C   1 
ATOM   2094 O  O   . GLU A 1 294 ? -8.178  10.763  67.541  1.00 22.17 ? 322 GLU A O   1 
ATOM   2095 C  CB  . GLU A 1 294 ? -5.193  12.109  67.020  1.00 23.47 ? 322 GLU A CB  1 
ATOM   2096 C  CG  . GLU A 1 294 ? -4.473  13.443  66.733  1.00 28.85 ? 322 GLU A CG  1 
ATOM   2097 C  CD  . GLU A 1 294 ? -5.424  14.522  66.223  1.00 36.27 ? 322 GLU A CD  1 
ATOM   2098 O  OE1 . GLU A 1 294 ? -5.126  15.714  66.444  1.00 40.58 ? 322 GLU A OE1 1 
ATOM   2099 O  OE2 . GLU A 1 294 ? -6.455  14.205  65.603  1.00 35.41 ? 322 GLU A OE2 1 
ATOM   2100 N  N   . MET A 1 295 ? -6.576  9.982   68.903  1.00 21.11 ? 323 MET A N   1 
ATOM   2101 C  CA  . MET A 1 295 ? -7.277  8.705   69.051  1.00 24.94 ? 323 MET A CA  1 
ATOM   2102 C  C   . MET A 1 295 ? -8.618  8.891   69.752  1.00 26.45 ? 323 MET A C   1 
ATOM   2103 O  O   . MET A 1 295 ? -9.618  8.258   69.376  1.00 21.61 ? 323 MET A O   1 
ATOM   2104 C  CB  . MET A 1 295 ? -6.399  7.705   69.806  1.00 22.11 ? 323 MET A CB  1 
ATOM   2105 C  CG  . MET A 1 295 ? -5.153  7.301   69.049  1.00 25.00 ? 323 MET A CG  1 
ATOM   2106 S  SD  . MET A 1 295 ? -4.279  5.922   69.833  1.00 20.09 ? 323 MET A SD  1 
ATOM   2107 C  CE  . MET A 1 295 ? -5.454  4.582   69.569  1.00 18.85 ? 323 MET A CE  1 
ATOM   2108 N  N   . ARG A 1 296 ? -8.670  9.756   70.772  1.00 25.82 ? 324 ARG A N   1 
ATOM   2109 C  CA  . ARG A 1 296 ? -9.920  9.922   71.505  1.00 26.65 ? 324 ARG A CA  1 
ATOM   2110 C  C   . ARG A 1 296 ? -10.990 10.609  70.668  1.00 25.95 ? 324 ARG A C   1 
ATOM   2111 O  O   . ARG A 1 296 ? -12.177 10.288  70.809  1.00 24.97 ? 324 ARG A O   1 
ATOM   2112 C  CB  . ARG A 1 296 ? -9.691  10.693  72.797  1.00 31.46 ? 324 ARG A CB  1 
ATOM   2113 C  CG  . ARG A 1 296 ? -9.221  9.837   73.943  1.00 33.59 ? 324 ARG A CG  1 
ATOM   2114 C  CD  . ARG A 1 296 ? -9.286  10.639  75.234  1.00 37.17 ? 324 ARG A CD  1 
ATOM   2115 N  NE  . ARG A 1 296 ? -8.846  9.882   76.401  1.00 40.26 ? 324 ARG A NE  1 
ATOM   2116 C  CZ  . ARG A 1 296 ? -9.568  8.940   76.994  1.00 35.20 ? 324 ARG A CZ  1 
ATOM   2117 N  NH1 . ARG A 1 296 ? -10.759 8.607   76.517  1.00 36.38 ? 324 ARG A NH1 1 
ATOM   2118 N  NH2 . ARG A 1 296 ? -9.095  8.323   78.062  1.00 37.65 ? 324 ARG A NH2 1 
ATOM   2119 N  N   . LYS A 1 297 ? -10.600 11.524  69.775  1.00 25.84 ? 325 LYS A N   1 
ATOM   2120 C  CA  . LYS A 1 297 ? -11.582 12.127  68.874  1.00 24.71 ? 325 LYS A CA  1 
ATOM   2121 C  C   . LYS A 1 297 ? -12.245 11.082  67.992  1.00 23.37 ? 325 LYS A C   1 
ATOM   2122 O  O   . LYS A 1 297 ? -13.389 11.265  67.557  1.00 24.11 ? 325 LYS A O   1 
ATOM   2123 C  CB  . LYS A 1 297 ? -10.914 13.187  67.997  1.00 30.24 ? 325 LYS A CB  1 
ATOM   2124 C  CG  . LYS A 1 297 ? -10.437 14.398  68.753  1.00 38.13 ? 325 LYS A CG  1 
ATOM   2125 C  CD  . LYS A 1 297 ? -10.321 15.606  67.850  1.00 41.78 ? 325 LYS A CD  1 
ATOM   2126 C  CE  . LYS A 1 297 ? -9.030  15.572  67.084  1.00 42.63 ? 325 LYS A CE  1 
ATOM   2127 N  NZ  . LYS A 1 297 ? -8.573  16.938  66.755  1.00 46.20 ? 325 LYS A NZ  1 
ATOM   2128 N  N   . ARG A 1 298 ? -11.562 9.967   67.746  1.00 25.53 ? 326 ARG A N   1 
ATOM   2129 C  CA  . ARG A 1 298 ? -12.048 8.968   66.808  1.00 23.77 ? 326 ARG A CA  1 
ATOM   2130 C  C   . ARG A 1 298 ? -12.647 7.739   67.478  1.00 20.24 ? 326 ARG A C   1 
ATOM   2131 O  O   . ARG A 1 298 ? -13.161 6.866   66.768  1.00 21.60 ? 326 ARG A O   1 
ATOM   2132 C  CB  . ARG A 1 298 ? -10.910 8.569   65.857  1.00 23.68 ? 326 ARG A CB  1 
ATOM   2133 C  CG  . ARG A 1 298 ? -10.364 9.802   65.130  1.00 24.69 ? 326 ARG A CG  1 
ATOM   2134 C  CD  . ARG A 1 298 ? -9.115  9.515   64.321  1.00 22.54 ? 326 ARG A CD  1 
ATOM   2135 N  NE  . ARG A 1 298 ? -8.764  10.585  63.380  1.00 27.40 ? 326 ARG A NE  1 
ATOM   2136 C  CZ  . ARG A 1 298 ? -8.202  11.748  63.701  1.00 25.28 ? 326 ARG A CZ  1 
ATOM   2137 N  NH1 . ARG A 1 298 ? -7.943  12.061  64.966  1.00 25.97 ? 326 ARG A NH1 1 
ATOM   2138 N  NH2 . ARG A 1 298 ? -7.926  12.624  62.745  1.00 27.84 ? 326 ARG A NH2 1 
ATOM   2139 N  N   . SER A 1 299 ? -12.668 7.679   68.814  1.00 21.78 ? 327 SER A N   1 
ATOM   2140 C  CA  . SER A 1 299 ? -13.145 6.477   69.500  1.00 20.14 ? 327 SER A CA  1 
ATOM   2141 C  C   . SER A 1 299 ? -14.531 6.055   69.029  1.00 25.28 ? 327 SER A C   1 
ATOM   2142 O  O   . SER A 1 299 ? -14.776 4.870   68.769  1.00 26.69 ? 327 SER A O   1 
ATOM   2143 C  CB  . SER A 1 299 ? -13.157 6.698   71.011  1.00 25.40 ? 327 SER A CB  1 
ATOM   2144 O  OG  . SER A 1 299 ? -11.842 6.799   71.522  1.00 22.39 ? 327 SER A OG  1 
ATOM   2145 N  N   . SER A 1 300 ? -15.450 7.010   68.918  1.00 24.12 ? 328 SER A N   1 
ATOM   2146 C  CA  . SER A 1 300 ? -16.842 6.718   68.609  1.00 29.14 ? 328 SER A CA  1 
ATOM   2147 C  C   . SER A 1 300 ? -17.161 6.800   67.121  1.00 23.54 ? 328 SER A C   1 
ATOM   2148 O  O   . SER A 1 300 ? -18.331 6.629   66.739  1.00 25.09 ? 328 SER A O   1 
ATOM   2149 C  CB  . SER A 1 300 ? -17.744 7.664   69.402  1.00 39.18 ? 328 SER A CB  1 
ATOM   2150 O  OG  . SER A 1 300 ? -17.622 7.370   70.787  1.00 45.65 ? 328 SER A OG  1 
ATOM   2151 N  N   . ILE A 1 301 ? -16.156 7.027   66.278  1.00 21.30 ? 329 ILE A N   1 
ATOM   2152 C  CA  . ILE A 1 301 ? -16.362 7.072   64.835  1.00 19.47 ? 329 ILE A CA  1 
ATOM   2153 C  C   . ILE A 1 301 ? -15.403 6.126   64.124  1.00 18.15 ? 329 ILE A C   1 
ATOM   2154 O  O   . ILE A 1 301 ? -14.810 6.472   63.095  1.00 16.74 ? 329 ILE A O   1 
ATOM   2155 C  CB  . ILE A 1 301 ? -16.241 8.508   64.298  1.00 19.94 ? 329 ILE A CB  1 
ATOM   2156 C  CG1 . ILE A 1 301 ? -14.884 9.124   64.669  1.00 21.63 ? 329 ILE A CG1 1 
ATOM   2157 C  CG2 . ILE A 1 301 ? -17.427 9.357   64.806  1.00 22.76 ? 329 ILE A CG2 1 
ATOM   2158 C  CD1 . ILE A 1 301 ? -14.624 10.502  63.995  1.00 22.93 ? 329 ILE A CD1 1 
ATOM   2159 N  N   . GLY A 1 302 ? -15.303 4.898   64.626  1.00 20.29 ? 330 GLY A N   1 
ATOM   2160 C  CA  . GLY A 1 302 ? -14.559 3.844   63.960  1.00 18.14 ? 330 GLY A CA  1 
ATOM   2161 C  C   . GLY A 1 302 ? -13.237 3.493   64.612  1.00 18.74 ? 330 GLY A C   1 
ATOM   2162 O  O   . GLY A 1 302 ? -12.623 2.483   64.226  1.00 18.60 ? 330 GLY A O   1 
ATOM   2163 N  N   . GLY A 1 303 ? -12.775 4.282   65.579  1.00 17.87 ? 331 GLY A N   1 
ATOM   2164 C  CA  . GLY A 1 303 ? -11.452 4.116   66.165  1.00 16.47 ? 331 GLY A CA  1 
ATOM   2165 C  C   . GLY A 1 303 ? -11.468 3.188   67.360  1.00 22.19 ? 331 GLY A C   1 
ATOM   2166 O  O   . GLY A 1 303 ? -12.258 2.238   67.429  1.00 20.70 ? 331 GLY A O   1 
ATOM   2167 N  N   . PHE A 1 304 ? -10.584 3.452   68.319  1.00 17.88 ? 332 PHE A N   1 
ATOM   2168 C  CA  . PHE A 1 304 ? -10.436 2.594   69.486  1.00 20.59 ? 332 PHE A CA  1 
ATOM   2169 C  C   . PHE A 1 304 ? -10.968 3.285   70.735  1.00 20.75 ? 332 PHE A C   1 
ATOM   2170 O  O   . PHE A 1 304 ? -10.808 4.494   70.900  1.00 24.12 ? 332 PHE A O   1 
ATOM   2171 C  CB  . PHE A 1 304 ? -8.962  2.198   69.675  1.00 16.70 ? 332 PHE A CB  1 
ATOM   2172 C  CG  . PHE A 1 304 ? -8.446  1.331   68.555  1.00 17.06 ? 332 PHE A CG  1 
ATOM   2173 C  CD1 . PHE A 1 304 ? -8.704  -0.039  68.550  1.00 20.83 ? 332 PHE A CD1 1 
ATOM   2174 C  CD2 . PHE A 1 304 ? -7.794  1.891   67.475  1.00 18.33 ? 332 PHE A CD2 1 
ATOM   2175 C  CE1 . PHE A 1 304 ? -8.255  -0.838  67.508  1.00 20.37 ? 332 PHE A CE1 1 
ATOM   2176 C  CE2 . PHE A 1 304 ? -7.332  1.098   66.422  1.00 16.32 ? 332 PHE A CE2 1 
ATOM   2177 C  CZ  . PHE A 1 304 ? -7.577  -0.268  66.434  1.00 15.31 ? 332 PHE A CZ  1 
ATOM   2178 N  N   . ASP A 1 305 ? -11.558 2.506   71.629  1.00 21.83 ? 333 ASP A N   1 
ATOM   2179 C  CA  . ASP A 1 305 ? -12.004 3.015   72.918  1.00 24.27 ? 333 ASP A CA  1 
ATOM   2180 C  C   . ASP A 1 305 ? -10.896 2.843   73.936  1.00 26.62 ? 333 ASP A C   1 
ATOM   2181 O  O   . ASP A 1 305 ? -10.074 1.937   73.825  1.00 25.93 ? 333 ASP A O   1 
ATOM   2182 C  CB  . ASP A 1 305 ? -13.237 2.267   73.411  1.00 23.70 ? 333 ASP A CB  1 
ATOM   2183 C  CG  . ASP A 1 305 ? -14.427 2.430   72.484  1.00 24.22 ? 333 ASP A CG  1 
ATOM   2184 O  OD1 . ASP A 1 305 ? -14.460 3.398   71.707  1.00 30.53 ? 333 ASP A OD1 1 
ATOM   2185 O  OD2 . ASP A 1 305 ? -15.300 1.560   72.507  1.00 33.35 ? 333 ASP A OD2 1 
ATOM   2186 N  N   . PHE A 1 306 ? -10.904 3.694   74.955  1.00 24.37 ? 334 PHE A N   1 
ATOM   2187 C  CA  . PHE A 1 306 ? -9.911  3.621   76.015  1.00 24.82 ? 334 PHE A CA  1 
ATOM   2188 C  C   . PHE A 1 306 ? -10.560 3.124   77.300  1.00 27.41 ? 334 PHE A C   1 
ATOM   2189 O  O   . PHE A 1 306 ? -11.776 3.241   77.490  1.00 27.17 ? 334 PHE A O   1 
ATOM   2190 C  CB  . PHE A 1 306 ? -9.237  4.981   76.202  1.00 26.99 ? 334 PHE A CB  1 
ATOM   2191 C  CG  . PHE A 1 306 ? -8.286  5.305   75.096  1.00 23.95 ? 334 PHE A CG  1 
ATOM   2192 C  CD1 . PHE A 1 306 ? -6.992  4.815   75.130  1.00 22.02 ? 334 PHE A CD1 1 
ATOM   2193 C  CD2 . PHE A 1 306 ? -8.707  6.021   73.983  1.00 24.35 ? 334 PHE A CD2 1 
ATOM   2194 C  CE1 . PHE A 1 306 ? -6.116  5.071   74.102  1.00 24.95 ? 334 PHE A CE1 1 
ATOM   2195 C  CE2 . PHE A 1 306 ? -7.831  6.295   72.946  1.00 28.33 ? 334 PHE A CE2 1 
ATOM   2196 C  CZ  . PHE A 1 306 ? -6.525  5.813   73.006  1.00 22.30 ? 334 PHE A CZ  1 
ATOM   2197 N  N   . MET A 1 307 ? -9.745  2.505   78.145  1.00 25.81 ? 335 MET A N   1 
ATOM   2198 C  CA  . MET A 1 307 ? -10.194 2.088   79.460  1.00 29.38 ? 335 MET A CA  1 
ATOM   2199 C  C   . MET A 1 307 ? -10.742 3.287   80.238  1.00 32.47 ? 335 MET A C   1 
ATOM   2200 O  O   . MET A 1 307 ? -10.391 4.435   79.952  1.00 33.19 ? 335 MET A O   1 
ATOM   2201 C  CB  . MET A 1 307 ? -9.039  1.441   80.224  1.00 31.52 ? 335 MET A CB  1 
ATOM   2202 C  CG  . MET A 1 307 ? -8.638  0.089   79.669  1.00 30.24 ? 335 MET A CG  1 
ATOM   2203 S  SD  . MET A 1 307 ? -9.982  -1.114  79.819  1.00 36.37 ? 335 MET A SD  1 
ATOM   2204 C  CE  . MET A 1 307 ? -9.852  -1.549  81.556  1.00 35.36 ? 335 MET A CE  1 
ATOM   2205 N  N   . PRO A 1 308 ? -11.629 3.052   81.204  1.00 39.66 ? 336 PRO A N   1 
ATOM   2206 C  CA  . PRO A 1 308 ? -12.182 4.170   81.980  1.00 38.41 ? 336 PRO A CA  1 
ATOM   2207 C  C   . PRO A 1 308 ? -11.090 4.942   82.710  1.00 42.04 ? 336 PRO A C   1 
ATOM   2208 O  O   . PRO A 1 308 ? -10.154 4.362   83.264  1.00 41.38 ? 336 PRO A O   1 
ATOM   2209 C  CB  . PRO A 1 308 ? -13.148 3.490   82.959  1.00 41.04 ? 336 PRO A CB  1 
ATOM   2210 C  CG  . PRO A 1 308 ? -12.935 2.023   82.810  1.00 42.90 ? 336 PRO A CG  1 
ATOM   2211 C  CD  . PRO A 1 308 ? -12.321 1.784   81.473  1.00 36.68 ? 336 PRO A CD  1 
ATOM   2212 N  N   . SER A 1 309 ? -11.220 6.264   82.692  1.00 39.68 ? 337 SER A N   1 
ATOM   2213 C  CA  . SER A 1 309 ? -10.181 7.129   83.216  1.00 41.20 ? 337 SER A CA  1 
ATOM   2214 C  C   . SER A 1 309 ? -10.136 7.054   84.741  1.00 42.29 ? 337 SER A C   1 
ATOM   2215 O  O   . SER A 1 309 ? -11.143 6.758   85.385  1.00 42.83 ? 337 SER A O   1 
ATOM   2216 C  CB  . SER A 1 309 ? -10.424 8.564   82.768  1.00 44.53 ? 337 SER A CB  1 
ATOM   2217 O  OG  . SER A 1 309 ? -10.442 8.642   81.355  1.00 41.56 ? 337 SER A OG  1 
ATOM   2218 N  N   . PRO A 1 310 ? -8.974  7.300   85.340  1.00 45.80 ? 338 PRO A N   1 
ATOM   2219 C  CA  . PRO A 1 310 ? -8.870  7.270   86.801  1.00 50.04 ? 338 PRO A CA  1 
ATOM   2220 C  C   . PRO A 1 310 ? -9.600  8.451   87.408  1.00 45.76 ? 338 PRO A C   1 
ATOM   2221 O  O   . PRO A 1 310 ? -9.807  9.471   86.734  1.00 50.74 ? 338 PRO A O   1 
ATOM   2222 C  CB  . PRO A 1 310 ? -7.357  7.361   87.056  1.00 45.01 ? 338 PRO A CB  1 
ATOM   2223 C  CG  . PRO A 1 310 ? -6.720  7.097   85.744  1.00 48.02 ? 338 PRO A CG  1 
ATOM   2224 C  CD  . PRO A 1 310 ? -7.678  7.569   84.708  1.00 43.17 ? 338 PRO A CD  1 
ATOM   2225 N  N   . PRO A 1 311 ? -9.999  8.361   88.672  1.00 52.52 ? 339 PRO A N   1 
ATOM   2226 C  CA  . PRO A 1 311 ? -10.736 9.462   89.293  1.00 52.19 ? 339 PRO A CA  1 
ATOM   2227 C  C   . PRO A 1 311 ? -9.858  10.691  89.445  1.00 53.06 ? 339 PRO A C   1 
ATOM   2228 O  O   . PRO A 1 311 ? -8.635  10.626  89.235  1.00 50.82 ? 339 PRO A O   1 
ATOM   2229 C  CB  . PRO A 1 311 ? -11.149 8.886   90.657  1.00 52.83 ? 339 PRO A CB  1 
ATOM   2230 C  CG  . PRO A 1 311 ? -10.174 7.807   90.933  1.00 55.92 ? 339 PRO A CG  1 
ATOM   2231 C  CD  . PRO A 1 311 ? -9.829  7.221   89.590  1.00 53.96 ? 339 PRO A CD  1 
ATOM   2232 N  N   . PRO A 1 312 ? -10.446 11.840  89.784  1.00 50.70 ? 340 PRO A N   1 
ATOM   2233 C  CA  . PRO A 1 312 ? -9.625  13.044  89.986  1.00 51.49 ? 340 PRO A CA  1 
ATOM   2234 C  C   . PRO A 1 312 ? -8.589  12.886  91.081  1.00 49.69 ? 340 PRO A C   1 
ATOM   2235 O  O   . PRO A 1 312 ? -7.547  13.551  91.031  1.00 53.74 ? 340 PRO A O   1 
ATOM   2236 C  CB  . PRO A 1 312 ? -10.665 14.122  90.333  1.00 53.10 ? 340 PRO A CB  1 
ATOM   2237 C  CG  . PRO A 1 312 ? -11.880 13.362  90.765  1.00 59.60 ? 340 PRO A CG  1 
ATOM   2238 C  CD  . PRO A 1 312 ? -11.882 12.120  89.942  1.00 57.67 ? 340 PRO A CD  1 
ATOM   2239 N  N   . THR A 1 313 ? -8.833  12.007  92.058  1.00 51.93 ? 341 THR A N   1 
ATOM   2240 C  CA  . THR A 1 313 ? -7.859  11.783  93.122  1.00 54.76 ? 341 THR A CA  1 
ATOM   2241 C  C   . THR A 1 313 ? -6.529  11.291  92.567  1.00 53.52 ? 341 THR A C   1 
ATOM   2242 O  O   . THR A 1 313 ? -5.465  11.705  93.040  1.00 54.94 ? 341 THR A O   1 
ATOM   2243 C  CB  . THR A 1 313 ? -8.401  10.783  94.148  1.00 54.54 ? 341 THR A CB  1 
ATOM   2244 O  OG1 . THR A 1 313 ? -9.046  9.697   93.476  1.00 52.56 ? 341 THR A OG1 1 
ATOM   2245 C  CG2 . THR A 1 313 ? -9.395  11.458  95.084  1.00 63.49 ? 341 THR A CG2 1 
ATOM   2246 N  N   . TYR A 1 314 ? -6.567  10.394  91.577  1.00 52.29 ? 342 TYR A N   1 
ATOM   2247 C  CA  . TYR A 1 314 ? -5.328  9.915   90.970  1.00 52.04 ? 342 TYR A CA  1 
ATOM   2248 C  C   . TYR A 1 314 ? -4.477  11.077  90.485  1.00 48.69 ? 342 TYR A C   1 
ATOM   2249 O  O   . TYR A 1 314 ? -3.248  11.055  90.611  1.00 44.77 ? 342 TYR A O   1 
ATOM   2250 C  CB  . TYR A 1 314 ? -5.635  8.969   89.804  1.00 50.69 ? 342 TYR A CB  1 
ATOM   2251 C  CG  . TYR A 1 314 ? -4.402  8.449   89.087  1.00 46.04 ? 342 TYR A CG  1 
ATOM   2252 C  CD1 . TYR A 1 314 ? -3.753  7.297   89.519  1.00 48.03 ? 342 TYR A CD1 1 
ATOM   2253 C  CD2 . TYR A 1 314 ? -3.883  9.116   87.983  1.00 45.61 ? 342 TYR A CD2 1 
ATOM   2254 C  CE1 . TYR A 1 314 ? -2.629  6.822   88.872  1.00 40.83 ? 342 TYR A CE1 1 
ATOM   2255 C  CE2 . TYR A 1 314 ? -2.751  8.649   87.329  1.00 42.15 ? 342 TYR A CE2 1 
ATOM   2256 C  CZ  . TYR A 1 314 ? -2.131  7.503   87.780  1.00 42.73 ? 342 TYR A CZ  1 
ATOM   2257 O  OH  . TYR A 1 314 ? -1.008  7.020   87.140  1.00 36.42 ? 342 TYR A OH  1 
ATOM   2258 N  N   . TYR A 1 315 ? -5.117  12.111  89.938  1.00 44.01 ? 343 TYR A N   1 
ATOM   2259 C  CA  . TYR A 1 315 ? -4.370  13.221  89.365  1.00 51.96 ? 343 TYR A CA  1 
ATOM   2260 C  C   . TYR A 1 315 ? -3.955  14.240  90.416  1.00 52.41 ? 343 TYR A C   1 
ATOM   2261 O  O   . TYR A 1 315 ? -2.914  14.885  90.258  1.00 49.82 ? 343 TYR A O   1 
ATOM   2262 C  CB  . TYR A 1 315 ? -5.184  13.854  88.233  1.00 50.27 ? 343 TYR A CB  1 
ATOM   2263 C  CG  . TYR A 1 315 ? -5.237  12.904  87.064  1.00 47.10 ? 343 TYR A CG  1 
ATOM   2264 C  CD1 . TYR A 1 315 ? -6.354  12.116  86.828  1.00 47.56 ? 343 TYR A CD1 1 
ATOM   2265 C  CD2 . TYR A 1 315 ? -4.126  12.729  86.247  1.00 47.36 ? 343 TYR A CD2 1 
ATOM   2266 C  CE1 . TYR A 1 315 ? -6.377  11.212  85.777  1.00 46.33 ? 343 TYR A CE1 1 
ATOM   2267 C  CE2 . TYR A 1 315 ? -4.134  11.827  85.202  1.00 41.72 ? 343 TYR A CE2 1 
ATOM   2268 C  CZ  . TYR A 1 315 ? -5.260  11.072  84.970  1.00 41.98 ? 343 TYR A CZ  1 
ATOM   2269 O  OH  . TYR A 1 315 ? -5.273  10.172  83.929  1.00 39.99 ? 343 TYR A OH  1 
ATOM   2270 N  N   . GLN A 1 316 ? -4.727  14.385  91.495  1.00 53.37 ? 344 GLN A N   1 
ATOM   2271 C  CA  . GLN A 1 316 ? -4.236  15.152  92.635  1.00 53.66 ? 344 GLN A CA  1 
ATOM   2272 C  C   . GLN A 1 316 ? -2.976  14.512  93.204  1.00 53.39 ? 344 GLN A C   1 
ATOM   2273 O  O   . GLN A 1 316 ? -1.991  15.203  93.488  1.00 56.37 ? 344 GLN A O   1 
ATOM   2274 C  CB  . GLN A 1 316 ? -5.322  15.267  93.708  1.00 55.10 ? 344 GLN A CB  1 
ATOM   2275 N  N   . ASN A 1 317 ? -2.972  13.183  93.337  1.00 55.31 ? 345 ASN A N   1 
ATOM   2276 C  CA  . ASN A 1 317 ? -1.808  12.469  93.852  1.00 55.43 ? 345 ASN A CA  1 
ATOM   2277 C  C   . ASN A 1 317 ? -0.612  12.516  92.909  1.00 52.18 ? 345 ASN A C   1 
ATOM   2278 O  O   . ASN A 1 317 ? 0.501   12.195  93.337  1.00 53.58 ? 345 ASN A O   1 
ATOM   2279 C  CB  . ASN A 1 317 ? -2.176  11.012  94.144  1.00 57.27 ? 345 ASN A CB  1 
ATOM   2280 C  CG  . ASN A 1 317 ? -3.321  10.885  95.131  1.00 56.41 ? 345 ASN A CG  1 
ATOM   2281 O  OD1 . ASN A 1 317 ? -3.656  11.838  95.836  1.00 56.85 ? 345 ASN A OD1 1 
ATOM   2282 N  ND2 . ASN A 1 317 ? -3.915  9.699   95.201  1.00 54.59 ? 345 ASN A ND2 1 
ATOM   2283 N  N   . LEU A 1 318 ? -0.807  12.910  91.649  1.00 51.37 ? 346 LEU A N   1 
ATOM   2284 C  CA  . LEU A 1 318 ? 0.305   12.951  90.704  1.00 54.71 ? 346 LEU A CA  1 
ATOM   2285 C  C   . LEU A 1 318 ? 1.304   14.043  91.056  1.00 56.30 ? 346 LEU A C   1 
ATOM   2286 O  O   . LEU A 1 318 ? 2.516   13.858  90.886  1.00 54.71 ? 346 LEU A O   1 
ATOM   2287 C  CB  . LEU A 1 318 ? -0.212  13.171  89.288  1.00 52.49 ? 346 LEU A CB  1 
ATOM   2288 C  CG  . LEU A 1 318 ? -0.505  11.919  88.480  1.00 54.97 ? 346 LEU A CG  1 
ATOM   2289 C  CD1 . LEU A 1 318 ? -0.911  12.325  87.079  1.00 53.27 ? 346 LEU A CD1 1 
ATOM   2290 C  CD2 . LEU A 1 318 ? 0.706   10.995  88.464  1.00 47.61 ? 346 LEU A CD2 1 
ATOM   2291 N  N   . LYS A 1 319 ? 0.809   15.200  91.507  1.00 55.18 ? 347 LYS A N   1 
ATOM   2292 C  CA  . LYS A 1 319 ? 1.697   16.303  91.863  1.00 58.84 ? 347 LYS A CA  1 
ATOM   2293 C  C   . LYS A 1 319 ? 2.783   15.843  92.826  1.00 57.07 ? 347 LYS A C   1 
ATOM   2294 O  O   . LYS A 1 319 ? 3.968   16.135  92.622  1.00 55.06 ? 347 LYS A O   1 
ATOM   2295 C  CB  . LYS A 1 319 ? 0.890   17.445  92.476  1.00 56.08 ? 347 LYS A CB  1 
ATOM   2296 C  CG  . LYS A 1 319 ? 1.309   18.835  92.018  1.00 61.71 ? 347 LYS A CG  1 
ATOM   2297 C  CD  . LYS A 1 319 ? 0.114   19.775  92.052  1.00 61.54 ? 347 LYS A CD  1 
ATOM   2298 C  CE  . LYS A 1 319 ? 0.543   21.193  92.404  1.00 60.80 ? 347 LYS A CE  1 
ATOM   2299 N  NZ  . LYS A 1 319 ? -0.570  22.160  92.217  1.00 56.14 ? 347 LYS A NZ  1 
ATOM   2300 N  N   . LYS A 1 320 ? 2.401   15.096  93.866  1.00 55.29 ? 348 LYS A N   1 
ATOM   2301 C  CA  . LYS A 1 320 ? 3.348   14.612  94.863  1.00 57.93 ? 348 LYS A CA  1 
ATOM   2302 C  C   . LYS A 1 320 ? 4.235   13.494  94.343  1.00 57.72 ? 348 LYS A C   1 
ATOM   2303 O  O   . LYS A 1 320 ? 5.161   13.091  95.052  1.00 54.54 ? 348 LYS A O   1 
ATOM   2304 C  CB  . LYS A 1 320 ? 2.600   14.128  96.107  1.00 58.13 ? 348 LYS A CB  1 
ATOM   2305 N  N   . ARG A 1 321 ? 3.978   12.980  93.143  1.00 53.93 ? 349 ARG A N   1 
ATOM   2306 C  CA  . ARG A 1 321 ? 4.777   11.897  92.582  1.00 55.56 ? 349 ARG A CA  1 
ATOM   2307 C  C   . ARG A 1 321 ? 5.677   12.328  91.436  1.00 53.67 ? 349 ARG A C   1 
ATOM   2308 O  O   . ARG A 1 321 ? 6.814   11.860  91.349  1.00 51.50 ? 349 ARG A O   1 
ATOM   2309 C  CB  . ARG A 1 321 ? 3.867   10.759  92.106  1.00 53.98 ? 349 ARG A CB  1 
ATOM   2310 C  CG  . ARG A 1 321 ? 3.360   9.883   93.229  1.00 51.06 ? 349 ARG A CG  1 
ATOM   2311 C  CD  . ARG A 1 321 ? 2.047   9.227   92.865  1.00 59.10 ? 349 ARG A CD  1 
ATOM   2312 N  NE  . ARG A 1 321 ? 2.157   8.376   91.683  1.00 57.32 ? 349 ARG A NE  1 
ATOM   2313 C  CZ  . ARG A 1 321 ? 1.180   8.197   90.799  1.00 56.05 ? 349 ARG A CZ  1 
ATOM   2314 N  NH1 . ARG A 1 321 ? 0.008   8.808   90.965  1.00 53.85 ? 349 ARG A NH1 1 
ATOM   2315 N  NH2 . ARG A 1 321 ? 1.374   7.406   89.750  1.00 48.19 ? 349 ARG A NH2 1 
ATOM   2316 N  N   . VAL A 1 322 ? 5.201   13.198  90.547  1.00 52.60 ? 350 VAL A N   1 
ATOM   2317 C  CA  . VAL A 1 322 ? 5.967   13.556  89.359  1.00 53.73 ? 350 VAL A CA  1 
ATOM   2318 C  C   . VAL A 1 322 ? 5.968   15.064  89.151  1.00 50.67 ? 350 VAL A C   1 
ATOM   2319 O  O   . VAL A 1 322 ? 6.235   15.545  88.043  1.00 53.34 ? 350 VAL A O   1 
ATOM   2320 C  CB  . VAL A 1 322 ? 5.416   12.839  88.114  1.00 50.30 ? 350 VAL A CB  1 
ATOM   2321 C  CG1 . VAL A 1 322 ? 5.634   11.335  88.220  1.00 50.37 ? 350 VAL A CG1 1 
ATOM   2322 C  CG2 . VAL A 1 322 ? 3.944   13.165  87.934  1.00 46.19 ? 350 VAL A CG2 1 
ATOM   2323 N  N   . GLY A 1 323 ? 5.676   15.822  90.211  1.00 54.07 ? 351 GLY A N   1 
ATOM   2324 C  CA  . GLY A 1 323 ? 5.692   17.272  90.108  1.00 55.05 ? 351 GLY A CA  1 
ATOM   2325 C  C   . GLY A 1 323 ? 7.037   17.844  89.710  1.00 51.51 ? 351 GLY A C   1 
ATOM   2326 O  O   . GLY A 1 323 ? 7.102   18.988  89.252  1.00 52.81 ? 351 GLY A O   1 
ATOM   2327 N  N   . ASP A 1 324 ? 8.111   17.070  89.879  1.00 54.41 ? 352 ASP A N   1 
ATOM   2328 C  CA  . ASP A 1 324 ? 9.445   17.451  89.436  1.00 55.09 ? 352 ASP A CA  1 
ATOM   2329 C  C   . ASP A 1 324 ? 9.667   17.217  87.947  1.00 56.39 ? 352 ASP A C   1 
ATOM   2330 O  O   . ASP A 1 324 ? 10.554  17.850  87.360  1.00 55.24 ? 352 ASP A O   1 
ATOM   2331 C  CB  . ASP A 1 324 ? 10.489  16.657  90.217  1.00 56.29 ? 352 ASP A CB  1 
ATOM   2332 C  CG  . ASP A 1 324 ? 10.205  15.166  90.204  1.00 58.64 ? 352 ASP A CG  1 
ATOM   2333 O  OD1 . ASP A 1 324 ? 9.063   14.786  89.863  1.00 59.08 ? 352 ASP A OD1 1 
ATOM   2334 O  OD2 . ASP A 1 324 ? 11.117  14.372  90.525  1.00 64.21 ? 352 ASP A OD2 1 
ATOM   2335 N  N   . VAL A 1 325 ? 8.904   16.313  87.336  1.00 51.22 ? 353 VAL A N   1 
ATOM   2336 C  CA  . VAL A 1 325 ? 9.073   15.962  85.933  1.00 49.54 ? 353 VAL A CA  1 
ATOM   2337 C  C   . VAL A 1 325 ? 8.041   16.649  85.054  1.00 46.37 ? 353 VAL A C   1 
ATOM   2338 O  O   . VAL A 1 325 ? 8.347   17.042  83.928  1.00 49.42 ? 353 VAL A O   1 
ATOM   2339 C  CB  . VAL A 1 325 ? 9.010   14.430  85.757  1.00 51.06 ? 353 VAL A CB  1 
ATOM   2340 C  CG1 . VAL A 1 325 ? 9.357   14.042  84.318  1.00 44.96 ? 353 VAL A CG1 1 
ATOM   2341 C  CG2 . VAL A 1 325 ? 9.937   13.742  86.753  1.00 50.31 ? 353 VAL A CG2 1 
ATOM   2342 N  N   . LEU A 1 326 ? 6.821   16.796  85.558  1.00 41.94 ? 354 LEU A N   1 
ATOM   2343 C  CA  . LEU A 1 326 ? 5.701   17.328  84.799  1.00 46.99 ? 354 LEU A CA  1 
ATOM   2344 C  C   . LEU A 1 326 ? 5.182   18.569  85.504  1.00 50.93 ? 354 LEU A C   1 
ATOM   2345 O  O   . LEU A 1 326 ? 4.917   18.538  86.710  1.00 49.90 ? 354 LEU A O   1 
ATOM   2346 C  CB  . LEU A 1 326 ? 4.572   16.298  84.668  1.00 45.26 ? 354 LEU A CB  1 
ATOM   2347 C  CG  . LEU A 1 326 ? 4.698   15.137  83.674  1.00 44.86 ? 354 LEU A CG  1 
ATOM   2348 C  CD1 . LEU A 1 326 ? 3.572   14.132  83.894  1.00 39.28 ? 354 LEU A CD1 1 
ATOM   2349 C  CD2 . LEU A 1 326 ? 4.670   15.653  82.245  1.00 48.29 ? 354 LEU A CD2 1 
ATOM   2350 N  N   . SER A 1 327 ? 5.047   19.654  84.753  1.00 47.81 ? 355 SER A N   1 
ATOM   2351 C  CA  . SER A 1 327 ? 4.389   20.842  85.264  1.00 51.02 ? 355 SER A CA  1 
ATOM   2352 C  C   . SER A 1 327 ? 2.945   20.525  85.644  1.00 51.38 ? 355 SER A C   1 
ATOM   2353 O  O   . SER A 1 327 ? 2.355   19.548  85.174  1.00 45.64 ? 355 SER A O   1 
ATOM   2354 C  CB  . SER A 1 327 ? 4.417   21.943  84.213  1.00 42.94 ? 355 SER A CB  1 
ATOM   2355 O  OG  . SER A 1 327 ? 3.476   21.664  83.190  1.00 45.45 ? 355 SER A OG  1 
ATOM   2356 N  N   . ASP A 1 328 ? 2.381   21.366  86.522  1.00 43.36 ? 356 ASP A N   1 
ATOM   2357 C  CA  . ASP A 1 328 ? 0.946   21.316  86.800  1.00 48.02 ? 356 ASP A CA  1 
ATOM   2358 C  C   . ASP A 1 328 ? 0.155   21.313  85.501  1.00 45.83 ? 356 ASP A C   1 
ATOM   2359 O  O   . ASP A 1 328 ? -0.825  20.575  85.340  1.00 41.31 ? 356 ASP A O   1 
ATOM   2360 C  CB  . ASP A 1 328 ? 0.525   22.525  87.647  1.00 48.43 ? 356 ASP A CB  1 
ATOM   2361 C  CG  . ASP A 1 328 ? 1.041   22.473  89.079  1.00 56.81 ? 356 ASP A CG  1 
ATOM   2362 O  OD1 . ASP A 1 328 ? 2.109   21.878  89.341  1.00 54.19 ? 356 ASP A OD1 1 
ATOM   2363 O  OD2 . ASP A 1 328 ? 0.374   23.070  89.950  1.00 61.66 ? 356 ASP A OD2 1 
ATOM   2364 N  N   . ASP A 1 329 ? 0.561   22.180  84.580  1.00 39.93 ? 357 ASP A N   1 
ATOM   2365 C  CA  . ASP A 1 329 ? -0.018  22.265  83.247  1.00 44.02 ? 357 ASP A CA  1 
ATOM   2366 C  C   . ASP A 1 329 ? -0.047  20.904  82.553  1.00 49.07 ? 357 ASP A C   1 
ATOM   2367 O  O   . ASP A 1 329 ? -1.099  20.430  82.103  1.00 41.78 ? 357 ASP A O   1 
ATOM   2368 C  CB  . ASP A 1 329 ? 0.814   23.263  82.452  1.00 50.88 ? 357 ASP A CB  1 
ATOM   2369 C  CG  . ASP A 1 329 ? 0.313   23.459  81.057  1.00 61.44 ? 357 ASP A CG  1 
ATOM   2370 O  OD1 . ASP A 1 329 ? -0.824  23.944  80.887  1.00 69.20 ? 357 ASP A OD1 1 
ATOM   2371 O  OD2 . ASP A 1 329 ? 1.049   23.118  80.108  1.00 68.63 ? 357 ASP A OD2 1 
ATOM   2372 N  N   . GLN A 1 330 ? 1.120   20.263  82.467  1.00 42.33 ? 358 GLN A N   1 
ATOM   2373 C  CA  . GLN A 1 330 ? 1.215   18.969  81.806  1.00 43.85 ? 358 GLN A CA  1 
ATOM   2374 C  C   . GLN A 1 330 ? 0.459   17.890  82.569  1.00 43.96 ? 358 GLN A C   1 
ATOM   2375 O  O   . GLN A 1 330 ? -0.105  16.983  81.947  1.00 44.37 ? 358 GLN A O   1 
ATOM   2376 C  CB  . GLN A 1 330 ? 2.684   18.602  81.623  1.00 40.04 ? 358 GLN A CB  1 
ATOM   2377 C  CG  . GLN A 1 330 ? 3.355   19.419  80.535  1.00 40.55 ? 358 GLN A CG  1 
ATOM   2378 C  CD  . GLN A 1 330 ? 4.773   19.841  80.873  1.00 47.15 ? 358 GLN A CD  1 
ATOM   2379 O  OE1 . GLN A 1 330 ? 5.437   19.244  81.732  1.00 44.82 ? 358 GLN A OE1 1 
ATOM   2380 N  NE2 . GLN A 1 330 ? 5.256   20.865  80.177  1.00 44.02 ? 358 GLN A NE2 1 
ATOM   2381 N  N   . ILE A 1 331 ? 0.421   17.972  83.902  1.00 43.19 ? 359 ILE A N   1 
ATOM   2382 C  CA  . ILE A 1 331 ? -0.400  17.037  84.672  1.00 40.94 ? 359 ILE A CA  1 
ATOM   2383 C  C   . ILE A 1 331 ? -1.876  17.249  84.364  1.00 40.84 ? 359 ILE A C   1 
ATOM   2384 O  O   . ILE A 1 331 ? -2.641  16.288  84.225  1.00 40.65 ? 359 ILE A O   1 
ATOM   2385 C  CB  . ILE A 1 331 ? -0.110  17.170  86.179  1.00 44.96 ? 359 ILE A CB  1 
ATOM   2386 C  CG1 . ILE A 1 331 ? 1.309   16.700  86.501  1.00 43.43 ? 359 ILE A CG1 1 
ATOM   2387 C  CG2 . ILE A 1 331 ? -1.133  16.396  86.995  1.00 46.74 ? 359 ILE A CG2 1 
ATOM   2388 C  CD1 . ILE A 1 331 ? 1.667   16.788  87.977  1.00 49.99 ? 359 ILE A CD1 1 
ATOM   2389 N  N   . LYS A 1 332 ? -2.304  18.510  84.254  1.00 39.18 ? 360 LYS A N   1 
ATOM   2390 C  CA  . LYS A 1 332 ? -3.691  18.781  83.893  1.00 39.53 ? 360 LYS A CA  1 
ATOM   2391 C  C   . LYS A 1 332 ? -4.035  18.199  82.528  1.00 40.99 ? 360 LYS A C   1 
ATOM   2392 O  O   . LYS A 1 332 ? -5.154  17.723  82.323  1.00 37.65 ? 360 LYS A O   1 
ATOM   2393 C  CB  . LYS A 1 332 ? -3.965  20.287  83.919  1.00 41.83 ? 360 LYS A CB  1 
ATOM   2394 N  N   . GLU A 1 333 ? -3.082  18.203  81.593  1.00 41.62 ? 361 GLU A N   1 
ATOM   2395 C  CA  . GLU A 1 333 ? -3.330  17.609  80.282  1.00 38.31 ? 361 GLU A CA  1 
ATOM   2396 C  C   . GLU A 1 333 ? -3.410  16.084  80.367  1.00 40.79 ? 361 GLU A C   1 
ATOM   2397 O  O   . GLU A 1 333 ? -4.197  15.461  79.641  1.00 36.09 ? 361 GLU A O   1 
ATOM   2398 C  CB  . GLU A 1 333 ? -2.245  18.051  79.302  1.00 41.45 ? 361 GLU A CB  1 
ATOM   2399 C  CG  . GLU A 1 333 ? -2.597  17.872  77.838  1.00 43.72 ? 361 GLU A CG  1 
ATOM   2400 C  CD  . GLU A 1 333 ? -1.737  18.735  76.939  1.00 49.62 ? 361 GLU A CD  1 
ATOM   2401 O  OE1 . GLU A 1 333 ? -1.742  18.505  75.712  1.00 54.72 ? 361 GLU A OE1 1 
ATOM   2402 O  OE2 . GLU A 1 333 ? -1.051  19.643  77.458  1.00 50.27 ? 361 GLU A OE2 1 
ATOM   2403 N  N   . CYS A 1 334 ? -2.612  15.465  81.250  1.00 34.56 ? 362 CYS A N   1 
ATOM   2404 C  CA  . CYS A 1 334 ? -2.775  14.033  81.521  1.00 35.93 ? 362 CYS A CA  1 
ATOM   2405 C  C   . CYS A 1 334 ? -4.186  13.728  82.016  1.00 39.77 ? 362 CYS A C   1 
ATOM   2406 O  O   . CYS A 1 334 ? -4.800  12.731  81.609  1.00 35.40 ? 362 CYS A O   1 
ATOM   2407 C  CB  . CYS A 1 334 ? -1.749  13.555  82.556  1.00 34.29 ? 362 CYS A CB  1 
ATOM   2408 S  SG  . CYS A 1 334 ? -0.022  13.445  81.992  1.00 39.57 ? 362 CYS A SG  1 
ATOM   2409 N  N   . GLU A 1 335 ? -4.721  14.585  82.892  1.00 40.40 ? 363 GLU A N   1 
ATOM   2410 C  CA  . GLU A 1 335 ? -6.031  14.325  83.482  1.00 38.95 ? 363 GLU A CA  1 
ATOM   2411 C  C   . GLU A 1 335 ? -7.143  14.446  82.450  1.00 37.40 ? 363 GLU A C   1 
ATOM   2412 O  O   . GLU A 1 335 ? -8.102  13.667  82.472  1.00 40.90 ? 363 GLU A O   1 
ATOM   2413 C  CB  . GLU A 1 335 ? -6.284  15.275  84.653  1.00 44.43 ? 363 GLU A CB  1 
ATOM   2414 C  CG  . GLU A 1 335 ? -7.612  15.048  85.363  1.00 40.66 ? 363 GLU A CG  1 
ATOM   2415 C  CD  . GLU A 1 335 ? -7.869  16.092  86.428  1.00 50.60 ? 363 GLU A CD  1 
ATOM   2416 O  OE1 . GLU A 1 335 ? -8.216  15.719  87.567  1.00 51.10 ? 363 GLU A OE1 1 
ATOM   2417 O  OE2 . GLU A 1 335 ? -7.694  17.288  86.124  1.00 53.33 ? 363 GLU A OE2 1 
ATOM   2418 N  N   . GLU A 1 336 ? -7.048  15.423  81.547  1.00 37.83 ? 364 GLU A N   1 
ATOM   2419 C  CA  . GLU A 1 336 ? -8.006  15.495  80.447  1.00 41.00 ? 364 GLU A CA  1 
ATOM   2420 C  C   . GLU A 1 336 ? -8.030  14.190  79.663  1.00 41.98 ? 364 GLU A C   1 
ATOM   2421 O  O   . GLU A 1 336 ? -9.097  13.625  79.402  1.00 46.69 ? 364 GLU A O   1 
ATOM   2422 C  CB  . GLU A 1 336 ? -7.659  16.652  79.513  1.00 42.17 ? 364 GLU A CB  1 
ATOM   2423 C  CG  . GLU A 1 336 ? -8.090  18.027  79.978  1.00 53.17 ? 364 GLU A CG  1 
ATOM   2424 C  CD  . GLU A 1 336 ? -7.283  19.114  79.301  1.00 58.84 ? 364 GLU A CD  1 
ATOM   2425 O  OE1 . GLU A 1 336 ? -6.979  20.139  79.953  1.00 62.40 ? 364 GLU A OE1 1 
ATOM   2426 O  OE2 . GLU A 1 336 ? -6.929  18.928  78.114  1.00 60.46 ? 364 GLU A OE2 1 
ATOM   2427 N  N   . LEU A 1 337 ? -6.849  13.685  79.305  1.00 38.17 ? 365 LEU A N   1 
ATOM   2428 C  CA  . LEU A 1 337 ? -6.704  12.561  78.393  1.00 35.73 ? 365 LEU A CA  1 
ATOM   2429 C  C   . LEU A 1 337 ? -6.760  11.198  79.072  1.00 35.40 ? 365 LEU A C   1 
ATOM   2430 O  O   . LEU A 1 337 ? -6.774  10.181  78.367  1.00 36.10 ? 365 LEU A O   1 
ATOM   2431 C  CB  . LEU A 1 337 ? -5.389  12.690  77.623  1.00 33.55 ? 365 LEU A CB  1 
ATOM   2432 C  CG  . LEU A 1 337 ? -5.215  14.028  76.915  1.00 38.13 ? 365 LEU A CG  1 
ATOM   2433 C  CD1 . LEU A 1 337 ? -3.814  14.141  76.338  1.00 32.88 ? 365 LEU A CD1 1 
ATOM   2434 C  CD2 . LEU A 1 337 ? -6.273  14.158  75.828  1.00 34.06 ? 365 LEU A CD2 1 
ATOM   2435 N  N   . GLY A 1 338 ? -6.809  11.143  80.402  1.00 36.67 ? 366 GLY A N   1 
ATOM   2436 C  CA  . GLY A 1 338 ? -6.871  9.867   81.092  1.00 35.49 ? 366 GLY A CA  1 
ATOM   2437 C  C   . GLY A 1 338 ? -5.534  9.175   81.249  1.00 34.19 ? 366 GLY A C   1 
ATOM   2438 O  O   . GLY A 1 338 ? -5.489  8.007   81.650  1.00 32.50 ? 366 GLY A O   1 
ATOM   2439 N  N   . ILE A 1 339 ? -4.439  9.877   80.969  1.00 32.43 ? 367 ILE A N   1 
ATOM   2440 C  CA  . ILE A 1 339 ? -3.116  9.267   80.944  1.00 28.23 ? 367 ILE A CA  1 
ATOM   2441 C  C   . ILE A 1 339 ? -2.668  8.882   82.348  1.00 35.84 ? 367 ILE A C   1 
ATOM   2442 O  O   . ILE A 1 339 ? -2.838  9.649   83.310  1.00 35.83 ? 367 ILE A O   1 
ATOM   2443 C  CB  . ILE A 1 339 ? -2.119  10.229  80.284  1.00 29.77 ? 367 ILE A CB  1 
ATOM   2444 C  CG1 . ILE A 1 339 ? -2.582  10.546  78.859  1.00 32.78 ? 367 ILE A CG1 1 
ATOM   2445 C  CG2 . ILE A 1 339 ? -0.713  9.651   80.319  1.00 28.97 ? 367 ILE A CG2 1 
ATOM   2446 C  CD1 . ILE A 1 339 ? -1.678  11.512  78.125  1.00 37.88 ? 367 ILE A CD1 1 
ATOM   2447 N  N   . LEU A 1 340 ? -2.092  7.679   82.462  1.00 27.38 ? 368 LEU A N   1 
ATOM   2448 C  CA  . LEU A 1 340 ? -1.451  7.171   83.668  1.00 34.43 ? 368 LEU A CA  1 
ATOM   2449 C  C   . LEU A 1 340 ? 0.027   7.541   83.674  1.00 31.30 ? 368 LEU A C   1 
ATOM   2450 O  O   . LEU A 1 340 ? 0.659   7.661   82.622  1.00 33.08 ? 368 LEU A O   1 
ATOM   2451 C  CB  . LEU A 1 340 ? -1.561  5.642   83.762  1.00 33.94 ? 368 LEU A CB  1 
ATOM   2452 C  CG  . LEU A 1 340 ? -2.883  4.873   83.919  1.00 41.80 ? 368 LEU A CG  1 
ATOM   2453 C  CD1 . LEU A 1 340 ? -3.833  5.614   84.807  1.00 37.61 ? 368 LEU A CD1 1 
ATOM   2454 C  CD2 . LEU A 1 340 ? -3.542  4.548   82.592  1.00 43.49 ? 368 LEU A CD2 1 
ATOM   2455 N  N   . VAL A 1 341 ? 0.587   7.684   84.870  1.00 31.76 ? 369 VAL A N   1 
ATOM   2456 C  CA  . VAL A 1 341 ? 2.000   8.004   85.038  1.00 32.11 ? 369 VAL A CA  1 
ATOM   2457 C  C   . VAL A 1 341 ? 2.580   7.059   86.078  1.00 36.89 ? 369 VAL A C   1 
ATOM   2458 O  O   . VAL A 1 341 ? 1.936   6.772   87.094  1.00 37.63 ? 369 VAL A O   1 
ATOM   2459 C  CB  . VAL A 1 341 ? 2.215   9.480   85.460  1.00 35.27 ? 369 VAL A CB  1 
ATOM   2460 C  CG1 . VAL A 1 341 ? 3.700   9.856   85.410  1.00 33.28 ? 369 VAL A CG1 1 
ATOM   2461 C  CG2 . VAL A 1 341 ? 1.405   10.415  84.586  1.00 36.94 ? 369 VAL A CG2 1 
ATOM   2462 N  N   . ASP A 1 342 ? 3.782   6.542   85.805  1.00 35.89 ? 370 ASP A N   1 
ATOM   2463 C  CA  . ASP A 1 342 ? 4.542   5.783   86.784  1.00 35.48 ? 370 ASP A CA  1 
ATOM   2464 C  C   . ASP A 1 342 ? 6.011   6.151   86.651  1.00 36.60 ? 370 ASP A C   1 
ATOM   2465 O  O   . ASP A 1 342 ? 6.429   6.822   85.704  1.00 34.68 ? 370 ASP A O   1 
ATOM   2466 C  CB  . ASP A 1 342 ? 4.370   4.264   86.632  1.00 33.71 ? 370 ASP A CB  1 
ATOM   2467 C  CG  . ASP A 1 342 ? 4.757   3.500   87.898  1.00 40.60 ? 370 ASP A CG  1 
ATOM   2468 O  OD1 . ASP A 1 342 ? 4.718   4.092   88.996  1.00 44.19 ? 370 ASP A OD1 1 
ATOM   2469 O  OD2 . ASP A 1 342 ? 5.105   2.307   87.801  1.00 43.51 ? 370 ASP A OD2 1 
ATOM   2470 N  N   . ARG A 1 343 ? 6.803   5.664   87.596  1.00 39.12 ? 371 ARG A N   1 
ATOM   2471 C  CA  . ARG A 1 343 ? 8.176   6.122   87.716  1.00 44.35 ? 371 ARG A CA  1 
ATOM   2472 C  C   . ARG A 1 343 ? 9.002   5.068   88.439  1.00 41.03 ? 371 ARG A C   1 
ATOM   2473 O  O   . ARG A 1 343 ? 8.535   4.472   89.413  1.00 46.97 ? 371 ARG A O   1 
ATOM   2474 C  CB  . ARG A 1 343 ? 8.203   7.442   88.480  1.00 42.71 ? 371 ARG A CB  1 
ATOM   2475 C  CG  . ARG A 1 343 ? 9.390   8.301   88.233  1.00 46.90 ? 371 ARG A CG  1 
ATOM   2476 C  CD  . ARG A 1 343 ? 9.314   9.487   89.162  1.00 48.97 ? 371 ARG A CD  1 
ATOM   2477 N  NE  . ARG A 1 343 ? 10.581  10.198  89.247  1.00 53.04 ? 371 ARG A NE  1 
ATOM   2478 C  CZ  . ARG A 1 343 ? 10.711  11.402  89.785  1.00 55.14 ? 371 ARG A CZ  1 
ATOM   2479 N  NH1 . ARG A 1 343 ? 9.646   12.025  90.275  1.00 52.71 ? 371 ARG A NH1 1 
ATOM   2480 N  NH2 . ARG A 1 343 ? 11.901  11.985  89.824  1.00 62.10 ? 371 ARG A NH2 1 
ATOM   2481 N  N   . ASP A 1 344 ? 10.219  4.837   87.956  1.00 43.17 ? 372 ASP A N   1 
ATOM   2482 C  CA  . ASP A 1 344 ? 11.184  4.052   88.700  1.00 45.96 ? 372 ASP A CA  1 
ATOM   2483 C  C   . ASP A 1 344 ? 12.295  4.990   89.187  1.00 47.48 ? 372 ASP A C   1 
ATOM   2484 O  O   . ASP A 1 344 ? 12.099  6.211   89.272  1.00 50.54 ? 372 ASP A O   1 
ATOM   2485 C  CB  . ASP A 1 344 ? 11.682  2.872   87.845  1.00 45.47 ? 372 ASP A CB  1 
ATOM   2486 C  CG  . ASP A 1 344 ? 12.375  3.301   86.561  1.00 47.68 ? 372 ASP A CG  1 
ATOM   2487 O  OD1 . ASP A 1 344 ? 12.553  2.427   85.679  1.00 44.97 ? 372 ASP A OD1 1 
ATOM   2488 O  OD2 . ASP A 1 344 ? 12.760  4.483   86.423  1.00 44.76 ? 372 ASP A OD2 1 
ATOM   2489 N  N   . ASP A 1 345 ? 13.456  4.427   89.515  1.00 54.70 ? 373 ASP A N   1 
ATOM   2490 C  CA  . ASP A 1 345 ? 14.558  5.247   90.005  1.00 57.14 ? 373 ASP A CA  1 
ATOM   2491 C  C   . ASP A 1 345 ? 15.341  5.921   88.885  1.00 58.57 ? 373 ASP A C   1 
ATOM   2492 O  O   . ASP A 1 345 ? 16.246  6.715   89.171  1.00 62.86 ? 373 ASP A O   1 
ATOM   2493 C  CB  . ASP A 1 345 ? 15.503  4.404   90.870  1.00 58.24 ? 373 ASP A CB  1 
ATOM   2494 C  CG  . ASP A 1 345 ? 16.088  3.220   90.122  1.00 63.33 ? 373 ASP A CG  1 
ATOM   2495 O  OD1 . ASP A 1 345 ? 15.591  2.896   89.022  1.00 61.94 ? 373 ASP A OD1 1 
ATOM   2496 O  OD2 . ASP A 1 345 ? 17.041  2.601   90.647  1.00 72.91 ? 373 ASP A OD2 1 
ATOM   2497 N  N   . GLN A 1 346 ? 15.018  5.632   87.629  1.00 51.79 ? 374 GLN A N   1 
ATOM   2498 C  CA  . GLN A 1 346 ? 15.725  6.196   86.492  1.00 49.12 ? 374 GLN A CA  1 
ATOM   2499 C  C   . GLN A 1 346 ? 14.854  7.062   85.594  1.00 55.44 ? 374 GLN A C   1 
ATOM   2500 O  O   . GLN A 1 346 ? 15.356  8.049   85.046  1.00 48.96 ? 374 GLN A O   1 
ATOM   2501 C  CB  . GLN A 1 346 ? 16.349  5.074   85.646  1.00 53.77 ? 374 GLN A CB  1 
ATOM   2502 N  N   . GLY A 1 347 ? 13.571  6.738   85.429  1.00 42.42 ? 375 GLY A N   1 
ATOM   2503 C  CA  . GLY A 1 347 ? 12.769  7.449   84.459  1.00 37.74 ? 375 GLY A CA  1 
ATOM   2504 C  C   . GLY A 1 347 ? 11.299  7.472   84.816  1.00 38.27 ? 375 GLY A C   1 
ATOM   2505 O  O   . GLY A 1 347 ? 10.861  6.876   85.802  1.00 37.32 ? 375 GLY A O   1 
ATOM   2506 N  N   . THR A 1 348 ? 10.537  8.172   83.976  1.00 35.01 ? 376 THR A N   1 
ATOM   2507 C  CA  . THR A 1 348 ? 9.103   8.377   84.148  1.00 35.11 ? 376 THR A CA  1 
ATOM   2508 C  C   . THR A 1 348 ? 8.363   7.837   82.929  1.00 31.92 ? 376 THR A C   1 
ATOM   2509 O  O   . THR A 1 348 ? 8.834   7.980   81.800  1.00 33.35 ? 376 THR A O   1 
ATOM   2510 C  CB  . THR A 1 348 ? 8.787   9.875   84.345  1.00 35.25 ? 376 THR A CB  1 
ATOM   2511 O  OG1 . THR A 1 348 ? 9.340   10.313  85.590  1.00 38.89 ? 376 THR A OG1 1 
ATOM   2512 C  CG2 . THR A 1 348 ? 7.291   10.129  84.359  1.00 35.86 ? 376 THR A CG2 1 
ATOM   2513 N  N   . LEU A 1 349 ? 7.203   7.224   83.159  1.00 31.96 ? 377 LEU A N   1 
ATOM   2514 C  CA  . LEU A 1 349 ? 6.412   6.595   82.108  1.00 29.23 ? 377 LEU A CA  1 
ATOM   2515 C  C   . LEU A 1 349 ? 5.016   7.205   82.064  1.00 28.34 ? 377 LEU A C   1 
ATOM   2516 O  O   . LEU A 1 349 ? 4.311   7.222   83.076  1.00 33.16 ? 377 LEU A O   1 
ATOM   2517 C  CB  . LEU A 1 349 ? 6.339   5.082   82.355  1.00 32.21 ? 377 LEU A CB  1 
ATOM   2518 C  CG  . LEU A 1 349 ? 5.246   4.257   81.700  1.00 35.59 ? 377 LEU A CG  1 
ATOM   2519 C  CD1 . LEU A 1 349 ? 5.548   4.220   80.227  1.00 36.30 ? 377 LEU A CD1 1 
ATOM   2520 C  CD2 . LEU A 1 349 ? 5.268   2.837   82.260  1.00 37.04 ? 377 LEU A CD2 1 
ATOM   2521 N  N   . LEU A 1 350 ? 4.620   7.709   80.898  1.00 28.58 ? 378 LEU A N   1 
ATOM   2522 C  CA  . LEU A 1 350 ? 3.230   8.042   80.610  1.00 26.53 ? 378 LEU A CA  1 
ATOM   2523 C  C   . LEU A 1 350 ? 2.627   6.893   79.799  1.00 24.45 ? 378 LEU A C   1 
ATOM   2524 O  O   . LEU A 1 350 ? 3.233   6.454   78.818  1.00 24.16 ? 378 LEU A O   1 
ATOM   2525 C  CB  . LEU A 1 350 ? 3.111   9.359   79.838  1.00 28.40 ? 378 LEU A CB  1 
ATOM   2526 C  CG  . LEU A 1 350 ? 3.899   10.590  80.326  1.00 35.86 ? 378 LEU A CG  1 
ATOM   2527 C  CD1 . LEU A 1 350 ? 3.558   11.814  79.501  1.00 32.10 ? 378 LEU A CD1 1 
ATOM   2528 C  CD2 . LEU A 1 350 ? 3.636   10.851  81.792  1.00 36.86 ? 378 LEU A CD2 1 
ATOM   2529 N  N   . GLN A 1 351 ? 1.452   6.409   80.209  1.00 27.05 ? 379 GLN A N   1 
ATOM   2530 C  CA  . GLN A 1 351 ? 0.837   5.243   79.575  1.00 24.87 ? 379 GLN A CA  1 
ATOM   2531 C  C   . GLN A 1 351 ? -0.685  5.337   79.634  1.00 26.78 ? 379 GLN A C   1 
ATOM   2532 O  O   . GLN A 1 351 ? -1.254  5.939   80.546  1.00 25.62 ? 379 GLN A O   1 
ATOM   2533 C  CB  . GLN A 1 351 ? 1.302   3.927   80.236  1.00 25.16 ? 379 GLN A CB  1 
ATOM   2534 C  CG  . GLN A 1 351 ? 0.888   3.795   81.709  1.00 28.23 ? 379 GLN A CG  1 
ATOM   2535 C  CD  . GLN A 1 351 ? 1.380   2.521   82.410  1.00 31.42 ? 379 GLN A CD  1 
ATOM   2536 O  OE1 . GLN A 1 351 ? 1.340   2.440   83.636  1.00 32.74 ? 379 GLN A OE1 1 
ATOM   2537 N  NE2 . GLN A 1 351 ? 1.827   1.525   81.640  1.00 26.39 ? 379 GLN A NE2 1 
ATOM   2538 N  N   . ILE A 1 352 ? -1.344  4.695   78.667  1.00 24.28 ? 380 ILE A N   1 
ATOM   2539 C  CA  . ILE A 1 352 ? -2.796  4.550   78.687  1.00 22.11 ? 380 ILE A CA  1 
ATOM   2540 C  C   . ILE A 1 352 ? -3.131  3.311   77.872  1.00 24.50 ? 380 ILE A C   1 
ATOM   2541 O  O   . ILE A 1 352 ? -2.346  2.880   77.026  1.00 25.12 ? 380 ILE A O   1 
ATOM   2542 C  CB  . ILE A 1 352 ? -3.509  5.818   78.153  1.00 24.85 ? 380 ILE A CB  1 
ATOM   2543 C  CG1 . ILE A 1 352 ? -5.019  5.781   78.469  1.00 25.65 ? 380 ILE A CG1 1 
ATOM   2544 C  CG2 . ILE A 1 352 ? -3.226  6.020   76.661  1.00 23.24 ? 380 ILE A CG2 1 
ATOM   2545 C  CD1 . ILE A 1 352 ? -5.732  7.089   78.139  1.00 25.95 ? 380 ILE A CD1 1 
ATOM   2546 N  N   . PHE A 1 353 ? -4.283  2.718   78.153  1.00 23.23 ? 381 PHE A N   1 
ATOM   2547 C  CA  . PHE A 1 353 ? -4.651  1.411   77.618  1.00 20.73 ? 381 PHE A CA  1 
ATOM   2548 C  C   . PHE A 1 353 ? -5.979  1.485   76.876  1.00 22.48 ? 381 PHE A C   1 
ATOM   2549 O  O   . PHE A 1 353 ? -6.929  2.124   77.347  1.00 23.80 ? 381 PHE A O   1 
ATOM   2550 C  CB  . PHE A 1 353 ? -4.725  0.407   78.743  1.00 21.83 ? 381 PHE A CB  1 
ATOM   2551 C  CG  . PHE A 1 353 ? -3.401  0.157   79.393  1.00 23.05 ? 381 PHE A CG  1 
ATOM   2552 C  CD1 . PHE A 1 353 ? -2.964  0.945   80.445  1.00 24.84 ? 381 PHE A CD1 1 
ATOM   2553 C  CD2 . PHE A 1 353 ? -2.577  -0.838  78.909  1.00 23.67 ? 381 PHE A CD2 1 
ATOM   2554 C  CE1 . PHE A 1 353 ? -1.728  0.714   81.031  1.00 29.27 ? 381 PHE A CE1 1 
ATOM   2555 C  CE2 . PHE A 1 353 ? -1.335  -1.076  79.491  1.00 24.88 ? 381 PHE A CE2 1 
ATOM   2556 C  CZ  . PHE A 1 353 ? -0.919  -0.297  80.551  1.00 25.75 ? 381 PHE A CZ  1 
ATOM   2557 N  N   . THR A 1 354 ? -6.037  0.846   75.705  1.00 19.56 ? 382 THR A N   1 
ATOM   2558 C  CA  . THR A 1 354 ? -7.307  0.738   75.003  1.00 19.97 ? 382 THR A CA  1 
ATOM   2559 C  C   . THR A 1 354 ? -8.134  -0.397  75.590  1.00 20.14 ? 382 THR A C   1 
ATOM   2560 O  O   . THR A 1 354 ? -7.626  -1.293  76.269  1.00 21.48 ? 382 THR A O   1 
ATOM   2561 C  CB  . THR A 1 354 ? -7.119  0.476   73.499  1.00 19.06 ? 382 THR A CB  1 
ATOM   2562 O  OG1 . THR A 1 354 ? -6.698  -0.885  73.288  1.00 19.59 ? 382 THR A OG1 1 
ATOM   2563 C  CG2 . THR A 1 354 ? -6.080  1.435   72.891  1.00 20.30 ? 382 THR A CG2 1 
ATOM   2564 N  N   . LYS A 1 355 ? -9.430  -0.338  75.324  1.00 20.34 ? 383 LYS A N   1 
ATOM   2565 C  CA  . LYS A 1 355 ? -10.270 -1.505  75.472  1.00 19.17 ? 383 LYS A CA  1 
ATOM   2566 C  C   . LYS A 1 355 ? -9.838  -2.548  74.441  1.00 18.44 ? 383 LYS A C   1 
ATOM   2567 O  O   . LYS A 1 355 ? -9.094  -2.240  73.507  1.00 18.00 ? 383 LYS A O   1 
ATOM   2568 C  CB  . LYS A 1 355 ? -11.733 -1.094  75.305  1.00 20.80 ? 383 LYS A CB  1 
ATOM   2569 C  CG  . LYS A 1 355 ? -12.249 -0.307  76.502  1.00 23.35 ? 383 LYS A CG  1 
ATOM   2570 C  CD  . LYS A 1 355 ? -13.773 -0.291  76.502  1.00 36.32 ? 383 LYS A CD  1 
ATOM   2571 C  CE  . LYS A 1 355 ? -14.326 0.478   77.692  1.00 37.06 ? 383 LYS A CE  1 
ATOM   2572 N  NZ  . LYS A 1 355 ? -15.774 0.772   77.475  1.00 41.99 ? 383 LYS A NZ  1 
ATOM   2573 N  N   . PRO A 1 356 ? -10.310 -3.798  74.561  1.00 21.14 ? 384 PRO A N   1 
ATOM   2574 C  CA  . PRO A 1 356 ? -9.880  -4.830  73.610  1.00 21.41 ? 384 PRO A CA  1 
ATOM   2575 C  C   . PRO A 1 356 ? -10.112 -4.408  72.164  1.00 19.31 ? 384 PRO A C   1 
ATOM   2576 O  O   . PRO A 1 356 ? -11.100 -3.746  71.840  1.00 20.20 ? 384 PRO A O   1 
ATOM   2577 C  CB  . PRO A 1 356 ? -10.739 -6.042  73.995  1.00 19.95 ? 384 PRO A CB  1 
ATOM   2578 C  CG  . PRO A 1 356 ? -10.877 -5.879  75.489  1.00 23.62 ? 384 PRO A CG  1 
ATOM   2579 C  CD  . PRO A 1 356 ? -11.037 -4.378  75.704  1.00 20.64 ? 384 PRO A CD  1 
ATOM   2580 N  N   . LEU A 1 357 ? -9.190  -4.837  71.296  1.00 16.15 ? 385 LEU A N   1 
ATOM   2581 C  CA  . LEU A 1 357 ? -9.182  -4.427  69.894  1.00 16.96 ? 385 LEU A CA  1 
ATOM   2582 C  C   . LEU A 1 357 ? -10.305 -5.074  69.101  1.00 19.23 ? 385 LEU A C   1 
ATOM   2583 O  O   . LEU A 1 357 ? -10.676 -4.570  68.038  1.00 17.06 ? 385 LEU A O   1 
ATOM   2584 C  CB  . LEU A 1 357 ? -7.845  -4.806  69.253  1.00 16.31 ? 385 LEU A CB  1 
ATOM   2585 C  CG  . LEU A 1 357 ? -6.592  -4.346  70.003  1.00 17.05 ? 385 LEU A CG  1 
ATOM   2586 C  CD1 . LEU A 1 357 ? -5.356  -4.671  69.178  1.00 17.66 ? 385 LEU A CD1 1 
ATOM   2587 C  CD2 . LEU A 1 357 ? -6.703  -2.820  70.314  1.00 16.82 ? 385 LEU A CD2 1 
ATOM   2588 N  N   . GLY A 1 358 ? -10.779 -6.244  69.536  1.00 17.22 ? 386 GLY A N   1 
ATOM   2589 C  CA  . GLY A 1 358 ? -11.840 -6.908  68.797  1.00 19.95 ? 386 GLY A CA  1 
ATOM   2590 C  C   . GLY A 1 358 ? -12.931 -7.458  69.695  1.00 19.87 ? 386 GLY A C   1 
ATOM   2591 O  O   . GLY A 1 358 ? -13.172 -6.919  70.784  1.00 20.43 ? 386 GLY A O   1 
ATOM   2592 N  N   . ASP A 1 359 ? -13.638 -8.464  69.220  1.00 20.34 ? 387 ASP A N   1 
ATOM   2593 C  CA  . ASP A 1 359 ? -14.770 -9.016  69.930  1.00 18.48 ? 387 ASP A CA  1 
ATOM   2594 C  C   . ASP A 1 359 ? -14.485 -9.569  71.313  1.00 19.96 ? 387 ASP A C   1 
ATOM   2595 O  O   . ASP A 1 359 ? -15.238 -9.397  72.200  1.00 19.09 ? 387 ASP A O   1 
ATOM   2596 C  CB  . ASP A 1 359 ? -15.431 -10.134 69.118  1.00 20.03 ? 387 ASP A CB  1 
ATOM   2597 C  CG  . ASP A 1 359 ? -16.135 -9.639  67.874  1.00 21.91 ? 387 ASP A CG  1 
ATOM   2598 O  OD1 . ASP A 1 359 ? -16.493 -8.478  67.812  1.00 19.61 ? 387 ASP A OD1 1 
ATOM   2599 O  OD2 . ASP A 1 359 ? -16.303 -10.445 66.973  1.00 22.23 ? 387 ASP A OD2 1 
ATOM   2600 N  N   . ARG A 1 360 ? -13.402 -10.305 71.420  1.00 17.22 ? 388 ARG A N   1 
ATOM   2601 C  CA  . ARG A 1 360 ? -13.085 -10.938 72.673  1.00 19.32 ? 388 ARG A CA  1 
ATOM   2602 C  C   . ARG A 1 360 ? -12.274 -10.053 73.582  1.00 21.97 ? 388 ARG A C   1 
ATOM   2603 O  O   . ARG A 1 360 ? -11.476 -9.297  73.115  1.00 22.42 ? 388 ARG A O   1 
ATOM   2604 C  CB  . ARG A 1 360 ? -12.333 -12.237 72.437  1.00 19.94 ? 388 ARG A CB  1 
ATOM   2605 C  CG  . ARG A 1 360 ? -12.819 -13.089 71.292  1.00 22.03 ? 388 ARG A CG  1 
ATOM   2606 C  CD  . ARG A 1 360 ? -12.064 -14.393 71.200  1.00 20.44 ? 388 ARG A CD  1 
ATOM   2607 N  NE  . ARG A 1 360 ? -12.568 -15.267 70.178  1.00 24.32 ? 388 ARG A NE  1 
ATOM   2608 C  CZ  . ARG A 1 360 ? -12.283 -16.551 70.070  1.00 22.54 ? 388 ARG A CZ  1 
ATOM   2609 N  NH1 . ARG A 1 360 ? -12.764 -17.252 69.093  1.00 22.57 ? 388 ARG A NH1 1 
ATOM   2610 N  NH2 . ARG A 1 360 ? -11.496 -17.127 70.921  1.00 24.65 ? 388 ARG A NH2 1 
ATOM   2611 N  N   . PRO A 1 361 ? -12.409 -10.225 74.912  1.00 22.43 ? 389 PRO A N   1 
ATOM   2612 C  CA  . PRO A 1 361 ? -11.637 -9.482  75.908  1.00 22.22 ? 389 PRO A CA  1 
ATOM   2613 C  C   . PRO A 1 361 ? -10.242 -10.084 76.032  1.00 23.32 ? 389 PRO A C   1 
ATOM   2614 O  O   . PRO A 1 361 ? -9.926  -10.600 77.043  1.00 25.88 ? 389 PRO A O   1 
ATOM   2615 C  CB  . PRO A 1 361 ? -12.430 -9.704  77.204  1.00 22.55 ? 389 PRO A CB  1 
ATOM   2616 C  CG  . PRO A 1 361 ? -13.086 -10.986 77.015  1.00 21.41 ? 389 PRO A CG  1 
ATOM   2617 C  CD  . PRO A 1 361 ? -13.430 -11.062 75.548  1.00 23.19 ? 389 PRO A CD  1 
ATOM   2618 N  N   . THR A 1 362 ? -9.429  -9.950  75.008  1.00 19.11 ? 390 THR A N   1 
ATOM   2619 C  CA  . THR A 1 362 ? -8.155  -10.537 74.924  1.00 19.37 ? 390 THR A CA  1 
ATOM   2620 C  C   . THR A 1 362 ? -7.091  -9.484  74.621  1.00 19.63 ? 390 THR A C   1 
ATOM   2621 O  O   . THR A 1 362 ? -6.667  -8.839  75.494  1.00 21.13 ? 390 THR A O   1 
ATOM   2622 C  CB  . THR A 1 362 ? -8.163  -11.626 73.841  1.00 22.20 ? 390 THR A CB  1 
ATOM   2623 O  OG1 . THR A 1 362 ? -8.667  -11.094 72.630  1.00 20.51 ? 390 THR A OG1 1 
ATOM   2624 C  CG2 . THR A 1 362 ? -9.011  -12.792 74.280  1.00 19.59 ? 390 THR A CG2 1 
ATOM   2625 N  N   . ILE A 1 363 ? -6.759  -9.277  73.361  1.00 19.01 ? 391 ILE A N   1 
ATOM   2626 C  CA  . ILE A 1 363 ? -5.665  -8.348  73.042  1.00 18.64 ? 391 ILE A CA  1 
ATOM   2627 C  C   . ILE A 1 363 ? -6.128  -6.897  73.166  1.00 20.20 ? 391 ILE A C   1 
ATOM   2628 O  O   . ILE A 1 363 ? -7.270  -6.549  72.829  1.00 18.46 ? 391 ILE A O   1 
ATOM   2629 C  CB  . ILE A 1 363 ? -5.104  -8.652  71.635  1.00 18.70 ? 391 ILE A CB  1 
ATOM   2630 C  CG1 . ILE A 1 363 ? -3.948  -7.705  71.274  1.00 19.53 ? 391 ILE A CG1 1 
ATOM   2631 C  CG2 . ILE A 1 363 ? -6.212  -8.579  70.585  1.00 20.51 ? 391 ILE A CG2 1 
ATOM   2632 C  CD1 . ILE A 1 363 ? -3.248  -8.068  69.970  1.00 18.89 ? 391 ILE A CD1 1 
ATOM   2633 N  N   . PHE A 1 364 ? -5.234  -6.033  73.657  1.00 17.18 ? 392 PHE A N   1 
ATOM   2634 C  CA  . PHE A 1 364 ? -5.473  -4.588  73.672  1.00 20.16 ? 392 PHE A CA  1 
ATOM   2635 C  C   . PHE A 1 364 ? -4.153  -3.893  73.361  1.00 20.55 ? 392 PHE A C   1 
ATOM   2636 O  O   . PHE A 1 364 ? -3.108  -4.539  73.221  1.00 18.76 ? 392 PHE A O   1 
ATOM   2637 C  CB  . PHE A 1 364 ? -6.066  -4.114  75.012  1.00 20.36 ? 392 PHE A CB  1 
ATOM   2638 C  CG  . PHE A 1 364 ? -5.280  -4.561  76.231  1.00 22.58 ? 392 PHE A CG  1 
ATOM   2639 C  CD1 . PHE A 1 364 ? -5.512  -5.802  76.804  1.00 20.92 ? 392 PHE A CD1 1 
ATOM   2640 C  CD2 . PHE A 1 364 ? -4.323  -3.730  76.812  1.00 21.87 ? 392 PHE A CD2 1 
ATOM   2641 C  CE1 . PHE A 1 364 ? -4.794  -6.209  77.927  1.00 24.87 ? 392 PHE A CE1 1 
ATOM   2642 C  CE2 . PHE A 1 364 ? -3.605  -4.129  77.940  1.00 22.82 ? 392 PHE A CE2 1 
ATOM   2643 C  CZ  . PHE A 1 364 ? -3.827  -5.370  78.495  1.00 22.34 ? 392 PHE A CZ  1 
ATOM   2644 N  N   . ILE A 1 365 ? -4.201  -2.571  73.240  1.00 19.78 ? 393 ILE A N   1 
ATOM   2645 C  CA  . ILE A 1 365 ? -3.026  -1.764  72.934  1.00 19.36 ? 393 ILE A CA  1 
ATOM   2646 C  C   . ILE A 1 365 ? -2.749  -0.792  74.078  1.00 19.73 ? 393 ILE A C   1 
ATOM   2647 O  O   . ILE A 1 365 ? -3.659  -0.323  74.774  1.00 21.85 ? 393 ILE A O   1 
ATOM   2648 C  CB  . ILE A 1 365 ? -3.216  -1.039  71.573  1.00 17.03 ? 393 ILE A CB  1 
ATOM   2649 C  CG1 . ILE A 1 365 ? -2.827  -1.981  70.419  1.00 17.55 ? 393 ILE A CG1 1 
ATOM   2650 C  CG2 . ILE A 1 365 ? -2.395  0.259   71.453  1.00 18.70 ? 393 ILE A CG2 1 
ATOM   2651 C  CD1 . ILE A 1 365 ? -3.259  -1.494  69.053  1.00 17.82 ? 393 ILE A CD1 1 
ATOM   2652 N  N   . GLU A 1 366 ? -1.462  -0.531  74.304  1.00 18.56 ? 394 GLU A N   1 
ATOM   2653 C  CA  . GLU A 1 366 ? -1.008  0.499   75.229  1.00 21.78 ? 394 GLU A CA  1 
ATOM   2654 C  C   . GLU A 1 366 ? -0.292  1.578   74.427  1.00 21.08 ? 394 GLU A C   1 
ATOM   2655 O  O   . GLU A 1 366 ? 0.496   1.262   73.530  1.00 19.83 ? 394 GLU A O   1 
ATOM   2656 C  CB  . GLU A 1 366 ? -0.055  -0.111  76.271  1.00 23.39 ? 394 GLU A CB  1 
ATOM   2657 C  CG  . GLU A 1 366 ? 0.563   0.857   77.262  1.00 21.26 ? 394 GLU A CG  1 
ATOM   2658 C  CD  . GLU A 1 366 ? 1.570   0.155   78.153  1.00 24.54 ? 394 GLU A CD  1 
ATOM   2659 O  OE1 . GLU A 1 366 ? 1.770   -1.067  77.960  1.00 21.94 ? 394 GLU A OE1 1 
ATOM   2660 O  OE2 . GLU A 1 366 ? 2.173   0.811   79.032  1.00 25.13 ? 394 GLU A OE2 1 
ATOM   2661 N  N   . ILE A 1 367 ? -0.581  2.851   74.717  1.00 18.66 ? 395 ILE A N   1 
ATOM   2662 C  CA  . ILE A 1 367 ? 0.218   3.953   74.182  1.00 20.20 ? 395 ILE A CA  1 
ATOM   2663 C  C   . ILE A 1 367 ? 1.126   4.449   75.291  1.00 20.48 ? 395 ILE A C   1 
ATOM   2664 O  O   . ILE A 1 367 ? 0.681   4.622   76.436  1.00 23.70 ? 395 ILE A O   1 
ATOM   2665 C  CB  . ILE A 1 367 ? -0.659  5.098   73.642  1.00 21.35 ? 395 ILE A CB  1 
ATOM   2666 C  CG1 . ILE A 1 367 ? -1.765  4.549   72.731  1.00 22.01 ? 395 ILE A CG1 1 
ATOM   2667 C  CG2 . ILE A 1 367 ? 0.230   6.146   72.932  1.00 21.74 ? 395 ILE A CG2 1 
ATOM   2668 C  CD1 . ILE A 1 367 ? -1.256  3.799   71.484  1.00 21.54 ? 395 ILE A CD1 1 
ATOM   2669 N  N   . ILE A 1 368 ? 2.405   4.660   74.974  1.00 23.48 ? 396 ILE A N   1 
ATOM   2670 C  CA  . ILE A 1 368 ? 3.359   5.072   75.996  1.00 20.43 ? 396 ILE A CA  1 
ATOM   2671 C  C   . ILE A 1 368 ? 4.302   6.150   75.479  1.00 24.98 ? 396 ILE A C   1 
ATOM   2672 O  O   . ILE A 1 368 ? 4.586   6.263   74.281  1.00 24.59 ? 396 ILE A O   1 
ATOM   2673 C  CB  . ILE A 1 368 ? 4.216   3.911   76.545  1.00 24.25 ? 396 ILE A CB  1 
ATOM   2674 C  CG1 . ILE A 1 368 ? 5.091   3.304   75.459  1.00 26.66 ? 396 ILE A CG1 1 
ATOM   2675 C  CG2 . ILE A 1 368 ? 3.367   2.827   77.112  1.00 27.99 ? 396 ILE A CG2 1 
ATOM   2676 C  CD1 . ILE A 1 368 ? 6.245   2.565   76.066  1.00 30.54 ? 396 ILE A CD1 1 
ATOM   2677 N  N   . GLN A 1 369 ? 4.808   6.933   76.424  1.00 24.07 ? 397 GLN A N   1 
ATOM   2678 C  CA  . GLN A 1 369 ? 5.965   7.779   76.167  1.00 21.69 ? 397 GLN A CA  1 
ATOM   2679 C  C   . GLN A 1 369 ? 6.833   7.769   77.413  1.00 22.47 ? 397 GLN A C   1 
ATOM   2680 O  O   . GLN A 1 369 ? 6.315   7.770   78.533  1.00 26.04 ? 397 GLN A O   1 
ATOM   2681 C  CB  . GLN A 1 369 ? 5.550   9.210   75.791  1.00 24.61 ? 397 GLN A CB  1 
ATOM   2682 C  CG  . GLN A 1 369 ? 6.718   10.007  75.246  1.00 26.43 ? 397 GLN A CG  1 
ATOM   2683 C  CD  . GLN A 1 369 ? 6.297   11.282  74.530  1.00 30.66 ? 397 GLN A CD  1 
ATOM   2684 O  OE1 . GLN A 1 369 ? 5.155   11.745  74.656  1.00 26.14 ? 397 GLN A OE1 1 
ATOM   2685 N  NE2 . GLN A 1 369 ? 7.230   11.854  73.765  1.00 28.54 ? 397 GLN A NE2 1 
ATOM   2686 N  N   . ARG A 1 370 ? 8.144   7.749   77.216  1.00 23.52 ? 398 ARG A N   1 
ATOM   2687 C  CA  . ARG A 1 370 ? 9.102   7.620   78.305  1.00 25.39 ? 398 ARG A CA  1 
ATOM   2688 C  C   . ARG A 1 370 ? 9.933   8.893   78.426  1.00 26.16 ? 398 ARG A C   1 
ATOM   2689 O  O   . ARG A 1 370 ? 10.332  9.473   77.416  1.00 26.59 ? 398 ARG A O   1 
ATOM   2690 C  CB  . ARG A 1 370 ? 10.019  6.425   78.066  1.00 24.21 ? 398 ARG A CB  1 
ATOM   2691 C  CG  . ARG A 1 370 ? 9.283   5.076   78.019  1.00 24.40 ? 398 ARG A CG  1 
ATOM   2692 C  CD  . ARG A 1 370 ? 10.251  3.947   77.702  1.00 25.45 ? 398 ARG A CD  1 
ATOM   2693 N  NE  . ARG A 1 370 ? 9.604   2.631   77.611  1.00 25.02 ? 398 ARG A NE  1 
ATOM   2694 C  CZ  . ARG A 1 370 ? 9.211   1.918   78.665  1.00 27.02 ? 398 ARG A CZ  1 
ATOM   2695 N  NH1 . ARG A 1 370 ? 9.365   2.402   79.888  1.00 27.03 ? 398 ARG A NH1 1 
ATOM   2696 N  NH2 . ARG A 1 370 ? 8.653   0.720   78.502  1.00 25.19 ? 398 ARG A NH2 1 
ATOM   2697 N  N   . VAL A 1 371 ? 10.193  9.309   79.664  1.00 28.23 ? 399 VAL A N   1 
ATOM   2698 C  CA  . VAL A 1 371 ? 10.956  10.526  79.965  1.00 27.64 ? 399 VAL A CA  1 
ATOM   2699 C  C   . VAL A 1 371 ? 12.169  10.126  80.797  1.00 33.23 ? 399 VAL A C   1 
ATOM   2700 O  O   . VAL A 1 371 ? 12.016  9.543   81.878  1.00 35.33 ? 399 VAL A O   1 
ATOM   2701 C  CB  . VAL A 1 371 ? 10.108  11.560  80.727  1.00 30.33 ? 399 VAL A CB  1 
ATOM   2702 C  CG1 . VAL A 1 371 ? 10.941  12.795  81.094  1.00 37.43 ? 399 VAL A CG1 1 
ATOM   2703 C  CG2 . VAL A 1 371 ? 8.880   11.935  79.939  1.00 33.10 ? 399 VAL A CG2 1 
ATOM   2704 N  N   . GLY A 1 372 ? 13.368  10.439  80.303  1.00 35.45 ? 400 GLY A N   1 
ATOM   2705 C  CA  . GLY A 1 372 ? 14.577  10.200  81.073  1.00 40.43 ? 400 GLY A CA  1 
ATOM   2706 C  C   . GLY A 1 372 ? 15.569  9.245   80.438  1.00 42.21 ? 400 GLY A C   1 
ATOM   2707 O  O   . GLY A 1 372 ? 15.494  8.961   79.237  1.00 40.38 ? 400 GLY A O   1 
ATOM   2708 N  N   . CYS A 1 373 ? 16.514  8.756   81.246  1.00 48.34 ? 401 CYS A N   1 
ATOM   2709 C  CA  . CYS A 1 373 ? 17.499  7.753   80.827  1.00 44.07 ? 401 CYS A CA  1 
ATOM   2710 C  C   . CYS A 1 373 ? 18.215  8.165   79.542  1.00 46.70 ? 401 CYS A C   1 
ATOM   2711 O  O   . CYS A 1 373 ? 18.403  7.370   78.620  1.00 47.74 ? 401 CYS A O   1 
ATOM   2712 C  CB  . CYS A 1 373 ? 16.843  6.383   80.660  1.00 46.22 ? 401 CYS A CB  1 
ATOM   2713 S  SG  . CYS A 1 373 ? 15.656  5.953   81.935  1.00 45.56 ? 401 CYS A SG  1 
ATOM   2714 N  N   . MET A 1 374 ? 18.615  9.430   79.478  1.00 50.71 ? 402 MET A N   1 
ATOM   2715 C  CA  . MET A 1 374 ? 19.308  9.931   78.303  1.00 50.92 ? 402 MET A CA  1 
ATOM   2716 C  C   . MET A 1 374 ? 20.798  9.639   78.416  1.00 53.94 ? 402 MET A C   1 
ATOM   2717 O  O   . MET A 1 374 ? 21.392  9.768   79.492  1.00 53.78 ? 402 MET A O   1 
ATOM   2718 C  CB  . MET A 1 374 ? 19.066  11.429  78.127  1.00 47.74 ? 402 MET A CB  1 
ATOM   2719 C  CG  . MET A 1 374 ? 17.600  11.770  77.917  1.00 46.69 ? 402 MET A CG  1 
ATOM   2720 S  SD  . MET A 1 374 ? 16.888  10.845  76.537  1.00 50.45 ? 402 MET A SD  1 
ATOM   2721 C  CE  . MET A 1 374 ? 17.900  11.403  75.164  1.00 42.39 ? 402 MET A CE  1 
ATOM   2722 N  N   . MET A 1 375 ? 21.387  9.216   77.302  1.00 56.06 ? 403 MET A N   1 
ATOM   2723 C  CA  . MET A 1 375 ? 22.814  8.936   77.227  1.00 56.17 ? 403 MET A CA  1 
ATOM   2724 C  C   . MET A 1 375 ? 23.417  9.668   76.037  1.00 60.70 ? 403 MET A C   1 
ATOM   2725 O  O   . MET A 1 375 ? 22.709  10.009  75.087  1.00 62.19 ? 403 MET A O   1 
ATOM   2726 C  CB  . MET A 1 375 ? 23.071  7.432   77.106  1.00 59.46 ? 403 MET A CB  1 
ATOM   2727 C  CG  . MET A 1 375 ? 22.083  6.558   77.860  1.00 58.57 ? 403 MET A CG  1 
ATOM   2728 S  SD  . MET A 1 375 ? 22.526  6.296   79.591  1.00 68.81 ? 403 MET A SD  1 
ATOM   2729 C  CE  . MET A 1 375 ? 23.982  5.266   79.412  1.00 66.03 ? 403 MET A CE  1 
ATOM   2730 N  N   . TYR A 1 383 ? 20.586  9.343   72.771  1.00 59.14 ? 411 TYR A N   1 
ATOM   2731 C  CA  . TYR A 1 383 ? 19.599  8.269   72.690  1.00 46.86 ? 411 TYR A CA  1 
ATOM   2732 C  C   . TYR A 1 383 ? 19.006  7.968   74.064  1.00 52.75 ? 411 TYR A C   1 
ATOM   2733 O  O   . TYR A 1 383 ? 19.621  8.258   75.093  1.00 52.86 ? 411 TYR A O   1 
ATOM   2734 C  CB  . TYR A 1 383 ? 20.231  7.003   72.103  1.00 57.19 ? 411 TYR A CB  1 
ATOM   2735 C  CG  . TYR A 1 383 ? 21.166  6.286   73.056  1.00 57.55 ? 411 TYR A CG  1 
ATOM   2736 C  CD1 . TYR A 1 383 ? 20.700  5.282   73.901  1.00 54.50 ? 411 TYR A CD1 1 
ATOM   2737 C  CD2 . TYR A 1 383 ? 22.515  6.616   73.115  1.00 56.62 ? 411 TYR A CD2 1 
ATOM   2738 C  CE1 . TYR A 1 383 ? 21.549  4.633   74.776  1.00 56.80 ? 411 TYR A CE1 1 
ATOM   2739 C  CE2 . TYR A 1 383 ? 23.371  5.966   73.985  1.00 56.71 ? 411 TYR A CE2 1 
ATOM   2740 C  CZ  . TYR A 1 383 ? 22.884  4.978   74.811  1.00 59.11 ? 411 TYR A CZ  1 
ATOM   2741 O  OH  . TYR A 1 383 ? 23.736  4.334   75.680  1.00 69.74 ? 411 TYR A OH  1 
ATOM   2742 N  N   . GLN A 1 384 ? 17.817  7.370   74.078  1.00 49.62 ? 412 GLN A N   1 
ATOM   2743 C  CA  . GLN A 1 384 ? 17.164  6.941   75.307  1.00 46.50 ? 412 GLN A CA  1 
ATOM   2744 C  C   . GLN A 1 384 ? 17.307  5.434   75.471  1.00 46.32 ? 412 GLN A C   1 
ATOM   2745 O  O   . GLN A 1 384 ? 17.137  4.677   74.511  1.00 47.18 ? 412 GLN A O   1 
ATOM   2746 C  CB  . GLN A 1 384 ? 15.683  7.323   75.300  1.00 40.44 ? 412 GLN A CB  1 
ATOM   2747 C  CG  . GLN A 1 384 ? 14.989  7.122   76.633  1.00 43.63 ? 412 GLN A CG  1 
ATOM   2748 C  CD  . GLN A 1 384 ? 13.526  7.547   76.602  1.00 45.50 ? 412 GLN A CD  1 
ATOM   2749 O  OE1 . GLN A 1 384 ? 13.087  8.373   77.412  1.00 42.56 ? 412 GLN A OE1 1 
ATOM   2750 N  NE2 . GLN A 1 384 ? 12.767  6.981   75.675  1.00 36.42 ? 412 GLN A NE2 1 
ATOM   2751 N  N   . SER A 1 385 ? 17.615  4.998   76.688  1.00 42.31 ? 413 SER A N   1 
ATOM   2752 C  CA  . SER A 1 385 ? 17.776  3.571   76.934  1.00 44.13 ? 413 SER A CA  1 
ATOM   2753 C  C   . SER A 1 385 ? 16.415  2.899   77.066  1.00 36.84 ? 413 SER A C   1 
ATOM   2754 O  O   . SER A 1 385 ? 15.448  3.493   77.548  1.00 35.91 ? 413 SER A O   1 
ATOM   2755 C  CB  . SER A 1 385 ? 18.597  3.325   78.197  1.00 49.00 ? 413 SER A CB  1 
ATOM   2756 O  OG  . SER A 1 385 ? 17.857  3.689   79.349  1.00 52.37 ? 413 SER A OG  1 
ATOM   2757 N  N   . GLY A 1 386 ? 16.353  1.640   76.649  1.00 37.35 ? 414 GLY A N   1 
ATOM   2758 C  CA  . GLY A 1 386 ? 15.079  0.953   76.584  1.00 32.25 ? 414 GLY A CA  1 
ATOM   2759 C  C   . GLY A 1 386 ? 14.514  0.667   77.958  1.00 36.75 ? 414 GLY A C   1 
ATOM   2760 O  O   . GLY A 1 386 ? 15.241  0.495   78.934  1.00 32.71 ? 414 GLY A O   1 
ATOM   2761 N  N   . GLY A 1 387 ? 13.183  0.615   78.023  1.00 33.71 ? 415 GLY A N   1 
ATOM   2762 C  CA  . GLY A 1 387 ? 12.517  0.348   79.277  1.00 29.29 ? 415 GLY A CA  1 
ATOM   2763 C  C   . GLY A 1 387 ? 12.559  1.466   80.286  1.00 31.26 ? 415 GLY A C   1 
ATOM   2764 O  O   . GLY A 1 387 ? 12.177  1.246   81.440  1.00 33.54 ? 415 GLY A O   1 
ATOM   2765 N  N   . CYS A 1 388 ? 12.991  2.663   79.884  1.00 31.16 ? 416 CYS A N   1 
ATOM   2766 C  CA  . CYS A 1 388 ? 13.122  3.805   80.785  1.00 32.87 ? 416 CYS A CA  1 
ATOM   2767 C  C   . CYS A 1 388 ? 11.839  4.128   81.536  1.00 34.35 ? 416 CYS A C   1 
ATOM   2768 O  O   . CYS A 1 388 ? 10.883  4.651   80.952  1.00 32.52 ? 416 CYS A O   1 
ATOM   2769 C  CB  . CYS A 1 388 ? 13.560  5.045   80.007  1.00 33.91 ? 416 CYS A CB  1 
ATOM   2770 S  SG  . CYS A 1 388 ? 13.861  6.458   81.097  1.00 41.07 ? 416 CYS A SG  1 
ATOM   2771 N  N   . GLY A 1 389 ? 11.821  3.868   82.840  1.00 33.21 ? 417 GLY A N   1 
ATOM   2772 C  CA  . GLY A 1 389 ? 10.647  4.101   83.652  1.00 33.35 ? 417 GLY A CA  1 
ATOM   2773 C  C   . GLY A 1 389 ? 9.871   2.844   83.980  1.00 37.10 ? 417 GLY A C   1 
ATOM   2774 O  O   . GLY A 1 389 ? 8.994   2.884   84.852  1.00 35.23 ? 417 GLY A O   1 
ATOM   2775 N  N   . GLY A 1 390 ? 10.183  1.731   83.315  1.00 32.67 ? 418 GLY A N   1 
ATOM   2776 C  CA  . GLY A 1 390 ? 9.534   0.462   83.589  1.00 29.72 ? 418 GLY A CA  1 
ATOM   2777 C  C   . GLY A 1 390 ? 8.304   0.220   82.738  1.00 31.85 ? 418 GLY A C   1 
ATOM   2778 O  O   . GLY A 1 390 ? 8.241   0.650   81.585  1.00 29.58 ? 418 GLY A O   1 
ATOM   2779 N  N   . PHE A 1 391 ? 7.315   -0.473  83.304  1.00 30.56 ? 419 PHE A N   1 
ATOM   2780 C  CA  . PHE A 1 391 ? 6.141   -0.901  82.551  1.00 26.85 ? 419 PHE A CA  1 
ATOM   2781 C  C   . PHE A 1 391 ? 4.840   -0.510  83.236  1.00 33.17 ? 419 PHE A C   1 
ATOM   2782 O  O   . PHE A 1 391 ? 3.755   -0.866  82.746  1.00 30.47 ? 419 PHE A O   1 
ATOM   2783 C  CB  . PHE A 1 391 ? 6.229   -2.412  82.299  1.00 27.21 ? 419 PHE A CB  1 
ATOM   2784 C  CG  . PHE A 1 391 ? 7.479   -2.795  81.546  1.00 26.14 ? 419 PHE A CG  1 
ATOM   2785 C  CD1 . PHE A 1 391 ? 8.660   -3.060  82.223  1.00 26.74 ? 419 PHE A CD1 1 
ATOM   2786 C  CD2 . PHE A 1 391 ? 7.493   -2.797  80.156  1.00 27.16 ? 419 PHE A CD2 1 
ATOM   2787 C  CE1 . PHE A 1 391 ? 9.818   -3.357  81.534  1.00 26.63 ? 419 PHE A CE1 1 
ATOM   2788 C  CE2 . PHE A 1 391 ? 8.653   -3.100  79.458  1.00 25.84 ? 419 PHE A CE2 1 
ATOM   2789 C  CZ  . PHE A 1 391 ? 9.819   -3.382  80.153  1.00 28.85 ? 419 PHE A CZ  1 
ATOM   2790 N  N   . GLY A 1 392 ? 4.912   0.246   84.328  1.00 32.76 ? 420 GLY A N   1 
ATOM   2791 C  CA  . GLY A 1 392 ? 3.718   0.749   84.968  1.00 31.60 ? 420 GLY A CA  1 
ATOM   2792 C  C   . GLY A 1 392 ? 3.144   -0.134  86.044  1.00 38.55 ? 420 GLY A C   1 
ATOM   2793 O  O   . GLY A 1 392 ? 1.957   -0.007  86.362  1.00 38.27 ? 420 GLY A O   1 
ATOM   2794 N  N   . LYS A 1 393 ? 3.943   -1.025  86.627  1.00 35.40 ? 421 LYS A N   1 
ATOM   2795 C  CA  . LYS A 1 393 ? 3.388   -1.909  87.641  1.00 44.30 ? 421 LYS A CA  1 
ATOM   2796 C  C   . LYS A 1 393 ? 2.955   -1.150  88.893  1.00 43.51 ? 421 LYS A C   1 
ATOM   2797 O  O   . LYS A 1 393 ? 2.088   -1.636  89.625  1.00 48.23 ? 421 LYS A O   1 
ATOM   2798 C  CB  . LYS A 1 393 ? 4.387   -3.013  87.992  1.00 41.79 ? 421 LYS A CB  1 
ATOM   2799 C  CG  . LYS A 1 393 ? 4.353   -4.168  86.973  1.00 46.59 ? 421 LYS A CG  1 
ATOM   2800 C  CD  . LYS A 1 393 ? 4.958   -5.471  87.519  1.00 51.69 ? 421 LYS A CD  1 
ATOM   2801 C  CE  . LYS A 1 393 ? 3.866   -6.574  87.576  1.00 51.37 ? 421 LYS A CE  1 
ATOM   2802 N  NZ  . LYS A 1 393 ? 4.080   -7.559  88.653  1.00 57.89 ? 421 LYS A NZ  1 
ATOM   2803 N  N   . GLY A 1 394 ? 3.512   0.039   89.139  1.00 43.61 ? 422 GLY A N   1 
ATOM   2804 C  CA  . GLY A 1 394 ? 3.078   0.843   90.267  1.00 41.22 ? 422 GLY A CA  1 
ATOM   2805 C  C   . GLY A 1 394 ? 1.674   1.390   90.127  1.00 48.13 ? 422 GLY A C   1 
ATOM   2806 O  O   . GLY A 1 394 ? 1.087   1.823   91.124  1.00 47.47 ? 422 GLY A O   1 
ATOM   2807 N  N   . ASN A 1 395 ? 1.119   1.379   88.912  1.00 43.52 ? 423 ASN A N   1 
ATOM   2808 C  CA  . ASN A 1 395 ? -0.207  1.935   88.687  1.00 44.44 ? 423 ASN A CA  1 
ATOM   2809 C  C   . ASN A 1 395 ? -1.328  0.986   89.087  1.00 44.25 ? 423 ASN A C   1 
ATOM   2810 O  O   . ASN A 1 395 ? -2.474  1.428   89.186  1.00 47.22 ? 423 ASN A O   1 
ATOM   2811 C  CB  . ASN A 1 395 ? -0.368  2.348   87.223  1.00 40.64 ? 423 ASN A CB  1 
ATOM   2812 C  CG  . ASN A 1 395 ? 0.031   3.794   86.979  1.00 38.95 ? 423 ASN A CG  1 
ATOM   2813 O  OD1 . ASN A 1 395 ? -0.268  4.679   87.785  1.00 38.97 ? 423 ASN A OD1 1 
ATOM   2814 N  ND2 . ASN A 1 395 ? 0.695   4.043   85.859  1.00 38.07 ? 423 ASN A ND2 1 
ATOM   2815 N  N   . PHE A 1 396 ? -1.036  -0.295  89.320  1.00 43.23 ? 424 PHE A N   1 
ATOM   2816 C  CA  . PHE A 1 396 ? -2.030  -1.175  89.927  1.00 48.15 ? 424 PHE A CA  1 
ATOM   2817 C  C   . PHE A 1 396 ? -2.422  -0.671  91.312  1.00 50.05 ? 424 PHE A C   1 
ATOM   2818 O  O   . PHE A 1 396 ? -3.593  -0.378  91.579  1.00 47.46 ? 424 PHE A O   1 
ATOM   2819 C  CB  . PHE A 1 396 ? -1.492  -2.605  90.013  1.00 48.59 ? 424 PHE A CB  1 
ATOM   2820 C  CG  . PHE A 1 396 ? -1.354  -3.291  88.680  1.00 48.59 ? 424 PHE A CG  1 
ATOM   2821 C  CD1 . PHE A 1 396 ? -0.121  -3.378  88.057  1.00 46.81 ? 424 PHE A CD1 1 
ATOM   2822 C  CD2 . PHE A 1 396 ? -2.459  -3.841  88.050  1.00 47.62 ? 424 PHE A CD2 1 
ATOM   2823 C  CE1 . PHE A 1 396 ? 0.009   -4.010  86.834  1.00 45.26 ? 424 PHE A CE1 1 
ATOM   2824 C  CE2 . PHE A 1 396 ? -2.335  -4.470  86.818  1.00 48.05 ? 424 PHE A CE2 1 
ATOM   2825 C  CZ  . PHE A 1 396 ? -1.098  -4.555  86.213  1.00 41.28 ? 424 PHE A CZ  1 
ATOM   2826 N  N   . SER A 1 397 ? -1.439  -0.554  92.207  1.00 52.63 ? 425 SER A N   1 
ATOM   2827 C  CA  . SER A 1 397 ? -1.713  -0.071  93.556  1.00 54.85 ? 425 SER A CA  1 
ATOM   2828 C  C   . SER A 1 397 ? -2.201  1.373   93.543  1.00 52.23 ? 425 SER A C   1 
ATOM   2829 O  O   . SER A 1 397 ? -3.172  1.713   94.228  1.00 55.73 ? 425 SER A O   1 
ATOM   2830 C  CB  . SER A 1 397 ? -0.462  -0.209  94.419  1.00 55.70 ? 425 SER A CB  1 
ATOM   2831 O  OG  . SER A 1 397 ? 0.359   0.935   94.304  1.00 60.58 ? 425 SER A OG  1 
ATOM   2832 N  N   . GLU A 1 398 ? -1.554  2.236   92.758  1.00 52.88 ? 426 GLU A N   1 
ATOM   2833 C  CA  . GLU A 1 398 ? -1.920  3.647   92.788  1.00 53.06 ? 426 GLU A CA  1 
ATOM   2834 C  C   . GLU A 1 398 ? -3.311  3.882   92.217  1.00 55.68 ? 426 GLU A C   1 
ATOM   2835 O  O   . GLU A 1 398 ? -4.020  4.776   92.688  1.00 55.93 ? 426 GLU A O   1 
ATOM   2836 C  CB  . GLU A 1 398 ? -0.876  4.484   92.047  1.00 53.22 ? 426 GLU A CB  1 
ATOM   2837 C  CG  . GLU A 1 398 ? 0.464   4.536   92.763  1.00 52.96 ? 426 GLU A CG  1 
ATOM   2838 C  CD  . GLU A 1 398 ? 0.423   5.414   94.002  1.00 56.02 ? 426 GLU A CD  1 
ATOM   2839 O  OE1 . GLU A 1 398 ? -0.469  6.283   94.092  1.00 54.92 ? 426 GLU A OE1 1 
ATOM   2840 O  OE2 . GLU A 1 398 ? 1.272   5.222   94.897  1.00 60.64 ? 426 GLU A OE2 1 
ATOM   2841 N  N   . LEU A 1 399 ? -3.734  3.085   91.232  1.00 53.54 ? 427 LEU A N   1 
ATOM   2842 C  CA  . LEU A 1 399 ? -5.115  3.178   90.766  1.00 55.71 ? 427 LEU A CA  1 
ATOM   2843 C  C   . LEU A 1 399 ? -6.084  2.728   91.848  1.00 55.97 ? 427 LEU A C   1 
ATOM   2844 O  O   . LEU A 1 399 ? -7.099  3.388   92.098  1.00 58.85 ? 427 LEU A O   1 
ATOM   2845 C  CB  . LEU A 1 399 ? -5.318  2.346   89.501  1.00 50.89 ? 427 LEU A CB  1 
ATOM   2846 C  CG  . LEU A 1 399 ? -5.388  3.101   88.180  1.00 56.53 ? 427 LEU A CG  1 
ATOM   2847 C  CD1 . LEU A 1 399 ? -5.463  2.121   87.021  1.00 55.09 ? 427 LEU A CD1 1 
ATOM   2848 C  CD2 . LEU A 1 399 ? -6.586  4.045   88.165  1.00 52.12 ? 427 LEU A CD2 1 
ATOM   2849 N  N   . PHE A 1 400 ? -5.787  1.598   92.496  1.00 57.73 ? 428 PHE A N   1 
ATOM   2850 C  CA  . PHE A 1 400 ? -6.653  1.088   93.554  1.00 57.91 ? 428 PHE A CA  1 
ATOM   2851 C  C   . PHE A 1 400 ? -6.828  2.116   94.666  1.00 62.99 ? 428 PHE A C   1 
ATOM   2852 O  O   . PHE A 1 400 ? -7.957  2.460   95.037  1.00 65.28 ? 428 PHE A O   1 
ATOM   2853 C  CB  . PHE A 1 400 ? -6.079  -0.218  94.104  1.00 53.42 ? 428 PHE A CB  1 
ATOM   2854 N  N   . LYS A 1 401 ? -5.714  2.616   95.212  1.00 60.78 ? 429 LYS A N   1 
ATOM   2855 C  CA  . LYS A 1 401 ? -5.775  3.676   96.218  1.00 63.22 ? 429 LYS A CA  1 
ATOM   2856 C  C   . LYS A 1 401 ? -6.551  4.878   95.698  1.00 65.33 ? 429 LYS A C   1 
ATOM   2857 O  O   . LYS A 1 401 ? -7.497  5.348   96.334  1.00 65.46 ? 429 LYS A O   1 
ATOM   2858 C  CB  . LYS A 1 401 ? -4.362  4.093   96.634  1.00 59.64 ? 429 LYS A CB  1 
ATOM   2859 N  N   . SER A 1 402 ? -6.153  5.386   94.534  1.00 63.39 ? 430 SER A N   1 
ATOM   2860 C  CA  . SER A 1 402 ? -6.893  6.462   93.891  1.00 60.96 ? 430 SER A CA  1 
ATOM   2861 C  C   . SER A 1 402 ? -8.400  6.201   93.877  1.00 67.33 ? 430 SER A C   1 
ATOM   2862 O  O   . SER A 1 402 ? -9.193  7.122   94.112  1.00 64.98 ? 430 SER A O   1 
ATOM   2863 C  CB  . SER A 1 402 ? -6.346  6.656   92.494  1.00 60.59 ? 430 SER A CB  1 
ATOM   2864 O  OG  . SER A 1 402 ? -7.323  7.061   91.564  1.00 57.48 ? 430 SER A OG  1 
ATOM   2865 N  N   . ILE A 1 403 ? -8.824  4.953   93.651  1.00 65.85 ? 431 ILE A N   1 
ATOM   2866 C  CA  . ILE A 1 403 ? -10.248 4.656   93.495  1.00 66.89 ? 431 ILE A CA  1 
ATOM   2867 C  C   . ILE A 1 403 ? -10.952 4.705   94.845  1.00 70.98 ? 431 ILE A C   1 
ATOM   2868 O  O   . ILE A 1 403 ? -12.055 5.246   94.965  1.00 71.58 ? 431 ILE A O   1 
ATOM   2869 C  CB  . ILE A 1 403 ? -10.432 3.292   92.799  1.00 66.50 ? 431 ILE A CB  1 
ATOM   2870 C  CG1 . ILE A 1 403 ? -10.248 3.454   91.288  1.00 62.39 ? 431 ILE A CG1 1 
ATOM   2871 C  CG2 . ILE A 1 403 ? -11.809 2.680   93.144  1.00 63.90 ? 431 ILE A CG2 1 
ATOM   2872 C  CD1 . ILE A 1 403 ? -10.091 2.150   90.557  1.00 60.01 ? 431 ILE A CD1 1 
ATOM   2873 N  N   . GLU A 1 404 ? -10.323 4.134   95.880  1.00 68.92 ? 432 GLU A N   1 
ATOM   2874 C  CA  . GLU A 1 404 ? -10.907 4.147   97.219  1.00 73.92 ? 432 GLU A CA  1 
ATOM   2875 C  C   . GLU A 1 404 ? -11.000 5.566   97.774  1.00 72.69 ? 432 GLU A C   1 
ATOM   2876 O  O   . GLU A 1 404 ? -12.012 5.937   98.379  1.00 75.10 ? 432 GLU A O   1 
ATOM   2877 C  CB  . GLU A 1 404 ? -10.084 3.253   98.148  1.00 69.30 ? 432 GLU A CB  1 
ATOM   2878 N  N   . GLU A 1 405 ? -9.954  6.373   97.573  1.00 72.49 ? 433 GLU A N   1 
ATOM   2879 C  CA  . GLU A 1 405 ? -9.986  7.760   98.027  1.00 72.38 ? 433 GLU A CA  1 
ATOM   2880 C  C   . GLU A 1 405 ? -11.143 8.530   97.403  1.00 75.32 ? 433 GLU A C   1 
ATOM   2881 O  O   . GLU A 1 405 ? -11.686 9.449   98.029  1.00 75.96 ? 433 GLU A O   1 
ATOM   2882 C  CB  . GLU A 1 405 ? -8.657  8.443   97.706  1.00 67.52 ? 433 GLU A CB  1 
ATOM   2883 N  N   . TYR A 1 406 ? -11.547 8.165   96.184  1.00 73.02 ? 434 TYR A N   1 
ATOM   2884 C  CA  . TYR A 1 406 ? -12.602 8.908   95.508  1.00 71.18 ? 434 TYR A CA  1 
ATOM   2885 C  C   . TYR A 1 406 ? -13.994 8.482   95.957  1.00 77.63 ? 434 TYR A C   1 
ATOM   2886 O  O   . TYR A 1 406 ? -14.913 9.309   95.964  1.00 79.88 ? 434 TYR A O   1 
ATOM   2887 C  CB  . TYR A 1 406 ? -12.472 8.752   93.995  1.00 67.95 ? 434 TYR A CB  1 
ATOM   2888 C  CG  . TYR A 1 406 ? -13.457 9.607   93.247  1.00 65.98 ? 434 TYR A CG  1 
ATOM   2889 C  CD1 . TYR A 1 406 ? -13.375 10.990  93.297  1.00 65.24 ? 434 TYR A CD1 1 
ATOM   2890 C  CD2 . TYR A 1 406 ? -14.480 9.034   92.506  1.00 68.07 ? 434 TYR A CD2 1 
ATOM   2891 C  CE1 . TYR A 1 406 ? -14.279 11.780  92.626  1.00 65.96 ? 434 TYR A CE1 1 
ATOM   2892 C  CE2 . TYR A 1 406 ? -15.390 9.817   91.826  1.00 67.23 ? 434 TYR A CE2 1 
ATOM   2893 C  CZ  . TYR A 1 406 ? -15.284 11.190  91.890  1.00 68.61 ? 434 TYR A CZ  1 
ATOM   2894 O  OH  . TYR A 1 406 ? -16.190 11.982  91.220  1.00 71.02 ? 434 TYR A OH  1 
ATOM   2895 N  N   . GLU A 1 407 ? -14.179 7.209   96.316  1.00 77.54 ? 435 GLU A N   1 
ATOM   2896 C  CA  . GLU A 1 407 ? -15.429 6.800   96.947  1.00 78.21 ? 435 GLU A CA  1 
ATOM   2897 C  C   . GLU A 1 407 ? -15.716 7.666   98.168  1.00 79.55 ? 435 GLU A C   1 
ATOM   2898 O  O   . GLU A 1 407 ? -16.783 8.282   98.276  1.00 81.57 ? 435 GLU A O   1 
ATOM   2899 C  CB  . GLU A 1 407 ? -15.367 5.322   97.329  1.00 73.89 ? 435 GLU A CB  1 
ATOM   2900 N  N   . LYS A 1 408 ? -14.758 7.748   99.084  1.00 79.32 ? 436 LYS A N   1 
ATOM   2901 C  CA  . LYS A 1 408 ? -14.879 8.624   100.242 1.00 79.57 ? 436 LYS A CA  1 
ATOM   2902 C  C   . LYS A 1 408 ? -14.338 10.017  99.924  1.00 80.44 ? 436 LYS A C   1 
ATOM   2903 O  O   . LYS A 1 408 ? -15.027 10.845  99.319  1.00 77.74 ? 436 LYS A O   1 
ATOM   2904 C  CB  . LYS A 1 408 ? -14.143 8.023   101.444 1.00 78.72 ? 436 LYS A CB  1 
HETATM 2905 CO CO  . CO  B 2 .   ? 2.887   -2.639  78.928  1.00 25.91 ? 501 CO  A CO  1 
HETATM 2906 C  C13 . YDF C 3 .   ? 1.469   -3.389  81.557  1.00 29.91 ? 502 YDF A C13 1 
HETATM 2907 C  C17 . YDF C 3 .   ? 4.592   -5.807  81.722  1.00 27.87 ? 502 YDF A C17 1 
HETATM 2908 C  C20 . YDF C 3 .   ? 1.894   -5.531  83.013  1.00 32.14 ? 502 YDF A C20 1 
HETATM 2909 C  C24 . YDF C 3 .   ? -5.878  -3.961  82.633  1.00 39.71 ? 502 YDF A C24 1 
HETATM 2910 C  C26 . YDF C 3 .   ? -2.626  0.076   85.569  1.00 53.38 ? 502 YDF A C26 1 
HETATM 2911 C  C01 . YDF C 3 .   ? 0.265   -2.929  82.330  1.00 27.79 ? 502 YDF A C01 1 
HETATM 2912 C  C02 . YDF C 3 .   ? 0.551   -1.798  83.286  1.00 34.79 ? 502 YDF A C02 1 
HETATM 2913 C  C03 . YDF C 3 .   ? -0.621  -1.239  84.038  1.00 35.91 ? 502 YDF A C03 1 
HETATM 2914 C  C04 . YDF C 3 .   ? -2.020  -1.823  83.818  1.00 38.07 ? 502 YDF A C04 1 
HETATM 2915 C  C05 . YDF C 3 .   ? -2.381  -2.930  82.855  1.00 36.07 ? 502 YDF A C05 1 
HETATM 2916 C  C06 . YDF C 3 .   ? -1.131  -3.503  82.066  1.00 33.08 ? 502 YDF A C06 1 
HETATM 2917 C  C08 . YDF C 3 .   ? -4.800  -1.281  84.763  1.00 54.73 ? 502 YDF A C08 1 
HETATM 2918 C  C09 . YDF C 3 .   ? -5.368  -2.408  83.941  1.00 56.91 ? 502 YDF A C09 1 
HETATM 2919 C  C11 . YDF C 3 .   ? -3.599  -3.410  82.682  1.00 42.05 ? 502 YDF A C11 1 
HETATM 2920 C  C12 . YDF C 3 .   ? -1.159  -4.636  81.034  1.00 29.41 ? 502 YDF A C12 1 
HETATM 2921 C  C14 . YDF C 3 .   ? 2.332   -4.554  81.940  1.00 25.98 ? 502 YDF A C14 1 
HETATM 2922 C  C16 . YDF C 3 .   ? 3.556   -4.879  81.106  1.00 28.38 ? 502 YDF A C16 1 
HETATM 2923 C  C18 . YDF C 3 .   ? 4.383   -6.002  83.223  1.00 29.32 ? 502 YDF A C18 1 
HETATM 2924 C  C19 . YDF C 3 .   ? 2.967   -6.456  83.585  1.00 31.57 ? 502 YDF A C19 1 
HETATM 2925 C  C27 . YDF C 3 .   ? -6.408  -3.628  81.223  1.00 37.89 ? 502 YDF A C27 1 
HETATM 2926 F  F28 . YDF C 3 .   ? -6.112  -2.377  80.754  1.00 38.83 ? 502 YDF A F28 1 
HETATM 2927 N  N07 . YDF C 3 .   ? -3.144  -1.008  84.755  1.00 36.62 ? 502 YDF A N07 1 
HETATM 2928 N  N10 . YDF C 3 .   ? -4.827  -3.097  83.168  1.00 46.34 ? 502 YDF A N10 1 
HETATM 2929 O  O15 . YDF C 3 .   ? 1.734   -2.743  80.591  1.00 26.16 ? 502 YDF A O15 1 
HETATM 2930 O  O21 . YDF C 3 .   ? 3.849   -4.162  79.948  1.00 23.53 ? 502 YDF A O21 1 
HETATM 2931 O  O22 . YDF C 3 .   ? 0.768   -5.572  83.385  1.00 32.49 ? 502 YDF A O22 1 
HETATM 2932 O  O23 . YDF C 3 .   ? -3.676  -4.309  81.927  1.00 41.03 ? 502 YDF A O23 1 
HETATM 2933 O  O25 . YDF C 3 .   ? -5.486  -0.615  85.454  1.00 62.58 ? 502 YDF A O25 1 
HETATM 2934 O  O   . HOH D 4 .   ? 8.072   -12.571 49.213  1.00 39.35 ? 601 HOH A O   1 
HETATM 2935 O  O   . HOH D 4 .   ? 7.642   -3.566  49.867  1.00 52.34 ? 602 HOH A O   1 
HETATM 2936 O  O   . HOH D 4 .   ? 2.627   -10.393 46.172  1.00 27.79 ? 603 HOH A O   1 
HETATM 2937 O  O   . HOH D 4 .   ? 18.227  -5.291  70.560  1.00 34.38 ? 604 HOH A O   1 
HETATM 2938 O  O   . HOH D 4 .   ? -13.499 12.501  98.560  1.00 66.30 ? 605 HOH A O   1 
HETATM 2939 O  O   . HOH D 4 .   ? 3.382   16.270  67.515  1.00 36.36 ? 606 HOH A O   1 
HETATM 2940 O  O   . HOH D 4 .   ? 15.454  -2.970  62.917  1.00 44.74 ? 607 HOH A O   1 
HETATM 2941 O  O   . HOH D 4 .   ? -9.130  6.644   79.925  1.00 38.60 ? 608 HOH A O   1 
HETATM 2942 O  O   . HOH D 4 .   ? 2.659   11.963  57.477  1.00 45.90 ? 609 HOH A O   1 
HETATM 2943 O  O   . HOH D 4 .   ? 21.820  -8.959  70.215  1.00 34.74 ? 610 HOH A O   1 
HETATM 2944 O  O   . HOH D 4 .   ? 3.607   -23.168 64.458  1.00 45.98 ? 611 HOH A O   1 
HETATM 2945 O  O   . HOH D 4 .   ? -14.459 -14.496 68.647  1.00 33.21 ? 612 HOH A O   1 
HETATM 2946 O  O   . HOH D 4 .   ? -11.805 -21.316 77.105  1.00 35.93 ? 613 HOH A O   1 
HETATM 2947 O  O   . HOH D 4 .   ? 17.855  -0.177  79.075  1.00 38.65 ? 614 HOH A O   1 
HETATM 2948 O  O   . HOH D 4 .   ? 0.930   -22.049 47.590  1.00 37.04 ? 615 HOH A O   1 
HETATM 2949 O  O   . HOH D 4 .   ? -2.699  7.150   93.132  1.00 54.92 ? 616 HOH A O   1 
HETATM 2950 O  O   . HOH D 4 .   ? 20.742  -10.590 76.923  1.00 33.77 ? 617 HOH A O   1 
HETATM 2951 O  O   . HOH D 4 .   ? -10.883 -12.798 53.969  1.00 29.59 ? 618 HOH A O   1 
HETATM 2952 O  O   . HOH D 4 .   ? 11.944  1.082   75.242  1.00 27.71 ? 619 HOH A O   1 
HETATM 2953 O  O   . HOH D 4 .   ? 3.168   -13.006 45.172  1.00 32.67 ? 620 HOH A O   1 
HETATM 2954 O  O   . HOH D 4 .   ? 3.634   -22.774 54.710  1.00 35.43 ? 621 HOH A O   1 
HETATM 2955 O  O   . HOH D 4 .   ? 1.376   -14.775 56.932  1.00 21.02 ? 622 HOH A O   1 
HETATM 2956 O  O   . HOH D 4 .   ? 3.954   -0.903  80.148  1.00 24.14 ? 623 HOH A O   1 
HETATM 2957 O  O   . HOH D 4 .   ? -5.706  -19.644 47.737  1.00 25.30 ? 624 HOH A O   1 
HETATM 2958 O  O   . HOH D 4 .   ? 14.550  1.789   84.077  1.00 46.20 ? 625 HOH A O   1 
HETATM 2959 O  O   . HOH D 4 .   ? -1.986  -18.181 70.856  1.00 21.95 ? 626 HOH A O   1 
HETATM 2960 O  O   . HOH D 4 .   ? -7.605  -8.819  48.675  1.00 25.31 ? 627 HOH A O   1 
HETATM 2961 O  O   . HOH D 4 .   ? 5.543   -20.563 86.763  1.00 41.26 ? 628 HOH A O   1 
HETATM 2962 O  O   . HOH D 4 .   ? 25.482  -18.241 70.037  1.00 41.78 ? 629 HOH A O   1 
HETATM 2963 O  O   . HOH D 4 .   ? -8.713  -12.579 70.296  1.00 26.38 ? 630 HOH A O   1 
HETATM 2964 O  O   . HOH D 4 .   ? 2.856   -16.794 58.079  1.00 23.67 ? 631 HOH A O   1 
HETATM 2965 O  O   . HOH D 4 .   ? 8.139   19.351  82.614  1.00 48.46 ? 632 HOH A O   1 
HETATM 2966 O  O   . HOH D 4 .   ? 13.663  12.187  78.312  1.00 40.67 ? 633 HOH A O   1 
HETATM 2967 O  O   . HOH D 4 .   ? 6.889   1.494   85.990  1.00 36.52 ? 634 HOH A O   1 
HETATM 2968 O  O   . HOH D 4 .   ? 9.087   13.863  71.986  1.00 31.38 ? 635 HOH A O   1 
HETATM 2969 O  O   . HOH D 4 .   ? -5.442  -4.197  46.213  1.00 33.44 ? 636 HOH A O   1 
HETATM 2970 O  O   . HOH D 4 .   ? 6.267   -11.289 75.228  1.00 24.58 ? 637 HOH A O   1 
HETATM 2971 O  O   . HOH D 4 .   ? -13.296 -11.797 53.615  1.00 21.74 ? 638 HOH A O   1 
HETATM 2972 O  O   . HOH D 4 .   ? -5.768  4.852   55.480  1.00 33.00 ? 639 HOH A O   1 
HETATM 2973 O  O   . HOH D 4 .   ? 17.875  -6.906  51.017  1.00 42.58 ? 640 HOH A O   1 
HETATM 2974 O  O   . HOH D 4 .   ? -13.488 -24.269 71.946  1.00 35.83 ? 641 HOH A O   1 
HETATM 2975 O  O   . HOH D 4 .   ? 11.812  -1.096  73.143  1.00 24.47 ? 642 HOH A O   1 
HETATM 2976 O  O   . HOH D 4 .   ? -16.436 3.649   66.993  1.00 27.00 ? 643 HOH A O   1 
HETATM 2977 O  O   . HOH D 4 .   ? 5.171   -20.848 60.960  1.00 30.86 ? 644 HOH A O   1 
HETATM 2978 O  O   . HOH D 4 .   ? 2.005   7.625   60.515  1.00 31.40 ? 645 HOH A O   1 
HETATM 2979 O  O   . HOH D 4 .   ? -16.251 8.840   72.662  1.00 47.81 ? 646 HOH A O   1 
HETATM 2980 O  O   . HOH D 4 .   ? -10.429 -15.474 55.435  1.00 26.68 ? 647 HOH A O   1 
HETATM 2981 O  O   . HOH D 4 .   ? -14.907 -1.119  73.002  1.00 37.26 ? 648 HOH A O   1 
HETATM 2982 O  O   . HOH D 4 .   ? 3.257   -18.010 60.508  1.00 24.71 ? 649 HOH A O   1 
HETATM 2983 O  O   . HOH D 4 .   ? -9.619  -8.146  71.427  1.00 22.55 ? 650 HOH A O   1 
HETATM 2984 O  O   . HOH D 4 .   ? -10.712 11.826  85.611  1.00 55.93 ? 651 HOH A O   1 
HETATM 2985 O  O   . HOH D 4 .   ? 28.047  -8.692  64.362  1.00 39.60 ? 652 HOH A O   1 
HETATM 2986 O  O   . HOH D 4 .   ? -14.879 -13.967 74.033  1.00 24.18 ? 653 HOH A O   1 
HETATM 2987 O  O   . HOH D 4 .   ? -4.544  -24.081 48.184  1.00 33.87 ? 654 HOH A O   1 
HETATM 2988 O  O   . HOH D 4 .   ? -9.010  5.785   67.792  1.00 20.26 ? 655 HOH A O   1 
HETATM 2989 O  O   . HOH D 4 .   ? -6.973  5.655   81.562  1.00 38.43 ? 656 HOH A O   1 
HETATM 2990 O  O   . HOH D 4 .   ? 11.220  -0.582  68.405  1.00 26.48 ? 657 HOH A O   1 
HETATM 2991 O  O   . HOH D 4 .   ? -14.921 13.573  67.827  1.00 37.49 ? 658 HOH A O   1 
HETATM 2992 O  O   . HOH D 4 .   ? 14.766  -27.406 69.538  1.00 39.23 ? 659 HOH A O   1 
HETATM 2993 O  O   . HOH D 4 .   ? 13.038  -2.640  69.003  1.00 27.31 ? 660 HOH A O   1 
HETATM 2994 O  O   . HOH D 4 .   ? -7.386  4.285   83.647  1.00 43.52 ? 661 HOH A O   1 
HETATM 2995 O  O   . HOH D 4 .   ? 4.557   5.992   57.255  1.00 40.07 ? 662 HOH A O   1 
HETATM 2996 O  O   . HOH D 4 .   ? -12.540 -2.239  69.961  1.00 25.32 ? 663 HOH A O   1 
HETATM 2997 O  O   . HOH D 4 .   ? -11.024 -24.135 66.513  1.00 42.98 ? 664 HOH A O   1 
HETATM 2998 O  O   . HOH D 4 .   ? 9.887   -18.650 56.895  1.00 41.74 ? 665 HOH A O   1 
HETATM 2999 O  O   . HOH D 4 .   ? 14.640  -23.183 75.437  1.00 33.67 ? 666 HOH A O   1 
HETATM 3000 O  O   . HOH D 4 .   ? -12.164 8.169   73.955  1.00 31.74 ? 667 HOH A O   1 
HETATM 3001 O  O   . HOH D 4 .   ? 4.721   8.158   59.635  1.00 42.60 ? 668 HOH A O   1 
HETATM 3002 O  O   . HOH D 4 .   ? -3.284  5.494   54.406  1.00 26.80 ? 669 HOH A O   1 
HETATM 3003 O  O   . HOH D 4 .   ? -1.811  -13.805 70.073  1.00 20.68 ? 670 HOH A O   1 
HETATM 3004 O  O   . HOH D 4 .   ? 25.631  -11.423 73.108  1.00 35.85 ? 671 HOH A O   1 
HETATM 3005 O  O   . HOH D 4 .   ? -15.196 9.811   69.175  1.00 32.71 ? 672 HOH A O   1 
HETATM 3006 O  O   . HOH D 4 .   ? 2.015   -25.294 40.258  1.00 50.17 ? 673 HOH A O   1 
HETATM 3007 O  O   . HOH D 4 .   ? -1.256  -28.804 44.724  1.00 46.25 ? 674 HOH A O   1 
HETATM 3008 O  O   . HOH D 4 .   ? 18.992  -7.283  58.833  1.00 36.83 ? 675 HOH A O   1 
HETATM 3009 O  O   . HOH D 4 .   ? 11.429  -0.860  65.886  1.00 30.04 ? 676 HOH A O   1 
HETATM 3010 O  O   . HOH D 4 .   ? 19.347  -12.587 52.969  1.00 45.20 ? 677 HOH A O   1 
HETATM 3011 O  O   . HOH D 4 .   ? -5.886  -12.666 70.870  1.00 30.26 ? 678 HOH A O   1 
HETATM 3012 O  O   . HOH D 4 .   ? 3.696   -20.919 68.565  1.00 29.33 ? 679 HOH A O   1 
HETATM 3013 O  O   . HOH D 4 .   ? -8.491  -3.475  77.898  1.00 30.52 ? 680 HOH A O   1 
HETATM 3014 O  O   . HOH D 4 .   ? 3.403   -21.511 80.012  1.00 50.81 ? 681 HOH A O   1 
HETATM 3015 O  O   . HOH D 4 .   ? -9.175  -9.013  68.792  1.00 26.12 ? 682 HOH A O   1 
HETATM 3016 O  O   . HOH D 4 .   ? -12.153 -16.960 54.588  1.00 32.60 ? 683 HOH A O   1 
HETATM 3017 O  O   . HOH D 4 .   ? -15.411 14.710  91.675  1.00 58.34 ? 684 HOH A O   1 
HETATM 3018 O  O   . HOH D 4 .   ? -12.970 5.687   75.101  1.00 33.79 ? 685 HOH A O   1 
HETATM 3019 O  O   . HOH D 4 .   ? -3.870  -0.185  45.999  1.00 44.94 ? 686 HOH A O   1 
HETATM 3020 O  O   . HOH D 4 .   ? 6.874   -23.099 56.667  1.00 37.81 ? 687 HOH A O   1 
HETATM 3021 O  O   . HOH D 4 .   ? -6.866  3.239   51.528  1.00 40.64 ? 688 HOH A O   1 
HETATM 3022 O  O   . HOH D 4 .   ? 20.089  -15.179 56.183  1.00 41.39 ? 689 HOH A O   1 
HETATM 3023 O  O   . HOH D 4 .   ? -7.244  -8.764  78.330  1.00 31.94 ? 690 HOH A O   1 
HETATM 3024 O  O   . HOH D 4 .   ? 21.743  -4.341  68.343  1.00 42.49 ? 691 HOH A O   1 
HETATM 3025 O  O   . HOH D 4 .   ? 0.157   7.454   64.642  1.00 19.58 ? 692 HOH A O   1 
HETATM 3026 O  O   . HOH D 4 .   ? -8.830  -4.720  49.590  1.00 40.40 ? 693 HOH A O   1 
HETATM 3027 O  O   . HOH D 4 .   ? -8.477  -16.660 59.138  1.00 27.48 ? 694 HOH A O   1 
HETATM 3028 O  O   . HOH D 4 .   ? -9.191  -9.918  79.787  1.00 38.85 ? 695 HOH A O   1 
HETATM 3029 O  O   . HOH D 4 .   ? 21.499  -12.850 63.640  1.00 35.17 ? 696 HOH A O   1 
HETATM 3030 O  O   . HOH D 4 .   ? 13.084  1.200   65.331  1.00 48.03 ? 697 HOH A O   1 
HETATM 3031 O  O   . HOH D 4 .   ? 8.851   -0.774  65.806  1.00 22.68 ? 698 HOH A O   1 
HETATM 3032 O  O   . HOH D 4 .   ? 0.841   -21.839 51.441  1.00 39.37 ? 699 HOH A O   1 
HETATM 3033 O  O   . HOH D 4 .   ? 8.905   -21.316 47.832  1.00 47.82 ? 700 HOH A O   1 
HETATM 3034 O  O   . HOH D 4 .   ? -13.511 7.611   81.412  1.00 43.21 ? 701 HOH A O   1 
HETATM 3035 O  O   . HOH D 4 .   ? -3.221  -20.926 72.896  1.00 32.13 ? 702 HOH A O   1 
HETATM 3036 O  O   . HOH D 4 .   ? 28.265  -11.449 64.503  1.00 40.55 ? 703 HOH A O   1 
HETATM 3037 O  O   . HOH D 4 .   ? -5.284  -9.636  80.149  1.00 26.64 ? 704 HOH A O   1 
HETATM 3038 O  O   . HOH D 4 .   ? -13.674 -3.432  73.304  1.00 31.51 ? 705 HOH A O   1 
HETATM 3039 O  O   . HOH D 4 .   ? -5.674  3.132   80.755  1.00 28.93 ? 706 HOH A O   1 
HETATM 3040 O  O   . HOH D 4 .   ? -9.026  -24.836 65.810  1.00 43.32 ? 707 HOH A O   1 
HETATM 3041 O  O   . HOH D 4 .   ? -11.193 -16.446 47.375  1.00 24.60 ? 708 HOH A O   1 
HETATM 3042 O  O   . HOH D 4 .   ? -11.493 -10.324 60.902  1.00 14.18 ? 709 HOH A O   1 
HETATM 3043 O  O   . HOH D 4 .   ? 22.643  -28.296 71.229  1.00 45.75 ? 710 HOH A O   1 
HETATM 3044 O  O   . HOH D 4 .   ? 15.582  -20.582 50.975  1.00 49.46 ? 711 HOH A O   1 
HETATM 3045 O  O   . HOH D 4 .   ? 7.970   -16.982 56.188  1.00 32.73 ? 712 HOH A O   1 
HETATM 3046 O  O   . HOH D 4 .   ? -3.603  -25.508 54.330  1.00 47.64 ? 713 HOH A O   1 
HETATM 3047 O  O   . HOH D 4 .   ? -2.186  -22.303 76.838  1.00 31.58 ? 714 HOH A O   1 
HETATM 3048 O  O   . HOH D 4 .   ? 1.903   -16.378 93.003  1.00 52.15 ? 715 HOH A O   1 
HETATM 3049 O  O   . HOH D 4 .   ? -17.375 4.197   71.393  1.00 37.51 ? 716 HOH A O   1 
HETATM 3050 O  O   . HOH D 4 .   ? 7.022   -1.900  85.993  1.00 36.44 ? 717 HOH A O   1 
HETATM 3051 O  O   . HOH D 4 .   ? -5.453  -14.257 68.540  1.00 24.59 ? 718 HOH A O   1 
HETATM 3052 O  O   . HOH D 4 .   ? -2.259  -25.756 47.387  1.00 53.26 ? 719 HOH A O   1 
HETATM 3053 O  O   . HOH D 4 .   ? -12.200 6.429   78.486  1.00 41.05 ? 720 HOH A O   1 
HETATM 3054 O  O   . HOH D 4 .   ? 6.618   -1.337  44.724  1.00 42.67 ? 721 HOH A O   1 
HETATM 3055 O  O   . HOH D 4 .   ? -3.387  -11.725 70.365  1.00 18.85 ? 722 HOH A O   1 
HETATM 3056 O  O   . HOH D 4 .   ? -11.104 -10.892 69.467  1.00 26.10 ? 723 HOH A O   1 
HETATM 3057 O  O   . HOH D 4 .   ? 18.374  11.669  81.577  1.00 51.13 ? 724 HOH A O   1 
HETATM 3058 O  O   . HOH D 4 .   ? 7.293   -2.699  64.245  1.00 25.17 ? 725 HOH A O   1 
HETATM 3059 O  O   . HOH D 4 .   ? 24.857  -8.623  69.963  1.00 46.25 ? 726 HOH A O   1 
HETATM 3060 O  O   . HOH D 4 .   ? -3.691  -15.898 70.311  1.00 23.75 ? 727 HOH A O   1 
HETATM 3061 O  O   . HOH D 4 .   ? 20.754  -6.008  71.088  1.00 35.57 ? 728 HOH A O   1 
HETATM 3062 O  O   . HOH D 4 .   ? 10.561  -24.802 79.509  1.00 48.38 ? 729 HOH A O   1 
HETATM 3063 O  O   . HOH D 4 .   ? 2.305   -22.939 60.007  1.00 53.12 ? 730 HOH A O   1 
HETATM 3064 O  O   . HOH D 4 .   ? 24.212  -13.478 64.170  1.00 54.61 ? 731 HOH A O   1 
HETATM 3065 O  O   . HOH D 4 .   ? 2.664   -22.157 66.408  1.00 34.13 ? 732 HOH A O   1 
HETATM 3066 O  O   . HOH D 4 .   ? -9.349  -26.423 64.130  1.00 59.15 ? 733 HOH A O   1 
HETATM 3067 O  O   . HOH D 4 .   ? -10.371 -2.423  49.661  1.00 37.23 ? 734 HOH A O   1 
HETATM 3068 O  O   . HOH D 4 .   ? 12.757  6.153   71.774  1.00 50.29 ? 735 HOH A O   1 
HETATM 3069 O  O   . HOH D 4 .   ? -6.485  1.814   82.973  1.00 34.38 ? 736 HOH A O   1 
HETATM 3070 O  O   . HOH D 4 .   ? -15.748 10.660  71.516  1.00 58.81 ? 737 HOH A O   1 
HETATM 3071 O  O   . HOH D 4 .   ? -15.312 5.443   74.797  1.00 40.29 ? 738 HOH A O   1 
HETATM 3072 O  O   . HOH D 4 .   ? 1.010   -24.271 48.290  1.00 42.66 ? 739 HOH A O   1 
HETATM 3073 O  O   . HOH D 4 .   ? 4.969   -23.409 86.854  1.00 47.08 ? 740 HOH A O   1 
HETATM 3074 O  O   . HOH D 4 .   ? 3.682   -24.382 58.122  1.00 54.42 ? 741 HOH A O   1 
HETATM 3075 O  O   . HOH D 4 .   ? 2.528   -26.520 59.469  1.00 50.33 ? 742 HOH A O   1 
HETATM 3076 O  O   . HOH D 4 .   ? -11.358 -18.015 59.498  1.00 41.40 ? 743 HOH A O   1 
HETATM 3077 O  O   . HOH D 4 .   ? 5.474   -23.377 74.025  1.00 58.42 ? 744 HOH A O   1 
HETATM 3078 O  O   . HOH D 4 .   ? 8.819   -18.784 47.921  1.00 48.66 ? 745 HOH A O   1 
HETATM 3079 O  O   . HOH D 4 .   ? -14.041 15.837  65.974  1.00 51.21 ? 746 HOH A O   1 
HETATM 3080 O  O   . HOH D 4 .   ? -8.530  -5.965  79.026  1.00 45.61 ? 747 HOH A O   1 
HETATM 3081 O  O   . HOH D 4 .   ? 6.359   -24.399 75.826  1.00 55.58 ? 748 HOH A O   1 
# 
